data_8X4S
# 
_entry.id   8X4S 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.398 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   8X4S         pdb_00008x4s 10.2210/pdb8x4s/pdb 
WWPDB D_1300042619 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2024-11-20 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        8X4S 
_pdbx_database_status.recvd_initial_deposition_date   2023-11-15 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBJ 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           N 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              bxwu15@fudan.edu.cn 
_pdbx_contact_author.name_first         Baixing 
_pdbx_contact_author.name_last          Wu 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-2502-9785 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Meng, C.Y.' 1 ? 
'Wen, Y.'    2 ? 
'Guo, W.T.'  3 ? 
'Wu, B.X.'   4 ? 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            0353 
_citation.journal_id_ISSN           ? 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     'The L-tryptophan specific decarboxylase PsiD covalent bonding with tryptamine' 
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Meng, C.Y.' 1 ? 
primary 'Wen, Y.'    2 ? 
primary 'Guo, W.T.'  3 ? 
primary 'Wu, B.X.'   4 ? 
# 
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 'L-tryptophan decarboxylase'                               45684.344 6   4.1.1.105 ? ? ? 
2 polymer     man 'L-tryptophan decarboxylase'                               3951.634  6   4.1.1.105 ? ? ? 
3 non-polymer syn '(2~{R})-2-[2-(1~{H}-indol-3-yl)ethylamino]propanoic acid' 232.278   6   ?         ? ? ? 
4 water       nat water                                                      18.015    467 ?         ? ? ? 
# 
loop_
_entity_name_com.entity_id 
_entity_name_com.name 
1 'Psilocybin biosynthesis decarboxylase' 
2 'Psilocybin biosynthesis decarboxylase' 
# 
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 
;MQVIPACNSAAIRSLCPTPESFRNMGWLSVSDAVYSEFIGELATRASNRNYSNEFGLMQPIQEFKAFIESDPVVHQEFID
MFEGIQDSPRNYQELCNMFNDIFRKAPVYGDLGPPVYMIMAKLMNTRAGFSAFTRQRLNLHFKKLFDTWGLFLSSKDSRN
VLVADQFDDRHCGWLNERALSAMVKHYNGRAFDEVFLCDKNAPYYGFNSYDDFFNRRFRNRDIDRPVVGGVNNTTLISAA
CESLSYNVSYDVQSLDTLVFKGETYSLKHLLNNDPFTPQFEHGSILQGFLNVTAYHRWHAPVNGTIVKIINVPGTYFAQA
PSTIGDPIPDNDYDPPPYLKSLVYFSNIAARQIMFIEADNKEIGLIFLVFIGMTEISTCEATVSEGQHVNRGDDLGMFHF
GG
;
;MQVIPACNSAAIRSLCPTPESFRNMGWLSVSDAVYSEFIGELATRASNRNYSNEFGLMQPIQEFKAFIESDPVVHQEFID
MFEGIQDSPRNYQELCNMFNDIFRKAPVYGDLGPPVYMIMAKLMNTRAGFSAFTRQRLNLHFKKLFDTWGLFLSSKDSRN
VLVADQFDDRHCGWLNERALSAMVKHYNGRAFDEVFLCDKNAPYYGFNSYDDFFNRRFRNRDIDRPVVGGVNNTTLISAA
CESLSYNVSYDVQSLDTLVFKGETYSLKHLLNNDPFTPQFEHGSILQGFLNVTAYHRWHAPVNGTIVKIINVPGTYFAQA
PSTIGDPIPDNDYDPPPYLKSLVYFSNIAARQIMFIEADNKEIGLIFLVFIGMTEISTCEATVSEGQHVNRGDDLGMFHF
GG
;
I,G,A,C,E,K ? 
2 'polypeptide(L)' no no SFALGLRKDCRAEIVEKFTEPGTVIRINEVVAALKA SFALGLRKDCRAEIVEKFTEPGTVIRINEVVAALKA J,H,B,D,F,L ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
3 '(2~{R})-2-[2-(1~{H}-indol-3-yl)ethylamino]propanoic acid' A1LWG 
4 water                                                      HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   GLN n 
1 3   VAL n 
1 4   ILE n 
1 5   PRO n 
1 6   ALA n 
1 7   CYS n 
1 8   ASN n 
1 9   SER n 
1 10  ALA n 
1 11  ALA n 
1 12  ILE n 
1 13  ARG n 
1 14  SER n 
1 15  LEU n 
1 16  CYS n 
1 17  PRO n 
1 18  THR n 
1 19  PRO n 
1 20  GLU n 
1 21  SER n 
1 22  PHE n 
1 23  ARG n 
1 24  ASN n 
1 25  MET n 
1 26  GLY n 
1 27  TRP n 
1 28  LEU n 
1 29  SER n 
1 30  VAL n 
1 31  SER n 
1 32  ASP n 
1 33  ALA n 
1 34  VAL n 
1 35  TYR n 
1 36  SER n 
1 37  GLU n 
1 38  PHE n 
1 39  ILE n 
1 40  GLY n 
1 41  GLU n 
1 42  LEU n 
1 43  ALA n 
1 44  THR n 
1 45  ARG n 
1 46  ALA n 
1 47  SER n 
1 48  ASN n 
1 49  ARG n 
1 50  ASN n 
1 51  TYR n 
1 52  SER n 
1 53  ASN n 
1 54  GLU n 
1 55  PHE n 
1 56  GLY n 
1 57  LEU n 
1 58  MET n 
1 59  GLN n 
1 60  PRO n 
1 61  ILE n 
1 62  GLN n 
1 63  GLU n 
1 64  PHE n 
1 65  LYS n 
1 66  ALA n 
1 67  PHE n 
1 68  ILE n 
1 69  GLU n 
1 70  SER n 
1 71  ASP n 
1 72  PRO n 
1 73  VAL n 
1 74  VAL n 
1 75  HIS n 
1 76  GLN n 
1 77  GLU n 
1 78  PHE n 
1 79  ILE n 
1 80  ASP n 
1 81  MET n 
1 82  PHE n 
1 83  GLU n 
1 84  GLY n 
1 85  ILE n 
1 86  GLN n 
1 87  ASP n 
1 88  SER n 
1 89  PRO n 
1 90  ARG n 
1 91  ASN n 
1 92  TYR n 
1 93  GLN n 
1 94  GLU n 
1 95  LEU n 
1 96  CYS n 
1 97  ASN n 
1 98  MET n 
1 99  PHE n 
1 100 ASN n 
1 101 ASP n 
1 102 ILE n 
1 103 PHE n 
1 104 ARG n 
1 105 LYS n 
1 106 ALA n 
1 107 PRO n 
1 108 VAL n 
1 109 TYR n 
1 110 GLY n 
1 111 ASP n 
1 112 LEU n 
1 113 GLY n 
1 114 PRO n 
1 115 PRO n 
1 116 VAL n 
1 117 TYR n 
1 118 MET n 
1 119 ILE n 
1 120 MET n 
1 121 ALA n 
1 122 LYS n 
1 123 LEU n 
1 124 MET n 
1 125 ASN n 
1 126 THR n 
1 127 ARG n 
1 128 ALA n 
1 129 GLY n 
1 130 PHE n 
1 131 SER n 
1 132 ALA n 
1 133 PHE n 
1 134 THR n 
1 135 ARG n 
1 136 GLN n 
1 137 ARG n 
1 138 LEU n 
1 139 ASN n 
1 140 LEU n 
1 141 HIS n 
1 142 PHE n 
1 143 LYS n 
1 144 LYS n 
1 145 LEU n 
1 146 PHE n 
1 147 ASP n 
1 148 THR n 
1 149 TRP n 
1 150 GLY n 
1 151 LEU n 
1 152 PHE n 
1 153 LEU n 
1 154 SER n 
1 155 SER n 
1 156 LYS n 
1 157 ASP n 
1 158 SER n 
1 159 ARG n 
1 160 ASN n 
1 161 VAL n 
1 162 LEU n 
1 163 VAL n 
1 164 ALA n 
1 165 ASP n 
1 166 GLN n 
1 167 PHE n 
1 168 ASP n 
1 169 ASP n 
1 170 ARG n 
1 171 HIS n 
1 172 CYS n 
1 173 GLY n 
1 174 TRP n 
1 175 LEU n 
1 176 ASN n 
1 177 GLU n 
1 178 ARG n 
1 179 ALA n 
1 180 LEU n 
1 181 SER n 
1 182 ALA n 
1 183 MET n 
1 184 VAL n 
1 185 LYS n 
1 186 HIS n 
1 187 TYR n 
1 188 ASN n 
1 189 GLY n 
1 190 ARG n 
1 191 ALA n 
1 192 PHE n 
1 193 ASP n 
1 194 GLU n 
1 195 VAL n 
1 196 PHE n 
1 197 LEU n 
1 198 CYS n 
1 199 ASP n 
1 200 LYS n 
1 201 ASN n 
1 202 ALA n 
1 203 PRO n 
1 204 TYR n 
1 205 TYR n 
1 206 GLY n 
1 207 PHE n 
1 208 ASN n 
1 209 SER n 
1 210 TYR n 
1 211 ASP n 
1 212 ASP n 
1 213 PHE n 
1 214 PHE n 
1 215 ASN n 
1 216 ARG n 
1 217 ARG n 
1 218 PHE n 
1 219 ARG n 
1 220 ASN n 
1 221 ARG n 
1 222 ASP n 
1 223 ILE n 
1 224 ASP n 
1 225 ARG n 
1 226 PRO n 
1 227 VAL n 
1 228 VAL n 
1 229 GLY n 
1 230 GLY n 
1 231 VAL n 
1 232 ASN n 
1 233 ASN n 
1 234 THR n 
1 235 THR n 
1 236 LEU n 
1 237 ILE n 
1 238 SER n 
1 239 ALA n 
1 240 ALA n 
1 241 CYS n 
1 242 GLU n 
1 243 SER n 
1 244 LEU n 
1 245 SER n 
1 246 TYR n 
1 247 ASN n 
1 248 VAL n 
1 249 SER n 
1 250 TYR n 
1 251 ASP n 
1 252 VAL n 
1 253 GLN n 
1 254 SER n 
1 255 LEU n 
1 256 ASP n 
1 257 THR n 
1 258 LEU n 
1 259 VAL n 
1 260 PHE n 
1 261 LYS n 
1 262 GLY n 
1 263 GLU n 
1 264 THR n 
1 265 TYR n 
1 266 SER n 
1 267 LEU n 
1 268 LYS n 
1 269 HIS n 
1 270 LEU n 
1 271 LEU n 
1 272 ASN n 
1 273 ASN n 
1 274 ASP n 
1 275 PRO n 
1 276 PHE n 
1 277 THR n 
1 278 PRO n 
1 279 GLN n 
1 280 PHE n 
1 281 GLU n 
1 282 HIS n 
1 283 GLY n 
1 284 SER n 
1 285 ILE n 
1 286 LEU n 
1 287 GLN n 
1 288 GLY n 
1 289 PHE n 
1 290 LEU n 
1 291 ASN n 
1 292 VAL n 
1 293 THR n 
1 294 ALA n 
1 295 TYR n 
1 296 HIS n 
1 297 ARG n 
1 298 TRP n 
1 299 HIS n 
1 300 ALA n 
1 301 PRO n 
1 302 VAL n 
1 303 ASN n 
1 304 GLY n 
1 305 THR n 
1 306 ILE n 
1 307 VAL n 
1 308 LYS n 
1 309 ILE n 
1 310 ILE n 
1 311 ASN n 
1 312 VAL n 
1 313 PRO n 
1 314 GLY n 
1 315 THR n 
1 316 TYR n 
1 317 PHE n 
1 318 ALA n 
1 319 GLN n 
1 320 ALA n 
1 321 PRO n 
1 322 SER n 
1 323 THR n 
1 324 ILE n 
1 325 GLY n 
1 326 ASP n 
1 327 PRO n 
1 328 ILE n 
1 329 PRO n 
1 330 ASP n 
1 331 ASN n 
1 332 ASP n 
1 333 TYR n 
1 334 ASP n 
1 335 PRO n 
1 336 PRO n 
1 337 PRO n 
1 338 TYR n 
1 339 LEU n 
1 340 LYS n 
1 341 SER n 
1 342 LEU n 
1 343 VAL n 
1 344 TYR n 
1 345 PHE n 
1 346 SER n 
1 347 ASN n 
1 348 ILE n 
1 349 ALA n 
1 350 ALA n 
1 351 ARG n 
1 352 GLN n 
1 353 ILE n 
1 354 MET n 
1 355 PHE n 
1 356 ILE n 
1 357 GLU n 
1 358 ALA n 
1 359 ASP n 
1 360 ASN n 
1 361 LYS n 
1 362 GLU n 
1 363 ILE n 
1 364 GLY n 
1 365 LEU n 
1 366 ILE n 
1 367 PHE n 
1 368 LEU n 
1 369 VAL n 
1 370 PHE n 
1 371 ILE n 
1 372 GLY n 
1 373 MET n 
1 374 THR n 
1 375 GLU n 
1 376 ILE n 
1 377 SER n 
1 378 THR n 
1 379 CYS n 
1 380 GLU n 
1 381 ALA n 
1 382 THR n 
1 383 VAL n 
1 384 SER n 
1 385 GLU n 
1 386 GLY n 
1 387 GLN n 
1 388 HIS n 
1 389 VAL n 
1 390 ASN n 
1 391 ARG n 
1 392 GLY n 
1 393 ASP n 
1 394 ASP n 
1 395 LEU n 
1 396 GLY n 
1 397 MET n 
1 398 PHE n 
1 399 HIS n 
1 400 PHE n 
1 401 GLY n 
1 402 GLY n 
2 1   SER n 
2 2   PHE n 
2 3   ALA n 
2 4   LEU n 
2 5   GLY n 
2 6   LEU n 
2 7   ARG n 
2 8   LYS n 
2 9   ASP n 
2 10  CYS n 
2 11  ARG n 
2 12  ALA n 
2 13  GLU n 
2 14  ILE n 
2 15  VAL n 
2 16  GLU n 
2 17  LYS n 
2 18  PHE n 
2 19  THR n 
2 20  GLU n 
2 21  PRO n 
2 22  GLY n 
2 23  THR n 
2 24  VAL n 
2 25  ILE n 
2 26  ARG n 
2 27  ILE n 
2 28  ASN n 
2 29  GLU n 
2 30  VAL n 
2 31  VAL n 
2 32  ALA n 
2 33  ALA n 
2 34  LEU n 
2 35  LYS n 
2 36  ALA 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' 1 402 ? ? psiD ? ? ? ? ? ? 'Psilocybe cubensis' 181762 ? ? ? ? ? ? ? ? 
'Escherichia coli BL21(DE3)' 469008 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
2 1 sample 'Biological sequence' 1 36  ? ? psiD ? ? ? ? ? ? 'Psilocybe cubensis' 181762 ? ? ? ? ? ? ? ? 
'Escherichia coli BL21(DE3)' 469008 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
# 
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 
A1LWG non-polymer         . '(2~{R})-2-[2-(1~{H}-indol-3-yl)ethylamino]propanoic acid' ? 'C13 H16 N2 O2'  232.278 
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 
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  
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 
PHE   'L-peptide linking' y PHENYLALANINE                                              ? 'C9 H11 N O2'    165.189 
PRO   'L-peptide linking' y PROLINE                                                    ? 'C5 H9 N O2'     115.130 
SER   'L-peptide linking' y SERINE                                                     ? 'C3 H7 N O3'     105.093 
THR   'L-peptide linking' y THREONINE                                                  ? 'C4 H9 N O3'     119.119 
TRP   'L-peptide linking' y TRYPTOPHAN                                                 ? 'C11 H12 N2 O2'  204.225 
TYR   'L-peptide linking' y TYROSINE                                                   ? 'C9 H11 N O3'    181.189 
VAL   'L-peptide linking' y VALINE                                                     ? 'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   1   ?   ?   ?   I . n 
A 1 2   GLN 2   2   ?   ?   ?   I . n 
A 1 3   VAL 3   3   ?   ?   ?   I . n 
A 1 4   ILE 4   4   ?   ?   ?   I . n 
A 1 5   PRO 5   5   ?   ?   ?   I . n 
A 1 6   ALA 6   6   ?   ?   ?   I . n 
A 1 7   CYS 7   7   ?   ?   ?   I . n 
A 1 8   ASN 8   8   ?   ?   ?   I . n 
A 1 9   SER 9   9   ?   ?   ?   I . n 
A 1 10  ALA 10  10  ?   ?   ?   I . n 
A 1 11  ALA 11  11  ?   ?   ?   I . n 
A 1 12  ILE 12  12  ?   ?   ?   I . n 
A 1 13  ARG 13  13  ?   ?   ?   I . n 
A 1 14  SER 14  14  ?   ?   ?   I . n 
A 1 15  LEU 15  15  ?   ?   ?   I . n 
A 1 16  CYS 16  16  ?   ?   ?   I . n 
A 1 17  PRO 17  17  ?   ?   ?   I . n 
A 1 18  THR 18  18  ?   ?   ?   I . n 
A 1 19  PRO 19  19  ?   ?   ?   I . n 
A 1 20  GLU 20  20  ?   ?   ?   I . n 
A 1 21  SER 21  21  ?   ?   ?   I . n 
A 1 22  PHE 22  22  ?   ?   ?   I . n 
A 1 23  ARG 23  23  ?   ?   ?   I . n 
A 1 24  ASN 24  24  ?   ?   ?   I . n 
A 1 25  MET 25  25  ?   ?   ?   I . n 
A 1 26  GLY 26  26  ?   ?   ?   I . n 
A 1 27  TRP 27  27  ?   ?   ?   I . n 
A 1 28  LEU 28  28  ?   ?   ?   I . n 
A 1 29  SER 29  29  ?   ?   ?   I . n 
A 1 30  VAL 30  30  ?   ?   ?   I . n 
A 1 31  SER 31  31  ?   ?   ?   I . n 
A 1 32  ASP 32  32  ?   ?   ?   I . n 
A 1 33  ALA 33  33  ?   ?   ?   I . n 
A 1 34  VAL 34  34  ?   ?   ?   I . n 
A 1 35  TYR 35  35  ?   ?   ?   I . n 
A 1 36  SER 36  36  ?   ?   ?   I . n 
A 1 37  GLU 37  37  ?   ?   ?   I . n 
A 1 38  PHE 38  38  ?   ?   ?   I . n 
A 1 39  ILE 39  39  ?   ?   ?   I . n 
A 1 40  GLY 40  40  ?   ?   ?   I . n 
A 1 41  GLU 41  41  ?   ?   ?   I . n 
A 1 42  LEU 42  42  ?   ?   ?   I . n 
A 1 43  ALA 43  43  ?   ?   ?   I . n 
A 1 44  THR 44  44  ?   ?   ?   I . n 
A 1 45  ARG 45  45  ?   ?   ?   I . n 
A 1 46  ALA 46  46  ?   ?   ?   I . n 
A 1 47  SER 47  47  ?   ?   ?   I . n 
A 1 48  ASN 48  48  ?   ?   ?   I . n 
A 1 49  ARG 49  49  ?   ?   ?   I . n 
A 1 50  ASN 50  50  ?   ?   ?   I . n 
A 1 51  TYR 51  51  ?   ?   ?   I . n 
A 1 52  SER 52  52  ?   ?   ?   I . n 
A 1 53  ASN 53  53  ?   ?   ?   I . n 
A 1 54  GLU 54  54  ?   ?   ?   I . n 
A 1 55  PHE 55  55  ?   ?   ?   I . n 
A 1 56  GLY 56  56  ?   ?   ?   I . n 
A 1 57  LEU 57  57  57  LEU LEU I . n 
A 1 58  MET 58  58  58  MET MET I . n 
A 1 59  GLN 59  59  59  GLN GLN I . n 
A 1 60  PRO 60  60  60  PRO PRO I . n 
A 1 61  ILE 61  61  61  ILE ILE I . n 
A 1 62  GLN 62  62  62  GLN GLN I . n 
A 1 63  GLU 63  63  63  GLU GLU I . n 
A 1 64  PHE 64  64  64  PHE PHE I . n 
A 1 65  LYS 65  65  65  LYS LYS I . n 
A 1 66  ALA 66  66  66  ALA ALA I . n 
A 1 67  PHE 67  67  67  PHE PHE I . n 
A 1 68  ILE 68  68  68  ILE ILE I . n 
A 1 69  GLU 69  69  69  GLU GLU I . n 
A 1 70  SER 70  70  70  SER SER I . n 
A 1 71  ASP 71  71  71  ASP ASP I . n 
A 1 72  PRO 72  72  72  PRO PRO I . n 
A 1 73  VAL 73  73  73  VAL VAL I . n 
A 1 74  VAL 74  74  74  VAL VAL I . n 
A 1 75  HIS 75  75  75  HIS HIS I . n 
A 1 76  GLN 76  76  76  GLN GLN I . n 
A 1 77  GLU 77  77  77  GLU GLU I . n 
A 1 78  PHE 78  78  78  PHE PHE I . n 
A 1 79  ILE 79  79  79  ILE ILE I . n 
A 1 80  ASP 80  80  80  ASP ASP I . n 
A 1 81  MET 81  81  81  MET MET I . n 
A 1 82  PHE 82  82  82  PHE PHE I . n 
A 1 83  GLU 83  83  83  GLU GLU I . n 
A 1 84  GLY 84  84  84  GLY GLY I . n 
A 1 85  ILE 85  85  85  ILE ILE I . n 
A 1 86  GLN 86  86  86  GLN GLN I . n 
A 1 87  ASP 87  87  87  ASP ASP I . n 
A 1 88  SER 88  88  88  SER SER I . n 
A 1 89  PRO 89  89  89  PRO PRO I . n 
A 1 90  ARG 90  90  90  ARG ARG I . n 
A 1 91  ASN 91  91  91  ASN ASN I . n 
A 1 92  TYR 92  92  92  TYR TYR I . n 
A 1 93  GLN 93  93  93  GLN GLN I . n 
A 1 94  GLU 94  94  94  GLU GLU I . n 
A 1 95  LEU 95  95  95  LEU LEU I . n 
A 1 96  CYS 96  96  96  CYS CYS I . n 
A 1 97  ASN 97  97  97  ASN ASN I . n 
A 1 98  MET 98  98  98  MET MET I . n 
A 1 99  PHE 99  99  99  PHE PHE I . n 
A 1 100 ASN 100 100 100 ASN ASN I . n 
A 1 101 ASP 101 101 101 ASP ASP I . n 
A 1 102 ILE 102 102 102 ILE ILE I . n 
A 1 103 PHE 103 103 103 PHE PHE I . n 
A 1 104 ARG 104 104 104 ARG ARG I . n 
A 1 105 LYS 105 105 105 LYS LYS I . n 
A 1 106 ALA 106 106 106 ALA ALA I . n 
A 1 107 PRO 107 107 107 PRO PRO I . n 
A 1 108 VAL 108 108 108 VAL VAL I . n 
A 1 109 TYR 109 109 109 TYR TYR I . n 
A 1 110 GLY 110 110 110 GLY GLY I . n 
A 1 111 ASP 111 111 111 ASP ASP I . n 
A 1 112 LEU 112 112 112 LEU LEU I . n 
A 1 113 GLY 113 113 113 GLY GLY I . n 
A 1 114 PRO 114 114 114 PRO PRO I . n 
A 1 115 PRO 115 115 115 PRO PRO I . n 
A 1 116 VAL 116 116 116 VAL VAL I . n 
A 1 117 TYR 117 117 117 TYR TYR I . n 
A 1 118 MET 118 118 118 MET MET I . n 
A 1 119 ILE 119 119 119 ILE ILE I . n 
A 1 120 MET 120 120 120 MET MET I . n 
A 1 121 ALA 121 121 121 ALA ALA I . n 
A 1 122 LYS 122 122 122 LYS LYS I . n 
A 1 123 LEU 123 123 123 LEU LEU I . n 
A 1 124 MET 124 124 124 MET MET I . n 
A 1 125 ASN 125 125 125 ASN ASN I . n 
A 1 126 THR 126 126 126 THR THR I . n 
A 1 127 ARG 127 127 127 ARG ARG I . n 
A 1 128 ALA 128 128 128 ALA ALA I . n 
A 1 129 GLY 129 129 129 GLY GLY I . n 
A 1 130 PHE 130 130 130 PHE PHE I . n 
A 1 131 SER 131 131 131 SER SER I . n 
A 1 132 ALA 132 132 132 ALA ALA I . n 
A 1 133 PHE 133 133 133 PHE PHE I . n 
A 1 134 THR 134 134 134 THR THR I . n 
A 1 135 ARG 135 135 135 ARG ARG I . n 
A 1 136 GLN 136 136 136 GLN GLN I . n 
A 1 137 ARG 137 137 137 ARG ARG I . n 
A 1 138 LEU 138 138 138 LEU LEU I . n 
A 1 139 ASN 139 139 139 ASN ASN I . n 
A 1 140 LEU 140 140 140 LEU LEU I . n 
A 1 141 HIS 141 141 141 HIS HIS I . n 
A 1 142 PHE 142 142 142 PHE PHE I . n 
A 1 143 LYS 143 143 143 LYS LYS I . n 
A 1 144 LYS 144 144 144 LYS LYS I . n 
A 1 145 LEU 145 145 145 LEU LEU I . n 
A 1 146 PHE 146 146 146 PHE PHE I . n 
A 1 147 ASP 147 147 147 ASP ASP I . n 
A 1 148 THR 148 148 148 THR THR I . n 
A 1 149 TRP 149 149 149 TRP TRP I . n 
A 1 150 GLY 150 150 150 GLY GLY I . n 
A 1 151 LEU 151 151 151 LEU LEU I . n 
A 1 152 PHE 152 152 152 PHE PHE I . n 
A 1 153 LEU 153 153 153 LEU LEU I . n 
A 1 154 SER 154 154 154 SER SER I . n 
A 1 155 SER 155 155 155 SER SER I . n 
A 1 156 LYS 156 156 156 LYS LYS I . n 
A 1 157 ASP 157 157 157 ASP ASP I . n 
A 1 158 SER 158 158 158 SER SER I . n 
A 1 159 ARG 159 159 159 ARG ARG I . n 
A 1 160 ASN 160 160 160 ASN ASN I . n 
A 1 161 VAL 161 161 161 VAL VAL I . n 
A 1 162 LEU 162 162 162 LEU LEU I . n 
A 1 163 VAL 163 163 163 VAL VAL I . n 
A 1 164 ALA 164 164 164 ALA ALA I . n 
A 1 165 ASP 165 165 165 ASP ASP I . n 
A 1 166 GLN 166 166 166 GLN GLN I . n 
A 1 167 PHE 167 167 167 PHE PHE I . n 
A 1 168 ASP 168 168 168 ASP ASP I . n 
A 1 169 ASP 169 169 169 ASP ASP I . n 
A 1 170 ARG 170 170 170 ARG ARG I . n 
A 1 171 HIS 171 171 171 HIS HIS I . n 
A 1 172 CYS 172 172 172 CYS CYS I . n 
A 1 173 GLY 173 173 173 GLY GLY I . n 
A 1 174 TRP 174 174 174 TRP TRP I . n 
A 1 175 LEU 175 175 175 LEU LEU I . n 
A 1 176 ASN 176 176 176 ASN ASN I . n 
A 1 177 GLU 177 177 177 GLU GLU I . n 
A 1 178 ARG 178 178 178 ARG ARG I . n 
A 1 179 ALA 179 179 179 ALA ALA I . n 
A 1 180 LEU 180 180 180 LEU LEU I . n 
A 1 181 SER 181 181 181 SER SER I . n 
A 1 182 ALA 182 182 182 ALA ALA I . n 
A 1 183 MET 183 183 183 MET MET I . n 
A 1 184 VAL 184 184 184 VAL VAL I . n 
A 1 185 LYS 185 185 185 LYS LYS I . n 
A 1 186 HIS 186 186 186 HIS HIS I . n 
A 1 187 TYR 187 187 187 TYR TYR I . n 
A 1 188 ASN 188 188 188 ASN ASN I . n 
A 1 189 GLY 189 189 189 GLY GLY I . n 
A 1 190 ARG 190 190 190 ARG ARG I . n 
A 1 191 ALA 191 191 191 ALA ALA I . n 
A 1 192 PHE 192 192 192 PHE PHE I . n 
A 1 193 ASP 193 193 193 ASP ASP I . n 
A 1 194 GLU 194 194 194 GLU GLU I . n 
A 1 195 VAL 195 195 195 VAL VAL I . n 
A 1 196 PHE 196 196 196 PHE PHE I . n 
A 1 197 LEU 197 197 197 LEU LEU I . n 
A 1 198 CYS 198 198 198 CYS CYS I . n 
A 1 199 ASP 199 199 199 ASP ASP I . n 
A 1 200 LYS 200 200 200 LYS LYS I . n 
A 1 201 ASN 201 201 201 ASN ASN I . n 
A 1 202 ALA 202 202 202 ALA ALA I . n 
A 1 203 PRO 203 203 203 PRO PRO I . n 
A 1 204 TYR 204 204 204 TYR TYR I . n 
A 1 205 TYR 205 205 205 TYR TYR I . n 
A 1 206 GLY 206 206 206 GLY GLY I . n 
A 1 207 PHE 207 207 207 PHE PHE I . n 
A 1 208 ASN 208 208 208 ASN ASN I . n 
A 1 209 SER 209 209 209 SER SER I . n 
A 1 210 TYR 210 210 210 TYR TYR I . n 
A 1 211 ASP 211 211 211 ASP ASP I . n 
A 1 212 ASP 212 212 212 ASP ASP I . n 
A 1 213 PHE 213 213 213 PHE PHE I . n 
A 1 214 PHE 214 214 214 PHE PHE I . n 
A 1 215 ASN 215 215 215 ASN ASN I . n 
A 1 216 ARG 216 216 216 ARG ARG I . n 
A 1 217 ARG 217 217 217 ARG ARG I . n 
A 1 218 PHE 218 218 218 PHE PHE I . n 
A 1 219 ARG 219 219 219 ARG ARG I . n 
A 1 220 ASN 220 220 220 ASN ASN I . n 
A 1 221 ARG 221 221 221 ARG ARG I . n 
A 1 222 ASP 222 222 222 ASP ASP I . n 
A 1 223 ILE 223 223 223 ILE ILE I . n 
A 1 224 ASP 224 224 224 ASP ASP I . n 
A 1 225 ARG 225 225 225 ARG ARG I . n 
A 1 226 PRO 226 226 226 PRO PRO I . n 
A 1 227 VAL 227 227 227 VAL VAL I . n 
A 1 228 VAL 228 228 228 VAL VAL I . n 
A 1 229 GLY 229 229 229 GLY GLY I . n 
A 1 230 GLY 230 230 230 GLY GLY I . n 
A 1 231 VAL 231 231 231 VAL VAL I . n 
A 1 232 ASN 232 232 232 ASN ASN I . n 
A 1 233 ASN 233 233 233 ASN ASN I . n 
A 1 234 THR 234 234 234 THR THR I . n 
A 1 235 THR 235 235 235 THR THR I . n 
A 1 236 LEU 236 236 236 LEU LEU I . n 
A 1 237 ILE 237 237 237 ILE ILE I . n 
A 1 238 SER 238 238 238 SER SER I . n 
A 1 239 ALA 239 239 239 ALA ALA I . n 
A 1 240 ALA 240 240 240 ALA ALA I . n 
A 1 241 CYS 241 241 241 CYS CYS I . n 
A 1 242 GLU 242 242 242 GLU GLU I . n 
A 1 243 SER 243 243 243 SER SER I . n 
A 1 244 LEU 244 244 244 LEU LEU I . n 
A 1 245 SER 245 245 245 SER SER I . n 
A 1 246 TYR 246 246 246 TYR TYR I . n 
A 1 247 ASN 247 247 247 ASN ASN I . n 
A 1 248 VAL 248 248 248 VAL VAL I . n 
A 1 249 SER 249 249 249 SER SER I . n 
A 1 250 TYR 250 250 250 TYR TYR I . n 
A 1 251 ASP 251 251 251 ASP ASP I . n 
A 1 252 VAL 252 252 252 VAL VAL I . n 
A 1 253 GLN 253 253 253 GLN GLN I . n 
A 1 254 SER 254 254 254 SER SER I . n 
A 1 255 LEU 255 255 255 LEU LEU I . n 
A 1 256 ASP 256 256 256 ASP ASP I . n 
A 1 257 THR 257 257 257 THR THR I . n 
A 1 258 LEU 258 258 258 LEU LEU I . n 
A 1 259 VAL 259 259 259 VAL VAL I . n 
A 1 260 PHE 260 260 260 PHE PHE I . n 
A 1 261 LYS 261 261 261 LYS LYS I . n 
A 1 262 GLY 262 262 262 GLY GLY I . n 
A 1 263 GLU 263 263 263 GLU GLU I . n 
A 1 264 THR 264 264 264 THR THR I . n 
A 1 265 TYR 265 265 265 TYR TYR I . n 
A 1 266 SER 266 266 266 SER SER I . n 
A 1 267 LEU 267 267 267 LEU LEU I . n 
A 1 268 LYS 268 268 268 LYS LYS I . n 
A 1 269 HIS 269 269 269 HIS HIS I . n 
A 1 270 LEU 270 270 270 LEU LEU I . n 
A 1 271 LEU 271 271 271 LEU LEU I . n 
A 1 272 ASN 272 272 272 ASN ASN I . n 
A 1 273 ASN 273 273 273 ASN ASN I . n 
A 1 274 ASP 274 274 274 ASP ASP I . n 
A 1 275 PRO 275 275 275 PRO PRO I . n 
A 1 276 PHE 276 276 276 PHE PHE I . n 
A 1 277 THR 277 277 277 THR THR I . n 
A 1 278 PRO 278 278 278 PRO PRO I . n 
A 1 279 GLN 279 279 279 GLN GLN I . n 
A 1 280 PHE 280 280 280 PHE PHE I . n 
A 1 281 GLU 281 281 281 GLU GLU I . n 
A 1 282 HIS 282 282 282 HIS HIS I . n 
A 1 283 GLY 283 283 283 GLY GLY I . n 
A 1 284 SER 284 284 284 SER SER I . n 
A 1 285 ILE 285 285 285 ILE ILE I . n 
A 1 286 LEU 286 286 286 LEU LEU I . n 
A 1 287 GLN 287 287 287 GLN GLN I . n 
A 1 288 GLY 288 288 288 GLY GLY I . n 
A 1 289 PHE 289 289 289 PHE PHE I . n 
A 1 290 LEU 290 290 290 LEU LEU I . n 
A 1 291 ASN 291 291 291 ASN ASN I . n 
A 1 292 VAL 292 292 292 VAL VAL I . n 
A 1 293 THR 293 293 293 THR THR I . n 
A 1 294 ALA 294 294 294 ALA ALA I . n 
A 1 295 TYR 295 295 295 TYR TYR I . n 
A 1 296 HIS 296 296 296 HIS HIS I . n 
A 1 297 ARG 297 297 297 ARG ARG I . n 
A 1 298 TRP 298 298 298 TRP TRP I . n 
A 1 299 HIS 299 299 299 HIS HIS I . n 
A 1 300 ALA 300 300 300 ALA ALA I . n 
A 1 301 PRO 301 301 301 PRO PRO I . n 
A 1 302 VAL 302 302 302 VAL VAL I . n 
A 1 303 ASN 303 303 303 ASN ASN I . n 
A 1 304 GLY 304 304 304 GLY GLY I . n 
A 1 305 THR 305 305 305 THR THR I . n 
A 1 306 ILE 306 306 306 ILE ILE I . n 
A 1 307 VAL 307 307 307 VAL VAL I . n 
A 1 308 LYS 308 308 308 LYS LYS I . n 
A 1 309 ILE 309 309 309 ILE ILE I . n 
A 1 310 ILE 310 310 310 ILE ILE I . n 
A 1 311 ASN 311 311 311 ASN ASN I . n 
A 1 312 VAL 312 312 312 VAL VAL I . n 
A 1 313 PRO 313 313 313 PRO PRO I . n 
A 1 314 GLY 314 314 314 GLY GLY I . n 
A 1 315 THR 315 315 315 THR THR I . n 
A 1 316 TYR 316 316 316 TYR TYR I . n 
A 1 317 PHE 317 317 317 PHE PHE I . n 
A 1 318 ALA 318 318 318 ALA ALA I . n 
A 1 319 GLN 319 319 319 GLN GLN I . n 
A 1 320 ALA 320 320 320 ALA ALA I . n 
A 1 321 PRO 321 321 321 PRO PRO I . n 
A 1 322 SER 322 322 322 SER SER I . n 
A 1 323 THR 323 323 323 THR THR I . n 
A 1 324 ILE 324 324 324 ILE ILE I . n 
A 1 325 GLY 325 325 325 GLY GLY I . n 
A 1 326 ASP 326 326 326 ASP ASP I . n 
A 1 327 PRO 327 327 327 PRO PRO I . n 
A 1 328 ILE 328 328 328 ILE ILE I . n 
A 1 329 PRO 329 329 329 PRO PRO I . n 
A 1 330 ASP 330 330 330 ASP ASP I . n 
A 1 331 ASN 331 331 331 ASN ASN I . n 
A 1 332 ASP 332 332 332 ASP ASP I . n 
A 1 333 TYR 333 333 333 TYR TYR I . n 
A 1 334 ASP 334 334 334 ASP ASP I . n 
A 1 335 PRO 335 335 335 PRO PRO I . n 
A 1 336 PRO 336 336 336 PRO PRO I . n 
A 1 337 PRO 337 337 337 PRO PRO I . n 
A 1 338 TYR 338 338 338 TYR TYR I . n 
A 1 339 LEU 339 339 339 LEU LEU I . n 
A 1 340 LYS 340 340 340 LYS LYS I . n 
A 1 341 SER 341 341 341 SER SER I . n 
A 1 342 LEU 342 342 342 LEU LEU I . n 
A 1 343 VAL 343 343 343 VAL VAL I . n 
A 1 344 TYR 344 344 344 TYR TYR I . n 
A 1 345 PHE 345 345 345 PHE PHE I . n 
A 1 346 SER 346 346 346 SER SER I . n 
A 1 347 ASN 347 347 347 ASN ASN I . n 
A 1 348 ILE 348 348 348 ILE ILE I . n 
A 1 349 ALA 349 349 349 ALA ALA I . n 
A 1 350 ALA 350 350 350 ALA ALA I . n 
A 1 351 ARG 351 351 351 ARG ARG I . n 
A 1 352 GLN 352 352 352 GLN GLN I . n 
A 1 353 ILE 353 353 353 ILE ILE I . n 
A 1 354 MET 354 354 354 MET MET I . n 
A 1 355 PHE 355 355 355 PHE PHE I . n 
A 1 356 ILE 356 356 356 ILE ILE I . n 
A 1 357 GLU 357 357 357 GLU GLU I . n 
A 1 358 ALA 358 358 358 ALA ALA I . n 
A 1 359 ASP 359 359 359 ASP ASP I . n 
A 1 360 ASN 360 360 360 ASN ASN I . n 
A 1 361 LYS 361 361 361 LYS LYS I . n 
A 1 362 GLU 362 362 362 GLU GLU I . n 
A 1 363 ILE 363 363 363 ILE ILE I . n 
A 1 364 GLY 364 364 364 GLY GLY I . n 
A 1 365 LEU 365 365 365 LEU LEU I . n 
A 1 366 ILE 366 366 366 ILE ILE I . n 
A 1 367 PHE 367 367 367 PHE PHE I . n 
A 1 368 LEU 368 368 368 LEU LEU I . n 
A 1 369 VAL 369 369 369 VAL VAL I . n 
A 1 370 PHE 370 370 370 PHE PHE I . n 
A 1 371 ILE 371 371 371 ILE ILE I . n 
A 1 372 GLY 372 372 372 GLY GLY I . n 
A 1 373 MET 373 373 373 MET MET I . n 
A 1 374 THR 374 374 374 THR THR I . n 
A 1 375 GLU 375 375 375 GLU GLU I . n 
A 1 376 ILE 376 376 376 ILE ILE I . n 
A 1 377 SER 377 377 377 SER SER I . n 
A 1 378 THR 378 378 378 THR THR I . n 
A 1 379 CYS 379 379 379 CYS CYS I . n 
A 1 380 GLU 380 380 380 GLU GLU I . n 
A 1 381 ALA 381 381 381 ALA ALA I . n 
A 1 382 THR 382 382 382 THR THR I . n 
A 1 383 VAL 383 383 383 VAL VAL I . n 
A 1 384 SER 384 384 384 SER SER I . n 
A 1 385 GLU 385 385 385 GLU GLU I . n 
A 1 386 GLY 386 386 386 GLY GLY I . n 
A 1 387 GLN 387 387 387 GLN GLN I . n 
A 1 388 HIS 388 388 388 HIS HIS I . n 
A 1 389 VAL 389 389 389 VAL VAL I . n 
A 1 390 ASN 390 390 390 ASN ASN I . n 
A 1 391 ARG 391 391 391 ARG ARG I . n 
A 1 392 GLY 392 392 392 GLY GLY I . n 
A 1 393 ASP 393 393 393 ASP ASP I . n 
A 1 394 ASP 394 394 394 ASP ASP I . n 
A 1 395 LEU 395 395 395 LEU LEU I . n 
A 1 396 GLY 396 396 396 GLY GLY I . n 
A 1 397 MET 397 397 397 MET MET I . n 
A 1 398 PHE 398 398 398 PHE PHE I . n 
A 1 399 HIS 399 399 399 HIS HIS I . n 
A 1 400 PHE 400 400 400 PHE PHE I . n 
A 1 401 GLY 401 401 401 GLY GLY I . n 
A 1 402 GLY 402 402 402 GLY GLY I . n 
B 2 1   SER 1   404 404 SER SER J . n 
B 2 2   PHE 2   405 405 PHE PHE J . n 
B 2 3   ALA 3   406 406 ALA ALA J . n 
B 2 4   LEU 4   407 407 LEU LEU J . n 
B 2 5   GLY 5   408 408 GLY GLY J . n 
B 2 6   LEU 6   409 409 LEU LEU J . n 
B 2 7   ARG 7   410 410 ARG ARG J . n 
B 2 8   LYS 8   411 411 LYS LYS J . n 
B 2 9   ASP 9   412 412 ASP ASP J . n 
B 2 10  CYS 10  413 413 CYS CYS J . n 
B 2 11  ARG 11  414 414 ARG ARG J . n 
B 2 12  ALA 12  415 415 ALA ALA J . n 
B 2 13  GLU 13  416 416 GLU GLU J . n 
B 2 14  ILE 14  417 417 ILE ILE J . n 
B 2 15  VAL 15  418 418 VAL VAL J . n 
B 2 16  GLU 16  419 419 GLU GLU J . n 
B 2 17  LYS 17  420 420 LYS LYS J . n 
B 2 18  PHE 18  421 421 PHE PHE J . n 
B 2 19  THR 19  422 422 THR THR J . n 
B 2 20  GLU 20  423 423 GLU GLU J . n 
B 2 21  PRO 21  424 424 PRO PRO J . n 
B 2 22  GLY 22  425 425 GLY GLY J . n 
B 2 23  THR 23  426 426 THR THR J . n 
B 2 24  VAL 24  427 427 VAL VAL J . n 
B 2 25  ILE 25  428 428 ILE ILE J . n 
B 2 26  ARG 26  429 429 ARG ARG J . n 
B 2 27  ILE 27  430 430 ILE ILE J . n 
B 2 28  ASN 28  431 431 ASN ASN J . n 
B 2 29  GLU 29  432 432 GLU GLU J . n 
B 2 30  VAL 30  433 433 VAL VAL J . n 
B 2 31  VAL 31  434 434 VAL VAL J . n 
B 2 32  ALA 32  435 435 ALA ALA J . n 
B 2 33  ALA 33  436 436 ALA ALA J . n 
B 2 34  LEU 34  437 437 LEU LEU J . n 
B 2 35  LYS 35  438 ?   ?   ?   J . n 
B 2 36  ALA 36  439 ?   ?   ?   J . n 
C 1 1   MET 1   1   ?   ?   ?   G . n 
C 1 2   GLN 2   2   ?   ?   ?   G . n 
C 1 3   VAL 3   3   ?   ?   ?   G . n 
C 1 4   ILE 4   4   ?   ?   ?   G . n 
C 1 5   PRO 5   5   ?   ?   ?   G . n 
C 1 6   ALA 6   6   ?   ?   ?   G . n 
C 1 7   CYS 7   7   ?   ?   ?   G . n 
C 1 8   ASN 8   8   ?   ?   ?   G . n 
C 1 9   SER 9   9   ?   ?   ?   G . n 
C 1 10  ALA 10  10  ?   ?   ?   G . n 
C 1 11  ALA 11  11  ?   ?   ?   G . n 
C 1 12  ILE 12  12  ?   ?   ?   G . n 
C 1 13  ARG 13  13  ?   ?   ?   G . n 
C 1 14  SER 14  14  ?   ?   ?   G . n 
C 1 15  LEU 15  15  ?   ?   ?   G . n 
C 1 16  CYS 16  16  ?   ?   ?   G . n 
C 1 17  PRO 17  17  ?   ?   ?   G . n 
C 1 18  THR 18  18  ?   ?   ?   G . n 
C 1 19  PRO 19  19  ?   ?   ?   G . n 
C 1 20  GLU 20  20  ?   ?   ?   G . n 
C 1 21  SER 21  21  ?   ?   ?   G . n 
C 1 22  PHE 22  22  ?   ?   ?   G . n 
C 1 23  ARG 23  23  ?   ?   ?   G . n 
C 1 24  ASN 24  24  ?   ?   ?   G . n 
C 1 25  MET 25  25  ?   ?   ?   G . n 
C 1 26  GLY 26  26  ?   ?   ?   G . n 
C 1 27  TRP 27  27  ?   ?   ?   G . n 
C 1 28  LEU 28  28  ?   ?   ?   G . n 
C 1 29  SER 29  29  ?   ?   ?   G . n 
C 1 30  VAL 30  30  ?   ?   ?   G . n 
C 1 31  SER 31  31  ?   ?   ?   G . n 
C 1 32  ASP 32  32  ?   ?   ?   G . n 
C 1 33  ALA 33  33  ?   ?   ?   G . n 
C 1 34  VAL 34  34  ?   ?   ?   G . n 
C 1 35  TYR 35  35  ?   ?   ?   G . n 
C 1 36  SER 36  36  ?   ?   ?   G . n 
C 1 37  GLU 37  37  ?   ?   ?   G . n 
C 1 38  PHE 38  38  ?   ?   ?   G . n 
C 1 39  ILE 39  39  ?   ?   ?   G . n 
C 1 40  GLY 40  40  ?   ?   ?   G . n 
C 1 41  GLU 41  41  ?   ?   ?   G . n 
C 1 42  LEU 42  42  ?   ?   ?   G . n 
C 1 43  ALA 43  43  ?   ?   ?   G . n 
C 1 44  THR 44  44  ?   ?   ?   G . n 
C 1 45  ARG 45  45  ?   ?   ?   G . n 
C 1 46  ALA 46  46  ?   ?   ?   G . n 
C 1 47  SER 47  47  ?   ?   ?   G . n 
C 1 48  ASN 48  48  ?   ?   ?   G . n 
C 1 49  ARG 49  49  ?   ?   ?   G . n 
C 1 50  ASN 50  50  ?   ?   ?   G . n 
C 1 51  TYR 51  51  ?   ?   ?   G . n 
C 1 52  SER 52  52  ?   ?   ?   G . n 
C 1 53  ASN 53  53  ?   ?   ?   G . n 
C 1 54  GLU 54  54  ?   ?   ?   G . n 
C 1 55  PHE 55  55  ?   ?   ?   G . n 
C 1 56  GLY 56  56  ?   ?   ?   G . n 
C 1 57  LEU 57  57  57  LEU LEU G . n 
C 1 58  MET 58  58  58  MET MET G . n 
C 1 59  GLN 59  59  59  GLN GLN G . n 
C 1 60  PRO 60  60  60  PRO PRO G . n 
C 1 61  ILE 61  61  61  ILE ILE G . n 
C 1 62  GLN 62  62  62  GLN GLN G . n 
C 1 63  GLU 63  63  63  GLU GLU G . n 
C 1 64  PHE 64  64  64  PHE PHE G . n 
C 1 65  LYS 65  65  65  LYS LYS G . n 
C 1 66  ALA 66  66  66  ALA ALA G . n 
C 1 67  PHE 67  67  67  PHE PHE G . n 
C 1 68  ILE 68  68  68  ILE ILE G . n 
C 1 69  GLU 69  69  69  GLU GLU G . n 
C 1 70  SER 70  70  70  SER SER G . n 
C 1 71  ASP 71  71  71  ASP ASP G . n 
C 1 72  PRO 72  72  72  PRO PRO G . n 
C 1 73  VAL 73  73  73  VAL VAL G . n 
C 1 74  VAL 74  74  74  VAL VAL G . n 
C 1 75  HIS 75  75  75  HIS HIS G . n 
C 1 76  GLN 76  76  76  GLN GLN G . n 
C 1 77  GLU 77  77  77  GLU GLU G . n 
C 1 78  PHE 78  78  78  PHE PHE G . n 
C 1 79  ILE 79  79  79  ILE ILE G . n 
C 1 80  ASP 80  80  80  ASP ASP G . n 
C 1 81  MET 81  81  81  MET MET G . n 
C 1 82  PHE 82  82  82  PHE PHE G . n 
C 1 83  GLU 83  83  83  GLU GLU G . n 
C 1 84  GLY 84  84  84  GLY GLY G . n 
C 1 85  ILE 85  85  85  ILE ILE G . n 
C 1 86  GLN 86  86  86  GLN GLN G . n 
C 1 87  ASP 87  87  87  ASP ASP G . n 
C 1 88  SER 88  88  88  SER SER G . n 
C 1 89  PRO 89  89  89  PRO PRO G . n 
C 1 90  ARG 90  90  90  ARG ARG G . n 
C 1 91  ASN 91  91  91  ASN ASN G . n 
C 1 92  TYR 92  92  92  TYR TYR G . n 
C 1 93  GLN 93  93  93  GLN GLN G . n 
C 1 94  GLU 94  94  94  GLU GLU G . n 
C 1 95  LEU 95  95  95  LEU LEU G . n 
C 1 96  CYS 96  96  96  CYS CYS G . n 
C 1 97  ASN 97  97  97  ASN ASN G . n 
C 1 98  MET 98  98  98  MET MET G . n 
C 1 99  PHE 99  99  99  PHE PHE G . n 
C 1 100 ASN 100 100 100 ASN ASN G . n 
C 1 101 ASP 101 101 101 ASP ASP G . n 
C 1 102 ILE 102 102 102 ILE ILE G . n 
C 1 103 PHE 103 103 103 PHE PHE G . n 
C 1 104 ARG 104 104 104 ARG ARG G . n 
C 1 105 LYS 105 105 105 LYS LYS G . n 
C 1 106 ALA 106 106 106 ALA ALA G . n 
C 1 107 PRO 107 107 107 PRO PRO G . n 
C 1 108 VAL 108 108 108 VAL VAL G . n 
C 1 109 TYR 109 109 109 TYR TYR G . n 
C 1 110 GLY 110 110 110 GLY GLY G . n 
C 1 111 ASP 111 111 111 ASP ASP G . n 
C 1 112 LEU 112 112 112 LEU LEU G . n 
C 1 113 GLY 113 113 113 GLY GLY G . n 
C 1 114 PRO 114 114 114 PRO PRO G . n 
C 1 115 PRO 115 115 115 PRO PRO G . n 
C 1 116 VAL 116 116 116 VAL VAL G . n 
C 1 117 TYR 117 117 117 TYR TYR G . n 
C 1 118 MET 118 118 118 MET MET G . n 
C 1 119 ILE 119 119 119 ILE ILE G . n 
C 1 120 MET 120 120 120 MET MET G . n 
C 1 121 ALA 121 121 121 ALA ALA G . n 
C 1 122 LYS 122 122 122 LYS LYS G . n 
C 1 123 LEU 123 123 123 LEU LEU G . n 
C 1 124 MET 124 124 124 MET MET G . n 
C 1 125 ASN 125 125 125 ASN ASN G . n 
C 1 126 THR 126 126 126 THR THR G . n 
C 1 127 ARG 127 127 127 ARG ARG G . n 
C 1 128 ALA 128 128 128 ALA ALA G . n 
C 1 129 GLY 129 129 129 GLY GLY G . n 
C 1 130 PHE 130 130 130 PHE PHE G . n 
C 1 131 SER 131 131 131 SER SER G . n 
C 1 132 ALA 132 132 132 ALA ALA G . n 
C 1 133 PHE 133 133 133 PHE PHE G . n 
C 1 134 THR 134 134 134 THR THR G . n 
C 1 135 ARG 135 135 135 ARG ARG G . n 
C 1 136 GLN 136 136 136 GLN GLN G . n 
C 1 137 ARG 137 137 137 ARG ARG G . n 
C 1 138 LEU 138 138 138 LEU LEU G . n 
C 1 139 ASN 139 139 139 ASN ASN G . n 
C 1 140 LEU 140 140 140 LEU LEU G . n 
C 1 141 HIS 141 141 141 HIS HIS G . n 
C 1 142 PHE 142 142 142 PHE PHE G . n 
C 1 143 LYS 143 143 143 LYS LYS G . n 
C 1 144 LYS 144 144 144 LYS LYS G . n 
C 1 145 LEU 145 145 145 LEU LEU G . n 
C 1 146 PHE 146 146 146 PHE PHE G . n 
C 1 147 ASP 147 147 147 ASP ASP G . n 
C 1 148 THR 148 148 148 THR THR G . n 
C 1 149 TRP 149 149 149 TRP TRP G . n 
C 1 150 GLY 150 150 150 GLY GLY G . n 
C 1 151 LEU 151 151 151 LEU LEU G . n 
C 1 152 PHE 152 152 152 PHE PHE G . n 
C 1 153 LEU 153 153 153 LEU LEU G . n 
C 1 154 SER 154 154 154 SER SER G . n 
C 1 155 SER 155 155 155 SER SER G . n 
C 1 156 LYS 156 156 156 LYS LYS G . n 
C 1 157 ASP 157 157 157 ASP ASP G . n 
C 1 158 SER 158 158 158 SER SER G . n 
C 1 159 ARG 159 159 159 ARG ARG G . n 
C 1 160 ASN 160 160 160 ASN ASN G . n 
C 1 161 VAL 161 161 161 VAL VAL G . n 
C 1 162 LEU 162 162 162 LEU LEU G . n 
C 1 163 VAL 163 163 163 VAL VAL G . n 
C 1 164 ALA 164 164 164 ALA ALA G . n 
C 1 165 ASP 165 165 165 ASP ASP G . n 
C 1 166 GLN 166 166 166 GLN GLN G . n 
C 1 167 PHE 167 167 167 PHE PHE G . n 
C 1 168 ASP 168 168 168 ASP ASP G . n 
C 1 169 ASP 169 169 169 ASP ASP G . n 
C 1 170 ARG 170 170 170 ARG ARG G . n 
C 1 171 HIS 171 171 171 HIS HIS G . n 
C 1 172 CYS 172 172 172 CYS CYS G . n 
C 1 173 GLY 173 173 173 GLY GLY G . n 
C 1 174 TRP 174 174 174 TRP TRP G . n 
C 1 175 LEU 175 175 175 LEU LEU G . n 
C 1 176 ASN 176 176 176 ASN ASN G . n 
C 1 177 GLU 177 177 177 GLU GLU G . n 
C 1 178 ARG 178 178 178 ARG ARG G . n 
C 1 179 ALA 179 179 179 ALA ALA G . n 
C 1 180 LEU 180 180 180 LEU LEU G . n 
C 1 181 SER 181 181 181 SER SER G . n 
C 1 182 ALA 182 182 182 ALA ALA G . n 
C 1 183 MET 183 183 183 MET MET G . n 
C 1 184 VAL 184 184 184 VAL VAL G . n 
C 1 185 LYS 185 185 185 LYS LYS G . n 
C 1 186 HIS 186 186 186 HIS HIS G . n 
C 1 187 TYR 187 187 187 TYR TYR G . n 
C 1 188 ASN 188 188 188 ASN ASN G . n 
C 1 189 GLY 189 189 189 GLY GLY G . n 
C 1 190 ARG 190 190 190 ARG ARG G . n 
C 1 191 ALA 191 191 191 ALA ALA G . n 
C 1 192 PHE 192 192 192 PHE PHE G . n 
C 1 193 ASP 193 193 193 ASP ASP G . n 
C 1 194 GLU 194 194 194 GLU GLU G . n 
C 1 195 VAL 195 195 195 VAL VAL G . n 
C 1 196 PHE 196 196 196 PHE PHE G . n 
C 1 197 LEU 197 197 197 LEU LEU G . n 
C 1 198 CYS 198 198 198 CYS CYS G . n 
C 1 199 ASP 199 199 199 ASP ASP G . n 
C 1 200 LYS 200 200 200 LYS LYS G . n 
C 1 201 ASN 201 201 201 ASN ASN G . n 
C 1 202 ALA 202 202 202 ALA ALA G . n 
C 1 203 PRO 203 203 203 PRO PRO G . n 
C 1 204 TYR 204 204 204 TYR TYR G . n 
C 1 205 TYR 205 205 205 TYR TYR G . n 
C 1 206 GLY 206 206 206 GLY GLY G . n 
C 1 207 PHE 207 207 207 PHE PHE G . n 
C 1 208 ASN 208 208 208 ASN ASN G . n 
C 1 209 SER 209 209 209 SER SER G . n 
C 1 210 TYR 210 210 210 TYR TYR G . n 
C 1 211 ASP 211 211 211 ASP ASP G . n 
C 1 212 ASP 212 212 212 ASP ASP G . n 
C 1 213 PHE 213 213 213 PHE PHE G . n 
C 1 214 PHE 214 214 214 PHE PHE G . n 
C 1 215 ASN 215 215 215 ASN ASN G . n 
C 1 216 ARG 216 216 216 ARG ARG G . n 
C 1 217 ARG 217 217 217 ARG ARG G . n 
C 1 218 PHE 218 218 218 PHE PHE G . n 
C 1 219 ARG 219 219 219 ARG ARG G . n 
C 1 220 ASN 220 220 220 ASN ASN G . n 
C 1 221 ARG 221 221 221 ARG ARG G . n 
C 1 222 ASP 222 222 222 ASP ASP G . n 
C 1 223 ILE 223 223 223 ILE ILE G . n 
C 1 224 ASP 224 224 224 ASP ASP G . n 
C 1 225 ARG 225 225 225 ARG ARG G . n 
C 1 226 PRO 226 226 226 PRO PRO G . n 
C 1 227 VAL 227 227 227 VAL VAL G . n 
C 1 228 VAL 228 228 228 VAL VAL G . n 
C 1 229 GLY 229 229 229 GLY GLY G . n 
C 1 230 GLY 230 230 230 GLY GLY G . n 
C 1 231 VAL 231 231 231 VAL VAL G . n 
C 1 232 ASN 232 232 232 ASN ASN G . n 
C 1 233 ASN 233 233 233 ASN ASN G . n 
C 1 234 THR 234 234 234 THR THR G . n 
C 1 235 THR 235 235 235 THR THR G . n 
C 1 236 LEU 236 236 236 LEU LEU G . n 
C 1 237 ILE 237 237 237 ILE ILE G . n 
C 1 238 SER 238 238 238 SER SER G . n 
C 1 239 ALA 239 239 239 ALA ALA G . n 
C 1 240 ALA 240 240 240 ALA ALA G . n 
C 1 241 CYS 241 241 241 CYS CYS G . n 
C 1 242 GLU 242 242 242 GLU GLU G . n 
C 1 243 SER 243 243 243 SER SER G . n 
C 1 244 LEU 244 244 244 LEU LEU G . n 
C 1 245 SER 245 245 245 SER SER G . n 
C 1 246 TYR 246 246 246 TYR TYR G . n 
C 1 247 ASN 247 247 247 ASN ASN G . n 
C 1 248 VAL 248 248 248 VAL VAL G . n 
C 1 249 SER 249 249 249 SER SER G . n 
C 1 250 TYR 250 250 250 TYR TYR G . n 
C 1 251 ASP 251 251 251 ASP ASP G . n 
C 1 252 VAL 252 252 252 VAL VAL G . n 
C 1 253 GLN 253 253 253 GLN GLN G . n 
C 1 254 SER 254 254 254 SER SER G . n 
C 1 255 LEU 255 255 255 LEU LEU G . n 
C 1 256 ASP 256 256 256 ASP ASP G . n 
C 1 257 THR 257 257 257 THR THR G . n 
C 1 258 LEU 258 258 258 LEU LEU G . n 
C 1 259 VAL 259 259 259 VAL VAL G . n 
C 1 260 PHE 260 260 260 PHE PHE G . n 
C 1 261 LYS 261 261 261 LYS LYS G . n 
C 1 262 GLY 262 262 262 GLY GLY G . n 
C 1 263 GLU 263 263 263 GLU GLU G . n 
C 1 264 THR 264 264 264 THR THR G . n 
C 1 265 TYR 265 265 265 TYR TYR G . n 
C 1 266 SER 266 266 266 SER SER G . n 
C 1 267 LEU 267 267 267 LEU LEU G . n 
C 1 268 LYS 268 268 268 LYS LYS G . n 
C 1 269 HIS 269 269 269 HIS HIS G . n 
C 1 270 LEU 270 270 270 LEU LEU G . n 
C 1 271 LEU 271 271 271 LEU LEU G . n 
C 1 272 ASN 272 272 272 ASN ASN G . n 
C 1 273 ASN 273 273 273 ASN ASN G . n 
C 1 274 ASP 274 274 274 ASP ASP G . n 
C 1 275 PRO 275 275 275 PRO PRO G . n 
C 1 276 PHE 276 276 276 PHE PHE G . n 
C 1 277 THR 277 277 277 THR THR G . n 
C 1 278 PRO 278 278 278 PRO PRO G . n 
C 1 279 GLN 279 279 279 GLN GLN G . n 
C 1 280 PHE 280 280 280 PHE PHE G . n 
C 1 281 GLU 281 281 281 GLU GLU G . n 
C 1 282 HIS 282 282 282 HIS HIS G . n 
C 1 283 GLY 283 283 283 GLY GLY G . n 
C 1 284 SER 284 284 284 SER SER G . n 
C 1 285 ILE 285 285 285 ILE ILE G . n 
C 1 286 LEU 286 286 286 LEU LEU G . n 
C 1 287 GLN 287 287 287 GLN GLN G . n 
C 1 288 GLY 288 288 288 GLY GLY G . n 
C 1 289 PHE 289 289 289 PHE PHE G . n 
C 1 290 LEU 290 290 290 LEU LEU G . n 
C 1 291 ASN 291 291 291 ASN ASN G . n 
C 1 292 VAL 292 292 292 VAL VAL G . n 
C 1 293 THR 293 293 293 THR THR G . n 
C 1 294 ALA 294 294 294 ALA ALA G . n 
C 1 295 TYR 295 295 295 TYR TYR G . n 
C 1 296 HIS 296 296 296 HIS HIS G . n 
C 1 297 ARG 297 297 297 ARG ARG G . n 
C 1 298 TRP 298 298 298 TRP TRP G . n 
C 1 299 HIS 299 299 299 HIS HIS G . n 
C 1 300 ALA 300 300 300 ALA ALA G . n 
C 1 301 PRO 301 301 301 PRO PRO G . n 
C 1 302 VAL 302 302 302 VAL VAL G . n 
C 1 303 ASN 303 303 303 ASN ASN G . n 
C 1 304 GLY 304 304 304 GLY GLY G . n 
C 1 305 THR 305 305 305 THR THR G . n 
C 1 306 ILE 306 306 306 ILE ILE G . n 
C 1 307 VAL 307 307 307 VAL VAL G . n 
C 1 308 LYS 308 308 308 LYS LYS G . n 
C 1 309 ILE 309 309 309 ILE ILE G . n 
C 1 310 ILE 310 310 310 ILE ILE G . n 
C 1 311 ASN 311 311 311 ASN ASN G . n 
C 1 312 VAL 312 312 312 VAL VAL G . n 
C 1 313 PRO 313 313 313 PRO PRO G . n 
C 1 314 GLY 314 314 314 GLY GLY G . n 
C 1 315 THR 315 315 315 THR THR G . n 
C 1 316 TYR 316 316 316 TYR TYR G . n 
C 1 317 PHE 317 317 317 PHE PHE G . n 
C 1 318 ALA 318 318 318 ALA ALA G . n 
C 1 319 GLN 319 319 319 GLN GLN G . n 
C 1 320 ALA 320 320 320 ALA ALA G . n 
C 1 321 PRO 321 321 321 PRO PRO G . n 
C 1 322 SER 322 322 322 SER SER G . n 
C 1 323 THR 323 323 323 THR THR G . n 
C 1 324 ILE 324 324 324 ILE ILE G . n 
C 1 325 GLY 325 325 325 GLY GLY G . n 
C 1 326 ASP 326 326 326 ASP ASP G . n 
C 1 327 PRO 327 327 327 PRO PRO G . n 
C 1 328 ILE 328 328 328 ILE ILE G . n 
C 1 329 PRO 329 329 329 PRO PRO G . n 
C 1 330 ASP 330 330 330 ASP ASP G . n 
C 1 331 ASN 331 331 331 ASN ASN G . n 
C 1 332 ASP 332 332 332 ASP ASP G . n 
C 1 333 TYR 333 333 333 TYR TYR G . n 
C 1 334 ASP 334 334 334 ASP ASP G . n 
C 1 335 PRO 335 335 335 PRO PRO G . n 
C 1 336 PRO 336 336 336 PRO PRO G . n 
C 1 337 PRO 337 337 337 PRO PRO G . n 
C 1 338 TYR 338 338 338 TYR TYR G . n 
C 1 339 LEU 339 339 339 LEU LEU G . n 
C 1 340 LYS 340 340 340 LYS LYS G . n 
C 1 341 SER 341 341 341 SER SER G . n 
C 1 342 LEU 342 342 342 LEU LEU G . n 
C 1 343 VAL 343 343 343 VAL VAL G . n 
C 1 344 TYR 344 344 344 TYR TYR G . n 
C 1 345 PHE 345 345 345 PHE PHE G . n 
C 1 346 SER 346 346 346 SER SER G . n 
C 1 347 ASN 347 347 347 ASN ASN G . n 
C 1 348 ILE 348 348 348 ILE ILE G . n 
C 1 349 ALA 349 349 349 ALA ALA G . n 
C 1 350 ALA 350 350 350 ALA ALA G . n 
C 1 351 ARG 351 351 351 ARG ARG G . n 
C 1 352 GLN 352 352 352 GLN GLN G . n 
C 1 353 ILE 353 353 353 ILE ILE G . n 
C 1 354 MET 354 354 354 MET MET G . n 
C 1 355 PHE 355 355 355 PHE PHE G . n 
C 1 356 ILE 356 356 356 ILE ILE G . n 
C 1 357 GLU 357 357 357 GLU GLU G . n 
C 1 358 ALA 358 358 358 ALA ALA G . n 
C 1 359 ASP 359 359 359 ASP ASP G . n 
C 1 360 ASN 360 360 360 ASN ASN G . n 
C 1 361 LYS 361 361 361 LYS LYS G . n 
C 1 362 GLU 362 362 362 GLU GLU G . n 
C 1 363 ILE 363 363 363 ILE ILE G . n 
C 1 364 GLY 364 364 364 GLY GLY G . n 
C 1 365 LEU 365 365 365 LEU LEU G . n 
C 1 366 ILE 366 366 366 ILE ILE G . n 
C 1 367 PHE 367 367 367 PHE PHE G . n 
C 1 368 LEU 368 368 368 LEU LEU G . n 
C 1 369 VAL 369 369 369 VAL VAL G . n 
C 1 370 PHE 370 370 370 PHE PHE G . n 
C 1 371 ILE 371 371 371 ILE ILE G . n 
C 1 372 GLY 372 372 372 GLY GLY G . n 
C 1 373 MET 373 373 373 MET MET G . n 
C 1 374 THR 374 374 374 THR THR G . n 
C 1 375 GLU 375 375 375 GLU GLU G . n 
C 1 376 ILE 376 376 376 ILE ILE G . n 
C 1 377 SER 377 377 377 SER SER G . n 
C 1 378 THR 378 378 378 THR THR G . n 
C 1 379 CYS 379 379 379 CYS CYS G . n 
C 1 380 GLU 380 380 380 GLU GLU G . n 
C 1 381 ALA 381 381 381 ALA ALA G . n 
C 1 382 THR 382 382 382 THR THR G . n 
C 1 383 VAL 383 383 383 VAL VAL G . n 
C 1 384 SER 384 384 384 SER SER G . n 
C 1 385 GLU 385 385 385 GLU GLU G . n 
C 1 386 GLY 386 386 386 GLY GLY G . n 
C 1 387 GLN 387 387 387 GLN GLN G . n 
C 1 388 HIS 388 388 388 HIS HIS G . n 
C 1 389 VAL 389 389 389 VAL VAL G . n 
C 1 390 ASN 390 390 390 ASN ASN G . n 
C 1 391 ARG 391 391 391 ARG ARG G . n 
C 1 392 GLY 392 392 392 GLY GLY G . n 
C 1 393 ASP 393 393 393 ASP ASP G . n 
C 1 394 ASP 394 394 394 ASP ASP G . n 
C 1 395 LEU 395 395 395 LEU LEU G . n 
C 1 396 GLY 396 396 396 GLY GLY G . n 
C 1 397 MET 397 397 397 MET MET G . n 
C 1 398 PHE 398 398 398 PHE PHE G . n 
C 1 399 HIS 399 399 399 HIS HIS G . n 
C 1 400 PHE 400 400 400 PHE PHE G . n 
C 1 401 GLY 401 401 401 GLY GLY G . n 
C 1 402 GLY 402 402 402 GLY GLY G . n 
D 2 1   SER 1   404 404 SER SER H . n 
D 2 2   PHE 2   405 405 PHE PHE H . n 
D 2 3   ALA 3   406 406 ALA ALA H . n 
D 2 4   LEU 4   407 407 LEU LEU H . n 
D 2 5   GLY 5   408 408 GLY GLY H . n 
D 2 6   LEU 6   409 409 LEU LEU H . n 
D 2 7   ARG 7   410 410 ARG ARG H . n 
D 2 8   LYS 8   411 411 LYS LYS H . n 
D 2 9   ASP 9   412 412 ASP ASP H . n 
D 2 10  CYS 10  413 413 CYS CYS H . n 
D 2 11  ARG 11  414 414 ARG ARG H . n 
D 2 12  ALA 12  415 415 ALA ALA H . n 
D 2 13  GLU 13  416 416 GLU GLU H . n 
D 2 14  ILE 14  417 417 ILE ILE H . n 
D 2 15  VAL 15  418 418 VAL VAL H . n 
D 2 16  GLU 16  419 419 GLU GLU H . n 
D 2 17  LYS 17  420 420 LYS LYS H . n 
D 2 18  PHE 18  421 421 PHE PHE H . n 
D 2 19  THR 19  422 422 THR THR H . n 
D 2 20  GLU 20  423 423 GLU GLU H . n 
D 2 21  PRO 21  424 424 PRO PRO H . n 
D 2 22  GLY 22  425 425 GLY GLY H . n 
D 2 23  THR 23  426 426 THR THR H . n 
D 2 24  VAL 24  427 427 VAL VAL H . n 
D 2 25  ILE 25  428 428 ILE ILE H . n 
D 2 26  ARG 26  429 429 ARG ARG H . n 
D 2 27  ILE 27  430 430 ILE ILE H . n 
D 2 28  ASN 28  431 431 ASN ASN H . n 
D 2 29  GLU 29  432 432 GLU GLU H . n 
D 2 30  VAL 30  433 433 VAL VAL H . n 
D 2 31  VAL 31  434 434 VAL VAL H . n 
D 2 32  ALA 32  435 435 ALA ALA H . n 
D 2 33  ALA 33  436 436 ALA ALA H . n 
D 2 34  LEU 34  437 437 LEU LEU H . n 
D 2 35  LYS 35  438 ?   ?   ?   H . n 
D 2 36  ALA 36  439 ?   ?   ?   H . n 
E 1 1   MET 1   1   ?   ?   ?   A . n 
E 1 2   GLN 2   2   ?   ?   ?   A . n 
E 1 3   VAL 3   3   ?   ?   ?   A . n 
E 1 4   ILE 4   4   ?   ?   ?   A . n 
E 1 5   PRO 5   5   ?   ?   ?   A . n 
E 1 6   ALA 6   6   ?   ?   ?   A . n 
E 1 7   CYS 7   7   ?   ?   ?   A . n 
E 1 8   ASN 8   8   ?   ?   ?   A . n 
E 1 9   SER 9   9   ?   ?   ?   A . n 
E 1 10  ALA 10  10  ?   ?   ?   A . n 
E 1 11  ALA 11  11  ?   ?   ?   A . n 
E 1 12  ILE 12  12  ?   ?   ?   A . n 
E 1 13  ARG 13  13  ?   ?   ?   A . n 
E 1 14  SER 14  14  ?   ?   ?   A . n 
E 1 15  LEU 15  15  ?   ?   ?   A . n 
E 1 16  CYS 16  16  ?   ?   ?   A . n 
E 1 17  PRO 17  17  ?   ?   ?   A . n 
E 1 18  THR 18  18  ?   ?   ?   A . n 
E 1 19  PRO 19  19  ?   ?   ?   A . n 
E 1 20  GLU 20  20  ?   ?   ?   A . n 
E 1 21  SER 21  21  ?   ?   ?   A . n 
E 1 22  PHE 22  22  ?   ?   ?   A . n 
E 1 23  ARG 23  23  ?   ?   ?   A . n 
E 1 24  ASN 24  24  ?   ?   ?   A . n 
E 1 25  MET 25  25  ?   ?   ?   A . n 
E 1 26  GLY 26  26  ?   ?   ?   A . n 
E 1 27  TRP 27  27  ?   ?   ?   A . n 
E 1 28  LEU 28  28  ?   ?   ?   A . n 
E 1 29  SER 29  29  ?   ?   ?   A . n 
E 1 30  VAL 30  30  ?   ?   ?   A . n 
E 1 31  SER 31  31  ?   ?   ?   A . n 
E 1 32  ASP 32  32  ?   ?   ?   A . n 
E 1 33  ALA 33  33  ?   ?   ?   A . n 
E 1 34  VAL 34  34  ?   ?   ?   A . n 
E 1 35  TYR 35  35  ?   ?   ?   A . n 
E 1 36  SER 36  36  ?   ?   ?   A . n 
E 1 37  GLU 37  37  ?   ?   ?   A . n 
E 1 38  PHE 38  38  ?   ?   ?   A . n 
E 1 39  ILE 39  39  ?   ?   ?   A . n 
E 1 40  GLY 40  40  ?   ?   ?   A . n 
E 1 41  GLU 41  41  ?   ?   ?   A . n 
E 1 42  LEU 42  42  ?   ?   ?   A . n 
E 1 43  ALA 43  43  ?   ?   ?   A . n 
E 1 44  THR 44  44  ?   ?   ?   A . n 
E 1 45  ARG 45  45  ?   ?   ?   A . n 
E 1 46  ALA 46  46  ?   ?   ?   A . n 
E 1 47  SER 47  47  ?   ?   ?   A . n 
E 1 48  ASN 48  48  ?   ?   ?   A . n 
E 1 49  ARG 49  49  ?   ?   ?   A . n 
E 1 50  ASN 50  50  ?   ?   ?   A . n 
E 1 51  TYR 51  51  ?   ?   ?   A . n 
E 1 52  SER 52  52  ?   ?   ?   A . n 
E 1 53  ASN 53  53  53  ASN ASN A . n 
E 1 54  GLU 54  54  54  GLU GLU A . n 
E 1 55  PHE 55  55  55  PHE PHE A . n 
E 1 56  GLY 56  56  56  GLY GLY A . n 
E 1 57  LEU 57  57  57  LEU LEU A . n 
E 1 58  MET 58  58  58  MET MET A . n 
E 1 59  GLN 59  59  59  GLN GLN A . n 
E 1 60  PRO 60  60  60  PRO PRO A . n 
E 1 61  ILE 61  61  61  ILE ILE A . n 
E 1 62  GLN 62  62  62  GLN GLN A . n 
E 1 63  GLU 63  63  63  GLU GLU A . n 
E 1 64  PHE 64  64  64  PHE PHE A . n 
E 1 65  LYS 65  65  65  LYS LYS A . n 
E 1 66  ALA 66  66  66  ALA ALA A . n 
E 1 67  PHE 67  67  67  PHE PHE A . n 
E 1 68  ILE 68  68  68  ILE ILE A . n 
E 1 69  GLU 69  69  69  GLU GLU A . n 
E 1 70  SER 70  70  70  SER SER A . n 
E 1 71  ASP 71  71  71  ASP ASP A . n 
E 1 72  PRO 72  72  72  PRO PRO A . n 
E 1 73  VAL 73  73  73  VAL VAL A . n 
E 1 74  VAL 74  74  74  VAL VAL A . n 
E 1 75  HIS 75  75  75  HIS HIS A . n 
E 1 76  GLN 76  76  76  GLN GLN A . n 
E 1 77  GLU 77  77  77  GLU GLU A . n 
E 1 78  PHE 78  78  78  PHE PHE A . n 
E 1 79  ILE 79  79  79  ILE ILE A . n 
E 1 80  ASP 80  80  80  ASP ASP A . n 
E 1 81  MET 81  81  81  MET MET A . n 
E 1 82  PHE 82  82  82  PHE PHE A . n 
E 1 83  GLU 83  83  83  GLU GLU A . n 
E 1 84  GLY 84  84  84  GLY GLY A . n 
E 1 85  ILE 85  85  85  ILE ILE A . n 
E 1 86  GLN 86  86  86  GLN GLN A . n 
E 1 87  ASP 87  87  87  ASP ASP A . n 
E 1 88  SER 88  88  88  SER SER A . n 
E 1 89  PRO 89  89  89  PRO PRO A . n 
E 1 90  ARG 90  90  90  ARG ARG A . n 
E 1 91  ASN 91  91  91  ASN ASN A . n 
E 1 92  TYR 92  92  92  TYR TYR A . n 
E 1 93  GLN 93  93  93  GLN GLN A . n 
E 1 94  GLU 94  94  94  GLU GLU A . n 
E 1 95  LEU 95  95  95  LEU LEU A . n 
E 1 96  CYS 96  96  96  CYS CYS A . n 
E 1 97  ASN 97  97  97  ASN ASN A . n 
E 1 98  MET 98  98  98  MET MET A . n 
E 1 99  PHE 99  99  99  PHE PHE A . n 
E 1 100 ASN 100 100 100 ASN ASN A . n 
E 1 101 ASP 101 101 101 ASP ASP A . n 
E 1 102 ILE 102 102 102 ILE ILE A . n 
E 1 103 PHE 103 103 103 PHE PHE A . n 
E 1 104 ARG 104 104 104 ARG ARG A . n 
E 1 105 LYS 105 105 105 LYS LYS A . n 
E 1 106 ALA 106 106 106 ALA ALA A . n 
E 1 107 PRO 107 107 107 PRO PRO A . n 
E 1 108 VAL 108 108 108 VAL VAL A . n 
E 1 109 TYR 109 109 109 TYR TYR A . n 
E 1 110 GLY 110 110 110 GLY GLY A . n 
E 1 111 ASP 111 111 111 ASP ASP A . n 
E 1 112 LEU 112 112 112 LEU LEU A . n 
E 1 113 GLY 113 113 113 GLY GLY A . n 
E 1 114 PRO 114 114 114 PRO PRO A . n 
E 1 115 PRO 115 115 115 PRO PRO A . n 
E 1 116 VAL 116 116 116 VAL VAL A . n 
E 1 117 TYR 117 117 117 TYR TYR A . n 
E 1 118 MET 118 118 118 MET MET A . n 
E 1 119 ILE 119 119 119 ILE ILE A . n 
E 1 120 MET 120 120 120 MET MET A . n 
E 1 121 ALA 121 121 121 ALA ALA A . n 
E 1 122 LYS 122 122 122 LYS LYS A . n 
E 1 123 LEU 123 123 123 LEU LEU A . n 
E 1 124 MET 124 124 124 MET MET A . n 
E 1 125 ASN 125 125 125 ASN ASN A . n 
E 1 126 THR 126 126 126 THR THR A . n 
E 1 127 ARG 127 127 127 ARG ARG A . n 
E 1 128 ALA 128 128 128 ALA ALA A . n 
E 1 129 GLY 129 129 129 GLY GLY A . n 
E 1 130 PHE 130 130 130 PHE PHE A . n 
E 1 131 SER 131 131 131 SER SER A . n 
E 1 132 ALA 132 132 132 ALA ALA A . n 
E 1 133 PHE 133 133 133 PHE PHE A . n 
E 1 134 THR 134 134 134 THR THR A . n 
E 1 135 ARG 135 135 135 ARG ARG A . n 
E 1 136 GLN 136 136 136 GLN GLN A . n 
E 1 137 ARG 137 137 137 ARG ARG A . n 
E 1 138 LEU 138 138 138 LEU LEU A . n 
E 1 139 ASN 139 139 139 ASN ASN A . n 
E 1 140 LEU 140 140 140 LEU LEU A . n 
E 1 141 HIS 141 141 141 HIS HIS A . n 
E 1 142 PHE 142 142 142 PHE PHE A . n 
E 1 143 LYS 143 143 143 LYS LYS A . n 
E 1 144 LYS 144 144 144 LYS LYS A . n 
E 1 145 LEU 145 145 145 LEU LEU A . n 
E 1 146 PHE 146 146 146 PHE PHE A . n 
E 1 147 ASP 147 147 147 ASP ASP A . n 
E 1 148 THR 148 148 148 THR THR A . n 
E 1 149 TRP 149 149 149 TRP TRP A . n 
E 1 150 GLY 150 150 150 GLY GLY A . n 
E 1 151 LEU 151 151 151 LEU LEU A . n 
E 1 152 PHE 152 152 152 PHE PHE A . n 
E 1 153 LEU 153 153 153 LEU LEU A . n 
E 1 154 SER 154 154 154 SER SER A . n 
E 1 155 SER 155 155 155 SER SER A . n 
E 1 156 LYS 156 156 156 LYS LYS A . n 
E 1 157 ASP 157 157 157 ASP ASP A . n 
E 1 158 SER 158 158 158 SER SER A . n 
E 1 159 ARG 159 159 159 ARG ARG A . n 
E 1 160 ASN 160 160 160 ASN ASN A . n 
E 1 161 VAL 161 161 161 VAL VAL A . n 
E 1 162 LEU 162 162 162 LEU LEU A . n 
E 1 163 VAL 163 163 163 VAL VAL A . n 
E 1 164 ALA 164 164 164 ALA ALA A . n 
E 1 165 ASP 165 165 165 ASP ASP A . n 
E 1 166 GLN 166 166 166 GLN GLN A . n 
E 1 167 PHE 167 167 167 PHE PHE A . n 
E 1 168 ASP 168 168 168 ASP ASP A . n 
E 1 169 ASP 169 169 169 ASP ASP A . n 
E 1 170 ARG 170 170 170 ARG ARG A . n 
E 1 171 HIS 171 171 171 HIS HIS A . n 
E 1 172 CYS 172 172 172 CYS CYS A . n 
E 1 173 GLY 173 173 173 GLY GLY A . n 
E 1 174 TRP 174 174 174 TRP TRP A . n 
E 1 175 LEU 175 175 175 LEU LEU A . n 
E 1 176 ASN 176 176 176 ASN ASN A . n 
E 1 177 GLU 177 177 177 GLU GLU A . n 
E 1 178 ARG 178 178 178 ARG ARG A . n 
E 1 179 ALA 179 179 179 ALA ALA A . n 
E 1 180 LEU 180 180 180 LEU LEU A . n 
E 1 181 SER 181 181 181 SER SER A . n 
E 1 182 ALA 182 182 182 ALA ALA A . n 
E 1 183 MET 183 183 183 MET MET A . n 
E 1 184 VAL 184 184 184 VAL VAL A . n 
E 1 185 LYS 185 185 185 LYS LYS A . n 
E 1 186 HIS 186 186 186 HIS HIS A . n 
E 1 187 TYR 187 187 187 TYR TYR A . n 
E 1 188 ASN 188 188 188 ASN ASN A . n 
E 1 189 GLY 189 189 189 GLY GLY A . n 
E 1 190 ARG 190 190 190 ARG ARG A . n 
E 1 191 ALA 191 191 191 ALA ALA A . n 
E 1 192 PHE 192 192 192 PHE PHE A . n 
E 1 193 ASP 193 193 193 ASP ASP A . n 
E 1 194 GLU 194 194 194 GLU GLU A . n 
E 1 195 VAL 195 195 195 VAL VAL A . n 
E 1 196 PHE 196 196 196 PHE PHE A . n 
E 1 197 LEU 197 197 197 LEU LEU A . n 
E 1 198 CYS 198 198 198 CYS CYS A . n 
E 1 199 ASP 199 199 199 ASP ASP A . n 
E 1 200 LYS 200 200 200 LYS LYS A . n 
E 1 201 ASN 201 201 201 ASN ASN A . n 
E 1 202 ALA 202 202 202 ALA ALA A . n 
E 1 203 PRO 203 203 203 PRO PRO A . n 
E 1 204 TYR 204 204 204 TYR TYR A . n 
E 1 205 TYR 205 205 205 TYR TYR A . n 
E 1 206 GLY 206 206 206 GLY GLY A . n 
E 1 207 PHE 207 207 207 PHE PHE A . n 
E 1 208 ASN 208 208 208 ASN ASN A . n 
E 1 209 SER 209 209 209 SER SER A . n 
E 1 210 TYR 210 210 210 TYR TYR A . n 
E 1 211 ASP 211 211 211 ASP ASP A . n 
E 1 212 ASP 212 212 212 ASP ASP A . n 
E 1 213 PHE 213 213 213 PHE PHE A . n 
E 1 214 PHE 214 214 214 PHE PHE A . n 
E 1 215 ASN 215 215 215 ASN ASN A . n 
E 1 216 ARG 216 216 216 ARG ARG A . n 
E 1 217 ARG 217 217 217 ARG ARG A . n 
E 1 218 PHE 218 218 218 PHE PHE A . n 
E 1 219 ARG 219 219 219 ARG ARG A . n 
E 1 220 ASN 220 220 220 ASN ASN A . n 
E 1 221 ARG 221 221 221 ARG ARG A . n 
E 1 222 ASP 222 222 222 ASP ASP A . n 
E 1 223 ILE 223 223 223 ILE ILE A . n 
E 1 224 ASP 224 224 224 ASP ASP A . n 
E 1 225 ARG 225 225 225 ARG ARG A . n 
E 1 226 PRO 226 226 226 PRO PRO A . n 
E 1 227 VAL 227 227 227 VAL VAL A . n 
E 1 228 VAL 228 228 228 VAL VAL A . n 
E 1 229 GLY 229 229 229 GLY GLY A . n 
E 1 230 GLY 230 230 230 GLY GLY A . n 
E 1 231 VAL 231 231 231 VAL VAL A . n 
E 1 232 ASN 232 232 232 ASN ASN A . n 
E 1 233 ASN 233 233 233 ASN ASN A . n 
E 1 234 THR 234 234 234 THR THR A . n 
E 1 235 THR 235 235 235 THR THR A . n 
E 1 236 LEU 236 236 236 LEU LEU A . n 
E 1 237 ILE 237 237 237 ILE ILE A . n 
E 1 238 SER 238 238 238 SER SER A . n 
E 1 239 ALA 239 239 239 ALA ALA A . n 
E 1 240 ALA 240 240 240 ALA ALA A . n 
E 1 241 CYS 241 241 241 CYS CYS A . n 
E 1 242 GLU 242 242 242 GLU GLU A . n 
E 1 243 SER 243 243 243 SER SER A . n 
E 1 244 LEU 244 244 244 LEU LEU A . n 
E 1 245 SER 245 245 245 SER SER A . n 
E 1 246 TYR 246 246 246 TYR TYR A . n 
E 1 247 ASN 247 247 247 ASN ASN A . n 
E 1 248 VAL 248 248 248 VAL VAL A . n 
E 1 249 SER 249 249 249 SER SER A . n 
E 1 250 TYR 250 250 250 TYR TYR A . n 
E 1 251 ASP 251 251 251 ASP ASP A . n 
E 1 252 VAL 252 252 252 VAL VAL A . n 
E 1 253 GLN 253 253 253 GLN GLN A . n 
E 1 254 SER 254 254 254 SER SER A . n 
E 1 255 LEU 255 255 255 LEU LEU A . n 
E 1 256 ASP 256 256 256 ASP ASP A . n 
E 1 257 THR 257 257 257 THR THR A . n 
E 1 258 LEU 258 258 258 LEU LEU A . n 
E 1 259 VAL 259 259 259 VAL VAL A . n 
E 1 260 PHE 260 260 260 PHE PHE A . n 
E 1 261 LYS 261 261 261 LYS LYS A . n 
E 1 262 GLY 262 262 262 GLY GLY A . n 
E 1 263 GLU 263 263 263 GLU GLU A . n 
E 1 264 THR 264 264 264 THR THR A . n 
E 1 265 TYR 265 265 265 TYR TYR A . n 
E 1 266 SER 266 266 266 SER SER A . n 
E 1 267 LEU 267 267 267 LEU LEU A . n 
E 1 268 LYS 268 268 268 LYS LYS A . n 
E 1 269 HIS 269 269 269 HIS HIS A . n 
E 1 270 LEU 270 270 270 LEU LEU A . n 
E 1 271 LEU 271 271 271 LEU LEU A . n 
E 1 272 ASN 272 272 272 ASN ASN A . n 
E 1 273 ASN 273 273 273 ASN ASN A . n 
E 1 274 ASP 274 274 274 ASP ASP A . n 
E 1 275 PRO 275 275 275 PRO PRO A . n 
E 1 276 PHE 276 276 276 PHE PHE A . n 
E 1 277 THR 277 277 277 THR THR A . n 
E 1 278 PRO 278 278 278 PRO PRO A . n 
E 1 279 GLN 279 279 279 GLN GLN A . n 
E 1 280 PHE 280 280 280 PHE PHE A . n 
E 1 281 GLU 281 281 281 GLU GLU A . n 
E 1 282 HIS 282 282 282 HIS HIS A . n 
E 1 283 GLY 283 283 283 GLY GLY A . n 
E 1 284 SER 284 284 284 SER SER A . n 
E 1 285 ILE 285 285 285 ILE ILE A . n 
E 1 286 LEU 286 286 286 LEU LEU A . n 
E 1 287 GLN 287 287 287 GLN GLN A . n 
E 1 288 GLY 288 288 288 GLY GLY A . n 
E 1 289 PHE 289 289 289 PHE PHE A . n 
E 1 290 LEU 290 290 290 LEU LEU A . n 
E 1 291 ASN 291 291 291 ASN ASN A . n 
E 1 292 VAL 292 292 292 VAL VAL A . n 
E 1 293 THR 293 293 293 THR THR A . n 
E 1 294 ALA 294 294 294 ALA ALA A . n 
E 1 295 TYR 295 295 295 TYR TYR A . n 
E 1 296 HIS 296 296 296 HIS HIS A . n 
E 1 297 ARG 297 297 297 ARG ARG A . n 
E 1 298 TRP 298 298 298 TRP TRP A . n 
E 1 299 HIS 299 299 299 HIS HIS A . n 
E 1 300 ALA 300 300 300 ALA ALA A . n 
E 1 301 PRO 301 301 301 PRO PRO A . n 
E 1 302 VAL 302 302 302 VAL VAL A . n 
E 1 303 ASN 303 303 303 ASN ASN A . n 
E 1 304 GLY 304 304 304 GLY GLY A . n 
E 1 305 THR 305 305 305 THR THR A . n 
E 1 306 ILE 306 306 306 ILE ILE A . n 
E 1 307 VAL 307 307 307 VAL VAL A . n 
E 1 308 LYS 308 308 308 LYS LYS A . n 
E 1 309 ILE 309 309 309 ILE ILE A . n 
E 1 310 ILE 310 310 310 ILE ILE A . n 
E 1 311 ASN 311 311 311 ASN ASN A . n 
E 1 312 VAL 312 312 312 VAL VAL A . n 
E 1 313 PRO 313 313 313 PRO PRO A . n 
E 1 314 GLY 314 314 314 GLY GLY A . n 
E 1 315 THR 315 315 315 THR THR A . n 
E 1 316 TYR 316 316 316 TYR TYR A . n 
E 1 317 PHE 317 317 317 PHE PHE A . n 
E 1 318 ALA 318 318 318 ALA ALA A . n 
E 1 319 GLN 319 319 319 GLN GLN A . n 
E 1 320 ALA 320 320 320 ALA ALA A . n 
E 1 321 PRO 321 321 321 PRO PRO A . n 
E 1 322 SER 322 322 322 SER SER A . n 
E 1 323 THR 323 323 323 THR THR A . n 
E 1 324 ILE 324 324 324 ILE ILE A . n 
E 1 325 GLY 325 325 325 GLY GLY A . n 
E 1 326 ASP 326 326 326 ASP ASP A . n 
E 1 327 PRO 327 327 327 PRO PRO A . n 
E 1 328 ILE 328 328 328 ILE ILE A . n 
E 1 329 PRO 329 329 329 PRO PRO A . n 
E 1 330 ASP 330 330 330 ASP ASP A . n 
E 1 331 ASN 331 331 331 ASN ASN A . n 
E 1 332 ASP 332 332 332 ASP ASP A . n 
E 1 333 TYR 333 333 333 TYR TYR A . n 
E 1 334 ASP 334 334 334 ASP ASP A . n 
E 1 335 PRO 335 335 335 PRO PRO A . n 
E 1 336 PRO 336 336 336 PRO PRO A . n 
E 1 337 PRO 337 337 337 PRO PRO A . n 
E 1 338 TYR 338 338 338 TYR TYR A . n 
E 1 339 LEU 339 339 339 LEU LEU A . n 
E 1 340 LYS 340 340 340 LYS LYS A . n 
E 1 341 SER 341 341 341 SER SER A . n 
E 1 342 LEU 342 342 342 LEU LEU A . n 
E 1 343 VAL 343 343 343 VAL VAL A . n 
E 1 344 TYR 344 344 344 TYR TYR A . n 
E 1 345 PHE 345 345 345 PHE PHE A . n 
E 1 346 SER 346 346 346 SER SER A . n 
E 1 347 ASN 347 347 347 ASN ASN A . n 
E 1 348 ILE 348 348 348 ILE ILE A . n 
E 1 349 ALA 349 349 349 ALA ALA A . n 
E 1 350 ALA 350 350 350 ALA ALA A . n 
E 1 351 ARG 351 351 351 ARG ARG A . n 
E 1 352 GLN 352 352 352 GLN GLN A . n 
E 1 353 ILE 353 353 353 ILE ILE A . n 
E 1 354 MET 354 354 354 MET MET A . n 
E 1 355 PHE 355 355 355 PHE PHE A . n 
E 1 356 ILE 356 356 356 ILE ILE A . n 
E 1 357 GLU 357 357 357 GLU GLU A . n 
E 1 358 ALA 358 358 358 ALA ALA A . n 
E 1 359 ASP 359 359 359 ASP ASP A . n 
E 1 360 ASN 360 360 360 ASN ASN A . n 
E 1 361 LYS 361 361 361 LYS LYS A . n 
E 1 362 GLU 362 362 362 GLU GLU A . n 
E 1 363 ILE 363 363 363 ILE ILE A . n 
E 1 364 GLY 364 364 364 GLY GLY A . n 
E 1 365 LEU 365 365 365 LEU LEU A . n 
E 1 366 ILE 366 366 366 ILE ILE A . n 
E 1 367 PHE 367 367 367 PHE PHE A . n 
E 1 368 LEU 368 368 368 LEU LEU A . n 
E 1 369 VAL 369 369 369 VAL VAL A . n 
E 1 370 PHE 370 370 370 PHE PHE A . n 
E 1 371 ILE 371 371 371 ILE ILE A . n 
E 1 372 GLY 372 372 372 GLY GLY A . n 
E 1 373 MET 373 373 373 MET MET A . n 
E 1 374 THR 374 374 374 THR THR A . n 
E 1 375 GLU 375 375 375 GLU GLU A . n 
E 1 376 ILE 376 376 376 ILE ILE A . n 
E 1 377 SER 377 377 377 SER SER A . n 
E 1 378 THR 378 378 378 THR THR A . n 
E 1 379 CYS 379 379 379 CYS CYS A . n 
E 1 380 GLU 380 380 380 GLU GLU A . n 
E 1 381 ALA 381 381 381 ALA ALA A . n 
E 1 382 THR 382 382 382 THR THR A . n 
E 1 383 VAL 383 383 383 VAL VAL A . n 
E 1 384 SER 384 384 384 SER SER A . n 
E 1 385 GLU 385 385 385 GLU GLU A . n 
E 1 386 GLY 386 386 386 GLY GLY A . n 
E 1 387 GLN 387 387 387 GLN GLN A . n 
E 1 388 HIS 388 388 388 HIS HIS A . n 
E 1 389 VAL 389 389 389 VAL VAL A . n 
E 1 390 ASN 390 390 390 ASN ASN A . n 
E 1 391 ARG 391 391 391 ARG ARG A . n 
E 1 392 GLY 392 392 392 GLY GLY A . n 
E 1 393 ASP 393 393 393 ASP ASP A . n 
E 1 394 ASP 394 394 394 ASP ASP A . n 
E 1 395 LEU 395 395 395 LEU LEU A . n 
E 1 396 GLY 396 396 396 GLY GLY A . n 
E 1 397 MET 397 397 397 MET MET A . n 
E 1 398 PHE 398 398 398 PHE PHE A . n 
E 1 399 HIS 399 399 399 HIS HIS A . n 
E 1 400 PHE 400 400 400 PHE PHE A . n 
E 1 401 GLY 401 401 401 GLY GLY A . n 
E 1 402 GLY 402 402 402 GLY GLY A . n 
F 2 1   SER 1   404 404 SER SER B . n 
F 2 2   PHE 2   405 405 PHE PHE B . n 
F 2 3   ALA 3   406 406 ALA ALA B . n 
F 2 4   LEU 4   407 407 LEU LEU B . n 
F 2 5   GLY 5   408 408 GLY GLY B . n 
F 2 6   LEU 6   409 409 LEU LEU B . n 
F 2 7   ARG 7   410 410 ARG ARG B . n 
F 2 8   LYS 8   411 411 LYS LYS B . n 
F 2 9   ASP 9   412 412 ASP ASP B . n 
F 2 10  CYS 10  413 413 CYS CYS B . n 
F 2 11  ARG 11  414 414 ARG ARG B . n 
F 2 12  ALA 12  415 415 ALA ALA B . n 
F 2 13  GLU 13  416 416 GLU GLU B . n 
F 2 14  ILE 14  417 417 ILE ILE B . n 
F 2 15  VAL 15  418 418 VAL VAL B . n 
F 2 16  GLU 16  419 419 GLU GLU B . n 
F 2 17  LYS 17  420 420 LYS LYS B . n 
F 2 18  PHE 18  421 421 PHE PHE B . n 
F 2 19  THR 19  422 422 THR THR B . n 
F 2 20  GLU 20  423 423 GLU GLU B . n 
F 2 21  PRO 21  424 424 PRO PRO B . n 
F 2 22  GLY 22  425 425 GLY GLY B . n 
F 2 23  THR 23  426 426 THR THR B . n 
F 2 24  VAL 24  427 427 VAL VAL B . n 
F 2 25  ILE 25  428 428 ILE ILE B . n 
F 2 26  ARG 26  429 429 ARG ARG B . n 
F 2 27  ILE 27  430 430 ILE ILE B . n 
F 2 28  ASN 28  431 431 ASN ASN B . n 
F 2 29  GLU 29  432 432 GLU GLU B . n 
F 2 30  VAL 30  433 433 VAL VAL B . n 
F 2 31  VAL 31  434 434 VAL VAL B . n 
F 2 32  ALA 32  435 435 ALA ALA B . n 
F 2 33  ALA 33  436 436 ALA ALA B . n 
F 2 34  LEU 34  437 437 LEU LEU B . n 
F 2 35  LYS 35  438 ?   ?   ?   B . n 
F 2 36  ALA 36  439 ?   ?   ?   B . n 
G 1 1   MET 1   1   ?   ?   ?   C . n 
G 1 2   GLN 2   2   ?   ?   ?   C . n 
G 1 3   VAL 3   3   ?   ?   ?   C . n 
G 1 4   ILE 4   4   ?   ?   ?   C . n 
G 1 5   PRO 5   5   ?   ?   ?   C . n 
G 1 6   ALA 6   6   ?   ?   ?   C . n 
G 1 7   CYS 7   7   ?   ?   ?   C . n 
G 1 8   ASN 8   8   ?   ?   ?   C . n 
G 1 9   SER 9   9   ?   ?   ?   C . n 
G 1 10  ALA 10  10  ?   ?   ?   C . n 
G 1 11  ALA 11  11  ?   ?   ?   C . n 
G 1 12  ILE 12  12  ?   ?   ?   C . n 
G 1 13  ARG 13  13  ?   ?   ?   C . n 
G 1 14  SER 14  14  ?   ?   ?   C . n 
G 1 15  LEU 15  15  ?   ?   ?   C . n 
G 1 16  CYS 16  16  ?   ?   ?   C . n 
G 1 17  PRO 17  17  ?   ?   ?   C . n 
G 1 18  THR 18  18  ?   ?   ?   C . n 
G 1 19  PRO 19  19  ?   ?   ?   C . n 
G 1 20  GLU 20  20  ?   ?   ?   C . n 
G 1 21  SER 21  21  ?   ?   ?   C . n 
G 1 22  PHE 22  22  ?   ?   ?   C . n 
G 1 23  ARG 23  23  ?   ?   ?   C . n 
G 1 24  ASN 24  24  ?   ?   ?   C . n 
G 1 25  MET 25  25  ?   ?   ?   C . n 
G 1 26  GLY 26  26  ?   ?   ?   C . n 
G 1 27  TRP 27  27  ?   ?   ?   C . n 
G 1 28  LEU 28  28  ?   ?   ?   C . n 
G 1 29  SER 29  29  ?   ?   ?   C . n 
G 1 30  VAL 30  30  ?   ?   ?   C . n 
G 1 31  SER 31  31  ?   ?   ?   C . n 
G 1 32  ASP 32  32  ?   ?   ?   C . n 
G 1 33  ALA 33  33  ?   ?   ?   C . n 
G 1 34  VAL 34  34  ?   ?   ?   C . n 
G 1 35  TYR 35  35  ?   ?   ?   C . n 
G 1 36  SER 36  36  ?   ?   ?   C . n 
G 1 37  GLU 37  37  ?   ?   ?   C . n 
G 1 38  PHE 38  38  ?   ?   ?   C . n 
G 1 39  ILE 39  39  ?   ?   ?   C . n 
G 1 40  GLY 40  40  ?   ?   ?   C . n 
G 1 41  GLU 41  41  ?   ?   ?   C . n 
G 1 42  LEU 42  42  ?   ?   ?   C . n 
G 1 43  ALA 43  43  ?   ?   ?   C . n 
G 1 44  THR 44  44  ?   ?   ?   C . n 
G 1 45  ARG 45  45  ?   ?   ?   C . n 
G 1 46  ALA 46  46  ?   ?   ?   C . n 
G 1 47  SER 47  47  ?   ?   ?   C . n 
G 1 48  ASN 48  48  ?   ?   ?   C . n 
G 1 49  ARG 49  49  ?   ?   ?   C . n 
G 1 50  ASN 50  50  ?   ?   ?   C . n 
G 1 51  TYR 51  51  ?   ?   ?   C . n 
G 1 52  SER 52  52  ?   ?   ?   C . n 
G 1 53  ASN 53  53  ?   ?   ?   C . n 
G 1 54  GLU 54  54  ?   ?   ?   C . n 
G 1 55  PHE 55  55  ?   ?   ?   C . n 
G 1 56  GLY 56  56  ?   ?   ?   C . n 
G 1 57  LEU 57  57  57  LEU LEU C . n 
G 1 58  MET 58  58  58  MET MET C . n 
G 1 59  GLN 59  59  59  GLN GLN C . n 
G 1 60  PRO 60  60  60  PRO PRO C . n 
G 1 61  ILE 61  61  61  ILE ILE C . n 
G 1 62  GLN 62  62  62  GLN GLN C . n 
G 1 63  GLU 63  63  63  GLU GLU C . n 
G 1 64  PHE 64  64  64  PHE PHE C . n 
G 1 65  LYS 65  65  65  LYS LYS C . n 
G 1 66  ALA 66  66  66  ALA ALA C . n 
G 1 67  PHE 67  67  67  PHE PHE C . n 
G 1 68  ILE 68  68  68  ILE ILE C . n 
G 1 69  GLU 69  69  69  GLU GLU C . n 
G 1 70  SER 70  70  70  SER SER C . n 
G 1 71  ASP 71  71  71  ASP ASP C . n 
G 1 72  PRO 72  72  72  PRO PRO C . n 
G 1 73  VAL 73  73  73  VAL VAL C . n 
G 1 74  VAL 74  74  74  VAL VAL C . n 
G 1 75  HIS 75  75  75  HIS HIS C . n 
G 1 76  GLN 76  76  76  GLN GLN C . n 
G 1 77  GLU 77  77  77  GLU GLU C . n 
G 1 78  PHE 78  78  78  PHE PHE C . n 
G 1 79  ILE 79  79  79  ILE ILE C . n 
G 1 80  ASP 80  80  80  ASP ASP C . n 
G 1 81  MET 81  81  81  MET MET C . n 
G 1 82  PHE 82  82  82  PHE PHE C . n 
G 1 83  GLU 83  83  83  GLU GLU C . n 
G 1 84  GLY 84  84  84  GLY GLY C . n 
G 1 85  ILE 85  85  85  ILE ILE C . n 
G 1 86  GLN 86  86  86  GLN GLN C . n 
G 1 87  ASP 87  87  87  ASP ASP C . n 
G 1 88  SER 88  88  88  SER SER C . n 
G 1 89  PRO 89  89  89  PRO PRO C . n 
G 1 90  ARG 90  90  90  ARG ARG C . n 
G 1 91  ASN 91  91  91  ASN ASN C . n 
G 1 92  TYR 92  92  92  TYR TYR C . n 
G 1 93  GLN 93  93  93  GLN GLN C . n 
G 1 94  GLU 94  94  94  GLU GLU C . n 
G 1 95  LEU 95  95  95  LEU LEU C . n 
G 1 96  CYS 96  96  96  CYS CYS C . n 
G 1 97  ASN 97  97  97  ASN ASN C . n 
G 1 98  MET 98  98  98  MET MET C . n 
G 1 99  PHE 99  99  99  PHE PHE C . n 
G 1 100 ASN 100 100 100 ASN ASN C . n 
G 1 101 ASP 101 101 101 ASP ASP C . n 
G 1 102 ILE 102 102 102 ILE ILE C . n 
G 1 103 PHE 103 103 103 PHE PHE C . n 
G 1 104 ARG 104 104 104 ARG ARG C . n 
G 1 105 LYS 105 105 105 LYS LYS C . n 
G 1 106 ALA 106 106 106 ALA ALA C . n 
G 1 107 PRO 107 107 107 PRO PRO C . n 
G 1 108 VAL 108 108 108 VAL VAL C . n 
G 1 109 TYR 109 109 109 TYR TYR C . n 
G 1 110 GLY 110 110 110 GLY GLY C . n 
G 1 111 ASP 111 111 111 ASP ASP C . n 
G 1 112 LEU 112 112 112 LEU LEU C . n 
G 1 113 GLY 113 113 113 GLY GLY C . n 
G 1 114 PRO 114 114 114 PRO PRO C . n 
G 1 115 PRO 115 115 115 PRO PRO C . n 
G 1 116 VAL 116 116 116 VAL VAL C . n 
G 1 117 TYR 117 117 117 TYR TYR C . n 
G 1 118 MET 118 118 118 MET MET C . n 
G 1 119 ILE 119 119 119 ILE ILE C . n 
G 1 120 MET 120 120 120 MET MET C . n 
G 1 121 ALA 121 121 121 ALA ALA C . n 
G 1 122 LYS 122 122 122 LYS LYS C . n 
G 1 123 LEU 123 123 123 LEU LEU C . n 
G 1 124 MET 124 124 124 MET MET C . n 
G 1 125 ASN 125 125 125 ASN ASN C . n 
G 1 126 THR 126 126 126 THR THR C . n 
G 1 127 ARG 127 127 127 ARG ARG C . n 
G 1 128 ALA 128 128 128 ALA ALA C . n 
G 1 129 GLY 129 129 129 GLY GLY C . n 
G 1 130 PHE 130 130 130 PHE PHE C . n 
G 1 131 SER 131 131 131 SER SER C . n 
G 1 132 ALA 132 132 132 ALA ALA C . n 
G 1 133 PHE 133 133 133 PHE PHE C . n 
G 1 134 THR 134 134 134 THR THR C . n 
G 1 135 ARG 135 135 135 ARG ARG C . n 
G 1 136 GLN 136 136 136 GLN GLN C . n 
G 1 137 ARG 137 137 137 ARG ARG C . n 
G 1 138 LEU 138 138 138 LEU LEU C . n 
G 1 139 ASN 139 139 139 ASN ASN C . n 
G 1 140 LEU 140 140 140 LEU LEU C . n 
G 1 141 HIS 141 141 141 HIS HIS C . n 
G 1 142 PHE 142 142 142 PHE PHE C . n 
G 1 143 LYS 143 143 143 LYS LYS C . n 
G 1 144 LYS 144 144 144 LYS LYS C . n 
G 1 145 LEU 145 145 145 LEU LEU C . n 
G 1 146 PHE 146 146 146 PHE PHE C . n 
G 1 147 ASP 147 147 147 ASP ASP C . n 
G 1 148 THR 148 148 148 THR THR C . n 
G 1 149 TRP 149 149 149 TRP TRP C . n 
G 1 150 GLY 150 150 150 GLY GLY C . n 
G 1 151 LEU 151 151 151 LEU LEU C . n 
G 1 152 PHE 152 152 152 PHE PHE C . n 
G 1 153 LEU 153 153 153 LEU LEU C . n 
G 1 154 SER 154 154 154 SER SER C . n 
G 1 155 SER 155 155 155 SER SER C . n 
G 1 156 LYS 156 156 156 LYS LYS C . n 
G 1 157 ASP 157 157 157 ASP ASP C . n 
G 1 158 SER 158 158 158 SER SER C . n 
G 1 159 ARG 159 159 159 ARG ARG C . n 
G 1 160 ASN 160 160 160 ASN ASN C . n 
G 1 161 VAL 161 161 161 VAL VAL C . n 
G 1 162 LEU 162 162 162 LEU LEU C . n 
G 1 163 VAL 163 163 163 VAL VAL C . n 
G 1 164 ALA 164 164 164 ALA ALA C . n 
G 1 165 ASP 165 165 165 ASP ASP C . n 
G 1 166 GLN 166 166 166 GLN GLN C . n 
G 1 167 PHE 167 167 167 PHE PHE C . n 
G 1 168 ASP 168 168 168 ASP ASP C . n 
G 1 169 ASP 169 169 169 ASP ASP C . n 
G 1 170 ARG 170 170 170 ARG ARG C . n 
G 1 171 HIS 171 171 171 HIS HIS C . n 
G 1 172 CYS 172 172 172 CYS CYS C . n 
G 1 173 GLY 173 173 173 GLY GLY C . n 
G 1 174 TRP 174 174 174 TRP TRP C . n 
G 1 175 LEU 175 175 175 LEU LEU C . n 
G 1 176 ASN 176 176 176 ASN ASN C . n 
G 1 177 GLU 177 177 177 GLU GLU C . n 
G 1 178 ARG 178 178 178 ARG ARG C . n 
G 1 179 ALA 179 179 179 ALA ALA C . n 
G 1 180 LEU 180 180 180 LEU LEU C . n 
G 1 181 SER 181 181 181 SER SER C . n 
G 1 182 ALA 182 182 182 ALA ALA C . n 
G 1 183 MET 183 183 183 MET MET C . n 
G 1 184 VAL 184 184 184 VAL VAL C . n 
G 1 185 LYS 185 185 185 LYS LYS C . n 
G 1 186 HIS 186 186 186 HIS HIS C . n 
G 1 187 TYR 187 187 187 TYR TYR C . n 
G 1 188 ASN 188 188 188 ASN ASN C . n 
G 1 189 GLY 189 189 189 GLY GLY C . n 
G 1 190 ARG 190 190 190 ARG ARG C . n 
G 1 191 ALA 191 191 191 ALA ALA C . n 
G 1 192 PHE 192 192 192 PHE PHE C . n 
G 1 193 ASP 193 193 193 ASP ASP C . n 
G 1 194 GLU 194 194 194 GLU GLU C . n 
G 1 195 VAL 195 195 195 VAL VAL C . n 
G 1 196 PHE 196 196 196 PHE PHE C . n 
G 1 197 LEU 197 197 197 LEU LEU C . n 
G 1 198 CYS 198 198 198 CYS CYS C . n 
G 1 199 ASP 199 199 199 ASP ASP C . n 
G 1 200 LYS 200 200 200 LYS LYS C . n 
G 1 201 ASN 201 201 201 ASN ASN C . n 
G 1 202 ALA 202 202 202 ALA ALA C . n 
G 1 203 PRO 203 203 203 PRO PRO C . n 
G 1 204 TYR 204 204 204 TYR TYR C . n 
G 1 205 TYR 205 205 205 TYR TYR C . n 
G 1 206 GLY 206 206 206 GLY GLY C . n 
G 1 207 PHE 207 207 207 PHE PHE C . n 
G 1 208 ASN 208 208 208 ASN ASN C . n 
G 1 209 SER 209 209 209 SER SER C . n 
G 1 210 TYR 210 210 210 TYR TYR C . n 
G 1 211 ASP 211 211 211 ASP ASP C . n 
G 1 212 ASP 212 212 212 ASP ASP C . n 
G 1 213 PHE 213 213 213 PHE PHE C . n 
G 1 214 PHE 214 214 214 PHE PHE C . n 
G 1 215 ASN 215 215 215 ASN ASN C . n 
G 1 216 ARG 216 216 216 ARG ARG C . n 
G 1 217 ARG 217 217 217 ARG ARG C . n 
G 1 218 PHE 218 218 218 PHE PHE C . n 
G 1 219 ARG 219 219 219 ARG ARG C . n 
G 1 220 ASN 220 220 220 ASN ASN C . n 
G 1 221 ARG 221 221 221 ARG ARG C . n 
G 1 222 ASP 222 222 222 ASP ASP C . n 
G 1 223 ILE 223 223 223 ILE ILE C . n 
G 1 224 ASP 224 224 224 ASP ASP C . n 
G 1 225 ARG 225 225 225 ARG ARG C . n 
G 1 226 PRO 226 226 226 PRO PRO C . n 
G 1 227 VAL 227 227 227 VAL VAL C . n 
G 1 228 VAL 228 228 228 VAL VAL C . n 
G 1 229 GLY 229 229 229 GLY GLY C . n 
G 1 230 GLY 230 230 230 GLY GLY C . n 
G 1 231 VAL 231 231 231 VAL VAL C . n 
G 1 232 ASN 232 232 232 ASN ASN C . n 
G 1 233 ASN 233 233 233 ASN ASN C . n 
G 1 234 THR 234 234 234 THR THR C . n 
G 1 235 THR 235 235 235 THR THR C . n 
G 1 236 LEU 236 236 236 LEU LEU C . n 
G 1 237 ILE 237 237 237 ILE ILE C . n 
G 1 238 SER 238 238 238 SER SER C . n 
G 1 239 ALA 239 239 239 ALA ALA C . n 
G 1 240 ALA 240 240 240 ALA ALA C . n 
G 1 241 CYS 241 241 241 CYS CYS C . n 
G 1 242 GLU 242 242 242 GLU GLU C . n 
G 1 243 SER 243 243 243 SER SER C . n 
G 1 244 LEU 244 244 244 LEU LEU C . n 
G 1 245 SER 245 245 245 SER SER C . n 
G 1 246 TYR 246 246 246 TYR TYR C . n 
G 1 247 ASN 247 247 247 ASN ASN C . n 
G 1 248 VAL 248 248 248 VAL VAL C . n 
G 1 249 SER 249 249 249 SER SER C . n 
G 1 250 TYR 250 250 250 TYR TYR C . n 
G 1 251 ASP 251 251 251 ASP ASP C . n 
G 1 252 VAL 252 252 252 VAL VAL C . n 
G 1 253 GLN 253 253 253 GLN GLN C . n 
G 1 254 SER 254 254 254 SER SER C . n 
G 1 255 LEU 255 255 255 LEU LEU C . n 
G 1 256 ASP 256 256 256 ASP ASP C . n 
G 1 257 THR 257 257 257 THR THR C . n 
G 1 258 LEU 258 258 258 LEU LEU C . n 
G 1 259 VAL 259 259 259 VAL VAL C . n 
G 1 260 PHE 260 260 260 PHE PHE C . n 
G 1 261 LYS 261 261 261 LYS LYS C . n 
G 1 262 GLY 262 262 262 GLY GLY C . n 
G 1 263 GLU 263 263 263 GLU GLU C . n 
G 1 264 THR 264 264 264 THR THR C . n 
G 1 265 TYR 265 265 265 TYR TYR C . n 
G 1 266 SER 266 266 266 SER SER C . n 
G 1 267 LEU 267 267 267 LEU LEU C . n 
G 1 268 LYS 268 268 268 LYS LYS C . n 
G 1 269 HIS 269 269 269 HIS HIS C . n 
G 1 270 LEU 270 270 270 LEU LEU C . n 
G 1 271 LEU 271 271 271 LEU LEU C . n 
G 1 272 ASN 272 272 272 ASN ASN C . n 
G 1 273 ASN 273 273 273 ASN ASN C . n 
G 1 274 ASP 274 274 274 ASP ASP C . n 
G 1 275 PRO 275 275 275 PRO PRO C . n 
G 1 276 PHE 276 276 276 PHE PHE C . n 
G 1 277 THR 277 277 277 THR THR C . n 
G 1 278 PRO 278 278 278 PRO PRO C . n 
G 1 279 GLN 279 279 279 GLN GLN C . n 
G 1 280 PHE 280 280 280 PHE PHE C . n 
G 1 281 GLU 281 281 281 GLU GLU C . n 
G 1 282 HIS 282 282 282 HIS HIS C . n 
G 1 283 GLY 283 283 283 GLY GLY C . n 
G 1 284 SER 284 284 284 SER SER C . n 
G 1 285 ILE 285 285 285 ILE ILE C . n 
G 1 286 LEU 286 286 286 LEU LEU C . n 
G 1 287 GLN 287 287 287 GLN GLN C . n 
G 1 288 GLY 288 288 288 GLY GLY C . n 
G 1 289 PHE 289 289 289 PHE PHE C . n 
G 1 290 LEU 290 290 290 LEU LEU C . n 
G 1 291 ASN 291 291 291 ASN ASN C . n 
G 1 292 VAL 292 292 292 VAL VAL C . n 
G 1 293 THR 293 293 293 THR THR C . n 
G 1 294 ALA 294 294 294 ALA ALA C . n 
G 1 295 TYR 295 295 295 TYR TYR C . n 
G 1 296 HIS 296 296 296 HIS HIS C . n 
G 1 297 ARG 297 297 297 ARG ARG C . n 
G 1 298 TRP 298 298 298 TRP TRP C . n 
G 1 299 HIS 299 299 299 HIS HIS C . n 
G 1 300 ALA 300 300 300 ALA ALA C . n 
G 1 301 PRO 301 301 301 PRO PRO C . n 
G 1 302 VAL 302 302 302 VAL VAL C . n 
G 1 303 ASN 303 303 303 ASN ASN C . n 
G 1 304 GLY 304 304 304 GLY GLY C . n 
G 1 305 THR 305 305 305 THR THR C . n 
G 1 306 ILE 306 306 306 ILE ILE C . n 
G 1 307 VAL 307 307 307 VAL VAL C . n 
G 1 308 LYS 308 308 308 LYS LYS C . n 
G 1 309 ILE 309 309 309 ILE ILE C . n 
G 1 310 ILE 310 310 310 ILE ILE C . n 
G 1 311 ASN 311 311 311 ASN ASN C . n 
G 1 312 VAL 312 312 312 VAL VAL C . n 
G 1 313 PRO 313 313 313 PRO PRO C . n 
G 1 314 GLY 314 314 314 GLY GLY C . n 
G 1 315 THR 315 315 315 THR THR C . n 
G 1 316 TYR 316 316 316 TYR TYR C . n 
G 1 317 PHE 317 317 317 PHE PHE C . n 
G 1 318 ALA 318 318 318 ALA ALA C . n 
G 1 319 GLN 319 319 319 GLN GLN C . n 
G 1 320 ALA 320 320 320 ALA ALA C . n 
G 1 321 PRO 321 321 321 PRO PRO C . n 
G 1 322 SER 322 322 322 SER SER C . n 
G 1 323 THR 323 323 323 THR THR C . n 
G 1 324 ILE 324 324 324 ILE ILE C . n 
G 1 325 GLY 325 325 325 GLY GLY C . n 
G 1 326 ASP 326 326 326 ASP ASP C . n 
G 1 327 PRO 327 327 327 PRO PRO C . n 
G 1 328 ILE 328 328 328 ILE ILE C . n 
G 1 329 PRO 329 329 329 PRO PRO C . n 
G 1 330 ASP 330 330 330 ASP ASP C . n 
G 1 331 ASN 331 331 331 ASN ASN C . n 
G 1 332 ASP 332 332 332 ASP ASP C . n 
G 1 333 TYR 333 333 333 TYR TYR C . n 
G 1 334 ASP 334 334 334 ASP ASP C . n 
G 1 335 PRO 335 335 335 PRO PRO C . n 
G 1 336 PRO 336 336 336 PRO PRO C . n 
G 1 337 PRO 337 337 337 PRO PRO C . n 
G 1 338 TYR 338 338 338 TYR TYR C . n 
G 1 339 LEU 339 339 339 LEU LEU C . n 
G 1 340 LYS 340 340 340 LYS LYS C . n 
G 1 341 SER 341 341 341 SER SER C . n 
G 1 342 LEU 342 342 342 LEU LEU C . n 
G 1 343 VAL 343 343 343 VAL VAL C . n 
G 1 344 TYR 344 344 344 TYR TYR C . n 
G 1 345 PHE 345 345 345 PHE PHE C . n 
G 1 346 SER 346 346 346 SER SER C . n 
G 1 347 ASN 347 347 347 ASN ASN C . n 
G 1 348 ILE 348 348 348 ILE ILE C . n 
G 1 349 ALA 349 349 349 ALA ALA C . n 
G 1 350 ALA 350 350 350 ALA ALA C . n 
G 1 351 ARG 351 351 351 ARG ARG C . n 
G 1 352 GLN 352 352 352 GLN GLN C . n 
G 1 353 ILE 353 353 353 ILE ILE C . n 
G 1 354 MET 354 354 354 MET MET C . n 
G 1 355 PHE 355 355 355 PHE PHE C . n 
G 1 356 ILE 356 356 356 ILE ILE C . n 
G 1 357 GLU 357 357 357 GLU GLU C . n 
G 1 358 ALA 358 358 358 ALA ALA C . n 
G 1 359 ASP 359 359 359 ASP ASP C . n 
G 1 360 ASN 360 360 360 ASN ASN C . n 
G 1 361 LYS 361 361 361 LYS LYS C . n 
G 1 362 GLU 362 362 362 GLU GLU C . n 
G 1 363 ILE 363 363 363 ILE ILE C . n 
G 1 364 GLY 364 364 364 GLY GLY C . n 
G 1 365 LEU 365 365 365 LEU LEU C . n 
G 1 366 ILE 366 366 366 ILE ILE C . n 
G 1 367 PHE 367 367 367 PHE PHE C . n 
G 1 368 LEU 368 368 368 LEU LEU C . n 
G 1 369 VAL 369 369 369 VAL VAL C . n 
G 1 370 PHE 370 370 370 PHE PHE C . n 
G 1 371 ILE 371 371 371 ILE ILE C . n 
G 1 372 GLY 372 372 372 GLY GLY C . n 
G 1 373 MET 373 373 373 MET MET C . n 
G 1 374 THR 374 374 374 THR THR C . n 
G 1 375 GLU 375 375 375 GLU GLU C . n 
G 1 376 ILE 376 376 376 ILE ILE C . n 
G 1 377 SER 377 377 377 SER SER C . n 
G 1 378 THR 378 378 378 THR THR C . n 
G 1 379 CYS 379 379 379 CYS CYS C . n 
G 1 380 GLU 380 380 380 GLU GLU C . n 
G 1 381 ALA 381 381 381 ALA ALA C . n 
G 1 382 THR 382 382 382 THR THR C . n 
G 1 383 VAL 383 383 383 VAL VAL C . n 
G 1 384 SER 384 384 384 SER SER C . n 
G 1 385 GLU 385 385 385 GLU GLU C . n 
G 1 386 GLY 386 386 386 GLY GLY C . n 
G 1 387 GLN 387 387 387 GLN GLN C . n 
G 1 388 HIS 388 388 388 HIS HIS C . n 
G 1 389 VAL 389 389 389 VAL VAL C . n 
G 1 390 ASN 390 390 390 ASN ASN C . n 
G 1 391 ARG 391 391 391 ARG ARG C . n 
G 1 392 GLY 392 392 392 GLY GLY C . n 
G 1 393 ASP 393 393 393 ASP ASP C . n 
G 1 394 ASP 394 394 394 ASP ASP C . n 
G 1 395 LEU 395 395 395 LEU LEU C . n 
G 1 396 GLY 396 396 396 GLY GLY C . n 
G 1 397 MET 397 397 397 MET MET C . n 
G 1 398 PHE 398 398 398 PHE PHE C . n 
G 1 399 HIS 399 399 399 HIS HIS C . n 
G 1 400 PHE 400 400 400 PHE PHE C . n 
G 1 401 GLY 401 401 401 GLY GLY C . n 
G 1 402 GLY 402 402 402 GLY GLY C . n 
H 2 1   SER 1   404 404 SER SER D . n 
H 2 2   PHE 2   405 405 PHE PHE D . n 
H 2 3   ALA 3   406 406 ALA ALA D . n 
H 2 4   LEU 4   407 407 LEU LEU D . n 
H 2 5   GLY 5   408 408 GLY GLY D . n 
H 2 6   LEU 6   409 409 LEU LEU D . n 
H 2 7   ARG 7   410 410 ARG ARG D . n 
H 2 8   LYS 8   411 411 LYS LYS D . n 
H 2 9   ASP 9   412 412 ASP ASP D . n 
H 2 10  CYS 10  413 413 CYS CYS D . n 
H 2 11  ARG 11  414 414 ARG ARG D . n 
H 2 12  ALA 12  415 415 ALA ALA D . n 
H 2 13  GLU 13  416 416 GLU GLU D . n 
H 2 14  ILE 14  417 417 ILE ILE D . n 
H 2 15  VAL 15  418 418 VAL VAL D . n 
H 2 16  GLU 16  419 419 GLU GLU D . n 
H 2 17  LYS 17  420 420 LYS LYS D . n 
H 2 18  PHE 18  421 421 PHE PHE D . n 
H 2 19  THR 19  422 422 THR THR D . n 
H 2 20  GLU 20  423 423 GLU GLU D . n 
H 2 21  PRO 21  424 424 PRO PRO D . n 
H 2 22  GLY 22  425 425 GLY GLY D . n 
H 2 23  THR 23  426 426 THR THR D . n 
H 2 24  VAL 24  427 427 VAL VAL D . n 
H 2 25  ILE 25  428 428 ILE ILE D . n 
H 2 26  ARG 26  429 429 ARG ARG D . n 
H 2 27  ILE 27  430 430 ILE ILE D . n 
H 2 28  ASN 28  431 431 ASN ASN D . n 
H 2 29  GLU 29  432 432 GLU GLU D . n 
H 2 30  VAL 30  433 433 VAL VAL D . n 
H 2 31  VAL 31  434 434 VAL VAL D . n 
H 2 32  ALA 32  435 435 ALA ALA D . n 
H 2 33  ALA 33  436 436 ALA ALA D . n 
H 2 34  LEU 34  437 437 LEU LEU D . n 
H 2 35  LYS 35  438 ?   ?   ?   D . n 
H 2 36  ALA 36  439 ?   ?   ?   D . n 
I 1 1   MET 1   1   ?   ?   ?   E . n 
I 1 2   GLN 2   2   ?   ?   ?   E . n 
I 1 3   VAL 3   3   ?   ?   ?   E . n 
I 1 4   ILE 4   4   ?   ?   ?   E . n 
I 1 5   PRO 5   5   ?   ?   ?   E . n 
I 1 6   ALA 6   6   ?   ?   ?   E . n 
I 1 7   CYS 7   7   ?   ?   ?   E . n 
I 1 8   ASN 8   8   ?   ?   ?   E . n 
I 1 9   SER 9   9   ?   ?   ?   E . n 
I 1 10  ALA 10  10  ?   ?   ?   E . n 
I 1 11  ALA 11  11  ?   ?   ?   E . n 
I 1 12  ILE 12  12  ?   ?   ?   E . n 
I 1 13  ARG 13  13  ?   ?   ?   E . n 
I 1 14  SER 14  14  ?   ?   ?   E . n 
I 1 15  LEU 15  15  ?   ?   ?   E . n 
I 1 16  CYS 16  16  ?   ?   ?   E . n 
I 1 17  PRO 17  17  ?   ?   ?   E . n 
I 1 18  THR 18  18  ?   ?   ?   E . n 
I 1 19  PRO 19  19  ?   ?   ?   E . n 
I 1 20  GLU 20  20  ?   ?   ?   E . n 
I 1 21  SER 21  21  ?   ?   ?   E . n 
I 1 22  PHE 22  22  ?   ?   ?   E . n 
I 1 23  ARG 23  23  ?   ?   ?   E . n 
I 1 24  ASN 24  24  ?   ?   ?   E . n 
I 1 25  MET 25  25  ?   ?   ?   E . n 
I 1 26  GLY 26  26  ?   ?   ?   E . n 
I 1 27  TRP 27  27  ?   ?   ?   E . n 
I 1 28  LEU 28  28  ?   ?   ?   E . n 
I 1 29  SER 29  29  ?   ?   ?   E . n 
I 1 30  VAL 30  30  ?   ?   ?   E . n 
I 1 31  SER 31  31  ?   ?   ?   E . n 
I 1 32  ASP 32  32  ?   ?   ?   E . n 
I 1 33  ALA 33  33  ?   ?   ?   E . n 
I 1 34  VAL 34  34  ?   ?   ?   E . n 
I 1 35  TYR 35  35  ?   ?   ?   E . n 
I 1 36  SER 36  36  ?   ?   ?   E . n 
I 1 37  GLU 37  37  ?   ?   ?   E . n 
I 1 38  PHE 38  38  ?   ?   ?   E . n 
I 1 39  ILE 39  39  ?   ?   ?   E . n 
I 1 40  GLY 40  40  ?   ?   ?   E . n 
I 1 41  GLU 41  41  ?   ?   ?   E . n 
I 1 42  LEU 42  42  ?   ?   ?   E . n 
I 1 43  ALA 43  43  ?   ?   ?   E . n 
I 1 44  THR 44  44  ?   ?   ?   E . n 
I 1 45  ARG 45  45  ?   ?   ?   E . n 
I 1 46  ALA 46  46  ?   ?   ?   E . n 
I 1 47  SER 47  47  ?   ?   ?   E . n 
I 1 48  ASN 48  48  ?   ?   ?   E . n 
I 1 49  ARG 49  49  ?   ?   ?   E . n 
I 1 50  ASN 50  50  ?   ?   ?   E . n 
I 1 51  TYR 51  51  ?   ?   ?   E . n 
I 1 52  SER 52  52  ?   ?   ?   E . n 
I 1 53  ASN 53  53  ?   ?   ?   E . n 
I 1 54  GLU 54  54  ?   ?   ?   E . n 
I 1 55  PHE 55  55  ?   ?   ?   E . n 
I 1 56  GLY 56  56  ?   ?   ?   E . n 
I 1 57  LEU 57  57  57  LEU LEU E . n 
I 1 58  MET 58  58  58  MET MET E . n 
I 1 59  GLN 59  59  59  GLN GLN E . n 
I 1 60  PRO 60  60  60  PRO PRO E . n 
I 1 61  ILE 61  61  61  ILE ILE E . n 
I 1 62  GLN 62  62  62  GLN GLN E . n 
I 1 63  GLU 63  63  63  GLU GLU E . n 
I 1 64  PHE 64  64  64  PHE PHE E . n 
I 1 65  LYS 65  65  65  LYS LYS E . n 
I 1 66  ALA 66  66  66  ALA ALA E . n 
I 1 67  PHE 67  67  67  PHE PHE E . n 
I 1 68  ILE 68  68  68  ILE ILE E . n 
I 1 69  GLU 69  69  69  GLU GLU E . n 
I 1 70  SER 70  70  70  SER SER E . n 
I 1 71  ASP 71  71  71  ASP ASP E . n 
I 1 72  PRO 72  72  72  PRO PRO E . n 
I 1 73  VAL 73  73  73  VAL VAL E . n 
I 1 74  VAL 74  74  74  VAL VAL E . n 
I 1 75  HIS 75  75  75  HIS HIS E . n 
I 1 76  GLN 76  76  76  GLN GLN E . n 
I 1 77  GLU 77  77  77  GLU GLU E . n 
I 1 78  PHE 78  78  78  PHE PHE E . n 
I 1 79  ILE 79  79  79  ILE ILE E . n 
I 1 80  ASP 80  80  80  ASP ASP E . n 
I 1 81  MET 81  81  81  MET MET E . n 
I 1 82  PHE 82  82  82  PHE PHE E . n 
I 1 83  GLU 83  83  83  GLU GLU E . n 
I 1 84  GLY 84  84  84  GLY GLY E . n 
I 1 85  ILE 85  85  85  ILE ILE E . n 
I 1 86  GLN 86  86  86  GLN GLN E . n 
I 1 87  ASP 87  87  87  ASP ASP E . n 
I 1 88  SER 88  88  88  SER SER E . n 
I 1 89  PRO 89  89  89  PRO PRO E . n 
I 1 90  ARG 90  90  90  ARG ARG E . n 
I 1 91  ASN 91  91  91  ASN ASN E . n 
I 1 92  TYR 92  92  92  TYR TYR E . n 
I 1 93  GLN 93  93  93  GLN GLN E . n 
I 1 94  GLU 94  94  94  GLU GLU E . n 
I 1 95  LEU 95  95  95  LEU LEU E . n 
I 1 96  CYS 96  96  96  CYS CYS E . n 
I 1 97  ASN 97  97  97  ASN ASN E . n 
I 1 98  MET 98  98  98  MET MET E . n 
I 1 99  PHE 99  99  99  PHE PHE E . n 
I 1 100 ASN 100 100 100 ASN ASN E . n 
I 1 101 ASP 101 101 101 ASP ASP E . n 
I 1 102 ILE 102 102 102 ILE ILE E . n 
I 1 103 PHE 103 103 103 PHE PHE E . n 
I 1 104 ARG 104 104 104 ARG ARG E . n 
I 1 105 LYS 105 105 105 LYS LYS E . n 
I 1 106 ALA 106 106 106 ALA ALA E . n 
I 1 107 PRO 107 107 107 PRO PRO E . n 
I 1 108 VAL 108 108 108 VAL VAL E . n 
I 1 109 TYR 109 109 109 TYR TYR E . n 
I 1 110 GLY 110 110 110 GLY GLY E . n 
I 1 111 ASP 111 111 111 ASP ASP E . n 
I 1 112 LEU 112 112 112 LEU LEU E . n 
I 1 113 GLY 113 113 113 GLY GLY E . n 
I 1 114 PRO 114 114 114 PRO PRO E . n 
I 1 115 PRO 115 115 115 PRO PRO E . n 
I 1 116 VAL 116 116 116 VAL VAL E . n 
I 1 117 TYR 117 117 117 TYR TYR E . n 
I 1 118 MET 118 118 118 MET MET E . n 
I 1 119 ILE 119 119 119 ILE ILE E . n 
I 1 120 MET 120 120 120 MET MET E . n 
I 1 121 ALA 121 121 121 ALA ALA E . n 
I 1 122 LYS 122 122 122 LYS LYS E . n 
I 1 123 LEU 123 123 123 LEU LEU E . n 
I 1 124 MET 124 124 124 MET MET E . n 
I 1 125 ASN 125 125 125 ASN ASN E . n 
I 1 126 THR 126 126 126 THR THR E . n 
I 1 127 ARG 127 127 127 ARG ARG E . n 
I 1 128 ALA 128 128 128 ALA ALA E . n 
I 1 129 GLY 129 129 129 GLY GLY E . n 
I 1 130 PHE 130 130 130 PHE PHE E . n 
I 1 131 SER 131 131 131 SER SER E . n 
I 1 132 ALA 132 132 132 ALA ALA E . n 
I 1 133 PHE 133 133 133 PHE PHE E . n 
I 1 134 THR 134 134 134 THR THR E . n 
I 1 135 ARG 135 135 135 ARG ARG E . n 
I 1 136 GLN 136 136 136 GLN GLN E . n 
I 1 137 ARG 137 137 137 ARG ARG E . n 
I 1 138 LEU 138 138 138 LEU LEU E . n 
I 1 139 ASN 139 139 139 ASN ASN E . n 
I 1 140 LEU 140 140 140 LEU LEU E . n 
I 1 141 HIS 141 141 141 HIS HIS E . n 
I 1 142 PHE 142 142 142 PHE PHE E . n 
I 1 143 LYS 143 143 143 LYS LYS E . n 
I 1 144 LYS 144 144 144 LYS LYS E . n 
I 1 145 LEU 145 145 145 LEU LEU E . n 
I 1 146 PHE 146 146 146 PHE PHE E . n 
I 1 147 ASP 147 147 147 ASP ASP E . n 
I 1 148 THR 148 148 148 THR THR E . n 
I 1 149 TRP 149 149 149 TRP TRP E . n 
I 1 150 GLY 150 150 150 GLY GLY E . n 
I 1 151 LEU 151 151 151 LEU LEU E . n 
I 1 152 PHE 152 152 152 PHE PHE E . n 
I 1 153 LEU 153 153 153 LEU LEU E . n 
I 1 154 SER 154 154 154 SER SER E . n 
I 1 155 SER 155 155 155 SER SER E . n 
I 1 156 LYS 156 156 156 LYS LYS E . n 
I 1 157 ASP 157 157 157 ASP ASP E . n 
I 1 158 SER 158 158 158 SER SER E . n 
I 1 159 ARG 159 159 159 ARG ARG E . n 
I 1 160 ASN 160 160 160 ASN ASN E . n 
I 1 161 VAL 161 161 161 VAL VAL E . n 
I 1 162 LEU 162 162 162 LEU LEU E . n 
I 1 163 VAL 163 163 163 VAL VAL E . n 
I 1 164 ALA 164 164 164 ALA ALA E . n 
I 1 165 ASP 165 165 165 ASP ASP E . n 
I 1 166 GLN 166 166 166 GLN GLN E . n 
I 1 167 PHE 167 167 167 PHE PHE E . n 
I 1 168 ASP 168 168 168 ASP ASP E . n 
I 1 169 ASP 169 169 169 ASP ASP E . n 
I 1 170 ARG 170 170 170 ARG ARG E . n 
I 1 171 HIS 171 171 171 HIS HIS E . n 
I 1 172 CYS 172 172 172 CYS CYS E . n 
I 1 173 GLY 173 173 173 GLY GLY E . n 
I 1 174 TRP 174 174 174 TRP TRP E . n 
I 1 175 LEU 175 175 175 LEU LEU E . n 
I 1 176 ASN 176 176 176 ASN ASN E . n 
I 1 177 GLU 177 177 177 GLU GLU E . n 
I 1 178 ARG 178 178 178 ARG ARG E . n 
I 1 179 ALA 179 179 179 ALA ALA E . n 
I 1 180 LEU 180 180 180 LEU LEU E . n 
I 1 181 SER 181 181 181 SER SER E . n 
I 1 182 ALA 182 182 182 ALA ALA E . n 
I 1 183 MET 183 183 183 MET MET E . n 
I 1 184 VAL 184 184 184 VAL VAL E . n 
I 1 185 LYS 185 185 185 LYS LYS E . n 
I 1 186 HIS 186 186 186 HIS HIS E . n 
I 1 187 TYR 187 187 187 TYR TYR E . n 
I 1 188 ASN 188 188 188 ASN ASN E . n 
I 1 189 GLY 189 189 189 GLY GLY E . n 
I 1 190 ARG 190 190 190 ARG ARG E . n 
I 1 191 ALA 191 191 191 ALA ALA E . n 
I 1 192 PHE 192 192 192 PHE PHE E . n 
I 1 193 ASP 193 193 193 ASP ASP E . n 
I 1 194 GLU 194 194 194 GLU GLU E . n 
I 1 195 VAL 195 195 195 VAL VAL E . n 
I 1 196 PHE 196 196 196 PHE PHE E . n 
I 1 197 LEU 197 197 197 LEU LEU E . n 
I 1 198 CYS 198 198 198 CYS CYS E . n 
I 1 199 ASP 199 199 199 ASP ASP E . n 
I 1 200 LYS 200 200 200 LYS LYS E . n 
I 1 201 ASN 201 201 201 ASN ASN E . n 
I 1 202 ALA 202 202 202 ALA ALA E . n 
I 1 203 PRO 203 203 203 PRO PRO E . n 
I 1 204 TYR 204 204 204 TYR TYR E . n 
I 1 205 TYR 205 205 205 TYR TYR E . n 
I 1 206 GLY 206 206 206 GLY GLY E . n 
I 1 207 PHE 207 207 207 PHE PHE E . n 
I 1 208 ASN 208 208 208 ASN ASN E . n 
I 1 209 SER 209 209 209 SER SER E . n 
I 1 210 TYR 210 210 210 TYR TYR E . n 
I 1 211 ASP 211 211 211 ASP ASP E . n 
I 1 212 ASP 212 212 212 ASP ASP E . n 
I 1 213 PHE 213 213 213 PHE PHE E . n 
I 1 214 PHE 214 214 214 PHE PHE E . n 
I 1 215 ASN 215 215 215 ASN ASN E . n 
I 1 216 ARG 216 216 216 ARG ARG E . n 
I 1 217 ARG 217 217 217 ARG ARG E . n 
I 1 218 PHE 218 218 218 PHE PHE E . n 
I 1 219 ARG 219 219 219 ARG ARG E . n 
I 1 220 ASN 220 220 220 ASN ASN E . n 
I 1 221 ARG 221 221 221 ARG ARG E . n 
I 1 222 ASP 222 222 222 ASP ASP E . n 
I 1 223 ILE 223 223 223 ILE ILE E . n 
I 1 224 ASP 224 224 224 ASP ASP E . n 
I 1 225 ARG 225 225 225 ARG ARG E . n 
I 1 226 PRO 226 226 226 PRO PRO E . n 
I 1 227 VAL 227 227 227 VAL VAL E . n 
I 1 228 VAL 228 228 228 VAL VAL E . n 
I 1 229 GLY 229 229 229 GLY GLY E . n 
I 1 230 GLY 230 230 230 GLY GLY E . n 
I 1 231 VAL 231 231 231 VAL VAL E . n 
I 1 232 ASN 232 232 232 ASN ASN E . n 
I 1 233 ASN 233 233 233 ASN ASN E . n 
I 1 234 THR 234 234 234 THR THR E . n 
I 1 235 THR 235 235 235 THR THR E . n 
I 1 236 LEU 236 236 236 LEU LEU E . n 
I 1 237 ILE 237 237 237 ILE ILE E . n 
I 1 238 SER 238 238 238 SER SER E . n 
I 1 239 ALA 239 239 239 ALA ALA E . n 
I 1 240 ALA 240 240 240 ALA ALA E . n 
I 1 241 CYS 241 241 241 CYS CYS E . n 
I 1 242 GLU 242 242 242 GLU GLU E . n 
I 1 243 SER 243 243 243 SER SER E . n 
I 1 244 LEU 244 244 244 LEU LEU E . n 
I 1 245 SER 245 245 245 SER SER E . n 
I 1 246 TYR 246 246 246 TYR TYR E . n 
I 1 247 ASN 247 247 247 ASN ASN E . n 
I 1 248 VAL 248 248 248 VAL VAL E . n 
I 1 249 SER 249 249 249 SER SER E . n 
I 1 250 TYR 250 250 250 TYR TYR E . n 
I 1 251 ASP 251 251 251 ASP ASP E . n 
I 1 252 VAL 252 252 252 VAL VAL E . n 
I 1 253 GLN 253 253 253 GLN GLN E . n 
I 1 254 SER 254 254 254 SER SER E . n 
I 1 255 LEU 255 255 255 LEU LEU E . n 
I 1 256 ASP 256 256 256 ASP ASP E . n 
I 1 257 THR 257 257 257 THR THR E . n 
I 1 258 LEU 258 258 258 LEU LEU E . n 
I 1 259 VAL 259 259 259 VAL VAL E . n 
I 1 260 PHE 260 260 260 PHE PHE E . n 
I 1 261 LYS 261 261 261 LYS LYS E . n 
I 1 262 GLY 262 262 262 GLY GLY E . n 
I 1 263 GLU 263 263 263 GLU GLU E . n 
I 1 264 THR 264 264 264 THR THR E . n 
I 1 265 TYR 265 265 265 TYR TYR E . n 
I 1 266 SER 266 266 266 SER SER E . n 
I 1 267 LEU 267 267 267 LEU LEU E . n 
I 1 268 LYS 268 268 268 LYS LYS E . n 
I 1 269 HIS 269 269 269 HIS HIS E . n 
I 1 270 LEU 270 270 270 LEU LEU E . n 
I 1 271 LEU 271 271 271 LEU LEU E . n 
I 1 272 ASN 272 272 272 ASN ASN E . n 
I 1 273 ASN 273 273 273 ASN ASN E . n 
I 1 274 ASP 274 274 274 ASP ASP E . n 
I 1 275 PRO 275 275 275 PRO PRO E . n 
I 1 276 PHE 276 276 276 PHE PHE E . n 
I 1 277 THR 277 277 277 THR THR E . n 
I 1 278 PRO 278 278 278 PRO PRO E . n 
I 1 279 GLN 279 279 279 GLN GLN E . n 
I 1 280 PHE 280 280 280 PHE PHE E . n 
I 1 281 GLU 281 281 281 GLU GLU E . n 
I 1 282 HIS 282 282 282 HIS HIS E . n 
I 1 283 GLY 283 283 283 GLY GLY E . n 
I 1 284 SER 284 284 284 SER SER E . n 
I 1 285 ILE 285 285 285 ILE ILE E . n 
I 1 286 LEU 286 286 286 LEU LEU E . n 
I 1 287 GLN 287 287 287 GLN GLN E . n 
I 1 288 GLY 288 288 288 GLY GLY E . n 
I 1 289 PHE 289 289 289 PHE PHE E . n 
I 1 290 LEU 290 290 290 LEU LEU E . n 
I 1 291 ASN 291 291 291 ASN ASN E . n 
I 1 292 VAL 292 292 292 VAL VAL E . n 
I 1 293 THR 293 293 293 THR THR E . n 
I 1 294 ALA 294 294 294 ALA ALA E . n 
I 1 295 TYR 295 295 295 TYR TYR E . n 
I 1 296 HIS 296 296 296 HIS HIS E . n 
I 1 297 ARG 297 297 297 ARG ARG E . n 
I 1 298 TRP 298 298 298 TRP TRP E . n 
I 1 299 HIS 299 299 299 HIS HIS E . n 
I 1 300 ALA 300 300 300 ALA ALA E . n 
I 1 301 PRO 301 301 301 PRO PRO E . n 
I 1 302 VAL 302 302 302 VAL VAL E . n 
I 1 303 ASN 303 303 303 ASN ASN E . n 
I 1 304 GLY 304 304 304 GLY GLY E . n 
I 1 305 THR 305 305 305 THR THR E . n 
I 1 306 ILE 306 306 306 ILE ILE E . n 
I 1 307 VAL 307 307 307 VAL VAL E . n 
I 1 308 LYS 308 308 308 LYS LYS E . n 
I 1 309 ILE 309 309 309 ILE ILE E . n 
I 1 310 ILE 310 310 310 ILE ILE E . n 
I 1 311 ASN 311 311 311 ASN ASN E . n 
I 1 312 VAL 312 312 312 VAL VAL E . n 
I 1 313 PRO 313 313 313 PRO PRO E . n 
I 1 314 GLY 314 314 314 GLY GLY E . n 
I 1 315 THR 315 315 315 THR THR E . n 
I 1 316 TYR 316 316 316 TYR TYR E . n 
I 1 317 PHE 317 317 317 PHE PHE E . n 
I 1 318 ALA 318 318 318 ALA ALA E . n 
I 1 319 GLN 319 319 319 GLN GLN E . n 
I 1 320 ALA 320 320 320 ALA ALA E . n 
I 1 321 PRO 321 321 321 PRO PRO E . n 
I 1 322 SER 322 322 322 SER SER E . n 
I 1 323 THR 323 323 323 THR THR E . n 
I 1 324 ILE 324 324 324 ILE ILE E . n 
I 1 325 GLY 325 325 325 GLY GLY E . n 
I 1 326 ASP 326 326 326 ASP ASP E . n 
I 1 327 PRO 327 327 327 PRO PRO E . n 
I 1 328 ILE 328 328 328 ILE ILE E . n 
I 1 329 PRO 329 329 329 PRO PRO E . n 
I 1 330 ASP 330 330 330 ASP ASP E . n 
I 1 331 ASN 331 331 331 ASN ASN E . n 
I 1 332 ASP 332 332 332 ASP ASP E . n 
I 1 333 TYR 333 333 333 TYR TYR E . n 
I 1 334 ASP 334 334 334 ASP ASP E . n 
I 1 335 PRO 335 335 335 PRO PRO E . n 
I 1 336 PRO 336 336 336 PRO PRO E . n 
I 1 337 PRO 337 337 337 PRO PRO E . n 
I 1 338 TYR 338 338 338 TYR TYR E . n 
I 1 339 LEU 339 339 339 LEU LEU E . n 
I 1 340 LYS 340 340 340 LYS LYS E . n 
I 1 341 SER 341 341 341 SER SER E . n 
I 1 342 LEU 342 342 342 LEU LEU E . n 
I 1 343 VAL 343 343 343 VAL VAL E . n 
I 1 344 TYR 344 344 344 TYR TYR E . n 
I 1 345 PHE 345 345 345 PHE PHE E . n 
I 1 346 SER 346 346 346 SER SER E . n 
I 1 347 ASN 347 347 347 ASN ASN E . n 
I 1 348 ILE 348 348 348 ILE ILE E . n 
I 1 349 ALA 349 349 349 ALA ALA E . n 
I 1 350 ALA 350 350 350 ALA ALA E . n 
I 1 351 ARG 351 351 351 ARG ARG E . n 
I 1 352 GLN 352 352 352 GLN GLN E . n 
I 1 353 ILE 353 353 353 ILE ILE E . n 
I 1 354 MET 354 354 354 MET MET E . n 
I 1 355 PHE 355 355 355 PHE PHE E . n 
I 1 356 ILE 356 356 356 ILE ILE E . n 
I 1 357 GLU 357 357 357 GLU GLU E . n 
I 1 358 ALA 358 358 358 ALA ALA E . n 
I 1 359 ASP 359 359 359 ASP ASP E . n 
I 1 360 ASN 360 360 360 ASN ASN E . n 
I 1 361 LYS 361 361 361 LYS LYS E . n 
I 1 362 GLU 362 362 362 GLU GLU E . n 
I 1 363 ILE 363 363 363 ILE ILE E . n 
I 1 364 GLY 364 364 364 GLY GLY E . n 
I 1 365 LEU 365 365 365 LEU LEU E . n 
I 1 366 ILE 366 366 366 ILE ILE E . n 
I 1 367 PHE 367 367 367 PHE PHE E . n 
I 1 368 LEU 368 368 368 LEU LEU E . n 
I 1 369 VAL 369 369 369 VAL VAL E . n 
I 1 370 PHE 370 370 370 PHE PHE E . n 
I 1 371 ILE 371 371 371 ILE ILE E . n 
I 1 372 GLY 372 372 372 GLY GLY E . n 
I 1 373 MET 373 373 373 MET MET E . n 
I 1 374 THR 374 374 374 THR THR E . n 
I 1 375 GLU 375 375 375 GLU GLU E . n 
I 1 376 ILE 376 376 376 ILE ILE E . n 
I 1 377 SER 377 377 377 SER SER E . n 
I 1 378 THR 378 378 378 THR THR E . n 
I 1 379 CYS 379 379 379 CYS CYS E . n 
I 1 380 GLU 380 380 380 GLU GLU E . n 
I 1 381 ALA 381 381 381 ALA ALA E . n 
I 1 382 THR 382 382 382 THR THR E . n 
I 1 383 VAL 383 383 383 VAL VAL E . n 
I 1 384 SER 384 384 384 SER SER E . n 
I 1 385 GLU 385 385 385 GLU GLU E . n 
I 1 386 GLY 386 386 386 GLY GLY E . n 
I 1 387 GLN 387 387 387 GLN GLN E . n 
I 1 388 HIS 388 388 388 HIS HIS E . n 
I 1 389 VAL 389 389 389 VAL VAL E . n 
I 1 390 ASN 390 390 390 ASN ASN E . n 
I 1 391 ARG 391 391 391 ARG ARG E . n 
I 1 392 GLY 392 392 392 GLY GLY E . n 
I 1 393 ASP 393 393 393 ASP ASP E . n 
I 1 394 ASP 394 394 394 ASP ASP E . n 
I 1 395 LEU 395 395 395 LEU LEU E . n 
I 1 396 GLY 396 396 396 GLY GLY E . n 
I 1 397 MET 397 397 397 MET MET E . n 
I 1 398 PHE 398 398 398 PHE PHE E . n 
I 1 399 HIS 399 399 399 HIS HIS E . n 
I 1 400 PHE 400 400 400 PHE PHE E . n 
I 1 401 GLY 401 401 401 GLY GLY E . n 
I 1 402 GLY 402 402 402 GLY GLY E . n 
J 2 1   SER 1   404 404 SER SER F . n 
J 2 2   PHE 2   405 405 PHE PHE F . n 
J 2 3   ALA 3   406 406 ALA ALA F . n 
J 2 4   LEU 4   407 407 LEU LEU F . n 
J 2 5   GLY 5   408 408 GLY GLY F . n 
J 2 6   LEU 6   409 409 LEU LEU F . n 
J 2 7   ARG 7   410 410 ARG ARG F . n 
J 2 8   LYS 8   411 411 LYS LYS F . n 
J 2 9   ASP 9   412 412 ASP ASP F . n 
J 2 10  CYS 10  413 413 CYS CYS F . n 
J 2 11  ARG 11  414 414 ARG ARG F . n 
J 2 12  ALA 12  415 415 ALA ALA F . n 
J 2 13  GLU 13  416 416 GLU GLU F . n 
J 2 14  ILE 14  417 417 ILE ILE F . n 
J 2 15  VAL 15  418 418 VAL VAL F . n 
J 2 16  GLU 16  419 419 GLU GLU F . n 
J 2 17  LYS 17  420 420 LYS LYS F . n 
J 2 18  PHE 18  421 421 PHE PHE F . n 
J 2 19  THR 19  422 422 THR THR F . n 
J 2 20  GLU 20  423 423 GLU GLU F . n 
J 2 21  PRO 21  424 424 PRO PRO F . n 
J 2 22  GLY 22  425 425 GLY GLY F . n 
J 2 23  THR 23  426 426 THR THR F . n 
J 2 24  VAL 24  427 427 VAL VAL F . n 
J 2 25  ILE 25  428 428 ILE ILE F . n 
J 2 26  ARG 26  429 429 ARG ARG F . n 
J 2 27  ILE 27  430 430 ILE ILE F . n 
J 2 28  ASN 28  431 431 ASN ASN F . n 
J 2 29  GLU 29  432 432 GLU GLU F . n 
J 2 30  VAL 30  433 433 VAL VAL F . n 
J 2 31  VAL 31  434 434 VAL VAL F . n 
J 2 32  ALA 32  435 435 ALA ALA F . n 
J 2 33  ALA 33  436 436 ALA ALA F . n 
J 2 34  LEU 34  437 437 LEU LEU F . n 
J 2 35  LYS 35  438 ?   ?   ?   F . n 
J 2 36  ALA 36  439 ?   ?   ?   F . n 
K 1 1   MET 1   1   ?   ?   ?   K . n 
K 1 2   GLN 2   2   ?   ?   ?   K . n 
K 1 3   VAL 3   3   ?   ?   ?   K . n 
K 1 4   ILE 4   4   ?   ?   ?   K . n 
K 1 5   PRO 5   5   ?   ?   ?   K . n 
K 1 6   ALA 6   6   ?   ?   ?   K . n 
K 1 7   CYS 7   7   ?   ?   ?   K . n 
K 1 8   ASN 8   8   ?   ?   ?   K . n 
K 1 9   SER 9   9   ?   ?   ?   K . n 
K 1 10  ALA 10  10  ?   ?   ?   K . n 
K 1 11  ALA 11  11  ?   ?   ?   K . n 
K 1 12  ILE 12  12  ?   ?   ?   K . n 
K 1 13  ARG 13  13  ?   ?   ?   K . n 
K 1 14  SER 14  14  ?   ?   ?   K . n 
K 1 15  LEU 15  15  ?   ?   ?   K . n 
K 1 16  CYS 16  16  ?   ?   ?   K . n 
K 1 17  PRO 17  17  ?   ?   ?   K . n 
K 1 18  THR 18  18  ?   ?   ?   K . n 
K 1 19  PRO 19  19  ?   ?   ?   K . n 
K 1 20  GLU 20  20  ?   ?   ?   K . n 
K 1 21  SER 21  21  ?   ?   ?   K . n 
K 1 22  PHE 22  22  ?   ?   ?   K . n 
K 1 23  ARG 23  23  ?   ?   ?   K . n 
K 1 24  ASN 24  24  ?   ?   ?   K . n 
K 1 25  MET 25  25  ?   ?   ?   K . n 
K 1 26  GLY 26  26  ?   ?   ?   K . n 
K 1 27  TRP 27  27  ?   ?   ?   K . n 
K 1 28  LEU 28  28  ?   ?   ?   K . n 
K 1 29  SER 29  29  ?   ?   ?   K . n 
K 1 30  VAL 30  30  ?   ?   ?   K . n 
K 1 31  SER 31  31  ?   ?   ?   K . n 
K 1 32  ASP 32  32  ?   ?   ?   K . n 
K 1 33  ALA 33  33  ?   ?   ?   K . n 
K 1 34  VAL 34  34  ?   ?   ?   K . n 
K 1 35  TYR 35  35  ?   ?   ?   K . n 
K 1 36  SER 36  36  ?   ?   ?   K . n 
K 1 37  GLU 37  37  ?   ?   ?   K . n 
K 1 38  PHE 38  38  ?   ?   ?   K . n 
K 1 39  ILE 39  39  ?   ?   ?   K . n 
K 1 40  GLY 40  40  ?   ?   ?   K . n 
K 1 41  GLU 41  41  ?   ?   ?   K . n 
K 1 42  LEU 42  42  ?   ?   ?   K . n 
K 1 43  ALA 43  43  ?   ?   ?   K . n 
K 1 44  THR 44  44  ?   ?   ?   K . n 
K 1 45  ARG 45  45  ?   ?   ?   K . n 
K 1 46  ALA 46  46  ?   ?   ?   K . n 
K 1 47  SER 47  47  ?   ?   ?   K . n 
K 1 48  ASN 48  48  ?   ?   ?   K . n 
K 1 49  ARG 49  49  ?   ?   ?   K . n 
K 1 50  ASN 50  50  ?   ?   ?   K . n 
K 1 51  TYR 51  51  ?   ?   ?   K . n 
K 1 52  SER 52  52  ?   ?   ?   K . n 
K 1 53  ASN 53  53  ?   ?   ?   K . n 
K 1 54  GLU 54  54  ?   ?   ?   K . n 
K 1 55  PHE 55  55  ?   ?   ?   K . n 
K 1 56  GLY 56  56  56  GLY GLY K . n 
K 1 57  LEU 57  57  57  LEU LEU K . n 
K 1 58  MET 58  58  58  MET MET K . n 
K 1 59  GLN 59  59  59  GLN GLN K . n 
K 1 60  PRO 60  60  60  PRO PRO K . n 
K 1 61  ILE 61  61  61  ILE ILE K . n 
K 1 62  GLN 62  62  62  GLN GLN K . n 
K 1 63  GLU 63  63  63  GLU GLU K . n 
K 1 64  PHE 64  64  64  PHE PHE K . n 
K 1 65  LYS 65  65  65  LYS LYS K . n 
K 1 66  ALA 66  66  66  ALA ALA K . n 
K 1 67  PHE 67  67  67  PHE PHE K . n 
K 1 68  ILE 68  68  68  ILE ILE K . n 
K 1 69  GLU 69  69  69  GLU GLU K . n 
K 1 70  SER 70  70  70  SER SER K . n 
K 1 71  ASP 71  71  71  ASP ASP K . n 
K 1 72  PRO 72  72  72  PRO PRO K . n 
K 1 73  VAL 73  73  73  VAL VAL K . n 
K 1 74  VAL 74  74  74  VAL VAL K . n 
K 1 75  HIS 75  75  75  HIS HIS K . n 
K 1 76  GLN 76  76  76  GLN GLN K . n 
K 1 77  GLU 77  77  77  GLU GLU K . n 
K 1 78  PHE 78  78  78  PHE PHE K . n 
K 1 79  ILE 79  79  79  ILE ILE K . n 
K 1 80  ASP 80  80  80  ASP ASP K . n 
K 1 81  MET 81  81  81  MET MET K . n 
K 1 82  PHE 82  82  82  PHE PHE K . n 
K 1 83  GLU 83  83  83  GLU GLU K . n 
K 1 84  GLY 84  84  84  GLY GLY K . n 
K 1 85  ILE 85  85  85  ILE ILE K . n 
K 1 86  GLN 86  86  86  GLN GLN K . n 
K 1 87  ASP 87  87  87  ASP ASP K . n 
K 1 88  SER 88  88  88  SER SER K . n 
K 1 89  PRO 89  89  89  PRO PRO K . n 
K 1 90  ARG 90  90  90  ARG ARG K . n 
K 1 91  ASN 91  91  91  ASN ASN K . n 
K 1 92  TYR 92  92  92  TYR TYR K . n 
K 1 93  GLN 93  93  93  GLN GLN K . n 
K 1 94  GLU 94  94  94  GLU GLU K . n 
K 1 95  LEU 95  95  95  LEU LEU K . n 
K 1 96  CYS 96  96  96  CYS CYS K . n 
K 1 97  ASN 97  97  97  ASN ASN K . n 
K 1 98  MET 98  98  98  MET MET K . n 
K 1 99  PHE 99  99  99  PHE PHE K . n 
K 1 100 ASN 100 100 100 ASN ASN K . n 
K 1 101 ASP 101 101 101 ASP ASP K . n 
K 1 102 ILE 102 102 102 ILE ILE K . n 
K 1 103 PHE 103 103 103 PHE PHE K . n 
K 1 104 ARG 104 104 104 ARG ARG K . n 
K 1 105 LYS 105 105 105 LYS LYS K . n 
K 1 106 ALA 106 106 106 ALA ALA K . n 
K 1 107 PRO 107 107 107 PRO PRO K . n 
K 1 108 VAL 108 108 108 VAL VAL K . n 
K 1 109 TYR 109 109 109 TYR TYR K . n 
K 1 110 GLY 110 110 110 GLY GLY K . n 
K 1 111 ASP 111 111 111 ASP ASP K . n 
K 1 112 LEU 112 112 112 LEU LEU K . n 
K 1 113 GLY 113 113 113 GLY GLY K . n 
K 1 114 PRO 114 114 114 PRO PRO K . n 
K 1 115 PRO 115 115 115 PRO PRO K . n 
K 1 116 VAL 116 116 116 VAL VAL K . n 
K 1 117 TYR 117 117 117 TYR TYR K . n 
K 1 118 MET 118 118 118 MET MET K . n 
K 1 119 ILE 119 119 119 ILE ILE K . n 
K 1 120 MET 120 120 120 MET MET K . n 
K 1 121 ALA 121 121 121 ALA ALA K . n 
K 1 122 LYS 122 122 122 LYS LYS K . n 
K 1 123 LEU 123 123 123 LEU LEU K . n 
K 1 124 MET 124 124 124 MET MET K . n 
K 1 125 ASN 125 125 125 ASN ASN K . n 
K 1 126 THR 126 126 126 THR THR K . n 
K 1 127 ARG 127 127 127 ARG ARG K . n 
K 1 128 ALA 128 128 128 ALA ALA K . n 
K 1 129 GLY 129 129 129 GLY GLY K . n 
K 1 130 PHE 130 130 130 PHE PHE K . n 
K 1 131 SER 131 131 131 SER SER K . n 
K 1 132 ALA 132 132 132 ALA ALA K . n 
K 1 133 PHE 133 133 133 PHE PHE K . n 
K 1 134 THR 134 134 134 THR THR K . n 
K 1 135 ARG 135 135 135 ARG ARG K . n 
K 1 136 GLN 136 136 136 GLN GLN K . n 
K 1 137 ARG 137 137 137 ARG ARG K . n 
K 1 138 LEU 138 138 138 LEU LEU K . n 
K 1 139 ASN 139 139 139 ASN ASN K . n 
K 1 140 LEU 140 140 140 LEU LEU K . n 
K 1 141 HIS 141 141 141 HIS HIS K . n 
K 1 142 PHE 142 142 142 PHE PHE K . n 
K 1 143 LYS 143 143 143 LYS LYS K . n 
K 1 144 LYS 144 144 144 LYS LYS K . n 
K 1 145 LEU 145 145 145 LEU LEU K . n 
K 1 146 PHE 146 146 146 PHE PHE K . n 
K 1 147 ASP 147 147 147 ASP ASP K . n 
K 1 148 THR 148 148 148 THR THR K . n 
K 1 149 TRP 149 149 149 TRP TRP K . n 
K 1 150 GLY 150 150 150 GLY GLY K . n 
K 1 151 LEU 151 151 151 LEU LEU K . n 
K 1 152 PHE 152 152 152 PHE PHE K . n 
K 1 153 LEU 153 153 153 LEU LEU K . n 
K 1 154 SER 154 154 154 SER SER K . n 
K 1 155 SER 155 155 155 SER SER K . n 
K 1 156 LYS 156 156 156 LYS LYS K . n 
K 1 157 ASP 157 157 157 ASP ASP K . n 
K 1 158 SER 158 158 158 SER SER K . n 
K 1 159 ARG 159 159 159 ARG ARG K . n 
K 1 160 ASN 160 160 160 ASN ASN K . n 
K 1 161 VAL 161 161 161 VAL VAL K . n 
K 1 162 LEU 162 162 162 LEU LEU K . n 
K 1 163 VAL 163 163 163 VAL VAL K . n 
K 1 164 ALA 164 164 164 ALA ALA K . n 
K 1 165 ASP 165 165 165 ASP ASP K . n 
K 1 166 GLN 166 166 166 GLN GLN K . n 
K 1 167 PHE 167 167 167 PHE PHE K . n 
K 1 168 ASP 168 168 168 ASP ASP K . n 
K 1 169 ASP 169 169 169 ASP ASP K . n 
K 1 170 ARG 170 170 170 ARG ARG K . n 
K 1 171 HIS 171 171 171 HIS HIS K . n 
K 1 172 CYS 172 172 172 CYS CYS K . n 
K 1 173 GLY 173 173 173 GLY GLY K . n 
K 1 174 TRP 174 174 174 TRP TRP K . n 
K 1 175 LEU 175 175 175 LEU LEU K . n 
K 1 176 ASN 176 176 176 ASN ASN K . n 
K 1 177 GLU 177 177 177 GLU GLU K . n 
K 1 178 ARG 178 178 178 ARG ARG K . n 
K 1 179 ALA 179 179 179 ALA ALA K . n 
K 1 180 LEU 180 180 180 LEU LEU K . n 
K 1 181 SER 181 181 181 SER SER K . n 
K 1 182 ALA 182 182 182 ALA ALA K . n 
K 1 183 MET 183 183 183 MET MET K . n 
K 1 184 VAL 184 184 184 VAL VAL K . n 
K 1 185 LYS 185 185 185 LYS LYS K . n 
K 1 186 HIS 186 186 186 HIS HIS K . n 
K 1 187 TYR 187 187 187 TYR TYR K . n 
K 1 188 ASN 188 188 188 ASN ASN K . n 
K 1 189 GLY 189 189 189 GLY GLY K . n 
K 1 190 ARG 190 190 190 ARG ARG K . n 
K 1 191 ALA 191 191 191 ALA ALA K . n 
K 1 192 PHE 192 192 192 PHE PHE K . n 
K 1 193 ASP 193 193 193 ASP ASP K . n 
K 1 194 GLU 194 194 194 GLU GLU K . n 
K 1 195 VAL 195 195 195 VAL VAL K . n 
K 1 196 PHE 196 196 196 PHE PHE K . n 
K 1 197 LEU 197 197 197 LEU LEU K . n 
K 1 198 CYS 198 198 198 CYS CYS K . n 
K 1 199 ASP 199 199 199 ASP ASP K . n 
K 1 200 LYS 200 200 200 LYS LYS K . n 
K 1 201 ASN 201 201 201 ASN ASN K . n 
K 1 202 ALA 202 202 202 ALA ALA K . n 
K 1 203 PRO 203 203 203 PRO PRO K . n 
K 1 204 TYR 204 204 204 TYR TYR K . n 
K 1 205 TYR 205 205 205 TYR TYR K . n 
K 1 206 GLY 206 206 206 GLY GLY K . n 
K 1 207 PHE 207 207 207 PHE PHE K . n 
K 1 208 ASN 208 208 208 ASN ASN K . n 
K 1 209 SER 209 209 209 SER SER K . n 
K 1 210 TYR 210 210 210 TYR TYR K . n 
K 1 211 ASP 211 211 211 ASP ASP K . n 
K 1 212 ASP 212 212 212 ASP ASP K . n 
K 1 213 PHE 213 213 213 PHE PHE K . n 
K 1 214 PHE 214 214 214 PHE PHE K . n 
K 1 215 ASN 215 215 215 ASN ASN K . n 
K 1 216 ARG 216 216 216 ARG ARG K . n 
K 1 217 ARG 217 217 217 ARG ARG K . n 
K 1 218 PHE 218 218 218 PHE PHE K . n 
K 1 219 ARG 219 219 219 ARG ARG K . n 
K 1 220 ASN 220 220 220 ASN ASN K . n 
K 1 221 ARG 221 221 221 ARG ARG K . n 
K 1 222 ASP 222 222 222 ASP ASP K . n 
K 1 223 ILE 223 223 223 ILE ILE K . n 
K 1 224 ASP 224 224 224 ASP ASP K . n 
K 1 225 ARG 225 225 225 ARG ARG K . n 
K 1 226 PRO 226 226 226 PRO PRO K . n 
K 1 227 VAL 227 227 227 VAL VAL K . n 
K 1 228 VAL 228 228 228 VAL VAL K . n 
K 1 229 GLY 229 229 229 GLY GLY K . n 
K 1 230 GLY 230 230 230 GLY GLY K . n 
K 1 231 VAL 231 231 231 VAL VAL K . n 
K 1 232 ASN 232 232 232 ASN ASN K . n 
K 1 233 ASN 233 233 233 ASN ASN K . n 
K 1 234 THR 234 234 234 THR THR K . n 
K 1 235 THR 235 235 235 THR THR K . n 
K 1 236 LEU 236 236 236 LEU LEU K . n 
K 1 237 ILE 237 237 237 ILE ILE K . n 
K 1 238 SER 238 238 238 SER SER K . n 
K 1 239 ALA 239 239 239 ALA ALA K . n 
K 1 240 ALA 240 240 240 ALA ALA K . n 
K 1 241 CYS 241 241 241 CYS CYS K . n 
K 1 242 GLU 242 242 242 GLU GLU K . n 
K 1 243 SER 243 243 243 SER SER K . n 
K 1 244 LEU 244 244 244 LEU LEU K . n 
K 1 245 SER 245 245 245 SER SER K . n 
K 1 246 TYR 246 246 246 TYR TYR K . n 
K 1 247 ASN 247 247 247 ASN ASN K . n 
K 1 248 VAL 248 248 248 VAL VAL K . n 
K 1 249 SER 249 249 249 SER SER K . n 
K 1 250 TYR 250 250 250 TYR TYR K . n 
K 1 251 ASP 251 251 251 ASP ASP K . n 
K 1 252 VAL 252 252 252 VAL VAL K . n 
K 1 253 GLN 253 253 253 GLN GLN K . n 
K 1 254 SER 254 254 254 SER SER K . n 
K 1 255 LEU 255 255 255 LEU LEU K . n 
K 1 256 ASP 256 256 256 ASP ASP K . n 
K 1 257 THR 257 257 257 THR THR K . n 
K 1 258 LEU 258 258 258 LEU LEU K . n 
K 1 259 VAL 259 259 259 VAL VAL K . n 
K 1 260 PHE 260 260 260 PHE PHE K . n 
K 1 261 LYS 261 261 261 LYS LYS K . n 
K 1 262 GLY 262 262 262 GLY GLY K . n 
K 1 263 GLU 263 263 263 GLU GLU K . n 
K 1 264 THR 264 264 264 THR THR K . n 
K 1 265 TYR 265 265 265 TYR TYR K . n 
K 1 266 SER 266 266 266 SER SER K . n 
K 1 267 LEU 267 267 267 LEU LEU K . n 
K 1 268 LYS 268 268 268 LYS LYS K . n 
K 1 269 HIS 269 269 269 HIS HIS K . n 
K 1 270 LEU 270 270 270 LEU LEU K . n 
K 1 271 LEU 271 271 271 LEU LEU K . n 
K 1 272 ASN 272 272 272 ASN ASN K . n 
K 1 273 ASN 273 273 273 ASN ASN K . n 
K 1 274 ASP 274 274 274 ASP ASP K . n 
K 1 275 PRO 275 275 275 PRO PRO K . n 
K 1 276 PHE 276 276 276 PHE PHE K . n 
K 1 277 THR 277 277 277 THR THR K . n 
K 1 278 PRO 278 278 278 PRO PRO K . n 
K 1 279 GLN 279 279 279 GLN GLN K . n 
K 1 280 PHE 280 280 280 PHE PHE K . n 
K 1 281 GLU 281 281 281 GLU GLU K . n 
K 1 282 HIS 282 282 282 HIS HIS K . n 
K 1 283 GLY 283 283 283 GLY GLY K . n 
K 1 284 SER 284 284 284 SER SER K . n 
K 1 285 ILE 285 285 285 ILE ILE K . n 
K 1 286 LEU 286 286 286 LEU LEU K . n 
K 1 287 GLN 287 287 287 GLN GLN K . n 
K 1 288 GLY 288 288 288 GLY GLY K . n 
K 1 289 PHE 289 289 289 PHE PHE K . n 
K 1 290 LEU 290 290 290 LEU LEU K . n 
K 1 291 ASN 291 291 291 ASN ASN K . n 
K 1 292 VAL 292 292 292 VAL VAL K . n 
K 1 293 THR 293 293 293 THR THR K . n 
K 1 294 ALA 294 294 294 ALA ALA K . n 
K 1 295 TYR 295 295 295 TYR TYR K . n 
K 1 296 HIS 296 296 296 HIS HIS K . n 
K 1 297 ARG 297 297 297 ARG ARG K . n 
K 1 298 TRP 298 298 298 TRP TRP K . n 
K 1 299 HIS 299 299 299 HIS HIS K . n 
K 1 300 ALA 300 300 300 ALA ALA K . n 
K 1 301 PRO 301 301 301 PRO PRO K . n 
K 1 302 VAL 302 302 302 VAL VAL K . n 
K 1 303 ASN 303 303 303 ASN ASN K . n 
K 1 304 GLY 304 304 304 GLY GLY K . n 
K 1 305 THR 305 305 305 THR THR K . n 
K 1 306 ILE 306 306 306 ILE ILE K . n 
K 1 307 VAL 307 307 307 VAL VAL K . n 
K 1 308 LYS 308 308 308 LYS LYS K . n 
K 1 309 ILE 309 309 309 ILE ILE K . n 
K 1 310 ILE 310 310 310 ILE ILE K . n 
K 1 311 ASN 311 311 311 ASN ASN K . n 
K 1 312 VAL 312 312 312 VAL VAL K . n 
K 1 313 PRO 313 313 313 PRO PRO K . n 
K 1 314 GLY 314 314 314 GLY GLY K . n 
K 1 315 THR 315 315 315 THR THR K . n 
K 1 316 TYR 316 316 316 TYR TYR K . n 
K 1 317 PHE 317 317 317 PHE PHE K . n 
K 1 318 ALA 318 318 318 ALA ALA K . n 
K 1 319 GLN 319 319 319 GLN GLN K . n 
K 1 320 ALA 320 320 320 ALA ALA K . n 
K 1 321 PRO 321 321 321 PRO PRO K . n 
K 1 322 SER 322 322 322 SER SER K . n 
K 1 323 THR 323 323 323 THR THR K . n 
K 1 324 ILE 324 324 324 ILE ILE K . n 
K 1 325 GLY 325 325 325 GLY GLY K . n 
K 1 326 ASP 326 326 326 ASP ASP K . n 
K 1 327 PRO 327 327 327 PRO PRO K . n 
K 1 328 ILE 328 328 328 ILE ILE K . n 
K 1 329 PRO 329 329 329 PRO PRO K . n 
K 1 330 ASP 330 330 330 ASP ASP K . n 
K 1 331 ASN 331 331 331 ASN ASN K . n 
K 1 332 ASP 332 332 332 ASP ASP K . n 
K 1 333 TYR 333 333 333 TYR TYR K . n 
K 1 334 ASP 334 334 334 ASP ASP K . n 
K 1 335 PRO 335 335 335 PRO PRO K . n 
K 1 336 PRO 336 336 336 PRO PRO K . n 
K 1 337 PRO 337 337 337 PRO PRO K . n 
K 1 338 TYR 338 338 338 TYR TYR K . n 
K 1 339 LEU 339 339 339 LEU LEU K . n 
K 1 340 LYS 340 340 340 LYS LYS K . n 
K 1 341 SER 341 341 341 SER SER K . n 
K 1 342 LEU 342 342 342 LEU LEU K . n 
K 1 343 VAL 343 343 343 VAL VAL K . n 
K 1 344 TYR 344 344 344 TYR TYR K . n 
K 1 345 PHE 345 345 345 PHE PHE K . n 
K 1 346 SER 346 346 346 SER SER K . n 
K 1 347 ASN 347 347 347 ASN ASN K . n 
K 1 348 ILE 348 348 348 ILE ILE K . n 
K 1 349 ALA 349 349 349 ALA ALA K . n 
K 1 350 ALA 350 350 350 ALA ALA K . n 
K 1 351 ARG 351 351 351 ARG ARG K . n 
K 1 352 GLN 352 352 352 GLN GLN K . n 
K 1 353 ILE 353 353 353 ILE ILE K . n 
K 1 354 MET 354 354 354 MET MET K . n 
K 1 355 PHE 355 355 355 PHE PHE K . n 
K 1 356 ILE 356 356 356 ILE ILE K . n 
K 1 357 GLU 357 357 357 GLU GLU K . n 
K 1 358 ALA 358 358 358 ALA ALA K . n 
K 1 359 ASP 359 359 359 ASP ASP K . n 
K 1 360 ASN 360 360 360 ASN ASN K . n 
K 1 361 LYS 361 361 361 LYS LYS K . n 
K 1 362 GLU 362 362 362 GLU GLU K . n 
K 1 363 ILE 363 363 363 ILE ILE K . n 
K 1 364 GLY 364 364 364 GLY GLY K . n 
K 1 365 LEU 365 365 365 LEU LEU K . n 
K 1 366 ILE 366 366 366 ILE ILE K . n 
K 1 367 PHE 367 367 367 PHE PHE K . n 
K 1 368 LEU 368 368 368 LEU LEU K . n 
K 1 369 VAL 369 369 369 VAL VAL K . n 
K 1 370 PHE 370 370 370 PHE PHE K . n 
K 1 371 ILE 371 371 371 ILE ILE K . n 
K 1 372 GLY 372 372 372 GLY GLY K . n 
K 1 373 MET 373 373 373 MET MET K . n 
K 1 374 THR 374 374 374 THR THR K . n 
K 1 375 GLU 375 375 375 GLU GLU K . n 
K 1 376 ILE 376 376 376 ILE ILE K . n 
K 1 377 SER 377 377 377 SER SER K . n 
K 1 378 THR 378 378 378 THR THR K . n 
K 1 379 CYS 379 379 379 CYS CYS K . n 
K 1 380 GLU 380 380 380 GLU GLU K . n 
K 1 381 ALA 381 381 381 ALA ALA K . n 
K 1 382 THR 382 382 382 THR THR K . n 
K 1 383 VAL 383 383 383 VAL VAL K . n 
K 1 384 SER 384 384 384 SER SER K . n 
K 1 385 GLU 385 385 385 GLU GLU K . n 
K 1 386 GLY 386 386 386 GLY GLY K . n 
K 1 387 GLN 387 387 387 GLN GLN K . n 
K 1 388 HIS 388 388 388 HIS HIS K . n 
K 1 389 VAL 389 389 389 VAL VAL K . n 
K 1 390 ASN 390 390 390 ASN ASN K . n 
K 1 391 ARG 391 391 391 ARG ARG K . n 
K 1 392 GLY 392 392 392 GLY GLY K . n 
K 1 393 ASP 393 393 393 ASP ASP K . n 
K 1 394 ASP 394 394 394 ASP ASP K . n 
K 1 395 LEU 395 395 395 LEU LEU K . n 
K 1 396 GLY 396 396 396 GLY GLY K . n 
K 1 397 MET 397 397 397 MET MET K . n 
K 1 398 PHE 398 398 398 PHE PHE K . n 
K 1 399 HIS 399 399 399 HIS HIS K . n 
K 1 400 PHE 400 400 400 PHE PHE K . n 
K 1 401 GLY 401 401 401 GLY GLY K . n 
K 1 402 GLY 402 402 402 GLY GLY K . n 
L 2 1   SER 1   404 404 SER SER L . n 
L 2 2   PHE 2   405 405 PHE PHE L . n 
L 2 3   ALA 3   406 406 ALA ALA L . n 
L 2 4   LEU 4   407 407 LEU LEU L . n 
L 2 5   GLY 5   408 408 GLY GLY L . n 
L 2 6   LEU 6   409 409 LEU LEU L . n 
L 2 7   ARG 7   410 410 ARG ARG L . n 
L 2 8   LYS 8   411 411 LYS LYS L . n 
L 2 9   ASP 9   412 412 ASP ASP L . n 
L 2 10  CYS 10  413 413 CYS CYS L . n 
L 2 11  ARG 11  414 414 ARG ARG L . n 
L 2 12  ALA 12  415 415 ALA ALA L . n 
L 2 13  GLU 13  416 416 GLU GLU L . n 
L 2 14  ILE 14  417 417 ILE ILE L . n 
L 2 15  VAL 15  418 418 VAL VAL L . n 
L 2 16  GLU 16  419 419 GLU GLU L . n 
L 2 17  LYS 17  420 420 LYS LYS L . n 
L 2 18  PHE 18  421 421 PHE PHE L . n 
L 2 19  THR 19  422 422 THR THR L . n 
L 2 20  GLU 20  423 423 GLU GLU L . n 
L 2 21  PRO 21  424 424 PRO PRO L . n 
L 2 22  GLY 22  425 425 GLY GLY L . n 
L 2 23  THR 23  426 426 THR THR L . n 
L 2 24  VAL 24  427 427 VAL VAL L . n 
L 2 25  ILE 25  428 428 ILE ILE L . n 
L 2 26  ARG 26  429 429 ARG ARG L . n 
L 2 27  ILE 27  430 430 ILE ILE L . n 
L 2 28  ASN 28  431 431 ASN ASN L . n 
L 2 29  GLU 29  432 432 GLU GLU L . n 
L 2 30  VAL 30  433 433 VAL VAL L . n 
L 2 31  VAL 31  434 434 VAL VAL L . n 
L 2 32  ALA 32  435 435 ALA ALA L . n 
L 2 33  ALA 33  436 436 ALA ALA L . n 
L 2 34  LEU 34  437 437 LEU LEU L . n 
L 2 35  LYS 35  438 ?   ?   ?   L . n 
L 2 36  ALA 36  439 ?   ?   ?   L . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1LWG 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1LWG 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
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 
M  3 A1LWG 1  501 403  A1LWG PVL J . 
N  3 A1LWG 1  501 403  A1LWG PVL H . 
O  3 A1LWG 1  501 403  A1LWG PVL B . 
P  3 A1LWG 1  501 403  A1LWG PVL D . 
Q  3 A1LWG 1  501 403  A1LWG PVL F . 
R  3 A1LWG 1  501 403  A1LWG PVL L . 
S  4 HOH   1  501 1032 HOH   HOH I . 
S  4 HOH   2  502 210  HOH   HOH I . 
S  4 HOH   3  503 295  HOH   HOH I . 
S  4 HOH   4  504 1082 HOH   HOH I . 
S  4 HOH   5  505 161  HOH   HOH I . 
S  4 HOH   6  506 1124 HOH   HOH I . 
S  4 HOH   7  507 1771 HOH   HOH I . 
S  4 HOH   8  508 540  HOH   HOH I . 
S  4 HOH   9  509 658  HOH   HOH I . 
S  4 HOH   10 510 903  HOH   HOH I . 
S  4 HOH   11 511 1258 HOH   HOH I . 
S  4 HOH   12 512 199  HOH   HOH I . 
S  4 HOH   13 513 108  HOH   HOH I . 
S  4 HOH   14 514 1710 HOH   HOH I . 
S  4 HOH   15 515 825  HOH   HOH I . 
S  4 HOH   16 516 1243 HOH   HOH I . 
S  4 HOH   17 517 136  HOH   HOH I . 
S  4 HOH   18 518 419  HOH   HOH I . 
S  4 HOH   19 519 359  HOH   HOH I . 
S  4 HOH   20 520 251  HOH   HOH I . 
S  4 HOH   21 521 115  HOH   HOH I . 
S  4 HOH   22 522 80   HOH   HOH I . 
S  4 HOH   23 523 42   HOH   HOH I . 
S  4 HOH   24 524 297  HOH   HOH I . 
S  4 HOH   25 525 84   HOH   HOH I . 
S  4 HOH   26 526 351  HOH   HOH I . 
S  4 HOH   27 527 621  HOH   HOH I . 
S  4 HOH   28 528 207  HOH   HOH I . 
S  4 HOH   29 529 10   HOH   HOH I . 
S  4 HOH   30 530 23   HOH   HOH I . 
S  4 HOH   31 531 410  HOH   HOH I . 
S  4 HOH   32 532 18   HOH   HOH I . 
S  4 HOH   33 533 298  HOH   HOH I . 
S  4 HOH   34 534 1192 HOH   HOH I . 
S  4 HOH   35 535 31   HOH   HOH I . 
S  4 HOH   36 536 22   HOH   HOH I . 
S  4 HOH   37 537 282  HOH   HOH I . 
S  4 HOH   38 538 1380 HOH   HOH I . 
S  4 HOH   39 539 721  HOH   HOH I . 
S  4 HOH   40 540 1106 HOH   HOH I . 
S  4 HOH   41 541 148  HOH   HOH I . 
S  4 HOH   42 542 936  HOH   HOH I . 
S  4 HOH   43 543 369  HOH   HOH I . 
S  4 HOH   44 544 1520 HOH   HOH I . 
S  4 HOH   45 545 66   HOH   HOH I . 
S  4 HOH   46 546 1276 HOH   HOH I . 
S  4 HOH   47 547 55   HOH   HOH I . 
S  4 HOH   48 548 826  HOH   HOH I . 
S  4 HOH   49 549 312  HOH   HOH I . 
S  4 HOH   50 550 258  HOH   HOH I . 
S  4 HOH   51 551 315  HOH   HOH I . 
S  4 HOH   52 552 44   HOH   HOH I . 
S  4 HOH   53 553 413  HOH   HOH I . 
S  4 HOH   54 554 396  HOH   HOH I . 
S  4 HOH   55 555 24   HOH   HOH I . 
S  4 HOH   56 556 423  HOH   HOH I . 
S  4 HOH   57 557 1521 HOH   HOH I . 
S  4 HOH   58 558 1731 HOH   HOH I . 
S  4 HOH   59 559 1585 HOH   HOH I . 
S  4 HOH   60 560 301  HOH   HOH I . 
S  4 HOH   61 561 265  HOH   HOH I . 
S  4 HOH   62 562 507  HOH   HOH I . 
S  4 HOH   63 563 230  HOH   HOH I . 
S  4 HOH   64 564 317  HOH   HOH I . 
T  4 HOH   1  601 924  HOH   HOH J . 
T  4 HOH   2  602 814  HOH   HOH J . 
U  4 HOH   1  501 105  HOH   HOH G . 
U  4 HOH   2  502 103  HOH   HOH G . 
U  4 HOH   3  503 106  HOH   HOH G . 
U  4 HOH   4  504 96   HOH   HOH G . 
U  4 HOH   5  505 1303 HOH   HOH G . 
U  4 HOH   6  506 59   HOH   HOH G . 
U  4 HOH   7  507 7    HOH   HOH G . 
U  4 HOH   8  508 546  HOH   HOH G . 
U  4 HOH   9  509 116  HOH   HOH G . 
U  4 HOH   10 510 1144 HOH   HOH G . 
U  4 HOH   11 511 206  HOH   HOH G . 
U  4 HOH   12 512 146  HOH   HOH G . 
U  4 HOH   13 513 1189 HOH   HOH G . 
U  4 HOH   14 514 169  HOH   HOH G . 
U  4 HOH   15 515 208  HOH   HOH G . 
U  4 HOH   16 516 3    HOH   HOH G . 
U  4 HOH   17 517 254  HOH   HOH G . 
U  4 HOH   18 518 75   HOH   HOH G . 
U  4 HOH   19 519 6    HOH   HOH G . 
U  4 HOH   20 520 123  HOH   HOH G . 
U  4 HOH   21 521 1    HOH   HOH G . 
U  4 HOH   22 522 611  HOH   HOH G . 
U  4 HOH   23 523 16   HOH   HOH G . 
U  4 HOH   24 524 41   HOH   HOH G . 
U  4 HOH   25 525 237  HOH   HOH G . 
U  4 HOH   26 526 186  HOH   HOH G . 
U  4 HOH   27 527 28   HOH   HOH G . 
U  4 HOH   28 528 46   HOH   HOH G . 
U  4 HOH   29 529 125  HOH   HOH G . 
U  4 HOH   30 530 222  HOH   HOH G . 
U  4 HOH   31 531 51   HOH   HOH G . 
U  4 HOH   32 532 1262 HOH   HOH G . 
U  4 HOH   33 533 52   HOH   HOH G . 
U  4 HOH   34 534 89   HOH   HOH G . 
U  4 HOH   35 535 147  HOH   HOH G . 
U  4 HOH   36 536 138  HOH   HOH G . 
U  4 HOH   37 537 209  HOH   HOH G . 
U  4 HOH   38 538 1263 HOH   HOH G . 
U  4 HOH   39 539 461  HOH   HOH G . 
U  4 HOH   40 540 675  HOH   HOH G . 
U  4 HOH   41 541 399  HOH   HOH G . 
U  4 HOH   42 542 34   HOH   HOH G . 
U  4 HOH   43 543 1054 HOH   HOH G . 
U  4 HOH   44 544 97   HOH   HOH G . 
U  4 HOH   45 545 1690 HOH   HOH G . 
U  4 HOH   46 546 416  HOH   HOH G . 
U  4 HOH   47 547 426  HOH   HOH G . 
U  4 HOH   48 548 1055 HOH   HOH G . 
U  4 HOH   49 549 53   HOH   HOH G . 
U  4 HOH   50 550 470  HOH   HOH G . 
U  4 HOH   51 551 142  HOH   HOH G . 
U  4 HOH   52 552 535  HOH   HOH G . 
U  4 HOH   53 553 166  HOH   HOH G . 
U  4 HOH   54 554 92   HOH   HOH G . 
U  4 HOH   55 555 203  HOH   HOH G . 
U  4 HOH   56 556 204  HOH   HOH G . 
U  4 HOH   57 557 869  HOH   HOH G . 
U  4 HOH   58 558 292  HOH   HOH G . 
U  4 HOH   59 559 27   HOH   HOH G . 
U  4 HOH   60 560 1138 HOH   HOH G . 
U  4 HOH   61 561 824  HOH   HOH G . 
U  4 HOH   62 562 107  HOH   HOH G . 
U  4 HOH   63 563 451  HOH   HOH G . 
U  4 HOH   64 564 145  HOH   HOH G . 
U  4 HOH   65 565 1152 HOH   HOH G . 
U  4 HOH   66 566 70   HOH   HOH G . 
U  4 HOH   67 567 321  HOH   HOH G . 
U  4 HOH   68 568 304  HOH   HOH G . 
U  4 HOH   69 569 253  HOH   HOH G . 
U  4 HOH   70 570 1098 HOH   HOH G . 
U  4 HOH   71 571 109  HOH   HOH G . 
U  4 HOH   72 572 90   HOH   HOH G . 
U  4 HOH   73 573 1354 HOH   HOH G . 
U  4 HOH   74 574 307  HOH   HOH G . 
U  4 HOH   75 575 1087 HOH   HOH G . 
U  4 HOH   76 576 374  HOH   HOH G . 
U  4 HOH   77 577 788  HOH   HOH G . 
U  4 HOH   78 578 412  HOH   HOH G . 
U  4 HOH   79 579 296  HOH   HOH G . 
U  4 HOH   80 580 614  HOH   HOH G . 
U  4 HOH   81 581 1267 HOH   HOH G . 
U  4 HOH   82 582 131  HOH   HOH G . 
U  4 HOH   83 583 1051 HOH   HOH G . 
U  4 HOH   84 584 956  HOH   HOH G . 
U  4 HOH   85 585 160  HOH   HOH G . 
U  4 HOH   86 586 130  HOH   HOH G . 
U  4 HOH   87 587 35   HOH   HOH G . 
U  4 HOH   88 588 502  HOH   HOH G . 
U  4 HOH   89 589 428  HOH   HOH G . 
U  4 HOH   90 590 367  HOH   HOH G . 
U  4 HOH   91 591 198  HOH   HOH G . 
U  4 HOH   92 592 441  HOH   HOH G . 
U  4 HOH   93 593 310  HOH   HOH G . 
U  4 HOH   94 594 379  HOH   HOH G . 
U  4 HOH   95 595 120  HOH   HOH G . 
U  4 HOH   96 596 1334 HOH   HOH G . 
U  4 HOH   97 597 113  HOH   HOH G . 
U  4 HOH   98 598 140  HOH   HOH G . 
U  4 HOH   99 599 277  HOH   HOH G . 
V  4 HOH   1  601 1080 HOH   HOH H . 
V  4 HOH   2  602 698  HOH   HOH H . 
V  4 HOH   3  603 885  HOH   HOH H . 
V  4 HOH   4  604 1508 HOH   HOH H . 
V  4 HOH   5  605 453  HOH   HOH H . 
V  4 HOH   6  606 276  HOH   HOH H . 
V  4 HOH   7  607 418  HOH   HOH H . 
V  4 HOH   8  608 1156 HOH   HOH H . 
W  4 HOH   1  501 343  HOH   HOH A . 
W  4 HOH   2  502 668  HOH   HOH A . 
W  4 HOH   3  503 188  HOH   HOH A . 
W  4 HOH   4  504 288  HOH   HOH A . 
W  4 HOH   5  505 564  HOH   HOH A . 
W  4 HOH   6  506 663  HOH   HOH A . 
W  4 HOH   7  507 47   HOH   HOH A . 
W  4 HOH   8  508 79   HOH   HOH A . 
W  4 HOH   9  509 95   HOH   HOH A . 
W  4 HOH   10 510 300  HOH   HOH A . 
W  4 HOH   11 511 205  HOH   HOH A . 
W  4 HOH   12 512 2    HOH   HOH A . 
W  4 HOH   13 513 1069 HOH   HOH A . 
W  4 HOH   14 514 82   HOH   HOH A . 
W  4 HOH   15 515 252  HOH   HOH A . 
W  4 HOH   16 516 554  HOH   HOH A . 
W  4 HOH   17 517 607  HOH   HOH A . 
W  4 HOH   18 518 78   HOH   HOH A . 
W  4 HOH   19 519 1716 HOH   HOH A . 
W  4 HOH   20 520 190  HOH   HOH A . 
W  4 HOH   21 521 185  HOH   HOH A . 
W  4 HOH   22 522 132  HOH   HOH A . 
W  4 HOH   23 523 464  HOH   HOH A . 
W  4 HOH   24 524 29   HOH   HOH A . 
W  4 HOH   25 525 56   HOH   HOH A . 
W  4 HOH   26 526 305  HOH   HOH A . 
W  4 HOH   27 527 33   HOH   HOH A . 
W  4 HOH   28 528 50   HOH   HOH A . 
W  4 HOH   29 529 1665 HOH   HOH A . 
W  4 HOH   30 530 843  HOH   HOH A . 
W  4 HOH   31 531 1618 HOH   HOH A . 
W  4 HOH   32 532 71   HOH   HOH A . 
W  4 HOH   33 533 1045 HOH   HOH A . 
W  4 HOH   34 534 48   HOH   HOH A . 
W  4 HOH   35 535 213  HOH   HOH A . 
W  4 HOH   36 536 62   HOH   HOH A . 
W  4 HOH   37 537 641  HOH   HOH A . 
W  4 HOH   38 538 439  HOH   HOH A . 
W  4 HOH   39 539 1037 HOH   HOH A . 
W  4 HOH   40 540 281  HOH   HOH A . 
W  4 HOH   41 541 81   HOH   HOH A . 
W  4 HOH   42 542 54   HOH   HOH A . 
W  4 HOH   43 543 799  HOH   HOH A . 
W  4 HOH   44 544 196  HOH   HOH A . 
W  4 HOH   45 545 896  HOH   HOH A . 
W  4 HOH   46 546 223  HOH   HOH A . 
W  4 HOH   47 547 193  HOH   HOH A . 
W  4 HOH   48 548 19   HOH   HOH A . 
W  4 HOH   49 549 26   HOH   HOH A . 
W  4 HOH   50 550 1109 HOH   HOH A . 
W  4 HOH   51 551 818  HOH   HOH A . 
W  4 HOH   52 552 37   HOH   HOH A . 
W  4 HOH   53 553 469  HOH   HOH A . 
W  4 HOH   54 554 640  HOH   HOH A . 
W  4 HOH   55 555 157  HOH   HOH A . 
W  4 HOH   56 556 609  HOH   HOH A . 
W  4 HOH   57 557 1000 HOH   HOH A . 
W  4 HOH   58 558 112  HOH   HOH A . 
W  4 HOH   59 559 201  HOH   HOH A . 
W  4 HOH   60 560 1604 HOH   HOH A . 
W  4 HOH   61 561 978  HOH   HOH A . 
W  4 HOH   62 562 43   HOH   HOH A . 
W  4 HOH   63 563 98   HOH   HOH A . 
W  4 HOH   64 564 36   HOH   HOH A . 
W  4 HOH   65 565 1679 HOH   HOH A . 
W  4 HOH   66 566 118  HOH   HOH A . 
W  4 HOH   67 567 1402 HOH   HOH A . 
W  4 HOH   68 568 180  HOH   HOH A . 
W  4 HOH   69 569 907  HOH   HOH A . 
W  4 HOH   70 570 1378 HOH   HOH A . 
W  4 HOH   71 571 1272 HOH   HOH A . 
W  4 HOH   72 572 516  HOH   HOH A . 
W  4 HOH   73 573 179  HOH   HOH A . 
W  4 HOH   74 574 135  HOH   HOH A . 
W  4 HOH   75 575 1643 HOH   HOH A . 
W  4 HOH   76 576 358  HOH   HOH A . 
W  4 HOH   77 577 100  HOH   HOH A . 
W  4 HOH   78 578 328  HOH   HOH A . 
W  4 HOH   79 579 708  HOH   HOH A . 
W  4 HOH   80 580 181  HOH   HOH A . 
W  4 HOH   81 581 58   HOH   HOH A . 
W  4 HOH   82 582 1511 HOH   HOH A . 
W  4 HOH   83 583 680  HOH   HOH A . 
W  4 HOH   84 584 1588 HOH   HOH A . 
W  4 HOH   85 585 1387 HOH   HOH A . 
W  4 HOH   86 586 323  HOH   HOH A . 
W  4 HOH   87 587 340  HOH   HOH A . 
W  4 HOH   88 588 526  HOH   HOH A . 
W  4 HOH   89 589 673  HOH   HOH A . 
W  4 HOH   90 590 172  HOH   HOH A . 
X  4 HOH   1  601 731  HOH   HOH B . 
X  4 HOH   2  602 672  HOH   HOH B . 
X  4 HOH   3  603 782  HOH   HOH B . 
X  4 HOH   4  604 338  HOH   HOH B . 
X  4 HOH   5  605 458  HOH   HOH B . 
X  4 HOH   6  606 40   HOH   HOH B . 
X  4 HOH   7  607 491  HOH   HOH B . 
X  4 HOH   8  608 1076 HOH   HOH B . 
X  4 HOH   9  609 1517 HOH   HOH B . 
Y  4 HOH   1  501 692  HOH   HOH C . 
Y  4 HOH   2  502 560  HOH   HOH C . 
Y  4 HOH   3  503 348  HOH   HOH C . 
Y  4 HOH   4  504 121  HOH   HOH C . 
Y  4 HOH   5  505 368  HOH   HOH C . 
Y  4 HOH   6  506 261  HOH   HOH C . 
Y  4 HOH   7  507 474  HOH   HOH C . 
Y  4 HOH   8  508 1028 HOH   HOH C . 
Y  4 HOH   9  509 61   HOH   HOH C . 
Y  4 HOH   10 510 456  HOH   HOH C . 
Y  4 HOH   11 511 345  HOH   HOH C . 
Y  4 HOH   12 512 152  HOH   HOH C . 
Y  4 HOH   13 513 855  HOH   HOH C . 
Y  4 HOH   14 514 1073 HOH   HOH C . 
Y  4 HOH   15 515 239  HOH   HOH C . 
Y  4 HOH   16 516 164  HOH   HOH C . 
Y  4 HOH   17 517 1120 HOH   HOH C . 
Y  4 HOH   18 518 1154 HOH   HOH C . 
Y  4 HOH   19 519 57   HOH   HOH C . 
Y  4 HOH   20 520 15   HOH   HOH C . 
Y  4 HOH   21 521 12   HOH   HOH C . 
Y  4 HOH   22 522 1227 HOH   HOH C . 
Y  4 HOH   23 523 17   HOH   HOH C . 
Y  4 HOH   24 524 238  HOH   HOH C . 
Y  4 HOH   25 525 153  HOH   HOH C . 
Y  4 HOH   26 526 9    HOH   HOH C . 
Y  4 HOH   27 527 111  HOH   HOH C . 
Y  4 HOH   28 528 144  HOH   HOH C . 
Y  4 HOH   29 529 39   HOH   HOH C . 
Y  4 HOH   30 530 234  HOH   HOH C . 
Y  4 HOH   31 531 1280 HOH   HOH C . 
Y  4 HOH   32 532 49   HOH   HOH C . 
Y  4 HOH   33 533 347  HOH   HOH C . 
Y  4 HOH   34 534 506  HOH   HOH C . 
Y  4 HOH   35 535 218  HOH   HOH C . 
Y  4 HOH   36 536 421  HOH   HOH C . 
Y  4 HOH   37 537 394  HOH   HOH C . 
Y  4 HOH   38 538 143  HOH   HOH C . 
Y  4 HOH   39 539 30   HOH   HOH C . 
Y  4 HOH   40 540 76   HOH   HOH C . 
Y  4 HOH   41 541 162  HOH   HOH C . 
Y  4 HOH   42 542 1273 HOH   HOH C . 
Y  4 HOH   43 543 422  HOH   HOH C . 
Y  4 HOH   44 544 1822 HOH   HOH C . 
Y  4 HOH   45 545 69   HOH   HOH C . 
Y  4 HOH   46 546 408  HOH   HOH C . 
Y  4 HOH   47 547 1102 HOH   HOH C . 
Y  4 HOH   48 548 247  HOH   HOH C . 
Y  4 HOH   49 549 83   HOH   HOH C . 
Y  4 HOH   50 550 339  HOH   HOH C . 
Y  4 HOH   51 551 308  HOH   HOH C . 
Y  4 HOH   52 552 1582 HOH   HOH C . 
Y  4 HOH   53 553 637  HOH   HOH C . 
Y  4 HOH   54 554 573  HOH   HOH C . 
Y  4 HOH   55 555 1702 HOH   HOH C . 
Y  4 HOH   56 556 481  HOH   HOH C . 
Y  4 HOH   57 557 262  HOH   HOH C . 
Y  4 HOH   58 558 442  HOH   HOH C . 
Y  4 HOH   59 559 232  HOH   HOH C . 
Y  4 HOH   60 560 1501 HOH   HOH C . 
Y  4 HOH   61 561 1071 HOH   HOH C . 
Y  4 HOH   62 562 455  HOH   HOH C . 
Y  4 HOH   63 563 1136 HOH   HOH C . 
Y  4 HOH   64 564 1698 HOH   HOH C . 
Y  4 HOH   65 565 487  HOH   HOH C . 
Y  4 HOH   66 566 508  HOH   HOH C . 
Y  4 HOH   67 567 450  HOH   HOH C . 
Y  4 HOH   68 568 1268 HOH   HOH C . 
Y  4 HOH   69 569 884  HOH   HOH C . 
Y  4 HOH   70 570 1654 HOH   HOH C . 
Y  4 HOH   71 571 336  HOH   HOH C . 
Y  4 HOH   72 572 1169 HOH   HOH C . 
Y  4 HOH   73 573 1394 HOH   HOH C . 
Y  4 HOH   74 574 1481 HOH   HOH C . 
Z  4 HOH   1  601 466  HOH   HOH D . 
Z  4 HOH   2  602 406  HOH   HOH D . 
Z  4 HOH   3  603 74   HOH   HOH D . 
Z  4 HOH   4  604 14   HOH   HOH D . 
Z  4 HOH   5  605 128  HOH   HOH D . 
Z  4 HOH   6  606 1428 HOH   HOH D . 
Z  4 HOH   7  607 268  HOH   HOH D . 
Z  4 HOH   8  608 85   HOH   HOH D . 
Z  4 HOH   9  609 1374 HOH   HOH D . 
AA 4 HOH   1  501 212  HOH   HOH E . 
AA 4 HOH   2  502 1046 HOH   HOH E . 
AA 4 HOH   3  503 813  HOH   HOH E . 
AA 4 HOH   4  504 1686 HOH   HOH E . 
AA 4 HOH   5  505 363  HOH   HOH E . 
AA 4 HOH   6  506 241  HOH   HOH E . 
AA 4 HOH   7  507 1118 HOH   HOH E . 
AA 4 HOH   8  508 929  HOH   HOH E . 
AA 4 HOH   9  509 1328 HOH   HOH E . 
AA 4 HOH   10 510 63   HOH   HOH E . 
AA 4 HOH   11 511 659  HOH   HOH E . 
AA 4 HOH   12 512 352  HOH   HOH E . 
AA 4 HOH   13 513 1638 HOH   HOH E . 
AA 4 HOH   14 514 60   HOH   HOH E . 
AA 4 HOH   15 515 87   HOH   HOH E . 
AA 4 HOH   16 516 173  HOH   HOH E . 
AA 4 HOH   17 517 1526 HOH   HOH E . 
AA 4 HOH   18 518 271  HOH   HOH E . 
AA 4 HOH   19 519 1225 HOH   HOH E . 
AA 4 HOH   20 520 267  HOH   HOH E . 
AA 4 HOH   21 521 8    HOH   HOH E . 
AA 4 HOH   22 522 248  HOH   HOH E . 
AA 4 HOH   23 523 437  HOH   HOH E . 
AA 4 HOH   24 524 362  HOH   HOH E . 
AA 4 HOH   25 525 4    HOH   HOH E . 
AA 4 HOH   26 526 485  HOH   HOH E . 
AA 4 HOH   27 527 1238 HOH   HOH E . 
AA 4 HOH   28 528 353  HOH   HOH E . 
AA 4 HOH   29 529 961  HOH   HOH E . 
AA 4 HOH   30 530 216  HOH   HOH E . 
AA 4 HOH   31 531 1522 HOH   HOH E . 
AA 4 HOH   32 532 5    HOH   HOH E . 
AA 4 HOH   33 533 1533 HOH   HOH E . 
AA 4 HOH   34 534 195  HOH   HOH E . 
AA 4 HOH   35 535 341  HOH   HOH E . 
AA 4 HOH   36 536 319  HOH   HOH E . 
AA 4 HOH   37 537 467  HOH   HOH E . 
AA 4 HOH   38 538 159  HOH   HOH E . 
AA 4 HOH   39 539 617  HOH   HOH E . 
AA 4 HOH   40 540 425  HOH   HOH E . 
AA 4 HOH   41 541 126  HOH   HOH E . 
AA 4 HOH   42 542 275  HOH   HOH E . 
AA 4 HOH   43 543 357  HOH   HOH E . 
AA 4 HOH   44 544 1158 HOH   HOH E . 
AA 4 HOH   45 545 414  HOH   HOH E . 
AA 4 HOH   46 546 665  HOH   HOH E . 
AA 4 HOH   47 547 217  HOH   HOH E . 
AA 4 HOH   48 548 124  HOH   HOH E . 
AA 4 HOH   49 549 192  HOH   HOH E . 
AA 4 HOH   50 550 1064 HOH   HOH E . 
AA 4 HOH   51 551 344  HOH   HOH E . 
AA 4 HOH   52 552 167  HOH   HOH E . 
AA 4 HOH   53 553 385  HOH   HOH E . 
AA 4 HOH   54 554 273  HOH   HOH E . 
AA 4 HOH   55 555 274  HOH   HOH E . 
AA 4 HOH   56 556 1282 HOH   HOH E . 
AA 4 HOH   57 557 1074 HOH   HOH E . 
AA 4 HOH   58 558 225  HOH   HOH E . 
AA 4 HOH   59 559 1083 HOH   HOH E . 
AA 4 HOH   60 560 1383 HOH   HOH E . 
AA 4 HOH   61 561 723  HOH   HOH E . 
AA 4 HOH   62 562 170  HOH   HOH E . 
AA 4 HOH   63 563 1443 HOH   HOH E . 
AA 4 HOH   64 564 1175 HOH   HOH E . 
AA 4 HOH   65 565 266  HOH   HOH E . 
AA 4 HOH   66 566 245  HOH   HOH E . 
AA 4 HOH   67 567 1031 HOH   HOH E . 
AA 4 HOH   68 568 349  HOH   HOH E . 
AA 4 HOH   69 569 748  HOH   HOH E . 
AA 4 HOH   70 570 318  HOH   HOH E . 
AA 4 HOH   71 571 1425 HOH   HOH E . 
AA 4 HOH   72 572 867  HOH   HOH E . 
AA 4 HOH   73 573 1058 HOH   HOH E . 
BA 4 HOH   1  601 322  HOH   HOH F . 
BA 4 HOH   2  602 873  HOH   HOH F . 
BA 4 HOH   3  603 1424 HOH   HOH F . 
BA 4 HOH   4  604 151  HOH   HOH F . 
CA 4 HOH   1  501 1215 HOH   HOH K . 
CA 4 HOH   2  502 1030 HOH   HOH K . 
CA 4 HOH   3  503 1457 HOH   HOH K . 
CA 4 HOH   4  504 1130 HOH   HOH K . 
CA 4 HOH   5  505 789  HOH   HOH K . 
CA 4 HOH   6  506 586  HOH   HOH K . 
CA 4 HOH   7  507 1255 HOH   HOH K . 
CA 4 HOH   8  508 527  HOH   HOH K . 
CA 4 HOH   9  509 719  HOH   HOH K . 
CA 4 HOH   10 510 1461 HOH   HOH K . 
CA 4 HOH   11 511 38   HOH   HOH K . 
CA 4 HOH   12 512 475  HOH   HOH K . 
CA 4 HOH   13 513 364  HOH   HOH K . 
CA 4 HOH   14 514 178  HOH   HOH K . 
CA 4 HOH   15 515 543  HOH   HOH K . 
CA 4 HOH   16 516 411  HOH   HOH K . 
CA 4 HOH   17 517 623  HOH   HOH K . 
CA 4 HOH   18 518 350  HOH   HOH K . 
CA 4 HOH   19 519 682  HOH   HOH K . 
CA 4 HOH   20 520 13   HOH   HOH K . 
CA 4 HOH   21 521 1247 HOH   HOH K . 
CA 4 HOH   22 522 127  HOH   HOH K . 
CA 4 HOH   23 523 1241 HOH   HOH K . 
CA 4 HOH   24 524 837  HOH   HOH K . 
CA 4 HOH   25 525 720  HOH   HOH K . 
CA 4 HOH   26 526 337  HOH   HOH K . 
CA 4 HOH   27 527 284  HOH   HOH K . 
CA 4 HOH   28 528 688  HOH   HOH K . 
CA 4 HOH   29 529 1360 HOH   HOH K . 
CA 4 HOH   30 530 1594 HOH   HOH K . 
CA 4 HOH   31 531 68   HOH   HOH K . 
CA 4 HOH   32 532 1506 HOH   HOH K . 
CA 4 HOH   33 533 1758 HOH   HOH K . 
CA 4 HOH   34 534 1439 HOH   HOH K . 
DA 4 HOH   1  601 1184 HOH   HOH L . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1   1 Y 1 I GLU 83  ? CG  ? A GLU 83  CG  
2   1 Y 1 I GLU 83  ? CD  ? A GLU 83  CD  
3   1 Y 1 I GLU 83  ? OE1 ? A GLU 83  OE1 
4   1 Y 1 I GLU 83  ? OE2 ? A GLU 83  OE2 
5   1 Y 1 I GLN 86  ? CG  ? A GLN 86  CG  
6   1 Y 1 I GLN 86  ? CD  ? A GLN 86  CD  
7   1 Y 1 I GLN 86  ? OE1 ? A GLN 86  OE1 
8   1 Y 1 I GLN 86  ? NE2 ? A GLN 86  NE2 
9   1 Y 1 I ARG 90  ? CG  ? A ARG 90  CG  
10  1 Y 1 I ARG 90  ? CD  ? A ARG 90  CD  
11  1 Y 1 I ARG 90  ? NE  ? A ARG 90  NE  
12  1 Y 1 I ARG 90  ? CZ  ? A ARG 90  CZ  
13  1 Y 1 I ARG 90  ? NH1 ? A ARG 90  NH1 
14  1 Y 1 I ARG 90  ? NH2 ? A ARG 90  NH2 
15  1 Y 1 I LYS 122 ? CG  ? A LYS 122 CG  
16  1 Y 1 I LYS 122 ? CD  ? A LYS 122 CD  
17  1 Y 1 I LYS 122 ? CE  ? A LYS 122 CE  
18  1 Y 1 I LYS 122 ? NZ  ? A LYS 122 NZ  
19  1 Y 1 I LYS 156 ? CG  ? A LYS 156 CG  
20  1 Y 1 I LYS 156 ? CD  ? A LYS 156 CD  
21  1 Y 1 I LYS 156 ? CE  ? A LYS 156 CE  
22  1 Y 1 I LYS 156 ? NZ  ? A LYS 156 NZ  
23  1 Y 1 I ASP 169 ? CG  ? A ASP 169 CG  
24  1 Y 1 I ASP 169 ? OD1 ? A ASP 169 OD1 
25  1 Y 1 I ASP 169 ? OD2 ? A ASP 169 OD2 
26  1 Y 1 I ARG 170 ? CG  ? A ARG 170 CG  
27  1 Y 1 I ARG 170 ? CD  ? A ARG 170 CD  
28  1 Y 1 I ARG 170 ? NE  ? A ARG 170 NE  
29  1 Y 1 I ARG 170 ? CZ  ? A ARG 170 CZ  
30  1 Y 1 I ARG 170 ? NH1 ? A ARG 170 NH1 
31  1 Y 1 I ARG 170 ? NH2 ? A ARG 170 NH2 
32  1 Y 1 I GLU 177 ? CG  ? A GLU 177 CG  
33  1 Y 1 I GLU 177 ? CD  ? A GLU 177 CD  
34  1 Y 1 I GLU 177 ? OE1 ? A GLU 177 OE1 
35  1 Y 1 I GLU 177 ? OE2 ? A GLU 177 OE2 
36  1 Y 1 I ASP 330 ? CG  ? A ASP 330 CG  
37  1 Y 1 I ASP 330 ? OD1 ? A ASP 330 OD1 
38  1 Y 1 I ASP 330 ? OD2 ? A ASP 330 OD2 
39  1 Y 1 I GLU 362 ? CG  ? A GLU 362 CG  
40  1 Y 1 I GLU 362 ? CD  ? A GLU 362 CD  
41  1 Y 1 I GLU 362 ? OE1 ? A GLU 362 OE1 
42  1 Y 1 I GLU 362 ? OE2 ? A GLU 362 OE2 
43  1 Y 1 J LYS 411 ? CG  ? B LYS 8   CG  
44  1 Y 1 J LYS 411 ? CD  ? B LYS 8   CD  
45  1 Y 1 J LYS 411 ? CE  ? B LYS 8   CE  
46  1 Y 1 J LYS 411 ? NZ  ? B LYS 8   NZ  
47  1 Y 1 J ARG 414 ? CG  ? B ARG 11  CG  
48  1 Y 1 J ARG 414 ? CD  ? B ARG 11  CD  
49  1 Y 1 J ARG 414 ? NE  ? B ARG 11  NE  
50  1 Y 1 J ARG 414 ? CZ  ? B ARG 11  CZ  
51  1 Y 1 J ARG 414 ? NH1 ? B ARG 11  NH1 
52  1 Y 1 J ARG 414 ? NH2 ? B ARG 11  NH2 
53  1 Y 1 J GLU 416 ? CG  ? B GLU 13  CG  
54  1 Y 1 J GLU 416 ? CD  ? B GLU 13  CD  
55  1 Y 1 J GLU 416 ? OE1 ? B GLU 13  OE1 
56  1 Y 1 J GLU 416 ? OE2 ? B GLU 13  OE2 
57  1 Y 1 J GLU 419 ? CG  ? B GLU 16  CG  
58  1 Y 1 J GLU 419 ? CD  ? B GLU 16  CD  
59  1 Y 1 J GLU 419 ? OE1 ? B GLU 16  OE1 
60  1 Y 1 J GLU 419 ? OE2 ? B GLU 16  OE2 
61  1 Y 1 J GLU 423 ? CG  ? B GLU 20  CG  
62  1 Y 1 J GLU 423 ? CD  ? B GLU 20  CD  
63  1 Y 1 J GLU 423 ? OE1 ? B GLU 20  OE1 
64  1 Y 1 J GLU 423 ? OE2 ? B GLU 20  OE2 
65  1 Y 1 G GLN 86  ? CG  ? C GLN 86  CG  
66  1 Y 1 G GLN 86  ? CD  ? C GLN 86  CD  
67  1 Y 1 G GLN 86  ? OE1 ? C GLN 86  OE1 
68  1 Y 1 G GLN 86  ? NE2 ? C GLN 86  NE2 
69  1 Y 1 G ARG 90  ? CG  ? C ARG 90  CG  
70  1 Y 1 G ARG 90  ? CD  ? C ARG 90  CD  
71  1 Y 1 G ARG 90  ? NE  ? C ARG 90  NE  
72  1 Y 1 G ARG 90  ? CZ  ? C ARG 90  CZ  
73  1 Y 1 G ARG 90  ? NH1 ? C ARG 90  NH1 
74  1 Y 1 G ARG 90  ? NH2 ? C ARG 90  NH2 
75  1 Y 1 G LYS 122 ? CG  ? C LYS 122 CG  
76  1 Y 1 G LYS 122 ? CD  ? C LYS 122 CD  
77  1 Y 1 G LYS 122 ? CE  ? C LYS 122 CE  
78  1 Y 1 G LYS 122 ? NZ  ? C LYS 122 NZ  
79  1 Y 1 G LYS 156 ? CG  ? C LYS 156 CG  
80  1 Y 1 G LYS 156 ? CD  ? C LYS 156 CD  
81  1 Y 1 G LYS 156 ? CE  ? C LYS 156 CE  
82  1 Y 1 G LYS 156 ? NZ  ? C LYS 156 NZ  
83  1 Y 1 G ASP 169 ? CG  ? C ASP 169 CG  
84  1 Y 1 G ASP 169 ? OD1 ? C ASP 169 OD1 
85  1 Y 1 G ASP 169 ? OD2 ? C ASP 169 OD2 
86  1 Y 1 G ARG 170 ? CG  ? C ARG 170 CG  
87  1 Y 1 G ARG 170 ? CD  ? C ARG 170 CD  
88  1 Y 1 G ARG 170 ? NE  ? C ARG 170 NE  
89  1 Y 1 G ARG 170 ? CZ  ? C ARG 170 CZ  
90  1 Y 1 G ARG 170 ? NH1 ? C ARG 170 NH1 
91  1 Y 1 G ARG 170 ? NH2 ? C ARG 170 NH2 
92  1 Y 1 G GLU 177 ? CG  ? C GLU 177 CG  
93  1 Y 1 G GLU 177 ? CD  ? C GLU 177 CD  
94  1 Y 1 G GLU 177 ? OE1 ? C GLU 177 OE1 
95  1 Y 1 G GLU 177 ? OE2 ? C GLU 177 OE2 
96  1 Y 1 G LYS 340 ? CG  ? C LYS 340 CG  
97  1 Y 1 G LYS 340 ? CD  ? C LYS 340 CD  
98  1 Y 1 G LYS 340 ? CE  ? C LYS 340 CE  
99  1 Y 1 G LYS 340 ? NZ  ? C LYS 340 NZ  
100 1 Y 1 H ARG 414 ? CG  ? D ARG 11  CG  
101 1 Y 1 H ARG 414 ? CD  ? D ARG 11  CD  
102 1 Y 1 H ARG 414 ? NE  ? D ARG 11  NE  
103 1 Y 1 H ARG 414 ? CZ  ? D ARG 11  CZ  
104 1 Y 1 H ARG 414 ? NH1 ? D ARG 11  NH1 
105 1 Y 1 H ARG 414 ? NH2 ? D ARG 11  NH2 
106 1 Y 1 H GLU 416 ? CG  ? D GLU 13  CG  
107 1 Y 1 H GLU 416 ? CD  ? D GLU 13  CD  
108 1 Y 1 H GLU 416 ? OE1 ? D GLU 13  OE1 
109 1 Y 1 H GLU 416 ? OE2 ? D GLU 13  OE2 
110 1 Y 1 H GLU 419 ? CG  ? D GLU 16  CG  
111 1 Y 1 H GLU 419 ? CD  ? D GLU 16  CD  
112 1 Y 1 H GLU 419 ? OE1 ? D GLU 16  OE1 
113 1 Y 1 H GLU 419 ? OE2 ? D GLU 16  OE2 
114 1 Y 1 H GLU 423 ? CG  ? D GLU 20  CG  
115 1 Y 1 H GLU 423 ? CD  ? D GLU 20  CD  
116 1 Y 1 H GLU 423 ? OE1 ? D GLU 20  OE1 
117 1 Y 1 H GLU 423 ? OE2 ? D GLU 20  OE2 
118 1 Y 1 A GLN 86  ? CG  ? E GLN 86  CG  
119 1 Y 1 A GLN 86  ? CD  ? E GLN 86  CD  
120 1 Y 1 A GLN 86  ? OE1 ? E GLN 86  OE1 
121 1 Y 1 A GLN 86  ? NE2 ? E GLN 86  NE2 
122 1 Y 1 A LYS 122 ? CG  ? E LYS 122 CG  
123 1 Y 1 A LYS 122 ? CD  ? E LYS 122 CD  
124 1 Y 1 A LYS 122 ? CE  ? E LYS 122 CE  
125 1 Y 1 A LYS 122 ? NZ  ? E LYS 122 NZ  
126 1 Y 1 A LYS 156 ? CG  ? E LYS 156 CG  
127 1 Y 1 A LYS 156 ? CD  ? E LYS 156 CD  
128 1 Y 1 A LYS 156 ? CE  ? E LYS 156 CE  
129 1 Y 1 A LYS 156 ? NZ  ? E LYS 156 NZ  
130 1 Y 1 A ASP 169 ? CG  ? E ASP 169 CG  
131 1 Y 1 A ASP 169 ? OD1 ? E ASP 169 OD1 
132 1 Y 1 A ASP 169 ? OD2 ? E ASP 169 OD2 
133 1 Y 1 A ARG 170 ? CG  ? E ARG 170 CG  
134 1 Y 1 A ARG 170 ? CD  ? E ARG 170 CD  
135 1 Y 1 A ARG 170 ? NE  ? E ARG 170 NE  
136 1 Y 1 A ARG 170 ? CZ  ? E ARG 170 CZ  
137 1 Y 1 A ARG 170 ? NH1 ? E ARG 170 NH1 
138 1 Y 1 A ARG 170 ? NH2 ? E ARG 170 NH2 
139 1 Y 1 A GLU 177 ? CG  ? E GLU 177 CG  
140 1 Y 1 A GLU 177 ? CD  ? E GLU 177 CD  
141 1 Y 1 A GLU 177 ? OE1 ? E GLU 177 OE1 
142 1 Y 1 A GLU 177 ? OE2 ? E GLU 177 OE2 
143 1 Y 1 A GLU 362 ? CG  ? E GLU 362 CG  
144 1 Y 1 A GLU 362 ? CD  ? E GLU 362 CD  
145 1 Y 1 A GLU 362 ? OE1 ? E GLU 362 OE1 
146 1 Y 1 A GLU 362 ? OE2 ? E GLU 362 OE2 
147 1 Y 1 B LYS 411 ? CG  ? F LYS 8   CG  
148 1 Y 1 B LYS 411 ? CD  ? F LYS 8   CD  
149 1 Y 1 B LYS 411 ? CE  ? F LYS 8   CE  
150 1 Y 1 B LYS 411 ? NZ  ? F LYS 8   NZ  
151 1 Y 1 B ARG 414 ? CG  ? F ARG 11  CG  
152 1 Y 1 B ARG 414 ? CD  ? F ARG 11  CD  
153 1 Y 1 B ARG 414 ? NE  ? F ARG 11  NE  
154 1 Y 1 B ARG 414 ? CZ  ? F ARG 11  CZ  
155 1 Y 1 B ARG 414 ? NH1 ? F ARG 11  NH1 
156 1 Y 1 B ARG 414 ? NH2 ? F ARG 11  NH2 
157 1 Y 1 B GLU 416 ? CG  ? F GLU 13  CG  
158 1 Y 1 B GLU 416 ? CD  ? F GLU 13  CD  
159 1 Y 1 B GLU 416 ? OE1 ? F GLU 13  OE1 
160 1 Y 1 B GLU 416 ? OE2 ? F GLU 13  OE2 
161 1 Y 1 B GLU 419 ? CG  ? F GLU 16  CG  
162 1 Y 1 B GLU 419 ? CD  ? F GLU 16  CD  
163 1 Y 1 B GLU 419 ? OE1 ? F GLU 16  OE1 
164 1 Y 1 B GLU 419 ? OE2 ? F GLU 16  OE2 
165 1 Y 1 B GLU 423 ? CG  ? F GLU 20  CG  
166 1 Y 1 B GLU 423 ? CD  ? F GLU 20  CD  
167 1 Y 1 B GLU 423 ? OE1 ? F GLU 20  OE1 
168 1 Y 1 B GLU 423 ? OE2 ? F GLU 20  OE2 
169 1 Y 1 C ASP 169 ? CG  ? G ASP 169 CG  
170 1 Y 1 C ASP 169 ? OD1 ? G ASP 169 OD1 
171 1 Y 1 C ASP 169 ? OD2 ? G ASP 169 OD2 
172 1 Y 1 C ARG 170 ? CG  ? G ARG 170 CG  
173 1 Y 1 C ARG 170 ? CD  ? G ARG 170 CD  
174 1 Y 1 C ARG 170 ? NE  ? G ARG 170 NE  
175 1 Y 1 C ARG 170 ? CZ  ? G ARG 170 CZ  
176 1 Y 1 C ARG 170 ? NH1 ? G ARG 170 NH1 
177 1 Y 1 C ARG 170 ? NH2 ? G ARG 170 NH2 
178 1 Y 1 C GLU 177 ? CG  ? G GLU 177 CG  
179 1 Y 1 C GLU 177 ? CD  ? G GLU 177 CD  
180 1 Y 1 C GLU 177 ? OE1 ? G GLU 177 OE1 
181 1 Y 1 C GLU 177 ? OE2 ? G GLU 177 OE2 
182 1 Y 1 C ARG 178 ? CZ  ? G ARG 178 CZ  
183 1 Y 1 C ARG 178 ? NH1 ? G ARG 178 NH1 
184 1 Y 1 C ARG 178 ? NH2 ? G ARG 178 NH2 
185 1 Y 1 C ASP 330 ? CG  ? G ASP 330 CG  
186 1 Y 1 C ASP 330 ? OD1 ? G ASP 330 OD1 
187 1 Y 1 C ASP 330 ? OD2 ? G ASP 330 OD2 
188 1 Y 1 C ASP 332 ? CG  ? G ASP 332 CG  
189 1 Y 1 C ASP 332 ? OD1 ? G ASP 332 OD1 
190 1 Y 1 C ASP 332 ? OD2 ? G ASP 332 OD2 
191 1 Y 1 C LYS 361 ? CG  ? G LYS 361 CG  
192 1 Y 1 C LYS 361 ? CD  ? G LYS 361 CD  
193 1 Y 1 C LYS 361 ? CE  ? G LYS 361 CE  
194 1 Y 1 C LYS 361 ? NZ  ? G LYS 361 NZ  
195 1 Y 1 D LYS 411 ? CG  ? H LYS 8   CG  
196 1 Y 1 D LYS 411 ? CD  ? H LYS 8   CD  
197 1 Y 1 D LYS 411 ? CE  ? H LYS 8   CE  
198 1 Y 1 D LYS 411 ? NZ  ? H LYS 8   NZ  
199 1 Y 1 D ARG 414 ? CG  ? H ARG 11  CG  
200 1 Y 1 D ARG 414 ? CD  ? H ARG 11  CD  
201 1 Y 1 D ARG 414 ? NE  ? H ARG 11  NE  
202 1 Y 1 D ARG 414 ? CZ  ? H ARG 11  CZ  
203 1 Y 1 D ARG 414 ? NH1 ? H ARG 11  NH1 
204 1 Y 1 D ARG 414 ? NH2 ? H ARG 11  NH2 
205 1 Y 1 D GLU 419 ? CG  ? H GLU 16  CG  
206 1 Y 1 D GLU 419 ? CD  ? H GLU 16  CD  
207 1 Y 1 D GLU 419 ? OE1 ? H GLU 16  OE1 
208 1 Y 1 D GLU 419 ? OE2 ? H GLU 16  OE2 
209 1 Y 1 D GLU 423 ? CG  ? H GLU 20  CG  
210 1 Y 1 D GLU 423 ? CD  ? H GLU 20  CD  
211 1 Y 1 D GLU 423 ? OE1 ? H GLU 20  OE1 
212 1 Y 1 D GLU 423 ? OE2 ? H GLU 20  OE2 
213 1 Y 1 E LYS 122 ? CG  ? I LYS 122 CG  
214 1 Y 1 E LYS 122 ? CD  ? I LYS 122 CD  
215 1 Y 1 E LYS 122 ? CE  ? I LYS 122 CE  
216 1 Y 1 E LYS 122 ? NZ  ? I LYS 122 NZ  
217 1 Y 1 E LYS 156 ? CG  ? I LYS 156 CG  
218 1 Y 1 E LYS 156 ? CD  ? I LYS 156 CD  
219 1 Y 1 E LYS 156 ? CE  ? I LYS 156 CE  
220 1 Y 1 E LYS 156 ? NZ  ? I LYS 156 NZ  
221 1 Y 1 E ASP 169 ? CG  ? I ASP 169 CG  
222 1 Y 1 E ASP 169 ? OD1 ? I ASP 169 OD1 
223 1 Y 1 E ASP 169 ? OD2 ? I ASP 169 OD2 
224 1 Y 1 E ARG 170 ? CG  ? I ARG 170 CG  
225 1 Y 1 E ARG 170 ? CD  ? I ARG 170 CD  
226 1 Y 1 E ARG 170 ? NE  ? I ARG 170 NE  
227 1 Y 1 E ARG 170 ? CZ  ? I ARG 170 CZ  
228 1 Y 1 E ARG 170 ? NH1 ? I ARG 170 NH1 
229 1 Y 1 E ARG 170 ? NH2 ? I ARG 170 NH2 
230 1 Y 1 E ARG 178 ? CG  ? I ARG 178 CG  
231 1 Y 1 E ARG 178 ? CD  ? I ARG 178 CD  
232 1 Y 1 E ARG 178 ? NE  ? I ARG 178 NE  
233 1 Y 1 E ARG 178 ? CZ  ? I ARG 178 CZ  
234 1 Y 1 E ARG 178 ? NH1 ? I ARG 178 NH1 
235 1 Y 1 E ARG 178 ? NH2 ? I ARG 178 NH2 
236 1 Y 1 E ARG 217 ? CZ  ? I ARG 217 CZ  
237 1 Y 1 E ARG 217 ? NH1 ? I ARG 217 NH1 
238 1 Y 1 E ARG 217 ? NH2 ? I ARG 217 NH2 
239 1 Y 1 E ASP 330 ? CG  ? I ASP 330 CG  
240 1 Y 1 E ASP 330 ? OD1 ? I ASP 330 OD1 
241 1 Y 1 E ASP 330 ? OD2 ? I ASP 330 OD2 
242 1 Y 1 E ASP 332 ? CG  ? I ASP 332 CG  
243 1 Y 1 E ASP 332 ? OD1 ? I ASP 332 OD1 
244 1 Y 1 E ASP 332 ? OD2 ? I ASP 332 OD2 
245 1 Y 1 E LYS 361 ? CG  ? I LYS 361 CG  
246 1 Y 1 E LYS 361 ? CD  ? I LYS 361 CD  
247 1 Y 1 E LYS 361 ? CE  ? I LYS 361 CE  
248 1 Y 1 E LYS 361 ? NZ  ? I LYS 361 NZ  
249 1 Y 1 F LYS 411 ? CG  ? J LYS 8   CG  
250 1 Y 1 F LYS 411 ? CD  ? J LYS 8   CD  
251 1 Y 1 F LYS 411 ? CE  ? J LYS 8   CE  
252 1 Y 1 F LYS 411 ? NZ  ? J LYS 8   NZ  
253 1 Y 1 F ARG 414 ? CG  ? J ARG 11  CG  
254 1 Y 1 F ARG 414 ? CD  ? J ARG 11  CD  
255 1 Y 1 F ARG 414 ? NE  ? J ARG 11  NE  
256 1 Y 1 F ARG 414 ? CZ  ? J ARG 11  CZ  
257 1 Y 1 F ARG 414 ? NH1 ? J ARG 11  NH1 
258 1 Y 1 F ARG 414 ? NH2 ? J ARG 11  NH2 
259 1 Y 1 F GLU 416 ? CG  ? J GLU 13  CG  
260 1 Y 1 F GLU 416 ? CD  ? J GLU 13  CD  
261 1 Y 1 F GLU 416 ? OE1 ? J GLU 13  OE1 
262 1 Y 1 F GLU 416 ? OE2 ? J GLU 13  OE2 
263 1 Y 1 K LYS 156 ? CG  ? K LYS 156 CG  
264 1 Y 1 K LYS 156 ? CD  ? K LYS 156 CD  
265 1 Y 1 K LYS 156 ? CE  ? K LYS 156 CE  
266 1 Y 1 K LYS 156 ? NZ  ? K LYS 156 NZ  
267 1 Y 1 K ASP 169 ? CG  ? K ASP 169 CG  
268 1 Y 1 K ASP 169 ? OD1 ? K ASP 169 OD1 
269 1 Y 1 K ASP 169 ? OD2 ? K ASP 169 OD2 
270 1 Y 1 K ARG 170 ? CG  ? K ARG 170 CG  
271 1 Y 1 K ARG 170 ? CD  ? K ARG 170 CD  
272 1 Y 1 K ARG 170 ? NE  ? K ARG 170 NE  
273 1 Y 1 K ARG 170 ? CZ  ? K ARG 170 CZ  
274 1 Y 1 K ARG 170 ? NH1 ? K ARG 170 NH1 
275 1 Y 1 K ARG 170 ? NH2 ? K ARG 170 NH2 
276 1 Y 1 K GLU 177 ? CG  ? K GLU 177 CG  
277 1 Y 1 K GLU 177 ? CD  ? K GLU 177 CD  
278 1 Y 1 K GLU 177 ? OE1 ? K GLU 177 OE1 
279 1 Y 1 K GLU 177 ? OE2 ? K GLU 177 OE2 
280 1 Y 1 K ARG 225 ? CG  ? K ARG 225 CG  
281 1 Y 1 K ARG 225 ? CD  ? K ARG 225 CD  
282 1 Y 1 K ARG 225 ? NE  ? K ARG 225 NE  
283 1 Y 1 K ARG 225 ? CZ  ? K ARG 225 CZ  
284 1 Y 1 K ARG 225 ? NH1 ? K ARG 225 NH1 
285 1 Y 1 K ARG 225 ? NH2 ? K ARG 225 NH2 
286 1 Y 1 K LYS 361 ? CG  ? K LYS 361 CG  
287 1 Y 1 K LYS 361 ? CD  ? K LYS 361 CD  
288 1 Y 1 K LYS 361 ? CE  ? K LYS 361 CE  
289 1 Y 1 K LYS 361 ? NZ  ? K LYS 361 NZ  
290 1 Y 1 K GLU 362 ? CG  ? K GLU 362 CG  
291 1 Y 1 K GLU 362 ? CD  ? K GLU 362 CD  
292 1 Y 1 K GLU 362 ? OE1 ? K GLU 362 OE1 
293 1 Y 1 K GLU 362 ? OE2 ? K GLU 362 OE2 
294 1 Y 1 L LYS 411 ? CG  ? L LYS 8   CG  
295 1 Y 1 L LYS 411 ? CD  ? L LYS 8   CD  
296 1 Y 1 L LYS 411 ? CE  ? L LYS 8   CE  
297 1 Y 1 L LYS 411 ? NZ  ? L LYS 8   NZ  
298 1 Y 1 L ARG 414 ? CG  ? L ARG 11  CG  
299 1 Y 1 L ARG 414 ? CD  ? L ARG 11  CD  
300 1 Y 1 L ARG 414 ? NE  ? L ARG 11  NE  
301 1 Y 1 L ARG 414 ? CZ  ? L ARG 11  CZ  
302 1 Y 1 L ARG 414 ? NH1 ? L ARG 11  NH1 
303 1 Y 1 L ARG 414 ? NH2 ? L ARG 11  NH2 
304 1 Y 1 L GLU 416 ? CG  ? L GLU 13  CG  
305 1 Y 1 L GLU 416 ? CD  ? L GLU 13  CD  
306 1 Y 1 L GLU 416 ? OE1 ? L GLU 13  OE1 
307 1 Y 1 L GLU 416 ? OE2 ? L GLU 13  OE2 
308 1 Y 1 L GLU 423 ? CG  ? L GLU 20  CG  
309 1 Y 1 L GLU 423 ? CD  ? L GLU 20  CD  
310 1 Y 1 L GLU 423 ? OE1 ? L GLU 20  OE1 
311 1 Y 1 L GLU 423 ? OE2 ? L GLU 20  OE2 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement        ? ? ? ? ? ? ? ? ? ? ? PHENIX   ? ? ? 1.21rc1_5156 1 
? 'data processing' ? ? ? ? ? ? ? ? ? ? ? autoPROC ? ? ? 1.20.1_4487  2 
? 'data reduction'  ? ? ? ? ? ? ? ? ? ? ? XDS      ? ? ? .            3 
? 'data scaling'    ? ? ? ? ? ? ? ? ? ? ? SCALA    ? ? ? .            4 
? phasing           ? ? ? ? ? ? ? ? ? ? ? PHASER   ? ? ? .            5 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   99.770 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8X4S 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     82.681 
_cell.length_a_esd                 ? 
_cell.length_b                     122.502 
_cell.length_b_esd                 ? 
_cell.length_c                     128.716 
_cell.length_c_esd                 ? 
_cell.volume                       1284803.440 
_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             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         8X4S 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                4 
_symmetry.space_group_name_Hall            'P 2yb' 
_symmetry.space_group_name_H-M             'P 1 21 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   8X4S 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             2.16 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          42.98 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '0.2 M Sodium chloride, 0.1 M Tris pH 8.5, 25% w/v Polyethylene glycol 3,350' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS 6M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2023-07-10 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.97853 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'SSRF BEAMLINE BL18U1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.97853 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL18U1 
_diffrn_source.pdbx_synchrotron_site       SSRF 
# 
_reflns.B_iso_Wilson_estimate                          40.56 
_reflns.entry_id                                       8X4S 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.7 
_reflns.d_resolution_low                               30 
_reflns.details                                        ? 
_reflns.limit_h_max                                    ? 
_reflns.limit_h_min                                    ? 
_reflns.limit_k_max                                    ? 
_reflns.limit_k_min                                    ? 
_reflns.limit_l_max                                    ? 
_reflns.limit_l_min                                    ? 
_reflns.number_all                                     ? 
_reflns.number_obs                                     69245 
_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                                6.8 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          7.7 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.206 
_reflns.pdbx_Rpim_I_all                                0.079 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.987 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.190 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    2.70 
_reflns_shell.d_res_low                                     2.85 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           2.6 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             10086 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               6.9 
_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                               0.822 
_reflns_shell.pdbx_Rpim_I_all                               0.308 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.820 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          99.8 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  0.761 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               45.05 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 8X4S 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            2.70 
_refine.ls_d_res_low                             29.77 
_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                     69201 
_refine.ls_number_reflns_R_free                  3487 
_refine.ls_number_reflns_R_work                  65714 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.68 
_refine.ls_percent_reflns_R_free                 5.04 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2001 
_refine.ls_R_factor_R_free                       0.2329 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1984 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.34 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      8X4Q 
_refine.pdbx_stereochemistry_target_values       'GeoStd + Monomer Library + CDL v1.2' 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.1000 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_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                 24.6536 
_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                            0.3361 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       2.70 
_refine_hist.d_res_low                        29.77 
_refine_hist.number_atoms_solvent             467 
_refine_hist.number_atoms_total               18594 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        18047 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         80 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.0094  ? 18608 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.0738  ? 25273 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0560  ? 2721  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0097  ? 3325  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 16.0086 ? 6608  ? f_dihedral_angle_d ? ? 
# 
loop_
_refine_ls_restr_ncs.pdbx_ordinal 
_refine_ls_restr_ncs.pdbx_refine_id 
_refine_ls_restr_ncs.dom_id 
_refine_ls_restr_ncs.pdbx_ens_id 
_refine_ls_restr_ncs.rms_dev_position 
_refine_ls_restr_ncs.weight_position 
_refine_ls_restr_ncs.rms_dev_B_iso 
_refine_ls_restr_ncs.weight_B_iso 
_refine_ls_restr_ncs.pdbx_type 
_refine_ls_restr_ncs.pdbx_asym_id 
_refine_ls_restr_ncs.pdbx_auth_asym_id 
_refine_ls_restr_ncs.pdbx_number 
_refine_ls_restr_ncs.pdbx_rms 
_refine_ls_restr_ncs.pdbx_weight 
_refine_ls_restr_ncs.ncs_model_details 
1  'X-RAY DIFFRACTION' d_2 ens_1 0.0121255230445   ? ? ? 'NCS constraints' E A ? ? ? ? 
2  'X-RAY DIFFRACTION' d_3 ens_1 0.0041756256518   ? ? ? 'NCS constraints' E A ? ? ? ? 
3  'X-RAY DIFFRACTION' d_4 ens_1 0.0121255230445   ? ? ? 'NCS constraints' E A ? ? ? ? 
4  'X-RAY DIFFRACTION' d_5 ens_1 4.2111106205e-13  ? ? ? 'NCS constraints' E A ? ? ? ? 
5  'X-RAY DIFFRACTION' d_6 ens_1 0.0030204953913   ? ? ? 'NCS constraints' E A ? ? ? ? 
6  'X-RAY DIFFRACTION' d_2 ens_2 0.0087393732666   ? ? ? 'NCS constraints' H D ? ? ? ? 
7  'X-RAY DIFFRACTION' d_3 ens_2 5.15514611559e-11 ? ? ? 'NCS constraints' H D ? ? ? ? 
8  'X-RAY DIFFRACTION' d_4 ens_2 0                 ? ? ? 'NCS constraints' H D ? ? ? ? 
9  'X-RAY DIFFRACTION' d_5 ens_2 6.90164152732e-12 ? ? ? 'NCS constraints' H D ? ? ? ? 
10 'X-RAY DIFFRACTION' d_6 ens_2 2.31698127489e-13 ? ? ? 'NCS constraints' H D ? ? ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 2.70 2.74  . . 139 2654 99.64 . . . . 0.2802 . . . . . . . . . . . 0.3320 
'X-RAY DIFFRACTION' 2.74 2.78  . . 153 2569 99.82 . . . . 0.2812 . . . . . . . . . . . 0.3578 
'X-RAY DIFFRACTION' 2.78 2.82  . . 114 2634 99.67 . . . . 0.2772 . . . . . . . . . . . 0.3446 
'X-RAY DIFFRACTION' 2.82 2.86  . . 134 2621 99.57 . . . . 0.2860 . . . . . . . . . . . 0.3668 
'X-RAY DIFFRACTION' 2.86 2.91  . . 154 2584 99.78 . . . . 0.2730 . . . . . . . . . . . 0.3516 
'X-RAY DIFFRACTION' 2.91 2.96  . . 123 2673 99.68 . . . . 0.2601 . . . . . . . . . . . 0.2706 
'X-RAY DIFFRACTION' 2.96 3.01  . . 143 2593 99.78 . . . . 0.2507 . . . . . . . . . . . 0.3247 
'X-RAY DIFFRACTION' 3.01 3.07  . . 129 2680 99.79 . . . . 0.2399 . . . . . . . . . . . 0.2987 
'X-RAY DIFFRACTION' 3.07 3.13  . . 137 2563 99.78 . . . . 0.2379 . . . . . . . . . . . 0.2877 
'X-RAY DIFFRACTION' 3.13 3.20  . . 136 2642 99.78 . . . . 0.2469 . . . . . . . . . . . 0.2599 
'X-RAY DIFFRACTION' 3.20 3.27  . . 131 2631 99.82 . . . . 0.2483 . . . . . . . . . . . 0.2785 
'X-RAY DIFFRACTION' 3.28 3.36  . . 150 2614 99.78 . . . . 0.2295 . . . . . . . . . . . 0.2836 
'X-RAY DIFFRACTION' 3.36 3.45  . . 146 2618 99.75 . . . . 0.2223 . . . . . . . . . . . 0.2864 
'X-RAY DIFFRACTION' 3.45 3.55  . . 131 2633 99.78 . . . . 0.2154 . . . . . . . . . . . 0.2260 
'X-RAY DIFFRACTION' 3.55 3.66  . . 156 2599 99.89 . . . . 0.2058 . . . . . . . . . . . 0.2488 
'X-RAY DIFFRACTION' 3.66 3.79  . . 142 2654 99.79 . . . . 0.2024 . . . . . . . . . . . 0.2231 
'X-RAY DIFFRACTION' 3.79 3.95  . . 149 2610 99.71 . . . . 0.1915 . . . . . . . . . . . 0.2282 
'X-RAY DIFFRACTION' 3.95 4.12  . . 141 2623 99.82 . . . . 0.1817 . . . . . . . . . . . 0.2075 
'X-RAY DIFFRACTION' 4.12 4.34  . . 125 2657 99.82 . . . . 0.1575 . . . . . . . . . . . 0.1923 
'X-RAY DIFFRACTION' 4.34 4.61  . . 127 2640 99.82 . . . . 0.1562 . . . . . . . . . . . 0.1628 
'X-RAY DIFFRACTION' 4.61 4.97  . . 146 2618 99.89 . . . . 0.1487 . . . . . . . . . . . 0.1806 
'X-RAY DIFFRACTION' 4.97 5.46  . . 147 2656 99.64 . . . . 0.1581 . . . . . . . . . . . 0.1976 
'X-RAY DIFFRACTION' 5.46 6.25  . . 138 2634 99.60 . . . . 0.1726 . . . . . . . . . . . 0.1885 
'X-RAY DIFFRACTION' 6.25 7.85  . . 162 2645 99.65 . . . . 0.1634 . . . . . . . . . . . 0.1889 
'X-RAY DIFFRACTION' 7.85 29.77 . . 134 2669 98.14 . . . . 0.1449 . . . . . . . . . . . 0.1560 
# 
loop_
_struct_ncs_oper.id 
_struct_ncs_oper.code 
_struct_ncs_oper.matrix[1][1] 
_struct_ncs_oper.matrix[1][2] 
_struct_ncs_oper.matrix[1][3] 
_struct_ncs_oper.matrix[2][1] 
_struct_ncs_oper.matrix[2][2] 
_struct_ncs_oper.matrix[2][3] 
_struct_ncs_oper.matrix[3][1] 
_struct_ncs_oper.matrix[3][2] 
_struct_ncs_oper.matrix[3][3] 
_struct_ncs_oper.vector[1] 
_struct_ncs_oper.vector[2] 
_struct_ncs_oper.vector[3] 
_struct_ncs_oper.details 
1  given 0.999737753658  -0.0113765880908 -0.0198745353083  -0.0166669462995  -0.956642826389  -0.290786374542 -0.0157046748249  
0.291041364692  -0.95658156329  26.2735552958  107.502098085  15.513139422  ? 
2  given -0.855224213257 -0.153025447384  0.495151247108    0.261684430084    0.697169703472   0.667439632935  -0.447339696552   
0.700383906878  -0.556192034171 11.026030627   -77.204928479  42.4823727553 ? 
3  given -0.999918843828 0.00202624137527 0.0125777622448   -0.00788395013846 0.67710387609    -0.735845217634 -0.0100074515942  
-0.735884661703 -0.677032950145 30.8334792704  11.6753274683  75.3539116954 ? 
4  given 0.999370628853  -0.0228793252579 -0.0271087192756  -0.0040389869552  -0.832624431403  0.55382329566   -0.0352424852897  
-0.553365243494 -0.832192810906 -4.11534937292 44.5273277531  33.3272149322 ? 
5  given 0.874154203292  0.427824889018   0.229826659038    -0.211702539196   -0.0902184899919 0.97316116803   0.437077182847    
-0.899347812807 0.0117067430952 -13.7948283487 -12.6918390033 92.3996872194 ? 
6  given 0.999511076251  -0.0254818322353 -0.0181186278974  -0.0296661570142  -0.955915275636  -0.292140214509 -0.00987560524535 
0.292534890281  -0.956203853992 27.1477283049  107.700328556  15.2422574889 ? 
7  given -0.862144929966 -0.150020217367  0.483942201213    0.261578532229    0.686223393239   0.678729788685  -0.43391564988    
0.711752336809  -0.552381951041 11.3548724743  -76.6610766876 41.3121985833 ? 
8  given -0.999867671065 0.00946012140012 0.0132342911598   -0.0032853180644  0.679340758058   -0.733815604308 -0.0159325780909  
-0.733761978127 -0.679219782111 30.3795170079  11.3462065904  75.3873132011 ? 
9  given 0.999412732365  -0.0327891766795 -0.00995290306396 -0.0218331145879  -0.833194421699  0.55254897589   -0.0264103293071  
-0.552007178887 -0.833421003433 -4.01079939518 44.941826644   32.930440587  ? 
10 given 0.865767609446  0.431540474377   0.253415203586    -0.23505699196    -0.0963896142856 0.967190391179  0.44180839395     
-0.896929128322 0.0179855998805 -14.5953241639 -11.1900130997 91.7748689122 ? 
# 
loop_
_struct_ncs_dom.pdbx_ens_id 
_struct_ncs_dom.id 
_struct_ncs_dom.details 
ens_1 d_1 
;(chain "A" and (resid 57 through 61 or resid 63 through 82 or (resid 83 and (name N or name CA or name C or name O or name CB )) or resid 84 through 89 or (resid 90 and (name N or name CA or name C or name O or name CB )) or resid 91 through 103 or resid 105 through 111 or resid 113 through 126 or resid 128 through 136 or resid 138 through 143 or resid 145 through 177 or (resid 178 through 179 and (name N or name CA or name C or name O or name CB )) or resid 180 through 216 or resid 218 through 224 or (resid 225 and (name N or name CA or name C or name O or name CB )) or resid 226 through 260 or resid 262 through 329 or (resid 330 and (name N or name CA or name C or name O or name CB )) or resid 331 or resid 334 through 339 or (resid 340 and (name N or name CA or name C or name O or name CB )) or resid 341 through 360 or (resid 361 through 362 and (name N or name CA or name C or name O or name CB )) or resid 363 through 402))
;
ens_1 d_2 
;(chain "C" and (resid 57 through 61 or resid 63 through 82 or (resid 83 and (name N or name CA or name C or name O or name CB )) or resid 84 through 85 or (resid 86 and (name N or name CA or name C or name O or name CB )) or resid 87 through 89 or (resid 90 and (name N or name CA or name C or name O or name CB )) or resid 91 through 103 or resid 105 through 111 or resid 113 through 121 or (resid 122 and (name N or name CA or name C or name O or name CB )) or resid 123 through 126 or resid 128 through 136 or resid 138 through 143 or resid 145 through 155 or (resid 156 and (name N or name CA or name C or name O or name CB )) or resid 157 through 177 or (resid 178 through 179 and (name N or name CA or name C or name O or name CB )) or resid 180 through 216 or resid 218 through 224 or (resid 225 and (name N or name CA or name C or name O or name CB )) or resid 226 through 260 or resid 262 through 331 or resid 334 through 339 or (resid 340 and (name N or name CA or name C or name O or name CB )) or resid 341 through 361 or (resid 362 and (name N or name CA or name C or name O or name CB )) or resid 363 through 402))
;
ens_1 d_3 
;(chain "E" and (resid 57 through 61 or resid 63 through 82 or (resid 83 and (name N or name CA or name C or name O or name CB )) or resid 84 through 85 or (resid 86 and (name N or name CA or name C or name O or name CB )) or resid 87 through 89 or (resid 90 and (name N or name CA or name C or name O or name CB )) or resid 91 through 103 or resid 105 through 111 or resid 113 through 126 or resid 128 through 136 or resid 138 through 143 or resid 145 through 176 or (resid 177 through 179 and (name N or name CA or name C or name O or name CB )) or resid 180 through 216 or resid 218 through 224 or (resid 225 and (name N or name CA or name C or name O or name CB )) or resid 226 through 260 or resid 262 through 331 or resid 334 through 339 or (resid 340 and (name N or name CA or name C or name O or name CB )) or resid 341 through 361 or (resid 362 and (name N or name CA or name C or name O or name CB )) or resid 363 through 402))
;
ens_1 d_4 
;(chain "G" and (resid 57 through 61 or resid 63 through 82 or (resid 83 and (name N or name CA or name C or name O or name CB )) or resid 84 through 103 or resid 105 through 111 or resid 113 through 126 or resid 128 through 136 or resid 138 through 143 or resid 145 through 177 or (resid 178 through 179 and (name N or name CA or name C or name O or name CB )) or resid 180 through 216 or resid 218 through 224 or (resid 225 and (name N or name CA or name C or name O or name CB )) or resid 226 through 260 or resid 262 through 329 or (resid 330 and (name N or name CA or name C or name O or name CB )) or resid 331 or resid 334 through 360 or (resid 361 through 362 and (name N or name CA or name C or name O or name CB )) or resid 363 through 402))
;
ens_1 d_5 
;(chain "I" and (resid 57 through 61 or resid 63 through 103 or resid 105 through 111 or resid 113 through 126 or resid 128 through 136 or resid 138 through 143 or resid 145 through 177 or (resid 178 through 179 and (name N or name CA or name C or name O or name CB )) or resid 180 through 216 or resid 218 through 224 or (resid 225 and (name N or name CA or name C or name O or name CB )) or resid 226 through 260 or resid 262 through 331 or resid 334 through 339 or (resid 340 and (name N or name CA or name C or name O or name CB )) or resid 341 through 360 or (resid 361 through 362 and (name N or name CA or name C or name O or name CB )) or resid 363 through 402))
;
ens_1 d_6 
;(chain "K" and (resid 57 through 61 or resid 63 through 82 or (resid 83 and (name N or name CA or name C or name O or name CB )) or resid 84 through 85 or (resid 86 and (name N or name CA or name C or name O or name CB )) or resid 87 through 89 or (resid 90 and (name N or name CA or name C or name O or name CB )) or resid 91 through 103 or resid 105 through 111 or resid 113 through 121 or (resid 122 and (name N or name CA or name C or name O or name CB )) or resid 123 through 126 or resid 128 through 136 or resid 138 through 143 or resid 145 through 177 or (resid 178 through 179 and (name N or name CA or name C or name O or name CB )) or resid 180 through 216 or resid 218 through 260 or resid 262 through 329 or (resid 330 and (name N or name CA or name C or name O or name CB )) or resid 331 or resid 334 through 339 or (resid 340 and (name N or name CA or name C or name O or name CB )) or resid 341 through 402))
;
ens_2 d_1 
;(chain "D" and (resid 404 through 415 or (resid 416 and (name N or name CA or name C or name O or name CB )) or resid 417 through 437))
;
ens_2 d_2 
;(chain "B" and resid 404 through 437)
;
ens_2 d_3 
;(chain "F" and (resid 404 through 418 or (resid 419 and (name N or name CA or name C or name O or name CB )) or resid 420 through 422 or (resid 423 and (name N or name CA or name C or name O or name CB )) or resid 424 through 437))
;
ens_2 d_4 
;(chain "H" and (resid 404 through 410 or (resid 411 and (name N or name CA or name C or name O or name CB )) or resid 412 through 437))
;
ens_2 d_5 
;(chain "J" and resid 404 through 437)
;
ens_2 d_6 
;(chain "L" and (resid 404 through 418 or (resid 419 and (name N or name CA or name C or name O or name CB )) or resid 420 through 437))
;
# 
loop_
_struct_ncs_dom_lim.pdbx_ens_id 
_struct_ncs_dom_lim.dom_id 
_struct_ncs_dom_lim.pdbx_component_id 
_struct_ncs_dom_lim.beg_label_asym_id 
_struct_ncs_dom_lim.beg_label_comp_id 
_struct_ncs_dom_lim.beg_label_seq_id 
_struct_ncs_dom_lim.beg_label_alt_id 
_struct_ncs_dom_lim.end_label_asym_id 
_struct_ncs_dom_lim.end_label_comp_id 
_struct_ncs_dom_lim.end_label_seq_id 
_struct_ncs_dom_lim.end_label_alt_id 
_struct_ncs_dom_lim.beg_auth_asym_id 
_struct_ncs_dom_lim.beg_auth_comp_id 
_struct_ncs_dom_lim.beg_auth_seq_id 
_struct_ncs_dom_lim.end_auth_asym_id 
_struct_ncs_dom_lim.end_auth_comp_id 
_struct_ncs_dom_lim.end_auth_seq_id 
_struct_ncs_dom_lim.pdbx_refine_code 
_struct_ncs_dom_lim.selection_details 
ens_1 d_1 1  E LEU 57  . E ILE 61  . A LEU 57  A ILE 61  ? ? 
ens_1 d_1 2  E GLU 63  . E PHE 103 . A GLU 63  A PHE 103 ? ? 
ens_1 d_1 3  E LYS 105 . E ASP 111 . A LYS 105 A ASP 111 ? ? 
ens_1 d_1 4  E GLY 113 . E THR 126 . A GLY 113 A THR 126 ? ? 
ens_1 d_1 5  E ALA 128 . E GLN 136 . A ALA 128 A GLN 136 ? ? 
ens_1 d_1 6  E LEU 138 . E LYS 143 . A LEU 138 A LYS 143 ? ? 
ens_1 d_1 7  E LEU 145 . E ARG 216 . A LEU 145 A ARG 216 ? ? 
ens_1 d_1 8  E PHE 218 . E PHE 260 . A PHE 218 A PHE 260 ? ? 
ens_1 d_1 9  E GLY 262 . E ASN 331 . A GLY 262 A ASN 331 ? ? 
ens_1 d_1 10 E ASP 334 . E GLY 402 . A ASP 334 A GLY 402 ? ? 
ens_1 d_2 1  G LEU 57  . G ILE 61  . C LEU 57  C ILE 61  ? ? 
ens_1 d_2 2  G GLU 63  . G PHE 103 . C GLU 63  C PHE 103 ? ? 
ens_1 d_2 3  G LYS 105 . G ASP 111 . C LYS 105 C ASP 111 ? ? 
ens_1 d_2 4  G GLY 113 . G THR 126 . C GLY 113 C THR 126 ? ? 
ens_1 d_2 5  G ALA 128 . G GLN 136 . C ALA 128 C GLN 136 ? ? 
ens_1 d_2 6  G LEU 138 . G LYS 143 . C LEU 138 C LYS 143 ? ? 
ens_1 d_2 7  G LEU 145 . G ARG 216 . C LEU 145 C ARG 216 ? ? 
ens_1 d_2 8  G PHE 218 . G PHE 260 . C PHE 218 C PHE 260 ? ? 
ens_1 d_2 9  G GLY 262 . G ASN 331 . C GLY 262 C ASN 331 ? ? 
ens_1 d_2 10 G ASP 334 . G GLY 402 . C ASP 334 C GLY 402 ? ? 
ens_1 d_3 1  I LEU 57  . I ILE 61  . E LEU 57  E ILE 61  ? ? 
ens_1 d_3 2  I GLU 63  . I PHE 103 . E GLU 63  E PHE 103 ? ? 
ens_1 d_3 3  I LYS 105 . I ASP 111 . E LYS 105 E ASP 111 ? ? 
ens_1 d_3 4  I GLY 113 . I THR 126 . E GLY 113 E THR 126 ? ? 
ens_1 d_3 5  I ALA 128 . I GLN 136 . E ALA 128 E GLN 136 ? ? 
ens_1 d_3 6  I LEU 138 . I LYS 143 . E LEU 138 E LYS 143 ? ? 
ens_1 d_3 7  I LEU 145 . I ARG 216 . E LEU 145 E ARG 216 ? ? 
ens_1 d_3 8  I PHE 218 . I PHE 260 . E PHE 218 E PHE 260 ? ? 
ens_1 d_3 9  I GLY 262 . I ASN 331 . E GLY 262 E ASN 331 ? ? 
ens_1 d_3 10 I ASP 334 . I GLY 402 . E ASP 334 E GLY 402 ? ? 
ens_1 d_4 1  C LEU 57  . C ILE 61  . G LEU 57  G ILE 61  ? ? 
ens_1 d_4 2  C GLU 63  . C PHE 103 . G GLU 63  G PHE 103 ? ? 
ens_1 d_4 3  C LYS 105 . C ASP 111 . G LYS 105 G ASP 111 ? ? 
ens_1 d_4 4  C GLY 113 . C THR 126 . G GLY 113 G THR 126 ? ? 
ens_1 d_4 5  C ALA 128 . C GLN 136 . G ALA 128 G GLN 136 ? ? 
ens_1 d_4 6  C LEU 138 . C LYS 143 . G LEU 138 G LYS 143 ? ? 
ens_1 d_4 7  C LEU 145 . C ARG 216 . G LEU 145 G ARG 216 ? ? 
ens_1 d_4 8  C PHE 218 . C PHE 260 . G PHE 218 G PHE 260 ? ? 
ens_1 d_4 9  C GLY 262 . C ASN 331 . G GLY 262 G ASN 331 ? ? 
ens_1 d_4 10 C ASP 334 . C GLY 402 . G ASP 334 G GLY 402 ? ? 
ens_1 d_5 1  A LEU 57  . A ILE 61  . I LEU 57  I ILE 61  ? ? 
ens_1 d_5 2  A GLU 63  . A PHE 103 . I GLU 63  I PHE 103 ? ? 
ens_1 d_5 3  A LYS 105 . A ASP 111 . I LYS 105 I ASP 111 ? ? 
ens_1 d_5 4  A GLY 113 . A THR 126 . I GLY 113 I THR 126 ? ? 
ens_1 d_5 5  A ALA 128 . A GLN 136 . I ALA 128 I GLN 136 ? ? 
ens_1 d_5 6  A LEU 138 . A LYS 143 . I LEU 138 I LYS 143 ? ? 
ens_1 d_5 7  A LEU 145 . A ARG 216 . I LEU 145 I ARG 216 ? ? 
ens_1 d_5 8  A PHE 218 . A PHE 260 . I PHE 218 I PHE 260 ? ? 
ens_1 d_5 9  A GLY 262 . A ASN 331 . I GLY 262 I ASN 331 ? ? 
ens_1 d_5 10 A ASP 334 . A GLY 402 . I ASP 334 I GLY 402 ? ? 
ens_1 d_6 1  K LEU 57  . K ILE 61  . K LEU 57  K ILE 61  ? ? 
ens_1 d_6 2  K GLU 63  . K PHE 103 . K GLU 63  K PHE 103 ? ? 
ens_1 d_6 3  K LYS 105 . K ASP 111 . K LYS 105 K ASP 111 ? ? 
ens_1 d_6 4  K GLY 113 . K THR 126 . K GLY 113 K THR 126 ? ? 
ens_1 d_6 5  K ALA 128 . K GLN 136 . K ALA 128 K GLN 136 ? ? 
ens_1 d_6 6  K LEU 138 . K LYS 143 . K LEU 138 K LYS 143 ? ? 
ens_1 d_6 7  K LEU 145 . K ARG 216 . K LEU 145 K ARG 216 ? ? 
ens_1 d_6 8  K PHE 218 . K PHE 260 . K PHE 218 K PHE 260 ? ? 
ens_1 d_6 9  K GLY 262 . K ASN 331 . K GLY 262 K ASN 331 ? ? 
ens_1 d_6 10 K ASP 334 . K GLY 402 . K ASP 334 K GLY 402 ? ? 
ens_2 d_1 1  H SER 1   . H LEU 34  . D SER 404 D LEU 437 ? ? 
ens_2 d_2 1  F SER 1   . F LEU 34  . B SER 404 B LEU 437 ? ? 
ens_2 d_3 1  J SER 1   . J LEU 34  . F SER 404 F LEU 437 ? ? 
ens_2 d_4 1  D SER 1   . D LEU 34  . H SER 404 H LEU 437 ? ? 
ens_2 d_5 1  B SER 1   . B LEU 34  . J SER 404 J LEU 437 ? ? 
ens_2 d_6 1  L SER 1   . L LEU 34  . L SER 404 L LEU 437 ? ? 
# 
loop_
_struct_ncs_ens.id 
_struct_ncs_ens.details 
ens_1 ? 
ens_2 ? 
# 
loop_
_struct_ncs_ens_gen.ens_id 
_struct_ncs_ens_gen.dom_id_1 
_struct_ncs_ens_gen.dom_id_2 
_struct_ncs_ens_gen.oper_id 
ens_1 d_2 d_1 1  
ens_1 d_3 d_1 2  
ens_1 d_4 d_1 3  
ens_1 d_5 d_1 4  
ens_1 d_6 d_1 5  
ens_2 d_2 d_1 6  
ens_2 d_3 d_1 7  
ens_2 d_4 d_1 8  
ens_2 d_5 d_1 9  
ens_2 d_6 d_1 10 
# 
_struct.entry_id                     8X4S 
_struct.title                        'The L-tryptophan specific decarboxylase PsiD covalent bonding with tryptamine' 
_struct.pdbx_model_details           ? 
_struct.pdbx_formula_weight          ? 
_struct.pdbx_formula_weight_method   ? 
_struct.pdbx_model_type_details      ? 
_struct.pdbx_CASP_flag               N 
# 
_struct_keywords.entry_id        8X4S 
_struct_keywords.text            'decarboxylase, psilocybin, L-tryptophan, psilocin, tryptamine, OXIDOREDUCTASE' 
_struct_keywords.pdbx_keywords   OXIDOREDUCTASE 
# 
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 1 ? 
D  N N 2 ? 
E  N N 1 ? 
F  N N 2 ? 
G  N N 1 ? 
H  N N 2 ? 
I  N N 1 ? 
J  N N 2 ? 
K  N N 1 ? 
L  N N 2 ? 
M  N N 3 ? 
N  N N 3 ? 
O  N N 3 ? 
P  N N 3 ? 
Q  N N 3 ? 
R  N N 3 ? 
S  N N 4 ? 
T  N N 4 ? 
U  N N 4 ? 
V  N N 4 ? 
W  N N 4 ? 
X  N N 4 ? 
Y  N N 4 ? 
Z  N N 4 ? 
AA N N 4 ? 
BA N N 4 ? 
CA N N 4 ? 
DA N N 4 ? 
# 
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 PSID_PSICU P0DPA6 ? 1 
;MQVIPACNSAAIRSLCPTPESFRNMGWLSVSDAVYSEFIGELATRASNRNYSNEFGLMQPIQEFKAFIESDPVVHQEFID
MFEGIQDSPRNYQELCNMFNDIFRKAPVYGDLGPPVYMIMAKLMNTRAGFSAFTRQRLNLHFKKLFDTWGLFLSSKDSRN
VLVADQFDDRHCGWLNERALSAMVKHYNGRAFDEVFLCDKNAPYYGFNSYDDFFNRRFRNRDIDRPVVGGVNNTTLISAA
CESLSYNVSYDVQSLDTLVFKGETYSLKHLLNNDPFTPQFEHGSILQGFLNVTAYHRWHAPVNGTIVKIINVPGTYFAQA
PSTIGDPIPDNDYDPPPYLKSLVYFSNIAARQIMFIEADNKEIGLIFLVFIGMTEISTCEATVSEGQHVNRGDDLGMFHF
GG
;
1   
2 UNP PSID_PSICU P0DPA6 ? 2 SFALGLRKDCRAEIVEKFTEPGTVIRINEVVAALKA 404 
# 
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 8X4S I 1 ? 402 ? P0DPA6 1   ? 402 ? 1   402 
2  2 8X4S J 1 ? 36  ? P0DPA6 404 ? 439 ? 404 439 
3  1 8X4S G 1 ? 402 ? P0DPA6 1   ? 402 ? 1   402 
4  2 8X4S H 1 ? 36  ? P0DPA6 404 ? 439 ? 404 439 
5  1 8X4S A 1 ? 402 ? P0DPA6 1   ? 402 ? 1   402 
6  2 8X4S B 1 ? 36  ? P0DPA6 404 ? 439 ? 404 439 
7  1 8X4S C 1 ? 402 ? P0DPA6 1   ? 402 ? 1   402 
8  2 8X4S D 1 ? 36  ? P0DPA6 404 ? 439 ? 404 439 
9  1 8X4S E 1 ? 402 ? P0DPA6 1   ? 402 ? 1   402 
10 2 8X4S F 1 ? 36  ? P0DPA6 404 ? 439 ? 404 439 
11 1 8X4S K 1 ? 402 ? P0DPA6 1   ? 402 ? 1   402 
12 2 8X4S L 1 ? 36  ? P0DPA6 404 ? 439 ? 404 439 
# 
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 ? dimeric 2 
2 author_defined_assembly ? dimeric 2 
3 author_defined_assembly ? dimeric 2 
4 author_defined_assembly ? dimeric 2 
5 author_defined_assembly ? dimeric 2 
6 author_defined_assembly ? dimeric 2 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,B,M,S,T   
2 1 C,D,N,U,V   
3 1 E,F,O,W,X   
4 1 G,H,P,Y,Z   
5 1 I,J,Q,AA,BA 
6 1 K,L,R,CA,DA 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1   AA1 MET A 58  ? ASP A 71  ? MET I 58  ASP I 71  1 ? 14 
HELX_P HELX_P2   AA2 ASP A 71  ? MET A 81  ? ASP I 71  MET I 81  1 ? 11 
HELX_P HELX_P3   AA3 ASN A 91  ? PHE A 103 ? ASN I 91  PHE I 103 1 ? 13 
HELX_P HELX_P4   AA4 PRO A 114 ? ASN A 125 ? PRO I 114 ASN I 125 1 ? 12 
HELX_P HELX_P5   AA5 THR A 126 ? THR A 134 ? THR I 126 THR I 134 1 ? 9  
HELX_P HELX_P6   AA6 ARG A 135 ? LEU A 153 ? ARG I 135 LEU I 153 1 ? 19 
HELX_P HELX_P7   AA7 SER A 154 ? LEU A 162 ? SER I 154 LEU I 162 5 ? 9  
HELX_P HELX_P8   AA8 ASN A 176 ? VAL A 184 ? ASN I 176 VAL I 184 1 ? 9  
HELX_P HELX_P9   AA9 ALA A 191 ? PHE A 196 ? ALA I 191 PHE I 196 1 ? 6  
HELX_P HELX_P10  AB1 ALA A 202 ? PHE A 207 ? ALA I 202 PHE I 207 5 ? 6  
HELX_P HELX_P11  AB2 SER A 209 ? ASN A 215 ? SER I 209 ASN I 215 1 ? 7  
HELX_P HELX_P12  AB3 ASN A 220 ? ARG A 225 ? ASN I 220 ARG I 225 1 ? 6  
HELX_P HELX_P13  AB4 SER A 266 ? LEU A 271 ? SER I 266 LEU I 271 1 ? 6  
HELX_P HELX_P14  AB5 PHE A 276 ? GLU A 281 ? PHE I 276 GLU I 281 5 ? 6  
HELX_P HELX_P15  AB6 ALA A 320 ? ILE A 324 ? ALA I 320 ILE I 324 5 ? 5  
HELX_P HELX_P16  AB7 PRO A 337 ? LYS A 340 ? PRO I 337 LYS I 340 5 ? 4  
HELX_P HELX_P17  AB8 SER A 341 ? ASN A 347 ? SER I 341 ASN I 347 1 ? 7  
HELX_P HELX_P18  AB9 GLU B 16  ? GLU B 20  ? GLU J 419 GLU J 423 5 ? 5  
HELX_P HELX_P19  AC1 MET C 58  ? ASP C 71  ? MET G 58  ASP G 71  1 ? 14 
HELX_P HELX_P20  AC2 ASP C 71  ? MET C 81  ? ASP G 71  MET G 81  1 ? 11 
HELX_P HELX_P21  AC3 ASN C 91  ? PHE C 103 ? ASN G 91  PHE G 103 1 ? 13 
HELX_P HELX_P22  AC4 PRO C 114 ? ASN C 125 ? PRO G 114 ASN G 125 1 ? 12 
HELX_P HELX_P23  AC5 THR C 126 ? THR C 134 ? THR G 126 THR G 134 1 ? 9  
HELX_P HELX_P24  AC6 ARG C 135 ? LEU C 153 ? ARG G 135 LEU G 153 1 ? 19 
HELX_P HELX_P25  AC7 SER C 154 ? LEU C 162 ? SER G 154 LEU G 162 5 ? 9  
HELX_P HELX_P26  AC8 ASN C 176 ? VAL C 184 ? ASN G 176 VAL G 184 1 ? 9  
HELX_P HELX_P27  AC9 ALA C 191 ? PHE C 196 ? ALA G 191 PHE G 196 1 ? 6  
HELX_P HELX_P28  AD1 ALA C 202 ? PHE C 207 ? ALA G 202 PHE G 207 5 ? 6  
HELX_P HELX_P29  AD2 SER C 209 ? ASN C 215 ? SER G 209 ASN G 215 1 ? 7  
HELX_P HELX_P30  AD3 ASN C 220 ? ARG C 225 ? ASN G 220 ARG G 225 1 ? 6  
HELX_P HELX_P31  AD4 SER C 266 ? LEU C 271 ? SER G 266 LEU G 271 1 ? 6  
HELX_P HELX_P32  AD5 PHE C 276 ? GLU C 281 ? PHE G 276 GLU G 281 5 ? 6  
HELX_P HELX_P33  AD6 ALA C 320 ? ILE C 324 ? ALA G 320 ILE G 324 5 ? 5  
HELX_P HELX_P34  AD7 PRO C 337 ? LYS C 340 ? PRO G 337 LYS G 340 5 ? 4  
HELX_P HELX_P35  AD8 SER C 341 ? ASN C 347 ? SER G 341 ASN G 347 1 ? 7  
HELX_P HELX_P36  AD9 GLU D 16  ? GLU D 20  ? GLU H 419 GLU H 423 5 ? 5  
HELX_P HELX_P37  AE1 MET E 58  ? ASP E 71  ? MET A 58  ASP A 71  1 ? 14 
HELX_P HELX_P38  AE2 ASP E 71  ? MET E 81  ? ASP A 71  MET A 81  1 ? 11 
HELX_P HELX_P39  AE3 ASN E 91  ? PHE E 103 ? ASN A 91  PHE A 103 1 ? 13 
HELX_P HELX_P40  AE4 PRO E 114 ? ASN E 125 ? PRO A 114 ASN A 125 1 ? 12 
HELX_P HELX_P41  AE5 THR E 126 ? THR E 134 ? THR A 126 THR A 134 1 ? 9  
HELX_P HELX_P42  AE6 ARG E 135 ? LEU E 153 ? ARG A 135 LEU A 153 1 ? 19 
HELX_P HELX_P43  AE7 SER E 154 ? LEU E 162 ? SER A 154 LEU A 162 5 ? 9  
HELX_P HELX_P44  AE8 ASN E 176 ? VAL E 184 ? ASN A 176 VAL A 184 1 ? 9  
HELX_P HELX_P45  AE9 ALA E 191 ? PHE E 196 ? ALA A 191 PHE A 196 1 ? 6  
HELX_P HELX_P46  AF1 ALA E 202 ? PHE E 207 ? ALA A 202 PHE A 207 5 ? 6  
HELX_P HELX_P47  AF2 SER E 209 ? ASN E 215 ? SER A 209 ASN A 215 1 ? 7  
HELX_P HELX_P48  AF3 ASN E 220 ? ARG E 225 ? ASN A 220 ARG A 225 1 ? 6  
HELX_P HELX_P49  AF4 SER E 266 ? LEU E 271 ? SER A 266 LEU A 271 1 ? 6  
HELX_P HELX_P50  AF5 PHE E 276 ? GLU E 281 ? PHE A 276 GLU A 281 5 ? 6  
HELX_P HELX_P51  AF6 ALA E 320 ? ILE E 324 ? ALA A 320 ILE A 324 5 ? 5  
HELX_P HELX_P52  AF7 PRO E 337 ? LYS E 340 ? PRO A 337 LYS A 340 5 ? 4  
HELX_P HELX_P53  AF8 SER E 341 ? ASN E 347 ? SER A 341 ASN A 347 1 ? 7  
HELX_P HELX_P54  AF9 GLU F 16  ? GLU F 20  ? GLU B 419 GLU B 423 5 ? 5  
HELX_P HELX_P55  AG1 MET G 58  ? ASP G 71  ? MET C 58  ASP C 71  1 ? 14 
HELX_P HELX_P56  AG2 ASP G 71  ? MET G 81  ? ASP C 71  MET C 81  1 ? 11 
HELX_P HELX_P57  AG3 ASN G 91  ? PHE G 103 ? ASN C 91  PHE C 103 1 ? 13 
HELX_P HELX_P58  AG4 PRO G 114 ? ASN G 125 ? PRO C 114 ASN C 125 1 ? 12 
HELX_P HELX_P59  AG5 THR G 126 ? THR G 134 ? THR C 126 THR C 134 1 ? 9  
HELX_P HELX_P60  AG6 ARG G 135 ? LEU G 153 ? ARG C 135 LEU C 153 1 ? 19 
HELX_P HELX_P61  AG7 SER G 154 ? LEU G 162 ? SER C 154 LEU C 162 5 ? 9  
HELX_P HELX_P62  AG8 ASN G 176 ? VAL G 184 ? ASN C 176 VAL C 184 1 ? 9  
HELX_P HELX_P63  AG9 ALA G 191 ? PHE G 196 ? ALA C 191 PHE C 196 1 ? 6  
HELX_P HELX_P64  AH1 ALA G 202 ? PHE G 207 ? ALA C 202 PHE C 207 5 ? 6  
HELX_P HELX_P65  AH2 SER G 209 ? ASN G 215 ? SER C 209 ASN C 215 1 ? 7  
HELX_P HELX_P66  AH3 ASN G 220 ? ARG G 225 ? ASN C 220 ARG C 225 1 ? 6  
HELX_P HELX_P67  AH4 SER G 266 ? LEU G 271 ? SER C 266 LEU C 271 1 ? 6  
HELX_P HELX_P68  AH5 PHE G 276 ? GLU G 281 ? PHE C 276 GLU C 281 5 ? 6  
HELX_P HELX_P69  AH6 ALA G 320 ? ILE G 324 ? ALA C 320 ILE C 324 5 ? 5  
HELX_P HELX_P70  AH7 PRO G 337 ? LYS G 340 ? PRO C 337 LYS C 340 5 ? 4  
HELX_P HELX_P71  AH8 SER G 341 ? ASN G 347 ? SER C 341 ASN C 347 1 ? 7  
HELX_P HELX_P72  AH9 GLU H 16  ? GLU H 20  ? GLU D 419 GLU D 423 5 ? 5  
HELX_P HELX_P73  AI1 MET I 58  ? ASP I 71  ? MET E 58  ASP E 71  1 ? 14 
HELX_P HELX_P74  AI2 ASP I 71  ? MET I 81  ? ASP E 71  MET E 81  1 ? 11 
HELX_P HELX_P75  AI3 ASN I 91  ? PHE I 103 ? ASN E 91  PHE E 103 1 ? 13 
HELX_P HELX_P76  AI4 PRO I 114 ? ASN I 125 ? PRO E 114 ASN E 125 1 ? 12 
HELX_P HELX_P77  AI5 THR I 126 ? THR I 134 ? THR E 126 THR E 134 1 ? 9  
HELX_P HELX_P78  AI6 ARG I 135 ? LEU I 153 ? ARG E 135 LEU E 153 1 ? 19 
HELX_P HELX_P79  AI7 SER I 154 ? LEU I 162 ? SER E 154 LEU E 162 5 ? 9  
HELX_P HELX_P80  AI8 ASN I 176 ? VAL I 184 ? ASN E 176 VAL E 184 1 ? 9  
HELX_P HELX_P81  AI9 ALA I 191 ? PHE I 196 ? ALA E 191 PHE E 196 1 ? 6  
HELX_P HELX_P82  AJ1 ALA I 202 ? PHE I 207 ? ALA E 202 PHE E 207 5 ? 6  
HELX_P HELX_P83  AJ2 SER I 209 ? ASN I 215 ? SER E 209 ASN E 215 1 ? 7  
HELX_P HELX_P84  AJ3 ASN I 220 ? ARG I 225 ? ASN E 220 ARG E 225 1 ? 6  
HELX_P HELX_P85  AJ4 SER I 266 ? LEU I 271 ? SER E 266 LEU E 271 1 ? 6  
HELX_P HELX_P86  AJ5 PHE I 276 ? GLU I 281 ? PHE E 276 GLU E 281 5 ? 6  
HELX_P HELX_P87  AJ6 ALA I 320 ? ILE I 324 ? ALA E 320 ILE E 324 5 ? 5  
HELX_P HELX_P88  AJ7 PRO I 337 ? LYS I 340 ? PRO E 337 LYS E 340 5 ? 4  
HELX_P HELX_P89  AJ8 SER I 341 ? ASN I 347 ? SER E 341 ASN E 347 1 ? 7  
HELX_P HELX_P90  AJ9 GLU J 16  ? GLU J 20  ? GLU F 419 GLU F 423 5 ? 5  
HELX_P HELX_P91  AK1 MET K 58  ? ASP K 71  ? MET K 58  ASP K 71  1 ? 14 
HELX_P HELX_P92  AK2 ASP K 71  ? MET K 81  ? ASP K 71  MET K 81  1 ? 11 
HELX_P HELX_P93  AK3 ASN K 91  ? PHE K 103 ? ASN K 91  PHE K 103 1 ? 13 
HELX_P HELX_P94  AK4 PRO K 114 ? ASN K 125 ? PRO K 114 ASN K 125 1 ? 12 
HELX_P HELX_P95  AK5 THR K 126 ? THR K 134 ? THR K 126 THR K 134 1 ? 9  
HELX_P HELX_P96  AK6 ARG K 135 ? LEU K 153 ? ARG K 135 LEU K 153 1 ? 19 
HELX_P HELX_P97  AK7 SER K 154 ? LEU K 162 ? SER K 154 LEU K 162 5 ? 9  
HELX_P HELX_P98  AK8 ASN K 176 ? VAL K 184 ? ASN K 176 VAL K 184 1 ? 9  
HELX_P HELX_P99  AK9 ALA K 191 ? PHE K 196 ? ALA K 191 PHE K 196 1 ? 6  
HELX_P HELX_P100 AL1 ALA K 202 ? PHE K 207 ? ALA K 202 PHE K 207 5 ? 6  
HELX_P HELX_P101 AL2 SER K 209 ? ASN K 215 ? SER K 209 ASN K 215 1 ? 7  
HELX_P HELX_P102 AL3 ASN K 220 ? ARG K 225 ? ASN K 220 ARG K 225 1 ? 6  
HELX_P HELX_P103 AL4 SER K 266 ? LEU K 271 ? SER K 266 LEU K 271 1 ? 6  
HELX_P HELX_P104 AL5 PHE K 276 ? GLU K 281 ? PHE K 276 GLU K 281 5 ? 6  
HELX_P HELX_P105 AL6 ALA K 320 ? ILE K 324 ? ALA K 320 ILE K 324 5 ? 5  
HELX_P HELX_P106 AL7 PRO K 337 ? LYS K 340 ? PRO K 337 LYS K 340 5 ? 4  
HELX_P HELX_P107 AL8 SER K 341 ? ASN K 347 ? SER K 341 ASN K 347 1 ? 7  
HELX_P HELX_P108 AL9 GLU L 16  ? GLU L 20  ? GLU L 419 GLU L 423 5 ? 5  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
covale1 covale one ? B SER 1 N ? ? ? 1_555 M A1LWG . C ? ? J SER 404 J A1LWG 501 1_555 ? ? ? ? ? ? ? 1.435 ? ? 
covale2 covale one ? D SER 1 N ? ? ? 1_555 N A1LWG . C ? ? H SER 404 H A1LWG 501 1_555 ? ? ? ? ? ? ? 1.432 ? ? 
covale3 covale one ? F SER 1 N ? ? ? 1_555 O A1LWG . C ? ? B SER 404 B A1LWG 501 1_555 ? ? ? ? ? ? ? 1.431 ? ? 
covale4 covale one ? H SER 1 N ? ? ? 1_555 P A1LWG . C ? ? D SER 404 D A1LWG 501 1_555 ? ? ? ? ? ? ? 1.431 ? ? 
covale5 covale one ? J SER 1 N ? ? ? 1_555 Q A1LWG . C ? ? F SER 404 F A1LWG 501 1_555 ? ? ? ? ? ? ? 1.429 ? ? 
covale6 covale one ? L SER 1 N ? ? ? 1_555 R A1LWG . C ? ? L SER 404 L A1LWG 501 1_555 ? ? ? ? ? ? ? 1.429 ? ? 
# 
_struct_conn_type.id          covale 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_modification_feature.ordinal 
_pdbx_modification_feature.label_comp_id 
_pdbx_modification_feature.label_asym_id 
_pdbx_modification_feature.label_seq_id 
_pdbx_modification_feature.label_alt_id 
_pdbx_modification_feature.modified_residue_label_comp_id 
_pdbx_modification_feature.modified_residue_label_asym_id 
_pdbx_modification_feature.modified_residue_label_seq_id 
_pdbx_modification_feature.modified_residue_label_alt_id 
_pdbx_modification_feature.auth_comp_id 
_pdbx_modification_feature.auth_asym_id 
_pdbx_modification_feature.auth_seq_id 
_pdbx_modification_feature.PDB_ins_code 
_pdbx_modification_feature.symmetry 
_pdbx_modification_feature.modified_residue_auth_comp_id 
_pdbx_modification_feature.modified_residue_auth_asym_id 
_pdbx_modification_feature.modified_residue_auth_seq_id 
_pdbx_modification_feature.modified_residue_PDB_ins_code 
_pdbx_modification_feature.modified_residue_symmetry 
_pdbx_modification_feature.comp_id_linking_atom 
_pdbx_modification_feature.modified_residue_id_linking_atom 
_pdbx_modification_feature.modified_residue_id 
_pdbx_modification_feature.ref_pcm_id 
_pdbx_modification_feature.ref_comp_id 
_pdbx_modification_feature.type 
_pdbx_modification_feature.category 
1 A1LWG M . ? SER B 1 ? A1LWG J 501 ? 1_555 SER J 404 ? 1_555 C N SER 1 A1LWG None 'Covalent chemical modification' 
2 A1LWG N . ? SER D 1 ? A1LWG H 501 ? 1_555 SER H 404 ? 1_555 C N SER 1 A1LWG None 'Covalent chemical modification' 
3 A1LWG O . ? SER F 1 ? A1LWG B 501 ? 1_555 SER B 404 ? 1_555 C N SER 1 A1LWG None 'Covalent chemical modification' 
4 A1LWG P . ? SER H 1 ? A1LWG D 501 ? 1_555 SER D 404 ? 1_555 C N SER 1 A1LWG None 'Covalent chemical modification' 
5 A1LWG Q . ? SER J 1 ? A1LWG F 501 ? 1_555 SER F 404 ? 1_555 C N SER 1 A1LWG None 'Covalent chemical modification' 
6 A1LWG R . ? SER L 1 ? A1LWG L 501 ? 1_555 SER L 404 ? 1_555 C N SER 1 A1LWG None 'Covalent chemical modification' 
# 
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 SER 88 A . ? SER 88 I PRO 89 A ? PRO 89 I 1 2.82 
2 SER 88 C . ? SER 88 G PRO 89 C ? PRO 89 G 1 2.82 
3 SER 88 E . ? SER 88 A PRO 89 E ? PRO 89 A 1 2.82 
4 SER 88 G . ? SER 88 C PRO 89 G ? PRO 89 C 1 2.82 
5 SER 88 I . ? SER 88 E PRO 89 I ? PRO 89 E 1 2.82 
6 SER 88 K . ? SER 88 K PRO 89 K ? PRO 89 K 1 2.82 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 3 ? 
AA2 ? 8 ? 
AA3 ? 3 ? 
AA4 ? 3 ? 
AA5 ? 8 ? 
AA6 ? 3 ? 
AA7 ? 3 ? 
AA8 ? 8 ? 
AA9 ? 3 ? 
AB1 ? 3 ? 
AB2 ? 8 ? 
AB3 ? 3 ? 
AB4 ? 3 ? 
AB5 ? 8 ? 
AB6 ? 3 ? 
AB7 ? 3 ? 
AB8 ? 8 ? 
AB9 ? 3 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA2 5 6 ? anti-parallel 
AA2 6 7 ? anti-parallel 
AA2 7 8 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA5 1 2 ? anti-parallel 
AA5 2 3 ? anti-parallel 
AA5 3 4 ? anti-parallel 
AA5 4 5 ? anti-parallel 
AA5 5 6 ? anti-parallel 
AA5 6 7 ? anti-parallel 
AA5 7 8 ? anti-parallel 
AA6 1 2 ? anti-parallel 
AA6 2 3 ? anti-parallel 
AA7 1 2 ? anti-parallel 
AA7 2 3 ? anti-parallel 
AA8 1 2 ? anti-parallel 
AA8 2 3 ? anti-parallel 
AA8 3 4 ? anti-parallel 
AA8 4 5 ? anti-parallel 
AA8 5 6 ? anti-parallel 
AA8 6 7 ? anti-parallel 
AA8 7 8 ? anti-parallel 
AA9 1 2 ? anti-parallel 
AA9 2 3 ? anti-parallel 
AB1 1 2 ? anti-parallel 
AB1 2 3 ? anti-parallel 
AB2 1 2 ? anti-parallel 
AB2 2 3 ? anti-parallel 
AB2 3 4 ? anti-parallel 
AB2 4 5 ? anti-parallel 
AB2 5 6 ? anti-parallel 
AB2 6 7 ? anti-parallel 
AB2 7 8 ? anti-parallel 
AB3 1 2 ? anti-parallel 
AB3 2 3 ? anti-parallel 
AB4 1 2 ? anti-parallel 
AB4 2 3 ? anti-parallel 
AB5 1 2 ? anti-parallel 
AB5 2 3 ? anti-parallel 
AB5 3 4 ? anti-parallel 
AB5 4 5 ? anti-parallel 
AB5 5 6 ? anti-parallel 
AB5 6 7 ? anti-parallel 
AB5 7 8 ? anti-parallel 
AB6 1 2 ? anti-parallel 
AB6 2 3 ? anti-parallel 
AB7 1 2 ? anti-parallel 
AB7 2 3 ? anti-parallel 
AB8 1 2 ? anti-parallel 
AB8 2 3 ? anti-parallel 
AB8 3 4 ? anti-parallel 
AB8 4 5 ? anti-parallel 
AB8 5 6 ? anti-parallel 
AB8 6 7 ? anti-parallel 
AB8 7 8 ? anti-parallel 
AB9 1 2 ? anti-parallel 
AB9 2 3 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 LEU A 236 ? SER A 238 ? LEU I 236 SER I 238 
AA1 2 VAL B 30  ? ALA B 33  ? VAL J 433 ALA J 436 
AA1 3 GLU B 13  ? ILE B 14  ? GLU J 416 ILE J 417 
AA2 1 HIS A 388 ? VAL A 389 ? HIS I 388 VAL I 389 
AA2 2 GLY A 304 ? VAL A 312 ? GLY I 304 VAL I 312 
AA2 3 ARG A 351 ? ALA A 358 ? ARG I 351 ALA I 358 
AA2 4 LEU A 365 ? ILE A 371 ? LEU I 365 ILE I 371 
AA2 5 PHE B 2   ? LEU B 6   ? PHE J 405 LEU J 409 
AA2 6 SER A 284 ? PHE A 289 ? SER I 284 PHE I 289 
AA2 7 SER A 243 ? SER A 249 ? SER I 243 SER I 249 
AA2 8 VAL B 24  ? ILE B 25  ? VAL J 427 ILE J 428 
AA3 1 ARG A 297 ? HIS A 299 ? ARG I 297 HIS I 299 
AA3 2 ASP A 394 ? HIS A 399 ? ASP I 394 HIS I 399 
AA3 3 THR A 378 ? ALA A 381 ? THR I 378 ALA I 381 
AA4 1 LEU C 236 ? SER C 238 ? LEU G 236 SER G 238 
AA4 2 VAL D 30  ? ALA D 33  ? VAL H 433 ALA H 436 
AA4 3 GLU D 13  ? ILE D 14  ? GLU H 416 ILE H 417 
AA5 1 HIS C 388 ? VAL C 389 ? HIS G 388 VAL G 389 
AA5 2 GLY C 304 ? VAL C 312 ? GLY G 304 VAL G 312 
AA5 3 ARG C 351 ? ALA C 358 ? ARG G 351 ALA G 358 
AA5 4 LEU C 365 ? ILE C 371 ? LEU G 365 ILE G 371 
AA5 5 PHE D 2   ? LEU D 6   ? PHE H 405 LEU H 409 
AA5 6 SER C 284 ? PHE C 289 ? SER G 284 PHE G 289 
AA5 7 SER C 243 ? SER C 249 ? SER G 243 SER G 249 
AA5 8 VAL D 24  ? ILE D 25  ? VAL H 427 ILE H 428 
AA6 1 ARG C 297 ? HIS C 299 ? ARG G 297 HIS G 299 
AA6 2 ASP C 394 ? HIS C 399 ? ASP G 394 HIS G 399 
AA6 3 THR C 378 ? ALA C 381 ? THR G 378 ALA G 381 
AA7 1 LEU E 236 ? SER E 238 ? LEU A 236 SER A 238 
AA7 2 VAL F 30  ? ALA F 33  ? VAL B 433 ALA B 436 
AA7 3 GLU F 13  ? ILE F 14  ? GLU B 416 ILE B 417 
AA8 1 HIS E 388 ? VAL E 389 ? HIS A 388 VAL A 389 
AA8 2 GLY E 304 ? VAL E 312 ? GLY A 304 VAL A 312 
AA8 3 ARG E 351 ? ALA E 358 ? ARG A 351 ALA A 358 
AA8 4 LEU E 365 ? ILE E 371 ? LEU A 365 ILE A 371 
AA8 5 PHE F 2   ? LEU F 6   ? PHE B 405 LEU B 409 
AA8 6 SER E 284 ? PHE E 289 ? SER A 284 PHE A 289 
AA8 7 SER E 243 ? SER E 249 ? SER A 243 SER A 249 
AA8 8 VAL F 24  ? ILE F 25  ? VAL B 427 ILE B 428 
AA9 1 ARG E 297 ? HIS E 299 ? ARG A 297 HIS A 299 
AA9 2 ASP E 394 ? HIS E 399 ? ASP A 394 HIS A 399 
AA9 3 THR E 378 ? ALA E 381 ? THR A 378 ALA A 381 
AB1 1 LEU G 236 ? SER G 238 ? LEU C 236 SER C 238 
AB1 2 VAL H 30  ? ALA H 33  ? VAL D 433 ALA D 436 
AB1 3 GLU H 13  ? ILE H 14  ? GLU D 416 ILE D 417 
AB2 1 HIS G 388 ? VAL G 389 ? HIS C 388 VAL C 389 
AB2 2 GLY G 304 ? VAL G 312 ? GLY C 304 VAL C 312 
AB2 3 ARG G 351 ? ALA G 358 ? ARG C 351 ALA C 358 
AB2 4 LEU G 365 ? ILE G 371 ? LEU C 365 ILE C 371 
AB2 5 PHE H 2   ? LEU H 6   ? PHE D 405 LEU D 409 
AB2 6 SER G 284 ? PHE G 289 ? SER C 284 PHE C 289 
AB2 7 SER G 243 ? SER G 249 ? SER C 243 SER C 249 
AB2 8 VAL H 24  ? ILE H 25  ? VAL D 427 ILE D 428 
AB3 1 ARG G 297 ? HIS G 299 ? ARG C 297 HIS C 299 
AB3 2 ASP G 394 ? HIS G 399 ? ASP C 394 HIS C 399 
AB3 3 THR G 378 ? ALA G 381 ? THR C 378 ALA C 381 
AB4 1 LEU I 236 ? SER I 238 ? LEU E 236 SER E 238 
AB4 2 VAL J 30  ? ALA J 33  ? VAL F 433 ALA F 436 
AB4 3 GLU J 13  ? ILE J 14  ? GLU F 416 ILE F 417 
AB5 1 HIS I 388 ? VAL I 389 ? HIS E 388 VAL E 389 
AB5 2 GLY I 304 ? VAL I 312 ? GLY E 304 VAL E 312 
AB5 3 ARG I 351 ? ALA I 358 ? ARG E 351 ALA E 358 
AB5 4 LEU I 365 ? ILE I 371 ? LEU E 365 ILE E 371 
AB5 5 PHE J 2   ? LEU J 6   ? PHE F 405 LEU F 409 
AB5 6 SER I 284 ? PHE I 289 ? SER E 284 PHE E 289 
AB5 7 SER I 243 ? SER I 249 ? SER E 243 SER E 249 
AB5 8 VAL J 24  ? ILE J 25  ? VAL F 427 ILE F 428 
AB6 1 ARG I 297 ? HIS I 299 ? ARG E 297 HIS E 299 
AB6 2 ASP I 394 ? HIS I 399 ? ASP E 394 HIS E 399 
AB6 3 THR I 378 ? ALA I 381 ? THR E 378 ALA E 381 
AB7 1 LEU K 236 ? SER K 238 ? LEU K 236 SER K 238 
AB7 2 VAL L 30  ? ALA L 33  ? VAL L 433 ALA L 436 
AB7 3 GLU L 13  ? ILE L 14  ? GLU L 416 ILE L 417 
AB8 1 HIS K 388 ? VAL K 389 ? HIS K 388 VAL K 389 
AB8 2 GLY K 304 ? VAL K 312 ? GLY K 304 VAL K 312 
AB8 3 ARG K 351 ? ALA K 358 ? ARG K 351 ALA K 358 
AB8 4 LEU K 365 ? ILE K 371 ? LEU K 365 ILE K 371 
AB8 5 PHE L 2   ? LEU L 6   ? PHE L 405 LEU L 409 
AB8 6 SER K 284 ? PHE K 289 ? SER K 284 PHE K 289 
AB8 7 SER K 243 ? SER K 249 ? SER K 243 SER K 249 
AB8 8 VAL L 24  ? ILE L 25  ? VAL L 427 ILE L 428 
AB9 1 ARG K 297 ? HIS K 299 ? ARG K 297 HIS K 299 
AB9 2 ASP K 394 ? HIS K 399 ? ASP K 394 HIS K 399 
AB9 3 THR K 378 ? ALA K 381 ? THR K 378 ALA K 381 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N ILE A 237 ? N ILE I 237 O ALA B 32  ? O ALA J 435 
AA1 2 3 O ALA B 33  ? O ALA J 436 N GLU B 13  ? N GLU J 416 
AA2 1 2 O VAL A 389 ? O VAL I 389 N GLY A 304 ? N GLY I 304 
AA2 2 3 N VAL A 312 ? N VAL I 312 O ARG A 351 ? O ARG I 351 
AA2 3 4 N MET A 354 ? N MET I 354 O LEU A 368 ? O LEU I 368 
AA2 4 5 N PHE A 367 ? N PHE I 367 O GLY B 5   ? O GLY J 408 
AA2 5 6 O LEU B 4   ? O LEU J 407 N LEU A 286 ? N LEU I 286 
AA2 6 7 O PHE A 289 ? O PHE I 289 N LEU A 244 ? N LEU I 244 
AA2 7 8 N SER A 243 ? N SER I 243 O ILE B 25  ? O ILE J 428 
AA3 1 2 N TRP A 298 ? N TRP I 298 O GLY A 396 ? O GLY I 396 
AA3 2 3 O MET A 397 ? O MET I 397 N GLU A 380 ? N GLU I 380 
AA4 1 2 N ILE C 237 ? N ILE G 237 O ALA D 32  ? O ALA H 435 
AA4 2 3 O ALA D 33  ? O ALA H 436 N GLU D 13  ? N GLU H 416 
AA5 1 2 O VAL C 389 ? O VAL G 389 N GLY C 304 ? N GLY G 304 
AA5 2 3 N VAL C 312 ? N VAL G 312 O ARG C 351 ? O ARG G 351 
AA5 3 4 N MET C 354 ? N MET G 354 O LEU C 368 ? O LEU G 368 
AA5 4 5 N PHE C 367 ? N PHE G 367 O GLY D 5   ? O GLY H 408 
AA5 5 6 O LEU D 6   ? O LEU H 409 N SER C 284 ? N SER G 284 
AA5 6 7 O PHE C 289 ? O PHE G 289 N LEU C 244 ? N LEU G 244 
AA5 7 8 N SER C 243 ? N SER G 243 O ILE D 25  ? O ILE H 428 
AA6 1 2 N TRP C 298 ? N TRP G 298 O GLY C 396 ? O GLY G 396 
AA6 2 3 O MET C 397 ? O MET G 397 N GLU C 380 ? N GLU G 380 
AA7 1 2 N ILE E 237 ? N ILE A 237 O ALA F 32  ? O ALA B 435 
AA7 2 3 O ALA F 33  ? O ALA B 436 N GLU F 13  ? N GLU B 416 
AA8 1 2 O VAL E 389 ? O VAL A 389 N GLY E 304 ? N GLY A 304 
AA8 2 3 N VAL E 312 ? N VAL A 312 O ARG E 351 ? O ARG A 351 
AA8 3 4 N MET E 354 ? N MET A 354 O LEU E 368 ? O LEU A 368 
AA8 4 5 N PHE E 367 ? N PHE A 367 O GLY F 5   ? O GLY B 408 
AA8 5 6 O LEU F 6   ? O LEU B 409 N SER E 284 ? N SER A 284 
AA8 6 7 O PHE E 289 ? O PHE A 289 N LEU E 244 ? N LEU A 244 
AA8 7 8 N SER E 243 ? N SER A 243 O ILE F 25  ? O ILE B 428 
AA9 1 2 N TRP E 298 ? N TRP A 298 O GLY E 396 ? O GLY A 396 
AA9 2 3 O MET E 397 ? O MET A 397 N GLU E 380 ? N GLU A 380 
AB1 1 2 N ILE G 237 ? N ILE C 237 O ALA H 32  ? O ALA D 435 
AB1 2 3 O ALA H 33  ? O ALA D 436 N GLU H 13  ? N GLU D 416 
AB2 1 2 O VAL G 389 ? O VAL C 389 N GLY G 304 ? N GLY C 304 
AB2 2 3 N VAL G 312 ? N VAL C 312 O ARG G 351 ? O ARG C 351 
AB2 3 4 N MET G 354 ? N MET C 354 O LEU G 368 ? O LEU C 368 
AB2 4 5 N PHE G 367 ? N PHE C 367 O GLY H 5   ? O GLY D 408 
AB2 5 6 O LEU H 6   ? O LEU D 409 N SER G 284 ? N SER C 284 
AB2 6 7 O PHE G 289 ? O PHE C 289 N LEU G 244 ? N LEU C 244 
AB2 7 8 N SER G 243 ? N SER C 243 O ILE H 25  ? O ILE D 428 
AB3 1 2 N TRP G 298 ? N TRP C 298 O GLY G 396 ? O GLY C 396 
AB3 2 3 O MET G 397 ? O MET C 397 N GLU G 380 ? N GLU C 380 
AB4 1 2 N ILE I 237 ? N ILE E 237 O ALA J 32  ? O ALA F 435 
AB4 2 3 O ALA J 33  ? O ALA F 436 N GLU J 13  ? N GLU F 416 
AB5 1 2 O VAL I 389 ? O VAL E 389 N GLY I 304 ? N GLY E 304 
AB5 2 3 N VAL I 312 ? N VAL E 312 O ARG I 351 ? O ARG E 351 
AB5 3 4 N MET I 354 ? N MET E 354 O LEU I 368 ? O LEU E 368 
AB5 4 5 N PHE I 367 ? N PHE E 367 O GLY J 5   ? O GLY F 408 
AB5 5 6 O LEU J 4   ? O LEU F 407 N LEU I 286 ? N LEU E 286 
AB5 6 7 O PHE I 289 ? O PHE E 289 N LEU I 244 ? N LEU E 244 
AB5 7 8 N SER I 243 ? N SER E 243 O ILE J 25  ? O ILE F 428 
AB6 1 2 N TRP I 298 ? N TRP E 298 O GLY I 396 ? O GLY E 396 
AB6 2 3 O MET I 397 ? O MET E 397 N GLU I 380 ? N GLU E 380 
AB7 1 2 N ILE K 237 ? N ILE K 237 O ALA L 32  ? O ALA L 435 
AB7 2 3 O ALA L 33  ? O ALA L 436 N GLU L 13  ? N GLU L 416 
AB8 1 2 O VAL K 389 ? O VAL K 389 N GLY K 304 ? N GLY K 304 
AB8 2 3 N VAL K 312 ? N VAL K 312 O ARG K 351 ? O ARG K 351 
AB8 3 4 N MET K 354 ? N MET K 354 O LEU K 368 ? O LEU K 368 
AB8 4 5 N PHE K 367 ? N PHE K 367 O GLY L 5   ? O GLY L 408 
AB8 5 6 O LEU L 4   ? O LEU L 407 N LEU K 286 ? N LEU K 286 
AB8 6 7 O PHE K 289 ? O PHE K 289 N LEU K 244 ? N LEU K 244 
AB8 7 8 N SER K 243 ? N SER K 243 O ILE L 25  ? O ILE L 428 
AB9 1 2 N TRP K 298 ? N TRP K 298 O GLY K 396 ? O GLY K 396 
AB9 2 3 O MET K 397 ? O MET K 397 N GLU K 380 ? N GLU K 380 
# 
_pdbx_entry_details.entry_id                   8X4S 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   Y 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1  1 N   L SER 404 ? ? O L A1LWG 501 ? ? 1.87 
2  1 N   F SER 404 ? ? O F A1LWG 501 ? ? 1.97 
3  1 O   K HIS 186 ? ? O K HOH   501 ? ? 1.99 
4  1 O   C HIS 388 ? ? O C HOH   501 ? ? 2.02 
5  1 N   H SER 404 ? ? O H A1LWG 501 ? ? 2.06 
6  1 N   J SER 404 ? ? O J A1LWG 501 ? ? 2.09 
7  1 O   E PRO 327 ? ? O E HOH   501 ? ? 2.09 
8  1 O   I ARG 190 ? ? O I HOH   501 ? ? 2.11 
9  1 OE1 E GLU 281 ? ? O E HOH   502 ? ? 2.11 
10 1 OD1 K ASN 331 ? ? N K TYR   333 ? ? 2.13 
11 1 O   E ASP 334 ? ? O E HOH   503 ? ? 2.15 
12 1 OD1 A ASP 193 ? ? O A HOH   501 ? ? 2.16 
13 1 OD1 G ASP 193 ? ? O G HOH   501 ? ? 2.18 
14 1 O   E PRO 329 ? ? O E HOH   504 ? ? 2.18 
# 
loop_
_pdbx_validate_symm_contact.id 
_pdbx_validate_symm_contact.PDB_model_num 
_pdbx_validate_symm_contact.auth_atom_id_1 
_pdbx_validate_symm_contact.auth_asym_id_1 
_pdbx_validate_symm_contact.auth_comp_id_1 
_pdbx_validate_symm_contact.auth_seq_id_1 
_pdbx_validate_symm_contact.PDB_ins_code_1 
_pdbx_validate_symm_contact.label_alt_id_1 
_pdbx_validate_symm_contact.site_symmetry_1 
_pdbx_validate_symm_contact.auth_atom_id_2 
_pdbx_validate_symm_contact.auth_asym_id_2 
_pdbx_validate_symm_contact.auth_comp_id_2 
_pdbx_validate_symm_contact.auth_seq_id_2 
_pdbx_validate_symm_contact.PDB_ins_code_2 
_pdbx_validate_symm_contact.label_alt_id_2 
_pdbx_validate_symm_contact.site_symmetry_2 
_pdbx_validate_symm_contact.dist 
1 1 O  A PHE 82  ? ? 1_555 ND2 E ASN 188 ? ? 2_656 2.03 
2 1 NZ I LYS 268 ? ? 1_555 O   A HOH 588 ? ? 2_645 2.04 
3 1 O  A ARG 90  ? ? 1_555 OD1 E ASN 188 ? ? 2_656 2.07 
# 
loop_
_pdbx_validate_rmsd_bond.id 
_pdbx_validate_rmsd_bond.PDB_model_num 
_pdbx_validate_rmsd_bond.auth_atom_id_1 
_pdbx_validate_rmsd_bond.auth_asym_id_1 
_pdbx_validate_rmsd_bond.auth_comp_id_1 
_pdbx_validate_rmsd_bond.auth_seq_id_1 
_pdbx_validate_rmsd_bond.PDB_ins_code_1 
_pdbx_validate_rmsd_bond.label_alt_id_1 
_pdbx_validate_rmsd_bond.auth_atom_id_2 
_pdbx_validate_rmsd_bond.auth_asym_id_2 
_pdbx_validate_rmsd_bond.auth_comp_id_2 
_pdbx_validate_rmsd_bond.auth_seq_id_2 
_pdbx_validate_rmsd_bond.PDB_ins_code_2 
_pdbx_validate_rmsd_bond.label_alt_id_2 
_pdbx_validate_rmsd_bond.bond_value 
_pdbx_validate_rmsd_bond.bond_target_value 
_pdbx_validate_rmsd_bond.bond_deviation 
_pdbx_validate_rmsd_bond.bond_standard_deviation 
_pdbx_validate_rmsd_bond.linker_flag 
1 1 CG A GLU 83  ? ? CD A GLU 83  ? ? 1.632 1.515 0.117 0.015 N 
2 1 CG E GLU 177 ? ? CD E GLU 177 ? ? 1.614 1.515 0.099 0.015 N 
3 1 CB K ASP 330 ? ? CG K ASP 330 ? ? 1.691 1.513 0.178 0.021 N 
# 
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 I LEU 112 ? ? CG I LEU 112 ? ? CD2 I LEU 112 ? ? 99.08  111.00 -11.92 1.70 N 
2 1 CA G GLU 83  ? ? CB G GLU 83  ? ? CG  G GLU 83  ? ? 94.15  113.40 -19.25 2.20 N 
3 1 CB G LEU 112 ? ? CG G LEU 112 ? ? CD2 G LEU 112 ? ? 99.53  111.00 -11.47 1.70 N 
4 1 CB A ASP 330 ? ? CG A ASP 330 ? ? OD2 A ASP 330 ? ? 112.58 118.30 -5.72  0.90 N 
5 1 CB K ASP 330 ? ? CG K ASP 330 ? ? OD2 K ASP 330 ? ? 125.93 118.30 7.63   0.90 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 I 168 ? ? -166.42 -164.85 
2  1 ASN I 220 ? ? -160.50 83.57   
3  1 LEU I 258 ? ? -103.13 68.43   
4  1 ASN I 331 ? ? -126.51 -148.27 
5  1 ASP I 332 ? ? -140.29 -12.01  
6  1 THR I 374 ? ? 39.56   -125.48 
7  1 ASN J 431 ? ? 72.96   -8.59   
8  1 ASP G 168 ? ? -166.42 -164.85 
9  1 ASN G 220 ? ? -160.50 83.57   
10 1 LEU G 258 ? ? -103.13 68.43   
11 1 ASN G 331 ? ? -126.51 -163.36 
12 1 THR G 374 ? ? 39.56   -125.48 
13 1 ASN H 431 ? ? 72.97   -8.59   
14 1 ASP A 168 ? ? -166.42 -164.85 
15 1 ASN A 220 ? ? -160.50 83.57   
16 1 LEU A 258 ? ? -103.13 68.43   
17 1 TYR A 333 ? ? -145.79 -24.20  
18 1 THR A 374 ? ? 39.56   -125.48 
19 1 ASN B 431 ? ? 72.97   -8.59   
20 1 ASP C 168 ? ? -166.42 -164.85 
21 1 ASN C 220 ? ? -160.50 83.57   
22 1 LEU C 258 ? ? -103.13 68.43   
23 1 ASN C 331 ? ? -126.51 -167.88 
24 1 THR C 374 ? ? 39.56   -125.48 
25 1 ASN D 431 ? ? 72.97   -8.59   
26 1 ASP E 168 ? ? -166.42 -164.85 
27 1 ASN E 220 ? ? -160.50 83.57   
28 1 LEU E 258 ? ? -103.13 68.43   
29 1 PHE E 260 ? ? 64.51   -1.33   
30 1 ASN E 331 ? ? -126.51 -160.81 
31 1 THR E 374 ? ? 39.56   -125.48 
32 1 ASN F 431 ? ? 72.97   -8.59   
33 1 ASP K 168 ? ? -166.42 -164.85 
34 1 ASN K 220 ? ? -160.50 83.57   
35 1 LEU K 258 ? ? -103.13 68.43   
36 1 ASN K 331 ? ? -126.51 -168.49 
37 1 THR K 374 ? ? 39.56   -125.48 
38 1 ASN L 431 ? ? 72.97   -8.59   
# 
_pdbx_validate_peptide_omega.id               1 
_pdbx_validate_peptide_omega.PDB_model_num    1 
_pdbx_validate_peptide_omega.auth_comp_id_1   ASN 
_pdbx_validate_peptide_omega.auth_asym_id_1   K 
_pdbx_validate_peptide_omega.auth_seq_id_1    331 
_pdbx_validate_peptide_omega.PDB_ins_code_1   ? 
_pdbx_validate_peptide_omega.label_alt_id_1   ? 
_pdbx_validate_peptide_omega.auth_comp_id_2   ASP 
_pdbx_validate_peptide_omega.auth_asym_id_2   K 
_pdbx_validate_peptide_omega.auth_seq_id_2    332 
_pdbx_validate_peptide_omega.PDB_ins_code_2   ? 
_pdbx_validate_peptide_omega.label_alt_id_2   ? 
_pdbx_validate_peptide_omega.omega            148.38 
# 
loop_
_pdbx_validate_planes.id 
_pdbx_validate_planes.PDB_model_num 
_pdbx_validate_planes.auth_comp_id 
_pdbx_validate_planes.auth_asym_id 
_pdbx_validate_planes.auth_seq_id 
_pdbx_validate_planes.PDB_ins_code 
_pdbx_validate_planes.label_alt_id 
_pdbx_validate_planes.rmsd 
_pdbx_validate_planes.type 
1 1 ARG A 90  ? ? 0.103 'SIDE CHAIN' 
2 1 ARG K 178 ? ? 0.152 'SIDE CHAIN' 
# 
loop_
_pdbx_validate_main_chain_plane.id 
_pdbx_validate_main_chain_plane.PDB_model_num 
_pdbx_validate_main_chain_plane.auth_comp_id 
_pdbx_validate_main_chain_plane.auth_asym_id 
_pdbx_validate_main_chain_plane.auth_seq_id 
_pdbx_validate_main_chain_plane.PDB_ins_code 
_pdbx_validate_main_chain_plane.label_alt_id 
_pdbx_validate_main_chain_plane.improper_torsion_angle 
1 1 ASN I 331 ? ? -10.37 
2 1 ASN A 331 ? ? 12.14  
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1 x,y,z       
2 -x,y+1/2,-z 
# 
_pdbx_refine_tls.id               1 
_pdbx_refine_tls.pdbx_refine_id   'X-RAY DIFFRACTION' 
_pdbx_refine_tls.details          ? 
_pdbx_refine_tls.method           refined 
_pdbx_refine_tls.origin_x         23.7140437583 
_pdbx_refine_tls.origin_y         24.3759248216 
_pdbx_refine_tls.origin_z         19.381366769 
_pdbx_refine_tls.T[1][1]          0.232220725106 
_pdbx_refine_tls.T[1][1]_esd      ? 
_pdbx_refine_tls.T[1][2]          -0.0144692934102 
_pdbx_refine_tls.T[1][2]_esd      ? 
_pdbx_refine_tls.T[1][3]          -0.00391429638208 
_pdbx_refine_tls.T[1][3]_esd      ? 
_pdbx_refine_tls.T[2][2]          0.240280103686 
_pdbx_refine_tls.T[2][2]_esd      ? 
_pdbx_refine_tls.T[2][3]          0.0122000842131 
_pdbx_refine_tls.T[2][3]_esd      ? 
_pdbx_refine_tls.T[3][3]          0.232007511697 
_pdbx_refine_tls.T[3][3]_esd      ? 
_pdbx_refine_tls.L[1][1]          0.0134845706741 
_pdbx_refine_tls.L[1][1]_esd      ? 
_pdbx_refine_tls.L[1][2]          -0.0113645953237 
_pdbx_refine_tls.L[1][2]_esd      ? 
_pdbx_refine_tls.L[1][3]          -0.00831635858761 
_pdbx_refine_tls.L[1][3]_esd      ? 
_pdbx_refine_tls.L[2][2]          0.0128966598721 
_pdbx_refine_tls.L[2][2]_esd      ? 
_pdbx_refine_tls.L[2][3]          0.0230226598027 
_pdbx_refine_tls.L[2][3]_esd      ? 
_pdbx_refine_tls.L[3][3]          -0.0474028397624 
_pdbx_refine_tls.L[3][3]_esd      ? 
_pdbx_refine_tls.S[1][1]          0.0135591257637 
_pdbx_refine_tls.S[1][1]_esd      ? 
_pdbx_refine_tls.S[1][2]          0.00554917528998 
_pdbx_refine_tls.S[1][2]_esd      ? 
_pdbx_refine_tls.S[1][3]          0.0176979204182 
_pdbx_refine_tls.S[1][3]_esd      ? 
_pdbx_refine_tls.S[2][1]          0.0128198973227 
_pdbx_refine_tls.S[2][1]_esd      ? 
_pdbx_refine_tls.S[2][2]          -0.0316089131456 
_pdbx_refine_tls.S[2][2]_esd      ? 
_pdbx_refine_tls.S[2][3]          -0.0180080799139 
_pdbx_refine_tls.S[2][3]_esd      ? 
_pdbx_refine_tls.S[3][1]          0.0264387952557 
_pdbx_refine_tls.S[3][1]_esd      ? 
_pdbx_refine_tls.S[3][2]          0.00623527539133 
_pdbx_refine_tls.S[3][2]_esd      ? 
_pdbx_refine_tls.S[3][3]          0.00288140723511 
_pdbx_refine_tls.S[3][3]_esd      ? 
# 
_pdbx_refine_tls_group.id                  1 
_pdbx_refine_tls_group.pdbx_refine_id      'X-RAY DIFFRACTION' 
_pdbx_refine_tls_group.refine_tls_id       1 
_pdbx_refine_tls_group.beg_label_asym_id   A 
_pdbx_refine_tls_group.beg_label_seq_id    1 
_pdbx_refine_tls_group.beg_auth_asym_id    I 
_pdbx_refine_tls_group.beg_auth_seq_id     57 
_pdbx_refine_tls_group.beg_PDB_ins_code    ? 
_pdbx_refine_tls_group.end_label_asym_id   R 
_pdbx_refine_tls_group.end_label_seq_id    1 
_pdbx_refine_tls_group.end_auth_asym_id    L 
_pdbx_refine_tls_group.end_auth_seq_id     403 
_pdbx_refine_tls_group.end_PDB_ins_code    ? 
_pdbx_refine_tls_group.selection           ? 
_pdbx_refine_tls_group.selection_details   all 
# 
_pdbx_distant_solvent_atoms.id                                1 
_pdbx_distant_solvent_atoms.PDB_model_num                     1 
_pdbx_distant_solvent_atoms.auth_atom_id                      O 
_pdbx_distant_solvent_atoms.label_alt_id                      ? 
_pdbx_distant_solvent_atoms.auth_asym_id                      G 
_pdbx_distant_solvent_atoms.auth_comp_id                      HOH 
_pdbx_distant_solvent_atoms.auth_seq_id                       599 
_pdbx_distant_solvent_atoms.PDB_ins_code                      ? 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance   6.25 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance          . 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1   1 Y 1 I MET 1   ? A MET 1  
2   1 Y 1 I GLN 2   ? A GLN 2  
3   1 Y 1 I VAL 3   ? A VAL 3  
4   1 Y 1 I ILE 4   ? A ILE 4  
5   1 Y 1 I PRO 5   ? A PRO 5  
6   1 Y 1 I ALA 6   ? A ALA 6  
7   1 Y 1 I CYS 7   ? A CYS 7  
8   1 Y 1 I ASN 8   ? A ASN 8  
9   1 Y 1 I SER 9   ? A SER 9  
10  1 Y 1 I ALA 10  ? A ALA 10 
11  1 Y 1 I ALA 11  ? A ALA 11 
12  1 Y 1 I ILE 12  ? A ILE 12 
13  1 Y 1 I ARG 13  ? A ARG 13 
14  1 Y 1 I SER 14  ? A SER 14 
15  1 Y 1 I LEU 15  ? A LEU 15 
16  1 Y 1 I CYS 16  ? A CYS 16 
17  1 Y 1 I PRO 17  ? A PRO 17 
18  1 Y 1 I THR 18  ? A THR 18 
19  1 Y 1 I PRO 19  ? A PRO 19 
20  1 Y 1 I GLU 20  ? A GLU 20 
21  1 Y 1 I SER 21  ? A SER 21 
22  1 Y 1 I PHE 22  ? A PHE 22 
23  1 Y 1 I ARG 23  ? A ARG 23 
24  1 Y 1 I ASN 24  ? A ASN 24 
25  1 Y 1 I MET 25  ? A MET 25 
26  1 Y 1 I GLY 26  ? A GLY 26 
27  1 Y 1 I TRP 27  ? A TRP 27 
28  1 Y 1 I LEU 28  ? A LEU 28 
29  1 Y 1 I SER 29  ? A SER 29 
30  1 Y 1 I VAL 30  ? A VAL 30 
31  1 Y 1 I SER 31  ? A SER 31 
32  1 Y 1 I ASP 32  ? A ASP 32 
33  1 Y 1 I ALA 33  ? A ALA 33 
34  1 Y 1 I VAL 34  ? A VAL 34 
35  1 Y 1 I TYR 35  ? A TYR 35 
36  1 Y 1 I SER 36  ? A SER 36 
37  1 Y 1 I GLU 37  ? A GLU 37 
38  1 Y 1 I PHE 38  ? A PHE 38 
39  1 Y 1 I ILE 39  ? A ILE 39 
40  1 Y 1 I GLY 40  ? A GLY 40 
41  1 Y 1 I GLU 41  ? A GLU 41 
42  1 Y 1 I LEU 42  ? A LEU 42 
43  1 Y 1 I ALA 43  ? A ALA 43 
44  1 Y 1 I THR 44  ? A THR 44 
45  1 Y 1 I ARG 45  ? A ARG 45 
46  1 Y 1 I ALA 46  ? A ALA 46 
47  1 Y 1 I SER 47  ? A SER 47 
48  1 Y 1 I ASN 48  ? A ASN 48 
49  1 Y 1 I ARG 49  ? A ARG 49 
50  1 Y 1 I ASN 50  ? A ASN 50 
51  1 Y 1 I TYR 51  ? A TYR 51 
52  1 Y 1 I SER 52  ? A SER 52 
53  1 Y 1 I ASN 53  ? A ASN 53 
54  1 Y 1 I GLU 54  ? A GLU 54 
55  1 Y 1 I PHE 55  ? A PHE 55 
56  1 Y 1 I GLY 56  ? A GLY 56 
57  1 Y 1 J LYS 438 ? B LYS 35 
58  1 Y 1 J ALA 439 ? B ALA 36 
59  1 Y 1 G MET 1   ? C MET 1  
60  1 Y 1 G GLN 2   ? C GLN 2  
61  1 Y 1 G VAL 3   ? C VAL 3  
62  1 Y 1 G ILE 4   ? C ILE 4  
63  1 Y 1 G PRO 5   ? C PRO 5  
64  1 Y 1 G ALA 6   ? C ALA 6  
65  1 Y 1 G CYS 7   ? C CYS 7  
66  1 Y 1 G ASN 8   ? C ASN 8  
67  1 Y 1 G SER 9   ? C SER 9  
68  1 Y 1 G ALA 10  ? C ALA 10 
69  1 Y 1 G ALA 11  ? C ALA 11 
70  1 Y 1 G ILE 12  ? C ILE 12 
71  1 Y 1 G ARG 13  ? C ARG 13 
72  1 Y 1 G SER 14  ? C SER 14 
73  1 Y 1 G LEU 15  ? C LEU 15 
74  1 Y 1 G CYS 16  ? C CYS 16 
75  1 Y 1 G PRO 17  ? C PRO 17 
76  1 Y 1 G THR 18  ? C THR 18 
77  1 Y 1 G PRO 19  ? C PRO 19 
78  1 Y 1 G GLU 20  ? C GLU 20 
79  1 Y 1 G SER 21  ? C SER 21 
80  1 Y 1 G PHE 22  ? C PHE 22 
81  1 Y 1 G ARG 23  ? C ARG 23 
82  1 Y 1 G ASN 24  ? C ASN 24 
83  1 Y 1 G MET 25  ? C MET 25 
84  1 Y 1 G GLY 26  ? C GLY 26 
85  1 Y 1 G TRP 27  ? C TRP 27 
86  1 Y 1 G LEU 28  ? C LEU 28 
87  1 Y 1 G SER 29  ? C SER 29 
88  1 Y 1 G VAL 30  ? C VAL 30 
89  1 Y 1 G SER 31  ? C SER 31 
90  1 Y 1 G ASP 32  ? C ASP 32 
91  1 Y 1 G ALA 33  ? C ALA 33 
92  1 Y 1 G VAL 34  ? C VAL 34 
93  1 Y 1 G TYR 35  ? C TYR 35 
94  1 Y 1 G SER 36  ? C SER 36 
95  1 Y 1 G GLU 37  ? C GLU 37 
96  1 Y 1 G PHE 38  ? C PHE 38 
97  1 Y 1 G ILE 39  ? C ILE 39 
98  1 Y 1 G GLY 40  ? C GLY 40 
99  1 Y 1 G GLU 41  ? C GLU 41 
100 1 Y 1 G LEU 42  ? C LEU 42 
101 1 Y 1 G ALA 43  ? C ALA 43 
102 1 Y 1 G THR 44  ? C THR 44 
103 1 Y 1 G ARG 45  ? C ARG 45 
104 1 Y 1 G ALA 46  ? C ALA 46 
105 1 Y 1 G SER 47  ? C SER 47 
106 1 Y 1 G ASN 48  ? C ASN 48 
107 1 Y 1 G ARG 49  ? C ARG 49 
108 1 Y 1 G ASN 50  ? C ASN 50 
109 1 Y 1 G TYR 51  ? C TYR 51 
110 1 Y 1 G SER 52  ? C SER 52 
111 1 Y 1 G ASN 53  ? C ASN 53 
112 1 Y 1 G GLU 54  ? C GLU 54 
113 1 Y 1 G PHE 55  ? C PHE 55 
114 1 Y 1 G GLY 56  ? C GLY 56 
115 1 Y 1 H LYS 438 ? D LYS 35 
116 1 Y 1 H ALA 439 ? D ALA 36 
117 1 Y 1 A MET 1   ? E MET 1  
118 1 Y 1 A GLN 2   ? E GLN 2  
119 1 Y 1 A VAL 3   ? E VAL 3  
120 1 Y 1 A ILE 4   ? E ILE 4  
121 1 Y 1 A PRO 5   ? E PRO 5  
122 1 Y 1 A ALA 6   ? E ALA 6  
123 1 Y 1 A CYS 7   ? E CYS 7  
124 1 Y 1 A ASN 8   ? E ASN 8  
125 1 Y 1 A SER 9   ? E SER 9  
126 1 Y 1 A ALA 10  ? E ALA 10 
127 1 Y 1 A ALA 11  ? E ALA 11 
128 1 Y 1 A ILE 12  ? E ILE 12 
129 1 Y 1 A ARG 13  ? E ARG 13 
130 1 Y 1 A SER 14  ? E SER 14 
131 1 Y 1 A LEU 15  ? E LEU 15 
132 1 Y 1 A CYS 16  ? E CYS 16 
133 1 Y 1 A PRO 17  ? E PRO 17 
134 1 Y 1 A THR 18  ? E THR 18 
135 1 Y 1 A PRO 19  ? E PRO 19 
136 1 Y 1 A GLU 20  ? E GLU 20 
137 1 Y 1 A SER 21  ? E SER 21 
138 1 Y 1 A PHE 22  ? E PHE 22 
139 1 Y 1 A ARG 23  ? E ARG 23 
140 1 Y 1 A ASN 24  ? E ASN 24 
141 1 Y 1 A MET 25  ? E MET 25 
142 1 Y 1 A GLY 26  ? E GLY 26 
143 1 Y 1 A TRP 27  ? E TRP 27 
144 1 Y 1 A LEU 28  ? E LEU 28 
145 1 Y 1 A SER 29  ? E SER 29 
146 1 Y 1 A VAL 30  ? E VAL 30 
147 1 Y 1 A SER 31  ? E SER 31 
148 1 Y 1 A ASP 32  ? E ASP 32 
149 1 Y 1 A ALA 33  ? E ALA 33 
150 1 Y 1 A VAL 34  ? E VAL 34 
151 1 Y 1 A TYR 35  ? E TYR 35 
152 1 Y 1 A SER 36  ? E SER 36 
153 1 Y 1 A GLU 37  ? E GLU 37 
154 1 Y 1 A PHE 38  ? E PHE 38 
155 1 Y 1 A ILE 39  ? E ILE 39 
156 1 Y 1 A GLY 40  ? E GLY 40 
157 1 Y 1 A GLU 41  ? E GLU 41 
158 1 Y 1 A LEU 42  ? E LEU 42 
159 1 Y 1 A ALA 43  ? E ALA 43 
160 1 Y 1 A THR 44  ? E THR 44 
161 1 Y 1 A ARG 45  ? E ARG 45 
162 1 Y 1 A ALA 46  ? E ALA 46 
163 1 Y 1 A SER 47  ? E SER 47 
164 1 Y 1 A ASN 48  ? E ASN 48 
165 1 Y 1 A ARG 49  ? E ARG 49 
166 1 Y 1 A ASN 50  ? E ASN 50 
167 1 Y 1 A TYR 51  ? E TYR 51 
168 1 Y 1 A SER 52  ? E SER 52 
169 1 Y 1 B LYS 438 ? F LYS 35 
170 1 Y 1 B ALA 439 ? F ALA 36 
171 1 Y 1 C MET 1   ? G MET 1  
172 1 Y 1 C GLN 2   ? G GLN 2  
173 1 Y 1 C VAL 3   ? G VAL 3  
174 1 Y 1 C ILE 4   ? G ILE 4  
175 1 Y 1 C PRO 5   ? G PRO 5  
176 1 Y 1 C ALA 6   ? G ALA 6  
177 1 Y 1 C CYS 7   ? G CYS 7  
178 1 Y 1 C ASN 8   ? G ASN 8  
179 1 Y 1 C SER 9   ? G SER 9  
180 1 Y 1 C ALA 10  ? G ALA 10 
181 1 Y 1 C ALA 11  ? G ALA 11 
182 1 Y 1 C ILE 12  ? G ILE 12 
183 1 Y 1 C ARG 13  ? G ARG 13 
184 1 Y 1 C SER 14  ? G SER 14 
185 1 Y 1 C LEU 15  ? G LEU 15 
186 1 Y 1 C CYS 16  ? G CYS 16 
187 1 Y 1 C PRO 17  ? G PRO 17 
188 1 Y 1 C THR 18  ? G THR 18 
189 1 Y 1 C PRO 19  ? G PRO 19 
190 1 Y 1 C GLU 20  ? G GLU 20 
191 1 Y 1 C SER 21  ? G SER 21 
192 1 Y 1 C PHE 22  ? G PHE 22 
193 1 Y 1 C ARG 23  ? G ARG 23 
194 1 Y 1 C ASN 24  ? G ASN 24 
195 1 Y 1 C MET 25  ? G MET 25 
196 1 Y 1 C GLY 26  ? G GLY 26 
197 1 Y 1 C TRP 27  ? G TRP 27 
198 1 Y 1 C LEU 28  ? G LEU 28 
199 1 Y 1 C SER 29  ? G SER 29 
200 1 Y 1 C VAL 30  ? G VAL 30 
201 1 Y 1 C SER 31  ? G SER 31 
202 1 Y 1 C ASP 32  ? G ASP 32 
203 1 Y 1 C ALA 33  ? G ALA 33 
204 1 Y 1 C VAL 34  ? G VAL 34 
205 1 Y 1 C TYR 35  ? G TYR 35 
206 1 Y 1 C SER 36  ? G SER 36 
207 1 Y 1 C GLU 37  ? G GLU 37 
208 1 Y 1 C PHE 38  ? G PHE 38 
209 1 Y 1 C ILE 39  ? G ILE 39 
210 1 Y 1 C GLY 40  ? G GLY 40 
211 1 Y 1 C GLU 41  ? G GLU 41 
212 1 Y 1 C LEU 42  ? G LEU 42 
213 1 Y 1 C ALA 43  ? G ALA 43 
214 1 Y 1 C THR 44  ? G THR 44 
215 1 Y 1 C ARG 45  ? G ARG 45 
216 1 Y 1 C ALA 46  ? G ALA 46 
217 1 Y 1 C SER 47  ? G SER 47 
218 1 Y 1 C ASN 48  ? G ASN 48 
219 1 Y 1 C ARG 49  ? G ARG 49 
220 1 Y 1 C ASN 50  ? G ASN 50 
221 1 Y 1 C TYR 51  ? G TYR 51 
222 1 Y 1 C SER 52  ? G SER 52 
223 1 Y 1 C ASN 53  ? G ASN 53 
224 1 Y 1 C GLU 54  ? G GLU 54 
225 1 Y 1 C PHE 55  ? G PHE 55 
226 1 Y 1 C GLY 56  ? G GLY 56 
227 1 Y 1 D LYS 438 ? H LYS 35 
228 1 Y 1 D ALA 439 ? H ALA 36 
229 1 Y 1 E MET 1   ? I MET 1  
230 1 Y 1 E GLN 2   ? I GLN 2  
231 1 Y 1 E VAL 3   ? I VAL 3  
232 1 Y 1 E ILE 4   ? I ILE 4  
233 1 Y 1 E PRO 5   ? I PRO 5  
234 1 Y 1 E ALA 6   ? I ALA 6  
235 1 Y 1 E CYS 7   ? I CYS 7  
236 1 Y 1 E ASN 8   ? I ASN 8  
237 1 Y 1 E SER 9   ? I SER 9  
238 1 Y 1 E ALA 10  ? I ALA 10 
239 1 Y 1 E ALA 11  ? I ALA 11 
240 1 Y 1 E ILE 12  ? I ILE 12 
241 1 Y 1 E ARG 13  ? I ARG 13 
242 1 Y 1 E SER 14  ? I SER 14 
243 1 Y 1 E LEU 15  ? I LEU 15 
244 1 Y 1 E CYS 16  ? I CYS 16 
245 1 Y 1 E PRO 17  ? I PRO 17 
246 1 Y 1 E THR 18  ? I THR 18 
247 1 Y 1 E PRO 19  ? I PRO 19 
248 1 Y 1 E GLU 20  ? I GLU 20 
249 1 Y 1 E SER 21  ? I SER 21 
250 1 Y 1 E PHE 22  ? I PHE 22 
251 1 Y 1 E ARG 23  ? I ARG 23 
252 1 Y 1 E ASN 24  ? I ASN 24 
253 1 Y 1 E MET 25  ? I MET 25 
254 1 Y 1 E GLY 26  ? I GLY 26 
255 1 Y 1 E TRP 27  ? I TRP 27 
256 1 Y 1 E LEU 28  ? I LEU 28 
257 1 Y 1 E SER 29  ? I SER 29 
258 1 Y 1 E VAL 30  ? I VAL 30 
259 1 Y 1 E SER 31  ? I SER 31 
260 1 Y 1 E ASP 32  ? I ASP 32 
261 1 Y 1 E ALA 33  ? I ALA 33 
262 1 Y 1 E VAL 34  ? I VAL 34 
263 1 Y 1 E TYR 35  ? I TYR 35 
264 1 Y 1 E SER 36  ? I SER 36 
265 1 Y 1 E GLU 37  ? I GLU 37 
266 1 Y 1 E PHE 38  ? I PHE 38 
267 1 Y 1 E ILE 39  ? I ILE 39 
268 1 Y 1 E GLY 40  ? I GLY 40 
269 1 Y 1 E GLU 41  ? I GLU 41 
270 1 Y 1 E LEU 42  ? I LEU 42 
271 1 Y 1 E ALA 43  ? I ALA 43 
272 1 Y 1 E THR 44  ? I THR 44 
273 1 Y 1 E ARG 45  ? I ARG 45 
274 1 Y 1 E ALA 46  ? I ALA 46 
275 1 Y 1 E SER 47  ? I SER 47 
276 1 Y 1 E ASN 48  ? I ASN 48 
277 1 Y 1 E ARG 49  ? I ARG 49 
278 1 Y 1 E ASN 50  ? I ASN 50 
279 1 Y 1 E TYR 51  ? I TYR 51 
280 1 Y 1 E SER 52  ? I SER 52 
281 1 Y 1 E ASN 53  ? I ASN 53 
282 1 Y 1 E GLU 54  ? I GLU 54 
283 1 Y 1 E PHE 55  ? I PHE 55 
284 1 Y 1 E GLY 56  ? I GLY 56 
285 1 Y 1 F LYS 438 ? J LYS 35 
286 1 Y 1 F ALA 439 ? J ALA 36 
287 1 Y 1 K MET 1   ? K MET 1  
288 1 Y 1 K GLN 2   ? K GLN 2  
289 1 Y 1 K VAL 3   ? K VAL 3  
290 1 Y 1 K ILE 4   ? K ILE 4  
291 1 Y 1 K PRO 5   ? K PRO 5  
292 1 Y 1 K ALA 6   ? K ALA 6  
293 1 Y 1 K CYS 7   ? K CYS 7  
294 1 Y 1 K ASN 8   ? K ASN 8  
295 1 Y 1 K SER 9   ? K SER 9  
296 1 Y 1 K ALA 10  ? K ALA 10 
297 1 Y 1 K ALA 11  ? K ALA 11 
298 1 Y 1 K ILE 12  ? K ILE 12 
299 1 Y 1 K ARG 13  ? K ARG 13 
300 1 Y 1 K SER 14  ? K SER 14 
301 1 Y 1 K LEU 15  ? K LEU 15 
302 1 Y 1 K CYS 16  ? K CYS 16 
303 1 Y 1 K PRO 17  ? K PRO 17 
304 1 Y 1 K THR 18  ? K THR 18 
305 1 Y 1 K PRO 19  ? K PRO 19 
306 1 Y 1 K GLU 20  ? K GLU 20 
307 1 Y 1 K SER 21  ? K SER 21 
308 1 Y 1 K PHE 22  ? K PHE 22 
309 1 Y 1 K ARG 23  ? K ARG 23 
310 1 Y 1 K ASN 24  ? K ASN 24 
311 1 Y 1 K MET 25  ? K MET 25 
312 1 Y 1 K GLY 26  ? K GLY 26 
313 1 Y 1 K TRP 27  ? K TRP 27 
314 1 Y 1 K LEU 28  ? K LEU 28 
315 1 Y 1 K SER 29  ? K SER 29 
316 1 Y 1 K VAL 30  ? K VAL 30 
317 1 Y 1 K SER 31  ? K SER 31 
318 1 Y 1 K ASP 32  ? K ASP 32 
319 1 Y 1 K ALA 33  ? K ALA 33 
320 1 Y 1 K VAL 34  ? K VAL 34 
321 1 Y 1 K TYR 35  ? K TYR 35 
322 1 Y 1 K SER 36  ? K SER 36 
323 1 Y 1 K GLU 37  ? K GLU 37 
324 1 Y 1 K PHE 38  ? K PHE 38 
325 1 Y 1 K ILE 39  ? K ILE 39 
326 1 Y 1 K GLY 40  ? K GLY 40 
327 1 Y 1 K GLU 41  ? K GLU 41 
328 1 Y 1 K LEU 42  ? K LEU 42 
329 1 Y 1 K ALA 43  ? K ALA 43 
330 1 Y 1 K THR 44  ? K THR 44 
331 1 Y 1 K ARG 45  ? K ARG 45 
332 1 Y 1 K ALA 46  ? K ALA 46 
333 1 Y 1 K SER 47  ? K SER 47 
334 1 Y 1 K ASN 48  ? K ASN 48 
335 1 Y 1 K ARG 49  ? K ARG 49 
336 1 Y 1 K ASN 50  ? K ASN 50 
337 1 Y 1 K TYR 51  ? K TYR 51 
338 1 Y 1 K SER 52  ? K SER 52 
339 1 Y 1 K ASN 53  ? K ASN 53 
340 1 Y 1 K GLU 54  ? K GLU 54 
341 1 Y 1 K PHE 55  ? K PHE 55 
342 1 Y 1 L LYS 438 ? L LYS 35 
343 1 Y 1 L ALA 439 ? L ALA 36 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
A1LWG C    C N N 1   
A1LWG CA   C N R 2   
A1LWG CB   C N N 3   
A1LWG C06  C N N 4   
A1LWG C07  C N N 5   
A1LWG C08  C Y N 6   
A1LWG C09  C Y N 7   
A1LWG C11  C Y N 8   
A1LWG C12  C Y N 9   
A1LWG C13  C Y N 10  
A1LWG C14  C Y N 11  
A1LWG C15  C Y N 12  
A1LWG C16  C Y N 13  
A1LWG N    N N N 14  
A1LWG N10  N Y N 15  
A1LWG O    O N N 16  
A1LWG H031 H N N 17  
A1LWG H043 H N N 18  
A1LWG H042 H N N 19  
A1LWG H041 H N N 20  
A1LWG H062 H N N 21  
A1LWG H061 H N N 22  
A1LWG H071 H N N 23  
A1LWG H072 H N N 24  
A1LWG H091 H N N 25  
A1LWG H131 H N N 26  
A1LWG H141 H N N 27  
A1LWG H151 H N N 28  
A1LWG H161 H N N 29  
A1LWG H051 H N N 30  
A1LWG H101 H N N 31  
A1LWG OXT  O N N 32  
A1LWG H1   H N N 33  
ALA   N    N N N 34  
ALA   CA   C N S 35  
ALA   C    C N N 36  
ALA   O    O N N 37  
ALA   CB   C N N 38  
ALA   OXT  O N N 39  
ALA   H    H N N 40  
ALA   H2   H N N 41  
ALA   HA   H N N 42  
ALA   HB1  H N N 43  
ALA   HB2  H N N 44  
ALA   HB3  H N N 45  
ALA   HXT  H N N 46  
ARG   N    N N N 47  
ARG   CA   C N S 48  
ARG   C    C N N 49  
ARG   O    O N N 50  
ARG   CB   C N N 51  
ARG   CG   C N N 52  
ARG   CD   C N N 53  
ARG   NE   N N N 54  
ARG   CZ   C N N 55  
ARG   NH1  N N N 56  
ARG   NH2  N N N 57  
ARG   OXT  O N N 58  
ARG   H    H N N 59  
ARG   H2   H N N 60  
ARG   HA   H N N 61  
ARG   HB2  H N N 62  
ARG   HB3  H N N 63  
ARG   HG2  H N N 64  
ARG   HG3  H N N 65  
ARG   HD2  H N N 66  
ARG   HD3  H N N 67  
ARG   HE   H N N 68  
ARG   HH11 H N N 69  
ARG   HH12 H N N 70  
ARG   HH21 H N N 71  
ARG   HH22 H N N 72  
ARG   HXT  H N N 73  
ASN   N    N N N 74  
ASN   CA   C N S 75  
ASN   C    C N N 76  
ASN   O    O N N 77  
ASN   CB   C N N 78  
ASN   CG   C N N 79  
ASN   OD1  O N N 80  
ASN   ND2  N N N 81  
ASN   OXT  O N N 82  
ASN   H    H N N 83  
ASN   H2   H N N 84  
ASN   HA   H N N 85  
ASN   HB2  H N N 86  
ASN   HB3  H N N 87  
ASN   HD21 H N N 88  
ASN   HD22 H N N 89  
ASN   HXT  H N N 90  
ASP   N    N N N 91  
ASP   CA   C N S 92  
ASP   C    C N N 93  
ASP   O    O N N 94  
ASP   CB   C N N 95  
ASP   CG   C N N 96  
ASP   OD1  O N N 97  
ASP   OD2  O N N 98  
ASP   OXT  O N N 99  
ASP   H    H N N 100 
ASP   H2   H N N 101 
ASP   HA   H N N 102 
ASP   HB2  H N N 103 
ASP   HB3  H N N 104 
ASP   HD2  H N N 105 
ASP   HXT  H N N 106 
CYS   N    N N N 107 
CYS   CA   C N R 108 
CYS   C    C N N 109 
CYS   O    O N N 110 
CYS   CB   C N N 111 
CYS   SG   S N N 112 
CYS   OXT  O N N 113 
CYS   H    H N N 114 
CYS   H2   H N N 115 
CYS   HA   H N N 116 
CYS   HB2  H N N 117 
CYS   HB3  H N N 118 
CYS   HG   H N N 119 
CYS   HXT  H N N 120 
GLN   N    N N N 121 
GLN   CA   C N S 122 
GLN   C    C N N 123 
GLN   O    O N N 124 
GLN   CB   C N N 125 
GLN   CG   C N N 126 
GLN   CD   C N N 127 
GLN   OE1  O N N 128 
GLN   NE2  N N N 129 
GLN   OXT  O N N 130 
GLN   H    H N N 131 
GLN   H2   H N N 132 
GLN   HA   H N N 133 
GLN   HB2  H N N 134 
GLN   HB3  H N N 135 
GLN   HG2  H N N 136 
GLN   HG3  H N N 137 
GLN   HE21 H N N 138 
GLN   HE22 H N N 139 
GLN   HXT  H N N 140 
GLU   N    N N N 141 
GLU   CA   C N S 142 
GLU   C    C N N 143 
GLU   O    O N N 144 
GLU   CB   C N N 145 
GLU   CG   C N N 146 
GLU   CD   C N N 147 
GLU   OE1  O N N 148 
GLU   OE2  O N N 149 
GLU   OXT  O N N 150 
GLU   H    H N N 151 
GLU   H2   H N N 152 
GLU   HA   H N N 153 
GLU   HB2  H N N 154 
GLU   HB3  H N N 155 
GLU   HG2  H N N 156 
GLU   HG3  H N N 157 
GLU   HE2  H N N 158 
GLU   HXT  H N N 159 
GLY   N    N N N 160 
GLY   CA   C N N 161 
GLY   C    C N N 162 
GLY   O    O N N 163 
GLY   OXT  O N N 164 
GLY   H    H N N 165 
GLY   H2   H N N 166 
GLY   HA2  H N N 167 
GLY   HA3  H N N 168 
GLY   HXT  H N N 169 
HIS   N    N N N 170 
HIS   CA   C N S 171 
HIS   C    C N N 172 
HIS   O    O N N 173 
HIS   CB   C N N 174 
HIS   CG   C Y N 175 
HIS   ND1  N Y N 176 
HIS   CD2  C Y N 177 
HIS   CE1  C Y N 178 
HIS   NE2  N Y N 179 
HIS   OXT  O N N 180 
HIS   H    H N N 181 
HIS   H2   H N N 182 
HIS   HA   H N N 183 
HIS   HB2  H N N 184 
HIS   HB3  H N N 185 
HIS   HD1  H N N 186 
HIS   HD2  H N N 187 
HIS   HE1  H N N 188 
HIS   HE2  H N N 189 
HIS   HXT  H N N 190 
HOH   O    O N N 191 
HOH   H1   H N N 192 
HOH   H2   H N N 193 
ILE   N    N N N 194 
ILE   CA   C N S 195 
ILE   C    C N N 196 
ILE   O    O N N 197 
ILE   CB   C N S 198 
ILE   CG1  C N N 199 
ILE   CG2  C N N 200 
ILE   CD1  C N N 201 
ILE   OXT  O N N 202 
ILE   H    H N N 203 
ILE   H2   H N N 204 
ILE   HA   H N N 205 
ILE   HB   H N N 206 
ILE   HG12 H N N 207 
ILE   HG13 H N N 208 
ILE   HG21 H N N 209 
ILE   HG22 H N N 210 
ILE   HG23 H N N 211 
ILE   HD11 H N N 212 
ILE   HD12 H N N 213 
ILE   HD13 H N N 214 
ILE   HXT  H N N 215 
LEU   N    N N N 216 
LEU   CA   C N S 217 
LEU   C    C N N 218 
LEU   O    O N N 219 
LEU   CB   C N N 220 
LEU   CG   C N N 221 
LEU   CD1  C N N 222 
LEU   CD2  C N N 223 
LEU   OXT  O N N 224 
LEU   H    H N N 225 
LEU   H2   H N N 226 
LEU   HA   H N N 227 
LEU   HB2  H N N 228 
LEU   HB3  H N N 229 
LEU   HG   H N N 230 
LEU   HD11 H N N 231 
LEU   HD12 H N N 232 
LEU   HD13 H N N 233 
LEU   HD21 H N N 234 
LEU   HD22 H N N 235 
LEU   HD23 H N N 236 
LEU   HXT  H N N 237 
LYS   N    N N N 238 
LYS   CA   C N S 239 
LYS   C    C N N 240 
LYS   O    O N N 241 
LYS   CB   C N N 242 
LYS   CG   C N N 243 
LYS   CD   C N N 244 
LYS   CE   C N N 245 
LYS   NZ   N N N 246 
LYS   OXT  O N N 247 
LYS   H    H N N 248 
LYS   H2   H N N 249 
LYS   HA   H N N 250 
LYS   HB2  H N N 251 
LYS   HB3  H N N 252 
LYS   HG2  H N N 253 
LYS   HG3  H N N 254 
LYS   HD2  H N N 255 
LYS   HD3  H N N 256 
LYS   HE2  H N N 257 
LYS   HE3  H N N 258 
LYS   HZ1  H N N 259 
LYS   HZ2  H N N 260 
LYS   HZ3  H N N 261 
LYS   HXT  H N N 262 
MET   N    N N N 263 
MET   CA   C N S 264 
MET   C    C N N 265 
MET   O    O N N 266 
MET   CB   C N N 267 
MET   CG   C N N 268 
MET   SD   S N N 269 
MET   CE   C N N 270 
MET   OXT  O N N 271 
MET   H    H N N 272 
MET   H2   H N N 273 
MET   HA   H N N 274 
MET   HB2  H N N 275 
MET   HB3  H N N 276 
MET   HG2  H N N 277 
MET   HG3  H N N 278 
MET   HE1  H N N 279 
MET   HE2  H N N 280 
MET   HE3  H N N 281 
MET   HXT  H N N 282 
PHE   N    N N N 283 
PHE   CA   C N S 284 
PHE   C    C N N 285 
PHE   O    O N N 286 
PHE   CB   C N N 287 
PHE   CG   C Y N 288 
PHE   CD1  C Y N 289 
PHE   CD2  C Y N 290 
PHE   CE1  C Y N 291 
PHE   CE2  C Y N 292 
PHE   CZ   C Y N 293 
PHE   OXT  O N N 294 
PHE   H    H N N 295 
PHE   H2   H N N 296 
PHE   HA   H N N 297 
PHE   HB2  H N N 298 
PHE   HB3  H N N 299 
PHE   HD1  H N N 300 
PHE   HD2  H N N 301 
PHE   HE1  H N N 302 
PHE   HE2  H N N 303 
PHE   HZ   H N N 304 
PHE   HXT  H N N 305 
PRO   N    N N N 306 
PRO   CA   C N S 307 
PRO   C    C N N 308 
PRO   O    O N N 309 
PRO   CB   C N N 310 
PRO   CG   C N N 311 
PRO   CD   C N N 312 
PRO   OXT  O N N 313 
PRO   H    H N N 314 
PRO   HA   H N N 315 
PRO   HB2  H N N 316 
PRO   HB3  H N N 317 
PRO   HG2  H N N 318 
PRO   HG3  H N N 319 
PRO   HD2  H N N 320 
PRO   HD3  H N N 321 
PRO   HXT  H N N 322 
SER   N    N N N 323 
SER   CA   C N S 324 
SER   C    C N N 325 
SER   O    O N N 326 
SER   CB   C N N 327 
SER   OG   O N N 328 
SER   OXT  O N N 329 
SER   H    H N N 330 
SER   H2   H N N 331 
SER   HA   H N N 332 
SER   HB2  H N N 333 
SER   HB3  H N N 334 
SER   HG   H N N 335 
SER   HXT  H N N 336 
THR   N    N N N 337 
THR   CA   C N S 338 
THR   C    C N N 339 
THR   O    O N N 340 
THR   CB   C N R 341 
THR   OG1  O N N 342 
THR   CG2  C N N 343 
THR   OXT  O N N 344 
THR   H    H N N 345 
THR   H2   H N N 346 
THR   HA   H N N 347 
THR   HB   H N N 348 
THR   HG1  H N N 349 
THR   HG21 H N N 350 
THR   HG22 H N N 351 
THR   HG23 H N N 352 
THR   HXT  H N N 353 
TRP   N    N N N 354 
TRP   CA   C N S 355 
TRP   C    C N N 356 
TRP   O    O N N 357 
TRP   CB   C N N 358 
TRP   CG   C Y N 359 
TRP   CD1  C Y N 360 
TRP   CD2  C Y N 361 
TRP   NE1  N Y N 362 
TRP   CE2  C Y N 363 
TRP   CE3  C Y N 364 
TRP   CZ2  C Y N 365 
TRP   CZ3  C Y N 366 
TRP   CH2  C Y N 367 
TRP   OXT  O N N 368 
TRP   H    H N N 369 
TRP   H2   H N N 370 
TRP   HA   H N N 371 
TRP   HB2  H N N 372 
TRP   HB3  H N N 373 
TRP   HD1  H N N 374 
TRP   HE1  H N N 375 
TRP   HE3  H N N 376 
TRP   HZ2  H N N 377 
TRP   HZ3  H N N 378 
TRP   HH2  H N N 379 
TRP   HXT  H N N 380 
TYR   N    N N N 381 
TYR   CA   C N S 382 
TYR   C    C N N 383 
TYR   O    O N N 384 
TYR   CB   C N N 385 
TYR   CG   C Y N 386 
TYR   CD1  C Y N 387 
TYR   CD2  C Y N 388 
TYR   CE1  C Y N 389 
TYR   CE2  C Y N 390 
TYR   CZ   C Y N 391 
TYR   OH   O N N 392 
TYR   OXT  O N N 393 
TYR   H    H N N 394 
TYR   H2   H N N 395 
TYR   HA   H N N 396 
TYR   HB2  H N N 397 
TYR   HB3  H N N 398 
TYR   HD1  H N N 399 
TYR   HD2  H N N 400 
TYR   HE1  H N N 401 
TYR   HE2  H N N 402 
TYR   HH   H N N 403 
TYR   HXT  H N N 404 
VAL   N    N N N 405 
VAL   CA   C N S 406 
VAL   C    C N N 407 
VAL   O    O N N 408 
VAL   CB   C N N 409 
VAL   CG1  C N N 410 
VAL   CG2  C N N 411 
VAL   OXT  O N N 412 
VAL   H    H N N 413 
VAL   H2   H N N 414 
VAL   HA   H N N 415 
VAL   HB   H N N 416 
VAL   HG11 H N N 417 
VAL   HG12 H N N 418 
VAL   HG13 H N N 419 
VAL   HG21 H N N 420 
VAL   HG22 H N N 421 
VAL   HG23 H N N 422 
VAL   HXT  H N N 423 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
A1LWG C   O    doub N N 1   
A1LWG CA  C    sing N N 2   
A1LWG CB  CA   sing N N 3   
A1LWG N   CA   sing N N 4   
A1LWG C06 N    sing N N 5   
A1LWG C07 C06  sing N N 6   
A1LWG C08 C07  sing N N 7   
A1LWG C09 C08  doub Y N 8   
A1LWG N10 C09  sing Y N 9   
A1LWG C11 N10  sing Y N 10  
A1LWG C12 C11  doub Y N 11  
A1LWG C13 C12  sing Y N 12  
A1LWG C14 C13  doub Y N 13  
A1LWG C15 C14  sing Y N 14  
A1LWG C16 C15  doub Y N 15  
A1LWG C08 C12  sing Y N 16  
A1LWG C11 C16  sing Y N 17  
A1LWG CA  H031 sing N N 18  
A1LWG CB  H043 sing N N 19  
A1LWG CB  H042 sing N N 20  
A1LWG CB  H041 sing N N 21  
A1LWG C06 H062 sing N N 22  
A1LWG C06 H061 sing N N 23  
A1LWG C07 H071 sing N N 24  
A1LWG C07 H072 sing N N 25  
A1LWG C09 H091 sing N N 26  
A1LWG C13 H131 sing N N 27  
A1LWG C14 H141 sing N N 28  
A1LWG C15 H151 sing N N 29  
A1LWG C16 H161 sing N N 30  
A1LWG N   H051 sing N N 31  
A1LWG N10 H101 sing N N 32  
A1LWG C   OXT  sing N N 33  
A1LWG OXT H1   sing N N 34  
ALA   N   CA   sing N N 35  
ALA   N   H    sing N N 36  
ALA   N   H2   sing N N 37  
ALA   CA  C    sing N N 38  
ALA   CA  CB   sing N N 39  
ALA   CA  HA   sing N N 40  
ALA   C   O    doub N N 41  
ALA   C   OXT  sing N N 42  
ALA   CB  HB1  sing N N 43  
ALA   CB  HB2  sing N N 44  
ALA   CB  HB3  sing N N 45  
ALA   OXT HXT  sing N N 46  
ARG   N   CA   sing N N 47  
ARG   N   H    sing N N 48  
ARG   N   H2   sing N N 49  
ARG   CA  C    sing N N 50  
ARG   CA  CB   sing N N 51  
ARG   CA  HA   sing N N 52  
ARG   C   O    doub N N 53  
ARG   C   OXT  sing N N 54  
ARG   CB  CG   sing N N 55  
ARG   CB  HB2  sing N N 56  
ARG   CB  HB3  sing N N 57  
ARG   CG  CD   sing N N 58  
ARG   CG  HG2  sing N N 59  
ARG   CG  HG3  sing N N 60  
ARG   CD  NE   sing N N 61  
ARG   CD  HD2  sing N N 62  
ARG   CD  HD3  sing N N 63  
ARG   NE  CZ   sing N N 64  
ARG   NE  HE   sing N N 65  
ARG   CZ  NH1  sing N N 66  
ARG   CZ  NH2  doub N N 67  
ARG   NH1 HH11 sing N N 68  
ARG   NH1 HH12 sing N N 69  
ARG   NH2 HH21 sing N N 70  
ARG   NH2 HH22 sing N N 71  
ARG   OXT HXT  sing N N 72  
ASN   N   CA   sing N N 73  
ASN   N   H    sing N N 74  
ASN   N   H2   sing N N 75  
ASN   CA  C    sing N N 76  
ASN   CA  CB   sing N N 77  
ASN   CA  HA   sing N N 78  
ASN   C   O    doub N N 79  
ASN   C   OXT  sing N N 80  
ASN   CB  CG   sing N N 81  
ASN   CB  HB2  sing N N 82  
ASN   CB  HB3  sing N N 83  
ASN   CG  OD1  doub N N 84  
ASN   CG  ND2  sing N N 85  
ASN   ND2 HD21 sing N N 86  
ASN   ND2 HD22 sing N N 87  
ASN   OXT HXT  sing N N 88  
ASP   N   CA   sing N N 89  
ASP   N   H    sing N N 90  
ASP   N   H2   sing N N 91  
ASP   CA  C    sing N N 92  
ASP   CA  CB   sing N N 93  
ASP   CA  HA   sing N N 94  
ASP   C   O    doub N N 95  
ASP   C   OXT  sing N N 96  
ASP   CB  CG   sing N N 97  
ASP   CB  HB2  sing N N 98  
ASP   CB  HB3  sing N N 99  
ASP   CG  OD1  doub N N 100 
ASP   CG  OD2  sing N N 101 
ASP   OD2 HD2  sing N N 102 
ASP   OXT HXT  sing N N 103 
CYS   N   CA   sing N N 104 
CYS   N   H    sing N N 105 
CYS   N   H2   sing N N 106 
CYS   CA  C    sing N N 107 
CYS   CA  CB   sing N N 108 
CYS   CA  HA   sing N N 109 
CYS   C   O    doub N N 110 
CYS   C   OXT  sing N N 111 
CYS   CB  SG   sing N N 112 
CYS   CB  HB2  sing N N 113 
CYS   CB  HB3  sing N N 114 
CYS   SG  HG   sing N N 115 
CYS   OXT HXT  sing N N 116 
GLN   N   CA   sing N N 117 
GLN   N   H    sing N N 118 
GLN   N   H2   sing N N 119 
GLN   CA  C    sing N N 120 
GLN   CA  CB   sing N N 121 
GLN   CA  HA   sing N N 122 
GLN   C   O    doub N N 123 
GLN   C   OXT  sing N N 124 
GLN   CB  CG   sing N N 125 
GLN   CB  HB2  sing N N 126 
GLN   CB  HB3  sing N N 127 
GLN   CG  CD   sing N N 128 
GLN   CG  HG2  sing N N 129 
GLN   CG  HG3  sing N N 130 
GLN   CD  OE1  doub N N 131 
GLN   CD  NE2  sing N N 132 
GLN   NE2 HE21 sing N N 133 
GLN   NE2 HE22 sing N N 134 
GLN   OXT HXT  sing N N 135 
GLU   N   CA   sing N N 136 
GLU   N   H    sing N N 137 
GLU   N   H2   sing N N 138 
GLU   CA  C    sing N N 139 
GLU   CA  CB   sing N N 140 
GLU   CA  HA   sing N N 141 
GLU   C   O    doub N N 142 
GLU   C   OXT  sing N N 143 
GLU   CB  CG   sing N N 144 
GLU   CB  HB2  sing N N 145 
GLU   CB  HB3  sing N N 146 
GLU   CG  CD   sing N N 147 
GLU   CG  HG2  sing N N 148 
GLU   CG  HG3  sing N N 149 
GLU   CD  OE1  doub N N 150 
GLU   CD  OE2  sing N N 151 
GLU   OE2 HE2  sing N N 152 
GLU   OXT HXT  sing N N 153 
GLY   N   CA   sing N N 154 
GLY   N   H    sing N N 155 
GLY   N   H2   sing N N 156 
GLY   CA  C    sing N N 157 
GLY   CA  HA2  sing N N 158 
GLY   CA  HA3  sing N N 159 
GLY   C   O    doub N N 160 
GLY   C   OXT  sing N N 161 
GLY   OXT HXT  sing N N 162 
HIS   N   CA   sing N N 163 
HIS   N   H    sing N N 164 
HIS   N   H2   sing N N 165 
HIS   CA  C    sing N N 166 
HIS   CA  CB   sing N N 167 
HIS   CA  HA   sing N N 168 
HIS   C   O    doub N N 169 
HIS   C   OXT  sing N N 170 
HIS   CB  CG   sing N N 171 
HIS   CB  HB2  sing N N 172 
HIS   CB  HB3  sing N N 173 
HIS   CG  ND1  sing Y N 174 
HIS   CG  CD2  doub Y N 175 
HIS   ND1 CE1  doub Y N 176 
HIS   ND1 HD1  sing N N 177 
HIS   CD2 NE2  sing Y N 178 
HIS   CD2 HD2  sing N N 179 
HIS   CE1 NE2  sing Y N 180 
HIS   CE1 HE1  sing N N 181 
HIS   NE2 HE2  sing N N 182 
HIS   OXT HXT  sing N N 183 
HOH   O   H1   sing N N 184 
HOH   O   H2   sing N N 185 
ILE   N   CA   sing N N 186 
ILE   N   H    sing N N 187 
ILE   N   H2   sing N N 188 
ILE   CA  C    sing N N 189 
ILE   CA  CB   sing N N 190 
ILE   CA  HA   sing N N 191 
ILE   C   O    doub N N 192 
ILE   C   OXT  sing N N 193 
ILE   CB  CG1  sing N N 194 
ILE   CB  CG2  sing N N 195 
ILE   CB  HB   sing N N 196 
ILE   CG1 CD1  sing N N 197 
ILE   CG1 HG12 sing N N 198 
ILE   CG1 HG13 sing N N 199 
ILE   CG2 HG21 sing N N 200 
ILE   CG2 HG22 sing N N 201 
ILE   CG2 HG23 sing N N 202 
ILE   CD1 HD11 sing N N 203 
ILE   CD1 HD12 sing N N 204 
ILE   CD1 HD13 sing N N 205 
ILE   OXT HXT  sing N N 206 
LEU   N   CA   sing N N 207 
LEU   N   H    sing N N 208 
LEU   N   H2   sing N N 209 
LEU   CA  C    sing N N 210 
LEU   CA  CB   sing N N 211 
LEU   CA  HA   sing N N 212 
LEU   C   O    doub N N 213 
LEU   C   OXT  sing N N 214 
LEU   CB  CG   sing N N 215 
LEU   CB  HB2  sing N N 216 
LEU   CB  HB3  sing N N 217 
LEU   CG  CD1  sing N N 218 
LEU   CG  CD2  sing N N 219 
LEU   CG  HG   sing N N 220 
LEU   CD1 HD11 sing N N 221 
LEU   CD1 HD12 sing N N 222 
LEU   CD1 HD13 sing N N 223 
LEU   CD2 HD21 sing N N 224 
LEU   CD2 HD22 sing N N 225 
LEU   CD2 HD23 sing N N 226 
LEU   OXT HXT  sing N N 227 
LYS   N   CA   sing N N 228 
LYS   N   H    sing N N 229 
LYS   N   H2   sing N N 230 
LYS   CA  C    sing N N 231 
LYS   CA  CB   sing N N 232 
LYS   CA  HA   sing N N 233 
LYS   C   O    doub N N 234 
LYS   C   OXT  sing N N 235 
LYS   CB  CG   sing N N 236 
LYS   CB  HB2  sing N N 237 
LYS   CB  HB3  sing N N 238 
LYS   CG  CD   sing N N 239 
LYS   CG  HG2  sing N N 240 
LYS   CG  HG3  sing N N 241 
LYS   CD  CE   sing N N 242 
LYS   CD  HD2  sing N N 243 
LYS   CD  HD3  sing N N 244 
LYS   CE  NZ   sing N N 245 
LYS   CE  HE2  sing N N 246 
LYS   CE  HE3  sing N N 247 
LYS   NZ  HZ1  sing N N 248 
LYS   NZ  HZ2  sing N N 249 
LYS   NZ  HZ3  sing N N 250 
LYS   OXT HXT  sing N N 251 
MET   N   CA   sing N N 252 
MET   N   H    sing N N 253 
MET   N   H2   sing N N 254 
MET   CA  C    sing N N 255 
MET   CA  CB   sing N N 256 
MET   CA  HA   sing N N 257 
MET   C   O    doub N N 258 
MET   C   OXT  sing N N 259 
MET   CB  CG   sing N N 260 
MET   CB  HB2  sing N N 261 
MET   CB  HB3  sing N N 262 
MET   CG  SD   sing N N 263 
MET   CG  HG2  sing N N 264 
MET   CG  HG3  sing N N 265 
MET   SD  CE   sing N N 266 
MET   CE  HE1  sing N N 267 
MET   CE  HE2  sing N N 268 
MET   CE  HE3  sing N N 269 
MET   OXT HXT  sing N N 270 
PHE   N   CA   sing N N 271 
PHE   N   H    sing N N 272 
PHE   N   H2   sing N N 273 
PHE   CA  C    sing N N 274 
PHE   CA  CB   sing N N 275 
PHE   CA  HA   sing N N 276 
PHE   C   O    doub N N 277 
PHE   C   OXT  sing N N 278 
PHE   CB  CG   sing N N 279 
PHE   CB  HB2  sing N N 280 
PHE   CB  HB3  sing N N 281 
PHE   CG  CD1  doub Y N 282 
PHE   CG  CD2  sing Y N 283 
PHE   CD1 CE1  sing Y N 284 
PHE   CD1 HD1  sing N N 285 
PHE   CD2 CE2  doub Y N 286 
PHE   CD2 HD2  sing N N 287 
PHE   CE1 CZ   doub Y N 288 
PHE   CE1 HE1  sing N N 289 
PHE   CE2 CZ   sing Y N 290 
PHE   CE2 HE2  sing N N 291 
PHE   CZ  HZ   sing N N 292 
PHE   OXT HXT  sing N N 293 
PRO   N   CA   sing N N 294 
PRO   N   CD   sing N N 295 
PRO   N   H    sing N N 296 
PRO   CA  C    sing N N 297 
PRO   CA  CB   sing N N 298 
PRO   CA  HA   sing N N 299 
PRO   C   O    doub N N 300 
PRO   C   OXT  sing N N 301 
PRO   CB  CG   sing N N 302 
PRO   CB  HB2  sing N N 303 
PRO   CB  HB3  sing N N 304 
PRO   CG  CD   sing N N 305 
PRO   CG  HG2  sing N N 306 
PRO   CG  HG3  sing N N 307 
PRO   CD  HD2  sing N N 308 
PRO   CD  HD3  sing N N 309 
PRO   OXT HXT  sing N N 310 
SER   N   CA   sing N N 311 
SER   N   H    sing N N 312 
SER   N   H2   sing N N 313 
SER   CA  C    sing N N 314 
SER   CA  CB   sing N N 315 
SER   CA  HA   sing N N 316 
SER   C   O    doub N N 317 
SER   C   OXT  sing N N 318 
SER   CB  OG   sing N N 319 
SER   CB  HB2  sing N N 320 
SER   CB  HB3  sing N N 321 
SER   OG  HG   sing N N 322 
SER   OXT HXT  sing N N 323 
THR   N   CA   sing N N 324 
THR   N   H    sing N N 325 
THR   N   H2   sing N N 326 
THR   CA  C    sing N N 327 
THR   CA  CB   sing N N 328 
THR   CA  HA   sing N N 329 
THR   C   O    doub N N 330 
THR   C   OXT  sing N N 331 
THR   CB  OG1  sing N N 332 
THR   CB  CG2  sing N N 333 
THR   CB  HB   sing N N 334 
THR   OG1 HG1  sing N N 335 
THR   CG2 HG21 sing N N 336 
THR   CG2 HG22 sing N N 337 
THR   CG2 HG23 sing N N 338 
THR   OXT HXT  sing N N 339 
TRP   N   CA   sing N N 340 
TRP   N   H    sing N N 341 
TRP   N   H2   sing N N 342 
TRP   CA  C    sing N N 343 
TRP   CA  CB   sing N N 344 
TRP   CA  HA   sing N N 345 
TRP   C   O    doub N N 346 
TRP   C   OXT  sing N N 347 
TRP   CB  CG   sing N N 348 
TRP   CB  HB2  sing N N 349 
TRP   CB  HB3  sing N N 350 
TRP   CG  CD1  doub Y N 351 
TRP   CG  CD2  sing Y N 352 
TRP   CD1 NE1  sing Y N 353 
TRP   CD1 HD1  sing N N 354 
TRP   CD2 CE2  doub Y N 355 
TRP   CD2 CE3  sing Y N 356 
TRP   NE1 CE2  sing Y N 357 
TRP   NE1 HE1  sing N N 358 
TRP   CE2 CZ2  sing Y N 359 
TRP   CE3 CZ3  doub Y N 360 
TRP   CE3 HE3  sing N N 361 
TRP   CZ2 CH2  doub Y N 362 
TRP   CZ2 HZ2  sing N N 363 
TRP   CZ3 CH2  sing Y N 364 
TRP   CZ3 HZ3  sing N N 365 
TRP   CH2 HH2  sing N N 366 
TRP   OXT HXT  sing N N 367 
TYR   N   CA   sing N N 368 
TYR   N   H    sing N N 369 
TYR   N   H2   sing N N 370 
TYR   CA  C    sing N N 371 
TYR   CA  CB   sing N N 372 
TYR   CA  HA   sing N N 373 
TYR   C   O    doub N N 374 
TYR   C   OXT  sing N N 375 
TYR   CB  CG   sing N N 376 
TYR   CB  HB2  sing N N 377 
TYR   CB  HB3  sing N N 378 
TYR   CG  CD1  doub Y N 379 
TYR   CG  CD2  sing Y N 380 
TYR   CD1 CE1  sing Y N 381 
TYR   CD1 HD1  sing N N 382 
TYR   CD2 CE2  doub Y N 383 
TYR   CD2 HD2  sing N N 384 
TYR   CE1 CZ   doub Y N 385 
TYR   CE1 HE1  sing N N 386 
TYR   CE2 CZ   sing Y N 387 
TYR   CE2 HE2  sing N N 388 
TYR   CZ  OH   sing N N 389 
TYR   OH  HH   sing N N 390 
TYR   OXT HXT  sing N N 391 
VAL   N   CA   sing N N 392 
VAL   N   H    sing N N 393 
VAL   N   H2   sing N N 394 
VAL   CA  C    sing N N 395 
VAL   CA  CB   sing N N 396 
VAL   CA  HA   sing N N 397 
VAL   C   O    doub N N 398 
VAL   C   OXT  sing N N 399 
VAL   CB  CG1  sing N N 400 
VAL   CB  CG2  sing N N 401 
VAL   CB  HB   sing N N 402 
VAL   CG1 HG11 sing N N 403 
VAL   CG1 HG12 sing N N 404 
VAL   CG1 HG13 sing N N 405 
VAL   CG2 HG21 sing N N 406 
VAL   CG2 HG22 sing N N 407 
VAL   CG2 HG23 sing N N 408 
VAL   OXT HXT  sing N N 409 
# 
_pdbx_audit_support.funding_organization   'Not funded' 
_pdbx_audit_support.country                ? 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   8X4Q 
_pdbx_initial_refinement_model.details          ? 
# 
_space_group.name_H-M_alt     'P 1 21 1' 
_space_group.name_Hall        'P 2yb' 
_space_group.IT_number        4 
_space_group.crystal_system   monoclinic 
_space_group.id               1 
# 
_atom_sites.entry_id                    8X4S 
_atom_sites.Cartn_transf_matrix[1][1]   ? 
_atom_sites.Cartn_transf_matrix[1][2]   ? 
_atom_sites.Cartn_transf_matrix[1][3]   ? 
_atom_sites.Cartn_transf_matrix[2][1]   ? 
_atom_sites.Cartn_transf_matrix[2][2]   ? 
_atom_sites.Cartn_transf_matrix[2][3]   ? 
_atom_sites.Cartn_transf_matrix[3][1]   ? 
_atom_sites.Cartn_transf_matrix[3][2]   ? 
_atom_sites.Cartn_transf_matrix[3][3]   ? 
_atom_sites.Cartn_transf_vector[1]      ? 
_atom_sites.Cartn_transf_vector[2]      ? 
_atom_sites.Cartn_transf_vector[3]      ? 
_atom_sites.Cartn_transform_axes        ? 
_atom_sites.fract_transf_matrix[1][1]   0.012095 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.002083 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.008163 
_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]   0.007883 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
_atom_type.scat_dispersion_real 
_atom_type.scat_dispersion_imag 
_atom_type.scat_Cromer_Mann_a1 
_atom_type.scat_Cromer_Mann_a2 
_atom_type.scat_Cromer_Mann_a3 
_atom_type.scat_Cromer_Mann_a4 
_atom_type.scat_Cromer_Mann_b1 
_atom_type.scat_Cromer_Mann_b2 
_atom_type.scat_Cromer_Mann_b3 
_atom_type.scat_Cromer_Mann_b4 
_atom_type.scat_Cromer_Mann_c 
_atom_type.scat_source 
_atom_type.scat_dispersion_source 
C ? ? 3.54356 2.42580 ? ? 25.62398 1.50364  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
N ? ? 4.01032 2.96436 ? ? 19.97189 1.75589  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O ? ? 7.96527 ?       ? ? 9.05267  ?        ? ? 0.0 
;1-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
S ? ? 9.55732 6.39887 ? ? 1.23737  29.19336 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1     N N   . LEU   A  1 57  ? 32.85933  41.67197  -27.15279 1.000 58.90146  ?  57  LEU   I N   1 
ATOM   2     C CA  . LEU   A  1 57  ? 32.58664  40.23890  -27.18106 1.000 55.79879  ?  57  LEU   I CA  1 
ATOM   3     C C   . LEU   A  1 57  ? 32.71582  39.65473  -25.79202 1.000 71.94090  ?  57  LEU   I C   1 
ATOM   4     O O   . LEU   A  1 57  ? 33.65991  39.98092  -25.07468 1.000 73.93476  ?  57  LEU   I O   1 
ATOM   5     C CB  . LEU   A  1 57  ? 33.56631  39.49734  -28.09352 1.000 52.44401  ?  57  LEU   I CB  1 
ATOM   6     C CG  . LEU   A  1 57  ? 33.62379  39.70605  -29.60544 1.000 68.70770  ?  57  LEU   I CG  1 
ATOM   7     C CD1 . LEU   A  1 57  ? 34.79310  38.90130  -30.17161 1.000 61.09375  ?  57  LEU   I CD1 1 
ATOM   8     C CD2 . LEU   A  1 57  ? 32.31687  39.33576  -30.29837 1.000 67.17255  ?  57  LEU   I CD2 1 
ATOM   9     N N   . MET   A  1 58  ? 31.80644  38.75249  -25.42825 1.000 69.75236  ?  58  MET   I N   1 
ATOM   10    C CA  . MET   A  1 58  ? 31.90905  38.10738  -24.12591 1.000 68.65107  ?  58  MET   I CA  1 
ATOM   11    C C   . MET   A  1 58  ? 33.15481  37.23283  -24.06141 1.000 59.35945  ?  58  MET   I C   1 
ATOM   12    O O   . MET   A  1 58  ? 33.58284  36.65105  -25.06043 1.000 80.02504  ?  58  MET   I O   1 
ATOM   13    C CB  . MET   A  1 58  ? 30.66341  37.27825  -23.83824 1.000 61.59357  ?  58  MET   I CB  1 
ATOM   14    C CG  . MET   A  1 58  ? 30.27174  36.30005  -24.92594 1.000 76.89529  ?  58  MET   I CG  1 
ATOM   15    S SD  . MET   A  1 58  ? 28.80564  35.36700  -24.43760 1.000 82.76034  ?  58  MET   I SD  1 
ATOM   16    C CE  . MET   A  1 58  ? 27.51439  36.57301  -24.78264 1.000 59.38711  ?  58  MET   I CE  1 
ATOM   17    N N   . GLN   A  1 59  ? 33.74017  37.14474  -22.86817 1.000 62.79819  ?  59  GLN   I N   1 
ATOM   18    C CA  . GLN   A  1 59  ? 35.03328  36.48112  -22.69675 1.000 51.63643  ?  59  GLN   I CA  1 
ATOM   19    C C   . GLN   A  1 59  ? 35.11420  35.09140  -23.32410 1.000 61.36597  ?  59  GLN   I C   1 
ATOM   20    O O   . GLN   A  1 59  ? 36.12664  34.80421  -23.98194 1.000 55.41648  ?  59  GLN   I O   1 
ATOM   21    C CB  . GLN   A  1 59  ? 35.38676  36.38887  -21.20505 1.000 45.38637  ?  59  GLN   I CB  1 
ATOM   22    C CG  . GLN   A  1 59  ? 36.84528  36.08053  -20.97649 1.000 74.93824  ?  59  GLN   I CG  1 
ATOM   23    C CD  . GLN   A  1 59  ? 37.72246  37.17938  -21.55157 1.000 97.53016  ?  59  GLN   I CD  1 
ATOM   24    O OE1 . GLN   A  1 59  ? 37.33696  38.35250  -21.55929 1.000 109.11380 ?  59  GLN   I OE1 1 
ATOM   25    N NE2 . GLN   A  1 59  ? 38.89754  36.80763  -22.05856 1.000 82.15683  ?  59  GLN   I NE2 1 
ATOM   26    N N   . PRO   A  1 60  ? 34.12730  34.19292  -23.16888 1.000 70.30197  ?  60  PRO   I N   1 
ATOM   27    C CA  . PRO   A  1 60  ? 34.25616  32.87322  -23.82116 1.000 52.02178  ?  60  PRO   I CA  1 
ATOM   28    C C   . PRO   A  1 60  ? 34.45154  32.96517  -25.32625 1.000 76.10990  ?  60  PRO   I C   1 
ATOM   29    O O   . PRO   A  1 60  ? 35.22878  32.17609  -25.88580 1.000 55.21329  ?  60  PRO   I O   1 
ATOM   30    C CB  . PRO   A  1 60  ? 32.94479  32.16840  -23.44563 1.000 52.78536  ?  60  PRO   I CB  1 
ATOM   31    C CG  . PRO   A  1 60  ? 32.48541  32.84948  -22.19622 1.000 59.77393  ?  60  PRO   I CG  1 
ATOM   32    C CD  . PRO   A  1 60  ? 32.88441  34.28949  -22.38174 1.000 48.05322  ?  60  PRO   I CD  1 
ATOM   33    N N   . ILE   A  1 61  ? 33.78321  33.91640  -25.99371 1.000 45.62415  ?  61  ILE   I N   1 
ATOM   34    C CA  . ILE   A  1 61  ? 34.01112  34.11864  -27.42546 1.000 69.95775  ?  61  ILE   I CA  1 
ATOM   35    C C   . ILE   A  1 61  ? 35.39850  34.68898  -27.68388 1.000 56.27694  ?  61  ILE   I C   1 
ATOM   36    O O   . ILE   A  1 61  ? 36.03361  34.36235  -28.69398 1.000 60.61092  ?  61  ILE   I O   1 
ATOM   37    C CB  . ILE   A  1 61  ? 32.91825  35.01495  -28.03357 1.000 55.84838  ?  61  ILE   I CB  1 
ATOM   38    C CG1 . ILE   A  1 61  ? 31.54912  34.37255  -27.82092 1.000 46.40024  ?  61  ILE   I CG1 1 
ATOM   39    C CG2 . ILE   A  1 61  ? 33.16035  35.24366  -29.53624 1.000 44.53746  ?  61  ILE   I CG2 1 
ATOM   40    C CD1 . ILE   A  1 61  ? 30.43611  35.15593  -28.42895 1.000 52.98902  ?  61  ILE   I CD1 1 
ATOM   41    N N   . GLN   A  1 62  ? 35.87022  35.54921  -26.77638 1.000 33.46231  ?  62  GLN   I N   1 
ATOM   42    C CA  . GLN   A  1 62  ? 37.23049  36.05560  -26.89551 1.000 57.72299  ?  62  GLN   I CA  1 
ATOM   43    C C   . GLN   A  1 62  ? 38.24002  34.91227  -26.88381 1.000 108.13490 ?  62  GLN   I C   1 
ATOM   44    O O   . GLN   A  1 62  ? 39.06910  34.77784  -27.79803 1.000 65.80676  ?  62  GLN   I O   1 
ATOM   45    C CB  . GLN   A  1 62  ? 37.50612  37.05913  -25.78402 1.000 44.81391  ?  62  GLN   I CB  1 
ATOM   46    C CG  . GLN   A  1 62  ? 36.45888  38.12675  -25.79179 1.000 101.96608 ?  62  GLN   I CG  1 
ATOM   47    C CD  . GLN   A  1 62  ? 36.91258  39.39488  -25.14978 1.000 108.51763 ?  62  GLN   I CD  1 
ATOM   48    O OE1 . GLN   A  1 62  ? 36.50503  39.71252  -24.03481 1.000 112.27440 ?  62  GLN   I OE1 1 
ATOM   49    N NE2 . GLN   A  1 62  ? 37.74581  40.15020  -25.85281 1.000 121.52059 ?  62  GLN   I NE2 1 
ATOM   50    N N   . GLU   A  1 63  ? 38.14008  34.04799  -25.86971 1.000 44.13482  ?  63  GLU   I N   1 
ATOM   51    C CA  . GLU   A  1 63  ? 39.04940  32.91018  -25.75429 1.000 59.97158  ?  63  GLU   I CA  1 
ATOM   52    C C   . GLU   A  1 63  ? 38.91366  31.97599  -26.94959 1.000 62.19099  ?  63  GLU   I C   1 
ATOM   53    O O   . GLU   A  1 63  ? 39.90980  31.41370  -27.42223 1.000 55.51143  ?  63  GLU   I O   1 
ATOM   54    C CB  . GLU   A  1 63  ? 38.79142  32.16519  -24.45487 1.000 44.09118  ?  63  GLU   I CB  1 
ATOM   55    C CG  . GLU   A  1 63  ? 39.58125  32.71099  -23.27802 1.000 81.66607  ?  63  GLU   I CG  1 
ATOM   56    C CD  . GLU   A  1 63  ? 38.76140  32.80747  -22.01186 1.000 68.45836  ?  63  GLU   I CD  1 
ATOM   57    O OE1 . GLU   A  1 63  ? 37.64688  32.23813  -21.97269 1.000 114.91784 ?  63  GLU   I OE1 1 
ATOM   58    O OE2 . GLU   A  1 63  ? 39.23161  33.45573  -21.04973 1.000 142.51138 ?  63  GLU   I OE2 1 
ATOM   59    N N   . PHE   A  1 64  ? 37.68221  31.81099  -27.45265 1.000 45.16653  ?  64  PHE   I N   1 
ATOM   60    C CA  . PHE   A  1 64  ? 37.43799  31.04080  -28.66943 1.000 38.61517  ?  64  PHE   I CA  1 
ATOM   61    C C   . PHE   A  1 64  ? 38.22172  31.61429  -29.84342 1.000 52.65190  ?  64  PHE   I C   1 
ATOM   62    O O   . PHE   A  1 64  ? 38.97960  30.89805  -30.51065 1.000 47.21101  ?  64  PHE   I O   1 
ATOM   63    C CB  . PHE   A  1 64  ? 35.93320  31.02878  -28.95635 1.000 41.70916  ?  64  PHE   I CB  1 
ATOM   64    C CG  . PHE   A  1 64  ? 35.54543  30.39049  -30.26493 1.000 46.88190  ?  64  PHE   I CG  1 
ATOM   65    C CD1 . PHE   A  1 64  ? 35.62275  29.01994  -30.43802 1.000 54.82698  ?  64  PHE   I CD1 1 
ATOM   66    C CD2 . PHE   A  1 64  ? 35.05347  31.16484  -31.31064 1.000 35.91663  ?  64  PHE   I CD2 1 
ATOM   67    C CE1 . PHE   A  1 64  ? 35.24038  28.43673  -31.64522 1.000 40.81890  ?  64  PHE   I CE1 1 
ATOM   68    C CE2 . PHE   A  1 64  ? 34.65678  30.59072  -32.51536 1.000 34.16719  ?  64  PHE   I CE2 1 
ATOM   69    C CZ  . PHE   A  1 64  ? 34.74922  29.22774  -32.68473 1.000 42.90465  ?  64  PHE   I CZ  1 
ATOM   70    N N   . LYS   A  1 65  ? 38.05395  32.92002  -30.09953 1.000 54.85507  ?  65  LYS   I N   1 
ATOM   71    C CA  . LYS   A  1 65  ? 38.80887  33.59939  -31.15688 1.000 49.79171  ?  65  LYS   I CA  1 
ATOM   72    C C   . LYS   A  1 65  ? 40.31668  33.50255  -30.92610 1.000 69.97803  ?  65  LYS   I C   1 
ATOM   73    O O   . LYS   A  1 65  ? 41.09030  33.28647  -31.86827 1.000 61.53372  ?  65  LYS   I O   1 
ATOM   74    C CB  . LYS   A  1 65  ? 38.37425  35.06357  -31.24671 1.000 57.04891  ?  65  LYS   I CB  1 
ATOM   75    C CG  . LYS   A  1 65  ? 39.03409  35.87244  -32.35309 1.000 58.08395  ?  65  LYS   I CG  1 
ATOM   76    C CD  . LYS   A  1 65  ? 38.11731  37.00856  -32.77010 1.000 68.61815  ?  65  LYS   I CD  1 
ATOM   77    C CE  . LYS   A  1 65  ? 38.67293  38.35627  -32.39584 1.000 76.37135  ?  65  LYS   I CE  1 
ATOM   78    N NZ  . LYS   A  1 65  ? 38.76441  39.19247  -33.61728 1.000 87.43611  ?  65  LYS   I NZ  1 
ATOM   79    N N   . ALA   A  1 66  ? 40.75625  33.66946  -29.67677 1.000 60.17833  ?  66  ALA   I N   1 
ATOM   80    C CA  . ALA   A  1 66  ? 42.18445  33.57974  -29.39372 1.000 63.41233  ?  66  ALA   I CA  1 
ATOM   81    C C   . ALA   A  1 66  ? 42.71414  32.18079  -29.69545 1.000 73.72666  ?  66  ALA   I C   1 
ATOM   82    O O   . ALA   A  1 66  ? 43.86668  32.01316  -30.12614 1.000 58.15036  ?  66  ALA   I O   1 
ATOM   83    C CB  . ALA   A  1 66  ? 42.44871  33.96222  -27.93988 1.000 40.70564  ?  66  ALA   I CB  1 
ATOM   84    N N   . PHE   A  1 67  ? 41.87971  31.16189  -29.48697 1.000 70.53071  ?  67  PHE   I N   1 
ATOM   85    C CA  . PHE   A  1 67  ? 42.31447  29.80425  -29.77274 1.000 48.98000  ?  67  PHE   I CA  1 
ATOM   86    C C   . PHE   A  1 67  ? 42.48170  29.59871  -31.27416 1.000 64.96520  ?  67  PHE   I C   1 
ATOM   87    O O   . PHE   A  1 67  ? 43.50077  29.06112  -31.72664 1.000 61.23596  ?  67  PHE   I O   1 
ATOM   88    C CB  . PHE   A  1 67  ? 41.33047  28.78820  -29.18262 1.000 50.19644  ?  67  PHE   I CB  1 
ATOM   89    C CG  . PHE   A  1 67  ? 41.60254  27.39937  -29.63406 1.000 51.17130  ?  67  PHE   I CG  1 
ATOM   90    C CD1 . PHE   A  1 67  ? 42.64893  26.68748  -29.06890 1.000 37.55633  ?  67  PHE   I CD1 1 
ATOM   91    C CD2 . PHE   A  1 67  ? 40.86951  26.82716  -30.68452 1.000 45.13166  ?  67  PHE   I CD2 1 
ATOM   92    C CE1 . PHE   A  1 67  ? 42.95710  25.40336  -29.50754 1.000 44.69460  ?  67  PHE   I CE1 1 
ATOM   93    C CE2 . PHE   A  1 67  ? 41.16978  25.55098  -31.14843 1.000 55.01958  ?  67  PHE   I CE2 1 
ATOM   94    C CZ  . PHE   A  1 67  ? 42.21082  24.82893  -30.55803 1.000 42.07451  ?  67  PHE   I CZ  1 
ATOM   95    N N   . ILE   A  1 68  ? 41.48505  30.02290  -32.05878 1.000 51.83811  ?  68  ILE   I N   1 
ATOM   96    C CA  . ILE   A  1 68  ? 41.56019  29.93039  -33.51751 1.000 54.02038  ?  68  ILE   I CA  1 
ATOM   97    C C   . ILE   A  1 68  ? 42.86122  30.53533  -34.02446 1.000 60.10764  ?  68  ILE   I C   1 
ATOM   98    O O   . ILE   A  1 68  ? 43.52384  29.98825  -34.91505 1.000 57.73963  ?  68  ILE   I O   1 
ATOM   99    C CB  . ILE   A  1 68  ? 40.33749  30.62740  -34.14699 1.000 43.93764  ?  68  ILE   I CB  1 
ATOM   100   C CG1 . ILE   A  1 68  ? 39.04823  29.87237  -33.78837 1.000 51.03633  ?  68  ILE   I CG1 1 
ATOM   101   C CG2 . ILE   A  1 68  ? 40.50224  30.76572  -35.64784 1.000 49.32853  ?  68  ILE   I CG2 1 
ATOM   102   C CD1 . ILE   A  1 68  ? 37.79546  30.55951  -34.23312 1.000 44.01469  ?  68  ILE   I CD1 1 
ATOM   103   N N   . GLU   A  1 69  ? 43.24913  31.67180  -33.45234 1.000 85.61627  ?  69  GLU   I N   1 
ATOM   104   C CA  . GLU   A  1 69  ? 44.43763  32.40046  -33.86245 1.000 60.17924  ?  69  GLU   I CA  1 
ATOM   105   C C   . GLU   A  1 69  ? 45.71824  31.81904  -33.27802 1.000 69.52980  ?  69  GLU   I C   1 
ATOM   106   O O   . GLU   A  1 69  ? 46.79778  32.10336  -33.79951 1.000 70.03715  ?  69  GLU   I O   1 
ATOM   107   C CB  . GLU   A  1 69  ? 44.28707  33.86625  -33.45185 1.000 66.51931  ?  69  GLU   I CB  1 
ATOM   108   C CG  . GLU   A  1 69  ? 43.32312  34.64560  -34.34607 1.000 52.52663  ?  69  GLU   I CG  1 
ATOM   109   C CD  . GLU   A  1 69  ? 42.80019  35.93559  -33.71044 1.000 93.73716  ?  69  GLU   I CD  1 
ATOM   110   O OE1 . GLU   A  1 69  ? 43.11578  36.20685  -32.51937 1.000 66.18513  ?  69  GLU   I OE1 1 
ATOM   111   O OE2 . GLU   A  1 69  ? 42.06047  36.67061  -34.41277 1.000 72.99144  ?  69  GLU   I OE2 1 
ATOM   112   N N   . SER   A  1 70  ? 45.62152  31.00074  -32.22856 1.000 70.21938  ?  70  SER   I N   1 
ATOM   113   C CA  . SER   A  1 70  ? 46.79921  30.46839  -31.55453 1.000 42.00105  ?  70  SER   I CA  1 
ATOM   114   C C   . SER   A  1 70  ? 47.50839  29.36231  -32.32981 1.000 70.76322  ?  70  SER   I C   1 
ATOM   115   O O   . SER   A  1 70  ? 48.64734  29.03362  -31.98378 1.000 55.49610  ?  70  SER   I O   1 
ATOM   116   C CB  . SER   A  1 70  ? 46.41731  29.91663  -30.17698 1.000 54.60003  ?  70  SER   I CB  1 
ATOM   117   O OG  . SER   A  1 70  ? 45.62552  28.74085  -30.30638 1.000 75.93744  ?  70  SER   I OG  1 
ATOM   118   N N   . ASP   A  1 71  ? 46.87046  28.76004  -33.33380 1.000 47.11182  ?  71  ASP   I N   1 
ATOM   119   C CA  . ASP   A  1 71  ? 47.43664  27.61034  -34.04402 1.000 42.39419  ?  71  ASP   I CA  1 
ATOM   120   C C   . ASP   A  1 71  ? 47.28211  27.87323  -35.53535 1.000 48.66314  ?  71  ASP   I C   1 
ATOM   121   O O   . ASP   A  1 71  ? 46.13844  27.96148  -36.03690 1.000 48.56633  ?  71  ASP   I O   1 
ATOM   122   C CB  . ASP   A  1 71  ? 46.74878  26.29800  -33.62890 1.000 51.55971  ?  71  ASP   I CB  1 
ATOM   123   C CG  . ASP   A  1 71  ? 47.28311  25.04786  -34.37610 1.000 90.81958  ?  71  ASP   I CG  1 
ATOM   124   O OD1 . ASP   A  1 71  ? 47.77898  25.13731  -35.53092 1.000 54.74370  ?  71  ASP   I OD1 1 
ATOM   125   O OD2 . ASP   A  1 71  ? 47.17851  23.93794  -33.80376 1.000 68.64866  ?  71  ASP   I OD2 1 
ATOM   126   N N   . PRO   A  1 72  ? 48.37773  27.97370  -36.27900 1.000 56.69952  ?  72  PRO   I N   1 
ATOM   127   C CA  . PRO   A  1 72  ? 48.26373  28.32039  -37.70652 1.000 54.94824  ?  72  PRO   I CA  1 
ATOM   128   C C   . PRO   A  1 72  ? 47.43827  27.32987  -38.52010 1.000 45.80145  ?  72  PRO   I C   1 
ATOM   129   O O   . PRO   A  1 72  ? 46.79177  27.73633  -39.49206 1.000 51.54054  ?  72  PRO   I O   1 
ATOM   130   C CB  . PRO   A  1 72  ? 49.72687  28.36354  -38.16885 1.000 41.16645  ?  72  PRO   I CB  1 
ATOM   131   C CG  . PRO   A  1 72  ? 50.48902  27.55485  -37.13728 1.000 47.01116  ?  72  PRO   I CG  1 
ATOM   132   C CD  . PRO   A  1 72  ? 49.76391  27.73604  -35.84522 1.000 32.96644  ?  72  PRO   I CD  1 
ATOM   133   N N   . VAL   A  1 73  ? 47.42982  26.04426  -38.15739 1.000 55.65223  ?  73  VAL   I N   1 
ATOM   134   C CA  . VAL   A  1 73  ? 46.61835  25.07445  -38.89200 1.000 66.63765  ?  73  VAL   I CA  1 
ATOM   135   C C   . VAL   A  1 73  ? 45.13555  25.30850  -38.63422 1.000 74.23281  ?  73  VAL   I C   1 
ATOM   136   O O   . VAL   A  1 73  ? 44.32101  25.30821  -39.56818 1.000 45.25211  ?  73  VAL   I O   1 
ATOM   137   C CB  . VAL   A  1 73  ? 47.01785  23.64181  -38.51294 1.000 63.38150  ?  73  VAL   I CB  1 
ATOM   138   C CG1 . VAL   A  1 73  ? 46.22527  22.66414  -39.33495 1.000 40.43308  ?  73  VAL   I CG1 1 
ATOM   139   C CG2 . VAL   A  1 73  ? 48.49094  23.43725  -38.72663 1.000 38.27152  ?  73  VAL   I CG2 1 
ATOM   140   N N   . VAL   A  1 74  ? 44.76475  25.47235  -37.35662 1.000 55.88160  ?  74  VAL   I N   1 
ATOM   141   C CA  . VAL   A  1 74  ? 43.38442  25.78780  -36.99427 1.000 46.47895  ?  74  VAL   I CA  1 
ATOM   142   C C   . VAL   A  1 74  ? 42.94925  27.07553  -37.67858 1.000 57.31130  ?  74  VAL   I C   1 
ATOM   143   O O   . VAL   A  1 74  ? 41.88409  27.14267  -38.30823 1.000 61.94115  ?  74  VAL   I O   1 
ATOM   144   C CB  . VAL   A  1 74  ? 43.24814  25.89349  -35.46163 1.000 48.60550  ?  74  VAL   I CB  1 
ATOM   145   C CG1 . VAL   A  1 74  ? 41.84027  26.33826  -35.04451 1.000 31.53363  ?  74  VAL   I CG1 1 
ATOM   146   C CG2 . VAL   A  1 74  ? 43.58466  24.58863  -34.82294 1.000 38.37024  ?  74  VAL   I CG2 1 
ATOM   147   N N   . HIS   A  1 75  ? 43.77971  28.11609  -37.56446 1.000 61.96513  ?  75  HIS   I N   1 
ATOM   148   C CA  . HIS   A  1 75  ? 43.49576  29.39727  -38.20212 1.000 54.66561  ?  75  HIS   I CA  1 
ATOM   149   C C   . HIS   A  1 75  ? 43.21961  29.22551  -39.69472 1.000 43.50627  ?  75  HIS   I C   1 
ATOM   150   O O   . HIS   A  1 75  ? 42.23871  29.75965  -40.22964 1.000 50.42095  ?  75  HIS   I O   1 
ATOM   151   C CB  . HIS   A  1 75  ? 44.67792  30.33452  -37.97186 1.000 46.23843  ?  75  HIS   I CB  1 
ATOM   152   C CG  . HIS   A  1 75  ? 44.38093  31.76800  -38.26358 1.000 79.06610  ?  75  HIS   I CG  1 
ATOM   153   N ND1 . HIS   A  1 75  ? 45.06147  32.80018  -37.66034 1.000 88.51403  ?  75  HIS   I ND1 1 
ATOM   154   C CD2 . HIS   A  1 75  ? 43.47601  32.34257  -39.08919 1.000 80.51350  ?  75  HIS   I CD2 1 
ATOM   155   C CE1 . HIS   A  1 75  ? 44.58428  33.95000  -38.09859 1.000 76.00651  ?  75  HIS   I CE1 1 
ATOM   156   N NE2 . HIS   A  1 75  ? 43.62616  33.70029  -38.97141 1.000 62.68634  ?  75  HIS   I NE2 1 
ATOM   157   N N   . GLN   A  1 76  ? 44.07630  28.46767  -40.38320 1.000 59.45341  ?  76  GLN   I N   1 
ATOM   158   C CA  . GLN   A  1 76  ? 43.87623  28.25197  -41.81000 1.000 38.12850  ?  76  GLN   I CA  1 
ATOM   159   C C   . GLN   A  1 76  ? 42.54043  27.56488  -42.07455 1.000 61.32260  ?  76  GLN   I C   1 
ATOM   160   O O   . GLN   A  1 76  ? 41.82622  27.92519  -43.01830 1.000 50.58958  ?  76  GLN   I O   1 
ATOM   161   C CB  . GLN   A  1 76  ? 45.03994  27.43693  -42.38151 1.000 63.54942  ?  76  GLN   I CB  1 
ATOM   162   C CG  . GLN   A  1 76  ? 45.09981  27.44825  -43.89820 1.000 39.52746  ?  76  GLN   I CG  1 
ATOM   163   C CD  . GLN   A  1 76  ? 45.09696  28.84848  -44.47000 1.000 97.79650  ?  76  GLN   I CD  1 
ATOM   164   O OE1 . GLN   A  1 76  ? 45.94975  29.67238  -44.12664 1.000 57.44298  ?  76  GLN   I OE1 1 
ATOM   165   N NE2 . GLN   A  1 76  ? 44.13488  29.12974  -45.34423 1.000 49.51828  ?  76  GLN   I NE2 1 
ATOM   166   N N   . GLU   A  1 77  ? 42.17767  26.58507  -41.23529 1.000 51.40649  ?  77  GLU   I N   1 
ATOM   167   C CA  . GLU   A  1 77  ? 40.87596  25.94024  -41.36897 1.000 42.40031  ?  77  GLU   I CA  1 
ATOM   168   C C   . GLU   A  1 77  ? 39.74250  26.95627  -41.24422 1.000 69.76112  ?  77  GLU   I C   1 
ATOM   169   O O   . GLU   A  1 77  ? 38.76626  26.90490  -42.00699 1.000 36.36675  ?  77  GLU   I O   1 
ATOM   170   C CB  . GLU   A  1 77  ? 40.73804  24.82929  -40.33198 1.000 41.94123  ?  77  GLU   I CB  1 
ATOM   171   C CG  . GLU   A  1 77  ? 41.43513  23.54611  -40.75850 1.000 37.03691  ?  77  GLU   I CG  1 
ATOM   172   C CD  . GLU   A  1 77  ? 41.70216  22.56943  -39.61164 1.000 69.42594  ?  77  GLU   I CD  1 
ATOM   173   O OE1 . GLU   A  1 77  ? 41.37735  22.90644  -38.44546 1.000 51.08490  ?  77  GLU   I OE1 1 
ATOM   174   O OE2 . GLU   A  1 77  ? 42.23826  21.45981  -39.88983 1.000 44.84292  ?  77  GLU   I OE2 1 
ATOM   175   N N   . PHE   A  1 78  ? 39.87313  27.91871  -40.32140 1.000 46.86823  ?  78  PHE   I N   1 
ATOM   176   C CA  . PHE   A  1 78  ? 38.85401  28.95195  -40.14866 1.000 67.93505  ?  78  PHE   I CA  1 
ATOM   177   C C   . PHE   A  1 78  ? 38.93967  30.04519  -41.20039 1.000 67.20229  ?  78  PHE   I C   1 
ATOM   178   O O   . PHE   A  1 78  ? 38.16718  31.00838  -41.14687 1.000 74.86387  ?  78  PHE   I O   1 
ATOM   179   C CB  . PHE   A  1 78  ? 38.92888  29.57443  -38.74586 1.000 48.51302  ?  78  PHE   I CB  1 
ATOM   180   C CG  . PHE   A  1 78  ? 38.13830  28.82519  -37.73525 1.000 66.97197  ?  78  PHE   I CG  1 
ATOM   181   C CD1 . PHE   A  1 78  ? 36.77574  29.07151  -37.59006 1.000 53.30998  ?  78  PHE   I CD1 1 
ATOM   182   C CD2 . PHE   A  1 78  ? 38.73758  27.82303  -36.96711 1.000 41.76110  ?  78  PHE   I CD2 1 
ATOM   183   C CE1 . PHE   A  1 78  ? 36.01672  28.35621  -36.66070 1.000 51.21031  ?  78  PHE   I CE1 1 
ATOM   184   C CE2 . PHE   A  1 78  ? 37.99238  27.09301  -36.03876 1.000 61.54487  ?  78  PHE   I CE2 1 
ATOM   185   C CZ  . PHE   A  1 78  ? 36.62657  27.35854  -35.87782 1.000 48.95173  ?  78  PHE   I CZ  1 
ATOM   186   N N   . ILE   A  1 79  ? 39.84387  29.92616  -42.16025 1.000 53.53593  ?  79  ILE   I N   1 
ATOM   187   C CA  . ILE   A  1 79  ? 39.79721  30.74112  -43.35407 1.000 47.18580  ?  79  ILE   I CA  1 
ATOM   188   C C   . ILE   A  1 79  ? 39.21531  29.95440  -44.51566 1.000 63.92130  ?  79  ILE   I C   1 
ATOM   189   O O   . ILE   A  1 79  ? 38.22734  30.36550  -45.12723 1.000 40.25546  ?  79  ILE   I O   1 
ATOM   190   C CB  . ILE   A  1 79  ? 41.20090  31.29133  -43.69408 1.000 55.95063  ?  79  ILE   I CB  1 
ATOM   191   C CG1 . ILE   A  1 79  ? 41.59378  32.35932  -42.68990 1.000 42.39762  ?  79  ILE   I CG1 1 
ATOM   192   C CG2 . ILE   A  1 79  ? 41.22054  31.83454  -45.10282 1.000 43.20066  ?  79  ILE   I CG2 1 
ATOM   193   C CD1 . ILE   A  1 79  ? 43.04024  32.64185  -42.69753 1.000 39.64641  ?  79  ILE   I CD1 1 
ATOM   194   N N   . ASP   A  1 80  ? 39.79849  28.78365  -44.80268 1.000 41.20406  ?  80  ASP   I N   1 
ATOM   195   C CA  . ASP   A  1 80  ? 39.37502  28.01174  -45.96350 1.000 57.30420  ?  80  ASP   I CA  1 
ATOM   196   C C   . ASP   A  1 80  ? 37.89684  27.65411  -45.90557 1.000 48.48126  ?  80  ASP   I C   1 
ATOM   197   O O   . ASP   A  1 80  ? 37.23846  27.59571  -46.95204 1.000 57.63458  ?  80  ASP   I O   1 
ATOM   198   C CB  . ASP   A  1 80  ? 40.22985  26.75551  -46.08094 1.000 51.10502  ?  80  ASP   I CB  1 
ATOM   199   C CG  . ASP   A  1 80  ? 41.72367  27.07161  -46.23526 1.000 69.39602  ?  80  ASP   I CG  1 
ATOM   200   O OD1 . ASP   A  1 80  ? 42.07397  28.23370  -46.53090 1.000 67.58188  ?  80  ASP   I OD1 1 
ATOM   201   O OD2 . ASP   A  1 80  ? 42.54997  26.14067  -46.04970 1.000 75.27342  ?  80  ASP   I OD2 1 
ATOM   202   N N   . MET   A  1 81  ? 37.35315  27.42223  -44.69878 1.000 54.27184  ?  81  MET   I N   1 
ATOM   203   C CA  . MET   A  1 81  ? 35.95639  27.00767  -44.57501 1.000 47.97726  ?  81  MET   I CA  1 
ATOM   204   C C   . MET   A  1 81  ? 34.98119  28.08855  -45.06309 1.000 70.75158  ?  81  MET   I C   1 
ATOM   205   O O   . MET   A  1 81  ? 33.82236  27.75764  -45.36839 1.000 58.11327  ?  81  MET   I O   1 
ATOM   206   C CB  . MET   A  1 81  ? 35.61845  26.61441  -43.12036 1.000 47.98226  ?  81  MET   I CB  1 
ATOM   207   C CG  . MET   A  1 81  ? 35.58024  27.76185  -42.11069 1.000 54.44462  ?  81  MET   I CG  1 
ATOM   208   S SD  . MET   A  1 81  ? 35.09121  27.33434  -40.39924 1.000 54.32899  ?  81  MET   I SD  1 
ATOM   209   C CE  . MET   A  1 81  ? 36.24839  26.02353  -39.96933 1.000 50.94704  ?  81  MET   I CE  1 
ATOM   210   N N   . PHE   A  1 82  ? 35.42332  29.35503  -45.18980 1.000 49.93779  ?  82  PHE   I N   1 
ATOM   211   C CA  . PHE   A  1 82  ? 34.56733  30.44136  -45.64571 1.000 75.33797  ?  82  PHE   I CA  1 
ATOM   212   C C   . PHE   A  1 82  ? 34.68444  30.71506  -47.13607 1.000 48.19919  ?  82  PHE   I C   1 
ATOM   213   O O   . PHE   A  1 82  ? 34.04332  31.65268  -47.62635 1.000 111.58074 ?  82  PHE   I O   1 
ATOM   214   C CB  . PHE   A  1 82  ? 34.90439  31.70497  -44.87705 1.000 50.83059  ?  82  PHE   I CB  1 
ATOM   215   C CG  . PHE   A  1 82  ? 34.39020  31.70608  -43.49754 1.000 93.98532  ?  82  PHE   I CG  1 
ATOM   216   C CD1 . PHE   A  1 82  ? 33.07492  32.05550  -43.24764 1.000 47.91079  ?  82  PHE   I CD1 1 
ATOM   217   C CD2 . PHE   A  1 82  ? 35.20422  31.33307  -42.44843 1.000 50.52298  ?  82  PHE   I CD2 1 
ATOM   218   C CE1 . PHE   A  1 82  ? 32.58416  32.04797  -41.96499 1.000 66.67364  ?  82  PHE   I CE1 1 
ATOM   219   C CE2 . PHE   A  1 82  ? 34.72383  31.32288  -41.16803 1.000 67.94045  ?  82  PHE   I CE2 1 
ATOM   220   C CZ  . PHE   A  1 82  ? 33.40469  31.67709  -40.92406 1.000 43.64474  ?  82  PHE   I CZ  1 
ATOM   221   N N   . GLU   A  1 83  ? 35.48422  29.92486  -47.85985 1.000 70.36149  ?  83  GLU   I N   1 
ATOM   222   C CA  . GLU   A  1 83  ? 35.83851  30.24418  -49.23899 1.000 75.12605  ?  83  GLU   I CA  1 
ATOM   223   C C   . GLU   A  1 83  ? 34.61189  30.51476  -50.08557 1.000 83.45471  ?  83  GLU   I C   1 
ATOM   224   O O   . GLU   A  1 83  ? 33.72621  29.67026  -50.19513 1.000 59.71901  ?  83  GLU   I O   1 
ATOM   225   C CB  . GLU   A  1 83  ? 36.67190  29.11881  -49.84370 1.000 50.45989  ?  83  GLU   I CB  1 
ATOM   226   N N   . GLY   A  1 84  ? 34.56409  31.71075  -50.67169 1.000 94.41969  ?  84  GLY   I N   1 
ATOM   227   C CA  . GLY   A  1 84  ? 33.47564  32.08920  -51.54996 1.000 58.77683  ?  84  GLY   I CA  1 
ATOM   228   C C   . GLY   A  1 84  ? 32.13993  32.35461  -50.89833 1.000 91.86266  ?  84  GLY   I C   1 
ATOM   229   O O   . GLY   A  1 84  ? 31.15636  32.58254  -51.60527 1.000 76.97990  ?  84  GLY   I O   1 
ATOM   230   N N   . ILE   A  1 85  ? 32.06839  32.33367  -49.57347 1.000 101.33155 ?  85  ILE   I N   1 
ATOM   231   C CA  . ILE   A  1 85  ? 30.82012  32.62872  -48.88057 1.000 80.94137  ?  85  ILE   I CA  1 
ATOM   232   C C   . ILE   A  1 85  ? 30.55155  34.12057  -48.96879 1.000 91.15061  ?  85  ILE   I C   1 
ATOM   233   O O   . ILE   A  1 85  ? 31.36369  34.95112  -48.53366 1.000 85.29728  ?  85  ILE   I O   1 
ATOM   234   C CB  . ILE   A  1 85  ? 30.87323  32.14487  -47.42480 1.000 74.35735  ?  85  ILE   I CB  1 
ATOM   235   C CG1 . ILE   A  1 85  ? 31.01353  30.61997  -47.40170 1.000 89.63196  ?  85  ILE   I CG1 1 
ATOM   236   C CG2 . ILE   A  1 85  ? 29.66288  32.66260  -46.62656 1.000 76.47361  ?  85  ILE   I CG2 1 
ATOM   237   C CD1 . ILE   A  1 85  ? 30.63170  29.97161  -46.11076 1.000 81.53755  ?  85  ILE   I CD1 1 
ATOM   238   N N   . GLN   A  1 86  ? 29.43763  34.45928  -49.60051 1.000 89.55597  ?  86  GLN   I N   1 
ATOM   239   C CA  . GLN   A  1 86  ? 29.09734  35.84756  -49.82858 1.000 121.17115 ?  86  GLN   I CA  1 
ATOM   240   C C   . GLN   A  1 86  ? 28.22056  36.42545  -48.71712 1.000 72.01057  ?  86  GLN   I C   1 
ATOM   241   O O   . GLN   A  1 86  ? 28.21041  37.64783  -48.52937 1.000 118.70718 ?  86  GLN   I O   1 
ATOM   242   C CB  . GLN   A  1 86  ? 28.39230  36.01146  -51.18027 1.000 85.30664  ?  86  GLN   I CB  1 
ATOM   243   N N   . ASP   A  1 87  ? 27.53870  35.58813  -47.93281 1.000 107.59693 ?  87  ASP   I N   1 
ATOM   244   C CA  . ASP   A  1 87  ? 26.65519  36.06835  -46.87704 1.000 73.86933  ?  87  ASP   I CA  1 
ATOM   245   C C   . ASP   A  1 87  ? 27.32871  36.06434  -45.50857 1.000 63.02117  ?  87  ASP   I C   1 
ATOM   246   O O   . ASP   A  1 87  ? 28.39018  35.47653  -45.29326 1.000 83.40884  ?  87  ASP   I O   1 
ATOM   247   C CB  . ASP   A  1 87  ? 25.38680  35.21675  -46.80829 1.000 66.12389  ?  87  ASP   I CB  1 
ATOM   248   C CG  . ASP   A  1 87  ? 24.77692  35.00255  -48.16104 1.000 138.88938 ?  87  ASP   I CG  1 
ATOM   249   O OD1 . ASP   A  1 87  ? 25.07730  35.80566  -49.07627 1.000 119.14509 ?  87  ASP   I OD1 1 
ATOM   250   O OD2 . ASP   A  1 87  ? 24.00720  34.01113  -48.30072 1.000 117.18430 ?  87  ASP   I OD2 1 
ATOM   251   N N   . SER   A  1 88  ? 26.66090  36.70400  -44.57665 1.000 67.88040  ?  88  SER   I N   1 
ATOM   252   C CA  . SER   A  1 88  ? 27.11887  36.76616  -43.20340 1.000 56.95803  ?  88  SER   I CA  1 
ATOM   253   C C   . SER   A  1 88  ? 26.79937  35.45161  -42.48452 1.000 99.34655  ?  88  SER   I C   1 
ATOM   254   O O   . SER   A  1 88  ? 25.65281  34.98314  -42.53490 1.000 66.84675  ?  88  SER   I O   1 
ATOM   255   C CB  . SER   A  1 88  ? 26.46293  37.94590  -42.50212 1.000 58.00713  ?  88  SER   I CB  1 
ATOM   256   O OG  . SER   A  1 88  ? 27.43109  38.87191  -42.03540 1.000 74.13742  ?  88  SER   I OG  1 
ATOM   257   N N   . PRO   A  1 89  ? 27.78785  34.81425  -41.80474 1.000 82.95504  ?  89  PRO   I N   1 
ATOM   258   C CA  . PRO   A  1 89  ? 29.18391  35.22341  -41.58521 1.000 59.47154  ?  89  PRO   I CA  1 
ATOM   259   C C   . PRO   A  1 89  ? 30.10133  34.99247  -42.78888 1.000 87.17667  ?  89  PRO   I C   1 
ATOM   260   O O   . PRO   A  1 89  ? 30.05486  33.93203  -43.40840 1.000 69.77512  ?  89  PRO   I O   1 
ATOM   261   C CB  . PRO   A  1 89  ? 29.64459  34.33422  -40.42085 1.000 81.84021  ?  89  PRO   I CB  1 
ATOM   262   C CG  . PRO   A  1 89  ? 28.51778  33.34287  -40.15219 1.000 79.50986  ?  89  PRO   I CG  1 
ATOM   263   C CD  . PRO   A  1 89  ? 27.56158  33.45489  -41.30107 1.000 74.10628  ?  89  PRO   I CD  1 
ATOM   264   N N   . ARG   A  1 90  ? 30.97929  35.94458  -43.11456 1.000 73.87266  ?  90  ARG   I N   1 
ATOM   265   C CA  . ARG   A  1 90  ? 31.93487  35.75520  -44.19827 1.000 90.87163  ?  90  ARG   I CA  1 
ATOM   266   C C   . ARG   A  1 90  ? 33.33505  35.41275  -43.70244 1.000 81.55654  ?  90  ARG   I C   1 
ATOM   267   O O   . ARG   A  1 90  ? 34.17051  34.98291  -44.49377 1.000 81.14393  ?  90  ARG   I O   1 
ATOM   268   C CB  . ARG   A  1 90  ? 32.00954  37.00483  -45.08622 1.000 75.26277  ?  90  ARG   I CB  1 
ATOM   269   N N   . ASN   A  1 91  ? 33.62057  35.56720  -42.41742 1.000 58.61390  ?  91  ASN   I N   1 
ATOM   270   C CA  . ASN   A  1 91  ? 34.91787  35.17929  -41.88639 1.000 63.09404  ?  91  ASN   I CA  1 
ATOM   271   C C   . ASN   A  1 91  ? 34.71251  34.77418  -40.44485 1.000 61.72058  ?  91  ASN   I C   1 
ATOM   272   O O   . ASN   A  1 91  ? 33.59792  34.83032  -39.90574 1.000 68.27390  ?  91  ASN   I O   1 
ATOM   273   C CB  . ASN   A  1 91  ? 35.93424  36.31821  -41.99439 1.000 55.09544  ?  91  ASN   I CB  1 
ATOM   274   C CG  . ASN   A  1 91  ? 35.33978  37.63053  -41.53481 1.000 65.77295  ?  91  ASN   I CG  1 
ATOM   275   O OD1 . ASN   A  1 91  ? 35.01478  37.81229  -40.35679 1.000 75.96298  ?  91  ASN   I OD1 1 
ATOM   276   N ND2 . ASN   A  1 91  ? 35.16808  38.54466  -42.46560 1.000 61.79866  ?  91  ASN   I ND2 1 
ATOM   277   N N   . TYR   A  1 92  ? 35.80827  34.36466  -39.81693 1.000 63.13378  ?  92  TYR   I N   1 
ATOM   278   C CA  . TYR   A  1 92  ? 35.67246  33.91957  -38.44456 1.000 56.87553  ?  92  TYR   I CA  1 
ATOM   279   C C   . TYR   A  1 92  ? 35.38962  35.09499  -37.51359 1.000 60.96950  ?  92  TYR   I C   1 
ATOM   280   O O   . TYR   A  1 92  ? 34.75554  34.91041  -36.46744 1.000 65.68612  ?  92  TYR   I O   1 
ATOM   281   C CB  . TYR   A  1 92  ? 36.89965  33.08530  -38.01875 1.000 46.09254  ?  92  TYR   I CB  1 
ATOM   282   C CG  . TYR   A  1 92  ? 38.18330  33.81406  -37.70453 1.000 51.55892  ?  92  TYR   I CG  1 
ATOM   283   C CD1 . TYR   A  1 92  ? 38.40046  34.36377  -36.44224 1.000 49.77683  ?  92  TYR   I CD1 1 
ATOM   284   C CD2 . TYR   A  1 92  ? 39.22517  33.87796  -38.64773 1.000 57.99272  ?  92  TYR   I CD2 1 
ATOM   285   C CE1 . TYR   A  1 92  ? 39.59056  35.00749  -36.13909 1.000 68.75823  ?  92  TYR   I CE1 1 
ATOM   286   C CE2 . TYR   A  1 92  ? 40.42185  34.51914  -38.34977 1.000 65.85303  ?  92  TYR   I CE2 1 
ATOM   287   C CZ  . TYR   A  1 92  ? 40.59479  35.08449  -37.09528 1.000 61.39639  ?  92  TYR   I CZ  1 
ATOM   288   O OH  . TYR   A  1 92  ? 41.75567  35.72650  -36.77530 1.000 78.15284  ?  92  TYR   I OH  1 
ATOM   289   N N   . GLN   A  1 93  ? 35.76343  36.31661  -37.90083 1.000 55.08232  ?  93  GLN   I N   1 
ATOM   290   C CA  . GLN   A  1 93  ? 35.45474  37.44999  -37.03201 1.000 67.69011  ?  93  GLN   I CA  1 
ATOM   291   C C   . GLN   A  1 93  ? 33.95742  37.73284  -37.00868 1.000 53.73868  ?  93  GLN   I C   1 
ATOM   292   O O   . GLN   A  1 93  ? 33.38573  38.00604  -35.94650 1.000 59.14879  ?  93  GLN   I O   1 
ATOM   293   C CB  . GLN   A  1 93  ? 36.21128  38.69915  -37.47201 1.000 48.56380  ?  93  GLN   I CB  1 
ATOM   294   C CG  . GLN   A  1 93  ? 37.66611  38.74597  -37.00363 1.000 65.29384  ?  93  GLN   I CG  1 
ATOM   295   C CD  . GLN   A  1 93  ? 38.63860  38.26043  -38.06808 1.000 184.60070 ?  93  GLN   I CD  1 
ATOM   296   O OE1 . GLN   A  1 93  ? 38.25461  37.56419  -39.02769 1.000 62.87347  ?  93  GLN   I OE1 1 
ATOM   297   N NE2 . GLN   A  1 93  ? 39.90850  38.62832  -37.90814 1.000 65.09275  ?  93  GLN   I NE2 1 
ATOM   298   N N   . GLU   A  1 94  ? 33.29580  37.67416  -38.17018 1.000 68.65617  ?  94  GLU   I N   1 
ATOM   299   C CA  . GLU   A  1 94  ? 31.84664  37.86063  -38.18488 1.000 40.99897  ?  94  GLU   I CA  1 
ATOM   300   C C   . GLU   A  1 94  ? 31.15570  36.71688  -37.46787 1.000 75.50432  ?  94  GLU   I C   1 
ATOM   301   O O   . GLU   A  1 94  ? 30.14273  36.91573  -36.78735 1.000 72.56290  ?  94  GLU   I O   1 
ATOM   302   C CB  . GLU   A  1 94  ? 31.32430  37.93879  -39.61103 1.000 72.44011  ?  94  GLU   I CB  1 
ATOM   303   C CG  . GLU   A  1 94  ? 31.53567  39.27194  -40.26158 1.000 93.98295  ?  94  GLU   I CG  1 
ATOM   304   C CD  . GLU   A  1 94  ? 30.88376  39.30892  -41.62532 1.000 156.68174 ?  94  GLU   I CD  1 
ATOM   305   O OE1 . GLU   A  1 94  ? 29.83255  38.62418  -41.77805 1.000 65.14723  ?  94  GLU   I OE1 1 
ATOM   306   O OE2 . GLU   A  1 94  ? 31.42753  39.99823  -42.52374 1.000 118.85438 ?  94  GLU   I OE2 1 
ATOM   307   N N   . LEU   A  1 95  ? 31.67769  35.49550  -37.63196 1.000 76.27530  ?  95  LEU   I N   1 
ATOM   308   C CA  . LEU   A  1 95  ? 31.14397  34.36023  -36.88853 1.000 57.31810  ?  95  LEU   I CA  1 
ATOM   309   C C   . LEU   A  1 95  ? 31.12863  34.66182  -35.39838 1.000 61.44655  ?  95  LEU   I C   1 
ATOM   310   O O   . LEU   A  1 95  ? 30.09001  34.52813  -34.73672 1.000 57.45613  ?  95  LEU   I O   1 
ATOM   311   C CB  . LEU   A  1 95  ? 31.96365  33.10350  -37.17281 1.000 64.42721  ?  95  LEU   I CB  1 
ATOM   312   C CG  . LEU   A  1 95  ? 31.35840  31.82672  -36.57115 1.000 64.49452  ?  95  LEU   I CG  1 
ATOM   313   C CD1 . LEU   A  1 95  ? 29.97905  31.52482  -37.17079 1.000 58.78298  ?  95  LEU   I CD1 1 
ATOM   314   C CD2 . LEU   A  1 95  ? 32.31537  30.68216  -36.81217 1.000 49.98157  ?  95  LEU   I CD2 1 
ATOM   315   N N   . CYS   A  1 96  ? 32.26747  35.13269  -34.86502 1.000 49.89487  ?  96  CYS   I N   1 
ATOM   316   C CA  . CYS   A  1 96  ? 32.33801  35.45702  -33.44448 1.000 60.68389  ?  96  CYS   I CA  1 
ATOM   317   C C   . CYS   A  1 96  ? 31.34608  36.54936  -33.06325 1.000 60.88300  ?  96  CYS   I C   1 
ATOM   318   O O   . CYS   A  1 96  ? 30.75770  36.50598  -31.97421 1.000 80.22223  ?  96  CYS   I O   1 
ATOM   319   C CB  . CYS   A  1 96  ? 33.75117  35.87882  -33.07069 1.000 54.21731  ?  96  CYS   I CB  1 
ATOM   320   S SG  . CYS   A  1 96  ? 35.00262  34.57492  -33.12466 1.000 69.92170  ?  96  CYS   I SG  1 
ATOM   321   N N   . ASN   A  1 97  ? 31.16232  37.55215  -33.93356 1.000 66.25616  ?  97  ASN   I N   1 
ATOM   322   C CA  . ASN   A  1 97  ? 30.22859  38.62956  -33.60830 1.000 56.52628  ?  97  ASN   I CA  1 
ATOM   323   C C   . ASN   A  1 97  ? 28.79107  38.12683  -33.59175 1.000 81.35581  ?  97  ASN   I C   1 
ATOM   324   O O   . ASN   A  1 97  ? 28.00497  38.51637  -32.71794 1.000 62.76814  ?  97  ASN   I O   1 
ATOM   325   C CB  . ASN   A  1 97  ? 30.36659  39.78445  -34.59572 1.000 68.05285  ?  97  ASN   I CB  1 
ATOM   326   C CG  . ASN   A  1 97  ? 31.64095  40.56084  -34.40251 1.000 107.52751 ?  97  ASN   I CG  1 
ATOM   327   O OD1 . ASN   A  1 97  ? 32.12903  40.70486  -33.27772 1.000 80.09341  ?  97  ASN   I OD1 1 
ATOM   328   N ND2 . ASN   A  1 97  ? 32.19569  41.06944  -35.50021 1.000 65.09877  ?  97  ASN   I ND2 1 
ATOM   329   N N   . MET   A  1 98  ? 28.42898  37.26192  -34.55007 1.000 42.01305  ?  98  MET   I N   1 
ATOM   330   C CA  . MET   A  1 98  ? 27.07955  36.70802  -34.56386 1.000 38.34260  ?  98  MET   I CA  1 
ATOM   331   C C   . MET   A  1 98  ? 26.84331  35.78977  -33.36500 1.000 76.38827  ?  98  MET   I C   1 
ATOM   332   O O   . MET   A  1 98  ? 25.73862  35.77436  -32.80612 1.000 56.24719  ?  98  MET   I O   1 
ATOM   333   C CB  . MET   A  1 98  ? 26.82920  35.98325  -35.89207 1.000 45.19962  ?  98  MET   I CB  1 
ATOM   334   C CG  . MET   A  1 98  ? 26.82715  36.93605  -37.09629 1.000 34.19343  ?  98  MET   I CG  1 
ATOM   335   S SD  . MET   A  1 98  ? 26.76359  36.20596  -38.73601 1.000 65.29839  ?  98  MET   I SD  1 
ATOM   336   C CE  . MET   A  1 98  ? 25.04393  35.73090  -38.84076 1.000 51.99606  ?  98  MET   I CE  1 
ATOM   337   N N   . PHE   A  1 99  ? 27.86831  35.02934  -32.94410 1.000 53.62225  ?  99  PHE   I N   1 
ATOM   338   C CA  . PHE   A  1 99  ? 27.75667  34.24735  -31.70959 1.000 49.65075  ?  99  PHE   I CA  1 
ATOM   339   C C   . PHE   A  1 99  ? 27.40904  35.15470  -30.53560 1.000 58.99838  ?  99  PHE   I C   1 
ATOM   340   O O   . PHE   A  1 99  ? 26.57764  34.81254  -29.68238 1.000 57.86339  ?  99  PHE   I O   1 
ATOM   341   C CB  . PHE   A  1 99  ? 29.06632  33.49790  -31.39535 1.000 48.12667  ?  99  PHE   I CB  1 
ATOM   342   C CG  . PHE   A  1 99  ? 29.29958  32.25044  -32.21091 1.000 56.33905  ?  99  PHE   I CG  1 
ATOM   343   C CD1 . PHE   A  1 99  ? 28.35189  31.77979  -33.12585 1.000 46.16469  ?  99  PHE   I CD1 1 
ATOM   344   C CD2 . PHE   A  1 99  ? 30.48743  31.54026  -32.05233 1.000 54.98977  ?  99  PHE   I CD2 1 
ATOM   345   C CE1 . PHE   A  1 99  ? 28.58414  30.63301  -33.87323 1.000 61.71024  ?  99  PHE   I CE1 1 
ATOM   346   C CE2 . PHE   A  1 99  ? 30.73040  30.38741  -32.79224 1.000 45.30397  ?  99  PHE   I CE2 1 
ATOM   347   C CZ  . PHE   A  1 99  ? 29.77590  29.93688  -33.71581 1.000 49.40770  ?  99  PHE   I CZ  1 
ATOM   348   N N   . ASN   A  1 100 ? 28.05955  36.32254  -30.48069 1.000 52.51535  ?  100 ASN   I N   1 
ATOM   349   C CA  . ASN   A  1 100 ? 27.85489  37.25901  -29.38349 1.000 56.76813  ?  100 ASN   I CA  1 
ATOM   350   C C   . ASN   A  1 100 ? 26.41203  37.76416  -29.33391 1.000 60.55275  ?  100 ASN   I C   1 
ATOM   351   O O   . ASN   A  1 100 ? 25.87079  37.97659  -28.23924 1.000 67.80856  ?  100 ASN   I O   1 
ATOM   352   C CB  . ASN   A  1 100 ? 28.86074  38.40725  -29.50608 1.000 56.25598  ?  100 ASN   I CB  1 
ATOM   353   C CG  . ASN   A  1 100 ? 29.04658  39.15587  -28.20651 1.000 67.70788  ?  100 ASN   I CG  1 
ATOM   354   O OD1 . ASN   A  1 100 ? 29.53203  38.60846  -27.21057 1.000 80.35450  ?  100 ASN   I OD1 1 
ATOM   355   N ND2 . ASN   A  1 100 ? 28.67196  40.42322  -28.21058 1.000 67.38788  ?  100 ASN   I ND2 1 
ATOM   356   N N   . ASP   A  1 101 ? 25.76204  37.92504  -30.49623 1.000 53.91391  ?  101 ASP   I N   1 
ATOM   357   C CA  . ASP   A  1 101 ? 24.33030  38.22723  -30.50350 1.000 47.63985  ?  101 ASP   I CA  1 
ATOM   358   C C   . ASP   A  1 101 ? 23.50967  37.01402  -30.08328 1.000 70.30074  ?  101 ASP   I C   1 
ATOM   359   O O   . ASP   A  1 101 ? 22.63849  37.11880  -29.20783 1.000 61.97500  ?  101 ASP   I O   1 
ATOM   360   C CB  . ASP   A  1 101 ? 23.87429  38.70819  -31.88568 1.000 47.71512  ?  101 ASP   I CB  1 
ATOM   361   C CG  . ASP   A  1 101 ? 24.52949  40.01528  -32.31317 1.000 130.47526 ?  101 ASP   I CG  1 
ATOM   362   O OD1 . ASP   A  1 101 ? 24.83223  40.85859  -31.44029 1.000 65.76494  ?  101 ASP   I OD1 1 
ATOM   363   O OD2 . ASP   A  1 101 ? 24.72898  40.19979  -33.53912 1.000 75.42171  ?  101 ASP   I OD2 1 
ATOM   364   N N   . ILE   A  1 102 ? 23.77077  35.85370  -30.70794 1.000 61.25684  ?  102 ILE   I N   1 
ATOM   365   C CA  . ILE   A  1 102 ? 22.91949  34.67979  -30.50791 1.000 45.71300  ?  102 ILE   I CA  1 
ATOM   366   C C   . ILE   A  1 102 ? 22.88426  34.27548  -29.04358 1.000 71.27472  ?  102 ILE   I C   1 
ATOM   367   O O   . ILE   A  1 102 ? 21.81152  33.98851  -28.49851 1.000 54.81273  ?  102 ILE   I O   1 
ATOM   368   C CB  . ILE   A  1 102 ? 23.38393  33.50728  -31.38374 1.000 48.54194  ?  102 ILE   I CB  1 
ATOM   369   C CG1 . ILE   A  1 102 ? 23.22526  33.82469  -32.86577 1.000 33.35935  ?  102 ILE   I CG1 1 
ATOM   370   C CG2 . ILE   A  1 102 ? 22.58557  32.26993  -31.04796 1.000 37.77352  ?  102 ILE   I CG2 1 
ATOM   371   C CD1 . ILE   A  1 102 ? 23.52477  32.62150  -33.76426 1.000 54.44462  ?  102 ILE   I CD1 1 
ATOM   372   N N   . PHE   A  1 103 ? 24.05202  34.26144  -28.37886 1.000 46.59991  ?  103 PHE   I N   1 
ATOM   373   C CA  . PHE   A  1 103 ? 24.16400  33.77267  -27.00646 1.000 71.11319  ?  103 PHE   I CA  1 
ATOM   374   C C   . PHE   A  1 103 ? 23.55755  34.72404  -25.97918 1.000 48.99755  ?  103 PHE   I C   1 
ATOM   375   O O   . PHE   A  1 103 ? 23.56210  34.40853  -24.78468 1.000 57.35801  ?  103 PHE   I O   1 
ATOM   376   C CB  . PHE   A  1 103 ? 25.63091  33.51105  -26.65167 1.000 38.52095  ?  103 PHE   I CB  1 
ATOM   377   C CG  . PHE   A  1 103 ? 26.29593  32.45286  -27.50844 1.000 55.77904  ?  103 PHE   I CG  1 
ATOM   378   C CD1 . PHE   A  1 103 ? 25.54420  31.48877  -28.17723 1.000 51.75455  ?  103 PHE   I CD1 1 
ATOM   379   C CD2 . PHE   A  1 103 ? 27.67941  32.42969  -27.64628 1.000 43.80963  ?  103 PHE   I CD2 1 
ATOM   380   C CE1 . PHE   A  1 103 ? 26.16889  30.52809  -28.97131 1.000 64.00225  ?  103 PHE   I CE1 1 
ATOM   381   C CE2 . PHE   A  1 103 ? 28.31137  31.47523  -28.43598 1.000 55.94190  ?  103 PHE   I CE2 1 
ATOM   382   C CZ  . PHE   A  1 103 ? 27.55604  30.52483  -29.09747 1.000 55.22488  ?  103 PHE   I CZ  1 
ATOM   383   N N   . ARG   A  1 104 ? 23.01498  35.86622  -26.39180 1.000 75.93250  ?  104 ARG   I N   1 
ATOM   384   C CA  . ARG   A  1 104 ? 22.42371  36.81689  -25.46279 1.000 65.52051  ?  104 ARG   I CA  1 
ATOM   385   C C   . ARG   A  1 104 ? 20.90393  36.79375  -25.53336 1.000 43.41810  ?  104 ARG   I C   1 
ATOM   386   O O   . ARG   A  1 104 ? 20.23649  37.54354  -24.81127 1.000 71.19415  ?  104 ARG   I O   1 
ATOM   387   C CB  . ARG   A  1 104 ? 22.96105  38.22438  -25.74899 1.000 45.11805  ?  104 ARG   I CB  1 
ATOM   388   C CG  . ARG   A  1 104 ? 24.26824  38.55196  -25.05570 1.000 44.51115  ?  104 ARG   I CG  1 
ATOM   389   C CD  . ARG   A  1 104 ? 24.86119  39.85699  -25.61329 1.000 64.50351  ?  104 ARG   I CD  1 
ATOM   390   N NE  . ARG   A  1 104 ? 26.31309  39.93638  -25.52223 1.000 69.89446  ?  104 ARG   I NE  1 
ATOM   391   C CZ  . ARG   A  1 104 ? 26.96030  40.28644  -24.41721 1.000 97.20130  ?  104 ARG   I CZ  1 
ATOM   392   N NH1 . ARG   A  1 104 ? 26.31385  40.48959  -23.27791 1.000 65.90097  ?  104 ARG   I NH1 1 
ATOM   393   N NH2 . ARG   A  1 104 ? 28.28580  40.44159  -24.45534 1.000 56.36051  ?  104 ARG   I NH2 1 
ATOM   394   N N   . LYS   A  1 105 ? 20.34186  35.97657  -26.41888 1.000 48.76431  ?  105 LYS   I N   1 
ATOM   395   C CA  . LYS   A  1 105 ? 18.89784  35.93170  -26.55878 1.000 69.50165  ?  105 LYS   I CA  1 
ATOM   396   C C   . LYS   A  1 105 ? 18.45758  34.49634  -26.80026 1.000 52.03242  ?  105 LYS   I C   1 
ATOM   397   O O   . LYS   A  1 105 ? 19.25367  33.63935  -27.18121 1.000 56.65969  ?  105 LYS   I O   1 
ATOM   398   C CB  . LYS   A  1 105 ? 18.42484  36.88538  -27.66525 1.000 59.71888  ?  105 LYS   I CB  1 
ATOM   399   C CG  . LYS   A  1 105 ? 19.03350  36.61763  -29.00406 1.000 49.66371  ?  105 LYS   I CG  1 
ATOM   400   C CD  . LYS   A  1 105 ? 18.66094  37.69610  -30.02128 1.000 50.12867  ?  105 LYS   I CD  1 
ATOM   401   C CE  . LYS   A  1 105 ? 19.33820  39.00815  -29.70783 1.000 80.33584  ?  105 LYS   I CE  1 
ATOM   402   N NZ  . LYS   A  1 105 ? 19.50500  39.82424  -30.93994 1.000 93.18875  ?  105 LYS   I NZ  1 
ATOM   403   N N   . ALA   A  1 106 ? 17.18586  34.24702  -26.53833 1.000 52.14106  ?  106 ALA   I N   1 
ATOM   404   C CA  . ALA   A  1 106 ? 16.60567  32.92497  -26.68040 1.000 45.40268  ?  106 ALA   I CA  1 
ATOM   405   C C   . ALA   A  1 106 ? 16.19194  32.67061  -28.12614 1.000 28.79332  ?  106 ALA   I C   1 
ATOM   406   O O   . ALA   A  1 106 ? 15.92571  33.61280  -28.87489 1.000 48.14290  ?  106 ALA   I O   1 
ATOM   407   C CB  . ALA   A  1 106 ? 15.39768  32.77018  -25.75650 1.000 31.70984  ?  106 ALA   I CB  1 
ATOM   408   N N   . PRO   A  1 107 ? 16.14629  31.40658  -28.55145 1.000 61.25727  ?  107 PRO   I N   1 
ATOM   409   C CA  . PRO   A  1 107 ? 15.72184  31.11211  -29.92326 1.000 43.58962  ?  107 PRO   I CA  1 
ATOM   410   C C   . PRO   A  1 107 ? 14.24454  31.42884  -30.11824 1.000 53.47245  ?  107 PRO   I C   1 
ATOM   411   O O   . PRO   A  1 107 ? 13.46509  31.52647  -29.16634 1.000 48.73585  ?  107 PRO   I O   1 
ATOM   412   C CB  . PRO   A  1 107 ? 15.98324  29.60692  -30.07290 1.000 41.64542  ?  107 PRO   I CB  1 
ATOM   413   C CG  . PRO   A  1 107 ? 16.65060  29.17203  -28.84585 1.000 38.25656  ?  107 PRO   I CG  1 
ATOM   414   C CD  . PRO   A  1 107 ? 16.40667  30.17838  -27.78168 1.000 32.08526  ?  107 PRO   I CD  1 
ATOM   415   N N   . VAL   A  1 108 ? 13.85759  31.56870  -31.38267 1.000 43.02243  ?  108 VAL   I N   1 
ATOM   416   C CA  . VAL   A  1 108 ? 12.47085  31.81201  -31.73983 1.000 38.88831  ?  108 VAL   I CA  1 
ATOM   417   C C   . VAL   A  1 108 ? 12.00943  30.72852  -32.71682 1.000 50.12010  ?  108 VAL   I C   1 
ATOM   418   O O   . VAL   A  1 108 ? 12.80410  29.95516  -33.25631 1.000 50.73548  ?  108 VAL   I O   1 
ATOM   419   C CB  . VAL   A  1 108 ? 12.26159  33.22604  -32.32078 1.000 49.12396  ?  108 VAL   I CB  1 
ATOM   420   C CG1 . VAL   A  1 108 ? 12.74068  34.29198  -31.31587 1.000 30.14642  ?  108 VAL   I CG1 1 
ATOM   421   C CG2 . VAL   A  1 108 ? 12.98962  33.37538  -33.62476 1.000 29.89262  ?  108 VAL   I CG2 1 
ATOM   422   N N   . TYR   A  1 109 ? 10.69696  30.66617  -32.91565 1.000 34.55923  ?  109 TYR   I N   1 
ATOM   423   C CA  . TYR   A  1 109 ? 10.11249  29.67080  -33.80639 1.000 64.01254  ?  109 TYR   I CA  1 
ATOM   424   C C   . TYR   A  1 109 ? 10.19457  30.13807  -35.25502 1.000 34.27583  ?  109 TYR   I C   1 
ATOM   425   O O   . TYR   A  1 109 ? 10.01756  31.32259  -35.55269 1.000 48.20049  ?  109 TYR   I O   1 
ATOM   426   C CB  . TYR   A  1 109 ? 8.65362   29.39441  -33.42632 1.000 28.43007  ?  109 TYR   I CB  1 
ATOM   427   C CG  . TYR   A  1 109 ? 7.99313   28.38922  -34.34085 1.000 61.23503  ?  109 TYR   I CG  1 
ATOM   428   C CD1 . TYR   A  1 109 ? 8.07982   27.03360  -34.08886 1.000 29.72611  ?  109 TYR   I CD1 1 
ATOM   429   C CD2 . TYR   A  1 109 ? 7.30339   28.79827  -35.47396 1.000 33.70501  ?  109 TYR   I CD2 1 
ATOM   430   C CE1 . TYR   A  1 109 ? 7.48783   26.11684  -34.93968 1.000 71.39803  ?  109 TYR   I CE1 1 
ATOM   431   C CE2 . TYR   A  1 109 ? 6.71214   27.89205  -36.32785 1.000 54.84641  ?  109 TYR   I CE2 1 
ATOM   432   C CZ  . TYR   A  1 109 ? 6.80466   26.55342  -36.06025 1.000 31.06314  ?  109 TYR   I CZ  1 
ATOM   433   O OH  . TYR   A  1 109 ? 6.22196   25.63447  -36.90379 1.000 57.33323  ?  109 TYR   I OH  1 
ATOM   434   N N   . GLY   A  1 110 ? 10.47856  29.20736  -36.15816 1.000 61.02304  ?  110 GLY   I N   1 
ATOM   435   C CA  . GLY   A  1 110 ? 10.51679  29.58815  -37.55278 1.000 26.02231  ?  110 GLY   I CA  1 
ATOM   436   C C   . GLY   A  1 110 ? 11.56032  28.92244  -38.42529 1.000 59.71913  ?  110 GLY   I C   1 
ATOM   437   O O   . GLY   A  1 110 ? 11.25454  28.57457  -39.56766 1.000 53.72119  ?  110 GLY   I O   1 
ATOM   438   N N   . ASP   A  1 111 ? 12.78712  28.74706  -37.93222 1.000 60.32416  ?  111 ASP   I N   1 
ATOM   439   C CA  . ASP   A  1 111 ? 13.83972  28.22165  -38.78920 1.000 50.90287  ?  111 ASP   I CA  1 
ATOM   440   C C   . ASP   A  1 111 ? 13.83455  26.69689  -38.78818 1.000 34.94944  ?  111 ASP   I C   1 
ATOM   441   O O   . ASP   A  1 111 ? 13.23422  26.05423  -37.92227 1.000 48.28162  ?  111 ASP   I O   1 
ATOM   442   C CB  . ASP   A  1 111 ? 15.20014  28.75903  -38.35696 1.000 63.63460  ?  111 ASP   I CB  1 
ATOM   443   C CG  . ASP   A  1 111 ? 15.41673  30.18551  -38.79454 1.000 62.34560  ?  111 ASP   I CG  1 
ATOM   444   O OD1 . ASP   A  1 111 ? 15.51515  30.41839  -40.01807 1.000 78.16303  ?  111 ASP   I OD1 1 
ATOM   445   O OD2 . ASP   A  1 111 ? 15.46304  31.07351  -37.91498 1.000 97.03129  ?  111 ASP   I OD2 1 
ATOM   446   N N   . LEU   A  1 112 ? 14.52680  26.10889  -39.76520 1.000 107.40049 ?  112 LEU   I N   1 
ATOM   447   C CA  . LEU   A  1 112 ? 14.55690  24.65484  -39.87487 1.000 17.29279  ?  112 LEU   I CA  1 
ATOM   448   C C   . LEU   A  1 112 ? 15.37595  24.02644  -38.75179 1.000 59.43549  ?  112 LEU   I C   1 
ATOM   449   O O   . LEU   A  1 112 ? 15.12746  22.86773  -38.38626 1.000 51.30397  ?  112 LEU   I O   1 
ATOM   450   C CB  . LEU   A  1 112 ? 15.10222  24.26486  -41.22628 1.000 59.47051  ?  112 LEU   I CB  1 
ATOM   451   C CG  . LEU   A  1 112 ? 14.52749  25.03642  -42.40712 1.000 85.11774  ?  112 LEU   I CG  1 
ATOM   452   C CD1 . LEU   A  1 112 ? 15.11447  26.45037  -42.63025 1.000 94.51974  ?  112 LEU   I CD1 1 
ATOM   453   C CD2 . LEU   A  1 112 ? 14.98576  24.19889  -43.46798 1.000 123.67773 ?  112 LEU   I CD2 1 
ATOM   454   N N   . GLY   A  1 113 ? 16.34060  24.76083  -38.19149 1.000 40.02028  ?  113 GLY   I N   1 
ATOM   455   C CA  . GLY   A  1 113 ? 17.05835  24.29574  -37.03184 1.000 38.49909  ?  113 GLY   I CA  1 
ATOM   456   C C   . GLY   A  1 113 ? 17.38484  25.43528  -36.08705 1.000 42.08890  ?  113 GLY   I C   1 
ATOM   457   O O   . GLY   A  1 113 ? 17.04118  26.60135  -36.33048 1.000 40.52763  ?  113 GLY   I O   1 
ATOM   458   N N   . PRO   A  1 114 ? 18.06926  25.11928  -34.99029 1.000 39.02155  ?  114 PRO   I N   1 
ATOM   459   C CA  . PRO   A  1 114 ? 18.41485  26.15589  -33.99161 1.000 32.33970  ?  114 PRO   I CA  1 
ATOM   460   C C   . PRO   A  1 114 ? 19.42186  27.14794  -34.55488 1.000 35.29987  ?  114 PRO   I C   1 
ATOM   461   O O   . PRO   A  1 114 ? 20.01738  26.91951  -35.62582 1.000 39.76846  ?  114 PRO   I O   1 
ATOM   462   C CB  . PRO   A  1 114 ? 18.98735  25.34016  -32.81938 1.000 37.35084  ?  114 PRO   I CB  1 
ATOM   463   C CG  . PRO   A  1 114 ? 19.46962  24.04734  -33.45716 1.000 34.30642  ?  114 PRO   I CG  1 
ATOM   464   C CD  . PRO   A  1 114 ? 18.58799  23.78529  -34.64278 1.000 35.39180  ?  114 PRO   I CD  1 
ATOM   465   N N   . PRO   A  1 115 ? 19.60863  28.29359  -33.88836 1.000 39.05613  ?  115 PRO   I N   1 
ATOM   466   C CA  . PRO   A  1 115 ? 20.28401  29.42493  -34.56514 1.000 50.04119  ?  115 PRO   I CA  1 
ATOM   467   C C   . PRO   A  1 115 ? 21.76423  29.22553  -34.83322 1.000 42.13998  ?  115 PRO   I C   1 
ATOM   468   O O   . PRO   A  1 115 ? 22.25225  29.71362  -35.86266 1.000 47.23303  ?  115 PRO   I O   1 
ATOM   469   C CB  . PRO   A  1 115 ? 20.04498  30.61026  -33.61605 1.000 31.81386  ?  115 PRO   I CB  1 
ATOM   470   C CG  . PRO   A  1 115 ? 19.46356  30.03791  -32.35184 1.000 34.37196  ?  115 PRO   I CG  1 
ATOM   471   C CD  . PRO   A  1 115 ? 18.84369  28.72472  -32.70248 1.000 44.33982  ?  115 PRO   I CD  1 
ATOM   472   N N   . VAL   A  1 116 ? 22.50309  28.55317  -33.93917 1.000 42.98912  ?  116 VAL   I N   1 
ATOM   473   C CA  . VAL   A  1 116 ? 23.91449  28.28797  -34.22391 1.000 33.25017  ?  116 VAL   I CA  1 
ATOM   474   C C   . VAL   A  1 116 ? 24.05315  27.33742  -35.40829 1.000 35.73118  ?  116 VAL   I C   1 
ATOM   475   O O   . VAL   A  1 116 ? 24.88295  27.55479  -36.30304 1.000 39.30505  ?  116 VAL   I O   1 
ATOM   476   C CB  . VAL   A  1 116 ? 24.65711  27.74622  -32.99070 1.000 40.42049  ?  116 VAL   I CB  1 
ATOM   477   C CG1 . VAL   A  1 116 ? 26.10982  27.46952  -33.37134 1.000 32.49484  ?  116 VAL   I CG1 1 
ATOM   478   C CG2 . VAL   A  1 116 ? 24.59150  28.73833  -31.83815 1.000 24.45437  ?  116 VAL   I CG2 1 
ATOM   479   N N   . TYR   A  1 117 ? 23.24726  26.27479  -35.44400 1.000 38.49491  ?  117 TYR   I N   1 
ATOM   480   C CA  . TYR   A  1 117 ? 23.26325  25.40563  -36.61548 1.000 52.02765  ?  117 TYR   I CA  1 
ATOM   481   C C   . TYR   A  1 117 ? 23.03884  26.20547  -37.90281 1.000 46.04836  ?  117 TYR   I C   1 
ATOM   482   O O   . TYR   A  1 117 ? 23.76398  26.02705  -38.88859 1.000 51.05998  ?  117 TYR   I O   1 
ATOM   483   C CB  . TYR   A  1 117 ? 22.21563  24.28710  -36.49919 1.000 37.61279  ?  117 TYR   I CB  1 
ATOM   484   C CG  . TYR   A  1 117 ? 22.00767  23.66938  -37.86229 1.000 44.88309  ?  117 TYR   I CG  1 
ATOM   485   C CD1 . TYR   A  1 117 ? 22.92819  22.75162  -38.37061 1.000 41.11188  ?  117 TYR   I CD1 1 
ATOM   486   C CD2 . TYR   A  1 117 ? 20.95090  24.06384  -38.68068 1.000 57.82179  ?  117 TYR   I CD2 1 
ATOM   487   C CE1 . TYR   A  1 117 ? 22.78279  22.20871  -39.64086 1.000 41.54375  ?  117 TYR   I CE1 1 
ATOM   488   C CE2 . TYR   A  1 117 ? 20.80401  23.53358  -39.94467 1.000 35.23672  ?  117 TYR   I CE2 1 
ATOM   489   C CZ  . TYR   A  1 117 ? 21.72398  22.60608  -40.41934 1.000 51.66453  ?  117 TYR   I CZ  1 
ATOM   490   O OH  . TYR   A  1 117 ? 21.58132  22.06703  -41.67185 1.000 41.40807  ?  117 TYR   I OH  1 
ATOM   491   N N   . MET   A  1 118 ? 22.03345  27.09328  -37.90935 1.000 47.89643  ?  118 MET   I N   1 
ATOM   492   C CA  . MET   A  1 118 ? 21.68286  27.82148  -39.13058 1.000 37.72862  ?  118 MET   I CA  1 
ATOM   493   C C   . MET   A  1 118 ? 22.88355  28.58761  -39.69593 1.000 53.34904  ?  118 MET   I C   1 
ATOM   494   O O   . MET   A  1 118 ? 23.18362  28.48954  -40.89178 1.000 45.51657  ?  118 MET   I O   1 
ATOM   495   C CB  . MET   A  1 118 ? 20.50951  28.77709  -38.87609 1.000 40.79745  ?  118 MET   I CB  1 
ATOM   496   C CG  . MET   A  1 118 ? 19.12535  28.15278  -38.64375 1.000 30.46830  ?  118 MET   I CG  1 
ATOM   497   S SD  . MET   A  1 118 ? 18.47801  27.09414  -39.95707 1.000 48.68390  ?  118 MET   I SD  1 
ATOM   498   C CE  . MET   A  1 118 ? 18.45396  28.25197  -41.32449 1.000 53.25582  ?  118 MET   I CE  1 
ATOM   499   N N   . ILE   A  1 119 ? 23.60803  29.33854  -38.85408 1.000 34.35093  ?  119 ILE   I N   1 
ATOM   500   C CA  . ILE   A  1 119 ? 24.77903  30.04519  -39.38243 1.000 45.83017  ?  119 ILE   I CA  1 
ATOM   501   C C   . ILE   A  1 119 ? 26.00989  29.16021  -39.55099 1.000 46.26528  ?  119 ILE   I C   1 
ATOM   502   O O   . ILE   A  1 119 ? 26.97724  29.59793  -40.19279 1.000 50.92732  ?  119 ILE   I O   1 
ATOM   503   C CB  . ILE   A  1 119 ? 25.16222  31.26961  -38.52667 1.000 37.80239  ?  119 ILE   I CB  1 
ATOM   504   C CG1 . ILE   A  1 119 ? 25.83855  30.86013  -37.22551 1.000 40.09182  ?  119 ILE   I CG1 1 
ATOM   505   C CG2 . ILE   A  1 119 ? 23.93621  32.09510  -38.21225 1.000 45.31165  ?  119 ILE   I CG2 1 
ATOM   506   C CD1 . ILE   A  1 119 ? 26.25082  32.06089  -36.40505 1.000 44.97006  ?  119 ILE   I CD1 1 
ATOM   507   N N   . MET   A  1 120 ? 26.00335  27.92176  -39.02956 1.000 41.64229  ?  120 MET   I N   1 
ATOM   508   C CA  . MET   A  1 120 ? 27.15765  27.02587  -39.15708 1.000 39.64096  ?  120 MET   I CA  1 
ATOM   509   C C   . MET   A  1 120 ? 27.05586  26.05009  -40.32330 1.000 45.47189  ?  120 MET   I C   1 
ATOM   510   O O   . MET   A  1 120 ? 28.07775  25.48202  -40.72293 1.000 45.07683  ?  120 MET   I O   1 
ATOM   511   C CB  . MET   A  1 120 ? 27.35518  26.19626  -37.87515 1.000 27.26603  ?  120 MET   I CB  1 
ATOM   512   C CG  . MET   A  1 120 ? 27.84045  26.98797  -36.68150 1.000 35.15714  ?  120 MET   I CG  1 
ATOM   513   S SD  . MET   A  1 120 ? 29.50400  27.61877  -36.84324 1.000 51.27612  ?  120 MET   I SD  1 
ATOM   514   C CE  . MET   A  1 120 ? 30.45356  26.14824  -36.44801 1.000 35.91635  ?  120 MET   I CE  1 
ATOM   515   N N   . ALA   A  1 121 ? 25.85320  25.83555  -40.86494 1.000 34.11436  ?  121 ALA   I N   1 
ATOM   516   C CA  . ALA   A  1 121 ? 25.63331  24.70740  -41.76909 1.000 39.89922  ?  121 ALA   I CA  1 
ATOM   517   C C   . ALA   A  1 121 ? 26.53024  24.78488  -42.99747 1.000 40.27484  ?  121 ALA   I C   1 
ATOM   518   O O   . ALA   A  1 121 ? 27.04682  23.75881  -43.46259 1.000 47.24836  ?  121 ALA   I O   1 
ATOM   519   C CB  . ALA   A  1 121 ? 24.15774  24.64137  -42.18265 1.000 31.81511  ?  121 ALA   I CB  1 
ATOM   520   N N   . LYS   A  1 122 ? 26.72226  25.99245  -43.54666 1.000 47.98465  ?  122 LYS   I N   1 
ATOM   521   C CA  . LYS   A  1 122 ? 27.57596  26.12603  -44.72527 1.000 40.52137  ?  122 LYS   I CA  1 
ATOM   522   C C   . LYS   A  1 122 ? 29.02726  25.76450  -44.38526 1.000 54.74662  ?  122 LYS   I C   1 
ATOM   523   O O   . LYS   A  1 122 ? 29.69882  25.07756  -45.15787 1.000 48.57873  ?  122 LYS   I O   1 
ATOM   524   C CB  . LYS   A  1 122 ? 27.46804  27.54970  -45.30855 1.000 39.93606  ?  122 LYS   I CB  1 
ATOM   525   N N   . LEU   A  1 123 ? 29.50909  26.16793  -43.20293 1.000 45.91229  ?  123 LEU   I N   1 
ATOM   526   C CA  . LEU   A  1 123 ? 30.86509  25.81983  -42.76078 1.000 45.41298  ?  123 LEU   I CA  1 
ATOM   527   C C   . LEU   A  1 123 ? 31.02214  24.31846  -42.53704 1.000 70.40255  ?  123 LEU   I C   1 
ATOM   528   O O   . LEU   A  1 123 ? 32.01818  23.71155  -42.96946 1.000 37.48185  ?  123 LEU   I O   1 
ATOM   529   C CB  . LEU   A  1 123 ? 31.20999  26.58248  -41.47905 1.000 36.49991  ?  123 LEU   I CB  1 
ATOM   530   C CG  . LEU   A  1 123 ? 30.86102  28.06312  -41.56197 1.000 45.44234  ?  123 LEU   I CG  1 
ATOM   531   C CD1 . LEU   A  1 123 ? 31.23471  28.80418  -40.28610 1.000 39.59690  ?  123 LEU   I CD1 1 
ATOM   532   C CD2 . LEU   A  1 123 ? 31.56611  28.65971  -42.75455 1.000 39.42636  ?  123 LEU   I CD2 1 
ATOM   533   N N   . MET   A  1 124 ? 30.06605  23.70852  -41.82224 1.000 43.62528  ?  124 MET   I N   1 
ATOM   534   C CA  . MET   A  1 124 ? 30.12484  22.26961  -41.58569 1.000 55.01657  ?  124 MET   I CA  1 
ATOM   535   C C   . MET   A  1 124 ? 30.22368  21.48246  -42.87993 1.000 47.58306  ?  124 MET   I C   1 
ATOM   536   O O   . MET   A  1 124 ? 30.73226  20.35594  -42.88271 1.000 46.73272  ?  124 MET   I O   1 
ATOM   537   C CB  . MET   A  1 124 ? 28.89315  21.80110  -40.82248 1.000 32.59933  ?  124 MET   I CB  1 
ATOM   538   C CG  . MET   A  1 124 ? 28.71602  22.44438  -39.48338 1.000 52.84457  ?  124 MET   I CG  1 
ATOM   539   S SD  . MET   A  1 124 ? 26.97822  22.38309  -38.99704 1.000 54.73021  ?  124 MET   I SD  1 
ATOM   540   C CE  . MET   A  1 124 ? 26.63900  20.63555  -38.95916 1.000 30.40258  ?  124 MET   I CE  1 
ATOM   541   N N   . ASN   A  1 125 ? 29.73399  22.04852  -43.98193 1.000 50.19447  ?  125 ASN   I N   1 
ATOM   542   C CA  . ASN   A  1 125 ? 29.66426  21.35135  -45.25346 1.000 44.07659  ?  125 ASN   I CA  1 
ATOM   543   C C   . ASN   A  1 125 ? 30.94332  21.49659  -46.08959 1.000 49.70028  ?  125 ASN   I C   1 
ATOM   544   O O   . ASN   A  1 125 ? 30.90757  21.30843  -47.30945 1.000 53.68867  ?  125 ASN   I O   1 
ATOM   545   C CB  . ASN   A  1 125 ? 28.46017  21.84766  -46.05075 1.000 42.56260  ?  125 ASN   I CB  1 
ATOM   546   C CG  . ASN   A  1 125 ? 28.00215  20.84332  -47.08609 1.000 40.69351  ?  125 ASN   I CG  1 
ATOM   547   O OD1 . ASN   A  1 125 ? 28.35295  19.65729  -47.02918 1.000 46.85685  ?  125 ASN   I OD1 1 
ATOM   548   N ND2 . ASN   A  1 125 ? 27.20356  21.30782  -48.03449 1.000 58.00666  ?  125 ASN   I ND2 1 
ATOM   549   N N   . THR   A  1 126 ? 32.06915  21.80544  -45.46787 1.000 48.24797  ?  126 THR   I N   1 
ATOM   550   C CA  . THR   A  1 126 ? 33.34561  21.88429  -46.15756 1.000 57.33789  ?  126 THR   I CA  1 
ATOM   551   C C   . THR   A  1 126 ? 34.32581  20.91369  -45.51908 1.000 36.20828  ?  126 THR   I C   1 
ATOM   552   O O   . THR   A  1 126 ? 34.14048  20.47172  -44.38143 1.000 55.13094  ?  126 THR   I O   1 
ATOM   553   C CB  . THR   A  1 126 ? 33.92731  23.30261  -46.09958 1.000 42.08800  ?  126 THR   I CB  1 
ATOM   554   O OG1 . THR   A  1 126 ? 34.39939  23.57775  -44.76669 1.000 41.51034  ?  126 THR   I OG1 1 
ATOM   555   C CG2 . THR   A  1 126 ? 32.86829  24.33118  -46.48885 1.000 27.10818  ?  126 THR   I CG2 1 
ATOM   556   N N   . ARG   A  1 127 ? 35.38771  20.60583  -46.25766 1.000 116.40107 ?  127 ARG   I N   1 
ATOM   557   C CA  . ARG   A  1 127 ? 36.44757  19.82119  -45.63875 1.000 18.63604  ?  127 ARG   I CA  1 
ATOM   558   C C   . ARG   A  1 127 ? 37.09911  20.59702  -44.51422 1.000 26.32943  ?  127 ARG   I C   1 
ATOM   559   O O   . ARG   A  1 127 ? 37.31064  20.07908  -43.40964 1.000 58.47506  ?  127 ARG   I O   1 
ATOM   560   C CB  . ARG   A  1 127 ? 37.48543  19.37665  -46.67192 1.000 19.70195  ?  127 ARG   I CB  1 
ATOM   561   C CG  . ARG   A  1 127 ? 37.19784  17.91391  -47.02413 1.000 124.25433 ?  127 ARG   I CG  1 
ATOM   562   C CD  . ARG   A  1 127 ? 37.94796  17.40026  -48.17748 1.000 24.08240  ?  127 ARG   I CD  1 
ATOM   563   N NE  . ARG   A  1 127 ? 39.38298  17.53259  -47.97873 1.000 55.97865  ?  127 ARG   I NE  1 
ATOM   564   C CZ  . ARG   A  1 127 ? 40.26475  16.71597  -48.53105 1.000 115.69467 ?  127 ARG   I CZ  1 
ATOM   565   N NH1 . ARG   A  1 127 ? 39.86785  15.70370  -49.29094 1.000 102.72294 ?  127 ARG   I NH1 1 
ATOM   566   N NH2 . ARG   A  1 127 ? 41.56806  16.91247  -48.30723 1.000 83.82376  ?  127 ARG   I NH2 1 
ATOM   567   N N   . ALA   A  1 128 ? 37.43632  21.83639  -44.77918 1.000 30.18237  ?  128 ALA   I N   1 
ATOM   568   C CA  . ALA   A  1 128 ? 38.10029  22.64026  -43.75792 1.000 43.15362  ?  128 ALA   I CA  1 
ATOM   569   C C   . ALA   A  1 128 ? 37.27074  22.68887  -42.47694 1.000 34.08490  ?  128 ALA   I C   1 
ATOM   570   O O   . ALA   A  1 128 ? 37.81672  22.55602  -41.37188 1.000 44.92466  ?  128 ALA   I O   1 
ATOM   571   C CB  . ALA   A  1 128 ? 38.37564  24.05569  -44.29323 1.000 31.92185  ?  128 ALA   I CB  1 
ATOM   572   N N   . GLY   A  1 129 ? 35.94641  22.85531  -42.60652 1.000 58.24504  ?  129 GLY   I N   1 
ATOM   573   C CA  . GLY   A  1 129 ? 35.09079  22.91967  -41.42442 1.000 26.25425  ?  129 GLY   I CA  1 
ATOM   574   C C   . GLY   A  1 129 ? 35.05415  21.60613  -40.65720 1.000 50.75113  ?  129 GLY   I C   1 
ATOM   575   O O   . GLY   A  1 129 ? 35.19184  21.57957  -39.42794 1.000 40.59645  ?  129 GLY   I O   1 
ATOM   576   N N   . PHE   A  1 130 ? 34.88560  20.49316  -41.37647 1.000 33.55159  ?  130 PHE   I N   1 
ATOM   577   C CA  . PHE   A  1 130 ? 34.91563  19.19088  -40.72313 1.000 33.63798  ?  130 PHE   I CA  1 
ATOM   578   C C   . PHE   A  1 130 ? 36.23104  18.96869  -39.96970 1.000 54.56954  ?  130 PHE   I C   1 
ATOM   579   O O   . PHE   A  1 130 ? 36.21488  18.48846  -38.83137 1.000 45.72428  ?  130 PHE   I O   1 
ATOM   580   C CB  . PHE   A  1 130 ? 34.67498  18.09517  -41.75938 1.000 22.23021  ?  130 PHE   I CB  1 
ATOM   581   C CG  . PHE   A  1 130 ? 34.75501  16.70840  -41.20370 1.000 35.67489  ?  130 PHE   I CG  1 
ATOM   582   C CD1 . PHE   A  1 130 ? 35.98722  16.06237  -41.06697 1.000 35.67087  ?  130 PHE   I CD1 1 
ATOM   583   C CD2 . PHE   A  1 130 ? 33.60607  16.03905  -40.82432 1.000 29.27211  ?  130 PHE   I CD2 1 
ATOM   584   C CE1 . PHE   A  1 130 ? 36.07783  14.77646  -40.55409 1.000 34.50384  ?  130 PHE   I CE1 1 
ATOM   585   C CE2 . PHE   A  1 130 ? 33.68583  14.74724  -40.30426 1.000 43.09698  ?  130 PHE   I CE2 1 
ATOM   586   C CZ  . PHE   A  1 130 ? 34.94289  14.11403  -40.17524 1.000 29.54553  ?  130 PHE   I CZ  1 
ATOM   587   N N   . SER   A  1 131 ? 37.37940  19.29806  -40.58561 1.000 33.59551  ?  131 SER   I N   1 
ATOM   588   C CA  . SER   A  1 131 ? 38.65565  19.19025  -39.87087 1.000 51.26889  ?  131 SER   I CA  1 
ATOM   589   C C   . SER   A  1 131 ? 38.62933  19.97218  -38.56312 1.000 38.92794  ?  131 SER   I C   1 
ATOM   590   O O   . SER   A  1 131 ? 38.99236  19.44505  -37.50084 1.000 49.77452  ?  131 SER   I O   1 
ATOM   591   C CB  . SER   A  1 131 ? 39.81415  19.68386  -40.73669 1.000 22.49395  ?  131 SER   I CB  1 
ATOM   592   O OG  . SER   A  1 131 ? 40.39617  18.60700  -41.41975 1.000 94.36096  ?  131 SER   I OG  1 
ATOM   593   N N   . ALA   A  1 132 ? 38.24043  21.25042  -38.63072 1.000 32.45222  ?  132 ALA   I N   1 
ATOM   594   C CA  . ALA   A  1 132 ? 38.24326  22.08071  -37.43198 1.000 26.71444  ?  132 ALA   I CA  1 
ATOM   595   C C   . ALA   A  1 132 ? 37.33905  21.48712  -36.36467 1.000 41.00467  ?  132 ALA   I C   1 
ATOM   596   O O   . ALA   A  1 132 ? 37.73477  21.35397  -35.19639 1.000 34.76881  ?  132 ALA   I O   1 
ATOM   597   C CB  . ALA   A  1 132 ? 37.80301  23.50041  -37.77339 1.000 27.43665  ?  132 ALA   I CB  1 
ATOM   598   N N   . PHE   A  1 133 ? 36.12938  21.08717  -36.76809 1.000 30.68356  ?  133 PHE   I N   1 
ATOM   599   C CA  . PHE   A  1 133 ? 35.08437  20.63364  -35.85843 1.000 41.25826  ?  133 PHE   I CA  1 
ATOM   600   C C   . PHE   A  1 133 ? 35.32486  19.22054  -35.33391 1.000 48.20692  ?  133 PHE   I C   1 
ATOM   601   O O   . PHE   A  1 133 ? 34.55120  18.74240  -34.49318 1.000 37.71950  ?  133 PHE   I O   1 
ATOM   602   C CB  . PHE   A  1 133 ? 33.72153  20.73008  -36.55176 1.000 33.47707  ?  133 PHE   I CB  1 
ATOM   603   C CG  . PHE   A  1 133 ? 33.44020  22.09887  -37.12521 1.000 44.42711  ?  133 PHE   I CG  1 
ATOM   604   C CD1 . PHE   A  1 133 ? 34.07665  23.23633  -36.60313 1.000 39.97931  ?  133 PHE   I CD1 1 
ATOM   605   C CD2 . PHE   A  1 133 ? 32.55988  22.25355  -38.19246 1.000 34.69181  ?  133 PHE   I CD2 1 
ATOM   606   C CE1 . PHE   A  1 133 ? 33.83591  24.50051  -37.13424 1.000 31.84371  ?  133 PHE   I CE1 1 
ATOM   607   C CE2 . PHE   A  1 133 ? 32.31057  23.50654  -38.73611 1.000 34.11482  ?  133 PHE   I CE2 1 
ATOM   608   C CZ  . PHE   A  1 133 ? 32.94919  24.63831  -38.20519 1.000 27.90734  ?  133 PHE   I CZ  1 
ATOM   609   N N   . THR   A  1 134 ? 36.38621  18.54660  -35.77993 1.000 29.09250  ?  134 THR   I N   1 
ATOM   610   C CA  . THR   A  1 134 ? 36.75230  17.25101  -35.22585 1.000 33.75125  ?  134 THR   I CA  1 
ATOM   611   C C   . THR   A  1 134 ? 38.05206  17.31690  -34.41930 1.000 31.57795  ?  134 THR   I C   1 
ATOM   612   O O   . THR   A  1 134 ? 38.73407  16.30382  -34.24518 1.000 39.52953  ?  134 THR   I O   1 
ATOM   613   C CB  . THR   A  1 134 ? 36.83392  16.18271  -36.31839 1.000 33.76803  ?  134 THR   I CB  1 
ATOM   614   O OG1 . THR   A  1 134 ? 37.56438  16.67433  -37.45108 1.000 39.45630  ?  134 THR   I OG1 1 
ATOM   615   C CG2 . THR   A  1 134 ? 35.42956  15.76757  -36.75347 1.000 26.76319  ?  134 THR   I CG2 1 
ATOM   616   N N   . ARG   A  1 135 ? 38.38078  18.49672  -33.88694 1.000 34.47090  ?  135 ARG   I N   1 
ATOM   617   C CA  . ARG   A  1 135 ? 39.48919  18.67006  -32.94944 1.000 34.64932  ?  135 ARG   I CA  1 
ATOM   618   C C   . ARG   A  1 135 ? 38.91775  18.79990  -31.54297 1.000 48.27412  ?  135 ARG   I C   1 
ATOM   619   O O   . ARG   A  1 135 ? 38.12832  19.71604  -31.27187 1.000 34.88316  ?  135 ARG   I O   1 
ATOM   620   C CB  . ARG   A  1 135 ? 40.32785  19.90554  -33.28413 1.000 25.46742  ?  135 ARG   I CB  1 
ATOM   621   C CG  . ARG   A  1 135 ? 40.96049  19.90380  -34.67446 1.000 29.67273  ?  135 ARG   I CG  1 
ATOM   622   C CD  . ARG   A  1 135 ? 41.40315  21.30627  -34.99868 1.000 32.40866  ?  135 ARG   I CD  1 
ATOM   623   N NE  . ARG   A  1 135 ? 42.07916  21.40192  -36.28054 1.000 51.70348  ?  135 ARG   I NE  1 
ATOM   624   C CZ  . ARG   A  1 135 ? 43.29687  20.93476  -36.51364 1.000 55.51957  ?  135 ARG   I CZ  1 
ATOM   625   N NH1 . ARG   A  1 135 ? 43.99937  20.33363  -35.56632 1.000 46.69409  ?  135 ARG   I NH1 1 
ATOM   626   N NH2 . ARG   A  1 135 ? 43.81561  21.05722  -37.73388 1.000 44.62399  ?  135 ARG   I NH2 1 
ATOM   627   N N   . GLN   A  1 136 ? 39.31298  17.88268  -30.65139 1.000 31.01824  ?  136 GLN   I N   1 
ATOM   628   C CA  . GLN   A  1 136 ? 38.83591  17.94393  -29.27252 1.000 33.03671  ?  136 GLN   I CA  1 
ATOM   629   C C   . GLN   A  1 136 ? 39.14369  19.28892  -28.63573 1.000 30.40080  ?  136 GLN   I C   1 
ATOM   630   O O   . GLN   A  1 136 ? 38.35020  19.78098  -27.81975 1.000 47.89519  ?  136 GLN   I O   1 
ATOM   631   C CB  . GLN   A  1 136 ? 39.44527  16.81180  -28.44711 1.000 31.08919  ?  136 GLN   I CB  1 
ATOM   632   C CG  . GLN   A  1 136 ? 39.06372  15.44534  -28.96105 1.000 26.32199  ?  136 GLN   I CG  1 
ATOM   633   C CD  . GLN   A  1 136 ? 38.64398  14.50755  -27.85701 1.000 51.58031  ?  136 GLN   I CD  1 
ATOM   634   O OE1 . GLN   A  1 136 ? 39.30246  14.41680  -26.79855 1.000 39.50028  ?  136 GLN   I OE1 1 
ATOM   635   N NE2 . GLN   A  1 136 ? 37.53179  13.80171  -28.08671 1.000 26.82440  ?  136 GLN   I NE2 1 
ATOM   636   N N   . ARG   A  1 137 ? 40.26589  19.92445  -29.03008 1.000 60.63808  ?  137 ARG   I N   1 
ATOM   637   C CA  . ARG   A  1 137 ? 40.67001  21.20898  -28.44387 1.000 26.43590  ?  137 ARG   I CA  1 
ATOM   638   C C   . ARG   A  1 137 ? 39.65926  22.29807  -28.74826 1.000 45.49391  ?  137 ARG   I C   1 
ATOM   639   O O   . ARG   A  1 137 ? 39.22251  23.03373  -27.84399 1.000 35.02919  ?  137 ARG   I O   1 
ATOM   640   C CB  . ARG   A  1 137 ? 42.04370  21.63835  -28.95965 1.000 60.24153  ?  137 ARG   I CB  1 
ATOM   641   C CG  . ARG   A  1 137 ? 43.19241  21.32326  -28.02827 1.000 24.12451  ?  137 ARG   I CG  1 
ATOM   642   C CD  . ARG   A  1 137 ? 44.52234  21.54770  -28.74649 1.000 26.05779  ?  137 ARG   I CD  1 
ATOM   643   N NE  . ARG   A  1 137 ? 45.61424  20.78276  -28.15955 1.000 77.39877  ?  137 ARG   I NE  1 
ATOM   644   C CZ  . ARG   A  1 137 ? 46.80193  20.66911  -28.73089 1.000 78.31824  ?  137 ARG   I CZ  1 
ATOM   645   N NH1 . ARG   A  1 137 ? 47.05522  21.26600  -29.88919 1.000 35.83857  ?  137 ARG   I NH1 1 
ATOM   646   N NH2 . ARG   A  1 137 ? 47.75268  19.93262  -28.13393 1.000 28.77403  ?  137 ARG   I NH2 1 
ATOM   647   N N   . LEU   A  1 138 ? 39.27189  22.40943  -30.02583 1.000 30.75036  ?  138 LEU   I N   1 
ATOM   648   C CA  . LEU   A  1 138 ? 38.21971  23.35512  -30.41172 1.000 43.80783  ?  138 LEU   I CA  1 
ATOM   649   C C   . LEU   A  1 138 ? 36.88404  23.02712  -29.74564 1.000 53.24684  ?  138 LEU   I C   1 
ATOM   650   O O   . LEU   A  1 138 ? 36.17536  23.92694  -29.27455 1.000 42.79613  ?  138 LEU   I O   1 
ATOM   651   C CB  . LEU   A  1 138 ? 38.04398  23.35677  -31.92652 1.000 37.59116  ?  138 LEU   I CB  1 
ATOM   652   C CG  . LEU   A  1 138 ? 37.08039  24.41637  -32.43567 1.000 51.47102  ?  138 LEU   I CG  1 
ATOM   653   C CD1 . LEU   A  1 138 ? 37.68158  25.77602  -32.14669 1.000 37.94955  ?  138 LEU   I CD1 1 
ATOM   654   C CD2 . LEU   A  1 138 ? 36.81566  24.24986  -33.92289 1.000 35.28254  ?  138 LEU   I CD2 1 
ATOM   655   N N   . ASN   A  1 139 ? 36.51740  21.74629  -29.70410 1.000 34.22306  ?  139 ASN   I N   1 
ATOM   656   C CA  . ASN   A  1 139 ? 35.21877  21.39233  -29.14708 1.000 50.42550  ?  139 ASN   I CA  1 
ATOM   657   C C   . ASN   A  1 139 ? 35.11668  21.75184  -27.66990 1.000 37.03278  ?  139 ASN   I C   1 
ATOM   658   O O   . ASN   A  1 139 ? 34.01028  22.02770  -27.18523 1.000 50.93497  ?  139 ASN   I O   1 
ATOM   659   C CB  . ASN   A  1 139 ? 34.93476  19.91362  -29.40396 1.000 26.72667  ?  139 ASN   I CB  1 
ATOM   660   C CG  . ASN   A  1 139 ? 34.55869  19.66998  -30.84965 1.000 43.54913  ?  139 ASN   I CG  1 
ATOM   661   O OD1 . ASN   A  1 139 ? 33.80686  20.46368  -31.43042 1.000 35.12798  ?  139 ASN   I OD1 1 
ATOM   662   N ND2 . ASN   A  1 139 ? 35.10490  18.62020  -31.45691 1.000 31.94885  ?  139 ASN   I ND2 1 
ATOM   663   N N   . LEU   A  1 140 ? 36.24804  21.78698  -26.94999 1.000 42.01873  ?  140 LEU   I N   1 
ATOM   664   C CA  . LEU   A  1 140 ? 36.23484  22.30591  -25.58144 1.000 30.17034  ?  140 LEU   I CA  1 
ATOM   665   C C   . LEU   A  1 140 ? 35.68798  23.72540  -25.53718 1.000 52.45050  ?  140 LEU   I C   1 
ATOM   666   O O   . LEU   A  1 140 ? 34.97916  24.09477  -24.58917 1.000 31.37591  ?  140 LEU   I O   1 
ATOM   667   C CB  . LEU   A  1 140 ? 37.63526  22.28560  -24.98292 1.000 29.70899  ?  140 LEU   I CB  1 
ATOM   668   C CG  . LEU   A  1 140 ? 38.14888  20.90595  -24.60027 1.000 45.95007  ?  140 LEU   I CG  1 
ATOM   669   C CD1 . LEU   A  1 140 ? 39.58275  20.96666  -24.11210 1.000 23.91825  ?  140 LEU   I CD1 1 
ATOM   670   C CD2 . LEU   A  1 140 ? 37.24711  20.30924  -23.55088 1.000 17.77340  ?  140 LEU   I CD2 1 
ATOM   671   N N   . HIS   A  1 141 ? 36.00818  24.53871  -26.55728 1.000 42.06925  ?  141 HIS   I N   1 
ATOM   672   C CA  . HIS   A  1 141 ? 35.51992  25.91410  -26.57656 1.000 39.96796  ?  141 HIS   I CA  1 
ATOM   673   C C   . HIS   A  1 141 ? 34.03419  25.97420  -26.90857 1.000 41.14500  ?  141 HIS   I C   1 
ATOM   674   O O   . HIS   A  1 141 ? 33.27871  26.69546  -26.24691 1.000 47.83199  ?  141 HIS   I O   1 
ATOM   675   C CB  . HIS   A  1 141 ? 36.33601  26.74140  -27.55301 1.000 29.94385  ?  141 HIS   I CB  1 
ATOM   676   C CG  . HIS   A  1 141 ? 37.71467  27.03542  -27.05636 1.000 57.49461  ?  141 HIS   I CG  1 
ATOM   677   N ND1 . HIS   A  1 141 ? 37.98041  28.06537  -26.18135 1.000 55.33208  ?  141 HIS   I ND1 1 
ATOM   678   C CD2 . HIS   A  1 141 ? 38.89930  26.41574  -27.28087 1.000 50.65335  ?  141 HIS   I CD2 1 
ATOM   679   C CE1 . HIS   A  1 141 ? 39.27117  28.07775  -25.89985 1.000 42.85436  ?  141 HIS   I CE1 1 
ATOM   680   N NE2 . HIS   A  1 141 ? 39.85295  27.09005  -26.55748 1.000 56.10265  ?  141 HIS   I NE2 1 
ATOM   681   N N   . PHE   A  1 142 ? 33.58618  25.20703  -27.91079 1.000 42.77492  ?  142 PHE   I N   1 
ATOM   682   C CA  . PHE   A  1 142 ? 32.14916  25.12725  -28.17552 1.000 56.00994  ?  142 PHE   I CA  1 
ATOM   683   C C   . PHE   A  1 142 ? 31.38480  24.74000  -26.91820 1.000 42.90468  ?  142 PHE   I C   1 
ATOM   684   O O   . PHE   A  1 142 ? 30.31654  25.29905  -26.62807 1.000 44.86385  ?  142 PHE   I O   1 
ATOM   685   C CB  . PHE   A  1 142 ? 31.86434  24.12922  -29.29674 1.000 41.97575  ?  142 PHE   I CB  1 
ATOM   686   C CG  . PHE   A  1 142 ? 32.19170  24.64881  -30.66344 1.000 49.16013  ?  142 PHE   I CG  1 
ATOM   687   C CD1 . PHE   A  1 142 ? 31.76870  25.90388  -31.05808 1.000 43.99217  ?  142 PHE   I CD1 1 
ATOM   688   C CD2 . PHE   A  1 142 ? 32.93307  23.88515  -31.55300 1.000 45.48323  ?  142 PHE   I CD2 1 
ATOM   689   C CE1 . PHE   A  1 142 ? 32.07639  26.38276  -32.31714 1.000 43.07093  ?  142 PHE   I CE1 1 
ATOM   690   C CE2 . PHE   A  1 142 ? 33.23608  24.36580  -32.81670 1.000 46.58850  ?  142 PHE   I CE2 1 
ATOM   691   C CZ  . PHE   A  1 142 ? 32.80740  25.61220  -33.19156 1.000 41.80515  ?  142 PHE   I CZ  1 
ATOM   692   N N   . LYS   A  1 143 ? 31.91919  23.78541  -26.15870 1.000 41.51762  ?  143 LYS   I N   1 
ATOM   693   C CA  . LYS   A  1 143 ? 31.27361  23.40185  -24.91353 1.000 37.18459  ?  143 LYS   I CA  1 
ATOM   694   C C   . LYS   A  1 143 ? 31.08196  24.61240  -24.01937 1.000 40.46022  ?  143 LYS   I C   1 
ATOM   695   O O   . LYS   A  1 143 ? 29.96671  24.87040  -23.54555 1.000 43.82179  ?  143 LYS   I O   1 
ATOM   696   C CB  . LYS   A  1 143 ? 32.09027  22.33124  -24.19990 1.000 40.73773  ?  143 LYS   I CB  1 
ATOM   697   C CG  . LYS   A  1 143 ? 31.32596  21.65892  -23.09530 1.000 27.30243  ?  143 LYS   I CG  1 
ATOM   698   C CD  . LYS   A  1 143 ? 32.22550  21.28894  -21.95258 1.000 35.46404  ?  143 LYS   I CD  1 
ATOM   699   C CE  . LYS   A  1 143 ? 31.51473  20.33826  -21.00859 1.000 42.02234  ?  143 LYS   I CE  1 
ATOM   700   N NZ  . LYS   A  1 143 ? 30.34871  20.94974  -20.31608 1.000 46.63149  ?  143 LYS   I NZ  1 
ATOM   701   N N   . LYS   A  1 144 ? 32.15748  25.36063  -23.75990 1.000 56.53477  ?  144 LYS   I N   1 
ATOM   702   C CA  . LYS   A  1 144 ? 32.05779  26.54224  -22.90237 1.000 47.29942  ?  144 LYS   I CA  1 
ATOM   703   C C   . LYS   A  1 144 ? 31.14502  27.61538  -23.50022 1.000 54.19809  ?  144 LYS   I C   1 
ATOM   704   O O   . LYS   A  1 144 ? 30.44259  28.28069  -22.75181 1.000 32.81181  ?  144 LYS   I O   1 
ATOM   705   C CB  . LYS   A  1 144 ? 33.45636  27.12271  -22.61667 1.000 17.88824  ?  144 LYS   I CB  1 
ATOM   706   C CG  . LYS   A  1 144 ? 33.48161  28.41518  -21.76353 1.000 49.84607  ?  144 LYS   I CG  1 
ATOM   707   C CD  . LYS   A  1 144 ? 33.69640  28.15659  -20.27619 1.000 85.11806  ?  144 LYS   I CD  1 
ATOM   708   C CE  . LYS   A  1 144 ? 33.11900  29.30305  -19.45485 1.000 81.87267  ?  144 LYS   I CE  1 
ATOM   709   N NZ  . LYS   A  1 144 ? 32.27734  28.81346  -18.33834 1.000 125.98291 ?  144 LYS   I NZ  1 
ATOM   710   N N   . LEU   A  1 145 ? 31.13363  27.80358  -24.82461 1.000 35.05026  ?  145 LEU   I N   1 
ATOM   711   C CA  . LEU   A  1 145 ? 30.20553  28.75317  -25.43276 1.000 29.47829  ?  145 LEU   I CA  1 
ATOM   712   C C   . LEU   A  1 145 ? 28.75940  28.36147  -25.13583 1.000 49.63955  ?  145 LEU   I C   1 
ATOM   713   O O   . LEU   A  1 145 ? 27.98220  29.16098  -24.59854 1.000 47.86645  ?  145 LEU   I O   1 
ATOM   714   C CB  . LEU   A  1 145 ? 30.45534  28.84914  -26.94207 1.000 40.31457  ?  145 LEU   I CB  1 
ATOM   715   C CG  . LEU   A  1 145 ? 31.83554  29.39379  -27.33189 1.000 42.96589  ?  145 LEU   I CG  1 
ATOM   716   C CD1 . LEU   A  1 145 ? 31.98968  29.54380  -28.83991 1.000 36.66700  ?  145 LEU   I CD1 1 
ATOM   717   C CD2 . LEU   A  1 145 ? 32.07663  30.71869  -26.65288 1.000 36.04683  ?  145 LEU   I CD2 1 
ATOM   718   N N   . PHE   A  1 146 ? 28.39838  27.10822  -25.42016 1.000 32.76588  ?  146 PHE   I N   1 
ATOM   719   C CA  . PHE   A  1 146 ? 27.00721  26.69409  -25.26517 1.000 36.72000  ?  146 PHE   I CA  1 
ATOM   720   C C   . PHE   A  1 146 ? 26.60555  26.58959  -23.80047 1.000 44.95927  ?  146 PHE   I C   1 
ATOM   721   O O   . PHE   A  1 146 ? 25.45651  26.88716  -23.45736 1.000 45.66899  ?  146 PHE   I O   1 
ATOM   722   C CB  . PHE   A  1 146 ? 26.77304  25.36624  -25.99139 1.000 36.94867  ?  146 PHE   I CB  1 
ATOM   723   C CG  . PHE   A  1 146 ? 27.12333  25.40510  -27.46611 1.000 40.52231  ?  146 PHE   I CG  1 
ATOM   724   C CD1 . PHE   A  1 146 ? 27.12593  26.60884  -28.17363 1.000 40.56573  ?  146 PHE   I CD1 1 
ATOM   725   C CD2 . PHE   A  1 146 ? 27.43872  24.24085  -28.14306 1.000 33.63078  ?  146 PHE   I CD2 1 
ATOM   726   C CE1 . PHE   A  1 146 ? 27.43757  26.64073  -29.52263 1.000 40.68101  ?  146 PHE   I CE1 1 
ATOM   727   C CE2 . PHE   A  1 146 ? 27.75623  24.26253  -29.49515 1.000 37.21384  ?  146 PHE   I CE2 1 
ATOM   728   C CZ  . PHE   A  1 146 ? 27.75334  25.46195  -30.18896 1.000 42.87202  ?  146 PHE   I CZ  1 
ATOM   729   N N   . ASP   A  1 147 ? 27.52056  26.17512  -22.92065 1.000 42.52683  ?  147 ASP   I N   1 
ATOM   730   C CA  . ASP   A  1 147 ? 27.19450  26.20246  -21.49744 1.000 36.15485  ?  147 ASP   I CA  1 
ATOM   731   C C   . ASP   A  1 147 ? 26.89056  27.62595  -21.04795 1.000 45.71957  ?  147 ASP   I C   1 
ATOM   732   O O   . ASP   A  1 147 ? 25.93633  27.86163  -20.28588 1.000 44.03341  ?  147 ASP   I O   1 
ATOM   733   C CB  . ASP   A  1 147 ? 28.33529  25.61619  -20.65899 1.000 28.60130  ?  147 ASP   I CB  1 
ATOM   734   C CG  . ASP   A  1 147 ? 28.45269  24.09930  -20.77984 1.000 61.67946  ?  147 ASP   I CG  1 
ATOM   735   O OD1 . ASP   A  1 147 ? 27.47953  23.42368  -21.20942 1.000 53.79545  ?  147 ASP   I OD1 1 
ATOM   736   O OD2 . ASP   A  1 147 ? 29.53551  23.58728  -20.42162 1.000 57.97592  ?  147 ASP   I OD2 1 
ATOM   737   N N   . THR   A  1 148 ? 27.69830  28.58864  -21.51195 1.000 38.06487  ?  148 THR   I N   1 
ATOM   738   C CA  . THR   A  1 148 ? 27.46297  29.98912  -21.17943 1.000 47.51366  ?  148 THR   I CA  1 
ATOM   739   C C   . THR   A  1 148 ? 26.08857  30.42498  -21.67045 1.000 44.41944  ?  148 THR   I C   1 
ATOM   740   O O   . THR   A  1 148 ? 25.31106  31.03046  -20.91985 1.000 50.43509  ?  148 THR   I O   1 
ATOM   741   C CB  . THR   A  1 148 ? 28.57529  30.86111  -21.77874 1.000 42.37489  ?  148 THR   I CB  1 
ATOM   742   O OG1 . THR   A  1 148 ? 29.79395  30.63296  -21.06370 1.000 43.24244  ?  148 THR   I OG1 1 
ATOM   743   C CG2 . THR   A  1 148 ? 28.23042  32.34137  -21.68740 1.000 31.67828  ?  148 THR   I CG2 1 
ATOM   744   N N   . TRP   A  1 149 ? 25.76334  30.08641  -22.92752 1.000 40.15936  ?  149 TRP   I N   1 
ATOM   745   C CA  . TRP   A  1 149 ? 24.45224  30.40352  -23.48502 1.000 33.26526  ?  149 TRP   I CA  1 
ATOM   746   C C   . TRP   A  1 149 ? 23.34471  29.78539  -22.64242 1.000 57.29157  ?  149 TRP   I C   1 
ATOM   747   O O   . TRP   A  1 149 ? 22.33914  30.44127  -22.34549 1.000 42.11080  ?  149 TRP   I O   1 
ATOM   748   C CB  . TRP   A  1 149 ? 24.37633  29.91126  -24.93682 1.000 30.83612  ?  149 TRP   I CB  1 
ATOM   749   C CG  . TRP   A  1 149 ? 23.12222  30.32885  -25.70494 1.000 41.86089  ?  149 TRP   I CG  1 
ATOM   750   C CD1 . TRP   A  1 149 ? 22.20079  31.26938  -25.33074 1.000 36.18297  ?  149 TRP   I CD1 1 
ATOM   751   C CD2 . TRP   A  1 149 ? 22.66506  29.81005  -26.97146 1.000 52.19954  ?  149 TRP   I CD2 1 
ATOM   752   N NE1 . TRP   A  1 149 ? 21.20952  31.37181  -26.28061 1.000 48.39488  ?  149 TRP   I NE1 1 
ATOM   753   C CE2 . TRP   A  1 149 ? 21.46832  30.48729  -27.29449 1.000 34.67340  ?  149 TRP   I CE2 1 
ATOM   754   C CE3 . TRP   A  1 149 ? 23.15039  28.83660  -27.86134 1.000 33.79086  ?  149 TRP   I CE3 1 
ATOM   755   C CZ2 . TRP   A  1 149 ? 20.75482  30.23391  -28.47421 1.000 44.11892  ?  149 TRP   I CZ2 1 
ATOM   756   C CZ3 . TRP   A  1 149 ? 22.42864  28.57840  -29.04305 1.000 36.65305  ?  149 TRP   I CZ3 1 
ATOM   757   C CH2 . TRP   A  1 149 ? 21.24942  29.27668  -29.33225 1.000 43.87042  ?  149 TRP   I CH2 1 
ATOM   758   N N   . GLY   A  1 150 ? 23.53105  28.52843  -22.22151 1.000 45.20068  ?  150 GLY   I N   1 
ATOM   759   C CA  . GLY   A  1 150 ? 22.48712  27.83375  -21.49171 1.000 34.55766  ?  150 GLY   I CA  1 
ATOM   760   C C   . GLY   A  1 150 ? 22.17191  28.47301  -20.15564 1.000 55.85015  ?  150 GLY   I C   1 
ATOM   761   O O   . GLY   A  1 150 ? 21.04429  28.35806  -19.65718 1.000 67.90385  ?  150 GLY   I O   1 
ATOM   762   N N   . LEU   A  1 151 ? 23.16116  29.14062  -19.55413 1.000 40.91986  ?  151 LEU   I N   1 
ATOM   763   C CA  . LEU   A  1 151 ? 22.91437  29.94556  -18.35900 1.000 35.63801  ?  151 LEU   I CA  1 
ATOM   764   C C   . LEU   A  1 151 ? 21.82559  30.97177  -18.59862 1.000 75.07854  ?  151 LEU   I C   1 
ATOM   765   O O   . LEU   A  1 151 ? 20.87604  31.09629  -17.81088 1.000 48.13641  ?  151 LEU   I O   1 
ATOM   766   C CB  . LEU   A  1 151 ? 24.17242  30.68229  -17.96647 1.000 47.83340  ?  151 LEU   I CB  1 
ATOM   767   C CG  . LEU   A  1 151 ? 25.23797  29.82004  -17.36907 1.000 68.93007  ?  151 LEU   I CG  1 
ATOM   768   C CD1 . LEU   A  1 151 ? 26.27830  30.80502  -16.96806 1.000 34.10351  ?  151 LEU   I CD1 1 
ATOM   769   C CD2 . LEU   A  1 151 ? 24.60654  29.12852  -16.19773 1.000 22.62642  ?  151 LEU   I CD2 1 
ATOM   770   N N   . PHE   A  1 152 ? 22.00164  31.77546  -19.64909 1.000 37.22824  ?  152 PHE   I N   1 
ATOM   771   C CA  . PHE   A  1 152 ? 20.98386  32.74342  -20.01337 1.000 49.97863  ?  152 PHE   I CA  1 
ATOM   772   C C   . PHE   A  1 152 ? 19.63925  32.07056  -20.26795 1.000 63.21189  ?  152 PHE   I C   1 
ATOM   773   O O   . PHE   A  1 152 ? 18.59272  32.61073  -19.89634 1.000 55.66699  ?  152 PHE   I O   1 
ATOM   774   C CB  . PHE   A  1 152 ? 21.42656  33.52604  -21.24251 1.000 32.24201  ?  152 PHE   I CB  1 
ATOM   775   C CG  . PHE   A  1 152 ? 20.36676  34.40804  -21.77076 1.000 58.49962  ?  152 PHE   I CG  1 
ATOM   776   C CD1 . PHE   A  1 152 ? 20.04824  35.57687  -21.11305 1.000 41.45036  ?  152 PHE   I CD1 1 
ATOM   777   C CD2 . PHE   A  1 152 ? 19.63944  34.04271  -22.88989 1.000 49.31752  ?  152 PHE   I CD2 1 
ATOM   778   C CE1 . PHE   A  1 152 ? 19.04144  36.38424  -21.57862 1.000 48.44464  ?  152 PHE   I CE1 1 
ATOM   779   C CE2 . PHE   A  1 152 ? 18.63456  34.84788  -23.36689 1.000 58.89608  ?  152 PHE   I CE2 1 
ATOM   780   C CZ  . PHE   A  1 152 ? 18.33387  36.02249  -22.71392 1.000 50.64498  ?  152 PHE   I CZ  1 
ATOM   781   N N   . LEU   A  1 153 ? 19.64073  30.89005  -20.89301 1.000 46.34545  ?  153 LEU   I N   1 
ATOM   782   C CA  . LEU   A  1 153 ? 18.38066  30.24264  -21.24158 1.000 48.25242  ?  153 LEU   I CA  1 
ATOM   783   C C   . LEU   A  1 153 ? 17.68649  29.60649  -20.04088 1.000 47.83777  ?  153 LEU   I C   1 
ATOM   784   O O   . LEU   A  1 153 ? 16.57148  29.09372  -20.18471 1.000 52.23295  ?  153 LEU   I O   1 
ATOM   785   C CB  . LEU   A  1 153 ? 18.62024  29.20239  -22.32612 1.000 40.97283  ?  153 LEU   I CB  1 
ATOM   786   C CG  . LEU   A  1 153 ? 19.21033  29.73199  -23.62666 1.000 54.04076  ?  153 LEU   I CG  1 
ATOM   787   C CD1 . LEU   A  1 153 ? 19.52218  28.56118  -24.54516 1.000 36.21884  ?  153 LEU   I CD1 1 
ATOM   788   C CD2 . LEU   A  1 153 ? 18.26467  30.72472  -24.30006 1.000 36.23508  ?  153 LEU   I CD2 1 
ATOM   789   N N   . SER   A  1 154 ? 18.32385  29.62798  -18.87230 1.000 47.46230  ?  154 SER   I N   1 
ATOM   790   C CA  . SER   A  1 154 ? 17.73584  29.19660  -17.61420 1.000 45.21334  ?  154 SER   I CA  1 
ATOM   791   C C   . SER   A  1 154 ? 17.24603  30.36963  -16.77537 1.000 55.29540  ?  154 SER   I C   1 
ATOM   792   O O   . SER   A  1 154 ? 16.67871  30.15249  -15.70045 1.000 59.53677  ?  154 SER   I O   1 
ATOM   793   C CB  . SER   A  1 154 ? 18.76337  28.38870  -16.81367 1.000 32.41010  ?  154 SER   I CB  1 
ATOM   794   O OG  . SER   A  1 154 ? 19.06909  27.19490  -17.50152 1.000 113.04417 ?  154 SER   I OG  1 
ATOM   795   N N   . SER   A  1 155 ? 17.45407  31.59892  -17.24207 1.000 47.72707  ?  155 SER   I N   1 
ATOM   796   C CA  . SER   A  1 155 ? 17.21956  32.82071  -16.48842 1.000 48.35094  ?  155 SER   I CA  1 
ATOM   797   C C   . SER   A  1 155 ? 15.87054  33.42323  -16.85765 1.000 112.95538 ?  155 SER   I C   1 
ATOM   798   O O   . SER   A  1 155 ? 15.36585  33.22570  -17.97137 1.000 46.44052  ?  155 SER   I O   1 
ATOM   799   C CB  . SER   A  1 155 ? 18.32634  33.83818  -16.76660 1.000 45.10358  ?  155 SER   I CB  1 
ATOM   800   O OG  . SER   A  1 155 ? 18.23481  34.36715  -18.08194 1.000 55.15306  ?  155 SER   I OG  1 
ATOM   801   N N   . LYS   A  1 156 ? 15.29986  34.18817  -15.91015 1.000 61.24023  ?  156 LYS   I N   1 
ATOM   802   C CA  . LYS   A  1 156 ? 13.97844  34.77349  -16.13358 1.000 78.05846  ?  156 LYS   I CA  1 
ATOM   803   C C   . LYS   A  1 156 ? 13.95763  35.60475  -17.41476 1.000 51.47938  ?  156 LYS   I C   1 
ATOM   804   O O   . LYS   A  1 156 ? 12.93288  35.65722  -18.10827 1.000 67.32359  ?  156 LYS   I O   1 
ATOM   805   C CB  . LYS   A  1 156 ? 13.54795  35.61031  -14.91789 1.000 44.19471  ?  156 LYS   I CB  1 
ATOM   806   N N   . ASP   A  1 157 ? 15.10528  36.18969  -17.78774 1.000 55.72137  ?  157 ASP   I N   1 
ATOM   807   C CA  . ASP   A  1 157 ? 15.17773  37.07150  -18.95486 1.000 54.69375  ?  157 ASP   I CA  1 
ATOM   808   C C   . ASP   A  1 157 ? 14.94977  36.34101  -20.27071 1.000 57.21283  ?  157 ASP   I C   1 
ATOM   809   O O   . ASP   A  1 157 ? 14.56274  36.97739  -21.25949 1.000 53.09870  ?  157 ASP   I O   1 
ATOM   810   C CB  . ASP   A  1 157 ? 16.53118  37.78303  -19.00154 1.000 66.04526  ?  157 ASP   I CB  1 
ATOM   811   C CG  . ASP   A  1 157 ? 16.70312  38.79523  -17.87518 1.000 67.08331  ?  157 ASP   I CG  1 
ATOM   812   O OD1 . ASP   A  1 157 ? 15.79855  39.63446  -17.67772 1.000 77.68445  ?  157 ASP   I OD1 1 
ATOM   813   O OD2 . ASP   A  1 157 ? 17.74676  38.74363  -17.18523 1.000 96.38748  ?  157 ASP   I OD2 1 
ATOM   814   N N   . SER   A  1 158 ? 15.19188  35.02925  -20.31423 1.000 69.94818  ?  158 SER   I N   1 
ATOM   815   C CA  . SER   A  1 158 ? 14.94953  34.28644  -21.54301 1.000 55.37724  ?  158 SER   I CA  1 
ATOM   816   C C   . SER   A  1 158 ? 13.46497  34.03054  -21.79301 1.000 58.22217  ?  158 SER   I C   1 
ATOM   817   O O   . SER   A  1 158 ? 13.13558  33.44925  -22.83337 1.000 53.28106  ?  158 SER   I O   1 
ATOM   818   C CB  . SER   A  1 158 ? 15.71660  32.95859  -21.51840 1.000 48.83477  ?  158 SER   I CB  1 
ATOM   819   O OG  . SER   A  1 158 ? 15.16617  32.06560  -20.56102 1.000 48.29327  ?  158 SER   I OG  1 
ATOM   820   N N   . ARG   A  1 159 ? 12.56478  34.44923  -20.88998 1.000 49.95942  ?  159 ARG   I N   1 
ATOM   821   C CA  . ARG   A  1 159 ? 11.13170  34.26380  -21.12387 1.000 57.17562  ?  159 ARG   I CA  1 
ATOM   822   C C   . ARG   A  1 159 ? 10.58950  35.14664  -22.24306 1.000 57.93210  ?  159 ARG   I C   1 
ATOM   823   O O   . ARG   A  1 159 ? 9.49843   34.87506  -22.74956 1.000 52.34995  ?  159 ARG   I O   1 
ATOM   824   C CB  . ARG   A  1 159 ? 10.33560  34.54545  -19.85214 1.000 39.80813  ?  159 ARG   I CB  1 
ATOM   825   C CG  . ARG   A  1 159 ? 10.48025  33.47501  -18.79569 1.000 75.77791  ?  159 ARG   I CG  1 
ATOM   826   C CD  . ARG   A  1 159 ? 9.87920   33.96332  -17.50857 1.000 59.86117  ?  159 ARG   I CD  1 
ATOM   827   N NE  . ARG   A  1 159 ? 10.43226  35.26380  -17.16397 1.000 73.72376  ?  159 ARG   I NE  1 
ATOM   828   C CZ  . ARG   A  1 159 ? 9.90490   36.09201  -16.27493 1.000 64.89116  ?  159 ARG   I CZ  1 
ATOM   829   N NH1 . ARG   A  1 159 ? 8.79058   35.79171  -15.62436 1.000 57.36299  ?  159 ARG   I NH1 1 
ATOM   830   N NH2 . ARG   A  1 159 ? 10.50898  37.25103  -16.03627 1.000 54.58355  ?  159 ARG   I NH2 1 
ATOM   831   N N   . ASN   A  1 160 ? 11.32538  36.17964  -22.65751 1.000 53.26578  ?  160 ASN   I N   1 
ATOM   832   C CA  . ASN   A  1 160 ? 10.77815  37.15414  -23.59806 1.000 57.61122  ?  160 ASN   I CA  1 
ATOM   833   C C   . ASN   A  1 160 ? 10.39022  36.55848  -24.94985 1.000 50.03887  ?  160 ASN   I C   1 
ATOM   834   O O   . ASN   A  1 160 ? 9.66436   37.20924  -25.70638 1.000 79.81068  ?  160 ASN   I O   1 
ATOM   835   C CB  . ASN   A  1 160 ? 11.77712  38.28757  -23.80238 1.000 55.66076  ?  160 ASN   I CB  1 
ATOM   836   C CG  . ASN   A  1 160 ? 12.94391  37.87245  -24.64501 1.000 67.83525  ?  160 ASN   I CG  1 
ATOM   837   O OD1 . ASN   A  1 160 ? 13.76048  37.04244  -24.23137 1.000 81.29122  ?  160 ASN   I OD1 1 
ATOM   838   N ND2 . ASN   A  1 160 ? 13.03172  38.43355  -25.84324 1.000 72.02868  ?  160 ASN   I ND2 1 
ATOM   839   N N   . VAL   A  1 161 ? 10.86172  35.35668  -25.29083 1.000 59.96044  ?  161 VAL   I N   1 
ATOM   840   C CA  . VAL   A  1 161 ? 10.38021  34.70031  -26.50817 1.000 62.76544  ?  161 VAL   I CA  1 
ATOM   841   C C   . VAL   A  1 161 ? 9.12284   33.88530  -26.25877 1.000 65.46546  ?  161 VAL   I C   1 
ATOM   842   O O   . VAL   A  1 161 ? 8.53173   33.36054  -27.21768 1.000 48.16943  ?  161 VAL   I O   1 
ATOM   843   C CB  . VAL   A  1 161 ? 11.43865  33.76550  -27.12927 1.000 56.71184  ?  161 VAL   I CB  1 
ATOM   844   C CG1 . VAL   A  1 161 ? 12.66890  34.55409  -27.59593 1.000 45.57706  ?  161 VAL   I CG1 1 
ATOM   845   C CG2 . VAL   A  1 161 ? 11.81087  32.68426  -26.13668 1.000 40.46921  ?  161 VAL   I CG2 1 
ATOM   846   N N   . LEU   A  1 162 ? 8.70911   33.74253  -25.00141 1.000 46.86085  ?  162 LEU   I N   1 
ATOM   847   C CA  . LEU   A  1 162 ? 7.51975   32.97472  -24.64695 1.000 57.30669  ?  162 LEU   I CA  1 
ATOM   848   C C   . LEU   A  1 162 ? 6.29505   33.88928  -24.72682 1.000 76.23710  ?  162 LEU   I C   1 
ATOM   849   O O   . LEU   A  1 162 ? 5.66548   34.26302  -23.73149 1.000 58.83339  ?  162 LEU   I O   1 
ATOM   850   C CB  . LEU   A  1 162 ? 7.68891   32.36344  -23.26502 1.000 53.96352  ?  162 LEU   I CB  1 
ATOM   851   C CG  . LEU   A  1 162 ? 8.89339   31.43859  -23.15431 1.000 42.60297  ?  162 LEU   I CG  1 
ATOM   852   C CD1 . LEU   A  1 162 ? 8.89090   30.72337  -21.81462 1.000 38.29667  ?  162 LEU   I CD1 1 
ATOM   853   C CD2 . LEU   A  1 162 ? 8.85330   30.44123  -24.31422 1.000 37.13965  ?  162 LEU   I CD2 1 
ATOM   854   N N   . VAL   A  1 163 ? 5.97463   34.25734  -25.96548 1.000 43.56184  ?  163 VAL   I N   1 
ATOM   855   C CA  . VAL   A  1 163 ? 4.96383   35.25799  -26.29036 1.000 40.60694  ?  163 VAL   I CA  1 
ATOM   856   C C   . VAL   A  1 163 ? 4.32031   34.85441  -27.61193 1.000 61.03237  ?  163 VAL   I C   1 
ATOM   857   O O   . VAL   A  1 163 ? 4.80997   33.97281  -28.32364 1.000 53.61506  ?  163 VAL   I O   1 
ATOM   858   C CB  . VAL   A  1 163 ? 5.56038   36.68370  -26.41166 1.000 42.56754  ?  163 VAL   I CB  1 
ATOM   859   C CG1 . VAL   A  1 163 ? 6.21060   37.14022  -25.08720 1.000 36.15176  ?  163 VAL   I CG1 1 
ATOM   860   C CG2 . VAL   A  1 163 ? 6.56514   36.74753  -27.56641 1.000 35.68072  ?  163 VAL   I CG2 1 
ATOM   861   N N   . ALA   A  1 164 ? 3.21971   35.52017  -27.96268 1.000 56.06880  ?  164 ALA   I N   1 
ATOM   862   C CA  . ALA   A  1 164 ? 2.58737   35.24667  -29.24911 1.000 63.67479  ?  164 ALA   I CA  1 
ATOM   863   C C   . ALA   A  1 164 ? 3.05350   36.18250  -30.35425 1.000 54.67509  ?  164 ALA   I C   1 
ATOM   864   O O   . ALA   A  1 164 ? 2.81412   35.88536  -31.53169 1.000 52.58983  ?  164 ALA   I O   1 
ATOM   865   C CB  . ALA   A  1 164 ? 1.06868   35.32905  -29.12566 1.000 34.53131  ?  164 ALA   I CB  1 
ATOM   866   N N   . ASP   A  1 165 ? 3.72252   37.28648  -29.99174 1.000 51.70264  ?  165 ASP   I N   1 
ATOM   867   C CA  . ASP   A  1 165 ? 4.20212   38.29292  -30.93451 1.000 50.03709  ?  165 ASP   I CA  1 
ATOM   868   C C   . ASP   A  1 165 ? 4.82993   37.65454  -32.16830 1.000 49.89757  ?  165 ASP   I C   1 
ATOM   869   O O   . ASP   A  1 165 ? 5.63292   36.72535  -32.07131 1.000 84.91960  ?  165 ASP   I O   1 
ATOM   870   C CB  . ASP   A  1 165 ? 5.23450   39.21078  -30.25493 1.000 57.31309  ?  165 ASP   I CB  1 
ATOM   871   C CG  . ASP   A  1 165 ? 4.78010   39.72576  -28.89288 1.000 45.26606  ?  165 ASP   I CG  1 
ATOM   872   O OD1 . ASP   A  1 165 ? 3.63344   39.44615  -28.47651 1.000 91.51702  ?  165 ASP   I OD1 1 
ATOM   873   O OD2 . ASP   A  1 165 ? 5.59065   40.41974  -28.23735 1.000 94.21512  ?  165 ASP   I OD2 1 
ATOM   874   N N   . GLN   A  1 166 ? 4.44033   38.14829  -33.33266 1.000 57.63834  ?  166 GLN   I N   1 
ATOM   875   C CA  . GLN   A  1 166 ? 5.16003   37.86271  -34.56161 1.000 72.10668  ?  166 GLN   I CA  1 
ATOM   876   C C   . GLN   A  1 166 ? 6.34442   38.82093  -34.61828 1.000 34.36581  ?  166 GLN   I C   1 
ATOM   877   O O   . GLN   A  1 166 ? 6.18448   40.01628  -34.35988 1.000 107.96734 ?  166 GLN   I O   1 
ATOM   878   C CB  . GLN   A  1 166 ? 4.23165   38.01644  -35.77237 1.000 31.69225  ?  166 GLN   I CB  1 
ATOM   879   C CG  . GLN   A  1 166 ? 4.86845   37.78397  -37.11857 1.000 68.20822  ?  166 GLN   I CG  1 
ATOM   880   C CD  . GLN   A  1 166 ? 4.70670   36.35582  -37.57195 1.000 127.62756 ?  166 GLN   I CD  1 
ATOM   881   O OE1 . GLN   A  1 166 ? 5.49910   35.85225  -38.37643 1.000 82.39264  ?  166 GLN   I OE1 1 
ATOM   882   N NE2 . GLN   A  1 166 ? 3.67922   35.68794  -37.06066 1.000 68.79628  ?  166 GLN   I NE2 1 
ATOM   883   N N   . PHE   A  1 167 ? 7.53697   38.28989  -34.89562 1.000 65.89456  ?  167 PHE   I N   1 
ATOM   884   C CA  . PHE   A  1 167 ? 8.77543   39.06476  -34.81608 1.000 64.85248  ?  167 PHE   I CA  1 
ATOM   885   C C   . PHE   A  1 167 ? 9.23528   39.62021  -36.15690 1.000 66.35631  ?  167 PHE   I C   1 
ATOM   886   O O   . PHE   A  1 167 ? 9.91577   40.64970  -36.18754 1.000 62.33585  ?  167 PHE   I O   1 
ATOM   887   C CB  . PHE   A  1 167 ? 9.91375   38.20548  -34.24928 1.000 54.95411  ?  167 PHE   I CB  1 
ATOM   888   C CG  . PHE   A  1 167 ? 9.72949   37.80505  -32.81355 1.000 60.45017  ?  167 PHE   I CG  1 
ATOM   889   C CD1 . PHE   A  1 167 ? 9.88251   36.49032  -32.41084 1.000 48.66447  ?  167 PHE   I CD1 1 
ATOM   890   C CD2 . PHE   A  1 167 ? 9.42873   38.74140  -31.86500 1.000 39.77244  ?  167 PHE   I CD2 1 
ATOM   891   C CE1 . PHE   A  1 167 ? 9.71964   36.12931  -31.08140 1.000 119.38788 ?  167 PHE   I CE1 1 
ATOM   892   C CE2 . PHE   A  1 167 ? 9.26586   38.38689  -30.53852 1.000 108.20894 ?  167 PHE   I CE2 1 
ATOM   893   C CZ  . PHE   A  1 167 ? 9.40450   37.09438  -30.14527 1.000 27.49010  ?  167 PHE   I CZ  1 
ATOM   894   N N   . ASP   A  1 168 ? 8.92349   38.93580  -37.25023 1.000 68.01271  ?  168 ASP   I N   1 
ATOM   895   C CA  . ASP   A  1 168 ? 9.21614   39.38034  -38.60547 1.000 33.28629  ?  168 ASP   I CA  1 
ATOM   896   C C   . ASP   A  1 168 ? 8.40762   38.49861  -39.54939 1.000 84.59682  ?  168 ASP   I C   1 
ATOM   897   O O   . ASP   A  1 168 ? 7.45408   37.81167  -39.09782 1.000 58.12134  ?  168 ASP   I O   1 
ATOM   898   C CB  . ASP   A  1 168 ? 10.74161  39.38804  -38.86611 1.000 47.36585  ?  168 ASP   I CB  1 
ATOM   899   C CG  . ASP   A  1 168 ? 11.36028  37.98086  -38.96353 1.000 72.15317  ?  168 ASP   I CG  1 
ATOM   900   O OD1 . ASP   A  1 168 ? 12.54775  37.81010  -38.58115 1.000 57.98426  ?  168 ASP   I OD1 1 
ATOM   901   O OD2 . ASP   A  1 168 ? 10.68015  37.05054  -39.45138 1.000 69.90884  ?  168 ASP   I OD2 1 
ATOM   902   N N   . ASP   A  1 169 ? 8.72401   38.49456  -40.83933 1.000 68.22292  ?  169 ASP   I N   1 
ATOM   903   C CA  . ASP   A  1 169 ? 7.89178   37.75505  -41.78410 1.000 72.11468  ?  169 ASP   I CA  1 
ATOM   904   C C   . ASP   A  1 169 ? 7.96648   36.24739  -41.53386 1.000 88.96253  ?  169 ASP   I C   1 
ATOM   905   O O   . ASP   A  1 169 ? 6.97594   35.53475  -41.73728 1.000 76.79133  ?  169 ASP   I O   1 
ATOM   906   C CB  . ASP   A  1 169 ? 8.28605   38.09669  -43.22760 1.000 50.69765  ?  169 ASP   I CB  1 
ATOM   907   N N   . ARG   A  1 170 ? 9.10606   35.74674  -41.04182 1.000 141.30702 ?  170 ARG   I N   1 
ATOM   908   C CA  . ARG   A  1 170 ? 9.32925   34.30895  -40.93503 1.000 52.20713  ?  170 ARG   I CA  1 
ATOM   909   C C   . ARG   A  1 170 ? 9.39228   33.76988  -39.50082 1.000 70.49087  ?  170 ARG   I C   1 
ATOM   910   O O   . ARG   A  1 170 ? 9.31814   32.54853  -39.32281 1.000 61.50745  ?  170 ARG   I O   1 
ATOM   911   C CB  . ARG   A  1 170 ? 10.61840  33.93072  -41.68378 1.000 58.06015  ?  170 ARG   I CB  1 
ATOM   912   N N   . HIS   A  1 171 ? 9.49764   34.62872  -38.47571 1.000 65.94093  ?  171 HIS   I N   1 
ATOM   913   C CA  . HIS   A  1 171 ? 9.71782   34.20023  -37.09442 1.000 69.17125  ?  171 HIS   I CA  1 
ATOM   914   C C   . HIS   A  1 171 ? 8.62018   34.71564  -36.17241 1.000 35.72365  ?  171 HIS   I C   1 
ATOM   915   O O   . HIS   A  1 171 ? 8.09497   35.81492  -36.35877 1.000 107.00237 ?  171 HIS   I O   1 
ATOM   916   C CB  . HIS   A  1 171 ? 11.07289  34.69687  -36.54238 1.000 71.94050  ?  171 HIS   I CB  1 
ATOM   917   C CG  . HIS   A  1 171 ? 12.24733  34.35046  -37.40328 1.000 67.12410  ?  171 HIS   I CG  1 
ATOM   918   N ND1 . HIS   A  1 171 ? 12.24254  33.28737  -38.28122 1.000 72.78739  ?  171 HIS   I ND1 1 
ATOM   919   C CD2 . HIS   A  1 171 ? 13.45964  34.93856  -37.53272 1.000 67.35155  ?  171 HIS   I CD2 1 
ATOM   920   C CE1 . HIS   A  1 171 ? 13.40169  33.23147  -38.91051 1.000 47.54153  ?  171 HIS   I CE1 1 
ATOM   921   N NE2 . HIS   A  1 171 ? 14.15939  34.22087  -38.47295 1.000 122.80472 ?  171 HIS   I NE2 1 
ATOM   922   N N   . CYS   A  1 172 ? 8.31056   33.92532  -35.14432 1.000 73.79223  ?  172 CYS   I N   1 
ATOM   923   C CA  . CYS   A  1 172 ? 7.32789   34.31514  -34.14236 1.000 43.11826  ?  172 CYS   I CA  1 
ATOM   924   C C   . CYS   A  1 172 ? 7.70621   33.73126  -32.78805 1.000 44.17684  ?  172 CYS   I C   1 
ATOM   925   O O   . CYS   A  1 172 ? 8.59339   32.88116  -32.67800 1.000 67.10641  ?  172 CYS   I O   1 
ATOM   926   C CB  . CYS   A  1 172 ? 5.92730   33.84624  -34.52189 1.000 52.23378  ?  172 CYS   I CB  1 
ATOM   927   S SG  . CYS   A  1 172 ? 5.79992   32.06253  -34.60954 1.000 60.20797  ?  172 CYS   I SG  1 
ATOM   928   N N   . GLY   A  1 173 ? 6.99697   34.18955  -31.75558 1.000 56.57586  ?  173 GLY   I N   1 
ATOM   929   C CA  . GLY   A  1 173 ? 7.17945   33.66820  -30.41667 1.000 41.22799  ?  173 GLY   I CA  1 
ATOM   930   C C   . GLY   A  1 173 ? 6.58264   32.27877  -30.25518 1.000 55.79609  ?  173 GLY   I C   1 
ATOM   931   O O   . GLY   A  1 173 ? 5.80854   31.79311  -31.08387 1.000 55.85174  ?  173 GLY   I O   1 
ATOM   932   N N   . TRP   A  1 174 ? 6.95108   31.63091  -29.13994 1.000 38.12744  ?  174 TRP   I N   1 
ATOM   933   C CA  . TRP   A  1 174 ? 6.60264   30.23175  -28.91942 1.000 63.70513  ?  174 TRP   I CA  1 
ATOM   934   C C   . TRP   A  1 174 ? 5.15762   30.04659  -28.47398 1.000 72.28795  ?  174 TRP   I C   1 
ATOM   935   O O   . TRP   A  1 174 ? 4.64656   28.92668  -28.54611 1.000 56.46919  ?  174 TRP   I O   1 
ATOM   936   C CB  . TRP   A  1 174 ? 7.56476   29.60674  -27.89818 1.000 41.45949  ?  174 TRP   I CB  1 
ATOM   937   C CG  . TRP   A  1 174 ? 8.93756   29.45365  -28.46613 1.000 71.50962  ?  174 TRP   I CG  1 
ATOM   938   C CD1 . TRP   A  1 174 ? 10.01053  30.26902  -28.24724 1.000 49.46083  ?  174 TRP   I CD1 1 
ATOM   939   C CD2 . TRP   A  1 174 ? 9.37851   28.44394  -29.38590 1.000 58.17340  ?  174 TRP   I CD2 1 
ATOM   940   N NE1 . TRP   A  1 174 ? 11.09450  29.82471  -28.96361 1.000 51.94152  ?  174 TRP   I NE1 1 
ATOM   941   C CE2 . TRP   A  1 174 ? 10.73681  28.70528  -29.66958 1.000 44.00090  ?  174 TRP   I CE2 1 
ATOM   942   C CE3 . TRP   A  1 174 ? 8.76097   27.33606  -29.98360 1.000 46.21871  ?  174 TRP   I CE3 1 
ATOM   943   C CZ2 . TRP   A  1 174 ? 11.49408  27.89952  -30.53061 1.000 36.41227  ?  174 TRP   I CZ2 1 
ATOM   944   C CZ3 . TRP   A  1 174 ? 9.50633   26.54509  -30.84485 1.000 48.25402  ?  174 TRP   I CZ3 1 
ATOM   945   C CH2 . TRP   A  1 174 ? 10.86467  26.83146  -31.10799 1.000 39.40659  ?  174 TRP   I CH2 1 
ATOM   946   N N   . LEU   A  1 175 ? 4.48445   31.11137  -28.03878 1.000 51.75235  ?  175 LEU   I N   1 
ATOM   947   C CA  . LEU   A  1 175 ? 3.07422   31.05779  -27.67247 1.000 46.70591  ?  175 LEU   I CA  1 
ATOM   948   C C   . LEU   A  1 175 ? 2.15265   31.55332  -28.78639 1.000 56.40288  ?  175 LEU   I C   1 
ATOM   949   O O   . LEU   A  1 175 ? 0.93138   31.56042  -28.60881 1.000 65.25211  ?  175 LEU   I O   1 
ATOM   950   C CB  . LEU   A  1 175 ? 2.84622   31.85885  -26.39118 1.000 41.70275  ?  175 LEU   I CB  1 
ATOM   951   C CG  . LEU   A  1 175 ? 3.71313   31.33792  -25.24067 1.000 52.31423  ?  175 LEU   I CG  1 
ATOM   952   C CD1 . LEU   A  1 175 ? 3.40159   32.01717  -23.90371 1.000 42.86026  ?  175 LEU   I CD1 1 
ATOM   953   C CD2 . LEU   A  1 175 ? 3.55376   29.82706  -25.13600 1.000 39.80537  ?  175 LEU   I CD2 1 
ATOM   954   N N   . ASN   A  1 176 ? 2.71725   31.97915  -29.91686 1.000 32.59141  ?  176 ASN   I N   1 
ATOM   955   C CA  . ASN   A  1 176 ? 1.95771   32.23240  -31.13545 1.000 28.18115  ?  176 ASN   I CA  1 
ATOM   956   C C   . ASN   A  1 176 ? 1.25373   30.95557  -31.58940 1.000 44.59013  ?  176 ASN   I C   1 
ATOM   957   O O   . ASN   A  1 176 ? 1.77362   29.84961  -31.40958 1.000 58.47505  ?  176 ASN   I O   1 
ATOM   958   C CB  . ASN   A  1 176 ? 2.92817   32.72333  -32.20161 1.000 55.10389  ?  176 ASN   I CB  1 
ATOM   959   C CG  . ASN   A  1 176 ? 2.24917   33.19700  -33.44237 1.000 53.41507  ?  176 ASN   I CG  1 
ATOM   960   O OD1 . ASN   A  1 176 ? 1.93066   32.40624  -34.33959 1.000 39.60176  ?  176 ASN   I OD1 1 
ATOM   961   N ND2 . ASN   A  1 176 ? 2.07647   34.50994  -33.54049 1.000 40.94311  ?  176 ASN   I ND2 1 
ATOM   962   N N   . GLU   A  1 177 ? 0.05699   31.09896  -32.17212 1.000 51.66685  ?  177 GLU   I N   1 
ATOM   963   C CA  . GLU   A  1 177 ? -0.72434  29.90063  -32.46958 1.000 48.96566  ?  177 GLU   I CA  1 
ATOM   964   C C   . GLU   A  1 177 ? -0.07717  29.06812  -33.56863 1.000 42.73608  ?  177 GLU   I C   1 
ATOM   965   O O   . GLU   A  1 177 ? -0.24950  27.84685  -33.59917 1.000 51.98332  ?  177 GLU   I O   1 
ATOM   966   C CB  . GLU   A  1 177 ? -2.16524  30.25716  -32.84547 1.000 30.71785  ?  177 GLU   I CB  1 
ATOM   967   N N   . ARG   A  1 178 ? 0.68014   29.69346  -34.47094 1.000 41.56880  ?  178 ARG   I N   1 
ATOM   968   C CA  . ARG   A  1 178 ? 1.42215   28.92117  -35.46715 1.000 65.13138  ?  178 ARG   I CA  1 
ATOM   969   C C   . ARG   A  1 178 ? 2.34127   27.90577  -34.78842 1.000 61.30739  ?  178 ARG   I C   1 
ATOM   970   O O   . ARG   A  1 178 ? 2.39605   26.73235  -35.18148 1.000 59.76711  ?  178 ARG   I O   1 
ATOM   971   C CB  . ARG   A  1 178 ? 2.22295   29.87298  -36.36994 1.000 30.31529  ?  178 ARG   I CB  1 
ATOM   972   C CG  . ARG   A  1 178 ? 3.08617   29.24792  -37.45092 1.000 70.04521  ?  178 ARG   I CG  1 
ATOM   973   C CD  . ARG   A  1 178 ? 3.60652   30.32391  -38.39477 1.000 64.95427  ?  178 ARG   I CD  1 
ATOM   974   N NE  . ARG   A  1 178 ? 4.90797   30.01880  -38.98544 1.000 98.70528  ?  178 ARG   I NE  1 
ATOM   975   C CZ  . ARG   A  1 178 ? 5.96304   30.82235  -38.91366 1.000 103.10343 ?  178 ARG   I CZ  1 
ATOM   976   N NH1 . ARG   A  1 178 ? 5.91846   31.96588  -38.25415 1.000 62.02672  ?  178 ARG   I NH1 1 
ATOM   977   N NH2 . ARG   A  1 178 ? 7.08904   30.47612  -39.54148 1.000 99.66108  ?  178 ARG   I NH2 1 
ATOM   978   N N   . ALA   A  1 179 ? 3.04614   28.34054  -33.73705 1.000 50.31191  ?  179 ALA   I N   1 
ATOM   979   C CA  . ALA   A  1 179 ? 3.99134   27.47924  -33.04054 1.000 48.97767  ?  179 ALA   I CA  1 
ATOM   980   C C   . ALA   A  1 179 ? 3.26697   26.52110  -32.10246 1.000 37.79207  ?  179 ALA   I C   1 
ATOM   981   O O   . ALA   A  1 179 ? 3.60007   25.32991  -32.02930 1.000 45.43741  ?  179 ALA   I O   1 
ATOM   982   C CB  . ALA   A  1 179 ? 4.99270   28.33992  -32.26785 1.000 24.81693  ?  179 ALA   I CB  1 
ATOM   983   N N   . LEU   A  1 180 ? 2.28908   27.04493  -31.35520 1.000 45.56473  ?  180 LEU   I N   1 
ATOM   984   C CA  . LEU   A  1 180 ? 1.42746   26.21244  -30.51861 1.000 32.52005  ?  180 LEU   I CA  1 
ATOM   985   C C   . LEU   A  1 180 ? 0.81371   25.06646  -31.32152 1.000 48.89831  ?  180 LEU   I C   1 
ATOM   986   O O   . LEU   A  1 180 ? 0.75332   23.92200  -30.84995 1.000 49.01842  ?  180 LEU   I O   1 
ATOM   987   C CB  . LEU   A  1 180 ? 0.33841   27.08673  -29.89766 1.000 27.85458  ?  180 LEU   I CB  1 
ATOM   988   C CG  . LEU   A  1 180 ? 0.44380   27.44608  -28.42070 1.000 52.67144  ?  180 LEU   I CG  1 
ATOM   989   C CD1 . LEU   A  1 180 ? 1.81299   27.91315  -28.06709 1.000 50.30259  ?  180 LEU   I CD1 1 
ATOM   990   C CD2 . LEU   A  1 180 ? -0.55885  28.51580  -28.07082 1.000 40.34628  ?  180 LEU   I CD2 1 
ATOM   991   N N   . SER   A  1 181 ? 0.36541   25.35414  -32.54660 1.000 47.23214  ?  181 SER   I N   1 
ATOM   992   C CA  . SER   A  1 181 ? -0.20295  24.30963  -33.39105 1.000 51.14352  ?  181 SER   I CA  1 
ATOM   993   C C   . SER   A  1 181 ? 0.84747   23.26202  -33.75830 1.000 38.84226  ?  181 SER   I C   1 
ATOM   994   O O   . SER   A  1 181 ? 0.59796   22.05400  -33.64265 1.000 50.15533  ?  181 SER   I O   1 
ATOM   995   C CB  . SER   A  1 181 ? -0.82282  24.94007  -34.64176 1.000 33.52325  ?  181 SER   I CB  1 
ATOM   996   O OG  . SER   A  1 181 ? -1.03942  23.97320  -35.65941 1.000 101.74394 ?  181 SER   I OG  1 
ATOM   997   N N   . ALA   A  1 182 ? 2.03311   23.70927  -34.20005 1.000 54.55445  ?  182 ALA   I N   1 
ATOM   998   C CA  . ALA   A  1 182 ? 3.08221   22.77802  -34.61422 1.000 76.22329  ?  182 ALA   I CA  1 
ATOM   999   C C   . ALA   A  1 182 ? 3.44782   21.81424  -33.49212 1.000 55.73252  ?  182 ALA   I C   1 
ATOM   1000  O O   . ALA   A  1 182 ? 3.62068   20.61139  -33.73021 1.000 43.55914  ?  182 ALA   I O   1 
ATOM   1001  C CB  . ALA   A  1 182 ? 4.31722   23.55142  -35.08596 1.000 34.74814  ?  182 ALA   I CB  1 
ATOM   1002  N N   . MET   A  1 183 ? 3.52699   22.32047  -32.25562 1.000 38.08251  ?  183 MET   I N   1 
ATOM   1003  C CA  . MET   A  1 183 ? 3.96044   21.53133  -31.10995 1.000 54.20931  ?  183 MET   I CA  1 
ATOM   1004  C C   . MET   A  1 183 ? 2.95591   20.47887  -30.64243 1.000 39.54955  ?  183 MET   I C   1 
ATOM   1005  O O   . MET   A  1 183 ? 3.34367   19.59611  -29.86641 1.000 58.14437  ?  183 MET   I O   1 
ATOM   1006  C CB  . MET   A  1 183 ? 4.30899   22.46811  -29.96100 1.000 38.86913  ?  183 MET   I CB  1 
ATOM   1007  C CG  . MET   A  1 183 ? 5.70453   23.04713  -30.11963 1.000 40.97059  ?  183 MET   I CG  1 
ATOM   1008  S SD  . MET   A  1 183 ? 6.21380   24.08170  -28.75087 1.000 50.18099  ?  183 MET   I SD  1 
ATOM   1009  C CE  . MET   A  1 183 ? 5.38183   25.63352  -29.04117 1.000 46.43468  ?  183 MET   I CE  1 
ATOM   1010  N N   . VAL   A  1 184 ? 1.69670   20.52442  -31.07901 1.000 43.96657  ?  184 VAL   I N   1 
ATOM   1011  C CA  . VAL   A  1 184 ? 0.74423   19.48488  -30.70753 1.000 50.82475  ?  184 VAL   I CA  1 
ATOM   1012  C C   . VAL   A  1 184 ? 0.26035   18.69608  -31.91138 1.000 32.36843  ?  184 VAL   I C   1 
ATOM   1013  O O   . VAL   A  1 184 ? -0.71747  17.96072  -31.80822 1.000 43.29185  ?  184 VAL   I O   1 
ATOM   1014  C CB  . VAL   A  1 184 ? -0.44939  20.05088  -29.91622 1.000 30.23729  ?  184 VAL   I CB  1 
ATOM   1015  C CG1 . VAL   A  1 184 ? 0.03637   20.64877  -28.60451 1.000 35.74890  ?  184 VAL   I CG1 1 
ATOM   1016  C CG2 . VAL   A  1 184 ? -1.21351  21.06772  -30.74864 1.000 31.34747  ?  184 VAL   I CG2 1 
ATOM   1017  N N   . LYS   A  1 185 ? 0.95331   18.81962  -33.04214 1.000 41.74402  ?  185 LYS   I N   1 
ATOM   1018  C CA  . LYS   A  1 185 ? 0.61139   18.08062  -34.25275 1.000 44.61962  ?  185 LYS   I CA  1 
ATOM   1019  C C   . LYS   A  1 185 ? 0.29715   16.60438  -33.98422 1.000 20.34101  ?  185 LYS   I C   1 
ATOM   1020  O O   . LYS   A  1 185 ? -0.67420  16.05738  -34.52441 1.000 78.76917  ?  185 LYS   I O   1 
ATOM   1021  C CB  . LYS   A  1 185 ? 1.76657   18.23695  -35.23947 1.000 33.23902  ?  185 LYS   I CB  1 
ATOM   1022  C CG  . LYS   A  1 185 ? 1.67337   17.39575  -36.46922 1.000 39.44316  ?  185 LYS   I CG  1 
ATOM   1023  C CD  . LYS   A  1 185 ? 2.71773   17.85280  -37.47454 1.000 64.87986  ?  185 LYS   I CD  1 
ATOM   1024  C CE  . LYS   A  1 185 ? 2.36974   17.33309  -38.84877 1.000 65.52431  ?  185 LYS   I CE  1 
ATOM   1025  N NZ  . LYS   A  1 185 ? 3.53337   16.67058  -39.48330 1.000 79.24937  ?  185 LYS   I NZ  1 
ATOM   1026  N N   . HIS   A  1 186 ? 1.09140   15.94551  -33.13803 1.000 52.05718  ?  186 HIS   I N   1 
ATOM   1027  C CA  . HIS   A  1 186 ? 0.95199   14.51125  -32.90919 1.000 34.14640  ?  186 HIS   I CA  1 
ATOM   1028  C C   . HIS   A  1 186 ? 0.19196   14.18048  -31.63082 1.000 53.38486  ?  186 HIS   I C   1 
ATOM   1029  O O   . HIS   A  1 186 ? 0.30795   13.06326  -31.11364 1.000 39.53838  ?  186 HIS   I O   1 
ATOM   1030  C CB  . HIS   A  1 186 ? 2.32253   13.83740  -32.89573 1.000 42.59252  ?  186 HIS   I CB  1 
ATOM   1031  C CG  . HIS   A  1 186 ? 3.08309   14.02190  -34.16404 1.000 68.63610  ?  186 HIS   I CG  1 
ATOM   1032  N ND1 . HIS   A  1 186 ? 2.65152   13.51390  -35.37140 1.000 55.61406  ?  186 HIS   I ND1 1 
ATOM   1033  C CD2 . HIS   A  1 186 ? 4.24668   14.66288  -34.41647 1.000 28.27449  ?  186 HIS   I CD2 1 
ATOM   1034  C CE1 . HIS   A  1 186 ? 3.52385   13.83133  -36.31289 1.000 43.39332  ?  186 HIS   I CE1 1 
ATOM   1035  N NE2 . HIS   A  1 186 ? 4.50107   14.52742  -35.76012 1.000 59.44886  ?  186 HIS   I NE2 1 
ATOM   1036  N N   . TYR   A  1 187 ? -0.59195  15.11513  -31.11005 1.000 42.92137  ?  187 TYR   I N   1 
ATOM   1037  C CA  . TYR   A  1 187 ? -1.32722  14.85432  -29.88266 1.000 50.88075  ?  187 TYR   I CA  1 
ATOM   1038  C C   . TYR   A  1 187 ? -2.82006  14.74862  -30.13218 1.000 86.76819  ?  187 TYR   I C   1 
ATOM   1039  O O   . TYR   A  1 187 ? -3.61737  14.84927  -29.19229 1.000 44.31961  ?  187 TYR   I O   1 
ATOM   1040  C CB  . TYR   A  1 187 ? -0.99610  15.90737  -28.82949 1.000 55.39157  ?  187 TYR   I CB  1 
ATOM   1041  C CG  . TYR   A  1 187 ? 0.41222   15.70461  -28.34422 1.000 39.39889  ?  187 TYR   I CG  1 
ATOM   1042  C CD1 . TYR   A  1 187 ? 0.68939   14.82527  -27.30247 1.000 47.82349  ?  187 TYR   I CD1 1 
ATOM   1043  C CD2 . TYR   A  1 187 ? 1.47719   16.33213  -28.97945 1.000 54.12540  ?  187 TYR   I CD2 1 
ATOM   1044  C CE1 . TYR   A  1 187 ? 1.98969   14.61022  -26.86432 1.000 43.73640  ?  187 TYR   I CE1 1 
ATOM   1045  C CE2 . TYR   A  1 187 ? 2.77565   16.12797  -28.56436 1.000 26.28232  ?  187 TYR   I CE2 1 
ATOM   1046  C CZ  . TYR   A  1 187 ? 3.02522   15.26880  -27.49929 1.000 53.66205  ?  187 TYR   I CZ  1 
ATOM   1047  O OH  . TYR   A  1 187 ? 4.31536   15.08144  -27.08556 1.000 47.05434  ?  187 TYR   I OH  1 
ATOM   1048  N N   . ASN   A  1 188 ? -3.20745  14.52920  -31.38705 1.000 38.58495  ?  188 ASN   I N   1 
ATOM   1049  C CA  . ASN   A  1 188 ? -4.52241  14.00403  -31.69639 1.000 88.29384  ?  188 ASN   I CA  1 
ATOM   1050  C C   . ASN   A  1 188 ? -5.61833  14.99356  -31.29246 1.000 37.55375  ?  188 ASN   I C   1 
ATOM   1051  O O   . ASN   A  1 188 ? -6.55148  14.66297  -30.56240 1.000 71.03709  ?  188 ASN   I O   1 
ATOM   1052  C CB  . ASN   A  1 188 ? -4.68574  12.65061  -31.00539 1.000 49.03524  ?  188 ASN   I CB  1 
ATOM   1053  C CG  . ASN   A  1 188 ? -5.91237  11.91459  -31.44531 1.000 88.34195  ?  188 ASN   I CG  1 
ATOM   1054  O OD1 . ASN   A  1 188 ? -6.99090  12.09096  -30.88835 1.000 116.19141 ?  188 ASN   I OD1 1 
ATOM   1055  N ND2 . ASN   A  1 188 ? -5.75673  11.07353  -32.44532 1.000 101.18253 ?  188 ASN   I ND2 1 
ATOM   1056  N N   . GLY   A  1 189 ? -5.47318  16.24200  -31.73399 1.000 61.76325  ?  189 GLY   I N   1 
ATOM   1057  C CA  . GLY   A  1 189 ? -6.47497  17.25395  -31.47254 1.000 28.68003  ?  189 GLY   I CA  1 
ATOM   1058  C C   . GLY   A  1 189 ? -6.40925  17.94856  -30.12185 1.000 32.84529  ?  189 GLY   I C   1 
ATOM   1059  O O   . GLY   A  1 189 ? -6.99042  19.03303  -29.97724 1.000 65.74156  ?  189 GLY   I O   1 
ATOM   1060  N N   . ARG   A  1 190 ? -5.73269  17.37303  -29.12279 1.000 42.09445  ?  190 ARG   I N   1 
ATOM   1061  C CA  . ARG   A  1 190 ? -5.53687  18.08095  -27.86041 1.000 30.25599  ?  190 ARG   I CA  1 
ATOM   1062  C C   . ARG   A  1 190 ? -4.64766  19.31986  -28.04530 1.000 37.37133  ?  190 ARG   I C   1 
ATOM   1063  O O   . ARG   A  1 190 ? -3.76530  19.37736  -28.91435 1.000 48.05791  ?  190 ARG   I O   1 
ATOM   1064  C CB  . ARG   A  1 190 ? -4.93199  17.15373  -26.80798 1.000 37.46581  ?  190 ARG   I CB  1 
ATOM   1065  C CG  . ARG   A  1 190 ? -5.64977  15.83043  -26.63976 1.000 32.12197  ?  190 ARG   I CG  1 
ATOM   1066  C CD  . ARG   A  1 190 ? -6.35003  15.74585  -25.28683 1.000 22.62797  ?  190 ARG   I CD  1 
ATOM   1067  N NE  . ARG   A  1 190 ? -5.42966  15.66835  -24.15597 1.000 37.28459  ?  190 ARG   I NE  1 
ATOM   1068  C CZ  . ARG   A  1 190 ? -5.73678  16.05018  -22.92401 1.000 54.26487  ?  190 ARG   I CZ  1 
ATOM   1069  N NH1 . ARG   A  1 190 ? -6.91469  16.57989  -22.64033 1.000 50.52153  ?  190 ARG   I NH1 1 
ATOM   1070  N NH2 . ARG   A  1 190 ? -4.83798  15.90779  -21.95449 1.000 39.91912  ?  190 ARG   I NH2 1 
ATOM   1071  N N   . ALA   A  1 191 ? -4.89320  20.31810  -27.20930 1.000 42.07310  ?  191 ALA   I N   1 
ATOM   1072  C CA  . ALA   A  1 191 ? -4.23571  21.61037  -27.31443 1.000 29.86839  ?  191 ALA   I CA  1 
ATOM   1073  C C   . ALA   A  1 191 ? -3.01870  21.67151  -26.39715 1.000 92.90565  ?  191 ALA   I C   1 
ATOM   1074  O O   . ALA   A  1 191 ? -2.87637  20.87758  -25.45981 1.000 31.12364  ?  191 ALA   I O   1 
ATOM   1075  C CB  . ALA   A  1 191 ? -5.20471  22.73663  -26.94964 1.000 42.18495  ?  191 ALA   I CB  1 
ATOM   1076  N N   . PHE   A  1 192 ? -2.16218  22.66735  -26.65536 1.000 31.82230  ?  192 PHE   I N   1 
ATOM   1077  C CA  . PHE   A  1 192 ? -0.87599  22.76557  -25.96783 1.000 35.69503  ?  192 PHE   I CA  1 
ATOM   1078  C C   . PHE   A  1 192 ? -1.02990  22.72959  -24.44710 1.000 59.54127  ?  192 PHE   I C   1 
ATOM   1079  O O   . PHE   A  1 192 ? -0.31971  21.98368  -23.75696 1.000 49.13102  ?  192 PHE   I O   1 
ATOM   1080  C CB  . PHE   A  1 192 ? -0.15136  24.03584  -26.42110 1.000 37.23336  ?  192 PHE   I CB  1 
ATOM   1081  C CG  . PHE   A  1 192 ? 1.23421   24.18432  -25.85413 1.000 44.69356  ?  192 PHE   I CG  1 
ATOM   1082  C CD1 . PHE   A  1 192 ? 1.42755   24.66370  -24.56390 1.000 53.83989  ?  192 PHE   I CD1 1 
ATOM   1083  C CD2 . PHE   A  1 192 ? 2.34645   23.85138  -26.61331 1.000 52.78888  ?  192 PHE   I CD2 1 
ATOM   1084  C CE1 . PHE   A  1 192 ? 2.69797   24.80167  -24.03392 1.000 34.43261  ?  192 PHE   I CE1 1 
ATOM   1085  C CE2 . PHE   A  1 192 ? 3.62771   23.98920  -26.09027 1.000 58.89075  ?  192 PHE   I CE2 1 
ATOM   1086  C CZ  . PHE   A  1 192 ? 3.79909   24.47044  -24.79838 1.000 42.33484  ?  192 PHE   I CZ  1 
ATOM   1087  N N   . ASP   A  1 193 ? -1.94819  23.53461  -23.90579 1.000 51.59335  ?  193 ASP   I N   1 
ATOM   1088  C CA  . ASP   A  1 193 ? -2.12379  23.63145  -22.45751 1.000 31.69052  ?  193 ASP   I CA  1 
ATOM   1089  C C   . ASP   A  1 193 ? -2.84925  22.42534  -21.85624 1.000 58.18393  ?  193 ASP   I C   1 
ATOM   1090  O O   . ASP   A  1 193 ? -2.80688  22.23324  -20.63388 1.000 19.07061  ?  193 ASP   I O   1 
ATOM   1091  C CB  . ASP   A  1 193 ? -2.86463  24.92748  -22.11652 1.000 44.58099  ?  193 ASP   I CB  1 
ATOM   1092  C CG  . ASP   A  1 193 ? -4.24456  24.98447  -22.73946 1.000 87.46227  ?  193 ASP   I CG  1 
ATOM   1093  O OD1 . ASP   A  1 193 ? -4.33874  25.08560  -23.98137 1.000 48.17886  ?  193 ASP   I OD1 1 
ATOM   1094  O OD2 . ASP   A  1 193 ? -5.23405  24.88830  -21.98222 1.000 46.67684  ?  193 ASP   I OD2 1 
ATOM   1095  N N   . GLU   A  1 194 ? -3.51189  21.60862  -22.67481 1.000 23.30863  ?  194 GLU   I N   1 
ATOM   1096  C CA  . GLU   A  1 194 ? -3.98342  20.30782  -22.20859 1.000 50.27981  ?  194 GLU   I CA  1 
ATOM   1097  C C   . GLU   A  1 194 ? -2.83333  19.31189  -22.11580 1.000 54.65677  ?  194 GLU   I C   1 
ATOM   1098  O O   . GLU   A  1 194 ? -2.68243  18.62182  -21.09898 1.000 43.15041  ?  194 GLU   I O   1 
ATOM   1099  C CB  . GLU   A  1 194 ? -5.05780  19.76712  -23.14900 1.000 42.04262  ?  194 GLU   I CB  1 
ATOM   1100  C CG  . GLU   A  1 194 ? -6.27770  20.67039  -23.31504 1.000 27.81937  ?  194 GLU   I CG  1 
ATOM   1101  C CD  . GLU   A  1 194 ? -7.28428  20.09336  -24.30629 1.000 85.39345  ?  194 GLU   I CD  1 
ATOM   1102  O OE1 . GLU   A  1 194 ? -6.99436  20.13330  -25.52184 1.000 60.00436  ?  194 GLU   I OE1 1 
ATOM   1103  O OE2 . GLU   A  1 194 ? -8.34616  19.57888  -23.87620 1.000 57.55687  ?  194 GLU   I OE2 1 
ATOM   1104  N N   . VAL   A  1 195 ? -2.00631  19.25039  -23.17222 1.000 53.63999  ?  195 VAL   I N   1 
ATOM   1105  C CA  . VAL   A  1 195 ? -0.93297  18.26048  -23.27599 1.000 21.43992  ?  195 VAL   I CA  1 
ATOM   1106  C C   . VAL   A  1 195 ? 0.17970   18.54163  -22.26524 1.000 82.86592  ?  195 VAL   I C   1 
ATOM   1107  O O   . VAL   A  1 195 ? 0.61450   17.64970  -21.52615 1.000 34.65543  ?  195 VAL   I O   1 
ATOM   1108  C CB  . VAL   A  1 195 ? -0.38063  18.23615  -24.71015 1.000 56.67524  ?  195 VAL   I CB  1 
ATOM   1109  C CG1 . VAL   A  1 195 ? 0.81126   17.29144  -24.80373 1.000 26.34639  ?  195 VAL   I CG1 1 
ATOM   1110  C CG2 . VAL   A  1 195 ? -1.47548  17.85478  -25.70100 1.000 31.34331  ?  195 VAL   I CG2 1 
ATOM   1111  N N   . PHE   A  1 196 ? 0.67680   19.76988  -22.23171 1.000 25.64777  ?  196 PHE   I N   1 
ATOM   1112  C CA  . PHE   A  1 196 ? 1.81853   20.10027  -21.39872 1.000 57.56803  ?  196 PHE   I CA  1 
ATOM   1113  C C   . PHE   A  1 196 ? 1.36723   20.87138  -20.16415 1.000 38.06260  ?  196 PHE   I C   1 
ATOM   1114  O O   . PHE   A  1 196 ? 0.36689   21.58970  -20.19215 1.000 40.32350  ?  196 PHE   I O   1 
ATOM   1115  C CB  . PHE   A  1 196 ? 2.84363   20.91061  -22.19711 1.000 30.30991  ?  196 PHE   I CB  1 
ATOM   1116  C CG  . PHE   A  1 196 ? 3.28657   20.23432  -23.45182 1.000 47.76601  ?  196 PHE   I CG  1 
ATOM   1117  C CD1 . PHE   A  1 196 ? 4.02343   19.06027  -23.39661 1.000 31.47057  ?  196 PHE   I CD1 1 
ATOM   1118  C CD2 . PHE   A  1 196 ? 2.94968   20.75243  -24.68977 1.000 24.88390  ?  196 PHE   I CD2 1 
ATOM   1119  C CE1 . PHE   A  1 196 ? 4.42322   18.41709  -24.56746 1.000 35.48625  ?  196 PHE   I CE1 1 
ATOM   1120  C CE2 . PHE   A  1 196 ? 3.35360   20.12014  -25.86617 1.000 43.06893  ?  196 PHE   I CE2 1 
ATOM   1121  C CZ  . PHE   A  1 196 ? 4.09384   18.95341  -25.80574 1.000 34.45731  ?  196 PHE   I CZ  1 
ATOM   1122  N N   . LEU   A  1 197 ? 2.11968   20.70859  -19.07730 1.000 44.07986  ?  197 LEU   I N   1 
ATOM   1123  C CA  . LEU   A  1 197 ? 1.83063   21.35317  -17.79736 1.000 46.90632  ?  197 LEU   I CA  1 
ATOM   1124  C C   . LEU   A  1 197 ? 2.24125   22.81749  -17.86964 1.000 65.50016  ?  197 LEU   I C   1 
ATOM   1125  O O   . LEU   A  1 197 ? 3.43283   23.13968  -17.86252 1.000 40.89917  ?  197 LEU   I O   1 
ATOM   1126  C CB  . LEU   A  1 197 ? 2.58406   20.64161  -16.68055 1.000 44.43933  ?  197 LEU   I CB  1 
ATOM   1127  C CG  . LEU   A  1 197 ? 2.23967   20.82338  -15.20928 1.000 41.13541  ?  197 LEU   I CG  1 
ATOM   1128  C CD1 . LEU   A  1 197 ? 3.05993   19.79812  -14.49061 1.000 49.38029  ?  197 LEU   I CD1 1 
ATOM   1129  C CD2 . LEU   A  1 197 ? 2.60546   22.18835  -14.68144 1.000 88.33607  ?  197 LEU   I CD2 1 
ATOM   1130  N N   . CYS   A  1 198 ? 1.26438   23.71005  -17.90638 1.000 51.31349  ?  198 CYS   I N   1 
ATOM   1131  C CA  . CYS   A  1 198 ? 1.54798   25.12961  -17.94234 1.000 50.48752  ?  198 CYS   I CA  1 
ATOM   1132  C C   . CYS   A  1 198 ? 0.33231   25.85268  -17.38496 1.000 54.11831  ?  198 CYS   I C   1 
ATOM   1133  O O   . CYS   A  1 198 ? -0.57950  25.23115  -16.82872 1.000 61.21520  ?  198 CYS   I O   1 
ATOM   1134  C CB  . CYS   A  1 198 ? 1.87751   25.57073  -19.37186 1.000 43.94168  ?  198 CYS   I CB  1 
ATOM   1135  S SG  . CYS   A  1 198 ? 0.56624   25.10800  -20.56408 1.000 52.67790  ?  198 CYS   I SG  1 
ATOM   1136  N N   . ASP   A  1 199 ? 0.31564   27.17193  -17.55691 1.000 54.31504  ?  199 ASP   I N   1 
ATOM   1137  C CA  . ASP   A  1 199 ? -0.81033  28.02188  -17.18241 1.000 42.78925  ?  199 ASP   I CA  1 
ATOM   1138  C C   . ASP   A  1 199 ? -1.12293  28.93009  -18.36956 1.000 77.40548  ?  199 ASP   I C   1 
ATOM   1139  O O   . ASP   A  1 199 ? -0.40915  29.91353  -18.60113 1.000 42.54466  ?  199 ASP   I O   1 
ATOM   1140  C CB  . ASP   A  1 199 ? -0.46882  28.83083  -15.93020 1.000 44.59408  ?  199 ASP   I CB  1 
ATOM   1141  C CG  . ASP   A  1 199 ? -1.60899  29.73117  -15.46603 1.000 145.94286 ?  199 ASP   I CG  1 
ATOM   1142  O OD1 . ASP   A  1 199 ? -2.63729  29.87114  -16.18242 1.000 47.43024  ?  199 ASP   I OD1 1 
ATOM   1143  O OD2 . ASP   A  1 199 ? -1.45008  30.29515  -14.35804 1.000 55.13027  ?  199 ASP   I OD2 1 
ATOM   1144  N N   . LYS   A  1 200 ? -2.18836  28.61395  -19.12309 1.000 44.91718  ?  200 LYS   I N   1 
ATOM   1145  C CA  . LYS   A  1 200 ? -2.47621  29.38276  -20.33563 1.000 70.37796  ?  200 LYS   I CA  1 
ATOM   1146  C C   . LYS   A  1 200 ? -2.88523  30.81848  -20.03764 1.000 67.12225  ?  200 LYS   I C   1 
ATOM   1147  O O   . LYS   A  1 200 ? -2.87878  31.64264  -20.95545 1.000 58.83902  ?  200 LYS   I O   1 
ATOM   1148  C CB  . LYS   A  1 200 ? -3.56522  28.70406  -21.17817 1.000 44.73249  ?  200 LYS   I CB  1 
ATOM   1149  C CG  . LYS   A  1 200 ? -4.97554  28.85727  -20.64351 1.000 67.52202  ?  200 LYS   I CG  1 
ATOM   1150  C CD  . LYS   A  1 200 ? -6.00051  28.10996  -21.50370 1.000 88.03196  ?  200 LYS   I CD  1 
ATOM   1151  C CE  . LYS   A  1 200 ? -6.17013  28.72105  -22.89802 1.000 71.31033  ?  200 LYS   I CE  1 
ATOM   1152  N NZ  . LYS   A  1 200 ? -7.43502  28.24337  -23.55524 1.000 65.89011  ?  200 LYS   I NZ  1 
ATOM   1153  N N   . ASN   A  1 201 ? -3.21134  31.13986  -18.78639 1.000 54.43567  ?  201 ASN   I N   1 
ATOM   1154  C CA  . ASN   A  1 201 ? -3.61514  32.48060  -18.39147 1.000 77.59737  ?  201 ASN   I CA  1 
ATOM   1155  C C   . ASN   A  1 201 ? -2.48437  33.28317  -17.78156 1.000 53.34233  ?  201 ASN   I C   1 
ATOM   1156  O O   . ASN   A  1 201 ? -2.65634  34.47655  -17.51994 1.000 85.38298  ?  201 ASN   I O   1 
ATOM   1157  C CB  . ASN   A  1 201 ? -4.77322  32.39403  -17.40565 1.000 51.59524  ?  201 ASN   I CB  1 
ATOM   1158  C CG  . ASN   A  1 201 ? -5.94862  31.68053  -17.99478 1.000 89.05899  ?  201 ASN   I CG  1 
ATOM   1159  O OD1 . ASN   A  1 201 ? -6.30540  31.90990  -19.16310 1.000 42.29157  ?  201 ASN   I OD1 1 
ATOM   1160  N ND2 . ASN   A  1 201 ? -6.53720  30.77438  -17.22219 1.000 57.17349  ?  201 ASN   I ND2 1 
ATOM   1161  N N   . ALA   A  1 202 ? -1.40137  32.69524  -17.56191 1.000 105.81398 ?  202 ALA   I N   1 
ATOM   1162  C CA  . ALA   A  1 202 ? -0.28219  33.40463  -16.97745 1.000 58.30965  ?  202 ALA   I CA  1 
ATOM   1163  C C   . ALA   A  1 202 ? 0.59430   33.99889  -18.07244 1.000 51.54052  ?  202 ALA   I C   1 
ATOM   1164  O O   . ALA   A  1 202 ? 0.57091   33.53590  -19.22076 1.000 63.29466  ?  202 ALA   I O   1 
ATOM   1165  C CB  . ALA   A  1 202 ? 0.54050   32.46615  -16.10713 1.000 35.67798  ?  202 ALA   I CB  1 
ATOM   1166  N N   . PRO   A  1 203 ? 1.33640   35.05789  -17.76308 1.000 85.53159  ?  203 PRO   I N   1 
ATOM   1167  C CA  . PRO   A  1 203 ? 2.35995   35.52104  -18.70657 1.000 80.35184  ?  203 PRO   I CA  1 
ATOM   1168  C C   . PRO   A  1 203 ? 3.42278   34.44707  -18.88460 1.000 70.17688  ?  203 PRO   I C   1 
ATOM   1169  O O   . PRO   A  1 203 ? 3.81738   33.76490  -17.92690 1.000 50.43369  ?  203 PRO   I O   1 
ATOM   1170  C CB  . PRO   A  1 203 ? 2.92484   36.78926  -18.04932 1.000 57.63474  ?  203 PRO   I CB  1 
ATOM   1171  C CG  . PRO   A  1 203 ? 2.51471   36.70993  -16.59975 1.000 48.34324  ?  203 PRO   I CG  1 
ATOM   1172  C CD  . PRO   A  1 203 ? 1.24300   35.90100  -16.55781 1.000 36.47657  ?  203 PRO   I CD  1 
ATOM   1173  N N   . TYR   A  1 204 ? 3.85441   34.27927  -20.13868 1.000 53.73939  ?  204 TYR   I N   1 
ATOM   1174  C CA  . TYR   A  1 204 ? 4.81910   33.25732  -20.53234 1.000 64.80902  ?  204 TYR   I CA  1 
ATOM   1175  C C   . TYR   A  1 204 ? 4.29932   31.85478  -20.28609 1.000 58.51789  ?  204 TYR   I C   1 
ATOM   1176  O O   . TYR   A  1 204 ? 5.08900   30.93824  -20.04820 1.000 62.87120  ?  204 TYR   I O   1 
ATOM   1177  C CB  . TYR   A  1 204 ? 6.15484   33.44723  -19.80337 1.000 52.21533  ?  204 TYR   I CB  1 
ATOM   1178  C CG  . TYR   A  1 204 ? 6.57689   34.89415  -19.75404 1.000 56.49091  ?  204 TYR   I CG  1 
ATOM   1179  C CD1 . TYR   A  1 204 ? 6.75917   35.61674  -20.93610 1.000 51.25234  ?  204 TYR   I CD1 1 
ATOM   1180  C CD2 . TYR   A  1 204 ? 6.78377   35.54524  -18.53601 1.000 47.43978  ?  204 TYR   I CD2 1 
ATOM   1181  C CE1 . TYR   A  1 204 ? 7.13438   36.95145  -20.91648 1.000 33.96772  ?  204 TYR   I CE1 1 
ATOM   1182  C CE2 . TYR   A  1 204 ? 7.16507   36.87984  -18.50036 1.000 44.48265  ?  204 TYR   I CE2 1 
ATOM   1183  C CZ  . TYR   A  1 204 ? 7.32853   37.57659  -19.69800 1.000 57.69591  ?  204 TYR   I CZ  1 
ATOM   1184  O OH  . TYR   A  1 204 ? 7.70940   38.89692  -19.69686 1.000 59.70583  ?  204 TYR   I OH  1 
ATOM   1185  N N   . TYR   A  1 205 ? 2.97898   31.68062  -20.29316 1.000 39.73132  ?  205 TYR   I N   1 
ATOM   1186  C CA  . TYR   A  1 205 ? 2.34143   30.40622  -19.97730 1.000 37.69132  ?  205 TYR   I CA  1 
ATOM   1187  C C   . TYR   A  1 205 ? 2.84572   29.81011  -18.65676 1.000 45.11435  ?  205 TYR   I C   1 
ATOM   1188  O O   . TYR   A  1 205 ? 2.75302   28.59381  -18.43396 1.000 43.09785  ?  205 TYR   I O   1 
ATOM   1189  C CB  . TYR   A  1 205 ? 2.52813   29.40151  -21.11329 1.000 44.80978  ?  205 TYR   I CB  1 
ATOM   1190  C CG  . TYR   A  1 205 ? 1.37798   29.30783  -22.07602 1.000 58.51653  ?  205 TYR   I CG  1 
ATOM   1191  C CD1 . TYR   A  1 205 ? 0.60785   30.41523  -22.39669 1.000 50.76754  ?  205 TYR   I CD1 1 
ATOM   1192  C CD2 . TYR   A  1 205 ? 1.05157   28.09074  -22.66247 1.000 46.02010  ?  205 TYR   I CD2 1 
ATOM   1193  C CE1 . TYR   A  1 205 ? -0.46283  30.30591  -23.30445 1.000 35.64519  ?  205 TYR   I CE1 1 
ATOM   1194  C CE2 . TYR   A  1 205 ? -0.00339  27.97378  -23.55780 1.000 59.64560  ?  205 TYR   I CE2 1 
ATOM   1195  C CZ  . TYR   A  1 205 ? -0.75517  29.08008  -23.87442 1.000 79.53943  ?  205 TYR   I CZ  1 
ATOM   1196  O OH  . TYR   A  1 205 ? -1.78980  28.93631  -24.76106 1.000 50.12722  ?  205 TYR   I OH  1 
ATOM   1197  N N   . GLY   A  1 206 ? 3.38834   30.63766  -17.76789 1.000 34.95392  ?  206 GLY   I N   1 
ATOM   1198  C CA  . GLY   A  1 206 ? 3.83696   30.16646  -16.47927 1.000 33.84134  ?  206 GLY   I CA  1 
ATOM   1199  C C   . GLY   A  1 206 ? 5.25384   29.63579  -16.43474 1.000 47.63026  ?  206 GLY   I C   1 
ATOM   1200  O O   . GLY   A  1 206 ? 5.75673   29.36106  -15.33927 1.000 39.64634  ?  206 GLY   I O   1 
ATOM   1201  N N   . PHE   A  1 207 ? 5.91636   29.47914  -17.57642 1.000 43.05255  ?  207 PHE   I N   1 
ATOM   1202  C CA  . PHE   A  1 207 ? 7.29695   29.01562  -17.57078 1.000 55.11185  ?  207 PHE   I CA  1 
ATOM   1203  C C   . PHE   A  1 207 ? 8.21604   30.11845  -17.05901 1.000 50.57586  ?  207 PHE   I C   1 
ATOM   1204  O O   . PHE   A  1 207 ? 8.01153   31.29844  -17.35601 1.000 60.61757  ?  207 PHE   I O   1 
ATOM   1205  C CB  . PHE   A  1 207 ? 7.71127   28.58890  -18.97686 1.000 42.44758  ?  207 PHE   I CB  1 
ATOM   1206  C CG  . PHE   A  1 207 ? 6.88798   27.46799  -19.54313 1.000 58.09565  ?  207 PHE   I CG  1 
ATOM   1207  C CD1 . PHE   A  1 207 ? 7.07100   26.16672  -19.09616 1.000 31.87331  ?  207 PHE   I CD1 1 
ATOM   1208  C CD2 . PHE   A  1 207 ? 5.94635   27.70732  -20.54140 1.000 36.24969  ?  207 PHE   I CD2 1 
ATOM   1209  C CE1 . PHE   A  1 207 ? 6.32493   25.12453  -19.62846 1.000 52.17998  ?  207 PHE   I CE1 1 
ATOM   1210  C CE2 . PHE   A  1 207 ? 5.19444   26.66462  -21.08391 1.000 39.90528  ?  207 PHE   I CE2 1 
ATOM   1211  C CZ  . PHE   A  1 207 ? 5.38498   25.37504  -20.62465 1.000 56.86219  ?  207 PHE   I CZ  1 
ATOM   1212  N N   . ASN   A  1 208 ? 9.23429   29.73876  -16.28131 1.000 44.58663  ?  208 ASN   I N   1 
ATOM   1213  C CA  . ASN   A  1 208 ? 10.12711  30.72724  -15.68074 1.000 67.10000  ?  208 ASN   I CA  1 
ATOM   1214  C C   . ASN   A  1 208 ? 11.40297  30.98184  -16.47515 1.000 36.72448  ?  208 ASN   I C   1 
ATOM   1215  O O   . ASN   A  1 208 ? 12.24324  31.77495  -16.02663 1.000 94.89889  ?  208 ASN   I O   1 
ATOM   1216  C CB  . ASN   A  1 208 ? 10.49205  30.33831  -14.23995 1.000 37.17450  ?  208 ASN   I CB  1 
ATOM   1217  C CG  . ASN   A  1 208 ? 10.80899  28.88405  -14.08210 1.000 93.64369  ?  208 ASN   I CG  1 
ATOM   1218  O OD1 . ASN   A  1 208 ? 11.76611  28.36692  -14.67402 1.000 148.69286 ?  208 ASN   I OD1 1 
ATOM   1219  N ND2 . ASN   A  1 208 ? 10.02578  28.20929  -13.24616 1.000 70.61923  ?  208 ASN   I ND2 1 
ATOM   1220  N N   . SER   A  1 209 ? 11.55601  30.36251  -17.64377 1.000 59.45405  ?  209 SER   I N   1 
ATOM   1221  C CA  . SER   A  1 209 ? 12.71600  30.55201  -18.51170 1.000 42.91809  ?  209 SER   I CA  1 
ATOM   1222  C C   . SER   A  1 209 ? 12.44798  29.79542  -19.79454 1.000 65.06546  ?  209 SER   I C   1 
ATOM   1223  O O   . SER   A  1 209 ? 11.50202  29.00604  -19.88389 1.000 40.29839  ?  209 SER   I O   1 
ATOM   1224  C CB  . SER   A  1 209 ? 14.01889  30.03086  -17.90444 1.000 53.91065  ?  209 SER   I CB  1 
ATOM   1225  O OG  . SER   A  1 209 ? 13.98310  28.61422  -17.85334 1.000 33.23454  ?  209 SER   I OG  1 
ATOM   1226  N N   . TYR   A  1 210 ? 13.32241  30.01368  -20.77838 1.000 45.93831  ?  210 TYR   I N   1 
ATOM   1227  C CA  . TYR   A  1 210 ? 13.17708  29.27740  -22.02534 1.000 34.05163  ?  210 TYR   I CA  1 
ATOM   1228  C C   . TYR   A  1 210 ? 13.42333  27.78814  -21.80986 1.000 47.05997  ?  210 TYR   I C   1 
ATOM   1229  O O   . TYR   A  1 210 ? 12.65517  26.94740  -22.29417 1.000 40.00625  ?  210 TYR   I O   1 
ATOM   1230  C CB  . TYR   A  1 210 ? 14.11940  29.84193  -23.08750 1.000 23.45633  ?  210 TYR   I CB  1 
ATOM   1231  C CG  . TYR   A  1 210 ? 14.11786  29.01019  -24.33761 1.000 56.52961  ?  210 TYR   I CG  1 
ATOM   1232  C CD1 . TYR   A  1 210 ? 13.07812  29.11289  -25.25205 1.000 33.55219  ?  210 TYR   I CD1 1 
ATOM   1233  C CD2 . TYR   A  1 210 ? 15.13018  28.09302  -24.58854 1.000 48.96575  ?  210 TYR   I CD2 1 
ATOM   1234  C CE1 . TYR   A  1 210 ? 13.04086  28.33375  -26.39808 1.000 37.17498  ?  210 TYR   I CE1 1 
ATOM   1235  C CE2 . TYR   A  1 210 ? 15.10745  27.30909  -25.73056 1.000 50.73541  ?  210 TYR   I CE2 1 
ATOM   1236  C CZ  . TYR   A  1 210 ? 14.05989  27.43946  -26.62909 1.000 59.73061  ?  210 TYR   I CZ  1 
ATOM   1237  O OH  . TYR   A  1 210 ? 14.03043  26.67875  -27.76091 1.000 41.50676  ?  210 TYR   I OH  1 
ATOM   1238  N N   . ASP   A  1 211 ? 14.48060  27.44967  -21.06936 1.000 39.08304  ?  211 ASP   I N   1 
ATOM   1239  C CA  . ASP   A  1 211 ? 14.78147  26.05078  -20.78551 1.000 33.80680  ?  211 ASP   I CA  1 
ATOM   1240  C C   . ASP   A  1 211 ? 13.61149  25.36105  -20.10424 1.000 55.19550  ?  211 ASP   I C   1 
ATOM   1241  O O   . ASP   A  1 211 ? 13.33165  24.18149  -20.37300 1.000 36.07780  ?  211 ASP   I O   1 
ATOM   1242  C CB  . ASP   A  1 211 ? 16.03284  25.93951  -19.90985 1.000 36.94642  ?  211 ASP   I CB  1 
ATOM   1243  C CG  . ASP   A  1 211 ? 16.40010  24.49527  -19.61487 1.000 37.48972  ?  211 ASP   I CG  1 
ATOM   1244  O OD1 . ASP   A  1 211 ? 16.78353  23.77147  -20.57027 1.000 42.24106  ?  211 ASP   I OD1 1 
ATOM   1245  O OD2 . ASP   A  1 211 ? 16.29619  24.08036  -18.43653 1.000 60.15624  ?  211 ASP   I OD2 1 
ATOM   1246  N N   . ASP   A  1 212 ? 12.93507  26.07580  -19.19751 1.000 41.87509  ?  212 ASP   I N   1 
ATOM   1247  C CA  . ASP   A  1 212 ? 11.73713  25.53330  -18.56258 1.000 51.39297  ?  212 ASP   I CA  1 
ATOM   1248  C C   . ASP   A  1 212 ? 10.68332  25.16731  -19.60904 1.000 43.65674  ?  212 ASP   I C   1 
ATOM   1249  O O   . ASP   A  1 212 ? 10.06943  24.09202  -19.54642 1.000 44.34369  ?  212 ASP   I O   1 
ATOM   1250  C CB  . ASP   A  1 212 ? 11.19762  26.55317  -17.55594 1.000 52.87155  ?  212 ASP   I CB  1 
ATOM   1251  C CG  . ASP   A  1 212 ? 10.08372  25.99917  -16.68113 1.000 60.99214  ?  212 ASP   I CG  1 
ATOM   1252  O OD1 . ASP   A  1 212 ? 10.03258  24.76472  -16.48890 1.000 75.99240  ?  212 ASP   I OD1 1 
ATOM   1253  O OD2 . ASP   A  1 212 ? 9.24994   26.80974  -16.20484 1.000 61.86481  ?  212 ASP   I OD2 1 
ATOM   1254  N N   . PHE   A  1 213 ? 10.48416  26.03799  -20.59656 1.000 30.36891  ?  213 PHE   I N   1 
ATOM   1255  C CA  . PHE   A  1 213 ? 9.53471   25.74954  -21.66548 1.000 27.63913  ?  213 PHE   I CA  1 
ATOM   1256  C C   . PHE   A  1 213 ? 10.02279  24.60167  -22.54330 1.000 64.54808  ?  213 PHE   I C   1 
ATOM   1257  O O   . PHE   A  1 213 ? 9.23918   23.71126  -22.91771 1.000 39.04527  ?  213 PHE   I O   1 
ATOM   1258  C CB  . PHE   A  1 213 ? 9.31208   27.01474  -22.50048 1.000 34.31736  ?  213 PHE   I CB  1 
ATOM   1259  C CG  . PHE   A  1 213 ? 8.72920   26.74739  -23.83304 1.000 47.01692  ?  213 PHE   I CG  1 
ATOM   1260  C CD1 . PHE   A  1 213 ? 7.35694   26.55110  -23.97592 1.000 50.49873  ?  213 PHE   I CD1 1 
ATOM   1261  C CD2 . PHE   A  1 213 ? 9.54474   26.67590  -24.95200 1.000 35.22269  ?  213 PHE   I CD2 1 
ATOM   1262  C CE1 . PHE   A  1 213 ? 6.80453   26.29415  -25.22412 1.000 59.97389  ?  213 PHE   I CE1 1 
ATOM   1263  C CE2 . PHE   A  1 213 ? 9.00147   26.42181  -26.19975 1.000 62.91503  ?  213 PHE   I CE2 1 
ATOM   1264  C CZ  . PHE   A  1 213 ? 7.62808   26.22865  -26.33633 1.000 52.36783  ?  213 PHE   I CZ  1 
ATOM   1265  N N   . PHE   A  1 214 ? 11.31473  24.63022  -22.89339 1.000 34.15814  ?  214 PHE   I N   1 
ATOM   1266  C CA  . PHE   A  1 214 ? 11.92112  23.59718  -23.72649 1.000 32.45088  ?  214 PHE   I CA  1 
ATOM   1267  C C   . PHE   A  1 214 ? 11.75653  22.20859  -23.10514 1.000 31.25655  ?  214 PHE   I C   1 
ATOM   1268  O O   . PHE   A  1 214 ? 11.50453  21.22286  -23.81588 1.000 58.87948  ?  214 PHE   I O   1 
ATOM   1269  C CB  . PHE   A  1 214 ? 13.39721  23.94772  -23.93394 1.000 41.18505  ?  214 PHE   I CB  1 
ATOM   1270  C CG  . PHE   A  1 214 ? 14.13293  23.01853  -24.85537 1.000 39.39577  ?  214 PHE   I CG  1 
ATOM   1271  C CD1 . PHE   A  1 214 ? 13.98869  23.12778  -26.22866 1.000 37.93446  ?  214 PHE   I CD1 1 
ATOM   1272  C CD2 . PHE   A  1 214 ? 14.99664  22.05571  -24.35050 1.000 46.82875  ?  214 PHE   I CD2 1 
ATOM   1273  C CE1 . PHE   A  1 214 ? 14.66177  22.28107  -27.08748 1.000 34.37938  ?  214 PHE   I CE1 1 
ATOM   1274  C CE2 . PHE   A  1 214 ? 15.68880  21.20358  -25.20799 1.000 46.21993  ?  214 PHE   I CE2 1 
ATOM   1275  C CZ  . PHE   A  1 214 ? 15.52553  21.31968  -26.58309 1.000 40.14014  ?  214 PHE   I CZ  1 
ATOM   1276  N N   . ASN   A  1 215 ? 11.86682  22.11565  -21.77844 1.000 23.57422  ?  215 ASN   I N   1 
ATOM   1277  C CA  . ASN   A  1 215 ? 11.72986  20.85335  -21.05634 1.000 31.23293  ?  215 ASN   I CA  1 
ATOM   1278  C C   . ASN   A  1 215 ? 10.40363  20.75152  -20.30652 1.000 41.01549  ?  215 ASN   I C   1 
ATOM   1279  O O   . ASN   A  1 215 ? 10.33458  20.19378  -19.20723 1.000 34.75916  ?  215 ASN   I O   1 
ATOM   1280  C CB  . ASN   A  1 215 ? 12.90502  20.65272  -20.10787 1.000 31.08021  ?  215 ASN   I CB  1 
ATOM   1281  C CG  . ASN   A  1 215 ? 14.16395  20.26263  -20.85195 1.000 54.20212  ?  215 ASN   I CG  1 
ATOM   1282  O OD1 . ASN   A  1 215 ? 14.13961  19.40240  -21.74123 1.000 32.86255  ?  215 ASN   I OD1 1 
ATOM   1283  N ND2 . ASN   A  1 215 ? 15.26380  20.91494  -20.52097 1.000 29.59042  ?  215 ASN   I ND2 1 
ATOM   1284  N N   . ARG   A  1 216 ? 9.33812   21.28598  -20.91013 1.000 22.33231  ?  216 ARG   I N   1 
ATOM   1285  C CA  . ARG   A  1 216 ? 8.00879   21.22176  -20.32711 1.000 31.21299  ?  216 ARG   I CA  1 
ATOM   1286  C C   . ARG   A  1 216 ? 7.58930   19.77049  -20.09124 1.000 54.25635  ?  216 ARG   I C   1 
ATOM   1287  O O   . ARG   A  1 216 ? 7.89540   18.87732  -20.88693 1.000 30.44074  ?  216 ARG   I O   1 
ATOM   1288  C CB  . ARG   A  1 216 ? 7.02352   21.92539  -21.25987 1.000 27.49587  ?  216 ARG   I CB  1 
ATOM   1289  C CG  . ARG   A  1 216 ? 6.92223   21.28323  -22.62493 1.000 26.78717  ?  216 ARG   I CG  1 
ATOM   1290  C CD  . ARG   A  1 216 ? 6.16862   22.15564  -23.59666 1.000 37.10119  ?  216 ARG   I CD  1 
ATOM   1291  N NE  . ARG   A  1 216 ? 6.25819   21.63973  -24.95974 1.000 26.04150  ?  216 ARG   I NE  1 
ATOM   1292  C CZ  . ARG   A  1 216 ? 7.29778   21.84472  -25.75815 1.000 50.82062  ?  216 ARG   I CZ  1 
ATOM   1293  N NH1 . ARG   A  1 216 ? 8.33912   22.56566  -25.36507 1.000 29.63377  ?  216 ARG   I NH1 1 
ATOM   1294  N NH2 . ARG   A  1 216 ? 7.29803   21.30797  -26.97472 1.000 34.11813  ?  216 ARG   I NH2 1 
ATOM   1295  N N   . ARG   A  1 217 ? 6.93821   19.49551  -18.96232 1.000 49.86925  ?  217 ARG   I N   1 
ATOM   1296  C CA  . ARG   A  1 217 ? 6.51364   18.11899  -18.70452 1.000 37.40249  ?  217 ARG   I CA  1 
ATOM   1297  C C   . ARG   A  1 217 ? 5.06155   17.90949  -19.16346 1.000 22.79184  ?  217 ARG   I C   1 
ATOM   1298  O O   . ARG   A  1 217 ? 4.33044   18.85259  -19.45248 1.000 37.21947  ?  217 ARG   I O   1 
ATOM   1299  C CB  . ARG   A  1 217 ? 6.66594   17.73609  -17.22521 1.000 23.75203  ?  217 ARG   I CB  1 
ATOM   1300  C CG  . ARG   A  1 217 ? 7.78642   18.42956  -16.43186 1.000 60.86702  ?  217 ARG   I CG  1 
ATOM   1301  C CD  . ARG   A  1 217 ? 7.57789   18.25223  -14.90181 1.000 46.22262  ?  217 ARG   I CD  1 
ATOM   1302  N NE  . ARG   A  1 217 ? 8.21959   19.30499  -14.12165 1.000 80.42002  ?  217 ARG   I NE  1 
ATOM   1303  C CZ  . ARG   A  1 217 ? 7.78684   20.55795  -14.01520 1.000 82.14424  ?  217 ARG   I CZ  1 
ATOM   1304  N NH1 . ARG   A  1 217 ? 6.64000   20.94758  -14.55760 1.000 92.44839  ?  217 ARG   I NH1 1 
ATOM   1305  N NH2 . ARG   A  1 217 ? 8.53674   21.44942  -13.36219 1.000 112.03033 ?  217 ARG   I NH2 1 
ATOM   1306  N N   . PHE   A  1 218 ? 4.67801   16.64303  -19.30699 1.000 38.34614  ?  218 PHE   I N   1 
ATOM   1307  C CA  . PHE   A  1 218 ? 3.31566   16.31759  -19.72623 1.000 27.21397  ?  218 PHE   I CA  1 
ATOM   1308  C C   . PHE   A  1 218 ? 2.34151   16.57142  -18.57783 1.000 57.66427  ?  218 PHE   I C   1 
ATOM   1309  O O   . PHE   A  1 218 ? 2.61940   16.21952  -17.42844 1.000 29.42505  ?  218 PHE   I O   1 
ATOM   1310  C CB  . PHE   A  1 218 ? 3.20982   14.86224  -20.16652 1.000 18.06489  ?  218 PHE   I CB  1 
ATOM   1311  C CG  . PHE   A  1 218 ? 3.86198   14.57219  -21.48324 1.000 37.72071  ?  218 PHE   I CG  1 
ATOM   1312  C CD1 . PHE   A  1 218 ? 3.41444   15.19334  -22.65277 1.000 19.73281  ?  218 PHE   I CD1 1 
ATOM   1313  C CD2 . PHE   A  1 218 ? 4.91653   13.65715  -21.56052 1.000 28.39348  ?  218 PHE   I CD2 1 
ATOM   1314  C CE1 . PHE   A  1 218 ? 4.00945   14.91710  -23.88103 1.000 44.98267  ?  218 PHE   I CE1 1 
ATOM   1315  C CE2 . PHE   A  1 218 ? 5.51973   13.37705  -22.77645 1.000 27.66067  ?  218 PHE   I CE2 1 
ATOM   1316  C CZ  . PHE   A  1 218 ? 5.06527   14.01012  -23.94253 1.000 20.91627  ?  218 PHE   I CZ  1 
ATOM   1317  N N   . ARG   A  1 219 ? 1.18869   17.17001  -18.88466 1.000 41.04784  ?  219 ARG   I N   1 
ATOM   1318  C CA  . ARG   A  1 219 ? 0.18076   17.37904  -17.84794 1.000 45.37915  ?  219 ARG   I CA  1 
ATOM   1319  C C   . ARG   A  1 219 ? -0.45130  16.06684  -17.40721 1.000 42.31836  ?  219 ARG   I C   1 
ATOM   1320  O O   . ARG   A  1 219 ? -0.82143  15.91119  -16.23937 1.000 40.85433  ?  219 ARG   I O   1 
ATOM   1321  C CB  . ARG   A  1 219 ? -0.91113  18.32476  -18.34072 1.000 38.16635  ?  219 ARG   I CB  1 
ATOM   1322  C CG  . ARG   A  1 219 ? -1.89084  18.68108  -17.21803 1.000 54.60606  ?  219 ARG   I CG  1 
ATOM   1323  C CD  . ARG   A  1 219 ? -3.07876  19.47607  -17.70382 1.000 44.51021  ?  219 ARG   I CD  1 
ATOM   1324  N NE  . ARG   A  1 219 ? -2.69795  20.78663  -18.21167 1.000 30.63719  ?  219 ARG   I NE  1 
ATOM   1325  C CZ  . ARG   A  1 219 ? -2.29872  21.79126  -17.44365 1.000 98.54422  ?  219 ARG   I CZ  1 
ATOM   1326  N NH1 . ARG   A  1 219 ? -2.22363  21.67308  -16.12926 1.000 30.89124  ?  219 ARG   I NH1 1 
ATOM   1327  N NH2 . ARG   A  1 219 ? -1.96254  22.94428  -18.00699 1.000 22.70672  ?  219 ARG   I NH2 1 
ATOM   1328  N N   . ASN   A  1 220 ? -0.58265  15.11671  -18.32187 1.000 36.00478  ?  220 ASN   I N   1 
ATOM   1329  C CA  . ASN   A  1 220 ? -1.28522  13.88302  -18.02345 1.000 42.05173  ?  220 ASN   I CA  1 
ATOM   1330  C C   . ASN   A  1 220 ? -0.87190  12.82560  -19.03684 1.000 38.93969  ?  220 ASN   I C   1 
ATOM   1331  O O   . ASN   A  1 220 ? -1.56943  12.60978  -20.03877 1.000 44.38178  ?  220 ASN   I O   1 
ATOM   1332  C CB  . ASN   A  1 220 ? -2.79547  14.12534  -18.06153 1.000 49.96309  ?  220 ASN   I CB  1 
ATOM   1333  C CG  . ASN   A  1 220 ? -3.58946  12.98437  -17.46411 1.000 75.24607  ?  220 ASN   I CG  1 
ATOM   1334  O OD1 . ASN   A  1 220 ? -3.10172  11.85493  -17.33245 1.000 50.49420  ?  220 ASN   I OD1 1 
ATOM   1335  N ND2 . ASN   A  1 220 ? -4.82851  13.27224  -17.10336 1.000 51.77884  ?  220 ASN   I ND2 1 
ATOM   1336  N N   . ARG   A  1 221 ? 0.25968   12.16067  -18.78890 1.000 34.82577  ?  221 ARG   I N   1 
ATOM   1337  C CA  . ARG   A  1 221 ? 0.77895   11.23295  -19.79099 1.000 38.16783  ?  221 ARG   I CA  1 
ATOM   1338  C C   . ARG   A  1 221 ? -0.18816  10.08050  -20.04869 1.000 46.85845  ?  221 ARG   I C   1 
ATOM   1339  O O   . ARG   A  1 221 ? -0.24757  9.57836   -21.17476 1.000 36.79134  ?  221 ARG   I O   1 
ATOM   1340  C CB  . ARG   A  1 221 ? 2.16530   10.71349  -19.38039 1.000 25.64408  ?  221 ARG   I CB  1 
ATOM   1341  C CG  . ARG   A  1 221 ? 2.18432   9.80737   -18.14364 1.000 26.16846  ?  221 ARG   I CG  1 
ATOM   1342  C CD  . ARG   A  1 221 ? 2.23603   8.31817   -18.51734 1.000 37.86795  ?  221 ARG   I CD  1 
ATOM   1343  N NE  . ARG   A  1 221 ? 2.18342   7.45822   -17.33651 1.000 32.89835  ?  221 ARG   I NE  1 
ATOM   1344  C CZ  . ARG   A  1 221 ? 3.24112   7.03857   -16.64943 1.000 44.42749  ?  221 ARG   I CZ  1 
ATOM   1345  N NH1 . ARG   A  1 221 ? 4.47682   7.37871   -16.98532 1.000 38.79889  ?  221 ARG   I NH1 1 
ATOM   1346  N NH2 . ARG   A  1 221 ? 3.05764   6.24787   -15.60168 1.000 29.51787  ?  221 ARG   I NH2 1 
ATOM   1347  N N   . ASP   A  1 222 ? -0.98242  9.67569   -19.04440 1.000 34.29480  ?  222 ASP   I N   1 
ATOM   1348  C CA  . ASP   A  1 222 ? -1.92202  8.57079   -19.24510 1.000 51.27762  ?  222 ASP   I CA  1 
ATOM   1349  C C   . ASP   A  1 222 ? -2.99763  8.87647   -20.29160 1.000 54.00387  ?  222 ASP   I C   1 
ATOM   1350  O O   . ASP   A  1 222 ? -3.57070  7.94088   -20.86760 1.000 40.82650  ?  222 ASP   I O   1 
ATOM   1351  C CB  . ASP   A  1 222 ? -2.58115  8.18257   -17.92133 1.000 28.80031  ?  222 ASP   I CB  1 
ATOM   1352  C CG  . ASP   A  1 222 ? -1.56660  7.67032   -16.88210 1.000 47.79241  ?  222 ASP   I CG  1 
ATOM   1353  O OD1 . ASP   A  1 222 ? -0.95428  6.58810   -17.06740 1.000 54.75709  ?  222 ASP   I OD1 1 
ATOM   1354  O OD2 . ASP   A  1 222 ? -1.36751  8.38966   -15.88496 1.000 63.89109  ?  222 ASP   I OD2 1 
ATOM   1355  N N   . ILE   A  1 223 ? -3.27651  10.14837  -20.57349 1.000 27.14033  ?  223 ILE   I N   1 
ATOM   1356  C CA  . ILE   A  1 223 ? -4.14472  10.47129  -21.70302 1.000 36.69655  ?  223 ILE   I CA  1 
ATOM   1357  C C   . ILE   A  1 223 ? -3.34473  10.52333  -23.00326 1.000 47.90541  ?  223 ILE   I C   1 
ATOM   1358  O O   . ILE   A  1 223 ? -3.63620  9.79567   -23.96004 1.000 50.43239  ?  223 ILE   I O   1 
ATOM   1359  C CB  . ILE   A  1 223 ? -4.89863  11.78950  -21.43927 1.000 49.32568  ?  223 ILE   I CB  1 
ATOM   1360  C CG1 . ILE   A  1 223 ? -5.91534  11.60680  -20.31623 1.000 30.34236  ?  223 ILE   I CG1 1 
ATOM   1361  C CG2 . ILE   A  1 223 ? -5.61278  12.28164  -22.68578 1.000 18.13080  ?  223 ILE   I CG2 1 
ATOM   1362  C CD1 . ILE   A  1 223 ? -6.53942  12.90551  -19.89891 1.000 33.37068  ?  223 ILE   I CD1 1 
ATOM   1363  N N   . ASP   A  1 224 ? -2.30205  11.36186  -23.04117 1.000 39.35387  ?  224 ASP   I N   1 
ATOM   1364  C CA  . ASP   A  1 224 ? -1.62619  11.73052  -24.28534 1.000 40.45941  ?  224 ASP   I CA  1 
ATOM   1365  C C   . ASP   A  1 224 ? -0.48442  10.80628  -24.70554 1.000 41.33617  ?  224 ASP   I C   1 
ATOM   1366  O O   . ASP   A  1 224 ? -0.25510  10.64277  -25.91128 1.000 36.92789  ?  224 ASP   I O   1 
ATOM   1367  C CB  . ASP   A  1 224 ? -1.08701  13.15186  -24.16363 1.000 36.36952  ?  224 ASP   I CB  1 
ATOM   1368  C CG  . ASP   A  1 224 ? -2.16654  14.14517  -23.80347 1.000 49.73817  ?  224 ASP   I CG  1 
ATOM   1369  O OD1 . ASP   A  1 224 ? -3.06358  14.35102  -24.64694 1.000 52.86834  ?  224 ASP   I OD1 1 
ATOM   1370  O OD2 . ASP   A  1 224 ? -2.12070  14.69684  -22.68030 1.000 49.39020  ?  224 ASP   I OD2 1 
ATOM   1371  N N   . ARG   A  1 225 ? 0.25989   10.22794  -23.76298 1.000 42.56821  ?  225 ARG   I N   1 
ATOM   1372  C CA  . ARG   A  1 225 ? 1.42361   9.38765   -24.07185 1.000 33.24212  ?  225 ARG   I CA  1 
ATOM   1373  C C   . ARG   A  1 225 ? 1.45927   8.23070   -23.08806 1.000 48.34036  ?  225 ARG   I C   1 
ATOM   1374  O O   . ARG   A  1 225 ? 2.34865   8.13635   -22.23233 1.000 42.37767  ?  225 ARG   I O   1 
ATOM   1375  C CB  . ARG   A  1 225 ? 2.72014   10.20432  -24.00682 1.000 34.29409  ?  225 ARG   I CB  1 
ATOM   1376  C CG  . ARG   A  1 225 ? 3.05586   11.12951  -25.28695 1.000 22.51717  ?  225 ARG   I CG  1 
ATOM   1377  C CD  . ARG   A  1 225 ? 3.10963   10.38357  -26.63831 1.000 14.55533  ?  225 ARG   I CD  1 
ATOM   1378  N NE  . ARG   A  1 225 ? 3.26979   11.29196  -27.78415 1.000 49.74102  ?  225 ARG   I NE  1 
ATOM   1379  C CZ  . ARG   A  1 225 ? 2.27853   11.71243  -28.57093 1.000 33.96993  ?  225 ARG   I CZ  1 
ATOM   1380  N NH1 . ARG   A  1 225 ? 1.02929   11.33823  -28.35181 1.000 47.66745  ?  225 ARG   I NH1 1 
ATOM   1381  N NH2 . ARG   A  1 225 ? 2.55297   12.52466  -29.60567 1.000 25.57515  ?  225 ARG   I NH2 1 
ATOM   1382  N N   . PRO   A  1 226 ? 0.48253   7.33471   -23.16259 1.000 42.54950  ?  226 PRO   I N   1 
ATOM   1383  C CA  . PRO   A  1 226 ? 0.38846   6.26760   -22.15753 1.000 24.35170  ?  226 PRO   I CA  1 
ATOM   1384  C C   . PRO   A  1 226 ? 1.52737   5.26818   -22.27549 1.000 48.88809  ?  226 PRO   I C   1 
ATOM   1385  O O   . PRO   A  1 226 ? 2.04316   5.00175   -23.36275 1.000 32.11943  ?  226 PRO   I O   1 
ATOM   1386  C CB  . PRO   A  1 226 ? -0.95405  5.59543   -22.47757 1.000 23.46694  ?  226 PRO   I CB  1 
ATOM   1387  C CG  . PRO   A  1 226 ? -1.18827  5.90170   -23.95338 1.000 22.24370  ?  226 PRO   I CG  1 
ATOM   1388  C CD  . PRO   A  1 226 ? -0.59878  7.27129   -24.16957 1.000 25.44623  ?  226 PRO   I CD  1 
ATOM   1389  N N   . VAL   A  1 227 ? 1.90519   4.70080   -21.13059 1.000 32.32058  ?  227 VAL   I N   1 
ATOM   1390  C CA  . VAL   A  1 227 ? 2.82239   3.56835   -21.08942 1.000 29.34451  ?  227 VAL   I CA  1 
ATOM   1391  C C   . VAL   A  1 227 ? 2.08465   2.35383   -21.63672 1.000 41.78050  ?  227 VAL   I C   1 
ATOM   1392  O O   . VAL   A  1 227 ? 1.46013   1.60547   -20.87661 1.000 42.77092  ?  227 VAL   I O   1 
ATOM   1393  C CB  . VAL   A  1 227 ? 3.34167   3.31783   -19.66007 1.000 32.51629  ?  227 VAL   I CB  1 
ATOM   1394  C CG1 . VAL   A  1 227 ? 4.34182   2.16910   -19.63023 1.000 33.67498  ?  227 VAL   I CG1 1 
ATOM   1395  C CG2 . VAL   A  1 227 ? 3.96805   4.58732   -19.10352 1.000 27.74025  ?  227 VAL   I CG2 1 
ATOM   1396  N N   . VAL   A  1 228 ? 2.15788   2.15781   -22.96042 1.000 33.20594  ?  228 VAL   I N   1 
ATOM   1397  C CA  . VAL   A  1 228 ? 1.31564   1.19051   -23.65728 1.000 20.79780  ?  228 VAL   I CA  1 
ATOM   1398  C C   . VAL   A  1 228 ? 1.48783   -0.20017  -23.06749 1.000 61.08346  ?  228 VAL   I C   1 
ATOM   1399  O O   . VAL   A  1 228 ? 2.60953   -0.68310  -22.87566 1.000 31.35450  ?  228 VAL   I O   1 
ATOM   1400  C CB  . VAL   A  1 228 ? 1.63576   1.21659   -25.15768 1.000 39.21430  ?  228 VAL   I CB  1 
ATOM   1401  C CG1 . VAL   A  1 228 ? 0.79031   0.19951   -25.90537 1.000 25.60880  ?  228 VAL   I CG1 1 
ATOM   1402  C CG2 . VAL   A  1 228 ? 1.41843   2.62595   -25.69998 1.000 20.22366  ?  228 VAL   I CG2 1 
ATOM   1403  N N   . GLY   A  1 229 ? 0.36130   -0.85213  -22.77581 1.000 37.69109  ?  229 GLY   I N   1 
ATOM   1404  C CA  . GLY   A  1 229 ? 0.35760   -2.15758  -22.14711 1.000 21.59731  ?  229 GLY   I CA  1 
ATOM   1405  C C   . GLY   A  1 229 ? 0.50928   -2.14101  -20.64080 1.000 28.61374  ?  229 GLY   I C   1 
ATOM   1406  O O   . GLY   A  1 229 ? 0.35941   -3.19791  -20.00366 1.000 43.81543  ?  229 GLY   I O   1 
ATOM   1407  N N   . GLY   A  1 230 ? 0.81774   -0.98944  -20.05855 1.000 44.26001  ?  230 GLY   I N   1 
ATOM   1408  C CA  . GLY   A  1 230 ? 0.93439   -0.81164  -18.61624 1.000 15.31402  ?  230 GLY   I CA  1 
ATOM   1409  C C   . GLY   A  1 230 ? 2.29696   -1.20426  -18.07548 1.000 62.86926  ?  230 GLY   I C   1 
ATOM   1410  O O   . GLY   A  1 230 ? 2.94954   -2.13927  -18.54914 1.000 32.87669  ?  230 GLY   I O   1 
ATOM   1411  N N   . VAL   A  1 231 ? 2.71505   -0.48062  -17.03112 1.000 32.40008  ?  231 VAL   I N   1 
ATOM   1412  C CA  . VAL   A  1 231 ? 4.01257   -0.66810  -16.39164 1.000 72.74462  ?  231 VAL   I CA  1 
ATOM   1413  C C   . VAL   A  1 231 ? 4.22258   -2.10545  -15.92706 1.000 32.60851  ?  231 VAL   I C   1 
ATOM   1414  O O   . VAL   A  1 231 ? 5.36847   -2.55436  -15.79079 1.000 67.72158  ?  231 VAL   I O   1 
ATOM   1415  C CB  . VAL   A  1 231 ? 4.13292   0.33795   -15.23150 1.000 25.20739  ?  231 VAL   I CB  1 
ATOM   1416  C CG1 . VAL   A  1 231 ? 2.99092   0.14411   -14.27926 1.000 80.01427  ?  231 VAL   I CG1 1 
ATOM   1417  C CG2 . VAL   A  1 231 ? 5.42232   0.17080   -14.49173 1.000 52.56244  ?  231 VAL   I CG2 1 
ATOM   1418  N N   . ASN   A  1 232 ? 3.14104   -2.86400  -15.74524 1.000 48.32024  ?  232 ASN   I N   1 
ATOM   1419  C CA  . ASN   A  1 232 ? 3.23690   -4.23379  -15.24727 1.000 37.29652  ?  232 ASN   I CA  1 
ATOM   1420  C C   . ASN   A  1 232 ? 3.61832   -5.25506  -16.31167 1.000 48.97981  ?  232 ASN   I C   1 
ATOM   1421  O O   . ASN   A  1 232 ? 4.03847   -6.36164  -15.95292 1.000 44.18768  ?  232 ASN   I O   1 
ATOM   1422  C CB  . ASN   A  1 232 ? 1.91466   -4.65770  -14.62111 1.000 54.04065  ?  232 ASN   I CB  1 
ATOM   1423  C CG  . ASN   A  1 232 ? 1.82216   -4.28031  -13.16665 1.000 53.66183  ?  232 ASN   I CG  1 
ATOM   1424  O OD1 . ASN   A  1 232 ? 2.61544   -3.46732  -12.67426 1.000 54.66730  ?  232 ASN   I OD1 1 
ATOM   1425  N ND2 . ASN   A  1 232 ? 0.85646   -4.86897  -12.46052 1.000 129.79418 ?  232 ASN   I ND2 1 
ATOM   1426  N N   . ASN   A  1 233 ? 3.45947   -4.94070  -17.59730 1.000 26.97273  ?  233 ASN   I N   1 
ATOM   1427  C CA  . ASN   A  1 233 ? 3.84901   -5.85764  -18.66086 1.000 34.67201  ?  233 ASN   I CA  1 
ATOM   1428  C C   . ASN   A  1 233 ? 5.32229   -5.59468  -18.96490 1.000 87.14061  ?  233 ASN   I C   1 
ATOM   1429  O O   . ASN   A  1 233 ? 5.67377   -4.57387  -19.57762 1.000 32.42022  ?  233 ASN   I O   1 
ATOM   1430  C CB  . ASN   A  1 233 ? 2.96963   -5.65699  -19.89365 1.000 14.58570  ?  233 ASN   I CB  1 
ATOM   1431  C CG  . ASN   A  1 233 ? 3.23608   -6.68604  -20.97010 1.000 51.97579  ?  233 ASN   I CG  1 
ATOM   1432  O OD1 . ASN   A  1 233 ? 4.33435   -7.23964  -21.07126 1.000 45.03864  ?  233 ASN   I OD1 1 
ATOM   1433  N ND2 . ASN   A  1 233 ? 2.23198   -6.93877  -21.79446 1.000 40.72530  ?  233 ASN   I ND2 1 
ATOM   1434  N N   . THR   A  1 234 ? 6.19167   -6.49487  -18.51714 1.000 37.78951  ?  234 THR   I N   1 
ATOM   1435  C CA  . THR   A  1 234 ? 7.62299   -6.26940  -18.66530 1.000 53.12396  ?  234 THR   I CA  1 
ATOM   1436  C C   . THR   A  1 234 ? 8.17726   -6.86936  -19.95008 1.000 33.35809  ?  234 THR   I C   1 
ATOM   1437  O O   . THR   A  1 234 ? 9.39273   -6.83226  -20.16531 1.000 83.85575  ?  234 THR   I O   1 
ATOM   1438  C CB  . THR   A  1 234 ? 8.38421   -6.79848  -17.44241 1.000 39.02050  ?  234 THR   I CB  1 
ATOM   1439  O OG1 . THR   A  1 234 ? 8.31689   -8.22412  -17.39109 1.000 49.20430  ?  234 THR   I OG1 1 
ATOM   1440  C CG2 . THR   A  1 234 ? 7.79786   -6.22629  -16.16351 1.000 29.00858  ?  234 THR   I CG2 1 
ATOM   1441  N N   . THR   A  1 235 ? 7.31044   -7.36827  -20.82470 1.000 56.79110  ?  235 THR   I N   1 
ATOM   1442  C CA  . THR   A  1 235 ? 7.72977   -7.86188  -22.12701 1.000 39.00151  ?  235 THR   I CA  1 
ATOM   1443  C C   . THR   A  1 235 ? 7.81137   -6.76188  -23.17567 1.000 59.10588  ?  235 THR   I C   1 
ATOM   1444  O O   . THR   A  1 235 ? 8.13932   -7.05635  -24.33273 1.000 42.36177  ?  235 THR   I O   1 
ATOM   1445  C CB  . THR   A  1 235 ? 6.76424   -8.94778  -22.60401 1.000 74.15190  ?  235 THR   I CB  1 
ATOM   1446  O OG1 . THR   A  1 235 ? 5.57529   -8.34199  -23.14535 1.000 35.34124  ?  235 THR   I OG1 1 
ATOM   1447  C CG2 . THR   A  1 235 ? 6.37130   -9.82498  -21.43902 1.000 45.30970  ?  235 THR   I CG2 1 
ATOM   1448  N N   . LEU   A  1 236 ? 7.52867   -5.51036  -22.80315 1.000 43.88923  ?  236 LEU   I N   1 
ATOM   1449  C CA  . LEU   A  1 236 ? 7.44992   -4.39681  -23.74195 1.000 44.36088  ?  236 LEU   I CA  1 
ATOM   1450  C C   . LEU   A  1 236 ? 8.53938   -3.38598  -23.43559 1.000 37.97911  ?  236 LEU   I C   1 
ATOM   1451  O O   . LEU   A  1 236 ? 8.84695   -3.12750  -22.26649 1.000 39.69740  ?  236 LEU   I O   1 
ATOM   1452  C CB  . LEU   A  1 236 ? 6.09174   -3.70078  -23.67352 1.000 37.88715  ?  236 LEU   I CB  1 
ATOM   1453  C CG  . LEU   A  1 236 ? 4.89481   -4.64361  -23.76462 1.000 45.18024  ?  236 LEU   I CG  1 
ATOM   1454  C CD1 . LEU   A  1 236 ? 3.63038   -3.92910  -23.28466 1.000 37.13108  ?  236 LEU   I CD1 1 
ATOM   1455  C CD2 . LEU   A  1 236 ? 4.75534   -5.18343  -25.18812 1.000 27.60672  ?  236 LEU   I CD2 1 
ATOM   1456  N N   . ILE   A  1 237 ? 9.12154   -2.82114  -24.49141 1.000 35.68105  ?  237 ILE   I N   1 
ATOM   1457  C CA  . ILE   A  1 237 ? 10.13025  -1.77460  -24.37510 1.000 29.00757  ?  237 ILE   I CA  1 
ATOM   1458  C C   . ILE   A  1 237 ? 9.56198   -0.51032  -25.00589 1.000 40.24398  ?  237 ILE   I C   1 
ATOM   1459  O O   . ILE   A  1 237 ? 9.15720   -0.51911  -26.18285 1.000 27.16697  ?  237 ILE   I O   1 
ATOM   1460  C CB  . ILE   A  1 237 ? 11.46232  -2.17280  -25.03540 1.000 27.83079  ?  237 ILE   I CB  1 
ATOM   1461  C CG1 . ILE   A  1 237 ? 12.00904  -3.46547  -24.41692 1.000 24.75322  ?  237 ILE   I CG1 1 
ATOM   1462  C CG2 . ILE   A  1 237 ? 12.48248  -1.03479  -24.87637 1.000 25.70010  ?  237 ILE   I CG2 1 
ATOM   1463  C CD1 . ILE   A  1 237 ? 13.35139  -3.92581  -24.99135 1.000 26.64798  ?  237 ILE   I CD1 1 
ATOM   1464  N N   . SER   A  1 238 ? 9.54973   0.57755   -24.22258 1.000 22.94281  ?  238 SER   I N   1 
ATOM   1465  C CA  . SER   A  1 238 ? 8.96971   1.85617   -24.62868 1.000 29.71182  ?  238 SER   I CA  1 
ATOM   1466  C C   . SER   A  1 238 ? 9.99148   2.75861   -25.30569 1.000 38.45783  ?  238 SER   I C   1 
ATOM   1467  O O   . SER   A  1 238 ? 11.18953  2.70769   -25.01245 1.000 23.43000  ?  238 SER   I O   1 
ATOM   1468  C CB  . SER   A  1 238 ? 8.39042   2.60612   -23.42496 1.000 28.17437  ?  238 SER   I CB  1 
ATOM   1469  O OG  . SER   A  1 238 ? 7.07163   2.18299   -23.14938 1.000 41.95568  ?  238 SER   I OG  1 
ATOM   1470  N N   . ALA   A  1 239 ? 9.48958   3.61774   -26.19237 1.000 34.33437  ?  239 ALA   I N   1 
ATOM   1471  C CA  . ALA   A  1 239 ? 10.29492  4.69312   -26.75775 1.000 42.38957  ?  239 ALA   I CA  1 
ATOM   1472  C C   . ALA   A  1 239 ? 10.72310  5.66751   -25.67222 1.000 18.59009  ?  239 ALA   I C   1 
ATOM   1473  O O   . ALA   A  1 239 ? 9.88976   6.15438   -24.90639 1.000 34.02282  ?  239 ALA   I O   1 
ATOM   1474  C CB  . ALA   A  1 239 ? 9.49568   5.43301   -27.82239 1.000 14.96480  ?  239 ALA   I CB  1 
ATOM   1475  N N   . ALA   A  1 240 ? 12.02383  5.98344   -25.62755 1.000 38.84244  ?  240 ALA   I N   1 
ATOM   1476  C CA  . ALA   A  1 240 ? 12.54290  6.86401   -24.57902 1.000 32.46201  ?  240 ALA   I CA  1 
ATOM   1477  C C   . ALA   A  1 240 ? 12.34565  8.34604   -24.87721 1.000 38.93162  ?  240 ALA   I C   1 
ATOM   1478  O O   . ALA   A  1 240 ? 12.37432  9.16177   -23.94426 1.000 34.24712  ?  240 ALA   I O   1 
ATOM   1479  C CB  . ALA   A  1 240 ? 14.03088  6.60057   -24.35015 1.000 24.19201  ?  240 ALA   I CB  1 
ATOM   1480  N N   . CYS   A  1 241 ? 12.17006  8.71213   -26.14808 1.000 23.88389  ?  241 CYS   I N   1 
ATOM   1481  C CA  . CYS   A  1 241 ? 12.06513  10.10476  -26.55642 1.000 33.78994  ?  241 CYS   I CA  1 
ATOM   1482  C C   . CYS   A  1 241 ? 10.95690  10.23848  -27.58555 1.000 34.09975  ?  241 CYS   I C   1 
ATOM   1483  O O   . CYS   A  1 241 ? 10.81210  9.38792   -28.47352 1.000 33.10220  ?  241 CYS   I O   1 
ATOM   1484  C CB  . CYS   A  1 241 ? 13.37044  10.63974  -27.16570 1.000 35.42742  ?  241 CYS   I CB  1 
ATOM   1485  S SG  . CYS   A  1 241 ? 14.76198  10.69009  -26.01996 1.000 35.68375  ?  241 CYS   I SG  1 
ATOM   1486  N N   . GLU   A  1 242 ? 10.17246  11.31043  -27.44669 1.000 38.84159  ?  242 GLU   I N   1 
ATOM   1487  C CA  . GLU   A  1 242 ? 9.28301   11.76786  -28.50420 1.000 22.50940  ?  242 GLU   I CA  1 
ATOM   1488  C C   . GLU   A  1 242 ? 10.10089  12.12908  -29.73890 1.000 25.41119  ?  242 GLU   I C   1 
ATOM   1489  O O   . GLU   A  1 242 ? 10.85844  13.10886  -29.71748 1.000 47.99183  ?  242 GLU   I O   1 
ATOM   1490  C CB  . GLU   A  1 242 ? 8.48444   12.97375  -28.01365 1.000 33.39041  ?  242 GLU   I CB  1 
ATOM   1491  C CG  . GLU   A  1 242 ? 7.47730   13.52954  -29.01358 1.000 27.72350  ?  242 GLU   I CG  1 
ATOM   1492  C CD  . GLU   A  1 242 ? 6.22627   12.67011  -29.15921 1.000 51.72806  ?  242 GLU   I CD  1 
ATOM   1493  O OE1 . GLU   A  1 242 ? 5.94193   11.80789  -28.27833 1.000 31.20418  ?  242 GLU   I OE1 1 
ATOM   1494  O OE2 . GLU   A  1 242 ? 5.52643   12.87763  -30.17672 1.000 37.74905  ?  242 GLU   I OE2 1 
ATOM   1495  N N   . SER   A  1 243 ? 9.96633   11.36704  -30.82162 1.000 30.54737  ?  243 SER   I N   1 
ATOM   1496  C CA  . SER   A  1 243 ? 10.92126  11.49606  -31.91644 1.000 42.03082  ?  243 SER   I CA  1 
ATOM   1497  C C   . SER   A  1 243 ? 10.30875  10.96673  -33.20606 1.000 32.26299  ?  243 SER   I C   1 
ATOM   1498  O O   . SER   A  1 243 ? 9.18131   10.46013  -33.22855 1.000 36.76705  ?  243 SER   I O   1 
ATOM   1499  C CB  . SER   A  1 243 ? 12.22086  10.73956  -31.59184 1.000 31.26073  ?  243 SER   I CB  1 
ATOM   1500  O OG  . SER   A  1 243 ? 11.93321  9.36668   -31.33747 1.000 38.75693  ?  243 SER   I OG  1 
ATOM   1501  N N   . LEU   A  1 244 ? 11.09323  11.07380  -34.28078 1.000 35.06156  ?  244 LEU   I N   1 
ATOM   1502  C CA  . LEU   A  1 244 ? 10.84737  10.40214  -35.54969 1.000 40.59687  ?  244 LEU   I CA  1 
ATOM   1503  C C   . LEU   A  1 244 ? 11.86140  9.27577   -35.72728 1.000 38.09999  ?  244 LEU   I C   1 
ATOM   1504  O O   . LEU   A  1 244 ? 13.03686  9.43346   -35.37821 1.000 44.38132  ?  244 LEU   I O   1 
ATOM   1505  C CB  . LEU   A  1 244 ? 10.95306  11.38852  -36.70948 1.000 25.46486  ?  244 LEU   I CB  1 
ATOM   1506  C CG  . LEU   A  1 244 ? 9.92635   12.52008  -36.70945 1.000 43.90281  ?  244 LEU   I CG  1 
ATOM   1507  C CD1 . LEU   A  1 244 ? 10.33946  13.61789  -37.66109 1.000 37.86360  ?  244 LEU   I CD1 1 
ATOM   1508  C CD2 . LEU   A  1 244 ? 8.61180   11.93241  -37.11345 1.000 31.09189  ?  244 LEU   I CD2 1 
ATOM   1509  N N   . SER   A  1 245 ? 11.39524  8.13251   -36.22552 1.000 69.02256  ?  245 SER   I N   1 
ATOM   1510  C CA  . SER   A  1 245 ? 12.26651  7.05010   -36.66797 1.000 29.64439  ?  245 SER   I CA  1 
ATOM   1511  C C   . SER   A  1 245 ? 13.39852  7.59365   -37.54159 1.000 29.69002  ?  245 SER   I C   1 
ATOM   1512  O O   . SER   A  1 245 ? 13.15618  8.37497   -38.46999 1.000 38.65301  ?  245 SER   I O   1 
ATOM   1513  C CB  . SER   A  1 245 ? 11.41112  6.05459   -37.45614 1.000 32.38472  ?  245 SER   I CB  1 
ATOM   1514  O OG  . SER   A  1 245 ? 12.17467  4.98888   -37.95104 1.000 77.95752  ?  245 SER   I OG  1 
ATOM   1515  N N   . TYR   A  1 246 ? 14.64414  7.19858   -37.24664 1.000 43.38976  ?  246 TYR   I N   1 
ATOM   1516  C CA  . TYR   A  1 246 ? 15.74793  7.62907   -38.11002 1.000 33.52637  ?  246 TYR   I CA  1 
ATOM   1517  C C   . TYR   A  1 246 ? 16.50070  6.48081   -38.76983 1.000 35.14152  ?  246 TYR   I C   1 
ATOM   1518  O O   . TYR   A  1 246 ? 16.82316  6.56728   -39.96596 1.000 38.20186  ?  246 TYR   I O   1 
ATOM   1519  C CB  . TYR   A  1 246 ? 16.75054  8.51638   -37.35400 1.000 23.89869  ?  246 TYR   I CB  1 
ATOM   1520  C CG  . TYR   A  1 246 ? 17.81538  9.05338   -38.28449 1.000 40.07964  ?  246 TYR   I CG  1 
ATOM   1521  C CD1 . TYR   A  1 246 ? 18.96417  8.30650   -38.58878 1.000 33.18434  ?  246 TYR   I CD1 1 
ATOM   1522  C CD2 . TYR   A  1 246 ? 17.66670  10.30140  -38.87816 1.000 19.29305  ?  246 TYR   I CD2 1 
ATOM   1523  C CE1 . TYR   A  1 246 ? 19.91232  8.79742   -39.46451 1.000 26.92222  ?  246 TYR   I CE1 1 
ATOM   1524  C CE2 . TYR   A  1 246 ? 18.61994  10.80772  -39.75135 1.000 45.58552  ?  246 TYR   I CE2 1 
ATOM   1525  C CZ  . TYR   A  1 246 ? 19.73101  10.05290  -40.04202 1.000 36.60526  ?  246 TYR   I CZ  1 
ATOM   1526  O OH  . TYR   A  1 246 ? 20.64951  10.57248  -40.90901 1.000 52.70278  ?  246 TYR   I OH  1 
ATOM   1527  N N   . ASN   A  1 247 ? 16.85956  5.44400   -38.01249 1.000 31.48410  ?  247 ASN   I N   1 
ATOM   1528  C CA  . ASN   A  1 247 ? 17.56344  4.28815   -38.55533 1.000 23.86807  ?  247 ASN   I CA  1 
ATOM   1529  C C   . ASN   A  1 247 ? 17.35003  3.11780   -37.60940 1.000 30.94314  ?  247 ASN   I C   1 
ATOM   1530  O O   . ASN   A  1 247 ? 17.24161  3.30186   -36.39160 1.000 34.17808  ?  247 ASN   I O   1 
ATOM   1531  C CB  . ASN   A  1 247 ? 19.06543  4.54328   -38.73285 1.000 34.10611  ?  247 ASN   I CB  1 
ATOM   1532  C CG  . ASN   A  1 247 ? 19.82668  3.27854   -39.11278 1.000 31.75519  ?  247 ASN   I CG  1 
ATOM   1533  O OD1 . ASN   A  1 247 ? 19.76641  2.83975   -40.26371 1.000 49.23326  ?  247 ASN   I OD1 1 
ATOM   1534  N ND2 . ASN   A  1 247 ? 20.52205  2.66823   -38.14193 1.000 30.19676  ?  247 ASN   I ND2 1 
ATOM   1535  N N   . VAL   A  1 248 ? 17.26431  1.91598   -38.18342 1.000 34.20904  ?  248 VAL   I N   1 
ATOM   1536  C CA  . VAL   A  1 248 ? 17.40600  0.67415   -37.43275 1.000 40.00025  ?  248 VAL   I CA  1 
ATOM   1537  C C   . VAL   A  1 248 ? 18.52108  -0.13210  -38.07399 1.000 31.53563  ?  248 VAL   I C   1 
ATOM   1538  O O   . VAL   A  1 248 ? 18.60265  -0.21615  -39.30397 1.000 39.04403  ?  248 VAL   I O   1 
ATOM   1539  C CB  . VAL   A  1 248 ? 16.10137  -0.13674  -37.40351 1.000 35.54961  ?  248 VAL   I CB  1 
ATOM   1540  C CG1 . VAL   A  1 248 ? 16.36871  -1.55621  -36.89460 1.000 28.34547  ?  248 VAL   I CG1 1 
ATOM   1541  C CG2 . VAL   A  1 248 ? 15.06972  0.58084   -36.54915 1.000 33.64565  ?  248 VAL   I CG2 1 
ATOM   1542  N N   . SER   A  1 249 ? 19.40808  -0.68427  -37.24895 1.000 39.21335  ?  249 SER   I N   1 
ATOM   1543  C CA  . SER   A  1 249 ? 20.48253  -1.52496  -37.75761 1.000 26.58502  ?  249 SER   I CA  1 
ATOM   1544  C C   . SER   A  1 249 ? 20.50875  -2.82292  -36.97843 1.000 39.16442  ?  249 SER   I C   1 
ATOM   1545  O O   . SER   A  1 249 ? 20.34522  -2.82826  -35.75192 1.000 28.96621  ?  249 SER   I O   1 
ATOM   1546  C CB  . SER   A  1 249 ? 21.84325  -0.84218  -37.66915 1.000 26.17307  ?  249 SER   I CB  1 
ATOM   1547  O OG  . SER   A  1 249 ? 21.94875  0.17278   -38.64842 1.000 31.86636  ?  249 SER   I OG  1 
ATOM   1548  N N   . TYR   A  1 250 ? 20.70847  -3.91899  -37.70103 1.000 33.39162  ?  250 TYR   I N   1 
ATOM   1549  C CA  . TYR   A  1 250 ? 20.84101  -5.23611  -37.10759 1.000 59.53865  ?  250 TYR   I CA  1 
ATOM   1550  C C   . TYR   A  1 250 ? 22.27987  -5.71055  -37.24011 1.000 30.79234  ?  250 TYR   I C   1 
ATOM   1551  O O   . TYR   A  1 250 ? 23.03451  -5.24125  -38.10643 1.000 39.90028  ?  250 TYR   I O   1 
ATOM   1552  C CB  . TYR   A  1 250 ? 19.89211  -6.23389  -37.77735 1.000 30.22400  ?  250 TYR   I CB  1 
ATOM   1553  C CG  . TYR   A  1 250 ? 18.44181  -5.85310  -37.68477 1.000 45.75959  ?  250 TYR   I CG  1 
ATOM   1554  C CD1 . TYR   A  1 250 ? 17.70663  -6.12385  -36.53248 1.000 32.13974  ?  250 TYR   I CD1 1 
ATOM   1555  C CD2 . TYR   A  1 250 ? 17.80504  -5.21153  -38.73482 1.000 28.25795  ?  250 TYR   I CD2 1 
ATOM   1556  C CE1 . TYR   A  1 250 ? 16.35519  -5.77040  -36.43798 1.000 43.99045  ?  250 TYR   I CE1 1 
ATOM   1557  C CE2 . TYR   A  1 250 ? 16.46864  -4.85695  -38.65043 1.000 39.34053  ?  250 TYR   I CE2 1 
ATOM   1558  C CZ  . TYR   A  1 250 ? 15.74155  -5.13589  -37.50429 1.000 51.24658  ?  250 TYR   I CZ  1 
ATOM   1559  O OH  . TYR   A  1 250 ? 14.40050  -4.77813  -37.41842 1.000 56.76565  ?  250 TYR   I OH  1 
ATOM   1560  N N   . ASP   A  1 251 ? 22.64407  -6.64703  -36.35787 1.000 36.79988  ?  251 ASP   I N   1 
ATOM   1561  C CA  . ASP   A  1 251 ? 23.96979  -7.25991  -36.34655 1.000 37.05811  ?  251 ASP   I CA  1 
ATOM   1562  C C   . ASP   A  1 251 ? 25.06193  -6.18615  -36.34287 1.000 55.71210  ?  251 ASP   I C   1 
ATOM   1563  O O   . ASP   A  1 251 ? 25.91977  -6.11728  -37.22731 1.000 40.57835  ?  251 ASP   I O   1 
ATOM   1564  C CB  . ASP   A  1 251 ? 24.12351  -8.19818  -37.54520 1.000 36.38906  ?  251 ASP   I CB  1 
ATOM   1565  C CG  . ASP   A  1 251 ? 25.35495  -9.07606  -37.45186 1.000 58.59918  ?  251 ASP   I CG  1 
ATOM   1566  O OD1 . ASP   A  1 251 ? 25.62745  -9.57616  -36.33634 1.000 45.03237  ?  251 ASP   I OD1 1 
ATOM   1567  O OD2 . ASP   A  1 251 ? 26.02900  -9.26919  -38.49888 1.000 44.57516  ?  251 ASP   I OD2 1 
ATOM   1568  N N   . VAL   A  1 252 ? 24.99437  -5.30893  -35.34217 1.000 40.13271  ?  252 VAL   I N   1 
ATOM   1569  C CA  . VAL   A  1 252 ? 25.93042  -4.19090  -35.27940 1.000 42.42181  ?  252 VAL   I CA  1 
ATOM   1570  C C   . VAL   A  1 252 ? 27.29435  -4.66870  -34.79569 1.000 43.38770  ?  252 VAL   I C   1 
ATOM   1571  O O   . VAL   A  1 252 ? 27.43070  -5.68474  -34.10289 1.000 45.04149  ?  252 VAL   I O   1 
ATOM   1572  C CB  . VAL   A  1 252 ? 25.39456  -3.05950  -34.38942 1.000 45.26929  ?  252 VAL   I CB  1 
ATOM   1573  C CG1 . VAL   A  1 252 ? 24.12773  -2.46702  -35.00449 1.000 33.26437  ?  252 VAL   I CG1 1 
ATOM   1574  C CG2 . VAL   A  1 252 ? 25.18803  -3.56138  -32.94918 1.000 33.65484  ?  252 VAL   I CG2 1 
ATOM   1575  N N   . GLN   A  1 253 ? 28.31175  -3.88499  -35.13755 1.000 32.66627  ?  253 GLN   I N   1 
ATOM   1576  C CA  . GLN   A  1 253 ? 29.69764  -4.28568  -34.97599 1.000 38.43271  ?  253 GLN   I CA  1 
ATOM   1577  C C   . GLN   A  1 253 ? 30.55477  -3.07286  -34.60103 1.000 50.28955  ?  253 GLN   I C   1 
ATOM   1578  O O   . GLN   A  1 253 ? 30.07413  -1.93380  -34.51261 1.000 37.71936  ?  253 GLN   I O   1 
ATOM   1579  C CB  . GLN   A  1 253 ? 30.19226  -4.92349  -36.27286 1.000 27.06296  ?  253 GLN   I CB  1 
ATOM   1580  C CG  . GLN   A  1 253 ? 30.02778  -3.96750  -37.44016 1.000 64.63932  ?  253 GLN   I CG  1 
ATOM   1581  C CD  . GLN   A  1 253 ? 30.51835  -4.54482  -38.73198 1.000 55.90327  ?  253 GLN   I CD  1 
ATOM   1582  O OE1 . GLN   A  1 253 ? 30.13266  -4.09323  -39.81205 1.000 56.78382  ?  253 GLN   I OE1 1 
ATOM   1583  N NE2 . GLN   A  1 253 ? 31.38196  -5.54627  -38.63761 1.000 64.01356  ?  253 GLN   I NE2 1 
ATOM   1584  N N   . SER   A  1 254 ? 31.84831  -3.31944  -34.39883 1.000 47.68611  ?  254 SER   I N   1 
ATOM   1585  C CA  . SER   A  1 254 ? 32.80900  -2.25083  -34.17865 1.000 27.63135  ?  254 SER   I CA  1 
ATOM   1586  C C   . SER   A  1 254 ? 33.70816  -2.06314  -35.40114 1.000 29.72159  ?  254 SER   I C   1 
ATOM   1587  O O   . SER   A  1 254 ? 34.00926  -3.00600  -36.14220 1.000 41.47915  ?  254 SER   I O   1 
ATOM   1588  C CB  . SER   A  1 254 ? 33.64271  -2.52008  -32.93009 1.000 38.39852  ?  254 SER   I CB  1 
ATOM   1589  O OG  . SER   A  1 254 ? 32.79921  -2.57493  -31.78363 1.000 29.97027  ?  254 SER   I OG  1 
ATOM   1590  N N   . LEU   A  1 255 ? 34.10197  -0.81520  -35.62109 1.000 33.32340  ?  255 LEU   I N   1 
ATOM   1591  C CA  . LEU   A  1 255 ? 34.97934  -0.43601  -36.71259 1.000 35.68507  ?  255 LEU   I CA  1 
ATOM   1592  C C   . LEU   A  1 255 ? 36.28695  0.12370   -36.15785 1.000 37.22438  ?  255 LEU   I C   1 
ATOM   1593  O O   . LEU   A  1 255 ? 36.32970  0.68395   -35.05794 1.000 38.47277  ?  255 LEU   I O   1 
ATOM   1594  C CB  . LEU   A  1 255 ? 34.29556  0.59890   -37.60326 1.000 38.40347  ?  255 LEU   I CB  1 
ATOM   1595  C CG  . LEU   A  1 255 ? 32.92002  0.11777   -38.05860 1.000 39.67543  ?  255 LEU   I CG  1 
ATOM   1596  C CD1 . LEU   A  1 255 ? 32.16179  1.20019   -38.80814 1.000 38.46180  ?  255 LEU   I CD1 1 
ATOM   1597  C CD2 . LEU   A  1 255 ? 33.07526  -1.12436  -38.91013 1.000 28.29241  ?  255 LEU   I CD2 1 
ATOM   1598  N N   . ASP   A  1 256 ? 37.36836  -0.02718  -36.92410 1.000 37.75948  ?  256 ASP   I N   1 
ATOM   1599  C CA  . ASP   A  1 256 ? 38.63229  0.54894   -36.47441 1.000 23.13281  ?  256 ASP   I CA  1 
ATOM   1600  C C   . ASP   A  1 256 ? 38.72482  2.04172   -36.79257 1.000 45.66866  ?  256 ASP   I C   1 
ATOM   1601  O O   . ASP   A  1 256 ? 39.33614  2.78343   -36.01061 1.000 25.67144  ?  256 ASP   I O   1 
ATOM   1602  C CB  . ASP   A  1 256 ? 39.81159  -0.22296  -37.07190 1.000 33.15805  ?  256 ASP   I CB  1 
ATOM   1603  C CG  . ASP   A  1 256 ? 39.94147  -1.63100  -36.48941 1.000 59.88200  ?  256 ASP   I CG  1 
ATOM   1604  O OD1 . ASP   A  1 256 ? 40.32551  -1.80814  -35.30166 1.000 33.69206  ?  256 ASP   I OD1 1 
ATOM   1605  O OD2 . ASP   A  1 256 ? 39.64699  -2.57778  -37.22962 1.000 34.37231  ?  256 ASP   I OD2 1 
ATOM   1606  N N   . THR   A  1 257 ? 38.11699  2.49931   -37.90079 1.000 29.56781  ?  257 THR   I N   1 
ATOM   1607  C CA  . THR   A  1 257 ? 37.98193  3.92087   -38.20659 1.000 57.75849  ?  257 THR   I CA  1 
ATOM   1608  C C   . THR   A  1 257 ? 36.58972  4.19708   -38.75066 1.000 23.87579  ?  257 THR   I C   1 
ATOM   1609  O O   . THR   A  1 257 ? 35.91373  3.30261   -39.26574 1.000 45.85429  ?  257 THR   I O   1 
ATOM   1610  C CB  . THR   A  1 257 ? 39.00998  4.39455   -39.24156 1.000 30.91069  ?  257 THR   I CB  1 
ATOM   1611  O OG1 . THR   A  1 257 ? 38.85313  3.63128   -40.44643 1.000 53.62327  ?  257 THR   I OG1 1 
ATOM   1612  C CG2 . THR   A  1 257 ? 40.39128  4.20993   -38.73012 1.000 42.49653  ?  257 THR   I CG2 1 
ATOM   1613  N N   . LEU   A  1 258 ? 36.18770  5.46526   -38.66551 1.000 45.00661  ?  258 LEU   I N   1 
ATOM   1614  C CA  . LEU   A  1 258 ? 34.90061  5.91920   -39.20955 1.000 30.45197  ?  258 LEU   I CA  1 
ATOM   1615  C C   . LEU   A  1 258 ? 35.12766  6.66108   -40.52705 1.000 57.68955  ?  258 LEU   I C   1 
ATOM   1616  O O   . LEU   A  1 258 ? 34.95314  7.88621   -40.64405 1.000 60.99857  ?  258 LEU   I O   1 
ATOM   1617  C CB  . LEU   A  1 258 ? 34.17772  6.81079   -38.20014 1.000 30.58245  ?  258 LEU   I CB  1 
ATOM   1618  C CG  . LEU   A  1 258 ? 34.19332  6.32946   -36.75727 1.000 26.44042  ?  258 LEU   I CG  1 
ATOM   1619  C CD1 . LEU   A  1 258 ? 33.57781  7.40241   -35.91036 1.000 33.62983  ?  258 LEU   I CD1 1 
ATOM   1620  C CD2 . LEU   A  1 258 ? 33.46596  4.99242   -36.59800 1.000 22.85304  ?  258 LEU   I CD2 1 
ATOM   1621  N N   . VAL   A  1 259 ? 35.54433  5.88721   -41.52648 1.000 45.83744  ?  259 VAL   I N   1 
ATOM   1622  C CA  . VAL   A  1 259 ? 35.93338  6.39767   -42.83832 1.000 49.17516  ?  259 VAL   I CA  1 
ATOM   1623  C C   . VAL   A  1 259 ? 35.31030  5.49683   -43.88636 1.000 113.32358 ?  259 VAL   I C   1 
ATOM   1624  O O   . VAL   A  1 259 ? 35.45214  4.26513   -43.80467 1.000 44.83050  ?  259 VAL   I O   1 
ATOM   1625  C CB  . VAL   A  1 259 ? 37.46131  6.40407   -43.05618 1.000 68.85436  ?  259 VAL   I CB  1 
ATOM   1626  C CG1 . VAL   A  1 259 ? 37.81648  7.27304   -44.24879 1.000 30.98209  ?  259 VAL   I CG1 1 
ATOM   1627  C CG2 . VAL   A  1 259 ? 38.25092  6.78670   -41.80186 1.000 55.35960  ?  259 VAL   I CG2 1 
ATOM   1628  N N   . PHE   A  1 260 ? 34.65583  6.10691   -44.88686 1.000 36.86112  ?  260 PHE   I N   1 
ATOM   1629  C CA  . PHE   A  1 260 ? 34.17270  5.40308   -46.08075 1.000 97.39434  ?  260 PHE   I CA  1 
ATOM   1630  C C   . PHE   A  1 260 ? 33.10840  4.38924   -45.72737 1.000 54.47250  ?  260 PHE   I C   1 
ATOM   1631  O O   . PHE   A  1 260 ? 32.72886  3.55625   -46.56077 1.000 130.81049 ?  260 PHE   I O   1 
ATOM   1632  C CB  . PHE   A  1 260 ? 35.29732  4.67716   -46.85050 1.000 49.97313  ?  260 PHE   I CB  1 
ATOM   1633  C CG  . PHE   A  1 260 ? 36.37161  5.58384   -47.37242 1.000 67.69802  ?  260 PHE   I CG  1 
ATOM   1634  C CD1 . PHE   A  1 260 ? 36.05297  6.83210   -47.87724 1.000 45.24603  ?  260 PHE   I CD1 1 
ATOM   1635  C CD2 . PHE   A  1 260 ? 37.69841  5.18951   -47.35500 1.000 60.86612  ?  260 PHE   I CD2 1 
ATOM   1636  C CE1 . PHE   A  1 260 ? 37.03519  7.68020   -48.35430 1.000 144.25962 ?  260 PHE   I CE1 1 
ATOM   1637  C CE2 . PHE   A  1 260 ? 38.69074  6.03593   -47.83555 1.000 62.40840  ?  260 PHE   I CE2 1 
ATOM   1638  C CZ  . PHE   A  1 260 ? 38.35356  7.28636   -48.33584 1.000 79.09064  ?  260 PHE   I CZ  1 
ATOM   1639  N N   . LYS   A  1 261 ? 32.69279  4.33895   -44.53671 1.000 92.47902  ?  261 LYS   I N   1 
ATOM   1640  C CA  . LYS   A  1 261 ? 31.45333  3.64524   -44.29020 1.000 111.42880 ?  261 LYS   I CA  1 
ATOM   1641  C C   . LYS   A  1 261 ? 30.84535  4.56534   -43.22373 1.000 107.62198 ?  261 LYS   I C   1 
ATOM   1642  O O   . LYS   A  1 261 ? 31.05603  4.36558   -42.02485 1.000 132.52483 ?  261 LYS   I O   1 
ATOM   1643  C CB  . LYS   A  1 261 ? 31.65628  2.17644   -43.91036 1.000 78.08119  ?  261 LYS   I CB  1 
ATOM   1644  C CG  . LYS   A  1 261 ? 30.46245  1.24741   -44.28237 1.000 38.24504  ?  261 LYS   I CG  1 
ATOM   1645  C CD  . LYS   A  1 261 ? 30.53718  0.08444   -43.26082 1.000 110.40859 ?  261 LYS   I CD  1 
ATOM   1646  C CE  . LYS   A  1 261 ? 29.94353  -1.23391  -43.73430 1.000 96.20562  ?  261 LYS   I CE  1 
ATOM   1647  N NZ  . LYS   A  1 261 ? 29.16351  -1.94586  -42.67731 1.000 59.28224  ?  261 LYS   I NZ  1 
ATOM   1648  N N   . GLY   A  1 262 ? 30.42046  5.71002   -43.79106 1.000 94.33128  ?  262 GLY   I N   1 
ATOM   1649  C CA  . GLY   A  1 262 ? 29.51966  6.67872   -43.19597 1.000 38.92502  ?  262 GLY   I CA  1 
ATOM   1650  C C   . GLY   A  1 262 ? 28.14492  6.11154   -42.95459 1.000 95.78663  ?  262 GLY   I C   1 
ATOM   1651  O O   . GLY   A  1 262 ? 27.64862  5.29862   -43.72794 1.000 89.11057  ?  262 GLY   I O   1 
ATOM   1652  N N   . GLU   A  1 263 ? 27.54335  6.51209   -41.84761 1.000 53.98830  ?  263 GLU   I N   1 
ATOM   1653  C CA  . GLU   A  1 263 ? 26.18321  6.07137   -41.52598 1.000 88.39046  ?  263 GLU   I CA  1 
ATOM   1654  C C   . GLU   A  1 263 ? 26.16648  4.58295   -41.18590 1.000 98.49634  ?  263 GLU   I C   1 
ATOM   1655  O O   . GLU   A  1 263 ? 25.19264  3.86794   -41.46991 1.000 63.32725  ?  263 GLU   I O   1 
ATOM   1656  C CB  . GLU   A  1 263 ? 25.18872  6.39406   -42.66074 1.000 52.41038  ?  263 GLU   I CB  1 
ATOM   1657  C CG  . GLU   A  1 263 ? 23.78174  6.77777   -42.21905 1.000 88.04162  ?  263 GLU   I CG  1 
ATOM   1658  C CD  . GLU   A  1 263 ? 23.69719  8.18197   -41.56005 1.000 81.29075  ?  263 GLU   I CD  1 
ATOM   1659  O OE1 . GLU   A  1 263 ? 24.75858  8.81500   -41.33449 1.000 51.63715  ?  263 GLU   I OE1 1 
ATOM   1660  O OE2 . GLU   A  1 263 ? 22.56272  8.65327   -41.26532 1.000 65.47085  ?  263 GLU   I OE2 1 
ATOM   1661  N N   . THR   A  1 264 ? 27.27475  4.12133   -40.59715 1.000 43.82816  ?  264 THR   I N   1 
ATOM   1662  C CA  . THR   A  1 264 ? 27.35835  2.83639   -39.92466 1.000 29.35727  ?  264 THR   I CA  1 
ATOM   1663  C C   . THR   A  1 264 ? 27.70902  3.06975   -38.46513 1.000 44.60600  ?  264 THR   I C   1 
ATOM   1664  O O   . THR   A  1 264 ? 28.56368  3.90444   -38.15641 1.000 35.68640  ?  264 THR   I O   1 
ATOM   1665  C CB  . THR   A  1 264 ? 28.43376  1.96407   -40.54726 1.000 50.20318  ?  264 THR   I CB  1 
ATOM   1666  O OG1 . THR   A  1 264 ? 28.24241  1.91960   -41.96285 1.000 101.27402 ?  264 THR   I OG1 1 
ATOM   1667  C CG2 . THR   A  1 264 ? 28.39385  0.56315   -39.94164 1.000 37.19089  ?  264 THR   I CG2 1 
ATOM   1668  N N   . TYR   A  1 265 ? 27.05856  2.34092   -37.56402 1.000 35.13089  ?  265 TYR   I N   1 
ATOM   1669  C CA  . TYR   A  1 265 ? 27.49769  2.38085   -36.17549 1.000 25.64514  ?  265 TYR   I CA  1 
ATOM   1670  C C   . TYR   A  1 265 ? 28.80961  1.62442   -36.01071 1.000 30.48387  ?  265 TYR   I C   1 
ATOM   1671  O O   . TYR   A  1 265 ? 29.09203  0.65306   -36.72608 1.000 38.50316  ?  265 TYR   I O   1 
ATOM   1672  C CB  . TYR   A  1 265 ? 26.46073  1.76855   -35.23003 1.000 21.71959  ?  265 TYR   I CB  1 
ATOM   1673  C CG  . TYR   A  1 265 ? 25.09437  2.39899   -35.28621 1.000 40.57779  ?  265 TYR   I CG  1 
ATOM   1674  C CD1 . TYR   A  1 265 ? 24.89117  3.69708   -34.86290 1.000 31.92760  ?  265 TYR   I CD1 1 
ATOM   1675  C CD2 . TYR   A  1 265 ? 24.00361  1.68043   -35.74692 1.000 29.49074  ?  265 TYR   I CD2 1 
ATOM   1676  C CE1 . TYR   A  1 265 ? 23.62428  4.27259   -34.90479 1.000 39.83840  ?  265 TYR   I CE1 1 
ATOM   1677  C CE2 . TYR   A  1 265 ? 22.74736  2.23680   -35.79921 1.000 38.07279  ?  265 TYR   I CE2 1 
ATOM   1678  C CZ  . TYR   A  1 265 ? 22.55925  3.53743   -35.37787 1.000 31.98382  ?  265 TYR   I CZ  1 
ATOM   1679  O OH  . TYR   A  1 265 ? 21.29852  4.08997   -35.44099 1.000 35.31546  ?  265 TYR   I OH  1 
ATOM   1680  N N   . SER   A  1 266 ? 29.61119  2.08875   -35.04835 1.000 29.73826  ?  266 SER   I N   1 
ATOM   1681  C CA  . SER   A  1 266 ? 30.75807  1.35232   -34.52308 1.000 18.79653  ?  266 SER   I CA  1 
ATOM   1682  C C   . SER   A  1 266 ? 30.57186  1.28600   -33.00770 1.000 32.30477  ?  266 SER   I C   1 
ATOM   1683  O O   . SER   A  1 266 ? 30.75628  2.29324   -32.31439 1.000 22.84627  ?  266 SER   I O   1 
ATOM   1684  C CB  . SER   A  1 266 ? 32.07573  2.02307   -34.91179 1.000 20.55779  ?  266 SER   I CB  1 
ATOM   1685  O OG  . SER   A  1 266 ? 33.15711  1.47678   -34.17477 1.000 31.10776  ?  266 SER   I OG  1 
ATOM   1686  N N   . LEU   A  1 267 ? 30.18802  0.10642   -32.50046 1.000 22.68955  ?  267 LEU   I N   1 
ATOM   1687  C CA  . LEU   A  1 267 ? 29.88468  -0.04606  -31.07603 1.000 32.27521  ?  267 LEU   I CA  1 
ATOM   1688  C C   . LEU   A  1 267 ? 31.00375  0.49497   -30.19601 1.000 22.05394  ?  267 LEU   I C   1 
ATOM   1689  O O   . LEU   A  1 267 ? 30.75233  1.23580   -29.23807 1.000 37.65040  ?  267 LEU   I O   1 
ATOM   1690  C CB  . LEU   A  1 267 ? 29.64680  -1.51313  -30.74352 1.000 15.73293  ?  267 LEU   I CB  1 
ATOM   1691  C CG  . LEU   A  1 267 ? 28.30503  -2.14267  -31.05435 1.000 35.33331  ?  267 LEU   I CG  1 
ATOM   1692  C CD1 . LEU   A  1 267 ? 28.42243  -3.52786  -30.52404 1.000 27.40988  ?  267 LEU   I CD1 1 
ATOM   1693  C CD2 . LEU   A  1 267 ? 27.12706  -1.38312  -30.38412 1.000 21.69554  ?  267 LEU   I CD2 1 
ATOM   1694  N N   . LYS   A  1 268 ? 32.25020  0.10102   -30.50077 1.000 42.53382  ?  268 LYS   I N   1 
ATOM   1695  C CA  . LYS   A  1 268 ? 33.42616  0.57005   -29.76644 1.000 21.38946  ?  268 LYS   I CA  1 
ATOM   1696  C C   . LYS   A  1 268 ? 33.43965  2.10054   -29.64634 1.000 40.32202  ?  268 LYS   I C   1 
ATOM   1697  O O   . LYS   A  1 268 ? 33.75561  2.64151   -28.57952 1.000 19.44274  ?  268 LYS   I O   1 
ATOM   1698  C CB  . LYS   A  1 268 ? 34.68265  0.03206   -30.46923 1.000 27.79641  ?  268 LYS   I CB  1 
ATOM   1699  C CG  . LYS   A  1 268 ? 36.01292  0.68369   -30.13398 1.000 40.71135  ?  268 LYS   I CG  1 
ATOM   1700  C CD  . LYS   A  1 268 ? 37.02453  0.47513   -31.28875 1.000 34.31238  ?  268 LYS   I CD  1 
ATOM   1701  C CE  . LYS   A  1 268 ? 38.35731  1.24361   -31.03331 1.000 46.89580  ?  268 LYS   I CE  1 
ATOM   1702  N NZ  . LYS   A  1 268 ? 39.10786  1.51764   -32.33142 1.000 43.67787  ?  268 LYS   I NZ  1 
ATOM   1703  N N   . HIS   A  1 269 ? 33.05048  2.81334   -30.71491 1.000 30.53942  ?  269 HIS   I N   1 
ATOM   1704  C CA  . HIS   A  1 269 ? 32.99428  4.27501   -30.68747 1.000 15.04177  ?  269 HIS   I CA  1 
ATOM   1705  C C   . HIS   A  1 269 ? 31.73694  4.77359   -29.98591 1.000 39.97254  ?  269 HIS   I C   1 
ATOM   1706  O O   . HIS   A  1 269 ? 31.82427  5.53122   -29.01231 1.000 22.70886  ?  269 HIS   I O   1 
ATOM   1707  C CB  . HIS   A  1 269 ? 33.03755  4.84425   -32.10610 1.000 22.70403  ?  269 HIS   I CB  1 
ATOM   1708  C CG  . HIS   A  1 269 ? 34.34455  4.65021   -32.79909 1.000 26.75096  ?  269 HIS   I CG  1 
ATOM   1709  N ND1 . HIS   A  1 269 ? 34.71606  3.45291   -33.36929 1.000 48.11512  ?  269 HIS   I ND1 1 
ATOM   1710  C CD2 . HIS   A  1 269 ? 35.36877  5.50656   -33.02252 1.000 34.02597  ?  269 HIS   I CD2 1 
ATOM   1711  C CE1 . HIS   A  1 269 ? 35.91765  3.57736   -33.90640 1.000 23.33699  ?  269 HIS   I CE1 1 
ATOM   1712  N NE2 . HIS   A  1 269 ? 36.33595  4.81387   -33.70941 1.000 38.88366  ?  269 HIS   I NE2 1 
ATOM   1713  N N   . LEU   A  1 270 ? 30.55632  4.38643   -30.50070 1.000 23.70259  ?  270 LEU   I N   1 
ATOM   1714  C CA  . LEU   A  1 270 ? 29.28301  4.77499   -29.88590 1.000 18.95743  ?  270 LEU   I CA  1 
ATOM   1715  C C   . LEU   A  1 270 ? 29.33254  4.64930   -28.36145 1.000 22.64529  ?  270 LEU   I C   1 
ATOM   1716  O O   . LEU   A  1 270 ? 29.06269  5.61781   -27.63828 1.000 26.20148  ?  270 LEU   I O   1 
ATOM   1717  C CB  . LEU   A  1 270 ? 28.14213  3.92497   -30.45458 1.000 25.67881  ?  270 LEU   I CB  1 
ATOM   1718  C CG  . LEU   A  1 270 ? 26.75237  4.20497   -29.88713 1.000 22.74117  ?  270 LEU   I CG  1 
ATOM   1719  C CD1 . LEU   A  1 270 ? 26.17043  5.53702   -30.40077 1.000 20.47616  ?  270 LEU   I CD1 1 
ATOM   1720  C CD2 . LEU   A  1 270 ? 25.82195  3.03635   -30.17196 1.000 28.47141  ?  270 LEU   I CD2 1 
ATOM   1721  N N   . LEU   A  1 271 ? 29.73165  3.47894   -27.85540 1.000 27.78265  ?  271 LEU   I N   1 
ATOM   1722  C CA  . LEU   A  1 271 ? 29.77190  3.22565   -26.41822 1.000 24.40954  ?  271 LEU   I CA  1 
ATOM   1723  C C   . LEU   A  1 271 ? 31.10239  3.59791   -25.77728 1.000 32.84221  ?  271 LEU   I C   1 
ATOM   1724  O O   . LEU   A  1 271 ? 31.31597  3.27627   -24.60076 1.000 22.40448  ?  271 LEU   I O   1 
ATOM   1725  C CB  . LEU   A  1 271 ? 29.45644  1.75740   -26.12817 1.000 14.87233  ?  271 LEU   I CB  1 
ATOM   1726  C CG  . LEU   A  1 271 ? 28.11676  1.28905   -26.70668 1.000 27.96170  ?  271 LEU   I CG  1 
ATOM   1727  C CD1 . LEU   A  1 271 ? 27.97722  -0.18681  -26.42442 1.000 19.07851  ?  271 LEU   I CD1 1 
ATOM   1728  C CD2 . LEU   A  1 271 ? 26.91976  2.09419   -26.15921 1.000 12.60478  ?  271 LEU   I CD2 1 
ATOM   1729  N N   . ASN   A  1 272 ? 32.00161  4.25833   -26.51776 1.000 27.62868  ?  272 ASN   I N   1 
ATOM   1730  C CA  . ASN   A  1 272 ? 33.22915  4.82628   -25.94135 1.000 19.62917  ?  272 ASN   I CA  1 
ATOM   1731  C C   . ASN   A  1 272 ? 34.06437  3.75477   -25.22696 1.000 31.76606  ?  272 ASN   I C   1 
ATOM   1732  O O   . ASN   A  1 272 ? 34.55086  3.95547   -24.11523 1.000 38.56016  ?  272 ASN   I O   1 
ATOM   1733  C CB  . ASN   A  1 272 ? 32.89190  5.98667   -24.99494 1.000 41.53929  ?  272 ASN   I CB  1 
ATOM   1734  C CG  . ASN   A  1 272 ? 34.10730  6.81810   -24.61534 1.000 32.03029  ?  272 ASN   I CG  1 
ATOM   1735  O OD1 . ASN   A  1 272 ? 34.96478  7.13561   -25.45441 1.000 31.83412  ?  272 ASN   I OD1 1 
ATOM   1736  N ND2 . ASN   A  1 272 ? 34.18714  7.17744   -23.33569 1.000 38.26212  ?  272 ASN   I ND2 1 
ATOM   1737  N N   . ASN   A  1 273 ? 34.21066  2.59233   -25.87793 1.000 32.11265  ?  273 ASN   I N   1 
ATOM   1738  C CA  . ASN   A  1 273 ? 35.04265  1.47947   -25.39024 1.000 41.21904  ?  273 ASN   I CA  1 
ATOM   1739  C C   . ASN   A  1 273 ? 34.61519  0.97492   -24.01726 1.000 29.22828  ?  273 ASN   I C   1 
ATOM   1740  O O   . ASN   A  1 273 ? 35.45616  0.53624   -23.23092 1.000 38.02377  ?  273 ASN   I O   1 
ATOM   1741  C CB  . ASN   A  1 273 ? 36.52733  1.85456   -25.35861 1.000 35.70820  ?  273 ASN   I CB  1 
ATOM   1742  C CG  . ASN   A  1 273 ? 37.18863  1.67460   -26.69239 1.000 72.21173  ?  273 ASN   I CG  1 
ATOM   1743  O OD1 . ASN   A  1 273 ? 37.29419  0.54805   -27.19240 1.000 77.64859  ?  273 ASN   I OD1 1 
ATOM   1744  N ND2 . ASN   A  1 273 ? 37.62577  2.78165   -27.29670 1.000 74.87310  ?  273 ASN   I ND2 1 
ATOM   1745  N N   . ASP   A  1 274 ? 33.31763  1.00831   -23.71078 1.000 34.93777  ?  274 ASP   I N   1 
ATOM   1746  C CA  . ASP   A  1 274 ? 32.87954  0.53109   -22.40366 1.000 32.15635  ?  274 ASP   I CA  1 
ATOM   1747  C C   . ASP   A  1 274 ? 33.15798  -0.96648  -22.26095 1.000 26.55390  ?  274 ASP   I C   1 
ATOM   1748  O O   . ASP   A  1 274 ? 33.02967  -1.72183  -23.23789 1.000 27.38348  ?  274 ASP   I O   1 
ATOM   1749  C CB  . ASP   A  1 274 ? 31.38687  0.80135   -22.19270 1.000 28.74720  ?  274 ASP   I CB  1 
ATOM   1750  C CG  . ASP   A  1 274 ? 30.97165  0.63777   -20.74314 1.000 38.37799  ?  274 ASP   I CG  1 
ATOM   1751  O OD1 . ASP   A  1 274 ? 30.73311  -0.51338  -20.29383 1.000 46.84709  ?  274 ASP   I OD1 1 
ATOM   1752  O OD2 . ASP   A  1 274 ? 30.92300  1.67109   -20.03792 1.000 60.57057  ?  274 ASP   I OD2 1 
ATOM   1753  N N   . PRO   A  1 275 ? 33.52069  -1.43660  -21.06448 1.000 39.45393  ?  275 PRO   I N   1 
ATOM   1754  C CA  . PRO   A  1 275 ? 33.60160  -2.89523  -20.84125 1.000 19.42692  ?  275 PRO   I CA  1 
ATOM   1755  C C   . PRO   A  1 275 ? 32.36036  -3.67309  -21.26961 1.000 29.02870  ?  275 PRO   I C   1 
ATOM   1756  O O   . PRO   A  1 275 ? 32.51231  -4.82729  -21.68249 1.000 42.34406  ?  275 PRO   I O   1 
ATOM   1757  C CB  . PRO   A  1 275 ? 33.85024  -3.00731  -19.33378 1.000 21.65284  ?  275 PRO   I CB  1 
ATOM   1758  C CG  . PRO   A  1 275 ? 34.49876  -1.70351  -18.96867 1.000 23.69925  ?  275 PRO   I CG  1 
ATOM   1759  C CD  . PRO   A  1 275 ? 33.93747  -0.65789  -19.88877 1.000 27.63625  ?  275 PRO   I CD  1 
ATOM   1760  N N   . PHE   A  1 276 ? 31.14745  -3.08769  -21.22499 1.000 33.96551  ?  276 PHE   I N   1 
ATOM   1761  C CA  . PHE   A  1 276 ? 29.95586  -3.79628  -21.71284 1.000 24.29798  ?  276 PHE   I CA  1 
ATOM   1762  C C   . PHE   A  1 276 ? 29.91087  -3.94371  -23.23038 1.000 41.38859  ?  276 PHE   I C   1 
ATOM   1763  O O   . PHE   A  1 276 ? 29.09075  -4.72744  -23.72954 1.000 37.24688  ?  276 PHE   I O   1 
ATOM   1764  C CB  . PHE   A  1 276 ? 28.66378  -3.09928  -21.28475 1.000 25.53623  ?  276 PHE   I CB  1 
ATOM   1765  C CG  . PHE   A  1 276 ? 28.43837  -3.08062  -19.80498 1.000 41.04864  ?  276 PHE   I CG  1 
ATOM   1766  C CD1 . PHE   A  1 276 ? 28.84674  -4.13499  -19.01005 1.000 34.05538  ?  276 PHE   I CD1 1 
ATOM   1767  C CD2 . PHE   A  1 276 ? 27.80674  -2.00123  -19.20658 1.000 31.12156  ?  276 PHE   I CD2 1 
ATOM   1768  C CE1 . PHE   A  1 276 ? 28.62061  -4.11163  -17.64036 1.000 45.83482  ?  276 PHE   I CE1 1 
ATOM   1769  C CE2 . PHE   A  1 276 ? 27.58207  -1.96498  -17.83690 1.000 49.64779  ?  276 PHE   I CE2 1 
ATOM   1770  C CZ  . PHE   A  1 276 ? 27.99254  -3.01657  -17.05307 1.000 40.14253  ?  276 PHE   I CZ  1 
ATOM   1771  N N   . THR   A  1 277 ? 30.74576  -3.21102  -23.97017 1.000 31.94383  ?  277 THR   I N   1 
ATOM   1772  C CA  . THR   A  1 277 ? 30.65476  -3.20740  -25.43137 1.000 37.66752  ?  277 THR   I CA  1 
ATOM   1773  C C   . THR   A  1 277 ? 30.55576  -4.59813  -26.05072 1.000 29.24472  ?  277 THR   I C   1 
ATOM   1774  O O   . THR   A  1 277 ? 29.70403  -4.78862  -26.93146 1.000 35.30585  ?  277 THR   I O   1 
ATOM   1775  C CB  . THR   A  1 277 ? 31.84945  -2.44474  -26.02472 1.000 26.41145  ?  277 THR   I CB  1 
ATOM   1776  O OG1 . THR   A  1 277 ? 31.93429  -1.15044  -25.42057 1.000 32.64809  ?  277 THR   I OG1 1 
ATOM   1777  C CG2 . THR   A  1 277 ? 31.68051  -2.26917  -27.52833 1.000 16.40708  ?  277 THR   I CG2 1 
ATOM   1778  N N   . PRO   A  1 278 ? 31.35957  -5.59670  -25.65453 1.000 54.62596  ?  278 PRO   I N   1 
ATOM   1779  C CA  . PRO   A  1 278 ? 31.26340  -6.90550  -26.32674 1.000 27.31805  ?  278 PRO   I CA  1 
ATOM   1780  C C   . PRO   A  1 278 ? 29.88752  -7.54466  -26.23519 1.000 41.32497  ?  278 PRO   I C   1 
ATOM   1781  O O   . PRO   A  1 278 ? 29.50854  -8.27667  -27.16069 1.000 29.88741  ?  278 PRO   I O   1 
ATOM   1782  C CB  . PRO   A  1 278 ? 32.31414  -7.75823  -25.60077 1.000 20.05325  ?  278 PRO   I CB  1 
ATOM   1783  C CG  . PRO   A  1 278 ? 33.22437  -6.81652  -24.96717 1.000 23.82812  ?  278 PRO   I CG  1 
ATOM   1784  C CD  . PRO   A  1 278 ? 32.42538  -5.59062  -24.63490 1.000 26.73805  ?  278 PRO   I CD  1 
ATOM   1785  N N   . GLN   A  1 279 ? 29.12936  -7.29230  -25.15202 1.000 32.36719  ?  279 GLN   I N   1 
ATOM   1786  C CA  . GLN   A  1 279 ? 27.80169  -7.89406  -24.99531 1.000 30.18136  ?  279 GLN   I CA  1 
ATOM   1787  C C   . GLN   A  1 279 ? 26.82290  -7.46000  -26.08642 1.000 43.58347  ?  279 GLN   I C   1 
ATOM   1788  O O   . GLN   A  1 279 ? 25.83153  -8.16434  -26.33285 1.000 41.97458  ?  279 GLN   I O   1 
ATOM   1789  C CB  . GLN   A  1 279 ? 27.20647  -7.55308  -23.62217 1.000 27.61901  ?  279 GLN   I CB  1 
ATOM   1790  C CG  . GLN   A  1 279 ? 27.99341  -8.08827  -22.42606 1.000 19.12158  ?  279 GLN   I CG  1 
ATOM   1791  C CD  . GLN   A  1 279 ? 27.25687  -7.90788  -21.10705 1.000 58.64772  ?  279 GLN   I CD  1 
ATOM   1792  O OE1 . GLN   A  1 279 ? 26.07725  -8.25438  -20.98117 1.000 44.47866  ?  279 GLN   I OE1 1 
ATOM   1793  N NE2 . GLN   A  1 279 ? 27.95390  -7.36593  -20.11549 1.000 35.50256  ?  279 GLN   I NE2 1 
ATOM   1794  N N   . PHE   A  1 280 ? 27.07422  -6.31856  -26.73492 1.000 31.59362  ?  280 PHE   I N   1 
ATOM   1795  C CA  . PHE   A  1 280 ? 26.17951  -5.76718  -27.74228 1.000 33.17142  ?  280 PHE   I CA  1 
ATOM   1796  C C   . PHE   A  1 280 ? 26.66036  -6.04000  -29.15048 1.000 31.49386  ?  280 PHE   I C   1 
ATOM   1797  O O   . PHE   A  1 280 ? 25.97391  -5.66269  -30.11290 1.000 34.16735  ?  280 PHE   I O   1 
ATOM   1798  C CB  . PHE   A  1 280 ? 25.98959  -4.26300  -27.51306 1.000 15.08516  ?  280 PHE   I CB  1 
ATOM   1799  C CG  . PHE   A  1 280 ? 25.18492  -3.97879  -26.30080 1.000 45.01099  ?  280 PHE   I CG  1 
ATOM   1800  C CD1 . PHE   A  1 280 ? 23.79252  -3.96987  -26.35948 1.000 25.71106  ?  280 PHE   I CD1 1 
ATOM   1801  C CD2 . PHE   A  1 280 ? 25.80630  -3.82416  -25.07483 1.000 16.03528  ?  280 PHE   I CD2 1 
ATOM   1802  C CE1 . PHE   A  1 280 ? 23.04801  -3.75641  -25.21541 1.000 40.42855  ?  280 PHE   I CE1 1 
ATOM   1803  C CE2 . PHE   A  1 280 ? 25.06128  -3.60833  -23.92608 1.000 39.73984  ?  280 PHE   I CE2 1 
ATOM   1804  C CZ  . PHE   A  1 280 ? 23.68171  -3.57749  -23.99788 1.000 32.11419  ?  280 PHE   I CZ  1 
ATOM   1805  N N   . GLU   A  1 281 ? 27.81593  -6.68870  -29.28782 1.000 31.80809  ?  281 GLU   I N   1 
ATOM   1806  C CA  . GLU   A  1 281 ? 28.26674  -7.15172  -30.58806 1.000 44.65227  ?  281 GLU   I CA  1 
ATOM   1807  C C   . GLU   A  1 281 ? 27.20215  -8.05761  -31.20493 1.000 21.89964  ?  281 GLU   I C   1 
ATOM   1808  O O   . GLU   A  1 281 ? 26.64822  -8.92561  -30.52491 1.000 41.59703  ?  281 GLU   I O   1 
ATOM   1809  C CB  . GLU   A  1 281 ? 29.60008  -7.88071  -30.42520 1.000 25.16768  ?  281 GLU   I CB  1 
ATOM   1810  C CG  . GLU   A  1 281 ? 30.52657  -7.72056  -31.60055 1.000 57.14547  ?  281 GLU   I CG  1 
ATOM   1811  C CD  . GLU   A  1 281 ? 31.12423  -6.32914  -31.69738 1.000 125.35252 ?  281 GLU   I CD  1 
ATOM   1812  O OE1 . GLU   A  1 281 ? 31.50225  -5.72752  -30.65401 1.000 44.49699  ?  281 GLU   I OE1 1 
ATOM   1813  O OE2 . GLU   A  1 281 ? 31.21956  -5.84344  -32.84292 1.000 60.47108  ?  281 GLU   I OE2 1 
ATOM   1814  N N   . HIS   A  1 282 ? 26.86979  -7.80714  -32.47572 1.000 33.66538  ?  282 HIS   I N   1 
ATOM   1815  C CA  . HIS   A  1 282 ? 25.83541  -8.50539  -33.23957 1.000 57.25077  ?  282 HIS   I CA  1 
ATOM   1816  C C   . HIS   A  1 282 ? 24.41558  -8.15345  -32.80532 1.000 44.83240  ?  282 HIS   I C   1 
ATOM   1817  O O   . HIS   A  1 282 ? 23.46456  -8.74327  -33.32920 1.000 50.05862  ?  282 HIS   I O   1 
ATOM   1818  C CB  . HIS   A  1 282 ? 25.97306  -10.02892 -33.16354 1.000 24.75818  ?  282 HIS   I CB  1 
ATOM   1819  C CG  . HIS   A  1 282 ? 27.27683  -10.54734 -33.67404 1.000 71.49735  ?  282 HIS   I CG  1 
ATOM   1820  N ND1 . HIS   A  1 282 ? 27.59367  -10.57277 -35.01617 1.000 56.20785  ?  282 HIS   I ND1 1 
ATOM   1821  C CD2 . HIS   A  1 282 ? 28.34326  -11.07024 -33.02272 1.000 31.76546  ?  282 HIS   I CD2 1 
ATOM   1822  C CE1 . HIS   A  1 282 ? 28.80414  -11.07941 -35.17033 1.000 40.10664  ?  282 HIS   I CE1 1 
ATOM   1823  N NE2 . HIS   A  1 282 ? 29.28148  -11.39037 -33.97602 1.000 52.06545  ?  282 HIS   I NE2 1 
ATOM   1824  N N   . GLY   A  1 283 ? 24.23494  -7.22245  -31.86496 1.000 45.47523  ?  283 GLY   I N   1 
ATOM   1825  C CA  . GLY   A  1 283 ? 22.91155  -6.81420  -31.42806 1.000 25.03301  ?  283 GLY   I CA  1 
ATOM   1826  C C   . GLY   A  1 283 ? 22.25590  -5.84428  -32.39365 1.000 37.20849  ?  283 GLY   I C   1 
ATOM   1827  O O   . GLY   A  1 283 ? 22.66474  -5.75268  -33.55794 1.000 36.25063  ?  283 GLY   I O   1 
ATOM   1828  N N   . SER   A  1 284 ? 21.24677  -5.10412  -31.93612 1.000 28.64828  ?  284 SER   I N   1 
ATOM   1829  C CA  . SER   A  1 284 ? 20.51799  -4.20687  -32.82810 1.000 37.35400  ?  284 SER   I CA  1 
ATOM   1830  C C   . SER   A  1 284 ? 20.33476  -2.85557  -32.15841 1.000 31.36072  ?  284 SER   I C   1 
ATOM   1831  O O   . SER   A  1 284 ? 20.34642  -2.73300  -30.92432 1.000 24.29658  ?  284 SER   I O   1 
ATOM   1832  C CB  . SER   A  1 284 ? 19.14690  -4.78582  -33.23293 1.000 20.39915  ?  284 SER   I CB  1 
ATOM   1833  O OG  . SER   A  1 284 ? 18.47577  -5.31384  -32.08844 1.000 39.11988  ?  284 SER   I OG  1 
ATOM   1834  N N   . ILE   A  1 285 ? 20.14102  -1.83975  -32.99599 1.000 22.16640  ?  285 ILE   I N   1 
ATOM   1835  C CA  . ILE   A  1 285 ? 20.04209  -0.45504  -32.55234 1.000 20.90860  ?  285 ILE   I CA  1 
ATOM   1836  C C   . ILE   A  1 285 ? 18.88723  0.20973   -33.29062 1.000 17.06612  ?  285 ILE   I C   1 
ATOM   1837  O O   . ILE   A  1 285 ? 18.79361  0.11825   -34.52285 1.000 36.06098  ?  285 ILE   I O   1 
ATOM   1838  C CB  . ILE   A  1 285 ? 21.35010  0.32850   -32.81196 1.000 24.31293  ?  285 ILE   I CB  1 
ATOM   1839  C CG1 . ILE   A  1 285 ? 22.52251  -0.19829  -31.97093 1.000 20.80251  ?  285 ILE   I CG1 1 
ATOM   1840  C CG2 . ILE   A  1 285 ? 21.12345  1.80222   -32.58965 1.000 16.74515  ?  285 ILE   I CG2 1 
ATOM   1841  C CD1 . ILE   A  1 285 ? 23.87420  0.39608   -32.37815 1.000 29.09193  ?  285 ILE   I CD1 1 
ATOM   1842  N N   . LEU   A  1 286 ? 18.02098  0.88532   -32.53702 1.000 34.02671  ?  286 LEU   I N   1 
ATOM   1843  C CA  . LEU   A  1 286 ? 17.00894  1.79202   -33.06462 1.000 16.89572  ?  286 LEU   I CA  1 
ATOM   1844  C C   . LEU   A  1 286 ? 17.39352  3.21106   -32.66283 1.000 23.79568  ?  286 LEU   I C   1 
ATOM   1845  O O   . LEU   A  1 286 ? 17.69781  3.45975   -31.48800 1.000 28.51060  ?  286 LEU   I O   1 
ATOM   1846  C CB  . LEU   A  1 286 ? 15.60829  1.43644   -32.52302 1.000 32.08204  ?  286 LEU   I CB  1 
ATOM   1847  C CG  . LEU   A  1 286 ? 14.57844  2.58564   -32.54085 1.000 27.74438  ?  286 LEU   I CG  1 
ATOM   1848  C CD1 . LEU   A  1 286 ? 14.18888  2.92523   -33.95839 1.000 22.70453  ?  286 LEU   I CD1 1 
ATOM   1849  C CD2 . LEU   A  1 286 ? 13.33310  2.27992   -31.72642 1.000 27.94209  ?  286 LEU   I CD2 1 
ATOM   1850  N N   . GLN   A  1 287 ? 17.37191  4.13630   -33.62637 1.000 19.53174  ?  287 GLN   I N   1 
ATOM   1851  C CA  . GLN   A  1 287 ? 17.76734  5.52202   -33.39022 1.000 33.59408  ?  287 GLN   I CA  1 
ATOM   1852  C C   . GLN   A  1 287 ? 16.66274  6.46750   -33.85052 1.000 34.27417  ?  287 GLN   I C   1 
ATOM   1853  O O   . GLN   A  1 287 ? 16.15550  6.34632   -34.97536 1.000 27.84174  ?  287 GLN   I O   1 
ATOM   1854  C CB  . GLN   A  1 287 ? 19.08702  5.86663   -34.10736 1.000 22.63776  ?  287 GLN   I CB  1 
ATOM   1855  C CG  . GLN   A  1 287 ? 19.50610  7.32014   -33.94895 1.000 30.54733  ?  287 GLN   I CG  1 
ATOM   1856  C CD  . GLN   A  1 287 ? 20.90418  7.62672   -34.47821 1.000 27.80748  ?  287 GLN   I CD  1 
ATOM   1857  O OE1 . GLN   A  1 287 ? 21.55422  6.78676   -35.10572 1.000 29.94608  ?  287 GLN   I OE1 1 
ATOM   1858  N NE2 . GLN   A  1 287 ? 21.37229  8.85117   -34.22328 1.000 23.92331  ?  287 GLN   I NE2 1 
ATOM   1859  N N   . GLY   A  1 288 ? 16.30413  7.41550   -32.98271 1.000 31.35056  ?  288 GLY   I N   1 
ATOM   1860  C CA  . GLY   A  1 288 ? 15.31460  8.43346   -33.29657 1.000 23.17982  ?  288 GLY   I CA  1 
ATOM   1861  C C   . GLY   A  1 288 ? 15.87259  9.85205   -33.35112 1.000 27.79760  ?  288 GLY   I C   1 
ATOM   1862  O O   . GLY   A  1 288 ? 16.93398  10.15622  -32.79163 1.000 42.83465  ?  288 GLY   I O   1 
ATOM   1863  N N   . PHE   A  1 289 ? 15.16245  10.73078  -34.04517 1.000 35.12167  ?  289 PHE   I N   1 
ATOM   1864  C CA  . PHE   A  1 289 ? 15.51488  12.13728  -34.15852 1.000 41.67445  ?  289 PHE   I CA  1 
ATOM   1865  C C   . PHE   A  1 289 ? 14.39848  12.96218  -33.53890 1.000 36.97450  ?  289 PHE   I C   1 
ATOM   1866  O O   . PHE   A  1 289 ? 13.22523  12.74349  -33.85113 1.000 39.36743  ?  289 PHE   I O   1 
ATOM   1867  C CB  . PHE   A  1 289 ? 15.71205  12.51917  -35.62520 1.000 30.71507  ?  289 PHE   I CB  1 
ATOM   1868  C CG  . PHE   A  1 289 ? 15.71284  14.00384  -35.88423 1.000 36.39861  ?  289 PHE   I CG  1 
ATOM   1869  C CD1 . PHE   A  1 289 ? 16.66945  14.82528  -35.30344 1.000 25.18578  ?  289 PHE   I CD1 1 
ATOM   1870  C CD2 . PHE   A  1 289 ? 14.77732  14.57783  -36.73207 1.000 35.83923  ?  289 PHE   I CD2 1 
ATOM   1871  C CE1 . PHE   A  1 289 ? 16.68871  16.20824  -35.55944 1.000 43.82843  ?  289 PHE   I CE1 1 
ATOM   1872  C CE2 . PHE   A  1 289 ? 14.79533  15.95268  -36.99305 1.000 39.19461  ?  289 PHE   I CE2 1 
ATOM   1873  C CZ  . PHE   A  1 289 ? 15.75705  16.76614  -36.40754 1.000 37.49440  ?  289 PHE   I CZ  1 
ATOM   1874  N N   . LEU   A  1 290 ? 14.76298  13.89319  -32.65846 1.000 33.84439  ?  290 LEU   I N   1 
ATOM   1875  C CA  . LEU   A  1 290 ? 13.81298  14.80192  -32.02628 1.000 33.21473  ?  290 LEU   I CA  1 
ATOM   1876  C C   . LEU   A  1 290 ? 13.80247  16.12985  -32.78817 1.000 37.58278  ?  290 LEU   I C   1 
ATOM   1877  O O   . LEU   A  1 290 ? 14.84453  16.78418  -32.89030 1.000 57.20839  ?  290 LEU   I O   1 
ATOM   1878  C CB  . LEU   A  1 290 ? 14.19157  15.02341  -30.55846 1.000 26.35205  ?  290 LEU   I CB  1 
ATOM   1879  C CG  . LEU   A  1 290 ? 14.12742  13.89517  -29.50960 1.000 34.10582  ?  290 LEU   I CG  1 
ATOM   1880  C CD1 . LEU   A  1 290 ? 15.24242  12.87146  -29.68758 1.000 31.75328  ?  290 LEU   I CD1 1 
ATOM   1881  C CD2 . LEU   A  1 290 ? 14.14506  14.44093  -28.06666 1.000 26.17571  ?  290 LEU   I CD2 1 
ATOM   1882  N N   . ASN   A  1 291 ? 12.63557  16.53161  -33.32024 1.000 44.71562  ?  291 ASN   I N   1 
ATOM   1883  C CA  . ASN   A  1 291 ? 12.49487  17.85513  -33.95216 1.000 32.13662  ?  291 ASN   I CA  1 
ATOM   1884  C C   . ASN   A  1 291 ? 12.74779  18.95993  -32.93899 1.000 36.65683  ?  291 ASN   I C   1 
ATOM   1885  O O   . ASN   A  1 291 ? 12.71718  18.74623  -31.72050 1.000 36.27473  ?  291 ASN   I O   1 
ATOM   1886  C CB  . ASN   A  1 291 ? 11.09282  18.09600  -34.52854 1.000 59.19520  ?  291 ASN   I CB  1 
ATOM   1887  C CG  . ASN   A  1 291 ? 10.49217  16.86579  -35.12895 1.000 70.16479  ?  291 ASN   I CG  1 
ATOM   1888  O OD1 . ASN   A  1 291 ? 9.95645   16.01066  -34.41698 1.000 115.96732 ?  291 ASN   I OD1 1 
ATOM   1889  N ND2 . ASN   A  1 291 ? 10.57258  16.75697  -36.44894 1.000 70.88048  ?  291 ASN   I ND2 1 
ATOM   1890  N N   . VAL   A  1 292 ? 12.95438  20.17418  -33.45499 1.000 38.70783  ?  292 VAL   I N   1 
ATOM   1891  C CA  . VAL   A  1 292 ? 13.27137  21.26487  -32.54286 1.000 66.67991  ?  292 VAL   I CA  1 
ATOM   1892  C C   . VAL   A  1 292 ? 12.07928  21.59865  -31.65194 1.000 67.42079  ?  292 VAL   I C   1 
ATOM   1893  O O   . VAL   A  1 292 ? 12.25980  22.07368  -30.52153 1.000 49.79573  ?  292 VAL   I O   1 
ATOM   1894  C CB  . VAL   A  1 292 ? 13.76247  22.49569  -33.31513 1.000 64.99987  ?  292 VAL   I CB  1 
ATOM   1895  C CG1 . VAL   A  1 292 ? 14.57751  23.38008  -32.37176 1.000 57.85823  ?  292 VAL   I CG1 1 
ATOM   1896  C CG2 . VAL   A  1 292 ? 14.56906  22.06371  -34.55812 1.000 49.77748  ?  292 VAL   I CG2 1 
ATOM   1897  N N   . THR   A  1 293 ? 10.85438  21.32967  -32.11433 1.000 44.34332  ?  293 THR   I N   1 
ATOM   1898  C CA  . THR   A  1 293 ? 9.65219   21.60865  -31.33321 1.000 50.73219  ?  293 THR   I CA  1 
ATOM   1899  C C   . THR   A  1 293 ? 9.16786   20.42853  -30.48589 1.000 77.99436  ?  293 THR   I C   1 
ATOM   1900  O O   . THR   A  1 293 ? 8.08149   20.51538  -29.90094 1.000 65.24409  ?  293 THR   I O   1 
ATOM   1901  C CB  . THR   A  1 293 ? 8.50376   22.02615  -32.25226 1.000 75.30398  ?  293 THR   I CB  1 
ATOM   1902  O OG1 . THR   A  1 293 ? 8.26284   20.99316  -33.23174 1.000 53.32764  ?  293 THR   I OG1 1 
ATOM   1903  C CG2 . THR   A  1 293 ? 8.81993   23.34298  -32.92133 1.000 44.00128  ?  293 THR   I CG2 1 
ATOM   1904  N N   . ALA   A  1 294 ? 9.92101   19.33378  -30.41207 1.000 38.62524  ?  294 ALA   I N   1 
ATOM   1905  C CA  . ALA   A  1 294 ? 9.42802   18.15081  -29.72338 1.000 31.98181  ?  294 ALA   I CA  1 
ATOM   1906  C C   . ALA   A  1 294 ? 9.66602   18.23134  -28.21062 1.000 31.43049  ?  294 ALA   I C   1 
ATOM   1907  O O   . ALA   A  1 294 ? 10.47454  19.01397  -27.70169 1.000 48.90558  ?  294 ALA   I O   1 
ATOM   1908  C CB  . ALA   A  1 294 ? 10.07097  16.87987  -30.28797 1.000 30.33017  ?  294 ALA   I CB  1 
ATOM   1909  N N   . TYR   A  1 295 ? 8.89189   17.43485  -27.49106 1.000 38.70164  ?  295 TYR   I N   1 
ATOM   1910  C CA  . TYR   A  1 295 ? 9.17182   17.18001  -26.09224 1.000 46.14839  ?  295 TYR   I CA  1 
ATOM   1911  C C   . TYR   A  1 295 ? 10.59772  16.64645  -25.97489 1.000 44.07509  ?  295 TYR   I C   1 
ATOM   1912  O O   . TYR   A  1 295 ? 10.99714  15.74809  -26.72041 1.000 41.00020  ?  295 TYR   I O   1 
ATOM   1913  C CB  . TYR   A  1 295 ? 8.12522   16.18371  -25.59021 1.000 19.35904  ?  295 TYR   I CB  1 
ATOM   1914  C CG  . TYR   A  1 295 ? 8.23777   15.66495  -24.17605 1.000 49.15325  ?  295 TYR   I CG  1 
ATOM   1915  C CD1 . TYR   A  1 295 ? 7.62641   16.33396  -23.10214 1.000 37.40753  ?  295 TYR   I CD1 1 
ATOM   1916  C CD2 . TYR   A  1 295 ? 8.87918   14.45900  -23.92255 1.000 33.27097  ?  295 TYR   I CD2 1 
ATOM   1917  C CE1 . TYR   A  1 295 ? 7.70288   15.82427  -21.79589 1.000 30.30568  ?  295 TYR   I CE1 1 
ATOM   1918  C CE2 . TYR   A  1 295 ? 8.96293   13.94443  -22.64326 1.000 28.32854  ?  295 TYR   I CE2 1 
ATOM   1919  C CZ  . TYR   A  1 295 ? 8.37522   14.62261  -21.57552 1.000 42.61672  ?  295 TYR   I CZ  1 
ATOM   1920  O OH  . TYR   A  1 295 ? 8.47238   14.09381  -20.29840 1.000 33.62315  ?  295 TYR   I OH  1 
ATOM   1921  N N   . HIS   A  1 296 ? 11.39458  17.22722  -25.07758 1.000 34.25747  ?  296 HIS   I N   1 
ATOM   1922  C CA  . HIS   A  1 296 ? 12.81810  16.89617  -25.03118 1.000 42.48572  ?  296 HIS   I CA  1 
ATOM   1923  C C   . HIS   A  1 296 ? 13.25250  16.20444  -23.73739 1.000 27.07429  ?  296 HIS   I C   1 
ATOM   1924  O O   . HIS   A  1 296 ? 14.45108  16.21176  -23.41154 1.000 32.97485  ?  296 HIS   I O   1 
ATOM   1925  C CB  . HIS   A  1 296 ? 13.67076  18.14778  -25.28698 1.000 31.47278  ?  296 HIS   I CB  1 
ATOM   1926  C CG  . HIS   A  1 296 ? 14.10705  18.27906  -26.71812 1.000 41.36658  ?  296 HIS   I CG  1 
ATOM   1927  N ND1 . HIS   A  1 296 ? 13.28414  18.78062  -27.70332 1.000 49.18248  ?  296 HIS   I ND1 1 
ATOM   1928  C CD2 . HIS   A  1 296 ? 15.25413  17.91397  -27.34012 1.000 40.81289  ?  296 HIS   I CD2 1 
ATOM   1929  C CE1 . HIS   A  1 296 ? 13.90922  18.73432  -28.86601 1.000 41.21496  ?  296 HIS   I CE1 1 
ATOM   1930  N NE2 . HIS   A  1 296 ? 15.10838  18.21536  -28.67310 1.000 55.12115  ?  296 HIS   I NE2 1 
ATOM   1931  N N   . ARG   A  1 297 ? 12.32957  15.58207  -23.00480 1.000 29.83910  ?  297 ARG   I N   1 
ATOM   1932  C CA  . ARG   A  1 297 ? 12.74753  14.80439  -21.84585 1.000 25.26397  ?  297 ARG   I CA  1 
ATOM   1933  C C   . ARG   A  1 297 ? 12.91609  13.33900  -22.22893 1.000 42.24125  ?  297 ARG   I C   1 
ATOM   1934  O O   . ARG   A  1 297 ? 12.48728  12.90231  -23.30009 1.000 31.88735  ?  297 ARG   I O   1 
ATOM   1935  C CB  . ARG   A  1 297 ? 11.75339  14.93830  -20.70429 1.000 29.14526  ?  297 ARG   I CB  1 
ATOM   1936  C CG  . ARG   A  1 297 ? 11.38116  16.36300  -20.38358 1.000 34.16458  ?  297 ARG   I CG  1 
ATOM   1937  C CD  . ARG   A  1 297 ? 10.48987  16.37279  -19.15745 1.000 31.02829  ?  297 ARG   I CD  1 
ATOM   1938  N NE  . ARG   A  1 297 ? 10.89025  17.42148  -18.22757 1.000 48.53525  ?  297 ARG   I NE  1 
ATOM   1939  C CZ  . ARG   A  1 297 ? 11.45147  17.18866  -17.05131 1.000 40.85566  ?  297 ARG   I CZ  1 
ATOM   1940  N NH1 . ARG   A  1 297 ? 11.63348  15.94909  -16.60797 1.000 49.23083  ?  297 ARG   I NH1 1 
ATOM   1941  N NH2 . ARG   A  1 297 ? 11.83257  18.22067  -16.30034 1.000 84.53281  ?  297 ARG   I NH2 1 
ATOM   1942  N N   . TRP   A  1 298 ? 13.58049  12.58752  -21.34640 1.000 28.91499  ?  298 TRP   I N   1 
ATOM   1943  C CA  . TRP   A  1 298 ? 13.82195  11.16509  -21.52809 1.000 26.76336  ?  298 TRP   I CA  1 
ATOM   1944  C C   . TRP   A  1 298 ? 12.95588  10.37892  -20.55444 1.000 34.68313  ?  298 TRP   I C   1 
ATOM   1945  O O   . TRP   A  1 298 ? 12.85451  10.73029  -19.37254 1.000 38.72082  ?  298 TRP   I O   1 
ATOM   1946  C CB  . TRP   A  1 298 ? 15.28915  10.78265  -21.27522 1.000 20.94226  ?  298 TRP   I CB  1 
ATOM   1947  C CG  . TRP   A  1 298 ? 16.34747  11.69211  -21.83226 1.000 31.67370  ?  298 TRP   I CG  1 
ATOM   1948  C CD1 . TRP   A  1 298 ? 16.24225  12.54940  -22.90086 1.000 26.94413  ?  298 TRP   I CD1 1 
ATOM   1949  C CD2 . TRP   A  1 298 ? 17.69221  11.82984  -21.33844 1.000 21.05617  ?  298 TRP   I CD2 1 
ATOM   1950  N NE1 . TRP   A  1 298 ? 17.43674  13.22044  -23.08683 1.000 18.35306  ?  298 TRP   I NE1 1 
ATOM   1951  C CE2 . TRP   A  1 298 ? 18.34064  12.78822  -22.14758 1.000 24.65101  ?  298 TRP   I CE2 1 
ATOM   1952  C CE3 . TRP   A  1 298 ? 18.40193  11.24763  -20.27756 1.000 14.11912  ?  298 TRP   I CE3 1 
ATOM   1953  C CZ2 . TRP   A  1 298 ? 19.66562  13.17158  -21.92903 1.000 29.77656  ?  298 TRP   I CZ2 1 
ATOM   1954  C CZ3 . TRP   A  1 298 ? 19.70906  11.62098  -20.06905 1.000 36.02270  ?  298 TRP   I CZ3 1 
ATOM   1955  C CH2 . TRP   A  1 298 ? 20.33102  12.57521  -20.89001 1.000 27.57808  ?  298 TRP   I CH2 1 
ATOM   1956  N N   . HIS   A  1 299 ? 12.37159  9.29366   -21.04466 1.000 28.02858  ?  299 HIS   I N   1 
ATOM   1957  C CA  . HIS   A  1 299 ? 11.60239  8.37331   -20.22558 1.000 36.90663  ?  299 HIS   I CA  1 
ATOM   1958  C C   . HIS   A  1 299 ? 12.28376  7.01216   -20.20866 1.000 27.06166  ?  299 HIS   I C   1 
ATOM   1959  O O   . HIS   A  1 299 ? 12.97257  6.63725   -21.16444 1.000 29.15526  ?  299 HIS   I O   1 
ATOM   1960  C CB  . HIS   A  1 299 ? 10.16176  8.21964   -20.73805 1.000 16.23900  ?  299 HIS   I CB  1 
ATOM   1961  C CG  . HIS   A  1 299 ? 9.32888   9.45749   -20.59405 1.000 33.15751  ?  299 HIS   I CG  1 
ATOM   1962  N ND1 . HIS   A  1 299 ? 8.00985   9.52061   -20.99213 1.000 26.20227  ?  299 HIS   I ND1 1 
ATOM   1963  C CD2 . HIS   A  1 299 ? 9.63566   10.68372  -20.10818 1.000 26.50421  ?  299 HIS   I CD2 1 
ATOM   1964  C CE1 . HIS   A  1 299 ? 7.54098   10.73311  -20.75575 1.000 39.93248  ?  299 HIS   I CE1 1 
ATOM   1965  N NE2 . HIS   A  1 299 ? 8.50837   11.45766  -20.21915 1.000 28.29341  ?  299 HIS   I NE2 1 
ATOM   1966  N N   . ALA   A  1 300 ? 12.07388  6.27033   -19.11522 1.000 29.20502  ?  300 ALA   I N   1 
ATOM   1967  C CA  . ALA   A  1 300 ? 12.68540  4.95012   -18.97350 1.000 34.24053  ?  300 ALA   I CA  1 
ATOM   1968  C C   . ALA   A  1 300 ? 12.01917  3.96485   -19.92586 1.000 27.22543  ?  300 ALA   I C   1 
ATOM   1969  O O   . ALA   A  1 300 ? 10.78577  3.86898   -19.94649 1.000 37.42548  ?  300 ALA   I O   1 
ATOM   1970  C CB  . ALA   A  1 300 ? 12.56270  4.45246   -17.53913 1.000 22.77997  ?  300 ALA   I CB  1 
ATOM   1971  N N   . PRO   A  1 301 ? 12.78896  3.22835   -20.73473 1.000 40.46211  ?  301 PRO   I N   1 
ATOM   1972  C CA  . PRO   A  1 301 ? 12.17813  2.31785   -21.72241 1.000 26.30288  ?  301 PRO   I CA  1 
ATOM   1973  C C   . PRO   A  1 301 ? 11.72590  0.98108   -21.14800 1.000 47.08920  ?  301 PRO   I C   1 
ATOM   1974  O O   . PRO   A  1 301 ? 10.99424  0.25085   -21.83300 1.000 31.48878  ?  301 PRO   I O   1 
ATOM   1975  C CB  . PRO   A  1 301 ? 13.30359  2.12441   -22.75337 1.000 35.20063  ?  301 PRO   I CB  1 
ATOM   1976  C CG  . PRO   A  1 301 ? 14.56416  2.29025   -21.95574 1.000 32.45020  ?  301 PRO   I CG  1 
ATOM   1977  C CD  . PRO   A  1 301 ? 14.25988  3.27577   -20.83539 1.000 17.76019  ?  301 PRO   I CD  1 
ATOM   1978  N N   . VAL   A  1 302 ? 12.13989  0.64425   -19.92205 1.000 25.97284  ?  302 VAL   I N   1 
ATOM   1979  C CA  . VAL   A  1 302 ? 11.81455  -0.62184  -19.26988 1.000 50.80515  ?  302 VAL   I CA  1 
ATOM   1980  C C   . VAL   A  1 302 ? 11.73040  -0.38581  -17.76703 1.000 25.21790  ?  302 VAL   I C   1 
ATOM   1981  O O   . VAL   A  1 302 ? 12.22156  0.61676   -17.24700 1.000 41.88999  ?  302 VAL   I O   1 
ATOM   1982  C CB  . VAL   A  1 302 ? 12.86863  -1.72242  -19.54798 1.000 24.97571  ?  302 VAL   I CB  1 
ATOM   1983  C CG1 . VAL   A  1 302 ? 12.92644  -2.06226  -21.02652 1.000 49.24299  ?  302 VAL   I CG1 1 
ATOM   1984  C CG2 . VAL   A  1 302 ? 14.24469  -1.29466  -18.99915 1.000 23.66346  ?  302 VAL   I CG2 1 
ATOM   1985  N N   . ASN   A  1 303 ? 11.10550  -1.32661  -17.06008 1.000 45.03048  ?  303 ASN   I N   1 
ATOM   1986  C CA  . ASN   A  1 303 ? 11.32494  -1.42054  -15.62110 1.000 29.90231  ?  303 ASN   I CA  1 
ATOM   1987  C C   . ASN   A  1 303 ? 12.71244  -2.00419  -15.39448 1.000 49.20497  ?  303 ASN   I C   1 
ATOM   1988  O O   . ASN   A  1 303 ? 13.04437  -3.06285  -15.94628 1.000 44.70691  ?  303 ASN   I O   1 
ATOM   1989  C CB  . ASN   A  1 303 ? 10.27703  -2.31069  -14.94839 1.000 48.72954  ?  303 ASN   I CB  1 
ATOM   1990  C CG  . ASN   A  1 303 ? 8.84338   -1.88824  -15.24606 1.000 41.46868  ?  303 ASN   I CG  1 
ATOM   1991  O OD1 . ASN   A  1 303 ? 8.56995   -0.79320  -15.75390 1.000 46.17593  ?  303 ASN   I OD1 1 
ATOM   1992  N ND2 . ASN   A  1 303 ? 7.91501   -2.77116  -14.92055 1.000 44.22861  ?  303 ASN   I ND2 1 
ATOM   1993  N N   . GLY   A  1 304 ? 13.53933  -1.31947  -14.61436 1.000 37.42575  ?  304 GLY   I N   1 
ATOM   1994  C CA  . GLY   A  1 304 ? 14.87130  -1.84908  -14.41219 1.000 24.19796  ?  304 GLY   I CA  1 
ATOM   1995  C C   . GLY   A  1 304 ? 15.71670  -0.95349  -13.54068 1.000 40.72450  ?  304 GLY   I C   1 
ATOM   1996  O O   . GLY   A  1 304 ? 15.23699  0.01810   -12.94474 1.000 43.54024  ?  304 GLY   I O   1 
ATOM   1997  N N   . THR   A  1 305 ? 16.99962  -1.30259  -13.49403 1.000 35.19329  ?  305 THR   I N   1 
ATOM   1998  C CA  . THR   A  1 305 ? 17.98110  -0.63115  -12.65469 1.000 36.49209  ?  305 THR   I CA  1 
ATOM   1999  C C   . THR   A  1 305 ? 19.00890  0.08969   -13.52009 1.000 58.42452  ?  305 THR   I C   1 
ATOM   2000  O O   . THR   A  1 305 ? 19.48532  -0.45548  -14.52946 1.000 23.29810  ?  305 THR   I O   1 
ATOM   2001  C CB  . THR   A  1 305 ? 18.68506  -1.64071  -11.74546 1.000 26.11196  ?  305 THR   I CB  1 
ATOM   2002  O OG1 . THR   A  1 305 ? 17.70883  -2.54813  -11.21844 1.000 43.18341  ?  305 THR   I OG1 1 
ATOM   2003  C CG2 . THR   A  1 305 ? 19.39069  -0.92353  -10.60708 1.000 25.89903  ?  305 THR   I CG2 1 
ATOM   2004  N N   . ILE   A  1 306 ? 19.34056  1.31938   -13.13028 1.000 23.15083  ?  306 ILE   I N   1 
ATOM   2005  C CA  . ILE   A  1 306 ? 20.37916  2.05933   -13.83215 1.000 35.97618  ?  306 ILE   I CA  1 
ATOM   2006  C C   . ILE   A  1 306 ? 21.70979  1.43355   -13.45953 1.000 36.61538  ?  306 ILE   I C   1 
ATOM   2007  O O   . ILE   A  1 306 ? 22.09599  1.43077   -12.28612 1.000 39.67073  ?  306 ILE   I O   1 
ATOM   2008  C CB  . ILE   A  1 306 ? 20.34947  3.54847   -13.46846 1.000 32.24518  ?  306 ILE   I CB  1 
ATOM   2009  C CG1 . ILE   A  1 306 ? 18.93107  4.12446   -13.59338 1.000 19.64788  ?  306 ILE   I CG1 1 
ATOM   2010  C CG2 . ILE   A  1 306 ? 21.36631  4.31426   -14.32386 1.000 27.93899  ?  306 ILE   I CG2 1 
ATOM   2011  C CD1 . ILE   A  1 306 ? 18.26539  3.92517   -14.95970 1.000 26.40555  ?  306 ILE   I CD1 1 
ATOM   2012  N N   . VAL   A  1 307 ? 22.40011  0.87416   -14.44343 1.000 33.16175  ?  307 VAL   I N   1 
ATOM   2013  C CA  . VAL   A  1 307 ? 23.66322  0.21600   -14.15766 1.000 27.04676  ?  307 VAL   I CA  1 
ATOM   2014  C C   . VAL   A  1 307 ? 24.82292  1.20495   -14.18348 1.000 35.76400  ?  307 VAL   I C   1 
ATOM   2015  O O   . VAL   A  1 307 ? 25.67864  1.17541   -13.29468 1.000 34.26750  ?  307 VAL   I O   1 
ATOM   2016  C CB  . VAL   A  1 307 ? 23.88856  -0.95056  -15.13538 1.000 42.96937  ?  307 VAL   I CB  1 
ATOM   2017  C CG1 . VAL   A  1 307 ? 25.21301  -1.63198  -14.83671 1.000 16.94436  ?  307 VAL   I CG1 1 
ATOM   2018  C CG2 . VAL   A  1 307 ? 22.73409  -1.94981  -15.06678 1.000 28.01582  ?  307 VAL   I CG2 1 
ATOM   2019  N N   . LYS   A  1 308 ? 24.83689  2.11636   -15.16034 1.000 46.70569  ?  308 LYS   I N   1 
ATOM   2020  C CA  . LYS   A  1 308 ? 26.01747  2.92940   -15.44021 1.000 37.32463  ?  308 LYS   I CA  1 
ATOM   2021  C C   . LYS   A  1 308 ? 25.63534  4.10032   -16.33368 1.000 50.84827  ?  308 LYS   I C   1 
ATOM   2022  O O   . LYS   A  1 308 ? 24.95806  3.91120   -17.35230 1.000 34.01852  ?  308 LYS   I O   1 
ATOM   2023  C CB  . LYS   A  1 308 ? 27.08564  2.08155   -16.12598 1.000 34.14067  ?  308 LYS   I CB  1 
ATOM   2024  C CG  . LYS   A  1 308 ? 28.49867  2.63706   -16.14016 1.000 25.48179  ?  308 LYS   I CG  1 
ATOM   2025  C CD  . LYS   A  1 308 ? 29.31253  1.69874   -17.03458 1.000 36.33922  ?  308 LYS   I CD  1 
ATOM   2026  C CE  . LYS   A  1 308 ? 30.81776  1.80270   -16.83404 1.000 56.28231  ?  308 LYS   I CE  1 
ATOM   2027  N NZ  . LYS   A  1 308 ? 31.44387  0.59597   -17.48259 1.000 67.92818  ?  308 LYS   I NZ  1 
ATOM   2028  N N   . ILE   A  1 309 ? 26.08356  5.29686   -15.95715 1.000 29.31029  ?  309 ILE   I N   1 
ATOM   2029  C CA  . ILE   A  1 309 ? 25.87109  6.52066   -16.72135 1.000 36.38871  ?  309 ILE   I CA  1 
ATOM   2030  C C   . ILE   A  1 309 ? 27.24015  7.09905   -17.04100 1.000 28.83647  ?  309 ILE   I C   1 
ATOM   2031  O O   . ILE   A  1 309 ? 28.02234  7.36332   -16.12151 1.000 37.41143  ?  309 ILE   I O   1 
ATOM   2032  C CB  . ILE   A  1 309 ? 25.04198  7.54862   -15.94274 1.000 20.83910  ?  309 ILE   I CB  1 
ATOM   2033  C CG1 . ILE   A  1 309 ? 23.67539  6.99377   -15.57054 1.000 41.52908  ?  309 ILE   I CG1 1 
ATOM   2034  C CG2 . ILE   A  1 309 ? 24.91307  8.83291   -16.75682 1.000 23.49415  ?  309 ILE   I CG2 1 
ATOM   2035  C CD1 . ILE   A  1 309 ? 22.98540  7.83156   -14.53143 1.000 22.22663  ?  309 ILE   I CD1 1 
ATOM   2036  N N   . ILE   A  1 310 ? 27.53007  7.30742   -18.32989 1.000 34.10903  ?  310 ILE   I N   1 
ATOM   2037  C CA  . ILE   A  1 310 ? 28.82037  7.83557   -18.76316 1.000 17.98691  ?  310 ILE   I CA  1 
ATOM   2038  C C   . ILE   A  1 310 ? 28.60057  9.06046   -19.63483 1.000 35.39869  ?  310 ILE   I C   1 
ATOM   2039  O O   . ILE   A  1 310 ? 27.84408  9.00661   -20.61279 1.000 28.39288  ?  310 ILE   I O   1 
ATOM   2040  C CB  . ILE   A  1 310 ? 29.64683  6.80250   -19.54600 1.000 35.37628  ?  310 ILE   I CB  1 
ATOM   2041  C CG1 . ILE   A  1 310 ? 29.72298  5.47872   -18.79273 1.000 36.46701  ?  310 ILE   I CG1 1 
ATOM   2042  C CG2 . ILE   A  1 310 ? 31.01715  7.37533   -19.82198 1.000 22.81230  ?  310 ILE   I CG2 1 
ATOM   2043  C CD1 . ILE   A  1 310 ? 29.04825  4.34004   -19.52615 1.000 40.83829  ?  310 ILE   I CD1 1 
ATOM   2044  N N   . ASN   A  1 311 ? 29.29985  10.14461  -19.32309 1.000 34.06977  ?  311 ASN   I N   1 
ATOM   2045  C CA  . ASN   A  1 311 ? 29.21370  11.35388  -20.12760 1.000 30.88194  ?  311 ASN   I CA  1 
ATOM   2046  C C   . ASN   A  1 311 ? 30.46801  11.47744  -20.97628 1.000 20.23868  ?  311 ASN   I C   1 
ATOM   2047  O O   . ASN   A  1 311 ? 31.58684  11.46740  -20.45566 1.000 47.25163  ?  311 ASN   I O   1 
ATOM   2048  C CB  . ASN   A  1 311 ? 28.98821  12.58058  -19.25301 1.000 15.63665  ?  311 ASN   I CB  1 
ATOM   2049  C CG  . ASN   A  1 311 ? 27.52373  12.71704  -18.84461 1.000 61.35967  ?  311 ASN   I CG  1 
ATOM   2050  O OD1 . ASN   A  1 311 ? 26.64822  12.93212  -19.69462 1.000 41.35075  ?  311 ASN   I OD1 1 
ATOM   2051  N ND2 . ASN   A  1 311 ? 27.24730  12.55386  -17.55445 1.000 43.55431  ?  311 ASN   I ND2 1 
ATOM   2052  N N   . VAL   A  1 312 ? 30.27806  11.54876  -22.28807 1.000 25.22516  ?  312 VAL   I N   1 
ATOM   2053  C CA  . VAL   A  1 312 ? 31.37382  11.46555  -23.23763 1.000 23.67086  ?  312 VAL   I CA  1 
ATOM   2054  C C   . VAL   A  1 312 ? 31.49328  12.79886  -23.97126 1.000 22.51670  ?  312 VAL   I C   1 
ATOM   2055  O O   . VAL   A  1 312 ? 30.54847  13.22676  -24.64249 1.000 47.41987  ?  312 VAL   I O   1 
ATOM   2056  C CB  . VAL   A  1 312 ? 31.18304  10.30381  -24.22869 1.000 27.23675  ?  312 VAL   I CB  1 
ATOM   2057  C CG1 . VAL   A  1 312 ? 32.48598  10.06571  -25.01144 1.000 13.53360  ?  312 VAL   I CG1 1 
ATOM   2058  C CG2 . VAL   A  1 312 ? 30.78394  9.03661   -23.48054 1.000 19.93285  ?  312 VAL   I CG2 1 
ATOM   2059  N N   . PRO   A  1 313 ? 32.61914  13.49328  -23.86226 1.000 34.18151  ?  313 PRO   I N   1 
ATOM   2060  C CA  . PRO   A  1 313 ? 32.83879  14.68499  -24.69603 1.000 29.86433  ?  313 PRO   I CA  1 
ATOM   2061  C C   . PRO   A  1 313 ? 32.97464  14.28754  -26.15630 1.000 33.54440  ?  313 PRO   I C   1 
ATOM   2062  O O   . PRO   A  1 313 ? 33.44248  13.19098  -26.48162 1.000 28.78270  ?  313 PRO   I O   1 
ATOM   2063  C CB  . PRO   A  1 313 ? 34.16101  15.26629  -24.16758 1.000 12.90341  ?  313 PRO   I CB  1 
ATOM   2064  C CG  . PRO   A  1 313 ? 34.45400  14.51349  -22.85561 1.000 18.75207  ?  313 PRO   I CG  1 
ATOM   2065  C CD  . PRO   A  1 313 ? 33.74715  13.19052  -22.96726 1.000 14.92301  ?  313 PRO   I CD  1 
ATOM   2066  N N   . GLY   A  1 314 ? 32.56906  15.19111  -27.04280 1.000 28.34740  ?  314 GLY   I N   1 
ATOM   2067  C CA  . GLY   A  1 314 ? 32.62474  14.87814  -28.45167 1.000 20.80884  ?  314 GLY   I CA  1 
ATOM   2068  C C   . GLY   A  1 314 ? 32.41840  16.07042  -29.35464 1.000 37.77166  ?  314 GLY   I C   1 
ATOM   2069  O O   . GLY   A  1 314 ? 32.66505  17.21722  -28.97255 1.000 29.02269  ?  314 GLY   I O   1 
ATOM   2070  N N   . THR   A  1 315 ? 31.97441  15.78063  -30.57415 1.000 33.02255  ?  315 THR   I N   1 
ATOM   2071  C CA  . THR   A  1 315 ? 31.71596  16.80706  -31.56770 1.000 35.37416  ?  315 THR   I CA  1 
ATOM   2072  C C   . THR   A  1 315 ? 30.35225  17.46869  -31.33276 1.000 43.70462  ?  315 THR   I C   1 
ATOM   2073  O O   . THR   A  1 315 ? 29.50381  16.97703  -30.58047 1.000 35.88801  ?  315 THR   I O   1 
ATOM   2074  C CB  . THR   A  1 315 ? 31.77149  16.20851  -32.97779 1.000 34.99662  ?  315 THR   I CB  1 
ATOM   2075  O OG1 . THR   A  1 315 ? 30.65862  15.31499  -33.18450 1.000 28.77592  ?  315 THR   I OG1 1 
ATOM   2076  C CG2 . THR   A  1 315 ? 33.01343  15.42128  -33.13956 1.000 25.48793  ?  315 THR   I CG2 1 
ATOM   2077  N N   . TYR   A  1 316 ? 30.16078  18.59929  -32.00772 1.000 36.80036  ?  316 TYR   I N   1 
ATOM   2078  C CA  . TYR   A  1 316 ? 28.94997  19.41003  -32.13667 1.000 36.36016  ?  316 TYR   I CA  1 
ATOM   2079  C C   . TYR   A  1 316 ? 28.59193  19.66514  -33.59436 1.000 31.38510  ?  316 TYR   I C   1 
ATOM   2080  O O   . TYR   A  1 316 ? 27.40784  19.68715  -33.94309 1.000 41.24712  ?  316 TYR   I O   1 
ATOM   2081  C CB  . TYR   A  1 316 ? 29.11268  20.77397  -31.39780 1.000 31.30562  ?  316 TYR   I CB  1 
ATOM   2082  C CG  . TYR   A  1 316 ? 29.42292  20.59620  -29.93626 1.000 42.05180  ?  316 TYR   I CG  1 
ATOM   2083  C CD1 . TYR   A  1 316 ? 28.40417  20.32461  -29.01651 1.000 43.43095  ?  316 TYR   I CD1 1 
ATOM   2084  C CD2 . TYR   A  1 316 ? 30.73757  20.64323  -29.47935 1.000 36.15049  ?  316 TYR   I CD2 1 
ATOM   2085  C CE1 . TYR   A  1 316 ? 28.68007  20.12300  -27.66764 1.000 35.06968  ?  316 TYR   I CE1 1 
ATOM   2086  C CE2 . TYR   A  1 316 ? 31.03671  20.44965  -28.13125 1.000 28.33868  ?  316 TYR   I CE2 1 
ATOM   2087  C CZ  . TYR   A  1 316 ? 30.00367  20.19121  -27.23210 1.000 46.12300  ?  316 TYR   I CZ  1 
ATOM   2088  O OH  . TYR   A  1 316 ? 30.30957  19.99551  -25.90308 1.000 37.39633  ?  316 TYR   I OH  1 
ATOM   2089  N N   . PHE   A  1 317 ? 29.58972  19.84253  -34.46793 1.000 42.80533  ?  317 PHE   I N   1 
ATOM   2090  C CA  . PHE   A  1 317 ? 29.33240  20.31960  -35.82082 1.000 24.05497  ?  317 PHE   I CA  1 
ATOM   2091  C C   . PHE   A  1 317 ? 29.91144  19.39532  -36.88336 1.000 45.72484  ?  317 PHE   I C   1 
ATOM   2092  O O   . PHE   A  1 317 ? 30.19398  19.84438  -38.00349 1.000 33.65623  ?  317 PHE   I O   1 
ATOM   2093  C CB  . PHE   A  1 317 ? 29.87803  21.73694  -35.99266 1.000 23.93420  ?  317 PHE   I CB  1 
ATOM   2094  C CG  . PHE   A  1 317 ? 29.20715  22.73993  -35.10355 1.000 44.07730  ?  317 PHE   I CG  1 
ATOM   2095  C CD1 . PHE   A  1 317 ? 27.89982  23.13526  -35.35537 1.000 24.73456  ?  317 PHE   I CD1 1 
ATOM   2096  C CD2 . PHE   A  1 317 ? 29.87190  23.26639  -34.00015 1.000 39.84069  ?  317 PHE   I CD2 1 
ATOM   2097  C CE1 . PHE   A  1 317 ? 27.26990  24.05629  -34.53773 1.000 40.04357  ?  317 PHE   I CE1 1 
ATOM   2098  C CE2 . PHE   A  1 317 ? 29.24959  24.18221  -33.17872 1.000 32.63315  ?  317 PHE   I CE2 1 
ATOM   2099  C CZ  . PHE   A  1 317 ? 27.94094  24.57573  -33.44799 1.000 34.03977  ?  317 PHE   I CZ  1 
ATOM   2100  N N   . ALA   A  1 318 ? 30.07653  18.10538  -36.56332 1.000 30.53861  ?  318 ALA   I N   1 
ATOM   2101  C CA  . ALA   A  1 318 ? 30.64830  17.13822  -37.50175 1.000 27.41415  ?  318 ALA   I CA  1 
ATOM   2102  C C   . ALA   A  1 318 ? 29.52944  16.43246  -38.25474 1.000 32.22987  ?  318 ALA   I C   1 
ATOM   2103  O O   . ALA   A  1 318 ? 28.75458  15.68153  -37.65630 1.000 37.14668  ?  318 ALA   I O   1 
ATOM   2104  C CB  . ALA   A  1 318 ? 31.51245  16.11601  -36.76950 1.000 20.93610  ?  318 ALA   I CB  1 
ATOM   2105  N N   . GLN   A  1 319 ? 29.44982  16.65322  -39.56735 1.000 37.22254  ?  319 GLN   I N   1 
ATOM   2106  C CA  . GLN   A  1 319 ? 28.58179  15.82392  -40.39080 1.000 33.70366  ?  319 GLN   I CA  1 
ATOM   2107  C C   . GLN   A  1 319 ? 29.39266  14.65087  -40.94223 1.000 31.79881  ?  319 GLN   I C   1 
ATOM   2108  O O   . GLN   A  1 319 ? 30.61110  14.56301  -40.75220 1.000 46.07188  ?  319 GLN   I O   1 
ATOM   2109  C CB  . GLN   A  1 319 ? 27.93656  16.63957  -41.50839 1.000 33.18951  ?  319 GLN   I CB  1 
ATOM   2110  C CG  . GLN   A  1 319 ? 28.93840  17.17303  -42.48993 1.000 41.29198  ?  319 GLN   I CG  1 
ATOM   2111  C CD  . GLN   A  1 319 ? 28.31916  18.15933  -43.45057 1.000 30.30438  ?  319 GLN   I CD  1 
ATOM   2112  O OE1 . GLN   A  1 319 ? 28.02077  19.30431  -43.08495 1.000 53.62499  ?  319 GLN   I OE1 1 
ATOM   2113  N NE2 . GLN   A  1 319 ? 28.13600  17.73057  -44.69235 1.000 39.11159  ?  319 GLN   I NE2 1 
ATOM   2114  N N   . ALA   A  1 320 ? 28.71307  13.72574  -41.61456 1.000 34.10902  ?  320 ALA   I N   1 
ATOM   2115  C CA  . ALA   A  1 320 ? 29.40768  12.57471  -42.18539 1.000 34.85442  ?  320 ALA   I CA  1 
ATOM   2116  C C   . ALA   A  1 320 ? 30.28237  13.02153  -43.35731 1.000 34.59723  ?  320 ALA   I C   1 
ATOM   2117  O O   . ALA   A  1 320 ? 29.79429  13.71602  -44.25961 1.000 36.13544  ?  320 ALA   I O   1 
ATOM   2118  C CB  . ALA   A  1 320 ? 28.41277  11.51265  -42.63858 1.000 18.59692  ?  320 ALA   I CB  1 
ATOM   2119  N N   . PRO   A  1 321 ? 31.56159  12.63175  -43.39084 1.000 49.70161  ?  321 PRO   I N   1 
ATOM   2120  C CA  . PRO   A  1 321 ? 32.45304  13.09235  -44.47355 1.000 35.60058  ?  321 PRO   I CA  1 
ATOM   2121  C C   . PRO   A  1 321 ? 31.93271  12.77445  -45.87424 1.000 41.28584  ?  321 PRO   I C   1 
ATOM   2122  O O   . PRO   A  1 321 ? 32.13012  13.58461  -46.78874 1.000 46.05233  ?  321 PRO   I O   1 
ATOM   2123  C CB  . PRO   A  1 321 ? 33.77344  12.36200  -44.17606 1.000 28.79716  ?  321 PRO   I CB  1 
ATOM   2124  C CG  . PRO   A  1 321 ? 33.63140  11.77578  -42.79969 1.000 49.95730  ?  321 PRO   I CG  1 
ATOM   2125  C CD  . PRO   A  1 321 ? 32.17234  11.57533  -42.56557 1.000 32.24707  ?  321 PRO   I CD  1 
ATOM   2126  N N   . SER   A  1 322 ? 31.24016  11.63991  -46.05590 1.000 44.10733  ?  322 SER   I N   1 
ATOM   2127  C CA  . SER   A  1 322 ? 30.63217  11.29765  -47.34426 1.000 43.58956  ?  322 SER   I CA  1 
ATOM   2128  C C   . SER   A  1 322 ? 29.61672  12.33008  -47.83477 1.000 43.19354  ?  322 SER   I C   1 
ATOM   2129  O O   . SER   A  1 322 ? 29.30987  12.34617  -49.03344 1.000 62.57330  ?  322 SER   I O   1 
ATOM   2130  C CB  . SER   A  1 322 ? 29.94690  9.92396   -47.26728 1.000 34.65379  ?  322 SER   I CB  1 
ATOM   2131  O OG  . SER   A  1 322 ? 29.28528  9.72053   -46.02287 1.000 59.74612  ?  322 SER   I OG  1 
ATOM   2132  N N   . THR   A  1 323 ? 29.06444  13.16707  -46.94768 1.000 64.24218  ?  323 THR   I N   1 
ATOM   2133  C CA  . THR   A  1 323 ? 28.08625  14.17565  -47.34706 1.000 46.58649  ?  323 THR   I CA  1 
ATOM   2134  C C   . THR   A  1 323 ? 28.70033  15.54765  -47.56160 1.000 62.06109  ?  323 THR   I C   1 
ATOM   2135  O O   . THR   A  1 323 ? 27.97901  16.47096  -47.94242 1.000 44.97246  ?  323 THR   I O   1 
ATOM   2136  C CB  . THR   A  1 323 ? 26.96129  14.30708  -46.30703 1.000 53.32080  ?  323 THR   I CB  1 
ATOM   2137  O OG1 . THR   A  1 323 ? 27.42170  15.07736  -45.18277 1.000 54.85612  ?  323 THR   I OG1 1 
ATOM   2138  C CG2 . THR   A  1 323 ? 26.52012  12.95114  -45.82933 1.000 35.27107  ?  323 THR   I CG2 1 
ATOM   2139  N N   . ILE   A  1 324 ? 29.99828  15.71486  -47.30689 1.000 42.60356  ?  324 ILE   I N   1 
ATOM   2140  C CA  . ILE   A  1 324 ? 30.60876  17.03063  -47.44819 1.000 44.34936  ?  324 ILE   I CA  1 
ATOM   2141  C C   . ILE   A  1 324 ? 30.47664  17.47930  -48.89362 1.000 62.89887  ?  324 ILE   I C   1 
ATOM   2142  O O   . ILE   A  1 324 ? 30.89838  16.77520  -49.82049 1.000 55.56918  ?  324 ILE   I O   1 
ATOM   2143  C CB  . ILE   A  1 324 ? 32.06582  16.99724  -46.99638 1.000 32.35842  ?  324 ILE   I CB  1 
ATOM   2144  C CG1 . ILE   A  1 324 ? 32.12656  16.74956  -45.48989 1.000 45.73685  ?  324 ILE   I CG1 1 
ATOM   2145  C CG2 . ILE   A  1 324 ? 32.75942  18.30702  -47.37290 1.000 34.90085  ?  324 ILE   I CG2 1 
ATOM   2146  C CD1 . ILE   A  1 324 ? 33.50039  16.63034  -44.96231 1.000 39.23993  ?  324 ILE   I CD1 1 
ATOM   2147  N N   . GLY   A  1 325 ? 29.85176  18.63939  -49.09680 1.000 49.48471  ?  325 GLY   I N   1 
ATOM   2148  C CA  . GLY   A  1 325 ? 29.62676  19.16995  -50.42391 1.000 44.70434  ?  325 GLY   I CA  1 
ATOM   2149  C C   . GLY   A  1 325 ? 28.22680  18.97847  -50.98200 1.000 53.73528  ?  325 GLY   I C   1 
ATOM   2150  O O   . GLY   A  1 325 ? 27.86654  19.67507  -51.93766 1.000 58.90675  ?  325 GLY   I O   1 
ATOM   2151  N N   . ASP   A  1 326 ? 27.44256  18.04700  -50.43560 1.000 51.53421  ?  326 ASP   I N   1 
ATOM   2152  C CA  . ASP   A  1 326 ? 26.05602  17.87704  -50.85870 1.000 58.73857  ?  326 ASP   I CA  1 
ATOM   2153  C C   . ASP   A  1 326 ? 25.28101  19.19405  -50.74945 1.000 49.91304  ?  326 ASP   I C   1 
ATOM   2154  O O   . ASP   A  1 326 ? 25.61801  20.06607  -49.94063 1.000 60.28104  ?  326 ASP   I O   1 
ATOM   2155  C CB  . ASP   A  1 326 ? 25.35905  16.81561  -50.00672 1.000 41.17058  ?  326 ASP   I CB  1 
ATOM   2156  C CG  . ASP   A  1 326 ? 25.90407  15.41866  -50.23288 1.000 77.84333  ?  326 ASP   I CG  1 
ATOM   2157  O OD1 . ASP   A  1 326 ? 26.74769  15.22762  -51.14753 1.000 63.44444  ?  326 ASP   I OD1 1 
ATOM   2158  O OD2 . ASP   A  1 326 ? 25.47033  14.51091  -49.47865 1.000 66.03790  ?  326 ASP   I OD2 1 
ATOM   2159  N N   . PRO   A  1 327 ? 24.23028  19.36279  -51.54372 1.000 69.83865  ?  327 PRO   I N   1 
ATOM   2160  C CA  . PRO   A  1 327 ? 23.46477  20.61496  -51.48295 1.000 55.29600  ?  327 PRO   I CA  1 
ATOM   2161  C C   . PRO   A  1 327 ? 22.76344  20.80137  -50.13953 1.000 50.01447  ?  327 PRO   I C   1 
ATOM   2162  O O   . PRO   A  1 327 ? 22.26065  19.84729  -49.54083 1.000 62.99714  ?  327 PRO   I O   1 
ATOM   2163  C CB  . PRO   A  1 327 ? 22.45586  20.46786  -52.63076 1.000 35.18703  ?  327 PRO   I CB  1 
ATOM   2164  C CG  . PRO   A  1 327 ? 22.45071  19.01404  -52.99361 1.000 49.85607  ?  327 PRO   I CG  1 
ATOM   2165  C CD  . PRO   A  1 327 ? 23.82021  18.50331  -52.67005 1.000 52.77118  ?  327 PRO   I CD  1 
ATOM   2166  N N   . ILE   A  1 328 ? 22.74403  22.04490  -49.66429 1.000 39.84085  ?  328 ILE   I N   1 
ATOM   2167  C CA  . ILE   A  1 328 ? 21.95093  22.40474  -48.48866 1.000 39.64016  ?  328 ILE   I CA  1 
ATOM   2168  C C   . ILE   A  1 328 ? 20.62181  22.99218  -48.94904 1.000 41.93588  ?  328 ILE   I C   1 
ATOM   2169  O O   . ILE   A  1 328 ? 20.56553  24.17724  -49.31137 1.000 50.97677  ?  328 ILE   I O   1 
ATOM   2170  C CB  . ILE   A  1 328 ? 22.69728  23.39026  -47.57258 1.000 44.86504  ?  328 ILE   I CB  1 
ATOM   2171  C CG1 . ILE   A  1 328 ? 24.05435  22.81873  -47.15477 1.000 32.32163  ?  328 ILE   I CG1 1 
ATOM   2172  C CG2 . ILE   A  1 328 ? 21.87720  23.69802  -46.31950 1.000 34.04611  ?  328 ILE   I CG2 1 
ATOM   2173  C CD1 . ILE   A  1 328 ? 24.84050  23.73656  -46.21715 1.000 28.33143  ?  328 ILE   I CD1 1 
ATOM   2174  N N   . PRO   A  1 329 ? 19.53232  22.21855  -48.92670 1.000 69.34752  ?  329 PRO   I N   1 
ATOM   2175  C CA  . PRO   A  1 329 ? 18.25934  22.69325  -49.49102 1.000 54.81973  ?  329 PRO   I CA  1 
ATOM   2176  C C   . PRO   A  1 329 ? 17.77809  23.97433  -48.82598 1.000 57.07263  ?  329 PRO   I C   1 
ATOM   2177  O O   . PRO   A  1 329 ? 17.98743  24.19908  -47.62847 1.000 89.42299  ?  329 PRO   I O   1 
ATOM   2178  C CB  . PRO   A  1 329 ? 17.29301  21.53212  -49.22739 1.000 41.68053  ?  329 PRO   I CB  1 
ATOM   2179  C CG  . PRO   A  1 329 ? 18.19398  20.32167  -49.03449 1.000 52.38891  ?  329 PRO   I CG  1 
ATOM   2180  C CD  . PRO   A  1 329 ? 19.45015  20.83585  -48.42911 1.000 57.28016  ?  329 PRO   I CD  1 
ATOM   2181  N N   . ASP   A  1 330 ? 17.17089  24.83910  -49.64316 1.000 78.93497  ?  330 ASP   I N   1 
ATOM   2182  C CA  . ASP   A  1 330 ? 16.57776  26.09077  -49.18689 1.000 89.00688  ?  330 ASP   I CA  1 
ATOM   2183  C C   . ASP   A  1 330 ? 15.08831  25.96840  -48.86180 1.000 67.70019  ?  330 ASP   I C   1 
ATOM   2184  O O   . ASP   A  1 330 ? 14.38293  26.99412  -48.87307 1.000 96.42514  ?  330 ASP   I O   1 
ATOM   2185  C CB  . ASP   A  1 330 ? 16.81377  27.20237  -50.22723 1.000 60.24111  ?  330 ASP   I CB  1 
ATOM   2186  N N   . ASN   A  1 331 ? 14.62813  24.75294  -48.54486 1.000 82.27411  ?  331 ASN   I N   1 
ATOM   2187  C CA  . ASN   A  1 331 ? 13.25509  24.43727  -48.18450 1.000 82.39919  ?  331 ASN   I CA  1 
ATOM   2188  C C   . ASN   A  1 331 ? 13.27883  23.70327  -46.84608 1.000 65.06757  ?  331 ASN   I C   1 
ATOM   2189  O O   . ASN   A  1 331 ? 14.30639  23.67616  -46.18101 1.000 108.77752 ?  331 ASN   I O   1 
ATOM   2190  C CB  . ASN   A  1 331 ? 12.62505  23.61240  -49.29651 1.000 60.32347  ?  331 ASN   I CB  1 
ATOM   2191  C CG  . ASN   A  1 331 ? 13.21755  22.24827  -49.44317 1.000 71.41462  ?  331 ASN   I CG  1 
ATOM   2192  O OD1 . ASN   A  1 331 ? 13.38649  21.45316  -48.51844 1.000 140.92785 ?  331 ASN   I OD1 1 
ATOM   2193  N ND2 . ASN   A  1 331 ? 13.64662  22.00911  -50.65527 1.000 75.58434  ?  331 ASN   I ND2 1 
ATOM   2194  N N   . ASP   A  1 332 ? 12.24304  22.74114  -46.67184 1.000 78.39207  ?  332 ASP   I N   1 
ATOM   2195  C CA  . ASP   A  1 332 ? 12.12258  21.88576  -45.45988 1.000 86.89162  ?  332 ASP   I CA  1 
ATOM   2196  C C   . ASP   A  1 332 ? 11.70838  20.44711  -45.75103 1.000 59.56404  ?  332 ASP   I C   1 
ATOM   2197  O O   . ASP   A  1 332 ? 11.60949  19.71954  -44.80295 1.000 65.04920  ?  332 ASP   I O   1 
ATOM   2198  C CB  . ASP   A  1 332 ? 11.13335  22.52050  -44.47282 1.000 90.34658  ?  332 ASP   I CB  1 
ATOM   2199  C CG  . ASP   A  1 332 ? 9.65242   22.36868  -45.03890 1.000 99.20347  ?  332 ASP   I CG  1 
ATOM   2200  O OD1 . ASP   A  1 332 ? 9.34419   22.95449  -46.12839 1.000 99.39578  ?  332 ASP   I OD1 1 
ATOM   2201  O OD2 . ASP   A  1 332 ? 8.77959   21.73566  -44.41146 1.000 85.66403  ?  332 ASP   I OD2 1 
ATOM   2202  N N   . TYR   A  1 333 ? 11.25437  20.09108  -46.95944 1.000 103.01248 ?  333 TYR   I N   1 
ATOM   2203  C CA  . TYR   A  1 333 ? 11.10728  18.63443  -47.17676 1.000 99.96784  ?  333 TYR   I CA  1 
ATOM   2204  C C   . TYR   A  1 333 ? 12.43749  17.94013  -47.50160 1.000 113.12580 ?  333 TYR   I C   1 
ATOM   2205  O O   . TYR   A  1 333 ? 12.55779  16.67594  -47.53419 1.000 42.48122  ?  333 TYR   I O   1 
ATOM   2206  C CB  . TYR   A  1 333 ? 10.08661  18.19703  -48.26785 1.000 35.08585  ?  333 TYR   I CB  1 
ATOM   2207  C CG  . TYR   A  1 333 ? 10.19811  18.99048  -49.56140 1.000 70.88957  ?  333 TYR   I CG  1 
ATOM   2208  C CD1 . TYR   A  1 333 ? 9.85568   20.36202  -49.60769 1.000 116.72870 ?  333 TYR   I CD1 1 
ATOM   2209  C CD2 . TYR   A  1 333 ? 10.63177  18.38351  -50.75345 1.000 82.01238  ?  333 TYR   I CD2 1 
ATOM   2210  C CE1 . TYR   A  1 333 ? 9.96212   21.09751  -50.79773 1.000 125.47656 ?  333 TYR   I CE1 1 
ATOM   2211  C CE2 . TYR   A  1 333 ? 10.73442  19.11241  -51.96256 1.000 85.25832  ?  333 TYR   I CE2 1 
ATOM   2212  C CZ  . TYR   A  1 333 ? 10.39403  20.45299  -51.97743 1.000 88.25490  ?  333 TYR   I CZ  1 
ATOM   2213  O OH  . TYR   A  1 333 ? 10.49279  21.10175  -53.18186 1.000 84.08062  ?  333 TYR   I OH  1 
ATOM   2214  N N   . ASP   A  1 334 ? 13.43268  18.72107  -47.74283 1.000 68.59513  ?  334 ASP   I N   1 
ATOM   2215  C CA  . ASP   A  1 334 ? 14.64719  17.97969  -48.08851 1.000 66.66985  ?  334 ASP   I CA  1 
ATOM   2216  C C   . ASP   A  1 334 ? 15.70035  18.07229  -46.98791 1.000 76.11022  ?  334 ASP   I C   1 
ATOM   2217  O O   . ASP   A  1 334 ? 16.07028  19.18487  -46.57368 1.000 41.83778  ?  334 ASP   I O   1 
ATOM   2218  C CB  . ASP   A  1 334 ? 15.23965  18.49250  -49.39084 1.000 95.47191  ?  334 ASP   I CB  1 
ATOM   2219  C CG  . ASP   A  1 334 ? 14.40688  18.11655  -50.58742 1.000 110.09324 ?  334 ASP   I CG  1 
ATOM   2220  O OD1 . ASP   A  1 334 ? 13.76211  17.03102  -50.55265 1.000 66.29888  ?  334 ASP   I OD1 1 
ATOM   2221  O OD2 . ASP   A  1 334 ? 14.39620  18.88609  -51.56775 1.000 77.62309  ?  334 ASP   I OD2 1 
ATOM   2222  N N   . PRO   A  1 335 ? 16.21285  16.93796  -46.51124 1.000 67.55469  ?  335 PRO   I N   1 
ATOM   2223  C CA  . PRO   A  1 335 ? 17.17496  16.95860  -45.40880 1.000 47.36115  ?  335 PRO   I CA  1 
ATOM   2224  C C   . PRO   A  1 335 ? 18.51128  17.50074  -45.86555 1.000 31.39069  ?  335 PRO   I C   1 
ATOM   2225  O O   . PRO   A  1 335 ? 19.03927  17.09712  -46.92009 1.000 60.33228  ?  335 PRO   I O   1 
ATOM   2226  C CB  . PRO   A  1 335 ? 17.28583  15.47945  -45.00820 1.000 53.13994  ?  335 PRO   I CB  1 
ATOM   2227  C CG  . PRO   A  1 335 ? 16.17972  14.77683  -45.74670 1.000 66.00057  ?  335 PRO   I CG  1 
ATOM   2228  C CD  . PRO   A  1 335 ? 15.90344  15.57544  -46.95729 1.000 39.57662  ?  335 PRO   I CD  1 
ATOM   2229  N N   . PRO   A  1 336 ? 19.10785  18.41548  -45.09849 1.000 60.51488  ?  336 PRO   I N   1 
ATOM   2230  C CA  . PRO   A  1 336 ? 20.47289  18.87979  -45.39455 1.000 24.93000  ?  336 PRO   I CA  1 
ATOM   2231  C C   . PRO   A  1 336 ? 21.49857  17.83996  -44.96568 1.000 91.22225  ?  336 PRO   I C   1 
ATOM   2232  O O   . PRO   A  1 336 ? 21.16010  16.85756  -44.28150 1.000 30.28849  ?  336 PRO   I O   1 
ATOM   2233  C CB  . PRO   A  1 336 ? 20.58082  20.17279  -44.57607 1.000 43.91304  ?  336 PRO   I CB  1 
ATOM   2234  C CG  . PRO   A  1 336 ? 19.66818  19.94221  -43.40008 1.000 40.88961  ?  336 PRO   I CG  1 
ATOM   2235  C CD  . PRO   A  1 336 ? 18.59142  18.96703  -43.82713 1.000 24.91265  ?  336 PRO   I CD  1 
ATOM   2236  N N   . PRO   A  1 337 ? 22.76330  17.99354  -45.37206 1.000 43.92941  ?  337 PRO   I N   1 
ATOM   2237  C CA  . PRO   A  1 337 ? 23.75220  16.92070  -45.10073 1.000 59.54089  ?  337 PRO   I CA  1 
ATOM   2238  C C   . PRO   A  1 337 ? 23.86401  16.51982  -43.62986 1.000 48.09446  ?  337 PRO   I C   1 
ATOM   2239  O O   . PRO   A  1 337 ? 23.91918  15.32196  -43.32043 1.000 45.94018  ?  337 PRO   I O   1 
ATOM   2240  C CB  . PRO   A  1 337 ? 25.06554  17.51697  -45.62271 1.000 46.06357  ?  337 PRO   I CB  1 
ATOM   2241  C CG  . PRO   A  1 337 ? 24.66777  18.53502  -46.60704 1.000 54.44625  ?  337 PRO   I CG  1 
ATOM   2242  C CD  . PRO   A  1 337 ? 23.34187  19.09504  -46.15515 1.000 63.12099  ?  337 PRO   I CD  1 
ATOM   2243  N N   . TYR   A  1 338 ? 23.87091  17.49017  -42.71303 1.000 44.88652  ?  338 TYR   I N   1 
ATOM   2244  C CA  . TYR   A  1 338 ? 23.93709  17.17300  -41.29053 1.000 47.47163  ?  338 TYR   I CA  1 
ATOM   2245  C C   . TYR   A  1 338 ? 22.80232  16.24499  -40.86309 1.000 41.28402  ?  338 TYR   I C   1 
ATOM   2246  O O   . TYR   A  1 338 ? 23.03886  15.25874  -40.15205 1.000 42.61215  ?  338 TYR   I O   1 
ATOM   2247  C CB  . TYR   A  1 338 ? 23.92310  18.46413  -40.47101 1.000 34.98937  ?  338 TYR   I CB  1 
ATOM   2248  C CG  . TYR   A  1 338 ? 24.16600  18.28460  -38.98656 1.000 48.06582  ?  338 TYR   I CG  1 
ATOM   2249  C CD1 . TYR   A  1 338 ? 25.33159  17.67789  -38.50617 1.000 40.79356  ?  338 TYR   I CD1 1 
ATOM   2250  C CD2 . TYR   A  1 338 ? 23.24297  18.74643  -38.06375 1.000 38.63407  ?  338 TYR   I CD2 1 
ATOM   2251  C CE1 . TYR   A  1 338 ? 25.55564  17.53419  -37.13169 1.000 43.50597  ?  338 TYR   I CE1 1 
ATOM   2252  C CE2 . TYR   A  1 338 ? 23.45373  18.60769  -36.70279 1.000 32.54266  ?  338 TYR   I CE2 1 
ATOM   2253  C CZ  . TYR   A  1 338 ? 24.60205  17.99865  -36.23761 1.000 52.78752  ?  338 TYR   I CZ  1 
ATOM   2254  O OH  . TYR   A  1 338 ? 24.78250  17.87563  -34.87538 1.000 41.33612  ?  338 TYR   I OH  1 
ATOM   2255  N N   . LEU   A  1 339 ? 21.55746  16.53972  -41.27831 1.000 38.33380  ?  339 LEU   I N   1 
ATOM   2256  C CA  . LEU   A  1 339 ? 20.44200  15.66608  -40.88118 1.000 29.49517  ?  339 LEU   I CA  1 
ATOM   2257  C C   . LEU   A  1 339 ? 20.42172  14.33873  -41.62875 1.000 41.48029  ?  339 LEU   I C   1 
ATOM   2258  O O   . LEU   A  1 339 ? 19.58071  13.49122  -41.31044 1.000 43.17185  ?  339 LEU   I O   1 
ATOM   2259  C CB  . LEU   A  1 339 ? 19.09388  16.36196  -41.06288 1.000 30.31822  ?  339 LEU   I CB  1 
ATOM   2260  C CG  . LEU   A  1 339 ? 18.95533  17.60028  -40.16534 1.000 52.33347  ?  339 LEU   I CG  1 
ATOM   2261  C CD1 . LEU   A  1 339 ? 17.56533  18.19063  -40.25873 1.000 36.15898  ?  339 LEU   I CD1 1 
ATOM   2262  C CD2 . LEU   A  1 339 ? 19.28660  17.27028  -38.72633 1.000 37.51303  ?  339 LEU   I CD2 1 
ATOM   2263  N N   . LYS   A  1 340 ? 21.31078  14.12938  -42.60039 1.000 32.63022  ?  340 LYS   I N   1 
ATOM   2264  C CA  . LYS   A  1 340 ? 21.56037  12.79880  -43.14027 1.000 52.44886  ?  340 LYS   I CA  1 
ATOM   2265  C C   . LYS   A  1 340 ? 22.75798  12.09987  -42.47802 1.000 34.66085  ?  340 LYS   I C   1 
ATOM   2266  O O   . LYS   A  1 340 ? 23.21123  11.07320  -42.98792 1.000 41.05216  ?  340 LYS   I O   1 
ATOM   2267  C CB  . LYS   A  1 340 ? 21.77104  12.87368  -44.65642 1.000 35.31091  ?  340 LYS   I CB  1 
ATOM   2268  C CG  . LYS   A  1 340 ? 20.74916  13.60958  -45.45561 1.000 99.70689  ?  340 LYS   I CG  1 
ATOM   2269  C CD  . LYS   A  1 340 ? 20.98661  13.38963  -46.93189 1.000 110.19017 ?  340 LYS   I CD  1 
ATOM   2270  C CE  . LYS   A  1 340 ? 22.06387  14.32446  -47.49206 1.000 121.54509 ?  340 LYS   I CE  1 
ATOM   2271  N NZ  . LYS   A  1 340 ? 21.68793  14.79912  -48.85743 1.000 92.49308  ?  340 LYS   I NZ  1 
ATOM   2272  N N   . SER   A  1 341 ? 23.25905  12.61639  -41.34171 1.000 38.79719  ?  341 SER   I N   1 
ATOM   2273  C CA  . SER   A  1 341 ? 24.48606  12.13482  -40.71154 1.000 31.95224  ?  341 SER   I CA  1 
ATOM   2274  C C   . SER   A  1 341 ? 24.29759  11.53820  -39.31625 1.000 36.83787  ?  341 SER   I C   1 
ATOM   2275  O O   . SER   A  1 341 ? 25.30110  11.21559  -38.65846 1.000 47.38653  ?  341 SER   I O   1 
ATOM   2276  C CB  . SER   A  1 341 ? 25.51099  13.27941  -40.61069 1.000 38.49782  ?  341 SER   I CB  1 
ATOM   2277  O OG  . SER   A  1 341 ? 25.91143  13.75591  -41.88302 1.000 38.25972  ?  341 SER   I OG  1 
ATOM   2278  N N   . LEU   A  1 342 ? 23.05880  11.38128  -38.84496 1.000 33.53769  ?  342 LEU   I N   1 
ATOM   2279  C CA  . LEU   A  1 342 ? 22.83059  11.06332  -37.43722 1.000 44.72695  ?  342 LEU   I CA  1 
ATOM   2280  C C   . LEU   A  1 342 ? 23.45229  9.72839   -37.03880 1.000 33.32944  ?  342 LEU   I C   1 
ATOM   2281  O O   . LEU   A  1 342 ? 23.93840  9.58101   -35.91206 1.000 39.24584  ?  342 LEU   I O   1 
ATOM   2282  C CB  . LEU   A  1 342 ? 21.33522  11.05095  -37.12521 1.000 27.59241  ?  342 LEU   I CB  1 
ATOM   2283  C CG  . LEU   A  1 342 ? 20.70697  12.34335  -36.62211 1.000 45.85856  ?  342 LEU   I CG  1 
ATOM   2284  C CD1 . LEU   A  1 342 ? 20.78390  13.43339  -37.69267 1.000 26.03548  ?  342 LEU   I CD1 1 
ATOM   2285  C CD2 . LEU   A  1 342 ? 19.25236  12.06127  -36.20256 1.000 21.64667  ?  342 LEU   I CD2 1 
ATOM   2286  N N   . VAL   A  1 343 ? 23.43270  8.72930   -37.92267 1.000 41.08835  ?  343 VAL   I N   1 
ATOM   2287  C CA  . VAL   A  1 343 ? 24.07390  7.47133   -37.54764 1.000 35.38241  ?  343 VAL   I CA  1 
ATOM   2288  C C   . VAL   A  1 343 ? 25.57557  7.67485   -37.41040 1.000 48.29654  ?  343 VAL   I C   1 
ATOM   2289  O O   . VAL   A  1 343 ? 26.18021  7.27504   -36.40944 1.000 32.62507  ?  343 VAL   I O   1 
ATOM   2290  C CB  . VAL   A  1 343 ? 23.74490  6.34883   -38.54742 1.000 36.26305  ?  343 VAL   I CB  1 
ATOM   2291  C CG1 . VAL   A  1 343 ? 24.62404  5.13033   -38.26799 1.000 22.47839  ?  343 VAL   I CG1 1 
ATOM   2292  C CG2 . VAL   A  1 343 ? 22.28739  5.94864   -38.42134 1.000 29.82606  ?  343 VAL   I CG2 1 
ATOM   2293  N N   . TYR   A  1 344 ? 26.18749  8.34130   -38.39117 1.000 25.61229  ?  344 TYR   I N   1 
ATOM   2294  C CA  . TYR   A  1 344 ? 27.62321  8.59451   -38.34103 1.000 43.06808  ?  344 TYR   I CA  1 
ATOM   2295  C C   . TYR   A  1 344 ? 28.03585  9.27118   -37.03870 1.000 44.60127  ?  344 TYR   I C   1 
ATOM   2296  O O   . TYR   A  1 344 ? 28.90657  8.76690   -36.32223 1.000 34.58635  ?  344 TYR   I O   1 
ATOM   2297  C CB  . TYR   A  1 344 ? 28.06196  9.44500   -39.53467 1.000 29.96876  ?  344 TYR   I CB  1 
ATOM   2298  C CG  . TYR   A  1 344 ? 29.51572  9.86643   -39.46989 1.000 50.35335  ?  344 TYR   I CG  1 
ATOM   2299  C CD1 . TYR   A  1 344 ? 30.52720  9.00182   -39.87299 1.000 33.10496  ?  344 TYR   I CD1 1 
ATOM   2300  C CD2 . TYR   A  1 344 ? 29.87869  11.12679  -39.00245 1.000 42.33063  ?  344 TYR   I CD2 1 
ATOM   2301  C CE1 . TYR   A  1 344 ? 31.86408  9.37494   -39.81476 1.000 33.30403  ?  344 TYR   I CE1 1 
ATOM   2302  C CE2 . TYR   A  1 344 ? 31.22062  11.51782  -38.94008 1.000 32.40127  ?  344 TYR   I CE2 1 
ATOM   2303  C CZ  . TYR   A  1 344 ? 32.20067  10.63567  -39.34897 1.000 50.67096  ?  344 TYR   I CZ  1 
ATOM   2304  O OH  . TYR   A  1 344 ? 33.51935  11.01088  -39.30061 1.000 45.71043  ?  344 TYR   I OH  1 
ATOM   2305  N N   . PHE   A  1 345 ? 27.42540  10.42091  -36.71313 1.000 23.90602  ?  345 PHE   I N   1 
ATOM   2306  C CA  . PHE   A  1 345 ? 27.97008  11.21291  -35.61295 1.000 32.95436  ?  345 PHE   I CA  1 
ATOM   2307  C C   . PHE   A  1 345 ? 27.47222  10.76010  -34.24378 1.000 38.13375  ?  345 PHE   I C   1 
ATOM   2308  O O   . PHE   A  1 345 ? 27.97768  11.25000  -33.22617 1.000 34.47691  ?  345 PHE   I O   1 
ATOM   2309  C CB  . PHE   A  1 345 ? 27.75134  12.73714  -35.82964 1.000 23.45539  ?  345 PHE   I CB  1 
ATOM   2310  C CG  . PHE   A  1 345 ? 26.30905  13.22758  -35.76448 1.000 36.66043  ?  345 PHE   I CG  1 
ATOM   2311  C CD1 . PHE   A  1 345 ? 25.57062  13.17939  -34.58767 1.000 41.87055  ?  345 PHE   I CD1 1 
ATOM   2312  C CD2 . PHE   A  1 345 ? 25.73745  13.85318  -36.86940 1.000 30.20908  ?  345 PHE   I CD2 1 
ATOM   2313  C CE1 . PHE   A  1 345 ? 24.25699  13.67655  -34.54189 1.000 26.05349  ?  345 PHE   I CE1 1 
ATOM   2314  C CE2 . PHE   A  1 345 ? 24.42563  14.36163  -36.83809 1.000 31.67622  ?  345 PHE   I CE2 1 
ATOM   2315  C CZ  . PHE   A  1 345 ? 23.68371  14.27508  -35.67654 1.000 33.97395  ?  345 PHE   I CZ  1 
ATOM   2316  N N   . SER   A  1 346 ? 26.55273  9.79767   -34.18251 1.000 20.13646  ?  346 SER   I N   1 
ATOM   2317  C CA  . SER   A  1 346 ? 26.30629  9.12573   -32.91266 1.000 42.34373  ?  346 SER   I CA  1 
ATOM   2318  C C   . SER   A  1 346 ? 27.59071  8.50068   -32.38083 1.000 29.71576  ?  346 SER   I C   1 
ATOM   2319  O O   . SER   A  1 346 ? 27.74884  8.33337   -31.16384 1.000 29.71868  ?  346 SER   I O   1 
ATOM   2320  C CB  . SER   A  1 346 ? 25.22813  8.05705   -33.07982 1.000 29.12124  ?  346 SER   I CB  1 
ATOM   2321  O OG  . SER   A  1 346 ? 25.76816  6.91864   -33.73543 1.000 25.72770  ?  346 SER   I OG  1 
ATOM   2322  N N   . ASN   A  1 347 ? 28.52851  8.17877   -33.28204 1.000 35.68090  ?  347 ASN   I N   1 
ATOM   2323  C CA  . ASN   A  1 347 ? 29.80396  7.59384   -32.88295 1.000 16.78204  ?  347 ASN   I CA  1 
ATOM   2324  C C   . ASN   A  1 347 ? 30.71685  8.59205   -32.17442 1.000 33.65392  ?  347 ASN   I C   1 
ATOM   2325  O O   . ASN   A  1 347 ? 31.56547  8.17807   -31.37189 1.000 33.99648  ?  347 ASN   I O   1 
ATOM   2326  C CB  . ASN   A  1 347 ? 30.52007  7.01899   -34.10704 1.000 24.30215  ?  347 ASN   I CB  1 
ATOM   2327  C CG  . ASN   A  1 347 ? 29.79621  5.82909   -34.69842 1.000 39.44755  ?  347 ASN   I CG  1 
ATOM   2328  O OD1 . ASN   A  1 347 ? 29.62526  4.79534   -34.04146 1.000 30.58292  ?  347 ASN   I OD1 1 
ATOM   2329  N ND2 . ASN   A  1 347 ? 29.37549  5.95955   -35.94775 1.000 21.31409  ?  347 ASN   I ND2 1 
ATOM   2330  N N   . ILE   A  1 348 ? 30.57141  9.89549   -32.44942 1.000 28.50496  ?  348 ILE   I N   1 
ATOM   2331  C CA  . ILE   A  1 348 ? 31.58805  10.86190  -32.02624 1.000 21.50034  ?  348 ILE   I CA  1 
ATOM   2332  C C   . ILE   A  1 348 ? 31.03207  12.11020  -31.33909 1.000 32.57966  ?  348 ILE   I C   1 
ATOM   2333  O O   . ILE   A  1 348 ? 31.79527  12.90017  -30.77025 1.000 36.05124  ?  348 ILE   I O   1 
ATOM   2334  C CB  . ILE   A  1 348 ? 32.44736  11.27007  -33.23335 1.000 30.48391  ?  348 ILE   I CB  1 
ATOM   2335  C CG1 . ILE   A  1 348 ? 31.55426  11.85810  -34.32912 1.000 19.01435  ?  348 ILE   I CG1 1 
ATOM   2336  C CG2 . ILE   A  1 348 ? 33.24661  10.07063  -33.74970 1.000 16.92104  ?  348 ILE   I CG2 1 
ATOM   2337  C CD1 . ILE   A  1 348 ? 32.34745  12.54543  -35.43175 1.000 41.56866  ?  348 ILE   I CD1 1 
ATOM   2338  N N   . ALA   A  1 349 ? 29.71911  12.31408  -31.39300 1.000 26.75357  ?  349 ALA   I N   1 
ATOM   2339  C CA  . ALA   A  1 349 ? 29.14075  13.53031  -30.83170 1.000 27.21633  ?  349 ALA   I CA  1 
ATOM   2340  C C   . ALA   A  1 349 ? 29.14446  13.49127  -29.30600 1.000 30.39832  ?  349 ALA   I C   1 
ATOM   2341  O O   . ALA   A  1 349 ? 29.08842  12.42103  -28.68619 1.000 35.33412  ?  349 ALA   I O   1 
ATOM   2342  C CB  . ALA   A  1 349 ? 27.70140  13.72237  -31.32038 1.000 12.41701  ?  349 ALA   I CB  1 
ATOM   2343  N N   . ALA   A  1 350 ? 29.20588  14.67660  -28.69696 1.000 26.60155  ?  350 ALA   I N   1 
ATOM   2344  C CA  . ALA   A  1 350 ? 28.93228  14.78113  -27.26695 1.000 29.08792  ?  350 ALA   I CA  1 
ATOM   2345  C C   . ALA   A  1 350 ? 27.62925  14.05980  -26.92710 1.000 35.02721  ?  350 ALA   I C   1 
ATOM   2346  O O   . ALA   A  1 350 ? 26.58455  14.30867  -27.53822 1.000 28.55679  ?  350 ALA   I O   1 
ATOM   2347  C CB  . ALA   A  1 350 ? 28.84628  16.24685  -26.85797 1.000 14.96154  ?  350 ALA   I CB  1 
ATOM   2348  N N   . ARG   A  1 351 ? 27.70091  13.15050  -25.96160 1.000 20.01041  ?  351 ARG   I N   1 
ATOM   2349  C CA  . ARG   A  1 351 ? 26.61656  12.20574  -25.75169 1.000 30.26455  ?  351 ARG   I CA  1 
ATOM   2350  C C   . ARG   A  1 351 ? 26.71621  11.63522  -24.34454 1.000 22.60141  ?  351 ARG   I C   1 
ATOM   2351  O O   . ARG   A  1 351 ? 27.75867  11.73115  -23.68015 1.000 36.83673  ?  351 ARG   I O   1 
ATOM   2352  C CB  . ARG   A  1 351 ? 26.64717  11.08381  -26.80848 1.000 15.98470  ?  351 ARG   I CB  1 
ATOM   2353  C CG  . ARG   A  1 351 ? 27.88910  10.22241  -26.75095 1.000 15.99043  ?  351 ARG   I CG  1 
ATOM   2354  C CD  . ARG   A  1 351 ? 28.09685  9.44407   -28.04006 1.000 23.90552  ?  351 ARG   I CD  1 
ATOM   2355  N NE  . ARG   A  1 351 ? 29.25343  8.55854   -27.95233 1.000 25.46961  ?  351 ARG   I NE  1 
ATOM   2356  C CZ  . ARG   A  1 351 ? 30.51338  8.94445   -28.12296 1.000 46.99108  ?  351 ARG   I CZ  1 
ATOM   2357  N NH1 . ARG   A  1 351 ? 30.82975  10.20243  -28.39759 1.000 25.73995  ?  351 ARG   I NH1 1 
ATOM   2358  N NH2 . ARG   A  1 351 ? 31.48435  8.04398   -28.01967 1.000 21.10688  ?  351 ARG   I NH2 1 
ATOM   2359  N N   . GLN   A  1 352 ? 25.60214  11.05945  -23.88920 1.000 30.15541  ?  352 GLN   I N   1 
ATOM   2360  C CA  . GLN   A  1 352 ? 25.56419  10.33477  -22.62551 1.000 23.51505  ?  352 GLN   I CA  1 
ATOM   2361  C C   . GLN   A  1 352 ? 25.10162  8.91474   -22.89657 1.000 35.69128  ?  352 GLN   I C   1 
ATOM   2362  O O   . GLN   A  1 352 ? 24.10949  8.70219   -23.60966 1.000 34.56993  ?  352 GLN   I O   1 
ATOM   2363  C CB  . GLN   A  1 352 ? 24.64521  10.99072  -21.60619 1.000 33.68007  ?  352 GLN   I CB  1 
ATOM   2364  C CG  . GLN   A  1 352 ? 24.55200  10.20400  -20.30870 1.000 28.73358  ?  352 GLN   I CG  1 
ATOM   2365  C CD  . GLN   A  1 352 ? 23.54050  10.81723  -19.35148 1.000 37.07990  ?  352 GLN   I CD  1 
ATOM   2366  O OE1 . GLN   A  1 352 ? 22.44260  10.29493  -19.17354 1.000 39.13883  ?  352 GLN   I OE1 1 
ATOM   2367  N NE2 . GLN   A  1 352 ? 23.90379  11.94024  -18.74438 1.000 26.24508  ?  352 GLN   I NE2 1 
ATOM   2368  N N   . ILE   A  1 353 ? 25.85691  7.95373   -22.37211 1.000 27.30235  ?  353 ILE   I N   1 
ATOM   2369  C CA  . ILE   A  1 353 ? 25.56133  6.53188   -22.49948 1.000 30.12537  ?  353 ILE   I CA  1 
ATOM   2370  C C   . ILE   A  1 353 ? 24.93777  6.08271   -21.19305 1.000 23.14233  ?  353 ILE   I C   1 
ATOM   2371  O O   . ILE   A  1 353 ? 25.46476  6.38911   -20.11292 1.000 37.23264  ?  353 ILE   I O   1 
ATOM   2372  C CB  . ILE   A  1 353 ? 26.83798  5.72272   -22.77944 1.000 28.02740  ?  353 ILE   I CB  1 
ATOM   2373  C CG1 . ILE   A  1 353 ? 27.51581  6.18800   -24.07194 1.000 35.26919  ?  353 ILE   I CG1 1 
ATOM   2374  C CG2 . ILE   A  1 353 ? 26.52395  4.22954   -22.75510 1.000 18.89100  ?  353 ILE   I CG2 1 
ATOM   2375  C CD1 . ILE   A  1 353 ? 28.98869  5.86467   -24.11702 1.000 15.44056  ?  353 ILE   I CD1 1 
ATOM   2376  N N   . MET   A  1 354 ? 23.82494  5.36200   -21.27112 1.000 20.02937  ?  354 MET   I N   1 
ATOM   2377  C CA  . MET   A  1 354 ? 23.16731  4.86680   -20.06629 1.000 25.33617  ?  354 MET   I CA  1 
ATOM   2378  C C   . MET   A  1 354 ? 22.87412  3.38301   -20.23568 1.000 30.43057  ?  354 MET   I C   1 
ATOM   2379  O O   . MET   A  1 354 ? 22.17373  2.98871   -21.17699 1.000 31.90075  ?  354 MET   I O   1 
ATOM   2380  C CB  . MET   A  1 354 ? 21.89292  5.65783   -19.77904 1.000 14.35230  ?  354 MET   I CB  1 
ATOM   2381  C CG  . MET   A  1 354 ? 21.26314  5.38173   -18.42125 1.000 36.19475  ?  354 MET   I CG  1 
ATOM   2382  S SD  . MET   A  1 354 ? 19.76673  6.35624   -18.19449 1.000 33.43374  ?  354 MET   I SD  1 
ATOM   2383  C CE  . MET   A  1 354 ? 20.49923  7.97275   -17.90485 1.000 31.64011  ?  354 MET   I CE  1 
ATOM   2384  N N   . PHE   A  1 355 ? 23.44140  2.55905   -19.35338 1.000 28.06029  ?  355 PHE   I N   1 
ATOM   2385  C CA  . PHE   A  1 355 ? 23.18998  1.11985   -19.35113 1.000 29.69131  ?  355 PHE   I CA  1 
ATOM   2386  C C   . PHE   A  1 355 ? 22.11451  0.80020   -18.32705 1.000 28.43109  ?  355 PHE   I C   1 
ATOM   2387  O O   . PHE   A  1 355 ? 22.19358  1.24745   -17.17487 1.000 33.04217  ?  355 PHE   I O   1 
ATOM   2388  C CB  . PHE   A  1 355 ? 24.46351  0.33651   -19.03213 1.000 33.54948  ?  355 PHE   I CB  1 
ATOM   2389  C CG  . PHE   A  1 355 ? 25.47381  0.39391   -20.11572 1.000 35.40888  ?  355 PHE   I CG  1 
ATOM   2390  C CD1 . PHE   A  1 355 ? 25.33141  -0.40089  -21.24330 1.000 22.45227  ?  355 PHE   I CD1 1 
ATOM   2391  C CD2 . PHE   A  1 355 ? 26.55159  1.25454   -20.02704 1.000 31.14644  ?  355 PHE   I CD2 1 
ATOM   2392  C CE1 . PHE   A  1 355 ? 26.25732  -0.35492  -22.27089 1.000 35.33035  ?  355 PHE   I CE1 1 
ATOM   2393  C CE2 . PHE   A  1 355 ? 27.48193  1.30942   -21.04459 1.000 18.31123  ?  355 PHE   I CE2 1 
ATOM   2394  C CZ  . PHE   A  1 355 ? 27.33942  0.49617   -22.17113 1.000 19.86994  ?  355 PHE   I CZ  1 
ATOM   2395  N N   . ILE   A  1 356 ? 21.10900  0.04041   -18.74022 1.000 29.03637  ?  356 ILE   I N   1 
ATOM   2396  C CA  . ILE   A  1 356 ? 20.01676  -0.31975  -17.84686 1.000 32.39555  ?  356 ILE   I CA  1 
ATOM   2397  C C   . ILE   A  1 356 ? 19.87439  -1.82866  -17.82387 1.000 45.33602  ?  356 ILE   I C   1 
ATOM   2398  O O   . ILE   A  1 356 ? 19.94845  -2.48344  -18.87270 1.000 32.07624  ?  356 ILE   I O   1 
ATOM   2399  C CB  . ILE   A  1 356 ? 18.69335  0.34884   -18.25805 1.000 26.47659  ?  356 ILE   I CB  1 
ATOM   2400  C CG1 . ILE   A  1 356 ? 18.87026  1.87902   -18.23483 1.000 25.77692  ?  356 ILE   I CG1 1 
ATOM   2401  C CG2 . ILE   A  1 356 ? 17.57051  -0.12677  -17.32834 1.000 29.51526  ?  356 ILE   I CG2 1 
ATOM   2402  C CD1 . ILE   A  1 356 ? 17.66457  2.66082   -18.76631 1.000 19.88195  ?  356 ILE   I CD1 1 
ATOM   2403  N N   . GLU   A  1 357 ? 19.68766  -2.38162  -16.62074 1.000 21.72068  ?  357 GLU   I N   1 
ATOM   2404  C CA  . GLU   A  1 357 ? 19.38906  -3.80154  -16.45871 1.000 36.71343  ?  357 GLU   I CA  1 
ATOM   2405  C C   . GLU   A  1 357 ? 17.87705  -3.97252  -16.28314 1.000 34.91931  ?  357 GLU   I C   1 
ATOM   2406  O O   . GLU   A  1 357 ? 17.32666  -3.67737  -15.21181 1.000 33.60729  ?  357 GLU   I O   1 
ATOM   2407  C CB  . GLU   A  1 357 ? 20.16236  -4.38322  -15.28218 1.000 27.22869  ?  357 GLU   I CB  1 
ATOM   2408  C CG  . GLU   A  1 357 ? 19.91191  -5.87672  -15.04083 1.000 26.00873  ?  357 GLU   I CG  1 
ATOM   2409  C CD  . GLU   A  1 357 ? 20.63289  -6.78704  -16.02641 1.000 79.30869  ?  357 GLU   I CD  1 
ATOM   2410  O OE1 . GLU   A  1 357 ? 21.82174  -6.51886  -16.33426 1.000 61.83807  ?  357 GLU   I OE1 1 
ATOM   2411  O OE2 . GLU   A  1 357 ? 20.01181  -7.78291  -16.47795 1.000 48.91731  ?  357 GLU   I OE2 1 
ATOM   2412  N N   . ALA   A  1 358 ? 17.21482  -4.43821  -17.34791 1.000 23.40975  ?  358 ALA   I N   1 
ATOM   2413  C CA  . ALA   A  1 358 ? 15.77293  -4.67021  -17.33146 1.000 42.27142  ?  358 ALA   I CA  1 
ATOM   2414  C C   . ALA   A  1 358 ? 15.41134  -5.71832  -16.29343 1.000 36.69899  ?  358 ALA   I C   1 
ATOM   2415  O O   . ALA   A  1 358 ? 16.09092  -6.74081  -16.16630 1.000 62.69366  ?  358 ALA   I O   1 
ATOM   2416  C CB  . ALA   A  1 358 ? 15.28881  -5.14238  -18.70561 1.000 30.91187  ?  358 ALA   I CB  1 
ATOM   2417  N N   . ASP   A  1 359 ? 14.32948  -5.45829  -15.55026 1.000 51.65064  ?  359 ASP   I N   1 
ATOM   2418  C CA  . ASP   A  1 359 ? 13.82536  -6.44987  -14.60049 1.000 46.96211  ?  359 ASP   I CA  1 
ATOM   2419  C C   . ASP   A  1 359 ? 13.52060  -7.77340  -15.29749 1.000 29.11525  ?  359 ASP   I C   1 
ATOM   2420  O O   . ASP   A  1 359 ? 13.74813  -8.85040  -14.73407 1.000 35.87878  ?  359 ASP   I O   1 
ATOM   2421  C CB  . ASP   A  1 359 ? 12.57583  -5.92704  -13.87903 1.000 26.02538  ?  359 ASP   I CB  1 
ATOM   2422  C CG  . ASP   A  1 359 ? 12.87248  -4.75109  -12.93789 1.000 63.31450  ?  359 ASP   I CG  1 
ATOM   2423  O OD1 . ASP   A  1 359 ? 14.06255  -4.50277  -12.63485 1.000 43.33900  ?  359 ASP   I OD1 1 
ATOM   2424  O OD2 . ASP   A  1 359 ? 11.90962  -4.05886  -12.51502 1.000 37.04933  ?  359 ASP   I OD2 1 
ATOM   2425  N N   . ASN   A  1 360 ? 13.02245  -7.71821  -16.52413 1.000 36.64739  ?  360 ASN   I N   1 
ATOM   2426  C CA  . ASN   A  1 360 ? 12.75340  -8.93481  -17.28128 1.000 27.89942  ?  360 ASN   I CA  1 
ATOM   2427  C C   . ASN   A  1 360 ? 14.07418  -9.50644  -17.79678 1.000 38.86445  ?  360 ASN   I C   1 
ATOM   2428  O O   . ASN   A  1 360 ? 14.69905  -8.92965  -18.69736 1.000 49.53726  ?  360 ASN   I O   1 
ATOM   2429  C CB  . ASN   A  1 360 ? 11.78827  -8.63501  -18.42682 1.000 29.17996  ?  360 ASN   I CB  1 
ATOM   2430  C CG  . ASN   A  1 360 ? 11.28554  -9.88096  -19.09240 1.000 47.96591  ?  360 ASN   I CG  1 
ATOM   2431  O OD1 . ASN   A  1 360 ? 12.05468  -10.80908 -19.36977 1.000 51.07027  ?  360 ASN   I OD1 1 
ATOM   2432  N ND2 . ASN   A  1 360 ? 9.97884   -9.92667  -19.34350 1.000 53.92894  ?  360 ASN   I ND2 1 
ATOM   2433  N N   . LYS   A  1 361 ? 14.48197  -10.65641 -17.24719 1.000 46.58849  ?  361 LYS   I N   1 
ATOM   2434  C CA  . LYS   A  1 361 ? 15.76848  -11.25594 -17.59548 1.000 54.35736  ?  361 LYS   I CA  1 
ATOM   2435  C C   . LYS   A  1 361 ? 15.88860  -11.57667 -19.08240 1.000 26.67447  ?  361 LYS   I C   1 
ATOM   2436  O O   . LYS   A  1 361 ? 17.01097  -11.63174 -19.60308 1.000 77.05777  ?  361 LYS   I O   1 
ATOM   2437  C CB  . LYS   A  1 361 ? 16.00281  -12.52051 -16.75889 1.000 30.83101  ?  361 LYS   I CB  1 
ATOM   2438  C CG  . LYS   A  1 361 ? 16.37949  -12.29585 -15.28463 1.000 101.75023 ?  361 LYS   I CG  1 
ATOM   2439  C CD  . LYS   A  1 361 ? 15.14839  -12.38842 -14.47509 1.000 120.51436 ?  361 LYS   I CD  1 
ATOM   2440  C CE  . LYS   A  1 361 ? 14.92341  -13.82396 -14.02034 1.000 137.58258 ?  361 LYS   I CE  1 
ATOM   2441  N NZ  . LYS   A  1 361 ? 13.61430  -14.04455 -13.25279 1.000 118.20650 ?  361 LYS   I NZ  1 
ATOM   2442  N N   . GLU   A  1 362 ? 14.76773  -11.76401 -19.77908 1.000 42.12114  ?  362 GLU   I N   1 
ATOM   2443  C CA  . GLU   A  1 362 ? 14.78811  -12.02993 -21.21501 1.000 37.58475  ?  362 GLU   I CA  1 
ATOM   2444  C C   . GLU   A  1 362 ? 15.11198  -10.78931 -22.04084 1.000 57.86699  ?  362 GLU   I C   1 
ATOM   2445  O O   . GLU   A  1 362 ? 15.36569  -10.91060 -23.24833 1.000 50.12948  ?  362 GLU   I O   1 
ATOM   2446  C CB  . GLU   A  1 362 ? 13.43921  -12.60943 -21.66682 1.000 46.44333  ?  362 GLU   I CB  1 
ATOM   2447  N N   . ILE   A  1 363 ? 15.06580  -9.60888  -21.42873 1.000 32.19564  ?  363 ILE   I N   1 
ATOM   2448  C CA  . ILE   A  1 363 ? 15.50377  -8.37202  -22.05454 1.000 50.16364  ?  363 ILE   I CA  1 
ATOM   2449  C C   . ILE   A  1 363 ? 16.89668  -7.99137  -21.57188 1.000 38.65513  ?  363 ILE   I C   1 
ATOM   2450  O O   . ILE   A  1 363 ? 17.77807  -7.66645  -22.37041 1.000 47.00826  ?  363 ILE   I O   1 
ATOM   2451  C CB  . ILE   A  1 363 ? 14.46248  -7.26032  -21.77137 1.000 40.40013  ?  363 ILE   I CB  1 
ATOM   2452  C CG1 . ILE   A  1 363 ? 13.17166  -7.52735  -22.55202 1.000 34.30746  ?  363 ILE   I CG1 1 
ATOM   2453  C CG2 . ILE   A  1 363 ? 14.98608  -5.89167  -22.15385 1.000 20.18334  ?  363 ILE   I CG2 1 
ATOM   2454  C CD1 . ILE   A  1 363 ? 12.05461  -6.52952  -22.25625 1.000 37.70897  ?  363 ILE   I CD1 1 
ATOM   2455  N N   . GLY   A  1 364 ? 17.10518  -8.08232  -20.26455 1.000 38.01063  ?  364 GLY   I N   1 
ATOM   2456  C CA  . GLY   A  1 364 ? 18.42081  -8.02171  -19.70497 1.000 25.90638  ?  364 GLY   I CA  1 
ATOM   2457  C C   . GLY   A  1 364 ? 19.05710  -6.65214  -19.82457 1.000 71.14931  ?  364 GLY   I C   1 
ATOM   2458  O O   . GLY   A  1 364 ? 18.41013  -5.60691  -19.67039 1.000 35.74010  ?  364 GLY   I O   1 
ATOM   2459  N N   . LEU   A  1 365 ? 20.36110  -6.66814  -20.08649 1.000 46.82434  ?  365 LEU   I N   1 
ATOM   2460  C CA  . LEU   A  1 365 ? 21.10943  -5.42932  -20.21066 1.000 23.71229  ?  365 LEU   I CA  1 
ATOM   2461  C C   . LEU   A  1 365 ? 20.76266  -4.76322  -21.53648 1.000 48.36794  ?  365 LEU   I C   1 
ATOM   2462  O O   . LEU   A  1 365 ? 20.78869  -5.40633  -22.59219 1.000 35.66912  ?  365 LEU   I O   1 
ATOM   2463  C CB  . LEU   A  1 365 ? 22.61150  -5.70835  -20.11997 1.000 37.81514  ?  365 LEU   I CB  1 
ATOM   2464  C CG  . LEU   A  1 365 ? 23.49412  -4.46590  -19.97484 1.000 41.37363  ?  365 LEU   I CG  1 
ATOM   2465  C CD1 . LEU   A  1 365 ? 23.14586  -3.72903  -18.67760 1.000 28.60812  ?  365 LEU   I CD1 1 
ATOM   2466  C CD2 . LEU   A  1 365 ? 24.95706  -4.84789  -20.02915 1.000 27.64544  ?  365 LEU   I CD2 1 
ATOM   2467  N N   . ILE   A  1 366 ? 20.38872  -3.48540  -21.47481 1.000 20.61460  ?  366 ILE   I N   1 
ATOM   2468  C CA  . ILE   A  1 366 ? 20.15703  -2.67697  -22.66245 1.000 34.94291  ?  366 ILE   I CA  1 
ATOM   2469  C C   . ILE   A  1 366 ? 21.01827  -1.43508  -22.52208 1.000 37.25489  ?  366 ILE   I C   1 
ATOM   2470  O O   . ILE   A  1 366 ? 21.55722  -1.14398  -21.45069 1.000 32.77942  ?  366 ILE   I O   1 
ATOM   2471  C CB  . ILE   A  1 366 ? 18.67260  -2.28050  -22.86014 1.000 28.30499  ?  366 ILE   I CB  1 
ATOM   2472  C CG1 . ILE   A  1 366 ? 18.21506  -1.34443  -21.74916 1.000 31.82937  ?  366 ILE   I CG1 1 
ATOM   2473  C CG2 . ILE   A  1 366 ? 17.76593  -3.49066  -22.92370 1.000 20.24841  ?  366 ILE   I CG2 1 
ATOM   2474  C CD1 . ILE   A  1 366 ? 16.96744  -0.59383  -22.10756 1.000 32.59956  ?  366 ILE   I CD1 1 
ATOM   2475  N N   . PHE   A  1 367 ? 21.14555  -0.68972  -23.61359 1.000 29.98435  ?  367 PHE   I N   1 
ATOM   2476  C CA  . PHE   A  1 367 ? 21.76418  0.61902   -23.49493 1.000 26.95279  ?  367 PHE   I CA  1 
ATOM   2477  C C   . PHE   A  1 367 ? 20.90989  1.66882   -24.19103 1.000 36.22771  ?  367 PHE   I C   1 
ATOM   2478  O O   . PHE   A  1 367 ? 20.11734  1.37941   -25.09393 1.000 31.73417  ?  367 PHE   I O   1 
ATOM   2479  C CB  . PHE   A  1 367 ? 23.25426  0.63679   -24.00263 1.000 25.92083  ?  367 PHE   I CB  1 
ATOM   2480  C CG  . PHE   A  1 367 ? 23.43661  0.60241   -25.51250 1.000 17.92581  ?  367 PHE   I CG  1 
ATOM   2481  C CD1 . PHE   A  1 367 ? 23.09100  1.69800   -26.30967 1.000 34.21875  ?  367 PHE   I CD1 1 
ATOM   2482  C CD2 . PHE   A  1 367 ? 24.05850  -0.48814  -26.12129 1.000 29.36734  ?  367 PHE   I CD2 1 
ATOM   2483  C CE1 . PHE   A  1 367 ? 23.29193  1.68024   -27.69103 1.000 18.37469  ?  367 PHE   I CE1 1 
ATOM   2484  C CE2 . PHE   A  1 367 ? 24.28137  -0.51533  -27.51302 1.000 27.42863  ?  367 PHE   I CE2 1 
ATOM   2485  C CZ  . PHE   A  1 367 ? 23.90403  0.56614   -28.30042 1.000 24.15078  ?  367 PHE   I CZ  1 
ATOM   2486  N N   . LEU   A  1 368 ? 21.05761  2.88722   -23.70474 1.000 30.02010  ?  368 LEU   I N   1 
ATOM   2487  C CA  . LEU   A  1 368 ? 20.55006  4.09079   -24.32834 1.000 20.97608  ?  368 LEU   I CA  1 
ATOM   2488  C C   . LEU   A  1 368 ? 21.74027  5.01479   -24.55749 1.000 21.72500  ?  368 LEU   I C   1 
ATOM   2489  O O   . LEU   A  1 368 ? 22.62286  5.12038   -23.69610 1.000 30.23673  ?  368 LEU   I O   1 
ATOM   2490  C CB  . LEU   A  1 368 ? 19.51012  4.76067   -23.42457 1.000 18.64078  ?  368 LEU   I CB  1 
ATOM   2491  C CG  . LEU   A  1 368 ? 18.15702  4.06782   -23.33055 1.000 29.23704  ?  368 LEU   I CG  1 
ATOM   2492  C CD1 . LEU   A  1 368 ? 17.40311  4.58465   -22.12000 1.000 25.01799  ?  368 LEU   I CD1 1 
ATOM   2493  C CD2 . LEU   A  1 368 ? 17.34323  4.31804   -24.60121 1.000 26.67189  ?  368 LEU   I CD2 1 
ATOM   2494  N N   . VAL   A  1 369 ? 21.79151  5.66374   -25.71764 1.000 22.81366  ?  369 VAL   I N   1 
ATOM   2495  C CA  . VAL   A  1 369 ? 22.73042  6.75869   -25.94714 1.000 25.15359  ?  369 VAL   I CA  1 
ATOM   2496  C C   . VAL   A  1 369 ? 21.92045  8.00129   -26.30131 1.000 22.63778  ?  369 VAL   I C   1 
ATOM   2497  O O   . VAL   A  1 369 ? 21.16139  7.99542   -27.28088 1.000 32.08473  ?  369 VAL   I O   1 
ATOM   2498  C CB  . VAL   A  1 369 ? 23.75228  6.44082   -27.05271 1.000 31.38513  ?  369 VAL   I CB  1 
ATOM   2499  C CG1 . VAL   A  1 369 ? 24.75822  7.60338   -27.17938 1.000 21.15264  ?  369 VAL   I CG1 1 
ATOM   2500  C CG2 . VAL   A  1 369 ? 24.46664  5.13720   -26.76651 1.000 28.54645  ?  369 VAL   I CG2 1 
ATOM   2501  N N   . PHE   A  1 370 ? 22.08824  9.06795   -25.52219 1.000 30.42567  ?  370 PHE   I N   1 
ATOM   2502  C CA  . PHE   A  1 370 ? 21.46898  10.35074  -25.83907 1.000 12.07073  ?  370 PHE   I CA  1 
ATOM   2503  C C   . PHE   A  1 370 ? 22.48872  11.22384  -26.57065 1.000 25.91149  ?  370 PHE   I C   1 
ATOM   2504  O O   . PHE   A  1 370 ? 23.56779  11.51666  -26.03802 1.000 24.13421  ?  370 PHE   I O   1 
ATOM   2505  C CB  . PHE   A  1 370 ? 20.93208  11.00536  -24.56522 1.000 19.55454  ?  370 PHE   I CB  1 
ATOM   2506  C CG  . PHE   A  1 370 ? 19.88303  10.17692  -23.89621 1.000 29.56211  ?  370 PHE   I CG  1 
ATOM   2507  C CD1 . PHE   A  1 370 ? 18.58865  10.14065  -24.40482 1.000 20.08697  ?  370 PHE   I CD1 1 
ATOM   2508  C CD2 . PHE   A  1 370 ? 20.19727  9.37260   -22.80620 1.000 34.34945  ?  370 PHE   I CD2 1 
ATOM   2509  C CE1 . PHE   A  1 370 ? 17.60951  9.33453   -23.82180 1.000 30.24607  ?  370 PHE   I CE1 1 
ATOM   2510  C CE2 . PHE   A  1 370 ? 19.21425  8.56454   -22.20327 1.000 18.73165  ?  370 PHE   I CE2 1 
ATOM   2511  C CZ  . PHE   A  1 370 ? 17.92598  8.53958   -22.71922 1.000 29.73964  ?  370 PHE   I CZ  1 
ATOM   2512  N N   . ILE   A  1 371 ? 22.15835  11.61206  -27.79997 1.000 30.31501  ?  371 ILE   I N   1 
ATOM   2513  C CA  . ILE   A  1 371 ? 23.13081  12.12831  -28.76475 1.000 26.09372  ?  371 ILE   I CA  1 
ATOM   2514  C C   . ILE   A  1 371 ? 22.86912  13.61561  -28.98594 1.000 27.01345  ?  371 ILE   I C   1 
ATOM   2515  O O   . ILE   A  1 371 ? 21.78199  14.00791  -29.43324 1.000 36.92072  ?  371 ILE   I O   1 
ATOM   2516  C CB  . ILE   A  1 371 ? 23.06230  11.34595  -30.08767 1.000 35.20918  ?  371 ILE   I CB  1 
ATOM   2517  C CG1 . ILE   A  1 371 ? 23.21535  9.83907   -29.81777 1.000 24.79691  ?  371 ILE   I CG1 1 
ATOM   2518  C CG2 . ILE   A  1 371 ? 24.11902  11.84697  -31.08220 1.000 20.68205  ?  371 ILE   I CG2 1 
ATOM   2519  C CD1 . ILE   A  1 371 ? 22.50370  8.97405   -30.83940 1.000 22.66406  ?  371 ILE   I CD1 1 
ATOM   2520  N N   . GLY   A  1 372 ? 23.86897  14.44679  -28.67420 1.000 35.91517  ?  372 GLY   I N   1 
ATOM   2521  C CA  . GLY   A  1 372 ? 23.74443  15.87158  -28.91097 1.000 27.21279  ?  372 GLY   I CA  1 
ATOM   2522  C C   . GLY   A  1 372 ? 23.78927  16.22356  -30.38805 1.000 35.54153  ?  372 GLY   I C   1 
ATOM   2523  O O   . GLY   A  1 372 ? 24.26629  15.46132  -31.22951 1.000 35.71370  ?  372 GLY   I O   1 
ATOM   2524  N N   . MET   A  1 373 ? 23.25106  17.39796  -30.69865 1.000 28.24893  ?  373 MET   I N   1 
ATOM   2525  C CA  . MET   A  1 373 ? 23.29229  17.95474  -32.04602 1.000 41.28443  ?  373 MET   I CA  1 
ATOM   2526  C C   . MET   A  1 373 ? 23.48703  19.45145  -31.92012 1.000 39.03628  ?  373 MET   I C   1 
ATOM   2527  O O   . MET   A  1 373 ? 22.64993  20.12981  -31.31036 1.000 34.32838  ?  373 MET   I O   1 
ATOM   2528  C CB  . MET   A  1 373 ? 22.01656  17.65547  -32.82792 1.000 21.28810  ?  373 MET   I CB  1 
ATOM   2529  C CG  . MET   A  1 373 ? 21.81023  16.18626  -33.05146 1.000 43.11211  ?  373 MET   I CG  1 
ATOM   2530  S SD  . MET   A  1 373 ? 20.23015  15.80673  -33.86409 1.000 36.62216  ?  373 MET   I SD  1 
ATOM   2531  C CE  . MET   A  1 373 ? 20.29771  16.89752  -35.28515 1.000 12.40357  ?  373 MET   I CE  1 
ATOM   2532  N N   . THR   A  1 374 ? 24.58026  19.95270  -32.51056 1.000 32.84499  ?  374 THR   I N   1 
ATOM   2533  C CA  . THR   A  1 374 ? 24.99655  21.35393  -32.43323 1.000 34.21668  ?  374 THR   I CA  1 
ATOM   2534  C C   . THR   A  1 374 ? 24.76110  21.90862  -31.02761 1.000 31.12526  ?  374 THR   I C   1 
ATOM   2535  O O   . THR   A  1 374 ? 25.22588  21.31747  -30.04971 1.000 41.74675  ?  374 THR   I O   1 
ATOM   2536  C CB  . THR   A  1 374 ? 24.30305  22.19293  -33.53373 1.000 43.19448  ?  374 THR   I CB  1 
ATOM   2537  O OG1 . THR   A  1 374 ? 22.87692  22.23933  -33.35221 1.000 38.14695  ?  374 THR   I OG1 1 
ATOM   2538  C CG2 . THR   A  1 374 ? 24.58834  21.58874  -34.89870 1.000 27.76744  ?  374 THR   I CG2 1 
ATOM   2539  N N   . GLU   A  1 375 ? 24.03326  23.01477  -30.89541 1.000 40.10507  ?  375 GLU   I N   1 
ATOM   2540  C CA  . GLU   A  1 375 ? 23.89931  23.65131  -29.58495 1.000 27.63650  ?  375 GLU   I CA  1 
ATOM   2541  C C   . GLU   A  1 375 ? 22.95931  22.91600  -28.62039 1.000 42.48360  ?  375 GLU   I C   1 
ATOM   2542  O O   . GLU   A  1 375 ? 22.93195  23.26021  -27.42984 1.000 28.57717  ?  375 GLU   I O   1 
ATOM   2543  C CB  . GLU   A  1 375 ? 23.41611  25.09406  -29.75367 1.000 40.49422  ?  375 GLU   I CB  1 
ATOM   2544  C CG  . GLU   A  1 375 ? 22.03384  25.20754  -30.44285 1.000 29.15046  ?  375 GLU   I CG  1 
ATOM   2545  C CD  . GLU   A  1 375 ? 22.14199  25.58451  -31.93453 1.000 39.51191  ?  375 GLU   I CD  1 
ATOM   2546  O OE1 . GLU   A  1 375 ? 22.69223  24.78184  -32.72506 1.000 44.84573  ?  375 GLU   I OE1 1 
ATOM   2547  O OE2 . GLU   A  1 375 ? 21.67606  26.69096  -32.31274 1.000 43.88847  ?  375 GLU   I OE2 1 
ATOM   2548  N N   . ILE   A  1 376 ? 22.17589  21.93671  -29.08011 1.000 26.01928  ?  376 ILE   I N   1 
ATOM   2549  C CA  . ILE   A  1 376 ? 21.37116  21.15009  -28.14696 1.000 26.24499  ?  376 ILE   I CA  1 
ATOM   2550  C C   . ILE   A  1 376 ? 22.12253  19.86170  -27.82378 1.000 30.11572  ?  376 ILE   I C   1 
ATOM   2551  O O   . ILE   A  1 376 ? 21.82769  18.79490  -28.37406 1.000 37.67424  ?  376 ILE   I O   1 
ATOM   2552  C CB  . ILE   A  1 376 ? 19.96569  20.87362  -28.71073 1.000 37.16487  ?  376 ILE   I CB  1 
ATOM   2553  C CG1 . ILE   A  1 376 ? 19.30370  22.20309  -29.10518 1.000 26.59738  ?  376 ILE   I CG1 1 
ATOM   2554  C CG2 . ILE   A  1 376 ? 19.11918  20.08344  -27.69960 1.000 15.23811  ?  376 ILE   I CG2 1 
ATOM   2555  C CD1 . ILE   A  1 376 ? 18.02687  22.04029  -29.92857 1.000 47.42686  ?  376 ILE   I CD1 1 
ATOM   2556  N N   . SER   A  1 377 ? 23.11289  19.95417  -26.93452 1.000 27.88547  ?  377 SER   I N   1 
ATOM   2557  C CA  . SER   A  1 377 ? 24.03633  18.84934  -26.71916 1.000 41.42434  ?  377 SER   I CA  1 
ATOM   2558  C C   . SER   A  1 377 ? 24.29243  18.53689  -25.25263 1.000 25.41094  ?  377 SER   I C   1 
ATOM   2559  O O   . SER   A  1 377 ? 25.10141  17.65010  -24.95758 1.000 49.64600  ?  377 SER   I O   1 
ATOM   2560  C CB  . SER   A  1 377 ? 25.36919  19.12592  -27.42916 1.000 19.26411  ?  377 SER   I CB  1 
ATOM   2561  O OG  . SER   A  1 377 ? 25.18461  19.00588  -28.83120 1.000 25.34176  ?  377 SER   I OG  1 
ATOM   2562  N N   . THR   A  1 378 ? 23.62167  19.21792  -24.33313 1.000 38.47468  ?  378 THR   I N   1 
ATOM   2563  C CA  . THR   A  1 378 ? 23.72242  18.87552  -22.92264 1.000 24.60021  ?  378 THR   I CA  1 
ATOM   2564  C C   . THR   A  1 378 ? 22.74763  17.74848  -22.56618 1.000 39.96033  ?  378 THR   I C   1 
ATOM   2565  O O   . THR   A  1 378 ? 21.54773  17.81182  -22.88061 1.000 31.69455  ?  378 THR   I O   1 
ATOM   2566  C CB  . THR   A  1 378 ? 23.46505  20.10871  -22.05808 1.000 37.12299  ?  378 THR   I CB  1 
ATOM   2567  O OG1 . THR   A  1 378 ? 24.54203  21.03957  -22.23214 1.000 31.91709  ?  378 THR   I OG1 1 
ATOM   2568  C CG2 . THR   A  1 378 ? 23.40746  19.70759  -20.61307 1.000 12.33471  ?  378 THR   I CG2 1 
ATOM   2569  N N   . CYS   A  1 379 ? 23.27321  16.71616  -21.90382 1.000 24.15110  ?  379 CYS   I N   1 
ATOM   2570  C CA  . CYS   A  1 379 ? 22.52192  15.51094  -21.55400 1.000 22.43327  ?  379 CYS   I CA  1 
ATOM   2571  C C   . CYS   A  1 379 ? 22.51077  15.41000  -20.03353 1.000 30.50332  ?  379 CYS   I C   1 
ATOM   2572  O O   . CYS   A  1 379 ? 23.48472  14.95753  -19.42226 1.000 35.86591  ?  379 CYS   I O   1 
ATOM   2573  C CB  . CYS   A  1 379 ? 23.14680  14.27159  -22.19123 1.000 23.01455  ?  379 CYS   I CB  1 
ATOM   2574  S SG  . CYS   A  1 379 ? 23.24097  14.35157  -24.00272 1.000 34.53977  ?  379 CYS   I SG  1 
ATOM   2575  N N   . GLU   A  1 380 ? 21.41676  15.83870  -19.41661 1.000 33.25066  ?  380 GLU   I N   1 
ATOM   2576  C CA  . GLU   A  1 380 ? 21.27130  15.74638  -17.97142 1.000 18.75446  ?  380 GLU   I CA  1 
ATOM   2577  C C   . GLU   A  1 380 ? 20.49552  14.48564  -17.60893 1.000 35.04714  ?  380 GLU   I C   1 
ATOM   2578  O O   . GLU   A  1 380 ? 19.31931  14.34584  -17.97571 1.000 33.90685  ?  380 GLU   I O   1 
ATOM   2579  C CB  . GLU   A  1 380 ? 20.56620  16.96482  -17.38783 1.000 30.23104  ?  380 GLU   I CB  1 
ATOM   2580  C CG  . GLU   A  1 380 ? 20.37825  16.78435  -15.90498 1.000 43.00186  ?  380 GLU   I CG  1 
ATOM   2581  C CD  . GLU   A  1 380 ? 19.58023  17.87593  -15.25657 1.000 38.77630  ?  380 GLU   I CD  1 
ATOM   2582  O OE1 . GLU   A  1 380 ? 18.98811  18.70037  -15.99057 1.000 43.80225  ?  380 GLU   I OE1 1 
ATOM   2583  O OE2 . GLU   A  1 380 ? 19.55029  17.88880  -14.00601 1.000 50.89267  ?  380 GLU   I OE2 1 
ATOM   2584  N N   . ALA   A  1 381 ? 21.15853  13.57525  -16.89215 1.000 25.93560  ?  381 ALA   I N   1 
ATOM   2585  C CA  . ALA   A  1 381 ? 20.46990  12.48226  -16.21624 1.000 44.43375  ?  381 ALA   I CA  1 
ATOM   2586  C C   . ALA   A  1 381 ? 19.87668  12.98708  -14.90057 1.000 34.82353  ?  381 ALA   I C   1 
ATOM   2587  O O   . ALA   A  1 381 ? 20.54580  13.69284  -14.13292 1.000 35.43906  ?  381 ALA   I O   1 
ATOM   2588  C CB  . ALA   A  1 381 ? 21.43388  11.31987  -15.95351 1.000 24.91538  ?  381 ALA   I CB  1 
ATOM   2589  N N   . THR   A  1 382 ? 18.61717  12.63660  -14.64354 1.000 31.54987  ?  382 THR   I N   1 
ATOM   2590  C CA  . THR   A  1 382 ? 18.00209  12.86775  -13.33828 1.000 31.13192  ?  382 THR   I CA  1 
ATOM   2591  C C   . THR   A  1 382 ? 17.81732  11.57425  -12.54378 1.000 26.26513  ?  382 THR   I C   1 
ATOM   2592  O O   . THR   A  1 382 ? 17.03160  11.53600  -11.59110 1.000 53.80721  ?  382 THR   I O   1 
ATOM   2593  C CB  . THR   A  1 382 ? 16.66864  13.58692  -13.50855 1.000 20.84437  ?  382 THR   I CB  1 
ATOM   2594  O OG1 . THR   A  1 382 ? 15.79416  12.79978  -14.34385 1.000 29.73608  ?  382 THR   I OG1 1 
ATOM   2595  C CG2 . THR   A  1 382 ? 16.90100  14.96103  -14.14207 1.000 31.63201  ?  382 THR   I CG2 1 
ATOM   2596  N N   . VAL   A  1 383 ? 18.49943  10.50555  -12.94899 1.000 36.30067  ?  383 VAL   I N   1 
ATOM   2597  C CA  . VAL   A  1 383 ? 18.53494  9.25405   -12.21190 1.000 25.63889  ?  383 VAL   I CA  1 
ATOM   2598  C C   . VAL   A  1 383 ? 19.98536  8.98081   -11.83360 1.000 39.64089  ?  383 VAL   I C   1 
ATOM   2599  O O   . VAL   A  1 383 ? 20.91859  9.59077   -12.36056 1.000 35.39271  ?  383 VAL   I O   1 
ATOM   2600  C CB  . VAL   A  1 383 ? 17.95040  8.06873   -13.00507 1.000 46.35126  ?  383 VAL   I CB  1 
ATOM   2601  C CG1 . VAL   A  1 383 ? 16.48218  8.27910   -13.26706 1.000 26.40454  ?  383 VAL   I CG1 1 
ATOM   2602  C CG2 . VAL   A  1 383 ? 18.71514  7.87068   -14.30573 1.000 31.11361  ?  383 VAL   I CG2 1 
ATOM   2603  N N   . SER   A  1 384 ? 20.16442  8.05446   -10.89998 1.000 45.34872  ?  384 SER   I N   1 
ATOM   2604  C CA  . SER   A  1 384 ? 21.48092  7.73704   -10.36715 1.000 25.86964  ?  384 SER   I CA  1 
ATOM   2605  C C   . SER   A  1 384 ? 21.79824  6.27518   -10.63207 1.000 50.26697  ?  384 SER   I C   1 
ATOM   2606  O O   . SER   A  1 384 ? 20.89301  5.43712   -10.76465 1.000 39.03308  ?  384 SER   I O   1 
ATOM   2607  C CB  . SER   A  1 384 ? 21.54928  8.02284   -8.86549  1.000 28.26638  ?  384 SER   I CB  1 
ATOM   2608  O OG  . SER   A  1 384 ? 21.10558  9.34769   -8.60139  1.000 55.47208  ?  384 SER   I OG  1 
ATOM   2609  N N   . GLU   A  1 385 ? 23.08857  5.96629   -10.72208 1.000 34.63382  ?  385 GLU   I N   1 
ATOM   2610  C CA  . GLU   A  1 385 ? 23.45731  4.56210   -10.83541 1.000 43.36214  ?  385 GLU   I CA  1 
ATOM   2611  C C   . GLU   A  1 385 ? 22.90808  3.80306   -9.62652  1.000 42.97933  ?  385 GLU   I C   1 
ATOM   2612  O O   . GLU   A  1 385 ? 22.89739  4.30787   -8.49678  1.000 40.93530  ?  385 GLU   I O   1 
ATOM   2613  C CB  . GLU   A  1 385 ? 24.97366  4.41586   -10.94928 1.000 21.30216  ?  385 GLU   I CB  1 
ATOM   2614  C CG  . GLU   A  1 385 ? 25.58554  5.20820   -12.11047 1.000 35.10181  ?  385 GLU   I CG  1 
ATOM   2615  C CD  . GLU   A  1 385 ? 27.06565  4.89805   -12.32822 1.000 52.01116  ?  385 GLU   I CD  1 
ATOM   2616  O OE1 . GLU   A  1 385 ? 27.71197  4.42311   -11.36377 1.000 50.40022  ?  385 GLU   I OE1 1 
ATOM   2617  O OE2 . GLU   A  1 385 ? 27.57725  5.11715   -13.46026 1.000 37.56188  ?  385 GLU   I OE2 1 
ATOM   2618  N N   . GLY   A  1 386 ? 22.37541  2.61484   -9.88186  1.000 40.55472  ?  386 GLY   I N   1 
ATOM   2619  C CA  . GLY   A  1 386 ? 21.78054  1.79857   -8.84562  1.000 26.71137  ?  386 GLY   I CA  1 
ATOM   2620  C C   . GLY   A  1 386 ? 20.29589  2.01899   -8.62002  1.000 45.42057  ?  386 GLY   I C   1 
ATOM   2621  O O   . GLY   A  1 386 ? 19.62548  1.14186   -8.07196  1.000 40.00535  ?  386 GLY   I O   1 
ATOM   2622  N N   . GLN   A  1 387 ? 19.76831  3.16081   -9.02569  1.000 36.12904  ?  387 GLN   I N   1 
ATOM   2623  C CA  . GLN   A  1 387 ? 18.35686  3.46433   -8.84870  1.000 32.81976  ?  387 GLN   I CA  1 
ATOM   2624  C C   . GLN   A  1 387 ? 17.47041  2.54936   -9.69777  1.000 52.05494  ?  387 GLN   I C   1 
ATOM   2625  O O   . GLN   A  1 387 ? 17.86007  2.09756   -10.78268 1.000 45.19141  ?  387 GLN   I O   1 
ATOM   2626  C CB  . GLN   A  1 387 ? 18.12530  4.92497   -9.21970  1.000 31.67544  ?  387 GLN   I CB  1 
ATOM   2627  C CG  . GLN   A  1 387 ? 16.72468  5.40516   -9.15492  1.000 32.23914  ?  387 GLN   I CG  1 
ATOM   2628  C CD  . GLN   A  1 387 ? 16.66109  6.87323   -9.47668  1.000 40.23960  ?  387 GLN   I CD  1 
ATOM   2629  O OE1 . GLN   A  1 387 ? 17.68715  7.57261   -9.46037  1.000 45.20277  ?  387 GLN   I OE1 1 
ATOM   2630  N NE2 . GLN   A  1 387 ? 15.46445  7.35286   -9.80019  1.000 33.61976  ?  387 GLN   I NE2 1 
ATOM   2631  N N   . HIS   A  1 388 ? 16.26659  2.26482   -9.18719  1.000 30.33765  ?  388 HIS   I N   1 
ATOM   2632  C CA  . HIS   A  1 388 ? 15.25781  1.52978   -9.94329  1.000 41.63147  ?  388 HIS   I CA  1 
ATOM   2633  C C   . HIS   A  1 388 ? 14.26304  2.50576   -10.55630 1.000 55.28112  ?  388 HIS   I C   1 
ATOM   2634  O O   . HIS   A  1 388 ? 13.95186  3.54828   -9.96773  1.000 29.36417  ?  388 HIS   I O   1 
ATOM   2635  C CB  . HIS   A  1 388 ? 14.51047  0.53273   -9.06769  1.000 19.64857  ?  388 HIS   I CB  1 
ATOM   2636  C CG  . HIS   A  1 388 ? 13.52758  -0.31422  -9.81384  1.000 36.98114  ?  388 HIS   I CG  1 
ATOM   2637  N ND1 . HIS   A  1 388 ? 12.21367  0.06397   -10.01684 1.000 37.93960  ?  388 HIS   I ND1 1 
ATOM   2638  C CD2 . HIS   A  1 388 ? 13.66629  -1.52625  -10.40346 1.000 25.91240  ?  388 HIS   I CD2 1 
ATOM   2639  C CE1 . HIS   A  1 388 ? 11.58937  -0.87596  -10.70643 1.000 34.25531  ?  388 HIS   I CE1 1 
ATOM   2640  N NE2 . HIS   A  1 388 ? 12.44667  -1.85398  -10.95062 1.000 30.19638  ?  388 HIS   I NE2 1 
ATOM   2641  N N   . VAL   A  1 389 ? 13.78406  2.17102   -11.75394 1.000 24.92219  ?  389 VAL   I N   1 
ATOM   2642  C CA  . VAL   A  1 389 ? 12.80498  2.98361   -12.46829 1.000 37.32539  ?  389 VAL   I CA  1 
ATOM   2643  C C   . VAL   A  1 389 ? 11.80418  2.05463   -13.13957 1.000 36.26897  ?  389 VAL   I C   1 
ATOM   2644  O O   . VAL   A  1 389 ? 12.10152  0.88997   -13.44170 1.000 50.40247  ?  389 VAL   I O   1 
ATOM   2645  C CB  . VAL   A  1 389 ? 13.44969  3.93270   -13.52012 1.000 42.51224  ?  389 VAL   I CB  1 
ATOM   2646  C CG1 . VAL   A  1 389 ? 14.39202  4.95728   -12.84570 1.000 27.31103  ?  389 VAL   I CG1 1 
ATOM   2647  C CG2 . VAL   A  1 389 ? 14.18532  3.14943   -14.59551 1.000 21.59842  ?  389 VAL   I CG2 1 
ATOM   2648  N N   . ASN   A  1 390 ? 10.60435  2.58672   -13.35794 1.000 25.24689  ?  390 ASN   I N   1 
ATOM   2649  C CA  . ASN   A  1 390 ? 9.55757   1.93171   -14.13141 1.000 28.71025  ?  390 ASN   I CA  1 
ATOM   2650  C C   . ASN   A  1 390 ? 9.46075   2.56595   -15.50736 1.000 54.07314  ?  390 ASN   I C   1 
ATOM   2651  O O   . ASN   A  1 390 ? 9.70300   3.76745   -15.67629 1.000 31.54701  ?  390 ASN   I O   1 
ATOM   2652  C CB  . ASN   A  1 390 ? 8.19502   2.02606   -13.43357 1.000 41.41075  ?  390 ASN   I CB  1 
ATOM   2653  C CG  . ASN   A  1 390 ? 8.14051   1.20672   -12.15431 1.000 34.95869  ?  390 ASN   I CG  1 
ATOM   2654  O OD1 . ASN   A  1 390 ? 8.61001   0.05905   -12.10484 1.000 45.44279  ?  390 ASN   I OD1 1 
ATOM   2655  N ND2 . ASN   A  1 390 ? 7.59750   1.80233   -11.10481 1.000 44.89557  ?  390 ASN   I ND2 1 
ATOM   2656  N N   . ARG   A  1 391 ? 9.12371   1.73346   -16.49033 1.000 32.74772  ?  391 ARG   I N   1 
ATOM   2657  C CA  . ARG   A  1 391 ? 8.84803   2.18642   -17.84573 1.000 43.34240  ?  391 ARG   I CA  1 
ATOM   2658  C C   . ARG   A  1 391 ? 7.97486   3.44184   -17.82599 1.000 31.34973  ?  391 ARG   I C   1 
ATOM   2659  O O   . ARG   A  1 391 ? 6.89936   3.45385   -17.21872 1.000 42.02937  ?  391 ARG   I O   1 
ATOM   2660  C CB  . ARG   A  1 391 ? 8.16887   1.04307   -18.60745 1.000 22.71943  ?  391 ARG   I CB  1 
ATOM   2661  C CG  . ARG   A  1 391 ? 8.07257   1.18688   -20.11801 1.000 32.38951  ?  391 ARG   I CG  1 
ATOM   2662  C CD  . ARG   A  1 391 ? 7.87198   -0.17211  -20.78933 1.000 41.97737  ?  391 ARG   I CD  1 
ATOM   2663  N NE  . ARG   A  1 391 ? 6.59671   -0.80916  -20.47815 1.000 34.33767  ?  391 ARG   I NE  1 
ATOM   2664  C CZ  . ARG   A  1 391 ? 5.51647   -0.70968  -21.24355 1.000 75.90721  ?  391 ARG   I CZ  1 
ATOM   2665  N NH1 . ARG   A  1 391 ? 5.50359   0.04365   -22.32938 1.000 35.30265  ?  391 ARG   I NH1 1 
ATOM   2666  N NH2 . ARG   A  1 391 ? 4.41959   -1.38120  -20.91547 1.000 36.25049  ?  391 ARG   I NH2 1 
ATOM   2667  N N   . GLY   A  1 392 ? 8.48727   4.53507   -18.41510 1.000 24.73708  ?  392 GLY   I N   1 
ATOM   2668  C CA  . GLY   A  1 392 ? 7.78911   5.81019   -18.49311 1.000 21.16491  ?  392 GLY   I CA  1 
ATOM   2669  C C   . GLY   A  1 392 ? 8.23830   6.87029   -17.50081 1.000 29.94591  ?  392 GLY   I C   1 
ATOM   2670  O O   . GLY   A  1 392 ? 7.83661   8.03932   -17.64592 1.000 28.52163  ?  392 GLY   I O   1 
ATOM   2671  N N   . ASP   A  1 393 ? 9.06133   6.50655   -16.50878 1.000 22.19883  ?  393 ASP   I N   1 
ATOM   2672  C CA  . ASP   A  1 393 ? 9.58976   7.47769   -15.54953 1.000 34.88907  ?  393 ASP   I CA  1 
ATOM   2673  C C   . ASP   A  1 393 ? 10.65437  8.36573   -16.20023 1.000 29.44451  ?  393 ASP   I C   1 
ATOM   2674  O O   . ASP   A  1 393 ? 11.24785  8.01587   -17.22686 1.000 48.49939  ?  393 ASP   I O   1 
ATOM   2675  C CB  . ASP   A  1 393 ? 10.19811  6.76588   -14.33328 1.000 25.52873  ?  393 ASP   I CB  1 
ATOM   2676  C CG  . ASP   A  1 393 ? 9.18281   5.90997   -13.55720 1.000 54.41661  ?  393 ASP   I CG  1 
ATOM   2677  O OD1 . ASP   A  1 393 ? 7.96147   5.94169   -13.85330 1.000 51.01867  ?  393 ASP   I OD1 1 
ATOM   2678  O OD2 . ASP   A  1 393 ? 9.62363   5.19184   -12.63402 1.000 39.11942  ?  393 ASP   I OD2 1 
ATOM   2679  N N   . ASP   A  1 394 ? 10.91581  9.51975   -15.57786 1.000 45.50533  ?  394 ASP   I N   1 
ATOM   2680  C CA  . ASP   A  1 394 ? 11.96776  10.40574  -16.07954 1.000 21.22204  ?  394 ASP   I CA  1 
ATOM   2681  C C   . ASP   A  1 394 ? 13.33685  9.73434   -15.97373 1.000 47.90439  ?  394 ASP   I C   1 
ATOM   2682  O O   . ASP   A  1 394 ? 13.67866  9.17041   -14.92923 1.000 30.72930  ?  394 ASP   I O   1 
ATOM   2683  C CB  . ASP   A  1 394 ? 11.98613  11.72699  -15.30286 1.000 40.72025  ?  394 ASP   I CB  1 
ATOM   2684  C CG  . ASP   A  1 394 ? 10.67636  12.49184  -15.39127 1.000 30.22217  ?  394 ASP   I CG  1 
ATOM   2685  O OD1 . ASP   A  1 394 ? 10.02526  12.48483  -16.46941 1.000 74.58122  ?  394 ASP   I OD1 1 
ATOM   2686  O OD2 . ASP   A  1 394 ? 10.31499  13.12834  -14.37786 1.000 69.83132  ?  394 ASP   I OD2 1 
ATOM   2687  N N   . LEU   A  1 395 ? 14.12162  9.77953   -17.05685 1.000 25.08787  ?  395 LEU   I N   1 
ATOM   2688  C CA  . LEU   A  1 395 ? 15.54707  9.47377   -16.94461 1.000 44.02914  ?  395 LEU   I CA  1 
ATOM   2689  C C   . LEU   A  1 395 ? 16.39512  10.72580  -16.92349 1.000 36.96423  ?  395 LEU   I C   1 
ATOM   2690  O O   . LEU   A  1 395 ? 17.49283  10.72345  -16.34460 1.000 34.42931  ?  395 LEU   I O   1 
ATOM   2691  C CB  . LEU   A  1 395 ? 16.03836  8.60099   -18.10330 1.000 21.49887  ?  395 LEU   I CB  1 
ATOM   2692  C CG  . LEU   A  1 395 ? 15.61176  7.14896   -18.20162 1.000 35.97347  ?  395 LEU   I CG  1 
ATOM   2693  C CD1 . LEU   A  1 395 ? 16.27622  6.59037   -19.41942 1.000 20.97051  ?  395 LEU   I CD1 1 
ATOM   2694  C CD2 . LEU   A  1 395 ? 15.99581  6.37820   -16.94960 1.000 31.00074  ?  395 LEU   I CD2 1 
ATOM   2695  N N   . GLY   A  1 396 ? 15.90122  11.78239  -17.55288 1.000 32.63859  ?  396 GLY   I N   1 
ATOM   2696  C CA  . GLY   A  1 396 ? 16.65493  13.01243  -17.67555 1.000 41.03720  ?  396 GLY   I CA  1 
ATOM   2697  C C   . GLY   A  1 396 ? 16.10553  13.79845  -18.84553 1.000 37.20532  ?  396 GLY   I C   1 
ATOM   2698  O O   . GLY   A  1 396 ? 14.95200  13.61007  -19.24522 1.000 40.65641  ?  396 GLY   I O   1 
ATOM   2699  N N   . MET   A  1 397 ? 16.95966  14.65293  -19.40408 1.000 32.74186  ?  397 MET   I N   1 
ATOM   2700  C CA  . MET   A  1 397 ? 16.49019  15.50774  -20.48528 1.000 31.61876  ?  397 MET   I CA  1 
ATOM   2701  C C   . MET   A  1 397 ? 17.66672  16.13552  -21.21626 1.000 47.12912  ?  397 MET   I C   1 
ATOM   2702  O O   . MET   A  1 397 ? 18.80742  16.12591  -20.73927 1.000 36.35796  ?  397 MET   I O   1 
ATOM   2703  C CB  . MET   A  1 397 ? 15.56536  16.59620  -19.95127 1.000 29.44308  ?  397 MET   I CB  1 
ATOM   2704  C CG  . MET   A  1 397 ? 16.30775  17.76960  -19.33760 1.000 33.92393  ?  397 MET   I CG  1 
ATOM   2705  S SD  . MET   A  1 397 ? 15.25439  18.48047  -18.09059 1.000 44.32495  ?  397 MET   I SD  1 
ATOM   2706  C CE  . MET   A  1 397 ? 15.41119  17.26167  -16.79933 1.000 22.57059  ?  397 MET   I CE  1 
ATOM   2707  N N   . PHE   A  1 398 ? 17.35624  16.68274  -22.39272 1.000 29.13669  ?  398 PHE   I N   1 
ATOM   2708  C CA  . PHE   A  1 398 ? 18.26515  17.50630  -23.17343 1.000 22.41904  ?  398 PHE   I CA  1 
ATOM   2709  C C   . PHE   A  1 398 ? 18.17016  18.97973  -22.75960 1.000 32.19842  ?  398 PHE   I C   1 
ATOM   2710  O O   . PHE   A  1 398 ? 17.11583  19.46509  -22.34743 1.000 41.90888  ?  398 PHE   I O   1 
ATOM   2711  C CB  . PHE   A  1 398 ? 17.93444  17.39930  -24.66460 1.000 22.50089  ?  398 PHE   I CB  1 
ATOM   2712  C CG  . PHE   A  1 398 ? 18.24144  16.07179  -25.28137 1.000 36.14704  ?  398 PHE   I CG  1 
ATOM   2713  C CD1 . PHE   A  1 398 ? 19.56457  15.70850  -25.56426 1.000 22.81483  ?  398 PHE   I CD1 1 
ATOM   2714  C CD2 . PHE   A  1 398 ? 17.20615  15.20584  -25.65091 1.000 29.57298  ?  398 PHE   I CD2 1 
ATOM   2715  C CE1 . PHE   A  1 398 ? 19.85657  14.47803  -26.17222 1.000 34.85489  ?  398 PHE   I CE1 1 
ATOM   2716  C CE2 . PHE   A  1 398 ? 17.48146  13.96791  -26.26814 1.000 25.61768  ?  398 PHE   I CE2 1 
ATOM   2717  C CZ  . PHE   A  1 398 ? 18.80506  13.60365  -26.52844 1.000 32.95375  ?  398 PHE   I CZ  1 
ATOM   2718  N N   . HIS   A  1 399 ? 19.27751  19.70377  -22.91155 1.000 38.88891  ?  399 HIS   I N   1 
ATOM   2719  C CA  . HIS   A  1 399 ? 19.26707  21.15712  -22.78690 1.000 47.28262  ?  399 HIS   I CA  1 
ATOM   2720  C C   . HIS   A  1 399 ? 20.12311  21.76045  -23.88714 1.000 25.74188  ?  399 HIS   I C   1 
ATOM   2721  O O   . HIS   A  1 399 ? 21.08290  21.14247  -24.35493 1.000 54.14044  ?  399 HIS   I O   1 
ATOM   2722  C CB  . HIS   A  1 399 ? 19.83920  21.69747  -21.44456 1.000 23.24270  ?  399 HIS   I CB  1 
ATOM   2723  C CG  . HIS   A  1 399 ? 19.20360  21.13048  -20.21186 1.000 26.99649  ?  399 HIS   I CG  1 
ATOM   2724  N ND1 . HIS   A  1 399 ? 18.08258  21.68173  -19.62785 1.000 35.04140  ?  399 HIS   I ND1 1 
ATOM   2725  C CD2 . HIS   A  1 399 ? 19.55705  20.07798  -19.43181 1.000 42.42470  ?  399 HIS   I CD2 1 
ATOM   2726  C CE1 . HIS   A  1 399 ? 17.75860  20.97920  -18.55557 1.000 52.69447  ?  399 HIS   I CE1 1 
ATOM   2727  N NE2 . HIS   A  1 399 ? 18.64232  20.00650  -18.40874 1.000 23.90543  ?  399 HIS   I NE2 1 
ATOM   2728  N N   . PHE   A  1 400 ? 19.79952  22.99849  -24.25659 1.000 43.12398  ?  400 PHE   I N   1 
ATOM   2729  C CA  . PHE   A  1 400 ? 20.78903  23.84558  -24.90443 1.000 24.59307  ?  400 PHE   I CA  1 
ATOM   2730  C C   . PHE   A  1 400 ? 22.02720  23.91074  -24.01511 1.000 33.22362  ?  400 PHE   I C   1 
ATOM   2731  O O   . PHE   A  1 400 ? 21.92823  24.15854  -22.80752 1.000 43.71369  ?  400 PHE   I O   1 
ATOM   2732  C CB  . PHE   A  1 400 ? 20.21664  25.24659  -25.14376 1.000 42.27083  ?  400 PHE   I CB  1 
ATOM   2733  C CG  . PHE   A  1 400 ? 19.32782  25.34327  -26.34920 1.000 22.19782  ?  400 PHE   I CG  1 
ATOM   2734  C CD1 . PHE   A  1 400 ? 18.05468  24.77087  -26.34320 1.000 41.24207  ?  400 PHE   I CD1 1 
ATOM   2735  C CD2 . PHE   A  1 400 ? 19.76205  25.99664  -27.50015 1.000 42.23513  ?  400 PHE   I CD2 1 
ATOM   2736  C CE1 . PHE   A  1 400 ? 17.23865  24.83387  -27.46600 1.000 25.90998  ?  400 PHE   I CE1 1 
ATOM   2737  C CE2 . PHE   A  1 400 ? 18.94131  26.07868  -28.63098 1.000 38.08103  ?  400 PHE   I CE2 1 
ATOM   2738  C CZ  . PHE   A  1 400 ? 17.68451  25.49254  -28.61034 1.000 40.99609  ?  400 PHE   I CZ  1 
ATOM   2739  N N   . GLY   A  1 401 ? 23.18022  23.64222  -24.60115 1.000 28.85156  ?  401 GLY   I N   1 
ATOM   2740  C CA  . GLY   A  1 401 ? 24.42605  23.63150  -23.85885 1.000 24.78008  ?  401 GLY   I CA  1 
ATOM   2741  C C   . GLY   A  1 401 ? 25.40969  22.67939  -24.50378 1.000 35.23927  ?  401 GLY   I C   1 
ATOM   2742  O O   . GLY   A  1 401 ? 25.13514  22.07197  -25.53856 1.000 41.43210  ?  401 GLY   I O   1 
ATOM   2743  N N   . GLY   A  1 402 ? 26.57113  22.55904  -23.85903 1.000 34.16998  ?  402 GLY   I N   1 
ATOM   2744  C CA  . GLY   A  1 402 ? 27.64044  21.69634  -24.35405 1.000 26.77565  ?  402 GLY   I CA  1 
ATOM   2745  C C   . GLY   A  1 402 ? 27.55898  20.25572  -23.85973 1.000 56.01378  ?  402 GLY   I C   1 
ATOM   2746  O O   . GLY   A  1 402 ? 28.26855  19.33295  -24.31549 1.000 37.63187  ?  402 GLY   I O   1 
ATOM   2747  O OXT . GLY   A  1 402 ? 26.74868  19.97224  -22.97062 1.000 46.81520  ?  402 GLY   I OXT 1 
ATOM   2748  N N   . SER   B  2 1   ? 19.12079  13.64700  -30.48669 1.000 25.28650  ?  404 SER   J N   1 
ATOM   2749  C CA  . SER   B  2 1   ? 18.92959  12.28772  -31.01122 1.000 20.40617  ?  404 SER   J CA  1 
ATOM   2750  C C   . SER   B  2 1   ? 19.11991  11.23166  -29.91558 1.000 31.83138  ?  404 SER   J C   1 
ATOM   2751  O O   . SER   B  2 1   ? 19.76454  11.49957  -28.90553 1.000 35.34681  ?  404 SER   J O   1 
ATOM   2752  C CB  . SER   B  2 1   ? 19.89276  12.02989  -32.18870 1.000 26.68137  ?  404 SER   J CB  1 
ATOM   2753  O OG  . SER   B  2 1   ? 19.69636  10.74844  -32.77329 1.000 29.41968  ?  404 SER   J OG  1 
ATOM   2754  N N   . PHE   B  2 2   ? 18.56060  10.03273  -30.09840 1.000 19.10501  ?  405 PHE   J N   1 
ATOM   2755  C CA  . PHE   B  2 2   ? 18.73671  8.97134   -29.11032 1.000 25.37979  ?  405 PHE   J CA  1 
ATOM   2756  C C   . PHE   B  2 2   ? 18.80790  7.61916   -29.81129 1.000 23.05068  ?  405 PHE   J C   1 
ATOM   2757  O O   . PHE   B  2 2   ? 18.26565  7.44183   -30.91143 1.000 32.34880  ?  405 PHE   J O   1 
ATOM   2758  C CB  . PHE   B  2 2   ? 17.60691  8.96378   -28.06495 1.000 26.06060  ?  405 PHE   J CB  1 
ATOM   2759  C CG  . PHE   B  2 2   ? 16.44923  8.08061   -28.43160 1.000 28.53299  ?  405 PHE   J CG  1 
ATOM   2760  C CD1 . PHE   B  2 2   ? 15.45428  8.53189   -29.30580 1.000 34.82628  ?  405 PHE   J CD1 1 
ATOM   2761  C CD2 . PHE   B  2 2   ? 16.36199  6.78618   -27.91371 1.000 31.96833  ?  405 PHE   J CD2 1 
ATOM   2762  C CE1 . PHE   B  2 2   ? 14.38312  7.71194   -29.66016 1.000 28.55498  ?  405 PHE   J CE1 1 
ATOM   2763  C CE2 . PHE   B  2 2   ? 15.29576  5.94867   -28.26046 1.000 24.69233  ?  405 PHE   J CE2 1 
ATOM   2764  C CZ  . PHE   B  2 2   ? 14.29113  6.42541   -29.13814 1.000 30.88027  ?  405 PHE   J CZ  1 
ATOM   2765  N N   . ALA   B  2 3   ? 19.46313  6.65540   -29.14854 1.000 24.83875  ?  406 ALA   J N   1 
ATOM   2766  C CA  . ALA   B  2 3   ? 19.55652  5.29995   -29.66729 1.000 29.09065  ?  406 ALA   J CA  1 
ATOM   2767  C C   . ALA   B  2 3   ? 19.30659  4.28825   -28.56087 1.000 32.23085  ?  406 ALA   J C   1 
ATOM   2768  O O   . ALA   B  2 3   ? 19.81640  4.43032   -27.44055 1.000 31.13946  ?  406 ALA   J O   1 
ATOM   2769  C CB  . ALA   B  2 3   ? 20.91027  5.03160   -30.31396 1.000 12.89067  ?  406 ALA   J CB  1 
ATOM   2770  N N   . LEU   B  2 4   ? 18.51618  3.26523   -28.90040 1.000 34.22931  ?  407 LEU   J N   1 
ATOM   2771  C CA  . LEU   B  2 4   ? 18.23881  2.12180   -28.04231 1.000 33.50701  ?  407 LEU   J CA  1 
ATOM   2772  C C   . LEU   B  2 4   ? 19.03640  0.93067   -28.55494 1.000 18.72535  ?  407 LEU   J C   1 
ATOM   2773  O O   . LEU   B  2 4   ? 19.01540  0.64512   -29.75677 1.000 38.28257  ?  407 LEU   J O   1 
ATOM   2774  C CB  . LEU   B  2 4   ? 16.74119  1.80075   -28.03589 1.000 22.45514  ?  407 LEU   J CB  1 
ATOM   2775  C CG  . LEU   B  2 4   ? 16.35634  0.44874   -27.42939 1.000 34.18385  ?  407 LEU   J CG  1 
ATOM   2776  C CD1 . LEU   B  2 4   ? 16.59903  0.45207   -25.90953 1.000 20.57859  ?  407 LEU   J CD1 1 
ATOM   2777  C CD2 . LEU   B  2 4   ? 14.91860  0.11813   -27.77071 1.000 26.52604  ?  407 LEU   J CD2 1 
ATOM   2778  N N   . GLY   B  2 5   ? 19.74823  0.25081   -27.64865 1.000 37.86731  ?  408 GLY   J N   1 
ATOM   2779  C CA  . GLY   B  2 5   ? 20.56535  -0.90357  -28.00544 1.000 14.57969  ?  408 GLY   J CA  1 
ATOM   2780  C C   . GLY   B  2 5   ? 20.11661  -2.20631  -27.35913 1.000 30.10424  ?  408 GLY   J C   1 
ATOM   2781  O O   . GLY   B  2 5   ? 19.92902  -2.28313  -26.13398 1.000 36.42894  ?  408 GLY   J O   1 
ATOM   2782  N N   . LEU   B  2 6   ? 19.93675  -3.24054  -28.18329 1.000 26.20536  ?  409 LEU   J N   1 
ATOM   2783  C CA  . LEU   B  2 6   ? 19.53145  -4.56852  -27.73419 1.000 45.56086  ?  409 LEU   J CA  1 
ATOM   2784  C C   . LEU   B  2 6   ? 20.60755  -5.58909  -28.07918 1.000 38.95697  ?  409 LEU   J C   1 
ATOM   2785  O O   . LEU   B  2 6   ? 21.17210  -5.55987  -29.18184 1.000 44.02244  ?  409 LEU   J O   1 
ATOM   2786  C CB  . LEU   B  2 6   ? 18.21065  -4.99120  -28.38346 1.000 36.84261  ?  409 LEU   J CB  1 
ATOM   2787  C CG  . LEU   B  2 6   ? 17.08095  -3.97013  -28.23049 1.000 43.71772  ?  409 LEU   J CG  1 
ATOM   2788  C CD1 . LEU   B  2 6   ? 15.82466  -4.44669  -28.94172 1.000 29.80028  ?  409 LEU   J CD1 1 
ATOM   2789  C CD2 . LEU   B  2 6   ? 16.80730  -3.64498  -26.74606 1.000 25.35152  ?  409 LEU   J CD2 1 
ATOM   2790  N N   . ARG   B  2 7   ? 20.87115  -6.49686  -27.13903 1.000 36.98120  ?  410 ARG   J N   1 
ATOM   2791  C CA  . ARG   B  2 7   ? 21.78260  -7.61817  -27.35242 1.000 35.70847  ?  410 ARG   J CA  1 
ATOM   2792  C C   . ARG   B  2 7   ? 21.17306  -8.65451  -28.31268 1.000 41.60730  ?  410 ARG   J C   1 
ATOM   2793  O O   . ARG   B  2 7   ? 19.94893  -8.74606  -28.46961 1.000 52.86993  ?  410 ARG   J O   1 
ATOM   2794  C CB  . ARG   B  2 7   ? 22.12137  -8.26093  -26.00089 1.000 22.55806  ?  410 ARG   J CB  1 
ATOM   2795  C CG  . ARG   B  2 7   ? 22.75846  -7.27853  -25.03252 1.000 24.56626  ?  410 ARG   J CG  1 
ATOM   2796  C CD  . ARG   B  2 7   ? 22.98105  -7.82936  -23.63939 1.000 35.81168  ?  410 ARG   J CD  1 
ATOM   2797  N NE  . ARG   B  2 7   ? 21.73045  -8.06619  -22.93362 1.000 54.90514  ?  410 ARG   J NE  1 
ATOM   2798  C CZ  . ARG   B  2 7   ? 21.14938  -9.25323  -22.81088 1.000 45.76536  ?  410 ARG   J CZ  1 
ATOM   2799  N NH1 . ARG   B  2 7   ? 21.72088  -10.35538 -23.26744 1.000 49.12934  ?  410 ARG   J NH1 1 
ATOM   2800  N NH2 . ARG   B  2 7   ? 19.95793  -9.33541  -22.22599 1.000 54.99307  ?  410 ARG   J NH2 1 
ATOM   2801  N N   . LYS   B  2 8   ? 22.04480  -9.44209  -28.97185 1.000 40.07370  ?  411 LYS   J N   1 
ATOM   2802  C CA  . LYS   B  2 8   ? 21.55536  -10.52238 -29.83797 1.000 58.13437  ?  411 LYS   J CA  1 
ATOM   2803  C C   . LYS   B  2 8   ? 20.77513  -11.55093 -29.03607 1.000 50.35939  ?  411 LYS   J C   1 
ATOM   2804  O O   . LYS   B  2 8   ? 19.69212  -11.98255 -29.45197 1.000 47.27101  ?  411 LYS   J O   1 
ATOM   2805  C CB  . LYS   B  2 8   ? 22.70418  -11.21237 -30.57971 1.000 30.25438  ?  411 LYS   J CB  1 
ATOM   2806  N N   . ASP   B  2 9   ? 21.30098  -11.93624 -27.86718 1.000 37.08837  ?  412 ASP   J N   1 
ATOM   2807  C CA  . ASP   B  2 9   ? 20.63356  -12.86003 -26.95285 1.000 88.51683  ?  412 ASP   J CA  1 
ATOM   2808  C C   . ASP   B  2 9   ? 19.33799  -12.31081 -26.36256 1.000 43.83371  ?  412 ASP   J C   1 
ATOM   2809  O O   . ASP   B  2 9   ? 18.66455  -13.01859 -25.60132 1.000 74.41089  ?  412 ASP   J O   1 
ATOM   2810  C CB  . ASP   B  2 9   ? 21.59231  -13.23490 -25.82411 1.000 62.07237  ?  412 ASP   J CB  1 
ATOM   2811  C CG  . ASP   B  2 9   ? 22.69453  -14.16562 -26.28940 1.000 71.50565  ?  412 ASP   J CG  1 
ATOM   2812  O OD1 . ASP   B  2 9   ? 22.60767  -14.67557 -27.43392 1.000 74.09535  ?  412 ASP   J OD1 1 
ATOM   2813  O OD2 . ASP   B  2 9   ? 23.64469  -14.38889 -25.51216 1.000 96.75670  ?  412 ASP   J OD2 1 
ATOM   2814  N N   . CYS   B  2 10  ? 18.98832  -11.06962 -26.65308 1.000 78.31189  ?  413 CYS   J N   1 
ATOM   2815  C CA  . CYS   B  2 10  ? 17.74158  -10.51366 -26.16514 1.000 55.23457  ?  413 CYS   J CA  1 
ATOM   2816  C C   . CYS   B  2 10  ? 16.61961  -10.97807 -27.08519 1.000 65.78244  ?  413 CYS   J C   1 
ATOM   2817  O O   . CYS   B  2 10  ? 16.68023  -10.77700 -28.30739 1.000 63.78649  ?  413 CYS   J O   1 
ATOM   2818  C CB  . CYS   B  2 10  ? 17.83832  -8.99119  -26.09973 1.000 46.72202  ?  413 CYS   J CB  1 
ATOM   2819  S SG  . CYS   B  2 10  ? 16.27399  -8.11012  -25.90331 1.000 58.59794  ?  413 CYS   J SG  1 
ATOM   2820  N N   . ARG   B  2 11  ? 15.61206  -11.62192 -26.49506 1.000 63.74125  ?  414 ARG   J N   1 
ATOM   2821  C CA  . ARG   B  2 11  ? 14.47194  -12.17094 -27.21593 1.000 86.10649  ?  414 ARG   J CA  1 
ATOM   2822  C C   . ARG   B  2 11  ? 13.45915  -11.08869 -27.65749 1.000 97.43654  ?  414 ARG   J C   1 
ATOM   2823  O O   . ARG   B  2 11  ? 12.40825  -11.41972 -28.21904 1.000 69.98057  ?  414 ARG   J O   1 
ATOM   2824  C CB  . ARG   B  2 11  ? 13.80401  -13.24474 -26.34402 1.000 57.75665  ?  414 ARG   J CB  1 
ATOM   2825  N N   . ALA   B  2 12  ? 13.75135  -9.80680  -27.43975 1.000 77.76578  ?  415 ALA   J N   1 
ATOM   2826  C CA  . ALA   B  2 12  ? 12.88939  -8.72889  -27.90540 1.000 66.66611  ?  415 ALA   J CA  1 
ATOM   2827  C C   . ALA   B  2 12  ? 13.29087  -8.31091  -29.31167 1.000 60.54492  ?  415 ALA   J C   1 
ATOM   2828  O O   . ALA   B  2 12  ? 14.47296  -8.35684  -29.67776 1.000 88.19508  ?  415 ALA   J O   1 
ATOM   2829  C CB  . ALA   B  2 12  ? 12.96262  -7.52388  -26.96824 1.000 46.34445  ?  415 ALA   J CB  1 
ATOM   2830  N N   . GLU   B  2 13  ? 12.30092  -7.89111  -30.09244 1.000 39.23480  ?  416 GLU   J N   1 
ATOM   2831  C CA  . GLU   B  2 13  ? 12.49875  -7.55596  -31.49488 1.000 52.91825  ?  416 GLU   J CA  1 
ATOM   2832  C C   . GLU   B  2 13  ? 11.90611  -6.17686  -31.76282 1.000 55.21833  ?  416 GLU   J C   1 
ATOM   2833  O O   . GLU   B  2 13  ? 10.75802  -5.90081  -31.39671 1.000 60.38637  ?  416 GLU   J O   1 
ATOM   2834  C CB  . GLU   B  2 13  ? 11.87518  -8.61698  -32.42121 1.000 42.19663  ?  416 GLU   J CB  1 
ATOM   2835  N N   . ILE   B  2 14  ? 12.70870  -5.30900  -32.38094 1.000 49.66684  ?  417 ILE   J N   1 
ATOM   2836  C CA  . ILE   B  2 14  ? 12.24408  -3.98592  -32.76282 1.000 57.39269  ?  417 ILE   J CA  1 
ATOM   2837  C C   . ILE   B  2 14  ? 10.99232  -4.09988  -33.63166 1.000 47.53455  ?  417 ILE   J C   1 
ATOM   2838  O O   . ILE   B  2 14  ? 10.88904  -4.95178  -34.51903 1.000 55.87308  ?  417 ILE   J O   1 
ATOM   2839  C CB  . ILE   B  2 14  ? 13.37956  -3.23146  -33.47980 1.000 37.75506  ?  417 ILE   J CB  1 
ATOM   2840  C CG1 . ILE   B  2 14  ? 14.57106  -3.05962  -32.53812 1.000 41.12573  ?  417 ILE   J CG1 1 
ATOM   2841  C CG2 . ILE   B  2 14  ? 12.90074  -1.86955  -34.02190 1.000 44.77216  ?  417 ILE   J CG2 1 
ATOM   2842  C CD1 . ILE   B  2 14  ? 15.78829  -2.42472  -33.20229 1.000 51.19245  ?  417 ILE   J CD1 1 
ATOM   2843  N N   . VAL   B  2 15  ? 10.03044  -3.22816  -33.36450 1.000 53.89730  ?  418 VAL   J N   1 
ATOM   2844  C CA  . VAL   B  2 15  ? 8.77667   -3.23338  -34.09746 1.000 35.59691  ?  418 VAL   J CA  1 
ATOM   2845  C C   . VAL   B  2 15  ? 9.01914   -2.75467  -35.52414 1.000 39.39209  ?  418 VAL   J C   1 
ATOM   2846  O O   . VAL   B  2 15  ? 9.56126   -1.66174  -35.74217 1.000 59.49568  ?  418 VAL   J O   1 
ATOM   2847  C CB  . VAL   B  2 15  ? 7.75095   -2.36517  -33.35190 1.000 58.96062  ?  418 VAL   J CB  1 
ATOM   2848  C CG1 . VAL   B  2 15  ? 6.48013   -2.15823  -34.17367 1.000 27.27345  ?  418 VAL   J CG1 1 
ATOM   2849  C CG2 . VAL   B  2 15  ? 7.45674   -2.99140  -31.98326 1.000 25.54162  ?  418 VAL   J CG2 1 
ATOM   2850  N N   . GLU   B  2 16  ? 8.57858   -3.56255  -36.50379 1.000 55.21920  ?  419 GLU   J N   1 
ATOM   2851  C CA  . GLU   B  2 16  ? 9.01599   -3.39789  -37.89305 1.000 44.69044  ?  419 GLU   J CA  1 
ATOM   2852  C C   . GLU   B  2 16  ? 8.67668   -2.02894  -38.46870 1.000 55.13138  ?  419 GLU   J C   1 
ATOM   2853  O O   . GLU   B  2 16  ? 9.42982   -1.53143  -39.31458 1.000 55.25125  ?  419 GLU   J O   1 
ATOM   2854  C CB  . GLU   B  2 16  ? 8.42202   -4.48425  -38.80814 1.000 45.38344  ?  419 GLU   J CB  1 
ATOM   2855  N N   . LYS   B  2 17  ? 7.56180   -1.40292  -38.05839 1.000 44.65470  ?  420 LYS   J N   1 
ATOM   2856  C CA  . LYS   B  2 17  ? 7.21029   -0.14305  -38.72126 1.000 46.91129  ?  420 LYS   J CA  1 
ATOM   2857  C C   . LYS   B  2 17  ? 8.27493   0.92599   -38.50778 1.000 53.43008  ?  420 LYS   J C   1 
ATOM   2858  O O   . LYS   B  2 17  ? 8.38346   1.85998   -39.31586 1.000 51.83110  ?  420 LYS   J O   1 
ATOM   2859  C CB  . LYS   B  2 17  ? 5.82835   0.38753   -38.27623 1.000 29.38515  ?  420 LYS   J CB  1 
ATOM   2860  C CG  . LYS   B  2 17  ? 5.65280   0.89509   -36.81860 1.000 34.38527  ?  420 LYS   J CG  1 
ATOM   2861  C CD  . LYS   B  2 17  ? 4.71857   2.12405   -36.83007 1.000 55.52192  ?  420 LYS   J CD  1 
ATOM   2862  C CE  . LYS   B  2 17  ? 3.96629   2.35213   -35.52356 1.000 65.31820  ?  420 LYS   J CE  1 
ATOM   2863  N NZ  . LYS   B  2 17  ? 3.16713   1.15121   -35.16687 1.000 88.21330  ?  420 LYS   J NZ  1 
ATOM   2864  N N   . PHE   B  2 18  ? 9.08007   0.79846   -37.44960 1.000 41.83687  ?  421 PHE   J N   1 
ATOM   2865  C CA  . PHE   B  2 18  ? 10.11540  1.78228   -37.16906 1.000 65.51477  ?  421 PHE   J CA  1 
ATOM   2866  C C   . PHE   B  2 18  ? 11.37940  1.57284   -37.98872 1.000 52.72211  ?  421 PHE   J C   1 
ATOM   2867  O O   . PHE   B  2 18  ? 12.25526  2.44170   -37.97290 1.000 47.43578  ?  421 PHE   J O   1 
ATOM   2868  C CB  . PHE   B  2 18  ? 10.43886  1.77469   -35.68323 1.000 30.66291  ?  421 PHE   J CB  1 
ATOM   2869  C CG  . PHE   B  2 18  ? 9.25587   2.09928   -34.83430 1.000 41.89296  ?  421 PHE   J CG  1 
ATOM   2870  C CD1 . PHE   B  2 18  ? 8.57488   3.30220   -35.01806 1.000 41.33225  ?  421 PHE   J CD1 1 
ATOM   2871  C CD2 . PHE   B  2 18  ? 8.79113   1.20450   -33.87871 1.000 58.71829  ?  421 PHE   J CD2 1 
ATOM   2872  C CE1 . PHE   B  2 18  ? 7.46865   3.60930   -34.25332 1.000 33.64683  ?  421 PHE   J CE1 1 
ATOM   2873  C CE2 . PHE   B  2 18  ? 7.67694   1.50520   -33.10611 1.000 49.10404  ?  421 PHE   J CE2 1 
ATOM   2874  C CZ  . PHE   B  2 18  ? 7.01427   2.70491   -33.29853 1.000 54.77596  ?  421 PHE   J CZ  1 
ATOM   2875  N N   . THR   B  2 19  ? 11.49521  0.47402   -38.73431 1.000 41.43536  ?  422 THR   J N   1 
ATOM   2876  C CA  . THR   B  2 19  ? 12.61663  0.40108   -39.65880 1.000 31.65721  ?  422 THR   J CA  1 
ATOM   2877  C C   . THR   B  2 19  ? 12.44166  1.32143   -40.86619 1.000 39.70496  ?  422 THR   J C   1 
ATOM   2878  O O   . THR   B  2 19  ? 13.40122  1.49102   -41.62694 1.000 37.84038  ?  422 THR   J O   1 
ATOM   2879  C CB  . THR   B  2 19  ? 12.82838  -1.03784  -40.12459 1.000 43.28181  ?  422 THR   J CB  1 
ATOM   2880  O OG1 . THR   B  2 19  ? 11.81476  -1.38366  -41.06592 1.000 39.48540  ?  422 THR   J OG1 1 
ATOM   2881  C CG2 . THR   B  2 19  ? 12.74766  -2.00313  -38.95213 1.000 45.20323  ?  422 THR   J CG2 1 
ATOM   2882  N N   . GLU   B  2 20  ? 11.25815  1.93289   -41.05800 1.000 51.97885  ?  423 GLU   J N   1 
ATOM   2883  C CA  . GLU   B  2 20  ? 11.09214  2.92444   -42.12025 1.000 50.26882  ?  423 GLU   J CA  1 
ATOM   2884  C C   . GLU   B  2 20  ? 11.43516  4.30750   -41.57489 1.000 40.71849  ?  423 GLU   J C   1 
ATOM   2885  O O   . GLU   B  2 20  ? 10.74482  4.79857   -40.66601 1.000 56.49112  ?  423 GLU   J O   1 
ATOM   2886  C CB  . GLU   B  2 20  ? 9.67450   2.91298   -42.68873 1.000 36.54292  ?  423 GLU   J CB  1 
ATOM   2887  N N   . PRO   B  2 21  ? 12.49965  4.93682   -42.05542 1.000 36.15723  ?  424 PRO   J N   1 
ATOM   2888  C CA  . PRO   B  2 21  ? 12.82635  6.29515   -41.60798 1.000 49.59724  ?  424 PRO   J CA  1 
ATOM   2889  C C   . PRO   B  2 21  ? 11.62599  7.21339   -41.76126 1.000 35.21181  ?  424 PRO   J C   1 
ATOM   2890  O O   . PRO   B  2 21  ? 10.83698  7.07822   -42.69644 1.000 43.90931  ?  424 PRO   J O   1 
ATOM   2891  C CB  . PRO   B  2 21  ? 13.96442  6.71630   -42.54570 1.000 18.10336  ?  424 PRO   J CB  1 
ATOM   2892  C CG  . PRO   B  2 21  ? 14.58134  5.43390   -42.99881 1.000 33.22200  ?  424 PRO   J CG  1 
ATOM   2893  C CD  . PRO   B  2 21  ? 13.49173  4.37914   -42.98264 1.000 31.91297  ?  424 PRO   J CD  1 
ATOM   2894  N N   . GLY   B  2 22  ? 11.49404  8.15484   -40.82640 1.000 38.80381  ?  425 GLY   J N   1 
ATOM   2895  C CA  . GLY   B  2 22  ? 10.43334  9.13506   -40.86081 1.000 21.48095  ?  425 GLY   J CA  1 
ATOM   2896  C C   . GLY   B  2 22  ? 9.17927   8.75525   -40.09441 1.000 30.12060  ?  425 GLY   J C   1 
ATOM   2897  O O   . GLY   B  2 22  ? 8.32185   9.61734   -39.88321 1.000 35.99906  ?  425 GLY   J O   1 
ATOM   2898  N N   . THR   B  2 23  ? 9.04600   7.50054   -39.67113 1.000 28.95349  ?  426 THR   J N   1 
ATOM   2899  C CA  . THR   B  2 23  ? 7.88204   7.07974   -38.89942 1.000 26.62257  ?  426 THR   J CA  1 
ATOM   2900  C C   . THR   B  2 23  ? 7.81847   7.80511   -37.55258 1.000 26.59572  ?  426 THR   J C   1 
ATOM   2901  O O   . THR   B  2 23  ? 8.82717   7.96509   -36.86103 1.000 55.86643  ?  426 THR   J O   1 
ATOM   2902  C CB  . THR   B  2 23  ? 7.93335   5.56029   -38.68944 1.000 35.29445  ?  426 THR   J CB  1 
ATOM   2903  O OG1 . THR   B  2 23  ? 7.94142   4.89426   -39.96043 1.000 43.59342  ?  426 THR   J OG1 1 
ATOM   2904  C CG2 . THR   B  2 23  ? 6.76237   5.05964   -37.84230 1.000 25.73400  ?  426 THR   J CG2 1 
ATOM   2905  N N   . VAL   B  2 24  ? 6.61738   8.23682   -37.17570 1.000 57.51435  ?  427 VAL   J N   1 
ATOM   2906  C CA  . VAL   B  2 24  ? 6.43981   8.95113   -35.91915 1.000 38.67879  ?  427 VAL   J CA  1 
ATOM   2907  C C   . VAL   B  2 24  ? 6.60897   7.99452   -34.74398 1.000 33.13426  ?  427 VAL   J C   1 
ATOM   2908  O O   . VAL   B  2 24  ? 6.02317   6.90210   -34.71271 1.000 57.98885  ?  427 VAL   J O   1 
ATOM   2909  C CB  . VAL   B  2 24  ? 5.07010   9.64452   -35.89917 1.000 31.54708  ?  427 VAL   J CB  1 
ATOM   2910  C CG1 . VAL   B  2 24  ? 4.71102   10.09168  -34.49549 1.000 24.28649  ?  427 VAL   J CG1 1 
ATOM   2911  C CG2 . VAL   B  2 24  ? 5.10401   10.83064  -36.83565 1.000 31.49355  ?  427 VAL   J CG2 1 
ATOM   2912  N N   . ILE   B  2 25  ? 7.41838   8.40539   -33.76942 1.000 53.52051  ?  428 ILE   J N   1 
ATOM   2913  C CA  . ILE   B  2 25  ? 7.66413   7.64492   -32.54518 1.000 22.41721  ?  428 ILE   J CA  1 
ATOM   2914  C C   . ILE   B  2 25  ? 7.04884   8.44161   -31.39796 1.000 43.82922  ?  428 ILE   J C   1 
ATOM   2915  O O   . ILE   B  2 25  ? 7.58447   9.47669   -30.97817 1.000 35.12972  ?  428 ILE   J O   1 
ATOM   2916  C CB  . ILE   B  2 25  ? 9.16155   7.38346   -32.30316 1.000 40.82360  ?  428 ILE   J CB  1 
ATOM   2917  C CG1 . ILE   B  2 25  ? 9.77976   6.52575   -33.41857 1.000 31.69224  ?  428 ILE   J CG1 1 
ATOM   2918  C CG2 . ILE   B  2 25  ? 9.35386   6.71560   -30.95976 1.000 19.65610  ?  428 ILE   J CG2 1 
ATOM   2919  C CD1 . ILE   B  2 25  ? 11.22261  6.08088   -33.14841 1.000 26.32110  ?  428 ILE   J CD1 1 
ATOM   2920  N N   . ARG   B  2 26  ? 5.91085   7.97572   -30.89606 1.000 35.23662  ?  429 ARG   J N   1 
ATOM   2921  C CA  . ARG   B  2 26  ? 5.27726   8.60503   -29.74593 1.000 34.04898  ?  429 ARG   J CA  1 
ATOM   2922  C C   . ARG   B  2 26  ? 5.96033   8.09453   -28.49220 1.000 34.57917  ?  429 ARG   J C   1 
ATOM   2923  O O   . ARG   B  2 26  ? 6.01949   6.87970   -28.26899 1.000 33.61881  ?  429 ARG   J O   1 
ATOM   2924  C CB  . ARG   B  2 26  ? 3.78034   8.30141   -29.71332 1.000 42.06384  ?  429 ARG   J CB  1 
ATOM   2925  C CG  . ARG   B  2 26  ? 3.04879   8.89122   -30.88683 1.000 35.84189  ?  429 ARG   J CG  1 
ATOM   2926  C CD  . ARG   B  2 26  ? 1.61027   8.44714   -30.95267 1.000 49.46439  ?  429 ARG   J CD  1 
ATOM   2927  N NE  . ARG   B  2 26  ? 0.78824   9.52895   -31.48204 1.000 35.24696  ?  429 ARG   J NE  1 
ATOM   2928  C CZ  . ARG   B  2 26  ? 0.71001   9.84125   -32.77022 1.000 167.75079 ?  429 ARG   J CZ  1 
ATOM   2929  N NH1 . ARG   B  2 26  ? 1.32966   9.12289   -33.70130 1.000 30.88466  ?  429 ARG   J NH1 1 
ATOM   2930  N NH2 . ARG   B  2 26  ? -0.00080  10.90421  -33.13613 1.000 37.71127  ?  429 ARG   J NH2 1 
ATOM   2931  N N   . ILE   B  2 27  ? 6.47995   9.01522   -27.67744 1.000 17.09622  ?  430 ILE   J N   1 
ATOM   2932  C CA  . ILE   B  2 27  ? 7.17821   8.59911   -26.47079 1.000 34.48971  ?  430 ILE   J CA  1 
ATOM   2933  C C   . ILE   B  2 27  ? 6.26637   7.69080   -25.63976 1.000 22.12111  ?  430 ILE   J C   1 
ATOM   2934  O O   . ILE   B  2 27  ? 5.03937   7.84396   -25.63087 1.000 48.92308  ?  430 ILE   J O   1 
ATOM   2935  C CB  . ILE   B  2 27  ? 7.66535   9.83457   -25.68954 1.000 27.99376  ?  430 ILE   J CB  1 
ATOM   2936  C CG1 . ILE   B  2 27  ? 8.73835   9.42971   -24.66035 1.000 22.47812  ?  430 ILE   J CG1 1 
ATOM   2937  C CG2 . ILE   B  2 27  ? 6.47082   10.60737  -25.07944 1.000 26.10831  ?  430 ILE   J CG2 1 
ATOM   2938  C CD1 . ILE   B  2 27  ? 9.40908   10.62900  -23.99478 1.000 19.66160  ?  430 ILE   J CD1 1 
ATOM   2939  N N   . ASN   B  2 28  ? 6.88368   6.70999   -24.97611 1.000 47.13332  ?  431 ASN   J N   1 
ATOM   2940  C CA  . ASN   B  2 28  ? 6.23333   5.66338   -24.18898 1.000 26.58539  ?  431 ASN   J CA  1 
ATOM   2941  C C   . ASN   B  2 28  ? 5.53322   4.61442   -25.04670 1.000 38.15345  ?  431 ASN   J C   1 
ATOM   2942  O O   . ASN   B  2 28  ? 5.06879   3.61219   -24.49671 1.000 28.69842  ?  431 ASN   J O   1 
ATOM   2943  C CB  . ASN   B  2 28  ? 5.20681   6.22996   -23.19221 1.000 22.25514  ?  431 ASN   J CB  1 
ATOM   2944  C CG  . ASN   B  2 28  ? 5.82831   7.15623   -22.16513 1.000 34.16425  ?  431 ASN   J CG  1 
ATOM   2945  O OD1 . ASN   B  2 28  ? 7.02501   7.08956   -21.88150 1.000 39.11491  ?  431 ASN   J OD1 1 
ATOM   2946  N ND2 . ASN   B  2 28  ? 5.00927   8.03787   -21.60431 1.000 26.31211  ?  431 ASN   J ND2 1 
ATOM   2947  N N   . GLU   B  2 29  ? 5.41344   4.80831   -26.36230 1.000 22.41357  ?  432 GLU   J N   1 
ATOM   2948  C CA  . GLU   B  2 29  ? 4.78661   3.74859   -27.14610 1.000 31.05913  ?  432 GLU   J CA  1 
ATOM   2949  C C   . GLU   B  2 29  ? 5.78176   2.59262   -27.35139 1.000 26.83645  ?  432 GLU   J C   1 
ATOM   2950  O O   . GLU   B  2 29  ? 6.98054   2.71262   -27.07602 1.000 42.29902  ?  432 GLU   J O   1 
ATOM   2951  C CB  . GLU   B  2 29  ? 4.24448   4.30940   -28.46907 1.000 15.23557  ?  432 GLU   J CB  1 
ATOM   2952  C CG  . GLU   B  2 29  ? 5.13334   4.15779   -29.69090 1.000 28.51692  ?  432 GLU   J CG  1 
ATOM   2953  C CD  . GLU   B  2 29  ? 4.42266   4.51843   -31.00457 1.000 52.89565  ?  432 GLU   J CD  1 
ATOM   2954  O OE1 . GLU   B  2 29  ? 4.45555   5.70366   -31.40606 1.000 37.90977  ?  432 GLU   J OE1 1 
ATOM   2955  O OE2 . GLU   B  2 29  ? 3.84382   3.60882   -31.65106 1.000 44.16255  ?  432 GLU   J OE2 1 
ATOM   2956  N N   . VAL   B  2 30  ? 5.26798   1.44269   -27.78049 1.000 47.26815  ?  433 VAL   J N   1 
ATOM   2957  C CA  . VAL   B  2 30  ? 6.07828   0.22477   -27.86229 1.000 22.58512  ?  433 VAL   J CA  1 
ATOM   2958  C C   . VAL   B  2 30  ? 6.97001   0.28550   -29.09849 1.000 42.68732  ?  433 VAL   J C   1 
ATOM   2959  O O   . VAL   B  2 30  ? 6.46885   0.38096   -30.22561 1.000 33.52381  ?  433 VAL   J O   1 
ATOM   2960  C CB  . VAL   B  2 30  ? 5.18352   -1.02616  -27.90071 1.000 43.53699  ?  433 VAL   J CB  1 
ATOM   2961  C CG1 . VAL   B  2 30  ? 6.01952   -2.30796  -28.00485 1.000 33.36458  ?  433 VAL   J CG1 1 
ATOM   2962  C CG2 . VAL   B  2 30  ? 4.24552   -1.07657  -26.68716 1.000 28.14022  ?  433 VAL   J CG2 1 
ATOM   2963  N N   . VAL   B  2 31  ? 8.29240   0.20936   -28.89655 1.000 36.07741  ?  434 VAL   J N   1 
ATOM   2964  C CA  . VAL   B  2 31  ? 9.22719   0.12535   -30.01782 1.000 47.15889  ?  434 VAL   J CA  1 
ATOM   2965  C C   . VAL   B  2 31  ? 9.89293   -1.24479  -30.12969 1.000 34.75566  ?  434 VAL   J C   1 
ATOM   2966  O O   . VAL   B  2 31  ? 10.43328  -1.56710  -31.20146 1.000 33.93733  ?  434 VAL   J O   1 
ATOM   2967  C CB  . VAL   B  2 31  ? 10.30110  1.24120   -29.98135 1.000 37.47898  ?  434 VAL   J CB  1 
ATOM   2968  C CG1 . VAL   B  2 31  ? 9.67270   2.61296   -30.18812 1.000 21.24337  ?  434 VAL   J CG1 1 
ATOM   2969  C CG2 . VAL   B  2 31  ? 11.12059  1.21182   -28.66717 1.000 23.82230  ?  434 VAL   J CG2 1 
ATOM   2970  N N   . ALA   B  2 32  ? 9.86447   -2.06197  -29.08252 1.000 28.07958  ?  435 ALA   J N   1 
ATOM   2971  C CA  . ALA   B  2 32  ? 10.33696  -3.43687  -29.18095 1.000 31.35722  ?  435 ALA   J CA  1 
ATOM   2972  C C   . ALA   B  2 32  ? 9.55401   -4.28312  -28.18630 1.000 41.29961  ?  435 ALA   J C   1 
ATOM   2973  O O   . ALA   B  2 32  ? 9.13017   -3.79269  -27.13109 1.000 33.36947  ?  435 ALA   J O   1 
ATOM   2974  C CB  . ALA   B  2 32  ? 11.84395  -3.55772  -28.91318 1.000 25.05485  ?  435 ALA   J CB  1 
ATOM   2975  N N   . ALA   B  2 33  ? 9.37492   -5.56044  -28.52813 1.000 32.37687  ?  436 ALA   J N   1 
ATOM   2976  C CA  . ALA   B  2 33  ? 8.57727   -6.47845  -27.72461 1.000 41.37527  ?  436 ALA   J CA  1 
ATOM   2977  C C   . ALA   B  2 33  ? 9.11961   -7.89152  -27.86924 1.000 60.99746  ?  436 ALA   J C   1 
ATOM   2978  O O   . ALA   B  2 33  ? 9.69837   -8.24607  -28.90114 1.000 38.39370  ?  436 ALA   J O   1 
ATOM   2979  C CB  . ALA   B  2 33  ? 7.10673   -6.46243  -28.13703 1.000 25.47801  ?  436 ALA   J CB  1 
ATOM   2980  N N   . LEU   B  2 34  ? 8.90437   -8.69747  -26.83075 1.000 40.72454  ?  437 LEU   J N   1 
ATOM   2981  C CA  . LEU   B  2 34  ? 9.32470   -10.09911 -26.80993 1.000 70.44898  ?  437 LEU   J CA  1 
ATOM   2982  C C   . LEU   B  2 34  ? 8.59446   -10.96865 -27.83933 1.000 38.31916  ?  437 LEU   J C   1 
ATOM   2983  O O   . LEU   B  2 34  ? 7.36984   -10.97013 -27.91090 1.000 45.05691  ?  437 LEU   J O   1 
ATOM   2984  C CB  . LEU   B  2 34  ? 9.11901   -10.68269 -25.40650 1.000 37.14071  ?  437 LEU   J CB  1 
ATOM   2985  C CG  . LEU   B  2 34  ? 10.12636  -10.26638 -24.32366 1.000 62.26371  ?  437 LEU   J CG  1 
ATOM   2986  C CD1 . LEU   B  2 34  ? 9.76063   -10.83128 -22.92511 1.000 43.41843  ?  437 LEU   J CD1 1 
ATOM   2987  C CD2 . LEU   B  2 34  ? 11.56181  -10.63664 -24.73889 1.000 65.01799  ?  437 LEU   J CD2 1 
ATOM   2988  N N   . LEU   C  1 57  ? -7.48115  -0.08030  16.95037  1.000 32.67342  ?  57  LEU   G N   1 
ATOM   2989  C CA  . LEU   C  1 57  ? -7.22563  1.30587   16.57342  1.000 29.57076  ?  57  LEU   G CA  1 
ATOM   2990  C C   . LEU   C  1 57  ? -7.33106  2.20496   17.78497  1.000 45.71287  ?  57  LEU   G C   1 
ATOM   2991  O O   . LEU   C  1 57  ? -8.25540  2.05451   18.58200  1.000 47.70673  ?  57  LEU   G O   1 
ATOM   2992  C CB  . LEU   C  1 57  ? -8.23351  1.80147   15.53380  1.000 26.21597  ?  57  LEU   G CB  1 
ATOM   2993  C CG  . LEU   C  1 57  ? -8.32169  1.23637   14.11759  1.000 42.47967  ?  57  LEU   G CG  1 
ATOM   2994  C CD1 . LEU   C  1 57  ? -9.51229  1.87515   13.40354  1.000 34.86571  ?  57  LEU   G CD1 1 
ATOM   2995  C CD2 . LEU   C  1 57  ? -7.03461  1.43763   13.32500  1.000 40.94451  ?  57  LEU   G CD2 1 
ATOM   2996  N N   . MET   C  1 58  ? -6.42436  3.17343   17.90030  1.000 49.50113  ?  58  MET   G N   1 
ATOM   2997  C CA  . MET   C  1 58  ? -6.50583  4.11108   19.01249  1.000 48.39984  ?  58  MET   G CA  1 
ATOM   2998  C C   . MET   C  1 58  ? -7.75984  4.96825   18.89571  1.000 39.10822  ?  58  MET   G C   1 
ATOM   2999  O O   . MET   C  1 58  ? -8.21632  5.29126   17.79708  1.000 59.77382  ?  58  MET   G O   1 
ATOM   3000  C CB  . MET   C  1 58  ? -5.26380  4.99233   19.06337  1.000 41.34234  ?  58  MET   G CB  1 
ATOM   3001  C CG  . MET   C  1 58  ? -4.90731  5.68383   17.76409  1.000 56.64407  ?  58  MET   G CG  1 
ATOM   3002  S SD  . MET   C  1 58  ? -3.44169  6.71534   17.97958  1.000 62.50911  ?  58  MET   G SD  1 
ATOM   3003  C CE  . MET   C  1 58  ? -2.14454  5.46945   17.90228  1.000 39.13588  ?  58  MET   G CE  1 
ATOM   3004  N N   . GLN   C  1 59  ? -8.31990  5.33611   20.04691  1.000 50.62394  ?  59  GLN   G N   1 
ATOM   3005  C CA  . GLN   C  1 59  ? -9.61649  6.01382   20.08553  1.000 39.46219  ?  59  GLN   G CA  1 
ATOM   3006  C C   . GLN   C  1 59  ? -9.72710  7.21231   19.14596  1.000 49.19173  ?  59  GLN   G C   1 
ATOM   3007  O O   . GLN   C  1 59  ? -10.75694 7.32758   18.46302  1.000 43.24224  ?  59  GLN   G O   1 
ATOM   3008  C CB  . GLN   C  1 59  ? -9.93824  6.45858   21.51986  1.000 33.21213  ?  59  GLN   G CB  1 
ATOM   3009  C CG  . GLN   C  1 59  ? -11.39486 6.80405   21.70295  1.000 62.76400  ?  59  GLN   G CG  1 
ATOM   3010  C CD  . GLN   C  1 59  ? -12.27174 5.59429   21.42879  1.000 85.35591  ?  59  GLN   G CD  1 
ATOM   3011  O OE1 . GLN   C  1 59  ? -11.87305 4.45576   21.69280  1.000 96.93955  ?  59  GLN   G OE1 1 
ATOM   3012  N NE2 . GLN   C  1 59  ? -13.46183 5.82682   20.87595  1.000 69.98258  ?  59  GLN   G NE2 1 
ATOM   3013  N N   . PRO   C  1 60  ? -8.74743  8.12764   19.05789  1.000 50.91909  ?  60  PRO   G N   1 
ATOM   3014  C CA  . PRO   C  1 60  ? -8.90571  9.25190   18.11203  1.000 32.63890  ?  60  PRO   G CA  1 
ATOM   3015  C C   . PRO   C  1 60  ? -9.13294  8.80097   16.67782  1.000 56.72702  ?  60  PRO   G C   1 
ATOM   3016  O O   . PRO   C  1 60  ? -9.93126  9.42844   15.96453  1.000 35.83041  ?  60  PRO   G O   1 
ATOM   3017  C CB  . PRO   C  1 60  ? -7.59461  10.03389  18.27636  1.000 33.40248  ?  60  PRO   G CB  1 
ATOM   3018  C CG  . PRO   C  1 60  ? -7.10017  9.67464   19.64106  1.000 40.39105  ?  60  PRO   G CG  1 
ATOM   3019  C CD  . PRO   C  1 60  ? -7.48657  8.22977   19.81518  1.000 28.67034  ?  60  PRO   G CD  1 
ATOM   3020  N N   . ILE   C  1 61  ? -8.46849  7.72153   16.24155  1.000 24.99075  ?  61  ILE   G N   1 
ATOM   3021  C CA  . ILE   C  1 61  ? -8.72537  7.18090   14.90571  1.000 49.32435  ?  61  ILE   G CA  1 
ATOM   3022  C C   . ILE   C  1 61  ? -10.11143 6.55707   14.82468  1.000 35.64354  ?  61  ILE   G C   1 
ATOM   3023  O O   . ILE   C  1 61  ? -10.77223 6.62848   13.78132  1.000 39.97752  ?  61  ILE   G O   1 
ATOM   3024  C CB  . ILE   C  1 61  ? -7.63585  6.17150   14.50370  1.000 35.21498  ?  61  ILE   G CB  1 
ATOM   3025  C CG1 . ILE   C  1 61  ? -6.26987  6.85422   14.52349  1.000 25.76684  ?  61  ILE   G CG1 1 
ATOM   3026  C CG2 . ILE   C  1 61  ? -7.90816  5.58810   13.10569  1.000 23.90406  ?  61  ILE   G CG2 1 
ATOM   3027  C CD1 . ILE   C  1 61  ? -5.16151  5.95461   14.09405  1.000 32.35562  ?  61  ILE   G CD1 1 
ATOM   3028  N N   . GLN   C  1 62  ? -10.57950 5.92108   15.88260  1.000 69.64865  ?  62  GLN   G N   1 
ATOM   3029  C CA  . GLN   C  1 62  ? -11.92651 5.39241   15.80889  1.000 23.42620  ?  62  GLN   G CA  1 
ATOM   3030  C C   . GLN   C  1 62  ? -12.95969 6.51599   15.70050  1.000 67.16770  ?  62  GLN   G C   1 
ATOM   3031  O O   . GLN   C  1 62  ? -13.92504 6.38174   14.95198  1.000 17.57747  ?  62  GLN   G O   1 
ATOM   3032  C CB  . GLN   C  1 62  ? -12.21506 4.50458   17.02395  1.000 22.78654  ?  62  GLN   G CB  1 
ATOM   3033  C CG  . GLN   C  1 62  ? -11.46680 3.15315   17.10892  1.000 84.93596  ?  62  GLN   G CG  1 
ATOM   3034  C CD  . GLN   C  1 62  ? -11.79419 2.48685   18.43879  1.000 116.54780 ?  62  GLN   G CD  1 
ATOM   3035  O OE1 . GLN   C  1 62  ? -12.25067 3.14183   19.38419  1.000 67.44115  ?  62  GLN   G OE1 1 
ATOM   3036  N NE2 . GLN   C  1 62  ? -11.56585 1.18993   18.51980  1.000 106.47336 ?  62  GLN   G NE2 1 
ATOM   3037  N N   . GLU   C  1 63  ? -12.81980 7.59770   16.49804  1.000 29.12778  ?  63  GLU   G N   1 
ATOM   3038  C CA  . GLU   C  1 63  ? -13.73940 8.72464   16.35963  1.000 44.96454  ?  63  GLU   G CA  1 
ATOM   3039  C C   . GLU   C  1 63  ? -13.64061 9.34613   14.97258  1.000 47.18395  ?  63  GLU   G C   1 
ATOM   3040  O O   . GLU   C  1 63  ? -14.65326 9.77294   14.40317  1.000 40.50439  ?  63  GLU   G O   1 
ATOM   3041  C CB  . GLU   C  1 63  ? -13.46159 9.76070   17.43640  1.000 29.08413  ?  63  GLU   G CB  1 
ATOM   3042  C CG  . GLU   C  1 63  ? -14.21913 9.50800   18.72831  1.000 66.65902  ?  63  GLU   G CG  1 
ATOM   3043  C CD  . GLU   C  1 63  ? -13.37069 9.72246   19.96069  1.000 53.45132  ?  63  GLU   G CD  1 
ATOM   3044  O OE1 . GLU   C  1 63  ? -12.26219 10.29119  19.83568  1.000 99.91080  ?  63  GLU   G OE1 1 
ATOM   3045  O OE2 . GLU   C  1 63  ? -13.81223 9.32075   21.06101  1.000 127.50433 -1 63  GLU   G OE2 1 
ATOM   3046  N N   . PHE   C  1 64  ? -12.42246 9.39311   14.41522  1.000 34.41121  ?  64  PHE   G N   1 
ATOM   3047  C CA  . PHE   C  1 64  ? -12.21382 9.85087   13.04398  1.000 27.85985  ?  64  PHE   G CA  1 
ATOM   3048  C C   . PHE   C  1 64  ? -13.01643 9.00825   12.06052  1.000 41.89658  ?  64  PHE   G C   1 
ATOM   3049  O O   . PHE   C  1 64  ? -13.79692 9.53932   11.25967  1.000 36.45569  ?  64  PHE   G O   1 
ATOM   3050  C CB  . PHE   C  1 64  ? -10.71591 9.80271   12.72646  1.000 30.95385  ?  64  PHE   G CB  1 
ATOM   3051  C CG  . PHE   C  1 64  ? -10.36426 10.11127  11.29422  1.000 36.12659  ?  64  PHE   G CG  1 
ATOM   3052  C CD1 . PHE   C  1 64  ? -10.46110 11.39997  10.80008  1.000 44.07166  ?  64  PHE   G CD1 1 
ATOM   3053  C CD2 . PHE   C  1 64  ? -9.88645  9.11191   10.45271  1.000 25.16131  ?  64  PHE   G CD2 1 
ATOM   3054  C CE1 . PHE   C  1 64  ? -10.11199 11.67931  9.47955   1.000 30.06358  ?  64  PHE   G CE1 1 
ATOM   3055  C CE2 . PHE   C  1 64  ? -9.52287  9.38310   9.13643   1.000 23.41187  ?  64  PHE   G CE2 1 
ATOM   3056  C CZ  . PHE   C  1 64  ? -9.63465  10.66526  8.64807   1.000 32.14934  ?  64  PHE   G CZ  1 
ATOM   3057  N N   . LYS   C  1 65  ? -12.83932 7.68019   12.12039  1.000 32.02055  ?  65  LYS   G N   1 
ATOM   3058  C CA  . LYS   C  1 65  ? -13.60936 6.76288   11.27479  1.000 26.95719  ?  65  LYS   G CA  1 
ATOM   3059  C C   . LYS   C  1 65  ? -15.11276 6.90326   11.51184  1.000 47.14352  ?  65  LYS   G C   1 
ATOM   3060  O O   . LYS   C  1 65  ? -15.90927 6.88281   10.56420  1.000 38.69921  ?  65  LYS   G O   1 
ATOM   3061  C CB  . LYS   C  1 65  ? -13.16000 5.32241   11.52757  1.000 34.21439  ?  65  LYS   G CB  1 
ATOM   3062  C CG  . LYS   C  1 65  ? -13.83458 4.26819   10.66309  1.000 35.24943  ?  65  LYS   G CG  1 
ATOM   3063  C CD  . LYS   C  1 65  ? -12.91415 3.07071   10.50820  1.000 45.78364  ?  65  LYS   G CD  1 
ATOM   3064  C CE  . LYS   C  1 65  ? -13.44591 1.84860   11.20735  1.000 53.53683  ?  65  LYS   G CE  1 
ATOM   3065  N NZ  . LYS   C  1 65  ? -13.55452 0.74366   10.22409  1.000 64.60160  ?  65  LYS   G NZ  1 
ATOM   3066  N N   . ALA   C  1 66  ? -15.52291 7.03786   12.77499  1.000 37.54241  ?  66  ALA   G N   1 
ATOM   3067  C CA  . ALA   C  1 66  ? -16.94551 7.18431   13.06257  1.000 40.77640  ?  66  ALA   G CA  1 
ATOM   3068  C C   . ALA   C  1 66  ? -17.49773 8.46711   12.44763  1.000 51.09074  ?  66  ALA   G C   1 
ATOM   3069  O O   . ALA   C  1 66  ? -18.66127 8.51988   12.01714  1.000 35.51444  ?  66  ALA   G O   1 
ATOM   3070  C CB  . ALA   C  1 66  ? -17.17345 7.15965   14.57161  1.000 18.06971  ?  66  ALA   G CB  1 
ATOM   3071  N N   . PHE   C  1 67  ? -16.67069 9.51121   12.38610  1.000 47.64680  ?  67  PHE   G N   1 
ATOM   3072  C CA  . PHE   C  1 67  ? -17.12718 10.75829  11.79425  1.000 26.09609  ?  67  PHE   G CA  1 
ATOM   3073  C C   . PHE   C  1 67  ? -17.32961 10.59723  10.29174  1.000 42.08129  ?  67  PHE   G C   1 
ATOM   3074  O O   . PHE   C  1 67  ? -18.36446 11.00475  9.74836   1.000 38.35205  ?  67  PHE   G O   1 
ATOM   3075  C CB  . PHE   C  1 67  ? -16.14223 11.89191  12.10025  1.000 27.31253  ?  67  PHE   G CB  1 
ATOM   3076  C CG  . PHE   C  1 67  ? -16.44008 13.13055  11.33623  1.000 28.28739  ?  67  PHE   G CG  1 
ATOM   3077  C CD1 . PHE   C  1 67  ? -17.48194 13.95088  11.73956  1.000 14.67242  ?  67  PHE   G CD1 1 
ATOM   3078  C CD2 . PHE   C  1 67  ? -15.73685 13.43882  10.16206  1.000 22.24775  ?  67  PHE   G CD2 1 
ATOM   3079  C CE1 . PHE   C  1 67  ? -17.81439 15.09071  11.01388  1.000 21.81069  ?  67  PHE   G CE1 1 
ATOM   3080  C CE2 . PHE   C  1 67  ? -16.06187 14.56494  9.41356   1.000 32.13567  ?  67  PHE   G CE2 1 
ATOM   3081  C CZ  . PHE   C  1 67  ? -17.09795 15.40121  9.83883   1.000 19.19059  ?  67  PHE   G CZ  1 
ATOM   3082  N N   . ILE   C  1 68  ? -16.34558 10.00335  9.60773   1.000 36.82377  ?  68  ILE   G N   1 
ATOM   3083  C CA  . ILE   C  1 68  ? -16.45371 9.74333   8.17149   1.000 39.00604  ?  68  ILE   G CA  1 
ATOM   3084  C C   . ILE   C  1 68  ? -17.75849 9.02689   7.85544   1.000 45.09330  ?  68  ILE   G C   1 
ATOM   3085  O O   . ILE   C  1 68  ? -18.44670 9.34079   6.87598   1.000 42.72530  ?  68  ILE   G O   1 
ATOM   3086  C CB  . ILE   C  1 68  ? -15.23716 8.92308   7.69793   1.000 28.92330  ?  68  ILE   G CB  1 
ATOM   3087  C CG1 . ILE   C  1 68  ? -13.94911 9.74963   7.83435   1.000 36.02199  ?  68  ILE   G CG1 1 
ATOM   3088  C CG2 . ILE   C  1 68  ? -15.43314 8.42832   6.27819   1.000 34.31419  ?  68  ILE   G CG2 1 
ATOM   3089  C CD1 . ILE   C  1 68  ? -12.69857 8.98339   7.53701   1.000 29.00035  ?  68  ILE   G CD1 1 
ATOM   3090  N N   . GLU   C  1 69  ? -18.12069 8.05826   8.69206   1.000 60.61389  ?  69  GLU   G N   1 
ATOM   3091  C CA  . GLU   C  1 69  ? -19.30944 7.24556   8.49692   1.000 35.17686  ?  69  GLU   G CA  1 
ATOM   3092  C C   . GLU   C  1 69  ? -20.58353 7.94246   8.95581   1.000 44.52742  ?  69  GLU   G C   1 
ATOM   3093  O O   . GLU   C  1 69  ? -21.67089 7.53513   8.54360   1.000 45.03477  ?  69  GLU   G O   1 
ATOM   3094  C CB  . GLU   C  1 69  ? -19.13308 5.92170   9.24264   1.000 41.51692  ?  69  GLU   G CB  1 
ATOM   3095  C CG  . GLU   C  1 69  ? -18.18005 4.95657   8.53803   1.000 27.52425  ?  69  GLU   G CG  1 
ATOM   3096  C CD  . GLU   C  1 69  ? -17.62853 3.85949   9.45117   1.000 68.73478  ?  69  GLU   G CD  1 
ATOM   3097  O OE1 . GLU   C  1 69  ? -17.91482 3.87956   10.67976  1.000 41.18275  ?  69  GLU   G OE1 1 
ATOM   3098  O OE2 . GLU   C  1 69  ? -16.89598 2.98204   8.92758   1.000 47.98906  -1 69  GLU   G OE2 1 
ATOM   3099  N N   . SER   C  1 70  ? -20.47326 8.98886   9.77630   1.000 47.33534  ?  70  SER   G N   1 
ATOM   3100  C CA  . SER   C  1 70  ? -21.64194 9.66019   10.33143  1.000 19.11701  ?  70  SER   G CA  1 
ATOM   3101  C C   . SER   C  1 70  ? -22.38060 10.54416  9.33123   1.000 47.87918  ?  70  SER   G C   1 
ATOM   3102  O O   . SER   C  1 70  ? -23.51541 10.93942  9.61580   1.000 32.61206  ?  70  SER   G O   1 
ATOM   3103  C CB  . SER   C  1 70  ? -21.23633 10.52809  11.52731  1.000 31.71599  ?  70  SER   G CB  1 
ATOM   3104  O OG  . SER   C  1 70  ? -20.46113 11.64331  11.10131  1.000 53.05340  ?  70  SER   G OG  1 
ATOM   3105  N N   . ASP   C  1 71  ? -21.77178 10.89218  8.19726   1.000 35.00397  ?  71  ASP   G N   1 
ATOM   3106  C CA  . ASP   C  1 71  ? -22.36656 11.83493  7.24634   1.000 30.28635  ?  71  ASP   G CA  1 
ATOM   3107  C C   . ASP   C  1 71  ? -22.24171 11.22340  5.85799   1.000 36.55530  ?  71  ASP   G C   1 
ATOM   3108  O O   . ASP   C  1 71  ? -21.10837 11.02436  5.36481   1.000 36.45848  ?  71  ASP   G O   1 
ATOM   3109  C CB  . ASP   C  1 71  ? -21.68490 13.21254  7.31868   1.000 39.45186  ?  71  ASP   G CB  1 
ATOM   3110  C CG  . ASP   C  1 71  ? -22.24980 14.24415  6.30707   1.000 78.71174  ?  71  ASP   G CG  1 
ATOM   3111  O OD1 . ASP   C  1 71  ? -22.76979 13.87776  5.21947   1.000 42.63586  ?  71  ASP   G OD1 1 
ATOM   3112  O OD2 . ASP   C  1 71  ? -22.14545 15.45944  6.59448   1.000 56.54082  -1 71  ASP   G OD2 1 
ATOM   3113  N N   . PRO   C  1 72  ? -23.35214 10.94126  5.18653   1.000 45.61308  ?  72  PRO   G N   1 
ATOM   3114  C CA  . PRO   C  1 72  ? -23.26545 10.26342  3.88115   1.000 43.86180  ?  72  PRO   G CA  1 
ATOM   3115  C C   . PRO   C  1 72  ? -22.46945 11.03511  2.83458   1.000 34.71502  ?  72  PRO   G C   1 
ATOM   3116  O O   . PRO   C  1 72  ? -21.83976 10.41150  1.97290   1.000 40.45410  ?  72  PRO   G O   1 
ATOM   3117  C CB  . PRO   C  1 72  ? -24.73777 10.10214  3.47786   1.000 30.08002  ?  72  PRO   G CB  1 
ATOM   3118  C CG  . PRO   C  1 72  ? -25.48640 11.12984  4.30392   1.000 35.92472  ?  72  PRO   G CG  1 
ATOM   3119  C CD  . PRO   C  1 72  ? -24.73112 11.26770  5.58400   1.000 21.88000  ?  72  PRO   G CD  1 
ATOM   3120  N N   . VAL   C  1 73  ? -22.46783 12.37020  2.87877   1.000 40.41048  ?  73  VAL   G N   1 
ATOM   3121  C CA  . VAL   C  1 73  ? -21.68385 13.14060  1.91414   1.000 51.39590  ?  73  VAL   G CA  1 
ATOM   3122  C C   . VAL   C  1 73  ? -20.19317 12.98388  2.18474   1.000 58.99106  ?  73  VAL   G C   1 
ATOM   3123  O O   . VAL   C  1 73  ? -19.39934 12.76528  1.25857   1.000 30.01036  ?  73  VAL   G O   1 
ATOM   3124  C CB  . VAL   C  1 73  ? -22.09140 14.61994  1.94881   1.000 48.13974  ?  73  VAL   G CB  1 
ATOM   3125  C CG1 . VAL   C  1 73  ? -21.32830 15.37694  0.89792   1.000 25.19133  ?  73  VAL   G CG1 1 
ATOM   3126  C CG2 . VAL   C  1 73  ? -23.57107 14.75865  1.72782   1.000 23.02976  ?  73  VAL   G CG2 1 
ATOM   3127  N N   . VAL   C  1 74  ? -19.79261 13.13301  3.45515   1.000 41.75606  ?  74  VAL   G N   1 
ATOM   3128  C CA  . VAL   C  1 74  ? -18.40115 12.92170  3.84920   1.000 32.35342  ?  74  VAL   G CA  1 
ATOM   3129  C C   . VAL   C  1 74  ? -17.96630 11.51015  3.48270   1.000 43.18576  ?  74  VAL   G C   1 
ATOM   3130  O O   . VAL   C  1 74  ? -16.91448 11.30045  2.86202   1.000 47.81561  ?  74  VAL   G O   1 
ATOM   3131  C CB  . VAL   C  1 74  ? -18.23012 13.18699  5.35887   1.000 34.47997  ?  74  VAL   G CB  1 
ATOM   3132  C CG1 . VAL   C  1 74  ? -16.80844 12.86342  5.83637   1.000 17.40809  ?  74  VAL   G CG1 1 
ATOM   3133  C CG2 . VAL   C  1 74  ? -18.56755 14.60484  5.67461   1.000 24.24470  ?  74  VAL   G CG2 1 
ATOM   3134  N N   . HIS   C  1 75  ? -18.78204 10.52232  3.86245   1.000 45.48285  ?  75  HIS   G N   1 
ATOM   3135  C CA  . HIS   C  1 75  ? -18.49742 9.12740   3.54330   1.000 38.18333  ?  75  HIS   G CA  1 
ATOM   3136  C C   . HIS   C  1 75  ? -18.25602 8.93828   2.04678   1.000 27.02399  ?  75  HIS   G C   1 
ATOM   3137  O O   . HIS   C  1 75  ? -17.28100 8.29738   1.63183   1.000 33.93868  ?  75  HIS   G O   1 
ATOM   3138  C CB  . HIS   C  1 75  ? -19.66340 8.26561   4.01950   1.000 29.75615  ?  75  HIS   G CB  1 
ATOM   3139  C CG  . HIS   C  1 75  ? -19.35641 6.80577   4.07227   1.000 62.58382  ?  75  HIS   G CG  1 
ATOM   3140  N ND1 . HIS   C  1 75  ? -20.01167 5.94412   4.92116   1.000 72.03175  ?  75  HIS   G ND1 1 
ATOM   3141  C CD2 . HIS   C  1 75  ? -18.46325 6.05554   3.38666   1.000 64.03123  ?  75  HIS   G CD2 1 
ATOM   3142  C CE1 . HIS   C  1 75  ? -19.53101 4.72564   4.75949   1.000 59.52424  ?  75  HIS   G CE1 1 
ATOM   3143  N NE2 . HIS   C  1 75  ? -18.59517 4.76469   3.82952   1.000 46.20406  ?  75  HIS   G NE2 1 
ATOM   3144  N N   . GLN   C  1 76  ? -19.13624 9.50407   1.21772   1.000 45.85899  ?  76  GLN   G N   1 
ATOM   3145  C CA  . GLN   C  1 76  ? -18.96997 9.37292   -0.22363  1.000 24.53408  ?  76  GLN   G CA  1 
ATOM   3146  C C   . GLN   C  1 76  ? -17.64827 9.98454   -0.67692  1.000 47.72818  ?  76  GLN   G C   1 
ATOM   3147  O O   . GLN   C  1 76  ? -16.95080 9.41289   -1.52389  1.000 36.99517  ?  76  GLN   G O   1 
ATOM   3148  C CB  . GLN   C  1 76  ? -20.15521 10.02045  -0.94546  1.000 49.95500  ?  76  GLN   G CB  1 
ATOM   3149  C CG  . GLN   C  1 76  ? -20.24815 9.64583   -2.41348  1.000 25.93305  ?  76  GLN   G CG  1 
ATOM   3150  C CD  . GLN   C  1 76  ? -20.24173 8.14944   -2.63345  1.000 84.20208  ?  76  GLN   G CD  1 
ATOM   3151  O OE1 . GLN   C  1 76  ? -21.07726 7.42674   -2.08252  1.000 43.84856  ?  76  GLN   G OE1 1 
ATOM   3152  N NE2 . GLN   C  1 76  ? -19.29586 7.67267   -3.43782  1.000 35.92386  ?  76  GLN   G NE2 1 
ATOM   3153  N N   . GLU   C  1 77  ? -17.27850 11.13898  -0.10550  1.000 41.44556  ?  77  GLU   G N   1 
ATOM   3154  C CA  . GLU   C  1 77  ? -15.98752 11.74070  -0.42084  1.000 32.43938  ?  77  GLU   G CA  1 
ATOM   3155  C C   . GLU   C  1 77  ? -14.84000 10.79084  -0.08383  1.000 59.80019  ?  77  GLU   G C   1 
ATOM   3156  O O   . GLU   C  1 77  ? -13.88135 10.66379  -0.85994  1.000 26.40582  ?  77  GLU   G O   1 
ATOM   3157  C CB  . GLU   C  1 77  ? -15.83970 13.06849  0.31652   1.000 31.98030  ?  77  GLU   G CB  1 
ATOM   3158  C CG  . GLU   C  1 77  ? -16.56067 14.20801  -0.38782  1.000 27.07598  ?  77  GLU   G CG  1 
ATOM   3159  C CD  . GLU   C  1 77  ? -16.81372 15.42936  0.49805   1.000 59.46501  ?  77  GLU   G CD  1 
ATOM   3160  O OE1 . GLU   C  1 77  ? -16.45960 15.38342  1.70284   1.000 41.12396  ?  77  GLU   G OE1 1 
ATOM   3161  O OE2 . GLU   C  1 77  ? -17.36850 16.43685  -0.02466  1.000 34.88199  -1 77  GLU   G OE2 1 
ATOM   3162  N N   . PHE   C  1 78  ? -14.93931 10.07671  1.04537   1.000 26.02260  ?  78  PHE   G N   1 
ATOM   3163  C CA  . PHE   C  1 78  ? -13.90485 9.12097   1.43585   1.000 47.08942  ?  78  PHE   G CA  1 
ATOM   3164  C C   . PHE   C  1 78  ? -14.00095 7.80714   0.67868   1.000 46.35666  ?  78  PHE   G C   1 
ATOM   3165  O O   . PHE   C  1 78  ? -13.21645 6.88940   0.94258   1.000 54.01825  ?  78  PHE   G O   1 
ATOM   3166  C CB  . PHE   C  1 78  ? -13.94182 8.85217   2.94823   1.000 27.66740  ?  78  PHE   G CB  1 
ATOM   3167  C CG  . PHE   C  1 78  ? -13.13795 9.82633   3.73088   1.000 46.12634  ?  78  PHE   G CG  1 
ATOM   3168  C CD1 . PHE   C  1 78  ? -11.76980 9.63002   3.89802   1.000 32.46436  ?  78  PHE   G CD1 1 
ATOM   3169  C CD2 . PHE   C  1 78  ? -13.73174 10.97974  4.25102   1.000 20.91547  ?  78  PHE   G CD2 1 
ATOM   3170  C CE1 . PHE   C  1 78  ? -10.99887 10.55158  4.61069   1.000 30.36469  ?  78  PHE   G CE1 1 
ATOM   3171  C CE2 . PHE   C  1 78  ? -12.97483 11.91527  4.95952   1.000 40.69924  ?  78  PHE   G CE2 1 
ATOM   3172  C CZ  . PHE   C  1 78  ? -11.60286 11.70409  5.14647   1.000 28.10611  ?  78  PHE   G CZ  1 
ATOM   3173  N N   . ILE   C  1 79  ? -14.92727 7.68745   -0.25977  1.000 45.39117  ?  79  ILE   G N   1 
ATOM   3174  C CA  . ILE   C  1 79  ? -14.89740 6.61056   -1.22463  1.000 39.04104  ?  79  ILE   G CA  1 
ATOM   3175  C C   . ILE   C  1 79  ? -14.35016 7.09958   -2.55438  1.000 55.77654  ?  79  ILE   G C   1 
ATOM   3176  O O   . ILE   C  1 79  ? -13.37117 6.55982   -3.07334  1.000 32.11070  ?  79  ILE   G O   1 
ATOM   3177  C CB  . ILE   C  1 79  ? -16.30178 5.98663   -1.38927  1.000 47.80587  ?  79  ILE   G CB  1 
ATOM   3178  C CG1 . ILE   C  1 79  ? -16.66028 5.18795   -0.14954  1.000 34.25286  ?  79  ILE   G CG1 1 
ATOM   3179  C CG2 . ILE   C  1 79  ? -16.34604 5.12170   -2.62618  1.000 35.05590  ?  79  ILE   G CG2 1 
ATOM   3180  C CD1 . ILE   C  1 79  ? -18.10322 4.90327   -0.05459  1.000 31.50165  ?  79  ILE   G CD1 1 
ATOM   3181  N N   . ASP   C  1 80  ? -14.95291 8.16403   -3.09915  1.000 25.17991  ?  80  ASP   G N   1 
ATOM   3182  C CA  . ASP   C  1 80  ? -14.56387 8.63792   -4.42080  1.000 41.28005  ?  80  ASP   G CA  1 
ATOM   3183  C C   . ASP   C  1 80  ? -13.08898 9.00775   -4.48565  1.000 32.45711  ?  80  ASP   G C   1 
ATOM   3184  O O   . ASP   C  1 80  ? -12.45440 8.81769   -5.53120  1.000 41.61044  ?  80  ASP   G O   1 
ATOM   3185  C CB  . ASP   C  1 80  ? -15.43545 9.82438   -4.81489  1.000 35.08088  ?  80  ASP   G CB  1 
ATOM   3186  C CG  . ASP   C  1 80  ? -16.92856 9.47168   -4.85316  1.000 53.37187  ?  80  ASP   G CG  1 
ATOM   3187  O OD1 . ASP   C  1 80  ? -17.27187 8.27056   -4.85359  1.000 51.55773  ?  80  ASP   G OD1 1 
ATOM   3188  O OD2 . ASP   C  1 80  ? -17.76124 10.41507  -4.87599  1.000 59.24927  -1 80  ASP   G OD2 1 
ATOM   3189  N N   . MET   C  1 81  ? -12.52170 9.52515   -3.38284  1.000 36.79835  ?  81  MET   G N   1 
ATOM   3190  C CA  . MET   C  1 81  ? -11.12742 9.96554   -3.39547  1.000 30.50377  ?  81  MET   G CA  1 
ATOM   3191  C C   . MET   C  1 81  ? -10.15078 8.80500   -3.63396  1.000 53.27809  ?  81  MET   G C   1 
ATOM   3192  O O   . MET   C  1 81  ? -9.00280  9.06000   -4.03733  1.000 40.63978  ?  81  MET   G O   1 
ATOM   3193  C CB  . MET   C  1 81  ? -10.76224 10.69776  -2.08575  1.000 30.50877  ?  81  MET   G CB  1 
ATOM   3194  C CG  . MET   C  1 81  ? -10.68873 9.82581   -0.83204  1.000 36.97113  ?  81  MET   G CG  1 
ATOM   3195  S SD  . MET   C  1 81  ? -10.16728 10.65369  0.71512   1.000 36.85550  ?  81  MET   G SD  1 
ATOM   3196  C CE  . MET   C  1 81  ? -11.32976 12.02245  0.84649   1.000 33.47355  ?  81  MET   G CE  1 
ATOM   3197  N N   . PHE   C  1 82  ? -10.58099 7.54245   -3.44324  1.000 36.26696  ?  82  PHE   G N   1 
ATOM   3198  C CA  . PHE   C  1 82  ? -9.72276  6.38362   -3.64635  1.000 61.66714  ?  82  PHE   G CA  1 
ATOM   3199  C C   . PHE   C  1 82  ? -9.86934  5.76023   -5.02464  1.000 34.52837  ?  82  PHE   G C   1 
ATOM   3200  O O   . PHE   C  1 82  ? -9.22837  4.73628   -5.29154  1.000 97.90992  ?  82  PHE   G O   1 
ATOM   3201  C CB  . PHE   C  1 82  ? -10.02836 5.33894   -2.58976  1.000 37.15977  ?  82  PHE   G CB  1 
ATOM   3202  C CG  . PHE   C  1 82  ? -9.48410  5.67132   -1.26282  1.000 80.31450  ?  82  PHE   G CG  1 
ATOM   3203  C CD1 . PHE   C  1 82  ? -8.15973  5.39972   -0.96823  1.000 34.23997  ?  82  PHE   G CD1 1 
ATOM   3204  C CD2 . PHE   C  1 82  ? -10.27918 6.27994   -0.31423  1.000 36.85216  ?  82  PHE   G CD2 1 
ATOM   3205  C CE1 . PHE   C  1 82  ? -7.64112  5.71716   0.26318   1.000 53.00281  ?  82  PHE   G CE1 1 
ATOM   3206  C CE2 . PHE   C  1 82  ? -9.77101  6.59935   0.91461   1.000 54.26963  ?  82  PHE   G CE2 1 
ATOM   3207  C CZ  . PHE   C  1 82  ? -8.44286  6.32170   1.20449   1.000 29.97392  ?  82  PHE   G CZ  1 
ATOM   3208  N N   . GLU   C  1 83  ? -10.69381 6.34932   -5.89708  1.000 65.14966  ?  83  GLU   G N   1 
ATOM   3209  C CA  . GLU   C  1 83  ? -11.07452 5.70687   -7.15080  1.000 69.91421  ?  83  GLU   G CA  1 
ATOM   3210  C C   . GLU   C  1 83  ? -9.86372  5.24866   -7.93724  1.000 78.24288  ?  83  GLU   G C   1 
ATOM   3211  O O   . GLU   C  1 83  ? -8.99041  6.04755   -8.26696  1.000 54.50717  ?  83  GLU   G O   1 
ATOM   3212  C CB  . GLU   C  1 83  ? -11.93385 6.64969   -7.98707  1.000 45.24805  ?  83  GLU   G CB  1 
ATOM   3213  C CG  . GLU   C  1 83  ? -13.33162 6.11586   -7.36622  1.000 111.57288 ?  83  GLU   G CG  1 
ATOM   3214  C CD  . GLU   C  1 83  ? -14.60373 6.77834   -7.81334  1.000 157.52772 ?  83  GLU   G CD  1 
ATOM   3215  O OE1 . GLU   C  1 83  ? -14.59191 7.63999   -8.75324  1.000 85.04716  ?  83  GLU   G OE1 1 
ATOM   3216  O OE2 . GLU   C  1 83  ? -15.64189 6.41587   -7.19935  1.000 103.07304 ?  83  GLU   G OE2 1 
ATOM   3217  N N   . GLY   C  1 84  ? -9.81502  3.94740   -8.22108  1.000 94.24611  ?  84  GLY   G N   1 
ATOM   3218  C CA  . GLY   C  1 84  ? -8.74179  3.37603   -9.00913  1.000 58.60325  ?  84  GLY   G CA  1 
ATOM   3219  C C   . GLY   C  1 84  ? -7.38917  3.28234   -8.34520  1.000 91.68907  ?  84  GLY   G C   1 
ATOM   3220  O O   . GLY   C  1 84  ? -6.41876  2.89754   -9.00046  1.000 76.80632  ?  84  GLY   G O   1 
ATOM   3221  N N   . ILE   C  1 85  ? -7.28887  3.62042   -7.06597  1.000 98.76048  ?  85  ILE   G N   1 
ATOM   3222  C CA  . ILE   C  1 85  ? -6.02242  3.50732   -6.35277  1.000 78.37030  ?  85  ILE   G CA  1 
ATOM   3223  C C   . ILE   C  1 85  ? -5.73871  2.03937   -6.08783  1.000 88.57955  ?  85  ILE   G C   1 
ATOM   3224  O O   . ILE   C  1 85  ? -6.53153  1.33243   -5.44720  1.000 82.72621  ?  85  ILE   G O   1 
ATOM   3225  C CB  . ILE   C  1 85  ? -6.04918  4.32545   -5.05426  1.000 71.78629  ?  85  ILE   G CB  1 
ATOM   3226  C CG1 . ILE   C  1 85  ? -6.20646  5.81064   -5.39340  1.000 87.06090  ?  85  ILE   G CG1 1 
ATOM   3227  C CG2 . ILE   C  1 85  ? -4.81577  4.02115   -4.18462  1.000 73.90255  ?  85  ILE   G CG2 1 
ATOM   3228  C CD1 . ILE   C  1 85  ? -5.80393  6.75157   -4.30470  1.000 78.96648  ?  85  ILE   G CD1 1 
ATOM   3229  N N   . GLN   C  1 86  ? -4.63508  1.56581   -6.64670  1.000 82.81690  ?  86  GLN   G N   1 
ATOM   3230  C CA  . GLN   C  1 86  ? -4.28393  0.16535   -6.54400  1.000 114.43209 ?  86  GLN   G CA  1 
ATOM   3231  C C   . GLN   C  1 86  ? -3.37643  -0.12430  -5.34793  1.000 65.27150  ?  86  GLN   G C   1 
ATOM   3232  O O   . GLN   C  1 86  ? -3.34813  -1.26605  -4.87340  1.000 111.96811 ?  86  GLN   G O   1 
ATOM   3233  C CB  . GLN   C  1 86  ? -3.60683  -0.31337  -7.83372  1.000 78.56758  ?  86  GLN   G CB  1 
ATOM   3234  N N   . ASP   C  1 87  ? -2.68723  0.88052   -4.80341  1.000 100.52195 ?  87  ASP   G N   1 
ATOM   3235  C CA  . ASP   C  1 87  ? -1.77534  0.67240   -3.68493  1.000 66.79434  ?  87  ASP   G CA  1 
ATOM   3236  C C   . ASP   C  1 87  ? -2.41873  1.00009   -2.34141  1.000 55.94618  ?  87  ASP   G C   1 
ATOM   3237  O O   . ASP   C  1 87  ? -3.48192  1.61607   -2.24760  1.000 76.33385  ?  87  ASP   G O   1 
ATOM   3238  C CB  . ASP   C  1 87  ? -0.51562  1.52316   -3.85246  1.000 59.04890  ?  87  ASP   G CB  1 
ATOM   3239  C CG  . ASP   C  1 87  ? 0.06198   1.41071   -5.23141  1.000 131.81440 ?  87  ASP   G CG  1 
ATOM   3240  O OD1 . ASP   C  1 87  ? -0.24912  0.41000   -5.92036  1.000 112.07011 -1 87  ASP   G OD1 1 
ATOM   3241  O OD2 . ASP   C  1 87  ? 0.81701   2.34435   -5.62274  1.000 110.10932 ?  87  ASP   G OD2 1 
ATOM   3242  N N   . SER   C  1 88  ? -1.72336  0.60622   -1.29981  1.000 54.43253  ?  88  SER   G N   1 
ATOM   3243  C CA  . SER   C  1 88  ? -2.15039  0.87209   0.05900   1.000 43.51016  ?  88  SER   G CA  1 
ATOM   3244  C C   . SER   C  1 88  ? -1.83036  2.32242   0.43451   1.000 85.89868  ?  88  SER   G C   1 
ATOM   3245  O O   . SER   C  1 88  ? -0.69063  2.77196   0.24596   1.000 53.39888  ?  88  SER   G O   1 
ATOM   3246  C CB  . SER   C  1 88  ? -1.46573  -0.10144  1.00628   1.000 44.55926  ?  88  SER   G CB  1 
ATOM   3247  O OG  . SER   C  1 88  ? -2.27735  -1.23868  1.25251   1.000 60.68955  ?  88  SER   G OG  1 
ATOM   3248  N N   . PRO   C  1 89  ? -2.81097  3.09820   0.96554   1.000 57.54851  ?  89  PRO   G N   1 
ATOM   3249  C CA  . PRO   C  1 89  ? -4.19709  2.74528   1.31008   1.000 34.06501  ?  89  PRO   G CA  1 
ATOM   3250  C C   . PRO   C  1 89  ? -5.14325  2.67576   0.10852   1.000 61.77014  ?  89  PRO   G C   1 
ATOM   3251  O O   . PRO   C  1 89  ? -5.12255  3.55720   -0.74772  1.000 44.36859  ?  89  PRO   G O   1 
ATOM   3252  C CB  . PRO   C  1 89  ? -4.64234  3.88474   2.23853   1.000 56.43368  ?  89  PRO   G CB  1 
ATOM   3253  C CG  . PRO   C  1 89  ? -3.52139  4.91823   2.23498   1.000 54.10334  ?  89  PRO   G CG  1 
ATOM   3254  C CD  . PRO   C  1 89  ? -2.58936  4.53994   1.12368   1.000 48.69975  ?  89  PRO   G CD  1 
ATOM   3255  N N   . ARG   C  1 90  ? -6.01713  1.66819   0.04134   1.000 31.63948  ?  90  ARG   G N   1 
ATOM   3256  C CA  . ARG   C  1 90  ? -6.99833  1.58682   -1.03292  1.000 48.63845  ?  90  ARG   G CA  1 
ATOM   3257  C C   . ARG   C  1 90  ? -8.39116  2.02978   -0.59998  1.000 39.32336  ?  90  ARG   G C   1 
ATOM   3258  O O   . ARG   C  1 90  ? -9.24863  2.25261   -1.45088  1.000 38.91075  ?  90  ARG   G O   1 
ATOM   3259  C CB  . ARG   C  1 90  ? -7.07806  0.16046   -1.59395  1.000 33.02959  ?  90  ARG   G CB  1 
ATOM   3260  N N   . ASN   C  1 91  ? -8.64667  2.18593   0.69114   1.000 39.02346  ?  91  ASN   G N   1 
ATOM   3261  C CA  . ASN   C  1 91  ? -9.93640  2.68206   1.14491   1.000 43.50359  ?  91  ASN   G CA  1 
ATOM   3262  C C   . ASN   C  1 91  ? -9.70418  3.42186   2.44224   1.000 42.13014  ?  91  ASN   G C   1 
ATOM   3263  O O   . ASN   C  1 91  ? -8.57748  3.50309   2.95219   1.000 48.68346  ?  91  ASN   G O   1 
ATOM   3264  C CB  . ASN   C  1 91  ? -10.94174 1.54444   1.33705   1.000 35.50500  ?  91  ASN   G CB  1 
ATOM   3265  C CG  . ASN   C  1 91  ? -10.32231 0.38393   2.08293   1.000 46.18251  ?  91  ASN   G CG  1 
ATOM   3266  O OD1 . ASN   C  1 91  ? -9.96951  0.49156   3.26206   1.000 56.37254  ?  91  ASN   G OD1 1 
ATOM   3267  N ND2 . ASN   C  1 91  ? -10.16054 -0.72550  1.39411   1.000 42.20822  ?  91  ASN   G ND2 1 
ATOM   3268  N N   . TYR   C  1 92  ? -10.79056 3.96338   2.98005   1.000 40.44289  ?  92  TYR   G N   1 
ATOM   3269  C CA  . TYR   C  1 92  ? -10.62985 4.72502   4.20235   1.000 34.18464  ?  92  TYR   G CA  1 
ATOM   3270  C C   . TYR   C  1 92  ? -10.31319 3.80850   5.38049   1.000 38.27861  ?  92  TYR   G C   1 
ATOM   3271  O O   . TYR   C  1 92  ? -9.65852  4.24202   6.33653   1.000 42.99523  ?  92  TYR   G O   1 
ATOM   3272  C CB  . TYR   C  1 92  ? -11.85692 5.62973   4.44548   1.000 23.40165  ?  92  TYR   G CB  1 
ATOM   3273  C CG  . TYR   C  1 92  ? -13.12493 4.98987   4.95571   1.000 28.86803  ?  92  TYR   G CG  1 
ATOM   3274  C CD1 . TYR   C  1 92  ? -13.30805 4.75722   6.31772   1.000 27.08594  ?  92  TYR   G CD1 1 
ATOM   3275  C CD2 . TYR   C  1 92  ? -14.18640 4.69575   4.08051   1.000 35.30183  ?  92  TYR   G CD2 1 
ATOM   3276  C CE1 . TYR   C  1 92  ? -14.48375 4.19783   6.79460   1.000 46.06734  ?  92  TYR   G CE1 1 
ATOM   3277  C CE2 . TYR   C  1 92  ? -15.36882 4.13753   4.55191   1.000 43.16214  ?  92  TYR   G CE2 1 
ATOM   3278  C CZ  . TYR   C  1 92  ? -15.50773 3.88810   5.90904   1.000 38.70550  ?  92  TYR   G CZ  1 
ATOM   3279  O OH  . TYR   C  1 92  ? -16.65387 3.33457   6.40115   1.000 55.46195  ?  92  TYR   G OH  1 
ATOM   3280  N N   . GLN   C  1 93  ? -10.68133 2.52750   5.30596   1.000 40.94038  ?  93  GLN   G N   1 
ATOM   3281  C CA  . GLN   C  1 93  ? -10.34067 1.63706   6.41309   1.000 53.54816  ?  93  GLN   G CA  1 
ATOM   3282  C C   . GLN   C  1 93  ? -8.84005  1.37689   6.46747   1.000 39.59673  ?  93  GLN   G C   1 
ATOM   3283  O O   . GLN   C  1 93  ? -8.24213  1.36944   7.55012   1.000 45.00684  ?  93  GLN   G O   1 
ATOM   3284  C CB  . GLN   C  1 93  ? -11.09227 0.31442   6.30313   1.000 34.42185  ?  93  GLN   G CB  1 
ATOM   3285  C CG  . GLN   C  1 93  ? -12.53585 0.37254   6.80391   1.000 51.15189  ?  93  GLN   G CG  1 
ATOM   3286  C CD  . GLN   C  1 93  ? -13.53694 0.58323   5.67787   1.000 170.45875 ?  93  GLN   G CD  1 
ATOM   3287  O OE1 . GLN   C  1 93  ? -13.18210 1.03161   4.57058   1.000 48.73153  ?  93  GLN   G OE1 1 
ATOM   3288  N NE2 . GLN   C  1 93  ? -14.79872 0.25685   5.95166   1.000 50.95080  ?  93  GLN   G NE2 1 
ATOM   3289  N N   . GLU   C  1 94  ? -8.20475  1.15957   5.31013   1.000 53.66975  ?  94  GLU   G N   1 
ATOM   3290  C CA  . GLU   C  1 94  ? -6.75422  0.98358   5.30569   1.000 26.01255  ?  94  GLU   G CA  1 
ATOM   3291  C C   . GLU   C  1 94  ? -6.06093  2.26985   5.71133   1.000 60.51790  ?  94  GLU   G C   1 
ATOM   3292  O O   . GLU   C  1 94  ? -5.03107  2.24577   6.39513   1.000 57.57648  ?  94  GLU   G O   1 
ATOM   3293  C CB  . GLU   C  1 94  ? -6.26237  0.56919   3.92756   1.000 57.45369  ?  94  GLU   G CB  1 
ATOM   3294  C CG  . GLU   C  1 94  ? -6.47261  -0.88220  3.62024   1.000 78.99653  ?  94  GLU   G CG  1 
ATOM   3295  C CD  . GLU   C  1 94  ? -5.85034  -1.24089  2.28972   1.000 141.69532 ?  94  GLU   G CD  1 
ATOM   3296  O OE1 . GLU   C  1 94  ? -4.81066  -0.60647  1.95235   1.000 50.16081  ?  94  GLU   G OE1 1 
ATOM   3297  O OE2 . GLU   C  1 94  ? -6.40570  -2.12853  1.59570   1.000 103.86795 -1 94  GLU   G OE2 1 
ATOM   3298  N N   . LEU   C  1 95  ? -6.60039  3.41326   5.27229   1.000 48.37488  ?  95  LEU   G N   1 
ATOM   3299  C CA  . LEU   C  1 95  ? -6.06360  4.69668   5.70939   1.000 29.41768  ?  95  LEU   G CA  1 
ATOM   3300  C C   . LEU   C  1 95  ? -6.01215  4.76089   7.22760   1.000 33.54613  ?  95  LEU   G C   1 
ATOM   3301  O O   . LEU   C  1 95  ? -4.96090  5.05531   7.81290   1.000 29.55570  ?  95  LEU   G O   1 
ATOM   3302  C CB  . LEU   C  1 95  ? -6.90370  5.84387   5.15238   1.000 36.52678  ?  95  LEU   G CB  1 
ATOM   3303  C CG  . LEU   C  1 95  ? -6.30013  7.23115   5.41628   1.000 36.59409  ?  95  LEU   G CG  1 
ATOM   3304  C CD1 . LEU   C  1 95  ? -4.93780  7.38879   4.72887   1.000 30.88255  ?  95  LEU   G CD1 1 
ATOM   3305  C CD2 . LEU   C  1 95  ? -7.27524  8.27899   4.93141   1.000 22.08115  ?  95  LEU   G CD2 1 
ATOM   3306  N N   . CYS   C  1 96  ? -7.13355  4.42476   7.88534   1.000 23.98672  ?  96  CYS   G N   1 
ATOM   3307  C CA  . CYS   C  1 96  ? -7.16923  4.44970   9.34350   1.000 34.77574  ?  96  CYS   G CA  1 
ATOM   3308  C C   . CYS   C  1 96  ? -6.15670  3.48636   9.95113   1.000 34.97486  ?  96  CYS   G C   1 
ATOM   3309  O O   . CYS   C  1 96  ? -5.54514  3.79281   10.98369  1.000 54.31408  ?  96  CYS   G O   1 
ATOM   3310  C CB  . CYS   C  1 96  ? -8.56892  4.12136   9.84120   1.000 28.30917  ?  96  CYS   G CB  1 
ATOM   3311  S SG  . CYS   C  1 96  ? -9.83616  5.36696   9.50683   1.000 44.01356  ?  96  CYS   G SG  1 
ATOM   3312  N N   . ASN   C  1 97  ? -5.98053  2.30541   9.34194   1.000 44.55401  ?  97  ASN   G N   1 
ATOM   3313  C CA  . ASN   C  1 97  ? -5.02758  1.34281   9.89307   1.000 34.82414  ?  97  ASN   G CA  1 
ATOM   3314  C C   . ASN   C  1 97  ? -3.59591  1.84336   9.75429   1.000 59.65366  ?  97  ASN   G C   1 
ATOM   3315  O O   . ASN   C  1 97  ? -2.78644  1.67912   10.67679  1.000 41.06600  ?  97  ASN   G O   1 
ATOM   3316  C CB  . ASN   C  1 97  ? -5.17389  -0.01577  9.21434   1.000 46.35070  ?  97  ASN   G CB  1 
ATOM   3317  C CG  . ASN   C  1 97  ? -6.43471  -0.73080  9.61829   1.000 85.82536  ?  97  ASN   G CG  1 
ATOM   3318  O OD1 . ASN   C  1 97  ? -6.89634  -0.60410  10.75625  1.000 58.39126  ?  97  ASN   G OD1 1 
ATOM   3319  N ND2 . ASN   C  1 97  ? -7.00747  -1.49079  8.68786   1.000 43.39662  ?  97  ASN   G ND2 1 
ATOM   3320  N N   . MET   C  1 98  ? -3.26486  2.45568   8.60842   1.000 28.32150  ?  98  MET   G N   1 
ATOM   3321  C CA  . MET   C  1 98  ? -1.92251  2.99812   8.43006   1.000 24.65105  ?  98  MET   G CA  1 
ATOM   3322  C C   . MET   C  1 98  ? -1.67065  4.17818   9.36830   1.000 62.69671  ?  98  MET   G C   1 
ATOM   3323  O O   . MET   C  1 98  ? -0.55422  4.33354   9.88056   1.000 42.55563  ?  98  MET   G O   1 
ATOM   3324  C CB  . MET   C  1 98  ? -1.70967  3.38514   6.96138   1.000 31.50806  ?  98  MET   G CB  1 
ATOM   3325  C CG  . MET   C  1 98  ? -1.72305  2.17166   6.02049   1.000 20.50187  ?  98  MET   G CG  1 
ATOM   3326  S SD  . MET   C  1 98  ? -1.70381  2.48811   4.25265   1.000 51.60684  ?  98  MET   G SD  1 
ATOM   3327  C CE  . MET   C  1 98  ? 0.00757   2.93441   3.99598   1.000 38.30451  ?  98  MET   G CE  1 
ATOM   3328  N N   . PHE   C  1 99  ? -2.69485  5.01121   9.61948   1.000 35.00878  ?  99  PHE   G N   1 
ATOM   3329  C CA  . PHE   C  1 99  ? -2.56520  6.06678   10.62792  1.000 31.03728  ?  99  PHE   G CA  1 
ATOM   3330  C C   . PHE   C  1 99  ? -2.18153  5.46911   11.97625  1.000 40.38490  ?  99  PHE   G C   1 
ATOM   3331  O O   . PHE   C  1 99  ? -1.33563  6.01058   12.70256  1.000 39.24991  ?  99  PHE   G O   1 
ATOM   3332  C CB  . PHE   C  1 99  ? -3.87618  6.86192   10.78504  1.000 29.51319  ?  99  PHE   G CB  1 
ATOM   3333  C CG  . PHE   C  1 99  ? -4.14156  7.87632   9.70047   1.000 37.72558  ?  99  PHE   G CG  1 
ATOM   3334  C CD1 . PHE   C  1 99  ? -3.21961  8.11973   8.67700   1.000 27.55122  ?  99  PHE   G CD1 1 
ATOM   3335  C CD2 . PHE   C  1 99  ? -5.33374  8.59678   9.71298   1.000 36.37629  ?  99  PHE   G CD2 1 
ATOM   3336  C CE1 . PHE   C  1 99  ? -3.48134  9.05272   7.68269   1.000 43.09677  ?  99  PHE   G CE1 1 
ATOM   3337  C CE2 . PHE   C  1 99  ? -5.60609  9.53739   8.72472   1.000 26.69049  ?  99  PHE   G CE2 1 
ATOM   3338  C CZ  . PHE   C  1 99  ? -4.67729  9.75923   7.69752   1.000 30.79422  ?  99  PHE   G CZ  1 
ATOM   3339  N N   . ASN   C  1 100 ? -2.81721  4.34460   12.32466  1.000 33.33797  ?  100 ASN   G N   1 
ATOM   3340  C CA  . ASN   C  1 100 ? -2.57782  3.69941   13.60884  1.000 37.59074  ?  100 ASN   G CA  1 
ATOM   3341  C C   . ASN   C  1 100 ? -1.12851  3.22939   13.74321  1.000 41.37537  ?  100 ASN   G C   1 
ATOM   3342  O O   . ASN   C  1 100 ? -0.56101  3.28854   14.84358  1.000 48.63118  ?  100 ASN   G O   1 
ATOM   3343  C CB  . ASN   C  1 100 ? -3.57285  2.54931   13.78881  1.000 37.07859  ?  100 ASN   G CB  1 
ATOM   3344  C CG  . ASN   C  1 100 ? -3.72157  2.13267   15.23385  1.000 48.53049  ?  100 ASN   G CG  1 
ATOM   3345  O OD1 . ASN   C  1 100 ? -4.19134  2.89981   16.08121  1.000 61.17711  ?  100 ASN   G OD1 1 
ATOM   3346  N ND2 . ASN   C  1 100 ? -3.33258  0.90347   15.52420  1.000 48.21049  ?  100 ASN   G ND2 1 
ATOM   3347  N N   . ASP   C  1 101 ? -0.50232  2.79863   12.63789  1.000 37.61992  ?  101 ASP   G N   1 
ATOM   3348  C CA  . ASP   C  1 101 ? 0.93229   2.51198   12.66877  1.000 31.34586  ?  101 ASP   G CA  1 
ATOM   3349  C C   . ASP   C  1 101 ? 1.74793   3.79535   12.76660  1.000 54.00675  ?  101 ASP   G C   1 
ATOM   3350  O O   . ASP   C  1 101 ? 2.63923   3.90847   13.62051  1.000 45.68100  ?  101 ASP   G O   1 
ATOM   3351  C CB  . ASP   C  1 101 ? 1.36341   1.71665   11.43131  1.000 31.42113  ?  101 ASP   G CB  1 
ATOM   3352  C CG  . ASP   C  1 101 ? 0.71407   0.34137   11.34493  1.000 114.18127 ?  101 ASP   G CG  1 
ATOM   3353  O OD1 . ASP   C  1 101 ? 0.44024   -0.27010  12.40127  1.000 49.47094  ?  101 ASP   G OD1 1 
ATOM   3354  O OD2 . ASP   C  1 101 ? 0.48991   -0.13259  10.20391  1.000 59.12772  -1 101 ASP   G OD2 1 
ATOM   3355  N N   . ILE   C  1 102 ? 1.45989   4.77072   11.88886  1.000 40.95389  ?  102 ILE   G N   1 
ATOM   3356  C CA  . ILE   C  1 102 ? 2.30180   5.96337   11.78163  1.000 25.41005  ?  102 ILE   G CA  1 
ATOM   3357  C C   . ILE   C  1 102 ? 2.36444   6.70686   13.10537  1.000 50.97177  ?  102 ILE   G C   1 
ATOM   3358  O O   . ILE   C  1 102 ? 3.44550   7.12236   13.54000  1.000 34.50978  ?  102 ILE   G O   1 
ATOM   3359  C CB  . ILE   C  1 102 ? 1.80484   6.88921   10.66207  1.000 28.23899  ?  102 ILE   G CB  1 
ATOM   3360  C CG1 . ILE   C  1 102 ? 1.93465   6.22700   9.29570   1.000 13.05640  ?  102 ILE   G CG1 1 
ATOM   3361  C CG2 . ILE   C  1 102 ? 2.59609   8.17567   10.67269  1.000 17.47057  ?  102 ILE   G CG2 1 
ATOM   3362  C CD1 . ILE   C  1 102 ? 1.60172   7.17817   8.14283   1.000 34.14167  ?  102 ILE   G CD1 1 
ATOM   3363  N N   . PHE   C  1 103 ? 1.21144   6.87279   13.77527  1.000 26.02482  ?  103 PHE   G N   1 
ATOM   3364  C CA  . PHE   C  1 103 ? 1.12394   7.67538   14.99310  1.000 50.53810  ?  103 PHE   G CA  1 
ATOM   3365  C C   . PHE   C  1 103 ? 1.76364   7.00137   16.20333  1.000 28.42246  ?  103 PHE   G C   1 
ATOM   3366  O O   . PHE   C  1 103 ? 1.78162   7.59377   17.28737  1.000 36.78293  ?  103 PHE   G O   1 
ATOM   3367  C CB  . PHE   C  1 103 ? -0.33776  8.00569   15.31010  1.000 17.94586  ?  103 PHE   G CB  1 
ATOM   3368  C CG  . PHE   C  1 103 ? -1.03351  8.82391   14.24120  1.000 35.20395  ?  103 PHE   G CG  1 
ATOM   3369  C CD1 . PHE   C  1 103 ? -0.30773  9.60418   13.34326  1.000 31.17946  ?  103 PHE   G CD1 1 
ATOM   3370  C CD2 . PHE   C  1 103 ? -2.41985  8.80521   14.13509  1.000 23.23454  ?  103 PHE   G CD2 1 
ATOM   3371  C CE1 . PHE   C  1 103 ? -0.96067  10.34298  12.35759  1.000 43.42716  ?  103 PHE   G CE1 1 
ATOM   3372  C CE2 . PHE   C  1 103 ? -3.07988  9.53898   13.15533  1.000 35.36681  ?  103 PHE   G CE2 1 
ATOM   3373  C CZ  . PHE   C  1 103 ? -2.35019  10.30772  12.26767  1.000 34.64979  ?  103 PHE   G CZ  1 
ATOM   3374  N N   . ARG   C  1 104 ? 2.29624   5.78311   16.00798  1.000 41.07974  ?  104 ARG   G N   1 
ATOM   3375  C CA  . ARG   C  1 104 ? 2.92176   4.96924   17.04858  1.000 32.34580  ?  104 ARG   G CA  1 
ATOM   3376  C C   . ARG   C  1 104 ? 4.43366   4.94872   16.94000  1.000 34.16643  ?  104 ARG   G C   1 
ATOM   3377  O O   . ARG   C  1 104 ? 5.10366   4.28353   17.74020  1.000 26.97366  ?  104 ARG   G O   1 
ATOM   3378  C CB  . ARG   C  1 104 ? 2.38705   3.52890   16.99787  1.000 50.79476  ?  104 ARG   G CB  1 
ATOM   3379  C CG  . ARG   C  1 104 ? 1.15763   3.29213   17.87778  1.000 69.71477  ?  104 ARG   G CG  1 
ATOM   3380  C CD  . ARG   C  1 104 ? 0.39425   2.02713   17.49483  1.000 42.87033  ?  104 ARG   G CD  1 
ATOM   3381  N NE  . ARG   C  1 104 ? 1.22427   1.13098   16.69790  1.000 123.31414 ?  104 ARG   G NE  1 
ATOM   3382  C CZ  . ARG   C  1 104 ? 0.75778   0.18340   15.89271  1.000 126.73738 ?  104 ARG   G CZ  1 
ATOM   3383  N NH1 . ARG   C  1 104 ? -0.54349  -0.04391  15.77024  1.000 149.26266 ?  104 ARG   G NH1 1 
ATOM   3384  N NH2 . ARG   C  1 104 ? 1.61715   -0.54721  15.18266  1.000 112.38324 ?  104 ARG   G NH2 1 
ATOM   3385  N N   . LYS   C  1 105 ? 4.98311   5.69902   15.99906  1.000 29.53688  ?  105 LYS   G N   1 
ATOM   3386  C CA  . LYS   C  1 105 ? 6.42311   5.71762   15.81784  1.000 50.27422  ?  105 LYS   G CA  1 
ATOM   3387  C C   . LYS   C  1 105 ? 6.84145   7.05593   15.22937  1.000 32.80499  ?  105 LYS   G C   1 
ATOM   3388  O O   . LYS   C  1 105 ? 6.02740   7.79201   14.67363  1.000 37.43226  ?  105 LYS   G O   1 
ATOM   3389  C CB  . LYS   C  1 105 ? 6.88269   4.52949   14.96073  1.000 40.49145  ?  105 LYS   G CB  1 
ATOM   3390  C CG  . LYS   C  1 105 ? 6.24181   4.46517   13.61176  1.000 30.43628  ?  105 LYS   G CG  1 
ATOM   3391  C CD  . LYS   C  1 105 ? 6.60437   3.17667   12.87355  1.000 30.90124  ?  105 LYS   G CD  1 
ATOM   3392  C CE  . LYS   C  1 105 ? 5.94927   1.97391   13.50807  1.000 61.10841  ?  105 LYS   G CE  1 
ATOM   3393  N NZ  . LYS   C  1 105 ? 5.76491   0.88548   12.51144  1.000 73.96132  ?  105 LYS   G NZ  1 
ATOM   3394  N N   . ALA   C  1 106 ? 8.11565   7.36825   15.39340  1.000 49.86418  ?  106 ALA   G N   1 
ATOM   3395  C CA  . ALA   C  1 106 ? 8.67735   8.62120   14.92517  1.000 43.12581  ?  106 ALA   G CA  1 
ATOM   3396  C C   . ALA   C  1 106 ? 9.05636   8.52431   13.45106  1.000 26.51644  ?  106 ALA   G C   1 
ATOM   3397  O O   . ALA   C  1 106 ? 9.31694   7.43179   12.94338  1.000 45.86603  ?  106 ALA   G O   1 
ATOM   3398  C CB  . ALA   C  1 106 ? 9.90343   8.99992   15.75589  1.000 29.43297  ?  106 ALA   G CB  1 
ATOM   3399  N N   . PRO   C  1 107 ? 9.07816   9.64992   12.73463  1.000 51.01910  ?  107 PRO   G N   1 
ATOM   3400  C CA  . PRO   C  1 107 ? 9.46905   9.60974   11.32243  1.000 33.35145  ?  107 PRO   G CA  1 
ATOM   3401  C C   . PRO   C  1 107 ? 10.94526  9.26428   11.17349  1.000 43.23428  ?  107 PRO   G C   1 
ATOM   3402  O O   . PRO   C  1 107 ? 11.74645  9.40210   12.10209  1.000 38.49768  ?  107 PRO   G O   1 
ATOM   3403  C CB  . PRO   C  1 107 ? 9.18715   11.03370  10.82324  1.000 31.40725  ?  107 PRO   G CB  1 
ATOM   3404  C CG  . PRO   C  1 107 ? 8.54187   11.74589  11.92622  1.000 28.01839  ?  107 PRO   G CG  1 
ATOM   3405  C CD  . PRO   C  1 107 ? 8.82060   11.02519  13.19413  1.000 21.84709  ?  107 PRO   G CD  1 
ATOM   3406  N N   . VAL   C  1 108 ? 11.30600  8.82792   9.97036   1.000 40.71209  ?  108 VAL   G N   1 
ATOM   3407  C CA  . VAL   C  1 108 ? 12.68730  8.51434   9.64860   1.000 36.57797  ?  108 VAL   G CA  1 
ATOM   3408  C C   . VAL   C  1 108 ? 13.11473  9.33500   8.42991   1.000 47.80975  ?  108 VAL   G C   1 
ATOM   3409  O O   . VAL   C  1 108 ? 12.29959  9.95191   7.74026   1.000 48.42513  ?  108 VAL   G O   1 
ATOM   3410  C CB  . VAL   C  1 108 ? 12.90002  7.00360   9.41809   1.000 46.81361  ?  108 VAL   G CB  1 
ATOM   3411  C CG1 . VAL   C  1 108 ? 12.45534  6.20656   10.66010  1.000 27.83607  ?  108 VAL   G CG1 1 
ATOM   3412  C CG2 . VAL   C  1 108 ? 12.14536  6.54197   8.20561   1.000 27.58228  ?  108 VAL   G CG2 1 
ATOM   3413  N N   . TYR   C  1 109 ? 14.42171  9.35566   8.19047   1.000 34.16445  ?  109 TYR   G N   1 
ATOM   3414  C CA  . TYR   C  1 109 ? 14.97505  10.11215  7.07363   1.000 63.61777  ?  109 TYR   G CA  1 
ATOM   3415  C C   . TYR   C  1 109 ? 14.86665  9.31102   5.78132   1.000 33.88105  ?  109 TYR   G C   1 
ATOM   3416  O O   . TYR   C  1 109 ? 15.05070  8.09075   5.77162   1.000 47.80572  ?  109 TYR   G O   1 
ATOM   3417  C CB  . TYR   C  1 109 ? 16.43863  10.48016  7.34136   1.000 28.03529  ?  109 TYR   G CB  1 
ATOM   3418  C CG  . TYR   C  1 109 ? 17.06733  11.24092  6.19725   1.000 60.84025  ?  109 TYR   G CG  1 
ATOM   3419  C CD1 . TYR   C  1 109 ? 16.97061  12.61691  6.11950   1.000 29.33133  ?  109 TYR   G CD1 1 
ATOM   3420  C CD2 . TYR   C  1 109 ? 17.73674  10.57646  5.17873   1.000 33.31023  ?  109 TYR   G CD2 1 
ATOM   3421  C CE1 . TYR   C  1 109 ? 17.53324  13.30667  5.06004   1.000 71.00325  ?  109 TYR   G CE1 1 
ATOM   3422  C CE2 . TYR   C  1 109 ? 18.29869  11.25525  4.11883   1.000 54.45163  ?  109 TYR   G CE2 1 
ATOM   3423  C CZ  . TYR   C  1 109 ? 18.19668  12.61844  4.06044   1.000 30.66836  ?  109 TYR   G CZ  1 
ATOM   3424  O OH  . TYR   C  1 109 ? 18.75016  13.31203  3.00774   1.000 56.93845  ?  109 TYR   G OH  1 
ATOM   3425  N N   . GLY   C  1 110 ? 14.55227  9.99662   4.68878   1.000 49.44944  ?  110 GLY   G N   1 
ATOM   3426  C CA  . GLY   C  1 110 ? 14.48788  9.29266   3.42716   1.000 14.44870  ?  110 GLY   G CA  1 
ATOM   3427  C C   . GLY   C  1 110 ? 13.41790  9.72382   2.44600   1.000 48.14553  ?  110 GLY   G C   1 
ATOM   3428  O O   . GLY   C  1 110 ? 13.69457  9.78974   1.24657   1.000 42.14758  ?  110 GLY   G O   1 
ATOM   3429  N N   . ASP   C  1 111 ? 12.20026  10.00494  2.91209   1.000 59.94820  ?  111 ASP   G N   1 
ATOM   3430  C CA  . ASP   C  1 111 ? 11.12317  10.30355  1.97981   1.000 50.52691  ?  111 ASP   G CA  1 
ATOM   3431  C C   . ASP   C  1 111 ? 11.11084  11.78418  1.61577   1.000 34.57348  ?  111 ASP   G C   1 
ATOM   3432  O O   . ASP   C  1 111 ? 11.72257  12.61907  2.28804   1.000 47.90566  ?  111 ASP   G O   1 
ATOM   3433  C CB  . ASP   C  1 111 ? 9.77882   9.87731   2.56065   1.000 63.25864  ?  111 ASP   G CB  1 
ATOM   3434  C CG  . ASP   C  1 111 ? 9.56910   8.38629   2.48250   1.000 61.96964  ?  111 ASP   G CG  1 
ATOM   3435  O OD1 . ASP   C  1 111 ? 9.44658   7.86655   1.35297   1.000 77.78706  ?  111 ASP   G OD1 1 
ATOM   3436  O OD2 . ASP   C  1 111 ? 9.55228   7.73456   3.54986   1.000 96.65533  -1 111 ASP   G OD2 1 
ATOM   3437  N N   . LEU   C  1 112 ? 10.39095  12.11035  0.54375   1.000 64.61832  ?  112 LEU   G N   1 
ATOM   3438  C CA  . LEU   C  1 112 ? 10.30605  13.50378  0.09585   1.000 13.32154  ?  112 LEU   G CA  1 
ATOM   3439  C C   . LEU   C  1 112 ? 9.55114   14.37387  1.08399   1.000 73.54260  ?  112 LEU   G C   1 
ATOM   3440  O O   . LEU   C  1 112 ? 9.81179   15.57813  1.19043   1.000 34.73219  ?  112 LEU   G O   1 
ATOM   3441  C CB  . LEU   C  1 112 ? 9.60123   13.59636  -1.24638  1.000 71.86160  ?  112 LEU   G CB  1 
ATOM   3442  C CG  . LEU   C  1 112 ? 10.01775  12.56039  -2.27795  1.000 140.13185 ?  112 LEU   G CG  1 
ATOM   3443  C CD1 . LEU   C  1 112 ? 9.33964   11.14565  -2.15104  1.000 80.21597  ?  112 LEU   G CD1 1 
ATOM   3444  C CD2 . LEU   C  1 112 ? 9.64472   13.27484  -3.50400  1.000 144.48934 ?  112 LEU   G CD2 1 
ATOM   3445  N N   . GLY   C  1 113 ? 8.59637   13.79194  1.79180   1.000 34.26611  ?  113 GLY   G N   1 
ATOM   3446  C CA  . GLY   C  1 113 ? 7.89890   14.51700  2.82334   1.000 32.74492  ?  113 GLY   G CA  1 
ATOM   3447  C C   . GLY   C  1 113 ? 7.60630   13.63503  4.02095   1.000 36.33473  ?  113 GLY   G C   1 
ATOM   3448  O O   . GLY   C  1 113 ? 7.95792   12.44665  4.05548   1.000 34.77346  ?  113 GLY   G O   1 
ATOM   3449  N N   . PRO   C  1 114 ? 6.94248   14.20048  5.02633   1.000 34.30107  ?  114 PRO   G N   1 
ATOM   3450  C CA  . PRO   C  1 114 ? 6.63078   13.43122  6.25207   1.000 27.61922  ?  114 PRO   G CA  1 
ATOM   3451  C C   . PRO   C  1 114 ? 5.62315   12.32719  5.96695   1.000 30.57939  ?  114 PRO   G C   1 
ATOM   3452  O O   . PRO   C  1 114 ? 5.00173   12.28893  4.88707   1.000 35.04799  ?  114 PRO   G O   1 
ATOM   3453  C CB  . PRO   C  1 114 ? 6.07476   14.50057  7.20842   1.000 32.63036  ?  114 PRO   G CB  1 
ATOM   3454  C CG  . PRO   C  1 114 ? 5.56381   15.60012  6.29155   1.000 29.58595  ?  114 PRO   G CG  1 
ATOM   3455  C CD  . PRO   C  1 114 ? 6.41618   15.57577  5.05685   1.000 30.67133  ?  114 PRO   G CD  1 
ATOM   3456  N N   . PRO   C  1 115 ? 5.46420   11.37346  6.89256   1.000 28.44301  ?  115 PRO   G N   1 
ATOM   3457  C CA  . PRO   C  1 115 ? 4.78721   10.10896  6.52262   1.000 39.42806  ?  115 PRO   G CA  1 
ATOM   3458  C C   . PRO   C  1 115 ? 3.29928   10.22959  6.25024   1.000 31.52686  ?  115 PRO   G C   1 
ATOM   3459  O O   . PRO   C  1 115 ? 2.79447   9.50626   5.37956   1.000 36.61991  ?  115 PRO   G O   1 
ATOM   3460  C CB  . PRO   C  1 115 ? 5.06057   9.18691   7.72178   1.000 21.20074  ?  115 PRO   G CB  1 
ATOM   3461  C CG  . PRO   C  1 115 ? 5.66293   10.04882  8.79793   1.000 23.75884  ?  115 PRO   G CG  1 
ATOM   3462  C CD  . PRO   C  1 115 ? 6.25984   11.24344  8.12843   1.000 33.72669  ?  115 PRO   G CD  1 
ATOM   3463  N N   . VAL   C  1 116 ? 2.57250   11.09214  6.97488   1.000 36.09180  ?  116 VAL   G N   1 
ATOM   3464  C CA  . VAL   C  1 116 ? 1.15225   11.27307  6.66893   1.000 26.35285  ?  116 VAL   G CA  1 
ATOM   3465  C C   . VAL   C  1 116 ? 0.97676   11.91142  5.29517   1.000 28.83387  ?  116 VAL   G C   1 
ATOM   3466  O O   . VAL   C  1 116 ? 0.13011   11.48117  4.49864   1.000 32.40773  ?  116 VAL   G O   1 
ATOM   3467  C CB  . VAL   C  1 116 ? 0.43064   12.09003  7.75413   1.000 33.52317  ?  116 VAL   G CB  1 
ATOM   3468  C CG1 . VAL   C  1 116 ? -1.03315  12.25890  7.35333   1.000 25.59752  ?  116 VAL   G CG1 1 
ATOM   3469  C CG2 . VAL   C  1 116 ? 0.53287   11.40326  9.10870   1.000 17.55705  ?  116 VAL   G CG2 1 
ATOM   3470  N N   . TYR   C  1 117 ? 1.76941   12.93932  4.98684   1.000 26.70675  ?  117 TYR   G N   1 
ATOM   3471  C CA  . TYR   C  1 117 ? 1.71777   13.50247  3.64213   1.000 40.23949  ?  117 TYR   G CA  1 
ATOM   3472  C C   . TYR   C  1 117 ? 1.92311   12.41892  2.57862   1.000 34.26019  ?  117 TYR   G C   1 
ATOM   3473  O O   . TYR   C  1 117 ? 1.17455   12.35173  1.59650   1.000 39.27182  ?  117 TYR   G O   1 
ATOM   3474  C CB  . TYR   C  1 117 ? 2.75477   14.62248  3.46216   1.000 25.82462  ?  117 TYR   G CB  1 
ATOM   3475  C CG  . TYR   C  1 117 ? 2.92571   14.89694  1.98625   1.000 33.09492  ?  117 TYR   G CG  1 
ATOM   3476  C CD1 . TYR   C  1 117 ? 1.98378   15.66077  1.29532   1.000 29.32372  ?  117 TYR   G CD1 1 
ATOM   3477  C CD2 . TYR   C  1 117 ? 3.96876   14.32419  1.26091   1.000 46.03363  ?  117 TYR   G CD2 1 
ATOM   3478  C CE1 . TYR   C  1 117 ? 2.09508   15.88447  -0.07106  1.000 29.75559  ?  117 TYR   G CE1 1 
ATOM   3479  C CE2 . TYR   C  1 117 ? 4.08182   14.53713  -0.09641  1.000 23.44856  ?  117 TYR   G CE2 1 
ATOM   3480  C CZ  . TYR   C  1 117 ? 3.14108   15.31847  -0.75702  1.000 39.87636  ?  117 TYR   G CZ  1 
ATOM   3481  O OH  . TYR   C  1 117 ? 3.25006   15.54267  -2.10519  1.000 29.61991  ?  117 TYR   G OH  1 
ATOM   3482  N N   . MET   C  1 118 ? 2.93825   11.56134  2.76059   1.000 35.70816  ?  118 MET   G N   1 
ATOM   3483  C CA  . MET   C  1 118 ? 3.27036   10.56392  1.74107   1.000 25.54034  ?  118 MET   G CA  1 
ATOM   3484  C C   . MET   C  1 118 ? 2.06645   9.67758   1.40450   1.000 41.16077  ?  118 MET   G C   1 
ATOM   3485  O O   . MET   C  1 118 ? 1.73916   9.48459   0.22750   1.000 33.32830  ?  118 MET   G O   1 
ATOM   3486  C CB  . MET   C  1 118 ? 4.45990   9.70403   2.18860   1.000 28.60918  ?  118 MET   G CB  1 
ATOM   3487  C CG  . MET   C  1 118 ? 5.84156   10.37400  2.23146   1.000 18.28003  ?  118 MET   G CG  1 
ATOM   3488  S SD  . MET   C  1 118 ? 6.44776   11.09107  0.68780   1.000 36.49563  ?  118 MET   G SD  1 
ATOM   3489  C CE  . MET   C  1 118 ? 6.45516   9.63957   -0.36297  1.000 41.06755  ?  118 MET   G CE  1 
ATOM   3490  N N   . ILE   C  1 119 ? 1.36927   9.14589   2.41875   1.000 32.07552  ?  119 ILE   G N   1 
ATOM   3491  C CA  . ILE   C  1 119 ? 0.19517   8.32634   2.10316   1.000 43.55477  ?  119 ILE   G CA  1 
ATOM   3492  C C   . ILE   C  1 119 ? -1.04918  9.13789   1.75731   1.000 43.98988  ?  119 ILE   G C   1 
ATOM   3493  O O   . ILE   C  1 119 ? -2.02526  8.55348   1.26234   1.000 48.65192  ?  119 ILE   G O   1 
ATOM   3494  C CB  . ILE   C  1 119 ? -0.15508  7.34029   3.23602   1.000 35.52699  ?  119 ILE   G CB  1 
ATOM   3495  C CG1 . ILE   C  1 119 ? -0.80741  8.04551   4.41723   1.000 37.81642  ?  119 ILE   G CG1 1 
ATOM   3496  C CG2 . ILE   C  1 119 ? 1.08692   6.62140   3.70932   1.000 43.03624  ?  119 ILE   G CG2 1 
ATOM   3497  C CD1 . ILE   C  1 119 ? -1.18778  7.07379   5.51088   1.000 42.69466  ?  119 ILE   G CD1 1 
ATOM   3498  N N   . MET   C  1 120 ? -1.04545  10.46520  1.96689   1.000 26.01092  ?  120 MET   G N   1 
ATOM   3499  C CA  . MET   C  1 120 ? -2.21249  11.29763  1.65643   1.000 24.00959  ?  120 MET   G CA  1 
ATOM   3500  C C   . MET   C  1 120 ? -2.14749  11.96625  0.28848   1.000 29.84052  ?  120 MET   G C   1 
ATOM   3501  O O   . MET   C  1 120 ? -3.18434  12.41601  -0.21083  1.000 29.44545  ?  120 MET   G O   1 
ATOM   3502  C CB  . MET   C  1 120 ? -2.39141  12.40896  2.70693   1.000 11.63466  ?  120 MET   G CB  1 
ATOM   3503  C CG  . MET   C  1 120 ? -2.84129  11.92334  4.06667   1.000 19.52577  ?  120 MET   G CG  1 
ATOM   3504  S SD  . MET   C  1 120 ? -4.50062  11.26233  4.10060   1.000 35.64474  ?  120 MET   G SD  1 
ATOM   3505  C CE  . MET   C  1 120 ? -5.45813  12.77908  4.15510   1.000 20.28498  ?  120 MET   G CE  1 
ATOM   3506  N N   . ALA   C  1 121 ? -0.95952  12.05192  -0.31748  1.000 26.95267  ?  121 ALA   G N   1 
ATOM   3507  C CA  . ALA   C  1 121 ? -0.77247  12.93194  -1.47036  1.000 32.73753  ?  121 ALA   G CA  1 
ATOM   3508  C C   . ALA   C  1 121 ? -1.69514  12.55719  -2.62259  1.000 33.11315  ?  121 ALA   G C   1 
ATOM   3509  O O   . ALA   C  1 121 ? -2.23355  13.43891  -3.30722  1.000 40.08666  ?  121 ALA   G O   1 
ATOM   3510  C CB  . ALA   C  1 121 ? 0.69283   12.90572  -1.92302  1.000 24.65342  ?  121 ALA   G CB  1 
ATOM   3511  N N   . LYS   C  1 122 ? -1.88525  11.25212  -2.86206  1.000 28.74353  ?  122 LYS   G N   1 
ATOM   3512  C CA  . LYS   C  1 122 ? -2.76298  10.83508  -3.95360  1.000 21.28025  ?  122 LYS   G CA  1 
ATOM   3513  C C   . LYS   C  1 122 ? -4.21053  11.25893  -3.67523  1.000 35.50550  ?  122 LYS   G C   1 
ATOM   3514  O O   . LYS   C  1 122 ? -4.90671  11.73683  -4.57343  1.000 29.33762  ?  122 LYS   G O   1 
ATOM   3515  C CB  . LYS   C  1 122 ? -2.65150  9.31380   -4.18163  1.000 20.69495  ?  122 LYS   G CB  1 
ATOM   3516  N N   . LEU   C  1 123 ? -4.66169  11.14760  -2.41949  1.000 31.55033  ?  123 LEU   G N   1 
ATOM   3517  C CA  . LEU   C  1 123 ? -6.01158  11.58344  -2.04105  1.000 31.05102  ?  123 LEU   G CA  1 
ATOM   3518  C C   . LEU   C  1 123 ? -6.18094  13.09375  -2.17942  1.000 56.04059  ?  123 LEU   G C   1 
ATOM   3519  O O   . LEU   C  1 123 ? -7.19312  13.57351  -2.72046  1.000 23.11989  ?  123 LEU   G O   1 
ATOM   3520  C CB  . LEU   C  1 123 ? -6.31954  11.14797  -0.60615  1.000 22.13795  ?  123 LEU   G CB  1 
ATOM   3521  C CG  . LEU   C  1 123 ? -5.95547  9.69266   -0.34067  1.000 31.08038  ?  123 LEU   G CG  1 
ATOM   3522  C CD1 . LEU   C  1 123 ? -6.29259  9.27657   1.08406   1.000 25.23494  ?  123 LEU   G CD1 1 
ATOM   3523  C CD2 . LEU   C  1 123 ? -6.67962  8.82362   -1.33853  1.000 25.06440  ?  123 LEU   G CD2 1 
ATOM   3524  N N   . MET   C  1 124 ? -5.21650  13.86278  -1.65454  1.000 26.35054  ?  124 MET   G N   1 
ATOM   3525  C CA  . MET   C  1 124 ? -5.28663  15.31609  -1.76788  1.000 37.74184  ?  124 MET   G CA  1 
ATOM   3526  C C   . MET   C  1 124 ? -5.42283  15.76973  -3.21013  1.000 30.30833  ?  124 MET   G C   1 
ATOM   3527  O O   . MET   C  1 124 ? -5.94426  16.85977  -3.47022  1.000 29.45799  ?  124 MET   G O   1 
ATOM   3528  C CB  . MET   C  1 124 ? -4.04398  15.96104  -1.16878  1.000 15.32460  ?  124 MET   G CB  1 
ATOM   3529  C CG  . MET   C  1 124 ? -3.83018  15.65830  0.28071   1.000 35.56983  ?  124 MET   G CG  1 
ATOM   3530  S SD  . MET   C  1 124 ? -2.08297  15.84457  0.69636   1.000 37.45548  ?  124 MET   G SD  1 
ATOM   3531  C CE  . MET   C  1 124 ? -1.76310  17.55229  0.30676   1.000 13.12785  ?  124 MET   G CE  1 
ATOM   3532  N N   . ASN   C  1 125 ? -4.95093  14.95910  -4.15608  1.000 36.04103  ?  125 ASN   G N   1 
ATOM   3533  C CA  . ASN   C  1 125 ? -4.91708  15.33182  -5.55880  1.000 29.92315  ?  125 ASN   G CA  1 
ATOM   3534  C C   . ASN   C  1 125 ? -6.21239  14.98297  -6.30490  1.000 35.54684  ?  125 ASN   G C   1 
ATOM   3535  O O   . ASN   C  1 125 ? -6.20554  14.87368  -7.53484  1.000 39.53523  ?  125 ASN   G O   1 
ATOM   3536  C CB  . ASN   C  1 125 ? -3.72512  14.66611  -6.24283  1.000 28.40916  ?  125 ASN   G CB  1 
ATOM   3537  C CG  . ASN   C  1 125 ? -3.30146  15.39592  -7.49913  1.000 26.54007  ?  125 ASN   G CG  1 
ATOM   3538  O OD1 . ASN   C  1 125 ? -3.66454  16.55897  -7.71931  1.000 32.70341  ?  125 ASN   G OD1 1 
ATOM   3539  N ND2 . ASN   C  1 125 ? -2.51855  14.72252  -8.32771  1.000 43.85322  ?  125 ASN   G ND2 1 
ATOM   3540  N N   . THR   C  1 126 ? -7.32071  14.82537  -5.60048  1.000 34.50253  ?  126 THR   G N   1 
ATOM   3541  C CA  . THR   C  1 126 ? -8.61098  14.57608  -6.22039  1.000 43.59245  ?  126 THR   G CA  1 
ATOM   3542  C C   . THR   C  1 126 ? -9.58806  15.66553  -5.80939  1.000 22.46284  ?  126 THR   G C   1 
ATOM   3543  O O   . THR   C  1 126 ? -9.38294  16.36822  -4.81537  1.000 41.38550  ?  126 THR   G O   1 
ATOM   3544  C CB  . THR   C  1 126 ? -9.17493  13.20952  -5.81071  1.000 28.34255  ?  126 THR   G CB  1 
ATOM   3545  O OG1 . THR   C  1 126 ? -9.61451  13.25885  -4.43976  1.000 27.76490  ?  126 THR   G OG1 1 
ATOM   3546  C CG2 . THR   C  1 126 ? -8.11294  12.12393  -5.96784  1.000 13.36274  ?  126 THR   G CG2 1 
ATOM   3547  N N   . ARG   C  1 127 ? -10.67424 15.77830  -6.55937  1.000 31.62963  ?  127 ARG   G N   1 
ATOM   3548  C CA  . ARG   C  1 127 ? -11.68874 16.73643  -6.13672  1.000 23.85319  ?  127 ARG   G CA  1 
ATOM   3549  C C   . ARG   C  1 127 ? -12.40037 16.24001  -4.88220  1.000 46.06489  ?  127 ARG   G C   1 
ATOM   3550  O O   . ARG   C  1 127 ? -12.66258 17.03378  -3.96500  1.000 31.80987  ?  127 ARG   G O   1 
ATOM   3551  C CB  . ARG   C  1 127 ? -12.67249 17.03442  -7.28840  1.000 8.88689   ?  127 ARG   G CB  1 
ATOM   3552  C CG  . ARG   C  1 127 ? -11.91227 17.29161  -8.61257  1.000 110.31031 ?  127 ARG   G CG  1 
ATOM   3553  C CD  . ARG   C  1 127 ? -12.50494 18.40175  -9.39940  1.000 60.34687  ?  127 ARG   G CD  1 
ATOM   3554  N NE  . ARG   C  1 127 ? -13.94761 18.38453  -9.22471  1.000 127.32307 ?  127 ARG   G NE  1 
ATOM   3555  C CZ  . ARG   C  1 127 ? -14.78787 19.03169  -10.01258 1.000 75.11469  ?  127 ARG   G CZ  1 
ATOM   3556  N NH1 . ARG   C  1 127 ? -14.34890 19.76640  -11.02518 1.000 65.48323  ?  127 ARG   G NH1 1 
ATOM   3557  N NH2 . ARG   C  1 127 ? -16.09565 18.92842  -9.78649  1.000 96.63529  ?  127 ARG   G NH2 1 
ATOM   3558  N N   . ALA   C  1 128 ? -12.67080 14.92854  -4.79569  1.000 18.91470  ?  128 ALA   G N   1 
ATOM   3559  C CA  . ALA   C  1 128 ? -13.30296 14.38877  -3.59607  1.000 31.88595  ?  128 ALA   G CA  1 
ATOM   3560  C C   . ALA   C  1 128 ? -12.44504 14.65331  -2.36099  1.000 22.81723  ?  128 ALA   G C   1 
ATOM   3561  O O   . ALA   C  1 128 ? -12.96818 15.04374  -1.30706  1.000 33.65700  ?  128 ALA   G O   1 
ATOM   3562  C CB  . ALA   C  1 128 ? -13.57368 12.88472  -3.77032  1.000 20.65418  ?  128 ALA   G CB  1 
ATOM   3563  N N   . GLY   C  1 129 ? -11.12205 14.46851  -2.47875  1.000 45.35822  ?  129 GLY   G N   1 
ATOM   3564  C CA  . GLY   C  1 129 ? -10.24006 14.69422  -1.33650  1.000 13.36743  ?  129 GLY   G CA  1 
ATOM   3565  C C   . GLY   C  1 129 ? -10.20172 16.15349  -0.90704  1.000 37.86432  ?  129 GLY   G C   1 
ATOM   3566  O O   . GLY   C  1 129 ? -10.31275 16.47290  0.28308   1.000 27.70964  ?  129 GLY   G O   1 
ATOM   3567  N N   . PHE   C  1 130 ? -10.06177 17.06275  -1.87559  1.000 24.96942  ?  130 PHE   G N   1 
ATOM   3568  C CA  . PHE   C  1 130 ? -10.09245 18.48341  -1.55237  1.000 25.05581  ?  130 PHE   G CA  1 
ATOM   3569  C C   . PHE   C  1 130 ? -11.39351 18.87182  -0.84264  1.000 45.98737  ?  130 PHE   G C   1 
ATOM   3570  O O   . PHE   C  1 130 ? -11.35793 19.61081  0.14695   1.000 37.14212  ?  130 PHE   G O   1 
ATOM   3571  C CB  . PHE   C  1 130 ? -9.88716  19.30043  -2.82620  1.000 13.64804  ?  130 PHE   G CB  1 
ATOM   3572  C CG  . PHE   C  1 130 ? -9.97094  20.77943  -2.61680  1.000 27.09272  ?  130 PHE   G CG  1 
ATOM   3573  C CD1 . PHE   C  1 130 ? -11.20720 21.43210  -2.60909  1.000 27.08871  ?  130 PHE   G CD1 1 
ATOM   3574  C CD2 . PHE   C  1 130 ? -8.82173  21.52695  -2.43634  1.000 20.68995  ?  130 PHE   G CD2 1 
ATOM   3575  C CE1 . PHE   C  1 130 ? -11.30132 22.80287  -2.41683  1.000 25.92168  ?  130 PHE   G CE1 1 
ATOM   3576  C CE2 . PHE   C  1 130 ? -8.90492  22.90523  -2.23879  1.000 34.51481  ?  130 PHE   G CE2 1 
ATOM   3577  C CZ  . PHE   C  1 130 ? -10.16605 23.54347  -2.23490  1.000 20.96337  ?  130 PHE   G CZ  1 
ATOM   3578  N N   . SER   C  1 131 ? -12.55121 18.39772  -1.33406  1.000 24.08413  ?  131 SER   G N   1 
ATOM   3579  C CA  . SER   C  1 131 ? -13.81266 18.66605  -0.63545  1.000 41.75751  ?  131 SER   G CA  1 
ATOM   3580  C C   . SER   C  1 131 ? -13.74872 18.22028  0.82041   1.000 29.41656  ?  131 SER   G C   1 
ATOM   3581  O O   . SER   C  1 131 ? -14.09442 18.98435  1.73407   1.000 40.26314  ?  131 SER   G O   1 
ATOM   3582  C CB  . SER   C  1 131 ? -14.98410 17.97258  -1.32990  1.000 12.98257  ?  131 SER   G CB  1 
ATOM   3583  O OG  . SER   C  1 131 ? -15.59328 18.85102  -2.23665  1.000 84.84958  ?  131 SER   G OG  1 
ATOM   3584  N N   . ALA   C  1 132 ? -13.34673 16.96538  1.05136   1.000 27.19692  ?  132 ALA   G N   1 
ATOM   3585  C CA  . ALA   C  1 132 ? -13.31375 16.44638  2.41368   1.000 21.45914  ?  132 ALA   G CA  1 
ATOM   3586  C C   . ALA   C  1 132 ? -12.39327 17.28367  3.28588   1.000 35.74937  ?  132 ALA   G C   1 
ATOM   3587  O O   . ALA   C  1 132 ? -12.76481 17.69043  4.39750   1.000 29.51350  ?  132 ALA   G O   1 
ATOM   3588  C CB  . ALA   C  1 132 ? -12.86480 14.98886  2.41148   1.000 22.18135  ?  132 ALA   G CB  1 
ATOM   3589  N N   . PHE   C  1 133 ? -11.19740 17.58250  2.76953   1.000 22.06189  ?  133 PHE   G N   1 
ATOM   3590  C CA  . PHE   C  1 133 ? -10.13800 18.24688  3.51885   1.000 32.63660  ?  133 PHE   G CA  1 
ATOM   3591  C C   . PHE   C  1 133 ? -10.38317 19.74304  3.69557   1.000 39.58526  ?  133 PHE   G C   1 
ATOM   3592  O O   . PHE   C  1 133 ? -9.59683  20.41320  4.37860   1.000 29.09783  ?  133 PHE   G O   1 
ATOM   3593  C CB  . PHE   C  1 133 ? -8.78966  17.99525  2.83622   1.000 24.85540  ?  133 PHE   G CB  1 
ATOM   3594  C CG  . PHE   C  1 133 ? -8.50524  16.53063  2.60042   1.000 35.80545  ?  133 PHE   G CG  1 
ATOM   3595  C CD1 . PHE   C  1 133 ? -9.11698  15.54759  3.39468   1.000 31.35765  ?  133 PHE   G CD1 1 
ATOM   3596  C CD2 . PHE   C  1 133 ? -7.64679  16.13004  1.58038   1.000 26.07015  ?  133 PHE   G CD2 1 
ATOM   3597  C CE1 . PHE   C  1 133 ? -8.87342  14.19445  3.17592   1.000 23.22204  ?  133 PHE   G CE1 1 
ATOM   3598  C CE2 . PHE   C  1 133 ? -7.39505  14.78480  1.34656   1.000 25.49316  ?  133 PHE   G CE2 1 
ATOM   3599  C CZ  . PHE   C  1 133 ? -8.00885  13.80939  2.14809   1.000 19.28567  ?  133 PHE   G CZ  1 
ATOM   3600  N N   . THR   C  1 134 ? -11.46171 20.28424  3.12685   1.000 22.46831  ?  134 THR   G N   1 
ATOM   3601  C CA  . THR   C  1 134 ? -11.83044 21.67264  3.36340   1.000 27.12707  ?  134 THR   G CA  1 
ATOM   3602  C C   . THR   C  1 134 ? -13.11137 21.79417  4.19326   1.000 24.95377  ?  134 THR   G C   1 
ATOM   3603  O O   . THR   C  1 134 ? -13.80101 22.81542  4.13619   1.000 32.90534  ?  134 THR   G O   1 
ATOM   3604  C CB  . THR   C  1 134 ? -11.94825 22.44766  2.04922   1.000 27.14384  ?  134 THR   G CB  1 
ATOM   3605  O OG1 . THR   C  1 134 ? -12.69764 21.69473  1.08498   1.000 32.83211  ?  134 THR   G OG1 1 
ATOM   3606  C CG2 . THR   C  1 134 ? -10.55861 22.75480  1.49383   1.000 20.13900  ?  134 THR   G CG2 1 
ATOM   3607  N N   . ARG   C  1 135 ? -13.41478 20.77428  5.00024   1.000 27.03633  ?  135 ARG   G N   1 
ATOM   3608  C CA  . ARG   C  1 135 ? -14.50032 20.82399  5.97832   1.000 27.21475  ?  135 ARG   G CA  1 
ATOM   3609  C C   . ARG   C  1 135 ? -13.89676 21.03819  7.36085   1.000 40.83955  ?  135 ARG   G C   1 
ATOM   3610  O O   . ARG   C  1 135 ? -13.09110 20.21834  7.82428   1.000 27.44859  ?  135 ARG   G O   1 
ATOM   3611  C CB  . ARG   C  1 135 ? -15.33185 19.53937  5.96927   1.000 18.03285  ?  135 ARG   G CB  1 
ATOM   3612  C CG  . ARG   C  1 135 ? -15.99477 19.20430  4.63454   1.000 22.23816  ?  135 ARG   G CG  1 
ATOM   3613  C CD  . ARG   C  1 135 ? -16.42828 17.76241  4.66610   1.000 24.97409  ?  135 ARG   G CD  1 
ATOM   3614  N NE  . ARG   C  1 135 ? -17.13107 17.35851  3.46100   1.000 44.26891  ?  135 ARG   G NE  1 
ATOM   3615  C CZ  . ARG   C  1 135 ? -18.35888 17.74903  3.15219   1.000 48.08500  ?  135 ARG   G CZ  1 
ATOM   3616  N NH1 . ARG   C  1 135 ? -19.04732 18.55539  3.94471   1.000 39.25952  ?  135 ARG   G NH1 1 
ATOM   3617  N NH2 . ARG   C  1 135 ? -18.90278 17.33479  2.00954   1.000 37.18942  ?  135 ARG   G NH2 1 
ATOM   3618  N N   . GLN   C  1 136 ? -14.28288 22.13990  8.01624   1.000 25.77440  ?  136 GLN   G N   1 
ATOM   3619  C CA  . GLN   C  1 136 ? -13.77505 22.41354  9.35783   1.000 27.79287  ?  136 GLN   G CA  1 
ATOM   3620  C C   . GLN   C  1 136 ? -14.05333 21.25842  10.30521  1.000 25.15696  ?  136 GLN   G C   1 
ATOM   3621  O O   . GLN   C  1 136 ? -13.23655 20.98083  11.19593  1.000 42.65135  ?  136 GLN   G O   1 
ATOM   3622  C CB  . GLN   C  1 136 ? -14.37915 23.70679  9.90271   1.000 25.84535  ?  136 GLN   G CB  1 
ATOM   3623  C CG  . GLN   C  1 136 ? -14.02468 24.91261  9.06766   1.000 21.07815  ?  136 GLN   G CG  1 
ATOM   3624  C CD  . GLN   C  1 136 ? -13.59167 26.09001  9.90478   1.000 46.33647  ?  136 GLN   G CD  1 
ATOM   3625  O OE1 . GLN   C  1 136 ? -14.22781 26.42774  10.92627  1.000 34.25644  ?  136 GLN   G OE1 1 
ATOM   3626  N NE2 . GLN   C  1 136 ? -12.49296 26.72684  9.48619   1.000 21.58056  ?  136 GLN   G NE2 1 
ATOM   3627  N N   . ARG   C  1 137 ? -15.20440 20.56633  10.12409  1.000 24.54903  ?  137 ARG   G N   1 
ATOM   3628  C CA  . ARG   C  1 137 ? -15.56270 19.46559  11.03127  1.000 23.78089  ?  137 ARG   G CA  1 
ATOM   3629  C C   . ARG   C  1 137 ? -14.59330 18.28972  10.93543  1.000 18.92903  ?  137 ARG   G C   1 
ATOM   3630  O O   . ARG   C  1 137 ? -14.22591 17.71792  11.96623  1.000 37.34624  ?  137 ARG   G O   1 
ATOM   3631  C CB  . ARG   C  1 137 ? -16.99399 18.99590  10.78243  1.000 16.53766  ?  137 ARG   G CB  1 
ATOM   3632  C CG  . ARG   C  1 137 ? -18.04643 19.91186  11.37143  1.000 18.53253  ?  137 ARG   G CG  1 
ATOM   3633  C CD  . ARG   C  1 137 ? -19.41734 19.24108  11.16611  1.000 26.36957  ?  137 ARG   G CD  1 
ATOM   3634  N NE  . ARG   C  1 137 ? -20.55204 20.09121  11.54118  1.000 28.91479  ?  137 ARG   G NE  1 
ATOM   3635  C CZ  . ARG   C  1 137 ? -21.79761 19.90497  11.10553  1.000 47.47028  ?  137 ARG   G CZ  1 
ATOM   3636  N NH1 . ARG   C  1 137 ? -22.09072 18.96438  10.21848  1.000 15.61468  ?  137 ARG   G NH1 1 
ATOM   3637  N NH2 . ARG   C  1 137 ? -22.77320 20.67971  11.56964  1.000 30.72721  ?  137 ARG   G NH2 1 
ATOM   3638  N N   . LEU   C  1 138 ? -14.17607 17.89508  9.70579   1.000 13.88597  ?  138 LEU   G N   1 
ATOM   3639  C CA  . LEU   C  1 138 ? -13.12179 16.89074  9.53227   1.000 26.94344  ?  138 LEU   G CA  1 
ATOM   3640  C C   . LEU   C  1 138 ? -11.77572 17.37663  10.06823  1.000 36.38245  ?  138 LEU   G C   1 
ATOM   3641  O O   . LEU   C  1 138 ? -11.04659 16.62004  10.72381  1.000 25.93174  ?  138 LEU   G O   1 
ATOM   3642  C CB  . LEU   C  1 138 ? -12.97928 16.52735  8.05812   1.000 20.72677  ?  138 LEU   G CB  1 
ATOM   3643  C CG  . LEU   C  1 138 ? -12.01496 15.38235  7.79436   1.000 34.60663  ?  138 LEU   G CG  1 
ATOM   3644  C CD1 . LEU   C  1 138 ? -12.59401 14.12798  8.41468   1.000 21.08516  ?  138 LEU   G CD1 1 
ATOM   3645  C CD2 . LEU   C  1 138 ? -11.78480 15.18936  6.30459   1.000 18.41815  ?  138 LEU   G CD2 1 
ATOM   3646  N N   . ASN   C  1 139 ? -11.42300 18.63227  9.79321   1.000 20.03802  ?  139 ASN   G N   1 
ATOM   3647  C CA  . ASN   C  1 139 ? -10.11663 19.11702  10.21798  1.000 36.24046  ?  139 ASN   G CA  1 
ATOM   3648  C C   . ASN   C  1 139 ? -9.97809  19.12240  11.73537  1.000 22.84775  ?  139 ASN   G C   1 
ATOM   3649  O O   . ASN   C  1 139 ? -8.85824  18.97720  12.24527  1.000 36.74993  ?  139 ASN   G O   1 
ATOM   3650  C CB  . ASN   C  1 139 ? -9.85533  20.49281  9.60793   1.000 12.54164  ?  139 ASN   G CB  1 
ATOM   3651  C CG  . ASN   C  1 139 ? -9.51385  20.38530  8.13734   1.000 29.36409  ?  139 ASN   G CG  1 
ATOM   3652  O OD1 . ASN   C  1 139 ? -8.76584  19.48006  7.74551   1.000 20.94294  ?  139 ASN   G OD1 1 
ATOM   3653  N ND2 . ASN   C  1 139 ? -10.08526 21.25582  7.30980   1.000 17.76381  ?  139 ASN   G ND2 1 
ATOM   3654  N N   . LEU   C  1 140 ? -11.09293 19.25402  12.46974  1.000 36.06966  ?  140 LEU   G N   1 
ATOM   3655  C CA  . LEU   C  1 140 ? -11.04379 19.07809  13.92199  1.000 24.22127  ?  140 LEU   G CA  1 
ATOM   3656  C C   . LEU   C  1 140 ? -10.47982 17.71378  14.29152  1.000 46.50143  ?  140 LEU   G C   1 
ATOM   3657  O O   . LEU   C  1 140 ? -9.74620  17.58643  15.28308  1.000 25.42684  ?  140 LEU   G O   1 
ATOM   3658  C CB  . LEU   C  1 140 ? -12.43091 19.23288  14.53171  1.000 23.75993  ?  140 LEU   G CB  1 
ATOM   3659  C CG  . LEU   C  1 140 ? -12.95185 20.66097  14.58529  1.000 40.00100  ?  140 LEU   G CG  1 
ATOM   3660  C CD1 . LEU   C  1 140 ? -14.37389 20.71047  15.10810  1.000 17.96918  ?  140 LEU   G CD1 1 
ATOM   3661  C CD2 . LEU   C  1 140 ? -12.03423 21.49698  15.43941  1.000 11.82433  ?  140 LEU   G CD2 1 
ATOM   3662  N N   . HIS   C  1 141 ? -10.81292 16.67793  13.50370  1.000 28.07199  ?  141 HIS   G N   1 
ATOM   3663  C CA  . HIS   C  1 141 ? -10.30941 15.34087  13.80242  1.000 25.97070  ?  141 HIS   G CA  1 
ATOM   3664  C C   . HIS   C  1 141 ? -8.83072  15.21178  13.45885  1.000 27.14773  ?  141 HIS   G C   1 
ATOM   3665  O O   . HIS   C  1 141 ? -8.05269  14.67448  14.25556  1.000 33.83473  ?  141 HIS   G O   1 
ATOM   3666  C CB  . HIS   C  1 141 ? -11.13713 14.29895  13.07222  1.000 15.94658  ?  141 HIS   G CB  1 
ATOM   3667  C CG  . HIS   C  1 141 ? -12.50112 14.12431  13.65777  1.000 43.49735  ?  141 HIS   G CG  1 
ATOM   3668  N ND1 . HIS   C  1 141 ? -12.73577 13.33237  14.75996  1.000 41.33482  ?  141 HIS   G ND1 1 
ATOM   3669  C CD2 . HIS   C  1 141 ? -13.69743 14.66515  13.32001  1.000 36.65609  ?  141 HIS   G CD2 1 
ATOM   3670  C CE1 . HIS   C  1 141 ? -14.01983 13.38014  15.06717  1.000 28.85709  ?  141 HIS   G CE1 1 
ATOM   3671  N NE2 . HIS   C  1 141 ? -14.62719 14.17811  14.20644  1.000 42.10539  ?  141 HIS   G NE2 1 
ATOM   3672  N N   . PHE   C  1 142 ? -8.41362  15.71920  12.29170  1.000 31.63626  ?  142 PHE   G N   1 
ATOM   3673  C CA  . PHE   C  1 142 ? -6.98375  15.74175  11.98113  1.000 44.87128  ?  142 PHE   G CA  1 
ATOM   3674  C C   . PHE   C  1 142 ? -6.19654  16.42340  13.09050  1.000 31.76602  ?  142 PHE   G C   1 
ATOM   3675  O O   . PHE   C  1 142 ? -5.11583  15.95644  13.48025  1.000 33.72519  ?  142 PHE   G O   1 
ATOM   3676  C CB  . PHE   C  1 142 ? -6.73505  16.44384  10.64714  1.000 30.83709  ?  142 PHE   G CB  1 
ATOM   3677  C CG  . PHE   C  1 142 ? -7.08628  15.61009  9.45277   1.000 38.02147  ?  142 PHE   G CG  1 
ATOM   3678  C CD1 . PHE   C  1 142 ? -6.65762  14.29955  9.35992   1.000 32.85352  ?  142 PHE   G CD1 1 
ATOM   3679  C CD2 . PHE   C  1 142 ? -7.85568  16.13405  8.42437   1.000 34.34457  ?  142 PHE   G CD2 1 
ATOM   3680  C CE1 . PHE   C  1 142 ? -6.98729  13.53123  8.25981   1.000 31.93227  ?  142 PHE   G CE1 1 
ATOM   3681  C CE2 . PHE   C  1 142 ? -8.18076  15.36292  7.32007   1.000 35.44984  ?  142 PHE   G CE2 1 
ATOM   3682  C CZ  . PHE   C  1 142 ? -7.74609  14.06558  7.24421   1.000 30.66649  ?  142 PHE   G CZ  1 
ATOM   3683  N N   . LYS   C  1 143 ? -6.72510  17.52894  13.61209  1.000 33.62606  ?  143 LYS   G N   1 
ATOM   3684  C CA  . LYS   C  1 143 ? -6.05685  18.20339  14.71341  1.000 29.29302  ?  143 LYS   G CA  1 
ATOM   3685  C C   . LYS   C  1 143 ? -5.83176  17.24340  15.86642  1.000 32.56866  ?  143 LYS   G C   1 
ATOM   3686  O O   . LYS   C  1 143 ? -4.70351  17.11300  16.36129  1.000 35.93023  ?  143 LYS   G O   1 
ATOM   3687  C CB  . LYS   C  1 143 ? -6.86994  19.40891  15.16949  1.000 32.84616  ?  143 LYS   G CB  1 
ATOM   3688  C CG  . LYS   C  1 143 ? -6.08940  20.33075  16.06240  1.000 19.41086  ?  143 LYS   G CG  1 
ATOM   3689  C CD  . LYS   C  1 143 ? -6.96788  20.95834  17.10464  1.000 27.57247  ?  143 LYS   G CD  1 
ATOM   3690  C CE  . LYS   C  1 143 ? -6.24758  22.11164  17.77632  1.000 34.13077  ?  143 LYS   G CE  1 
ATOM   3691  N NZ  . LYS   C  1 143 ? -5.05972  21.69074  18.56685  1.000 38.73993  ?  143 LYS   G NZ  1 
ATOM   3692  N N   . LYS   C  1 144 ? -6.88027  16.49199  16.22686  1.000 40.30930  ?  144 LYS   G N   1 
ATOM   3693  C CA  . LYS   C  1 144 ? -6.76700  15.59660  17.36844  1.000 26.25608  ?  144 LYS   G CA  1 
ATOM   3694  C C   . LYS   C  1 144 ? -5.80112  14.47510  17.06751  1.000 47.68731  ?  144 LYS   G C   1 
ATOM   3695  O O   . LYS   C  1 144 ? -4.95304  14.12205  17.90079  1.000 18.67272  ?  144 LYS   G O   1 
ATOM   3696  C CB  . LYS   C  1 144 ? -8.12478  15.03167  17.75744  1.000 21.02794  ?  144 LYS   G CB  1 
ATOM   3697  C CG  . LYS   C  1 144 ? -7.94263  13.97201  18.82496  1.000 18.46919  ?  144 LYS   G CG  1 
ATOM   3698  C CD  . LYS   C  1 144 ? -8.98052  14.06902  19.88617  1.000 109.30636 ?  144 LYS   G CD  1 
ATOM   3699  C CE  . LYS   C  1 144 ? -8.45399  13.40417  21.10949  1.000 102.20153 ?  144 LYS   G CE  1 
ATOM   3700  N NZ  . LYS   C  1 144 ? -7.31207  14.16586  21.59063  1.000 93.38167  ?  144 LYS   G NZ  1 
ATOM   3701  N N   . LEU   C  1 145 ? -5.86438  13.95200  15.84977  1.000 25.86124  ?  145 LEU   G N   1 
ATOM   3702  C CA  . LEU   C  1 145 ? -4.93896  12.88989  15.46445  1.000 20.28928  ?  145 LEU   G CA  1 
ATOM   3703  C C   . LEU   C  1 145 ? -3.49127  13.34986  15.62418  1.000 40.45054  ?  145 LEU   G C   1 
ATOM   3704  O O   . LEU   C  1 145 ? -2.69336  12.70692  16.31837  1.000 38.67743  ?  145 LEU   G O   1 
ATOM   3705  C CB  . LEU   C  1 145 ? -5.22066  12.43373  14.02840  1.000 31.12555  ?  145 LEU   G CB  1 
ATOM   3706  C CG  . LEU   C  1 145 ? -6.60271  11.80340  13.81353  1.000 33.77688  ?  145 LEU   G CG  1 
ATOM   3707  C CD1 . LEU   C  1 145 ? -6.78811  11.29564  12.38938  1.000 27.47798  ?  145 LEU   G CD1 1 
ATOM   3708  C CD2 . LEU   C  1 145 ? -6.81363  10.67831  14.79547  1.000 26.85781  ?  145 LEU   G CD2 1 
ATOM   3709  N N   . PHE   C  1 146 ? -3.15100  14.50064  15.03960  1.000 21.60707  ?  146 PHE   G N   1 
ATOM   3710  C CA  . PHE   C  1 146 ? -1.76163  14.94805  15.05751  1.000 25.56119  ?  146 PHE   G CA  1 
ATOM   3711  C C   . PHE   C  1 146 ? -1.32921  15.40271  16.44456  1.000 33.80046  ?  146 PHE   G C   1 
ATOM   3712  O O   . PHE   C  1 146 ? -0.16958  15.20278  16.82122  1.000 34.51018  ?  146 PHE   G O   1 
ATOM   3713  C CB  . PHE   C  1 146 ? -1.55870  16.06466  14.02921  1.000 25.78986  ?  146 PHE   G CB  1 
ATOM   3714  C CG  . PHE   C  1 146 ? -1.94073  15.67163  12.61550  1.000 29.36350  ?  146 PHE   G CG  1 
ATOM   3715  C CD1 . PHE   C  1 146 ? -1.94500  14.33348  12.21689  1.000 29.40692  ?  146 PHE   G CD1 1 
ATOM   3716  C CD2 . PHE   C  1 146 ? -2.28423  16.63797  11.68736  1.000 22.47197  ?  146 PHE   G CD2 1 
ATOM   3717  C CE1 . PHE   C  1 146 ? -2.28572  13.97756  10.92261  1.000 29.52219  ?  146 PHE   G CE1 1 
ATOM   3718  C CE2 . PHE   C  1 146 ? -2.63101  16.29118  10.38778  1.000 26.05503  ?  146 PHE   G CE2 1 
ATOM   3719  C CZ  . PHE   C  1 146 ? -2.62954  14.96053  10.00131  1.000 31.71321  ?  146 PHE   G CZ  1 
ATOM   3720  N N   . ASP   C  1 147 ? -2.22942  16.01043  17.22134  1.000 29.87392  ?  147 ASP   G N   1 
ATOM   3721  C CA  . ASP   C  1 147 ? -1.87198  16.32671  18.60148  1.000 23.50194  ?  147 ASP   G CA  1 
ATOM   3722  C C   . ASP   C  1 147 ? -1.54193  15.05414  19.37115  1.000 33.06666  ?  147 ASP   G C   1 
ATOM   3723  O O   . ASP   C  1 147 ? -0.56858  15.01350  20.14433  1.000 31.38050  ?  147 ASP   G O   1 
ATOM   3724  C CB  . ASP   C  1 147 ? -3.00079  17.08998  19.30242  1.000 15.94839  ?  147 ASP   G CB  1 
ATOM   3725  C CG  . ASP   C  1 147 ? -3.13824  18.53305  18.82491  1.000 49.02655  ?  147 ASP   G CG  1 
ATOM   3726  O OD1 . ASP   C  1 147 ? -2.18255  19.09185  18.22287  1.000 41.14254  ?  147 ASP   G OD1 1 
ATOM   3727  O OD2 . ASP   C  1 147 ? -4.21876  19.10955  19.07608  1.000 45.32302  -1 147 ASP   G OD2 1 
ATOM   3728  N N   . THR   C  1 148 ? -2.34851  14.00358  19.17056  1.000 27.26911  ?  148 THR   G N   1 
ATOM   3729  C CA  . THR   C  1 148 ? -2.08988  12.72492  19.82283  1.000 36.71790  ?  148 THR   G CA  1 
ATOM   3730  C C   . THR   C  1 148 ? -0.72165  12.19228  19.41752  1.000 33.62369  ?  148 THR   G C   1 
ATOM   3731  O O   . THR   C  1 148 ? 0.07902   11.78882  20.27232  1.000 39.63934  ?  148 THR   G O   1 
ATOM   3732  C CB  . THR   C  1 148 ? -3.20497  11.72821  19.47651  1.000 31.57914  ?  148 THR   G CB  1 
ATOM   3733  O OG1 . THR   C  1 148 ? -4.41021  12.11377  20.14523  1.000 32.44669  ?  148 THR   G OG1 1 
ATOM   3734  C CG2 . THR   C  1 148 ? -2.84118  10.31498  19.91113  1.000 20.88253  ?  148 THR   G CG2 1 
ATOM   3735  N N   . TRP   C  1 149 ? -0.42794  12.22182  18.10852  1.000 30.79232  ?  149 TRP   G N   1 
ATOM   3736  C CA  . TRP   C  1 149 ? 0.87419   11.78816  17.61178  1.000 23.89823  ?  149 TRP   G CA  1 
ATOM   3737  C C   . TRP   C  1 149 ? 1.99274   12.59666  18.25511  1.000 47.92453  ?  149 TRP   G C   1 
ATOM   3738  O O   . TRP   C  1 149 ? 3.01204   12.03695  18.67614  1.000 32.74377  ?  149 TRP   G O   1 
ATOM   3739  C CB  . TRP   C  1 149 ? 0.91262   11.91879  16.08297  1.000 21.46908  ?  149 TRP   G CB  1 
ATOM   3740  C CG  . TRP   C  1 149 ? 2.15433   11.33680  15.40721  1.000 32.49386  ?  149 TRP   G CG  1 
ATOM   3741  C CD1 . TRP   C  1 149 ? 3.09448   10.51875  15.97338  1.000 26.81593  ?  149 TRP   G CD1 1 
ATOM   3742  C CD2 . TRP   C  1 149 ? 2.57764   11.53984  14.04273  1.000 42.83250  ?  149 TRP   G CD2 1 
ATOM   3743  N NE1 . TRP   C  1 149 ? 4.06582   10.19765  15.05210  1.000 39.02785  ?  149 TRP   G NE1 1 
ATOM   3744  C CE2 . TRP   C  1 149 ? 3.77472   10.81203  13.86252  1.000 25.30636  ?  149 TRP   G CE2 1 
ATOM   3745  C CE3 . TRP   C  1 149 ? 2.06177   12.26892  12.95767  1.000 24.42382  ?  149 TRP   G CE3 1 
ATOM   3746  C CZ2 . TRP   C  1 149 ? 4.45925   10.77967  12.63965  1.000 34.75189  ?  149 TRP   G CZ2 1 
ATOM   3747  C CZ3 . TRP   C  1 149 ? 2.75446   12.24082  11.73152  1.000 27.28602  ?  149 TRP   G CZ3 1 
ATOM   3748  C CH2 . TRP   C  1 149 ? 3.93500   11.50058  11.58960  1.000 34.50338  ?  149 TRP   G CH2 1 
ATOM   3749  N N   . GLY   C  1 150 ? 1.80122   13.91672  18.36732  1.000 31.58690  ?  150 GLY   G N   1 
ATOM   3750  C CA  . GLY   C  1 150 ? 2.85284   14.77215  18.88437  1.000 20.94388  ?  150 GLY   G CA  1 
ATOM   3751  C C   . GLY   C  1 150 ? 3.20456   14.47339  20.32664  1.000 42.23638  ?  150 GLY   G C   1 
ATOM   3752  O O   . GLY   C  1 150 ? 4.34143   14.71105  20.75588  1.000 54.29008  ?  150 GLY   G O   1 
ATOM   3753  N N   . LEU   C  1 151 ? 2.23646   13.96345  21.09403  1.000 42.68682  ?  151 LEU   G N   1 
ATOM   3754  C CA  . LEU   C  1 151 ? 2.51861   13.46968  22.44078  1.000 37.40496  ?  151 LEU   G CA  1 
ATOM   3755  C C   . LEU   C  1 151 ? 3.61360   12.42240  22.42764  1.000 76.84550  ?  151 LEU   G C   1 
ATOM   3756  O O   . LEU   C  1 151 ? 4.58155   12.49580  23.19925  1.000 49.90337  ?  151 LEU   G O   1 
ATOM   3757  C CB  . LEU   C  1 151 ? 1.27801   12.84098  23.02832  1.000 49.60036  ?  151 LEU   G CB  1 
ATOM   3758  C CG  . LEU   C  1 151 ? 0.21596   13.81491  23.42742  1.000 70.69703  ?  151 LEU   G CG  1 
ATOM   3759  C CD1 . LEU   C  1 151 ? -0.80395  12.94851  24.07737  1.000 35.87047  ?  151 LEU   G CD1 1 
ATOM   3760  C CD2 . LEU   C  1 151 ? 0.86490   14.77058  24.38372  1.000 24.39338  ?  151 LEU   G CD2 1 
ATOM   3761  N N   . PHE   C  1 152 ? 3.42384   11.38947  21.60457  1.000 23.70432  ?  152 PHE   G N   1 
ATOM   3762  C CA  . PHE   C  1 152 ? 4.44445   10.36846  21.45820  1.000 36.45472  ?  152 PHE   G CA  1 
ATOM   3763  C C   . PHE   C  1 152 ? 5.77534   10.96871  21.01776  1.000 49.68797  ?  152 PHE   G C   1 
ATOM   3764  O O   . PHE   C  1 152 ? 6.83589   10.53946  21.48260  1.000 42.14307  ?  152 PHE   G O   1 
ATOM   3765  C CB  . PHE   C  1 152 ? 3.98395   9.31162   20.46307  1.000 18.71809  ?  152 PHE   G CB  1 
ATOM   3766  C CG  . PHE   C  1 152 ? 5.04200   8.33505   20.13594  1.000 44.97571  ?  152 PHE   G CG  1 
ATOM   3767  C CD1 . PHE   C  1 152 ? 5.38826   7.35968   21.04642  1.000 27.92645  ?  152 PHE   G CD1 1 
ATOM   3768  C CD2 . PHE   C  1 152 ? 5.74038   8.42598   18.94477  1.000 35.79361  ?  152 PHE   G CD2 1 
ATOM   3769  C CE1 . PHE   C  1 152 ? 6.39384   6.47027   20.76356  1.000 34.92073  ?  152 PHE   G CE1 1 
ATOM   3770  C CE2 . PHE   C  1 152 ? 6.74376   7.53596   18.65033  1.000 45.37216  ?  152 PHE   G CE2 1 
ATOM   3771  C CZ  . PHE   C  1 152 ? 7.07217   6.55374   19.55802  1.000 37.12107  ?  152 PHE   G CZ  1 
ATOM   3772  N N   . LEU   C  1 153 ? 5.74659   11.96510  20.12857  1.000 30.15029  ?  153 LEU   G N   1 
ATOM   3773  C CA  . LEU   C  1 153 ? 6.99120   12.51762  19.60503  1.000 32.05727  ?  153 LEU   G CA  1 
ATOM   3774  C C   . LEU   C  1 153 ? 7.70415   13.42694  20.60156  1.000 31.64262  ?  153 LEU   G C   1 
ATOM   3775  O O   . LEU   C  1 153 ? 8.80978   13.89692  20.31246  1.000 36.03779  ?  153 LEU   G O   1 
ATOM   3776  C CB  . LEU   C  1 153 ? 6.71599   13.26639  18.30912  1.000 24.77767  ?  153 LEU   G CB  1 
ATOM   3777  C CG  . LEU   C  1 153 ? 6.10368   12.43721  17.18768  1.000 37.84560  ?  153 LEU   G CG  1 
ATOM   3778  C CD1 . LEU   C  1 153 ? 5.75835   13.35207  16.02344  1.000 20.02368  ?  153 LEU   G CD1 1 
ATOM   3779  C CD2 . LEU   C  1 153 ? 7.04571   11.31770  16.74892  1.000 20.03993  ?  153 LEU   G CD2 1 
ATOM   3780  N N   . SER   C  1 154 ? 7.09282   13.68221  21.75629  1.000 41.94512  ?  154 SER   G N   1 
ATOM   3781  C CA  . SER   C  1 154 ? 7.70326   14.40585  22.86010  1.000 39.69616  ?  154 SER   G CA  1 
ATOM   3782  C C   . SER   C  1 154 ? 8.22478   13.47079  23.94327  1.000 49.77822  ?  154 SER   G C   1 
ATOM   3783  O O   . SER   C  1 154 ? 8.81297   13.94244  24.92104  1.000 54.01958  ?  154 SER   G O   1 
ATOM   3784  C CB  . SER   C  1 154 ? 6.68429   15.37588  23.46846  1.000 26.89291  ?  154 SER   G CB  1 
ATOM   3785  O OG  . SER   C  1 154 ? 6.34988   16.36835  22.52245  1.000 107.52699 ?  154 SER   G OG  1 
ATOM   3786  N N   . SER   C  1 155 ? 8.02071   12.16429  23.78946  1.000 28.65003  ?  155 SER   G N   1 
ATOM   3787  C CA  . SER   C  1 155 ? 8.28570   11.15999  24.80775  1.000 29.27390  ?  155 SER   G CA  1 
ATOM   3788  C C   . SER   C  1 155 ? 9.63313   10.49457  24.56115  1.000 93.87834  ?  155 SER   G C   1 
ATOM   3789  O O   . SER   C  1 155 ? 10.11101  10.42257  23.42072  1.000 27.36348  ?  155 SER   G O   1 
ATOM   3790  C CB  . SER   C  1 155 ? 7.18485   10.09898  24.80781  1.000 26.02654  ?  155 SER   G CB  1 
ATOM   3791  O OG  . SER   C  1 155 ? 7.25362   9.27091   23.65548  1.000 36.07601  ?  155 SER   G OG  1 
ATOM   3792  N N   . LYS   C  1 156 ? 10.23319  9.98223   25.65020  1.000 36.05274  ?  156 LYS   G N   1 
ATOM   3793  C CA  . LYS   C  1 156 ? 11.55604  9.36825   25.54166  1.000 52.87097  ?  156 LYS   G CA  1 
ATOM   3794  C C   . LYS   C  1 156 ? 11.55833  8.25446   24.49653  1.000 26.29189  ?  156 LYS   G C   1 
ATOM   3795  O O   . LYS   C  1 156 ? 12.56818  8.04347   23.81133  1.000 42.13611  ?  156 LYS   G O   1 
ATOM   3796  C CB  . LYS   C  1 156 ? 12.02264  8.84954   26.91159  1.000 19.00723  ?  156 LYS   G CB  1 
ATOM   3797  N N   . ASP   C  1 157 ? 10.40958  7.59043   24.30205  1.000 42.05294  ?  157 ASP   G N   1 
ATOM   3798  C CA  . ASP   C  1 157 ? 10.32173  6.45433   23.38197  1.000 41.02532  ?  157 ASP   G CA  1 
ATOM   3799  C C   . ASP   C  1 157 ? 10.51240  6.84972   21.92445  1.000 43.54440  ?  157 ASP   G C   1 
ATOM   3800  O O   . ASP   C  1 157 ? 10.88498  5.99732   21.10770  1.000 39.43027  ?  157 ASP   G O   1 
ATOM   3801  C CB  . ASP   C  1 157 ? 8.97585   5.74434   23.53945  1.000 52.37683  ?  157 ASP   G CB  1 
ATOM   3802  C CG  . ASP   C  1 157 ? 8.84027   5.03039   24.87912  1.000 53.41488  ?  157 ASP   G CG  1 
ATOM   3803  O OD1 . ASP   C  1 157 ? 9.75853   4.26825   25.24989  1.000 64.01602  ?  157 ASP   G OD1 1 
ATOM   3804  O OD2 . ASP   C  1 157 ? 7.81146   5.23958   25.56152  1.000 82.71904  -1 157 ASP   G OD2 1 
ATOM   3805  N N   . SER   C  1 158 ? 10.25434  8.11141   21.57409  1.000 57.15205  ?  158 SER   G N   1 
ATOM   3806  C CA  . SER   C  1 158 ? 10.46116  8.53970   20.19779  1.000 42.58112  ?  158 SER   G CA  1 
ATOM   3807  C C   . SER   C  1 158 ? 11.93685  8.73704   19.85824  1.000 45.42604  ?  158 SER   G C   1 
ATOM   3808  O O   . SER   C  1 158 ? 12.23667  9.05416   18.70139  1.000 40.48493  ?  158 SER   G O   1 
ATOM   3809  C CB  . SER   C  1 158 ? 9.67960   9.83023   19.92233  1.000 36.03864  ?  158 SER   G CB  1 
ATOM   3810  O OG  . SER   C  1 158 ? 10.24057  10.92978  20.62467  1.000 35.49715  ?  158 SER   G OG  1 
ATOM   3811  N N   . ARG   C  1 159 ? 12.86135  8.55217   20.81334  1.000 30.07035  ?  159 ARG   G N   1 
ATOM   3812  C CA  . ARG   C  1 159 ? 14.28674  8.68465   20.50751  1.000 37.28655  ?  159 ARG   G CA  1 
ATOM   3813  C C   . ARG   C  1 159 ? 14.81441  7.56266   19.61944  1.000 38.04304  ?  159 ARG   G C   1 
ATOM   3814  O O   . ARG   C  1 159 ? 15.89093  7.71147   19.03661  1.000 32.46088  ?  159 ARG   G O   1 
ATOM   3815  C CB  . ARG   C  1 159 ? 15.11369  8.72052   21.79020  1.000 19.91906  ?  159 ARG   G CB  1 
ATOM   3816  C CG  . ARG   C  1 159 ? 14.97993  10.01197  22.56292  1.000 55.88885  ?  159 ARG   G CG  1 
ATOM   3817  C CD  . ARG   C  1 159 ? 15.61460  9.84973   23.91469  1.000 39.97210  ?  159 ARG   G CD  1 
ATOM   3818  N NE  . ARG   C  1 159 ? 15.08420  8.66639   24.57369  1.000 53.83469  ?  159 ARG   G NE  1 
ATOM   3819  C CZ  . ARG   C  1 159 ? 15.64039  8.07838   25.62217  1.000 45.00209  ?  159 ARG   G CZ  1 
ATOM   3820  N NH1 . ARG   C  1 159 ? 16.76516  8.53235   26.15501  1.000 37.47392  ?  159 ARG   G NH1 1 
ATOM   3821  N NH2 . ARG   C  1 159 ? 15.05504  7.00671   26.14571  1.000 34.69449  ?  159 ARG   G NH2 1 
ATOM   3822  N N   . ASN   C  1 160 ? 14.08155  6.45612   19.48205  1.000 33.67775  ?  160 ASN   G N   1 
ATOM   3823  C CA  . ASN   C  1 160 ? 14.61922  5.28797   18.78918  1.000 38.02320  ?  160 ASN   G CA  1 
ATOM   3824  C C   . ASN   C  1 160 ? 14.97057  5.54479   17.32521  1.000 30.45084  ?  160 ASN   G C   1 
ATOM   3825  O O   . ASN   C  1 160 ? 15.68712  4.73607   16.72919  1.000 60.22265  ?  160 ASN   G O   1 
ATOM   3826  C CB  . ASN   C  1 160 ? 13.62910  4.13271   18.88610  1.000 36.07273  ?  160 ASN   G CB  1 
ATOM   3827  C CG  . ASN   C  1 160 ? 12.43944  4.32700   17.99689  1.000 48.24723  ?  160 ASN   G CG  1 
ATOM   3828  O OD1 . ASN   C  1 160 ? 11.62264  5.22708   18.21936  1.000 61.70319  ?  160 ASN   G OD1 1 
ATOM   3829  N ND2 . ASN   C  1 160 ? 12.33186  3.49473   16.97022  1.000 52.44065  ?  160 ASN   G ND2 1 
ATOM   3830  N N   . VAL   C  1 161 ? 14.47794  6.62712   16.71794  1.000 42.90143  ?  161 VAL   G N   1 
ATOM   3831  C CA  . VAL   C  1 161 ? 14.92509  6.97564   15.36769  1.000 45.70643  ?  161 VAL   G CA  1 
ATOM   3832  C C   . VAL   C  1 161 ? 16.17816  7.83409   15.38453  1.000 48.40645  ?  161 VAL   G C   1 
ATOM   3833  O O   . VAL   C  1 161 ? 16.74206  8.11737   14.31398  1.000 31.11041  ?  161 VAL   G O   1 
ATOM   3834  C CB  . VAL   C  1 161 ? 13.84262  7.72819   14.56653  1.000 39.65283  ?  161 VAL   G CB  1 
ATOM   3835  C CG1 . VAL   C  1 161 ? 12.61159  6.84352   14.33185  1.000 28.51804  ?  161 VAL   G CG1 1 
ATOM   3836  C CG2 . VAL   C  1 161 ? 13.47983  9.01349   15.28015  1.000 23.41020  ?  161 VAL   G CG2 1 
ATOM   3837  N N   . LEU   C  1 162 ? 16.61767  8.27631   16.56087  1.000 31.56107  ?  162 LEU   G N   1 
ATOM   3838  C CA  . LEU   C  1 162 ? 17.80560  9.11369   16.69260  1.000 42.00691  ?  162 LEU   G CA  1 
ATOM   3839  C C   . LEU   C  1 162 ? 19.03869  8.21388   16.80453  1.000 60.93733  ?  162 LEU   G C   1 
ATOM   3840  O O   . LEU   C  1 162 ? 19.69417  8.09316   17.84496  1.000 43.53361  ?  162 LEU   G O   1 
ATOM   3841  C CB  . LEU   C  1 162 ? 17.65974  10.03717  17.89174  1.000 38.66374  ?  162 LEU   G CB  1 
ATOM   3842  C CG  . LEU   C  1 162 ? 16.44742  10.95447  17.80679  1.000 27.30319  ?  162 LEU   G CG  1 
ATOM   3843  C CD1 . LEU   C  1 162 ? 16.47104  11.96977  18.93593  1.000 22.99689  ?  162 LEU   G CD1 1 
ATOM   3844  C CD2 . LEU   C  1 162 ? 16.45063  11.64520  16.44128  1.000 21.83988  ?  162 LEU   G CD2 1 
ATOM   3845  N N   . VAL   C  1 163 ? 19.33611  7.56175   15.68263  1.000 32.41464  ?  163 VAL   G N   1 
ATOM   3846  C CA  . VAL   C  1 163 ? 20.35099  6.51841   15.58248  1.000 29.45973  ?  163 VAL   G CA  1 
ATOM   3847  C C   . VAL   C  1 163 ? 20.96073  6.59750   14.18767  1.000 49.88516  ?  163 VAL   G C   1 
ATOM   3848  O O   . VAL   C  1 163 ? 20.44549  7.28005   13.29763  1.000 42.46785  ?  163 VAL   G O   1 
ATOM   3849  C CB  . VAL   C  1 163 ? 19.76835  5.10165   15.82027  1.000 31.42033  ?  163 VAL   G CB  1 
ATOM   3850  C CG1 . VAL   C  1 163 ? 19.15259  4.97181   17.23072  1.000 25.00455  ?  163 VAL   G CG1 1 
ATOM   3851  C CG2 . VAL   C  1 163 ? 18.73934  4.75714   14.73883  1.000 24.53351  ?  163 VAL   G CG2 1 
ATOM   3852  N N   . ALA   C  1 164 ? 22.06096  5.87363   13.98011  1.000 41.93714  ?  164 ALA   G N   1 
ATOM   3853  C CA  . ALA   C  1 164 ? 22.66178  5.83477   12.65080  1.000 49.54313  ?  164 ALA   G CA  1 
ATOM   3854  C C   . ALA   C  1 164 ? 22.18235  4.65873   11.81326  1.000 40.54343  ?  164 ALA   G C   1 
ATOM   3855  O O   . ALA   C  1 164 ? 22.39245  4.66661   10.59353  1.000 38.45817  ?  164 ALA   G O   1 
ATOM   3856  C CB  . ALA   C  1 164 ? 24.18366  5.79334   12.75386  1.000 20.39965  ?  164 ALA   G CB  1 
ATOM   3857  N N   . ASP   C  1 165 ? 21.53416  3.66978   12.44540  1.000 42.07336  ?  165 ASP   G N   1 
ATOM   3858  C CA  . ASP   C  1 165 ? 21.04563  2.46400   11.78268  1.000 40.40781  ?  165 ASP   G CA  1 
ATOM   3859  C C   . ASP   C  1 165 ? 20.38364  2.78456   10.44742  1.000 40.26829  ?  165 ASP   G C   1 
ATOM   3860  O O   . ASP   C  1 165 ? 19.57234  3.70517   10.33848  1.000 75.29032  ?  165 ASP   G O   1 
ATOM   3861  C CB  . ASP   C  1 165 ? 20.03899  1.72955   12.68677  1.000 47.68381  ?  165 ASP   G CB  1 
ATOM   3862  C CG  . ASP   C  1 165 ? 20.52901  1.55850   14.12117  1.000 35.63678  ?  165 ASP   G CG  1 
ATOM   3863  O OD1 . ASP   C  1 165 ? 21.68123  1.93647   14.43086  1.000 81.88774  ?  165 ASP   G OD1 1 
ATOM   3864  O OD2 . ASP   C  1 165 ? 19.74105  1.03695   14.94300  1.000 84.58584  -1 165 ASP   G OD2 1 
ATOM   3865  N N   . GLN   C  1 166 ? 20.75329  2.02860   9.42605   1.000 70.51955  ?  166 GLN   G N   1 
ATOM   3866  C CA  . GLN   C  1 166 ? 20.00362  2.00725   8.18211   1.000 84.98789  ?  166 GLN   G CA  1 
ATOM   3867  C C   . GLN   C  1 166 ? 18.82936  1.05636   8.38487   1.000 47.24702  ?  166 GLN   G C   1 
ATOM   3868  O O   . GLN   C  1 166 ? 19.00865  -0.04134  8.91792   1.000 120.84855 ?  166 GLN   G O   1 
ATOM   3869  C CB  . GLN   C  1 166 ? 20.90696  1.57348   7.02138   1.000 44.57346  ?  166 GLN   G CB  1 
ATOM   3870  C CG  . GLN   C  1 166 ? 20.23819  1.47297   5.67437   1.000 81.08943  ?  166 GLN   G CG  1 
ATOM   3871  C CD  . GLN   C  1 166 ? 20.37355  2.75189   4.88863   1.000 140.50877 ?  166 GLN   G CD  1 
ATOM   3872  O OE1 . GLN   C  1 166 ? 19.55798  3.04341   4.00628   1.000 95.27386  ?  166 GLN   G OE1 1 
ATOM   3873  N NE2 . GLN   C  1 166 ? 21.40424  3.52885   5.20040   1.000 81.67749  ?  166 GLN   G NE2 1 
ATOM   3874  N N   . PHE   C  1 167 ? 17.62499  1.49845   8.01723   1.000 92.52007  ?  167 PHE   G N   1 
ATOM   3875  C CA  . PHE   C  1 167 ? 16.39757  0.75788   8.30963   1.000 91.47799  ?  167 PHE   G CA  1 
ATOM   3876  C C   . PHE   C  1 167 ? 15.91487  -0.10527  7.15214   1.000 92.98182  ?  167 PHE   G C   1 
ATOM   3877  O O   . PHE   C  1 167 ? 15.24575  -1.11614  7.38512   1.000 88.96136  ?  167 PHE   G O   1 
ATOM   3878  C CB  . PHE   C  1 167 ? 15.26214  1.72116   8.68149   1.000 81.57962  ?  167 PHE   G CB  1 
ATOM   3879  C CG  . PHE   C  1 167 ? 15.47319  2.45491   9.97480   1.000 87.07568  ?  167 PHE   G CG  1 
ATOM   3880  C CD1 . PHE   C  1 167 ? 15.31391  3.82689   10.05473  1.000 75.28998  ?  167 PHE   G CD1 1 
ATOM   3881  C CD2 . PHE   C  1 167 ? 15.80539  1.77481   11.11238  1.000 66.39795  ?  167 PHE   G CD2 1 
ATOM   3882  C CE1 . PHE   C  1 167 ? 15.50171  4.49678   11.25483  1.000 146.01339 ?  167 PHE   G CE1 1 
ATOM   3883  C CE2 . PHE   C  1 167 ? 15.99319  2.43767   12.31116  1.000 134.83445 ?  167 PHE   G CE2 1 
ATOM   3884  C CZ  . PHE   C  1 167 ? 15.84835  3.78591   12.38688  1.000 54.11561  ?  167 PHE   G CZ  1 
ATOM   3885  N N   . ASP   C  1 168 ? 16.19475  0.29918   5.91962   1.000 112.85539 ?  168 ASP   G N   1 
ATOM   3886  C CA  . ASP   C  1 168 ? 15.87761  -0.45876  4.71759   1.000 78.12897  ?  168 ASP   G CA  1 
ATOM   3887  C C   . ASP   C  1 168 ? 16.65508  0.17598   3.57094   1.000 129.43951 ?  168 ASP   G C   1 
ATOM   3888  O O   . ASP   C  1 168 ? 17.61032  0.95671   3.82195   1.000 102.96403 ?  168 ASP   G O   1 
ATOM   3889  C CB  . ASP   C  1 168 ? 14.34699  -0.53769  4.50308   1.000 92.20854  ?  168 ASP   G CB  1 
ATOM   3890  C CG  . ASP   C  1 168 ? 13.71021  0.80152   4.08661   1.000 116.99586 ?  168 ASP   G CG  1 
ATOM   3891  O OD1 . ASP   C  1 168 ? 12.52951  1.05187   4.44542   1.000 102.82695 ?  168 ASP   G OD1 1 
ATOM   3892  O OD2 . ASP   C  1 168 ? 14.36875  1.59190   3.37411   1.000 114.75153 -1 168 ASP   G OD2 1 
ATOM   3893  N N   . ASP   C  1 169 ? 16.31048  -0.13093  2.32550   1.000 105.04228 ?  169 ASP   G N   1 
ATOM   3894  C CA  . ASP   C  1 169 ? 17.11327  0.36567   1.21149   1.000 108.93404 ?  169 ASP   G CA  1 
ATOM   3895  C C   . ASP   C  1 169 ? 17.02674  1.88892   1.09537   1.000 125.78189 ?  169 ASP   G C   1 
ATOM   3896  O O   . ASP   C  1 169 ? 18.00433  2.53793   0.70358   1.000 113.61069 ?  169 ASP   G O   1 
ATOM   3897  C CB  . ASP   C  1 169 ? 16.69143  -0.31411  -0.09840  1.000 87.51701  ?  169 ASP   G CB  1 
ATOM   3898  N N   . ARG   C  1 170 ? 15.89253  2.48609   1.48053   1.000 151.92576 ?  170 ARG   G N   1 
ATOM   3899  C CA  . ARG   C  1 170 ? 15.65523  3.90627   1.24545   1.000 62.82587  ?  170 ARG   G CA  1 
ATOM   3900  C C   . ARG   C  1 170 ? 15.61743  4.77278   2.51006   1.000 81.10960  ?  170 ARG   G C   1 
ATOM   3901  O O   . ARG   C  1 170 ? 15.68141  6.00163   2.38877   1.000 72.12618  ?  170 ARG   G O   1 
ATOM   3902  C CB  . ARG   C  1 170 ? 14.34572  4.08651   0.45913   1.000 68.67889  ?  170 ARG   G CB  1 
ATOM   3903  N N   . HIS   C  1 171 ? 15.54443  4.18387   3.71315   1.000 66.98607  ?  171 HIS   G N   1 
ATOM   3904  C CA  . HIS   C  1 171 ? 15.34965  4.92943   4.95662   1.000 70.21638  ?  171 HIS   G CA  1 
ATOM   3905  C C   . HIS   C  1 171 ? 16.47307  4.65637   5.94855   1.000 36.76879  ?  171 HIS   G C   1 
ATOM   3906  O O   . HIS   C  1 171 ? 17.00667  3.54758   6.01813   1.000 108.04750 ?  171 HIS   G O   1 
ATOM   3907  C CB  . HIS   C  1 171 ? 14.01280  4.57146   5.64386   1.000 72.98564  ?  171 HIS   G CB  1 
ATOM   3908  C CG  . HIS   C  1 171 ? 12.81587  4.69464   4.75354   1.000 68.16924  ?  171 HIS   G CG  1 
ATOM   3909  N ND1 . HIS   C  1 171 ? 12.78922  5.51650   3.64684   1.000 73.83253  ?  171 HIS   G ND1 1 
ATOM   3910  C CD2 . HIS   C  1 171 ? 11.60786  4.08549   4.79776   1.000 68.39669  ?  171 HIS   G CD2 1 
ATOM   3911  C CE1 . HIS   C  1 171 ? 11.61599  5.41319   3.05049   1.000 48.58667  ?  171 HIS   G CE1 1 
ATOM   3912  N NE2 . HIS   C  1 171 ? 10.87948  4.55293   3.73018   1.000 123.84985 ?  171 HIS   G NE2 1 
ATOM   3913  N N   . CYS   C  1 172 ? 16.79604  5.67174   6.74989   1.000 71.65171  ?  172 CYS   G N   1 
ATOM   3914  C CA  . CYS   C  1 172 ? 17.80483  5.53908   7.79213   1.000 40.97775  ?  172 CYS   G CA  1 
ATOM   3915  C C   . CYS   C  1 172 ? 17.44958  6.42811   8.97603   1.000 42.03632  ?  172 CYS   G C   1 
ATOM   3916  O O   . CYS   C  1 172 ? 16.55531  7.27456   8.90071   1.000 64.96589  ?  172 CYS   G O   1 
ATOM   3917  C CB  . CYS   C  1 172 ? 19.19129  5.91170   7.27787   1.000 50.09326  ?  172 CYS   G CB  1 
ATOM   3918  S SG  . CYS   C  1 172 ? 19.29621  7.62322   6.76287   1.000 58.06745  ?  172 CYS   G SG  1 
ATOM   3919  N N   . GLY   C  1 173 ? 18.18648  6.23466   10.07083  1.000 57.00396  ?  173 GLY   G N   1 
ATOM   3920  C CA  . GLY   C  1 173 ? 18.02739  7.06044   11.25005  1.000 41.65610  ?  173 GLY   G CA  1 
ATOM   3921  C C   . GLY   C  1 173 ? 18.61159  8.45161   11.05995  1.000 56.22420  ?  173 GLY   G C   1 
ATOM   3922  O O   . GLY   C  1 173 ? 19.36172  8.72922   10.12076  1.000 56.27984  ?  173 GLY   G O   1 
ATOM   3923  N N   . TRP   C  1 174 ? 18.26024  9.34555   11.99626  1.000 29.69155  ?  174 TRP   G N   1 
ATOM   3924  C CA  . TRP   C  1 174 ? 18.59732  10.75884  11.86709  1.000 55.26924  ?  174 TRP   G CA  1 
ATOM   3925  C C   . TRP   C  1 174 ? 20.04953  11.05384  12.22042  1.000 63.85206  ?  174 TRP   G C   1 
ATOM   3926  O O   . TRP   C  1 174 ? 20.54598  12.12688  11.87012  1.000 48.03330  ?  174 TRP   G O   1 
ATOM   3927  C CB  . TRP   C  1 174 ? 17.65069  11.60457  12.73188  1.000 33.02360  ?  174 TRP   G CB  1 
ATOM   3928  C CG  . TRP   C  1 174 ? 16.26410  11.60904  12.17693  1.000 63.07373  ?  174 TRP   G CG  1 
ATOM   3929  C CD1 . TRP   C  1 174 ? 15.20562  10.86350  12.61030  1.000 41.02493  ?  174 TRP   G CD1 1 
ATOM   3930  C CD2 . TRP   C  1 174 ? 15.79154  12.36643  11.05311  1.000 49.73751  ?  174 TRP   G CD2 1 
ATOM   3931  N NE1 . TRP   C  1 174 ? 14.10119  11.11687  11.83467  1.000 43.50563  ?  174 TRP   G NE1 1 
ATOM   3932  C CE2 . TRP   C  1 174 ? 14.43045  12.03671  10.87293  1.000 35.56501  ?  174 TRP   G CE2 1 
ATOM   3933  C CE3 . TRP   C  1 174 ? 16.38307  13.30252  10.19299  1.000 37.78282  ?  174 TRP   G CE3 1 
ATOM   3934  C CZ2 . TRP   C  1 174 ? 13.64528  12.60830  9.86253   1.000 27.97638  ?  174 TRP   G CZ2 1 
ATOM   3935  C CZ3 . TRP   C  1 174 ? 15.60997  13.85976  9.18563   1.000 39.81813  ?  174 TRP   G CZ3 1 
ATOM   3936  C CH2 . TRP   C  1 174 ? 14.24958  13.51067  9.03137   1.000 30.97070  ?  174 TRP   G CH2 1 
ATOM   3937  N N   . LEU   C  1 175 ? 20.74426  10.12830  12.88151  1.000 41.56028  ?  175 LEU   G N   1 
ATOM   3938  C CA  . LEU   C  1 175 ? 22.16147  10.27639  13.19036  1.000 36.51384  ?  175 LEU   G CA  1 
ATOM   3939  C C   . LEU   C  1 175 ? 23.06405  9.53394   12.20561  1.000 46.21081  ?  175 LEU   G C   1 
ATOM   3940  O O   . LEU   C  1 175 ? 24.28892  9.57681   12.35033  1.000 55.06003  ?  175 LEU   G O   1 
ATOM   3941  C CB  . LEU   C  1 175 ? 22.42667  9.80691   14.62027  1.000 31.51067  ?  175 LEU   G CB  1 
ATOM   3942  C CG  . LEU   C  1 175 ? 21.57924  10.58312  15.63316  1.000 42.12216  ?  175 LEU   G CG  1 
ATOM   3943  C CD1 . LEU   C  1 175 ? 21.92778  10.24573  17.08595  1.000 32.66819  ?  175 LEU   G CD1 1 
ATOM   3944  C CD2 . LEU   C  1 175 ? 21.72349  12.07598  15.36936  1.000 29.61329  ?  175 LEU   G CD2 1 
ATOM   3945  N N   . ASN   C  1 176 ? 22.47976  8.84641   11.22379  1.000 34.59322  ?  176 ASN   G N   1 
ATOM   3946  C CA  . ASN   C  1 176 ? 23.21529  8.31314   10.08334  1.000 30.18296  ?  176 ASN   G CA  1 
ATOM   3947  C C   . ASN   C  1 176 ? 23.89444  9.44822   9.32024   1.000 46.59194  ?  176 ASN   G C   1 
ATOM   3948  O O   . ASN   C  1 176 ? 23.36593  10.56196  9.24259   1.000 60.47686  ?  176 ASN   G O   1 
ATOM   3949  C CB  . ASN   C  1 176 ? 22.22742  7.57540   9.18927   1.000 57.10570  ?  176 ASN   G CB  1 
ATOM   3950  C CG  . ASN   C  1 176 ? 22.88448  6.82236   8.08199   1.000 55.41687  ?  176 ASN   G CG  1 
ATOM   3951  O OD1 . ASN   C  1 176 ? 23.17415  7.37707   7.01421   1.000 41.60357  ?  176 ASN   G OD1 1 
ATOM   3952  N ND2 . ASN   C  1 176 ? 23.07006  5.52518   8.29681   1.000 42.94491  ?  176 ASN   G ND2 1 
ATOM   3953  N N   . GLU   C  1 177 ? 25.07970  9.17650   8.76019   1.000 47.00587  ?  177 GLU   G N   1 
ATOM   3954  C CA  . GLU   C  1 177 ? 25.84049  10.27331  8.16592   1.000 44.30469  ?  177 GLU   G CA  1 
ATOM   3955  C C   . GLU   C  1 177 ? 25.15988  10.81450  6.91543   1.000 38.07510  ?  177 GLU   G C   1 
ATOM   3956  O O   . GLU   C  1 177 ? 25.31745  11.99389  6.58938   1.000 47.32234  ?  177 GLU   G O   1 
ATOM   3957  C CB  . GLU   C  1 177 ? 27.27682  9.84565   7.85178   1.000 26.05687  ?  177 GLU   G CB  1 
ATOM   3958  N N   . ARG   C  1 178 ? 24.39022  9.98677   6.20746   1.000 41.37555  ?  178 ARG   G N   1 
ATOM   3959  C CA  . ARG   C  1 178 ? 23.61775  10.49356  5.07349   1.000 64.93813  ?  178 ARG   G CA  1 
ATOM   3960  C C   . ARG   C  1 178 ? 22.70210  11.63652  5.51137   1.000 61.11414  ?  178 ARG   G C   1 
ATOM   3961  O O   . ARG   C  1 178 ? 22.62524  12.68129  4.85034   1.000 59.57386  ?  178 ARG   G O   1 
ATOM   3962  C CB  . ARG   C  1 178 ? 22.80836  9.34849   4.44422   1.000 30.12204  ?  178 ARG   G CB  1 
ATOM   3963  C CG  . ARG   C  1 178 ? 21.75554  9.89551   3.51357   1.000 67.02203  ?  178 ARG   G CG  1 
ATOM   3964  C CD  . ARG   C  1 178 ? 21.24422  8.91920   2.46568   1.000 48.83929  ?  178 ARG   G CD  1 
ATOM   3965  N NE  . ARG   C  1 178 ? 20.69210  7.67494   3.00896   1.000 96.42263  ?  178 ARG   G NE  1 
ATOM   3966  C CZ  . ARG   C  1 178 ? 19.47223  7.19167   2.76703   1.000 116.47126 ?  178 ARG   G CZ  1 
ATOM   3967  N NH1 . ARG   C  1 178 ? 18.58502  7.85922   2.04977   1.000 72.08182  ?  178 ARG   G NH1 1 
ATOM   3968  N NH2 . ARG   C  1 178 ? 19.14444  5.98585   3.24490   1.000 103.44659 ?  178 ARG   G NH2 1 
ATOM   3969  N N   . ALA   C  1 179 ? 22.02547  11.46207  6.65285   1.000 51.33705  ?  179 ALA   G N   1 
ATOM   3970  C CA  . ALA   C  1 179 ? 21.08593  12.45952  7.14550   1.000 50.00281  ?  179 ALA   G CA  1 
ATOM   3971  C C   . ALA   C  1 179 ? 21.81961  13.61872  7.80933   1.000 38.81721  ?  179 ALA   G C   1 
ATOM   3972  O O   . ALA   C  1 179 ? 21.47452  14.79078  7.60327   1.000 46.46255  ?  179 ALA   G O   1 
ATOM   3973  C CB  . ALA   C  1 179 ? 20.11168  11.80306  8.12553   1.000 25.84207  ?  179 ALA   G CB  1 
ATOM   3974  N N   . LEU   C  1 180 ? 22.81958  13.29493  8.63654   1.000 40.06679  ?  180 LEU   G N   1 
ATOM   3975  C CA  . LEU   C  1 180 ? 23.68970  14.30864  9.22864   1.000 27.02211  ?  180 LEU   G CA  1 
ATOM   3976  C C   . LEU   C  1 180 ? 24.27250  15.23256  8.16030   1.000 43.40037  ?  180 LEU   G C   1 
ATOM   3977  O O   . LEU   C  1 180 ? 24.33005  16.45700  8.34268   1.000 43.52047  ?  180 LEU   G O   1 
ATOM   3978  C CB  . LEU   C  1 180 ? 24.80206  13.61500  10.01444  1.000 22.35664  ?  180 LEU   G CB  1 
ATOM   3979  C CG  . LEU   C  1 180 ? 24.76463  13.66981  11.53669  1.000 47.17349  ?  180 LEU   G CG  1 
ATOM   3980  C CD1 . LEU   C  1 180 ? 23.38980  13.43648  12.05942  1.000 44.80465  ?  180 LEU   G CD1 1 
ATOM   3981  C CD2 . LEU   C  1 180 ? 25.70503  12.64594  12.11926  1.000 34.84833  ?  180 LEU   G CD2 1 
ATOM   3982  N N   . SER   C  1 181 ? 24.69713  14.66248  7.02927   1.000 45.01832  ?  181 SER   G N   1 
ATOM   3983  C CA  . SER   C  1 181 ? 25.23482  15.47766  5.94598   1.000 48.92971  ?  181 SER   G CA  1 
ATOM   3984  C C   . SER   C  1 181 ? 24.16464  16.40057  5.36403   1.000 36.62845  ?  181 SER   G C   1 
ATOM   3985  O O   . SER   C  1 181 ? 24.40272  17.60259  5.18119   1.000 47.94152  ?  181 SER   G O   1 
ATOM   3986  C CB  . SER   C  1 181 ? 25.83435  14.56968  4.86798   1.000 31.30944  ?  181 SER   G CB  1 
ATOM   3987  O OG  . SER   C  1 181 ? 26.01748  15.26592  3.64361   1.000 99.53012  ?  181 SER   G OG  1 
ATOM   3988  N N   . ALA   C  1 182 ? 22.97482  15.85353  5.07077   1.000 51.45070  ?  182 ALA   G N   1 
ATOM   3989  C CA  . ALA   C  1 182 ? 21.90627  16.65225  4.47109   1.000 73.11954  ?  182 ALA   G CA  1 
ATOM   3990  C C   . ALA   C  1 182 ? 21.55427  17.85457  5.33837   1.000 52.62877  ?  182 ALA   G C   1 
ATOM   3991  O O   . ALA   C  1 182 ? 21.36243  18.96433  4.82355   1.000 40.45539  ?  182 ALA   G O   1 
ATOM   3992  C CB  . ALA   C  1 182 ? 20.67020  15.78109  4.22794   1.000 31.64439  ?  182 ALA   G CB  1 
ATOM   3993  N N   . MET   C  1 183 ? 21.50802  17.65878  6.66162   1.000 24.62504  ?  183 MET   G N   1 
ATOM   3994  C CA  . MET   C  1 183 ? 21.09073  18.69679  7.59522   1.000 40.75183  ?  183 MET   G CA  1 
ATOM   3995  C C   . MET   C  1 183 ? 22.09310  19.83652  7.77301   1.000 26.09208  ?  183 MET   G C   1 
ATOM   3996  O O   . MET   C  1 183 ? 21.71231  20.87715  8.32430   1.000 44.68690  ?  183 MET   G O   1 
ATOM   3997  C CB  . MET   C  1 183 ? 20.77822  18.06043  8.94300   1.000 25.41166  ?  183 MET   G CB  1 
ATOM   3998  C CG  . MET   C  1 183 ? 19.38629  17.45202  8.96111   1.000 27.51311  ?  183 MET   G CG  1 
ATOM   3999  S SD  . MET   C  1 183 ? 18.91905  16.77242  10.54952  1.000 36.72351  ?  183 MET   G SD  1 
ATOM   4000  C CE  . MET   C  1 183 ? 19.76224  15.20119  10.61913  1.000 32.97721  ?  183 MET   G CE  1 
ATOM   4001  N N   . VAL   C  1 184 ? 23.34289  19.69516  7.32990   1.000 35.03015  ?  184 VAL   G N   1 
ATOM   4002  C CA  . VAL   C  1 184 ? 24.29126  20.79904  7.41882   1.000 41.88834  ?  184 VAL   G CA  1 
ATOM   4003  C C   . VAL   C  1 184 ? 24.73955  21.27937  6.04991   1.000 23.43202  ?  184 VAL   G C   1 
ATOM   4004  O O   . VAL   C  1 184 ? 25.71088  22.02381  5.95057   1.000 34.35544  ?  184 VAL   G O   1 
ATOM   4005  C CB  . VAL   C  1 184 ? 25.50834  20.44612  8.29368   1.000 21.30087  ?  184 VAL   G CB  1 
ATOM   4006  C CG1 . VAL   C  1 184 ? 25.05834  20.17696  9.72164   1.000 26.81249  ?  184 VAL   G CG1 1 
ATOM   4007  C CG2 . VAL   C  1 184 ? 26.26569  19.26404  7.71070   1.000 22.41105  ?  184 VAL   G CG2 1 
ATOM   4008  N N   . LYS   C  1 185 ? 24.02346  20.88449  4.99855   1.000 44.05320  ?  185 LYS   G N   1 
ATOM   4009  C CA  . LYS   C  1 185 ? 24.33026  21.31402  3.63841   1.000 46.92879  ?  185 LYS   G CA  1 
ATOM   4010  C C   . LYS   C  1 185 ? 24.63332  22.81345  3.53822   1.000 22.65018  ?  185 LYS   G C   1 
ATOM   4011  O O   . LYS   C  1 185 ? 25.58625  23.22087  2.85966   1.000 81.07834  ?  185 LYS   G O   1 
ATOM   4012  C CB  . LYS   C  1 185 ? 23.15562  20.91907  2.74582   1.000 35.54819  ?  185 LYS   G CB  1 
ATOM   4013  C CG  . LYS   C  1 185 ? 23.21218  21.44177  1.34861   1.000 41.75233  ?  185 LYS   G CG  1 
ATOM   4014  C CD  . LYS   C  1 185 ? 22.15138  20.75106  0.50727   1.000 67.18903  ?  185 LYS   G CD  1 
ATOM   4015  C CE  . LYS   C  1 185 ? 22.46319  20.92853  -0.95935  1.000 67.83348  ?  185 LYS   G CE  1 
ATOM   4016  N NZ  . LYS   C  1 185 ? 21.27840  21.41287  -1.70586  1.000 81.55854  ?  185 LYS   G NZ  1 
ATOM   4017  N N   . HIS   C  1 186 ? 23.85028  23.65111  4.22096   1.000 45.39021  ?  186 HIS   G N   1 
ATOM   4018  C CA  . HIS   C  1 186 ? 23.97817  25.09922  4.09650   1.000 27.47942  ?  186 HIS   G CA  1 
ATOM   4019  C C   . HIS   C  1 186 ? 24.76217  25.73106  5.23992   1.000 46.71788  ?  186 HIS   G C   1 
ATOM   4020  O O   . HIS   C  1 186 ? 24.64470  26.93892  5.47734   1.000 32.87140  ?  186 HIS   G O   1 
ATOM   4021  C CB  . HIS   C  1 186 ? 22.60060  25.74856  3.98121   1.000 35.92554  ?  186 HIS   G CB  1 
ATOM   4022  C CG  . HIS   C  1 186 ? 21.81461  25.26115  2.81256   1.000 61.96912  ?  186 HIS   G CG  1 
ATOM   4023  N ND1 . HIS   C  1 186 ? 22.21377  25.46772  1.50871   1.000 48.94709  ?  186 HIS   G ND1 1 
ATOM   4024  C CD2 . HIS   C  1 186 ? 20.65321  24.57150  2.74888   1.000 21.60752  ?  186 HIS   G CD2 1 
ATOM   4025  C CE1 . HIS   C  1 186 ? 21.32473  24.92886  0.69177   1.000 36.72635  ?  186 HIS   G CE1 1 
ATOM   4026  N NE2 . HIS   C  1 186 ? 20.36792  24.37968  1.41837   1.000 52.78189  ?  186 HIS   G NE2 1 
ATOM   4027  N N   . TYR   C  1 187 ? 25.56798  24.95300  5.95026   1.000 32.33151  ?  187 TYR   G N   1 
ATOM   4028  C CA  . TYR   C  1 187 ? 26.32691  25.50455  7.06154   1.000 40.29090  ?  187 TYR   G CA  1 
ATOM   4029  C C   . TYR   C  1 187 ? 27.81262  25.55623  6.75819   1.000 76.17833  ?  187 TYR   G C   1 
ATOM   4030  O O   . TYR   C  1 187 ? 28.63142  25.68836  7.67543   1.000 33.72975  ?  187 TYR   G O   1 
ATOM   4031  C CB  . TYR   C  1 187 ? 26.03107  24.73247  8.34376   1.000 44.80172  ?  187 TYR   G CB  1 
ATOM   4032  C CG  . TYR   C  1 187 ? 24.63148  25.03723  8.80008   1.000 28.80903  ?  187 TYR   G CG  1 
ATOM   4033  C CD1 . TYR   C  1 187 ? 24.36710  26.13884  9.60747   1.000 37.23364  ?  187 TYR   G CD1 1 
ATOM   4034  C CD2 . TYR   C  1 187 ? 23.56013  24.26954  8.35926   1.000 43.53555  ?  187 TYR   G CD2 1 
ATOM   4035  C CE1 . TYR   C  1 187 ? 23.07433  26.44488  10.01252  1.000 33.14655  ?  187 TYR   G CE1 1 
ATOM   4036  C CE2 . TYR   C  1 187 ? 22.26882  24.55950  8.74449   1.000 15.69247  ?  187 TYR   G CE2 1 
ATOM   4037  C CZ  . TYR   C  1 187 ? 22.03277  25.64727  9.57867   1.000 43.07219  ?  187 TYR   G CZ  1 
ATOM   4038  O OH  . TYR   C  1 187 ? 20.74994  25.92065  9.96641   1.000 36.46448  ?  187 TYR   G OH  1 
ATOM   4039  N N   . ASN   C  1 188 ? 28.16988  25.47098  5.47834   1.000 32.92651  ?  188 ASN   G N   1 
ATOM   4040  C CA  . ASN   C  1 188 ? 29.47163  25.91455  5.02082   1.000 82.63540  ?  188 ASN   G CA  1 
ATOM   4041  C C   . ASN   C  1 188 ? 30.58743  25.05706  5.62338   1.000 31.89531  ?  188 ASN   G C   1 
ATOM   4042  O O   . ASN   C  1 188 ? 31.53249  25.55841  6.23048   1.000 65.37865  ?  188 ASN   G O   1 
ATOM   4043  C CB  . ASN   C  1 188 ? 29.63449  27.39502  5.36371   1.000 43.37680  ?  188 ASN   G CB  1 
ATOM   4044  C CG  . ASN   C  1 188 ? 30.84265  28.01148  4.73110   1.000 82.68351  ?  188 ASN   G CG  1 
ATOM   4045  O OD1 . ASN   C  1 188 ? 31.93508  27.98004  5.28801   1.000 110.53297 ?  188 ASN   G OD1 1 
ATOM   4046  N ND2 . ASN   C  1 188 ? 30.65549  28.58760  3.56290   1.000 95.52409  ?  188 ASN   G ND2 1 
ATOM   4047  N N   . GLY   C  1 189 ? 30.44701  23.73838  5.49707   1.000 51.20712  ?  189 GLY   G N   1 
ATOM   4048  C CA  . GLY   C  1 189 ? 31.46585  22.82445  5.96897   1.000 18.12390  ?  189 GLY   G CA  1 
ATOM   4049  C C   . GLY   C  1 189 ? 31.43772  22.47320  7.44782   1.000 22.28916  ?  189 GLY   G C   1 
ATOM   4050  O O   . GLY   C  1 189 ? 32.03434  21.45839  7.83376   1.000 55.18543  ?  189 GLY   G O   1 
ATOM   4051  N N   . ARG   C  1 190 ? 30.77664  23.26727  8.29607   1.000 42.85873  ?  190 ARG   G N   1 
ATOM   4052  C CA  . ARG   C  1 190 ? 30.61666  22.88117  9.69551   1.000 31.02027  ?  190 ARG   G CA  1 
ATOM   4053  C C   . ARG   C  1 190 ? 29.73791  21.62880  9.83390   1.000 38.13561  ?  190 ARG   G C   1 
ATOM   4054  O O   . ARG   C  1 190 ? 28.83745  21.35960  9.02531   1.000 48.82219  ?  190 ARG   G O   1 
ATOM   4055  C CB  . ARG   C  1 190 ? 30.02436  24.02989  10.50967  1.000 38.23008  ?  190 ARG   G CB  1 
ATOM   4056  C CG  . ARG   C  1 190 ? 30.73039  25.35919  10.33902  1.000 32.88625  ?  190 ARG   G CG  1 
ATOM   4057  C CD  . ARG   C  1 190 ? 31.45911  25.76950  11.61517  1.000 23.39225  ?  190 ARG   G CD  1 
ATOM   4058  N NE  . ARG   C  1 190 ? 30.56289  26.11016  12.71639  1.000 38.04887  ?  190 ARG   G NE  1 
ATOM   4059  C CZ  . ARG   C  1 190 ? 30.90129  26.03635  13.99619  1.000 55.02914  ?  190 ARG   G CZ  1 
ATOM   4060  N NH1 . ARG   C  1 190 ? 32.09114  25.59698  14.37002  1.000 51.28581  ?  190 ARG   G NH1 1 
ATOM   4061  N NH2 . ARG   C  1 190 ? 30.02236  26.40150  14.92476  1.000 40.68340  ?  190 ARG   G NH2 1 
ATOM   4062  N N   . ALA   C  1 191 ? 30.01316  20.86133  10.87836  1.000 39.93474  ?  191 ALA   G N   1 
ATOM   4063  C CA  . ALA   C  1 191 ? 29.36842  19.57763  11.10137  1.000 27.73003  ?  191 ALA   G CA  1 
ATOM   4064  C C   . ALA   C  1 191 ? 28.17258  19.73079  12.03558  1.000 90.76729  ?  191 ALA   G C   1 
ATOM   4065  O O   . ALA   C  1 191 ? 28.04170  20.72527  12.75882  1.000 28.98528  ?  191 ALA   G O   1 
ATOM   4066  C CB  . ALA   C  1 191 ? 30.35806  18.57729  11.70171  1.000 40.04659  ?  191 ALA   G CB  1 
ATOM   4067  N N   . PHE   C  1 192 ? 27.32211  18.69704  12.04386  1.000 27.47617  ?  192 PHE   G N   1 
ATOM   4068  C CA  . PHE   C  1 192 ? 26.05250  18.75875  12.76560  1.000 31.34890  ?  192 PHE   G CA  1 
ATOM   4069  C C   . PHE   C  1 192 ? 26.23926  19.15884  14.22938  1.000 55.19514  ?  192 PHE   G C   1 
ATOM   4070  O O   . PHE   C  1 192 ? 25.53584  20.04413  14.73780  1.000 44.78489  ?  192 PHE   G O   1 
ATOM   4071  C CB  . PHE   C  1 192 ? 25.33277  17.41263  12.64704  1.000 32.88722  ?  192 PHE   G CB  1 
ATOM   4072  C CG  . PHE   C  1 192 ? 23.96175  17.39608  13.26617  1.000 40.34743  ?  192 PHE   G CG  1 
ATOM   4073  C CD1 . PHE   C  1 192 ? 23.80224  17.23856  14.63789  1.000 49.49375  ?  192 PHE   G CD1 1 
ATOM   4074  C CD2 . PHE   C  1 192 ? 22.82939  17.53090  12.47632  1.000 48.44275  ?  192 PHE   G CD2 1 
ATOM   4075  C CE1 . PHE   C  1 192 ? 22.54539  17.22403  15.21585  1.000 30.08648  ?  192 PHE   G CE1 1 
ATOM   4076  C CE2 . PHE   C  1 192 ? 21.56156  17.51480  13.04776  1.000 54.54462  ?  192 PHE   G CE2 1 
ATOM   4077  C CZ  . PHE   C  1 192 ? 21.42406  17.35600  14.42102  1.000 37.98870  ?  192 PHE   G CZ  1 
ATOM   4078  N N   . ASP   C  1 193 ? 27.17837  18.51235  14.92540  1.000 49.76168  ?  193 ASP   G N   1 
ATOM   4079  C CA  . ASP   C  1 193 ? 27.38676  18.76628  16.35012  1.000 29.85884  ?  193 ASP   G CA  1 
ATOM   4080  C C   . ASP   C  1 193 ? 28.11131  20.08556  16.62767  1.000 56.35225  ?  193 ASP   G C   1 
ATOM   4081  O O   . ASP   C  1 193 ? 28.09351  20.56460  17.76919  1.000 17.23894  ?  193 ASP   G O   1 
ATOM   4082  C CB  . ASP   C  1 193 ? 28.14974  17.59404  16.97347  1.000 42.74932  ?  193 ASP   G CB  1 
ATOM   4083  C CG  . ASP   C  1 193 ? 29.51625  17.39767  16.34931  1.000 85.63060  ?  193 ASP   G CG  1 
ATOM   4084  O OD1 . ASP   C  1 193 ? 29.58437  17.00258  15.16580  1.000 46.34718  ?  193 ASP   G OD1 1 
ATOM   4085  O OD2 . ASP   C  1 193 ? 30.52092  17.67827  17.03755  1.000 44.84517  -1 193 ASP   G OD2 1 
ATOM   4086  N N   . GLU   C  1 194 ? 28.74643  20.68635  15.62176  1.000 26.87594  ?  194 GLU   G N   1 
ATOM   4087  C CA  . GLU   C  1 194 ? 29.21308  22.06372  15.75166  1.000 53.84712  ?  194 GLU   G CA  1 
ATOM   4088  C C   . GLU   C  1 194 ? 28.05392  23.04606  15.63100  1.000 58.22408  ?  194 GLU   G C   1 
ATOM   4089  O O   . GLU   C  1 194 ? 27.91741  23.95869  16.45645  1.000 46.71772  ?  194 GLU   G O   1 
ATOM   4090  C CB  . GLU   C  1 194 ? 30.26031  22.36977  14.68365  1.000 45.60992  ?  194 GLU   G CB  1 
ATOM   4091  C CG  . GLU   C  1 194 ? 31.48658  21.46025  14.70935  1.000 31.38668  ?  194 GLU   G CG  1 
ATOM   4092  C CD  . GLU   C  1 194 ? 32.46451  21.78901  13.58493  1.000 88.96076  ?  194 GLU   G CD  1 
ATOM   4093  O OE1 . GLU   C  1 194 ? 32.14851  21.45736  12.42159  1.000 63.57167  ?  194 GLU   G OE1 1 
ATOM   4094  O OE2 . GLU   C  1 194 ? 33.52958  22.39780  13.85376  1.000 61.12418  -1 194 GLU   G OE2 1 
ATOM   4095  N N   . VAL   C  1 195 ? 27.20331  22.84784  14.61074  1.000 53.18610  ?  195 VAL   G N   1 
ATOM   4096  C CA  . VAL   C  1 195 ? 26.11665  23.77772  14.29889  1.000 20.98603  ?  195 VAL   G CA  1 
ATOM   4097  C C   . VAL   C  1 195 ? 25.02968  23.74027  15.37398  1.000 82.41203  ?  195 VAL   G C   1 
ATOM   4098  O O   . VAL   C  1 195 ? 24.60096  24.78068  15.88836  1.000 34.20153  ?  195 VAL   G O   1 
ATOM   4099  C CB  . VAL   C  1 195 ? 25.53278  23.45456  12.91428  1.000 56.22134  ?  195 VAL   G CB  1 
ATOM   4100  C CG1 . VAL   C  1 195 ? 24.32835  24.34228  12.62598  1.000 25.89250  ?  195 VAL   G CG1 1 
ATOM   4101  C CG2 . VAL   C  1 195 ? 26.60121  23.59396  11.83495  1.000 30.88942  ?  195 VAL   G CG2 1 
ATOM   4102  N N   . PHE   C  1 196 ? 24.54759  22.55289  15.71240  1.000 23.52223  ?  196 PHE   G N   1 
ATOM   4103  C CA  . PHE   C  1 196 ? 23.42825  22.42488  16.62744  1.000 55.44249  ?  196 PHE   G CA  1 
ATOM   4104  C C   . PHE   C  1 196 ? 23.91532  21.97462  17.99946  1.000 35.93706  ?  196 PHE   G C   1 
ATOM   4105  O O   . PHE   C  1 196 ? 24.92300  21.27643  18.12017  1.000 38.19796  ?  196 PHE   G O   1 
ATOM   4106  C CB  . PHE   C  1 196 ? 22.39529  21.44085  16.07104  1.000 28.18438  ?  196 PHE   G CB  1 
ATOM   4107  C CG  . PHE   C  1 196 ? 21.91723  21.79430  14.70195  1.000 45.64047  ?  196 PHE   G CG  1 
ATOM   4108  C CD1 . PHE   C  1 196 ? 21.16832  22.94301  14.49226  1.000 29.34503  ?  196 PHE   G CD1 1 
ATOM   4109  C CD2 . PHE   C  1 196 ? 22.23285  20.99676  13.61624  1.000 22.75837  ?  196 PHE   G CD2 1 
ATOM   4110  C CE1 . PHE   C  1 196 ? 20.73561  23.28465  13.21146  1.000 33.36071  ?  196 PHE   G CE1 1 
ATOM   4111  C CE2 . PHE   C  1 196 ? 21.79602  21.32647  12.33276  1.000 40.94339  ?  196 PHE   G CE2 1 
ATOM   4112  C CZ  . PHE   C  1 196 ? 21.04393  22.46931  12.12997  1.000 32.33177  ?  196 PHE   G CZ  1 
ATOM   4113  N N   . LEU   C  1 197 ? 23.18503  22.38854  19.03352  1.000 38.43892  ?  197 LEU   G N   1 
ATOM   4114  C CA  . LEU   C  1 197 ? 23.50944  22.07102  20.42321  1.000 41.26538  ?  197 LEU   G CA  1 
ATOM   4115  C C   . LEU   C  1 197 ? 23.11420  20.62960  20.71335  1.000 59.85922  ?  197 LEU   G C   1 
ATOM   4116  O O   . LEU   C  1 197 ? 21.92683  20.31146  20.82599  1.000 35.25823  ?  197 LEU   G O   1 
ATOM   4117  C CB  . LEU   C  1 197 ? 22.77252  23.02490  21.35504  1.000 38.79839  ?  197 LEU   G CB  1 
ATOM   4118  C CG  . LEU   C  1 197 ? 23.15112  23.20285  22.81835  1.000 35.49447  ?  197 LEU   G CG  1 
ATOM   4119  C CD1 . LEU   C  1 197 ? 22.33507  24.36554  23.29025  1.000 43.73935  ?  197 LEU   G CD1 1 
ATOM   4120  C CD2 . LEU   C  1 197 ? 22.81270  22.00191  23.66615  1.000 82.69513  ?  197 LEU   G CD2 1 
ATOM   4121  N N   . CYS   C  1 198 ? 24.10021  19.76003  20.86784  1.000 40.35279  ?  198 CYS   G N   1 
ATOM   4122  C CA  . CYS   C  1 198 ? 23.83223  18.37152  21.17947  1.000 39.52682  ?  198 CYS   G CA  1 
ATOM   4123  C C   . CYS   C  1 198 ? 25.06805  17.81020  21.86433  1.000 43.15761  ?  198 CYS   G C   1 
ATOM   4124  O O   . CYS   C  1 198 ? 25.98462  18.55226  22.23359  1.000 50.25450  ?  198 CYS   G O   1 
ATOM   4125  C CB  . CYS   C  1 198 ? 23.47657  17.59889  19.90540  1.000 32.98098  ?  198 CYS   G CB  1 
ATOM   4126  S SG  . CYS   C  1 198 ? 24.75600  17.77034  18.60595  1.000 41.71720  ?  198 CYS   G SG  1 
ATOM   4127  N N   . ASP   C  1 199 ? 25.09611  16.48829  22.01275  1.000 39.24314  ?  199 ASP   G N   1 
ATOM   4128  C CA  . ASP   C  1 199 ? 26.23971  15.75946  22.55263  1.000 27.71735  ?  199 ASP   G CA  1 
ATOM   4129  C C   . ASP   C  1 199 ? 26.53665  14.59520  21.61017  1.000 62.33358  ?  199 ASP   G C   1 
ATOM   4130  O O   . ASP   C  1 199 ? 25.82931  13.58072  21.63789  1.000 27.47276  ?  199 ASP   G O   1 
ATOM   4131  C CB  . ASP   C  1 199 ? 25.93502  15.27199  23.96988  1.000 29.52218  ?  199 ASP   G CB  1 
ATOM   4132  C CG  . ASP   C  1 199 ? 27.09536  14.51579  24.60850  1.000 130.87096 ?  199 ASP   G CG  1 
ATOM   4133  O OD1 . ASP   C  1 199 ? 28.10927  14.21439  23.92194  1.000 32.35834  ?  199 ASP   G OD1 1 
ATOM   4134  O OD2 . ASP   C  1 199 ? 26.96725  14.23269  25.82276  1.000 40.05837  -1 199 ASP   G OD2 1 
ATOM   4135  N N   . LYS   C  1 200 ? 27.58161  14.72795  20.77751  1.000 36.31337  ?  200 LYS   G N   1 
ATOM   4136  C CA  . LYS   C  1 200 ? 27.85165  13.69281  19.77764  1.000 61.77415  ?  200 LYS   G CA  1 
ATOM   4137  C C   . LYS   C  1 200 ? 28.28357  12.37269  20.40066  1.000 58.51844  ?  200 LYS   G C   1 
ATOM   4138  O O   . LYS   C  1 200 ? 28.26650  11.35267  19.70719  1.000 50.23521  ?  200 LYS   G O   1 
ATOM   4139  C CB  . LYS   C  1 200 ? 28.91408  14.15637  18.77125  1.000 36.12868  ?  200 LYS   G CB  1 
ATOM   4140  C CG  . LYS   C  1 200 ? 30.33744  14.14402  19.29302  1.000 58.91821  ?  200 LYS   G CG  1 
ATOM   4141  C CD  . LYS   C  1 200 ? 31.33466  14.66960  18.25461  1.000 79.42815  ?  200 LYS   G CD  1 
ATOM   4142  C CE  . LYS   C  1 200 ? 31.48071  13.74333  17.04339  1.000 62.70652  ?  200 LYS   G CE  1 
ATOM   4143  N NZ  . LYS   C  1 200 ? 32.72533  14.05716  16.26076  1.000 57.28630  ?  200 LYS   G NZ  1 
ATOM   4144  N N   . ASN   C  1 201 ? 28.64069  12.36231  21.68426  1.000 48.56040  ?  201 ASN   G N   1 
ATOM   4145  C CA  . ASN   C  1 201 ? 29.06842  11.15760  22.37875  1.000 71.72210  ?  201 ASN   G CA  1 
ATOM   4146  C C   . ASN   C  1 201 ? 27.96058  10.51781  23.18998  1.000 47.46706  ?  201 ASN   G C   1 
ATOM   4147  O O   . ASN   C  1 201 ? 28.15195  9.42287   23.72540  1.000 79.50771  ?  201 ASN   G O   1 
ATOM   4148  C CB  . ASN   C  1 201 ? 30.24674  11.48463  23.28710  1.000 45.71997  ?  201 ASN   G CB  1 
ATOM   4149  C CG  . ASN   C  1 201 ? 31.40068  12.04319  22.51627  1.000 83.18372  ?  201 ASN   G CG  1 
ATOM   4150  O OD1 . ASN   C  1 201 ? 31.73440  11.54277  21.42858  1.000 36.41630  ?  201 ASN   G OD1 1 
ATOM   4151  N ND2 . ASN   C  1 201 ? 31.99559  13.11148  23.03518  1.000 51.29822  ?  201 ASN   G ND2 1 
ATOM   4152  N N   . ALA   C  1 202 ? 26.87597  11.13482  23.28849  1.000 93.57560  ?  202 ALA   G N   1 
ATOM   4153  C CA  . ALA   C  1 202 ? 25.77809  10.57946  24.05245  1.000 46.07126  ?  202 ALA   G CA  1 
ATOM   4154  C C   . ALA   C  1 202 ? 24.88471  9.73506   23.15288  1.000 39.30214  ?  202 ALA   G C   1 
ATOM   4155  O O   . ALA   C  1 202 ? 24.87762  9.90965   21.92690  1.000 51.05628  ?  202 ALA   G O   1 
ATOM   4156  C CB  . ALA   C  1 202 ? 24.96393  11.69420  24.69238  1.000 23.43960  ?  202 ALA   G CB  1 
ATOM   4157  N N   . PRO   C  1 203 ? 24.16178  8.77660   23.72441  1.000 74.82172  ?  203 PRO   G N   1 
ATOM   4158  C CA  . PRO   C  1 203 ? 23.12320  8.09491   22.94405  1.000 69.64197  ?  203 PRO   G CA  1 
ATOM   4159  C C   . PRO   C  1 203 ? 22.04446  9.08867   22.53975  1.000 59.46700  ?  203 PRO   G C   1 
ATOM   4160  O O   . PRO   C  1 203 ? 21.66312  9.97802   23.31555  1.000 39.72382  ?  203 PRO   G O   1 
ATOM   4161  C CB  . PRO   C  1 203 ? 22.58747  7.01772   23.89908  1.000 46.92486  ?  203 PRO   G CB  1 
ATOM   4162  C CG  . PRO   C  1 203 ? 23.02830  7.44437   25.27726  1.000 37.63337  ?  203 PRO   G CG  1 
ATOM   4163  C CD  . PRO   C  1 203 ? 24.29124  8.24730   25.09383  1.000 25.76669  ?  203 PRO   G CD  1 
ATOM   4164  N N   . TYR   C  1 204 ? 21.58357  8.94864   21.29270  1.000 36.58470  ?  204 TYR   G N   1 
ATOM   4165  C CA  . TYR   C  1 204 ? 20.59880  9.84083   20.68919  1.000 47.65433  ?  204 TYR   G CA  1 
ATOM   4166  C C   . TYR   C  1 204 ? 21.10770  11.26458  20.58007  1.000 41.36319  ?  204 TYR   G C   1 
ATOM   4167  O O   . TYR   C  1 204 ? 20.31294  12.20673  20.61060  1.000 45.71651  ?  204 TYR   G O   1 
ATOM   4168  C CB  . TYR   C  1 204 ? 19.28162  9.82316   21.47429  1.000 35.06064  ?  204 TYR   G CB  1 
ATOM   4169  C CG  . TYR   C  1 204 ? 18.87741  8.42771   21.87859  1.000 39.33621  ?  204 TYR   G CG  1 
ATOM   4170  C CD1 . TYR   C  1 204 ? 18.67760  7.44195   20.90853  1.000 34.09764  ?  204 TYR   G CD1 1 
ATOM   4171  C CD2 . TYR   C  1 204 ? 18.70476  8.08610   23.22165  1.000 30.28509  ?  204 TYR   G CD2 1 
ATOM   4172  C CE1 . TYR   C  1 204 ? 18.31828  6.14860   21.25601  1.000 16.81302  ?  204 TYR   G CE1 1 
ATOM   4173  C CE2 . TYR   C  1 204 ? 18.33969  6.79666   23.58481  1.000 27.32796  ?  204 TYR   G CE2 1 
ATOM   4174  C CZ  . TYR   C  1 204 ? 18.15805  5.83237   22.59299  1.000 40.54121  ?  204 TYR   G CZ  1 
ATOM   4175  O OH  . TYR   C  1 204 ? 17.79251  4.54852   22.91923  1.000 42.55114  ?  204 TYR   G OH  1 
ATOM   4176  N N   . TYR   C  1 205 ? 22.42548  11.43978  20.49982  1.000 29.79365  ?  205 TYR   G N   1 
ATOM   4177  C CA  . TYR   C  1 205 ? 23.05510  12.75648  20.48610  1.000 27.75365  ?  205 TYR   G CA  1 
ATOM   4178  C C   . TYR   C  1 205 ? 22.57304  13.64856  21.63733  1.000 35.17669  ?  205 TYR   G C   1 
ATOM   4179  O O   . TYR   C  1 205 ? 22.65661  14.88334  21.56028  1.000 33.16018  ?  205 TYR   G O   1 
ATOM   4180  C CB  . TYR   C  1 205 ? 22.83203  13.45874  19.14750  1.000 34.87211  ?  205 TYR   G CB  1 
ATOM   4181  C CG  . TYR   C  1 205 ? 23.95966  13.32590  18.16299  1.000 48.57886  ?  205 TYR   G CG  1 
ATOM   4182  C CD1 . TYR   C  1 205 ? 24.73526  12.17849  18.09826  1.000 40.82988  ?  205 TYR   G CD1 1 
ATOM   4183  C CD2 . TYR   C  1 205 ? 24.25914  14.36899  17.29464  1.000 36.08244  ?  205 TYR   G CD2 1 
ATOM   4184  C CE1 . TYR   C  1 205 ? 25.78447  12.07353  17.16527  1.000 25.70753  ?  205 TYR   G CE1 1 
ATOM   4185  C CE2 . TYR   C  1 205 ? 25.29282  14.27434  16.37227  1.000 49.70794  ?  205 TYR   G CE2 1 
ATOM   4186  C CZ  . TYR   C  1 205 ? 26.05014  13.12887  16.31164  1.000 69.60177  ?  205 TYR   G CZ  1 
ATOM   4187  O OH  . TYR   C  1 205 ? 27.06339  13.06220  15.39177  1.000 40.18955  ?  205 TYR   G OH  1 
ATOM   4188  N N   . GLY   C  1 206 ? 22.05956  13.05480  22.71118  1.000 25.24515  ?  206 GLY   G N   1 
ATOM   4189  C CA  . GLY   C  1 206 ? 21.63389  13.81828  23.85999  1.000 24.13256  ?  206 GLY   G CA  1 
ATOM   4190  C C   . GLY   C  1 206 ? 20.21232  14.33577  23.81024  1.000 37.92149  ?  206 GLY   G C   1 
ATOM   4191  O O   . GLY   C  1 206 ? 19.73042  14.86192  24.81988  1.000 29.93757  ?  206 GLY   G O   1 
ATOM   4192  N N   . PHE   C  1 207 ? 19.52320  14.21049  22.68050  1.000 26.63874  ?  207 PHE   G N   1 
ATOM   4193  C CA  . PHE   C  1 207 ? 18.13782  14.65369  22.60820  1.000 38.69803  ?  207 PHE   G CA  1 
ATOM   4194  C C   . PHE   C  1 207 ? 17.24290  13.70012  23.39095  1.000 34.16205  ?  207 PHE   G C   1 
ATOM   4195  O O   . PHE   C  1 207 ? 17.45441  12.48458  23.38016  1.000 44.20375  ?  207 PHE   G O   1 
ATOM   4196  C CB  . PHE   C  1 207 ? 17.68793  14.72875  21.15123  1.000 26.03376  ?  207 PHE   G CB  1 
ATOM   4197  C CG  . PHE   C  1 207 ? 18.48567  15.68624  20.31355  1.000 41.68183  ?  207 PHE   G CG  1 
ATOM   4198  C CD1 . PHE   C  1 207 ? 18.29755  17.05558  20.44038  1.000 15.45949  ?  207 PHE   G CD1 1 
ATOM   4199  C CD2 . PHE   C  1 207 ? 19.40791  15.22035  19.37925  1.000 19.83588  ?  207 PHE   G CD2 1 
ATOM   4200  C CE1 . PHE   C  1 207 ? 19.01975  17.94433  19.65637  1.000 35.76616  ?  207 PHE   G CE1 1 
ATOM   4201  C CE2 . PHE   C  1 207 ? 20.13572  16.10717  18.58507  1.000 23.49147  ?  207 PHE   G CE2 1 
ATOM   4202  C CZ  . PHE   C  1 207 ? 19.94047  17.46807  18.72680  1.000 40.44838  ?  207 PHE   G CZ  1 
ATOM   4203  N N   . ASN   C  1 208 ? 16.23763  14.24901  24.07941  1.000 39.05087  ?  208 ASN   G N   1 
ATOM   4204  C CA  . ASN   C  1 208 ? 15.36960  13.42789  24.92036  1.000 61.56424  ?  208 ASN   G CA  1 
ATOM   4205  C C   . ASN   C  1 208 ? 14.07966  12.98289  24.24084  1.000 31.18872  ?  208 ASN   G C   1 
ATOM   4206  O O   . ASN   C  1 208 ? 13.25859  12.31533  24.88618  1.000 89.36313  ?  208 ASN   G O   1 
ATOM   4207  C CB  . ASN   C  1 208 ? 15.03186  14.14844  26.23454  1.000 31.63874  ?  208 ASN   G CB  1 
ATOM   4208  C CG  . ASN   C  1 208 ? 14.70176  15.59627  26.04734  1.000 88.10793  ?  208 ASN   G CG  1 
ATOM   4209  O OD1 . ASN   C  1 208 ? 13.72603  15.95090  25.37202  1.000 143.15710 ?  208 ASN   G OD1 1 
ATOM   4210  N ND2 . ASN   C  1 208 ? 15.49529  16.45624  26.67844  1.000 65.08347  ?  208 ASN   G ND2 1 
ATOM   4211  N N   . SER   C  1 209 ? 13.89395  13.30336  22.96199  1.000 50.21310  ?  209 SER   G N   1 
ATOM   4212  C CA  . SER   C  1 209 ? 12.71749  12.90463  22.19274  1.000 33.67714  ?  209 SER   G CA  1 
ATOM   4213  C C   . SER   C  1 209 ? 12.94862  13.33350  20.76006  1.000 55.82451  ?  209 SER   G C   1 
ATOM   4214  O O   . SER   C  1 209 ? 13.88326  14.08408  20.46170  1.000 31.05743  ?  209 SER   G O   1 
ATOM   4215  C CB  . SER   C  1 209 ? 11.42230  13.54834  22.68876  1.000 44.66970  ?  209 SER   G CB  1 
ATOM   4216  O OG  . SER   C  1 209 ? 11.44292  14.93618  22.39847  1.000 23.99359  ?  209 SER   G OG  1 
ATOM   4217  N N   . TYR   C  1 210 ? 12.05542  12.88078  19.87834  1.000 33.94504  ?  210 TYR   G N   1 
ATOM   4218  C CA  . TYR   C  1 210 ? 12.16493  13.29779  18.48830  1.000 22.05836  ?  210 TYR   G CA  1 
ATOM   4219  C C   . TYR   C  1 210 ? 11.90636  14.79383  18.34695  1.000 35.06669  ?  210 TYR   G C   1 
ATOM   4220  O O   . TYR   C  1 210 ? 12.65401  15.49862  17.65721  1.000 28.01298  ?  210 TYR   G O   1 
ATOM   4221  C CB  . TYR   C  1 210 ? 11.20613  12.48972  17.61505  1.000 11.46306  ?  210 TYR   G CB  1 
ATOM   4222  C CG  . TYR   C  1 210 ? 11.17072  12.99781  16.20255  1.000 44.53634  ?  210 TYR   G CG  1 
ATOM   4223  C CD1 . TYR   C  1 210 ? 12.19129  12.68522  15.31456  1.000 21.55892  ?  210 TYR   G CD1 1 
ATOM   4224  C CD2 . TYR   C  1 210 ? 10.14268  13.82218  15.76380  1.000 36.97247  ?  210 TYR   G CD2 1 
ATOM   4225  C CE1 . TYR   C  1 210 ? 12.19449  13.16740  14.01481  1.000 25.18170  ?  210 TYR   G CE1 1 
ATOM   4226  C CE2 . TYR   C  1 210 ? 10.13137  14.30987  14.46716  1.000 38.74214  ?  210 TYR   G CE2 1 
ATOM   4227  C CZ  . TYR   C  1 210 ? 11.16043  13.97427  13.60104  1.000 47.73733  ?  210 TYR   G CZ  1 
ATOM   4228  O OH  . TYR   C  1 210 ? 11.15634  14.44191  12.31969  1.000 29.51349  ?  210 TYR   G OH  1 
ATOM   4229  N N   . ASP   C  1 211 ? 10.86174  15.29355  19.01011  1.000 32.04139  ?  211 ASP   G N   1 
ATOM   4230  C CA  . ASP   C  1 211 ? 10.55110  16.71790  18.95807  1.000 26.76516  ?  211 ASP   G CA  1 
ATOM   4231  C C   . ASP   C  1 211 ? 11.72772  17.55765  19.42617  1.000 48.15386  ?  211 ASP   G C   1 
ATOM   4232  O O   . ASP   C  1 211 ? 11.98803  18.64013  18.87629  1.000 29.03615  ?  211 ASP   G O   1 
ATOM   4233  C CB  . ASP   C  1 211 ? 9.31802   17.02827  19.81145  1.000 29.90477  ?  211 ASP   G CB  1 
ATOM   4234  C CG  . ASP   C  1 211 ? 8.94073   18.49893  19.76095  1.000 30.44807  ?  211 ASP   G CG  1 
ATOM   4235  O OD1 . ASP   C  1 211 ? 8.52817   18.97054  18.66959  1.000 35.19941  ?  211 ASP   G OD1 1 
ATOM   4236  O OD2 . ASP   C  1 211 ? 9.06565   19.18461  20.80292  1.000 53.11460  -1 211 ASP   G OD2 1 
ATOM   4237  N N   . ASP   C  1 212 ? 12.43201  17.08490  20.46109  1.000 31.14233  ?  212 ASP   G N   1 
ATOM   4238  C CA  . ASP   C  1 212 ? 13.63726  17.77076  20.91877  1.000 40.66021  ?  212 ASP   G CA  1 
ATOM   4239  C C   . ASP   C  1 212 ? 14.66361  17.88167  19.79014  1.000 32.92398  ?  212 ASP   G C   1 
ATOM   4240  O O   . ASP   C  1 212 ? 15.26633  18.94428  19.57883  1.000 33.61092  ?  212 ASP   G O   1 
ATOM   4241  C CB  . ASP   C  1 212 ? 14.21037  17.02490  22.12699  1.000 42.13878  ?  212 ASP   G CB  1 
ATOM   4242  C CG  . ASP   C  1 212 ? 15.33672  17.77889  22.81678  1.000 50.25938  ?  212 ASP   G CG  1 
ATOM   4243  O OD1 . ASP   C  1 212 ? 15.37787  19.02373  22.70671  1.000 65.25964  ?  212 ASP   G OD1 1 
ATOM   4244  O OD2 . ASP   C  1 212 ? 16.18999  17.11094  23.45304  1.000 51.13204  -1 212 ASP   G OD2 1 
ATOM   4245  N N   . PHE   C  1 213 ? 14.85109  16.80100  19.03519  1.000 18.39226  ?  213 PHE   G N   1 
ATOM   4246  C CA  . PHE   C  1 213 ? 15.77353  16.83064  17.90581  1.000 15.66248  ?  213 PHE   G CA  1 
ATOM   4247  C C   . PHE   C  1 213 ? 15.25317  17.73192  16.79078  1.000 52.57143  ?  213 PHE   G C   1 
ATOM   4248  O O   . PHE   C  1 213 ? 16.01810  18.51135  16.19545  1.000 27.06861  ?  213 PHE   G O   1 
ATOM   4249  C CB  . PHE   C  1 213 ? 15.99233  15.40360  17.39277  1.000 22.34070  ?  213 PHE   G CB  1 
ATOM   4250  C CG  . PHE   C  1 213 ? 16.54278  15.34744  16.02135  1.000 35.04026  ?  213 PHE   G CG  1 
ATOM   4251  C CD1 . PHE   C  1 213 ? 17.90923  15.51190  15.80272  1.000 38.52208  ?  213 PHE   G CD1 1 
ATOM   4252  C CD2 . PHE   C  1 213 ? 15.70216  15.14400  14.93772  1.000 23.24603  ?  213 PHE   G CD2 1 
ATOM   4253  C CE1 . PHE   C  1 213 ? 18.43118  15.46566  14.51641  1.000 47.99723  ?  213 PHE   G CE1 1 
ATOM   4254  C CE2 . PHE   C  1 213 ? 16.21501  15.09504  13.65274  1.000 50.93837  ?  213 PHE   G CE2 1 
ATOM   4255  C CZ  . PHE   C  1 213 ? 17.58277  15.25798  13.44095  1.000 40.39117  ?  213 PHE   G CZ  1 
ATOM   4256  N N   . PHE   C  1 214 ? 13.95428  17.61271  16.48883  1.000 22.78458  ?  214 PHE   G N   1 
ATOM   4257  C CA  . PHE   C  1 214 ? 13.31796  18.41253  15.44753  1.000 21.07733  ?  214 PHE   G CA  1 
ATOM   4258  C C   . PHE   C  1 214 ? 13.48015  19.91048  15.71436  1.000 19.88299  ?  214 PHE   G C   1 
ATOM   4259  O O   . PHE   C  1 214 ? 13.70517  20.69875  14.78253  1.000 47.50592  ?  214 PHE   G O   1 
ATOM   4260  C CB  . PHE   C  1 214 ? 11.84181  18.01379  15.36551  1.000 29.81149  ?  214 PHE   G CB  1 
ATOM   4261  C CG  . PHE   C  1 214 ? 11.07545  18.69085  14.26643  1.000 28.02221  ?  214 PHE   G CG  1 
ATOM   4262  C CD1 . PHE   C  1 214 ? 11.19082  18.25671  12.95614  1.000 26.56090  ?  214 PHE   G CD1 1 
ATOM   4263  C CD2 . PHE   C  1 214 ? 10.21199  19.74145  14.54681  1.000 35.45519  ?  214 PHE   G CD2 1 
ATOM   4264  C CE1 . PHE   C  1 214 ? 10.48940  18.86907  11.93606  1.000 23.00582  ?  214 PHE   G CE1 1 
ATOM   4265  C CE2 . PHE   C  1 214 ? 9.49147   20.35928  13.52718  1.000 34.84637  ?  214 PHE   G CE2 1 
ATOM   4266  C CZ  . PHE   C  1 214 ? 9.62591   19.91815  12.21631  1.000 28.76658  ?  214 PHE   G CZ  1 
ATOM   4267  N N   . ASN   C  1 215 ? 13.39788  20.31783  16.98253  1.000 18.16226  ?  215 ASN   G N   1 
ATOM   4268  C CA  . ASN   C  1 215 ? 13.53611  21.71713  17.37804  1.000 25.82097  ?  215 ASN   G CA  1 
ATOM   4269  C C   . ASN   C  1 215 ? 14.87719  22.00344  18.04963  1.000 35.60353  ?  215 ASN   G C   1 
ATOM   4270  O O   . ASN   C  1 215 ? 14.96389  22.80865  18.98151  1.000 29.34721  ?  215 ASN   G O   1 
ATOM   4271  C CB  . ASN   C  1 215 ? 12.37978  22.13214  18.27888  1.000 25.66825  ?  215 ASN   G CB  1 
ATOM   4272  C CG  . ASN   C  1 215 ? 11.10045  22.32521  17.49353  1.000 48.79016  ?  215 ASN   G CG  1 
ATOM   4273  O OD1 . ASN   C  1 215 ? 11.09541  22.94753  16.42390  1.000 27.45059  ?  215 ASN   G OD1 1 
ATOM   4274  N ND2 . ASN   C  1 215 ? 10.01568  21.76467  17.99732  1.000 24.17846  ?  215 ASN   G ND2 1 
ATOM   4275  N N   . ARG   C  1 216 ? 15.93530  21.34627  17.56606  1.000 20.39052  ?  216 ARG   G N   1 
ATOM   4276  C CA  . ARG   C  1 216 ? 17.27625  21.55612  18.08467  1.000 29.27120  ?  216 ARG   G CA  1 
ATOM   4277  C C   . ARG   C  1 216 ? 17.68409  23.02410  17.95621  1.000 52.31456  ?  216 ARG   G C   1 
ATOM   4278  O O   . ARG   C  1 216 ? 17.35040  23.69886  16.97749  1.000 28.49895  ?  216 ARG   G O   1 
ATOM   4279  C CB  . ARG   C  1 216 ? 18.24888  20.65540  17.32401  1.000 25.55408  ?  216 ARG   G CB  1 
ATOM   4280  C CG  . ARG   C  1 216 ? 18.31285  20.95249  15.84292  1.000 24.84538  ?  216 ARG   G CG  1 
ATOM   4281  C CD  . ARG   C  1 216 ? 19.05497  19.87720  15.09039  1.000 35.15940  ?  216 ARG   G CD  1 
ATOM   4282  N NE  . ARG   C  1 216 ? 18.92964  20.05107  13.64602  1.000 24.09971  ?  216 ARG   G NE  1 
ATOM   4283  C CZ  . ARG   C  1 216 ? 17.87525  19.65466  12.94506  1.000 48.87883  ?  216 ARG   G CZ  1 
ATOM   4284  N NH1 . ARG   C  1 216 ? 16.85112  19.04272  13.52416  1.000 27.69198  ?  216 ARG   G NH1 1 
ATOM   4285  N NH2 . ARG   C  1 216 ? 17.84218  19.88438  11.63576  1.000 32.17633  ?  216 ARG   G NH2 1 
ATOM   4286  N N   . ARG   C  1 217 ? 18.37316  23.53594  19.00071  1.000 25.17817  ?  217 ARG   G N   1 
ATOM   4287  C CA  . ARG   C  1 217 ? 18.87714  24.91769  19.08307  1.000 29.91078  ?  217 ARG   G CA  1 
ATOM   4288  C C   . ARG   C  1 217 ? 20.27249  25.06471  18.45202  1.000 33.54118  ?  217 ARG   G C   1 
ATOM   4289  O O   . ARG   C  1 217 ? 21.08150  24.13144  18.49145  1.000 50.57342  ?  217 ARG   G O   1 
ATOM   4290  C CB  . ARG   C  1 217 ? 18.93887  25.37771  20.55287  1.000 11.11434  ?  217 ARG   G CB  1 
ATOM   4291  C CG  . ARG   C  1 217 ? 17.63291  25.23432  21.32489  1.000 18.63097  ?  217 ARG   G CG  1 
ATOM   4292  C CD  . ARG   C  1 217 ? 17.67757  25.90949  22.69636  1.000 56.53572  ?  217 ARG   G CD  1 
ATOM   4293  N NE  . ARG   C  1 217 ? 16.49420  25.61840  23.50900  1.000 109.41835 ?  217 ARG   G NE  1 
ATOM   4294  C CZ  . ARG   C  1 217 ? 15.52067  26.48527  23.76338  1.000 68.61720  ?  217 ARG   G CZ  1 
ATOM   4295  N NH1 . ARG   C  1 217 ? 15.54968  27.72128  23.27819  1.000 95.84107  ?  217 ARG   G NH1 1 
ATOM   4296  N NH2 . ARG   C  1 217 ? 14.48868  26.10155  24.51562  1.000 124.89000 ?  217 ARG   G NH2 1 
ATOM   4297  N N   . PHE   C  1 218 ? 20.57572  26.26553  17.89906  1.000 32.83097  ?  218 PHE   G N   1 
ATOM   4298  C CA  . PHE   C  1 218 ? 21.92473  26.48913  17.38152  1.000 21.69879  ?  218 PHE   G CA  1 
ATOM   4299  C C   . PHE   C  1 218 ? 22.92666  26.52353  18.53356  1.000 52.14910  ?  218 PHE   G C   1 
ATOM   4300  O O   . PHE   C  1 218 ? 22.66998  27.13884  19.57166  1.000 23.90987  ?  218 PHE   G O   1 
ATOM   4301  C CB  . PHE   C  1 218 ? 22.00418  27.79726  16.60332  1.000 12.54972  ?  218 PHE   G CB  1 
ATOM   4302  C CG  . PHE   C  1 218 ? 21.32004  27.75962  15.27150  1.000 32.20553  ?  218 PHE   G CG  1 
ATOM   4303  C CD1 . PHE   C  1 218 ? 21.74896  26.87908  14.27421  1.000 14.21764  ?  218 PHE   G CD1 1 
ATOM   4304  C CD2 . PHE   C  1 218 ? 20.25360  28.62325  15.00283  1.000 22.87831  ?  218 PHE   G CD2 1 
ATOM   4305  C CE1 . PHE   C  1 218 ? 21.12406  26.84956  13.03019  1.000 39.46749  ?  218 PHE   G CE1 1 
ATOM   4306  C CE2 . PHE   C  1 218 ? 19.62074  28.60039  13.77005  1.000 22.14549  ?  218 PHE   G CE2 1 
ATOM   4307  C CZ  . PHE   C  1 218 ? 20.05679  27.70915  12.77879  1.000 15.40110  ?  218 PHE   G CZ  1 
ATOM   4308  N N   . ARG   C  1 219 ? 24.07928  25.87570  18.35129  1.000 31.53910  ?  219 ARG   G N   1 
ATOM   4309  C CA  . ARG   C  1 219 ? 25.11202  25.92703  19.38340  1.000 35.87041  ?  219 ARG   G CA  1 
ATOM   4310  C C   . ARG   C  1 219 ? 25.73846  27.31032  19.48198  1.000 32.80962  ?  219 ARG   G C   1 
ATOM   4311  O O   . ARG   C  1 219 ? 26.13226  27.74335  20.56939  1.000 31.34559  ?  219 ARG   G O   1 
ATOM   4312  C CB  . ARG   C  1 219 ? 26.20365  24.89729  19.10519  1.000 28.65761  ?  219 ARG   G CB  1 
ATOM   4313  C CG  . ARG   C  1 219 ? 27.21175  24.82605  20.25666  1.000 45.09732  ?  219 ARG   G CG  1 
ATOM   4314  C CD  . ARG   C  1 219 ? 28.39780  23.94488  19.94686  1.000 35.00147  ?  219 ARG   G CD  1 
ATOM   4315  N NE  . ARG   C  1 219 ? 28.02105  22.54860  19.77671  1.000 21.12845  ?  219 ARG   G NE  1 
ATOM   4316  C CZ  . ARG   C  1 219 ? 27.65031  21.75483  20.77219  1.000 89.03548  ?  219 ARG   G CZ  1 
ATOM   4317  N NH1 . ARG   C  1 219 ? 27.60268  22.18395  22.02152  1.000 21.38250  ?  219 ARG   G NH1 1 
ATOM   4318  N NH2 . ARG   C  1 219 ? 27.31514  20.49847  20.50941  1.000 13.19798  ?  219 ARG   G NH2 1 
ATOM   4319  N N   . ASN   C  1 220 ? 25.83882  28.01446  18.36362  1.000 29.93616  ?  220 ASN   G N   1 
ATOM   4320  C CA  . ASN   C  1 220 ? 26.53353  29.28786  18.34117  1.000 35.98312  ?  220 ASN   G CA  1 
ATOM   4321  C C   . ASN   C  1 220 ? 26.08598  30.06930  17.11439  1.000 32.87107  ?  220 ASN   G C   1 
ATOM   4322  O O   . ASN   C  1 220 ? 26.75887  30.04297  16.07347  1.000 38.31316  ?  220 ASN   G O   1 
ATOM   4323  C CB  . ASN   C  1 220 ? 28.04526  29.05240  18.32592  1.000 43.89448  ?  220 ASN   G CB  1 
ATOM   4324  C CG  . ASN   C  1 220 ? 28.83898  30.30793  18.61368  1.000 69.17746  ?  220 ASN   G CG  1 
ATOM   4325  O OD1 . ASN   C  1 220 ? 28.34129  31.43312  18.48289  1.000 44.42558  ?  220 ASN   G OD1 1 
ATOM   4326  N ND2 . ASN   C  1 220 ? 30.08887  30.12218  19.00296  1.000 45.71022  ?  220 ASN   G ND2 1 
ATOM   4327  N N   . ARG   C  1 221 ? 24.95253  30.76756  17.22310  1.000 30.94945  ?  221 ARG   G N   1 
ATOM   4328  C CA  . ARG   C  1 221 ? 24.40081  31.42516  16.04088  1.000 34.29151  ?  221 ARG   G CA  1 
ATOM   4329  C C   . ARG   C  1 221 ? 25.34873  32.48804  15.49171  1.000 42.98213  ?  221 ARG   G C   1 
ATOM   4330  O O   . ARG   C  1 221 ? 25.37769  32.70618  14.27710  1.000 32.91502  ?  221 ARG   G O   1 
ATOM   4331  C CB  . ARG   C  1 221 ? 23.01791  32.01964  16.34840  1.000 21.76776  ?  221 ARG   G CB  1 
ATOM   4332  C CG  . ARG   C  1 221 ? 23.01557  33.19549  17.33245  1.000 22.29214  ?  221 ARG   G CG  1 
ATOM   4333  C CD  . ARG   C  1 221 ? 22.93857  34.55150  16.61457  1.000 33.99163  ?  221 ARG   G CD  1 
ATOM   4334  N NE  . ARG   C  1 221 ? 23.00714  35.66954  17.55367  1.000 29.02203  ?  221 ARG   G NE  1 
ATOM   4335  C CZ  . ARG   C  1 221 ? 21.95999  36.23528  18.14556  1.000 40.55118  ?  221 ARG   G CZ  1 
ATOM   4336  N NH1 . ARG   C  1 221 ? 20.72123  35.81729  17.93060  1.000 34.92257  ?  221 ARG   G NH1 1 
ATOM   4337  N NH2 . ARG   C  1 221 ? 22.15728  37.25500  18.96892  1.000 25.64156  ?  221 ARG   G NH2 1 
ATOM   4338  N N   . ASP   C  1 222 ? 26.16009  33.12631  16.35056  1.000 29.37372  ?  222 ASP   G N   1 
ATOM   4339  C CA  . ASP   C  1 222 ? 27.08232  34.15651  15.86876  1.000 46.35654  ?  222 ASP   G CA  1 
ATOM   4340  C C   . ASP   C  1 222 ? 28.13818  33.61544  14.90031  1.000 49.08279  ?  222 ASP   G C   1 
ATOM   4341  O O   . ASP   C  1 222 ? 28.68771  34.38920  14.10355  1.000 35.90542  ?  222 ASP   G O   1 
ATOM   4342  C CB  . ASP   C  1 222 ? 27.76577  34.85439  17.04494  1.000 23.87923  ?  222 ASP   G CB  1 
ATOM   4343  C CG  . ASP   C  1 222 ? 26.76841  35.59464  17.95543  1.000 42.87134  ?  222 ASP   G CG  1 
ATOM   4344  O OD1 . ASP   C  1 222 ? 26.13978  36.59733  17.53128  1.000 49.83601  ?  222 ASP   G OD1 1 
ATOM   4345  O OD2 . ASP   C  1 222 ? 26.59949  35.13391  19.10023  1.000 58.97001  -1 222 ASP   G OD2 1 
ATOM   4346  N N   . ILE   C  1 223 ? 28.42543  32.31472  14.92438  1.000 27.20532  ?  223 ILE   G N   1 
ATOM   4347  C CA  . ILE   C  1 223 ? 29.27234  31.73578  13.88444  1.000 36.76154  ?  223 ILE   G CA  1 
ATOM   4348  C C   . ILE   C  1 223 ? 28.44471  31.36910  12.65404  1.000 47.97040  ?  223 ILE   G C   1 
ATOM   4349  O O   . ILE   C  1 223 ? 28.70677  31.84811  11.54420  1.000 50.49739  ?  223 ILE   G O   1 
ATOM   4350  C CB  . ILE   C  1 223 ? 30.04695  30.52360  14.43781  1.000 49.39067  ?  223 ILE   G CB  1 
ATOM   4351  C CG1 . ILE   C  1 223 ? 31.08584  30.97599  15.45974  1.000 30.40736  ?  223 ILE   G CG1 1 
ATOM   4352  C CG2 . ILE   C  1 223 ? 30.73924  29.75146  13.32852  1.000 18.19579  ?  223 ILE   G CG2 1 
ATOM   4353  C CD1 . ILE   C  1 223 ? 31.73380  29.81876  16.16063  1.000 33.43567  ?  223 ILE   G CD1 1 
ATOM   4354  N N   . ASP   C  1 224 ? 27.41116  30.53974  12.84296  1.000 32.83681  ?  224 ASP   G N   1 
ATOM   4355  C CA  . ASP   C  1 224 ? 26.71249  29.87982  11.73978  1.000 33.94235  ?  224 ASP   G CA  1 
ATOM   4356  C C   . ASP   C  1 224 ? 25.55124  30.66973  11.13815  1.000 34.81911  ?  224 ASP   G C   1 
ATOM   4357  O O   . ASP   C  1 224 ? 25.29371  30.53833  9.93418   1.000 30.41083  ?  224 ASP   G O   1 
ATOM   4358  C CB  . ASP   C  1 224 ? 26.19248  28.52583  12.21102  1.000 29.85246  ?  224 ASP   G CB  1 
ATOM   4359  C CG  . ASP   C  1 224 ? 27.29099  27.65411  12.77240  1.000 43.22111  ?  224 ASP   G CG  1 
ATOM   4360  O OD1 . ASP   C  1 224 ? 28.17164  27.25753  11.98140  1.000 46.35128  ?  224 ASP   G OD1 1 
ATOM   4361  O OD2 . ASP   C  1 224 ? 27.27610  27.38726  13.99572  1.000 42.87314  -1 224 ASP   G OD2 1 
ATOM   4362  N N   . ARG   C  1 225 ? 24.82116  31.45259  11.93251  1.000 43.37812  ?  225 ARG   G N   1 
ATOM   4363  C CA  . ARG   C  1 225 ? 23.64138  32.18754  11.45956  1.000 34.05204  ?  225 ARG   G CA  1 
ATOM   4364  C C   . ARG   C  1 225 ? 23.61397  33.54622  12.13844  1.000 49.15027  ?  225 ARG   G C   1 
ATOM   4365  O O   . ARG   C  1 225 ? 22.74253  33.83753  12.96783  1.000 43.18759  ?  225 ARG   G O   1 
ATOM   4366  C CB  . ARG   C  1 225 ? 22.35605  31.40257  11.74926  1.000 35.10401  ?  225 ARG   G CB  1 
ATOM   4367  C CG  . ARG   C  1 225 ? 22.13307  30.19102  10.92752  1.000 20.92154  ?  225 ARG   G CG  1 
ATOM   4368  C CD  . ARG   C  1 225 ? 22.07076  30.62888  9.49546   1.000 18.30441  ?  225 ARG   G CD  1 
ATOM   4369  N NE  . ARG   C  1 225 ? 21.70153  29.56425  8.58141   1.000 68.58098  ?  225 ARG   G NE  1 
ATOM   4370  C CZ  . ARG   C  1 225 ? 22.61746  28.90633  7.90032   1.000 28.44922  ?  225 ARG   G CZ  1 
ATOM   4371  N NH1 . ARG   C  1 225 ? 23.89615  29.14786  8.10320   1.000 14.08196  ?  225 ARG   G NH1 1 
ATOM   4372  N NH2 . ARG   C  1 225 ? 22.24206  28.02234  6.96764   1.000 32.57850  ?  225 ARG   G NH2 1 
ATOM   4373  N N   . PRO   C  1 226 ? 24.57849  34.40404  11.82821  1.000 42.22405  ?  226 PRO   G N   1 
ATOM   4374  C CA  . PRO   C  1 226 ? 24.68228  35.68136  12.54613  1.000 24.02626  ?  226 PRO   G CA  1 
ATOM   4375  C C   . PRO   C  1 226 ? 23.52964  36.61668  12.21981  1.000 48.56265  ?  226 PRO   G C   1 
ATOM   4376  O O   . PRO   C  1 226 ? 22.98713  36.61187  11.11309  1.000 31.79398  ?  226 PRO   G O   1 
ATOM   4377  C CB  . PRO   C  1 226 ? 26.00964  36.26524  12.04238  1.000 23.14150  ?  226 PRO   G CB  1 
ATOM   4378  C CG  . PRO   C  1 226 ? 26.21498  35.61578  10.67756  1.000 21.91825  ?  226 PRO   G CG  1 
ATOM   4379  C CD  . PRO   C  1 226 ? 25.63668  34.23082  10.80964  1.000 25.12079  ?  226 PRO   G CD  1 
ATOM   4380  N N   . VAL   C  1 227 ? 23.17050  37.43953  13.20438  1.000 20.11688  ?  227 VAL   G N   1 
ATOM   4381  C CA  . VAL   C  1 227 ? 22.24146  38.54343  12.99535  1.000 17.14081  ?  227 VAL   G CA  1 
ATOM   4382  C C   . VAL   C  1 227 ? 22.95303  39.59585  12.15574  1.000 29.57680  ?  227 VAL   G C   1 
ATOM   4383  O O   . VAL   C  1 227 ? 23.58541  40.50816  12.69945  1.000 30.56722  ?  227 VAL   G O   1 
ATOM   4384  C CB  . VAL   C  1 227 ? 21.75077  39.12594  14.33526  1.000 20.31259  ?  227 VAL   G CB  1 
ATOM   4385  C CG1 . VAL   C  1 227 ? 20.73837  40.24244  14.11334  1.000 21.47128  ?  227 VAL   G CG1 1 
ATOM   4386  C CG2 . VAL   C  1 227 ? 21.15136  38.02302  15.19433  1.000 15.53655  ?  227 VAL   G CG2 1 
ATOM   4387  N N   . VAL   C  1 228 ? 22.84857  39.46867  10.82575  1.000 25.72941  ?  228 VAL   G N   1 
ATOM   4388  C CA  . VAL   C  1 228 ? 23.66418  40.24586  9.89763   1.000 13.32127  ?  228 VAL   G CA  1 
ATOM   4389  C C   . VAL   C  1 228 ? 23.48897  41.73628  10.14142  1.000 53.60693  ?  228 VAL   G C   1 
ATOM   4390  O O   . VAL   C  1 228 ? 22.36627  42.24446  10.23899  1.000 23.87797  ?  228 VAL   G O   1 
ATOM   4391  C CB  . VAL   C  1 228 ? 23.31159  39.85927  8.45520   1.000 31.73776  ?  228 VAL   G CB  1 
ATOM   4392  C CG1 . VAL   C  1 228 ? 24.12871  40.67263  7.46575   1.000 18.13227  ?  228 VAL   G CG1 1 
ATOM   4393  C CG2 . VAL   C  1 228 ? 23.53317  38.36234  8.26089   1.000 12.74713  ?  228 VAL   G CG2 1 
ATOM   4394  N N   . GLY   C  1 229 ? 24.61405  42.44578  10.24146  1.000 30.08447  ?  229 GLY   G N   1 
ATOM   4395  C CA  . GLY   C  1 229 ? 24.61652  43.86381  10.53919  1.000 13.99069  ?  229 GLY   G CA  1 
ATOM   4396  C C   . GLY   C  1 229 ? 24.49807  44.20762  12.00889  1.000 21.00713  ?  229 GLY   G C   1 
ATOM   4397  O O   . GLY   C  1 229 ? 24.64970  45.38723  12.37079  1.000 36.20881  ?  229 GLY   G O   1 
ATOM   4398  N N   . GLY   C  1 230 ? 24.21569  43.22723  12.85705  1.000 36.13806  ?  230 GLY   G N   1 
ATOM   4399  C CA  . GLY   C  1 230 ? 24.13271  43.39939  14.30237  1.000 8.25524   ?  230 GLY   G CA  1 
ATOM   4400  C C   . GLY   C  1 230 ? 22.77789  43.90204  14.76602  1.000 54.74731  ?  230 GLY   G C   1 
ATOM   4401  O O   . GLY   C  1 230 ? 22.10439  44.69250  14.09817  1.000 24.75474  ?  230 GLY   G O   1 
ATOM   4402  N N   . VAL   C  1 231 ? 22.39112  43.44715  15.96294  1.000 25.77329  ?  231 VAL   G N   1 
ATOM   4403  C CA  . VAL   C  1 231 ? 21.10585  43.77466  16.56995  1.000 66.11783  ?  231 VAL   G CA  1 
ATOM   4404  C C   . VAL   C  1 231 ? 20.88956  45.28019  16.68195  1.000 25.98172  ?  231 VAL   G C   1 
ATOM   4405  O O   . VAL   C  1 231 ? 19.74185  45.74188  16.73431  1.000 61.09479  ?  231 VAL   G O   1 
ATOM   4406  C CB  . VAL   C  1 231 ? 21.02251  43.07509  17.93969  1.000 18.58060  ?  231 VAL   G CB  1 
ATOM   4407  C CG1 . VAL   C  1 231 ? 22.18279  43.49811  18.79016  1.000 73.38748  ?  231 VAL   G CG1 1 
ATOM   4408  C CG2 . VAL   C  1 231 ? 19.74779  43.40693  18.64871  1.000 45.93565  ?  231 VAL   G CG2 1 
ATOM   4409  N N   . ASN   C  1 232 ? 21.96604  46.06658  16.65092  1.000 37.63767  ?  232 ASN   G N   1 
ATOM   4410  C CA  . ASN   C  1 232 ? 21.86537  47.51519  16.80875  1.000 26.61395  ?  232 ASN   G CA  1 
ATOM   4411  C C   . ASN   C  1 232 ? 21.44901  48.24950  15.54036  1.000 38.29723  ?  232 ASN   G C   1 
ATOM   4412  O O   . ASN   C  1 232 ? 21.02413  49.40730  15.63384  1.000 33.50510  ?  232 ASN   G O   1 
ATOM   4413  C CB  . ASN   C  1 232 ? 23.19605  48.08455  17.28333  1.000 43.35807  ?  232 ASN   G CB  1 
ATOM   4414  C CG  . ASN   C  1 232 ? 23.32471  48.06707  18.78318  1.000 42.97926  ?  232 ASN   G CG  1 
ATOM   4415  O OD1 . ASN   C  1 232 ? 22.55180  47.39101  19.47473  1.000 43.98472  ?  232 ASN   G OD1 1 
ATOM   4416  N ND2 . ASN   C  1 232 ? 24.29882  48.81343  19.30452  1.000 119.11161 ?  232 ASN   G ND2 1 
ATOM   4417  N N   . ASN   C  1 233 ? 21.58326  47.63731  14.36389  1.000 24.22544  ?  233 ASN   G N   1 
ATOM   4418  C CA  . ASN   C  1 233 ? 21.16001  48.27049  13.12146  1.000 31.92472  ?  233 ASN   G CA  1 
ATOM   4419  C C   . ASN   C  1 233 ? 19.68354  47.93365  12.92466  1.000 84.39332  ?  233 ASN   G C   1 
ATOM   4420  O O   . ASN   C  1 233 ? 19.33048  46.79374  12.58267  1.000 29.67292  ?  233 ASN   G O   1 
ATOM   4421  C CB  . ASN   C  1 233 ? 22.01443  47.78560  11.95176  1.000 11.83841  ?  233 ASN   G CB  1 
ATOM   4422  C CG  . ASN   C  1 233 ? 21.71265  48.52527  10.66703  1.000 49.22849  ?  233 ASN   G CG  1 
ATOM   4423  O OD1 . ASN   C  1 233 ? 20.60614  49.03202  10.46274  1.000 42.29135  ?  233 ASN   G OD1 1 
ATOM   4424  N ND2 . ASN   C  1 233 ? 22.69548  48.57912  9.78228   1.000 37.97801  ?  233 ASN   G ND2 1 
ATOM   4425  N N   . THR   C  1 234 ? 18.81390  48.90973  13.16473  1.000 26.52486  ?  234 THR   G N   1 
ATOM   4426  C CA  . THR   C  1 234 ? 17.38236  48.64687  13.10925  1.000 41.85930  ?  234 THR   G CA  1 
ATOM   4427  C C   . THR   C  1 234 ? 16.79321  48.91834  11.73192  1.000 22.09343  ?  234 THR   G C   1 
ATOM   4428  O O   . THR   C  1 234 ? 15.57383  48.82358  11.56108  1.000 72.59109  ?  234 THR   G O   1 
ATOM   4429  C CB  . THR   C  1 234 ? 16.64207  49.44895  14.18791  1.000 27.75585  ?  234 THR   G CB  1 
ATOM   4430  O OG1 . THR   C  1 234 ? 16.69411  50.84575  13.89492  1.000 37.93965  ?  234 THR   G OG1 1 
ATOM   4431  C CG2 . THR   C  1 234 ? 17.26283  49.20322  15.55212  1.000 17.74393  ?  234 THR   G CG2 1 
ATOM   4432  N N   . THR   C  1 235 ? 17.63488  49.19836  10.74276  1.000 41.92619  ?  235 THR   G N   1 
ATOM   4433  C CA  . THR   C  1 235 ? 17.18148  49.36318  9.37062   1.000 24.13660  ?  235 THR   G CA  1 
ATOM   4434  C C   . THR   C  1 235 ? 17.08958  48.04356  8.61796   1.000 44.24097  ?  235 THR   G C   1 
ATOM   4435  O O   . THR   C  1 235 ? 16.73300  48.05037  7.43227   1.000 27.49685  ?  235 THR   G O   1 
ATOM   4436  C CB  . THR   C  1 235 ? 18.12379  50.30890  8.62455   1.000 59.28699  ?  235 THR   G CB  1 
ATOM   4437  O OG1 . THR   C  1 235 ? 19.30748  49.59813  8.21552   1.000 20.47633  ?  235 THR   G OG1 1 
ATOM   4438  C CG2 . THR   C  1 235 ? 18.53204  51.44192  9.53597   1.000 30.44479  ?  235 THR   G CG2 1 
ATOM   4439  N N   . LEU   C  1 236 ? 17.39473  46.91939  9.27226   1.000 36.66324  ?  236 LEU   G N   1 
ATOM   4440  C CA  . LEU   C  1 236 ? 17.46570  45.61388  8.62562   1.000 37.13489  ?  236 LEU   G CA  1 
ATOM   4441  C C   . LEU   C  1 236 ? 16.39490  44.69942  9.19107   1.000 30.75313  ?  236 LEU   G C   1 
ATOM   4442  O O   . LEU   C  1 236 ? 16.11600  44.72668  10.39510  1.000 32.47142  ?  236 LEU   G O   1 
ATOM   4443  C CB  . LEU   C  1 236 ? 18.83296  44.96254  8.82600   1.000 30.66116  ?  236 LEU   G CB  1 
ATOM   4444  C CG  . LEU   C  1 236 ? 20.01669  45.86317  8.48319   1.000 37.95426  ?  236 LEU   G CG  1 
ATOM   4445  C CD1 . LEU   C  1 236 ? 21.29946  45.29191  9.08968   1.000 29.90509  ?  236 LEU   G CD1 1 
ATOM   4446  C CD2 . LEU   C  1 236 ? 20.11874  46.04713  6.96894   1.000 20.38074  ?  236 LEU   G CD2 1 
ATOM   4447  N N   . ILE   C  1 237 ? 15.79628  43.89470  8.31541   1.000 34.79415  ?  237 ILE   G N   1 
ATOM   4448  C CA  . ILE   C  1 237 ? 14.80246  42.90054  8.70299   1.000 28.12068  ?  237 ILE   G CA  1 
ATOM   4449  C C   . ILE   C  1 237 ? 15.37127  41.52535  8.37963   1.000 39.35708  ?  237 ILE   G C   1 
ATOM   4450  O O   . ILE   C  1 237 ? 15.75004  41.25438  7.22540   1.000 26.28007  ?  237 ILE   G O   1 
ATOM   4451  C CB  . ILE   C  1 237 ? 13.45176  43.12110  7.99877   1.000 26.94390  ?  237 ILE   G CB  1 
ATOM   4452  C CG1 . ILE   C  1 237 ? 12.90389  44.52102  8.30286   1.000 23.86632  ?  237 ILE   G CG1 1 
ATOM   4453  C CG2 . ILE   C  1 237 ? 12.44847  42.04830  8.44998   1.000 24.81321  ?  237 ILE   G CG2 1 
ATOM   4454  C CD1 . ILE   C  1 237 ? 11.54408  44.82244  7.66737   1.000 25.76108  ?  237 ILE   G CD1 1 
ATOM   4455  N N   . SER   C  1 238 ? 15.41318  40.65686  9.40000   1.000 22.04137  ?  238 SER   G N   1 
ATOM   4456  C CA  . SER   C  1 238 ? 15.99882  39.32165  9.29788   1.000 28.81037  ?  238 SER   G CA  1 
ATOM   4457  C C   . SER   C  1 238 ? 14.97290  38.27729  8.88127   1.000 37.55638  ?  238 SER   G C   1 
ATOM   4458  O O   . SER   C  1 238 ? 13.78107  38.38988  9.18249   1.000 22.52856  ?  238 SER   G O   1 
ATOM   4459  C CB  . SER   C  1 238 ? 16.61292  38.88529  10.63184  1.000 27.27292  ?  238 SER   G CB  1 
ATOM   4460  O OG  . SER   C  1 238 ? 17.93248  39.36990  10.76638  1.000 41.05423  ?  238 SER   G OG  1 
ATOM   4461  N N   . ALA   C  1 239 ? 15.46511  37.23377  8.21417   1.000 32.09816  ?  239 ALA   G N   1 
ATOM   4462  C CA  . ALA   C  1 239 ? 14.65999  36.04953  7.94208   1.000 40.15336  ?  239 ALA   G CA  1 
ATOM   4463  C C   . ALA   C  1 239 ? 14.26692  35.36100  9.23923   1.000 16.35388  ?  239 ALA   G C   1 
ATOM   4464  O O   . ALA   C  1 239 ? 15.12237  35.07667  10.07907  1.000 31.78661  ?  239 ALA   G O   1 
ATOM   4465  C CB  . ALA   C  1 239 ? 15.44416  35.08091  7.06658   1.000 12.72859  ?  239 ALA   G CB  1 
ATOM   4466  N N   . ALA   C  1 240 ? 12.97119  35.05728  9.38943   1.000 27.89215  ?  240 ALA   G N   1 
ATOM   4467  C CA  . ALA   C  1 240 ? 12.48537  34.45043  10.63039  1.000 21.51172  ?  240 ALA   G CA  1 
ATOM   4468  C C   . ALA   C  1 240 ? 12.69307  32.94131  10.69089  1.000 27.98133  ?  240 ALA   G C   1 
ATOM   4469  O O   . ALA   C  1 240 ? 12.69421  32.37264  11.79236  1.000 23.29683  ?  240 ALA   G O   1 
ATOM   4470  C CB  . ALA   C  1 240 ? 10.99983  34.75221  10.82524  1.000 13.24172  ?  240 ALA   G CB  1 
ATOM   4471  N N   . CYS   C  1 241 ? 12.84497  32.28253  9.54072   1.000 19.47140  ?  241 CYS   G N   1 
ATOM   4472  C CA  . CYS   C  1 241 ? 12.95693  30.83327  9.47514   1.000 29.37745  ?  241 CYS   G CA  1 
ATOM   4473  C C   . CYS   C  1 241 ? 14.04381  30.46350  8.48160   1.000 29.68726  ?  241 CYS   G C   1 
ATOM   4474  O O   . CYS   C  1 241 ? 14.15934  31.07745  7.41266   1.000 28.68972  ?  241 CYS   G O   1 
ATOM   4475  C CB  . CYS   C  1 241 ? 11.64483  30.16022  9.04312   1.000 31.01493  ?  241 CYS   G CB  1 
ATOM   4476  S SG  . CYS   C  1 241 ? 10.27939  30.37753  10.20070  1.000 31.27126  ?  241 CYS   G SG  1 
ATOM   4477  N N   . GLU   C  1 242 ? 14.84338  29.46067  8.85409   1.000 33.99854  ?  242 GLU   G N   1 
ATOM   4478  C CA  . GLU   C  1 242 ? 15.71465  28.76853  7.91572   1.000 17.66636  ?  242 GLU   G CA  1 
ATOM   4479  C C   . GLU   C  1 242 ? 14.87413  28.11726  6.82336   1.000 20.56815  ?  242 GLU   G C   1 
ATOM   4480  O O   . GLU   C  1 242 ? 14.12854  27.16667  7.09683   1.000 43.14879  ?  242 GLU   G O   1 
ATOM   4481  C CB  . GLU   C  1 242 ? 16.53758  27.71999  8.66129   1.000 28.54737  ?  242 GLU   G CB  1 
ATOM   4482  C CG  . GLU   C  1 242 ? 17.52890  26.94684  7.79953   1.000 22.88045  ?  242 GLU   G CG  1 
ATOM   4483  C CD  . GLU   C  1 242 ? 18.76648  27.75375  7.42245   1.000 46.88502  ?  242 GLU   G CD  1 
ATOM   4484  O OE1 . GLU   C  1 242 ? 19.06012  28.80352  8.06430   1.000 26.36114  ?  242 GLU   G OE1 1 
ATOM   4485  O OE2 . GLU   C  1 242 ? 19.44620  27.31270  6.46766   1.000 32.90600  -1 242 GLU   G OE2 1 
ATOM   4486  N N   . SER   C  1 243 ? 14.97617  28.59856  5.58683   1.000 22.85567  ?  243 SER   G N   1 
ATOM   4487  C CA  . SER   C  1 243 ? 13.99904  28.20542  4.57795   1.000 34.33912  ?  243 SER   G CA  1 
ATOM   4488  C C   . SER   C  1 243 ? 14.57703  28.41405  3.18480   1.000 24.57129  ?  243 SER   G C   1 
ATOM   4489  O O   . SER   C  1 243 ? 15.69781  28.90718  3.01466   1.000 29.07535  ?  243 SER   G O   1 
ATOM   4490  C CB  . SER   C  1 243 ? 12.69825  29.00994  4.74319   1.000 23.56903  ?  243 SER   G CB  1 
ATOM   4491  O OG  . SER   C  1 243 ? 12.97560  30.40546  4.65463   1.000 31.06523  ?  243 SER   G OG  1 
ATOM   4492  N N   . LEU   C  1 244 ? 13.77048  28.04805  2.18610   1.000 27.81298  ?  244 LEU   G N   1 
ATOM   4493  C CA  . LEU   C  1 244 ? 13.98075  28.39767  0.78780   1.000 33.34829  ?  244 LEU   G CA  1 
ATOM   4494  C C   . LEU   C  1 244 ? 12.95019  29.44270  0.37021   1.000 30.85141  ?  244 LEU   G C   1 
ATOM   4495  O O   . LEU   C  1 244 ? 11.78456  29.36625  0.77500   1.000 37.13274  ?  244 LEU   G O   1 
ATOM   4496  C CB  . LEU   C  1 244 ? 13.86102  27.16160  -0.09935  1.000 18.21628  ?  244 LEU   G CB  1 
ATOM   4497  C CG  . LEU   C  1 244 ? 14.90042  26.06908  0.14682   1.000 36.65423  ?  244 LEU   G CG  1 
ATOM   4498  C CD1 . LEU   C  1 244 ? 14.47922  24.77286  -0.50423  1.000 30.61502  ?  244 LEU   G CD1 1 
ATOM   4499  C CD2 . LEU   C  1 244 ? 16.19897  26.55063  -0.41753  1.000 23.84331  ?  244 LEU   G CD2 1 
ATOM   4500  N N   . SER   C  1 245 ? 13.39216  30.43607  -0.39820  1.000 63.40802  ?  245 SER   G N   1 
ATOM   4501  C CA  . SER   C  1 245 ? 12.49902  31.37582  -1.06578  1.000 24.02985  ?  245 SER   G CA  1 
ATOM   4502  C C   . SER   C  1 245 ? 11.35447  30.63217  -1.75648  1.000 24.07548  ?  245 SER   G C   1 
ATOM   4503  O O   . SER   C  1 245 ? 11.58538  29.65266  -2.47647  1.000 33.03847  ?  245 SER   G O   1 
ATOM   4504  C CB  . SER   C  1 245 ? 13.32544  32.15861  -2.08960  1.000 26.77018  ?  245 SER   G CB  1 
ATOM   4505  O OG  . SER   C  1 245 ? 12.53904  33.07023  -2.80668  1.000 72.34298  ?  245 SER   G OG  1 
ATOM   4506  N N   . TYR   C  1 246 ? 10.11115  31.07900  -1.53482  1.000 33.33963  ?  246 TYR   G N   1 
ATOM   4507  C CA  . TYR   C  1 246 ? 8.99374   30.44773  -2.24332  1.000 23.47624  ?  246 TYR   G CA  1 
ATOM   4508  C C   . TYR   C  1 246 ? 8.21355   31.40004  -3.14048  1.000 25.09138  ?  246 TYR   G C   1 
ATOM   4509  O O   . TYR   C  1 246 ? 7.86598   31.02769  -4.27306  1.000 28.15173  ?  246 TYR   G O   1 
ATOM   4510  C CB  . TYR   C  1 246 ? 8.01819   29.76141  -1.27306  1.000 13.84855  ?  246 TYR   G CB  1 
ATOM   4511  C CG  . TYR   C  1 246 ? 6.93946   29.01089  -2.02215  1.000 30.02951  ?  246 TYR   G CG  1 
ATOM   4512  C CD1 . TYR   C  1 246 ? 5.77578   29.65633  -2.46865  1.000 23.13421  ?  246 TYR   G CD1 1 
ATOM   4513  C CD2 . TYR   C  1 246 ? 7.08945   27.65790  -2.30328  1.000 9.24292   ?  246 TYR   G CD2 1 
ATOM   4514  C CE1 . TYR   C  1 246 ? 4.81438   28.96434  -3.17842  1.000 16.87208  ?  246 TYR   G CE1 1 
ATOM   4515  C CE2 . TYR   C  1 246 ? 6.12319   26.95154  -3.00677  1.000 35.53539  ?  246 TYR   G CE2 1 
ATOM   4516  C CZ  . TYR   C  1 246 ? 4.99742   27.60818  -3.44286  1.000 26.55513  ?  246 TYR   G CZ  1 
ATOM   4517  O OH  . TYR   C  1 246 ? 4.06618   26.89064  -4.13799  1.000 42.65264  ?  246 TYR   G OH  1 
ATOM   4518  N N   . ASN   C  1 247 ? 7.85947   32.58594  -2.64488  1.000 22.33607  ?  247 ASN   G N   1 
ATOM   4519  C CA  . ASN   C  1 247 ? 7.13063   33.57393  -3.43150  1.000 14.72004  ?  247 ASN   G CA  1 
ATOM   4520  C C   . ASN   C  1 247 ? 7.35124   34.93803  -2.79855  1.000 21.79511  ?  247 ASN   G C   1 
ATOM   4521  O O   . ASN   C  1 247 ? 7.48842   35.05166  -1.57506  1.000 25.03004  ?  247 ASN   G O   1 
ATOM   4522  C CB  . ASN   C  1 247 ? 5.62814   33.27483  -3.50667  1.000 24.95808  ?  247 ASN   G CB  1 
ATOM   4523  C CG  . ASN   C  1 247 ? 4.84427   34.40723  -4.15984  1.000 22.60716  ?  247 ASN   G CG  1 
ATOM   4524  O OD1 . ASN   C  1 247 ? 4.87427   34.55792  -5.38344  1.000 40.08523  ?  247 ASN   G OD1 1 
ATOM   4525  N ND2 . ASN   C  1 247 ? 4.16336   35.22819  -3.34685  1.000 21.04873  ?  247 ASN   G ND2 1 
ATOM   4526  N N   . VAL   C  1 248 ? 7.41055   35.96786  -3.64540  1.000 22.18905  ?  248 VAL   G N   1 
ATOM   4527  C CA  . VAL   C  1 248 ? 7.27107   37.35248  -3.21055  1.000 27.98026  ?  248 VAL   G CA  1 
ATOM   4528  C C   . VAL   C  1 248 ? 6.13302   37.97506  -3.99914  1.000 19.51564  ?  248 VAL   G C   1 
ATOM   4529  O O   . VAL   C  1 248 ? 6.02357   37.76157  -5.21117  1.000 27.02404  ?  248 VAL   G O   1 
ATOM   4530  C CB  . VAL   C  1 248 ? 8.56662   38.15447  -3.40757  1.000 23.52962  ?  248 VAL   G CB  1 
ATOM   4531  C CG1 . VAL   C  1 248 ? 8.29420   39.65291  -3.24689  1.000 16.32548  ?  248 VAL   G CG1 1 
ATOM   4532  C CG2 . VAL   C  1 248 ? 9.62492   37.66854  -2.43134  1.000 21.62566  ?  248 VAL   G CG2 1 
ATOM   4533  N N   . SER   C  1 249 ? 5.25802   38.70352  -3.30916  1.000 34.04080  ?  249 SER   G N   1 
ATOM   4534  C CA  . SER   C  1 249 ? 4.16309   39.39153  -3.97827  1.000 21.41248  ?  249 SER   G CA  1 
ATOM   4535  C C   . SER   C  1 249 ? 4.13903   40.83817  -3.53197  1.000 33.99188  ?  249 SER   G C   1 
ATOM   4536  O O   . SER   C  1 249 ? 4.32931   41.13809  -2.34666  1.000 23.79366  ?  249 SER   G O   1 
ATOM   4537  C CB  . SER   C  1 249 ? 2.81257   38.74178  -3.69633  1.000 21.00052  ?  249 SER   G CB  1 
ATOM   4538  O OG  . SER   C  1 249 ? 2.69732   37.52120  -4.40141  1.000 26.69381  ?  249 SER   G OG  1 
ATOM   4539  N N   . TYR   C  1 250 ? 3.91094   41.72805  -4.49086  1.000 24.62922  ?  250 TYR   G N   1 
ATOM   4540  C CA  . TYR   C  1 250 ? 3.77631   43.14816  -4.22687  1.000 50.77624  ?  250 TYR   G CA  1 
ATOM   4541  C C   . TYR   C  1 250 ? 2.32953   43.56853  -4.43449  1.000 22.02993  ?  250 TYR   G C   1 
ATOM   4542  O O   . TYR   C  1 250 ? 1.56154   42.90093  -5.14494  1.000 31.13787  ?  250 TYR   G O   1 
ATOM   4543  C CB  . TYR   C  1 250 ? 4.69877   43.96206  -5.13856  1.000 21.46159  ?  250 TYR   G CB  1 
ATOM   4544  C CG  . TYR   C  1 250 ? 6.15504   43.62312  -4.99239  1.000 36.99718  ?  250 TYR   G CG  1 
ATOM   4545  C CD1 . TYR   C  1 250 ? 6.91212   44.16634  -3.95639  1.000 23.37733  ?  250 TYR   G CD1 1 
ATOM   4546  C CD2 . TYR   C  1 250 ? 6.77598   42.75250  -5.87338  1.000 19.49554  ?  250 TYR   G CD2 1 
ATOM   4547  C CE1 . TYR   C  1 250 ? 8.26927   43.85381  -3.81254  1.000 35.22804  ?  250 TYR   G CE1 1 
ATOM   4548  C CE2 . TYR   C  1 250 ? 8.11790   42.43636  -5.73870  1.000 30.57812  ?  250 TYR   G CE2 1 
ATOM   4549  C CZ  . TYR   C  1 250 ? 8.86667   42.98600  -4.71043  1.000 42.48417  ?  250 TYR   G CZ  1 
ATOM   4550  O OH  . TYR   C  1 250 ? 10.21329  42.66716  -4.57367  1.000 48.00324  ?  250 TYR   G OH  1 
ATOM   4551  N N   . ASP   C  1 251 ? 1.97400   44.68690  -3.79352  1.000 29.00914  ?  251 ASP   G N   1 
ATOM   4552  C CA  . ASP   C  1 251 ? 0.64189   45.27680  -3.89737  1.000 29.26737  ?  251 ASP   G CA  1 
ATOM   4553  C C   . ASP   C  1 251 ? -0.43749  44.22873  -3.61058  1.000 47.92136  ?  251 ASP   G C   1 
ATOM   4554  O O   . ASP   C  1 251 ? -1.31366  43.94495  -4.43198  1.000 32.78761  ?  251 ASP   G O   1 
ATOM   4555  C CB  . ASP   C  1 251 ? 0.45118   45.89972  -5.28167  1.000 28.59832  ?  251 ASP   G CB  1 
ATOM   4556  C CG  . ASP   C  1 251 ? -0.78793  46.76711  -5.37160  1.000 50.80844  ?  251 ASP   G CG  1 
ATOM   4557  O OD1 . ASP   C  1 251 ? -1.04166  47.51822  -4.40196  1.000 37.24163  ?  251 ASP   G OD1 1 
ATOM   4558  O OD2 . ASP   C  1 251 ? -1.48693  46.69984  -6.41791  1.000 36.78442  -1 251 ASP   G OD2 1 
ATOM   4559  N N   . VAL   C  1 252 ? -0.33796  43.61715  -2.43095  1.000 29.85011  ?  252 VAL   G N   1 
ATOM   4560  C CA  . VAL   C  1 252 ? -1.25949  42.54119  -2.07997  1.000 32.13921  ?  252 VAL   G CA  1 
ATOM   4561  C C   . VAL   C  1 252 ? -2.61791  43.11286  -1.69205  1.000 33.10510  ?  252 VAL   G C   1 
ATOM   4562  O O   . VAL   C  1 252 ? -2.75072  44.26444  -1.25947  1.000 34.75889  ?  252 VAL   G O   1 
ATOM   4563  C CB  . VAL   C  1 252 ? -0.69129  41.65908  -0.95822  1.000 34.98670  ?  252 VAL   G CB  1 
ATOM   4564  C CG1 . VAL   C  1 252 ? 0.56849   40.94403  -1.44387  1.000 22.98177  ?  252 VAL   G CG1 1 
ATOM   4565  C CG2 . VAL   C  1 252 ? -0.45906  42.49253  0.31466   1.000 23.37225  ?  252 VAL   G CG2 1 
ATOM   4566  N N   . GLN   C  1 253 ? -3.63347  42.26408  -1.81188  1.000 24.45504  ?  253 GLN   G N   1 
ATOM   4567  C CA  . GLN   C  1 253 ? -5.02001  42.68360  -1.71767  1.000 30.22148  ?  253 GLN   G CA  1 
ATOM   4568  C C   . GLN   C  1 253 ? -5.85471  41.59085  -1.04288  1.000 42.07831  ?  253 GLN   G C   1 
ATOM   4569  O O   . GLN   C  1 253 ? -5.35920  40.50899  -0.69600  1.000 29.50813  ?  253 GLN   G O   1 
ATOM   4570  C CB  . GLN   C  1 253 ? -5.55021  42.98927  -3.11723  1.000 18.85173  ?  253 GLN   G CB  1 
ATOM   4571  C CG  . GLN   C  1 253 ? -5.40036  41.78251  -4.02543  1.000 56.42808  ?  253 GLN   G CG  1 
ATOM   4572  C CD  . GLN   C  1 253 ? -5.92571  42.03069  -5.40571  1.000 47.69203  ?  253 GLN   G CD  1 
ATOM   4573  O OE1 . GLN   C  1 253 ? -5.55860  41.33583  -6.35525  1.000 48.57259  ?  253 GLN   G OE1 1 
ATOM   4574  N NE2 . GLN   C  1 253 ? -6.79850  43.02047  -5.53303  1.000 55.80233  ?  253 GLN   G NE2 1 
ATOM   4575  N N   . SER   C  1 254 ? -7.14627  41.87102  -0.87456  1.000 44.16478  ?  254 SER   G N   1 
ATOM   4576  C CA  . SER   C  1 254 ? -8.08956  40.88059  -0.38203  1.000 24.11002  ?  254 SER   G CA  1 
ATOM   4577  C C   . SER   C  1 254 ? -9.01306  40.40025  -1.50211  1.000 26.20026  ?  254 SER   G C   1 
ATOM   4578  O O   . SER   C  1 254 ? -9.34114  41.13636  -2.43984  1.000 37.95782  ?  254 SER   G O   1 
ATOM   4579  C CB  . SER   C  1 254 ? -8.89876  41.43614  0.78546   1.000 34.87718  ?  254 SER   G CB  1 
ATOM   4580  O OG  . SER   C  1 254 ? -8.03104  41.76897  1.86489   1.000 26.44894  ?  254 SER   G OG  1 
ATOM   4581  N N   . LEU   C  1 255 ? -9.39723  39.13364  -1.40750  1.000 29.97970  ?  255 LEU   G N   1 
ATOM   4582  C CA  . LEU   C  1 255 ? -10.29388 38.49887  -2.35513  1.000 32.34137  ?  255 LEU   G CA  1 
ATOM   4583  C C   . LEU   C  1 255 ? -11.58250 38.08060  -1.65132  1.000 33.88068  ?  255 LEU   G C   1 
ATOM   4584  O O   . LEU   C  1 255 ? -11.59471 37.79987  -0.44860  1.000 35.12906  ?  255 LEU   G O   1 
ATOM   4585  C CB  . LEU   C  1 255 ? -9.61792  37.28481  -2.98840  1.000 35.05976  ?  255 LEU   G CB  1 
ATOM   4586  C CG  . LEU   C  1 255 ? -8.25830  37.65100  -3.57856  1.000 36.33173  ?  255 LEU   G CG  1 
ATOM   4587  C CD1 . LEU   C  1 255 ? -7.50428  36.42505  -4.06527  1.000 35.11810  ?  255 LEU   G CD1 1 
ATOM   4588  C CD2 . LEU   C  1 255 ? -8.44642  38.65207  -4.69863  1.000 24.94871  ?  255 LEU   G CD2 1 
ATOM   4589  N N   . ASP   C  1 256 ? -12.68210 38.03716  -2.40521  1.000 41.55251  ?  256 ASP   G N   1 
ATOM   4590  C CA  . ASP   C  1 256 ? -13.92918 37.57806  -1.80048  1.000 26.92584  ?  256 ASP   G CA  1 
ATOM   4591  C C   . ASP   C  1 256 ? -14.01149 36.05199  -1.74984  1.000 49.46169  ?  256 ASP   G C   1 
ATOM   4592  O O   . ASP   C  1 256 ? -14.59697 35.51557  -0.79864  1.000 29.46446  ?  256 ASP   G O   1 
ATOM   4593  C CB  . ASP   C  1 256 ? -15.13007 38.17738  -2.53684  1.000 36.95107  ?  256 ASP   G CB  1 
ATOM   4594  C CG  . ASP   C  1 256 ? -15.26334 39.68316  -2.30531  1.000 63.67503  ?  256 ASP   G CG  1 
ATOM   4595  O OD1 . ASP   C  1 256 ? -15.62328 40.13736  -1.18559  1.000 37.48509  ?  256 ASP   G OD1 1 
ATOM   4596  O OD2 . ASP   C  1 256 ? -14.99604 40.42681  -3.25744  1.000 38.16534  -1 256 ASP   G OD2 1 
ATOM   4597  N N   . THR   C  1 257 ? -13.42286 35.34589  -2.73061  1.000 26.96101  ?  257 THR   G N   1 
ATOM   4598  C CA  . THR   C  1 257 ? -13.27819 33.89328  -2.69047  1.000 55.15169  ?  257 THR   G CA  1 
ATOM   4599  C C   . THR   C  1 257 ? -11.89516 33.50304  -3.18590  1.000 21.26899  ?  257 THR   G C   1 
ATOM   4600  O O   . THR   C  1 257 ? -11.24094 34.25208  -3.91617  1.000 43.24749  ?  257 THR   G O   1 
ATOM   4601  C CB  . THR   C  1 257 ? -14.32316 33.17943  -3.55700  1.000 28.30389  ?  257 THR   G CB  1 
ATOM   4602  O OG1 . THR   C  1 257 ? -14.20152 33.63280  -4.91293  1.000 51.01647  ?  257 THR   G OG1 1 
ATOM   4603  C CG2 . THR   C  1 257 ? -15.69495 33.47300  -3.07159  1.000 39.88973  ?  257 THR   G CG2 1 
ATOM   4604  N N   . LEU   C  1 258 ? -11.47682 32.29457  -2.80941  1.000 42.34411  ?  258 LEU   G N   1 
ATOM   4605  C CA  . LEU   C  1 258 ? -10.19681 31.73116  -3.25975  1.000 27.78947  ?  258 LEU   G CA  1 
ATOM   4606  C C   . LEU   C  1 258 ? -10.44413 30.69397  -4.35558  1.000 55.02705  ?  258 LEU   G C   1 
ATOM   4607  O O   . LEU   C  1 258 ? -10.25814 29.47754  -4.18014  1.000 58.33607  ?  258 LEU   G O   1 
ATOM   4608  C CB  . LEU   C  1 258 ? -9.44179  31.11158  -2.08397  1.000 27.91995  ?  258 LEU   G CB  1 
ATOM   4609  C CG  . LEU   C  1 258 ? -9.43131  31.92440  -0.79827  1.000 23.77792  ?  258 LEU   G CG  1 
ATOM   4610  C CD1 . LEU   C  1 258 ? -8.78512  31.08920  0.26577   1.000 30.96733  ?  258 LEU   G CD1 1 
ATOM   4611  C CD2 . LEU   C  1 258 ? -8.71605  33.26495  -0.98113  1.000 20.19054  ?  258 LEU   G CD2 1 
ATOM   4612  N N   . VAL   C  1 259 ? -10.89146 31.20345  -5.50087  1.000 49.58283  ?  259 VAL   G N   1 
ATOM   4613  C CA  . VAL   C  1 259 ? -11.30326 30.39134  -6.64269  1.000 52.92055  ?  259 VAL   G CA  1 
ATOM   4614  C C   . VAL   C  1 259 ? -10.71368 31.01860  -7.89051  1.000 117.06896 ?  259 VAL   G C   1 
ATOM   4615  O O   . VAL   C  1 259 ? -10.86784 32.23315  -8.10258  1.000 48.57589  ?  259 VAL   G O   1 
ATOM   4616  C CB  . VAL   C  1 259 ? -12.83542 30.32391  -6.81592  1.000 72.59975  ?  259 VAL   G CB  1 
ATOM   4617  C CG1 . VAL   C  1 259 ? -13.20661 29.19249  -7.75702  1.000 34.72748  ?  259 VAL   G CG1 1 
ATOM   4618  C CG2 . VAL   C  1 259 ? -13.59292 30.24819  -5.48788  1.000 59.10499  ?  259 VAL   G CG2 1 
ATOM   4619  N N   . PHE   C  1 260 ? -10.07431 30.19052  -8.73136  1.000 30.61083  ?  260 PHE   G N   1 
ATOM   4620  C CA  . PHE   C  1 260 ? -9.62557  30.59074  -10.07025 1.000 91.14406  ?  260 PHE   G CA  1 
ATOM   4621  C C   . PHE   C  1 260 ? -8.56550  31.66599  -9.99544  1.000 48.22222  ?  260 PHE   G C   1 
ATOM   4622  O O   . PHE   C  1 260 ? -8.21391  32.27734  -11.01284 1.000 124.56021 ?  260 PHE   G O   1 
ATOM   4623  C CB  . PHE   C  1 260 ? -10.77505 31.10450  -10.96411 1.000 43.72284  ?  260 PHE   G CB  1 
ATOM   4624  C CG  . PHE   C  1 260 ? -11.85002 30.09285  -11.22792 1.000 61.44774  ?  260 PHE   G CG  1 
ATOM   4625  C CD1 . PHE   C  1 260 ? -11.52819 28.76193  -11.42684 1.000 38.99575  ?  260 PHE   G CD1 1 
ATOM   4626  C CD2 . PHE   C  1 260 ? -13.18056 30.47202  -11.27352 1.000 54.61583  ?  260 PHE   G CD2 1 
ATOM   4627  C CE1 . PHE   C  1 260 ? -12.51081 27.81845  -11.66333 1.000 138.00934 ?  260 PHE   G CE1 1 
ATOM   4628  C CE2 . PHE   C  1 260 ? -14.17339 29.52929  -11.51356 1.000 56.15812  ?  260 PHE   G CE2 1 
ATOM   4629  C CZ  . PHE   C  1 260 ? -13.83289 28.19745  -11.70801 1.000 72.84036  ?  260 PHE   G CZ  1 
ATOM   4630  N N   . LYS   C  1 261 ? -7.98391  31.87670  -8.85265  1.000 60.22878  ?  261 LYS   G N   1 
ATOM   4631  C CA  . LYS   C  1 261 ? -6.86811  32.77546  -8.83369  1.000 96.36458  ?  261 LYS   G CA  1 
ATOM   4632  C C   . LYS   C  1 261 ? -5.62989  32.05691  -8.43173  1.000 61.85150  ?  261 LYS   G C   1 
ATOM   4633  O O   . LYS   C  1 261 ? -4.52956  32.52375  -8.75694  1.000 34.10355  ?  261 LYS   G O   1 
ATOM   4634  C CB  . LYS   C  1 261 ? -7.14031  33.94715  -7.89432  1.000 62.14331  ?  261 LYS   G CB  1 
ATOM   4635  C CG  . LYS   C  1 261 ? -7.56949  35.15089  -8.68281  1.000 67.39972  ?  261 LYS   G CG  1 
ATOM   4636  C CD  . LYS   C  1 261 ? -9.07012  35.15010  -8.96250  1.000 54.01683  ?  261 LYS   G CD  1 
ATOM   4637  C CE  . LYS   C  1 261 ? -9.80411  35.72741  -7.75357  1.000 76.82567  ?  261 LYS   G CE  1 
ATOM   4638  N NZ  . LYS   C  1 261 ? -11.24937 35.48096  -7.69630  1.000 58.68924  ?  261 LYS   G NZ  1 
ATOM   4639  N N   . GLY   C  1 262 ? -5.82079  30.86336  -7.86444  1.000 79.96487  ?  262 GLY   G N   1 
ATOM   4640  C CA  . GLY   C  1 262 ? -4.89610  30.07074  -7.07663  1.000 24.55860  ?  262 GLY   G CA  1 
ATOM   4641  C C   . GLY   C  1 262 ? -3.52302  30.68735  -7.01109  1.000 81.42022  ?  262 GLY   G C   1 
ATOM   4642  O O   . GLY   C  1 262 ? -3.05315  31.29429  -7.96820  1.000 74.74416  ?  262 GLY   G O   1 
ATOM   4643  N N   . GLU   C  1 263 ? -2.89278  30.56717  -5.85520  1.000 36.73617  ?  263 GLU   G N   1 
ATOM   4644  C CA  . GLU   C  1 263 ? -1.53108  31.08013  -5.68115  1.000 71.13833  ?  263 GLU   G CA  1 
ATOM   4645  C C   . GLU   C  1 263 ? -1.52401  32.60676  -5.70766  1.000 81.24420  ?  263 GLU   G C   1 
ATOM   4646  O O   . GLU   C  1 263 ? -0.56491  33.23868  -6.17784  1.000 46.07512  ?  263 GLU   G O   1 
ATOM   4647  C CB  . GLU   C  1 263 ? -0.55803  30.50092  -6.72926  1.000 35.15825  ?  263 GLU   G CB  1 
ATOM   4648  C CG  . GLU   C  1 263 ? 0.86260   30.24251  -6.24250  1.000 70.78948  ?  263 GLU   G CG  1 
ATOM   4649  C CD  . GLU   C  1 263 ? 0.97769   29.03756  -5.26882  1.000 64.03861  ?  263 GLU   G CD  1 
ATOM   4650  O OE1 . GLU   C  1 263 ? -0.07115  28.47072  -4.87289  1.000 34.38502  ?  263 GLU   G OE1 1 
ATOM   4651  O OE2 . GLU   C  1 263 ? 2.12370   28.65729  -4.89720  1.000 48.21872  -1 263 GLU   G OE2 1 
ATOM   4652  N N   . THR   C  1 264 ? -2.62435  33.18940  -5.22004  1.000 40.90379  ?  264 THR   G N   1 
ATOM   4653  C CA  . THR   C  1 264 ? -2.70796  34.59749  -4.87281  1.000 26.43291  ?  264 THR   G CA  1 
ATOM   4654  C C   . THR   C  1 264 ? -3.02387  34.71844  -3.39185  1.000 41.68163  ?  264 THR   G C   1 
ATOM   4655  O O   . THR   C  1 264 ? -3.86192  33.97696  -2.87191  1.000 32.76203  ?  264 THR   G O   1 
ATOM   4656  C CB  . THR   C  1 264 ? -3.80670  35.28891  -5.66006  1.000 47.27882  ?  264 THR   G CB  1 
ATOM   4657  O OG1 . THR   C  1 264 ? -3.64694  34.99416  -7.04933  1.000 98.34965  ?  264 THR   G OG1 1 
ATOM   4658  C CG2 . THR   C  1 264 ? -3.76965  36.79433  -5.40845  1.000 34.26652  ?  264 THR   G CG2 1 
ATOM   4659  N N   . TYR   C  1 265 ? -2.36225  35.64573  -2.70724  1.000 32.36131  ?  265 TYR   G N   1 
ATOM   4660  C CA  . TYR   C  1 265 ? -2.77037  35.93695  -1.33937  1.000 22.87557  ?  265 TYR   G CA  1 
ATOM   4661  C C   . TYR   C  1 265 ? -4.08698  36.70306  -1.32895  1.000 27.71430  ?  265 TYR   G C   1 
ATOM   4662  O O   . TYR   C  1 265 ? -4.39615  37.47311  -2.24899  1.000 35.73359  ?  265 TYR   G O   1 
ATOM   4663  C CB  . TYR   C  1 265 ? -1.72006  36.76400  -0.59311  1.000 18.95002  ?  265 TYR   G CB  1 
ATOM   4664  C CG  . TYR   C  1 265 ? -0.34811  36.14656  -0.52958  1.000 37.80822  ?  265 TYR   G CG  1 
ATOM   4665  C CD1 . TYR   C  1 265 ? -0.12078  34.98887  0.18709   1.000 29.15803  ?  265 TYR   G CD1 1 
ATOM   4666  C CD2 . TYR   C  1 265 ? 0.72397   36.74029  -1.17493  1.000 26.72116  ?  265 TYR   G CD2 1 
ATOM   4667  C CE1 . TYR   C  1 265 ? 1.15142   34.42758  0.25373   1.000 37.06883  ?  265 TYR   G CE1 1 
ATOM   4668  C CE2 . TYR   C  1 265 ? 1.98509   36.19503  -1.12270  1.000 35.30322  ?  265 TYR   G CE2 1 
ATOM   4669  C CZ  . TYR   C  1 265 ? 2.19732   35.03431  -0.40699  1.000 29.21425  ?  265 TYR   G CZ  1 
ATOM   4670  O OH  . TYR   C  1 265 ? 3.46263   34.49020  -0.36630  1.000 32.54588  ?  265 TYR   G OH  1 
ATOM   4671  N N   . SER   C  1 266 ? -4.86190  36.47802  -0.26446  1.000 26.34640  ?  266 SER   G N   1 
ATOM   4672  C CA  . SER   C  1 266 ? -6.00539  37.31203  0.09670   1.000 15.40467  ?  266 SER   G CA  1 
ATOM   4673  C C   . SER   C  1 266 ? -5.78681  37.74049  1.54724   1.000 28.91291  ?  266 SER   G C   1 
ATOM   4674  O O   . SER   C  1 266 ? -5.94441  36.92755  2.46569   1.000 19.45441  ?  266 SER   G O   1 
ATOM   4675  C CB  . SER   C  1 266 ? -7.32345  36.55992  -0.08843  1.000 17.16593  ?  266 SER   G CB  1 
ATOM   4676  O OG  . SER   C  1 266 ? -8.39464  37.26043  0.52219   1.000 27.71590  ?  266 SER   G OG  1 
ATOM   4677  N N   . LEU   C  1 267 ? -5.40553  39.00948  1.74807   1.000 22.40755  ?  267 LEU   G N   1 
ATOM   4678  C CA  . LEU   C  1 267 ? -5.07284  39.50048  3.08692   1.000 31.99322  ?  267 LEU   G CA  1 
ATOM   4679  C C   . LEU   C  1 267 ? -6.16606  39.17938  4.09746   1.000 21.77194  ?  267 LEU   G C   1 
ATOM   4680  O O   . LEU   C  1 267 ? -5.88523  38.69107  5.19854   1.000 37.36841  ?  267 LEU   G O   1 
ATOM   4681  C CB  . LEU   C  1 267 ? -4.84461  41.00588  3.05285   1.000 15.45093  ?  267 LEU   G CB  1 
ATOM   4682  C CG  . LEU   C  1 267 ? -3.51728  41.55057  2.56826   1.000 35.05132  ?  267 LEU   G CG  1 
ATOM   4683  C CD1 . LEU   C  1 267 ? -3.63895  43.02174  2.75432   1.000 27.12789  ?  267 LEU   G CD1 1 
ATOM   4684  C CD2 . LEU   C  1 267 ? -2.31627  40.98064  3.37230   1.000 21.41354  ?  267 LEU   G CD2 1 
ATOM   4685  N N   . LYS   C  1 268 ? -7.42333  39.48149  3.73730   1.000 45.32694  ?  268 LYS   G N   1 
ATOM   4686  C CA  . LYS   C  1 268 ? -8.57747  39.19505  4.59057   1.000 24.18258  ?  268 LYS   G CA  1 
ATOM   4687  C C   . LYS   C  1 268 ? -8.57073  37.73783  5.07374   1.000 43.11514  ?  268 LYS   G C   1 
ATOM   4688  O O   . LYS   C  1 268 ? -8.85700  37.46627  6.24630   1.000 22.23586  ?  268 LYS   G O   1 
ATOM   4689  C CB  . LYS   C  1 268 ? -9.85515  39.54161  3.80984   1.000 30.58953  ?  268 LYS   G CB  1 
ATOM   4690  C CG  . LYS   C  1 268 ? -11.17017 38.98139  4.32314   1.000 43.50447  ?  268 LYS   G CG  1 
ATOM   4691  C CD  . LYS   C  1 268 ? -12.20917 38.90130  3.17666   1.000 37.10550  ?  268 LYS   G CD  1 
ATOM   4692  C CE  . LYS   C  1 268 ? -13.52711 38.20850  3.64053   1.000 49.68892  ?  268 LYS   G CE  1 
ATOM   4693  N NZ  . LYS   C  1 268 ? -14.30272 37.62710  2.46413   1.000 46.47100  ?  268 LYS   G NZ  1 
ATOM   4694  N N   . HIS   C  1 269 ? -8.19689  36.79215  4.19779   1.000 26.01662  ?  269 HIS   G N   1 
ATOM   4695  C CA  . HIS   C  1 269 ? -8.12330  35.37995  4.57287   1.000 10.51897  ?  269 HIS   G CA  1 
ATOM   4696  C C   . HIS   C  1 269 ? -6.84525  35.07138  5.34296   1.000 35.44974  ?  269 HIS   G C   1 
ATOM   4697  O O   . HIS   C  1 269 ? -6.90252  34.56849  6.47139   1.000 18.18607  ?  269 HIS   G O   1 
ATOM   4698  C CB  . HIS   C  1 269 ? -8.19109  34.48724  3.33316   1.000 18.18123  ?  269 HIS   G CB  1 
ATOM   4699  C CG  . HIS   C  1 269 ? -9.51510  34.50192  2.64547   1.000 22.22816  ?  269 HIS   G CG  1 
ATOM   4700  N ND1 . HIS   C  1 269 ? -9.91275  35.52558  1.81439   1.000 43.59232  ?  269 HIS   G ND1 1 
ATOM   4701  C CD2 . HIS   C  1 269 ? -10.53406 33.61094  2.65813   1.000 29.50317  ?  269 HIS   G CD2 1 
ATOM   4702  C CE1 . HIS   C  1 269 ? -11.12431 35.26900  1.35170   1.000 18.81419  ?  269 HIS   G CE1 1 
ATOM   4703  N NE2 . HIS   C  1 269 ? -11.52395 34.11320  1.84887   1.000 34.36086  ?  269 HIS   G NE2 1 
ATOM   4704  N N   . LEU   C  1 270 ? -5.68072  35.33094  4.72226   1.000 22.47188  ?  270 LEU   G N   1 
ATOM   4705  C CA  . LEU   C  1 270 ? -4.38987  35.10848  5.38143   1.000 17.72673  ?  270 LEU   G CA  1 
ATOM   4706  C C   . LEU   C  1 270 ? -4.40744  35.59536  6.83223   1.000 21.41458  ?  270 LEU   G C   1 
ATOM   4707  O O   . LEU   C  1 270 ? -4.11069  34.82987  7.75948   1.000 24.97077  ?  270 LEU   G O   1 
ATOM   4708  C CB  . LEU   C  1 270 ? -3.27156  35.80428  4.59862   1.000 24.44810  ?  270 LEU   G CB  1 
ATOM   4709  C CG  . LEU   C  1 270 ? -1.86658  35.67657  5.18303   1.000 21.51046  ?  270 LEU   G CG  1 
ATOM   4710  C CD1 . LEU   C  1 270 ? -1.28076  34.26373  4.98928   1.000 19.24545  ?  270 LEU   G CD1 1 
ATOM   4711  C CD2 . LEU   C  1 270 ? -0.95612  36.74844  4.60455   1.000 27.24071  ?  270 LEU   G CD2 1 
ATOM   4712  N N   . LEU   C  1 271 ? -4.80879  36.85048  7.05293   1.000 28.52332  ?  271 LEU   G N   1 
ATOM   4713  C CA  . LEU   C  1 271 ? -4.82046  37.44039  8.38827   1.000 25.15022  ?  271 LEU   G CA  1 
ATOM   4714  C C   . LEU   C  1 271 ? -6.13222  37.22463  9.13144   1.000 33.58288  ?  271 LEU   G C   1 
ATOM   4715  O O   . LEU   C  1 271 ? -6.32366  37.81744  10.20157  1.000 23.14515  ?  271 LEU   G O   1 
ATOM   4716  C CB  . LEU   C  1 271 ? -4.51562  38.93722  8.31084   1.000 15.61300  ?  271 LEU   G CB  1 
ATOM   4717  C CG  . LEU   C  1 271 ? -3.19441  39.26128  7.60505   1.000 28.70237  ?  271 LEU   G CG  1 
ATOM   4718  C CD1 . LEU   C  1 271 ? -3.06569  40.76258  7.52247   1.000 19.81918  ?  271 LEU   G CD1 1 
ATOM   4719  C CD2 . LEU   C  1 271 ? -1.97652  38.61780  8.30039   1.000 13.34545  ?  271 LEU   G CD2 1 
ATOM   4720  N N   . ASN   C  1 272 ? -7.03980  36.40076  8.59234   1.000 19.82329  ?  272 ASN   G N   1 
ATOM   4721  C CA  . ASN   C  1 272 ? -8.24781  35.98016  9.31724   1.000 11.82378  ?  272 ASN   G CA  1 
ATOM   4722  C C   . ASN   C  1 272 ? -9.07944  37.18663  9.77428   1.000 23.96067  ?  272 ASN   G C   1 
ATOM   4723  O O   . ASN   C  1 272 ? -9.53913  37.25518  10.91309  1.000 30.75476  ?  272 ASN   G O   1 
ATOM   4724  C CB  . ASN   C  1 272 ? -7.87659  35.08225  10.50546  1.000 33.73390  ?  272 ASN   G CB  1 
ATOM   4725  C CG  . ASN   C  1 272 ? -9.07376  34.35876  11.10209  1.000 24.22489  ?  272 ASN   G CG  1 
ATOM   4726  O OD1 . ASN   C  1 272 ? -9.94570  33.84445  10.38423  1.000 24.02873  ?  272 ASN   G OD1 1 
ATOM   4727  N ND2 . ASN   C  1 272 ? -9.12142  34.31593  12.43210  1.000 30.45672  ?  272 ASN   G ND2 1 
ATOM   4728  N N   . ASN   C  1 273 ? -9.25331  38.15843  8.86774   1.000 20.56937  ?  273 ASN   G N   1 
ATOM   4729  C CA  . ASN   C  1 273 ? -10.08715 39.35076  9.09477   1.000 29.67576  ?  273 ASN   G CA  1 
ATOM   4730  C C   . ASN   C  1 273 ? -9.63555  40.17200  10.29643  1.000 17.68500  ?  273 ASN   G C   1 
ATOM   4731  O O   . ASN   C  1 273 ? -10.46408 40.78128  10.97490  1.000 26.48049  ?  273 ASN   G O   1 
ATOM   4732  C CB  . ASN   C  1 273 ? -11.56638 38.98539  9.25090   1.000 24.16492  ?  273 ASN   G CB  1 
ATOM   4733  C CG  . ASN   C  1 273 ? -12.25876 38.83672  7.92908   1.000 60.66845  ?  273 ASN   G CG  1 
ATOM   4734  O OD1 . ASN   C  1 273 ? -12.38818 39.81008  7.17669   1.000 66.10531  ?  273 ASN   G OD1 1 
ATOM   4735  N ND2 . ASN   C  1 273 ? -12.69627 37.61460  7.61795   1.000 63.32981  ?  273 ASN   G ND2 1 
ATOM   4736  N N   . ASP   C  1 274 ? -8.33128  40.22066  10.57074  1.000 33.17618  ?  274 ASP   G N   1 
ATOM   4737  C CA  . ASP   C  1 274 ? -7.87019  40.99966  11.71476  1.000 30.39476  ?  274 ASP   G CA  1 
ATOM   4738  C C   . ASP   C  1 274 ? -8.16263  42.48615  11.50156  1.000 24.79231  ?  274 ASP   G C   1 
ATOM   4739  O O   . ASP   C  1 274 ? -8.06444  42.98626  10.36945  1.000 25.62189  ?  274 ASP   G O   1 
ATOM   4740  C CB  . ASP   C  1 274 ? -6.37025  40.79664  11.94835  1.000 26.98561  ?  274 ASP   G CB  1 
ATOM   4741  C CG  . ASP   C  1 274 ? -5.92529  41.30510  13.30623  1.000 36.61640  ?  274 ASP   G CG  1 
ATOM   4742  O OD1 . ASP   C  1 274 ? -5.69021  42.53175  13.46113  1.000 45.08550  ?  274 ASP   G OD1 1 
ATOM   4743  O OD2 . ASP   C  1 274 ? -5.84933  40.47109  14.23687  1.000 58.80898  -1 274 ASP   G OD2 1 
ATOM   4744  N N   . PRO   C  1 275 ? -8.50442  43.22701  12.55911  1.000 36.03206  ?  275 PRO   G N   1 
ATOM   4745  C CA  . PRO   C  1 275 ? -8.59719  44.69615  12.42866  1.000 16.00506  ?  275 PRO   G CA  1 
ATOM   4746  C C   . PRO   C  1 275 ? -7.37465  45.35608  11.79690  1.000 25.60683  ?  275 PRO   G C   1 
ATOM   4747  O O   . PRO   C  1 275 ? -7.54886  46.37687  11.12357  1.000 38.92219  ?  275 PRO   G O   1 
ATOM   4748  C CB  . PRO   C  1 275 ? -8.81402  45.16457  13.87102  1.000 18.23098  ?  275 PRO   G CB  1 
ATOM   4749  C CG  . PRO   C  1 275 ? -9.43935  43.98235  14.55301  1.000 20.27738  ?  275 PRO   G CG  1 
ATOM   4750  C CD  . PRO   C  1 275 ? -8.88638  42.75013  13.89668  1.000 24.21439  ?  275 PRO   G CD  1 
ATOM   4751  N N   . PHE   C  1 276 ? -6.15440  44.80560  11.95117  1.000 32.65238  ?  276 PHE   G N   1 
ATOM   4752  C CA  . PHE   C  1 276 ? -4.98201  45.38374  11.27945  1.000 22.98485  ?  276 PHE   G CA  1 
ATOM   4753  C C   . PHE   C  1 276 ? -4.97197  45.16366  9.77010   1.000 40.07546  ?  276 PHE   G C   1 
ATOM   4754  O O   . PHE   C  1 276 ? -4.17204  45.80986  9.07833   1.000 35.93376  ?  276 PHE   G O   1 
ATOM   4755  C CB  . PHE   C  1 276 ? -3.67294  44.81722  11.83074  1.000 24.22310  ?  276 PHE   G CB  1 
ATOM   4756  C CG  . PHE   C  1 276 ? -3.41496  45.15488  13.26613  1.000 39.73551  ?  276 PHE   G CG  1 
ATOM   4757  C CD1 . PHE   C  1 276 ? -3.81792  46.36653  13.79520  1.000 32.74226  ?  276 PHE   G CD1 1 
ATOM   4758  C CD2 . PHE   C  1 276 ? -2.75802  44.25399  14.09010  1.000 29.80844  ?  276 PHE   G CD2 1 
ATOM   4759  C CE1 . PHE   C  1 276 ? -3.56159  46.67326  15.12483  1.000 44.52169  ?  276 PHE   G CE1 1 
ATOM   4760  C CE2 . PHE   C  1 276 ? -2.50300  44.54820  15.42286  1.000 48.33467  ?  276 PHE   G CE2 1 
ATOM   4761  C CZ  . PHE   C  1 276 ? -2.90826  45.75448  15.94187  1.000 38.82941  ?  276 PHE   G CZ  1 
ATOM   4762  N N   . THR   C  1 277 ? -5.81438  44.27018  9.24742   1.000 28.39321  ?  277 THR   G N   1 
ATOM   4763  C CA  . THR   C  1 277 ? -5.75538  43.91722  7.82779   1.000 34.11689  ?  277 THR   G CA  1 
ATOM   4764  C C   . THR   C  1 277 ? -5.68596  45.11967  6.89142   1.000 25.69410  ?  277 THR   G C   1 
ATOM   4765  O O   . THR   C  1 277 ? -4.85597  45.09870  5.97050   1.000 31.75522  ?  277 THR   G O   1 
ATOM   4766  C CB  . THR   C  1 277 ? -6.95393  43.02758  7.46307   1.000 22.86083  ?  277 THR   G CB  1 
ATOM   4767  O OG1 . THR   C  1 277 ? -7.01064  41.91519  8.36129   1.000 29.09747  ?  277 THR   G OG1 1 
ATOM   4768  C CG2 . THR   C  1 277 ? -6.81596  42.49798  6.04156   1.000 12.85645  ?  277 THR   G CG2 1 
ATOM   4769  N N   . PRO   C  1 278 ? -6.49231  46.17930  7.05631   1.000 52.83428  ?  278 PRO   G N   1 
ATOM   4770  C CA  . PRO   C  1 278 ? -6.42595  47.28954  6.08831   1.000 25.52637  ?  278 PRO   G CA  1 
ATOM   4771  C C   . PRO   C  1 278 ? -5.05583  47.94014  5.99115   1.000 39.53329  ?  278 PRO   G C   1 
ATOM   4772  O O   . PRO   C  1 278 ? -4.70564  48.43140  4.90854   1.000 28.09573  ?  278 PRO   G O   1 
ATOM   4773  C CB  . PRO   C  1 278 ? -7.47026  48.28510  6.61412   1.000 18.26156  ?  278 PRO   G CB  1 
ATOM   4774  C CG  . PRO   C  1 278 ? -8.35551  47.51720  7.47635   1.000 22.03643  ?  278 PRO   G CG  1 
ATOM   4775  C CD  . PRO   C  1 278 ? -7.53540  46.41132  8.07306   1.000 24.94636  ?  278 PRO   G CD  1 
ATOM   4776  N N   . GLN   C  1 279 ? -4.27128  47.95907  7.08471   1.000 28.30612  ?  279 GLN   G N   1 
ATOM   4777  C CA  . GLN   C  1 279 ? -2.94749  48.58868  7.06092   1.000 26.12029  ?  279 GLN   G CA  1 
ATOM   4778  C C   . GLN   C  1 279 ? -1.98791  47.91171  6.08221   1.000 39.52240  ?  279 GLN   G C   1 
ATOM   4779  O O   . GLN   C  1 279 ? -1.01034  48.54237  5.65064   1.000 37.91350  ?  279 GLN   G O   1 
ATOM   4780  C CB  . GLN   C  1 279 ? -2.31846  48.59005  8.46105   1.000 23.55793  ?  279 GLN   G CB  1 
ATOM   4781  C CG  . GLN   C  1 279 ? -3.08511  49.39149  9.51287   1.000 15.06050  ?  279 GLN   G CG  1 
ATOM   4782  C CD  . GLN   C  1 279 ? -2.31783  49.53666  10.81864  1.000 54.58665  ?  279 GLN   G CD  1 
ATOM   4783  O OE1 . GLN   C  1 279 ? -1.13980  49.91019  10.82957  1.000 40.41759  ?  279 GLN   G OE1 1 
ATOM   4784  N NE2 . GLN   C  1 279 ? -2.98670  49.24386  11.92753  1.000 31.44149  ?  279 GLN   G NE2 1 
ATOM   4785  N N   . PHE   C  1 280 ? -2.24025  46.64671  5.73196   1.000 27.93375  ?  280 PHE   G N   1 
ATOM   4786  C CA  . PHE   C  1 280 ? -1.36153  45.87539  4.86463   1.000 29.51156  ?  280 PHE   G CA  1 
ATOM   4787  C C   . PHE   C  1 280 ? -1.87622  45.80012  3.44403   1.000 27.83400  ?  280 PHE   G C   1 
ATOM   4788  O O   . PHE   C  1 280 ? -1.20672  45.20735  2.58367   1.000 30.50749  ?  280 PHE   G O   1 
ATOM   4789  C CB  . PHE   C  1 280 ? -1.14936  44.47104  5.44255   1.000 11.42529  ?  280 PHE   G CB  1 
ATOM   4790  C CG  . PHE   C  1 280 ? -0.31512  44.49024  6.66791   1.000 41.35113  ?  280 PHE   G CG  1 
ATOM   4791  C CD1 . PHE   C  1 280 ? 1.07567   44.47576  6.57963   1.000 22.05120  ?  280 PHE   G CD1 1 
ATOM   4792  C CD2 . PHE   C  1 280 ? -0.90768  44.63009  7.90982   1.000 12.37541  ?  280 PHE   G CD2 1 
ATOM   4793  C CE1 . PHE   C  1 280 ? 1.84747   44.54695  7.72332   1.000 36.76868  ?  280 PHE   G CE1 1 
ATOM   4794  C CE2 . PHE   C  1 280 ? -0.13525  44.70010  9.05859   1.000 36.07998  ?  280 PHE   G CE2 1 
ATOM   4795  C CZ  . PHE   C  1 280 ? 1.24268   44.66112  8.96316   1.000 28.45432  ?  280 PHE   G CZ  1 
ATOM   4796  N N   . GLU   C  1 281 ? -3.04189  46.39020  3.18323   1.000 31.92293  ?  281 GLU   G N   1 
ATOM   4797  C CA  . GLU   C  1 281 ? -3.52637  46.52563  1.82118   1.000 44.76711  ?  281 GLU   G CA  1 
ATOM   4798  C C   . GLU   C  1 281 ? -2.48603  47.26368  0.98005   1.000 22.01448  ?  281 GLU   G C   1 
ATOM   4799  O O   . GLU   C  1 281 ? -1.92735  48.27255  1.41907   1.000 41.71186  ?  281 GLU   G O   1 
ATOM   4800  C CB  . GLU   C  1 281 ? -4.86412  47.26451  1.83682   1.000 25.28252  ?  281 GLU   G CB  1 
ATOM   4801  C CG  . GLU   C  1 281 ? -5.81423  46.82202  0.75656   1.000 57.26031  ?  281 GLU   G CG  1 
ATOM   4802  C CD  . GLU   C  1 281 ? -6.39783  45.44440  1.00991   1.000 125.46736 ?  281 GLU   G CD  1 
ATOM   4803  O OE1 . GLU   C  1 281 ? -6.74596  45.10798  2.17571   1.000 44.61183  ?  281 GLU   G OE1 1 
ATOM   4804  O OE2 . GLU   C  1 281 ? -6.51264  44.69790  0.01653   1.000 60.58592  -1 281 GLU   G OE2 1 
ATOM   4805  N N   . HIS   C  1 282 ? -2.17873  46.71808  -0.20147  1.000 20.61994  ?  282 HIS   G N   1 
ATOM   4806  C CA  . HIS   C  1 282 ? -1.16942  47.21915  -1.13485  1.000 44.20533  ?  282 HIS   G CA  1 
ATOM   4807  C C   . HIS   C  1 282 ? 0.26353   46.98987  -0.66322  1.000 31.78696  ?  282 HIS   G C   1 
ATOM   4808  O O   . HIS   C  1 282 ? 1.19600   47.44266  -1.33573  1.000 37.01319  ?  282 HIS   G O   1 
ATOM   4809  C CB  . HIS   C  1 282 ? -1.32288  48.71571  -1.42236  1.000 11.71275  ?  282 HIS   G CB  1 
ATOM   4810  C CG  . HIS   C  1 282 ? -2.64339  49.08903  -2.01062  1.000 58.45192  ?  282 HIS   G CG  1 
ATOM   4811  N ND1 . HIS   C  1 282 ? -2.98982  48.79039  -3.31183  1.000 43.16241  ?  282 HIS   G ND1 1 
ATOM   4812  C CD2 . HIS   C  1 282 ? -3.70124  49.74641  -1.47795  1.000 18.72002  ?  282 HIS   G CD2 1 
ATOM   4813  C CE1 . HIS   C  1 282 ? -4.20912  49.23818  -3.55364  1.000 27.06120  ?  282 HIS   G CE1 1 
ATOM   4814  N NE2 . HIS   C  1 282 ? -4.66373  49.82332  -2.45734  1.000 39.02002  ?  282 HIS   G NE2 1 
ATOM   4815  N N   . GLY   C  1 283 ? 0.47541   46.31230  0.46800   1.000 41.31384  ?  283 GLY   G N   1 
ATOM   4816  C CA  . GLY   C  1 283 ? 1.81266   46.02841  0.95799   1.000 20.87163  ?  283 GLY   G CA  1 
ATOM   4817  C C   . GLY   C  1 283 ? 2.45811   44.85934  0.23712   1.000 33.04710  ?  283 GLY   G C   1 
ATOM   4818  O O   . GLY   C  1 283 ? 2.02495   44.48912  -0.86126  1.000 32.08925  ?  283 GLY   G O   1 
ATOM   4819  N N   . SER   C  1 284 ? 3.48546   44.25630  0.83411   1.000 23.04788  ?  284 SER   G N   1 
ATOM   4820  C CA  . SER   C  1 284 ? 4.20479   43.17584  0.16554   1.000 31.75361  ?  284 SER   G CA  1 
ATOM   4821  C C   . SER   C  1 284 ? 4.41816   42.02539  1.13456   1.000 25.76033  ?  284 SER   G C   1 
ATOM   4822  O O   . SER   C  1 284 ? 4.43495   42.20192  2.36204   1.000 18.69619  ?  284 SER   G O   1 
ATOM   4823  C CB  . SER   C  1 284 ? 5.55994   43.64908  -0.39889  1.000 14.79876  ?  284 SER   G CB  1 
ATOM   4824  O OG  . SER   C  1 284 ? 6.24987   44.43981  0.56952   1.000 33.51948  ?  284 SER   G OG  1 
ATOM   4825  N N   . ILE   C  1 285 ? 4.60518   40.83969  0.56003   1.000 24.74646  ?  285 ILE   G N   1 
ATOM   4826  C CA  . ILE   C  1 285 ? 4.72971   39.60216  1.31966   1.000 23.48866  ?  285 ILE   G CA  1 
ATOM   4827  C C   . ILE   C  1 285 ? 5.87569   38.78675  0.73441   1.000 19.64618  ?  285 ILE   G C   1 
ATOM   4828  O O   . ILE   C  1 285 ? 5.94124   38.58097  -0.48579  1.000 38.64104  ?  285 ILE   G O   1 
ATOM   4829  C CB  . ILE   C  1 285 ? 3.42542   38.77152  1.28660   1.000 26.89299  ?  285 ILE   G CB  1 
ATOM   4830  C CG1 . ILE   C  1 285 ? 2.26573   39.47748  2.00503   1.000 23.38257  ?  285 ILE   G CG1 1 
ATOM   4831  C CG2 . ILE   C  1 285 ? 3.67380   37.39532  1.84963   1.000 19.32521  ?  285 ILE   G CG2 1 
ATOM   4832  C CD1 . ILE   C  1 285 ? 0.91237   38.79489  1.78447   1.000 31.67199  ?  285 ILE   G CD1 1 
ATOM   4833  N N   . LEU   C  1 286 ? 6.76594   38.31646  1.60676   1.000 33.89338  ?  286 LEU   G N   1 
ATOM   4834  C CA  . LEU   C  1 286 ? 7.77654   37.31578  1.28734   1.000 16.76239  ?  286 LEU   G CA  1 
ATOM   4835  C C   . LEU   C  1 286 ? 7.41718   36.03204  2.02618   1.000 23.66235  ?  286 LEU   G C   1 
ATOM   4836  O O   . LEU   C  1 286 ? 7.14158   36.07020  3.23333   1.000 28.37727  ?  286 LEU   G O   1 
ATOM   4837  C CB  . LEU   C  1 286 ? 9.18453   37.79902  1.69429   1.000 31.94872  ?  286 LEU   G CB  1 
ATOM   4838  C CG  . LEU   C  1 286 ? 10.22689  36.68511  1.92729   1.000 27.61105  ?  286 LEU   G CG  1 
ATOM   4839  C CD1 . LEU   C  1 286 ? 10.58918  36.01818  0.62327   1.000 22.57120  ?  286 LEU   G CD1 1 
ATOM   4840  C CD2 . LEU   C  1 286 ? 11.48618  37.18436  2.61472   1.000 27.80876  ?  286 LEU   G CD2 1 
ATOM   4841  N N   . GLN   C  1 287 ? 7.42831   34.90309  1.31183   1.000 16.28552  ?  287 GLN   G N   1 
ATOM   4842  C CA  . GLN   C  1 287 ? 7.05410   33.61196  1.88217   1.000 30.34786  ?  287 GLN   G CA  1 
ATOM   4843  C C   . GLN   C  1 287 ? 8.15916   32.59030  1.63512   1.000 31.02794  ?  287 GLN   G C   1 
ATOM   4844  O O   . GLN   C  1 287 ? 8.64021   32.44152  0.50212   1.000 24.59552  ?  287 GLN   G O   1 
ATOM   4845  C CB  . GLN   C  1 287 ? 5.72309   33.09781  1.30025   1.000 19.39154  ?  287 GLN   G CB  1 
ATOM   4846  C CG  . GLN   C  1 287 ? 5.32431   31.72210  1.81194   1.000 27.30111  ?  287 GLN   G CG  1 
ATOM   4847  C CD  . GLN   C  1 287 ? 3.91859   31.28941  1.40515   1.000 24.56126  ?  287 GLN   G CD  1 
ATOM   4848  O OE1 . GLN   C  1 287 ? 3.24535   31.95076  0.61066   1.000 26.69986  ?  287 GLN   G OE1 1 
ATOM   4849  N NE2 . GLN   C  1 287 ? 3.47028   30.15892  1.95688   1.000 20.67709  ?  287 GLN   G NE2 1 
ATOM   4850  N N   . GLY   C  1 288 ? 8.54756   31.87989  2.69572   1.000 27.16921  ?  288 GLY   G N   1 
ATOM   4851  C CA  . GLY   C  1 288 ? 9.54161   30.82225  2.61092   1.000 18.99847  ?  288 GLY   G CA  1 
ATOM   4852  C C   . GLY   C  1 288 ? 8.99890   29.42862  2.91087   1.000 23.61625  ?  288 GLY   G C   1 
ATOM   4853  O O   . GLY   C  1 288 ? 7.95359   29.26104  3.55222   1.000 38.65330  ?  288 GLY   G O   1 
ATOM   4854  N N   . PHE   C  1 289 ? 9.70372   28.41344  2.43044   1.000 28.65666  ?  289 PHE   G N   1 
ATOM   4855  C CA  . PHE   C  1 289 ? 9.36508   27.01868  2.66549   1.000 35.20944  ?  289 PHE   G CA  1 
ATOM   4856  C C   . PHE   C  1 289 ? 10.50420  26.37282  3.43751   1.000 30.50949  ?  289 PHE   G C   1 
ATOM   4857  O O   . PHE   C  1 289 ? 11.66773  26.51729  3.05393   1.000 32.90242  ?  289 PHE   G O   1 
ATOM   4858  C CB  . PHE   C  1 289 ? 9.14023   26.29544  1.33799   1.000 24.25006  ?  289 PHE   G CB  1 
ATOM   4859  C CG  . PHE   C  1 289 ? 9.15084   24.79197  1.44189   1.000 29.93360  ?  289 PHE   G CG  1 
ATOM   4860  C CD1 . PHE   C  1 289 ? 8.21668   24.12791  2.22519   1.000 18.72077  ?  289 PHE   G CD1 1 
ATOM   4861  C CD2 . PHE   C  1 289 ? 10.07410  24.03716  0.73384   1.000 29.37422  ?  289 PHE   G CD2 1 
ATOM   4862  C CE1 . PHE   C  1 289 ? 8.20772   22.72380  2.30814   1.000 37.36342  ?  289 PHE   G CE1 1 
ATOM   4863  C CE2 . PHE   C  1 289 ? 10.06618  22.63973  0.80998   1.000 32.72960  ?  289 PHE   G CE2 1 
ATOM   4864  C CZ  . PHE   C  1 289 ? 9.12693   21.98452  1.59608   1.000 31.02939  ?  289 PHE   G CZ  1 
ATOM   4865  N N   . LEU   C  1 290 ? 10.16979  25.67765  4.52367   1.000 25.97230  ?  290 LEU   G N   1 
ATOM   4866  C CA  . LEU   C  1 290 ? 11.14379  24.95244  5.33195   1.000 25.34264  ?  290 LEU   G CA  1 
ATOM   4867  C C   . LEU   C  1 290 ? 11.15287  23.48076  4.90998   1.000 29.71069  ?  290 LEU   G C   1 
ATOM   4868  O O   . LEU   C  1 290 ? 10.11641  22.81486  4.99247   1.000 49.33630  ?  290 LEU   G O   1 
ATOM   4869  C CB  . LEU   C  1 290 ? 10.80001  25.08674  6.81878   1.000 18.47996  ?  290 LEU   G CB  1 
ATOM   4870  C CG  . LEU   C  1 290 ? 10.87416  26.43372  7.56530   1.000 26.23373  ?  290 LEU   G CG  1 
ATOM   4871  C CD1 . LEU   C  1 290 ? 9.74383   27.37838  7.17434   1.000 23.88119  ?  290 LEU   G CD1 1 
ATOM   4872  C CD2 . LEU   C  1 290 ? 10.89439  26.24937  9.09692   1.000 18.30362  ?  290 LEU   G CD2 1 
ATOM   4873  N N   . ASN   C  1 291 ? 12.31239  22.97015  4.46165   1.000 42.42031  ?  291 ASN   G N   1 
ATOM   4874  C CA  . ASN   C  1 291 ? 12.45441  21.53467  4.16164   1.000 29.84130  ?  291 ASN   G CA  1 
ATOM   4875  C C   . ASN   C  1 291 ? 12.23645  20.70322  5.41554   1.000 34.36152  ?  291 ASN   G C   1 
ATOM   4876  O O   . ASN   C  1 291 ? 12.29129  21.20273  6.54639   1.000 33.97942  ?  291 ASN   G O   1 
ATOM   4877  C CB  . ASN   C  1 291 ? 13.84617  21.17104  3.62615   1.000 56.89989  ?  291 ASN   G CB  1 
ATOM   4878  C CG  . ASN   C  1 291 ? 14.41935  22.22516  2.73453   1.000 67.86947  ?  291 ASN   G CG  1 
ATOM   4879  O OD1 . ASN   C  1 291 ? 14.96067  23.22908  3.20809   1.000 113.67200 ?  291 ASN   G OD1 1 
ATOM   4880  N ND2 . ASN   C  1 291 ? 14.30880  22.01417  1.42918   1.000 68.58516  ?  291 ASN   G ND2 1 
ATOM   4881  N N   . VAL   C  1 292 ? 12.03258  19.39953  5.21025   1.000 30.02451  ?  292 VAL   G N   1 
ATOM   4882  C CA  . VAL   C  1 292 ? 11.74821  18.55720  6.36424   1.000 57.99659  ?  292 VAL   G CA  1 
ATOM   4883  C C   . VAL   C  1 292 ? 12.96328  18.45359  7.28025   1.000 58.73747  ?  292 VAL   G C   1 
ATOM   4884  O O   . VAL   C  1 292 ? 12.81304  18.26208  8.49549   1.000 41.11242  ?  292 VAL   G O   1 
ATOM   4885  C CB  . VAL   C  1 292 ? 11.25448  17.17435  5.92100   1.000 56.31656  ?  292 VAL   G CB  1 
ATOM   4886  C CG1 . VAL   C  1 292 ? 10.47052  16.53686  7.06790   1.000 49.17492  ?  292 VAL   G CG1 1 
ATOM   4887  C CG2 . VAL   C  1 292 ? 10.41596  17.29126  4.63049   1.000 41.09416  ?  292 VAL   G CG2 1 
ATOM   4888  N N   . THR   C  1 293 ? 14.17459  18.61123  6.73764   1.000 28.22800  ?  293 THR   G N   1 
ATOM   4889  C CA  . THR   C  1 293 ? 15.39673  18.53458  7.53372   1.000 34.61686  ?  293 THR   G CA  1 
ATOM   4890  C C   . THR   C  1 293 ? 15.88590  19.88614  8.06211   1.000 61.87903  ?  293 THR   G C   1 
ATOM   4891  O O   . THR   C  1 293 ? 16.98575  19.94836  8.62458   1.000 49.12876  ?  293 THR   G O   1 
ATOM   4892  C CB  . THR   C  1 293 ? 16.52947  17.91590  6.71398   1.000 59.18866  ?  293 THR   G CB  1 
ATOM   4893  O OG1 . THR   C  1 293 ? 16.73699  18.68562  5.51026   1.000 37.21231  ?  293 THR   G OG1 1 
ATOM   4894  C CG2 . THR   C  1 293 ? 16.21388  16.47530  6.38730   1.000 27.88595  ?  293 THR   G CG2 1 
ATOM   4895  N N   . ALA   C  1 294 ? 15.12202  20.96223  7.88986   1.000 38.63559  ?  294 ALA   G N   1 
ATOM   4896  C CA  . ALA   C  1 294 ? 15.61635  22.27862  8.26338   1.000 31.99216  ?  294 ALA   G CA  1 
ATOM   4897  C C   . ALA   C  1 294 ? 15.41248  22.56137  9.75672   1.000 31.44084  ?  294 ALA   G C   1 
ATOM   4898  O O   . ALA   C  1 294 ? 14.62435  21.91865  10.45743  1.000 48.91593  ?  294 ALA   G O   1 
ATOM   4899  C CB  . ALA   C  1 294 ? 14.94661  23.37351  7.42665   1.000 30.34053  ?  294 ALA   G CB  1 
ATOM   4900  N N   . TYR   C  1 295 ? 16.19298  23.51159  10.24595  1.000 27.54775  ?  295 TYR   G N   1 
ATOM   4901  C CA  . TYR   C  1 295 ? 15.94084  24.09240  11.54944  1.000 34.99451  ?  295 TYR   G CA  1 
ATOM   4902  C C   . TYR   C  1 295 ? 14.51182  24.63009  11.56991  1.000 32.92121  ?  295 TYR   G C   1 
ATOM   4903  O O   . TYR   C  1 295 ? 14.08587  25.32135  10.64087  1.000 29.84632  ?  295 TYR   G O   1 
ATOM   4904  C CB  . TYR   C  1 295 ? 16.98666  25.18611  11.77316  1.000 8.20515   ?  295 TYR   G CB  1 
ATOM   4905  C CG  . TYR   C  1 295 ? 16.89916  26.02782  13.02436  1.000 37.99937  ?  295 TYR   G CG  1 
ATOM   4906  C CD1 . TYR   C  1 295 ? 17.54155  25.63914  14.21217  1.000 26.25364  ?  295 TYR   G CD1 1 
ATOM   4907  C CD2 . TYR   C  1 295 ? 16.24964  27.25556  12.99721  1.000 22.11708  ?  295 TYR   G CD2 1 
ATOM   4908  C CE1 . TYR   C  1 295 ? 17.48785  26.44641  15.35993  1.000 19.15179  ?  295 TYR   G CE1 1 
ATOM   4909  C CE2 . TYR   C  1 295 ? 16.18802  28.06108  14.11782  1.000 17.17465  ?  295 TYR   G CE2 1 
ATOM   4910  C CZ  . TYR   C  1 295 ? 16.80674  27.66188  15.30240  1.000 31.46283  ?  295 TYR   G CZ  1 
ATOM   4911  O OH  . TYR   C  1 295 ? 16.73150  28.48060  16.41781  1.000 22.46927  ?  295 TYR   G OH  1 
ATOM   4912  N N   . HIS   C  1 296 ? 13.74153  24.27645  12.59900  1.000 31.32859  ?  296 HIS   G N   1 
ATOM   4913  C CA  . HIS   C  1 296 ? 12.31565  24.60055  12.59900  1.000 39.55684  ?  296 HIS   G CA  1 
ATOM   4914  C C   . HIS   C  1 296 ? 11.90178  25.57945  13.69970  1.000 24.14541  ?  296 HIS   G C   1 
ATOM   4915  O O   . HIS   C  1 296 ? 10.71079  25.64330  14.04652  1.000 30.04598  ?  296 HIS   G O   1 
ATOM   4916  C CB  . HIS   C  1 296 ? 11.47204  23.31908  12.67073  1.000 28.54391  ?  296 HIS   G CB  1 
ATOM   4917  C CG  . HIS   C  1 296 ? 11.00604  22.84626  11.32349  1.000 38.43770  ?  296 HIS   G CG  1 
ATOM   4918  N ND1 . HIS   C  1 296 ? 11.81289  22.12819  10.46749  1.000 46.25360  ?  296 HIS   G ND1 1 
ATOM   4919  C CD2 . HIS   C  1 296 ? 9.84150   23.04495  10.65993  1.000 37.88401  ?  296 HIS   G CD2 1 
ATOM   4920  C CE1 . HIS   C  1 296 ? 11.16200  21.89096  9.34286   1.000 38.28608  ?  296 HIS   G CE1 1 
ATOM   4921  N NE2 . HIS   C  1 296 ? 9.96147   22.43392  9.43471   1.000 52.19227  ?  296 HIS   G NE2 1 
ATOM   4922  N N   . ARG   C  1 297 ? 12.83332  26.36463  14.23967  1.000 24.97448  ?  297 ARG   G N   1 
ATOM   4923  C CA  . ARG   C  1 297 ? 12.43194  27.39478  15.18852  1.000 20.39935  ?  297 ARG   G CA  1 
ATOM   4924  C C   . ARG   C  1 297 ? 12.23819  28.72473  14.47005  1.000 37.37663  ?  297 ARG   G C   1 
ATOM   4925  O O   . ARG   C  1 297 ? 12.63839  28.89467  13.31552  1.000 27.02274  ?  297 ARG   G O   1 
ATOM   4926  C CB  . ARG   C  1 297 ? 13.45231  27.54408  16.30474  1.000 24.28065  ?  297 ARG   G CB  1 
ATOM   4927  C CG  . ARG   C  1 297 ? 13.84783  26.23990  16.94806  1.000 29.29996  ?  297 ARG   G CG  1 
ATOM   4928  C CD  . ARG   C  1 297 ? 14.76582  26.52935  18.11912  1.000 26.16367  ?  297 ARG   G CD  1 
ATOM   4929  N NE  . ARG   C  1 297 ? 14.39798  25.73156  19.28230  1.000 43.67063  ?  297 ARG   G NE  1 
ATOM   4930  C CZ  . ARG   C  1 297 ? 13.86002  26.23602  20.38179  1.000 35.99104  ?  297 ARG   G CZ  1 
ATOM   4931  N NH1 . ARG   C  1 297 ? 13.67353  27.54460  20.51983  1.000 44.36621  ?  297 ARG   G NH1 1 
ATOM   4932  N NH2 . ARG   C  1 297 ? 13.50735  25.41169  21.36684  1.000 79.66820  ?  297 ARG   G NH2 1 
ATOM   4933  N N   . TRP   C  1 298 ? 11.58469  29.66178  15.16278  1.000 28.72093  ?  298 TRP   G N   1 
ATOM   4934  C CA  . TRP   C  1 298 ? 11.32297  30.99783  14.65181  1.000 26.56930  ?  298 TRP   G CA  1 
ATOM   4935  C C   . TRP   C  1 298 ? 12.20107  31.99944  15.38792  1.000 34.48907  ?  298 TRP   G C   1 
ATOM   4936  O O   . TRP   C  1 298 ? 12.33234  31.94199  16.61678  1.000 38.52676  ?  298 TRP   G O   1 
ATOM   4937  C CB  . TRP   C  1 298 ? 9.85737   31.42103  14.84096  1.000 20.74820  ?  298 TRP   G CB  1 
ATOM   4938  C CG  . TRP   C  1 298 ? 8.79762   30.39837  14.54335  1.000 31.47964  ?  298 TRP   G CG  1 
ATOM   4939  C CD1 . TRP   C  1 298 ? 8.88925   29.31072  13.70876  1.000 26.75007  ?  298 TRP   G CD1 1 
ATOM   4940  C CD2 . TRP   C  1 298 ? 7.46569   30.37498  15.08794  1.000 20.86211  ?  298 TRP   G CD2 1 
ATOM   4941  N NE1 . TRP   C  1 298 ? 7.69877   28.60762  13.71753  1.000 18.15900  ?  298 TRP   G NE1 1 
ATOM   4942  C CE2 . TRP   C  1 298 ? 6.81075   29.24687  14.54749  1.000 24.45695  ?  298 TRP   G CE2 1 
ATOM   4943  C CE3 . TRP   C  1 298 ? 6.77273   31.19014  15.99538  1.000 13.92506  ?  298 TRP   G CE3 1 
ATOM   4944  C CZ2 . TRP   C  1 298 ? 5.49537   28.91919  14.88319  1.000 29.58250  ?  298 TRP   G CZ2 1 
ATOM   4945  C CZ3 . TRP   C  1 298 ? 5.47486   30.86987  16.31852  1.000 35.82864  ?  298 TRP   G CZ3 1 
ATOM   4946  C CH2 . TRP   C  1 298 ? 4.84608   29.74312  15.76496  1.000 27.38402  ?  298 TRP   G CH2 1 
ATOM   4947  N N   . HIS   C  1 299 ? 12.76197  32.93912  14.63834  1.000 27.86344  ?  299 HIS   G N   1 
ATOM   4948  C CA  . HIS   C  1 299 ? 13.53830  34.03340  15.19464  1.000 36.74150  ?  299 HIS   G CA  1 
ATOM   4949  C C   . HIS   C  1 299 ? 12.84186  35.35492  14.90168  1.000 26.89652  ?  299 HIS   G C   1 
ATOM   4950  O O   . HIS   C  1 299 ? 12.12802  35.48592  13.90078  1.000 28.99012  ?  299 HIS   G O   1 
ATOM   4951  C CB  . HIS   C  1 299 ? 14.96550  34.06837  14.62584  1.000 16.07386  ?  299 HIS   G CB  1 
ATOM   4952  C CG  . HIS   C  1 299 ? 15.81550  32.90599  15.04184  1.000 32.99237  ?  299 HIS   G CG  1 
ATOM   4953  N ND1 . HIS   C  1 299 ? 17.12613  32.75716  14.63888  1.000 26.03713  ?  299 HIS   G ND1 1 
ATOM   4954  C CD2 . HIS   C  1 299 ? 15.53355  31.83004  15.81429  1.000 26.33907  ?  299 HIS   G CD2 1 
ATOM   4955  C CE1 . HIS   C  1 299 ? 17.61397  31.63937  15.14723  1.000 39.76735  ?  299 HIS   G CE1 1 
ATOM   4956  N NE2 . HIS   C  1 299 ? 16.66696  31.05873  15.86472  1.000 28.12828  ?  299 HIS   G NE2 1 
ATOM   4957  N N   . ALA   C  1 300 ? 13.06710  36.33829  15.78044  1.000 23.36592  ?  300 ALA   G N   1 
ATOM   4958  C CA  . ALA   C  1 300 ? 12.44370  37.65038  15.61674  1.000 28.40143  ?  300 ALA   G CA  1 
ATOM   4959  C C   . ALA   C  1 300 ? 13.07754  38.38278  14.44054  1.000 21.38633  ?  300 ALA   G C   1 
ATOM   4960  O O   . ALA   C  1 300 ? 14.30901  38.47821  14.36795  1.000 31.58638  ?  300 ALA   G O   1 
ATOM   4961  C CB  . ALA   C  1 300 ? 12.59206  38.47784  16.88696  1.000 16.94087  ?  300 ALA   G CB  1 
ATOM   4962  N N   . PRO   C  1 301 ? 12.28180  38.89954  13.49765  1.000 35.47138  ?  301 PRO   G N   1 
ATOM   4963  C CA  . PRO   C  1 301 ? 12.86035  39.55055  12.30639  1.000 21.31215  ?  301 PRO   G CA  1 
ATOM   4964  C C   . PRO   C  1 301 ? 13.30965  40.98865  12.53316  1.000 42.09847  ?  301 PRO   G C   1 
ATOM   4965  O O   . PRO   C  1 301 ? 14.01770  41.53786  11.67594  1.000 26.49806  ?  301 PRO   G O   1 
ATOM   4966  C CB  . PRO   C  1 301 ? 11.71042  39.48476  11.28643  1.000 30.20991  ?  301 PRO   G CB  1 
ATOM   4967  C CG  . PRO   C  1 301 ? 10.46962  39.50735  12.13061  1.000 27.45948  ?  301 PRO   G CG  1 
ATOM   4968  C CD  . PRO   C  1 301 ? 10.80967  38.82068  13.44663  1.000 12.76947  ?  301 PRO   G CD  1 
ATOM   4969  N N   . VAL   C  1 302 ? 12.91877  41.60686  13.65246  1.000 18.16700  ?  302 VAL   G N   1 
ATOM   4970  C CA  . VAL   C  1 302 ? 13.24375  42.99421  13.97466  1.000 42.99931  ?  302 VAL   G CA  1 
ATOM   4971  C C   . VAL   C  1 302 ? 13.36350  43.12551  15.48787  1.000 17.41206  ?  302 VAL   G C   1 
ATOM   4972  O O   . VAL   C  1 302 ? 12.89540  42.27381  16.24436  1.000 34.08415  ?  302 VAL   G O   1 
ATOM   4973  C CB  . VAL   C  1 302 ? 12.17125  43.98989  13.46666  1.000 17.16987  ?  302 VAL   G CB  1 
ATOM   4974  C CG1 . VAL   C  1 302 ? 12.07717  43.96534  11.95158  1.000 41.43715  ?  302 VAL   G CG1 1 
ATOM   4975  C CG2 . VAL   C  1 302 ? 10.81254  43.69790  14.13480  1.000 15.85762  ?  302 VAL   G CG2 1 
ATOM   4976  N N   . ASN   C  1 303 ? 13.99288  44.21194  15.93390  1.000 35.57489  ?  303 ASN   G N   1 
ATOM   4977  C CA  . ASN   C  1 303 ? 13.80395  44.64650  17.31342  1.000 20.44672  ?  303 ASN   G CA  1 
ATOM   4978  C C   . ASN   C  1 303 ? 12.41513  45.25922  17.42704  1.000 39.74938  ?  303 ASN   G C   1 
ATOM   4979  O O   . ASN   C  1 303 ? 12.05904  46.15292  16.64605  1.000 35.25132  ?  303 ASN   G O   1 
ATOM   4980  C CB  . ASN   C  1 303 ? 14.85604  45.67805  17.72819  1.000 39.27395  ?  303 ASN   G CB  1 
ATOM   4981  C CG  . ASN   C  1 303 ? 16.28758  45.20508  17.50592  1.000 32.01309  ?  303 ASN   G CG  1 
ATOM   4982  O OD1 . ASN   C  1 303 ? 16.56239  44.02192  17.26849  1.000 36.72034  ?  303 ASN   G OD1 1 
ATOM   4983  N ND2 . ASN   C  1 303 ? 17.21266  46.14575  17.58828  1.000 34.77302  ?  303 ASN   G ND2 1 
ATOM   4984  N N   . GLY   C  1 304 ? 11.61345  44.77642  18.36799  1.000 30.67180  ?  304 GLY   G N   1 
ATOM   4985  C CA  . GLY   C  1 304 ? 10.28023  45.33115  18.46947  1.000 17.44402  ?  304 GLY   G CA  1 
ATOM   4986  C C   . GLY   C  1 304 ? 9.46447   44.66539  19.55003  1.000 33.97056  ?  304 GLY   G C   1 
ATOM   4987  O O   . GLY   C  1 304 ? 9.96825   43.86767  20.34948  1.000 36.78629  ?  304 GLY   G O   1 
ATOM   4988  N N   . THR   C  1 305 ? 8.17895   45.00790  19.54258  1.000 29.05717  ?  305 THR   G N   1 
ATOM   4989  C CA  . THR   C  1 305 ? 7.22387   44.55126  20.54154  1.000 30.35597  ?  305 THR   G CA  1 
ATOM   4990  C C   . THR   C  1 305 ? 6.18571   43.63805  19.89874  1.000 52.28840  ?  305 THR   G C   1 
ATOM   4991  O O   . THR   C  1 305 ? 5.68107   43.92276  18.79998  1.000 17.16198  ?  305 THR   G O   1 
ATOM   4992  C CB  . THR   C  1 305 ? 6.52844   45.74504  21.19938  1.000 19.97584  ?  305 THR   G CB  1 
ATOM   4993  O OG1 . THR   C  1 305 ? 7.50548   46.75802  21.47032  1.000 37.04729  ?  305 THR   G OG1 1 
ATOM   4994  C CG2 . THR   C  1 305 ? 5.85621   45.31724  22.49293  1.000 19.76291  ?  305 THR   G CG2 1 
ATOM   4995  N N   . ILE   C  1 306 ? 5.87683   42.53558  20.57937  1.000 16.99831  ?  306 ILE   G N   1 
ATOM   4996  C CA  . ILE   C  1 306 ? 4.83168   41.64294  20.10013  1.000 29.82366  ?  306 ILE   G CA  1 
ATOM   4997  C C   . ILE   C  1 306 ? 3.50242   42.33187  20.34401  1.000 30.46286  ?  306 ILE   G C   1 
ATOM   4998  O O   . ILE   C  1 306 ? 3.14201   42.61334  21.49159  1.000 33.51822  ?  306 ILE   G O   1 
ATOM   4999  C CB  . ILE   C  1 306 ? 4.88644   40.28446  20.80881  1.000 26.09266  ?  306 ILE   G CB  1 
ATOM   5000  C CG1 . ILE   C  1 306 ? 6.30830   39.70371  20.79133  1.000 13.49536  ?  306 ILE   G CG1 1 
ATOM   5001  C CG2 . ILE   C  1 306 ? 3.85998   39.33007  20.18622  1.000 21.78647  ?  306 ILE   G CG2 1 
ATOM   5002  C CD1 . ILE   C  1 306 ? 6.94155   39.57387  19.40145  1.000 20.25303  ?  306 ILE   G CD1 1 
ATOM   5003  N N   . VAL   C  1 307 ? 2.78433   42.63521  19.27170  1.000 26.79039  ?  307 VAL   G N   1 
ATOM   5004  C CA  . VAL   C  1 307 ? 1.52031   43.33518  19.42191  1.000 20.67540  ?  307 VAL   G CA  1 
ATOM   5005  C C   . VAL   C  1 307 ? 0.37176   42.36199  19.66138  1.000 29.39263  ?  307 VAL   G C   1 
ATOM   5006  O O   . VAL   C  1 307 ? -0.46456  42.59850  20.53757  1.000 27.89614  ?  307 VAL   G O   1 
ATOM   5007  C CB  . VAL   C  1 307 ? 1.26021   44.23224  18.19913  1.000 36.59801  ?  307 VAL   G CB  1 
ATOM   5008  C CG1 . VAL   C  1 307 ? -0.06512  44.95752  18.35776  1.000 10.57300  ?  307 VAL   G CG1 1 
ATOM   5009  C CG2 . VAL   C  1 307 ? 2.40434   45.22565  17.99884  1.000 21.64445  ?  307 VAL   G CG2 1 
ATOM   5010  N N   . LYS   C  1 308 ? 0.34688   41.24308  18.93165  1.000 41.01391  ?  308 LYS   G N   1 
ATOM   5011  C CA  . LYS   C  1 308 ? -0.83013  40.37969  18.88293  1.000 31.63285  ?  308 LYS   G CA  1 
ATOM   5012  C C   . LYS   C  1 308 ? -0.45422  39.03113  18.28673  1.000 45.15649  ?  308 LYS   G C   1 
ATOM   5013  O O   . LYS   C  1 308 ? 0.19836   38.97477  17.23649  1.000 28.32674  ?  308 LYS   G O   1 
ATOM   5014  C CB  . LYS   C  1 308 ? -1.92274  41.03227  18.04004  1.000 28.44890  ?  308 LYS   G CB  1 
ATOM   5015  C CG  . LYS   C  1 308 ? -3.32926  40.48119  18.19316  1.000 19.79001  ?  308 LYS   G CG  1 
ATOM   5016  C CD  . LYS   C  1 308 ? -4.17324  41.17313  17.11999  1.000 30.64744  ?  308 LYS   G CD  1 
ATOM   5017  C CE  . LYS   C  1 308 ? -5.67242  41.11133  17.37567  1.000 50.59053  ?  308 LYS   G CE  1 
ATOM   5018  N NZ  . LYS   C  1 308 ? -6.32642  42.12387  16.47240  1.000 62.23640  ?  308 LYS   G NZ  1 
ATOM   5019  N N   . ILE   C  1 309 ? -0.88031  37.95698  18.94933  1.000 25.97052  ?  309 ILE   G N   1 
ATOM   5020  C CA  . ILE   C  1 309 ? -0.67058  36.58704  18.49534  1.000 33.04894  ?  309 ILE   G CA  1 
ATOM   5021  C C   . ILE   C  1 309 ? -2.03958  35.94084  18.35638  1.000 25.49669  ?  309 ILE   G C   1 
ATOM   5022  O O   . ILE   C  1 309 ? -2.79835  35.89988  19.33091  1.000 34.07166  ?  309 ILE   G O   1 
ATOM   5023  C CB  . ILE   C  1 309 ? 0.18715   35.78042  19.47719  1.000 17.49932  ?  309 ILE   G CB  1 
ATOM   5024  C CG1 . ILE   C  1 309 ? 1.55509   36.41635  19.67285  1.000 38.18931  ?  309 ILE   G CG1 1 
ATOM   5025  C CG2 . ILE   C  1 309 ? 0.31295   34.33931  18.99126  1.000 20.15438  ?  309 ILE   G CG2 1 
ATOM   5026  C CD1 . ILE   C  1 309 ? 2.27726   35.85593  20.86539  1.000 18.88686  ?  309 ILE   G CD1 1 
ATOM   5027  N N   . ILE   C  1 310 ? -2.35524  35.42811  17.16216  1.000 26.49516  ?  310 ILE   G N   1 
ATOM   5028  C CA  . ILE   C  1 310 ? -3.64857  34.80393  16.89899  1.000 10.37305  ?  310 ILE   G CA  1 
ATOM   5029  C C   . ILE   C  1 310 ? -3.43384  33.40723  16.34077  1.000 27.78482  ?  310 ILE   G C   1 
ATOM   5030  O O   . ILE   C  1 310 ? -2.69963  33.22975  15.36046  1.000 20.77901  ?  310 ILE   G O   1 
ATOM   5031  C CB  . ILE   C  1 310 ? -4.50379  35.61452  15.91174  1.000 27.76241  ?  310 ILE   G CB  1 
ATOM   5032  C CG1 . ILE   C  1 310 ? -4.57863  37.07971  16.32793  1.000 28.85314  ?  310 ILE   G CG1 1 
ATOM   5033  C CG2 . ILE   C  1 310 ? -5.87315  34.98416  15.81388  1.000 15.19843  ?  310 ILE   G CG2 1 
ATOM   5034  C CD1 . ILE   C  1 310 ? -3.93326  38.01355  15.32732  1.000 33.22443  ?  310 ILE   G CD1 1 
ATOM   5035  N N   . ASN   C  1 311 ? -4.11362  32.42519  16.91962  1.000 26.07695  ?  311 ASN   G N   1 
ATOM   5036  C CA  . ASN   C  1 311 ? -4.03122  31.05895  16.42606  1.000 22.88913  ?  311 ASN   G CA  1 
ATOM   5037  C C   . ASN   C  1 311 ? -5.30232  30.72830  15.66199  1.000 12.24586  ?  311 ASN   G C   1 
ATOM   5038  O O   . ASN   C  1 311 ? -6.40951  30.85612  16.19179  1.000 39.25881  ?  311 ASN   G O   1 
ATOM   5039  C CB  . ASN   C  1 311 ? -3.77255  30.07880  17.56313  1.000 7.64384   ?  311 ASN   G CB  1 
ATOM   5040  C CG  . ASN   C  1 311 ? -2.29799  30.05281  17.95702  1.000 53.36685  ?  311 ASN   G CG  1 
ATOM   5041  O OD1 . ASN   C  1 311 ? -1.43890  29.64557  17.16241  1.000 33.35794  ?  311 ASN   G OD1 1 
ATOM   5042  N ND2 . ASN   C  1 311 ? -1.99527  30.52188  19.16361  1.000 35.56149  ?  311 ASN   G ND2 1 
ATOM   5043  N N   . VAL   C  1 312 ? -5.14034  30.34598  14.40121  1.000 24.44503  ?  312 VAL   G N   1 
ATOM   5044  C CA  . VAL   C  1 312 ? -6.25752  30.19285  13.48593  1.000 22.89073  ?  312 VAL   G CA  1 
ATOM   5045  C C   . VAL   C  1 312 ? -6.37769  28.72194  13.09579  1.000 21.73657  ?  312 VAL   G C   1 
ATOM   5046  O O   . VAL   C  1 312 ? -5.44295  28.15132  12.52398  1.000 46.63973  ?  312 VAL   G O   1 
ATOM   5047  C CB  . VAL   C  1 312 ? -6.10186  31.08449  12.24135  1.000 26.45662  ?  312 VAL   G CB  1 
ATOM   5048  C CG1 . VAL   C  1 312 ? -7.42428  31.12046  11.45589  1.000 12.75347  ?  312 VAL   G CG1 1 
ATOM   5049  C CG2 . VAL   C  1 312 ? -5.70106  32.49634  12.65469  1.000 19.15272  ?  312 VAL   G CG2 1 
ATOM   5050  N N   . PRO   C  1 313 ? -7.49283  28.06720  13.39482  1.000 35.79421  ?  313 PRO   G N   1 
ATOM   5051  C CA  . PRO   C  1 313 ? -7.71698  26.70919  12.87600  1.000 31.47703  ?  313 PRO   G CA  1 
ATOM   5052  C C   . PRO   C  1 313 ? -7.88934  26.74449  11.36674  1.000 35.15710  ?  313 PRO   G C   1 
ATOM   5053  O O   . PRO   C  1 313 ? -8.37677  27.72843  10.79978  1.000 30.39541  ?  313 PRO   G O   1 
ATOM   5054  C CB  . PRO   C  1 313 ? -9.02054  26.26358  13.55981  1.000 14.51612  ?  313 PRO   G CB  1 
ATOM   5055  C CG  . PRO   C  1 313 ? -9.29336  27.30697  14.66015  1.000 20.36478  ?  313 PRO   G CG  1 
ATOM   5056  C CD  . PRO   C  1 313 ? -8.60438  28.56884  14.21818  1.000 16.53571  ?  313 PRO   G CD  1 
ATOM   5057  N N   . GLY   C  1 314 ? -7.49291  25.65731  10.71277  1.000 23.48012  ?  314 GLY   G N   1 
ATOM   5058  C CA  . GLY   C  1 314 ? -7.58304  25.62337  9.27169   1.000 15.94156  ?  314 GLY   G CA  1 
ATOM   5059  C C   . GLY   C  1 314 ? -7.38283  24.25076  8.67562   1.000 32.90438  ?  314 GLY   G C   1 
ATOM   5060  O O   . GLY   C  1 314 ? -7.60786  23.22742  9.32687   1.000 24.15542  ?  314 GLY   G O   1 
ATOM   5061  N N   . THR   C  1 315 ? -6.96902  24.24264  7.41189   1.000 17.98841  ?  315 THR   G N   1 
ATOM   5062  C CA  . THR   C  1 315 ? -6.72062  23.00966  6.68694   1.000 20.34002  ?  315 THR   G CA  1 
ATOM   5063  C C   . THR   C  1 315 ? -5.34457  22.43163  7.04057   1.000 28.67048  ?  315 THR   G C   1 
ATOM   5064  O O   . THR   C  1 315 ? -4.48556  23.09418  7.63273   1.000 20.85387  ?  315 THR   G O   1 
ATOM   5065  C CB  . THR   C  1 315 ? -6.81390  23.25269  5.17634   1.000 19.96248  ?  315 THR   G CB  1 
ATOM   5066  O OG1 . THR   C  1 315 ? -5.71617  24.07725  4.73513   1.000 13.74178  ?  315 THR   G OG1 1 
ATOM   5067  C CG2 . THR   C  1 315 ? -8.06804  23.97090  4.86074   1.000 10.45379  ?  315 THR   G CG2 1 
ATOM   5068  N N   . TYR   C  1 316 ? -5.15495  21.17343  6.65141   1.000 23.90483  ?  316 TYR   G N   1 
ATOM   5069  C CA  . TYR   C  1 316 ? -3.93802  20.36258  6.69119   1.000 23.46463  ?  316 TYR   G CA  1 
ATOM   5070  C C   . TYR   C  1 316 ? -3.60909  19.76787  5.32874   1.000 18.48957  ?  316 TYR   G C   1 
ATOM   5071  O O   . TYR   C  1 316 ? -2.43274  19.66997  4.96707   1.000 28.35159  ?  316 TYR   G O   1 
ATOM   5072  C CB  . TYR   C  1 316 ? -4.06882  19.21438  7.73869   1.000 18.41009  ?  316 TYR   G CB  1 
ATOM   5073  C CG  . TYR   C  1 316 ? -4.34900  19.73521  9.12223   1.000 29.15627  ?  316 TYR   G CG  1 
ATOM   5074  C CD1 . TYR   C  1 316 ? -3.31353  20.22522  9.92551   1.000 30.53542  ?  316 TYR   G CD1 1 
ATOM   5075  C CD2 . TYR   C  1 316 ? -5.65270  19.79122  9.60856   1.000 23.25495  ?  316 TYR   G CD2 1 
ATOM   5076  C CE1 . TYR   C  1 316 ? -3.56212  20.74241  11.19316  1.000 22.17415  ?  316 TYR   G CE1 1 
ATOM   5077  C CE2 . TYR   C  1 316 ? -5.92444  20.30029  10.87794  1.000 15.44315  ?  316 TYR   G CE2 1 
ATOM   5078  C CZ  . TYR   C  1 316 ? -4.87499  20.77267  11.66403  1.000 33.22747  ?  316 TYR   G CZ  1 
ATOM   5079  O OH  . TYR   C  1 316 ? -5.15394  21.27919  12.91455  1.000 24.50080  ?  316 TYR   G OH  1 
ATOM   5080  N N   . PHE   C  1 317 ? -4.62367  19.38050  4.54723   1.000 36.05090  ?  317 PHE   G N   1 
ATOM   5081  C CA  . PHE   C  1 317 ? -4.39058  18.59480  3.34204   1.000 17.30054  ?  317 PHE   G CA  1 
ATOM   5082  C C   . PHE   C  1 317 ? -5.00333  19.23423  2.10341   1.000 38.97042  ?  317 PHE   G C   1 
ATOM   5083  O O   . PHE   C  1 317 ? -5.30516  18.52829  1.13042   1.000 26.90181  ?  317 PHE   G O   1 
ATOM   5084  C CB  . PHE   C  1 317 ? -4.92351  17.17436  3.52755   1.000 17.17978  ?  317 PHE   G CB  1 
ATOM   5085  C CG  . PHE   C  1 317 ? -4.22184  16.41751  4.61449   1.000 37.32288  ?  317 PHE   G CG  1 
ATOM   5086  C CD1 . PHE   C  1 317 ? -2.91587  15.98112  4.43326   1.000 17.98013  ?  317 PHE   G CD1 1 
ATOM   5087  C CD2 . PHE   C  1 317 ? -4.85616  16.16674  5.82745   1.000 33.08626  ?  317 PHE   G CD2 1 
ATOM   5088  C CE1 . PHE   C  1 317 ? -2.25765  15.28648  5.43219   1.000 33.28915  ?  317 PHE   G CE1 1 
ATOM   5089  C CE2 . PHE   C  1 317 ? -4.20552  15.47804  6.82900   1.000 25.87872  ?  317 PHE   G CE2 1 
ATOM   5090  C CZ  . PHE   C  1 317 ? -2.89865  15.03922  6.63037   1.000 27.28534  ?  317 PHE   G CZ  1 
ATOM   5091  N N   . ALA   C  1 318 ? -5.17619  20.56228  2.10931   1.000 22.46513  ?  318 ALA   G N   1 
ATOM   5092  C CA  . ALA   C  1 318 ? -5.77945  21.27311  0.98070   1.000 19.34066  ?  318 ALA   G CA  1 
ATOM   5093  C C   . ALA   C  1 318 ? -4.68555  21.78458  0.05404   1.000 24.15638  ?  318 ALA   G C   1 
ATOM   5094  O O   . ALA   C  1 318 ? -3.90644  22.66156  0.43659   1.000 29.07320  ?  318 ALA   G O   1 
ATOM   5095  C CB  . ALA   C  1 318 ? -6.63905  22.43583  1.46758   1.000 12.86261  ?  318 ALA   G CB  1 
ATOM   5096  N N   . GLN   C  1 319 ? -4.63216  21.25632  -1.16912  1.000 25.57334  ?  319 GLN   G N   1 
ATOM   5097  C CA  . GLN   C  1 319 ? -3.79196  21.86937  -2.18771  1.000 22.05446  ?  319 GLN   G CA  1 
ATOM   5098  C C   . GLN   C  1 319 ? -4.62814  22.87137  -2.98420  1.000 20.14961  ?  319 GLN   G C   1 
ATOM   5099  O O   . GLN   C  1 319 ? -5.84306  22.99499  -2.79152  1.000 34.42268  ?  319 GLN   G O   1 
ATOM   5100  C CB  . GLN   C  1 319 ? -3.16203  20.81360  -3.09279  1.000 21.54031  ?  319 GLN   G CB  1 
ATOM   5101  C CG  . GLN   C  1 319 ? -4.17894  20.05466  -3.89379  1.000 29.64278  ?  319 GLN   G CG  1 
ATOM   5102  C CD  . GLN   C  1 319 ? -3.56959  18.87065  -4.60505  1.000 18.65519  ?  319 GLN   G CD  1 
ATOM   5103  O OE1 . GLN   C  1 319 ? -3.25012  17.84836  -3.98331  1.000 41.97580  ?  319 GLN   G OE1 1 
ATOM   5104  N NE2 . GLN   C  1 319 ? -3.41862  18.99057  -5.91738  1.000 27.46239  ?  319 GLN   G NE2 1 
ATOM   5105  N N   . ALA   C  1 320 ? -3.97413  23.61254  -3.87453  1.000 27.17735  ?  320 ALA   G N   1 
ATOM   5106  C CA  . ALA   C  1 320 ? -4.69426  24.58921  -4.68738  1.000 27.92276  ?  320 ALA   G CA  1 
ATOM   5107  C C   . ALA   C  1 320 ? -5.58921  23.86953  -5.69695  1.000 27.66557  ?  320 ALA   G C   1 
ATOM   5108  O O   . ALA   C  1 320 ? -5.11306  22.98203  -6.41828  1.000 29.20377  ?  320 ALA   G O   1 
ATOM   5109  C CB  . ALA   C  1 320 ? -3.72179  25.51767  -5.40533  1.000 11.66526  ?  320 ALA   G CB  1 
ATOM   5110  N N   . PRO   C  1 321 ? -6.87325  24.23236  -5.79205  1.000 40.70275  ?  321 PRO   G N   1 
ATOM   5111  C CA  . PRO   C  1 321 ? -7.78285  23.52057  -6.71133  1.000 26.60172  ?  321 PRO   G CA  1 
ATOM   5112  C C   . PRO   C  1 321 ? -7.29702  23.49679  -8.15949  1.000 32.28698  ?  321 PRO   G C   1 
ATOM   5113  O O   . PRO   C  1 321 ? -7.50509  22.49001  -8.84851  1.000 37.05347  ?  321 PRO   G O   1 
ATOM   5114  C CB  . PRO   C  1 321 ? -9.10473  24.29309  -6.56565  1.000 19.79830  ?  321 PRO   G CB  1 
ATOM   5115  C CG  . PRO   C  1 321 ? -8.93932  25.19275  -5.37339  1.000 40.95844  ?  321 PRO   G CG  1 
ATOM   5116  C CD  . PRO   C  1 321 ? -7.47788  25.45207  -5.22917  1.000 23.24821  ?  321 PRO   G CD  1 
ATOM   5117  N N   . SER   C  1 322 ? -6.62170  24.55887  -8.62396  1.000 37.82708  ?  322 SER   G N   1 
ATOM   5118  C CA  . SER   C  1 322 ? -6.04604  24.58616  -9.97102  1.000 37.30931  ?  322 SER   G CA  1 
ATOM   5119  C C   . SER   C  1 322 ? -5.02978  23.47232  -10.22444 1.000 36.91329  ?  322 SER   G C   1 
ATOM   5120  O O   . SER   C  1 322 ? -4.74910  23.17141  -11.39144 1.000 56.29305  ?  322 SER   G O   1 
ATOM   5121  C CB  . SER   C  1 322 ? -5.37508  25.94234  -10.24151 1.000 28.37353  ?  322 SER   G CB  1 
ATOM   5122  O OG  . SER   C  1 322 ? -4.68875  26.44182  -9.09821  1.000 53.46587  ?  322 SER   G OG  1 
ATOM   5123  N N   . THR   C  1 323 ? -4.44862  22.87545  -9.17635  1.000 45.14235  ?  323 THR   G N   1 
ATOM   5124  C CA  . THR   C  1 323 ? -3.46789  21.80638  -9.34612  1.000 27.48666  ?  323 THR   G CA  1 
ATOM   5125  C C   . THR   C  1 323 ? -4.07071  20.41932  -9.21127  1.000 42.96126  ?  323 THR   G C   1 
ATOM   5126  O O   . THR   C  1 323 ? -3.34734  19.43596  -9.37727  1.000 25.87263  ?  323 THR   G O   1 
ATOM   5127  C CB  . THR   C  1 323 ? -2.31898  21.93454  -8.33219  1.000 34.22097  ?  323 THR   G CB  1 
ATOM   5128  O OG1 . THR   C  1 323 ? -2.74577  21.45326  -7.04553  1.000 35.75629  ?  323 THR   G OG1 1 
ATOM   5129  C CG2 . THR   C  1 323 ? -1.88307  23.36802  -8.20361  1.000 16.17124  ?  323 THR   G CG2 1 
ATOM   5130  N N   . ILE   C  1 324 ? -5.36076  20.31031  -8.89284  1.000 33.03326  ?  324 ILE   G N   1 
ATOM   5131  C CA  . ILE   C  1 324 ? -5.95903  18.99541  -8.70044  1.000 34.77905  ?  324 ILE   G CA  1 
ATOM   5132  C C   . ILE   C  1 324 ? -5.85345  18.21438  -9.99923  1.000 53.32857  ?  324 ILE   G C   1 
ATOM   5133  O O   . ILE   C  1 324 ? -6.30345  18.67347  -11.05727 1.000 45.99888  ?  324 ILE   G O   1 
ATOM   5134  C CB  . ILE   C  1 324 ? -7.40613  19.12743  -8.23489  1.000 22.78811  ?  324 ILE   G CB  1 
ATOM   5135  C CG1 . ILE   C  1 324 ? -7.43670  19.72838  -6.83044  1.000 36.16655  ?  324 ILE   G CG1 1 
ATOM   5136  C CG2 . ILE   C  1 324 ? -8.09271  17.76152  -8.27024  1.000 25.33055  ?  324 ILE   G CG2 1 
ATOM   5137  C CD1 . ILE   C  1 324 ? -8.79992  19.96237  -6.31388  1.000 29.66963  ?  324 ILE   G CD1 1 
ATOM   5138  N N   . GLY   C  1 325 ? -5.21987  17.04311  -9.93383  1.000 35.28946  ?  325 GLY   G N   1 
ATOM   5139  C CA  . GLY   C  1 325 ? -5.01792  16.21146  -11.10041 1.000 30.50909  ?  325 GLY   G CA  1 
ATOM   5140  C C   . GLY   C  1 325 ? -3.63281  16.27197  -11.72157 1.000 39.54003  ?  325 GLY   G C   1 
ATOM   5141  O O   . GLY   C  1 325 ? -3.28559  15.36889  -12.49112 1.000 44.71150  ?  325 GLY   G O   1 
ATOM   5142  N N   . ASP   C  1 326 ? -2.84755  17.31182  -11.43297 1.000 34.00730  ?  326 ASP   G N   1 
ATOM   5143  C CA  . ASP   C  1 326 ? -1.47265  17.38369  -11.91763 1.000 41.21166  ?  326 ASP   G CA  1 
ATOM   5144  C C   . ASP   C  1 326 ? -0.68035  16.13580  -11.51501 1.000 32.38612  ?  326 ASP   G C   1 
ATOM   5145  O O   . ASP   C  1 326 ? -0.98950  15.48091  -10.51315 1.000 42.75413  ?  326 ASP   G O   1 
ATOM   5146  C CB  . ASP   C  1 326 ? -0.76943  18.62240  -11.36141 1.000 23.64366  ?  326 ASP   G CB  1 
ATOM   5147  C CG  . ASP   C  1 326 ? -1.33530  19.92126  -11.90216 1.000 60.31642  ?  326 ASP   G CG  1 
ATOM   5148  O OD1 . ASP   C  1 326 ? -2.20089  19.88267  -12.81541 1.000 45.91752  ?  326 ASP   G OD1 1 
ATOM   5149  O OD2 . ASP   C  1 326 ? -0.89561  20.98579  -11.39773 1.000 48.51098  -1 326 ASP   G OD2 1 
ATOM   5150  N N   . PRO   C  1 327 ? 0.35460   15.78794  -12.27082 1.000 51.20792  ?  327 PRO   G N   1 
ATOM   5151  C CA  . PRO   C  1 327 ? 1.13560   14.59132  -11.93054 1.000 36.66527  ?  327 PRO   G CA  1 
ATOM   5152  C C   . PRO   C  1 327 ? 1.86828   14.73627  -10.59879 1.000 31.38374  ?  327 PRO   G C   1 
ATOM   5153  O O   . PRO   C  1 327 ? 2.37307   15.80893  -10.25808 1.000 44.36641  ?  327 PRO   G O   1 
ATOM   5154  C CB  . PRO   C  1 327 ? 2.11737   14.46518  -13.10410 1.000 16.55629  ?  327 PRO   G CB  1 
ATOM   5155  C CG  . PRO   C  1 327 ? 2.09786   15.78978  -13.80435 1.000 31.22534  ?  327 PRO   G CG  1 
ATOM   5156  C CD  . PRO   C  1 327 ? 0.73000   16.35502  -13.57962 1.000 34.14045  ?  327 PRO   G CD  1 
ATOM   5157  N N   . ILE   C  1 328 ? 1.91239   13.64291  -9.84037  1.000 33.43715  ?  328 ILE   G N   1 
ATOM   5158  C CA  . ILE   C  1 328 ? 2.73514   13.57982  -8.63219  1.000 33.23646  ?  328 ILE   G CA  1 
ATOM   5159  C C   . ILE   C  1 328 ? 4.06051   12.90709  -8.97039  1.000 35.53219  ?  328 ILE   G C   1 
ATOM   5160  O O   . ILE   C  1 328 ? 4.12247   11.67009  -9.03983  1.000 44.57308  ?  328 ILE   G O   1 
ATOM   5161  C CB  . ILE   C  1 328 ? 2.02040   12.83802  -7.48922  1.000 38.46134  ?  328 ILE   G CB  1 
ATOM   5162  C CG1 . ILE   C  1 328 ? 0.66633   13.48495  -7.18786  1.000 25.91794  ?  328 ILE   G CG1 1 
ATOM   5163  C CG2 . ILE   C  1 328 ? 2.87122   12.84421  -6.21897  1.000 27.64242  ?  328 ILE   G CG2 1 
ATOM   5164  C CD1 . ILE   C  1 328 ? -0.08849  12.81379  -6.03923  1.000 21.92773  ?  328 ILE   G CD1 1 
ATOM   5165  N N   . PRO   C  1 329 ? 5.14127   13.66997  -9.16002  1.000 44.68377  ?  329 PRO   G N   1 
ATOM   5166  C CA  . PRO   C  1 329 ? 6.40696   13.08147  -9.62474  1.000 30.15598  ?  329 PRO   G CA  1 
ATOM   5167  C C   . PRO   C  1 329 ? 6.91735   11.99984  -8.68420  1.000 32.40888  ?  329 PRO   G C   1 
ATOM   5168  O O   . PRO   C  1 329 ? 6.73688   12.06723  -7.46303  1.000 64.75923  ?  329 PRO   G O   1 
ATOM   5169  C CB  . PRO   C  1 329 ? 7.36542   14.27764  -9.66994  1.000 17.01678  ?  329 PRO   G CB  1 
ATOM   5170  C CG  . PRO   C  1 329 ? 6.45504   15.49370  -9.75075  1.000 27.72516  ?  329 PRO   G CG  1 
ATOM   5171  C CD  . PRO   C  1 329 ? 5.21842   15.13207  -9.00992  1.000 32.61641  ?  329 PRO   G CD  1 
ATOM   5172  N N   . ASP   C  1 330 ? 7.51640   10.96812  -9.28502  1.000 57.08609  ?  330 ASP   G N   1 
ATOM   5173  C CA  . ASP   C  1 330 ? 8.13374   9.86570   -8.55683  1.000 67.15800  ?  330 ASP   G CA  1 
ATOM   5174  C C   . ASP   C  1 330 ? 9.62844   10.07118  -8.30636  1.000 45.85131  ?  330 ASP   G C   1 
ATOM   5175  O O   . ASP   C  1 330 ? 10.34515  9.07681   -8.08876  1.000 74.57626  ?  330 ASP   G O   1 
ATOM   5176  C CB  . ASP   C  1 330 ? 7.88778   8.53589   -9.29495  1.000 38.39223  ?  330 ASP   G CB  1 
ATOM   5177  C CG  . ASP   C  1 330 ? 6.39219   8.42615   -9.86036  1.000 61.16657  ?  330 ASP   G CG  1 
ATOM   5178  O OD1 . ASP   C  1 330 ? 5.32605   8.39307   -9.08517  1.000 117.65765 ?  330 ASP   G OD1 1 
ATOM   5179  O OD2 . ASP   C  1 330 ? 6.22129   8.28441   -11.09022 1.000 84.17126  ?  330 ASP   G OD2 1 
ATOM   5180  N N   . ASN   C  1 331 ? 10.08145  11.32987  -8.30066  1.000 65.60081  ?  331 ASN   G N   1 
ATOM   5181  C CA  . ASN   C  1 331 ? 11.45834  11.73078  -8.05939  1.000 65.72589  ?  331 ASN   G CA  1 
ATOM   5182  C C   . ASN   C  1 331 ? 11.45548  12.76384  -6.93536  1.000 48.39427  ?  331 ASN   G C   1 
ATOM   5183  O O   . ASN   C  1 331 ? 10.44249  12.94339  -6.27162  1.000 92.10422  ?  331 ASN   G O   1 
ATOM   5184  C CB  . ASN   C  1 331 ? 12.05434  12.26901  -9.35130  1.000 43.65017  ?  331 ASN   G CB  1 
ATOM   5185  C CG  . ASN   C  1 331 ? 11.44313  13.55477  -9.80589  1.000 54.74132  ?  331 ASN   G CG  1 
ATOM   5186  O OD1 . ASN   C  1 331 ? 11.28536  14.54721  -9.09453  1.000 124.25455 ?  331 ASN   G OD1 1 
ATOM   5187  N ND2 . ASN   C  1 331 ? 10.98489  13.49410  -11.02934 1.000 58.91104  ?  331 ASN   G ND2 1 
ATOM   5188  N N   . ASP   C  1 332 ? 12.53885  13.49269  -6.79331  1.000 118.51881 ?  332 ASP   G N   1 
ATOM   5189  C CA  . ASP   C  1 332 ? 12.80056  14.40278  -5.68241  1.000 19.16640  ?  332 ASP   G CA  1 
ATOM   5190  C C   . ASP   C  1 332 ? 13.12753  15.79890  -6.20101  1.000 75.76868  ?  332 ASP   G C   1 
ATOM   5191  O O   . ASP   C  1 332 ? 13.52581  16.67082  -5.42105  1.000 57.06791  ?  332 ASP   G O   1 
ATOM   5192  C CB  . ASP   C  1 332 ? 13.96469  13.87146  -4.84042  1.000 83.29032  ?  332 ASP   G CB  1 
ATOM   5193  C CG  . ASP   C  1 332 ? 15.32999  14.21915  -5.45052  1.000 137.99466 ?  332 ASP   G CG  1 
ATOM   5194  O OD1 . ASP   C  1 332 ? 15.93712  13.35314  -6.12910  1.000 144.09943 ?  332 ASP   G OD1 1 
ATOM   5195  O OD2 . ASP   C  1 332 ? 15.81364  15.36822  -5.24256  1.000 119.98727 ?  332 ASP   G OD2 1 
ATOM   5196  N N   . TYR   C  1 333 ? 13.05765  16.01182  -7.52150  1.000 69.26778  ?  333 TYR   G N   1 
ATOM   5197  C CA  . TYR   C  1 333 ? 13.41609  17.31749  -8.05457  1.000 69.99535  ?  333 TYR   G CA  1 
ATOM   5198  C C   . TYR   C  1 333 ? 12.21975  18.08166  -8.60223  1.000 85.41198  ?  333 TYR   G C   1 
ATOM   5199  O O   . TYR   C  1 333 ? 12.22395  19.32284  -8.61609  1.000 83.32508  ?  333 TYR   G O   1 
ATOM   5200  C CB  . TYR   C  1 333 ? 14.49173  17.20875  -9.15437  1.000 12.77549  ?  333 TYR   G CB  1 
ATOM   5201  C CG  . TYR   C  1 333 ? 14.20328  16.18755  -10.21302 1.000 90.40388  ?  333 TYR   G CG  1 
ATOM   5202  C CD1 . TYR   C  1 333 ? 13.56577  16.57436  -11.40852 1.000 43.23568  ?  333 TYR   G CD1 1 
ATOM   5203  C CD2 . TYR   C  1 333 ? 14.58771  14.83118  -10.03852 1.000 53.05564  ?  333 TYR   G CD2 1 
ATOM   5204  C CE1 . TYR   C  1 333 ? 13.30550  15.66621  -12.40335 1.000 65.45009  ?  333 TYR   G CE1 1 
ATOM   5205  C CE2 . TYR   C  1 333 ? 14.33124  13.89548  -11.03877 1.000 61.69754  ?  333 TYR   G CE2 1 
ATOM   5206  C CZ  . TYR   C  1 333 ? 13.67632  14.33603  -12.21671 1.000 98.42927  ?  333 TYR   G CZ  1 
ATOM   5207  O OH  . TYR   C  1 333 ? 13.40133  13.48413  -13.23699 1.000 17.62316  ?  333 TYR   G OH  1 
ATOM   5208  N N   . ASP   C  1 334 ? 11.22477  17.38523  -8.99443  1.000 64.14636  ?  334 ASP   G N   1 
ATOM   5209  C CA  . ASP   C  1 334 ? 9.99454   18.01503  -9.47821  1.000 62.22108  ?  334 ASP   G CA  1 
ATOM   5210  C C   . ASP   C  1 334 ? 8.96688   18.18251  -8.36246  1.000 71.66145  ?  334 ASP   G C   1 
ATOM   5211  O O   . ASP   C  1 334 ? 8.61892   17.19938  -7.68525  1.000 37.38901  ?  334 ASP   G O   1 
ATOM   5212  C CB  . ASP   C  1 334 ? 9.37963   17.20171  -10.60536 1.000 91.02314  ?  334 ASP   G CB  1 
ATOM   5213  C CG  . ASP   C  1 334 ? 10.18162  17.28503  -11.87679 1.000 105.64447 ?  334 ASP   G CG  1 
ATOM   5214  O OD1 . ASP   C  1 334 ? 10.81447  18.35108  -12.11830 1.000 61.85011  ?  334 ASP   G OD1 1 
ATOM   5215  O OD2 . ASP   C  1 334 ? 10.17967  16.30316  -12.64443 1.000 73.17432  -1 334 ASP   G OD2 1 
ATOM   5216  N N   . PRO   C  1 335 ? 8.45194   19.39495  -8.15895  1.000 61.72100  ?  335 PRO   G N   1 
ATOM   5217  C CA  . PRO   C  1 335 ? 7.51450   19.63328  -7.06083  1.000 41.52746  ?  335 PRO   G CA  1 
ATOM   5218  C C   . PRO   C  1 335 ? 6.17482   18.98963  -7.34232  1.000 25.55700  ?  335 PRO   G C   1 
ATOM   5219  O O   . PRO   C  1 335 ? 5.61925   19.12578  -8.44982  1.000 54.49859  ?  335 PRO   G O   1 
ATOM   5220  C CB  . PRO   C  1 335 ? 7.39544   21.16464  -7.02331  1.000 47.30625  ?  335 PRO   G CB  1 
ATOM   5221  C CG  . PRO   C  1 335 ? 8.47696   21.67645  -7.93485  1.000 60.16688  ?  335 PRO   G CG  1 
ATOM   5222  C CD  . PRO   C  1 335 ? 8.73582   20.61278  -8.92541  1.000 33.74293  ?  335 PRO   G CD  1 
ATOM   5223  N N   . PRO   C  1 336 ? 5.60575   18.28173  -6.36453  1.000 54.80775  ?  336 PRO   G N   1 
ATOM   5224  C CA  . PRO   C  1 336 ? 4.23998   17.75195  -6.50800  1.000 19.22287  ?  336 PRO   G CA  1 
ATOM   5225  C C   . PRO   C  1 336 ? 3.21205   18.85815  -6.31594  1.000 85.51511  ?  336 PRO   G C   1 
ATOM   5226  O O   . PRO   C  1 336 ? 3.55411   19.97782  -5.89508  1.000 24.58136  ?  336 PRO   G O   1 
ATOM   5227  C CB  . PRO   C  1 336 ? 4.16487   16.69202  -5.40151  1.000 38.20591  ?  336 PRO   G CB  1 
ATOM   5228  C CG  . PRO   C  1 336 ? 5.10034   17.20296  -4.33715  1.000 35.18247  ?  336 PRO   G CG  1 
ATOM   5229  C CD  . PRO   C  1 336 ? 6.15621   18.05382  -5.01090  1.000 19.20551  ?  336 PRO   G CD  1 
ATOM   5230  N N   . PRO   C  1 337 ? 1.94057   18.60424  -6.64325  1.000 24.39067  ?  337 PRO   G N   1 
ATOM   5231  C CA  . PRO   C  1 337 ? 0.94559   19.70496  -6.61289  1.000 40.00215  ?  337 PRO   G CA  1 
ATOM   5232  C C   . PRO   C  1 337 ? 0.86143   20.44581  -5.27845  1.000 28.55572  ?  337 PRO   G C   1 
ATOM   5233  O O   . PRO   C  1 337 ? 0.79928   21.68257  -5.26345  1.000 26.40145  ?  337 PRO   G O   1 
ATOM   5234  C CB  . PRO   C  1 337 ? -0.37193  18.99327  -6.94531  1.000 26.52483  ?  337 PRO   G CB  1 
ATOM   5235  C CG  . PRO   C  1 337 ? 0.01586   17.77146  -7.66666  1.000 34.90752  ?  337 PRO   G CG  1 
ATOM   5236  C CD  . PRO   C  1 337 ? 1.35769   17.34383  -7.12585  1.000 43.58225  ?  337 PRO   G CD  1 
ATOM   5237  N N   . TYR   C  1 338 ? 0.88577   19.72329  -4.15615  1.000 27.31087  ?  338 TYR   G N   1 
ATOM   5238  C CA  . TYR   C  1 338 ? 0.84712   20.37155  -2.84973  1.000 29.89597  ?  338 TYR   G CA  1 
ATOM   5239  C C   . TYR   C  1 338 ? 1.98024   21.38161  -2.68418  1.000 23.70837  ?  338 TYR   G C   1 
ATOM   5240  O O   . TYR   C  1 338 ? 1.74801   22.50805  -2.22435  1.000 25.03650  ?  338 TYR   G O   1 
ATOM   5241  C CB  . TYR   C  1 338 ? 0.89389   19.31440  -1.74561  1.000 17.41372  ?  338 TYR   G CB  1 
ATOM   5242  C CG  . TYR   C  1 338 ? 0.68152   19.84282  -0.34186  1.000 30.49017  ?  338 TYR   G CG  1 
ATOM   5243  C CD1 . TYR   C  1 338 ? -0.48017  20.54003  0.00722   1.000 23.21790  ?  338 TYR   G CD1 1 
ATOM   5244  C CD2 . TYR   C  1 338 ? 1.62979   19.62093  0.64222   1.000 21.05842  ?  338 TYR   G CD2 1 
ATOM   5245  C CE1 . TYR   C  1 338 ? -0.67570  21.00744  1.31234   1.000 25.93032  ?  338 TYR   G CE1 1 
ATOM   5246  C CE2 . TYR   C  1 338 ? 1.44730   20.08037  1.93508   1.000 14.96701  ?  338 TYR   G CE2 1 
ATOM   5247  C CZ  . TYR   C  1 338 ? 0.30253   20.77630  2.26843   1.000 35.21187  ?  338 TYR   G CZ  1 
ATOM   5248  O OH  . TYR   C  1 338 ? 0.15055   21.22095  3.56556   1.000 23.76047  ?  338 TYR   G OH  1 
ATOM   5249  N N   . LEU   C  1 339 ? 3.21901   21.00338  -3.04657  1.000 29.19362  ?  339 LEU   G N   1 
ATOM   5250  C CA  . LEU   C  1 339 ? 4.33278   21.95329  -2.89697  1.000 20.35499  ?  339 LEU   G CA  1 
ATOM   5251  C C   . LEU   C  1 339 ? 4.32142   23.06305  -3.94075  1.000 32.34010  ?  339 LEU   G C   1 
ATOM   5252  O O   . LEU   C  1 339 ? 5.15941   23.96708  -3.85480  1.000 34.03167  ?  339 LEU   G O   1 
ATOM   5253  C CB  . LEU   C  1 339 ? 5.68450   21.24214  -2.93918  1.000 21.17803  ?  339 LEU   G CB  1 
ATOM   5254  C CG  . LEU   C  1 339 ? 5.85690   20.25568  -1.77496  1.000 43.19329  ?  339 LEU   G CG  1 
ATOM   5255  C CD1 . LEU   C  1 339 ? 7.25122   19.66838  -1.75771  1.000 27.01879  ?  339 LEU   G CD1 1 
ATOM   5256  C CD2 . LEU   C  1 339 ? 5.55346   20.91879  -0.44922  1.000 28.37284  ?  339 LEU   G CD2 1 
ATOM   5257  N N   . LYS   C  1 340 ? 3.40894   23.02831  -4.91261  1.000 21.10034  ?  340 LYS   G N   1 
ATOM   5258  C CA  . LYS   C  1 340 ? 3.13232   24.18934  -5.74907  1.000 40.91898  ?  340 LYS   G CA  1 
ATOM   5259  C C   . LYS   C  1 340 ? 1.94154   25.01946  -5.24477  1.000 23.13098  ?  340 LYS   G C   1 
ATOM   5260  O O   . LYS   C  1 340 ? 1.46547   25.89141  -5.97452  1.000 29.52228  ?  340 LYS   G O   1 
ATOM   5261  C CB  . LYS   C  1 340 ? 2.88936   23.75225  -7.19774  1.000 23.78103  ?  340 LYS   G CB  1 
ATOM   5262  N N   . SER   C  1 341 ? 1.47146   24.78719  -4.00617  1.000 31.71123  ?  341 SER   G N   1 
ATOM   5263  C CA  . SER   C  1 341 ? 0.25308   25.39841  -3.48028  1.000 24.86629  ?  341 SER   G CA  1 
ATOM   5264  C C   . SER   C  1 341 ? 0.46521   26.31297  -2.27326  1.000 29.75191  ?  341 SER   G C   1 
ATOM   5265  O O   . SER   C  1 341 ? -0.52730  26.77781  -1.68788  1.000 40.30057  ?  341 SER   G O   1 
ATOM   5266  C CB  . SER   C  1 341 ? -0.75616  24.30526  -3.08385  1.000 31.41187  ?  341 SER   G CB  1 
ATOM   5267  O OG  . SER   C  1 341 ? -1.17888  23.53551  -4.19517  1.000 31.17377  ?  341 SER   G OG  1 
ATOM   5268  N N   . LEU   C  1 342 ? 1.71213   26.58554  -1.88312  1.000 29.98094  ?  342 LEU   G N   1 
ATOM   5269  C CA  . LEU   C  1 342 ? 1.96746   27.23276  -0.59828  1.000 41.17020  ?  342 LEU   G CA  1 
ATOM   5270  C C   . LEU   C  1 342 ? 1.33933   28.62057  -0.51610  1.000 29.77268  ?  342 LEU   G C   1 
ATOM   5271  O O   . LEU   C  1 342 ? 0.87635   29.03066  0.55397   1.000 35.68909  ?  342 LEU   G O   1 
ATOM   5272  C CB  . LEU   C  1 342 ? 3.46906   27.32835  -0.33430  1.000 24.03566  ?  342 LEU   G CB  1 
ATOM   5273  C CG  . LEU   C  1 342 ? 4.12299   26.19781  0.44824   1.000 42.30181  ?  342 LEU   G CG  1 
ATOM   5274  C CD1 . LEU   C  1 342 ? 4.03516   24.88265  -0.32818  1.000 22.47873  ?  342 LEU   G CD1 1 
ATOM   5275  C CD2 . LEU   C  1 342 ? 5.58310   26.58077  0.75303   1.000 18.08992  ?  342 LEU   G CD2 1 
ATOM   5276  N N   . VAL   C  1 343 ? 1.32807   29.37897  -1.61359  1.000 36.92246  ?  343 VAL   G N   1 
ATOM   5277  C CA  . VAL   C  1 343 ? 0.68082   30.68633  -1.53523  1.000 31.21652  ?  343 VAL   G CA  1 
ATOM   5278  C C   . VAL   C  1 343 ? -0.81505  30.51273  -1.31723  1.000 44.13064  ?  343 VAL   G C   1 
ATOM   5279  O O   . VAL   C  1 343 ? -1.40217  31.13707  -0.42682  1.000 28.45918  ?  343 VAL   G O   1 
ATOM   5280  C CB  . VAL   C  1 343 ? 0.97492   31.53861  -2.78219  1.000 32.09716  ?  343 VAL   G CB  1 
ATOM   5281  C CG1 . VAL   C  1 343 ? 0.08816   32.78336  -2.78145  1.000 18.31250  ?  343 VAL   G CG1 1 
ATOM   5282  C CG2 . VAL   C  1 343 ? 2.43015   31.96596  -2.79059  1.000 25.66017  ?  343 VAL   G CG2 1 
ATOM   5283  N N   . TYR   C  1 344 ? -1.44060  29.62716  -2.09502  1.000 18.60183  ?  344 TYR   G N   1 
ATOM   5284  C CA  . TYR   C  1 344 ? -2.87187  29.38483  -1.95127  1.000 36.05762  ?  344 TYR   G CA  1 
ATOM   5285  C C   . TYR   C  1 344 ? -3.24808  29.03738  -0.51532  1.000 37.59081  ?  344 TYR   G C   1 
ATOM   5286  O O   . TYR   C  1 344 ? -4.10864  29.69342  0.08034   1.000 27.57589  ?  344 TYR   G O   1 
ATOM   5287  C CB  . TYR   C  1 344 ? -3.32686  28.27063  -2.89580  1.000 22.95830  ?  344 TYR   G CB  1 
ATOM   5288  C CG  . TYR   C  1 344 ? -4.77391  27.86839  -2.69714  1.000 43.34289  ?  344 TYR   G CG  1 
ATOM   5289  C CD1 . TYR   C  1 344 ? -5.80385  28.60528  -3.27103  1.000 26.09450  ?  344 TYR   G CD1 1 
ATOM   5290  C CD2 . TYR   C  1 344 ? -5.11204  26.75455  -1.93308  1.000 35.32017  ?  344 TYR   G CD2 1 
ATOM   5291  C CE1 . TYR   C  1 344 ? -7.13475  28.24907  -3.09310  1.000 26.29357  ?  344 TYR   G CE1 1 
ATOM   5292  C CE2 . TYR   C  1 344 ? -6.44770  26.38192  -1.74672  1.000 25.39081  ?  344 TYR   G CE2 1 
ATOM   5293  C CZ  . TYR   C  1 344 ? -7.44655  27.13463  -2.33118  1.000 43.66050  ?  344 TYR   G CZ  1 
ATOM   5294  O OH  . TYR   C  1 344 ? -8.75945  26.77414  -2.16278  1.000 38.69997  ?  344 TYR   G OH  1 
ATOM   5295  N N   . PHE   C  1 345 ? -2.61748  28.00273  0.06118   1.000 18.75984  ?  345 PHE   G N   1 
ATOM   5296  C CA  . PHE   C  1 345 ? -3.12879  27.49409  1.33169   1.000 27.80818  ?  345 PHE   G CA  1 
ATOM   5297  C C   . PHE   C  1 345 ? -2.60630  28.26460  2.54034   1.000 32.98757  ?  345 PHE   G C   1 
ATOM   5298  O O   . PHE   C  1 345 ? -3.08368  28.02972  3.65746   1.000 29.33073  ?  345 PHE   G O   1 
ATOM   5299  C CB  . PHE   C  1 345 ? -2.89735  25.96365  1.48088   1.000 18.30920  ?  345 PHE   G CB  1 
ATOM   5300  C CG  . PHE   C  1 345 ? -1.44843  25.51163  1.62687   1.000 31.51425  ?  345 PHE   G CG  1 
ATOM   5301  C CD1 . PHE   C  1 345 ? -0.68500  25.84465  2.73985   1.000 36.72437  ?  345 PHE   G CD1 1 
ATOM   5302  C CD2 . PHE   C  1 345 ? -0.89401  24.64298  0.69036   1.000 25.06290  ?  345 PHE   G CD2 1 
ATOM   5303  C CE1 . PHE   C  1 345 ? 0.63494   25.38072  2.87172   1.000 20.90730  ?  345 PHE   G CE1 1 
ATOM   5304  C CE2 . PHE   C  1 345 ? 0.42394   24.16460  0.81093   1.000 26.53003  ?  345 PHE   G CE2 1 
ATOM   5305  C CZ  . PHE   C  1 345 ? 1.19008   24.53123  1.89985   1.000 28.82777  ?  345 PHE   G CZ  1 
ATOM   5306  N N   . SER   C  1 346 ? -1.69680  29.21911  2.34740   1.000 16.60703  ?  346 SER   G N   1 
ATOM   5307  C CA  . SER   C  1 346 ? -1.43034  30.17709  3.41325   1.000 38.81430  ?  346 SER   G CA  1 
ATOM   5308  C C   . SER   C  1 346 ? -2.70991  30.90373  3.81072   1.000 26.18633  ?  346 SER   G C   1 
ATOM   5309  O O   . SER   C  1 346 ? -2.84326  31.35672  4.95574   1.000 26.18924  ?  346 SER   G O   1 
ATOM   5310  C CB  . SER   C  1 346 ? -0.36847  31.18099  2.96934   1.000 25.59180  ?  346 SER   G CB  1 
ATOM   5311  O OG  . SER   C  1 346 ? -0.93578  32.12601  2.07350   1.000 22.19827  ?  346 SER   G OG  1 
ATOM   5312  N N   . ASN   C  1 347 ? -3.67086  30.99486  2.88145   1.000 34.01911  ?  347 ASN   G N   1 
ATOM   5313  C CA  . ASN   C  1 347 ? -4.94390  31.65080  3.15948   1.000 15.12025  ?  347 ASN   G CA  1 
ATOM   5314  C C   . ASN   C  1 347 ? -5.82952  30.84597  4.10803   1.000 31.99213  ?  347 ASN   G C   1 
ATOM   5315  O O   . ASN   C  1 347 ? -6.66507  31.43510  4.80830   1.000 32.33469  ?  347 ASN   G O   1 
ATOM   5316  C CB  . ASN   C  1 347 ? -5.69322  31.91147  1.85095   1.000 22.64036  ?  347 ASN   G CB  1 
ATOM   5317  C CG  . ASN   C  1 347 ? -4.99621  32.92934  0.97478   1.000 37.78576  ?  347 ASN   G CG  1 
ATOM   5318  O OD1 . ASN   C  1 347 ? -4.82280  34.09135  1.36095   1.000 28.92113  ?  347 ASN   G OD1 1 
ATOM   5319  N ND2 . ASN   C  1 347 ? -4.60149  32.50593  -0.21676  1.000 19.65230  ?  347 ASN   G ND2 1 
ATOM   5320  N N   . ILE   C  1 348 ? -5.67517  29.51549  4.14954   1.000 24.77100  ?  348 ILE   G N   1 
ATOM   5321  C CA  . ILE   C  1 348 ? -6.67112  28.67257  4.81600   1.000 17.76638  ?  348 ILE   G CA  1 
ATOM   5322  C C   . ILE   C  1 348 ? -6.08592  27.62851  5.76837   1.000 28.84570  ?  348 ILE   G C   1 
ATOM   5323  O O   . ILE   C  1 348 ? -6.82734  26.99328  6.52789   1.000 32.31728  ?  348 ILE   G O   1 
ATOM   5324  C CB  . ILE   C  1 348 ? -7.55192  27.98208  3.76264   1.000 26.74995  ?  348 ILE   G CB  1 
ATOM   5325  C CG1 . ILE   C  1 348 ? -6.67634  27.15400  2.81832   1.000 15.28039  ?  348 ILE   G CG1 1 
ATOM   5326  C CG2 . ILE   C  1 348 ? -8.37602  29.01818  2.99361   1.000 13.18708  ?  348 ILE   G CG2 1 
ATOM   5327  C CD1 . ILE   C  1 348 ? -7.48554  26.21789  1.93160   1.000 37.83470  ?  348 ILE   G CD1 1 
ATOM   5328  N N   . ALA   C  1 349 ? -4.77219  27.42542  5.73330   1.000 24.71848  ?  349 ALA   G N   1 
ATOM   5329  C CA  . ALA   C  1 349 ? -4.16774  26.38248  6.55529   1.000 25.18125  ?  349 ALA   G CA  1 
ATOM   5330  C C   . ALA   C  1 349 ? -4.13848  26.78580  8.02695   1.000 28.36324  ?  349 ALA   G C   1 
ATOM   5331  O O   . ALA   C  1 349 ? -4.08117  27.97366  8.37109   1.000 33.29904  ?  349 ALA   G O   1 
ATOM   5332  C CB  . ALA   C  1 349 ? -2.73733  26.08748  6.09235   1.000 10.38192  ?  349 ALA   G CB  1 
ATOM   5333  N N   . ALA   C  1 350 ? -4.17291  25.78052  8.90326   1.000 21.72565  ?  350 ALA   G N   1 
ATOM   5334  C CA  . ALA   C  1 350 ? -3.86687  26.02316  10.30973  1.000 24.21202  ?  350 ALA   G CA  1 
ATOM   5335  C C   . ALA   C  1 350 ? -2.56509  26.81260  10.43568  1.000 30.15131  ?  350 ALA   G C   1 
ATOM   5336  O O   . ALA   C  1 350 ? -1.53123  26.43077  9.87697   1.000 23.68089  ?  350 ALA   G O   1 
ATOM   5337  C CB  . ALA   C  1 350 ? -3.75509  24.69860  11.05542  1.000 10.08564  ?  350 ALA   G CB  1 
ATOM   5338  N N   . ARG   C  1 351 ? -2.62603  27.92625  11.15695  1.000 18.06072  ?  351 ARG   G N   1 
ATOM   5339  C CA  . ARG   C  1 351 ? -1.54828  28.90018  11.10855  1.000 28.31486  ?  351 ARG   G CA  1 
ATOM   5340  C C   . ARG   C  1 351 ? -1.62363  29.79053  12.34025  1.000 20.65172  ?  351 ARG   G C   1 
ATOM   5341  O O   . ARG   C  1 351 ? -2.65011  29.85036  13.03313  1.000 34.88704  ?  351 ARG   G O   1 
ATOM   5342  C CB  . ARG   C  1 351 ? -1.61492  29.73612  9.81502   1.000 14.03501  ?  351 ARG   G CB  1 
ATOM   5343  C CG  . ARG   C  1 351 ? -2.86511  30.57887  9.69454   1.000 14.04074  ?  351 ARG   G CG  1 
ATOM   5344  C CD  . ARG   C  1 351 ? -3.10997  31.02454  8.26199   1.000 21.95583  ?  351 ARG   G CD  1 
ATOM   5345  N NE  . ARG   C  1 351 ? -4.27446  31.89845  8.16300   1.000 23.51992  ?  351 ARG   G NE  1 
ATOM   5346  C CZ  . ARG   C  1 351 ? -5.53332  31.47545  8.12000   1.000 45.04139  ?  351 ARG   G CZ  1 
ATOM   5347  N NH1 . ARG   C  1 351 ? -5.84115  30.18646  8.16209   1.000 23.79026  ?  351 ARG   G NH1 1 
ATOM   5348  N NH2 . ARG   C  1 351 ? -6.51209  32.36869  8.02808   1.000 19.15718  ?  351 ARG   G NH2 1 
ATOM   5349  N N   . GLN   C  1 352 ? -0.50654  30.46519  12.61767  1.000 21.08005  ?  352 GLN   G N   1 
ATOM   5350  C CA  . GLN   C  1 352 ? -0.44925  31.47166  13.66993  1.000 14.43969  ?  352 GLN   G CA  1 
ATOM   5351  C C   . GLN   C  1 352 ? -0.00908  32.78814  13.05587  1.000 26.61592  ?  352 GLN   G C   1 
ATOM   5352  O O   . GLN   C  1 352 ? 0.96468   32.82957  12.28902  1.000 25.49457  ?  352 GLN   G O   1 
ATOM   5353  C CB  . GLN   C  1 352 ? 0.49931   31.08440  14.79423  1.000 24.60471  ?  352 GLN   G CB  1 
ATOM   5354  C CG  . GLN   C  1 352 ? 0.61187   32.15954  15.86312  1.000 19.65822  ?  352 GLN   G CG  1 
ATOM   5355  C CD  . GLN   C  1 352 ? 1.65108   31.79943  16.91469  1.000 28.00453  ?  352 GLN   G CD  1 
ATOM   5356  O OE1 . GLN   C  1 352 ? 2.74653   32.35563  16.93604  1.000 30.06347  ?  352 GLN   G OE1 1 
ATOM   5357  N NE2 . GLN   C  1 352 ? 1.31410   30.85239  17.78146  1.000 17.16972  ?  352 GLN   G NE2 1 
ATOM   5358  N N   . ILE   C  1 353 ? -0.76370  33.84232  13.35309  1.000 23.64666  ?  353 ILE   G N   1 
ATOM   5359  C CA  . ILE   C  1 353 ? -0.48735  35.19399  12.88208  1.000 26.46967  ?  353 ILE   G CA  1 
ATOM   5360  C C   . ILE   C  1 353 ? 0.15948   35.94669  14.02768  1.000 19.48663  ?  353 ILE   G C   1 
ATOM   5361  O O   . ILE   C  1 353 ? -0.34018  35.90480  15.16209  1.000 33.57694  ?  353 ILE   G O   1 
ATOM   5362  C CB  . ILE   C  1 353 ? -1.77904  35.90498  12.44736  1.000 24.37170  ?  353 ILE   G CB  1 
ATOM   5363  C CG1 . ILE   C  1 353 ? -2.47962  35.13966  11.32043  1.000 31.61350  ?  353 ILE   G CG1 1 
ATOM   5364  C CG2 . ILE   C  1 353 ? -1.48174  37.36235  12.10609  1.000 15.23531  ?  353 ILE   G CG2 1 
ATOM   5365  C CD1 . ILE   C  1 353 ? -3.95675  35.43405  11.23467  1.000 11.78486  ?  353 ILE   G CD1 1 
ATOM   5366  N N   . MET   C  1 354 ? 1.26198   36.63428  13.75270  1.000 20.09164  ?  354 MET   G N   1 
ATOM   5367  C CA  . MET   C  1 354 ? 1.94010   37.40754  14.78785  1.000 25.39845  ?  354 MET   G CA  1 
ATOM   5368  C C   . MET   C  1 354 ? 2.21243   38.80927  14.26130  1.000 30.49284  ?  354 MET   G C   1 
ATOM   5369  O O   . MET   C  1 354 ? 2.88746   38.97076  13.23644  1.000 31.96302  ?  354 MET   G O   1 
ATOM   5370  C CB  . MET   C  1 354 ? 3.22949   36.71588  15.22537  1.000 14.41457  ?  354 MET   G CB  1 
ATOM   5371  C CG  . MET   C  1 354 ? 3.88564   37.31289  16.46210  1.000 36.25702  ?  354 MET   G CG  1 
ATOM   5372  S SD  . MET   C  1 354 ? 5.39775   36.42992  16.87948  1.000 33.49601  ?  354 MET   G SD  1 
ATOM   5373  C CE  . MET   C  1 354 ? 4.69041   34.92555  17.56507  1.000 31.70238  ?  354 MET   G CE  1 
ATOM   5374  N N   . PHE   C  1 355 ? 1.65518   39.81720  14.93413  1.000 28.83294  ?  355 PHE   G N   1 
ATOM   5375  C CA  . PHE   C  1 355 ? 1.89003   41.21650  14.58584  1.000 30.46396  ?  355 PHE   G CA  1 
ATOM   5376  C C   . PHE   C  1 355 ? 2.98393   41.77850  15.47753  1.000 29.20374  ?  355 PHE   G C   1 
ATOM   5377  O O   . PHE   C  1 355 ? 2.93526   41.61978  16.70483  1.000 33.81482  ?  355 PHE   G O   1 
ATOM   5378  C CB  . PHE   C  1 355 ? 0.61488   42.04590  14.73860  1.000 34.32213  ?  355 PHE   G CB  1 
ATOM   5379  C CG  . PHE   C  1 355 ? -0.41819  41.72466  13.72482  1.000 36.18153  ?  355 PHE   G CG  1 
ATOM   5380  C CD1 . PHE   C  1 355 ? -0.30967  42.22707  12.43672  1.000 23.22492  ?  355 PHE   G CD1 1 
ATOM   5381  C CD2 . PHE   C  1 355 ? -1.48380  40.90396  14.04275  1.000 31.91909  ?  355 PHE   G CD2 1 
ATOM   5382  C CE1 . PHE   C  1 355 ? -1.25726  41.93083  11.47253  1.000 36.10300  ?  355 PHE   G CE1 1 
ATOM   5383  C CE2 . PHE   C  1 355 ? -2.43552  40.60145  13.09055  1.000 19.08388  ?  355 PHE   G CE2 1 
ATOM   5384  C CZ  . PHE   C  1 355 ? -2.32707  41.12202  11.79904  1.000 20.64259  ?  355 PHE   G CZ  1 
ATOM   5385  N N   . ILE   C  1 356 ? 3.97135   42.42314  14.87051  1.000 24.34805  ?  356 ILE   G N   1 
ATOM   5386  C CA  . ILE   C  1 356 ? 5.07869   42.99325  15.62521  1.000 27.70723  ?  356 ILE   G CA  1 
ATOM   5387  C C   . ILE   C  1 356 ? 5.20417   44.46456  15.28300  1.000 40.64770  ?  356 ILE   G C   1 
ATOM   5388  O O   . ILE   C  1 356 ? 5.09964   44.84861  14.11003  1.000 27.38792  ?  356 ILE   G O   1 
ATOM   5389  C CB  . ILE   C  1 356 ? 6.40037   42.25347  15.35432  1.000 21.78827  ?  356 ILE   G CB  1 
ATOM   5390  C CG1 . ILE   C  1 356 ? 6.24161   40.77237  15.74731  1.000 21.08860  ?  356 ILE   G CG1 1 
ATOM   5391  C CG2 . ILE   C  1 356 ? 7.53777   42.94456  16.11594  1.000 24.82694  ?  356 ILE   G CG2 1 
ATOM   5392  C CD1 . ILE   C  1 356 ? 7.44428   39.89318  15.38956  1.000 15.19363  ?  356 ILE   G CD1 1 
ATOM   5393  N N   . GLU   C  1 357 ? 5.41085   45.29069  16.31399  1.000 16.58761  ?  357 GLU   G N   1 
ATOM   5394  C CA  . GLU   C  1 357 ? 5.69658   46.70983  16.12428  1.000 31.58036  ?  357 GLU   G CA  1 
ATOM   5395  C C   . GLU   C  1 357 ? 7.21001   46.92683  16.21746  1.000 29.78624  ?  357 GLU   G C   1 
ATOM   5396  O O   . GLU   C  1 357 ? 7.78709   46.90014  17.31475  1.000 28.47422  ?  357 GLU   G O   1 
ATOM   5397  C CB  . GLU   C  1 357 ? 4.94260   47.55180  17.14563  1.000 22.09562  ?  357 GLU   G CB  1 
ATOM   5398  C CG  . GLU   C  1 357 ? 5.18110   49.06109  17.01646  1.000 20.87566  ?  357 GLU   G CG  1 
ATOM   5399  C CD  . GLU   C  1 357 ? 4.42829   49.70457  15.85928  1.000 74.17563  ?  357 GLU   G CD  1 
ATOM   5400  O OE1 . GLU   C  1 357 ? 3.23614   49.36342  15.65319  1.000 56.70500  ?  357 GLU   G OE1 1 
ATOM   5401  O OE2 . GLU   C  1 357 ? 5.02784   50.56694  15.16774  1.000 43.78424  -1 357 GLU   G OE2 1 
ATOM   5402  N N   . ALA   C  1 358 ? 7.84336   47.12783  15.05659  1.000 16.62713  ?  358 ALA   G N   1 
ATOM   5403  C CA  . ALA   C  1 358 ? 9.28250   47.36555  14.98241  1.000 35.48880  ?  358 ALA   G CA  1 
ATOM   5404  C C   . ALA   C  1 358 ? 9.65468   48.63389  15.73045  1.000 29.91637  ?  358 ALA   G C   1 
ATOM   5405  O O   . ALA   C  1 358 ? 8.96634   49.65303  15.62546  1.000 55.91104  ?  358 ALA   G O   1 
ATOM   5406  C CB  . ALA   C  1 358 ? 9.73095   47.49768  13.52397  1.000 24.12925  ?  358 ALA   G CB  1 
ATOM   5407  N N   . ASP   C  1 359 ? 10.75547  48.56584  16.48804  1.000 43.26884  ?  359 ASP   G N   1 
ATOM   5408  C CA  . ASP   C  1 359 ? 11.26884  49.75901  17.16052  1.000 38.58031  ?  359 ASP   G CA  1 
ATOM   5409  C C   . ASP   C  1 359 ? 11.54303  50.87885  16.15991  1.000 20.73345  ?  359 ASP   G C   1 
ATOM   5410  O O   . ASP   C  1 359 ? 11.31553  52.05809  16.45451  1.000 27.49698  ?  359 ASP   G O   1 
ATOM   5411  C CB  . ASP   C  1 359 ? 12.53980  49.43161  17.95591  1.000 17.64358  ?  359 ASP   G CB  1 
ATOM   5412  C CG  . ASP   C  1 359 ? 12.27737  48.51358  19.15798  1.000 54.93270  ?  359 ASP   G CG  1 
ATOM   5413  O OD1 . ASP   C  1 359 ? 11.09716  48.33804  19.54013  1.000 34.95720  ?  359 ASP   G OD1 1 
ATOM   5414  O OD2 . ASP   C  1 359 ? 13.25716  47.94850  19.71097  1.000 28.66753  -1 359 ASP   G OD2 1 
ATOM   5415  N N   . ASN   C  1 360 ? 12.01480  50.53440  14.97052  1.000 26.68419  ?  360 ASN   G N   1 
ATOM   5416  C CA  . ASN   C  1 360 ? 12.25320  51.53581  13.93799  1.000 17.93622  ?  360 ASN   G CA  1 
ATOM   5417  C C   . ASN   C  1 360 ? 10.91496  51.95949  13.33254  1.000 28.90125  ?  360 ASN   G C   1 
ATOM   5418  O O   . ASN   C  1 360 ? 10.27718  51.18010  12.61144  1.000 39.57405  ?  360 ASN   G O   1 
ATOM   5419  C CB  . ASN   C  1 360 ? 13.19638  50.97606  12.87464  1.000 19.21676  ?  360 ASN   G CB  1 
ATOM   5420  C CG  . ASN   C  1 360 ? 13.67006  52.02927  11.91834  1.000 38.00271  ?  360 ASN   G CG  1 
ATOM   5421  O OD1 . ASN   C  1 360 ? 12.88441  52.85938  11.44547  1.000 41.10707  ?  360 ASN   G OD1 1 
ATOM   5422  N ND2 . ASN   C  1 360 ? 14.97034  52.02124  11.63229  1.000 43.96574  ?  360 ASN   G ND2 1 
ATOM   5423  N N   . LYS   C  1 361 ? 10.50611  53.20520  13.60058  1.000 38.74357  ?  361 LYS   G N   1 
ATOM   5424  C CA  . LYS   C  1 361 ? 9.20548   53.69624  13.14994  1.000 46.51244  ?  361 LYS   G CA  1 
ATOM   5425  C C   . LYS   C  1 361 ? 9.04914   53.65076  11.63279  1.000 18.82955  ?  361 LYS   G C   1 
ATOM   5426  O O   . LYS   C  1 361 ? 7.91507   53.57288  11.14118  1.000 69.21284  ?  361 LYS   G O   1 
ATOM   5427  C CB  . LYS   C  1 361 ? 8.97500   55.12297  13.66496  1.000 22.98609  ?  361 LYS   G CB  1 
ATOM   5428  C CG  . LYS   C  1 361 ? 8.57405   55.09985  15.09585  1.000 26.73988  ?  361 LYS   G CG  1 
ATOM   5429  C CD  . LYS   C  1 361 ? 8.40116   56.46839  15.67996  1.000 8.77222   ?  361 LYS   G CD  1 
ATOM   5430  C CE  . LYS   C  1 361 ? 7.64336   56.39661  17.03762  1.000 90.88849  ?  361 LYS   G CE  1 
ATOM   5431  N NZ  . LYS   C  1 361 ? 6.18048   56.72118  16.92814  1.000 98.98978  ?  361 LYS   G NZ  1 
ATOM   5432  N N   . GLU   C  1 362 ? 10.15225  53.67241  10.88481  1.000 31.27433  ?  362 GLU   G N   1 
ATOM   5433  C CA  . GLU   C  1 362 ? 10.09737  53.58652  9.42789   1.000 26.73794  ?  362 GLU   G CA  1 
ATOM   5434  C C   . GLU   C  1 362 ? 9.76977   52.18232  8.93098   1.000 47.02018  ?  362 GLU   G C   1 
ATOM   5435  O O   . GLU   C  1 362 ? 9.48830   52.00935  7.73600   1.000 39.28267  ?  362 GLU   G O   1 
ATOM   5436  C CB  . GLU   C  1 362 ? 11.42930  54.04890  8.81825   1.000 35.59652  ?  362 GLU   G CB  1 
ATOM   5437  C CG  . GLU   C  1 362 ? 11.68492  55.56054  8.75310   1.000 23.88430  ?  362 GLU   G CG  1 
ATOM   5438  C CD  . GLU   C  1 362 ? 12.21953  56.02117  7.39166   1.000 103.09786 ?  362 GLU   G CD  1 
ATOM   5439  O OE1 . GLU   C  1 362 ? 13.34460  55.63202  6.99898   1.000 101.55979 ?  362 GLU   G OE1 1 
ATOM   5440  O OE2 . GLU   C  1 362 ? 11.50622  56.79303  6.71134   1.000 99.53343  ?  362 GLU   G OE2 1 
ATOM   5441  N N   . ILE   C  1 363 ? 9.84291   51.18315  9.80652   1.000 28.26068  ?  363 ILE   G N   1 
ATOM   5442  C CA  . ILE   C  1 363 ? 9.40558   49.82984  9.50559   1.000 46.22868  ?  363 ILE   G CA  1 
ATOM   5443  C C   . ILE   C  1 363 ? 8.02805   49.56765  10.09864  1.000 34.72018  ?  363 ILE   G C   1 
ATOM   5444  O O   . ILE   C  1 363 ? 7.13317   49.05571  9.42248   1.000 43.07330  ?  363 ILE   G O   1 
ATOM   5445  C CB  . ILE   C  1 363 ? 10.46554  48.82450  10.02150  1.000 36.46517  ?  363 ILE   G CB  1 
ATOM   5446  C CG1 . ILE   C  1 363 ? 11.73579  48.90440  9.16885   1.000 30.37251  ?  363 ILE   G CG1 1 
ATOM   5447  C CG2 . ILE   C  1 363 ? 9.94945   47.40101  9.99036   1.000 16.24838  ?  363 ILE   G CG2 1 
ATOM   5448  C CD1 . ILE   C  1 363 ? 12.87045  48.01309  9.66791   1.000 33.77401  ?  363 ILE   G CD1 1 
ATOM   5449  N N   . GLY   C  1 364 ? 7.84720   49.96785  11.35083  1.000 29.90371  ?  364 GLY   G N   1 
ATOM   5450  C CA  . GLY   C  1 364 ? 6.54493   50.03525  11.94009  1.000 17.79945  ?  364 GLY   G CA  1 
ATOM   5451  C C   . GLY   C  1 364 ? 5.92195   48.67316  12.16705  1.000 63.04238  ?  364 GLY   G C   1 
ATOM   5452  O O   . GLY   C  1 364 ? 6.58411   47.69914  12.55131  1.000 27.63318  ?  364 GLY   G O   1 
ATOM   5453  N N   . LEU   C  1 365 ? 4.61243   48.61825  11.94031  1.000 41.33284  ?  365 LEU   G N   1 
ATOM   5454  C CA  . LEU   C  1 365 ? 3.87585   47.38134  12.13423  1.000 18.22079  ?  365 LEU   G CA  1 
ATOM   5455  C C   . LEU   C  1 365 ? 4.20112   46.41913  10.99842  1.000 42.87645  ?  365 LEU   G C   1 
ATOM   5456  O O   . LEU   C  1 365 ? 4.14459   46.79049  9.82041   1.000 30.17762  ?  365 LEU   G O   1 
ATOM   5457  C CB  . LEU   C  1 365 ? 2.37302   47.66508  12.19156  1.000 32.32364  ?  365 LEU   G CB  1 
ATOM   5458  C CG  . LEU   C  1 365 ? 1.50813   46.48837  12.65097  1.000 35.88214  ?  365 LEU   G CG  1 
ATOM   5459  C CD1 . LEU   C  1 365 ? 1.89316   46.08574  14.07811  1.000 23.11662  ?  365 LEU   G CD1 1 
ATOM   5460  C CD2 . LEU   C  1 365 ? 0.04005   46.83757  12.54198  1.000 22.15394  ?  365 LEU   G CD2 1 
ATOM   5461  N N   . ILE   C  1 366 ? 4.59099   45.19552  11.35510  1.000 13.52487  ?  366 ILE   G N   1 
ATOM   5462  C CA  . ILE   C  1 366 ? 4.80589   44.12754  10.39023  1.000 27.85317  ?  366 ILE   G CA  1 
ATOM   5463  C C   . ILE   C  1 366 ? 3.96226   42.95034  10.84437  1.000 30.16516  ?  366 ILE   G C   1 
ATOM   5464  O O   . ILE   C  1 366 ? 3.45028   42.92117  11.96692  1.000 25.68969  ?  366 ILE   G O   1 
ATOM   5465  C CB  . ILE   C  1 366 ? 6.29009   43.70405  10.25758  1.000 21.21526  ?  366 ILE   G CB  1 
ATOM   5466  C CG1 . ILE   C  1 366 ? 6.78258   43.06405  11.54897  1.000 24.73964  ?  366 ILE   G CG1 1 
ATOM   5467  C CG2 . ILE   C  1 366 ? 7.18118   44.86909  9.88449   1.000 13.15867  ?  366 ILE   G CG2 1 
ATOM   5468  C CD1 . ILE   C  1 366 ? 8.03060   42.25685  11.35075  1.000 25.50983  ?  366 ILE   G CD1 1 
ATOM   5469  N N   . PHE   C  1 367 ? 3.81968   41.96451  9.96634   1.000 25.80856  ?  367 PHE   G N   1 
ATOM   5470  C CA  . PHE   C  1 367 ? 3.21888   40.71865  10.40958  1.000 22.77700  ?  367 PHE   G CA  1 
ATOM   5471  C C   . PHE   C  1 367 ? 4.06972   39.53775  9.96464   1.000 32.05192  ?  367 PHE   G C   1 
ATOM   5472  O O   . PHE   C  1 367 ? 4.83893   39.60715  8.99995   1.000 27.55837  ?  367 PHE   G O   1 
ATOM   5473  C CB  . PHE   C  1 367 ? 1.71834   40.57098  9.95684   1.000 21.74503  ?  367 PHE   G CB  1 
ATOM   5474  C CG  . PHE   C  1 367 ? 1.50258   40.24163  8.48744   1.000 13.75001  ?  367 PHE   G CG  1 
ATOM   5475  C CD1 . PHE   C  1 367 ? 1.84322   38.98906  7.96757   1.000 30.04296  ?  367 PHE   G CD1 1 
ATOM   5476  C CD2 . PHE   C  1 367 ? 0.85501   41.15092  7.65046   1.000 25.19155  ?  367 PHE   G CD2 1 
ATOM   5477  C CE1 . PHE   C  1 367 ? 1.61189   38.67425  6.62733   1.000 14.19889  ?  367 PHE   G CE1 1 
ATOM   5478  C CE2 . PHE   C  1 367 ? 0.60141   40.84265  6.29845   1.000 23.25283  ?  367 PHE   G CE2 1 
ATOM   5479  C CZ  . PHE   C  1 367 ? 0.97382   39.60631  5.78391   1.000 19.97499  ?  367 PHE   G CZ  1 
ATOM   5480  N N   . LEU   C  1 368 ? 3.94671   38.47044  10.73179  1.000 28.40250  ?  368 LEU   G N   1 
ATOM   5481  C CA  . LEU   C  1 368 ? 4.45428   37.15556  10.40234  1.000 19.35848  ?  368 LEU   G CA  1 
ATOM   5482  C C   . LEU   C  1 368 ? 3.27003   36.19655  10.42963  1.000 20.10741  ?  368 LEU   G C   1 
ATOM   5483  O O   . LEU   C  1 368 ? 2.40779   36.29514  11.31221  1.000 28.61913  ?  368 LEU   G O   1 
ATOM   5484  C CB  . LEU   C  1 368 ? 5.52140   36.72782  11.41492  1.000 17.02319  ?  368 LEU   G CB  1 
ATOM   5485  C CG  . LEU   C  1 368 ? 6.86817   37.43101  11.30786  1.000 27.61944  ?  368 LEU   G CG  1 
ATOM   5486  C CD1 . LEU   C  1 368 ? 7.65431   37.22365  12.58846  1.000 23.40040  ?  368 LEU   G CD1 1 
ATOM   5487  C CD2 . LEU   C  1 368 ? 7.65676   36.88854  10.11484  1.000 25.05430  ?  368 LEU   G CD2 1 
ATOM   5488  N N   . VAL   C  1 369 ? 3.20086   35.28832  9.46008   1.000 19.95466  ?  369 VAL   G N   1 
ATOM   5489  C CA  . VAL   C  1 369 ? 2.26979   34.16474  9.52192   1.000 22.29459  ?  369 VAL   G CA  1 
ATOM   5490  C C   . VAL   C  1 369 ? 3.08604   32.87829  9.45606   1.000 19.77878  ?  369 VAL   G C   1 
ATOM   5491  O O   . VAL   C  1 369 ? 3.82334   32.65385  8.48562   1.000 29.22572  ?  369 VAL   G O   1 
ATOM   5492  C CB  . VAL   C  1 369 ? 1.22037   34.20249  8.39727   1.000 28.52613  ?  369 VAL   G CB  1 
ATOM   5493  C CG1 . VAL   C  1 369 ? 0.22533   33.03751  8.57670   1.000 18.29364  ?  369 VAL   G CG1 1 
ATOM   5494  C CG2 . VAL   C  1 369 ? 0.49752   35.53247  8.38024   1.000 25.68744  ?  369 VAL   G CG2 1 
ATOM   5495  N N   . PHE   C  1 370 ? 2.94763   32.02832  10.47162  1.000 28.53876  ?  370 PHE   G N   1 
ATOM   5496  C CA  . PHE   C  1 370 ? 3.57450   30.71066  10.45616  1.000 10.18383  ?  370 PHE   G CA  1 
ATOM   5497  C C   . PHE   C  1 370 ? 2.54908   29.68173  9.97950   1.000 24.02459  ?  370 PHE   G C   1 
ATOM   5498  O O   . PHE   C  1 370 ? 1.48537   29.51863  10.59249  1.000 22.24731  ?  370 PHE   G O   1 
ATOM   5499  C CB  . PHE   C  1 370 ? 4.14666   30.38340  11.83638  1.000 17.66764  ?  370 PHE   G CB  1 
ATOM   5500  C CG  . PHE   C  1 370 ? 5.20052   31.35416  12.26229  1.000 27.67521  ?  370 PHE   G CG  1 
ATOM   5501  C CD1 . PHE   C  1 370 ? 6.48294   31.27520  11.72884  1.000 18.20006  ?  370 PHE   G CD1 1 
ATOM   5502  C CD2 . PHE   C  1 370 ? 4.90100   32.39427  13.13537  1.000 32.46255  ?  370 PHE   G CD2 1 
ATOM   5503  C CE1 . PHE   C  1 370 ? 7.46529   32.20328  12.07832  1.000 28.35916  ?  370 PHE   G CE1 1 
ATOM   5504  C CE2 . PHE   C  1 370 ? 5.88765   33.32903  13.50360  1.000 16.84475  ?  370 PHE   G CE2 1 
ATOM   5505  C CZ  . PHE   C  1 370 ? 7.16394   33.23729  12.96588  1.000 27.85274  ?  370 PHE   G CZ  1 
ATOM   5506  N N   . ILE   C  1 371 ? 2.85688   29.01232  8.87125   1.000 23.84869  ?  371 ILE   G N   1 
ATOM   5507  C CA  . ILE   C  1 371 ? 1.86953   28.27427  8.08169   1.000 19.62740  ?  371 ILE   G CA  1 
ATOM   5508  C C   . ILE   C  1 371 ? 2.14339   26.77886  8.21665   1.000 20.54713  ?  371 ILE   G C   1 
ATOM   5509  O O   . ILE   C  1 371 ? 3.22489   26.29728  7.85026   1.000 30.45441  ?  371 ILE   G O   1 
ATOM   5510  C CB  . ILE   C  1 371 ? 1.90004   28.71738  6.60873   1.000 28.74287  ?  371 ILE   G CB  1 
ATOM   5511  C CG1 . ILE   C  1 371 ? 1.73563   30.24411  6.51375   1.000 18.33059  ?  371 ILE   G CG1 1 
ATOM   5512  C CG2 . ILE   C  1 371 ? 0.82762   27.98649  5.78867   1.000 14.21574  ?  371 ILE   G CG2 1 
ATOM   5513  C CD1 . ILE   C  1 371 ? 2.41475   30.84344  5.29801   1.000 16.19775  ?  371 ILE   G CD1 1 
ATOM   5514  N N   . GLY   C  1 372 ? 1.16022   26.04065  8.74217   1.000 28.56864  ?  372 GLY   G N   1 
ATOM   5515  C CA  . GLY   C  1 372 ? 1.29591   24.60138  8.85034   1.000 19.86625  ?  372 GLY   G CA  1 
ATOM   5516  C C   . GLY   C  1 372 ? 1.22278   23.90559  7.50194   1.000 28.19499  ?  372 GLY   G C   1 
ATOM   5517  O O   . GLY   C  1 372 ? 0.71872   24.44126  6.51421   1.000 28.36716  ?  372 GLY   G O   1 
ATOM   5518  N N   . MET   C  1 373 ? 1.76752   22.69419  7.46858   1.000 21.98246  ?  373 MET   G N   1 
ATOM   5519  C CA  . MET   C  1 373 ? 1.70319   21.83066  6.29500   1.000 35.01796  ?  373 MET   G CA  1 
ATOM   5520  C C   . MET   C  1 373 ? 1.52847   20.40654  6.78007   1.000 32.76981  ?  373 MET   G C   1 
ATOM   5521  O O   . MET   C  1 373 ? 2.38646   19.89894  7.51417   1.000 28.06191  ?  373 MET   G O   1 
ATOM   5522  C CB  . MET   C  1 373 ? 2.95796   21.94147  5.43379   1.000 15.02163  ?  373 MET   G CB  1 
ATOM   5523  C CG  . MET   C  1 373 ? 3.14244   23.31556  4.86025   1.000 36.84564  ?  373 MET   G CG  1 
ATOM   5524  S SD  . MET   C  1 373 ? 4.69988   23.49875  3.94269   1.000 30.35569  ?  373 MET   G SD  1 
ATOM   5525  C CE  . MET   C  1 373 ? 4.61375   22.09895  2.82602   1.000 6.13710   ?  373 MET   G CE  1 
ATOM   5526  N N   . THR   C  1 374 ? 0.42840   19.77200  6.35319   1.000 20.54289  ?  374 THR   G N   1 
ATOM   5527  C CA  . THR   C  1 374 ? 0.03004   18.42765  6.77359   1.000 21.91458  ?  374 THR   G CA  1 
ATOM   5528  C C   . THR   C  1 374 ? 0.30258   18.22719  8.26504   1.000 18.82317  ?  374 THR   G C   1 
ATOM   5529  O O   . THR   C  1 374 ? -0.14743  19.03260  9.08392   1.000 29.44466  ?  374 THR   G O   1 
ATOM   5530  C CB  . THR   C  1 374 ? 0.70887   17.35359  5.88952   1.000 30.89239  ?  374 THR   G CB  1 
ATOM   5531  O OG1 . THR   C  1 374 ? 2.13906   17.36046  6.04256   1.000 25.84485  ?  374 THR   G OG1 1 
ATOM   5532  C CG2 . THR   C  1 374 ? 0.38682   17.61155  4.42688   1.000 15.46535  ?  374 THR   G CG2 1 
ATOM   5533  N N   . GLU   C  1 375 ? 1.04580   17.18923  8.64059   1.000 31.55841  ?  375 GLU   G N   1 
ATOM   5534  C CA  . GLU   C  1 375 ? 1.21573   16.88590  10.06171  1.000 19.08985  ?  375 GLU   G CA  1 
ATOM   5535  C C   . GLU   C  1 375 ? 2.16812   17.83639  10.79940  1.000 33.93695  ?  375 GLU   G C   1 
ATOM   5536  O O   . GLU   C  1 375 ? 2.22551   17.78753  12.03672  1.000 20.03052  ?  375 GLU   G O   1 
ATOM   5537  C CB  . GLU   C  1 375 ? 1.71167   15.44762  10.23161  1.000 31.94757  ?  375 GLU   G CB  1 
ATOM   5538  C CG  . GLU   C  1 375 ? 3.07973   15.18054  9.55662   1.000 20.60380  ?  375 GLU   G CG  1 
ATOM   5539  C CD  . GLU   C  1 375 ? 2.94328   14.45663  8.20154   1.000 30.96526  ?  375 GLU   G CD  1 
ATOM   5540  O OE1 . GLU   C  1 375 ? 2.36666   15.04332  7.25534   1.000 36.29908  ?  375 GLU   G OE1 1 
ATOM   5541  O OE2 . GLU   C  1 375 ? 3.41350   13.29458  8.08804   1.000 35.34181  -1 375 GLU   G OE2 1 
ATOM   5542  N N   . ILE   C  1 376 ? 2.92998   18.68167  10.09999  1.000 19.07052  ?  376 ILE   G N   1 
ATOM   5543  C CA  . ILE   C  1 376 ? 3.74586   19.67365  10.79817  1.000 19.29623  ?  376 ILE   G CA  1 
ATOM   5544  C C   . ILE   C  1 376 ? 2.98699   20.99748  10.82157  1.000 23.16695  ?  376 ILE   G C   1 
ATOM   5545  O O   . ILE   C  1 376 ? 3.25743   21.90315  10.02506  1.000 30.72547  ?  376 ILE   G O   1 
ATOM   5546  C CB  . ILE   C  1 376 ? 5.13537   19.81535  10.15102  1.000 30.21610  ?  376 ILE   G CB  1 
ATOM   5547  C CG1 . ILE   C  1 376 ? 5.80380   18.43404  10.07042  1.000 19.64861  ?  376 ILE   G CG1 1 
ATOM   5548  C CG2 . ILE   C  1 376 ? 5.99469   20.82970  10.92304  1.000 8.28935   ?  376 ILE   G CG2 1 
ATOM   5549  C CD1 . ILE   C  1 376 ? 7.06034   18.40243  9.20158   1.000 40.47809  ?  376 ILE   G CD1 1 
ATOM   5550  N N   . SER   C  1 377 ? 2.01748   21.11485  11.73064  1.000 20.08797  ?  377 SER   G N   1 
ATOM   5551  C CA  . SER   C  1 377 ? 1.08634   22.23361  11.69746  1.000 33.62684  ?  377 SER   G CA  1 
ATOM   5552  C C   . SER   C  1 377 ? 0.85884   22.88671  13.05231  1.000 17.61344  ?  377 SER   G C   1 
ATOM   5553  O O   . SER   C  1 377 ? 0.04639   23.81356  13.14590  1.000 41.84850  ?  377 SER   G O   1 
ATOM   5554  C CB  . SER   C  1 377 ? -0.25849  21.78715  11.10650  1.000 11.46661  ?  377 SER   G CB  1 
ATOM   5555  O OG  . SER   C  1 377 ? -0.10606  21.56897  9.71246   1.000 17.54426  ?  377 SER   G OG  1 
ATOM   5556  N N   . THR   C  1 378 ? 1.55736   22.44973  14.09168  1.000 32.73016  ?  378 THR   G N   1 
ATOM   5557  C CA  . THR   C  1 378 ? 1.48361   23.11940  15.38125  1.000 18.85570  ?  378 THR   G CA  1 
ATOM   5558  C C   . THR   C  1 378 ? 2.45295   24.30476  15.43410  1.000 34.21582  ?  378 THR   G C   1 
ATOM   5559  O O   . THR   C  1 378 ? 3.64632   24.17505  15.11524  1.000 25.95004  ?  378 THR   G O   1 
ATOM   5560  C CB  . THR   C  1 378 ? 1.77402   22.13073  16.50937  1.000 31.37848  ?  378 THR   G CB  1 
ATOM   5561  O OG1 . THR   C  1 378 ? 0.70425   21.17893  16.58906  1.000 26.17258  ?  378 THR   G OG1 1 
ATOM   5562  C CG2 . THR   C  1 378 ? 1.85863   22.86663  17.81458  1.000 6.59020   ?  378 THR   G CG2 1 
ATOM   5563  N N   . CYS   C  1 379 ? 1.93017   25.46256  15.84259  1.000 24.02883  ?  379 CYS   G N   1 
ATOM   5564  C CA  . CYS   C  1 379 ? 2.67505   26.72090  15.87567  1.000 22.31100  ?  379 CYS   G CA  1 
ATOM   5565  C C   . CYS   C  1 379 ? 2.71833   27.18315  17.32707  1.000 30.38105  ?  379 CYS   G C   1 
ATOM   5566  O O   . CYS   C  1 379 ? 1.75287   27.76310  17.83551  1.000 35.74364  ?  379 CYS   G O   1 
ATOM   5567  C CB  . CYS   C  1 379 ? 2.02216   27.76782  14.97555  1.000 22.89228  ?  379 CYS   G CB  1 
ATOM   5568  S SG  . CYS   C  1 379 ? 1.88926   27.25573  13.23864  1.000 34.41750  ?  379 CYS   G SG  1 
ATOM   5569  N N   . GLU   C  1 380 ? 3.83046   26.92118  18.00220  1.000 25.65741  ?  380 GLU   G N   1 
ATOM   5570  C CA  . GLU   C  1 380 ? 4.00646   27.35783  19.37937  1.000 11.16122  ?  380 GLU   G CA  1 
ATOM   5571  C C   . GLU   C  1 380 ? 4.77546   28.67326  19.41087  1.000 27.45390  ?  380 GLU   G C   1 
ATOM   5572  O O   . GLU   C  1 380 ? 5.94166   28.72809  18.99315  1.000 26.31360  ?  380 GLU   G O   1 
ATOM   5573  C CB  . GLU   C  1 380 ? 4.73814   26.31883  20.22050  1.000 22.63780  ?  380 GLU   G CB  1 
ATOM   5574  C CG  . GLU   C  1 380 ? 4.95643   26.85033  21.61212  1.000 35.40862  ?  380 GLU   G CG  1 
ATOM   5575  C CD  . GLU   C  1 380 ? 5.78096   25.95057  22.48356  1.000 31.18305  ?  380 GLU   G CD  1 
ATOM   5576  O OE1 . GLU   C  1 380 ? 6.36629   24.97784  21.95418  1.000 36.20901  ?  380 GLU   G OE1 1 
ATOM   5577  O OE2 . GLU   C  1 380 ? 5.83842   26.23779  23.69977  1.000 43.29943  -1 380 GLU   G OE2 1 
ATOM   5578  N N   . ALA   C  1 381 ? 4.11789   29.72489  19.90466  1.000 19.20224  ?  381 ALA   G N   1 
ATOM   5579  C CA  . ALA   C  1 381 ? 4.80855   30.95201  20.28262  1.000 37.70040  ?  381 ALA   G CA  1 
ATOM   5580  C C   . ALA   C  1 381 ? 5.43620   30.78054  21.66623  1.000 28.09018  ?  381 ALA   G C   1 
ATOM   5581  O O   . ALA   C  1 381 ? 4.79221   30.27525  22.59632  1.000 28.70571  ?  381 ALA   G O   1 
ATOM   5582  C CB  . ALA   C  1 381 ? 3.83726   32.13777  20.28261  1.000 18.18203  ?  381 ALA   G CB  1 
ATOM   5583  N N   . THR   C  1 382 ? 6.69693   31.18982  21.80159  1.000 23.75262  ?  382 THR   G N   1 
ATOM   5584  C CA  . THR   C  1 382 ? 7.34307   31.28168  23.10908  1.000 23.33467  ?  382 THR   G CA  1 
ATOM   5585  C C   . THR   C  1 382 ? 7.53032   32.72891  23.56626  1.000 18.46788  ?  382 THR   G C   1 
ATOM   5586  O O   . THR   C  1 382 ? 8.33623   32.99887  24.46294  1.000 46.00996  ?  382 THR   G O   1 
ATOM   5587  C CB  . THR   C  1 382 ? 8.68065   30.55056  23.08389  1.000 13.04712  ?  382 THR   G CB  1 
ATOM   5588  O OG1 . THR   C  1 382 ? 9.52751   31.11987  22.06373  1.000 21.93883  ?  382 THR   G OG1 1 
ATOM   5589  C CG2 . THR   C  1 382 ? 8.45028   29.06336  22.80340  1.000 23.83476  ?  382 THR   G CG2 1 
ATOM   5590  N N   . VAL   C  1 383 ? 6.82725   33.66538  22.93356  1.000 29.13782  ?  383 VAL   G N   1 
ATOM   5591  C CA  . VAL   C  1 383 ? 6.79352   35.05677  23.35035  1.000 18.47605  ?  383 VAL   G CA  1 
ATOM   5592  C C   . VAL   C  1 383 ? 5.34869   35.40408  23.68700  1.000 32.47805  ?  383 VAL   G C   1 
ATOM   5593  O O   . VAL   C  1 383 ? 4.41121   34.68015  23.34390  1.000 28.22986  ?  383 VAL   G O   1 
ATOM   5594  C CB  . VAL   C  1 383 ? 7.34688   36.02104  22.28276  1.000 39.18842  ?  383 VAL   G CB  1 
ATOM   5595  C CG1 . VAL   C  1 383 ? 8.81133   35.76273  22.04354  1.000 19.24170  ?  383 VAL   G CG1 1 
ATOM   5596  C CG2 . VAL   C  1 383 ? 6.55161   35.89726  20.99125  1.000 23.95076  ?  383 VAL   G CG2 1 
ATOM   5597  N N   . SER   C  1 384 ? 5.17948   36.52601  24.37582  1.000 39.16626  ?  384 SER   G N   1 
ATOM   5598  C CA  . SER   C  1 384 ? 3.87141   36.95403  24.84866  1.000 19.68718  ?  384 SER   G CA  1 
ATOM   5599  C C   . SER   C  1 384 ? 3.53158   38.30798  24.24929  1.000 44.08451  ?  384 SER   G C   1 
ATOM   5600  O O   . SER   C  1 384 ? 4.42400   39.09523  23.89830  1.000 32.85062  ?  384 SER   G O   1 
ATOM   5601  C CB  . SER   C  1 384 ? 3.83924   37.03582  26.37628  1.000 22.08392  ?  384 SER   G CB  1 
ATOM   5602  O OG  . SER   C  1 384 ? 4.30382   35.81545  26.93903  1.000 49.28962  ?  384 SER   G OG  1 
ATOM   5603  N N   . GLU   C  1 385 ? 2.23613   38.57868  24.11899  1.000 27.11800  ?  385 GLU   G N   1 
ATOM   5604  C CA  . GLU   C  1 385 ? 1.84888   39.91265  23.68179  1.000 35.84632  ?  385 GLU   G CA  1 
ATOM   5605  C C   . GLU   C  1 385 ? 2.41569   40.94237  24.66035  1.000 35.46352  ?  385 GLU   G C   1 
ATOM   5606  O O   . GLU   C  1 385 ? 2.45693   40.72293  25.87748  1.000 33.41949  ?  385 GLU   G O   1 
ATOM   5607  C CB  . GLU   C  1 385 ? 0.32882   40.01838  23.57269  1.000 13.78635  ?  385 GLU   G CB  1 
ATOM   5608  C CG  . GLU   C  1 385 ? -0.29920  38.96737  22.64991  1.000 27.58600  ?  385 GLU   G CG  1 
ATOM   5609  C CD  . GLU   C  1 385 ? -1.78720  39.20758  22.39987  1.000 44.49535  ?  385 GLU   G CD  1 
ATOM   5610  O OE1 . GLU   C  1 385 ? -2.41765  39.89587  23.23787  1.000 42.88441  ?  385 GLU   G OE1 1 
ATOM   5611  O OE2 . GLU   C  1 385 ? -2.32092  38.72069  21.36579  1.000 30.04607  -1 385 GLU   G OE2 1 
ATOM   5612  N N   . GLY   C  1 386 ? 2.92895   42.03798  24.11535  1.000 34.25000  ?  386 GLY   G N   1 
ATOM   5613  C CA  . GLY   C  1 386 ? 3.53695   43.08219  24.91154  1.000 20.40665  ?  386 GLY   G CA  1 
ATOM   5614  C C   . GLY   C  1 386 ? 5.02863   42.93101  25.14760  1.000 39.11585  ?  386 GLY   G C   1 
ATOM   5615  O O   . GLY   C  1 386 ? 5.70076   43.91783  25.45356  1.000 33.70064  ?  386 GLY   G O   1 
ATOM   5616  N N   . GLN   C  1 387 ? 5.56029   41.72840  25.01443  1.000 31.69139  ?  387 GLN   G N   1 
ATOM   5617  C CA  . GLN   C  1 387 ? 6.97866   41.48446  25.22496  1.000 28.38211  ?  387 GLN   G CA  1 
ATOM   5618  C C   . GLN   C  1 387 ? 7.83573   42.17465  24.16056  1.000 47.61729  ?  387 GLN   G C   1 
ATOM   5619  O O   . GLN   C  1 387 ? 7.41723   42.35113  23.00872  1.000 40.75377  ?  387 GLN   G O   1 
ATOM   5620  C CB  . GLN   C  1 387 ? 7.21882   39.97888  25.20885  1.000 27.23779  ?  387 GLN   G CB  1 
ATOM   5621  C CG  . GLN   C  1 387 ? 8.62595   39.53647  25.35300  1.000 27.80149  ?  387 GLN   G CG  1 
ATOM   5622  C CD  . GLN   C  1 387 ? 8.69934   38.03447  25.39050  1.000 35.80196  ?  387 GLN   G CD  1 
ATOM   5623  O OE1 . GLN   C  1 387 ? 7.68199   37.35330  25.59835  1.000 40.76512  ?  387 GLN   G OE1 1 
ATOM   5624  N NE2 . GLN   C  1 387 ? 9.89404   37.49840  25.16253  1.000 29.18212  ?  387 GLN   G NE2 1 
ATOM   5625  N N   . HIS   C  1 388 ? 9.04709   42.58032  24.55914  1.000 26.85236  ?  388 HIS   G N   1 
ATOM   5626  C CA  . HIS   C  1 388 ? 10.03056  43.11882  23.62509  1.000 38.14619  ?  388 HIS   G CA  1 
ATOM   5627  C C   . HIS   C  1 388 ? 11.02281  42.03032  23.23975  1.000 51.79583  ?  388 HIS   G C   1 
ATOM   5628  O O   . HIS   C  1 388 ? 11.35877  41.16098  24.05306  1.000 25.87889  ?  388 HIS   G O   1 
ATOM   5629  C CB  . HIS   C  1 388 ? 10.78539  44.30097  24.21842  1.000 16.16329  ?  388 HIS   G CB  1 
ATOM   5630  C CG  . HIS   C  1 388 ? 11.74189  44.95035  23.26788  1.000 33.49586  ?  388 HIS   G CG  1 
ATOM   5631  N ND1 . HIS   C  1 388 ? 13.05531  44.54232  23.12978  1.000 34.45432  ?  388 HIS   G ND1 1 
ATOM   5632  C CD2 . HIS   C  1 388 ? 11.57638  45.98503  22.40884  1.000 22.42712  ?  388 HIS   G CD2 1 
ATOM   5633  C CE1 . HIS   C  1 388 ? 13.65351  45.29339  22.22050  1.000 30.77003  ?  388 HIS   G CE1 1 
ATOM   5634  N NE2 . HIS   C  1 388 ? 12.77988  46.17937  21.77001  1.000 26.71109  ?  388 HIS   G NE2 1 
ATOM   5635  N N   . VAL   C  1 389 ? 11.47157  42.07128  21.98566  1.000 16.27767  ?  389 VAL   G N   1 
ATOM   5636  C CA  . VAL   C  1 389 ? 12.44404  41.11704  21.46323  1.000 28.68086  ?  389 VAL   G CA  1 
ATOM   5637  C C   . VAL   C  1 389 ? 13.41915  41.86410  20.56529  1.000 27.62445  ?  389 VAL   G C   1 
ATOM   5638  O O   . VAL   C  1 389 ? 13.10190  42.92071  20.00045  1.000 41.75795  ?  389 VAL   G O   1 
ATOM   5639  C CB  . VAL   C  1 389 ? 11.78739  39.93985  20.68490  1.000 33.86772  ?  389 VAL   G CB  1 
ATOM   5640  C CG1 . VAL   C  1 389 ? 10.87190  39.10108  21.60736  1.000 18.66650  ?  389 VAL   G CG1 1 
ATOM   5641  C CG2 . VAL   C  1 389 ? 11.01944  40.43838  19.47130  1.000 12.95390  ?  389 VAL   G CG2 1 
ATOM   5642  N N   . ASN   C  1 390 ? 14.61995  41.30230  20.45186  1.000 19.29143  ?  390 ASN   G N   1 
ATOM   5643  C CA  . ASN   C  1 390 ? 15.64194  41.75916  19.51920  1.000 22.75479  ?  390 ASN   G CA  1 
ATOM   5644  C C   . ASN   C  1 390 ? 15.71588  40.81440  18.33310  1.000 48.11768  ?  390 ASN   G C   1 
ATOM   5645  O O   . ASN   C  1 390 ? 15.48381  39.60600  18.46249  1.000 25.59154  ?  390 ASN   G O   1 
ATOM   5646  C CB  . ASN   C  1 390 ? 17.02044  41.84276  20.18640  1.000 35.45529  ?  390 ASN   G CB  1 
ATOM   5647  C CG  . ASN   C  1 390 ? 17.09353  42.94497  21.23072  1.000 29.00323  ?  390 ASN   G CG  1 
ATOM   5648  O OD1 . ASN   C  1 390 ? 16.61208  44.06828  21.01535  1.000 39.48732  ?  390 ASN   G OD1 1 
ATOM   5649  N ND2 . ASN   C  1 390 ? 17.66621  42.62130  22.37890  1.000 38.94010  ?  390 ASN   G ND2 1 
ATOM   5650  N N   . ARG   C  1 391 ? 16.02172  41.38919  17.17166  1.000 22.93248  ?  391 ARG   G N   1 
ATOM   5651  C CA  . ARG   C  1 391 ? 16.27283  40.62640  15.95783  1.000 33.52716  ?  391 ARG   G CA  1 
ATOM   5652  C C   . ARG   C  1 391 ? 17.16060  39.41745  16.25646  1.000 21.53449  ?  391 ARG   G C   1 
ATOM   5653  O O   . ARG   C  1 391 ? 18.24920  39.55760  16.82294  1.000 32.21412  ?  391 ARG   G O   1 
ATOM   5654  C CB  . ARG   C  1 391 ? 16.92196  41.55802  14.92854  1.000 12.90419  ?  391 ARG   G CB  1 
ATOM   5655  C CG  . ARG   C  1 391 ? 16.98679  41.05715  13.49442  1.000 22.57427  ?  391 ARG   G CG  1 
ATOM   5656  C CD  . ARG   C  1 391 ? 17.15699  42.21695  12.51275  1.000 32.16213  ?  391 ARG   G CD  1 
ATOM   5657  N NE  . ARG   C  1 391 ? 18.43137  42.91752  12.63172  1.000 24.52243  ?  391 ARG   G NE  1 
ATOM   5658  C CZ  . ARG   C  1 391 ? 19.49566  42.64400  11.88664  1.000 66.09197  ?  391 ARG   G CZ  1 
ATOM   5659  N NH1 . ARG   C  1 391 ? 19.49341  41.65261  11.01266  1.000 25.48741  ?  391 ARG   G NH1 1 
ATOM   5660  N NH2 . ARG   C  1 391 ? 20.59167  43.38103  12.01804  1.000 26.43525  ?  391 ARG   G NH2 1 
ATOM   5661  N N   . GLY   C  1 392 ? 16.64800  38.21192  15.95858  1.000 22.58980  ?  392 GLY   G N   1 
ATOM   5662  C CA  . GLY   C  1 392 ? 17.35890  36.95939  16.17126  1.000 19.01763  ?  392 GLY   G CA  1 
ATOM   5663  C C   . GLY   C  1 392 ? 16.94376  36.16518  17.39892  1.000 27.79863  ?  392 GLY   G C   1 
ATOM   5664  O O   . GLY   C  1 392 ? 17.35559  34.99783  17.52819  1.000 26.37435  ?  392 GLY   G O   1 
ATOM   5665  N N   . ASP   C  1 393 ? 16.13853  36.75107  18.29455  1.000 17.39700  ?  393 ASP   G N   1 
ATOM   5666  C CA  . ASP   C  1 393 ? 15.64244  36.03486  19.47074  1.000 30.08724  ?  393 ASP   G CA  1 
ATOM   5667  C C   . ASP   C  1 393 ? 14.57411  35.01053  19.07724  1.000 24.64268  ?  393 ASP   G C   1 
ATOM   5668  O O   . ASP   C  1 393 ? 13.95430  35.10078  18.01127  1.000 43.69755  ?  393 ASP   G O   1 
ATOM   5669  C CB  . ASP   C  1 393 ? 15.05273  37.01365  20.49555  1.000 20.72689  ?  393 ASP   G CB  1 
ATOM   5670  C CG  . ASP   C  1 393 ? 16.07488  38.03653  21.01962  1.000 49.61478  ?  393 ASP   G CG  1 
ATOM   5671  O OD1 . ASP   C  1 393 ? 17.28972  37.94204  20.71048  1.000 46.21684  ?  393 ASP   G OD1 1 
ATOM   5672  O OD2 . ASP   C  1 393 ? 15.64617  38.95226  21.75443  1.000 34.31758  -1 393 ASP   G OD2 1 
ATOM   5673  N N   . ASP   C  1 394 ? 14.33965  34.03765  19.96380  1.000 44.20799  ?  394 ASP   G N   1 
ATOM   5674  C CA  . ASP   C  1 394 ? 13.28721  33.05108  19.71415  1.000 19.92470  ?  394 ASP   G CA  1 
ATOM   5675  C C   . ASP   C  1 394 ? 11.91314  33.72017  19.68905  1.000 46.60705  ?  394 ASP   G C   1 
ATOM   5676  O O   . ASP   C  1 394 ? 11.58783  34.51583  20.57614  1.000 29.43197  ?  394 ASP   G O   1 
ATOM   5677  C CB  . ASP   C  1 394 ? 13.30105  31.95424  20.78467  1.000 39.42291  ?  394 ASP   G CB  1 
ATOM   5678  C CG  . ASP   C  1 394 ? 14.61727  31.19824  20.85044  1.000 28.92483  ?  394 ASP   G CG  1 
ATOM   5679  O OD1 . ASP   C  1 394 ? 15.24447  30.95065  19.78663  1.000 73.28388  ?  394 ASP   G OD1 1 
ATOM   5680  O OD2 . ASP   C  1 394 ? 15.00804  30.82514  21.97775  1.000 68.53398  -1 394 ASP   G OD2 1 
ATOM   5681  N N   . LEU   C  1 395 ? 11.10541  33.41222  18.66739  1.000 25.96562  ?  395 LEU   G N   1 
ATOM   5682  C CA  . LEU   C  1 395 ? 9.67933   33.72753  18.73741  1.000 44.90688  ?  395 LEU   G CA  1 
ATOM   5683  C C   . LEU   C  1 395 ? 8.84640   32.51201  19.07791  1.000 37.84197  ?  395 LEU   G C   1 
ATOM   5684  O O   . LEU   C  1 395 ? 7.76167   32.64646  19.66561  1.000 35.30705  ?  395 LEU   G O   1 
ATOM   5685  C CB  . LEU   C  1 395 ? 9.15279   34.29445  17.41565  1.000 22.37661  ?  395 LEU   G CB  1 
ATOM   5686  C CG  . LEU   C  1 395 ? 9.56042   35.68316  16.96247  1.000 36.85121  ?  395 LEU   G CG  1 
ATOM   5687  C CD1 . LEU   C  1 395 ? 8.86306   35.92986  15.66270  1.000 21.84825  ?  395 LEU   G CD1 1 
ATOM   5688  C CD2 . LEU   C  1 395 ? 9.19505   36.72909  18.00250  1.000 31.87848  ?  395 LEU   G CD2 1 
ATOM   5689  N N   . GLY   C  1 396 ? 9.33851   31.33837  18.70799  1.000 24.85856  ?  396 GLY   G N   1 
ATOM   5690  C CA  . GLY   C  1 396 ? 8.59648   30.11032  18.90140  1.000 33.25717  ?  396 GLY   G CA  1 
ATOM   5691  C C   . GLY   C  1 396 ? 9.12911   29.07020  17.94068  1.000 29.42529  ?  396 GLY   G C   1 
ATOM   5692  O O   . GLY   C  1 396 ? 10.27137  29.16418  17.47993  1.000 32.87638  ?  396 GLY   G O   1 
ATOM   5693  N N   . MET   C  1 397 ? 8.27283   28.10177  17.62354  1.000 25.19710  ?  397 MET   G N   1 
ATOM   5694  C CA  . MET   C  1 397 ? 8.72830   27.01566  16.76737  1.000 24.07400  ?  397 MET   G CA  1 
ATOM   5695  C C   . MET   C  1 397 ? 7.54334   26.22412  16.23635  1.000 39.58436  ?  397 MET   G C   1 
ATOM   5696  O O   . MET   C  1 397 ? 6.41333   26.34097  16.72444  1.000 28.81320  ?  397 MET   G O   1 
ATOM   5697  C CB  . MET   C  1 397 ? 9.67705   26.09229  17.52398  1.000 21.89831  ?  397 MET   G CB  1 
ATOM   5698  C CG  . MET   C  1 397 ? 8.96182   25.09567  18.41829  1.000 26.37917  ?  397 MET   G CG  1 
ATOM   5699  S SD  . MET   C  1 397 ? 10.05035  24.71042  19.77351  1.000 36.78019  ?  397 MET   G SD  1 
ATOM   5700  C CE  . MET   C  1 397 ? 9.90787   26.20207  20.73895  1.000 15.02583  ?  397 MET   G CE  1 
ATOM   5701  N N   . PHE   C  1 398 ? 7.83425   25.41289  15.21793  1.000 26.84644  ?  398 PHE   G N   1 
ATOM   5702  C CA  . PHE   C  1 398 ? 6.91798   24.42095  14.67906  1.000 20.12879  ?  398 PHE   G CA  1 
ATOM   5703  C C   . PHE   C  1 398 ? 7.03894   23.09012  15.43108  1.000 29.90817  ?  398 PHE   G C   1 
ATOM   5704  O O   . PHE   C  1 398 ? 8.10756   22.72385  15.92198  1.000 39.61863  ?  398 PHE   G O   1 
ATOM   5705  C CB  . PHE   C  1 398 ? 7.21469   24.16962  13.19811  1.000 20.21064  ?  398 PHE   G CB  1 
ATOM   5706  C CG  . PHE   C  1 398 ? 6.87902   25.30892  12.28912  1.000 33.85679  ?  398 PHE   G CG  1 
ATOM   5707  C CD1 . PHE   C  1 398 ? 5.54592   25.58604  11.95938  1.000 20.52458  ?  398 PHE   G CD1 1 
ATOM   5708  C CD2 . PHE   C  1 398 ? 7.89595   26.06726  11.69833  1.000 27.28273  ?  398 PHE   G CD2 1 
ATOM   5709  C CE1 . PHE   C  1 398 ? 5.22655   26.63332  11.08180  1.000 32.56464  ?  398 PHE   G CE1 1 
ATOM   5710  C CE2 . PHE   C  1 398 ? 7.59298   27.11966  10.80958  1.000 23.32743  ?  398 PHE   G CE2 1 
ATOM   5711  C CZ  . PHE   C  1 398 ? 6.25989   27.40313  10.50154  1.000 30.66350  ?  398 PHE   G CZ  1 
ATOM   5712  N N   . HIS   C  1 399 ? 5.93692   22.34423  15.48347  1.000 28.83829  ?  399 HIS   G N   1 
ATOM   5713  C CA  . HIS   C  1 399 ? 5.96679   20.96313  15.95202  1.000 37.23200  ?  399 HIS   G CA  1 
ATOM   5714  C C   . HIS   C  1 399 ? 5.09385   20.10877  15.04903  1.000 15.69126  ?  399 HIS   G C   1 
ATOM   5715  O O   . HIS   C  1 399 ? 4.11701   20.59103  14.47013  1.000 44.08982  ?  399 HIS   G O   1 
ATOM   5716  C CB  . HIS   C  1 399 ? 5.43045   20.75665  17.39801  1.000 13.19207  ?  399 HIS   G CB  1 
ATOM   5717  C CG  . HIS   C  1 399 ? 6.08634   21.60614  18.44357  1.000 16.94587  ?  399 HIS   G CG  1 
ATOM   5718  N ND1 . HIS   C  1 399 ? 7.22614   21.21746  19.11544  1.000 24.99078  ?  399 HIS   G ND1 1 
ATOM   5719  C CD2 . HIS   C  1 399 ? 5.73798   22.81274  18.95733  1.000 32.37408  ?  399 HIS   G CD2 1 
ATOM   5720  C CE1 . HIS   C  1 399 ? 7.56543   22.15829  19.98033  1.000 42.64385  ?  399 HIS   G CE1 1 
ATOM   5721  N NE2 . HIS   C  1 399 ? 6.67402   23.13259  19.91129  1.000 13.85481  ?  399 HIS   G NE2 1 
ATOM   5722  N N   . PHE   C  1 400 ? 5.42348   18.82021  14.97894  1.000 35.30048  ?  400 PHE   G N   1 
ATOM   5723  C CA  . PHE   C  1 400 ? 4.42982   17.83678  14.57661  1.000 16.76958  ?  400 PHE   G CA  1 
ATOM   5724  C C   . PHE   C  1 400 ? 3.21225   17.97920  15.48515  1.000 25.40012  ?  400 PHE   G C   1 
ATOM   5725  O O   . PHE   C  1 400 ? 3.34049   18.02845  16.71422  1.000 35.89019  ?  400 PHE   G O   1 
ATOM   5726  C CB  . PHE   C  1 400 ? 5.01289   16.42263  14.66585  1.000 34.44733  ?  400 PHE   G CB  1 
ATOM   5727  C CG  . PHE   C  1 400 ? 5.87615   16.04529  13.49758  1.000 14.37432  ?  400 PHE   G CG  1 
ATOM   5728  C CD1 . PHE   C  1 400 ? 7.14245   16.60998  13.33584  1.000 33.41857  ?  400 PHE   G CD1 1 
ATOM   5729  C CD2 . PHE   C  1 400 ? 5.42435   15.13271  12.54721  1.000 34.41163  ?  400 PHE   G CD2 1 
ATOM   5730  C CE1 . PHE   C  1 400 ? 7.93436   16.28471  12.24148  1.000 18.08648  ?  400 PHE   G CE1 1 
ATOM   5731  C CE2 . PHE   C  1 400 ? 6.22102   14.78706  11.44950  1.000 30.25753  ?  400 PHE   G CE2 1 
ATOM   5732  C CZ  . PHE   C  1 400 ? 7.47114   15.36850  11.29907  1.000 33.17259  ?  400 PHE   G CZ  1 
ATOM   5733  N N   . GLY   C  1 401 ? 2.04366   18.09271  14.87975  1.000 22.46170  ?  401 GLY   G N   1 
ATOM   5734  C CA  . GLY   C  1 401 ? 0.81435   18.27355  15.62762  1.000 18.39021  ?  401 GLY   G CA  1 
ATOM   5735  C C   . GLY   C  1 401 ? -0.19406  19.03763  14.79739  1.000 28.84941  ?  401 GLY   G C   1 
ATOM   5736  O O   . GLY   C  1 401 ? 0.05076   19.38113  13.64102  1.000 35.04224  ?  401 GLY   G O   1 
ATOM   5737  N N   . GLY   C  1 402 ? -1.34240  19.30204  15.42231  1.000 30.60617  ?  402 GLY   G N   1 
ATOM   5738  C CA  . GLY   C  1 402 ? -2.43215  20.01472  14.76104  1.000 23.21184  ?  402 GLY   G CA  1 
ATOM   5739  C C   . GLY   C  1 402 ? -2.35644  21.53226  14.89412  1.000 52.44997  ?  402 GLY   G C   1 
ATOM   5740  O O   . GLY   C  1 402 ? -3.08638  22.31479  14.24794  1.000 34.06806  ?  402 GLY   G O   1 
ATOM   5741  O OXT . GLY   C  1 402 ? -1.53017  22.02524  15.66983  1.000 43.25140  -1 402 GLY   G OXT 1 
ATOM   5742  N N   . SER   D  2 1   ? 6.00498   26.31387  6.81067   1.000 20.51185  ?  404 SER   H N   1 
ATOM   5743  C CA  . SER   D  2 1   ? 6.15531   27.50899  5.96899   1.000 15.63152  ?  404 SER   H CA  1 
ATOM   5744  C C   . SER   D  2 1   ? 5.95414   28.79510  6.77977   1.000 27.05673  ?  404 SER   H C   1 
ATOM   5745  O O   . SER   D  2 1   ? 5.33034   28.76695  7.83694   1.000 30.57216  ?  404 SER   H O   1 
ATOM   5746  C CB  . SER   D  2 1   ? 5.16988   27.45365  4.78302   1.000 21.90672  ?  404 SER   H CB  1 
ATOM   5747  O OG  . SER   D  2 1   ? 5.32651   28.55883  3.90183   1.000 24.64503  ?  404 SER   H OG  1 
ATOM   5748  N N   . PHE   D  2 2   ? 6.48112   29.92515  6.30126   1.000 16.73736  ?  405 PHE   H N   1 
ATOM   5749  C CA  . PHE   D  2 2   ? 6.29254   31.19064  7.00613   1.000 23.01214  ?  405 PHE   H CA  1 
ATOM   5750  C C   . PHE   D  2 2   ? 6.17832   32.33068  6.00010   1.000 20.68303  ?  405 PHE   H C   1 
ATOM   5751  O O   . PHE   D  2 2   ? 6.70078   32.24701  4.87947   1.000 29.98116  ?  405 PHE   H O   1 
ATOM   5752  C CB  . PHE   D  2 2   ? 7.43615   31.47477  7.99645   1.000 23.69295  ?  405 PHE   H CB  1 
ATOM   5753  C CG  . PHE   D  2 2   ? 8.56651   32.26629  7.40447   1.000 26.16534  ?  405 PHE   H CG  1 
ATOM   5754  C CD1 . PHE   D  2 2   ? 9.56011   31.63704  6.64645   1.000 32.45863  ?  405 PHE   H CD1 1 
ATOM   5755  C CD2 . PHE   D  2 2   ? 8.62893   33.64919  7.59171   1.000 29.60069  ?  405 PHE   H CD2 1 
ATOM   5756  C CE1 . PHE   D  2 2   ? 10.60571  32.36845  6.08338   1.000 26.18733  ?  405 PHE   H CE1 1 
ATOM   5757  C CE2 . PHE   D  2 2   ? 9.66927   34.39937  7.03187   1.000 22.32469  ?  405 PHE   H CE2 1 
ATOM   5758  C CZ  . PHE   D  2 2   ? 10.67314  33.74479  6.27644   1.000 28.51263  ?  405 PHE   H CZ  1 
ATOM   5759  N N   . ALA   D  2 3   ? 5.50873   33.41270  6.42234   1.000 23.21974  ?  406 ALA   H N   1 
ATOM   5760  C CA  . ALA   D  2 3   ? 5.37476   34.59964  5.59270   1.000 27.47164  ?  406 ALA   H CA  1 
ATOM   5761  C C   . ALA   D  2 3   ? 5.61491   35.85440  6.41615   1.000 30.61184  ?  406 ALA   H C   1 
ATOM   5762  O O   . ALA   D  2 3   ? 5.12430   35.97783  7.54720   1.000 29.52044  ?  406 ALA   H O   1 
ATOM   5763  C CB  . ALA   D  2 3   ? 4.00600   34.67521  4.92668   1.000 11.27165  ?  406 ALA   H CB  1 
ATOM   5764  N N   . LEU   D  2 4   ? 6.37508   36.78059  5.82374   1.000 29.62468  ?  407 LEU   H N   1 
ATOM   5765  C CA  . LEU   D  2 4   ? 6.63598   38.10345  6.37386   1.000 28.90238  ?  407 LEU   H CA  1 
ATOM   5766  C C   . LEU   D  2 4   ? 5.80223   39.11800  5.60362   1.000 14.12072  ?  407 LEU   H C   1 
ATOM   5767  O O   . LEU   D  2 4   ? 5.79956   39.10391  4.36824   1.000 33.67794  ?  407 LEU   H O   1 
ATOM   5768  C CB  . LEU   D  2 4   ? 8.12516   38.44725  6.27331   1.000 17.85051  ?  407 LEU   H CB  1 
ATOM   5769  C CG  . LEU   D  2 4   ? 8.48488   39.91361  6.52679   1.000 29.57922  ?  407 LEU   H CG  1 
ATOM   5770  C CD1 . LEU   D  2 4   ? 8.26337   40.27400  8.00663   1.000 15.97396  ?  407 LEU   H CD1 1 
ATOM   5771  C CD2 . LEU   D  2 4   ? 9.90917   40.18110  6.08775   1.000 21.92141  ?  407 LEU   H CD2 1 
ATOM   5772  N N   . GLY   D  2 5   ? 5.08643   39.98257  6.33194   1.000 36.42913  ?  408 GLY   H N   1 
ATOM   5773  C CA  . GLY   D  2 5   ? 4.23622   40.99887  5.72214   1.000 13.14151  ?  408 GLY   H CA  1 
ATOM   5774  C C   . GLY   D  2 5   ? 4.66156   42.42842  6.02492   1.000 28.66606  ?  408 GLY   H C   1 
ATOM   5775  O O   . GLY   D  2 5   ? 4.86412   42.80394  7.19114   1.000 34.99076  ?  408 GLY   H O   1 
ATOM   5776  N N   . LEU   D  2 6   ? 4.80444   43.23536  4.97152   1.000 13.85948  ?  409 LEU   H N   1 
ATOM   5777  C CA  . LEU   D  2 6   ? 5.18301   44.64067  5.07774   1.000 33.21498  ?  409 LEU   H CA  1 
ATOM   5778  C C   . LEU   D  2 6   ? 4.07739   45.52472  4.51682   1.000 26.61109  ?  409 LEU   H C   1 
ATOM   5779  O O   . LEU   D  2 6   ? 3.49855   45.21732  3.46521   1.000 31.67656  ?  409 LEU   H O   1 
ATOM   5780  C CB  . LEU   D  2 6   ? 6.48389   44.92036  4.31996   1.000 24.49673  ?  409 LEU   H CB  1 
ATOM   5781  C CG  . LEU   D  2 6   ? 7.64045   43.99037  4.69369   1.000 31.37184  ?  409 LEU   H CG  1 
ATOM   5782  C CD1 . LEU   D  2 6   ? 8.87464   44.30596  3.86401   1.000 17.45440  ?  409 LEU   H CD1 1 
ATOM   5783  C CD2 . LEU   D  2 6   ? 7.94253   44.04065  6.20709   1.000 13.00564  ?  409 LEU   H CD2 1 
ATOM   5784  N N   . ARG   D  2 7   ? 3.80449   46.62778  5.21410   1.000 27.80256  ?  410 ARG   H N   1 
ATOM   5785  C CA  . ARG   D  2 7   ? 2.86279   47.64484  4.75325   1.000 26.52983  ?  410 ARG   H CA  1 
ATOM   5786  C C   . ARG   D  2 7   ? 3.43324   48.42967  3.55898   1.000 32.42866  ?  410 ARG   H C   1 
ATOM   5787  O O   . ARG   D  2 7   ? 4.65245   48.50561  3.36085   1.000 43.69129  ?  410 ARG   H O   1 
ATOM   5788  C CB  . ARG   D  2 7   ? 2.52697   48.58909  5.91521   1.000 13.37942  ?  410 ARG   H CB  1 
ATOM   5789  C CG  . ARG   D  2 7   ? 1.92776   47.85797  7.10482   1.000 15.38762  ?  410 ARG   H CG  1 
ATOM   5790  C CD  . ARG   D  2 7   ? 1.71092   48.72553  8.32715   1.000 26.63304  ?  410 ARG   H CD  1 
ATOM   5791  N NE  . ARG   D  2 7   ? 2.96493   49.15216  8.93018   1.000 45.72650  ?  410 ARG   H NE  1 
ATOM   5792  C CZ  . ARG   D  2 7   ? 3.51817   50.34524  8.75053   1.000 36.58672  ?  410 ARG   H CZ  1 
ATOM   5793  N NH1 . ARG   D  2 7   ? 2.91340   51.29174  8.05184   1.000 39.95070  ?  410 ARG   H NH1 1 
ATOM   5794  N NH2 . ARG   D  2 7   ? 4.71520   50.59133  9.27490   1.000 45.81443  ?  410 ARG   H NH2 1 
ATOM   5795  N N   . LYS   D  2 8   ? 2.53331   49.01574  2.74574   1.000 45.14301  ?  411 LYS   H N   1 
ATOM   5796  C CA  . LYS   D  2 8   ? 2.98392   49.86355  1.63448   1.000 63.20368  ?  411 LYS   H CA  1 
ATOM   5797  C C   . LYS   D  2 8   ? 3.74954   51.07172  2.14817   1.000 55.42869  ?  411 LYS   H C   1 
ATOM   5798  O O   . LYS   D  2 8   ? 4.81571   51.41179  1.61921   1.000 52.34031  ?  411 LYS   H O   1 
ATOM   5799  C CB  . LYS   D  2 8   ? 1.80828   50.32924  0.77015   1.000 35.32369  ?  411 LYS   H CB  1 
ATOM   5800  C CG  . LYS   D  2 8   ? 2.25992   51.01767  -0.55985  1.000 74.65003  ?  411 LYS   H CG  1 
ATOM   5801  C CD  . LYS   D  2 8   ? 2.91733   50.02021  -1.51542  1.000 72.83052  ?  411 LYS   H CD  1 
ATOM   5802  C CE  . LYS   D  2 8   ? 2.50314   50.22576  -2.98211  1.000 100.70760 ?  411 LYS   H CE  1 
ATOM   5803  N NZ  . LYS   D  2 8   ? 3.00637   49.15783  -3.90842  1.000 94.24643  ?  411 LYS   H NZ  1 
ATOM   5804  N N   . ASP   D  2 9   ? 3.23054   51.71811  3.19894   1.000 38.07666  ?  412 ASP   H N   1 
ATOM   5805  C CA  . ASP   D  2 9   ? 3.88754   52.84961  3.84924   1.000 89.50513  ?  412 ASP   H CA  1 
ATOM   5806  C C   . ASP   D  2 9   ? 5.20431   52.48676  4.52972   1.000 44.82200  ?  412 ASP   H C   1 
ATOM   5807  O O   . ASP   D  2 9   ? 5.87052   53.37174  5.08371   1.000 75.39919  ?  412 ASP   H O   1 
ATOM   5808  C CB  . ASP   D  2 9   ? 2.93552   53.46723  4.87198   1.000 63.06066  ?  412 ASP   H CB  1 
ATOM   5809  C CG  . ASP   D  2 9   ? 1.80434   54.23441  4.21662   1.000 72.49394  ?  412 ASP   H CG  1 
ATOM   5810  O OD1 . ASP   D  2 9   ? 1.86276   54.45322  2.98122   1.000 75.08365  ?  412 ASP   H OD1 1 
ATOM   5811  O OD2 . ASP   D  2 9   ? 0.85980   54.61990  4.93494   1.000 97.74499  -1 412 ASP   H OD2 1 
ATOM   5812  N N   . CYS   D  2 10  ? 5.58045   51.21963  4.54168   1.000 68.29211  ?  413 CYS   H N   1 
ATOM   5813  C CA  . CYS   D  2 10  ? 6.84714   50.82441  5.12546   1.000 45.21479  ?  413 CYS   H CA  1 
ATOM   5814  C C   . CYS   D  2 10  ? 7.94449   51.07482  4.09876   1.000 55.76266  ?  413 CYS   H C   1 
ATOM   5815  O O   . CYS   D  2 10  ? 7.87197   50.58212  2.96303   1.000 53.76672  ?  413 CYS   H O   1 
ATOM   5816  C CB  . CYS   D  2 10  ? 6.78892   49.36160  5.55945   1.000 36.70224  ?  413 CYS   H CB  1 
ATOM   5817  S SG  . CYS   D  2 10  ? 8.37709   48.58688  5.93301   1.000 48.57816  ?  413 CYS   H SG  1 
ATOM   5818  N N   . ARG   D  2 11  ? 8.94391   51.86317  4.49576   1.000 46.64214  ?  414 ARG   H N   1 
ATOM   5819  C CA  . ARG   D  2 11  ? 10.06006  52.24432  3.64143   1.000 69.00738  ?  414 ARG   H CA  1 
ATOM   5820  C C   . ARG   D  2 11  ? 11.09305  51.10838  3.45553   1.000 80.33743  ?  414 ARG   H C   1 
ATOM   5821  O O   . ARG   D  2 11  ? 12.12760  51.31490  2.81027   1.000 52.88145  ?  414 ARG   H O   1 
ATOM   5822  C CB  . ARG   D  2 11  ? 10.71328  53.51104  4.21425   1.000 40.65754  ?  414 ARG   H CB  1 
ATOM   5823  N N   . ALA   D  2 12  ? 10.83561  49.91184  3.98282   1.000 56.85617  ?  415 ALA   H N   1 
ATOM   5824  C CA  . ALA   D  2 12  ? 11.71739  48.77116  3.77544   1.000 45.75650  ?  415 ALA   H CA  1 
ATOM   5825  C C   . ALA   D  2 12  ? 11.30694  48.01641  2.52028   1.000 39.63531  ?  415 ALA   H C   1 
ATOM   5826  O O   . ALA   D  2 12  ? 10.11914  47.94784  2.17696   1.000 67.28547  ?  415 ALA   H O   1 
ATOM   5827  C CB  . ALA   D  2 12  ? 11.68687  47.82818  4.97774   1.000 25.43484  ?  415 ALA   H CB  1 
ATOM   5828  N N   . GLU   D  2 13  ? 12.29607  47.44026  1.84536   1.000 25.23916  ?  416 GLU   H N   1 
ATOM   5829  C CA  . GLU   D  2 13  ? 12.08721  46.77098  0.56993   1.000 38.92261  ?  416 GLU   H CA  1 
ATOM   5830  C C   . GLU   D  2 13  ? 12.70994  45.38058  0.63248   1.000 41.22269  ?  416 GLU   H C   1 
ATOM   5831  O O   . GLU   D  2 13  ? 13.86944  45.22526  1.03220   1.000 46.39074  ?  416 GLU   H O   1 
ATOM   5832  C CB  . GLU   D  2 13  ? 12.67155  47.58826  -0.59767  1.000 28.20099  ?  416 GLU   H CB  1 
ATOM   5833  N N   . ILE   D  2 14  ? 11.92054  44.37237  0.25859   1.000 38.87702  ?  417 ILE   H N   1 
ATOM   5834  C CA  . ILE   D  2 14  ? 12.41235  43.00604  0.19953   1.000 46.60287  ?  417 ILE   H CA  1 
ATOM   5835  C C   . ILE   D  2 14  ? 13.64880  42.93162  -0.69515  1.000 36.74473  ?  417 ILE   H C   1 
ATOM   5836  O O   . ILE   D  2 14  ? 13.71875  43.54481  -1.76423  1.000 45.08326  ?  417 ILE   H O   1 
ATOM   5837  C CB  . ILE   D  2 14  ? 11.28603  42.07699  -0.29127  1.000 26.96525  ?  417 ILE   H CB  1 
ATOM   5838  C CG1 . ILE   D  2 14  ? 10.11226  42.11418  0.68692   1.000 30.33591  ?  417 ILE   H CG1 1 
ATOM   5839  C CG2 . ILE   D  2 14  ? 11.79078  40.63442  -0.49662  1.000 33.98234  ?  417 ILE   H CG2 1 
ATOM   5840  C CD1 . ILE   D  2 14  ? 8.90201   41.31223  0.21999   1.000 40.40263  ?  417 ILE   H CD1 1 
ATOM   5841  N N   . VAL   D  2 15  ? 14.63549  42.17072  -0.24356  1.000 44.42542  ?  418 VAL   H N   1 
ATOM   5842  C CA  . VAL   D  2 15  ? 15.87850  42.02383  -0.98014  1.000 26.12503  ?  418 VAL   H CA  1 
ATOM   5843  C C   . VAL   D  2 15  ? 15.62822  41.20851  -2.24346  1.000 29.92020  ?  418 VAL   H C   1 
ATOM   5844  O O   . VAL   D  2 15  ? 15.11028  40.08440  -2.17979  1.000 50.02380  ?  418 VAL   H O   1 
ATOM   5845  C CB  . VAL   D  2 15  ? 16.93554  41.38368  -0.06656  1.000 49.48873  ?  418 VAL   H CB  1 
ATOM   5846  C CG1 . VAL   D  2 15  ? 18.19960  41.00982  -0.83824  1.000 17.80157  ?  418 VAL   H CG1 1 
ATOM   5847  C CG2 . VAL   D  2 15  ? 17.23309  42.32907  1.10373   1.000 16.06974  ?  418 VAL   H CG2 1 
ATOM   5848  N N   . GLU   D  2 16  ? 16.03514  41.76357  -3.39793  1.000 45.74340  ?  419 GLU   H N   1 
ATOM   5849  C CA  . GLU   D  2 16  ? 15.58276  41.25790  -4.69722  1.000 35.21465  ?  419 GLU   H CA  1 
ATOM   5850  C C   . GLU   D  2 16  ? 15.94776  39.79750  -4.93072  1.000 45.65558  ?  419 GLU   H C   1 
ATOM   5851  O O   . GLU   D  2 16  ? 15.19551  39.09429  -5.61618  1.000 45.77545  ?  419 GLU   H O   1 
ATOM   5852  C CB  . GLU   D  2 16  ? 16.13704  42.10188  -5.85949  1.000 35.90764  ?  419 GLU   H CB  1 
ATOM   5853  N N   . LYS   D  2 17  ? 17.08331  39.31278  -4.40272  1.000 38.58393  ?  420 LYS   H N   1 
ATOM   5854  C CA  . LYS   D  2 17  ? 17.45661  37.93727  -4.74746  1.000 40.84051  ?  420 LYS   H CA  1 
ATOM   5855  C C   . LYS   D  2 17  ? 16.42173  36.93023  -4.26087  1.000 47.35930  ?  420 LYS   H C   1 
ATOM   5856  O O   . LYS   D  2 17  ? 16.32512  35.82611  -4.81647  1.000 45.76032  ?  420 LYS   H O   1 
ATOM   5857  C CB  . LYS   D  2 17  ? 18.85724  37.55903  -4.21408  1.000 23.31437  ?  420 LYS   H CB  1 
ATOM   5858  C CG  . LYS   D  2 17  ? 19.06539  37.42388  -2.68061  1.000 28.31449  ?  420 LYS   H CG  1 
ATOM   5859  C CD  . LYS   D  2 17  ? 20.02942  36.24834  -2.41226  1.000 49.45114  ?  420 LYS   H CD  1 
ATOM   5860  C CE  . LYS   D  2 17  ? 20.80508  36.35948  -1.10424  1.000 59.24742  ?  420 LYS   H CE  1 
ATOM   5861  N NZ  . LYS   D  2 17  ? 21.57921  37.62725  -1.06454  1.000 82.14252  ?  420 LYS   H NZ  1 
ATOM   5862  N N   . PHE   D  2 18  ? 15.62838  37.29399  -3.24966  1.000 33.46882  ?  421 PHE   H N   1 
ATOM   5863  C CA  . PHE   D  2 18  ? 14.62162  36.38649  -2.71921  1.000 57.14672  ?  421 PHE   H CA  1 
ATOM   5864  C C   . PHE   D  2 18  ? 13.34163  36.36480  -3.54053  1.000 44.35406  ?  421 PHE   H C   1 
ATOM   5865  O O   . PHE   D  2 18  ? 12.48778  35.50787  -3.29780  1.000 39.06773  ?  421 PHE   H O   1 
ATOM   5866  C CB  . PHE   D  2 18  ? 14.31864  36.74755  -1.27346  1.000 22.29486  ?  421 PHE   H CB  1 
ATOM   5867  C CG  . PHE   D  2 18  ? 15.52090  36.66297  -0.39430  1.000 33.52491  ?  421 PHE   H CG  1 
ATOM   5868  C CD1 . PHE   D  2 18  ? 16.22876  35.46569  -0.29446  1.000 32.96420  ?  421 PHE   H CD1 1 
ATOM   5869  C CD2 . PHE   D  2 18  ? 15.97658  37.77217  0.30698   1.000 50.35024  ?  421 PHE   H CD2 1 
ATOM   5870  C CE1 . PHE   D  2 18  ? 17.35270  35.37608  0.50028   1.000 25.27878  ?  421 PHE   H CE1 1 
ATOM   5871  C CE2 . PHE   D  2 18  ? 17.10843  37.69085  1.10765   1.000 40.73599  ?  421 PHE   H CE2 1 
ATOM   5872  C CZ  . PHE   D  2 18  ? 17.79778  36.49420  1.19866   1.000 46.40791  ?  421 PHE   H CZ  1 
ATOM   5873  N N   . THR   D  2 19  ? 13.18845  37.24736  -4.52762  1.000 41.54938  ?  422 THR   H N   1 
ATOM   5874  C CA  . THR   D  2 19  ? 12.05290  37.07080  -5.42034  1.000 31.77122  ?  422 THR   H CA  1 
ATOM   5875  C C   . THR   D  2 19  ? 12.23383  35.88889  -6.37208  1.000 39.81897  ?  422 THR   H C   1 
ATOM   5876  O O   . THR   D  2 19  ? 11.26833  35.52014  -7.05038  1.000 37.95439  ?  422 THR   H O   1 
ATOM   5877  C CB  . THR   D  2 19  ? 11.79929  38.34911  -6.21650  1.000 43.39582  ?  422 THR   H CB  1 
ATOM   5878  O OG1 . THR   D  2 19  ? 12.79096  38.47709  -7.23303  1.000 39.59941  ?  422 THR   H OG1 1 
ATOM   5879  C CG2 . THR   D  2 19  ? 11.87236  39.57139  -5.31447  1.000 45.31725  ?  422 THR   H CG2 1 
ATOM   5880  N N   . GLU   D  2 20  ? 13.42930  35.27367  -6.43303  1.000 44.29752  ?  423 GLU   H N   1 
ATOM   5881  C CA  . GLU   D  2 20  ? 13.60503  34.05773  -7.22657  1.000 42.58748  ?  423 GLU   H CA  1 
ATOM   5882  C C   . GLU   D  2 20  ? 13.30382  32.84148  -6.35598  1.000 33.03715  ?  423 GLU   H C   1 
ATOM   5883  O O   . GLU   D  2 20  ? 14.01857  32.59982  -5.36881  1.000 48.80978  ?  423 GLU   H O   1 
ATOM   5884  C CB  . GLU   D  2 20  ? 15.01397  33.96016  -7.80828  1.000 28.86158  ?  423 GLU   H CB  1 
ATOM   5885  N N   . PRO   D  2 21  ? 12.24865  32.09261  -6.64909  1.000 28.79704  ?  424 PRO   H N   1 
ATOM   5886  C CA  . PRO   D  2 21  ? 11.96177  30.87694  -5.87980  1.000 42.23704  ?  424 PRO   H CA  1 
ATOM   5887  C C   . PRO   D  2 21  ? 13.18220  29.97386  -5.82940  1.000 27.85162  ?  424 PRO   H C   1 
ATOM   5888  O O   . PRO   D  2 21  ? 13.95464  29.89439  -6.78460  1.000 36.54911  ?  424 PRO   H O   1 
ATOM   5889  C CB  . PRO   D  2 21  ? 10.82159  30.21759  -6.66538  1.000 10.74317  ?  424 PRO   H CB  1 
ATOM   5890  C CG  . PRO   D  2 21  ? 10.16702  31.33882  -7.40349  1.000 25.86181  ?  424 PRO   H CG  1 
ATOM   5891  C CD  . PRO   D  2 21  ? 11.23039  32.38822  -7.66435  1.000 24.55277  ?  424 PRO   H CD  1 
ATOM   5892  N N   . GLY   D  2 22  ? 13.35025  29.29017  -4.69713  1.000 33.45660  ?  425 GLY   H N   1 
ATOM   5893  C CA  . GLY   D  2 22  ? 14.43423  28.35292  -4.51372  1.000 16.13374  ?  425 GLY   H CA  1 
ATOM   5894  C C   . GLY   D  2 22  ? 15.68903  28.93301  -3.88656  1.000 24.77339  ?  425 GLY   H C   1 
ATOM   5895  O O   . GLY   D  2 22  ? 16.57029  28.16572  -3.48956  1.000 30.65185  ?  425 GLY   H O   1 
ATOM   5896  N N   . THR   D  2 23  ? 15.79712  30.25539  -3.78238  1.000 31.01385  ?  426 THR   H N   1 
ATOM   5897  C CA  . THR   D  2 23  ? 16.96090  30.87467  -3.15825  1.000 28.68293  ?  426 THR   H CA  1 
ATOM   5898  C C   . THR   D  2 23  ? 17.06096  30.49908  -1.67734  1.000 28.65608  ?  426 THR   H C   1 
ATOM   5899  O O   . THR   D  2 23  ? 16.06617  30.49086  -0.94821  1.000 57.92680  ?  426 THR   H O   1 
ATOM   5900  C CB  . THR   D  2 23  ? 16.87502  32.39829  -3.32150  1.000 37.35481  ?  426 THR   H CB  1 
ATOM   5901  O OG1 . THR   D  2 23  ? 16.83295  32.73586  -4.71554  1.000 45.65379  ?  426 THR   H OG1 1 
ATOM   5902  C CG2 . THR   D  2 23  ? 18.04489  33.11345  -2.64368  1.000 27.79436  ?  426 THR   H CG2 1 
ATOM   5903  N N   . VAL   D  2 24  ? 18.27743  30.19649  -1.23050  1.000 49.93933  ?  427 VAL   H N   1 
ATOM   5904  C CA  . VAL   D  2 24  ? 18.48992  29.81208  0.15794   1.000 31.10378  ?  427 VAL   H CA  1 
ATOM   5905  C C   . VAL   D  2 24  ? 18.31347  31.02144  1.06954   1.000 25.55924  ?  427 VAL   H C   1 
ATOM   5906  O O   . VAL   D  2 24  ? 18.87251  32.10066  0.82399   1.000 50.41384  ?  427 VAL   H O   1 
ATOM   5907  C CB  . VAL   D  2 24  ? 19.87648  29.17258  0.31867   1.000 23.97206  ?  427 VAL   H CB  1 
ATOM   5908  C CG1 . VAL   D  2 24  ? 20.26584  29.08671  1.78162   1.000 16.71148  ?  427 VAL   H CG1 1 
ATOM   5909  C CG2 . VAL   D  2 24  ? 19.85890  27.79431  -0.30188  1.000 23.91854  ?  427 VAL   H CG2 1 
ATOM   5910  N N   . ILE   D  2 25  ? 17.52799  30.84263  2.13009   1.000 48.45840  ?  428 ILE   H N   1 
ATOM   5911  C CA  . ILE   D  2 25  ? 17.28049  31.87209  3.13828   1.000 17.35510  ?  428 ILE   H CA  1 
ATOM   5912  C C   . ILE   D  2 25  ? 17.93105  31.39027  4.43213   1.000 38.76710  ?  428 ILE   H C   1 
ATOM   5913  O O   . ILE   D  2 25  ? 17.42697  30.47710  5.10037   1.000 30.06760  ?  428 ILE   H O   1 
ATOM   5914  C CB  . ILE   D  2 25  ? 15.78056  32.15355  3.33877   1.000 35.76148  ?  428 ILE   H CB  1 
ATOM   5915  C CG1 . ILE   D  2 25  ? 15.12602  32.70221  2.06106   1.000 26.63012  ?  428 ILE   H CG1 1 
ATOM   5916  C CG2 . ILE   D  2 25  ? 15.59041  33.12318  4.48394   1.000 14.59399  ?  428 ILE   H CG2 1 
ATOM   5917  C CD1 . ILE   D  2 25  ? 13.67650  33.16951  2.24338   1.000 21.25898  ?  428 ILE   H CD1 1 
ATOM   5918  N N   . ARG   D  2 26  ? 19.06402  31.98731  4.78411   1.000 27.82096  ?  429 ARG   H N   1 
ATOM   5919  C CA  . ARG   D  2 26  ? 19.72878  31.66892  6.03989   1.000 26.63332  ?  429 ARG   H CA  1 
ATOM   5920  C C   . ARG   D  2 26  ? 19.05071  32.45407  7.14569   1.000 27.16351  ?  429 ARG   H C   1 
ATOM   5921  O O   . ARG   D  2 26  ? 18.96469  33.68528  7.06919   1.000 26.20315  ?  429 ARG   H O   1 
ATOM   5922  C CB  . ARG   D  2 26  ? 21.21806  32.00214  5.96898   1.000 34.64818  ?  429 ARG   H CB  1 
ATOM   5923  C CG  . ARG   D  2 26  ? 21.94766  31.16052  4.95926   1.000 28.42623  ?  429 ARG   H CG  1 
ATOM   5924  C CD  . ARG   D  2 26  ? 23.37373  31.60489  4.75997   1.000 42.04873  ?  429 ARG   H CD  1 
ATOM   5925  N NE  . ARG   D  2 26  ? 24.21482  30.44416  4.49247   1.000 27.83130  ?  429 ARG   H NE  1 
ATOM   5926  C CZ  . ARG   D  2 26  ? 24.28291  29.83043  3.31698   1.000 160.33513 ?  429 ARG   H CZ  1 
ATOM   5927  N NH1 . ARG   D  2 26  ? 23.63292  30.28860  2.25186   1.000 23.46899  ?  429 ARG   H NH1 1 
ATOM   5928  N NH2 . ARG   D  2 26  ? 25.01462  28.72533  3.20565   1.000 30.29561  ?  429 ARG   H NH2 1 
ATOM   5929  N N   . ILE   D  2 27  ? 18.56528  31.74798  8.16907   1.000 15.96599  ?  430 ILE   H N   1 
ATOM   5930  C CA  . ILE   D  2 27  ? 17.87371  32.42985  9.25234   1.000 33.35948  ?  430 ILE   H CA  1 
ATOM   5931  C C   . ILE   D  2 27  ? 18.77426  33.53117  9.82086   1.000 20.99088  ?  430 ILE   H C   1 
ATOM   5932  O O   . ILE   D  2 27  ? 20.00467  33.41004  9.84277   1.000 47.79285  ?  430 ILE   H O   1 
ATOM   5933  C CB  . ILE   D  2 27  ? 17.42805  31.41099  10.31881  1.000 26.86353  ?  430 ILE   H CB  1 
ATOM   5934  C CG1 . ILE   D  2 27  ? 16.35971  32.03120  11.23994  1.000 21.34789  ?  430 ILE   H CG1 1 
ATOM   5935  C CG2 . ILE   D  2 27  ? 18.64960  30.83401  11.07460  1.000 24.97808  ?  430 ILE   H CG2 1 
ATOM   5936  C CD1 . ILE   D  2 27  ? 15.72805  31.01559  12.18898  1.000 18.53137  ?  430 ILE   H CD1 1 
ATOM   5937  N N   . ASN   D  2 28  ? 18.14217  34.63073  10.23909  1.000 44.91486  ?  431 ASN   H N   1 
ATOM   5938  C CA  . ASN   D  2 28  ? 18.77731  35.85016  10.73659  1.000 24.36693  ?  431 ASN   H CA  1 
ATOM   5939  C C   . ASN   D  2 28  ? 19.43939  36.67396  9.63698   1.000 35.93498  ?  431 ASN   H C   1 
ATOM   5940  O O   . ASN   D  2 28  ? 19.88651  37.78900  9.91880   1.000 26.47996  ?  431 ASN   H O   1 
ATOM   5941  C CB  . ASN   D  2 28  ? 19.83117  35.56350  11.82080  1.000 20.03668  ?  431 ASN   H CB  1 
ATOM   5942  C CG  . ASN   D  2 28  ? 19.24697  34.90140  13.05346  1.000 31.94579  ?  431 ASN   H CG  1 
ATOM   5943  O OD1 . ASN   D  2 28  ? 18.05303  35.01021  13.33565  1.000 36.89645  ?  431 ASN   H OD1 1 
ATOM   5944  N ND2 . ASN   D  2 28  ? 20.09519  34.19915  13.79509  1.000 24.09365  ?  431 ASN   H ND2 1 
ATOM   5945  N N   . GLU   D  2 29  ? 19.54572  36.16928  8.40541   1.000 23.65837  ?  432 GLU   H N   1 
ATOM   5946  C CA  . GLU   D  2 29  ? 20.13532  37.01994  7.37633   1.000 32.30393  ?  432 GLU   H CA  1 
ATOM   5947  C C   . GLU   D  2 29  ? 19.10922  38.07087  6.91656   1.000 28.08126  ?  432 GLU   H C   1 
ATOM   5948  O O   . GLU   D  2 29  ? 17.91768  37.99658  7.23599   1.000 43.54383  ?  432 GLU   H O   1 
ATOM   5949  C CB  . GLU   D  2 29  ? 20.67279  36.16630  6.21828   1.000 16.48038  ?  432 GLU   H CB  1 
ATOM   5950  C CG  . GLU   D  2 29  ? 19.76366  35.99872  5.01357   1.000 29.76172  ?  432 GLU   H CG  1 
ATOM   5951  C CD  . GLU   D  2 29  ? 20.46480  35.34495  3.81280   1.000 54.14045  ?  432 GLU   H CD  1 
ATOM   5952  O OE1 . GLU   D  2 29  ? 20.45562  34.09731  3.71098   1.000 39.15457  ?  432 GLU   H OE1 1 
ATOM   5953  O OE2 . GLU   D  2 29  ? 21.01203  36.08232  2.95419   1.000 45.40735  -1 432 GLU   H OE2 1 
ATOM   5954  N N   . VAL   D  2 30  ? 19.58848  39.09272  6.21190   1.000 43.00439  ?  433 VAL   H N   1 
ATOM   5955  C CA  . VAL   D  2 30  ? 18.74732  40.23749  5.85334   1.000 18.32136  ?  433 VAL   H CA  1 
ATOM   5956  C C   . VAL   D  2 30  ? 17.84036  39.86040  4.68616   1.000 38.42356  ?  433 VAL   H C   1 
ATOM   5957  O O   . VAL   D  2 30  ? 18.32810  39.50477  3.60620   1.000 29.26006  ?  433 VAL   H O   1 
ATOM   5958  C CB  . VAL   D  2 30  ? 19.61032  41.45990  5.49580   1.000 39.27323  ?  433 VAL   H CB  1 
ATOM   5959  C CG1 . VAL   D  2 30  ? 18.74159  42.66067  5.10060   1.000 29.10082  ?  433 VAL   H CG1 1 
ATOM   5960  C CG2 . VAL   D  2 30  ? 20.56347  41.82243  6.64261   1.000 23.87647  ?  433 VAL   H CG2 1 
ATOM   5961  N N   . VAL   D  2 31  ? 16.51941  39.95600  4.88926   1.000 33.06190  ?  434 VAL   H N   1 
ATOM   5962  C CA  . VAL   D  2 31  ? 15.56742  39.74629  3.79936   1.000 44.14337  ?  434 VAL   H CA  1 
ATOM   5963  C C   . VAL   D  2 31  ? 14.86660  41.03438  3.37196   1.000 31.74015  ?  434 VAL   H C   1 
ATOM   5964  O O   . VAL   D  2 31  ? 14.30369  41.07593  2.26473   1.000 30.92181  ?  434 VAL   H O   1 
ATOM   5965  C CB  . VAL   D  2 31  ? 14.52198  38.65073  4.12576   1.000 34.46347  ?  434 VAL   H CB  1 
ATOM   5966  C CG1 . VAL   D  2 31  ? 15.18112  37.28302  4.24517   1.000 18.22786  ?  434 VAL   H CG1 1 
ATOM   5967  C CG2 . VAL   D  2 31  ? 13.72025  38.98108  5.40935   1.000 20.80679  ?  434 VAL   H CG2 1 
ATOM   5968  N N   . ALA   D  2 32  ? 14.88935  42.08154  4.18933   1.000 26.20786  ?  435 ALA   H N   1 
ATOM   5969  C CA  . ALA   D  2 32  ? 14.38176  43.38149  3.77008   1.000 29.48549  ?  435 ALA   H CA  1 
ATOM   5970  C C   . ALA   D  2 32  ? 15.15726  44.45964  4.51482   1.000 39.42788  ?  435 ALA   H C   1 
ATOM   5971  O O   . ALA   D  2 32  ? 15.60761  44.24862  5.64897   1.000 31.49775  ?  435 ALA   H O   1 
ATOM   5972  C CB  . ALA   D  2 32  ? 12.87609  43.53263  4.02978   1.000 23.18313  ?  435 ALA   H CB  1 
ATOM   5973  N N   . ALA   D  2 33  ? 15.30004  45.61933  3.87046   1.000 34.61844  ?  436 ALA   H N   1 
ATOM   5974  C CA  . ALA   D  2 33  ? 16.08581  46.72104  4.41215   1.000 43.61684  ?  436 ALA   H CA  1 
ATOM   5975  C C   . ALA   D  2 33  ? 15.50682  48.04536  3.94019   1.000 63.23903  ?  436 ALA   H C   1 
ATOM   5976  O O   . ALA   D  2 33  ? 14.90528  48.12707  2.86457   1.000 40.63527  ?  436 ALA   H O   1 
ATOM   5977  C CB  . ALA   D  2 33  ? 17.55046  46.63576  3.98744   1.000 27.71958  ?  436 ALA   H CB  1 
ATOM   5978  N N   . LEU   D  2 34  ? 15.71645  49.08338  4.74823   1.000 30.87994  ?  437 LEU   H N   1 
ATOM   5979  C CA  . LEU   D  2 34  ? 15.26198  50.43926  4.43717   1.000 60.60438  ?  437 LEU   H CA  1 
ATOM   5980  C C   . LEU   D  2 34  ? 15.95624  51.04802  3.21388   1.000 28.47457  ?  437 LEU   H C   1 
ATOM   5981  O O   . LEU   D  2 34  ? 17.17935  51.05731  3.12036   1.000 35.21232  ?  437 LEU   H O   1 
ATOM   5982  C CB  . LEU   D  2 34  ? 15.47258  51.34990  5.65325   1.000 27.29612  ?  437 LEU   H CB  1 
ATOM   5983  C CG  . LEU   D  2 34  ? 14.49088  51.18799  6.82399   1.000 52.41911  ?  437 LEU   H CG  1 
ATOM   5984  C CD1 . LEU   D  2 34  ? 14.86184  52.08263  8.03677   1.000 33.57384  ?  437 LEU   H CD1 1 
ATOM   5985  C CD2 . LEU   D  2 34  ? 13.04112  51.41685  6.35938   1.000 55.17340  ?  437 LEU   H CD2 1 
ATOM   5986  N N   . ASN   E  1 53  ? 36.56892  32.14135  43.87123  1.000 16.91949  ?  53  ASN   A N   1 
ATOM   5987  C CA  . ASN   E  1 53  ? 35.16380  31.91971  43.54076  1.000 99.25791  ?  53  ASN   A CA  1 
ATOM   5988  C C   . ASN   E  1 53  ? 34.43952  31.15732  44.63338  1.000 129.89991 ?  53  ASN   A C   1 
ATOM   5989  O O   . ASN   E  1 53  ? 33.57105  31.74437  45.27066  1.000 132.75568 ?  53  ASN   A O   1 
ATOM   5990  C CB  . ASN   E  1 53  ? 34.95779  31.17730  42.23127  1.000 81.52551  ?  53  ASN   A CB  1 
ATOM   5991  C CG  . ASN   E  1 53  ? 33.46730  31.10738  41.84672  1.000 90.17517  ?  53  ASN   A CG  1 
ATOM   5992  O OD1 . ASN   E  1 53  ? 32.88691  32.06099  41.30355  1.000 91.19770  ?  53  ASN   A OD1 1 
ATOM   5993  N ND2 . ASN   E  1 53  ? 32.84038  29.98689  42.16335  1.000 122.21362 ?  53  ASN   A ND2 1 
ATOM   5994  N N   . GLU   E  1 54  ? 34.73056  29.86495  44.85328  1.000 75.85756  ?  54  GLU   A N   1 
ATOM   5995  C CA  . GLU   E  1 54  ? 34.16969  29.24819  46.05834  1.000 111.10041 ?  54  GLU   A CA  1 
ATOM   5996  C C   . GLU   E  1 54  ? 34.94807  29.68246  47.29240  1.000 53.47634  ?  54  GLU   A C   1 
ATOM   5997  O O   . GLU   E  1 54  ? 34.36559  30.10696  48.30652  1.000 38.29598  ?  54  GLU   A O   1 
ATOM   5998  C CB  . GLU   E  1 54  ? 34.16212  27.71772  45.97031  1.000 90.88952  ?  54  GLU   A CB  1 
ATOM   5999  C CG  . GLU   E  1 54  ? 34.17246  27.04483  47.37711  1.000 71.59490  ?  54  GLU   A CG  1 
ATOM   6000  C CD  . GLU   E  1 54  ? 33.53080  25.66528  47.42208  1.000 131.95773 ?  54  GLU   A CD  1 
ATOM   6001  O OE1 . GLU   E  1 54  ? 33.30983  25.12857  48.52880  1.000 153.62486 ?  54  GLU   A OE1 1 
ATOM   6002  O OE2 . GLU   E  1 54  ? 33.22909  25.10859  46.35256  1.000 130.22266 ?  54  GLU   A OE2 1 
ATOM   6003  N N   . PHE   E  1 55  ? 36.27097  29.58851  47.21259  1.000 99.25346  ?  55  PHE   A N   1 
ATOM   6004  C CA  . PHE   E  1 55  ? 37.11722  29.74066  48.37590  1.000 58.15465  ?  55  PHE   A CA  1 
ATOM   6005  C C   . PHE   E  1 55  ? 38.02317  30.92861  48.15773  1.000 72.42785  ?  55  PHE   A C   1 
ATOM   6006  O O   . PHE   E  1 55  ? 38.73721  31.00108  47.15063  1.000 138.81680 ?  55  PHE   A O   1 
ATOM   6007  C CB  . PHE   E  1 55  ? 37.89472  28.45750  48.66618  1.000 33.57025  ?  55  PHE   A CB  1 
ATOM   6008  C CG  . PHE   E  1 55  ? 37.06176  27.42396  49.37188  1.000 59.72537  ?  55  PHE   A CG  1 
ATOM   6009  C CD1 . PHE   E  1 55  ? 36.15013  27.79988  50.34905  1.000 85.16044  ?  55  PHE   A CD1 1 
ATOM   6010  C CD2 . PHE   E  1 55  ? 37.13321  26.09921  49.01853  1.000 30.59495  ?  55  PHE   A CD2 1 
ATOM   6011  C CE1 . PHE   E  1 55  ? 35.36346  26.86843  50.99669  1.000 76.17691  ?  55  PHE   A CE1 1 
ATOM   6012  C CE2 . PHE   E  1 55  ? 36.34377  25.16306  49.66026  1.000 17.57228  ?  55  PHE   A CE2 1 
ATOM   6013  C CZ  . PHE   E  1 55  ? 35.45762  25.55271  50.66448  1.000 78.73782  ?  55  PHE   A CZ  1 
ATOM   6014  N N   . GLY   E  1 56  ? 37.94419  31.87331  49.09471  1.000 41.52310  ?  56  GLY   A N   1 
ATOM   6015  C CA  . GLY   E  1 56  ? 38.70885  33.09079  49.07536  1.000 21.52372  ?  56  GLY   A CA  1 
ATOM   6016  C C   . GLY   E  1 56  ? 38.12822  34.13990  48.14664  1.000 101.55705 ?  56  GLY   A C   1 
ATOM   6017  O O   . GLY   E  1 56  ? 36.94453  34.17572  47.77778  1.000 104.78662 ?  56  GLY   A O   1 
ATOM   6018  N N   . LEU   E  1 57  ? 39.04029  34.98316  47.73852  1.000 33.12320  ?  57  LEU   A N   1 
ATOM   6019  C CA  . LEU   E  1 57  ? 38.77643  36.19861  46.97568  1.000 30.02053  ?  57  LEU   A CA  1 
ATOM   6020  C C   . LEU   E  1 57  ? 38.86027  35.91356  45.49276  1.000 46.16264  ?  57  LEU   A C   1 
ATOM   6021  O O   . LEU   E  1 57  ? 39.77703  35.22269  45.05172  1.000 48.15650  ?  57  LEU   A O   1 
ATOM   6022  C CB  . LEU   E  1 57  ? 39.79125  37.29762  47.29904  1.000 26.66575  ?  57  LEU   A CB  1 
ATOM   6023  C CG  . LEU   E  1 57  ? 39.90025  37.95886  48.67150  1.000 42.92944  ?  57  LEU   A CG  1 
ATOM   6024  C CD1 . LEU   E  1 57  ? 41.09287  38.91442  48.66670  1.000 35.31549  ?  57  LEU   A CD1 1 
ATOM   6025  C CD2 . LEU   E  1 57  ? 38.62027  38.68156  49.07725  1.000 41.39429  ?  57  LEU   A CD2 1 
ATOM   6026  N N   . MET   E  1 58  ? 37.94361  36.48522  44.71411  1.000 38.30266  ?  58  MET   A N   1 
ATOM   6027  C CA  . MET   E  1 58  ? 38.00424  36.29951  43.27028  1.000 37.20137  ?  58  MET   A CA  1 
ATOM   6028  C C   . MET   E  1 58  ? 39.25166  36.96250  42.69993  1.000 27.90974  ?  58  MET   A C   1 
ATOM   6029  O O   . MET   E  1 58  ? 39.71735  37.98944  43.19816  1.000 48.57534  ?  58  MET   A O   1 
ATOM   6030  C CB  . MET   E  1 58  ? 36.75379  36.86038  42.60422  1.000 30.14386  ?  58  MET   A CB  1 
ATOM   6031  C CG  . MET   E  1 58  ? 36.40550  38.28595  42.97812  1.000 45.44559  ?  58  MET   A CG  1 
ATOM   6032  S SD  . MET   E  1 58  ? 34.92830  38.82758  42.09324  1.000 51.31063  ?  58  MET   A SD  1 
ATOM   6033  C CE  . MET   E  1 58  ? 33.64342  38.04487  43.08180  1.000 27.93741  ?  58  MET   A CE  1 
ATOM   6034  N N   . GLN   E  1 59  ? 39.79556  36.36185  41.64275  1.000 44.23264  ?  59  GLN   A N   1 
ATOM   6035  C CA  . GLN   E  1 59  ? 41.08546  36.78891  41.09896  1.000 33.07089  ?  59  GLN   A CA  1 
ATOM   6036  C C   . GLN   E  1 59  ? 41.19562  38.29127  40.84954  1.000 42.80042  ?  59  GLN   A C   1 
ATOM   6037  O O   . GLN   E  1 59  ? 42.23189  38.87029  41.21169  1.000 36.85093  ?  59  GLN   A O   1 
ATOM   6038  C CB  . GLN   E  1 59  ? 41.38724  36.03212  39.79711  1.000 26.82082  ?  59  GLN   A CB  1 
ATOM   6039  C CG  . GLN   E  1 59  ? 42.83854  36.12779  39.39816  1.000 56.37269  ?  59  GLN   A CG  1 
ATOM   6040  C CD  . GLN   E  1 59  ? 43.72933  35.51008  40.46238  1.000 78.96461  ?  59  GLN   A CD  1 
ATOM   6041  O OE1 . GLN   E  1 59  ? 43.33805  34.54663  41.12838  1.000 90.54825  ?  59  GLN   A OE1 1 
ATOM   6042  N NE2 . GLN   E  1 59  ? 44.92333  36.07220  40.64792  1.000 63.59128  ?  59  GLN   A NE2 1 
ATOM   6043  N N   . PRO   E  1 60  ? 40.20875  38.97701  40.24858  1.000 53.20162  ?  60  PRO   A N   1 
ATOM   6044  C CA  . PRO   E  1 60  ? 40.36732  40.43372  40.05742  1.000 34.92142  ?  60  PRO   A CA  1 
ATOM   6045  C C   . PRO   E  1 60  ? 40.61452  41.18512  41.35596  1.000 59.00954  ?  60  PRO   A C   1 
ATOM   6046  O O   . PRO   E  1 60  ? 41.41500  42.13328  41.36454  1.000 38.11293  ?  60  PRO   A O   1 
ATOM   6047  C CB  . PRO   E  1 60  ? 39.04746  40.84402  39.38877  1.000 35.68501  ?  60  PRO   A CB  1 
ATOM   6048  C CG  . PRO   E  1 60  ? 38.54118  39.59662  38.73793  1.000 42.67357  ?  60  PRO   A CG  1 
ATOM   6049  C CD  . PRO   E  1 60  ? 38.93869  38.49067  39.67927  1.000 30.95286  ?  60  PRO   A CD  1 
ATOM   6050  N N   . ILE   E  1 61  ? 39.96476  40.77814  42.45558  1.000 24.47051  ?  61  ILE   A N   1 
ATOM   6051  C CA  . ILE   E  1 61  ? 40.24132  41.39637  43.75330  1.000 48.80411  ?  61  ILE   A CA  1 
ATOM   6052  C C   . ILE   E  1 61  ? 41.63379  41.03146  44.24804  1.000 35.12330  ?  61  ILE   A C   1 
ATOM   6053  O O   . ILE   E  1 61  ? 42.30545  41.84715  44.89138  1.000 39.45728  ?  61  ILE   A O   1 
ATOM   6054  C CB  . ILE   E  1 61  ? 39.16552  41.01237  44.78418  1.000 34.69473  ?  61  ILE   A CB  1 
ATOM   6055  C CG1 . ILE   E  1 61  ? 37.79328  41.46217  44.28716  1.000 25.24659  ?  61  ILE   A CG1 1 
ATOM   6056  C CG2 . ILE   E  1 61  ? 39.45859  41.64745  46.15521  1.000 23.38382  ?  61  ILE   A CG2 1 
ATOM   6057  C CD1 . ILE   E  1 61  ? 36.69794  41.17265  45.25597  1.000 31.83538  ?  61  ILE   A CD1 1 
ATOM   6058  N N   . GLN   E  1 62  ? 42.10848  39.82339  43.92636  1.000 26.06648  ?  62  GLN   A N   1 
ATOM   6059  C CA  . GLN   E  1 62  ? 43.45157  39.46065  44.36057  1.000 34.32940  ?  62  GLN   A CA  1 
ATOM   6060  C C   . GLN   E  1 62  ? 44.49950  40.28710  43.62618  1.000 19.71269  ?  62  GLN   A C   1 
ATOM   6061  O O   . GLN   E  1 62  ? 45.45844  40.76187  44.24228  1.000 97.78355  ?  62  GLN   A O   1 
ATOM   6062  C CB  . GLN   E  1 62  ? 43.70994  37.96483  44.20276  1.000 30.28362  ?  62  GLN   A CB  1 
ATOM   6063  C CG  . GLN   E  1 62  ? 43.84319  37.25446  45.56087  1.000 43.17319  ?  62  GLN   A CG  1 
ATOM   6064  C CD  . GLN   E  1 62  ? 44.88320  37.88131  46.52419  1.000 98.18452  ?  62  GLN   A CD  1 
ATOM   6065  O OE1 . GLN   E  1 62  ? 45.87348  38.50644  46.11326  1.000 49.57228  ?  62  GLN   A OE1 1 
ATOM   6066  N NE2 . GLN   E  1 62  ? 44.65641  37.68849  47.82022  1.000 103.40483 ?  62  GLN   A NE2 1 
ATOM   6067  N N   . GLU   E  1 63  ? 44.31390  40.49650  42.31176  1.000 25.91539  ?  63  GLU   A N   1 
ATOM   6068  C CA  . GLU   E  1 63  ? 45.22473  41.35851  41.56202  1.000 41.75216  ?  63  GLU   A CA  1 
ATOM   6069  C C   . GLU   E  1 63  ? 45.13572  42.80089  42.04317  1.000 43.97157  ?  63  GLU   A C   1 
ATOM   6070  O O   . GLU   E  1 63  ? 46.15072  43.50693  42.09928  1.000 37.29200  ?  63  GLU   A O   1 
ATOM   6071  C CB  . GLU   E  1 63  ? 44.92563  41.26617  40.07472  1.000 25.87175  ?  63  GLU   A CB  1 
ATOM   6072  C CG  . GLU   E  1 63  ? 45.67105  40.14187  39.37683  1.000 63.44664  ?  63  GLU   A CG  1 
ATOM   6073  C CD  . GLU   E  1 63  ? 44.80707  39.38057  38.39776  1.000 50.23894  ?  63  GLU   A CD  1 
ATOM   6074  O OE1 . GLU   E  1 63  ? 43.69493  39.85946  38.07895  1.000 96.69842  ?  63  GLU   A OE1 1 
ATOM   6075  O OE2 . GLU   E  1 63  ? 45.24000  38.29733  37.94364  1.000 124.29195 -1 63  GLU   A OE2 1 
ATOM   6076  N N   . PHE   E  1 64  ? 43.92345  43.24583  42.40260  1.000 34.10163  ?  64  PHE   A N   1 
ATOM   6077  C CA  . PHE   E  1 64  ? 43.72590  44.56610  42.99526  1.000 27.55027  ?  64  PHE   A CA  1 
ATOM   6078  C C   . PHE   E  1 64  ? 44.54696  44.71939  44.26951  1.000 41.58700  ?  64  PHE   A C   1 
ATOM   6079  O O   . PHE   E  1 64  ? 45.33145  45.66692  44.40855  1.000 36.14610  ?  64  PHE   A O   1 
ATOM   6080  C CB  . PHE   E  1 64  ? 42.23210  44.77057  43.26661  1.000 30.64426  ?  64  PHE   A CB  1 
ATOM   6081  C CG  . PHE   E  1 64  ? 41.89358  46.03520  44.01245  1.000 35.81700  ?  64  PHE   A CG  1 
ATOM   6082  C CD1 . PHE   E  1 64  ? 41.98423  47.27038  43.39566  1.000 43.76208  ?  64  PHE   A CD1 1 
ATOM   6083  C CD2 . PHE   E  1 64  ? 41.43421  45.98056  45.32438  1.000 24.85173  ?  64  PHE   A CD2 1 
ATOM   6084  C CE1 . PHE   E  1 64  ? 41.64728  48.43293  44.08748  1.000 29.75399  ?  64  PHE   A CE1 1 
ATOM   6085  C CE2 . PHE   E  1 64  ? 41.08281  47.13451  46.01954  1.000 23.10229  ?  64  PHE   A CE2 1 
ATOM   6086  C CZ  . PHE   E  1 64  ? 41.18839  48.36097  45.40344  1.000 31.83975  ?  64  PHE   A CZ  1 
ATOM   6087  N N   . LYS   E  1 65  ? 44.38123  43.77776  45.21002  1.000 31.48037  ?  65  LYS   A N   1 
ATOM   6088  C CA  . LYS   E  1 65  ? 45.16888  43.77904  46.44657  1.000 26.41701  ?  65  LYS   A CA  1 
ATOM   6089  C C   . LYS   E  1 65  ? 46.66823  43.69620  46.16159  1.000 46.60334  ?  65  LYS   A C   1 
ATOM   6090  O O   . LYS   E  1 65  ? 47.47535  44.37898  46.80598  1.000 38.15903  ?  65  LYS   A O   1 
ATOM   6091  C CB  . LYS   E  1 65  ? 44.72981  42.61983  47.34335  1.000 33.67421  ?  65  LYS   A CB  1 
ATOM   6092  C CG  . LYS   E  1 65  ? 45.42346  42.54266  48.69488  1.000 34.70926  ?  65  LYS   A CG  1 
ATOM   6093  C CD  . LYS   E  1 65  ? 44.51568  41.84906  49.69490  1.000 45.24346  ?  65  LYS   A CD  1 
ATOM   6094  C CE  . LYS   E  1 65  ? 45.05069  40.50657  50.11513  1.000 52.99666  ?  65  LYS   A CE  1 
ATOM   6095  N NZ  . LYS   E  1 65  ? 45.18020  40.48379  51.59237  1.000 64.06142  ?  65  LYS   A NZ  1 
ATOM   6096  N N   . ALA   E  1 66  ? 47.06310  42.85565  45.20272  1.000 41.30408  ?  66  ALA   A N   1 
ATOM   6097  C CA  . ALA   E  1 66  ? 48.48104  42.73986  44.88025  1.000 44.53807  ?  66  ALA   A CA  1 
ATOM   6098  C C   . ALA   E  1 66  ? 49.02841  44.05911  44.34301  1.000 54.85241  ?  66  ALA   A C   1 
ATOM   6099  O O   . ALA   E  1 66  ? 50.19613  44.40959  44.57865  1.000 39.27611  ?  66  ALA   A O   1 
ATOM   6100  C CB  . ALA   E  1 66  ? 48.69244  41.61082  43.87508  1.000 21.83138  ?  66  ALA   A CB  1 
ATOM   6101  N N   . PHE   E  1 67  ? 48.19268  44.81205  43.62707  1.000 48.92231  ?  67  PHE   A N   1 
ATOM   6102  C CA  . PHE   E  1 67  ? 48.64441  46.09033  43.10189  1.000 27.37161  ?  67  PHE   A CA  1 
ATOM   6103  C C   . PHE   E  1 67  ? 48.86495  47.08810  44.23339  1.000 43.35681  ?  67  PHE   A C   1 
ATOM   6104  O O   . PHE   E  1 67  ? 49.90202  47.76186  44.28580  1.000 39.62756  ?  67  PHE   A O   1 
ATOM   6105  C CB  . PHE   E  1 67  ? 47.64590  46.63332  42.07378  1.000 28.58805  ?  67  PHE   A CB  1 
ATOM   6106  C CG  . PHE   E  1 67  ? 47.94097  48.03308  41.67346  1.000 29.56291  ?  67  PHE   A CG  1 
ATOM   6107  C CD1 . PHE   E  1 67  ? 48.97083  48.28838  40.78165  1.000 15.94793  ?  67  PHE   A CD1 1 
ATOM   6108  C CD2 . PHE   E  1 67  ? 47.24806  49.10809  42.25005  1.000 23.52327  ?  67  PHE   A CD2 1 
ATOM   6109  C CE1 . PHE   E  1 67  ? 49.30098  49.59301  40.42771  1.000 23.08620  ?  67  PHE   A CE1 1 
ATOM   6110  C CE2 . PHE   E  1 67  ? 47.57115  50.42028  41.92174  1.000 33.41119  ?  67  PHE   A CE2 1 
ATOM   6111  C CZ  . PHE   E  1 67  ? 48.59483  50.67021  41.00344  1.000 20.46611  ?  67  PHE   A CZ  1 
ATOM   6112  N N   . ILE   E  1 68  ? 47.89397  47.19259  45.14727  1.000 35.41047  ?  68  ILE   A N   1 
ATOM   6113  C CA  . ILE   E  1 68  ? 48.02038  48.07482  46.30822  1.000 37.59273  ?  68  ILE   A CA  1 
ATOM   6114  C C   . ILE   E  1 68  ? 49.33502  47.82063  47.03122  1.000 43.67999  ?  68  ILE   A C   1 
ATOM   6115  O O   . ILE   E  1 68  ? 50.03119  48.75312  47.45231  1.000 41.31199  ?  68  ILE   A O   1 
ATOM   6116  C CB  . ILE   E  1 68  ? 46.81664  47.87168  47.24992  1.000 27.50999  ?  68  ILE   A CB  1 
ATOM   6117  C CG1 . ILE   E  1 68  ? 45.51973  48.33263  46.56697  1.000 34.60868  ?  68  ILE   A CG1 1 
ATOM   6118  C CG2 . ILE   E  1 68  ? 47.03283  48.58286  48.57140  1.000 32.90088  ?  68  ILE   A CG2 1 
ATOM   6119  C CD1 . ILE   E  1 68  ? 44.27955  48.03623  47.35023  1.000 27.58704  ?  68  ILE   A CD1 1 
ATOM   6120  N N   . GLU   E  1 69  ? 49.69667  46.54857  47.17418  1.000 57.75150  ?  69  GLU   A N   1 
ATOM   6121  C CA  . GLU   E  1 69  ? 50.89482  46.14046  47.88802  1.000 32.31447  ?  69  GLU   A CA  1 
ATOM   6122  C C   . GLU   E  1 69  ? 52.15739  46.27089  47.04630  1.000 41.66503  ?  69  GLU   A C   1 
ATOM   6123  O O   . GLU   E  1 69  ? 53.25290  46.29698  47.60965  1.000 42.17238  ?  69  GLU   A O   1 
ATOM   6124  C CB  . GLU   E  1 69  ? 50.72220  44.69631  48.36177  1.000 38.65454  ?  69  GLU   A CB  1 
ATOM   6125  C CG  . GLU   E  1 69  ? 49.78582  44.56492  49.56267  1.000 24.66186  ?  69  GLU   A CG  1 
ATOM   6126  C CD  . GLU   E  1 69  ? 49.23416  43.15151  49.76149  1.000 65.87239  ?  69  GLU   A CD  1 
ATOM   6127  O OE1 . GLU   E  1 69  ? 49.50661  42.25924  48.91212  1.000 38.32036  ?  69  GLU   A OE1 1 
ATOM   6128  O OE2 . GLU   E  1 69  ? 48.51543  42.94556  50.77229  1.000 45.12667  -1 69  GLU   A OE2 1 
ATOM   6129  N N   . SER   E  1 70  ? 52.02855  46.37402  45.72226  1.000 48.77542  ?  70  SER   A N   1 
ATOM   6130  C CA  . SER   E  1 70  ? 53.18487  46.41648  44.83582  1.000 20.55710  ?  70  SER   A CA  1 
ATOM   6131  C C   . SER   E  1 70  ? 53.92655  47.74957  44.85021  1.000 49.31926  ?  70  SER   A C   1 
ATOM   6132  O O   . SER   E  1 70  ? 55.05450  47.80479  44.35055  1.000 34.05215  ?  70  SER   A O   1 
ATOM   6133  C CB  . SER   E  1 70  ? 52.75818  46.12294  43.39371  1.000 33.15608  ?  70  SER   A CB  1 
ATOM   6134  O OG  . SER   E  1 70  ? 51.97769  47.19241  42.87102  1.000 54.49349  ?  70  SER   A OG  1 
ATOM   6135  N N   . ASP   E  1 71  ? 53.32723  48.82164  45.36900  1.000 34.97078  ?  71  ASP   A N   1 
ATOM   6136  C CA  . ASP   E  1 71  ? 53.92395  50.15845  45.30880  1.000 30.25316  ?  71  ASP   A CA  1 
ATOM   6137  C C   . ASP   E  1 71  ? 53.82006  50.76822  46.69965  1.000 36.52210  ?  71  ASP   A C   1 
ATOM   6138  O O   . ASP   E  1 71  ? 52.69411  50.99936  47.19575  1.000 36.42529  ?  71  ASP   A O   1 
ATOM   6139  C CB  . ASP   E  1 71  ? 53.22909  51.03794  44.25459  1.000 39.41867  ?  71  ASP   A CB  1 
ATOM   6140  C CG  . ASP   E  1 71  ? 53.79582  52.47961  44.17039  1.000 78.67854  ?  71  ASP   A CG  1 
ATOM   6141  O OD1 . ASP   E  1 71  ? 54.33113  53.03220  45.16818  1.000 42.60266  ?  71  ASP   A OD1 1 
ATOM   6142  O OD2 . ASP   E  1 71  ? 53.67728  53.08970  43.08219  1.000 56.50762  -1 71  ASP   A OD2 1 
ATOM   6143  N N   . PRO   E  1 72  ? 54.94038  51.06992  47.34570  1.000 45.10300  ?  72  PRO   A N   1 
ATOM   6144  C CA  . PRO   E  1 72  ? 54.87432  51.57365  48.72878  1.000 43.35172  ?  72  PRO   A CA  1 
ATOM   6145  C C   . PRO   E  1 72  ? 54.08302  52.86814  48.87899  1.000 34.20494  ?  72  PRO   A C   1 
ATOM   6146  O O   . PRO   E  1 72  ? 53.46861  53.08272  49.92986  1.000 39.94402  ?  72  PRO   A O   1 
ATOM   6147  C CB  . PRO   E  1 72  ? 56.35242  51.75873  49.09935  1.000 29.56994  ?  72  PRO   A CB  1 
ATOM   6148  C CG  . PRO   E  1 72  ? 57.08250  51.84337  47.77315  1.000 35.41464  ?  72  PRO   A CG  1 
ATOM   6149  C CD  . PRO   E  1 72  ? 56.31185  50.99494  46.81696  1.000 21.36993  ?  72  PRO   A CD  1 
ATOM   6150  N N   . VAL   E  1 73  ? 54.06883  53.73823  47.86549  1.000 37.02938  ?  73  VAL   A N   1 
ATOM   6151  C CA  . VAL   E  1 73  ? 53.28865  54.97145  47.96109  1.000 48.01479  ?  73  VAL   A CA  1 
ATOM   6152  C C   . VAL   E  1 73  ? 51.79654  54.66917  47.91475  1.000 55.60995  ?  73  VAL   A C   1 
ATOM   6153  O O   . VAL   E  1 73  ? 51.01505  55.20543  48.71316  1.000 26.62925  ?  73  VAL   A O   1 
ATOM   6154  C CB  . VAL   E  1 73  ? 53.68238  55.94524  46.84196  1.000 44.75864  ?  73  VAL   A CB  1 
ATOM   6155  C CG1 . VAL   E  1 73  ? 52.92416  57.23292  47.00544  1.000 21.81022  ?  73  VAL   A CG1 1 
ATOM   6156  C CG2 . VAL   E  1 73  ? 55.16309  56.19881  46.86818  1.000 19.64866  ?  73  VAL   A CG2 1 
ATOM   6157  N N   . VAL   E  1 74  ? 51.38058  53.83477  46.95176  1.000 41.13258  ?  74  VAL   A N   1 
ATOM   6158  C CA  . VAL   E  1 74  ? 49.98680  53.40441  46.86078  1.000 31.72993  ?  74  VAL   A CA  1 
ATOM   6159  C C   . VAL   E  1 74  ? 49.56884  52.72101  48.15468  1.000 42.56228  ?  74  VAL   A C   1 
ATOM   6160  O O   . VAL   E  1 74  ? 48.52592  53.03873  48.74367  1.000 47.19212  ?  74  VAL   A O   1 
ATOM   6161  C CB  . VAL   E  1 74  ? 49.79664  52.47178  45.64721  1.000 33.85648  ?  74  VAL   A CB  1 
ATOM   6162  C CG1 . VAL   E  1 74  ? 48.37273  51.90410  45.58296  1.000 16.78460  ?  74  VAL   A CG1 1 
ATOM   6163  C CG2 . VAL   E  1 74  ? 50.11769  53.19703  44.38437  1.000 23.62122  ?  74  VAL   A CG2 1 
ATOM   6164  N N   . HIS   E  1 75  ? 50.38923  51.77167  48.61421  1.000 43.67632  ?  75  HIS   A N   1 
ATOM   6165  C CA  . HIS   E  1 75  ? 50.12081  51.06432  49.86171  1.000 36.37680  ?  75  HIS   A CA  1 
ATOM   6166  C C   . HIS   E  1 75  ? 49.89775  52.03961  51.01612  1.000 25.21746  ?  75  HIS   A C   1 
ATOM   6167  O O   . HIS   E  1 75  ? 48.93323  51.91405  51.78264  1.000 32.13214  ?  75  HIS   A O   1 
ATOM   6168  C CB  . HIS   E  1 75  ? 51.28919  50.12841  50.15821  1.000 27.94962  ?  75  HIS   A CB  1 
ATOM   6169  C CG  . HIS   E  1 75  ? 50.99487  49.10317  51.20244  1.000 60.77729  ?  75  HIS   A CG  1 
ATOM   6170  N ND1 . HIS   E  1 75  ? 51.64844  47.89380  51.25414  1.000 70.22522  ?  75  HIS   A ND1 1 
ATOM   6171  C CD2 . HIS   E  1 75  ? 50.11620  49.10295  52.23132  1.000 62.22469  ?  75  HIS   A CD2 1 
ATOM   6172  C CE1 . HIS   E  1 75  ? 51.18066  47.19010  52.26797  1.000 57.71770  ?  75  HIS   A CE1 1 
ATOM   6173  N NE2 . HIS   E  1 75  ? 50.25487  47.90364  52.88113  1.000 44.39753  ?  75  HIS   A NE2 1 
ATOM   6174  N N   . GLN   E  1 76  ? 50.78196  53.03120  51.14723  1.000 38.56381  ?  76  GLN   A N   1 
ATOM   6175  C CA  . GLN   E  1 76  ? 50.63287  54.00488  52.22057  1.000 17.23889  ?  76  GLN   A CA  1 
ATOM   6176  C C   . GLN   E  1 76  ? 49.31080  54.75509  52.09511  1.000 40.43300  ?  76  GLN   A C   1 
ATOM   6177  O O   . GLN   E  1 76  ? 48.62798  54.99411  53.09872  1.000 29.69998  ?  76  GLN   A O   1 
ATOM   6178  C CB  . GLN   E  1 76  ? 51.82014  54.97209  52.21466  1.000 42.65981  ?  76  GLN   A CB  1 
ATOM   6179  C CG  . GLN   E  1 76  ? 51.93275  55.80028  53.48173  1.000 18.63786  ?  76  GLN   A CG  1 
ATOM   6180  C CD  . GLN   E  1 76  ? 51.94232  54.95068  54.73301  1.000 76.90690  ?  76  GLN   A CD  1 
ATOM   6181  O OE1 . GLN   E  1 76  ? 52.77820  54.05442  54.88120  1.000 36.55337  ?  76  GLN   A OE1 1 
ATOM   6182  N NE2 . GLN   E  1 76  ? 51.00979  55.22295  55.64144  1.000 28.62867  ?  76  GLN   A NE2 1 
ATOM   6183  N N   . GLU   E  1 77  ? 48.92428  55.11532  50.86352  1.000 38.91298  ?  77  GLU   A N   1 
ATOM   6184  C CA  . GLU   E  1 77  ? 47.63148  55.75714  50.65166  1.000 29.90680  ?  77  GLU   A CA  1 
ATOM   6185  C C   . GLU   E  1 77  ? 46.48894  54.86899  51.13992  1.000 57.26761  ?  77  GLU   A C   1 
ATOM   6186  O O   . GLU   E  1 77  ? 45.54015  55.35692  51.77177  1.000 23.87324  ?  77  GLU   A O   1 
ATOM   6187  C CB  . GLU   E  1 77  ? 47.46348  56.11185  49.17703  1.000 29.44772  ?  77  GLU   A CB  1 
ATOM   6188  C CG  . GLU   E  1 77  ? 48.18187  57.39976  48.80340  1.000 24.54340  ?  77  GLU   A CG  1 
ATOM   6189  C CD  . GLU   E  1 77  ? 48.41401  57.57226  47.30111  1.000 56.93243  ?  77  GLU   A CD  1 
ATOM   6190  O OE1 . GLU   E  1 77  ? 48.04697  56.65422  46.52554  1.000 38.59138  ?  77  GLU   A OE1 1 
ATOM   6191  O OE2 . GLU   E  1 77  ? 48.96541  58.63742  46.90432  1.000 32.34941  -1 77  GLU   A OE2 1 
ATOM   6192  N N   . PHE   E  1 78  ? 46.58218  53.55396  50.90132  1.000 24.57191  ?  78  PHE   A N   1 
ATOM   6193  C CA  . PHE   E  1 78  ? 45.55215  52.62221  51.35618  1.000 45.63874  ?  78  PHE   A CA  1 
ATOM   6194  C C   . PHE   E  1 78  ? 45.66854  52.29164  52.83464  1.000 44.90597  ?  78  PHE   A C   1 
ATOM   6195  O O   . PHE   E  1 78  ? 44.88950  51.47833  53.34352  1.000 52.56756  ?  78  PHE   A O   1 
ATOM   6196  C CB  . PHE   E  1 78  ? 45.57477  51.32605  50.53132  1.000 26.21671  ?  78  PHE   A CB  1 
ATOM   6197  C CG  . PHE   E  1 78  ? 44.75348  51.40965  49.29592  1.000 44.67566  ?  78  PHE   A CG  1 
ATOM   6198  C CD1 . PHE   E  1 78  ? 43.38539  51.15659  49.34695  1.000 31.01367  ?  78  PHE   A CD1 1 
ATOM   6199  C CD2 . PHE   E  1 78  ? 45.33099  51.80499  48.08609  1.000 19.46478  ?  78  PHE   A CD2 1 
ATOM   6200  C CE1 . PHE   E  1 78  ? 42.59829  51.25612  48.19714  1.000 28.91400  ?  78  PHE   A CE1 1 
ATOM   6201  C CE2 . PHE   E  1 78  ? 44.55783  51.91702  46.92861  1.000 39.24855  ?  78  PHE   A CE2 1 
ATOM   6202  C CZ  . PHE   E  1 78  ? 43.18583  51.63931  46.97726  1.000 26.65542  ?  78  PHE   A CZ  1 
ATOM   6203  N N   . ILE   E  1 79  ? 46.60625  52.90028  53.54409  1.000 37.32262  ?  79  ILE   A N   1 
ATOM   6204  C CA  . ILE   E  1 79  ? 46.59684  52.88319  54.99018  1.000 30.97249  ?  79  ILE   A CA  1 
ATOM   6205  C C   . ILE   E  1 79  ? 46.05999  54.19472  55.53655  1.000 47.70799  ?  79  ILE   A C   1 
ATOM   6206  O O   . ILE   E  1 79  ? 45.09174  54.21417  56.29892  1.000 24.04215  ?  79  ILE   A O   1 
ATOM   6207  C CB  . ILE   E  1 79  ? 48.00856  52.57978  55.54126  1.000 39.73732  ?  79  ILE   A CB  1 
ATOM   6208  C CG1 . ILE   E  1 79  ? 48.36049  51.12561  55.28656  1.000 26.18431  ?  79  ILE   A CG1 1 
ATOM   6209  C CG2 . ILE   E  1 79  ? 48.07436  52.90630  57.01403  1.000 26.98735  ?  79  ILE   A CG2 1 
ATOM   6210  C CD1 . ILE   E  1 79  ? 49.80481  50.86023  55.41166  1.000 23.43310  ?  79  ILE   A CD1 1 
ATOM   6211  N N   . ASP   E  1 80  ? 46.65908  55.31454  55.11203  1.000 22.15060  ?  80  ASP   A N   1 
ATOM   6212  C CA  . ASP   E  1 80  ? 46.28045  56.60954  55.66183  1.000 38.25074  ?  80  ASP   A CA  1 
ATOM   6213  C C   . ASP   E  1 80  ? 44.80308  56.91040  55.45410  1.000 29.42780  ?  80  ASP   A C   1 
ATOM   6214  O O   . ASP   E  1 80  ? 44.18188  57.55358  56.30991  1.000 38.58113  ?  80  ASP   A O   1 
ATOM   6215  C CB  . ASP   E  1 80  ? 47.14557  57.70028  55.04175  1.000 32.05156  ?  80  ASP   A CB  1 
ATOM   6216  C CG  . ASP   E  1 80  ? 48.64214  57.48695  55.30631  1.000 50.34256  ?  80  ASP   A CG  1 
ATOM   6217  O OD1 . ASP   E  1 80  ? 48.99630  56.67450  56.18668  1.000 48.52842  ?  80  ASP   A OD1 1 
ATOM   6218  O OD2 . ASP   E  1 80  ? 49.46645  58.13988  54.61489  1.000 56.21996  -1 80  ASP   A OD2 1 
ATOM   6219  N N   . MET   E  1 81  ? 44.21894  56.44880  54.33544  1.000 33.86731  ?  81  MET   A N   1 
ATOM   6220  C CA  . MET   E  1 81  ? 42.82095  56.75871  54.03926  1.000 27.57274  ?  81  MET   A CA  1 
ATOM   6221  C C   . MET   E  1 81  ? 41.85757  56.15181  55.06937  1.000 50.34705  ?  81  MET   A C   1 
ATOM   6222  O O   . MET   E  1 81  ? 40.71187  56.62379  55.17044  1.000 37.70874  ?  81  MET   A O   1 
ATOM   6223  C CB  . MET   E  1 81  ? 42.43465  56.28949  52.61960  1.000 27.57773  ?  81  MET   A CB  1 
ATOM   6224  C CG  . MET   E  1 81  ? 42.35514  54.77636  52.41555  1.000 34.04010  ?  81  MET   A CG  1 
ATOM   6225  S SD  . MET   E  1 81  ? 41.80908  54.19719  50.76710  1.000 33.92446  ?  81  MET   A SD  1 
ATOM   6226  C CE  . MET   E  1 81  ? 42.95759  55.02341  49.65337  1.000 30.54252  ?  81  MET   A CE  1 
ATOM   6227  N N   . PHE   E  1 82  ? 42.29705  55.15680  55.86455  1.000 25.51883  ?  82  PHE   A N   1 
ATOM   6228  C CA  . PHE   E  1 82  ? 41.45166  54.52475  56.86780  1.000 50.91901  ?  82  PHE   A CA  1 
ATOM   6229  C C   . PHE   E  1 82  ? 41.61915  55.11853  58.25674  1.000 23.78024  ?  82  PHE   A C   1 
ATOM   6230  O O   . PHE   E  1 82  ? 40.99048  54.62421  59.20066  1.000 87.16179  ?  82  PHE   A O   1 
ATOM   6231  C CB  . PHE   E  1 82  ? 41.75496  53.03931  56.91889  1.000 26.41164  ?  82  PHE   A CB  1 
ATOM   6232  C CG  . PHE   E  1 82  ? 41.19302  52.28744  55.78471  1.000 69.56637  ?  82  PHE   A CG  1 
ATOM   6233  C CD1 . PHE   E  1 82  ? 39.86799  51.88947  55.80444  1.000 23.49184  ?  82  PHE   A CD1 1 
ATOM   6234  C CD2 . PHE   E  1 82  ? 41.97198  51.99834  54.68378  1.000 26.10403  ?  82  PHE   A CD2 1 
ATOM   6235  C CE1 . PHE   E  1 82  ? 39.33289  51.19783  54.74548  1.000 42.25468  ?  82  PHE   A CE1 1 
ATOM   6236  C CE2 . PHE   E  1 82  ? 41.44735  51.30991  53.62495  1.000 43.52150  ?  82  PHE   A CE2 1 
ATOM   6237  C CZ  . PHE   E  1 82  ? 40.11863  50.91133  53.65237  1.000 19.22579  ?  82  PHE   A CZ  1 
ATOM   6238  N N   . GLU   E  1 83  ? 42.44789  56.15794  58.40081  1.000 53.67149  ?  83  GLU   A N   1 
ATOM   6239  C CA  . GLU   E  1 83  ? 42.84829  56.64656  59.71626  1.000 58.43604  ?  83  GLU   A CA  1 
ATOM   6240  C C   . GLU   E  1 83  ? 41.65048  56.91871  60.60265  1.000 66.76471  ?  83  GLU   A C   1 
ATOM   6241  O O   . GLU   E  1 83  ? 40.77369  57.70358  60.24932  1.000 43.02900  ?  83  GLU   A O   1 
ATOM   6242  C CB  . GLU   E  1 83  ? 43.70826  57.89841  59.57477  1.000 33.76988  ?  83  GLU   A CB  1 
ATOM   6243  C CG  . GLU   E  1 83  ? 43.84220  58.88418  60.77975  1.000 35.60004  ?  83  GLU   A CG  1 
ATOM   6244  C CD  . GLU   E  1 83  ? 44.42290  60.36076  60.39967  1.000 24.43792  ?  83  GLU   A CD  1 
ATOM   6245  O OE1 . GLU   E  1 83  ? 45.51912  60.45275  59.76389  1.000 104.71426 ?  83  GLU   A OE1 1 
ATOM   6246  O OE2 . GLU   E  1 83  ? 43.80100  61.43629  60.72204  1.000 64.17090  ?  83  GLU   A OE2 1 
ATOM   6247  N N   . GLY   E  1 84  ? 41.61672  56.24818  61.75394  1.000 77.67883  ?  84  GLY   A N   1 
ATOM   6248  C CA  . GLY   E  1 84  ? 40.55752  56.44475  62.72283  1.000 42.03598  ?  84  GLY   A CA  1 
ATOM   6249  C C   . GLY   E  1 84  ? 39.19851  55.89498  62.36221  1.000 75.12180  ?  84  GLY   A C   1 
ATOM   6250  O O   . GLY   E  1 84  ? 38.23896  56.11962  63.10243  1.000 60.23904  ?  84  GLY   A O   1 
ATOM   6251  N N   . ILE   E  1 85  ? 39.08097  55.18120  61.24978  1.000 75.96304  ?  85  ILE   A N   1 
ATOM   6252  C CA  . ILE   E  1 85  ? 37.80776  54.58184  60.86894  1.000 55.57286  ?  85  ILE   A CA  1 
ATOM   6253  C C   . ILE   E  1 85  ? 37.53443  53.39475  61.77539  1.000 65.78210  ?  85  ILE   A C   1 
ATOM   6254  O O   . ILE   E  1 85  ? 38.32646  52.44314  61.85193  1.000 59.92877  ?  85  ILE   A O   1 
ATOM   6255  C CB  . ILE   E  1 85  ? 37.81271  54.17815  59.38800  1.000 48.98885  ?  85  ILE   A CB  1 
ATOM   6256  C CG1 . ILE   E  1 85  ? 37.96029  55.43183  58.52079  1.000 64.26345  ?  85  ILE   A CG1 1 
ATOM   6257  C CG2 . ILE   E  1 85  ? 36.57253  53.33419  59.04179  1.000 51.10510  ?  85  ILE   A CG2 1 
ATOM   6258  C CD1 . ILE   E  1 85  ? 37.53720  55.26665  57.09728  1.000 56.16904  ?  85  ILE   A CD1 1 
ATOM   6259  N N   . GLN   E  1 86  ? 36.44140  53.48863  62.51773  1.000 64.85287  ?  86  GLN   A N   1 
ATOM   6260  C CA  . GLN   E  1 86  ? 36.10183  52.46684  63.48509  1.000 96.46805  ?  86  GLN   A CA  1 
ATOM   6261  C C   . GLN   E  1 86  ? 35.18378  51.39159  62.90281  1.000 47.30747  ?  86  GLN   A C   1 
ATOM   6262  O O   . GLN   E  1 86  ? 35.16055  50.27008  63.42362  1.000 94.00408  ?  86  GLN   A O   1 
ATOM   6263  C CB  . GLN   E  1 86  ? 35.44344  53.09486  64.71924  1.000 60.60354  ?  86  GLN   A CB  1 
ATOM   6264  N N   . ASP   E  1 87  ? 34.47951  51.67114  61.80416  1.000 84.24634  ?  87  ASP   A N   1 
ATOM   6265  C CA  . ASP   E  1 87  ? 33.55718  50.70819  61.21433  1.000 50.51873  ?  87  ASP   A CA  1 
ATOM   6266  C C   . ASP   E  1 87  ? 34.18264  49.93849  60.05556  1.000 39.67057  ?  87  ASP   A C   1 
ATOM   6267  O O   . ASP   E  1 87  ? 35.23910  50.28365  59.52325  1.000 60.05824  ?  87  ASP   A O   1 
ATOM   6268  C CB  . ASP   E  1 87  ? 32.29175  51.40941  60.71862  1.000 42.77329  ?  87  ASP   A CB  1 
ATOM   6269  C CG  . ASP   E  1 87  ? 31.73053  52.35061  61.74183  1.000 115.53879 ?  87  ASP   A CG  1 
ATOM   6270  O OD1 . ASP   E  1 87  ? 32.05830  52.18102  62.94044  1.000 95.79450  ?  87  ASP   A OD1 1 
ATOM   6271  O OD2 . ASP   E  1 87  ? 30.97146  53.27172  61.32920  1.000 93.83371  -1 87  ASP   A OD2 1 
ATOM   6272  N N   . SER   E  1 88  ? 33.47935  48.90616  59.65148  1.000 44.13452  ?  88  SER   A N   1 
ATOM   6273  C CA  . SER   E  1 88  ? 33.88886  48.08384  58.53098  1.000 33.21216  ?  88  SER   A CA  1 
ATOM   6274  C C   . SER   E  1 88  ? 33.55156  48.78837  57.21312  1.000 75.60068  ?  88  SER   A C   1 
ATOM   6275  O O   . SER   E  1 88  ? 32.40997  49.23357  57.02553  1.000 43.10088  ?  88  SER   A O   1 
ATOM   6276  C CB  . SER   E  1 88  ? 33.20257  46.72908  58.61758  1.000 34.26126  ?  88  SER   A CB  1 
ATOM   6277  O OG  . SER   E  1 88  ? 34.14891  45.67680  58.71662  1.000 50.39154  ?  88  SER   A OG  1 
ATOM   6278  N N   . PRO   E  1 89  ? 34.51915  48.91958  56.26868  1.000 47.54511  ?  89  PRO   A N   1 
ATOM   6279  C CA  . PRO   E  1 89  ? 35.90451  48.42427  56.27615  1.000 24.06162  ?  89  PRO   A CA  1 
ATOM   6280  C C   . PRO   E  1 89  ? 36.86453  49.26065  57.12622  1.000 51.76674  ?  89  PRO   A C   1 
ATOM   6281  O O   . PRO   E  1 89  ? 36.84535  50.48752  57.05591  1.000 34.36519  ?  89  PRO   A O   1 
ATOM   6282  C CB  . PRO   E  1 89  ? 36.32910  48.50963  54.80269  1.000 46.43028  ?  89  PRO   A CB  1 
ATOM   6283  C CG  . PRO   E  1 89  ? 35.19894  49.21328  54.05954  1.000 44.09994  ?  89  PRO   A CG  1 
ATOM   6284  C CD  . PRO   E  1 89  ? 34.28276  49.77827  55.10270  1.000 38.69635  ?  89  PRO   A CD  1 
ATOM   6285  N N   . ARG   E  1 90  ? 37.74818  48.62715  57.90159  1.000 37.92321  ?  90  ARG   A N   1 
ATOM   6286  C CA  . ARG   E  1 90  ? 38.74194  49.36165  58.67383  1.000 54.92218  ?  90  ARG   A CA  1 
ATOM   6287  C C   . ARG   E  1 90  ? 40.12581  49.33928  58.03507  1.000 45.60709  ?  90  ARG   A C   1 
ATOM   6288  O O   . ARG   E  1 90  ? 40.99062  50.11513  58.43395  1.000 45.19449  ?  90  ARG   A O   1 
ATOM   6289  C CB  . ARG   E  1 90  ? 38.84080  48.81053  60.10285  1.000 39.31332  ?  90  ARG   A CB  1 
ATOM   6290  C CG  . ARG   E  1 90  ? 37.94295  49.38032  61.13067  1.000 114.95184 ?  90  ARG   A CG  1 
ATOM   6291  C CD  . ARG   E  1 90  ? 37.49829  48.24418  62.05772  1.000 19.30294  ?  90  ARG   A CD  1 
ATOM   6292  N NE  . ARG   E  1 90  ? 38.44175  47.13802  62.19720  1.000 83.93895  ?  90  ARG   A NE  1 
ATOM   6293  C CZ  . ARG   E  1 90  ? 38.47514  46.32804  63.25128  1.000 121.97050 ?  90  ARG   A CZ  1 
ATOM   6294  N NH1 . ARG   E  1 90  ? 37.89463  46.66231  64.39345  1.000 99.17070  ?  90  ARG   A NH1 1 
ATOM   6295  N NH2 . ARG   E  1 90  ? 39.03851  45.11498  63.12903  1.000 49.56118  ?  90  ARG   A NH2 1 
ATOM   6296  N N   . ASN   E  1 91  ? 40.36556  48.49301  57.04360  1.000 34.85802  ?  91  ASN   A N   1 
ATOM   6297  C CA  . ASN   E  1 91  ? 41.64563  48.49144  56.35305  1.000 39.33816  ?  91  ASN   A CA  1 
ATOM   6298  C C   . ASN   E  1 91  ? 41.39235  48.03620  54.93427  1.000 37.96470  ?  91  ASN   A C   1 
ATOM   6299  O O   . ASN   E  1 91  ? 40.25937  47.71769  54.54567  1.000 44.51802  ?  91  ASN   A O   1 
ATOM   6300  C CB  . ASN   E  1 91  ? 42.65903  47.57867  57.04707  1.000 31.33956  ?  91  ASN   A CB  1 
ATOM   6301  C CG  . ASN   E  1 91  ? 42.04190  46.24577  57.40665  1.000 42.01707  ?  91  ASN   A CG  1 
ATOM   6302  O OD1 . ASN   E  1 91  ? 41.67509  45.45045  56.53526  1.000 52.20710  ?  91  ASN   A OD1 1 
ATOM   6303  N ND2 . ASN   E  1 91  ? 41.89784  46.00355  58.69197  1.000 38.04278  ?  91  ASN   A ND2 1 
ATOM   6304  N N   . TYR   E  1 92  ? 42.46775  48.00382  54.15635  1.000 41.13203  ?  92  TYR   A N   1 
ATOM   6305  C CA  . TYR   E  1 92  ? 42.28659  47.61848  52.77120  1.000 34.87378  ?  92  TYR   A CA  1 
ATOM   6306  C C   . TYR   E  1 92  ? 41.96519  46.13140  52.65452  1.000 38.96775  ?  92  TYR   A C   1 
ATOM   6307  O O   . TYR   E  1 92  ? 41.29605  45.72142  51.69811  1.000 43.68437  ?  92  TYR   A O   1 
ATOM   6308  C CB  . TYR   E  1 92  ? 43.50265  48.04848  51.92290  1.000 24.09079  ?  92  TYR   A CB  1 
ATOM   6309  C CG  . TYR   E  1 92  ? 44.77066  47.23732  52.03144  1.000 29.55718  ?  92  TYR   A CG  1 
ATOM   6310  C CD1 . TYR   E  1 92  ? 44.94076  46.07611  51.27953  1.000 27.77508  ?  92  TYR   A CD1 1 
ATOM   6311  C CD2 . TYR   E  1 92  ? 45.84439  47.68115  52.82473  1.000 35.99098  ?  92  TYR   A CD2 1 
ATOM   6312  C CE1 . TYR   E  1 92  ? 46.11611  45.34412  51.35263  1.000 46.75648  ?  92  TYR   A CE1 1 
ATOM   6313  C CE2 . TYR   E  1 92  ? 47.02652  46.95398  52.90058  1.000 43.85128  ?  92  TYR   A CE2 1 
ATOM   6314  C CZ  . TYR   E  1 92  ? 47.15261  45.78511  52.16496  1.000 39.39464  ?  92  TYR   A CZ  1 
ATOM   6315  O OH  . TYR   E  1 92  ? 48.29819  45.04593  52.22387  1.000 56.15110  ?  92  TYR   A OH  1 
ATOM   6316  N N   . GLN   E  1 93  ? 42.34572  45.31948  53.64348  1.000 33.94509  ?  93  GLN   A N   1 
ATOM   6317  C CA  . GLN   E  1 93  ? 42.00088  43.90241  53.55593  1.000 46.55287  ?  93  GLN   A CA  1 
ATOM   6318  C C   . GLN   E  1 93  ? 40.50216  43.68953  53.73212  1.000 32.60144  ?  93  GLN   A C   1 
ATOM   6319  O O   . GLN   E  1 93  ? 39.89236  42.88801  53.01421  1.000 38.01155  ?  93  GLN   A O   1 
ATOM   6320  C CB  . GLN   E  1 93  ? 42.76559  43.08767  54.59409  1.000 27.42657  ?  93  GLN   A CB  1 
ATOM   6321  C CG  . GLN   E  1 93  ? 44.20294  42.75502  54.19228  1.000 44.15660  ?  93  GLN   A CG  1 
ATOM   6322  C CD  . GLN   E  1 93  ? 45.21451  43.72509  54.78407  1.000 163.46346 ?  93  GLN   A CD  1 
ATOM   6323  O OE1 . GLN   E  1 93  ? 44.86793  44.84484  55.20727  1.000 41.73624  ?  93  GLN   A OE1 1 
ATOM   6324  N NE2 . GLN   E  1 93  ? 46.47608  43.30011  54.82156  1.000 43.95552  ?  93  GLN   A NE2 1 
ATOM   6325  N N   . GLU   E  1 94  ? 39.88173  44.39666  54.68360  1.000 47.86677  ?  94  GLU   A N   1 
ATOM   6326  C CA  . GLU   E  1 94  ? 38.43299  44.28392  54.83682  1.000 20.20957  ?  94  GLU   A CA  1 
ATOM   6327  C C   . GLU   E  1 94  ? 37.72363  44.85610  53.62476  1.000 54.71492  ?  94  GLU   A C   1 
ATOM   6328  O O   . GLU   E  1 94  ? 36.68651  44.33810  53.19484  1.000 51.77350  ?  94  GLU   A O   1 
ATOM   6329  C CB  . GLU   E  1 94  ? 37.96024  45.02020  56.08072  1.000 51.65071  ?  94  GLU   A CB  1 
ATOM   6330  C CG  . GLU   E  1 94  ? 38.18700  44.26494  57.35482  1.000 73.19355  ?  94  GLU   A CG  1 
ATOM   6331  C CD  . GLU   E  1 94  ? 37.58281  45.00405  58.52734  1.000 135.89234 ?  94  GLU   A CD  1 
ATOM   6332  O OE1 . GLU   E  1 94  ? 36.54124  45.68369  58.30272  1.000 44.35783  ?  94  GLU   A OE1 1 
ATOM   6333  O OE2 . GLU   E  1 94  ? 38.15385  44.91415  59.64262  1.000 98.06498  -1 94  GLU   A OE2 1 
ATOM   6334  N N   . LEU   E  1 95  ? 38.25755  45.95153  53.07148  1.000 52.99934  ?  95  LEU   A N   1 
ATOM   6335  C CA  . LEU   E  1 95  ? 37.70434  46.49828  51.83803  1.000 34.04214  ?  95  LEU   A CA  1 
ATOM   6336  C C   . LEU   E  1 95  ? 37.63548  45.42316  50.76514  1.000 38.17059  ?  95  LEU   A C   1 
ATOM   6337  O O   . LEU   E  1 95  ? 36.57518  45.19311  50.16745  1.000 34.18016  ?  95  LEU   A O   1 
ATOM   6338  C CB  . LEU   E  1 95  ? 38.54016  47.68257  51.35746  1.000 41.15124  ?  95  LEU   A CB  1 
ATOM   6339  C CG  . LEU   E  1 95  ? 37.92116  48.42728  50.16552  1.000 41.21855  ?  95  LEU   A CG  1 
ATOM   6340  C CD1 . LEU   E  1 95  ? 36.56517  49.04316  50.53338  1.000 35.50701  ?  95  LEU   A CD1 1 
ATOM   6341  C CD2 . LEU   E  1 95  ? 38.89206  49.49098  49.70746  1.000 26.70561  ?  95  LEU   A CD2 1 
ATOM   6342  N N   . CYS   E  1 96  ? 38.75251  44.70896  50.55226  1.000 24.79521  ?  96  CYS   A N   1 
ATOM   6343  C CA  . CYS   E  1 96  ? 38.77178  43.65136  49.54766  1.000 35.58423  ?  96  CYS   A CA  1 
ATOM   6344  C C   . CYS   E  1 96  ? 37.76133  42.55442  49.86101  1.000 35.78335  ?  96  CYS   A C   1 
ATOM   6345  O O   . CYS   E  1 96  ? 37.13561  42.00206  48.94588  1.000 55.12257  ?  96  CYS   A O   1 
ATOM   6346  C CB  . CYS   E  1 96  ? 40.16878  43.05978  49.43329  1.000 29.11766  ?  96  CYS   A CB  1 
ATOM   6347  S SG  . CYS   E  1 96  ? 41.42832  44.14569  48.72366  1.000 44.82205  ?  96  CYS   A SG  1 
ATOM   6348  N N   . ASN   E  1 97  ? 37.60264  42.20521  51.14539  1.000 37.42385  ?  97  ASN   A N   1 
ATOM   6349  C CA  . ASN   E  1 97  ? 36.65238  41.15028  51.49555  1.000 27.69397  ?  97  ASN   A CA  1 
ATOM   6350  C C   . ASN   E  1 97  ? 35.21787  41.59389  51.24086  1.000 52.52350  ?  97  ASN   A C   1 
ATOM   6351  O O   . ASN   E  1 97  ? 34.39973  40.80480  50.74973  1.000 33.93583  ?  97  ASN   A O   1 
ATOM   6352  C CB  . ASN   E  1 97  ? 36.81851  40.73156  52.95324  1.000 39.22054  ?  97  ASN   A CB  1 
ATOM   6353  C CG  . ASN   E  1 97  ? 38.08119  39.94791  53.18912  1.000 78.69520  ?  97  ASN   A CG  1 
ATOM   6354  O OD1 . ASN   E  1 97  ? 38.52900  39.19415  52.31997  1.000 51.26110  ?  97  ASN   A OD1 1 
ATOM   6355  N ND2 . ASN   E  1 97  ? 38.67110  40.11846  54.36991  1.000 36.26645  ?  97  ASN   A ND2 1 
ATOM   6356  N N   . MET   E  1 98  ? 34.89403  42.85285  51.56903  1.000 26.95041  ?  98  MET   A N   1 
ATOM   6357  C CA  . MET   E  1 98  ? 33.54888  43.35377  51.30897  1.000 23.27997  ?  98  MET   A CA  1 
ATOM   6358  C C   . MET   E  1 98  ? 33.27595  43.46080  49.80887  1.000 61.32563  ?  98  MET   A C   1 
ATOM   6359  O O   . MET   E  1 98  ? 32.15255  43.19069  49.36394  1.000 41.18455  ?  98  MET   A O   1 
ATOM   6360  C CB  . MET   E  1 98  ? 33.34885  44.69801  52.01969  1.000 30.13698  ?  98  MET   A CB  1 
ATOM   6361  C CG  . MET   E  1 98  ? 33.38365  44.57083  53.54958  1.000 19.13079  ?  98  MET   A CG  1 
ATOM   6362  S SD  . MET   E  1 98  ? 33.38116  46.08739  54.51177  1.000 50.23575  ?  98  MET   A SD  1 
ATOM   6363  C CE  . MET   E  1 98  ? 31.66876  46.58176  54.38072  1.000 36.93342  ?  98  MET   A CE  1 
ATOM   6364  N N   . PHE   E  1 99  ? 34.28972  43.83683  49.01081  1.000 30.20650  ?  99  PHE   A N   1 
ATOM   6365  C CA  . PHE   E  1 99  ? 34.13933  43.80771  47.55324  1.000 26.23500  ?  99  PHE   A CA  1 
ATOM   6366  C C   . PHE   E  1 99  ? 33.74615  42.41096  47.08754  1.000 35.58262  ?  99  PHE   A C   1 
ATOM   6367  O O   . PHE   E  1 99  ? 32.88738  42.24362  46.20960  1.000 34.44764  ?  99  PHE   A O   1 
ATOM   6368  C CB  . PHE   E  1 99  ? 35.44123  44.22685  46.84261  1.000 24.71091  ?  99  PHE   A CB  1 
ATOM   6369  C CG  . PHE   E  1 99  ? 35.70944  45.71125  46.82464  1.000 32.92330  ?  99  PHE   A CG  1 
ATOM   6370  C CD1 . PHE   E  1 99  ? 34.79674  46.63182  47.35025  1.000 22.74894  ?  99  PHE   A CD1 1 
ATOM   6371  C CD2 . PHE   E  1 99  ? 36.89484  46.18669  46.26849  1.000 31.57402  ?  99  PHE   A CD2 1 
ATOM   6372  C CE1 . PHE   E  1 99  ? 35.06103  47.99469  47.33130  1.000 38.29449  ?  99  PHE   A CE1 1 
ATOM   6373  C CE2 . PHE   E  1 99  ? 37.16961  47.55023  46.23969  1.000 21.88822  ?  99  PHE   A CE2 1 
ATOM   6374  C CZ  . PHE   E  1 99  ? 36.25029  48.45898  46.78380  1.000 25.99194  ?  99  PHE   A CZ  1 
ATOM   6375  N N   . ASN   E  1 100 ? 34.38809  41.39267  47.67150  1.000 26.80583  ?  100 ASN   A N   1 
ATOM   6376  C CA  . ASN   E  1 100 ? 34.14032  40.01075  47.28214  1.000 31.05861  ?  100 ASN   A CA  1 
ATOM   6377  C C   . ASN   E  1 100 ? 32.69392  39.59694  47.55814  1.000 34.84323  ?  100 ASN   A C   1 
ATOM   6378  O O   . ASN   E  1 100 ? 32.11373  38.82733  46.77875  1.000 42.09904  ?  100 ASN   A O   1 
ATOM   6379  C CB  . ASN   E  1 100 ? 35.14366  39.09853  47.99373  1.000 30.54645  ?  100 ASN   A CB  1 
ATOM   6380  C CG  . ASN   E  1 100 ? 35.28010  37.75180  47.32174  1.000 41.99835  ?  100 ASN   A CG  1 
ATOM   6381  O OD1 . ASN   E  1 100 ? 35.73348  37.64515  46.17706  1.000 54.64498  ?  100 ASN   A OD1 1 
ATOM   6382  N ND2 . ASN   E  1 100 ? 34.89906  36.70762  48.03660  1.000 41.67836  ?  100 ASN   A ND2 1 
ATOM   6383  N N   . ASP   E  1 101 ? 32.08396  40.12141  48.63157  1.000 32.66874  ?  101 ASP   A N   1 
ATOM   6384  C CA  . ASP   E  1 101 ? 30.65175  39.90780  48.84223  1.000 26.39468  ?  101 ASP   A CA  1 
ATOM   6385  C C   . ASP   E  1 101 ? 29.82349  40.70507  47.84211  1.000 49.05557  ?  101 ASP   A C   1 
ATOM   6386  O O   . ASP   E  1 101 ? 28.92178  40.15421  47.19416  1.000 40.72982  ?  101 ASP   A O   1 
ATOM   6387  C CB  . ASP   E  1 101 ? 30.24159  40.28275  50.27083  1.000 26.46995  ?  101 ASP   A CB  1 
ATOM   6388  C CG  . ASP   E  1 101 ? 30.90428  39.41526  51.33328  1.000 109.23009 ?  101 ASP   A CG  1 
ATOM   6389  O OD1 . ASP   E  1 101 ? 31.17190  38.22296  51.06582  1.000 44.51976  ?  101 ASP   A OD1 1 
ATOM   6390  O OD2 . ASP   E  1 101 ? 31.14537  39.93507  52.45063  1.000 54.17654  -1 101 ASP   A OD2 1 
ATOM   6391  N N   . ILE   E  1 102 ? 30.11240  42.01064  47.71277  1.000 43.24939  ?  102 ILE   A N   1 
ATOM   6392  C CA  . ILE   E  1 102 ? 29.26097  42.89772  46.91848  1.000 27.70555  ?  102 ILE   A CA  1 
ATOM   6393  C C   . ILE   E  1 102 ? 29.17692  42.42517  45.47675  1.000 53.26727  ?  102 ILE   A C   1 
ATOM   6394  O O   . ILE   E  1 102 ? 28.08739  42.38806  44.89213  1.000 36.80528  ?  102 ILE   A O   1 
ATOM   6395  C CB  . ILE   E  1 102 ? 29.76191  44.34757  46.98615  1.000 30.53449  ?  102 ILE   A CB  1 
ATOM   6396  C CG1 . ILE   E  1 102 ? 29.65327  44.90688  48.39955  1.000 15.35190  ?  102 ILE   A CG1 1 
ATOM   6397  C CG2 . ILE   E  1 102 ? 28.95898  45.21112  46.04236  1.000 19.76607  ?  102 ILE   A CG2 1 
ATOM   6398  C CD1 . ILE   E  1 102 ? 29.99035  46.39873  48.47338  1.000 36.43717  ?  102 ILE   A CD1 1 
ATOM   6399  N N   . PHE   E  1 103 ? 30.32086  42.04139  44.88530  1.000 29.76374  ?  103 PHE   A N   1 
ATOM   6400  C CA  . PHE   E  1 103 ? 30.38758  41.68652  43.46949  1.000 54.27701  ?  103 PHE   A CA  1 
ATOM   6401  C C   . PHE   E  1 103 ? 29.74062  40.34042  43.15702  1.000 32.16138  ?  103 PHE   A C   1 
ATOM   6402  O O   . PHE   E  1 103 ? 29.70525  39.94224  41.98800  1.000 40.52184  ?  103 PHE   A O   1 
ATOM   6403  C CB  . PHE   E  1 103 ? 31.84263  41.67327  42.99112  1.000 21.68478  ?  103 PHE   A CB  1 
ATOM   6404  C CG  . PHE   E  1 103 ? 32.54275  43.01261  43.10100  1.000 38.94287  ?  103 PHE   A CG  1 
ATOM   6405  C CD1 . PHE   E  1 103 ? 31.81994  44.20324  43.14343  1.000 34.91838  ?  103 PHE   A CD1 1 
ATOM   6406  C CD2 . PHE   E  1 103 ? 33.93030  43.07530  43.16687  1.000 26.97346  ?  103 PHE   A CD2 1 
ATOM   6407  C CE1 . PHE   E  1 103 ? 32.47706  45.42766  43.25617  1.000 47.16608  ?  103 PHE   A CE1 1 
ATOM   6408  C CE2 . PHE   E  1 103 ? 34.59449  44.29194  43.27922  1.000 39.10573  ?  103 PHE   A CE2 1 
ATOM   6409  C CZ  . PHE   E  1 103 ? 33.86776  45.46723  43.32324  1.000 38.38871  ?  103 PHE   A CZ  1 
ATOM   6410  N N   . ARG   E  1 104 ? 29.21027  39.65398  44.16566  1.000 35.53683  ?  104 ARG   A N   1 
ATOM   6411  C CA  . ARG   E  1 104 ? 28.59704  38.35377  43.99768  1.000 18.05956  ?  104 ARG   A CA  1 
ATOM   6412  C C   . ARG   E  1 104 ? 27.07585  38.43114  44.10622  1.000 38.04784  ?  104 ARG   A C   1 
ATOM   6413  O O   . ARG   E  1 104 ? 26.38671  37.41438  44.00350  1.000 51.90295  ?  104 ARG   A O   1 
ATOM   6414  C CB  . ARG   E  1 104 ? 29.15163  37.37776  45.04775  1.000 28.00565  ?  104 ARG   A CB  1 
ATOM   6415  C CG  . ARG   E  1 104 ? 30.59711  36.99879  44.85572  1.000 18.86176  ?  104 ARG   A CG  1 
ATOM   6416  C CD  . ARG   E  1 104 ? 31.09842  36.02972  45.94489  1.000 60.28985  ?  104 ARG   A CD  1 
ATOM   6417  N NE  . ARG   E  1 104 ? 32.54799  35.86455  45.87894  1.000 61.68856  ?  104 ARG   A NE  1 
ATOM   6418  C CZ  . ARG   E  1 104 ? 33.16665  34.77407  45.43483  1.000 91.49090  ?  104 ARG   A CZ  1 
ATOM   6419  N NH1 . ARG   E  1 104 ? 32.49083  33.67902  45.12570  1.000 106.00282 ?  104 ARG   A NH1 1 
ATOM   6420  N NH2 . ARG   E  1 104 ? 34.49616  34.78310  45.29506  1.000 82.64975  ?  104 ARG   A NH2 1 
ATOM   6421  N N   . LYS   E  1 105 ? 26.53554  39.61704  44.30025  1.000 31.86145  ?  105 LYS   A N   1 
ATOM   6422  C CA  . LYS   E  1 105 ? 25.09753  39.76609  44.42947  1.000 52.59879  ?  105 LYS   A CA  1 
ATOM   6423  C C   . LYS   E  1 105 ? 24.67365  41.10537  43.84718  1.000 35.12955  ?  105 LYS   A C   1 
ATOM   6424  O O   . LYS   E  1 105 ? 25.48711  42.01083  43.66901  1.000 39.75683  ?  105 LYS   A O   1 
ATOM   6425  C CB  . LYS   E  1 105 ? 24.65826  39.59529  45.89076  1.000 42.81602  ?  105 LYS   A CB  1 
ATOM   6426  C CG  . LYS   E  1 105 ? 25.31462  40.54442  46.84097  1.000 32.76085  ?  105 LYS   A CG  1 
ATOM   6427  C CD  . LYS   E  1 105 ? 24.97196  40.21795  48.29446  1.000 33.22580  ?  105 LYS   A CD  1 
ATOM   6428  C CE  . LYS   E  1 105 ? 25.63084  38.93591  48.74239  1.000 63.43298  ?  105 LYS   A CE  1 
ATOM   6429  N NZ  . LYS   E  1 105 ? 25.83609  38.93399  50.21541  1.000 76.28588  ?  105 LYS   A NZ  1 
ATOM   6430  N N   . ALA   E  1 106 ? 23.39493  41.19828  43.52425  1.000 51.61912  ?  106 ALA   A N   1 
ATOM   6431  C CA  . ALA   E  1 106 ? 22.82713  42.39153  42.92561  1.000 44.88074  ?  106 ALA   A CA  1 
ATOM   6432  C C   . ALA   E  1 106 ? 22.46539  43.41296  43.99887  1.000 28.27138  ?  106 ALA   A C   1 
ATOM   6433  O O   . ALA   E  1 106 ? 22.22036  43.04892  45.15068  1.000 47.62097  ?  106 ALA   A O   1 
ATOM   6434  C CB  . ALA   E  1 106 ? 21.58854  42.03802  42.10239  1.000 31.18790  ?  106 ALA   A CB  1 
ATOM   6435  N N   . PRO   E  1 107 ? 22.44136  44.70189  43.65417  1.000 51.84035  ?  107 PRO   A N   1 
ATOM   6436  C CA  . PRO   E  1 107 ? 22.06654  45.71607  44.64397  1.000 34.17271  ?  107 PRO   A CA  1 
ATOM   6437  C C   . PRO   E  1 107 ? 20.59525  45.59527  45.02010  1.000 44.05553  ?  107 PRO   A C   1 
ATOM   6438  O O   . PRO   E  1 107 ? 19.78260  45.00589  44.30217  1.000 39.31893  ?  107 PRO   A O   1 
ATOM   6439  C CB  . PRO   E  1 107 ? 22.34106  47.04602  43.92830  1.000 32.22851  ?  107 PRO   A CB  1 
ATOM   6440  C CG  . PRO   E  1 107 ? 22.96758  46.71350  42.64883  1.000 28.83965  ?  107 PRO   A CG  1 
ATOM   6441  C CD  . PRO   E  1 107 ? 22.68134  45.29261  42.32666  1.000 22.66835  ?  107 PRO   A CD  1 
ATOM   6442  N N   . VAL   E  1 108 ? 20.25185  46.18748  46.16002  1.000 36.64958  ?  108 VAL   A N   1 
ATOM   6443  C CA  . VAL   E  1 108 ? 18.87710  46.21539  46.62814  1.000 32.51546  ?  108 VAL   A CA  1 
ATOM   6444  C C   . VAL   E  1 108 ? 18.45581  47.66906  46.85341  1.000 43.74725  ?  108 VAL   A C   1 
ATOM   6445  O O   . VAL   E  1 108 ? 19.27293  48.59261  46.85354  1.000 44.36263  ?  108 VAL   A O   1 
ATOM   6446  C CB  . VAL   E  1 108 ? 18.68064  45.36427  47.90004  1.000 42.75111  ?  108 VAL   A CB  1 
ATOM   6447  C CG1 . VAL   E  1 108 ? 19.11871  43.90936  47.64136  1.000 23.77357  ?  108 VAL   A CG1 1 
ATOM   6448  C CG2 . VAL   E  1 108 ? 19.45285  45.94399  49.04910  1.000 23.51977  ?  108 VAL   A CG2 1 
ATOM   6449  N N   . TYR   E  1 109 ? 17.15143  47.86213  47.01856  1.000 37.62236  ?  109 TYR   A N   1 
ATOM   6450  C CA  . TYR   E  1 109 ? 16.60368  49.19763  47.22404  1.000 67.07567  ?  109 TYR   A CA  1 
ATOM   6451  C C   . TYR   E  1 109 ? 16.73367  49.60796  48.68634  1.000 37.33895  ?  109 TYR   A C   1 
ATOM   6452  O O   . TYR   E  1 109 ? 16.56080  48.79048  49.59457  1.000 51.26362  ?  109 TYR   A O   1 
ATOM   6453  C CB  . TYR   E  1 109 ? 15.13396  49.25217  46.79266  1.000 31.49320  ?  109 TYR   A CB  1 
ATOM   6454  C CG  . TYR   E  1 109 ? 14.51112  50.61081  47.01449  1.000 64.29816  ?  109 TYR   A CG  1 
ATOM   6455  C CD1 . TYR   E  1 109 ? 14.59624  51.59818  46.05190  1.000 32.78924  ?  109 TYR   A CD1 1 
ATOM   6456  C CD2 . TYR   E  1 109 ? 13.85910  50.91341  48.20205  1.000 36.76814  ?  109 TYR   A CD2 1 
ATOM   6457  C CE1 . TYR   E  1 109 ? 14.03918  52.84631  46.26788  1.000 74.46116  ?  109 TYR   A CE1 1 
ATOM   6458  C CE2 . TYR   E  1 109 ? 13.30282  52.15444  48.42640  1.000 57.90954  ?  109 TYR   A CE2 1 
ATOM   6459  C CZ  . TYR   E  1 109 ? 13.39312  53.11889  47.46007  1.000 34.12627  ?  109 TYR   A CZ  1 
ATOM   6460  O OH  . TYR   E  1 109 ? 12.84510  54.36459  47.66854  1.000 60.39636  ?  109 TYR   A OH  1 
ATOM   6461  N N   . GLY   E  1 110 ? 17.05393  50.87585  48.91533  1.000 49.92123  ?  110 GLY   A N   1 
ATOM   6462  C CA  . GLY   E  1 110 ? 17.13869  51.32936  50.28593  1.000 14.92049  ?  110 GLY   A CA  1 
ATOM   6463  C C   . GLY   E  1 110 ? 18.21554  52.34160  50.61636  1.000 48.61732  ?  110 GLY   A C   1 
ATOM   6464  O O   . GLY   E  1 110 ? 17.95161  53.27049  51.38254  1.000 42.61937  ?  110 GLY   A O   1 
ATOM   6465  N N   . ASP   E  1 111 ? 19.42534  52.18574  50.07691  1.000 51.38294  ?  111 ASP   A N   1 
ATOM   6466  C CA  . ASP   E  1 111 ? 20.50995  53.07234  50.47187  1.000 41.96165  ?  111 ASP   A CA  1 
ATOM   6467  C C   . ASP   E  1 111 ? 20.51291  54.34157  49.62691  1.000 26.00822  ?  111 ASP   A C   1 
ATOM   6468  O O   . ASP   E  1 111 ? 19.88623  54.41195  48.56600  1.000 39.34040  ?  111 ASP   A O   1 
ATOM   6469  C CB  . ASP   E  1 111 ? 21.85158  52.35343  50.37421  1.000 54.69338  ?  111 ASP   A CB  1 
ATOM   6470  C CG  . ASP   E  1 111 ? 22.07565  51.40251  51.52259  1.000 53.40438  ?  111 ASP   A CG  1 
ATOM   6471  O OD1 . ASP   E  1 111 ? 22.21539  51.88312  52.66734  1.000 69.22180  ?  111 ASP   A OD1 1 
ATOM   6472  O OD2 . ASP   E  1 111 ? 22.08652  50.17540  51.28099  1.000 88.09007  -1 111 ASP   A OD2 1 
ATOM   6473  N N   . LEU   E  1 112 ? 21.19745  55.37770  50.17889  1.000 33.30255  ?  112 LEU   A N   1 
ATOM   6474  C CA  . LEU   E  1 112 ? 21.40859  56.64568  49.47544  1.000 16.40676  ?  112 LEU   A CA  1 
ATOM   6475  C C   . LEU   E  1 112 ? 21.98459  56.41839  48.08280  1.000 52.96969  ?  112 LEU   A C   1 
ATOM   6476  O O   . LEU   E  1 112 ? 21.49841  56.98072  47.08779  1.000 27.75075  ?  112 LEU   A O   1 
ATOM   6477  C CB  . LEU   E  1 112 ? 22.32962  57.58488  50.27888  1.000 72.24151  ?  112 LEU   A CB  1 
ATOM   6478  C CG  . LEU   E  1 112 ? 22.63801  58.98698  49.65164  1.000 76.37451  ?  112 LEU   A CG  1 
ATOM   6479  C CD1 . LEU   E  1 112 ? 23.86834  58.98238  48.76081  1.000 92.27039  ?  112 LEU   A CD1 1 
ATOM   6480  C CD2 . LEU   E  1 112 ? 21.48242  59.65351  48.87192  1.000 96.38104  ?  112 LEU   A CD2 1 
ATOM   6481  N N   . GLY   E  1 113 ? 23.00700  55.56414  47.99304  1.000 32.15588  ?  113 GLY   A N   1 
ATOM   6482  C CA  . GLY   E  1 113 ? 23.68639  55.29285  46.75163  1.000 30.63469  ?  113 GLY   A CA  1 
ATOM   6483  C C   . GLY   E  1 113 ? 23.97366  53.81354  46.58770  1.000 34.22451  ?  113 GLY   A C   1 
ATOM   6484  O O   . GLY   E  1 113 ? 23.63245  52.98537  47.44490  1.000 32.66323  ?  113 GLY   A O   1 
ATOM   6485  N N   . PRO   E  1 114 ? 24.62113  53.45369  45.48205  1.000 28.51040  ?  114 PRO   A N   1 
ATOM   6486  C CA  . PRO   E  1 114 ? 24.92617  52.02982  45.21579  1.000 21.82855  ?  114 PRO   A CA  1 
ATOM   6487  C C   . PRO   E  1 114 ? 25.94685  51.49141  46.20767  1.000 24.78872  ?  114 PRO   A C   1 
ATOM   6488  O O   . PRO   E  1 114 ? 26.58054  52.25994  46.95704  1.000 29.25731  ?  114 PRO   A O   1 
ATOM   6489  C CB  . PRO   E  1 114 ? 25.46183  52.04700  43.77356  1.000 26.83969  ?  114 PRO   A CB  1 
ATOM   6490  C CG  . PRO   E  1 114 ? 25.97295  53.46491  43.57601  1.000 23.79527  ?  114 PRO   A CG  1 
ATOM   6491  C CD  . PRO   E  1 114 ? 25.13458  54.35995  44.44070  1.000 24.88065  ?  114 PRO   A CD  1 
ATOM   6492  N N   . PRO   E  1 115 ? 26.10416  50.16427  46.28238  1.000 29.63759  ?  115 PRO   A N   1 
ATOM   6493  C CA  . PRO   E  1 115 ? 26.79663  49.58055  47.45449  1.000 40.62264  ?  115 PRO   A CA  1 
ATOM   6494  C C   . PRO   E  1 115 ? 28.28634  49.85974  47.52866  1.000 32.72144  ?  115 PRO   A C   1 
ATOM   6495  O O   . PRO   E  1 115 ? 28.80730  50.01120  48.64301  1.000 37.81449  ?  115 PRO   A O   1 
ATOM   6496  C CB  . PRO   E  1 115 ? 26.51834  48.07415  47.32707  1.000 22.39531  ?  115 PRO   A CB  1 
ATOM   6497  C CG  . PRO   E  1 115 ? 25.89630  47.86520  45.97309  1.000 24.95342  ?  115 PRO   A CG  1 
ATOM   6498  C CD  . PRO   E  1 115 ? 25.29606  49.16739  45.55398  1.000 34.92127  ?  115 PRO   A CD  1 
ATOM   6499  N N   . VAL   E  1 116 ? 28.99719  49.90748  46.39300  1.000 40.32986  ?  116 VAL   A N   1 
ATOM   6500  C CA  . VAL   E  1 116 ? 30.41905  50.25232  46.44639  1.000 30.59091  ?  116 VAL   A CA  1 
ATOM   6501  C C   . VAL   E  1 116 ? 30.60398  51.69576  46.90226  1.000 33.07192  ?  116 VAL   A C   1 
ATOM   6502  O O   . VAL   E  1 116 ? 31.46328  51.99002  47.74571  1.000 36.64579  ?  116 VAL   A O   1 
ATOM   6503  C CB  . VAL   E  1 116 ? 31.12115  50.00358  45.10067  1.000 37.76123  ?  116 VAL   A CB  1 
ATOM   6504  C CG1 . VAL   E  1 116 ? 32.58770  50.41007  45.22644  1.000 29.83558  ?  116 VAL   A CG1 1 
ATOM   6505  C CG2 . VAL   E  1 116 ? 31.01012  48.54141  44.69241  1.000 21.79511  ?  116 VAL   A CG2 1 
ATOM   6506  N N   . TYR   E  1 117 ? 29.80553  52.61951  46.36461  1.000 22.56384  ?  117 TYR   A N   1 
ATOM   6507  C CA  . TYR   E  1 117 ? 29.86699  53.99095  46.85799  1.000 36.09658  ?  117 TYR   A CA  1 
ATOM   6508  C C   . TYR   E  1 117 ? 29.68328  54.04241  48.37817  1.000 30.11728  ?  117 TYR   A C   1 
ATOM   6509  O O   . TYR   E  1 117 ? 30.44326  54.71909  49.08097  1.000 35.12891  ?  117 TYR   A O   1 
ATOM   6510  C CB  . TYR   E  1 117 ? 28.82195  54.88291  46.16917  1.000 21.68171  ?  117 TYR   A CB  1 
ATOM   6511  C CG  . TYR   E  1 117 ? 28.66492  56.15630  46.96710  1.000 28.95201  ?  117 TYR   A CG  1 
ATOM   6512  C CD1 . TYR   E  1 117 ? 29.60749  57.17987  46.85806  1.000 25.18081  ?  117 TYR   A CD1 1 
ATOM   6513  C CD2 . TYR   E  1 117 ? 27.63520  56.30566  47.89420  1.000 41.89072  ?  117 TYR   A CD2 1 
ATOM   6514  C CE1 . TYR   E  1 117 ? 29.50934  58.33811  47.61849  1.000 25.61268  ?  117 TYR   A CE1 1 
ATOM   6515  C CE2 . TYR   E  1 117 ? 27.53528  57.44995  48.65647  1.000 19.30565  ?  117 TYR   A CE2 1 
ATOM   6516  C CZ  . TYR   E  1 117 ? 28.47618  58.46302  48.51404  1.000 35.73345  ?  117 TYR   A CZ  1 
ATOM   6517  O OH  . TYR   E  1 117 ? 28.38014  59.60817  49.26177  1.000 25.47700  ?  117 TYR   A OH  1 
ATOM   6518  N N   . MET   E  1 118 ? 28.67399  53.33061  48.90137  1.000 36.26705  ?  118 MET   A N   1 
ATOM   6519  C CA  . MET   E  1 118 ? 28.36225  53.40815  50.33014  1.000 26.09924  ?  118 MET   A CA  1 
ATOM   6520  C C   . MET   E  1 118 ? 29.57779  53.05442  51.19362  1.000 41.71966  ?  118 MET   A C   1 
ATOM   6521  O O   . MET   E  1 118 ? 29.91986  53.79050  52.12683  1.000 33.88719  ?  118 MET   A O   1 
ATOM   6522  C CB  . MET   E  1 118 ? 27.17565  52.49949  50.67800  1.000 29.16807  ?  118 MET   A CB  1 
ATOM   6523  C CG  . MET   E  1 118 ? 25.78760  52.92369  50.17500  1.000 18.83892  ?  118 MET   A CG  1 
ATOM   6524  S SD  . MET   E  1 118 ? 25.19208  54.54714  50.69880  1.000 37.05452  ?  118 MET   A SD  1 
ATOM   6525  C CE  . MET   E  1 118 ? 25.20949  54.34004  52.47863  1.000 41.62644  ?  118 MET   A CE  1 
ATOM   6526  N N   . ILE   E  1 119 ? 30.26847  51.94620  50.88984  1.000 24.92162  ?  119 ILE   A N   1 
ATOM   6527  C CA  . ILE   E  1 119 ? 31.45336  51.62223  51.69035  1.000 36.40087  ?  119 ILE   A CA  1 
ATOM   6528  C C   . ILE   E  1 119 ? 32.69407  52.42319  51.30859  1.000 36.83598  ?  119 ILE   A C   1 
ATOM   6529  O O   . ILE   E  1 119 ? 33.68084  52.39077  52.05993  1.000 41.49802  ?  119 ILE   A O   1 
ATOM   6530  C CB  . ILE   E  1 119 ? 31.79994  50.12015  51.64605  1.000 28.37309  ?  119 ILE   A CB  1 
ATOM   6531  C CG1 . ILE   E  1 119 ? 32.43271  49.72526  50.31873  1.000 30.66252  ?  119 ILE   A CG1 1 
ATOM   6532  C CG2 . ILE   E  1 119 ? 30.55932  49.28793  51.87336  1.000 35.88234  ?  119 ILE   A CG2 1 
ATOM   6533  C CD1 . ILE   E  1 119 ? 32.80971  48.26170  50.28996  1.000 35.54076  ?  119 ILE   A CD1 1 
ATOM   6534  N N   . MET   E  1 120 ? 32.67600  53.16615  50.18905  1.000 29.71677  ?  120 MET   A N   1 
ATOM   6535  C CA  . MET   E  1 120 ? 33.83883  53.95530  49.76908  1.000 27.71543  ?  120 MET   A CA  1 
ATOM   6536  C C   . MET   E  1 120 ? 33.78296  55.41542  50.20213  1.000 33.54636  ?  120 MET   A C   1 
ATOM   6537  O O   . MET   E  1 120 ? 34.82118  56.08526  50.19360  1.000 33.15130  ?  120 MET   A O   1 
ATOM   6538  C CB  . MET   E  1 120 ? 33.99602  53.93227  48.23762  1.000 15.34050  ?  120 MET   A CB  1 
ATOM   6539  C CG  . MET   E  1 120 ? 34.43516  52.60115  47.66984  1.000 23.23161  ?  120 MET   A CG  1 
ATOM   6540  S SD  . MET   E  1 120 ? 36.09993  52.12584  48.11040  1.000 39.35059  ?  120 MET   A SD  1 
ATOM   6541  C CE  . MET   E  1 120 ? 37.04301  53.10918  46.94249  1.000 23.99082  ?  120 MET   A CE  1 
ATOM   6542  N N   . ALA   E  1 121 ? 32.60106  55.92226  50.56547  1.000 28.75904  ?  121 ALA   A N   1 
ATOM   6543  C CA  . ALA   E  1 121 ? 32.41885  57.36708  50.69911  1.000 34.54391  ?  121 ALA   A CA  1 
ATOM   6544  C C   . ALA   E  1 121 ? 33.35760  57.96080  51.74104  1.000 34.91952  ?  121 ALA   A C   1 
ATOM   6545  O O   . ALA   E  1 121 ? 33.89557  59.06026  51.54660  1.000 41.89304  ?  121 ALA   A O   1 
ATOM   6546  C CB  . ALA   E  1 121 ? 30.95896  57.68589  51.04519  1.000 26.45979  ?  121 ALA   A CB  1 
ATOM   6547  N N   . LYS   E  1 122 ? 33.56217  57.25450  52.86176  1.000 32.61392  ?  122 LYS   A N   1 
ATOM   6548  C CA  . LYS   E  1 122 ? 34.45569  57.77501  53.89446  1.000 25.15064  ?  122 LYS   A CA  1 
ATOM   6549  C C   . LYS   E  1 122 ? 35.89617  57.85350  53.37349  1.000 39.37589  ?  122 LYS   A C   1 
ATOM   6550  O O   . LYS   E  1 122 ? 36.59791  58.83697  53.61871  1.000 33.20800  ?  122 LYS   A O   1 
ATOM   6551  C CB  . LYS   E  1 122 ? 34.36052  56.91474  55.17101  1.000 24.56533  ?  122 LYS   A CB  1 
ATOM   6552  N N   . LEU   E  1 123 ? 36.33436  56.85205  52.60024  1.000 36.57037  ?  123 LEU   A N   1 
ATOM   6553  C CA  . LEU   E  1 123 ? 37.67597  56.86511  52.00417  1.000 36.07106  ?  123 LEU   A CA  1 
ATOM   6554  C C   . LEU   E  1 123 ? 37.83317  57.98781  50.98257  1.000 61.06063  ?  123 LEU   A C   1 
ATOM   6555  O O   . LEU   E  1 123 ? 38.84691  58.70875  50.98050  1.000 28.13993  ?  123 LEU   A O   1 
ATOM   6556  C CB  . LEU   E  1 123 ? 37.97192  55.51280  51.35065  1.000 27.15799  ?  123 LEU   A CB  1 
ATOM   6557  C CG  . LEU   E  1 123 ? 37.61812  54.33401  52.24856  1.000 36.10041  ?  123 LEU   A CG  1 
ATOM   6558  C CD1 . LEU   E  1 123 ? 37.94316  53.00224  51.58722  1.000 30.25497  ?  123 LEU   A CD1 1 
ATOM   6559  C CD2 . LEU   E  1 123 ? 38.36113  54.48022  53.55313  1.000 30.08444  ?  123 LEU   A CD2 1 
ATOM   6560  N N   . MET   E  1 124 ? 36.85604  58.12299  50.07482  1.000 27.42253  ?  124 MET   A N   1 
ATOM   6561  C CA  . MET   E  1 124 ? 36.91426  59.18892  49.07970  1.000 38.81383  ?  124 MET   A CA  1 
ATOM   6562  C C   . MET   E  1 124 ? 37.06235  60.55801  49.71851  1.000 31.38032  ?  124 MET   A C   1 
ATOM   6563  O O   . MET   E  1 124 ? 37.57674  61.48554  49.08384  1.000 30.52997  ?  124 MET   A O   1 
ATOM   6564  C CB  . MET   E  1 124 ? 35.65926  59.18609  48.21714  1.000 16.39659  ?  124 MET   A CB  1 
ATOM   6565  C CG  . MET   E  1 124 ? 35.43214  57.91385  47.46336  1.000 36.64182  ?  124 MET   A CG  1 
ATOM   6566  S SD  . MET   E  1 124 ? 33.67880  57.73711  47.06991  1.000 38.52747  ?  124 MET   A SD  1 
ATOM   6567  C CE  . MET   E  1 124 ? 33.34783  59.17940  46.07963  1.000 14.19984  ?  124 MET   A CE  1 
ATOM   6568  N N   . ASN   E  1 125 ? 36.60833  60.70791  50.96190  1.000 34.25275  ?  125 ASN   A N   1 
ATOM   6569  C CA  . ASN   E  1 125 ? 36.58666  61.99353  51.63601  1.000 28.13487  ?  125 ASN   A CA  1 
ATOM   6570  C C   . ASN   E  1 125 ? 37.89328  62.30475  52.37905  1.000 33.75856  ?  125 ASN   A C   1 
ATOM   6571  O O   . ASN   E  1 125 ? 37.90107  63.13712  53.29111  1.000 37.74695  ?  125 ASN   A O   1 
ATOM   6572  C CB  . ASN   E  1 125 ? 35.40844  62.04990  52.60578  1.000 26.62088  ?  125 ASN   A CB  1 
ATOM   6573  C CG  . ASN   E  1 125 ? 34.99216  63.46985  52.92335  1.000 24.75180  ?  125 ASN   A CG  1 
ATOM   6574  O OD1 . ASN   E  1 125 ? 35.34712  64.41766  52.21016  1.000 30.91513  ?  125 ASN   A OD1 1 
ATOM   6575  N ND2 . ASN   E  1 125 ? 34.22461  63.62668  53.99071  1.000 42.06494  ?  125 ASN   A ND2 1 
ATOM   6576  N N   . THR   E  1 126 ? 38.99510  61.67690  52.00326  1.000 32.22666  ?  126 THR   A N   1 
ATOM   6577  C CA  . THR   E  1 126 ? 40.29437  61.96246  52.58771  1.000 41.31658  ?  126 THR   A CA  1 
ATOM   6578  C C   . THR   E  1 126 ? 41.25692  62.39420  51.49336  1.000 20.18697  ?  126 THR   A C   1 
ATOM   6579  O O   . THR   E  1 126 ? 41.03444  62.13728  50.30658  1.000 39.10963  ?  126 THR   A O   1 
ATOM   6580  C CB  . THR   E  1 126 ? 40.86609  60.73553  53.30960  1.000 26.06669  ?  126 THR   A CB  1 
ATOM   6581  O OG1 . THR   E  1 126 ? 41.28997  59.75784  52.34026  1.000 25.48903  ?  126 THR   A OG1 1 
ATOM   6582  C CG2 . THR   E  1 126 ? 39.81578  60.11953  54.23069  1.000 11.08687  ?  126 THR   A CG2 1 
ATOM   6583  N N   . ARG   E  1 127 ? 42.36962  63.06135  51.86531  1.000 49.63755  ?  127 ARG   A N   1 
ATOM   6584  C CA  . ARG   E  1 127 ? 43.39203  63.34594  50.84423  1.000 23.64919  ?  127 ARG   A CA  1 
ATOM   6585  C C   . ARG   E  1 127 ? 44.06084  62.07221  50.37266  1.000 31.97759  ?  127 ARG   A C   1 
ATOM   6586  O O   . ARG   E  1 127 ? 44.31707  61.90564  49.16747  1.000 16.89477  ?  127 ARG   A O   1 
ATOM   6587  C CB  . ARG   E  1 127 ? 44.47498  64.28746  51.33872  1.000 34.80708  ?  127 ARG   A CB  1 
ATOM   6588  C CG  . ARG   E  1 127 ? 44.17639  65.72219  51.09803  1.000 80.99427  ?  127 ARG   A CG  1 
ATOM   6589  C CD  . ARG   E  1 127 ? 45.38366  66.59515  51.29874  1.000 59.47362  ?  127 ARG   A CD  1 
ATOM   6590  N NE  . ARG   E  1 127 ? 44.91726  67.96084  51.48659  1.000 121.96349 ?  127 ARG   A NE  1 
ATOM   6591  C CZ  . ARG   E  1 127 ? 45.68894  69.03814  51.49800  1.000 106.40622 ?  127 ARG   A CZ  1 
ATOM   6592  N NH1 . ARG   E  1 127 ? 47.00675  68.94681  51.35635  1.000 83.13608  ?  127 ARG   A NH1 1 
ATOM   6593  N NH2 . ARG   E  1 127 ? 45.12124  70.23944  51.63241  1.000 101.42516 ?  127 ARG   A NH2 1 
ATOM   6594  N N   . ALA   E  1 128 ? 44.33478  61.14268  51.30739  1.000 19.69181  ?  128 ALA   A N   1 
ATOM   6595  C CA  . ALA   E  1 128 ? 44.95845  59.89256  50.88517  1.000 32.66306  ?  128 ALA   A CA  1 
ATOM   6596  C C   . ALA   E  1 128 ? 44.08452  59.16314  49.86751  1.000 23.59434  ?  128 ALA   A C   1 
ATOM   6597  O O   . ALA   E  1 128 ? 44.59238  58.64948  48.85998  1.000 34.43410  ?  128 ALA   A O   1 
ATOM   6598  C CB  . ALA   E  1 128 ? 45.24469  59.00351  52.10725  1.000 21.43129  ?  128 ALA   A CB  1 
ATOM   6599  N N   . GLY   E  1 129 ? 42.76464  59.12768  50.10201  1.000 48.32431  ?  129 GLY   A N   1 
ATOM   6600  C CA  . GLY   E  1 129 ? 41.86803  58.44047  49.17605  1.000 16.33353  ?  129 GLY   A CA  1 
ATOM   6601  C C   . GLY   E  1 129 ? 41.81172  59.11071  47.81115  1.000 40.83041  ?  129 GLY   A C   1 
ATOM   6602  O O   . GLY   E  1 129 ? 41.90664  58.44952  46.76972  1.000 30.67573  ?  129 GLY   A O   1 
ATOM   6603  N N   . PHE   E  1 130 ? 41.67429  60.43938  47.79796  1.000 25.66882  ?  130 PHE   A N   1 
ATOM   6604  C CA  . PHE   E  1 130 ? 41.68852  61.16166  46.53234  1.000 25.75521  ?  130 PHE   A CA  1 
ATOM   6605  C C   . PHE   E  1 130 ? 42.97806  60.89864  45.74796  1.000 46.68677  ?  130 PHE   A C   1 
ATOM   6606  O O   . PHE   E  1 130 ? 42.92482  60.66919  44.53504  1.000 37.84152  ?  130 PHE   A O   1 
ATOM   6607  C CB  . PHE   E  1 130 ? 41.48999  62.65304  46.79442  1.000 14.34744  ?  130 PHE   A CB  1 
ATOM   6608  C CG  . PHE   E  1 130 ? 41.55805  63.49852  45.56200  1.000 27.79212  ?  130 PHE   A CG  1 
ATOM   6609  C CD1 . PHE   E  1 130 ? 42.78818  63.93156  45.05840  1.000 27.78811  ?  130 PHE   A CD1 1 
ATOM   6610  C CD2 . PHE   E  1 130 ? 40.40018  63.87330  44.90555  1.000 21.38934  ?  130 PHE   A CD2 1 
ATOM   6611  C CE1 . PHE   E  1 130 ? 42.86775  64.71647  43.91717  1.000 26.62107  ?  130 PHE   A CE1 1 
ATOM   6612  C CE2 . PHE   E  1 130 ? 40.46869  64.65941  43.75536  1.000 35.21421  ?  130 PHE   A CE2 1 
ATOM   6613  C CZ  . PHE   E  1 130 ? 41.72388  65.08546  43.26463  1.000 21.66276  ?  130 PHE   A CZ  1 
ATOM   6614  N N   . SER   E  1 131 ? 44.14539  60.93782  46.41305  1.000 21.56074  ?  131 SER   A N   1 
ATOM   6615  C CA  . SER   E  1 131 ? 45.39653  60.60190  45.72522  1.000 39.23411  ?  131 SER   A CA  1 
ATOM   6616  C C   . SER   E  1 131 ? 45.32048  59.22795  45.07039  1.000 26.89316  ?  131 SER   A C   1 
ATOM   6617  O O   . SER   E  1 131 ? 45.64909  59.07062  43.88491  1.000 37.73975  ?  131 SER   A O   1 
ATOM   6618  C CB  . SER   E  1 131 ? 46.58183  60.64232  46.68899  1.000 10.45918  ?  131 SER   A CB  1 
ATOM   6619  O OG  . SER   E  1 131 ? 47.19305  61.90309  46.64611  1.000 82.32618  ?  131 SER   A OG  1 
ATOM   6620  N N   . ALA   E  1 132 ? 44.92733  58.21018  45.84453  1.000 28.66145  ?  132 ALA   A N   1 
ATOM   6621  C CA  . ALA   E  1 132 ? 44.88394  56.85558  45.30644  1.000 22.92368  ?  132 ALA   A CA  1 
ATOM   6622  C C   . ALA   E  1 132 ? 43.94629  56.78090  44.11299  1.000 37.21391  ?  132 ALA   A C   1 
ATOM   6623  O O   . ALA   E  1 132 ? 44.30178  56.23608  43.05658  1.000 30.97804  ?  132 ALA   A O   1 
ATOM   6624  C CB  . ALA   E  1 132 ? 44.44825  55.87270  46.38814  1.000 23.64588  ?  132 ALA   A CB  1 
ATOM   6625  N N   . PHE   E  1 133 ? 42.75357  57.36585  44.25882  1.000 19.92473  ?  133 PHE   A N   1 
ATOM   6626  C CA  . PHE   E  1 133 ? 41.67994  57.26509  43.27780  1.000 30.49943  ?  133 PHE   A CA  1 
ATOM   6627  C C   . PHE   E  1 133 ? 41.90958  58.14592  42.05256  1.000 37.44810  ?  133 PHE   A C   1 
ATOM   6628  O O   . PHE   E  1 133 ? 41.10968  58.09735  41.10822  1.000 26.96067  ?  133 PHE   A O   1 
ATOM   6629  C CB  . PHE   E  1 133 ? 40.34159  57.60071  43.94377  1.000 22.71824  ?  133 PHE   A CB  1 
ATOM   6630  C CG  . PHE   E  1 133 ? 40.07308  56.78482  45.18627  1.000 33.66829  ?  133 PHE   A CG  1 
ATOM   6631  C CD1 . PHE   E  1 133 ? 40.68485  55.53371  45.36495  1.000 29.22049  ?  133 PHE   A CD1 1 
ATOM   6632  C CD2 . PHE   E  1 133 ? 39.22966  57.26732  46.18313  1.000 23.93298  ?  133 PHE   A CD2 1 
ATOM   6633  C CE1 . PHE   E  1 133 ? 40.45600  54.78055  46.51324  1.000 21.08488  ?  133 PHE   A CE1 1 
ATOM   6634  C CE2 . PHE   E  1 133 ? 38.99273  56.53062  47.33588  1.000 23.35599  ?  133 PHE   A CE2 1 
ATOM   6635  C CZ  . PHE   E  1 133 ? 39.60640  55.27932  47.50400  1.000 17.14851  ?  133 PHE   A CZ  1 
ATOM   6636  N N   . THR   E  1 134 ? 42.98943  58.92865  42.02299  1.000 22.45404  ?  134 THR   A N   1 
ATOM   6637  C CA  . THR   E  1 134 ? 43.34293  59.69228  40.83494  1.000 27.11280  ?  134 THR   A CA  1 
ATOM   6638  C C   . THR   E  1 134 ? 44.61342  59.16036  40.16625  1.000 24.93950  ?  134 THR   A C   1 
ATOM   6639  O O   . THR   E  1 134 ? 45.29437  59.89144  39.44264  1.000 32.89107  ?  134 THR   A O   1 
ATOM   6640  C CB  . THR   E  1 134 ? 43.46828  61.18432  41.15065  1.000 27.12957  ?  134 THR   A CB  1 
ATOM   6641  O OG1 . THR   E  1 134 ? 44.23511  61.38420  42.34658  1.000 32.81785  ?  134 THR   A OG1 1 
ATOM   6642  C CG2 . THR   E  1 134 ? 42.08217  61.80405  41.31949  1.000 20.12474  ?  134 THR   A CG2 1 
ATOM   6643  N N   . ARG   E  1 135 ? 44.91707  57.87560  40.36786  1.000 33.81409  ?  135 ARG   A N   1 
ATOM   6644  C CA  . ARG   E  1 135 ? 45.99121  57.18632  39.65466  1.000 33.99251  ?  135 ARG   A CA  1 
ATOM   6645  C C   . ARG   E  1 135 ? 45.37042  56.31371  38.57080  1.000 47.61731  ?  135 ARG   A C   1 
ATOM   6646  O O   . ARG   E  1 135 ? 44.56713  55.41960  38.87298  1.000 34.22635  ?  135 ARG   A O   1 
ATOM   6647  C CB  . ARG   E  1 135 ? 46.83438  56.32276  40.59546  1.000 24.81061  ?  135 ARG   A CB  1 
ATOM   6648  C CG  . ARG   E  1 135 ? 47.51507  57.07831  41.73520  1.000 29.01592  ?  135 ARG   A CG  1 
ATOM   6649  C CD  . ARG   E  1 135 ? 47.96124  56.07931  42.77006  1.000 31.75185  ?  135 ARG   A CD  1 
ATOM   6650  N NE  . ARG   E  1 135 ? 48.68098  56.69274  43.87233  1.000 51.04667  ?  135 ARG   A NE  1 
ATOM   6651  C CZ  . ARG   E  1 135 ? 49.90856  57.18178  43.77597  1.000 54.86276  ?  135 ARG   A CZ  1 
ATOM   6652  N NH1 . ARG   E  1 135 ? 50.58084  57.14160  42.63636  1.000 46.03729  ?  135 ARG   A NH1 1 
ATOM   6653  N NH2 . ARG   E  1 135 ? 50.46883  57.74252  44.84588  1.000 43.96718  ?  135 ARG   A NH2 1 
ATOM   6654  N N   . GLN   E  1 136 ? 45.73927  56.57487  37.31058  1.000 26.61674  ?  136 GLN   A N   1 
ATOM   6655  C CA  . GLN   E  1 136 ? 45.21413  55.77240  36.20926  1.000 28.63522  ?  136 GLN   A CA  1 
ATOM   6656  C C   . GLN   E  1 136 ? 45.49232  54.29283  36.41593  1.000 25.99931  ?  136 GLN   A C   1 
ATOM   6657  O O   . GLN   E  1 136 ? 44.66826  53.45053  36.02990  1.000 43.49369  ?  136 GLN   A O   1 
ATOM   6658  C CB  . GLN   E  1 136 ? 45.80041  56.24404  34.87954  1.000 26.68770  ?  136 GLN   A CB  1 
ATOM   6659  C CG  . GLN   E  1 136 ? 45.44432  57.67528  34.56065  1.000 21.92050  ?  136 GLN   A CG  1 
ATOM   6660  C CD  . GLN   E  1 136 ? 44.99140  57.85540  33.13343  1.000 47.17882  ?  136 GLN   A CD  1 
ATOM   6661  O OE1 . GLN   E  1 136 ? 45.61309  57.32979  32.18506  1.000 35.09879  ?  136 GLN   A OE1 1 
ATOM   6662  N NE2 . GLN   E  1 136 ? 43.89169  58.59664  32.96277  1.000 22.42291  ?  136 GLN   A NE2 1 
ATOM   6663  N N   . ARG   E  1 137 ? 46.64570  53.96574  37.02036  1.000 26.35452  ?  137 ARG   A N   1 
ATOM   6664  C CA  . ARG   E  1 137 ? 46.98918  52.56291  37.22592  1.000 16.52874  ?  137 ARG   A CA  1 
ATOM   6665  C C   . ARG   E  1 137 ? 45.97020  51.86458  38.13455  1.000 56.58473  ?  137 ARG   A C   1 
ATOM   6666  O O   . ARG   E  1 137 ? 45.47526  50.78768  37.79844  1.000 27.76480  ?  137 ARG   A O   1 
ATOM   6667  C CB  . ARG   E  1 137 ? 48.39808  52.42954  37.79190  1.000 38.21751  ?  137 ARG   A CB  1 
ATOM   6668  C CG  . ARG   E  1 137 ? 49.48107  52.35987  36.72086  1.000 7.52485   ?  137 ARG   A CG  1 
ATOM   6669  C CD  . ARG   E  1 137 ? 50.85274  52.36753  37.30706  1.000 50.39148  ?  137 ARG   A CD  1 
ATOM   6670  N NE  . ARG   E  1 137 ? 51.88701  52.78244  36.36025  1.000 58.91317  ?  137 ARG   A NE  1 
ATOM   6671  C CZ  . ARG   E  1 137 ? 53.14454  52.99940  36.72558  1.000 32.70399  ?  137 ARG   A CZ  1 
ATOM   6672  N NH1 . ARG   E  1 137 ? 53.53342  52.83279  37.97613  1.000 26.26103  ?  137 ARG   A NH1 1 
ATOM   6673  N NH2 . ARG   E  1 137 ? 54.03258  53.40800  35.82459  1.000 45.40019  ?  137 ARG   A NH2 1 
ATOM   6674  N N   . LEU   E  1 138 ? 45.65215  52.46032  39.29739  1.000 16.81141  ?  138 LEU   A N   1 
ATOM   6675  C CA  . LEU   E  1 138 ? 44.60900  51.91130  40.16959  1.000 29.86889  ?  138 LEU   A CA  1 
ATOM   6676  C C   . LEU   E  1 138 ? 43.25272  51.84767  39.46837  1.000 39.30789  ?  138 LEU   A C   1 
ATOM   6677  O O   . LEU   E  1 138 ? 42.52324  50.85460  39.59296  1.000 28.85718  ?  138 LEU   A O   1 
ATOM   6678  C CB  . LEU   E  1 138 ? 44.48615  52.75209  41.43587  1.000 23.65222  ?  138 LEU   A CB  1 
ATOM   6679  C CG  . LEU   E  1 138 ? 43.53522  52.17430  42.47143  1.000 37.53207  ?  138 LEU   A CG  1 
ATOM   6680  C CD1 . LEU   E  1 138 ? 44.11868  50.86797  42.96807  1.000 24.01060  ?  138 LEU   A CD1 1 
ATOM   6681  C CD2 . LEU   E  1 138 ? 43.32336  53.14197  43.62397  1.000 21.34359  ?  138 LEU   A CD2 1 
ATOM   6682  N N   . ASN   E  1 139 ? 42.89172  52.89996  38.73417  1.000 25.04651  ?  139 ASN   A N   1 
ATOM   6683  C CA  . ASN   E  1 139 ? 41.57638  52.91740  38.10840  1.000 41.24895  ?  139 ASN   A CA  1 
ATOM   6684  C C   . ASN   E  1 139 ? 41.42097  51.80328  37.08063  1.000 27.85624  ?  139 ASN   A C   1 
ATOM   6685  O O   . ASN   E  1 139 ? 40.29689  51.33172  36.85879  1.000 41.75842  ?  139 ASN   A O   1 
ATOM   6686  C CB  . ASN   E  1 139 ? 41.30942  54.29759  37.51086  1.000 17.55012  ?  139 ASN   A CB  1 
ATOM   6687  C CG  . ASN   E  1 139 ? 40.98526  55.30915  38.58904  1.000 34.37258  ?  139 ASN   A CG  1 
ATOM   6688  O OD1 . ASN   E  1 139 ? 40.24987  54.98738  39.53146  1.000 25.95143  ?  139 ASN   A OD1 1 
ATOM   6689  N ND2 . ASN   E  1 139 ? 41.55791  56.50628  38.49899  1.000 22.77230  ?  139 ASN   A ND2 1 
ATOM   6690  N N   . LEU   E  1 140 ? 42.52636  51.34889  36.47143  1.000 34.95895  ?  140 LEU   A N   1 
ATOM   6691  C CA  . LEU   E  1 140 ? 42.46270  50.16000  35.62002  1.000 23.11056  ?  140 LEU   A CA  1 
ATOM   6692  C C   . LEU   E  1 140 ? 41.90704  48.96649  36.38338  1.000 45.39072  ?  140 LEU   A C   1 
ATOM   6693  O O   . LEU   E  1 140 ? 41.16365  48.15130  35.81731  1.000 24.31613  ?  140 LEU   A O   1 
ATOM   6694  C CB  . LEU   E  1 140 ? 43.84152  49.81255  35.07414  1.000 22.64922  ?  140 LEU   A CB  1 
ATOM   6695  C CG  . LEU   E  1 140 ? 44.34888  50.73752  33.97838  1.000 38.89029  ?  140 LEU   A CG  1 
ATOM   6696  C CD1 . LEU   E  1 140 ? 45.76452  50.38285  33.56834  1.000 16.85847  ?  140 LEU   A CD1 1 
ATOM   6697  C CD2 . LEU   E  1 140 ? 43.41431  50.67530  32.79806  1.000 10.71362  ?  140 LEU   A CD2 1 
ATOM   6698  N N   . HIS   E  1 141 ? 42.25823  48.84596  37.67441  1.000 25.55284  ?  141 HIS   A N   1 
ATOM   6699  C CA  . HIS   E  1 141 ? 41.76357  47.72291  38.46470  1.000 23.45155  ?  141 HIS   A CA  1 
ATOM   6700  C C   . HIS   E  1 141 ? 40.29000  47.89182  38.81302  1.000 24.62859  ?  141 HIS   A C   1 
ATOM   6701  O O   . HIS   E  1 141 ? 39.50808  46.94313  38.68134  1.000 31.31559  ?  141 HIS   A O   1 
ATOM   6702  C CB  . HIS   E  1 141 ? 42.60874  47.55481  39.71424  1.000 13.42744  ?  141 HIS   A CB  1 
ATOM   6703  C CG  . HIS   E  1 141 ? 43.96767  47.00249  39.42774  1.000 40.97821  ?  141 HIS   A CG  1 
ATOM   6704  N ND1 . HIS   E  1 141 ? 44.19724  45.65447  39.26281  1.000 38.81568  ?  141 HIS   A ND1 1 
ATOM   6705  C CD2 . HIS   E  1 141 ? 45.16270  47.61456  39.24065  1.000 34.13694  ?  141 HIS   A CD2 1 
ATOM   6706  C CE1 . HIS   E  1 141 ? 45.47733  45.45778  39.00174  1.000 26.33795  ?  141 HIS   A CE1 1 
ATOM   6707  N NE2 . HIS   E  1 141 ? 46.08695  46.63023  38.98708  1.000 39.58624  ?  141 HIS   A NE2 1 
ATOM   6708  N N   . PHE   E  1 142 ? 39.88130  49.09572  39.23408  1.000 25.39180  ?  142 PHE   A N   1 
ATOM   6709  C CA  . PHE   E  1 142 ? 38.45482  49.34273  39.44768  1.000 38.62682  ?  142 PHE   A CA  1 
ATOM   6710  C C   . PHE   E  1 142 ? 37.64921  48.98780  38.20669  1.000 25.52155  ?  142 PHE   A C   1 
ATOM   6711  O O   . PHE   E  1 142 ? 36.56852  48.38714  38.30257  1.000 27.48073  ?  142 PHE   A O   1 
ATOM   6712  C CB  . PHE   E  1 142 ? 38.21459  50.80082  39.83571  1.000 24.59262  ?  142 PHE   A CB  1 
ATOM   6713  C CG  . PHE   E  1 142 ? 38.58658  51.11645  41.25240  1.000 31.77701  ?  142 PHE   A CG  1 
ATOM   6714  C CD1 . PHE   E  1 142 ? 38.17087  50.29969  42.28681  1.000 26.60905  ?  142 PHE   A CD1 1 
ATOM   6715  C CD2 . PHE   E  1 142 ? 39.36257  52.22685  41.55067  1.000 28.10011  ?  142 PHE   A CD2 1 
ATOM   6716  C CE1 . PHE   E  1 142 ? 38.51966  50.59014  43.59188  1.000 25.68780  ?  142 PHE   A CE1 1 
ATOM   6717  C CE2 . PHE   E  1 142 ? 39.70684  52.51849  42.86071  1.000 29.20538  ?  142 PHE   A CE2 1 
ATOM   6718  C CZ  . PHE   E  1 142 ? 39.28481  51.69816  43.87398  1.000 24.42203  ?  142 PHE   A CZ  1 
ATOM   6719  N N   . LYS   E  1 143 ? 38.16193  49.34984  37.03208  1.000 35.22831  ?  143 LYS   A N   1 
ATOM   6720  C CA  . LYS   E  1 143 ? 37.47542  48.99574  35.80014  1.000 30.89527  ?  143 LYS   A CA  1 
ATOM   6721  C C   . LYS   E  1 143 ? 37.24625  47.49760  35.73118  1.000 34.17090  ?  143 LYS   A C   1 
ATOM   6722  O O   . LYS   E  1 143 ? 36.11380  47.04713  35.50871  1.000 37.53247  ?  143 LYS   A O   1 
ATOM   6723  C CB  . LYS   E  1 143 ? 38.27245  49.47306  34.59212  1.000 34.44841  ?  143 LYS   A CB  1 
ATOM   6724  C CG  . LYS   E  1 143 ? 37.47373  49.44000  33.32039  1.000 21.01311  ?  143 LYS   A CG  1 
ATOM   6725  C CD  . LYS   E  1 143 ? 38.33488  49.09456  32.14100  1.000 29.17472  ?  143 LYS   A CD  1 
ATOM   6726  C CE  . LYS   E  1 143 ? 37.59676  49.38087  30.84744  1.000 35.73302  ?  143 LYS   A CE  1 
ATOM   6727  N NZ  . LYS   E  1 143 ? 36.40406  48.51627  30.63999  1.000 40.34218  ?  143 LYS   A NZ  1 
ATOM   6728  N N   . LYS   E  1 144 ? 38.29944  46.69889  35.92235  1.000 33.54967  ?  144 LYS   A N   1 
ATOM   6729  C CA  . LYS   E  1 144 ? 38.13119  45.24943  35.85140  1.000 57.28265  ?  144 LYS   A CA  1 
ATOM   6730  C C   . LYS   E  1 144 ? 37.21334  44.73306  36.95455  1.000 36.37778  ?  144 LYS   A C   1 
ATOM   6731  O O   . LYS   E  1 144 ? 36.44399  43.79726  36.72810  1.000 34.87886  ?  144 LYS   A O   1 
ATOM   6732  C CB  . LYS   E  1 144 ? 39.48661  44.53801  35.91470  1.000 26.12091  ?  144 LYS   A CB  1 
ATOM   6733  C CG  . LYS   E  1 144 ? 39.39446  43.02119  35.48496  1.000 16.25211  ?  144 LYS   A CG  1 
ATOM   6734  C CD  . LYS   E  1 144 ? 40.50373  42.70260  34.50199  1.000 103.71507 ?  144 LYS   A CD  1 
ATOM   6735  C CE  . LYS   E  1 144 ? 41.77901  43.42617  34.95572  1.000 127.88622 ?  144 LYS   A CE  1 
ATOM   6736  N NZ  . LYS   E  1 144 ? 43.08363  42.87704  34.49508  1.000 26.25291  ?  144 LYS   A NZ  1 
ATOM   6737  N N   . LEU   E  1 145 ? 37.30885  45.28452  38.16696  1.000 23.81870  ?  145 LEU   A N   1 
ATOM   6738  C CA  . LEU   E  1 145 ? 36.39742  44.85225  39.22307  1.000 18.24673  ?  145 LEU   A CA  1 
ATOM   6739  C C   . LEU   E  1 145 ? 34.94394  45.04851  38.79673  1.000 38.40799  ?  145 LEU   A C   1 
ATOM   6740  O O   . LEU   E  1 145 ? 34.14423  44.10397  38.81246  1.000 36.63489  ?  145 LEU   A O   1 
ATOM   6741  C CB  . LEU   E  1 145 ? 36.69915  45.60136  40.52593  1.000 29.08301  ?  145 LEU   A CB  1 
ATOM   6742  C CG  . LEU   E  1 145 ? 38.08915  45.33069  41.11600  1.000 31.73433  ?  145 LEU   A CG  1 
ATOM   6743  C CD1 . LEU   E  1 145 ? 38.29492  46.03636  42.45020  1.000 25.43544  ?  145 LEU   A CD1 1 
ATOM   6744  C CD2 . LEU   E  1 145 ? 38.29934  43.84608  41.27815  1.000 24.81527  ?  145 LEU   A CD2 1 
ATOM   6745  N N   . PHE   E  1 146 ? 34.59977  46.25797  38.34887  1.000 23.12132  ?  146 PHE   A N   1 
ATOM   6746  C CA  . PHE   E  1 146 ? 33.20629  46.55011  38.02682  1.000 27.07544  ?  146 PHE   A CA  1 
ATOM   6747  C C   . PHE   E  1 146 ? 32.75441  45.83639  36.76032  1.000 35.31471  ?  146 PHE   A C   1 
ATOM   6748  O O   . PHE   E  1 146 ? 31.59254  45.42607  36.66943  1.000 36.02443  ?  146 PHE   A O   1 
ATOM   6749  C CB  . PHE   E  1 146 ? 33.00468  48.06313  37.90215  1.000 27.30411  ?  146 PHE   A CB  1 
ATOM   6750  C CG  . PHE   E  1 146 ? 33.40592  48.83827  39.14197  1.000 30.87775  ?  146 PHE   A CG  1 
ATOM   6751  C CD1 . PHE   E  1 146 ? 33.42672  48.22725  40.39727  1.000 30.92117  ?  146 PHE   A CD1 1 
ATOM   6752  C CD2 . PHE   E  1 146 ? 33.75093  50.17475  39.05257  1.000 23.98622  ?  146 PHE   A CD2 1 
ATOM   6753  C CE1 . PHE   E  1 146 ? 33.78499  48.93956  41.52961  1.000 31.03644  ?  146 PHE   A CE1 1 
ATOM   6754  C CE2 . PHE   E  1 146 ? 34.11523  50.89714  40.18167  1.000 27.56928  ?  146 PHE   A CE2 1 
ATOM   6755  C CZ  . PHE   E  1 146 ? 34.13009  50.28226  41.42332  1.000 33.22746  ?  146 PHE   A CZ  1 
ATOM   6756  N N   . ASP   E  1 147 ? 33.64041  45.67307  35.77471  1.000 29.17799  ?  147 ASP   A N   1 
ATOM   6757  C CA  . ASP   E  1 147 ? 33.26483  44.87073  34.61377  1.000 22.80601  ?  147 ASP   A CA  1 
ATOM   6758  C C   . ASP   E  1 147 ? 32.93779  43.44394  35.03574  1.000 32.37073  ?  147 ASP   A C   1 
ATOM   6759  O O   . ASP   E  1 147 ? 31.95634  42.84877  34.55680  1.000 30.68457  ?  147 ASP   A O   1 
ATOM   6760  C CB  . ASP   E  1 147 ? 34.37884  44.86799  33.56159  1.000 15.25246  ?  147 ASP   A CB  1 
ATOM   6761  C CG  . ASP   E  1 147 ? 34.50851  46.19519  32.81924  1.000 48.33062  ?  147 ASP   A CG  1 
ATOM   6762  O OD1 . ASP   E  1 147 ? 33.55453  47.01854  32.82806  1.000 40.44661  ?  147 ASP   A OD1 1 
ATOM   6763  O OD2 . ASP   E  1 147 ? 35.58091  46.39767  32.20939  1.000 44.62708  -1 147 ASP   A OD2 1 
ATOM   6764  N N   . THR   E  1 148 ? 33.75604  42.87980  35.93392  1.000 30.25859  ?  148 THR   A N   1 
ATOM   6765  C CA  . THR   E  1 148 ? 33.50177  41.53524  36.43872  1.000 39.70738  ?  148 THR   A CA  1 
ATOM   6766  C C   . THR   E  1 148 ? 32.14299  41.47658  37.12453  1.000 36.61317  ?  148 THR   A C   1 
ATOM   6767  O O   . THR   E  1 148 ? 31.33658  40.57561  36.85529  1.000 42.62882  ?  148 THR   A O   1 
ATOM   6768  C CB  . THR   E  1 148 ? 34.62961  41.11426  37.39137  1.000 34.56862  ?  148 THR   A CB  1 
ATOM   6769  O OG1 . THR   E  1 148 ? 35.82382  40.87974  36.63816  1.000 35.43617  ?  148 THR   A OG1 1 
ATOM   6770  C CG2 . THR   E  1 148 ? 34.27383  39.83930  38.14393  1.000 23.87201  ?  148 THR   A CG2 1 
ATOM   6771  N N   . TRP   E  1 149 ? 31.86357  42.46164  37.99182  1.000 28.44412  ?  149 TRP   A N   1 
ATOM   6772  C CA  . TRP   E  1 149 ? 30.57102  42.53713  38.66556  1.000 21.55002  ?  149 TRP   A CA  1 
ATOM   6773  C C   . TRP   E  1 149 ? 29.43812  42.61202  37.65085  1.000 45.57633  ?  149 TRP   A C   1 
ATOM   6774  O O   . TRP   E  1 149 ? 28.41932  41.92549  37.79306  1.000 30.39556  ?  149 TRP   A O   1 
ATOM   6775  C CB  . TRP   E  1 149 ? 30.54836  43.75198  39.60335  1.000 19.12088  ?  149 TRP   A CB  1 
ATOM   6776  C CG  . TRP   E  1 149 ? 29.31955  43.85896  40.50655  1.000 30.14565  ?  149 TRP   A CG  1 
ATOM   6777  C CD1 . TRP   E  1 149 ? 28.38062  42.89065  40.73985  1.000 24.46773  ?  149 TRP   A CD1 1 
ATOM   6778  C CD2 . TRP   E  1 149 ? 28.90958  45.00247  41.28535  1.000 40.48430  ?  149 TRP   A CD2 1 
ATOM   6779  N NE1 . TRP   E  1 149 ? 27.42251  43.35436  41.61298  1.000 36.67964  ?  149 TRP   A NE1 1 
ATOM   6780  C CE2 . TRP   E  1 149 ? 27.72121  44.64565  41.96036  1.000 22.95816  ?  149 TRP   A CE2 1 
ATOM   6781  C CE3 . TRP   E  1 149 ? 29.43083  46.29383  41.47438  1.000 22.07562  ?  149 TRP   A CE3 1 
ATOM   6782  C CZ2 . TRP   E  1 149 ? 27.05062  45.52621  42.82056  1.000 32.40368  ?  149 TRP   A CZ2 1 
ATOM   6783  C CZ3 . TRP   E  1 149 ? 28.75208  47.17970  42.33378  1.000 24.93781  ?  149 TRP   A CZ3 1 
ATOM   6784  C CH2 . TRP   E  1 149 ? 27.57993  46.78622  42.99183  1.000 32.15518  ?  149 TRP   A CH2 1 
ATOM   6785  N N   . GLY   E  1 150 ? 29.61642  43.42144  36.59971  1.000 29.05061  ?  150 GLY   A N   1 
ATOM   6786  C CA  . GLY   E  1 150 ? 28.55143  43.62097  35.63484  1.000 18.40759  ?  150 GLY   A CA  1 
ATOM   6787  C C   . GLY   E  1 150 ? 28.18645  42.35702  34.88497  1.000 39.70009  ?  150 GLY   A C   1 
ATOM   6788  O O   . GLY   E  1 150 ? 27.04278  42.20376  34.43581  1.000 51.75379  ?  150 GLY   A O   1 
ATOM   6789  N N   . LEU   E  1 151 ? 29.15056  41.44484  34.72820  1.000 35.45639  ?  151 LEU   A N   1 
ATOM   6790  C CA  . LEU   E  1 151 ? 28.85796  40.11928  34.18558  1.000 30.17454  ?  151 LEU   A CA  1 
ATOM   6791  C C   . LEU   E  1 151 ? 27.77271  39.42315  34.98158  1.000 69.61508  ?  151 LEU   A C   1 
ATOM   6792  O O   . LEU   E  1 151 ? 26.79564  38.90623  34.41961  1.000 42.67294  ?  151 LEU   A O   1 
ATOM   6793  C CB  . LEU   E  1 151 ? 30.09761  39.25877  34.23402  1.000 42.36993  ?  151 LEU   A CB  1 
ATOM   6794  C CG  . LEU   E  1 151 ? 31.14630  39.62098  33.23162  1.000 63.46660  ?  151 LEU   A CG  1 
ATOM   6795  C CD1 . LEU   E  1 151 ? 32.16674  38.55423  33.41613  1.000 28.64004  ?  151 LEU   A CD1 1 
ATOM   6796  C CD2 . LEU   E  1 151 ? 30.47817  39.56382  31.89026  1.000 17.16295  ?  151 LEU   A CD2 1 
ATOM   6797  N N   . PHE   E  1 152 ? 27.98094  39.33086  36.29631  1.000 25.17395  ?  152 PHE   A N   1 
ATOM   6798  C CA  . PHE   E  1 152 ? 26.97130  38.75052  37.16196  1.000 37.92435  ?  152 PHE   A CA  1 
ATOM   6799  C C   . PHE   E  1 152 ? 25.64000  39.48358  37.03632  1.000 51.15760  ?  152 PHE   A C   1 
ATOM   6800  O O   . PHE   E  1 152 ? 24.57828  38.85306  37.05337  1.000 43.61270  ?  152 PHE   A O   1 
ATOM   6801  C CB  . PHE   E  1 152 ? 27.45236  38.76827  38.60679  1.000 20.18772  ?  152 PHE   A CB  1 
ATOM   6802  C CG  . PHE   E  1 152 ? 26.40690  38.35123  39.56242  1.000 46.44534  ?  152 PHE   A CG  1 
ATOM   6803  C CD1 . PHE   E  1 152 ? 26.05940  37.02165  39.67046  1.000 29.39607  ?  152 PHE   A CD1 1 
ATOM   6804  C CD2 . PHE   E  1 152 ? 25.72097  39.29182  40.31056  1.000 37.26323  ?  152 PHE   A CD2 1 
ATOM   6805  C CE1 . PHE   E  1 152 ? 25.06511  36.63080  40.53121  1.000 36.39036  ?  152 PHE   A CE1 1 
ATOM   6806  C CE2 . PHE   E  1 152 ? 24.72902  38.90909  41.17955  1.000 46.84179  ?  152 PHE   A CE2 1 
ATOM   6807  C CZ  . PHE   E  1 152 ? 24.39947  37.57689  41.29428  1.000 38.59070  ?  152 PHE   A CZ  1 
ATOM   6808  N N   . LEU   E  1 153 ? 25.66959  40.81235  36.90290  1.000 33.07477  ?  153 LEU   A N   1 
ATOM   6809  C CA  . LEU   E  1 153 ? 24.42591  41.57421  36.86738  1.000 34.98174  ?  153 LEU   A CA  1 
ATOM   6810  C C   . LEU   E  1 153 ? 23.69375  41.45620  35.53387  1.000 34.56710  ?  153 LEU   A C   1 
ATOM   6811  O O   . LEU   E  1 153 ? 22.58719  41.98923  35.39871  1.000 38.96227  ?  153 LEU   A O   1 
ATOM   6812  C CB  . LEU   E  1 153 ? 24.70869  43.03472  37.18785  1.000 27.70215  ?  153 LEU   A CB  1 
ATOM   6813  C CG  . LEU   E  1 153 ? 25.34089  43.29917  38.54817  1.000 40.77008  ?  153 LEU   A CG  1 
ATOM   6814  C CD1 . LEU   E  1 153 ? 25.69081  44.77481  38.65627  1.000 22.94816  ?  153 LEU   A CD1 1 
ATOM   6815  C CD2 . LEU   E  1 153 ? 24.41396  42.86749  39.68295  1.000 22.96440  ?  153 LEU   A CD2 1 
ATOM   6816  N N   . SER   E  1 154 ? 24.28989  40.77670  34.55653  1.000 36.53827  ?  154 SER   A N   1 
ATOM   6817  C CA  . SER   E  1 154 ? 23.66072  40.45390  33.28586  1.000 34.28932  ?  154 SER   A CA  1 
ATOM   6818  C C   . SER   E  1 154 ? 23.13570  39.02469  33.24994  1.000 44.37138  ?  154 SER   A C   1 
ATOM   6819  O O   . SER   E  1 154 ? 22.53246  38.62433  32.24981  1.000 48.61274  ?  154 SER   A O   1 
ATOM   6820  C CB  . SER   E  1 154 ? 24.66405  40.65938  32.14548  1.000 21.48607  ?  154 SER   A CB  1 
ATOM   6821  O OG  . SER   E  1 154 ? 24.99994  42.02673  32.04903  1.000 102.12015 ?  154 SER   A OG  1 
ATOM   6822  N N   . SER   E  1 155 ? 23.35329  38.25429  34.31361  1.000 35.04822  ?  155 SER   A N   1 
ATOM   6823  C CA  . SER   E  1 155 ? 23.08612  36.82554  34.36892  1.000 35.67209  ?  155 SER   A CA  1 
ATOM   6824  C C   . SER   E  1 155 ? 21.74758  36.56012  35.04498  1.000 100.27653 ?  155 SER   A C   1 
ATOM   6825  O O   . SER   E  1 155 ? 21.28306  37.35271  35.87573  1.000 33.76167  ?  155 SER   A O   1 
ATOM   6826  C CB  . SER   E  1 155 ? 24.19646  36.10590  35.13499  1.000 32.42473  ?  155 SER   A CB  1 
ATOM   6827  O OG  . SER   E  1 155 ? 24.14797  36.39524  36.52504  1.000 42.47420  ?  155 SER   A OG  1 
ATOM   6828  N N   . LYS   E  1 156 ? 21.14014  35.41254  34.69476  1.000 42.08681  ?  156 LYS   A N   1 
ATOM   6829  C CA  . LYS   E  1 156 ? 19.82419  35.08012  35.23923  1.000 58.90504  ?  156 LYS   A CA  1 
ATOM   6830  C C   . LYS   E  1 156 ? 19.84358  35.09717  36.76638  1.000 32.32596  ?  156 LYS   A C   1 
ATOM   6831  O O   . LYS   E  1 156 ? 18.84334  35.46146  37.39934  1.000 48.17017  ?  156 LYS   A O   1 
ATOM   6832  C CB  . LYS   E  1 156 ? 19.34714  33.72100  34.70193  1.000 25.04129  ?  156 LYS   A CB  1 
ATOM   6833  N N   . ASP   E  1 157 ? 21.00038  34.78916  37.37080  1.000 46.53150  ?  157 ASP   A N   1 
ATOM   6834  C CA  . ASP   E  1 157 ? 21.10872  34.69881  38.82857  1.000 45.50387  ?  157 ASP   A CA  1 
ATOM   6835  C C   . ASP   E  1 157 ? 20.93066  36.04044  39.52525  1.000 48.02295  ?  157 ASP   A C   1 
ATOM   6836  O O   . ASP   E  1 157 ? 20.57490  36.06670  40.71067  1.000 43.90883  ?  157 ASP   A O   1 
ATOM   6837  C CB  . ASP   E  1 157 ? 22.45914  34.09999  39.22614  1.000 56.85539  ?  157 ASP   A CB  1 
ATOM   6838  C CG  . ASP   E  1 157 ? 22.58631  32.62993  38.84461  1.000 57.89344  ?  157 ASP   A CG  1 
ATOM   6839  O OD1 . ASP   E  1 157 ? 21.67093  31.84335  39.16849  1.000 68.49458  ?  157 ASP   A OD1 1 
ATOM   6840  O OD2 . ASP   E  1 157 ? 23.60555  32.26644  38.21459  1.000 87.19760  -1 157 ASP   A OD2 1 
ATOM   6841  N N   . SER   E  1 158 ? 21.18116  37.15108  38.82887  1.000 56.84487  ?  158 SER   A N   1 
ATOM   6842  C CA  . SER   E  1 158 ? 20.98575  38.45514  39.44663  1.000 42.27394  ?  158 SER   A CA  1 
ATOM   6843  C C   . SER   E  1 158 ? 19.51219  38.84179  39.55169  1.000 45.11887  ?  158 SER   A C   1 
ATOM   6844  O O   . SER   E  1 158 ? 19.22236  39.90918  40.10433  1.000 40.17776  ?  158 SER   A O   1 
ATOM   6845  C CB  . SER   E  1 158 ? 21.75860  39.52902  38.67095  1.000 35.73146  ?  158 SER   A CB  1 
ATOM   6846  O OG  . SER   E  1 158 ? 21.17994  39.75607  37.39401  1.000 35.18997  ?  158 SER   A OG  1 
ATOM   6847  N N   . ARG   E  1 159 ? 18.57886  38.01496  39.05535  1.000 32.70555  ?  159 ARG   A N   1 
ATOM   6848  C CA  . ARG   E  1 159 ? 17.15581  38.33280  39.18468  1.000 39.92175  ?  159 ARG   A CA  1 
ATOM   6849  C C   . ARG   E  1 159 ? 16.64820  38.22966  40.61914  1.000 40.67824  ?  159 ARG   A C   1 
ATOM   6850  O O   . ARG   E  1 159 ? 15.57691  38.76192  40.91875  1.000 35.09608  ?  159 ARG   A O   1 
ATOM   6851  C CB  . ARG   E  1 159 ? 16.31439  37.41364  38.30288  1.000 22.55426  ?  159 ARG   A CB  1 
ATOM   6852  C CG  . ARG   E  1 159 ? 16.42788  37.71715  36.82712  1.000 58.52405  ?  159 ARG   A CG  1 
ATOM   6853  C CD  . ARG   E  1 159 ? 15.77974  36.61276  36.04185  1.000 42.60730  ?  159 ARG   A CD  1 
ATOM   6854  N NE  . ARG   E  1 159 ? 16.31348  35.32607  36.46069  1.000 56.46989  ?  159 ARG   A NE  1 
ATOM   6855  C CZ  . ARG   E  1 159 ? 15.75104  34.15712  36.19302  1.000 47.63729  ?  159 ARG   A CZ  1 
ATOM   6856  N NH1 . ARG   E  1 159 ? 14.61637  34.07375  35.51429  1.000 40.10912  ?  159 ARG   A NH1 1 
ATOM   6857  N NH2 . ARG   E  1 159 ? 16.34023  33.04562  36.62038  1.000 37.32968  ?  159 ARG   A NH2 1 
ATOM   6858  N N   . ASN   E  1 160 ? 17.39253  37.58127  41.51689  1.000 33.11869  ?  160 ASN   A N   1 
ATOM   6859  C CA  . ASN   E  1 160 ? 16.87319  37.30311  42.85354  1.000 37.46414  ?  160 ASN   A CA  1 
ATOM   6860  C C   . ASN   E  1 160 ? 16.53578  38.55614  43.65895  1.000 29.89178  ?  160 ASN   A C   1 
ATOM   6861  O O   . ASN   E  1 160 ? 15.83325  38.45000  44.66785  1.000 59.66359  ?  160 ASN   A O   1 
ATOM   6862  C CB  . ASN   E  1 160 ? 17.87259  36.44860  43.62515  1.000 35.51367  ?  160 ASN   A CB  1 
ATOM   6863  C CG  . ASN   E  1 160 ? 19.07024  37.23270  44.06624  1.000 47.68816  ?  160 ASN   A CG  1 
ATOM   6864  O OD1 . ASN   E  1 160 ? 19.87633  37.67565  43.24113  1.000 61.14413  ?  160 ASN   A OD1 1 
ATOM   6865  N ND2 . ASN   E  1 160 ? 19.19673  37.42626  45.37194  1.000 51.88159  ?  160 ASN   A ND2 1 
ATOM   6866  N N   . VAL   E  1 161 ? 17.02531  39.73433  43.26506  1.000 42.27924  ?  161 VAL   A N   1 
ATOM   6867  C CA  . VAL   E  1 161 ? 16.59002  40.96576  43.92739  1.000 45.08424  ?  161 VAL   A CA  1 
ATOM   6868  C C   . VAL   E  1 161 ? 15.32912  41.53632  43.30130  1.000 47.78425  ?  161 VAL   A C   1 
ATOM   6869  O O   . VAL   E  1 161 ? 14.77460  42.51780  43.82427  1.000 30.48822  ?  161 VAL   A O   1 
ATOM   6870  C CB  . VAL   E  1 161 ? 17.67446  42.06264  43.89918  1.000 39.03064  ?  161 VAL   A CB  1 
ATOM   6871  C CG1 . VAL   E  1 161 ? 18.91597  41.63492  44.69218  1.000 27.89585  ?  161 VAL   A CG1 1 
ATOM   6872  C CG2 . VAL   E  1 161 ? 18.01765  42.40506  42.46467  1.000 22.78801  ?  161 VAL   A CG2 1 
ATOM   6873  N N   . LEU   E  1 162 ? 14.87260  40.96946  42.18650  1.000 28.59628  ?  162 LEU   A N   1 
ATOM   6874  C CA  . LEU   E  1 162 ? 13.67575  41.44098  41.49733  1.000 39.04213  ?  162 LEU   A CA  1 
ATOM   6875  C C   . LEU   E  1 162 ? 12.44969  40.75269  42.10209  1.000 57.97254  ?  162 LEU   A C   1 
ATOM   6876  O O   . LEU   E  1 162 ? 11.78383  39.90580  41.49699  1.000 40.56883  ?  162 LEU   A O   1 
ATOM   6877  C CB  . LEU   E  1 162 ? 13.79993  41.18149  40.00426  1.000 35.69895  ?  162 LEU   A CB  1 
ATOM   6878  C CG  . LEU   E  1 162 ? 15.00476  41.86177  39.36867  1.000 24.33840  ?  162 LEU   A CG  1 
ATOM   6879  C CD1 . LEU   E  1 162 ? 14.95943  41.71628  37.85768  1.000 20.03211  ?  162 LEU   A CD1 1 
ATOM   6880  C CD2 . LEU   E  1 162 ? 15.01045  43.33490  39.78291  1.000 18.87509  ?  162 LEU   A CD2 1 
ATOM   6881  N N   . VAL   E  1 163 ? 12.17065  41.13904  43.34518  1.000 32.41734  ?  163 VAL   A N   1 
ATOM   6882  C CA  . VAL   E  1 163 ? 11.16643  40.50952  44.19597  1.000 29.46244  ?  163 VAL   A CA  1 
ATOM   6883  C C   . VAL   E  1 163 ? 10.57152  41.59196  45.08923  1.000 49.88787  ?  163 VAL   A C   1 
ATOM   6884  O O   . VAL   E  1 163 ? 11.09040  42.70816  45.18072  1.000 42.47056  ?  163 VAL   A O   1 
ATOM   6885  C CB  . VAL   E  1 163 ? 11.75921  39.37525  45.07078  1.000 31.42304  ?  163 VAL   A CB  1 
ATOM   6886  C CG1 . VAL   E  1 163 ? 12.36043  38.24697  44.20425  1.000 25.00726  ?  163 VAL   A CG1 1 
ATOM   6887  C CG2 . VAL   E  1 163 ? 12.80323  39.93705  46.04107  1.000 24.53622  ?  163 VAL   A CG2 1 
ATOM   6888  N N   . ALA   E  1 164 ? 9.48026   41.25775  45.77846  1.000 49.06456  ?  164 ALA   A N   1 
ATOM   6889  C CA  . ALA   E  1 164 ? 8.89460   42.21217  46.71422  1.000 56.67054  ?  164 ALA   A CA  1 
ATOM   6890  C C   . ALA   E  1 164 ? 9.39392   42.03319  48.14006  1.000 47.67084  ?  164 ALA   A C   1 
ATOM   6891  O O   . ALA   E  1 164 ? 9.19730   42.93767  48.96178  1.000 45.58559  ?  164 ALA   A O   1 
ATOM   6892  C CB  . ALA   E  1 164 ? 7.37211   42.11135  46.69664  1.000 27.52707  ?  164 ALA   A CB  1 
ATOM   6893  N N   . ASP   E  1 165 ? 10.04398  40.89746  48.43217  1.000 43.95944  ?  165 ASP   A N   1 
ATOM   6894  C CA  . ASP   E  1 165 ? 10.55073  40.56955  49.76162  1.000 42.29388  ?  165 ASP   A CA  1 
ATOM   6895  C C   . ASP   E  1 165 ? 11.22456  41.76876  50.41870  1.000 42.15437  ?  165 ASP   A C   1 
ATOM   6896  O O   . ASP   E  1 165 ? 12.02865  42.46978  49.80258  1.000 77.17639  ?  165 ASP   A O   1 
ATOM   6897  C CB  . ASP   E  1 165 ? 11.55389  39.40478  49.67731  1.000 49.56988  ?  165 ASP   A CB  1 
ATOM   6898  C CG  . ASP   E  1 165 ? 11.04956  38.23325  48.84062  1.000 37.52286  ?  165 ASP   A CG  1 
ATOM   6899  O OD1 . ASP   E  1 165 ? 9.89060   38.26298  48.36911  1.000 83.77381  ?  165 ASP   A OD1 1 
ATOM   6900  O OD2 . ASP   E  1 165 ? 11.83304  37.27348  48.65815  1.000 86.47191  -1 165 ASP   A OD2 1 
ATOM   6901  N N   . GLN   E  1 166 ? 10.87313  42.01099  51.67135  1.000 64.29568  ?  166 GLN   A N   1 
ATOM   6902  C CA  . GLN   E  1 166 ? 11.63672  42.91156  52.51736  1.000 78.76402  ?  166 GLN   A CA  1 
ATOM   6903  C C   . GLN   E  1 166 ? 12.81722  42.11687  53.06424  1.000 41.02315  ?  166 GLN   A C   1 
ATOM   6904  O O   . GLN   E  1 166 ? 12.64197  40.98234  53.51518  1.000 114.62468 ?  166 GLN   A O   1 
ATOM   6905  C CB  . GLN   E  1 166 ? 10.75028  43.47540  53.63440  1.000 38.34960  ?  166 GLN   A CB  1 
ATOM   6906  C CG  . GLN   E  1 166 ? 11.43483  44.39857  54.60956  1.000 74.86557  ?  166 GLN   A CG  1 
ATOM   6907  C CD  . GLN   E  1 166 ? 11.29662  45.84246  54.20038  1.000 134.28490 ?  166 GLN   A CD  1 
ATOM   6908  O OE1 . GLN   E  1 166 ? 12.11926  46.68800  54.57051  1.000 89.04999  ?  166 GLN   A OE1 1 
ATOM   6909  N NE2 . GLN   E  1 166 ? 10.25555  46.14015  53.43179  1.000 75.45363  ?  166 GLN   A NE2 1 
ATOM   6910  N N   . PHE   E  1 167 ? 14.02154  42.68417  52.96998  1.000 74.49021  ?  167 PHE   A N   1 
ATOM   6911  C CA  . PHE   E  1 167 ? 15.25230  41.96552  53.30055  1.000 73.44813  ?  167 PHE   A CA  1 
ATOM   6912  C C   . PHE   E  1 167 ? 15.75560  42.23381  54.71210  1.000 74.95195  ?  167 PHE   A C   1 
ATOM   6913  O O   . PHE   E  1 167 ? 16.43122  41.37734  55.28990  1.000 70.93149  ?  167 PHE   A O   1 
ATOM   6914  C CB  . PHE   E  1 167 ? 16.37476  42.34046  52.32337  1.000 63.54975  ?  167 PHE   A CB  1 
ATOM   6915  C CG  . PHE   E  1 167 ? 16.14275  41.88403  50.91148  1.000 69.04581  ?  167 PHE   A CG  1 
ATOM   6916  C CD1 . PHE   E  1 167 ? 16.28869  42.75240  49.84436  1.000 57.26011  ?  167 PHE   A CD1 1 
ATOM   6917  C CD2 . PHE   E  1 167 ? 15.80411  40.58672  50.64826  1.000 48.36809  ?  167 PHE   A CD2 1 
ATOM   6918  C CE1 . PHE   E  1 167 ? 16.08154  42.32144  48.54220  1.000 127.98352 ?  167 PHE   A CE1 1 
ATOM   6919  C CE2 . PHE   E  1 167 ? 15.59703  40.15198  49.35216  1.000 116.80458 ?  167 PHE   A CE2 1 
ATOM   6920  C CZ  . PHE   E  1 167 ? 15.72881  41.00742  48.30559  1.000 36.08574  ?  167 PHE   A CZ  1 
ATOM   6921  N N   . ASP   E  1 168 ? 15.48576  43.41597  55.25128  1.000 79.60134  ?  168 ASP   A N   1 
ATOM   6922  C CA  . ASP   E  1 168 ? 15.82306  43.78856  56.61778  1.000 44.87492  ?  168 ASP   A CA  1 
ATOM   6923  C C   . ASP   E  1 168 ? 15.05265  45.06417  56.93628  1.000 96.18546  ?  168 ASP   A C   1 
ATOM   6924  O O   . ASP   E  1 168 ? 14.08765  45.40902  56.20492  1.000 69.70998  ?  168 ASP   A O   1 
ATOM   6925  C CB  . ASP   E  1 168 ? 17.35663  43.89011  56.79925  1.000 58.95449  ?  168 ASP   A CB  1 
ATOM   6926  C CG  . ASP   E  1 168 ? 17.98584  45.10109  56.08508  1.000 83.74181  ?  168 ASP   A CG  1 
ATOM   6927  O OD1 . ASP   E  1 168 ? 19.16016  45.00355  55.64134  1.000 69.57290  ?  168 ASP   A OD1 1 
ATOM   6928  O OD2 . ASP   E  1 168 ? 17.32811  46.16180  55.99374  1.000 81.49748  -1 168 ASP   A OD2 1 
ATOM   6929  N N   . ASP   E  1 169 ? 15.41381  45.77363  57.99943  1.000 68.73681  ?  169 ASP   A N   1 
ATOM   6930  C CA  . ASP   E  1 169 ? 14.61897  46.93184  58.39801  1.000 72.62857  ?  169 ASP   A CA  1 
ATOM   6931  C C   . ASP   E  1 169 ? 14.69299  48.04707  57.35301  1.000 89.47641  ?  169 ASP   A C   1 
ATOM   6932  O O   . ASP   E  1 169 ? 13.71397  48.77655  57.15354  1.000 77.30522  ?  169 ASP   A O   1 
ATOM   6933  C CB  . ASP   E  1 169 ? 15.06146  47.43653  59.77836  1.000 51.21154  ?  169 ASP   A CB  1 
ATOM   6934  N N   . ARG   E  1 170 ? 15.81740  48.16470  56.63659  1.000 139.48948 ?  170 ARG   A N   1 
ATOM   6935  C CA  . ARG   E  1 170 ? 16.04443  49.29759  55.74581  1.000 50.38959  ?  170 ARG   A CA  1 
ATOM   6936  C C   . ARG   E  1 170 ? 16.06034  48.95156  54.25198  1.000 68.67332  ?  170 ARG   A C   1 
ATOM   6937  O O   . ARG   E  1 170 ? 15.98659  49.87188  53.42950  1.000 59.68991  ?  170 ARG   A O   1 
ATOM   6938  C CB  . ARG   E  1 170 ? 17.36089  49.99614  56.12601  1.000 56.24261  ?  170 ARG   A CB  1 
ATOM   6939  N N   . HIS   E  1 171 ? 16.12532  47.66680  53.87154  1.000 63.02209  ?  171 HIS   A N   1 
ATOM   6940  C CA  . HIS   E  1 171 ? 16.29953  47.25426  52.47889  1.000 66.25241  ?  171 HIS   A CA  1 
ATOM   6941  C C   . HIS   E  1 171 ? 15.16770  46.34108  52.02545  1.000 32.80481  ?  171 HIS   A C   1 
ATOM   6942  O O   . HIS   E  1 171 ? 14.64342  45.54127  52.80289  1.000 104.08353 ?  171 HIS   A O   1 
ATOM   6943  C CB  . HIS   E  1 171 ? 17.63187  46.50313  52.25910  1.000 69.02166  ?  171 HIS   A CB  1 
ATOM   6944  C CG  . HIS   E  1 171 ? 18.83743  47.23995  52.75325  1.000 64.20526  ?  171 HIS   A CG  1 
ATOM   6945  N ND1 . HIS   E  1 171 ? 18.86892  48.61098  52.89548  1.000 69.86855  ?  171 HIS   A ND1 1 
ATOM   6946  C CD2 . HIS   E  1 171 ? 20.05035  46.79305  53.15503  1.000 64.43271  ?  171 HIS   A CD2 1 
ATOM   6947  C CE1 . HIS   E  1 171 ? 20.04958  48.97812  53.35811  1.000 44.62270  ?  171 HIS   A CE1 1 
ATOM   6948  N NE2 . HIS   E  1 171 ? 20.78627  47.89419  53.52200  1.000 119.88588 ?  171 HIS   A NE2 1 
ATOM   6949  N N   . CYS   E  1 172 ? 14.82668  46.43779  50.74023  1.000 65.93863  ?  172 CYS   A N   1 
ATOM   6950  C CA  . CYS   E  1 172 ? 13.80764  45.58223  50.14771  1.000 35.26466  ?  172 CYS   A CA  1 
ATOM   6951  C C   . CYS   E  1 172 ? 14.14166  45.31024  48.68735  1.000 36.32324  ?  172 CYS   A C   1 
ATOM   6952  O O   . CYS   E  1 172 ? 15.02901  45.93618  48.10195  1.000 59.25281  ?  172 CYS   A O   1 
ATOM   6953  C CB  . CYS   E  1 172 ? 12.42364  46.21591  50.24046  1.000 44.38018  ?  172 CYS   A CB  1 
ATOM   6954  S SG  . CYS   E  1 172 ? 12.30896  47.75273  49.32911  1.000 52.35437  ?  172 CYS   A SG  1 
ATOM   6955  N N   . GLY   E  1 173 ? 13.39444  44.37430  48.10023  1.000 45.43976  ?  173 GLY   A N   1 
ATOM   6956  C CA  . GLY   E  1 173 ? 13.53296  44.06341  46.69241  1.000 30.09189  ?  173 GLY   A CA  1 
ATOM   6957  C C   . GLY   E  1 173 ? 12.93833  45.14524  45.80424  1.000 44.65999  ?  173 GLY   A C   1 
ATOM   6958  O O   . GLY   E  1 173 ? 12.19619  46.02647  46.24523  1.000 44.71563  ?  173 GLY   A O   1 
ATOM   6959  N N   . TRP   E  1 174 ? 13.27116  45.05901  44.50769  1.000 26.61865  ?  174 TRP   A N   1 
ATOM   6960  C CA  . TRP   E  1 174 ? 12.92275  46.11039  43.55853  1.000 52.19633  ?  174 TRP   A CA  1 
ATOM   6961  C C   . TRP   E  1 174 ? 11.46410  46.05248  43.12291  1.000 60.77916  ?  174 TRP   A C   1 
ATOM   6962  O O   . TRP   E  1 174 ? 10.96188  47.03707  42.57617  1.000 44.96040  ?  174 TRP   A O   1 
ATOM   6963  C CB  . TRP   E  1 174 ? 13.85204  46.04304  42.33741  1.000 29.95070  ?  174 TRP   A CB  1 
ATOM   6964  C CG  . TRP   E  1 174 ? 15.24460  46.45211  42.68961  1.000 60.00083  ?  174 TRP   A CG  1 
ATOM   6965  C CD1 . TRP   E  1 174 ? 16.30491  45.62657  42.93094  1.000 37.95203  ?  174 TRP   A CD1 1 
ATOM   6966  C CD2 . TRP   E  1 174 ? 15.72272  47.79125  42.88461  1.000 46.66461  ?  174 TRP   A CD2 1 
ATOM   6967  N NE1 . TRP   E  1 174 ? 17.41554  46.36710  43.25294  1.000 40.43273  ?  174 TRP   A NE1 1 
ATOM   6968  C CE2 . TRP   E  1 174 ? 17.08866  47.69830  43.23004  1.000 32.49211  ?  174 TRP   A CE2 1 
ATOM   6969  C CE3 . TRP   E  1 174 ? 15.13232  49.05910  42.78475  1.000 34.70992  ?  174 TRP   A CE3 1 
ATOM   6970  C CZ2 . TRP   E  1 174 ? 17.87978  48.82761  43.48082  1.000 24.90348  ?  174 TRP   A CZ2 1 
ATOM   6971  C CZ3 . TRP   E  1 174 ? 15.91147  50.17650  43.04422  1.000 36.74523  ?  174 TRP   A CZ3 1 
ATOM   6972  C CH2 . TRP   E  1 174 ? 17.27660  50.05135  43.38642  1.000 27.89780  ?  174 TRP   A CH2 1 
ATOM   6973  N N   . LEU   E  1 175 ? 10.77049  44.94105  43.36777  1.000 42.15606  ?  175 LEU   A N   1 
ATOM   6974  C CA  . LEU   E  1 175 ? 9.34865   44.81652  43.06995  1.000 37.10963  ?  175 LEU   A CA  1 
ATOM   6975  C C   . LEU   E  1 175 ? 8.46381   45.04199  44.29545  1.000 46.80659  ?  175 LEU   A C   1 
ATOM   6976  O O   . LEU   E  1 175 ? 7.23708   44.96685  44.18339  1.000 55.65582  ?  175 LEU   A O   1 
ATOM   6977  C CB  . LEU   E  1 175 ? 9.07187   43.44607  42.45298  1.000 32.10646  ?  175 LEU   A CB  1 
ATOM   6978  C CG  . LEU   E  1 175 ? 9.90094   43.22281  41.18438  1.000 42.71795  ?  175 LEU   A CG  1 
ATOM   6979  C CD1 . LEU   E  1 175 ? 9.53939   41.92498  40.45581  1.000 33.26397  ?  175 LEU   A CD1 1 
ATOM   6980  C CD2 . LEU   E  1 175 ? 9.74613   44.42678  40.26487  1.000 30.20908  ?  175 LEU   A CD2 1 
ATOM   6981  N N   . ASN   E  1 176 ? 9.06517   45.29937  45.45743  1.000 40.07714  ?  176 ASN   A N   1 
ATOM   6982  C CA  . ASN   E  1 176 ? 8.34719   45.78065  46.63169  1.000 35.66687  ?  176 ASN   A CA  1 
ATOM   6983  C C   . ASN   E  1 176 ? 7.66630   47.11173  46.32089  1.000 52.07586  ?  176 ASN   A C   1 
ATOM   6984  O O   . ASN   E  1 176 ? 8.18553   47.92085  45.54533  1.000 65.96077  ?  176 ASN   A O   1 
ATOM   6985  C CB  . ASN   E  1 176 ? 9.35156   45.93861  47.76562  1.000 62.58961  ?  176 ASN   A CB  1 
ATOM   6986  C CG  . ASN   E  1 176 ? 8.71367   46.24670  49.07828  1.000 60.90079  ?  176 ASN   A CG  1 
ATOM   6987  O OD1 . ASN   E  1 176 ? 8.43085   47.40908  49.39551  1.000 47.08749  ?  176 ASN   A OD1 1 
ATOM   6988  N ND2 . ASN   E  1 176 ? 8.53747   45.21179  49.89140  1.000 48.42883  ?  176 ASN   A ND2 1 
ATOM   6989  N N   . GLU   E  1 177 ? 6.48984   47.34311  46.91647  1.000 58.22655  ?  177 GLU   A N   1 
ATOM   6990  C CA  . GLU   E  1 177 ? 5.72578   48.52408  46.52090  1.000 55.52537  ?  177 GLU   A CA  1 
ATOM   6991  C C   . GLU   E  1 177 ? 6.41529   49.80995  46.95786  1.000 49.29578  ?  177 GLU   A C   1 
ATOM   6992  O O   . GLU   E  1 177 ? 6.25068   50.84790  46.31157  1.000 58.54302  ?  177 GLU   A O   1 
ATOM   6993  C CB  . GLU   E  1 177 ? 4.29696   48.46936  47.06869  1.000 37.27755  ?  177 GLU   A CB  1 
ATOM   6994  N N   . ARG   E  1 178 ? 7.20023   49.77040  48.03538  1.000 43.22121  ?  178 ARG   A N   1 
ATOM   6995  C CA  . ARG   E  1 178 ? 7.98061   50.94697  48.41761  1.000 66.78380  ?  178 ARG   A CA  1 
ATOM   6996  C C   . ARG   E  1 178 ? 8.88096   51.39520  47.26654  1.000 62.95980  ?  178 ARG   A C   1 
ATOM   6997  O O   . ARG   E  1 178 ? 8.95569   52.58846  46.94256  1.000 61.41952  ?  178 ARG   A O   1 
ATOM   6998  C CB  . ARG   E  1 178 ? 8.80727   50.63480  49.67517  1.000 31.96771  ?  178 ARG   A CB  1 
ATOM   6999  C CG  . ARG   E  1 178 ? 9.23622   51.86042  50.48786  1.000 69.55646  ?  178 ARG   A CG  1 
ATOM   7000  C CD  . ARG   E  1 178 ? 10.04694  51.39991  51.69604  1.000 61.49975  ?  178 ARG   A CD  1 
ATOM   7001  N NE  . ARG   E  1 178 ? 11.45984  51.73887  51.58620  1.000 82.45902  ?  178 ARG   A NE  1 
ATOM   7002  C CZ  . ARG   E  1 178 ? 12.43668  51.07847  52.19415  1.000 131.91140 ?  178 ARG   A CZ  1 
ATOM   7003  N NH1 . ARG   E  1 178 ? 12.20909  49.95664  52.85320  1.000 138.83274 ?  178 ARG   A NH1 1 
ATOM   7004  N NH2 . ARG   E  1 178 ? 13.68295  51.56477  52.14223  1.000 54.27531  ?  178 ARG   A NH2 1 
ATOM   7005  N N   . ALA   E  1 179 ? 9.54644   50.43481  46.61383  1.000 60.67143  ?  179 ALA   A N   1 
ATOM   7006  C CA  . ALA   E  1 179 ? 10.47139  50.74426  45.53260  1.000 59.33719  ?  179 ALA   A CA  1 
ATOM   7007  C C   . ALA   E  1 179 ? 9.71992   51.04036  44.24019  1.000 48.15159  ?  179 ALA   A C   1 
ATOM   7008  O O   . ALA   E  1 179 ? 10.05665  51.98390  43.51107  1.000 55.79692  ?  179 ALA   A O   1 
ATOM   7009  C CB  . ALA   E  1 179 ? 11.44060  49.57632  45.33995  1.000 35.17645  ?  179 ALA   A CB  1 
ATOM   7010  N N   . LEU   E  1 180 ? 8.71380   50.21400  43.93373  1.000 50.92852  ?  180 LEU   A N   1 
ATOM   7011  C CA  . LEU   E  1 180 ? 7.82803   50.46488  42.79893  1.000 37.88384  ?  180 LEU   A CA  1 
ATOM   7012  C C   . LEU   E  1 180 ? 7.24877   51.87790  42.84868  1.000 54.26210  ?  180 LEU   A C   1 
ATOM   7013  O O   . LEU   E  1 180 ? 7.17812   52.57146  41.82408  1.000 54.38221  ?  180 LEU   A O   1 
ATOM   7014  C CB  . LEU   E  1 180 ? 6.71334   49.41921  42.79454  1.000 33.21837  ?  180 LEU   A CB  1 
ATOM   7015  C CG  . LEU   E  1 180 ? 6.76529   48.30041  41.76147  1.000 58.03522  ?  180 LEU   A CG  1 
ATOM   7016  C CD1 . LEU   E  1 180 ? 8.11880   47.68335  41.69010  1.000 55.66638  ?  180 LEU   A CD1 1 
ATOM   7017  C CD2 . LEU   E  1 180 ? 5.74534   47.23990  42.08867  1.000 45.71006  ?  180 LEU   A CD2 1 
ATOM   7018  N N   . SER   E  1 181 ? 6.84190   52.32671  44.03930  1.000 49.17525  ?  181 SER   A N   1 
ATOM   7019  C CA  . SER   E  1 181 ? 6.30890   53.67713  44.17862  1.000 53.08663  ?  181 SER   A CA  1 
ATOM   7020  C C   . SER   E  1 181 ? 7.37707   54.72770  43.87688  1.000 40.78537  ?  181 SER   A C   1 
ATOM   7021  O O   . SER   E  1 181 ? 7.13016   55.67558  43.11825  1.000 52.09844  ?  181 SER   A O   1 
ATOM   7022  C CB  . SER   E  1 181 ? 5.72961   53.85878  45.58482  1.000 35.46636  ?  181 SER   A CB  1 
ATOM   7023  O OG  . SER   E  1 181 ? 5.55378   55.23201  45.90213  1.000 103.68705 ?  181 SER   A OG  1 
ATOM   7024  N N   . ALA   E  1 182 ? 8.57497   54.57149  44.46131  1.000 45.58966  ?  182 ALA   A N   1 
ATOM   7025  C CA  . ALA   E  1 182 ? 9.64284   55.55115  44.26309  1.000 67.25850  ?  182 ALA   A CA  1 
ATOM   7026  C C   . ALA   E  1 182 ? 9.97429   55.72428  42.78599  1.000 46.76773  ?  182 ALA   A C   1 
ATOM   7027  O O   . ALA   E  1 182 ? 10.16178  56.85351  42.31365  1.000 34.59435  ?  182 ALA   A O   1 
ATOM   7028  C CB  . ALA   E  1 182 ? 10.88937  55.13878  45.05178  1.000 25.78335  ?  182 ALA   A CB  1 
ATOM   7029  N N   . MET   E  1 183 ? 10.00763  54.61682  42.03506  1.000 29.00092  ?  183 MET   A N   1 
ATOM   7030  C CA  . MET   E  1 183 ? 10.40512  54.62986  40.63327  1.000 45.12772  ?  183 MET   A CA  1 
ATOM   7031  C C   . MET   E  1 183 ? 9.39056   55.27147  39.68758  1.000 30.46797  ?  183 MET   A C   1 
ATOM   7032  O O   . MET   E  1 183 ? 9.75577   55.56805  38.54281  1.000 49.06278  ?  183 MET   A O   1 
ATOM   7033  C CB  . MET   E  1 183 ? 10.70841  53.20591  40.18658  1.000 29.78755  ?  183 MET   A CB  1 
ATOM   7034  C CG  . MET   E  1 183 ? 12.10550  52.77837  40.60286  1.000 31.88900  ?  183 MET   A CG  1 
ATOM   7035  S SD  . MET   E  1 183 ? 12.56123  51.14758  40.02318  1.000 41.09940  ?  183 MET   A SD  1 
ATOM   7036  C CE  . MET   E  1 183 ? 11.73157  50.03572  41.14569  1.000 37.35310  ?  183 MET   A CE  1 
ATOM   7037  N N   . VAL   E  1 184 ? 8.14710   55.50496  40.10897  1.000 34.74898  ?  184 VAL   A N   1 
ATOM   7038  C CA  . VAL   E  1 184 ? 7.18784   56.18772  39.24901  1.000 41.60717  ?  184 VAL   A CA  1 
ATOM   7039  C C   . VAL   E  1 184 ? 6.75043   57.52202  39.82686  1.000 23.15085  ?  184 VAL   A C   1 
ATOM   7040  O O   . VAL   E  1 184 ? 5.77357   58.10052  39.35930  1.000 34.07427  ?  184 VAL   A O   1 
ATOM   7041  C CB  . VAL   E  1 184 ? 5.96437   55.30699  38.93487  1.000 21.01970  ?  184 VAL   A CB  1 
ATOM   7042  C CG1 . VAL   E  1 184 ? 6.40093   54.07195  38.16149  1.000 26.53132  ?  184 VAL   A CG1 1 
ATOM   7043  C CG2 . VAL   E  1 184 ? 5.22428   54.93890  40.21061  1.000 22.12988  ?  184 VAL   A CG2 1 
ATOM   7044  N N   . LYS   E  1 185 ? 7.48170   58.02823  40.81836  1.000 36.33393  ?  185 LYS   A N   1 
ATOM   7045  C CA  . LYS   E  1 185 ? 7.18612   59.32143  41.42571  1.000 39.20953  ?  185 LYS   A CA  1 
ATOM   7046  C C   . LYS   E  1 185 ? 6.87063   60.40963  40.39301  1.000 14.93092  ?  185 LYS   A C   1 
ATOM   7047  O O   . LYS   E  1 185 ? 5.92164   61.18701  40.56505  1.000 73.35908  ?  185 LYS   A O   1 
ATOM   7048  C CB  . LYS   E  1 185 ? 8.37412   59.70968  42.30344  1.000 27.82893  ?  185 LYS   A CB  1 
ATOM   7049  C CG  . LYS   E  1 185 ? 8.32833   61.09267  42.86365  1.000 34.03307  ?  185 LYS   A CG  1 
ATOM   7050  C CD  . LYS   E  1 185 ? 9.40462   61.24342  43.92625  1.000 59.46977  ?  185 LYS   A CD  1 
ATOM   7051  C CE  . LYS   E  1 185 ? 9.10751   62.44468  44.79136  1.000 60.11422  ?  185 LYS   A CE  1 
ATOM   7052  N NZ  . LYS   E  1 185 ? 10.29607  63.31974  44.92236  1.000 73.83928  ?  185 LYS   A NZ  1 
ATOM   7053  N N   . HIS   E  1 186 ? 7.63844   60.47129  39.30322  1.000 42.65103  ?  186 HIS   A N   1 
ATOM   7054  C CA  . HIS   E  1 186 ? 7.49883   61.54232  38.32225  1.000 24.74025  ?  186 HIS   A CA  1 
ATOM   7055  C C   . HIS   E  1 186 ? 6.69650   61.12862  37.09489  1.000 43.97871  ?  186 HIS   A C   1 
ATOM   7056  O O   . HIS   E  1 186 ? 6.80039   61.77007  36.04282  1.000 30.13223  ?  186 HIS   A O   1 
ATOM   7057  C CB  . HIS   E  1 186 ? 8.87166   62.06345  37.90225  1.000 33.18637  ?  186 HIS   A CB  1 
ATOM   7058  C CG  . HIS   E  1 186 ? 9.67494   62.59339  39.04023  1.000 59.22995  ?  186 HIS   A CG  1 
ATOM   7059  N ND1 . HIS   E  1 186 ? 9.28842   63.69456  39.77511  1.000 46.20791  ?  186 HIS   A ND1 1 
ATOM   7060  C CD2 . HIS   E  1 186 ? 10.84317  62.17165  39.57493  1.000 18.86834  ?  186 HIS   A CD2 1 
ATOM   7061  C CE1 . HIS   E  1 186 ? 10.19131  63.93036  40.71177  1.000 33.98717  ?  186 HIS   A CE1 1 
ATOM   7062  N NE2 . HIS   E  1 186 ? 11.14493  63.02172  40.61164  1.000 50.04271  ?  186 HIS   A NE2 1 
ATOM   7063  N N   . TYR   E  1 187 ? 5.88994   60.08084  37.19937  1.000 35.18690  ?  187 TYR   A N   1 
ATOM   7064  C CA  . TYR   E  1 187 ? 5.11376   59.63650  36.05253  1.000 43.14628  ?  187 TYR   A CA  1 
ATOM   7065  C C   . TYR   E  1 187 ? 3.63111   59.89800  36.24058  1.000 79.03372  ?  187 TYR   A C   1 
ATOM   7066  O O   . TYR   E  1 187 ? 2.80101   59.31317  35.53478  1.000 36.58514  ?  187 TYR   A O   1 
ATOM   7067  C CB  . TYR   E  1 187 ? 5.40234   58.16913  35.75040  1.000 47.65711  ?  187 TYR   A CB  1 
ATOM   7068  C CG  . TYR   E  1 187 ? 6.79397   58.03607  35.19755  1.000 31.66442  ?  187 TYR   A CG  1 
ATOM   7069  C CD1 . TYR   E  1 187 ? 7.03938   58.18543  33.83638  1.000 40.08903  ?  187 TYR   A CD1 1 
ATOM   7070  C CD2 . TYR   E  1 187 ? 7.87704   57.83965  36.04597  1.000 46.39093  ?  187 TYR   A CD2 1 
ATOM   7071  C CE1 . TYR   E  1 187 ? 8.32476   58.09123  33.31876  1.000 36.00193  ?  187 TYR   A CE1 1 
ATOM   7072  C CE2 . TYR   E  1 187 ? 9.16132   57.74919  35.55362  1.000 18.54786  ?  187 TYR   A CE2 1 
ATOM   7073  C CZ  . TYR   E  1 187 ? 9.37824   57.86950  34.18494  1.000 45.92758  ?  187 TYR   A CZ  1 
ATOM   7074  O OH  . TYR   E  1 187 ? 10.65416  57.76601  33.70324  1.000 39.31987  ?  187 TYR   A OH  1 
ATOM   7075  N N   . ASN   E  1 188 ? 3.28885   60.78411  37.17363  1.000 36.08311  ?  188 ASN   A N   1 
ATOM   7076  C CA  . ASN   E  1 188 ? 1.98830   61.42378  37.17456  1.000 85.79200  ?  188 ASN   A CA  1 
ATOM   7077  C C   . ASN   E  1 188 ? 0.87369   60.40236  37.41481  1.000 35.05191  ?  188 ASN   A C   1 
ATOM   7078  O O   . ASN   E  1 188 ? -0.08255  60.29594  36.64843  1.000 68.53525  ?  188 ASN   A O   1 
ATOM   7079  C CB  . ASN   E  1 188 ? 1.80824   62.17240  35.85432  1.000 46.53340  ?  188 ASN   A CB  1 
ATOM   7080  C CG  . ASN   E  1 188 ? 0.60165   63.05778  35.84490  1.000 85.84011  ?  188 ASN   A CG  1 
ATOM   7081  O OD1 . ASN   E  1 188 ? -0.49656  62.62842  35.50707  1.000 113.68957 ?  188 ASN   A OD1 1 
ATOM   7082  N ND2 . ASN   E  1 188 ? 0.79653   64.30765  36.20749  1.000 98.68069  ?  188 ASN   A ND2 1 
ATOM   7083  N N   . GLY   E  1 189 ? 1.02744   59.60359  38.46976  1.000 62.47029  ?  189 GLY   A N   1 
ATOM   7084  C CA  . GLY   E  1 189 ? 0.01174   58.64008  38.83854  1.000 29.38707  ?  189 GLY   A CA  1 
ATOM   7085  C C   . GLY   E  1 189 ? 0.02664   57.31291  38.09722  1.000 33.55232  ?  189 GLY   A C   1 
ATOM   7086  O O   . GLY   E  1 189 ? -0.56501  56.34366  38.59245  1.000 66.44859  ?  189 GLY   A O   1 
ATOM   7087  N N   . ARG   E  1 190 ? 0.67105   57.22341  36.92940  1.000 44.40062  ?  190 ARG   A N   1 
ATOM   7088  C CA  . ARG   E  1 190 ? 0.81899   55.93091  36.26557  1.000 32.56216  ?  190 ARG   A CA  1 
ATOM   7089  C C   . ARG   E  1 190 ? 1.70745   54.98042  37.08227  1.000 39.67750  ?  190 ARG   A C   1 
ATOM   7090  O O   . ARG   E  1 190 ? 2.61923   55.39235  37.81444  1.000 50.36408  ?  190 ARG   A O   1 
ATOM   7091  C CB  . ARG   E  1 190 ? 1.39179   56.10645  34.86046  1.000 39.77197  ?  190 ARG   A CB  1 
ATOM   7092  C CG  . ARG   E  1 190 ? 0.67569   57.13235  34.00645  1.000 34.42813  ?  190 ARG   A CG  1 
ATOM   7093  C CD  . ARG   E  1 190 ? -0.07082  56.47097  32.85180  1.000 24.93413  ?  190 ARG   A CD  1 
ATOM   7094  N NE  . ARG   E  1 190 ? 0.81000   55.88806  31.84368  1.000 39.59075  ?  190 ARG   A NE  1 
ATOM   7095  C CZ  . ARG   E  1 190 ? 0.45811   54.89587  31.03771  1.000 56.57103  ?  190 ARG   A CZ  1 
ATOM   7096  N NH1 . ARG   E  1 190 ? -0.73179  54.32582  31.12558  1.000 52.82769  ?  190 ARG   A NH1 1 
ATOM   7097  N NH2 . ARG   E  1 190 ? 1.32333   54.45675  30.12851  1.000 42.22528  ?  190 ARG   A NH2 1 
ATOM   7098  N N   . ALA   E  1 191 ? 1.42759   53.69254  36.94555  1.000 38.61393  ?  191 ALA   A N   1 
ATOM   7099  C CA  . ALA   E  1 191 ? 2.08141   52.65900  37.73144  1.000 26.40922  ?  191 ALA   A CA  1 
ATOM   7100  C C   . ALA   E  1 191 ? 3.26538   52.07174  36.97012  1.000 89.44648  ?  191 ALA   A C   1 
ATOM   7101  O O   . ALA   E  1 191 ? 3.37922   52.21094  35.74666  1.000 27.66447  ?  191 ALA   A O   1 
ATOM   7102  C CB  . ALA   E  1 191 ? 1.09427   51.54236  38.07665  1.000 38.72578  ?  191 ALA   A CB  1 
ATOM   7103  N N   . PHE   E  1 192 ? 4.12502   51.36500  37.71410  1.000 25.03207  ?  192 PHE   A N   1 
ATOM   7104  C CA  . PHE   E  1 192 ? 5.38594   50.87232  37.16275  1.000 28.90480  ?  192 PHE   A CA  1 
ATOM   7105  C C   . PHE   E  1 192 ? 5.17934   50.06466  35.88110  1.000 52.75104  ?  192 PHE   A C   1 
ATOM   7106  O O   . PHE   E  1 192 ? 5.86903   50.28714  34.87519  1.000 42.34079  ?  192 PHE   A O   1 
ATOM   7107  C CB  . PHE   E  1 192 ? 6.11910   50.04810  38.22447  1.000 30.44312  ?  192 PHE   A CB  1 
ATOM   7108  C CG  . PHE   E  1 192 ? 7.48326   49.57790  37.79869  1.000 37.90333  ?  192 PHE   A CG  1 
ATOM   7109  C CD1 . PHE   E  1 192 ? 7.62896   48.46037  36.98520  1.000 47.04965  ?  192 PHE   A CD1 1 
ATOM   7110  C CD2 . PHE   E  1 192 ? 8.62305   50.24871  38.21726  1.000 45.99865  ?  192 PHE   A CD2 1 
ATOM   7111  C CE1 . PHE   E  1 192 ? 8.87940   48.02212  36.58739  1.000 27.64238  ?  192 PHE   A CE1 1 
ATOM   7112  C CE2 . PHE   E  1 192 ? 9.88455   49.81417  37.82486  1.000 52.10052  ?  192 PHE   A CE2 1 
ATOM   7113  C CZ  . PHE   E  1 192 ? 10.00824  48.69469  37.01158  1.000 35.54460  ?  192 PHE   A CZ  1 
ATOM   7114  N N   . ASP   E  1 193 ? 4.23845   49.11667  35.90021  1.000 49.87010  ?  193 ASP   A N   1 
ATOM   7115  C CA  . ASP   E  1 193 ? 4.01198   48.23901  34.75297  1.000 29.96726  ?  193 ASP   A CA  1 
ATOM   7116  C C   . ASP   E  1 193 ? 3.27248   48.92795  33.60361  1.000 56.46067  ?  193 ASP   A C   1 
ATOM   7117  O O   . ASP   E  1 193 ? 3.27327   48.41070  32.47875  1.000 17.34736  ?  193 ASP   A O   1 
ATOM   7118  C CB  . ASP   E  1 193 ? 3.25278   46.98875  35.20605  1.000 42.85773  ?  193 ASP   A CB  1 
ATOM   7119  C CG  . ASP   E  1 193 ? 1.89511   47.31868  35.79203  1.000 85.73901  ?  193 ASP   A CG  1 
ATOM   7120  O OD1 . ASP   E  1 193 ? 1.84371   47.92374  36.88414  1.000 46.45560  ?  193 ASP   A OD1 1 
ATOM   7121  O OD2 . ASP   E  1 193 ? 0.88036   47.00335  35.13429  1.000 44.95359  -1 193 ASP   A OD2 1 
ATOM   7122  N N   . GLU   E  1 194 ? 2.64314   50.07662  33.84997  1.000 20.76743  ?  194 GLU   A N   1 
ATOM   7123  C CA  . GLU   E  1 194 ? 2.16263   50.91309  32.75398  1.000 47.73861  ?  194 GLU   A CA  1 
ATOM   7124  C C   . GLU   E  1 194 ? 3.31412   51.66376  32.09536  1.000 52.11557  ?  194 GLU   A C   1 
ATOM   7125  O O   . GLU   E  1 194 ? 3.43319   51.67229  30.86303  1.000 40.60921  ?  194 GLU   A O   1 
ATOM   7126  C CB  . GLU   E  1 194 ? 1.12459   51.90909  33.26530  1.000 39.50141  ?  194 GLU   A CB  1 
ATOM   7127  C CG  . GLU   E  1 194 ? -0.09361  51.27775  33.93541  1.000 25.27817  ?  194 GLU   A CG  1 
ATOM   7128  C CD  . GLU   E  1 194 ? -1.06194  52.33051  34.46716  1.000 82.85225  ?  194 GLU   A CD  1 
ATOM   7129  O OE1 . GLU   E  1 194 ? -0.73007  52.96281  35.49345  1.000 57.46316  ?  194 GLU   A OE1 1 
ATOM   7130  O OE2 . GLU   E  1 194 ? -2.13539  52.54622  33.85199  1.000 55.01567  -1 194 GLU   A OE2 1 
ATOM   7131  N N   . VAL   E  1 195 ? 4.17776   52.27974  32.91904  1.000 50.10050  ?  195 VAL   A N   1 
ATOM   7132  C CA  . VAL   E  1 195 ? 5.25934   53.13597  32.42935  1.000 17.90043  ?  195 VAL   A CA  1 
ATOM   7133  C C   . VAL   E  1 195 ? 6.33461   52.31627  31.71478  1.000 79.32643  ?  195 VAL   A C   1 
ATOM   7134  O O   . VAL   E  1 195 ? 6.74816   52.63980  30.59444  1.000 31.11593  ?  195 VAL   A O   1 
ATOM   7135  C CB  . VAL   E  1 195 ? 5.86144   53.93649  33.59517  1.000 53.13574  ?  195 VAL   A CB  1 
ATOM   7136  C CG1 . VAL   E  1 195 ? 7.06091   54.74662  33.11895  1.000 22.80690  ?  195 VAL   A CG1 1 
ATOM   7137  C CG2 . VAL   E  1 195 ? 4.80383   54.82820  34.23724  1.000 27.80382  ?  195 VAL   A CG2 1 
ATOM   7138  N N   . PHE   E  1 196 ? 6.82365   51.26315  32.35399  1.000 18.94787  ?  196 PHE   A N   1 
ATOM   7139  C CA  . PHE   E  1 196 ? 7.93388   50.50010  31.81387  1.000 50.86813  ?  196 PHE   A CA  1 
ATOM   7140  C C   . PHE   E  1 196 ? 7.43572   49.18575  31.22502  1.000 31.36270  ?  196 PHE   A C   1 
ATOM   7141  O O   . PHE   E  1 196 ? 6.43313   48.62684  31.67211  1.000 33.62359  ?  196 PHE   A O   1 
ATOM   7142  C CB  . PHE   E  1 196 ? 8.98182   50.24265  32.90036  1.000 23.61001  ?  196 PHE   A CB  1 
ATOM   7143  C CG  . PHE   E  1 196 ? 9.47182   51.48940  33.55869  1.000 41.06610  ?  196 PHE   A CG  1 
ATOM   7144  C CD1 . PHE   E  1 196 ? 10.21258  52.41900  32.84349  1.000 24.77067  ?  196 PHE   A CD1 1 
ATOM   7145  C CD2 . PHE   E  1 196 ? 9.17549   51.75080  34.88470  1.000 18.18400  ?  196 PHE   A CD2 1 
ATOM   7146  C CE1 . PHE   E  1 196 ? 10.65636  53.59280  33.45147  1.000 28.78635  ?  196 PHE   A CE1 1 
ATOM   7147  C CE2 . PHE   E  1 196 ? 9.62353   52.91851  35.50322  1.000 36.36903  ?  196 PHE   A CE2 1 
ATOM   7148  C CZ  . PHE   E  1 196 ? 10.36745  53.83905  34.78764  1.000 27.75741  ?  196 PHE   A CZ  1 
ATOM   7149  N N   . LEU   E  1 197 ? 8.15071   48.70219  30.21068  1.000 29.33302  ?  197 LEU   A N   1 
ATOM   7150  C CA  . LEU   E  1 197 ? 7.81379   47.46423  29.50979  1.000 32.15947  ?  197 LEU   A CA  1 
ATOM   7151  C C   . LEU   E  1 197 ? 8.21883   46.27512  30.37003  1.000 50.75331  ?  197 LEU   A C   1 
ATOM   7152  O O   . LEU   E  1 197 ? 9.40770   45.97459  30.51146  1.000 26.15233  ?  197 LEU   A O   1 
ATOM   7153  C CB  . LEU   E  1 197 ? 8.53166   47.42105  28.16665  1.000 29.69249  ?  197 LEU   A CB  1 
ATOM   7154  C CG  . LEU   E  1 197 ? 8.13526   46.46395  27.05170  1.000 26.38857  ?  197 LEU   A CG  1 
ATOM   7155  C CD1 . LEU   E  1 197 ? 8.93546   46.90064  25.86450  1.000 34.63345  ?  197 LEU   A CD1 1 
ATOM   7156  C CD2 . LEU   E  1 197 ? 8.47511   45.02664  27.35860  1.000 73.58923  ?  197 LEU   A CD2 1 
ATOM   7157  N N   . CYS   E  1 198 ? 7.23907   45.57540  30.92025  1.000 41.22421  ?  198 CYS   A N   1 
ATOM   7158  C CA  . CYS   E  1 198 ? 7.51614   44.40648  31.72879  1.000 40.39824  ?  198 CYS   A CA  1 
ATOM   7159  C C   . CYS   E  1 198 ? 6.27794   43.52490  31.69689  1.000 44.02903  ?  198 CYS   A C   1 
ATOM   7160  O O   . CYS   E  1 198 ? 5.35064   43.75640  30.91354  1.000 51.12592  ?  198 CYS   A O   1 
ATOM   7161  C CB  . CYS   E  1 198 ? 7.89290   44.82214  33.15426  1.000 33.85241  ?  198 CYS   A CB  1 
ATOM   7162  S SG  . CYS   E  1 198 ? 6.62646   45.89814  33.92451  1.000 42.58862  ?  198 CYS   A SG  1 
ATOM   7163  N N   . ASP   E  1 199 ? 6.26019   42.52187  32.57089  1.000 43.93788  ?  199 ASP   A N   1 
ATOM   7164  C CA  . ASP   E  1 199 ? 5.11732   41.63367  32.75911  1.000 32.41208  ?  199 ASP   A CA  1 
ATOM   7165  C C   . ASP   E  1 199 ? 4.84141   41.54156  34.25821  1.000 67.02832  ?  199 ASP   A C   1 
ATOM   7166  O O   . ASP   E  1 199 ? 5.55755   40.83380  34.97688  1.000 32.16750  ?  199 ASP   A O   1 
ATOM   7167  C CB  . ASP   E  1 199 ? 5.41067   40.25922  32.15589  1.000 34.21692  ?  199 ASP   A CB  1 
ATOM   7168  C CG  . ASP   E  1 199 ? 4.25021   39.27980  32.29776  1.000 135.56570 ?  199 ASP   A CG  1 
ATOM   7169  O OD1 . ASP   E  1 199 ? 3.24675   39.58397  32.99830  1.000 37.05307  ?  199 ASP   A OD1 1 
ATOM   7170  O OD2 . ASP   E  1 199 ? 4.36740   38.19345  31.68368  1.000 44.75310  -1 199 ASP   A OD2 1 
ATOM   7171  N N   . LYS   E  1 200 ? 3.80459   42.24697  34.73809  1.000 34.08951  ?  200 LYS   A N   1 
ATOM   7172  C CA  . LYS   E  1 200 ? 3.55504   42.28439  36.18049  1.000 59.55029  ?  200 LYS   A CA  1 
ATOM   7173  C C   . LYS   E  1 200 ? 3.12821   40.93371  36.73806  1.000 56.29457  ?  200 LYS   A C   1 
ATOM   7174  O O   . LYS   E  1 200 ? 3.16221   40.75502  37.95812  1.000 48.01134  ?  200 LYS   A O   1 
ATOM   7175  C CB  . LYS   E  1 200 ? 2.49969   43.34151  36.53433  1.000 33.90481  ?  200 LYS   A CB  1 
ATOM   7176  C CG  . LYS   E  1 200 ? 1.07080   42.95164  36.21089  1.000 56.69434  ?  200 LYS   A CG  1 
ATOM   7177  C CD  . LYS   E  1 200 ? 0.08045   44.07414  36.53976  1.000 77.20429  ?  200 LYS   A CD  1 
ATOM   7178  C CE  . LYS   E  1 200 ? -0.04376  44.34064  38.04305  1.000 60.48265  ?  200 LYS   A CE  1 
ATOM   7179  N NZ  . LYS   E  1 200 ? -1.28242  45.13203  38.35853  1.000 55.06244  ?  200 LYS   A NZ  1 
ATOM   7180  N N   . ASN   E  1 201 ? 2.75698   39.98165  35.88306  1.000 46.06913  ?  201 ASN   A N   1 
ATOM   7181  C CA  . ASN   E  1 201 ? 2.33250   38.65632  36.30722  1.000 69.23083  ?  201 ASN   A CA  1 
ATOM   7182  C C   . ASN   E  1 201 ? 3.43701   37.62377  36.21451  1.000 44.97579  ?  201 ASN   A C   1 
ATOM   7183  O O   . ASN   E  1 201 ? 3.24964   36.48938  36.66199  1.000 77.01644  ?  201 ASN   A O   1 
ATOM   7184  C CB  . ASN   E  1 201 ? 1.14126   38.21056  35.46894  1.000 43.22870  ?  201 ASN   A CB  1 
ATOM   7185  C CG  . ASN   E  1 201 ? -0.00907  39.15852  35.59484  1.000 80.69246  ?  201 ASN   A CG  1 
ATOM   7186  O OD1 . ASN   E  1 201 ? -0.32615  39.62231  36.70355  1.000 33.92503  ?  201 ASN   A OD1 1 
ATOM   7187  N ND2 . ASN   E  1 201 ? -0.61934  39.49966  34.46541  1.000 48.80695  ?  201 ASN   A ND2 1 
ATOM   7188  N N   . ALA   E  1 202 ? 4.51484   37.96611  35.67795  1.000 93.92905  ?  202 ALA   A N   1 
ATOM   7189  C CA  . ALA   E  1 202 ? 5.60915   37.02549  35.55513  1.000 46.42471  ?  202 ALA   A CA  1 
ATOM   7190  C C   . ALA   E  1 202 ? 6.52007   37.11558  36.77270  1.000 39.65559  ?  202 ALA   A C   1 
ATOM   7191  O O   . ALA   E  1 202 ? 6.53918   38.13692  37.47273  1.000 51.40973  ?  202 ALA   A O   1 
ATOM   7192  C CB  . ALA   E  1 202 ? 6.40604   37.30597  34.28969  1.000 23.79305  ?  202 ALA   A CB  1 
ATOM   7193  N N   . PRO   E  1 203 ? 7.24526   36.04498  37.08225  1.000 79.60908  ?  203 PRO   A N   1 
ATOM   7194  C CA  . PRO   E  1 203 ? 8.29856   36.15694  38.09731  1.000 74.42933  ?  203 PRO   A CA  1 
ATOM   7195  C C   . PRO   E  1 203 ? 9.37268   37.12449  37.62316  1.000 64.25436  ?  203 PRO   A C   1 
ATOM   7196  O O   . PRO   E  1 203 ? 9.73732   37.15336  36.43807  1.000 44.51118  ?  203 PRO   A O   1 
ATOM   7197  C CB  . PRO   E  1 203 ? 8.83340   34.72388  38.23775  1.000 51.71222  ?  203 PRO   A CB  1 
ATOM   7198  C CG  . PRO   E  1 203 ? 8.37346   33.99777  36.99800  1.000 42.42073  ?  203 PRO   A CG  1 
ATOM   7199  C CD  . PRO   E  1 203 ? 7.10541   34.67837  36.54833  1.000 30.55405  ?  203 PRO   A CD  1 
ATOM   7200  N N   . TYR   E  1 204 ? 9.84863   37.94772  38.56280  1.000 39.38281  ?  204 TYR   A N   1 
ATOM   7201  C CA  . TYR   E  1 204 ? 10.83192  38.99358  38.29949  1.000 50.45244  ?  204 TYR   A CA  1 
ATOM   7202  C C   . TYR   E  1 204 ? 10.31139  40.03760  37.33150  1.000 44.16131  ?  204 TYR   A C   1 
ATOM   7203  O O   . TYR   E  1 204 ? 11.09720  40.65045  36.60545  1.000 48.51462  ?  204 TYR   A O   1 
ATOM   7204  C CB  . TYR   E  1 204 ? 12.14041  38.40044  37.76311  1.000 37.85875  ?  204 TYR   A CB  1 
ATOM   7205  C CG  . TYR   E  1 204 ? 12.55273  37.15827  38.51219  1.000 42.13433  ?  204 TYR   A CG  1 
ATOM   7206  C CD1 . TYR   E  1 204 ? 12.77220  37.20616  39.89139  1.000 36.89576  ?  204 TYR   A CD1 1 
ATOM   7207  C CD2 . TYR   E  1 204 ? 12.71356  35.93737  37.85352  1.000 33.08320  ?  204 TYR   A CD2 1 
ATOM   7208  C CE1 . TYR   E  1 204 ? 13.13934  36.07497  40.60430  1.000 19.61114  ?  204 TYR   A CE1 1 
ATOM   7209  C CE2 . TYR   E  1 204 ? 13.08623  34.79727  38.55286  1.000 30.12607  ?  204 TYR   A CE2 1 
ATOM   7210  C CZ  . TYR   E  1 204 ? 13.28758  34.87573  39.93121  1.000 43.33933  ?  204 TYR   A CZ  1 
ATOM   7211  O OH  . TYR   E  1 204 ? 13.66109  33.76661  40.65138  1.000 45.34925  ?  204 TYR   A OH  1 
ATOM   7212  N N   . TYR   E  1 205 ? 8.99305   40.21789  37.27534  1.000 30.11855  ?  205 TYR   A N   1 
ATOM   7213  C CA  . TYR   E  1 205 ? 8.35172   41.11950  36.32344  1.000 28.07855  ?  205 TYR   A CA  1 
ATOM   7214  C C   . TYR   E  1 205 ? 8.81289   40.87339  34.88113  1.000 35.50158  ?  205 TYR   A C   1 
ATOM   7215  O O   . TYR   E  1 205 ? 8.71900   41.76516  34.02466  1.000 33.48508  ?  205 TYR   A O   1 
ATOM   7216  C CB  . TYR   E  1 205 ? 8.58327   42.58013  36.70778  1.000 35.19701  ?  205 TYR   A CB  1 
ATOM   7217  C CG  . TYR   E  1 205 ? 7.46787   43.21804  37.48717  1.000 48.90376  ?  205 TYR   A CG  1 
ATOM   7218  C CD1 . TYR   E  1 205 ? 6.70346   42.49158  38.38728  1.000 41.15477  ?  205 TYR   A CD1 1 
ATOM   7219  C CD2 . TYR   E  1 205 ? 7.16861   44.56369  37.30990  1.000 36.40733  ?  205 TYR   A CD2 1 
ATOM   7220  C CE1 . TYR   E  1 205 ? 5.66566   43.11021  39.11019  1.000 26.03242  ?  205 TYR   A CE1 1 
ATOM   7221  C CE2 . TYR   E  1 205 ? 6.14613   45.18144  38.01781  1.000 50.03283  ?  205 TYR   A CE2 1 
ATOM   7222  C CZ  . TYR   E  1 205 ? 5.39993   44.45323  38.91347  1.000 69.92666  ?  205 TYR   A CZ  1 
ATOM   7223  O OH  . TYR   E  1 205 ? 4.39760   45.08801  39.59879  1.000 40.51444  ?  205 TYR   A OH  1 
ATOM   7224  N N   . GLY   E  1 206 ? 9.31977   39.67967  34.58539  1.000 38.06849  ?  206 GLY   A N   1 
ATOM   7225  C CA  . GLY   E  1 206 ? 9.72574   39.34852  33.24026  1.000 36.95591  ?  206 GLY   A CA  1 
ATOM   7226  C C   . GLY   E  1 206 ? 11.14304  39.73213  32.87247  1.000 50.74483  ?  206 GLY   A C   1 
ATOM   7227  O O   . GLY   E  1 206 ? 11.60892  39.34294  31.79548  1.000 42.76091  ?  206 GLY   A O   1 
ATOM   7228  N N   . PHE   E  1 207 ? 11.84575  40.47842  33.71871  1.000 29.23628  ?  207 PHE   A N   1 
ATOM   7229  C CA  . PHE   E  1 207 ? 13.22778  40.82849  33.42142  1.000 41.29557  ?  207 PHE   A CA  1 
ATOM   7230  C C   . PHE   E  1 207 ? 14.12256  39.60521  33.58215  1.000 36.75958  ?  207 PHE   A C   1 
ATOM   7231  O O   . PHE   E  1 207 ? 13.92219  38.79178  34.48801  1.000 46.80129  ?  207 PHE   A O   1 
ATOM   7232  C CB  . PHE   E  1 207 ? 13.69310  41.95183  34.34466  1.000 28.63130  ?  207 PHE   A CB  1 
ATOM   7233  C CG  . PHE   E  1 207 ? 12.89607  43.21804  34.21679  1.000 44.27937  ?  207 PHE   A CG  1 
ATOM   7234  C CD1 . PHE   E  1 207 ? 13.07037  44.05000  33.11951  1.000 18.05703  ?  207 PHE   A CD1 1 
ATOM   7235  C CD2 . PHE   E  1 207 ? 11.98851  43.59335  35.20470  1.000 22.43342  ?  207 PHE   A CD2 1 
ATOM   7236  C CE1 . PHE   E  1 207 ? 12.34889  45.23003  33.00494  1.000 38.36370  ?  207 PHE   A CE1 1 
ATOM   7237  C CE2 . PHE   E  1 207 ? 11.26155  44.77959  35.09851  1.000 26.08901  ?  207 PHE   A CE2 1 
ATOM   7238  C CZ  . PHE   E  1 207 ? 11.44289  45.59485  33.99727  1.000 43.04592  ?  207 PHE   A CZ  1 
ATOM   7239  N N   . ASN   E  1 208 ? 15.11511  39.46698  32.69810  1.000 33.29028  ?  208 ASN   A N   1 
ATOM   7240  C CA  . ASN   E  1 208 ? 15.98116  38.29042  32.72229  1.000 55.80365  ?  208 ASN   A CA  1 
ATOM   7241  C C   . ASN   E  1 208 ? 17.28254  38.48759  33.49123  1.000 25.42813  ?  208 ASN   A C   1 
ATOM   7242  O O   . ASN   E  1 208 ? 18.10241  37.55908  33.53517  1.000 83.60254  ?  208 ASN   A O   1 
ATOM   7243  C CB  . ASN   E  1 208 ? 16.29776  37.80857  31.29824  1.000 25.87814  ?  208 ASN   A CB  1 
ATOM   7244  C CG  . ASN   E  1 208 ? 16.61680  38.92469  30.35340  1.000 82.34734  ?  208 ASN   A CG  1 
ATOM   7245  O OD1 . ASN   E  1 208 ? 17.59671  39.66004  30.53481  1.000 137.39651 ?  208 ASN   A OD1 1 
ATOM   7246  N ND2 . ASN   E  1 208 ? 15.80856  39.04273  29.30442  1.000 59.32288  ?  208 ASN   A ND2 1 
ATOM   7247  N N   . SER   E  1 209 ? 17.47951  39.64615  34.11699  1.000 47.71845  ?  209 SER   A N   1 
ATOM   7248  C CA  . SER   E  1 209 ? 18.66800  39.94095  34.91409  1.000 31.18249  ?  209 SER   A CA  1 
ATOM   7249  C C   . SER   E  1 209 ? 18.44890  41.28700  35.56989  1.000 53.32986  ?  209 SER   A C   1 
ATOM   7250  O O   . SER   E  1 209 ? 17.51087  42.01622  35.23183  1.000 28.56279  ?  209 SER   A O   1 
ATOM   7251  C CB  . SER   E  1 209 ? 19.95172  40.00803  34.08617  1.000 42.17506  ?  209 SER   A CB  1 
ATOM   7252  O OG  . SER   E  1 209 ? 19.92176  41.16027  33.26019  1.000 21.49895  ?  209 SER   A OG  1 
ATOM   7253  N N   . TYR   E  1 210 ? 19.35589  41.62876  36.48683  1.000 34.40576  ?  210 TYR   A N   1 
ATOM   7254  C CA  . TYR   E  1 210 ? 19.25804  42.93513  37.12081  1.000 22.51908  ?  210 TYR   A CA  1 
ATOM   7255  C C   . TYR   E  1 210 ? 19.50461  44.05020  36.11047  1.000 35.52741  ?  210 TYR   A C   1 
ATOM   7256  O O   . TYR   E  1 210 ? 18.75830  45.03645  36.06807  1.000 28.47370  ?  210 TYR   A O   1 
ATOM   7257  C CB  . TYR   E  1 210 ? 20.23375  43.03025  38.29289  1.000 11.92377  ?  210 TYR   A CB  1 
ATOM   7258  C CG  . TYR   E  1 210 ? 20.28022  44.41444  38.87290  1.000 44.99706  ?  210 TYR   A CG  1 
ATOM   7259  C CD1 . TYR   E  1 210 ? 19.27244  44.85949  39.71796  1.000 22.01963  ?  210 TYR   A CD1 1 
ATOM   7260  C CD2 . TYR   E  1 210 ? 21.30557  45.29296  38.54757  1.000 37.43319  ?  210 TYR   A CD2 1 
ATOM   7261  C CE1 . TYR   E  1 210 ? 19.27930  46.14317  40.24139  1.000 25.64242  ?  210 TYR   A CE1 1 
ATOM   7262  C CE2 . TYR   E  1 210 ? 21.32684  46.57805  39.06463  1.000 39.20286  ?  210 TYR   A CE2 1 
ATOM   7263  C CZ  . TYR   E  1 210 ? 20.31053  46.99144  39.91197  1.000 48.19805  ?  210 TYR   A CZ  1 
ATOM   7264  O OH  . TYR   E  1 210 ? 20.32460  48.25171  40.43357  1.000 29.97420  ?  210 TYR   A OH  1 
ATOM   7265  N N   . ASP   E  1 211 ? 20.53724  43.89729  35.27920  1.000 29.12043  ?  211 ASP   A N   1 
ATOM   7266  C CA  . ASP   E  1 211 ? 20.83552  44.89798  34.26056  1.000 23.84419  ?  211 ASP   A CA  1 
ATOM   7267  C C   . ASP   E  1 211 ? 19.64623  45.12323  33.34211  1.000 45.23289  ?  211 ASP   A C   1 
ATOM   7268  O O   . ASP   E  1 211 ? 19.38225  46.26078  32.91998  1.000 26.11519  ?  211 ASP   A O   1 
ATOM   7269  C CB  . ASP   E  1 211 ? 22.05620  44.47651  33.43753  1.000 26.98381  ?  211 ASP   A CB  1 
ATOM   7270  C CG  . ASP   E  1 211 ? 22.42070  45.50723  32.38279  1.000 27.52711  ?  211 ASP   A CG  1 
ATOM   7271  O OD1 . ASP   E  1 211 ? 22.84105  46.62937  32.76724  1.000 32.27845  ?  211 ASP   A OD1 1 
ATOM   7272  O OD2 . ASP   E  1 211 ? 22.27802  45.20333  31.17501  1.000 50.19363  -1 211 ASP   A OD2 1 
ATOM   7273  N N   . ASP   E  1 212 ? 18.93481  44.04251  33.00078  1.000 24.92301  ?  212 ASP   A N   1 
ATOM   7274  C CA  . ASP   E  1 212 ? 17.71840  44.17146  32.20315  1.000 34.44089  ?  212 ASP   A CA  1 
ATOM   7275  C C   . ASP   E  1 212 ? 16.70367  45.08015  32.89894  1.000 26.70466  ?  212 ASP   A C   1 
ATOM   7276  O O   . ASP   E  1 212 ? 16.09374  45.95550  32.26743  1.000 27.39160  ?  212 ASP   A O   1 
ATOM   7277  C CB  . ASP   E  1 212 ? 17.13869  42.77814  31.94404  1.000 35.91947  ?  212 ASP   A CB  1 
ATOM   7278  C CG  . ASP   E  1 212 ? 15.99798  42.78197  30.93819  1.000 44.04006  ?  212 ASP   A CG  1 
ATOM   7279  O OD1 . ASP   E  1 212 ? 15.94679  43.70478  30.09603  1.000 59.04032  ?  212 ASP   A OD1 1 
ATOM   7280  O OD2 . ASP   E  1 212 ? 15.14378  41.86332  31.01228  1.000 44.91273  -1 212 ASP   A OD2 1 
ATOM   7281  N N   . PHE   E  1 213 ? 16.53436  44.90617  34.20814  1.000 16.68499  ?  213 PHE   A N   1 
ATOM   7282  C CA  . PHE   E  1 213 ? 15.62429  45.76024  34.96284  1.000 13.95521  ?  213 PHE   A CA  1 
ATOM   7283  C C   . PHE   E  1 213 ? 16.14880  47.19010  35.04519  1.000 50.86416  ?  213 PHE   A C   1 
ATOM   7284  O O   . PHE   E  1 213 ? 15.38349  48.15728  34.88423  1.000 25.36134  ?  213 PHE   A O   1 
ATOM   7285  C CB  . PHE   E  1 213 ? 15.42412  45.17391  36.36415  1.000 20.63343  ?  213 PHE   A CB  1 
ATOM   7286  C CG  . PHE   E  1 213 ? 14.88945  46.14755  37.34041  1.000 33.33299  ?  213 PHE   A CG  1 
ATOM   7287  C CD1 . PHE   E  1 213 ? 13.52407  46.42263  37.38640  1.000 36.81481  ?  213 PHE   A CD1 1 
ATOM   7288  C CD2 . PHE   E  1 213 ? 15.74385  46.80672  38.21092  1.000 21.53876  ?  213 PHE   A CD2 1 
ATOM   7289  C CE1 . PHE   E  1 213 ? 13.01687  47.34022  38.29742  1.000 46.28996  ?  213 PHE   A CE1 1 
ATOM   7290  C CE2 . PHE   E  1 213 ? 15.24575  47.72146  39.12291  1.000 49.23110  ?  213 PHE   A CE2 1 
ATOM   7291  C CZ  . PHE   E  1 213 ? 13.87901  47.99048  39.16541  1.000 38.68390  ?  213 PHE   A CZ  1 
ATOM   7292  N N   . PHE   E  1 214 ? 17.45199  47.32931  35.31873  1.000 19.03025  ?  214 PHE   A N   1 
ATOM   7293  C CA  . PHE   E  1 214 ? 18.09256  48.63601  35.42437  1.000 17.32299  ?  214 PHE   A CA  1 
ATOM   7294  C C   . PHE   E  1 214 ? 17.91386  49.45248  34.14265  1.000 16.12866  ?  214 PHE   A C   1 
ATOM   7295  O O   . PHE   E  1 214 ? 17.69206  50.67247  34.19499  1.000 43.75159  ?  214 PHE   A O   1 
ATOM   7296  C CB  . PHE   E  1 214 ? 19.57307  48.42382  35.75267  1.000 26.05716  ?  214 PHE   A CB  1 
ATOM   7297  C CG  . PHE   E  1 214 ? 20.34542  49.68982  35.98596  1.000 24.26788  ?  214 PHE   A CG  1 
ATOM   7298  C CD1 . PHE   E  1 214 ? 20.24853  50.36198  37.19321  1.000 22.80657  ?  214 PHE   A CD1 1 
ATOM   7299  C CD2 . PHE   E  1 214 ? 21.19616  50.19176  35.01014  1.000 31.70086  ?  214 PHE   A CD2 1 
ATOM   7300  C CE1 . PHE   E  1 214 ? 20.95564  51.52617  37.42168  1.000 19.25149  ?  214 PHE   A CE1 1 
ATOM   7301  C CE2 . PHE   E  1 214 ? 21.92233  51.35927  35.23401  1.000 31.09204  ?  214 PHE   A CE2 1 
ATOM   7302  C CZ  . PHE   E  1 214 ? 21.80644  52.02718  36.44707  1.000 25.01225  ?  214 PHE   A CZ  1 
ATOM   7303  N N   . ASN   E  1 215 ? 17.97836  48.79331  32.98408  1.000 21.33466  ?  215 ASN   A N   1 
ATOM   7304  C CA  . ASN   E  1 215 ? 17.82309  49.44823  31.68772  1.000 28.99337  ?  215 ASN   A CA  1 
ATOM   7305  C C   . ASN   E  1 215 ? 16.47210  49.14972  31.04179  1.000 38.77593  ?  215 ASN   A C   1 
ATOM   7306  O O   . ASN   E  1 215 ? 16.36779  49.00766  29.81981  1.000 32.51960  ?  215 ASN   A O   1 
ATOM   7307  C CB  . ASN   E  1 215 ? 18.96555  49.06268  30.75659  1.000 28.84065  ?  215 ASN   A CB  1 
ATOM   7308  C CG  . ASN   E  1 215 ? 20.25171  49.76925  31.12712  1.000 51.96256  ?  215 ASN   A CG  1 
ATOM   7309  O OD1 . ASN   E  1 215 ? 20.26298  50.97810  31.39162  1.000 30.62299  ?  215 ASN   A OD1 1 
ATOM   7310  N ND2 . ASN   E  1 215 ? 21.33585  49.01684  31.18417  1.000 27.35086  ?  215 ASN   A ND2 1 
ATOM   7311  N N   . ARG   E  1 216 ? 15.42542  49.06389  31.86785  1.000 19.12657  ?  216 ARG   A N   1 
ATOM   7312  C CA  . ARG   E  1 216 ? 14.07695  48.82640  31.38167  1.000 28.00726  ?  216 ARG   A CA  1 
ATOM   7313  C C   . ARG   E  1 216 ? 13.65728  49.91437  30.39273  1.000 51.05061  ?  216 ARG   A C   1 
ATOM   7314  O O   . ARG   E  1 216 ? 13.99569  51.09102  30.55248  1.000 27.23501  ?  216 ARG   A O   1 
ATOM   7315  C CB  . ARG   E  1 216 ? 13.12102  48.77989  32.57327  1.000 24.29013  ?  216 ARG   A CB  1 
ATOM   7316  C CG  . ARG   E  1 216 ? 13.07079  50.07218  33.35652  1.000 23.58144  ?  216 ARG   A CG  1 
ATOM   7317  C CD  . ARG   E  1 216 ? 12.34683  49.90118  34.66798  1.000 33.89545  ?  216 ARG   A CD  1 
ATOM   7318  N NE  . ARG   E  1 216 ? 12.48660  51.08271  35.51451  1.000 22.83577  ?  216 ARG   A NE  1 
ATOM   7319  C CZ  . ARG   E  1 216 ? 13.55225  51.32901  36.26547  1.000 47.61489  ?  216 ARG   A CZ  1 
ATOM   7320  N NH1 . ARG   E  1 216 ? 14.57539  50.48649  36.31034  1.000 26.42803  ?  216 ARG   A NH1 1 
ATOM   7321  N NH2 . ARG   E  1 216 ? 13.59776  52.44898  36.98084  1.000 30.91239  ?  216 ARG   A NH2 1 
ATOM   7322  N N   . ARG   E  1 217 ? 12.82856  49.51632  29.44756  1.000 31.24807  ?  217 ARG   A N   1 
ATOM   7323  C CA  . ARG   E  1 217 ? 12.40206  50.40491  28.38683  1.000 27.59298  ?  217 ARG   A CA  1 
ATOM   7324  C C   . ARG   E  1 217 ? 11.05504  51.03684  28.74492  1.000 110.19978 ?  217 ARG   A C   1 
ATOM   7325  O O   . ARG   E  1 217 ? 10.32589  50.56365  29.62296  1.000 19.41402  ?  217 ARG   A O   1 
ATOM   7326  C CB  . ARG   E  1 217 ? 12.33790  49.62930  27.06454  1.000 30.38851  ?  217 ARG   A CB  1 
ATOM   7327  C CG  . ARG   E  1 217 ? 13.46215  48.63963  26.86369  1.000 56.22197  ?  217 ARG   A CG  1 
ATOM   7328  C CD  . ARG   E  1 217 ? 13.27790  47.86691  25.58047  1.000 30.68802  ?  217 ARG   A CD  1 
ATOM   7329  N NE  . ARG   E  1 217 ? 13.93715  48.50835  24.44841  1.000 45.14691  ?  217 ARG   A NE  1 
ATOM   7330  C CZ  . ARG   E  1 217 ? 15.09277  48.09375  23.91566  1.000 22.64632  ?  217 ARG   A CZ  1 
ATOM   7331  N NH1 . ARG   E  1 217 ? 15.69818  46.98666  24.33585  1.000 33.17975  ?  217 ARG   A NH1 1 
ATOM   7332  N NH2 . ARG   E  1 217 ? 15.67416  48.82041  22.95370  1.000 77.39990  ?  217 ARG   A NH2 1 
ATOM   7333  N N   . PHE   E  1 218 ? 10.73723  52.15391  28.08418  1.000 35.64264  ?  218 PHE   A N   1 
ATOM   7334  C CA  . PHE   E  1 218 ? 9.39208   52.68919  28.28842  1.000 24.51047  ?  218 PHE   A CA  1 
ATOM   7335  C C   . PHE   E  1 218 ? 8.37717   51.86566  27.49849  1.000 54.96077  ?  218 PHE   A C   1 
ATOM   7336  O O   . PHE   E  1 218 ? 8.61673   51.51625  26.33975  1.000 26.72155  ?  218 PHE   A O   1 
ATOM   7337  C CB  . PHE   E  1 218 ? 9.30944   54.14715  27.85182  1.000 15.36140  ?  218 PHE   A CB  1 
ATOM   7338  C CG  . PHE   E  1 218 ? 10.00862  55.10161  28.77017  1.000 35.01721  ?  218 PHE   A CG  1 
ATOM   7339  C CD1 . PHE   E  1 218 ? 9.59878   55.24199  30.09917  1.000 17.02931  ?  218 PHE   A CD1 1 
ATOM   7340  C CD2 . PHE   E  1 218 ? 11.07011  55.88128  28.30039  1.000 25.68998  ?  218 PHE   A CD2 1 
ATOM   7341  C CE1 . PHE   E  1 218 ? 10.23769  56.13736  30.95303  1.000 42.27917  ?  218 PHE   A CE1 1 
ATOM   7342  C CE2 . PHE   E  1 218 ? 11.71679  56.77285  29.14163  1.000 24.95717  ?  218 PHE   A CE2 1 
ATOM   7343  C CZ  . PHE   E  1 218 ? 11.29986  56.90156  30.47453  1.000 18.21277  ?  218 PHE   A CZ  1 
ATOM   7344  N N   . ARG   E  1 219 ? 7.23255   51.56434  28.11533  1.000 34.90262  ?  219 ARG   A N   1 
ATOM   7345  C CA  . ARG   E  1 219 ? 6.18800   50.84069  27.39445  1.000 39.23394  ?  219 ARG   A CA  1 
ATOM   7346  C C   . ARG   E  1 219 ? 5.54801   51.70457  26.31753  1.000 36.17315  ?  219 ARG   A C   1 
ATOM   7347  O O   . ARG   E  1 219 ? 5.13826   51.19692  25.26897  1.000 34.70911  ?  219 ARG   A O   1 
ATOM   7348  C CB  . ARG   E  1 219 ? 5.10889   50.35172  28.35666  1.000 32.02114  ?  219 ARG   A CB  1 
ATOM   7349  C CG  . ARG   E  1 219 ? 4.08877   49.45720  27.64504  1.000 48.46085  ?  219 ARG   A CG  1 
ATOM   7350  C CD  . ARG   E  1 219 ? 2.91426   49.09215  28.52048  1.000 38.36500  ?  219 ARG   A CD  1 
ATOM   7351  N NE  . ARG   E  1 219 ? 3.30549   48.27274  29.65889  1.000 24.49198  ?  219 ARG   A NE  1 
ATOM   7352  C CZ  . ARG   E  1 219 ? 3.67234   47.00183  29.56551  1.000 92.39900  ?  219 ARG   A CZ  1 
ATOM   7353  N NH1 . ARG   E  1 219 ? 3.70222   46.37133  28.40413  1.000 24.74602  ?  219 ARG   A NH1 1 
ATOM   7354  N NH2 . ARG   E  1 219 ? 4.02176   46.34536  30.66404  1.000 16.56151  ?  219 ARG   A NH2 1 
ATOM   7355  N N   . ASN   E  1 220 ? 5.45369   53.00486  26.55617  1.000 31.24087  ?  220 ASN   A N   1 
ATOM   7356  C CA  . ASN   E  1 220 ? 4.74777   53.88376  25.64301  1.000 37.28783  ?  220 ASN   A CA  1 
ATOM   7357  C C   . ASN   E  1 220 ? 5.20181   55.31508  25.89023  1.000 34.17578  ?  220 ASN   A C   1 
ATOM   7358  O O   . ASN   E  1 220 ? 4.54077   56.06563  26.62283  1.000 39.61787  ?  220 ASN   A O   1 
ATOM   7359  C CB  . ASN   E  1 220 ? 3.23850   53.73892  25.84821  1.000 45.19919  ?  220 ASN   A CB  1 
ATOM   7360  C CG  . ASN   E  1 220 ? 2.43030   54.37737  24.73991  1.000 70.48217  ?  220 ASN   A CG  1 
ATOM   7361  O OD1 . ASN   E  1 220 ? 2.91920   55.23345  23.99227  1.000 45.73029  ?  220 ASN   A OD1 1 
ATOM   7362  N ND2 . ASN   E  1 220 ? 1.17790   53.96752  24.63131  1.000 47.01493  ?  220 ASN   A ND2 1 
ATOM   7363  N N   . ARG   E  1 221 ? 6.32761   55.70474  25.28623  1.000 34.88246  ?  221 ARG   A N   1 
ATOM   7364  C CA  . ARG   E  1 221 ? 6.88644   57.01928  25.59309  1.000 38.22452  ?  221 ARG   A CA  1 
ATOM   7365  C C   . ARG   E  1 221 ? 5.93508   58.14447  25.19468  1.000 46.91513  ?  221 ARG   A C   1 
ATOM   7366  O O   . ARG   E  1 221 ? 5.91763   59.18696  25.85545  1.000 36.84803  ?  221 ARG   A O   1 
ATOM   7367  C CB  . ARG   E  1 221 ? 8.26041   57.19178  24.92762  1.000 25.70076  ?  221 ARG   A CB  1 
ATOM   7368  C CG  . ARG   E  1 221 ? 8.24119   57.26169  23.39604  1.000 26.22514  ?  221 ARG   A CG  1 
ATOM   7369  C CD  . ARG   E  1 221 ? 8.31386   58.70726  22.88119  1.000 37.92463  ?  221 ARG   A CD  1 
ATOM   7370  N NE  . ARG   E  1 221 ? 8.22475   58.77135  21.42359  1.000 32.95504  ?  221 ARG   A NE  1 
ATOM   7371  C CZ  . ARG   E  1 221 ? 9.26011   58.71558  20.59182  1.000 44.48418  ?  221 ARG   A CZ  1 
ATOM   7372  N NH1 . ARG   E  1 221 ? 10.50491  58.58882  21.02753  1.000 38.85557  ?  221 ARG   A NH1 1 
ATOM   7373  N NH2 . ARG   E  1 221 ? 9.04447   58.79874  19.28673  1.000 29.57456  ?  221 ARG   A NH2 1 
ATOM   7374  N N   . ASP   E  1 222 ? 5.10850   57.94484  24.15534  1.000 33.32831  ?  222 ASP   A N   1 
ATOM   7375  C CA  . ASP   E  1 222 ? 4.18239   58.99825  23.73509  1.000 50.31113  ?  222 ASP   A CA  1 
ATOM   7376  C C   . ASP   E  1 222 ? 3.14227   59.34817  24.80338  1.000 53.03738  ?  222 ASP   A C   1 
ATOM   7377  O O   . ASP   E  1 222 ? 2.59463   60.45950  24.77969  1.000 39.86001  ?  222 ASP   A O   1 
ATOM   7378  C CB  . ASP   E  1 222 ? 3.47964   58.60485  22.43551  1.000 27.83382  ?  222 ASP   A CB  1 
ATOM   7379  C CG  . ASP   E  1 222 ? 4.46010   58.43241  21.26049  1.000 46.82593  ?  222 ASP   A CG  1 
ATOM   7380  O OD1 . ASP   E  1 222 ? 5.08428   59.42156  20.79956  1.000 53.79060  ?  222 ASP   A OD1 1 
ATOM   7381  O OD2 . ASP   E  1 222 ? 4.62046   57.27706  20.82365  1.000 62.92460  -1 222 ASP   A OD2 1 
ATOM   7382  N N   . ILE   E  1 223 ? 2.86657   58.45162  25.74949  1.000 22.96644  ?  223 ILE   A N   1 
ATOM   7383  C CA  . ILE   E  1 223 ? 2.03652   58.82819  26.89104  1.000 32.52266  ?  223 ILE   A CA  1 
ATOM   7384  C C   . ILE   E  1 223 ? 2.88104   59.48516  27.98122  1.000 43.73153  ?  223 ILE   A C   1 
ATOM   7385  O O   . ILE   E  1 223 ? 2.62698   60.62730  28.38227  1.000 46.25851  ?  223 ILE   A O   1 
ATOM   7386  C CB  . ILE   E  1 223 ? 1.26683   57.60251  27.42103  1.000 45.15180  ?  223 ILE   A CB  1 
ATOM   7387  C CG1 . ILE   E  1 223 ? 0.21261   57.15752  26.41162  1.000 26.16848  ?  223 ILE   A CG1 1 
ATOM   7388  C CG2 . ILE   E  1 223 ? 0.59391   57.89923  28.74960  1.000 13.95692  ?  223 ILE   A CG2 1 
ATOM   7389  C CD1 . ILE   E  1 223 ? -0.43258  55.86003  26.79961  1.000 29.19680  ?  223 ILE   A CD1 1 
ATOM   7390  N N   . ASP   E  1 224 ? 3.91989   58.78312  28.44990  1.000 32.93504  ?  224 ASP   A N   1 
ATOM   7391  C CA  . ASP   E  1 224 ? 4.63670   59.14836  29.67196  1.000 34.04058  ?  224 ASP   A CA  1 
ATOM   7392  C C   . ASP   E  1 224 ? 5.79736   60.12332  29.48022  1.000 34.91734  ?  224 ASP   A C   1 
ATOM   7393  O O   . ASP   E  1 224 ? 6.06941   60.92105  30.38728  1.000 30.50906  ?  224 ASP   A O   1 
ATOM   7394  C CB  . ASP   E  1 224 ? 5.16370   57.88466  30.34360  1.000 29.95069  ?  224 ASP   A CB  1 
ATOM   7395  C CG  . ASP   E  1 224 ? 4.06697   56.88392  30.62193  1.000 43.31934  ?  224 ASP   A CG  1 
ATOM   7396  O OD1 . ASP   E  1 224 ? 3.19876   57.20042  31.46131  1.000 46.44951  ?  224 ASP   A OD1 1 
ATOM   7397  O OD2 . ASP   E  1 224 ? 4.07069   55.80210  29.99135  1.000 42.97137  -1 224 ASP   A OD2 1 
ATOM   7398  N N   . ARG   E  1 225 ? 6.51147   60.06580  28.35611  1.000 43.33626  ?  225 ARG   A N   1 
ATOM   7399  C CA  . ARG   E  1 225 ? 7.68972   60.90875  28.11762  1.000 34.01018  ?  225 ARG   A CA  1 
ATOM   7400  C C   . ARG   E  1 225 ? 7.69729   61.32707  26.65728  1.000 49.10841  ?  225 ARG   A C   1 
ATOM   7401  O O   . ARG   E  1 225 ? 8.55680   60.91112  25.86964  1.000 43.14573  ?  225 ARG   A O   1 
ATOM   7402  C CB  . ARG   E  1 225 ? 8.97881   60.16194  28.48190  1.000 35.06215  ?  225 ARG   A CB  1 
ATOM   7403  C CG  . ARG   E  1 225 ? 9.32516   59.95547  29.91135  1.000 15.38190  ?  225 ARG   A CG  1 
ATOM   7404  C CD  . ARG   E  1 225 ? 9.36468   61.34549  30.58472  1.000 13.51046  ?  225 ARG   A CD  1 
ATOM   7405  N NE  . ARG   E  1 225 ? 9.63413   61.23452  32.01833  1.000 45.96409  ?  225 ARG   A NE  1 
ATOM   7406  C CZ  . ARG   E  1 225 ? 8.70418   61.32723  32.96415  1.000 26.89457  ?  225 ARG   A CZ  1 
ATOM   7407  N NH1 . ARG   E  1 225 ? 7.43278   61.51790  32.65834  1.000 49.63002  ?  225 ARG   A NH1 1 
ATOM   7408  N NH2 . ARG   E  1 225 ? 9.06212   61.23653  34.25281  1.000 10.58062  ?  225 ARG   A NH2 1 
ATOM   7409  N N   . PRO   E  1 226 ? 6.72855   62.13760  26.24865  1.000 38.90211  ?  226 PRO   A N   1 
ATOM   7410  C CA  . PRO   E  1 226 ? 6.60524   62.47242  24.82373  1.000 20.70432  ?  226 PRO   A CA  1 
ATOM   7411  C C   . PRO   E  1 226 ? 7.75291   63.34285  24.33888  1.000 45.24071  ?  226 PRO   A C   1 
ATOM   7412  O O   . PRO   E  1 226 ? 8.30769   64.15393  25.08288  1.000 28.47204  ?  226 PRO   A O   1 
ATOM   7413  C CB  . PRO   E  1 226 ? 5.27831   63.24107  24.75290  1.000 19.81955  ?  226 PRO   A CB  1 
ATOM   7414  C CG  . PRO   E  1 226 ? 5.09402   63.80803  26.15692  1.000 18.59631  ?  226 PRO   A CG  1 
ATOM   7415  C CD  . PRO   E  1 226 ? 5.68333   62.77315  27.07983  1.000 21.79885  ?  226 PRO   A CD  1 
ATOM   7416  N N   . VAL   E  1 227 ? 8.09364   63.17298  23.06197  1.000 25.91504  ?  227 VAL   A N   1 
ATOM   7417  C CA  . VAL   E  1 227 ? 9.01490   64.07143  22.37680  1.000 22.93897  ?  227 VAL   A CA  1 
ATOM   7418  C C   . VAL   E  1 227 ? 8.30320   65.40306  22.17907  1.000 35.37496  ?  227 VAL   A C   1 
ATOM   7419  O O   . VAL   E  1 227 ? 7.65659   65.62055  21.14833  1.000 36.36538  ?  227 VAL   A O   1 
ATOM   7420  C CB  . VAL   E  1 227 ? 9.48541   63.47699  21.03489  1.000 26.11076  ?  227 VAL   A CB  1 
ATOM   7421  C CG1 . VAL   E  1 227 ? 10.49006  64.39328  20.34796  1.000 27.26944  ?  227 VAL   A CG1 1 
ATOM   7422  C CG2 . VAL   E  1 227 ? 10.08521  62.09711  21.25825  1.000 21.33471  ?  227 VAL   A CG2 1 
ATOM   7423  N N   . VAL   E  1 228 ? 8.42355   66.29682  23.17037  1.000 26.93670  ?  228 VAL   A N   1 
ATOM   7424  C CA  . VAL   E  1 228 ? 7.61129   67.50781  23.23674  1.000 14.52856  ?  228 VAL   A CA  1 
ATOM   7425  C C   . VAL   E  1 228 ? 7.77028   68.33548  21.97136  1.000 54.81422  ?  228 VAL   A C   1 
ATOM   7426  O O   . VAL   E  1 228 ? 8.88718   68.60485  21.51509  1.000 25.08526  ?  228 VAL   A O   1 
ATOM   7427  C CB  . VAL   E  1 228 ? 7.98335   68.30851  24.49165  1.000 32.94506  ?  228 VAL   A CB  1 
ATOM   7428  C CG1 . VAL   E  1 228 ? 7.16992   69.58914  24.57285  1.000 19.33956  ?  228 VAL   A CG1 1 
ATOM   7429  C CG2 . VAL   E  1 228 ? 7.77750   67.44008  25.72903  1.000 13.95442  ?  228 VAL   A CG2 1 
ATOM   7430  N N   . GLY   E  1 229 ? 6.63778   68.74375  21.39695  1.000 36.76771  ?  229 GLY   A N   1 
ATOM   7431  C CA  . GLY   E  1 229 ? 6.61917   69.48310  20.15096  1.000 20.67393  ?  229 GLY   A CA  1 
ATOM   7432  C C   . GLY   E  1 229 ? 6.71819   68.63241  18.90245  1.000 27.69036  ?  229 GLY   A C   1 
ATOM   7433  O O   . GLY   E  1 229 ? 6.55188   69.16359  17.79087  1.000 42.89205  ?  229 GLY   A O   1 
ATOM   7434  N N   . GLY   E  1 230 ? 7.00000   67.34406  19.04741  1.000 35.61090  ?  230 GLY   A N   1 
ATOM   7435  C CA  . GLY   E  1 230 ? 7.06538   66.39535  17.94236  1.000 8.25524   ?  230 GLY   A CA  1 
ATOM   7436  C C   . GLY   E  1 230 ? 8.41037   66.39078  17.23940  1.000 54.22015  ?  230 GLY   A C   1 
ATOM   7437  O O   . GLY   E  1 230 ? 9.08406   67.41590  17.09893  1.000 24.22758  ?  230 GLY   A O   1 
ATOM   7438  N N   . VAL   E  1 231 ? 8.78794   65.20052  16.75994  1.000 20.37503  ?  231 VAL   A N   1 
ATOM   7439  C CA  . VAL   E  1 231 ? 10.06338  64.97206  16.09008  1.000 60.71958  ?  231 VAL   A CA  1 
ATOM   7440  C C   . VAL   E  1 231 ? 10.26478  65.90697  14.90210  1.000 20.58346  ?  231 VAL   A C   1 
ATOM   7441  O O   . VAL   E  1 231 ? 11.40761  66.17818  14.51027  1.000 55.69654  ?  231 VAL   A O   1 
ATOM   7442  C CB  . VAL   E  1 231 ? 10.13785  63.48967  15.67838  1.000 13.18235  ?  231 VAL   A CB  1 
ATOM   7443  C CG1 . VAL   E  1 231 ? 8.96442   63.15142  14.80823  1.000 67.98923  ?  231 VAL   A CG1 1 
ATOM   7444  C CG2 . VAL   E  1 231 ? 11.40157  63.18900  14.93652  1.000 40.53740  ?  231 VAL   A CG2 1 
ATOM   7445  N N   . ASN   E  1 232 ? 9.18163   66.46371  14.35893  1.000 42.76848  ?  232 ASN   A N   1 
ATOM   7446  C CA  . ASN   E  1 232 ? 9.26742   67.32660  13.18354  1.000 31.74476  ?  232 ASN   A CA  1 
ATOM   7447  C C   . ASN   E  1 232 ? 9.69116   68.75678  13.49406  1.000 43.42804  ?  232 ASN   A C   1 
ATOM   7448  O O   . ASN   E  1 232 ? 10.10448  69.46981  12.57182  1.000 38.63592  ?  232 ASN   A O   1 
ATOM   7449  C CB  . ASN   E  1 232 ? 7.92646   67.36460  12.46209  1.000 48.48888  ?  232 ASN   A CB  1 
ATOM   7450  C CG  . ASN   E  1 232 ? 7.78133   66.24793  11.46289  1.000 48.11007  ?  232 ASN   A CG  1 
ATOM   7451  O OD1 . ASN   E  1 232 ? 8.55261   65.27972  11.48255  1.000 49.11553  ?  232 ASN   A OD1 1 
ATOM   7452  N ND2 . ASN   E  1 232 ? 6.79478   66.37041  10.57438  1.000 124.24242 ?  232 ASN   A ND2 1 
ATOM   7453  N N   . ASN   E  1 233 ? 9.57552   69.21000  14.74230  1.000 25.95735  ?  233 ASN   A N   1 
ATOM   7454  C CA  . ASN   E  1 233 ? 10.00678  70.55266  15.10968  1.000 33.65663  ?  233 ASN   A CA  1 
ATOM   7455  C C   . ASN   E  1 233 ? 11.48833  70.46690  15.46997  1.000 86.12523  ?  233 ASN   A C   1 
ATOM   7456  O O   . ASN   E  1 233 ? 11.85547  69.94747  16.53599  1.000 31.40484  ?  233 ASN   A O   1 
ATOM   7457  C CB  . ASN   E  1 233 ? 9.16982   71.08844  16.26976  1.000 13.57032  ?  233 ASN   A CB  1 
ATOM   7458  C CG  . ASN   E  1 233 ? 9.47912   72.53451  16.58899  1.000 50.96041  ?  233 ASN   A CG  1 
ATOM   7459  O OD1 . ASN   E  1 233 ? 10.58319  73.02537  16.33806  1.000 44.02326  ?  233 ASN   A OD1 1 
ATOM   7460  N ND2 . ASN   E  1 233 ? 8.50572   73.22484  17.16134  1.000 39.70992  ?  233 ASN   A ND2 1 
ATOM   7461  N N   . THR   E  1 234 ? 12.34639  70.94815  14.57621  1.000 25.46082  ?  234 THR   A N   1 
ATOM   7462  C CA  . THR   E  1 234 ? 13.78077  70.80837  14.78709  1.000 40.79527  ?  234 THR   A CA  1 
ATOM   7463  C C   . THR   E  1 234 ? 14.38268  72.00553  15.50981  1.000 21.02940  ?  234 THR   A C   1 
ATOM   7464  O O   . THR   E  1 234 ? 15.60469  72.06484  15.67784  1.000 71.52706  ?  234 THR   A O   1 
ATOM   7465  C CB  . THR   E  1 234 ? 14.50175  70.55435  13.45648  1.000 26.69182  ?  234 THR   A CB  1 
ATOM   7466  O OG1 . THR   E  1 234 ? 14.44033  71.71470  12.62617  1.000 36.87561  ?  234 THR   A OG1 1 
ATOM   7467  C CG2 . THR   E  1 234 ? 13.86814  69.38432  12.72412  1.000 16.67990  ?  234 THR   A CG2 1 
ATOM   7468  N N   . THR   E  1 235 ? 13.54954  72.92541  15.98411  1.000 44.60965  ?  235 THR   A N   1 
ATOM   7469  C CA  . THR   E  1 235 ? 14.01662  74.04693  16.78381  1.000 26.82006  ?  235 THR   A CA  1 
ATOM   7470  C C   . THR   E  1 235 ? 14.12881  73.70913  18.26356  1.000 46.92443  ?  235 THR   A C   1 
ATOM   7471  O O   . THR   E  1 235 ? 14.49845  74.58664  19.05502  1.000 30.18031  ?  235 THR   A O   1 
ATOM   7472  C CB  . THR   E  1 235 ? 13.07412  75.23797  16.60474  1.000 61.97045  ?  235 THR   A CB  1 
ATOM   7473  O OG1 . THR   E  1 235 ? 11.90153  75.06124  17.42169  1.000 23.15979  ?  235 THR   A OG1 1 
ATOM   7474  C CG2 . THR   E  1 235 ? 12.64555  75.33328  15.15964  1.000 33.12825  ?  235 THR   A CG2 1 
ATOM   7475  N N   . LEU   E  1 236 ? 13.82661  72.46762  18.65383  1.000 42.27008  ?  236 LEU   A N   1 
ATOM   7476  C CA  . LEU   E  1 236 ? 13.77464  72.06157  20.05381  1.000 42.74172  ?  236 LEU   A CA  1 
ATOM   7477  C C   . LEU   E  1 236 ? 14.84733  71.02449  20.33013  1.000 36.35996  ?  236 LEU   A C   1 
ATOM   7478  O O   . LEU   E  1 236 ? 15.11261  70.15520  19.49217  1.000 38.07825  ?  236 LEU   A O   1 
ATOM   7479  C CB  . LEU   E  1 236 ? 12.41120  71.47638  20.41762  1.000 36.26800  ?  236 LEU   A CB  1 
ATOM   7480  C CG  . LEU   E  1 236 ? 11.22323  72.34030  20.00258  1.000 43.56109  ?  236 LEU   A CG  1 
ATOM   7481  C CD1 . LEU   E  1 236 ? 9.93904   71.50984  20.03165  1.000 35.51193  ?  236 LEU   A CD1 1 
ATOM   7482  C CD2 . LEU   E  1 236 ? 11.13633  73.58061  20.89213  1.000 25.98757  ?  236 LEU   A CD2 1 
ATOM   7483  N N   . ILE   E  1 237 ? 15.46289  71.12440  21.50649  1.000 33.22044  ?  237 ILE   A N   1 
ATOM   7484  C CA  . ILE   E  1 237 ? 16.46132  70.16464  21.96286  1.000 26.54696  ?  237 ILE   A CA  1 
ATOM   7485  C C   . ILE   E  1 237 ? 15.90861  69.47431  23.20270  1.000 37.78336  ?  237 ILE   A C   1 
ATOM   7486  O O   . ILE   E  1 237 ? 15.54513  70.14234  24.18798  1.000 24.70636  ?  237 ILE   A O   1 
ATOM   7487  C CB  . ILE   E  1 237 ? 17.81769  70.82987  22.25727  1.000 25.37018  ?  237 ILE   A CB  1 
ATOM   7488  C CG1 . ILE   E  1 237 ? 18.34946  71.55115  21.01252  1.000 22.29260  ?  237 ILE   A CG1 1 
ATOM   7489  C CG2 . ILE   E  1 237 ? 18.82559  69.77004  22.72843  1.000 23.23949  ?  237 ILE   A CG2 1 
ATOM   7490  C CD1 . ILE   E  1 237 ? 19.71345  72.22039  21.20078  1.000 24.18737  ?  237 ILE   A CD1 1 
ATOM   7491  N N   . SER   E  1 238 ? 15.86324  68.13540  23.15339  1.000 21.14863  ?  238 SER   A N   1 
ATOM   7492  C CA  . SER   E  1 238 ? 15.29089  67.30911  24.21446  1.000 27.91764  ?  238 SER   A CA  1 
ATOM   7493  C C   . SER   E  1 238 ? 16.33077  66.90790  25.25100  1.000 36.66365  ?  238 SER   A C   1 
ATOM   7494  O O   . SER   E  1 238 ? 17.51813  66.75962  24.94753  1.000 21.63583  ?  238 SER   A O   1 
ATOM   7495  C CB  . SER   E  1 238 ? 14.66599  66.03248  23.64290  1.000 26.38019  ?  238 SER   A CB  1 
ATOM   7496  O OG  . SER   E  1 238 ? 13.34070  66.26369  23.21360  1.000 40.16150  ?  238 SER   A OG  1 
ATOM   7497  N N   . ALA   E  1 239 ? 15.85547  66.69493  26.47776  1.000 39.56176  ?  239 ALA   A N   1 
ATOM   7498  C CA  . ALA   E  1 239 ? 16.67424  66.09310  27.52278  1.000 47.61696  ?  239 ALA   A CA  1 
ATOM   7499  C C   . ALA   E  1 239 ? 17.05912  64.67102  27.14763  1.000 23.81748  ?  239 ALA   A C   1 
ATOM   7500  O O   . ALA   E  1 239 ? 16.19701  63.86174  26.80150  1.000 39.25021  ?  239 ALA   A O   1 
ATOM   7501  C CB  . ALA   E  1 239 ? 15.90863  66.08492  28.83938  1.000 20.19219  ?  239 ALA   A CB  1 
ATOM   7502  N N   . ALA   E  1 240 ? 18.35580  64.35234  27.25150  1.000 36.16753  ?  240 ALA   A N   1 
ATOM   7503  C CA  . ALA   E  1 240 ? 18.83329  63.02670  26.85282  1.000 29.78710  ?  240 ALA   A CA  1 
ATOM   7504  C C   . ALA   E  1 240 ? 18.63861  61.96225  27.92673  1.000 36.25671  ?  240 ALA   A C   1 
ATOM   7505  O O   . ALA   E  1 240 ? 18.63039  60.76620  27.60113  1.000 31.57221  ?  240 ALA   A O   1 
ATOM   7506  C CB  . ALA   E  1 240 ? 20.31379  63.08412  26.47771  1.000 21.51709  ?  240 ALA   A CB  1 
ATOM   7507  N N   . CYS   E  1 241 ? 18.50545  62.36463  29.19177  1.000 17.49903  ?  241 CYS   A N   1 
ATOM   7508  C CA  . CYS   E  1 241 ? 18.40735  61.43336  30.30545  1.000 27.40508  ?  241 CYS   A CA  1 
ATOM   7509  C C   . CYS   E  1 241 ? 17.33495  61.91764  31.26492  1.000 27.71490  ?  241 CYS   A C   1 
ATOM   7510  O O   . CYS   E  1 241 ? 17.22573  63.12058  31.53682  1.000 26.71735  ?  241 CYS   A O   1 
ATOM   7511  C CB  . CYS   E  1 241 ? 19.73020  61.29394  31.07478  1.000 29.04256  ?  241 CYS   A CB  1 
ATOM   7512  S SG  . CYS   E  1 241 ? 21.08069  60.58514  30.11279  1.000 29.29889  ?  241 CYS   A SG  1 
ATOM   7513  N N   . GLU   E  1 242 ? 16.54041  60.96683  31.76330  1.000 30.29892  ?  242 GLU   A N   1 
ATOM   7514  C CA  . GLU   E  1 242 ? 15.68591  61.19207  32.91992  1.000 13.96673  ?  242 GLU   A CA  1 
ATOM   7515  C C   . GLU   E  1 242 ? 16.54436  61.55490  34.12629  1.000 16.86852  ?  242 GLU   A C   1 
ATOM   7516  O O   . GLU   E  1 242 ? 17.29545  60.70918  34.63121  1.000 39.44916  ?  242 GLU   A O   1 
ATOM   7517  C CB  . GLU   E  1 242 ? 14.86428  59.93551  33.20011  1.000 24.84774  ?  242 GLU   A CB  1 
ATOM   7518  C CG  . GLU   E  1 242 ? 13.88962  60.04978  34.36634  1.000 19.18083  ?  242 GLU   A CG  1 
ATOM   7519  C CD  . GLU   E  1 242 ? 12.64905  60.87570  34.04428  1.000 43.18539  ?  242 GLU   A CD  1 
ATOM   7520  O OE1 . GLU   E  1 242 ? 12.33882  61.11313  32.84112  1.000 22.66151  ?  242 GLU   A OE1 1 
ATOM   7521  O OE2 . GLU   E  1 242 ? 11.98399  61.28241  35.02431  1.000 29.20638  -1 242 GLU   A OE2 1 
ATOM   7522  N N   . SER   E  1 243 ? 16.45168  62.79161  34.60903  1.000 23.84444  ?  243 SER   A N   1 
ATOM   7523  C CA  . SER   E  1 243 ? 17.44347  63.26716  35.56683  1.000 35.32790  ?  243 SER   A CA  1 
ATOM   7524  C C   . SER   E  1 243 ? 16.87910  64.43589  36.36308  1.000 25.56007  ?  243 SER   A C   1 
ATOM   7525  O O   . SER   E  1 243 ? 15.75586  64.89696  36.13066  1.000 30.06413  ?  243 SER   A O   1 
ATOM   7526  C CB  . SER   E  1 243 ? 18.73500  63.68667  34.84395  1.000 24.55780  ?  243 SER   A CB  1 
ATOM   7527  O OG  . SER   E  1 243 ? 18.44603  64.69598  33.87958  1.000 32.05400  ?  243 SER   A OG  1 
ATOM   7528  N N   . LEU   E  1 244 ? 17.69996  64.92264  37.29643  1.000 29.50807  ?  244 LEU   A N   1 
ATOM   7529  C CA  . LEU   E  1 244 ? 17.50207  66.18975  37.98709  1.000 35.04338  ?  244 LEU   A CA  1 
ATOM   7530  C C   . LEU   E  1 244 ? 18.52769  67.20185  37.48483  1.000 32.54650  ?  244 LEU   A C   1 
ATOM   7531  O O   . LEU   E  1 244 ? 19.68941  66.84951  37.25099  1.000 38.82783  ?  244 LEU   A O   1 
ATOM   7532  C CB  . LEU   E  1 244 ? 17.64281  66.00747  39.49579  1.000 19.91137  ?  244 LEU   A CB  1 
ATOM   7533  C CG  . LEU   E  1 244 ? 16.61068  65.08958  40.14904  1.000 38.34933  ?  244 LEU   A CG  1 
ATOM   7534  C CD1 . LEU   E  1 244 ? 17.05080  64.69206  41.53819  1.000 32.31012  ?  244 LEU   A CD1 1 
ATOM   7535  C CD2 . LEU   E  1 244 ? 15.31417  65.83364  40.19415  1.000 25.53841  ?  244 LEU   A CD2 1 
ATOM   7536  N N   . SER   E  1 245 ? 18.08530  68.44054  37.27866  1.000 59.35890  ?  245 SER   A N   1 
ATOM   7537  C CA  . SER   E  1 245 ? 18.97724  69.56595  37.02491  1.000 19.98072  ?  245 SER   A CA  1 
ATOM   7538  C C   . SER   E  1 245 ? 20.13607  69.56974  38.02351  1.000 20.02635  ?  245 SER   A C   1 
ATOM   7539  O O   . SER   E  1 245 ? 19.92204  69.43848  39.23515  1.000 28.98934  ?  245 SER   A O   1 
ATOM   7540  C CB  . SER   E  1 245 ? 18.15518  70.85125  37.15200  1.000 22.72106  ?  245 SER   A CB  1 
ATOM   7541  O OG  . SER   E  1 245 ? 18.94120  71.99432  36.95395  1.000 68.29385  ?  245 SER   A OG  1 
ATOM   7542  N N   . TYR   E  1 246 ? 21.37276  69.70596  37.52683  1.000 35.27603  ?  246 TYR   A N   1 
ATOM   7543  C CA  . TYR   E  1 246 ? 22.50364  69.79890  38.45504  1.000 25.41264  ?  246 TYR   A CA  1 
ATOM   7544  C C   . TYR   E  1 246 ? 23.28507  71.10220  38.34883  1.000 27.02779  ?  246 TYR   A C   1 
ATOM   7545  O O   . TYR   E  1 246 ? 23.64854  71.68425  39.38387  1.000 30.08813  ?  246 TYR   A O   1 
ATOM   7546  C CB  . TYR   E  1 246 ? 23.47453  68.61799  38.29097  1.000 15.78496  ?  246 TYR   A CB  1 
ATOM   7547  C CG  . TYR   E  1 246 ? 24.56825  68.66029  39.33503  1.000 31.96591  ?  246 TYR   A CG  1 
ATOM   7548  C CD1 . TYR   E  1 246 ? 25.73093  69.42327  39.14483  1.000 25.07061  ?  246 TYR   A CD1 1 
ATOM   7549  C CD2 . TYR   E  1 246 ? 24.43365  67.95300  40.52403  1.000 11.17932  ?  246 TYR   A CD2 1 
ATOM   7550  C CE1 . TYR   E  1 246 ? 26.70636  69.47642  40.12084  1.000 18.80849  ?  246 TYR   A CE1 1 
ATOM   7551  C CE2 . TYR   E  1 246 ? 25.41401  67.99179  41.50632  1.000 37.47179  ?  246 TYR   A CE2 1 
ATOM   7552  C CZ  . TYR   E  1 246 ? 26.53856  68.75475  41.30137  1.000 28.49153  ?  246 TYR   A CZ  1 
ATOM   7553  O OH  . TYR   E  1 246 ? 27.48391  68.77990  42.28675  1.000 44.58905  ?  246 TYR   A OH  1 
ATOM   7554  N N   . ASN   E  1 247 ? 23.62288  71.53808  37.13506  1.000 26.27899  ?  247 ASN   A N   1 
ATOM   7555  C CA  . ASN   E  1 247 ? 24.35143  72.78415  36.92858  1.000 18.66296  ?  247 ASN   A CA  1 
ATOM   7556  C C   . ASN   E  1 247 ? 24.11146  73.24048  35.49881  1.000 25.73802  ?  247 ASN   A C   1 
ATOM   7557  O O   . ASN   E  1 247 ? 23.95970  72.41610  34.58995  1.000 28.97296  ?  247 ASN   A O   1 
ATOM   7558  C CB  . ASN   E  1 247 ? 25.85730  72.63423  37.17846  1.000 28.90100  ?  247 ASN   A CB  1 
ATOM   7559  C CG  . ASN   E  1 247 ? 26.63809  73.87950  36.77459  1.000 26.55007  ?  247 ASN   A CG  1 
ATOM   7560  O OD1 . ASN   E  1 247 ? 26.62030  74.88300  37.49115  1.000 44.02815  ?  247 ASN   A OD1 1 
ATOM   7561  N ND2 . ASN   E  1 247 ? 27.30248  73.83411  35.61050  1.000 24.99164  ?  247 ASN   A ND2 1 
ATOM   7562  N N   . VAL   E  1 248 ? 24.05224  74.56084  35.31338  1.000 25.28316  ?  248 VAL   A N   1 
ATOM   7563  C CA  . VAL   E  1 248 ? 24.17434  75.17628  33.99731  1.000 31.07438  ?  248 VAL   A CA  1 
ATOM   7564  C C   . VAL   E  1 248 ? 25.31538  76.17591  34.05557  1.000 22.60976  ?  248 VAL   A C   1 
ATOM   7565  O O   . VAL   E  1 248 ? 25.44020  76.92439  35.03065  1.000 30.11816  ?  248 VAL   A O   1 
ATOM   7566  C CB  . VAL   E  1 248 ? 22.87385  75.86632  33.55798  1.000 26.62374  ?  248 VAL   A CB  1 
ATOM   7567  C CG1 . VAL   E  1 248 ? 23.13089  76.76045  32.34150  1.000 19.41960  ?  248 VAL   A CG1 1 
ATOM   7568  C CG2 . VAL   E  1 248 ? 21.80923  74.82065  33.27106  1.000 24.71978  ?  248 VAL   A CG2 1 
ATOM   7569  N N   . SER   E  1 249 ? 26.17604  76.15823  33.04004  1.000 40.34770  ?  249 SER   A N   1 
ATOM   7570  C CA  . SER   E  1 249 ? 27.27205  77.11415  32.96994  1.000 27.71938  ?  249 SER   A CA  1 
ATOM   7571  C C   . SER   E  1 249 ? 27.27806  77.76331  31.60207  1.000 40.29878  ?  249 SER   A C   1 
ATOM   7572  O O   . SER   E  1 249 ? 27.07194  77.09312  30.58253  1.000 30.10057  ?  249 SER   A O   1 
ATOM   7573  C CB  . SER   E  1 249 ? 28.62519  76.46434  33.23893  1.000 27.30742  ?  249 SER   A CB  1 
ATOM   7574  O OG  . SER   E  1 249 ? 28.75931  76.15840  34.61321  1.000 33.00071  ?  249 SER   A OG  1 
ATOM   7575  N N   . TYR   E  1 250 ? 27.50871  79.07101  31.59142  1.000 24.28273  ?  250 TYR   A N   1 
ATOM   7576  C CA  . TYR   E  1 250 ? 27.62755  79.83635  30.36477  1.000 50.42976  ?  250 TYR   A CA  1 
ATOM   7577  C C   . TYR   E  1 250 ? 29.07268  80.27055  30.17491  1.000 21.68345  ?  250 TYR   A C   1 
ATOM   7578  O O   . TYR   E  1 250 ? 29.85451  80.34109  31.13615  1.000 30.79139  ?  250 TYR   A O   1 
ATOM   7579  C CB  . TYR   E  1 250 ? 26.70792  81.06025  30.39449  1.000 21.11511  ?  250 TYR   A CB  1 
ATOM   7580  C CG  . TYR   E  1 250 ? 25.25325  80.72639  30.56604  1.000 36.65069  ?  250 TYR   A CG  1 
ATOM   7581  C CD1 . TYR   E  1 250 ? 24.47984  80.33186  29.47621  1.000 23.03085  ?  250 TYR   A CD1 1 
ATOM   7582  C CD2 . TYR   E  1 250 ? 24.65003  80.78817  31.81183  1.000 19.14906  ?  250 TYR   A CD2 1 
ATOM   7583  C CE1 . TYR   E  1 250 ? 23.12405  80.01736  29.62846  1.000 34.88156  ?  250 TYR   A CE1 1 
ATOM   7584  C CE2 . TYR   E  1 250 ? 23.30961  80.47796  31.97273  1.000 30.23164  ?  250 TYR   A CE2 1 
ATOM   7585  C CZ  . TYR   E  1 250 ? 22.54454  80.09345  30.88327  1.000 42.13768  ?  250 TYR   A CZ  1 
ATOM   7586  O OH  . TYR   E  1 250 ? 21.19942  79.77989  31.04481  1.000 47.65675  ?  250 TYR   A OH  1 
ATOM   7587  N N   . ASP   E  1 251 ? 29.41093  80.55367  28.91260  1.000 29.97541  ?  251 ASP   A N   1 
ATOM   7588  C CA  . ASP   E  1 251 ? 30.73871  81.02627  28.52930  1.000 30.23364  ?  251 ASP   A CA  1 
ATOM   7589  C C   . ASP   E  1 251 ? 31.82429  80.10416  29.09232  1.000 48.88763  ?  251 ASP   A C   1 
ATOM   7590  O O   . ASP   E  1 251 ? 32.71205  80.51572  29.84424  1.000 33.75388  ?  251 ASP   A O   1 
ATOM   7591  C CB  . ASP   E  1 251 ? 30.93912  82.46701  29.00345  1.000 29.56459  ?  251 ASP   A CB  1 
ATOM   7592  C CG  . ASP   E  1 251 ? 32.17125  83.11716  28.40762  1.000 51.77472  ?  251 ASP   A CG  1 
ATOM   7593  O OD1 . ASP   E  1 251 ? 32.40740  82.91001  27.19515  1.000 38.20791  ?  251 ASP   A OD1 1 
ATOM   7594  O OD2 . ASP   E  1 251 ? 32.88239  83.84118  29.15458  1.000 37.75070  -1 251 ASP   A OD2 1 
ATOM   7595  N N   . VAL   E  1 252 ? 31.71722  78.82171  28.74688  1.000 29.71692  ?  252 VAL   A N   1 
ATOM   7596  C CA  . VAL   E  1 252 ? 32.64450  77.83376  29.28929  1.000 32.00602  ?  252 VAL   A CA  1 
ATOM   7597  C C   . VAL   E  1 252 ? 33.99330  77.93165  28.58662  1.000 32.97191  ?  252 VAL   A C   1 
ATOM   7598  O O   . VAL   E  1 252 ? 34.11087  78.39122  27.44386  1.000 34.62570  ?  252 VAL   A O   1 
ATOM   7599  C CB  . VAL   E  1 252 ? 32.07191  76.41202  29.18894  1.000 34.85350  ?  252 VAL   A CB  1 
ATOM   7600  C CG1 . VAL   E  1 252 ? 30.82412  76.28901  30.06192  1.000 22.84858  ?  252 VAL   A CG1 1 
ATOM   7601  C CG2 . VAL   E  1 252 ? 31.81803  76.03810  27.71771  1.000 23.23905  ?  252 VAL   A CG2 1 
ATOM   7602  N N   . GLN   E  1 253 ? 35.01777  77.44401  29.27858  1.000 28.21153  ?  253 GLN   A N   1 
ATOM   7603  C CA  . GLN   E  1 253 ? 36.39932  77.65537  28.88616  1.000 33.97797  ?  253 GLN   A CA  1 
ATOM   7604  C C   . GLN   E  1 253 ? 37.23635  76.41767  29.22327  1.000 45.83481  ?  253 GLN   A C   1 
ATOM   7605  O O   . GLN   E  1 253 ? 36.74684  75.43166  29.79287  1.000 33.26462  ?  253 GLN   A O   1 
ATOM   7606  C CB  . GLN   E  1 253 ? 36.94223  78.89217  29.59954  1.000 22.60822  ?  253 GLN   A CB  1 
ATOM   7607  C CG  . GLN   E  1 253 ? 36.81340  78.74577  31.10471  1.000 60.18458  ?  253 GLN   A CG  1 
ATOM   7608  C CD  . GLN   E  1 253 ? 37.35177  79.92949  31.84748  1.000 51.44852  ?  253 GLN   A CD  1 
ATOM   7609  O OE1 . GLN   E  1 253 ? 37.00152  80.16010  33.00652  1.000 52.32908  ?  253 GLN   A OE1 1 
ATOM   7610  N NE2 . GLN   E  1 253 ? 38.21692  80.69069  31.19195  1.000 59.55882  ?  253 GLN   A NE2 1 
ATOM   7611  N N   . SER   E  1 254 ? 38.52337  76.48042  28.88476  1.000 41.80096  ?  254 SER   A N   1 
ATOM   7612  C CA  . SER   E  1 254 ? 39.47007  75.44596  29.26815  1.000 21.74620  ?  254 SER   A CA  1 
ATOM   7613  C C   . SER   E  1 254 ? 40.41025  75.94460  30.36614  1.000 23.83644  ?  254 SER   A C   1 
ATOM   7614  O O   . SER   E  1 254 ? 40.74204  77.13253  30.45305  1.000 35.59400  ?  254 SER   A O   1 
ATOM   7615  C CB  . SER   E  1 254 ? 40.26120  74.95966  28.05815  1.000 32.51336  ?  254 SER   A CB  1 
ATOM   7616  O OG  . SER   E  1 254 ? 39.37858  74.39114  27.09553  1.000 24.08512  ?  254 SER   A OG  1 
ATOM   7617  N N   . LEU   E  1 255 ? 40.80480  75.01775  31.22993  1.000 30.16755  ?  255 LEU   A N   1 
ATOM   7618  C CA  . LEU   E  1 255 ? 41.71762  75.28498  32.32550  1.000 32.52922  ?  255 LEU   A CA  1 
ATOM   7619  C C   . LEU   E  1 255 ? 43.00209  74.48097  32.13962  1.000 34.06853  ?  255 LEU   A C   1 
ATOM   7620  O O   . LEU   E  1 255 ? 43.00350  73.40496  31.53324  1.000 35.31691  ?  255 LEU   A O   1 
ATOM   7621  C CB  . LEU   E  1 255 ? 41.05975  74.93216  33.65764  1.000 35.24761  ?  255 LEU   A CB  1 
ATOM   7622  C CG  . LEU   E  1 255 ? 39.70350  75.61737  33.80607  1.000 36.51958  ?  255 LEU   A CG  1 
ATOM   7623  C CD1 . LEU   E  1 255 ? 38.96605  75.14868  35.04900  1.000 35.30595  ?  255 LEU   A CD1 1 
ATOM   7624  C CD2 . LEU   E  1 255 ? 39.89497  77.11908  33.82302  1.000 25.13656  ?  255 LEU   A CD2 1 
ATOM   7625  N N   . ASP   E  1 256 ? 44.11033  75.00482  32.66568  1.000 39.62104  ?  256 ASP   A N   1 
ATOM   7626  C CA  . ASP   E  1 256 ? 45.35473  74.24629  32.57746  1.000 24.99438  ?  256 ASP   A CA  1 
ATOM   7627  C C   . ASP   E  1 256 ? 45.45028  73.17705  33.66640  1.000 47.53023  ?  256 ASP   A C   1 
ATOM   7628  O O   . ASP   E  1 256 ? 46.03001  72.11232  33.41031  1.000 27.53300  ?  256 ASP   A O   1 
ATOM   7629  C CB  . ASP   E  1 256 ? 46.55824  75.19159  32.61666  1.000 35.01961  ?  256 ASP   A CB  1 
ATOM   7630  C CG  . ASP   E  1 256 ? 46.67529  76.03876  31.34884  1.000 61.74356  ?  256 ASP   A CG  1 
ATOM   7631  O OD1 . ASP   E  1 256 ? 47.01866  75.52008  30.25218  1.000 35.55362  ?  256 ASP   A OD1 1 
ATOM   7632  O OD2 . ASP   E  1 256 ? 46.41185  77.24362  31.44838  1.000 36.23387  -1 256 ASP   A OD2 1 
ATOM   7633  N N   . THR   E  1 257 ? 44.87899  73.42352  34.85798  1.000 30.58440  ?  257 THR   A N   1 
ATOM   7634  C CA  . THR   E  1 257 ? 44.74704  72.41215  35.90312  1.000 58.77508  ?  257 THR   A CA  1 
ATOM   7635  C C   . THR   E  1 257 ? 43.37318  72.51619  36.54515  1.000 24.89238  ?  257 THR   A C   1 
ATOM   7636  O O   . THR   E  1 257 ? 42.72035  73.56202  36.49622  1.000 46.87088  ?  257 THR   A O   1 
ATOM   7637  C CB  . THR   E  1 257 ? 45.80798  72.56584  37.00003  1.000 31.92728  ?  257 THR   A CB  1 
ATOM   7638  O OG1 . THR   E  1 257 ? 45.69729  73.87169  37.58434  1.000 54.63986  ?  257 THR   A OG1 1 
ATOM   7639  C CG2 . THR   E  1 257 ? 47.17159  72.40385  36.43616  1.000 43.51312  ?  257 THR   A CG2 1 
ATOM   7640  N N   . LEU   E  1 258 ? 42.96165  71.42261  37.18693  1.000 45.85610  ?  258 LEU   A N   1 
ATOM   7641  C CA  . LEU   E  1 258 ? 41.69187  71.37614  37.92460  1.000 31.30147  ?  258 LEU   A CA  1 
ATOM   7642  C C   . LEU   E  1 258 ? 41.96071  71.48182  39.42604  1.000 58.53904  ?  258 LEU   A C   1 
ATOM   7643  O O   . LEU   E  1 258 ? 41.78381  70.53052  40.20630  1.000 61.84807  ?  258 LEU   A O   1 
ATOM   7644  C CB  . LEU   E  1 258 ? 40.92950  70.09246  37.59695  1.000 31.43195  ?  258 LEU   A CB  1 
ATOM   7645  C CG  . LEU   E  1 258 ? 40.89739  69.69470  36.12911  1.000 27.28991  ?  258 LEU   A CG  1 
ATOM   7646  C CD1 . LEU   E  1 258 ? 40.24702  68.34735  36.03432  1.000 34.47932  ?  258 LEU   A CD1 1 
ATOM   7647  C CD2 . LEU   E  1 258 ? 40.17210  70.73724  35.27519  1.000 23.70254  ?  258 LEU   A CD2 1 
ATOM   7648  N N   . VAL   E  1 259 ? 42.41609  72.66922  39.81855  1.000 54.23506  ?  259 VAL   A N   1 
ATOM   7649  C CA  . VAL   E  1 259 ? 42.84787  72.96063  41.18292  1.000 57.57278  ?  259 VAL   A CA  1 
ATOM   7650  C C   . VAL   E  1 259 ? 42.26651  74.30534  41.57267  1.000 121.72119 ?  259 VAL   A C   1 
ATOM   7651  O O   . VAL   E  1 259 ? 42.41202  75.28243  40.81900  1.000 53.22812  ?  259 VAL   A O   1 
ATOM   7652  C CB  . VAL   E  1 259 ? 44.38240  73.03954  41.32799  1.000 77.25197  ?  259 VAL   A CB  1 
ATOM   7653  C CG1 . VAL   E  1 259 ? 44.77424  72.96726  42.79251  1.000 39.37971  ?  259 VAL   A CG1 1 
ATOM   7654  C CG2 . VAL   E  1 259 ? 45.12577  72.00827  40.47529  1.000 63.75722  ?  259 VAL   A CG2 1 
ATOM   7655  N N   . PHE   E  1 260 ? 41.64403  74.36635  42.76024  1.000 36.17709  ?  260 PHE   A N   1 
ATOM   7656  C CA  . PHE   E  1 260 ? 41.20657  75.62437  43.37682  1.000 96.71031  ?  260 PHE   A CA  1 
ATOM   7657  C C   . PHE   E  1 260 ? 40.13605  76.29839  42.54907  1.000 53.78847  ?  260 PHE   A C   1 
ATOM   7658  O O   . PHE   E  1 260 ? 39.79024  77.46208  42.79139  1.000 130.12646 ?  260 PHE   A O   1 
ATOM   7659  C CB  . PHE   E  1 260 ? 42.36119  76.62797  43.58627  1.000 49.28910  ?  260 PHE   A CB  1 
ATOM   7660  C CG  . PHE   E  1 260 ? 43.44814  76.13618  44.49472  1.000 67.01399  ?  260 PHE   A CG  1 
ATOM   7661  C CD1 . PHE   E  1 260 ? 43.14061  75.38358  45.61432  1.000 44.56200  ?  260 PHE   A CD1 1 
ATOM   7662  C CD2 . PHE   E  1 260 ? 44.77562  76.42340  44.22732  1.000 60.18209  ?  260 PHE   A CD2 1 
ATOM   7663  C CE1 . PHE   E  1 260 ? 44.13429  74.91794  46.45539  1.000 143.57560 ?  260 PHE   A CE1 1 
ATOM   7664  C CE2 . PHE   E  1 260 ? 45.77954  75.96085  45.07009  1.000 61.72437  ?  260 PHE   A CE2 1 
ATOM   7665  C CZ  . PHE   E  1 260 ? 45.45330  75.20438  46.18762  1.000 78.40661  ?  260 PHE   A CZ  1 
ATOM   7666  N N   . LYS   E  1 261 ? 39.58060  75.60807  41.57898  1.000 27.29456  ?  261 LYS   A N   1 
ATOM   7667  C CA  . LYS   E  1 261 ? 38.48622  76.11670  40.77080  1.000 77.09334  ?  261 LYS   A CA  1 
ATOM   7668  C C   . LYS   E  1 261 ? 37.38998  75.06866  40.70638  1.000 129.82346 ?  261 LYS   A C   1 
ATOM   7669  O O   . LYS   E  1 261 ? 36.59089  75.04220  39.76457  1.000 138.45199 ?  261 LYS   A O   1 
ATOM   7670  C CB  . LYS   E  1 261 ? 38.97319  76.50058  39.37903  1.000 120.10928 ?  261 LYS   A CB  1 
ATOM   7671  C CG  . LYS   E  1 261 ? 38.54093  77.87617  38.95874  1.000 94.57675  ?  261 LYS   A CG  1 
ATOM   7672  C CD  . LYS   E  1 261 ? 39.74729  78.76555  38.71277  1.000 93.00270  ?  261 LYS   A CD  1 
ATOM   7673  C CE  . LYS   E  1 261 ? 41.07466  77.99249  38.65306  1.000 58.10117  ?  261 LYS   A CE  1 
ATOM   7674  N NZ  . LYS   E  1 261 ? 41.66962  77.72573  37.30078  1.000 26.41286  ?  261 LYS   A NZ  1 
ATOM   7675  N N   . GLY   E  1 262 ? 37.37524  74.19122  41.73875  1.000 85.29179  ?  262 GLY   A N   1 
ATOM   7676  C CA  . GLY   E  1 262 ? 36.44908  73.07677  41.80327  1.000 29.88552  ?  262 GLY   A CA  1 
ATOM   7677  C C   . GLY   E  1 262 ? 35.06983  73.44818  41.32413  1.000 86.74714  ?  262 GLY   A C   1 
ATOM   7678  O O   . GLY   E  1 262 ? 34.60514  74.56471  41.53063  1.000 80.07108  ?  262 GLY   A O   1 
ATOM   7679  N N   . GLU   E  1 263 ? 34.42792  72.51654  40.64022  1.000 42.73517  ?  263 GLU   A N   1 
ATOM   7680  C CA  . GLU   E  1 263 ? 33.05978  72.73791  40.16393  1.000 77.13733  ?  263 GLU   A CA  1 
ATOM   7681  C C   . GLU   E  1 263 ? 33.03919  73.78959  39.05719  1.000 87.24320  ?  263 GLU   A C   1 
ATOM   7682  O O   . GLU   E  1 263 ? 32.07968  74.56523  38.92305  1.000 52.07412  ?  263 GLU   A O   1 
ATOM   7683  C CB  . GLU   E  1 263 ? 32.10371  73.12057  41.31298  1.000 41.15725  ?  263 GLU   A CB  1 
ATOM   7684  C CG  . GLU   E  1 263 ? 30.68016  72.59013  41.19446  1.000 76.78849  ?  263 GLU   A CG  1 
ATOM   7685  C CD  . GLU   E  1 263 ? 30.56519  71.05828  41.42565  1.000 70.03761  ?  263 GLU   A CD  1 
ATOM   7686  O OE1 . GLU   E  1 263 ? 31.61466  70.38117  41.56076  1.000 40.38402  ?  263 GLU   A OE1 1 
ATOM   7687  O OE2 . GLU   E  1 263 ? 29.41862  70.52972  41.47084  1.000 54.21772  -1 263 GLU   A OE2 1 
ATOM   7688  N N   . THR   E  1 264 ? 34.12873  73.82197  38.28270  1.000 44.37378  ?  264 THR   A N   1 
ATOM   7689  C CA  . THR   E  1 264 ? 34.19573  74.51794  37.00935  1.000 29.90289  ?  264 THR   A CA  1 
ATOM   7690  C C   . THR   E  1 264 ? 34.49408  73.50787  35.91463  1.000 45.15162  ?  264 THR   A C   1 
ATOM   7691  O O   . THR   E  1 264 ? 35.33299  72.62175  36.09757  1.000 36.23202  ?  264 THR   A O   1 
ATOM   7692  C CB  . THR   E  1 264 ? 35.29684  75.56321  37.01655  1.000 50.74881  ?  264 THR   A CB  1 
ATOM   7693  O OG1 . THR   E  1 264 ? 35.15517  76.38789  38.17513  1.000 101.81964 ?  264 THR   A OG1 1 
ATOM   7694  C CG2 . THR   E  1 264 ? 35.24336  76.39569  35.73785  1.000 37.73651  ?  264 THR   A CG2 1 
ATOM   7695  N N   . TYR   E  1 265 ? 33.81654  73.63174  34.77802  1.000 33.90305  ?  265 TYR   A N   1 
ATOM   7696  C CA  . TYR   E  1 265 ? 34.20681  72.81991  33.63299  1.000 24.41730  ?  265 TYR   A CA  1 
ATOM   7697  C C   . TYR   E  1 265 ? 35.51623  73.32749  33.04285  1.000 29.25603  ?  265 TYR   A C   1 
ATOM   7698  O O   . TYR   E  1 265 ? 35.82860  74.52538  33.09307  1.000 37.27532  ?  265 TYR   A O   1 
ATOM   7699  C CB  . TYR   E  1 265 ? 33.14084  72.83137  32.53406  1.000 20.49175  ?  265 TYR   A CB  1 
ATOM   7700  C CG  . TYR   E  1 265 ? 31.77391  72.36993  32.96547  1.000 39.34995  ?  265 TYR   A CG  1 
ATOM   7701  C CD1 . TYR   E  1 265 ? 31.54914  71.05965  33.33716  1.000 30.69976  ?  265 TYR   A CD1 1 
ATOM   7702  C CD2 . TYR   E  1 265 ? 30.70373  73.24906  32.97948  1.000 28.26289  ?  265 TYR   A CD2 1 
ATOM   7703  C CE1 . TYR   E  1 265 ? 30.28141  70.63368  33.72368  1.000 38.61056  ?  265 TYR   A CE1 1 
ATOM   7704  C CE2 . TYR   E  1 265 ? 29.44710  72.84452  33.36377  1.000 36.84495  ?  265 TYR   A CE2 1 
ATOM   7705  C CZ  . TYR   E  1 265 ? 29.23746  71.53285  33.73813  1.000 30.75598  ?  265 TYR   A CZ  1 
ATOM   7706  O OH  . TYR   E  1 265 ? 27.97675  71.13761  34.12944  1.000 34.08762  ?  265 TYR   A OH  1 
ATOM   7707  N N   . SER   E  1 266 ? 36.28130  72.38941  32.47807  1.000 28.61793  ?  266 SER   A N   1 
ATOM   7708  C CA  . SER   E  1 266 ? 37.41311  72.68483  31.60325  1.000 17.67620  ?  266 SER   A CA  1 
ATOM   7709  C C   . SER   E  1 266 ? 37.17458  71.90617  30.31011  1.000 31.18444  ?  266 SER   A C   1 
ATOM   7710  O O   . SER   E  1 266 ? 37.32933  70.67951  30.28594  1.000 21.72594  ?  266 SER   A O   1 
ATOM   7711  C CB  . SER   E  1 266 ? 38.73990  72.31003  32.26385  1.000 19.43746  ?  266 SER   A CB  1 
ATOM   7712  O OG  . SER   E  1 266 ? 39.79786  72.33153  31.31978  1.000 29.98743  ?  266 SER   A OG  1 
ATOM   7713  N N   . LEU   E  1 267 ? 36.77962  72.61693  29.24480  1.000 24.27892  ?  267 LEU   A N   1 
ATOM   7714  C CA  . LEU   E  1 267 ? 36.42767  71.96309  27.98270  1.000 33.86458  ?  267 LEU   A CA  1 
ATOM   7715  C C   . LEU   E  1 267 ? 37.51248  70.99917  27.52066  1.000 23.64330  ?  267 LEU   A C   1 
ATOM   7716  O O   . LEU   E  1 267 ? 37.22388  69.85831  27.14008  1.000 39.23977  ?  267 LEU   A O   1 
ATOM   7717  C CB  . LEU   E  1 267 ? 36.18621  73.00645  26.89985  1.000 17.32229  ?  267 LEU   A CB  1 
ATOM   7718  C CG  . LEU   E  1 267 ? 34.85947  73.73449  26.84493  1.000 36.92268  ?  267 LEU   A CG  1 
ATOM   7719  C CD1 . LEU   E  1 267 ? 34.96574  74.59179  25.63353  1.000 28.99925  ?  267 LEU   A CD1 1 
ATOM   7720  C CD2 . LEU   E  1 267 ? 33.65481  72.75920  26.73832  1.000 23.28491  ?  267 LEU   A CD2 1 
ATOM   7721  N N   . LYS   E  1 268 ? 38.77088  71.46621  27.52373  1.000 42.74311  ?  268 LYS   A N   1 
ATOM   7722  C CA  . LYS   E  1 268 ? 39.91802  70.64148  27.14159  1.000 21.59875  ?  268 LYS   A CA  1 
ATOM   7723  C C   . LYS   E  1 268 ? 39.91912  69.30028  27.88869  1.000 40.53131  ?  268 LYS   A C   1 
ATOM   7724  O O   . LYS   E  1 268 ? 40.19481  68.25213  27.29205  1.000 19.65203  ?  268 LYS   A O   1 
ATOM   7725  C CB  . LYS   E  1 268 ? 41.20109  71.44842  27.39593  1.000 28.00570  ?  268 LYS   A CB  1 
ATOM   7726  C CG  . LYS   E  1 268 ? 42.51536  70.68875  27.44305  1.000 40.92064  ?  268 LYS   A CG  1 
ATOM   7727  C CD  . LYS   E  1 268 ? 43.56769  71.47722  28.26236  1.000 34.52167  ?  268 LYS   A CD  1 
ATOM   7728  C CE  . LYS   E  1 268 ? 44.88663  70.66433  28.44053  1.000 47.10509  ?  268 LYS   A CE  1 
ATOM   7729  N NZ  . LYS   E  1 268 ? 45.68047  71.13644  29.65315  1.000 43.88717  ?  268 LYS   A NZ  1 
ATOM   7730  N N   . HIS   E  1 269 ? 39.56359  69.30710  29.18288  1.000 30.44027  ?  269 HIS   A N   1 
ATOM   7731  C CA  . HIS   E  1 269 ? 39.49864  68.07611  29.97082  1.000 14.94262  ?  269 HIS   A CA  1 
ATOM   7732  C C   . HIS   E  1 269 ? 38.21497  67.30269  29.69570  1.000 39.87339  ?  269 HIS   A C   1 
ATOM   7733  O O   . HIS   E  1 269 ? 38.26427  66.13114  29.30257  1.000 22.60972  ?  269 HIS   A O   1 
ATOM   7734  C CB  . HIS   E  1 269 ? 39.58826  68.38586  31.46562  1.000 22.60488  ?  269 HIS   A CB  1 
ATOM   7735  C CG  . HIS   E  1 269 ? 40.91963  68.89976  31.90093  1.000 26.65182  ?  269 HIS   A CG  1 
ATOM   7736  N ND1 . HIS   E  1 269 ? 41.31719  70.20338  31.70290  1.000 48.01597  ?  269 HIS   A ND1 1 
ATOM   7737  C CD2 . HIS   E  1 269 ? 41.94641  68.28596  32.53436  1.000 33.92682  ?  269 HIS   A CD2 1 
ATOM   7738  C CE1 . HIS   E  1 269 ? 42.53608  70.36834  32.18756  1.000 23.23785  ?  269 HIS   A CE1 1 
ATOM   7739  N NE2 . HIS   E  1 269 ? 42.94063  69.21977  32.69735  1.000 38.78451  ?  269 HIS   A NE2 1 
ATOM   7740  N N   . LEU   E  1 270 ? 37.05509  67.93791  29.94056  1.000 25.54200  ?  270 LEU   A N   1 
ATOM   7741  C CA  . LEU   E  1 270 ? 35.75908  67.30448  29.67716  1.000 20.79684  ?  270 LEU   A CA  1 
ATOM   7742  C C   . LEU   E  1 270 ? 35.75614  66.56464  28.33744  1.000 24.48469  ?  270 LEU   A C   1 
ATOM   7743  O O   . LEU   E  1 270 ? 35.45607  65.36450  28.27881  1.000 28.04089  ?  270 LEU   A O   1 
ATOM   7744  C CB  . LEU   E  1 270 ? 34.64327  68.35399  29.70954  1.000 27.51822  ?  270 LEU   A CB  1 
ATOM   7745  C CG  . LEU   E  1 270 ? 33.23310  67.83992  29.42848  1.000 24.58057  ?  270 LEU   A CG  1 
ATOM   7746  C CD1 . LEU   E  1 270 ? 32.66228  67.02867  30.60869  1.000 22.31556  ?  270 LEU   A CD1 1 
ATOM   7747  C CD2 . LEU   E  1 270 ? 32.31945  68.99270  29.04273  1.000 30.31082  ?  270 LEU   A CD2 1 
ATOM   7748  N N   . LEU   E  1 271 ? 36.14364  67.24978  27.25783  1.000 31.67847  ?  271 LEU   A N   1 
ATOM   7749  C CA  . LEU   E  1 271 ? 36.13516  66.66468  25.92035  1.000 28.30536  ?  271 LEU   A CA  1 
ATOM   7750  C C   . LEU   E  1 271 ? 37.44049  65.96853  25.55835  1.000 36.73803  ?  271 LEU   A C   1 
ATOM   7751  O O   . LEU   E  1 271 ? 37.61467  65.58044  24.39546  1.000 26.30030  ?  271 LEU   A O   1 
ATOM   7752  C CB  . LEU   E  1 271 ? 35.81765  67.73435  24.87421  1.000 18.76815  ?  271 LEU   A CB  1 
ATOM   7753  C CG  . LEU   E  1 271 ? 34.50147  68.47620  25.13129  1.000 31.85751  ?  271 LEU   A CG  1 
ATOM   7754  C CD1 . LEU   E  1 271 ? 34.36009  69.55232  24.08283  1.000 22.97433  ?  271 LEU   A CD1 1 
ATOM   7755  C CD2 . LEU   E  1 271 ? 33.28182  67.53131  25.15259  1.000 16.50059  ?  271 LEU   A CD2 1 
ATOM   7756  N N   . ASN   E  1 272 ? 38.36142  65.80688  26.51691  1.000 25.31693  ?  272 ASN   A N   1 
ATOM   7757  C CA  . ASN   E  1 272 ? 39.56507  64.98592  26.31964  1.000 17.31742  ?  272 ASN   A CA  1 
ATOM   7758  C C   . ASN   E  1 272 ? 40.38062  65.46314  25.11001  1.000 29.45431  ?  272 ASN   A C   1 
ATOM   7759  O O   . ASN   E  1 272 ? 40.82700  64.66945  24.28315  1.000 36.24841  ?  272 ASN   A O   1 
ATOM   7760  C CB  . ASN   E  1 272 ? 39.18883  63.50411  26.18321  1.000 39.22754  ?  272 ASN   A CB  1 
ATOM   7761  C CG  . ASN   E  1 272 ? 40.38581  62.57290  26.29596  1.000 29.71854  ?  272 ASN   A CG  1 
ATOM   7762  O OD1 . ASN   E  1 272 ? 41.27028  62.75233  27.14780  1.000 29.52238  ?  272 ASN   A OD1 1 
ATOM   7763  N ND2 . ASN   E  1 272 ? 40.41909  61.56388  25.42776  1.000 35.95037  ?  272 ASN   A ND2 1 
ATOM   7764  N N   . ASN   E  1 273 ? 40.55573  66.78775  25.00438  1.000 23.89404  ?  273 ASN   A N   1 
ATOM   7765  C CA  . ASN   E  1 273 ? 41.37617  67.42489  23.96063  1.000 33.00042  ?  273 ASN   A CA  1 
ATOM   7766  C C   . ASN   E  1 273 ? 40.90385  67.09565  22.54964  1.000 21.00967  ?  273 ASN   A C   1 
ATOM   7767  O O   . ASN   E  1 273 ? 41.71925  67.00597  21.63037  1.000 29.80516  ?  273 ASN   A O   1 
ATOM   7768  C CB  . ASN   E  1 273 ? 42.85682  67.05979  24.10331  1.000 27.48958  ?  273 ASN   A CB  1 
ATOM   7769  C CG  . ASN   E  1 273 ? 43.56514  67.93179  25.09658  1.000 63.99312  ?  273 ASN   A CG  1 
ATOM   7770  O OD1 . ASN   E  1 273 ? 43.69409  69.14398  24.88624  1.000 69.42997  ?  273 ASN   A OD1 1 
ATOM   7771  N ND2 . ASN   E  1 273 ? 44.01712  67.33387  26.20113  1.000 66.65448  ?  273 ASN   A ND2 1 
ATOM   7772  N N   . ASP   E  1 274 ? 39.59623  66.92911  22.34684  1.000 28.39361  ?  274 ASP   A N   1 
ATOM   7773  C CA  . ASP   E  1 274 ? 39.11544  66.61380  21.00608  1.000 25.61219  ?  274 ASP   A CA  1 
ATOM   7774  C C   . ASP   E  1 274 ? 39.39676  67.77529  20.05087  1.000 20.00974  ?  274 ASP   A C   1 
ATOM   7775  O O   . ASP   E  1 274 ? 39.30661  68.94776  20.44911  1.000 20.83932  ?  274 ASP   A O   1 
ATOM   7776  C CB  . ASP   E  1 274 ? 37.61490  66.30750  21.01901  1.000 22.20304  ?  274 ASP   A CB  1 
ATOM   7777  C CG  . ASP   E  1 274 ? 37.15032  65.65167  19.73276  1.000 31.83383  ?  274 ASP   A CG  1 
ATOM   7778  O OD1 . ASP   E  1 274 ? 36.90243  66.36735  18.72764  1.000 40.30293  ?  274 ASP   A OD1 1 
ATOM   7779  O OD2 . ASP   E  1 274 ? 37.07159  64.40225  19.71920  1.000 54.02641  -1 274 ASP   A OD2 1 
ATOM   7780  N N   . PRO   E  1 275 ? 39.72007  67.49625  18.78528  1.000 30.12638  ?  275 PRO   A N   1 
ATOM   7781  C CA  . PRO   E  1 275 ? 39.80097  68.58545  17.78974  1.000 10.09938  ?  275 PRO   A CA  1 
ATOM   7782  C C   . PRO   E  1 275 ? 38.57960  69.49963  17.74792  1.000 19.70115  ?  275 PRO   A C   1 
ATOM   7783  O O   . PRO   E  1 275 ? 38.75202  70.68553  17.44855  1.000 33.01651  ?  275 PRO   A O   1 
ATOM   7784  C CB  . PRO   E  1 275 ? 39.99754  67.83894  16.46652  1.000 12.32529  ?  275 PRO   A CB  1 
ATOM   7785  C CG  . PRO   E  1 275 ? 40.62595  66.53587  16.86764  1.000 14.37170  ?  275 PRO   A CG  1 
ATOM   7786  C CD  . PRO   E  1 275 ? 40.09147  66.18751  18.22701  1.000 18.30870  ?  275 PRO   A CD  1 
ATOM   7787  N N   . PHE   E  1 276 ? 37.36275  69.01628  18.06650  1.000 24.55495  ?  276 PHE   A N   1 
ATOM   7788  C CA  . PHE   E  1 276 ? 36.19269  69.90450  18.11125  1.000 14.88742  ?  276 PHE   A CA  1 
ATOM   7789  C C   . PHE   E  1 276 ? 36.20139  70.86785  19.29387  1.000 31.97803  ?  276 PHE   A C   1 
ATOM   7790  O O   . PHE   E  1 276 ? 35.40337  71.81608  19.29674  1.000 27.83633  ?  276 PHE   A O   1 
ATOM   7791  C CB  . PHE   E  1 276 ? 34.88277  69.11797  18.17452  1.000 16.12567  ?  276 PHE   A CB  1 
ATOM   7792  C CG  . PHE   E  1 276 ? 34.60584  68.28917  16.95908  1.000 31.63808  ?  276 PHE   A CG  1 
ATOM   7793  C CD1 . PHE   E  1 276 ? 34.99192  68.71771  15.70301  1.000 24.64483  ?  276 PHE   A CD1 1 
ATOM   7794  C CD2 . PHE   E  1 276 ? 33.94798  67.07433  17.07512  1.000 21.71101  ?  276 PHE   A CD2 1 
ATOM   7795  C CE1 . PHE   E  1 276 ? 34.71808  67.94591  14.58182  1.000 36.42426  ?  276 PHE   A CE1 1 
ATOM   7796  C CE2 . PHE   E  1 276 ? 33.67553  66.29176  15.96102  1.000 40.23724  ?  276 PHE   A CE2 1 
ATOM   7797  C CZ  . PHE   E  1 276 ? 34.06408  66.72407  14.71569  1.000 30.73198  ?  276 PHE   A CZ  1 
ATOM   7798  N N   . THR   E  1 277 ? 37.05760  70.64716  20.29354  1.000 28.94051  ?  277 THR   A N   1 
ATOM   7799  C CA  . THR   E  1 277 ? 37.01755  71.45465  21.51410  1.000 34.66420  ?  277 THR   A CA  1 
ATOM   7800  C C   . THR   E  1 277 ? 36.94764  72.95770  21.26215  1.000 26.24140  ?  277 THR   A C   1 
ATOM   7801  O O   . THR   E  1 277 ? 36.12814  73.62377  21.91191  1.000 32.30253  ?  277 THR   A O   1 
ATOM   7802  C CB  . THR   E  1 277 ? 38.22808  71.11944  22.39912  1.000 23.40813  ?  277 THR   A CB  1 
ATOM   7803  O OG1 . THR   E  1 277 ? 38.28489  69.70544  22.61069  1.000 29.64477  ?  277 THR   A OG1 1 
ATOM   7804  C CG2 . THR   E  1 277 ? 38.11069  71.80906  23.75221  1.000 13.40376  ?  277 THR   A CG2 1 
ATOM   7805  N N   . PRO   E  1 278 ? 37.74249  73.55095  20.35855  1.000 51.37811  ?  278 PRO   A N   1 
ATOM   7806  C CA  . PRO   E  1 278 ? 37.67682  75.01495  20.19589  1.000 24.07020  ?  278 PRO   A CA  1 
ATOM   7807  C C   . PRO   E  1 278 ? 36.30202  75.52921  19.80164  1.000 38.07712  ?  278 PRO   A C   1 
ATOM   7808  O O   . PRO   E  1 278 ? 35.95944  76.65975  20.17651  1.000 26.63956  ?  278 PRO   A O   1 
ATOM   7809  C CB  . PRO   E  1 278 ? 38.70618  75.29846  19.09214  1.000 16.80540  ?  278 PRO   A CB  1 
ATOM   7810  C CG  . PRO   E  1 278 ? 39.58872  74.14217  19.06249  1.000 20.58027  ?  278 PRO   A CG  1 
ATOM   7811  C CD  . PRO   E  1 278 ? 38.77209  72.95652  19.48551  1.000 23.49020  ?  278 PRO   A CD  1 
ATOM   7812  N N   . GLN   E  1 279 ? 35.50525  74.73786  19.05957  1.000 31.21296  ?  279 GLN   A N   1 
ATOM   7813  C CA  . GLN   E  1 279 ? 34.17616  75.18379  18.63053  1.000 29.02713  ?  279 GLN   A CA  1 
ATOM   7814  C C   . GLN   E  1 279 ? 33.23367  75.44920  19.80451  1.000 42.42924  ?  279 GLN   A C   1 
ATOM   7815  O O   . GLN   E  1 279 ? 32.25528  76.19557  19.64546  1.000 40.82034  ?  279 GLN   A O   1 
ATOM   7816  C CB  . GLN   E  1 279 ? 33.53165  74.15437  17.69195  1.000 26.46477  ?  279 GLN   A CB  1 
ATOM   7817  C CG  . GLN   E  1 279 ? 34.27930  73.91964  16.37958  1.000 17.96734  ?  279 GLN   A CG  1 
ATOM   7818  C CD  . GLN   E  1 279 ? 33.49630  73.05725  15.40080  1.000 57.49349  ?  279 GLN   A CD  1 
ATOM   7819  O OE1 . GLN   E  1 279 ? 32.31489  73.30416  15.13490  1.000 43.32442  ?  279 GLN   A OE1 1 
ATOM   7820  N NE2 . GLN   E  1 279 ? 34.15544  72.04087  14.85742  1.000 34.34833  ?  279 GLN   A NE2 1 
ATOM   7821  N N   . PHE   E  1 280 ? 33.50132  74.85150  20.96972  1.000 32.31133  ?  280 PHE   A N   1 
ATOM   7822  C CA  . PHE   E  1 280 ? 32.63930  74.97088  22.13676  1.000 33.88913  ?  280 PHE   A CA  1 
ATOM   7823  C C   . PHE   E  1 280 ? 33.17038  75.96566  23.14525  1.000 32.21157  ?  280 PHE   A C   1 
ATOM   7824  O O   . PHE   E  1 280 ? 32.51586  76.20019  24.17308  1.000 34.88506  ?  280 PHE   A O   1 
ATOM   7825  C CB  . PHE   E  1 280 ? 32.43345  73.59603  22.78377  1.000 15.80287  ?  280 PHE   A CB  1 
ATOM   7826  C CG  . PHE   E  1 280 ? 31.58553  72.70786  21.95310  1.000 45.72870  ?  280 PHE   A CG  1 
ATOM   7827  C CD1 . PHE   E  1 280 ? 30.19599  72.76597  22.04315  1.000 26.42877  ?  280 PHE   A CD1 1 
ATOM   7828  C CD2 . PHE   E  1 280 ? 32.16298  71.88613  21.00213  1.000 16.75298  ?  280 PHE   A CD2 1 
ATOM   7829  C CE1 . PHE   E  1 280 ? 29.41094  71.97299  21.22851  1.000 41.14626  ?  280 PHE   A CE1 1 
ATOM   7830  C CE2 . PHE   E  1 280 ? 31.37725  71.08862  20.18492  1.000 40.45755  ?  280 PHE   A CE2 1 
ATOM   7831  C CZ  . PHE   E  1 280 ? 30.00088  71.13541  20.29769  1.000 32.83190  ?  280 PHE   A CZ  1 
ATOM   7832  N N   . GLU   E  1 281 ? 34.33349  76.55437  22.87028  1.000 28.10604  ?  281 GLU   A N   1 
ATOM   7833  C CA  . GLU   E  1 281 ? 34.83179  77.64852  23.68439  1.000 40.95022  ?  281 GLU   A CA  1 
ATOM   7834  C C   . GLU   E  1 281 ? 33.79421  78.76940  23.72397  1.000 18.19759  ?  281 GLU   A C   1 
ATOM   7835  O O   . GLU   E  1 281 ? 33.22158  79.12916  22.69181  1.000 37.89498  ?  281 GLU   A O   1 
ATOM   7836  C CB  . GLU   E  1 281 ? 36.16254  78.13380  23.11047  1.000 21.46563  ?  281 GLU   A CB  1 
ATOM   7837  C CG  . GLU   E  1 281 ? 37.12854  78.62864  24.15328  1.000 53.44342  ?  281 GLU   A CG  1 
ATOM   7838  C CD  . GLU   E  1 281 ? 37.72175  77.50937  24.98872  1.000 121.65047 ?  281 GLU   A CD  1 
ATOM   7839  O OE1 . GLU   E  1 281 ? 38.05996  76.42222  24.44357  1.000 40.79494  ?  281 GLU   A OE1 1 
ATOM   7840  O OE2 . GLU   E  1 281 ? 37.85432  77.73637  26.20862  1.000 56.76903  -1 281 GLU   A OE2 1 
ATOM   7841  N N   . HIS   E  1 282 ? 33.50499  79.27172  24.92901  1.000 28.26815  ?  282 HIS   A N   1 
ATOM   7842  C CA  . HIS   E  1 282 ? 32.50160  80.30030  25.20511  1.000 51.85354  ?  282 HIS   A CA  1 
ATOM   7843  C C   . HIS   E  1 282 ? 31.06564  79.80072  25.07552  1.000 39.43517  ?  282 HIS   A C   1 
ATOM   7844  O O   . HIS   E  1 282 ? 30.13663  80.60427  25.20975  1.000 44.66139  ?  282 HIS   A O   1 
ATOM   7845  C CB  . HIS   E  1 282 ? 32.64468  81.52362  24.29468  1.000 19.36096  ?  282 HIS   A CB  1 
ATOM   7846  C CG  . HIS   E  1 282 ? 33.96821  82.20676  24.39859  1.000 66.10012  ?  282 HIS   A CG  1 
ATOM   7847  N ND1 . HIS   E  1 282 ? 34.33174  82.96288  25.49332  1.000 50.81062  ?  282 HIS   A ND1 1 
ATOM   7848  C CD2 . HIS   E  1 282 ? 35.01408  82.25655  23.53918  1.000 26.36823  ?  282 HIS   A CD2 1 
ATOM   7849  C CE1 . HIS   E  1 282 ? 35.54955  83.44130  25.30959  1.000 34.70941  ?  282 HIS   A CE1 1 
ATOM   7850  N NE2 . HIS   E  1 282 ? 35.98665  83.02820  24.13094  1.000 46.66823  ?  282 HIS   A NE2 1 
ATOM   7851  N N   . GLY   E  1 283 ? 30.84737  78.50955  24.81303  1.000 44.50333  ?  283 GLY   A N   1 
ATOM   7852  C CA  . GLY   E  1 283 ? 29.50739  77.95933  24.70990  1.000 24.06112  ?  283 GLY   A CA  1 
ATOM   7853  C C   . GLY   E  1 283 ? 28.88059  77.70141  26.06768  1.000 36.23659  ?  283 GLY   A C   1 
ATOM   7854  O O   . GLY   E  1 283 ? 29.32925  78.25951  27.07682  1.000 35.27874  ?  283 GLY   A O   1 
ATOM   7855  N N   . SER   E  1 284 ? 27.85218  76.85593  26.12297  1.000 24.56377  ?  284 SER   A N   1 
ATOM   7856  C CA  . SER   E  1 284 ? 27.15012  76.61953  27.38117  1.000 33.26950  ?  284 SER   A CA  1 
ATOM   7857  C C   . SER   E  1 284 ? 26.93644  75.12818  27.57674  1.000 27.27622  ?  284 SER   A C   1 
ATOM   7858  O O   . SER   E  1 284 ? 26.90444  74.34313  26.61714  1.000 20.21208  ?  284 SER   A O   1 
ATOM   7859  C CB  . SER   E  1 284 ? 25.79709  77.35815  27.43327  1.000 16.31465  ?  284 SER   A CB  1 
ATOM   7860  O OG  . SER   E  1 284 ? 25.08933  77.18063  26.20581  1.000 35.03538  ?  284 SER   A OG  1 
ATOM   7861  N N   . ILE   E  1 285 ? 26.76655  74.75024  28.84136  1.000 20.98697  ?  285 ILE   A N   1 
ATOM   7862  C CA  . ILE   E  1 285 ? 26.64481  73.35411  29.24138  1.000 19.72917  ?  285 ILE   A CA  1 
ATOM   7863  C C   . ILE   E  1 285 ? 25.51283  73.23639  30.25402  1.000 15.88669  ?  285 ILE   A C   1 
ATOM   7864  O O   . ILE   E  1 285 ? 25.46269  73.99646  31.23141  1.000 34.88155  ?  285 ILE   A O   1 
ATOM   7865  C CB  . ILE   E  1 285 ? 27.95685  72.81421  29.85723  1.000 23.13351  ?  285 ILE   A CB  1 
ATOM   7866  C CG1 . ILE   E  1 285 ? 29.10206  72.75977  28.83501  1.000 19.62309  ?  285 ILE   A CG1 1 
ATOM   7867  C CG2 . ILE   E  1 285 ? 27.71471  71.46943  30.49407  1.000 15.56573  ?  285 ILE   A CG2 1 
ATOM   7868  C CD1 . ILE   E  1 285 ? 30.46392  72.45801  29.46784  1.000 27.91251  ?  285 ILE   A CD1 1 
ATOM   7869  N N   . LEU   E  1 286 ? 24.61725  72.27750  30.02341  1.000 32.62211  ?  286 LEU   A N   1 
ATOM   7870  C CA  . LEU   E  1 286 ? 23.61935  71.83839  30.99093  1.000 15.49112  ?  286 LEU   A CA  1 
ATOM   7871  C C   . LEU   E  1 286 ? 23.98210  70.42533  31.43220  1.000 22.39107  ?  286 LEU   A C   1 
ATOM   7872  O O   . LEU   E  1 286 ? 24.24394  69.56111  30.58413  1.000 27.10599  ?  286 LEU   A O   1 
ATOM   7873  C CB  . LEU   E  1 286 ? 22.20261  71.86813  30.37975  1.000 30.67744  ?  286 LEU   A CB  1 
ATOM   7874  C CG  . LEU   E  1 286 ? 21.16787  70.94550  31.05770  1.000 26.33977  ?  286 LEU   A CG  1 
ATOM   7875  C CD1 . LEU   E  1 286 ? 20.82611  71.45616  32.43572  1.000 21.29992  ?  286 LEU   A CD1 1 
ATOM   7876  C CD2 . LEU   E  1 286 ? 19.89656  70.77911  30.24301  1.000 26.53748  ?  286 LEU   A CD2 1 
ATOM   7877  N N   . GLN   E  1 287 ? 23.98912  70.18843  32.74702  1.000 18.11529  ?  287 GLN   A N   1 
ATOM   7878  C CA  . GLN   E  1 287 ? 24.36865  68.89450  33.30743  1.000 32.17763  ?  287 GLN   A CA  1 
ATOM   7879  C C   . GLN   E  1 287 ? 23.27570  68.38806  34.24281  1.000 32.85772  ?  287 GLN   A C   1 
ATOM   7880  O O   . GLN   E  1 287 ? 22.80862  69.12328  35.12515  1.000 26.42529  ?  287 GLN   A O   1 
ATOM   7881  C CB  . GLN   E  1 287 ? 25.71064  68.97293  34.06075  1.000 21.22131  ?  287 GLN   A CB  1 
ATOM   7882  C CG  . GLN   E  1 287 ? 26.11616  67.66498  34.72277  1.000 29.13088  ?  287 GLN   A CG  1 
ATOM   7883  C CD  . GLN   E  1 287 ? 27.53017  67.66928  35.29662  1.000 26.39103  ?  287 GLN   A CD  1 
ATOM   7884  O OE1 . GLN   E  1 287 ? 28.20616  68.70043  35.33690  1.000 28.52963  ?  287 GLN   A OE1 1 
ATOM   7885  N NE2 . GLN   E  1 287 ? 27.98254  66.49753  35.75020  1.000 22.50686  ?  287 GLN   A NE2 1 
ATOM   7886  N N   . GLY   E  1 288 ? 22.88200  67.12710  34.05475  1.000 26.18052  ?  288 GLY   A N   1 
ATOM   7887  C CA  . GLY   E  1 288 ? 21.89857  66.47656  34.90539  1.000 18.00978  ?  288 GLY   A CA  1 
ATOM   7888  C C   . GLY   E  1 288 ? 22.45051  65.31222  35.72171  1.000 22.62756  ?  288 GLY   A C   1 
ATOM   7889  O O   . GLY   E  1 288 ? 23.49012  64.72421  35.39681  1.000 37.66461  ?  288 GLY   A O   1 
ATOM   7890  N N   . PHE   E  1 289 ? 21.76029  64.98130  36.80442  1.000 22.68510  ?  289 PHE   A N   1 
ATOM   7891  C CA  . PHE   E  1 289 ? 22.10891  63.86444  37.66834  1.000 29.23788  ?  289 PHE   A CA  1 
ATOM   7892  C C   . PHE   E  1 289 ? 20.96720  62.86128  37.63844  1.000 24.53792  ?  289 PHE   A C   1 
ATOM   7893  O O   . PHE   E  1 289 ? 19.80673  63.24397  37.80778  1.000 26.93086  ?  289 PHE   A O   1 
ATOM   7894  C CB  . PHE   E  1 289 ? 22.35501  64.35312  39.09540  1.000 18.27850  ?  289 PHE   A CB  1 
ATOM   7895  C CG  . PHE   E  1 289 ? 22.35687  63.26010  40.13302  1.000 23.96204  ?  289 PHE   A CG  1 
ATOM   7896  C CD1 . PHE   E  1 289 ? 23.28826  62.23208  40.07952  1.000 12.74921  ?  289 PHE   A CD1 1 
ATOM   7897  C CD2 . PHE   E  1 289 ? 21.44840  63.27338  41.18086  1.000 23.40265  ?  289 PHE   A CD2 1 
ATOM   7898  C CE1 . PHE   E  1 289 ? 23.30900  61.22163  41.05782  1.000 31.39186  ?  289 PHE   A CE1 1 
ATOM   7899  C CE2 . PHE   E  1 289 ? 21.46812  62.27248  42.15885  1.000 26.75804  ?  289 PHE   A CE2 1 
ATOM   7900  C CZ  . PHE   E  1 289 ? 22.40449  61.24836  42.09687  1.000 25.05783  ?  289 PHE   A CZ  1 
ATOM   7901  N N   . LEU   E  1 290 ? 21.29581  61.59029  37.41163  1.000 22.95759  ?  290 LEU   A N   1 
ATOM   7902  C CA  . LEU   E  1 290 ? 20.31951  60.50643  37.41334  1.000 22.32792  ?  290 LEU   A CA  1 
ATOM   7903  C C   . LEU   E  1 290 ? 20.32844  59.82238  38.78300  1.000 26.69597  ?  290 LEU   A C   1 
ATOM   7904  O O   . LEU   E  1 290 ? 21.36991  59.30926  39.20316  1.000 46.32158  ?  290 LEU   A O   1 
ATOM   7905  C CB  . LEU   E  1 290 ? 20.64555  59.50100  36.30442  1.000 15.46525  ?  290 LEU   A CB  1 
ATOM   7906  C CG  . LEU   E  1 290 ? 20.55093  59.86179  34.80842  1.000 23.21901  ?  290 LEU   A CG  1 
ATOM   7907  C CD1 . LEU   E  1 290 ? 21.67693  60.78621  34.36070  1.000 20.86647  ?  290 LEU   A CD1 1 
ATOM   7908  C CD2 . LEU   E  1 290 ? 20.51537  58.60867  33.90915  1.000 15.28890  ?  290 LEU   A CD2 1 
ATOM   7909  N N   . ASN   E  1 291 ? 19.17864  59.80988  39.47870  1.000 40.61234  ?  291 ASN   A N   1 
ATOM   7910  C CA  . ASN   E  1 291 ? 19.05295  59.06070  40.74113  1.000 28.03333  ?  291 ASN   A CA  1 
ATOM   7911  C C   . ASN   E  1 291 ? 19.26451  57.57423  40.50299  1.000 32.55355  ?  291 ASN   A C   1 
ATOM   7912  O O   . ASN   E  1 291 ? 19.19260  57.07883  39.37129  1.000 32.17145  ?  291 ASN   A O   1 
ATOM   7913  C CB  . ASN   E  1 291 ? 17.67057  59.21228  41.39076  1.000 55.09192  ?  291 ASN   A CB  1 
ATOM   7914  C CG  . ASN   E  1 291 ? 17.09780  60.58309  41.22498  1.000 66.06150  ?  291 ASN   A CG  1 
ATOM   7915  O OD1 . ASN   E  1 291 ? 16.54219  60.91402  40.17288  1.000 111.86403 ?  291 ASN   A OD1 1 
ATOM   7916  N ND2 . ASN   E  1 291 ? 17.22472  61.40202  42.26128  1.000 66.77720  ?  291 ASN   A ND2 1 
ATOM   7917  N N   . VAL   E  1 292 ? 19.48244  56.84366  41.59939  1.000 24.80567  ?  292 VAL   A N   1 
ATOM   7918  C CA  . VAL   E  1 292 ? 19.76161  55.42331  41.43586  1.000 52.77775  ?  292 VAL   A CA  1 
ATOM   7919  C C   . VAL   E  1 292 ? 18.53743  54.68082  40.91018  1.000 53.51864  ?  292 VAL   A C   1 
ATOM   7920  O O   . VAL   E  1 292 ? 18.67591  53.65562  40.22764  1.000 35.89358  ?  292 VAL   A O   1 
ATOM   7921  C CB  . VAL   E  1 292 ? 20.27272  54.81395  42.74732  1.000 51.09772  ?  292 VAL   A CB  1 
ATOM   7922  C CG1 . VAL   E  1 292 ? 21.04965  53.53629  42.43058  1.000 43.95608  ?  292 VAL   A CG1 1 
ATOM   7923  C CG2 . VAL   E  1 292 ? 21.12442  55.84213  43.52169  1.000 35.87533  ?  292 VAL   A CG2 1 
ATOM   7924  N N   . THR   E  1 293 ? 17.33084  55.18969  41.17801  1.000 33.36448  ?  293 THR   A N   1 
ATOM   7925  C CA  . THR   E  1 293 ? 16.10069  54.55381  40.71365  1.000 39.75334  ?  293 THR   A CA  1 
ATOM   7926  C C   . THR   E  1 293 ? 15.59347  55.07927  39.36762  1.000 67.01552  ?  293 THR   A C   1 
ATOM   7927  O O   . THR   E  1 293 ? 14.48693  54.70915  38.95713  1.000 54.26525  ?  293 THR   A O   1 
ATOM   7928  C CB  . THR   E  1 293 ? 14.98276  54.74185  41.73967  1.000 64.32514  ?  293 THR   A CB  1 
ATOM   7929  O OG1 . THR   E  1 293 ? 14.78165  56.14960  41.98923  1.000 42.34880  ?  293 THR   A OG1 1 
ATOM   7930  C CG2 . THR   E  1 293 ? 15.31499  54.00794  43.01742  1.000 33.02243  ?  293 THR   A CG2 1 
ATOM   7931  N N   . ALA   E  1 294 ? 16.34944  55.93215  38.68041  1.000 34.30598  ?  294 ALA   A N   1 
ATOM   7932  C CA  . ALA   E  1 294 ? 15.83910  56.54795  37.46504  1.000 27.66255  ?  294 ALA   A CA  1 
ATOM   7933  C C   . ALA   E  1 294 ? 16.02382  55.63838  36.24434  1.000 27.11123  ?  294 ALA   A C   1 
ATOM   7934  O O   . ALA   E  1 294 ? 16.80991  54.68593  36.23301  1.000 44.58632  ?  294 ALA   A O   1 
ATOM   7935  C CB  . ALA   E  1 294 ? 16.50814  57.90333  37.21451  1.000 26.01092  ?  294 ALA   A CB  1 
ATOM   7936  N N   . TYR   E  1 295 ? 15.22937  55.92194  35.22459  1.000 29.90852  ?  295 TYR   A N   1 
ATOM   7937  C CA  . TYR   E  1 295 ? 15.46176  55.35367  33.91193  1.000 37.35527  ?  295 TYR   A CA  1 
ATOM   7938  C C   . TYR   E  1 295 ? 16.88555  55.69918  33.48170  1.000 35.28198  ?  295 TYR   A C   1 
ATOM   7939  O O   . TYR   E  1 295 ? 17.31550  56.85019  33.59439  1.000 32.20709  ?  295 TYR   A O   1 
ATOM   7940  C CB  . TYR   E  1 295 ? 14.40366  55.93043  32.96971  1.000 10.56592  ?  295 TYR   A CB  1 
ATOM   7941  C CG  . TYR   E  1 295 ? 14.46965  55.57741  31.50252  1.000 40.36014  ?  295 TYR   A CG  1 
ATOM   7942  C CD1 . TYR   E  1 295 ? 13.81768  54.44075  30.99502  1.000 28.61441  ?  295 TYR   A CD1 1 
ATOM   7943  C CD2 . TYR   E  1 295 ? 15.10829  56.42614  30.60711  1.000 24.47785  ?  295 TYR   A CD2 1 
ATOM   7944  C CE1 . TYR   E  1 295 ? 13.85132  54.14073  29.62361  1.000 21.51256  ?  295 TYR   A CE1 1 
ATOM   7945  C CE2 . TYR   E  1 295 ? 15.15018  56.14494  29.25523  1.000 19.53542  ?  295 TYR   A CE2 1 
ATOM   7946  C CZ  . TYR   E  1 295 ? 14.52200  55.00349  28.75734  1.000 33.82360  ?  295 TYR   A CZ  1 
ATOM   7947  O OH  . TYR   E  1 295 ? 14.57744  54.73501  27.39905  1.000 24.83004  ?  295 TYR   A OH  1 
ATOM   7948  N N   . HIS   E  1 296 ? 17.64753  54.70026  33.03566  1.000 31.61080  ?  296 HIS   A N   1 
ATOM   7949  C CA  . HIS   E  1 296 ? 19.07033  54.91644  32.77666  1.000 39.83905  ?  296 HIS   A CA  1 
ATOM   7950  C C   . HIS   E  1 296 ? 19.46309  54.76641  31.30551  1.000 24.42762  ?  296 HIS   A C   1 
ATOM   7951  O O   . HIS   E  1 296 ? 20.64954  54.55159  31.00713  1.000 30.32819  ?  296 HIS   A O   1 
ATOM   7952  C CB  . HIS   E  1 296 ? 19.92466  53.99548  33.66036  1.000 28.82612  ?  296 HIS   A CB  1 
ATOM   7953  C CG  . HIS   E  1 296 ? 20.40984  54.66751  34.91285  1.000 38.71991  ?  296 HIS   A CG  1 
ATOM   7954  N ND1 . HIS   E  1 296 ? 19.61908  54.81441  36.03199  1.000 46.53581  ?  296 HIS   A ND1 1 
ATOM   7955  C CD2 . HIS   E  1 296 ? 21.57983  55.28838  35.19853  1.000 38.16622  ?  296 HIS   A CD2 1 
ATOM   7956  C CE1 . HIS   E  1 296 ? 20.28453  55.48133  36.95780  1.000 38.56829  ?  296 HIS   A CE1 1 
ATOM   7957  N NE2 . HIS   E  1 296 ? 21.47899  55.77828  36.47866  1.000 52.47448  ?  296 HIS   A NE2 1 
ATOM   7958  N N   . ARG   E  1 297 ? 18.51855  54.90131  30.37520  1.000 25.42092  ?  297 ARG   A N   1 
ATOM   7959  C CA  . ARG   E  1 297 ? 18.90003  54.89784  28.96911  1.000 20.84578  ?  297 ARG   A CA  1 
ATOM   7960  C C   . ARG   E  1 297 ? 19.08969  56.32599  28.47219  1.000 37.82307  ?  297 ARG   A C   1 
ATOM   7961  O O   . ARG   E  1 297 ? 18.70080  57.29238  29.13312  1.000 27.46917  ?  297 ARG   A O   1 
ATOM   7962  C CB  . ARG   E  1 297 ? 17.86603  54.17842  28.11901  1.000 24.72708  ?  297 ARG   A CB  1 
ATOM   7963  C CG  . ARG   E  1 297 ? 17.47522  52.82349  28.65060  1.000 29.74640  ?  297 ARG   A CG  1 
ATOM   7964  C CD  . ARG   E  1 297 ? 16.54172  52.15820  27.65871  1.000 26.61011  ?  297 ARG   A CD  1 
ATOM   7965  N NE  . ARG   E  1 297 ? 16.90384  50.76103  27.45497  1.000 44.11707  ?  297 ARG   A NE  1 
ATOM   7966  C CZ  . ARG   E  1 297 ? 17.42497  50.29086  26.33242  1.000 36.43747  ?  297 ARG   A CZ  1 
ATOM   7967  N NH1 . ARG   E  1 297 ? 17.59807  51.07348  25.27234  1.000 44.81265  ?  297 ARG   A NH1 1 
ATOM   7968  N NH2 . ARG   E  1 297 ? 17.77415  49.00701  26.26885  1.000 80.11463  ?  297 ARG   A NH2 1 
ATOM   7969  N N   . TRP   E  1 298 ? 19.72696  56.44776  27.30426  1.000 28.66234  ?  298 TRP   A N   1 
ATOM   7970  C CA  . TRP   E  1 298 ? 19.98222  57.72700  26.66161  1.000 26.51070  ?  298 TRP   A CA  1 
ATOM   7971  C C   . TRP   E  1 298 ? 19.08698  57.86360  25.43850  1.000 34.43048  ?  298 TRP   A C   1 
ATOM   7972  O O   . TRP   E  1 298 ? 18.94261  56.91959  24.65197  1.000 38.46817  ?  298 TRP   A O   1 
ATOM   7973  C CB  . TRP   E  1 298 ? 21.44174  57.87074  26.20118  1.000 20.68960  ?  298 TRP   A CB  1 
ATOM   7974  C CG  . TRP   E  1 298 ? 22.51394  57.39644  27.14080  1.000 31.42104  ?  298 TRP   A CG  1 
ATOM   7975  C CD1 . TRP   E  1 298 ? 22.44143  57.27623  28.50763  1.000 26.69147  ?  298 TRP   A CD1 1 
ATOM   7976  C CD2 . TRP   E  1 298 ? 23.83990  56.97663  26.77102  1.000 20.80351  ?  298 TRP   A CD2 1 
ATOM   7977  N NE1 . TRP   E  1 298 ? 23.63806  56.79195  29.00284  1.000 18.10041  ?  298 TRP   A NE1 1 
ATOM   7978  C CE2 . TRP   E  1 298 ? 24.51099  56.61080  27.95823  1.000 24.39836  ?  298 TRP   A CE2 1 
ATOM   7979  C CE3 . TRP   E  1 298 ? 24.51534  56.85772  25.54718  1.000 13.86647  ?  298 TRP   A CE3 1 
ATOM   7980  C CZ2 . TRP   E  1 298 ? 25.82547  56.13921  27.95408  1.000 29.52390  ?  298 TRP   A CZ2 1 
ATOM   7981  C CZ3 . TRP   E  1 298 ? 25.81240  56.40043  25.54631  1.000 35.77005  ?  298 TRP   A CZ3 1 
ATOM   7982  C CH2 . TRP   E  1 298 ? 26.45745  56.04522  26.74175  1.000 27.32542  ?  298 TRP   A CH2 1 
ATOM   7983  N N   . HIS   E  1 299 ? 18.52594  59.05237  25.26084  1.000 32.21236  ?  299 HIS   A N   1 
ATOM   7984  C CA  . HIS   E  1 299 ? 17.73361  59.38390  24.08956  1.000 41.09041  ?  299 HIS   A CA  1 
ATOM   7985  C C   . HIS   E  1 299 ? 18.42126  60.49180  23.30408  1.000 31.24544  ?  299 HIS   A C   1 
ATOM   7986  O O   . HIS   E  1 299 ? 19.14495  61.31638  23.87406  1.000 33.33904  ?  299 HIS   A O   1 
ATOM   7987  C CB  . HIS   E  1 299 ? 16.31255  59.82958  24.46853  1.000 20.42278  ?  299 HIS   A CB  1 
ATOM   7988  C CG  . HIS   E  1 299 ? 15.46855  58.73893  25.05575  1.000 37.34129  ?  299 HIS   A CG  1 
ATOM   7989  N ND1 . HIS   E  1 299 ? 14.16387  58.93791  25.45639  1.000 30.38605  ?  299 HIS   A ND1 1 
ATOM   7990  C CD2 . HIS   E  1 299 ? 15.75164  57.44177  25.32231  1.000 30.68799  ?  299 HIS   A CD2 1 
ATOM   7991  C CE1 . HIS   E  1 299 ? 13.68056  57.80862  25.94320  1.000 44.11626  ?  299 HIS   A CE1 1 
ATOM   7992  N NE2 . HIS   E  1 299 ? 14.62477  56.88546  25.87255  1.000 32.47719  ?  299 HIS   A NE2 1 
ATOM   7993  N N   . ALA   E  1 300 ? 18.17740  60.50962  21.98871  1.000 30.00104  ?  300 ALA   A N   1 
ATOM   7994  C CA  . ALA   E  1 300 ? 18.79067  61.51605  21.12384  1.000 35.03655  ?  300 ALA   A CA  1 
ATOM   7995  C C   . ALA   E  1 300 ? 18.16331  62.87916  21.38833  1.000 28.02145  ?  300 ALA   A C   1 
ATOM   7996  O O   . ALA   E  1 300 ? 16.93191  62.99970  21.38455  1.000 38.22150  ?  300 ALA   A O   1 
ATOM   7997  C CB  . ALA   E  1 300 ? 18.62074  61.13987  19.65763  1.000 23.57598  ?  300 ALA   A CB  1 
ATOM   7998  N N   . PRO   E  1 301 ? 18.96475  63.92164  21.63373  1.000 36.70359  ?  301 PRO   A N   1 
ATOM   7999  C CA  . PRO   E  1 301 ? 18.39358  65.24071  21.96758  1.000 22.54436  ?  301 PRO   A CA  1 
ATOM   8000  C C   . PRO   E  1 301 ? 17.92879  66.04683  20.76111  1.000 43.33068  ?  301 PRO   A C   1 
ATOM   8001  O O   . PRO   E  1 301 ? 17.22535  67.05122  20.94599  1.000 27.73027  ?  301 PRO   A O   1 
ATOM   8002  C CB  . PRO   E  1 301 ? 19.55530  65.94539  22.68924  1.000 31.44212  ?  301 PRO   A CB  1 
ATOM   8003  C CG  . PRO   E  1 301 ? 20.78641  65.33611  22.08435  1.000 28.69168  ?  301 PRO   A CG  1 
ATOM   8004  C CD  . PRO   E  1 301 ? 20.43801  63.90290  21.70545  1.000 14.00167  ?  301 PRO   A CD  1 
ATOM   8005  N N   . VAL   E  1 302 ? 18.30161  65.63928  19.54345  1.000 22.37347  ?  302 VAL   A N   1 
ATOM   8006  C CA  . VAL   E  1 302 ? 17.96053  66.34051  18.30809  1.000 47.20578  ?  302 VAL   A CA  1 
ATOM   8007  C C   . VAL   E  1 302 ? 17.82282  65.31457  17.19012  1.000 21.61853  ?  302 VAL   A C   1 
ATOM   8008  O O   . VAL   E  1 302 ? 18.29019  64.18039  17.29960  1.000 38.29062  ?  302 VAL   A O   1 
ATOM   8009  C CB  . VAL   E  1 302 ? 19.02955  67.38578  17.90272  1.000 21.37634  ?  302 VAL   A CB  1 
ATOM   8010  C CG1 . VAL   E  1 302 ? 19.14065  68.48533  18.94368  1.000 45.64362  ?  302 VAL   A CG1 1 
ATOM   8011  C CG2 . VAL   E  1 302 ? 20.38334  66.69328  17.64693  1.000 20.06409  ?  302 VAL   A CG2 1 
ATOM   8012  N N   . ASN   E  1 303 ? 17.17871  65.72175  16.09708  1.000 39.83203  ?  303 ASN   A N   1 
ATOM   8013  C CA  . ASN   E  1 303 ? 17.34839  64.99871  14.84167  1.000 24.70386  ?  303 ASN   A CA  1 
ATOM   8014  C C   . ASN   E  1 303 ? 18.73026  65.32640  14.29375  1.000 44.00651  ?  303 ASN   A C   1 
ATOM   8015  O O   . ASN   E  1 303 ? 19.08689  66.50533  14.15822  1.000 39.50846  ?  303 ASN   A O   1 
ATOM   8016  C CB  . ASN   E  1 303 ? 16.28247  65.39268  13.81619  1.000 43.53109  ?  303 ASN   A CB  1 
ATOM   8017  C CG  . ASN   E  1 303 ? 14.85782  65.23962  14.33520  1.000 36.27022  ?  303 ASN   A CG  1 
ATOM   8018  O OD1 . ASN   E  1 303 ? 14.59638  64.61521  15.37131  1.000 40.97747  ?  303 ASN   A OD1 1 
ATOM   8019  N ND2 . ASN   E  1 303 ? 13.92341  65.81681  13.59959  1.000 39.03016  ?  303 ASN   A ND2 1 
ATOM   8020  N N   . GLY   E  1 304 ? 19.52579  64.30502  14.00202  1.000 42.47416  ?  304 GLY   A N   1 
ATOM   8021  C CA  . GLY   E  1 304 ? 20.85272  64.60256  13.50582  1.000 29.24637  ?  304 GLY   A CA  1 
ATOM   8022  C C   . GLY   E  1 304 ? 21.66244  63.35460  13.25431  1.000 45.77291  ?  304 GLY   A C   1 
ATOM   8023  O O   . GLY   E  1 304 ? 21.15707  62.22726  13.30875  1.000 48.58865  ?  304 GLY   A O   1 
ATOM   8024  N N   . THR   E  1 305 ? 22.94481  63.58902  12.98878  1.000 40.17058  ?  305 THR   A N   1 
ATOM   8025  C CA  . THR   E  1 305 ? 23.89284  62.54227  12.63638  1.000 41.46938  ?  305 THR   A CA  1 
ATOM   8026  C C   . THR   E  1 305 ? 24.94630  62.39635  13.72902  1.000 63.40181  ?  305 THR   A C   1 
ATOM   8027  O O   . THR   E  1 305 ? 25.46050  63.39740  14.25487  1.000 28.27539  ?  305 THR   A O   1 
ATOM   8028  C CB  . THR   E  1 305 ? 24.57009  62.86324  11.30229  1.000 31.08925  ?  305 THR   A CB  1 
ATOM   8029  O OG1 . THR   E  1 305 ? 23.58098  63.35048  10.38665  1.000 48.16070  ?  305 THR   A OG1 1 
ATOM   8030  C CG2 . THR   E  1 305 ? 25.23178  61.61952  10.73351  1.000 30.87632  ?  305 THR   A CG2 1 
ATOM   8031  N N   . ILE   E  1 306 ? 25.25758  61.14886  14.07679  1.000 24.73441  ?  306 ILE   A N   1 
ATOM   8032  C CA  . ILE   E  1 306 ? 26.31602  60.89631  15.04362  1.000 37.55976  ?  306 ILE   A CA  1 
ATOM   8033  C C   . ILE   E  1 306 ? 27.63620  61.17967  14.35233  1.000 38.19896  ?  306 ILE   A C   1 
ATOM   8034  O O   . ILE   E  1 306 ? 27.98129  60.52367  13.36409  1.000 41.25432  ?  306 ILE   A O   1 
ATOM   8035  C CB  . ILE   E  1 306 ? 26.26570  59.45581  15.56620  1.000 33.82876  ?  306 ILE   A CB  1 
ATOM   8036  C CG1 . ILE   E  1 306 ? 24.84944  59.07897  16.02604  1.000 21.23146  ?  306 ILE   A CG1 1 
ATOM   8037  C CG2 . ILE   E  1 306 ? 27.30761  59.26718  16.67569  1.000 29.52257  ?  306 ILE   A CG2 1 
ATOM   8038  C CD1 . ILE   E  1 306 ? 24.23285  60.01657  17.07024  1.000 27.98913  ?  306 ILE   A CD1 1 
ATOM   8039  N N   . VAL   E  1 307 ? 28.36336  62.17338  14.84355  1.000 34.31057  ?  307 VAL   A N   1 
ATOM   8040  C CA  . VAL   E  1 307 ? 29.61925  62.53335  14.20838  1.000 28.19558  ?  307 VAL   A CA  1 
ATOM   8041  C C   . VAL   E  1 307 ? 30.77383  61.69658  14.74723  1.000 36.91282  ?  307 VAL   A C   1 
ATOM   8042  O O   . VAL   E  1 307 ? 31.59821  61.20917  13.96883  1.000 35.41632  ?  307 VAL   A O   1 
ATOM   8043  C CB  . VAL   E  1 307 ? 29.88476  64.04027  14.37038  1.000 44.11819  ?  307 VAL   A CB  1 
ATOM   8044  C CG1 . VAL   E  1 307 ? 31.20164  64.41102  13.71000  1.000 18.09318  ?  307 VAL   A CG1 1 
ATOM   8045  C CG2 . VAL   E  1 307 ? 28.73398  64.86183  13.79008  1.000 29.16464  ?  307 VAL   A CG2 1 
ATOM   8046  N N   . LYS   E  1 308 ? 30.81694  61.47772  16.06456  1.000 39.19028  ?  308 LYS   A N   1 
ATOM   8047  C CA  . LYS   E  1 308 ? 32.00219  60.92747  16.71692  1.000 29.80922  ?  308 LYS   A CA  1 
ATOM   8048  C C   . LYS   E  1 308 ? 31.64515  60.45579  18.11885  1.000 43.33285  ?  308 LYS   A C   1 
ATOM   8049  O O   . LYS   E  1 308 ? 31.00479  61.19285  18.87959  1.000 26.50311  ?  308 LYS   A O   1 
ATOM   8050  C CB  . LYS   E  1 308 ? 33.09813  61.98748  16.79043  1.000 26.62526  ?  308 LYS   A CB  1 
ATOM   8051  C CG  . LYS   E  1 308 ? 34.50780  61.49920  17.07301  1.000 17.96638  ?  308 LYS   A CG  1 
ATOM   8052  C CD  . LYS   E  1 308 ? 35.35734  62.75601  17.27672  1.000 28.82381  ?  308 LYS   A CD  1 
ATOM   8053  C CE  . LYS   E  1 308 ? 36.85409  62.52276  17.12816  1.000 48.76690  ?  308 LYS   A CE  1 
ATOM   8054  N NZ  . LYS   E  1 308 ? 37.50887  63.87152  16.98350  1.000 60.41277  ?  308 LYS   A NZ  1 
ATOM   8055  N N   . ILE   E  1 309 ? 32.07356  59.24048  18.45629  1.000 27.59774  ?  309 ILE   A N   1 
ATOM   8056  C CA  . ILE   E  1 309 ? 31.88129  58.64921  19.77549  1.000 34.67616  ?  309 ILE   A CA  1 
ATOM   8057  C C   . ILE   E  1 309 ? 33.25754  58.31190  20.32611  1.000 27.12392  ?  309 ILE   A C   1 
ATOM   8058  O O   . ILE   E  1 309 ? 34.00580  57.56460  19.68676  1.000 35.69888  ?  309 ILE   A O   1 
ATOM   8059  C CB  . ILE   E  1 309 ? 31.02006  57.38218  19.71819  1.000 19.12655  ?  309 ILE   A CB  1 
ATOM   8060  C CG1 . ILE   E  1 309 ? 29.64433  57.67076  19.13678  1.000 39.81653  ?  309 ILE   A CG1 1 
ATOM   8061  C CG2 . ILE   E  1 309 ? 30.91271  56.76615  21.11022  1.000 21.78160  ?  309 ILE   A CG2 1 
ATOM   8062  C CD1 . ILE   E  1 309 ? 28.91408  56.41468  18.75376  1.000 20.51408  ?  309 ILE   A CD1 1 
ATOM   8063  N N   . ILE   E  1 310 ? 33.59107  58.84452  21.50670  1.000 31.14280  ?  310 ILE   A N   1 
ATOM   8064  C CA  . ILE   E  1 310 ? 34.89283  58.61377  22.12615  1.000 15.02068  ?  310 ILE   A CA  1 
ATOM   8065  C C   . ILE   E  1 310 ? 34.69697  58.08122  23.53558  1.000 32.43246  ?  310 ILE   A C   1 
ATOM   8066  O O   . ILE   E  1 310 ? 33.97531  58.68504  24.33944  1.000 25.42665  ?  310 ILE   A O   1 
ATOM   8067  C CB  . ILE   E  1 310 ? 35.75158  59.88746  22.18420  1.000 32.41005  ?  310 ILE   A CB  1 
ATOM   8068  C CG1 . ILE   E  1 310 ? 35.80853  60.57125  20.82229  1.000 33.50078  ?  310 ILE   A CG1 1 
ATOM   8069  C CG2 . ILE   E  1 310 ? 37.12759  59.53058  22.69537  1.000 19.84607  ?  310 ILE   A CG2 1 
ATOM   8070  C CD1 . ILE   E  1 310 ? 35.16588  61.94120  20.81983  1.000 37.87206  ?  310 ILE   A CD1 1 
ATOM   8071  N N   . ASN   E  1 311 ? 35.37914  56.98937  23.85818  1.000 27.71462  ?  311 ASN   A N   1 
ATOM   8072  C CA  . ASN   E  1 311 ? 35.31460  56.42951  25.19959  1.000 24.52680  ?  311 ASN   A CA  1 
ATOM   8073  C C   . ASN   E  1 311 ? 36.59704  56.76633  25.94170  1.000 13.88353  ?  311 ASN   A C   1 
ATOM   8074  O O   . ASN   E  1 311 ? 37.69708  56.46011  25.47369  1.000 40.89648  ?  311 ASN   A O   1 
ATOM   8075  C CB  . ASN   E  1 311 ? 35.05221  54.92955  25.15673  1.000 9.28151   ?  311 ASN   A CB  1 
ATOM   8076  C CG  . ASN   E  1 311 ? 33.57367  54.62478  24.93051  1.000 55.00452  ?  311 ASN   A CG  1 
ATOM   8077  O OD1 . ASN   E  1 311 ? 32.72717  54.93670  25.77988  1.000 34.99561  ?  311 ASN   A OD1 1 
ATOM   8078  N ND2 . ASN   E  1 311 ? 33.25335  54.05350  23.77354  1.000 37.19916  ?  311 ASN   A ND2 1 
ATOM   8079  N N   . VAL   E  1 312 ? 36.45252  57.43713  27.07796  1.000 21.62150  ?  312 VAL   A N   1 
ATOM   8080  C CA  . VAL   E  1 312 ? 37.58113  58.00570  27.79369  1.000 20.06720  ?  312 VAL   A CA  1 
ATOM   8081  C C   . VAL   E  1 312 ? 37.71893  57.29845  29.13943  1.000 18.91304  ?  312 VAL   A C   1 
ATOM   8082  O O   . VAL   E  1 312 ? 36.79580  57.33590  29.95963  1.000 43.81620  ?  312 VAL   A O   1 
ATOM   8083  C CB  . VAL   E  1 312 ? 37.43122  59.52588  27.98030  1.000 23.63309  ?  312 VAL   A CB  1 
ATOM   8084  C CG1 . VAL   E  1 312 ? 38.76189  60.12622  28.46603  1.000 9.92994   ?  312 VAL   A CG1 1 
ATOM   8085  C CG2 . VAL   E  1 312 ? 37.01309  60.17669  26.66636  1.000 16.32918  ?  312 VAL   A CG2 1 
ATOM   8086  N N   . PRO   E  1 313 ? 38.83657  56.63317  29.40387  1.000 34.31595  ?  313 PRO   A N   1 
ATOM   8087  C CA  . PRO   E  1 313 ? 39.07875  56.09684  30.75194  1.000 29.99877  ?  313 PRO   A CA  1 
ATOM   8088  C C   . PRO   E  1 313 ? 39.26752  57.23241  31.74375  1.000 33.67885  ?  313 PRO   A C   1 
ATOM   8089  O O   . PRO   E  1 313 ? 39.75227  58.31438  31.39518  1.000 28.91715  ?  313 PRO   A O   1 
ATOM   8090  C CB  . PRO   E  1 313 ? 40.37862  55.28905  30.59952  1.000 13.03786  ?  313 PRO   A CB  1 
ATOM   8091  C CG  . PRO   E  1 313 ? 40.62976  55.18317  29.08309  1.000 18.88652  ?  313 PRO   A CG  1 
ATOM   8092  C CD  . PRO   E  1 313 ? 39.93432  56.36338  28.46193  1.000 15.05745  ?  313 PRO   A CD  1 
ATOM   8093  N N   . GLY   E  1 314 ? 38.88823  56.98004  32.99246  1.000 22.27411  ?  314 GLY   A N   1 
ATOM   8094  C CA  . GLY   E  1 314 ? 38.99464  58.01872  33.99035  1.000 14.73555  ?  314 GLY   A CA  1 
ATOM   8095  C C   . GLY   E  1 314 ? 38.81350  57.53032  35.40743  1.000 31.69836  ?  314 GLY   A C   1 
ATOM   8096  O O   . GLY   E  1 314 ? 39.04054  56.35814  35.71795  1.000 22.94940  ?  314 GLY   A O   1 
ATOM   8097  N N   . THR   E  1 315 ? 38.41382  58.45682  36.27356  1.000 28.74766  ?  315 THR   A N   1 
ATOM   8098  C CA  . THR   E  1 315 ? 38.18465  58.15787  37.67557  1.000 31.09927  ?  315 THR   A CA  1 
ATOM   8099  C C   . THR   E  1 315 ? 36.81005  57.50934  37.88187  1.000 39.42974  ?  315 THR   A C   1 
ATOM   8100  O O   . THR   E  1 315 ? 35.93856  57.52273  37.00561  1.000 31.61312  ?  315 THR   A O   1 
ATOM   8101  C CB  . THR   E  1 315 ? 38.29248  59.43503  38.51635  1.000 30.72174  ?  315 THR   A CB  1 
ATOM   8102  O OG1 . THR   E  1 315 ? 37.19229  60.31986  38.22266  1.000 24.50103  ?  315 THR   A OG1 1 
ATOM   8103  C CG2 . THR   E  1 315 ? 39.54349  60.15056  38.18277  1.000 21.21304  ?  315 THR   A CG2 1 
ATOM   8104  N N   . TYR   E  1 316 ? 36.63616  56.94581  39.07464  1.000 25.78151  ?  316 TYR   A N   1 
ATOM   8105  C CA  . TYR   E  1 316 ? 35.42625  56.37080  39.66240  1.000 25.34132  ?  316 TYR   A CA  1 
ATOM   8106  C C   . TYR   E  1 316 ? 35.11786  56.97326  41.02624  1.000 20.36625  ?  316 TYR   A C   1 
ATOM   8107  O O   . TYR   E  1 316 ? 33.94653  57.17598  41.35952  1.000 30.22827  ?  316 TYR   A O   1 
ATOM   8108  C CB  . TYR   E  1 316 ? 35.55581  54.82243  39.79838  1.000 20.28677  ?  316 TYR   A CB  1 
ATOM   8109  C CG  . TYR   E  1 316 ? 35.81590  54.15456  38.47541  1.000 31.03296  ?  316 TYR   A CG  1 
ATOM   8110  C CD1 . TYR   E  1 316 ? 34.76719  53.89611  37.58604  1.000 32.41210  ?  316 TYR   A CD1 1 
ATOM   8111  C CD2 . TYR   E  1 316 ? 37.11356  53.83142  38.08691  1.000 25.13164  ?  316 TYR   A CD2 1 
ATOM   8112  C CE1 . TYR   E  1 316 ? 34.99701  53.31124  36.34454  1.000 24.05083  ?  316 TYR   A CE1 1 
ATOM   8113  C CE2 . TYR   E  1 316 ? 37.36658  53.23973  36.84988  1.000 17.31983  ?  316 TYR   A CE2 1 
ATOM   8114  C CZ  . TYR   E  1 316 ? 36.30425  52.98206  35.98532  1.000 35.10415  ?  316 TYR   A CZ  1 
ATOM   8115  O OH  . TYR   E  1 316 ? 36.56470  52.40254  34.76283  1.000 26.37749  ?  316 TYR   A OH  1 
ATOM   8116  N N   . PHE   E  1 317 ? 36.14451  57.28512  41.82555  1.000 35.98207  ?  317 PHE   A N   1 
ATOM   8117  C CA  . PHE   E  1 317 ? 35.93193  57.64239  43.22244  1.000 17.23171  ?  317 PHE   A CA  1 
ATOM   8118  C C   . PHE   E  1 317 ? 36.55257  58.98609  43.57997  1.000 38.90158  ?  317 PHE   A C   1 
ATOM   8119  O O   . PHE   E  1 317 ? 36.87155  59.22511  44.75355  1.000 26.83298  ?  317 PHE   A O   1 
ATOM   8120  C CB  . PHE   E  1 317 ? 36.47561  56.54427  44.13602  1.000 17.11095  ?  317 PHE   A CB  1 
ATOM   8121  C CG  . PHE   E  1 317 ? 35.76880  55.23314  43.96881  1.000 37.25404  ?  317 PHE   A CG  1 
ATOM   8122  C CD1 . PHE   E  1 317 ? 34.46893  55.07431  44.43135  1.000 17.91130  ?  317 PHE   A CD1 1 
ATOM   8123  C CD2 . PHE   E  1 317 ? 36.39188  54.16856  43.32461  1.000 33.01743  ?  317 PHE   A CD2 1 
ATOM   8124  C CE1 . PHE   E  1 317 ? 33.80598  53.86999  44.27718  1.000 33.22032  ?  317 PHE   A CE1 1 
ATOM   8125  C CE2 . PHE   E  1 317 ? 35.73642  52.96632  43.16420  1.000 25.80989  ?  317 PHE   A CE2 1 
ATOM   8126  C CZ  . PHE   E  1 317 ? 34.43586  52.81867  43.64029  1.000 27.21651  ?  317 PHE   A CZ  1 
ATOM   8127  N N   . ALA   E  1 318 ? 36.71332  59.87927  42.59507  1.000 21.27535  ?  318 ALA   A N   1 
ATOM   8128  C CA  . ALA   E  1 318 ? 37.32260  61.19019  42.82575  1.000 18.15088  ?  318 ALA   A CA  1 
ATOM   8129  C C   . ALA   E  1 318 ? 36.23446  62.22102  43.09085  1.000 22.96661  ?  318 ALA   A C   1 
ATOM   8130  O O   . ALA   E  1 318 ? 35.44325  62.53366  42.19716  1.000 27.88342  ?  318 ALA   A O   1 
ATOM   8131  C CB  . ALA   E  1 318 ? 38.16619  61.61580  41.62779  1.000 11.67283  ?  318 ALA   A CB  1 
ATOM   8132  N N   . GLN   E  1 319 ? 36.19943  62.76522  44.30766  1.000 26.88209  ?  319 GLN   A N   1 
ATOM   8133  C CA  . GLN   E  1 319 ? 35.36508  63.93193  44.55647  1.000 23.36322  ?  319 GLN   A CA  1 
ATOM   8134  C C   . GLN   E  1 319 ? 36.20093  65.19453  44.34481  1.000 21.45837  ?  319 GLN   A C   1 
ATOM   8135  O O   . GLN   E  1 319 ? 37.41247  65.13364  44.10627  1.000 35.73144  ?  319 GLN   A O   1 
ATOM   8136  C CB  . GLN   E  1 319 ? 34.75481  63.88631  45.95508  1.000 22.84907  ?  319 GLN   A CB  1 
ATOM   8137  C CG  . GLN   E  1 319 ? 35.78737  63.96130  47.04131  1.000 30.95153  ?  319 GLN   A CG  1 
ATOM   8138  C CD  . GLN   E  1 319 ? 35.19669  63.68613  48.40310  1.000 19.96394  ?  319 GLN   A CD  1 
ATOM   8139  O OE1 . GLN   E  1 319 ? 34.87961  62.53752  48.74051  1.000 43.28455  ?  319 GLN   A OE1 1 
ATOM   8140  N NE2 . GLN   E  1 319 ? 35.05921  64.73446  49.20402  1.000 28.77115  ?  319 GLN   A NE2 1 
ATOM   8141  N N   . ALA   E  1 320 ? 35.55015  66.35298  44.40988  1.000 32.59507  ?  320 ALA   A N   1 
ATOM   8142  C CA  . ALA   E  1 320 ? 36.27038  67.61073  44.22959  1.000 33.34047  ?  320 ALA   A CA  1 
ATOM   8143  C C   . ALA   E  1 320 ? 37.18296  67.86619  45.42961  1.000 33.08328  ?  320 ALA   A C   1 
ATOM   8144  O O   . ALA   E  1 320 ? 36.72290  67.79864  46.57786  1.000 34.62149  ?  320 ALA   A O   1 
ATOM   8145  C CB  . ALA   E  1 320 ? 35.29757  68.76946  44.04466  1.000 17.08298  ?  320 ALA   A CB  1 
ATOM   8146  N N   . PRO   E  1 321 ? 38.46464  68.17894  45.20838  1.000 39.69428  ?  321 PRO   A N   1 
ATOM   8147  C CA  . PRO   E  1 321 ? 39.39079  68.37318  46.34135  1.000 25.59324  ?  321 PRO   A CA  1 
ATOM   8148  C C   . PRO   E  1 321 ? 38.92129  69.42512  47.34471  1.000 31.27851  ?  321 PRO   A C   1 
ATOM   8149  O O   . PRO   E  1 321 ? 39.14610  69.25171  48.54930  1.000 36.04500  ?  321 PRO   A O   1 
ATOM   8150  C CB  . PRO   E  1 321 ? 40.70392  68.78542  45.65497  1.000 18.78983  ?  321 PRO   A CB  1 
ATOM   8151  C CG  . PRO   E  1 321 ? 40.51716  68.51553  44.18851  1.000 39.94997  ?  321 PRO   A CG  1 
ATOM   8152  C CD  . PRO   E  1 321 ? 39.05192  68.58759  43.92067  1.000 22.23974  ?  321 PRO   A CD  1 
ATOM   8153  N N   . SER   E  1 322 ? 38.24158  70.48680  46.88576  1.000 29.81316  ?  322 SER   A N   1 
ATOM   8154  C CA  . SER   E  1 322 ? 37.68067  71.49897  47.78442  1.000 29.29539  ?  322 SER   A CA  1 
ATOM   8155  C C   . SER   E  1 322 ? 36.67742  70.93473  48.79078  1.000 28.89937  ?  322 SER   A C   1 
ATOM   8156  O O   . SER   E  1 322 ? 36.41243  71.59172  49.80535  1.000 48.27914  ?  322 SER   A O   1 
ATOM   8157  C CB  . SER   E  1 322 ? 37.00051  72.61655  46.97761  1.000 20.35962  ?  322 SER   A CB  1 
ATOM   8158  O OG  . SER   E  1 322 ? 36.29703  72.11325  45.84646  1.000 45.45196  ?  322 SER   A OG  1 
ATOM   8159  N N   . THR   E  1 323 ? 36.09009  69.76013  48.53025  1.000 47.74657  ?  323 THR   A N   1 
ATOM   8160  C CA  . THR   E  1 323 ? 35.12102  69.16445  49.44657  1.000 30.09088  ?  323 THR   A CA  1 
ATOM   8161  C C   . THR   E  1 323 ? 35.73484  68.12607  50.36880  1.000 45.56548  ?  323 THR   A C   1 
ATOM   8162  O O   . THR   E  1 323 ? 35.02229  67.58503  51.21578  1.000 28.47685  ?  323 THR   A O   1 
ATOM   8163  C CB  . THR   E  1 323 ? 33.95982  68.50637  48.68301  1.000 36.82519  ?  323 THR   A CB  1 
ATOM   8164  O OG1 . THR   E  1 323 ? 34.37665  67.23207  48.16177  1.000 38.36051  ?  323 THR   A OG1 1 
ATOM   8165  C CG2 . THR   E  1 323 ? 33.50955  69.38169  47.54614  1.000 18.77546  ?  323 THR   A CG2 1 
ATOM   8166  N N   . ILE   E  1 324 ? 37.02221  67.81510  50.21558  1.000 32.35722  ?  324 ILE   A N   1 
ATOM   8167  C CA  . ILE   E  1 324 ? 37.63019  66.78312  51.04581  1.000 34.10301  ?  324 ILE   A CA  1 
ATOM   8168  C C   . ILE   E  1 324 ? 37.54610  67.21226  52.50073  1.000 52.65252  ?  324 ILE   A C   1 
ATOM   8169  O O   . ILE   E  1 324 ? 38.00365  68.30130  52.87134  1.000 45.32284  ?  324 ILE   A O   1 
ATOM   8170  C CB  . ILE   E  1 324 ? 39.07078  66.52638  50.61332  1.000 22.11207  ?  324 ILE   A CB  1 
ATOM   8171  C CG1 . ILE   E  1 324 ? 39.08033  65.89779  49.22072  1.000 35.49050  ?  324 ILE   A CG1 1 
ATOM   8172  C CG2 . ILE   E  1 324 ? 39.77006  65.62754  51.63384  1.000 24.65451  ?  324 ILE   A CG2 1 
ATOM   8173  C CD1 . ILE   E  1 324 ? 40.43556  65.67258  48.67981  1.000 28.99359  ?  324 ILE   A CD1 1 
ATOM   8174  N N   . GLY   E  1 325 ? 36.92247  66.37348  53.32844  1.000 35.31570  ?  325 GLY   A N   1 
ATOM   8175  C CA  . GLY   E  1 325 ? 36.74101  66.67119  54.73264  1.000 30.53533  ?  325 GLY   A CA  1 
ATOM   8176  C C   . GLY   E  1 325 ? 35.36239  67.17263  55.12760  1.000 39.56628  ?  325 GLY   A C   1 
ATOM   8177  O O   . GLY   E  1 325 ? 35.03191  67.12979  56.31809  1.000 44.73774  ?  325 GLY   A O   1 
ATOM   8178  N N   . ASP   E  1 326 ? 34.56459  67.66462  54.17750  1.000 33.11724  ?  326 ASP   A N   1 
ATOM   8179  C CA  . ASP   E  1 326 ? 33.19456  68.07314  54.47167  1.000 40.32160  ?  326 ASP   A CA  1 
ATOM   8180  C C   . ASP   E  1 326 ? 32.40917  66.93442  55.13013  1.000 31.49606  ?  326 ASP   A C   1 
ATOM   8181  O O   . ASP   E  1 326 ? 32.71311  65.75283  54.93098  1.000 41.86407  ?  326 ASP   A O   1 
ATOM   8182  C CB  . ASP   E  1 326 ? 32.47403  68.50223  53.19300  1.000 22.75360  ?  326 ASP   A CB  1 
ATOM   8183  C CG  . ASP   E  1 326 ? 33.03408  69.77765  52.59357  1.000 59.42636  ?  326 ASP   A CG  1 
ATOM   8184  O OD1 . ASP   E  1 326 ? 33.91006  70.42268  53.22710  1.000 45.02746  ?  326 ASP   A OD1 1 
ATOM   8185  O OD2 . ASP   E  1 326 ? 32.57919  70.12660  51.47450  1.000 47.62092  -1 326 ASP   A OD2 1 
ATOM   8186  N N   . PRO   E  1 327 ? 31.38586  67.25825  55.91201  1.000 46.77936  ?  327 PRO   A N   1 
ATOM   8187  C CA  . PRO   E  1 327 ? 30.61200  66.20012  56.57468  1.000 32.23671  ?  327 PRO   A CA  1 
ATOM   8188  C C   . PRO   E  1 327 ? 29.86331  65.31836  55.57801  1.000 26.95518  ?  327 PRO   A C   1 
ATOM   8189  O O   . PRO   E  1 327 ? 29.34508  65.79357  54.56453  1.000 39.93785  ?  327 PRO   A O   1 
ATOM   8190  C CB  . PRO   E  1 327 ? 29.64449  66.98154  57.47486  1.000 12.55138  ?  327 PRO   A CB  1 
ATOM   8191  C CG  . PRO   E  1 327 ? 29.65978  68.39300  56.97203  1.000 26.79678  ?  327 PRO   A CG  1 
ATOM   8192  C CD  . PRO   E  1 327 ? 31.01989  68.60677  56.38428  1.000 29.71189  ?  327 PRO   A CD  1 
ATOM   8193  N N   . ILE   E  1 328 ? 29.82069  64.02043  55.87148  1.000 29.48704  ?  328 ILE   A N   1 
ATOM   8194  C CA  . ILE   E  1 328 ? 28.98519  63.08926  55.11289  1.000 29.28636  ?  328 ILE   A CA  1 
ATOM   8195  C C   . ILE   E  1 328 ? 27.66980  62.88634  55.85594  1.000 31.58208  ?  328 ILE   A C   1 
ATOM   8196  O O   . ILE   E  1 328 ? 27.61982  62.10131  56.81514  1.000 40.62297  ?  328 ILE   A O   1 
ATOM   8197  C CB  . ILE   E  1 328 ? 29.69389  61.74410  54.87664  1.000 34.51123  ?  328 ILE   A CB  1 
ATOM   8198  C CG1 . ILE   E  1 328 ? 31.03863  61.95666  54.17710  1.000 21.96783  ?  328 ILE   A CG1 1 
ATOM   8199  C CG2 . ILE   E  1 328 ? 28.82902  60.81410  54.02545  1.000 23.69231  ?  328 ILE   A CG2 1 
ATOM   8200  C CD1 . ILE   E  1 328 ? 31.78670  60.65502  53.88441  1.000 17.97762  ?  328 ILE   A CD1 1 
ATOM   8201  N N   . PRO   E  1 329 ? 26.58435  63.54406  55.43739  1.000 46.84798  ?  329 PRO   A N   1 
ATOM   8202  C CA  . PRO   E  1 329 ? 25.32927  63.49119  56.20306  1.000 32.32020  ?  329 PRO   A CA  1 
ATOM   8203  C C   . PRO   E  1 329 ? 24.81829  62.06795  56.37139  1.000 34.57310  ?  329 PRO   A C   1 
ATOM   8204  O O   . PRO   E  1 329 ? 24.98458  61.21337  55.49367  1.000 66.92345  ?  329 PRO   A O   1 
ATOM   8205  C CB  . PRO   E  1 329 ? 24.36058  64.33518  55.36591  1.000 19.18100  ?  329 PRO   A CB  1 
ATOM   8206  C CG  . PRO   E  1 329 ? 25.26076  65.21503  54.51168  1.000 29.88938  ?  329 PRO   A CG  1 
ATOM   8207  C CD  . PRO   E  1 329 ? 26.49230  64.42213  54.25979  1.000 34.78062  ?  329 PRO   A CD  1 
ATOM   8208  N N   . ASP   E  1 330 ? 24.23531  61.81434  57.54617  1.000 61.82203  ?  330 ASP   A N   1 
ATOM   8209  C CA  . ASP   E  1 330 ? 23.61994  60.53373  57.87489  1.000 71.89395  ?  330 ASP   A CA  1 
ATOM   8210  C C   . ASP   E  1 330 ? 22.12075  60.49117  57.57536  1.000 50.58726  ?  330 ASP   A C   1 
ATOM   8211  O O   . ASP   E  1 330 ? 21.41070  59.66003  58.17103  1.000 79.31221  ?  330 ASP   A O   1 
ATOM   8212  C CB  . ASP   E  1 330 ? 23.88610  60.17801  59.35012  1.000 43.12817  ?  330 ASP   A CB  1 
ATOM   8213  C CG  . ASP   E  1 330 ? 23.92371  58.68557  59.66314  1.000 62.15373  ?  330 ASP   A CG  1 
ATOM   8214  O OD1 . ASP   E  1 330 ? 24.16152  57.76678  58.75096  1.000 93.25933  ?  330 ASP   A OD1 1 
ATOM   8215  O OD2 . ASP   E  1 330 ? 23.79487  58.45166  60.86291  1.000 53.68250  ?  330 ASP   A OD2 1 
ATOM   8216  N N   . ASN   E  1 331 ? 21.65633  61.33889  56.65057  1.000 80.01547  ?  331 ASN   A N   1 
ATOM   8217  C CA  . ASN   E  1 331 ? 20.27327  61.43500  56.21161  1.000 80.14055  ?  331 ASN   A CA  1 
ATOM   8218  C C   . ASN   E  1 331 ? 20.25430  61.30523  54.69060  1.000 62.80893  ?  331 ASN   A C   1 
ATOM   8219  O O   . ASN   E  1 331 ? 21.25820  60.93549  54.09527  1.000 106.51888 ?  331 ASN   A O   1 
ATOM   8220  C CB  . ASN   E  1 331 ? 19.68679  62.75201  56.69684  1.000 58.06482  ?  331 ASN   A CB  1 
ATOM   8221  C CG  . ASN   E  1 331 ? 20.29134  63.95500  56.04818  1.000 69.15598  ?  331 ASN   A CG  1 
ATOM   8222  O OD1 . ASN   E  1 331 ? 20.43222  64.10152  54.83387  1.000 138.66921 ?  331 ASN   A OD1 1 
ATOM   8223  N ND2 . ASN   E  1 331 ? 20.76365  64.81449  56.91344  1.000 73.32570  ?  331 ASN   A ND2 1 
ATOM   8224  N N   . ASP   E  1 332 ? 19.15708  61.16721  54.10160  1.000 159.96346 ?  332 ASP   A N   1 
ATOM   8225  C CA  . ASP   E  1 332 ? 19.25411  60.86797  52.65800  1.000 28.08439  ?  332 ASP   A CA  1 
ATOM   8226  C C   . ASP   E  1 332 ? 18.79738  62.05620  51.80594  1.000 77.56763  ?  332 ASP   A C   1 
ATOM   8227  O O   . ASP   E  1 332 ? 18.47964  61.85646  50.64498  1.000 102.15594 ?  332 ASP   A O   1 
ATOM   8228  C CB  . ASP   E  1 332 ? 18.50697  59.56395  52.20021  1.000 58.30699  ?  332 ASP   A CB  1 
ATOM   8229  C CG  . ASP   E  1 332 ? 19.07705  58.30023  52.96514  1.000 125.96937 ?  332 ASP   A CG  1 
ATOM   8230  O OD1 . ASP   E  1 332 ? 18.84322  58.17504  54.19283  1.000 128.93804 ?  332 ASP   A OD1 1 
ATOM   8231  O OD2 . ASP   E  1 332 ? 19.66588  57.39551  52.32075  1.000 131.59076 ?  332 ASP   A OD2 1 
ATOM   8232  N N   . TYR   E  1 333 ? 19.07970  63.30008  52.30191  1.000 99.16237  ?  333 TYR   A N   1 
ATOM   8233  C CA  . TYR   E  1 333 ? 18.46627  64.48604  51.74083  1.000 74.81618  ?  333 TYR   A CA  1 
ATOM   8234  C C   . TYR   E  1 333 ? 19.35559  65.76804  51.73097  1.000 123.71711 ?  333 TYR   A C   1 
ATOM   8235  O O   . TYR   E  1 333 ? 19.03686  66.64596  50.92423  1.000 117.71055 ?  333 TYR   A O   1 
ATOM   8236  C CB  . TYR   E  1 333 ? 17.10726  64.74885  52.44687  1.000 20.21463  ?  333 TYR   A CB  1 
ATOM   8237  C CG  . TYR   E  1 333 ? 17.07014  64.60241  53.95903  1.000 101.76580 ?  333 TYR   A CG  1 
ATOM   8238  C CD1 . TYR   E  1 333 ? 17.50718  65.64503  54.76160  1.000 100.58545 ?  333 TYR   A CD1 1 
ATOM   8239  C CD2 . TYR   E  1 333 ? 16.58764  63.45002  54.58198  1.000 113.86489 ?  333 TYR   A CD2 1 
ATOM   8240  C CE1 . TYR   E  1 333 ? 17.48726  65.55579  56.13001  1.000 102.19892 ?  333 TYR   A CE1 1 
ATOM   8241  C CE2 . TYR   E  1 333 ? 16.55889  63.35677  55.96809  1.000 125.42430 ?  333 TYR   A CE2 1 
ATOM   8242  C CZ  . TYR   E  1 333 ? 17.01323  64.43215  56.73006  1.000 118.50244 ?  333 TYR   A CZ  1 
ATOM   8243  O OH  . TYR   E  1 333 ? 17.05553  64.45113  58.10011  1.000 32.00816  ?  333 TYR   A OH  1 
ATOM   8244  N N   . ASP   E  1 334 ? 20.46600  65.94639  52.67439  1.000 69.23399  ?  334 ASP   A N   1 
ATOM   8245  C CA  . ASP   E  1 334 ? 21.69576  66.72613  52.51998  1.000 67.30871  ?  334 ASP   A CA  1 
ATOM   8246  C C   . ASP   E  1 334 ? 22.70943  66.01514  51.62777  1.000 76.74908  ?  334 ASP   A C   1 
ATOM   8247  O O   . ASP   E  1 334 ? 23.05874  64.85076  51.88938  1.000 42.47664  ?  334 ASP   A O   1 
ATOM   8248  C CB  . ASP   E  1 334 ? 22.33048  67.00549  53.87245  1.000 96.11077  ?  334 ASP   A CB  1 
ATOM   8249  C CG  . ASP   E  1 334 ? 21.54193  68.00027  54.68191  1.000 110.73210 ?  334 ASP   A CG  1 
ATOM   8250  O OD1 . ASP   E  1 334 ? 20.90216  68.90027  54.06872  1.000 66.93774  ?  334 ASP   A OD1 1 
ATOM   8251  O OD2 . ASP   E  1 334 ? 21.56128  67.90204  55.92422  1.000 78.26195  -1 334 ASP   A OD2 1 
ATOM   8252  N N   . PRO   E  1 335 ? 23.21108  66.68386  50.58962  1.000 58.90731  ?  335 PRO   A N   1 
ATOM   8253  C CA  . PRO   E  1 335 ? 24.13408  66.03394  49.65841  1.000 38.71377  ?  335 PRO   A CA  1 
ATOM   8254  C C   . PRO   E  1 335 ? 25.48258  65.80344  50.30394  1.000 22.74331  ?  335 PRO   A C   1 
ATOM   8255  O O   . PRO   E  1 335 ? 26.04914  66.71037  50.94442  1.000 51.68490  ?  335 PRO   A O   1 
ATOM   8256  C CB  . PRO   E  1 335 ? 24.23885  67.04139  48.50311  1.000 44.49256  ?  335 PRO   A CB  1 
ATOM   8257  C CG  . PRO   E  1 335 ? 23.16291  68.06128  48.75756  1.000 57.35319  ?  335 PRO   A CG  1 
ATOM   8258  C CD  . PRO   E  1 335 ? 22.92471  68.07254  50.21453  1.000 30.92924  ?  335 PRO   A CD  1 
ATOM   8259  N N   . PRO   E  1 336 ? 26.04715  64.60321  50.15644  1.000 53.82367  ?  336 PRO   A N   1 
ATOM   8260  C CA  . PRO   E  1 336 ? 27.41917  64.34794  50.62439  1.000 18.23879  ?  336 PRO   A CA  1 
ATOM   8261  C C   . PRO   E  1 336 ? 28.43484  64.95221  49.66498  1.000 84.53103  ?  336 PRO   A C   1 
ATOM   8262  O O   . PRO   E  1 336 ? 28.07801  65.39981  48.56039  1.000 23.59728  ?  336 PRO   A O   1 
ATOM   8263  C CB  . PRO   E  1 336 ? 27.49158  62.81590  50.65625  1.000 37.22183  ?  336 PRO   A CB  1 
ATOM   8264  C CG  . PRO   E  1 336 ? 26.53978  62.37902  49.57356  1.000 34.19839  ?  336 PRO   A CG  1 
ATOM   8265  C CD  . PRO   E  1 336 ? 25.48379  63.45288  49.41710  1.000 18.22143  ?  336 PRO   A CD  1 
ATOM   8266  N N   . PRO   E  1 337 ? 29.71212  65.01910  50.05530  1.000 25.14419  ?  337 PRO   A N   1 
ATOM   8267  C CA  . PRO   E  1 337 ? 30.69669  65.73888  49.20970  1.000 40.75567  ?  337 PRO   A CA  1 
ATOM   8268  C C   . PRO   E  1 337 ? 30.75934  65.25634  47.76059  1.000 29.30924  ?  337 PRO   A C   1 
ATOM   8269  O O   . PRO   E  1 337 ? 30.81012  66.08133  46.83837  1.000 27.15497  ?  337 PRO   A O   1 
ATOM   8270  C CB  . PRO   E  1 337 ? 32.02421  65.49993  49.94009  1.000 27.27835  ?  337 PRO   A CB  1 
ATOM   8271  C CG  . PRO   E  1 337 ? 31.65553  65.20617  51.33341  1.000 35.66104  ?  337 PRO   A CG  1 
ATOM   8272  C CD  . PRO   E  1 337 ? 30.31171  64.52133  51.30190  1.000 44.33577  ?  337 PRO   A CD  1 
ATOM   8273  N N   . TYR   E  1 338 ? 30.72909  63.94097  47.53459  1.000 30.68261  ?  338 TYR   A N   1 
ATOM   8274  C CA  . TYR   E  1 338 ? 30.74738  63.41658  46.17328  1.000 33.26772  ?  338 TYR   A CA  1 
ATOM   8275  C C   . TYR   E  1 338 ? 29.60339  63.97983  45.33325  1.000 27.08011  ?  338 TYR   A C   1 
ATOM   8276  O O   . TYR   E  1 338 ? 29.82030  64.40212  44.18920  1.000 28.40824  ?  338 TYR   A O   1 
ATOM   8277  C CB  . TYR   E  1 338 ? 30.69793  61.88842  46.20642  1.000 20.78546  ?  338 TYR   A CB  1 
ATOM   8278  C CG  . TYR   E  1 338 ? 30.88992  61.21094  44.86516  1.000 33.86191  ?  338 TYR   A CG  1 
ATOM   8279  C CD1 . TYR   E  1 338 ? 32.04130  61.42272  44.09903  1.000 26.58965  ?  338 TYR   A CD1 1 
ATOM   8280  C CD2 . TYR   E  1 338 ? 29.93284  60.33779  44.37684  1.000 24.43016  ?  338 TYR   A CD2 1 
ATOM   8281  C CE1 . TYR   E  1 338 ? 32.21810  60.77670  42.86963  1.000 29.30206  ?  338 TYR   A CE1 1 
ATOM   8282  C CE2 . TYR   E  1 338 ? 30.09680  59.69543  43.16178  1.000 18.33876  ?  338 TYR   A CE2 1 
ATOM   8283  C CZ  . TYR   E  1 338 ? 31.23146  59.91797  42.40747  1.000 38.58361  ?  338 TYR   A CZ  1 
ATOM   8284  O OH  . TYR   E  1 338 ? 31.36501  59.26254  41.20085  1.000 27.13221  ?  338 TYR   A OH  1 
ATOM   8285  N N   . LEU   E  1 339 ? 28.37219  63.99367  45.87445  1.000 32.07045  ?  339 LEU   A N   1 
ATOM   8286  C CA  . LEU   E  1 339 ? 27.24828  64.52795  45.08924  1.000 23.23182  ?  339 LEU   A CA  1 
ATOM   8287  C C   . LEU   E  1 339 ? 27.26116  66.04729  44.97705  1.000 35.21694  ?  339 LEU   A C   1 
ATOM   8288  O O   . LEU   E  1 339 ? 26.41412  66.59689  44.26477  1.000 36.90850  ?  339 LEU   A O   1 
ATOM   8289  C CB  . LEU   E  1 339 ? 25.90360  64.08103  45.66089  1.000 24.05487  ?  339 LEU   A CB  1 
ATOM   8290  C CG  . LEU   E  1 339 ? 25.72723  62.55663  45.60310  1.000 46.07012  ?  339 LEU   A CG  1 
ATOM   8291  C CD1 . LEU   E  1 339 ? 24.33818  62.14971  46.04391  1.000 29.89563  ?  339 LEU   A CD1 1 
ATOM   8292  C CD2 . LEU   E  1 339 ? 26.00993  62.02750  44.21404  1.000 31.24968  ?  339 LEU   A CD2 1 
ATOM   8293  N N   . LYS   E  1 340 ? 28.18464  66.73802  45.64670  1.000 20.48568  ?  340 LYS   A N   1 
ATOM   8294  C CA  . LYS   E  1 340 ? 28.46001  68.13873  45.35282  1.000 40.30432  ?  340 LYS   A CA  1 
ATOM   8295  C C   . LYS   E  1 340 ? 29.63755  68.32595  44.38344  1.000 22.51632  ?  340 LYS   A C   1 
ATOM   8296  O O   . LYS   E  1 340 ? 30.11378  69.45217  44.22758  1.000 28.90762  ?  340 LYS   A O   1 
ATOM   8297  C CB  . LYS   E  1 340 ? 28.72297  68.91012  46.65071  1.000 23.16637  ?  340 LYS   A CB  1 
ATOM   8298  C CG  . LYS   E  1 340 ? 27.47714  68.91100  47.57690  1.000 20.14948  ?  340 LYS   A CG  1 
ATOM   8299  C CD  . LYS   E  1 340 ? 27.21920  70.36305  48.01349  1.000 66.29573  ?  340 LYS   A CD  1 
ATOM   8300  C CE  . LYS   E  1 340 ? 26.61702  70.45864  49.38695  1.000 65.83100  ?  340 LYS   A CE  1 
ATOM   8301  N NZ  . LYS   E  1 340 ? 27.16047  71.61071  50.19448  1.000 68.70403  ?  340 LYS   A NZ  1 
ATOM   8302  N N   . SER   E  1 341 ? 30.09595  67.25532  43.71060  1.000 26.94443  ?  341 SER   A N   1 
ATOM   8303  C CA  . SER   E  1 341 ? 31.30283  67.27858  42.88751  1.000 20.09949  ?  341 SER   A CA  1 
ATOM   8304  C C   . SER   E  1 341 ? 31.06906  67.00798  41.40075  1.000 24.98511  ?  341 SER   A C   1 
ATOM   8305  O O   . SER   E  1 341 ? 32.05076  66.88890  40.64850  1.000 35.53377  ?  341 SER   A O   1 
ATOM   8306  C CB  . SER   E  1 341 ? 32.31747  66.24534  43.41061  1.000 26.64507  ?  341 SER   A CB  1 
ATOM   8307  O OG  . SER   E  1 341 ? 32.75944  66.54289  44.72300  1.000 26.40697  ?  341 SER   A OG  1 
ATOM   8308  N N   . LEU   E  1 342 ? 29.81546  66.90736  40.95387  1.000 28.15835  ?  342 LEU   A N   1 
ATOM   8309  C CA  . LEU   E  1 342 ? 29.54005  66.39878  39.61208  1.000 39.34762  ?  342 LEU   A CA  1 
ATOM   8310  C C   . LEU   E  1 342 ? 30.15464  67.27522  38.52514  1.000 27.95010  ?  342 LEU   A C   1 
ATOM   8311  O O   . LEU   E  1 342 ? 30.60198  66.76308  37.49307  1.000 33.86651  ?  342 LEU   A O   1 
ATOM   8312  C CB  . LEU   E  1 342 ? 28.03481  66.27199  39.38449  1.000 22.21308  ?  342 LEU   A CB  1 
ATOM   8313  C CG  . LEU   E  1 342 ? 27.38250  64.93240  39.69770  1.000 40.47923  ?  342 LEU   A CG  1 
ATOM   8314  C CD1 . LEU   E  1 342 ? 27.49084  64.61512  41.19028  1.000 20.65614  ?  342 LEU   A CD1 1 
ATOM   8315  C CD2 . LEU   E  1 342 ? 25.91569  64.96974  39.23020  1.000 16.26733  ?  342 LEU   A CD2 1 
ATOM   8316  N N   . VAL   E  1 343 ? 30.17120  68.59659  38.70813  1.000 36.75800  ?  343 VAL   A N   1 
ATOM   8317  C CA  . VAL   E  1 343 ? 30.80569  69.42142  37.68276  1.000 31.05206  ?  343 VAL   A CA  1 
ATOM   8318  C C   . VAL   E  1 343 ? 32.30055  69.14035  37.64211  1.000 43.96618  ?  343 VAL   A C   1 
ATOM   8319  O O   . VAL   E  1 343 ? 32.87208  68.90519  36.57187  1.000 28.29472  ?  343 VAL   A O   1 
ATOM   8320  C CB  . VAL   E  1 343 ? 30.51773  70.91702  37.90196  1.000 31.93270  ?  343 VAL   A CB  1 
ATOM   8321  C CG1 . VAL   E  1 343 ? 31.39312  71.75622  36.97181  1.000 18.14804  ?  343 VAL   A CG1 1 
ATOM   8322  C CG2 . VAL   E  1 343 ? 29.05888  71.21513  37.61340  1.000 25.49571  ?  343 VAL   A CG2 1 
ATOM   8323  N N   . TYR   E  1 344 ? 32.94269  69.11343  38.81148  1.000 20.99227  ?  344 TYR   A N   1 
ATOM   8324  C CA  . TYR   E  1 344 ? 34.37441  68.84075  38.87256  1.000 38.44805  ?  344 TYR   A CA  1 
ATOM   8325  C C   . TYR   E  1 344 ? 34.73780  67.54703  38.15251  1.000 39.98125  ?  344 TYR   A C   1 
ATOM   8326  O O   . TYR   E  1 344 ? 35.58572  67.54991  37.25430  1.000 29.96632  ?  344 TYR   A O   1 
ATOM   8327  C CB  . TYR   E  1 344 ? 34.84992  68.78245  40.32552  1.000 25.34873  ?  344 TYR   A CB  1 
ATOM   8328  C CG  . TYR   E  1 344 ? 36.29826  68.36116  40.46708  1.000 45.73333  ?  344 TYR   A CG  1 
ATOM   8329  C CD1 . TYR   E  1 344 ? 37.32779  69.28010  40.29752  1.000 28.48493  ?  344 TYR   A CD1 1 
ATOM   8330  C CD2 . TYR   E  1 344 ? 36.63796  67.04443  40.76641  1.000 37.71060  ?  344 TYR   A CD2 1 
ATOM   8331  C CE1 . TYR   E  1 344 ? 38.65980  68.90543  40.42082  1.000 28.68400  ?  344 TYR   A CE1 1 
ATOM   8332  C CE2 . TYR   E  1 344 ? 37.97479  66.65245  40.89605  1.000 27.78124  ?  344 TYR   A CE2 1 
ATOM   8333  C CZ  . TYR   E  1 344 ? 38.97321  67.58994  40.72241  1.000 46.05094  ?  344 TYR   A CZ  1 
ATOM   8334  O OH  . TYR   E  1 344 ? 40.28737  67.21944  40.85557  1.000 41.09040  ?  344 TYR   A OH  1 
ATOM   8335  N N   . PHE   E  1 345 ? 34.11023  66.42403  38.53403  1.000 18.86856  ?  345 PHE   A N   1 
ATOM   8336  C CA  . PHE   E  1 345 ? 34.61200  65.14296  38.04267  1.000 27.91691  ?  345 PHE   A CA  1 
ATOM   8337  C C   . PHE   E  1 345 ? 34.06917  64.77442  36.66533  1.000 33.09629  ?  345 PHE   A C   1 
ATOM   8338  O O   . PHE   E  1 345 ? 34.53624  63.79153  36.07644  1.000 29.43945  ?  345 PHE   A O   1 
ATOM   8339  C CB  . PHE   E  1 345 ? 34.39278  63.99880  39.07266  1.000 18.41793  ?  345 PHE   A CB  1 
ATOM   8340  C CG  . PHE   E  1 345 ? 32.94648  63.58860  39.32754  1.000 31.62297  ?  345 PHE   A CG  1 
ATOM   8341  C CD1 . PHE   E  1 345 ? 32.16777  62.99526  38.34062  1.000 36.83309  ?  345 PHE   A CD1 1 
ATOM   8342  C CD2 . PHE   E  1 345 ? 32.41038  63.69249  40.60846  1.000 25.17162  ?  345 PHE   A CD2 1 
ATOM   8343  C CE1 . PHE   E  1 345 ? 30.85070  62.58715  38.61199  1.000 21.01603  ?  345 PHE   A CE1 1 
ATOM   8344  C CE2 . PHE   E  1 345 ? 31.09556  63.28293  40.89809  1.000 26.63876  ?  345 PHE   A CE2 1 
ATOM   8345  C CZ  . PHE   E  1 345 ? 30.31410  62.73004  39.90271  1.000 28.93650  ?  345 PHE   A CZ  1 
ATOM   8346  N N   . SER   E  1 346 ? 33.15327  65.56378  36.10540  1.000 16.78017  ?  346 SER   A N   1 
ATOM   8347  C CA  . SER   E  1 346 ? 32.86634  65.42668  34.68286  1.000 38.98744  ?  346 SER   A CA  1 
ATOM   8348  C C   . SER   E  1 346 ? 34.13479  65.62246  33.86067  1.000 26.35947  ?  346 SER   A C   1 
ATOM   8349  O O   . SER   E  1 346 ? 34.25132  65.08478  32.75099  1.000 26.36239  ?  346 SER   A O   1 
ATOM   8350  C CB  . SER   E  1 346 ? 31.80041  66.43466  34.25835  1.000 25.76495  ?  346 SER   A CB  1 
ATOM   8351  O OG  . SER   E  1 346 ? 32.36904  67.73249  34.15965  1.000 22.37141  ?  346 SER   A OG  1 
ATOM   8352  N N   . ASN   E  1 347 ? 35.10513  66.36680  34.40810  1.000 31.42473  ?  347 ASN   A N   1 
ATOM   8353  C CA  . ASN   E  1 347 ? 36.36901  66.60280  33.71884  1.000 12.52587  ?  347 ASN   A CA  1 
ATOM   8354  C C   . ASN   E  1 347 ? 37.25130  65.35794  33.65803  1.000 29.39774  ?  347 ASN   A C   1 
ATOM   8355  O O   . ASN   E  1 347 ? 38.07366  65.23856  32.73876  1.000 29.74030  ?  347 ASN   A O   1 
ATOM   8356  C CB  . ASN   E  1 347 ? 37.13041  67.74165  34.40074  1.000 20.04598  ?  347 ASN   A CB  1 
ATOM   8357  C CG  . ASN   E  1 347 ? 36.43397  69.07683  34.25298  1.000 35.19138  ?  347 ASN   A CG  1 
ATOM   8358  O OD1 . ASN   E  1 347 ? 36.24578  69.57827  33.13825  1.000 26.32674  ?  347 ASN   A OD1 1 
ATOM   8359  N ND2 . ASN   E  1 347 ? 36.05634  69.66932  35.37600  1.000 17.05792  ?  347 ASN   A ND2 1 
ATOM   8360  N N   . ILE   E  1 348 ? 37.10855  64.42814  34.61241  1.000 26.94093  ?  348 ILE   A N   1 
ATOM   8361  C CA  . ILE   E  1 348 ? 38.10464  63.36515  34.76879  1.000 19.93630  ?  348 ILE   A CA  1 
ATOM   8362  C C   . ILE   E  1 348 ? 37.51838  61.95876  34.90251  1.000 31.01562  ?  348 ILE   A C   1 
ATOM   8363  O O   . ILE   E  1 348 ? 38.25705  60.96813  34.84658  1.000 34.48721  ?  348 ILE   A O   1 
ATOM   8364  C CB  . ILE   E  1 348 ? 39.00328  63.67264  35.97711  1.000 28.91987  ?  348 ILE   A CB  1 
ATOM   8365  C CG1 . ILE   E  1 348 ? 38.14577  63.81038  37.23799  1.000 17.45031  ?  348 ILE   A CG1 1 
ATOM   8366  C CG2 . ILE   E  1 348 ? 39.82646  64.93808  35.72194  1.000 15.35701  ?  348 ILE   A CG2 1 
ATOM   8367  C CD1 . ILE   E  1 348 ? 38.97320  63.82917  38.51563  1.000 40.00463  ?  348 ILE   A CD1 1 
ATOM   8368  N N   . ALA   E  1 349 ? 36.20702  61.84999  35.09447  1.000 26.60669  ?  349 ALA   A N   1 
ATOM   8369  C CA  . ALA   E  1 349 ? 35.60295  60.54045  35.31576  1.000 27.06946  ?  349 ALA   A CA  1 
ATOM   8370  C C   . ALA   E  1 349 ? 35.55372  59.72885  34.02418  1.000 30.25145  ?  349 ALA   A C   1 
ATOM   8371  O O   . ALA   E  1 349 ? 35.48185  60.27850  32.91718  1.000 35.18725  ?  349 ALA   A O   1 
ATOM   8372  C CB  . ALA   E  1 349 ? 34.18049  60.68504  35.86632  1.000 12.27013  ?  349 ALA   A CB  1 
ATOM   8373  N N   . ALA   E  1 350 ? 35.58752  58.40344  34.17197  1.000 23.91814  ?  350 ALA   A N   1 
ATOM   8374  C CA  . ALA   E  1 350 ? 35.26372  57.53180  33.04675  1.000 26.40451  ?  350 ALA   A CA  1 
ATOM   8375  C C   . ALA   E  1 350 ? 33.95352  57.97540  32.39843  1.000 32.34380  ?  350 ALA   A C   1 
ATOM   8376  O O   . ALA   E  1 350 ? 32.92943  58.13105  33.07209  1.000 25.87338  ?  350 ALA   A O   1 
ATOM   8377  C CB  . ALA   E  1 350 ? 35.15567  56.08708  33.52014  1.000 12.27813  ?  350 ALA   A CB  1 
ATOM   8378  N N   . ARG   E  1 351 ? 33.99637  58.19676  31.08949  1.000 17.78211  ?  351 ARG   A N   1 
ATOM   8379  C CA  . ARG   E  1 351 ? 32.91045  58.89310  30.41992  1.000 28.03625  ?  351 ARG   A CA  1 
ATOM   8380  C C   . ARG   E  1 351 ? 32.96407  58.58737  28.93025  1.000 20.37312  ?  351 ARG   A C   1 
ATOM   8381  O O   . ARG   E  1 351 ? 33.98222  58.11519  28.40323  1.000 34.60844  ?  351 ARG   A O   1 
ATOM   8382  C CB  . ARG   E  1 351 ? 32.98387  60.41123  30.67752  1.000 13.75640  ?  351 ARG   A CB  1 
ATOM   8383  C CG  . ARG   E  1 351 ? 34.22763  61.06721  30.12034  1.000 13.76213  ?  351 ARG   A CG  1 
ATOM   8384  C CD  . ARG   E  1 351 ? 34.48433  62.42354  30.75693  1.000 21.67722  ?  351 ARG   A CD  1 
ATOM   8385  N NE  . ARG   E  1 351 ? 35.64188  63.08493  30.16347  1.000 23.24131  ?  351 ARG   A NE  1 
ATOM   8386  C CZ  . ARG   E  1 351 ? 36.90492  62.82805  30.48635  1.000 44.76278  ?  351 ARG   A CZ  1 
ATOM   8387  N NH1 . ARG   E  1 351 ? 37.22393  61.92493  31.40322  1.000 23.51165  ?  351 ARG   A NH1 1 
ATOM   8388  N NH2 . ARG   E  1 351 ? 37.87652  63.49768  29.87651  1.000 18.87858  ?  351 ARG   A NH2 1 
ATOM   8389  N N   . GLN   E  1 352 ? 31.83791  58.84139  28.26148  1.000 25.47700  ?  352 GLN   A N   1 
ATOM   8390  C CA  . GLN   E  1 352 ? 31.75984  58.74665  26.80943  1.000 18.83665  ?  352 GLN   A CA  1 
ATOM   8391  C C   . GLN   E  1 352 ? 31.31461  60.09006  26.26084  1.000 31.01288  ?  352 GLN   A C   1 
ATOM   8392  O O   . GLN   E  1 352 ? 30.34907  60.68510  26.76251  1.000 29.89153  ?  352 GLN   A O   1 
ATOM   8393  C CB  . GLN   E  1 352 ? 30.80241  57.65837  26.34816  1.000 29.00167  ?  352 GLN   A CB  1 
ATOM   8394  C CG  . GLN   E  1 352 ? 30.66826  57.59792  24.83507  1.000 24.05517  ?  352 GLN   A CG  1 
ATOM   8395  C CD  . GLN   E  1 352 ? 29.62076  56.58177  24.40424  1.000 32.40149  ?  352 GLN   A CD  1 
ATOM   8396  O OE1 . GLN   E  1 352 ? 28.52014  56.94433  23.99554  1.000 34.46043  ?  352 GLN   A OE1 1 
ATOM   8397  N NE2 . GLN   E  1 352 ? 29.95665  55.30215  24.51127  1.000 21.56668  ?  352 GLN   A NE2 1 
ATOM   8398  N N   . ILE   E  1 353 ? 32.05630  60.58223  25.27255  1.000 25.19669  ?  353 ILE   A N   1 
ATOM   8399  C CA  . ILE   E  1 353 ? 31.77297  61.84370  24.59900  1.000 28.01970  ?  353 ILE   A CA  1 
ATOM   8400  C C   . ILE   E  1 353 ? 31.10669  61.50982  23.27918  1.000 21.03666  ?  353 ILE   A C   1 
ATOM   8401  O O   . ILE   E  1 353 ? 31.59408  60.64462  22.53609  1.000 35.12697  ?  353 ILE   A O   1 
ATOM   8402  C CB  . ILE   E  1 353 ? 33.06291  62.64205  24.35074  1.000 25.92173  ?  353 ILE   A CB  1 
ATOM   8403  C CG1 . ILE   E  1 353 ? 33.78285  62.95353  25.66648  1.000 33.16352  ?  353 ILE   A CG1 1 
ATOM   8404  C CG2 . ILE   E  1 353 ? 32.75623  63.87942  23.51191  1.000 16.78533  ?  353 ILE   A CG2 1 
ATOM   8405  C CD1 . ILE   E  1 353 ? 35.25812  63.21272  25.48662  1.000 13.33489  ?  353 ILE   A CD1 1 
ATOM   8406  N N   . MET   E  1 354 ? 30.00112  62.17958  22.97410  1.000 20.29812  ?  354 MET   A N   1 
ATOM   8407  C CA  . MET   E  1 354 ? 29.30459  61.94103  21.71424  1.000 25.60492  ?  354 MET   A CA  1 
ATOM   8408  C C   . MET   E  1 354 ? 29.02543  63.27727  21.04130  1.000 30.69931  ?  354 MET   A C   1 
ATOM   8409  O O   . MET   E  1 354 ? 28.36038  64.14297  21.62470  1.000 32.16950  ?  354 MET   A O   1 
ATOM   8410  C CB  . MET   E  1 354 ? 28.01674  61.15369  21.94634  1.000 14.62104  ?  354 MET   A CB  1 
ATOM   8411  C CG  . MET   E  1 354 ? 27.34153  60.64743  20.67975  1.000 36.46350  ?  354 MET   A CG  1 
ATOM   8412  S SD  . MET   E  1 354 ? 25.83293  59.74604  21.06956  1.000 33.70248  ?  354 MET   A SD  1 
ATOM   8413  C CE  . MET   E  1 354 ? 26.54622  58.22233  21.70445  1.000 31.90886  ?  354 MET   A CE  1 
ATOM   8414  N N   . PHE   E  1 355 ? 29.56604  63.46183  19.83596  1.000 32.75069  ?  355 PHE   A N   1 
ATOM   8415  C CA  . PHE   E  1 355 ? 29.32240  64.66498  19.04378  1.000 34.38171  ?  355 PHE   A CA  1 
ATOM   8416  C C   . PHE   E  1 355 ? 28.21363  64.39018  18.04244  1.000 33.12149  ?  355 PHE   A C   1 
ATOM   8417  O O   . PHE   E  1 355 ? 28.25012  63.37848  17.32903  1.000 37.73257  ?  355 PHE   A O   1 
ATOM   8418  C CB  . PHE   E  1 355 ? 30.58822  65.11056  18.31137  1.000 38.23988  ?  355 PHE   A CB  1 
ATOM   8419  C CG  . PHE   E  1 355 ? 31.63534  65.63822  19.21873  1.000 40.09928  ?  355 PHE   A CG  1 
ATOM   8420  C CD1 . PHE   E  1 355 ? 31.53657  66.92721  19.72087  1.000 27.14267  ?  355 PHE   A CD1 1 
ATOM   8421  C CD2 . PHE   E  1 355 ? 32.70474  64.84691  19.59337  1.000 35.83684  ?  355 PHE   A CD2 1 
ATOM   8422  C CE1 . PHE   E  1 355 ? 32.49745  67.43541  20.57750  1.000 40.02075  ?  355 PHE   A CE1 1 
ATOM   8423  C CE2 . PHE   E  1 355 ? 33.66966  65.34202  20.44645  1.000 23.00163  ?  355 PHE   A CE2 1 
ATOM   8424  C CZ  . PHE   E  1 355 ? 33.57085  66.64581  20.93751  1.000 24.56034  ?  355 PHE   A CZ  1 
ATOM   8425  N N   . ILE   E  1 356 ? 27.22721  65.27531  17.99183  1.000 31.19941  ?  356 ILE   A N   1 
ATOM   8426  C CA  . ILE   E  1 356 ? 26.10645  65.10694  17.07731  1.000 34.55859  ?  356 ILE   A CA  1 
ATOM   8427  C C   . ILE   E  1 356 ? 25.97146  66.35409  16.22642  1.000 47.49906  ?  356 ILE   A C   1 
ATOM   8428  O O   . ILE   E  1 356 ? 26.08552  67.47779  16.73491  1.000 34.23928  ?  356 ILE   A O   1 
ATOM   8429  C CB  . ILE   E  1 356 ? 24.79462  64.80910  17.82421  1.000 28.63963  ?  356 ILE   A CB  1 
ATOM   8430  C CG1 . ILE   E  1 356 ? 24.96241  63.51786  18.64751  1.000 27.93996  ?  356 ILE   A CG1 1 
ATOM   8431  C CG2 . ILE   E  1 356 ? 23.64263  64.71750  16.81630  1.000 31.67830  ?  356 ILE   A CG2 1 
ATOM   8432  C CD1 . ILE   E  1 356 ? 23.77179  63.18951  19.55415  1.000 22.04499  ?  356 ILE   A CD1 1 
ATOM   8433  N N   . GLU   E  1 357 ? 25.74589  66.15341  14.92373  1.000 21.55741  ?  357 GLU   A N   1 
ATOM   8434  C CA  . GLU   E  1 357 ? 25.44944  67.25324  14.01045  1.000 36.55016  ?  357 GLU   A CA  1 
ATOM   8435  C C   . GLU   E  1 357 ? 23.93317  67.33440  13.80904  1.000 34.75603  ?  357 GLU   A C   1 
ATOM   8436  O O   . GLU   E  1 357 ? 23.34422  66.50903  13.09511  1.000 33.44401  ?  357 GLU   A O   1 
ATOM   8437  C CB  . GLU   E  1 357 ? 26.18439  67.06838  12.68900  1.000 27.06542  ?  357 GLU   A CB  1 
ATOM   8438  C CG  . GLU   E  1 357 ? 25.93368  68.18447  11.66771  1.000 25.84545  ?  357 GLU   A CG  1 
ATOM   8439  C CD  . GLU   E  1 357 ? 26.69343  69.47060  11.96521  1.000 79.14542  ?  357 GLU   A CD  1 
ATOM   8440  O OE1 . GLU   E  1 357 ? 27.89083  69.38936  12.33897  1.000 61.67479  ?  357 GLU   A OE1 1 
ATOM   8441  O OE2 . GLU   E  1 357 ? 26.09380  70.56441  11.80582  1.000 48.75404  -1 357 GLU   A OE2 1 
ATOM   8442  N N   . ALA   E  1 358 ? 23.31094  68.32694  14.45468  1.000 19.11587  ?  358 ALA   A N   1 
ATOM   8443  C CA  . ALA   E  1 358 ? 21.87061  68.54527  14.35008  1.000 37.97755  ?  358 ALA   A CA  1 
ATOM   8444  C C   . ALA   E  1 358 ? 21.47870  68.85238  12.91520  1.000 32.40512  ?  358 ALA   A C   1 
ATOM   8445  O O   . ALA   E  1 358 ? 22.15890  69.61736  12.22556  1.000 58.39979  ?  358 ALA   A O   1 
ATOM   8446  C CB  . ALA   E  1 358 ? 21.43720  69.71013  15.24499  1.000 26.61800  ?  358 ALA   A CB  1 
ATOM   8447  N N   . ASP   E  1 359 ? 20.37023  68.25043  12.46881  1.000 47.13561  ?  359 ASP   A N   1 
ATOM   8448  C CA  . ASP   E  1 359 ? 19.83865  68.56268  11.14240  1.000 42.44707  ?  359 ASP   A CA  1 
ATOM   8449  C C   . ASP   E  1 359 ? 19.56544  70.05762  10.99764  1.000 24.60022  ?  359 ASP   A C   1 
ATOM   8450  O O   . ASP   E  1 359 ? 19.77898  70.63736  9.92645   1.000 31.36374  ?  359 ASP   A O   1 
ATOM   8451  C CB  . ASP   E  1 359 ? 18.56196  67.75788  10.86394  1.000 21.51034  ?  359 ASP   A CB  1 
ATOM   8452  C CG  . ASP   E  1 359 ? 18.81933  66.25096  10.72400  1.000 58.79946  ?  359 ASP   A CG  1 
ATOM   8453  O OD1 . ASP   E  1 359 ? 19.99678  65.84829  10.57827  1.000 38.82397  ?  359 ASP   A OD1 1 
ATOM   8454  O OD2 . ASP   E  1 359 ? 17.83863  65.46348  10.78039  1.000 32.53429  -1 359 ASP   A OD2 1 
ATOM   8455  N N   . ASN   E  1 360 ? 19.11005  70.70207  12.06214  1.000 35.92316  ?  360 ASN   A N   1 
ATOM   8456  C CA  . ASN   E  1 360 ? 18.87405  72.14039  12.02571  1.000 27.17519  ?  360 ASN   A CA  1 
ATOM   8457  C C   . ASN   E  1 360 ? 20.21504  72.87020  12.10388  1.000 38.14022  ?  360 ASN   A C   1 
ATOM   8458  O O   . ASN   E  1 360 ? 20.86781  72.87327  13.15653  1.000 48.81303  ?  360 ASN   A O   1 
ATOM   8459  C CB  . ASN   E  1 360 ? 17.94783  72.54738  13.17030  1.000 28.45573  ?  360 ASN   A CB  1 
ATOM   8460  C CG  . ASN   E  1 360 ? 17.47528  73.96503  13.04751  1.000 47.24168  ?  360 ASN   A CG  1 
ATOM   8461  O OD1 . ASN   E  1 360 ? 18.25858  74.87306  12.74444  1.000 50.34604  ?  360 ASN   A OD1 1 
ATOM   8462  N ND2 . ASN   E  1 360 ? 16.17838  74.17304  13.26522  1.000 53.20471  ?  360 ASN   A ND2 1 
ATOM   8463  N N   . LYS   E  1 361 ? 20.60959  73.51407  10.99910  1.000 41.50940  ?  361 LYS   A N   1 
ATOM   8464  C CA  . LYS   E  1 361 ? 21.91064  74.17543  10.92352  1.000 49.27827  ?  361 LYS   A CA  1 
ATOM   8465  C C   . LYS   E  1 361 ? 22.08421  75.26222  11.98040  1.000 21.59538  ?  361 LYS   A C   1 
ATOM   8466  O O   . LYS   E  1 361 ? 23.22432  75.56946  12.35404  1.000 71.97868  ?  361 LYS   A O   1 
ATOM   8467  C CB  . LYS   E  1 361 ? 22.12246  74.76007  9.52093   1.000 25.75192  ?  361 LYS   A CB  1 
ATOM   8468  C CG  . LYS   E  1 361 ? 23.17562  74.14839  8.75872   1.000 69.04145  ?  361 LYS   A CG  1 
ATOM   8469  C CD  . LYS   E  1 361 ? 22.64837  72.97220  8.04722   1.000 16.91218  ?  361 LYS   A CD  1 
ATOM   8470  C CE  . LYS   E  1 361 ? 23.75854  72.32333  7.27547   1.000 92.40613  ?  361 LYS   A CE  1 
ATOM   8471  N NZ  . LYS   E  1 361 ? 24.34419  73.33244  6.34938   1.000 96.00979  ?  361 LYS   A NZ  1 
ATOM   8472  N N   . GLU   E  1 362 ? 20.98931  75.83024  12.48572  1.000 43.01602  ?  362 GLU   A N   1 
ATOM   8473  C CA  . GLU   E  1 362 ? 21.06113  76.84555  13.53310  1.000 38.47963  ?  362 GLU   A CA  1 
ATOM   8474  C C   . GLU   E  1 362 ? 21.40693  76.26164  14.89894  1.000 58.76187  ?  362 GLU   A C   1 
ATOM   8475  O O   . GLU   E  1 362 ? 21.70319  77.02460  15.83019  1.000 51.02436  ?  362 GLU   A O   1 
ATOM   8476  C CB  . GLU   E  1 362 ? 19.73192  77.61008  13.62343  1.000 47.33822  ?  362 GLU   A CB  1 
ATOM   8477  N N   . ILE   E  1 363 ? 21.33312  74.94115  15.04426  1.000 37.45672  ?  363 ILE   A N   1 
ATOM   8478  C CA  . ILE   E  1 363 ? 21.78600  74.24701  16.23856  1.000 55.42472  ?  363 ILE   A CA  1 
ATOM   8479  C C   . ILE   E  1 363 ? 23.15919  73.62996  16.01131  1.000 43.91621  ?  363 ILE   A C   1 
ATOM   8480  O O   . ILE   E  1 363 ? 24.06611  73.78021  16.83289  1.000 52.26934  ?  363 ILE   A O   1 
ATOM   8481  C CB  . ILE   E  1 363 ? 20.72953  73.18937  16.64553  1.000 45.66121  ?  363 ILE   A CB  1 
ATOM   8482  C CG1 . ILE   E  1 363 ? 19.46815  73.87424  17.18105  1.000 39.56855  ?  363 ILE   A CG1 1 
ATOM   8483  C CG2 . ILE   E  1 363 ? 21.25880  72.24884  17.70804  1.000 25.44442  ?  363 ILE   A CG2 1 
ATOM   8484  C CD1 . ILE   E  1 363 ? 18.33613  72.90624  17.51645  1.000 42.97005  ?  363 ILE   A CD1 1 
ATOM   8485  N N   . GLY   E  1 364 ? 23.32250  72.97752  14.86741  1.000 36.86703  ?  364 GLY   A N   1 
ATOM   8486  C CA  . GLY   E  1 364 ? 24.61749  72.58624  14.40095  1.000 24.76278  ?  364 GLY   A CA  1 
ATOM   8487  C C   . GLY   E  1 364 ? 25.25022  71.49684  15.24223  1.000 70.00571  ?  364 GLY   A C   1 
ATOM   8488  O O   . GLY   E  1 364 ? 24.59268  70.55655  15.70949  1.000 34.59650  ?  364 GLY   A O   1 
ATOM   8489  N N   . LEU   E  1 365 ? 26.56262  71.62409  15.41741  1.000 44.08701  ?  365 LEU   A N   1 
ATOM   8490  C CA  . LEU   E  1 365 ? 27.30817  70.64343  16.18719  1.000 20.97496  ?  365 LEU   A CA  1 
ATOM   8491  C C   . LEU   E  1 365 ? 27.00424  70.83045  17.66853  1.000 45.63061  ?  365 LEU   A C   1 
ATOM   8492  O O   . LEU   E  1 365 ? 27.07048  71.94938  18.19046  1.000 32.93179  ?  365 LEU   A O   1 
ATOM   8493  C CB  . LEU   E  1 365 ? 28.80764  70.78994  15.91809  1.000 35.07781  ?  365 LEU   A CB  1 
ATOM   8494  C CG  . LEU   E  1 365 ? 29.67800  69.65410  16.46223  1.000 38.63630  ?  365 LEU   A CG  1 
ATOM   8495  C CD1 . LEU   E  1 365 ? 29.28082  68.33113  15.79957  1.000 25.87079  ?  365 LEU   A CD1 1 
ATOM   8496  C CD2 . LEU   E  1 365 ? 31.14397  69.96748  16.25783  1.000 24.90811  ?  365 LEU   A CD2 1 
ATOM   8497  N N   . ILE   E  1 366 ? 26.62154  69.74117  18.33445  1.000 21.52009  ?  366 ILE   A N   1 
ATOM   8498  C CA  . ILE   E  1 366 ? 26.42703  69.73049  19.77660  1.000 35.84839  ?  366 ILE   A CA  1 
ATOM   8499  C C   . ILE   E  1 366 ? 27.27620  68.59825  20.32496  1.000 38.16038  ?  366 ILE   A C   1 
ATOM   8500  O O   . ILE   E  1 366 ? 27.77593  67.75035  19.58035  1.000 33.68491  ?  366 ILE   A O   1 
ATOM   8501  C CB  . ILE   E  1 366 ? 24.94829  69.54495  20.19932  1.000 29.21048  ?  366 ILE   A CB  1 
ATOM   8502  C CG1 . ILE   E  1 366 ? 24.44732  68.16176  19.80484  1.000 32.73486  ?  366 ILE   A CG1 1 
ATOM   8503  C CG2 . ILE   E  1 366 ? 24.05089  70.60936  19.60579  1.000 21.15389  ?  366 ILE   A CG2 1 
ATOM   8504  C CD1 . ILE   E  1 366 ? 23.20893  67.76463  20.55124  1.000 33.50505  ?  366 ILE   A CD1 1 
ATOM   8505  N N   . PHE   E  1 367 ? 27.43743  68.57839  21.64282  1.000 28.43872  ?  367 PHE   A N   1 
ATOM   8506  C CA  . PHE   E  1 367 ? 28.04453  67.40825  22.25257  1.000 25.40716  ?  367 PHE   A CA  1 
ATOM   8507  C C   . PHE   E  1 367 ? 27.20940  66.93945  23.43546  1.000 34.68208  ?  367 PHE   A C   1 
ATOM   8508  O O   . PHE   E  1 367 ? 26.45035  67.69875  24.04736  1.000 30.18853  ?  367 PHE   A O   1 
ATOM   8509  C CB  . PHE   E  1 367 ? 29.55128  67.63893  22.64616  1.000 24.37519  ?  367 PHE   A CB  1 
ATOM   8510  C CG  . PHE   E  1 367 ? 29.78630  68.49848  23.87907  1.000 16.38018  ?  367 PHE   A CG  1 
ATOM   8511  C CD1 . PHE   E  1 367 ? 29.46280  68.03539  25.15818  1.000 32.67312  ?  367 PHE   A CD1 1 
ATOM   8512  C CD2 . PHE   E  1 367 ? 30.43486  69.72862  23.76576  1.000 27.82171  ?  367 PHE   A CD2 1 
ATOM   8513  C CE1 . PHE   E  1 367 ? 29.71183  68.80958  26.29285  1.000 16.82906  ?  367 PHE   A CE1 1 
ATOM   8514  C CE2 . PHE   E  1 367 ? 30.70622  70.51587  24.90326  1.000 25.88299  ?  367 PHE   A CE2 1 
ATOM   8515  C CZ  . PHE   E  1 367 ? 30.35075  70.05988  26.16725  1.000 22.60515  ?  367 PHE   A CZ  1 
ATOM   8516  N N   . LEU   E  1 368 ? 27.33356  65.65235  23.70148  1.000 24.63321  ?  368 LEU   A N   1 
ATOM   8517  C CA  . LEU   E  1 368 ? 26.84160  65.00716  24.90013  1.000 15.58919  ?  368 LEU   A CA  1 
ATOM   8518  C C   . LEU   E  1 368 ? 28.03410  64.33624  25.57146  1.000 16.33811  ?  368 LEU   A C   1 
ATOM   8519  O O   . LEU   E  1 368 ? 28.88557  63.75083  24.88998  1.000 24.84984  ?  368 LEU   A O   1 
ATOM   8520  C CB  . LEU   E  1 368 ? 25.76723  63.97407  24.54589  1.000 13.25389  ?  368 LEU   A CB  1 
ATOM   8521  C CG  . LEU   E  1 368 ? 24.41541  64.53113  24.11927  1.000 23.85015  ?  368 LEU   A CG  1 
ATOM   8522  C CD1 . LEU   E  1 368 ? 23.61703  63.44899  23.41750  1.000 19.63110  ?  368 LEU   A CD1 1 
ATOM   8523  C CD2 . LEU   E  1 368 ? 23.64505  65.04504  25.33660  1.000 21.28501  ?  368 LEU   A CD2 1 
ATOM   8524  N N   . VAL   E  1 369 ? 28.12225  64.43643  26.89505  1.000 21.86926  ?  369 VAL   A N   1 
ATOM   8525  C CA  . VAL   E  1 369 ? 29.06271  63.62932  27.66787  1.000 24.20919  ?  369 VAL   A CA  1 
ATOM   8526  C C   . VAL   E  1 369 ? 28.25893  62.80976  28.67176  1.000 21.69338  ?  369 VAL   A C   1 
ATOM   8527  O O   . VAL   E  1 369 ? 27.53450  63.37457  29.50359  1.000 31.14032  ?  369 VAL   A O   1 
ATOM   8528  C CB  . VAL   E  1 369 ? 30.12416  64.48135  28.38544  1.000 30.44073  ?  369 VAL   A CB  1 
ATOM   8529  C CG1 . VAL   E  1 369 ? 31.12766  63.55946  29.10836  1.000 20.20824  ?  369 VAL   A CG1 1 
ATOM   8530  C CG2 . VAL   E  1 369 ? 30.83508  65.39159  27.40683  1.000 27.60204  ?  369 VAL   A CG2 1 
ATOM   8531  N N   . PHE   E  1 370 ? 28.39375  61.48654  28.60951  1.000 30.61699  ?  370 PHE   A N   1 
ATOM   8532  C CA  . PHE   E  1 370 ? 27.77904  60.60836  29.59965  1.000 12.26206  ?  370 PHE   A CA  1 
ATOM   8533  C C   . PHE   E  1 370 ? 28.81897  60.26182  30.66542  1.000 26.10281  ?  370 PHE   A C   1 
ATOM   8534  O O   . PHE   E  1 370 ? 29.87724  59.69770  30.35612  1.000 24.32553  ?  370 PHE   A O   1 
ATOM   8535  C CB  . PHE   E  1 370 ? 27.19460  59.37131  28.91584  1.000 19.74587  ?  370 PHE   A CB  1 
ATOM   8536  C CG  . PHE   E  1 370 ? 26.12733  59.71598  27.92764  1.000 29.75343  ?  370 PHE   A CG  1 
ATOM   8537  C CD1 . PHE   E  1 370 ? 24.85167  60.05828  28.36460  1.000 20.27829  ?  370 PHE   A CD1 1 
ATOM   8538  C CD2 . PHE   E  1 370 ? 26.40771  59.77527  26.56687  1.000 34.54078  ?  370 PHE   A CD2 1 
ATOM   8539  C CE1 . PHE   E  1 370 ? 23.85714  60.43026  27.45850  1.000 30.43739  ?  370 PHE   A CE1 1 
ATOM   8540  C CE2 . PHE   E  1 370 ? 25.40862  60.13796  25.64323  1.000 18.92297  ?  370 PHE   A CE2 1 
ATOM   8541  C CZ  . PHE   E  1 370 ? 24.13925  60.47476  26.09241  1.000 29.93096  ?  370 PHE   A CZ  1 
ATOM   8542  N N   . ILE   E  1 371 ? 28.52955  60.62645  31.91216  1.000 31.12446  ?  371 ILE   A N   1 
ATOM   8543  C CA  . ILE   E  1 371 ? 29.53224  60.70719  32.97567  1.000 26.90317  ?  371 ILE   A CA  1 
ATOM   8544  C C   . ILE   E  1 371 ? 29.27046  59.59728  33.99008  1.000 27.82290  ?  371 ILE   A C   1 
ATOM   8545  O O   . ILE   E  1 371 ? 28.19749  59.54388  34.60790  1.000 37.73018  ?  371 ILE   A O   1 
ATOM   8546  C CB  . ILE   E  1 371 ? 29.51406  62.09214  33.64536  1.000 36.01864  ?  371 ILE   A CB  1 
ATOM   8547  C CG1 . ILE   E  1 371 ? 29.66569  63.19399  32.58240  1.000 25.60636  ?  371 ILE   A CG1 1 
ATOM   8548  C CG2 . ILE   E  1 371 ? 30.60209  62.20002  34.72302  1.000 21.49151  ?  371 ILE   A CG2 1 
ATOM   8549  C CD1 . ILE   E  1 371 ? 28.99470  64.49637  32.97230  1.000 23.47351  ?  371 ILE   A CD1 1 
ATOM   8550  N N   . GLY   E  1 372 ? 30.25438  58.70895  34.16479  1.000 26.90806  ?  372 GLY   A N   1 
ATOM   8551  C CA  . GLY   E  1 372 ? 30.13053  57.65646  35.15398  1.000 18.20568  ?  372 GLY   A CA  1 
ATOM   8552  C C   . GLY   E  1 372 ? 30.22491  58.17941  36.57710  1.000 26.53442  ?  372 GLY   A C   1 
ATOM   8553  O O   . GLY   E  1 372 ? 30.73503  59.26831  36.84300  1.000 26.70659  ?  372 GLY   A O   1 
ATOM   8554  N N   . MET   E  1 373 ? 29.69156  57.38610  37.49989  1.000 23.67479  ?  373 MET   A N   1 
ATOM   8555  C CA  . MET   E  1 373 ? 29.77673  57.66685  38.92854  1.000 36.71029  ?  373 MET   A CA  1 
ATOM   8556  C C   . MET   E  1 373 ? 29.95894  56.34625  39.64739  1.000 34.46214  ?  373 MET   A C   1 
ATOM   8557  O O   . MET   E  1 373 ? 29.09749  55.46394  39.53728  1.000 29.75424  ?  373 MET   A O   1 
ATOM   8558  C CB  . MET   E  1 373 ? 28.53063  58.37890  39.44686  1.000 16.71396  ?  373 MET   A CB  1 
ATOM   8559  C CG  . MET   E  1 373 ? 28.34009  59.73088  38.82481  1.000 38.53797  ?  373 MET   A CG  1 
ATOM   8560  S SD  . MET   E  1 373 ? 26.79134  60.53400  39.33219  1.000 32.04802  ?  373 MET   A SD  1 
ATOM   8561  C CE  . MET   E  1 373 ? 26.90252  60.41021  41.11716  1.000 7.82943   ?  373 MET   A CE  1 
ATOM   8562  N N   . THR   E  1 374 ? 31.06938  56.22952  40.38788  1.000 23.41117  ?  374 THR   A N   1 
ATOM   8563  C CA  . THR   E  1 374 ? 31.47520  55.01004  41.08852  1.000 24.78286  ?  374 THR   A CA  1 
ATOM   8564  C C   . THR   E  1 374 ? 31.18796  53.77615  40.23184  1.000 21.69145  ?  374 THR   A C   1 
ATOM   8565  O O   . THR   E  1 374 ? 31.62155  53.71639  39.07850  1.000 32.31294  ?  374 THR   A O   1 
ATOM   8566  C CB  . THR   E  1 374 ? 30.81598  54.93667  42.48709  1.000 33.76067  ?  374 THR   A CB  1 
ATOM   8567  O OG1 . THR   E  1 374 ? 29.38417  54.83149  42.39884  1.000 28.71313  ?  374 THR   A OG1 1 
ATOM   8568  C CG2 . THR   E  1 374 ? 31.15189  56.18811  43.28122  1.000 18.33363  ?  374 THR   A CG2 1 
ATOM   8569  N N   . GLU   E  1 375 ? 30.45005  52.79920  40.75324  1.000 32.40644  ?  375 GLU   A N   1 
ATOM   8570  C CA  . GLU   E  1 375 ? 30.26711  51.54738  40.01844  1.000 19.93788  ?  375 GLU   A CA  1 
ATOM   8571  C C   . GLU   E  1 375 ? 29.29804  51.64840  38.83298  1.000 34.78498  ?  375 GLU   A C   1 
ATOM   8572  O O   . GLU   E  1 375 ? 29.22736  50.70381  38.03336  1.000 20.87855  ?  375 GLU   A O   1 
ATOM   8573  C CB  . GLU   E  1 375 ? 29.78236  50.45080  40.97029  1.000 32.79560  ?  375 GLU   A CB  1 
ATOM   8574  C CG  . GLU   E  1 375 ? 28.42435  50.77039  41.64275  1.000 21.45183  ?  375 GLU   A CG  1 
ATOM   8575  C CD  . GLU   E  1 375 ? 28.58238  51.27912  43.09021  1.000 31.81329  ?  375 GLU   A CD  1 
ATOM   8576  O OE1 . GLU   E  1 375 ? 29.16412  52.37176  43.28941  1.000 37.14711  ?  375 GLU   A OE1 1 
ATOM   8577  O OE2 . GLU   E  1 375 ? 28.12399  50.57806  44.02975  1.000 36.18984  -1 375 GLU   A OE2 1 
ATOM   8578  N N   . ILE   E  1 376 ? 28.53636  52.73679  38.69381  1.000 22.35965  ?  376 ILE   A N   1 
ATOM   8579  C CA  . ILE   E  1 376 ? 27.70383  52.89470  37.50254  1.000 22.58537  ?  376 ILE   A CA  1 
ATOM   8580  C C   . ILE   E  1 376 ? 28.45038  53.77093  36.50062  1.000 26.45609  ?  376 ILE   A C   1 
ATOM   8581  O O   . ILE   E  1 376 ? 28.18061  54.97068  36.37563  1.000 34.01461  ?  376 ILE   A O   1 
ATOM   8582  C CB  . ILE   E  1 376 ? 26.32036  53.47019  37.85531  1.000 33.50524  ?  376 ILE   A CB  1 
ATOM   8583  C CG1 . ILE   E  1 376 ? 25.66540  52.59706  38.93697  1.000 22.93775  ?  376 ILE   A CG1 1 
ATOM   8584  C CG2 . ILE   E  1 376 ? 25.44338  53.58891  36.59827  1.000 11.57849  ?  376 ILE   A CG2 1 
ATOM   8585  C CD1 . ILE   E  1 376 ? 24.41892  53.21844  39.56541  1.000 43.76723  ?  376 ILE   A CD1 1 
ATOM   8586  N N   . SER   E  1 377 ? 29.40865  53.17847  35.78588  1.000 29.31375  ?  377 SER   A N   1 
ATOM   8587  C CA  . SER   E  1 377 ? 30.32993  53.95740  34.97084  1.000 42.85262  ?  377 SER   A CA  1 
ATOM   8588  C C   . SER   E  1 377 ? 30.53646  53.40021  33.57056  1.000 26.83922  ?  377 SER   A C   1 
ATOM   8589  O O   . SER   E  1 377 ? 31.33940  53.95621  32.81291  1.000 51.07428  ?  377 SER   A O   1 
ATOM   8590  C CB  . SER   E  1 377 ? 31.68522  54.08821  35.68021  1.000 20.69239  ?  377 SER   A CB  1 
ATOM   8591  O OG  . SER   E  1 377 ? 31.55024  54.96817  36.78550  1.000 26.77004  ?  377 SER   A OG  1 
ATOM   8592  N N   . THR   E  1 378 ? 29.83043  52.34037  33.19979  1.000 40.16623  ?  378 THR   A N   1 
ATOM   8593  C CA  . THR   E  1 378 ? 29.88381  51.84281  31.83361  1.000 26.29177  ?  378 THR   A CA  1 
ATOM   8594  C C   . THR   E  1 378 ? 28.90325  52.60727  30.93828  1.000 41.65189  ?  378 THR   A C   1 
ATOM   8595  O O   . THR   E  1 378 ? 27.71471  52.75696  31.26631  1.000 33.38611  ?  378 THR   A O   1 
ATOM   8596  C CB  . THR   E  1 378 ? 29.58987  50.34376  31.80352  1.000 38.81455  ?  378 THR   A CB  1 
ATOM   8597  O OG1 . THR   E  1 378 ? 30.66726  49.63934  32.43575  1.000 33.60865  ?  378 THR   A OG1 1 
ATOM   8598  C CG2 . THR   E  1 378 ? 29.48412  49.87976  30.38022  1.000 14.02627  ?  378 THR   A CG2 1 
ATOM   8599  N N   . CYS   E  1 379 ? 29.41096  53.08799  29.80172  1.000 23.91817  ?  379 CYS   A N   1 
ATOM   8600  C CA  . CYS   E  1 379 ? 28.65440  53.91590  28.86281  1.000 22.20034  ?  379 CYS   A CA  1 
ATOM   8601  C C   . CYS   E  1 379 ? 28.59083  53.15909  27.54170  1.000 30.27039  ?  379 CYS   A C   1 
ATOM   8602  O O   . CYS   E  1 379 ? 29.54530  53.17458  26.75703  1.000 35.63298  ?  379 CYS   A O   1 
ATOM   8603  C CB  . CYS   E  1 379 ? 29.30773  55.28559  28.69070  1.000 22.78162  ?  379 CYS   A CB  1 
ATOM   8604  S SG  . CYS   E  1 379 ? 29.46453  56.21888  30.24027  1.000 34.30685  ?  379 CYS   A SG  1 
ATOM   8605  N N   . GLU   E  1 380 ? 27.47370  52.48682  27.29408  1.000 29.99395  ?  380 GLU   A N   1 
ATOM   8606  C CA  . GLU   E  1 380 ? 27.27848  51.76766  26.04390  1.000 15.49775  ?  380 GLU   A CA  1 
ATOM   8607  C C   . GLU   E  1 380 ? 26.49731  52.63538  25.06434  1.000 31.79043  ?  380 GLU   A C   1 
ATOM   8608  O O   . GLU   E  1 380 ? 25.33536  52.98263  25.32285  1.000 30.65014  ?  380 GLU   A O   1 
ATOM   8609  C CB  . GLU   E  1 380 ? 26.54696  50.44696  26.25116  1.000 26.97433  ?  380 GLU   A CB  1 
ATOM   8610  C CG  . GLU   E  1 380 ? 26.30844  49.78138  24.92193  1.000 39.74515  ?  380 GLU   A CG  1 
ATOM   8611  C CD  . GLU   E  1 380 ? 25.48247  48.53266  25.00743  1.000 35.51959  ?  380 GLU   A CD  1 
ATOM   8612  O OE1 . GLU   E  1 380 ? 24.91188  48.26626  26.09026  1.000 40.54555  ?  380 GLU   A OE1 1 
ATOM   8613  O OE2 . GLU   E  1 380 ? 25.40892  47.83084  23.97447  1.000 47.63596  -1 380 GLU   A OE2 1 
ATOM   8614  N N   . ALA   E  1 381 ? 27.13981  52.98120  23.94642  1.000 23.17358  ?  381 ALA   A N   1 
ATOM   8615  C CA  . ALA   E  1 381 ? 26.43392  53.53378  22.79660  1.000 41.67173  ?  381 ALA   A CA  1 
ATOM   8616  C C   . ALA   E  1 381 ? 25.79253  52.39967  21.99652  1.000 32.06151  ?  381 ALA   A C   1 
ATOM   8617  O O   . ALA   E  1 381 ? 26.43071  51.37142  21.73093  1.000 32.67704  ?  381 ALA   A O   1 
ATOM   8618  C CB  . ALA   E  1 381 ? 27.39437  54.33347  21.90922  1.000 22.15337  ?  381 ALA   A CB  1 
ATOM   8619  N N   . THR   E  1 382 ? 24.52672  52.57923  21.62134  1.000 31.55086  ?  382 THR   A N   1 
ATOM   8620  C CA  . THR   E  1 382 ? 23.86532  51.67929  20.67895  1.000 31.13291  ?  382 THR   A CA  1 
ATOM   8621  C C   . THR   E  1 382 ? 23.65991  52.32127  19.30629  1.000 26.26612  ?  382 THR   A C   1 
ATOM   8622  O O   . THR   E  1 382 ? 22.84169  51.84476  18.51265  1.000 53.80820  ?  382 THR   A O   1 
ATOM   8623  C CB  . THR   E  1 382 ? 22.53477  51.20629  21.25359  1.000 20.84536  ?  382 THR   A CB  1 
ATOM   8624  O OG1 . THR   E  1 382 ? 21.69416  52.34461  21.53578  1.000 29.73707  ?  382 THR   A OG1 1 
ATOM   8625  C CG2 . THR   E  1 382 ? 22.78170  50.40700  22.53565  1.000 31.63300  ?  382 THR   A CG2 1 
ATOM   8626  N N   . VAL   E  1 383 ? 24.36144  53.41915  19.03406  1.000 28.16025  ?  383 VAL   A N   1 
ATOM   8627  C CA  . VAL   E  1 383 ? 24.37795  54.05268  17.72671  1.000 17.49847  ?  383 VAL   A CA  1 
ATOM   8628  C C   . VAL   E  1 383 ? 25.81576  54.03649  17.22278  1.000 31.50048  ?  383 VAL   A C   1 
ATOM   8629  O O   . VAL   E  1 383 ? 26.76350  53.79791  17.97479  1.000 27.25229  ?  383 VAL   A O   1 
ATOM   8630  C CB  . VAL   E  1 383 ? 23.82776  55.49237  17.74581  1.000 38.21085  ?  383 VAL   A CB  1 
ATOM   8631  C CG1 . VAL   E  1 383 ? 22.36845  55.49700  18.11859  1.000 18.26413  ?  383 VAL   A CG1 1 
ATOM   8632  C CG2 . VAL   E  1 383 ? 24.63840  56.35865  18.69880  1.000 22.97319  ?  383 VAL   A CG2 1 
ATOM   8633  N N   . SER   E  1 384 ? 25.96715  54.28713  15.92813  1.000 41.46697  ?  384 SER   A N   1 
ATOM   8634  C CA  . SER   E  1 384 ? 27.26596  54.22542  15.27461  1.000 21.98789  ?  384 SER   A CA  1 
ATOM   8635  C C   . SER   E  1 384 ? 27.60014  55.58175  14.67743  1.000 46.38523  ?  384 SER   A C   1 
ATOM   8636  O O   . SER   E  1 384 ? 26.70459  56.37444  14.34733  1.000 35.15133  ?  384 SER   A O   1 
ATOM   8637  C CB  . SER   E  1 384 ? 27.28044  53.15509  14.18122  1.000 24.38464  ?  384 SER   A CB  1 
ATOM   8638  O OG  . SER   E  1 384 ? 26.82071  51.91631  14.70650  1.000 51.59033  ?  384 SER   A OG  1 
ATOM   8639  N N   . GLU   E  1 385 ? 28.89446  55.85811  14.54771  1.000 36.93048  ?  385 GLU   A N   1 
ATOM   8640  C CA  . GLU   E  1 385 ? 29.27445  57.08133  13.85495  1.000 45.65881  ?  385 GLU   A CA  1 
ATOM   8641  C C   . GLU   E  1 385 ? 28.68751  57.05767  12.44281  1.000 45.27600  ?  385 GLU   A C   1 
ATOM   8642  O O   . GLU   E  1 385 ? 28.63476  56.01259  11.78229  1.000 43.23197  ?  385 GLU   A O   1 
ATOM   8643  C CB  . GLU   E  1 385 ? 30.79460  57.23008  13.82926  1.000 23.59883  ?  385 GLU   A CB  1 
ATOM   8644  C CG  . GLU   E  1 385 ? 31.44231  57.19814  15.21851  1.000 37.39848  ?  385 GLU   A CG  1 
ATOM   8645  C CD  . GLU   E  1 385 ? 32.93075  57.54172  15.18947  1.000 54.30783  ?  385 GLU   A CD  1 
ATOM   8646  O OE1 . GLU   E  1 385 ? 33.54561  57.38831  14.10694  1.000 52.69689  ?  385 GLU   A OE1 1 
ATOM   8647  O OE2 . GLU   E  1 385 ? 33.48030  57.97337  16.23967  1.000 39.85855  -1 385 GLU   A OE2 1 
ATOM   8648  N N   . GLY   E  1 386 ? 28.17043  58.20102  12.01130  1.000 27.24256  ?  386 GLY   A N   1 
ATOM   8649  C CA  . GLY   E  1 386 ? 27.54420  58.32160  10.71236  1.000 13.39922  ?  386 GLY   A CA  1 
ATOM   8650  C C   . GLY   E  1 386 ? 26.05143  58.04851  10.68530  1.000 32.10841  ?  386 GLY   A C   1 
ATOM   8651  O O   . GLY   E  1 386 ? 25.36704  58.49164  9.76095   1.000 26.69320  ?  386 GLY   A O   1 
ATOM   8652  N N   . GLN   E  1 387 ? 25.53219  57.33466  11.66890  1.000 27.47235  ?  387 GLN   A N   1 
ATOM   8653  C CA  . GLN   E  1 387 ? 24.11383  57.01752  11.72641  1.000 24.16307  ?  387 GLN   A CA  1 
ATOM   8654  C C   . GLN   E  1 387 ? 23.26242  58.27018  11.94958  1.000 43.39825  ?  387 GLN   A C   1 
ATOM   8655  O O   . GLN   E  1 387 ? 23.69205  59.23733  12.59227  1.000 36.53472  ?  387 GLN   A O   1 
ATOM   8656  C CB  . GLN   E  1 387 ? 23.88752  56.01197  12.84996  1.000 23.01875  ?  387 GLN   A CB  1 
ATOM   8657  C CG  . GLN   E  1 387 ? 22.48294  55.60954  13.09841  1.000 23.58245  ?  387 GLN   A CG  1 
ATOM   8658  C CD  . GLN   E  1 387 ? 22.42273  54.56658  14.18072  1.000 31.58291  ?  387 GLN   A CD  1 
ATOM   8659  O OE1 . GLN   E  1 387 ? 23.44384  53.95081  14.52764  1.000 36.54608  ?  387 GLN   A OE1 1 
ATOM   8660  N NE2 . GLN   E  1 387 ? 21.23554  54.37457  14.74671  1.000 24.96307  ?  387 GLN   A NE2 1 
ATOM   8661  N N   . HIS   E  1 388 ? 22.04308  58.25326  11.39843  1.000 29.71530  ?  388 HIS   A N   1 
ATOM   8662  C CA  . HIS   E  1 388 ? 21.06520  59.30757  11.64704  1.000 41.00912  ?  388 HIS   A CA  1 
ATOM   8663  C C   . HIS   E  1 388 ? 20.08718  58.85761  12.72356  1.000 54.65877  ?  388 HIS   A C   1 
ATOM   8664  O O   . HIS   E  1 388 ? 19.75010  57.67128  12.81902  1.000 28.74182  ?  388 HIS   A O   1 
ATOM   8665  C CB  . HIS   E  1 388 ? 20.29317  59.67118  10.38568  1.000 19.02622  ?  388 HIS   A CB  1 
ATOM   8666  C CG  . HIS   E  1 388 ? 19.34143  60.81256  10.56336  1.000 36.35879  ?  388 HIS   A CG  1 
ATOM   8667  N ND1 . HIS   E  1 388 ? 18.03337  60.64114  10.97595  1.000 37.31725  ?  388 HIS   A ND1 1 
ATOM   8668  C CD2 . HIS   E  1 388 ? 19.50708  62.14471  10.37941  1.000 25.29005  ?  388 HIS   A CD2 1 
ATOM   8669  C CE1 . HIS   E  1 388 ? 17.43852  61.82014  11.04574  1.000 33.63296  ?  388 HIS   A CE1 1 
ATOM   8670  N NE2 . HIS   E  1 388 ? 18.30904  62.74927  10.68514  1.000 29.57403  ?  388 HIS   A NE2 1 
ATOM   8671  N N   . VAL   E  1 389 ? 19.65201  59.81026  13.54751  1.000 20.61236  ?  389 VAL   A N   1 
ATOM   8672  C CA  . VAL   E  1 389 ? 18.69407  59.55204  14.61750  1.000 33.01555  ?  389 VAL   A CA  1 
ATOM   8673  C C   . VAL   E  1 389 ? 17.72227  60.72073  14.68792  1.000 31.95913  ?  389 VAL   A C   1 
ATOM   8674  O O   . VAL   E  1 389 ? 18.03618  61.85063  14.28679  1.000 46.09263  ?  389 VAL   A O   1 
ATOM   8675  C CB  . VAL   E  1 389 ? 19.36995  59.32829  16.00166  1.000 38.20240  ?  389 VAL   A CB  1 
ATOM   8676  C CG1 . VAL   E  1 389 ? 20.28271  58.07964  15.98307  1.000 23.00119  ?  389 VAL   A CG1 1 
ATOM   8677  C CG2 . VAL   E  1 389 ? 20.14678  60.55796  16.44387  1.000 17.28858  ?  389 VAL   A CG2 1 
ATOM   8678  N N   . ASN   E  1 390 ? 16.52794  60.42695  15.19554  1.000 24.37582  ?  390 ASN   A N   1 
ATOM   8679  C CA  . ASN   E  1 390 ? 15.51226  61.42512  15.50390  1.000 27.83917  ?  390 ASN   A CA  1 
ATOM   8680  C C   . ASN   E  1 390 ? 15.46004  61.66047  17.00282  1.000 53.20206  ?  390 ASN   A C   1 
ATOM   8681  O O   . ASN   E  1 390 ? 15.70159  60.74767  17.80237  1.000 30.67593  ?  390 ASN   A O   1 
ATOM   8682  C CB  . ASN   E  1 390 ? 14.12575  60.99287  15.01081  1.000 40.53967  ?  390 ASN   A CB  1 
ATOM   8683  C CG  . ASN   E  1 390 ? 14.03109  60.96875  13.49382  1.000 34.08762  ?  390 ASN   A CG  1 
ATOM   8684  O OD1 . ASN   E  1 390 ? 14.50472  61.88591  12.80497  1.000 44.57171  ?  390 ASN   A OD1 1 
ATOM   8685  N ND2 . ASN   E  1 390 ? 13.44866  59.90509  12.96423  1.000 44.02449  ?  390 ASN   A ND2 1 
ATOM   8686  N N   . ARG   E  1 391 ? 15.16192  62.90548  17.36881  1.000 27.63140  ?  391 ARG   A N   1 
ATOM   8687  C CA  . ARG   E  1 391 ? 14.93120  63.28465  18.75491  1.000 38.22608  ?  391 ARG   A CA  1 
ATOM   8688  C C   . ARG   E  1 391 ? 14.05116  62.24907  19.45633  1.000 26.23341  ?  391 ARG   A C   1 
ATOM   8689  O O   . ARG   E  1 391 ? 12.95511  61.92867  18.98555  1.000 36.91305  ?  391 ARG   A O   1 
ATOM   8690  C CB  . ARG   E  1 391 ? 14.28512  64.67424  18.77353  1.000 17.60311  ?  391 ARG   A CB  1 
ATOM   8691  C CG  . ARG   E  1 391 ? 14.24075  65.39242  20.11294  1.000 27.27319  ?  391 ARG   A CG  1 
ATOM   8692  C CD  . ARG   E  1 391 ? 14.07095  66.90021  19.92446  1.000 36.86105  ?  391 ARG   A CD  1 
ATOM   8693  N NE  . ARG   E  1 391 ? 12.78904  67.28882  19.34595  1.000 29.22135  ?  391 ARG   A NE  1 
ATOM   8694  C CZ  . ARG   E  1 391 ? 11.73560  67.65506  20.06622  1.000 70.79089  ?  391 ARG   A CZ  1 
ATOM   8695  N NH1 . ARG   E  1 391 ? 11.75652  67.62875  21.38742  1.000 30.18633  ?  391 ARG   A NH1 1 
ATOM   8696  N NH2 . ARG   E  1 391 ? 10.63157  68.05880  19.44991  1.000 31.13417  ?  391 ARG   A NH2 1 
ATOM   8697  N N   . GLY   E  1 392 ? 14.57792  61.65246  20.53862  1.000 26.47975  ?  392 GLY   A N   1 
ATOM   8698  C CA  . GLY   E  1 392 ? 13.87607  60.65039  21.32774  1.000 22.90758  ?  392 GLY   A CA  1 
ATOM   8699  C C   . GLY   E  1 392 ? 14.28474  59.20802  21.07710  1.000 31.68858  ?  392 GLY   A C   1 
ATOM   8700  O O   . GLY   E  1 392 ? 13.88209  58.32438  21.85561  1.000 30.26431  ?  392 GLY   A O   1 
ATOM   8701  N N   . ASP   E  1 393 ? 15.07465  58.94258  20.02858  1.000 22.33601  ?  393 ASP   A N   1 
ATOM   8702  C CA  . ASP   E  1 393 ? 15.56413  57.59069  19.75412  1.000 35.02624  ?  393 ASP   A CA  1 
ATOM   8703  C C   . ASP   E  1 393 ? 16.64598  57.18589  20.75968  1.000 29.58169  ?  393 ASP   A C   1 
ATOM   8704  O O   . ASP   E  1 393 ? 17.27674  58.03107  21.40500  1.000 48.63656  ?  393 ASP   A O   1 
ATOM   8705  C CB  . ASP   E  1 393 ? 16.13354  57.49614  18.33185  1.000 25.66590  ?  393 ASP   A CB  1 
ATOM   8706  C CG  . ASP   E  1 393 ? 15.09642  57.80365  17.23845  1.000 54.55379  ?  393 ASP   A CG  1 
ATOM   8707  O OD1 . ASP   E  1 393 ? 13.88599  57.97004  17.53427  1.000 51.15584  ?  393 ASP   A OD1 1 
ATOM   8708  O OD2 . ASP   E  1 393 ? 15.50865  57.88046  16.06096  1.000 39.25659  -1 393 ASP   A OD2 1 
ATOM   8709  N N   . ASP   E  1 394 ? 16.87940  55.87443  20.87382  1.000 47.07068  ?  394 ASP   A N   1 
ATOM   8710  C CA  . ASP   E  1 394 ? 17.94342  55.38920  21.75454  1.000 22.78739  ?  394 ASP   A CA  1 
ATOM   8711  C C   . ASP   E  1 394 ? 19.31158  55.85724  21.25907  1.000 49.46974  ?  394 ASP   A C   1 
ATOM   8712  O O   . ASP   E  1 394 ? 19.61980  55.74089  20.06857  1.000 32.29466  ?  394 ASP   A O   1 
ATOM   8713  C CB  . ASP   E  1 394 ? 17.92765  53.85889  21.83917  1.000 42.28560  ?  394 ASP   A CB  1 
ATOM   8714  C CG  . ASP   E  1 394 ? 16.61767  53.30201  22.37036  1.000 31.78752  ?  394 ASP   A CG  1 
ATOM   8715  O OD1 . ASP   E  1 394 ? 16.00458  53.91974  23.28080  1.000 76.14657  ?  394 ASP   A OD1 1 
ATOM   8716  O OD2 . ASP   E  1 394 ? 16.21782  52.21995  21.88872  1.000 71.39667  -1 394 ASP   A OD2 1 
ATOM   8717  N N   . LEU   E  1 395 ? 20.13335  56.40015  22.16515  1.000 23.53753  ?  395 LEU   A N   1 
ATOM   8718  C CA  . LEU   E  1 395 ? 21.55565  56.55882  21.86531  1.000 42.47880  ?  395 LEU   A CA  1 
ATOM   8719  C C   . LEU   E  1 395 ? 22.39572  55.48442  22.51887  1.000 35.41389  ?  395 LEU   A C   1 
ATOM   8720  O O   . LEU   E  1 395 ? 23.47260  55.14006  22.00715  1.000 32.87897  ?  395 LEU   A O   1 
ATOM   8721  C CB  . LEU   E  1 395 ? 22.09167  57.91492  22.33366  1.000 19.94852  ?  395 LEU   A CB  1 
ATOM   8722  C CG  . LEU   E  1 395 ? 21.67654  59.18856  21.62264  1.000 34.42313  ?  395 LEU   A CG  1 
ATOM   8723  C CD1 . LEU   E  1 395 ? 22.38600  60.31161  22.30965  1.000 19.42017  ?  395 LEU   A CD1 1 
ATOM   8724  C CD2 . LEU   E  1 395 ? 22.02086  59.12863  20.14380  1.000 29.45040  ?  395 LEU   A CD2 1 
ATOM   8725  N N   . GLY   E  1 396 ? 21.91840  54.96450  23.64061  1.000 21.09174  ?  396 GLY   A N   1 
ATOM   8726  C CA  . GLY   E  1 396 ? 22.66932  53.99020  24.40413  1.000 29.49036  ?  396 GLY   A CA  1 
ATOM   8727  C C   . GLY   E  1 396 ? 22.15682  53.99596  25.82744  1.000 25.65848  ?  396 GLY   A C   1 
ATOM   8728  O O   . GLY   E  1 396 ? 21.01894  54.40133  26.08586  1.000 29.10957  ?  396 GLY   A O   1 
ATOM   8729  N N   . MET   E  1 397 ? 23.02530  53.57313  26.74320  1.000 25.00246  ?  397 MET   A N   1 
ATOM   8730  C CA  . MET   E  1 397 ? 22.58921  53.47059  28.12863  1.000 23.87936  ?  397 MET   A CA  1 
ATOM   8731  C C   . MET   E  1 397 ? 23.78710  53.32427  29.05399  1.000 39.38972  ?  397 MET   A C   1 
ATOM   8732  O O   . MET   E  1 397 ? 24.91053  53.04132  28.62194  1.000 28.61856  ?  397 MET   A O   1 
ATOM   8733  C CB  . MET   E  1 397 ? 21.64052  52.29078  28.31091  1.000 21.70368  ?  397 MET   A CB  1 
ATOM   8734  C CG  . MET   E  1 397 ? 22.35478  50.95656  28.43050  1.000 26.18453  ?  397 MET   A CG  1 
ATOM   8735  S SD  . MET   E  1 397 ? 21.25482  49.69978  27.81363  1.000 36.58555  ?  397 MET   A SD  1 
ATOM   8736  C CE  . MET   E  1 397 ? 21.37307  49.99663  26.05998  1.000 14.83119  ?  397 MET   A CE  1 
ATOM   8737  N N   . PHE   E  1 398 ? 23.51487  53.52679  30.34425  1.000 25.61018  ?  398 PHE   A N   1 
ATOM   8738  C CA  . PHE   E  1 398 ? 24.44601  53.25131  31.42637  1.000 18.89252  ?  398 PHE   A CA  1 
ATOM   8739  C C   . PHE   E  1 398 ? 24.32876  51.79770  31.90022  1.000 28.67191  ?  398 PHE   A C   1 
ATOM   8740  O O   . PHE   E  1 398 ? 23.25813  51.19056  31.85337  1.000 38.38236  ?  398 PHE   A O   1 
ATOM   8741  C CB  . PHE   E  1 398 ? 24.16803  54.17319  32.61687  1.000 18.97437  ?  398 PHE   A CB  1 
ATOM   8742  C CG  . PHE   E  1 398 ? 24.50343  55.61252  32.38720  1.000 32.62052  ?  398 PHE   A CG  1 
ATOM   8743  C CD1 . PHE   E  1 398 ? 25.83754  56.04011  32.38703  1.000 19.28831  ?  398 PHE   A CD1 1 
ATOM   8744  C CD2 . PHE   E  1 398 ? 23.48630  56.56262  32.24227  1.000 26.04647  ?  398 PHE   A CD2 1 
ATOM   8745  C CE1 . PHE   E  1 398 ? 26.15713  57.39412  32.20415  1.000 31.32838  ?  398 PHE   A CE1 1 
ATOM   8746  C CE2 . PHE   E  1 398 ? 23.78957  57.92837  32.06340  1.000 22.09116  ?  398 PHE   A CE2 1 
ATOM   8747  C CZ  . PHE   E  1 398 ? 25.12338  58.34426  32.04390  1.000 29.42723  ?  398 PHE   A CZ  1 
ATOM   8748  N N   . HIS   E  1 399 ? 25.43684  51.25255  32.39874  1.000 37.61474  ?  399 HIS   A N   1 
ATOM   8749  C CA  . HIS   E  1 399 ? 25.41428  49.97362  33.09996  1.000 46.00844  ?  399 HIS   A CA  1 
ATOM   8750  C C   . HIS   E  1 399 ? 26.30488  50.05955  34.32747  1.000 24.46770  ?  399 HIS   A C   1 
ATOM   8751  O O   . HIS   E  1 399 ? 27.28368  50.81014  34.34966  1.000 52.86627  ?  399 HIS   A O   1 
ATOM   8752  C CB  . HIS   E  1 399 ? 25.93639  48.76750  32.26699  1.000 21.96852  ?  399 HIS   A CB  1 
ATOM   8753  C CG  . HIS   E  1 399 ? 25.26128  48.57279  30.94361  1.000 25.72231  ?  399 HIS   A CG  1 
ATOM   8754  N ND1 . HIS   E  1 399 ? 24.11766  47.81731  30.79195  1.000 33.76723  ?  399 HIS   A ND1 1 
ATOM   8755  C CD2 . HIS   E  1 399 ? 25.59297  49.00930  29.70240  1.000 41.15053  ?  399 HIS   A CD2 1 
ATOM   8756  C CE1 . HIS   E  1 399 ? 23.76029  47.81682  29.51893  1.000 51.42029  ?  399 HIS   A CE1 1 
ATOM   8757  N NE2 . HIS   E  1 399 ? 24.64356  48.52458  28.83513  1.000 22.63126  ?  399 HIS   A NE2 1 
ATOM   8758  N N   . PHE   E  1 400 ? 25.98774  49.24069  35.32889  1.000 37.82909  ?  400 PHE   A N   1 
ATOM   8759  C CA  . PHE   E  1 400 ? 26.99466  48.87020  36.31135  1.000 19.29819  ?  400 PHE   A CA  1 
ATOM   8760  C C   . PHE   E  1 400 ? 28.20073  48.29456  35.57498  1.000 27.92873  ?  400 PHE   A C   1 
ATOM   8761  O O   . PHE   E  1 400 ? 28.05843  47.42253  34.70966  1.000 38.41880  ?  400 PHE   A O   1 
ATOM   8762  C CB  . PHE   E  1 400 ? 26.42346  47.84955  37.30117  1.000 36.97595  ?  400 PHE   A CB  1 
ATOM   8763  C CG  . PHE   E  1 400 ? 25.57667  48.45701  38.38116  1.000 16.90293  ?  400 PHE   A CG  1 
ATOM   8764  C CD1 . PHE   E  1 400 ? 24.30718  48.96057  38.09240  1.000 35.94718  ?  400 PHE   A CD1 1 
ATOM   8765  C CD2 . PHE   E  1 400 ? 26.04722  48.53934  39.68957  1.000 36.94024  ?  400 PHE   A CD2 1 
ATOM   8766  C CE1 . PHE   E  1 400 ? 23.53044  49.54862  39.08306  1.000 20.61509  ?  400 PHE   A CE1 1 
ATOM   8767  C CE2 . PHE   E  1 400 ? 25.26595  49.11610  40.69758  1.000 32.78614  ?  400 PHE   A CE2 1 
ATOM   8768  C CZ  . PHE   E  1 400 ? 24.01235  49.62261  40.38860  1.000 35.70120  ?  400 PHE   A CZ  1 
ATOM   8769  N N   . GLY   E  1 401 ? 29.37489  48.81498  35.88404  1.000 33.99531  ?  401 GLY   A N   1 
ATOM   8770  C CA  . GLY   E  1 401 ? 30.59414  48.38367  35.22782  1.000 29.92383  ?  401 GLY   A CA  1 
ATOM   8771  C C   . GLY   E  1 401 ? 31.60474  49.50992  35.21182  1.000 40.38303  ?  401 GLY   A C   1 
ATOM   8772  O O   . GLY   E  1 401 ? 31.36967  50.59469  35.74392  1.000 46.57585  ?  401 GLY   A O   1 
ATOM   8773  N N   . GLY   E  1 402 ? 32.74364  49.22587  34.57830  1.000 30.10656  ?  402 GLY   A N   1 
ATOM   8774  C CA  . GLY   E  1 402 ? 33.83415  50.19271  34.48479  1.000 22.71222  ?  402 GLY   A CA  1 
ATOM   8775  C C   . GLY   E  1 402 ? 33.74324  51.12080  33.27783  1.000 51.95036  ?  402 GLY   A C   1 
ATOM   8776  O O   . GLY   E  1 402 ? 34.47319  52.12447  33.12777  1.000 33.56844  ?  402 GLY   A O   1 
ATOM   8777  O OXT . GLY   E  1 402 ? 32.90398  50.88424  32.40196  1.000 42.75178  -1 402 GLY   A OXT 1 
ATOM   8778  N N   . SER   F  2 1   ? 25.45660  60.32400  35.35106  1.000 17.34576  ?  404 SER   B N   1 
ATOM   8779  C CA  . SER   F  2 1   ? 25.30543  61.75230  35.04053  1.000 12.46543  ?  404 SER   B CA  1 
ATOM   8780  C C   . SER   F  2 1   ? 25.49262  62.02368  33.54279  1.000 23.89063  ?  404 SER   B C   1 
ATOM   8781  O O   . SER   F  2 1   ? 26.10854  61.22456  32.84309  1.000 27.40607  ?  404 SER   B O   1 
ATOM   8782  C CB  . SER   F  2 1   ? 26.30015  62.58751  35.87336  1.000 18.74063  ?  404 SER   B CB  1 
ATOM   8783  O OG  . SER   F  2 1   ? 26.14353  63.98415  35.65589  1.000 21.47893  ?  404 SER   B OG  1 
ATOM   8784  N N   . PHE   F  2 2   ? 24.96246  63.14091  33.03840  1.000 17.20652  ?  405 PHE   B N   1 
ATOM   8785  C CA  . PHE   F  2 2   ? 25.13800  63.47642  31.62755  1.000 23.48130  ?  405 PHE   B CA  1 
ATOM   8786  C C   . PHE   F  2 2   ? 25.25294  64.98823  31.46616  1.000 21.15219  ?  405 PHE   B C   1 
ATOM   8787  O O   . PHE   F  2 2   ? 24.73954  65.75840  32.29019  1.000 30.45032  ?  405 PHE   B O   1 
ATOM   8788  C CB  . PHE   F  2 2   ? 23.98520  62.94029  30.75985  1.000 24.16211  ?  405 PHE   B CB  1 
ATOM   8789  C CG  . PHE   F  2 2   ? 22.85459  63.91326  30.58743  1.000 26.63450  ?  405 PHE   B CG  1 
ATOM   8790  C CD1 . PHE   F  2 2   ? 21.87061  64.04813  31.57302  1.000 32.92779  ?  405 PHE   B CD1 1 
ATOM   8791  C CD2 . PHE   F  2 2   ? 22.78237  64.71000  29.44230  1.000 30.06985  ?  405 PHE   B CD2 1 
ATOM   8792  C CE1 . PHE   F  2 2   ? 20.82491  64.95904  31.42456  1.000 26.65649  ?  405 PHE   B CE1 1 
ATOM   8793  C CE2 . PHE   F  2 2   ? 21.74178  65.63121  29.27777  1.000 22.79385  ?  405 PHE   B CE2 1 
ATOM   8794  C CZ  . PHE   F  2 2   ? 20.74767  65.74707  30.28037  1.000 28.98179  ?  405 PHE   B CZ  1 
ATOM   8795  N N   . ALA   F  2 3   ? 25.91274  65.40733  30.37692  1.000 19.97917  ?  406 ALA   B N   1 
ATOM   8796  C CA  . ALA   F  2 3   ? 26.04581  66.82080  30.06155  1.000 24.23106  ?  406 ALA   B CA  1 
ATOM   8797  C C   . ALA   F  2 3   ? 25.79180  67.06232  28.58259  1.000 27.37127  ?  406 ALA   B C   1 
ATOM   8798  O O   . ALA   F  2 3   ? 26.27305  66.31140  27.72252  1.000 26.27987  ?  406 ALA   B O   1 
ATOM   8799  C CB  . ALA   F  2 3   ? 27.41911  67.36070  30.44283  1.000 8.03108   ?  406 ALA   B CB  1 
ATOM   8800  N N   . LEU   F  2 4   ? 25.03056  68.12606  28.30766  1.000 34.45462  ?  407 LEU   B N   1 
ATOM   8801  C CA  . LEU   F  2 4   ? 24.75748  68.61508  26.96343  1.000 33.73231  ?  407 LEU   B CA  1 
ATOM   8802  C C   . LEU   F  2 4   ? 25.59088  69.86722  26.72825  1.000 18.95065  ?  407 LEU   B C   1 
ATOM   8803  O O   . LEU   F  2 4   ? 25.60303  70.76819  27.57352  1.000 38.50788  ?  407 LEU   B O   1 
ATOM   8804  C CB  . LEU   F  2 4   ? 23.26704  68.92379  26.79232  1.000 22.68044  ?  407 LEU   B CB  1 
ATOM   8805  C CG  . LEU   F  2 4   ? 22.89652  69.72858  25.54376  1.000 34.40915  ?  407 LEU   B CG  1 
ATOM   8806  C CD1 . LEU   F  2 4   ? 23.10459  68.88115  24.27591  1.000 20.80389  ?  407 LEU   B CD1 1 
ATOM   8807  C CD2 . LEU   F  2 4   ? 21.47401  70.23509  25.65700  1.000 26.75135  ?  407 LEU   B CD2 1 
ATOM   8808  N N   . GLY   F  2 5   ? 26.29587  69.91369  25.59198  1.000 37.90867  ?  408 GLY   B N   1 
ATOM   8809  C CA  . GLY   F  2 5   ? 27.14452  71.04873  25.24692  1.000 14.62105  ?  408 GLY   B CA  1 
ATOM   8810  C C   . GLY   F  2 5   ? 26.70823  71.79240  23.99280  1.000 30.14560  ?  408 GLY   B C   1 
ATOM   8811  O O   . GLY   F  2 5   ? 26.49454  71.18697  22.92983  1.000 36.47030  ?  408 GLY   B O   1 
ATOM   8812  N N   . LEU   F  2 6   ? 26.56847  73.11438  24.11138  1.000 20.92680  ?  409 LEU   B N   1 
ATOM   8813  C CA  . LEU   F  2 6   ? 26.18059  73.98647  23.00752  1.000 40.28230  ?  409 LEU   B CA  1 
ATOM   8814  C C   . LEU   F  2 6   ? 27.28506  74.99571  22.72444  1.000 33.67841  ?  409 LEU   B C   1 
ATOM   8815  O O   . LEU   F  2 6   ? 27.87373  75.56214  23.65614  1.000 38.74388  ?  409 LEU   B O   1 
ATOM   8816  C CB  . LEU   F  2 6   ? 24.88384  74.73595  23.32600  1.000 31.56405  ?  409 LEU   B CB  1 
ATOM   8817  C CG  . LEU   F  2 6   ? 23.73014  73.83369  23.76994  1.000 38.43916  ?  409 LEU   B CG  1 
ATOM   8818  C CD1 . LEU   F  2 6   ? 22.50039  74.66034  24.10992  1.000 24.52172  ?  409 LEU   B CD1 1 
ATOM   8819  C CD2 . LEU   F  2 6   ? 23.41626  72.75273  22.71299  1.000 20.07296  ?  409 LEU   B CD2 1 
ATOM   8820  N N   . ARG   F  2 7   ? 27.54596  75.22691  21.43763  1.000 33.78864  ?  410 ARG   B N   1 
ATOM   8821  C CA  . ARG   F  2 7   ? 28.48496  76.25255  20.99047  1.000 32.51590  ?  410 ARG   B CA  1 
ATOM   8822  C C   . ARG   F  2 7   ? 27.91885  77.66406  21.22465  1.000 38.41473  ?  410 ARG   B C   1 
ATOM   8823  O O   . ARG   F  2 7   ? 26.70074  77.86324  21.31430  1.000 49.67737  ?  410 ARG   B O   1 
ATOM   8824  C CB  . ARG   F  2 7   ? 28.80620  76.03384  19.50605  1.000 19.36549  ?  410 ARG   B CB  1 
ATOM   8825  C CG  . ARG   F  2 7   ? 29.40078  74.66204  19.23515  1.000 21.37369  ?  410 ARG   B CG  1 
ATOM   8826  C CD  . ARG   F  2 7   ? 29.60306  74.34719  17.76760  1.000 32.61911  ?  410 ARG   B CD  1 
ATOM   8827  N NE  . ARG   F  2 7   ? 28.34194  74.19297  17.05767  1.000 51.71257  ?  410 ARG   B NE  1 
ATOM   8828  C CZ  . ARG   F  2 7   ? 27.78286  75.13257  16.30510  1.000 42.57279  ?  410 ARG   B CZ  1 
ATOM   8829  N NH1 . ARG   F  2 7   ? 28.38718  76.28633  16.07392  1.000 45.93678  ?  410 ARG   B NH1 1 
ATOM   8830  N NH2 . ARG   F  2 7   ? 26.58041  74.91423  15.78085  1.000 51.80051  ?  410 ARG   B NH2 1 
ATOM   8831  N N   . LYS   F  2 8   ? 28.82137  78.65818  21.33368  1.000 57.27047  ?  411 LYS   B N   1 
ATOM   8832  C CA  . LYS   F  2 8   ? 28.37408  80.05089  21.46419  1.000 75.33113  ?  411 LYS   B CA  1 
ATOM   8833  C C   . LYS   F  2 8   ? 27.59727  80.49001  20.23397  1.000 67.55615  ?  411 LYS   B C   1 
ATOM   8834  O O   . LYS   F  2 8   ? 26.53310  81.11130  20.35106  1.000 64.46777  ?  411 LYS   B O   1 
ATOM   8835  C CB  . LYS   F  2 8   ? 29.55342  81.00089  21.69383  1.000 47.45114  ?  411 LYS   B CB  1 
ATOM   8836  N N   . ASP   F  2 9   ? 28.10434  80.15166  19.04246  1.000 46.22214  ?  412 ASP   B N   1 
ATOM   8837  C CA  . ASP   F  2 9   ? 27.43557  80.43811  17.77536  1.000 97.65061  ?  412 ASP   B CA  1 
ATOM   8838  C C   . ASP   F  2 9   ? 26.11590  79.69332  17.59554  1.000 52.96748  ?  412 ASP   B C   1 
ATOM   8839  O O   . ASP   F  2 9   ? 25.44014  79.88415  16.57531  1.000 83.54467  ?  412 ASP   B O   1 
ATOM   8840  C CB  . ASP   F  2 9   ? 28.37603  80.10032  16.61983  1.000 71.20615  ?  412 ASP   B CB  1 
ATOM   8841  C CG  . ASP   F  2 9   ? 29.50748  81.10015  16.48647  1.000 80.63943  ?  412 ASP   B CG  1 
ATOM   8842  O OD1 . ASP   F  2 9   ? 29.45713  82.15864  17.16069  1.000 83.22913  ?  412 ASP   B OD1 1 
ATOM   8843  O OD2 . ASP   F  2 9   ? 30.44419  80.82986  15.70783  1.000 105.89048 -1 412 ASP   B OD2 1 
ATOM   8844  N N   . CYS   F  2 10  ? 25.74736  78.82866  18.52494  1.000 80.06013  ?  413 CYS   B N   1 
ATOM   8845  C CA  . CYS   F  2 10  ? 24.47869  78.13319  18.43385  1.000 56.98282  ?  413 CYS   B CA  1 
ATOM   8846  C C   . CYS   F  2 10  ? 23.38768  79.06078  18.95371  1.000 67.53068  ?  413 CYS   B C   1 
ATOM   8847  O O   . CYS   F  2 10  ? 23.47182  79.56473  20.08368  1.000 65.53474  ?  413 CYS   B O   1 
ATOM   8848  C CB  . CYS   F  2 10  ? 24.54248  76.82457  19.21807  1.000 48.47026  ?  413 CYS   B CB  1 
ATOM   8849  S SG  . CYS   F  2 10  ? 22.95625  76.02803  19.55183  1.000 60.34619  ?  413 CYS   B SG  1 
ATOM   8850  N N   . ARG   F  2 11  ? 22.38051  79.30251  18.11398  1.000 50.00796  ?  414 ARG   B N   1 
ATOM   8851  C CA  . ARG   F  2 11  ? 21.26859  80.19145  18.42118  1.000 72.37320  ?  414 ARG   B CA  1 
ATOM   8852  C C   . ARG   F  2 11  ? 20.24395  79.56227  19.39392  1.000 83.70325  ?  414 ARG   B C   1 
ATOM   8853  O O   . ARG   F  2 11  ? 19.21310  80.17898  19.68774  1.000 56.24728  ?  414 ARG   B O   1 
ATOM   8854  C CB  . ARG   F  2 11  ? 20.60337  80.62639  17.10676  1.000 44.02336  ?  414 ARG   B CB  1 
ATOM   8855  N N   . ALA   F  2 12  ? 20.50462  78.36455  19.91694  1.000 56.99724  ?  415 ALA   B N   1 
ATOM   8856  C CA  . ALA   F  2 12  ? 19.63138  77.74778  20.90625  1.000 45.89757  ?  415 ALA   B CA  1 
ATOM   8857  C C   . ALA   F  2 12  ? 20.05592  78.16213  22.30681  1.000 39.77638  ?  415 ALA   B C   1 
ATOM   8858  O O   . ALA   F  2 12  ? 21.24670  78.36703  22.57797  1.000 67.42654  ?  415 ALA   B O   1 
ATOM   8859  C CB  . ALA   F  2 12  ? 19.65847  76.22428  20.78838  1.000 25.57591  ?  415 ALA   B CB  1 
ATOM   8860  N N   . GLU   F  2 13  ? 19.07546  78.27164  23.19707  1.000 33.69421  ?  416 GLU   B N   1 
ATOM   8861  C CA  . GLU   F  2 13  ? 19.29807  78.75900  24.55029  1.000 47.37766  ?  416 GLU   B CA  1 
ATOM   8862  C C   . GLU   F  2 13  ? 18.68332  77.77411  25.53872  1.000 49.67774  ?  416 GLU   B C   1 
ATOM   8863  O O   . GLU   F  2 13  ? 17.52177  77.37628  25.39418  1.000 54.84579  ?  416 GLU   B O   1 
ATOM   8864  C CB  . GLU   F  2 13  ? 18.71767  80.17281  24.74267  1.000 36.65604  ?  416 GLU   B CB  1 
ATOM   8865  N N   . ILE   F  2 14  ? 19.48163  77.36708  26.52687  1.000 38.73245  ?  417 ILE   B N   1 
ATOM   8866  C CA  . ILE   F  2 14  ? 18.99858  76.48788  27.57850  1.000 46.45829  ?  417 ILE   B CA  1 
ATOM   8867  C C   . ILE   F  2 14  ? 17.76944  77.09884  28.24987  1.000 36.60015  ?  417 ILE   B C   1 
ATOM   8868  O O   . ILE   F  2 14  ? 17.70390  78.30132  28.52113  1.000 44.93869  ?  417 ILE   B O   1 
ATOM   8869  C CB  . ILE   F  2 14  ? 20.13420  76.22001  28.58408  1.000 26.82067  ?  417 ILE   B CB  1 
ATOM   8870  C CG1 . ILE   F  2 14  ? 21.30026  75.52243  27.88431  1.000 30.19133  ?  417 ILE   B CG1 1 
ATOM   8871  C CG2 . ILE   F  2 14  ? 19.63979  75.39712  29.79088  1.000 33.83776  ?  417 ILE   B CG2 1 
ATOM   8872  C CD1 . ILE   F  2 14  ? 22.51886  75.32273  28.77929  1.000 40.25805  ?  417 ILE   B CD1 1 
ATOM   8873  N N   . VAL   F  2 15  ? 16.78397  76.25322  28.51493  1.000 48.88177  ?  418 VAL   B N   1 
ATOM   8874  C CA  . VAL   F  2 15  ? 15.54751  76.69869  29.13292  1.000 30.58137  ?  418 VAL   B CA  1 
ATOM   8875  C C   . VAL   F  2 15  ? 15.81232  77.07836  30.58519  1.000 34.37655  ?  418 VAL   B C   1 
ATOM   8876  O O   . VAL   F  2 15  ? 16.33657  76.27091  31.36565  1.000 54.48014  ?  418 VAL   B O   1 
ATOM   8877  C CB  . VAL   F  2 15  ? 14.48746  75.59429  28.99744  1.000 53.94508  ?  418 VAL   B CB  1 
ATOM   8878  C CG1 . VAL   F  2 15  ? 13.23159  75.91226  29.80664  1.000 22.25792  ?  418 VAL   B CG1 1 
ATOM   8879  C CG2 . VAL   F  2 15  ? 14.17530  75.37117  27.51263  1.000 20.52608  ?  418 VAL   B CG2 1 
ATOM   8880  N N   . GLU   F  2 16  ? 15.41083  78.30498  30.96025  1.000 41.82667  ?  419 GLU   B N   1 
ATOM   8881  C CA  . GLU   F  2 16  ? 15.87613  78.92015  32.20667  1.000 31.29792  ?  419 GLU   B CA  1 
ATOM   8882  C C   . GLU   F  2 16  ? 15.52177  78.10575  33.44430  1.000 41.73885  ?  419 GLU   B C   1 
ATOM   8883  O O   . GLU   F  2 16  ? 16.28345  78.13454  34.41858  1.000 41.85872  ?  419 GLU   B O   1 
ATOM   8884  C CB  . GLU   F  2 16  ? 15.32558  80.34802  32.37547  1.000 31.99091  ?  419 GLU   B CB  1 
ATOM   8885  N N   . LYS   F  2 17  ? 14.38520  77.39071  33.45560  1.000 35.53538  ?  420 LYS   B N   1 
ATOM   8886  C CA  . LYS   F  2 17  ? 14.02287  76.71569  34.70592  1.000 37.79196  ?  420 LYS   B CA  1 
ATOM   8887  C C   . LYS   F  2 17  ? 15.06012  75.67487  35.10931  1.000 44.31076  ?  420 LYS   B C   1 
ATOM   8888  O O   . LYS   F  2 17  ? 15.16763  75.33798  36.29761  1.000 42.71177  ?  420 LYS   B O   1 
ATOM   8889  C CB  . LYS   F  2 17  ? 12.62055  76.06904  34.63766  1.000 20.26582  ?  420 LYS   B CB  1 
ATOM   8890  C CG  . LYS   F  2 17  ? 12.38198  74.89615  33.64744  1.000 25.26594  ?  420 LYS   B CG  1 
ATOM   8891  C CD  . LYS   F  2 17  ? 11.50874  73.82957  34.34250  1.000 46.40259  ?  420 LYS   B CD  1 
ATOM   8892  C CE  . LYS   F  2 17  ? 10.69138  72.96792  33.38625  1.000 56.19887  ?  420 LYS   B CE  1 
ATOM   8893  N NZ  . LYS   F  2 17  ? 9.86860   73.82171  32.49061  1.000 79.09397  ?  420 LYS   B NZ  1 
ATOM   8894  N N   . PHE   F  2 18  ? 15.84353  75.17425  34.15020  1.000 35.51532  ?  421 PHE   B N   1 
ATOM   8895  C CA  . PHE   F  2 18  ? 16.85171  74.16843  34.45087  1.000 59.19322  ?  421 PHE   B CA  1 
ATOM   8896  C C   . PHE   F  2 18  ? 18.13802  74.75718  35.00963  1.000 46.40056  ?  421 PHE   B C   1 
ATOM   8897  O O   . PHE   F  2 18  ? 18.99518  73.99783  35.46894  1.000 41.11424  ?  421 PHE   B O   1 
ATOM   8898  C CB  . PHE   F  2 18  ? 17.14151  73.34646  33.20478  1.000 24.34136  ?  421 PHE   B CB  1 
ATOM   8899  C CG  . PHE   F  2 18  ? 15.93314  72.64314  32.68450  1.000 35.57141  ?  421 PHE   B CG  1 
ATOM   8900  C CD1 . PHE   F  2 18  ? 15.23181  71.76143  33.50622  1.000 35.01071  ?  421 PHE   B CD1 1 
ATOM   8901  C CD2 . PHE   F  2 18  ? 15.46542  72.87664  31.39745  1.000 52.39674  ?  421 PHE   B CD2 1 
ATOM   8902  C CE1 . PHE   F  2 18  ? 14.10243  71.11681  33.04595  1.000 27.32528  ?  421 PHE   B CE1 1 
ATOM   8903  C CE2 . PHE   F  2 18  ? 14.32804  72.23327  30.92715  1.000 42.78250  ?  421 PHE   B CE2 1 
ATOM   8904  C CZ  . PHE   F  2 18  ? 13.64529  71.35845  31.75419  1.000 48.45441  ?  421 PHE   B CZ  1 
ATOM   8905  N N   . THR   F  2 19  ? 18.29335  76.08095  35.02482  1.000 34.82053  ?  422 THR   B N   1 
ATOM   8906  C CA  . THR   F  2 19  ? 19.43669  76.61786  35.74736  1.000 25.04237  ?  422 THR   B CA  1 
ATOM   8907  C C   . THR   F  2 19  ? 19.27017  76.52078  37.26337  1.000 33.09012  ?  422 THR   B C   1 
ATOM   8908  O O   . THR   F  2 19  ? 20.24302  76.77002  37.98428  1.000 31.22554  ?  422 THR   B O   1 
ATOM   8909  C CB  . THR   F  2 19  ? 19.68860  78.06824  35.34088  1.000 36.66697  ?  422 THR   B CB  1 
ATOM   8910  O OG1 . THR   F  2 19  ? 18.70392  78.90543  35.94308  1.000 32.87056  ?  422 THR   B OG1 1 
ATOM   8911  C CG2 . THR   F  2 19  ? 19.60126  78.22964  33.83115  1.000 38.58840  ?  422 THR   B CG2 1 
ATOM   8912  N N   . GLU   F  2 20  ? 18.07895  76.15169  37.76946  1.000 41.84833  ?  423 GLU   B N   1 
ATOM   8913  C CA  . GLU   F  2 20  ? 17.91663  75.91499  39.20359  1.000 40.13830  ?  423 GLU   B CA  1 
ATOM   8914  C C   . GLU   F  2 20  ? 18.21858  74.45087  39.50871  1.000 30.58797  ?  423 GLU   B C   1 
ATOM   8915  O O   . GLU   F  2 20  ? 17.49784  73.56105  39.02651  1.000 46.36060  ?  423 GLU   B O   1 
ATOM   8916  C CB  . GLU   F  2 20  ? 16.51277  76.27990  39.68217  1.000 26.41240  ?  423 GLU   B CB  1 
ATOM   8917  N N   . PRO   F  2 21  ? 19.28047  74.15918  40.24858  1.000 37.19980  ?  424 PRO   B N   1 
ATOM   8918  C CA  . PRO   F  2 21  ? 19.56886  72.77012  40.62186  1.000 50.63980  ?  424 PRO   B CA  1 
ATOM   8919  C C   . PRO   F  2 21  ? 18.35358  72.12446  41.26509  1.000 36.25438  ?  424 PRO   B C   1 
ATOM   8920  O O   . PRO   F  2 21  ? 17.58892  72.77591  41.97663  1.000 44.95187  ?  424 PRO   B O   1 
ATOM   8921  C CB  . PRO   F  2 21  ? 20.71895  72.90177  41.62777  1.000 19.14593  ?  424 PRO   B CB  1 
ATOM   8922  C CG  . PRO   F  2 21  ? 21.37231  74.20259  41.29397  1.000 34.26457  ?  424 PRO   B CG  1 
ATOM   8923  C CD  . PRO   F  2 21  ? 20.30461  75.10570  40.70707  1.000 32.95554  ?  424 PRO   B CD  1 
ATOM   8924  N N   . GLY   F  2 22  ? 18.18108  70.82812  41.00536  1.000 43.73792  ?  425 GLY   B N   1 
ATOM   8925  C CA  . GLY   F  2 22  ? 17.10144  70.06111  41.58257  1.000 26.41506  ?  425 GLY   B CA  1 
ATOM   8926  C C   . GLY   F  2 22  ? 15.83842  69.99283  40.74325  1.000 35.05471  ?  425 GLY   B C   1 
ATOM   8927  O O   . GLY   F  2 22  ? 14.95883  69.18297  41.04889  1.000 40.93317  ?  425 GLY   B O   1 
ATOM   8928  N N   . THR   F  2 23  ? 15.72152  70.80997  39.69928  1.000 28.76068  ?  426 THR   B N   1 
ATOM   8929  C CA  . THR   F  2 23  ? 14.54930  70.77027  38.83225  1.000 26.42976  ?  426 THR   B CA  1 
ATOM   8930  C C   . THR   F  2 23  ? 14.44027  69.42511  38.10918  1.000 26.40291  ?  426 THR   B C   1 
ATOM   8931  O O   . THR   F  2 23  ? 15.42952  68.88068  37.61292  1.000 55.67363  ?  426 THR   B O   1 
ATOM   8932  C CB  . THR   F  2 23  ? 14.62718  71.92023  37.81885  1.000 35.10164  ?  426 THR   B CB  1 
ATOM   8933  O OG1 . THR   F  2 23  ? 14.67780  73.17575  38.51179  1.000 43.40062  ?  426 THR   B OG1 1 
ATOM   8934  C CG2 . THR   F  2 23  ? 13.44788  71.90577  36.84493  1.000 25.54119  ?  426 THR   B CG2 1 
ATOM   8935  N N   . VAL   F  2 24  ? 13.22230  68.89310  38.04189  1.000 49.39442  ?  427 VAL   B N   1 
ATOM   8936  C CA  . VAL   F  2 24  ? 13.00159  67.61029  37.38889  1.000 30.55886  ?  427 VAL   B CA  1 
ATOM   8937  C C   . VAL   F  2 24  ? 13.16378  67.75553  35.87981  1.000 25.01433  ?  427 VAL   B C   1 
ATOM   8938  O O   . VAL   F  2 24  ? 12.60009  68.66676  35.25575  1.000 49.86893  ?  427 VAL   B O   1 
ATOM   8939  C CB  . VAL   F  2 24  ? 11.61776  67.06170  37.76489  1.000 23.42715  ?  427 VAL   B CB  1 
ATOM   8940  C CG1 . VAL   F  2 24  ? 11.21782  65.92603  36.84321  1.000 16.16656  ?  427 VAL   B CG1 1 
ATOM   8941  C CG2 . VAL   F  2 24  ? 11.64840  66.58751  39.19989  1.000 23.37362  ?  427 VAL   B CG2 1 
ATOM   8942  N N   . ILE   F  2 25  ? 13.94224  66.85185  35.28731  1.000 52.93622  ?  428 ILE   B N   1 
ATOM   8943  C CA  . ILE   F  2 25  ? 14.17583  66.80420  33.84485  1.000 21.83292  ?  428 ILE   B CA  1 
ATOM   8944  C C   . ILE   F  2 25  ? 13.51839  65.52594  33.33179  1.000 43.24493  ?  428 ILE   B C   1 
ATOM   8945  O O   . ILE   F  2 25  ? 14.02290  64.41549  33.54833  1.000 34.54543  ?  428 ILE   B O   1 
ATOM   8946  C CB  . ILE   F  2 25  ? 15.67246  66.84441  33.48752  1.000 40.23931  ?  428 ILE   B CB  1 
ATOM   8947  C CG1 . ILE   F  2 25  ? 16.33336  68.15595  33.94038  1.000 31.10795  ?  428 ILE   B CG1 1 
ATOM   8948  C CG2 . ILE   F  2 25  ? 15.84802  66.65546  31.99714  1.000 19.07181  ?  428 ILE   B CG2 1 
ATOM   8949  C CD1 . ILE   F  2 25  ? 17.77859  68.33523  33.45884  1.000 25.73681  ?  428 ILE   B CD1 1 
ATOM   8950  N N   . ARG   F  2 26  ? 12.37918  65.67175  32.66477  1.000 30.27296  ?  429 ARG   B N   1 
ATOM   8951  C CA  . ARG   F  2 26  ? 11.70684  64.53201  32.05712  1.000 29.08532  ?  429 ARG   B CA  1 
ATOM   8952  C C   . ARG   F  2 26  ? 12.37171  64.24666  30.72463  1.000 29.61551  ?  429 ARG   B C   1 
ATOM   8953  O O   . ARG   F  2 26  ? 12.45085  65.13505  29.86810  1.000 28.65516  ?  429 ARG   B O   1 
ATOM   8954  C CB  . ARG   F  2 26  ? 10.21615  64.81173  31.87377  1.000 37.10018  ?  429 ARG   B CB  1 
ATOM   8955  C CG  . ARG   F  2 26  ? 9.49936   64.98819  33.18344  1.000 30.87823  ?  429 ARG   B CG  1 
ATOM   8956  C CD  . ARG   F  2 26  ? 8.07217   65.43756  33.00432  1.000 44.50073  ?  429 ARG   B CD  1 
ATOM   8957  N NE  . ARG   F  2 26  ? 7.24020   64.85146  34.04864  1.000 30.28331  ?  429 ARG   B NE  1 
ATOM   8958  C CZ  . ARG   F  2 26  ? 7.18476   65.30313  35.29603  1.000 162.78713 ?  429 ARG   B CZ  1 
ATOM   8959  N NH1 . ARG   F  2 26  ? 7.84004   66.39684  35.67196  1.000 25.92100  ?  429 ARG   B NH1 1 
ATOM   8960  N NH2 . ARG   F  2 26  ? 6.46063   64.63938  36.19276  1.000 32.74761  ?  429 ARG   B NH2 1 
ATOM   8961  N N   . ILE   F  2 27  ? 12.85362  63.01445  30.54873  1.000 17.14114  ?  430 ILE   B N   1 
ATOM   8962  C CA  . ILE   F  2 27  ? 13.53280  62.67587  29.30744  1.000 34.53463  ?  430 ILE   B CA  1 
ATOM   8963  C C   . ILE   F  2 27  ? 12.62129  63.00256  28.12020  1.000 22.16602  ?  430 ILE   B C   1 
ATOM   8964  O O   . ILE   F  2 27  ? 11.39151  62.90640  28.20648  1.000 48.96800  ?  430 ILE   B O   1 
ATOM   8965  C CB  . ILE   F  2 27  ? 13.97651  61.20058  29.33331  1.000 28.03867  ?  430 ILE   B CB  1 
ATOM   8966  C CG1 . ILE   F  2 27  ? 15.03404  60.93926  28.24343  1.000 22.52303  ?  430 ILE   B CG1 1 
ATOM   8967  C CG2 . ILE   F  2 27  ? 12.75277  60.25541  29.25949  1.000 26.15323  ?  430 ILE   B CG2 1 
ATOM   8968  C CD1 . ILE   F  2 27  ? 15.66462  59.55243  28.34448  1.000 19.70652  ?  430 ILE   B CD1 1 
ATOM   8969  N N   . ASN   F  2 28  ? 13.24351  63.43653  27.02110  1.000 41.56836  ?  431 ASN   B N   1 
ATOM   8970  C CA  . ASN   F  2 28  ? 12.59723  63.89499  25.79226  1.000 21.02043  ?  431 ASN   B CA  1 
ATOM   8971  C C   . ASN   F  2 28  ? 11.93854  65.26320  25.93463  1.000 32.58848  ?  431 ASN   B C   1 
ATOM   8972  O O   . ASN   F  2 28  ? 11.48254  65.80978  24.92668  1.000 23.13345  ?  431 ASN   B O   1 
ATOM   8973  C CB  . ASN   F  2 28  ? 11.53691  62.90374  25.28091  1.000 16.69018  ?  431 ASN   B CB  1 
ATOM   8974  C CG  . ASN   F  2 28  ? 12.11573  61.54687  24.93020  1.000 28.59929  ?  431 ASN   B CG  1 
ATOM   8975  O OD1 . ASN   F  2 28  ? 13.30681  61.41064  24.64784  1.000 33.54995  ?  431 ASN   B OD1 1 
ATOM   8976  N ND2 . ASN   F  2 28  ? 11.26617  60.52693  24.95469  1.000 20.74715  ?  431 ASN   B ND2 1 
ATOM   8977  N N   . GLU   F  2 29  ? 11.84463  65.82995  27.13992  1.000 26.69561  ?  432 GLU   B N   1 
ATOM   8978  C CA  . GLU   F  2 29  ? 11.25772  67.16423  27.21413  1.000 35.34117  ?  432 GLU   B CA  1 
ATOM   8979  C C   . GLU   F  2 29  ? 12.28090  68.21183  26.74047  1.000 31.11850  ?  432 GLU   B C   1 
ATOM   8980  O O   . GLU   F  2 29  ? 13.47041  67.92441  26.56790  1.000 46.58107  ?  432 GLU   B O   1 
ATOM   8981  C CB  . GLU   F  2 29  ? 10.73425  67.44160  28.63107  1.000 19.51762  ?  432 GLU   B CB  1 
ATOM   8982  C CG  . GLU   F  2 29  ? 11.65351  68.21486  29.56002  1.000 32.79896  ?  432 GLU   B CG  1 
ATOM   8983  C CD  . GLU   F  2 29  ? 10.96549  68.65904  30.86009  1.000 57.17769  ?  432 GLU   B CD  1 
ATOM   8984  O OE1 . GLU   F  2 29  ? 10.98301  67.89084  31.84832  1.000 42.19181  ?  432 GLU   B OE1 1 
ATOM   8985  O OE2 . GLU   F  2 29  ? 10.42035  69.79105  30.90218  1.000 48.44459  -1 432 GLU   B OE2 1 
ATOM   8986  N N   . VAL   F  2 30  ? 11.80082  69.42254  26.46820  1.000 43.92719  ?  433 VAL   B N   1 
ATOM   8987  C CA  . VAL   F  2 30  ? 12.63772  70.45926  25.85876  1.000 19.24416  ?  433 VAL   B CA  1 
ATOM   8988  C C   . VAL   F  2 30  ? 13.55580  71.06326  26.91677  1.000 39.34636  ?  433 VAL   B C   1 
ATOM   8989  O O   . VAL   F  2 30  ? 13.07844  71.61959  27.91342  1.000 30.18286  ?  433 VAL   B O   1 
ATOM   8990  C CB  . VAL   F  2 30  ? 11.77007  71.55025  25.20776  1.000 40.19603  ?  433 VAL   B CB  1 
ATOM   8991  C CG1 . VAL   F  2 30  ? 12.63448  72.65178  24.58154  1.000 30.02362  ?  433 VAL   B CG1 1 
ATOM   8992  C CG2 . VAL   F  2 30  ? 10.80605  70.95149  24.17469  1.000 24.79927  ?  433 VAL   B CG2 1 
ATOM   8993  N N   . VAL   F  2 31  ? 14.87456  70.97620  26.69637  1.000 32.56293  ?  434 VAL   B N   1 
ATOM   8994  C CA  . VAL   F  2 31  ? 15.83606  71.63631  27.57836  1.000 43.64440  ?  434 VAL   B CA  1 
ATOM   8995  C C   . VAL   F  2 31  ? 16.53229  72.82085  26.91116  1.000 31.24118  ?  434 VAL   B C   1 
ATOM   8996  O O   . VAL   F  2 31  ? 17.10333  73.66413  27.62343  1.000 30.42284  ?  434 VAL   B O   1 
ATOM   8997  C CB  . VAL   F  2 31  ? 16.88561  70.65373  28.15516  1.000 33.96450  ?  434 VAL   B CB  1 
ATOM   8998  C CG1 . VAL   F  2 31  ? 16.23388  69.64232  29.08878  1.000 17.72889  ?  434 VAL   B CG1 1 
ATOM   8999  C CG2 . VAL   F  2 31  ? 17.67554  69.92976  27.03650  1.000 20.30782  ?  434 VAL   B CG2 1 
ATOM   9000  N N   . ALA   F  2 32  ? 16.49698  72.92620  25.58722  1.000 30.94756  ?  435 ALA   B N   1 
ATOM   9001  C CA  . ALA   F  2 32  ? 16.99985  74.11303  24.90763  1.000 34.22520  ?  435 ALA   B CA  1 
ATOM   9002  C C   . ALA   F  2 32  ? 16.21219  74.29399  23.61716  1.000 44.16759  ?  435 ALA   B C   1 
ATOM   9003  O O   . ALA   F  2 32  ? 15.75452  73.31615  23.01053  1.000 36.23745  ?  435 ALA   B O   1 
ATOM   9004  C CB  . ALA   F  2 32  ? 18.50256  74.02151  24.60627  1.000 27.92283  ?  435 ALA   B CB  1 
ATOM   9005  N N   . ALA   F  2 33  ? 16.06729  75.55291  23.19932  1.000 30.64793  ?  436 ALA   B N   1 
ATOM   9006  C CA  . ALA   F  2 33  ? 15.27075  75.89947  22.02883  1.000 39.64633  ?  436 ALA   B CA  1 
ATOM   9007  C C   . ALA   F  2 33  ? 15.84527  77.14151  21.36621  1.000 59.26851  ?  436 ALA   B C   1 
ATOM   9008  O O   . ALA   F  2 33  ? 16.45446  77.98858  22.02715  1.000 36.66476  ?  436 ALA   B O   1 
ATOM   9009  C CB  . ALA   F  2 33  ? 13.80991  76.15705  22.39277  1.000 23.74906  ?  436 ALA   B CB  1 
ATOM   9010  N N   . LEU   F  2 34  ? 15.62323  77.24784  20.05711  1.000 34.30221  ?  437 LEU   B N   1 
ATOM   9011  C CA  . LEU   F  2 34  ? 16.07181  78.39281  19.26368  1.000 64.02666  ?  437 LEU   B CA  1 
ATOM   9012  C C   . LEU   F  2 34  ? 15.38319  79.70689  19.64843  1.000 31.89684  ?  437 LEU   B C   1 
ATOM   9013  O O   . LEU   F  2 34  ? 14.16080  79.78394  19.71653  1.000 38.63459  ?  437 LEU   B O   1 
ATOM   9014  C CB  . LEU   F  2 34  ? 15.84646  78.11232  17.77271  1.000 30.71839  ?  437 LEU   B CB  1 
ATOM   9015  C CG  . LEU   F  2 34  ? 16.82020  77.13856  17.09138  1.000 55.84138  ?  437 LEU   B CG  1 
ATOM   9016  C CD1 . LEU   F  2 34  ? 16.43462  76.84993  15.61597  1.000 36.99611  ?  437 LEU   B CD1 1 
ATOM   9017  C CD2 . LEU   F  2 34  ? 18.27204  77.63349  17.22279  1.000 58.59567  ?  437 LEU   B CD2 1 
ATOM   9018  N N   . LEU   G  1 57  ? 63.96826  59.52098  -20.59500 1.000 36.48061  ?  57  LEU   C N   1 
ATOM   9019  C CA  . LEU   G  1 57  ? 63.70562  58.58334  -19.50839 1.000 33.37794  ?  57  LEU   C CA  1 
ATOM   9020  C C   . LEU   G  1 57  ? 63.82224  59.28441  -18.17338 1.000 49.52005  ?  57  LEU   C C   1 
ATOM   9021  O O   . LEU   G  1 57  ? 64.75550  60.05792  -17.96612 1.000 51.51392  ?  57  LEU   C O   1 
ATOM   9022  C CB  . LEU   G  1 57  ? 64.70106  57.42088  -19.51500 1.000 30.02316  ?  57  LEU   C CB  1 
ATOM   9023  C CG  . LEU   G  1 57  ? 64.77509  56.38858  -20.63823 1.000 46.28685  ?  57  LEU   C CG  1 
ATOM   9024  C CD1 . LEU   G  1 57  ? 65.95646  55.45550  -20.37522 1.000 38.67290  ?  57  LEU   C CD1 1 
ATOM   9025  C CD2 . LEU   G  1 57  ? 63.47903  55.60094  -20.79680 1.000 44.75170  ?  57  LEU   C CD2 1 
ATOM   9026  N N   . MET   G  1 58  ? 62.91472  58.97839  -17.24812 1.000 52.17319  ?  58  MET   C N   1 
ATOM   9027  C CA  . MET   G  1 58  ? 63.00620  59.57346  -15.92135 1.000 51.07190  ?  58  MET   C CA  1 
ATOM   9028  C C   . MET   G  1 58  ? 64.25699  59.08331  -15.20288 1.000 41.78028  ?  58  MET   C C   1 
ATOM   9029  O O   . MET   G  1 58  ? 64.70080  57.94838  -15.38910 1.000 62.44587  ?  58  MET   C O   1 
ATOM   9030  C CB  . MET   G  1 58  ? 61.76287  59.25077  -15.10171 1.000 44.01440  ?  58  MET   C CB  1 
ATOM   9031  C CG  . MET   G  1 58  ? 61.39078  57.78407  -15.04057 1.000 59.31612  ?  58  MET   C CG  1 
ATOM   9032  S SD  . MET   G  1 58  ? 59.92532  57.54701  -14.01356 1.000 65.18116  ?  58  MET   C SD  1 
ATOM   9033  C CE  . MET   G  1 58  ? 58.63014  58.03118  -15.16634 1.000 41.80794  ?  58  MET   C CE  1 
ATOM   9034  N N   . GLN   G  1 59  ? 64.82872  59.95529  -14.37402 1.000 45.57654  ?  59  GLN   C N   1 
ATOM   9035  C CA  . GLN   G  1 59  ? 66.12416  59.68250  -13.75005 1.000 34.41479  ?  59  GLN   C CA  1 
ATOM   9036  C C   . GLN   G  1 59  ? 66.22192  58.31524  -13.07740 1.000 44.14433  ?  59  GLN   C C   1 
ATOM   9037  O O   . GLN   G  1 59  ? 67.24403  57.63878  -13.27227 1.000 38.19484  ?  59  GLN   C O   1 
ATOM   9038  C CB  . GLN   G  1 59  ? 66.46050  60.77887  -12.72855 1.000 28.16473  ?  59  GLN   C CB  1 
ATOM   9039  C CG  . GLN   G  1 59  ? 67.91826  60.77851  -12.34184 1.000 57.71660  ?  59  GLN   C CG  1 
ATOM   9040  C CD  . GLN   G  1 59  ? 68.79476  61.04628  -13.55331 1.000 80.30852  ?  59  GLN   C CD  1 
ATOM   9041  O OE1 . GLN   G  1 59  ? 68.40145  61.78184  -14.46388 1.000 91.89216  ?  59  GLN   C OE1 1 
ATOM   9042  N NE2 . GLN   G  1 59  ? 69.97826  60.43452  -13.58656 1.000 64.93518  ?  59  GLN   C NE2 1 
ATOM   9043  N N   . PRO   G  1 60  ? 65.23935  57.84975  -12.28797 1.000 52.39674  ?  60  PRO   C N   1 
ATOM   9044  C CA  . PRO   G  1 60  ? 65.38488  56.50848  -11.68506 1.000 34.11655  ?  60  PRO   C CA  1 
ATOM   9045  C C   . PRO   G  1 60  ? 65.59750  55.40899  -12.71358 1.000 58.20467  ?  60  PRO   C C   1 
ATOM   9046  O O   . PRO   G  1 60  ? 66.38665  54.48570  -12.45936 1.000 37.30806  ?  60  PRO   C O   1 
ATOM   9047  C CB  . PRO   G  1 60  ? 64.07393  56.33178  -10.90552 1.000 34.88013  ?  60  PRO   C CB  1 
ATOM   9048  C CG  . PRO   G  1 60  ? 63.59514  57.72259  -10.63657 1.000 41.86869  ?  60  PRO   C CG  1 
ATOM   9049  C CD  . PRO   G  1 60  ? 63.98657  58.50147  -11.86432 1.000 30.14798  ?  60  PRO   C CD  1 
ATOM   9050  N N   . ILE   G  1 61  ? 64.93073  55.49074  -13.87363 1.000 29.44433  ?  61  ILE   C N   1 
ATOM   9051  C CA  . ILE   G  1 61  ? 65.17426  54.51845  -14.94045 1.000 53.77794  ?  61  ILE   C CA  1 
ATOM   9052  C C   . ILE   G  1 61  ? 66.56073  54.70088  -15.54156 1.000 40.09712  ?  61  ILE   C C   1 
ATOM   9053  O O   . ILE   G  1 61  ? 67.20999  53.72259  -15.93113 1.000 44.43110  ?  61  ILE   C O   1 
ATOM   9054  C CB  . ILE   G  1 61  ? 64.08266  54.60529  -16.02137 1.000 39.66856  ?  61  ILE   C CB  1 
ATOM   9055  C CG1 . ILE   G  1 61  ? 62.71548  54.34194  -15.39378 1.000 30.22042  ?  61  ILE   C CG1 1 
ATOM   9056  C CG2 . ILE   G  1 61  ? 64.34105  53.59534  -17.15370 1.000 28.35764  ?  61  ILE   C CG2 1 
ATOM   9057  C CD1 . ILE   G  1 61  ? 61.60450  54.35669  -16.38761 1.000 36.80920  ?  61  ILE   C CD1 1 
ATOM   9058  N N   . GLN   G  1 62  ? 67.02240  55.94424  -15.63156 1.000 80.13096  ?  62  GLN   C N   1 
ATOM   9059  C CA  . GLN   G  1 62  ? 68.37285  56.18742  -16.11590 1.000 12.25178  ?  62  GLN   C CA  1 
ATOM   9060  C C   . GLN   G  1 62  ? 69.41710  55.52858  -15.21889 1.000 73.74898  ?  62  GLN   C C   1 
ATOM   9061  O O   . GLN   G  1 62  ? 70.34095  54.85678  -15.71400 1.000 47.01709  ?  62  GLN   C O   1 
ATOM   9062  C CB  . GLN   G  1 62  ? 68.62508  57.68109  -16.20486 1.000 54.88878  ?  62  GLN   C CB  1 
ATOM   9063  C CG  . GLN   G  1 62  ? 67.71928  58.37792  -17.14820 1.000 72.92612  ?  62  GLN   C CG  1 
ATOM   9064  C CD  . GLN   G  1 62  ? 68.50409  59.28901  -17.99729 1.000 86.40898  ?  62  GLN   C CD  1 
ATOM   9065  O OE1 . GLN   G  1 62  ? 68.48212  60.49911  -17.78619 1.000 117.06914 ?  62  GLN   C OE1 1 
ATOM   9066  N NE2 . GLN   G  1 62  ? 69.25260  58.72420  -18.95104 1.000 123.55104 ?  62  GLN   C NE2 1 
ATOM   9067  N N   . GLU   G  1 63  ? 69.28483  55.72881  -13.88597 1.000 29.44769  ?  63  GLU   C N   1 
ATOM   9068  C CA  . GLU   G  1 63  ? 70.20039  55.10584  -12.93283 1.000 45.28446  ?  63  GLU   C CA  1 
ATOM   9069  C C   . GLU   G  1 63  ? 70.08518  53.58763  -12.97353 1.000 47.50387  ?  63  GLU   C C   1 
ATOM   9070  O O   . GLU   G  1 63  ? 71.09065  52.87866  -12.83838 1.000 40.82430  ?  63  GLU   C O   1 
ATOM   9071  C CB  . GLU   G  1 63  ? 69.93203  55.63021  -11.53174 1.000 29.40405  ?  63  GLU   C CB  1 
ATOM   9072  C CG  . GLU   G  1 63  ? 70.70411  56.89579  -11.20171 1.000 66.97894  ?  63  GLU   C CG  1 
ATOM   9073  C CD  . GLU   G  1 63  ? 69.86863  57.92255  -10.47208 1.000 53.77124  ?  63  GLU   C CD  1 
ATOM   9074  O OE1 . GLU   G  1 63  ? 68.75760  57.57535  -10.01067 1.000 100.23072 ?  63  GLU   C OE1 1 
ATOM   9075  O OE2 . GLU   G  1 63  ? 70.32298  59.08346  -10.35850 1.000 127.82425 -1 63  GLU   C OE2 1 
ATOM   9076  N N   . PHE   G  1 64  ? 68.86094  53.07808  -13.16939 1.000 39.09744  ?  64  PHE   C N   1 
ATOM   9077  C CA  . PHE   G  1 64  ? 68.63642  51.64624  -13.35049 1.000 32.54608  ?  64  PHE   C CA  1 
ATOM   9078  C C   . PHE   G  1 64  ? 69.43014  51.11650  -14.53824 1.000 46.58281  ?  64  PHE   C C   1 
ATOM   9079  O O   . PHE   G  1 64  ? 70.20072  50.15628  -14.40879 1.000 41.14192  ?  64  PHE   C O   1 
ATOM   9080  C CB  . PHE   G  1 64  ? 67.13526  51.39706  -13.52739 1.000 35.64007  ?  64  PHE   C CB  1 
ATOM   9081  C CG  . PHE   G  1 64  ? 66.76739  49.97644  -13.86900 1.000 40.81281  ?  64  PHE   C CG  1 
ATOM   9082  C CD1 . PHE   G  1 64  ? 66.85603  48.97164  -12.92198 1.000 48.75789  ?  64  PHE   C CD1 1 
ATOM   9083  C CD2 . PHE   G  1 64  ? 66.28267  49.65630  -15.13300 1.000 29.84754  ?  64  PHE   C CD2 1 
ATOM   9084  C CE1 . PHE   G  1 64  ? 66.49198  47.66434  -13.24152 1.000 34.74980  ?  64  PHE   C CE1 1 
ATOM   9085  C CE2 . PHE   G  1 64  ? 65.90421  48.35651  -15.45801 1.000 28.09810  ?  64  PHE   C CE2 1 
ATOM   9086  C CZ  . PHE   G  1 64  ? 66.00787  47.35959  -14.51443 1.000 36.83556  ?  64  PHE   C CZ  1 
ATOM   9087  N N   . LYS   G  1 65  ? 69.25660  51.74786  -15.70869 1.000 38.41185  ?  65  LYS   C N   1 
ATOM   9088  C CA  . LYS   G  1 65  ? 70.01942  51.37508  -16.90393 1.000 33.34849  ?  65  LYS   C CA  1 
ATOM   9089  C C   . LYS   G  1 65  ? 71.52500  51.51172  -16.67880 1.000 53.53481  ?  65  LYS   C C   1 
ATOM   9090  O O   . LYS   G  1 65  ? 72.31121  50.65804  -17.11006 1.000 45.09050  ?  65  LYS   C O   1 
ATOM   9091  C CB  . LYS   G  1 65  ? 69.57601  52.23192  -18.09136 1.000 40.60569  ?  65  LYS   C CB  1 
ATOM   9092  C CG  . LYS   G  1 65  ? 70.24347  51.90247  -19.41790 1.000 41.64073  ?  65  LYS   C CG  1 
ATOM   9093  C CD  . LYS   G  1 65  ? 69.32404  52.29170  -20.56171 1.000 52.17493  ?  65  LYS   C CD  1 
ATOM   9094  C CE  . LYS   G  1 65  ? 69.86604  53.44563  -21.36158 1.000 59.92813  ?  65  LYS   C CE  1 
ATOM   9095  N NZ  . LYS   G  1 65  ? 69.96638  53.03720  -22.78378 1.000 70.99289  ?  65  LYS   C NZ  1 
ATOM   9096  N N   . ALA   G  1 66  ? 71.94855  52.58730  -16.01124 1.000 42.76524  ?  66  ALA   C N   1 
ATOM   9097  C CA  . ALA   G  1 66  ? 73.37387  52.76770  -15.75852 1.000 45.99923  ?  66  ALA   C CA  1 
ATOM   9098  C C   . ALA   G  1 66  ? 73.91656  51.65171  -14.87041 1.000 56.31357  ?  66  ALA   C C   1 
ATOM   9099  O O   . ALA   G  1 66  ? 75.07523  51.22841  -15.01258 1.000 40.73727  ?  66  ALA   C O   1 
ATOM   9100  C CB  . ALA   G  1 66  ? 73.61824  54.13584  -15.12744 1.000 23.29254  ?  66  ALA   C CB  1 
ATOM   9101  N N   . PHE   G  1 67  ? 73.08661  51.15269  -13.95385 1.000 55.91921  ?  67  PHE   C N   1 
ATOM   9102  C CA  . PHE   G  1 67  ? 73.53391  50.07402  -13.08767 1.000 34.36851  ?  67  PHE   C CA  1 
ATOM   9103  C C   . PHE   G  1 67  ? 73.72036  48.78763  -13.88447 1.000 50.35371  ?  67  PHE   C C   1 
ATOM   9104  O O   . PHE   G  1 67  ? 74.74834  48.11025  -13.75550 1.000 46.62446  ?  67  PHE   C O   1 
ATOM   9105  C CB  . PHE   G  1 67  ? 72.54986  49.86911  -11.93073 1.000 35.58495  ?  67  PHE   C CB  1 
ATOM   9106  C CG  . PHE   G  1 67  ? 72.83667  48.64065  -11.14633 1.000 36.55981  ?  67  PHE   C CG  1 
ATOM   9107  C CD1 . PHE   G  1 67  ? 73.88105  48.63744  -10.23509 1.000 22.94483  ?  67  PHE   C CD1 1 
ATOM   9108  C CD2 . PHE   G  1 67  ? 72.12005  47.45650  -11.37541 1.000 30.52017  ?  67  PHE   C CD2 1 
ATOM   9109  C CE1 . PHE   G  1 67  ? 74.20310  47.48598  -9.52322  1.000 30.08310  ?  67  PHE   C CE1 1 
ATOM   9110  C CE2 . PHE   G  1 67  ? 72.43444  46.29049  -10.68576 1.000 40.40809  ?  67  PHE   C CE2 1 
ATOM   9111  C CZ  . PHE   G  1 67  ? 73.47325  46.30020  -9.75063  1.000 27.46301  ?  67  PHE   C CZ  1 
ATOM   9112  N N   . ILE   G  1 68  ? 72.73026  48.43915  -14.71342 1.000 35.76392  ?  68  ILE   C N   1 
ATOM   9113  C CA  . ILE   G  1 68  ? 72.82335  47.25638  -15.57043 1.000 37.94619  ?  68  ILE   C CA  1 
ATOM   9114  C C   . ILE   G  1 68  ? 74.12619  47.26802  -16.35663 1.000 44.03345  ?  68  ILE   C C   1 
ATOM   9115  O O   . ILE   G  1 68  ? 74.80303  46.24195  -16.50004 1.000 41.66544  ?  68  ILE   C O   1 
ATOM   9116  C CB  . ILE   G  1 68  ? 71.60353  47.19814  -16.51155 1.000 27.86345  ?  68  ILE   C CB  1 
ATOM   9117  C CG1 . ILE   G  1 68  ? 70.31523  46.97674  -15.70400 1.000 34.96214  ?  68  ILE   C CG1 1 
ATOM   9118  C CG2 . ILE   G  1 68  ? 71.78516  46.13102  -17.57320 1.000 33.25434  ?  68  ILE   C CG2 1 
ATOM   9119  C CD1 . ILE   G  1 68  ? 69.06322  47.05426  -16.52000 1.000 27.94050  ?  68  ILE   C CD1 1 
ATOM   9120  N N   . GLU   G  1 69  ? 74.49958  48.43781  -16.86803 1.000 75.52641  ?  69  GLU   C N   1 
ATOM   9121  C CA  . GLU   G  1 69  ? 75.68792  48.60137  -17.68826 1.000 50.08938  ?  69  GLU   C CA  1 
ATOM   9122  C C   . GLU   G  1 69  ? 76.96539  48.69922  -16.86482 1.000 59.43994  ?  69  GLU   C C   1 
ATOM   9123  O O   . GLU   G  1 69  ? 78.04910  48.49259  -17.41351 1.000 59.94729  ?  69  GLU   C O   1 
ATOM   9124  C CB  . GLU   G  1 69  ? 75.52258  49.84897  -18.55772 1.000 56.42944  ?  69  GLU   C CB  1 
ATOM   9125  C CG  . GLU   G  1 69  ? 74.56407  49.64247  -19.73026 1.000 42.43677  ?  69  GLU   C CG  1 
ATOM   9126  C CD  . GLU   G  1 69  ? 74.02492  50.94669  -20.32177 1.000 83.64730  ?  69  GLU   C CD  1 
ATOM   9127  O OE1 . GLU   G  1 69  ? 74.32448  52.04208  -19.77206 1.000 56.09526  ?  69  GLU   C OE1 1 
ATOM   9128  O OE2 . GLU   G  1 69  ? 73.28864  50.86296  -21.33744 1.000 62.90158  -1 69  GLU   C OE2 1 
ATOM   9129  N N   . SER   G  1 70  ? 76.86174  48.98635  -15.56592 1.000 47.33343  ?  70  SER   C N   1 
ATOM   9130  C CA  . SER   G  1 70  ? 78.03491  49.18315  -14.72353 1.000 19.11510  ?  70  SER   C CA  1 
ATOM   9131  C C   . SER   G  1 70  ? 78.76072  47.89080  -14.36232 1.000 47.87727  ?  70  SER   C C   1 
ATOM   9132  O O   . SER   G  1 70  ? 79.89768  47.96378  -13.88588 1.000 32.61015  ?  70  SER   C O   1 
ATOM   9133  C CB  . SER   G  1 70  ? 77.64041  49.88909  -13.42202 1.000 31.71408  ?  70  SER   C CB  1 
ATOM   9134  O OG  . SER   G  1 70  ? 76.85818  49.03024  -12.59945 1.000 53.05149  ?  70  SER   C OG  1 
ATOM   9135  N N   . ASP   G  1 71  ? 78.13886  46.72463  -14.53841 1.000 49.45960  ?  71  ASP   C N   1 
ATOM   9136  C CA  . ASP   G  1 71  ? 78.72120  45.45278  -14.10247 1.000 44.74198  ?  71  ASP   C CA  1 
ATOM   9137  C C   . ASP   G  1 71  ? 78.58262  44.46799  -15.25488 1.000 51.01092  ?  71  ASP   C C   1 
ATOM   9138  O O   . ASP   G  1 71  ? 77.44443  44.12198  -15.64488 1.000 50.91411  ?  71  ASP   C O   1 
ATOM   9139  C CB  . ASP   G  1 71  ? 78.03735  44.92831  -12.82772 1.000 53.90749  ?  71  ASP   C CB  1 
ATOM   9140  C CG  . ASP   G  1 71  ? 78.58896  43.56357  -12.33793 1.000 93.16736  ?  71  ASP   C CG  1 
ATOM   9141  O OD1 . ASP   G  1 71  ? 79.09790  42.73665  -13.14084 1.000 57.09148  ?  71  ASP   C OD1 1 
ATOM   9142  O OD2 . ASP   G  1 71  ? 78.48507  43.29706  -11.11784 1.000 70.99644  -1 71  ASP   C OD2 1 
ATOM   9143  N N   . PRO   G  1 72  ? 79.68630  43.97323  -15.80316 1.000 54.83044  ?  72  PRO   C N   1 
ATOM   9144  C CA  . PRO   G  1 72  ? 79.58693  43.09154  -16.97949 1.000 53.07916  ?  72  PRO   C CA  1 
ATOM   9145  C C   . PRO   G  1 72  ? 78.77791  41.82255  -16.73537 1.000 43.93237  ?  72  PRO   C C   1 
ATOM   9146  O O   . PRO   G  1 72  ? 78.14027  41.32303  -17.66906 1.000 49.67146  ?  72  PRO   C O   1 
ATOM   9147  C CB  . PRO   G  1 72  ? 81.05513  42.78219  -17.30361 1.000 39.29738  ?  72  PRO   C CB  1 
ATOM   9148  C CG  . PRO   G  1 72  ? 81.81043  43.07321  -16.02150 1.000 45.14208  ?  72  PRO   C CG  1 
ATOM   9149  C CD  . PRO   G  1 72  ? 81.06880  44.17514  -15.34049 1.000 31.09736  ?  72  PRO   C CD  1 
ATOM   9150  N N   . VAL   G  1 73  ? 78.77385  41.28384  -15.51300 1.000 49.73450  ?  73  VAL   C N   1 
ATOM   9151  C CA  . VAL   G  1 73  ? 77.97774  40.08912  -15.23457 1.000 60.71991  ?  73  VAL   C CA  1 
ATOM   9152  C C   . VAL   G  1 73  ? 76.49044  40.41690  -15.25447 1.000 68.31507  ?  73  VAL   C C   1 
ATOM   9153  O O   . VAL   G  1 73  ? 75.68708  39.68552  -15.85066 1.000 39.33437  ?  73  VAL   C O   1 
ATOM   9154  C CB  . VAL   G  1 73  ? 78.38240  39.47492  -13.88744 1.000 57.46376  ?  73  VAL   C CB  1 
ATOM   9155  C CG1 . VAL   G  1 73  ? 77.60626  38.20805  -13.65852 1.000 34.51534  ?  73  VAL   C CG1 1 
ATOM   9156  C CG2 . VAL   G  1 73  ? 79.85927  39.19977  -13.86223 1.000 32.35378  ?  73  VAL   C CG2 1 
ATOM   9157  N N   . VAL   G  1 74  ? 76.10338  41.50142  -14.56846 1.000 51.40502  ?  74  VAL   C N   1 
ATOM   9158  C CA  . VAL   G  1 74  ? 74.71674  41.96305  -14.58434 1.000 42.00238  ?  74  VAL   C CA  1 
ATOM   9159  C C   . VAL   G  1 74  ? 74.28104  42.24913  -16.01410 1.000 52.83472  ?  74  VAL   C C   1 
ATOM   9160  O O   . VAL   G  1 74  ? 73.22300  41.79196  -16.46918 1.000 57.46457  ?  74  VAL   C O   1 
ATOM   9161  C CB  . VAL   G  1 74  ? 74.56155  43.21038  -13.69058 1.000 44.12893  ?  74  VAL   C CB  1 
ATOM   9162  C CG1 . VAL   G  1 74  ? 73.14584  43.79617  -13.77139 1.000 27.05705  ?  74  VAL   C CG1 1 
ATOM   9163  C CG2 . VAL   G  1 74  ? 74.89927  42.87687  -12.27688 1.000 33.89366  ?  74  VAL   C CG2 1 
ATOM   9164  N N   . HIS   G  1 75  ? 75.10302  43.01065  -16.74202 1.000 55.32876  ?  75  HIS   C N   1 
ATOM   9165  C CA  . HIS   G  1 75  ? 74.81801  43.33058  -18.13668 1.000 48.02925  ?  75  HIS   C CA  1 
ATOM   9166  C C   . HIS   G  1 75  ? 74.56079  42.06652  -18.95496 1.000 36.86991  ?  75  HIS   C C   1 
ATOM   9167  O O   . HIS   G  1 75  ? 73.58272  41.98078  -19.70972 1.000 43.78459  ?  75  HIS   C O   1 
ATOM   9168  C CB  . HIS   G  1 75  ? 75.99099  44.12064  -18.71018 1.000 39.60207  ?  75  HIS   C CB  1 
ATOM   9169  C CG  . HIS   G  1 75  ? 75.68779  44.80411  -20.00212 1.000 72.42974  ?  75  HIS   C CG  1 
ATOM   9170  N ND1 . HIS   G  1 75  ? 76.35413  45.93545  -20.41259 1.000 81.87767  ?  75  HIS   C ND1 1 
ATOM   9171  C CD2 . HIS   G  1 75  ? 74.78889  44.52096  -20.97291 1.000 73.87714  ?  75  HIS   C CD2 1 
ATOM   9172  C CE1 . HIS   G  1 75  ? 75.87441  46.32294  -21.57946 1.000 69.37015  ?  75  HIS   C CE1 1 
ATOM   9173  N NE2 . HIS   G  1 75  ? 74.92844  45.47802  -21.94471 1.000 56.04998  ?  75  HIS   C NE2 1 
ATOM   9174  N N   . GLN   G  1 76  ? 75.43071  41.06476  -18.80673 1.000 57.59480  ?  76  GLN   C N   1 
ATOM   9175  C CA  . GLN   G  1 76  ? 75.24907  39.82449  -19.54906 1.000 36.26989  ?  76  GLN   C CA  1 
ATOM   9176  C C   . GLN   G  1 76  ? 73.92119  39.16515  -19.19068 1.000 59.46399  ?  76  GLN   C C   1 
ATOM   9177  O O   . GLN   G  1 76  ? 73.21581  38.65710  -20.07099 1.000 48.73098  ?  76  GLN   C O   1 
ATOM   9178  C CB  . GLN   G  1 76  ? 76.42498  38.88067  -19.28153 1.000 61.69081  ?  76  GLN   C CB  1 
ATOM   9179  C CG  . GLN   G  1 76  ? 76.50278  37.71908  -20.25555 1.000 37.66886  ?  76  GLN   C CG  1 
ATOM   9180  C CD  . GLN   G  1 76  ? 76.49726  38.16937  -21.69945 1.000 95.93789  ?  76  GLN   C CD  1 
ATOM   9181  O OE1 . GLN   G  1 76  ? 77.34031  38.97005  -22.11430 1.000 55.58437  ?  76  GLN   C OE1 1 
ATOM   9182  N NE2 . GLN   G  1 76  ? 75.54376  37.66127  -22.47511 1.000 47.65967  ?  76  GLN   C NE2 1 
ATOM   9183  N N   . GLU   G  1 77  ? 73.55511  39.18380  -17.90164 1.000 51.37372  ?  77  GLU   C N   1 
ATOM   9184  C CA  . GLU   G  1 77  ? 72.25947  38.65274  -17.49248 1.000 42.36754  ?  77  GLU   C CA  1 
ATOM   9185  C C   . GLU   G  1 77  ? 71.11776  39.38038  -18.19934 1.000 69.72835  ?  77  GLU   C C   1 
ATOM   9186  O O   . GLU   G  1 77  ? 70.15102  38.74633  -18.64755 1.000 36.33398  ?  77  GLU   C O   1 
ATOM   9187  C CB  . GLU   G  1 77  ? 72.11675  38.74342  -15.97591 1.000 41.90846  ?  77  GLU   C CB  1 
ATOM   9188  C CG  . GLU   G  1 77  ? 72.82753  37.60715  -15.25613 1.000 37.00414  ?  77  GLU   C CG  1 
ATOM   9189  C CD  . GLU   G  1 77  ? 73.08750  37.87348  -13.77223 1.000 69.39317  ?  77  GLU   C CD  1 
ATOM   9190  O OE1 . GLU   G  1 77  ? 72.74659  38.98290  -13.29058 1.000 51.05213  ?  77  GLU   C OE1 1 
ATOM   9191  O OE2 . GLU   G  1 77  ? 73.63437  36.95988  -13.09227 1.000 44.81015  -1 77  GLU   C OE2 1 
ATOM   9192  N N   . PHE   G  1 78  ? 71.23090  40.70638  -18.35388 1.000 33.38652  ?  78  PHE   C N   1 
ATOM   9193  C CA  . PHE   G  1 78  ? 70.20284  41.48353  -19.04319 1.000 54.45335  ?  78  PHE   C CA  1 
ATOM   9194  C C   . PHE   G  1 78  ? 70.29360  41.36950  -20.55561 1.000 53.72058  ?  78  PHE   C C   1 
ATOM   9195  O O   . PHE   G  1 78  ? 69.51403  42.01345  -21.26621 1.000 61.38217  ?  78  PHE   C O   1 
ATOM   9196  C CB  . PHE   G  1 78  ? 70.25683  42.96252  -18.63016 1.000 35.03132  ?  78  PHE   C CB  1 
ATOM   9197  C CG  . PHE   G  1 78  ? 69.45937  43.25431  -17.41087 1.000 53.49027  ?  78  PHE   C CG  1 
ATOM   9198  C CD1 . PHE   G  1 78  ? 68.09355  43.50470  -17.51163 1.000 39.82828  ?  78  PHE   C CD1 1 
ATOM   9199  C CD2 . PHE   G  1 78  ? 70.05625  43.21684  -16.14761 1.000 28.27939  ?  78  PHE   C CD2 1 
ATOM   9200  C CE1 . PHE   G  1 78  ? 67.32839  43.75585  -16.37016 1.000 37.72861  ?  78  PHE   C CE1 1 
ATOM   9201  C CE2 . PHE   G  1 78  ? 69.30503  43.45804  -14.99540 1.000 48.06316  ?  78  PHE   C CE2 1 
ATOM   9202  C CZ  . PHE   G  1 78  ? 67.93563  43.73276  -15.10096 1.000 35.47003  ?  78  PHE   C CZ  1 
ATOM   9203  N N   . ILE   G  1 79  ? 71.20992  40.56572  -21.07268 1.000 52.45175  ?  79  ILE   C N   1 
ATOM   9204  C CA  . ILE   G  1 79  ? 71.17194  40.16321  -22.46123 1.000 46.10162  ?  79  ILE   C CA  1 
ATOM   9205  C C   . ILE   G  1 79  ? 70.60922  38.75885  -22.59525 1.000 62.83711  ?  79  ILE   C C   1 
ATOM   9206  O O   . ILE   G  1 79  ? 69.62583  38.53561  -23.30392 1.000 39.17127  ?  79  ILE   C O   1 
ATOM   9207  C CB  . ILE   G  1 79  ? 72.57582  40.27014  -23.09871 1.000 54.86645  ?  79  ILE   C CB  1 
ATOM   9208  C CG1 . ILE   G  1 79  ? 72.94951  41.72959  -23.28226 1.000 41.31344  ?  79  ILE   C CG1 1 
ATOM   9209  C CG2 . ILE   G  1 79  ? 72.60853  39.52981  -24.41433 1.000 42.11647  ?  79  ILE   C CG2 1 
ATOM   9210  C CD1 . ILE   G  1 79  ? 74.39401  41.92302  -23.50161 1.000 38.56222  ?  79  ILE   C CD1 1 
ATOM   9211  N N   . ASP   G  1 80  ? 71.20367  37.80018  -21.87366 1.000 37.94960  ?  80  ASP   C N   1 
ATOM   9212  C CA  . ASP   G  1 80  ? 70.79926  36.40798  -22.01824 1.000 54.04973  ?  80  ASP   C CA  1 
ATOM   9213  C C   . ASP   G  1 80  ? 69.32295  36.20511  -21.70902 1.000 45.22680  ?  80  ASP   C C   1 
ATOM   9214  O O   . ASP   G  1 80  ? 68.67746  35.35208  -22.33165 1.000 54.38012  ?  80  ASP   C O   1 
ATOM   9215  C CB  . ASP   G  1 80  ? 71.66390  35.52933  -21.12213 1.000 47.85056  ?  80  ASP   C CB  1 
ATOM   9216  C CG  . ASP   G  1 80  ? 73.15728  35.63165  -21.46065 1.000 66.14156  ?  80  ASP   C CG  1 
ATOM   9217  O OD1 . ASP   G  1 80  ? 73.50320  36.14807  -22.54426 1.000 64.32741  ?  80  ASP   C OD1 1 
ATOM   9218  O OD2 . ASP   G  1 80  ? 73.98759  35.19332  -20.62261 1.000 72.01896  -1 80  ASP   C OD2 1 
ATOM   9219  N N   . MET   G  1 81  ? 68.76654  36.98081  -20.76329 1.000 47.85724  ?  81  MET   C N   1 
ATOM   9220  C CA  . MET   G  1 81  ? 67.37125  36.79357  -20.36806 1.000 41.56266  ?  81  MET   C CA  1 
ATOM   9221  C C   . MET   G  1 81  ? 66.39462  37.09204  -21.51465 1.000 64.33698  ?  81  MET   C C   1 
ATOM   9222  O O   . MET   G  1 81  ? 65.24177  36.63037  -21.45650 1.000 51.69867  ?  81  MET   C O   1 
ATOM   9223  C CB  . MET   G  1 81  ? 67.01871  37.66045  -19.13961 1.000 41.56766  ?  81  MET   C CB  1 
ATOM   9224  C CG  . MET   G  1 81  ? 66.96074  39.16890  -19.38195 1.000 48.03002  ?  81  MET   C CG  1 
ATOM   9225  S SD  . MET   G  1 81  ? 66.45431  40.20999  -17.96397 1.000 47.91439  ?  81  MET   C SD  1 
ATOM   9226  C CE  . MET   G  1 81  ? 67.61514  39.72274  -16.67665 1.000 44.53244  ?  81  MET   C CE  1 
ATOM   9227  N N   . PHE   G  1 82  ? 66.82965  37.80641  -22.57103 1.000 38.75915  ?  82  PHE   C N   1 
ATOM   9228  C CA  . PHE   G  1 82  ? 65.97181  38.13477  -23.70106 1.000 64.15933  ?  82  PHE   C CA  1 
ATOM   9229  C C   . PHE   G  1 82  ? 66.10477  37.16127  -24.86054 1.000 37.02056  ?  82  PHE   C C   1 
ATOM   9230  O O   . PHE   G  1 82  ? 65.46319  37.37136  -25.89727 1.000 100.40211 ?  82  PHE   C O   1 
ATOM   9231  C CB  . PHE   G  1 82  ? 66.29116  39.53636  -24.18552 1.000 39.65196  ?  82  PHE   C CB  1 
ATOM   9232  C CG  . PHE   G  1 82  ? 65.76061  40.59395  -23.30947 1.000 82.80669  ?  82  PHE   C CG  1 
ATOM   9233  C CD1 . PHE   G  1 82  ? 64.44013  40.99135  -23.42297 1.000 36.73216  ?  82  PHE   C CD1 1 
ATOM   9234  C CD2 . PHE   G  1 82  ? 66.56461  41.17652  -22.35208 1.000 39.34435  ?  82  PHE   C CD2 1 
ATOM   9235  C CE1 . PHE   G  1 82  ? 63.93423  41.96906  -22.60186 1.000 55.49500  ?  82  PHE   C CE1 1 
ATOM   9236  C CE2 . PHE   G  1 82  ? 66.06913  42.15094  -21.53032 1.000 56.76182  ?  82  PHE   C CE2 1 
ATOM   9237  C CZ  . PHE   G  1 82  ? 64.74482  42.54676  -21.65130 1.000 32.46611  ?  82  PHE   C CZ  1 
ATOM   9238  N N   . GLU   G  1 83  ? 66.91842  36.11093  -24.70996 1.000 62.25775  ?  83  GLU   C N   1 
ATOM   9239  C CA  . GLU   G  1 83  ? 67.28691  35.25543  -25.83328 1.000 67.02231  ?  83  GLU   C CA  1 
ATOM   9240  C C   . GLU   G  1 83  ? 66.06864  34.75829  -26.58372 1.000 75.35097  ?  83  GLU   C C   1 
ATOM   9241  O O   . GLU   G  1 83  ? 65.19005  34.12434  -26.00424 1.000 51.61527  ?  83  GLU   C O   1 
ATOM   9242  C CB  . GLU   G  1 83  ? 68.13502  34.08402  -25.34832 1.000 42.35615  ?  83  GLU   C CB  1 
ATOM   9243  C CG  . GLU   G  1 83  ? 69.02580  33.32732  -26.36840 1.000 107.10783 ?  83  GLU   C CG  1 
ATOM   9244  C CD  . GLU   G  1 83  ? 70.41721  33.04932  -25.79507 1.000 104.12286 ?  83  GLU   C CD  1 
ATOM   9245  O OE1 . GLU   G  1 83  ? 71.14676  34.03504  -25.51046 1.000 110.93989 ?  83  GLU   C OE1 1 
ATOM   9246  O OE2 . GLU   G  1 83  ? 70.78899  31.86617  -25.60545 1.000 40.12393  ?  83  GLU   C OE2 1 
ATOM   9247  N N   . GLY   G  1 84  ? 66.01971  35.06692  -27.87932 1.000 82.35916  ?  84  GLY   C N   1 
ATOM   9248  C CA  . GLY   G  1 84  ? 64.93925  34.61587  -28.73281 1.000 46.71630  ?  84  GLY   C CA  1 
ATOM   9249  C C   . GLY   G  1 84  ? 63.59412  35.26932  -28.52585 1.000 79.80213  ?  84  GLY   C C   1 
ATOM   9250  O O   . GLY   G  1 84  ? 62.61750  34.85599  -29.15394 1.000 64.91937  ?  84  GLY   C O   1 
ATOM   9251  N N   . ILE   G  1 85  ? 63.50698  36.27669  -27.66654 1.000 89.45289  ?  85  ILE   C N   1 
ATOM   9252  C CA  . ILE   G  1 85  ? 62.24860  36.98201  -27.45596 1.000 69.06271  ?  85  ILE   C CA  1 
ATOM   9253  C C   . ILE   G  1 85  ? 61.97102  37.85994  -28.66333 1.000 79.27195  ?  85  ILE   C C   1 
ATOM   9254  O O   . ILE   G  1 85  ? 62.77229  38.73509  -29.02499 1.000 73.41862  ?  85  ILE   C O   1 
ATOM   9255  C CB  . ILE   G  1 85  ? 62.28768  37.79736  -26.15601 1.000 62.47870  ?  85  ILE   C CB  1 
ATOM   9256  C CG1 . ILE   G  1 85  ? 62.43801  36.84646  -24.96492 1.000 77.75331  ?  85  ILE   C CG1 1 
ATOM   9257  C CG2 . ILE   G  1 85  ? 61.06446  38.72616  -26.05004 1.000 64.59496  ?  85  ILE   C CG2 1 
ATOM   9258  C CD1 . ILE   G  1 85  ? 62.04526  37.42413  -23.64404 1.000 69.65889  ?  85  ILE   C CD1 1 
ATOM   9259  N N   . GLN   G  1 86  ? 60.86242  37.57338  -29.32928 1.000 67.64611  ?  86  GLN   C N   1 
ATOM   9260  C CA  . GLN   G  1 86  ? 60.51548  38.27657  -30.54594 1.000 99.26129  ?  86  GLN   C CA  1 
ATOM   9261  C C   . GLN   G  1 86  ? 59.62167  39.48970  -30.28621 1.000 50.10070  ?  86  GLN   C C   1 
ATOM   9262  O O   . GLN   G  1 86  ? 59.60102  40.41241  -31.10947 1.000 96.79732  ?  86  GLN   C O   1 
ATOM   9263  C CB  . GLN   G  1 86  ? 59.82546  37.32905  -31.53442 1.000 63.39678  ?  86  GLN   C CB  1 
ATOM   9264  C CG  . GLN   G  1 86  ? 60.45598  35.91735  -31.52410 1.000 136.86492 ?  86  GLN   C CG  1 
ATOM   9265  C CD  . GLN   G  1 86  ? 59.57474  34.88341  -30.80471 1.000 170.30698 ?  86  GLN   C CD  1 
ATOM   9266  O OE1 . GLN   G  1 86  ? 58.81662  35.19208  -29.86996 1.000 161.65317 ?  86  GLN   C OE1 1 
ATOM   9267  N NE2 . GLN   G  1 86  ? 59.63544  33.65202  -31.29453 1.000 154.42328 ?  86  GLN   C NE2 1 
ATOM   9268  N N   . ASP   G  1 87  ? 58.93622  39.55237  -29.14279 1.000 100.05535 ?  87  ASP   C N   1 
ATOM   9269  C CA  . ASP   G  1 87  ? 58.03699  40.66029  -28.84318 1.000 66.32775  ?  87  ASP   C CA  1 
ATOM   9270  C C   . ASP   G  1 87  ? 58.69422  41.72210  -27.96742 1.000 55.47959  ?  87  ASP   C C   1 
ATOM   9271  O O   . ASP   G  1 87  ? 59.75700  41.52830  -27.37453 1.000 75.86726  ?  87  ASP   C O   1 
ATOM   9272  C CB  . ASP   G  1 87  ? 56.77366  40.15418  -28.14562 1.000 58.58231  ?  87  ASP   C CB  1 
ATOM   9273  C CG  . ASP   G  1 87  ? 56.18136  38.96644  -28.84293 1.000 131.34780 ?  87  ASP   C CG  1 
ATOM   9274  O OD1 . ASP   G  1 87  ? 56.48716  38.77590  -30.04420 1.000 111.60351 ?  87  ASP   C OD1 1 
ATOM   9275  O OD2 . ASP   G  1 87  ? 55.42008  38.21731  -28.16903 1.000 109.64272 -1 87  ASP   C OD2 1 
ATOM   9276  N N   . SER   G  1 88  ? 58.01106  42.83891  -27.86912 1.000 61.68409  ?  88  SER   C N   1 
ATOM   9277  C CA  . SER   G  1 88  ? 58.45225  43.94363  -27.04184 1.000 50.76172  ?  88  SER   C CA  1 
ATOM   9278  C C   . SER   G  1 88  ? 58.13313  43.65696  -25.57117 1.000 93.15025  ?  88  SER   C C   1 
ATOM   9279  O O   . SER   G  1 88  ? 56.99044  43.30448  -25.24462 1.000 60.65045  ?  88  SER   C O   1 
ATOM   9280  C CB  . SER   G  1 88  ? 57.78006  45.22651  -27.50685 1.000 51.81083  ?  88  SER   C CB  1 
ATOM   9281  O OG  . SER   G  1 88  ? 58.59680  45.93250  -28.42727 1.000 67.94111  ?  88  SER   C OG  1 
ATOM   9282  N N   . PRO   G  1 89  ? 59.11775  43.78880  -24.64458 1.000 57.15800  ?  89  PRO   C N   1 
ATOM   9283  C CA  . PRO   G  1 89  ? 60.50831  44.23734  -24.81712 1.000 33.67451  ?  89  PRO   C CA  1 
ATOM   9284  C C   . PRO   G  1 89  ? 61.44150  43.17449  -25.40304 1.000 61.37963  ?  89  PRO   C C   1 
ATOM   9285  O O   . PRO   G  1 89  ? 61.40957  42.02114  -24.97965 1.000 43.97809  ?  89  PRO   C O   1 
ATOM   9286  C CB  . PRO   G  1 89  ? 60.96112  44.57546  -23.38909 1.000 56.04317  ?  89  PRO   C CB  1 
ATOM   9287  C CG  . PRO   G  1 89  ? 59.83792  44.13645  -22.45616 1.000 53.71283  ?  89  PRO   C CG  1 
ATOM   9288  C CD  . PRO   G  1 89  ? 58.89471  43.30892  -23.27611 1.000 48.30924  ?  89  PRO   C CD  1 
ATOM   9289  N N   . ARG   G  1 90  ? 62.31681  43.54119  -26.34259 1.000 36.07166  ?  90  ARG   C N   1 
ATOM   9290  C CA  . ARG   G  1 90  ? 63.28646  42.59783  -26.88412 1.000 53.07063  ?  90  ARG   C CA  1 
ATOM   9291  C C   . ARG   G  1 90  ? 64.68293  42.78107  -26.30111 1.000 43.75554  ?  90  ARG   C C   1 
ATOM   9292  O O   . ARG   G  1 90  ? 65.53063  41.90849  -26.47135 1.000 43.34294  ?  90  ARG   C O   1 
ATOM   9293  C CB  . ARG   G  1 90  ? 63.36323  42.70949  -28.41292 1.000 37.46177  ?  90  ARG   C CB  1 
ATOM   9294  C CG  . ARG   G  1 90  ? 62.06476  42.28100  -29.06017 1.000 85.41941  ?  90  ARG   C CG  1 
ATOM   9295  C CD  . ARG   G  1 90  ? 61.86143  42.65227  -30.54408 1.000 93.77302  ?  90  ARG   C CD  1 
ATOM   9296  N NE  . ARG   G  1 90  ? 62.57730  43.83808  -31.01334 1.000 125.17867 ?  90  ARG   C NE  1 
ATOM   9297  C CZ  . ARG   G  1 90  ? 62.09297  45.07735  -31.07503 1.000 111.51014 ?  90  ARG   C CZ  1 
ATOM   9298  N NH1 . ARG   G  1 90  ? 60.84422  45.36297  -30.71421 1.000 84.44626  ?  90  ARG   C NH1 1 
ATOM   9299  N NH2 . ARG   G  1 90  ? 62.89865  46.06560  -31.47023 1.000 116.29443 ?  90  ARG   C NH2 1 
ATOM   9300  N N   . ASN   G  1 91  ? 64.95211  43.87416  -25.60158 1.000 39.72167  ?  91  ASN   C N   1 
ATOM   9301  C CA  . ASN   G  1 91  ? 66.24560  44.05423  -24.96134 1.000 44.20180  ?  91  ASN   C CA  1 
ATOM   9302  C C   . ASN   G  1 91  ? 66.02587  44.90525  -23.73179 1.000 42.82835  ?  91  ASN   C C   1 
ATOM   9303  O O   . ASN   G  1 91  ? 64.90460  45.34170  -23.43453 1.000 49.38167  ?  91  ASN   C O   1 
ATOM   9304  C CB  . ASN   G  1 91  ? 67.25546  44.70957  -25.90608 1.000 36.20321  ?  91  ASN   C CB  1 
ATOM   9305  C CG  . ASN   G  1 91  ? 66.64672  45.89128  -26.62704 1.000 46.88072  ?  91  ASN   C CG  1 
ATOM   9306  O OD1 . ASN   G  1 91  ? 66.30652  46.91103  -26.01812 1.000 57.07075  ?  91  ASN   C OD1 1 
ATOM   9307  N ND2 . ASN   G  1 91  ? 66.47992  45.75304  -27.92494 1.000 42.90642  ?  91  ASN   C ND2 1 
ATOM   9308  N N   . TYR   G  1 92  ? 67.11684  45.14357  -23.01367 1.000 48.69184  ?  92  TYR   C N   1 
ATOM   9309  C CA  . TYR   G  1 92  ? 66.96774  45.91674  -21.79715 1.000 42.43358  ?  92  TYR   C CA  1 
ATOM   9310  C C   . TYR   G  1 92  ? 66.66591  47.37901  -22.11174 1.000 46.52755  ?  92  TYR   C C   1 
ATOM   9311  O O   . TYR   G  1 92  ? 66.02071  48.05972  -21.30496 1.000 51.24417  ?  92  TYR   C O   1 
ATOM   9312  C CB  . TYR   G  1 92  ? 68.19540  45.73061  -20.87980 1.000 31.65059  ?  92  TYR   C CB  1 
ATOM   9313  C CG  . TYR   G  1 92  ? 69.47027  46.45407  -21.23881 1.000 37.11698  ?  92  TYR   C CG  1 
ATOM   9314  C CD1 . TYR   G  1 92  ? 69.66869  47.78031  -20.85876 1.000 35.33488  ?  92  TYR   C CD1 1 
ATOM   9315  C CD2 . TYR   G  1 92  ? 70.52282  45.78143  -21.88604 1.000 43.55078  ?  92  TYR   C CD2 1 
ATOM   9316  C CE1 . TYR   G  1 92  ? 70.85072  48.43985  -21.15946 1.000 54.31629  ?  92  TYR   C CE1 1 
ATOM   9317  C CE2 . TYR   G  1 92  ? 71.71151  46.43544  -22.18807 1.000 51.41109  ?  92  TYR   C CE2 1 
ATOM   9318  C CZ  . TYR   G  1 92  ? 71.86570  47.76503  -21.82514 1.000 46.95445  ?  92  TYR   C CZ  1 
ATOM   9319  O OH  . TYR   G  1 92  ? 73.01833  48.43606  -22.11387 1.000 63.71090  ?  92  TYR   C OH  1 
ATOM   9320  N N   . GLN   G  1 93  ? 67.03603  47.86301  -23.29952 1.000 45.14355  ?  93  GLN   C N   1 
ATOM   9321  C CA  . GLN   G  1 93  ? 66.70938  49.25024  -23.62130 1.000 57.75134  ?  93  GLN   C CA  1 
ATOM   9322  C C   . GLN   G  1 93  ? 65.21001  49.42810  -23.82811 1.000 43.79991  ?  93  GLN   C C   1 
ATOM   9323  O O   . GLN   G  1 93  ? 64.62390  50.41340  -23.36404 1.000 49.21002  ?  93  GLN   C O   1 
ATOM   9324  C CB  . GLN   G  1 93  ? 67.46263  49.71623  -24.86301 1.000 38.62503  ?  93  GLN   C CB  1 
ATOM   9325  C CG  . GLN   G  1 93  ? 68.91144  50.12682  -24.59756 1.000 55.35507  ?  93  GLN   C CG  1 
ATOM   9326  C CD  . GLN   G  1 93  ? 69.89977  49.01002  -24.89837 1.000 174.66193 ?  93  GLN   C CD  1 
ATOM   9327  O OE1 . GLN   G  1 93  ? 69.53194  47.82168  -24.97314 1.000 52.93470  ?  93  GLN   C OE1 1 
ATOM   9328  N NE2 . GLN   G  1 93  ? 71.16517  49.38463  -25.07731 1.000 55.15398  ?  93  GLN   C NE2 1 
ATOM   9329  N N   . GLU   G  1 94  ? 64.56265  48.48615  -24.52375 1.000 48.51720  ?  94  GLU   C N   1 
ATOM   9330  C CA  . GLU   G  1 94  ? 63.11254  48.57399  -24.68033 1.000 20.85999  ?  94  GLU   C CA  1 
ATOM   9331  C C   . GLU   G  1 94  ? 62.42088  48.38959  -23.34344 1.000 55.36534  ?  94  GLU   C C   1 
ATOM   9332  O O   . GLU   G  1 94  ? 61.39857  49.02730  -23.06600 1.000 52.42392  ?  94  GLU   C O   1 
ATOM   9333  C CB  . GLU   G  1 94  ? 62.60667  47.51692  -25.64965 1.000 52.30113  ?  94  GLU   C CB  1 
ATOM   9334  C CG  . GLU   G  1 94  ? 62.81673  47.86667  -27.09142 1.000 73.84398  ?  94  GLU   C CG  1 
ATOM   9335  C CD  . GLU   G  1 94  ? 62.18084  46.82978  -27.98955 1.000 136.54277 ?  94  GLU   C CD  1 
ATOM   9336  O OE1 . GLU   G  1 94  ? 61.13617  46.26199  -27.56115 1.000 45.00825  ?  94  GLU   C OE1 1 
ATOM   9337  O OE2 . GLU   G  1 94  ? 62.73057  46.58303  -29.09179 1.000 98.71540  -1 94  GLU   C OE2 1 
ATOM   9338  N N   . LEU   G  1 95  ? 62.95303  47.49266  -22.50469 1.000 60.08536  ?  95  LEU   C N   1 
ATOM   9339  C CA  . LEU   G  1 95  ? 62.41820  47.33616  -21.15716 1.000 41.12816  ?  95  LEU   C CA  1 
ATOM   9340  C C   . LEU   G  1 95  ? 62.38311  48.67704  -20.44125 1.000 45.25661  ?  95  LEU   C C   1 
ATOM   9341  O O   . LEU   G  1 95  ? 61.33764  49.08820  -19.91941 1.000 41.26619  ?  95  LEU   C O   1 
ATOM   9342  C CB  . LEU   G  1 95  ? 63.24969  46.32805  -20.36695 1.000 48.23727  ?  95  LEU   C CB  1 
ATOM   9343  C CG  . LEU   G  1 95  ? 62.64598  45.97119  -19.00070 1.000 48.30458  ?  95  LEU   C CG  1 
ATOM   9344  C CD1 . LEU   G  1 95  ? 61.27592  45.29803  -19.15279 1.000 42.59304  ?  95  LEU   C CD1 1 
ATOM   9345  C CD2 . LEU   G  1 95  ? 63.61346  45.06969  -18.26913 1.000 33.79164  ?  95  LEU   C CD2 1 
ATOM   9346  N N   . CYS   G  1 96  ? 63.51233  49.40339  -20.46222 1.000 25.78112  ?  96  CYS   C N   1 
ATOM   9347  C CA  . CYS   G  1 96  ? 63.56379  50.70624  -19.80796 1.000 36.57014  ?  96  CYS   C CA  1 
ATOM   9348  C C   . CYS   G  1 96  ? 62.56003  51.68215  -20.41007 1.000 36.76926  ?  96  CYS   C C   1 
ATOM   9349  O O   . CYS   G  1 96  ? 61.95906  52.48643  -19.68477 1.000 56.10848  ?  96  CYS   C O   1 
ATOM   9350  C CB  . CYS   G  1 96  ? 64.96953  51.28200  -19.89201 1.000 30.10356  ?  96  CYS   C CB  1 
ATOM   9351  S SG  . CYS   G  1 96  ? 66.23031  50.42729  -18.91781 1.000 45.80796  ?  96  CYS   C SG  1 
ATOM   9352  N N   . ASN   G  1 97  ? 62.37985  51.64682  -21.73787 1.000 36.28684  ?  97  ASN   C N   1 
ATOM   9353  C CA  . ASN   G  1 97  ? 61.43506  52.57085  -22.36397 1.000 26.55697  ?  97  ASN   C CA  1 
ATOM   9354  C C   . ASN   G  1 97  ? 60.00087  52.24426  -21.96909 1.000 51.38649  ?  97  ASN   C C   1 
ATOM   9355  O O   . ASN   G  1 97  ? 59.20183  53.15545  -21.71514 1.000 32.79883  ?  97  ASN   C O   1 
ATOM   9356  C CB  . ASN   G  1 97  ? 61.57697  52.54636  -23.88287 1.000 38.08354  ?  97  ASN   C CB  1 
ATOM   9357  C CG  . ASN   G  1 97  ? 62.84366  53.20670  -24.35568 1.000 77.55819  ?  97  ASN   C CG  1 
ATOM   9358  O OD1 . ASN   G  1 97  ? 63.31735  54.17233  -23.74963 1.000 50.12409  ?  97  ASN   C OD1 1 
ATOM   9359  N ND2 . ASN   G  1 97  ? 63.40795  52.69142  -25.44536 1.000 35.12945  ?  97  ASN   C ND2 1 
ATOM   9360  N N   . MET   G  1 98  ? 59.65605  50.94985  -21.91290 1.000 28.23513  ?  98  MET   C N   1 
ATOM   9361  C CA  . MET   G  1 98  ? 58.31066  50.56847  -21.49766 1.000 24.56468  ?  98  MET   C CA  1 
ATOM   9362  C C   . MET   G  1 98  ? 58.06641  50.90531  -20.02690 1.000 62.61035  ?  98  MET   C C   1 
ATOM   9363  O O   . MET   G  1 98  ? 56.95528  51.31161  -19.66185 1.000 42.46927  ?  98  MET   C O   1 
ATOM   9364  C CB  . MET   G  1 98  ? 58.08102  49.07952  -21.78474 1.000 31.42169  ?  98  MET   C CB  1 
ATOM   9365  C CG  . MET   G  1 98  ? 58.08684  48.75733  -23.28611 1.000 20.41550  ?  98  MET   C CG  1 
ATOM   9366  S SD  . MET   G  1 98  ? 58.04771  47.02729  -23.76694 1.000 51.52047  ?  98  MET   C SD  1 
ATOM   9367  C CE  . MET   G  1 98  ? 56.33266  46.62097  -23.47128 1.000 38.21814  ?  98  MET   C CE  1 
ATOM   9368  N N   . PHE   G  1 99  ? 59.09145  50.75968  -19.17010 1.000 35.55322  ?  99  PHE   C N   1 
ATOM   9369  C CA  . PHE   G  1 99  ? 58.97044  51.21242  -17.78144 1.000 31.58172  ?  99  PHE   C CA  1 
ATOM   9370  C C   . PHE   G  1 99  ? 58.60276  52.69060  -17.73474 1.000 40.92934  ?  99  PHE   C C   1 
ATOM   9371  O O   . PHE   G  1 99  ? 57.76361  53.11957  -16.92970 1.000 39.79436  ?  99  PHE   C O   1 
ATOM   9372  C CB  . PHE   G  1 99  ? 60.28131  50.99536  -17.00033 1.000 30.05764  ?  99  PHE   C CB  1 
ATOM   9373  C CG  . PHE   G  1 99  ? 60.53267  49.57555  -16.55684 1.000 38.27002  ?  99  PHE   C CG  1 
ATOM   9374  C CD1 . PHE   G  1 99  ? 59.59912  48.55766  -16.77847 1.000 28.09566  ?  99  PHE   C CD1 1 
ATOM   9375  C CD2 . PHE   G  1 99  ? 61.72333  49.26181  -15.90538 1.000 36.92074  ?  99  PHE   C CD2 1 
ATOM   9376  C CE1 . PHE   G  1 99  ? 59.84799  47.25450  -16.36923 1.000 43.64121  ?  99  PHE   C CE1 1 
ATOM   9377  C CE2 . PHE   G  1 99  ? 61.98286  47.96069  -15.48667 1.000 27.23494  ?  99  PHE   C CE2 1 
ATOM   9378  C CZ  . PHE   G  1 99  ? 61.04247  46.94886  -15.72934 1.000 31.33866  ?  99  PHE   C CZ  1 
ATOM   9379  N N   . ASN   G  1 100 ? 59.24465  53.48505  -18.59894 1.000 32.22388  ?  100 ASN   C N   1 
ATOM   9380  C CA  . ASN   G  1 100 ? 59.02064  54.92447  -18.62325 1.000 36.47666  ?  100 ASN   C CA  1 
ATOM   9381  C C   . ASN   G  1 100 ? 57.57391  55.26480  -18.98467 1.000 40.26128  ?  100 ASN   C C   1 
ATOM   9382  O O   . ASN   G  1 100 ? 57.01827  56.23688  -18.45297 1.000 47.51709  ?  100 ASN   C O   1 
ATOM   9383  C CB  . ASN   G  1 100 ? 60.02009  55.57435  -19.58449 1.000 35.96451  ?  100 ASN   C CB  1 
ATOM   9384  C CG  . ASN   G  1 100 ? 60.18541  57.05553  -19.33419 1.000 47.41641  ?  100 ASN   C CG  1 
ATOM   9385  O OD1 . ASN   G  1 100 ? 60.66268  57.48165  -18.27690 1.000 60.06303  ?  100 ASN   C OD1 1 
ATOM   9386  N ND2 . ASN   G  1 100 ? 59.80229  57.85402  -20.31509 1.000 47.09641  ?  100 ASN   C ND2 1 
ATOM   9387  N N   . ASP   G  1 101 ? 56.93670  54.46212  -19.85015 1.000 38.31378  ?  101 ASP   C N   1 
ATOM   9388  C CA  . ASP   G  1 101 ? 55.50314  54.62958  -20.09119 1.000 32.03971  ?  101 ASP   C CA  1 
ATOM   9389  C C   . ASP   G  1 101 ? 54.68580  54.17035  -18.88996 1.000 54.70060  ?  101 ASP   C C   1 
ATOM   9390  O O   . ASP   G  1 101 ? 53.80358  54.90042  -18.41555 1.000 46.37486  ?  101 ASP   C O   1 
ATOM   9391  C CB  . ASP   G  1 101 ? 55.06035  53.86371  -21.34302 1.000 32.11498  ?  101 ASP   C CB  1 
ATOM   9392  C CG  . ASP   G  1 101 ? 55.71173  54.37485  -22.62167 1.000 114.87512 ?  101 ASP   C CG  1 
ATOM   9393  O OD1 . ASP   G  1 101 ? 55.99836  55.58883  -22.71573 1.000 50.16480  ?  101 ASP   C OD1 1 
ATOM   9394  O OD2 . ASP   G  1 101 ? 55.92452  53.54959  -23.54387 1.000 59.82157  -1 101 ASP   C OD2 1 
ATOM   9395  N N   . ILE   G  1 102 ? 54.96215  52.95361  -18.39208 1.000 43.19180  ?  102 ILE   C N   1 
ATOM   9396  C CA  . ILE   G  1 102 ? 54.11651  52.34919  -17.36140 1.000 27.64796  ?  102 ILE   C CA  1 
ATOM   9397  C C   . ILE   G  1 102 ? 54.06662  53.22058  -16.11755 1.000 53.20967  ?  102 ILE   C C   1 
ATOM   9398  O O   . ILE   G  1 102 ? 52.98944  53.44381  -15.55179 1.000 36.74769  ?  102 ILE   C O   1 
ATOM   9399  C CB  . ILE   G  1 102 ? 54.59924  50.93374  -17.01352 1.000 30.47689  ?  102 ILE   C CB  1 
ATOM   9400  C CG1 . ILE   G  1 102 ? 54.45605  49.99077  -18.20207 1.000 15.29430  ?  102 ILE   C CG1 1 
ATOM   9401  C CG2 . ILE   G  1 102 ? 53.80534  50.39433  -15.84737 1.000 19.70847  ?  102 ILE   C CG2 1 
ATOM   9402  C CD1 . ILE   G  1 102 ? 54.77435  48.53609  -17.84535 1.000 36.37957  ?  102 ILE   C CD1 1 
ATOM   9403  N N   . PHE   G  1 103 ? 55.22646  53.73998  -15.68085 1.000 30.14941  ?  103 PHE   C N   1 
ATOM   9404  C CA  . PHE   G  1 103 ? 55.32543  54.48871  -14.43005 1.000 54.66269  ?  103 PHE   C CA  1 
ATOM   9405  C C   . PHE   G  1 103 ? 54.70039  55.87828  -14.51129 1.000 32.54705  ?  103 PHE   C C   1 
ATOM   9406  O O   . PHE   G  1 103 ? 54.69288  56.59865  -13.50760 1.000 40.90752  ?  103 PHE   C O   1 
ATOM   9407  C CB  . PHE   G  1 103 ? 56.78976  54.61554  -13.99898 1.000 22.07046  ?  103 PHE   C CB  1 
ATOM   9408  C CG  . PHE   G  1 103 ? 57.47205  53.29024  -13.72668 1.000 39.32854  ?  103 PHE   C CG  1 
ATOM   9409  C CD1 . PHE   G  1 103 ? 56.73485  52.15073  -13.41062 1.000 35.30405  ?  103 PHE   C CD1 1 
ATOM   9410  C CD2 . PHE   G  1 103 ? 58.85720  53.18783  -13.79330 1.000 27.35914  ?  103 PHE   C CD2 1 
ATOM   9411  C CE1 . PHE   G  1 103 ? 57.37542  50.93531  -13.17370 1.000 47.55175  ?  103 PHE   C CE1 1 
ATOM   9412  C CE2 . PHE   G  1 103 ? 59.50494  51.97985  -13.55838 1.000 39.49141  ?  103 PHE   C CE2 1 
ATOM   9413  C CZ  . PHE   G  1 103 ? 58.76396  50.85462  -13.24824 1.000 38.77438  ?  103 PHE   C CZ  1 
ATOM   9414  N N   . ARG   G  1 104 ? 54.19554  56.28616  -15.66942 1.000 41.92106  ?  104 ARG   C N   1 
ATOM   9415  C CA  . ARG   G  1 104 ? 53.57643  57.59053  -15.83341 1.000 42.05610  ?  104 ARG   C CA  1 
ATOM   9416  C C   . ARG   G  1 104 ? 52.06228  57.49698  -15.94060 1.000 25.69875  ?  104 ARG   C C   1 
ATOM   9417  O O   . ARG   G  1 104 ? 51.41278  58.53241  -16.14067 1.000 68.56712  ?  104 ARG   C O   1 
ATOM   9418  C CB  . ARG   G  1 104 ? 54.15311  58.31873  -17.07118 1.000 63.15552  ?  104 ARG   C CB  1 
ATOM   9419  C CG  . ARG   G  1 104 ? 55.67282  58.60564  -17.03619 1.000 86.98679  ?  104 ARG   C CG  1 
ATOM   9420  C CD  . ARG   G  1 104 ? 56.04909  59.81420  -17.89205 1.000 89.42062  ?  104 ARG   C CD  1 
ATOM   9421  N NE  . ARG   G  1 104 ? 57.43970  59.82506  -18.35067 1.000 26.49550  ?  104 ARG   C NE  1 
ATOM   9422  C CZ  . ARG   G  1 104 ? 58.44146  60.52533  -17.81130 1.000 106.28875 ?  104 ARG   C CZ  1 
ATOM   9423  N NH1 . ARG   G  1 104 ? 58.29816  61.18914  -16.66970 1.000 104.24684 ?  104 ARG   C NH1 1 
ATOM   9424  N NH2 . ARG   G  1 104 ? 59.62228  60.56302  -18.43550 1.000 84.55695  ?  104 ARG   C NH2 1 
ATOM   9425  N N   . LYS   G  1 105 ? 51.48176  56.29314  -15.76473 1.000 38.23886  ?  105 LYS   C N   1 
ATOM   9426  C CA  . LYS   G  1 105 ? 50.03984  56.13724  -15.82257 1.000 58.97620  ?  105 LYS   C CA  1 
ATOM   9427  C C   . LYS   G  1 105 ? 49.61219  55.03148  -14.87031 1.000 41.50696  ?  105 LYS   C C   1 
ATOM   9428  O O   . LYS   G  1 105 ? 50.41853  54.20295  -14.44999 1.000 46.13424  ?  105 LYS   C O   1 
ATOM   9429  C CB  . LYS   G  1 105 ? 49.57358  55.88465  -17.26351 1.000 49.19343  ?  105 LYS   C CB  1 
ATOM   9430  C CG  . LYS   G  1 105 ? 50.19991  54.69000  -17.90779 1.000 39.13826  ?  105 LYS   C CG  1 
ATOM   9431  C CD  . LYS   G  1 105 ? 49.83218  54.58700  -19.38793 1.000 39.60322  ?  105 LYS   C CD  1 
ATOM   9432  C CE  . LYS   G  1 105 ? 50.49677  55.67299  -20.19871 1.000 69.81039  ?  105 LYS   C CE  1 
ATOM   9433  N NZ  . LYS   G  1 105 ? 50.67267  55.24454  -21.61201 1.000 82.66329  ?  105 LYS   C NZ  1 
ATOM   9434  N N   . ALA   G  1 106 ? 48.33916  55.05764  -14.51428 1.000 50.78918  ?  106 ALA   C N   1 
ATOM   9435  C CA  . ALA   G  1 106 ? 47.76966  54.09877  -13.58647 1.000 44.05080  ?  106 ALA   C CA  1 
ATOM   9436  C C   . ALA   G  1 106 ? 47.37487  52.81640  -14.31154 1.000 27.44144  ?  106 ALA   C C   1 
ATOM   9437  O O   . ALA   G  1 106 ? 47.11119  52.83514  -15.51543 1.000 46.79102  ?  106 ALA   C O   1 
ATOM   9438  C CB  . ALA   G  1 106 ? 46.55186  54.69643  -12.88182 1.000 30.35796  ?  106 ALA   C CB  1 
ATOM   9439  N N   . PRO   G  1 107 ? 47.34283  51.68324  -13.60751 1.000 56.06167  ?  107 PRO   C N   1 
ATOM   9440  C CA  . PRO   G  1 107 ? 46.93671  50.43222  -14.25462 1.000 38.39402  ?  107 PRO   C CA  1 
ATOM   9441  C C   . PRO   G  1 107 ? 45.45972  50.46357  -14.62647 1.000 48.27684  ?  107 PRO   C C   1 
ATOM   9442  O O   . PRO   G  1 107 ? 44.66837  51.24927  -14.09767 1.000 43.54024  ?  107 PRO   C O   1 
ATOM   9443  C CB  . PRO   G  1 107 ? 47.21005  49.36228  -13.18839 1.000 36.44982  ?  107 PRO   C CB  1 
ATOM   9444  C CG  . PRO   G  1 107 ? 47.86570  50.04070  -12.07035 1.000 33.06096  ?  107 PRO   C CG  1 
ATOM   9445  C CD  . PRO   G  1 107 ? 47.60234  51.49859  -12.16967 1.000 26.88966  ?  107 PRO   C CD  1 
ATOM   9446  N N   . VAL   G  1 108 ? 45.08689  49.57232  -15.54011 1.000 41.67379  ?  108 VAL   C N   1 
ATOM   9447  C CA  . VAL   G  1 108 ? 43.70288  49.43308  -15.95837 1.000 37.53966  ?  108 VAL   C CA  1 
ATOM   9448  C C   . VAL   G  1 108 ? 43.26044  47.98380  -15.74572 1.000 48.77145  ?  108 VAL   C C   1 
ATOM   9449  O O   . VAL   G  1 108 ? 44.06667  47.08623  -15.49082 1.000 49.38683  ?  108 VAL   C O   1 
ATOM   9450  C CB  . VAL   G  1 108 ? 43.49098  49.88231  -17.41920 1.000 47.77531  ?  108 VAL   C CB  1 
ATOM   9451  C CG1 . VAL   G  1 108 ? 43.95087  51.34218  -17.60051 1.000 28.79777  ?  108 VAL   C CG1 1 
ATOM   9452  C CG2 . VAL   G  1 108 ? 44.23343  48.98161  -18.36271 1.000 28.54398  ?  108 VAL   C CG2 1 
ATOM   9453  N N   . TYR   G  1 109 ? 41.95088  47.77311  -15.82728 1.000 39.34432  ?  109 TYR   C N   1 
ATOM   9454  C CA  . TYR   G  1 109 ? 41.38378  46.44478  -15.62798 1.000 68.79763  ?  109 TYR   C CA  1 
ATOM   9455  C C   . TYR   G  1 109 ? 41.47990  45.62620  -16.91028 1.000 39.06091  ?  109 TYR   C C   1 
ATOM   9456  O O   . TYR   G  1 109 ? 41.29844  46.14822  -18.01372 1.000 52.98558  ?  109 TYR   C O   1 
ATOM   9457  C CB  . TYR   G  1 109 ? 39.92240  46.54229  -15.17631 1.000 33.21516  ?  109 TYR   C CB  1 
ATOM   9458  C CG  . TYR   G  1 109 ? 39.27963  45.18834  -14.98476 1.000 66.02012  ?  109 TYR   C CG  1 
ATOM   9459  C CD1 . TYR   G  1 109 ? 39.37249  44.52097  -13.77864 1.000 34.51120  ?  109 TYR   C CD1 1 
ATOM   9460  C CD2 . TYR   G  1 109 ? 38.60066  44.56562  -16.02313 1.000 38.49010  ?  109 TYR   C CD2 1 
ATOM   9461  C CE1 . TYR   G  1 109 ? 38.79687  43.27335  -13.61458 1.000 76.18312  ?  109 TYR   C CE1 1 
ATOM   9462  C CE2 . TYR   G  1 109 ? 38.02574  43.32236  -15.86915 1.000 59.63150  ?  109 TYR   C CE2 1 
ATOM   9463  C CZ  . TYR   G  1 109 ? 38.12412  42.67792  -14.66619 1.000 35.84823  ?  109 TYR   C CZ  1 
ATOM   9464  O OH  . TYR   G  1 109 ? 37.55772  41.43465  -14.49578 1.000 62.11832  ?  109 TYR   C OH  1 
ATOM   9465  N N   . GLY   G  1 110 ? 41.78089  44.34116  -16.76670 1.000 53.39959  ?  110 GLY   C N   1 
ATOM   9466  C CA  . GLY   G  1 110 ? 41.83312  43.50860  -17.94803 1.000 18.39886  ?  110 GLY   C CA  1 
ATOM   9467  C C   . GLY   G  1 110 ? 42.89143  42.42608  -17.98754 1.000 52.09568  ?  110 GLY   C C   1 
ATOM   9468  O O   . GLY   G  1 110 ? 42.60160  41.31960  -18.44714 1.000 46.09774  ?  110 GLY   C O   1 
ATOM   9469  N N   . ASP   G  1 111 ? 44.11344  42.71120  -17.53554 1.000 61.23655  ?  111 ASP   C N   1 
ATOM   9470  C CA  . ASP   G  1 111 ? 45.17968  41.73009  -17.67336 1.000 51.81526  ?  111 ASP   C CA  1 
ATOM   9471  C C   . ASP   G  1 111 ? 45.18480  40.76028  -16.49677 1.000 35.86183  ?  111 ASP   C C   1 
ATOM   9472  O O   . ASP   G  1 111 ? 44.57858  41.01089  -15.45134 1.000 49.19401  ?  111 ASP   C O   1 
ATOM   9473  C CB  . ASP   G  1 111 ? 46.53119  42.42379  -17.80947 1.000 64.54699  ?  111 ASP   C CB  1 
ATOM   9474  C CG  . ASP   G  1 111 ? 46.74332  42.99724  -19.18765 1.000 63.25799  ?  111 ASP   C CG  1 
ATOM   9475  O OD1 . ASP   G  1 111 ? 46.85470  42.20327  -20.14586 1.000 79.07541  ?  111 ASP   C OD1 1 
ATOM   9476  O OD2 . ASP   G  1 111 ? 46.77316  44.24135  -19.31253 1.000 97.94368  -1 111 ASP   C OD2 1 
ATOM   9477  N N   . LEU   G  1 112 ? 45.89425  39.64622  -16.70831 1.000 72.45004  ?  112 LEU   C N   1 
ATOM   9478  C CA  . LEU   G  1 112 ? 45.97833  38.61247  -15.68331 1.000 40.26680  ?  112 LEU   C CA  1 
ATOM   9479  C C   . LEU   G  1 112 ? 46.72087  39.11812  -14.44423 1.000 78.58144  ?  112 LEU   C C   1 
ATOM   9480  O O   . LEU   G  1 112 ? 46.38221  38.72925  -13.32317 1.000 42.15804  ?  112 LEU   C O   1 
ATOM   9481  C CB  . LEU   G  1 112 ? 46.63615  37.36045  -16.27323 1.000 37.91260  ?  112 LEU   C CB  1 
ATOM   9482  C CG  . LEU   G  1 112 ? 45.93812  36.49704  -17.33814 1.000 137.66796 ?  112 LEU   C CG  1 
ATOM   9483  C CD1 . LEU   G  1 112 ? 45.21315  37.19866  -18.52424 1.000 142.81941 ?  112 LEU   C CD1 1 
ATOM   9484  C CD2 . LEU   G  1 112 ? 47.06042  35.65618  -17.85019 1.000 117.36179 ?  112 LEU   C CD2 1 
ATOM   9485  N N   . GLY   G  1 113 ? 47.69662  40.02185  -14.61790 1.000 40.60415  ?  113 GLY   C N   1 
ATOM   9486  C CA  . GLY   G  1 113 ? 48.40367  40.62975  -13.51936 1.000 39.08296  ?  113 GLY   C CA  1 
ATOM   9487  C C   . GLY   G  1 113 ? 48.71120  42.08805  -13.79604 1.000 42.67277  ?  113 GLY   C C   1 
ATOM   9488  O O   . GLY   G  1 113 ? 48.36258  42.63792  -14.85111 1.000 41.11150  ?  113 GLY   C O   1 
ATOM   9489  N N   . PRO   G  1 114 ? 49.38465  42.74190  -12.85258 1.000 36.83186  ?  114 PRO   C N   1 
ATOM   9490  C CA  . PRO   G  1 114 ? 49.71134  44.17650  -13.01554 1.000 30.15001  ?  114 PRO   C CA  1 
ATOM   9491  C C   . PRO   G  1 114 ? 50.71823  44.38715  -14.13683 1.000 33.11018  ?  114 PRO   C C   1 
ATOM   9492  O O   . PRO   G  1 114 ? 51.32797  43.42392  -14.64096 1.000 37.57877  ?  114 PRO   C O   1 
ATOM   9493  C CB  . PRO   G  1 114 ? 50.27536  44.56896  -11.63891 1.000 35.16115  ?  114 PRO   C CB  1 
ATOM   9494  C CG  . PRO   G  1 114 ? 50.77391  43.26074  -11.04668 1.000 32.11673  ?  114 PRO   C CG  1 
ATOM   9495  C CD  . PRO   G  1 114 ? 49.90823  42.16777  -11.60134 1.000 33.20211  ?  114 PRO   C CD  1 
ATOM   9496  N N   . PRO   G  1 115 ? 50.88932  45.63287  -14.59569 1.000 27.13088  ?  115 PRO   C N   1 
ATOM   9497  C CA  . PRO   G  1 115 ? 51.56502  45.84018  -15.89744 1.000 38.11594  ?  115 PRO   C CA  1 
ATOM   9498  C C   . PRO   G  1 115 ? 53.04964  45.52647  -15.91082 1.000 30.21474  ?  115 PRO   C C   1 
ATOM   9499  O O   . PRO   G  1 115 ? 53.54654  45.04987  -16.94139 1.000 35.30779  ?  115 PRO   C O   1 
ATOM   9500  C CB  . PRO   G  1 115 ? 51.30673  47.32333  -16.20803 1.000 19.88861  ?  115 PRO   C CB  1 
ATOM   9501  C CG  . PRO   G  1 115 ? 50.71421  47.92608  -14.96326 1.000 22.44671  ?  115 PRO   C CG  1 
ATOM   9502  C CD  . PRO   G  1 115 ? 50.10744  46.81148  -14.17513 1.000 32.41457  ?  115 PRO   C CD  1 
ATOM   9503  N N   . VAL   G  1 116 ? 53.78236  45.79790  -14.82144 1.000 45.08762  ?  116 VAL   C N   1 
ATOM   9504  C CA  . VAL   G  1 116 ? 55.19880  45.42853  -14.79484 1.000 35.34867  ?  116 VAL   C CA  1 
ATOM   9505  C C   . VAL   G  1 116 ? 55.35795  43.91203  -14.81533 1.000 37.82969  ?  116 VAL   C C   1 
ATOM   9506  O O   . VAL   G  1 116 ? 56.19684  43.37159  -15.55056 1.000 41.40355  ?  116 VAL   C O   1 
ATOM   9507  C CB  . VAL   G  1 116 ? 55.93036  46.04470  -13.59029 1.000 42.51899  ?  116 VAL   C CB  1 
ATOM   9508  C CG1 . VAL   G  1 116 ? 57.38933  45.59461  -13.61577 1.000 34.59334  ?  116 VAL   C CG1 1 
ATOM   9509  C CG2 . VAL   G  1 116 ? 55.84435  47.56409  -13.62195 1.000 26.55287  ?  116 VAL   C CG2 1 
ATOM   9510  N N   . TYR   G  1 117 ? 54.55974  43.19726  -14.02040 1.000 30.72775  ?  117 TYR   C N   1 
ATOM   9511  C CA  . TYR   G  1 117 ? 54.59554  41.74087  -14.09574 1.000 44.26048  ?  117 TYR   C CA  1 
ATOM   9512  C C   . TYR   G  1 117 ? 54.38104  41.25422  -15.53257 1.000 38.28119  ?  117 TYR   C C   1 
ATOM   9513  O O   . TYR   G  1 117 ? 55.11903  40.39024  -16.02075 1.000 43.29281  ?  117 TYR   C O   1 
ATOM   9514  C CB  . TYR   G  1 117 ? 53.55419  41.10447  -13.16152 1.000 29.84562  ?  117 TYR   C CB  1 
ATOM   9515  C CG  . TYR   G  1 117 ? 53.36663  39.65733  -13.55327 1.000 37.11592  ?  117 TYR   C CG  1 
ATOM   9516  C CD1 . TYR   G  1 117 ? 54.29931  38.69357  -13.16687 1.000 33.34472  ?  117 TYR   C CD1 1 
ATOM   9517  C CD2 . TYR   G  1 117 ? 52.31702  39.26308  -14.38092 1.000 50.05463  ?  117 TYR   C CD2 1 
ATOM   9518  C CE1 . TYR   G  1 117 ? 54.17269  37.36650  -13.55706 1.000 33.77658  ?  117 TYR   C CE1 1 
ATOM   9519  C CE2 . TYR   G  1 117 ? 52.18875  37.94885  -14.77689 1.000 27.46956  ?  117 TYR   C CE2 1 
ATOM   9520  C CZ  . TYR   G  1 117 ? 53.12054  37.00483  -14.36156 1.000 43.89736  ?  117 TYR   C CZ  1 
ATOM   9521  O OH  . TYR   G  1 117 ? 52.99643  35.69393  -14.74343 1.000 33.64090  ?  117 TYR   C OH  1 
ATOM   9522  N N   . MET   G  1 118 ? 53.36982  41.80074  -16.22381 1.000 41.82811  ?  118 MET   C N   1 
ATOM   9523  C CA  . MET   G  1 118 ? 53.02884  41.31777  -17.56361 1.000 31.66030  ?  118 MET   C CA  1 
ATOM   9524  C C   . MET   G  1 118 ? 54.23096  41.38562  -18.51153 1.000 47.28072  ?  118 MET   C C   1 
ATOM   9525  O O   . MET   G  1 118 ? 54.54587  40.40507  -19.19640 1.000 39.44825  ?  118 MET   C O   1 
ATOM   9526  C CB  . MET   G  1 118 ? 51.84612  42.10647  -18.14138 1.000 34.72913  ?  118 MET   C CB  1 
ATOM   9527  C CG  . MET   G  1 118 ? 50.46354  41.86962  -17.51524 1.000 24.39998  ?  118 MET   C CG  1 
ATOM   9528  S SD  . MET   G  1 118 ? 49.83903  40.17430  -17.53628 1.000 42.61558  ?  118 MET   C SD  1 
ATOM   9529  C CE  . MET   G  1 118 ? 49.82341  39.85646  -19.29972 1.000 47.18750  ?  118 MET   C CE  1 
ATOM   9530  N N   . ILE   G  1 119 ? 54.94029  42.52255  -18.55310 1.000 28.73305  ?  119 ILE   C N   1 
ATOM   9531  C CA  . ILE   G  1 119 ? 56.11268  42.58069  -19.43166 1.000 40.21230  ?  119 ILE   C CA  1 
ATOM   9532  C C   . ILE   G  1 119 ? 57.35142  41.90397  -18.85353 1.000 40.64741  ?  119 ILE   C C   1 
ATOM   9533  O O   . ILE   G  1 119 ? 58.32334  41.70069  -19.59738 1.000 45.30944  ?  119 ILE   C O   1 
ATOM   9534  C CB  . ILE   G  1 119 ? 56.47739  44.02512  -19.83035 1.000 32.18452  ?  119 ILE   C CB  1 
ATOM   9535  C CG1 . ILE   G  1 119 ? 57.14095  44.77698  -18.68471 1.000 34.47395  ?  119 ILE   C CG1 1 
ATOM   9536  C CG2 . ILE   G  1 119 ? 55.24217  44.77650  -20.26974 1.000 39.69377  ?  119 ILE   C CG2 1 
ATOM   9537  C CD1 . ILE   G  1 119 ? 57.53532  46.17953  -19.08756 1.000 39.35218  ?  119 ILE   C CD1 1 
ATOM   9538  N N   . MET   G  1 120 ? 57.34705  41.51770  -17.56650 1.000 33.09837  ?  120 MET   C N   1 
ATOM   9539  C CA  . MET   G  1 120 ? 58.50882  40.86466  -16.95401 1.000 31.09704  ?  120 MET   C CA  1 
ATOM   9540  C C   . MET   G  1 120 ? 58.42750  39.34286  -16.94405 1.000 36.92797  ?  120 MET   C C   1 
ATOM   9541  O O   . MET   G  1 120 ? 59.45788  38.68687  -16.75791 1.000 36.53291  ?  120 MET   C O   1 
ATOM   9542  C CB  . MET   G  1 120 ? 58.69671  41.32783  -15.49772 1.000 18.72211  ?  120 MET   C CB  1 
ATOM   9543  C CG  . MET   G  1 120 ? 59.16239  42.75878  -15.34736 1.000 26.61322  ?  120 MET   C CG  1 
ATOM   9544  S SD  . MET   G  1 120 ? 60.82344  43.05798  -15.93291 1.000 42.73220  ?  120 MET   C SD  1 
ATOM   9545  C CE  . MET   G  1 120 ? 61.77816  42.43954  -14.54497 1.000 27.37243  ?  120 MET   C CE  1 
ATOM   9546  N N   . ALA   G  1 121 ? 57.23283  38.77243  -17.12618 1.000 31.84300  ?  121 ALA   C N   1 
ATOM   9547  C CA  . ALA   G  1 121 ? 57.03133  37.35415  -16.83216 1.000 37.62786  ?  121 ALA   C CA  1 
ATOM   9548  C C   . ALA   G  1 121 ? 57.94226  36.46829  -17.67172 1.000 38.00347  ?  121 ALA   C C   1 
ATOM   9549  O O   . ALA   G  1 121 ? 58.47126  35.46346  -17.17524 1.000 44.97699  ?  121 ALA   C O   1 
ATOM   9550  C CB  . ALA   G  1 121 ? 55.56126  36.97333  -17.04795 1.000 29.54375  ?  121 ALA   C CB  1 
ATOM   9551  N N   . LYS   G  1 122 ? 58.13262  36.81599  -18.95218 1.000 41.78607  ?  122 LYS   C N   1 
ATOM   9552  C CA  . LYS   G  1 122 ? 58.99935  36.00363  -19.80343 1.000 34.32279  ?  122 LYS   C CA  1 
ATOM   9553  C C   . LYS   G  1 122 ? 60.44891  36.05526  -19.30477 1.000 48.54804  ?  122 LYS   C C   1 
ATOM   9554  O O   . LYS   G  1 122 ? 61.13423  35.03127  -19.26520 1.000 42.38016  ?  122 LYS   C O   1 
ATOM   9555  C CB  . LYS   G  1 122 ? 58.88874  36.45857  -21.27296 1.000 33.73749  ?  122 LYS   C CB  1 
ATOM   9556  C CG  . LYS   G  1 122 ? 57.89172  35.68816  -22.14249 1.000 120.83754 ?  122 LYS   C CG  1 
ATOM   9557  C CD  . LYS   G  1 122 ? 56.69655  36.53527  -22.58554 1.000 102.30353 ?  122 LYS   C CD  1 
ATOM   9558  C CE  . LYS   G  1 122 ? 55.70938  35.71352  -23.39043 1.000 99.14238  ?  122 LYS   C CE  1 
ATOM   9559  N NZ  . LYS   G  1 122 ? 55.03329  34.67252  -22.55145 1.000 73.92179  ?  122 LYS   C NZ  1 
ATOM   9560  N N   . LEU   G  1 123 ? 60.91392  37.23029  -18.86217 1.000 41.37549  ?  123 LEU   C N   1 
ATOM   9561  C CA  . LEU   G  1 123 ? 62.26689  37.36796  -18.30907 1.000 40.87617  ?  123 LEU   C CA  1 
ATOM   9562  C C   . LEU   G  1 123 ? 62.43142  36.58697  -17.00837 1.000 65.86575  ?  123 LEU   C C   1 
ATOM   9563  O O   . LEU   G  1 123 ? 63.43661  35.88062  -16.81321 1.000 32.94504  ?  123 LEU   C O   1 
ATOM   9564  C CB  . LEU   G  1 123 ? 62.59137  38.84644  -18.08058 1.000 31.96311  ?  123 LEU   C CB  1 
ATOM   9565  C CG  . LEU   G  1 123 ? 62.23340  39.72024  -19.27610 1.000 40.90553  ?  123 LEU   C CG  1 
ATOM   9566  C CD1 . LEU   G  1 123 ? 62.58689  41.18085  -19.03461 1.000 35.06009  ?  123 LEU   C CD1 1 
ATOM   9567  C CD2 . LEU   G  1 123 ? 62.94857  39.18982  -20.49369 1.000 34.88956  ?  123 LEU   C CD2 1 
ATOM   9568  N N   . MET   G  1 124 ? 61.47105  36.73707  -16.08521 1.000 33.88778  ?  124 MET   C N   1 
ATOM   9569  C CA  . MET   G  1 124 ? 61.53675  36.00440  -14.82476 1.000 45.27907  ?  124 MET   C CA  1 
ATOM   9570  C C   . MET   G  1 124 ? 61.65629  34.50665  -15.04128 1.000 37.84556  ?  124 MET   C C   1 
ATOM   9571  O O   . MET   G  1 124 ? 62.17247  33.79431  -14.17304 1.000 36.99522  ?  124 MET   C O   1 
ATOM   9572  C CB  . MET   G  1 124 ? 60.29928  36.27815  -13.98050 1.000 22.86183  ?  124 MET   C CB  1 
ATOM   9573  C CG  . MET   G  1 124 ? 60.10190  37.71786  -13.62464 1.000 43.10706  ?  124 MET   C CG  1 
ATOM   9574  S SD  . MET   G  1 124 ? 58.35890  38.03048  -13.27188 1.000 44.99271  ?  124 MET   C SD  1 
ATOM   9575  C CE  . MET   G  1 124 ? 58.03108  36.94279  -11.90079 1.000 20.66508  ?  124 MET   C CE  1 
ATOM   9576  N N   . ASN   G  1 125 ? 61.17592  34.01055  -16.18048 1.000 45.03203  ?  125 ASN   C N   1 
ATOM   9577  C CA  . ASN   G  1 125 ? 61.12601  32.58531  -16.45233 1.000 38.91415  ?  125 ASN   C CA  1 
ATOM   9578  C C   . ASN   G  1 125 ? 62.41391  32.05021  -17.09358 1.000 44.53784  ?  125 ASN   C C   1 
ATOM   9579  O O   . ASN   G  1 125 ? 62.39394  30.98926  -17.72504 1.000 48.52623  ?  125 ASN   C O   1 
ATOM   9580  C CB  . ASN   G  1 125 ? 59.92816  32.27017  -17.34545 1.000 37.40016  ?  125 ASN   C CB  1 
ATOM   9581  C CG  . ASN   G  1 125 ? 59.48927  30.82633  -17.23098 1.000 35.53108  ?  125 ASN   C CG  1 
ATOM   9582  O OD1 . ASN   G  1 125 ? 59.84739  30.12001  -16.27921 1.000 41.69441  ?  125 ASN   C OD1 1 
ATOM   9583  N ND2 . ASN   G  1 125 ? 58.69888  30.37987  -18.19478 1.000 52.84422  ?  125 ASN   C ND2 1 
ATOM   9584  N N   . THR   G  1 126 ? 63.53016  32.74140  -16.93338 1.000 44.16194  ?  126 THR   C N   1 
ATOM   9585  C CA  . THR   G  1 126 ? 64.81416  32.27693  -17.43021 1.000 53.25186  ?  126 THR   C CA  1 
ATOM   9586  C C   . THR   G  1 126 ? 65.79325  32.16470  -16.27293 1.000 32.12225  ?  126 THR   C C   1 
ATOM   9587  O O   . THR   G  1 126 ? 65.59740  32.75818  -15.20833 1.000 51.04491  ?  126 THR   C O   1 
ATOM   9588  C CB  . THR   G  1 126 ? 65.38552  33.23225  -18.48579 1.000 38.00196  ?  126 THR   C CB  1 
ATOM   9589  O OG1 . THR   G  1 126 ? 65.83986  34.44160  -17.84844 1.000 37.42431  ?  126 THR   C OG1 1 
ATOM   9590  C CG2 . THR   G  1 126 ? 64.32427  33.57249  -19.52934 1.000 23.02214  ?  126 THR   C CG2 1 
ATOM   9591  N N   . ARG   G  1 127 ? 66.89828  31.43152  -16.49416 1.000 65.42858  ?  127 ARG   C N   1 
ATOM   9592  C CA  . ARG   G  1 127 ? 67.94888  31.36668  -15.47377 1.000 27.34245  ?  127 ARG   C CA  1 
ATOM   9593  C C   . ARG   G  1 127 ? 68.68155  32.69997  -15.37364 1.000 85.77830  ?  127 ARG   C C   1 
ATOM   9594  O O   . ARG   G  1 127 ? 69.06838  33.13311  -14.27752 1.000 46.39322  ?  127 ARG   C O   1 
ATOM   9595  C CB  . ARG   G  1 127 ? 68.93593  30.20004  -15.76679 1.000 13.73242  ?  127 ARG   C CB  1 
ATOM   9596  C CG  . ARG   G  1 127 ? 70.33525  30.28807  -15.14625 1.000 67.38264  ?  127 ARG   C CG  1 
ATOM   9597  C CD  . ARG   G  1 127 ? 71.33467  31.07406  -16.02586 1.000 138.33578 ?  127 ARG   C CD  1 
ATOM   9598  N NE  . ARG   G  1 127 ? 72.42779  31.66916  -15.25813 1.000 136.90884 ?  127 ARG   C NE  1 
ATOM   9599  C CZ  . ARG   G  1 127 ? 73.29149  32.55076  -15.75008 1.000 126.03638 ?  127 ARG   C CZ  1 
ATOM   9600  N NH1 . ARG   G  1 127 ? 73.23777  32.92708  -17.02992 1.000 29.77376  ?  127 ARG   C NH1 1 
ATOM   9601  N NH2 . ARG   G  1 127 ? 74.22243  33.07414  -14.94098 1.000 70.61777  ?  127 ARG   C NH2 1 
ATOM   9602  N N   . ALA   G  1 128 ? 68.88843  33.36447  -16.50626 1.000 32.81227  ?  128 ALA   C N   1 
ATOM   9603  C CA  . ALA   G  1 128 ? 69.53477  34.67264  -16.47460 1.000 45.78352  ?  128 ALA   C CA  1 
ATOM   9604  C C   . ALA   G  1 128 ? 68.68974  35.68023  -15.69864 1.000 36.71480  ?  128 ALA   C C   1 
ATOM   9605  O O   . ALA   G  1 128 ? 69.22344  36.45519  -14.89148 1.000 47.55456  ?  128 ALA   C O   1 
ATOM   9606  C CB  . ALA   G  1 128 ? 69.80688  35.16448  -17.90633 1.000 34.55175  ?  128 ALA   C CB  1 
ATOM   9607  N N   . GLY   G  1 129 ? 67.36595  35.66841  -15.91260 1.000 50.97483  ?  129 GLY   C N   1 
ATOM   9608  C CA  . GLY   G  1 129 ? 66.49593  36.60942  -15.21179 1.000 18.98405  ?  129 GLY   C CA  1 
ATOM   9609  C C   . GLY   G  1 129 ? 66.45906  36.36448  -13.71045 1.000 43.48093  ?  129 GLY   C C   1 
ATOM   9610  O O   . GLY   G  1 129 ? 66.58231  37.29738  -12.90717 1.000 33.32625  ?  129 GLY   C O   1 
ATOM   9611  N N   . PHE   G  1 130 ? 66.30660  35.09914  -13.31033 1.000 30.07078  ?  130 PHE   C N   1 
ATOM   9612  C CA  . PHE   G  1 130 ? 66.33767  34.77445  -11.89002 1.000 30.15716  ?  130 PHE   C CA  1 
ATOM   9613  C C   . PHE   G  1 130 ? 67.64551  35.23175  -11.23597 1.000 51.08872  ?  130 PHE   C C   1 
ATOM   9614  O O   . PHE   G  1 130 ? 67.61906  35.80368  -10.14105 1.000 42.24347  ?  130 PHE   C O   1 
ATOM   9615  C CB  . PHE   G  1 130 ? 66.11676  33.27467  -11.70514 1.000 18.74939  ?  130 PHE   C CB  1 
ATOM   9616  C CG  . PHE   G  1 130 ? 66.19957  32.82156  -10.28171 1.000 32.19408  ?  130 PHE   C CG  1 
ATOM   9617  C CD1 . PHE   G  1 130 ? 67.43440  32.53240  -9.69355  1.000 32.19006  ?  130 PHE   C CD1 1 
ATOM   9618  C CD2 . PHE   G  1 130 ? 65.05075  32.67260  -9.52669  1.000 25.79130  ?  130 PHE   C CD2 1 
ATOM   9619  C CE1 . PHE   G  1 130 ? 67.52760  32.11063  -8.37512  1.000 31.02303  ?  130 PHE   C CE1 1 
ATOM   9620  C CE2 . PHE   G  1 130 ? 65.13305  32.25246  -8.19917  1.000 39.61616  ?  130 PHE   C CE2 1 
ATOM   9621  C CZ  . PHE   G  1 130 ? 66.39275  31.96584  -7.62573  1.000 26.06472  ?  130 PHE   C CZ  1 
ATOM   9622  N N   . SER   G  1 131 ? 68.79884  34.98190  -11.87935 1.000 28.77706  ?  131 SER   C N   1 
ATOM   9623  C CA  . SER   G  1 131 ? 70.06722  35.48164  -11.33824 1.000 46.45044  ?  131 SER   C CA  1 
ATOM   9624  C C   . SER   G  1 131 ? 70.02007  36.98747  -11.10892 1.000 34.10949  ?  131 SER   C C   1 
ATOM   9625  O O   . SER   G  1 131 ? 70.37400  37.47601  -10.02534 1.000 44.95607  ?  131 SER   C O   1 
ATOM   9626  C CB  . SER   G  1 131 ? 71.23256  35.14376  -12.26734 1.000 17.67550  ?  131 SER   C CB  1 
ATOM   9627  O OG  . SER   G  1 131 ? 71.82992  33.93942  -11.87026 1.000 89.54251  ?  131 SER   C OG  1 
ATOM   9628  N N   . ALA   G  1 132 ? 69.62337  37.74371  -12.13869 1.000 30.24329  ?  132 ALA   C N   1 
ATOM   9629  C CA  . ALA   G  1 132 ? 69.60633  39.19665  -12.01599 1.000 24.50551  ?  132 ALA   C CA  1 
ATOM   9630  C C   . ALA   G  1 132 ? 68.69354  39.62970  -10.88092 1.000 38.79574  ?  132 ALA   C C   1 
ATOM   9631  O O   . ALA   G  1 132 ? 69.07624  40.45120  -10.03364 1.000 32.55987  ?  132 ALA   C O   1 
ATOM   9632  C CB  . ALA   G  1 132 ? 69.16058  39.83110  -13.32927 1.000 25.22772  ?  132 ALA   C CB  1 
ATOM   9633  N N   . PHE   G  1 133 ? 67.49148  39.04773  -10.83210 1.000 25.01270  ?  133 PHE   C N   1 
ATOM   9634  C CA  . PHE   G  1 133 ? 66.43882  39.44647  -9.90574  1.000 35.58740  ?  133 PHE   C CA  1 
ATOM   9635  C C   . PHE   G  1 133 ? 66.68262  38.95473  -8.48146  1.000 42.53606  ?  133 PHE   C C   1 
ATOM   9636  O O   . PHE   G  1 133 ? 65.90228  39.28830  -7.57936  1.000 32.04863  ?  133 PHE   C O   1 
ATOM   9637  C CB  . PHE   G  1 133 ? 65.08370  38.95482  -10.42465 1.000 27.80620  ?  133 PHE   C CB  1 
ATOM   9638  C CG  . PHE   G  1 133 ? 64.79996  39.38007  -11.84600 1.000 38.75625  ?  133 PHE   C CG  1 
ATOM   9639  C CD1 . PHE   G  1 133 ? 65.42245  40.51526  -12.38943 1.000 34.30845  ?  133 PHE   C CD1 1 
ATOM   9640  C CD2 . PHE   G  1 133 ? 63.93136  38.64367  -12.64671 1.000 29.02095  ?  133 PHE   C CD2 1 
ATOM   9641  C CE1 . PHE   G  1 133 ? 65.17949  40.90711  -13.70305 1.000 26.17285  ?  133 PHE   C CE1 1 
ATOM   9642  C CE2 . PHE   G  1 133 ? 63.68005  39.01861  -13.95971 1.000 28.44396  ?  133 PHE   C CE2 1 
ATOM   9643  C CZ  . PHE   G  1 133 ? 64.30465  40.15701  -14.49312 1.000 22.23647  ?  133 PHE   C CZ  1 
ATOM   9644  N N   . THR   G  1 134 ? 67.75373  38.19611  -8.24310  1.000 28.57251  ?  134 THR   C N   1 
ATOM   9645  C CA  . THR   G  1 134 ? 68.12196  37.80367  -6.89035  1.000 33.23126  ?  134 THR   C CA  1 
ATOM   9646  C C   . THR   G  1 134 ? 69.41156  38.48508  -6.42470  1.000 31.05796  ?  134 THR   C C   1 
ATOM   9647  O O   . THR   G  1 134 ? 70.09829  37.98370  -5.53094  1.000 39.00954  ?  134 THR   C O   1 
ATOM   9648  C CB  . THR   G  1 134 ? 68.22378  36.28226  -6.76168  1.000 33.24803  ?  134 THR   C CB  1 
ATOM   9649  O OG1 . THR   G  1 134 ? 68.96430  35.73155  -7.86013  1.000 38.93631  ?  134 THR   C OG1 1 
ATOM   9650  C CG2 . THR   G  1 134 ? 66.82753  35.66359  -6.72176  1.000 26.24320  ?  134 THR   C CG2 1 
ATOM   9651  N N   . ARG   G  1 135 ? 69.72595  39.65101  -6.99499  1.000 30.91044  ?  135 ARG   C N   1 
ATOM   9652  C CA  . ARG   G  1 135 ? 70.82195  40.49922  -6.52931  1.000 31.08886  ?  135 ARG   C CA  1 
ATOM   9653  C C   . ARG   G  1 135 ? 70.23297  41.65876  -5.73551  1.000 44.71365  ?  135 ARG   C C   1 
ATOM   9654  O O   . ARG   G  1 135 ? 69.43419  42.44032  -6.27136  1.000 31.32270  ?  135 ARG   C O   1 
ATOM   9655  C CB  . ARG   G  1 135 ? 71.65614  41.03882  -7.69323  1.000 21.90696  ?  135 ARG   C CB  1 
ATOM   9656  C CG  . ARG   G  1 135 ? 72.30526  39.97408  -8.57540  1.000 26.11227  ?  135 ARG   C CG  1 
ATOM   9657  C CD  . ARG   G  1 135 ? 72.74225  40.62271  -9.86238  1.000 28.84820  ?  135 ARG   C CD  1 
ATOM   9658  N NE  . ARG   G  1 135 ? 73.43279  39.70419  -10.75053 1.000 48.14302  ?  135 ARG   C NE  1 
ATOM   9659  C CZ  . ARG   G  1 135 ? 74.65631  39.24348  -10.53575 1.000 51.95911  ?  135 ARG   C CZ  1 
ATOM   9660  N NH1 . ARG   G  1 135 ? 75.35155  39.60085  -9.46748  1.000 43.13363  ?  135 ARG   C NH1 1 
ATOM   9661  N NH2 . ARG   G  1 135 ? 75.18868  38.38743  -11.40571 1.000 41.06353  ?  135 ARG   C NH2 1 
ATOM   9662  N N   . GLN   G  1 136 ? 70.62377  41.76781  -4.45966  1.000 26.90118  ?  136 GLN   C N   1 
ATOM   9663  C CA  . GLN   G  1 136 ? 70.12995  42.86369  -3.63030  1.000 28.91965  ?  136 GLN   C CA  1 
ATOM   9664  C C   . GLN   G  1 136 ? 70.42103  44.21500  -4.26155  1.000 26.28375  ?  136 GLN   C C   1 
ATOM   9665  O O   . GLN   G  1 136 ? 69.61459  45.14675  -4.12350  1.000 43.77813  ?  136 GLN   C O   1 
ATOM   9666  C CB  . GLN   G  1 136 ? 70.73709  42.78780  -2.23033  1.000 26.97214  ?  136 GLN   C CB  1 
ATOM   9667  C CG  . GLN   G  1 136 ? 70.37092  41.51656  -1.50450  1.000 22.20493  ?  136 GLN   C CG  1 
ATOM   9668  C CD  . GLN   G  1 136 ? 69.94444  41.76538  -0.07946  1.000 47.46326  ?  136 GLN   C CD  1 
ATOM   9669  O OE1 . GLN   G  1 136 ? 70.59090  42.53271  0.66583   1.000 35.38323  ?  136 GLN   C OE1 1 
ATOM   9670  N NE2 . GLN   G  1 136 ? 68.83986  41.12399  0.31608   1.000 22.70735  ?  136 GLN   C NE2 1 
ATOM   9671  N N   . ARG   G  1 137 ? 71.56034  44.35430  -4.93184  1.000 22.59229  ?  137 ARG   C N   1 
ATOM   9672  C CA  . ARG   G  1 137 ? 71.88873  45.62126  -5.56763  1.000 31.54581  ?  137 ARG   C CA  1 
ATOM   9673  C C   . ARG   G  1 137 ? 70.84153  46.02323  -6.59522  1.000 19.76849  ?  137 ARG   C C   1 
ATOM   9674  O O   . ARG   G  1 137 ? 70.28101  47.11633  -6.51151  1.000 38.26170  ?  137 ARG   C O   1 
ATOM   9675  C CB  . ARG   G  1 137 ? 73.26894  45.52527  -6.19093  1.000 32.74414  ?  137 ARG   C CB  1 
ATOM   9676  C CG  . ARG   G  1 137 ? 74.32578  45.74233  -5.13291  1.000 24.25068  ?  137 ARG   C CG  1 
ATOM   9677  C CD  . ARG   G  1 137 ? 75.64727  45.94602  -5.80223  1.000 28.09636  ?  137 ARG   C CD  1 
ATOM   9678  N NE  . ARG   G  1 137 ? 76.76424  45.76627  -4.88525  1.000 25.82715  ?  137 ARG   C NE  1 
ATOM   9679  C CZ  . ARG   G  1 137 ? 77.97472  45.42295  -5.29533  1.000 38.25453  ?  137 ARG   C CZ  1 
ATOM   9680  N NH1 . ARG   G  1 137 ? 78.22165  45.16754  -6.58355  1.000 24.20102  ?  137 ARG   C NH1 1 
ATOM   9681  N NH2 . ARG   G  1 137 ? 78.95302  45.31779  -4.39933  1.000 25.11619  ?  137 ARG   C NH2 1 
ATOM   9682  N N   . LEU   G  1 138 ? 70.54463  45.13099  -7.55276  1.000 19.45001  ?  138 LEU   C N   1 
ATOM   9683  C CA  . LEU   G  1 138 ? 69.49074  45.42118  -8.53022  1.000 32.50749  ?  138 LEU   C CA  1 
ATOM   9684  C C   . LEU   G  1 138 ? 68.14950  45.70806  -7.85639  1.000 41.94650  ?  138 LEU   C C   1 
ATOM   9685  O O   . LEU   G  1 138 ? 67.42920  46.63454  -8.25217  1.000 31.49578  ?  138 LEU   C O   1 
ATOM   9686  C CB  . LEU   G  1 138 ? 69.33302  44.25173  -9.49613  1.000 26.29082  ?  138 LEU   C CB  1 
ATOM   9687  C CG  . LEU   G  1 138 ? 68.36841  44.52056  -10.63970 1.000 40.17068  ?  138 LEU   C CG  1 
ATOM   9688  C CD1 . LEU   G  1 138 ? 68.95691  45.61694  -11.50295 1.000 26.64921  ?  138 LEU   C CD1 1 
ATOM   9689  C CD2 . LEU   G  1 138 ? 68.12250  43.26414  -11.45858 1.000 23.98219  ?  138 LEU   C CD2 1 
ATOM   9690  N N   . ASN   G  1 139 ? 67.79106  44.91989  -6.84299  1.000 26.18820  ?  139 ASN   C N   1 
ATOM   9691  C CA  . ASN   G  1 139 ? 66.48833  45.10665  -6.21848  1.000 42.39064  ?  139 ASN   C CA  1 
ATOM   9692  C C   . ASN   G  1 139 ? 66.36626  46.47322  -5.55571  1.000 28.99793  ?  139 ASN   C C   1 
ATOM   9693  O O   . ASN   G  1 139 ? 65.25234  47.00767  -5.46255  1.000 42.90011  ?  139 ASN   C O   1 
ATOM   9694  C CB  . ASN   G  1 139 ? 66.21739  43.96351  -5.24223  1.000 18.69182  ?  139 ASN   C CB  1 
ATOM   9695  C CG  . ASN   G  1 139 ? 65.86019  42.68852  -5.97546  1.000 35.51427  ?  139 ASN   C CG  1 
ATOM   9696  O OD1 . ASN   G  1 139 ? 65.10996  42.73573  -6.95904  1.000 27.09312  ?  139 ASN   C OD1 1 
ATOM   9697  N ND2 . ASN   G  1 139 ? 66.42067  41.55939  -5.55109  1.000 23.91399  ?  139 ASN   C ND2 1 
ATOM   9698  N N   . LEU   G  1 140 ? 67.48873  47.06600  -5.12190  1.000 38.23135  ?  140 LEU   C N   1 
ATOM   9699  C CA  . LEU   G  1 140 ? 67.45575  48.45148  -4.65100  1.000 26.38297  ?  140 LEU   C CA  1 
ATOM   9700  C C   . LEU   G  1 140 ? 66.89882  49.38176  -5.71888  1.000 48.66312  ?  140 LEU   C C   1 
ATOM   9701  O O   . LEU   G  1 140 ? 66.17630  50.33838  -5.40197  1.000 27.58853  ?  140 LEU   C O   1 
ATOM   9702  C CB  . LEU   G  1 140 ? 68.84907  48.91896  -4.25107  1.000 25.92162  ?  140 LEU   C CB  1 
ATOM   9703  C CG  . LEU   G  1 140 ? 69.36742  48.34280  -2.94225  1.000 42.16269  ?  140 LEU   C CG  1 
ATOM   9704  C CD1 . LEU   G  1 140 ? 70.79495  48.77721  -2.67497  1.000 20.13087  ?  140 LEU   C CD1 1 
ATOM   9705  C CD2 . LEU   G  1 140 ? 68.45730  48.76007  -1.81618  1.000 13.98603  ?  140 LEU   C CD2 1 
ATOM   9706  N N   . HIS   G  1 141 ? 67.22561  49.11710  -6.99472  1.000 29.96489  ?  141 HIS   C N   1 
ATOM   9707  C CA  . HIS   G  1 141 ? 66.72832  49.97112  -8.06889  1.000 27.86360  ?  141 HIS   C CA  1 
ATOM   9708  C C   . HIS   G  1 141 ? 65.24627  49.73332  -8.33008  1.000 29.04063  ?  141 HIS   C C   1 
ATOM   9709  O O   . HIS   G  1 141 ? 64.47812  50.69249  -8.46694  1.000 35.72763  ?  141 HIS   C O   1 
ATOM   9710  C CB  . HIS   G  1 141 ? 67.55034  49.75570  -9.32658  1.000 17.83948  ?  141 HIS   C CB  1 
ATOM   9711  C CG  . HIS   G  1 141 ? 68.92099  50.34441  -9.23395  1.000 45.39025  ?  141 HIS   C CG  1 
ATOM   9712  N ND1 . HIS   G  1 141 ? 69.16934  51.67833  -9.47069  1.000 43.22772  ?  141 HIS   C ND1 1 
ATOM   9713  C CD2 . HIS   G  1 141 ? 70.11237  49.79281  -8.89617  1.000 38.54899  ?  141 HIS   C CD2 1 
ATOM   9714  C CE1 . HIS   G  1 141 ? 70.45655  51.92068  -9.29801  1.000 30.74999  ?  141 HIS   C CE1 1 
ATOM   9715  N NE2 . HIS   G  1 141 ? 71.05277  50.79270  -8.95351  1.000 43.99829  ?  141 HIS   C NE2 1 
ATOM   9716  N N   . PHE   G  1 142 ? 64.81540  48.46612  -8.37741  1.000 27.45664  ?  142 PHE   C N   1 
ATOM   9717  C CA  . PHE   G  1 142 ? 63.38220  48.19183  -8.48777  1.000 40.69166  ?  142 PHE   C CA  1 
ATOM   9718  C C   . PHE   G  1 142 ? 62.60559  48.90463  -7.39057  1.000 27.58639  ?  142 PHE   C C   1 
ATOM   9719  O O   . PHE   G  1 142 ? 61.53020  49.46981  -7.63956  1.000 29.54557  ?  142 PHE   C O   1 
ATOM   9720  C CB  . PHE   G  1 142 ? 63.11748  46.68812  -8.43242  1.000 26.65746  ?  142 PHE   C CB  1 
ATOM   9721  C CG  . PHE   G  1 142 ? 63.45754  45.96931  -9.70234  1.000 33.84185  ?  142 PHE   C CG  1 
ATOM   9722  C CD1 . PHE   G  1 142 ? 63.03078  46.45816  -10.92251 1.000 28.67389  ?  142 PHE   C CD1 1 
ATOM   9723  C CD2 . PHE   G  1 142 ? 64.21457  44.80724  -9.67789  1.000 30.16495  ?  142 PHE   C CD2 1 
ATOM   9724  C CE1 . PHE   G  1 142 ? 63.35016  45.79619  -12.09255 1.000 27.75264  ?  142 PHE   C CE1 1 
ATOM   9725  C CE2 . PHE   G  1 142 ? 64.52933  44.14276  -10.85227 1.000 31.27022  ?  142 PHE   C CE2 1 
ATOM   9726  C CZ  . PHE   G  1 142 ? 64.09671  44.64126  -12.05316 1.000 26.48687  ?  142 PHE   C CZ  1 
ATOM   9727  N N   . LYS   G  1 143 ? 63.13736  48.88991  -6.16964  1.000 33.51283  ?  143 LYS   C N   1 
ATOM   9728  C CA  . LYS   G  1 143 ? 62.47963  49.59728  -5.08273  1.000 29.17980  ?  143 LYS   C CA  1 
ATOM   9729  C C   . LYS   G  1 143 ? 62.26919  51.05476  -5.44764  1.000 32.45543  ?  143 LYS   C C   1 
ATOM   9730  O O   . LYS   G  1 143 ? 61.14667  51.56935  -5.34763  1.000 35.81700  ?  143 LYS   C O   1 
ATOM   9731  C CB  . LYS   G  1 143 ? 63.29498  49.47715  -3.80087  1.000 32.73293  ?  143 LYS   C CB  1 
ATOM   9732  C CG  . LYS   G  1 143 ? 62.52217  49.89072  -2.58102  1.000 19.29764  ?  143 LYS   C CG  1 
ATOM   9733  C CD  . LYS   G  1 143 ? 63.41054  50.54855  -1.56617  1.000 27.45924  ?  143 LYS   C CD  1 
ATOM   9734  C CE  . LYS   G  1 143 ? 62.69505  50.66181  -0.23375  1.000 34.01754  ?  143 LYS   C CE  1 
ATOM   9735  N NZ  . LYS   G  1 143 ? 61.51677  51.56936  -0.26727  1.000 38.62670  ?  143 LYS   C NZ  1 
ATOM   9736  N N   . LYS   G  1 144 ? 63.32198  51.74299  -5.94135  1.000 20.16755  ?  144 LYS   C N   1 
ATOM   9737  C CA  . LYS   G  1 144 ? 63.14904  53.16235  -6.24658  1.000 30.80157  ?  144 LYS   C CA  1 
ATOM   9738  C C   . LYS   G  1 144 ? 62.20000  53.33295  -7.40949  1.000 17.50669  ?  144 LYS   C C   1 
ATOM   9739  O O   . LYS   G  1 144 ? 61.36501  54.25333  -7.40226  1.000 32.91300  ?  144 LYS   C O   1 
ATOM   9740  C CB  . LYS   G  1 144 ? 64.49449  53.84927  -6.54738  1.000 11.28424  ?  144 LYS   C CB  1 
ATOM   9741  C CG  . LYS   G  1 144 ? 64.47484  55.39876  -6.45119  1.000 59.59568  ?  144 LYS   C CG  1 
ATOM   9742  C CD  . LYS   G  1 144 ? 65.51661  56.03539  -7.37123  1.000 103.10731 ?  144 LYS   C CD  1 
ATOM   9743  C CE  . LYS   G  1 144 ? 66.71549  55.10199  -7.53155  1.000 127.70844 ?  144 LYS   C CE  1 
ATOM   9744  N NZ  . LYS   G  1 144 ? 67.73643  55.41640  -8.59289  1.000 46.97099  ?  144 LYS   C NZ  1 
ATOM   9745  N N   . LEU   G  1 145 ? 62.30884  52.46572  -8.42124  1.000 25.36452  ?  145 LEU   C N   1 
ATOM   9746  C CA  . LEU   G  1 145 ? 61.38163  52.58867  -9.54289  1.000 19.79256  ?  145 LEU   C CA  1 
ATOM   9747  C C   . LEU   G  1 145 ? 59.93476  52.54884  -9.05519  1.000 39.95382  ?  145 LEU   C C   1 
ATOM   9748  O O   . LEU   G  1 145 ? 59.14584  53.46161  -9.33163  1.000 38.18071  ?  145 LEU   C O   1 
ATOM   9749  C CB  . LEU   G  1 145 ? 61.64871  51.48921  -10.57706 1.000 30.62883  ?  145 LEU   C CB  1 
ATOM   9750  C CG  . LEU   G  1 145 ? 63.02973  51.55388  -11.24201 1.000 33.28016  ?  145 LEU   C CG  1 
ATOM   9751  C CD1 . LEU   G  1 145 ? 63.20076  50.48853  -12.31727 1.000 26.98126  ?  145 LEU   C CD1 1 
ATOM   9752  C CD2 . LEU   G  1 145 ? 63.25377  52.92406  -11.83104 1.000 26.36109  ?  145 LEU   C CD2 1 
ATOM   9753  N N   . PHE   G  1 146 ? 59.58563  51.52701  -8.27047  1.000 27.29477  ?  146 PHE   C N   1 
ATOM   9754  C CA  . PHE   G  1 146 ? 58.19555  51.36420  -7.85570  1.000 31.24889  ?  146 PHE   C CA  1 
ATOM   9755  C C   . PHE   G  1 146 ? 57.77723  52.42177  -6.84369  1.000 39.48816  ?  146 PHE   C C   1 
ATOM   9756  O O   . PHE   G  1 146 ? 56.62221  52.86030  -6.85749  1.000 40.19788  ?  146 PHE   C O   1 
ATOM   9757  C CB  . PHE   G  1 146 ? 57.97902  49.95583  -7.29443  1.000 31.47756  ?  146 PHE   C CB  1 
ATOM   9758  C CG  . PHE   G  1 146 ? 58.34653  48.84806  -8.26229  1.000 35.05120  ?  146 PHE   C CG  1 
ATOM   9759  C CD1 . PHE   G  1 146 ? 58.34940  49.06868  -9.64102  1.000 35.09462  ?  146 PHE   C CD1 1 
ATOM   9760  C CD2 . PHE   G  1 146 ? 58.67781  47.58921  -7.79455  1.000 28.15967  ?  146 PHE   C CD2 1 
ATOM   9761  C CE1 . PHE   G  1 146 ? 58.67683  48.05290  -10.52358 1.000 35.20989  ?  146 PHE   C CE1 1 
ATOM   9762  C CE2 . PHE   G  1 146 ? 59.01121  46.56462  -8.67119  1.000 31.74272  ?  146 PHE   C CE2 1 
ATOM   9763  C CZ  . PHE   G  1 146 ? 59.00846  46.79300  -10.03787 1.000 37.40090  ?  146 PHE   C CZ  1 
ATOM   9764  N N   . ASP   G  1 147 ? 58.68450  52.84876  -5.96185  1.000 32.07868  ?  147 ASP   C N   1 
ATOM   9765  C CA  . ASP   G  1 147 ? 58.34138  53.95928  -5.07776  1.000 25.70670  ?  147 ASP   C CA  1 
ATOM   9766  C C   . ASP   G  1 147 ? 58.02250  55.20788  -5.89021  1.000 35.27142  ?  147 ASP   C C   1 
ATOM   9767  O O   . ASP   G  1 147 ? 57.05770  55.93271  -5.58912  1.000 33.58526  ?  147 ASP   C O   1 
ATOM   9768  C CB  . ASP   G  1 147 ? 59.47605  54.24805  -4.08922  1.000 18.15315  ?  147 ASP   C CB  1 
ATOM   9769  C CG  . ASP   G  1 147 ? 59.60514  53.19092  -2.99598  1.000 51.23131  ?  147 ASP   C CG  1 
ATOM   9770  O OD1 . ASP   G  1 147 ? 58.64175  52.41650  -2.75066  1.000 43.34730  ?  147 ASP   C OD1 1 
ATOM   9771  O OD2 . ASP   G  1 147 ? 60.68706  53.15583  -2.37054  1.000 47.52777  -1 147 ASP   C OD2 1 
ATOM   9772  N N   . THR   G  1 148 ? 58.82916  55.47371  -6.92612  1.000 28.81162  ?  148 THR   C N   1 
ATOM   9773  C CA  . THR   G  1 148 ? 58.58043  56.61838  -7.79512  1.000 38.26040  ?  148 THR   C CA  1 
ATOM   9774  C C   . THR   G  1 148 ? 57.20905  56.49865  -8.44705  1.000 35.16619  ?  148 THR   C C   1 
ATOM   9775  O O   . THR   G  1 148 ? 56.41860  57.45240  -8.43806  1.000 41.18184  ?  148 THR   C O   1 
ATOM   9776  C CB  . THR   G  1 148 ? 59.69387  56.72623  -8.84651  1.000 33.12164  ?  148 THR   C CB  1 
ATOM   9777  O OG1 . THR   G  1 148 ? 60.90546  57.14883  -8.21253  1.000 33.98919  ?  148 THR   C OG1 1 
ATOM   9778  C CG2 . THR   G  1 148 ? 59.33794  57.73423  -9.93081  1.000 22.42503  ?  148 THR   C CG2 1 
ATOM   9779  N N   . TRP   G  1 149 ? 56.90107  55.30938  -8.98688  1.000 36.54954  ?  149 TRP   C N   1 
ATOM   9780  C CA  . TRP   G  1 149 ? 55.59458  55.06364  -9.58940  1.000 29.65544  ?  149 TRP   C CA  1 
ATOM   9781  C C   . TRP   G  1 149 ? 54.48132  55.30505  -8.57893  1.000 53.68175  ?  149 TRP   C C   1 
ATOM   9782  O O   . TRP   G  1 149 ? 53.46788  55.93796  -8.89812  1.000 38.50098  ?  149 TRP   C O   1 
ATOM   9783  C CB  . TRP   G  1 149 ? 55.53925  53.62974  -10.13407 1.000 27.22630  ?  149 TRP   C CB  1 
ATOM   9784  C CG  . TRP   G  1 149 ? 54.29156  53.28630  -10.94801 1.000 38.25107  ?  149 TRP   C CG  1 
ATOM   9785  C CD1 . TRP   G  1 149 ? 53.35942  54.16112  -11.43735 1.000 32.57315  ?  149 TRP   C CD1 1 
ATOM   9786  C CD2 . TRP   G  1 149 ? 53.85301  51.97325  -11.35516 1.000 48.58972  ?  149 TRP   C CD2 1 
ATOM   9787  N NE1 . TRP   G  1 149 ? 52.37883  53.48047  -12.12332 1.000 44.78506  ?  149 TRP   C NE1 1 
ATOM   9788  C CE2 . TRP   G  1 149 ? 52.65564  52.13910  -12.08590 1.000 31.06358  ?  149 TRP   C CE2 1 
ATOM   9789  C CE3 . TRP   G  1 149 ? 54.35546  50.67394  -11.16970 1.000 30.18104  ?  149 TRP   C CE3 1 
ATOM   9790  C CZ2 . TRP   G  1 149 ? 51.95794  51.05847  -12.64311 1.000 40.50910  ?  149 TRP   C CZ2 1 
ATOM   9791  C CZ3 . TRP   G  1 149 ? 53.64956  49.58860  -11.72448 1.000 33.04323  ?  149 TRP   C CZ3 1 
ATOM   9792  C CH2 . TRP   G  1 149 ? 52.46917  49.79416  -12.44988 1.000 40.26060  ?  149 TRP   C CH2 1 
ATOM   9793  N N   . GLY   G  1 150 ? 54.67114  54.83207  -7.34115  1.000 34.12786  ?  150 GLY   C N   1 
ATOM   9794  C CA  . GLY   G  1 150 ? 53.62333  54.93862  -6.34329  1.000 23.48483  ?  150 GLY   C CA  1 
ATOM   9795  C C   . GLY   G  1 150 ? 53.28796  56.37158  -5.98658  1.000 44.77733  ?  150 GLY   C C   1 
ATOM   9796  O O   . GLY   G  1 150 ? 52.15529  56.66762  -5.58328  1.000 56.83103  ?  150 GLY   C O   1 
ATOM   9797  N N   . LEU   G  1 151 ? 54.26545  57.27370  -6.11626  1.000 40.52812  ?  151 LEU   C N   1 
ATOM   9798  C CA  . LEU   G  1 151 ? 53.99903  58.70435  -5.97689  1.000 35.24626  ?  151 LEU   C CA  1 
ATOM   9799  C C   . LEU   G  1 151 ? 52.90626  59.15811  -6.92342  1.000 74.68680  ?  151 LEU   C C   1 
ATOM   9800  O O   . LEU   G  1 151 ? 51.94660  59.83204  -6.52026  1.000 47.74467  ?  151 LEU   C O   1 
ATOM   9801  C CB  . LEU   G  1 151 ? 55.24732  59.49294  -6.29226  1.000 47.44166  ?  151 LEU   C CB  1 
ATOM   9802  C CG  . LEU   G  1 151 ? 56.31150  59.41915  -5.24448  1.000 68.53832  ?  151 LEU   C CG  1 
ATOM   9803  C CD1 . LEU   G  1 151 ? 57.34031  60.36935  -5.74644  1.000 33.71177  ?  151 LEU   C CD1 1 
ATOM   9804  C CD2 . LEU   G  1 151 ? 55.67089  59.87377  -3.96704  1.000 22.23468  ?  151 LEU   C CD2 1 
ATOM   9805  N N   . PHE   G  1 152 ? 53.08934  58.86196  -8.21152  1.000 26.16097  ?  152 PHE   C N   1 
ATOM   9806  C CA  . PHE   G  1 152 ? 52.06944  59.18346  -9.19231  1.000 38.91137  ?  152 PHE   C CA  1 
ATOM   9807  C C   . PHE   G  1 152 ? 50.73253  58.54074  -8.83858  1.000 52.14462  ?  152 PHE   C C   1 
ATOM   9808  O O   . PHE   G  1 152 ? 49.67803  59.15704  -9.02110  1.000 44.59972  ?  152 PHE   C O   1 
ATOM   9809  C CB  . PHE   G  1 152 ? 52.52142  58.73972  -10.57726 1.000 21.17474  ?  152 PHE   C CB  1 
ATOM   9810  C CG  . PHE   G  1 152 ? 51.46203  58.87948  -11.59624 1.000 47.43236  ?  152 PHE   C CG  1 
ATOM   9811  C CD1 . PHE   G  1 152 ? 51.12781  60.12636  -12.07977 1.000 30.38309  ?  152 PHE   C CD1 1 
ATOM   9812  C CD2 . PHE   G  1 152 ? 50.75054  57.77413  -12.02856 1.000 38.25025  ?  152 PHE   C CD2 1 
ATOM   9813  C CE1 . PHE   G  1 152 ? 50.12118  60.26768  -13.00116 1.000 37.37738  ?  152 PHE   C CE1 1 
ATOM   9814  C CE2 . PHE   G  1 152 ? 49.74598  57.90526  -12.95553 1.000 47.82881  ?  152 PHE   C CE2 1 
ATOM   9815  C CZ  . PHE   G  1 152 ? 49.42961  59.15240  -13.44650 1.000 39.57772  ?  152 PHE   C CZ  1 
ATOM   9816  N N   . LEU   G  1 153 ? 50.74943  57.30734  -8.32601  1.000 39.11643  ?  153 LEU   C N   1 
ATOM   9817  C CA  . LEU   G  1 153 ? 49.49800  56.60949  -8.05154  1.000 41.02341  ?  153 LEU   C CA  1 
ATOM   9818  C C   . LEU   G  1 153 ? 48.79393  57.12113  -6.79825  1.000 40.60876  ?  153 LEU   C C   1 
ATOM   9819  O O   . LEU   G  1 153 ? 47.68419  56.66882  -6.49696  1.000 45.00393  ?  153 LEU   C O   1 
ATOM   9820  C CB  . LEU   G  1 153 ? 49.75747  55.11423  -7.93905  1.000 33.74381  ?  153 LEU   C CB  1 
ATOM   9821  C CG  . LEU   G  1 153 ? 50.35938  54.45637  -9.17396  1.000 46.81174  ?  153 LEU   C CG  1 
ATOM   9822  C CD1 . LEU   G  1 153 ? 50.69003  53.00704  -8.85492  1.000 28.98982  ?  153 LEU   C CD1 1 
ATOM   9823  C CD2 . LEU   G  1 153 ? 49.41510  54.55623  -10.37046 1.000 29.00606  ?  153 LEU   C CD2 1 
ATOM   9824  N N   . SER   G  1 154 ? 49.41719  58.04455  -6.06947  1.000 42.10615  ?  154 SER   C N   1 
ATOM   9825  C CA  . SER   G  1 154 ? 48.81720  58.73223  -4.93732  1.000 39.85719  ?  154 SER   C CA  1 
ATOM   9826  C C   . SER   G  1 154 ? 48.30953  60.11915  -5.30921  1.000 49.93925  ?  154 SER   C C   1 
ATOM   9827  O O   . SER   G  1 154 ? 47.73097  60.80222  -4.45884  1.000 54.18061  ?  154 SER   C O   1 
ATOM   9828  C CB  . SER   G  1 154 ? 49.84058  58.84917  -3.80225  1.000 27.05394  ?  154 SER   C CB  1 
ATOM   9829  O OG  . SER   G  1 154 ? 50.16252  57.56298  -3.31868  1.000 107.68802 ?  154 SER   C OG  1 
ATOM   9830  N N   . SER   G  1 155 ? 48.51478  60.54451  -6.55387  1.000 40.69830  ?  155 SER   C N   1 
ATOM   9831  C CA  . SER   G  1 155 ? 48.26308  61.90022  -7.01698  1.000 41.32217  ?  155 SER   C CA  1 
ATOM   9832  C C   . SER   G  1 155 ? 46.91451  61.98082  -7.71986  1.000 105.92661 ?  155 SER   C C   1 
ATOM   9833  O O   . SER   G  1 155 ? 46.42443  60.98944  -8.27764  1.000 39.41175  ?  155 SER   C O   1 
ATOM   9834  C CB  . SER   G  1 155 ? 49.36618  62.34823  -7.97617  1.000 38.07481  ?  155 SER   C CB  1 
ATOM   9835  O OG  . SER   G  1 155 ? 49.28671  61.66937  -9.22162  1.000 48.12428  ?  155 SER   C OG  1 
ATOM   9836  N N   . LYS   G  1 156 ? 46.32744  63.19069  -7.70803  1.000 50.85024  ?  156 LYS   C N   1 
ATOM   9837  C CA  . LYS   G  1 156 ? 45.00484  63.37316  -8.30478  1.000 67.66847  ?  156 LYS   C CA  1 
ATOM   9838  C C   . LYS   G  1 156 ? 44.99364  62.91400  -9.76146  1.000 41.08939  ?  156 LYS   C C   1 
ATOM   9839  O O   . LYS   G  1 156 ? 43.97687  62.39880  -10.24578 1.000 56.93361  ?  156 LYS   C O   1 
ATOM   9840  C CB  . LYS   G  1 156 ? 44.55429  64.83748  -8.17733  1.000 33.80472  ?  156 LYS   C CB  1 
ATOM   9841  C CG  . LYS   G  1 156 ? 44.61418  65.45186  -6.81030  1.000 99.65520  ?  156 LYS   C CG  1 
ATOM   9842  C CD  . LYS   G  1 156 ? 43.50173  64.90882  -5.95786  1.000 135.34841 ?  156 LYS   C CD  1 
ATOM   9843  C CE  . LYS   G  1 156 ? 43.75828  65.17164  -4.49162  1.000 133.97705 ?  156 LYS   C CE  1 
ATOM   9844  N NZ  . LYS   G  1 156 ? 44.90360  64.39911  -3.92953  1.000 99.10716  ?  156 LYS   C NZ  1 
ATOM   9845  N N   . ASP   G  1 157 ? 46.14166  63.01416  -10.44730 1.000 47.20684  ?  157 ASP   C N   1 
ATOM   9846  C CA  . ASP   G  1 157 ? 46.22200  62.67640  -11.87014 1.000 46.17922  ?  157 ASP   C CA  1 
ATOM   9847  C C   . ASP   G  1 157 ? 46.01465  61.19364  -12.14488 1.000 48.69830  ?  157 ASP   C C   1 
ATOM   9848  O O   . ASP   G  1 157 ? 45.63509  60.83100  -13.26600 1.000 44.58417  ?  157 ASP   C O   1 
ATOM   9849  C CB  . ASP   G  1 157 ? 47.57107  63.11152  -12.44543 1.000 57.53073  ?  157 ASP   C CB  1 
ATOM   9850  C CG  . ASP   G  1 157 ? 47.72277  64.62671  -12.50870 1.000 58.56878  ?  157 ASP   C CG  1 
ATOM   9851  O OD1 . ASP   G  1 157 ? 46.81026  65.30097  -13.03238 1.000 69.16992  ?  157 ASP   C OD1 1 
ATOM   9852  O OD2 . ASP   G  1 157 ? 48.75846  65.13997  -12.02727 1.000 87.87295  -1 157 ASP   C OD2 1 
ATOM   9853  N N   . SER   G  1 158 ? 46.26612  60.32839  -11.16034 1.000 64.67760  ?  158 SER   C N   1 
ATOM   9854  C CA  . SER   G  1 158 ? 46.04342  58.90474  -11.37020 1.000 50.10667  ?  158 SER   C CA  1 
ATOM   9855  C C   . SER   G  1 158 ? 44.56370  58.52908  -11.33547 1.000 52.95160  ?  158 SER   C C   1 
ATOM   9856  O O   . SER   G  1 158 ? 44.25063  57.35237  -11.55016 1.000 48.01049  ?  158 SER   C O   1 
ATOM   9857  C CB  . SER   G  1 158 ? 46.81910  58.08886  -10.32864 1.000 43.56419  ?  158 SER   C CB  1 
ATOM   9858  O OG  . SER   G  1 158 ? 46.26339  58.25133  -9.03182  1.000 43.02270  ?  158 SER   C OG  1 
ATOM   9859  N N   . ARG   G  1 159 ? 43.65003  59.47983  -11.08567 1.000 46.88356  ?  159 ARG   C N   1 
ATOM   9860  C CA  . ARG   G  1 159 ? 42.22112  59.16212  -11.09491 1.000 54.09975  ?  159 ARG   C CA  1 
ATOM   9861  C C   . ARG   G  1 159 ? 41.68629  58.85370  -12.48947 1.000 54.85624  ?  159 ARG   C C   1 
ATOM   9862  O O   . ARG   G  1 159 ? 40.60318  58.27555  -12.60499 1.000 49.27408  ?  159 ARG   C O   1 
ATOM   9863  C CB  . ARG   G  1 159 ? 41.40807  60.31137  -10.50448 1.000 36.73226  ?  159 ARG   C CB  1 
ATOM   9864  C CG  . ARG   G  1 159 ? 41.54739  60.44665  -9.00611  1.000 72.70205  ?  159 ARG   C CG  1 
ATOM   9865  C CD  . ARG   G  1 159 ? 40.92780  61.74193  -8.56481  1.000 56.78530  ?  159 ARG   C CD  1 
ATOM   9866  N NE  . ARG   G  1 159 ? 41.46792  62.84289  -9.34715  1.000 70.64790  ?  159 ARG   C NE  1 
ATOM   9867  C CZ  . ARG   G  1 159 ? 40.92444  64.04853  -9.42121  1.000 61.81529  ?  159 ARG   C CZ  1 
ATOM   9868  N NH1 . ARG   G  1 159 ? 39.80453  64.34407  -8.77811  1.000 54.28712  ?  159 ARG   C NH1 1 
ATOM   9869  N NH2 . ARG   G  1 159 ? 41.51780  64.97845  -10.16175 1.000 51.50769  ?  159 ARG   C NH2 1 
ATOM   9870  N N   . ASN   G  1 160 ? 42.42005  59.20153  -13.54825 1.000 45.86129  ?  160 ASN   C N   1 
ATOM   9871  C CA  . ASN   G  1 160 ? 41.87745  59.08913  -14.89980 1.000 50.20673  ?  160 ASN   C CA  1 
ATOM   9872  C C   . ASN   G  1 160 ? 41.50965  57.66233  -15.30179 1.000 42.63438  ?  160 ASN   C C   1 
ATOM   9873  O O   . ASN   G  1 160 ? 40.78845  57.48337  -16.28696 1.000 72.40619  ?  160 ASN   C O   1 
ATOM   9874  C CB  . ASN   G  1 160 ? 42.87110  59.66646  -15.90166 1.000 48.25627  ?  160 ASN   C CB  1 
ATOM   9875  C CG  . ASN   G  1 160 ? 44.05060  58.76816  -16.11514 1.000 60.43076  ?  160 ASN   C CG  1 
ATOM   9876  O OD1 . ASN   G  1 160 ? 44.86779  58.56982  -15.20978 1.000 73.88673  ?  160 ASN   C OD1 1 
ATOM   9877  N ND2 . ASN   G  1 160 ? 44.14884  58.20247  -17.31040 1.000 64.62419  ?  160 ASN   C ND2 1 
ATOM   9878  N N   . VAL   G  1 161 ? 41.99329  56.64077  -14.59086 1.000 50.11525  ?  161 VAL   C N   1 
ATOM   9879  C CA  . VAL   G  1 161 ? 41.53073  55.27775  -14.86066 1.000 52.92025  ?  161 VAL   C CA  1 
ATOM   9880  C C   . VAL   G  1 161 ? 40.27603  54.93437  -14.07629 1.000 55.62027  ?  161 VAL   C C   1 
ATOM   9881  O O   . VAL   G  1 161 ? 39.69992  53.85293  -14.28336 1.000 38.32424  ?  161 VAL   C O   1 
ATOM   9882  C CB  . VAL   G  1 161 ? 42.60278  54.21803  -14.53257 1.000 46.86665  ?  161 VAL   C CB  1 
ATOM   9883  C CG1 . VAL   G  1 161 ? 43.83312  54.37668  -15.43492 1.000 35.73187  ?  161 VAL   C CG1 1 
ATOM   9884  C CG2 . VAL   G  1 161 ? 42.97047  54.30025  -13.06598 1.000 30.62402  ?  161 VAL   C CG2 1 
ATOM   9885  N N   . LEU   G  1 162 ? 39.84835  55.80754  -13.16679 1.000 40.79652  ?  162 LEU   C N   1 
ATOM   9886  C CA  . LEU   G  1 162 ? 38.66009  55.57614  -12.35179 1.000 51.24236  ?  162 LEU   C CA  1 
ATOM   9887  C C   . LEU   G  1 162 ? 37.43027  56.08018  -13.11086 1.000 70.17277  ?  162 LEU   C C   1 
ATOM   9888  O O   . LEU   G  1 162 ? 36.78640  57.07713  -12.76701 1.000 52.76906  ?  162 LEU   C O   1 
ATOM   9889  C CB  . LEU   G  1 162 ? 38.81694  56.25501  -11.00030 1.000 47.89918  ?  162 LEU   C CB  1 
ATOM   9890  C CG  . LEU   G  1 162 ? 40.02625  55.76793  -10.21372 1.000 36.53864  ?  162 LEU   C CG  1 
ATOM   9891  C CD1 . LEU   G  1 162 ? 40.01268  56.34575  -8.80935  1.000 32.23234  ?  162 LEU   C CD1 1 
ATOM   9892  C CD2 . LEU   G  1 162 ? 40.00670  54.23809  -10.18294 1.000 31.07532  ?  162 LEU   C CD2 1 
ATOM   9893  N N   . VAL   G  1 163 ? 37.12211  55.35495  -14.18393 1.000 52.81880  ?  163 VAL   C N   1 
ATOM   9894  C CA  . VAL   G  1 163 ? 36.10849  55.72772  -15.16485 1.000 49.86389  ?  163 VAL   C CA  1 
ATOM   9895  C C   . VAL   G  1 163 ? 35.48347  54.44305  -15.69633 1.000 70.28932  ?  163 VAL   C C   1 
ATOM   9896  O O   . VAL   G  1 163 ? 35.98751  53.33966  -15.46830 1.000 62.87202  ?  163 VAL   C O   1 
ATOM   9897  C CB  . VAL   G  1 163 ? 36.69679  56.54970  -16.34022 1.000 51.82450  ?  163 VAL   C CB  1 
ATOM   9898  C CG1 . VAL   G  1 163 ? 37.32812  57.87039  -15.84771 1.000 45.40871  ?  163 VAL   C CG1 1 
ATOM   9899  C CG2 . VAL   G  1 163 ? 37.71475  55.71338  -17.12213 1.000 44.93768  ?  163 VAL   C CG2 1 
ATOM   9900  N N   . ALA   G  1 164 ? 34.38264  54.58150  -16.43564 1.000 54.68058  ?  164 ALA   C N   1 
ATOM   9901  C CA  . ALA   G  1 164 ? 33.76750  53.40687  -17.04507 1.000 62.28657  ?  164 ALA   C CA  1 
ATOM   9902  C C   . ALA   G  1 164 ? 34.24038  53.15659  -18.46919 1.000 53.28687  ?  164 ALA   C C   1 
ATOM   9903  O O   . ALA   G  1 164 ? 34.01703  52.05625  -18.99008 1.000 51.20162  ?  164 ALA   C O   1 
ATOM   9904  C CB  . ALA   G  1 164 ? 32.24693  53.53404  -17.03359 1.000 33.14309  ?  164 ALA   C CB  1 
ATOM   9905  N N   . ASP   G  1 165 ? 34.89757  54.14785  -19.08830 1.000 57.05395  ?  165 ASP   C N   1 
ATOM   9906  C CA  . ASP   G  1 165 ? 35.38152  54.06789  -20.46349 1.000 55.38839  ?  165 ASP   C CA  1 
ATOM   9907  C C   . ASP   G  1 165 ? 36.02826  52.71858  -20.75502 1.000 55.24888  ?  165 ASP   C C   1 
ATOM   9908  O O   . ASP   G  1 165 ? 36.83630  52.21275  -19.97478 1.000 90.27090  ?  165 ASP   C O   1 
ATOM   9909  C CB  . ASP   G  1 165 ? 36.39952  55.19008  -20.73637 1.000 62.66439  ?  165 ASP   C CB  1 
ATOM   9910  C CG  . ASP   G  1 165 ? 35.92550  56.56210  -20.26761 1.000 50.61737  ?  165 ASP   C CG  1 
ATOM   9911  O OD1 . ASP   G  1 165 ? 34.77588  56.68977  -19.78961 1.000 96.86833  ?  165 ASP   C OD1 1 
ATOM   9912  O OD2 . ASP   G  1 165 ? 36.72348  57.52026  -20.38366 1.000 99.56642  -1 165 ASP   C OD2 1 
ATOM   9913  N N   . GLN   G  1 166 ? 35.64919  52.12972  -21.87791 1.000 68.13119  ?  166 GLN   C N   1 
ATOM   9914  C CA  . GLN   G  1 166 ? 36.38535  51.00993  -22.43824 1.000 82.59953  ?  166 GLN   C CA  1 
ATOM   9915  C C   . GLN   G  1 166 ? 37.56383  51.59210  -23.21056 1.000 44.85866  ?  166 GLN   C C   1 
ATOM   9916  O O   . GLN   G  1 166 ? 37.39275  52.55006  -23.96835 1.000 118.46019 ?  166 GLN   C O   1 
ATOM   9917  C CB  . GLN   G  1 166 ? 35.47041  50.16159  -23.32969 1.000 42.18510  ?  166 GLN   C CB  1 
ATOM   9918  C CG  . GLN   G  1 166 ? 36.12472  48.98408  -24.00582 1.000 78.70107  ?  166 GLN   C CG  1 
ATOM   9919  C CD  . GLN   G  1 166 ? 35.97803  47.72324  -23.19335 1.000 138.12041 ?  166 GLN   C CD  1 
ATOM   9920  O OE1 . GLN   G  1 166 ? 36.78332  46.79302  -23.31521 1.000 92.88549  ?  166 GLN   C OE1 1 
ATOM   9921  N NE2 . GLN   G  1 166 ? 34.94909  47.67858  -22.35522 1.000 79.28913  ?  166 GLN   C NE2 1 
ATOM   9922  N N   . PHE   G  1 167 ? 38.76316  51.05628  -22.97474 1.000 69.22317  ?  167 PHE   C N   1 
ATOM   9923  C CA  . PHE   G  1 167 ? 39.99531  51.62751  -23.51880 1.000 68.18109  ?  167 PHE   C CA  1 
ATOM   9924  C C   . PHE   G  1 167 ? 40.46729  50.95329  -24.79960 1.000 69.68492  ?  167 PHE   C C   1 
ATOM   9925  O O   . PHE   G  1 167 ? 41.14112  51.59410  -25.61149 1.000 65.66446  ?  167 PHE   C O   1 
ATOM   9926  C CB  . PHE   G  1 167 ? 41.13260  51.53299  -22.49262 1.000 58.28272  ?  167 PHE   C CB  1 
ATOM   9927  C CG  . PHE   G  1 167 ? 40.93400  52.38279  -21.27033 1.000 63.77878  ?  167 PHE   C CG  1 
ATOM   9928  C CD1 . PHE   G  1 167 ? 41.09112  51.85856  -19.99966 1.000 51.99308  ?  167 PHE   C CD1 1 
ATOM   9929  C CD2 . PHE   G  1 167 ? 40.61566  53.70621  -21.38939 1.000 43.10105  ?  167 PHE   C CD2 1 
ATOM   9930  C CE1 . PHE   G  1 167 ? 40.91490  52.65177  -18.87537 1.000 122.71649 ?  167 PHE   C CE1 1 
ATOM   9931  C CE2 . PHE   G  1 167 ? 40.43945  54.50128  -20.27201 1.000 111.53755 ?  167 PHE   C CE2 1 
ATOM   9932  C CZ  . PHE   G  1 167 ? 40.58214  53.98371  -19.02452 1.000 30.81871  ?  167 PHE   C CZ  1 
ATOM   9933  N N   . ASP   G  1 168 ? 40.17315  49.67032  -24.96844 1.000 81.44214  ?  168 ASP   C N   1 
ATOM   9934  C CA  . ASP   G  1 168 ? 40.47888  48.91213  -26.17327 1.000 46.71572  ?  168 ASP   C CA  1 
ATOM   9935  C C   . ASP   G  1 168 ? 39.68761  47.61210  -26.09599 1.000 98.02625  ?  168 ASP   C C   1 
ATOM   9936  O O   . ASP   G  1 168 ? 38.73344  47.51024  -25.28099 1.000 71.55077  ?  168 ASP   C O   1 
ATOM   9937  C CB  . ASP   G  1 168 ? 42.00725  48.73659  -26.34153 1.000 60.79528  ?  168 ASP   C CB  1 
ATOM   9938  C CG  . ASP   G  1 168 ? 42.63653  47.77411  -25.31682 1.000 85.58260  ?  168 ASP   C CG  1 
ATOM   9939  O OD1 . ASP   G  1 168 ? 43.82050  47.97628  -24.93893 1.000 71.41369  ?  168 ASP   C OD1 1 
ATOM   9940  O OD2 . ASP   G  1 168 ? 41.96856  46.79659  -24.91146 1.000 83.33827  -1 168 ASP   C OD2 1 
ATOM   9941  N N   . ASP   G  1 169 ? 40.01933  46.61905  -26.91322 1.000 65.55938  ?  169 ASP   C N   1 
ATOM   9942  C CA  . ASP   G  1 169 ? 39.20340  45.40857  -26.94623 1.000 69.45114  ?  169 ASP   C CA  1 
ATOM   9943  C C   . ASP   G  1 169 ? 39.28533  44.64291  -25.62399 1.000 86.29899  ?  169 ASP   C C   1 
ATOM   9944  O O   . ASP   G  1 169 ? 38.30211  44.01909  -25.20619 1.000 74.12779  ?  169 ASP   C O   1 
ATOM   9945  C CB  . ASP   G  1 169 ? 39.61248  44.51819  -28.12764 1.000 48.03412  ?  169 ASP   C CB  1 
ATOM   9946  N N   . ARG   G  1 170 ? 40.42234  44.71904  -24.92200 1.000 132.46642 ?  170 ARG   C N   1 
ATOM   9947  C CA  . ARG   G  1 170 ? 40.65396  43.88922  -23.74461 1.000 43.36653  ?  170 ARG   C CA  1 
ATOM   9948  C C   . ARG   G  1 170 ? 40.70358  44.65294  -22.41578 1.000 61.65026  ?  170 ARG   C C   1 
ATOM   9949  O O   . ARG   G  1 170 ? 40.63560  44.01181  -21.36070 1.000 52.66684  ?  170 ARG   C O   1 
ATOM   9950  C CB  . ARG   G  1 170 ? 41.95445  43.08844  -23.92649 1.000 49.21955  ?  170 ARG   C CB  1 
ATOM   9951  N N   . HIS   G  1 171 ? 40.79094  45.99153  -22.42538 1.000 62.61742  ?  171 HIS   C N   1 
ATOM   9952  C CA  . HIS   G  1 171 ? 40.99758  46.78693  -21.21514 1.000 65.84774  ?  171 HIS   C CA  1 
ATOM   9953  C C   . HIS   G  1 171 ? 39.88561  47.81122  -21.02833 1.000 32.40015  ?  171 HIS   C C   1 
ATOM   9954  O O   . HIS   G  1 171 ? 39.35523  48.36014  -21.99599 1.000 103.67886 ?  171 HIS   C O   1 
ATOM   9955  C CB  . HIS   G  1 171 ? 42.34261  47.54701  -21.24359 1.000 68.61699  ?  171 HIS   C CB  1 
ATOM   9956  C CG  . HIS   G  1 171 ? 43.52951  46.67845  -21.52167 1.000 63.80060  ?  171 HIS   C CG  1 
ATOM   9957  N ND1 . HIS   G  1 171 ? 43.54234  45.32469  -21.26063 1.000 69.46389  ?  171 HIS   C ND1 1 
ATOM   9958  C CD2 . HIS   G  1 171 ? 44.73927  46.96930  -22.05478 1.000 64.02805  ?  171 HIS   C CD2 1 
ATOM   9959  C CE1 . HIS   G  1 171 ? 44.70924  44.81945  -21.61537 1.000 44.21803  ?  171 HIS   C CE1 1 
ATOM   9960  N NE2 . HIS   G  1 171 ? 45.45499  45.79685  -22.09813 1.000 119.48121 ?  171 HIS   C NE2 1 
ATOM   9961  N N   . CYS   G  1 172 ? 39.56914  48.09682  -19.76511 1.000 71.97980  ?  172 CYS   C N   1 
ATOM   9962  C CA  . CYS   G  1 172 ? 38.57202  49.10437  -19.43027 1.000 41.30583  ?  172 CYS   C CA  1 
ATOM   9963  C C   . CYS   G  1 172 ? 38.93816  49.78219  -18.11699 1.000 42.36441  ?  172 CYS   C C   1 
ATOM   9964  O O   . CYS   G  1 172 ? 39.82970  49.33791  -17.38922 1.000 65.29398  ?  172 CYS   C O   1 
ATOM   9965  C CB  . CYS   G  1 172 ? 37.17924  48.49436  -19.31351 1.000 50.42135  ?  172 CYS   C CB  1 
ATOM   9966  S SG  . CYS   G  1 172 ? 37.06498  47.28971  -17.99394 1.000 58.39554  ?  172 CYS   C SG  1 
ATOM   9967  N N   . GLY   G  1 173 ? 38.21362  50.86053  -17.81490 1.000 62.25774  ?  173 GLY   C N   1 
ATOM   9968  C CA  . GLY   G  1 173 ? 38.38370  51.56365  -16.56011 1.000 46.90987  ?  173 GLY   C CA  1 
ATOM   9969  C C   . GLY   G  1 173 ? 37.79442  50.79575  -15.38714 1.000 61.47797  ?  173 GLY   C C   1 
ATOM   9970  O O   . GLY   G  1 173 ? 37.03353  49.83715  -15.54189 1.000 61.53361  ?  173 GLY   C O   1 
ATOM   9971  N N   . TRP   G  1 174 ? 38.15395  51.24836  -14.17671 1.000 36.77339  ?  174 TRP   C N   1 
ATOM   9972  C CA  . TRP   G  1 174 ? 37.81239  50.52314  -12.95807 1.000 62.35108  ?  174 TRP   C CA  1 
ATOM   9973  C C   . TRP   G  1 174 ? 36.36346  50.72932  -12.53513 1.000 70.93390  ?  174 TRP   C C   1 
ATOM   9974  O O   . TRP   G  1 174 ? 35.86088  49.95398  -11.71853 1.000 55.11514  ?  174 TRP   C O   1 
ATOM   9975  C CB  . TRP   G  1 174 ? 38.76651  50.92580  -11.82372 1.000 40.10544  ?  174 TRP   C CB  1 
ATOM   9976  C CG  . TRP   G  1 174 ? 40.14697  50.40887  -12.06395 1.000 70.15557  ?  174 TRP   C CG  1 
ATOM   9977  C CD1 . TRP   G  1 174 ? 41.21172  51.11112  -12.55095 1.000 48.10678  ?  174 TRP   C CD1 1 
ATOM   9978  C CD2 . TRP   G  1 174 ? 40.60563  49.06284  -11.86967 1.000 56.81935  ?  174 TRP   C CD2 1 
ATOM   9979  N NE1 . TRP   G  1 174 ? 42.30710  50.29049  -12.66173 1.000 50.58747  ?  174 TRP   C NE1 1 
ATOM   9980  C CE2 . TRP   G  1 174 ? 41.96540  49.02873  -12.24861 1.000 42.64685  ?  174 TRP   C CE2 1 
ATOM   9981  C CE3 . TRP   G  1 174 ? 40.00274  47.88843  -11.39714 1.000 44.86466  ?  174 TRP   C CE3 1 
ATOM   9982  C CZ2 . TRP   G  1 174 ? 42.73829  47.86207  -12.17347 1.000 35.05823  ?  174 TRP   C CZ2 1 
ATOM   9983  C CZ3 . TRP   G  1 174 ? 40.76362  46.73085  -11.33359 1.000 46.89998  ?  174 TRP   C CZ3 1 
ATOM   9984  C CH2 . TRP   G  1 174 ? 42.12303  46.72851  -11.71876 1.000 38.05254  ?  174 TRP   C CH2 1 
ATOM   9985  N N   . LEU   G  1 175 ? 35.67798  51.73360  -13.08089 1.000 49.72976  ?  175 LEU   C N   1 
ATOM   9986  C CA  . LEU   G  1 175 ? 34.26389  51.96298  -12.80971 1.000 44.68333  ?  175 LEU   C CA  1 
ATOM   9987  C C   . LEU   G  1 175 ? 33.35230  51.40698  -13.90310 1.000 54.38029  ?  175 LEU   C C   1 
ATOM   9988  O O   . LEU   G  1 175 ? 32.12898  51.53199  -13.79840 1.000 63.22952  ?  175 LEU   C O   1 
ATOM   9989  C CB  . LEU   G  1 175 ? 34.01527  53.45786  -12.61245 1.000 39.68016  ?  175 LEU   C CB  1 
ATOM   9990  C CG  . LEU   G  1 175 ? 34.87195  54.02517  -11.47630 1.000 50.29165  ?  175 LEU   C CG  1 
ATOM   9991  C CD1 . LEU   G  1 175 ? 34.53996  55.48432  -11.14987 1.000 40.83767  ?  175 LEU   C CD1 1 
ATOM   9992  C CD2 . LEU   G  1 175 ? 34.72157  53.14207  -10.24482 1.000 37.78278  ?  175 LEU   C CD2 1 
ATOM   9993  N N   . ASN   G  1 176 ? 33.92740  50.81387  -14.94978 1.000 51.81998  ?  176 ASN   C N   1 
ATOM   9994  C CA  . ASN   G  1 176 ? 33.18069  50.02512  -15.92257 1.000 47.40972  ?  176 ASN   C CA  1 
ATOM   9995  C C   . ASN   G  1 176 ? 32.49081  48.85286  -15.22843 1.000 63.81870  ?  176 ASN   C C   1 
ATOM   9996  O O   . ASN   G  1 176 ? 33.01600  48.29457  -14.25979 1.000 77.70361  ?  176 ASN   C O   1 
ATOM   9997  C CB  . ASN   G  1 176 ? 34.16041  49.52851  -16.97757 1.000 74.33245  ?  176 ASN   C CB  1 
ATOM   9998  C CG  . ASN   G  1 176 ? 33.49302  48.86404  -18.13427 1.000 72.64363  ?  176 ASN   C CG  1 
ATOM   9999  O OD1 . ASN   G  1 176 ? 33.19055  47.66453  -18.09627 1.000 58.83033  ?  176 ASN   C OD1 1 
ATOM   10000 N ND2 . ASN   G  1 176 ? 33.31262  49.62175  -19.20972 1.000 60.17167  ?  176 ASN   C ND2 1 
ATOM   10001 N N   . GLU   G  1 177 ? 31.30013  48.47864  -15.71276 1.000 60.23848  ?  177 GLU   C N   1 
ATOM   10002 C CA  . GLU   G  1 177 ? 30.53052  47.47598  -14.97974 1.000 57.53730  ?  177 GLU   C CA  1 
ATOM   10003 C C   . GLU   G  1 177 ? 31.19632  46.10726  -15.03576 1.000 51.30771  ?  177 GLU   C C   1 
ATOM   10004 O O   . GLU   G  1 177 ? 31.03263  45.30404  -14.11371 1.000 60.55495  ?  177 GLU   C O   1 
ATOM   10005 C CB  . GLU   G  1 177 ? 29.09181  47.39364  -15.49737 1.000 39.28948  ?  177 GLU   C CB  1 
ATOM   10006 N N   . ARG   G  1 178 ? 31.96006  45.81968  -16.09062 1.000 46.66083  ?  178 ARG   C N   1 
ATOM   10007 C CA  . ARG   G  1 178 ? 32.71905  44.56988  -16.12739 1.000 70.22342  ?  178 ARG   C CA  1 
ATOM   10008 C C   . ARG   G  1 178 ? 33.63690  44.45935  -14.91007 1.000 66.39942  ?  178 ARG   C C   1 
ATOM   10009 O O   . ARG   G  1 178 ? 33.70428  43.41008  -14.25516 1.000 64.85915  ?  178 ARG   C O   1 
ATOM   10010 C CB  . ARG   G  1 178 ? 33.52407  44.49032  -17.43425 1.000 35.40733  ?  178 ARG   C CB  1 
ATOM   10011 C CG  . ARG   G  1 178 ? 33.94693  43.05789  -17.92381 1.000 75.87121  ?  178 ARG   C CG  1 
ATOM   10012 C CD  . ARG   G  1 178 ? 34.78335  43.11813  -19.22865 1.000 90.41947  ?  178 ARG   C CD  1 
ATOM   10013 N NE  . ARG   G  1 178 ? 36.21415  43.02119  -18.95155 1.000 118.70298 ?  178 ARG   C NE  1 
ATOM   10014 N N   . ALA   G  1 179 ? 34.32626  45.55634  -14.57449 1.000 55.54693  ?  179 ALA   C N   1 
ATOM   10015 C CA  . ALA   G  1 179 ? 35.26892  45.55796  -13.46464 1.000 54.21269  ?  179 ALA   C CA  1 
ATOM   10016 C C   . ALA   G  1 179 ? 34.53995  45.66174  -12.13027 1.000 43.02709  ?  179 ALA   C C   1 
ATOM   10017 O O   . ALA   G  1 179 ? 34.88021  44.96443  -11.16422 1.000 50.67243  ?  179 ALA   C O   1 
ATOM   10018 C CB  . ALA   G  1 179 ? 36.25519  46.71515  -13.63423 1.000 30.05195  ?  179 ALA   C CB  1 
ATOM   10019 N N   . LEU   G  1 180 ? 33.54973  46.55824  -12.06089 1.000 49.29301  ?  180 LEU   C N   1 
ATOM   10020 C CA  . LEU   G  1 180 ? 32.68388  46.66188  -10.88835 1.000 36.24833  ?  180 LEU   C CA  1 
ATOM   10021 C C   . LEU   G  1 180 ? 32.08748  45.30502  -10.51705 1.000 52.62659  ?  180 LEU   C C   1 
ATOM   10022 O O   . LEU   G  1 180 ? 32.02923  44.93939  -9.33437  1.000 52.74669  ?  180 LEU   C O   1 
ATOM   10023 C CB  . LEU   G  1 180 ? 31.58164  47.68255  -11.16992 1.000 31.58285  ?  180 LEU   C CB  1 
ATOM   10024 C CG  . LEU   G  1 180 ? 31.63549  49.03020  -10.46097 1.000 56.39971  ?  180 LEU   C CG  1 
ATOM   10025 C CD1 . LEU   G  1 180 ? 33.01642  49.58760  -10.44849 1.000 54.03086  ?  180 LEU   C CD1 1 
ATOM   10026 C CD2 . LEU   G  1 180 ? 30.70372  50.00897  -11.12869 1.000 44.07455  ?  180 LEU   C CD2 1 
ATOM   10027 N N   . SER   G  1 181 ? 31.65184  44.53737  -11.51979 1.000 48.29822  ?  181 SER   C N   1 
ATOM   10028 C CA  . SER   G  1 181 ? 31.10062  43.21367  -11.25309 1.000 52.20960  ?  181 SER   C CA  1 
ATOM   10029 C C   . SER   G  1 181 ? 32.16239  42.27781  -10.67644 1.000 39.90834  ?  181 SER   C C   1 
ATOM   10030 O O   . SER   G  1 181 ? 31.91970  41.59471  -9.67173  1.000 51.22141  ?  181 SER   C O   1 
ATOM   10031 C CB  . SER   G  1 181 ? 30.49141  42.64212  -12.53689 1.000 34.58933  ?  181 SER   C CB  1 
ATOM   10032 O OG  . SER   G  1 181 ? 30.29346  41.23902  -12.43949 1.000 102.81002 ?  181 SER   C OG  1 
ATOM   10033 N N   . ALA   G  1 182 ? 33.35015  42.23780  -11.29978 1.000 52.12185  ?  182 ALA   C N   1 
ATOM   10034 C CA  . ALA   G  1 182 ? 34.41037  41.33980  -10.84274 1.000 73.79069  ?  182 ALA   C CA  1 
ATOM   10035 C C   . ALA   G  1 182 ? 34.76913  41.59656  -9.38431  1.000 53.29993  ?  182 ALA   C C   1 
ATOM   10036 O O   . ALA   G  1 182 ? 34.95293  40.64966  -8.60777  1.000 41.12655  ?  182 ALA   C O   1 
ATOM   10037 C CB  . ALA   G  1 182 ? 35.64564  41.48492  -11.73659 1.000 32.31554  ?  182 ALA   C CB  1 
ATOM   10038 N N   . MET   G  1 183 ? 34.83018  42.87338  -8.98746  1.000 37.07538  ?  183 MET   C N   1 
ATOM   10039 C CA  . MET   G  1 183 ? 35.25531  43.26041  -7.64856  1.000 53.20218  ?  183 MET   C CA  1 
ATOM   10040 C C   . MET   G  1 183 ? 34.25243  42.93750  -6.54162  1.000 38.54242  ?  183 MET   C C   1 
ATOM   10041 O O   . MET   G  1 183 ? 34.63690  42.97926  -5.36592  1.000 57.13724  ?  183 MET   C O   1 
ATOM   10042 C CB  . MET   G  1 183 ? 35.58384  44.74739  -7.63886  1.000 37.86200  ?  183 MET   C CB  1 
ATOM   10043 C CG  . MET   G  1 183 ? 36.97721  45.01241  -8.18313  1.000 39.96346  ?  183 MET   C CG  1 
ATOM   10044 S SD  . MET   G  1 183 ? 37.46318  46.73330  -8.10856  1.000 49.17385  ?  183 MET   C SD  1 
ATOM   10045 C CE  . MET   G  1 183 ? 36.62424  47.48598  -9.49212  1.000 45.42755  ?  183 MET   C CE  1 
ATOM   10046 N N   . VAL   G  1 184 ? 32.99822  42.61286  -6.85762  1.000 42.04980  ?  184 VAL   C N   1 
ATOM   10047 C CA  . VAL   G  1 184 ? 32.04845  42.22482  -5.82166  1.000 48.90798  ?  184 VAL   C CA  1 
ATOM   10048 C C   . VAL   G  1 184 ? 31.58426  40.78787  -5.98075  1.000 30.45166  ?  184 VAL   C C   1 
ATOM   10049 O O   . VAL   G  1 184 ? 30.61028  40.38618  -5.35024  1.000 41.37508  ?  184 VAL   C O   1 
ATOM   10050 C CB  . VAL   G  1 184 ? 30.84172  43.17923  -5.75728  1.000 28.32052  ?  184 VAL   C CB  1 
ATOM   10051 C CG1 . VAL   G  1 184 ? 31.30780  44.57786  -5.38229  1.000 33.83213  ?  184 VAL   C CG1 1 
ATOM   10052 C CG2 . VAL   G  1 184 ? 30.08068  43.17425  -7.07317  1.000 29.43070  ?  184 VAL   C CG2 1 
ATOM   10053 N N   . LYS   G  1 185 ? 32.28976  40.00386  -6.79417  1.000 40.90819  ?  185 LYS   C N   1 
ATOM   10054 C CA  . LYS   G  1 185 ? 31.96725  38.59531  -6.99564  1.000 43.78378  ?  185 LYS   C CA  1 
ATOM   10055 C C   . LYS   G  1 185 ? 31.65983  37.85850  -5.68691  1.000 19.50517  ?  185 LYS   C C   1 
ATOM   10056 O O   . LYS   G  1 185 ? 30.69870  37.08069  -5.61118  1.000 77.93333  ?  185 LYS   C O   1 
ATOM   10057 C CB  . LYS   G  1 185 ? 33.13299  37.94946  -7.74158  1.000 32.40318  ?  185 LYS   C CB  1 
ATOM   10058 C CG  . LYS   G  1 185 ? 33.06011  36.46445  -7.87583  1.000 38.60732  ?  185 LYS   C CG  1 
ATOM   10059 C CD  . LYS   G  1 185 ? 34.11322  35.99418  -8.86579  1.000 64.04402  ?  185 LYS   C CD  1 
ATOM   10060 C CE  . LYS   G  1 185 ? 33.78511  34.59897  -9.34055  1.000 64.68847  ?  185 LYS   C CE  1 
ATOM   10061 N NZ  . LYS   G  1 185 ? 34.96065  33.70362  -9.23077  1.000 78.41353  ?  185 LYS   C NZ  1 
ATOM   10062 N N   . HIS   G  1 186 ? 32.44841  38.10237  -4.63827  1.000 49.68849  ?  186 HIS   C N   1 
ATOM   10063 C CA  . HIS   G  1 186 ? 32.31600  37.36404  -3.38677  1.000 31.77770  ?  186 HIS   C CA  1 
ATOM   10064 C C   . HIS   G  1 186 ? 31.54308  38.12907  -2.31972  1.000 51.01616  ?  186 HIS   C C   1 
ATOM   10065 O O   . HIS   G  1 186 ? 31.66047  37.81834  -1.12859  1.000 37.16968  ?  186 HIS   C O   1 
ATOM   10066 C CB  . HIS   G  1 186 ? 33.69080  36.96397  -2.85529  1.000 40.22382  ?  186 HIS   C CB  1 
ATOM   10067 C CG  . HIS   G  1 186 ? 34.46512  36.11359  -3.80313  1.000 66.26740  ?  186 HIS   C CG  1 
ATOM   10068 N ND1 . HIS   G  1 186 ? 34.05137  34.85338  -4.18089  1.000 53.24537  ?  186 HIS   C ND1 1 
ATOM   10069 C CD2 . HIS   G  1 186 ? 35.62726  36.34259  -4.45543  1.000 25.90580  ?  186 HIS   C CD2 1 
ATOM   10070 C CE1 . HIS   G  1 186 ? 34.93266  34.34114  -5.02296  1.000 41.02463  ?  186 HIS   C CE1 1 
ATOM   10071 N NE2 . HIS   G  1 186 ? 35.89851  35.22364  -5.20564  1.000 57.08017  ?  186 HIS   C NE2 1 
ATOM   10072 N N   . TYR   G  1 187 ? 30.74674  39.11503  -2.71090  1.000 43.62628  ?  187 TYR   C N   1 
ATOM   10073 C CA  . TYR   G  1 187 ? 29.99871  39.88561  -1.73019  1.000 51.58567  ?  187 TYR   C CA  1 
ATOM   10074 C C   . TYR   G  1 187 ? 28.50969  39.60581  -1.81102  1.000 87.47310  ?  187 TYR   C C   1 
ATOM   10075 O O   . TYR   G  1 187 ? 27.70061  40.38393  -1.29223  1.000 45.02452  ?  187 TYR   C O   1 
ATOM   10076 C CB  . TYR   G  1 187 ? 30.31016  41.37250  -1.87118  1.000 56.09649  ?  187 TYR   C CB  1 
ATOM   10077 C CG  . TYR   G  1 187 ? 31.71396  41.63663  -1.40261  1.000 40.10380  ?  187 TYR   C CG  1 
ATOM   10078 C CD1 . TYR   G  1 187 ? 31.98467  41.88400  -0.06065  1.000 48.52841  ?  187 TYR   C CD1 1 
ATOM   10079 C CD2 . TYR   G  1 187 ? 32.78214  41.56054  -2.28841  1.000 54.83032  ?  187 TYR   C CD2 1 
ATOM   10080 C CE1 . TYR   G  1 187 ? 33.28109  42.10251  0.38716   1.000 44.44132  ?  187 TYR   C CE1 1 
ATOM   10081 C CE2 . TYR   G  1 187 ? 34.07692  41.76818  -1.86369  1.000 26.98724  ?  187 TYR   C CE2 1 
ATOM   10082 C CZ  . TYR   G  1 187 ? 34.31962  42.04600  -0.52252  1.000 54.36696  ?  187 TYR   C CZ  1 
ATOM   10083 O OH  . TYR   G  1 187 ? 35.60599  42.26316  -0.11163  1.000 47.75925  ?  187 TYR   C OH  1 
ATOM   10084 N N   . ASN   G  1 188 ? 28.13873  38.49323  -2.44148  1.000 35.01782  ?  188 ASN   C N   1 
ATOM   10085 C CA  . ASN   G  1 188 ? 26.83113  37.90270  -2.23644  1.000 84.72671  ?  188 ASN   C CA  1 
ATOM   10086 C C   . ASN   G  1 188 ? 25.72382  38.82927  -2.74507  1.000 33.98662  ?  188 ASN   C C   1 
ATOM   10087 O O   . ASN   G  1 188 ? 24.78431  39.16926  -2.02758  1.000 67.46996  ?  188 ASN   C O   1 
ATOM   10088 C CB  . ASN   G  1 188 ? 26.66875  37.57189  -0.75316  1.000 45.46811  ?  188 ASN   C CB  1 
ATOM   10089 C CG  . ASN   G  1 188 ? 25.45244  36.74765  -0.46843  1.000 84.77482  ?  188 ASN   C CG  1 
ATOM   10090 O OD1 . ASN   G  1 188 ? 24.36620  37.27488  -0.25245  1.000 112.62428 ?  188 ASN   C OD1 1 
ATOM   10091 N ND2 . ASN   G  1 188 ? 25.62564  35.44324  -0.45596  1.000 97.61540  ?  188 ASN   C ND2 1 
ATOM   10092 N N   . GLY   G  1 189 ? 25.86575  39.28539  -3.98862  1.000 66.64113  ?  189 GLY   C N   1 
ATOM   10093 C CA  . GLY   G  1 189 ? 24.85411  40.11763  -4.60500  1.000 33.55791  ?  189 GLY   C CA  1 
ATOM   10094 C C   . GLY   G  1 189 ? 24.89907  41.60222  -4.28078  1.000 37.72317  ?  189 GLY   C C   1 
ATOM   10095 O O   . GLY   G  1 189 ? 24.30891  42.39620  -5.02648  1.000 70.61943  ?  189 GLY   C O   1 
ATOM   10096 N N   . ARG   G  1 190 ? 25.56759  42.01543  -3.19937  1.000 50.12733  ?  190 ARG   C N   1 
ATOM   10097 C CA  . ARG   G  1 190 ? 25.74360  43.44215  -2.94133  1.000 38.28887  ?  190 ARG   C CA  1 
ATOM   10098 C C   . ARG   G  1 190 ? 26.62655  44.10013  -4.01244  1.000 45.40421  ?  190 ARG   C C   1 
ATOM   10099 O O   . ARG   G  1 190 ? 27.51876  43.47845  -4.60790  1.000 56.09079  ?  190 ARG   C O   1 
ATOM   10100 C CB  . ARG   G  1 190 ? 26.34219  43.67170  -1.55488  1.000 45.49868  ?  190 ARG   C CB  1 
ATOM   10101 C CG  . ARG   G  1 190 ? 25.63143  42.94946  -0.42891  1.000 40.15484  ?  190 ARG   C CG  1 
ATOM   10102 C CD  . ARG   G  1 190 ? 24.91572  43.92950  0.49587   1.000 30.66084  ?  190 ARG   C CD  1 
ATOM   10103 N NE  . ARG   G  1 190 ? 25.82310  44.76462  1.27764   1.000 45.31746  ?  190 ARG   C NE  1 
ATOM   10104 C CZ  . ARG   G  1 190 ? 25.49879  45.95355  1.76663   1.000 62.29774  ?  190 ARG   C CZ  1 
ATOM   10105 N NH1 . ARG   G  1 190 ? 24.31403  46.49362  1.53590   1.000 58.55440  ?  190 ARG   C NH1 1 
ATOM   10106 N NH2 . ARG   G  1 190 ? 26.38694  46.62267  2.49570   1.000 47.95199  ?  190 ARG   C NH2 1 
ATOM   10107 N N   . ALA   G  1 191 ? 26.36434  45.37690  -4.25074  1.000 47.13784  ?  191 ALA   C N   1 
ATOM   10108 C CA  . ALA   G  1 191 ? 27.01429  46.12723  -5.31276  1.000 34.93313  ?  191 ALA   C CA  1 
ATOM   10109 C C   . ALA   G  1 191 ? 28.21987  46.88990  -4.77317  1.000 97.97039  ?  191 ALA   C C   1 
ATOM   10110 O O   . ALA   G  1 191 ? 28.35641  47.10929  -3.56386  1.000 36.18837  ?  191 ALA   C O   1 
ATOM   10111 C CB  . ALA   G  1 191 ? 26.03342  47.11236  -5.95144  1.000 47.24969  ?  191 ALA   C CB  1 
ATOM   10112 N N   . PHE   G  1 192 ? 29.07264  47.33618  -5.70354  1.000 33.68120  ?  192 PHE   C N   1 
ATOM   10113 C CA  . PHE   G  1 192 ? 30.34988  47.94621  -5.33864  1.000 37.55393  ?  192 PHE   C CA  1 
ATOM   10114 C C   . PHE   G  1 192 ? 30.17815  49.09395  -4.34323  1.000 61.40017  ?  192 PHE   C C   1 
ATOM   10115 O O   . PHE   G  1 192 ? 30.88511  49.16093  -3.32699  1.000 50.98992  ?  192 PHE   C O   1 
ATOM   10116 C CB  . PHE   G  1 192 ? 31.07123  48.41497  -6.60513  1.000 39.09225  ?  192 PHE   C CB  1 
ATOM   10117 C CG  . PHE   G  1 192 ? 32.44893  48.96536  -6.35550  1.000 46.55246  ?  192 PHE   C CG  1 
ATOM   10118 C CD1 . PHE   G  1 192 ? 32.62368  50.26806  -5.90347  1.000 55.69878  ?  192 PHE   C CD1 1 
ATOM   10119 C CD2 . PHE   G  1 192 ? 33.57234  48.18299  -6.57936  1.000 54.64778  ?  192 PHE   C CD2 1 
ATOM   10120 C CE1 . PHE   G  1 192 ? 33.88675  50.78169  -5.66954  1.000 36.29151  ?  192 PHE   C CE1 1 
ATOM   10121 C CE2 . PHE   G  1 192 ? 34.84634  48.69131  -6.34971  1.000 60.74965  ?  192 PHE   C CE2 1 
ATOM   10122 C CZ  . PHE   G  1 192 ? 34.99909  49.99618  -5.89811  1.000 44.19373  ?  192 PHE   C CZ  1 
ATOM   10123 N N   . ASP   G  1 193 ? 29.24807  50.01142  -4.62169  1.000 57.22908  ?  193 ASP   C N   1 
ATOM   10124 C CA  . ASP   G  1 193 ? 29.05462  51.18753  -3.77489  1.000 37.32624  ?  193 ASP   C CA  1 
ATOM   10125 C C   . ASP   G  1 193 ? 28.33024  50.87373  -2.46367  1.000 63.81965  ?  193 ASP   C C   1 
ATOM   10126 O O   . ASP   G  1 193 ? 28.35938  51.69464  -1.53733  1.000 24.70634  ?  193 ASP   C O   1 
ATOM   10127 C CB  . ASP   G  1 193 ? 28.30103  52.26544  -4.55913  1.000 50.21671  ?  193 ASP   C CB  1 
ATOM   10128 C CG  . ASP   G  1 193 ? 26.92825  51.80275  -5.00285  1.000 93.09800  ?  193 ASP   C CG  1 
ATOM   10129 O OD1 . ASP   G  1 193 ? 26.84816  50.90815  -5.87159  1.000 53.81458  ?  193 ASP   C OD1 1 
ATOM   10130 O OD2 . ASP   G  1 193 ? 25.93051  52.31216  -4.44899  1.000 52.31257  -1 193 ASP   C OD2 1 
ATOM   10131 N N   . GLU   G  1 194 ? 27.68291  49.71371  -2.35639  1.000 31.63349  ?  194 GLU   C N   1 
ATOM   10132 C CA  . GLU   G  1 194 ? 27.21468  49.23891  -1.05750  1.000 58.60467  ?  194 GLU   C CA  1 
ATOM   10133 C C   . GLU   G  1 194 ? 28.37030  48.69203  -0.22764  1.000 62.98163  ?  194 GLU   C C   1 
ATOM   10134 O O   . GLU   G  1 194 ? 28.51377  49.03895  0.95217   1.000 51.47527  ?  194 GLU   C O   1 
ATOM   10135 C CB  . GLU   G  1 194 ? 26.15524  48.15507  -1.24163  1.000 50.36748  ?  194 GLU   C CB  1 
ATOM   10136 C CG  . GLU   G  1 194 ? 24.93131  48.58554  -2.04683  1.000 36.14423  ?  194 GLU   C CG  1 
ATOM   10137 C CD  . GLU   G  1 194 ? 23.94051  47.44030  -2.23513  1.000 93.71831  ?  194 GLU   C CD  1 
ATOM   10138 O OE1 . GLU   G  1 194 ? 24.24458  46.53226  -3.03901  1.000 68.32922  ?  194 GLU   C OE1 1 
ATOM   10139 O OE2 . GLU   G  1 194 ? 22.87709  47.43018  -1.56707  1.000 65.88173  -1 194 GLU   C OE2 1 
ATOM   10140 N N   . VAL   G  1 195 ? 29.21021  47.84937  -0.85072  1.000 57.19505  ?  195 VAL   C N   1 
ATOM   10141 C CA  . VAL   G  1 195 ? 30.29138  47.15372  -0.15080  1.000 24.99498  ?  195 VAL   C CA  1 
ATOM   10142 C C   . VAL   G  1 195 ? 31.39004  48.12710  0.27837   1.000 86.42098  ?  195 VAL   C C   1 
ATOM   10143 O O   . VAL   G  1 195 ? 31.82204  48.13518  1.43774   1.000 38.21049  ?  195 VAL   C O   1 
ATOM   10144 C CB  . VAL   G  1 195 ? 30.86088  46.03972  -1.04364  1.000 60.23030  ?  195 VAL   C CB  1 
ATOM   10145 C CG1 . VAL   G  1 195 ? 32.06016  45.38229  -0.37182  1.000 29.90145  ?  195 VAL   C CG1 1 
ATOM   10146 C CG2 . VAL   G  1 195 ? 29.78048  45.01813  -1.38281  1.000 34.89838  ?  195 VAL   C CG2 1 
ATOM   10147 N N   . PHE   G  1 196 ? 31.87838  48.94144  -0.64640  1.000 30.22939  ?  196 PHE   C N   1 
ATOM   10148 C CA  . PHE   G  1 196 ? 33.00787  49.80948  -0.36829  1.000 62.14965  ?  196 PHE   C CA  1 
ATOM   10149 C C   . PHE   G  1 196 ? 32.53673  51.24626  -0.17820  1.000 42.64422  ?  196 PHE   C C   1 
ATOM   10150 O O   . PHE   G  1 196 ? 31.53196  51.66841  -0.75237  1.000 44.90512  ?  196 PHE   C O   1 
ATOM   10151 C CB  . PHE   G  1 196 ? 34.03688  49.72340  -1.49906  1.000 34.89153  ?  196 PHE   C CB  1 
ATOM   10152 C CG  . PHE   G  1 196 ? 34.49926  48.33133  -1.77511  1.000 52.34763  ?  196 PHE   C CG  1 
ATOM   10153 C CD1 . PHE   G  1 196 ? 35.24334  47.63653  -0.83277  1.000 36.05219  ?  196 PHE   C CD1 1 
ATOM   10154 C CD2 . PHE   G  1 196 ? 34.17362  47.70193  -2.96350  1.000 29.46552  ?  196 PHE   C CD2 1 
ATOM   10155 C CE1 . PHE   G  1 196 ? 35.66136  46.32963  -1.08108  1.000 40.06787  ?  196 PHE   C CE1 1 
ATOM   10156 C CE2 . PHE   G  1 196 ? 34.59575  46.39773  -3.22373  1.000 47.65055  ?  196 PHE   C CE2 1 
ATOM   10157 C CZ  . PHE   G  1 196 ? 35.34309  45.71167  -2.28370  1.000 39.03893  ?  196 PHE   C CZ  1 
ATOM   10158 N N   . LEU   G  1 197 ? 33.27730  51.99090  0.64095   1.000 48.35466  ?  197 LEU   C N   1 
ATOM   10159 C CA  . LEU   G  1 197 ? 32.96870  53.38432  0.95788   1.000 51.18112  ?  197 LEU   C CA  1 
ATOM   10160 C C   . LEU   G  1 197 ? 33.37023  54.26616  -0.21651  1.000 69.77496  ?  197 LEU   C C   1 
ATOM   10161 O O   . LEU   G  1 197 ? 34.55945  54.49278  -0.45766  1.000 45.17397  ?  197 LEU   C O   1 
ATOM   10162 C CB  . LEU   G  1 197 ? 33.71360  53.80277  2.21933   1.000 48.71413  ?  197 LEU   C CB  1 
ATOM   10163 C CG  . LEU   G  1 197 ? 33.35053  55.04841  3.01485   1.000 45.41021  ?  197 LEU   C CG  1 
ATOM   10164 C CD1 . LEU   G  1 197 ? 34.16910  54.96107  4.26496   1.000 53.65509  ?  197 LEU   C CD1 1 
ATOM   10165 C CD2 . LEU   G  1 197 ? 33.70078  56.32920  2.29899   1.000 92.61087  ?  197 LEU   C CD2 1 
ATOM   10166 N N   . CYS   G  1 198 ? 32.38786  54.79280  -0.93056  1.000 61.38119  ?  198 CYS   C N   1 
ATOM   10167 C CA  . CYS   G  1 198 ? 32.66226  55.67245  -2.04761  1.000 60.55522  ?  198 CYS   C CA  1 
ATOM   10168 C C   . CYS   G  1 198 ? 31.43519  56.54614  -2.25333  1.000 64.18601  ?  198 CYS   C C   1 
ATOM   10169 O O   . CYS   G  1 198 ? 30.52106  56.56719  -1.42205  1.000 71.28290  ?  198 CYS   C O   1 
ATOM   10170 C CB  . CYS   G  1 198 ? 33.00576  54.85530  -3.29699  1.000 54.00939  ?  198 CYS   C CB  1 
ATOM   10171 S SG  . CYS   G  1 198 ? 31.71191  53.62373  -3.70210  1.000 62.74561  ?  198 CYS   C SG  1 
ATOM   10172 N N   . ASP   G  1 199 ? 31.41164  57.25304  -3.38027  1.000 54.63302  ?  199 ASP   C N   1 
ATOM   10173 C CA  . ASP   G  1 199 ? 30.27557  58.06767  -3.80004  1.000 43.10723  ?  199 ASP   C CA  1 
ATOM   10174 C C   . ASP   G  1 199 ? 29.97097  57.72608  -5.25690  1.000 77.72346  ?  199 ASP   C C   1 
ATOM   10175 O O   . ASP   G  1 199 ? 30.68079  58.18308  -6.16109  1.000 42.86264  ?  199 ASP   C O   1 
ATOM   10176 C CB  . ASP   G  1 199 ? 30.59671  59.55282  -3.62605  1.000 44.91206  ?  199 ASP   C CB  1 
ATOM   10177 C CG  . ASP   G  1 199 ? 29.44504  60.46848  -4.02764  1.000 146.26084 ?  199 ASP   C CG  1 
ATOM   10178 O OD1 . ASP   G  1 199 ? 28.42440  59.99128  -4.59402  1.000 47.74822  ?  199 ASP   C OD1 1 
ATOM   10179 O OD2 . ASP   G  1 199 ? 29.58695  61.68403  -3.75694  1.000 55.44824  -1 199 ASP   C OD2 1 
ATOM   10180 N N   . LYS   G  1 200 ? 28.91674  56.92941  -5.49523  1.000 50.95803  ?  200 LYS   C N   1 
ATOM   10181 C CA  . LYS   G  1 200 ? 28.63812  56.47984  -6.86068  1.000 76.41881  ?  200 LYS   C CA  1 
ATOM   10182 C C   . LYS   G  1 200 ? 28.21589  57.61798  -7.77924  1.000 73.16309  ?  200 LYS   C C   1 
ATOM   10183 O O   . LYS   G  1 200 ? 28.22767  57.43489  -8.99907  1.000 64.87987  ?  200 LYS   C O   1 
ATOM   10184 C CB  . LYS   G  1 200 ? 27.56381  55.38345  -6.87611  1.000 50.77334  ?  200 LYS   C CB  1 
ATOM   10185 C CG  . LYS   G  1 200 ? 26.14624  55.87428  -6.65725  1.000 73.56286  ?  200 LYS   C CG  1 
ATOM   10186 C CD  . LYS   G  1 200 ? 25.13664  54.72146  -6.63085  1.000 94.07281  ?  200 LYS   C CD  1 
ATOM   10187 C CE  . LYS   G  1 200 ? 24.97948  54.03292  -7.99009  1.000 77.35117  ?  200 LYS   C CE  1 
ATOM   10188 N NZ  . LYS   G  1 200 ? 23.72574  53.20501  -8.04301  1.000 71.93096  ?  200 LYS   C NZ  1 
ATOM   10189 N N   . ASN   G  1 201 ? 27.87276  58.78305  -7.23139  1.000 55.41647  ?  201 ASN   C N   1 
ATOM   10190 C CA  . ASN   G  1 201 ? 27.45525  59.93555  -8.01498  1.000 78.57817  ?  201 ASN   C CA  1 
ATOM   10191 C C   . ASN   G  1 201 ? 28.57324  60.93196  -8.24306  1.000 54.32313  ?  201 ASN   C C   1 
ATOM   10192 O O   . ASN   G  1 201 ? 28.39010  61.89099  -8.99731  1.000 86.36377  ?  201 ASN   C O   1 
ATOM   10193 C CB  . ASN   G  1 201 ? 26.28615  60.62507  -7.32342  1.000 52.57603  ?  201 ASN   C CB  1 
ATOM   10194 C CG  . ASN   G  1 201 ? 25.12268  59.70077  -7.15091  1.000 90.03979  ?  201 ASN   C CG  1 
ATOM   10195 O OD1 . ASN   G  1 201 ? 24.77827  58.94101  -8.07233  1.000 43.27236  ?  201 ASN   C OD1 1 
ATOM   10196 N ND2 . ASN   G  1 201 ? 24.53110  59.71185  -5.96165  1.000 58.15429  ?  201 ASN   C ND2 1 
ATOM   10197 N N   . ALA   G  1 202 ? 29.65750  60.74170  -7.64727  1.000 101.59509 ?  202 ALA   C N   1 
ATOM   10198 C CA  . ALA   G  1 202 ? 30.76483  61.65902  -7.81972  1.000 54.09075  ?  202 ALA   C CA  1 
ATOM   10199 C C   . ALA   G  1 202 ? 31.65023  61.20468  -8.97298  1.000 47.32162  ?  202 ALA   C C   1 
ATOM   10200 O O   . ALA   G  1 202 ? 31.64362  60.02414  -9.34692  1.000 59.07576  ?  202 ALA   C O   1 
ATOM   10201 C CB  . ALA   G  1 202 ? 31.58344  61.74390  -6.54000  1.000 31.45909  ?  202 ALA   C CB  1 
ATOM   10202 N N   . PRO   G  1 203 ? 32.38143  62.12730  -9.59107  1.000 79.15910  ?  203 PRO   C N   1 
ATOM   10203 C CA  . PRO   G  1 203 ? 33.41296  61.70832  -10.54643 1.000 73.97935  ?  203 PRO   C CA  1 
ATOM   10204 C C   . PRO   G  1 203 ? 34.48507  60.90176  -9.82897  1.000 63.80438  ?  203 PRO   C C   1 
ATOM   10205 O O   . PRO   G  1 203 ? 34.87286  61.21139  -8.69231  1.000 44.06120  ?  203 PRO   C O   1 
ATOM   10206 C CB  . PRO   G  1 203 ? 33.96140  63.03000  -11.10483 1.000 51.26224  ?  203 PRO   C CB  1 
ATOM   10207 C CG  . PRO   G  1 203 ? 33.53463  64.09182  -10.12189 1.000 41.97075  ?  203 PRO   C CG  1 
ATOM   10208 C CD  . PRO   G  1 203 ? 32.26801  63.59214  -9.47431  1.000 30.10407  ?  203 PRO   C CD  1 
ATOM   10209 N N   . TYR   G  1 204 ? 34.93269  59.83368  -10.49682 1.000 49.71603  ?  204 TYR   C N   1 
ATOM   10210 C CA  . TYR   G  1 204 ? 35.90889  58.89262  -9.95697  1.000 60.78566  ?  204 TYR   C CA  1 
ATOM   10211 C C   . TYR   G  1 204 ? 35.39571  58.18278  -8.71974  1.000 54.49453  ?  204 TYR   C C   1 
ATOM   10212 O O   . TYR   G  1 204 ? 36.18869  57.79348  -7.85959  1.000 58.84784  ?  204 TYR   C O   1 
ATOM   10213 C CB  . TYR   G  1 204 ? 37.23455  59.59364  -9.63628  1.000 48.19197  ?  204 TYR   C CB  1 
ATOM   10214 C CG  . TYR   G  1 204 ? 37.64619  60.55834  -10.71980 1.000 52.46755  ?  204 TYR   C CG  1 
ATOM   10215 C CD1 . TYR   G  1 204 ? 37.83761  60.10919  -12.02909 1.000 47.22898  ?  204 TYR   C CD1 1 
ATOM   10216 C CD2 . TYR   G  1 204 ? 37.83417  61.91484  -10.44613 1.000 43.41642  ?  204 TYR   C CD2 1 
ATOM   10217 C CE1 . TYR   G  1 204 ? 38.20353  60.97893  -13.04510 1.000 29.94435  ?  204 TYR   C CE1 1 
ATOM   10218 C CE2 . TYR   G  1 204 ? 38.20599  62.79696  -11.45183 1.000 40.45929  ?  204 TYR   C CE2 1 
ATOM   10219 C CZ  . TYR   G  1 204 ? 38.37896  62.31909  -12.75116 1.000 53.67255  ?  204 TYR   C CZ  1 
ATOM   10220 O OH  . TYR   G  1 204 ? 38.75084  63.16550  -13.76783 1.000 55.68247  ?  204 TYR   C OH  1 
ATOM   10221 N N   . TYR   G  1 205 ? 34.07675  58.04869  -8.59303  1.000 40.77048  ?  205 TYR   C N   1 
ATOM   10222 C CA  . TYR   G  1 205 ? 33.44413  57.47251  -7.41061  1.000 38.73048  ?  205 TYR   C CA  1 
ATOM   10223 C C   . TYR   G  1 205 ? 33.93671  58.11820  -6.10909  1.000 46.15352  ?  205 TYR   C C   1 
ATOM   10224 O O   . TYR   G  1 205 ? 33.84960  57.51458  -5.02943  1.000 44.13701  ?  205 TYR   C O   1 
ATOM   10225 C CB  . TYR   G  1 205 ? 33.65111  55.95949  -7.35840  1.000 45.84894  ?  205 TYR   C CB  1 
ATOM   10226 C CG  . TYR   G  1 205 ? 32.51314  55.14197  -7.90167  1.000 59.55569  ?  205 TYR   C CG  1 
ATOM   10227 C CD1 . TYR   G  1 205 ? 31.73940  55.58918  -8.96167  1.000 51.80671  ?  205 TYR   C CD1 1 
ATOM   10228 C CD2 . TYR   G  1 205 ? 32.20196  53.91064  -7.33707  1.000 47.05926  ?  205 TYR   C CD2 1 
ATOM   10229 C CE1 . TYR   G  1 205 ? 30.68035  54.80516  -9.45770  1.000 36.68435  ?  205 TYR   C CE1 1 
ATOM   10230 C CE2 . TYR   G  1 205 ? 31.15853  53.13155  -7.81926  1.000 60.68476  ?  205 TYR   C CE2 1 
ATOM   10231 C CZ  . TYR   G  1 205 ? 30.40311  53.58143  -8.87579  1.000 80.57859  ?  205 TYR   C CZ  1 
ATOM   10232 O OH  . TYR   G  1 205 ? 29.38008  52.79224  -9.33173  1.000 51.16638  ?  205 TYR   C OH  1 
ATOM   10233 N N   . GLY   G  1 206 ? 34.46313  59.33771  -6.18026  1.000 41.83410  ?  206 GLY   C N   1 
ATOM   10234 C CA  . GLY   G  1 206 ? 34.89958  60.03755  -4.99553  1.000 40.72151  ?  206 GLY   C CA  1 
ATOM   10235 C C   . GLY   G  1 206 ? 36.31939  59.75320  -4.55459  1.000 54.51044  ?  206 GLY   C C   1 
ATOM   10236 O O   . GLY   G  1 206 ? 36.81106  60.42987  -3.64421  1.000 46.52652  ?  206 GLY   C O   1 
ATOM   10237 N N   . PHE   G  1 207 ? 36.99646  58.78200  -5.15894  1.000 42.43457  ?  207 PHE   C N   1 
ATOM   10238 C CA  . PHE   G  1 207 ? 38.38000  58.50991  -4.79463  1.000 54.49386  ?  207 PHE   C CA  1 
ATOM   10239 C C   . PHE   G  1 207 ? 39.28546  59.61891  -5.31725  1.000 49.95788  ?  207 PHE   C C   1 
ATOM   10240 O O   . PHE   G  1 207 ? 39.07651  60.13820  -6.41684  1.000 59.99958  ?  207 PHE   C O   1 
ATOM   10241 C CB  . PHE   G  1 207 ? 38.81387  57.15958  -5.35958  1.000 41.82959  ?  207 PHE   C CB  1 
ATOM   10242 C CG  . PHE   G  1 207 ? 38.00497  55.99834  -4.85748  1.000 57.47766  ?  207 PHE   C CG  1 
ATOM   10243 C CD1 . PHE   G  1 207 ? 38.19146  55.51722  -3.56895  1.000 31.25532  ?  207 PHE   C CD1 1 
ATOM   10244 C CD2 . PHE   G  1 207 ? 37.07367  55.36818  -5.67971  1.000 35.63171  ?  207 PHE   C CD2 1 
ATOM   10245 C CE1 . PHE   G  1 207 ? 37.45883  54.43332  -3.10576  1.000 51.56199  ?  207 PHE   C CE1 1 
ATOM   10246 C CE2 . PHE   G  1 207 ? 36.33533  54.27600  -5.22264  1.000 39.28730  ?  207 PHE   C CE2 1 
ATOM   10247 C CZ  . PHE   G  1 207 ? 36.52912  53.81189  -3.93528  1.000 56.24421  ?  207 PHE   C CZ  1 
ATOM   10248 N N   . ASN   G  1 208 ? 40.29694  59.99067  -4.52699  1.000 44.46079  ?  208 ASN   C N   1 
ATOM   10249 C CA  . ASN   G  1 208 ? 41.17585  61.09501  -4.90495  1.000 66.97416  ?  208 ASN   C CA  1 
ATOM   10250 C C   . ASN   G  1 208 ? 42.45932  60.66163  -5.60399  1.000 36.59864  ?  208 ASN   C C   1 
ATOM   10251 O O   . ASN   G  1 208 ? 43.28881  61.52365  -5.92820  1.000 94.77305  ?  208 ASN   C O   1 
ATOM   10252 C CB  . ASN   G  1 208 ? 41.52627  61.96342  -3.68701  1.000 37.04866  ?  208 ASN   C CB  1 
ATOM   10253 C CG  . ASN   G  1 208 ? 41.85114  61.16377  -2.46421  1.000 93.51785  ?  208 ASN   C CG  1 
ATOM   10254 O OD1 . ASN   G  1 208 ? 42.81870  60.39104  -2.43991  1.000 148.56702 ?  208 ASN   C OD1 1 
ATOM   10255 N ND2 . ASN   G  1 208 ? 41.06263  61.36836  -1.41354  1.000 70.49339  ?  208 ASN   C ND2 1 
ATOM   10256 N N   . SER   G  1 209 ? 42.63041  59.36831  -5.86986  1.000 53.47297  ?  209 SER   C N   1 
ATOM   10257 C CA  . SER   G  1 209 ? 43.79933  58.83524  -6.56576  1.000 36.93701  ?  209 SER   C CA  1 
ATOM   10258 C C   . SER   G  1 209 ? 43.55170  57.36080  -6.79946  1.000 59.08438  ?  209 SER   C C   1 
ATOM   10259 O O   . SER   G  1 209 ? 42.61223  56.77670  -6.24976  1.000 34.31730  ?  209 SER   C O   1 
ATOM   10260 C CB  . SER   G  1 209 ? 45.09841  58.98937  -5.77422  1.000 47.92957  ?  209 SER   C CB  1 
ATOM   10261 O OG  . SER   G  1 209 ? 45.07159  58.12658  -4.64921  1.000 27.25346  ?  209 SER   C OG  1 
ATOM   10262 N N   . TYR   G  1 210 ? 44.43626  56.75281  -7.59199  1.000 45.03885  ?  210 TYR   C N   1 
ATOM   10263 C CA  . TYR   G  1 210 ? 44.31074  55.32061  -7.81823  1.000 33.15217  ?  210 TYR   C CA  1 
ATOM   10264 C C   . TYR   G  1 210 ? 44.56448  54.54216  -6.53192  1.000 46.16051  ?  210 TYR   C C   1 
ATOM   10265 O O   . TYR   G  1 210 ? 43.80784  53.62320  -6.19359  1.000 39.10680  ?  210 TYR   C O   1 
ATOM   10266 C CB  . TYR   G  1 210 ? 45.26178  54.87355  -8.92751  1.000 22.55687  ?  210 TYR   C CB  1 
ATOM   10267 C CG  . TYR   G  1 210 ? 45.28072  53.38010  -9.08180  1.000 55.63015  ?  210 TYR   C CG  1 
ATOM   10268 C CD1 . TYR   G  1 210 ? 44.25125  52.72629  -9.74553  1.000 32.65273  ?  210 TYR   C CD1 1 
ATOM   10269 C CD2 . TYR   G  1 210 ? 46.30213  52.61643  -8.53179  1.000 48.06629  ?  210 TYR   C CD2 1 
ATOM   10270 C CE1 . TYR   G  1 210 ? 44.23288  51.34609  -9.87421  1.000 36.27552  ?  210 TYR   C CE1 1 
ATOM   10271 C CE2 . TYR   G  1 210 ? 46.29828  51.23648  -8.65419  1.000 49.83596  ?  210 TYR   C CE2 1 
ATOM   10272 C CZ  . TYR   G  1 210 ? 45.26061  50.61245  -9.32916  1.000 58.83115  ?  210 TYR   C CZ  1 
ATOM   10273 O OH  . TYR   G  1 210 ? 45.24975  49.25505  -9.46298  1.000 40.60730  ?  210 TYR   C OH  1 
ATOM   10274 N N   . ASP   G  1 211 ? 45.61514  54.91200  -5.79703  1.000 38.30931  ?  211 ASP   C N   1 
ATOM   10275 C CA  . ASP   G  1 211 ? 45.92207  54.24454  -4.53677  1.000 33.03308  ?  211 ASP   C CA  1 
ATOM   10276 C C   . ASP   G  1 211 ? 44.74877  54.31512  -3.57391  1.000 54.42178  ?  211 ASP   C C   1 
ATOM   10277 O O   . ASP   G  1 211 ? 44.48013  53.35329  -2.83593  1.000 35.30407  ?  211 ASP   C O   1 
ATOM   10278 C CB  . ASP   G  1 211 ? 47.16367  54.86583  -3.89062  1.000 36.17269  ?  211 ASP   C CB  1 
ATOM   10279 C CG  . ASP   G  1 211 ? 47.53716  54.17897  -2.58813  1.000 36.71599  ?  211 ASP   C CG  1 
ATOM   10280 O OD1 . ASP   G  1 211 ? 47.93680  52.98668  -2.63716  1.000 41.46733  ?  211 ASP   C OD1 1 
ATOM   10281 O OD2 . ASP   G  1 211 ? 47.42206  54.82216  -1.51832  1.000 59.38252  -1 211 ASP   C OD2 1 
ATOM   10282 N N   . ASP   G  1 212 ? 44.05680  55.46018  -3.54956  1.000 34.41726  ?  212 ASP   C N   1 
ATOM   10283 C CA  . ASP   G  1 212 ? 42.85510  55.58836  -2.72983  1.000 43.93514  ?  212 ASP   C CA  1 
ATOM   10284 C C   . ASP   G  1 212 ? 41.81630  54.53423  -3.11615  1.000 36.19891  ?  212 ASP   C C   1 
ATOM   10285 O O   . ASP   G  1 212 ? 41.20899  53.88981  -2.24843  1.000 36.88585  ?  212 ASP   C O   1 
ATOM   10286 C CB  . ASP   G  1 212 ? 42.29678  57.00652  -2.87688  1.000 45.41371  ?  212 ASP   C CB  1 
ATOM   10287 C CG  . ASP   G  1 212 ? 41.17633  57.31350  -1.89538  1.000 53.53430  ?  212 ASP   C CG  1 
ATOM   10288 O OD1 . ASP   G  1 212 ? 41.13126  56.67531  -0.82108  1.000 68.53457  ?  212 ASP   C OD1 1 
ATOM   10289 O OD2 . ASP   G  1 212 ? 40.33149  58.18550  -2.21930  1.000 54.40697  -1 212 ASP   C OD2 1 
ATOM   10290 N N   . PHE   G  1 213 ? 41.62300  54.32421  -4.41672  1.000 29.83791  ?  213 PHE   C N   1 
ATOM   10291 C CA  . PHE   G  1 213 ? 40.68829  53.30353  -4.87690  1.000 27.10813  ?  213 PHE   C CA  1 
ATOM   10292 C C   . PHE   G  1 213 ? 41.19452  51.90254  -4.54924  1.000 64.01708  ?  213 PHE   C C   1 
ATOM   10293 O O   . PHE   G  1 213 ? 40.42146  51.03650  -4.10270  1.000 38.51427  ?  213 PHE   C O   1 
ATOM   10294 C CB  . PHE   G  1 213 ? 40.46705  53.46193  -6.38470  1.000 33.78635  ?  213 PHE   C CB  1 
ATOM   10295 C CG  . PHE   G  1 213 ? 39.90186  52.25631  -7.02811  1.000 46.48592  ?  213 PHE   C CG  1 
ATOM   10296 C CD1 . PHE   G  1 213 ? 38.53276  52.00270  -6.97090  1.000 49.96773  ?  213 PHE   C CD1 1 
ATOM   10297 C CD2 . PHE   G  1 213 ? 40.73111  51.35891  -7.68333  1.000 34.69169  ?  213 PHE   C CD2 1 
ATOM   10298 C CE1 . PHE   G  1 213 ? 37.99697  50.86916  -7.56856  1.000 59.44289  ?  213 PHE   C CE1 1 
ATOM   10299 C CE2 . PHE   G  1 213 ? 40.20444  50.22765  -8.28289  1.000 62.38402  ?  213 PHE   C CE2 1 
ATOM   10300 C CZ  . PHE   G  1 213 ? 38.83411  49.98088  -8.22408  1.000 51.83682  ?  213 PHE   C CZ  1 
ATOM   10301 N N   . PHE   G  1 214 ? 42.49031  51.66814  -4.79107  1.000 34.29473  ?  214 PHE   C N   1 
ATOM   10302 C CA  . PHE   G  1 214 ? 43.11353  50.37632  -4.52324  1.000 32.58747  ?  214 PHE   C CA  1 
ATOM   10303 C C   . PHE   G  1 214 ? 42.95096  49.96940  -3.05717  1.000 31.39314  ?  214 PHE   C C   1 
ATOM   10304 O O   . PHE   G  1 214 ? 42.71410  48.79050  -2.74995  1.000 59.01607  ?  214 PHE   C O   1 
ATOM   10305 C CB  . PHE   G  1 214 ? 44.58957  50.45935  -4.92216  1.000 41.32164  ?  214 PHE   C CB  1 
ATOM   10306 C CG  . PHE   G  1 214 ? 45.34246  49.16727  -4.79035  1.000 39.53236  ?  214 PHE   C CG  1 
ATOM   10307 C CD1 . PHE   G  1 214 ? 45.21382  48.17585  -5.74909  1.000 38.07105  ?  214 PHE   C CD1 1 
ATOM   10308 C CD2 . PHE   G  1 214 ? 46.20660  48.95539  -3.72438  1.000 46.96534  ?  214 PHE   C CD2 1 
ATOM   10309 C CE1 . PHE   G  1 214 ? 45.90276  46.98369  -5.64118  1.000 34.51597  ?  214 PHE   C CE1 1 
ATOM   10310 C CE2 . PHE   G  1 214 ? 46.91465  47.76106  -3.61139  1.000 46.35652  ?  214 PHE   C CE2 1 
ATOM   10311 C CZ  . PHE   G  1 214 ? 46.76695  46.77236  -4.57663  1.000 40.27673  ?  214 PHE   C CZ  1 
ATOM   10312 N N   . ASN   G  1 215 ? 43.04611  50.93482  -2.14073  1.000 28.69527  ?  215 ASN   C N   1 
ATOM   10313 C CA  . ASN   G  1 215 ? 42.90912  50.68635  -0.70788  1.000 36.35398  ?  215 ASN   C CA  1 
ATOM   10314 C C   . ASN   G  1 215 ? 41.57478  51.18189  -0.15516  1.000 46.13654  ?  215 ASN   C C   1 
ATOM   10315 O O   . ASN   G  1 215 ? 41.49645  51.67367  0.97457   1.000 39.88021  ?  215 ASN   C O   1 
ATOM   10316 C CB  . ASN   G  1 215 ? 44.07424  51.30590  0.05336   1.000 36.20126  ?  215 ASN   C CB  1 
ATOM   10317 C CG  . ASN   G  1 215 ? 45.34454  50.50075  -0.11647  1.000 59.32317  ?  215 ASN   C CG  1 
ATOM   10318 O OD1 . ASN   G  1 215 ? 45.33659  49.26712  -0.01914  1.000 37.98360  ?  215 ASN   C OD1 1 
ATOM   10319 N ND2 . ASN   G  1 215 ? 46.43595  51.18601  -0.40629  1.000 34.71147  ?  215 ASN   C ND2 1 
ATOM   10320 N N   . ARG   G  1 216 ? 40.51293  51.04226  -0.95408  1.000 24.88534  ?  216 ARG   C N   1 
ATOM   10321 C CA  . ARG   G  1 216 ? 39.17723  51.43308  -0.53656  1.000 33.76603  ?  216 ARG   C CA  1 
ATOM   10322 C C   . ARG   G  1 216 ? 38.76480  50.68556  0.73187   1.000 56.80938  ?  216 ARG   C C   1 
ATOM   10323 O O   . ARG   G  1 216 ? 39.08636  49.50758  0.91495   1.000 32.99378  ?  216 ARG   C O   1 
ATOM   10324 C CB  . ARG   G  1 216 ? 38.19838  51.14837  -1.67528  1.000 30.04890  ?  216 ARG   C CB  1 
ATOM   10325 C CG  . ARG   G  1 216 ? 38.11766  49.68561  -2.04918  1.000 29.34021  ?  216 ARG   C CG  1 
ATOM   10326 C CD  . ARG   G  1 216 ? 37.36978  49.48140  -3.34233  1.000 39.65422  ?  216 ARG   C CD  1 
ATOM   10327 N NE  . ARG   G  1 216 ? 37.47903  48.10309  -3.81189  1.000 28.59454  ?  216 ARG   C NE  1 
ATOM   10328 C CZ  . ARG   G  1 216 ? 38.52661  47.63187  -4.47577  1.000 53.37366  ?  216 ARG   C CZ  1 
ATOM   10329 N NH1 . ARG   G  1 216 ? 39.55831  48.40791  -4.77912  1.000 32.18680  ?  216 ARG   C NH1 1 
ATOM   10330 N NH2 . ARG   G  1 216 ? 38.54495  46.35207  -4.83621  1.000 36.67116  ?  216 ARG   C NH2 1 
ATOM   10331 N N   . ARG   G  1 217 ? 38.03056  51.37444  1.59771   1.000 32.01105  ?  217 ARG   C N   1 
ATOM   10332 C CA  . ARG   G  1 217 ? 37.56795  50.80040  2.85197   1.000 47.78423  ?  217 ARG   C CA  1 
ATOM   10333 C C   . ARG   G  1 217 ? 36.17875  50.17308  2.71333   1.000 33.57109  ?  217 ARG   C C   1 
ATOM   10334 O O   . ARG   G  1 217 ? 35.41293  50.47280  1.79876   1.000 50.57575  ?  217 ARG   C O   1 
ATOM   10335 C CB  . ARG   G  1 217 ? 37.52965  51.85897  3.93486   1.000 37.92547  ?  217 ARG   C CB  1 
ATOM   10336 C CG  . ARG   G  1 217 ? 38.84254  52.49857  4.18135   1.000 18.44667  ?  217 ARG   C CG  1 
ATOM   10337 C CD  . ARG   G  1 217 ? 38.66685  53.54820  5.25815   1.000 34.51458  ?  217 ARG   C CD  1 
ATOM   10338 N NE  . ARG   G  1 217 ? 39.89122  54.31065  5.45208   1.000 92.47928  ?  217 ARG   C NE  1 
ATOM   10339 C CZ  . ARG   G  1 217 ? 40.69037  54.22276  6.50786   1.000 118.64994 ?  217 ARG   C CZ  1 
ATOM   10340 N NH1 . ARG   G  1 217 ? 40.38195  53.46540  7.55288   1.000 93.68570  ?  217 ARG   C NH1 1 
ATOM   10341 N NH2 . ARG   G  1 217 ? 41.83290  54.90861  6.51102   1.000 112.56131 ?  217 ARG   C NH2 1 
ATOM   10342 N N   . PHE   G  1 218 ? 35.86561  49.26047  3.63626   1.000 42.81474  ?  218 PHE   C N   1 
ATOM   10343 C CA  . PHE   G  1 218 ? 34.51057  48.71167  3.61718   1.000 31.68257  ?  218 PHE   C CA  1 
ATOM   10344 C C   . PHE   G  1 218 ? 33.52115  49.74570  4.15014   1.000 62.13287  ?  218 PHE   C C   1 
ATOM   10345 O O   . PHE   G  1 218 ? 33.78773  50.41181  5.15383   1.000 33.89365  ?  218 PHE   C O   1 
ATOM   10346 C CB  . PHE   G  1 218 ? 34.41981  47.44437  4.45909   1.000 22.53349  ?  218 PHE   C CB  1 
ATOM   10347 C CG  . PHE   G  1 218 ? 35.08952  46.25315  3.84617   1.000 42.18931  ?  218 PHE   C CG  1 
ATOM   10348 C CD1 . PHE   G  1 218 ? 34.65172  45.74060  2.62161   1.000 24.20141  ?  218 PHE   C CD1 1 
ATOM   10349 C CD2 . PHE   G  1 218 ? 36.15108  45.62532  4.50517   1.000 32.86208  ?  218 PHE   C CD2 1 
ATOM   10350 C CE1 . PHE   G  1 218 ? 35.26314  44.62561  2.05421   1.000 49.45126  ?  218 PHE   C CE1 1 
ATOM   10351 C CE2 . PHE   G  1 218 ? 36.77056  44.51749  3.94862   1.000 32.12927  ?  218 PHE   C CE2 1 
ATOM   10352 C CZ  . PHE   G  1 218 ? 36.32573  44.01511  2.71704   1.000 25.38487  ?  218 PHE   C CZ  1 
ATOM   10353 N N   . ARG   G  1 219 ? 32.36804  49.87456  3.49047   1.000 46.38817  ?  219 ARG   C N   1 
ATOM   10354 C CA  . ARG   G  1 219 ? 31.34646  50.79351  3.98680   1.000 50.71948  ?  219 ARG   C CA  1 
ATOM   10355 C C   . ARG   G  1 219 ? 30.71810  50.28963  5.27789   1.000 47.65869  ?  219 ARG   C C   1 
ATOM   10356 O O   . ARG   G  1 219 ? 30.33518  51.08615  6.14044   1.000 46.19465  ?  219 ARG   C O   1 
ATOM   10357 C CB  . ARG   G  1 219 ? 30.25413  51.00075  2.94119   1.000 43.50668  ?  219 ARG   C CB  1 
ATOM   10358 C CG  . ARG   G  1 219 ? 29.25877  52.08012  3.37872   1.000 59.94639  ?  219 ARG   C CG  1 
ATOM   10359 C CD  . ARG   G  1 219 ? 28.07136  52.19553  2.45358   1.000 49.85054  ?  219 ARG   C CD  1 
ATOM   10360 N NE  . ARG   G  1 219 ? 28.44930  52.64321  1.12046   1.000 35.97752  ?  219 ARG   C NE  1 
ATOM   10361 C CZ  . ARG   G  1 219 ? 28.83257  53.88030  0.83546   1.000 103.88454 ?  219 ARG   C CZ  1 
ATOM   10362 N NH1 . ARG   G  1 219 ? 28.89283  54.81969  1.76345   1.000 36.23157  ?  219 ARG   C NH1 1 
ATOM   10363 N NH2 . ARG   G  1 219 ? 29.16762  54.18432  -0.41159  1.000 28.04705  ?  219 ARG   C NH2 1 
ATOM   10364 N N   . ASN   G  1 220 ? 30.60405  48.97776  5.42813   1.000 43.42911  ?  220 ASN   C N   1 
ATOM   10365 C CA  . ASN   G  1 220 ? 29.90634  48.41316  6.56790   1.000 49.47607  ?  220 ASN   C CA  1 
ATOM   10366 C C   . ASN   G  1 220 ? 30.33882  46.96419  6.73933   1.000 46.36402  ?  220 ASN   C C   1 
ATOM   10367 O O   . ASN   G  1 220 ? 29.65472  46.04479  6.26636   1.000 51.80612  ?  220 ASN   C O   1 
ATOM   10368 C CB  . ASN   G  1 220 ? 28.39506  48.51769  6.35323   1.000 57.38743  ?  220 ASN   C CB  1 
ATOM   10369 C CG  . ASN   G  1 220 ? 27.60176  48.24146  7.61160   1.000 82.67041  ?  220 ASN   C CG  1 
ATOM   10370 O OD1 . ASN   G  1 220 ? 28.09552  47.63066  8.56762   1.000 57.91853  ?  220 ASN   C OD1 1 
ATOM   10371 N ND2 . ASN   G  1 220 ? 26.35658  48.68619  7.61631   1.000 59.20317  ?  220 ASN   C ND2 1 
ATOM   10372 N N   . ARG   G  1 221 ? 31.47185  46.74740  7.41263   1.000 44.29298  ?  221 ARG   C N   1 
ATOM   10373 C CA  . ARG   G  1 221 ? 32.00925  45.39113  7.49147   1.000 47.63504  ?  221 ARG   C CA  1 
ATOM   10374 C C   . ARG   G  1 221 ? 31.05309  44.44582  8.21397   1.000 56.32566  ?  221 ARG   C C   1 
ATOM   10375 O O   . ARG   G  1 221 ? 31.01046  43.25704  7.88431   1.000 46.25855  ?  221 ARG   C O   1 
ATOM   10376 C CB  . ARG   G  1 221 ? 33.39411  45.39579  8.15672   1.000 35.11129  ?  221 ARG   C CB  1 
ATOM   10377 C CG  . ARG   G  1 221 ? 33.40456  45.77301  9.64284   1.000 35.63567  ?  221 ARG   C CG  1 
ATOM   10378 C CD  . ARG   G  1 221 ? 33.47077  44.53763  10.55361  1.000 47.33516  ?  221 ARG   C CD  1 
ATOM   10379 N NE  . ARG   G  1 221 ? 33.40996  44.90016  11.96836  1.000 42.36556  ?  221 ARG   C NE  1 
ATOM   10380 C CZ  . ARG   G  1 221 ? 34.46223  45.17714  12.73185  1.000 53.89471  ?  221 ARG   C CZ  1 
ATOM   10381 N NH1 . ARG   G  1 221 ? 35.69950  45.15126  12.25862  1.000 48.26610  ?  221 ARG   C NH1 1 
ATOM   10382 N NH2 . ARG   G  1 221 ? 34.27166  45.47935  14.00818  1.000 38.98509  ?  221 ARG   C NH2 1 
ATOM   10383 N N   . ASP   G  1 222 ? 30.24971  44.95192  9.16358   1.000 36.84353  ?  222 ASP   C N   1 
ATOM   10384 C CA  . ASP   G  1 222 ? 29.32005  44.08121  9.88577   1.000 53.82635  ?  222 ASP   C CA  1 
ATOM   10385 C C   . ASP   G  1 222 ? 28.25491  43.45429  8.98135   1.000 56.55260  ?  222 ASP   C C   1 
ATOM   10386 O O   . ASP   G  1 222 ? 27.69506  42.40687  9.33491   1.000 43.37523  ?  222 ASP   C O   1 
ATOM   10387 C CB  . ASP   G  1 222 ? 28.64788  44.84606  11.02626  1.000 31.34904  ?  222 ASP   C CB  1 
ATOM   10388 C CG  . ASP   G  1 222 ? 29.65345  45.33507  12.08523  1.000 50.34115  ?  222 ASP   C CG  1 
ATOM   10389 O OD1 . ASP   G  1 222 ? 30.27523  44.51158  12.80336  1.000 57.30582  ?  222 ASP   C OD1 1 
ATOM   10390 O OD2 . ASP   G  1 222 ? 29.83580  46.56456  12.16564  1.000 66.43982  -1 222 ASP   C OD2 1 
ATOM   10391 N N   . ILE   G  1 223 ? 27.97080  44.04273  7.82032   1.000 29.56471  ?  223 ILE   C N   1 
ATOM   10392 C CA  . ILE   G  1 223 ? 27.11391  43.36554  6.85023   1.000 39.12093  ?  223 ILE   C CA  1 
ATOM   10393 C C   . ILE   G  1 223 ? 27.92893  42.40676  5.98433   1.000 50.32979  ?  223 ILE   C C   1 
ATOM   10394 O O   . ILE   G  1 223 ? 27.65378  41.20185  5.93580   1.000 52.85678  ?  223 ILE   C O   1 
ATOM   10395 C CB  . ILE   G  1 223 ? 26.34802  44.39783  5.99970   1.000 51.75006  ?  223 ILE   C CB  1 
ATOM   10396 C CG1 . ILE   G  1 223 ? 25.31930  45.13388  6.85308   1.000 32.76675  ?  223 ILE   C CG1 1 
ATOM   10397 C CG2 . ILE   G  1 223 ? 25.64542  43.74022  4.82501   1.000 20.55518  ?  223 ILE   C CG2 1 
ATOM   10398 C CD1 . ILE   G  1 223 ? 24.68154  46.27393  6.11565   1.000 35.79507  ?  223 ILE   C CD1 1 
ATOM   10399 N N   . ASP   G  1 224 ? 28.96629  42.92530  5.31593   1.000 43.72652  ?  224 ASP   C N   1 
ATOM   10400 C CA  . ASP   G  1 224 ? 29.65438  42.20962  4.24123   1.000 44.83206  ?  224 ASP   C CA  1 
ATOM   10401 C C   . ASP   G  1 224 ? 30.80729  41.31268  4.68925   1.000 45.70882  ?  224 ASP   C C   1 
ATOM   10402 O O   . ASP   G  1 224 ? 31.05202  40.28188  4.04838   1.000 41.30054  ?  224 ASP   C O   1 
ATOM   10403 C CB  . ASP   G  1 224 ? 30.18245  43.21544  3.22377   1.000 40.74217  ?  224 ASP   C CB  1 
ATOM   10404 C CG  . ASP   G  1 224 ? 29.09202  44.11089  2.68442   1.000 54.11082  ?  224 ASP   C CG  1 
ATOM   10405 O OD1 . ASP   G  1 224 ? 28.20370  43.57939  1.98665   1.000 57.24099  ?  224 ASP   C OD1 1 
ATOM   10406 O OD2 . ASP   G  1 224 ? 29.12078  45.32879  2.97401   1.000 53.76285  -1 224 ASP   C OD2 1 
ATOM   10407 N N   . ARG   G  1 225 ? 31.54424  41.68144  5.73701   1.000 41.61219  ?  225 ARG   C N   1 
ATOM   10408 C CA  . ARG   G  1 225 ? 32.71720  40.92407  6.19120   1.000 32.28610  ?  225 ARG   C CA  1 
ATOM   10409 C C   . ARG   G  1 225 ? 32.74899  40.94679  7.70979   1.000 47.38434  ?  225 ARG   C C   1 
ATOM   10410 O O   . ARG   G  1 225 ? 33.62876  41.55861  8.32935   1.000 41.42165  ?  225 ARG   C O   1 
ATOM   10411 C CB  . ARG   G  1 225 ? 34.00732  41.51150  5.60579   1.000 33.33807  ?  225 ARG   C CB  1 
ATOM   10412 C CG  . ARG   G  1 225 ? 34.20113  41.22093  4.07937   1.000 19.35654  ?  225 ARG   C CG  1 
ATOM   10413 C CD  . ARG   G  1 225 ? 34.42070  39.70239  3.90107   1.000 10.47728  ?  225 ARG   C CD  1 
ATOM   10414 N NE  . ARG   G  1 225 ? 34.64157  39.31377  2.50455   1.000 52.89712  ?  225 ARG   C NE  1 
ATOM   10415 C CZ  . ARG   G  1 225 ? 33.67227  38.99317  1.65823   1.000 33.05388  ?  225 ARG   C CZ  1 
ATOM   10416 N NH1 . ARG   G  1 225 ? 32.39529  39.07911  2.01191   1.000 58.99494  ?  225 ARG   C NH1 1 
ATOM   10417 N NH2 . ARG   G  1 225 ? 33.99093  38.56499  0.43628   1.000 63.66742  ?  225 ARG   C NH2 1 
ATOM   10418 N N   . PRO   G  1 226 ? 31.77929  40.30585  8.35108   1.000 45.72894  ?  226 PRO   C N   1 
ATOM   10419 C CA  . PRO   G  1 226 ? 31.68050  40.40041  9.81361   1.000 27.53114  ?  226 PRO   C CA  1 
ATOM   10420 C C   . PRO   G  1 226 ? 32.82746  39.68865  10.51199  1.000 52.06753  ?  226 PRO   C C   1 
ATOM   10421 O O   . PRO   G  1 226 ? 33.35793  38.68757  10.02660  1.000 35.29887  ?  226 PRO   C O   1 
ATOM   10422 C CB  . PRO   G  1 226 ? 30.34646  39.70769  10.12515  1.000 26.64638  ?  226 PRO   C CB  1 
ATOM   10423 C CG  . PRO   G  1 226 ? 30.12774  38.76140  8.94897   1.000 25.42314  ?  226 PRO   C CG  1 
ATOM   10424 C CD  . PRO   G  1 226 ? 30.71047  39.47439  7.75646   1.000 28.62567  ?  226 PRO   C CD  1 
ATOM   10425 N N   . VAL   G  1 227 ? 33.19548  40.21548  11.67924  1.000 30.32446  ?  227 VAL   C N   1 
ATOM   10426 C CA  . VAL   G  1 227 ? 34.11976  39.53876  12.58099  1.000 27.34839  ?  227 VAL   C CA  1 
ATOM   10427 C C   . VAL   G  1 227 ? 33.39681  38.33372  13.16756  1.000 39.78438  ?  227 VAL   C C   1 
ATOM   10428 O O   . VAL   G  1 227 ? 32.76838  38.43513  14.22710  1.000 40.77480  ?  227 VAL   C O   1 
ATOM   10429 C CB  . VAL   G  1 227 ? 34.62370  40.48854  13.68526  1.000 30.52017  ?  227 VAL   C CB  1 
ATOM   10430 C CG1 . VAL   G  1 227 ? 35.63118  39.79384  14.59255  1.000 31.67885  ?  227 VAL   C CG1 1 
ATOM   10431 C CG2 . VAL   G  1 227 ? 35.23483  41.73421  13.06192  1.000 25.74412  ?  227 VAL   C CG2 1 
ATOM   10432 N N   . VAL   G  1 228 ? 33.48709  37.18916  12.47632  1.000 25.82180  ?  228 VAL   C N   1 
ATOM   10433 C CA  . VAL   G  1 228 ? 32.65975  36.02474  12.77678  1.000 13.41366  ?  228 VAL   C CA  1 
ATOM   10434 C C   . VAL   G  1 228 ? 32.83432  35.59669  14.22515  1.000 53.69931  ?  228 VAL   C C   1 
ATOM   10435 O O   . VAL   G  1 228 ? 33.95690  35.45234  14.72235  1.000 23.97036  ?  228 VAL   C O   1 
ATOM   10436 C CB  . VAL   G  1 228 ? 32.99750  34.88862  11.80235  1.000 31.83015  ?  228 VAL   C CB  1 
ATOM   10437 C CG1 . VAL   G  1 228 ? 32.16789  33.65327  12.10883  1.000 18.22466  ?  228 VAL   C CG1 1 
ATOM   10438 C CG2 . VAL   G  1 228 ? 32.77710  35.36457  10.36968  1.000 12.83951  ?  228 VAL   C CG2 1 
ATOM   10439 N N   . GLY   G  1 229 ? 31.70884  35.39147  14.91099  1.000 35.37626  ?  229 GLY   C N   1 
ATOM   10440 C CA  . GLY   G  1 229 ? 31.70650  35.04531  16.31798  1.000 19.28248  ?  229 GLY   C CA  1 
ATOM   10441 C C   . GLY   G  1 229 ? 31.84015  36.21949  17.26440  1.000 26.29891  ?  229 GLY   C C   1 
ATOM   10442 O O   . GLY   G  1 229 ? 31.68987  36.03607  18.48473  1.000 41.50059  ?  229 GLY   C O   1 
ATOM   10443 N N   . GLY   G  1 230 ? 32.13387  37.40563  16.74761  1.000 44.92223  ?  230 GLY   C N   1 
ATOM   10444 C CA  . GLY   G  1 230 ? 32.23217  38.63261  17.52885  1.000 15.97625  ?  230 GLY   C CA  1 
ATOM   10445 C C   . GLY   G  1 230 ? 33.59084  38.81806  18.17907  1.000 63.53148  ?  230 GLY   C C   1 
ATOM   10446 O O   . GLY   G  1 230 ? 34.25532  37.86645  18.60021  1.000 33.53891  ?  230 GLY   C O   1 
ATOM   10447 N N   . VAL   G  1 231 ? 33.99159  40.08966  18.28674  1.000 33.63145  ?  231 VAL   C N   1 
ATOM   10448 C CA  . VAL   G  1 231 ? 35.28266  40.48094  18.84143  1.000 73.97599  ?  231 VAL   C CA  1 
ATOM   10449 C C   . VAL   G  1 231 ? 35.49685  39.92713  20.24619  1.000 33.83988  ?  231 VAL   C C   1 
ATOM   10450 O O   . VAL   G  1 231 ? 36.64405  39.76192  20.68184  1.000 68.95295  ?  231 VAL   C O   1 
ATOM   10451 C CB  . VAL   G  1 231 ? 35.38241  42.01756  18.80429  1.000 26.43876  ?  231 VAL   C CB  1 
ATOM   10452 C CG1 . VAL   G  1 231 ? 34.23051  42.61312  19.55725  1.000 81.24564  ?  231 VAL   C CG1 1 
ATOM   10453 C CG2 . VAL   G  1 231 ? 36.66402  42.49901  19.40713  1.000 53.79382  ?  231 VAL   C CG2 1 
ATOM   10454 N N   . ASN   G  1 232 ? 34.41838  39.56996  20.94441  1.000 48.32641  ?  232 ASN   C N   1 
ATOM   10455 C CA  . ASN   G  1 232 ? 34.51758  39.08336  22.31805  1.000 37.30269  ?  232 ASN   C CA  1 
ATOM   10456 C C   . ASN   G  1 232 ? 34.91852  37.61765  22.42905  1.000 48.98598  ?  232 ASN   C C   1 
ATOM   10457 O O   . ASN   G  1 232 ? 35.34185  37.19560  23.51183  1.000 44.19385  ?  232 ASN   C O   1 
ATOM   10458 C CB  . ASN   G  1 232 ? 33.19088  39.27860  23.04046  1.000 54.04682  ?  232 ASN   C CB  1 
ATOM   10459 C CG  . ASN   G  1 232 ? 33.07856  40.63917  23.67501  1.000 53.66800  ?  232 ASN   C CG  1 
ATOM   10460 O OD1 . ASN   G  1 232 ? 33.86041  41.54703  23.36329  1.000 54.67347  ?  232 ASN   C OD1 1 
ATOM   10461 N ND2 . ASN   G  1 232 ? 32.10853  40.79601  24.57622  1.000 129.80035 ?  232 ASN   C ND2 1 
ATOM   10462 N N   . ASN   G  1 233 ? 34.77283  36.82419  21.36788  1.000 34.36391  ?  233 ASN   C N   1 
ATOM   10463 C CA  . ASN   G  1 233 ? 35.18117  35.42562  21.39896  1.000 42.06319  ?  233 ASN   C CA  1 
ATOM   10464 C C   . ASN   G  1 233 ? 36.65616  35.37838  21.00608  1.000 94.53179  ?  233 ASN   C C   1 
ATOM   10465 O O   . ASN   G  1 233 ? 37.00798  35.56038  19.82961  1.000 39.81139  ?  233 ASN   C O   1 
ATOM   10466 C CB  . ASN   G  1 233 ? 34.31517  34.59083  20.45742  1.000 21.97688  ?  233 ASN   C CB  1 
ATOM   10467 C CG  . ASN   G  1 233 ? 34.60135  33.10931  20.56649  1.000 59.36696  ?  233 ASN   C CG  1 
ATOM   10468 O OD1 . ASN   G  1 233 ? 35.70446  32.69373  20.93163  1.000 52.42982  ?  233 ASN   C OD1 1 
ATOM   10469 N ND2 . ASN   G  1 233 ? 33.60885  32.29922  20.23430  1.000 48.11648  ?  233 ASN   C ND2 1 
ATOM   10470 N N   . THR   G  1 234 ? 37.52621  35.16241  21.98741  1.000 38.45742  ?  234 THR   C N   1 
ATOM   10471 C CA  . THR   G  1 234 ? 38.95764  35.21094  21.72256  1.000 53.79186  ?  234 THR   C CA  1 
ATOM   10472 C C   . THR   G  1 234 ? 39.53119  33.84577  21.36876  1.000 34.02600  ?  234 THR   C C   1 
ATOM   10473 O O   . THR   G  1 234 ? 40.74885  33.71978  21.20600  1.000 84.52366  ?  234 THR   C O   1 
ATOM   10474 C CB  . THR   G  1 234 ? 39.70784  35.82747  22.91082  1.000 39.68841  ?  234 THR   C CB  1 
ATOM   10475 O OG1 . THR   G  1 234 ? 39.64956  34.95870  24.04284  1.000 49.87221  ?  234 THR   C OG1 1 
ATOM   10476 C CG2 . THR   G  1 234 ? 39.10247  37.17000  23.28223  1.000 29.67649  ?  234 THR   C CG2 1 
ATOM   10477 N N   . THR   G  1 235 ? 38.67821  32.84207  21.19478  1.000 53.44970  ?  235 THR   C N   1 
ATOM   10478 C CA  . THR   G  1 235 ? 39.11632  31.52926  20.74747  1.000 35.66011  ?  235 THR   C CA  1 
ATOM   10479 C C   . THR   G  1 235 ? 39.20294  31.42184  19.23179  1.000 55.76449  ?  235 THR   C C   1 
ATOM   10480 O O   . THR   G  1 235 ? 39.54660  30.34656  18.72314  1.000 39.02037  ?  235 THR   C O   1 
ATOM   10481 C CB  . THR   G  1 235 ? 38.16389  30.45722  21.27905  1.000 70.81050  ?  235 THR   C CB  1 
ATOM   10482 O OG1 . THR   G  1 235 ? 36.97739  30.40934  20.46447  1.000 31.99985  ?  235 THR   C OG1 1 
ATOM   10483 C CG2 . THR   G  1 235 ? 37.76308  30.79196  22.69623  1.000 41.96830  ?  235 THR   C CG2 1 
ATOM   10484 N N   . LEU   G  1 236 ? 38.90737  32.50191  18.50302  1.000 43.77685  ?  236 LEU   C N   1 
ATOM   10485 C CA  . LEU   G  1 236 ? 38.83225  32.48568  17.04644  1.000 44.24850  ?  236 LEU   C CA  1 
ATOM   10486 C C   . LEU   G  1 236 ? 39.91113  33.38001  16.46442  1.000 37.86673  ?  236 LEU   C C   1 
ATOM   10487 O O   . LEU   G  1 236 ? 40.20304  34.45023  17.00998  1.000 39.58503  ?  236 LEU   C O   1 
ATOM   10488 C CB  . LEU   G  1 236 ? 37.46868  32.96319  16.55000  1.000 37.77477  ?  236 LEU   C CB  1 
ATOM   10489 C CG  . LEU   G  1 236 ? 36.27932  32.27669  17.21635  1.000 45.06786  ?  236 LEU   C CG  1 
ATOM   10490 C CD1 . LEU   G  1 236 ? 35.00447  33.08458  16.96784  1.000 37.01870  ?  236 LEU   C CD1 1 
ATOM   10491 C CD2 . LEU   G  1 236 ? 36.16043  30.83348  16.72624  1.000 27.49434  ?  236 LEU   C CD2 1 
ATOM   10492 N N   . ILE   G  1 237 ? 40.50197  32.93319  15.35809  1.000 42.70022  ?  237 ILE   C N   1 
ATOM   10493 C CA  . ILE   G  1 237 ? 41.50212  33.70260  14.62736  1.000 36.02675  ?  237 ILE   C CA  1 
ATOM   10494 C C   . ILE   G  1 237 ? 40.93285  34.01324  13.24944  1.000 47.26315  ?  237 ILE   C C   1 
ATOM   10495 O O   . ILE   G  1 237 ? 40.54216  33.09458  12.50609  1.000 34.18614  ?  237 ILE   C O   1 
ATOM   10496 C CB  . ILE   G  1 237 ? 42.84460  32.95790  14.51729  1.000 34.84997  ?  237 ILE   C CB  1 
ATOM   10497 C CG1 . ILE   G  1 237 ? 43.39267  32.61940  15.90921  1.000 31.77239  ?  237 ILE   C CG1 1 
ATOM   10498 C CG2 . ILE   G  1 237 ? 43.85508  33.81863  13.74324  1.000 32.71928  ?  237 ILE   C CG2 1 
ATOM   10499 C CD1 . ILE   G  1 237 ? 44.74483  31.90149  15.90176  1.000 33.66715  ?  237 ILE   C CD1 1 
ATOM   10500 N N   . SER   G  1 238 ? 40.90394  35.30956  12.90901  1.000 30.88452  ?  238 SER   C N   1 
ATOM   10501 C CA  . SER   G  1 238 ? 40.32015  35.80244  11.66304  1.000 37.65352  ?  238 SER   C CA  1 
ATOM   10502 C C   . SER   G  1 238 ? 41.34377  35.86855  10.53850  1.000 46.39953  ?  238 SER   C C   1 
ATOM   10503 O O   . SER   G  1 238 ? 42.53856  36.07841  10.76724  1.000 31.37171  ?  238 SER   C O   1 
ATOM   10504 C CB  . SER   G  1 238 ? 39.72153  37.20024  11.84951  1.000 36.11607  ?  238 SER   C CB  1 
ATOM   10505 O OG  . SER   G  1 238 ? 38.40246  37.12566  12.34816  1.000 49.89739  ?  238 SER   C OG  1 
ATOM   10506 N N   . ALA   G  1 239 ? 40.84664  35.72487  9.31031   1.000 40.76997  ?  239 ALA   C N   1 
ATOM   10507 C CA  . ALA   G  1 239 ? 41.65135  35.98421  8.12294   1.000 48.82516  ?  239 ALA   C CA  1 
ATOM   10508 C C   . ALA   G  1 239 ? 42.06000  37.44730  8.06345   1.000 25.02569  ?  239 ALA   C C   1 
ATOM   10509 O O   . ALA   G  1 239 ? 41.21435  38.33654  8.17348   1.000 40.45841  ?  239 ALA   C O   1 
ATOM   10510 C CB  . ALA   G  1 239 ? 40.85984  35.62340  6.87274   1.000 21.40039  ?  239 ALA   C CB  1 
ATOM   10511 N N   . ALA   G  1 240 ? 43.35794  37.70036  7.85128   1.000 31.83415  ?  240 ALA   C N   1 
ATOM   10512 C CA  . ALA   G  1 240 ? 43.85854  39.07642  7.84080   1.000 25.45372  ?  240 ALA   C CA  1 
ATOM   10513 C C   . ALA   G  1 240 ? 43.65483  39.78714  6.50753   1.000 31.92333  ?  240 ALA   C C   1 
ATOM   10514 O O   . ALA   G  1 240 ? 43.66690  41.02619  6.47235   1.000 27.23883  ?  240 ALA   C O   1 
ATOM   10515 C CB  . ALA   G  1 240 ? 45.34545  39.10528  8.19316   1.000 17.18372  ?  240 ALA   C CB  1 
ATOM   10516 N N   . CYS   G  1 241 ? 43.49189  39.03776  5.41581   1.000 29.18545  ?  241 CYS   C N   1 
ATOM   10517 C CA  . CYS   G  1 241 ? 43.38240  39.60789  4.08160   1.000 39.09151  ?  241 CYS   C CA  1 
ATOM   10518 C C   . CYS   G  1 241 ? 42.28561  38.88446  3.32077   1.000 39.40132  ?  241 CYS   C C   1 
ATOM   10519 O O   . CYS   G  1 241 ? 42.15712  37.65636  3.41119   1.000 38.40377  ?  241 CYS   C O   1 
ATOM   10520 C CB  . CYS   G  1 241 ? 44.69121  39.49614  3.28423   1.000 40.72898  ?  241 CYS   C CB  1 
ATOM   10521 S SG  . CYS   G  1 241 ? 46.06866  40.43047  3.97798   1.000 40.98531  ?  241 CYS   C SG  1 
ATOM   10522 N N   . GLU   G  1 242 ? 41.49233  39.66329  2.58059   1.000 42.06813  ?  242 GLU   C N   1 
ATOM   10523 C CA  . GLU   G  1 242 ? 40.61245  39.12696  1.55257   1.000 25.73594  ?  242 GLU   C CA  1 
ATOM   10524 C C   . GLU   G  1 242 ? 41.44248  38.41576  0.48997   1.000 28.63773  ?  242 GLU   C C   1 
ATOM   10525 O O   . GLU   G  1 242 ? 42.19308  39.06613  -0.25026  1.000 51.21838  ?  242 GLU   C O   1 
ATOM   10526 C CB  . GLU   G  1 242 ? 39.79996  40.26206  0.93292   1.000 36.61695  ?  242 GLU   C CB  1 
ATOM   10527 C CG  . GLU   G  1 242 ? 38.80104  39.83116  -0.13459  1.000 30.95004  ?  242 GLU   C CG  1 
ATOM   10528 C CD  . GLU   G  1 242 ? 37.55767  39.15497  0.43260   1.000 54.95461  ?  242 GLU   C CD  1 
ATOM   10529 O OE1 . GLU   G  1 242 ? 37.26872  39.28162  1.65762   1.000 34.43073  ?  242 GLU   C OE1 1 
ATOM   10530 O OE2 . GLU   G  1 242 ? 36.86859  38.49298  -0.37678  1.000 40.97559  -1 242 GLU   C OE2 1 
ATOM   10531 N N   . SER   G  1 243 ? 41.32595  37.09397  0.38816   1.000 29.79065  ?  243 SER   C N   1 
ATOM   10532 C CA  . SER   G  1 243 ? 42.29293  36.34468  -0.40600  1.000 41.27411  ?  243 SER   C CA  1 
ATOM   10533 C C   . SER   G  1 243 ? 41.69938  35.00502  -0.82010  1.000 31.50628  ?  243 SER   C C   1 
ATOM   10534 O O   . SER   G  1 243 ? 40.57574  34.65003  -0.44635  1.000 36.01034  ?  243 SER   C O   1 
ATOM   10535 C CB  . SER   G  1 243 ? 43.59366  36.13098  0.38711   1.000 30.50401  ?  243 SER   C CB  1 
ATOM   10536 O OG  . SER   G  1 243 ? 43.31231  35.44941  1.60717   1.000 38.00021  ?  243 SER   C OG  1 
ATOM   10537 N N   . LEU   G  1 244 ? 42.49583  34.25497  -1.58493  1.000 34.59677  ?  244 LEU   C N   1 
ATOM   10538 C CA  . LEU   G  1 244 ? 42.26962  32.84561  -1.87522  1.000 40.13208  ?  244 LEU   C CA  1 
ATOM   10539 C C   . LEU   G  1 244 ? 43.29328  32.00537  -1.11718  1.000 37.63521  ?  244 LEU   C C   1 
ATOM   10540 O O   . LEU   G  1 244 ? 44.46341  32.39076  -1.01385  1.000 43.91653  ?  244 LEU   C O   1 
ATOM   10541 C CB  . LEU   G  1 244 ? 42.38241  32.58051  -3.37396  1.000 25.00008  ?  244 LEU   C CB  1 
ATOM   10542 C CG  . LEU   G  1 244 ? 41.34815  33.28695  -4.24905  1.000 43.43803  ?  244 LEU   C CG  1 
ATOM   10543 C CD1 . LEU   G  1 244 ? 41.76509  33.25743  -5.70052  1.000 37.39882  ?  244 LEU   C CD1 1 
ATOM   10544 C CD2 . LEU   G  1 244 ? 40.04250  32.58364  -4.05607  1.000 30.62711  ?  244 LEU   C CD2 1 
ATOM   10545 N N   . SER   G  1 245 ? 42.84082  30.88718  -0.55371  1.000 62.49847  ?  245 SER   C N   1 
ATOM   10546 C CA  . SER   G  1 245 ? 43.72459  29.86876  0.00149   1.000 23.12030  ?  245 SER   C CA  1 
ATOM   10547 C C   . SER   G  1 245 ? 44.86319  29.55629  -0.97114  1.000 23.16593  ?  245 SER   C C   1 
ATOM   10548 O O   . SER   G  1 245 ? 44.62662  29.33440  -2.16526  1.000 32.12892  ?  245 SER   C O   1 
ATOM   10549 C CB  . SER   G  1 245 ? 42.88538  28.61578  0.26556   1.000 25.86063  ?  245 SER   C CB  1 
ATOM   10550 O OG  . SER   G  1 245 ? 43.66194  27.56609  0.77425   1.000 71.43343  ?  245 SER   C OG  1 
ATOM   10551 N N   . TYR   G  1 246 ? 46.10787  29.54905  -0.47578  1.000 38.79211  ?  246 TYR   C N   1 
ATOM   10552 C CA  . TYR   G  1 246 ? 47.21890  29.17213  -1.35477  1.000 28.92872  ?  246 TYR   C CA  1 
ATOM   10553 C C   . TYR   G  1 246 ? 47.98720  27.94258  -0.88743  1.000 30.54386  ?  246 TYR   C C   1 
ATOM   10554 O O   . TYR   G  1 246 ? 48.32326  27.07956  -1.71474  1.000 33.60421  ?  246 TYR   C O   1 
ATOM   10555 C CB  . TYR   G  1 246 ? 48.20643  30.33343  -1.55551  1.000 19.30103  ?  246 TYR   C CB  1 
ATOM   10556 C CG  . TYR   G  1 246 ? 49.27860  29.97203  -2.55946  1.000 35.48199  ?  246 TYR   C CG  1 
ATOM   10557 C CD1 . TYR   G  1 246 ? 50.43595  29.27745  -2.17443  1.000 28.58669  ?  246 TYR   C CD1 1 
ATOM   10558 C CD2 . TYR   G  1 246 ? 49.12854  30.30660  -3.90022  1.000 14.69540  ?  246 TYR   C CD2 1 
ATOM   10559 C CE1 . TYR   G  1 246 ? 51.39109  28.92738  -3.10826  1.000 22.32456  ?  246 TYR   C CE1 1 
ATOM   10560 C CE2 . TYR   G  1 246 ? 50.08865  29.96836  -4.84430  1.000 40.98787  ?  246 TYR   C CE2 1 
ATOM   10561 C CZ  . TYR   G  1 246 ? 51.20817  29.27872  -4.44457  1.000 32.00761  ?  246 TYR   C CZ  1 
ATOM   10562 O OH  . TYR   G  1 246 ? 52.13338  28.95324  -5.39501  1.000 48.10512  ?  246 TYR   C OH  1 
ATOM   10563 N N   . ASN   G  1 247 ? 48.34404  27.87150  0.39513   1.000 27.84459  ?  247 ASN   C N   1 
ATOM   10564 C CA  . ASN   G  1 247 ? 49.06213  26.72665  0.94267   1.000 20.22856  ?  247 ASN   C CA  1 
ATOM   10565 C C   . ASN   G  1 247 ? 48.84541  26.70829  2.44691   1.000 27.30363  ?  247 ASN   C C   1 
ATOM   10566 O O   . ASN   G  1 247 ? 48.72128  27.76309  3.07989   1.000 30.53857  ?  247 ASN   C O   1 
ATOM   10567 C CB  . ASN   G  1 247 ? 50.56436  26.77239  0.63644   1.000 30.46660  ?  247 ASN   C CB  1 
ATOM   10568 C CG  . ASN   G  1 247 ? 51.33860  25.68463  1.37180   1.000 28.11568  ?  247 ASN   C CG  1 
ATOM   10569 O OD1 . ASN   G  1 247 ? 51.29499  24.51699  0.97745   1.000 45.59375  ?  247 ASN   C OD1 1 
ATOM   10570 N ND2 . ASN   G  1 247 ? 52.02651  26.05420  2.46212   1.000 26.55725  ?  247 ASN   C ND2 1 
ATOM   10571 N N   . VAL   G  1 248 ? 48.77465  25.49951  3.00821   1.000 27.66703  ?  248 VAL   C N   1 
ATOM   10572 C CA  . VAL   G  1 248 ? 48.91580  25.28986  4.44413   1.000 33.45825  ?  248 VAL   C CA  1 
ATOM   10573 C C   . VAL   G  1 248 ? 50.04385  24.29719  4.66038   1.000 24.99362  ?  248 VAL   C C   1 
ATOM   10574 O O   . VAL   G  1 248 ? 50.14059  23.29630  3.94246   1.000 32.50202  ?  248 VAL   C O   1 
ATOM   10575 C CB  . VAL   G  1 248 ? 47.61643  24.77869  5.08506   1.000 29.00760  ?  248 VAL   C CB  1 
ATOM   10576 C CG1 . VAL   G  1 248 ? 47.88729  24.27123  6.50438   1.000 21.80346  ?  248 VAL   C CG1 1 
ATOM   10577 C CG2 . VAL   G  1 248 ? 46.56987  25.88038  5.07306   1.000 27.10364  ?  248 VAL   C CG2 1 
ATOM   10578 N N   . SER   G  1 249 ? 50.92469  24.59391  5.61349   1.000 41.21856  ?  249 SER   C N   1 
ATOM   10579 C CA  . SER   G  1 249 ? 52.01077  23.68102  5.94060   1.000 28.59023  ?  249 SER   C CA  1 
ATOM   10580 C C   . SER   G  1 249 ? 52.03651  23.45607  7.43768   1.000 41.16963  ?  249 SER   C C   1 
ATOM   10581 O O   . SER   G  1 249 ? 51.85846  24.39630  8.22214   1.000 30.97142  ?  249 SER   C O   1 
ATOM   10582 C CB  . SER   G  1 249 ? 53.36570  24.20217  5.47352   1.000 28.17828  ?  249 SER   C CB  1 
ATOM   10583 O OG  . SER   G  1 249 ? 53.47597  24.09446  4.06764   1.000 33.87157  ?  249 SER   C OG  1 
ATOM   10584 N N   . TYR   G  1 250 ? 52.25221  22.20387  7.82352   1.000 29.25018  ?  250 TYR   C N   1 
ATOM   10585 C CA  . TYR   G  1 250 ? 52.38659  21.82493  9.21739   1.000 55.39721  ?  250 TYR   C CA  1 
ATOM   10586 C C   . TYR   G  1 250 ? 53.83011  21.44013  9.50231   1.000 26.65090  ?  250 TYR   C C   1 
ATOM   10587 O O   . TYR   G  1 250 ? 54.59179  21.08095  8.59070   1.000 35.75884  ?  250 TYR   C O   1 
ATOM   10588 C CB  . TYR   G  1 250 ? 51.45250  20.66056  9.55835   1.000 26.08256  ?  250 TYR   C CB  1 
ATOM   10589 C CG  . TYR   G  1 250 ? 49.99865  20.95480  9.32020   1.000 41.61814  ?  250 TYR   C CG  1 
ATOM   10590 C CD1 . TYR   G  1 250 ? 49.25168  21.66114  10.26077  1.000 27.99830  ?  250 TYR   C CD1 1 
ATOM   10591 C CD2 . TYR   G  1 250 ? 49.37009  20.54484  8.15550   1.000 24.11651  ?  250 TYR   C CD2 1 
ATOM   10592 C CE1 . TYR   G  1 250 ? 47.89686  21.94079  10.04515  1.000 39.84900  ?  250 TYR   C CE1 1 
ATOM   10593 C CE2 . TYR   G  1 250 ? 48.03041  20.81761  7.93261   1.000 35.19909  ?  250 TYR   C CE2 1 
ATOM   10594 C CZ  . TYR   G  1 250 ? 47.29165  21.51411  8.87560   1.000 47.10513  ?  250 TYR   C CZ  1 
ATOM   10595 O OH  . TYR   G  1 250 ? 45.94729  21.78999  8.65120   1.000 52.62420  ?  250 TYR   C OH  1 
ATOM   10596 N N   . ASP   G  1 251 ? 54.19012  21.52929  10.78701  1.000 29.52653  ?  251 ASP   C N   1 
ATOM   10597 C CA  . ASP   G  1 251 ? 55.51972  21.16577  11.27000  1.000 29.78475  ?  251 ASP   C CA  1 
ATOM   10598 C C   . ASP   G  1 251 ? 56.60446  21.86679  10.44678  1.000 48.43874  ?  251 ASP   C C   1 
ATOM   10599 O O   . ASP   G  1 251 ? 57.47227  21.24014  9.83270   1.000 33.30499  ?  251 ASP   C O   1 
ATOM   10600 C CB  . ASP   G  1 251 ? 55.69402  19.64629  11.23100  1.000 29.11570  ?  251 ASP   C CB  1 
ATOM   10601 C CG  . ASP   G  1 251 ? 56.93017  19.17607  11.97036  1.000 51.32583  ?  251 ASP   C CG  1 
ATOM   10602 O OD1 . ASP   G  1 251 ? 57.19278  19.72166  13.06677  1.000 37.75902  ?  251 ASP   C OD1 1 
ATOM   10603 O OD2 . ASP   G  1 251 ? 57.61791  18.25482  11.45442  1.000 37.30181  -1 251 ASP   C OD2 1 
ATOM   10604 N N   . VAL   G  1 252 ? 56.51908  23.19593  10.40707  1.000 28.08269  ?  252 VAL   C N   1 
ATOM   10605 C CA  . VAL   G  1 252 ? 57.44673  23.96858  9.58696   1.000 30.37179  ?  252 VAL   C CA  1 
ATOM   10606 C C   . VAL   G  1 252 ? 58.80803  24.05583  10.26656  1.000 31.33768  ?  252 VAL   C C   1 
ATOM   10607 O O   . VAL   G  1 252 ? 58.94300  23.94521  11.49149  1.000 32.99147  ?  252 VAL   C O   1 
ATOM   10608 C CB  . VAL   G  1 252 ? 56.89270  25.36782  9.27963   1.000 33.21928  ?  252 VAL   C CB  1 
ATOM   10609 C CG1 . VAL   G  1 252 ? 55.62929  25.25356  8.42820   1.000 21.21435  ?  252 VAL   C CG1 1 
ATOM   10610 C CG2 . VAL   G  1 252 ? 56.67247  26.15622  10.58299  1.000 21.60482  ?  252 VAL   C CG2 1 
ATOM   10611 N N   . GLN   G  1 253 ? 59.82409  24.30475  9.44692   1.000 18.91230  ?  253 GLN   C N   1 
ATOM   10612 C CA  . GLN   G  1 253 ? 61.21064  24.19297  9.86204   1.000 24.67873  ?  253 GLN   C CA  1 
ATOM   10613 C C   . GLN   G  1 253 ? 62.05503  25.26564  9.16736   1.000 36.53557  ?  253 GLN   C C   1 
ATOM   10614 O O   . GLN   G  1 253 ? 61.56569  26.05237  8.34403   1.000 23.96539  ?  253 GLN   C O   1 
ATOM   10615 C CB  . GLN   G  1 253 ? 61.72494  22.79358  9.52959   1.000 13.30898  ?  253 GLN   C CB  1 
ATOM   10616 C CG  . GLN   G  1 253 ? 61.56788  22.49969  8.04887   1.000 50.88534  ?  253 GLN   C CG  1 
ATOM   10617 C CD  . GLN   G  1 253 ? 62.07766  21.14265  7.67297   1.000 42.14929  ?  253 GLN   C CD  1 
ATOM   10618 O OE1 . GLN   G  1 253 ? 61.70179  20.59200  6.63628   1.000 43.02985  ?  253 GLN   C OE1 1 
ATOM   10619 N NE2 . GLN   G  1 253 ? 62.94685  20.58962  8.50743   1.000 50.25959  ?  253 GLN   C NE2 1 
ATOM   10620 N N   . SER   G  1 254 ? 63.34772  25.28204  9.48927   1.000 38.17360  ?  254 SER   C N   1 
ATOM   10621 C CA  . SER   G  1 254 ? 64.29848  26.14495  8.80753   1.000 18.11884  ?  254 SER   C CA  1 
ATOM   10622 C C   . SER   G  1 254 ? 65.21081  25.33381  7.88673   1.000 20.20908  ?  254 SER   C C   1 
ATOM   10623 O O   . SER   G  1 254 ? 65.52706  24.16625  8.14289   1.000 31.96664  ?  254 SER   C O   1 
ATOM   10624 C CB  . SER   G  1 254 ? 65.11908  26.94762  9.81192   1.000 28.88600  ?  254 SER   C CB  1 
ATOM   10625 O OG  . SER   G  1 254 ? 64.26242  27.78545  10.58200  1.000 20.45776  ?  254 SER   C OG  1 
ATOM   10626 N N   . LEU   G  1 255 ? 65.59876  25.96382  6.78518   1.000 25.26396  ?  255 LEU   C N   1 
ATOM   10627 C CA  . LEU   G  1 255 ? 66.48645  25.37530  5.80002   1.000 27.62563  ?  255 LEU   C CA  1 
ATOM   10628 C C   . LEU   G  1 255 ? 67.78356  26.17695  5.72453   1.000 29.16494  ?  255 LEU   C C   1 
ATOM   10629 O O   . LEU   G  1 255 ? 67.80945  27.38233  5.99269   1.000 30.41332  ?  255 LEU   C O   1 
ATOM   10630 C CB  . LEU   G  1 255 ? 65.80632  25.33797  4.43330   1.000 30.34402  ?  255 LEU   C CB  1 
ATOM   10631 C CG  . LEU   G  1 255 ? 64.43957  24.66206  4.51129   1.000 31.61599  ?  255 LEU   C CG  1 
ATOM   10632 C CD1 . LEU   G  1 255 ? 63.68299  24.76282  3.19758   1.000 30.40236  ?  255 LEU   C CD1 1 
ATOM   10633 C CD2 . LEU   G  1 255 ? 64.61332  23.21687  4.92759   1.000 20.23297  ?  255 LEU   C CD2 1 
ATOM   10634 N N   . ASP   G  1 256 ? 68.87499  25.50459  5.35569   1.000 34.42730  ?  256 ASP   C N   1 
ATOM   10635 C CA  . ASP   G  1 256 ? 70.12957  26.23510  5.20058   1.000 19.80063  ?  256 ASP   C CA  1 
ATOM   10636 C C   . ASP   G  1 256 ? 70.21577  26.94117  3.84697   1.000 42.33648  ?  256 ASP   C C   1 
ATOM   10637 O O   . ASP   G  1 256 ? 70.81273  28.02452  3.77413   1.000 22.33925  ?  256 ASP   C O   1 
ATOM   10638 C CB  . ASP   G  1 256 ? 71.32107  25.29891  5.41833   1.000 29.82586  ?  256 ASP   C CB  1 
ATOM   10639 C CG  . ASP   G  1 256 ? 71.45355  24.85361  6.87536   1.000 56.54982  ?  256 ASP   C CG  1 
ATOM   10640 O OD1 . ASP   G  1 256 ? 71.82463  25.66196  7.76893   1.000 30.35988  ?  256 ASP   C OD1 1 
ATOM   10641 O OD2 . ASP   G  1 256 ? 71.17429  23.67620  7.13368   1.000 31.04013  -1 256 ASP   C OD2 1 
ATOM   10642 N N   . THR   G  1 257 ? 69.61807  26.36964  2.78721   1.000 24.55471  ?  257 THR   C N   1 
ATOM   10643 C CA  . THR   G  1 257 ? 69.47704  27.03684  1.49588   1.000 52.74540  ?  257 THR   C CA  1 
ATOM   10644 C C   . THR   G  1 257 ? 68.08957  26.77434  0.93327   1.000 18.86269  ?  257 THR   C C   1 
ATOM   10645 O O   . THR   G  1 257 ? 67.42581  25.79869  1.29366   1.000 40.84119  ?  257 THR   C O   1 
ATOM   10646 C CB  . THR   G  1 257 ? 70.51410  26.55408  0.47418   1.000 25.89759  ?  257 THR   C CB  1 
ATOM   10647 O OG1 . THR   G  1 257 ? 70.37674  25.13700  0.29552   1.000 48.61017  ?  257 THR   C OG1 1 
ATOM   10648 C CG2 . THR   G  1 257 ? 71.89044  26.84956  0.94536   1.000 37.48344  ?  257 THR   C CG2 1 
ATOM   10649 N N   . LEU   G  1 258 ? 67.67800  27.64180  0.00845   1.000 40.01256  ?  258 LEU   C N   1 
ATOM   10650 C CA  . LEU   G  1 258 ? 66.39441  27.49387  -0.69097  1.000 25.45793  ?  258 LEU   C CA  1 
ATOM   10651 C C   . LEU   G  1 258 ? 66.63209  26.95315  -2.10125  1.000 52.69551  ?  258 LEU   C C   1 
ATOM   10652 O O   . LEU   G  1 258 ? 66.45068  27.64038  -3.12100  1.000 56.00453  ?  258 LEU   C O   1 
ATOM   10653 C CB  . LEU   G  1 258 ? 65.65357  28.83004  -0.73777  1.000 25.58841  ?  258 LEU   C CB  1 
ATOM   10654 C CG  . LEU   G  1 258 ? 65.65528  29.63655  0.55194   1.000 21.44638  ?  258 LEU   C CG  1 
ATOM   10655 C CD1 . LEU   G  1 258 ? 65.02251  30.96430  0.26209   1.000 28.63578  ?  258 LEU   C CD1 1 
ATOM   10656 C CD2 . LEU   G  1 258 ? 64.93513  28.89853  1.68279   1.000 17.85900  ?  258 LEU   C CD2 1 
ATOM   10657 N N   . VAL   G  1 259 ? 67.06583  25.69547  -2.13962  1.000 39.11843  ?  259 VAL   C N   1 
ATOM   10658 C CA  . VAL   G  1 259 ? 67.46698  25.01400  -3.36743  1.000 42.45615  ?  259 VAL   C CA  1 
ATOM   10659 C C   . VAL   G  1 259 ? 66.86251  23.62402  -3.34125  1.000 106.60456 ?  259 VAL   C C   1 
ATOM   10660 O O   . VAL   G  1 259 ? 67.01169  22.90494  -2.33898  1.000 38.11149  ?  259 VAL   C O   1 
ATOM   10661 C CB  . VAL   G  1 259 ? 68.99731  24.87065  -3.50745  1.000 62.13535  ?  259 VAL   C CB  1 
ATOM   10662 C CG1 . VAL   G  1 259 ? 69.36074  24.50887  -4.93594  1.000 24.26308  ?  259 VAL   C CG1 1 
ATOM   10663 C CG2 . VAL   G  1 259 ? 69.76936  26.09211  -3.00227  1.000 48.64059  ?  259 VAL   C CG2 1 
ATOM   10664 N N   . PHE   G  1 260 ? 66.21585  23.23199  -4.45016  1.000 29.59848  ?  260 PHE   C N   1 
ATOM   10665 C CA  . PHE   G  1 260 ? 65.75172  21.85682  -4.66844  1.000 90.13170  ?  260 PHE   C CA  1 
ATOM   10666 C C   . PHE   G  1 260 ? 64.69018  21.46967  -3.66409  1.000 47.20986  ?  260 PHE   C C   1 
ATOM   10667 O O   . PHE   G  1 260 ? 64.32621  20.29167  -3.55304  1.000 123.54785 ?  260 PHE   C O   1 
ATOM   10668 C CB  . PHE   G  1 260 ? 66.89029  20.81632  -4.59592  1.000 42.71049  ?  260 PHE   C CB  1 
ATOM   10669 C CG  . PHE   G  1 260 ? 67.96455  21.00542  -5.62490  1.000 60.43538  ?  260 PHE   C CG  1 
ATOM   10670 C CD1 . PHE   G  1 260 ? 67.64351  21.40637  -6.90968  1.000 37.98339  ?  260 PHE   C CD1 1 
ATOM   10671 C CD2 . PHE   G  1 260 ? 69.29369  20.78573  -5.30657  1.000 53.60348  ?  260 PHE   C CD2 1 
ATOM   10672 C CE1 . PHE   G  1 260 ? 68.62557  21.59155  -7.86513  1.000 136.99698 ?  260 PHE   C CE1 1 
ATOM   10673 C CE2 . PHE   G  1 260 ? 70.28591  20.96728  -6.26291  1.000 55.14576  ?  260 PHE   C CE2 1 
ATOM   10674 C CZ  . PHE   G  1 260 ? 69.94625  21.37285  -7.54654  1.000 71.82800  ?  260 PHE   C CZ  1 
ATOM   10675 N N   . LYS   G  1 261 ? 64.13778  22.37086  -2.92543  1.000 41.83292  ?  261 LYS   C N   1 
ATOM   10676 C CA  . LYS   G  1 261 ? 62.94395  21.91314  -2.23112  1.000 107.29711 ?  261 LYS   C CA  1 
ATOM   10677 C C   . LYS   G  1 261 ? 61.80373  22.86046  -2.46540  1.000 84.46709  ?  261 LYS   C C   1 
ATOM   10678 O O   . LYS   G  1 261 ? 60.79524  22.74513  -1.76353  1.000 40.60238  ?  261 LYS   C O   1 
ATOM   10679 C CB  . LYS   G  1 261 ? 63.16036  21.73223  -0.73696  1.000 84.75358  ?  261 LYS   C CB  1 
ATOM   10680 C CG  . LYS   G  1 261 ? 64.37666  20.94563  -0.45660  1.000 112.86069 ?  261 LYS   C CG  1 
ATOM   10681 C CD  . LYS   G  1 261 ? 64.56685  20.78765  0.99284   1.000 96.27123  ?  261 LYS   C CD  1 
ATOM   10682 C CE  . LYS   G  1 261 ? 66.01187  20.46224  1.21482   1.000 30.14134  ?  261 LYS   C CE  1 
ATOM   10683 N NZ  . LYS   G  1 261 ? 66.91261  21.73266  1.24186   1.000 44.03024  ?  261 LYS   C NZ  1 
ATOM   10684 N N   . GLY   G  1 262 ? 61.97055  23.76735  -3.45650  1.000 86.57480  ?  262 GLY   C N   1 
ATOM   10685 C CA  . GLY   G  1 262 ? 61.05621  24.83070  -3.82691  1.000 31.16853  ?  262 GLY   C CA  1 
ATOM   10686 C C   . GLY   G  1 262 ? 59.68257  24.63731  -3.23906  1.000 88.03015  ?  262 GLY   C C   1 
ATOM   10687 O O   . GLY   G  1 262 ? 59.20100  23.51682  -3.10554  1.000 81.35409  ?  262 GLY   C O   1 
ATOM   10688 N N   . GLU   G  1 263 ? 59.06519  25.73780  -2.84475  1.000 39.86429  ?  263 GLU   C N   1 
ATOM   10689 C CA  . GLU   G  1 263 ? 57.70433  25.68699  -2.30332  1.000 74.26645  ?  263 GLU   C CA  1 
ATOM   10690 C C   . GLU   G  1 263 ? 57.69363  25.00161  -0.93895  1.000 84.37233  ?  263 GLU   C C   1 
ATOM   10691 O O   . GLU   G  1 263 ? 56.72809  24.31438  -0.57058  1.000 49.20324  ?  263 GLU   C O   1 
ATOM   10692 C CB  . GLU   G  1 263 ? 56.72123  25.00392  -3.27685  1.000 38.28637  ?  263 GLU   C CB  1 
ATOM   10693 C CG  . GLU   G  1 263 ? 55.30654  25.56980  -3.29493  1.000 73.91761  ?  263 GLU   C CG  1 
ATOM   10694 C CD  . GLU   G  1 263 ? 55.20468  26.97065  -3.95861  1.000 67.16674  ?  263 GLU   C CD  1 
ATOM   10695 O OE1 . GLU   G  1 263 ? 56.25900  27.56181  -4.30076  1.000 37.51315  ?  263 GLU   C OE1 1 
ATOM   10696 O OE2 . GLU   G  1 263 ? 54.06362  27.48264  -4.13715  1.000 51.34685  -1 263 GLU   C OE2 1 
ATOM   10697 N N   . THR   G  1 264 ? 58.79792  25.17674  -0.20556  1.000 38.93189  ?  264 THR   C N   1 
ATOM   10698 C CA  . THR   G  1 264 ? 58.88221  24.87857  1.21369   1.000 24.46101  ?  264 THR   C CA  1 
ATOM   10699 C C   . THR   G  1 264 ? 59.21392  26.15735  1.96359   1.000 39.70974  ?  264 THR   C C   1 
ATOM   10700 O O   . THR   G  1 264 ? 60.05919  26.93821  1.51837   1.000 30.79014  ?  264 THR   C O   1 
ATOM   10701 C CB  . THR   G  1 264 ? 59.97082  23.85770  1.49267   1.000 45.30692  ?  264 THR   C CB  1 
ATOM   10702 O OG1 . THR   G  1 264 ? 59.79661  22.73518  0.62544   1.000 96.37776  ?  264 THR   C OG1 1 
ATOM   10703 C CG2 . THR   G  1 264 ? 59.93319  23.43248  2.95852   1.000 32.29462  ?  264 THR   C CG2 1 
ATOM   10704 N N   . TYR   G  1 265 ? 58.55774  26.37956  3.09777   1.000 30.58067  ?  265 TYR   C N   1 
ATOM   10705 C CA  . TYR   G  1 265 ? 58.98006  27.48166  3.95186   1.000 21.09492  ?  265 TYR   C CA  1 
ATOM   10706 C C   . TYR   G  1 265 ? 60.29502  27.14492  4.64322   1.000 25.93365  ?  265 TYR   C C   1 
ATOM   10707 O O   . TYR   G  1 265 ? 60.59248  25.97879  4.93767   1.000 33.95295  ?  265 TYR   C O   1 
ATOM   10708 C CB  . TYR   G  1 265 ? 57.93611  27.80705  5.02347   1.000 17.16937  ?  265 TYR   C CB  1 
ATOM   10709 C CG  . TYR   G  1 265 ? 56.56628  28.14661  4.49829   1.000 36.02758  ?  265 TYR   C CG  1 
ATOM   10710 C CD1 . TYR   G  1 265 ? 56.34929  29.29655  3.76614   1.000 27.37739  ?  265 TYR   C CD1 1 
ATOM   10711 C CD2 . TYR   G  1 265 ? 55.48596  27.31926  4.75665   1.000 24.94052  ?  265 TYR   C CD2 1 
ATOM   10712 C CE1 . TYR   G  1 265 ? 55.07913  29.61351  3.29264   1.000 35.28819  ?  265 TYR   C CE1 1 
ATOM   10713 C CE2 . TYR   G  1 265 ? 54.22668  27.61615  4.29132   1.000 33.52258  ?  265 TYR   C CE2 1 
ATOM   10714 C CZ  . TYR   G  1 265 ? 54.02479  28.76640  3.55598   1.000 27.43361  ?  265 TYR   C CZ  1 
ATOM   10715 O OH  . TYR   G  1 265 ? 52.76119  29.05244  3.08670   1.000 30.76524  ?  265 TYR   C OH  1 
ATOM   10716 N N   . SER   G  1 266 ? 61.08195  28.19340  4.89957   1.000 29.09055  ?  266 SER   C N   1 
ATOM   10717 C CA  . SER   G  1 266 ? 62.22746  28.14517  5.80459   1.000 18.14882  ?  266 SER   C CA  1 
ATOM   10718 C C   . SER   G  1 266 ? 62.02371  29.26902  6.81990   1.000 31.65706  ?  266 SER   C C   1 
ATOM   10719 O O   . SER   G  1 266 ? 62.19306  30.44728  6.48484   1.000 22.19856  ?  266 SER   C O   1 
ATOM   10720 C CB  . SER   G  1 266 ? 63.54508  28.29010  5.04295   1.000 19.91008  ?  266 SER   C CB  1 
ATOM   10721 O OG  . SER   G  1 266 ? 64.62130  28.52530  5.93595   1.000 30.46005  ?  266 SER   C OG  1 
ATOM   10722 N N   . LEU   G  1 267 ? 61.64185  28.90419  8.05162   1.000 23.01542  ?  267 LEU   C N   1 
ATOM   10723 C CA  . LEU   G  1 267 ? 61.32265  29.90151  9.07521   1.000 32.60108  ?  267 LEU   C CA  1 
ATOM   10724 C C   . LEU   G  1 267 ? 62.42749  30.93958  9.22075   1.000 22.37980  ?  267 LEU   C C   1 
ATOM   10725 O O   . LEU   G  1 267 ? 62.15971  32.14646  9.25858   1.000 37.97627  ?  267 LEU   C O   1 
ATOM   10726 C CB  . LEU   G  1 267 ? 61.09076  29.22091  10.41777  1.000 16.05879  ?  267 LEU   C CB  1 
ATOM   10727 C CG  . LEU   G  1 267 ? 59.75706  28.56243  10.70230  1.000 35.65918  ?  267 LEU   C CG  1 
ATOM   10728 C CD1 . LEU   G  1 267 ? 59.87752  28.09127  12.10844  1.000 27.73575  ?  267 LEU   C CD1 1 
ATOM   10729 C CD2 . LEU   G  1 267 ? 58.56610  29.54687  10.54036  1.000 22.02141  ?  267 LEU   C CD2 1 
ATOM   10730 N N   . LYS   G  1 268 ? 63.68011  30.47060  9.33351   1.000 39.43953  ?  268 LYS   C N   1 
ATOM   10731 C CA  . LYS   G  1 268 ? 64.84407  31.35126  9.44198   1.000 18.29516  ?  268 LYS   C CA  1 
ATOM   10732 C C   . LYS   G  1 268 ? 64.84578  32.41823  8.33809   1.000 37.22772  ?  268 LYS   C C   1 
ATOM   10733 O O   . LYS   G  1 268 ? 65.14537  33.58950  8.60069   1.000 16.34845  ?  268 LYS   C O   1 
ATOM   10734 C CB  . LYS   G  1 268 ? 66.11243  30.48379  9.41249   1.000 24.70212  ?  268 LYS   C CB  1 
ATOM   10735 C CG  . LYS   G  1 268 ? 67.43418  31.17501  9.12645   1.000 37.61705  ?  268 LYS   C CG  1 
ATOM   10736 C CD  . LYS   G  1 268 ? 68.46083  30.16538  8.55462   1.000 31.21808  ?  268 LYS   C CD  1 
ATOM   10737 C CE  . LYS   G  1 268 ? 69.78525  30.86947  8.12766   1.000 43.80150  ?  268 LYS   C CE  1 
ATOM   10738 N NZ  . LYS   G  1 268 ? 70.54931  30.05296  7.09179   1.000 40.58358  ?  268 LYS   C NZ  1 
ATOM   10739 N N   . HIS   G  1 269 ? 64.46452  32.04267  7.10725   1.000 28.60698  ?  269 HIS   C N   1 
ATOM   10740 C CA  . HIS   G  1 269 ? 64.39811  32.99344  5.99728   1.000 13.10933  ?  269 HIS   C CA  1 
ATOM   10741 C C   . HIS   G  1 269 ? 63.12918  33.83486  6.05638   1.000 38.04010  ?  269 HIS   C C   1 
ATOM   10742 O O   . HIS   G  1 269 ? 63.19981  35.06907  6.09201   1.000 20.77643  ?  269 HIS   C O   1 
ATOM   10743 C CB  . HIS   G  1 269 ? 64.45439  32.26238  4.65534   1.000 20.77159  ?  269 HIS   C CB  1 
ATOM   10744 C CG  . HIS   G  1 269 ? 65.77081  31.62208  4.36695   1.000 24.81852  ?  269 HIS   C CG  1 
ATOM   10745 N ND1 . HIS   G  1 269 ? 66.15717  30.42527  4.92827   1.000 46.18268  ?  269 HIS   C ND1 1 
ATOM   10746 C CD2 . HIS   G  1 269 ? 66.79180  32.00864  3.56669   1.000 32.09353  ?  269 HIS   C CD2 1 
ATOM   10747 C CE1 . HIS   G  1 269 ? 67.36418  30.10648  4.49322   1.000 21.40455  ?  269 HIS   C CE1 1 
ATOM   10748 N NE2 . HIS   G  1 269 ? 67.77174  31.05108  3.66595   1.000 36.95122  ?  269 HIS   C NE2 1 
ATOM   10749 N N   . LEU   G  1 270 ? 61.95740  33.17554  6.02451   1.000 24.26450  ?  270 LEU   C N   1 
ATOM   10750 C CA  . LEU   G  1 270 ? 60.67429  33.87982  6.11319   1.000 19.51934  ?  270 LEU   C CA  1 
ATOM   10751 C C   . LEU   G  1 270 ? 60.70655  34.97607  7.18063   1.000 23.20719  ?  270 LEU   C C   1 
ATOM   10752 O O   . LEU   G  1 270 ? 60.42157  36.14657  6.89337   1.000 26.76339  ?  270 LEU   C O   1 
ATOM   10753 C CB  . LEU   G  1 270 ? 59.54602  32.88487  6.40410   1.000 26.24072  ?  270 LEU   C CB  1 
ATOM   10754 C CG  . LEU   G  1 270 ? 58.14775  33.48196  6.54609   1.000 23.30308  ?  270 LEU   C CG  1 
ATOM   10755 C CD1 . LEU   G  1 270 ? 57.56296  33.92590  5.19044   1.000 21.03806  ?  270 LEU   C CD1 1 
ATOM   10756 C CD2 . LEU   G  1 270 ? 57.22871  32.50594  7.26389   1.000 29.03332  ?  270 LEU   C CD2 1 
ATOM   10757 N N   . LEU   G  1 271 ? 61.10752  34.62674  8.40632   1.000 29.15454  ?  271 LEU   C N   1 
ATOM   10758 C CA  . LEU   G  1 271 ? 61.13240  35.57434  9.51658   1.000 25.78143  ?  271 LEU   C CA  1 
ATOM   10759 C C   . LEU   G  1 271 ? 62.45263  36.32347  9.64060   1.000 34.21409  ?  271 LEU   C C   1 
ATOM   10760 O O   . LEU   G  1 271 ? 62.65438  37.02889  10.63806  1.000 23.77637  ?  271 LEU   C O   1 
ATOM   10761 C CB  . LEU   G  1 271 ? 60.82345  34.85920  10.83284  1.000 16.24422  ?  271 LEU   C CB  1 
ATOM   10762 C CG  . LEU   G  1 271 ? 59.49394  34.09693  10.82266  1.000 29.33358  ?  271 LEU   C CG  1 
ATOM   10763 C CD1 . LEU   G  1 271 ? 59.36104  33.37331  12.14024  1.000 20.45040  ?  271 LEU   C CD1 1 
ATOM   10764 C CD2 . LEU   G  1 271 ? 58.28510  35.01547  10.54738  1.000 13.97666  ?  271 LEU   C CD2 1 
ATOM   10765 N N   . ASN   G  1 272 ? 63.35610  36.18492  8.66201   1.000 24.38517  ?  272 ASN   C N   1 
ATOM   10766 C CA  . ASN   G  1 272 ? 64.57284  37.00746  8.59379   1.000 16.38566  ?  272 ASN   C CA  1 
ATOM   10767 C C   . ASN   G  1 272 ? 65.40673  36.88758  9.87687   1.000 28.52255  ?  272 ASN   C C   1 
ATOM   10768 O O   . ASN   G  1 272 ? 65.87861  37.87919  10.43089  1.000 35.31664  ?  272 ASN   C O   1 
ATOM   10769 C CB  . ASN   G  1 272 ? 64.21652  38.47134  8.30049   1.000 38.29578  ?  272 ASN   C CB  1 
ATOM   10770 C CG  . ASN   G  1 272 ? 65.42168  39.30966  7.90374   1.000 28.78677  ?  272 ASN   C CG  1 
ATOM   10771 O OD1 . ASN   G  1 272 ? 66.28689  38.87626  7.12677   1.000 28.59061  ?  272 ASN   C OD1 1 
ATOM   10772 N ND2 . ASN   G  1 272 ? 65.48387  40.52627  8.44135   1.000 35.01860  ?  272 ASN   C ND2 1 
ATOM   10773 N N   . ASN   G  1 273 ? 65.56861  35.64766  10.35937  1.000 28.71159  ?  273 ASN   C N   1 
ATOM   10774 C CA  . ASN   G  1 273 ? 66.40225  35.32659  11.53004  1.000 37.81798  ?  273 ASN   C CA  1 
ATOM   10775 C C   . ASN   G  1 273 ? 65.96193  36.05846  12.79212  1.000 25.82722  ?  273 ASN   C C   1 
ATOM   10776 O O   . ASN   G  1 273 ? 66.79644  36.39695  13.63296  1.000 34.62271  ?  273 ASN   C O   1 
ATOM   10777 C CB  . ASN   G  1 273 ? 67.88388  35.60974  11.26437  1.000 32.30713  ?  273 ASN   C CB  1 
ATOM   10778 C CG  . ASN   G  1 273 ? 68.56219  34.47555  10.55570  1.000 68.81067  ?  273 ASN   C CG  1 
ATOM   10779 O OD1 . ASN   G  1 273 ? 68.68130  33.37433  11.10652  1.000 74.24752  ?  273 ASN   C OD1 1 
ATOM   10780 N ND2 . ASN   G  1 273 ? 68.99897  34.72007  9.31827   1.000 71.47203  ?  273 ASN   C ND2 1 
ATOM   10781 N N   . ASP   G  1 274 ? 64.66061  36.29858  12.95841  1.000 28.44703  ?  274 ASP   C N   1 
ATOM   10782 C CA  . ASP   G  1 274 ? 64.21027  36.99691  14.15746  1.000 25.66562  ?  274 ASP   C CA  1 
ATOM   10783 C C   . ASP   G  1 274 ? 64.49711  36.15748  15.40394  1.000 20.06316  ?  274 ASP   C C   1 
ATOM   10784 O O   . ASP   G  1 274 ? 64.38553  34.92160  15.36433  1.000 20.89274  ?  274 ASP   C O   1 
ATOM   10785 C CB  . ASP   G  1 274 ? 62.71340  37.31150  14.07982  1.000 22.25647  ?  274 ASP   C CB  1 
ATOM   10786 C CG  . ASP   G  1 274 ? 62.28210  38.31962  15.12770  1.000 31.88726  ?  274 ASP   C CG  1 
ATOM   10787 O OD1 . ASP   G  1 274 ? 62.04603  37.93017  16.30095  1.000 40.35636  -1 274 ASP   C OD1 1 
ATOM   10788 O OD2 . ASP   G  1 274 ? 62.21809  39.52051  14.77955  1.000 54.07983  ?  274 ASP   C OD2 1 
ATOM   10789 N N   . PRO   G  1 275 ? 64.84874  36.78579  16.52898  1.000 35.24865  ?  275 PRO   C N   1 
ATOM   10790 C CA  . PRO   G  1 275 ? 64.93686  36.03059  17.79621  1.000 15.22164  ?  275 PRO   C CA  1 
ATOM   10791 C C   . PRO   G  1 275 ? 63.70609  35.18842  18.12054  1.000 24.82342  ?  275 PRO   C C   1 
ATOM   10792 O O   . PRO   G  1 275 ? 63.87074  34.13742  18.74824  1.000 38.13878  ?  275 PRO   C O   1 
ATOM   10793 C CB  . PRO   G  1 275 ? 65.16832  37.12508  18.84281  1.000 17.44756  ?  275 PRO   C CB  1 
ATOM   10794 C CG  . PRO   G  1 275 ? 65.80362  38.24526  18.07119  1.000 19.49397  ?  275 PRO   C CG  1 
ATOM   10795 C CD  . PRO   G  1 275 ? 65.24625  38.19371  16.67778  1.000 23.43097  ?  275 PRO   C CD  1 
ATOM   10796 N N   . PHE   G  1 276 ? 62.48880  35.57911  17.69461  1.000 28.13705  ?  276 PHE   C N   1 
ATOM   10797 C CA  . PHE   G  1 276 ? 61.30791  34.73583  17.92777  1.000 18.46952  ?  276 PHE   C CA  1 
ATOM   10798 C C   . PHE   G  1 276 ? 61.28196  33.47113  17.07538  1.000 35.56013  ?  276 PHE   C C   1 
ATOM   10799 O O   . PHE   G  1 276 ? 60.47315  32.57630  17.36017  1.000 31.41842  ?  276 PHE   C O   1 
ATOM   10800 C CB  . PHE   G  1 276 ? 60.00616  35.49220  17.65967  1.000 19.70777  ?  276 PHE   C CB  1 
ATOM   10801 C CG  . PHE   G  1 276 ? 59.76305  36.64216  18.58669  1.000 35.22018  ?  276 PHE   C CG  1 
ATOM   10802 C CD1 . PHE   G  1 276 ? 60.16907  36.58955  19.90683  1.000 28.22692  ?  276 PHE   C CD1 1 
ATOM   10803 C CD2 . PHE   G  1 276 ? 59.11707  37.78215  18.13365  1.000 25.29310  ?  276 PHE   C CD2 1 
ATOM   10804 C CE1 . PHE   G  1 276 ? 59.92652  37.65761  20.76015  1.000 40.00636  ?  276 PHE   C CE1 1 
ATOM   10805 C CE2 . PHE   G  1 276 ? 58.87590  38.85843  18.97703  1.000 43.81934  ?  276 PHE   C CE2 1 
ATOM   10806 C CZ  . PHE   G  1 276 ? 59.28413  38.79906  20.28796  1.000 34.31407  ?  276 PHE   C CZ  1 
ATOM   10807 N N   . THR   G  1 277 ? 62.12060  33.37825  16.04136  1.000 26.66384  ?  277 THR   C N   1 
ATOM   10808 C CA  . THR   G  1 277 ? 62.04696  32.25253  15.10824  1.000 32.38752  ?  277 THR   C CA  1 
ATOM   10809 C C   . THR   G  1 277 ? 61.96473  30.88836  15.78634  1.000 23.96472  ?  277 THR   C C   1 
ATOM   10810 O O   . THR   G  1 277 ? 61.12484  30.07647  15.37063  1.000 30.02585  ?  277 THR   C O   1 
ATOM   10811 C CB  . THR   G  1 277 ? 63.24343  32.29650  14.14515  1.000 21.13146  ?  277 THR   C CB  1 
ATOM   10812 O OG1 . THR   G  1 277 ? 63.31233  33.58737  13.53172  1.000 27.36809  ?  277 THR   C OG1 1 
ATOM   10813 C CG2 . THR   G  1 277 ? 63.09119  31.24646  13.05224  1.000 11.12708  ?  277 THR   C CG2 1 
ATOM   10814 N N   . PRO   G  1 278 ? 62.77051  30.56912  16.81056  1.000 48.86524  ?  278 PRO   C N   1 
ATOM   10815 C CA  . PRO   G  1 278 ? 62.69119  29.21638  17.39184  1.000 21.55733  ?  278 PRO   C CA  1 
ATOM   10816 C C   . PRO   G  1 278 ? 61.31867  28.86161  17.93982  1.000 35.56425  ?  278 PRO   C C   1 
ATOM   10817 O O   . PRO   G  1 278 ? 60.95567  27.67688  17.91438  1.000 24.12669  ?  278 PRO   C O   1 
ATOM   10818 C CB  . PRO   G  1 278 ? 63.73897  29.24759  18.51407  1.000 14.29252  ?  278 PRO   C CB  1 
ATOM   10819 C CG  . PRO   G  1 278 ? 64.63521  30.34786  18.19324  1.000 18.06740  ?  278 PRO   C CG  1 
ATOM   10820 C CD  . PRO   G  1 278 ? 63.82406  31.37363  17.45741  1.000 20.97733  ?  278 PRO   C CD  1 
ATOM   10821 N N   . GLN   G  1 279 ? 60.54601  29.84732  18.43290  1.000 26.49836  ?  279 GLN   C N   1 
ATOM   10822 C CA  . GLN   G  1 279 ? 59.22066  29.56726  18.99364  1.000 24.31253  ?  279 GLN   C CA  1 
ATOM   10823 C C   . GLN   G  1 279 ? 58.25199  28.98894  17.96203  1.000 37.71464  ?  279 GLN   C C   1 
ATOM   10824 O O   . GLN   G  1 279 ? 57.26841  28.33724  18.34605  1.000 36.10574  ?  279 GLN   C O   1 
ATOM   10825 C CB  . GLN   G  1 279 ? 58.60687  30.83516  19.60332  1.000 21.75017  ?  279 GLN   C CB  1 
ATOM   10826 C CG  . GLN   G  1 279 ? 59.38315  31.42750  20.77930  1.000 13.25274  ?  279 GLN   C CG  1 
ATOM   10827 C CD  . GLN   G  1 279 ? 58.62978  32.54955  21.47806  1.000 52.77889  ?  279 GLN   C CD  1 
ATOM   10828 O OE1 . GLN   G  1 279 ? 57.45112  32.41018  21.82265  1.000 38.60982  ?  279 GLN   C OE1 1 
ATOM   10829 N NE2 . GLN   G  1 279 ? 59.31130  33.66853  21.69289  1.000 29.63373  ?  279 GLN   C NE2 1 
ATOM   10830 N N   . PHE   G  1 280 ? 58.50328  29.21878  16.66951  1.000 28.87868  ?  280 PHE   C N   1 
ATOM   10831 C CA  . PHE   G  1 280 ? 57.61689  28.78085  15.60093  1.000 30.45648  ?  280 PHE   C CA  1 
ATOM   10832 C C   . PHE   G  1 280 ? 58.11628  27.52775  14.91609  1.000 28.77893  ?  280 PHE   C C   1 
ATOM   10833 O O   . PHE   G  1 280 ? 57.43878  27.01649  14.01086  1.000 31.45242  ?  280 PHE   C O   1 
ATOM   10834 C CB  . PHE   G  1 280 ? 57.41410  29.91250  14.58631  1.000 12.37022  ?  280 PHE   C CB  1 
ATOM   10835 C CG  . PHE   G  1 280 ? 56.59318  31.01739  15.13689  1.000 42.29605  ?  280 PHE   C CG  1 
ATOM   10836 C CD1 . PHE   G  1 280 ? 55.20154  30.95906  15.08939  1.000 22.99613  ?  280 PHE   C CD1 1 
ATOM   10837 C CD2 . PHE   G  1 280 ? 57.19888  32.06959  15.79948  1.000 13.32034  ?  280 PHE   C CD2 1 
ATOM   10838 C CE1 . PHE   G  1 280 ? 54.44206  31.96715  15.65125  1.000 37.71361  ?  280 PHE   C CE1 1 
ATOM   10839 C CE2 . PHE   G  1 280 ? 56.43882  33.08279  16.36249  1.000 37.02491  ?  280 PHE   C CE2 1 
ATOM   10840 C CZ  . PHE   G  1 280 ? 55.06003  33.02848  16.28976  1.000 29.39925  ?  280 PHE   C CZ  1 
ATOM   10841 N N   . GLU   G  1 281 ? 59.27776  27.02450  15.33169  1.000 29.62563  ?  281 GLU   C N   1 
ATOM   10842 C CA  . GLU   G  1 281 ? 59.74711  25.73318  14.86219  1.000 42.46981  ?  281 GLU   C CA  1 
ATOM   10843 C C   . GLU   G  1 281 ? 58.69608  24.66653  15.16568  1.000 19.71718  ?  281 GLU   C C   1 
ATOM   10844 O O   . GLU   G  1 281 ? 58.13999  24.63097  16.26667  1.000 39.41457  ?  281 GLU   C O   1 
ATOM   10845 C CB  . GLU   G  1 281 ? 61.08332  25.41272  15.53121  1.000 22.98522  ?  281 GLU   C CB  1 
ATOM   10846 C CG  . GLU   G  1 281 ? 62.02261  24.62077  14.66171  1.000 54.96301  ?  281 GLU   C CG  1 
ATOM   10847 C CD  . GLU   G  1 281 ? 62.61196  25.43979  13.52836  1.000 123.17006 ?  281 GLU   C CD  1 
ATOM   10848 O OE1 . GLU   G  1 281 ? 62.97347  26.63242  13.72940  1.000 42.31453  ?  281 GLU   C OE1 1 
ATOM   10849 O OE2 . GLU   G  1 281 ? 62.71760  24.86685  12.42480  1.000 58.28862  -1 281 GLU   C OE2 1 
ATOM   10850 N N   . HIS   G  1 282 ? 58.37716  23.84151  14.16281  1.000 21.46406  ?  282 HIS   C N   1 
ATOM   10851 C CA  . HIS   G  1 282 ? 57.35667  22.79409  14.21267  1.000 45.04946  ?  282 HIS   C CA  1 
ATOM   10852 C C   . HIS   G  1 282 ? 55.92943  23.33385  14.21433  1.000 32.63108  ?  282 HIS   C C   1 
ATOM   10853 O O   . HIS   G  1 282 ? 54.98872  22.54162  14.33351  1.000 37.85731  ?  282 HIS   C O   1 
ATOM   10854 C CB  . HIS   G  1 282 ? 57.50371  21.88483  15.43640  1.000 12.55687  ?  282 HIS   C CB  1 
ATOM   10855 C CG  . HIS   G  1 282 ? 58.81694  21.17874  15.51432  1.000 59.29604  ?  282 HIS   C CG  1 
ATOM   10856 N ND1 . HIS   G  1 282 ? 59.14986  20.13184  14.68037  1.000 44.00654  ?  282 HIS   C ND1 1 
ATOM   10857 C CD2 . HIS   G  1 282 ? 59.87906  21.36253  16.33471  1.000 19.56415  ?  282 HIS   C CD2 1 
ATOM   10858 C CE1 . HIS   G  1 282 ? 60.36548  19.70678  14.97582  1.000 27.90533  ?  282 HIS   C CE1 1 
ATOM   10859 N NE2 . HIS   G  1 282 ? 60.83069  20.43628  15.97699  1.000 39.86414  ?  282 HIS   C NE2 1 
ATOM   10860 N N   . GLY   G  1 283 ? 55.73134  24.64917  14.09446  1.000 37.96964  ?  283 GLY   C N   1 
ATOM   10861 C CA  . GLY   G  1 283 ? 54.40012  25.22812  14.05460  1.000 17.52743  ?  283 GLY   C CA  1 
ATOM   10862 C C   . GLY   G  1 283 ? 53.74945  25.09203  12.69038  1.000 29.70290  ?  283 GLY   C C   1 
ATOM   10863 O O   . GLY   G  1 283 ? 54.17147  24.25800  11.87957  1.000 28.74505  ?  283 GLY   C O   1 
ATOM   10864 N N   . SER   G  1 284 ? 52.72997  25.90238  12.40841  1.000 29.39020  ?  284 SER   C N   1 
ATOM   10865 C CA  . SER   G  1 284 ? 52.00579  25.77583  11.14692  1.000 38.09593  ?  284 SER   C CA  1 
ATOM   10866 C C   . SER   G  1 284 ? 51.80548  27.14991  10.53060  1.000 32.10265  ?  284 SER   C C   1 
ATOM   10867 O O   . SER   G  1 284 ? 51.80164  28.17975  11.22166  1.000 25.03851  ?  284 SER   C O   1 
ATOM   10868 C CB  . SER   G  1 284 ? 50.64356  25.07666  11.33252  1.000 21.14108  ?  284 SER   C CB  1 
ATOM   10869 O OG  . SER   G  1 284 ? 49.96245  25.61411  12.46669  1.000 39.86180  ?  284 SER   C OG  1 
ATOM   10870 N N   . ILE   G  1 285 ? 51.61484  27.14798  9.21355   1.000 23.66422  ?  285 ILE   C N   1 
ATOM   10871 C CA  . ILE   G  1 285 ? 51.50128  28.37015  8.42779   1.000 22.40642  ?  285 ILE   C CA  1 
ATOM   10872 C C   . ILE   G  1 285 ? 50.35081  28.20840  7.44243   1.000 18.56393  ?  285 ILE   C C   1 
ATOM   10873 O O   . ILE   G  1 285 ? 50.27246  27.19868  6.72839   1.000 37.55879  ?  285 ILE   C O   1 
ATOM   10874 C CB  . ILE   G  1 285 ? 52.80696  28.68630  7.66130   1.000 25.81075  ?  285 ILE   C CB  1 
ATOM   10875 C CG1 . ILE   G  1 285 ? 53.97283  29.01534  8.60569   1.000 22.30033  ?  285 ILE   C CG1 1 
ATOM   10876 C CG2 . ILE   G  1 285 ? 52.56772  29.79272  6.66570   1.000 18.24297  ?  285 ILE   C CG2 1 
ATOM   10877 C CD1 . ILE   G  1 285 ? 55.32521  29.09784  7.89125   1.000 30.58975  ?  285 ILE   C CD1 1 
ATOM   10878 N N   . LEU   G  1 286 ? 49.47112  29.20789  7.39905   1.000 36.91632  ?  286 LEU   C N   1 
ATOM   10879 C CA  . LEU   G  1 286 ? 48.45931  29.36453  6.36155   1.000 19.78533  ?  286 LEU   C CA  1 
ATOM   10880 C C   . LEU   G  1 286 ? 48.82949  30.58279  5.52380   1.000 26.68529  ?  286 LEU   C C   1 
ATOM   10881 O O   . LEU   G  1 286 ? 49.11810  31.65114  6.08054   1.000 31.40021  ?  286 LEU   C O   1 
ATOM   10882 C CB  . LEU   G  1 286 ? 47.05476  29.53699  6.97725   1.000 34.97166  ?  286 LEU   C CB  1 
ATOM   10883 C CG  . LEU   G  1 286 ? 46.01745  30.24085  6.07718   1.000 30.63399  ?  286 LEU   C CG  1 
ATOM   10884 C CD1 . LEU   G  1 286 ? 45.64247  29.35862  4.91204   1.000 25.59414  ?  286 LEU   C CD1 1 
ATOM   10885 C CD2 . LEU   G  1 286 ? 44.76461  30.65752  6.82845   1.000 30.83170  ?  286 LEU   C CD2 1 
ATOM   10886 N N   . GLN   G  1 287 ? 48.81307  30.42839  4.19683   1.000 18.69250  ?  287 GLN   C N   1 
ATOM   10887 C CA  . GLN   G  1 287 ? 49.19629  31.49784  3.27936   1.000 32.75484  ?  287 GLN   C CA  1 
ATOM   10888 C C   . GLN   G  1 287 ? 48.09086  31.72981  2.25458   1.000 33.43493  ?  287 GLN   C C   1 
ATOM   10889 O O   . GLN   G  1 287 ? 47.59786  30.77843  1.63083   1.000 27.00250  ?  287 GLN   C O   1 
ATOM   10890 C CB  . GLN   G  1 287 ? 50.52203  31.18194  2.56019   1.000 21.79852  ?  287 GLN   C CB  1 
ATOM   10891 C CG  . GLN   G  1 287 ? 50.92936  32.23493  1.54101   1.000 29.70809  ?  287 GLN   C CG  1 
ATOM   10892 C CD  . GLN   G  1 287 ? 52.33153  32.04076  0.97095   1.000 26.96824  ?  287 GLN   C CD  1 
ATOM   10893 O OE1 . GLN   G  1 287 ? 52.99464  31.03097  1.22085   1.000 29.10684  ?  287 GLN   C OE1 1 
ATOM   10894 N NE2 . GLN   G  1 287 ? 52.78828  33.02303  0.18998   1.000 23.08407  ?  287 GLN   C NE2 1 
ATOM   10895 N N   . GLY   G  1 288 ? 47.71556  32.99761  2.07500   1.000 29.78739  ?  288 GLY   C N   1 
ATOM   10896 C CA  . GLY   G  1 288 ? 46.72297  33.39019  1.08779   1.000 21.61665  ?  288 GLY   C CA  1 
ATOM   10897 C C   . GLY   G  1 288 ? 47.27196  34.25858  -0.03968  1.000 26.23443  ?  288 GLY   C C   1 
ATOM   10898 O O   . GLY   G  1 288 ? 48.32454  34.89794  0.08436   1.000 41.27148  ?  288 GLY   C O   1 
ATOM   10899 N N   . PHE   G  1 289 ? 46.56420  34.27313  -1.16086  1.000 35.14621  ?  289 PHE   C N   1 
ATOM   10900 C CA  . PHE   G  1 289 ? 46.90843  35.08572  -2.31692  1.000 41.69899  ?  289 PHE   C CA  1 
ATOM   10901 C C   . PHE   G  1 289 ? 45.77919  36.07355  -2.56132  1.000 36.99903  ?  289 PHE   C C   1 
ATOM   10902 O O   . PHE   G  1 289 ? 44.61124  35.67778  -2.59417  1.000 39.39197  ?  289 PHE   C O   1 
ATOM   10903 C CB  . PHE   G  1 289 ? 47.12043  34.20043  -3.54459  1.000 30.73961  ?  289 PHE   C CB  1 
ATOM   10904 C CG  . PHE   G  1 289 ? 47.11425  34.94569  -4.85451  1.000 36.42315  ?  289 PHE   C CG  1 
ATOM   10905 C CD1 . PHE   G  1 289 ? 48.05832  35.92930  -5.11609  1.000 25.21032  ?  289 PHE   C CD1 1 
ATOM   10906 C CD2 . PHE   G  1 289 ? 46.18502  34.64463  -5.83907  1.000 35.86376  ?  289 PHE   C CD2 1 
ATOM   10907 C CE1 . PHE   G  1 289 ? 48.07126  36.61242  -6.34559  1.000 43.85297  ?  289 PHE   C CE1 1 
ATOM   10908 C CE2 . PHE   G  1 289 ? 46.19682  35.31872  -7.06550  1.000 39.21915  ?  289 PHE   C CE2 1 
ATOM   10909 C CZ  . PHE   G  1 289 ? 47.14600  36.30097  -7.31791  1.000 37.51894  ?  289 PHE   C CZ  1 
ATOM   10910 N N   . LEU   G  1 290 ? 46.12690  37.35002  -2.71806  1.000 29.46331  ?  290 LEU   C N   1 
ATOM   10911 C CA  . LEU   G  1 290 ? 45.16333  38.40315  -3.01873  1.000 28.83365  ?  290 LEU   C CA  1 
ATOM   10912 C C   . LEU   G  1 290 ? 45.15289  38.66071  -4.52787  1.000 33.20170  ?  290 LEU   C C   1 
ATOM   10913 O O   . LEU   G  1 290 ? 46.19164  39.01249  -5.09509  1.000 52.82731  ?  290 LEU   C O   1 
ATOM   10914 C CB  . LEU   G  1 290 ? 45.52294  39.68113  -2.25433  1.000 21.97098  ?  290 LEU   C CB  1 
ATOM   10915 C CG  . LEU   G  1 290 ? 45.45396  39.77096  -0.71670  1.000 29.72474  ?  290 LEU   C CG  1 
ATOM   10916 C CD1 . LEU   G  1 290 ? 46.57789  38.99713  -0.03785  1.000 27.37220  ?  290 LEU   C CD1 1 
ATOM   10917 C CD2 . LEU   G  1 290 ? 45.45076  41.23130  -0.21907  1.000 21.79463  ?  290 LEU   C CD2 1 
ATOM   10918 N N   . ASN   G  1 291 ? 43.98970  38.49042  -5.17916  1.000 56.88828  ?  291 ASN   C N   1 
ATOM   10919 C CA  . ASN   G  1 291 ? 43.84757  38.84365  -6.60247  1.000 44.30927  ?  291 ASN   C CA  1 
ATOM   10920 C C   . ASN   G  1 291 ? 44.08096  40.33158  -6.80903  1.000 48.82949  ?  291 ASN   C C   1 
ATOM   10921 O O   . ASN   G  1 291 ? 44.03732  41.13479  -5.86866  1.000 48.44739  ?  291 ASN   C O   1 
ATOM   10922 C CB  . ASN   G  1 291 ? 42.45088  38.53360  -7.15843  1.000 71.36786  ?  291 ASN   C CB  1 
ATOM   10923 C CG  . ASN   G  1 291 ? 41.86574  37.27947  -6.59325  1.000 82.33744  ?  291 ASN   C CG  1 
ATOM   10924 O OD1 . ASN   G  1 291 ? 41.32739  37.27699  -5.48180  1.000 128.13997 ?  291 ASN   C OD1 1 
ATOM   10925 N ND2 . ASN   G  1 291 ? 41.96256  36.19338  -7.34936  1.000 83.05313  ?  291 ASN   C ND2 1 
ATOM   10926 N N   . VAL   G  1 292 ? 44.28545  40.70934  -8.07347  1.000 41.34873  ?  292 VAL   C N   1 
ATOM   10927 C CA  . VAL   G  1 292 ? 44.58420  42.11123  -8.33330  1.000 69.32081  ?  292 VAL   C CA  1 
ATOM   10928 C C   . VAL   G  1 292 ? 43.37937  42.99466  -8.02641  1.000 70.06169  ?  292 VAL   C C   1 
ATOM   10929 O O   . VAL   G  1 292 ? 43.54323  44.17117  -7.67280  1.000 52.43664  ?  292 VAL   C O   1 
ATOM   10930 C CB  . VAL   G  1 292 ? 45.07611  42.30574  -9.77298  1.000 67.64078  ?  292 VAL   C CB  1 
ATOM   10931 C CG1 . VAL   G  1 292 ? 45.87388  43.60712  -9.85264  1.000 60.49913  ?  292 VAL   C CG1 1 
ATOM   10932 C CG2 . VAL   G  1 292 ? 45.90031  41.08312  -10.22914 1.000 52.41838  ?  292 VAL   C CG2 1 
ATOM   10933 N N   . THR   G  1 293 ? 42.16190  42.45038  -8.11617  1.000 43.53815  ?  293 THR   C N   1 
ATOM   10934 C CA  . THR   G  1 293 ? 40.94865  43.21412  -7.83694  1.000 49.92701  ?  293 THR   C CA  1 
ATOM   10935 C C   . THR   G  1 293 ? 40.46228  43.10985  -6.38857  1.000 77.18918  ?  293 THR   C C   1 
ATOM   10936 O O   . THR   G  1 293 ? 39.36847  43.60158  -6.08575  1.000 64.43891  ?  293 THR   C O   1 
ATOM   10937 C CB  . THR   G  1 293 ? 39.80843  42.75567  -8.74664  1.000 74.49881  ?  293 THR   C CB  1 
ATOM   10938 O OG1 . THR   G  1 293 ? 39.58616  41.33959  -8.57401  1.000 52.52246  ?  293 THR   C OG1 1 
ATOM   10939 C CG2 . THR   G  1 293 ? 40.12361  43.08215  -10.18738 1.000 43.19610  ?  293 THR   C CG2 1 
ATOM   10940 N N   . ALA   G  1 294 ? 41.22188  42.48010  -5.49550  1.000 42.21069  ?  294 ALA   C N   1 
ATOM   10941 C CA  . ALA   G  1 294 ? 40.72876  42.25157  -4.14592  1.000 35.56725  ?  294 ALA   C CA  1 
ATOM   10942 C C   . ALA   G  1 294 ? 40.94821  43.47259  -3.24453  1.000 35.01593  ?  294 ALA   C C   1 
ATOM   10943 O O   . ALA   G  1 294 ? 41.74532  44.37410  -3.52227  1.000 52.49103  ?  294 ALA   C O   1 
ATOM   10944 C CB  . ALA   G  1 294 ? 41.38696  41.01588  -3.52360  1.000 33.91562  ?  294 ALA   C CB  1 
ATOM   10945 N N   . TYR   G  1 295 ? 40.17099  43.51008  -2.17404  1.000 34.52940  ?  295 TYR   C N   1 
ATOM   10946 C CA  . TYR   G  1 295 ? 40.43600  44.43034  -1.08643  1.000 41.97615  ?  295 TYR   C CA  1 
ATOM   10947 C C   . TYR   G  1 295 ? 41.86398  44.20043  -0.59688  1.000 39.90285  ?  295 TYR   C C   1 
ATOM   10948 O O   . TYR   G  1 295 ? 42.27829  43.05909  -0.37765  1.000 36.82797  ?  295 TYR   C O   1 
ATOM   10949 C CB  . TYR   G  1 295 ? 39.39027  44.16923  -0.00094  1.000 15.18680  ?  295 TYR   C CB  1 
ATOM   10950 C CG  . TYR   G  1 295 ? 39.48951  44.93108  1.29959   1.000 44.98102  ?  295 TYR   C CG  1 
ATOM   10951 C CD1 . TYR   G  1 295 ? 38.86093  46.17682  1.46578   1.000 33.23529  ?  295 TYR   C CD1 1 
ATOM   10952 C CD2 . TYR   G  1 295 ? 40.13600  44.36760  2.39252   1.000 29.09873  ?  295 TYR   C CD2 1 
ATOM   10953 C CE1 . TYR   G  1 295 ? 38.92531  46.86074  2.69053   1.000 26.13344  ?  295 TYR   C CE1 1 
ATOM   10954 C CE2 . TYR   G  1 295 ? 40.20803  45.02772  3.60390   1.000 24.15630  ?  295 TYR   C CE2 1 
ATOM   10955 C CZ  . TYR   G  1 295 ? 39.60309  46.27486  3.75915   1.000 38.44448  ?  295 TYR   C CZ  1 
ATOM   10956 O OH  . TYR   G  1 295 ? 39.68864  46.92444  4.98015   1.000 29.45092  ?  295 TYR   C OH  1 
ATOM   10957 N N   . HIS   G  1 296 ? 42.64617  45.27279  -0.47175  1.000 32.25755  ?  296 HIS   C N   1 
ATOM   10958 C CA  . HIS   G  1 296 ? 44.07125  45.11703  -0.18355  1.000 40.48580  ?  296 HIS   C CA  1 
ATOM   10959 C C   . HIS   G  1 296 ? 44.49491  45.68029  1.17451   1.000 25.07437  ?  296 HIS   C C   1 
ATOM   10960 O O   . HIS   G  1 296 ? 45.68946  45.95237  1.37910   1.000 30.97493  ?  296 HIS   C O   1 
ATOM   10961 C CB  . HIS   G  1 296 ? 44.91840  45.72792  -1.30967  1.000 29.47286  ?  296 HIS   C CB  1 
ATOM   10962 C CG  . HIS   G  1 296 ? 45.37077  44.71373  -2.32087  1.000 39.36665  ?  296 HIS   C CG  1 
ATOM   10963 N ND1 . HIS   G  1 296 ? 44.55626  44.26216  -3.33675  1.000 47.18256  ?  296 HIS   C ND1 1 
ATOM   10964 C CD2 . HIS   G  1 296 ? 46.52760  44.01714  -2.43253  1.000 38.81297  ?  296 HIS   C CD2 1 
ATOM   10965 C CE1 . HIS   G  1 296 ? 45.19541  43.34450  -4.03967  1.000 39.21504  ?  296 HIS   C CE1 1 
ATOM   10966 N NE2 . HIS   G  1 296 ? 46.39567  43.17909  -3.51381  1.000 53.12123  ?  296 HIS   C NE2 1 
ATOM   10967 N N   . ARG   G  1 297 ? 43.56757  45.83665  2.11866   1.000 30.74817  ?  297 ARG   C N   1 
ATOM   10968 C CA  . ARG   G  1 297 ? 43.97697  46.24100  3.45714   1.000 26.17303  ?  297 ARG   C CA  1 
ATOM   10969 C C   . ARG   G  1 297 ? 44.15999  45.01513  4.34386   1.000 43.15032  ?  297 ARG   C C   1 
ATOM   10970 O O   . ARG   G  1 297 ? 43.74690  43.90536  3.99780   1.000 32.79642  ?  297 ARG   C O   1 
ATOM   10971 C CB  . ARG   G  1 297 ? 42.96846  47.19316  4.07818   1.000 30.05433  ?  297 ARG   C CB  1 
ATOM   10972 C CG  . ARG   G  1 297 ? 42.58282  48.34230  3.18268   1.000 35.07365  ?  297 ARG   C CG  1 
ATOM   10973 C CD  . ARG   G  1 297 ? 41.67697  49.28205  3.95351   1.000 31.93736  ?  297 ARG   C CD  1 
ATOM   10974 N NE  . ARG   G  1 297 ? 42.05918  50.67203  3.73758   1.000 49.44432  ?  297 ARG   C NE  1 
ATOM   10975 C CZ  . ARG   G  1 297 ? 42.60794  51.43847  4.66720   1.000 41.76472  ?  297 ARG   C CZ  1 
ATOM   10976 N NH1 . ARG   G  1 297 ? 42.79305  50.99380  5.90583   1.000 50.13990  ?  297 ARG   C NH1 1 
ATOM   10977 N NH2 . ARG   G  1 297 ? 42.97310  52.67959  4.35019   1.000 85.44188  ?  297 ARG   C NH2 1 
ATOM   10978 N N   . TRP   G  1 298 ? 44.81892  45.22631  5.48675   1.000 34.23658  ?  298 TRP   C N   1 
ATOM   10979 C CA  . TRP   G  1 298 ? 45.07214  44.18406  6.46870   1.000 32.08495  ?  298 TRP   C CA  1 
ATOM   10980 C C   . TRP   G  1 298 ? 44.19989  44.42281  7.69276   1.000 40.00472  ?  298 TRP   C C   1 
ATOM   10981 O O   . TRP   G  1 298 ? 44.08211  45.55652  8.17386   1.000 44.04241  ?  298 TRP   C O   1 
ATOM   10982 C CB  . TRP   G  1 298 ? 46.53878  44.15539  6.92806   1.000 26.26384  ?  298 TRP   C CB  1 
ATOM   10983 C CG  . TRP   G  1 298 ? 47.59747  44.31897  5.87456   1.000 36.99528  ?  298 TRP   C CG  1 
ATOM   10984 C CD1 . TRP   G  1 298 ? 47.49916  44.03917  4.53293   1.000 32.26571  ?  298 TRP   C CD1 1 
ATOM   10985 C CD2 . TRP   G  1 298 ? 48.93528  44.80556  6.08583   1.000 26.37775  ?  298 TRP   C CD2 1 
ATOM   10986 N NE1 . TRP   G  1 298 ? 48.69121  44.33898  3.89983   1.000 23.67465  ?  298 TRP   C NE1 1 
ATOM   10987 C CE2 . TRP   G  1 298 ? 49.58679  44.80035  4.83316   1.000 29.97260  ?  298 TRP   C CE2 1 
ATOM   10988 C CE3 . TRP   G  1 298 ? 49.63627  45.26263  7.21182   1.000 19.44071  ?  298 TRP   C CE3 1 
ATOM   10989 C CZ2 . TRP   G  1 298 ? 50.90645  45.23074  4.67973   1.000 35.09814  ?  298 TRP   C CZ2 1 
ATOM   10990 C CZ3 . TRP   G  1 298 ? 50.93828  45.67868  7.05967   1.000 41.34429  ?  298 TRP   C CZ3 1 
ATOM   10991 C CH2 . TRP   G  1 298 ? 51.56347  45.66135  5.80262   1.000 32.89966  ?  298 TRP   C CH2 1 
ATOM   10992 N N   . HIS   G  1 299 ? 43.62882  43.34613  8.21634   1.000 37.25272  ?  299 HIS   C N   1 
ATOM   10993 C CA  . HIS   G  1 299 ? 42.85618  43.38159  9.44572   1.000 46.13078  ?  299 HIS   C CA  1 
ATOM   10994 C C   . HIS   G  1 299 ? 43.54649  42.53743  10.50786  1.000 36.28580  ?  299 HIS   C C   1 
ATOM   10995 O O   . HIS   G  1 299 ? 44.24913  41.57102  10.19023  1.000 38.37940  ?  299 HIS   C O   1 
ATOM   10996 C CB  . HIS   G  1 299 ? 41.42281  42.86918  9.23464   1.000 25.46314  ?  299 HIS   C CB  1 
ATOM   10997 C CG  . HIS   G  1 299 ? 40.57994  43.75691  8.36967   1.000 42.38165  ?  299 HIS   C CG  1 
ATOM   10998 N ND1 . HIS   G  1 299 ? 39.26533  43.47234  8.06449   1.000 35.42641  ?  299 HIS   C ND1 1 
ATOM   10999 C CD2 . HIS   G  1 299 ? 40.87262  44.91624  7.73396   1.000 35.72835  ?  299 HIS   C CD2 1 
ATOM   11000 C CE1 . HIS   G  1 299 ? 38.78549  44.42008  7.27874   1.000 49.15663  ?  299 HIS   C CE1 1 
ATOM   11001 N NE2 . HIS   G  1 299 ? 39.74151  45.30810  7.06378   1.000 37.51756  ?  299 HIS   C NE2 1 
ATOM   11002 N N   . ALA   G  1 300 ? 43.32866  42.90563  11.77551  1.000 32.89976  ?  300 ALA   C N   1 
ATOM   11003 C CA  . ALA   G  1 300 ? 43.94737  42.18282  12.88536  1.000 37.93527  ?  300 ALA   C CA  1 
ATOM   11004 C C   . ALA   G  1 300 ? 43.29917  40.81230  13.03745  1.000 30.92017  ?  300 ALA   C C   1 
ATOM   11005 O O   . ALA   G  1 300 ? 42.06679  40.71875  13.09536  1.000 41.12022  ?  300 ALA   C O   1 
ATOM   11006 C CB  . ALA   G  1 300 ? 43.81099  42.97052  14.18193  1.000 26.47471  ?  300 ALA   C CB  1 
ATOM   11007 N N   . PRO   G  1 301 ? 44.08349  39.73012  13.09240  1.000 40.00781  ?  301 PRO   C N   1 
ATOM   11008 C CA  . PRO   G  1 301 ? 43.49061  38.38070  13.16447  1.000 25.84858  ?  301 PRO   C CA  1 
ATOM   11009 C C   . PRO   G  1 301 ? 43.04064  37.96669  14.56002  1.000 46.63490  ?  301 PRO   C C   1 
ATOM   11010 O O   . PRO   G  1 301 ? 42.32212  36.96380  14.68544  1.000 31.03448  ?  301 PRO   C O   1 
ATOM   11011 C CB  . PRO   G  1 301 ? 44.62953  37.47770  12.66005  1.000 34.74633  ?  301 PRO   C CB  1 
ATOM   11012 C CG  . PRO   G  1 301 ? 45.87938  38.21534  13.04283  1.000 31.99590  ?  301 PRO   C CG  1 
ATOM   11013 C CD  . PRO   G  1 301 ? 45.55514  39.70250  12.99520  1.000 17.30589  ?  301 PRO   C CD  1 
ATOM   11014 N N   . VAL   G  1 302 ? 43.44230  38.70326  15.60113  1.000 26.78584  ?  302 VAL   C N   1 
ATOM   11015 C CA  . VAL   G  1 302 ? 43.11780  38.39592  16.99196  1.000 51.61815  ?  302 VAL   C CA  1 
ATOM   11016 C C   . VAL   G  1 302 ? 43.01420  39.70395  17.76635  1.000 26.03090  ?  302 VAL   C C   1 
ATOM   11017 O O   . VAL   G  1 302 ? 43.49236  40.74973  17.32531  1.000 42.70299  ?  302 VAL   C O   1 
ATOM   11018 C CB  . VAL   G  1 302 ? 44.18253  37.49513  17.66623  1.000 25.78871  ?  302 VAL   C CB  1 
ATOM   11019 C CG1 . VAL   G  1 302 ? 44.26020  36.13942  16.98730  1.000 50.05599  ?  302 VAL   C CG1 1 
ATOM   11020 C CG2 . VAL   G  1 302 ? 45.54905  38.20918  17.68890  1.000 24.47646  ?  302 VAL   C CG2 1 
ATOM   11021 N N   . ASN   G  1 303 ? 42.38732  39.64186  18.94047  1.000 50.28806  ?  303 ASN   C N   1 
ATOM   11022 C CA  . ASN   G  1 303 ? 42.59028  40.69470  19.92940  1.000 35.15989  ?  303 ASN   C CA  1 
ATOM   11023 C C   . ASN   G  1 303 ? 43.97890  40.51665  20.52704  1.000 54.46255  ?  303 ASN   C C   1 
ATOM   11024 O O   . ASN   G  1 303 ? 44.32452  39.42175  20.99306  1.000 49.96449  ?  303 ASN   C O   1 
ATOM   11025 C CB  . ASN   G  1 303 ? 41.54049  40.63275  21.04167  1.000 53.98713  ?  303 ASN   C CB  1 
ATOM   11026 C CG  . ASN   G  1 303 ? 40.10766  40.65279  20.52301  1.000 46.72626  ?  303 ASN   C CG  1 
ATOM   11027 O OD1 . ASN   G  1 303 ? 39.83288  40.95449  19.35457  1.000 51.43351  ?  303 ASN   C OD1 1 
ATOM   11028 N ND2 . ASN   G  1 303 ? 39.18147  40.32931  21.40897  1.000 49.48619  ?  303 ASN   C ND2 1 
ATOM   11029 N N   . GLY   G  1 304 ? 44.79181  41.56521  20.49749  1.000 41.90026  ?  304 GLY   C N   1 
ATOM   11030 C CA  . GLY   G  1 304 ? 46.12483  41.40195  21.03776  1.000 28.67248  ?  304 GLY   C CA  1 
ATOM   11031 C C   . GLY   G  1 304 ? 46.95374  42.65545  20.90379  1.000 45.19902  ?  304 GLY   C C   1 
ATOM   11032 O O   . GLY   G  1 304 ? 46.46043  43.72698  20.53267  1.000 48.01475  ?  304 GLY   C O   1 
ATOM   11033 N N   . THR   G  1 305 ? 48.23836  42.48650  21.20573  1.000 39.98026  ?  305 THR   C N   1 
ATOM   11034 C CA  . THR   G  1 305 ? 49.20522  43.57436  21.22448  1.000 41.27906  ?  305 THR   C CA  1 
ATOM   11035 C C   . THR   G  1 305 ? 50.23834  43.37967  20.12008  1.000 63.21149  ?  305 THR   C C   1 
ATOM   11036 O O   . THR   G  1 305 ? 50.73039  42.26071  19.89916  1.000 28.08507  ?  305 THR   C O   1 
ATOM   11037 C CB  . THR   G  1 305 ? 49.90514  43.64240  22.58351  1.000 30.89893  ?  305 THR   C CB  1 
ATOM   11038 O OG1 . THR   G  1 305 ? 48.92888  43.45808  23.61651  1.000 47.97038  ?  305 THR   C OG1 1 
ATOM   11039 C CG2 . THR   G  1 305 ? 50.59232  44.98626  22.75668  1.000 30.68600  ?  305 THR   C CG2 1 
ATOM   11040 N N   . ILE   G  1 306 ? 50.55702  44.46746  19.42061  1.000 30.08878  ?  306 ILE   C N   1 
ATOM   11041 C CA  . ILE   G  1 306 ? 51.59886  44.41118  18.40561  1.000 42.91413  ?  306 ILE   C CA  1 
ATOM   11042 C C   . ILE   G  1 306 ? 52.92917  44.31814  19.12854  1.000 43.55333  ?  306 ILE   C C   1 
ATOM   11043 O O   . ILE   G  1 306 ? 53.30141  45.22645  19.87852  1.000 46.60869  ?  306 ILE   C O   1 
ATOM   11044 C CB  . ILE   G  1 306 ? 51.55478  45.63909  17.48856  1.000 39.18313  ?  306 ILE   C CB  1 
ATOM   11045 C CG1 . ILE   G  1 306 ? 50.13410  45.89028  16.96148  1.000 26.58583  ?  306 ILE   C CG1 1 
ATOM   11046 C CG2 . ILE   G  1 306 ? 52.57651  45.48059  16.35585  1.000 34.87694  ?  306 ILE   C CG2 1 
ATOM   11047 C CD1 . ILE   G  1 306 ? 49.48607  44.70083  16.24390  1.000 33.34350  ?  306 ILE   C CD1 1 
ATOM   11048 N N   . VAL   G  1 307 ? 53.63490  43.21265  18.93529  1.000 37.26269  ?  307 VAL   C N   1 
ATOM   11049 C CA  . VAL   G  1 307 ? 54.89894  43.03110  19.62776  1.000 31.14771  ?  307 VAL   C CA  1 
ATOM   11050 C C   . VAL   G  1 307 ? 56.05215  43.65629  18.85133  1.000 39.86494  ?  307 VAL   C C   1 
ATOM   11051 O O   . VAL   G  1 307 ? 56.89743  44.33441  19.44188  1.000 38.36844  ?  307 VAL   C O   1 
ATOM   11052 C CB  . VAL   G  1 307 ? 55.14377  41.53765  19.90562  1.000 47.07031  ?  307 VAL   C CB  1 
ATOM   11053 C CG1 . VAL   G  1 307 ? 56.46916  41.35207  20.62439  1.000 21.04530  ?  307 VAL   C CG1 1 
ATOM   11054 C CG2 . VAL   G  1 307 ? 53.99536  40.93896  20.71724  1.000 32.11676  ?  307 VAL   C CG2 1 
ATOM   11055 N N   . LYS   G  1 308 ? 56.07156  43.48330  17.52665  1.000 43.32630  ?  308 LYS   C N   1 
ATOM   11056 C CA  . LYS   G  1 308 ? 57.24987  43.80089  16.72422  1.000 33.94524  ?  308 LYS   C CA  1 
ATOM   11057 C C   . LYS   G  1 308 ? 56.87047  43.85204  15.25153  1.000 47.46887  ?  308 LYS   C C   1 
ATOM   11058 O O   . LYS   G  1 308 ? 56.20664  42.93704  14.74740  1.000 30.63913  ?  308 LYS   C O   1 
ATOM   11059 C CB  . LYS   G  1 308 ? 58.33182  42.74678  16.94410  1.000 30.76128  ?  308 LYS   C CB  1 
ATOM   11060 C CG  . LYS   G  1 308 ? 59.74113  43.10847  16.50996  1.000 22.10240  ?  308 LYS   C CG  1 
ATOM   11061 C CD  . LYS   G  1 308 ? 60.57189  41.83245  16.66620  1.000 32.95983  ?  308 LYS   C CD  1 
ATOM   11062 C CE  . LYS   G  1 308 ? 62.07389  42.07354  16.71721  1.000 52.90292  ?  308 LYS   C CE  1 
ATOM   11063 N NZ  . LYS   G  1 308 ? 62.71581  40.81375  17.23653  1.000 64.54879  ?  308 LYS   C NZ  1 
ATOM   11064 N N   . ILE   G  1 309 ? 57.30608  44.91005  14.56945  1.000 30.33242  ?  309 ILE   C N   1 
ATOM   11065 C CA  . ILE   G  1 309 ? 57.09444  45.09684  13.13865  1.000 37.41084  ?  309 ILE   C CA  1 
ATOM   11066 C C   . ILE   G  1 309 ? 58.46326  45.23694  12.49233  1.000 29.85860  ?  309 ILE   C C   1 
ATOM   11067 O O   . ILE   G  1 309 ? 59.23266  46.12475  12.87565  1.000 38.43356  ?  309 ILE   C O   1 
ATOM   11068 C CB  . ILE   G  1 309 ? 56.24920  46.34041  12.83953  1.000 21.86123  ?  309 ILE   C CB  1 
ATOM   11069 C CG1 . ILE   G  1 309 ? 54.88207  46.25585  13.50117  1.000 42.55121  ?  309 ILE   C CG1 1 
ATOM   11070 C CG2 . ILE   G  1 309 ? 56.12129  46.52836  11.33053  1.000 24.51628  ?  309 ILE   C CG2 1 
ATOM   11071 C CD1 . ILE   G  1 309 ? 54.17413  47.58113  13.51484  1.000 23.24876  ?  309 ILE   C CD1 1 
ATOM   11072 N N   . ILE   G  1 310 ? 58.76706  44.37954  11.51188  1.000 34.00626  ?  310 ILE   C N   1 
ATOM   11073 C CA  . ILE   G  1 310 ? 60.05881  44.39898  10.83178  1.000 17.88415  ?  310 ILE   C CA  1 
ATOM   11074 C C   . ILE   G  1 310 ? 59.84111  44.50349  9.33172   1.000 35.29592  ?  310 ILE   C C   1 
ATOM   11075 O O   . ILE   G  1 310 ? 59.09668  43.70487  8.74897   1.000 28.29011  ?  310 ILE   C O   1 
ATOM   11076 C CB  . ILE   G  1 310 ? 60.90148  43.14886  11.13215  1.000 35.27351  ?  310 ILE   C CB  1 
ATOM   11077 C CG1 . ILE   G  1 310 ? 60.97763  42.88818  12.63277  1.000 36.36424  ?  310 ILE   C CG1 1 
ATOM   11078 C CG2 . ILE   G  1 310 ? 62.27108  43.31912  10.51791  1.000 22.70953  ?  310 ILE   C CG2 1 
ATOM   11079 C CD1 . ILE   G  1 310 ? 60.31938  41.58872  13.04252  1.000 40.73553  ?  310 ILE   C CD1 1 
ATOM   11080 N N   . ASN   G  1 311 ? 60.52928  45.44339  8.69567   1.000 34.78799  ?  311 ASN   C N   1 
ATOM   11081 C CA  . ASN   G  1 311 ? 60.44452  45.59154  7.25072   1.000 31.60016  ?  311 ASN   C CA  1 
ATOM   11082 C C   . ASN   G  1 311 ? 61.70797  45.03262  6.61816   1.000 20.95689  ?  311 ASN   C C   1 
ATOM   11083 O O   . ASN   G  1 311 ? 62.82057  45.44278  6.95992   1.000 47.96984  ?  311 ASN   C O   1 
ATOM   11084 C CB  . ASN   G  1 311 ? 60.20037  47.04375  6.86083   1.000 16.35487  ?  311 ASN   C CB  1 
ATOM   11085 C CG  . ASN   G  1 311 ? 58.73024  47.42581  7.01211   1.000 62.07789  ?  311 ASN   C CG  1 
ATOM   11086 O OD1 . ASN   G  1 311 ? 57.86346  46.89544  6.30311   1.000 42.06897  ?  311 ASN   C OD1 1 
ATOM   11087 N ND2 . ASN   G  1 311 ? 58.43962  48.31314  7.95855   1.000 44.27253  ?  311 ASN   C ND2 1 
ATOM   11088 N N   . VAL   G  1 312 ? 61.53314  44.06388  5.72770   1.000 28.79421  ?  312 VAL   C N   1 
ATOM   11089 C CA  . VAL   G  1 312 ? 62.64065  43.29341  5.19001   1.000 27.23991  ?  312 VAL   C CA  1 
ATOM   11090 C C   . VAL   G  1 312 ? 62.75980  43.57796  3.69500   1.000 26.08575  ?  312 VAL   C C   1 
ATOM   11091 O O   . VAL   G  1 312 ? 61.82016  43.31997  2.93550   1.000 50.98891  ?  312 VAL   C O   1 
ATOM   11092 C CB  . VAL   G  1 312 ? 62.46952  41.78712  5.45468   1.000 30.80580  ?  312 VAL   C CB  1 
ATOM   11093 C CG1 . VAL   G  1 312 ? 63.78324  41.04951  5.14312   1.000 17.10265  ?  312 VAL   C CG1 1 
ATOM   11094 C CG2 . VAL   G  1 312 ? 62.07014  41.55210  6.90728   1.000 23.50190  ?  312 VAL   C CG2 1 
ATOM   11095 N N   . PRO   G  1 313 ? 63.87956  44.11917  3.23147   1.000 36.86026  ?  313 PRO   C N   1 
ATOM   11096 C CA  . PRO   G  1 313 ? 64.10104  44.23772  1.78216   1.000 32.54308  ?  313 PRO   C CA  1 
ATOM   11097 C C   . PRO   G  1 313 ? 64.25692  42.86047  1.15948   1.000 36.22315  ?  313 PRO   C C   1 
ATOM   11098 O O   . PRO   G  1 313 ? 64.73599  41.91793  1.79921   1.000 31.46145  ?  313 PRO   C O   1 
ATOM   11099 C CB  . PRO   G  1 313 ? 65.41292  45.03304  1.67333   1.000 15.58216  ?  313 PRO   C CB  1 
ATOM   11100 C CG  . PRO   G  1 313 ? 65.69539  45.56955  3.08973   1.000 21.43082  ?  313 PRO   C CG  1 
ATOM   11101 C CD  . PRO   G  1 313 ? 64.99888  44.63184  4.03732   1.000 17.60176  ?  313 PRO   C CD  1 
ATOM   11102 N N   . GLY   G  1 314 ? 63.85579  42.74652  -0.10263  1.000 25.55220  ?  314 GLY   C N   1 
ATOM   11103 C CA  . GLY   G  1 314 ? 63.93033  41.46161  -0.75794  1.000 18.01364  ?  314 GLY   C CA  1 
ATOM   11104 C C   . GLY   G  1 314 ? 63.72668  41.52141  -2.25273  1.000 34.97645  ?  314 GLY   C C   1 
ATOM   11105 O O   . GLY   G  1 314 ? 63.96101  42.54933  -2.89339  1.000 26.22749  ?  314 GLY   C O   1 
ATOM   11106 N N   . THR   G  1 315 ? 63.29918  40.39055  -2.80655  1.000 23.45749  ?  315 THR   C N   1 
ATOM   11107 C CA  . THR   G  1 315 ? 63.04562  40.27422  -4.23121  1.000 25.80910  ?  315 THR   C CA  1 
ATOM   11108 C C   . THR   G  1 315 ? 61.67477  40.85817  -4.59514  1.000 34.13957  ?  315 THR   C C   1 
ATOM   11109 O O   . THR   G  1 315 ? 60.82079  41.11392  -3.73909  1.000 26.32295  ?  315 THR   C O   1 
ATOM   11110 C CB  . THR   G  1 315 ? 63.12196  38.80660  -4.66704  1.000 25.43157  ?  315 THR   C CB  1 
ATOM   11111 O OG1 . THR   G  1 315 ? 62.01769  38.06347  -4.11212  1.000 19.21086  ?  315 THR   C OG1 1 
ATOM   11112 C CG2 . THR   G  1 315 ? 64.37102  38.19750  -4.15996  1.000 15.92287  ?  315 THR   C CG2 1 
ATOM   11113 N N   . TYR   G  1 316 ? 61.48369  41.05473  -5.89719  1.000 28.19850  ?  316 TYR   C N   1 
ATOM   11114 C CA  . TYR   G  1 316 ? 60.26904  41.45503  -6.60739  1.000 27.75830  ?  316 TYR   C CA  1 
ATOM   11115 C C   . TYR   G  1 316 ? 59.92664  40.48849  -7.73287  1.000 22.78324  ?  316 TYR   C C   1 
ATOM   11116 O O   . TYR   G  1 316 ? 58.74665  40.21763  -7.97461  1.000 32.64526  ?  316 TYR   C O   1 
ATOM   11117 C CB  . TYR   G  1 316 ? 60.41374  42.89516  -7.18861  1.000 22.70376  ?  316 TYR   C CB  1 
ATOM   11118 C CG  . TYR   G  1 316 ? 60.70778  43.91325  -6.12045  1.000 33.44994  ?  316 TYR   C CG  1 
ATOM   11119 C CD1 . TYR   G  1 316 ? 59.68004  44.43592  -5.32791  1.000 34.82909  ?  316 TYR   C CD1 1 
ATOM   11120 C CD2 . TYR   G  1 316 ? 62.01657  44.31324  -5.86278  1.000 27.54862  ?  316 TYR   C CD2 1 
ATOM   11121 C CE1 . TYR   G  1 316 ? 59.94124  45.35149  -4.31316  1.000 26.46782  ?  316 TYR   C CE1 1 
ATOM   11122 C CE2 . TYR   G  1 316 ? 62.30096  45.23365  -4.85466  1.000 19.73682  ?  316 TYR   C CE2 1 
ATOM   11123 C CZ  . TYR   G  1 316 ? 61.25908  45.74861  -4.08542  1.000 37.52114  ?  316 TYR   C CZ  1 
ATOM   11124 O OH  . TYR   G  1 316 ? 61.55049  46.65303  -3.08780  1.000 28.79447  ?  316 TYR   C OH  1 
ATOM   11125 N N   . PHE   G  1 317 ? 60.93352  39.94119  -8.42340  1.000 43.95718  ?  317 PHE   C N   1 
ATOM   11126 C CA  . PHE   G  1 317 ? 60.68907  39.19810  -9.65311  1.000 25.20682  ?  317 PHE   C CA  1 
ATOM   11127 C C   . PHE   G  1 317 ? 61.28693  37.79821  -9.61526  1.000 46.87670  ?  317 PHE   C C   1 
ATOM   11128 O O   . PHE   G  1 317 ? 61.57972  37.22406  -10.67394 1.000 34.80809  ?  317 PHE   C O   1 
ATOM   11129 C CB  . PHE   G  1 317 ? 61.22711  39.97508  -10.85432 1.000 25.08606  ?  317 PHE   C CB  1 
ATOM   11130 C CG  . PHE   G  1 317 ? 60.53894  41.29011  -11.06348 1.000 45.22916  ?  317 PHE   C CG  1 
ATOM   11131 C CD1 . PHE   G  1 317 ? 59.23205  41.32993  -11.53174 1.000 25.88641  ?  317 PHE   C CD1 1 
ATOM   11132 C CD2 . PHE   G  1 317 ? 61.18696  42.48504  -10.76558 1.000 40.99255  ?  317 PHE   C CD2 1 
ATOM   11133 C CE1 . PHE   G  1 317 ? 58.58624  42.53821  -11.72309 1.000 41.19543  ?  317 PHE   C CE1 1 
ATOM   11134 C CE2 . PHE   G  1 317 ? 60.54875  43.69303  -10.95048 1.000 33.78500  ?  317 PHE   C CE2 1 
ATOM   11135 C CZ  . PHE   G  1 317 ? 59.24076  43.71823  -11.42845 1.000 35.19162  ?  317 PHE   C CZ  1 
ATOM   11136 N N   . ALA   G  1 318 ? 61.45693  37.22617  -8.41630  1.000 31.10013  ?  318 ALA   C N   1 
ATOM   11137 C CA  . ALA   G  1 318 ? 62.04633  35.89459  -8.26641  1.000 27.97566  ?  318 ALA   C CA  1 
ATOM   11138 C C   . ALA   G  1 318 ? 60.94131  34.84963  -8.20403  1.000 32.79139  ?  318 ALA   C C   1 
ATOM   11139 O O   . ALA   G  1 318 ? 60.16448  34.82270  -7.24578  1.000 37.70820  ?  318 ALA   C O   1 
ATOM   11140 C CB  . ALA   G  1 318 ? 62.90862  35.82025  -7.00990  1.000 21.49761  ?  318 ALA   C CB  1 
ATOM   11141 N N   . GLN   G  1 319 ? 60.87580  33.97685  -9.21001  1.000 37.39883  ?  319 GLN   C N   1 
ATOM   11142 C CA  . GLN   G  1 319 ? 60.02324  32.80230  -9.09662  1.000 33.87996  ?  319 GLN   C CA  1 
ATOM   11143 C C   . GLN   G  1 319 ? 60.84852  31.64133  -8.54103  1.000 31.97511  ?  319 GLN   C C   1 
ATOM   11144 O O   . GLN   G  1 319 ? 62.06518  31.74835  -8.34944  1.000 46.24818  ?  319 GLN   C O   1 
ATOM   11145 C CB  . GLN   G  1 319 ? 59.38583  32.45095  -10.43859 1.000 33.36581  ?  319 GLN   C CB  1 
ATOM   11146 C CG  . GLN   G  1 319 ? 60.39564  32.04708  -11.47245 1.000 41.46827  ?  319 GLN   C CG  1 
ATOM   11147 C CD  . GLN   G  1 319 ? 59.78120  31.92574  -12.84607 1.000 30.48068  ?  319 GLN   C CD  1 
ATOM   11148 O OE1 . GLN   G  1 319 ? 59.47075  32.93246  -13.49709 1.000 53.80129  ?  319 GLN   C OE1 1 
ATOM   11149 N NE2 . GLN   G  1 319 ? 59.61572  30.69276  -13.30627 1.000 39.28789  ?  319 GLN   C NE2 1 
ATOM   11150 N N   . ALA   G  1 320 ? 60.18324  30.52485  -8.25709  1.000 37.98397  ?  320 ALA   C N   1 
ATOM   11151 C CA  . ALA   G  1 320 ? 60.89236  29.36137  -7.73110  1.000 38.72938  ?  320 ALA   C CA  1 
ATOM   11152 C C   . ALA   G  1 320 ? 61.77787  28.75383  -8.81963  1.000 38.47219  ?  320 ALA   C C   1 
ATOM   11153 O O   . ALA   G  1 320 ? 61.29586  28.49350  -9.93075  1.000 40.01039  ?  320 ALA   C O   1 
ATOM   11154 C CB  . ALA   G  1 320 ? 59.91011  28.32247  -7.20282  1.000 22.47188  ?  320 ALA   C CB  1 
ATOM   11155 N N   . PRO   G  1 321 ? 63.06000  28.49711  -8.53735  1.000 46.33135  ?  321 PRO   C N   1 
ATOM   11156 C CA  . PRO   G  1 321 ? 63.96112  27.96736  -9.57969  1.000 32.23031  ?  321 PRO   C CA  1 
ATOM   11157 C C   . PRO   G  1 321 ? 63.45964  26.67786  -10.22733 1.000 37.91558  ?  321 PRO   C C   1 
ATOM   11158 O O   . PRO   G  1 321 ? 63.66242  26.49098  -11.43381 1.000 42.68207  ?  321 PRO   C O   1 
ATOM   11159 C CB  . PRO   G  1 321 ? 65.28280  27.74968  -8.82394  1.000 25.42690  ?  321 PRO   C CB  1 
ATOM   11160 C CG  . PRO   G  1 321 ? 65.12838  28.43602  -7.49605  1.000 46.58704  ?  321 PRO   C CG  1 
ATOM   11161 C CD  . PRO   G  1 321 ? 63.66803  28.46931  -7.19585  1.000 28.87681  ?  321 PRO   C CD  1 
ATOM   11162 N N   . SER   G  1 322 ? 62.77699  25.80630  -9.46959  1.000 44.86284  ?  322 SER   C N   1 
ATOM   11163 C CA  . SER   G  1 322 ? 62.18667  24.58674  -10.02715 1.000 44.34507  ?  322 SER   C CA  1 
ATOM   11164 C C   . SER   G  1 322 ? 61.17016  24.85195  -11.13802 1.000 43.94905  ?  322 SER   C C   1 
ATOM   11165 O O   . SER   G  1 322 ? 60.87748  23.93371  -11.91415 1.000 63.32882  ?  322 SER   C O   1 
ATOM   11166 C CB  . SER   G  1 322 ? 61.50984  23.76250  -8.92032  1.000 35.40930  ?  322 SER   C CB  1 
ATOM   11167 O OG  . SER   G  1 322 ? 60.83487  24.58372  -7.97286  1.000 60.50164  ?  322 SER   C OG  1 
ATOM   11168 N N   . THR   G  1 323 ? 60.60173  26.06135  -11.22017 1.000 55.17539  ?  323 THR   C N   1 
ATOM   11169 C CA  . THR   G  1 323 ? 59.62156  26.38216  -12.25453 1.000 37.51970  ?  323 THR   C CA  1 
ATOM   11170 C C   . THR   G  1 323 ? 60.22886  27.09829  -13.44779 1.000 52.99430  ?  323 THR   C C   1 
ATOM   11171 O O   . THR   G  1 323 ? 59.50588  27.38259  -14.40399 1.000 35.90567  ?  323 THR   C O   1 
ATOM   11172 C CB  . THR   G  1 323 ? 58.48346  27.25269  -11.69652 1.000 44.25401  ?  323 THR   C CB  1 
ATOM   11173 O OG1 . THR   G  1 323 ? 58.92525  28.61616  -11.57387 1.000 45.78933  ?  323 THR   C OG1 1 
ATOM   11174 C CG2 . THR   G  1 323 ? 58.04582  26.75205  -10.34772 1.000 26.20428  ?  323 THR   C CG2 1 
ATOM   11175 N N   . ILE   G  1 324 ? 61.52252  27.41862  -13.41157 1.000 41.44062  ?  324 ILE   C N   1 
ATOM   11176 C CA  . ILE   G  1 324 ? 62.12573  28.15539  -14.51486 1.000 43.18642  ?  324 ILE   C CA  1 
ATOM   11177 C C   . ILE   G  1 324 ? 62.00776  27.32455  -15.78127 1.000 61.73593  ?  324 ILE   C C   1 
ATOM   11178 O O   . ILE   G  1 324 ? 62.44524  26.16730  -15.82725 1.000 54.40624  ?  324 ILE   C O   1 
ATOM   11179 C CB  . ILE   G  1 324 ? 63.57751  28.50217  -14.19809 1.000 31.19548  ?  324 ILE   C CB  1 
ATOM   11180 C CG1 . ILE   G  1 324 ? 63.62202  29.50707  -13.04797 1.000 44.57391  ?  324 ILE   C CG1 1 
ATOM   11181 C CG2 . ILE   G  1 324 ? 64.26667  29.05485  -15.44627 1.000 33.73791  ?  324 ILE   C CG2 1 
ATOM   11182 C CD1 . ILE   G  1 324 ? 64.99026  29.85653  -12.61697 1.000 38.07700  ?  324 ILE   C CD1 1 
ATOM   11183 N N   . GLY   G  1 325 ? 61.37751  27.89786  -16.80678 1.000 43.06879  ?  325 GLY   C N   1 
ATOM   11184 C CA  . GLY   G  1 325 ? 61.16472  27.20913  -18.06126 1.000 38.28842  ?  325 GLY   C CA  1 
ATOM   11185 C C   . GLY   G  1 325 ? 59.77282  26.63802  -18.27212 1.000 47.31936  ?  325 GLY   C C   1 
ATOM   11186 O O   . GLY   G  1 325 ? 59.41923  26.33961  -19.41853 1.000 52.49083  ?  325 GLY   C O   1 
ATOM   11187 N N   . ASP   G  1 326 ? 58.98845  26.45593  -17.20777 1.000 45.58164  ?  326 ASP   C N   1 
ATOM   11188 C CA  . ASP   G  1 326 ? 57.60822  26.00279  -17.34927 1.000 52.78600  ?  326 ASP   C CA  1 
ATOM   11189 C C   . ASP   G  1 326 ? 56.82307  26.91489  -18.29727 1.000 43.96047  ?  326 ASP   C C   1 
ATOM   11190 O O   . ASP   G  1 326 ? 57.14453  28.09821  -18.45417 1.000 54.32847  ?  326 ASP   C O   1 
ATOM   11191 C CB  . ASP   G  1 326 ? 56.90837  25.97480  -15.98997 1.000 35.21801  ?  326 ASP   C CB  1 
ATOM   11192 C CG  . ASP   G  1 326 ? 57.46548  24.91856  -15.05527 1.000 71.89076  ?  326 ASP   C CG  1 
ATOM   11193 O OD1 . ASP   G  1 326 ? 58.32118  24.10300  -15.48816 1.000 57.49187  ?  326 ASP   C OD1 1 
ATOM   11194 O OD2 . ASP   G  1 326 ? 57.02895  24.91655  -13.87609 1.000 60.08533  -1 326 ASP   C OD2 1 
ATOM   11195 N N   . PRO   G  1 327 ? 55.78074  26.39564  -18.93546 1.000 72.67187  ?  327 PRO   C N   1 
ATOM   11196 C CA  . PRO   G  1 327 ? 55.00611  27.22922  -19.86430 1.000 58.12922  ?  327 PRO   C CA  1 
ATOM   11197 C C   . PRO   G  1 327 ? 54.28762  28.37440  -19.15457 1.000 52.84769  ?  327 PRO   C C   1 
ATOM   11198 O O   . PRO   G  1 327 ? 53.78422  28.22203  -18.03883 1.000 65.83036  ?  327 PRO   C O   1 
ATOM   11199 C CB  . PRO   G  1 327 ? 54.01193  26.23686  -20.48386 1.000 38.02024  ?  327 PRO   C CB  1 
ATOM   11200 C CG  . PRO   G  1 327 ? 54.02093  25.03161  -19.59359 1.000 52.68929  ?  327 PRO   C CG  1 
ATOM   11201 C CD  . PRO   G  1 327 ? 55.38990  24.97449  -18.99052 1.000 55.60440  ?  327 PRO   C CD  1 
ATOM   11202 N N   . ILE   G  1 328 ? 54.25415  29.53214  -19.81116 1.000 48.79085  ?  328 ILE   C N   1 
ATOM   11203 C CA  . ILE   G  1 328 ? 53.44472  30.65709  -19.34221 1.000 48.59016  ?  328 ILE   C CA  1 
ATOM   11204 C C   . ILE   G  1 328 ? 52.11723  30.65807  -20.09143 1.000 50.88589  ?  328 ILE   C C   1 
ATOM   11205 O O   . ILE   G  1 328 ? 52.05724  31.13221  -21.23617 1.000 59.92678  ?  328 ILE   C O   1 
ATOM   11206 C CB  . ILE   G  1 328 ? 54.17346  32.00087  -19.51740 1.000 53.81504  ?  328 ILE   C CB  1 
ATOM   11207 C CG1 . ILE   G  1 328 ? 55.52930  31.97756  -18.80747 1.000 41.27164  ?  328 ILE   C CG1 1 
ATOM   11208 C CG2 . ILE   G  1 328 ? 53.33648  33.15203  -18.95904 1.000 42.99612  ?  328 ILE   C CG2 1 
ATOM   11209 C CD1 . ILE   G  1 328 ? 56.29802  33.29540  -18.91666 1.000 37.28143  ?  328 ILE   C CD1 1 
ATOM   11210 N N   . PRO   G  1 329 ? 51.03281  30.16820  -19.48313 1.000 67.10286  ?  329 PRO   C N   1 
ATOM   11211 C CA  . PRO   G  1 329 ? 49.76344  30.01803  -20.21143 1.000 52.57507  ?  329 PRO   C CA  1 
ATOM   11212 C C   . PRO   G  1 329 ? 49.26567  31.33982  -20.77725 1.000 54.82797  ?  329 PRO   C C   1 
ATOM   11213 O O   . PRO   G  1 329 ? 49.45924  32.40914  -20.18783 1.000 87.17833  ?  329 PRO   C O   1 
ATOM   11214 C CB  . PRO   G  1 329 ? 48.80192  29.46924  -19.15038 1.000 39.43587  ?  329 PRO   C CB  1 
ATOM   11215 C CG  . PRO   G  1 329 ? 49.70870  28.85966  -18.09194 1.000 50.14425  ?  329 PRO   C CG  1 
ATOM   11216 C CD  . PRO   G  1 329 ? 50.95408  29.67071  -18.10019 1.000 55.03550  ?  329 PRO   C CD  1 
ATOM   11217 N N   . ASP   G  1 330 ? 48.66239  31.25190  -21.96579 1.000 79.27219  ?  330 ASP   C N   1 
ATOM   11218 C CA  . ASP   G  1 330 ? 48.05542  32.39247  -22.64209 1.000 89.34411  ?  330 ASP   C CA  1 
ATOM   11219 C C   . ASP   G  1 330 ? 46.56309  32.54521  -22.34428 1.000 68.03741  ?  330 ASP   C C   1 
ATOM   11220 O O   . ASP   G  1 330 ? 45.85096  33.17990  -23.14418 1.000 96.76237  ?  330 ASP   C O   1 
ATOM   11221 C CB  . ASP   G  1 330 ? 48.29627  32.30094  -24.16107 1.000 60.57833  ?  330 ASP   C CB  1 
ATOM   11222 N N   . ASN   G  1 331 ? 46.10740  32.00976  -21.20620 1.000 86.55759  ?  331 ASN   C N   1 
ATOM   11223 C CA  . ASN   G  1 331 ? 44.73234  32.06824  -20.73659 1.000 86.68267  ?  331 ASN   C CA  1 
ATOM   11224 C C   . ASN   G  1 331 ? 44.74514  32.63348  -19.31848 1.000 69.35106  ?  331 ASN   C C   1 
ATOM   11225 O O   . ASN   G  1 331 ? 45.76488  33.14293  -18.87181 1.000 113.06100 ?  331 ASN   C O   1 
ATOM   11226 C CB  . ASN   G  1 331 ? 44.12115  30.67718  -20.80973 1.000 64.60695  ?  331 ASN   C CB  1 
ATOM   11227 C CG  . ASN   G  1 331 ? 44.72457  29.70378  -19.84963 1.000 75.69810  ?  331 ASN   C CG  1 
ATOM   11228 O OD1 . ASN   G  1 331 ? 44.88788  29.91307  -18.64738 1.000 145.21133 ?  331 ASN   C OD1 1 
ATOM   11229 N ND2 . ASN   G  1 331 ? 45.16962  28.62262  -20.43573 1.000 79.86783  ?  331 ASN   C ND2 1 
ATOM   11230 N N   . ASP   G  1 332 ? 43.67368  32.56773  -18.59011 1.000 111.30644 ?  332 ASP   C N   1 
ATOM   11231 C CA  . ASP   G  1 332 ? 43.58912  33.16941  -17.26154 1.000 93.94943  ?  332 ASP   C CA  1 
ATOM   11232 C C   . ASP   G  1 332 ? 43.04105  32.17424  -16.24431 1.000 94.15389  ?  332 ASP   C C   1 
ATOM   11233 O O   . ASP   G  1 332 ? 42.55239  32.57933  -15.18887 1.000 35.95014  ?  332 ASP   C O   1 
ATOM   11234 C CB  . ASP   G  1 332 ? 42.76904  34.47352  -17.29773 1.000 104.26070 ?  332 ASP   C CB  1 
ATOM   11235 N N   . TYR   G  1 333 ? 43.09617  30.87527  -16.56133 1.000 80.45531  ?  333 TYR   C N   1 
ATOM   11236 C CA  . TYR   G  1 333 ? 42.76994  29.87668  -15.55152 1.000 99.73281  ?  333 TYR   C CA  1 
ATOM   11237 C C   . TYR   G  1 333 ? 43.96178  29.02638  -15.12044 1.000 65.05160  ?  333 TYR   C C   1 
ATOM   11238 O O   . TYR   G  1 333 ? 44.01780  28.62066  -13.95591 1.000 84.26583  ?  333 TYR   C O   1 
ATOM   11239 C CB  . TYR   G  1 333 ? 41.62350  28.95157  -16.01124 1.000 122.95121 ?  333 TYR   C CB  1 
ATOM   11240 C CG  . TYR   G  1 333 ? 41.82881  28.25483  -17.33667 1.000 76.40686  ?  333 TYR   C CG  1 
ATOM   11241 C CD1 . TYR   G  1 333 ? 41.51524  28.89475  -18.52068 1.000 71.97081  ?  333 TYR   C CD1 1 
ATOM   11242 C CD2 . TYR   G  1 333 ? 42.34138  26.95421  -17.40411 1.000 66.81303  ?  333 TYR   C CD2 1 
ATOM   11243 C CE1 . TYR   G  1 333 ? 41.70120  28.26262  -19.74959 1.000 100.09589 ?  333 TYR   C CE1 1 
ATOM   11244 C CE2 . TYR   G  1 333 ? 42.54176  26.31347  -18.63494 1.000 99.30508  ?  333 TYR   C CE2 1 
ATOM   11245 C CZ  . TYR   G  1 333 ? 42.21116  26.97319  -19.80472 1.000 105.47930 ?  333 TYR   C CZ  1 
ATOM   11246 O OH  . TYR   G  1 333 ? 42.39731  26.34811  -21.02573 1.000 87.45688  ?  333 TYR   C OH  1 
ATOM   11247 N N   . ASP   G  1 334 ? 44.94333  28.77279  -16.04648 1.000 69.57660  ?  334 ASP   C N   1 
ATOM   11248 C CA  . ASP   G  1 334 ? 46.16684  28.05068  -15.69188 1.000 67.65132  ?  334 ASP   C CA  1 
ATOM   11249 C C   . ASP   G  1 334 ? 47.20620  28.97254  -15.06025 1.000 77.09169  ?  334 ASP   C C   1 
ATOM   11250 O O   . ASP   G  1 334 ? 47.56365  30.00513  -15.65376 1.000 42.81925  ?  334 ASP   C O   1 
ATOM   11251 C CB  . ASP   G  1 334 ? 46.77125  27.38078  -16.91499 1.000 96.45339  ?  334 ASP   C CB  1 
ATOM   11252 C CG  . ASP   G  1 334 ? 45.95533  26.20752  -17.38866 1.000 111.07471 ?  334 ASP   C CG  1 
ATOM   11253 O OD1 . ASP   G  1 334 ? 45.31754  25.53471  -16.53085 1.000 67.28035  ?  334 ASP   C OD1 1 
ATOM   11254 O OD2 . ASP   G  1 334 ? 45.95109  25.94122  -18.60621 1.000 78.60456  -1 334 ASP   C OD2 1 
ATOM   11255 N N   . PRO   G  1 335 ? 47.72065  28.62501  -13.88079 1.000 66.91107  ?  335 PRO   C N   1 
ATOM   11256 C CA  . PRO   G  1 335 ? 48.66944  29.50125  -13.19270 1.000 46.71753  ?  335 PRO   C CA  1 
ATOM   11257 C C   . PRO   G  1 335 ? 50.00740  29.51211  -13.89841 1.000 30.74706  ?  335 PRO   C C   1 
ATOM   11258 O O   . PRO   G  1 335 ? 50.55060  28.44911  -14.25715 1.000 59.68866  ?  335 PRO   C O   1 
ATOM   11259 C CB  . PRO   G  1 335 ? 48.78554  28.87018  -11.79666 1.000 52.49632  ?  335 PRO   C CB  1 
ATOM   11260 C CG  . PRO   G  1 335 ? 47.69306  27.83856  -11.72746 1.000 65.35695  ?  335 PRO   C CG  1 
ATOM   11261 C CD  . PRO   G  1 335 ? 47.42580  27.40961  -13.11461 1.000 38.93300  ?  335 PRO   C CD  1 
ATOM   11262 N N   . PRO   G  1 336 ? 50.58861  30.69391  -14.11423 1.000 55.60894  ?  336 PRO   C N   1 
ATOM   11263 C CA  . PRO   G  1 336 ? 51.95390  30.77953  -14.65757 1.000 20.02406  ?  336 PRO   C CA  1 
ATOM   11264 C C   . PRO   G  1 336 ? 52.98142  30.46220  -13.58022 1.000 86.31630  ?  336 PRO   C C   1 
ATOM   11265 O O   . PRO   G  1 336 ? 52.64149  30.35994  -12.38783 1.000 25.38255  ?  336 PRO   C O   1 
ATOM   11266 C CB  . PRO   G  1 336 ? 52.04334  32.23516  -15.13353 1.000 39.00710  ?  336 PRO   C CB  1 
ATOM   11267 C CG  . PRO   G  1 336 ? 51.11838  32.98297  -14.20928 1.000 35.98366  ?  336 PRO   C CG  1 
ATOM   11268 C CD  . PRO   G  1 336 ? 50.05339  32.01843  -13.73154 1.000 20.00670  ?  336 PRO   C CD  1 
ATOM   11269 N N   . PRO   G  1 337 ? 54.24982  30.26361  -13.95436 1.000 29.30676  ?  337 PRO   C N   1 
ATOM   11270 C CA  . PRO   G  1 337 ? 55.24265  29.80329  -12.95192 1.000 44.91824  ?  337 PRO   C CA  1 
ATOM   11271 C C   . PRO   G  1 337 ? 55.33968  30.68390  -11.70621 1.000 33.47181  ?  337 PRO   C C   1 
ATOM   11272 O O   . PRO   G  1 337 ? 55.39928  30.16081  -10.58527 1.000 31.31754  ?  337 PRO   C O   1 
ATOM   11273 C CB  . PRO   G  1 337 ? 56.55805  29.79799  -13.74096 1.000 31.44092  ?  337 PRO   C CB  1 
ATOM   11274 C CG  . PRO   G  1 337 ? 56.16513  29.68157  -15.15362 1.000 39.82361  ?  337 PRO   C CG  1 
ATOM   11275 C CD  . PRO   G  1 337 ? 54.83019  30.36865  -15.30100 1.000 48.49834  ?  337 PRO   C CD  1 
ATOM   11276 N N   . TYR   G  1 338 ? 55.32913  32.00864  -11.87096 1.000 33.10917  ?  338 TYR   C N   1 
ATOM   11277 C CA  . TYR   G  1 338 ? 55.38054  32.90461  -10.72071 1.000 35.69428  ?  338 TYR   C CA  1 
ATOM   11278 C C   . TYR   G  1 338 ? 54.24707  32.62826  -9.73558  1.000 29.50667  ?  338 TYR   C C   1 
ATOM   11279 O O   . TYR   G  1 338 ? 54.48181  32.55201  -8.52178  1.000 30.83480  ?  338 TYR   C O   1 
ATOM   11280 C CB  . TYR   G  1 338 ? 55.34809  34.35821  -11.19485 1.000 23.21202  ?  338 TYR   C CB  1 
ATOM   11281 C CG  . TYR   G  1 338 ? 55.57454  35.39195  -10.11090 1.000 36.28847  ?  338 TYR   C CG  1 
ATOM   11282 C CD1 . TYR   G  1 338 ? 56.73841  35.39192  -9.33446  1.000 29.01621  ?  338 TYR   C CD1 1 
ATOM   11283 C CD2 . TYR   G  1 338 ? 54.63750  36.38510  -9.88184  1.000 26.85672  ?  338 TYR   C CD2 1 
ATOM   11284 C CE1 . TYR   G  1 338 ? 56.94708  36.36340  -8.34819  1.000 31.72862  ?  338 TYR   C CE1 1 
ATOM   11285 C CE2 . TYR   G  1 338 ? 54.83301  37.34913  -8.90804  1.000 20.76531  ?  338 TYR   C CE2 1 
ATOM   11286 C CZ  . TYR   G  1 338 ? 55.97981  37.33566  -8.13952  1.000 41.01017  ?  338 TYR   C CZ  1 
ATOM   11287 O OH  . TYR   G  1 338 ? 56.14489  38.31027  -7.17710  1.000 29.55877  ?  338 TYR   C OH  1 
ATOM   11288 N N   . LEU   G  1 339 ? 53.00527  32.47890  -10.23011 1.000 38.72454  ?  339 LEU   C N   1 
ATOM   11289 C CA  . LEU   G  1 339 ? 51.89111  32.21404  -9.30616  1.000 29.88591  ?  339 LEU   C CA  1 
ATOM   11290 C C   . LEU   G  1 339 ? 51.88869  30.79239  -8.75836  1.000 41.87103  ?  339 LEU   C C   1 
ATOM   11291 O O   . LEU   G  1 339 ? 51.04971  30.48709  -7.90409  1.000 43.56259  ?  339 LEU   C O   1 
ATOM   11292 C CB  . LEU   G  1 339 ? 50.54057  32.49869  -9.96167  1.000 30.70895  ?  339 LEU   C CB  1 
ATOM   11293 C CG  . LEU   G  1 339 ? 50.38299  33.97717  -10.34571 1.000 52.72421  ?  339 LEU   C CG  1 
ATOM   11294 C CD1 . LEU   G  1 339 ? 48.99023  34.26219  -10.86373 1.000 36.54972  ?  339 LEU   C CD1 1 
ATOM   11295 C CD2 . LEU   G  1 339 ? 50.69936  34.88127  -9.17443  1.000 37.90376  ?  339 LEU   C CD2 1 
ATOM   11296 N N   . LYS   G  1 340 ? 52.79063  29.92184  -9.21331  1.000 30.09765  ?  340 LYS   C N   1 
ATOM   11297 C CA  . LYS   G  1 340 ? 53.05561  28.66195  -8.53018  1.000 49.91629  ?  340 LYS   C CA  1 
ATOM   11298 C C   . LYS   G  1 340 ? 54.24997  28.74389  -7.56678  1.000 32.12829  ?  340 LYS   C C   1 
ATOM   11299 O O   . LYS   G  1 340 ? 54.71617  27.70330  -7.09848  1.000 38.51959  ?  340 LYS   C O   1 
ATOM   11300 C CB  . LYS   G  1 340 ? 53.28377  27.54326  -9.55253  1.000 32.77834  ?  340 LYS   C CB  1 
ATOM   11301 C CG  . LYS   G  1 340 ? 52.16258  27.33404  -10.57232 1.000 46.80307  ?  340 LYS   C CG  1 
ATOM   11302 C CD  . LYS   G  1 340 ? 52.46652  26.16407  -11.48050 1.000 113.61975 ?  340 LYS   C CD  1 
ATOM   11303 C CE  . LYS   G  1 340 ? 51.46347  25.03272  -11.31860 1.000 117.28980 ?  340 LYS   C CE  1 
ATOM   11304 N NZ  . LYS   G  1 340 ? 51.94290  23.80217  -12.02963 1.000 59.53904  ?  340 LYS   C NZ  1 
ATOM   11305 N N   . SER   G  1 341 ? 54.73399  29.95568  -7.24065  1.000 31.72778  ?  341 SER   C N   1 
ATOM   11306 C CA  . SER   G  1 341 ? 55.95666  30.15164  -6.46524  1.000 24.88284  ?  341 SER   C CA  1 
ATOM   11307 C C   . SER   G  1 341 ? 55.75565  30.84532  -5.11738  1.000 29.76846  ?  341 SER   C C   1 
ATOM   11308 O O   . SER   G  1 341 ? 56.75344  31.16075  -4.44750  1.000 40.31712  ?  341 SER   C O   1 
ATOM   11309 C CB  . SER   G  1 341 ? 56.97255  30.97176  -7.28138  1.000 31.42842  ?  341 SER   C CB  1 
ATOM   11310 O OG  . SER   G  1 341 ? 57.38485  30.29929  -8.45783  1.000 31.19032  ?  341 SER   C OG  1 
ATOM   11311 N N   . LEU   G  1 342 ? 54.51244  31.09218  -4.69927  1.000 29.67261  ?  342 LEU   C N   1 
ATOM   11312 C CA  . LEU   G  1 342 ? 54.26967  31.97230  -3.55850  1.000 40.86187  ?  342 LEU   C CA  1 
ATOM   11313 C C   . LEU   G  1 342 ? 54.89561  31.43822  -2.27388  1.000 29.46435  ?  342 LEU   C C   1 
ATOM   11314 O O   . LEU   G  1 342 ? 55.36928  32.21984  -1.44185  1.000 35.38076  ?  342 LEU   C O   1 
ATOM   11315 C CB  . LEU   G  1 342 ? 52.77082  32.18490  -3.35387  1.000 23.72733  ?  342 LEU   C CB  1 
ATOM   11316 C CG  . LEU   G  1 342 ? 52.12792  33.38703  -4.03184  1.000 41.99348  ?  342 LEU   C CG  1 
ATOM   11317 C CD1 . LEU   G  1 342 ? 52.21019  33.25632  -5.55380  1.000 22.17040  ?  342 LEU   C CD1 1 
ATOM   11318 C CD2 . LEU   G  1 342 ? 50.67036  33.51142  -3.55064  1.000 17.78158  ?  342 LEU   C CD2 1 
ATOM   11319 N N   . VAL   G  1 343 ? 54.89328  30.12043  -2.06601  1.000 36.51673  ?  343 VAL   C N   1 
ATOM   11320 C CA  . VAL   G  1 343 ? 55.53848  29.61756  -0.85559  1.000 30.81079  ?  343 VAL   C CA  1 
ATOM   11321 C C   . VAL   G  1 343 ? 57.03700  29.87317  -0.92166  1.000 43.72492  ?  343 VAL   C C   1 
ATOM   11322 O O   . VAL   G  1 343 ? 57.63239  30.39871  0.02526   1.000 28.05345  ?  343 VAL   C O   1 
ATOM   11323 C CB  . VAL   G  1 343 ? 55.22898  28.12766  -0.62705  1.000 31.69143  ?  343 VAL   C CB  1 
ATOM   11324 C CG1 . VAL   G  1 343 ? 56.11296  27.57940  0.49265   1.000 17.90677  ?  343 VAL   C CG1 1 
ATOM   11325 C CG2 . VAL   G  1 343 ? 53.77281  27.95053  -0.24157  1.000 25.25444  ?  343 VAL   C CG2 1 
ATOM   11326 N N   . TYR   G  1 344 ? 57.65601  29.54929  -2.05851  1.000 19.93393  ?  344 TYR   C N   1 
ATOM   11327 C CA  . TYR   G  1 344 ? 59.08928  29.76846  -2.21852  1.000 37.38971  ?  344 TYR   C CA  1 
ATOM   11328 C C   . TYR   G  1 344 ? 59.48184  31.20902  -1.91043  1.000 38.92290  ?  344 TYR   C C   1 
ATOM   11329 O O   . TYR   G  1 344 ? 60.34737  31.45228  -1.06340  1.000 28.90798  ?  344 TYR   C O   1 
ATOM   11330 C CB  . TYR   G  1 344 ? 59.53643  29.39524  -3.63321  1.000 24.29039  ?  344 TYR   C CB  1 
ATOM   11331 C CG  . TYR   G  1 344 ? 60.98643  29.73302  -3.91359  1.000 44.67499  ?  344 TYR   C CG  1 
ATOM   11332 C CD1 . TYR   G  1 344 ? 62.00846  28.88547  -3.50098  1.000 27.42659  ?  344 TYR   C CD1 1 
ATOM   11333 C CD2 . TYR   G  1 344 ? 61.33529  30.90062  -4.58723  1.000 36.65226  ?  344 TYR   C CD2 1 
ATOM   11334 C CE1 . TYR   G  1 344 ? 63.34199  29.18588  -3.74854  1.000 27.62566  ?  344 TYR   C CE1 1 
ATOM   11335 C CE2 . TYR   G  1 344 ? 62.67370  31.21568  -4.84595  1.000 26.72290  ?  344 TYR   C CE2 1 
ATOM   11336 C CZ  . TYR   G  1 344 ? 63.66449  30.35208  -4.42358  1.000 44.99260  ?  344 TYR   C CZ  1 
ATOM   11337 O OH  . TYR   G  1 344 ? 64.97994  30.64595  -4.67907  1.000 40.03206  ?  344 TYR   C OH  1 
ATOM   11338 N N   . PHE   G  1 345 ? 58.85980  32.18368  -2.59134  1.000 19.60561  ?  345 PHE   C N   1 
ATOM   11339 C CA  . PHE   G  1 345 ? 59.38600  33.54354  -2.50057  1.000 28.65395  ?  345 PHE   C CA  1 
ATOM   11340 C C   . PHE   G  1 345 ? 58.87498  34.30444  -1.28098  1.000 33.83333  ?  345 PHE   C C   1 
ATOM   11341 O O   . PHE   G  1 345 ? 59.36498  35.40781  -1.00987  1.000 30.17650  ?  345 PHE   C O   1 
ATOM   11342 C CB  . PHE   G  1 345 ? 59.15955  34.34367  -3.81456  1.000 19.15497  ?  345 PHE   C CB  1 
ATOM   11343 C CG  . PHE   G  1 345 ? 57.71330  34.68668  -4.15471  1.000 32.36002  ?  345 PHE   C CG  1 
ATOM   11344 C CD1 . PHE   G  1 345 ? 56.96128  35.55355  -3.37020  1.000 37.57013  ?  345 PHE   C CD1 1 
ATOM   11345 C CD2 . PHE   G  1 345 ? 57.15065  34.22511  -5.34187  1.000 25.90866  ?  345 PHE   C CD2 1 
ATOM   11346 C CE1 . PHE   G  1 345 ? 55.64387  35.88760  -3.72756  1.000 21.75307  ?  345 PHE   C CE1 1 
ATOM   11347 C CE2 . PHE   G  1 345 ? 55.83514  34.55522  -5.71716  1.000 27.37580  ?  345 PHE   C CE2 1 
ATOM   11348 C CZ  . PHE   G  1 345 ? 55.08007  35.38587  -4.91277  1.000 29.67354  ?  345 PHE   C CZ  1 
ATOM   11349 N N   . SER   G  1 346 ? 57.96135  33.72671  -0.50188  1.000 18.23288  ?  346 SER   C N   1 
ATOM   11350 C CA  . SER   G  1 346 ? 57.70438  34.27494  0.82409   1.000 40.44015  ?  346 SER   C CA  1 
ATOM   11351 C C   . SER   G  1 346 ? 58.98660  34.30451  1.64770   1.000 27.81218  ?  346 SER   C C   1 
ATOM   11352 O O   . SER   G  1 346 ? 59.13138  35.13863  2.55177   1.000 27.81510  ?  346 SER   C O   1 
ATOM   11353 C CB  . SER   G  1 346 ? 56.63555  33.45128  1.53936   1.000 27.21766  ?  346 SER   C CB  1 
ATOM   11354 O OG  . SER   G  1 346 ? 57.19101  32.22837  2.00128   1.000 23.82412  ?  346 SER   C OG  1 
ATOM   11355 N N   . ASN   G  1 347 ? 59.93719  33.41727  1.32451   1.000 34.06114  ?  347 ASN   C N   1 
ATOM   11356 C CA  . ASN   G  1 347 ? 61.21173  33.36989  2.03267   1.000 15.16228  ?  347 ASN   C CA  1 
ATOM   11357 C C   . ASN   G  1 347 ? 62.10937  34.56395  1.71597   1.000 32.03416  ?  347 ASN   C C   1 
ATOM   11358 O O   . ASN   G  1 347 ? 62.95118  34.93074  2.54808   1.000 32.37671  ?  347 ASN   C O   1 
ATOM   11359 C CB  . ASN   G  1 347 ? 61.94622  32.06969  1.69850   1.000 22.68239  ?  347 ASN   C CB  1 
ATOM   11360 C CG  . ASN   G  1 347 ? 61.23750  30.84651  2.23806   1.000 37.82779  ?  347 ASN   C CG  1 
ATOM   11361 O OD1 . ASN   G  1 347 ? 61.06574  30.69283  3.45311   1.000 28.96315  ?  347 ASN   C OD1 1 
ATOM   11362 N ND2 . ASN   G  1 347 ? 60.83079  29.96046  1.34121   1.000 19.69433  ?  347 ASN   C ND2 1 
ATOM   11363 N N   . ILE   G  1 348 ? 61.95839  35.17958  0.53531   1.000 20.28301  ?  348 ILE   C N   1 
ATOM   11364 C CA  . ILE   G  1 348 ? 62.96337  36.13474  0.06174   1.000 13.27839  ?  348 ILE   C CA  1 
ATOM   11365 C C   . ILE   G  1 348 ? 62.39084  37.45170  -0.46490  1.000 24.35771  ?  348 ILE   C C   1 
ATOM   11366 O O   . ILE   G  1 348 ? 63.14187  38.40347  -0.71028  1.000 27.82930  ?  348 ILE   C O   1 
ATOM   11367 C CB  . ILE   G  1 348 ? 63.83419  35.47525  -1.01942  1.000 22.26196  ?  348 ILE   C CB  1 
ATOM   11368 C CG1 . ILE   G  1 348 ? 62.95022  34.99251  -2.17253  1.000 10.79240  ?  348 ILE   C CG1 1 
ATOM   11369 C CG2 . ILE   G  1 348 ? 64.64762  34.32438  -0.42116  1.000 8.69909   ?  348 ILE   C CG2 1 
ATOM   11370 C CD1 . ILE   G  1 348 ? 63.75180  34.59039  -3.40263  1.000 33.34671  ?  348 ILE   C CD1 1 
ATOM   11371 N N   . ALA   G  1 349 ? 61.07727  37.52222  -0.65954  1.000 26.91629  ?  349 ALA   C N   1 
ATOM   11372 C CA  . ALA   G  1 349 ? 60.48407  38.72141  -1.24161  1.000 27.37906  ?  349 ALA   C CA  1 
ATOM   11373 C C   . ALA   G  1 349 ? 60.46991  39.87316  -0.24032  1.000 30.56104  ?  349 ALA   C C   1 
ATOM   11374 O O   . ALA   G  1 349 ? 60.41374  39.66915  0.97950   1.000 35.49685  ?  349 ALA   C O   1 
ATOM   11375 C CB  . ALA   G  1 349 ? 59.04936  38.44743  -1.70418  1.000 12.57973  ?  349 ALA   C CB  1 
ATOM   11376 N N   . ALA   G  1 350 ? 60.51607  41.09812  -0.76667  1.000 21.02858  ?  350 ALA   C N   1 
ATOM   11377 C CA  . ALA   G  1 350 ? 60.22479  42.26372  0.06233   1.000 23.51495  ?  350 ALA   C CA  1 
ATOM   11378 C C   . ALA   G  1 350 ? 58.92273  42.04911  0.83192   1.000 29.45424  ?  350 ALA   C C   1 
ATOM   11379 O O   . ALA   G  1 350 ? 57.88370  41.72218  0.24852   1.000 22.98383  ?  350 ALA   C O   1 
ATOM   11380 C CB  . ALA   G  1 350 ? 60.12403  43.51090  -0.80796  1.000 9.38857   ?  350 ALA   C CB  1 
ATOM   11381 N N   . ARG   G  1 351 ? 58.98905  42.21584  2.14796   1.000 19.26475  ?  351 ARG   C N   1 
ATOM   11382 C CA  . ARG   G  1 351 ? 57.90871  41.76176  3.00767   1.000 29.51890  ?  351 ARG   C CA  1 
ATOM   11383 C C   . ARG   G  1 351 ? 57.99548  42.48508  4.34361   1.000 21.85576  ?  351 ARG   C C   1 
ATOM   11384 O O   . ARG   G  1 351 ? 59.02930  43.07253  4.69498   1.000 36.09108  ?  351 ARG   C O   1 
ATOM   11385 C CB  . ARG   G  1 351 ? 57.95946  40.23310  3.20031   1.000 15.23904  ?  351 ARG   C CB  1 
ATOM   11386 C CG  . ARG   G  1 351 ? 59.20641  39.74590  3.90420   1.000 15.24478  ?  351 ARG   C CG  1 
ATOM   11387 C CD  . ARG   G  1 351 ? 59.43472  38.25918  3.68440   1.000 23.15987  ?  351 ARG   C CD  1 
ATOM   11388 N NE  . ARG   G  1 351 ? 60.59614  37.77877  4.42592   1.000 24.72396  ?  351 ARG   C NE  1 
ATOM   11389 C CZ  . ARG   G  1 351 ? 61.85539  37.90980  4.02263   1.000 46.24542  ?  351 ARG   C CZ  1 
ATOM   11390 N NH1 . ARG   G  1 351 ? 62.16649  38.50300  2.87836   1.000 24.99429  ?  351 ARG   C NH1 1 
ATOM   11391 N NH2 . ARG   G  1 351 ? 62.83114  37.42937  4.78513   1.000 20.36122  ?  351 ARG   C NH2 1 
ATOM   11392 N N   . GLN   G  1 352 ? 56.87999  42.45472  5.07490   1.000 26.83702  ?  352 GLN   C N   1 
ATOM   11393 C CA  . GLN   G  1 352 ? 56.83193  42.96745  6.43810   1.000 20.19667  ?  352 GLN   C CA  1 
ATOM   11394 C C   . GLN   G  1 352 ? 56.38223  41.84832  7.35966   1.000 32.37290  ?  352 GLN   C C   1 
ATOM   11395 O O   . GLN   G  1 352 ? 55.40010  41.14977  7.06734   1.000 31.25155  ?  352 GLN   C O   1 
ATOM   11396 C CB  . GLN   G  1 352 ? 55.89649  44.15863  6.57889   1.000 30.36168  ?  352 GLN   C CB  1 
ATOM   11397 C CG  . GLN   G  1 352 ? 55.79319  44.65718  8.01133   1.000 25.41519  ?  352 GLN   C CG  1 
ATOM   11398 C CD  . GLN   G  1 352 ? 54.76626  45.77204  8.14532   1.000 33.76151  ?  352 GLN   C CD  1 
ATOM   11399 O OE1 . GLN   G  1 352 ? 53.66988  45.56202  8.65882   1.000 35.82044  ?  352 GLN   C OE1 1 
ATOM   11400 N NE2 . GLN   G  1 352 ? 55.11470  46.95991  7.66651   1.000 22.92669  ?  352 GLN   C NE2 1 
ATOM   11401 N N   . ILE   G  1 353 ? 57.13771  41.65123  8.43644   1.000 24.35099  ?  353 ILE   C N   1 
ATOM   11402 C CA  . ILE   G  1 353 ? 56.85330  40.64401  9.45125   1.000 27.17400  ?  353 ILE   C CA  1 
ATOM   11403 C C   . ILE   G  1 353 ? 56.21731  41.35716  10.62780  1.000 20.19096  ?  353 ILE   C C   1 
ATOM   11404 O O   . ILE   G  1 353 ? 56.72934  42.39223  11.08028  1.000 34.28127  ?  353 ILE   C O   1 
ATOM   11405 C CB  . ILE   G  1 353 ? 58.13863  39.93028  9.90010   1.000 25.07603  ?  353 ILE   C CB  1 
ATOM   11406 C CG1 . ILE   G  1 353 ? 58.82860  39.23885  8.72012   1.000 32.31783  ?  353 ILE   C CG1 1 
ATOM   11407 C CG2 . ILE   G  1 353 ? 57.83444  38.99439  11.06645  1.000 15.93964  ?  353 ILE   C CG2 1 
ATOM   11408 C CD1 . ILE   G  1 353 ? 60.30406  39.01812  8.94424   1.000 12.48919  ?  353 ILE   C CD1 1 
ATOM   11409 N N   . MET   G  1 354 ? 55.11038  40.82322  11.13133  1.000 20.38781  ?  354 MET   C N   1 
ATOM   11410 C CA  . MET   G  1 354 ? 54.44185  41.42827  12.27863  1.000 25.69461  ?  354 MET   C CA  1 
ATOM   11411 C C   . MET   G  1 354 ? 54.16073  40.34925  13.31448  1.000 30.78900  ?  354 MET   C C   1 
ATOM   11412 O O   . MET   G  1 354 ? 53.47426  39.36295  13.01774  1.000 32.25919  ?  354 MET   C O   1 
ATOM   11413 C CB  . MET   G  1 354 ? 53.15881  42.13612  11.84841  1.000 14.71073  ?  354 MET   C CB  1 
ATOM   11414 C CG  . MET   G  1 354 ? 52.51482  42.99895  12.92417  1.000 36.55319  ?  354 MET   C CG  1 
ATOM   11415 S SD  . MET   G  1 354 ? 51.00927  43.77395  12.31341  1.000 33.79217  ?  354 MET   C SD  1 
ATOM   11416 C CE  . MET   G  1 354 ? 51.72732  45.03610  11.25279  1.000 31.99855  ?  354 MET   C CE  1 
ATOM   11417 N N   . PHE   G  1 355 ? 54.72305  40.51281  14.51290  1.000 29.34633  ?  355 PHE   C N   1 
ATOM   11418 C CA  . PHE   G  1 355 ? 54.48136  39.59510  15.62370  1.000 30.97735  ?  355 PHE   C CA  1 
ATOM   11419 C C   . PHE   G  1 355 ? 53.39598  40.16687  16.51957  1.000 29.71713  ?  355 PHE   C C   1 
ATOM   11420 O O   . PHE   G  1 355 ? 53.45832  41.34112  16.90824  1.000 34.32821  ?  355 PHE   C O   1 
ATOM   11421 C CB  . PHE   G  1 355 ? 55.75627  39.35964  16.43389  1.000 34.83552  ?  355 PHE   C CB  1 
ATOM   11422 C CG  . PHE   G  1 355 ? 56.77897  38.57418  15.70224  1.000 36.69493  ?  355 PHE   C CG  1 
ATOM   11423 C CD1 . PHE   G  1 355 ? 56.65536  37.19683  15.59714  1.000 23.73831  ?  355 PHE   C CD1 1 
ATOM   11424 C CD2 . PHE   G  1 355 ? 57.84977  39.20488  15.09747  1.000 32.43248  ?  355 PHE   C CD2 1 
ATOM   11425 C CE1 . PHE   G  1 355 ? 57.59307  36.44613  14.90975  1.000 36.61639  ?  355 PHE   C CE1 1 
ATOM   11426 C CE2 . PHE   G  1 355 ? 58.79175  38.46766  14.40962  1.000 19.59727  ?  355 PHE   C CE2 1 
ATOM   11427 C CZ  . PHE   G  1 355 ? 58.66814  37.07937  14.31940  1.000 21.15598  ?  355 PHE   C CZ  1 
ATOM   11428 N N   . ILE   G  1 356 ? 52.40061  39.35109  16.84019  1.000 26.87432  ?  356 ILE   C N   1 
ATOM   11429 C CA  . ILE   G  1 356 ? 51.30029  39.79605  17.68405  1.000 30.23349  ?  356 ILE   C CA  1 
ATOM   11430 C C   . ILE   G  1 356 ? 51.16787  38.85143  18.86208  1.000 43.17396  ?  356 ILE   C C   1 
ATOM   11431 O O   . ILE   G  1 356 ? 51.25881  37.62683  18.69962  1.000 29.91418  ?  356 ILE   C O   1 
ATOM   11432 C CB  . ILE   G  1 356 ? 49.97737  39.88670  16.90356  1.000 24.31454  ?  356 ILE   C CB  1 
ATOM   11433 C CG1 . ILE   G  1 356 ? 50.14364  40.88097  15.73863  1.000 23.61486  ?  356 ILE   C CG1 1 
ATOM   11434 C CG2 . ILE   G  1 356 ? 48.84680  40.28579  17.85954  1.000 27.35321  ?  356 ILE   C CG2 1 
ATOM   11435 C CD1 . ILE   G  1 356 ? 48.93909  40.95249  14.79453  1.000 17.71989  ?  356 ILE   C CD1 1 
ATOM   11436 N N   . GLU   G  1 357 ? 50.97059  39.42473  20.05395  1.000 25.41685  ?  357 GLU   C N   1 
ATOM   11437 C CA  . GLU   G  1 357 ? 50.67970  38.64187  21.25149  1.000 40.40960  ?  357 GLU   C CA  1 
ATOM   11438 C C   . GLU   G  1 357 ? 49.16690  38.64806  21.49156  1.000 38.61548  ?  357 GLU   C C   1 
ATOM   11439 O O   . GLU   G  1 357 ? 48.60184  39.65467  21.94458  1.000 37.30346  ?  357 GLU   C O   1 
ATOM   11440 C CB  . GLU   G  1 357 ? 51.44288  39.18932  22.45082  1.000 30.92486  ?  357 GLU   C CB  1 
ATOM   11441 C CG  . GLU   G  1 357 ? 51.19969  38.42143  23.75571  1.000 29.70490  ?  357 GLU   C CG  1 
ATOM   11442 C CD  . GLU   G  1 357 ? 51.93847  37.09168  23.83212  1.000 83.00486  ?  357 GLU   C CD  1 
ATOM   11443 O OE1 . GLU   G  1 357 ? 53.12905  37.04100  23.43212  1.000 65.53424  ?  357 GLU   C OE1 1 
ATOM   11444 O OE2 . GLU   G  1 357 ? 51.32955  36.10123  24.31128  1.000 52.61348  -1 357 GLU   C OE2 1 
ATOM   11445 N N   . ALA   G  1 358 ? 48.52053  37.52162  21.17138  1.000 24.28723  ?  358 ALA   C N   1 
ATOM   11446 C CA  . ALA   G  1 358 ? 47.08015  37.36722  21.35740  1.000 43.14890  ?  358 ALA   C CA  1 
ATOM   11447 C C   . ALA   G  1 358 ? 46.71335  37.49569  22.82564  1.000 37.57647  ?  358 ALA   C C   1 
ATOM   11448 O O   . ALA   G  1 358 ? 47.39827  36.95205  23.69674  1.000 63.57114  ?  358 ALA   C O   1 
ATOM   11449 C CB  . ALA   G  1 358 ? 46.61560  36.00049  20.84571  1.000 31.78935  ?  358 ALA   C CB  1 
ATOM   11450 N N   . ASP   G  1 359 ? 45.62100  38.21972  23.09561  1.000 49.93167  ?  359 ASP   C N   1 
ATOM   11451 C CA  . ASP   G  1 359 ? 45.11235  38.31420  24.46374  1.000 45.24314  ?  359 ASP   C CA  1 
ATOM   11452 C C   . ASP   G  1 359 ? 44.82485  36.93016  25.04012  1.000 27.39629  ?  359 ASP   C C   1 
ATOM   11453 O O   . ASP   G  1 359 ? 45.05295  36.68218  26.22991  1.000 34.15981  ?  359 ASP   C O   1 
ATOM   11454 C CB  . ASP   G  1 359 ? 43.85083  39.18651  24.51683  1.000 24.30641  ?  359 ASP   C CB  1 
ATOM   11455 C CG  . ASP   G  1 359 ? 44.12831  40.66477  24.20966  1.000 61.59553  ?  359 ASP   C CG  1 
ATOM   11456 O OD1 . ASP   G  1 359 ? 45.31299  41.07254  24.21384  1.000 41.62004  ?  359 ASP   C OD1 1 
ATOM   11457 O OD2 . ASP   G  1 359 ? 43.15583  41.41850  23.94270  1.000 35.33036  -1 359 ASP   C OD2 1 
ATOM   11458 N N   . ASN   G  1 360 ? 44.34095  36.01265  24.21557  1.000 32.35672  ?  360 ASN   C N   1 
ATOM   11459 C CA  . ASN   G  1 360 ? 44.08915  34.65078  24.67127  1.000 23.60875  ?  360 ASN   C CA  1 
ATOM   11460 C C   . ASN   G  1 360 ? 45.41979  33.90719  24.78709  1.000 34.57378  ?  360 ASN   C C   1 
ATOM   11461 O O   . ASN   G  1 360 ? 46.05141  33.58826  23.77046  1.000 45.24658  ?  360 ASN   C O   1 
ATOM   11462 C CB  . ASN   G  1 360 ? 43.13570  33.94522  23.70860  1.000 24.88929  ?  360 ASN   C CB  1 
ATOM   11463 C CG  . ASN   G  1 360 ? 42.64935  32.63212  24.24467  1.000 43.67524  ?  360 ASN   C CG  1 
ATOM   11464 O OD1 . ASN   G  1 360 ? 43.42800  31.83783  24.78572  1.000 46.77960  ?  360 ASN   C OD1 1 
ATOM   11465 N ND2 . ASN   G  1 360 ? 41.34606  32.39179  24.11702  1.000 49.63826  ?  360 ASN   C ND2 1 
ATOM   11466 N N   . LYS   G  1 361 ? 45.82879  33.60453  26.02478  1.000 40.73367  ?  361 LYS   C N   1 
ATOM   11467 C CA  . LYS   G  1 361 ? 47.12338  32.97167  26.26849  1.000 48.50254  ?  361 LYS   C CA  1 
ATOM   11468 C C   . LYS   G  1 361 ? 47.26333  31.62250  25.56964  1.000 20.81965  ?  361 LYS   C C   1 
ATOM   11469 O O   . LYS   G  1 361 ? 48.39216  31.20104  25.28332  1.000 71.20294  ?  361 LYS   C O   1 
ATOM   11470 C CB  . LYS   G  1 361 ? 47.35630  32.81505  27.77685  1.000 24.97619  ?  361 LYS   C CB  1 
ATOM   11471 N N   . GLU   G  1 362 ? 46.15211  30.95091  25.26803  1.000 31.30987  ?  362 GLU   C N   1 
ATOM   11472 C CA  . GLU   G  1 362 ? 46.19135  29.67461  24.55914  1.000 26.77348  ?  362 GLU   C CA  1 
ATOM   11473 C C   . GLU   G  1 362 ? 46.51661  29.83180  23.07741  1.000 47.05572  ?  362 GLU   C C   1 
ATOM   11474 O O   . GLU   G  1 362 ? 46.78547  28.82686  22.40292  1.000 39.31821  ?  362 GLU   C O   1 
ATOM   11475 C CB  . GLU   G  1 362 ? 44.85186  28.93917  24.71530  1.000 35.63206  ?  362 GLU   C CB  1 
ATOM   11476 C CG  . GLU   G  1 362 ? 44.88278  27.90112  25.80844  1.000 32.67165  ?  362 GLU   C CG  1 
ATOM   11477 C CD  . GLU   G  1 362 ? 43.53896  27.30829  26.01941  1.000 116.99463 ?  362 GLU   C CD  1 
ATOM   11478 O OE1 . GLU   G  1 362 ? 42.68950  28.02231  26.60446  1.000 116.54878 ?  362 GLU   C OE1 1 
ATOM   11479 O OE2 . GLU   G  1 362 ? 43.31917  26.16577  25.54421  1.000 107.31554 ?  362 GLU   C OE2 1 
ATOM   11480 N N   . ILE   G  1 363 ? 46.45518  31.05457  22.55654  1.000 36.64321  ?  363 ILE   C N   1 
ATOM   11481 C CA  . ILE   G  1 363 ? 46.89218  31.36514  21.20530  1.000 54.61121  ?  363 ILE   C CA  1 
ATOM   11482 C C   . ILE   G  1 363 ? 48.27665  31.99840  21.22223  1.000 43.10270  ?  363 ILE   C C   1 
ATOM   11483 O O   . ILE   G  1 363 ? 49.16525  31.60130  20.46541  1.000 51.45583  ?  363 ILE   C O   1 
ATOM   11484 C CB  . ILE   G  1 363 ? 45.84010  32.27710  20.52571  1.000 44.84770  ?  363 ILE   C CB  1 
ATOM   11485 C CG1 . ILE   G  1 363 ? 44.56049  31.48774  20.23171  1.000 38.75503  ?  363 ILE   C CG1 1 
ATOM   11486 C CG2 . ILE   G  1 363 ? 46.35894  32.86036  19.22793  1.000 24.63090  ?  363 ILE   C CG2 1 
ATOM   11487 C CD1 . ILE   G  1 363 ? 43.43328  32.33591  19.64779  1.000 42.15654  ?  363 ILE   C CD1 1 
ATOM   11488 N N   . GLY   G  1 364 ? 48.47021  32.95146  22.12504  1.000 35.52408  ?  364 GLY   C N   1 
ATOM   11489 C CA  . GLY   G  1 364 ? 49.77865  33.43929  22.43758  1.000 23.41983  ?  364 GLY   C CA  1 
ATOM   11490 C C   . GLY   G  1 364 ? 50.40705  34.22738  21.30668  1.000 68.66276  ?  364 GLY   C C   1 
ATOM   11491 O O   . GLY   G  1 364 ? 49.75124  35.00285  20.59718  1.000 33.25355  ?  364 GLY   C O   1 
ATOM   11492 N N   . LEU   G  1 365 ? 51.71415  34.03278  21.15536  1.000 41.06762  ?  365 LEU   C N   1 
ATOM   11493 C CA  . LEU   G  1 365 ? 52.45551  34.73563  20.12265  1.000 17.95557  ?  365 LEU   C CA  1 
ATOM   11494 C C   . LEU   G  1 365 ? 52.12002  34.13253  18.76417  1.000 42.61123  ?  365 LEU   C C   1 
ATOM   11495 O O   . LEU   G  1 365 ? 52.16294  32.90942  18.58822  1.000 29.91240  ?  365 LEU   C O   1 
ATOM   11496 C CB  . LEU   G  1 365 ? 53.95824  34.64819  20.39910  1.000 32.05842  ?  365 LEU   C CB  1 
ATOM   11497 C CG  . LEU   G  1 365 ? 54.83065  35.56282  19.53533  1.000 35.61692  ?  365 LEU   C CG  1 
ATOM   11498 C CD1 . LEU   G  1 365 ? 54.46203  37.02753  19.79197  1.000 22.85140  ?  365 LEU   C CD1 1 
ATOM   11499 C CD2 . LEU   G  1 365 ? 56.29668  35.29751  19.79880  1.000 21.88872  ?  365 LEU   C CD2 1 
ATOM   11500 N N   . ILE   G  1 366 ? 51.73674  34.98839  17.81705  1.000 17.92224  ?  366 ILE   C N   1 
ATOM   11501 C CA  . ILE   G  1 366 ? 51.51371  34.58400  16.43703  1.000 32.25054  ?  366 ILE   C CA  1 
ATOM   11502 C C   . ILE   G  1 366 ? 52.36481  35.49432  15.57061  1.000 34.56253  ?  366 ILE   C C   1 
ATOM   11503 O O   . ILE   G  1 366 ? 52.88901  36.51307  16.02936  1.000 30.08706  ?  366 ILE   C O   1 
ATOM   11504 C CB  . ILE   G  1 366 ? 50.02909  34.66392  16.00193  1.000 25.61263  ?  366 ILE   C CB  1 
ATOM   11505 C CG1 . ILE   G  1 366 ? 49.55207  36.11030  15.98611  1.000 29.13701  ?  366 ILE   C CG1 1 
ATOM   11506 C CG2 . ILE   G  1 366 ? 49.13145  33.83241  16.89266  1.000 17.55604  ?  366 ILE   C CG2 1 
ATOM   11507 C CD1 . ILE   G  1 366 ? 48.30374  36.29488  15.17615  1.000 29.90720  ?  366 ILE   C CD1 1 
ATOM   11508 N N   . PHE   G  1 367 ? 52.50000  35.12875  14.30127  1.000 24.89555  ?  367 PHE   C N   1 
ATOM   11509 C CA  . PHE   G  1 367 ? 53.10832  36.06161  13.36891  1.000 21.86399  ?  367 PHE   C CA  1 
ATOM   11510 C C   . PHE   G  1 367 ? 52.25528  36.18152  12.11415  1.000 31.13892  ?  367 PHE   C C   1 
ATOM   11511 O O   . PHE   G  1 367 ? 51.47549  35.29036  11.76076  1.000 26.64537  ?  367 PHE   C O   1 
ATOM   11512 C CB  . PHE   G  1 367 ? 54.60417  35.70149  13.03553  1.000 20.83203  ?  367 PHE   C CB  1 
ATOM   11513 C CG  . PHE   G  1 367 ? 54.80468  34.51773  12.10137  1.000 12.83701  ?  367 PHE   C CG  1 
ATOM   11514 C CD1 . PHE   G  1 367 ? 54.46116  34.59568  10.74817  1.000 29.12995  ?  367 PHE   C CD1 1 
ATOM   11515 C CD2 . PHE   G  1 367 ? 55.44112  33.36248  12.55638  1.000 24.27855  ?  367 PHE   C CD2 1 
ATOM   11516 C CE1 . PHE   G  1 367 ? 54.67861  33.52185  9.88305   1.000 13.28589  ?  367 PHE   C CE1 1 
ATOM   11517 C CE2 . PHE   G  1 367 ? 55.68070  32.27495  11.69199  1.000 22.33983  ?  367 PHE   C CE2 1 
ATOM   11518 C CZ  . PHE   G  1 367 ? 55.30543  32.35103  10.35581  1.000 19.06198  ?  367 PHE   C CZ  1 
ATOM   11519 N N   . LEU   G  1 368 ? 52.38896  37.33404  11.48437  1.000 31.00731  ?  368 LEU   C N   1 
ATOM   11520 C CA  . LEU   G  1 368 ? 51.88073  37.61240  10.15799  1.000 21.96329  ?  368 LEU   C CA  1 
ATOM   11521 C C   . LEU   G  1 368 ? 53.06730  38.03986  9.30230   1.000 22.71222  ?  368 LEU   C C   1 
ATOM   11522 O O   . LEU   G  1 368 ? 53.93887  38.78322  9.77125   1.000 31.22394  ?  368 LEU   C O   1 
ATOM   11523 C CB  . LEU   G  1 368 ? 50.82562  38.72172  10.21420  1.000 19.62800  ?  368 LEU   C CB  1 
ATOM   11524 C CG  . LEU   G  1 368 ? 49.47622  38.33499  10.80522  1.000 30.22425  ?  368 LEU   C CG  1 
ATOM   11525 C CD1 . LEU   G  1 368 ? 48.70450  39.58732  11.17542  1.000 26.00521  ?  368 LEU   C CD1 1 
ATOM   11526 C CD2 . LEU   G  1 368 ? 48.67591  37.50342  9.80150   1.000 27.65911  ?  368 LEU   C CD2 1 
ATOM   11527 N N   . VAL   G  1 369 ? 53.12794  37.55896  8.06344   1.000 16.81258  ?  369 VAL   C N   1 
ATOM   11528 C CA  . VAL   G  1 369 ? 54.06209  38.09158  7.07509   1.000 19.15252  ?  369 VAL   C CA  1 
ATOM   11529 C C   . VAL   G  1 369 ? 53.24800  38.59848  5.88941   1.000 16.63670  ?  369 VAL   C C   1 
ATOM   11530 O O   . VAL   G  1 369 ? 52.50069  37.82913  5.26861   1.000 26.08365  ?  369 VAL   C O   1 
ATOM   11531 C CB  . VAL   G  1 369 ? 55.09914  37.05046  6.61890   1.000 25.38405  ?  369 VAL   C CB  1 
ATOM   11532 C CG1 . VAL   G  1 369 ? 56.09863  37.70630  5.64402   1.000 15.15156  ?  369 VAL   C CG1 1 
ATOM   11533 C CG2 . VAL   G  1 369 ? 55.81884  36.45101  7.80816   1.000 22.54537  ?  369 VAL   C CG2 1 
ATOM   11534 N N   . PHE   G  1 370 ? 53.39930  39.88050  5.56309   1.000 31.29293  ?  370 PHE   C N   1 
ATOM   11535 C CA  . PHE   G  1 370 ? 52.77518  40.44431  4.37059   1.000 12.93800  ?  370 PHE   C CA  1 
ATOM   11536 C C   . PHE   G  1 370 ? 53.79762  40.44962  3.23394   1.000 26.77875  ?  370 PHE   C C   1 
ATOM   11537 O O   . PHE   G  1 370 ? 54.86828  41.06128  3.34969   1.000 25.00147  ?  370 PHE   C O   1 
ATOM   11538 C CB  . PHE   G  1 370 ? 52.21877  41.83608  4.67533   1.000 20.42181  ?  370 PHE   C CB  1 
ATOM   11539 C CG  . PHE   G  1 370 ? 51.16747  41.81054  5.73764   1.000 30.42937  ?  370 PHE   C CG  1 
ATOM   11540 C CD1 . PHE   G  1 370 ? 49.87950  41.37781  5.43882   1.000 20.95423  ?  370 PHE   C CD1 1 
ATOM   11541 C CD2 . PHE   G  1 370 ? 51.47417  42.14338  7.05254   1.000 35.21671  ?  370 PHE   C CD2 1 
ATOM   11542 C CE1 . PHE   G  1 370 ? 48.89898  41.30111  6.42935   1.000 31.11333  ?  370 PHE   C CE1 1 
ATOM   11543 C CE2 . PHE   G  1 370 ? 50.48954  42.08075  8.05723   1.000 19.59891  ?  370 PHE   C CE2 1 
ATOM   11544 C CZ  . PHE   G  1 370 ? 49.20769  41.64963  7.74503   1.000 30.60690  ?  370 PHE   C CZ  1 
ATOM   11545 N N   . ILE   G  1 371 ? 53.47927  39.74430  2.15124   1.000 22.61002  ?  371 ILE   C N   1 
ATOM   11546 C CA  . ILE   G  1 371 ? 54.45960  39.34200  1.14125   1.000 18.38873  ?  371 ILE   C CA  1 
ATOM   11547 C C   . ILE   G  1 371 ? 54.19051  40.11459  -0.14722  1.000 19.30846  ?  371 ILE   C C   1 
ATOM   11548 O O   . ILE   G  1 371 ? 53.10615  40.00471  -0.73705  1.000 29.21574  ?  371 ILE   C O   1 
ATOM   11549 C CB  . ILE   G  1 371 ? 54.41212  37.82293  0.90238   1.000 27.50420  ?  371 ILE   C CB  1 
ATOM   11550 C CG1 . ILE   G  1 371 ? 54.57214  37.07398  2.23671   1.000 17.09192  ?  371 ILE   C CG1 1 
ATOM   11551 C CG2 . ILE   G  1 371 ? 55.47717  37.38913  -0.11461  1.000 12.97707  ?  371 ILE   C CG2 1 
ATOM   11552 C CD1 . ILE   G  1 371 ? 53.87854  35.72596  2.25186   1.000 14.95908  ?  371 ILE   C CD1 1 
ATOM   11553 N N   . GLY   G  1 372 ? 55.18095  40.89751  -0.58747  1.000 24.34430  ?  372 GLY   C N   1 
ATOM   11554 C CA  . GLY   G  1 372 ? 55.04959  41.62014  -1.83733  1.000 15.64191  ?  372 GLY   C CA  1 
ATOM   11555 C C   . GLY   G  1 372 ? 55.10960  40.70574  -3.04891  1.000 23.97065  ?  372 GLY   C C   1 
ATOM   11556 O O   . GLY   G  1 372 ? 55.60173  39.57810  -2.99555  1.000 24.14282  ?  372 GLY   C O   1 
ATOM   11557 N N   . MET   G  1 373 ? 54.56719  41.20648  -4.15363  1.000 27.88678  ?  373 MET   C N   1 
ATOM   11558 C CA  . MET   G  1 373 ? 54.62066  40.52241  -5.44060  1.000 40.92227  ?  373 MET   C CA  1 
ATOM   11559 C C   . MET   G  1 373 ? 54.80376  41.57480  -6.51433  1.000 38.67412  ?  373 MET   C C   1 
ATOM   11560 O O   . MET   G  1 373 ? 53.95491  42.46552  -6.65133  1.000 33.96622  ?  373 MET   C O   1 
ATOM   11561 C CB  . MET   G  1 373 ? 53.35636  39.71178  -5.71050  1.000 20.92594  ?  373 MET   C CB  1 
ATOM   11562 C CG  . MET   G  1 373 ? 53.16265  38.60145  -4.72017  1.000 42.74995  ?  373 MET   C CG  1 
ATOM   11563 S SD  . MET   G  1 373 ? 51.59494  37.71193  -4.94845  1.000 36.26001  ?  373 MET   C SD  1 
ATOM   11564 C CE  . MET   G  1 373 ? 51.67200  37.31129  -6.69412  1.000 12.04141  ?  373 MET   C CE  1 
ATOM   11565 N N   . THR   G  1 374 ? 55.90052  41.45326  -7.27418  1.000 25.71161  ?  374 THR   C N   1 
ATOM   11566 C CA  . THR   G  1 374 ? 56.30637  42.41040  -8.30466  1.000 27.08330  ?  374 THR   C CA  1 
ATOM   11567 C C   . THR   G  1 374 ? 56.05049  43.84424  -7.83827  1.000 23.99188  ?  374 THR   C C   1 
ATOM   11568 O O   . THR   G  1 374 ? 56.50760  44.22833  -6.75878  1.000 34.61337  ?  374 THR   C O   1 
ATOM   11569 C CB  . THR   G  1 374 ? 55.62034  42.08644  -9.65388  1.000 36.06110  ?  374 THR   C CB  1 
ATOM   11570 O OG1 . THR   G  1 374 ? 54.19188  42.23674  -9.57746  1.000 31.01356  ?  374 THR   C OG1 1 
ATOM   11571 C CG2 . THR   G  1 374 ? 55.92591  40.65311  -10.05609 1.000 20.63406  ?  374 THR   C CG2 1 
ATOM   11572 N N   . GLU   G  1 375 ? 55.31367  44.64045  -8.60894  1.000 34.02184  ?  375 GLU   C N   1 
ATOM   11573 C CA  . GLU   G  1 375 ? 55.15985  46.05438  -8.26601  1.000 21.55328  ?  375 GLU   C CA  1 
ATOM   11574 C C   . GLU   G  1 375 ? 54.21346  46.31750  -7.08713  1.000 36.40038  ?  375 GLU   C C   1 
ATOM   11575 O O   . GLU   G  1 375 ? 54.16961  47.45432  -6.59483  1.000 22.49394  ?  375 GLU   C O   1 
ATOM   11576 C CB  . GLU   G  1 375 ? 54.66895  46.83609  -9.48724  1.000 34.41100  ?  375 GLU   C CB  1 
ATOM   11577 C CG  . GLU   G  1 375 ? 53.29422  46.35824  -10.01671 1.000 23.06723  ?  375 GLU   C CG  1 
ATOM   11578 C CD  . GLU   G  1 375 ? 53.41754  45.44933  -11.25670 1.000 33.42869  ?  375 GLU   C CD  1 
ATOM   11579 O OE1 . GLU   G  1 375 ? 53.98255  44.33622  -11.13956 1.000 38.76251  ?  375 GLU   C OE1 1 
ATOM   11580 O OE2 . GLU   G  1 375 ? 52.94866  45.85566  -12.35187 1.000 37.80524  -1 375 GLU   C OE2 1 
ATOM   11581 N N   . ILE   G  1 376 ? 53.44219  45.32911  -6.62635  1.000 28.69359  ?  376 ILE   C N   1 
ATOM   11582 C CA  . ILE   G  1 376 ? 52.63176  45.53717  -5.42757  1.000 28.91930  ?  376 ILE   C CA  1 
ATOM   11583 C C   . ILE   G  1 376 ? 53.38794  44.97644  -4.22643  1.000 32.79002  ?  376 ILE   C C   1 
ATOM   11584 O O   . ILE   G  1 376 ? 53.10688  43.86909  -3.75464  1.000 40.34854  ?  376 ILE   C O   1 
ATOM   11585 C CB  . ILE   G  1 376 ? 51.23500  44.90751  -5.57651  1.000 39.83918  ?  376 ILE   C CB  1 
ATOM   11586 C CG1 . ILE   G  1 376 ? 50.56877  45.44064  -6.85449  1.000 29.27168  ?  376 ILE   C CG1 1 
ATOM   11587 C CG2 . ILE   G  1 376 ? 50.38189  45.17289  -4.32546  1.000 17.91242  ?  376 ILE   C CG2 1 
ATOM   11588 C CD1 . ILE   G  1 376 ? 49.30294  44.68486  -7.25605  1.000 50.10116  ?  376 ILE   C CD1 1 
ATOM   11589 N N   . SER   G  1 377 ? 54.36701  45.73438  -3.72937  1.000 29.12786  ?  377 SER   C N   1 
ATOM   11590 C CA  . SER   G  1 377 ? 55.29528  45.20967  -2.73803  1.000 42.66673  ?  377 SER   C CA  1 
ATOM   11591 C C   . SER   G  1 377 ? 55.53604  46.14516  -1.56295  1.000 26.65333  ?  377 SER   C C   1 
ATOM   11592 O O   . SER   G  1 377 ? 56.34743  45.81912  -0.68931  1.000 50.88839  ?  377 SER   C O   1 
ATOM   11593 C CB  . SER   G  1 377 ? 56.63458  44.85615  -3.40015  1.000 20.50650  ?  377 SER   C CB  1 
ATOM   11594 O OG  . SER   G  1 377 ? 56.46749  43.69607  -4.20046  1.000 26.58415  ?  377 SER   C OG  1 
ATOM   11595 N N   . THR   G  1 378 ? 54.84982  47.27867  -1.50446  1.000 36.23348  ?  378 THR   C N   1 
ATOM   11596 C CA  . THR   G  1 378 ? 54.93610  48.14979  -0.34231  1.000 22.35902  ?  378 THR   C CA  1 
ATOM   11597 C C   . THR   G  1 378 ? 53.96479  47.69416  0.75152   1.000 37.71914  ?  378 THR   C C   1 
ATOM   11598 O O   . THR   G  1 378 ? 52.76832  47.47585  0.49970   1.000 29.45336  ?  378 THR   C O   1 
ATOM   11599 C CB  . THR   G  1 378 ? 54.66014  49.59796  -0.74367  1.000 34.88180  ?  378 THR   C CB  1 
ATOM   11600 O OG1 . THR   G  1 378 ? 55.73279  50.07074  -1.56985  1.000 29.67590  ?  378 THR   C OG1 1 
ATOM   11601 C CG2 . THR   G  1 378 ? 54.58810  50.45619  0.48537   1.000 10.09352  ?  378 THR   C CG2 1 
ATOM   11602 N N   . CYS   G  1 379 ? 54.48944  47.55494  1.97054   1.000 22.76368  ?  379 CYS   C N   1 
ATOM   11603 C CA  . CYS   G  1 379 ? 53.74220  47.04745  3.12096   1.000 21.04584  ?  379 CYS   C CA  1 
ATOM   11604 C C   . CYS   G  1 379 ? 53.71368  48.15556  4.16662   1.000 29.11589  ?  379 CYS   C C   1 
ATOM   11605 O O   . CYS   G  1 379 ? 54.68333  48.35206  4.90698   1.000 34.47848  ?  379 CYS   C O   1 
ATOM   11606 C CB  . CYS   G  1 379 ? 54.38298  45.77561  3.67263   1.000 21.62712  ?  379 CYS   C CB  1 
ATOM   11607 S SG  . CYS   G  1 379 ? 54.49813  44.43085  2.45808   1.000 33.15235  ?  379 CYS   C SG  1 
ATOM   11608 N N   . GLU   G  1 380 ? 52.60953  48.88943  4.22613   1.000 31.38961  ?  380 GLU   C N   1 
ATOM   11609 C CA  . GLU   G  1 380 ? 52.44754  49.94316  5.21691   1.000 16.89342  ?  380 GLU   C CA  1 
ATOM   11610 C C   . GLU   G  1 380 ? 51.67605  49.40977  6.41816   1.000 33.18610  ?  380 GLU   C C   1 
ATOM   11611 O O   . GLU   G  1 380 ? 50.50526  49.02210  6.28974   1.000 32.04580  ?  380 GLU   C O   1 
ATOM   11612 C CB  . GLU   G  1 380 ? 51.72733  51.15926  4.64703   1.000 28.37000  ?  380 GLU   C CB  1 
ATOM   11613 C CG  . GLU   G  1 380 ? 51.52299  52.18536  5.72967   1.000 41.14082  ?  380 GLU   C CG  1 
ATOM   11614 C CD  . GLU   G  1 380 ? 50.70996  53.36943  5.29867   1.000 36.91525  ?  380 GLU   C CD  1 
ATOM   11615 O OE1 . GLU   G  1 380 ? 50.12105  53.32019  4.19421   1.000 41.94121  ?  380 GLU   C OE1 1 
ATOM   11616 O OE2 . GLU   G  1 380 ? 50.66508  54.34159  6.08471   1.000 49.03163  -1 380 GLU   C OE2 1 
ATOM   11617 N N   . ALA   G  1 381 ? 52.33664  49.39198  7.57810   1.000 22.82210  ?  381 ALA   C N   1 
ATOM   11618 C CA  . ALA   G  1 381 ? 51.64743  49.20823  8.84969   1.000 41.32026  ?  381 ALA   C CA  1 
ATOM   11619 C C   . ALA   G  1 381 ? 51.03522  50.53614  9.29643   1.000 31.71004  ?  381 ALA   C C   1 
ATOM   11620 O O   . ALA   G  1 381 ? 51.69038  51.58635  9.24234   1.000 32.32557  ?  381 ALA   C O   1 
ATOM   11621 C CB  . ALA   G  1 381 ? 52.61606  48.68395  9.91567   1.000 21.80189  ?  381 ALA   C CB  1 
ATOM   11622 N N   . THR   G  1 382 ? 49.77514  50.49430  9.72739   1.000 30.91150  ?  382 THR   C N   1 
ATOM   11623 C CA  . THR   G  1 382 ? 49.14304  51.63970  10.37853  1.000 30.49355  ?  382 THR   C CA  1 
ATOM   11624 C C   . THR   G  1 382 ? 48.95759  51.42656  11.88143  1.000 25.62676  ?  382 THR   C C   1 
ATOM   11625 O O   . THR   G  1 382 ? 48.16089  52.12628  12.51550  1.000 53.16884  ?  382 THR   C O   1 
ATOM   11626 C CB  . THR   G  1 382 ? 47.80687  51.94820  9.71236   1.000 20.20599  ?  382 THR   C CB  1 
ATOM   11627 O OG1 . THR   G  1 382 ? 46.94773  50.79125  9.78567   1.000 29.09770  ?  382 THR   C OG1 1 
ATOM   11628 C CG2 . THR   G  1 382 ? 48.03745  52.33742  8.24988   1.000 30.99363  ?  382 THR   C CG2 1 
ATOM   11629 N N   . VAL   G  1 383 ? 49.65169  50.44303  12.44932  1.000 34.83870  ?  383 VAL   C N   1 
ATOM   11630 C CA  . VAL   G  1 383 ? 49.68690  50.21532  13.88379  1.000 24.17692  ?  383 VAL   C CA  1 
ATOM   11631 C C   . VAL   G  1 383 ? 51.13454  50.35266  14.33873  1.000 38.17893  ?  383 VAL   C C   1 
ATOM   11632 O O   . VAL   G  1 383 ? 52.06982  50.34712  13.53507  1.000 33.93074  ?  383 VAL   C O   1 
ATOM   11633 C CB  . VAL   G  1 383 ? 49.11986  48.84132  14.29169  1.000 44.88930  ?  383 VAL   C CB  1 
ATOM   11634 C CG1 . VAL   G  1 383 ? 47.65346  48.75341  13.95924  1.000 24.94258  ?  383 VAL   C CG1 1 
ATOM   11635 C CG2 . VAL   G  1 383 ? 49.90132  47.72256  13.61831  1.000 29.65164  ?  383 VAL   C CG2 1 
ATOM   11636 N N   . SER   G  1 384 ? 51.30875  50.48541  15.64788  1.000 45.02129  ?  384 SER   C N   1 
ATOM   11637 C CA  . SER   G  1 384 ? 52.62094  50.71199  16.23495  1.000 25.54222  ?  384 SER   C CA  1 
ATOM   11638 C C   . SER   G  1 384 ? 52.95126  49.58148  17.19451  1.000 49.93955  ?  384 SER   C C   1 
ATOM   11639 O O   . SER   G  1 384 ? 52.05337  48.93361  17.75433  1.000 38.70565  ?  384 SER   C O   1 
ATOM   11640 C CB  . SER   G  1 384 ? 52.66952  52.05283  16.97056  1.000 27.93896  ?  384 SER   C CB  1 
ATOM   11641 O OG  . SER   G  1 384 ? 52.21376  53.09379  16.11586  1.000 55.14466  ?  384 SER   C OG  1 
ATOM   11642 N N   . GLU   G  1 385 ? 54.24463  49.33283  17.37847  1.000 36.78717  ?  385 GLU   C N   1 
ATOM   11643 C CA  . GLU   G  1 385 ? 54.62418  48.35662  18.39016  1.000 45.51549  ?  385 GLU   C CA  1 
ATOM   11644 C C   . GLU   G  1 385 ? 54.06577  48.79832  19.74377  1.000 45.13268  ?  385 GLU   C C   1 
ATOM   11645 O O   . GLU   G  1 385 ? 54.03824  49.99069  20.07355  1.000 43.08865  ?  385 GLU   C O   1 
ATOM   11646 C CB  . GLU   G  1 385 ? 56.14273  48.19616  18.43402  1.000 23.45551  ?  385 GLU   C CB  1 
ATOM   11647 C CG  . GLU   G  1 385 ? 56.76299  47.81328  17.08523  1.000 37.25516  ?  385 GLU   C CG  1 
ATOM   11648 C CD  . GLU   G  1 385 ? 58.24765  47.46788  17.18930  1.000 54.16451  ?  385 GLU   C CD  1 
ATOM   11649 O OE1 . GLU   G  1 385 ? 58.88566  47.91802  18.17102  1.000 52.55357  ?  385 GLU   C OE1 1 
ATOM   11650 O OE2 . GLU   G  1 385 ? 58.77118  46.74126  16.30093  1.000 39.71523  -1 385 GLU   C OE2 1 
ATOM   11651 N N   . GLY   G  1 386 ? 53.54422  47.83793  20.49640  1.000 35.89181  ?  386 GLY   C N   1 
ATOM   11652 C CA  . GLY   G  1 386 ? 52.94262  48.10945  21.78415  1.000 22.04847  ?  386 GLY   C CA  1 
ATOM   11653 C C   . GLY   G  1 386 ? 51.45393  48.40372  21.75427  1.000 40.75767  ?  386 GLY   C C   1 
ATOM   11654 O O   . GLY   G  1 386 ? 50.78300  48.25902  22.77803  1.000 35.34245  ?  386 GLY   C O   1 
ATOM   11655 N N   . GLN   G  1 387 ? 50.92349  48.81056  20.61418  1.000 35.52912  ?  387 GLN   C N   1 
ATOM   11656 C CA  . GLN   G  1 387 ? 49.50802  49.12123  20.48944  1.000 32.21984  ?  387 GLN   C CA  1 
ATOM   11657 C C   . GLN   G  1 387 ? 48.63793  47.87214  20.65255  1.000 51.45503  ?  387 GLN   C C   1 
ATOM   11658 O O   . GLN   G  1 387 ? 49.04351  46.75318  20.31132  1.000 44.59150  ?  387 GLN   C O   1 
ATOM   11659 C CB  . GLN   G  1 387 ? 49.27102  49.76173  19.12625  1.000 31.07552  ?  387 GLN   C CB  1 
ATOM   11660 C CG  . GLN   G  1 387 ? 47.86651  50.09846  18.79385  1.000 31.63923  ?  387 GLN   C CG  1 
ATOM   11661 C CD  . GLN   G  1 387 ? 47.79682  50.78392  17.45665  1.000 39.63969  ?  387 GLN   C CD  1 
ATOM   11662 O OE1 . GLN   G  1 387 ? 48.81787  51.25549  16.93006  1.000 44.60286  ?  387 GLN   C OE1 1 
ATOM   11663 N NE2 . GLN   G  1 387 ? 46.60090  50.82363  16.87801  1.000 33.01985  ?  387 GLN   C NE2 1 
ATOM   11664 N N   . HIS   G  1 388 ? 47.43008  48.06855  21.19418  1.000 32.30699  ?  388 HIS   C N   1 
ATOM   11665 C CA  . HIS   G  1 388 ? 46.43535  47.00403  21.27741  1.000 43.60081  ?  388 HIS   C CA  1 
ATOM   11666 C C   . HIS   G  1 388 ? 45.44136  47.13913  20.13215  1.000 57.25046  ?  388 HIS   C C   1 
ATOM   11667 O O   . HIS   G  1 388 ? 45.11616  48.25239  19.70204  1.000 31.33351  ?  388 HIS   C O   1 
ATOM   11668 C CB  . HIS   G  1 388 ? 45.68442  47.03455  22.60197  1.000 21.61791  ?  388 HIS   C CB  1 
ATOM   11669 C CG  . HIS   G  1 388 ? 44.71622  45.90682  22.77791  1.000 38.95048  ?  388 HIS   C CG  1 
ATOM   11670 N ND1 . HIS   G  1 388 ? 43.40228  45.97330  22.35393  1.000 39.90894  ?  388 HIS   C ND1 1 
ATOM   11671 C CD2 . HIS   G  1 388 ? 44.87012  44.68253  23.33769  1.000 27.88174  ?  388 HIS   C CD2 1 
ATOM   11672 C CE1 . HIS   G  1 388 ? 42.79260  44.83484  22.63842  1.000 36.22465  ?  388 HIS   C CE1 1 
ATOM   11673 N NE2 . HIS   G  1 388 ? 43.65933  44.03556  23.23928  1.000 32.16571  ?  388 HIS   C NE2 1 
ATOM   11674 N N   . VAL   G  1 389 ? 44.97892  45.99605  19.62685  1.000 27.22518  ?  389 VAL   C N   1 
ATOM   11675 C CA  . VAL   G  1 389 ? 44.00292  45.94922  18.54313  1.000 39.62837  ?  389 VAL   C CA  1 
ATOM   11676 C C   . VAL   G  1 389 ? 43.01649  44.82677  18.82994  1.000 38.57195  ?  389 VAL   C C   1 
ATOM   11677 O O   . VAL   G  1 389 ? 43.32526  43.85647  19.53655  1.000 52.70545  ?  389 VAL   C O   1 
ATOM   11678 C CB  . VAL   G  1 389 ? 44.65366  45.75088  17.14314  1.000 44.81522  ?  389 VAL   C CB  1 
ATOM   11679 C CG1 . VAL   G  1 389 ? 45.58096  46.93582  16.78446  1.000 29.61401  ?  389 VAL   C CG1 1 
ATOM   11680 C CG2 . VAL   G  1 389 ? 45.40729  44.43295  17.06442  1.000 23.90140  ?  389 VAL   C CG2 1 
ATOM   11681 N N   . ASN   G  1 390 ? 41.81576  44.98090  18.27776  1.000 30.04827  ?  390 ASN   C N   1 
ATOM   11682 C CA  . ASN   G  1 390 ? 40.78270  43.95342  18.28812  1.000 33.51163  ?  390 ASN   C CA  1 
ATOM   11683 C C   . ASN   G  1 390 ? 40.69795  43.29475  16.92289  1.000 58.87451  ?  390 ASN   C C   1 
ATOM   11684 O O   . ASN   G  1 390 ? 40.93406  43.93251  15.88929  1.000 36.34838  ?  390 ASN   C O   1 
ATOM   11685 C CB  . ASN   G  1 390 ? 39.41135  44.53325  18.65635  1.000 46.21212  ?  390 ASN   C CB  1 
ATOM   11686 C CG  . ASN   G  1 390 ? 39.34718  44.99750  20.10244  1.000 39.76007  ?  390 ASN   C CG  1 
ATOM   11687 O OD1 . ASN   G  1 390 ? 39.82381  44.31147  21.02016  1.000 50.24416  ?  390 ASN   C OD1 1 
ATOM   11688 N ND2 . ASN   G  1 390 ? 38.78772  46.17862  20.30986  1.000 49.69694  ?  390 ASN   C ND2 1 
ATOM   11689 N N   . ARG   G  1 391 ? 40.37825  42.00230  16.93845  1.000 30.60669  ?  391 ARG   C N   1 
ATOM   11690 C CA  . ARG   G  1 391 ? 40.11564  41.24169  15.72569  1.000 41.20137  ?  391 ARG   C CA  1 
ATOM   11691 C C   . ARG   G  1 391 ? 39.23383  42.04423  14.76798  1.000 29.20870  ?  391 ARG   C C   1 
ATOM   11692 O O   . ARG   G  1 391 ? 38.15114  42.50568  15.14274  1.000 39.88834  ?  391 ARG   C O   1 
ATOM   11693 C CB  . ARG   G  1 391 ? 39.45333  39.91739  16.12102  1.000 20.57840  ?  391 ARG   C CB  1 
ATOM   11694 C CG  . ARG   G  1 391 ? 39.37402  38.84275  15.04834  1.000 30.24848  ?  391 ARG   C CG  1 
ATOM   11695 C CD  . ARG   G  1 391 ? 39.19062  37.45735  15.66865  1.000 39.83634  ?  391 ARG   C CD  1 
ATOM   11696 N NE  . ARG   G  1 391 ? 37.91607  37.27465  16.35506  1.000 32.19664  ?  391 ARG   C NE  1 
ATOM   11697 C CZ  . ARG   G  1 391 ? 36.84436  36.73318  15.78858  1.000 73.76618  ?  391 ARG   C CZ  1 
ATOM   11698 N NH1 . ARG   G  1 391 ? 36.83929  36.37517  14.51638  1.000 33.16162  ?  391 ARG   C NH1 1 
ATOM   11699 N NH2 . ARG   G  1 391 ? 35.74823  36.54397  16.51275  1.000 34.10946  ?  391 ARG   C NH2 1 
ATOM   11700 N N   . GLY   G  1 392 ? 39.74580  42.29269  13.55105  1.000 35.70638  ?  392 GLY   C N   1 
ATOM   11701 C CA  . GLY   G  1 392 ? 39.04000  43.03476  12.51633  1.000 32.13421  ?  392 GLY   C CA  1 
ATOM   11702 C C   . GLY   G  1 392 ? 39.47019  44.48080  12.33143  1.000 40.91521  ?  392 GLY   C C   1 
ATOM   11703 O O   . GLY   G  1 392 ? 39.06236  45.10758  11.33653  1.000 39.49093  ?  392 GLY   C O   1 
ATOM   11704 N N   . ASP   G  1 393 ? 40.28382  45.02536  13.24537  1.000 24.00934  ?  393 ASP   C N   1 
ATOM   11705 C CA  . ASP   G  1 393 ? 40.79423  46.39034  13.10824  1.000 36.69958  ?  393 ASP   C CA  1 
ATOM   11706 C C   . ASP   G  1 393 ? 41.86046  46.46815  12.01164  1.000 31.25502  ?  393 ASP   C C   1 
ATOM   11707 O O   . ASP   G  1 393 ? 42.46846  45.46176  11.62936  1.000 50.30990  ?  393 ASP   C O   1 
ATOM   11708 C CB  . ASP   G  1 393 ? 41.39288  46.88338  14.43283  1.000 27.33923  ?  393 ASP   C CB  1 
ATOM   11709 C CG  . ASP   G  1 393 ? 40.37425  46.92337  15.58456  1.000 56.22712  ?  393 ASP   C CG  1 
ATOM   11710 O OD1 . ASP   G  1 393 ? 39.15633  46.69878  15.36876  1.000 52.82918  ?  393 ASP   C OD1 1 
ATOM   11711 O OD2 . ASP   G  1 393 ? 40.80891  47.18413  16.72710  1.000 40.92992  -1 393 ASP   C OD2 1 
ATOM   11712 N N   . ASP   G  1 394 ? 42.10668  47.68616  11.51840  1.000 48.95936  ?  394 ASP   C N   1 
ATOM   11713 C CA  . ASP   G  1 394 ? 43.15850  47.87740  10.51822  1.000 24.67607  ?  394 ASP   C CA  1 
ATOM   11714 C C   . ASP   G  1 394 ? 44.53075  47.55008  11.10660  1.000 51.35842  ?  394 ASP   C C   1 
ATOM   11715 O O   . ASP   G  1 394 ? 44.86393  48.00120  12.20719  1.000 34.18333  ?  394 ASP   C O   1 
ATOM   11716 C CB  . ASP   G  1 394 ? 43.15871  49.31757  9.99366   1.000 44.17428  ?  394 ASP   C CB  1 
ATOM   11717 C CG  . ASP   G  1 394 ? 41.84494  49.71858  9.34443   1.000 33.67620  ?  394 ASP   C CG  1 
ATOM   11718 O OD1 . ASP   G  1 394 ? 41.20676  48.87395  8.66202   1.000 78.03525  ?  394 ASP   C OD1 1 
ATOM   11719 O OD2 . ASP   G  1 394 ? 41.46726  50.90035  9.49776   1.000 73.28535  -1 394 ASP   C OD2 1 
ATOM   11720 N N   . LEU   G  1 395 ? 45.32801  46.75417  10.38414  1.000 24.86458  ?  395 LEU   C N   1 
ATOM   11721 C CA  . LEU   G  1 395 ? 46.75407  46.66530  10.69474  1.000 43.80584  ?  395 LEU   C CA  1 
ATOM   11722 C C   . LEU   G  1 395 ? 47.59331  47.48994  9.74457   1.000 36.74093  ?  395 LEU   C C   1 
ATOM   11723 O O   . LEU   G  1 395 ? 48.68406  47.94965  10.11745  1.000 34.20602  ?  395 LEU   C O   1 
ATOM   11724 C CB  . LEU   G  1 395 ? 47.26498  45.22285  10.63146  1.000 21.27557  ?  395 LEU   C CB  1 
ATOM   11725 C CG  . LEU   G  1 395 ? 46.84940  44.21706  11.68774  1.000 35.75017  ?  395 LEU   C CG  1 
ATOM   11726 C CD1 . LEU   G  1 395 ? 47.53205  42.93136  11.34492  1.000 20.74722  ?  395 LEU   C CD1 1 
ATOM   11727 C CD2 . LEU   G  1 395 ? 47.22375  44.69713  13.08004  1.000 30.77744  ?  395 LEU   C CD2 1 
ATOM   11728 N N   . GLY   G  1 396 ? 47.09980  47.67047  8.52789   1.000 27.33843  ?  396 GLY   C N   1 
ATOM   11729 C CA  . GLY   G  1 396 ? 47.84657  48.36895  7.50293   1.000 35.73704  ?  396 GLY   C CA  1 
ATOM   11730 C C   . GLY   G  1 396 ? 47.30582  47.95963  6.15069   1.000 31.90517  ?  396 GLY   C C   1 
ATOM   11731 O O   . GLY   G  1 396 ? 46.15842  47.51597  6.03884   1.000 35.35626  ?  396 GLY   C O   1 
ATOM   11732 N N   . MET   G  1 397 ? 48.16073  48.08431  5.13814   1.000 34.14627  ?  397 MET   C N   1 
ATOM   11733 C CA  . MET   G  1 397 ? 47.69837  47.78831  3.78954   1.000 33.02317  ?  397 MET   C CA  1 
ATOM   11734 C C   . MET   G  1 397 ? 48.87922  47.64006  2.84284   1.000 48.53354  ?  397 MET   C C   1 
ATOM   11735 O O   . MET   G  1 397 ? 50.01421  48.01713  3.15656   1.000 37.76237  ?  397 MET   C O   1 
ATOM   11736 C CB  . MET   G  1 397 ? 46.75992  48.88047  3.28784   1.000 30.84749  ?  397 MET   C CB  1 
ATOM   11737 C CG  . MET   G  1 397 ? 47.48700  50.11058  2.77524   1.000 35.32834  ?  397 MET   C CG  1 
ATOM   11738 S SD  . MET   G  1 397 ? 46.41411  51.51050  3.01829   1.000 45.72937  ?  397 MET   C SD  1 
ATOM   11739 C CE  . MET   G  1 397 ? 46.56380  51.73259  4.78058   1.000 23.97501  ?  397 MET   C CE  1 
ATOM   11740 N N   . PHE   G  1 398 ? 48.57905  47.07696  1.67121   1.000 31.28050  ?  398 PHE   C N   1 
ATOM   11741 C CA  . PHE   G  1 398 ? 49.49159  47.01136  0.54123   1.000 24.56285  ?  398 PHE   C CA  1 
ATOM   11742 C C   . PHE   G  1 398 ? 49.38172  48.26706  -0.33194  1.000 34.34223  ?  398 PHE   C C   1 
ATOM   11743 O O   . PHE   G  1 398 ? 48.31931  48.87964  -0.44638  1.000 44.05269  ?  398 PHE   C O   1 
ATOM   11744 C CB  . PHE   G  1 398 ? 49.17936  45.78888  -0.32622  1.000 24.64470  ?  398 PHE   C CB  1 
ATOM   11745 C CG  . PHE   G  1 398 ? 49.50263  44.47242  0.30572   1.000 38.29085  ?  398 PHE   C CG  1 
ATOM   11746 C CD1 . PHE   G  1 398 ? 50.83146  44.04085  0.40895   1.000 24.95864  ?  398 PHE   C CD1 1 
ATOM   11747 C CD2 . PHE   G  1 398 ? 48.47768  43.62232  0.73592   1.000 31.71679  ?  398 PHE   C CD2 1 
ATOM   11748 C CE1 . PHE   G  1 398 ? 51.13897  42.79275  0.97162   1.000 36.99870  ?  398 PHE   C CE1 1 
ATOM   11749 C CE2 . PHE   G  1 398 ? 48.76867  42.36209  1.29841   1.000 27.76149  ?  398 PHE   C CE2 1 
ATOM   11750 C CZ  . PHE   G  1 398 ? 50.09771  41.94734  1.41676   1.000 35.09756  ?  398 PHE   C CZ  1 
ATOM   11751 N N   . HIS   G  1 399 ? 50.48588  48.62565  -0.98446  1.000 37.73521  ?  399 HIS   C N   1 
ATOM   11752 C CA  . HIS   G  1 399 ? 50.46413  49.64671  -2.02602  1.000 46.12892  ?  399 HIS   C CA  1 
ATOM   11753 C C   . HIS   G  1 399 ? 51.32908  49.19382  -3.18967  1.000 24.58818  ?  399 HIS   C C   1 
ATOM   11754 O O   . HIS   G  1 399 ? 52.29852  48.45266  -3.00858  1.000 52.98674  ?  399 HIS   C O   1 
ATOM   11755 C CB  . HIS   G  1 399 ? 51.01660  51.03350  -1.58696  1.000 22.08900  ?  399 HIS   C CB  1 
ATOM   11756 C CG  . HIS   G  1 399 ? 50.37025  51.61465  -0.36651  1.000 25.84279  ?  399 HIS   C CG  1 
ATOM   11757 N ND1 . HIS   G  1 399 ? 49.23866  52.40078  -0.42253  1.000 33.88770  ?  399 HIS   C ND1 1 
ATOM   11758 C CD2 . HIS   G  1 399 ? 50.72151  51.55101  0.94259   1.000 41.27100  ?  399 HIS   C CD2 1 
ATOM   11759 C CE1 . HIS   G  1 399 ? 48.90672  52.77613  0.80108   1.000 51.54077  ?  399 HIS   C CE1 1 
ATOM   11760 N NE2 . HIS   G  1 399 ? 49.79520  52.28214  1.64680   1.000 22.75173  ?  399 HIS   C NE2 1 
ATOM   11761 N N   . PHE   G  1 400 ? 51.00154  49.69258  -4.38043  1.000 41.72044  ?  400 PHE   C N   1 
ATOM   11762 C CA  . PHE   G  1 400 ? 51.99293  49.74551  -5.44379  1.000 23.18954  ?  400 PHE   C CA  1 
ATOM   11763 C C   . PHE   G  1 400 ? 53.21998  50.48947  -4.92505  1.000 31.82008  ?  400 PHE   C C   1 
ATOM   11764 O O   . PHE   G  1 400 ? 53.10499  51.57709  -4.34771  1.000 42.31015  ?  400 PHE   C O   1 
ATOM   11765 C CB  . PHE   G  1 400 ? 51.41396  50.44501  -6.67799  1.000 40.86730  ?  400 PHE   C CB  1 
ATOM   11766 C CG  . PHE   G  1 400 ? 50.53890  49.56500  -7.52196  1.000 20.79428  ?  400 PHE   C CG  1 
ATOM   11767 C CD1 . PHE   G  1 400 ? 49.26968  49.18814  -7.07968  1.000 39.83853  ?  400 PHE   C CD1 1 
ATOM   11768 C CD2 . PHE   G  1 400 ? 50.98234  49.09917  -8.75747  1.000 40.83159  ?  400 PHE   C CD2 1 
ATOM   11769 C CE1 . PHE   G  1 400 ? 48.46664  48.35140  -7.84489  1.000 24.50644  ?  400 PHE   C CE1 1 
ATOM   11770 C CE2 . PHE   G  1 400 ? 50.17456  48.26829  -9.54249  1.000 36.67749  ?  400 PHE   C CE2 1 
ATOM   11771 C CZ  . PHE   G  1 400 ? 48.92160  47.89420  -9.08025  1.000 39.59255  ?  400 PHE   C CZ  1 
ATOM   11772 N N   . GLY   G  1 401 ? 54.38167  49.88216  -5.08829  1.000 28.59335  ?  401 GLY   C N   1 
ATOM   11773 C CA  . GLY   G  1 401 ? 55.61863  50.46454  -4.60459  1.000 24.52186  ?  401 GLY   C CA  1 
ATOM   11774 C C   . GLY   G  1 401 ? 56.61629  49.37442  -4.27850  1.000 34.98106  ?  401 GLY   C C   1 
ATOM   11775 O O   . GLY   G  1 401 ? 56.35816  48.18613  -4.46936  1.000 41.17389  ?  401 GLY   C O   1 
ATOM   11776 N N   . GLY   G  1 402 ? 57.77077  49.81067  -3.77254  1.000 31.52236  ?  402 GLY   C N   1 
ATOM   11777 C CA  . GLY   G  1 402 ? 58.85169  48.89422  -3.41978  1.000 24.12802  ?  402 GLY   C CA  1 
ATOM   11778 C C   . GLY   G  1 402 ? 58.77410  48.35734  -1.99426  1.000 53.36616  ?  402 GLY   C C   1 
ATOM   11779 O O   . GLY   G  1 402 ? 59.49527  47.42809  -1.57103  1.000 34.98424  ?  402 GLY   C O   1 
ATOM   11780 O OXT . GLY   G  1 402 ? 57.95523  48.85163  -1.21158  1.000 44.16758  -1 402 GLY   C OXT 1 
ATOM   11781 N N   . SER   H  2 1   ? 50.43156  38.99361  -1.12013  1.000 20.30837  ?  404 SER   D N   1 
ATOM   11782 C CA  . SER   H  2 1   ? 50.25669  37.71906  -0.41000  1.000 15.42804  ?  404 SER   D CA  1 
ATOM   11783 C C   . SER   H  2 1   ? 50.46174  37.88579  1.10065   1.000 26.85325  ?  404 SER   D C   1 
ATOM   11784 O O   . SER   H  2 1   ? 51.10437  38.83765  1.53485   1.000 30.36868  ?  404 SER   D O   1 
ATOM   11785 C CB  . SER   H  2 1   ? 51.22139  36.65625  -0.97606  1.000 21.70324  ?  404 SER   D CB  1 
ATOM   11786 O OG  . SER   H  2 1   ? 51.04024  35.38536  -0.36411  1.000 24.44155  ?  404 SER   D OG  1 
ATOM   11787 N N   . PHE   H  2 2   ? 49.91724  36.97383  1.91029   1.000 18.00244  ?  405 PHE   D N   1 
ATOM   11788 C CA  . PHE   H  2 2   ? 50.10801  37.05442  3.35632   1.000 24.27723  ?  405 PHE   D CA  1 
ATOM   11789 C C   . PHE   H  2 2   ? 50.19517  35.65071  3.94525   1.000 21.94812  ?  405 PHE   D C   1 
ATOM   11790 O O   . PHE   H  2 2   ? 49.65366  34.68837  3.38271   1.000 31.24624  ?  405 PHE   D O   1 
ATOM   11791 C CB  . PHE   H  2 2   ? 48.97984  37.84467  4.04335   1.000 24.95804  ?  405 PHE   D CB  1 
ATOM   11792 C CG  . PHE   H  2 2   ? 47.83281  36.98951  4.49906   1.000 27.43043  ?  405 PHE   D CG  1 
ATOM   11793 C CD1 . PHE   H  2 2   ? 46.83108  36.60005  3.60316   1.000 33.72372  ?  405 PHE   D CD1 1 
ATOM   11794 C CD2 . PHE   H  2 2   ? 47.76251  36.55791  5.82577   1.000 30.86577  ?  405 PHE   D CD2 1 
ATOM   11795 C CE1 . PHE   H  2 2   ? 45.76979  35.79541  4.01727   1.000 27.45242  ?  405 PHE   D CE1 1 
ATOM   11796 C CE2 . PHE   H  2 2   ? 46.70638  35.74790  6.25819   1.000 23.58977  ?  405 PHE   D CE2 1 
ATOM   11797 C CZ  . PHE   H  2 2   ? 45.69464  35.37200  5.34060   1.000 29.77771  ?  405 PHE   D CZ  1 
ATOM   11798 N N   . ALA   H  2 3   ? 50.86334  35.54727  5.10294   1.000 21.56016  ?  406 ALA   D N   1 
ATOM   11799 C CA  . ALA   H  2 3   ? 50.97299  34.28160  5.81083   1.000 25.81206  ?  406 ALA   D CA  1 
ATOM   11800 C C   . ALA   H  2 3   ? 50.73729  34.48195  7.29895   1.000 28.95226  ?  406 ALA   D C   1 
ATOM   11801 O O   . ALA   H  2 3   ? 51.24682  35.43698  7.90183   1.000 27.86086  ?  406 ALA   D O   1 
ATOM   11802 C CB  . ALA   H  2 3   ? 52.32910  33.62249  5.58865   1.000 9.61207   ?  406 ALA   D CB  1 
ATOM   11803 N N   . LEU   H  2 4   ? 49.95928  33.56063  7.87557   1.000 29.68082  ?  407 LEU   D N   1 
ATOM   11804 C CA  . LEU   H  2 4   ? 49.69745  33.48569  9.30613   1.000 28.95851  ?  407 LEU   D CA  1 
ATOM   11805 C C   . LEU   H  2 4   ? 50.50919  32.33484  9.88435   1.000 14.17685  ?  407 LEU   D C   1 
ATOM   11806 O O   . LEU   H  2 4   ? 50.49012  31.22872  9.33433   1.000 33.73408  ?  407 LEU   D O   1 
ATOM   11807 C CB  . LEU   H  2 4   ? 48.20399  33.27464  9.57257   1.000 17.90664  ?  407 LEU   D CB  1 
ATOM   11808 C CG  . LEU   H  2 4   ? 47.83694  32.87216  11.00336  1.000 29.63535  ?  407 LEU   D CG  1 
ATOM   11809 C CD1 . LEU   H  2 4   ? 48.08168  34.04340  11.97144  1.000 16.03009  ?  407 LEU   D CD1 1 
ATOM   11810 C CD2 . LEU   H  2 4   ? 46.40298  32.38829  11.05384  1.000 21.97755  ?  407 LEU   D CD2 1 
ATOM   11811 N N   . GLY   H  2 5   ? 51.23074  32.60063  10.97934  1.000 38.74340  ?  408 GLY   D N   1 
ATOM   11812 C CA  . GLY   H  2 5   ? 52.06177  31.59313  11.62890  1.000 15.45578  ?  408 GLY   D CA  1 
ATOM   11813 C C   . GLY   H  2 5   ? 51.63028  31.25233  13.04802  1.000 30.98033  ?  408 GLY   D C   1 
ATOM   11814 O O   . GLY   H  2 5   ? 51.44536  32.14290  13.89347  1.000 37.30503  ?  408 GLY   D O   1 
ATOM   11815 N N   . LEU   H  2 6   ? 51.46225  29.95584  13.31652  1.000 12.82982  ?  409 LEU   D N   1 
ATOM   11816 C CA  . LEU   H  2 6   ? 51.07425  29.44770  14.62829  1.000 32.18532  ?  409 LEU   D CA  1 
ATOM   11817 C C   . LEU   H  2 6   ? 52.16258  28.53676  15.17992  1.000 25.58142  ?  409 LEU   D C   1 
ATOM   11818 O O   . LEU   H  2 6   ? 52.72518  27.71242  14.44549  1.000 30.64689  ?  409 LEU   D O   1 
ATOM   11819 C CB  . LEU   H  2 6   ? 49.75795  28.66917  14.55107  1.000 23.46707  ?  409 LEU   D CB  1 
ATOM   11820 C CG  . LEU   H  2 6   ? 48.61576  29.43256  13.87667  1.000 30.34218  ?  409 LEU   D CG  1 
ATOM   11821 C CD1 . LEU   H  2 6   ? 47.36456  28.57239  13.80047  1.000 16.42474  ?  409 LEU   D CD1 1 
ATOM   11822 C CD2 . LEU   H  2 6   ? 48.34011  30.77905  14.58031  1.000 11.97597  ?  409 LEU   D CD2 1 
ATOM   11823 N N   . ARG   H  2 7   ? 52.43883  28.67950  16.47634  1.000 31.17202  ?  410 ARG   D N   1 
ATOM   11824 C CA  . ARG   H  2 7   ? 53.36396  27.80399  17.19134  1.000 29.89928  ?  410 ARG   D CA  1 
ATOM   11825 C C   . ARG   H  2 7   ? 52.76612  26.39861  17.37883  1.000 35.79811  ?  410 ARG   D C   1 
ATOM   11826 O O   . ARG   H  2 7   ? 51.54302  26.21094  17.36152  1.000 47.06075  ?  410 ARG   D O   1 
ATOM   11827 C CB  . ARG   H  2 7   ? 53.71262  28.43293  18.54685  1.000 16.74887  ?  410 ARG   D CB  1 
ATOM   11828 C CG  . ARG   H  2 7   ? 54.33869  29.81019  18.40569  1.000 18.75707  ?  410 ARG   D CG  1 
ATOM   11829 C CD  . ARG   H  2 7   ? 54.57009  30.52914  19.71845  1.000 30.00250  ?  410 ARG   D CD  1 
ATOM   11830 N NE  . ARG   H  2 7   ? 53.32354  30.91091  20.36540  1.000 49.09596  ?  410 ARG   D NE  1 
ATOM   11831 C CZ  . ARG   H  2 7   ? 52.75756  30.24111  21.36180  1.000 39.95617  ?  410 ARG   D CZ  1 
ATOM   11832 N NH1 . ARG   H  2 7   ? 53.34219  29.18871  21.90995  1.000 43.32016  ?  410 ARG   D NH1 1 
ATOM   11833 N NH2 . ARG   H  2 7   ? 51.56804  30.62946  21.81195  1.000 49.18389  ?  410 ARG   D NH2 1 
ATOM   11834 N N   . LYS   H  2 8   ? 53.64675  25.39410  17.55248  1.000 36.88237  ?  411 LYS   D N   1 
ATOM   11835 C CA  . LYS   H  2 8   ? 53.16969  24.03373  17.83274  1.000 54.94304  ?  411 LYS   D CA  1 
ATOM   11836 C C   . LYS   H  2 8   ? 52.40351  23.98569  19.14438  1.000 47.16805  ?  411 LYS   D C   1 
ATOM   11837 O O   . LYS   H  2 8   ? 51.32543  23.38234  19.22096  1.000 44.07967  ?  411 LYS   D O   1 
ATOM   11838 C CB  . LYS   H  2 8   ? 54.32604  23.03020  17.87566  1.000 27.06305  ?  411 LYS   D CB  1 
ATOM   11839 N N   . ASP   H  2 9   ? 52.93578  24.64048  20.18324  1.000 41.32504  ?  412 ASP   D N   1 
ATOM   11840 C CA  . ASP   H  2 9   ? 52.28124  24.74666  21.48522  1.000 92.75351  ?  412 ASP   D CA  1 
ATOM   11841 C C   . ASP   H  2 9   ? 50.97971  25.54271  21.45499  1.000 48.07038  ?  412 ASP   D C   1 
ATOM   11842 O O   . ASP   H  2 9   ? 50.31625  25.66956  22.49311  1.000 78.64756  ?  412 ASP   D O   1 
ATOM   11843 C CB  . ASP   H  2 9   ? 53.24617  25.38031  22.48582  1.000 66.30904  ?  412 ASP   D CB  1 
ATOM   11844 C CG  . ASP   H  2 9   ? 54.35933  24.43467  22.89113  1.000 75.74232  ?  412 ASP   D CG  1 
ATOM   11845 O OD1 . ASP   H  2 9   ? 54.27729  23.22844  22.55085  1.000 78.33203  ?  412 ASP   D OD1 1 
ATOM   11846 O OD2 . ASP   H  2 9   ? 55.31328  24.89534  23.55030  1.000 100.99337 -1 412 ASP   D OD2 1 
ATOM   11847 N N   . CYS   H  2 10  ? 50.61411  26.11182  20.31936  1.000 75.63487  ?  413 CYS   D N   1 
ATOM   11848 C CA  . CYS   H  2 10  ? 49.36119  26.83391  20.21790  1.000 52.55755  ?  413 CYS   D CA  1 
ATOM   11849 C C   . CYS   H  2 10  ? 48.24385  25.82204  19.99726  1.000 63.10542  ?  413 CYS   D C   1 
ATOM   11850 O O   . CYS   H  2 10  ? 48.30026  25.01242  19.05960  1.000 61.10947  ?  413 CYS   D O   1 
ATOM   11851 C CB  . CYS   H  2 10  ? 49.43893  27.85963  19.08944  1.000 44.04500  ?  413 CYS   D CB  1 
ATOM   11852 S SG  . CYS   H  2 10  ? 47.86395  28.56374  18.55496  1.000 55.92092  ?  413 CYS   D SG  1 
ATOM   11853 N N   . ARG   H  2 11  ? 47.24526  25.85607  20.88022  1.000 49.56254  ?  414 ARG   D N   1 
ATOM   11854 C CA  . ARG   H  2 11  ? 46.11112  24.94290  20.85229  1.000 71.92778  ?  414 ARG   D CA  1 
ATOM   11855 C C   . ARG   H  2 11  ? 45.08423  25.28963  19.74898  1.000 83.25783  ?  414 ARG   D C   1 
ATOM   11856 O O   . ARG   H  2 11  ? 44.03679  24.63903  19.65470  1.000 55.80186  ?  414 ARG   D O   1 
ATOM   11857 C CB  . ARG   H  2 11  ? 45.45790  24.92045  22.24232  1.000 43.57794  ?  414 ARG   D CB  1 
ATOM   11858 N N   . ALA   H  2 12  ? 45.36065  26.27967  18.90079  1.000 56.63755  ?  415 ALA   D N   1 
ATOM   11859 C CA  . ALA   H  2 12  ? 44.48460  26.60617  17.78381  1.000 45.53788  ?  415 ALA   D CA  1 
ATOM   11860 C C   . ALA   H  2 12  ? 44.87888  25.79641  16.55810  1.000 39.41669  ?  415 ALA   D C   1 
ATOM   11861 O O   . ALA   H  2 12  ? 46.06094  25.49403  16.34655  1.000 67.06685  ?  415 ALA   D O   1 
ATOM   11862 C CB  . ALA   H  2 12  ? 44.54403  28.09806  17.45762  1.000 25.21622  ?  415 ALA   D CB  1 
ATOM   11863 N N   . GLU   H  2 13  ? 43.88266  25.45859  15.74615  1.000 33.21821  ?  416 GLU   D N   1 
ATOM   11864 C CA  . GLU   H  2 13  ? 44.07434  24.59732  14.58866  1.000 46.90166  ?  416 GLU   D CA  1 
ATOM   11865 C C   . GLU   H  2 13  ? 43.46410  25.27040  13.36412  1.000 49.20173  ?  416 GLU   D C   1 
ATOM   11866 O O   . GLU   H  2 13  ? 42.31314  25.72037  13.39859  1.000 54.36978  ?  416 GLU   D O   1 
ATOM   11867 C CB  . GLU   H  2 13  ? 43.46283  23.20211  14.81698  1.000 36.18004  ?  416 GLU   D CB  1 
ATOM   11868 C CG  . GLU   H  2 13  ? 44.09631  22.27284  15.86615  1.000 64.31234  ?  416 GLU   D CG  1 
ATOM   11869 C CD  . GLU   H  2 13  ? 44.27671  20.88945  15.29623  1.000 111.67899 ?  416 GLU   D CD  1 
ATOM   11870 O OE1 . GLU   H  2 13  ? 43.29686  20.27259  14.81813  1.000 116.07784 ?  416 GLU   D OE1 1 
ATOM   11871 O OE2 . GLU   H  2 13  ? 45.42377  20.42650  15.25507  1.000 115.31066 ?  416 GLU   D OE2 1 
ATOM   11872 N N   . ILE   H  2 14  ? 44.25489  25.35687  12.29333  1.000 37.64912  ?  417 ILE   D N   1 
ATOM   11873 C CA  . ILE   H  2 14  ? 43.77320  25.90745  11.03752  1.000 45.37496  ?  417 ILE   D CA  1 
ATOM   11874 C C   . ILE   H  2 14  ? 42.52176  25.15841  10.58187  1.000 35.51682  ?  417 ILE   D C   1 
ATOM   11875 O O   . ILE   H  2 14  ? 42.42794  23.93063  10.66905  1.000 43.85536  ?  417 ILE   D O   1 
ATOM   11876 C CB  . ILE   H  2 14  ? 44.89815  25.84769  9.98703   1.000 25.73734  ?  417 ILE   D CB  1 
ATOM   11877 C CG1 . ILE   H  2 14  ? 46.08870  26.68933  10.44550  1.000 29.10800  ?  417 ILE   D CG1 1 
ATOM   11878 C CG2 . ILE   H  2 14  ? 44.40155  26.29997  8.59895   1.000 32.75443  ?  417 ILE   D CG2 1 
ATOM   11879 C CD1 . ILE   H  2 14  ? 47.29696  26.59416  9.51980   1.000 39.17472  ?  417 ILE   D CD1 1 
ATOM   11880 N N   . VAL   H  2 15  ? 41.54941  25.91506  10.09353  1.000 46.76748  ?  418 VAL   D N   1 
ATOM   11881 C CA  . VAL   H  2 15  ? 40.29479  25.33999  9.64139   1.000 28.46709  ?  418 VAL   D CA  1 
ATOM   11882 C C   . VAL   H  2 15  ? 40.52927  24.55233  8.35765   1.000 32.26226  ?  418 VAL   D C   1 
ATOM   11883 O O   . VAL   H  2 15  ? 41.05735  25.08842  7.37292   1.000 52.36586  ?  418 VAL   D O   1 
ATOM   11884 C CB  . VAL   H  2 15  ? 39.25931  26.46142  9.46274   1.000 51.83080  ?  418 VAL   D CB  1 
ATOM   11885 C CG1 . VAL   H  2 15  ? 37.98486  25.95386  8.79097   1.000 20.14363  ?  418 VAL   D CG1 1 
ATOM   11886 C CG2 . VAL   H  2 15  ? 38.97486  27.10968  10.82316  1.000 18.41180  ?  418 VAL   D CG2 1 
ATOM   11887 N N   . GLU   H  2 16  ? 40.09751  23.27952  8.35548   1.000 42.16920  ?  419 GLU   D N   1 
ATOM   11888 C CA  . GLU   H  2 16  ? 40.53091  22.32089  7.33485   1.000 31.64045  ?  419 GLU   D CA  1 
ATOM   11889 C C   . GLU   H  2 16  ? 40.17367  22.75287  5.91841   1.000 42.08138  ?  419 GLU   D C   1 
ATOM   11890 O O   . GLU   H  2 16  ? 40.91934  22.42693  4.98676   1.000 42.20126  ?  419 GLU   D O   1 
ATOM   11891 C CB  . GLU   H  2 16  ? 39.94932  20.91829  7.58952   1.000 32.33344  ?  419 GLU   D CB  1 
ATOM   11892 N N   . LYS   H  2 17  ? 39.05160  23.46110  5.71205   1.000 34.59549  ?  420 LYS   D N   1 
ATOM   11893 C CA  . LYS   H  2 17  ? 38.68342  23.75617  4.32367   1.000 36.85207  ?  420 LYS   D CA  1 
ATOM   11894 C C   . LYS   H  2 17  ? 39.73487  24.61204  3.62810   1.000 43.37086  ?  420 LYS   D C   1 
ATOM   11895 O O   . LYS   H  2 17  ? 39.83057  24.59011  2.39219   1.000 41.77188  ?  420 LYS   D O   1 
ATOM   11896 C CB  . LYS   H  2 17  ? 37.29556  24.42810  4.21564   1.000 19.32593  ?  420 LYS   D CB  1 
ATOM   11897 C CG  . LYS   H  2 17  ? 37.11567  25.87148  4.76100   1.000 24.32605  ?  420 LYS   D CG  1 
ATOM   11898 C CD  . LYS   H  2 17  ? 36.16610  26.64304  3.81958   1.000 45.46270  ?  420 LYS   D CD  1 
ATOM   11899 C CE  . LYS   H  2 17  ? 35.41283  27.78738  4.48890   1.000 55.25898  ?  420 LYS   D CE  1 
ATOM   11900 N NZ  . LYS   H  2 17  ? 34.62928  27.28687  5.64804   1.000 78.15408  ?  420 LYS   D NZ  1 
ATOM   11901 N N   . PHE   H  2 18  ? 40.54302  25.34878  4.39516   1.000 32.47187  ?  421 PHE   D N   1 
ATOM   11902 C CA  . PHE   H  2 18  ? 41.56632  26.20140  3.80830   1.000 56.14977  ?  421 PHE   D CA  1 
ATOM   11903 C C   . PHE   H  2 18  ? 42.83171  25.44651  3.43103   1.000 43.35710  ?  421 PHE   D C   1 
ATOM   11904 O O   . PHE   H  2 18  ? 43.69664  26.02107  2.76463   1.000 38.07078  ?  421 PHE   D O   1 
ATOM   11905 C CB  . PHE   H  2 18  ? 41.89190  27.34007  4.76212   1.000 21.29790  ?  421 PHE   D CB  1 
ATOM   11906 C CG  . PHE   H  2 18  ? 40.70612  28.19174  5.06883   1.000 32.52796  ?  421 PHE   D CG  1 
ATOM   11907 C CD1 . PHE   H  2 18  ? 40.00985  28.81605  4.03445   1.000 31.96725  ?  421 PHE   D CD1 1 
ATOM   11908 C CD2 . PHE   H  2 18  ? 40.25394  28.34960  6.37283   1.000 49.35328  ?  421 PHE   D CD2 1 
ATOM   11909 C CE1 . PHE   H  2 18  ? 38.90091  29.59238  4.29987   1.000 24.28182  ?  421 PHE   D CE1 1 
ATOM   11910 C CE2 . PHE   H  2 18  ? 39.13714  29.12781  6.64830   1.000 39.73904  ?  421 PHE   D CE2 1 
ATOM   11911 C CZ  . PHE   H  2 18  ? 38.45922  29.74355  5.61063   1.000 45.41096  ?  421 PHE   D CZ  1 
ATOM   11912 N N   . THR   H  2 19  ? 42.96025  24.17106  3.79634   1.000 37.49363  ?  422 THR   D N   1 
ATOM   11913 C CA  . THR   H  2 19  ? 44.08121  23.42205  3.24861   1.000 27.71547  ?  422 THR   D CA  1 
ATOM   11914 C C   . THR   H  2 19  ? 43.89305  23.08271  1.77047   1.000 35.76322  ?  422 THR   D C   1 
ATOM   11915 O O   . THR   H  2 19  ? 44.84936  22.61363  1.14302   1.000 33.89864  ?  422 THR   D O   1 
ATOM   11916 C CB  . THR   H  2 19  ? 44.31034  22.14444  4.05328   1.000 39.34007  ?  422 THR   D CB  1 
ATOM   11917 O OG1 . THR   H  2 19  ? 43.29983  21.19292  3.72679   1.000 35.54366  ?  422 THR   D OG1 1 
ATOM   11918 C CG2 . THR   H  2 19  ? 44.24334  22.42641  5.54626   1.000 41.26150  ?  422 THR   D CG2 1 
ATOM   11919 N N   . GLU   H  2 20  ? 42.70171  23.31864  1.19046   1.000 38.81851  ?  423 GLU   D N   1 
ATOM   11920 C CA  . GLU   H  2 20  ? 42.52182  23.13643  -0.24951  1.000 37.10847  ?  423 GLU   D CA  1 
ATOM   11921 C C   . GLU   H  2 20  ? 42.84824  24.44326  -0.96616  1.000 27.55814  ?  423 GLU   D C   1 
ATOM   11922 O O   . GLU   H  2 20  ? 42.15305  25.45099  -0.75411  1.000 43.33078  ?  423 GLU   D O   1 
ATOM   11923 C CB  . GLU   H  2 20  ? 41.10365  22.68257  -0.58982  1.000 23.38257  ?  423 GLU   D CB  1 
ATOM   11924 N N   . PRO   H  2 21  ? 43.90409  24.48450  -1.76839  1.000 36.18961  ?  424 PRO   D N   1 
ATOM   11925 C CA  . PRO   H  2 21  ? 44.21437  25.70017  -2.52857  1.000 49.62961  ?  424 PRO   D CA  1 
ATOM   11926 C C   . PRO   H  2 21  ? 43.00238  26.16200  -3.31934  1.000 35.24419  ?  424 PRO   D C   1 
ATOM   11927 O O   . PRO   H  2 21  ? 42.21383  25.35164  -3.80605  1.000 43.94168  ?  424 PRO   D O   1 
ATOM   11928 C CB  . PRO   H  2 21  ? 45.34578  25.25746  -3.46443  1.000 18.13574  ?  424 PRO   D CB  1 
ATOM   11929 C CG  . PRO   H  2 21  ? 45.97808  24.09263  -2.77611  1.000 33.25438  ?  424 PRO   D CG  1 
ATOM   11930 C CD  . PRO   H  2 21  ? 44.90180  23.42212  -1.94420  1.000 31.94535  ?  424 PRO   D CD  1 
ATOM   11931 N N   . GLY   H  2 22  ? 42.85994  27.48195  -3.44243  1.000 37.45174  ?  425 GLY   D N   1 
ATOM   11932 C CA  . GLY   H  2 22  ? 41.78700  28.07575  -4.20617  1.000 20.12887  ?  425 GLY   D CA  1 
ATOM   11933 C C   . GLY   H  2 22  ? 40.53884  28.41252  -3.41054  1.000 28.76852  ?  425 GLY   D C   1 
ATOM   11934 O O   . GLY   H  2 22  ? 39.67099  29.12075  -3.92842  1.000 34.64698  ?  425 GLY   D O   1 
ATOM   11935 N N   . THR   H  2 23  ? 40.42190  27.93335  -2.17444  1.000 32.04637  ?  426 THR   D N   1 
ATOM   11936 C CA  . THR   H  2 23  ? 39.26436  28.24858  -1.34487  1.000 29.71545  ?  426 THR   D CA  1 
ATOM   11937 C C   . THR   H  2 23  ? 39.19357  29.74710  -1.03892  1.000 29.68860  ?  426 THR   D C   1 
ATOM   11938 O O   . THR   H  2 23  ? 40.20114  30.38774  -0.72958  1.000 58.95931  ?  426 THR   D O   1 
ATOM   11939 C CB  . THR   H  2 23  ? 39.33500  27.43736  -0.04396  1.000 38.38732  ?  426 THR   D CB  1 
ATOM   11940 O OG1 . THR   H  2 23  ? 39.34966  26.03471  -0.34634  1.000 46.68630  ?  426 THR   D OG1 1 
ATOM   11941 C CG2 . THR   H  2 23  ? 38.17155  27.75935  0.89530   1.000 28.82688  ?  426 THR   D CG2 1 
ATOM   11942 N N   . VAL   H  2 24  ? 37.98769  30.30464  -1.11655  1.000 50.43142  ?  427 VAL   D N   1 
ATOM   11943 C CA  . VAL   H  2 24  ? 37.80292  31.72593  -0.85871  1.000 31.59586  ?  427 VAL   D CA  1 
ATOM   11944 C C   . VAL   H  2 24  ? 37.98568  32.01728  0.62670   1.000 26.05133  ?  427 VAL   D C   1 
ATOM   11945 O O   . VAL   H  2 24  ? 37.41366  31.33777  1.49191   1.000 50.90593  ?  427 VAL   D O   1 
ATOM   11946 C CB  . VAL   H  2 24  ? 36.42466  32.17571  -1.36408  1.000 24.46415  ?  427 VAL   D CB  1 
ATOM   11947 C CG1 . VAL   H  2 24  ? 36.06195  33.53770  -0.80494  1.000 17.20356  ?  427 VAL   D CG1 1 
ATOM   11948 C CG2 . VAL   H  2 24  ? 36.44241  32.21607  -2.87506  1.000 24.41062  ?  427 VAL   D CG2 1 
ATOM   11949 N N   . ILE   H  2 25  ? 38.79122  33.03455  0.92665   1.000 54.96134  ?  428 ILE   D N   1 
ATOM   11950 C CA  . ILE   H  2 25  ? 39.04818  33.48971  2.29205   1.000 23.85804  ?  428 ILE   D CA  1 
ATOM   11951 C C   . ILE   H  2 25  ? 38.42454  34.87672  2.42120   1.000 45.27004  ?  428 ILE   D C   1 
ATOM   11952 O O   . ILE   H  2 25  ? 38.94774  35.86563  1.88938   1.000 36.57054  ?  428 ILE   D O   1 
ATOM   11953 C CB  . ILE   H  2 25  ? 40.54909  33.51862  2.63209   1.000 42.26442  ?  428 ILE   D CB  1 
ATOM   11954 C CG1 . ILE   H  2 25  ? 41.17646  32.11699  2.57013   1.000 33.13306  ?  428 ILE   D CG1 1 
ATOM   11955 C CG2 . ILE   H  2 25  ? 40.75161  34.12423  4.00320   1.000 21.09693  ?  428 ILE   D CG2 1 
ATOM   11956 C CD1 . ILE   H  2 25  ? 42.62514  32.04971  3.06963   1.000 27.76192  ?  428 ILE   D CD1 1 
ATOM   11957 N N   . ARG   H  2 26  ? 37.29318  34.95601  3.11236   1.000 38.84956  ?  429 ARG   D N   1 
ATOM   11958 C CA  . ARG   H  2 26  ? 36.65334  36.23797  3.37212   1.000 37.66193  ?  429 ARG   D CA  1 
ATOM   11959 C C   . ARG   H  2 26  ? 37.34449  36.87887  4.55981   1.000 38.19212  ?  429 ARG   D C   1 
ATOM   11960 O O   . ARG   H  2 26  ? 37.41917  36.27290  5.63515   1.000 37.23176  ?  429 ARG   D O   1 
ATOM   11961 C CB  . ARG   H  2 26  ? 35.16039  36.05820  3.64193   1.000 45.67678  ?  429 ARG   D CB  1 
ATOM   11962 C CG  . ARG   H  2 26  ? 34.41988  35.52936  2.44521   1.000 39.45484  ?  429 ARG   D CG  1 
ATOM   11963 C CD  . ARG   H  2 26  ? 32.98695  35.18444  2.75924   1.000 53.07733  ?  429 ARG   D CD  1 
ATOM   11964 N NE  . ARG   H  2 26  ? 32.15070  35.46475  1.59804   1.000 38.85991  ?  429 ARG   D NE  1 
ATOM   11965 C CZ  . ARG   H  2 26  ? 32.06678  34.67470  0.53416   1.000 171.36373 ?  429 ARG   D CZ  1 
ATOM   11966 N NH1 . ARG   H  2 26  ? 32.69409  33.50389  0.48320   1.000 34.49760  ?  429 ARG   D NH1 1 
ATOM   11967 N NH2 . ARG   H  2 26  ? 31.34220  35.06928  -0.50906  1.000 41.32422  ?  429 ARG   D NH2 1 
ATOM   11968 N N   . ILE   H  2 27  ? 37.85366  38.09781  4.36893   1.000 21.56391  ?  430 ILE   D N   1 
ATOM   11969 C CA  . ILE   H  2 27  ? 38.55874  38.76308  5.45381   1.000 38.95740  ?  430 ILE   D CA  1 
ATOM   11970 C C   . ILE   H  2 27  ? 37.65950  38.81349  6.69313   1.000 26.58879  ?  430 ILE   D C   1 
ATOM   11971 O O   . ILE   H  2 27  ? 36.43070  38.90984  6.59409   1.000 53.39077  ?  430 ILE   D O   1 
ATOM   11972 C CB  . ILE   H  2 27  ? 39.03145  40.15760  5.00005   1.000 32.46144  ?  430 ILE   D CB  1 
ATOM   11973 C CG1 . ILE   H  2 27  ? 40.11086  40.69638  5.95873   1.000 26.94581  ?  430 ILE   D CG1 1 
ATOM   11974 C CG2 . ILE   H  2 27  ? 37.82817  41.11271  4.80972   1.000 30.57600  ?  430 ILE   D CG2 1 
ATOM   11975 C CD1 . ILE   H  2 27  ? 40.76742  41.98015  5.45675   1.000 24.12929  ?  430 ILE   D CD1 1 
ATOM   11976 N N   . ASN   H  2 28  ? 38.28997  38.69955  7.86490   1.000 53.52995  ?  431 ASN   D N   1 
ATOM   11977 C CA  . ASN   H  2 28  ? 37.65388  38.62951  9.17958   1.000 32.98201  ?  431 ASN   D CA  1 
ATOM   11978 C C   . ASN   H  2 28  ? 36.96579  37.29418  9.44337   1.000 44.55007  ?  431 ASN   D C   1 
ATOM   11979 O O   . ASN   H  2 28  ? 36.51471  37.07171  10.57017  1.000 35.09504  ?  431 ASN   D O   1 
ATOM   11980 C CB  . ASN   H  2 28  ? 36.62172  39.75077  9.39345   1.000 28.65176  ?  431 ASN   D CB  1 
ATOM   11981 C CG  . ASN   H  2 28  ? 37.23298  41.13708  9.33317   1.000 40.56088  ?  431 ASN   D CG  1 
ATOM   11982 O OD1 . ASN   H  2 28  ? 38.43081  41.32057  9.55340   1.000 45.51153  ?  431 ASN   D OD1 1 
ATOM   11983 N ND2 . ASN   H  2 28  ? 36.40373  42.12664  9.02373   1.000 32.70873  ?  431 ASN   D ND2 1 
ATOM   11984 N N   . GLU   H  2 29  ? 36.84177  36.40697  8.45331   1.000 33.02080  ?  432 GLU   D N   1 
ATOM   11985 C CA  . GLU   H  2 29  ? 36.22718  35.12204  8.77193   1.000 41.66636  ?  432 GLU   D CA  1 
ATOM   11986 C C   . GLU   H  2 29  ? 37.23644  34.23114  9.51786   1.000 37.44368  ?  432 GLU   D C   1 
ATOM   11987 O O   . GLU   H  2 29  ? 38.43401  34.52784  9.58942   1.000 52.90625  ?  432 GLU   D O   1 
ATOM   11988 C CB  . GLU   H  2 29  ? 35.67624  34.46115  7.49979   1.000 25.84280  ?  432 GLU   D CB  1 
ATOM   11989 C CG  . GLU   H  2 29  ? 36.56523  33.43177  6.82454   1.000 39.12414  ?  432 GLU   D CG  1 
ATOM   11990 C CD  . GLU   H  2 29  ? 35.84827  32.64868  5.71386   1.000 63.50288  ?  432 GLU   D CD  1 
ATOM   11991 O OE1 . GLU   H  2 29  ? 35.86576  33.09940  4.54613   1.000 48.51699  ?  432 GLU   D OE1 1 
ATOM   11992 O OE2 . GLU   H  2 29  ? 35.27999  31.56567  6.00461   1.000 54.76978  -1 432 GLU   D OE2 1 
ATOM   11993 N N   . VAL   H  2 30  ? 36.73652  33.16170  10.13170  1.000 41.57427  ?  433 VAL   D N   1 
ATOM   11994 C CA  . VAL   H  2 30  ? 37.56190  32.32470  11.00621  1.000 16.89124  ?  433 VAL   D CA  1 
ATOM   11995 C C   . VAL   H  2 30  ? 38.45110  31.42025  10.15864  1.000 36.99344  ?  433 VAL   D C   1 
ATOM   11996 O O   . VAL   H  2 30  ? 37.94722  30.61212  9.36888   1.000 27.82994  ?  433 VAL   D O   1 
ATOM   11997 C CB  . VAL   H  2 30  ? 36.68284  31.48801  11.95178  1.000 37.84311  ?  433 VAL   D CB  1 
ATOM   11998 C CG1 . VAL   H  2 30  ? 37.53469  30.59314  12.86079  1.000 27.67070  ?  433 VAL   D CG1 1 
ATOM   11999 C CG2 . VAL   H  2 30  ? 35.74723  32.38136  12.77741  1.000 22.44634  ?  433 VAL   D CG2 1 
ATOM   12000 N N   . VAL   H  2 31  ? 39.77462  31.53581  10.33253  1.000 31.51932  ?  434 VAL   D N   1 
ATOM   12001 C CA  . VAL   H  2 31  ? 40.70884  30.62728  9.66926   1.000 42.60079  ?  434 VAL   D CA  1 
ATOM   12002 C C   . VAL   H  2 31  ? 41.39153  29.66870  10.64296  1.000 30.19757  ?  434 VAL   D C   1 
ATOM   12003 O O   . VAL   H  2 31  ? 41.93440  28.64286  10.19856  1.000 29.37923  ?  434 VAL   D O   1 
ATOM   12004 C CB  . VAL   H  2 31  ? 41.76873  31.37721  8.82430   1.000 32.92089  ?  434 VAL   D CB  1 
ATOM   12005 C CG1 . VAL   H  2 31  ? 41.12290  32.09232  7.64495   1.000 16.68528  ?  434 VAL   D CG1 1 
ATOM   12006 C CG2 . VAL   H  2 31  ? 42.59034  32.37355  9.67974   1.000 19.26421  ?  434 VAL   D CG2 1 
ATOM   12007 N N   . ALA   H  2 32  ? 41.37476  29.94963  11.94140  1.000 34.19378  ?  435 ALA   D N   1 
ATOM   12008 C CA  . ALA   H  2 32  ? 41.86431  28.99700  12.92939  1.000 37.47141  ?  435 ALA   D CA  1 
ATOM   12009 C C   . ALA   H  2 32  ? 41.09340  29.21371  14.22445  1.000 47.41380  ?  435 ALA   D C   1 
ATOM   12010 O O   . ALA   H  2 32  ? 40.66491  30.33529  14.52790  1.000 39.48367  ?  435 ALA   D O   1 
ATOM   12011 C CB  . ALA   H  2 32  ? 43.37306  29.13578  13.17783  1.000 31.16905  ?  435 ALA   D CB  1 
ATOM   12012 N N   . ALA   H  2 33  ? 40.92985  28.13206  14.98850  1.000 30.25265  ?  436 ALA   D N   1 
ATOM   12013 C CA  . ALA   H  2 33  ? 40.14488  28.15592  16.21646  1.000 39.25105  ?  436 ALA   D CA  1 
ATOM   12014 C C   . ALA   H  2 33  ? 40.70469  27.14385  17.20344  1.000 58.87323  ?  436 ALA   D C   1 
ATOM   12015 O O   . ALA   H  2 33  ? 41.28642  26.12825  16.80893  1.000 36.26948  ?  436 ALA   D O   1 
ATOM   12016 C CB  . ALA   H  2 33  ? 38.67369  27.83915  15.95553  1.000 23.35378  ?  436 ALA   D CB  1 
ATOM   12017 N N   . LEU   H  2 34  ? 40.50099  27.42399  18.48967  1.000 34.79220  ?  437 LEU   D N   1 
ATOM   12018 C CA  . LEU   H  2 34  ? 40.93888  26.54548  19.57510  1.000 64.51664  ?  437 LEU   D CA  1 
ATOM   12019 C C   . LEU   H  2 34  ? 40.21818  25.19295  19.59148  1.000 32.38682  ?  437 LEU   D C   1 
ATOM   12020 O O   . LEU   H  2 34  ? 38.99358  25.12850  19.55966  1.000 39.12457  ?  437 LEU   D O   1 
ATOM   12021 C CB  . LEU   H  2 34  ? 40.74247  27.24838  20.92411  1.000 31.20838  ?  437 LEU   D CB  1 
ATOM   12022 C CG  . LEU   H  2 34  ? 41.74601  28.35369  21.28714  1.000 56.33137  ?  437 LEU   D CG  1 
ATOM   12023 C CD1 . LEU   H  2 34  ? 41.38933  29.06369  22.62036  1.000 37.48610  ?  437 LEU   D CD1 1 
ATOM   12024 C CD2 . LEU   H  2 34  ? 43.18542  27.80767  21.29055  1.000 59.08565  ?  437 LEU   D CD2 1 
ATOM   12025 N N   . LEU   I  1 57  ? -4.08963  -10.71611 22.95036  1.000 58.58803  ?  57  LEU   E N   1 
ATOM   12026 C CA  . LEU   I  1 57  ? -4.42666  -10.44752 24.34432  1.000 55.48536  ?  57  LEU   E CA  1 
ATOM   12027 C C   . LEU   I  1 57  ? -5.18676  -11.61520 24.93265  1.000 71.62747  ?  57  LEU   E C   1 
ATOM   12028 O O   . LEU   I  1 57  ? -6.08334  -12.15256 24.28483  1.000 73.62133  ?  57  LEU   E O   1 
ATOM   12029 C CB  . LEU   I  1 57  ? -5.30428  -9.20120  24.48120  1.000 52.13058  ?  57  LEU   E CB  1 
ATOM   12030 C CG  . LEU   I  1 57  ? -4.82148  -7.79493  24.13182  1.000 68.39427  ?  57  LEU   E CG  1 
ATOM   12031 C CD1 . LEU   I  1 57  ? -5.99129  -6.82154  24.27149  1.000 60.78032  ?  57  LEU   E CD1 1 
ATOM   12032 C CD2 . LEU   I  1 57  ? -3.63626  -7.35358  24.98373  1.000 66.85912  ?  57  LEU   E CD2 1 
ATOM   12033 N N   . MET   I  1 58  ? -4.87407  -11.97587 26.17582  1.000 64.83753  ?  58  MET   E N   1 
ATOM   12034 C CA  . MET   I  1 58  ? -5.61022  -13.05424 26.82234  1.000 63.73624  ?  58  MET   E CA  1 
ATOM   12035 C C   . MET   I  1 58  ? -7.06126  -12.64837 27.04739  1.000 54.44462  ?  58  MET   E C   1 
ATOM   12036 O O   . MET   I  1 58  ? -7.37142  -11.47847 27.28160  1.000 75.11021  ?  58  MET   E O   1 
ATOM   12037 C CB  . MET   I  1 58  ? -4.95456  -13.43416 28.14431  1.000 56.67874  ?  58  MET   E CB  1 
ATOM   12038 C CG  . MET   I  1 58  ? -4.69040  -12.28156 29.09042  1.000 71.98046  ?  58  MET   E CG  1 
ATOM   12039 S SD  . MET   I  1 58  ? -3.94569  -12.88016 30.62196  1.000 77.84551  ?  58  MET   E SD  1 
ATOM   12040 C CE  . MET   I  1 58  ? -2.23777  -13.09980 30.09696  1.000 54.47228  ?  58  MET   E CE  1 
ATOM   12041 N N   . GLN   I  1 59  ? -7.95664  -13.63167 26.97222  1.000 67.88867  ?  59  GLN   E N   1 
ATOM   12042 C CA  . GLN   I  1 59  ? -9.39476  -13.36140 26.99823  1.000 56.72691  ?  59  GLN   E CA  1 
ATOM   12043 C C   . GLN   I  1 59  ? -9.84253  -12.45236 28.14042  1.000 66.45645  ?  59  GLN   E C   1 
ATOM   12044 O O   . GLN   I  1 59  ? -10.63963 -11.53692 27.88183  1.000 60.50696  ?  59  GLN   E O   1 
ATOM   12045 C CB  . GLN   I  1 59  ? -10.17971 -14.68008 27.05796  1.000 50.47685  ?  59  GLN   E CB  1 
ATOM   12046 C CG  . GLN   I  1 59  ? -11.63370 -14.50192 26.69912  1.000 80.02872  ?  59  GLN   E CG  1 
ATOM   12047 C CD  . GLN   I  1 59  ? -11.77621 -13.98927 25.27627  1.000 102.62064 ?  59  GLN   E CD  1 
ATOM   12048 O OE1 . GLN   I  1 59  ? -10.96479 -14.31760 24.40525  1.000 114.20428 ?  59  GLN   E OE1 1 
ATOM   12049 N NE2 . GLN   I  1 59  ? -12.79293 -13.16253 25.03373  1.000 87.24731  ?  59  GLN   E NE2 1 
ATOM   12050 N N   . PRO   I  1 60  ? -9.39951  -12.63310 29.39596  1.000 55.74415  ?  60  PRO   E N   1 
ATOM   12051 C CA  . PRO   I  1 60  ? -9.85295  -11.70434 30.45212  1.000 37.46396  ?  60  PRO   E CA  1 
ATOM   12052 C C   . PRO   I  1 60  ? -9.53877  -10.24862 30.14536  1.000 61.55208  ?  60  PRO   E C   1 
ATOM   12053 O O   . PRO   I  1 60  ? -10.36515 -9.37360  30.44747  1.000 40.65547  ?  60  PRO   E O   1 
ATOM   12054 C CB  . PRO   I  1 60  ? -9.11606  -12.20899 31.70104  1.000 38.22754  ?  60  PRO   E CB  1 
ATOM   12055 C CG  . PRO   I  1 60  ? -8.81269  -13.64507 31.41544  1.000 45.21610  ?  60  PRO   E CG  1 
ATOM   12056 C CD  . PRO   I  1 60  ? -8.51874  -13.68327 29.93916  1.000 33.49539  ?  60  PRO   E CD  1 
ATOM   12057 N N   . ILE   I  1 61  ? -8.37733  -9.96675  29.53822  1.000 39.17319  ?  61  ILE   E N   1 
ATOM   12058 C CA  . ILE   I  1 61  ? -8.06827  -8.59675  29.12551  1.000 63.50679  ?  61  ILE   E CA  1 
ATOM   12059 C C   . ILE   I  1 61  ? -8.96012  -8.15775  27.97278  1.000 49.82598  ?  61  ILE   E C   1 
ATOM   12060 O O   . ILE   I  1 61  ? -9.34258  -6.98447  27.88627  1.000 54.15996  ?  61  ILE   E O   1 
ATOM   12061 C CB  . ILE   I  1 61  ? -6.57958  -8.45578  28.76295  1.000 49.39742  ?  61  ILE   E CB  1 
ATOM   12062 C CG1 . ILE   I  1 61  ? -5.71918  -8.83187  29.96739  1.000 39.94928  ?  61  ILE   E CG1 1 
ATOM   12063 C CG2 . ILE   I  1 61  ? -6.25105  -7.02074  28.31386  1.000 38.08650  ?  61  ILE   E CG2 1 
ATOM   12064 C CD1 . ILE   I  1 61  ? -4.25889  -8.67161  29.71429  1.000 46.53806  ?  61  ILE   E CD1 1 
ATOM   12065 N N   . GLN   I  1 62  ? -9.33312  -9.03650  27.05968  1.000 62.21106  ?  62  GLN   E N   1 
ATOM   12066 C CA  . GLN   I  1 62  ? -10.24957 -8.56408  26.03029  1.000 31.77332  ?  62  GLN   E CA  1 
ATOM   12067 C C   . GLN   I  1 62  ? -11.59909 -8.22557  26.63082  1.000 86.74525  ?  62  GLN   E C   1 
ATOM   12068 O O   . GLN   I  1 62  ? -12.18499 -7.17368  26.32899  1.000 29.46103  ?  62  GLN   E O   1 
ATOM   12069 C CB  . GLN   I  1 62  ? -10.43046 -9.60303  24.95089  1.000 81.75985  ?  62  GLN   E CB  1 
ATOM   12070 C CG  . GLN   I  1 62  ? -9.28587  -9.81020  24.04546  1.000 101.44219 ?  62  GLN   E CG  1 
ATOM   12071 C CD  . GLN   I  1 62  ? -9.67643  -10.84013 23.03820  1.000 146.72179 ?  62  GLN   E CD  1 
ATOM   12072 O OE1 . GLN   I  1 62  ? -9.24930  -11.99033 23.11118  1.000 148.87048 ?  62  GLN   E OE1 1 
ATOM   12073 N NE2 . GLN   I  1 62  ? -10.55082 -10.45182 22.11338  1.000 148.68966 ?  62  GLN   E NE2 1 
ATOM   12074 N N   . GLU   I  1 63  ? -12.12822 -9.12622  27.47925  1.000 44.76264  ?  63  GLU   E N   1 
ATOM   12075 C CA  . GLU   I  1 63  ? -13.41020 -8.78919  28.09386  1.000 60.59941  ?  63  GLU   E CA  1 
ATOM   12076 C C   . GLU   I  1 63  ? -13.31762 -7.48567  28.87628  1.000 62.81882  ?  63  GLU   E C   1 
ATOM   12077 O O   . GLU   I  1 63  ? -14.26706 -6.69175  28.88653  1.000 56.13926  ?  63  GLU   E O   1 
ATOM   12078 C CB  . GLU   I  1 63  ? -13.87417 -9.92525  28.99060  1.000 44.71900  ?  63  GLU   E CB  1 
ATOM   12079 C CG  . GLU   I  1 63  ? -14.68442 -10.98091 28.25861  1.000 82.29389  ?  63  GLU   E CG  1 
ATOM   12080 C CD  . GLU   I  1 63  ? -14.31140 -12.39073 28.65597  1.000 69.08619  ?  63  GLU   E CD  1 
ATOM   12081 O OE1 . GLU   I  1 63  ? -13.59015 -12.55971 29.66547  1.000 115.54567 ?  63  GLU   E OE1 1 
ATOM   12082 O OE2 . GLU   I  1 63  ? -14.74009 -13.33630 27.95656  1.000 143.13920 -1 63  GLU   E OE2 1 
ATOM   12083 N N   . PHE   I  1 64  ? -12.17065 -7.25122  29.52916  1.000 51.21368  ?  64  PHE   E N   1 
ATOM   12084 C CA  . PHE   I  1 64  ? -11.91140 -5.98657  30.21242  1.000 44.66232  ?  64  PHE   E CA  1 
ATOM   12085 C C   . PHE   I  1 64  ? -12.00876 -4.81442  29.24393  1.000 58.69905  ?  64  PHE   E C   1 
ATOM   12086 O O   . PHE   I  1 64  ? -12.75696 -3.85683  29.48013  1.000 53.25816  ?  64  PHE   E O   1 
ATOM   12087 C CB  . PHE   I  1 64  ? -10.53004 -6.05188  30.87154  1.000 47.75631  ?  64  PHE   E CB  1 
ATOM   12088 C CG  . PHE   I  1 64  ? -10.06596 -4.76038  31.49349  1.000 52.92905  ?  64  PHE   E CG  1 
ATOM   12089 C CD1 . PHE   I  1 64  ? -10.63741 -4.28811  32.66171  1.000 60.87413  ?  64  PHE   E CD1 1 
ATOM   12090 C CD2 . PHE   I  1 64  ? -9.01674  -4.04151  30.93003  1.000 41.96378  ?  64  PHE   E CD2 1 
ATOM   12091 C CE1 . PHE   I  1 64  ? -10.18570 -3.10343  33.24151  1.000 46.86605  ?  64  PHE   E CE1 1 
ATOM   12092 C CE2 . PHE   I  1 64  ? -8.54968  -2.86436  31.50840  1.000 40.21434  ?  64  PHE   E CE2 1 
ATOM   12093 C CZ  . PHE   I  1 64  ? -9.13223  -2.39380  32.66345  1.000 48.95180  ?  64  PHE   E CZ  1 
ATOM   12094 N N   . LYS   I  1 65  ? -11.25825 -4.88539  28.13471  1.000 46.64345  ?  65  LYS   E N   1 
ATOM   12095 C CA  . LYS   I  1 65  ? -11.32231 -3.85307  27.09564  1.000 41.58009  ?  65  LYS   E CA  1 
ATOM   12096 C C   . LYS   I  1 65  ? -12.73380 -3.71066  26.52684  1.000 61.76641  ?  65  LYS   E C   1 
ATOM   12097 O O   . LYS   I  1 65  ? -13.21132 -2.59401  26.28613  1.000 53.32210  ?  65  LYS   E O   1 
ATOM   12098 C CB  . LYS   I  1 65  ? -10.32604 -4.17609  25.98034  1.000 48.83728  ?  65  LYS   E CB  1 
ATOM   12099 C CG  . LYS   I  1 65  ? -10.24084 -3.14610  24.86427  1.000 49.87233  ?  65  LYS   E CG  1 
ATOM   12100 C CD  . LYS   I  1 65  ? -8.86375  -3.19774  24.22698  1.000 60.40653  ?  65  LYS   E CD  1 
ATOM   12101 C CE  . LYS   I  1 65  ? -8.90848  -3.71316  22.81366  1.000 68.15973  ?  65  LYS   E CE  1 
ATOM   12102 N NZ  . LYS   I  1 65  ? -8.28664  -2.70823  21.91759  1.000 79.22449  ?  65  LYS   E NZ  1 
ATOM   12103 N N   . ALA   I  1 66  ? -13.41629 -4.83428  26.29541  1.000 53.61602  ?  66  ALA   E N   1 
ATOM   12104 C CA  . ALA   I  1 66  ? -14.77154 -4.76109  25.76073  1.000 56.85001  ?  66  ALA   E CA  1 
ATOM   12105 C C   . ALA   I  1 66  ? -15.70758 -4.05809  26.73966  1.000 67.16435  ?  66  ALA   E C   1 
ATOM   12106 O O   . ALA   I  1 66  ? -16.64462 -3.35221  26.33269  1.000 51.58805  ?  66  ALA   E O   1 
ATOM   12107 C CB  . ALA   I  1 66  ? -15.27560 -6.16448  25.43489  1.000 34.14332  ?  66  ALA   E CB  1 
ATOM   12108 N N   . PHE   I  1 67  ? -15.46101 -4.22945  28.03880  1.000 70.13817  ?  67  PHE   E N   1 
ATOM   12109 C CA  . PHE   I  1 67  ? -16.30294 -3.57185  29.02501  1.000 48.58747  ?  67  PHE   E CA  1 
ATOM   12110 C C   . PHE   I  1 67  ? -16.08616 -2.06301  28.99573  1.000 64.57267  ?  67  PHE   E C   1 
ATOM   12111 O O   . PHE   I  1 67  ? -17.05137 -1.28830  28.97558  1.000 60.84343  ?  67  PHE   E O   1 
ATOM   12112 C CB  . PHE   I  1 67  ? -16.03892 -4.14052  30.42350  1.000 49.80391  ?  67  PHE   E CB  1 
ATOM   12113 C CG  . PHE   I  1 67  ? -16.70374 -3.35565  31.49525  1.000 50.77877  ?  67  PHE   E CG  1 
ATOM   12114 C CD1 . PHE   I  1 67  ? -18.06472 -3.50536  31.71075  1.000 37.16380  ?  67  PHE   E CD1 1 
ATOM   12115 C CD2 . PHE   I  1 67  ? -15.99077 -2.40171  32.23680  1.000 44.73913  ?  67  PHE   E CD2 1 
ATOM   12116 C CE1 . PHE   I  1 67  ? -18.72208 -2.74665  32.67438  1.000 44.30207  ?  67  PHE   E CE1 1 
ATOM   12117 C CE2 . PHE   I  1 67  ? -16.63059 -1.62244  33.19461  1.000 54.62705  ?  67  PHE   E CE2 1 
ATOM   12118 C CZ  . PHE   I  1 67  ? -17.99854 -1.79521  33.42383  1.000 41.68197  ?  67  PHE   E CZ  1 
ATOM   12119 N N   . ILE   I  1 68  ? -14.81985 -1.63247  28.99373  1.000 52.31858  ?  68  ILE   E N   1 
ATOM   12120 C CA  . ILE   I  1 68  ? -14.49025 -0.20899  28.90913  1.000 54.50085  ?  68  ILE   E CA  1 
ATOM   12121 C C   . ILE   I  1 68  ? -15.21977 0.43942   27.74166  1.000 60.58811  ?  68  ILE   E C   1 
ATOM   12122 O O   . ILE   I  1 68  ? -15.75082 1.55198   27.84975  1.000 58.22011  ?  68  ILE   E O   1 
ATOM   12123 C CB  . ILE   I  1 68  ? -12.96378 -0.03490  28.78005  1.000 44.41811  ?  68  ILE   E CB  1 
ATOM   12124 C CG1 . ILE   I  1 68  ? -12.26136 -0.50783  30.06216  1.000 51.51680  ?  68  ILE   E CG1 1 
ATOM   12125 C CG2 . ILE   I  1 68  ? -12.60556 1.40004   28.44618  1.000 49.80900  ?  68  ILE   E CG2 1 
ATOM   12126 C CD1 . ILE   I  1 68  ? -10.76762 -0.51408  29.97220  1.000 44.49516  ?  68  ILE   E CD1 1 
ATOM   12127 N N   . GLU   I  1 69  ? -15.26376 -0.25736  26.60943  1.000 81.06424  ?  69  GLU   E N   1 
ATOM   12128 C CA  . GLU   I  1 69  ? -15.87449 0.24731   25.39124  1.000 55.62721  ?  69  GLU   E CA  1 
ATOM   12129 C C   . GLU   I  1 69  ? -17.39081 0.10468   25.38747  1.000 64.97777  ?  69  GLU   E C   1 
ATOM   12130 O O   . GLU   I  1 69  ? -18.05453 0.78465   24.60307  1.000 65.48512  ?  69  GLU   E O   1 
ATOM   12131 C CB  . GLU   I  1 69  ? -15.27144 -0.48753  24.19285  1.000 61.96727  ?  69  GLU   E CB  1 
ATOM   12132 C CG  . GLU   I  1 69  ? -13.85691 -0.02059  23.85038  1.000 47.97460  ?  69  GLU   E CG  1 
ATOM   12133 C CD  . GLU   I  1 69  ? -13.06982 -1.01644  22.99578  1.000 89.18513  ?  69  GLU   E CD  1 
ATOM   12134 O OE1 . GLU   I  1 69  ? -13.58552 -2.13484  22.72183  1.000 61.63309  ?  69  GLU   E OE1 1 
ATOM   12135 O OE2 . GLU   I  1 69  ? -11.92401 -0.67179  22.60972  1.000 68.43941  -1 69  GLU   E OE2 1 
ATOM   12136 N N   . SER   I  1 70  ? -17.94992 -0.74172  26.25427  1.000 66.01246  ?  70  SER   E N   1 
ATOM   12137 C CA  . SER   I  1 70  ? -19.38388 -1.00323  26.26119  1.000 37.79413  ?  70  SER   E CA  1 
ATOM   12138 C C   . SER   I  1 70  ? -20.21607 0.12862   26.85600  1.000 66.55630  ?  70  SER   E C   1 
ATOM   12139 O O   . SER   I  1 70  ? -21.43677 0.12706   26.66924  1.000 51.28918  ?  70  SER   E O   1 
ATOM   12140 C CB  . SER   I  1 70  ? -19.68547 -2.28254  27.04879  1.000 50.39311  ?  70  SER   E CB  1 
ATOM   12141 O OG  . SER   I  1 70  ? -19.43932 -2.08979  28.43745  1.000 71.73052  ?  70  SER   E OG  1 
ATOM   12142 N N   . ASP   I  1 71  ? -19.61129 1.06628   27.58587  1.000 46.68778  ?  71  ASP   E N   1 
ATOM   12143 C CA  . ASP   I  1 71  ? -20.35679 2.11312   28.28952  1.000 41.97016  ?  71  ASP   E CA  1 
ATOM   12144 C C   . ASP   I  1 71  ? -19.67477 3.44035   27.98889  1.000 48.23911  ?  71  ASP   E C   1 
ATOM   12145 O O   . ASP   I  1 71  ? -18.50145 3.63962   28.37736  1.000 48.14229  ?  71  ASP   E O   1 
ATOM   12146 C CB  . ASP   I  1 71  ? -20.41719 1.84062   29.80272  1.000 51.13568  ?  71  ASP   E CB  1 
ATOM   12147 C CG  . ASP   I  1 71  ? -21.16493 2.93669   30.60659  1.000 90.39555  ?  71  ASP   E CG  1 
ATOM   12148 O OD1 . ASP   I  1 71  ? -21.21536 4.12794   30.19932  1.000 54.31967  ?  71  ASP   E OD1 1 
ATOM   12149 O OD2 . ASP   I  1 71  ? -21.69417 2.60387   31.69267  1.000 68.22463  -1 71  ASP   E OD2 1 
ATOM   12150 N N   . PRO   I  1 72  ? -20.36116 4.37413   27.34047  1.000 58.95218  ?  72  PRO   E N   1 
ATOM   12151 C CA  . PRO   I  1 72  ? -19.69910 5.63212   26.95298  1.000 57.20090  ?  72  PRO   E CA  1 
ATOM   12152 C C   . PRO   I  1 72  ? -19.14604 6.42850   28.12956  1.000 48.05412  ?  72  PRO   E C   1 
ATOM   12153 O O   . PRO   I  1 72  ? -18.13422 7.12016   27.96924  1.000 53.79320  ?  72  PRO   E O   1 
ATOM   12154 C CB  . PRO   I  1 72  ? -20.80988 6.39375   26.21646  1.000 43.41912  ?  72  PRO   E CB  1 
ATOM   12155 C CG  . PRO   I  1 72  ? -22.10250 5.75676   26.68802  1.000 49.26382  ?  72  PRO   E CG  1 
ATOM   12156 C CD  . PRO   I  1 72  ? -21.78472 4.32583   26.96995  1.000 35.21911  ?  72  PRO   E CD  1 
ATOM   12157 N N   . VAL   I  1 73  ? -19.76758 6.35396   29.30962  1.000 51.03789  ?  73  VAL   E N   1 
ATOM   12158 C CA  . VAL   I  1 73  ? -19.24159 7.07405   30.46870  1.000 62.02330  ?  73  VAL   E CA  1 
ATOM   12159 C C   . VAL   I  1 73  ? -17.94081 6.44374   30.94889  1.000 69.61846  ?  73  VAL   E C   1 
ATOM   12160 O O   . VAL   I  1 73  ? -16.95991 7.14737   31.22906  1.000 40.63776  ?  73  VAL   E O   1 
ATOM   12161 C CB  . VAL   I  1 73  ? -20.28038 7.10745   31.59810  1.000 58.76715  ?  73  VAL   E CB  1 
ATOM   12162 C CG1 . VAL   I  1 73  ? -19.74803 7.91657   32.74774  1.000 35.81873  ?  73  VAL   E CG1 1 
ATOM   12163 C CG2 . VAL   I  1 73  ? -21.57388 7.68739   31.10007  1.000 33.65717  ?  73  VAL   E CG2 1 
ATOM   12164 N N   . VAL   I  1 74  ? -17.93216 5.11043   31.08607  1.000 54.62932  ?  74  VAL   E N   1 
ATOM   12165 C CA  . VAL   I  1 74  ? -16.71795 4.38666   31.45747  1.000 45.22668  ?  74  VAL   E CA  1 
ATOM   12166 C C   . VAL   I  1 74  ? -15.61667 4.66608   30.44506  1.000 56.05902  ?  74  VAL   E C   1 
ATOM   12167 O O   . VAL   I  1 74  ? -14.48184 5.00938   30.80541  1.000 60.68887  ?  74  VAL   E O   1 
ATOM   12168 C CB  . VAL   I  1 74  ? -17.01123 2.87628   31.56451  1.000 47.35322  ?  74  VAL   E CB  1 
ATOM   12169 C CG1 . VAL   I  1 74  ? -15.73698 2.06682   31.83828  1.000 30.28135  ?  74  VAL   E CG1 1 
ATOM   12170 C CG2 . VAL   I  1 74  ? -18.02064 2.62153   32.63223  1.000 37.11796  ?  74  VAL   E CG2 1 
ATOM   12171 N N   . HIS   I  1 75  ? -15.94657 4.52524   29.15789  1.000 62.91072  ?  75  HIS   E N   1 
ATOM   12172 C CA  . HIS   I  1 75  ? -14.99253 4.79593   28.08776  1.000 55.61120  ?  75  HIS   E CA  1 
ATOM   12173 C C   . HIS   I  1 75  ? -14.38125 6.18887   28.22803  1.000 44.45186  ?  75  HIS   E C   1 
ATOM   12174 O O   . HIS   I  1 75  ? -13.15795 6.36229   28.14400  1.000 51.36655  ?  75  HIS   E O   1 
ATOM   12175 C CB  . HIS   I  1 75  ? -15.70287 4.64617   26.74539  1.000 47.18402  ?  75  HIS   E CB  1 
ATOM   12176 C CG  . HIS   I  1 75  ? -14.77825 4.55275   25.57726  1.000 80.01169  ?  75  HIS   E CG  1 
ATOM   12177 N ND1 . HIS   I  1 75  ? -15.12681 3.91472   24.40942  1.000 89.45962  ?  75  HIS   E ND1 1 
ATOM   12178 C CD2 . HIS   I  1 75  ? -13.51815 5.01119   25.39668  1.000 81.45909  ?  75  HIS   E CD2 1 
ATOM   12179 C CE1 . HIS   I  1 75  ? -14.11801 3.97989   23.56092  1.000 76.95210  ?  75  HIS   E CE1 1 
ATOM   12180 N NE2 . HIS   I  1 75  ? -13.13222 4.64570   24.13283  1.000 63.63193  ?  75  HIS   E NE2 1 
ATOM   12181 N N   . GLN   I  1 76  ? -15.22548 7.19784   28.45497  1.000 57.49103  ?  76  GLN   E N   1 
ATOM   12182 C CA  . GLN   I  1 76  ? -14.71730 8.55476   28.60621  1.000 36.16612  ?  76  GLN   E CA  1 
ATOM   12183 C C   . GLN   I  1 76  ? -13.76250 8.64937   29.79189  1.000 59.36022  ?  76  GLN   E C   1 
ATOM   12184 O O   . GLN   I  1 76  ? -12.71919 9.30866   29.70554  1.000 48.62720  ?  76  GLN   E O   1 
ATOM   12185 C CB  . GLN   I  1 76  ? -15.88487 9.53413   28.75705  1.000 61.58704  ?  76  GLN   E CB  1 
ATOM   12186 C CG  . GLN   I  1 76  ? -15.48277 10.98727  28.58169  1.000 37.56508  ?  76  GLN   E CG  1 
ATOM   12187 C CD  . GLN   I  1 76  ? -14.74303 11.23377  27.28568  1.000 95.83412  ?  76  GLN   E CD  1 
ATOM   12188 O OE1 . GLN   I  1 76  ? -15.24802 10.92592  26.20210  1.000 55.48059  ?  76  GLN   E OE1 1 
ATOM   12189 N NE2 . GLN   I  1 76  ? -13.53806 11.78759  27.38710  1.000 47.55589  ?  76  GLN   E NE2 1 
ATOM   12190 N N   . GLU   I  1 77  ? -14.09480 7.97679   30.90239  1.000 51.41014  ?  77  GLU   E N   1 
ATOM   12191 C CA  . GLU   I  1 77  ? -13.19109 7.94575   32.04715  1.000 42.40396  ?  77  GLU   E CA  1 
ATOM   12192 C C   . GLU   I  1 77  ? -11.83582 7.35543   31.66323  1.000 69.76477  ?  77  GLU   E C   1 
ATOM   12193 O O   . GLU   I  1 77  ? -10.78652 7.87051   32.07695  1.000 36.37040  ?  77  GLU   E O   1 
ATOM   12194 C CB  . GLU   I  1 77  ? -13.82957 7.16386   33.19150  1.000 41.94488  ?  77  GLU   E CB  1 
ATOM   12195 C CG  . GLU   I  1 77  ? -14.82645 7.99888   33.98104  1.000 37.04056  ?  77  GLU   E CG  1 
ATOM   12196 C CD  . GLU   I  1 77  ? -15.79320 7.17576   34.83449  1.000 69.42959  ?  77  GLU   E CD  1 
ATOM   12197 O OE1 . GLU   I  1 77  ? -15.72110 5.92214   34.78691  1.000 51.08855  ?  77  GLU   E OE1 1 
ATOM   12198 O OE2 . GLU   I  1 77  ? -16.62441 7.79658   35.55542  1.000 44.84657  -1 77  GLU   E OE2 1 
ATOM   12199 N N   . PHE   I  1 78  ? -11.83180 6.30384   30.83312  1.000 38.45222  ?  78  PHE   E N   1 
ATOM   12200 C CA  . PHE   I  1 78  ? -10.58266 5.69011   30.38703  1.000 59.51904  ?  78  PHE   E CA  1 
ATOM   12201 C C   . PHE   I  1 78  ? -9.90180  6.47795   29.28050  1.000 58.78628  ?  78  PHE   E C   1 
ATOM   12202 O O   . PHE   I  1 78  ? -8.85900  6.04824   28.77524  1.000 66.44786  ?  78  PHE   E O   1 
ATOM   12203 C CB  . PHE   I  1 78  ? -10.81048 4.24156   29.92801  1.000 40.09701  ?  78  PHE   E CB  1 
ATOM   12204 C CG  . PHE   I  1 78  ? -10.73007 3.26040   31.04093  1.000 58.55596  ?  78  PHE   E CG  1 
ATOM   12205 C CD1 . PHE   I  1 78  ? -9.49493  2.76176   31.44602  1.000 44.89398  ?  78  PHE   E CD1 1 
ATOM   12206 C CD2 . PHE   I  1 78  ? -11.88228 2.87796   31.73351  1.000 33.34509  ?  78  PHE   E CD2 1 
ATOM   12207 C CE1 . PHE   I  1 78  ? -9.40398  1.85781   32.50720  1.000 42.79431  ?  78  PHE   E CE1 1 
ATOM   12208 C CE2 . PHE   I  1 78  ? -11.80896 1.98122   32.80148  1.000 53.12886  ?  78  PHE   E CE2 1 
ATOM   12209 C CZ  . PHE   I  1 78  ? -10.56787 1.46280   33.19238  1.000 40.53572  ?  78  PHE   E CZ  1 
ATOM   12210 N N   . ILE   I  1 79  ? -10.44763 7.62042   28.89334  1.000 49.82699  ?  79  ILE   E N   1 
ATOM   12211 C CA  . ILE   I  1 79  ? -9.72312  8.57232   28.08061  1.000 43.47687  ?  79  ILE   E CA  1 
ATOM   12212 C C   . ILE   I  1 79  ? -9.19491  9.71155   28.93500  1.000 60.21236  ?  79  ILE   E C   1 
ATOM   12213 O O   . ILE   I  1 79  ? -7.99270  9.98230   28.95654  1.000 36.54652  ?  79  ILE   E O   1 
ATOM   12214 C CB  . ILE   I  1 79  ? -10.61306 9.09683   26.93102  1.000 52.24169  ?  79  ILE   E CB  1 
ATOM   12215 C CG1 . ILE   I  1 79  ? -10.81712 8.00491   25.89690  1.000 38.68868  ?  79  ILE   E CG1 1 
ATOM   12216 C CG2 . ILE   I  1 79  ? -9.99244  10.32561  26.31059  1.000 39.49172  ?  79  ILE   E CG2 1 
ATOM   12217 C CD1 . ILE   I  1 79  ? -11.95107 8.27978   24.99651  1.000 35.93747  ?  79  ILE   E CD1 1 
ATOM   12218 N N   . ASP   I  1 80  ? -10.08901 10.36435  29.68837  1.000 34.02844  ?  80  ASP   E N   1 
ATOM   12219 C CA  . ASP   I  1 80  ? -9.69203  11.53559  30.45863  1.000 50.12857  ?  80  ASP   E CA  1 
ATOM   12220 C C   . ASP   I  1 80  ? -8.57600  11.22161  31.44462  1.000 41.30564  ?  80  ASP   E C   1 
ATOM   12221 O O   . ASP   I  1 80  ? -7.72038  12.07987  31.69618  1.000 50.45896  ?  80  ASP   E O   1 
ATOM   12222 C CB  . ASP   I  1 80  ? -10.90594 12.10675  31.18171  1.000 43.92940  ?  80  ASP   E CB  1 
ATOM   12223 C CG  . ASP   I  1 80  ? -12.02377 12.52470  30.21683  1.000 62.22040  ?  80  ASP   E CG  1 
ATOM   12224 O OD1 . ASP   I  1 80  ? -11.76781 12.63901  28.99947  1.000 60.40625  ?  80  ASP   E OD1 1 
ATOM   12225 O OD2 . ASP   I  1 80  ? -13.17084 12.73246  30.69112  1.000 68.09780  -1 80  ASP   E OD2 1 
ATOM   12226 N N   . MET   I  1 81  ? -8.55738  10.00028  32.00472  1.000 43.05243  ?  81  MET   E N   1 
ATOM   12227 C CA  . MET   I  1 81  ? -7.55436  9.65420   33.01085  1.000 36.75786  ?  81  MET   E CA  1 
ATOM   12228 C C   . MET   I  1 81  ? -6.12811  9.66860   32.44237  1.000 59.53217  ?  81  MET   E C   1 
ATOM   12229 O O   . MET   I  1 81  ? -5.16981  9.76661   33.22828  1.000 46.89386  ?  81  MET   E O   1 
ATOM   12230 C CB  . MET   I  1 81  ? -7.85252  8.27797   33.64483  1.000 36.76285  ?  81  MET   E CB  1 
ATOM   12231 C CG  . MET   I  1 81  ? -7.65320  7.06641   32.73384  1.000 43.22521  ?  81  MET   E CG  1 
ATOM   12232 S SD  . MET   I  1 81  ? -7.91067  5.41907   33.48947  1.000 43.10958  ?  81  MET   E SD  1 
ATOM   12233 C CE  . MET   I  1 81  ? -9.57030  5.54986   34.17550  1.000 39.72763  ?  81  MET   E CE  1 
ATOM   12234 N N   . PHE   I  1 82  ? -5.95925  9.62099   31.10644  1.000 37.00810  ?  82  PHE   E N   1 
ATOM   12235 C CA  . PHE   I  1 82  ? -4.64341  9.63064   30.48261  1.000 62.40828  ?  82  PHE   E CA  1 
ATOM   12236 C C   . PHE   I  1 82  ? -4.19220  11.01615  30.05068  1.000 35.26950  ?  82  PHE   E C   1 
ATOM   12237 O O   . PHE   I  1 82  ? -3.11229  11.13862  29.45962  1.000 98.65105  ?  82  PHE   E O   1 
ATOM   12238 C CB  . PHE   I  1 82  ? -4.65009  8.70859   29.27808  1.000 37.90090  ?  82  PHE   E CB  1 
ATOM   12239 C CG  . PHE   I  1 82  ? -4.61364  7.28038   29.63355  1.000 81.05563  ?  82  PHE   E CG  1 
ATOM   12240 C CD1 . PHE   I  1 82  ? -3.40859  6.67106   29.93533  1.000 34.98110  ?  82  PHE   E CD1 1 
ATOM   12241 C CD2 . PHE   I  1 82  ? -5.77960  6.54620   29.69606  1.000 37.59329  ?  82  PHE   E CD2 1 
ATOM   12242 C CE1 . PHE   I  1 82  ? -3.36722  5.34208   30.27913  1.000 53.74395  ?  82  PHE   E CE1 1 
ATOM   12243 C CE2 . PHE   I  1 82  ? -5.74761  5.22227   30.03738  1.000 55.01076  ?  82  PHE   E CE2 1 
ATOM   12244 C CZ  . PHE   I  1 82  ? -4.53552  4.61671   30.33609  1.000 30.71505  ?  82  PHE   E CZ  1 
ATOM   12245 N N   . GLU   I  1 83  ? -4.98988  12.05266  30.32869  1.000 67.83642  ?  83  GLU   E N   1 
ATOM   12246 C CA  . GLU   I  1 83  ? -4.75820  13.37646  29.76001  1.000 72.60097  ?  83  GLU   E CA  1 
ATOM   12247 C C   . GLU   I  1 83  ? -3.33700  13.84637  29.99205  1.000 80.92964  ?  83  GLU   E C   1 
ATOM   12248 O O   . GLU   I  1 83  ? -2.88116  13.92886  31.13004  1.000 57.19394  ?  83  GLU   E O   1 
ATOM   12249 C CB  . GLU   I  1 83  ? -5.75616  14.37834  30.33186  1.000 47.93481  ?  83  GLU   E CB  1 
ATOM   12250 C CG  . GLU   I  1 83  ? -5.90420  15.54082  29.41583  1.000 101.19723 ?  83  GLU   E CG  1 
ATOM   12251 C CD  . GLU   I  1 83  ? -7.26610  16.01887  29.55812  1.000 145.65790 ?  83  GLU   E CD  1 
ATOM   12252 O OE1 . GLU   I  1 83  ? -8.03646  15.31257  30.26153  1.000 158.81592 ?  83  GLU   E OE1 1 
ATOM   12253 O OE2 . GLU   I  1 83  ? -7.52849  17.06413  28.98161  1.000 150.22580 ?  83  GLU   E OE2 1 
ATOM   12254 N N   . GLY   I  1 84  ? -2.63697  14.13956  28.89650  1.000 78.58820  ?  84  GLY   E N   1 
ATOM   12255 C CA  . GLY   I  1 84  ? -1.28210  14.64803  28.96777  1.000 42.94534  ?  84  GLY   E CA  1 
ATOM   12256 C C   . GLY   I  1 84  ? -0.21246  13.66993  29.39008  1.000 76.03116  ?  84  GLY   E C   1 
ATOM   12257 O O   . GLY   I  1 84  ? 0.93993   14.07113  29.56383  1.000 61.14841  ?  84  GLY   E O   1 
ATOM   12258 N N   . ILE   I  1 85  ? -0.55153  12.39857  29.56173  1.000 73.84664  ?  85  ILE   E N   1 
ATOM   12259 C CA  . ILE   I  1 85  ? 0.44229   11.39474  29.92225  1.000 53.45646  ?  85  ILE   E CA  1 
ATOM   12260 C C   . ILE   I  1 85  ? 1.30573   11.10193  28.70804  1.000 63.66571  ?  85  ILE   E C   1 
ATOM   12261 O O   . ILE   I  1 85  ? 0.81139   10.69621  27.64515  1.000 57.81237  ?  85  ILE   E O   1 
ATOM   12262 C CB  . ILE   I  1 85  ? -0.23110  10.12515  30.46158  1.000 46.87245  ?  85  ILE   E CB  1 
ATOM   12263 C CG1 . ILE   I  1 85  ? -0.97772  10.45783  31.75673  1.000 62.14706  ?  85  ILE   E CG1 1 
ATOM   12264 C CG2 . ILE   I  1 85  ? 0.78905   8.98261   30.61671  1.000 48.98871  ?  85  ILE   E CG2 1 
ATOM   12265 C CD1 . ILE   I  1 85  ? -1.29290  9.28133   32.62228  1.000 54.05264  ?  85  ILE   E CD1 1 
ATOM   12266 N N   . GLN   I  1 86  ? 2.59346   11.37865  28.84859  1.000 59.72051  ?  86  GLN   E N   1 
ATOM   12267 C CA  . GLN   I  1 86  ? 3.51834   11.22449  27.74588  1.000 91.33569  ?  86  GLN   E CA  1 
ATOM   12268 C C   . GLN   I  1 86  ? 4.18165   9.84692   27.72656  1.000 42.17511  ?  86  GLN   E C   1 
ATOM   12269 O O   . GLN   I  1 86  ? 4.63058   9.40729   26.66131  1.000 88.87172  ?  86  GLN   E O   1 
ATOM   12270 C CB  . GLN   I  1 86  ? 4.59488   12.31529  27.79281  1.000 55.47118  ?  86  GLN   E CB  1 
ATOM   12271 C CG  . GLN   I  1 86  ? 4.26100   13.53570  27.00156  1.000 125.13180 ?  86  GLN   E CG  1 
ATOM   12272 C CD  . GLN   I  1 86  ? 5.40097   14.47060  26.90850  1.000 67.11263  ?  86  GLN   E CD  1 
ATOM   12273 O OE1 . GLN   I  1 86  ? 5.22943   15.57865  26.40473  1.000 96.50909  ?  86  GLN   E OE1 1 
ATOM   12274 N NE2 . GLN   I  1 86  ? 6.57187   14.05416  27.35906  1.000 97.93846  ?  86  GLN   E NE2 1 
ATOM   12275 N N   . ASP   I  1 87  ? 4.19935   9.12419   28.84839  1.000 103.85225 ?  87  ASP   E N   1 
ATOM   12276 C CA  . ASP   I  1 87  ? 4.84538   7.81873   28.91387  1.000 70.12465  ?  87  ASP   E CA  1 
ATOM   12277 C C   . ASP   I  1 87  ? 3.85596   6.67098   28.74041  1.000 59.27649  ?  87  ASP   E C   1 
ATOM   12278 O O   . ASP   I  1 87  ? 2.63589   6.83103   28.80686  1.000 79.66416  ?  87  ASP   E O   1 
ATOM   12279 C CB  . ASP   I  1 87  ? 5.57645   7.64656   30.24602  1.000 62.37921  ?  87  ASP   E CB  1 
ATOM   12280 C CG  . ASP   I  1 87  ? 6.41767   8.83998   30.58642  1.000 135.14471 ?  87  ASP   E CG  1 
ATOM   12281 O OD1 . ASP   I  1 87  ? 6.75475   9.60807   29.65407  1.000 115.40041 ?  87  ASP   E OD1 1 
ATOM   12282 O OD2 . ASP   I  1 87  ? 6.72256   9.00846   31.80032  1.000 113.43963 -1 87  ASP   E OD2 1 
ATOM   12283 N N   . SER   I  1 88  ? 4.41682   5.49834   28.55609  1.000 51.63719  ?  88  SER   E N   1 
ATOM   12284 C CA  . SER   I  1 88  ? 3.63922   4.28324   28.42087  1.000 40.71482  ?  88  SER   E CA  1 
ATOM   12285 C C   . SER   I  1 88  ? 3.16941   3.80579   29.79863  1.000 83.10334  ?  88  SER   E C   1 
ATOM   12286 O O   . SER   I  1 88  ? 3.98580   3.69333   30.72462  1.000 50.60354  ?  88  SER   E O   1 
ATOM   12287 C CB  . SER   I  1 88  ? 4.47717   3.21820   27.72994  1.000 41.76392  ?  88  SER   E CB  1 
ATOM   12288 O OG  . SER   I  1 88  ? 3.87727   2.79756   26.51509  1.000 57.89421  ?  88  SER   E OG  1 
ATOM   12289 N N   . PRO   I  1 89  ? 1.85477   3.51822   29.98428  1.000 59.43192  ?  89  PRO   E N   1 
ATOM   12290 C CA  . PRO   I  1 89  ? 0.74847   3.53889   29.01461  1.000 35.94842  ?  89  PRO   E CA  1 
ATOM   12291 C C   . PRO   I  1 89  ? 0.21804   4.93986   28.69877  1.000 63.65354  ?  89  PRO   E C   1 
ATOM   12292 O O   . PRO   I  1 89  ? 0.01165   5.74288   29.60599  1.000 46.25200  ?  89  PRO   E O   1 
ATOM   12293 C CB  . PRO   I  1 89  ? -0.35544  2.72445   29.70504  1.000 58.31709  ?  89  PRO   E CB  1 
ATOM   12294 C CG  . PRO   I  1 89  ? 0.13730   2.42386   31.11625  1.000 55.98674  ?  89  PRO   E CG  1 
ATOM   12295 C CD  . PRO   I  1 89  ? 1.34992   3.27597   31.34044  1.000 50.58315  ?  89  PRO   E CD  1 
ATOM   12296 N N   . ARG   I  1 90  ? -0.05854  5.24664   27.42883  1.000 45.92846  ?  90  ARG   E N   1 
ATOM   12297 C CA  . ARG   I  1 90  ? -0.64065  6.53339   27.06987  1.000 62.92743  ?  90  ARG   E CA  1 
ATOM   12298 C C   . ARG   I  1 90  ? -2.13719  6.45147   26.79192  1.000 53.61234  ?  90  ARG   E C   1 
ATOM   12299 O O   . ARG   I  1 90  ? -2.79957  7.48396   26.72733  1.000 53.19974  ?  90  ARG   E O   1 
ATOM   12300 C CB  . ARG   I  1 90  ? 0.06463   7.12991   25.84417  1.000 47.31857  ?  90  ARG   E CB  1 
ATOM   12301 C CG  . ARG   I  1 90  ? 1.50251   6.83976   25.72060  1.000 41.14124  ?  90  ARG   E CG  1 
ATOM   12302 C CD  . ARG   I  1 90  ? 2.10629   7.14210   24.34835  1.000 38.00777  ?  90  ARG   E CD  1 
ATOM   12303 N NE  . ARG   I  1 90  ? 3.55179   7.34482   24.46583  1.000 102.87621 ?  90  ARG   E NE  1 
ATOM   12304 C CZ  . ARG   I  1 90  ? 4.45300   6.37656   24.37669  1.000 27.18721  ?  90  ARG   E CZ  1 
ATOM   12305 N NH1 . ARG   I  1 90  ? 4.09458   5.14101   24.10845  1.000 59.18204  ?  90  ARG   E NH1 1 
ATOM   12306 N NH2 . ARG   I  1 90  ? 5.74109   6.65552   24.57342  1.000 44.06978  ?  90  ARG   E NH2 1 
ATOM   12307 N N   . ASN   I  1 91  ? -2.70210  5.26167   26.64389  1.000 40.25154  ?  91  ASN   E N   1 
ATOM   12308 C CA  . ASN   I  1 91  ? -4.13855  5.13260   26.45569  1.000 44.73167  ?  91  ASN   E CA  1 
ATOM   12309 C C   . ASN   I  1 91  ? -4.55229  3.80136   27.03958  1.000 43.35822  ?  91  ASN   E C   1 
ATOM   12310 O O   . ASN   I  1 91  ? -3.72540  3.02460   27.53858  1.000 49.91154  ?  91  ASN   E O   1 
ATOM   12311 C CB  . ASN   I  1 91  ? -4.52354  5.22421   24.97745  1.000 36.73308  ?  91  ASN   E CB  1 
ATOM   12312 C CG  . ASN   I  1 91  ? -3.61338  4.37481   24.11900  1.000 47.41059  ?  91  ASN   E CG  1 
ATOM   12313 O OD1 . ASN   I  1 91  ? -3.60759  3.14275   24.21063  1.000 57.60062  ?  91  ASN   E OD1 1 
ATOM   12314 N ND2 . ASN   I  1 91  ? -2.81844  5.02732   23.29815  1.000 43.43629  ?  91  ASN   E ND2 1 
ATOM   12315 N N   . TYR   I  1 92  ? -5.85193  3.53913   26.96980  1.000 54.62384  ?  92  TYR   E N   1 
ATOM   12316 C CA  . TYR   I  1 92  ? -6.32153  2.29786   27.55175  1.000 48.36558  ?  92  TYR   E CA  1 
ATOM   12317 C C   . TYR   I  1 92  ? -5.87600  1.09982   26.71836  1.000 52.45956  ?  92  TYR   E C   1 
ATOM   12318 O O   . TYR   I  1 92  ? -5.71244  0.00075   27.26226  1.000 57.17617  ?  92  TYR   E O   1 
ATOM   12319 C CB  . TYR   I  1 92  ? -7.84721  2.34748   27.78228  1.000 37.58259  ?  92  TYR   E CB  1 
ATOM   12320 C CG  . TYR   I  1 92  ? -8.75474  2.18501   26.58747  1.000 43.04898  ?  92  TYR   E CG  1 
ATOM   12321 C CD1 . TYR   I  1 92  ? -9.09349  0.91765   26.11654  1.000 41.26688  ?  92  TYR   E CD1 1 
ATOM   12322 C CD2 . TYR   I  1 92  ? -9.35037  3.30408   25.97745  1.000 49.48278  ?  92  TYR   E CD2 1 
ATOM   12323 C CE1 . TYR   I  1 92  ? -9.95134  0.76254   25.03828  1.000 60.24829  ?  92  TYR   E CE1 1 
ATOM   12324 C CE2 . TYR   I  1 92  ? -10.21339 3.15593   24.89801  1.000 57.34309  ?  92  TYR   E CE2 1 
ATOM   12325 C CZ  . TYR   I  1 92  ? -10.50525 1.88265   24.43230  1.000 52.88645  ?  92  TYR   E CZ  1 
ATOM   12326 O OH  . TYR   I  1 92  ? -11.34351 1.70529   23.37019  1.000 69.64290  ?  92  TYR   E OH  1 
ATOM   12327 N N   . GLN   I  1 93  ? -5.58908  1.29393   25.42916  1.000 45.30035  ?  93  GLN   E N   1 
ATOM   12328 C CA  . GLN   I  1 93  ? -5.11984  0.15805   24.63907  1.000 57.90813  ?  93  GLN   E CA  1 
ATOM   12329 C C   . GLN   I  1 93  ? -3.71725  -0.26299  25.06097  1.000 43.95670  ?  93  GLN   E C   1 
ATOM   12330 O O   . GLN   I  1 93  ? -3.42673  -1.46011  25.17130  1.000 49.36681  ?  93  GLN   E O   1 
ATOM   12331 C CB  . GLN   I  1 93  ? -5.13709  0.48313   23.14897  1.000 38.78182  ?  93  GLN   E CB  1 
ATOM   12332 C CG  . GLN   I  1 93  ? -6.51488  0.35724   22.49787  1.000 55.51186  ?  93  GLN   E CG  1 
ATOM   12333 C CD  . GLN   I  1 93  ? -7.23743  1.69222   22.39645  1.000 174.81872 ?  93  GLN   E CD  1 
ATOM   12334 O OE1 . GLN   I  1 93  ? -6.90350  2.66507   23.10009  1.000 53.09150  ?  93  GLN   E OE1 1 
ATOM   12335 N NE2 . GLN   I  1 93  ? -8.23373  1.74973   21.51460  1.000 55.31077  ?  93  GLN   E NE2 1 
ATOM   12336 N N   . GLU   I  1 94  ? -2.82487  0.70396   25.30373  1.000 52.74777  ?  94  GLU   E N   1 
ATOM   12337 C CA  . GLU   I  1 94  ? -1.49175  0.35039   25.78626  1.000 25.09057  ?  94  GLU   E CA  1 
ATOM   12338 C C   . GLU   I  1 94  ? -1.57054  -0.24552  27.17850  1.000 59.59592  ?  94  GLU   E C   1 
ATOM   12339 O O   . GLU   I  1 94  ? -0.81552  -1.16394  27.51795  1.000 56.65450  ?  94  GLU   E O   1 
ATOM   12340 C CB  . GLU   I  1 94  ? -0.58591  1.57151   25.82074  1.000 56.53171  ?  94  GLU   E CB  1 
ATOM   12341 C CG  . GLU   I  1 94  ? -0.03529  1.95557   24.48116  1.000 78.07456  ?  94  GLU   E CG  1 
ATOM   12342 C CD  . GLU   I  1 94  ? 0.94741   3.09674   24.61604  1.000 140.77335 ?  94  GLU   E CD  1 
ATOM   12343 O OE1 . GLU   I  1 94  ? 1.62396   3.14897   25.68224  1.000 49.23883  ?  94  GLU   E OE1 1 
ATOM   12344 O OE2 . GLU   I  1 94  ? 1.02289   3.92805   23.67730  1.000 102.94598 -1 94  GLU   E OE2 1 
ATOM   12345 N N   . LEU   I  1 95  ? -2.46867  0.28727   28.01556  1.000 51.36902  ?  95  LEU   E N   1 
ATOM   12346 C CA  . LEU   I  1 95  ? -2.68780  -0.29998  29.33218  1.000 32.41182  ?  95  LEU   E CA  1 
ATOM   12347 C C   . LEU   I  1 95  ? -2.99363  -1.78406  29.20692  1.000 36.54027  ?  95  LEU   E C   1 
ATOM   12348 O O   . LEU   I  1 95  ? -2.34573  -2.61995  29.85184  1.000 32.54984  ?  95  LEU   E O   1 
ATOM   12349 C CB  . LEU   I  1 95  ? -3.82210  0.42197   30.05623  1.000 39.52092  ?  95  LEU   E CB  1 
ATOM   12350 C CG  . LEU   I  1 95  ? -3.99476  -0.01672  31.51781  1.000 39.58823  ?  95  LEU   E CG  1 
ATOM   12351 C CD1 . LEU   I  1 95  ? -2.74681  0.30506   32.34991  1.000 33.87669  ?  95  LEU   E CD1 1 
ATOM   12352 C CD2 . LEU   I  1 95  ? -5.21510  0.67142   32.08452  1.000 25.07529  ?  95  LEU   E CD2 1 
ATOM   12353 N N   . CYS   I  1 96  ? -3.94545  -2.13305  28.32636  1.000 28.30659  ?  96  CYS   E N   1 
ATOM   12354 C CA  . CYS   I  1 96  ? -4.29570  -3.53633  28.13602  1.000 39.09561  ?  96  CYS   E CA  1 
ATOM   12355 C C   . CYS   I  1 96  ? -3.10785  -4.35463  27.64422  1.000 39.29472  ?  96  CYS   E C   1 
ATOM   12356 O O   . CYS   I  1 96  ? -2.93925  -5.51404  28.04600  1.000 58.63395  ?  96  CYS   E O   1 
ATOM   12357 C CB  . CYS   I  1 96  ? -5.45736  -3.66112  27.16152  1.000 32.62903  ?  96  CYS   E CB  1 
ATOM   12358 S SG  . CYS   I  1 96  ? -7.05237  -3.05042  27.75498  1.000 48.33342  ?  96  CYS   E SG  1 
ATOM   12359 N N   . ASN   I  1 97  ? -2.28444  -3.78112  26.75547  1.000 52.34381  ?  97  ASN   E N   1 
ATOM   12360 C CA  . ASN   I  1 97  ? -1.13640  -4.52987  26.24574  1.000 42.61393  ?  97  ASN   E CA  1 
ATOM   12361 C C   . ASN   I  1 97  ? -0.10212  -4.76457  27.33874  1.000 67.44346  ?  97  ASN   E C   1 
ATOM   12362 O O   . ASN   I  1 97  ? 0.47679   -5.85578  27.42457  1.000 48.85579  ?  97  ASN   E O   1 
ATOM   12363 C CB  . ASN   I  1 97  ? -0.49484  -3.80439  25.06680  1.000 54.14050  ?  97  ASN   E CB  1 
ATOM   12364 C CG  . ASN   I  1 97  ? -1.33917  -3.86399  23.82275  1.000 93.61516  ?  97  ASN   E CG  1 
ATOM   12365 O OD1 . ASN   I  1 97  ? -2.03600  -4.85339  23.57856  1.000 66.18106  ?  97  ASN   E OD1 1 
ATOM   12366 N ND2 . ASN   I  1 97  ? -1.28744  -2.80248  23.02159  1.000 51.18641  ?  97  ASN   E ND2 1 
ATOM   12367 N N   . MET   I  1 98  ? 0.14409   -3.75228  28.18267  1.000 31.42267  ?  98  MET   E N   1 
ATOM   12368 C CA  . MET   I  1 98  ? 1.09042   -3.92736  29.27891  1.000 27.75222  ?  98  MET   E CA  1 
ATOM   12369 C C   . MET   I  1 98  ? 0.56716   -4.92621  30.31077  1.000 65.79788  ?  98  MET   E C   1 
ATOM   12370 O O   . MET   I  1 98  ? 1.35062   -5.70438  30.87076  1.000 45.65680  ?  98  MET   E O   1 
ATOM   12371 C CB  . MET   I  1 98  ? 1.40640   -2.56777  29.91437  1.000 34.60923  ?  98  MET   E CB  1 
ATOM   12372 C CG  . MET   I  1 98  ? 2.15132   -1.62509  28.95812  1.000 23.60304  ?  98  MET   E CG  1 
ATOM   12373 S SD  . MET   I  1 98  ? 2.39590   0.07408   29.48611  1.000 54.70800  ?  98  MET   E SD  1 
ATOM   12374 C CE  . MET   I  1 98  ? 3.72131   -0.11503  30.66993  1.000 41.40568  ?  98  MET   E CE  1 
ATOM   12375 N N   . PHE   I  1 99  ? -0.75228  -4.93334  30.56585  1.000 39.33346  ?  99  PHE   E N   1 
ATOM   12376 C CA  . PHE   I  1 99  ? -1.33859  -5.96673  31.42394  1.000 35.36196  ?  99  PHE   E CA  1 
ATOM   12377 C C   . PHE   I  1 99  ? -1.01775  -7.35372  30.88015  1.000 44.70958  ?  99  PHE   E C   1 
ATOM   12378 O O   . PHE   I  1 99  ? -0.69032  -8.28067  31.63503  1.000 43.57459  ?  99  PHE   E O   1 
ATOM   12379 C CB  . PHE   I  1 99  ? -2.86813  -5.81033  31.53189  1.000 33.83787  ?  99  PHE   E CB  1 
ATOM   12380 C CG  . PHE   I  1 99  ? -3.33418  -4.71798  32.46211  1.000 42.05026  ?  99  PHE   E CG  1 
ATOM   12381 C CD1 . PHE   I  1 99  ? -2.43454  -3.96299  33.22196  1.000 31.87590  ?  99  PHE   E CD1 1 
ATOM   12382 C CD2 . PHE   I  1 99  ? -4.69637  -4.44949  32.57554  1.000 40.70097  ?  99  PHE   E CD2 1 
ATOM   12383 C CE1 . PHE   I  1 99  ? -2.87909  -2.95702  34.06932  1.000 47.42145  ?  99  PHE   E CE1 1 
ATOM   12384 C CE2 . PHE   I  1 99  ? -5.15485  -3.44690  33.42418  1.000 31.01517  ?  99  PHE   E CE2 1 
ATOM   12385 C CZ  . PHE   I  1 99  ? -4.23861  -2.68950  34.16840  1.000 35.11890  ?  99  PHE   E CZ  1 
ATOM   12386 N N   . ASN   I  1 100 ? -1.12289  -7.50595  29.55510  1.000 36.63230  ?  100 ASN   E N   1 
ATOM   12387 C CA  . ASN   I  1 100 ? -0.89112  -8.79373  28.91430  1.000 40.88507  ?  100 ASN   E CA  1 
ATOM   12388 C C   . ASN   I  1 100 ? 0.54676   -9.27446  29.11651  1.000 44.66970  ?  100 ASN   E C   1 
ATOM   12389 O O   . ASN   I  1 100 ? 0.77668   -10.48272 29.27021  1.000 51.92551  ?  100 ASN   E O   1 
ATOM   12390 C CB  . ASN   I  1 100 ? -1.25890  -8.69262  27.43115  1.000 40.37292  ?  100 ASN   E CB  1 
ATOM   12391 C CG  . ASN   I  1 100 ? -1.50095  -10.04463 26.80080  1.000 51.82482  ?  100 ASN   E CG  1 
ATOM   12392 O OD1 . ASN   I  1 100 ? -2.43776  -10.76571 27.16085  1.000 64.47144  ?  100 ASN   E OD1 1 
ATOM   12393 N ND2 . ASN   I  1 100 ? -0.66178  -10.39391 25.84146  1.000 51.50482  ?  100 ASN   E ND2 1 
ATOM   12394 N N   . ASP   I  1 101 ? 1.51839   -8.35059  29.15875  1.000 43.41409  ?  101 ASP   E N   1 
ATOM   12395 C CA  . ASP   I  1 101 ? 2.88117   -8.73178  29.53126  1.000 37.14003  ?  101 ASP   E CA  1 
ATOM   12396 C C   . ASP   I  1 101 ? 2.97427   -9.06018  31.01631  1.000 59.80091  ?  101 ASP   E C   1 
ATOM   12397 O O   . ASP   I  1 101 ? 3.51078   -10.11192 31.39363  1.000 51.47517  ?  101 ASP   E O   1 
ATOM   12398 C CB  . ASP   I  1 101 ? 3.88000   -7.62275  29.18184  1.000 37.21530  ?  101 ASP   E CB  1 
ATOM   12399 C CG  . ASP   I  1 101 ? 3.97017   -7.34476  27.68682  1.000 119.97543 ?  101 ASP   E CG  1 
ATOM   12400 O OD1 . ASP   I  1 101 ? 3.79184   -8.28468  26.88091  1.000 55.26511  ?  101 ASP   E OD1 1 
ATOM   12401 O OD2 . ASP   I  1 101 ? 4.23565   -6.17311  27.32140  1.000 64.92188  -1 101 ASP   E OD2 1 
ATOM   12402 N N   . ILE   I  1 102 ? 2.46293   -8.16149  31.87399  1.000 47.42119  ?  102 ILE   E N   1 
ATOM   12403 C CA  . ILE   I  1 102 ? 2.66370   -8.29580  33.31773  1.000 31.87735  ?  102 ILE   E CA  1 
ATOM   12404 C C   . ILE   I  1 102 ? 2.09642   -9.61037  33.82672  1.000 57.43907  ?  102 ILE   E C   1 
ATOM   12405 O O   . ILE   I  1 102 ? 2.74621   -10.31068 34.61258  1.000 40.97708  ?  102 ILE   E O   1 
ATOM   12406 C CB  . ILE   I  1 102 ? 2.04599   -7.10970  34.07216  1.000 34.70629  ?  102 ILE   E CB  1 
ATOM   12407 C CG1 . ILE   I  1 102 ? 2.75094   -5.80380  33.72575  1.000 19.52370  ?  102 ILE   E CG1 1 
ATOM   12408 C CG2 . ILE   I  1 102 ? 2.13505   -7.34767  35.56098  1.000 23.93787  ?  102 ILE   E CG2 1 
ATOM   12409 C CD1 . ILE   I  1 102 ? 2.27011   -4.62699  34.57932  1.000 40.60897  ?  102 ILE   E CD1 1 
ATOM   12410 N N   . PHE   I  1 103 ? 0.88403   -9.97503  33.37636  1.000 31.09744  ?  103 PHE   E N   1 
ATOM   12411 C CA  . PHE   I  1 103 ? 0.18243   -11.15099 33.88605  1.000 55.61072  ?  103 PHE   E CA  1 
ATOM   12412 C C   . PHE   I  1 103 ? 0.78839   -12.46641 33.40576  1.000 33.49508  ?  103 PHE   E C   1 
ATOM   12413 O O   . PHE   I  1 103 ? 0.30266   -13.53423 33.79332  1.000 41.85554  ?  103 PHE   E O   1 
ATOM   12414 C CB  . PHE   I  1 103 ? -1.29727  -11.10084 33.49343  1.000 23.01848  ?  103 PHE   E CB  1 
ATOM   12415 C CG  . PHE   I  1 103 ? -2.04771  -9.91165  34.05802  1.000 40.27657  ?  103 PHE   E CG  1 
ATOM   12416 C CD1 . PHE   I  1 103 ? -1.59055  -9.24184  35.19125  1.000 36.25208  ?  103 PHE   E CD1 1 
ATOM   12417 C CD2 . PHE   I  1 103 ? -3.21261  -9.46251  33.44579  1.000 28.30716  ?  103 PHE   E CD2 1 
ATOM   12418 C CE1 . PHE   I  1 103 ? -2.28515  -8.14204  35.69292  1.000 48.49978  ?  103 PHE   E CE1 1 
ATOM   12419 C CE2 . PHE   I  1 103 ? -3.91227  -8.36655  33.93908  1.000 40.43943  ?  103 PHE   E CE2 1 
ATOM   12420 C CZ  . PHE   I  1 103 ? -3.44861  -7.70738  35.06242  1.000 39.72241  ?  103 PHE   E CZ  1 
ATOM   12421 N N   . ARG   I  1 104 ? 1.78382   -12.44566 32.54002  1.000 68.48950  ?  104 ARG   E N   1 
ATOM   12422 C CA  . ARG   I  1 104 ? 2.40276   -13.68786 32.12236  1.000 26.60468  ?  104 ARG   E CA  1 
ATOM   12423 C C   . ARG   I  1 104 ? 3.73801   -13.94904 32.80527  1.000 95.55883  ?  104 ARG   E C   1 
ATOM   12424 O O   . ARG   I  1 104 ? 4.33203   -14.99914 32.54281  1.000 30.38706  ?  104 ARG   E O   1 
ATOM   12425 C CB  . ARG   I  1 104 ? 2.57170   -13.71295 30.61664  1.000 46.16229  ?  104 ARG   E CB  1 
ATOM   12426 C CG  . ARG   I  1 104 ? 1.25716   -14.00497 29.89328  1.000 34.82294  ?  104 ARG   E CG  1 
ATOM   12427 C CD  . ARG   I  1 104 ? 1.50171   -14.04691 28.42109  1.000 71.65799  ?  104 ARG   E CD  1 
ATOM   12428 N NE  . ARG   I  1 104 ? 0.27585   -13.93299 27.64486  1.000 88.03182  ?  104 ARG   E NE  1 
ATOM   12429 C CZ  . ARG   I  1 104 ? -0.34280  -14.94971 27.05543  1.000 122.45377 ?  104 ARG   E CZ  1 
ATOM   12430 N NH1 . ARG   I  1 104 ? 0.10916   -16.19462 27.15315  1.000 124.78067 ?  104 ARG   E NH1 1 
ATOM   12431 N NH2 . ARG   I  1 104 ? -1.44026  -14.71306 26.34389  1.000 139.04642 ?  104 ARG   E NH2 1 
ATOM   12432 N N   . LYS   I  1 105 ? 4.20734   -13.04154 33.69353  1.000 39.23255  ?  105 LYS   E N   1 
ATOM   12433 C CA  . LYS   I  1 105 ? 5.47928   -13.22591 34.36804  1.000 59.96990  ?  105 LYS   E CA  1 
ATOM   12434 C C   . LYS   I  1 105 ? 5.34938   -12.79206 35.81970  1.000 42.50066  ?  105 LYS   E C   1 
ATOM   12435 O O   . LYS   I  1 105 ? 4.42624   -12.06820 36.19005  1.000 47.12794  ?  105 LYS   E O   1 
ATOM   12436 C CB  . LYS   I  1 105 ? 6.60285   -12.48295 33.63108  1.000 50.18713  ?  105 LYS   E CB  1 
ATOM   12437 C CG  . LYS   I  1 105 ? 6.36451   -11.01560 33.47406  1.000 40.13196  ?  105 LYS   E CG  1 
ATOM   12438 C CD  . LYS   I  1 105 ? 7.42539   -10.36118 32.58925  1.000 40.59691  ?  105 LYS   E CD  1 
ATOM   12439 C CE  . LYS   I  1 105 ? 7.27903   -10.78371 31.14757  1.000 70.80409  ?  105 LYS   E CE  1 
ATOM   12440 N NZ  . LYS   I  1 105 ? 7.83075   -9.74732  30.23464  1.000 83.65699  ?  105 LYS   E NZ  1 
ATOM   12441 N N   . ALA   I  1 106 ? 6.27037   -13.27618 36.63544  1.000 51.51249  ?  106 ALA   E N   1 
ATOM   12442 C CA  . ALA   I  1 106 ? 6.27797   -12.99251 38.05815  1.000 44.77411  ?  106 ALA   E CA  1 
ATOM   12443 C C   . ALA   I  1 106 ? 6.96084   -11.65777 38.33783  1.000 28.16475  ?  106 ALA   E C   1 
ATOM   12444 O O   . ALA   I  1 106 ? 7.79498   -11.20568 37.55103  1.000 47.51433  ?  106 ALA   E O   1 
ATOM   12445 C CB  . ALA   I  1 106 ? 6.98610   -14.11158 38.82170  1.000 31.08127  ?  106 ALA   E CB  1 
ATOM   12446 N N   . PRO   I  1 107 ? 6.61364   -10.99609 39.44344  1.000 57.96140  ?  107 PRO   E N   1 
ATOM   12447 C CA  . PRO   I  1 107 ? 7.26761   -9.72558  39.77034  1.000 40.29375  ?  107 PRO   E CA  1 
ATOM   12448 C C   . PRO   I  1 107 ? 8.73129   -9.94170  40.13320  1.000 50.17658  ?  107 PRO   E C   1 
ATOM   12449 O O   . PRO   I  1 107 ? 9.16293   -11.04383 40.48274  1.000 45.43998  ?  107 PRO   E O   1 
ATOM   12450 C CB  . PRO   I  1 107 ? 6.47543   -9.20542  40.97790  1.000 38.34955  ?  107 PRO   E CB  1 
ATOM   12451 C CG  . PRO   I  1 107 ? 5.35848   -10.12888 41.17743  1.000 34.96069  ?  107 PRO   E CG  1 
ATOM   12452 C CD  . PRO   I  1 107 ? 5.66233   -11.40894 40.48910  1.000 28.78939  ?  107 PRO   E CD  1 
ATOM   12453 N N   . VAL   I  1 108 ? 9.49717   -8.85676  40.06688  1.000 53.28509  ?  108 VAL   E N   1 
ATOM   12454 C CA  . VAL   I  1 108 ? 10.90082  -8.88263  40.43963  1.000 49.15097  ?  108 VAL   E CA  1 
ATOM   12455 C C   . VAL   I  1 108 ? 11.14980  -7.82878  41.52074  1.000 60.38276  ?  108 VAL   E C   1 
ATOM   12456 O O   . VAL   I  1 108 ? 10.30877  -6.97222  41.80290  1.000 60.99814  ?  108 VAL   E O   1 
ATOM   12457 C CB  . VAL   I  1 108 ? 11.82735  -8.67708  39.22306  1.000 59.38662  ?  108 VAL   E CB  1 
ATOM   12458 C CG1 . VAL   I  1 108 ? 11.54771  -9.74974  38.15218  1.000 40.40908  ?  108 VAL   E CG1 1 
ATOM   12459 C CG2 . VAL   I  1 108 ? 11.64463  -7.30414  38.64483  1.000 40.15528  ?  108 VAL   E CG2 1 
ATOM   12460 N N   . TYR   I  1 109 ? 12.31834  -7.92366  42.14643  1.000 43.52168  ?  109 TYR   E N   1 
ATOM   12461 C CA  . TYR   I  1 109 ? 12.68391  -6.99833  43.21223  1.000 72.97500  ?  109 TYR   E CA  1 
ATOM   12462 C C   . TYR   I  1 109 ? 13.23157  -5.70142  42.62769  1.000 43.23828  ?  109 TYR   E C   1 
ATOM   12463 O O   . TYR   I  1 109 ? 13.95322  -5.70929  41.62660  1.000 57.16295  ?  109 TYR   E O   1 
ATOM   12464 C CB  . TYR   I  1 109 ? 13.72076  -7.63141  44.14674  1.000 37.39252  ?  109 TYR   E CB  1 
ATOM   12465 C CG  . TYR   I  1 109 ? 14.15514  -6.69860  45.25317  1.000 70.19749  ?  109 TYR   E CG  1 
ATOM   12466 C CD1 . TYR   I  1 109 ? 13.45573  -6.63151  46.44273  1.000 38.68856  ?  109 TYR   E CD1 1 
ATOM   12467 C CD2 . TYR   I  1 109 ? 15.25313  -5.86405  45.09523  1.000 42.66746  ?  109 TYR   E CD2 1 
ATOM   12468 C CE1 . TYR   I  1 109 ? 13.84785  -5.76249  47.44564  1.000 80.36049  ?  109 TYR   E CE1 1 
ATOM   12469 C CE2 . TYR   I  1 109 ? 15.64981  -4.99417  46.08815  1.000 63.80887  ?  109 TYR   E CE2 1 
ATOM   12470 C CZ  . TYR   I  1 109 ? 14.94763  -4.94421  47.26141  1.000 40.02559  ?  109 TYR   E CZ  1 
ATOM   12471 O OH  . TYR   I  1 109 ? 15.32868  -4.07954  48.26277  1.000 66.29569  ?  109 TYR   E OH  1 
ATOM   12472 N N   . GLY   I  1 110 ? 12.87605  -4.58140  43.24551  1.000 56.36198  ?  110 GLY   E N   1 
ATOM   12473 C CA  . GLY   I  1 110 ? 13.41055  -3.32745  42.76245  1.000 21.36124  ?  110 GLY   E CA  1 
ATOM   12474 C C   . GLY   I  1 110 ? 12.49663  -2.12072  42.80691  1.000 55.05807  ?  110 GLY   E C   1 
ATOM   12475 O O   . GLY   I  1 110 ? 12.95836  -1.03018  43.14903  1.000 49.06012  ?  110 GLY   E O   1 
ATOM   12476 N N   . ASP   I  1 111 ? 11.21859  -2.27465  42.45788  1.000 51.80408  ?  111 ASP   E N   1 
ATOM   12477 C CA  . ASP   I  1 111 ? 10.34913  -1.11034  42.37493  1.000 42.38279  ?  111 ASP   E CA  1 
ATOM   12478 C C   . ASP   I  1 111 ? 9.73491   -0.78963  43.73316  1.000 26.42937  ?  111 ASP   E C   1 
ATOM   12479 O O   . ASP   I  1 111 ? 9.73688   -1.61271  44.65280  1.000 39.76154  ?  111 ASP   E O   1 
ATOM   12480 C CB  . ASP   I  1 111 ? 9.26265   -1.32713  41.32665  1.000 55.11453  ?  111 ASP   E CB  1 
ATOM   12481 C CG  . ASP   I  1 111 ? 9.78351   -1.16411  39.92117  1.000 53.82552  ?  111 ASP   E CG  1 
ATOM   12482 O OD1 . ASP   I  1 111 ? 10.15529  -0.02787  39.55827  1.000 69.64295  ?  111 ASP   E OD1 1 
ATOM   12483 O OD2 . ASP   I  1 111 ? 9.84307   -2.17790  39.19111  1.000 88.51121  -1 111 ASP   E OD2 1 
ATOM   12484 N N   . LEU   I  1 112 ? 9.20674   0.42131   43.82888  1.000 72.28449  ?  112 LEU   E N   1 
ATOM   12485 C CA  . LEU   I  1 112 ? 8.61120   0.86513   45.07303  1.000 30.13223  ?  112 LEU   E CA  1 
ATOM   12486 C C   . LEU   I  1 112 ? 7.35438   0.05583   45.40556  1.000 76.90624  ?  112 LEU   E C   1 
ATOM   12487 O O   . LEU   I  1 112 ? 7.06119   -0.18530  46.58605  1.000 39.49644  ?  112 LEU   E O   1 
ATOM   12488 C CB  . LEU   I  1 112 ? 8.31273   2.35924   44.95179  1.000 84.98887  ?  112 LEU   E CB  1 
ATOM   12489 C CG  . LEU   I  1 112 ? 7.64925   3.04752   46.14866  1.000 124.52662 ?  112 LEU   E CG  1 
ATOM   12490 C CD1 . LEU   I  1 112 ? 8.67015   3.79743   46.96303  1.000 102.25013 ?  112 LEU   E CD1 1 
ATOM   12491 C CD2 . LEU   I  1 112 ? 6.53775   3.96713   45.68383  1.000 82.62488  ?  112 LEU   E CD2 1 
ATOM   12492 N N   . GLY   I  1 113 ? 6.60587   -0.37967  44.38565  1.000 41.36174  ?  113 GLY   E N   1 
ATOM   12493 C CA  . GLY   I  1 113 ? 5.45307   -1.22124  44.58330  1.000 39.84055  ?  113 GLY   E CA  1 
ATOM   12494 C C   . GLY   I  1 113 ? 5.35304   -2.28688  43.50990  1.000 43.43037  ?  113 GLY   E C   1 
ATOM   12495 O O   . GLY   I  1 113 ? 6.19525   -2.38015  42.60489  1.000 41.86909  ?  113 GLY   E O   1 
ATOM   12496 N N   . PRO   I  1 114 ? 4.30815   -3.10777  43.58418  1.000 37.68848  ?  114 PRO   E N   1 
ATOM   12497 C CA  . PRO   I  1 114 ? 4.13390   -4.19852  42.59866  1.000 31.00663  ?  114 PRO   E CA  1 
ATOM   12498 C C   . PRO   I  1 114 ? 3.83231   -3.64511  41.21365  1.000 33.96680  ?  114 PRO   E C   1 
ATOM   12499 O O   . PRO   I  1 114 ? 3.54194   -2.44373  41.05201  1.000 38.43539  ?  114 PRO   E O   1 
ATOM   12500 C CB  . PRO   I  1 114 ? 2.96077   -5.01070  43.17436  1.000 36.01777  ?  114 PRO   E CB  1 
ATOM   12501 C CG  . PRO   I  1 114 ? 2.20833   -4.02141  44.04950  1.000 32.97335  ?  114 PRO   E CG  1 
ATOM   12502 C CD  . PRO   I  1 114 ? 3.21562   -3.03827  44.56952  1.000 34.05873  ?  114 PRO   E CD  1 
ATOM   12503 N N   . PRO   I  1 115 ? 3.93800   -4.47910  40.17205  1.000 39.41125  ?  115 PRO   E N   1 
ATOM   12504 C CA  . PRO   I  1 115 ? 4.01331   -3.92232  38.80149  1.000 50.39631  ?  115 PRO   E CA  1 
ATOM   12505 C C   . PRO   I  1 115 ? 2.73185   -3.29014  38.29071  1.000 42.49510  ?  115 PRO   E C   1 
ATOM   12506 O O   . PRO   I  1 115 ? 2.81274   -2.30428  37.54394  1.000 47.58815  ?  115 PRO   E O   1 
ATOM   12507 C CB  . PRO   I  1 115 ? 4.41959   -5.12977  37.94131  1.000 32.16898  ?  115 PRO   E CB  1 
ATOM   12508 C CG  . PRO   I  1 115 ? 4.31576   -6.34213  38.82631  1.000 34.72708  ?  115 PRO   E CG  1 
ATOM   12509 C CD  . PRO   I  1 115 ? 4.42305   -5.87103  40.23989  1.000 44.69494  ?  115 PRO   E CD  1 
ATOM   12510 N N   . VAL   I  1 116 ? 1.55540   -3.83052  38.63895  1.000 42.01510  ?  116 VAL   E N   1 
ATOM   12511 C CA  . VAL   I  1 116 ? 0.31171   -3.18415  38.21602  1.000 32.27614  ?  116 VAL   E CA  1 
ATOM   12512 C C   . VAL   I  1 116 ? 0.15713   -1.82544  38.89095  1.000 34.75716  ?  116 VAL   E C   1 
ATOM   12513 O O   . VAL   I  1 116 ? -0.20723  -0.83295  38.24396  1.000 38.33102  ?  116 VAL   E O   1 
ATOM   12514 C CB  . VAL   I  1 116 ? -0.91548  -4.07379  38.47738  1.000 39.44646  ?  116 VAL   E CB  1 
ATOM   12515 C CG1 . VAL   I  1 116 ? -2.17116  -3.32446  38.03739  1.000 31.52081  ?  116 VAL   E CG1 1 
ATOM   12516 C CG2 . VAL   I  1 116 ? -0.79779  -5.39450  37.72983  1.000 23.48034  ?  116 VAL   E CG2 1 
ATOM   12517 N N   . TYR   I  1 117 ? 0.43361   -1.74892  40.19388  1.000 33.94966  ?  117 TYR   E N   1 
ATOM   12518 C CA  . TYR   I  1 117 ? 0.41429   -0.44748  40.85261  1.000 47.48239  ?  117 TYR   E CA  1 
ATOM   12519 C C   . TYR   I  1 117 ? 1.31407   0.55629   40.12448  1.000 41.50310  ?  117 TYR   E C   1 
ATOM   12520 O O   . TYR   I  1 117 ? 0.90667   1.69544   39.86805  1.000 46.51472  ?  117 TYR   E O   1 
ATOM   12521 C CB  . TYR   I  1 117 ? 0.83211   -0.55835  42.32750  1.000 33.06753  ?  117 TYR   E CB  1 
ATOM   12522 C CG  . TYR   I  1 117 ? 1.16519   0.82134   42.84557  1.000 40.33783  ?  117 TYR   E CG  1 
ATOM   12523 C CD1 . TYR   I  1 117 ? 0.14755   1.70734   43.20255  1.000 36.56662  ?  117 TYR   E CD1 1 
ATOM   12524 C CD2 . TYR   I  1 117 ? 2.48143   1.27666   42.89387  1.000 53.27654  ?  117 TYR   E CD2 1 
ATOM   12525 C CE1 . TYR   I  1 117 ? 0.42937   2.99706   43.63452  1.000 36.99849  ?  117 TYR   E CE1 1 
ATOM   12526 C CE2 . TYR   I  1 117 ? 2.76781   2.55743   43.31584  1.000 30.69147  ?  117 TYR   E CE2 1 
ATOM   12527 C CZ  . TYR   I  1 117 ? 1.73672   3.41337   43.68480  1.000 47.11927  ?  117 TYR   E CZ  1 
ATOM   12528 O OH  . TYR   I  1 117 ? 2.01247   4.68604   44.11373  1.000 36.86281  ?  117 TYR   E OH  1 
ATOM   12529 N N   . MET   I  1 118 ? 2.54548   0.14692   39.78518  1.000 44.24107  ?  118 MET   E N   1 
ATOM   12530 C CA  . MET   I  1 118 ? 3.50574   1.07444   39.18336  1.000 34.07326  ?  118 MET   E CA  1 
ATOM   12531 C C   . MET   I  1 118 ? 2.94565   1.72153   37.91221  1.000 49.69368  ?  118 MET   E C   1 
ATOM   12532 O O   . MET   I  1 118 ? 3.00064   2.94717   37.75571  1.000 41.86121  ?  118 MET   E O   1 
ATOM   12533 C CB  . MET   I  1 118 ? 4.83255   0.36453   38.88290  1.000 37.14209  ?  118 MET   E CB  1 
ATOM   12534 C CG  . MET   I  1 118 ? 5.70746   -0.03752  40.07979  1.000 26.81294  ?  118 MET   E CG  1 
ATOM   12535 S SD  . MET   I  1 118 ? 6.22691   1.28873   41.19146  1.000 45.02854  ?  118 MET   E SD  1 
ATOM   12536 C CE  . MET   I  1 118 ? 7.12235   2.33820   40.04786  1.000 49.60046  ?  118 MET   E CE  1 
ATOM   12537 N N   . ILE   I  1 119 ? 2.37435   0.92614   36.99654  1.000 30.82105  ?  119 ILE   E N   1 
ATOM   12538 C CA  . ILE   I  1 119 ? 1.80486   1.54392   35.79496  1.000 42.30029  ?  119 ILE   E CA  1 
ATOM   12539 C C   . ILE   I  1 119 ? 0.43150   2.17020   36.01468  1.000 42.73540  ?  119 ILE   E C   1 
ATOM   12540 O O   . ILE   I  1 119 ? -0.03736  2.90669   35.13319  1.000 47.39744  ?  119 ILE   E O   1 
ATOM   12541 C CB  . ILE   I  1 119 ? 1.71659   0.55779   34.61255  1.000 34.27251  ?  119 ILE   E CB  1 
ATOM   12542 C CG1 . ILE   I  1 119 ? 0.58025   -0.43948  34.79224  1.000 36.56194  ?  119 ILE   E CG1 1 
ATOM   12543 C CG2 . ILE   I  1 119 ? 3.01843   -0.19347  34.45687  1.000 41.78177  ?  119 ILE   E CG2 1 
ATOM   12544 C CD1 . ILE   I  1 119 ? 0.46770   -1.38046  33.61458  1.000 41.44018  ?  119 ILE   E CD1 1 
ATOM   12545 N N   . MET   I  1 120 ? -0.21959  1.93521   37.16645  1.000 38.44012  ?  120 MET   E N   1 
ATOM   12546 C CA  . MET   I  1 120 ? -1.54332  2.50746   37.43393  1.000 36.43879  ?  120 MET   E CA  1 
ATOM   12547 C C   . MET   I  1 120 ? -1.50559  3.79982   38.24077  1.000 42.26972  ?  120 MET   E C   1 
ATOM   12548 O O   . MET   I  1 120 ? -2.50126  4.53138   38.25128  1.000 41.87465  ?  120 MET   E O   1 
ATOM   12549 C CB  . MET   I  1 120 ? -2.43034  1.50905   38.20010  1.000 24.06386  ?  120 MET   E CB  1 
ATOM   12550 C CG  . MET   I  1 120 ? -2.88246  0.31640   37.38753  1.000 31.95497  ?  120 MET   E CG  1 
ATOM   12551 S SD  . MET   I  1 120 ? -4.01723  0.71319   36.06605  1.000 48.07394  ?  120 MET   E SD  1 
ATOM   12552 C CE  . MET   I  1 120 ? -5.55183  0.86377   36.98402  1.000 32.71417  ?  120 MET   E CE  1 
ATOM   12553 N N   . ALA   I  1 121 ? -0.39217  4.08794   38.92126  1.000 31.46277  ?  121 ALA   E N   1 
ATOM   12554 C CA  . ALA   I  1 121 ? -0.39174  5.13667   39.94045  1.000 37.24764  ?  121 ALA   E CA  1 
ATOM   12555 C C   . ALA   I  1 121 ? -0.77205  6.49118   39.35730  1.000 37.62325  ?  121 ALA   E C   1 
ATOM   12556 O O   . ALA   I  1 121 ? -1.49713  7.26761   39.99563  1.000 44.59677  ?  121 ALA   E O   1 
ATOM   12557 C CB  . ALA   I  1 121 ? 0.97995   5.20981   40.62294  1.000 29.16352  ?  121 ALA   E CB  1 
ATOM   12558 N N   . LYS   I  1 122 ? -0.28566  6.80109   38.14731  1.000 37.93104  ?  122 LYS   E N   1 
ATOM   12559 C CA  . LYS   I  1 122 ? -0.62058  8.08663   37.53820  1.000 30.46776  ?  122 LYS   E CA  1 
ATOM   12560 C C   . LYS   I  1 122 ? -2.12291  8.16845   37.24007  1.000 44.69301  ?  122 LYS   E C   1 
ATOM   12561 O O   . LYS   I  1 122 ? -2.75337  9.20049   37.47928  1.000 38.52513  ?  122 LYS   E O   1 
ATOM   12562 C CB  . LYS   I  1 122 ? 0.22293   8.31529   36.26741  1.000 29.88246  ?  122 LYS   E CB  1 
ATOM   12563 N N   . LEU   I  1 123 ? -2.72618  7.06801   36.77326  1.000 33.61360  ?  123 LEU   E N   1 
ATOM   12564 C CA  . LEU   I  1 123 ? -4.17091  7.02830   36.51523  1.000 33.11428  ?  123 LEU   E CA  1 
ATOM   12565 C C   . LEU   I  1 123 ? -4.98191  7.16904   37.80027  1.000 58.10386  ?  123 LEU   E C   1 
ATOM   12566 O O   . LEU   I  1 123 ? -5.96127  7.93415   37.85391  1.000 25.18315  ?  123 LEU   E O   1 
ATOM   12567 C CB  . LEU   I  1 123 ? -4.53952  5.72630   35.79947  1.000 24.20122  ?  123 LEU   E CB  1 
ATOM   12568 C CG  . LEU   I  1 123 ? -3.61269  5.41261   34.63177  1.000 33.14364  ?  123 LEU   E CG  1 
ATOM   12569 C CD1 . LEU   I  1 123 ? -4.01322  4.12727   33.92176  1.000 27.29820  ?  123 LEU   E CD1 1 
ATOM   12570 C CD2 . LEU   I  1 123 ? -3.62717  6.57975   33.67630  1.000 27.12767  ?  123 LEU   E CD2 1 
ATOM   12571 N N   . MET   I  1 124 ? -4.61425  6.40217   38.83651  1.000 35.58416  ?  124 MET   E N   1 
ATOM   12572 C CA  . MET   I  1 124 ? -5.31875  6.49526   40.11123  1.000 46.97546  ?  124 MET   E CA  1 
ATOM   12573 C C   . MET   I  1 124 ? -5.34008  7.91480   40.64869  1.000 39.54194  ?  124 MET   E C   1 
ATOM   12574 O O   . MET   I  1 124 ? -6.23593  8.27112   41.42214  1.000 38.69160  ?  124 MET   E O   1 
ATOM   12575 C CB  . MET   I  1 124 ? -4.66976  5.59002   41.14969  1.000 24.55822  ?  124 MET   E CB  1 
ATOM   12576 C CG  . MET   I  1 124 ? -4.65237  4.14057   40.77935  1.000 44.80345  ?  124 MET   E CG  1 
ATOM   12577 S SD  . MET   I  1 124 ? -3.31855  3.29777   41.65734  1.000 46.68910  ?  124 MET   E SD  1 
ATOM   12578 C CE  . MET   I  1 124 ? -3.74519  3.55500   43.36679  1.000 22.36146  ?  124 MET   E CE  1 
ATOM   12579 N N   . ASN   I  1 125 ? -4.36062  8.73182   40.26429  1.000 51.17823  ?  125 ASN   E N   1 
ATOM   12580 C CA  . ASN   I  1 125 ? -4.20642  10.07255  40.79940  1.000 45.06035  ?  125 ASN   E CA  1 
ATOM   12581 C C   . ASN   I  1 125 ? -5.00588  11.12629  40.02048  1.000 50.68404  ?  125 ASN   E C   1 
ATOM   12582 O O   . ASN   I  1 125 ? -4.68993  12.31783  40.09246  1.000 54.67243  ?  125 ASN   E O   1 
ATOM   12583 C CB  . ASN   I  1 125 ? -2.72773  10.45291  40.82510  1.000 43.54636  ?  125 ASN   E CB  1 
ATOM   12584 C CG  . ASN   I  1 125 ? -2.43231  11.54623  41.82898  1.000 41.67728  ?  125 ASN   E CG  1 
ATOM   12585 O OD1 . ASN   I  1 125 ? -3.23355  11.82268  42.73153  1.000 47.84061  ?  125 ASN   E OD1 1 
ATOM   12586 N ND2 . ASN   I  1 125 ? -1.27242  12.16879  41.68740  1.000 58.99042  ?  125 ASN   E ND2 1 
ATOM   12587 N N   . THR   I  1 126 ? -6.03833  10.72466  39.29788  1.000 49.95874  ?  126 THR   E N   1 
ATOM   12588 C CA  . THR   I  1 126 ? -6.90584  11.65264  38.59254  1.000 59.04867  ?  126 THR   E CA  1 
ATOM   12589 C C   . THR   I  1 126 ? -8.33624  11.47302  39.07444  1.000 37.91905  ?  126 THR   E C   1 
ATOM   12590 O O   . THR   I  1 126 ? -8.69222  10.44304  39.65439  1.000 56.84171  ?  126 THR   E O   1 
ATOM   12591 C CB  . THR   I  1 126 ? -6.85080  11.42887  37.07588  1.000 43.79877  ?  126 THR   E CB  1 
ATOM   12592 O OG1 . THR   I  1 126 ? -7.54227  10.21024  36.74126  1.000 43.22111  ?  126 THR   E OG1 1 
ATOM   12593 C CG2 . THR   I  1 126 ? -5.40256  11.34145  36.60052  1.000 28.81895  ?  126 THR   E CG2 1 
ATOM   12594 N N   . ARG   I  1 127 ? -9.15025  12.49172  38.82823  1.000 45.76714  ?  127 ARG   E N   1 
ATOM   12595 C CA  . ARG   I  1 127 ? -10.54904 12.31650  39.16260  1.000 29.64650  ?  127 ARG   E CA  1 
ATOM   12596 C C   . ARG   I  1 127 ? -11.23175 11.31007  38.21516  1.000 36.11247  ?  127 ARG   E C   1 
ATOM   12597 O O   . ARG   I  1 127 ? -12.04028 10.49896  38.67597  1.000 78.83958  ?  127 ARG   E O   1 
ATOM   12598 C CB  . ARG   I  1 127 ? -11.22762 13.69573  39.23765  1.000 29.29236  ?  127 ARG   E CB  1 
ATOM   12599 C CG  . ARG   I  1 127 ? -10.99675 14.35213  40.64881  1.000 114.12592 ?  127 ARG   E CG  1 
ATOM   12600 C CD  . ARG   I  1 127 ? -11.77330 15.64771  40.97009  1.000 122.39712 ?  127 ARG   E CD  1 
ATOM   12601 N NE  . ARG   I  1 127 ? -13.21721 15.50193  40.83197  1.000 129.19791 ?  127 ARG   E NE  1 
ATOM   12602 C CZ  . ARG   I  1 127 ? -13.90694 15.96084  39.79509  1.000 148.14356 ?  127 ARG   E CZ  1 
ATOM   12603 N NH1 . ARG   I  1 127 ? -13.31611 16.65009  38.82544  1.000 140.44833 ?  127 ARG   E NH1 1 
ATOM   12604 N NH2 . ARG   I  1 127 ? -15.21826 15.72158  39.72626  1.000 132.23644 ?  127 ARG   E NH2 1 
ATOM   12605 N N   . ALA   I  1 128 ? -10.87095 11.27833  36.92702  1.000 36.23128  ?  128 ALA   E N   1 
ATOM   12606 C CA  . ALA   I  1 128 ? -11.42160 10.28745  36.00778  1.000 49.20253  ?  128 ALA   E CA  1 
ATOM   12607 C C   . ALA   I  1 128 ? -11.06400 8.87149   36.45341  1.000 40.13381  ?  128 ALA   E C   1 
ATOM   12608 O O   . ALA   I  1 128 ? -11.91735 7.97259   36.42765  1.000 50.97357  ?  128 ALA   E O   1 
ATOM   12609 C CB  . ALA   I  1 128 ? -10.92707 10.55902  34.57687  1.000 37.97076  ?  128 ALA   E CB  1 
ATOM   12610 N N   . GLY   I  1 129 ? -9.81292  8.65965   36.88730  1.000 54.38712  ?  129 GLY   E N   1 
ATOM   12611 C CA  . GLY   I  1 129 ? -9.39710  7.32846   37.32158  1.000 22.39633  ?  129 GLY   E CA  1 
ATOM   12612 C C   . GLY   I  1 129 ? -10.12542 6.86887   38.57605  1.000 46.89321  ?  129 GLY   E C   1 
ATOM   12613 O O   . GLY   I  1 129 ? -10.61939 5.73695   38.65016  1.000 36.73853  ?  129 GLY   E O   1 
ATOM   12614 N N   . PHE   I  1 130 ? -10.21799 7.75022   39.57560  1.000 33.05459  ?  130 PHE   E N   1 
ATOM   12615 C CA  . PHE   I  1 130 ? -10.96566 7.41161   40.77976  1.000 33.14098  ?  130 PHE   E CA  1 
ATOM   12616 C C   . PHE   I  1 130 ? -12.41644 7.04011   40.45639  1.000 54.07254  ?  130 PHE   E C   1 
ATOM   12617 O O   . PHE   I  1 130 ? -12.93443 6.05588   40.99458  1.000 45.22729  ?  130 PHE   E O   1 
ATOM   12618 C CB  . PHE   I  1 130 ? -10.89499 8.57435   41.76736  1.000 21.73321  ?  130 PHE   E CB  1 
ATOM   12619 C CG  . PHE   I  1 130 ? -11.69125 8.35781   43.01532  1.000 35.17789  ?  130 PHE   E CG  1 
ATOM   12620 C CD1 . PHE   I  1 130 ? -13.05929 8.64354   43.04982  1.000 35.17388  ?  130 PHE   E CD1 1 
ATOM   12621 C CD2 . PHE   I  1 130 ? -11.08156 7.87875   44.16024  1.000 28.77512  ?  130 PHE   E CD2 1 
ATOM   12622 C CE1 . PHE   I  1 130 ? -13.81109 8.44872   44.19946  1.000 34.00685  ?  130 PHE   E CE1 1 
ATOM   12623 C CE2 . PHE   I  1 130 ? -11.82851 7.67589   45.32063  1.000 42.59998  ?  130 PHE   E CE2 1 
ATOM   12624 C CZ  . PHE   I  1 130 ? -13.21057 7.97188   45.33189  1.000 29.04854  ?  130 PHE   E CZ  1 
ATOM   12625 N N   . SER   I  1 131 ? -13.09343 7.81590   39.59246  1.000 33.38944  ?  131 SER   E N   1 
ATOM   12626 C CA  . SER   I  1 131 ? -14.45250 7.44811   39.18141  1.000 51.06281  ?  131 SER   E CA  1 
ATOM   12627 C C   . SER   I  1 131 ? -14.49999 6.03324   38.61730  1.000 38.72186  ?  131 SER   E C   1 
ATOM   12628 O O   . SER   I  1 131 ? -15.34237 5.21708   39.02025  1.000 49.56845  ?  131 SER   E O   1 
ATOM   12629 C CB  . SER   I  1 131 ? -14.99762 8.42901   38.14406  1.000 22.28787  ?  131 SER   E CB  1 
ATOM   12630 O OG  . SER   I  1 131 ? -15.73532 9.43821   38.77832  1.000 94.15488  ?  131 SER   E OG  1 
ATOM   12631 N N   . ALA   I  1 132 ? -13.62526 5.73881   37.64887  1.000 35.65447  ?  132 ALA   E N   1 
ATOM   12632 C CA  . ALA   I  1 132 ? -13.64604 4.42394   37.01874  1.000 29.91669  ?  132 ALA   E CA  1 
ATOM   12633 C C   . ALA   I  1 132 ? -13.42105 3.33020   38.04938  1.000 44.20692  ?  132 ALA   E C   1 
ATOM   12634 O O   . ALA   I  1 132 ? -14.16332 2.33724   38.09702  1.000 37.97106  ?  132 ALA   E O   1 
ATOM   12635 C CB  . ALA   I  1 132 ? -12.58842 4.34826   35.92255  1.000 30.63890  ?  132 ALA   E CB  1 
ATOM   12636 N N   . PHE   I  1 133 ? -12.41772 3.52460   38.91051  1.000 32.03044  ?  133 PHE   E N   1 
ATOM   12637 C CA  . PHE   I  1 133 ? -11.96746 2.51921   39.86532  1.000 42.60514  ?  133 PHE   E CA  1 
ATOM   12638 C C   . PHE   I  1 133 ? -12.90392 2.37419   41.06192  1.000 49.55380  ?  133 PHE   E C   1 
ATOM   12639 O O   . PHE   I  1 133 ? -12.67787 1.50098   41.91068  1.000 39.06637  ?  133 PHE   E O   1 
ATOM   12640 C CB  . PHE   I  1 133 ? -10.54448 2.84947   40.32727  1.000 34.82394  ?  133 PHE   E CB  1 
ATOM   12641 C CG  . PHE   I  1 133 ? -9.57619  3.04115   39.18391  1.000 45.77399  ?  133 PHE   E CG  1 
ATOM   12642 C CD1 . PHE   I  1 133 ? -9.81988  2.44800   37.93481  1.000 41.32619  ?  133 PHE   E CD1 1 
ATOM   12643 C CD2 . PHE   I  1 133 ? -8.43608  3.82379   39.34361  1.000 36.03869  ?  133 PHE   E CD2 1 
ATOM   12644 C CE1 . PHE   I  1 133 ? -8.94166  2.63078   36.87015  1.000 33.19059  ?  133 PHE   E CE1 1 
ATOM   12645 C CE2 . PHE   I  1 133 ? -7.55126  4.01892   38.29159  1.000 35.46170  ?  133 PHE   E CE2 1 
ATOM   12646 C CZ  . PHE   I  1 133 ? -7.80176  3.41907   37.04739  1.000 29.25421  ?  133 PHE   E CZ  1 
ATOM   12647 N N   . THR   I  1 134 ? -13.96291 3.18121   41.14465  1.000 29.20898  ?  134 THR   E N   1 
ATOM   12648 C CA  . THR   I  1 134 ? -14.96907 3.01162   42.18313  1.000 33.86774  ?  134 THR   E CA  1 
ATOM   12649 C C   . THR   I  1 134 ? -16.30520 2.52508   41.61548  1.000 31.69444  ?  134 THR   E C   1 
ATOM   12650 O O   . THR   I  1 134 ? -17.35742 2.72844   42.22644  1.000 39.64601  ?  134 THR   E O   1 
ATOM   12651 C CB  . THR   I  1 134 ? -15.14929 4.29504   42.99674  1.000 33.88451  ?  134 THR   E CB  1 
ATOM   12652 O OG1 . THR   I  1 134 ? -15.24602 5.43320   42.12871  1.000 39.57278  ?  134 THR   E OG1 1 
ATOM   12653 C CG2 . THR   I  1 134 ? -13.97438 4.47868   43.95577  1.000 26.87967  ?  134 THR   E CG2 1 
ATOM   12654 N N   . ARG   I  1 135 ? -16.26865 1.84353   40.46760  1.000 39.89665  ?  135 ARG   E N   1 
ATOM   12655 C CA  . ARG   I  1 135 ? -17.43454 1.16643   39.90214  1.000 40.07507  ?  135 ARG   E CA  1 
ATOM   12656 C C   . ARG   I  1 135 ? -17.30436 -0.32763  40.17127  1.000 53.69987  ?  135 ARG   E C   1 
ATOM   12657 O O   . ARG   I  1 135 ? -16.33046 -0.95807  39.73531  1.000 40.30891  ?  135 ARG   E O   1 
ATOM   12658 C CB  . ARG   I  1 135 ? -17.55953 1.41287   38.39701  1.000 30.89317  ?  135 ARG   E CB  1 
ATOM   12659 C CG  . ARG   I  1 135 ? -17.69546 2.87830   37.98800  1.000 35.09848  ?  135 ARG   E CG  1 
ATOM   12660 C CD  . ARG   I  1 135 ? -17.41340 2.98979   36.51288  1.000 37.83441  ?  135 ARG   E CD  1 
ATOM   12661 N NE  . ARG   I  1 135 ? -17.57946 4.34130   36.00773  1.000 57.12923  ?  135 ARG   E NE  1 
ATOM   12662 C CZ  . ARG   I  1 135 ? -18.75288 4.93750   35.85592  1.000 60.94532  ?  135 ARG   E CZ  1 
ATOM   12663 N NH1 . ARG   I  1 135 ? -19.88477 4.32315   36.16198  1.000 52.11985  ?  135 ARG   E NH1 1 
ATOM   12664 N NH2 . ARG   I  1 135 ? -18.79032 6.18913   35.40307  1.000 50.04974  ?  135 ARG   E NH2 1 
ATOM   12665 N N   . GLN   I  1 136 ? -18.28224 -0.89160  40.89106  1.000 39.01184  ?  136 GLN   E N   1 
ATOM   12666 C CA  . GLN   I  1 136 ? -18.25332 -2.32353  41.17636  1.000 41.03032  ?  136 GLN   E CA  1 
ATOM   12667 C C   . GLN   I  1 136 ? -18.16260 -3.14408  39.90054  1.000 38.39441  ?  136 GLN   E C   1 
ATOM   12668 O O   . GLN   I  1 136 ? -17.51858 -4.20368  39.89324  1.000 55.88879  ?  136 GLN   E O   1 
ATOM   12669 C CB  . GLN   I  1 136 ? -19.48391 -2.73062  41.98521  1.000 39.08280  ?  136 GLN   E CB  1 
ATOM   12670 C CG  . GLN   I  1 136 ? -19.55592 -2.03902  43.32441  1.000 34.31559  ?  136 GLN   E CG  1 
ATOM   12671 C CD  . GLN   I  1 136 ? -19.90035 -2.98513  44.44726  1.000 59.57392  ?  136 GLN   E CD  1 
ATOM   12672 O OE1 . GLN   I  1 136 ? -20.82010 -3.82317  44.32937  1.000 47.49389  ?  136 GLN   E OE1 1 
ATOM   12673 N NE2 . GLN   I  1 136 ? -19.15682 -2.86905  45.55254  1.000 34.81801  ?  136 GLN   E NE2 1 
ATOM   12674 N N   . ARG   I  1 137 ? -18.70618 -2.60667  38.80337  1.000 22.19505  ?  137 ARG   E N   1 
ATOM   12675 C CA  . ARG   I  1 137 ? -18.79180 -3.34276  37.54856  1.000 63.85541  ?  137 ARG   E CA  1 
ATOM   12676 C C   . ARG   I  1 137 ? -17.42677 -3.50068  36.88963  1.000 49.52893  ?  137 ARG   E C   1 
ATOM   12677 O O   . ARG   I  1 137 ? -17.08751 -4.59158  36.42206  1.000 25.49321  ?  137 ARG   E O   1 
ATOM   12678 C CB  . ARG   I  1 137 ? -19.82346 -2.65794  36.65221  1.000 91.48810  ?  137 ARG   E CB  1 
ATOM   12679 C CG  . ARG   I  1 137 ? -21.22202 -2.98834  37.13390  1.000 90.56407  ?  137 ARG   E CG  1 
ATOM   12680 C CD  . ARG   I  1 137 ? -21.32241 -4.51319  37.42196  1.000 146.94092 ?  137 ARG   E CD  1 
ATOM   12681 N NE  . ARG   I  1 137 ? -22.50032 -5.03147  36.74061  1.000 162.42371 ?  137 ARG   E NE  1 
ATOM   12682 C CZ  . ARG   I  1 137 ? -22.73930 -6.28453  36.36831  1.000 137.08624 ?  137 ARG   E CZ  1 
ATOM   12683 N NH1 . ARG   I  1 137 ? -21.91418 -7.27952  36.68446  1.000 102.60314 ?  137 ARG   E NH1 1 
ATOM   12684 N NH2 . ARG   I  1 137 ? -23.81662 -6.54330  35.64130  1.000 122.28695 ?  137 ARG   E NH2 1 
ATOM   12685 N N   . LEU   I  1 138 ? -16.59608 -2.45417  36.94141  1.000 28.91225  ?  138 LEU   E N   1 
ATOM   12686 C CA  . LEU   I  1 138 ? -15.18837 -2.52572  36.53699  1.000 41.96972  ?  138 LEU   E CA  1 
ATOM   12687 C C   . LEU   I  1 138 ? -14.36372 -3.39191  37.48827  1.000 51.40873  ?  138 LEU   E C   1 
ATOM   12688 O O   . LEU   I  1 138 ? -13.52549 -4.19076  37.04887  1.000 40.95801  ?  138 LEU   E O   1 
ATOM   12689 C CB  . LEU   I  1 138 ? -14.58703 -1.12567  36.47602  1.000 35.75305  ?  138 LEU   E CB  1 
ATOM   12690 C CG  . LEU   I  1 138 ? -13.17321 -1.08409  35.91934  1.000 49.63291  ?  138 LEU   E CG  1 
ATOM   12691 C CD1 . LEU   I  1 138 ? -13.22725 -1.51064  34.46720  1.000 36.11144  ?  138 LEU   E CD1 1 
ATOM   12692 C CD2 . LEU   I  1 138 ? -12.57128 0.30520   36.05031  1.000 33.44443  ?  138 LEU   E CD2 1 
ATOM   12693 N N   . ASN   I  1 139 ? -14.57844 -3.24319  38.79535  1.000 37.28903  ?  139 ASN   E N   1 
ATOM   12694 C CA  . ASN   I  1 139 ? -13.76403 -3.99181  39.74314  1.000 53.49147  ?  139 ASN   E CA  1 
ATOM   12695 C C   . ASN   I  1 139 ? -13.96751 -5.49545  39.60409  1.000 40.09876  ?  139 ASN   E C   1 
ATOM   12696 O O   . ASN   I  1 139 ? -13.04246 -6.26513  39.89906  1.000 54.00095  ?  139 ASN   E O   1 
ATOM   12697 C CB  . ASN   I  1 139 ? -14.04207 -3.49875  41.16189  1.000 29.79265  ?  139 ASN   E CB  1 
ATOM   12698 C CG  . ASN   I  1 139 ? -13.38744 -2.15781  41.41514  1.000 46.61510  ?  139 ASN   E CG  1 
ATOM   12699 O OD1 . ASN   I  1 139 ? -12.24336 -1.94390  40.99343  1.000 38.19396  ?  139 ASN   E OD1 1 
ATOM   12700 N ND2 . ASN   I  1 139 ? -14.10564 -1.23453  42.04829  1.000 35.01482  ?  139 ASN   E ND2 1 
ATOM   12701 N N   . LEU   I  1 140 ? -15.14484 -5.93124  39.13135  1.000 49.72080  ?  140 LEU   E N   1 
ATOM   12702 C CA  . LEU   I  1 140 ? -15.32836 -7.34526  38.80078  1.000 37.87241  ?  140 LEU   E CA  1 
ATOM   12703 C C   . LEU   I  1 140 ? -14.29288 -7.81170  37.78778  1.000 60.15257  ?  140 LEU   E C   1 
ATOM   12704 O O   . LEU   I  1 140 ? -13.81095 -8.95169  37.86366  1.000 39.07798  ?  140 LEU   E O   1 
ATOM   12705 C CB  . LEU   I  1 140 ? -16.72488 -7.59297  38.24564  1.000 37.41107  ?  140 LEU   E CB  1 
ATOM   12706 C CG  . LEU   I  1 140 ? -17.84192 -7.54837  39.27709  1.000 53.65214  ?  140 LEU   E CG  1 
ATOM   12707 C CD1 . LEU   I  1 140 ? -19.20182 -7.70076  38.62483  1.000 31.62032  ?  140 LEU   E CD1 1 
ATOM   12708 C CD2 . LEU   I  1 140 ? -17.61500 -8.62386  40.30777  1.000 25.47547  ?  140 LEU   E CD2 1 
ATOM   12709 N N   . HIS   I  1 141 ? -13.93773 -6.94157  36.82790  1.000 36.40126  ?  141 HIS   E N   1 
ATOM   12710 C CA  . HIS   I  1 141 ? -12.95198 -7.32501  35.82205  1.000 34.29997  ?  141 HIS   E CA  1 
ATOM   12711 C C   . HIS   I  1 141 ? -11.54449 -7.35840  36.40438  1.000 35.47701  ?  141 HIS   E C   1 
ATOM   12712 O O   . HIS   I  1 141 ? -10.79469 -8.31123  36.16213  1.000 42.16400  ?  141 HIS   E O   1 
ATOM   12713 C CB  . HIS   I  1 141 ? -13.03290 -6.38708  34.63139  1.000 24.27586  ?  141 HIS   E CB  1 
ATOM   12714 C CG  . HIS   I  1 141 ? -14.25296 -6.60944  33.79722  1.000 51.82662  ?  141 HIS   E CG  1 
ATOM   12715 N ND1 . HIS   I  1 141 ? -14.32423 -7.59928  32.84213  1.000 49.66409  ?  141 HIS   E ND1 1 
ATOM   12716 C CD2 . HIS   I  1 141 ? -15.46216 -5.99660  33.79664  1.000 44.98536  ?  141 HIS   E CD2 1 
ATOM   12717 C CE1 . HIS   I  1 141 ? -15.51876 -7.57734  32.27815  1.000 37.18637  ?  141 HIS   E CE1 1 
ATOM   12718 N NE2 . HIS   I  1 141 ? -16.22762 -6.61126  32.83554  1.000 50.43466  ?  141 HIS   E NE2 1 
ATOM   12719 N N   . PHE   I  1 142 ? -11.17135 -6.34453  37.19590  1.000 35.72887  ?  142 PHE   E N   1 
ATOM   12720 C CA  . PHE   I  1 142 ? -9.88265  -6.40124  37.88692  1.000 48.96389  ?  142 PHE   E CA  1 
ATOM   12721 C C   . PHE   I  1 142 ? -9.75119  -7.68767  38.68872  1.000 35.85862  ?  142 PHE   E C   1 
ATOM   12722 O O   . PHE   I  1 142 ? -8.68664  -8.32371  38.69702  1.000 37.81780  ?  142 PHE   E O   1 
ATOM   12723 C CB  . PHE   I  1 142 ? -9.70900  -5.18840  38.79970  1.000 34.92970  ?  142 PHE   E CB  1 
ATOM   12724 C CG  . PHE   I  1 142 ? -9.37651  -3.92492  38.06615  1.000 42.11408  ?  142 PHE   E CG  1 
ATOM   12725 C CD1 . PHE   I  1 142 ? -8.38480  -3.91124  37.10375  1.000 36.94612  ?  142 PHE   E CD1 1 
ATOM   12726 C CD2 . PHE   I  1 142 ? -10.06380 -2.74965  38.33161  1.000 38.43718  ?  142 PHE   E CD2 1 
ATOM   12727 C CE1 . PHE   I  1 142 ? -8.08368  -2.74594  36.42505  1.000 36.02488  ?  142 PHE   E CE1 1 
ATOM   12728 C CE2 . PHE   I  1 142 ? -9.75655  -1.58137  37.65300  1.000 39.54245  ?  142 PHE   E CE2 1 
ATOM   12729 C CZ  . PHE   I  1 142 ? -8.76931  -1.58594  36.70268  1.000 34.75910  ?  142 PHE   E CZ  1 
ATOM   12730 N N   . LYS   I  1 143 ? -10.82543 -8.08666  39.36730  1.000 36.38074  ?  143 LYS   E N   1 
ATOM   12731 C CA  . LYS   I  1 143 ? -10.79158 -9.33542  40.11147  1.000 32.04771  ?  143 LYS   E CA  1 
ATOM   12732 C C   . LYS   I  1 143 ? -10.39976 -10.48525 39.20259  1.000 35.32334  ?  143 LYS   E C   1 
ATOM   12733 O O   . LYS   I  1 143 ? -9.47108  -11.24283 39.51642  1.000 38.68491  ?  143 LYS   E O   1 
ATOM   12734 C CB  . LYS   I  1 143 ? -12.14338 -9.60234  40.76247  1.000 35.60085  ?  143 LYS   E CB  1 
ATOM   12735 C CG  . LYS   I  1 143 ? -12.08234 -10.68319 41.80380  1.000 22.16555  ?  143 LYS   E CG  1 
ATOM   12736 C CD  . LYS   I  1 143 ? -13.34875 -11.48766 41.83382  1.000 30.32716  ?  143 LYS   E CD  1 
ATOM   12737 C CE  . LYS   I  1 143 ? -13.39933 -12.34474 43.08400  1.000 36.88546  ?  143 LYS   E CE  1 
ATOM   12738 N NZ  . LYS   I  1 143 ? -12.34817 -13.39659 43.12624  1.000 41.49461  ?  143 LYS   E NZ  1 
ATOM   12739 N N   . LYS   I  1 144 ? -11.07190 -10.57082 38.03189  1.000 26.15979  ?  144 LYS   E N   1 
ATOM   12740 C CA  . LYS   I  1 144 ? -10.82675 -11.64308 37.07065  1.000 58.47777  ?  144 LYS   E CA  1 
ATOM   12741 C C   . LYS   I  1 144 ? -9.39722  -11.58667 36.57031  1.000 17.06059  ?  144 LYS   E C   1 
ATOM   12742 O O   . LYS   I  1 144 ? -8.70414  -12.61459 36.52674  1.000 78.55735  ?  144 LYS   E O   1 
ATOM   12743 C CB  . LYS   I  1 144 ? -11.83200 -11.56413 35.90945  1.000 29.28400  ?  144 LYS   E CB  1 
ATOM   12744 C CG  . LYS   I  1 144 ? -11.87118 -12.77057 34.96430  1.000 40.73924  ?  144 LYS   E CG  1 
ATOM   12745 C CD  . LYS   I  1 144 ? -12.16702 -14.10607 35.66015  1.000 93.19605  ?  144 LYS   E CD  1 
ATOM   12746 C CE  . LYS   I  1 144 ? -11.38226 -15.26236 35.03711  1.000 110.71771 ?  144 LYS   E CE  1 
ATOM   12747 N NZ  . LYS   I  1 144 ? -11.66945 -16.56263 35.71071  1.000 90.09712  ?  144 LYS   E NZ  1 
ATOM   12748 N N   . LEU   I  1 145 ? -8.91165  -10.38370 36.26833  1.000 27.58527  ?  145 LEU   E N   1 
ATOM   12749 C CA  . LEU   I  1 145 ? -7.54382  -10.21668 35.78452  1.000 22.01330  ?  145 LEU   E CA  1 
ATOM   12750 C C   . LEU   I  1 145 ? -6.54012  -10.74340 36.80826  1.000 42.17456  ?  145 LEU   E C   1 
ATOM   12751 O O   . LEU   I  1 145 ? -5.70295  -11.59946 36.49481  1.000 40.40146  ?  145 LEU   E O   1 
ATOM   12752 C CB  . LEU   I  1 145 ? -7.27383  -8.74547  35.44940  1.000 32.84958  ?  145 LEU   E CB  1 
ATOM   12753 C CG  . LEU   I  1 145 ? -8.13097  -8.17774  34.31073  1.000 35.50091  ?  145 LEU   E CG  1 
ATOM   12754 C CD1 . LEU   I  1 145 ? -7.75670  -6.74087  33.97057  1.000 29.20201  ?  145 LEU   E CD1 1 
ATOM   12755 C CD2 . LEU   I  1 145 ? -8.00324  -9.04927  33.08654  1.000 28.58184  ?  145 LEU   E CD2 1 
ATOM   12756 N N   . PHE   I  1 146 ? -6.65200  -10.28944 38.05854  1.000 24.73883  ?  146 PHE   E N   1 
ATOM   12757 C CA  . PHE   I  1 146 ? -5.66288  -10.66402 39.06461  1.000 28.69295  ?  146 PHE   E CA  1 
ATOM   12758 C C   . PHE   I  1 146 ? -5.79181  -12.12538 39.47133  1.000 36.93222  ?  146 PHE   E C   1 
ATOM   12759 O O   . PHE   I  1 146 ? -4.77915  -12.77472 39.75318  1.000 37.64194  ?  146 PHE   E O   1 
ATOM   12760 C CB  . PHE   I  1 146 ? -5.78381  -9.74542  40.28402  1.000 28.92162  ?  146 PHE   E CB  1 
ATOM   12761 C CG  . PHE   I  1 146 ? -5.63411  -8.27227  39.95780  1.000 32.49525  ?  146 PHE   E CG  1 
ATOM   12762 C CD1 . PHE   I  1 146 ? -4.93857  -7.85390  38.82168  1.000 32.53867  ?  146 PHE   E CD1 1 
ATOM   12763 C CD2 . PHE   I  1 146 ? -6.17850  -7.31073  40.78985  1.000 25.60373  ?  146 PHE   E CD2 1 
ATOM   12764 C CE1 . PHE   I  1 146 ? -4.79552  -6.50754  38.53046  1.000 32.65395  ?  146 PHE   E CE1 1 
ATOM   12765 C CE2 . PHE   I  1 146 ? -6.04374  -5.95796  40.50480  1.000 29.18678  ?  146 PHE   E CE2 1 
ATOM   12766 C CZ  . PHE   I  1 146 ? -5.34927  -5.55294  39.37623  1.000 34.84496  ?  146 PHE   E CZ  1 
ATOM   12767 N N   . ASP   I  1 147 ? -7.01176  -12.66697 39.50997  1.000 40.74644  ?  147 ASP   E N   1 
ATOM   12768 C CA  . ASP   I  1 147 ? -7.14032  -14.09969 39.76178  1.000 34.37446  ?  147 ASP   E CA  1 
ATOM   12769 C C   . ASP   I  1 147 ? -6.43331  -14.89726 38.67331  1.000 43.93918  ?  147 ASP   E C   1 
ATOM   12770 O O   . ASP   I  1 147 ? -5.73831  -15.88771 38.96111  1.000 42.25302  ?  147 ASP   E O   1 
ATOM   12771 C CB  . ASP   I  1 147 ? -8.61293  -14.51446 39.84819  1.000 26.82090  ?  147 ASP   E CB  1 
ATOM   12772 C CG  . ASP   I  1 147 ? -9.29387  -14.05178 41.13334  1.000 59.89907  ?  147 ASP   E CG  1 
ATOM   12773 O OD1 . ASP   I  1 147 ? -8.59910  -13.72059 42.13117  1.000 52.01506  ?  147 ASP   E OD1 1 
ATOM   12774 O OD2 . ASP   I  1 147 ? -10.54398 -14.03881 41.13588  1.000 56.19553  -1 147 ASP   E OD2 1 
ATOM   12775 N N   . THR   I  1 148 ? -6.60390  -14.47711 37.41280  1.000 36.30750  ?  148 THR   E N   1 
ATOM   12776 C CA  . THR   I  1 148 ? -5.93090  -15.14307 36.30335  1.000 45.75629  ?  148 THR   E CA  1 
ATOM   12777 C C   . THR   I  1 148 ? -4.42019  -15.07965 36.48713  1.000 42.66207  ?  148 THR   E C   1 
ATOM   12778 O O   . THR   I  1 148 ? -3.72463  -16.09750 36.36583  1.000 48.67772  ?  148 THR   E O   1 
ATOM   12779 C CB  . THR   I  1 148 ? -6.36158  -14.50611 34.97459  1.000 40.61752  ?  148 THR   E CB  1 
ATOM   12780 O OG1 . THR   I  1 148 ? -7.71974  -14.86175 34.69639  1.000 41.48507  ?  148 THR   E OG1 1 
ATOM   12781 C CG2 . THR   I  1 148 ? -5.49006  -14.98446 33.82130  1.000 29.92091  ?  148 THR   E CG2 1 
ATOM   12782 N N   . TRP   I  1 149 ? -3.90390  -13.88643 36.81923  1.000 34.91851  ?  149 TRP   E N   1 
ATOM   12783 C CA  . TRP   I  1 149 ? -2.47639  -13.72034 37.07415  1.000 28.02441  ?  149 TRP   E CA  1 
ATOM   12784 C C   . TRP   I  1 149 ? -2.01896  -14.64127 38.19725  1.000 52.05072  ?  149 TRP   E C   1 
ATOM   12785 O O   . TRP   I  1 149 ? -0.97137  -15.29008 38.09196  1.000 36.86996  ?  149 TRP   E O   1 
ATOM   12786 C CB  . TRP   I  1 149 ? -2.18034  -12.25299 37.41337  1.000 25.59527  ?  149 TRP   E CB  1 
ATOM   12787 C CG  . TRP   I  1 149 ? -0.69897  -11.89502 37.53417  1.000 36.62004  ?  149 TRP   E CG  1 
ATOM   12788 C CD1 . TRP   I  1 149 ? 0.36842   -12.65854 37.14511  1.000 30.94212  ?  149 TRP   E CD1 1 
ATOM   12789 C CD2 . TRP   I  1 149 ? -0.13889  -10.68452 38.08482  1.000 46.95869  ?  149 TRP   E CD2 1 
ATOM   12790 N NE1 . TRP   I  1 149 ? 1.54853   -12.00154 37.41172  1.000 43.15403  ?  149 TRP   E NE1 1 
ATOM   12791 C CE2 . TRP   I  1 149 ? 1.26633   -10.79172 37.98965  1.000 29.43255  ?  149 TRP   E CE2 1 
ATOM   12792 C CE3 . TRP   I  1 149 ? -0.68978  -9.52248  38.65159  1.000 28.55001  ?  149 TRP   E CE3 1 
ATOM   12793 C CZ2 . TRP   I  1 149 ? 2.13001   -9.77797  38.42712  1.000 38.87807  ?  149 TRP   E CZ2 1 
ATOM   12794 C CZ3 . TRP   I  1 149 ? 0.17968   -8.50769  39.09687  1.000 31.41221  ?  149 TRP   E CZ3 1 
ATOM   12795 C CH2 . TRP   I  1 149 ? 1.56826   -8.64753  38.97822  1.000 38.62957  ?  149 TRP   E CH2 1 
ATOM   12796 N N   . GLY   I  1 150 ? -2.81457  -14.73310 39.26982  1.000 32.38934  ?  150 GLY   E N   1 
ATOM   12797 C CA  . GLY   I  1 150 ? -2.40977  -15.51618 40.42217  1.000 21.74632  ?  150 GLY   E CA  1 
ATOM   12798 C C   . GLY   I  1 150 ? -2.27371  -16.99316 40.11703  1.000 43.03881  ?  150 GLY   E C   1 
ATOM   12799 O O   . GLY   I  1 150 ? -1.49290  -17.69800 40.77028  1.000 55.09251  ?  150 GLY   E O   1 
ATOM   12800 N N   . LEU   I  1 151 ? -3.03657  -17.48247 39.13480  1.000 29.85307  ?  151 LEU   E N   1 
ATOM   12801 C CA  . LEU   I  1 151 ? -2.85072  -18.84504 38.63880  1.000 24.57122  ?  151 LEU   E CA  1 
ATOM   12802 C C   . LEU   I  1 151 ? -1.42203  -19.08100 38.19254  1.000 64.01176  ?  151 LEU   E C   1 
ATOM   12803 O O   . LEU   I  1 151 ? -0.78376  -20.07125 38.57943  1.000 37.06963  ?  151 LEU   E O   1 
ATOM   12804 C CB  . LEU   I  1 151 ? -3.75607  -19.08944 37.45552  1.000 36.76662  ?  151 LEU   E CB  1 
ATOM   12805 C CG  . LEU   I  1 151 ? -5.20416  -19.23363 37.79907  1.000 57.86328  ?  151 LEU   E CG  1 
ATOM   12806 C CD1 . LEU   I  1 151 ? -5.82307  -19.58795 36.49343  1.000 23.03672  ?  151 LEU   E CD1 1 
ATOM   12807 C CD2 . LEU   I  1 151 ? -5.28558  -20.34379 38.80398  1.000 11.55963  ?  151 LEU   E CD2 1 
ATOM   12808 N N   . PHE   I  1 152 ? -0.93714  -18.21258 37.30308  1.000 32.53527  ?  152 PHE   E N   1 
ATOM   12809 C CA  . PHE   I  1 152 ? 0.44346   -18.30161 36.86540  1.000 45.28567  ?  152 PHE   E CA  1 
ATOM   12810 C C   . PHE   I  1 152 ? 1.40870   -18.22148 38.04329  1.000 58.51892  ?  152 PHE   E C   1 
ATOM   12811 O O   . PHE   I  1 152 ? 2.42267   -18.92607 38.06607  1.000 50.97402  ?  152 PHE   E O   1 
ATOM   12812 C CB  . PHE   I  1 152 ? 0.74214   -17.19851 35.85881  1.000 27.54905  ?  152 PHE   E CB  1 
ATOM   12813 C CG  . PHE   I  1 152 ? 2.17278   -17.12295 35.50144  1.000 53.80666  ?  152 PHE   E CG  1 
ATOM   12814 C CD1 . PHE   I  1 152 ? 2.72744   -18.06786 34.66496  1.000 36.75740  ?  152 PHE   E CD1 1 
ATOM   12815 C CD2 . PHE   I  1 152 ? 2.98507   -16.14623 36.05020  1.000 44.62456  ?  152 PHE   E CD2 1 
ATOM   12816 C CE1 . PHE   I  1 152 ? 4.06341   -18.02410 34.35592  1.000 43.75168  ?  152 PHE   E CE1 1 
ATOM   12817 C CE2 . PHE   I  1 152 ? 4.32186   -16.09070 35.74121  1.000 54.20312  ?  152 PHE   E CE2 1 
ATOM   12818 C CZ  . PHE   I  1 152 ? 4.86485   -17.02829 34.89116  1.000 45.95202  ?  152 PHE   E CZ  1 
ATOM   12819 N N   . LEU   I  1 153 ? 1.11380   -17.37690 39.03526  1.000 40.39783  ?  153 LEU   E N   1 
ATOM   12820 C CA  . LEU   I  1 153 ? 2.04410   -17.19366 40.14403  1.000 42.30481  ?  153 LEU   E CA  1 
ATOM   12821 C C   . LEU   I  1 153 ? 2.03069   -18.35766 41.13052  1.000 41.89016  ?  153 LEU   E C   1 
ATOM   12822 O O   . LEU   I  1 153 ? 2.82952   -18.36475 42.07322  1.000 46.28533  ?  153 LEU   E O   1 
ATOM   12823 C CB  . LEU   I  1 153 ? 1.73630   -15.88803 40.86261  1.000 35.02521  ?  153 LEU   E CB  1 
ATOM   12824 C CG  . LEU   I  1 153 ? 1.82607   -14.63011 40.00841  1.000 48.09314  ?  153 LEU   E CG  1 
ATOM   12825 C CD1 . LEU   I  1 153 ? 1.35363   -13.43835 40.82583  1.000 30.27122  ?  153 LEU   E CD1 1 
ATOM   12826 C CD2 . LEU   I  1 153 ? 3.24591   -14.41416 39.48816  1.000 30.28746  ?  153 LEU   E CD2 1 
ATOM   12827 N N   . SER   I  1 154 ? 1.14210   -19.32896 40.93235  1.000 34.57372  ?  154 SER   E N   1 
ATOM   12828 C CA  . SER   I  1 154 ? 1.10294   -20.56686 41.69441  1.000 32.32476  ?  154 SER   E CA  1 
ATOM   12829 C C   . SER   I  1 154 ? 1.75377   -21.72364 40.94752  1.000 42.40682  ?  154 SER   E C   1 
ATOM   12830 O O   . SER   I  1 154 ? 1.83787   -22.82806 41.49308  1.000 46.64818  ?  154 SER   E O   1 
ATOM   12831 C CB  . SER   I  1 154 ? -0.35039  -20.92428 42.02522  1.000 19.52151  ?  154 SER   E CB  1 
ATOM   12832 O OG  . SER   I  1 154 ? -0.89517  -19.94832 42.88688  1.000 100.15559 ?  154 SER   E OG  1 
ATOM   12833 N N   . SER   I  1 155 ? 2.21069   -21.49312 39.71856  1.000 36.63682  ?  155 SER   E N   1 
ATOM   12834 C CA  . SER   I  1 155 ? 2.68575   -22.52145 38.80609  1.000 37.26070  ?  155 SER   E CA  1 
ATOM   12835 C C   . SER   I  1 155 ? 4.20603   -22.60337 38.84141  1.000 101.86513 ?  155 SER   E C   1 
ATOM   12836 O O   . SER   I  1 155 ? 4.89225   -21.61692 39.14165  1.000 35.35027  ?  155 SER   E O   1 
ATOM   12837 C CB  . SER   I  1 155 ? 2.22374   -22.22187 37.37976  1.000 34.01334  ?  155 SER   E CB  1 
ATOM   12838 O OG  . SER   I  1 155 ? 2.90706   -21.10404 36.83036  1.000 44.06281  ?  155 SER   E OG  1 
ATOM   12839 N N   . LYS   I  1 156 ? 4.72908   -23.79537 38.50358  1.000 43.13887  ?  156 LYS   E N   1 
ATOM   12840 C CA  . LYS   I  1 156 ? 6.17534   -24.00601 38.55513  1.000 59.95710  ?  156 LYS   E CA  1 
ATOM   12841 C C   . LYS   I  1 156 ? 6.90998   -22.96866 37.70834  1.000 33.37802  ?  156 LYS   E C   1 
ATOM   12842 O O   . LYS   I  1 156 ? 8.02283   -22.55240 38.05779  1.000 49.22223  ?  156 LYS   E O   1 
ATOM   12843 C CB  . LYS   I  1 156 ? 6.52687   -25.43647 38.11502  1.000 26.09335  ?  156 LYS   E CB  1 
ATOM   12844 N N   . ASP   I  1 157 ? 6.26529   -22.47812 36.63965  1.000 53.53326  ?  157 ASP   E N   1 
ATOM   12845 C CA  . ASP   I  1 157 ? 6.90601   -21.53880 35.71652  1.000 52.50563  ?  157 ASP   E CA  1 
ATOM   12846 C C   . ASP   I  1 157 ? 7.19664   -20.18468 36.34814  1.000 55.02472  ?  157 ASP   E C   1 
ATOM   12847 O O   . ASP   I  1 157 ? 8.08232   -19.46697 35.86552  1.000 50.91059  ?  157 ASP   E O   1 
ATOM   12848 C CB  . ASP   I  1 157 ? 6.03804   -21.33869 34.47279  1.000 63.85715  ?  157 ASP   E CB  1 
ATOM   12849 C CG  . ASP   I  1 157 ? 5.96622   -22.58498 33.59848  1.000 64.89520  ?  157 ASP   E CG  1 
ATOM   12850 O OD1 . ASP   I  1 157 ? 7.03031   -23.15519 33.27580  1.000 75.49634  ?  157 ASP   E OD1 1 
ATOM   12851 O OD2 . ASP   I  1 157 ? 4.83844   -22.99377 33.23947  1.000 94.19936  -1 157 ASP   E OD2 1 
ATOM   12852 N N   . SER   I  1 158 ? 6.46816   -19.81074 37.40204  1.000 60.15581  ?  158 SER   E N   1 
ATOM   12853 C CA  . SER   I  1 158 ? 6.74046   -18.54005 38.05902  1.000 45.58487  ?  158 SER   E CA  1 
ATOM   12854 C C   . SER   I  1 158 ? 7.99447   -18.58425 38.92930  1.000 48.42980  ?  158 SER   E C   1 
ATOM   12855 O O   . SER   I  1 158 ? 8.35174   -17.54662 39.49888  1.000 43.48869  ?  158 SER   E O   1 
ATOM   12856 C CB  . SER   I  1 158 ? 5.53132   -18.10865 38.89810  1.000 39.04239  ?  158 SER   E CB  1 
ATOM   12857 O OG  . SER   I  1 158 ? 5.36152   -18.95438 40.02631  1.000 38.50090  ?  158 SER   E OG  1 
ATOM   12858 N N   . ARG   I  1 159 ? 8.67521   -19.73524 39.04301  1.000 40.47876  ?  159 ARG   E N   1 
ATOM   12859 C CA  . ARG   I  1 159 ? 9.90852   -19.79801 39.82902  1.000 47.69496  ?  159 ARG   E CA  1 
ATOM   12860 C C   . ARG   I  1 159 ? 11.06697  -19.04364 39.18491  1.000 48.45145  ?  159 ARG   E C   1 
ATOM   12861 O O   . ARG   I  1 159 ? 12.05034  -18.75157 39.86931  1.000 42.86929  ?  159 ARG   E O   1 
ATOM   12862 C CB  . ARG   I  1 159 ? 10.33445  -21.24697 40.05159  1.000 30.32747  ?  159 ARG   E CB  1 
ATOM   12863 C CG  . ARG   I  1 159 ? 9.46228   -21.99197 41.03502  1.000 66.29726  ?  159 ARG   E CG  1 
ATOM   12864 C CD  . ARG   I  1 159 ? 9.79880   -23.45516 40.98778  1.000 50.38051  ?  159 ARG   E CD  1 
ATOM   12865 N NE  . ARG   I  1 159 ? 9.74592   -23.93296 39.61491  1.000 64.24310  ?  159 ARG   E NE  1 
ATOM   12866 C CZ  . ARG   I  1 159 ? 10.27449  -25.07296 39.19606  1.000 55.41050  ?  159 ARG   E CZ  1 
ATOM   12867 N NH1 . ARG   I  1 159 ? 10.92356  -25.88016 40.02205  1.000 47.88233  ?  159 ARG   E NH1 1 
ATOM   12868 N NH2 . ARG   I  1 159 ? 10.15148  -25.40854 37.91642  1.000 45.10290  ?  159 ARG   E NH2 1 
ATOM   12869 N N   . ASN   I  1 160 ? 10.97235  -18.70174 37.89862  1.000 42.21756  ?  160 ASN   E N   1 
ATOM   12870 C CA  . ASN   I  1 160 ? 12.11940  -18.13774 37.19157  1.000 46.56301  ?  160 ASN   E CA  1 
ATOM   12871 C C   . ASN   I  1 160 ? 12.61371  -16.81423 37.77174  1.000 38.99065  ?  160 ASN   E C   1 
ATOM   12872 O O   . ASN   I  1 160 ? 13.72941  -16.39707 37.44943  1.000 68.76246  ?  160 ASN   E O   1 
ATOM   12873 C CB  . ASN   I  1 160 ? 11.77577  -17.95734 35.71722  1.000 44.61254  ?  160 ASN   E CB  1 
ATOM   12874 C CG  . ASN   I  1 160 ? 10.84805  -16.80419 35.48631  1.000 56.78703  ?  160 ASN   E CG  1 
ATOM   12875 O OD1 . ASN   I  1 160 ? 9.68278   -16.83685 35.89604  1.000 70.24300  ?  160 ASN   E OD1 1 
ATOM   12876 N ND2 . ASN   I  1 160 ? 11.35463  -15.76390 34.83863  1.000 60.98046  ?  160 ASN   E ND2 1 
ATOM   12877 N N   . VAL   I  1 161 ? 11.81957  -16.12883 38.59787  1.000 51.28951  ?  161 VAL   E N   1 
ATOM   12878 C CA  . VAL   I  1 161 ? 12.33035  -14.94146 39.28625  1.000 54.09451  ?  161 VAL   E CA  1 
ATOM   12879 C C   . VAL   I  1 161 ? 13.01321  -15.29064 40.59742  1.000 56.79452  ?  161 VAL   E C   1 
ATOM   12880 O O   . VAL   I  1 161 ? 13.59558  -14.40166 41.24150  1.000 39.49849  ?  161 VAL   E O   1 
ATOM   12881 C CB  . VAL   I  1 161 ? 11.21992  -13.91341 39.58625  1.000 48.04091  ?  161 VAL   E CB  1 
ATOM   12882 C CG1 . VAL   I  1 161 ? 10.61416  -13.35822 38.29090  1.000 36.90612  ?  161 VAL   E CG1 1 
ATOM   12883 C CG2 . VAL   I  1 161 ? 10.16551  -14.54390 40.47144  1.000 31.79828  ?  161 VAL   E CG2 1 
ATOM   12884 N N   . LEU   I  1 162 ? 12.94062  -16.54950 41.02465  1.000 36.66591  ?  162 LEU   E N   1 
ATOM   12885 C CA  . LEU   I  1 162 ? 13.55269  -16.99316 42.27296  1.000 47.11175  ?  162 LEU   E CA  1 
ATOM   12886 C C   . LEU   I  1 162 ? 15.00631  -17.38812 42.00150  1.000 66.04216  ?  162 LEU   E C   1 
ATOM   12887 O O   . LEU   I  1 162 ? 15.40746  -18.55608 42.04229  1.000 48.63845  ?  162 LEU   E O   1 
ATOM   12888 C CB  . LEU   I  1 162 ? 12.74914  -18.13930 42.86683  1.000 43.76858  ?  162 LEU   E CB  1 
ATOM   12889 C CG  . LEU   I  1 162 ? 11.29970  -17.77606 43.15932  1.000 32.40803  ?  162 LEU   E CG  1 
ATOM   12890 C CD1 . LEU   I  1 162 ? 10.61493  -18.89888 43.91871  1.000 28.10173  ?  162 LEU   E CD1 1 
ATOM   12891 C CD2 . LEU   I  1 162 ? 11.27345  -16.47116 43.95825  1.000 26.94471  ?  162 LEU   E CD2 1 
ATOM   12892 N N   . VAL   I  1 163 ? 15.79958  -16.36094 41.70479  1.000 46.52899  ?  163 VAL   E N   1 
ATOM   12893 C CA  . VAL   I  1 163 ? 17.17573  -16.49276 41.23852  1.000 43.57408  ?  163 VAL   E CA  1 
ATOM   12894 C C   . VAL   I  1 163 ? 17.96000  -15.29651 41.76523  1.000 63.99951  ?  163 VAL   E C   1 
ATOM   12895 O O   . VAL   I  1 163 ? 17.38984  -14.32233 42.26465  1.000 56.58220  ?  163 VAL   E O   1 
ATOM   12896 C CB  . VAL   I  1 163 ? 17.27403  -16.54428 39.69226  1.000 45.53468  ?  163 VAL   E CB  1 
ATOM   12897 C CG1 . VAL   I  1 163 ? 16.50459  -17.75298 39.11572  1.000 39.11890  ?  163 VAL   E CG1 1 
ATOM   12898 C CG2 . VAL   I  1 163 ? 16.77313  -15.23247 39.07963  1.000 38.64786  ?  163 VAL   E CG2 1 
ATOM   12899 N N   . ALA   I  1 164 ? 19.28564  -15.35315 41.63464  1.000 51.98981  ?  164 ALA   E N   1 
ATOM   12900 C CA  . ALA   I  1 164 ? 20.10259  -14.21531 42.04388  1.000 59.59580  ?  164 ALA   E CA  1 
ATOM   12901 C C   . ALA   I  1 164 ? 20.40643  -13.25725 40.90188  1.000 50.59610  ?  164 ALA   E C   1 
ATOM   12902 O O   . ALA   I  1 164 ? 20.84170  -12.12907 41.16592  1.000 48.51085  ?  164 ALA   E O   1 
ATOM   12903 C CB  . ALA   I  1 164 ? 21.41269  -14.69392 42.66277  1.000 30.45232  ?  164 ALA   E CB  1 
ATOM   12904 N N   . ASP   I  1 165 ? 20.16826  -13.68422 39.65338  1.000 46.52905  ?  165 ASP   E N   1 
ATOM   12905 C CA  . ASP   I  1 165 ? 20.44099  -12.89242 38.45738  1.000 44.86349  ?  165 ASP   E CA  1 
ATOM   12906 C C   . ASP   I  1 165 ? 20.00466  -11.44211 38.63093  1.000 44.72398  ?  165 ASP   E C   1 
ATOM   12907 O O   . ASP   I  1 165 ? 18.90471  -11.15579 39.10602  1.000 79.74600  ?  165 ASP   E O   1 
ATOM   12908 C CB  . ASP   I  1 165 ? 19.71921  -13.49917 37.24042  1.000 52.13949  ?  165 ASP   E CB  1 
ATOM   12909 C CG  . ASP   I  1 165 ? 19.91753  -15.00604 37.11056  1.000 40.09247  ?  165 ASP   E CG  1 
ATOM   12910 O OD1 . ASP   I  1 165 ? 20.67235  -15.60228 37.91127  1.000 86.34343  ?  165 ASP   E OD1 1 
ATOM   12911 O OD2 . ASP   I  1 165 ? 19.30391  -15.59275 36.18993  1.000 89.04153  -1 165 ASP   E OD2 1 
ATOM   12912 N N   . GLN   I  1 166 ? 20.88672  -10.52784 38.26025  1.000 68.55578  ?  166 GLN   E N   1 
ATOM   12913 C CA  . GLN   I  1 166 ? 20.51260  -9.13603  38.07934  1.000 83.02412  ?  166 GLN   E CA  1 
ATOM   12914 C C   . GLN   I  1 166 ? 19.89383  -9.01693  36.69113  1.000 45.28325  ?  166 GLN   E C   1 
ATOM   12915 O O   . GLN   I  1 166 ? 20.44039  -9.55192  35.72352  1.000 118.88478 ?  166 GLN   E O   1 
ATOM   12916 C CB  . GLN   I  1 166 ? 21.73640  -8.22761  38.24832  1.000 42.60969  ?  166 GLN   E CB  1 
ATOM   12917 C CG  . GLN   I  1 166 ? 21.49022  -6.75434  38.04665  1.000 79.12567  ?  166 GLN   E CG  1 
ATOM   12918 C CD  . GLN   I  1 166 ? 21.18518  -6.05750  39.34769  1.000 138.54500 ?  166 GLN   E CD  1 
ATOM   12919 O OE1 . GLN   I  1 166 ? 20.53404  -5.00663  39.36676  1.000 93.31009  ?  166 GLN   E OE1 1 
ATOM   12920 N NE2 . GLN   I  1 166 ? 21.65135  -6.63479  40.44887  1.000 79.71373  ?  166 GLN   E NE2 1 
ATOM   12921 N N   . PHE   I  1 167 ? 18.72937  -8.37084  36.60337  1.000 70.70497  ?  167 PHE   E N   1 
ATOM   12922 C CA  . PHE   I  1 167 ? 17.94914  -8.33019  35.36639  1.000 69.66289  ?  167 PHE   E CA  1 
ATOM   12923 C C   . PHE   I  1 167 ? 18.17395  -7.06892  34.54392  1.000 71.16671  ?  167 PHE   E C   1 
ATOM   12924 O O   . PHE   I  1 167 ? 18.01212  -7.10373  33.32062  1.000 67.14625  ?  167 PHE   E O   1 
ATOM   12925 C CB  . PHE   I  1 167 ? 16.44840  -8.42943  35.67188  1.000 59.76451  ?  167 PHE   E CB  1 
ATOM   12926 C CG  . PHE   I  1 167 ? 16.02004  -9.75136  36.24162  1.000 65.26057  ?  167 PHE   E CG  1 
ATOM   12927 C CD1 . PHE   I  1 167 ? 15.23520  -9.82122  37.37883  1.000 53.47487  ?  167 PHE   E CD1 1 
ATOM   12928 C CD2 . PHE   I  1 167 ? 16.37889  -10.91955 35.63045  1.000 44.58285  ?  167 PHE   E CD2 1 
ATOM   12929 C CE1 . PHE   I  1 167 ? 14.83581  -11.04560 37.89423  1.000 124.19828 ?  167 PHE   E CE1 1 
ATOM   12930 C CE2 . PHE   I  1 167 ? 15.98302  -12.14250 36.13979  1.000 113.01934 ?  167 PHE   E CE2 1 
ATOM   12931 C CZ  . PHE   I  1 167 ? 15.22243  -12.21131 37.26283  1.000 32.30050  ?  167 PHE   E CZ  1 
ATOM   12932 N N   . ASP   I  1 168 ? 18.48985  -5.95510  35.19247  1.000 93.80077  ?  168 ASP   E N   1 
ATOM   12933 C CA  . ASP   I  1 168 ? 18.81853  -4.69449  34.54225  1.000 59.07435  ?  168 ASP   E CA  1 
ATOM   12934 C C   . ASP   I  1 168 ? 19.43969  -3.79339  35.60259  1.000 110.38488 ?  168 ASP   E C   1 
ATOM   12935 O O   . ASP   I  1 168 ? 19.85188  -4.29312  36.68213  1.000 83.90941  ?  168 ASP   E O   1 
ATOM   12936 C CB  . ASP   I  1 168 ? 17.57974  -4.10299  33.82771  1.000 73.15391  ?  168 ASP   E CB  1 
ATOM   12937 C CG  . ASP   I  1 168 ? 16.50290  -3.57236  34.79273  1.000 97.94124  ?  168 ASP   E CG  1 
ATOM   12938 O OD1 . ASP   I  1 168 ? 15.29353  -3.63093  34.44711  1.000 83.77233  ?  168 ASP   E OD1 1 
ATOM   12939 O OD2 . ASP   I  1 168 ? 16.85823  -3.06551  35.88034  1.000 95.69691  -1 168 ASP   E OD2 1 
ATOM   12940 N N   . ASP   I  1 169 ? 19.54656  -2.49451  35.34659  1.000 76.34742  ?  169 ASP   E N   1 
ATOM   12941 C CA  . ASP   I  1 169 ? 20.24616  -1.62807  36.29102  1.000 80.23918  ?  169 ASP   E CA  1 
ATOM   12942 C C   . ASP   I  1 169 ? 19.49596  -1.52984  37.62098  1.000 97.08703  ?  169 ASP   E C   1 
ATOM   12943 O O   . ASP   I  1 169 ? 20.12375  -1.40977  38.68017  1.000 84.91583  ?  169 ASP   E O   1 
ATOM   12944 C CB  . ASP   I  1 169 ? 20.47138  -0.23876  35.67869  1.000 58.82215  ?  169 ASP   E CB  1 
ATOM   12945 N N   . ARG   I  1 170 ? 18.16173  -1.63367  37.60018  1.000 137.47335 ?  170 ARG   E N   1 
ATOM   12946 C CA  . ARG   I  1 170 ? 17.35397  -1.38022  38.78836  1.000 48.37346  ?  170 ARG   E CA  1 
ATOM   12947 C C   . ARG   I  1 170 ? 16.65599  -2.61538  39.37036  1.000 66.65720  ?  170 ARG   E C   1 
ATOM   12948 O O   . ARG   I  1 170 ? 16.17203  -2.54279  40.50587  1.000 57.67378  ?  170 ARG   E O   1 
ATOM   12949 C CB  . ARG   I  1 170 ? 16.30759  -0.29643  38.47837  1.000 54.22648  ?  170 ARG   E CB  1 
ATOM   12950 N N   . HIS   I  1 171 ? 16.60955  -3.74801  38.65303  1.000 64.78521  ?  171 HIS   E N   1 
ATOM   12951 C CA  . HIS   I  1 171 ? 15.83620  -4.92068  39.06144  1.000 68.01553  ?  171 HIS   E CA  1 
ATOM   12952 C C   . HIS   I  1 171 ? 16.72128  -6.15490  39.17940  1.000 34.56793  ?  171 HIS   E C   1 
ATOM   12953 O O   . HIS   I  1 171 ? 17.67648  -6.32937  38.42037  1.000 105.84665 ?  171 HIS   E O   1 
ATOM   12954 C CB  . HIS   I  1 171 ? 14.70233  -5.24394  38.06272  1.000 70.78478  ?  171 HIS   E CB  1 
ATOM   12955 C CG  . HIS   I  1 171 ? 13.80127  -4.08623  37.76563  1.000 65.96839  ?  171 HIS   E CG  1 
ATOM   12956 N ND1 . HIS   I  1 171 ? 13.63432  -3.02751  38.63293  1.000 71.63168  ?  171 HIS   E ND1 1 
ATOM   12957 C CD2 . HIS   I  1 171 ? 13.02980  -3.81326  36.68737  1.000 66.19584  ?  171 HIS   E CD2 1 
ATOM   12958 C CE1 . HIS   I  1 171 ? 12.79570  -2.15498  38.10551  1.000 46.38582  ?  171 HIS   E CE1 1 
ATOM   12959 N NE2 . HIS   I  1 171 ? 12.41214  -2.60896  36.92599  1.000 121.64900 ?  171 HIS   E NE2 1 
ATOM   12960 N N   . CYS   I  1 172 ? 16.36395  -7.03509  40.11482  1.000 67.32776  ?  172 CYS   E N   1 
ATOM   12961 C CA  . CYS   I  1 172 ? 17.07499  -8.29270  40.30021  1.000 36.65380  ?  172 CYS   E CA  1 
ATOM   12962 C C   . CYS   I  1 172 ? 16.10986  -9.37103  40.77343  1.000 37.71237  ?  172 CYS   E C   1 
ATOM   12963 O O   . CYS   I  1 172 ? 14.96531  -9.09481  41.14164  1.000 60.64194  ?  172 CYS   E O   1 
ATOM   12964 C CB  . CYS   I  1 172 ? 18.20838  -8.14963  41.31042  1.000 45.76931  ?  172 CYS   E CB  1 
ATOM   12965 S SG  . CYS   I  1 172 ? 17.62107  -7.71744  42.94560  1.000 53.74350  ?  172 CYS   E SG  1 
ATOM   12966 N N   . GLY   I  1 173 ? 16.60319  -10.61024 40.77814  1.000 50.03599  ?  173 GLY   E N   1 
ATOM   12967 C CA  . GLY   I  1 173 ? 15.83733  -11.73150 41.28214  1.000 34.68812  ?  173 GLY   E CA  1 
ATOM   12968 C C   . GLY   I  1 173 ? 15.74207  -11.72593 42.79993  1.000 49.25622  ?  173 GLY   E C   1 
ATOM   12969 O O   . GLY   I  1 173 ? 16.45996  -11.01046 43.50317  1.000 49.31187  ?  173 GLY   E O   1 
ATOM   12970 N N   . TRP   I  1 174 ? 14.83035  -12.56566 43.31264  1.000 26.30761  ?  174 TRP   E N   1 
ATOM   12971 C CA  . TRP   I  1 174 ? 14.49887  -12.55793 44.73312  1.000 51.88530  ?  174 TRP   E CA  1 
ATOM   12972 C C   . TRP   I  1 174 ? 15.54139  -13.26933 45.58626  1.000 60.46812  ?  174 TRP   E C   1 
ATOM   12973 O O   . TRP   I  1 174 ? 15.55047  -13.07931 46.80461  1.000 44.64936  ?  174 TRP   E O   1 
ATOM   12974 C CB  . TRP   I  1 174 ? 13.11090  -13.17873 44.95077  1.000 29.63966  ?  174 TRP   E CB  1 
ATOM   12975 C CG  . TRP   I  1 174 ? 12.02994  -12.29556 44.41960  1.000 59.68979  ?  174 TRP   E CG  1 
ATOM   12976 C CD1 . TRP   I  1 174 ? 11.36796  -12.43342 43.23351  1.000 37.64100  ?  174 TRP   E CD1 1 
ATOM   12977 C CD2 . TRP   I  1 174 ? 11.51158  -11.10747 45.03577  1.000 46.35357  ?  174 TRP   E CD2 1 
ATOM   12978 N NE1 . TRP   I  1 174 ? 10.46262  -11.41288 43.07723  1.000 40.12169  ?  174 TRP   E NE1 1 
ATOM   12979 C CE2 . TRP   I  1 174 ? 10.52704  -10.58562 44.16854  1.000 32.18108  ?  174 TRP   E CE2 1 
ATOM   12980 C CE3 . TRP   I  1 174 ? 11.77332  -10.44442 46.24318  1.000 34.39888  ?  174 TRP   E CE3 1 
ATOM   12981 C CZ2 . TRP   I  1 174 ? 9.80046   -9.42495  44.46691  1.000 24.59245  ?  174 TRP   E CZ2 1 
ATOM   12982 C CZ3 . TRP   I  1 174 ? 11.06310  -9.28937  46.53373  1.000 36.43420  ?  174 TRP   E CZ3 1 
ATOM   12983 C CH2 . TRP   I  1 174 ? 10.08259  -8.79234  45.64610  1.000 27.58676  ?  174 TRP   E CH2 1 
ATOM   12984 N N   . LEU   I  1 175 ? 16.42643  -14.06095 44.98098  1.000 49.23559  ?  175 LEU   E N   1 
ATOM   12985 C CA  . LEU   I  1 175 ? 17.51566  -14.71711 45.69430  1.000 44.18916  ?  175 LEU   E CA  1 
ATOM   12986 C C   . LEU   I  1 175 ? 18.84351  -13.97161 45.56514  1.000 53.88612  ?  175 LEU   E C   1 
ATOM   12987 O O   . LEU   I  1 175 ? 19.84986  -14.41840 46.12257  1.000 62.73535  ?  175 LEU   E O   1 
ATOM   12988 C CB  . LEU   I  1 175 ? 17.65816  -16.15653 45.20119  1.000 39.18599  ?  175 LEU   E CB  1 
ATOM   12989 C CG  . LEU   I  1 175 ? 16.35644  -16.94382 45.38078  1.000 49.79748  ?  175 LEU   E CG  1 
ATOM   12990 C CD1 . LEU   I  1 175 ? 16.50528  -18.42928 45.03851  1.000 40.34350  ?  175 LEU   E CD1 1 
ATOM   12991 C CD2 . LEU   I  1 175 ? 15.85047  -16.75950 46.80523  1.000 37.28861  ?  175 LEU   E CD2 1 
ATOM   12992 N N   . ASN   I  1 176 ? 18.86286  -12.85917 44.83017  1.000 43.37021  ?  176 ASN   E N   1 
ATOM   12993 C CA  . ASN   I  1 176 ? 19.98335  -11.92617 44.83425  1.000 38.95995  ?  176 ASN   E CA  1 
ATOM   12994 C C   . ASN   I  1 176 ? 20.20872  -11.38358 46.24378  1.000 55.36893  ?  176 ASN   E C   1 
ATOM   12995 O O   . ASN   I  1 176 ? 19.25734  -11.20267 47.01054  1.000 69.25385  ?  176 ASN   E O   1 
ATOM   12996 C CB  . ASN   I  1 176 ? 19.65909  -10.79678 43.86531  1.000 65.88269  ?  176 ASN   E CB  1 
ATOM   12997 C CG  . ASN   I  1 176 ? 20.80589  -9.87114  43.63526  1.000 64.19387  ?  176 ASN   E CG  1 
ATOM   12998 O OD1 . ASN   I  1 176 ? 21.02638  -8.92278  44.39929  1.000 50.38056  ?  176 ASN   E OD1 1 
ATOM   12999 N ND2 . ASN   I  1 176 ? 21.51678  -10.09496 42.53626  1.000 51.72191  ?  176 ASN   E ND2 1 
ATOM   13000 N N   . GLU   I  1 177 ? 21.47436  -11.13083 46.59960  1.000 47.97925  ?  177 GLU   E N   1 
ATOM   13001 C CA  . GLU   I  1 177 ? 21.75209  -10.77115 47.98828  1.000 45.27807  ?  177 GLU   E CA  1 
ATOM   13002 C C   . GLU   I  1 177 ? 21.18039  -9.40345  48.33808  1.000 39.04849  ?  177 GLU   E C   1 
ATOM   13003 O O   . GLU   I  1 177 ? 20.84314  -9.15483  49.49850  1.000 48.29572  ?  177 GLU   E O   1 
ATOM   13004 C CB  . GLU   I  1 177 ? 23.25404  -10.81545 48.28293  1.000 27.03025  ?  177 GLU   E CB  1 
ATOM   13005 C CG  . GLU   I  1 177 ? 23.70948  -12.33575 48.64411  1.000 51.75603  ?  177 GLU   E CG  1 
ATOM   13006 C CD  . GLU   I  1 177 ? 23.20970  -12.93043 50.05925  1.000 94.16210  ?  177 GLU   E CD  1 
ATOM   13007 O OE1 . GLU   I  1 177 ? 22.82806  -12.16462 50.99489  1.000 96.30432  ?  177 GLU   E OE1 1 
ATOM   13008 O OE2 . GLU   I  1 177 ? 23.20628  -14.18842 50.25893  1.000 30.67510  ?  177 GLU   E OE2 1 
ATOM   13009 N N   . ARG   I  1 178 ? 21.04642  -8.50656  47.36013  1.000 37.11370  ?  178 ARG   E N   1 
ATOM   13010 C CA  . ARG   I  1 178 ? 20.38667  -7.22791  47.62325  1.000 60.67628  ?  178 ARG   E CA  1 
ATOM   13011 C C   . ARG   I  1 178 ? 18.97899  -7.45014  48.17604  1.000 56.85229  ?  178 ARG   E C   1 
ATOM   13012 O O   . ARG   I  1 178 ? 18.57215  -6.81557  49.15900  1.000 55.31201  ?  178 ARG   E O   1 
ATOM   13013 C CB  . ARG   I  1 178 ? 20.34764  -6.38985  46.33546  1.000 25.86019  ?  178 ARG   E CB  1 
ATOM   13014 N N   . ALA   I  1 179 ? 18.23436  -8.38222  47.56942  1.000 48.84167  ?  179 ALA   E N   1 
ATOM   13015 C CA  . ALA   I  1 179 ? 16.86138  -8.64809  47.97512  1.000 47.50743  ?  179 ALA   E CA  1 
ATOM   13016 C C   . ALA   I  1 179 ? 16.82129  -9.50105  49.23748  1.000 36.32183  ?  179 ALA   E C   1 
ATOM   13017 O O   . ALA   I  1 179 ? 16.02846  -9.24298  50.15403  1.000 43.96716  ?  179 ALA   E O   1 
ATOM   13018 C CB  . ALA   I  1 179 ? 16.11564  -9.33828  46.83141  1.000 23.34669  ?  179 ALA   E CB  1 
ATOM   13019 N N   . LEU   I  1 180 ? 17.65799  -10.54380 49.27832  1.000 43.28209  ?  180 LEU   E N   1 
ATOM   13020 C CA  . LEU   I  1 180 ? 17.81762  -11.35796 50.48123  1.000 30.23741  ?  180 LEU   E CA  1 
ATOM   13021 C C   . LEU   I  1 180 ? 18.12141  -10.49087 51.70209  1.000 46.61568  ?  180 LEU   E C   1 
ATOM   13022 O O   . LEU   I  1 180 ? 17.56978  -10.71055 52.78987  1.000 46.73578  ?  180 LEU   E O   1 
ATOM   13023 C CB  . LEU   I  1 180 ? 18.93000  -12.37999 50.24875  1.000 25.57194  ?  180 LEU   E CB  1 
ATOM   13024 C CG  . LEU   I  1 180 ? 18.55096  -13.84558 50.07550  1.000 50.38880  ?  180 LEU   E CG  1 
ATOM   13025 C CD1 . LEU   I  1 180 ? 17.36180  -14.00303 49.19293  1.000 48.01995  ?  180 LEU   E CD1 1 
ATOM   13026 C CD2 . LEU   I  1 180 ? 19.70970  -14.62020 49.50161  1.000 38.06364  ?  180 LEU   E CD2 1 
ATOM   13027 N N   . SER   I  1 181 ? 18.98863  -9.48853  51.53543  1.000 46.94495  ?  181 SER   E N   1 
ATOM   13028 C CA  . SER   I  1 181 ? 19.30664  -8.59316  52.64192  1.000 50.85634  ?  181 SER   E CA  1 
ATOM   13029 C C   . SER   I  1 181 ? 18.08222  -7.78439  53.06900  1.000 38.55508  ?  181 SER   E C   1 
ATOM   13030 O O   . SER   I  1 181 ? 17.77377  -7.69504  54.26559  1.000 49.86815  ?  181 SER   E O   1 
ATOM   13031 C CB  . SER   I  1 181 ? 20.46884  -7.67787  52.24506  1.000 33.23607  ?  181 SER   E CB  1 
ATOM   13032 O OG  . SER   I  1 181 ? 20.56545  -6.55465  53.10900  1.000 101.45676 ?  181 SER   E OG  1 
ATOM   13033 N N   . ALA   I  1 182 ? 17.36919  -7.19071  52.09943  1.000 44.45229  ?  182 ALA   E N   1 
ATOM   13034 C CA  . ALA   I  1 182 ? 16.20700  -6.36226  52.41935  1.000 66.12112  ?  182 ALA   E CA  1 
ATOM   13035 C C   . ALA   I  1 182 ? 15.16757  -7.14224  53.21488  1.000 45.63036  ?  182 ALA   E C   1 
ATOM   13036 O O   . ALA   I  1 182 ? 14.60078  -6.62205  54.18522  1.000 33.45698  ?  182 ALA   E O   1 
ATOM   13037 C CB  . ALA   I  1 182 ? 15.59246  -5.79794  51.13491  1.000 24.64598  ?  182 ALA   E CB  1 
ATOM   13038 N N   . MET   I  1 183 ? 14.93814  -8.40711  52.84212  1.000 29.56194  ?  183 MET   E N   1 
ATOM   13039 C CA  . MET   I  1 183 ? 13.90390  -9.23114  53.45410  1.000 45.68874  ?  183 MET   E CA  1 
ATOM   13040 C C   . MET   I  1 183 ? 14.20721  -9.68018  54.88298  1.000 31.02899  ?  183 MET   E C   1 
ATOM   13041 O O   . MET   I  1 183 ? 13.28401  -10.14327 55.56493  1.000 49.62380  ?  183 MET   E O   1 
ATOM   13042 C CB  . MET   I  1 183 ? 13.64208  -10.44295 52.56974  1.000 30.34857  ?  183 MET   E CB  1 
ATOM   13043 C CG  . MET   I  1 183 ? 12.71715  -10.09882 51.41474  1.000 32.45002  ?  183 MET   E CG  1 
ATOM   13044 S SD  . MET   I  1 183 ? 12.29089  -11.50394 50.39144  1.000 41.66042  ?  183 MET   E SD  1 
ATOM   13045 C CE  . MET   I  1 183 ? 13.72570  -11.74487 49.35806  1.000 37.91412  ?  183 MET   E CE  1 
ATOM   13046 N N   . VAL   I  1 184 ? 15.44390  -9.55980  55.36714  1.000 46.68075  ?  184 VAL   E N   1 
ATOM   13047 C CA  . VAL   I  1 184 ? 15.73588  -9.90848  56.75243  1.000 53.53893  ?  184 VAL   E CA  1 
ATOM   13048 C C   . VAL   I  1 184 ? 16.19100  -8.70643  57.56085  1.000 35.08261  ?  184 VAL   E C   1 
ATOM   13049 O O   . VAL   I  1 184 ? 16.70775  -8.87015  58.66254  1.000 46.00603  ?  184 VAL   E O   1 
ATOM   13050 C CB  . VAL   I  1 184 ? 16.76319  -11.05086 56.85650  1.000 32.95147  ?  184 VAL   E CB  1 
ATOM   13051 C CG1 . VAL   I  1 184 ? 16.19706  -12.31461 56.22684  1.000 38.46308  ?  184 VAL   E CG1 1 
ATOM   13052 C CG2 . VAL   I  1 184 ? 18.08293  -10.64774 56.21891  1.000 34.06165  ?  184 VAL   E CG2 1 
ATOM   13053 N N   . LYS   I  1 185 ? 15.97683  -7.50066  57.03711  1.000 39.39831  ?  185 LYS   E N   1 
ATOM   13054 C CA  . LYS   I  1 185 ? 16.33139  -6.27060  57.73699  1.000 42.27391  ?  185 LYS   E CA  1 
ATOM   13055 C C   . LYS   I  1 185 ? 15.92486  -6.28445  59.21507  1.000 17.99530  ?  185 LYS   E C   1 
ATOM   13056 O O   . LYS   I  1 185 ? 16.70298  -5.87494  60.08761  1.000 76.42346  ?  185 LYS   E O   1 
ATOM   13057 C CB  . LYS   I  1 185 ? 15.68816  -5.10407  56.99002  1.000 30.89331  ?  185 LYS   E CB  1 
ATOM   13058 C CG  . LYS   I  1 185 ? 15.79186  -3.77787  57.66753  1.000 37.09745  ?  185 LYS   E CG  1 
ATOM   13059 C CD  . LYS   I  1 185 ? 15.37193  -2.68243  56.70114  1.000 62.53415  ?  185 LYS   E CD  1 
ATOM   13060 C CE  . LYS   I  1 185 ? 15.86915  -1.34462  57.19381  1.000 63.17860  ?  185 LYS   E CE  1 
ATOM   13061 N NZ  . LYS   I  1 185 ? 14.78219  -0.33764  57.20331  1.000 76.90365  ?  185 LYS   E NZ  1 
ATOM   13062 N N   . HIS   I  1 186 ? 14.72016  -6.76965  59.52210  1.000 43.69345  ?  186 HIS   E N   1 
ATOM   13063 C CA  . HIS   I  1 186 ? 14.19123  -6.71508  60.88083  1.000 25.78266  ?  186 HIS   E CA  1 
ATOM   13064 C C   . HIS   I  1 186 ? 14.33562  -8.03250  61.63240  1.000 45.02113  ?  186 HIS   E C   1 
ATOM   13065 O O   . HIS   I  1 186 ? 13.62901  -8.26139  62.62104  1.000 31.17465  ?  186 HIS   E O   1 
ATOM   13066 C CB  . HIS   I  1 186 ? 12.72880  -6.27494  60.86681  1.000 34.22878  ?  186 HIS   E CB  1 
ATOM   13067 C CG  . HIS   I  1 186 ? 12.52165  -4.93599  60.24599  1.000 60.27236  ?  186 HIS   E CG  1 
ATOM   13068 N ND1 . HIS   I  1 186 ? 13.04645  -3.77823  60.78096  1.000 47.25033  ?  186 HIS   E ND1 1 
ATOM   13069 C CD2 . HIS   I  1 186 ? 11.85019  -4.56831  59.13132  1.000 19.91076  ?  186 HIS   E CD2 1 
ATOM   13070 C CE1 . HIS   I  1 186 ? 12.69976  -2.75285  60.02167  1.000 35.02959  ?  186 HIS   E CE1 1 
ATOM   13071 N NE2 . HIS   I  1 186 ? 11.97329  -3.20457  59.01507  1.000 51.08513  ?  186 HIS   E NE2 1 
ATOM   13072 N N   . TYR   I  1 187 ? 15.23830  -8.90299  61.20029  1.000 33.66524  ?  187 TYR   E N   1 
ATOM   13073 C CA  . TYR   I  1 187 ? 15.40475  -10.18114 61.87389  1.000 41.62462  ?  187 TYR   E CA  1 
ATOM   13074 C C   . TYR   I  1 187 ? 16.72670  -10.25947 62.61437  1.000 77.51206  ?  187 TYR   E C   1 
ATOM   13075 O O   . TYR   I  1 187 ? 17.17857  -11.35487 62.96813  1.000 35.06348  ?  187 TYR   E O   1 
ATOM   13076 C CB  . TYR   I  1 187 ? 15.23354  -11.33046 60.88522  1.000 46.13545  ?  187 TYR   E CB  1 
ATOM   13077 C CG  . TYR   I  1 187 ? 13.78974  -11.43009 60.47843  1.000 30.14276  ?  187 TYR   E CG  1 
ATOM   13078 C CD1 . TYR   I  1 187 ? 12.88483  -12.17159 61.23119  1.000 38.56737  ?  187 TYR   E CD1 1 
ATOM   13079 C CD2 . TYR   I  1 187 ? 13.31149  -10.71794 59.38501  1.000 44.86928  ?  187 TYR   E CD2 1 
ATOM   13080 C CE1 . TYR   I  1 187 ? 11.54341  -12.24827 60.87946  1.000 34.48028  ?  187 TYR   E CE1 1 
ATOM   13081 C CE2 . TYR   I  1 187 ? 11.98291  -10.77541 59.02232  1.000 17.02620  ?  187 TYR   E CE2 1 
ATOM   13082 C CZ  . TYR   I  1 187 ? 11.10315  -11.54960 59.77163  1.000 44.40592  ?  187 TYR   E CZ  1 
ATOM   13083 O OH  . TYR   I  1 187 ? 9.78898   -11.61123 59.39761  1.000 37.79821  ?  187 TYR   E OH  1 
ATOM   13084 N N   . ASN   I  1 188 ? 17.34443  -9.10764  62.86859  1.000 39.58739  ?  188 ASN   E N   1 
ATOM   13085 C CA  . ASN   I  1 188 ? 18.36015  -9.00001  63.89686  1.000 89.29627  ?  188 ASN   E CA  1 
ATOM   13086 C C   . ASN   I  1 188 ? 19.58950  -9.84166  63.54516  1.000 38.55618  ?  188 ASN   E C   1 
ATOM   13087 O O   . ASN   I  1 188 ? 20.04610  -10.67700 64.32413  1.000 72.03952  ?  188 ASN   E O   1 
ATOM   13088 C CB  . ASN   I  1 188 ? 17.74779  -9.40737  65.23663  1.000 50.03767  ?  188 ASN   E CB  1 
ATOM   13089 C CG  . ASN   I  1 188 ? 18.64030  -9.11094  66.40085  1.000 89.34438  ?  188 ASN   E CG  1 
ATOM   13090 O OD1 . ASN   I  1 188 ? 19.47949  -9.92197  66.77840  1.000 117.19384 ?  188 ASN   E OD1 1 
ATOM   13091 N ND2 . ASN   I  1 188 ? 18.46083  -7.94686  66.98765  1.000 102.18497 ?  188 ASN   E ND2 1 
ATOM   13092 N N   . GLY   I  1 189 ? 20.10111  -9.65337  62.32968  1.000 69.74690  ?  189 GLY   E N   1 
ATOM   13093 C CA  . GLY   I  1 189 ? 21.30036  -10.34300 61.90284  1.000 36.66368  ?  189 GLY   E CA  1 
ATOM   13094 C C   . GLY   I  1 189 ? 21.12514  -11.75936 61.37904  1.000 40.82894  ?  189 GLY   E C   1 
ATOM   13095 O O   . GLY   I  1 189 ? 22.02469  -12.25805 60.68848  1.000 73.72521  ?  189 GLY   E O   1 
ATOM   13096 N N   . ARG   I  1 190 ? 20.01074  -12.43420 61.67870  1.000 46.82154  ?  190 ARG   E N   1 
ATOM   13097 C CA  . ARG   I  1 190 ? 19.75457  -13.73997 61.07666  1.000 34.98308  ?  190 ARG   E CA  1 
ATOM   13098 C C   . ARG   I  1 190 ? 19.54288  -13.62522 59.55949  1.000 42.09843  ?  190 ARG   E C   1 
ATOM   13099 O O   . ARG   I  1 190 ? 19.06063  -12.61141 59.03345  1.000 52.78501  ?  190 ARG   E O   1 
ATOM   13100 C CB  . ARG   I  1 190 ? 18.54371  -14.40730 61.72605  1.000 42.19290  ?  190 ARG   E CB  1 
ATOM   13101 C CG  . ARG   I  1 190 ? 18.57786  -14.44952 63.23987  1.000 36.84906  ?  190 ARG   E CG  1 
ATOM   13102 C CD  . ARG   I  1 190 ? 18.74834  -15.87643 63.75254  1.000 27.35506  ?  190 ARG   E CD  1 
ATOM   13103 N NE  . ARG   I  1 190 ? 17.58604  -16.72682 63.51207  1.000 42.01168  ?  190 ARG   E NE  1 
ATOM   13104 C CZ  . ARG   I  1 190 ? 17.64155  -18.04848 63.42270  1.000 58.99196  ?  190 ARG   E CZ  1 
ATOM   13105 N NH1 . ARG   I  1 190 ? 18.79093  -18.69700 63.50566  1.000 55.24862  ?  190 ARG   E NH1 1 
ATOM   13106 N NH2 . ARG   I  1 190 ? 16.51939  -18.73663 63.23487  1.000 44.64621  ?  190 ARG   E NH2 1 
ATOM   13107 N N   . ALA   I  1 191 ? 19.91243  -14.68701 58.85826  1.000 41.21059  ?  191 ALA   E N   1 
ATOM   13108 C CA  . ALA   I  1 191 ? 19.89912  -14.71185 57.40481  1.000 29.00589  ?  191 ALA   E CA  1 
ATOM   13109 C C   . ALA   I  1 191 ? 18.59981  -15.32139 56.88858  1.000 92.04314  ?  191 ALA   E C   1 
ATOM   13110 O O   . ALA   I  1 191 ? 17.87708  -16.01223 57.61631  1.000 30.26113  ?  191 ALA   E O   1 
ATOM   13111 C CB  . ALA   I  1 191 ? 21.08577  -15.51651 56.87107  1.000 41.32245  ?  191 ALA   E CB  1 
ATOM   13112 N N   . PHE   I  1 192 ? 18.33953  -15.09288 55.59551  1.000 26.83571  ?  192 PHE   E N   1 
ATOM   13113 C CA  . PHE   I  1 192 ? 17.06349  -15.47617 54.99431  1.000 30.70844  ?  192 PHE   E CA  1 
ATOM   13114 C C   . PHE   I  1 192 ? 16.73151  -16.94923 55.23414  1.000 54.55468  ?  192 PHE   E C   1 
ATOM   13115 O O   . PHE   I  1 192 ? 15.61044  -17.28666 55.64202  1.000 44.14443  ?  192 PHE   E O   1 
ATOM   13116 C CB  . PHE   I  1 192 ? 17.08633  -15.15017 53.49855  1.000 32.24676  ?  192 PHE   E CB  1 
ATOM   13117 C CG  . PHE   I  1 192 ? 15.78046  -15.40699 52.79710  1.000 39.70697  ?  192 PHE   E CG  1 
ATOM   13118 C CD1 . PHE   I  1 192 ? 15.42550  -16.69141 52.40195  1.000 48.85329  ?  192 PHE   E CD1 1 
ATOM   13119 C CD2 . PHE   I  1 192 ? 14.90852  -14.36292 52.52520  1.000 47.80229  ?  192 PHE   E CD2 1 
ATOM   13120 C CE1 . PHE   I  1 192 ? 14.22588  -16.93692 51.75809  1.000 29.44602  ?  192 PHE   E CE1 1 
ATOM   13121 C CE2 . PHE   I  1 192 ? 13.70153  -14.59934 51.87598  1.000 53.90416  ?  192 PHE   E CE2 1 
ATOM   13122 C CZ  . PHE   I  1 192 ? 13.36582  -15.89071 51.48917  1.000 37.34824  ?  192 PHE   E CZ  1 
ATOM   13123 N N   . ASP   I  1 193 ? 17.69173  -17.84221 54.97942  1.000 56.20472  ?  193 ASP   E N   1 
ATOM   13124 C CA  . ASP   I  1 193 ? 17.45385  -19.27942 55.10426  1.000 36.30188  ?  193 ASP   E CA  1 
ATOM   13125 C C   . ASP   I  1 193 ? 17.41390  -19.75992 56.55685  1.000 62.79529  ?  193 ASP   E C   1 
ATOM   13126 O O   . ASP   I  1 193 ? 16.93726  -20.87179 56.82027  1.000 23.68198  ?  193 ASP   E O   1 
ATOM   13127 C CB  . ASP   I  1 193 ? 18.51910  -20.04575 54.31509  1.000 49.19235  ?  193 ASP   E CB  1 
ATOM   13128 C CG  . ASP   I  1 193 ? 19.92001  -19.77794 54.82619  1.000 92.07363  ?  193 ASP   E CG  1 
ATOM   13129 O OD1 . ASP   I  1 193 ? 20.41035  -18.63993 54.66512  1.000 52.79022  ?  193 ASP   E OD1 1 
ATOM   13130 O OD2 . ASP   I  1 193 ? 20.51234  -20.70152 55.42444  1.000 51.28821  -1 193 ASP   E OD2 1 
ATOM   13131 N N   . GLU   I  1 194 ? 17.89815  -18.95873 57.50543  1.000 25.82443  ?  194 GLU   E N   1 
ATOM   13132 C CA  . GLU   I  1 194 ? 17.64022  -19.23329 58.91606  1.000 52.79561  ?  194 GLU   E CA  1 
ATOM   13133 C C   . GLU   I  1 194 ? 16.21429  -18.85027 59.29450  1.000 57.17257  ?  194 GLU   E C   1 
ATOM   13134 O O   . GLU   I  1 194 ? 15.50273  -19.63673 59.93328  1.000 45.66621  ?  194 GLU   E O   1 
ATOM   13135 C CB  . GLU   I  1 194 ? 18.62854  -18.46791 59.79266  1.000 44.55842  ?  194 GLU   E CB  1 
ATOM   13136 C CG  . GLU   I  1 194 ? 20.09897  -18.77747 59.52122  1.000 30.33517  ?  194 GLU   E CG  1 
ATOM   13137 C CD  . GLU   I  1 194 ? 21.02898  -17.94073 60.39509  1.000 87.90925  ?  194 GLU   E CD  1 
ATOM   13138 O OE1 . GLU   I  1 194 ? 21.15456  -16.72787 60.11863  1.000 62.52016  ?  194 GLU   E OE1 1 
ATOM   13139 O OE2 . GLU   I  1 194 ? 21.61117  -18.48107 61.36790  1.000 60.07267  -1 194 GLU   E OE2 1 
ATOM   13140 N N   . VAL   I  1 195 ? 15.78713  -17.64565 58.88197  1.000 52.70535  ?  195 VAL   E N   1 
ATOM   13141 C CA  . VAL   I  1 195 ? 14.48824  -17.09440 59.27153  1.000 20.50528  ?  195 VAL   E CA  1 
ATOM   13142 C C   . VAL   I  1 195 ? 13.34069  -17.86302 58.61497  1.000 81.93128  ?  195 VAL   E C   1 
ATOM   13143 O O   . VAL   I  1 195 ? 12.38403  -18.27842 59.28062  1.000 33.72078  ?  195 VAL   E O   1 
ATOM   13144 C CB  . VAL   I  1 195 ? 14.42557  -15.60069 58.91461  1.000 55.74059  ?  195 VAL   E CB  1 
ATOM   13145 C CG1 . VAL   I  1 195 ? 13.03948  -15.04187 59.21175  1.000 25.41175  ?  195 VAL   E CG1 1 
ATOM   13146 C CG2 . VAL   I  1 195 ? 15.51116  -14.82573 59.65411  1.000 30.40867  ?  195 VAL   E CG2 1 
ATOM   13147 N N   . PHE   I  1 196 ? 13.39905  -18.04244 57.30301  1.000 28.36442  ?  196 PHE   E N   1 
ATOM   13148 C CA  . PHE   I  1 196 ? 12.29901  -18.64590 56.57341  1.000 60.28468  ?  196 PHE   E CA  1 
ATOM   13149 C C   . PHE   I  1 196 ? 12.63629  -20.08510 56.20278  1.000 40.77924  ?  196 PHE   E C   1 
ATOM   13150 O O   . PHE   I  1 196 ? 13.80094  -20.43704 56.00996  1.000 43.04014  ?  196 PHE   E O   1 
ATOM   13151 C CB  . PHE   I  1 196 ? 11.97772  -17.82637 55.32040  1.000 33.02656  ?  196 PHE   E CB  1 
ATOM   13152 C CG  . PHE   I  1 196 ? 11.69208  -16.38998 55.60864  1.000 50.48265  ?  196 PHE   E CG  1 
ATOM   13153 C CD1 . PHE   I  1 196 ? 10.56238  -16.02707 56.32729  1.000 34.18721  ?  196 PHE   E CD1 1 
ATOM   13154 C CD2 . PHE   I  1 196 ? 12.56024  -15.39898 55.18595  1.000 27.60055  ?  196 PHE   E CD2 1 
ATOM   13155 C CE1 . PHE   I  1 196 ? 10.30264  -14.68719 56.61308  1.000 38.20289  ?  196 PHE   E CE1 1 
ATOM   13156 C CE2 . PHE   I  1 196 ? 12.30299  -14.05520 55.45970  1.000 45.78557  ?  196 PHE   E CE2 1 
ATOM   13157 C CZ  . PHE   I  1 196 ? 11.17179  -13.69803 56.17081  1.000 37.17395  ?  196 PHE   E CZ  1 
ATOM   13158 N N   . LEU   I  1 197 ? 11.59765  -20.91362 56.10941  1.000 36.47048  ?  197 LEU   E N   1 
ATOM   13159 C CA  . LEU   I  1 197 ? 11.72988  -22.33245 55.78269  1.000 39.29693  ?  197 LEU   E CA  1 
ATOM   13160 C C   . LEU   I  1 197 ? 11.99011  -22.48083 54.28993  1.000 57.89077  ?  197 LEU   E C   1 
ATOM   13161 O O   . LEU   I  1 197 ? 11.08826  -22.28608 53.46988  1.000 33.28979  ?  197 LEU   E O   1 
ATOM   13162 C CB  . LEU   I  1 197 ? 10.45895  -23.07301 56.17958  1.000 36.82995  ?  197 LEU   E CB  1 
ATOM   13163 C CG  . LEU   I  1 197 ? 10.39465  -24.58827 56.30666  1.000 33.52603  ?  197 LEU   E CG  1 
ATOM   13164 C CD1 . LEU   I  1 197 ? 9.05665   -24.86876 56.91619  1.000 41.77091  ?  197 LEU   E CD1 1 
ATOM   13165 C CD2 . LEU   I  1 197 ? 10.47558  -25.29634 54.97713  1.000 80.72669  ?  197 LEU   E CD2 1 
ATOM   13166 N N   . CYS   I  1 198 ? 13.20771  -22.85603 53.93086  1.000 43.91729  ?  198 CYS   E N   1 
ATOM   13167 C CA  . CYS   I  1 198 ? 13.54887  -23.05823 52.53816  1.000 43.09132  ?  198 CYS   E CA  1 
ATOM   13168 C C   . CYS   I  1 198 ? 14.72824  -24.01646 52.49110  1.000 46.72211  ?  198 CYS   E C   1 
ATOM   13169 O O   . CYS   I  1 198 ? 15.09987  -24.62010 53.50333  1.000 53.81900  ?  198 CYS   E O   1 
ATOM   13170 C CB  . CYS   I  1 198 ? 13.86627  -21.71793 51.86768  1.000 36.54548  ?  198 CYS   E CB  1 
ATOM   13171 S SG  . CYS   I  1 198 ? 15.16566  -20.78329 52.75817  1.000 45.28170  ?  198 CYS   E SG  1 
ATOM   13172 N N   . ASP   I  1 199 ? 15.32865  -24.13610 51.30981  1.000 55.92013  ?  199 ASP   E N   1 
ATOM   13173 C CA  . ASP   I  1 199 ? 16.53609  -24.92702 51.09302  1.000 44.39434  ?  199 ASP   E CA  1 
ATOM   13174 C C   . ASP   I  1 199 ? 17.52642  -24.06141 50.31720  1.000 79.01057  ?  199 ASP   E C   1 
ATOM   13175 O O   . ASP   I  1 199 ? 17.37663  -23.88790 49.10159  1.000 44.14975  ?  199 ASP   E O   1 
ATOM   13176 C CB  . ASP   I  1 199 ? 16.19793  -26.21154 50.33491  1.000 46.19917  ?  199 ASP   E CB  1 
ATOM   13177 C CG  . ASP   I  1 199 ? 17.41153  -27.10159 50.08786  1.000 147.54795 ?  199 ASP   E CG  1 
ATOM   13178 O OD1 . ASP   I  1 199 ? 18.56972  -26.68291 50.35901  1.000 49.03532  ?  199 ASP   E OD1 1 
ATOM   13179 O OD2 . ASP   I  1 199 ? 17.17464  -28.23846 49.61628  1.000 56.73535  -1 199 ASP   E OD2 1 
ATOM   13180 N N   . LYS   I  1 200 ? 18.54271  -23.51924 51.00718  1.000 43.78135  ?  200 LYS   E N   1 
ATOM   13181 C CA  . LYS   I  1 200 ? 19.46262  -22.59438 50.34191  1.000 69.24213  ?  200 LYS   E CA  1 
ATOM   13182 C C   . LYS   I  1 200 ? 20.31033  -23.27429 49.27584  1.000 65.98642  ?  200 LYS   E C   1 
ATOM   13183 O O   . LYS   I  1 200 ? 20.91088  -22.57474 48.45632  1.000 57.70319  ?  200 LYS   E O   1 
ATOM   13184 C CB  . LYS   I  1 200 ? 20.37865  -21.89615 51.35671  1.000 43.59666  ?  200 LYS   E CB  1 
ATOM   13185 C CG  . LYS   I  1 200 ? 21.50195  -22.75618 51.90156  1.000 66.38619  ?  200 LYS   E CG  1 
ATOM   13186 C CD  . LYS   I  1 200 ? 22.33999  -22.01214 52.94706  1.000 86.89613  ?  200 LYS   E CD  1 
ATOM   13187 C CE  . LYS   I  1 200 ? 23.14754  -20.85429 52.35243  1.000 70.17450  ?  200 LYS   E CE  1 
ATOM   13188 N NZ  . LYS   I  1 200 ? 24.24229  -20.41463 53.28426  1.000 64.75428  ?  200 LYS   E NZ  1 
ATOM   13189 N N   . ASN   I  1 201 ? 20.35203  -24.60579 49.25050  1.000 52.58592  ?  201 ASN   E N   1 
ATOM   13190 C CA  . ASN   I  1 201 ? 21.12798  -25.35657 48.27540  1.000 75.74761  ?  201 ASN   E CA  1 
ATOM   13191 C C   . ASN   I  1 201 ? 20.29500  -25.85039 47.11049  1.000 51.49257  ?  201 ASN   E C   1 
ATOM   13192 O O   . ASN   I  1 201 ? 20.85022  -26.39075 46.15032  1.000 83.53322  ?  201 ASN   E O   1 
ATOM   13193 C CB  . ASN   I  1 201 ? 21.80228  -26.53766 48.96157  1.000 49.74548  ?  201 ASN   E CB  1 
ATOM   13194 C CG  . ASN   I  1 201 ? 22.70383  -26.09254 50.06919  1.000 87.20924  ?  201 ASN   E CG  1 
ATOM   13195 O OD1 . ASN   I  1 201 ? 23.45145  -25.11110 49.91852  1.000 40.44181  ?  201 ASN   E OD1 1 
ATOM   13196 N ND2 . ASN   I  1 201 ? 22.61642  -26.76844 51.20934  1.000 55.32373  ?  201 ASN   E ND2 1 
ATOM   13197 N N   . ALA   I  1 202 ? 19.05499  -25.68957 47.16780  1.000 96.99777  ?  202 ALA   E N   1 
ATOM   13198 C CA  . ALA   I  1 202 ? 18.20178  -26.14210 46.08862  1.000 49.49343  ?  202 ALA   E CA  1 
ATOM   13199 C C   . ALA   I  1 202 ? 18.00922  -25.02846 45.06729  1.000 42.72431  ?  202 ALA   E C   1 
ATOM   13200 O O   . ALA   I  1 202 ? 18.18183  -23.84396 45.38463  1.000 54.47845  ?  202 ALA   E O   1 
ATOM   13201 C CB  . ALA   I  1 202 ? 16.85194  -26.58460 46.63374  1.000 26.86177  ?  202 ALA   E CB  1 
ATOM   13202 N N   . PRO   I  1 203 ? 17.70536  -25.37882 43.82116  1.000 70.56407  ?  203 PRO   E N   1 
ATOM   13203 C CA  . PRO   I  1 203 ? 17.28759  -24.34817 42.86432  1.000 65.38432  ?  203 PRO   E CA  1 
ATOM   13204 C C   . PRO   I  1 203 ? 15.98569  -23.71091 43.32656  1.000 55.20935  ?  203 PRO   E C   1 
ATOM   13205 O O   . PRO   I  1 203 ? 15.08411  -24.38766 43.84366  1.000 35.46617  ?  203 PRO   E O   1 
ATOM   13206 C CB  . PRO   I  1 203 ? 17.11878  -25.11371 41.54338  1.000 42.66722  ?  203 PRO   E CB  1 
ATOM   13207 C CG  . PRO   I  1 203 ? 17.01185  -26.56793 41.93012  1.000 33.37572  ?  203 PRO   E CG  1 
ATOM   13208 C CD  . PRO   I  1 203 ? 17.77104  -26.72440 43.22338  1.000 21.50904  ?  203 PRO   E CD  1 
ATOM   13209 N N   . TYR   I  1 204 ? 15.91588  -22.38536 43.16777  1.000 48.86156  ?  204 TYR   E N   1 
ATOM   13210 C CA  . TYR   I  1 204 ? 14.78381  -21.57631 43.60805  1.000 59.93119  ?  204 TYR   E CA  1 
ATOM   13211 C C   . TYR   I  1 204 ? 14.59151  -21.63111 45.11071  1.000 53.64005  ?  204 TYR   E C   1 
ATOM   13212 O O   . TYR   I  1 204 ? 13.46645  -21.48445 45.59338  1.000 57.99337  ?  204 TYR   E O   1 
ATOM   13213 C CB  . TYR   I  1 204 ? 13.48984  -22.00721 42.90690  1.000 47.33750  ?  204 TYR   E CB  1 
ATOM   13214 C CG  . TYR   I  1 204 ? 13.69710  -22.26495 41.43559  1.000 51.61308  ?  204 TYR   E CG  1 
ATOM   13215 C CD1 . TYR   I  1 204 ? 14.18269  -21.25285 40.60343  1.000 46.37451  ?  204 TYR   E CD1 1 
ATOM   13216 C CD2 . TYR   I  1 204 ? 13.42146  -23.51402 40.87509  1.000 42.56195  ?  204 TYR   E CD2 1 
ATOM   13217 C CE1 . TYR   I  1 204 ? 14.39375  -21.46919 39.25018  1.000 29.08988  ?  204 TYR   E CE1 1 
ATOM   13218 C CE2 . TYR   I  1 204 ? 13.62245  -23.74419 39.52067  1.000 39.60482  ?  204 TYR   E CE2 1 
ATOM   13219 C CZ  . TYR   I  1 204 ? 14.11845  -22.71607 38.71850  1.000 52.81807  ?  204 TYR   E CZ  1 
ATOM   13220 O OH  . TYR   I  1 204 ? 14.32426  -22.91051 37.37383  1.000 54.82800  ?  204 TYR   E OH  1 
ATOM   13221 N N   . TYR   I  1 205 ? 15.66471  -21.88641 45.85686  1.000 43.18408  ?  205 TYR   E N   1 
ATOM   13222 C CA  . TYR   I  1 205 ? 15.60560  -22.06118 47.30471  1.000 41.14408  ?  205 TYR   E CA  1 
ATOM   13223 C C   . TYR   I  1 205 ? 14.53657  -23.07630 47.72925  1.000 48.56712  ?  205 TYR   E C   1 
ATOM   13224 O O   . TYR   I  1 205 ? 14.05744  -23.05157 48.87268  1.000 46.55061  ?  205 TYR   E O   1 
ATOM   13225 C CB  . TYR   I  1 205 ? 15.37316  -20.72614 48.01069  1.000 48.26254  ?  205 TYR   E CB  1 
ATOM   13226 C CG  . TYR   I  1 205 ? 16.61493  -20.05136 48.52174  1.000 61.96929  ?  205 TYR   E CG  1 
ATOM   13227 C CD1 . TYR   I  1 205 ? 17.82501  -20.15531 47.85303  1.000 54.22031  ?  205 TYR   E CD1 1 
ATOM   13228 C CD2 . TYR   I  1 205 ? 16.57729  -19.30997 49.69677  1.000 49.47287  ?  205 TYR   E CD2 1 
ATOM   13229 C CE1 . TYR   I  1 205 ? 18.97542  -19.51148 48.34737  1.000 39.09796  ?  205 TYR   E CE1 1 
ATOM   13230 C CE2 . TYR   I  1 205 ? 17.70732  -18.67279 50.19199  1.000 63.09836  ?  205 TYR   E CE2 1 
ATOM   13231 C CZ  . TYR   I  1 205 ? 18.89989  -18.77620 49.51640  1.000 82.99219  ?  205 TYR   E CZ  1 
ATOM   13232 O OH  . TYR   I  1 205 ? 19.99890  -18.13699 50.02715  1.000 53.57998  ?  205 TYR   E OH  1 
ATOM   13233 N N   . GLY   I  1 206 ? 14.13968  -23.97378 46.83126  1.000 39.73969  ?  206 GLY   E N   1 
ATOM   13234 C CA  . GLY   I  1 206 ? 13.17892  -24.99761 47.16677  1.000 38.62710  ?  206 GLY   E CA  1 
ATOM   13235 C C   . GLY   I  1 206 ? 11.72528  -24.60683 47.00749  1.000 52.41603  ?  206 GLY   E C   1 
ATOM   13236 O O   . GLY   I  1 206 ? 10.85450  -25.47633 47.12633  1.000 44.43211  ?  206 GLY   E O   1 
ATOM   13237 N N   . PHE   I  1 207 ? 11.42704  -23.33823 46.74554  1.000 39.41801  ?  207 PHE   E N   1 
ATOM   13238 C CA  . PHE   I  1 207 ? 10.04353  -22.93292 46.53926  1.000 51.47731  ?  207 PHE   E CA  1 
ATOM   13239 C C   . PHE   I  1 207 ? 9.54445   -23.44494 45.19330  1.000 46.94132  ?  207 PHE   E C   1 
ATOM   13240 O O   . PHE   I  1 207 ? 10.28785  -23.45873 44.20863  1.000 56.98303  ?  207 PHE   E O   1 
ATOM   13241 C CB  . PHE   I  1 207 ? 9.92871   -21.41194 46.60460  1.000 38.81304  ?  207 PHE   E CB  1 
ATOM   13242 C CG  . PHE   I  1 207 ? 10.35376  -20.82258 47.91871  1.000 54.46111  ?  207 PHE   E CG  1 
ATOM   13243 C CD1 . PHE   I  1 207 ? 9.53534   -20.93057 49.03455  1.000 28.23877  ?  207 PHE   E CD1 1 
ATOM   13244 C CD2 . PHE   I  1 207 ? 11.56080  -20.13733 48.03692  1.000 32.61516  ?  207 PHE   E CD2 1 
ATOM   13245 C CE1 . PHE   I  1 207 ? 9.91548   -20.37271 50.24714  1.000 48.54544  ?  207 PHE   E CE1 1 
ATOM   13246 C CE2 . PHE   I  1 207 ? 11.94881  -19.57096 49.25165  1.000 36.27074  ?  207 PHE   E CE2 1 
ATOM   13247 C CZ  . PHE   I  1 207 ? 11.12498  -19.69140 50.35485  1.000 53.22765  ?  207 PHE   E CZ  1 
ATOM   13248 N N   . ASN   I  1 208 ? 8.27957   -23.87343 45.14542  1.000 37.34176  ?  208 ASN   E N   1 
ATOM   13249 C CA  . ASN   I  1 208 ? 7.73052   -24.45162 43.92102  1.000 59.85513  ?  208 ASN   E CA  1 
ATOM   13250 C C   . ASN   I  1 208 ? 6.96582   -23.46142 43.05012  1.000 29.47961  ?  208 ASN   E C   1 
ATOM   13251 O O   . ASN   I  1 208 ? 6.42802   -23.86557 42.00912  1.000 87.65402  ?  208 ASN   E O   1 
ATOM   13252 C CB  . ASN   I  1 208 ? 6.83040   -25.65647 44.23478  1.000 29.92963  ?  208 ASN   E CB  1 
ATOM   13253 C CG  . ASN   I  1 208 ? 5.91977   -25.42687 45.40022  1.000 86.39883  ?  208 ASN   E CG  1 
ATOM   13254 O OD1 . ASN   I  1 208 ? 5.05773   -24.53793 45.37693  1.000 141.44800 ?  208 ASN   E OD1 1 
ATOM   13255 N ND2 . ASN   I  1 208 ? 6.07575   -26.25606 46.42767  1.000 63.37436  ?  208 ASN   E ND2 1 
ATOM   13256 N N   . SER   I  1 209 ? 6.92847   -22.18458 43.42552  1.000 50.73143  ?  209 SER   E N   1 
ATOM   13257 C CA  . SER   I  1 209 ? 6.25935   -21.13692 42.65774  1.000 34.19547  ?  209 SER   E CA  1 
ATOM   13258 C C   . SER   I  1 209 ? 6.56426   -19.81774 43.33354  1.000 56.34284  ?  209 SER   E C   1 
ATOM   13259 O O   . SER   I  1 209 ? 7.08858   -19.77978 44.45140  1.000 31.57576  ?  209 SER   E O   1 
ATOM   13260 C CB  . SER   I  1 209 ? 4.74144   -21.30899 42.59247  1.000 45.18803  ?  209 SER   E CB  1 
ATOM   13261 O OG  . SER   I  1 209 ? 4.18270   -21.06570 43.87286  1.000 24.51192  ?  209 SER   E OG  1 
ATOM   13262 N N   . TYR   I  1 210 ? 6.18807   -18.73062 42.65763  1.000 36.09360  ?  210 TYR   E N   1 
ATOM   13263 C CA  . TYR   I  1 210 ? 6.38450   -17.42208 43.26364  1.000 24.20692  ?  210 TYR   E CA  1 
ATOM   13264 C C   . TYR   I  1 210 ? 5.50373   -17.25585 44.49716  1.000 37.21526  ?  210 TYR   E C   1 
ATOM   13265 O O   . TYR   I  1 210 ? 5.97046   -16.79127 45.54492  1.000 30.16155  ?  210 TYR   E O   1 
ATOM   13266 C CB  . TYR   I  1 210 ? 6.11324   -16.31846 42.24224  1.000 13.61162  ?  210 TYR   E CB  1 
ATOM   13267 C CG  . TYR   I  1 210 ? 6.14755   -14.95415 42.86838  1.000 46.68490  ?  210 TYR   E CG  1 
ATOM   13268 C CD1 . TYR   I  1 210 ? 7.35918   -14.34186 43.15971  1.000 23.70748  ?  210 TYR   E CD1 1 
ATOM   13269 C CD2 . TYR   I  1 210 ? 4.97452   -14.29220 43.20718  1.000 39.12104  ?  210 TYR   E CD2 1 
ATOM   13270 C CE1 . TYR   I  1 210 ? 7.41488   -13.09573 43.76461  1.000 27.33027  ?  210 TYR   E CE1 1 
ATOM   13271 C CE2 . TYR   I  1 210 ? 5.01452   -13.04559 43.81018  1.000 40.89070  ?  210 TYR   E CE2 1 
ATOM   13272 C CZ  . TYR   I  1 210 ? 6.23943   -12.45606 44.08187  1.000 49.88590  ?  210 TYR   E CZ  1 
ATOM   13273 O OH  . TYR   I  1 210 ? 6.29164   -11.22558 44.66817  1.000 31.66205  ?  210 TYR   E OH  1 
ATOM   13274 N N   . ASP   I  1 211 ? 4.23284   -17.64887 44.39173  1.000 31.03850  ?  211 ASP   E N   1 
ATOM   13275 C CA  . ASP   I  1 211 ? 3.32124   -17.55443 45.52665  1.000 25.76227  ?  211 ASP   E CA  1 
ATOM   13276 C C   . ASP   I  1 211 ? 3.85142   -18.32095 46.72668  1.000 47.15097  ?  211 ASP   E C   1 
ATOM   13277 O O   . ASP   I  1 211 ? 3.69462   -17.87901 47.87646  1.000 28.03326  ?  211 ASP   E O   1 
ATOM   13278 C CB  . ASP   I  1 211 ? 1.93463   -18.08011 45.14452  1.000 28.90188  ?  211 ASP   E CB  1 
ATOM   13279 C CG  . ASP   I  1 211 ? 0.94392   -17.97162 46.29102  1.000 29.44518  ?  211 ASP   E CG  1 
ATOM   13280 O OD1 . ASP   I  1 211 ? 0.60181   -16.82321 46.67550  1.000 34.19652  ?  211 ASP   E OD1 1 
ATOM   13281 O OD2 . ASP   I  1 211 ? 0.51644   -19.02759 46.81412  1.000 52.11171  -1 211 ASP   E OD2 1 
ATOM   13282 N N   . ASP   I  1 212 ? 4.45763   -19.48749 46.47716  1.000 28.99544  ?  212 ASP   E N   1 
ATOM   13283 C CA  . ASP   I  1 212 ? 5.08543   -20.24745 47.55457  1.000 38.51331  ?  212 ASP   E CA  1 
ATOM   13284 C C   . ASP   I  1 212 ? 6.15824   -19.41360 48.25692  1.000 30.77708  ?  212 ASP   E C   1 
ATOM   13285 O O   . ASP   I  1 212 ? 6.23443   -19.38441 49.49401  1.000 31.46403  ?  212 ASP   E O   1 
ATOM   13286 C CB  . ASP   I  1 212 ? 5.66740   -21.54260 46.98148  1.000 39.99189  ?  212 ASP   E CB  1 
ATOM   13287 C CG  . ASP   I  1 212 ? 6.14680   -22.50917 48.05334  1.000 48.11248  ?  212 ASP   E CG  1 
ATOM   13288 O OD1 . ASP   I  1 212 ? 5.63342   -22.44212 49.19149  1.000 63.11274  ?  212 ASP   E OD1 1 
ATOM   13289 O OD2 . ASP   I  1 212 ? 7.05545   -23.32239 47.74987  1.000 48.98515  -1 212 ASP   E OD2 1 
ATOM   13290 N N   . PHE   I  1 213 ? 6.97611   -18.70416 47.48185  1.000 25.37942  ?  213 PHE   E N   1 
ATOM   13291 C CA  . PHE   I  1 213 ? 7.99678   -17.84174 48.06642  1.000 22.64964  ?  213 PHE   E CA  1 
ATOM   13292 C C   . PHE   I  1 213 ? 7.36921   -16.65361 48.78814  1.000 59.55859  ?  213 PHE   E C   1 
ATOM   13293 O O   . PHE   I  1 213 ? 7.79660   -16.28649 49.89702  1.000 34.05578  ?  213 PHE   E O   1 
ATOM   13294 C CB  . PHE   I  1 213 ? 8.94977   -17.36617 46.96498  1.000 29.32787  ?  213 PHE   E CB  1 
ATOM   13295 C CG  . PHE   I  1 213 ? 9.74011   -16.17458 47.34238  1.000 42.02743  ?  213 PHE   E CG  1 
ATOM   13296 C CD1 . PHE   I  1 213 ? 10.88946  -16.30782 48.11908  1.000 45.50925  ?  213 PHE   E CD1 1 
ATOM   13297 C CD2 . PHE   I  1 213 ? 9.33735   -14.91098 46.93817  1.000 30.23320  ?  213 PHE   E CD2 1 
ATOM   13298 C CE1 . PHE   I  1 213 ? 11.63268  -15.19174 48.48127  1.000 54.98440  ?  213 PHE   E CE1 1 
ATOM   13299 C CE2 . PHE   I  1 213 ? 10.07369  -13.79387 47.29375  1.000 57.92554  ?  213 PHE   E CE2 1 
ATOM   13300 C CZ  . PHE   I  1 213 ? 11.22342  -13.93401 48.06876  1.000 47.37834  ?  213 PHE   E CZ  1 
ATOM   13301 N N   . PHE   I  1 214 ? 6.36730   -16.03435 48.15159  1.000 24.30790  ?  214 PHE   E N   1 
ATOM   13302 C CA  . PHE   I  1 214 ? 5.67075   -14.88627 48.72226  1.000 22.60065  ?  214 PHE   E CA  1 
ATOM   13303 C C   . PHE   I  1 214 ? 5.06584   -15.22024 50.08751  1.000 21.40631  ?  214 PHE   E C   1 
ATOM   13304 O O   . PHE   I  1 214 ? 5.09451   -14.39284 51.01211  1.000 49.02925  ?  214 PHE   E O   1 
ATOM   13305 C CB  . PHE   I  1 214 ? 4.59794   -14.42911 47.72986  1.000 31.33481  ?  214 PHE   E CB  1 
ATOM   13306 C CG  . PHE   I  1 214 ? 3.85784   -13.18977 48.14213  1.000 29.54553  ?  214 PHE   E CG  1 
ATOM   13307 C CD1 . PHE   I  1 214 ? 4.43367   -11.93991 47.98429  1.000 28.08423  ?  214 PHE   E CD1 1 
ATOM   13308 C CD2 . PHE   I  1 214 ? 2.57091   -13.27038 48.65715  1.000 36.97851  ?  214 PHE   E CD2 1 
ATOM   13309 C CE1 . PHE   I  1 214 ? 3.76264   -10.79172 48.35703  1.000 24.52914  ?  214 PHE   E CE1 1 
ATOM   13310 C CE2 . PHE   I  1 214 ? 1.88078   -12.11800 49.02627  1.000 36.36970  ?  214 PHE   E CE2 1 
ATOM   13311 C CZ  . PHE   I  1 214 ? 2.47640   -10.87217 48.87069  1.000 30.28990  ?  214 PHE   E CZ  1 
ATOM   13312 N N   . ASN   I  1 215 ? 4.53977   -16.43696 50.24182  1.000 22.52406  ?  215 ASN   E N   1 
ATOM   13313 C CA  . ASN   I  1 215 ? 3.93236   -16.88720 51.49158  1.000 30.18277  ?  215 ASN   E CA  1 
ATOM   13314 C C   . ASN   I  1 215 ? 4.81578   -17.87876 52.24516  1.000 39.96533  ?  215 ASN   E C   1 
ATOM   13315 O O   . ASN   I  1 215 ? 4.32365   -18.82143 52.87241  1.000 33.70900  ?  215 ASN   E O   1 
ATOM   13316 C CB  . ASN   I  1 215 ? 2.55384   -17.48045 51.22972  1.000 30.03004  ?  215 ASN   E CB  1 
ATOM   13317 C CG  . ASN   I  1 215 ? 1.52739   -16.40543 50.94425  1.000 53.15196  ?  215 ASN   E CG  1 
ATOM   13318 O OD1 . ASN   I  1 215 ? 1.46297   -15.38331 51.63890  1.000 31.81238  ?  215 ASN   E OD1 1 
ATOM   13319 N ND2 . ASN   I  1 215 ? 0.74283   -16.60925 49.90135  1.000 28.54025  ?  215 ASN   E ND2 1 
ATOM   13320 N N   . ARG   I  1 216 ? 6.13273   -17.65925 52.19250  1.000 20.39360  ?  216 ARG   E N   1 
ATOM   13321 C CA  . ARG   I  1 216 ? 7.08350   -18.50089 52.89879  1.000 29.27428  ?  216 ARG   E CA  1 
ATOM   13322 C C   . ARG   I  1 216 ? 6.78777   -18.51280 54.39886  1.000 52.31763  ?  216 ARG   E C   1 
ATOM   13323 O O   . ARG   I  1 216 ? 6.39654   -17.49789 54.98320  1.000 28.50203  ?  216 ARG   E O   1 
ATOM   13324 C CB  . ARG   I  1 216 ? 8.49717   -17.98610 52.62969  1.000 25.55716  ?  216 ARG   E CB  1 
ATOM   13325 C CG  . ARG   I  1 216 ? 8.72867   -16.57523 53.12149  1.000 24.84846  ?  216 ARG   E CG  1 
ATOM   13326 C CD  . ARG   I  1 216 ? 10.02201  -16.00669 52.59489  1.000 35.16248  ?  216 ARG   E CD  1 
ATOM   13327 N NE  . ARG   I  1 216 ? 10.13909  -14.58123 52.88904  1.000 24.10279  ?  216 ARG   E NE  1 
ATOM   13328 C CZ  . ARG   I  1 216 ? 9.55978   -13.63021 52.16781  1.000 48.88191  ?  216 ARG   E CZ  1 
ATOM   13329 N NH1 . ARG   I  1 216 ? 8.83525   -13.92086 51.09578  1.000 27.69506  ?  216 ARG   E NH1 1 
ATOM   13330 N NH2 . ARG   I  1 216 ? 9.70224   -12.35984 52.53391  1.000 32.17941  ?  216 ARG   E NH2 1 
ATOM   13331 N N   . ARG   I  1 217 ? 6.93577   -19.66980 55.01750  1.000 27.33784  ?  217 ARG   E N   1 
ATOM   13332 C CA  . ARG   I  1 217 ? 6.68405   -19.73889 56.44409  1.000 30.04592  ?  217 ARG   E CA  1 
ATOM   13333 C C   . ARG   I  1 217 ? 7.97213   -19.48424 57.24655  1.000 31.19436  ?  217 ARG   E C   1 
ATOM   13334 O O   . ARG   I  1 217 ? 9.08030   -19.46978 56.71524  1.000 46.04553  ?  217 ARG   E O   1 
ATOM   13335 C CB  . ARG   I  1 217 ? 6.03418   -21.09595 56.77703  1.000 27.88520  ?  217 ARG   E CB  1 
ATOM   13336 C CG  . ARG   I  1 217 ? 4.90894   -21.48202 55.80479  1.000 33.69210  ?  217 ARG   E CG  1 
ATOM   13337 C CD  . ARG   I  1 217 ? 4.43014   -22.92307 56.01780  1.000 62.88033  ?  217 ARG   E CD  1 
ATOM   13338 N NE  . ARG   I  1 217 ? 4.61704   -23.75862 54.83266  1.000 139.17988 ?  217 ARG   E NE  1 
ATOM   13339 N N   . PHE   I  1 218 ? 7.80453   -19.25524 58.55658  1.000 38.56670  ?  218 PHE   E N   1 
ATOM   13340 C CA  . PHE   I  1 218 ? 8.97480   -19.09614 59.41845  1.000 27.43453  ?  218 PHE   E CA  1 
ATOM   13341 C C   . PHE   I  1 218 ? 9.57995   -20.46225 59.73433  1.000 57.88483  ?  218 PHE   E C   1 
ATOM   13342 O O   . PHE   I  1 218 ? 8.85645   -21.41761 60.02758  1.000 29.64561  ?  218 PHE   E O   1 
ATOM   13343 C CB  . PHE   I  1 218 ? 8.60651   -18.39333 60.71981  1.000 18.28545  ?  218 PHE   E CB  1 
ATOM   13344 C CG  . PHE   I  1 218 ? 8.31496   -16.93242 60.56514  1.000 37.94126  ?  218 PHE   E CG  1 
ATOM   13345 C CD1 . PHE   I  1 218 ? 9.30033   -16.05333 60.10668  1.000 19.95337  ?  218 PHE   E CD1 1 
ATOM   13346 C CD2 . PHE   I  1 218 ? 7.05484   -16.42646 60.89895  1.000 28.61404  ?  218 PHE   E CD2 1 
ATOM   13347 C CE1 . PHE   I  1 218 ? 9.03761   -14.69237 59.97343  1.000 45.20322  ?  218 PHE   E CE1 1 
ATOM   13348 C CE2 . PHE   I  1 218 ? 6.77982   -15.07456 60.76659  1.000 27.88122  ?  218 PHE   E CE2 1 
ATOM   13349 C CZ  . PHE   I  1 218 ? 7.77497   -14.20284 60.30095  1.000 21.13683  ?  218 PHE   E CZ  1 
ATOM   13350 N N   . ARG   I  1 219 ? 10.91049  -20.55824 59.69088  1.000 35.50729  ?  219 ARG   E N   1 
ATOM   13351 C CA  . ARG   I  1 219 ? 11.55977  -21.81634 60.05153  1.000 39.83860  ?  219 ARG   E CA  1 
ATOM   13352 C C   . ARG   I  1 219 ? 11.44357  -22.10059 61.54194  1.000 36.77781  ?  219 ARG   E C   1 
ATOM   13353 O O   . ARG   I  1 219 ? 11.35457  -23.26174 61.95289  1.000 35.31377  ?  219 ARG   E O   1 
ATOM   13354 C CB  . ARG   I  1 219 ? 13.03348  -21.79525 59.65513  1.000 32.62580  ?  219 ARG   E CB  1 
ATOM   13355 C CG  . ARG   I  1 219 ? 13.69262  -23.15988 59.88000  1.000 49.06551  ?  219 ARG   E CG  1 
ATOM   13356 C CD  . ARG   I  1 219 ? 15.18618  -23.13527 59.66132  1.000 38.96966  ?  219 ARG   E CD  1 
ATOM   13357 N NE  . ARG   I  1 219 ? 15.53885  -22.84373 58.27889  1.000 25.09664  ?  219 ARG   E NE  1 
ATOM   13358 C CZ  . ARG   I  1 219 ? 15.37357  -23.69627 57.27670  1.000 93.00366  ?  219 ARG   E CZ  1 
ATOM   13359 N NH1 . ARG   I  1 219 ? 14.87135  -24.90390 57.46812  1.000 25.35069  ?  219 ARG   E NH1 1 
ATOM   13360 N NH2 . ARG   I  1 219 ? 15.71736  -23.32872 56.04929  1.000 17.16617  ?  219 ARG   E NH2 1 
ATOM   13361 N N   . ASN   I  1 220 ? 11.44276  -21.05953 62.36218  1.000 31.26258  ?  220 ASN   E N   1 
ATOM   13362 C CA  . ASN   I  1 220 ? 11.46154  -21.24107 63.80140  1.000 37.30954  ?  220 ASN   E CA  1 
ATOM   13363 C C   . ASN   I  1 220 ? 10.97546  -19.96011 64.46384  1.000 34.19749  ?  220 ASN   E C   1 
ATOM   13364 O O   . ASN   I  1 220 ? 11.78790  -19.11974 64.87699  1.000 39.63958  ?  220 ASN   E O   1 
ATOM   13365 C CB  . ASN   I  1 220 ? 12.87706  -21.59805 64.25952  1.000 45.22089  ?  220 ASN   E CB  1 
ATOM   13366 C CG  . ASN   I  1 220 ? 12.92394  -22.10419 65.68457  1.000 70.50388  ?  220 ASN   E CG  1 
ATOM   13367 O OD1 . ASN   I  1 220 ? 12.00510  -21.87980 66.48222  1.000 45.75200  ?  220 ASN   E OD1 1 
ATOM   13368 N ND2 . ASN   I  1 220 ? 14.00528  -22.78862 66.01703  1.000 47.03664  ?  220 ASN   E ND2 1 
ATOM   13369 N N   . ARG   I  1 221 ? 9.65382   -19.79889 64.57041  1.000 31.14324  ?  221 ARG   E N   1 
ATOM   13370 C CA  . ARG   I  1 221 ? 9.12538   -18.53217 65.07106  1.000 34.48530  ?  221 ARG   E CA  1 
ATOM   13371 C C   . ARG   I  1 221 ? 9.57060   -18.26206 66.50587  1.000 43.17591  ?  221 ARG   E C   1 
ATOM   13372 O O   . ARG   I  1 221 ? 9.75189   -17.09857 66.87620  1.000 33.10880  ?  221 ARG   E O   1 
ATOM   13373 C CB  . ARG   I  1 221 ? 7.59424   -18.49871 64.94892  1.000 21.96154  ?  221 ARG   E CB  1 
ATOM   13374 C CG  . ARG   I  1 221 ? 6.84394   -19.47837 65.85902  1.000 22.48592  ?  221 ARG   E CG  1 
ATOM   13375 C CD  . ARG   I  1 221 ? 6.30595   -18.79604 67.12592  1.000 34.18541  ?  221 ARG   E CD  1 
ATOM   13376 N NE  . ARG   I  1 221 ? 5.65288   -19.74853 68.02196  1.000 29.21582  ?  221 ARG   E NE  1 
ATOM   13377 C CZ  . ARG   I  1 221 ? 4.36453   -20.07348 67.98365  1.000 40.74496  ?  221 ARG   E CZ  1 
ATOM   13378 N NH1 . ARG   I  1 221 ? 3.53343   -19.54642 67.09656  1.000 35.11635  ?  221 ARG   E NH1 1 
ATOM   13379 N NH2 . ARG   I  1 221 ? 3.89213   -20.94373 68.86465  1.000 25.83534  ?  221 ARG   E NH2 1 
ATOM   13380 N N   . ASP   I  1 222 ? 9.79575   -19.31097 67.31359  1.000 35.41894  ?  222 ASP   E N   1 
ATOM   13381 C CA  . ASP   I  1 222 ? 10.21959  -19.09890 68.69899  1.000 52.40177  ?  222 ASP   E CA  1 
ATOM   13382 C C   . ASP   I  1 222 ? 11.58367  -18.41216 68.81386  1.000 55.12801  ?  222 ASP   E C   1 
ATOM   13383 O O   . ASP   I  1 222 ? 11.87040  -17.79615 69.85012  1.000 41.95064  ?  222 ASP   E O   1 
ATOM   13384 C CB  . ASP   I  1 222 ? 10.23998  -20.42448 69.46054  1.000 29.92445  ?  222 ASP   E CB  1 
ATOM   13385 C CG  . ASP   I  1 222 ? 8.84706   -21.07438 69.55606  1.000 48.91656  ?  222 ASP   E CG  1 
ATOM   13386 O OD1 . ASP   I  1 222 ? 7.93355   -20.53044 70.22694  1.000 55.88123  ?  222 ASP   E OD1 1 
ATOM   13387 O OD2 . ASP   I  1 222 ? 8.67128   -22.12966 68.91820  1.000 65.01524  -1 222 ASP   E OD2 1 
ATOM   13388 N N   . ILE   I  1 223 ? 12.42418  -18.47660 67.78218  1.000 34.09255  ?  223 ILE   E N   1 
ATOM   13389 C CA  . ILE   I  1 223 ? 13.64052  -17.66763 67.78116  1.000 43.64877  ?  223 ILE   E CA  1 
ATOM   13390 C C   . ILE   I  1 223 ? 13.35499  -16.26135 67.25753  1.000 54.85763  ?  223 ILE   E C   1 
ATOM   13391 O O   . ILE   I  1 223 ? 13.59534  -15.26360 67.94788  1.000 57.38461  ?  223 ILE   E O   1 
ATOM   13392 C CB  . ILE   I  1 223 ? 14.74895  -18.36817 66.97108  1.000 56.27790  ?  223 ILE   E CB  1 
ATOM   13393 C CG1 . ILE   I  1 223 ? 15.22136  -19.62737 67.69187  1.000 37.29458  ?  223 ILE   E CG1 1 
ATOM   13394 C CG2 . ILE   I  1 223 ? 15.93534  -17.44894 66.73984  1.000 25.08302  ?  223 ILE   E CG2 1 
ATOM   13395 C CD1 . ILE   I  1 223 ? 16.16412  -20.44041 66.85495  1.000 40.32290  ?  223 ILE   E CD1 1 
ATOM   13396 N N   . ASP   I  1 224 ? 12.80468  -16.16682 66.04100  1.000 33.32299  ?  224 ASP   E N   1 
ATOM   13397 C CA  . ASP   I  1 224 ? 12.73831  -14.90900 65.29660  1.000 34.42853  ?  224 ASP   E CA  1 
ATOM   13398 C C   . ASP   I  1 224 ? 11.50060  -14.05533 65.56819  1.000 35.30529  ?  224 ASP   E C   1 
ATOM   13399 O O   . ASP   I  1 224 ? 11.59316  -12.82244 65.50070  1.000 30.89701  ?  224 ASP   E O   1 
ATOM   13400 C CB  . ASP   I  1 224 ? 12.81246  -15.20362 63.80213  1.000 30.33864  ?  224 ASP   E CB  1 
ATOM   13401 C CG  . ASP   I  1 224 ? 14.04214  -16.00075 63.43573  1.000 43.70729  ?  224 ASP   E CG  1 
ATOM   13402 O OD1 . ASP   I  1 224 ? 15.15119  -15.44548 63.57785  1.000 46.83746  ?  224 ASP   E OD1 1 
ATOM   13403 O OD2 . ASP   I  1 224 ? 13.89353  -17.17504 63.02717  1.000 43.35932  -1 224 ASP   E OD2 1 
ATOM   13404 N N   . ARG   I  1 225 ? 10.34321  -14.66051 65.83481  1.000 42.61897  ?  225 ARG   E N   1 
ATOM   13405 C CA  . ARG   I  1 225 ? 9.08760   -13.92549 66.03208  1.000 33.29288  ?  225 ARG   E CA  1 
ATOM   13406 C C   . ARG   I  1 225 ? 8.29611   -14.60777 67.13466  1.000 48.39112  ?  225 ARG   E C   1 
ATOM   13407 O O   . ARG   I  1 225 ? 7.23529   -15.20004 66.89795  1.000 42.42843  ?  225 ARG   E O   1 
ATOM   13408 C CB  . ARG   I  1 225 ? 8.27840   -13.86674 64.73057  1.000 34.34485  ?  225 ARG   E CB  1 
ATOM   13409 C CG  . ARG   I  1 225 ? 8.93341   -12.88831 63.71192  1.000 10.49874  ?  225 ARG   E CG  1 
ATOM   13410 C CD  . ARG   I  1 225 ? 8.94982   -11.37385 64.21395  1.000 20.88721  ?  225 ARG   E CD  1 
ATOM   13411 N NE  . ARG   I  1 225 ? 9.30771   -10.33371 63.23371  1.000 17.35301  ?  225 ARG   E NE  1 
ATOM   13412 C CZ  . ARG   I  1 225 ? 10.53707  -9.86803  63.05387  1.000 29.52693  ?  225 ARG   E CZ  1 
ATOM   13413 N NH1 . ARG   I  1 225 ? 11.57207  -10.39863 63.68402  1.000 15.78606  ?  225 ARG   E NH1 1 
ATOM   13414 N NH2 . ARG   I  1 225 ? 10.73837  -8.86254  62.20843  1.000 23.29754  ?  225 ARG   E NH2 1 
ATOM   13415 N N   . PRO   I  1 226 ? 8.79942   -14.56830 68.36247  1.000 43.40560  ?  226 PRO   E N   1 
ATOM   13416 C CA  . PRO   I  1 226 ? 8.15026   -15.31919 69.44526  1.000 25.20780  ?  226 PRO   E CA  1 
ATOM   13417 C C   . PRO   I  1 226 ? 6.79501   -14.73760 69.81258  1.000 49.74419  ?  226 PRO   E C   1 
ATOM   13418 O O   . PRO   I  1 226 ? 6.56300   -13.53072 69.71899  1.000 32.97553  ?  226 PRO   E O   1 
ATOM   13419 C CB  . PRO   I  1 226 ? 9.13335   -15.17650 70.61562  1.000 24.32304  ?  226 PRO   E CB  1 
ATOM   13420 C CG  . PRO   I  1 226 ? 9.89727   -13.89125 70.31356  1.000 23.09980  ?  226 PRO   E CG  1 
ATOM   13421 C CD  . PRO   I  1 226 ? 10.00703  -13.84227 68.81170  1.000 26.30234  ?  226 PRO   E CD  1 
ATOM   13422 N N   . VAL   I  1 227 ? 5.89904   -15.62044 70.25223  1.000 28.59100  ?  227 VAL   E N   1 
ATOM   13423 C CA  . VAL   I  1 227 ? 4.63442   -15.21216 70.85176  1.000 25.61493  ?  227 VAL   E CA  1 
ATOM   13424 C C   . VAL   I  1 227 ? 4.94191   -14.60165 72.21249  1.000 38.05092  ?  227 VAL   E C   1 
ATOM   13425 O O   . VAL   I  1 227 ? 4.95328   -15.30724 73.22731  1.000 39.04134  ?  227 VAL   E O   1 
ATOM   13426 C CB  . VAL   I  1 227 ? 3.66037   -16.40051 70.97221  1.000 28.78672  ?  227 VAL   E CB  1 
ATOM   13427 C CG1 . VAL   I  1 227 ? 2.32077   -15.95923 71.54799  1.000 29.94540  ?  227 VAL   E CG1 1 
ATOM   13428 C CG2 . VAL   I  1 227 ? 3.46873   -17.05666 69.61337  1.000 24.01067  ?  227 VAL   E CG2 1 
ATOM   13429 N N   . VAL   I  1 228 ? 5.19119   -13.28506 72.23312  1.000 37.57223  ?  228 VAL   E N   1 
ATOM   13430 C CA  . VAL   I  1 228 ? 5.73362   -12.60837 73.40722  1.000 25.16409  ?  228 VAL   E CA  1 
ATOM   13431 C C   . VAL   I  1 228 ? 4.84599   -12.83565 74.62046  1.000 65.44975  ?  228 VAL   E C   1 
ATOM   13432 O O   . VAL   I  1 228 ? 3.62333   -12.66186 74.56451  1.000 35.72079  ?  228 VAL   E O   1 
ATOM   13433 C CB  . VAL   I  1 228 ? 5.91183   -11.11492 73.10354  1.000 43.58058  ?  228 VAL   E CB  1 
ATOM   13434 C CG1 . VAL   I  1 228 ? 6.45190   -10.38009 74.31869  1.000 29.97509  ?  228 VAL   E CG1 1 
ATOM   13435 C CG2 . VAL   I  1 228 ? 6.83200   -10.94696 71.89825  1.000 24.58995  ?  228 VAL   E CG2 1 
ATOM   13436 N N   . GLY   I  1 229 ? 5.46932   -13.22994 75.73185  1.000 41.06865  ?  229 GLY   E N   1 
ATOM   13437 C CA  . GLY   I  1 229 ? 4.75684   -13.55209 76.95171  1.000 24.97487  ?  229 GLY   E CA  1 
ATOM   13438 C C   . GLY   I  1 229 ? 4.18619   -14.95338 77.00649  1.000 31.99130  ?  229 GLY   E C   1 
ATOM   13439 O O   . GLY   I  1 229 ? 3.69840   -15.36927 78.07164  1.000 47.19298  ?  229 GLY   E O   1 
ATOM   13440 N N   . GLY   I  1 230 ? 4.21402   -15.68096 75.89738  1.000 47.15041  ?  230 GLY   E N   1 
ATOM   13441 C CA  . GLY   I  1 230 ? 3.75802   -17.06347 75.81865  1.000 18.20442  ?  230 GLY   E CA  1 
ATOM   13442 C C   . GLY   I  1 230 ? 2.26034   -17.18602 75.60627  1.000 65.75966  ?  230 GLY   E C   1 
ATOM   13443 O O   . GLY   I  1 230 ? 1.45712   -16.38997 76.10187  1.000 35.76709  ?  230 GLY   E O   1 
ATOM   13444 N N   . VAL   I  1 231 ? 1.88292   -18.23752 74.87071  1.000 27.63166  ?  231 VAL   E N   1 
ATOM   13445 C CA  . VAL   I  1 231 ? 0.49545   -18.51208 74.51409  1.000 67.97620  ?  231 VAL   E CA  1 
ATOM   13446 C C   . VAL   I  1 231 ? -0.40672  -18.60188 75.74045  1.000 27.84009  ?  231 VAL   E C   1 
ATOM   13447 O O   . VAL   I  1 231 ? -1.62004  -18.37699 75.63833  1.000 62.95316  ?  231 VAL   E O   1 
ATOM   13448 C CB  . VAL   I  1 231 ? 0.45574   -19.80086 73.67147  1.000 20.43897  ?  231 VAL   E CB  1 
ATOM   13449 C CG1 . VAL   I  1 231 ? 1.08258   -20.92367 74.44275  1.000 75.24585  ?  231 VAL   E CG1 1 
ATOM   13450 C CG2 . VAL   I  1 231 ? -0.94616  -20.17691 73.30958  1.000 47.79403  ?  231 VAL   E CG2 1 
ATOM   13451 N N   . ASN   I  1 232 ? 0.16702   -18.85896 76.91642  1.000 38.98034  ?  232 ASN   E N   1 
ATOM   13452 C CA  . ASN   I  1 232 ? -0.61893  -19.02065 78.13693  1.000 27.95661  ?  232 ASN   E CA  1 
ATOM   13453 C C   . ASN   I  1 232 ? -1.04766  -17.70609 78.77687  1.000 39.63990  ?  232 ASN   E C   1 
ATOM   13454 O O   . ASN   I  1 232 ? -1.96605  -17.71774 79.60523  1.000 34.84777  ?  232 ASN   E O   1 
ATOM   13455 C CB  . ASN   I  1 232 ? 0.16704   -19.82554 79.16382  1.000 44.70074  ?  232 ASN   E CB  1 
ATOM   13456 C CG  . ASN   I  1 232 ? -0.03076  -21.30921 79.00249  1.000 44.32192  ?  232 ASN   E CG  1 
ATOM   13457 O OD1 . ASN   I  1 232 ? -0.53286  -21.76991 77.96889  1.000 45.32739  ?  232 ASN   E OD1 1 
ATOM   13458 N ND2 . ASN   I  1 232 ? 0.35641   -22.07453 80.02334  1.000 120.45427 ?  232 ASN   E ND2 1 
ATOM   13459 N N   . ASN   I  1 233 ? -0.40197  -16.58631 78.45119  1.000 25.52560  ?  233 ASN   E N   1 
ATOM   13460 C CA  . ASN   I  1 233 ? -0.79565  -15.29279 78.99480  1.000 33.22488  ?  233 ASN   E CA  1 
ATOM   13461 C C   . ASN   I  1 233 ? -1.87294  -14.72589 78.07271  1.000 85.69348  ?  233 ASN   E C   1 
ATOM   13462 O O   . ASN   I  1 233 ? -1.58136  -14.27994 76.95150  1.000 30.97309  ?  233 ASN   E O   1 
ATOM   13463 C CB  . ASN   I  1 233 ? 0.41133   -14.36228 79.09808  1.000 13.13857  ?  233 ASN   E CB  1 
ATOM   13464 C CG  . ASN   I  1 233 ? 0.08244   -13.06063 79.79538  1.000 50.52866  ?  233 ASN   E CG  1 
ATOM   13465 O OD1 . ASN   I  1 233 ? -1.06183  -12.59861 79.78603  1.000 43.59151  ?  233 ASN   E OD1 1 
ATOM   13466 N ND2 . ASN   I  1 233 ? 1.09241   -12.45066 80.39501  1.000 39.27817  ?  233 ASN   E ND2 1 
ATOM   13467 N N   . THR   I  1 234 ? -3.12244  -14.76418 78.52428  1.000 35.78004  ?  234 THR   E N   1 
ATOM   13468 C CA  . THR   I  1 234 ? -4.22482  -14.34704 77.66858  1.000 51.11449  ?  234 THR   E CA  1 
ATOM   13469 C C   . THR   I  1 234 ? -4.56687  -12.87303 77.83627  1.000 31.34862  ?  234 THR   E C   1 
ATOM   13470 O O   . THR   I  1 234 ? -5.53912  -12.40111 77.23871  1.000 81.84628  ?  234 THR   E O   1 
ATOM   13471 C CB  . THR   I  1 234 ? -5.45991  -15.22535 77.90940  1.000 37.01104  ?  234 THR   E CB  1 
ATOM   13472 O OG1 . THR   I  1 234 ? -5.99510  -14.98751 79.21194  1.000 47.19483  ?  234 THR   E OG1 1 
ATOM   13473 C CG2 . THR   I  1 234 ? -5.09964  -16.69516 77.78024  1.000 26.99912  ?  234 THR   E CG2 1 
ATOM   13474 N N   . THR   I  1 235 ? -3.76056  -12.13208 78.58868  1.000 49.33414  ?  235 THR   E N   1 
ATOM   13475 C CA  . THR   I  1 235 ? -3.93760  -10.69447 78.72071  1.000 31.54454  ?  235 THR   E CA  1 
ATOM   13476 C C   . THR   I  1 235 ? -3.25139  -9.91190  77.61027  1.000 51.64892  ?  235 THR   E C   1 
ATOM   13477 O O   . THR   I  1 235 ? -3.31166  -8.67524  77.61945  1.000 34.90480  ?  235 THR   E O   1 
ATOM   13478 C CB  . THR   I  1 235 ? -3.40177  -10.22960 80.07561  1.000 66.69493  ?  235 THR   E CB  1 
ATOM   13479 O OG1 . THR   I  1 235 ? -1.96760  -10.11234 80.02055  1.000 27.88428  ?  235 THR   E OG1 1 
ATOM   13480 C CG2 . THR   I  1 235 ? -3.76286  -11.24041 81.13813  1.000 37.85273  ?  235 THR   E CG2 1 
ATOM   13481 N N   . LEU   I  1 236 ? -2.60970  -10.59507 76.65817  1.000 39.85042  ?  236 LEU   E N   1 
ATOM   13482 C CA  . LEU   I  1 236 ? -1.81188  -9.95613  75.61761  1.000 40.32206  ?  236 LEU   E CA  1 
ATOM   13483 C C   . LEU   I  1 236 ? -2.43475  -10.21481 74.25831  1.000 33.94030  ?  236 LEU   E C   1 
ATOM   13484 O O   . LEU   I  1 236 ? -2.94220  -11.31144 73.99731  1.000 35.65859  ?  236 LEU   E O   1 
ATOM   13485 C CB  . LEU   I  1 236 ? -0.37540  -10.47603 75.61384  1.000 33.84834  ?  236 LEU   E CB  1 
ATOM   13486 C CG  . LEU   I  1 236 ? 0.30423   -10.46073 76.98049  1.000 41.14143  ?  236 LEU   E CG  1 
ATOM   13487 C CD1 . LEU   I  1 236 ? 1.54524   -11.35458 76.95584  1.000 33.09227  ?  236 LEU   E CD1 1 
ATOM   13488 C CD2 . LEU   I  1 236 ? 0.62757   -9.02462  77.39308  1.000 23.56791  ?  236 LEU   E CD2 1 
ATOM   13489 N N   . ILE   I  1 237 ? -2.39633  -9.19882  73.39867  1.000 38.04780  ?  237 ILE   E N   1 
ATOM   13490 C CA  . ILE   I  1 237 ? -2.87860  -9.30265  72.02648  1.000 31.37432  ?  237 ILE   E CA  1 
ATOM   13491 C C   . ILE   I  1 237 ? -1.68758  -9.09928  71.09947  1.000 42.61072  ?  237 ILE   E C   1 
ATOM   13492 O O   . ILE   I  1 237 ? -0.99249  -8.07006  71.18131  1.000 29.53372  ?  237 ILE   E O   1 
ATOM   13493 C CB  . ILE   I  1 237 ? -3.99638  -8.28901  71.72309  1.000 30.19754  ?  237 ILE   E CB  1 
ATOM   13494 C CG1 . ILE   I  1 237 ? -5.17663  -8.47955  72.68389  1.000 27.11996  ?  237 ILE   E CG1 1 
ATOM   13495 C CG2 . ILE   I  1 237 ? -4.46411  -8.45024  70.26833  1.000 28.06685  ?  237 ILE   E CG2 1 
ATOM   13496 C CD1 . ILE   I  1 237 ? -6.35395  -7.53206  72.43898  1.000 29.01473  ?  237 ILE   E CD1 1 
ATOM   13497 N N   . SER   I  1 238 ? -1.46781  -10.07713 70.20914  1.000 26.71805  ?  238 SER   E N   1 
ATOM   13498 C CA  . SER   I  1 238 ? -0.32739  -10.09307 69.29516  1.000 33.48706  ?  238 SER   E CA  1 
ATOM   13499 C C   . SER   I  1 238 ? -0.64440  -9.40920  67.97282  1.000 42.23307  ?  238 SER   E C   1 
ATOM   13500 O O   . SER   I  1 238 ? -1.78790  -9.40600  67.50776  1.000 27.20525  ?  238 SER   E O   1 
ATOM   13501 C CB  . SER   I  1 238 ? 0.12114   -11.52745 68.99790  1.000 31.94961  ?  238 SER   E CB  1 
ATOM   13502 O OG  . SER   I  1 238 ? 1.00829   -11.99839 69.99055  1.000 45.73092  ?  238 SER   E OG  1 
ATOM   13503 N N   . ALA   I  1 239 ? 0.40071   -8.86172  67.35295  1.000 37.59518  ?  239 ALA   E N   1 
ATOM   13504 C CA  . ALA   I  1 239 ? 0.30793   -8.36959  65.98406  1.000 45.65037  ?  239 ALA   E CA  1 
ATOM   13505 C C   . ALA   I  1 239 ? 0.01130   -9.51105  65.02477  1.000 21.85089  ?  239 ALA   E C   1 
ATOM   13506 O O   . ALA   I  1 239 ? 0.70252   -10.53089 65.03536  1.000 37.28362  ?  239 ALA   E O   1 
ATOM   13507 C CB  . ALA   I  1 239 ? 1.61451   -7.69498  65.58727  1.000 18.22560  ?  239 ALA   E CB  1 
ATOM   13508 N N   . ALA   I  1 240 ? -0.99859  -9.32596  64.16478  1.000 37.30278  ?  240 ALA   E N   1 
ATOM   13509 C CA  . ALA   I  1 240 ? -1.40090  -10.39180 63.24479  1.000 30.92235  ?  240 ALA   E CA  1 
ATOM   13510 C C   . ALA   I  1 240 ? -0.54093  -10.46676 61.98818  1.000 37.39196  ?  240 ALA   E C   1 
ATOM   13511 O O   . ALA   I  1 240 ? -0.51125  -11.52000 61.33515  1.000 32.70746  ?  240 ALA   E O   1 
ATOM   13512 C CB  . ALA   I  1 240 ? -2.86225  -10.21678 62.83284  1.000 22.65234  ?  240 ALA   E CB  1 
ATOM   13513 N N   . CYS   I  1 241 ? 0.13584   -9.37575  61.62535  1.000 20.18861  ?  241 CYS   E N   1 
ATOM   13514 C CA  . CYS   I  1 241 ? 0.91235   -9.30617  60.39679  1.000 30.09466  ?  241 CYS   E CA  1 
ATOM   13515 C C   . CYS   I  1 241 ? 2.22975   -8.60691  60.68077  1.000 30.40448  ?  241 CYS   E C   1 
ATOM   13516 O O   . CYS   I  1 241 ? 2.27304   -7.61535  61.42094  1.000 29.40693  ?  241 CYS   E O   1 
ATOM   13517 C CB  . CYS   I  1 241 ? 0.18106   -8.54468  59.28027  1.000 31.73214  ?  241 CYS   E CB  1 
ATOM   13518 S SG  . CYS   I  1 241 ? -1.34122  -9.32964  58.71624  1.000 31.98847  ?  241 CYS   E SG  1 
ATOM   13519 N N   . GLU   I  1 242 ? 3.30171   -9.14350  60.09195  1.000 38.23382  ?  242 GLU   E N   1 
ATOM   13520 C CA  . GLU   I  1 242 ? 4.56962   -8.43627  59.98743  1.000 21.90164  ?  242 GLU   E CA  1 
ATOM   13521 C C   . GLU   I  1 242 ? 4.37462   -7.15373  59.18684  1.000 24.80343  ?  242 GLU   E C   1 
ATOM   13522 O O   . GLU   I  1 242 ? 4.11056   -7.21007  57.97795  1.000 47.38407  ?  242 GLU   E O   1 
ATOM   13523 C CB  . GLU   I  1 242 ? 5.60394   -9.33878  59.31795  1.000 32.78265  ?  242 GLU   E CB  1 
ATOM   13524 C CG  . GLU   I  1 242 ? 6.99646   -8.73378  59.18398  1.000 27.11573  ?  242 GLU   E CG  1 
ATOM   13525 C CD  . GLU   I  1 242 ? 7.77285   -8.69654  60.49575  1.000 51.12030  ?  242 GLU   E CD  1 
ATOM   13526 O OE1 . GLU   I  1 242 ? 7.40809   -9.41584  61.47032  1.000 30.59642  ?  242 GLU   E OE1 1 
ATOM   13527 O OE2 . GLU   I  1 242 ? 8.76359   -7.93151  60.53208  1.000 37.14128  -1 242 GLU   E OE2 1 
ATOM   13528 N N   . SER   I  1 243 ? 4.50264   -5.99344  59.82593  1.000 30.96707  ?  243 SER   E N   1 
ATOM   13529 C CA  . SER   I  1 243 ? 4.05352   -4.76369  59.18314  1.000 42.45053  ?  243 SER   E CA  1 
ATOM   13530 C C   . SER   I  1 243 ? 4.75051   -3.56416  59.81069  1.000 32.68270  ?  243 SER   E C   1 
ATOM   13531 O O   . SER   I  1 243 ? 5.52664   -3.69074  60.76456  1.000 37.18675  ?  243 SER   E O   1 
ATOM   13532 C CB  . SER   I  1 243 ? 2.52675   -4.61792  59.30282  1.000 31.68043  ?  243 SER   E CB  1 
ATOM   13533 O OG  . SER   I  1 243 ? 2.14333   -4.63417  60.67576  1.000 39.17663  ?  243 SER   E OG  1 
ATOM   13534 N N   . LEU   I  1 244 ? 4.43392   -2.38747  59.26567  1.000 33.59813  ?  244 LEU   E N   1 
ATOM   13535 C CA  . LEU   I  1 244 ? 4.75000   -1.09449  59.85729  1.000 39.13344  ?  244 LEU   E CA  1 
ATOM   13536 C C   . LEU   I  1 244 ? 3.46891   -0.45758  60.38804  1.000 36.63656  ?  244 LEU   E C   1 
ATOM   13537 O O   . LEU   I  1 244 ? 2.41301   -0.55676  59.75270  1.000 42.91789  ?  244 LEU   E O   1 
ATOM   13538 C CB  . LEU   I  1 244 ? 5.40221   -0.17676  58.82694  1.000 24.00143  ?  244 LEU   E CB  1 
ATOM   13539 C CG  . LEU   I  1 244 ? 6.74895   -0.64881  58.28106  1.000 42.43939  ?  244 LEU   E CG  1 
ATOM   13540 C CD1 . LEU   I  1 244 ? 7.11887   0.11702   57.03281  1.000 36.40017  ?  244 LEU   E CD1 1 
ATOM   13541 C CD2 . LEU   I  1 244 ? 7.76702   -0.43785  59.35607  1.000 29.62847  ?  244 LEU   E CD2 1 
ATOM   13542 N N   . SER   I  1 245 ? 3.55593   0.15266   61.56812  1.000 67.43354  ?  245 SER   E N   1 
ATOM   13543 C CA  . SER   I  1 245 ? 2.49458   0.99975   62.09960  1.000 28.05537  ?  245 SER   E CA  1 
ATOM   13544 C C   . SER   I  1 245 ? 1.99493   1.97150   61.02902  1.000 28.10100  ?  245 SER   E C   1 
ATOM   13545 O O   . SER   I  1 245 ? 2.79639   2.63388   60.35817  1.000 37.06399  ?  245 SER   E O   1 
ATOM   13546 C CB  . SER   I  1 245 ? 3.06399   1.76626   63.29634  1.000 30.79570  ?  245 SER   E CB  1 
ATOM   13547 O OG  . SER   I  1 245 ? 2.11810   2.63529   63.85648  1.000 76.36850  ?  245 SER   E OG  1 
ATOM   13548 N N   . TYR   I  1 246 ? 0.67020   2.05671   60.84880  1.000 40.01210  ?  246 TYR   E N   1 
ATOM   13549 C CA  . TYR   I  1 246 ? 0.14606   3.03629   59.89234  1.000 30.14871  ?  246 TYR   E CA  1 
ATOM   13550 C C   . TYR   I  1 246 ? -0.77513  4.07714   60.51566  1.000 31.76385  ?  246 TYR   E C   1 
ATOM   13551 O O   . TYR   I  1 246 ? -0.66458  5.26905   60.18501  1.000 34.82420  ?  246 TYR   E O   1 
ATOM   13552 C CB  . TYR   I  1 246 ? -0.58501  2.35659   58.72287  1.000 20.52102  ?  246 TYR   E CB  1 
ATOM   13553 C CG  . TYR   I  1 246 ? -1.01239  3.36859   57.68304  1.000 36.70198  ?  246 TYR   E CG  1 
ATOM   13554 C CD1 . TYR   I  1 246 ? -2.21856  4.07610   57.80436  1.000 29.80668  ?  246 TYR   E CD1 1 
ATOM   13555 C CD2 . TYR   I  1 246 ? -0.20179  3.63510   56.58577  1.000 15.91539  ?  246 TYR   E CD2 1 
ATOM   13556 C CE1 . TYR   I  1 246 ? -2.57994  5.01938   56.86281  1.000 23.54455  ?  246 TYR   E CE1 1 
ATOM   13557 C CE2 . TYR   I  1 246 ? -0.56208  4.57386   55.62847  1.000 42.20786  ?  246 TYR   E CE2 1 
ATOM   13558 C CZ  . TYR   I  1 246 ? -1.74290  5.26156   55.77501  1.000 33.22760  ?  246 TYR   E CZ  1 
ATOM   13559 O OH  . TYR   I  1 246 ? -2.06960  6.18375   54.82206  1.000 49.32511  ?  246 TYR   E OH  1 
ATOM   13560 N N   . ASN   I  1 247 ? -1.73029  3.65788   61.34585  1.000 28.77438  ?  247 ASN   E N   1 
ATOM   13561 C CA  . ASN   I  1 247 ? -2.64694  4.57808   62.00850  1.000 21.15835  ?  247 ASN   E CA  1 
ATOM   13562 C C   . ASN   I  1 247 ? -3.21726  3.87824   63.23121  1.000 28.23341  ?  247 ASN   E C   1 
ATOM   13563 O O   . ASN   I  1 247 ? -3.40960  2.65690   63.22732  1.000 31.46835  ?  247 ASN   E O   1 
ATOM   13564 C CB  . ASN   I  1 247 ? -3.78970  5.03284   61.09206  1.000 31.39639  ?  247 ASN   E CB  1 
ATOM   13565 C CG  . ASN   I  1 247 ? -4.84838  5.83419   61.84070  1.000 29.04546  ?  247 ASN   E CG  1 
ATOM   13566 O OD1 . ASN   I  1 247 ? -4.63329  7.00770   62.15282  1.000 46.52354  ?  247 ASN   E OD1 1 
ATOM   13567 N ND2 . ASN   I  1 247 ? -5.98481  5.19780   62.16027  1.000 27.48703  ?  247 ASN   E ND2 1 
ATOM   13568 N N   . VAL   I  1 248 ? -3.46053  4.65907   64.28589  1.000 32.44683  ?  248 VAL   E N   1 
ATOM   13569 C CA  . VAL   I  1 248 ? -4.30907  4.24039   65.39513  1.000 38.23805  ?  248 VAL   E CA  1 
ATOM   13570 C C   . VAL   I  1 248 ? -5.41036  5.27320   65.55360  1.000 29.77342  ?  248 VAL   E C   1 
ATOM   13571 O O   . VAL   I  1 248 ? -5.15063  6.47886   65.47948  1.000 37.28182  ?  248 VAL   E O   1 
ATOM   13572 C CB  . VAL   I  1 248 ? -3.51845  4.08896   66.70373  1.000 33.78741  ?  248 VAL   E CB  1 
ATOM   13573 C CG1 . VAL   I  1 248 ? -4.47607  3.96620   67.89253  1.000 26.58326  ?  248 VAL   E CG1 1 
ATOM   13574 C CG2 . VAL   I  1 248 ? -2.58840  2.89120   66.60617  1.000 31.88344  ?  248 VAL   E CG2 1 
ATOM   13575 N N   . SER   I  1 249 ? -6.64572  4.80651   65.72225  1.000 43.21066  ?  249 SER   E N   1 
ATOM   13576 C CA  . SER   I  1 249 ? -7.76511  5.71135   65.94165  1.000 30.58233  ?  249 SER   E CA  1 
ATOM   13577 C C   . SER   I  1 249 ? -8.54501  5.25132   67.15518  1.000 43.16173  ?  249 SER   E C   1 
ATOM   13578 O O   . SER   I  1 249 ? -8.76909  4.04933   67.34520  1.000 32.96352  ?  249 SER   E O   1 
ATOM   13579 C CB  . SER   I  1 249 ? -8.69106  5.79071   64.73256  1.000 30.17037  ?  249 SER   E CB  1 
ATOM   13580 O OG  . SER   I  1 249 ? -8.08057  6.53071   63.69336  1.000 35.86367  ?  249 SER   E OG  1 
ATOM   13581 N N   . TYR   I  1 250 ? -8.94821  6.21563   67.97429  1.000 29.49494  ?  250 TYR   E N   1 
ATOM   13582 C CA  . TYR   I  1 250 ? -9.77280  5.96032   69.14023  1.000 55.64197  ?  250 TYR   E CA  1 
ATOM   13583 C C   . TYR   I  1 250 ? -11.17019 6.51250   68.90493  1.000 26.89566  ?  250 TYR   E C   1 
ATOM   13584 O O   . TYR   I  1 250 ? -11.37579 7.40760   68.07022  1.000 36.00360  ?  250 TYR   E O   1 
ATOM   13585 C CB  . TYR   I  1 250 ? -9.15853  6.59356   70.39172  1.000 26.32732  ?  250 TYR   E CB  1 
ATOM   13586 C CG  . TYR   I  1 250 ? -7.77739  6.09659   70.71177  1.000 41.86290  ?  250 TYR   E CG  1 
ATOM   13587 C CD1 . TYR   I  1 250 ? -7.59280  4.89197   71.38732  1.000 28.24306  ?  250 TYR   E CD1 1 
ATOM   13588 C CD2 . TYR   I  1 250 ? -6.65551  6.81494   70.33091  1.000 24.36127  ?  250 TYR   E CD2 1 
ATOM   13589 C CE1 . TYR   I  1 250 ? -6.30881  4.42135   71.68753  1.000 40.09376  ?  250 TYR   E CE1 1 
ATOM   13590 C CE2 . TYR   I  1 250 ? -5.38106  6.35709   70.62245  1.000 35.44385  ?  250 TYR   E CE2 1 
ATOM   13591 C CZ  . TYR   I  1 250 ? -5.20496  5.16187   71.30109  1.000 47.34989  ?  250 TYR   E CZ  1 
ATOM   13592 O OH  . TYR   I  1 250 ? -3.92566  4.70090   71.59203  1.000 52.86896  ?  250 TYR   E OH  1 
ATOM   13593 N N   . ASP   I  1 251 ? -12.12628 5.95445   69.65491  1.000 38.71711  ?  251 ASP   E N   1 
ATOM   13594 C CA  . ASP   I  1 251 ? -13.52459 6.37357   69.60657  1.000 38.97534  ?  251 ASP   E CA  1 
ATOM   13595 C C   . ASP   I  1 251 ? -14.03460 6.38994   68.16249  1.000 57.62933  ?  251 ASP   E C   1 
ATOM   13596 O O   . ASP   I  1 251 ? -14.48649 7.41043   67.63592  1.000 42.49558  ?  251 ASP   E O   1 
ATOM   13597 C CB  . ASP   I  1 251 ? -13.68299 7.74665   70.26253  1.000 38.30629  ?  251 ASP   E CB  1 
ATOM   13598 C CG  . ASP   I  1 251 ? -15.13154 8.12257   70.49959  1.000 60.51641  ?  251 ASP   E CG  1 
ATOM   13599 O OD1 . ASP   I  1 251 ? -15.90046 7.22957   70.92395  1.000 46.94960  ?  251 ASP   E OD1 1 
ATOM   13600 O OD2 . ASP   I  1 251 ? -15.48260 9.31150   70.27354  1.000 46.49239  -1 251 ASP   E OD2 1 
ATOM   13601 N N   . VAL   I  1 252 ? -13.91684 5.23748   67.50411  1.000 43.27812  ?  252 VAL   E N   1 
ATOM   13602 C CA  . VAL   I  1 252 ? -14.29142 5.15297   66.09604  1.000 45.56722  ?  252 VAL   E CA  1 
ATOM   13603 C C   . VAL   I  1 252 ? -15.80793 5.10302   65.95358  1.000 46.53311  ?  252 VAL   E C   1 
ATOM   13604 O O   . VAL   I  1 252 ? -16.54313 4.69034   66.85916  1.000 48.18690  ?  252 VAL   E O   1 
ATOM   13605 C CB  . VAL   I  1 252 ? -13.63281 3.94595   65.41149  1.000 48.41471  ?  252 VAL   E CB  1 
ATOM   13606 C CG1 . VAL   I  1 252 ? -12.11485 4.11849   65.39646  1.000 36.40978  ?  252 VAL   E CG1 1 
ATOM   13607 C CG2 . VAL   I  1 252 ? -14.08440 2.63617   66.08183  1.000 36.80026  ?  252 VAL   E CG2 1 
ATOM   13608 N N   . GLN   I  1 253 ? -16.26858 5.49240   64.76938  1.000 45.10357  ?  253 GLN   E N   1 
ATOM   13609 C CA  . GLN   I  1 253 ? -17.67738 5.73737   64.51909  1.000 50.87001  ?  253 GLN   E CA  1 
ATOM   13610 C C   . GLN   I  1 253 ? -18.03775 5.31811   63.09062  1.000 62.72685  ?  253 GLN   E C   1 
ATOM   13611 O O   . GLN   I  1 253 ? -17.18635 4.88405   62.30132  1.000 50.15666  ?  253 GLN   E O   1 
ATOM   13612 C CB  . GLN   I  1 253 ? -17.97960 7.21739   64.74609  1.000 39.50026  ?  253 GLN   E CB  1 
ATOM   13613 C CG  . GLN   I  1 253 ? -17.10387 8.08754   63.86320  1.000 77.07662  ?  253 GLN   E CG  1 
ATOM   13614 C CD  . GLN   I  1 253 ? -17.37956 9.54903   64.03869  1.000 68.34057  ?  253 GLN   E CD  1 
ATOM   13615 O OE1 . GLN   I  1 253 ? -16.54295 10.39296  63.71145  1.000 69.22113  ?  253 GLN   E OE1 1 
ATOM   13616 N NE2 . GLN   I  1 253 ? -18.56048 9.86686   64.55062  1.000 76.45087  ?  253 GLN   E NE2 1 
ATOM   13617 N N   . SER   I  1 254 ? -19.31622 5.47091   62.74842  1.000 62.29326  ?  254 SER   E N   1 
ATOM   13618 C CA  . SER   I  1 254 ? -19.77878 5.25277   61.38761  1.000 42.23850  ?  254 SER   E CA  1 
ATOM   13619 C C   . SER   I  1 254 ? -20.11807 6.57885   60.70601  1.000 44.32874  ?  254 SER   E C   1 
ATOM   13620 O O   . SER   I  1 254 ? -20.54132 7.55122   61.34176  1.000 56.08630  ?  254 SER   E O   1 
ATOM   13621 C CB  . SER   I  1 254 ? -20.97877 4.31145   61.36725  1.000 53.00566  ?  254 SER   E CB  1 
ATOM   13622 O OG  . SER   I  1 254 ? -20.61122 3.04212   61.89884  1.000 44.57742  ?  254 SER   E OG  1 
ATOM   13623 N N   . LEU   I  1 255 ? -19.88732 6.61288   59.39970  1.000 43.37492  ?  255 LEU   E N   1 
ATOM   13624 C CA  . LEU   I  1 255 ? -20.16890 7.76893   58.56954  1.000 45.73658  ?  255 LEU   E CA  1 
ATOM   13625 C C   . LEU   I  1 255 ? -21.23695 7.41901   57.53627  1.000 47.27590  ?  255 LEU   E C   1 
ATOM   13626 O O   . LEU   I  1 255 ? -21.37252 6.26433   57.11934  1.000 48.52428  ?  255 LEU   E O   1 
ATOM   13627 C CB  . LEU   I  1 255 ? -18.89404 8.24180   57.87455  1.000 48.45498  ?  255 LEU   E CB  1 
ATOM   13628 C CG  . LEU   I  1 255 ? -17.76482 8.46521   58.87748  1.000 49.72694  ?  255 LEU   E CG  1 
ATOM   13629 C CD1 . LEU   I  1 255 ? -16.44811 8.77699   58.18649  1.000 48.51332  ?  255 LEU   E CD1 1 
ATOM   13630 C CD2 . LEU   I  1 255 ? -18.15059 9.57296   59.83464  1.000 38.34392  ?  255 LEU   E CD2 1 
ATOM   13631 N N   . ASP   I  1 256 ? -22.00630 8.42427   57.11566  1.000 46.56844  ?  256 ASP   E N   1 
ATOM   13632 C CA  . ASP   I  1 256 ? -22.99882 8.16086   56.07778  1.000 31.94177  ?  256 ASP   E CA  1 
ATOM   13633 C C   . ASP   I  1 256 ? -22.37914 8.16821   54.67987  1.000 54.47762  ?  256 ASP   E C   1 
ATOM   13634 O O   . ASP   I  1 256 ? -22.83859 7.40609   53.81766  1.000 34.48039  ?  256 ASP   E O   1 
ATOM   13635 C CB  . ASP   I  1 256 ? -24.15466 9.15933   56.18090  1.000 41.96700  ?  256 ASP   E CB  1 
ATOM   13636 C CG  . ASP   I  1 256 ? -25.01059 8.93308   57.42788  1.000 68.69096  ?  256 ASP   E CG  1 
ATOM   13637 O OD1 . ASP   I  1 256 ? -25.76635 7.92828   57.52165  1.000 42.50102  ?  256 ASP   E OD1 1 
ATOM   13638 O OD2 . ASP   I  1 256 ? -24.92065 9.77064   58.33420  1.000 43.18127  -1 256 ASP   E OD2 1 
ATOM   13639 N N   . THR   I  1 257 ? -21.33967 8.98736   54.44432  1.000 46.74925  ?  257 THR   E N   1 
ATOM   13640 C CA  . THR   I  1 257 ? -20.55574 8.94651   53.21290  1.000 74.93993  ?  257 THR   E CA  1 
ATOM   13641 C C   . THR   I  1 257 ? -19.07867 9.09013   53.54178  1.000 41.05722  ?  257 THR   E C   1 
ATOM   13642 O O   . THR   I  1 257 ? -18.70432 9.61622   54.59318  1.000 63.03573  ?  257 THR   E O   1 
ATOM   13643 C CB  . THR   I  1 257 ? -20.94604 10.06292  52.23632  1.000 48.09212  ?  257 THR   E CB  1 
ATOM   13644 O OG1 . THR   I  1 257 ? -20.76306 11.33456  52.87535  1.000 70.80470  ?  257 THR   E OG1 1 
ATOM   13645 C CG2 . THR   I  1 257 ? -22.36688 9.92846   51.82792  1.000 59.67797  ?  257 THR   E CG2 1 
ATOM   13646 N N   . LEU   I  1 258 ? -18.24192 8.64964   52.60212  1.000 65.08079  ?  258 LEU   E N   1 
ATOM   13647 C CA  . LEU   I  1 258 ? -16.78366 8.77939   52.72585  1.000 50.52615  ?  258 LEU   E CA  1 
ATOM   13648 C C   . LEU   I  1 258 ? -16.28884 9.92631   51.84410  1.000 77.76373  ?  258 LEU   E C   1 
ATOM   13649 O O   . LEU   I  1 258 ? -15.60639 9.73863   50.82227  1.000 81.07275  ?  258 LEU   E O   1 
ATOM   13650 C CB  . LEU   I  1 258 ? -16.09596 7.46727   52.34927  1.000 50.65663  ?  258 LEU   E CB  1 
ATOM   13651 C CG  . LEU   I  1 258 ? -16.73207 6.20092   52.90200  1.000 46.51460  ?  258 LEU   E CG  1 
ATOM   13652 C CD1 . LEU   I  1 258 ? -16.01554 5.02920   52.30120  1.000 53.70401  ?  258 LEU   E CD1 1 
ATOM   13653 C CD2 . LEU   I  1 258 ? -16.69255 6.16795   54.43153  1.000 42.92722  ?  258 LEU   E CD2 1 
ATOM   13654 N N   . VAL   I  1 259 ? -16.66696 11.13471  52.25417  1.000 67.98033  ?  259 VAL   E N   1 
ATOM   13655 C CA  . VAL   I  1 259 ? -16.40776 12.36192  51.50609  1.000 71.31805  ?  259 VAL   E CA  1 
ATOM   13656 C C   . VAL   I  1 259 ? -15.92386 13.40803  52.49078  1.000 135.46646 ?  259 VAL   E C   1 
ATOM   13657 O O   . VAL   I  1 259 ? -16.57026 13.62328  53.52988  1.000 66.97338  ?  259 VAL   E O   1 
ATOM   13658 C CB  . VAL   I  1 259 ? -17.66188 12.91358  50.79552  1.000 90.99724  ?  259 VAL   E CB  1 
ATOM   13659 C CG1 . VAL   I  1 259 ? -17.26330 13.94384  49.75472  1.000 53.12498  ?  259 VAL   E CG1 1 
ATOM   13660 C CG2 . VAL   I  1 259 ? -18.56105 11.81876  50.21579  1.000 77.50249  ?  259 VAL   E CG2 1 
ATOM   13661 N N   . PHE   I  1 260 ? -14.81412 14.08192  52.15038  1.000 74.32642  ?  260 PHE   E N   1 
ATOM   13662 C CA  . PHE   I  1 260 ? -14.32814 15.25667  52.88383  1.000 134.85964 ?  260 PHE   E CA  1 
ATOM   13663 C C   . PHE   I  1 260 ? -13.92366 14.89444  54.29474  1.000 91.93780  ?  260 PHE   E C   1 
ATOM   13664 O O   . PHE   I  1 260 ? -13.68643 15.77726  55.12951  1.000 168.27579 ?  260 PHE   E O   1 
ATOM   13665 C CB  . PHE   I  1 260 ? -15.36703 16.39680  52.95485  1.000 87.43843  ?  260 PHE   E CB  1 
ATOM   13666 C CG  . PHE   I  1 260 ? -15.77367 16.94423  51.61936  1.000 105.16332 ?  260 PHE   E CG  1 
ATOM   13667 C CD1 . PHE   I  1 260 ? -14.84234 17.08774  50.60618  1.000 82.71133  ?  260 PHE   E CD1 1 
ATOM   13668 C CD2 . PHE   I  1 260 ? -17.08609 17.31151  51.37675  1.000 98.33142  ?  260 PHE   E CD2 1 
ATOM   13669 C CE1 . PHE   I  1 260 ? -15.20642 17.58406  49.36814  1.000 181.72492 ?  260 PHE   E CE1 1 
ATOM   13670 C CE2 . PHE   I  1 260 ? -17.45856 17.81381  50.13537  1.000 99.87370  ?  260 PHE   E CE2 1 
ATOM   13671 C CZ  . PHE   I  1 260 ? -16.51165 17.94836  49.12898  1.000 116.55594 ?  260 PHE   E CZ  1 
ATOM   13672 N N   . LYS   I  1 261 ? -14.12471 13.58286  54.57668  1.000 122.22513 ?  261 LYS   E N   1 
ATOM   13673 C CA  . LYS   I  1 261 ? -13.70815 12.82100  55.75708  1.000 118.62889 ?  261 LYS   E CA  1 
ATOM   13674 C C   . LYS   I  1 261 ? -12.57917 11.81731  55.44051  1.000 131.03430 ?  261 LYS   E C   1 
ATOM   13675 O O   . LYS   I  1 261 ? -12.54412 10.74058  56.06661  1.000 133.67736 ?  261 LYS   E O   1 
ATOM   13676 C CB  . LYS   I  1 261 ? -14.86934 12.03515  56.43445  1.000 50.22304  ?  261 LYS   E CB  1 
ATOM   13677 C CG  . LYS   I  1 261 ? -16.39425 12.27570  56.14304  1.000 129.78978 ?  261 LYS   E CG  1 
ATOM   13678 C CD  . LYS   I  1 261 ? -17.04564 13.40947  56.98353  1.000 141.06933 ?  261 LYS   E CD  1 
ATOM   13679 C CE  . LYS   I  1 261 ? -18.53197 13.15014  57.30045  1.000 43.70953  ?  261 LYS   E CE  1 
ATOM   13680 N NZ  . LYS   I  1 261 ? -18.63685 12.79892  58.76168  1.000 23.82510  ?  261 LYS   E NZ  1 
ATOM   13681 N N   . GLY   I  1 262 ? -11.63722 12.16535  54.50213  1.000 102.06269 ?  262 GLY   E N   1 
ATOM   13682 C CA  . GLY   I  1 262 ? -10.64167 11.19054  54.09894  1.000 46.65643  ?  262 GLY   E CA  1 
ATOM   13683 C C   . GLY   I  1 262 ? -9.75442  10.76994  55.24163  1.000 103.51804 ?  262 GLY   E C   1 
ATOM   13684 O O   . GLY   I  1 262 ? -9.42587  11.56498  56.11638  1.000 96.84198  ?  262 GLY   E O   1 
ATOM   13685 N N   . GLU   I  1 263 ? -9.39968  9.49649   55.25622  1.000 52.63920  ?  263 GLU   E N   1 
ATOM   13686 C CA  . GLU   I  1 263 ? -8.49754  8.97612   56.28724  1.000 87.04136  ?  263 GLU   E CA  1 
ATOM   13687 C C   . GLU   I  1 263 ? -9.18748  8.96417   57.64930  1.000 97.14724  ?  263 GLU   E C   1 
ATOM   13688 O O   . GLU   I  1 263 ? -8.55123  9.16513   58.69575  1.000 61.97816  ?  263 GLU   E O   1 
ATOM   13689 C CB  . GLU   I  1 263 ? -7.17055  9.76153   56.34257  1.000 51.06129  ?  263 GLU   E CB  1 
ATOM   13690 C CG  . GLU   I  1 263 ? -5.92911  8.94184   56.67248  1.000 86.69252  ?  263 GLU   E CG  1 
ATOM   13691 C CD  . GLU   I  1 263 ? -5.48171  7.99883   55.52193  1.000 79.94165  ?  263 GLU   E CD  1 
ATOM   13692 O OE1 . GLU   I  1 263 ? -6.20960  7.89061   54.50379  1.000 50.28806  ?  263 GLU   E OE1 1 
ATOM   13693 O OE2 . GLU   I  1 263 ? -4.39685  7.36200   55.63836  1.000 64.12176  -1 263 GLU   E OE2 1 
ATOM   13694 N N   . THR   I  1 264 ? -10.50746 8.75304   57.61666  1.000 51.12221  ?  264 THR   E N   1 
ATOM   13695 C CA  . THR   I  1 264 ? -11.30009 8.40468   58.78314  1.000 36.65132  ?  264 THR   E CA  1 
ATOM   13696 C C   . THR   I  1 264 ? -11.94102 7.04701   58.55166  1.000 51.90005  ?  264 THR   E C   1 
ATOM   13697 O O   . THR   I  1 264 ? -12.43300 6.77023   57.45449  1.000 42.98045  ?  264 THR   E O   1 
ATOM   13698 C CB  . THR   I  1 264 ? -12.39939 9.42477   59.01983  1.000 57.49724  ?  264 THR   E CB  1 
ATOM   13699 O OG1 . THR   I  1 264 ? -11.83264 10.73674  59.01593  1.000 108.56807 ?  264 THR   E OG1 1 
ATOM   13700 C CG2 . THR   I  1 264 ? -13.11246 9.13659   60.33871  1.000 44.48494  ?  264 THR   E CG2 1 
ATOM   13701 N N   . TYR   I  1 265 ? -11.94107 6.19737   59.57362  1.000 35.56811  ?  265 TYR   E N   1 
ATOM   13702 C CA  . TYR   I  1 265 ? -12.71592 4.96817   59.46801  1.000 26.08237  ?  265 TYR   E CA  1 
ATOM   13703 C C   . TYR   I  1 265 ? -14.20598 5.26867   59.56751  1.000 30.92110  ?  265 TYR   E C   1 
ATOM   13704 O O   . TYR   I  1 265 ? -14.63225 6.21841   60.23932  1.000 38.94039  ?  265 TYR   E O   1 
ATOM   13705 C CB  . TYR   I  1 265 ? -12.34763 3.96419   60.56366  1.000 22.15682  ?  265 TYR   E CB  1 
ATOM   13706 C CG  . TYR   I  1 265 ? -10.89377 3.57480   60.61052  1.000 41.01502  ?  265 TYR   E CG  1 
ATOM   13707 C CD1 . TYR   I  1 265 ? -10.31698 2.85148   59.58600  1.000 32.36483  ?  265 TYR   E CD1 1 
ATOM   13708 C CD2 . TYR   I  1 265 ? -10.10551 3.91806   61.69641  1.000 29.92796  ?  265 TYR   E CD2 1 
ATOM   13709 C CE1 . TYR   I  1 265 ? -8.97563  2.48265   59.63840  1.000 40.27563  ?  265 TYR   E CE1 1 
ATOM   13710 C CE2 . TYR   I  1 265 ? -8.77804  3.56557   61.76012  1.000 38.51002  ?  265 TYR   E CE2 1 
ATOM   13711 C CZ  . TYR   I  1 265 ? -8.21269  2.84701   60.72639  1.000 32.42105  ?  265 TYR   E CZ  1 
ATOM   13712 O OH  . TYR   I  1 265 ? -6.87970  2.50462   60.79452  1.000 35.75268  ?  265 TYR   E OH  1 
ATOM   13713 N N   . SER   I  1 266 ? -14.99589 4.43684   58.88311  1.000 37.93957  ?  266 SER   E N   1 
ATOM   13714 C CA  . SER   I  1 266 ? -16.44191 4.35300   59.07173  1.000 26.99783  ?  266 SER   E CA  1 
ATOM   13715 C C   . SER   I  1 266 ? -16.75667 2.88416   59.35253  1.000 40.50608  ?  266 SER   E C   1 
ATOM   13716 O O   . SER   I  1 266 ? -16.71301 2.05346   58.43750  1.000 31.04758  ?  266 SER   E O   1 
ATOM   13717 C CB  . SER   I  1 266 ? -17.19415 4.87882   57.84908  1.000 28.75910  ?  266 SER   E CB  1 
ATOM   13718 O OG  . SER   I  1 266 ? -18.56914 4.53858   57.91731  1.000 39.30907  ?  266 SER   E OG  1 
ATOM   13719 N N   . LEU   I  1 267 ? -17.05341 2.56478   60.61980  1.000 33.30493  ?  267 LEU   E N   1 
ATOM   13720 C CA  . LEU   I  1 267 ? -17.27490 1.17412   61.02141  1.000 42.89060  ?  267 LEU   E CA  1 
ATOM   13721 C C   . LEU   I  1 267 ? -18.28384 0.47622   60.11897  1.000 32.66932  ?  267 LEU   E C   1 
ATOM   13722 O O   . LEU   I  1 267 ? -18.04974 -0.64833  59.66039  1.000 48.26579  ?  267 LEU   E O   1 
ATOM   13723 C CB  . LEU   I  1 267 ? -17.76269 1.11479   62.46293  1.000 26.34831  ?  267 LEU   E CB  1 
ATOM   13724 C CG  . LEU   I  1 267 ? -16.76567 1.23986   63.59589  1.000 45.94870  ?  267 LEU   E CG  1 
ATOM   13725 C CD1 . LEU   I  1 267 ? -17.58607 1.05556   64.82338  1.000 38.02527  ?  267 LEU   E CD1 1 
ATOM   13726 C CD2 . LEU   I  1 267 ? -15.63752 0.17515   63.50979  1.000 32.31093  ?  267 LEU   E CD2 1 
ATOM   13727 N N   . LYS   I  1 268 ? -19.43119 1.13155   59.88264  1.000 52.23333  ?  268 LYS   E N   1 
ATOM   13728 C CA  . LYS   I  1 268 ? -20.47538 0.60028   59.00541  1.000 31.08897  ?  268 LYS   E CA  1 
ATOM   13729 C C   . LYS   I  1 268 ? -19.90190 0.16508   57.64941  1.000 50.02153  ?  268 LYS   E C   1 
ATOM   13730 O O   . LYS   I  1 268 ? -20.27173 -0.89223  57.12412  1.000 29.14225  ?  268 LYS   E O   1 
ATOM   13731 C CB  . LYS   I  1 268 ? -21.57193 1.66681   58.85632  1.000 37.49593  ?  268 LYS   E CB  1 
ATOM   13732 C CG  . LYS   I  1 268 ? -22.55727 1.51123   57.71111  1.000 50.41086  ?  268 LYS   E CG  1 
ATOM   13733 C CD  . LYS   I  1 268 ? -23.17456 2.88229   57.33761  1.000 44.01189  ?  268 LYS   E CD  1 
ATOM   13734 C CE  . LYS   I  1 268 ? -24.09105 2.77841   56.08009  1.000 56.59531  ?  268 LYS   E CE  1 
ATOM   13735 N NZ  . LYS   I  1 268 ? -24.24442 4.12447   55.38143  1.000 53.37739  ?  268 LYS   E NZ  1 
ATOM   13736 N N   . HIS   I  1 269 ? -18.95974 0.94198   57.09252  1.000 37.79306  ?  269 HIS   E N   1 
ATOM   13737 C CA  . HIS   I  1 269 ? -18.32646 0.59367   55.82050  1.000 22.29541  ?  269 HIS   E CA  1 
ATOM   13738 C C   . HIS   I  1 269 ? -17.24480 -0.46354  56.00490  1.000 47.22618  ?  269 HIS   E C   1 
ATOM   13739 O O   . HIS   I  1 269 ? -17.30145 -1.52984  55.38095  1.000 29.96251  ?  269 HIS   E O   1 
ATOM   13740 C CB  . HIS   I  1 269 ? -17.71278 1.83169   55.16542  1.000 29.95767  ?  269 HIS   E CB  1 
ATOM   13741 C CG  . HIS   I  1 269 ? -18.71640 2.82750   54.68874  1.000 34.00460  ?  269 HIS   E CG  1 
ATOM   13742 N ND1 . HIS   I  1 269 ? -19.35435 3.70724   55.53477  1.000 55.36876  ?  269 HIS   E ND1 1 
ATOM   13743 C CD2 . HIS   I  1 269 ? -19.18858 3.09046   53.44771  1.000 41.27961  ?  269 HIS   E CD2 1 
ATOM   13744 C CE1 . HIS   I  1 269 ? -20.18383 4.46355   54.83638  1.000 30.59063  ?  269 HIS   E CE1 1 
ATOM   13745 N NE2 . HIS   I  1 269 ? -20.10240 4.10913   53.56732  1.000 46.13730  ?  269 HIS   E NE2 1 
ATOM   13746 N N   . LEU   I  1 270 ? -16.22841 -0.15938  56.83147  1.000 27.73949  ?  270 LEU   E N   1 
ATOM   13747 C CA  . LEU   I  1 270 ? -15.15187 -1.11442  57.11293  1.000 22.99433  ?  270 LEU   E CA  1 
ATOM   13748 C C   . LEU   I  1 270 ? -15.69725 -2.52596  57.34166  1.000 26.68219  ?  270 LEU   E C   1 
ATOM   13749 O O   . LEU   I  1 270 ? -15.28532 -3.47968  56.66746  1.000 30.23838  ?  270 LEU   E O   1 
ATOM   13750 C CB  . LEU   I  1 270 ? -14.34160 -0.65204  58.32834  1.000 29.71571  ?  270 LEU   E CB  1 
ATOM   13751 C CG  . LEU   I  1 270 ? -13.19436 -1.56543  58.75422  1.000 26.77807  ?  270 LEU   E CG  1 
ATOM   13752 C CD1 . LEU   I  1 270 ? -11.99874 -1.49088  57.78377  1.000 24.51306  ?  270 LEU   E CD1 1 
ATOM   13753 C CD2 . LEU   I  1 270 ? -12.77939 -1.25780  60.18448  1.000 32.50831  ?  270 LEU   E CD2 1 
ATOM   13754 N N   . LEU   I  1 271 ? -16.66695 -2.66893  58.24961  1.000 31.77849  ?  271 LEU   E N   1 
ATOM   13755 C CA  . LEU   I  1 271 ? -17.23020 -3.97258  58.58799  1.000 28.40538  ?  271 LEU   E CA  1 
ATOM   13756 C C   . LEU   I  1 271 ? -18.41960 -4.35958  57.71901  1.000 36.83805  ?  271 LEU   E C   1 
ATOM   13757 O O   . LEU   I  1 271 ? -19.08325 -5.36170  58.01667  1.000 26.40032  ?  271 LEU   E O   1 
ATOM   13758 C CB  . LEU   I  1 271 ? -17.63881 -4.00885  60.06147  1.000 18.86817  ?  271 LEU   E CB  1 
ATOM   13759 C CG  . LEU   I  1 271 ? -16.49893 -3.66293  61.02572  1.000 31.95753  ?  271 LEU   E CG  1 
ATOM   13760 C CD1 . LEU   I  1 271 ? -17.06044 -3.65037  62.42638  1.000 23.07435  ?  271 LEU   E CD1 1 
ATOM   13761 C CD2 . LEU   I  1 271 ? -15.29947 -4.62490  60.89641  1.000 16.60061  ?  271 LEU   E CD2 1 
ATOM   13762 N N   . ASN   I  1 272 ? -18.70999 -3.59185  56.66102  1.000 29.58359  ?  272 ASN   E N   1 
ATOM   13763 C CA  . ASN   I  1 272 ? -19.71189 -3.98225  55.65830  1.000 21.58408  ?  272 ASN   E CA  1 
ATOM   13764 C C   . ASN   I  1 272 ? -21.08032 -4.24549  56.30186  1.000 33.72097  ?  272 ASN   E C   1 
ATOM   13765 O O   . ASN   I  1 272 ? -21.74893 -5.23483  56.00678  1.000 40.51507  ?  272 ASN   E O   1 
ATOM   13766 C CB  . ASN   I  1 272 ? -19.22998 -5.20409  54.86408  1.000 43.49420  ?  272 ASN   E CB  1 
ATOM   13767 C CG  . ASN   I  1 272 ? -20.05622 -5.46591  53.61453  1.000 33.98520  ?  272 ASN   E CG  1 
ATOM   13768 O OD1 . ASN   I  1 272 ? -20.42038 -4.54129  52.87118  1.000 33.78903  ?  272 ASN   E OD1 1 
ATOM   13769 N ND2 . ASN   I  1 272 ? -20.35858 -6.74056  53.37603  1.000 40.21703  ?  272 ASN   E ND2 1 
ATOM   13770 N N   . ASN   I  1 273 ? -21.48545 -3.34733  57.21048  1.000 31.91045  ?  273 ASN   E N   1 
ATOM   13771 C CA  . ASN   I  1 273 ? -22.80071 -3.38701  57.87156  1.000 41.01683  ?  273 ASN   E CA  1 
ATOM   13772 C C   . ASN   I  1 273 ? -23.04241 -4.68230  58.63718  1.000 29.02608  ?  273 ASN   E C   1 
ATOM   13773 O O   . ASN   I  1 273 ? -24.18046 -5.14664  58.72202  1.000 37.82157  ?  273 ASN   E O   1 
ATOM   13774 C CB  . ASN   I  1 273 ? -23.94180 -3.16042  56.87530  1.000 35.50599  ?  273 ASN   E CB  1 
ATOM   13775 C CG  . ASN   I  1 273 ? -24.19154 -1.70451  56.61708  1.000 72.00953  ?  273 ASN   E CG  1 
ATOM   13776 O OD1 . ASN   I  1 273 ? -24.59161 -0.96670  57.52584  1.000 77.44638  ?  273 ASN   E OD1 1 
ATOM   13777 N ND2 . ASN   I  1 273 ? -23.94155 -1.26543  55.38156  1.000 74.67089  ?  273 ASN   E ND2 1 
ATOM   13778 N N   . ASP   I  1 274 ? -21.99760 -5.27449  59.21720  1.000 38.98677  ?  274 ASP   E N   1 
ATOM   13779 C CA  . ASP   I  1 274 ? -22.19952 -6.51535  59.95727  1.000 36.20536  ?  274 ASP   E CA  1 
ATOM   13780 C C   . ASP   I  1 274 ? -23.08995 -6.27089  61.17711  1.000 30.60290  ?  274 ASP   E C   1 
ATOM   13781 O O   . ASP   I  1 274 ? -22.99595 -5.21117  61.81710  1.000 31.43248  ?  274 ASP   E O   1 
ATOM   13782 C CB  . ASP   I  1 274 ? -20.86165 -7.11105  60.40542  1.000 32.79621  ?  274 ASP   E CB  1 
ATOM   13783 C CG  . ASP   I  1 274 ? -20.99832 -8.54857  60.86935  1.000 42.42700  ?  274 ASP   E CG  1 
ATOM   13784 O OD1 . ASP   I  1 274 ? -21.39202 -8.78599  62.04091  1.000 50.89610  ?  274 ASP   E OD1 1 
ATOM   13785 O OD2 . ASP   I  1 274 ? -20.74607 -9.44886  60.03672  1.000 64.61957  -1 274 ASP   E OD2 1 
ATOM   13786 N N   . PRO   I  1 275 ? -23.94868 -7.22677  61.54176  1.000 38.63829  ?  275 PRO   E N   1 
ATOM   13787 C CA  . PRO   I  1 275 ? -24.67635 -7.11184  62.82288  1.000 18.61128  ?  275 PRO   E CA  1 
ATOM   13788 C C   . PRO   I  1 275 ? -23.79160 -6.82085  64.03191  1.000 28.21306  ?  275 PRO   E C   1 
ATOM   13789 O O   . PRO   I  1 275 ? -24.26880 -6.14952  64.95241  1.000 41.52842  ?  275 PRO   E O   1 
ATOM   13790 C CB  . PRO   I  1 275 ? -25.38336 -8.46504  62.94869  1.000 20.83720  ?  275 PRO   E CB  1 
ATOM   13791 C CG  . PRO   I  1 275 ? -25.52352 -8.94143  61.53193  1.000 22.88361  ?  275 PRO   E CG  1 
ATOM   13792 C CD  . PRO   I  1 275 ? -24.34153 -8.41512  60.76981  1.000 26.82061  ?  275 PRO   E CD  1 
ATOM   13793 N N   . PHE   I  1 276 ? -22.51855 -7.26180  64.05922  1.000 38.62530  ?  276 PHE   E N   1 
ATOM   13794 C CA  . PHE   I  1 276 ? -21.63101 -6.91769  65.17898  1.000 28.95777  ?  276 PHE   E CA  1 
ATOM   13795 C C   . PHE   I  1 276 ? -21.20238 -5.45386  65.19170  1.000 46.04838  ?  276 PHE   E C   1 
ATOM   13796 O O   . PHE   I  1 276 ? -20.66319 -4.99899  66.21070  1.000 41.90668  ?  276 PHE   E O   1 
ATOM   13797 C CB  . PHE   I  1 276 ? -20.35784 -7.76477  65.17755  1.000 30.19602  ?  276 PHE   E CB  1 
ATOM   13798 C CG  . PHE   I  1 276 ? -20.59369 -9.22664  65.39711  1.000 45.70843  ?  276 PHE   E CG  1 
ATOM   13799 C CD1 . PHE   I  1 276 ? -21.60993 -9.66671  66.22415  1.000 38.71518  ?  276 PHE   E CD1 1 
ATOM   13800 C CD2 . PHE   I  1 276 ? -19.78699 -10.16710 64.77512  1.000 35.78135  ?  276 PHE   E CD2 1 
ATOM   13801 C CE1 . PHE   I  1 276 ? -21.81064 -11.02507 66.42980  1.000 50.49461  ?  276 PHE   E CE1 1 
ATOM   13802 C CE2 . PHE   I  1 276 ? -19.98374 -11.52786 64.96865  1.000 54.30759  ?  276 PHE   E CE2 1 
ATOM   13803 C CZ  . PHE   I  1 276 ? -20.99737 -11.95750 65.79126  1.000 44.80232  ?  276 PHE   E CZ  1 
ATOM   13804 N N   . THR   I  1 277 ? -21.40803 -4.71665  64.09836  1.000 33.71296  ?  277 THR   E N   1 
ATOM   13805 C CA  . THR   I  1 277 ? -20.89504 -3.34878  64.00254  1.000 39.43664  ?  277 THR   E CA  1 
ATOM   13806 C C   . THR   I  1 277 ? -21.19001 -2.48787  65.22702  1.000 31.01385  ?  277 THR   E C   1 
ATOM   13807 O O   . THR   I  1 277 ? -20.26985 -1.80299  65.69785  1.000 37.07497  ?  277 THR   E O   1 
ATOM   13808 C CB  . THR   I  1 277 ? -21.44304 -2.67570  62.73461  1.000 28.18058  ?  277 THR   E CB  1 
ATOM   13809 O OG1 . THR   I  1 277 ? -21.17044 -3.50496  61.60085  1.000 34.41722  ?  277 THR   E OG1 1 
ATOM   13810 C CG2 . THR   I  1 277 ? -20.78035 -1.32157  62.51697  1.000 18.17621  ?  277 THR   E CG2 1 
ATOM   13811 N N   . PRO   I  1 278 ? -22.40743 -2.47115  65.79076  1.000 56.30912  ?  278 PRO   E N   1 
ATOM   13812 C CA  . PRO   I  1 278 ? -22.65597 -1.57668  66.93628  1.000 29.00122  ?  278 PRO   E CA  1 
ATOM   13813 C C   . PRO   I  1 278 ? -21.75254 -1.83985  68.12981  1.000 43.00813  ?  278 PRO   E C   1 
ATOM   13814 O O   . PRO   I  1 278 ? -21.44755 -0.89073  68.86614  1.000 31.57057  ?  278 PRO   E O   1 
ATOM   13815 C CB  . PRO   I  1 278 ? -24.12547 -1.84847  67.28974  1.000 21.73641  ?  278 PRO   E CB  1 
ATOM   13816 C CG  . PRO   I  1 278 ? -24.71832 -2.44421  66.10214  1.000 25.51128  ?  278 PRO   E CG  1 
ATOM   13817 C CD  . PRO   I  1 278 ? -23.62865 -3.20057  65.40061  1.000 28.42121  ?  278 PRO   E CD  1 
ATOM   13818 N N   . GLN   I  1 279 ? -21.31545 -3.09473  68.34420  1.000 32.99239  ?  279 GLN   E N   1 
ATOM   13819 C CA  . GLN   I  1 279 ? -20.45784 -3.41686  69.48881  1.000 30.80657  ?  279 GLN   E CA  1 
ATOM   13820 C C   . GLN   I  1 279 ? -19.11219 -2.69297  69.44205  1.000 44.20868  ?  279 GLN   E C   1 
ATOM   13821 O O   . GLN   I  1 279 ? -18.46759 -2.53396  70.49030  1.000 42.59978  ?  279 GLN   E O   1 
ATOM   13822 C CB  . GLN   I  1 279 ? -20.21159 -4.92930  69.57782  1.000 28.24421  ?  279 GLN   E CB  1 
ATOM   13823 C CG  . GLN   I  1 279 ? -21.46346 -5.77504  69.81010  1.000 19.74678  ?  279 GLN   E CG  1 
ATOM   13824 C CD  . GLN   I  1 279 ? -21.14412 -7.23401  70.10033  1.000 59.27292  ?  279 GLN   E CD  1 
ATOM   13825 O OE1 . GLN   I  1 279 ? -20.30188 -7.54735  70.94877  1.000 45.10386  ?  279 GLN   E OE1 1 
ATOM   13826 N NE2 . GLN   I  1 279 ? -21.82077 -8.13370  69.39645  1.000 36.12776  ?  279 GLN   E NE2 1 
ATOM   13827 N N   . PHE   I  1 280 ? -18.67449 -2.26121  68.25521  1.000 37.40574  ?  280 PHE   E N   1 
ATOM   13828 C CA  . PHE   I  1 280 ? -17.37877 -1.62276  68.07408  1.000 38.98354  ?  280 PHE   E CA  1 
ATOM   13829 C C   . PHE   I  1 280 ? -17.48809 -0.11730  67.97253  1.000 37.30599  ?  280 PHE   E C   1 
ATOM   13830 O O   . PHE   I  1 280 ? -16.45638 0.56243   67.85692  1.000 39.97947  ?  280 PHE   E O   1 
ATOM   13831 C CB  . PHE   I  1 280 ? -16.67239 -2.20219  66.84263  1.000 20.89728  ?  280 PHE   E CB  1 
ATOM   13832 C CG  . PHE   I  1 280 ? -16.22040 -3.59708  67.06133  1.000 50.82311  ?  280 PHE   E CG  1 
ATOM   13833 C CD1 . PHE   I  1 280 ? -14.99534 -3.85838  67.67229  1.000 31.52318  ?  280 PHE   E CD1 1 
ATOM   13834 C CD2 . PHE   I  1 280 ? -17.05817 -4.65474  66.75718  1.000 21.84740  ?  280 PHE   E CD2 1 
ATOM   13835 C CE1 . PHE   I  1 280 ? -14.60386 -5.15983  67.92070  1.000 46.24067  ?  280 PHE   E CE1 1 
ATOM   13836 C CE2 . PHE   I  1 280 ? -16.66668 -5.96126  67.00414  1.000 45.55196  ?  280 PHE   E CE2 1 
ATOM   13837 C CZ  . PHE   I  1 280 ? -15.43994 -6.21183  67.58865  1.000 37.92631  ?  280 PHE   E CZ  1 
ATOM   13838 N N   . GLU   I  1 281 ? -18.70976 0.41223   68.01876  1.000 39.28282  ?  281 GLU   E N   1 
ATOM   13839 C CA  . GLU   I  1 281 ? -18.90222 1.84852   68.10966  1.000 52.12700  ?  281 GLU   E CA  1 
ATOM   13840 C C   . GLU   I  1 281 ? -18.16631 2.38583   69.33614  1.000 29.37437  ?  281 GLU   E C   1 
ATOM   13841 O O   . GLU   I  1 281 ? -18.24078 1.79771   70.41839  1.000 49.07176  ?  281 GLU   E O   1 
ATOM   13842 C CB  . GLU   I  1 281 ? -20.39911 2.14987   68.17498  1.000 32.64241  ?  281 GLU   E CB  1 
ATOM   13843 C CG  . GLU   I  1 281 ? -20.78715 3.44315   67.50991  1.000 64.62020  ?  281 GLU   E CG  1 
ATOM   13844 C CD  . GLU   I  1 281 ? -20.71097 3.37589   65.99588  1.000 132.82725 ?  281 GLU   E CD  1 
ATOM   13845 O OE1 . GLU   I  1 281 ? -21.10292 2.34210   65.38670  1.000 51.97172  ?  281 GLU   E OE1 1 
ATOM   13846 O OE2 . GLU   I  1 281 ? -20.25707 4.38374   65.41668  1.000 67.94581  -1 281 GLU   E OE2 1 
ATOM   13847 N N   . HIS   I  1 282 ? -17.40089 3.46575   69.14641  1.000 41.28666  ?  282 HIS   E N   1 
ATOM   13848 C CA  . HIS   I  1 282 ? -16.56334 4.10568   70.16130  1.000 64.87205  ?  282 HIS   E CA  1 
ATOM   13849 C C   . HIS   I  1 282 ? -15.32146 3.29688   70.52453  1.000 52.45368  ?  282 HIS   E C   1 
ATOM   13850 O O   . HIS   I  1 282 ? -14.58312 3.70457   71.42753  1.000 57.67990  ?  282 HIS   E O   1 
ATOM   13851 C CB  . HIS   I  1 282 ? -17.32280 4.38715   71.46125  1.000 32.37947  ?  282 HIS   E CB  1 
ATOM   13852 C CG  . HIS   I  1 282 ? -18.50925 5.27742   71.29111  1.000 79.11863  ?  282 HIS   E CG  1 
ATOM   13853 N ND1 . HIS   I  1 282 ? -18.39597 6.63055   71.04916  1.000 63.82913  ?  282 HIS   E ND1 1 
ATOM   13854 C CD2 . HIS   I  1 282 ? -19.83644 5.01032   71.33743  1.000 39.38674  ?  282 HIS   E CD2 1 
ATOM   13855 C CE1 . HIS   I  1 282 ? -19.60252 7.15842   70.94290  1.000 47.72792  ?  282 HIS   E CE1 1 
ATOM   13856 N NE2 . HIS   I  1 282 ? -20.49519 6.19683   71.11444  1.000 59.68674  ?  282 HIS   E NE2 1 
ATOM   13857 N N   . GLY   I  1 283 ? -15.06623 2.16480   69.86352  1.000 46.02055  ?  283 GLY   E N   1 
ATOM   13858 C CA  . GLY   I  1 283 ? -13.88569 1.36339   70.13369  1.000 25.57834  ?  283 GLY   E CA  1 
ATOM   13859 C C   . GLY   I  1 283 ? -12.63933 1.92763   69.47704  1.000 37.75382  ?  283 GLY   E C   1 
ATOM   13860 O O   . GLY   I  1 283 ? -12.61082 3.10773   69.10600  1.000 36.79596  ?  283 GLY   E O   1 
ATOM   13861 N N   . SER   I  1 284 ? -11.60204 1.10747   69.31307  1.000 30.68281  ?  284 SER   E N   1 
ATOM   13862 C CA  . SER   I  1 284 ? -10.34371 1.60055   68.76053  1.000 39.38854  ?  284 SER   E CA  1 
ATOM   13863 C C   . SER   I  1 284 ? -9.83560  0.63624   67.70224  1.000 33.39526  ?  284 SER   E C   1 
ATOM   13864 O O   . SER   I  1 284 ? -10.16154 -0.56039  67.70069  1.000 26.33112  ?  284 SER   E O   1 
ATOM   13865 C CB  . SER   I  1 284 ? -9.27298  1.79765   69.85306  1.000 22.43369  ?  284 SER   E CB  1 
ATOM   13866 O OG  . SER   I  1 284 ? -9.24580  0.66941   70.72794  1.000 41.15442  ?  284 SER   E OG  1 
ATOM   13867 N N   . ILE   I  1 285 ? -9.00797  1.17360   66.80936  1.000 26.36023  ?  285 ILE   E N   1 
ATOM   13868 C CA  . ILE   I  1 285 ? -8.49224  0.43621   65.66294  1.000 25.10243  ?  285 ILE   E CA  1 
ATOM   13869 C C   . ILE   I  1 285 ? -7.00528  0.73593   65.52217  1.000 21.25995  ?  285 ILE   E C   1 
ATOM   13870 O O   . ILE   I  1 285 ? -6.59641  1.90564   65.53299  1.000 40.25481  ?  285 ILE   E O   1 
ATOM   13871 C CB  . ILE   I  1 285 ? -9.22863  0.81323   64.35611  1.000 28.50676  ?  285 ILE   E CB  1 
ATOM   13872 C CG1 . ILE   I  1 285 ? -10.70524 0.39057   64.37569  1.000 24.99635  ?  285 ILE   E CG1 1 
ATOM   13873 C CG2 . ILE   I  1 285 ? -8.50079  0.23850   63.16759  1.000 20.93899  ?  285 ILE   E CG2 1 
ATOM   13874 C CD1 . ILE   I  1 285 ? -11.51240 0.95787   63.20401  1.000 33.28577  ?  285 ILE   E CD1 1 
ATOM   13875 N N   . LEU   I  1 286 ? -6.20544  -0.31970  65.37859  1.000 38.19444  ?  286 LEU   E N   1 
ATOM   13876 C CA  . LEU   I  1 286 ? -4.80627  -0.23918  64.97791  1.000 21.06345  ?  286 LEU   E CA  1 
ATOM   13877 C C   . LEU   I  1 286 ? -4.68233  -0.83460  63.58036  1.000 27.96341  ?  286 LEU   E C   1 
ATOM   13878 O O   . LEU   I  1 286 ? -5.19261  -1.93533  63.33007  1.000 32.67832  ?  286 LEU   E O   1 
ATOM   13879 C CB  . LEU   I  1 286 ? -3.89973  -0.99588  65.97147  1.000 36.24977  ?  286 LEU   E CB  1 
ATOM   13880 C CG  . LEU   I  1 286 ? -2.53783  -1.45540  65.40968  1.000 31.91210  ?  286 LEU   E CG  1 
ATOM   13881 C CD1 . LEU   I  1 286 ? -1.64332  -0.26778  65.15296  1.000 26.87225  ?  286 LEU   E CD1 1 
ATOM   13882 C CD2 . LEU   I  1 286 ? -1.82618  -2.44689  66.31419  1.000 32.10982  ?  286 LEU   E CD2 1 
ATOM   13883 N N   . GLN   I  1 287 ? -4.00298  -0.11932  62.67937  1.000 20.43134  ?  287 GLN   E N   1 
ATOM   13884 C CA  . GLN   I  1 287 ? -3.85286  -0.54774  61.29147  1.000 34.49368  ?  287 GLN   E CA  1 
ATOM   13885 C C   . GLN   I  1 287 ? -2.37786  -0.56037  60.90395  1.000 35.17376  ?  287 GLN   E C   1 
ATOM   13886 O O   . GLN   I  1 287 ? -1.65518  0.41990   61.13641  1.000 28.74134  ?  287 GLN   E O   1 
ATOM   13887 C CB  . GLN   I  1 287 ? -4.64183  0.35985   60.32794  1.000 23.53736  ?  287 GLN   E CB  1 
ATOM   13888 C CG  . GLN   I  1 287 ? -4.46164  -0.00367  58.86205  1.000 31.44693  ?  287 GLN   E CG  1 
ATOM   13889 C CD  . GLN   I  1 287 ? -5.38949  0.75110   57.91433  1.000 28.70708  ?  287 GLN   E CD  1 
ATOM   13890 O OE1 . GLN   I  1 287 ? -6.10638  1.67271   58.31252  1.000 30.84568  ?  287 GLN   E OE1 1 
ATOM   13891 N NE2 . GLN   I  1 287 ? -5.37319  0.35542   56.63897  1.000 24.82291  ?  287 GLN   E NE2 1 
ATOM   13892 N N   . GLY   I  1 288 ? -1.94034  -1.66735  60.30098  1.000 30.23196  ?  288 GLY   E N   1 
ATOM   13893 C CA  . GLY   I  1 288 ? -0.57883  -1.80850  59.81078  1.000 22.06122  ?  288 GLY   E CA  1 
ATOM   13894 C C   . GLY   I  1 288 ? -0.46984  -1.93070  58.29424  1.000 26.67900  ?  288 GLY   E C   1 
ATOM   13895 O O   . GLY   I  1 288 ? -1.43003  -2.28677  57.59900  1.000 41.71605  ?  288 GLY   E O   1 
ATOM   13896 N N   . PHE   I  1 289 ? 0.70622   -1.61767  57.76787  1.000 34.15399  ?  289 PHE   E N   1 
ATOM   13897 C CA  . PHE   I  1 289 ? 1.00548   -1.72794  56.34887  1.000 40.70677  ?  289 PHE   E CA  1 
ATOM   13898 C C   . PHE   I  1 289 ? 2.12188   -2.74443  56.17245  1.000 36.00682  ?  289 PHE   E C   1 
ATOM   13899 O O   . PHE   I  1 289 ? 3.14022   -2.66687  56.86439  1.000 38.39975  ?  289 PHE   E O   1 
ATOM   13900 C CB  . PHE   I  1 289 ? 1.42432   -0.36973  55.78700  1.000 29.74739  ?  289 PHE   E CB  1 
ATOM   13901 C CG  . PHE   I  1 289 ? 2.10252   -0.43765  54.44283  1.000 35.43093  ?  289 PHE   E CG  1 
ATOM   13902 C CD1 . PHE   I  1 289 ? 1.43641   -0.94721  53.33657  1.000 24.21810  ?  289 PHE   E CD1 1 
ATOM   13903 C CD2 . PHE   I  1 289 ? 3.39543   0.03512   54.27446  1.000 34.87155  ?  289 PHE   E CD2 1 
ATOM   13904 C CE1 . PHE   I  1 289 ? 2.05649   -0.99230  52.07483  1.000 42.86075  ?  289 PHE   E CE1 1 
ATOM   13905 C CE2 . PHE   I  1 289 ? 4.01478   -0.00380  53.02004  1.000 38.22693  ?  289 PHE   E CE2 1 
ATOM   13906 C CZ  . PHE   I  1 289 ? 3.33961   -0.51501  51.91900  1.000 36.52672  ?  289 PHE   E CZ  1 
ATOM   13907 N N   . LEU   I  1 290 ? 1.92347   -3.69613  55.26155  1.000 31.92780  ?  290 LEU   E N   1 
ATOM   13908 C CA  . LEU   I  1 290 ? 2.92625   -4.70465  54.93713  1.000 31.29814  ?  290 LEU   E CA  1 
ATOM   13909 C C   . LEU   I  1 290 ? 3.69960   -4.26385  53.69149  1.000 35.66619  ?  290 LEU   E C   1 
ATOM   13910 O O   . LEU   I  1 290 ? 3.09413   -4.06941  52.63316  1.000 55.29180  ?  290 LEU   E O   1 
ATOM   13911 C CB  . LEU   I  1 290 ? 2.25390   -6.06137  54.70445  1.000 24.43547  ?  290 LEU   E CB  1 
ATOM   13912 C CG  . LEU   I  1 290 ? 1.54111   -6.83419  55.83220  1.000 32.18923  ?  290 LEU   E CG  1 
ATOM   13913 C CD1 . LEU   I  1 290 ? 0.21446   -6.19581  56.22635  1.000 29.83669  ?  290 LEU   E CD1 1 
ATOM   13914 C CD2 . LEU   I  1 290 ? 1.31976   -8.31763  55.47073  1.000 24.25912  ?  290 LEU   E CD2 1 
ATOM   13915 N N   . ASN   I  1 291 ? 5.02922   -4.10722  53.80882  1.000 44.55208  ?  291 ASN   E N   1 
ATOM   13916 C CA  . ASN   I  1 291 ? 5.87486   -3.81852  52.63734  1.000 31.97308  ?  291 ASN   E CA  1 
ATOM   13917 C C   . ASN   I  1 291 ? 5.80410   -4.95846  51.63405  1.000 36.49330  ?  291 ASN   E C   1 
ATOM   13918 O O   . ASN   I  1 291 ? 5.38296   -6.07862  51.94904  1.000 36.11120  ?  291 ASN   E O   1 
ATOM   13919 C CB  . ASN   I  1 291 ? 7.35568   -3.63891  52.99910  1.000 59.03167  ?  291 ASN   E CB  1 
ATOM   13920 C CG  . ASN   I  1 291 ? 7.55400   -2.94356  54.30747  1.000 70.00125  ?  291 ASN   E CG  1 
ATOM   13921 O OD1 . ASN   I  1 291 ? 7.45953   -3.56067  55.37302  1.000 115.80378 ?  291 ASN   E OD1 1 
ATOM   13922 N ND2 . ASN   I  1 291 ? 7.83134   -1.64735  54.24769  1.000 70.71694  ?  291 ASN   E ND2 1 
ATOM   13923 N N   . VAL   I  1 292 ? 6.27077   -4.67823  50.41462  1.000 29.79395  ?  292 VAL   E N   1 
ATOM   13924 C CA  . VAL   I  1 292 ? 6.16882   -5.70462  49.38594  1.000 57.76603  ?  292 VAL   E CA  1 
ATOM   13925 C C   . VAL   I  1 292 ? 7.07112   -6.89220  49.70491  1.000 58.50691  ?  292 VAL   E C   1 
ATOM   13926 O O   . VAL   I  1 292 ? 6.77283   -8.02665  49.30478  1.000 40.88185  ?  292 VAL   E O   1 
ATOM   13927 C CB  . VAL   I  1 292 ? 6.47210   -5.11984  48.00082  1.000 56.08599  ?  292 VAL   E CB  1 
ATOM   13928 C CG1 . VAL   I  1 292 ? 5.84654   -6.01950  46.93515  1.000 48.94435  ?  292 VAL   E CG1 1 
ATOM   13929 C CG2 . VAL   I  1 292 ? 5.96762   -3.66401  47.90985  1.000 40.86360  ?  292 VAL   E CG2 1 
ATOM   13930 N N   . THR   I  1 293 ? 8.15822   -6.67291  50.45103  1.000 34.78212  ?  293 THR   E N   1 
ATOM   13931 C CA  . THR   I  1 293 ? 9.07955   -7.74678  50.81323  1.000 41.17099  ?  293 THR   E CA  1 
ATOM   13932 C C   . THR   I  1 293 ? 8.76875   -8.41212  52.15708  1.000 68.43316  ?  293 THR   E C   1 
ATOM   13933 O O   . THR   I  1 293 ? 9.57012   -9.23258  52.62030  1.000 55.68289  ?  293 THR   E O   1 
ATOM   13934 C CB  . THR   I  1 293 ? 10.51420  -7.22137  50.87295  1.000 65.74278  ?  293 THR   E CB  1 
ATOM   13935 O OG1 . THR   I  1 293 ? 10.59373  -6.12594  51.81008  1.000 43.76644  ?  293 THR   E OG1 1 
ATOM   13936 C CG2 . THR   I  1 293 ? 10.97307  -6.79252  49.49921  1.000 34.44008  ?  293 THR   E CG2 1 
ATOM   13937 N N   . ALA   I  1 294 ? 7.65161   -8.08000  52.79962  1.000 37.24835  ?  294 ALA   E N   1 
ATOM   13938 C CA  . ALA   I  1 294 ? 7.39413   -8.59588  54.13541  1.000 30.60492  ?  294 ALA   E CA  1 
ATOM   13939 C C   . ALA   I  1 294 ? 6.77287   -9.99730  54.09520  1.000 30.05360  ?  294 ALA   E C   1 
ATOM   13940 O O   . ALA   I  1 294 ? 6.24037   -10.46386 53.08328  1.000 47.52869  ?  294 ALA   E O   1 
ATOM   13941 C CB  . ALA   I  1 294 ? 6.48993   -7.64444  54.92573  1.000 28.95328  ?  294 ALA   E CB  1 
ATOM   13942 N N   . TYR   I  1 295 ? 6.90610   -10.68802 55.21619  1.000 32.26948  ?  295 TYR   E N   1 
ATOM   13943 C CA  . TYR   I  1 295 ? 6.14631   -11.90061 55.44499  1.000 39.71623  ?  295 TYR   E CA  1 
ATOM   13944 C C   . TYR   I  1 295 ? 4.66213   -11.57642 55.29088  1.000 37.64293  ?  295 TYR   E C   1 
ATOM   13945 O O   . TYR   I  1 295 ? 4.17323   -10.58697 55.84258  1.000 34.56804  ?  295 TYR   E O   1 
ATOM   13946 C CB  . TYR   I  1 295 ? 6.49856   -12.40387 56.84594  1.000 12.92688  ?  295 TYR   E CB  1 
ATOM   13947 C CG  . TYR   I  1 295 ? 5.77193   -13.61306 57.38587  1.000 42.72109  ?  295 TYR   E CG  1 
ATOM   13948 C CD1 . TYR   I  1 295 ? 6.25381   -14.91413 57.16311  1.000 30.97537  ?  295 TYR   E CD1 1 
ATOM   13949 C CD2 . TYR   I  1 295 ? 4.65310   -13.45351 58.19378  1.000 26.83881  ?  295 TYR   E CD2 1 
ATOM   13950 C CE1 . TYR   I  1 295 ? 5.59403   -16.03081 57.70129  1.000 23.87352  ?  295 TYR   E CE1 1 
ATOM   13951 C CE2 . TYR   I  1 295 ? 3.99302   -14.54188 58.73058  1.000 21.89638  ?  295 TYR   E CE2 1 
ATOM   13952 C CZ  . TYR   I  1 295 ? 4.46000   -15.83367 58.48851  1.000 36.18456  ?  295 TYR   E CZ  1 
ATOM   13953 O OH  . TYR   I  1 295 ? 3.78320   -16.91393 59.03174  1.000 27.19100  ?  295 TYR   E OH  1 
ATOM   13954 N N   . HIS   I  1 296 ? 3.94281   -12.37211 54.49914  1.000 29.56614  ?  296 HIS   E N   1 
ATOM   13955 C CA  . HIS   I  1 296 ? 2.56383   -12.02388 54.15954  1.000 37.79439  ?  296 HIS   E CA  1 
ATOM   13956 C C   . HIS   I  1 296 ? 1.52440   -13.00914 54.69799  1.000 22.38297  ?  296 HIS   E C   1 
ATOM   13957 O O   . HIS   I  1 296 ? 0.39439   -13.04916 54.18388  1.000 28.28353  ?  296 HIS   E O   1 
ATOM   13958 C CB  . HIS   I  1 296 ? 2.40990   -11.85268 52.64100  1.000 26.78146  ?  296 HIS   E CB  1 
ATOM   13959 C CG  . HIS   I  1 296 ? 2.50980   -10.42106 52.19801  1.000 36.67525  ?  296 HIS   E CG  1 
ATOM   13960 N ND1 . HIS   I  1 296 ? 3.71666   -9.77688  52.03101  1.000 44.49115  ?  296 HIS   E ND1 1 
ATOM   13961 C CD2 . HIS   I  1 296 ? 1.55407   -9.49272  51.95161  1.000 36.12157  ?  296 HIS   E CD2 1 
ATOM   13962 C CE1 . HIS   I  1 296 ? 3.50177   -8.52015  51.68580  1.000 36.52363  ?  296 HIS   E CE1 1 
ATOM   13963 N NE2 . HIS   I  1 296 ? 2.19719   -8.32221  51.62727  1.000 50.42982  ?  296 HIS   E NE2 1 
ATOM   13964 N N   . ARG   I  1 297 ? 1.85306   -13.78278 55.73205  1.000 29.15986  ?  297 ARG   E N   1 
ATOM   13965 C CA  . ARG   I  1 297 ? 0.83292   -14.62537 56.34199  1.000 24.58472  ?  297 ARG   E CA  1 
ATOM   13966 C C   . ARG   I  1 297 ? 0.20631   -13.91271 57.53447  1.000 41.56201  ?  297 ARG   E C   1 
ATOM   13967 O O   . ARG   I  1 297 ? 0.71732   -12.89891 58.01723  1.000 31.20811  ?  297 ARG   E O   1 
ATOM   13968 C CB  . ARG   I  1 297 ? 1.40874   -15.96410 56.77283  1.000 28.46602  ?  297 ARG   E CB  1 
ATOM   13969 C CG  . ARG   I  1 297 ? 2.21344   -16.65496 55.70214  1.000 33.48534  ?  297 ARG   E CG  1 
ATOM   13970 C CD  . ARG   I  1 297 ? 2.62493   -18.02453 56.20496  1.000 30.34905  ?  297 ARG   E CD  1 
ATOM   13971 N NE  . ARG   I  1 297 ? 2.42858   -19.04003 55.17785  1.000 47.85601  ?  297 ARG   E NE  1 
ATOM   13972 C CZ  . ARG   I  1 297 ? 1.50041   -19.98202 55.24065  1.000 40.17641  ?  297 ARG   E CZ  1 
ATOM   13973 N NH1 . ARG   I  1 297 ? 0.70896   -20.09984 56.30175  1.000 48.55159  ?  297 ARG   E NH1 1 
ATOM   13974 N NH2 . ARG   I  1 297 ? 1.36696   -20.82825 54.22070  1.000 83.85357  ?  297 ARG   E NH2 1 
ATOM   13975 N N   . TRP   I  1 298 ? -0.93442  -14.44224 57.98539  1.000 29.42747  ?  298 TRP   E N   1 
ATOM   13976 C CA  . TRP   I  1 298 ? -1.66630  -13.91365 59.12537  1.000 27.27584  ?  298 TRP   E CA  1 
ATOM   13977 C C   . TRP   I  1 298 ? -1.52464  -14.86893 60.30160  1.000 35.19561  ?  298 TRP   E C   1 
ATOM   13978 O O   . TRP   I  1 298 ? -1.64458  -16.08997 60.14250  1.000 39.23330  ?  298 TRP   E O   1 
ATOM   13979 C CB  . TRP   I  1 298 ? -3.16504  -13.74094 58.83075  1.000 21.45474  ?  298 TRP   E CB  1 
ATOM   13980 C CG  . TRP   I  1 298 ? -3.54635  -13.16434 57.49674  1.000 32.18618  ?  298 TRP   E CG  1 
ATOM   13981 C CD1 . TRP   I  1 298 ? -2.79113  -12.35372 56.68406  1.000 27.45661  ?  298 TRP   E CD1 1 
ATOM   13982 C CD2 . TRP   I  1 298 ? -4.79961  -13.35859 56.81647  1.000 21.56865  ?  298 TRP   E CD2 1 
ATOM   13983 N NE1 . TRP   I  1 298 ? -3.49680  -12.04860 55.53488  1.000 18.86554  ?  298 TRP   E NE1 1 
ATOM   13984 C CE2 . TRP   I  1 298 ? -4.73195  -12.64545 55.59971  1.000 25.16349  ?  298 TRP   E CE2 1 
ATOM   13985 C CE3 . TRP   I  1 298 ? -5.96371  -14.08327 57.11285  1.000 14.63160  ?  298 TRP   E CE3 1 
ATOM   13986 C CZ2 . TRP   I  1 298 ? -5.78696  -12.63447 54.68477  1.000 30.28904  ?  298 TRP   E CZ2 1 
ATOM   13987 C CZ3 . TRP   I  1 298 ? -7.00438  -14.06467 56.21388  1.000 36.53518  ?  298 TRP   E CZ3 1 
ATOM   13988 C CH2 . TRP   I  1 298 ? -6.91201  -13.34540 55.01160  1.000 28.09056  ?  298 TRP   E CH2 1 
ATOM   13989 N N   . HIS   I  1 299 ? -1.31433  -14.30533 61.48381  1.000 31.56710  ?  299 HIS   E N   1 
ATOM   13990 C CA  . HIS   I  1 299 ? -1.26507  -15.06331 62.72180  1.000 40.44515  ?  299 HIS   E CA  1 
ATOM   13991 C C   . HIS   I  1 299 ? -2.41133  -14.63694 63.62821  1.000 30.60018  ?  299 HIS   E C   1 
ATOM   13992 O O   . HIS   I  1 299 ? -2.87590  -13.49291 63.56552  1.000 32.69377  ?  299 HIS   E O   1 
ATOM   13993 C CB  . HIS   I  1 299 ? 0.07017   -14.86967 63.45753  1.000 19.77751  ?  299 HIS   E CB  1 
ATOM   13994 C CG  . HIS   I  1 299 ? 1.24977   -15.45722 62.74337  1.000 36.69602  ?  299 HIS   E CG  1 
ATOM   13995 N ND1 . HIS   I  1 299 ? 2.53390   -15.39071 63.24225  1.000 29.74079  ?  299 HIS   E ND1 1 
ATOM   13996 C CD2 . HIS   I  1 299 ? 1.33789   -16.10937 61.55983  1.000 30.04273  ?  299 HIS   E CD2 1 
ATOM   13997 C CE1 . HIS   I  1 299 ? 3.36108   -15.97833 62.39589  1.000 43.47100  ?  299 HIS   E CE1 1 
ATOM   13998 N NE2 . HIS   I  1 299 ? 2.65946   -16.42293 61.36691  1.000 31.83193  ?  299 HIS   E NE2 1 
ATOM   13999 N N   . ALA   I  1 300 ? -2.85461  -15.56695 64.48176  1.000 29.71978  ?  300 ALA   E N   1 
ATOM   14000 C CA  . ALA   I  1 300 ? -3.96083  -15.28371 65.39447  1.000 34.75530  ?  300 ALA   E CA  1 
ATOM   14001 C C   . ALA   I  1 300 ? -3.50220  -14.32045 66.48231  1.000 27.74020  ?  300 ALA   E C   1 
ATOM   14002 O O   . ALA   I  1 300 ? -2.46842  -14.55974 67.11864  1.000 37.94024  ?  300 ALA   E O   1 
ATOM   14003 C CB  . ALA   I  1 300 ? -4.48146  -16.56983 66.02295  1.000 23.29473  ?  300 ALA   E CB  1 
ATOM   14004 N N   . PRO   I  1 301 ? -4.22697  -13.22121 66.71825  1.000 39.56482  ?  301 PRO   E N   1 
ATOM   14005 C CA  . PRO   I  1 301 ? -3.77546  -12.22765 67.71155  1.000 25.40558  ?  301 PRO   E CA  1 
ATOM   14006 C C   . PRO   I  1 301 ? -4.09672  -12.59309 69.15539  1.000 46.19191  ?  301 PRO   E C   1 
ATOM   14007 O O   . PRO   I  1 301 ? -3.55727  -11.95284 70.07019  1.000 30.59149  ?  301 PRO   E O   1 
ATOM   14008 C CB  . PRO   I  1 301 ? -4.52175  -10.95174 67.28487  1.000 34.30334  ?  301 PRO   E CB  1 
ATOM   14009 C CG  . PRO   I  1 301 ? -5.78082  -11.45983 66.64508  1.000 31.55291  ?  301 PRO   E CG  1 
ATOM   14010 C CD  . PRO   I  1 301 ? -5.44987  -12.80257 66.00745  1.000 16.86290  ?  301 PRO   E CD  1 
ATOM   14011 N N   . VAL   I  1 302 ? -4.95447  -13.59362 69.38121  1.000 23.62157  ?  302 VAL   E N   1 
ATOM   14012 C CA  . VAL   I  1 302 ? -5.37981  -14.01923 70.71242  1.000 48.45388  ?  302 VAL   E CA  1 
ATOM   14013 C C   . VAL   I  1 302 ? -5.65650  -15.51709 70.67746  1.000 22.86662  ?  302 VAL   E C   1 
ATOM   14014 O O   . VAL   I  1 302 ? -5.82866  -16.11261 69.61326  1.000 39.53871  ?  302 VAL   E O   1 
ATOM   14015 C CB  . VAL   I  1 302 ? -6.65530  -13.28317 71.19310  1.000 22.62444  ?  302 VAL   E CB  1 
ATOM   14016 C CG1 . VAL   I  1 302 ? -6.40514  -11.79240 71.33438  1.000 46.89171  ?  302 VAL   E CG1 1 
ATOM   14017 C CG2 . VAL   I  1 302 ? -7.83432  -13.58404 70.24591  1.000 21.31219  ?  302 VAL   E CG2 1 
ATOM   14018 N N   . ASN   I  1 303 ? -5.70710  -16.13146 71.85872  1.000 36.20161  ?  303 ASN   E N   1 
ATOM   14019 C CA  . ASN   I  1 303 ? -6.36121  -17.43000 71.97522  1.000 21.07344  ?  303 ASN   E CA  1 
ATOM   14020 C C   . ASN   I  1 303 ? -7.86487  -17.20778 71.89285  1.000 40.37610  ?  303 ASN   E C   1 
ATOM   14021 O O   . ASN   I  1 303 ? -8.41782  -16.38385 72.63502  1.000 35.87804  ?  303 ASN   E O   1 
ATOM   14022 C CB  . ASN   I  1 303 ? -6.01535  -18.11832 73.29796  1.000 39.90068  ?  303 ASN   E CB  1 
ATOM   14023 C CG  . ASN   I  1 303 ? -4.51611  -18.24930 73.53787  1.000 32.63981  ?  303 ASN   E CG  1 
ATOM   14024 O OD1 . ASN   I  1 303 ? -3.68512  -18.06024 72.64039  1.000 37.34706  ?  303 ASN   E OD1 1 
ATOM   14025 N ND2 . ASN   I  1 303 ? -4.16783  -18.58198 74.76889  1.000 35.39974  ?  303 ASN   E ND2 1 
ATOM   14026 N N   . GLY   I  1 304 ? -8.53330  -17.90728 70.98450  1.000 37.09257  ?  304 GLY   E N   1 
ATOM   14027 C CA  . GLY   I  1 304 ? -9.95978  -17.68583 70.87674  1.000 23.86478  ?  304 GLY   E CA  1 
ATOM   14028 C C   . GLY   I  1 304 ? -10.58576 -18.51267 69.78094  1.000 40.39132  ?  304 GLY   E C   1 
ATOM   14029 O O   . GLY   I  1 304 ? -9.95342  -19.39358 69.18646  1.000 43.20706  ?  304 GLY   E O   1 
ATOM   14030 N N   . THR   I  1 305 ? -11.85055 -18.19268 69.52045  1.000 30.82790  ?  305 THR   E N   1 
ATOM   14031 C CA  . THR   I  1 305 ? -12.67558 -18.91067 68.56002  1.000 32.12670  ?  305 THR   E CA  1 
ATOM   14032 C C   . THR   I  1 305 ? -13.01565 -18.00786 67.37925  1.000 54.05913  ?  305 THR   E C   1 
ATOM   14033 O O   . THR   I  1 305 ? -13.34973 -16.82492 67.55829  1.000 18.93271  ?  305 THR   E O   1 
ATOM   14034 C CB  . THR   I  1 305 ? -13.96310 -19.40199 69.22513  1.000 21.74657  ?  305 THR   E CB  1 
ATOM   14035 O OG1 . THR   I  1 305 ? -13.64306 -19.93190 70.51777  1.000 38.81802  ?  305 THR   E OG1 1 
ATOM   14036 C CG2 . THR   I  1 305 ? -14.61962 -20.47643 68.37499  1.000 21.53364  ?  305 THR   E CG2 1 
ATOM   14037 N N   . ILE   I  1 306 ? -12.91919 -18.56377 66.17271  1.000 19.33778  ?  306 ILE   E N   1 
ATOM   14038 C CA  . ILE   I  1 306 ? -13.30928 -17.81805 64.98506  1.000 32.16313  ?  306 ILE   E CA  1 
ATOM   14039 C C   . ILE   I  1 306 ? -14.82411 -17.73859 64.97896  1.000 32.80232  ?  306 ILE   E C   1 
ATOM   14040 O O   . ILE   I  1 306 ? -15.50678 -18.76619 64.91541  1.000 35.85768  ?  306 ILE   E O   1 
ATOM   14041 C CB  . ILE   I  1 306 ? -12.78739 -18.48586 63.70743  1.000 28.43213  ?  306 ILE   E CB  1 
ATOM   14042 C CG1 . ILE   I  1 306 ? -11.29024 -18.81014 63.81975  1.000 15.83483  ?  306 ILE   E CG1 1 
ATOM   14043 C CG2 . ILE   I  1 306 ? -13.10272 -17.60456 62.49252  1.000 24.12594  ?  306 ILE   E CG2 1 
ATOM   14044 C CD1 . ILE   I  1 306 ? -10.39070 -17.61962 64.17066  1.000 22.59250  ?  306 ILE   E CD1 1 
ATOM   14045 N N   . VAL   I  1 307 ? -15.35647 -16.52843 65.07706  1.000 35.66548  ?  307 VAL   E N   1 
ATOM   14046 C CA  . VAL   I  1 307 ? -16.80030 -16.37482 65.12211  1.000 29.55049  ?  307 VAL   E CA  1 
ATOM   14047 C C   . VAL   I  1 307 ? -17.39439 -16.29715 63.72046  1.000 38.26772  ?  307 VAL   E C   1 
ATOM   14048 O O   . VAL   I  1 307 ? -18.40962 -16.94221 63.44423  1.000 36.77122  ?  307 VAL   E O   1 
ATOM   14049 C CB  . VAL   I  1 307 ? -17.17866 -15.14724 65.96913  1.000 45.47310  ?  307 VAL   E CB  1 
ATOM   14050 C CG1 . VAL   I  1 307 ? -18.68880 -14.98708 66.00853  1.000 19.44809  ?  307 VAL   E CG1 1 
ATOM   14051 C CG2 . VAL   I  1 307 ? -16.60595 -15.26221 67.38150  1.000 30.51954  ?  307 VAL   E CG2 1 
ATOM   14052 N N   . LYS   I  1 308 ? -16.74746 -15.55823 62.81460  1.000 43.72797  ?  308 LYS   E N   1 
ATOM   14053 C CA  . LYS   I  1 308 ? -17.35570 -15.19705 61.53681  1.000 34.34691  ?  308 LYS   E CA  1 
ATOM   14054 C C   . LYS   I  1 308 ? -16.28570 -14.68203 60.58539  1.000 47.87055  ?  308 LYS   E C   1 
ATOM   14055 O O   . LYS   I  1 308 ? -15.47500 -13.82686 60.96419  1.000 31.04080  ?  308 LYS   E O   1 
ATOM   14056 C CB  . LYS   I  1 308 ? -18.42011 -14.12373 61.74923  1.000 31.16295  ?  308 LYS   E CB  1 
ATOM   14057 C CG  . LYS   I  1 308 ? -19.41250 -13.90800 60.62049  1.000 22.50407  ?  308 LYS   E CG  1 
ATOM   14058 C CD  . LYS   I  1 308 ? -20.23188 -12.67471 61.00832  1.000 33.36150  ?  308 LYS   E CD  1 
ATOM   14059 C CE  . LYS   I  1 308 ? -21.55074 -12.54663 60.25936  1.000 53.30459  ?  308 LYS   E CE  1 
ATOM   14060 N NZ  . LYS   I  1 308 ? -22.38947 -11.53277 60.99248  1.000 64.95046  ?  308 LYS   E NZ  1 
ATOM   14061 N N   . ILE   I  1 309 ? -16.29954 -15.19191 59.35485  1.000 29.90352  ?  309 ILE   E N   1 
ATOM   14062 C CA  . ILE   I  1 309 ? -15.39310 -14.77258 58.29213  1.000 36.98195  ?  309 ILE   E CA  1 
ATOM   14063 C C   . ILE   I  1 309 ? -16.24771 -14.28123 57.13488  1.000 29.42970  ?  309 ILE   E C   1 
ATOM   14064 O O   . ILE   I  1 309 ? -17.08929 -15.03432 56.63316  1.000 38.00466  ?  309 ILE   E O   1 
ATOM   14065 C CB  . ILE   I  1 309 ? -14.48987 -15.91820 57.82087  1.000 21.43233  ?  309 ILE   E CB  1 
ATOM   14066 C CG1 . ILE   I  1 309 ? -13.64343 -16.46394 58.96089  1.000 42.12232  ?  309 ILE   E CG1 1 
ATOM   14067 C CG2 . ILE   I  1 309 ? -13.61637 -15.44534 56.66235  1.000 24.08739  ?  309 ILE   E CG2 1 
ATOM   14068 C CD1 . ILE   I  1 309 ? -13.01479 -17.78547 58.62012  1.000 22.81986  ?  309 ILE   E CD1 1 
ATOM   14069 N N   . ILE   I  1 310 ? -16.03211 -13.03431 56.70195  1.000 36.77740  ?  310 ILE   E N   1 
ATOM   14070 C CA  . ILE   I  1 310 ? -16.80532 -12.44212 55.61430  1.000 20.65529  ?  310 ILE   E CA  1 
ATOM   14071 C C   . ILE   I  1 310 ? -15.86026 -11.92251 54.54409  1.000 38.06707  ?  310 ILE   E C   1 
ATOM   14072 O O   . ILE   I  1 310 ? -14.93825 -11.15257 54.84184  1.000 31.06126  ?  310 ILE   E O   1 
ATOM   14073 C CB  . ILE   I  1 310 ? -17.70708 -11.29200 56.09092  1.000 38.04466  ?  310 ILE   E CB  1 
ATOM   14074 C CG1 . ILE   I  1 310 ? -18.53295 -11.71063 57.30265  1.000 39.13539  ?  310 ILE   E CG1 1 
ATOM   14075 C CG2 . ILE   I  1 310 ? -18.57796 -10.84071 54.94202  1.000 25.48067  ?  310 ILE   E CG2 1 
ATOM   14076 C CD1 . ILE   I  1 310 ? -18.19405 -10.92496 58.55070  1.000 43.50667  ?  310 ILE   E CD1 1 
ATOM   14077 N N   . ASN   I  1 311 ? -16.11759 -12.29016 53.29502  1.000 33.84701  ?  311 ASN   E N   1 
ATOM   14078 C CA  . ASN   I  1 311 ? -15.31433 -11.80084 52.18492  1.000 30.65919  ?  311 ASN   E CA  1 
ATOM   14079 C C   . ASN   I  1 311 ? -16.09748 -10.73618 51.43524  1.000 20.01592  ?  311 ASN   E C   1 
ATOM   14080 O O   . ASN   I  1 311 ? -17.22324 -10.97575 50.99010  1.000 47.02887  ?  311 ASN   E O   1 
ATOM   14081 C CB  . ASN   I  1 311 ? -14.88091 -12.94314 51.27507  1.000 15.41390  ?  311 ASN   E CB  1 
ATOM   14082 C CG  . ASN   I  1 311 ? -13.68015 -13.69184 51.84758  1.000 61.13691  ?  311 ASN   E CG  1 
ATOM   14083 O OD1 . ASN   I  1 311 ? -12.58405 -13.12744 51.97124  1.000 41.12800  ?  311 ASN   E OD1 1 
ATOM   14084 N ND2 . ASN   I  1 311 ? -13.88947 -14.94648 52.23438  1.000 43.33156  ?  311 ASN   E ND2 1 
ATOM   14085 N N   . VAL   I  1 312 ? -15.51571 -9.54710  51.33722  1.000 29.60467  ?  312 VAL   E N   1 
ATOM   14086 C CA  . VAL   I  1 312 ? -16.21572 -8.37863  50.83328  1.000 28.05037  ?  312 VAL   E CA  1 
ATOM   14087 C C   . VAL   I  1 312 ? -15.56095 -7.93642  49.52716  1.000 26.89621  ?  312 VAL   E C   1 
ATOM   14088 O O   . VAL   I  1 312 ? -14.37156 -7.60273  49.50898  1.000 51.79937  ?  312 VAL   E O   1 
ATOM   14089 C CB  . VAL   I  1 312 ? -16.22834 -7.23358  51.86135  1.000 31.61626  ?  312 VAL   E CB  1 
ATOM   14090 C CG1 . VAL   I  1 312 ? -17.21973 -6.14401  51.41747  1.000 17.91311  ?  312 VAL   E CG1 1 
ATOM   14091 C CG2 . VAL   I  1 312 ? -16.61878 -7.76690  53.23536  1.000 24.31236  ?  312 VAL   E CG2 1 
ATOM   14092 N N   . PRO   I  1 313 ? -16.28516 -7.93222  48.41490  1.000 37.78772  ?  313 PRO   E N   1 
ATOM   14093 C CA  . PRO   I  1 313 ? -15.74480 -7.34214  47.18063  1.000 33.47054  ?  313 PRO   E CA  1 
ATOM   14094 C C   . PRO   I  1 313 ? -15.59090 -5.83888  47.33983  1.000 37.15061  ?  313 PRO   E C   1 
ATOM   14095 O O   . PRO   I  1 313 ? -16.34382 -5.19148  48.07546  1.000 32.38891  ?  313 PRO   E O   1 
ATOM   14096 C CB  . PRO   I  1 313 ? -16.80894 -7.66833  46.11922  1.000 16.50962  ?  313 PRO   E CB  1 
ATOM   14097 C CG  . PRO   I  1 313 ? -17.75625 -8.68996  46.77702  1.000 22.35828  ?  313 PRO   E CG  1 
ATOM   14098 C CD  . PRO   I  1 313 ? -17.64850 -8.46368  48.26011  1.000 18.52922  ?  313 PRO   E CD  1 
ATOM   14099 N N   . GLY   I  1 314 ? -14.61112 -5.27919  46.63728  1.000 33.09714  ?  314 GLY   E N   1 
ATOM   14100 C CA  . GLY   I  1 314 ? -14.36886 -3.86083  46.76199  1.000 25.55859  ?  314 GLY   E CA  1 
ATOM   14101 C C   . GLY   I  1 314 ? -13.43940 -3.30151  45.71189  1.000 42.52140  ?  314 GLY   E C   1 
ATOM   14102 O O   . GLY   I  1 314 ? -13.30075 -3.85177  44.61646  1.000 33.77244  ?  314 GLY   E O   1 
ATOM   14103 N N   . THR   I  1 315 ? -12.81174 -2.18121  46.05729  1.000 28.73544  ?  315 THR   E N   1 
ATOM   14104 C CA  . THR   I  1 315 ? -11.87766 -1.51244  45.16975  1.000 31.08705  ?  315 THR   E CA  1 
ATOM   14105 C C   . THR   I  1 315 ? -10.49966 -2.18462  45.21426  1.000 39.41751  ?  315 THR   E C   1 
ATOM   14106 O O   . THR   I  1 315 ? -10.18823 -2.98781  46.10049  1.000 31.60090  ?  315 THR   E O   1 
ATOM   14107 C CB  . THR   I  1 315 ? -11.75073 -0.03249  45.54836  1.000 30.70951  ?  315 THR   E CB  1 
ATOM   14108 O OG1 . THR   I  1 315 ? -11.08955 0.10131   46.82292  1.000 24.48881  ?  315 THR   E OG1 1 
ATOM   14109 C CG2 . THR   I  1 315 ? -13.09603 0.56914   45.67681  1.000 21.20082  ?  315 THR   E CG2 1 
ATOM   14110 N N   . TYR   I  1 316 ? -9.67561  -1.82565  44.23315  1.000 29.82040  ?  316 TYR   E N   1 
ATOM   14111 C CA  . TYR   I  1 316 ? -8.26158  -2.14882  44.04331  1.000 29.38020  ?  316 TYR   E CA  1 
ATOM   14112 C C   . TYR   I  1 316 ? -7.41670  -0.89799  43.84390  1.000 24.40514  ?  316 TYR   E C   1 
ATOM   14113 O O   . TYR   I  1 316 ? -6.28055  -0.83915  44.32334  1.000 34.26716  ?  316 TYR   E O   1 
ATOM   14114 C CB  . TYR   I  1 316 ? -8.06797  -3.10327  42.82500  1.000 24.32566  ?  316 TYR   E CB  1 
ATOM   14115 C CG  . TYR   I  1 316 ? -8.84128  -4.38495  42.97741  1.000 35.07184  ?  316 TYR   E CG  1 
ATOM   14116 C CD1 . TYR   I  1 316 ? -8.34294  -5.43251  43.75960  1.000 36.45099  ?  316 TYR   E CD1 1 
ATOM   14117 C CD2 . TYR   I  1 316 ? -10.09438 -4.53171  42.38792  1.000 29.17053  ?  316 TYR   E CD2 1 
ATOM   14118 C CE1 . TYR   I  1 316 ? -9.06285  -6.60979  43.93832  1.000 28.08972  ?  316 TYR   E CE1 1 
ATOM   14119 C CE2 . TYR   I  1 316 ? -10.83090 -5.70470  42.54901  1.000 21.35872  ?  316 TYR   E CE2 1 
ATOM   14120 C CZ  . TYR   I  1 316 ? -10.30876 -6.73870  43.32403  1.000 39.14304  ?  316 TYR   E CZ  1 
ATOM   14121 O OH  . TYR   I  1 316 ? -11.04634 -7.89157  43.48223  1.000 30.41637  ?  316 TYR   E OH  1 
ATOM   14122 N N   . PHE   I  1 317 ? -7.94881  0.12086   43.15908  1.000 43.31717  ?  317 PHE   E N   1 
ATOM   14123 C CA  . PHE   I  1 317 ? -7.13205  1.24786   42.72673  1.000 24.56681  ?  317 PHE   E CA  1 
ATOM   14124 C C   . PHE   I  1 317 ? -7.69288  2.58485   43.19200  1.000 46.23668  ?  317 PHE   E C   1 
ATOM   14125 O O   . PHE   I  1 317 ? -7.42327  3.61868   42.56377  1.000 34.16807  ?  317 PHE   E O   1 
ATOM   14126 C CB  . PHE   I  1 317 ? -6.97814  1.23463   41.20613  1.000 24.44604  ?  317 PHE   E CB  1 
ATOM   14127 C CG  . PHE   I  1 317 ? -6.25460  0.02506   40.69620  1.000 44.58914  ?  317 PHE   E CG  1 
ATOM   14128 C CD1 . PHE   I  1 317 ? -4.88917  -0.11517  40.90780  1.000 25.24640  ?  317 PHE   E CD1 1 
ATOM   14129 C CD2 . PHE   I  1 317 ? -6.94276  -0.98498  40.03079  1.000 40.35253  ?  317 PHE   E CD2 1 
ATOM   14130 C CE1 . PHE   I  1 317 ? -4.21312  -1.23016  40.44587  1.000 40.55541  ?  317 PHE   E CE1 1 
ATOM   14131 C CE2 . PHE   I  1 317 ? -6.27652  -2.10075  39.57043  1.000 33.14499  ?  317 PHE   E CE2 1 
ATOM   14132 C CZ  . PHE   I  1 317 ? -4.90553  -2.22431  39.78263  1.000 34.55161  ?  317 PHE   E CZ  1 
ATOM   14133 N N   . ALA   I  1 318 ? -8.45361  2.59109   44.29422  1.000 34.70521  ?  318 ALA   E N   1 
ATOM   14134 C CA  . ALA   I  1 318 ? -9.06230  3.81752   44.81221  1.000 31.58075  ?  318 ALA   E CA  1 
ATOM   14135 C C   . ALA   I  1 318 ? -8.15798  4.42959   45.87263  1.000 36.39647  ?  318 ALA   E C   1 
ATOM   14136 O O   . ALA   I  1 318 ? -7.96976  3.84421   46.94238  1.000 41.31328  ?  318 ALA   E O   1 
ATOM   14137 C CB  . ALA   I  1 318 ? -10.44105 3.53341   45.40059  1.000 25.10270  ?  318 ALA   E CB  1 
ATOM   14138 N N   . GLN   I  1 319 ? -7.61077  5.61278   45.59220  1.000 38.71109  ?  319 GLN   E N   1 
ATOM   14139 C CA  . GLN   I  1 319 ? -6.95257  6.37477   46.64359  1.000 35.19222  ?  319 GLN   E CA  1 
ATOM   14140 C C   . GLN   I  1 319 ? -7.96617  7.33098   47.27280  1.000 33.28736  ?  319 GLN   E C   1 
ATOM   14141 O O   . GLN   I  1 319 ? -9.11172  7.44474   46.82202  1.000 47.56043  ?  319 GLN   E O   1 
ATOM   14142 C CB  . GLN   I  1 319 ? -5.73276  7.11854   46.10556  1.000 34.67806  ?  319 GLN   E CB  1 
ATOM   14143 C CG  . GLN   I  1 319 ? -6.09198  8.16557   45.09246  1.000 42.78053  ?  319 GLN   E CG  1 
ATOM   14144 C CD  . GLN   I  1 319 ? -4.87192  8.72986   44.40536  1.000 31.79294  ?  319 GLN   E CD  1 
ATOM   14145 O OE1 . GLN   I  1 319 ? -4.25782  8.07226   43.55440  1.000 55.11355  ?  319 GLN   E OE1 1 
ATOM   14146 N NE2 . GLN   I  1 319 ? -4.51959  9.95980   44.75536  1.000 40.60014  ?  319 GLN   E NE2 1 
ATOM   14147 N N   . ALA   I  1 320 ? -7.55456  8.01225   48.33872  1.000 41.15852  ?  320 ALA   E N   1 
ATOM   14148 C CA  . ALA   I  1 320 ? -8.45294  8.95593   48.99869  1.000 41.90393  ?  320 ALA   E CA  1 
ATOM   14149 C C   . ALA   I  1 320 ? -8.68095  10.17352  48.10225  1.000 41.64674  ?  320 ALA   E C   1 
ATOM   14150 O O   . ALA   I  1 320 ? -7.70994  10.77384  47.62116  1.000 43.18494  ?  320 ALA   E O   1 
ATOM   14151 C CB  . ALA   I  1 320 ? -7.88911  9.38647   50.34774  1.000 25.64643  ?  320 ALA   E CB  1 
ATOM   14152 N N   . PRO   I  1 321 ? -9.93528  10.57752  47.87228  1.000 58.58092  ?  321 PRO   E N   1 
ATOM   14153 C CA  . PRO   I  1 321 ? -10.19862 11.71117  46.96421  1.000 44.47989  ?  321 PRO   E CA  1 
ATOM   14154 C C   . PRO   I  1 321 ? -9.46269  12.99240  47.35229  1.000 50.16515  ?  321 PRO   E C   1 
ATOM   14155 O O   . PRO   I  1 321 ? -9.03393  13.73500  46.45991  1.000 54.93165  ?  321 PRO   E O   1 
ATOM   14156 C CB  . PRO   I  1 321 ? -11.72475 11.88189  47.04884  1.000 37.67647  ?  321 PRO   E CB  1 
ATOM   14157 C CG  . PRO   I  1 321 ? -12.24739 10.66528  47.75944  1.000 58.83662  ?  321 PRO   E CG  1 
ATOM   14158 C CD  . PRO   I  1 321 ? -11.13634 10.15485  48.61318  1.000 41.12639  ?  321 PRO   E CD  1 
ATOM   14159 N N   . SER   I  1 322 ? -9.27015  13.24857  48.65503  1.000 46.84093  ?  322 SER   E N   1 
ATOM   14160 C CA  . SER   I  1 322 ? -8.50156  14.40831  49.11433  1.000 46.32315  ?  322 SER   E CA  1 
ATOM   14161 C C   . SER   I  1 322 ? -7.05945  14.42618  48.60676  1.000 45.92714  ?  322 SER   E C   1 
ATOM   14162 O O   . SER   I  1 322 ? -6.43251  15.49294  48.62059  1.000 65.30690  ?  322 SER   E O   1 
ATOM   14163 C CB  . SER   I  1 322 ? -8.48893  14.47087  50.65006  1.000 37.38738  ?  322 SER   E CB  1 
ATOM   14164 O OG  . SER   I  1 322 ? -8.36793  13.18106  51.24117  1.000 62.47972  ?  322 SER   E OG  1 
ATOM   14165 N N   . THR   I  1 323 ? -6.50518  13.28053  48.19109  1.000 57.48033  ?  323 THR   E N   1 
ATOM   14166 C CA  . THR   I  1 323 ? -5.13196  13.22524  47.69634  1.000 39.82464  ?  323 THR   E CA  1 
ATOM   14167 C C   . THR   I  1 323 ? -5.04298  13.27771  46.18147  1.000 55.29924  ?  323 THR   E C   1 
ATOM   14168 O O   . THR   I  1 323 ? -3.93195  13.28098  45.64908  1.000 38.21061  ?  323 THR   E O   1 
ATOM   14169 C CB  . THR   I  1 323 ? -4.41395  11.95394  48.17876  1.000 46.55895  ?  323 THR   E CB  1 
ATOM   14170 O OG1 . THR   I  1 323 ? -4.83270  10.82617  47.39006  1.000 48.09427  ?  323 THR   E OG1 1 
ATOM   14171 C CG2 . THR   I  1 323 ? -4.72389  11.68701  49.62586  1.000 28.50922  ?  323 THR   E CG2 1 
ATOM   14172 N N   . ILE   I  1 324 ? -6.17299  13.29396  45.47414  1.000 43.57068  ?  324 ILE   E N   1 
ATOM   14173 C CA  . ILE   I  1 324 ? -6.12540  13.28789  44.01757  1.000 45.31647  ?  324 ILE   E CA  1 
ATOM   14174 C C   . ILE   I  1 324 ? -5.40101  14.53721  43.54589  1.000 63.86598  ?  324 ILE   E C   1 
ATOM   14175 O O   . ILE   I  1 324 ? -5.77671  15.66299  43.89828  1.000 56.53629  ?  324 ILE   E O   1 
ATOM   14176 C CB  . ILE   I  1 324 ? -7.53274  13.19524  43.43528  1.000 33.32553  ?  324 ILE   E CB  1 
ATOM   14177 C CG1 . ILE   I  1 324 ? -8.13198  11.82915  43.76582  1.000 46.70396  ?  324 ILE   E CG1 1 
ATOM   14178 C CG2 . ILE   I  1 324 ? -7.48978  13.43290  41.92530  1.000 35.86796  ?  324 ILE   E CG2 1 
ATOM   14179 C CD1 . ILE   I  1 324 ? -9.52461  11.66380  43.30407  1.000 40.20705  ?  324 ILE   E CD1 1 
ATOM   14180 N N   . GLY   I  1 325 ? -4.32997  14.34328  42.77594  1.000 50.38105  ?  325 GLY   E N   1 
ATOM   14181 C CA  . GLY   I  1 325 ? -3.52711  15.44175  42.28388  1.000 45.60068  ?  325 GLY   E CA  1 
ATOM   14182 C C   . GLY   I  1 325 ? -2.22886  15.69599  43.03083  1.000 54.63162  ?  325 GLY   E C   1 
ATOM   14183 O O   . GLY   I  1 325 ? -1.35172  16.37552  42.48568  1.000 59.80309  ?  325 GLY   E O   1 
ATOM   14184 N N   . ASP   I  1 326 ? -2.09033  15.19620  44.26056  1.000 47.32059  ?  326 ASP   E N   1 
ATOM   14185 C CA  . ASP   I  1 326 ? -0.83494  15.32057  44.99468  1.000 54.52495  ?  326 ASP   E CA  1 
ATOM   14186 C C   . ASP   I  1 326 ? 0.33702   14.76239  44.18103  1.000 45.69942  ?  326 ASP   E C   1 
ATOM   14187 O O   . ASP   I  1 326 ? 0.15968   13.88505  43.32838  1.000 56.06742  ?  326 ASP   E O   1 
ATOM   14188 C CB  . ASP   I  1 326 ? -0.91511  14.57753  46.32875  1.000 36.95696  ?  326 ASP   E CB  1 
ATOM   14189 C CG  . ASP   I  1 326 ? -1.88599  15.21173  47.30592  1.000 73.62971  ?  326 ASP   E CG  1 
ATOM   14190 O OD1 . ASP   I  1 326 ? -2.42203  16.31275  47.01408  1.000 59.23082  ?  326 ASP   E OD1 1 
ATOM   14191 O OD2 . ASP   I  1 326 ? -2.10249  14.58867  48.37640  1.000 61.82428  -1 326 ASP   E OD2 1 
ATOM   14192 N N   . PRO   I  1 327 ? 1.54933   15.24395  44.42954  1.000 61.79512  ?  327 PRO   E N   1 
ATOM   14193 C CA  . PRO   I  1 327 ? 2.70114   14.74774  43.66485  1.000 47.25247  ?  327 PRO   E CA  1 
ATOM   14194 C C   . PRO   I  1 327 ? 2.98525   13.27225  43.93615  1.000 41.97094  ?  327 PRO   E C   1 
ATOM   14195 O O   . PRO   I  1 327 ? 2.85574   12.79124  45.06459  1.000 54.95361  ?  327 PRO   E O   1 
ATOM   14196 C CB  . PRO   I  1 327 ? 3.85393   15.64177  44.14317  1.000 27.14350  ?  327 PRO   E CB  1 
ATOM   14197 C CG  . PRO   I  1 327 ? 3.37623   16.29342  45.40510  1.000 41.81254  ?  327 PRO   E CG  1 
ATOM   14198 C CD  . PRO   I  1 327 ? 1.88900   16.40396  45.27480  1.000 44.72765  ?  327 PRO   E CD  1 
ATOM   14199 N N   . ILE   I  1 328 ? 3.36561   12.55271  42.88250  1.000 50.46347  ?  328 ILE   E N   1 
ATOM   14200 C CA  . ILE   I  1 328 ? 3.84912   11.17925  43.02541  1.000 50.26278  ?  328 ILE   E CA  1 
ATOM   14201 C C   . ILE   I  1 328 ? 5.37307   11.19169  43.05691  1.000 52.55851  ?  328 ILE   E C   1 
ATOM   14202 O O   . ILE   I  1 328 ? 6.00971   11.27250  41.99531  1.000 61.59940  ?  328 ILE   E O   1 
ATOM   14203 C CB  . ILE   I  1 328 ? 3.33206   10.26857  41.89812  1.000 55.48766  ?  328 ILE   E CB  1 
ATOM   14204 C CG1 . ILE   I  1 328 ? 1.80299   10.29956  41.83606  1.000 42.94426  ?  328 ILE   E CG1 1 
ATOM   14205 C CG2 . ILE   I  1 328 ? 3.79484   8.82640   42.10651  1.000 44.66874  ?  328 ILE   E CG2 1 
ATOM   14206 C CD1 . ILE   I  1 328 ? 1.21769   9.39175   40.75309  1.000 38.95405  ?  328 ILE   E CD1 1 
ATOM   14207 N N   . PRO   I  1 329 ? 5.99481   11.08764  44.23529  1.000 67.19055  ?  329 PRO   E N   1 
ATOM   14208 C CA  . PRO   I  1 329 ? 7.45529   11.23547  44.33238  1.000 52.66276  ?  329 PRO   E CA  1 
ATOM   14209 C C   . PRO   I  1 329 ? 8.19401   10.22298  43.46972  1.000 54.91566  ?  329 PRO   E C   1 
ATOM   14210 O O   . PRO   I  1 329 ? 7.74941   9.08426   43.28534  1.000 87.26601  ?  329 PRO   E O   1 
ATOM   14211 C CB  . PRO   I  1 329 ? 7.74189   11.01193  45.82215  1.000 39.52356  ?  329 PRO   E CB  1 
ATOM   14212 C CG  . PRO   I  1 329 ? 6.41473   11.28881  46.51217  1.000 50.23194  ?  329 PRO   E CG  1 
ATOM   14213 C CD  . PRO   I  1 329 ? 5.35769   10.88873  45.54706  1.000 55.12319  ?  329 PRO   E CD  1 
ATOM   14214 N N   . ASP   I  1 330 ? 9.31187   10.67935  42.89838  1.000 69.32197  ?  330 ASP   E N   1 
ATOM   14215 C CA  . ASP   I  1 330 ? 10.19726  9.84624   42.09296  1.000 79.39389  ?  330 ASP   E CA  1 
ATOM   14216 C C   . ASP   I  1 330 ? 11.33930  9.22591   42.89920  1.000 58.08719  ?  330 ASP   E C   1 
ATOM   14217 O O   . ASP   I  1 330 ? 12.36862  8.85975   42.30235  1.000 86.81215  ?  330 ASP   E O   1 
ATOM   14218 C CB  . ASP   I  1 330 ? 10.75218  10.65340  40.90374  1.000 50.62811  ?  330 ASP   E CB  1 
ATOM   14219 N N   . ASN   I  1 331 ? 11.15040  9.07777   44.21523  1.000 75.51650  ?  331 ASN   E N   1 
ATOM   14220 C CA  . ASN   I  1 331 ? 12.10294  8.49118   45.14438  1.000 75.64157  ?  331 ASN   E CA  1 
ATOM   14221 C C   . ASN   I  1 331 ? 11.38825  7.37948   45.90860  1.000 58.30996  ?  331 ASN   E C   1 
ATOM   14222 O O   . ASN   I  1 331 ? 10.29168  6.98552   45.53274  1.000 102.01991 ?  331 ASN   E O   1 
ATOM   14223 C CB  . ASN   I  1 331 ? 12.64261  9.58046   46.05880  1.000 53.56585  ?  331 ASN   E CB  1 
ATOM   14224 C CG  . ASN   I  1 331 ? 11.62044  10.14287  46.99276  1.000 64.65700  ?  331 ASN   E CG  1 
ATOM   14225 O OD1 . ASN   I  1 331 ? 10.87796  9.47029   47.70846  1.000 134.17024 ?  331 ASN   E OD1 1 
ATOM   14226 N ND2 . ASN   I  1 331 ? 11.51147  11.44304  46.90241  1.000 68.82673  ?  331 ASN   E ND2 1 
ATOM   14227 N N   . ASP   I  1 332 ? 11.93343  6.97547   47.06305  1.000 109.98560 ?  332 ASP   E N   1 
ATOM   14228 C CA  . ASP   I  1 332 ? 11.49341  5.83792   47.91958  1.000 64.89869  ?  332 ASP   E CA  1 
ATOM   14229 C C   . ASP   I  1 332 ? 11.21726  6.19599   49.38293  1.000 82.08304  ?  332 ASP   E C   1 
ATOM   14230 O O   . ASP   I  1 332 ? 10.84868  5.30838   50.14947  1.000 80.47160  ?  332 ASP   E O   1 
ATOM   14231 C CB  . ASP   I  1 332 ? 12.56467  4.71435   47.89917  1.000 30.42933  ?  332 ASP   E CB  1 
ATOM   14232 N N   . TYR   I  1 333 ? 11.46745  7.43737   49.81566  1.000 119.28349 ?  333 TYR   E N   1 
ATOM   14233 C CA  . TYR   I  1 333 ? 11.10233  7.82222   51.18333  1.000 79.73489  ?  333 TYR   E CA  1 
ATOM   14234 C C   . TYR   I  1 333 ? 9.84045   8.66908   51.26509  1.000 77.24743  ?  333 TYR   E C   1 
ATOM   14235 O O   . TYR   I  1 333 ? 9.19556   8.71293   52.32493  1.000 60.13419  ?  333 TYR   E O   1 
ATOM   14236 C CB  . TYR   I  1 333 ? 12.21449  8.61178   51.89032  1.000 83.32882  ?  333 TYR   E CB  1 
ATOM   14237 C CG  . TYR   I  1 333 ? 12.64103  9.92165   51.23042  1.000 136.72839 ?  333 TYR   E CG  1 
ATOM   14238 C CD1 . TYR   I  1 333 ? 13.11838  9.93039   49.92398  1.000 114.76345 ?  333 TYR   E CD1 1 
ATOM   14239 C CD2 . TYR   I  1 333 ? 12.61832  11.14617  51.93023  1.000 133.34560 ?  333 TYR   E CD2 1 
ATOM   14240 C CE1 . TYR   I  1 333 ? 13.53116  11.12098  49.30996  1.000 100.63955 ?  333 TYR   E CE1 1 
ATOM   14241 C CE2 . TYR   I  1 333 ? 13.06655  12.34743  51.32851  1.000 60.91861  ?  333 TYR   E CE2 1 
ATOM   14242 C CZ  . TYR   I  1 333 ? 13.52998  12.31930  50.02399  1.000 84.77512  ?  333 TYR   E CZ  1 
ATOM   14243 O OH  . TYR   I  1 333 ? 13.94925  13.49163  49.42188  1.000 103.80578 ?  333 TYR   E OH  1 
ATOM   14244 N N   . ASP   I  1 334 ? 9.50020   9.32185   50.18793  1.000 74.45103  ?  334 ASP   E N   1 
ATOM   14245 C CA  . ASP   I  1 334 ? 8.25169   10.08242  50.27112  1.000 72.52575  ?  334 ASP   E CA  1 
ATOM   14246 C C   . ASP   I  1 334 ? 7.05252   9.25482   49.81709  1.000 81.96612  ?  334 ASP   E C   1 
ATOM   14247 O O   . ASP   I  1 334 ? 7.06116   8.70916   48.69976  1.000 47.69368  ?  334 ASP   E O   1 
ATOM   14248 C CB  . ASP   I  1 334 ? 8.33313   11.34614  49.43062  1.000 101.32781 ?  334 ASP   E CB  1 
ATOM   14249 C CG  . ASP   I  1 334 ? 9.25523   12.37487  50.02902  1.000 115.94914 ?  334 ASP   E CG  1 
ATOM   14250 O OD1 . ASP   I  1 334 ? 9.36222   12.42570  51.28651  1.000 72.15478  ?  334 ASP   E OD1 1 
ATOM   14251 O OD2 . ASP   I  1 334 ? 9.86697   13.14155  49.26004  1.000 83.47899  -1 334 ASP   E OD2 1 
ATOM   14252 N N   . PRO   I  1 335 ? 6.00810   9.15785   50.63950  1.000 66.93701  ?  335 PRO   E N   1 
ATOM   14253 C CA  . PRO   I  1 335 ? 4.85793   8.32313   50.29045  1.000 46.74347  ?  335 PRO   E CA  1 
ATOM   14254 C C   . PRO   I  1 335 ? 4.05754   8.94510   49.16758  1.000 30.77301  ?  335 PRO   E C   1 
ATOM   14255 O O   . PRO   I  1 335 ? 3.74965   10.15268  49.19350  1.000 59.71460  ?  335 PRO   E O   1 
ATOM   14256 C CB  . PRO   I  1 335 ? 4.04348   8.28056   51.59257  1.000 52.52226  ?  335 PRO   E CB  1 
ATOM   14257 C CG  . PRO   I  1 335 ? 4.93377   8.88107   52.64581  1.000 65.38289  ?  335 PRO   E CG  1 
ATOM   14258 C CD  . PRO   I  1 335 ? 5.85517   9.80039   51.94904  1.000 38.95894  ?  335 PRO   E CD  1 
ATOM   14259 N N   . PRO   I  1 336 ? 3.68544   8.15717   48.15677  1.000 62.45648  ?  336 PRO   E N   1 
ATOM   14260 C CA  . PRO   I  1 336 ? 2.78106   8.64934   47.10490  1.000 26.87160  ?  336 PRO   E CA  1 
ATOM   14261 C C   . PRO   I  1 336 ? 1.34535   8.69397   47.60883  1.000 93.16385  ?  336 PRO   E C   1 
ATOM   14262 O O   . PRO   I  1 336 ? 1.03693   8.17488   48.69659  1.000 32.23010  ?  336 PRO   E O   1 
ATOM   14263 C CB  . PRO   I  1 336 ? 2.96969   7.62182   45.98150  1.000 45.85464  ?  336 PRO   E CB  1 
ATOM   14264 C CG  . PRO   I  1 336 ? 3.31700   6.34598   46.70304  1.000 42.83121  ?  336 PRO   E CG  1 
ATOM   14265 C CD  . PRO   I  1 336 ? 3.97911   6.71473   48.01392  1.000 26.85425  ?  336 PRO   E CD  1 
ATOM   14266 N N   . PRO   I  1 337 ? 0.43436   9.33411   46.86817  1.000 33.41093  ?  337 PRO   E N   1 
ATOM   14267 C CA  . PRO   I  1 337 ? -0.93625  9.52718   47.40356  1.000 49.02241  ?  337 PRO   E CA  1 
ATOM   14268 C C   . PRO   I  1 337 ? -1.63123  8.23894   47.84418  1.000 37.57598  ?  337 PRO   E C   1 
ATOM   14269 O O   . PRO   I  1 337 ? -2.25642  8.21089   48.91283  1.000 35.42170  ?  337 PRO   E O   1 
ATOM   14270 C CB  . PRO   I  1 337 ? -1.67549  10.19450  46.23691  1.000 35.54509  ?  337 PRO   E CB  1 
ATOM   14271 C CG  . PRO   I  1 337 ? -0.62706  10.82474  45.42013  1.000 43.92777  ?  337 PRO   E CG  1 
ATOM   14272 C CD  . PRO   I  1 337 ? 0.61276   9.97637   45.55784  1.000 52.60251  ?  337 PRO   E CD  1 
ATOM   14273 N N   . TYR   I  1 338 ? -1.51523  7.16337   47.06195  1.000 36.28288  ?  338 TYR   E N   1 
ATOM   14274 C CA  . TYR   I  1 338 ? -2.12248  5.89308   47.44417  1.000 38.86799  ?  338 TYR   E CA  1 
ATOM   14275 C C   . TYR   I  1 338 ? -1.64419  5.42631   48.81711  1.000 32.68038  ?  338 TYR   E C   1 
ATOM   14276 O O   . TYR   I  1 338 ? -2.45936  5.01267   49.65296  1.000 34.00851  ?  338 TYR   E O   1 
ATOM   14277 C CB  . TYR   I  1 338 ? -1.82949  4.83736   46.37719  1.000 26.38573  ?  338 TYR   E CB  1 
ATOM   14278 C CG  . TYR   I  1 338 ? -2.55207  3.51902   46.56344  1.000 39.46218  ?  338 TYR   E CG  1 
ATOM   14279 C CD1 . TYR   I  1 338 ? -3.94837  3.45463   46.62423  1.000 32.18992  ?  338 TYR   E CD1 1 
ATOM   14280 C CD2 . TYR   I  1 338 ? -1.83995  2.33492   46.65084  1.000 30.03043  ?  338 TYR   E CD2 1 
ATOM   14281 C CE1 . TYR   I  1 338 ? -4.60754  2.22900   46.77704  1.000 34.90233  ?  338 TYR   E CE1 1 
ATOM   14282 C CE2 . TYR   I  1 338 ? -2.48161  1.11809   46.80397  1.000 23.93902  ?  338 TYR   E CE2 1 
ATOM   14283 C CZ  . TYR   I  1 338 ? -3.85941  1.06473   46.87318  1.000 44.18388  ?  338 TYR   E CZ  1 
ATOM   14284 O OH  . TYR   I  1 338 ? -4.46888  -0.16350  47.02603  1.000 32.73248  ?  338 TYR   E OH  1 
ATOM   14285 N N   . LEU   I  1 339 ? -0.32519  5.47686   49.07523  1.000 33.26303  ?  339 LEU   E N   1 
ATOM   14286 C CA  . LEU   I  1 339 ? 0.16742   5.03177   50.38841  1.000 24.42441  ?  339 LEU   E CA  1 
ATOM   14287 C C   . LEU   I  1 339 ? -0.13194  6.01899   51.50954  1.000 36.40952  ?  339 LEU   E C   1 
ATOM   14288 O O   . LEU   I  1 339 ? 0.15730   5.70543   52.66924  1.000 38.10108  ?  339 LEU   E O   1 
ATOM   14289 C CB  . LEU   I  1 339 ? 1.66923   4.75200   50.35744  1.000 25.24745  ?  339 LEU   E CB  1 
ATOM   14290 C CG  . LEU   I  1 339 ? 2.02540   3.60509   49.40038  1.000 47.26270  ?  339 LEU   E CG  1 
ATOM   14291 C CD1 . LEU   I  1 339 ? 3.49448   3.25421   49.49008  1.000 31.08821  ?  339 LEU   E CD1 1 
ATOM   14292 C CD2 . LEU   I  1 339 ? 1.17883   2.38183   49.67667  1.000 32.44226  ?  339 LEU   E CD2 1 
ATOM   14293 N N   . LYS   I  1 340 ? -0.69782  7.18837   51.20840  1.000 27.87816  ?  340 LYS   E N   1 
ATOM   14294 C CA  . LYS   I  1 340 ? -1.29337  8.03989   52.23037  1.000 47.69681  ?  340 LYS   E CA  1 
ATOM   14295 C C   . LYS   I  1 340 ? -2.80863  7.82937   52.37540  1.000 29.90880  ?  340 LYS   E C   1 
ATOM   14296 O O   . LYS   I  1 340 ? -3.46591  8.63415   53.03857  1.000 36.30010  ?  340 LYS   E O   1 
ATOM   14297 C CB  . LYS   I  1 340 ? -0.99606  9.51321   51.93093  1.000 30.55885  ?  340 LYS   E CB  1 
ATOM   14298 C CG  . LYS   I  1 340 ? 0.26297   10.10306  52.55803  1.000 32.66573  ?  340 LYS   E CG  1 
ATOM   14299 C CD  . LYS   I  1 340 ? 1.16505   10.66694  51.49404  1.000 82.50143  ?  340 LYS   E CD  1 
ATOM   14300 C CE  . LYS   I  1 340 ? 0.43982   11.76530  50.75606  1.000 104.70846 ?  340 LYS   E CE  1 
ATOM   14301 N NZ  . LYS   I  1 340 ? 1.19681   12.13194  49.54825  1.000 85.35720  ?  340 LYS   E NZ  1 
ATOM   14302 N N   . SER   I  1 341 ? -3.36903  6.75308   51.79521  1.000 35.13723  ?  341 SER   E N   1 
ATOM   14303 C CA  . SER   I  1 341 ? -4.81205  6.53369   51.73085  1.000 28.29228  ?  341 SER   E CA  1 
ATOM   14304 C C   . SER   I  1 341 ? -5.30435  5.29079   52.47324  1.000 33.17791  ?  341 SER   E C   1 
ATOM   14305 O O   . SER   I  1 341 ? -6.49782  4.96088   52.37026  1.000 43.72657  ?  341 SER   E O   1 
ATOM   14306 C CB  . SER   I  1 341 ? -5.26400  6.42746   50.26280  1.000 34.83786  ?  341 SER   E CB  1 
ATOM   14307 O OG  . SER   I  1 341 ? -5.04012  7.62688   49.54341  1.000 34.59977  ?  341 SER   E OG  1 
ATOM   14308 N N   . LEU   I  1 342 ? -4.43638  4.59551   53.21118  1.000 31.29628  ?  342 LEU   E N   1 
ATOM   14309 C CA  . LEU   I  1 342 ? -4.78500  3.27277   53.72473  1.000 42.48554  ?  342 LEU   E CA  1 
ATOM   14310 C C   . LEU   I  1 342 ? -5.98204  3.31738   54.66940  1.000 31.08802  ?  342 LEU   E C   1 
ATOM   14311 O O   . LEU   I  1 342 ? -6.79594  2.38739   54.68538  1.000 37.00443  ?  342 LEU   E O   1 
ATOM   14312 C CB  . LEU   I  1 342 ? -3.58934  2.64024   54.43462  1.000 25.35100  ?  342 LEU   E CB  1 
ATOM   14313 C CG  . LEU   I  1 342 ? -2.67095  1.74604   53.61300  1.000 43.61715  ?  342 LEU   E CG  1 
ATOM   14314 C CD1 . LEU   I  1 342 ? -1.97826  2.55047   52.51152  1.000 23.79407  ?  342 LEU   E CD1 1 
ATOM   14315 C CD2 . LEU   I  1 342 ? -1.65178  1.07759   54.55426  1.000 19.40526  ?  342 LEU   E CD2 1 
ATOM   14316 N N   . VAL   I  1 343 ? -6.10848  4.36483   55.48589  1.000 43.08007  ?  343 VAL   E N   1 
ATOM   14317 C CA  . VAL   I  1 343 ? -7.28424  4.41980   56.35124  1.000 37.37413  ?  343 VAL   E CA  1 
ATOM   14318 C C   . VAL   I  1 343 ? -8.54089  4.58616   55.50957  1.000 50.28825  ?  343 VAL   E C   1 
ATOM   14319 O O   . VAL   I  1 343 ? -9.52240  3.85604   55.68539  1.000 34.61678  ?  343 VAL   E O   1 
ATOM   14320 C CB  . VAL   I  1 343 ? -7.15884  5.53354   57.40559  1.000 38.25476  ?  343 VAL   E CB  1 
ATOM   14321 C CG1 . VAL   I  1 343 ? -8.49603  5.72490   58.12046  1.000 24.47010  ?  343 VAL   E CG1 1 
ATOM   14322 C CG2 . VAL   I  1 343 ? -6.09814  5.16846   58.42639  1.000 31.81777  ?  343 VAL   E CG2 1 
ATOM   14323 N N   . TYR   I  1 344 ? -8.50923  5.51603   54.55310  1.000 27.16518  ?  344 TYR   E N   1 
ATOM   14324 C CA  . TYR   I  1 344 ? -9.66289  5.73975   53.68885  1.000 44.62096  ?  344 TYR   E CA  1 
ATOM   14325 C C   . TYR   I  1 344 ? -10.13106 4.45169   53.02106  1.000 46.15416  ?  344 TYR   E C   1 
ATOM   14326 O O   . TYR   I  1 344 ? -11.30076 4.07440   53.14451  1.000 36.13923  ?  344 TYR   E O   1 
ATOM   14327 C CB  . TYR   I  1 344 ? -9.34378  6.79384   52.62693  1.000 31.52164  ?  344 TYR   E CB  1 
ATOM   14328 C CG  . TYR   I  1 344 ? -10.44916 6.97211   51.60636  1.000 51.90624  ?  344 TYR   E CG  1 
ATOM   14329 C CD1 . TYR   I  1 344 ? -11.55508 7.76740   51.88490  1.000 34.65784  ?  344 TYR   E CD1 1 
ATOM   14330 C CD2 . TYR   I  1 344 ? -10.39033 6.34298   50.36559  1.000 43.88351  ?  344 TYR   E CD2 1 
ATOM   14331 C CE1 . TYR   I  1 344 ? -12.57704 7.93566   50.95909  1.000 34.85691  ?  344 TYR   E CE1 1 
ATOM   14332 C CE2 . TYR   I  1 344 ? -11.41063 6.50466   49.42198  1.000 33.95415  ?  344 TYR   E CE2 1 
ATOM   14333 C CZ  . TYR   I  1 344 ? -12.49476 7.30206   49.72967  1.000 52.22385  ?  344 TYR   E CZ  1 
ATOM   14334 O OH  . TYR   I  1 344 ? -13.49722 7.47515   48.80926  1.000 47.26331  ?  344 TYR   E OH  1 
ATOM   14335 N N   . PHE   I  1 345 ? -9.23333  3.76052   52.30212  1.000 24.70017  ?  345 PHE   E N   1 
ATOM   14336 C CA  . PHE   I  1 345 ? -9.70901  2.67013   51.45411  1.000 33.74851  ?  345 PHE   E CA  1 
ATOM   14337 C C   . PHE   I  1 345 ? -9.86772  1.35157   52.20495  1.000 38.92790  ?  345 PHE   E C   1 
ATOM   14338 O O   . PHE   I  1 345 ? -10.40756 0.39477   51.63563  1.000 35.27106  ?  345 PHE   E O   1 
ATOM   14339 C CB  . PHE   I  1 345 ? -8.83749  2.50388   50.17706  1.000 24.24954  ?  345 PHE   E CB  1 
ATOM   14340 C CG  . PHE   I  1 345 ? -7.41068  2.01158   50.39352  1.000 37.45458  ?  345 PHE   E CG  1 
ATOM   14341 C CD1 . PHE   I  1 345 ? -7.14027  0.73578   50.87485  1.000 42.66470  ?  345 PHE   E CD1 1 
ATOM   14342 C CD2 . PHE   I  1 345 ? -6.33537  2.80022   49.99263  1.000 31.00323  ?  345 PHE   E CD2 1 
ATOM   14343 C CE1 . PHE   I  1 345 ? -5.81627  0.28961   51.02589  1.000 26.84764  ?  345 PHE   E CE1 1 
ATOM   14344 C CE2 . PHE   I  1 345 ? -5.00406  2.36582   50.13149  1.000 32.47036  ?  345 PHE   E CE2 1 
ATOM   14345 C CZ  . PHE   I  1 345 ? -4.74167  1.11186   50.64711  1.000 34.76810  ?  345 PHE   E CZ  1 
ATOM   14346 N N   . SER   I  1 346 ? -9.48109  1.28896   53.47856  1.000 19.74162  ?  346 SER   E N   1 
ATOM   14347 C CA  . SER   I  1 346 ? -9.91666  0.16814   54.30246  1.000 41.94889  ?  346 SER   E CA  1 
ATOM   14348 C C   . SER   I  1 346 ? -11.43839 0.08563   54.33098  1.000 29.32092  ?  346 SER   E C   1 
ATOM   14349 O O   . SER   I  1 346 ? -12.00349 -1.00020  54.51995  1.000 29.32384  ?  346 SER   E O   1 
ATOM   14350 C CB  . SER   I  1 346 ? -9.36826  0.30930   55.72083  1.000 28.72640  ?  346 SER   E CB  1 
ATOM   14351 O OG  . SER   I  1 346 ? -10.10274 1.29592   56.43115  1.000 25.33286  ?  346 SER   E OG  1 
ATOM   14352 N N   . ASN   I  1 347 ? -12.11293 1.22291   54.11451  1.000 41.29334  ?  347 ASN   E N   1 
ATOM   14353 C CA  . ASN   I  1 347 ? -13.57131 1.25606   54.09926  1.000 22.39448  ?  347 ASN   E CA  1 
ATOM   14354 C C   . ASN   I  1 347 ? -14.16575 0.57771   52.86707  1.000 39.26636  ?  347 ASN   E C   1 
ATOM   14355 O O   . ASN   I  1 347 ? -15.30521 0.09448   52.92798  1.000 39.60892  ?  347 ASN   E O   1 
ATOM   14356 C CB  . ASN   I  1 347 ? -14.06110 2.70369   54.17761  1.000 29.91459  ?  347 ASN   E CB  1 
ATOM   14357 C CG  . ASN   I  1 347 ? -13.74256 3.35403   55.50620  1.000 45.05999  ?  347 ASN   E CG  1 
ATOM   14358 O OD1 . ASN   I  1 347 ? -14.20860 2.90963   56.56203  1.000 36.19536  ?  347 ASN   E OD1 1 
ATOM   14359 N ND2 . ASN   I  1 347 ? -12.95576 4.41896   55.46476  1.000 26.92653  ?  347 ASN   E ND2 1 
ATOM   14360 N N   . ILE   I  1 348 ? -13.42988 0.53025   51.74814  1.000 36.40140  ?  348 ILE   E N   1 
ATOM   14361 C CA  . ILE   I  1 348 ? -14.04241 0.15341   50.47167  1.000 29.39678  ?  348 ILE   E CA  1 
ATOM   14362 C C   . ILE   I  1 348 ? -13.25891 -0.89007  49.67367  1.000 40.47610  ?  348 ILE   E C   1 
ATOM   14363 O O   . ILE   I  1 348 ? -13.76698 -1.42539  48.68100  1.000 43.94769  ?  348 ILE   E O   1 
ATOM   14364 C CB  . ILE   I  1 348 ? -14.26237 1.40918   49.61327  1.000 38.38035  ?  348 ILE   E CB  1 
ATOM   14365 C CG1 . ILE   I  1 348 ? -12.92700 2.12429   49.39076  1.000 26.91079  ?  348 ILE   E CG1 1 
ATOM   14366 C CG2 . ILE   I  1 348 ? -15.28702 2.33499   50.27436  1.000 24.81749  ?  348 ILE   E CG2 1 
ATOM   14367 C CD1 . ILE   I  1 348 ? -13.00751 3.20663   48.32332  1.000 49.46511  ?  348 ILE   E CD1 1 
ATOM   14368 N N   . ALA   I  1 349 ? -12.02489 -1.17921  50.07608  1.000 31.57152  ?  349 ALA   E N   1 
ATOM   14369 C CA  . ALA   I  1 349 ? -11.19777 -2.10132  49.30515  1.000 32.03429  ?  349 ALA   E CA  1 
ATOM   14370 C C   . ALA   I  1 349 ? -11.66875 -3.54276  49.47748  1.000 35.21627  ?  349 ALA   E C   1 
ATOM   14371 O O   . ALA   I  1 349 ? -12.23795 -3.91812  50.51085  1.000 40.15208  ?  349 ALA   E O   1 
ATOM   14372 C CB  . ALA   I  1 349 ? -9.73047  -2.00321  49.73505  1.000 17.23496  ?  349 ALA   E CB  1 
ATOM   14373 N N   . ALA   I  1 350 ? -11.42154 -4.35889  48.45156  1.000 27.08185  ?  350 ALA   E N   1 
ATOM   14374 C CA  . ALA   I  1 350 ? -11.56615 -5.80254  48.61181  1.000 29.56821  ?  350 ALA   E CA  1 
ATOM   14375 C C   . ALA   I  1 350 ? -10.83260 -6.26788  49.86842  1.000 35.50751  ?  350 ALA   E C   1 
ATOM   14376 O O   . ALA   I  1 350 ? -9.64725  -5.97605  50.05969  1.000 29.03709  ?  350 ALA   E O   1 
ATOM   14377 C CB  . ALA   I  1 350 ? -11.01848 -6.52120  47.38439  1.000 15.44184  ?  350 ALA   E CB  1 
ATOM   14378 N N   . ARG   I  1 351 ? -11.54936 -6.97707  50.73299  1.000 20.75087  ?  351 ARG   E N   1 
ATOM   14379 C CA  . ARG   I  1 351 ? -11.05704 -7.22206  52.07836  1.000 31.00501  ?  351 ARG   E CA  1 
ATOM   14380 C C   . ARG   I  1 351 ? -11.79142 -8.41654  52.66945  1.000 23.34187  ?  351 ARG   E C   1 
ATOM   14381 O O   . ARG   I  1 351 ? -12.85077 -8.83253  52.17745  1.000 37.57719  ?  351 ARG   E O   1 
ATOM   14382 C CB  . ARG   I  1 351 ? -11.22549 -5.97282  52.96578  1.000 16.72515  ?  351 ARG   E CB  1 
ATOM   14383 C CG  . ARG   I  1 351 ? -12.66582 -5.56398  53.18021  1.000 16.73089  ?  351 ARG   E CG  1 
ATOM   14384 C CD  . ARG   I  1 351 ? -12.77928 -4.12652  53.66148  1.000 24.64598  ?  351 ARG   E CD  1 
ATOM   14385 N NE  . ARG   I  1 351 ? -14.16455 -3.76061  53.93839  1.000 26.21007  ?  351 ARG   E NE  1 
ATOM   14386 C CZ  . ARG   I  1 351 ? -15.04701 -3.39488  53.01480  1.000 47.73153  ?  351 ARG   E CZ  1 
ATOM   14387 N NH1 . ARG   I  1 351 ? -14.72903 -3.32853  51.72929  1.000 26.48040  ?  351 ARG   E NH1 1 
ATOM   14388 N NH2 . ARG   I  1 351 ? -16.28244 -3.08261  53.38961  1.000 21.84733  ?  351 ARG   E NH2 1 
ATOM   14389 N N   . GLN   I  1 352 ? -11.19645 -8.97973  53.72246  1.000 28.38063  ?  352 GLN   E N   1 
ATOM   14390 C CA  . GLN   I  1 352 ? -11.83187 -10.03633 54.49922  1.000 21.74028  ?  352 GLN   E CA  1 
ATOM   14391 C C   . GLN   I  1 352 ? -11.92751 -9.58264  55.94455  1.000 33.91651  ?  352 GLN   E C   1 
ATOM   14392 O O   . GLN   I  1 352 ? -10.94455 -9.08426  56.51324  1.000 32.79516  ?  352 GLN   E O   1 
ATOM   14393 C CB  . GLN   I  1 352 ? -11.07311 -11.35237 54.42100  1.000 31.90530  ?  352 GLN   E CB  1 
ATOM   14394 C CG  . GLN   I  1 352 ? -11.69592 -12.44047 55.28079  1.000 26.95880  ?  352 GLN   E CG  1 
ATOM   14395 C CD  . GLN   I  1 352 ? -10.85609 -13.70936 55.27638  1.000 35.30512  ?  352 GLN   E CD  1 
ATOM   14396 O OE1 . GLN   I  1 352 ? -10.17124 -14.01648 56.24926  1.000 37.36406  ?  352 GLN   E OE1 1 
ATOM   14397 N NE2 . GLN   I  1 352 ? -10.89461 -14.44211 54.17035  1.000 24.47031  ?  352 GLN   E NE2 1 
ATOM   14398 N N   . ILE   I  1 353 ? -13.12574 -9.70680  56.50835  1.000 31.72674  ?  353 ILE   E N   1 
ATOM   14399 C CA  . ILE   I  1 353 ? -13.40909 -9.35155  57.89354  1.000 34.54975  ?  353 ILE   E CA  1 
ATOM   14400 C C   . ILE   I  1 353 ? -13.43903 -10.63967 58.69176  1.000 27.56671  ?  353 ILE   E C   1 
ATOM   14401 O O   . ILE   I  1 353 ? -14.09043 -11.61219 58.28165  1.000 41.65702  ?  353 ILE   E O   1 
ATOM   14402 C CB  . ILE   I  1 353 ? -14.75829 -8.62504  58.01513  1.000 32.45178  ?  353 ILE   E CB  1 
ATOM   14403 C CG1 . ILE   I  1 353 ? -14.77286 -7.34128  57.17953  1.000 39.69357  ?  353 ILE   E CG1 1 
ATOM   14404 C CG2 . ILE   I  1 353 ? -15.09954 -8.40309  59.48587  1.000 23.31538  ?  353 ILE   E CG2 1 
ATOM   14405 C CD1 . ILE   I  1 353 ? -16.16428 -6.89653  56.80259  1.000 19.86494  ?  353 ILE   E CD1 1 
ATOM   14406 N N   . MET   I  1 354 ? -12.74590 -10.66476 59.82439  1.000 23.92231  ?  354 MET   E N   1 
ATOM   14407 C CA  . MET   I  1 354 ? -12.73497 -11.85427 60.66954  1.000 29.22911  ?  354 MET   E CA  1 
ATOM   14408 C C   . MET   I  1 354 ? -13.03305 -11.44540 62.10491  1.000 34.32350  ?  354 MET   E C   1 
ATOM   14409 O O   . MET   I  1 354 ? -12.30848 -10.62552 62.68358  1.000 35.79369  ?  354 MET   E O   1 
ATOM   14410 C CB  . MET   I  1 354 ? -11.39723 -12.58335 60.56372  1.000 18.24523  ?  354 MET   E CB  1 
ATOM   14411 C CG  . MET   I  1 354 ? -11.36683 -13.95837 61.21553  1.000 40.08769  ?  354 MET   E CG  1 
ATOM   14412 S SD  . MET   I  1 354 ? -9.74477  -14.71906 61.04056  1.000 37.32667  ?  354 MET   E SD  1 
ATOM   14413 C CE  . MET   I  1 354 ? -9.80837  -15.17090 59.30122  1.000 35.53305  ?  354 MET   E CE  1 
ATOM   14414 N N   . PHE   I  1 355 ? -14.11913 -11.98136 62.66379  1.000 29.06873  ?  355 PHE   E N   1 
ATOM   14415 C CA  . PHE   I  1 355 ? -14.48608 -11.73566 64.05645  1.000 30.69975  ?  355 PHE   E CA  1 
ATOM   14416 C C   . PHE   I  1 355 ? -13.98908 -12.88508 64.91633  1.000 29.43952  ?  355 PHE   E C   1 
ATOM   14417 O O   . PHE   I  1 355 ? -14.21737 -14.05732 64.58837  1.000 34.05061  ?  355 PHE   E O   1 
ATOM   14418 C CB  . PHE   I  1 355 ? -15.99953 -11.58479 64.21117  1.000 34.55791  ?  355 PHE   E CB  1 
ATOM   14419 C CG  . PHE   I  1 355 ? -16.52891 -10.33802 63.60826  1.000 36.41732  ?  355 PHE   E CG  1 
ATOM   14420 C CD1 . PHE   I  1 355 ? -16.39412 -9.12992  64.27590  1.000 23.46071  ?  355 PHE   E CD1 1 
ATOM   14421 C CD2 . PHE   I  1 355 ? -17.13812 -10.36058 62.36790  1.000 32.15488  ?  355 PHE   E CD2 1 
ATOM   14422 C CE1 . PHE   I  1 355 ? -16.87173 -7.95307  63.72611  1.000 36.33879  ?  355 PHE   E CE1 1 
ATOM   14423 C CE2 . PHE   I  1 355 ? -17.61895 -9.19417  61.80911  1.000 19.31967  ?  355 PHE   E CE2 1 
ATOM   14424 C CZ  . PHE   I  1 355 ? -17.49184 -7.98318  62.49330  1.000 20.87837  ?  355 PHE   E CZ  1 
ATOM   14425 N N   . ILE   I  1 356 ? -13.30535 -12.55900 66.00501  1.000 26.82842  ?  356 ILE   E N   1 
ATOM   14426 C CA  . ILE   I  1 356 ? -12.77155 -13.57935 66.89649  1.000 30.18760  ?  356 ILE   E CA  1 
ATOM   14427 C C   . ILE   I  1 356 ? -13.26722 -13.31394 68.30413  1.000 43.12807  ?  356 ILE   E C   1 
ATOM   14428 O O   . ILE   I  1 356 ? -13.28614 -12.16135 68.75741  1.000 29.86829  ?  356 ILE   E O   1 
ATOM   14429 C CB  . ILE   I  1 356 ? -11.23419 -13.62957 66.85775  1.000 24.26864  ?  356 ILE   E CB  1 
ATOM   14430 C CG1 . ILE   I  1 356 ? -10.77345 -13.93561 65.41992  1.000 23.56897  ?  356 ILE   E CG1 1 
ATOM   14431 C CG2 . ILE   I  1 356 ? -10.73153 -14.66697 67.86894  1.000 27.30731  ?  356 ILE   E CG2 1 
ATOM   14432 C CD1 . ILE   I  1 356 ? -9.25633  -13.86878 65.21677  1.000 17.67400  ?  356 ILE   E CD1 1 
ATOM   14433 N N   . GLU   I  1 357 ? -13.68641 -14.38299 68.98938  1.000 22.35454  ?  357 GLU   E N   1 
ATOM   14434 C CA  . GLU   I  1 357 ? -14.05208 -14.30397 70.40063  1.000 37.34729  ?  357 GLU   E CA  1 
ATOM   14435 C C   . GLU   I  1 357 ? -12.86595 -14.77697 71.24656  1.000 35.55316  ?  357 GLU   E C   1 
ATOM   14436 O O   . GLU   I  1 357 ? -12.58765 -15.98262 71.32867  1.000 34.24114  ?  357 GLU   E O   1 
ATOM   14437 C CB  . GLU   I  1 357 ? -15.30521 -15.12433 70.67857  1.000 27.86255  ?  357 GLU   E CB  1 
ATOM   14438 C CG  . GLU   I  1 357 ? -15.76585 -15.09425 72.14091  1.000 26.64258  ?  357 GLU   E CG  1 
ATOM   14439 C CD  . GLU   I  1 357 ? -16.46656 -13.80124 72.53717  1.000 79.94255  ?  357 GLU   E CD  1 
ATOM   14440 O OE1 . GLU   I  1 357 ? -17.29463 -13.29621 71.73761  1.000 62.47192  ?  357 GLU   E OE1 1 
ATOM   14441 O OE2 . GLU   I  1 357 ? -16.19963 -13.30167 73.65991  1.000 49.55117  -1 357 GLU   E OE2 1 
ATOM   14442 N N   . ALA   I  1 358 ? -12.16675 -13.81595 71.86034  1.000 18.56723  ?  358 ALA   E N   1 
ATOM   14443 C CA  . ALA   I  1 358 ? -11.01887 -14.10887 72.71456  1.000 37.42890  ?  358 ALA   E CA  1 
ATOM   14444 C C   . ALA   I  1 358 ? -11.43876 -14.95570 73.90341  1.000 31.85647  ?  358 ALA   E C   1 
ATOM   14445 O O   . ALA   I  1 358 ? -12.47877 -14.70622 74.51954  1.000 57.85114  ?  358 ALA   E O   1 
ATOM   14446 C CB  . ALA   I  1 358 ? -10.38468 -12.81202 73.22600  1.000 26.06935  ?  358 ALA   E CB  1 
ATOM   14447 N N   . ASP   I  1 359 ? -10.61792 -15.96223 74.22505  1.000 53.85157  ?  359 ASP   E N   1 
ATOM   14448 C CA  . ASP   I  1 359 ? -10.86550 -16.76938 75.41948  1.000 49.16303  ?  359 ASP   E CA  1 
ATOM   14449 C C   . ASP   I  1 359 ? -10.93228 -15.89545 76.66937  1.000 31.31618  ?  359 ASP   E C   1 
ATOM   14450 O O   . ASP   I  1 359 ? -11.73274 -16.15155 77.57646  1.000 38.07970  ?  359 ASP   E O   1 
ATOM   14451 C CB  . ASP   I  1 359 ? -9.78666  -17.84887 75.58064  1.000 28.22630  ?  359 ASP   E CB  1 
ATOM   14452 C CG  . ASP   I  1 359 ? -9.84503  -18.92551 74.48790  1.000 65.51542  ?  359 ASP   E CG  1 
ATOM   14453 O OD1 . ASP   I  1 359 ? -10.86318 -18.99679 73.76123  1.000 45.53993  ?  359 ASP   E OD1 1 
ATOM   14454 O OD2 . ASP   I  1 359 ? -8.85693  -19.69209 74.34266  1.000 39.25025  -1 359 ASP   E OD2 1 
ATOM   14455 N N   . ASN   I  1 360 ? -10.11577 -14.85367 76.73164  1.000 37.65751  ?  360 ASN   E N   1 
ATOM   14456 C CA  . ASN   I  1 360 ? -10.15225 -13.93712 77.86494  1.000 28.90954  ?  360 ASN   E CA  1 
ATOM   14457 C C   . ASN   I  1 360 ? -11.37350 -13.02697 77.73403  1.000 39.87457  ?  360 ASN   E C   1 
ATOM   14458 O O   . ASN   I  1 360 ? -11.41315 -12.15143 76.85879  1.000 50.54738  ?  360 ASN   E O   1 
ATOM   14459 C CB  . ASN   I  1 360 ? -8.85675  -13.12996 77.92646  1.000 30.19008  ?  360 ASN   E CB  1 
ATOM   14460 C CG  . ASN   I  1 360 ? -8.73018  -12.34714 79.19898  1.000 48.97603  ?  360 ASN   E CG  1 
ATOM   14461 O OD1 . ASN   I  1 360 ? -9.68955  -11.71279 79.65412  1.000 52.08039  ?  360 ASN   E OD1 1 
ATOM   14462 N ND2 . ASN   I  1 360 ? -7.54440  -12.39454 79.80253  1.000 54.93906  ?  360 ASN   E ND2 1 
ATOM   14463 N N   . LYS   I  1 361 ? -12.35533 -13.21368 78.62393  1.000 38.55010  ?  361 LYS   E N   1 
ATOM   14464 C CA  . LYS   I  1 361 ? -13.60781 -12.46436 78.54848  1.000 46.31897  ?  361 LYS   E CA  1 
ATOM   14465 C C   . LYS   I  1 361 ? -13.40130 -10.95557 78.64407  1.000 18.63609  ?  361 LYS   E C   1 
ATOM   14466 O O   . LYS   I  1 361 ? -14.23995 -10.19480 78.14232  1.000 69.01938  ?  361 LYS   E O   1 
ATOM   14467 C CB  . LYS   I  1 361 ? -14.57113 -12.93893 79.64425  1.000 22.79263  ?  361 LYS   E CB  1 
ATOM   14468 N N   . GLU   I  1 362 ? -12.30166 -10.50728 79.24956  1.000 28.94923  ?  362 GLU   E N   1 
ATOM   14469 C CA  . GLU   I  1 362 ? -12.00178 -9.08116  79.34579  1.000 24.41284  ?  362 GLU   E CA  1 
ATOM   14470 C C   . GLU   I  1 362 ? -11.53405 -8.48538  78.02204  1.000 44.69508  ?  362 GLU   E C   1 
ATOM   14471 O O   . GLU   I  1 362 ? -11.44494 -7.25424  77.90592  1.000 36.95757  ?  362 GLU   E O   1 
ATOM   14472 C CB  . GLU   I  1 362 ? -10.93653 -8.83425  80.42457  1.000 33.27142  ?  362 GLU   E CB  1 
ATOM   14473 C CG  . GLU   I  1 362 ? -11.33046 -9.21861  81.81707  1.000 101.32507 ?  362 GLU   E CG  1 
ATOM   14474 C CD  . GLU   I  1 362 ? -10.87287 -8.13523  82.76482  1.000 132.71844 ?  362 GLU   E CD  1 
ATOM   14475 O OE1 . GLU   I  1 362 ? -9.76007  -8.30888  83.32012  1.000 107.91226 ?  362 GLU   E OE1 1 
ATOM   14476 O OE2 . GLU   I  1 362 ? -11.59757 -7.10602  82.88492  1.000 114.03695 ?  362 GLU   E OE2 1 
ATOM   14477 N N   . ILE   I  1 363 ? -11.19668 -9.32775  77.04899  1.000 31.90103  ?  363 ILE   E N   1 
ATOM   14478 C CA  . ILE   I  1 363 ? -10.88839 -8.89551  75.69569  1.000 49.86903  ?  363 ILE   E CA  1 
ATOM   14479 C C   . ILE   I  1 363 ? -12.08148 -9.11968  74.77682  1.000 38.36052  ?  363 ILE   E C   1 
ATOM   14480 O O   . ILE   I  1 363 ? -12.47532 -8.22976  74.01985  1.000 46.71365  ?  363 ILE   E O   1 
ATOM   14481 C CB  . ILE   I  1 363 ? -9.62096  -9.63585  75.19985  1.000 40.10552  ?  363 ILE   E CB  1 
ATOM   14482 C CG1 . ILE   I  1 363 ? -8.38180  -9.12932  75.94473  1.000 34.01285  ?  363 ILE   E CG1 1 
ATOM   14483 C CG2 . ILE   I  1 363 ? -9.40534  -9.44349  73.71319  1.000 19.88873  ?  363 ILE   E CG2 1 
ATOM   14484 C CD1 . ILE   I  1 363 ? -7.09877  -9.87468  75.58526  1.000 37.41436  ?  363 ILE   E CD1 1 
ATOM   14485 N N   . GLY   I  1 364 ? -12.68592 -10.29616 74.88356  1.000 37.38051  ?  364 GLY   E N   1 
ATOM   14486 C CA  . GLY   I  1 364 ? -13.96477 -10.54319 74.29093  1.000 25.27625  ?  364 GLY   E CA  1 
ATOM   14487 C C   . GLY   I  1 364 ? -13.92411 -10.57544 72.77692  1.000 70.51918  ?  364 GLY   E C   1 
ATOM   14488 O O   . GLY   I  1 364 ? -12.98640 -11.08980 72.15164  1.000 35.10998  ?  364 GLY   E O   1 
ATOM   14489 N N   . LEU   I  1 365 ? -14.98062 -10.02784 72.18263  1.000 50.30241  ?  365 LEU   E N   1 
ATOM   14490 C CA  . LEU   I  1 365 ? -15.08851 -10.00270 70.73425  1.000 27.19035  ?  365 LEU   E CA  1 
ATOM   14491 C C   . LEU   I  1 365 ? -14.12576 -8.96172  70.17637  1.000 51.84601  ?  365 LEU   E C   1 
ATOM   14492 O O   . LEU   I  1 365 ? -14.09637 -7.81594  70.64018  1.000 39.14719  ?  365 LEU   E O   1 
ATOM   14493 C CB  . LEU   I  1 365 ? -16.52743 -9.68980  70.31723  1.000 41.29320  ?  365 LEU   E CB  1 
ATOM   14494 C CG  . LEU   I  1 365 ? -16.82974 -9.89107  68.83000  1.000 44.85170  ?  365 LEU   E CG  1 
ATOM   14495 C CD1 . LEU   I  1 365 ? -16.61402 -11.35928 68.44933  1.000 32.08619  ?  365 LEU   E CD1 1 
ATOM   14496 C CD2 . LEU   I  1 365 ? -18.23364 -9.42738  68.50884  1.000 31.12351  ?  365 LEU   E CD2 1 
ATOM   14497 N N   . ILE   I  1 366 ? -13.30242 -9.37558  69.21342  1.000 22.87176  ?  366 ILE   E N   1 
ATOM   14498 C CA  . ILE   I  1 366 ? -12.42239 -8.47006  68.49002  1.000 37.20007  ?  366 ILE   E CA  1 
ATOM   14499 C C   . ILE   I  1 366 ? -12.70503 -8.67152  67.01242  1.000 39.51205  ?  366 ILE   E C   1 
ATOM   14500 O O   . ILE   I  1 366 ? -13.37039 -9.62977  66.60977  1.000 35.03658  ?  366 ILE   E O   1 
ATOM   14501 C CB  . ILE   I  1 366 ? -10.91939 -8.70210  68.78493  1.000 30.56215  ?  366 ILE   E CB  1 
ATOM   14502 C CG1 . ILE   I  1 366 ? -10.47320 -10.06014 68.25912  1.000 34.08653  ?  366 ILE   E CG1 1 
ATOM   14503 C CG2 . ILE   I  1 366 ? -10.60735 -8.59068  70.26167  1.000 22.50557  ?  366 ILE   E CG2 1 
ATOM   14504 C CD1 . ILE   I  1 366 ? -8.98375  -10.16076 68.11831  1.000 34.85672  ?  366 ILE   E CD1 1 
ATOM   14505 N N   . PHE   I  1 367 ? -12.18947 -7.76278  66.19295  1.000 34.22391  ?  367 PHE   E N   1 
ATOM   14506 C CA  . PHE   I  1 367 ? -12.22878 -8.01268  64.76271  1.000 31.19235  ?  367 PHE   E CA  1 
ATOM   14507 C C   . PHE   I  1 367 ? -10.85808 -7.76654  64.14867  1.000 40.46727  ?  367 PHE   E C   1 
ATOM   14508 O O   . PHE   I  1 367 ? -10.02265 -7.02625  64.67891  1.000 35.97372  ?  367 PHE   E O   1 
ATOM   14509 C CB  . PHE   I  1 367 ? -13.35971 -7.19644  64.03253  1.000 30.16039  ?  367 PHE   E CB  1 
ATOM   14510 C CG  . PHE   I  1 367 ? -13.08407 -5.71238  63.84350  1.000 22.16537  ?  367 PHE   E CG  1 
ATOM   14511 C CD1 . PHE   I  1 367 ? -12.10473 -5.26469  62.95148  1.000 38.45831  ?  367 PHE   E CD1 1 
ATOM   14512 C CD2 . PHE   I  1 367 ? -13.88381 -4.76186  64.47883  1.000 33.60690  ?  367 PHE   E CD2 1 
ATOM   14513 C CE1 . PHE   I  1 367 ? -11.87650 -3.90212  62.75108  1.000 22.61425  ?  367 PHE   E CE1 1 
ATOM   14514 C CE2 . PHE   I  1 367 ? -13.67530 -3.38248  64.27604  1.000 31.66819  ?  367 PHE   E CE2 1 
ATOM   14515 C CZ  . PHE   I  1 367 ? -12.67713 -2.94827  63.41169  1.000 28.39034  ?  367 PHE   E CZ  1 
ATOM   14516 N N   . LEU   I  1 368 ? -10.63571 -8.45343  63.04344  1.000 32.92892  ?  368 LEU   E N   1 
ATOM   14517 C CA  . LEU   I  1 368 ? -9.52396  -8.23029  62.14384  1.000 23.88489  ?  368 LEU   E CA  1 
ATOM   14518 C C   . LEU   I  1 368 ? -10.11054 -7.93865  60.76771  1.000 24.63382  ?  368 LEU   E C   1 
ATOM   14519 O O   . LEU   I  1 368 ? -11.08609 -8.58018  60.35677  1.000 33.14555  ?  368 LEU   E O   1 
ATOM   14520 C CB  . LEU   I  1 368 ? -8.62072  -9.46682  62.09692  1.000 21.54960  ?  368 LEU   E CB  1 
ATOM   14521 C CG  . LEU   I  1 368 ? -7.75950  -9.71580  63.32820  1.000 32.14586  ?  368 LEU   E CG  1 
ATOM   14522 C CD1 . LEU   I  1 368 ? -7.25655  -11.14683 63.31715  1.000 27.92681  ?  368 LEU   E CD1 1 
ATOM   14523 C CD2 . LEU   I  1 368 ? -6.57791  -8.74493  63.35455  1.000 29.58071  ?  368 LEU   E CD2 1 
ATOM   14524 N N   . VAL   I  1 369 ? -9.54800  -6.96146  60.06178  1.000 26.23370  ?  369 VAL   E N   1 
ATOM   14525 C CA  . VAL   I  1 369 ? -9.84784  -6.76257  58.64627  1.000 28.57363  ?  369 VAL   E CA  1 
ATOM   14526 C C   . VAL   I  1 369 ? -8.53855  -6.87231  57.87214  1.000 26.05782  ?  369 VAL   E C   1 
ATOM   14527 O O   . VAL   I  1 369 ? -7.59438  -6.11158  58.12823  1.000 35.50476  ?  369 VAL   E O   1 
ATOM   14528 C CB  . VAL   I  1 369 ? -10.53290 -5.41282  58.36986  1.000 34.80517  ?  369 VAL   E CB  1 
ATOM   14529 C CG1 . VAL   I  1 369 ? -10.89375 -5.31083  56.87357  1.000 24.57267  ?  369 VAL   E CG1 1 
ATOM   14530 C CG2 . VAL   I  1 369 ? -11.76412 -5.24717  59.23491  1.000 31.96648  ?  369 VAL   E CG2 1 
ATOM   14531 N N   . PHE   I  1 370 ? -8.48183  -7.80094  56.91957  1.000 34.79049  ?  370 PHE   E N   1 
ATOM   14532 C CA  . PHE   I  1 370 ? -7.33220  -7.91148  56.02761  1.000 16.43556  ?  370 PHE   E CA  1 
ATOM   14533 C C   . PHE   I  1 370 ? -7.64320  -7.16996  54.72730  1.000 30.27632  ?  370 PHE   E C   1 
ATOM   14534 O O   . PHE   I  1 370 ? -8.61532  -7.49409  54.03178  1.000 28.49904  ?  370 PHE   E O   1 
ATOM   14535 C CB  . PHE   I  1 370 ? -6.97978  -9.38273  55.80252  1.000 23.91937  ?  370 PHE   E CB  1 
ATOM   14536 C CG  . PHE   I  1 370 ? -6.60680  -10.08085 57.07056  1.000 33.92694  ?  370 PHE   E CG  1 
ATOM   14537 C CD1 . PHE   I  1 370 ? -5.35155  -9.88263  57.63667  1.000 24.45179  ?  370 PHE   E CD1 1 
ATOM   14538 C CD2 . PHE   I  1 370 ? -7.52763  -10.87573 57.74438  1.000 38.71428  ?  370 PHE   E CD2 1 
ATOM   14539 C CE1 . PHE   I  1 370 ? -5.00450  -10.48790 58.84567  1.000 34.61089  ?  370 PHE   E CE1 1 
ATOM   14540 C CE2 . PHE   I  1 370 ? -7.18390  -11.50039 58.95867  1.000 23.09648  ?  370 PHE   E CE2 1 
ATOM   14541 C CZ  . PHE   I  1 370 ? -5.92718  -11.29620 59.51132  1.000 34.10447  ?  370 PHE   E CZ  1 
ATOM   14542 N N   . ILE   I  1 371 ? -6.83591  -6.15818  54.41797  1.000 33.66834  ?  371 ILE   E N   1 
ATOM   14543 C CA  . ILE   I  1 371 ? -7.18166  -5.13009  53.43488  1.000 29.44705  ?  371 ILE   E CA  1 
ATOM   14544 C C   . ILE   I  1 371 ? -6.28664  -5.29397  52.20950  1.000 30.36678  ?  371 ILE   E C   1 
ATOM   14545 O O   . ILE   I  1 371 ? -5.05496  -5.19787  52.30722  1.000 40.27405  ?  371 ILE   E O   1 
ATOM   14546 C CB  . ILE   I  1 371 ? -7.04785  -3.72218  54.04049  1.000 38.56251  ?  371 ILE   E CB  1 
ATOM   14547 C CG1 . ILE   I  1 371 ? -7.87129  -3.62506  55.33643  1.000 28.15024  ?  371 ILE   E CG1 1 
ATOM   14548 C CG2 . ILE   I  1 371 ? -7.46382  -2.64350  53.03044  1.000 24.03538  ?  371 ILE   E CG2 1 
ATOM   14549 C CD1 . ILE   I  1 371 ? -7.30410  -2.63169  56.33139  1.000 26.01739  ?  371 ILE   E CD1 1 
ATOM   14550 N N   . GLY   I  1 372 ? -6.90649  -5.54001  51.05063  1.000 26.58373  ?  372 GLY   E N   1 
ATOM   14551 C CA  . GLY   I  1 372 ? -6.15080  -5.64479  49.81792  1.000 17.88135  ?  372 GLY   E CA  1 
ATOM   14552 C C   . GLY   I  1 372 ? -5.60928  -4.30484  49.34999  1.000 26.21009  ?  372 GLY   E C   1 
ATOM   14553 O O   . GLY   I  1 372 ? -6.08165  -3.23544  49.73710  1.000 26.38225  ?  372 GLY   E O   1 
ATOM   14554 N N   . MET   I  1 373 ? -4.57555  -4.38005  48.51865  1.000 27.97772  ?  373 MET   E N   1 
ATOM   14555 C CA  . MET   I  1 373 ? -3.98627  -3.20760  47.88207  1.000 41.01322  ?  373 MET   E CA  1 
ATOM   14556 C C   . MET   I  1 373 ? -3.58494  -3.60014  46.47539  1.000 38.76507  ?  373 MET   E C   1 
ATOM   14557 O O   . MET   I  1 373 ? -2.76657  -4.51300  46.30315  1.000 34.05717  ?  373 MET   E O   1 
ATOM   14558 C CB  . MET   I  1 373 ? -2.77286  -2.68964  48.64874  1.000 21.01689  ?  373 MET   E CB  1 
ATOM   14559 C CG  . MET   I  1 373 ? -3.12410  -2.21271  50.02725  1.000 42.84090  ?  373 MET   E CG  1 
ATOM   14560 S SD  . MET   I  1 373 ? -1.67096  -1.71744  50.99893  1.000 36.35096  ?  373 MET   E SD  1 
ATOM   14561 C CE  . MET   I  1 373 ? -0.86604  -0.58205  49.86898  1.000 12.13236  ?  373 MET   E CE  1 
ATOM   14562 N N   . THR   I  1 374 ? -4.15210  -2.89744  45.48566  1.000 26.42788  ?  374 THR   E N   1 
ATOM   14563 C CA  . THR   I  1 374 ? -3.96668  -3.17343  44.06011  1.000 27.79957  ?  374 THR   E CA  1 
ATOM   14564 C C   . THR   I  1 374 ? -3.95449  -4.68057  43.80077  1.000 24.70815  ?  374 THR   E C   1 
ATOM   14565 O O   . THR   I  1 374 ? -4.88583  -5.37992  44.20732  1.000 35.32965  ?  374 THR   E O   1 
ATOM   14566 C CB  . THR   I  1 374 ? -2.70072  -2.46177  43.52452  1.000 36.77737  ?  374 THR   E CB  1 
ATOM   14567 O OG1 . THR   I  1 374 ? -1.50246  -2.96702  44.13919  1.000 31.72984  ?  374 THR   E OG1 1 
ATOM   14568 C CG2 . THR   I  1 374 ? -2.78813  -0.97152  43.80925  1.000 21.35033  ?  374 THR   E CG2 1 
ATOM   14569 N N   . GLU   I  1 375 ? -2.91564  -5.20524  43.15555  1.000 36.45651  ?  375 GLU   E N   1 
ATOM   14570 C CA  . GLU   I  1 375 ? -2.92983  -6.61627  42.76923  1.000 23.98795  ?  375 GLU   E CA  1 
ATOM   14571 C C   . GLU   I  1 375 ? -2.70093  -7.59041  43.93254  1.000 38.83505  ?  375 GLU   E C   1 
ATOM   14572 O O   . GLU   I  1 375 ? -2.89033  -8.80141  43.74743  1.000 24.92862  ?  375 GLU   E O   1 
ATOM   14573 C CB  . GLU   I  1 375 ? -1.87688  -6.87074  41.68756  1.000 36.84567  ?  375 GLU   E CB  1 
ATOM   14574 C CG  . GLU   I  1 375 ? -0.43140  -6.55244  42.14344  1.000 25.50190  ?  375 GLU   E CG  1 
ATOM   14575 C CD  . GLU   I  1 375 ? 0.06983   -5.18957  41.62358  1.000 35.86336  ?  375 GLU   E CD  1 
ATOM   14576 O OE1 . GLU   I  1 375 ? -0.49735  -4.14346  42.01846  1.000 41.19718  ?  375 GLU   E OE1 1 
ATOM   14577 O OE2 . GLU   I  1 375 ? 1.03352   -5.16975  40.81408  1.000 40.23991  -1 375 GLU   E OE2 1 
ATOM   14578 N N   . ILE   I  1 376 ? -2.28447  -7.12332  45.11258  1.000 27.92683  ?  376 ILE   E N   1 
ATOM   14579 C CA  . ILE   I  1 376 ? -2.18404  -8.02612  46.25801  1.000 28.15254  ?  376 ILE   E CA  1 
ATOM   14580 C C   . ILE   I  1 376 ? -3.45205  -7.89048  47.09630  1.000 32.02327  ?  376 ILE   E C   1 
ATOM   14581 O O   . ILE   I  1 376 ? -3.46675  -7.20816  48.12684  1.000 39.58179  ?  376 ILE   E O   1 
ATOM   14582 C CB  . ILE   I  1 376 ? -0.91382  -7.74973  47.08248  1.000 39.07242  ?  376 ILE   E CB  1 
ATOM   14583 C CG1 . ILE   I  1 376 ? 0.31467   -7.80608  46.16109  1.000 28.50493  ?  376 ILE   E CG1 1 
ATOM   14584 C CG2 . ILE   I  1 376 ? -0.80180  -8.73538  48.25692  1.000 17.14566  ?  376 ILE   E CG2 1 
ATOM   14585 C CD1 . ILE   I  1 376 ? 1.59667   -7.27782  46.80311  1.000 49.33441  ?  376 ILE   E CD1 1 
ATOM   14586 N N   . SER   I  1 377 ? -4.53436  -8.53132  46.65126  1.000 23.45174  ?  377 SER   E N   1 
ATOM   14587 C CA  . SER   I  1 377 ? -5.84478  -8.29309  47.23933  1.000 36.99062  ?  377 SER   E CA  1 
ATOM   14588 C C   . SER   I  1 377 ? -6.62737  -9.56326  47.53622  1.000 20.97721  ?  377 SER   E C   1 
ATOM   14589 O O   . SER   I  1 377 ? -7.77398  -9.47286  47.98901  1.000 45.21228  ?  377 SER   E O   1 
ATOM   14590 C CB  . SER   I  1 377 ? -6.67485  -7.37490  46.33103  1.000 14.83039  ?  377 SER   E CB  1 
ATOM   14591 O OG  . SER   I  1 377 ? -6.14861  -6.05828  46.39253  1.000 20.90803  ?  377 SER   E OG  1 
ATOM   14592 N N   . THR   I  1 378 ? -6.04352  -10.73351 47.31531  1.000 34.94562  ?  378 THR   E N   1 
ATOM   14593 C CA  . THR   I  1 378 ? -6.68732  -11.97923 47.70337  1.000 21.07116  ?  378 THR   E CA  1 
ATOM   14594 C C   . THR   I  1 378 ? -6.40708  -12.30014 49.17510  1.000 36.43128  ?  378 THR   E C   1 
ATOM   14595 O O   . THR   I  1 378 ? -5.25066  -12.28624 49.62801  1.000 28.16550  ?  378 THR   E O   1 
ATOM   14596 C CB  . THR   I  1 378 ? -6.22071  -13.12058 46.80113  1.000 33.59394  ?  378 THR   E CB  1 
ATOM   14597 O OG1 . THR   I  1 378 ? -6.72292  -12.90840 45.47470  1.000 28.38804  ?  378 THR   E OG1 1 
ATOM   14598 C CG2 . THR   I  1 378 ? -6.76164  -14.42253 47.31555  1.000 8.80566   ?  378 THR   E CG2 1 
ATOM   14599 N N   . CYS   I  1 379 ? -7.47645  -12.59231 49.91788  1.000 22.42084  ?  379 CYS   E N   1 
ATOM   14600 C CA  . CYS   I  1 379 ? -7.41921  -12.83978 51.35831  1.000 20.70301  ?  379 CYS   E CA  1 
ATOM   14601 C C   . CYS   I  1 379 ? -7.90091  -14.26651 51.59186  1.000 28.77306  ?  379 CYS   E C   1 
ATOM   14602 O O   . CYS   I  1 379 ? -9.10770  -14.53139 51.61337  1.000 34.13565  ?  379 CYS   E O   1 
ATOM   14603 C CB  . CYS   I  1 379 ? -8.27345  -11.83005 52.12201  1.000 21.28429  ?  379 CYS   E CB  1 
ATOM   14604 S SG  . CYS   I  1 379 ? -7.78584  -10.10340 51.84331  1.000 32.80951  ?  379 CYS   E SG  1 
ATOM   14605 N N   . GLU   I  1 380 ? -6.96375  -15.19147 51.75746  1.000 36.93331  ?  380 GLU   E N   1 
ATOM   14606 C CA  . GLU   I  1 380 ? -7.30351  -16.57886 52.03670  1.000 22.43711  ?  380 GLU   E CA  1 
ATOM   14607 C C   . GLU   I  1 380 ? -7.25137  -16.83216 53.53864  1.000 38.72979  ?  380 GLU   E C   1 
ATOM   14608 O O   . GLU   I  1 380 ? -6.18231  -16.72011 54.15678  1.000 37.58950  ?  380 GLU   E O   1 
ATOM   14609 C CB  . GLU   I  1 380 ? -6.37249  -17.55133 51.32265  1.000 33.91369  ?  380 GLU   E CB  1 
ATOM   14610 C CG  . GLU   I  1 380 ? -6.72241  -18.96548 51.70276  1.000 46.68451  ?  380 GLU   E CG  1 
ATOM   14611 C CD  . GLU   I  1 380 ? -5.78170  -19.99374 51.14909  1.000 42.45895  ?  380 GLU   E CD  1 
ATOM   14612 O OE1 . GLU   I  1 380 ? -4.71788  -19.60450 50.61445  1.000 47.48490  ?  380 GLU   E OE1 1 
ATOM   14613 O OE2 . GLU   I  1 380 ? -6.12104  -21.19221 51.26524  1.000 54.57532  -1 380 GLU   E OE2 1 
ATOM   14614 N N   . ALA   I  1 381 ? -8.40625  -17.17078 54.11635  1.000 23.47450  ?  381 ALA   E N   1 
ATOM   14615 C CA  . ALA   I  1 381 ? -8.45427  -17.73785 55.45867  1.000 41.97266  ?  381 ALA   E CA  1 
ATOM   14616 C C   . ALA   I  1 381 ? -8.12629  -19.22990 55.39584  1.000 32.36243  ?  381 ALA   E C   1 
ATOM   14617 O O   . ALA   I  1 381 ? -8.64605  -19.95771 54.53838  1.000 32.97797  ?  381 ALA   E O   1 
ATOM   14618 C CB  . ALA   I  1 381 ? -9.83712  -17.52329 56.08407  1.000 22.45429  ?  381 ALA   E CB  1 
ATOM   14619 N N   . THR   I  1 382 ? -7.25542  -19.68518 56.29562  1.000 28.09767  ?  382 THR   E N   1 
ATOM   14620 C CA  . THR   I  1 382 ? -7.01645  -21.11434 56.48499  1.000 27.67972  ?  382 THR   E CA  1 
ATOM   14621 C C   . THR   I  1 382 ? -7.61663  -21.63764 57.79055  1.000 22.81293  ?  382 THR   E C   1 
ATOM   14622 O O   . THR   I  1 382 ? -7.23490  -22.71316 58.26378  1.000 50.35501  ?  382 THR   E O   1 
ATOM   14623 C CB  . THR   I  1 382 ? -5.52125  -21.40660 56.42778  1.000 17.39217  ?  382 THR   E CB  1 
ATOM   14624 O OG1 . THR   I  1 382 ? -4.83688  -20.64372 57.44349  1.000 26.28388  ?  382 THR   E OG1 1 
ATOM   14625 C CG2 . THR   I  1 382 ? -4.97722  -21.04264 55.04391  1.000 28.17981  ?  382 THR   E CG2 1 
ATOM   14626 N N   . VAL   I  1 383 ? -8.51988  -20.87168 58.39803  1.000 29.79283  ?  383 VAL   E N   1 
ATOM   14627 C CA  . VAL   I  1 383 ? -9.27649  -21.29942 59.56223  1.000 19.13105  ?  383 VAL   E CA  1 
ATOM   14628 C C   . VAL   I  1 383 ? -10.75360 -21.27290 59.18948  1.000 33.13306  ?  383 VAL   E C   1 
ATOM   14629 O O   . VAL   I  1 383 ? -11.15712 -20.68979 58.18061  1.000 28.88487  ?  383 VAL   E O   1 
ATOM   14630 C CB  . VAL   I  1 383 ? -9.01681  -20.42666 60.80587  1.000 39.84343  ?  383 VAL   E CB  1 
ATOM   14631 C CG1 . VAL   I  1 383 ? -7.58426  -20.55448 61.25313  1.000 19.89671  ?  383 VAL   E CG1 1 
ATOM   14632 C CG2 . VAL   I  1 383 ? -9.37314  -18.97501 60.52039  1.000 24.60577  ?  383 VAL   E CG2 1 
ATOM   14633 N N   . SER   I  1 384 ? -11.56071 -21.92385 60.01814  1.000 47.37916  ?  384 SER   E N   1 
ATOM   14634 C CA  . SER   I  1 384 ? -12.98569 -22.06520 59.75882  1.000 27.90009  ?  384 SER   E CA  1 
ATOM   14635 C C   . SER   I  1 384 ? -13.77451 -21.43195 60.89227  1.000 52.29742  ?  384 SER   E C   1 
ATOM   14636 O O   . SER   I  1 384 ? -13.29235 -21.33337 62.03119  1.000 41.06352  ?  384 SER   E O   1 
ATOM   14637 C CB  . SER   I  1 384 ? -13.37373 -23.53794 59.61113  1.000 30.29683  ?  384 SER   E CB  1 
ATOM   14638 O OG  . SER   I  1 384 ? -12.53095 -24.17001 58.65611  1.000 57.50253  ?  384 SER   E OG  1 
ATOM   14639 N N   . GLU   I  1 385 ? -14.98892 -20.98887 60.58023  1.000 36.63404  ?  385 GLU   E N   1 
ATOM   14640 C CA  . GLU   I  1 385 ? -15.84371 -20.50032 61.65318  1.000 45.36237  ?  385 GLU   E CA  1 
ATOM   14641 C C   . GLU   I  1 385 ? -16.03471 -21.61327 62.68470  1.000 44.97956  ?  385 GLU   E C   1 
ATOM   14642 O O   . GLU   I  1 385 ? -16.15538 -22.79668 62.34376  1.000 42.93553  ?  385 GLU   E O   1 
ATOM   14643 C CB  . GLU   I  1 385 ? -17.18052 -20.01783 61.09301  1.000 23.30239  ?  385 GLU   E CB  1 
ATOM   14644 C CG  . GLU   I  1 385 ? -17.04432 -18.94309 60.00814  1.000 37.10204  ?  385 GLU   E CG  1 
ATOM   14645 C CD  . GLU   I  1 385 ? -18.38551 -18.33533 59.60048  1.000 54.01139  ?  385 GLU   E CD  1 
ATOM   14646 O OE1 . GLU   I  1 385 ? -19.42271 -19.00541 59.82108  1.000 52.40045  ?  385 GLU   E OE1 1 
ATOM   14647 O OE2 . GLU   I  1 385 ? -18.40371 -17.18963 59.07294  1.000 39.56211  -1 385 GLU   E OE2 1 
ATOM   14648 N N   . GLY   I  1 386 ? -15.98037 -21.23950 63.95677  1.000 38.38634  ?  386 GLY   E N   1 
ATOM   14649 C CA  . GLY   I  1 386 ? -16.10398 -22.18652 65.04388  1.000 24.54300  ?  386 GLY   E CA  1 
ATOM   14650 C C   . GLY   I  1 386 ? -14.79759 -22.78377 65.53408  1.000 43.25220  ?  386 GLY   E C   1 
ATOM   14651 O O   . GLY   I  1 386 ? -14.73595 -23.27087 66.66462  1.000 37.83698  ?  386 GLY   E O   1 
ATOM   14652 N N   . GLN   I  1 387 ? -13.75811 -22.75928 64.71826  1.000 30.85766  ?  387 GLN   E N   1 
ATOM   14653 C CA  . GLN   I  1 387 ? -12.46691 -23.31134 65.09731  1.000 27.54838  ?  387 GLN   E CA  1 
ATOM   14654 C C   . GLN   I  1 387 ? -11.81994 -22.51102 66.23080  1.000 46.78357  ?  387 GLN   E C   1 
ATOM   14655 O O   . GLN   I  1 387 ? -12.01876 -21.29567 66.35881  1.000 39.92004  ?  387 GLN   E O   1 
ATOM   14656 C CB  . GLN   I  1 387 ? -11.56438 -23.32032 63.86846  1.000 26.40406  ?  387 GLN   E CB  1 
ATOM   14657 C CG  . GLN   I  1 387 ? -10.17765 -23.80065 64.07532  1.000 26.96776  ?  387 GLN   E CG  1 
ATOM   14658 C CD  . GLN   I  1 387 ? -9.43194  -23.81999 62.76904  1.000 34.96823  ?  387 GLN   E CD  1 
ATOM   14659 O OE1 . GLN   I  1 387 ? -10.04040 -23.75132 61.68864  1.000 39.93140  ?  387 GLN   E OE1 1 
ATOM   14660 N NE2 . GLN   I  1 387 ? -8.10682  -23.88487 62.84950  1.000 28.34839  ?  387 GLN   E NE2 1 
ATOM   14661 N N   . HIS   I  1 388 ? -11.04561 -23.20872 67.07012  1.000 27.09182  ?  388 HIS   E N   1 
ATOM   14662 C CA  . HIS   I  1 388 ? -10.24742 -22.56258 68.10696  1.000 38.38565  ?  388 HIS   E CA  1 
ATOM   14663 C C   . HIS   I  1 388 ? -8.80979  -22.41161 67.62913  1.000 52.03529  ?  388 HIS   E C   1 
ATOM   14664 O O   . HIS   I  1 388 ? -8.29223  -23.26238 66.89536  1.000 26.11834  ?  388 HIS   E O   1 
ATOM   14665 C CB  . HIS   I  1 388 ? -10.26492 -23.35311 69.40851  1.000 16.40274  ?  388 HIS   E CB  1 
ATOM   14666 C CG  . HIS   I  1 388 ? -9.53746  -22.68687 70.53415  1.000 33.73532  ?  388 HIS   E CG  1 
ATOM   14667 N ND1 . HIS   I  1 388 ? -8.18775  -22.87138 70.76839  1.000 34.69377  ?  388 HIS   E ND1 1 
ATOM   14668 C CD2 . HIS   I  1 388 ? -9.97431  -21.83825 71.49588  1.000 22.66657  ?  388 HIS   E CD2 1 
ATOM   14669 C CE1 . HIS   I  1 388 ? -7.82484  -22.15806 71.82110  1.000 31.00948  ?  388 HIS   E CE1 1 
ATOM   14670 N NE2 . HIS   I  1 388 ? -8.89051  -21.52474 72.28412  1.000 26.95055  ?  388 HIS   E NE2 1 
ATOM   14671 N N   . VAL   I  1 389 ? -8.17659  -21.31051 68.03218  1.000 18.31638  ?  389 VAL   E N   1 
ATOM   14672 C CA  . VAL   I  1 389 ? -6.78878  -21.02504 67.68335  1.000 30.71957  ?  389 VAL   E CA  1 
ATOM   14673 C C   . VAL   I  1 389 ? -6.10128  -20.41667 68.89679  1.000 29.66316  ?  389 VAL   E C   1 
ATOM   14674 O O   . VAL   I  1 389 ? -6.74126  -19.81550 69.77153  1.000 43.79666  ?  389 VAL   E O   1 
ATOM   14675 C CB  . VAL   I  1 389 ? -6.64979  -20.08004 66.45437  1.000 35.90643  ?  389 VAL   E CB  1 
ATOM   14676 C CG1 . VAL   I  1 389 ? -7.24889  -20.72488 65.18241  1.000 20.70521  ?  389 VAL   E CG1 1 
ATOM   14677 C CG2 . VAL   I  1 389 ? -7.28503  -18.72524 66.72288  1.000 14.99261  ?  389 VAL   E CG2 1 
ATOM   14678 N N   . ASN   I  1 390 ? -4.78326  -20.59334 68.94164  1.000 22.80303  ?  390 ASN   E N   1 
ATOM   14679 C CA  . ASN   I  1 390 ? -3.91461  -19.95624 69.92275  1.000 26.26639  ?  390 ASN   E CA  1 
ATOM   14680 C C   . ASN   I  1 390 ? -3.16607  -18.80427 69.27658  1.000 51.62928  ?  390 ASN   E C   1 
ATOM   14681 O O   . ASN   I  1 390 ? -2.83821  -18.84324 68.08418  1.000 29.10314  ?  390 ASN   E O   1 
ATOM   14682 C CB  . ASN   I  1 390 ? -2.90482  -20.94813 70.51342  1.000 38.96689  ?  390 ASN   E CB  1 
ATOM   14683 C CG  . ASN   I  1 390 ? -3.56893  -22.00323 71.38320  1.000 32.51483  ?  390 ASN   E CG  1 
ATOM   14684 O OD1 . ASN   I  1 390 ? -4.45503  -21.70097 72.19774  1.000 42.99892  ?  390 ASN   E OD1 1 
ATOM   14685 N ND2 . ASN   I  1 390 ? -3.16869  -23.25007 71.19284  1.000 42.45170  ?  390 ASN   E ND2 1 
ATOM   14686 N N   . ARG   I  1 391 ? -2.92108  -17.76974 70.07820  1.000 23.44795  ?  391 ARG   E N   1 
ATOM   14687 C CA  . ARG   I  1 391 ? -2.09748  -16.63942 69.67528  1.000 34.04263  ?  391 ARG   E CA  1 
ATOM   14688 C C   . ARG   I  1 391 ? -0.83911  -17.12168 68.95223  1.000 22.04996  ?  391 ARG   E C   1 
ATOM   14689 O O   . ARG   I  1 391 ? -0.08410  -17.94504 69.47915  1.000 32.72959  ?  391 ARG   E O   1 
ATOM   14690 C CB  . ARG   I  1 391 ? -1.74826  -15.82686 70.92689  1.000 13.41966  ?  391 ARG   E CB  1 
ATOM   14691 C CG  . ARG   I  1 391 ? -1.15920  -14.44295 70.70428  1.000 23.08973  ?  391 ARG   E CG  1 
ATOM   14692 C CD  . ARG   I  1 391 ? -1.33806  -13.56234 71.94133  1.000 32.67760  ?  391 ARG   E CD  1 
ATOM   14693 N NE  . ARG   I  1 391 ? -0.58583  -14.01200 73.10794  1.000 25.03790  ?  391 ARG   E NE  1 
ATOM   14694 C CZ  . ARG   I  1 391 ? 0.61536   -13.54989 73.43390  1.000 66.60744  ?  391 ARG   E CZ  1 
ATOM   14695 N NH1 . ARG   I  1 391 ? 1.25367   -12.67997 72.67069  1.000 26.00288  ?  391 ARG   E NH1 1 
ATOM   14696 N NH2 . ARG   I  1 391 ? 1.19433   -13.96793 74.55272  1.000 26.95072  ?  391 ARG   E NH2 1 
ATOM   14697 N N   . GLY   I  1 392 ? -0.66431  -16.67707 67.69662  1.000 27.68903  ?  392 GLY   E N   1 
ATOM   14698 C CA  . GLY   I  1 392 ? 0.47968   -17.03095 66.86867  1.000 24.11686  ?  392 GLY   E CA  1 
ATOM   14699 C C   . GLY   I  1 392 ? 0.22725   -18.09717 65.81523  1.000 32.89785  ?  392 GLY   E C   1 
ATOM   14700 O O   . GLY   I  1 392 ? 1.09171   -18.29767 64.94257  1.000 31.47358  ?  392 GLY   E O   1 
ATOM   14701 N N   . ASP   I  1 393 ? -0.92583  -18.77700 65.86025  1.000 21.00232  ?  393 ASP   E N   1 
ATOM   14702 C CA  . ASP   I  1 393 ? -1.27307  -19.77502 64.84738  1.000 33.69256  ?  393 ASP   E CA  1 
ATOM   14703 C C   . ASP   I  1 393 ? -1.64075  -19.10340 63.52104  1.000 28.24800  ?  393 ASP   E C   1 
ATOM   14704 O O   . ASP   I  1 393 ? -1.99174  -17.91890 63.47234  1.000 47.30287  ?  393 ASP   E O   1 
ATOM   14705 C CB  . ASP   I  1 393 ? -2.44810  -20.64293 65.31862  1.000 24.33221  ?  393 ASP   E CB  1 
ATOM   14706 C CG  . ASP   I  1 393 ? -2.14716  -21.42938 66.60572  1.000 53.22010  ?  393 ASP   E CG  1 
ATOM   14707 O OD1 . ASP   I  1 393 ? -0.99046  -21.43106 67.09804  1.000 49.82216  ?  393 ASP   E OD1 1 
ATOM   14708 O OD2 . ASP   I  1 393 ? -3.09307  -22.05524 67.13094  1.000 37.92290  -1 393 ASP   E OD2 1 
ATOM   14709 N N   . ASP   I  1 394 ? -1.58315  -19.88030 62.43450  1.000 49.43888  ?  394 ASP   E N   1 
ATOM   14710 C CA  . ASP   I  1 394 ? -1.98486  -19.35279 61.12927  1.000 25.15559  ?  394 ASP   E CA  1 
ATOM   14711 C C   . ASP   I  1 394 ? -3.47241  -19.00130 61.12214  1.000 51.83794  ?  394 ASP   E C   1 
ATOM   14712 O O   . ASP   I  1 394 ? -4.30610  -19.79756 61.56571  1.000 34.66286  ?  394 ASP   E O   1 
ATOM   14713 C CB  . ASP   I  1 394 ? -1.69496  -20.36683 60.01709  1.000 44.65381  ?  394 ASP   E CB  1 
ATOM   14714 C CG  . ASP   I  1 394 ? -0.22597  -20.74123 59.91611  1.000 34.15573  ?  394 ASP   E CG  1 
ATOM   14715 O OD1 . ASP   I  1 394 ? 0.65359   -19.86209 60.11581  1.000 78.51477  ?  394 ASP   E OD1 1 
ATOM   14716 O OD2 . ASP   I  1 394 ? 0.04447   -21.92130 59.60465  1.000 73.76488  -1 394 ASP   E OD2 1 
ATOM   14717 N N   . LEU   I  1 395 ? -3.81185  -17.80344 60.63125  1.000 29.67492  ?  395 LEU   E N   1 
ATOM   14718 C CA  . LEU   I  1 395 ? -5.20175  -17.52273 60.27432  1.000 48.61619  ?  395 LEU   E CA  1 
ATOM   14719 C C   . LEU   I  1 395 ? -5.43355  -17.61594 58.78275  1.000 41.55128  ?  395 LEU   E C   1 
ATOM   14720 O O   . LEU   I  1 395 ? -6.55521  -17.91733 58.34556  1.000 39.01636  ?  395 LEU   E O   1 
ATOM   14721 C CB  . LEU   I  1 395 ? -5.63732  -16.12508 60.72437  1.000 26.08591  ?  395 LEU   E CB  1 
ATOM   14722 C CG  . LEU   I  1 395 ? -5.82821  -15.82071 62.19779  1.000 40.56052  ?  395 LEU   E CG  1 
ATOM   14723 C CD1 . LEU   I  1 395 ? -6.26860  -14.39420 62.28542  1.000 25.55756  ?  395 LEU   E CD1 1 
ATOM   14724 C CD2 . LEU   I  1 395 ? -6.84378  -16.76092 62.82527  1.000 35.58779  ?  395 LEU   E CD2 1 
ATOM   14725 N N   . GLY   I  1 396 ? -4.39149  -17.35308 58.00720  1.000 24.73239  ?  396 GLY   E N   1 
ATOM   14726 C CA  . GLY   I  1 396 ? -4.50804  -17.32629 56.56435  1.000 33.13100  ?  396 GLY   E CA  1 
ATOM   14727 C C   . GLY   I  1 396 ? -3.36760  -16.50474 56.00492  1.000 29.29912  ?  396 GLY   E C   1 
ATOM   14728 O O   . GLY   I  1 396 ? -2.32811  -16.34598 56.65308  1.000 32.75021  ?  396 GLY   E O   1 
ATOM   14729 N N   . MET   I  1 397 ? -3.59418  -15.96128 54.81119  1.000 26.75112  ?  397 MET   E N   1 
ATOM   14730 C CA  . MET   I  1 397 ? -2.52125  -15.22061 54.16286  1.000 25.62802  ?  397 MET   E CA  1 
ATOM   14731 C C   . MET   I  1 397 ? -3.06749  -14.39224 53.01045  1.000 41.13839  ?  397 MET   E C   1 
ATOM   14732 O O   . MET   I  1 397 ? -4.19909  -14.58547 52.55115  1.000 30.36722  ?  397 MET   E O   1 
ATOM   14733 C CB  . MET   I  1 397 ? -1.43826  -16.16815 53.65838  1.000 23.45234  ?  397 MET   E CB  1 
ATOM   14734 C CG  . MET   I  1 397 ? -1.78611  -16.83201 52.33820  1.000 27.93319  ?  397 MET   E CG  1 
ATOM   14735 S SD  . MET   I  1 397 ? -0.95632  -18.40658 52.29217  1.000 38.33422  ?  397 MET   E SD  1 
ATOM   14736 C CE  . MET   I  1 397 ? -1.96872  -19.34066 53.42351  1.000 16.57985  ?  397 MET   E CE  1 
ATOM   14737 N N   . PHE   I  1 398 ? -2.22858  -13.45988 52.55566  1.000 28.84771  ?  398 PHE   E N   1 
ATOM   14738 C CA  . PHE   I  1 398 ? -2.44927  -12.68625 51.34459  1.000 22.13006  ?  398 PHE   E CA  1 
ATOM   14739 C C   . PHE   I  1 398 ? -1.89213  -13.41319 50.11479  1.000 31.90944  ?  398 PHE   E C   1 
ATOM   14740 O O   . PHE   I  1 398 ? -0.90566  -14.14650 50.19351  1.000 41.61989  ?  398 PHE   E O   1 
ATOM   14741 C CB  . PHE   I  1 398 ? -1.76497  -11.32072 51.45187  1.000 22.21190  ?  398 PHE   E CB  1 
ATOM   14742 C CG  . PHE   I  1 398 ? -2.38614  -10.38374 52.43835  1.000 35.85805  ?  398 PHE   E CG  1 
ATOM   14743 C CD1 . PHE   I  1 398 ? -3.59385  -9.73834  52.14238  1.000 22.52584  ?  398 PHE   E CD1 1 
ATOM   14744 C CD2 . PHE   I  1 398 ? -1.73263  -10.08341 53.63876  1.000 29.28400  ?  398 PHE   E CD2 1 
ATOM   14745 C CE1 . PHE   I  1 398 ? -4.16530  -8.83368  53.05009  1.000 34.56591  ?  398 PHE   E CE1 1 
ATOM   14746 C CE2 . PHE   I  1 398 ? -2.28994  -9.17214  54.55975  1.000 25.32870  ?  398 PHE   E CE2 1 
ATOM   14747 C CZ  . PHE   I  1 398 ? -3.50513  -8.54790  54.26648  1.000 32.66476  ?  398 PHE   E CZ  1 
ATOM   14748 N N   . HIS   I  1 399 ? -2.51104  -13.17136 48.96066  1.000 36.68807  ?  399 HIS   E N   1 
ATOM   14749 C CA  . HIS   I  1 399 ? -1.94949  -13.59998 47.68440  1.000 45.08178  ?  399 HIS   E CA  1 
ATOM   14750 C C   . HIS   I  1 399 ? -2.11912  -12.48789 46.66370  1.000 23.54104  ?  399 HIS   E C   1 
ATOM   14751 O O   . HIS   I  1 399 ? -3.06115  -11.69502 46.74020  1.000 51.93960  ?  399 HIS   E O   1 
ATOM   14752 C CB  . HIS   I  1 399 ? -2.62271  -14.86110 47.06997  1.000 21.04186  ?  399 HIS   E CB  1 
ATOM   14753 C CG  . HIS   I  1 399 ? -2.66819  -16.05691 47.97162  1.000 24.79565  ?  399 HIS   E CG  1 
ATOM   14754 N ND1 . HIS   I  1 399 ? -1.64824  -16.98266 48.03734  1.000 32.84057  ?  399 HIS   E ND1 1 
ATOM   14755 C CD2 . HIS   I  1 399 ? -3.63177  -16.49567 48.82026  1.000 40.22386  ?  399 HIS   E CD2 1 
ATOM   14756 C CE1 . HIS   I  1 399 ? -1.97064  -17.92670 48.90517  1.000 50.49363  ?  399 HIS   E CE1 1 
ATOM   14757 N NE2 . HIS   I  1 399 ? -3.17282  -17.66029 49.38730  1.000 21.70460  ?  399 HIS   E NE2 1 
ATOM   14758 N N   . PHE   I  1 400 ? -1.22775  -12.47204 45.67417  1.000 41.01104  ?  400 PHE   E N   1 
ATOM   14759 C CA  . PHE   I  1 400 ? -1.54795  -11.81147 44.41818  1.000 22.48013  ?  400 PHE   E CA  1 
ATOM   14760 C C   . PHE   I  1 400 ? -2.85565  -12.39050 43.88633  1.000 31.11068  ?  400 PHE   E C   1 
ATOM   14761 O O   . PHE   I  1 400 ? -3.02728  -13.61348 43.82060  1.000 41.60075  ?  400 PHE   E O   1 
ATOM   14762 C CB  . PHE   I  1 400 ? -0.41388  -12.01017 43.40717  1.000 40.15789  ?  400 PHE   E CB  1 
ATOM   14763 C CG  . PHE   I  1 400 ? 0.75100   -11.08578 43.60963  1.000 20.08488  ?  400 PHE   E CG  1 
ATOM   14764 C CD1 . PHE   I  1 400 ? 1.61800   -11.25848 44.68992  1.000 39.12912  ?  400 PHE   E CD1 1 
ATOM   14765 C CD2 . PHE   I  1 400 ? 0.98143   -10.03157 42.72891  1.000 40.12218  ?  400 PHE   E CD2 1 
ATOM   14766 C CE1 . PHE   I  1 400 ? 2.68179   -10.38906 44.89725  1.000 23.79704  ?  400 PHE   E CE1 1 
ATOM   14767 C CE2 . PHE   I  1 400 ? 2.05941   -9.15960  42.92068  1.000 35.96809  ?  400 PHE   E CE2 1 
ATOM   14768 C CZ  . PHE   I  1 400 ? 2.90236   -9.33962  44.00721  1.000 38.88315  ?  400 PHE   E CZ  1 
ATOM   14769 N N   . GLY   I  1 401 ? -3.78801  -11.51545 43.55468  1.000 23.69024  ?  401 GLY   E N   1 
ATOM   14770 C CA  . GLY   I  1 401 ? -5.08955  -11.93690 43.07344  1.000 19.61876  ?  401 GLY   E CA  1 
ATOM   14771 C C   . GLY   I  1 401 ? -6.13525  -10.89945 43.42020  1.000 30.07796  ?  401 GLY   E C   1 
ATOM   14772 O O   . GLY   I  1 401 ? -5.83766  -9.84918  43.98893  1.000 36.27078  ?  401 GLY   E O   1 
ATOM   14773 N N   . GLY   I  1 402 ? -7.37938  -11.22405 43.06537  1.000 33.37433  ?  402 GLY   E N   1 
ATOM   14774 C CA  . GLY   I  1 402 ? -8.50730  -10.32867 43.30790  1.000 25.98000  ?  402 GLY   E CA  1 
ATOM   14775 C C   . GLY   I  1 402 ? -9.16756  -10.51204 44.67055  1.000 55.21813  ?  402 GLY   E C   1 
ATOM   14776 O O   . GLY   I  1 402 ? -10.02039 -9.72270  45.13134  1.000 36.83622  ?  402 GLY   E O   1 
ATOM   14777 O OXT . GLY   I  1 402 ? -8.84521  -11.48076 45.36706  1.000 46.01956  -1 402 GLY   E OXT 1 
ATOM   14778 N N   . SER   J  2 1   ? -2.55281  -4.58796  53.66498  1.000 21.76610  ?  404 SER   F N   1 
ATOM   14779 C CA  . SER   J  2 1   ? -2.78971  -3.85837  54.91834  1.000 16.88576  ?  404 SER   F CA  1 
ATOM   14780 C C   . SER   J  2 1   ? -3.71725  -4.64069  55.85618  1.000 28.31097  ?  404 SER   F C   1 
ATOM   14781 O O   . SER   J  2 1   ? -4.46541  -5.50365  55.40551  1.000 31.82640  ?  404 SER   F O   1 
ATOM   14782 C CB  . SER   J  2 1   ? -3.37056  -2.46037  54.62023  1.000 23.16097  ?  404 SER   F CB  1 
ATOM   14783 O OG  . SER   J  2 1   ? -3.55291  -1.69071  55.80211  1.000 25.89927  ?  404 SER   F OG  1 
ATOM   14784 N N   . PHE   J  2 2   ? -3.67417  -4.35499  57.16009  1.000 19.04886  ?  405 PHE   F N   1 
ATOM   14785 C CA  . PHE   J  2 2   ? -4.55935  -5.03733  58.10070  1.000 25.32364  ?  405 PHE   F CA  1 
ATOM   14786 C C   . PHE   J  2 2   ? -4.96606  -4.07979  59.21539  1.000 22.99454  ?  405 PHE   F C   1 
ATOM   14787 O O   . PHE   J  2 2   ? -4.24167  -3.12552  59.53225  1.000 32.29266  ?  405 PHE   F O   1 
ATOM   14788 C CB  . PHE   J  2 2   ? -3.90456  -6.29504  58.69965  1.000 26.00446  ?  405 PHE   F CB  1 
ATOM   14789 C CG  . PHE   J  2 2   ? -3.16145  -6.03935  59.97913  1.000 28.47684  ?  405 PHE   F CG  1 
ATOM   14790 C CD1 . PHE   J  2 2   ? -1.85688  -5.53388  59.95967  1.000 34.77013  ?  405 PHE   F CD1 1 
ATOM   14791 C CD2 . PHE   J  2 2   ? -3.77451  -6.28936  61.20917  1.000 31.91219  ?  405 PHE   F CD2 1 
ATOM   14792 C CE1 . PHE   J  2 2   ? -1.16590  -5.28237  61.14481  1.000 28.49884  ?  405 PHE   F CE1 1 
ATOM   14793 C CE2 . PHE   J  2 2   ? -3.09730  -6.04035  62.40829  1.000 24.63619  ?  405 PHE   F CE2 1 
ATOM   14794 C CZ  . PHE   J  2 2   ? -1.77287  -5.53901  62.37032  1.000 30.82413  ?  405 PHE   F CZ  1 
ATOM   14795 N N   . ALA   J  2 3   ? -6.12555  -4.36009  59.82729  1.000 23.29853  ?  406 ALA   F N   1 
ATOM   14796 C CA  . ALA   J  2 3   ? -6.60748  -3.56987  60.94905  1.000 27.55043  ?  406 ALA   F CA  1 
ATOM   14797 C C   . ALA   J  2 3   ? -7.14120  -4.47494  62.04731  1.000 30.69063  ?  406 ALA   F C   1 
ATOM   14798 O O   . ALA   J  2 3   ? -7.85825  -5.44886  61.77801  1.000 29.59924  ?  406 ALA   F O   1 
ATOM   14799 C CB  . ALA   J  2 3   ? -7.68833  -2.58250  60.52515  1.000 11.35045  ?  406 ALA   F CB  1 
ATOM   14800 N N   . LEU   J  2 4   ? -6.77979  -4.13031  63.28716  1.000 29.03515  ?  407 LEU   F N   1 
ATOM   14801 C CA  . LEU   J  2 4   ? -7.26942  -4.77903  64.49550  1.000 28.31285  ?  407 LEU   F CA  1 
ATOM   14802 C C   . LEU   J  2 4   ? -8.29156  -3.86247  65.15342  1.000 13.53119  ?  407 LEU   F C   1 
ATOM   14803 O O   . LEU   J  2 4   ? -8.02964  -2.66704  65.32291  1.000 33.08841  ?  407 LEU   F O   1 
ATOM   14804 C CB  . LEU   J  2 4   ? -6.11474  -5.07199  65.45825  1.000 17.26097  ?  407 LEU   F CB  1 
ATOM   14805 C CG  . LEU   J  2 4   ? -6.52204  -5.46449  66.88089  1.000 28.98968  ?  407 LEU   F CG  1 
ATOM   14806 C CD1 . LEU   J  2 4   ? -7.18643  -6.85281  66.88678  1.000 15.38442  ?  407 LEU   F CD1 1 
ATOM   14807 C CD2 . LEU   J  2 4   ? -5.31827  -5.41088  67.79794  1.000 21.33188  ?  407 LEU   F CD2 1 
ATOM   14808 N N   . GLY   J  2 5   ? -9.45619  -4.41860  65.50647  1.000 34.35049  ?  408 GLY   F N   1 
ATOM   14809 C CA  . GLY   J  2 5   ? -10.52688 -3.65302  66.13506  1.000 11.06287  ?  408 GLY   F CA  1 
ATOM   14810 C C   . GLY   J  2 5   ? -10.87091 -4.10838  67.54591  1.000 26.58741  ?  408 GLY   F C   1 
ATOM   14811 O O   . GLY   J  2 5   ? -11.10941 -5.30145  67.79453  1.000 32.91211  ?  408 GLY   F O   1 
ATOM   14812 N N   . LEU   J  2 6   ? -10.89378 -3.15730  68.48193  1.000 26.10084  ?  409 LEU   F N   1 
ATOM   14813 C CA  . LEU   J  2 6   ? -11.22628 -3.40987  69.88020  1.000 45.45634  ?  409 LEU   F CA  1 
ATOM   14814 C C   . LEU   J  2 6   ? -12.46832 -2.62181  70.27374  1.000 38.85244  ?  409 LEU   F C   1 
ATOM   14815 O O   . LEU   J  2 6   ? -12.61058 -1.44691  69.90659  1.000 43.91791  ?  409 LEU   F O   1 
ATOM   14816 C CB  . LEU   J  2 6   ? -10.06842 -3.01738  70.80217  1.000 36.73809  ?  409 LEU   F CB  1 
ATOM   14817 C CG  . LEU   J  2 6   ? -8.72233  -3.63560  70.41744  1.000 43.61319  ?  409 LEU   F CG  1 
ATOM   14818 C CD1 . LEU   J  2 6   ? -7.62353  -3.15811  71.35330  1.000 29.69576  ?  409 LEU   F CD1 1 
ATOM   14819 C CD2 . LEU   J  2 6   ? -8.79939  -5.17695  70.36799  1.000 25.24699  ?  409 LEU   F CD2 1 
ATOM   14820 N N   . ARG   J  2 7   ? -13.35118 -3.26921  71.03456  1.000 34.72455  ?  410 ARG   F N   1 
ATOM   14821 C CA  . ARG   J  2 7   ? -14.53254 -2.62450  71.60230  1.000 33.45181  ?  410 ARG   F CA  1 
ATOM   14822 C C   . ARG   J  2 7   ? -14.14563 -1.64462  72.72381  1.000 39.35064  ?  410 ARG   F C   1 
ATOM   14823 O O   . ARG   J  2 7   ? -13.08277 -1.76461  73.34625  1.000 50.61328  ?  410 ARG   F O   1 
ATOM   14824 C CB  . ARG   J  2 7   ? -15.49474 -3.69907  72.12574  1.000 20.30140  ?  410 ARG   F CB  1 
ATOM   14825 C CG  . ARG   J  2 7   ? -15.92999 -4.66923  71.04034  1.000 22.30960  ?  410 ARG   F CG  1 
ATOM   14826 C CD  . ARG   J  2 7   ? -16.76691 -5.82932  71.53785  1.000 33.55503  ?  410 ARG   F CD  1 
ATOM   14827 N NE  . ARG   J  2 7   ? -16.00039 -6.74607  72.36864  1.000 52.64849  ?  410 ARG   F NE  1 
ATOM   14828 C CZ  . ARG   J  2 7   ? -16.02557 -6.75835  73.69566  1.000 43.50870  ?  410 ARG   F CZ  1 
ATOM   14829 N NH1 . ARG   J  2 7   ? -16.83342 -5.96628  74.38109  1.000 46.87269  ?  410 ARG   F NH1 1 
ATOM   14830 N NH2 . ARG   J  2 7   ? -15.20999 -7.57769  74.35287  1.000 52.73642  ?  410 ARG   F NH2 1 
ATOM   14831 N N   . LYS   J  2 8   ? -15.02153 -0.65325  72.97819  1.000 35.21332  ?  411 LYS   F N   1 
ATOM   14832 C CA  . LYS   J  2 8   ? -14.78434 0.27430   74.09181  1.000 53.27399  ?  411 LYS   F CA  1 
ATOM   14833 C C   . LYS   J  2 8   ? -14.77712 -0.46254  75.42099  1.000 45.49900  ?  411 LYS   F C   1 
ATOM   14834 O O   . LYS   J  2 8   ? -13.89772 -0.23416  76.26163  1.000 42.41062  ?  411 LYS   F O   1 
ATOM   14835 C CB  . LYS   J  2 8   ? -15.83370 1.38947   74.12778  1.000 25.39400  ?  411 LYS   F CB  1 
ATOM   14836 N N   . ASP   J  2 9   ? -15.73951 -1.37179  75.61685  1.000 37.92648  ?  412 ASP   F N   1 
ATOM   14837 C CA  . ASP   J  2 9   ? -15.82007 -2.21025  76.81073  1.000 89.35494  ?  412 ASP   F CA  1 
ATOM   14838 C C   . ASP   J  2 9   ? -14.65681 -3.18738  76.95437  1.000 44.67182  ?  412 ASP   F C   1 
ATOM   14839 O O   . ASP   J  2 9   ? -14.59732 -3.92558  77.94707  1.000 75.24900  ?  412 ASP   F O   1 
ATOM   14840 C CB  . ASP   J  2 9   ? -17.13860 -2.98171  76.79851  1.000 62.91048  ?  412 ASP   F CB  1 
ATOM   14841 C CG  . ASP   J  2 9   ? -18.32998 -2.09139  77.09101  1.000 72.34376  ?  412 ASP   F CG  1 
ATOM   14842 O OD1 . ASP   J  2 9   ? -18.12092 -0.92036  77.49414  1.000 74.93346  ?  412 ASP   F OD1 1 
ATOM   14843 O OD2 . ASP   J  2 9   ? -19.47307 -2.56152  76.92054  1.000 97.59481  -1 412 ASP   F OD2 1 
ATOM   14844 N N   . CYS   J  2 10  ? -13.75805 -3.24539  75.98685  1.000 67.33755  ?  413 CYS   F N   1 
ATOM   14845 C CA  . CYS   J  2 10  ? -12.60327 -4.11513  76.09444  1.000 44.26024  ?  413 CYS   F CA  1 
ATOM   14846 C C   . CYS   J  2 10  ? -11.55226 -3.41003  76.94250  1.000 54.80810  ?  413 CYS   F C   1 
ATOM   14847 O O   . CYS   J  2 10  ? -11.15428 -2.27484  76.64110  1.000 52.81216  ?  413 CYS   F O   1 
ATOM   14848 C CB  . CYS   J  2 10  ? -12.07993 -4.46364  74.70295  1.000 35.74769  ?  413 CYS   F CB  1 
ATOM   14849 S SG  . CYS   J  2 10  ? -10.43050 -5.19692  74.64248  1.000 47.62361  ?  413 CYS   F SG  1 
ATOM   14850 N N   . ARG   J  2 11  ? -11.12753 -4.07710  78.01608  1.000 42.10679  ?  414 ARG   F N   1 
ATOM   14851 C CA  . ARG   J  2 11  ? -10.15559 -3.54842  78.96307  1.000 64.47203  ?  414 ARG   F CA  1 
ATOM   14852 C C   . ARG   J  2 11  ? -8.70619  -3.58647  78.42475  1.000 75.80208  ?  414 ARG   F C   1 
ATOM   14853 O O   . ARG   J  2 11  ? -7.76926  -3.23252  79.15012  1.000 48.34610  ?  414 ARG   F O   1 
ATOM   14854 C CB  . ARG   J  2 11  ? -10.28466 -4.31622  80.28716  1.000 36.12219  ?  414 ARG   F CB  1 
ATOM   14855 N N   . ALA   J  2 12  ? -8.49580  -3.98499  77.17058  1.000 65.10648  ?  415 ALA   F N   1 
ATOM   14856 C CA  . ALA   J  2 12  ? -7.17074  -3.96382  76.56606  1.000 54.00682  ?  415 ALA   F CA  1 
ATOM   14857 C C   . ALA   J  2 12  ? -6.92150  -2.61757  75.90348  1.000 47.88563  ?  415 ALA   F C   1 
ATOM   14858 O O   . ALA   J  2 12  ? -7.84750  -1.98241  75.38141  1.000 75.53579  ?  415 ALA   F O   1 
ATOM   14859 C CB  . ALA   J  2 12  ? -7.01984  -5.08204  75.53529  1.000 33.68516  ?  415 ALA   F CB  1 
ATOM   14860 N N   . GLU   J  2 13  ? -5.66226  -2.19334  75.91703  1.000 28.87896  ?  416 GLU   F N   1 
ATOM   14861 C CA  . GLU   J  2 13  ? -5.27302  -0.88180  75.42041  1.000 42.56241  ?  416 GLU   F CA  1 
ATOM   14862 C C   . GLU   J  2 13  ? -4.11525  -1.04638  74.44194  1.000 44.86249  ?  416 GLU   F C   1 
ATOM   14863 O O   . GLU   J  2 13  ? -3.12385  -1.72029  74.74416  1.000 50.03053  ?  416 GLU   F O   1 
ATOM   14864 C CB  . GLU   J  2 13  ? -4.89438  0.06755   76.57284  1.000 31.84079  ?  416 GLU   F CB  1 
ATOM   14865 N N   . ILE   J  2 14  ? -4.26304  -0.44636  73.25976  1.000 38.44258  ?  417 ILE   F N   1 
ATOM   14866 C CA  . ILE   J  2 14  ? -3.20422  -0.46118  72.26432  1.000 46.16843  ?  417 ILE   F CA  1 
ATOM   14867 C C   . ILE   J  2 14  ? -1.91277  0.09358   72.86363  1.000 36.31029  ?  417 ILE   F C   1 
ATOM   14868 O O   . ILE   J  2 14  ? -1.90754  1.08574   73.59810  1.000 44.64882  ?  417 ILE   F O   1 
ATOM   14869 C CB  . ILE   J  2 14  ? -3.65539  0.33409   71.02473  1.000 26.53080  ?  417 ILE   F CB  1 
ATOM   14870 C CG1 . ILE   J  2 14  ? -4.89308  -0.31583  70.40690  1.000 29.90147  ?  417 ILE   F CG1 1 
ATOM   14871 C CG2 . ILE   J  2 14  ? -2.52021  0.46034   69.98870  1.000 33.54790  ?  417 ILE   F CG2 1 
ATOM   14872 C CD1 . ILE   J  2 14  ? -5.47965  0.47272   69.24072  1.000 39.96819  ?  417 ILE   F CD1 1 
ATOM   14873 N N   . VAL   J  2 15  ? -0.80685  -0.56342  72.54466  1.000 45.62012  ?  418 VAL   F N   1 
ATOM   14874 C CA  . VAL   J  2 15  ? 0.49020   -0.16036  73.05886  1.000 27.31973  ?  418 VAL   F CA  1 
ATOM   14875 C C   . VAL   J  2 15  ? 0.90738   1.15557   72.41260  1.000 31.11491  ?  418 VAL   F C   1 
ATOM   14876 O O   . VAL   J  2 15  ? 0.95600   1.26838   71.17938  1.000 51.21850  ?  418 VAL   F O   1 
ATOM   14877 C CB  . VAL   J  2 15  ? 1.50579   -1.28641  72.80917  1.000 50.68344  ?  418 VAL   F CB  1 
ATOM   14878 C CG1 . VAL   J  2 15  ? 2.93148   -0.84601  73.13562  1.000 18.99627  ?  418 VAL   F CG1 1 
ATOM   14879 C CG2 . VAL   J  2 15  ? 1.08990   -2.52939  73.60537  1.000 17.26444  ?  418 VAL   F CG2 1 
ATOM   14880 N N   . GLU   J  2 16  ? 1.24869   2.14722   73.25321  1.000 39.51986  ?  419 GLU   F N   1 
ATOM   14881 C CA  . GLU   J  2 16  ? 1.35769   3.53716   72.80081  1.000 28.99111  ?  419 GLU   F CA  1 
ATOM   14882 C C   . GLU   J  2 16  ? 2.38582   3.72668   71.69285  1.000 39.43204  ?  419 GLU   F C   1 
ATOM   14883 O O   . GLU   J  2 16  ? 2.19670   4.60675   70.84436  1.000 39.55191  ?  419 GLU   F O   1 
ATOM   14884 C CB  . GLU   J  2 16  ? 1.69706   4.48792   73.96326  1.000 29.68410  ?  419 GLU   F CB  1 
ATOM   14885 C CG  . GLU   J  2 16  ? 0.78420   4.48427   75.14372  1.000 104.89620 ?  419 GLU   F CG  1 
ATOM   14886 C CD  . GLU   J  2 16  ? -0.10109  5.71379   75.20321  1.000 127.50382 ?  419 GLU   F CD  1 
ATOM   14887 O OE1 . GLU   J  2 16  ? -0.25651  6.42272   74.15464  1.000 88.40655  ?  419 GLU   F OE1 1 
ATOM   14888 O OE2 . GLU   J  2 16  ? -0.60243  5.95373   76.32958  1.000 95.00144  ?  419 GLU   F OE2 1 
ATOM   14889 N N   . LYS   J  2 17  ? 3.47929   2.94751   71.67253  1.000 32.98684  ?  420 LYS   F N   1 
ATOM   14890 C CA  . LYS   J  2 17  ? 4.49927   3.23920   70.66020  1.000 35.24343  ?  420 LYS   F CA  1 
ATOM   14891 C C   . LYS   J  2 17  ? 3.95872   3.06951   69.24567  1.000 41.76222  ?  420 LYS   F C   1 
ATOM   14892 O O   . LYS   J  2 17  ? 4.49245   3.67353   68.30365  1.000 40.16324  ?  420 LYS   F O   1 
ATOM   14893 C CB  . LYS   J  2 17  ? 5.77285   2.38363   70.84811  1.000 17.71729  ?  420 LYS   F CB  1 
ATOM   14894 C CG  . LYS   J  2 17  ? 5.69447   0.85378   70.59014  1.000 22.71741  ?  420 LYS   F CG  1 
ATOM   14895 C CD  . LYS   J  2 17  ? 7.00731   0.39560   69.91950  1.000 43.85405  ?  420 LYS   F CD  1 
ATOM   14896 C CE  . LYS   J  2 17  ? 7.35566   -1.06944  70.15878  1.000 53.65034  ?  420 LYS   F CE  1 
ATOM   14897 N NZ  . LYS   J  2 17  ? 7.44211   -1.35253  71.61496  1.000 76.54543  ?  420 LYS   F NZ  1 
ATOM   14898 N N   . PHE   J  2 18  ? 2.89532   2.27881   69.07759  1.000 37.29575  ?  421 PHE   F N   1 
ATOM   14899 C CA  . PHE   J  2 18  ? 2.32478   2.05578   67.75727  1.000 60.97365  ?  421 PHE   F CA  1 
ATOM   14900 C C   . PHE   J  2 18  ? 1.39740   3.17454   67.30809  1.000 48.18098  ?  421 PHE   F C   1 
ATOM   14901 O O   . PHE   J  2 18  ? 0.99638   3.18899   66.14136  1.000 42.89466  ?  421 PHE   F O   1 
ATOM   14902 C CB  . PHE   J  2 18  ? 1.59664   0.72101   67.73370  1.000 26.12178  ?  421 PHE   F CB  1 
ATOM   14903 C CG  . PHE   J  2 18  ? 2.49287   -0.42990  68.04622  1.000 37.35183  ?  421 PHE   F CG  1 
ATOM   14904 C CD1 . PHE   J  2 18  ? 3.62889   -0.65951  67.27081  1.000 36.79113  ?  421 PHE   F CD1 1 
ATOM   14905 C CD2 . PHE   J  2 18  ? 2.23744   -1.26583  69.12592  1.000 54.17716  ?  421 PHE   F CD2 1 
ATOM   14906 C CE1 . PHE   J  2 18  ? 4.47719   -1.70880  67.55761  1.000 29.10570  ?  421 PHE   F CE1 1 
ATOM   14907 C CE2 . PHE   J  2 18  ? 3.08759   -2.32316  69.42263  1.000 44.56292  ?  421 PHE   F CE2 1 
ATOM   14908 C CZ  . PHE   J  2 18  ? 4.20912   -2.53958  68.64111  1.000 50.23483  ?  421 PHE   F CZ  1 
ATOM   14909 N N   . THR   J  2 19  ? 1.06993   4.13355   68.17399  1.000 40.75821  ?  422 THR   F N   1 
ATOM   14910 C CA  . THR   J  2 19  ? 0.35290   5.29073   67.65979  1.000 30.98005  ?  422 THR   F CA  1 
ATOM   14911 C C   . THR   J  2 19  ? 1.24502   6.21043   66.82689  1.000 39.02781  ?  422 THR   F C   1 
ATOM   14912 O O   . THR   J  2 19  ? 0.71780   7.12469   66.18312  1.000 37.16323  ?  422 THR   F O   1 
ATOM   14913 C CB  . THR   J  2 19  ? -0.28115  6.07537   68.80636  1.000 42.60466  ?  422 THR   F CB  1 
ATOM   14914 O OG1 . THR   J  2 19  ? 0.73180   6.80208   69.49840  1.000 38.80824  ?  422 THR   F OG1 1 
ATOM   14915 C CG2 . THR   J  2 19  ? -0.96123  5.13788   69.79204  1.000 44.52608  ?  422 THR   F CG2 1 
ATOM   14916 N N   . GLU   J  2 20  ? 2.57258   5.99043   66.80356  1.000 44.83027  ?  423 GLU   F N   1 
ATOM   14917 C CA  . GLU   J  2 20  ? 3.44263   6.75983   65.91467  1.000 43.12024  ?  423 GLU   F CA  1 
ATOM   14918 C C   . GLU   J  2 20  ? 3.55241   6.04129   64.57318  1.000 33.56991  ?  423 GLU   F C   1 
ATOM   14919 O O   . GLU   J  2 20  ? 4.07519   4.91540   64.51976  1.000 49.34254  ?  423 GLU   F O   1 
ATOM   14920 C CB  . GLU   J  2 20  ? 4.82867   6.96928   66.52131  1.000 29.39434  ?  423 GLU   F CB  1 
ATOM   14921 C CG  . GLU   J  2 20  ? 5.57033   8.26061   66.05707  1.000 17.73537  ?  423 GLU   F CG  1 
ATOM   14922 C CD  . GLU   J  2 20  ? 4.77448   9.57818   66.33203  1.000 115.92042 ?  423 GLU   F CD  1 
ATOM   14923 O OE1 . GLU   J  2 20  ? 4.00559   9.69153   67.33345  1.000 79.68694  ?  423 GLU   F OE1 1 
ATOM   14924 O OE2 . GLU   J  2 20  ? 4.91171   10.53316  65.52730  1.000 83.44169  ?  423 GLU   F OE2 1 
ATOM   14925 N N   . PRO   J  2 21  ? 3.03977   6.62052   63.49532  1.000 35.61608  ?  424 PRO   F N   1 
ATOM   14926 C CA  . PRO   J  2 21  ? 3.18284   5.99625   62.17555  1.000 49.05609  ?  424 PRO   F CA  1 
ATOM   14927 C C   . PRO   J  2 21  ? 4.63951   5.67338   61.89024  1.000 34.67066  ?  424 PRO   F C   1 
ATOM   14928 O O   . PRO   J  2 21  ? 5.54399   6.40429   62.29406  1.000 43.36816  ?  424 PRO   F O   1 
ATOM   14929 C CB  . PRO   J  2 21  ? 2.65870   7.06962   61.21374  1.000 17.56222  ?  424 PRO   F CB  1 
ATOM   14930 C CG  . PRO   J  2 21  ? 1.73659   7.90567   62.03907  1.000 32.68085  ?  424 PRO   F CG  1 
ATOM   14931 C CD  . PRO   J  2 21  ? 2.23546   7.84830   63.47011  1.000 31.37182  ?  424 PRO   F CD  1 
ATOM   14932 N N   . GLY   J  2 22  ? 4.85925   4.56261   61.18624  1.000 40.52578  ?  425 GLY   F N   1 
ATOM   14933 C CA  . GLY   J  2 22  ? 6.18550   4.14700   60.79199  1.000 23.20291  ?  425 GLY   F CA  1 
ATOM   14934 C C   . GLY   J  2 22  ? 6.87797   3.20083   61.75613  1.000 31.84256  ?  425 GLY   F C   1 
ATOM   14935 O O   . GLY   J  2 22  ? 7.90687   2.62352   61.39412  1.000 37.72102  ?  425 GLY   F O   1 
ATOM   14936 N N   . THR   J  2 23  ? 6.34928   3.02188   62.96431  1.000 28.78767  ?  426 THR   F N   1 
ATOM   14937 C CA  . THR   J  2 23  ? 6.94576   2.10016   63.92456  1.000 26.45676  ?  426 THR   F CA  1 
ATOM   14938 C C   . THR   J  2 23  ? 6.89392   0.65773   63.41379  1.000 26.42990  ?  426 THR   F C   1 
ATOM   14939 O O   . THR   J  2 23  ? 5.88385   0.20501   62.86962  1.000 55.70062  ?  426 THR   F O   1 
ATOM   14940 C CB  . THR   J  2 23  ? 6.21348   2.22109   65.26791  1.000 35.12863  ?  426 THR   F CB  1 
ATOM   14941 O OG1 . THR   J  2 23  ? 6.31468   3.56632   65.75695  1.000 43.42761  ?  426 THR   F OG1 1 
ATOM   14942 C CG2 . THR   J  2 23  ? 6.76048   1.24223   66.30816  1.000 25.56818  ?  426 THR   F CG2 1 
ATOM   14943 N N   . VAL   J  2 24  ? 7.99170   -0.07048  63.60248  1.000 49.36119  ?  427 VAL   F N   1 
ATOM   14944 C CA  . VAL   J  2 24  ? 8.06055   -1.45164  63.14603  1.000 30.52564  ?  427 VAL   F CA  1 
ATOM   14945 C C   . VAL   J  2 24  ? 7.16821   -2.33473  64.01126  1.000 24.98110  ?  427 VAL   F C   1 
ATOM   14946 O O   . VAL   J  2 24  ? 7.21353   -2.28038  65.24921  1.000 49.83570  ?  427 VAL   F O   1 
ATOM   14947 C CB  . VAL   J  2 24  ? 9.51837   -1.93337  63.15058  1.000 23.39392  ?  427 VAL   F CB  1 
ATOM   14948 C CG1 . VAL   J  2 24  ? 9.58927   -3.44281  63.02504  1.000 16.13333  ?  427 VAL   F CG1 1 
ATOM   14949 C CG2 . VAL   J  2 24  ? 10.25861  -1.27602  62.00823  1.000 23.34039  ?  427 VAL   F CG2 1 
ATOM   14950 N N   . ILE   J  2 25  ? 6.34775   -3.15424  63.35631  1.000 55.60000  ?  428 ILE   F N   1 
ATOM   14951 C CA  . ILE   J  2 25  ? 5.45542   -4.10579  64.01646  1.000 24.49670  ?  428 ILE   F CA  1 
ATOM   14952 C C   . ILE   J  2 25  ? 5.96768   -5.50264  63.67614  1.000 45.90870  ?  428 ILE   F C   1 
ATOM   14953 O O   . ILE   J  2 25  ? 5.80633   -5.98589  62.54700  1.000 37.20920  ?  428 ILE   F O   1 
ATOM   14954 C CB  . ILE   J  2 25  ? 3.98662   -3.93078  63.59080  1.000 42.90308  ?  428 ILE   F CB  1 
ATOM   14955 C CG1 . ILE   J  2 25  ? 3.43719   -2.55109  63.98652  1.000 33.77172  ?  428 ILE   F CG1 1 
ATOM   14956 C CG2 . ILE   J  2 25  ? 3.14256   -5.02695  64.20211  1.000 21.73559  ?  428 ILE   F CG2 1 
ATOM   14957 C CD1 . ILE   J  2 25  ? 1.93144   -2.37842  63.75070  1.000 28.40058  ?  428 ILE   F CD1 1 
ATOM   14958 N N   . ARG   J  2 26  ? 6.60437   -6.15263  64.64366  1.000 34.77085  ?  429 ARG   F N   1 
ATOM   14959 C CA  . ARG   J  2 26  ? 7.06264   -7.52257  64.46056  1.000 33.58321  ?  429 ARG   F CA  1 
ATOM   14960 C C   . ARG   J  2 26  ? 5.88797   -8.45009  64.70322  1.000 34.11340  ?  429 ARG   F C   1 
ATOM   14961 O O   . ARG   J  2 26  ? 5.27027   -8.40174  65.77337  1.000 33.15305  ?  429 ARG   F O   1 
ATOM   14962 C CB  . ARG   J  2 26  ? 8.21602   -7.84380  65.40954  1.000 41.59807  ?  429 ARG   F CB  1 
ATOM   14963 C CG  . ARG   J  2 26  ? 9.44091   -7.02002  65.12459  1.000 35.37612  ?  429 ARG   F CG  1 
ATOM   14964 C CD  . ARG   J  2 26  ? 10.51586  -7.20542  66.16430  1.000 48.99862  ?  429 ARG   F CD  1 
ATOM   14965 N NE  . ARG   J  2 26  ? 11.82733  -7.11507  65.53330  1.000 34.78119  ?  429 ARG   F NE  1 
ATOM   14966 C CZ  . ARG   J  2 26  ? 12.41037  -5.97238  65.19067  1.000 167.28502 ?  429 ARG   F CZ  1 
ATOM   14967 N NH1 . ARG   J  2 26  ? 11.86161  -4.79586  65.47628  1.000 30.41889  ?  429 ARG   F NH1 1 
ATOM   14968 N NH2 . ARG   J  2 26  ? 13.56925  -6.00744  64.53890  1.000 37.24550  ?  429 ARG   F NH2 1 
ATOM   14969 N N   . ILE   J  2 27  ? 5.57461   -9.28933  63.71377  1.000 20.70591  ?  430 ILE   F N   1 
ATOM   14970 C CA  . ILE   J  2 27  ? 4.43985   -10.18769 63.86202  1.000 38.09941  ?  430 ILE   F CA  1 
ATOM   14971 C C   . ILE   J  2 27  ? 4.60102   -11.00757 65.14612  1.000 25.73080  ?  430 ILE   F C   1 
ATOM   14972 O O   . ILE   J  2 27  ? 5.71715   -11.33552 65.56535  1.000 52.53278  ?  430 ILE   F O   1 
ATOM   14973 C CB  . ILE   J  2 27  ? 4.29399   -11.06661 62.60493  1.000 31.60345  ?  430 ILE   F CB  1 
ATOM   14974 C CG1 . ILE   J  2 27  ? 2.89475   -11.71049 62.55995  1.000 26.08781  ?  430 ILE   F CG1 1 
ATOM   14975 C CG2 . ILE   J  2 27  ? 5.45632   -12.08421 62.50577  1.000 29.71801  ?  430 ILE   F CG2 1 
ATOM   14976 C CD1 . ILE   J  2 27  ? 2.61082   -12.42895 61.24301  1.000 23.27130  ?  430 ILE   F CD1 1 
ATOM   14977 N N   . ASN   J  2 28  ? 3.46689   -11.29418 65.79039  1.000 52.58724  ?  431 ASN   F N   1 
ATOM   14978 C CA  . ASN   J  2 28  ? 3.35936   -11.98278 67.07576  1.000 32.03931  ?  431 ASN   F CA  1 
ATOM   14979 C C   . ASN   J  2 28  ? 3.78817   -11.11909 68.25742  1.000 43.60736  ?  431 ASN   F C   1 
ATOM   14980 O O   . ASN   J  2 28  ? 3.61021   -11.54759 69.40082  1.000 34.15233  ?  431 ASN   F O   1 
ATOM   14981 C CB  . ASN   J  2 28  ? 4.17604   -13.28657 67.11405  1.000 27.70905  ?  431 ASN   F CB  1 
ATOM   14982 C CG  . ASN   J  2 28  ? 3.71348   -14.30481 66.09016  1.000 39.61817  ?  431 ASN   F CG  1 
ATOM   14983 O OD1 . ASN   J  2 28  ? 2.57105   -14.27957 65.63059  1.000 44.56883  ?  431 ASN   F OD1 1 
ATOM   14984 N ND2 . ASN   J  2 28  ? 4.61229   -15.20939 65.72071  1.000 31.76602  ?  431 ASN   F ND2 1 
ATOM   14985 N N   . GLU   J  2 29  ? 4.36651   -9.93607  68.03665  1.000 32.01324  ?  432 GLU   F N   1 
ATOM   14986 C CA  . GLU   J  2 29  ? 4.70563   -9.12324  69.20052  1.000 40.65880  ?  432 GLU   F CA  1 
ATOM   14987 C C   . GLU   J  2 29  ? 3.43556   -8.45952  69.76187  1.000 36.43613  ?  432 GLU   F C   1 
ATOM   14988 O O   . GLU   J  2 29  ? 2.37061   -8.46385  69.13484  1.000 51.89870  ?  432 GLU   F O   1 
ATOM   14989 C CB  . GLU   J  2 29  ? 5.80053   -8.10699  68.84406  1.000 24.83525  ?  432 GLU   F CB  1 
ATOM   14990 C CG  . GLU   J  2 29  ? 5.34066   -6.70587  68.48169  1.000 38.11659  ?  432 GLU   F CG  1 
ATOM   14991 C CD  . GLU   J  2 29  ? 6.49546   -5.69744  68.38001  1.000 62.49532  ?  432 GLU   F CD  1 
ATOM   14992 O OE1 . GLU   J  2 29  ? 7.07538   -5.54868  67.28064  1.000 47.50944  ?  432 GLU   F OE1 1 
ATOM   14993 O OE2 . GLU   J  2 29  ? 6.81374   -5.03432  69.39950  1.000 53.76222  -1 432 GLU   F OE2 1 
ATOM   14994 N N   . VAL   J  2 30  ? 3.53366   -7.93897  70.98246  1.000 45.59886  ?  433 VAL   F N   1 
ATOM   14995 C CA  . VAL   J  2 30  ? 2.36004   -7.42349  71.69204  1.000 20.91583  ?  433 VAL   F CA  1 
ATOM   14996 C C   . VAL   J  2 30  ? 1.98935   -6.05114  71.13856  1.000 41.01802  ?  433 VAL   F C   1 
ATOM   14997 O O   . VAL   J  2 30  ? 2.79871   -5.11695  71.19237  1.000 31.85452  ?  433 VAL   F O   1 
ATOM   14998 C CB  . VAL   J  2 30  ? 2.62696   -7.34334  73.20505  1.000 41.86770  ?  433 VAL   F CB  1 
ATOM   14999 C CG1 . VAL   J  2 30  ? 1.41167   -6.78763  73.95804  1.000 31.69529  ?  433 VAL   F CG1 1 
ATOM   15000 C CG2 . VAL   J  2 30  ? 3.04852   -8.70713  73.76849  1.000 26.47093  ?  433 VAL   F CG2 1 
ATOM   15001 N N   . VAL   J  2 31  ? 0.75943   -5.91680  70.62423  1.000 33.66105  ?  434 VAL   F N   1 
ATOM   15002 C CA  . VAL   J  2 31  ? 0.25760   -4.61420  70.18888  1.000 44.74252  ?  434 VAL   F CA  1 
ATOM   15003 C C   . VAL   J  2 31  ? -0.84520  -4.07322  71.09672  1.000 32.33930  ?  434 VAL   F C   1 
ATOM   15004 O O   . VAL   J  2 31  ? -1.12053  -2.86201  71.05528  1.000 31.52096  ?  434 VAL   F O   1 
ATOM   15005 C CB  . VAL   J  2 31  ? -0.21846  -4.62295  68.71476  1.000 35.06262  ?  434 VAL   F CB  1 
ATOM   15006 C CG1 . VAL   J  2 31  ? 0.94867   -4.85260  67.76375  1.000 18.82701  ?  434 VAL   F CG1 1 
ATOM   15007 C CG2 . VAL   J  2 31  ? -1.33079  -5.67355  68.47294  1.000 21.40594  ?  434 VAL   F CG2 1 
ATOM   15008 N N   . ALA   J  2 32  ? -1.47167  -4.90940  71.91740  1.000 30.74152  ?  435 ALA   F N   1 
ATOM   15009 C CA  . ALA   J  2 32  ? -2.41418  -4.42565  72.91787  1.000 34.01916  ?  435 ALA   F CA  1 
ATOM   15010 C C   . ALA   J  2 32  ? -2.38758  -5.38335  74.10133  1.000 43.96155  ?  435 ALA   F C   1 
ATOM   15011 O O   . ALA   J  2 32  ? -2.13838  -6.58556  73.93943  1.000 36.03141  ?  435 ALA   F O   1 
ATOM   15012 C CB  . ALA   J  2 32  ? -3.84112  -4.30141  72.36496  1.000 27.71679  ?  435 ALA   F CB  1 
ATOM   15013 N N   . ALA   J  2 33  ? -2.65611  -4.84122  75.29064  1.000 35.52068  ?  436 ALA   F N   1 
ATOM   15014 C CA  . ALA   J  2 33  ? -2.58893  -5.60613  76.52960  1.000 44.51908  ?  436 ALA   F CA  1 
ATOM   15015 C C   . ALA   J  2 33  ? -3.59336  -5.05430  77.52881  1.000 64.14126  ?  436 ALA   F C   1 
ATOM   15016 O O   . ALA   J  2 33  ? -3.92698  -3.86542  77.50177  1.000 41.53751  ?  436 ALA   F O   1 
ATOM   15017 C CB  . ALA   J  2 33  ? -1.19298  -5.56302  77.14792  1.000 28.62181  ?  436 ALA   F CB  1 
ATOM   15018 N N   . LEU   J  2 34  ? -4.05186  -5.92841  78.42327  1.000 42.15483  ?  437 LEU   F N   1 
ATOM   15019 C CA  . LEU   J  2 34  ? -4.99635  -5.56486  79.48038  1.000 71.87927  ?  437 LEU   F CA  1 
ATOM   15020 C C   . LEU   J  2 34  ? -4.41619  -4.58149  80.50284  1.000 39.74946  ?  437 LEU   F C   1 
ATOM   15021 O O   . LEU   J  2 34  ? -3.34152  -4.80102  81.05212  1.000 46.48721  ?  437 LEU   F O   1 
ATOM   15022 C CB  . LEU   J  2 34  ? -5.48133  -6.82875  80.20138  1.000 38.57101  ?  437 LEU   F CB  1 
ATOM   15023 C CG  . LEU   J  2 34  ? -6.50242  -7.70576  79.46057  1.000 63.69400  ?  437 LEU   F CG  1 
ATOM   15024 C CD1 . LEU   J  2 34  ? -6.84054  -9.00644  80.23694  1.000 44.84873  ?  437 LEU   F CD1 1 
ATOM   15025 C CD2 . LEU   J  2 34  ? -7.76507  -6.89848  79.10834  1.000 66.44829  ?  437 LEU   F CD2 1 
ATOM   15026 N N   . GLY   K  1 56  ? 43.91624  23.42030  81.14813  1.000 42.89989  ?  56  GLY   K N   1 
ATOM   15027 C CA  . GLY   K  1 56  ? 45.17249  23.49554  80.40257  1.000 64.53263  ?  56  GLY   K CA  1 
ATOM   15028 C C   . GLY   K  1 56  ? 45.10729  22.78278  79.06067  1.000 87.78109  ?  56  GLY   K C   1 
ATOM   15029 O O   . GLY   K  1 56  ? 44.02764  22.63856  78.48541  1.000 86.93871  ?  56  GLY   K O   1 
ATOM   15030 N N   . LEU   K  1 57  ? 46.26460  22.36424  78.56483  1.000 47.61640  ?  57  LEU   K N   1 
ATOM   15031 C CA  . LEU   K  1 57  ? 46.37780  21.56755  77.34773  1.000 44.51374  ?  57  LEU   K CA  1 
ATOM   15032 C C   . LEU   K  1 57  ? 45.98584  20.13311  77.62361  1.000 60.65585  ?  57  LEU   K C   1 
ATOM   15033 O O   . LEU   K  1 57  ? 46.38895  19.57178  78.64080  1.000 62.64971  ?  57  LEU   K O   1 
ATOM   15034 C CB  . LEU   K  1 57  ? 47.80963  21.56572  76.80726  1.000 41.15895  ?  57  LEU   K CB  1 
ATOM   15035 C CG  . LEU   K  1 57  ? 48.50552  22.81731  76.27622  1.000 57.42265  ?  57  LEU   K CG  1 
ATOM   15036 C CD1 . LEU   K  1 57  ? 49.95534  22.47146  75.93874  1.000 49.80870  ?  57  LEU   K CD1 1 
ATOM   15037 C CD2 . LEU   K  1 57  ? 47.79055  23.41880  75.07109  1.000 55.88749  ?  57  LEU   K CD2 1 
ATOM   15038 N N   . MET   K  1 58  ? 45.24952  19.51881  76.69960  1.000 56.68698  ?  58  MET   K N   1 
ATOM   15039 C CA  . MET   K  1 58  ? 44.88885  18.11829  76.87646  1.000 55.58569  ?  58  MET   K CA  1 
ATOM   15040 C C   . MET   K  1 58  ? 46.13042  17.23728  76.81950  1.000 46.29407  ?  58  MET   K C   1 
ATOM   15041 O O   . MET   K  1 58  ? 47.09213  17.52911  76.10561  1.000 66.95967  ?  58  MET   K O   1 
ATOM   15042 C CB  . MET   K  1 58  ? 43.88236  17.68560  75.81742  1.000 48.52819  ?  58  MET   K CB  1 
ATOM   15043 C CG  . MET   K  1 58  ? 44.27482  17.99353  74.38755  1.000 63.82991  ?  58  MET   K CG  1 
ATOM   15044 S SD  . MET   K  1 58  ? 43.01135  17.39803  73.24407  1.000 69.69496  ?  58  MET   K SD  1 
ATOM   15045 C CE  . MET   K  1 58  ? 41.78259  18.70477  73.39712  1.000 46.32173  ?  58  MET   K CE  1 
ATOM   15046 N N   . GLN   K  1 59  ? 46.10382  16.14778  77.58534  1.000 60.15068  ?  59  GLN   K N   1 
ATOM   15047 C CA  . GLN   K  1 59  ? 47.28765  15.30507  77.75939  1.000 48.98893  ?  59  GLN   K CA  1 
ATOM   15048 C C   . GLN   K  1 59  ? 47.96924  14.90199  76.45387  1.000 58.71847  ?  59  GLN   K C   1 
ATOM   15049 O O   . GLN   K  1 59  ? 49.20621  14.98073  76.39078  1.000 52.76898  ?  59  GLN   K O   1 
ATOM   15050 C CB  . GLN   K  1 59  ? 46.92606  14.04336  78.55688  1.000 42.73887  ?  59  GLN   K CB  1 
ATOM   15051 C CG  . GLN   K  1 59  ? 48.14259  13.33739  79.10119  1.000 72.29074  ?  59  GLN   K CG  1 
ATOM   15052 C CD  . GLN   K  1 59  ? 48.90268  14.23920  80.05858  1.000 94.88266  ?  59  GLN   K CD  1 
ATOM   15053 O OE1 . GLN   K  1 59  ? 48.30260  15.05828  80.76137  1.000 106.46630 ?  59  GLN   K OE1 1 
ATOM   15054 N NE2 . GLN   K  1 59  ? 50.22934  14.11409  80.07766  1.000 79.50932  ?  59  GLN   K NE2 1 
ATOM   15055 N N   . PRO   K  1 60  ? 47.26153  14.46509  75.39861  1.000 61.41875  ?  60  PRO   K N   1 
ATOM   15056 C CA  . PRO   K  1 60  ? 47.97936  14.11253  74.15599  1.000 43.13855  ?  60  PRO   K CA  1 
ATOM   15057 C C   . PRO   K  1 60  ? 48.81747  15.25456  73.60348  1.000 67.22667  ?  60  PRO   K C   1 
ATOM   15058 O O   . PRO   K  1 60  ? 49.92462  15.00593  73.10125  1.000 46.33006  ?  60  PRO   K O   1 
ATOM   15059 C CB  . PRO   K  1 60  ? 46.84717  13.70583  73.20192  1.000 43.90214  ?  60  PRO   K CB  1 
ATOM   15060 C CG  . PRO   K  1 60  ? 45.72031  13.29429  74.09453  1.000 50.89070  ?  60  PRO   K CG  1 
ATOM   15061 C CD  . PRO   K  1 60  ? 45.81204  14.22617  75.27370  1.000 39.16999  ?  60  PRO   K CD  1 
ATOM   15062 N N   . ILE   K  1 61  ? 48.33010  16.49978  73.69782  1.000 32.13566  ?  61  ILE   K N   1 
ATOM   15063 C CA  . ILE   K  1 61  ? 49.13667  17.64689  73.27790  1.000 56.46926  ?  61  ILE   K CA  1 
ATOM   15064 C C   . ILE   K  1 61  ? 50.31147  17.86481  74.22091  1.000 42.78845  ?  61  ILE   K C   1 
ATOM   15065 O O   . ILE   K  1 61  ? 51.39628  18.27318  73.78874  1.000 47.12242  ?  61  ILE   K O   1 
ATOM   15066 C CB  . ILE   K  1 61  ? 48.27103  18.91390  73.16440  1.000 42.35988  ?  61  ILE   K CB  1 
ATOM   15067 C CG1 . ILE   K  1 61  ? 47.14972  18.68172  72.15389  1.000 32.91174  ?  61  ILE   K CG1 1 
ATOM   15068 C CG2 . ILE   K  1 61  ? 49.11621  20.12727  72.73739  1.000 31.04896  ?  61  ILE   K CG2 1 
ATOM   15069 C CD1 . ILE   K  1 61  ? 46.29309  19.88389  71.94618  1.000 39.50052  ?  61  ILE   K CD1 1 
ATOM   15070 N N   . GLN   K  1 62  ? 50.14521  17.58707  75.51617  1.000 69.04438  ?  62  GLN   K N   1 
ATOM   15071 C CA  . GLN   K  1 62  ? 51.26757  17.72380  76.45222  1.000 19.07781  ?  62  GLN   K CA  1 
ATOM   15072 C C   . GLN   K  1 62  ? 52.36708  16.70872  76.15218  1.000 34.91538  ?  62  GLN   K C   1 
ATOM   15073 O O   . GLN   K  1 62  ? 53.56205  17.04256  76.17771  1.000 27.92325  ?  62  GLN   K O   1 
ATOM   15074 C CB  . GLN   K  1 62  ? 50.78998  17.55364  77.89757  1.000 71.40436  ?  62  GLN   K CB  1 
ATOM   15075 C CG  . GLN   K  1 62  ? 50.59288  18.84932  78.67810  1.000 118.92644 ?  62  GLN   K CG  1 
ATOM   15076 C CD  . GLN   K  1 62  ? 49.74605  18.63395  79.91273  1.000 113.83387 ?  62  GLN   K CD  1 
ATOM   15077 O OE1 . GLN   K  1 62  ? 48.53087  18.52109  79.82090  1.000 151.31552 ?  62  GLN   K OE1 1 
ATOM   15078 N NE2 . GLN   K  1 62  ? 50.37877  18.57154  81.06877  1.000 87.97114  ?  62  GLN   K NE2 1 
ATOM   15079 N N   . GLU   K  1 63  ? 51.97578  15.45908  75.85212  1.000 34.72298  ?  63  GLU   K N   1 
ATOM   15080 C CA  . GLU   K  1 63  ? 52.96697  14.45711  75.46688  1.000 50.55975  ?  63  GLU   K CA  1 
ATOM   15081 C C   . GLU   K  1 63  ? 53.61796  14.81262  74.13658  1.000 52.77916  ?  63  GLU   K C   1 
ATOM   15082 O O   . GLU   K  1 63  ? 54.81988  14.58661  73.94645  1.000 46.09959  ?  63  GLU   K O   1 
ATOM   15083 C CB  . GLU   K  1 63  ? 52.32193  13.08243  75.40192  1.000 34.67934  ?  63  GLU   K CB  1 
ATOM   15084 C CG  . GLU   K  1 63  ? 52.33039  12.34725  76.73090  1.000 72.25423  ?  63  GLU   K CG  1 
ATOM   15085 C CD  . GLU   K  1 63  ? 51.02314  11.64829  77.02615  1.000 59.04653  ?  63  GLU   K CD  1 
ATOM   15086 O OE1 . GLU   K  1 63  ? 50.18275  11.53141  76.10532  1.000 105.50601 ?  63  GLU   K OE1 1 
ATOM   15087 O OE2 . GLU   K  1 63  ? 50.83260  11.21308  78.18431  1.000 133.09954 -1 63  GLU   K OE2 1 
ATOM   15088 N N   . PHE   K  1 64  ? 52.83252  15.37994  73.21030  1.000 46.64380  ?  64  PHE   K N   1 
ATOM   15089 C CA  . PHE   K  1 64  ? 53.36223  15.87817  71.94359  1.000 40.09245  ?  64  PHE   K CA  1 
ATOM   15090 C C   . PHE   K  1 64  ? 54.44005  16.92886  72.17965  1.000 54.12917  ?  64  PHE   K C   1 
ATOM   15091 O O   . PHE   K  1 64  ? 55.56316  16.81061  71.67249  1.000 48.68828  ?  64  PHE   K O   1 
ATOM   15092 C CB  . PHE   K  1 64  ? 52.20753  16.44171  71.10934  1.000 43.18644  ?  64  PHE   K CB  1 
ATOM   15093 C CG  . PHE   K  1 64  ? 52.62571  17.12407  69.83275  1.000 48.35918  ?  64  PHE   K CG  1 
ATOM   15094 C CD1 . PHE   K  1 64  ? 53.09087  16.39212  68.75469  1.000 56.30425  ?  64  PHE   K CD1 1 
ATOM   15095 C CD2 . PHE   K  1 64  ? 52.50463  18.50312  69.69603  1.000 37.39390  ?  64  PHE   K CD2 1 
ATOM   15096 C CE1 . PHE   K  1 64  ? 53.45423  17.03090  67.56994  1.000 42.29617  ?  64  PHE   K CE1 1 
ATOM   15097 C CE2 . PHE   K  1 64  ? 52.85245  19.14901  68.51274  1.000 35.64446  ?  64  PHE   K CE2 1 
ATOM   15098 C CZ  . PHE   K  1 64  ? 53.32709  18.41536  67.44905  1.000 44.38193  ?  64  PHE   K CZ  1 
ATOM   15099 N N   . LYS   K  1 65  ? 54.10986  17.96493  72.96465  1.000 42.02893  ?  65  LYS   K N   1 
ATOM   15100 C CA  . LYS   K  1 65  ? 55.08469  18.99992  73.32235  1.000 36.96557  ?  65  LYS   K CA  1 
ATOM   15101 C C   . LYS   K  1 65  ? 56.29315  18.41085  74.04950  1.000 57.15190  ?  65  LYS   K C   1 
ATOM   15102 O O   . LYS   K  1 65  ? 57.43966  18.80352  73.79613  1.000 48.70759  ?  65  LYS   K O   1 
ATOM   15103 C CB  . LYS   K  1 65  ? 54.41246  20.07152  74.18290  1.000 44.22277  ?  65  LYS   K CB  1 
ATOM   15104 C CG  . LYS   K  1 65  ? 55.29820  21.24554  74.57134  1.000 45.25781  ?  65  LYS   K CG  1 
ATOM   15105 C CD  . LYS   K  1 65  ? 54.43969  22.47496  74.80936  1.000 55.79202  ?  65  LYS   K CD  1 
ATOM   15106 C CE  . LYS   K  1 65  ? 54.42971  22.89219  76.25537  1.000 63.54521  ?  65  LYS   K CE  1 
ATOM   15107 N NZ  . LYS   K  1 65  ? 54.87497  24.30371  76.34954  1.000 74.60998  ?  65  LYS   K NZ  1 
ATOM   15108 N N   . ALA   K  1 66  ? 56.05642  17.47060  74.96699  1.000 48.95846  ?  66  ALA   K N   1 
ATOM   15109 C CA  . ALA   K  1 66  ? 57.17097  16.86542  75.68772  1.000 52.19246  ?  66  ALA   K CA  1 
ATOM   15110 C C   . ALA   K  1 66  ? 58.08953  16.10590  74.73479  1.000 62.50679  ?  66  ALA   K C   1 
ATOM   15111 O O   . ALA   K  1 66  ? 59.31423  16.05443  74.93325  1.000 46.93049  ?  66  ALA   K O   1 
ATOM   15112 C CB  . ALA   K  1 66  ? 56.63975  15.94551  76.78378  1.000 29.48577  ?  66  ALA   K CB  1 
ATOM   15113 N N   . PHE   K  1 67  ? 57.51602  15.51883  73.68391  1.000 69.77800  ?  67  PHE   K N   1 
ATOM   15114 C CA  . PHE   K  1 67  ? 58.33627  14.79517  72.72612  1.000 48.22730  ?  67  PHE   K CA  1 
ATOM   15115 C C   . PHE   K  1 67  ? 59.21789  15.75791  71.93850  1.000 64.21249  ?  67  PHE   K C   1 
ATOM   15116 O O   . PHE   K  1 67  ? 60.42443  15.52654  71.78701  1.000 60.48325  ?  67  PHE   K O   1 
ATOM   15117 C CB  . PHE   K  1 67  ? 57.45843  13.95824  71.78920  1.000 49.44374  ?  67  PHE   K CB  1 
ATOM   15118 C CG  . PHE   K  1 67  ? 58.22273  13.37833  70.65508  1.000 50.41860  ?  67  PHE   K CG  1 
ATOM   15119 C CD1 . PHE   K  1 67  ? 59.02533  12.26812  70.86580  1.000 36.80362  ?  67  PHE   K CD1 1 
ATOM   15120 C CD2 . PHE   K  1 67  ? 58.21097  13.98881  69.39199  1.000 44.37896  ?  67  PHE   K CD2 1 
ATOM   15121 C CE1 . PHE   K  1 67  ? 59.79028  11.73454  69.83310  1.000 43.94189  ?  67  PHE   K CE1 1 
ATOM   15122 C CE2 . PHE   K  1 67  ? 58.97892  13.48097  68.34970  1.000 54.26688  ?  67  PHE   K CE2 1 
ATOM   15123 C CZ  . PHE   K  1 67  ? 59.76769  12.34681  68.56225  1.000 41.32180  ?  67  PHE   K CZ  1 
ATOM   15124 N N   . ILE   K  1 68  ? 58.62585  16.84424  71.43029  1.000 38.33894  ?  68  ILE   K N   1 
ATOM   15125 C CA  . ILE   K  1 68  ? 59.38259  17.86622  70.70573  1.000 40.52121  ?  68  ILE   K CA  1 
ATOM   15126 C C   . ILE   K  1 68  ? 60.58961  18.31267  71.51776  1.000 46.60847  ?  68  ILE   K C   1 
ATOM   15127 O O   . ILE   K  1 68  ? 61.69440  18.48898  70.98873  1.000 44.24047  ?  68  ILE   K O   1 
ATOM   15128 C CB  . ILE   K  1 68  ? 58.46195  19.05724  70.37261  1.000 30.43847  ?  68  ILE   K CB  1 
ATOM   15129 C CG1 . ILE   K  1 68  ? 57.36819  18.62712  69.38288  1.000 37.53716  ?  68  ILE   K CG1 1 
ATOM   15130 C CG2 . ILE   K  1 68  ? 59.26107  20.23186  69.84297  1.000 35.82936  ?  68  ILE   K CG2 1 
ATOM   15131 C CD1 . ILE   K  1 68  ? 56.33914  19.68028  69.11585  1.000 30.51552  ?  68  ILE   K CD1 1 
ATOM   15132 N N   . GLU   K  1 69  ? 60.39415  18.49068  72.82140  1.000 66.75293  ?  69  GLU   K N   1 
ATOM   15133 C CA  . GLU   K  1 69  ? 61.43140  18.96707  73.72077  1.000 41.31591  ?  69  GLU   K CA  1 
ATOM   15134 C C   . GLU   K  1 69  ? 62.39544  17.86741  74.14615  1.000 50.66646  ?  69  GLU   K C   1 
ATOM   15135 O O   . GLU   K  1 69  ? 63.49405  18.17968  74.60846  1.000 51.17382  ?  69  GLU   K O   1 
ATOM   15136 C CB  . GLU   K  1 69  ? 60.77207  19.59638  74.94921  1.000 47.65597  ?  69  GLU   K CB  1 
ATOM   15137 C CG  . GLU   K  1 69  ? 60.17571  20.97604  74.67153  1.000 33.66330  ?  69  GLU   K CG  1 
ATOM   15138 C CD  . GLU   K  1 69  ? 59.13479  21.41584  75.70334  1.000 74.87383  ?  69  GLU   K CD  1 
ATOM   15139 O OE1 . GLU   K  1 69  ? 58.79431  20.61290  76.61502  1.000 47.32179  ?  69  GLU   K OE1 1 
ATOM   15140 O OE2 . GLU   K  1 69  ? 58.65267  22.57101  75.58573  1.000 54.12810  -1 69  GLU   K OE2 1 
ATOM   15141 N N   . SER   K  1 70  ? 62.02061  16.59744  73.98178  1.000 61.75786  ?  70  SER   K N   1 
ATOM   15142 C CA  . SER   K  1 70  ? 62.84382  15.48493  74.43928  1.000 33.53953  ?  70  SER   K CA  1 
ATOM   15143 C C   . SER   K  1 70  ? 64.06572  15.21939  73.56528  1.000 62.30170  ?  70  SER   K C   1 
ATOM   15144 O O   . SER   K  1 70  ? 64.95913  14.48801  74.00333  1.000 47.03458  ?  70  SER   K O   1 
ATOM   15145 C CB  . SER   K  1 70  ? 62.01166  14.19973  74.49991  1.000 46.13851  ?  70  SER   K CB  1 
ATOM   15146 O OG  . SER   K  1 70  ? 61.66661  13.76002  73.19081  1.000 67.47592  ?  70  SER   K OG  1 
ATOM   15147 N N   . ASP   K  1 71  ? 64.12109  15.75398  72.34510  1.000 45.21048  ?  71  ASP   K N   1 
ATOM   15148 C CA  . ASP   K  1 71  ? 65.20068  15.44642  71.40348  1.000 40.49286  ?  71  ASP   K CA  1 
ATOM   15149 C C   . ASP   K  1 71  ? 65.69281  16.76595  70.82579  1.000 46.76180  ?  71  ASP   K C   1 
ATOM   15150 O O   . ASP   K  1 71  ? 64.92290  17.46733  70.13109  1.000 46.66499  ?  71  ASP   K O   1 
ATOM   15151 C CB  . ASP   K  1 71  ? 64.72612  14.48873  70.29654  1.000 49.65837  ?  71  ASP   K CB  1 
ATOM   15152 C CG  . ASP   K  1 71  ? 65.81883  14.15465  69.24723  1.000 88.91824  ?  71  ASP   K CG  1 
ATOM   15153 O OD1 . ASP   K  1 71  ? 66.75394  14.96086  68.99608  1.000 52.84236  ?  71  ASP   K OD1 1 
ATOM   15154 O OD2 . ASP   K  1 71  ? 65.72458  13.06570  68.63426  1.000 66.74732  -1 71  ASP   K OD2 1 
ATOM   15155 N N   . PRO   K  1 72  ? 66.95020  17.12825  71.05209  1.000 57.64616  ?  72  PRO   K N   1 
ATOM   15156 C CA  . PRO   K  1 72  ? 67.42819  18.44183  70.58622  1.000 55.89488  ?  72  PRO   K CA  1 
ATOM   15157 C C   . PRO   K  1 72  ? 67.32576  18.63849  69.07782  1.000 46.74809  ?  72  PRO   K C   1 
ATOM   15158 O O   . PRO   K  1 72  ? 67.12404  19.77208  68.62819  1.000 52.48717  ?  72  PRO   K O   1 
ATOM   15159 C CB  . PRO   K  1 72  ? 68.88449  18.47057  71.07073  1.000 42.11309  ?  72  PRO   K CB  1 
ATOM   15160 C CG  . PRO   K  1 72  ? 69.25161  17.01723  71.29875  1.000 47.95780  ?  72  PRO   K CG  1 
ATOM   15161 C CD  . PRO   K  1 72  ? 67.99389  16.32858  71.71343  1.000 33.91308  ?  72  PRO   K CD  1 
ATOM   15162 N N   . VAL   K  1 73  ? 67.45124  17.57627  68.27759  1.000 46.15454  ?  73  VAL   K N   1 
ATOM   15163 C CA  . VAL   K  1 73  ? 67.31965  17.72302  66.82852  1.000 57.13996  ?  73  VAL   K CA  1 
ATOM   15164 C C   . VAL   K  1 73  ? 65.87600  18.02336  66.44699  1.000 64.73512  ?  73  VAL   K C   1 
ATOM   15165 O O   . VAL   K  1 73  ? 65.60758  18.91762  65.63213  1.000 35.75441  ?  73  VAL   K O   1 
ATOM   15166 C CB  . VAL   K  1 73  ? 67.82144  16.46169  66.11229  1.000 53.88380  ?  73  VAL   K CB  1 
ATOM   15167 C CG1 . VAL   K  1 73  ? 67.74806  16.66484  64.62465  1.000 30.93539  ?  73  VAL   K CG1 1 
ATOM   15168 C CG2 . VAL   K  1 73  ? 69.22964  16.14865  66.53240  1.000 28.77382  ?  73  VAL   K CG2 1 
ATOM   15169 N N   . VAL   K  1 74  ? 64.93257  17.25127  67.00416  1.000 48.60817  ?  74  VAL   K N   1 
ATOM   15170 C CA  . VAL   K  1 74  ? 63.50967  17.49891  66.78030  1.000 39.20552  ?  74  VAL   K CA  1 
ATOM   15171 C C   . VAL   K  1 74  ? 63.15145  18.90894  67.22684  1.000 50.03787  ?  74  VAL   K C   1 
ATOM   15172 O O   . VAL   K  1 74  ? 62.51263  19.67510  66.49169  1.000 54.66771  ?  74  VAL   K O   1 
ATOM   15173 C CB  . VAL   K  1 74  ? 62.66348  16.44391  67.52169  1.000 41.33207  ?  74  VAL   K CB  1 
ATOM   15174 C CG1 . VAL   K  1 74  ? 61.16166  16.73650  67.40842  1.000 24.26020  ?  74  VAL   K CG1 1 
ATOM   15175 C CG2 . VAL   K  1 74  ? 62.96214  15.08092  66.99547  1.000 31.09681  ?  74  VAL   K CG2 1 
ATOM   15176 N N   . HIS   K  1 75  ? 63.56816  19.26776  68.44465  1.000 48.23763  ?  75  HIS   K N   1 
ATOM   15177 C CA  . HIS   K  1 75  ? 63.31959  20.60298  68.97761  1.000 40.93811  ?  75  HIS   K CA  1 
ATOM   15178 C C   . HIS   K  1 75  ? 63.80935  21.68456  68.01640  1.000 29.77877  ?  75  HIS   K C   1 
ATOM   15179 O O   . HIS   K  1 75  ? 63.09038  22.64713  67.71617  1.000 36.69346  ?  75  HIS   K O   1 
ATOM   15180 C CB  . HIS   K  1 75  ? 64.00833  20.72785  70.33371  1.000 32.51094  ?  75  HIS   K CB  1 
ATOM   15181 C CG  . HIS   K  1 75  ? 63.55402  21.89984  71.13883  1.000 65.33861  ?  75  HIS   K CG  1 
ATOM   15182 N ND1 . HIS   K  1 75  ? 63.61930  21.92117  72.51276  1.000 74.78653  ?  75  HIS   K ND1 1 
ATOM   15183 C CD2 . HIS   K  1 75  ? 63.02441  23.08791  70.76648  1.000 66.78601  ?  75  HIS   K CD2 1 
ATOM   15184 C CE1 . HIS   K  1 75  ? 63.14405  23.07122  72.95252  1.000 62.27902  ?  75  HIS   K CE1 1 
ATOM   15185 N NE2 . HIS   K  1 75  ? 62.78260  23.79984  71.91299  1.000 48.95884  ?  75  HIS   K NE2 1 
ATOM   15186 N N   . GLN   K  1 76  ? 65.03660  21.53334  67.51317  1.000 48.75453  ?  76  GLN   K N   1 
ATOM   15187 C CA  . GLN   K  1 76  ? 65.57154  22.52045  66.58484  1.000 27.42961  ?  76  GLN   K CA  1 
ATOM   15188 C C   . GLN   K  1 76  ? 64.70863  22.61163  65.33044  1.000 50.62372  ?  76  GLN   K C   1 
ATOM   15189 O O   . GLN   K  1 76  ? 64.44667  23.71160  64.82837  1.000 39.89070  ?  76  GLN   K O   1 
ATOM   15190 C CB  . GLN   K  1 76  ? 67.02140  22.17359  66.23452  1.000 52.85053  ?  76  GLN   K CB  1 
ATOM   15191 C CG  . GLN   K  1 76  ? 67.76752  23.30668  65.55373  1.000 28.82858  ?  76  GLN   K CG  1 
ATOM   15192 C CD  . GLN   K  1 76  ? 67.70180  24.59933  66.33626  1.000 87.09761  ?  76  GLN   K CD  1 
ATOM   15193 O OE1 . GLN   K  1 76  ? 68.08270  24.64714  67.50953  1.000 46.74409  ?  76  GLN   K OE1 1 
ATOM   15194 N NE2 . GLN   K  1 76  ? 67.21390  25.65685  65.69394  1.000 38.81939  ?  76  GLN   K NE2 1 
ATOM   15195 N N   . GLU   K  1 77  ? 64.24012  21.46306  64.82324  1.000 42.39457  ?  77  GLU   K N   1 
ATOM   15196 C CA  . GLU   K  1 77  ? 63.33640  21.47384  63.67812  1.000 33.38839  ?  77  GLU   K CA  1 
ATOM   15197 C C   . GLU   K  1 77  ? 62.07108  22.27318  63.98247  1.000 60.74920  ?  77  GLU   K C   1 
ATOM   15198 O O   . GLU   K  1 77  ? 61.59727  23.04546  63.13595  1.000 27.35483  ?  77  GLU   K O   1 
ATOM   15199 C CB  . GLU   K  1 77  ? 63.00018  20.04280  63.26868  1.000 32.92931  ?  77  GLU   K CB  1 
ATOM   15200 C CG  . GLU   K  1 77  ? 64.09259  19.40886  62.42064  1.000 28.02499  ?  77  GLU   K CG  1 
ATOM   15201 C CD  . GLU   K  1 77  ? 64.02156  17.88229  62.34978  1.000 60.41402  ?  77  GLU   K CD  1 
ATOM   15202 O OE1 . GLU   K  1 77  ? 63.12845  17.28972  63.00572  1.000 42.07297  ?  77  GLU   K OE1 1 
ATOM   15203 O OE2 . GLU   K  1 77  ? 64.86738  17.28171  61.62870  1.000 35.83100  -1 77  GLU   K OE2 1 
ATOM   15204 N N   . PHE   K  1 78  ? 61.53442  22.14112  65.20292  1.000 29.50019  ?  78  PHE   K N   1 
ATOM   15205 C CA  . PHE   K  1 78  ? 60.34100  22.88797  65.59531  1.000 50.56701  ?  78  PHE   K CA  1 
ATOM   15206 C C   . PHE   K  1 78  ? 60.64335  24.33154  65.96050  1.000 49.83425  ?  78  PHE   K C   1 
ATOM   15207 O O   . PHE   K  1 78  ? 59.73239  25.06668  66.35684  1.000 57.49583  ?  78  PHE   K O   1 
ATOM   15208 C CB  . PHE   K  1 78  ? 59.61506  22.19892  66.76113  1.000 31.14498  ?  78  PHE   K CB  1 
ATOM   15209 C CG  . PHE   K  1 78  ? 58.64743  21.16447  66.31242  1.000 49.60393  ?  78  PHE   K CG  1 
ATOM   15210 C CD1 . PHE   K  1 78  ? 57.35572  21.52863  65.94202  1.000 35.94195  ?  78  PHE   K CD1 1 
ATOM   15211 C CD2 . PHE   K  1 78  ? 59.04120  19.82851  66.19566  1.000 24.39306  ?  78  PHE   K CD2 1 
ATOM   15212 C CE1 . PHE   K  1 78  ? 56.44460  20.56871  65.49491  1.000 33.84228  ?  78  PHE   K CE1 1 
ATOM   15213 C CE2 . PHE   K  1 78  ? 58.14582  18.85702  65.74333  1.000 44.17683  ?  78  PHE   K CE2 1 
ATOM   15214 C CZ  . PHE   K  1 78  ? 56.83960  19.22193  65.39335  1.000 31.58369  ?  78  PHE   K CZ  1 
ATOM   15215 N N   . ILE   K  1 79  ? 61.88727  24.76643  65.83167  1.000 45.36595  ?  79  ILE   K N   1 
ATOM   15216 C CA  . ILE   K  1 79  ? 62.20640  26.17672  65.85959  1.000 39.01582  ?  79  ILE   K CA  1 
ATOM   15217 C C   . ILE   K  1 79  ? 62.42522  26.70300  64.45176  1.000 55.75132  ?  79  ILE   K C   1 
ATOM   15218 O O   . ILE   K  1 79  ? 61.76410  27.64911  64.01946  1.000 32.08548  ?  79  ILE   K O   1 
ATOM   15219 C CB  . ILE   K  1 79  ? 63.43737  26.43973  66.75637  1.000 47.78065  ?  79  ILE   K CB  1 
ATOM   15220 C CG1 . ILE   K  1 79  ? 63.06344  26.24958  68.21491  1.000 34.22764  ?  79  ILE   K CG1 1 
ATOM   15221 C CG2 . ILE   K  1 79  ? 63.97547  27.82863  66.50855  1.000 35.03068  ?  79  ILE   K CG2 1 
ATOM   15222 C CD1 . ILE   K  1 79  ? 64.24059  26.08781  69.08686  1.000 31.47643  ?  79  ILE   K CD1 1 
ATOM   15223 N N   . ASP   K  1 80  ? 63.32969  26.06031  63.70208  1.000 32.04390  ?  80  ASP   K N   1 
ATOM   15224 C CA  . ASP   K  1 80  ? 63.68047  26.55773  62.37838  1.000 48.14404  ?  80  ASP   K CA  1 
ATOM   15225 C C   . ASP   K  1 80  ? 62.47050  26.64294  61.45913  1.000 39.32110  ?  80  ASP   K C   1 
ATOM   15226 O O   . ASP   K  1 80  ? 62.40118  27.54915  60.61891  1.000 48.47443  ?  80  ASP   K O   1 
ATOM   15227 C CB  . ASP   K  1 80  ? 64.75963  25.67079  61.76897  1.000 41.94487  ?  80  ASP   K CB  1 
ATOM   15228 C CG  . ASP   K  1 80  ? 66.03699  25.62879  62.61858  1.000 60.23586  ?  80  ASP   K CG  1 
ATOM   15229 O OD1 . ASP   K  1 80  ? 66.20237  26.48383  63.51418  1.000 58.42172  ?  80  ASP   K OD1 1 
ATOM   15230 O OD2 . ASP   K  1 80  ? 66.87659  24.72106  62.38416  1.000 66.11326  -1 80  ASP   K OD2 1 
ATOM   15231 N N   . MET   K  1 81  ? 61.50370  25.72125  61.60572  1.000 39.99734  ?  81  MET   K N   1 
ATOM   15232 C CA  . MET   K  1 81  ? 60.34650  25.70269  60.71204  1.000 33.70277  ?  81  MET   K CA  1 
ATOM   15233 C C   . MET   K  1 81  ? 59.48349  26.96532  60.84813  1.000 56.47708  ?  81  MET   K C   1 
ATOM   15234 O O   . MET   K  1 81  ? 58.70799  27.26467  59.92369  1.000 43.83877  ?  81  MET   K O   1 
ATOM   15235 C CB  . MET   K  1 81  ? 59.47962  24.44673  60.94857  1.000 33.70777  ?  81  MET   K CB  1 
ATOM   15236 C CG  . MET   K  1 81  ? 58.71525  24.40314  62.27196  1.000 40.17013  ?  81  MET   K CG  1 
ATOM   15237 S SD  . MET   K  1 81  ? 57.60879  22.96869  62.53481  1.000 40.05449  ?  81  MET   K SD  1 
ATOM   15238 C CE  . MET   K  1 81  ? 58.70806  21.56527  62.28155  1.000 36.67255  ?  81  MET   K CE  1 
ATOM   15239 N N   . PHE   K  1 82  ? 59.62555  27.73596  61.94423  1.000 35.16691  ?  82  PHE   K N   1 
ATOM   15240 C CA  . PHE   K  1 82  ? 58.84863  28.94962  62.15426  1.000 60.56710  ?  82  PHE   K CA  1 
ATOM   15241 C C   . PHE   K  1 82  ? 59.57056  30.21093  61.70965  1.000 33.42832  ?  82  PHE   K C   1 
ATOM   15242 O O   . PHE   K  1 82  ? 59.02821  31.30816  61.88995  1.000 96.80987  ?  82  PHE   K O   1 
ATOM   15243 C CB  . PHE   K  1 82  ? 58.48960  29.07015  63.62317  1.000 36.05972  ?  82  PHE   K CB  1 
ATOM   15244 C CG  . PHE   K  1 82  ? 57.41436  28.15509  64.04029  1.000 79.21445  ?  82  PHE   K CG  1 
ATOM   15245 C CD1 . PHE   K  1 82  ? 56.09099  28.49284  63.81865  1.000 33.13992  ?  82  PHE   K CD1 1 
ATOM   15246 C CD2 . PHE   K  1 82  ? 57.71635  26.94455  64.62833  1.000 35.75211  ?  82  PHE   K CD2 1 
ATOM   15247 C CE1 . PHE   K  1 82  ? 55.08239  27.63975  64.19423  1.000 51.90277  ?  82  PHE   K CE1 1 
ATOM   15248 C CE2 . PHE   K  1 82  ? 56.71829  26.08907  65.00559  1.000 53.16958  ?  82  PHE   K CE2 1 
ATOM   15249 C CZ  . PHE   K  1 82  ? 55.39323  26.43513  64.78299  1.000 28.87387  ?  82  PHE   K CZ  1 
ATOM   15250 N N   . GLU   K  1 83  ? 60.77282  30.07977  61.13929  1.000 50.12467  ?  83  GLU   K N   1 
ATOM   15251 C CA  . GLU   K  1 83  ? 61.63621  31.22958  60.89028  1.000 54.88922  ?  83  GLU   K CA  1 
ATOM   15252 C C   . GLU   K  1 83  ? 60.91140  32.32219  60.13177  1.000 63.21789  ?  83  GLU   K C   1 
ATOM   15253 O O   . GLU   K  1 83  ? 60.39960  32.09370  59.03839  1.000 39.48218  ?  83  GLU   K O   1 
ATOM   15254 C CB  . GLU   K  1 83  ? 62.89060  30.79460  60.13929  1.000 30.22306  ?  83  GLU   K CB  1 
ATOM   15255 C CG  . GLU   K  1 83  ? 63.73839  32.02634  59.60081  1.000 39.67014  ?  83  GLU   K CG  1 
ATOM   15256 C CD  . GLU   K  1 83  ? 64.24741  31.69413  58.19526  1.000 96.44271  ?  83  GLU   K CD  1 
ATOM   15257 O OE1 . GLU   K  1 83  ? 63.51831  31.85263  57.15484  1.000 107.75921 ?  83  GLU   K OE1 1 
ATOM   15258 O OE2 . GLU   K  1 83  ? 65.41426  31.25988  58.16772  1.000 120.37374 ?  83  GLU   K OE2 1 
ATOM   15259 N N   . GLY   K  1 84  ? 60.86133  33.51047  60.73317  1.000 86.49171  ?  84  GLY   K N   1 
ATOM   15260 C CA  . GLY   K  1 84  ? 60.24436  34.66071  60.10421  1.000 50.84886  ?  84  GLY   K CA  1 
ATOM   15261 C C   . GLY   K  1 84  ? 58.73832  34.64953  59.99982  1.000 83.93468  ?  84  GLY   K C   1 
ATOM   15262 O O   . GLY   K  1 84  ? 58.16749  35.55353  59.38657  1.000 69.05192  ?  84  GLY   K O   1 
ATOM   15263 N N   . ILE   K  1 85  ? 58.07265  33.65750  60.57736  1.000 68.78056  ?  85  ILE   K N   1 
ATOM   15264 C CA  . ILE   K  1 85  ? 56.61565  33.61289  60.55487  1.000 48.39038  ?  85  ILE   K CA  1 
ATOM   15265 C C   . ILE   K  1 85  ? 56.07852  34.66113  61.51311  1.000 58.59962  ?  85  ILE   K C   1 
ATOM   15266 O O   . ILE   K  1 85  ? 56.38084  34.65364  62.71614  1.000 52.74629  ?  85  ILE   K O   1 
ATOM   15267 C CB  . ILE   K  1 85  ? 56.10445  32.20801  60.90294  1.000 41.80637  ?  85  ILE   K CB  1 
ATOM   15268 C CG1 . ILE   K  1 85  ? 56.56931  31.21866  59.83026  1.000 57.08098  ?  85  ILE   K CG1 1 
ATOM   15269 C CG2 . ILE   K  1 85  ? 54.57962  32.21237  61.11522  1.000 43.92262  ?  85  ILE   K CG2 1 
ATOM   15270 C CD1 . ILE   K  1 85  ? 55.79953  29.93909  59.77728  1.000 48.98656  ?  85  ILE   K CD1 1 
ATOM   15271 N N   . GLN   K  1 86  ? 55.33561  35.60755  60.95907  1.000 55.92952  ?  86  GLN   K N   1 
ATOM   15272 C CA  . GLN   K  1 86  ? 54.82545  36.71408  61.74039  1.000 87.54470  ?  86  GLN   K CA  1 
ATOM   15273 C C   . GLN   K  1 86  ? 53.42841  36.44126  62.29885  1.000 38.38412  ?  86  GLN   K C   1 
ATOM   15274 O O   . GLN   K  1 86  ? 53.04860  37.05510  63.30309  1.000 85.08073  ?  86  GLN   K O   1 
ATOM   15275 C CB  . GLN   K  1 86  ? 54.80471  37.99763  60.90190  1.000 51.68019  ?  86  GLN   K CB  1 
ATOM   15276 C CG  . GLN   K  1 86  ? 56.02402  38.27679  60.14002  1.000 25.88164  ?  86  GLN   K CG  1 
ATOM   15277 C CD  . GLN   K  1 86  ? 57.17242  38.55569  61.07346  1.000 50.40559  ?  86  GLN   K CD  1 
ATOM   15278 O OE1 . GLN   K  1 86  ? 56.95270  39.12587  62.16367  1.000 35.80357  ?  86  GLN   K OE1 1 
ATOM   15279 N NE2 . GLN   K  1 86  ? 58.38364  38.04023  60.73677  1.000 57.77861  ?  86  GLN   K NE2 1 
ATOM   15280 N N   . ASP   K  1 87  ? 52.67855  35.49705  61.72671  1.000 88.93315  ?  87  ASP   K N   1 
ATOM   15281 C CA  . ASP   K  1 87  ? 51.32409  35.20754  62.18224  1.000 55.20555  ?  87  ASP   K CA  1 
ATOM   15282 C C   . ASP   K  1 87  ? 51.27287  34.01726  63.13458  1.000 44.35739  ?  87  ASP   K C   1 
ATOM   15283 O O   . ASP   K  1 87  ? 52.22037  33.24291  63.28030  1.000 64.74506  ?  87  ASP   K O   1 
ATOM   15284 C CB  . ASP   K  1 87  ? 50.40401  34.93097  60.99241  1.000 47.46011  ?  87  ASP   K CB  1 
ATOM   15285 C CG  . ASP   K  1 87  ? 50.55338  35.96006  59.91240  1.000 120.22561 ?  87  ASP   K CG  1 
ATOM   15286 O OD1 . ASP   K  1 87  ? 51.04454  37.07169  60.22210  1.000 100.48132 ?  87  ASP   K OD1 1 
ATOM   15287 O OD2 . ASP   K  1 87  ? 50.18902  35.63638  58.74734  1.000 98.52053  -1 87  ASP   K OD2 1 
ATOM   15288 N N   . SER   K  1 88  ? 50.12306  33.86812  63.75046  1.000 47.56847  ?  88  SER   K N   1 
ATOM   15289 C CA  . SER   K  1 88  ? 49.86951  32.76586  64.65609  1.000 36.64610  ?  88  SER   K CA  1 
ATOM   15290 C C   . SER   K  1 88  ? 49.57142  31.49148  63.85985  1.000 79.03462  ?  88  SER   K C   1 
ATOM   15291 O O   . SER   K  1 88  ? 48.72124  31.51159  62.95795  1.000 46.53482  ?  88  SER   K O   1 
ATOM   15292 C CB  . SER   K  1 88  ? 48.71010  33.11982  65.57497  1.000 37.69520  ?  88  SER   K CB  1 
ATOM   15293 O OG  . SER   K  1 88  ? 49.10936  33.11051  66.93628  1.000 53.82549  ?  88  SER   K OG  1 
ATOM   15294 N N   . PRO   K  1 89  ? 50.25432  30.35466  64.15430  1.000 55.05180  ?  89  PRO   K N   1 
ATOM   15295 C CA  . PRO   K  1 89  ? 51.25432  30.11197  65.20583  1.000 31.56831  ?  89  PRO   K CA  1 
ATOM   15296 C C   . PRO   K  1 89  ? 52.64775  30.65814  64.88360  1.000 59.27343  ?  89  PRO   K C   1 
ATOM   15297 O O   . PRO   K  1 89  ? 53.13987  30.48197  63.77126  1.000 41.87189  ?  89  PRO   K O   1 
ATOM   15298 C CB  . PRO   K  1 89  ? 51.32079  28.58039  65.29784  1.000 53.93697  ?  89  PRO   K CB  1 
ATOM   15299 C CG  . PRO   K  1 89  ? 50.46266  28.03405  64.16215  1.000 51.60663  ?  89  PRO   K CG  1 
ATOM   15300 C CD  . PRO   K  1 89  ? 50.14551  29.19248  63.26535  1.000 46.20304  ?  89  PRO   K CD  1 
ATOM   15301 N N   . ARG   K  1 90  ? 53.32802  31.28192  65.84874  1.000 35.92860  ?  90  ARG   K N   1 
ATOM   15302 C CA  . ARG   K  1 90  ? 54.68930  31.75449  65.63198  1.000 52.92757  ?  90  ARG   K CA  1 
ATOM   15303 C C   . ARG   K  1 90  ? 55.74088  30.84035  66.25017  1.000 43.61248  ?  90  ARG   K C   1 
ATOM   15304 O O   . ARG   K  1 90  ? 56.92081  30.97341  65.93551  1.000 43.19987  ?  90  ARG   K O   1 
ATOM   15305 C CB  . ARG   K  1 90  ? 54.87049  33.17380  66.18725  1.000 37.31871  ?  90  ARG   K CB  1 
ATOM   15306 C CG  . ARG   K  1 90  ? 54.41159  33.40409  67.48586  1.000 113.42985 ?  90  ARG   K CG  1 
ATOM   15307 C CD  . ARG   K  1 90  ? 54.19546  34.86976  67.68601  1.000 97.23183  ?  90  ARG   K CD  1 
ATOM   15308 N NE  . ARG   K  1 90  ? 53.42745  35.55103  66.65127  1.000 98.58659  ?  90  ARG   K NE  1 
ATOM   15309 C CZ  . ARG   K  1 90  ? 52.10299  35.61225  66.59599  1.000 40.94664  ?  90  ARG   K CZ  1 
ATOM   15310 N NH1 . ARG   K  1 90  ? 51.34555  34.84982  67.35067  1.000 99.85048  ?  90  ARG   K NH1 1 
ATOM   15311 N NH2 . ARG   K  1 90  ? 51.52512  36.45825  65.75275  1.000 58.61246  ?  90  ARG   K NH2 1 
ATOM   15312 N N   . ASN   K  1 91  ? 55.35864  29.90196  67.10455  1.000 42.91891  ?  91  ASN   K N   1 
ATOM   15313 C CA  . ASN   K  1 91  ? 56.31645  28.95765  67.65801  1.000 47.39904  ?  91  ASN   K CA  1 
ATOM   15314 C C   . ASN   K  1 91  ? 55.57197  27.67296  67.94018  1.000 46.02559  ?  91  ASN   K C   1 
ATOM   15315 O O   . ASN   K  1 91  ? 54.35590  27.56532  67.72642  1.000 52.57891  ?  91  ASN   K O   1 
ATOM   15316 C CB  . ASN   K  1 91  ? 56.97170  29.50013  68.93009  1.000 39.40045  ?  91  ASN   K CB  1 
ATOM   15317 C CG  . ASN   K  1 91  ? 55.94524  30.10292  69.86272  1.000 50.07796  ?  91  ASN   K CG  1 
ATOM   15318 O OD1 . ASN   K  1 91  ? 55.08268  29.40590  70.40731  1.000 60.26799  ?  91  ASN   K OD1 1 
ATOM   15319 N ND2 . ASN   K  1 91  ? 56.01317  31.40603  70.03230  1.000 46.10366  ?  91  ASN   K ND2 1 
ATOM   15320 N N   . TYR   K  1 92  ? 56.31757  26.69008  68.43081  1.000 42.08942  ?  92  TYR   K N   1 
ATOM   15321 C CA  . TYR   K  1 92  ? 55.67380  25.41635  68.68206  1.000 35.83116  ?  92  TYR   K CA  1 
ATOM   15322 C C   . TYR   K  1 92  ? 54.72949  25.50690  69.87721  1.000 39.92514  ?  92  TYR   K C   1 
ATOM   15323 O O   . TYR   K  1 92  ? 53.74808  24.75644  69.94207  1.000 44.64175  ?  92  TYR   K O   1 
ATOM   15324 C CB  . TYR   K  1 92  ? 56.72392  24.29288  68.81767  1.000 25.04818  ?  92  TYR   K CB  1 
ATOM   15325 C CG  . TYR   K  1 92  ? 57.50959  24.20230  70.10301  1.000 30.51456  ?  92  TYR   K CG  1 
ATOM   15326 C CD1 . TYR   K  1 92  ? 56.98714  23.54050  71.21286  1.000 28.73246  ?  92  TYR   K CD1 1 
ATOM   15327 C CD2 . TYR   K  1 92  ? 58.82120  24.70480  70.18284  1.000 36.94836  ?  92  TYR   K CD2 1 
ATOM   15328 C CE1 . TYR   K  1 92  ? 57.71755  23.42798  72.38608  1.000 47.71387  ?  92  TYR   K CE1 1 
ATOM   15329 C CE2 . TYR   K  1 92  ? 59.56023  24.59307  71.35472  1.000 44.80867  ?  92  TYR   K CE2 1 
ATOM   15330 C CZ  . TYR   K  1 92  ? 58.99982  23.95718  72.45239  1.000 40.35203  ?  92  TYR   K CZ  1 
ATOM   15331 O OH  . TYR   K  1 92  ? 59.69785  23.83785  73.61889  1.000 57.10848  ?  92  TYR   K OH  1 
ATOM   15332 N N   . GLN   K  1 93  ? 54.94326  26.46191  70.78512  1.000 38.41836  ?  93  GLN   K N   1 
ATOM   15333 C CA  . GLN   K  1 93  ? 54.01518  26.57940  71.90740  1.000 51.02614  ?  93  GLN   K CA  1 
ATOM   15334 C C   . GLN   K  1 93  ? 52.65551  27.08947  71.44517  1.000 37.07471  ?  93  GLN   K C   1 
ATOM   15335 O O   . GLN   K  1 93  ? 51.61355  26.59408  71.89080  1.000 42.48482  ?  93  GLN   K O   1 
ATOM   15336 C CB  . GLN   K  1 93  ? 54.57476  27.50069  72.98650  1.000 31.89984  ?  93  GLN   K CB  1 
ATOM   15337 C CG  . GLN   K  1 93  ? 55.59509  26.83395  73.90980  1.000 48.62987  ?  93  GLN   K CG  1 
ATOM   15338 C CD  . GLN   K  1 93  ? 57.03102  27.10570  73.48694  1.000 167.93673 ?  93  GLN   K CD  1 
ATOM   15339 O OE1 . GLN   K  1 93  ? 57.30547  27.48912  72.33338  1.000 46.20951  ?  93  GLN   K OE1 1 
ATOM   15340 N NE2 . GLN   K  1 93  ? 57.95992  26.91218  74.42142  1.000 48.42879  ?  93  GLN   K NE2 1 
ATOM   15341 N N   . GLU   K  1 94  ? 52.63637  28.08274  70.54890  1.000 47.40770  ?  94  GLU   K N   1 
ATOM   15342 C CA  . GLU   K  1 94  ? 51.35792  28.55070  70.01821  1.000 19.75050  ?  94  GLU   K CA  1 
ATOM   15343 C C   . GLU   K  1 94  ? 50.70261  27.47057  69.17943  1.000 54.25584  ?  94  GLU   K C   1 
ATOM   15344 O O   . GLU   K  1 94  ? 49.47534  27.32051  69.18649  1.000 51.31442  ?  94  GLU   K O   1 
ATOM   15345 C CB  . GLU   K  1 94  ? 51.54794  29.79432  69.16371  1.000 51.19164  ?  94  GLU   K CB  1 
ATOM   15346 C CG  . GLU   K  1 94  ? 51.71763  31.05429  69.95669  1.000 72.73448  ?  94  GLU   K CG  1 
ATOM   15347 C CD  . GLU   K  1 94  ? 51.77752  32.25622  69.04131  1.000 135.43327 ?  94  GLU   K CD  1 
ATOM   15348 O OE1 . GLU   K  1 94  ? 51.10651  32.19762  67.97194  1.000 43.89875  ?  94  GLU   K OE1 1 
ATOM   15349 O OE2 . GLU   K  1 94  ? 52.49602  33.22769  69.38482  1.000 97.60590  -1 94  GLU   K OE2 1 
ATOM   15350 N N   . LEU   K  1 95  ? 51.50990  26.71873  68.42168  1.000 49.75716  ?  95  LEU   K N   1 
ATOM   15351 C CA  . LEU   K  1 95  ? 50.97518  25.58684  67.67383  1.000 30.79996  ?  95  LEU   K CA  1 
ATOM   15352 C C   . LEU   K  1 95  ? 50.20652  24.65585  68.59803  1.000 34.92841  ?  95  LEU   K C   1 
ATOM   15353 O O   . LEU   K  1 95  ? 49.04342  24.32128  68.33411  1.000 30.93799  ?  95  LEU   K O   1 
ATOM   15354 C CB  . LEU   K  1 95  ? 52.10108  24.83332  66.96910  1.000 37.90907  ?  95  LEU   K CB  1 
ATOM   15355 C CG  . LEU   K  1 95  ? 51.60322  23.73778  66.01494  1.000 37.97637  ?  95  LEU   K CG  1 
ATOM   15356 C CD1 . LEU   K  1 95  ? 50.76735  24.32833  64.87218  1.000 32.26484  ?  95  LEU   K CD1 1 
ATOM   15357 C CD2 . LEU   K  1 95  ? 52.80073  22.98838  65.47800  1.000 23.46343  ?  95  LEU   K CD2 1 
ATOM   15358 N N   . CYS   K  1 96  ? 50.82742  24.27593  69.72643  1.000 25.97233  ?  96  CYS   K N   1 
ATOM   15359 C CA  . CYS   K  1 96  ? 50.15906  23.39099  70.67422  1.000 36.76134  ?  96  CYS   K CA  1 
ATOM   15360 C C   . CYS   K  1 96  ? 48.87929  24.01108  71.22208  1.000 36.96046  ?  96  CYS   K C   1 
ATOM   15361 O O   . CYS   K  1 96  ? 47.88442  23.30452  71.43444  1.000 56.29968  ?  96  CYS   K O   1 
ATOM   15362 C CB  . CYS   K  1 96  ? 51.09983  23.03608  71.81600  1.000 30.29477  ?  96  CYS   K CB  1 
ATOM   15363 S SG  . CYS   K  1 96  ? 52.50077  21.97844  71.38247  1.000 45.99916  ?  96  CYS   K SG  1 
ATOM   15364 N N   . ASN   K  1 97  ? 48.88842  25.32615  71.48145  1.000 48.27557  ?  97  ASN   K N   1 
ATOM   15365 C CA  . ASN   K  1 97  ? 47.68774  25.96539  72.01829  1.000 38.54569  ?  97  ASN   K CA  1 
ATOM   15366 C C   . ASN   K  1 97  ? 46.56545  25.98277  70.98890  1.000 63.37522  ?  97  ASN   K C   1 
ATOM   15367 O O   . ASN   K  1 97  ? 45.39928  25.75124  71.33482  1.000 44.78755  ?  97  ASN   K O   1 
ATOM   15368 C CB  . ASN   K  1 97  ? 47.99100  27.38620  72.48427  1.000 50.07226  ?  97  ASN   K CB  1 
ATOM   15369 C CG  . ASN   K  1 97  ? 48.81326  27.41813  73.74402  1.000 89.54692  ?  97  ASN   K CG  1 
ATOM   15370 O OD1 . ASN   K  1 97  ? 48.68069  26.54596  74.60766  1.000 62.11282  ?  97  ASN   K OD1 1 
ATOM   15371 N ND2 . ASN   K  1 97  ? 49.67489  28.42556  73.86236  1.000 47.11818  ?  97  ASN   K ND2 1 
ATOM   15372 N N   . MET   K  1 98  ? 46.89737  26.25621  69.71901  1.000 28.82952  ?  98  MET   K N   1 
ATOM   15373 C CA  . MET   K  1 98  ? 45.87644  26.24411  68.67712  1.000 25.15908  ?  98  MET   K CA  1 
ATOM   15374 C C   . MET   K  1 98  ? 45.33665  24.83322  68.44419  1.000 63.20474  ?  98  MET   K C   1 
ATOM   15375 O O   . MET   K  1 98  ? 44.13663  24.66434  68.19044  1.000 43.06366  ?  98  MET   K O   1 
ATOM   15376 C CB  . MET   K  1 98  ? 46.44156  26.85553  67.38913  1.000 32.01609  ?  98  MET   K CB  1 
ATOM   15377 C CG  . MET   K  1 98  ? 46.77159  28.34797  67.53635  1.000 21.00990  ?  98  MET   K CG  1 
ATOM   15378 S SD  . MET   K  1 98  ? 47.64125  29.14622  66.18274  1.000 52.11486  ?  98  MET   K SD  1 
ATOM   15379 C CE  . MET   K  1 98  ? 46.32653  29.33844  64.98756  1.000 38.81253  ?  98  MET   K CE  1 
ATOM   15380 N N   . PHE   K  1 99  ? 46.19856  23.80663  68.54040  1.000 39.04966  ?  99  PHE   K N   1 
ATOM   15381 C CA  . PHE   K  1 99  ? 45.71739  22.42342  68.48398  1.000 35.07816  ?  99  PHE   K CA  1 
ATOM   15382 C C   . PHE   K  1 99  ? 44.66826  22.18151  69.56249  1.000 44.42578  ?  99  PHE   K C   1 
ATOM   15383 O O   . PHE   K  1 99  ? 43.64320  21.52566  69.32712  1.000 43.29079  ?  99  PHE   K O   1 
ATOM   15384 C CB  . PHE   K  1 99  ? 46.86972  21.41659  68.66850  1.000 33.55407  ?  99  PHE   K CB  1 
ATOM   15385 C CG  . PHE   K  1 99  ? 47.73526  21.20663  67.45093  1.000 41.76646  ?  99  PHE   K CG  1 
ATOM   15386 C CD1 . PHE   K  1 99  ? 47.45358  21.82842  66.22996  1.000 31.59210  ?  99  PHE   K CD1 1 
ATOM   15387 C CD2 . PHE   K  1 99  ? 48.84564  20.36974  67.53563  1.000 40.41717  ?  99  PHE   K CD2 1 
ATOM   15388 C CE1 . PHE   K  1 99  ? 48.26345  21.62943  65.11994  1.000 47.13765  ?  99  PHE   K CE1 1 
ATOM   15389 C CE2 . PHE   K  1 99  ? 49.66267  20.15887  66.42949  1.000 30.73137  ?  99  PHE   K CE2 1 
ATOM   15390 C CZ  . PHE   K  1 99  ? 49.37444  20.80115  65.21646  1.000 34.83510  ?  99  PHE   K CZ  1 
ATOM   15391 N N   . ASN   K  1 100 ? 44.92834  22.70568  70.76565  1.000 38.30522  ?  100 ASN   K N   1 
ATOM   15392 C CA  . ASN   K  1 100 ? 44.03026  22.50569  71.89532  1.000 42.55799  ?  100 ASN   K CA  1 
ATOM   15393 C C   . ASN   K  1 100 ? 42.65340  23.12003  71.63778  1.000 46.34261  ?  100 ASN   K C   1 
ATOM   15394 O O   . ASN   K  1 100 ? 41.63673  22.55561  72.06697  1.000 53.59842  ?  100 ASN   K O   1 
ATOM   15395 C CB  . ASN   K  1 100 ? 44.68101  23.06735  73.16270  1.000 42.04584  ?  100 ASN   K CB  1 
ATOM   15396 C CG  . ASN   K  1 100 ? 44.06824  22.50737  74.42555  1.000 53.49774  ?  100 ASN   K CG  1 
ATOM   15397 O OD1 . ASN   K  1 100 ? 44.15376  21.30699  74.70660  1.000 66.14436  ?  100 ASN   K OD1 1 
ATOM   15398 N ND2 . ASN   K  1 100 ? 43.45384  23.37915  75.20596  1.000 53.17774  ?  100 ASN   K ND2 1 
ATOM   15399 N N   . ASP   K  1 101 ? 42.59344  24.24636  70.91173  1.000 44.04064  ?  101 ASP   K N   1 
ATOM   15400 C CA  . ASP   K  1 101 ? 41.29954  24.77585  70.47965  1.000 37.76657  ?  101 ASP   K CA  1 
ATOM   15401 C C   . ASP   K  1 101 ? 40.68576  23.90671  69.38889  1.000 60.42746  ?  101 ASP   K C   1 
ATOM   15402 O O   . ASP   K  1 101 ? 39.51226  23.51870  69.48224  1.000 52.10172  ?  101 ASP   K O   1 
ATOM   15403 C CB  . ASP   K  1 101 ? 41.43234  26.21876  69.97954  1.000 37.84184  ?  101 ASP   K CB  1 
ATOM   15404 C CG  . ASP   K  1 101 ? 41.88584  27.19022  71.06171  1.000 120.60198 ?  101 ASP   K CG  1 
ATOM   15405 O OD1 . ASP   K  1 101 ? 41.54738  26.98174  72.24777  1.000 55.89166  ?  101 ASP   K OD1 1 
ATOM   15406 O OD2 . ASP   K  1 101 ? 42.57754  28.17841  70.71268  1.000 65.54843  -1 101 ASP   K OD2 1 
ATOM   15407 N N   . ILE   K  1 102 ? 41.46707  23.60030  68.33990  1.000 50.26709  ?  102 ILE   K N   1 
ATOM   15408 C CA  . ILE   K  1 102 ? 40.91912  22.92812  67.16063  1.000 34.72325  ?  102 ILE   K CA  1 
ATOM   15409 C C   . ILE   K  1 102 ? 40.30976  21.58662  67.53213  1.000 60.28496  ?  102 ILE   K C   1 
ATOM   15410 O O   . ILE   K  1 102 ? 39.20674  21.25339  67.08209  1.000 43.82298  ?  102 ILE   K O   1 
ATOM   15411 C CB  . ILE   K  1 102 ? 41.99301  22.75504  66.07694  1.000 37.55218  ?  102 ILE   K CB  1 
ATOM   15412 C CG1 . ILE   K  1 102 ? 42.46461  24.10212  65.54280  1.000 22.36959  ?  102 ILE   K CG1 1 
ATOM   15413 C CG2 . ILE   K  1 102 ? 41.44277  21.92925  64.93832  1.000 26.78376  ?  102 ILE   K CG2 1 
ATOM   15414 C CD1 . ILE   K  1 102 ? 43.41475  23.96612  64.34973  1.000 43.45486  ?  102 ILE   K CD1 1 
ATOM   15415 N N   . PHE   K  1 103 ? 41.00799  20.80257  68.37085  1.000 35.02016  ?  103 PHE   K N   1 
ATOM   15416 C CA  . PHE   K  1 103 ? 40.58671  19.44344  68.70280  1.000 59.53344  ?  103 PHE   K CA  1 
ATOM   15417 C C   . PHE   K  1 103 ? 39.37301  19.40002  69.62650  1.000 37.41780  ?  103 PHE   K C   1 
ATOM   15418 O O   . PHE   K  1 103 ? 38.90112  18.30667  69.95557  1.000 45.77826  ?  103 PHE   K O   1 
ATOM   15419 C CB  . PHE   K  1 103 ? 41.74149  18.66934  69.34577  1.000 26.94120  ?  103 PHE   K CB  1 
ATOM   15420 C CG  . PHE   K  1 103 ? 42.95186  18.50497  68.44907  1.000 44.19929  ?  103 PHE   K CG  1 
ATOM   15421 C CD1 . PHE   K  1 103 ? 42.83986  18.59165  67.06278  1.000 40.17480  ?  103 PHE   K CD1 1 
ATOM   15422 C CD2 . PHE   K  1 103 ? 44.20614  18.26774  69.00050  1.000 32.22988  ?  103 PHE   K CD2 1 
ATOM   15423 C CE1 . PHE   K  1 103 ? 43.96412  18.44970  66.25064  1.000 52.42250  ?  103 PHE   K CE1 1 
ATOM   15424 C CE2 . PHE   K  1 103 ? 45.33316  18.12461  68.19844  1.000 44.36215  ?  103 PHE   K CE2 1 
ATOM   15425 C CZ  . PHE   K  1 103 ? 45.21154  18.21509  66.82425  1.000 43.64513  ?  103 PHE   K CZ  1 
ATOM   15426 N N   . ARG   K  1 104 ? 38.86577  20.53763  70.08713  1.000 122.33040 ?  104 ARG   K N   1 
ATOM   15427 C CA  . ARG   K  1 104 ? 37.68370  20.56575  70.93085  1.000 13.66539  ?  104 ARG   K CA  1 
ATOM   15428 C C   . ARG   K  1 104 ? 36.42895  20.98845  70.17822  1.000 100.35709 ?  104 ARG   K C   1 
ATOM   15429 O O   . ARG   K  1 104 ? 35.35426  21.07044  70.77270  1.000 42.10082  ?  104 ARG   K O   1 
ATOM   15430 C CB  . ARG   K  1 104 ? 37.90568  21.50170  72.11582  1.000 104.62625 ?  104 ARG   K CB  1 
ATOM   15431 C CG  . ARG   K  1 104 ? 39.02525  21.10403  73.03061  1.000 42.78813  ?  104 ARG   K CG  1 
ATOM   15432 C CD  . ARG   K  1 104 ? 39.14354  22.09815  74.18443  1.000 24.11854  ?  104 ARG   K CD  1 
ATOM   15433 N NE  . ARG   K  1 104 ? 40.31678  21.90755  75.05667  1.000 92.11698  ?  104 ARG   K NE  1 
ATOM   15434 C CZ  . ARG   K  1 104 ? 40.38145  21.11541  76.12597  1.000 68.73933  ?  104 ARG   K CZ  1 
ATOM   15435 N NH1 . ARG   K  1 104 ? 39.33148  20.39816  76.53031  1.000 110.83996 ?  104 ARG   K NH1 1 
ATOM   15436 N NH2 . ARG   K  1 104 ? 41.53650  21.03376  76.80236  1.000 62.75446  ?  104 ARG   K NH2 1 
ATOM   15437 N N   . LYS   K  1 105 ? 36.52791  21.26086  68.88791  1.000 48.01565  ?  105 LYS   K N   1 
ATOM   15438 C CA  . LYS   K  1 105 ? 35.36534  21.67930  68.12626  1.000 68.75299  ?  105 LYS   K CA  1 
ATOM   15439 C C   . LYS   K  1 105 ? 35.43353  21.08105  66.72989  1.000 51.28376  ?  105 LYS   K C   1 
ATOM   15440 O O   . LYS   K  1 105 ? 36.49053  20.65188  66.26958  1.000 55.91104  ?  105 LYS   K O   1 
ATOM   15441 C CB  . LYS   K  1 105 ? 35.24666  23.20997  68.10451  1.000 58.97023  ?  105 LYS   K CB  1 
ATOM   15442 C CG  . LYS   K  1 105 ? 36.44625  23.90796  67.54920  1.000 48.91505  ?  105 LYS   K CG  1 
ATOM   15443 C CD  . LYS   K  1 105 ? 36.34352  25.42465  67.70959  1.000 49.38001  ?  105 LYS   K CD  1 
ATOM   15444 C CE  . LYS   K  1 105 ? 36.47404  25.83692  69.15576  1.000 79.58718  ?  105 LYS   K CE  1 
ATOM   15445 N NZ  . LYS   K  1 105 ? 36.99343  27.22631  69.26426  1.000 92.44009  ?  105 LYS   K NZ  1 
ATOM   15446 N N   . ALA   K  1 106 ? 34.28144  21.03083  66.08320  1.000 64.54845  ?  106 ALA   K N   1 
ATOM   15447 C CA  . ALA   K  1 106 ? 34.15762  20.46064  64.75498  1.000 57.81007  ?  106 ALA   K CA  1 
ATOM   15448 C C   . ALA   K  1 106 ? 34.52719  21.48862  63.69068  1.000 41.20071  ?  106 ALA   K C   1 
ATOM   15449 O O   . ALA   K  1 106 ? 34.42386  22.69447  63.92409  1.000 60.55029  ?  106 ALA   K O   1 
ATOM   15450 C CB  . ALA   K  1 106 ? 32.73372  19.95591  64.52147  1.000 44.11723  ?  106 ALA   K CB  1 
ATOM   15451 N N   . PRO   K  1 107 ? 34.97814  21.04090  62.51725  1.000 70.97399  ?  107 PRO   K N   1 
ATOM   15452 C CA  . PRO   K  1 107 ? 35.31387  21.99114  61.45278  1.000 53.30634  ?  107 PRO   K CA  1 
ATOM   15453 C C   . PRO   K  1 107 ? 34.06385  22.68146  60.92206  1.000 63.18917  ?  107 PRO   K C   1 
ATOM   15454 O O   . PRO   K  1 107 ? 32.93547  22.20993  61.08819  1.000 58.45257  ?  107 PRO   K O   1 
ATOM   15455 C CB  . PRO   K  1 107 ? 35.95734  21.11521  60.36881  1.000 51.36214  ?  107 PRO   K CB  1 
ATOM   15456 C CG  . PRO   K  1 107 ? 36.06625  19.76741  60.92714  1.000 47.97328  ?  107 PRO   K CG  1 
ATOM   15457 C CD  . PRO   K  1 107 ? 35.13341  19.64454  62.07580  1.000 41.80198  ?  107 PRO   K CD  1 
ATOM   15458 N N   . VAL   K  1 108 ? 34.28115  23.80952  60.25248  1.000 55.18151  ?  108 VAL   K N   1 
ATOM   15459 C CA  . VAL   K  1 108 ? 33.20042  24.55520  59.63134  1.000 51.04739  ?  108 VAL   K CA  1 
ATOM   15460 C C   . VAL   K  1 108 ? 33.50674  24.73155  58.14256  1.000 62.27918  ?  108 VAL   K C   1 
ATOM   15461 O O   . VAL   K  1 108 ? 34.61594  24.47340  57.66963  1.000 62.89456  ?  108 VAL   K O   1 
ATOM   15462 C CB  . VAL   K  1 108 ? 32.95883  25.91194  60.32534  1.000 61.28304  ?  108 VAL   K CB  1 
ATOM   15463 C CG1 . VAL   K  1 108 ? 32.65891  25.69964  61.82219  1.000 42.30550  ?  108 VAL   K CG1 1 
ATOM   15464 C CG2 . VAL   K  1 108 ? 34.14752  26.81237  60.15516  1.000 42.05170  ?  108 VAL   K CG2 1 
ATOM   15465 N N   . TYR   K  1 109 ? 32.48806  25.15247  57.40020  1.000 46.38469  ?  109 TYR   K N   1 
ATOM   15466 C CA  . TYR   K  1 109 ? 32.62874  25.34727  55.96213  1.000 75.83800  ?  109 TYR   K CA  1 
ATOM   15467 C C   . TYR   K  1 109 ? 33.25636  26.70467  55.66691  1.000 46.10128  ?  109 TYR   K C   1 
ATOM   15468 O O   . TYR   K  1 109 ? 32.96560  27.69954  56.33678  1.000 60.02595  ?  109 TYR   K O   1 
ATOM   15469 C CB  . TYR   K  1 109 ? 31.26826  25.23575  55.26512  1.000 40.25553  ?  109 TYR   K CB  1 
ATOM   15470 C CG  . TYR   K  1 109 ? 31.35703  25.46034  53.77358  1.000 73.06049  ?  109 TYR   K CG  1 
ATOM   15471 C CD1 . TYR   K  1 109 ? 31.63125  24.41579  52.91192  1.000 41.55157  ?  109 TYR   K CD1 1 
ATOM   15472 C CD2 . TYR   K  1 109 ? 31.19176  26.72688  53.22993  1.000 45.53047  ?  109 TYR   K CD2 1 
ATOM   15473 C CE1 . TYR   K  1 109 ? 31.72882  24.63076  51.54845  1.000 83.22349  ?  109 TYR   K CE1 1 
ATOM   15474 C CE2 . TYR   K  1 109 ? 31.28892  26.95047  51.87328  1.000 66.67187  ?  109 TYR   K CE2 1 
ATOM   15475 C CZ  . TYR   K  1 109 ? 31.55700  25.90328  51.03446  1.000 42.88860  ?  109 TYR   K CZ  1 
ATOM   15476 O OH  . TYR   K  1 109 ? 31.65969  26.10923  49.67703  1.000 69.15869  ?  109 TYR   K OH  1 
ATOM   15477 N N   . GLY   K  1 110 ? 34.13185  26.74360  54.66964  1.000 67.83420  ?  110 GLY   K N   1 
ATOM   15478 C CA  . GLY   K  1 110 ? 34.71721  28.01749  54.31475  1.000 32.83346  ?  110 GLY   K CA  1 
ATOM   15479 C C   . GLY   K  1 110 ? 36.16773  28.01724  53.87952  1.000 66.53029  ?  110 GLY   K C   1 
ATOM   15480 O O   . GLY   K  1 110 ? 36.51207  28.73409  52.93767  1.000 60.53234  ?  110 GLY   K O   1 
ATOM   15481 N N   . ASP   K  1 111 ? 37.03308  27.24897  54.54272  1.000 55.64660  ?  111 ASP   K N   1 
ATOM   15482 C CA  . ASP   K  1 111 ? 38.45153  27.32128  54.22461  1.000 46.22532  ?  111 ASP   K CA  1 
ATOM   15483 C C   . ASP   K  1 111 ? 38.80186  26.38297  53.07493  1.000 30.27189  ?  111 ASP   K C   1 
ATOM   15484 O O   . ASP   K  1 111 ? 38.03897  25.47802  52.72525  1.000 43.60406  ?  111 ASP   K O   1 
ATOM   15485 C CB  . ASP   K  1 111 ? 39.29329  27.00603  55.45684  1.000 58.95705  ?  111 ASP   K CB  1 
ATOM   15486 C CG  . ASP   K  1 111 ? 39.34778  28.16213  56.42312  1.000 57.66804  ?  111 ASP   K CG  1 
ATOM   15487 O OD1 . ASP   K  1 111 ? 39.94051  29.20214  56.06531  1.000 73.48547  ?  111 ASP   K OD1 1 
ATOM   15488 O OD2 . ASP   K  1 111 ? 38.77611  28.03667  57.52845  1.000 92.35373  -1 111 ASP   K OD2 1 
ATOM   15489 N N   . LEU   K  1 112 ? 39.99600  26.58887  52.44537  1.000 47.90297  ?  112 LEU   K N   1 
ATOM   15490 C CA  . LEU   K  1 112 ? 40.40932  25.69733  51.33149  1.000 77.62468  ?  112 LEU   K CA  1 
ATOM   15491 C C   . LEU   K  1 112 ? 40.70258  24.29387  51.80817  1.000 27.20475  ?  112 LEU   K C   1 
ATOM   15492 O O   . LEU   K  1 112 ? 40.59054  23.33963  51.03560  1.000 32.66848  ?  112 LEU   K O   1 
ATOM   15493 C CB  . LEU   K  1 112 ? 41.66652  26.17274  50.60796  1.000 39.06518  ?  112 LEU   K CB  1 
ATOM   15494 C CG  . LEU   K  1 112 ? 41.57529  27.62784  50.25606  1.000 83.68849  ?  112 LEU   K CG  1 
ATOM   15495 C CD1 . LEU   K  1 112 ? 42.53345  28.41175  51.15986  1.000 63.52407  ?  112 LEU   K CD1 1 
ATOM   15496 C CD2 . LEU   K  1 112 ? 41.88174  27.70414  48.80806  1.000 86.20120  ?  112 LEU   K CD2 1 
ATOM   15497 N N   . GLY   K  1 113 ? 41.12593  24.15079  53.04797  1.000 41.67673  ?  113 GLY   K N   1 
ATOM   15498 C CA  . GLY   K  1 113 ? 41.31604  22.82318  53.57481  1.000 40.15554  ?  113 GLY   K CA  1 
ATOM   15499 C C   . GLY   K  1 113 ? 40.89587  22.73740  55.02872  1.000 43.74536  ?  113 GLY   K C   1 
ATOM   15500 O O   . GLY   K  1 113 ? 40.44166  23.71946  55.63397  1.000 42.18408  ?  113 GLY   K O   1 
ATOM   15501 N N   . PRO   K  1 114 ? 41.05161  21.55672  55.62279  1.000 41.83233  ?  114 PRO   K N   1 
ATOM   15502 C CA  . PRO   K  1 114 ? 40.64699  21.36255  57.03345  1.000 35.15048  ?  114 PRO   K CA  1 
ATOM   15503 C C   . PRO   K  1 114 ? 41.53778  22.15909  57.97553  1.000 38.11065  ?  114 PRO   K C   1 
ATOM   15504 O O   . PRO   K  1 114 ? 42.59377  22.68301  57.57039  1.000 42.57924  ?  114 PRO   K O   1 
ATOM   15505 C CB  . PRO   K  1 114 ? 40.78854  19.84390  57.23572  1.000 40.16162  ?  114 PRO   K CB  1 
ATOM   15506 C CG  . PRO   K  1 114 ? 41.79627  19.41357  56.18214  1.000 37.11720  ?  114 PRO   K CG  1 
ATOM   15507 C CD  . PRO   K  1 114 ? 41.64709  20.35170  55.02056  1.000 38.20258  ?  114 PRO   K CD  1 
ATOM   15508 N N   . PRO   K  1 115 ? 41.12442  22.31926  59.23851  1.000 30.89243  ?  115 PRO   K N   1 
ATOM   15509 C CA  . PRO   K  1 115 ? 41.75079  23.36519  60.07983  1.000 41.87748  ?  115 PRO   K CA  1 
ATOM   15510 C C   . PRO   K  1 115 ? 43.18890  23.09454  60.48138  1.000 33.97628  ?  115 PRO   K C   1 
ATOM   15511 O O   . PRO   K  1 115 ? 43.96676  24.05377  60.58596  1.000 39.06933  ?  115 PRO   K O   1 
ATOM   15512 C CB  . PRO   K  1 115 ? 40.83337  23.43786  61.31108  1.000 23.65016  ?  115 PRO   K CB  1 
ATOM   15513 C CG  . PRO   K  1 115 ? 39.88715  22.27230  61.21122  1.000 26.20826  ?  115 PRO   K CG  1 
ATOM   15514 C CD  . PRO   K  1 115 ? 39.82317  21.87373  59.77292  1.000 36.17611  ?  115 PRO   K CD  1 
ATOM   15515 N N   . VAL   K  1 116 ? 43.56754  21.83401  60.73636  1.000 40.42450  ?  116 VAL   K N   1 
ATOM   15516 C CA  . VAL   K  1 116 ? 44.96967  21.55161  61.04897  1.000 30.68555  ?  116 VAL   K CA  1 
ATOM   15517 C C   . VAL   K  1 116 ? 45.85458  21.82407  59.83727  1.000 33.16656  ?  116 VAL   K C   1 
ATOM   15518 O O   . VAL   K  1 116 ? 46.92644  22.43468  59.95834  1.000 36.74043  ?  116 VAL   K O   1 
ATOM   15519 C CB  . VAL   K  1 116 ? 45.16513  20.11563  61.56427  1.000 37.85586  ?  116 VAL   K CB  1 
ATOM   15520 C CG1 . VAL   K  1 116 ? 46.64945  19.88851  61.84184  1.000 29.93021  ?  116 VAL   K CG1 1 
ATOM   15521 C CG2 . VAL   K  1 116 ? 44.34778  19.87545  62.82570  1.000 21.88975  ?  116 VAL   K CG2 1 
ATOM   15522 N N   . TYR   K  1 117 ? 45.42801  21.38691  58.65116  1.000 28.57822  ?  117 TYR   K N   1 
ATOM   15523 C CA  . TYR   K  1 117 ? 46.18292  21.72873  57.45061  1.000 42.11095  ?  117 TYR   K CA  1 
ATOM   15524 C C   . TYR   K  1 117 ? 46.39626  23.24198  57.34149  1.000 36.13166  ?  117 TYR   K C   1 
ATOM   15525 O O   . TYR   K  1 117 ? 47.51250  23.70206  57.07365  1.000 41.14328  ?  117 TYR   K O   1 
ATOM   15526 C CB  . TYR   K  1 117 ? 45.49233  21.19995  56.18346  1.000 27.69609  ?  117 TYR   K CB  1 
ATOM   15527 C CG  . TYR   K  1 117 ? 46.08487  21.89351  54.97900  1.000 34.96639  ?  117 TYR   K CG  1 
ATOM   15528 C CD1 . TYR   K  1 117 ? 47.32122  21.49332  54.46977  1.000 31.19519  ?  117 TYR   K CD1 1 
ATOM   15529 C CD2 . TYR   K  1 117 ? 45.46377  23.00111  54.40490  1.000 47.90510  ?  117 TYR   K CD2 1 
ATOM   15530 C CE1 . TYR   K  1 117 ? 47.90724  22.14836  53.39417  1.000 31.62705  ?  117 TYR   K CE1 1 
ATOM   15531 C CE2 . TYR   K  1 117 ? 46.04269  23.65959  53.34109  1.000 25.32003  ?  117 TYR   K CE2 1 
ATOM   15532 C CZ  . TYR   K  1 117 ? 47.26537  23.22823  52.84018  1.000 41.74783  ?  117 TYR   K CZ  1 
ATOM   15533 O OH  . TYR   K  1 117 ? 47.84469  23.87166  51.77712  1.000 31.49137  ?  117 TYR   K OH  1 
ATOM   15534 N N   . MET   K  1 118 ? 45.33093  24.03084  57.54598  1.000 42.63899  ?  118 MET   K N   1 
ATOM   15535 C CA  . MET   K  1 118 ? 45.42244  25.48007  57.35635  1.000 32.47118  ?  118 MET   K CA  1 
ATOM   15536 C C   . MET   K  1 118 ? 46.53279  26.09335  58.21614  1.000 48.09160  ?  118 MET   K C   1 
ATOM   15537 O O   . MET   K  1 118 ? 47.36267  26.86118  57.71471  1.000 40.25913  ?  118 MET   K O   1 
ATOM   15538 C CB  . MET   K  1 118 ? 44.07735  26.15408  57.65825  1.000 35.54001  ?  118 MET   K CB  1 
ATOM   15539 C CG  . MET   K  1 118 ? 42.92988  25.92178  56.66377  1.000 25.21086  ?  118 MET   K CG  1 
ATOM   15540 S SD  . MET   K  1 118 ? 43.22575  26.41016  54.94955  1.000 43.42646  ?  118 MET   K SD  1 
ATOM   15541 C CE  . MET   K  1 118 ? 43.56422  28.15673  55.16390  1.000 47.99838  ?  118 MET   K CE  1 
ATOM   15542 N N   . ILE   K  1 119 ? 46.59151  25.75176  59.51126  1.000 30.97738  ?  119 ILE   K N   1 
ATOM   15543 C CA  . ILE   K  1 119 ? 47.67326  26.30761  60.33017  1.000 42.45663  ?  119 ILE   K CA  1 
ATOM   15544 C C   . ILE   K  1 119 ? 49.01166  25.59890  60.14840  1.000 42.89174  ?  119 ILE   K C   1 
ATOM   15545 O O   . ILE   K  1 119 ? 50.03373  26.12255  60.61791  1.000 47.55378  ?  119 ILE   K O   1 
ATOM   15546 C CB  . ILE   K  1 119 ? 47.32283  26.32764  61.83189  1.000 34.42885  ?  119 ILE   K CB  1 
ATOM   15547 C CG1 . ILE   K  1 119 ? 47.39942  24.93766  62.44848  1.000 36.71828  ?  119 ILE   K CG1 1 
ATOM   15548 C CG2 . ILE   K  1 119 ? 45.93537  26.88892  62.04003  1.000 41.93810  ?  119 ILE   K CG2 1 
ATOM   15549 C CD1 . ILE   K  1 119 ? 47.09566  24.96280  63.92904  1.000 41.59652  ?  119 ILE   K CD1 1 
ATOM   15550 N N   . MET   K  1 120 ? 49.05480  24.44594  59.45955  1.000 32.49444  ?  120 MET   K N   1 
ATOM   15551 C CA  . MET   K  1 120 ? 50.31127  23.71774  59.25387  1.000 30.49311  ?  120 MET   K CA  1 
ATOM   15552 C C   . MET   K  1 120 ? 50.98767  24.01777  57.92156  1.000 36.32404  ?  120 MET   K C   1 
ATOM   15553 O O   . MET   K  1 120 ? 52.17943  23.72724  57.77339  1.000 35.92898  ?  120 MET   K O   1 
ATOM   15554 C CB  . MET   K  1 120 ? 50.08431  22.19657  59.32570  1.000 18.11818  ?  120 MET   K CB  1 
ATOM   15555 C CG  . MET   K  1 120 ? 49.76678  21.67207  60.70815  1.000 26.00929  ?  120 MET   K CG  1 
ATOM   15556 S SD  . MET   K  1 120 ? 51.11967  21.78934  61.86892  1.000 42.12827  ?  120 MET   K SD  1 
ATOM   15557 C CE  . MET   K  1 120 ? 52.09419  20.36266  61.38388  1.000 26.76850  ?  120 MET   K CE  1 
ATOM   15558 N N   . ALA   K  1 121 ? 50.25618  24.57679  56.95296  1.000 27.32625  ?  121 ALA   K N   1 
ATOM   15559 C CA  . ALA   K  1 121 ? 50.74636  24.61387  55.57567  1.000 33.11112  ?  121 ALA   K CA  1 
ATOM   15560 C C   . ALA   K  1 121 ? 52.06175  25.37333  55.46454  1.000 33.48673  ?  121 ALA   K C   1 
ATOM   15561 O O   . ALA   K  1 121 ? 52.95735  24.96934  54.70908  1.000 40.46025  ?  121 ALA   K O   1 
ATOM   15562 C CB  . ALA   K  1 121 ? 49.68752  25.23246  54.65432  1.000 25.02700  ?  121 ALA   K CB  1 
ATOM   15563 N N   . LYS   K  1 122 ? 52.19751  26.48437  56.20202  1.000 39.75723  ?  122 LYS   K N   1 
ATOM   15564 C CA  . LYS   K  1 122 ? 53.43991  27.25117  56.13682  1.000 32.29394  ?  122 LYS   K CA  1 
ATOM   15565 C C   . LYS   K  1 122 ? 54.61138  26.43036  56.69045  1.000 46.51919  ?  122 LYS   K C   1 
ATOM   15566 O O   . LYS   K  1 122 ? 55.70215  26.42975  56.11599  1.000 40.35131  ?  122 LYS   K O   1 
ATOM   15567 C CB  . LYS   K  1 122 ? 53.28397  28.59168  56.88342  1.000 31.70864  ?  122 LYS   K CB  1 
ATOM   15568 C CG  . LYS   K  1 122 ? 52.50022  29.54689  56.05970  1.000 20.20572  ?  122 LYS   K CG  1 
ATOM   15569 C CD  . LYS   K  1 122 ? 52.36183  30.88866  56.65088  1.000 20.89226  ?  122 LYS   K CD  1 
ATOM   15570 C CE  . LYS   K  1 122 ? 51.89771  31.86120  55.56001  1.000 125.13464 ?  122 LYS   K CE  1 
ATOM   15571 N NZ  . LYS   K  1 122 ? 50.99272  31.35606  54.48830  1.000 84.22373  ?  122 LYS   K NZ  1 
ATOM   15572 N N   . LEU   K  1 123 ? 54.38657  25.67612  57.77369  1.000 40.86236  ?  123 LEU   K N   1 
ATOM   15573 C CA  . LEU   K  1 123 ? 55.42628  24.80929  58.34202  1.000 40.36305  ?  123 LEU   K CA  1 
ATOM   15574 C C   . LEU   K  1 123 ? 55.80774  23.67964  57.38954  1.000 65.35262  ?  123 LEU   K C   1 
ATOM   15575 O O   . LEU   K  1 123 ? 57.00148  23.39594  57.18479  1.000 32.43192  ?  123 LEU   K O   1 
ATOM   15576 C CB  . LEU   K  1 123 ? 54.95474  24.23381  59.67989  1.000 31.44998  ?  123 LEU   K CB  1 
ATOM   15577 C CG  . LEU   K  1 123 ? 54.34888  25.29013  60.59535  1.000 40.39241  ?  123 LEU   K CG  1 
ATOM   15578 C CD1 . LEU   K  1 123 ? 53.90974  24.69897  61.92739  1.000 34.54697  ?  123 LEU   K CD1 1 
ATOM   15579 C CD2 . LEU   K  1 123 ? 55.36250  26.38759  60.80399  1.000 34.37643  ?  123 LEU   K CD2 1 
ATOM   15580 N N   . MET   K  1 124 ? 54.80188  22.99242  56.83004  1.000 31.85362  ?  124 MET   K N   1 
ATOM   15581 C CA  . MET   K  1 124 ? 55.07871  21.91479  55.88561  1.000 43.24492  ?  124 MET   K CA  1 
ATOM   15582 C C   . MET   K  1 124 ? 55.94195  22.37984  54.72674  1.000 35.81141  ?  124 MET   K C   1 
ATOM   15583 O O   . MET   K  1 124 ? 56.64147  21.56830  54.11048  1.000 34.96107  ?  124 MET   K O   1 
ATOM   15584 C CB  . MET   K  1 124 ? 53.78147  21.34332  55.32915  1.000 20.82768  ?  124 MET   K CB  1 
ATOM   15585 C CG  . MET   K  1 124 ? 52.86404  20.77444  56.36504  1.000 41.07291  ?  124 MET   K CG  1 
ATOM   15586 S SD  . MET   K  1 124 ? 51.16557  20.78131  55.75234  1.000 42.95856  ?  124 MET   K SD  1 
ATOM   15587 C CE  . MET   K  1 124 ? 51.26461  19.75698  54.29930  1.000 18.63093  ?  124 MET   K CE  1 
ATOM   15588 N N   . ASN   K  1 125 ? 55.89723  23.67244  54.40766  1.000 38.35182  ?  125 ASN   K N   1 
ATOM   15589 C CA  . ASN   K  1 125 ? 56.58461  24.21560  53.25000  1.000 32.23394  ?  125 ASN   K CA  1 
ATOM   15590 C C   . ASN   K  1 125 ? 58.03128  24.63170  53.55037  1.000 37.85763  ?  125 ASN   K C   1 
ATOM   15591 O O   . ASN   K  1 125 ? 58.60545  25.44138  52.81587  1.000 41.84602  ?  125 ASN   K O   1 
ATOM   15592 C CB  . ASN   K  1 125 ? 55.80385  25.40483  52.69503  1.000 30.71995  ?  125 ASN   K CB  1 
ATOM   15593 C CG  . ASN   K  1 125 ? 56.12146  25.67297  51.23983  1.000 28.85087  ?  125 ASN   K CG  1 
ATOM   15594 O OD1 . ASN   K  1 125 ? 56.67221  24.81715  50.53468  1.000 35.01420  ?  125 ASN   K OD1 1 
ATOM   15595 N ND2 . ASN   K  1 125 ? 55.76507  26.86048  50.77532  1.000 46.16401  ?  125 ASN   K ND2 1 
ATOM   15596 N N   . THR   K  1 126 ? 58.63814  24.08867  54.59261  1.000 34.73756  ?  126 THR   K N   1 
ATOM   15597 C CA  . THR   K  1 126 ? 60.03071  24.35440  54.91100  1.000 43.82748  ?  126 THR   K CA  1 
ATOM   15598 C C   . THR   K  1 126 ? 60.80315  23.04542  54.93130  1.000 22.69786  ?  126 THR   K C   1 
ATOM   15599 O O   . THR   K  1 126 ? 60.22416  21.96176  55.05129  1.000 41.62053  ?  126 THR   K O   1 
ATOM   15600 C CB  . THR   K  1 126 ? 60.17206  25.04672  56.27264  1.000 28.57758  ?  126 THR   K CB  1 
ATOM   15601 O OG1 . THR   K  1 126 ? 59.89955  24.10261  57.32599  1.000 27.99992  ?  126 THR   K OG1 1 
ATOM   15602 C CG2 . THR   K  1 126 ? 59.20398  26.22265  56.37763  1.000 13.59776  ?  126 THR   K CG2 1 
ATOM   15603 N N   . ARG   K  1 127 ? 62.12708  23.15572  54.82980  1.000 89.48155  ?  127 ARG   K N   1 
ATOM   15604 C CA  . ARG   K  1 127 ? 62.95311  21.96093  54.95814  1.000 16.16610  ?  127 ARG   K CA  1 
ATOM   15605 C C   . ARG   K  1 127 ? 62.97510  21.44137  56.40348  1.000 16.92470  ?  127 ARG   K C   1 
ATOM   15606 O O   . ARG   K  1 127 ? 62.99047  20.22768  56.62006  1.000 41.23550  ?  127 ARG   K O   1 
ATOM   15607 C CB  . ARG   K  1 127 ? 64.36228  22.22667  54.43211  1.000 52.58495  ?  127 ARG   K CB  1 
ATOM   15608 C CG  . ARG   K  1 127 ? 64.62741  21.76456  52.95019  1.000 41.30427  ?  127 ARG   K CG  1 
ATOM   15609 C CD  . ARG   K  1 127 ? 65.95854  21.03268  52.81453  1.000 86.69070  ?  127 ARG   K CD  1 
ATOM   15610 N NE  . ARG   K  1 127 ? 67.00925  21.71951  53.56043  1.000 149.70692 ?  127 ARG   K NE  1 
ATOM   15611 C CZ  . ARG   K  1 127 ? 68.06063  21.11713  54.10128  1.000 136.41802 ?  127 ARG   K CZ  1 
ATOM   15612 N NH1 . ARG   K  1 127 ? 68.23224  19.80471  53.99164  1.000 68.18911  ?  127 ARG   K NH1 1 
ATOM   15613 N NH2 . ARG   K  1 127 ? 68.95805  21.84784  54.77294  1.000 101.09609 ?  127 ARG   K NH2 1 
ATOM   15614 N N   . ALA   K  1 128 ? 62.91330  22.32296  57.40099  1.000 26.77577  ?  128 ALA   K N   1 
ATOM   15615 C CA  . ALA   K  1 128 ? 62.82534  21.89336  58.79302  1.000 39.74703  ?  128 ALA   K CA  1 
ATOM   15616 C C   . ALA   K  1 128 ? 61.51412  21.15607  59.05481  1.000 30.67831  ?  128 ALA   K C   1 
ATOM   15617 O O   . ALA   K  1 128 ? 61.50475  20.11461  59.72724  1.000 41.51807  ?  128 ALA   K O   1 
ATOM   15618 C CB  . ALA   K  1 128 ? 62.97769  23.10227  59.73173  1.000 28.51525  ?  128 ALA   K CB  1 
ATOM   15619 N N   . GLY   K  1 129 ? 60.40013  21.66859  58.51196  1.000 47.57733  ?  129 GLY   K N   1 
ATOM   15620 C CA  . GLY   K  1 129 ? 59.10838  21.02149  58.72693  1.000 15.58654  ?  129 GLY   K CA  1 
ATOM   15621 C C   . GLY   K  1 129 ? 59.03019  19.64462  58.08391  1.000 40.08342  ?  129 GLY   K C   1 
ATOM   15622 O O   . GLY   K  1 129 ? 58.58909  18.67160  58.70794  1.000 29.92874  ?  129 GLY   K O   1 
ATOM   15623 N N   . PHE   K  1 130 ? 59.47581  19.53993  56.82896  1.000 34.41570  ?  130 PHE   K N   1 
ATOM   15624 C CA  . PHE   K  1 130 ? 59.50450  18.23986  56.17116  1.000 34.50209  ?  130 PHE   K CA  1 
ATOM   15625 C C   . PHE   K  1 130 ? 60.33696  17.22611  56.96277  1.000 55.43365  ?  130 PHE   K C   1 
ATOM   15626 O O   . PHE   K  1 130 ? 59.91153  16.07846  57.13181  1.000 46.58840  ?  130 PHE   K O   1 
ATOM   15627 C CB  . PHE   K  1 130 ? 60.03008  18.40112  54.74636  1.000 23.09432  ?  130 PHE   K CB  1 
ATOM   15628 C CG  . PHE   K  1 130 ? 60.16622  17.11065  54.00171  1.000 36.53900  ?  130 PHE   K CG  1 
ATOM   15629 C CD1 . PHE   K  1 130 ? 61.30971  16.31923  54.14471  1.000 36.53499  ?  130 PHE   K CD1 1 
ATOM   15630 C CD2 . PHE   K  1 130 ? 59.16318  16.68455  53.15060  1.000 30.13623  ?  130 PHE   K CD2 1 
ATOM   15631 C CE1 . PHE   K  1 130 ? 61.45108  15.12055  53.46062  1.000 35.36796  ?  130 PHE   K CE1 1 
ATOM   15632 C CE2 . PHE   K  1 130 ? 59.29333  15.47940  52.46049  1.000 43.96109  ?  130 PHE   K CE2 1 
ATOM   15633 C CZ  . PHE   K  1 130 ? 60.45869  14.69579  52.62088  1.000 30.40965  ?  130 PHE   K CZ  1 
ATOM   15634 N N   . SER   K  1 131 ? 61.52746  17.62086  57.44591  1.000 28.23353  ?  131 SER   K N   1 
ATOM   15635 C CA  . SER   K  1 131 ? 62.31752  16.71585  58.28739  1.000 45.90691  ?  131 SER   K CA  1 
ATOM   15636 C C   . SER   K  1 131 ? 61.51142  16.22032  59.48195  1.000 33.56596  ?  131 SER   K C   1 
ATOM   15637 O O   . SER   K  1 131 ? 61.45681  15.01145  59.75352  1.000 44.41254  ?  131 SER   K O   1 
ATOM   15638 C CB  . SER   K  1 131 ? 63.59337  17.39721  58.78072  1.000 17.13197  ?  131 SER   K CB  1 
ATOM   15639 O OG  . SER   K  1 131 ? 64.65709  17.11034  57.91401  1.000 88.99898  ?  131 SER   K OG  1 
ATOM   15640 N N   . ALA   K  1 132 ? 60.91147  17.14993  60.23400  1.000 35.02482  ?  132 ALA   K N   1 
ATOM   15641 C CA  . ALA   K  1 132 ? 60.16920  16.75925  61.42681  1.000 29.28705  ?  132 ALA   K CA  1 
ATOM   15642 C C   . ALA   K  1 132 ? 59.04189  15.80482  61.06998  1.000 43.57727  ?  132 ALA   K C   1 
ATOM   15643 O O   . ALA   K  1 132 ? 58.87476  14.75111  61.70320  1.000 37.34141  ?  132 ALA   K O   1 
ATOM   15644 C CB  . ALA   K  1 132 ? 59.61821  17.99393  62.13242  1.000 30.00925  ?  132 ALA   K CB  1 
ATOM   15645 N N   . PHE   K  1 133 ? 58.28403  16.14743  60.02390  1.000 27.86742  ?  133 PHE   K N   1 
ATOM   15646 C CA  . PHE   K  1 133 ? 57.07592  15.43101  59.63348  1.000 38.44212  ?  133 PHE   K CA  1 
ATOM   15647 C C   . PHE   K  1 133 ? 57.37001  14.10988  58.92783  1.000 45.39079  ?  133 PHE   K C   1 
ATOM   15648 O O   . PHE   K  1 133 ? 56.43185  13.36607  58.61066  1.000 34.90336  ?  133 PHE   K O   1 
ATOM   15649 C CB  . PHE   K  1 133 ? 56.20448  16.33335  58.75387  1.000 30.66093  ?  133 PHE   K CB  1 
ATOM   15650 C CG  . PHE   K  1 133 ? 55.90822  17.67363  59.38433  1.000 41.61098  ?  133 PHE   K CG  1 
ATOM   15651 C CD1 . PHE   K  1 133 ? 55.94851  17.83119  60.77896  1.000 37.16318  ?  133 PHE   K CD1 1 
ATOM   15652 C CD2 . PHE   K  1 133 ? 55.60863  18.77903  58.59299  1.000 31.87567  ?  133 PHE   K CD2 1 
ATOM   15653 C CE1 . PHE   K  1 133 ? 55.69193  19.06565  61.36928  1.000 29.02757  ?  133 PHE   K CE1 1 
ATOM   15654 C CE2 . PHE   K  1 133 ? 55.35308  20.01805  59.16502  1.000 31.29868  ?  133 PHE   K CE2 1 
ATOM   15655 C CZ  . PHE   K  1 133 ? 55.39249  20.16495  60.56054  1.000 25.09120  ?  133 PHE   K CZ  1 
ATOM   15656 N N   . THR   K  1 134 ? 58.64158  13.77972  58.69612  1.000 32.03763  ?  134 THR   K N   1 
ATOM   15657 C CA  . THR   K  1 134 ? 59.00232  12.47907  58.15046  1.000 36.69639  ?  134 THR   K CA  1 
ATOM   15658 C C   . THR   K  1 134 ? 59.72982  11.60644  59.17685  1.000 34.52309  ?  134 THR   K C   1 
ATOM   15659 O O   . THR   K  1 134 ? 60.47018  10.69080  58.80907  1.000 42.47466  ?  134 THR   K O   1 
ATOM   15660 C CB  . THR   K  1 134 ? 59.82356  12.62344  56.86737  1.000 36.71316  ?  134 THR   K CB  1 
ATOM   15661 O OG1 . THR   K  1 134 ? 60.85581  13.60525  57.03692  1.000 42.40143  ?  134 THR   K OG1 1 
ATOM   15662 C CG2 . THR   K  1 134 ? 58.91697  13.02646  55.70568  1.000 29.70832  ?  134 THR   K CG2 1 
ATOM   15663 N N   . ARG   K  1 135 ? 59.49183  11.85501  60.46721  1.000 30.77160  ?  135 ARG   K N   1 
ATOM   15664 C CA  . ARG   K  1 135 ? 59.97012  10.99526  61.54869  1.000 30.95002  ?  135 ARG   K CA  1 
ATOM   15665 C C   . ARG   K  1 135 ? 58.80344  10.15270  62.04921  1.000 44.57482  ?  135 ARG   K C   1 
ATOM   15666 O O   . ARG   K  1 135 ? 57.78888  10.69929  62.50519  1.000 31.18387  ?  135 ARG   K O   1 
ATOM   15667 C CB  . ARG   K  1 135 ? 60.55483  11.80956  62.70488  1.000 21.76812  ?  135 ARG   K CB  1 
ATOM   15668 C CG  . ARG   K  1 135 ? 61.73668  12.70440  62.33647  1.000 25.97343  ?  135 ARG   K CG  1 
ATOM   15669 C CD  . ARG   K  1 135 ? 61.93834  13.70713  63.44184  1.000 28.70936  ?  135 ARG   K CD  1 
ATOM   15670 N NE  . ARG   K  1 135 ? 63.08480  14.57015  63.21787  1.000 48.00418  ?  135 ARG   K NE  1 
ATOM   15671 C CZ  . ARG   K  1 135 ? 64.34427  14.17031  63.31409  1.000 51.82027  ?  135 ARG   K CZ  1 
ATOM   15672 N NH1 . ARG   K  1 135 ? 64.65065  12.92217  63.63120  1.000 42.99480  ?  135 ARG   K NH1 1 
ATOM   15673 N NH2 . ARG   K  1 135 ? 65.32137  15.04063  63.06735  1.000 40.92470  ?  135 ARG   K NH2 1 
ATOM   15674 N N   . GLN   K  1 136 ? 58.94580  8.82440   61.96122  1.000 31.38027  ?  136 GLN   K N   1 
ATOM   15675 C CA  . GLN   K  1 136 ? 57.88866  7.93808   62.44032  1.000 33.39874  ?  136 GLN   K CA  1 
ATOM   15676 C C   . GLN   K  1 136 ? 57.54621  8.21477   63.89476  1.000 30.76284  ?  136 GLN   K C   1 
ATOM   15677 O O   . GLN   K  1 136 ? 56.37641  8.09158   64.28714  1.000 48.25722  ?  136 GLN   K O   1 
ATOM   15678 C CB  . GLN   K  1 136 ? 58.29500  6.47666   62.25741  1.000 31.45122  ?  136 GLN   K CB  1 
ATOM   15679 C CG  . GLN   K  1 136 ? 58.52274  6.11181   60.81105  1.000 26.68402  ?  136 GLN   K CG  1 
ATOM   15680 C CD  . GLN   K  1 136 ? 57.87385  4.80349   60.43449  1.000 51.94235  ?  136 GLN   K CD  1 
ATOM   15681 O OE1 . GLN   K  1 136 ? 57.97251  3.79642   61.16815  1.000 39.86232  ?  136 GLN   K OE1 1 
ATOM   15682 N NE2 . GLN   K  1 136 ? 57.19090  4.80416   59.28492  1.000 27.18643  ?  136 GLN   K NE2 1 
ATOM   15683 N N   . ARG   K  1 137 ? 58.53649  8.65770   64.69426  1.000 36.88858  ?  137 ARG   K N   1 
ATOM   15684 C CA  . ARG   K  1 137 ? 58.29897  8.89994   66.12139  1.000 18.60346  ?  137 ARG   K CA  1 
ATOM   15685 C C   . ARG   K  1 137 ? 57.31349  10.02200  66.31514  1.000 70.97415  ?  137 ARG   K C   1 
ATOM   15686 O O   . ARG   K  1 137 ? 56.34218  9.88762   67.06508  1.000 32.70592  ?  137 ARG   K O   1 
ATOM   15687 C CB  . ARG   K  1 137 ? 59.59962  9.24005   66.85620  1.000 19.19908  ?  137 ARG   K CB  1 
ATOM   15688 C CG  . ARG   K  1 137 ? 60.49308  8.02727   67.10708  1.000 75.56951  ?  137 ARG   K CG  1 
ATOM   15689 C CD  . ARG   K  1 137 ? 61.70944  8.51121   67.79742  1.000 80.36694  ?  137 ARG   K CD  1 
ATOM   15690 N NE  . ARG   K  1 137 ? 62.76578  7.52440   67.76215  1.000 98.66757  ?  137 ARG   K NE  1 
ATOM   15691 C CZ  . ARG   K  1 137 ? 63.96459  7.72626   68.27715  1.000 92.94322  ?  137 ARG   K CZ  1 
ATOM   15692 N NH1 . ARG   K  1 137 ? 64.26613  8.86514   68.88965  1.000 56.21643  ?  137 ARG   K NH1 1 
ATOM   15693 N NH2 . ARG   K  1 137 ? 64.86269  6.74628   68.22772  1.000 116.49487 ?  137 ARG   K NH2 1 
ATOM   15694 N N   . LEU   K  1 138 ? 57.56831  11.15084  65.64560  1.000 24.61425  ?  138 LEU   K N   1 
ATOM   15695 C CA  . LEU   K  1 138 ? 56.62384  12.27158  65.69294  1.000 37.67172  ?  138 LEU   K CA  1 
ATOM   15696 C C   . LEU   K  1 138 ? 55.24944  11.88416  65.14870  1.000 47.11073  ?  138 LEU   K C   1 
ATOM   15697 O O   . LEU   K  1 138 ? 54.21590  12.25130  65.72391  1.000 36.66002  ?  138 LEU   K O   1 
ATOM   15698 C CB  . LEU   K  1 138 ? 57.16945  13.45290  64.89779  1.000 31.45505  ?  138 LEU   K CB  1 
ATOM   15699 C CG  . LEU   K  1 138 ? 56.33104  14.71553  65.01323  1.000 45.33491  ?  138 LEU   K CG  1 
ATOM   15700 C CD1 . LEU   K  1 138 ? 56.39654  15.19346  66.44880  1.000 31.81344  ?  138 LEU   K CD1 1 
ATOM   15701 C CD2 . LEU   K  1 138 ? 56.82689  15.79360  64.06375  1.000 29.14643  ?  138 LEU   K CD2 1 
ATOM   15702 N N   . ASN   K  1 139 ? 55.21456  11.15091  64.03614  1.000 28.50111  ?  139 ASN   K N   1 
ATOM   15703 C CA  . ASN   K  1 139 ? 53.92809  10.82077  63.43780  1.000 44.70355  ?  139 ASN   K CA  1 
ATOM   15704 C C   . ASN   K  1 139 ? 53.07758  9.95567   64.35971  1.000 31.31084  ?  139 ASN   K C   1 
ATOM   15705 O O   . ASN   K  1 139 ? 51.84237  10.02231  64.28938  1.000 45.21303  ?  139 ASN   K O   1 
ATOM   15706 C CB  . ASN   K  1 139 ? 54.14736  10.17053  62.07312  1.000 21.00473  ?  139 ASN   K CB  1 
ATOM   15707 C CG  . ASN   K  1 139 ? 54.54668  11.19618  61.03418  1.000 37.82718  ?  139 ASN   K CG  1 
ATOM   15708 O OD1 . ASN   K  1 139 ? 53.98460  12.29895  61.01264  1.000 29.40604  ?  139 ASN   K OD1 1 
ATOM   15709 N ND2 . ASN   K  1 139 ? 55.53854  10.87744  60.20728  1.000 26.22690  ?  139 ASN   K ND2 1 
ATOM   15710 N N   . LEU   K  1 140 ? 53.70779  9.16899   65.24486  1.000 44.58233  ?  140 LEU   K N   1 
ATOM   15711 C CA  . LEU   K  1 140 ? 52.94624  8.46272   66.27617  1.000 32.73395  ?  140 LEU   K CA  1 
ATOM   15712 C C   . LEU   K  1 140 ? 52.12659  9.43250   67.11502  1.000 55.01410  ?  140 LEU   K C   1 
ATOM   15713 O O   . LEU   K  1 140 ? 50.99721  9.11452   67.51625  1.000 33.93951  ?  140 LEU   K O   1 
ATOM   15714 C CB  . LEU   K  1 140 ? 53.87575  7.66966   67.18551  1.000 32.27260  ?  140 LEU   K CB  1 
ATOM   15715 C CG  . LEU   K  1 140 ? 54.46132  6.41131   66.56316  1.000 48.51367  ?  140 LEU   K CG  1 
ATOM   15716 C CD1 . LEU   K  1 140 ? 55.45136  5.74319   67.49667  1.000 26.48185  ?  140 LEU   K CD1 1 
ATOM   15717 C CD2 . LEU   K  1 140 ? 53.34507  5.46787   66.19663  1.000 20.33701  ?  140 LEU   K CD2 1 
ATOM   15718 N N   . HIS   K  1 141 ? 52.68058  10.62457  67.39192  1.000 37.66038  ?  141 HIS   K N   1 
ATOM   15719 C CA  . HIS   K  1 141 ? 51.95063  11.60112  68.19440  1.000 35.55909  ?  141 HIS   K CA  1 
ATOM   15720 C C   . HIS   K  1 141 ? 50.81620  12.23846  67.40187  1.000 36.73613  ?  141 HIS   K C   1 
ATOM   15721 O O   . HIS   K  1 141 ? 49.69653  12.36343  67.91129  1.000 43.42312  ?  141 HIS   K O   1 
ATOM   15722 C CB  . HIS   K  1 141 ? 52.90621  12.65193  68.72972  1.000 25.53498  ?  141 HIS   K CB  1 
ATOM   15723 C CG  . HIS   K  1 141 ? 53.79069  12.13411  69.81756  1.000 53.08574  ?  141 HIS   K CG  1 
ATOM   15724 N ND1 . HIS   K  1 141 ? 53.37607  12.04767  71.12815  1.000 50.92321  ?  141 HIS   K ND1 1 
ATOM   15725 C CD2 . HIS   K  1 141 ? 55.05339  11.64173  69.78787  1.000 46.24448  ?  141 HIS   K CD2 1 
ATOM   15726 C CE1 . HIS   K  1 141 ? 54.34977  11.53895  71.86203  1.000 38.44549  ?  141 HIS   K CE1 1 
ATOM   15727 N NE2 . HIS   K  1 141 ? 55.38082  11.28792  71.07436  1.000 51.69378  ?  141 HIS   K NE2 1 
ATOM   15728 N N   . PHE   K  1 142 ? 51.07191  12.62536  66.14544  1.000 31.78298  ?  142 PHE   K N   1 
ATOM   15729 C CA  . PHE   K  1 142 ? 49.98087  13.11449  65.30173  1.000 45.01799  ?  142 PHE   K CA  1 
ATOM   15730 C C   . PHE   K  1 142 ? 48.83794  12.11126  65.25411  1.000 31.91273  ?  142 PHE   K C   1 
ATOM   15731 O O   . PHE   K  1 142 ? 47.65889  12.48951  65.32250  1.000 33.87190  ?  142 PHE   K O   1 
ATOM   15732 C CB  . PHE   K  1 142 ? 50.48491  13.41020  63.89006  1.000 30.98380  ?  142 PHE   K CB  1 
ATOM   15733 C CG  . PHE   K  1 142 ? 51.27286  14.68031  63.78535  1.000 38.16819  ?  142 PHE   K CG  1 
ATOM   15734 C CD1 . PHE   K  1 142 ? 50.79947  15.84959  64.34978  1.000 33.00023  ?  142 PHE   K CD1 1 
ATOM   15735 C CD2 . PHE   K  1 142 ? 52.49511  14.70391  63.12986  1.000 34.49129  ?  142 PHE   K CD2 1 
ATOM   15736 C CE1 . PHE   K  1 142 ? 51.53054  17.01836  64.25627  1.000 32.07898  ?  142 PHE   K CE1 1 
ATOM   15737 C CE2 . PHE   K  1 142 ? 53.22390  15.87836  63.03335  1.000 35.59656  ?  142 PHE   K CE2 1 
ATOM   15738 C CZ  . PHE   K  1 142 ? 52.73856  17.02876  63.59799  1.000 30.81321  ?  142 PHE   K CZ  1 
ATOM   15739 N N   . LYS   K  1 143 ? 49.16898  10.82638  65.13935  1.000 38.18648  ?  143 LYS   K N   1 
ATOM   15740 C CA  . LYS   K  1 143 ? 48.13256  9.80651   65.14319  1.000 33.85345  ?  143 LYS   K CA  1 
ATOM   15741 C C   . LYS   K  1 143 ? 47.27512  9.92484   66.38919  1.000 37.12908  ?  143 LYS   K C   1 
ATOM   15742 O O   . LYS   K  1 143 ? 46.04148  9.99073   66.29622  1.000 40.49065  ?  143 LYS   K O   1 
ATOM   15743 C CB  . LYS   K  1 143 ? 48.75361  8.41806   65.04878  1.000 37.40659  ?  143 LYS   K CB  1 
ATOM   15744 C CG  . LYS   K  1 143 ? 47.74736  7.35410   64.71441  1.000 23.97129  ?  143 LYS   K CG  1 
ATOM   15745 C CD  . LYS   K  1 143 ? 48.07887  6.05486   65.38816  1.000 32.13290  ?  143 LYS   K CD  1 
ATOM   15746 C CE  . LYS   K  1 143 ? 47.25721  4.92764   64.79289  1.000 38.69120  ?  143 LYS   K CE  1 
ATOM   15747 N NZ  . LYS   K  1 143 ? 45.79715  5.05874   65.04611  1.000 43.30035  ?  143 LYS   K NZ  1 
ATOM   15748 N N   . LYS   K  1 144 ? 47.95129  10.01715  67.56384  1.000 19.45271  ?  144 LYS   K N   1 
ATOM   15749 C CA  . LYS   K  1 144 ? 47.27395  10.08460  68.85498  1.000 58.34016  ?  144 LYS   K CA  1 
ATOM   15750 C C   . LYS   K  1 144 ? 46.45449  11.36170  68.98841  1.000 56.92979  ?  144 LYS   K C   1 
ATOM   15751 O O   . LYS   K  1 144 ? 45.35432  11.31650  69.54691  1.000 42.62745  ?  144 LYS   K O   1 
ATOM   15752 C CB  . LYS   K  1 144 ? 48.29289  9.93312   70.00516  1.000 17.97298  ?  144 LYS   K CB  1 
ATOM   15753 C CG  . LYS   K  1 144 ? 47.65262  9.54025   71.41117  1.000 97.65736  ?  144 LYS   K CG  1 
ATOM   15754 C CD  . LYS   K  1 144 ? 46.72993  8.28932   71.35469  1.000 101.42329 ?  144 LYS   K CD  1 
ATOM   15755 C CE  . LYS   K  1 144 ? 46.40876  7.70286   72.73162  1.000 104.00714 ?  144 LYS   K CE  1 
ATOM   15756 N NZ  . LYS   K  1 144 ? 46.88434  6.28896   72.93463  1.000 81.01634  ?  144 LYS   K NZ  1 
ATOM   15757 N N   . LEU   K  1 145 ? 46.94623  12.48277  68.43454  1.000 36.01990  ?  145 LEU   K N   1 
ATOM   15758 C CA  . LEU   K  1 145 ? 46.20937  13.74371  68.43665  1.000 30.44793  ?  145 LEU   K CA  1 
ATOM   15759 C C   . LEU   K  1 145 ? 44.92492  13.62070  67.61938  1.000 50.60919  ?  145 LEU   K C   1 
ATOM   15760 O O   . LEU   K  1 145 ? 43.82560  13.89248  68.11897  1.000 48.83609  ?  145 LEU   K O   1 
ATOM   15761 C CB  . LEU   K  1 145 ? 47.09514  14.87853  67.91011  1.000 41.28421  ?  145 LEU   K CB  1 
ATOM   15762 C CG  . LEU   K  1 145 ? 48.33019  15.18112  68.76840  1.000 43.93553  ?  145 LEU   K CG  1 
ATOM   15763 C CD1 . LEU   K  1 145 ? 49.12078  16.37083  68.23931  1.000 37.63664  ?  145 LEU   K CD1 1 
ATOM   15764 C CD2 . LEU   K  1 145 ? 47.91586  15.42944  70.19711  1.000 37.01647  ?  145 LEU   K CD2 1 
ATOM   15765 N N   . PHE   K  1 146 ? 45.03829  13.14808  66.37616  1.000 29.09725  ?  146 PHE   K N   1 
ATOM   15766 C CA  . PHE   K  1 146 ? 43.87142  13.10499  65.50013  1.000 33.05137  ?  146 PHE   K CA  1 
ATOM   15767 C C   . PHE   K  1 146 ? 42.87804  12.03430  65.92957  1.000 41.29064  ?  146 PHE   K C   1 
ATOM   15768 O O   . PHE   K  1 146 ? 41.66634  12.23081  65.78915  1.000 42.00036  ?  146 PHE   K O   1 
ATOM   15769 C CB  . PHE   K  1 146 ? 44.31408  12.88871  64.05006  1.000 33.28004  ?  146 PHE   K CB  1 
ATOM   15770 C CG  . PHE   K  1 146 ? 45.28333  13.93865  63.54293  1.000 36.85367  ?  146 PHE   K CG  1 
ATOM   15771 C CD1 . PHE   K  1 146 ? 45.33048  15.21106  64.11590  1.000 36.89710  ?  146 PHE   K CD1 1 
ATOM   15772 C CD2 . PHE   K  1 146 ? 46.13613  13.65632  62.49114  1.000 29.96215  ?  146 PHE   K CD2 1 
ATOM   15773 C CE1 . PHE   K  1 146 ? 46.21043  16.17132  63.64522  1.000 37.01237  ?  146 PHE   K CE1 1 
ATOM   15774 C CE2 . PHE   K  1 146 ? 47.02491  14.61123  62.01401  1.000 33.54520  ?  146 PHE   K CE2 1 
ATOM   15775 C CZ  . PHE   K  1 146 ? 47.06205  15.87198  62.58769  1.000 39.20338  ?  146 PHE   K CZ  1 
ATOM   15776 N N   . ASP   K  1 147 ? 43.35407  10.90167  66.45268  1.000 41.18893  ?  147 ASP   K N   1 
ATOM   15777 C CA  . ASP   K  1 147 ? 42.41385  9.92549   66.99641  1.000 34.81695  ?  147 ASP   K CA  1 
ATOM   15778 C C   . ASP   K  1 147 ? 41.61507  10.53573  68.14109  1.000 44.38168  ?  147 ASP   K C   1 
ATOM   15779 O O   . ASP   K  1 147 ? 40.39205  10.33317  68.24134  1.000 42.69551  ?  147 ASP   K O   1 
ATOM   15780 C CB  . ASP   K  1 147 ? 43.14239  8.66489   67.47411  1.000 27.26340  ?  147 ASP   K CB  1 
ATOM   15781 C CG  . ASP   K  1 147 ? 43.65197  7.79410   66.32893  1.000 60.34156  ?  147 ASP   K CG  1 
ATOM   15782 O OD1 . ASP   K  1 147 ? 43.17302  7.93084   65.17136  1.000 52.45755  ?  147 ASP   K OD1 1 
ATOM   15783 O OD2 . ASP   K  1 147 ? 44.53438  6.95395   66.60901  1.000 56.63803  -1 147 ASP   K OD2 1 
ATOM   15784 N N   . THR   K  1 148 ? 42.29630  11.28660  69.01666  1.000 41.16346  ?  148 THR   K N   1 
ATOM   15785 C CA  . THR   K  1 148 ? 41.61546  11.95442  70.12020  1.000 50.61225  ?  148 THR   K CA  1 
ATOM   15786 C C   . THR   K  1 148 ? 40.56201  12.91636  69.58640  1.000 47.51804  ?  148 THR   K C   1 
ATOM   15787 O O   . THR   K  1 148 ? 39.40954  12.90839  70.04060  1.000 53.53369  ?  148 THR   K O   1 
ATOM   15788 C CB  . THR   K  1 148 ? 42.64104  12.67927  71.00313  1.000 45.47349  ?  148 THR   K CB  1 
ATOM   15789 O OG1 . THR   K  1 148 ? 43.40963  11.71355  71.72778  1.000 46.34104  ?  148 THR   K OG1 1 
ATOM   15790 C CG2 . THR   K  1 148 ? 41.95866  13.60338  72.00254  1.000 34.77688  ?  148 THR   K CG2 1 
ATOM   15791 N N   . TRP   K  1 149 ? 40.94026  13.72976  68.58844  1.000 46.52685  ?  149 TRP   K N   1 
ATOM   15792 C CA  . TRP   K  1 149 ? 39.99929  14.65363  67.96285  1.000 39.63275  ?  149 TRP   K CA  1 
ATOM   15793 C C   . TRP   K  1 149 ? 38.80679  13.90104  67.38818  1.000 63.65906  ?  149 TRP   K C   1 
ATOM   15794 O O   . TRP   K  1 149 ? 37.65578  14.31900  67.56139  1.000 48.47829  ?  149 TRP   K O   1 
ATOM   15795 C CB  . TRP   K  1 149 ? 40.71653  15.45995  66.87142  1.000 37.20361  ?  149 TRP   K CB  1 
ATOM   15796 C CG  . TRP   K  1 149 ? 39.89784  16.59058  66.24804  1.000 48.22838  ?  149 TRP   K CG  1 
ATOM   15797 C CD1 . TRP   K  1 149 ? 38.71708  17.10583  66.71061  1.000 42.55046  ?  149 TRP   K CD1 1 
ATOM   15798 C CD2 . TRP   K  1 149 ? 40.20938  17.33125  65.04948  1.000 58.56703  ?  149 TRP   K CD2 1 
ATOM   15799 N NE1 . TRP   K  1 149 ? 38.28060  18.11702  65.88456  1.000 54.76237  ?  149 TRP   K NE1 1 
ATOM   15800 C CE2 . TRP   K  1 149 ? 39.17468  18.27358  64.85819  1.000 41.04089  ?  149 TRP   K CE2 1 
ATOM   15801 C CE3 . TRP   K  1 149 ? 41.26126  17.28636  64.11858  1.000 40.15835  ?  149 TRP   K CE3 1 
ATOM   15802 C CZ2 . TRP   K  1 149 ? 39.16482  19.17293  63.78298  1.000 50.48641  ?  149 TRP   K CZ2 1 
ATOM   15803 C CZ3 . TRP   K  1 149 ? 41.24637  18.18619  63.03501  1.000 43.02054  ?  149 TRP   K CZ3 1 
ATOM   15804 C CH2 . TRP   K  1 149 ? 40.20622  19.11191  62.88358  1.000 50.23791  ?  149 TRP   K CH2 1 
ATOM   15805 N N   . GLY   K  1 150 ? 39.06575  12.76673  66.72628  1.000 41.92422  ?  150 GLY   K N   1 
ATOM   15806 C CA  . GLY   K  1 150 ? 37.99746  12.03679  66.06982  1.000 31.28120  ?  150 GLY   K CA  1 
ATOM   15807 C C   . GLY   K  1 150 ? 36.96404  11.50032  67.03798  1.000 52.57369  ?  150 GLY   K C   1 
ATOM   15808 O O   . GLY   K  1 150 ? 35.79535  11.32099  66.67025  1.000 64.62739  ?  150 GLY   K O   1 
ATOM   15809 N N   . LEU   K  1 151 ? 37.37957  11.22561  68.27814  1.000 45.02614  ?  151 LEU   K N   1 
ATOM   15810 C CA  . LEU   K  1 151 ? 36.43098  10.88095  69.33576  1.000 39.74428  ?  151 LEU   K CA  1 
ATOM   15811 C C   . LEU   K  1 151 ? 35.36912  11.94994  69.49606  1.000 79.18482  ?  151 LEU   K C   1 
ATOM   15812 O O   . LEU   K  1 151 ? 34.16421  11.65853  69.52691  1.000 52.24269  ?  151 LEU   K O   1 
ATOM   15813 C CB  . LEU   K  1 151 ? 37.15685  10.74245  70.65238  1.000 51.93968  ?  151 LEU   K CB  1 
ATOM   15814 C CG  . LEU   K  1 151 ? 37.99606  9.51091   70.77393  1.000 73.03634  ?  151 LEU   K CG  1 
ATOM   15815 C CD1 . LEU   K  1 151 ? 38.47363  9.57029   72.18166  1.000 38.20978  ?  151 LEU   K CD1 1 
ATOM   15816 C CD2 . LEU   K  1 151 ? 37.07747  8.35360   70.51757  1.000 26.73269  ?  151 LEU   K CD2 1 
ATOM   15817 N N   . PHE   K  1 152 ? 35.81580  13.19295  69.68530  1.000 35.46312  ?  152 PHE   K N   1 
ATOM   15818 C CA  . PHE   K  1 152 ? 34.88568  14.30303  69.77539  1.000 48.21351  ?  152 PHE   K CA  1 
ATOM   15819 C C   . PHE   K  1 152 ? 34.00733  14.39756  68.53237  1.000 61.44677  ?  152 PHE   K C   1 
ATOM   15820 O O   . PHE   K  1 152 ? 32.81384  14.69782  68.63501  1.000 53.90187  ?  152 PHE   K O   1 
ATOM   15821 C CB  . PHE   K  1 152 ? 35.64793  15.60443  69.98654  1.000 30.47689  ?  152 PHE   K CB  1 
ATOM   15822 C CG  . PHE   K  1 152 ? 34.77723  16.79479  69.91516  1.000 56.73451  ?  152 PHE   K CG  1 
ATOM   15823 C CD1 . PHE   K  1 152 ? 33.92953  17.09515  70.95987  1.000 39.68524  ?  152 PHE   K CD1 1 
ATOM   15824 C CD2 . PHE   K  1 152 ? 34.75374  17.58293  68.77797  1.000 47.55240  ?  152 PHE   K CD2 1 
ATOM   15825 C CE1 . PHE   K  1 152 ? 33.09281  18.17991  70.88622  1.000 46.67952  ?  152 PHE   K CE1 1 
ATOM   15826 C CE2 . PHE   K  1 152 ? 33.92444  18.67448  68.69815  1.000 57.13096  ?  152 PHE   K CE2 1 
ATOM   15827 C CZ  . PHE   K  1 152 ? 33.09285  18.97775  69.75314  1.000 48.87986  ?  152 PHE   K CZ  1 
ATOM   15828 N N   . LEU   K  1 153 ? 34.57107  14.14033  67.34901  1.000 47.52788  ?  153 LEU   K N   1 
ATOM   15829 C CA  . LEU   K  1 153 ? 33.80245  14.30124  66.11948  1.000 49.43485  ?  153 LEU   K CA  1 
ATOM   15830 C C   . LEU   K  1 153 ? 32.80369  13.17075  65.88991  1.000 49.02020  ?  153 LEU   K C   1 
ATOM   15831 O O   . LEU   K  1 153 ? 32.03385  13.22640  64.92496  1.000 53.41537  ?  153 LEU   K O   1 
ATOM   15832 C CB  . LEU   K  1 153 ? 34.74882  14.41958  64.93368  1.000 42.15526  ?  153 LEU   K CB  1 
ATOM   15833 C CG  . LEU   K  1 153 ? 35.72913  15.58410  64.98817  1.000 55.22319  ?  153 LEU   K CG  1 
ATOM   15834 C CD1 . LEU   K  1 153 ? 36.69149  15.48017  63.81568  1.000 37.40127  ?  153 LEU   K CD1 1 
ATOM   15835 C CD2 . LEU   K  1 153 ? 34.99719  16.92480  64.98386  1.000 37.41751  ?  153 LEU   K CD2 1 
ATOM   15836 N N   . SER   K  1 154 ? 32.80745  12.15498  66.75041  1.000 53.82468  ?  154 SER   K N   1 
ATOM   15837 C CA  . SER   K  1 154 ? 31.82555  11.08235  66.75075  1.000 51.57572  ?  154 SER   K CA  1 
ATOM   15838 C C   . SER   K  1 154 ? 30.74680  11.28956  67.80572  1.000 61.65778  ?  154 SER   K C   1 
ATOM   15839 O O   . SER   K  1 154 ? 29.81696  10.48166  67.89025  1.000 65.89914  ?  154 SER   K O   1 
ATOM   15840 C CB  . SER   K  1 154 ? 32.52612  9.74053   66.99179  1.000 38.77247  ?  154 SER   K CB  1 
ATOM   15841 O OG  . SER   K  1 154 ? 33.38252  9.45049   65.90818  1.000 119.40655 ?  154 SER   K OG  1 
ATOM   15842 N N   . SER   K  1 155 ? 30.85329  12.34817  68.60587  1.000 52.97150  ?  155 SER   K N   1 
ATOM   15843 C CA  . SER   K  1 155 ? 30.02113  12.58916  69.77429  1.000 53.59538  ?  155 SER   K CA  1 
ATOM   15844 C C   . SER   K  1 155 ? 28.89460  13.55616  69.43513  1.000 118.19981 ?  155 SER   K C   1 
ATOM   15845 O O   . SER   K  1 155 ? 29.02030  14.39099  68.52883  1.000 51.68495  ?  155 SER   K O   1 
ATOM   15846 C CB  . SER   K  1 155 ? 30.86040  13.16347  70.91595  1.000 50.34802  ?  155 SER   K CB  1 
ATOM   15847 O OG  . SER   K  1 155 ? 31.26359  14.49963  70.65060  1.000 60.39749  ?  155 SER   K OG  1 
ATOM   15848 N N   . LYS   K  1 156 ? 27.79166  13.44951  70.19719  1.000 67.82358  ?  156 LYS   K N   1 
ATOM   15849 C CA  . LYS   K  1 156 ? 26.62573  14.28980  69.92664  1.000 84.64181  ?  156 LYS   K CA  1 
ATOM   15850 C C   . LYS   K  1 156 ? 27.00339  15.76970  69.93740  1.000 58.06273  ?  156 LYS   K C   1 
ATOM   15851 O O   . LYS   K  1 156 ? 26.43198  16.56529  69.17955  1.000 73.90694  ?  156 LYS   K O   1 
ATOM   15852 C CB  . LYS   K  1 156 ? 25.50285  13.99267  70.93379  1.000 50.77806  ?  156 LYS   K CB  1 
ATOM   15853 N N   . ASP   K  1 157 ? 28.02204  16.13932  70.72740  1.000 57.59988  ?  157 ASP   K N   1 
ATOM   15854 C CA  . ASP   K  1 157 ? 28.41538  17.54258  70.87285  1.000 56.57225  ?  157 ASP   K CA  1 
ATOM   15855 C C   . ASP   K  1 157 ? 28.99534  18.13590  69.59665  1.000 59.09133  ?  157 ASP   K C   1 
ATOM   15856 O O   . ASP   K  1 157 ? 28.97012  19.36244  69.43106  1.000 54.97720  ?  157 ASP   K O   1 
ATOM   15857 C CB  . ASP   K  1 157 ? 29.43084  17.69625  72.00665  1.000 67.92376  ?  157 ASP   K CB  1 
ATOM   15858 C CG  . ASP   K  1 157 ? 28.82440  17.43205  73.37970  1.000 68.96181  ?  157 ASP   K CG  1 
ATOM   15859 O OD1 . ASP   K  1 157 ? 27.76296  18.01383  73.69021  1.000 79.56295  ?  157 ASP   K OD1 1 
ATOM   15860 O OD2 . ASP   K  1 157 ? 29.41343  16.63520  74.14517  1.000 98.26598  -1 157 ASP   K OD2 1 
ATOM   15861 N N   . SER   K  1 158 ? 29.52841  17.30384  68.69959  1.000 78.49850  ?  158 SER   K N   1 
ATOM   15862 C CA  . SER   K  1 158 ? 30.05886  17.82752  67.44867  1.000 63.92757  ?  158 SER   K CA  1 
ATOM   15863 C C   . SER   K  1 158 ? 28.96134  18.20837  66.45756  1.000 66.77249  ?  158 SER   K C   1 
ATOM   15864 O O   . SER   K  1 158 ? 29.29292  18.71038  65.37739  1.000 61.83138  ?  158 SER   K O   1 
ATOM   15865 C CB  . SER   K  1 158 ? 31.01419  16.81040  66.81227  1.000 57.38509  ?  158 SER   K CB  1 
ATOM   15866 O OG  . SER   K  1 158 ? 30.31033  15.67078  66.34024  1.000 56.84360  ?  158 SER   K OG  1 
ATOM   15867 N N   . ARG   K  1 159 ? 27.67717  17.99975  66.78696  1.000 59.71149  ?  159 ARG   K N   1 
ATOM   15868 C CA  . ARG   K  1 159 ? 26.59994  18.39972  65.88009  1.000 66.92769  ?  159 ARG   K CA  1 
ATOM   15869 C C   . ARG   K  1 159 ? 26.44431  19.91268  65.76729  1.000 67.68417  ?  159 ARG   K C   1 
ATOM   15870 O O   . ARG   K  1 159 ? 25.80557  20.38382  64.82348  1.000 62.10202  ?  159 ARG   K O   1 
ATOM   15871 C CB  . ARG   K  1 159 ? 25.26734  17.80497  66.32826  1.000 49.56020  ?  159 ARG   K CB  1 
ATOM   15872 C CG  . ARG   K  1 159 ? 25.15487  16.31753  66.08801  1.000 85.52998  ?  159 ARG   K CG  1 
ATOM   15873 C CD  . ARG   K  1 159 ? 23.93418  15.79240  66.78840  1.000 69.61324  ?  159 ARG   K CD  1 
ATOM   15874 N NE  . ARG   K  1 159 ? 23.94664  16.20345  68.18367  1.000 83.47583  ?  159 ARG   K NE  1 
ATOM   15875 C CZ  . ARG   K  1 159 ? 22.89298  16.16947  68.98558  1.000 74.64323  ?  159 ARG   K CZ  1 
ATOM   15876 N NH1 . ARG   K  1 159 ? 21.70893  15.75852  68.55630  1.000 67.11506  ?  159 ARG   K NH1 1 
ATOM   15877 N NH2 . ARG   K  1 159 ? 23.03084  16.56102  70.24767  1.000 64.33562  ?  159 ARG   K NH2 1 
ATOM   15878 N N   . ASN   K  1 160 ? 27.02481  20.68655  66.68628  1.000 50.13225  ?  160 ASN   K N   1 
ATOM   15879 C CA  . ASN   K  1 160 ? 26.76137  22.12282  66.72459  1.000 54.47770  ?  160 ASN   K CA  1 
ATOM   15880 C C   . ASN   K  1 160 ? 27.18935  22.86394  65.45959  1.000 46.90535  ?  160 ASN   K C   1 
ATOM   15881 O O   . ASN   K  1 160 ? 26.76366  24.00472  65.25931  1.000 76.67716  ?  160 ASN   K O   1 
ATOM   15882 C CB  . ASN   K  1 160 ? 27.44728  22.73844  67.93904  1.000 52.52724  ?  160 ASN   K CB  1 
ATOM   15883 C CG  . ASN   K  1 160 ? 28.93128  22.84091  67.76307  1.000 64.70173  ?  160 ASN   K CG  1 
ATOM   15884 O OD1 . ASN   K  1 160 ? 29.63415  21.82615  67.70794  1.000 78.15769  ?  160 ASN   K OD1 1 
ATOM   15885 N ND2 . ASN   K  1 160 ? 29.42682  24.06648  67.65942  1.000 68.89516  ?  160 ASN   K ND2 1 
ATOM   15886 N N   . VAL   K  1 161 ? 28.03017  22.26906  64.60985  1.000 68.89821  ?  161 VAL   K N   1 
ATOM   15887 C CA  . VAL   K  1 161 ? 28.33028  22.89381  63.31981  1.000 71.70321  ?  161 VAL   K CA  1 
ATOM   15888 C C   . VAL   K  1 161 ? 27.32805  22.50134  62.24795  1.000 74.40323  ?  161 VAL   K C   1 
ATOM   15889 O O   . VAL   K  1 161 ? 27.38475  23.03872  61.12888  1.000 57.10720  ?  161 VAL   K O   1 
ATOM   15890 C CB  . VAL   K  1 161 ? 29.74065  22.53535  62.80767  1.000 65.64961  ?  161 VAL   K CB  1 
ATOM   15891 C CG1 . VAL   K  1 161 ? 30.82571  23.08129  63.74455  1.000 54.51483  ?  161 VAL   K CG1 1 
ATOM   15892 C CG2 . VAL   K  1 161 ? 29.85506  21.03555  62.63338  1.000 49.40698  ?  161 VAL   K CG2 1 
ATOM   15893 N N   . LEU   K  1 162 ? 26.42858  21.56582  62.54506  1.000 56.31282  ?  162 LEU   K N   1 
ATOM   15894 C CA  . LEU   K  1 162 ? 25.42532  21.10738  61.58954  1.000 66.75866  ?  162 LEU   K CA  1 
ATOM   15895 C C   . LEU   K  1 162 ? 24.19955  22.01961  61.67899  1.000 85.68907  ?  162 LEU   K C   1 
ATOM   15896 O O   . LEU   K  1 162 ? 23.11530  21.65004  62.14218  1.000 68.28536  ?  162 LEU   K O   1 
ATOM   15897 C CB  . LEU   K  1 162 ? 25.07720  19.65215  61.85997  1.000 63.41549  ?  162 LEU   K CB  1 
ATOM   15898 C CG  . LEU   K  1 162 ? 26.27386  18.71517  61.76808  1.000 52.05494  ?  162 LEU   K CG  1 
ATOM   15899 C CD1 . LEU   K  1 162 ? 25.82229  17.26822  61.86164  1.000 47.74864  ?  162 LEU   K CD1 1 
ATOM   15900 C CD2 . LEU   K  1 162 ? 27.00526  18.98260  60.45078  1.000 46.59163  ?  162 LEU   K CD2 1 
ATOM   15901 N N   . VAL   K  1 163 ? 24.40883  23.25309  61.22386  1.000 65.42443  ?  163 VAL   K N   1 
ATOM   15902 C CA  . VAL   K  1 163 ? 23.45896  24.35204  61.36036  1.000 62.46953  ?  163 VAL   K CA  1 
ATOM   15903 C C   . VAL   K  1 163 ? 23.60929  25.24903  60.13712  1.000 82.89496  ?  163 VAL   K C   1 
ATOM   15904 O O   . VAL   K  1 163 ? 24.56155  25.12572  59.36154  1.000 75.47765  ?  163 VAL   K O   1 
ATOM   15905 C CB  . VAL   K  1 163 ? 23.69377  25.18018  62.64965  1.000 64.43013  ?  163 VAL   K CB  1 
ATOM   15906 C CG1 . VAL   K  1 163 ? 23.53552  24.31203  63.91719  1.000 58.01435  ?  163 VAL   K CG1 1 
ATOM   15907 C CG2 . VAL   K  1 163 ? 25.07088  25.85044  62.61245  1.000 57.54331  ?  163 VAL   K CG2 1 
ATOM   15908 N N   . ALA   K  1 164 ? 22.67238  26.18243  59.96814  1.000 72.46345  ?  164 ALA   K N   1 
ATOM   15909 C CA  . ALA   K  1 164 ? 22.78583  27.13046  58.86455  1.000 80.06943  ?  164 ALA   K CA  1 
ATOM   15910 C C   . ALA   K  1 164 ? 23.47542  28.42745  59.26036  1.000 71.06973  ?  164 ALA   K C   1 
ATOM   15911 O O   . ALA   K  1 164 ? 23.88098  29.18622  58.37056  1.000 68.98448  ?  164 ALA   K O   1 
ATOM   15912 C CB  . ALA   K  1 164 ? 21.40853  27.44688  58.28892  1.000 50.92595  ?  164 ALA   K CB  1 
ATOM   15913 N N   . ASP   K  1 165 ? 23.62480  28.67668  60.56931  1.000 67.32226  ?  165 ASP   K N   1 
ATOM   15914 C CA  . ASP   K  1 165 ? 24.23483  29.89189  61.10118  1.000 65.65671  ?  165 ASP   K CA  1 
ATOM   15915 C C   . ASP   K  1 165 ? 25.48888  30.27821  60.32529  1.000 65.51719  ?  165 ASP   K C   1 
ATOM   15916 O O   . ASP   K  1 165 ? 26.34883  29.44365  60.03965  1.000 100.53922 ?  165 ASP   K O   1 
ATOM   15917 C CB  . ASP   K  1 165 ? 24.59312  29.70238  62.58638  1.000 72.93271  ?  165 ASP   K CB  1 
ATOM   15918 C CG  . ASP   K  1 165 ? 23.45743  29.10272  63.40947  1.000 60.88568  ?  165 ASP   K CG  1 
ATOM   15919 O OD1 . ASP   K  1 165 ? 22.34853  28.88822  62.87027  1.000 107.13664 ?  165 ASP   K OD1 1 
ATOM   15920 O OD2 . ASP   K  1 165 ? 23.68885  28.84582  64.61312  1.000 109.83474 -1 165 ASP   K OD2 1 
ATOM   15921 N N   . GLN   K  1 166 ? 25.57544  31.54955  59.96818  1.000 86.08724  ?  166 GLN   K N   1 
ATOM   15922 C CA  . GLN   K  1 166 ? 26.82381  32.12775  59.50225  1.000 100.55558 ?  166 GLN   K CA  1 
ATOM   15923 C C   . GLN   K  1 166 ? 27.64152  32.48073  60.73956  1.000 62.81471  ?  166 GLN   K C   1 
ATOM   15924 O O   . GLN   K  1 166 ? 27.10716  33.06017  61.68820  1.000 136.41624 ?  166 GLN   K O   1 
ATOM   15925 C CB  . GLN   K  1 166 ? 26.54925  33.35182  58.62034  1.000 60.14115  ?  166 GLN   K CB  1 
ATOM   15926 C CG  . GLN   K  1 166 ? 27.76813  34.07044  58.10100  1.000 96.65712  ?  166 GLN   K CG  1 
ATOM   15927 C CD  . GLN   K  1 166 ? 28.17073  33.57019  56.73755  1.000 156.07645 ?  166 GLN   K CD  1 
ATOM   15928 O OE1 . GLN   K  1 166 ? 29.33700  33.67791  56.34145  1.000 110.84154 ?  166 GLN   K OE1 1 
ATOM   15929 N NE2 . GLN   K  1 166 ? 27.21078  33.01715  56.00556  1.000 97.24518  ?  166 GLN   K NE2 1 
ATOM   15930 N N   . PHE   K  1 167 ? 28.91466  32.08076  60.75526  1.000 80.30851  ?  167 PHE   K N   1 
ATOM   15931 C CA  . PHE   K  1 167 ? 29.75878  32.20568  61.94370  1.000 79.26643  ?  167 PHE   K CA  1 
ATOM   15932 C C   . PHE   K  1 167 ? 30.63999  33.44714  61.93893  1.000 80.77026  ?  167 PHE   K C   1 
ATOM   15933 O O   . PHE   K  1 167 ? 30.99734  33.94338  63.01126  1.000 76.74980  ?  167 PHE   K O   1 
ATOM   15934 C CB  . PHE   K  1 167 ? 30.67373  30.98179  62.08638  1.000 69.36806  ?  167 PHE   K CB  1 
ATOM   15935 C CG  . PHE   K  1 167 ? 29.94891  29.69937  62.37899  1.000 74.86411  ?  167 PHE   K CG  1 
ATOM   15936 C CD1 . PHE   K  1 167 ? 30.20115  28.55103  61.64975  1.000 63.07842  ?  167 PHE   K CD1 1 
ATOM   15937 C CD2 . PHE   K  1 167 ? 29.03685  29.63374  63.39428  1.000 54.18639  ?  167 PHE   K CD2 1 
ATOM   15938 C CE1 . PHE   K  1 167 ? 29.53434  27.36773  61.93161  1.000 133.80183 ?  167 PHE   K CE1 1 
ATOM   15939 C CE2 . PHE   K  1 167 ? 28.36990  28.45667  63.67964  1.000 122.62289 ?  167 PHE   K CE2 1 
ATOM   15940 C CZ  . PHE   K  1 167 ? 28.60898  27.33252  62.95606  1.000 41.90405  ?  167 PHE   K CZ  1 
ATOM   15941 N N   . ASP   K  1 168 ? 31.03504  33.92133  60.76416  1.000 108.54499 ?  168 ASP   K N   1 
ATOM   15942 C CA  . ASP   K  1 168 ? 31.80546  35.14482  60.59246  1.000 73.81857  ?  168 ASP   K CA  1 
ATOM   15943 C C   . ASP   K  1 168 ? 31.75213  35.50246  59.11213  1.000 125.12910 ?  168 ASP   K C   1 
ATOM   15944 O O   . ASP   K  1 168 ? 30.88743  34.96513  58.37144  1.000 98.65362  ?  168 ASP   K O   1 
ATOM   15945 C CB  . ASP   K  1 168 ? 33.23068  34.98540  61.17417  1.000 87.89813  ?  168 ASP   K CB  1 
ATOM   15946 C CG  . ASP   K  1 168 ? 34.13344  34.04622  60.35237  1.000 112.68545 ?  168 ASP   K CG  1 
ATOM   15947 O OD1 . ASP   K  1 168 ? 35.01492  33.37329  60.94871  1.000 98.51654  ?  168 ASP   K OD1 1 
ATOM   15948 O OD2 . ASP   K  1 168 ? 33.99172  34.00076  59.10983  1.000 110.44112 -1 168 ASP   K OD2 1 
ATOM   15949 N N   . ASP   K  1 169 ? 32.61737  36.39506  58.64448  1.000 89.08009  ?  169 ASP   K N   1 
ATOM   15950 C CA  . ASP   K  1 169 ? 32.51098  36.84650  57.25993  1.000 92.97185  ?  169 ASP   K CA  1 
ATOM   15951 C C   . ASP   K  1 169 ? 32.81117  35.71249  56.27751  1.000 109.81970 ?  169 ASP   K C   1 
ATOM   15952 O O   . ASP   K  1 169 ? 32.22196  35.66050  55.19099  1.000 97.64850  ?  169 ASP   K O   1 
ATOM   15953 C CB  . ASP   K  1 169 ? 33.43303  38.04900  57.01564  1.000 71.55482  ?  169 ASP   K CB  1 
ATOM   15954 N N   . ARG   K  1 170 ? 33.67803  34.76532  56.65541  1.000 155.48867 ?  170 ARG   K N   1 
ATOM   15955 C CA  . ARG   K  1 170 ? 34.15514  33.74712  55.72583  1.000 66.38878  ?  170 ARG   K CA  1 
ATOM   15956 C C   . ARG   K  1 170 ? 33.67521  32.32211  56.02670  1.000 84.67252  ?  170 ARG   K C   1 
ATOM   15957 O O   . ARG   K  1 170 ? 33.81437  31.45382  55.15745  1.000 75.68910  ?  170 ARG   K O   1 
ATOM   15958 C CB  . ARG   K  1 170 ? 35.69223  33.77284  55.67806  1.000 72.24180  ?  170 ARG   K CB  1 
ATOM   15959 N N   . HIS   K  1 171 ? 33.09400  32.05533  57.20592  1.000 83.59566  ?  171 HIS   K N   1 
ATOM   15960 C CA  . HIS   K  1 171 ? 32.74731  30.70108  57.63703  1.000 86.82598  ?  171 HIS   K CA  1 
ATOM   15961 C C   . HIS   K  1 171 ? 31.26269  30.58435  57.95772  1.000 53.37839  ?  171 HIS   K C   1 
ATOM   15962 O O   . HIS   K  1 171 ? 30.64224  31.52524  58.45646  1.000 124.65710 ?  171 HIS   K O   1 
ATOM   15963 C CB  . HIS   K  1 171 ? 33.53889  30.27194  58.89276  1.000 89.59523  ?  171 HIS   K CB  1 
ATOM   15964 C CG  . HIS   K  1 171 ? 35.02185  30.42864  58.76337  1.000 84.77884  ?  171 HIS   K CG  1 
ATOM   15965 N ND1 . HIS   K  1 171 ? 35.66914  30.43529  57.54602  1.000 90.44213  ?  171 HIS   K ND1 1 
ATOM   15966 C CD2 . HIS   K  1 171 ? 35.98318  30.60186  59.70047  1.000 85.00629  ?  171 HIS   K CD2 1 
ATOM   15967 C CE1 . HIS   K  1 171 ? 36.96481  30.60034  57.73777  1.000 65.19627  ?  171 HIS   K CE1 1 
ATOM   15968 N NE2 . HIS   K  1 171 ? 37.18236  30.70167  59.03657  1.000 140.45945 ?  171 HIS   K NE2 1 
ATOM   15969 N N   . CYS   K  1 172 ? 30.70873  29.39793  57.70674  1.000 85.65074  ?  172 CYS   K N   1 
ATOM   15970 C CA  . CYS   K  1 172 ? 29.31513  29.11663  58.02336  1.000 54.97677  ?  172 CYS   K CA  1 
ATOM   15971 C C   . CYS   K  1 172 ? 29.15254  27.64966  58.39722  1.000 56.03535  ?  172 CYS   K C   1 
ATOM   15972 O O   . CYS   K  1 172 ? 30.06021  26.83410  58.21587  1.000 78.96492  ?  172 CYS   K O   1 
ATOM   15973 C CB  . CYS   K  1 172 ? 28.39874  29.44391  56.84917  1.000 64.09229  ?  172 CYS   K CB  1 
ATOM   15974 S SG  . CYS   K  1 172 ? 28.74546  28.44167  55.40666  1.000 72.06648  ?  172 CYS   K SG  1 
ATOM   15975 N N   . GLY   K  1 173 ? 27.96326  27.32303  58.90509  1.000 61.29106  ?  173 GLY   K N   1 
ATOM   15976 C CA  . GLY   K  1 173 ? 27.62538  25.95238  59.22900  1.000 45.94319  ?  173 GLY   K CA  1 
ATOM   15977 C C   . GLY   K  1 173 ? 27.36342  25.11641  57.98589  1.000 60.51129  ?  173 GLY   K C   1 
ATOM   15978 O O   . GLY   K  1 173 ? 27.19432  25.62315  56.87394  1.000 60.56694  ?  173 GLY   K O   1 
ATOM   15979 N N   . TRP   K  1 174 ? 27.31722  23.79211  58.19409  1.000 50.71162  ?  174 TRP   K N   1 
ATOM   15980 C CA  . TRP   K  1 174 ? 27.24321  22.84713  57.08537  1.000 76.28931  ?  174 TRP   K CA  1 
ATOM   15981 C C   . TRP   K  1 174 ? 25.84329  22.73938  56.49427  1.000 84.87213  ?  174 TRP   K C   1 
ATOM   15982 O O   . TRP   K  1 174 ? 25.69945  22.22474  55.38296  1.000 69.05337  ?  174 TRP   K O   1 
ATOM   15983 C CB  . TRP   K  1 174 ? 27.74363  21.46743  57.53841  1.000 54.04367  ?  174 TRP   K CB  1 
ATOM   15984 C CG  . TRP   K  1 174 ? 29.21681  21.47610  57.78389  1.000 84.09380  ?  174 TRP   K CG  1 
ATOM   15985 C CD1 . TRP   K  1 174 ? 29.84561  21.56026  58.99283  1.000 62.04500  ?  174 TRP   K CD1 1 
ATOM   15986 C CD2 . TRP   K  1 174 ? 30.25285  21.44184  56.79123  1.000 70.75758  ?  174 TRP   K CD2 1 
ATOM   15987 N NE1 . TRP   K  1 174 ? 31.20738  21.56939  58.81659  1.000 64.52570  ?  174 TRP   K NE1 1 
ATOM   15988 C CE2 . TRP   K  1 174 ? 31.48632  21.49537  57.47637  1.000 56.58508  ?  174 TRP   K CE2 1 
ATOM   15989 C CE3 . TRP   K  1 174 ? 30.25664  21.35487  55.39180  1.000 58.80289  ?  174 TRP   K CE3 1 
ATOM   15990 C CZ2 . TRP   K  1 174 ? 32.71889  21.46783  56.80996  1.000 48.99645  ?  174 TRP   K CZ2 1 
ATOM   15991 C CZ3 . TRP   K  1 174 ? 31.47566  21.33942  54.73095  1.000 60.83820  ?  174 TRP   K CZ3 1 
ATOM   15992 C CH2 . TRP   K  1 174 ? 32.69390  21.39291  55.44467  1.000 51.99077  ?  174 TRP   K CH2 1 
ATOM   15993 N N   . LEU   K  1 175 ? 24.81826  23.22667  57.19298  1.000 69.85330  ?  175 LEU   K N   1 
ATOM   15994 C CA  . LEU   K  1 175 ? 23.45388  23.25120  56.67948  1.000 64.80686  ?  175 LEU   K CA  1 
ATOM   15995 C C   . LEU   K  1 175 ? 23.06100  24.61128  56.10377  1.000 74.50382  ?  175 LEU   K C   1 
ATOM   15996 O O   . LEU   K  1 175 ? 21.93119  24.77044  55.63334  1.000 83.35305  ?  175 LEU   K O   1 
ATOM   15997 C CB  . LEU   K  1 175 ? 22.48268  22.83494  57.78351  1.000 59.80369  ?  175 LEU   K CB  1 
ATOM   15998 C CG  . LEU   K  1 175 ? 22.81783  21.44460  58.33235  1.000 70.41518  ?  175 LEU   K CG  1 
ATOM   15999 C CD1 . LEU   K  1 175 ? 21.77782  20.93122  59.33271  1.000 60.96121  ?  175 LEU   K CD1 1 
ATOM   16000 C CD2 . LEU   K  1 175 ? 22.98512  20.47332  57.17146  1.000 57.90631  ?  175 LEU   K CD2 1 
ATOM   16001 N N   . ASN   K  1 176 ? 23.96544  25.59006  56.14883  1.000 52.97984  ?  176 ASN   K N   1 
ATOM   16002 C CA  . ASN   K  1 176 ? 23.81596  26.84143  55.41551  1.000 48.56958  ?  176 ASN   K CA  1 
ATOM   16003 C C   . ASN   K  1 176 ? 23.71895  26.56277  53.91721  1.000 64.97857  ?  176 ASN   K C   1 
ATOM   16004 O O   . ASN   K  1 176 ? 24.33941  25.62393  53.40791  1.000 78.86348  ?  176 ASN   K O   1 
ATOM   16005 C CB  . ASN   K  1 176 ? 25.02344  27.71614  55.72596  1.000 75.49232  ?  176 ASN   K CB  1 
ATOM   16006 C CG  . ASN   K  1 176 ? 24.90183  29.10086  55.18500  1.000 73.80350  ?  176 ASN   K CG  1 
ATOM   16007 O OD1 . ASN   K  1 176 ? 25.22572  29.36373  54.01978  1.000 59.99019  ?  176 ASN   K OD1 1 
ATOM   16008 N ND2 . ASN   K  1 176 ? 24.49309  30.02375  56.04783  1.000 61.33154  ?  176 ASN   K ND2 1 
ATOM   16009 N N   . GLU   K  1 177 ? 22.92804  27.37166  53.20134  1.000 81.08805  ?  177 GLU   K N   1 
ATOM   16010 C CA  . GLU   K  1 177 ? 22.67450  27.04194  51.80064  1.000 78.38686  ?  177 GLU   K CA  1 
ATOM   16011 C C   . GLU   K  1 177 ? 23.92840  27.20288  50.95115  1.000 72.15728  ?  177 GLU   K C   1 
ATOM   16012 O O   . GLU   K  1 177 ? 24.07931  26.51461  49.93841  1.000 81.40452  ?  177 GLU   K O   1 
ATOM   16013 C CB  . GLU   K  1 177 ? 21.52960  27.88419  51.23106  1.000 60.13905  ?  177 GLU   K CB  1 
ATOM   16014 N N   . ARG   K  1 178 ? 24.84658  28.08747  51.34254  1.000 54.01498  ?  178 ARG   K N   1 
ATOM   16015 C CA  . ARG   K  1 178 ? 26.12043  28.18578  50.63044  1.000 77.57757  ?  178 ARG   K CA  1 
ATOM   16016 C C   . ARG   K  1 178 ? 26.83246  26.83337  50.60804  1.000 73.75358  ?  178 ARG   K C   1 
ATOM   16017 O O   . ARG   K  1 178 ? 27.33353  26.39349  49.56408  1.000 72.21330  ?  178 ARG   K O   1 
ATOM   16018 C CB  . ARG   K  1 178 ? 27.00003  29.26148  51.28729  1.000 42.76148  ?  178 ARG   K CB  1 
ATOM   16019 C CG  . ARG   K  1 178 ? 28.12946  29.79969  50.43653  1.000 96.76458  ?  178 ARG   K CG  1 
ATOM   16020 C CD  . ARG   K  1 178 ? 28.98191  30.86712  51.15606  1.000 116.78084 ?  178 ARG   K CD  1 
ATOM   16021 N NE  . ARG   K  1 178 ? 30.19183  30.43173  51.88012  1.000 121.31752 ?  178 ARG   K NE  1 
ATOM   16022 C CZ  . ARG   K  1 178 ? 31.45769  30.59667  51.49094  1.000 170.59017 ?  178 ARG   K CZ  1 
ATOM   16023 N NH1 . ARG   K  1 178 ? 31.78270  30.59293  50.21558  1.000 159.76222 ?  178 ARG   K NH1 1 
ATOM   16024 N NH2 . ARG   K  1 178 ? 32.40246  30.78541  52.43369  1.000 129.78622 ?  178 ARG   K NH2 1 
ATOM   16025 N N   . ALA   K  1 179 ? 26.85169  26.14423  51.75519  1.000 81.69453  ?  179 ALA   K N   1 
ATOM   16026 C CA  . ALA   K  1 179 ? 27.54198  24.86718  51.86915  1.000 80.36029  ?  179 ALA   K CA  1 
ATOM   16027 C C   . ALA   K  1 179 ? 26.71313  23.74302  51.25924  1.000 69.17469  ?  179 ALA   K C   1 
ATOM   16028 O O   . ALA   K  1 179 ? 27.24243  22.87599  50.54978  1.000 76.82003  ?  179 ALA   K O   1 
ATOM   16029 C CB  . ALA   K  1 179 ? 27.84420  24.57979  53.34110  1.000 56.19955  ?  179 ALA   K CB  1 
ATOM   16030 N N   . LEU   K  1 180 ? 25.40952  23.73458  51.55856  1.000 82.79912  ?  180 LEU   K N   1 
ATOM   16031 C CA  . LEU   K  1 180 ? 24.48044  22.79648  50.93238  1.000 69.75444  ?  180 LEU   K CA  1 
ATOM   16032 C C   . LEU   K  1 180 ? 24.59073  22.83943  49.40902  1.000 86.13270  ?  180 LEU   K C   1 
ATOM   16033 O O   . LEU   K  1 180 ? 24.58876  21.79454  48.74268  1.000 86.25281  ?  180 LEU   K O   1 
ATOM   16034 C CB  . LEU   K  1 180 ? 23.05802  23.12501  51.38488  1.000 65.08897  ?  180 LEU   K CB  1 
ATOM   16035 C CG  . LEU   K  1 180 ? 22.38542  22.21100  52.40166  1.000 89.90582  ?  180 LEU   K CG  1 
ATOM   16036 C CD1 . LEU   K  1 180 ? 23.28724  21.90950  53.54781  1.000 87.53698  ?  180 LEU   K CD1 1 
ATOM   16037 C CD2 . LEU   K  1 180 ? 21.11615  22.84326  52.91276  1.000 77.58067  ?  180 LEU   K CD2 1 
ATOM   16038 N N   . SER   K  1 181 ? 24.70293  24.04340  48.84120  1.000 83.79171  ?  181 SER   K N   1 
ATOM   16039 C CA  . SER   K  1 181 ? 24.84757  24.16935  47.39539  1.000 87.70309  ?  181 SER   K CA  1 
ATOM   16040 C C   . SER   K  1 181 ? 26.16061  23.55249  46.91461  1.000 75.40184  ?  181 SER   K C   1 
ATOM   16041 O O   . SER   K  1 181 ? 26.17506  22.78068  45.94557  1.000 86.71491  ?  181 SER   K O   1 
ATOM   16042 C CB  . SER   K  1 181 ? 24.74468  25.64412  46.99484  1.000 70.08283  ?  181 SER   K CB  1 
ATOM   16043 O OG  . SER   K  1 181 ? 25.25230  25.86504  45.68683  1.000 138.30351 ?  181 SER   K OG  1 
ATOM   16044 N N   . ALA   K  1 182 ? 27.27551  23.88007  47.58588  1.000 83.28302  ?  182 ALA   K N   1 
ATOM   16045 C CA  . ALA   K  1 182 ? 28.58189  23.37044  47.16992  1.000 104.95186 ?  182 ALA   K CA  1 
ATOM   16046 C C   . ALA   K  1 182 ? 28.60372  21.84715  47.14223  1.000 84.46109  ?  182 ALA   K C   1 
ATOM   16047 O O   . ALA   K  1 182 ? 29.14156  21.24477  46.20346  1.000 72.28771  ?  182 ALA   K O   1 
ATOM   16048 C CB  . ALA   K  1 182 ? 29.67691  23.90972  48.09514  1.000 63.47671  ?  182 ALA   K CB  1 
ATOM   16049 N N   . MET   K  1 183 ? 27.98501  21.21053  48.14393  1.000 64.53001  ?  183 MET   K N   1 
ATOM   16050 C CA  . MET   K  1 183 ? 28.01344  19.76102  48.28994  1.000 80.65681  ?  183 MET   K CA  1 
ATOM   16051 C C   . MET   K  1 183 ? 27.18287  18.99870  47.25827  1.000 65.99705  ?  183 MET   K C   1 
ATOM   16052 O O   . MET   K  1 183 ? 27.36394  17.78025  47.13818  1.000 84.59187  ?  183 MET   K O   1 
ATOM   16053 C CB  . MET   K  1 183 ? 27.56551  19.39172  49.69782  1.000 65.31663  ?  183 MET   K CB  1 
ATOM   16054 C CG  . MET   K  1 183 ? 28.69938  19.53804  50.69826  1.000 67.41809  ?  183 MET   K CG  1 
ATOM   16055 S SD  . MET   K  1 183 ? 28.26532  19.02574  52.35727  1.000 76.62849  ?  183 MET   K SD  1 
ATOM   16056 C CE  . MET   K  1 183 ? 27.32437  20.39582  53.00697  1.000 72.88219  ?  183 MET   K CE  1 
ATOM   16057 N N   . VAL   K  1 184 ? 26.29402  19.65223  46.50918  1.000 93.46084  ?  184 VAL   K N   1 
ATOM   16058 C CA  . VAL   K  1 184 ? 25.54921  18.95776  45.46570  1.000 100.31902 ?  184 VAL   K CA  1 
ATOM   16059 C C   . VAL   K  1 184 ? 25.87195  19.49140  44.08127  1.000 81.86270  ?  184 VAL   K C   1 
ATOM   16060 O O   . VAL   K  1 184 ? 25.15795  19.19192  43.12835  1.000 92.78612  ?  184 VAL   K O   1 
ATOM   16061 C CB  . VAL   K  1 184 ? 24.03067  18.99310  45.71872  1.000 79.73156  ?  184 VAL   K CB  1 
ATOM   16062 C CG1 . VAL   K  1 184 ? 23.70442  18.26038  47.01128  1.000 85.24317  ?  184 VAL   K CG1 1 
ATOM   16063 C CG2 . VAL   K  1 184 ? 23.52180  20.42534  45.74061  1.000 80.84174  ?  184 VAL   K CG2 1 
ATOM   16064 N N   . LYS   K  1 185 ? 26.95694  20.25399  43.95746  1.000 86.67309  ?  185 LYS   K N   1 
ATOM   16065 C CA  . LYS   K  1 185 ? 27.39282  20.78986  42.67237  1.000 89.54869  ?  185 LYS   K CA  1 
ATOM   16066 C C   . LYS   K  1 185 ? 27.34400  19.75326  41.54399  1.000 65.27008  ?  185 LYS   K C   1 
ATOM   16067 O O   . LYS   K  1 185 ? 26.88750  20.05189  40.43181  1.000 123.69824 ?  185 LYS   K O   1 
ATOM   16068 C CB  . LYS   K  1 185 ? 28.80001  21.35523  42.85314  1.000 78.16809  ?  185 LYS   K CB  1 
ATOM   16069 C CG  . LYS   K  1 185 ? 29.48163  21.78385  41.59606  1.000 84.37223  ?  185 LYS   K CG  1 
ATOM   16070 C CD  . LYS   K  1 185 ? 30.73235  22.57451  41.94362  1.000 109.80893 ?  185 LYS   K CD  1 
ATOM   16071 C CE  . LYS   K  1 185 ? 31.18718  23.36983  40.74351  1.000 110.45338 ?  185 LYS   K CE  1 
ATOM   16072 N NZ  . LYS   K  1 185 ? 32.63042  23.16430  40.47819  1.000 124.17843 ?  185 LYS   K NZ  1 
ATOM   16073 N N   . HIS   K  1 186 ? 27.78896  18.52394  41.81189  1.000 87.44244  ?  186 HIS   K N   1 
ATOM   16074 C CA  . HIS   K  1 186 ? 27.89842  17.50176  40.77649  1.000 69.53165  ?  186 HIS   K CA  1 
ATOM   16075 C C   . HIS   K  1 186 ? 26.73635  16.51644  40.78331  1.000 88.77011  ?  186 HIS   K C   1 
ATOM   16076 O O   . HIS   K  1 186 ? 26.85819  15.41239  40.23987  1.000 74.92363  ?  186 HIS   K O   1 
ATOM   16077 C CB  . HIS   K  1 186 ? 29.22361  16.75323  40.90368  1.000 77.97777  ?  186 HIS   K CB  1 
ATOM   16078 C CG  . HIS   K  1 186 ? 30.41558  17.64080  40.79174  1.000 104.02135 ?  186 HIS   K CG  1 
ATOM   16079 N ND1 . HIS   K  1 186 ? 30.71933  18.33761  39.64099  1.000 90.99932  ?  186 HIS   K ND1 1 
ATOM   16080 C CD2 . HIS   K  1 186 ? 31.37940  17.95054  41.68820  1.000 63.65975  ?  186 HIS   K CD2 1 
ATOM   16081 C CE1 . HIS   K  1 186 ? 31.82581  19.03494  39.83478  1.000 78.77858  ?  186 HIS   K CE1 1 
ATOM   16082 N NE2 . HIS   K  1 186 ? 32.24682  18.81724  41.06783  1.000 94.83411  ?  186 HIS   K NE2 1 
ATOM   16083 N N   . TYR   K  1 187 ? 25.60740  16.88542  41.37375  1.000 85.35934  ?  187 TYR   K N   1 
ATOM   16084 C CA  . TYR   K  1 187 ? 24.47370  15.97566  41.42049  1.000 93.31872  ?  187 TYR   K CA  1 
ATOM   16085 C C   . TYR   K  1 187 ? 23.33387  16.45059  40.53888  1.000 129.20616 ?  187 TYR   K C   1 
ATOM   16086 O O   . TYR   K  1 187 ? 22.19501  15.99415  40.69343  1.000 86.75758  ?  187 TYR   K O   1 
ATOM   16087 C CB  . TYR   K  1 187 ? 24.02779  15.75407  42.86263  1.000 97.82955  ?  187 TYR   K CB  1 
ATOM   16088 C CG  . TYR   K  1 187 ? 25.05866  14.93195  43.58473  1.000 81.83686  ?  187 TYR   K CG  1 
ATOM   16089 C CD1 . TYR   K  1 187 ? 25.02197  13.54193  43.54212  1.000 90.26147  ?  187 TYR   K CD1 1 
ATOM   16090 C CD2 . TYR   K  1 187 ? 26.11713  15.54446  44.24496  1.000 96.56338  ?  187 TYR   K CD2 1 
ATOM   16091 C CE1 . TYR   K  1 187 ? 25.98480  12.77317  44.18319  1.000 86.17438  ?  187 TYR   K CE1 1 
ATOM   16092 C CE2 . TYR   K  1 187 ? 27.08645  14.80018  44.88248  1.000 68.72030  ?  187 TYR   K CE2 1 
ATOM   16093 C CZ  . TYR   K  1 187 ? 27.01069  13.41157  44.85343  1.000 96.10002  ?  187 TYR   K CZ  1 
ATOM   16094 O OH  . TYR   K  1 187 ? 27.96959  12.68061  45.49914  1.000 89.49231  ?  187 TYR   K OH  1 
ATOM   16095 N N   . ASN   K  1 188 ? 23.63010  17.35036  39.60315  1.000 96.75385  ?  188 ASN   K N   1 
ATOM   16096 C CA  . ASN   K  1 188 ? 22.76792  17.56999  38.45903  1.000 146.46274 ?  188 ASN   K CA  1 
ATOM   16097 C C   . ASN   K  1 188 ? 21.41256  18.13427  38.89257  1.000 95.72265  ?  188 ASN   K C   1 
ATOM   16098 O O   . ASN   K  1 188 ? 20.35425  17.60215  38.56108  1.000 129.20599 ?  188 ASN   K O   1 
ATOM   16099 C CB  . ASN   K  1 188 ? 22.62552  16.25578  37.69191  1.000 107.20414 ?  188 ASN   K CB  1 
ATOM   16100 C CG  . ASN   K  1 188 ? 21.94821  16.42293  36.36784  1.000 146.51084 ?  188 ASN   K CG  1 
ATOM   16101 O OD1 . ASN   K  1 188 ? 20.72682  16.36739  36.26954  1.000 174.36031 ?  188 ASN   K OD1 1 
ATOM   16102 N ND2 . ASN   K  1 188 ? 22.73738  16.62017  35.33346  1.000 159.35143 ?  188 ASN   K ND2 1 
ATOM   16103 N N   . GLY   K  1 189 ? 21.44912  19.20059  39.69021  1.000 92.94170  ?  189 GLY   K N   1 
ATOM   16104 C CA  . GLY   K  1 189 ? 20.23471  19.86355  40.11644  1.000 59.85848  ?  189 GLY   K CA  1 
ATOM   16105 C C   . GLY   K  1 189 ? 19.50808  19.26024  41.30773  1.000 64.02373  ?  189 GLY   K C   1 
ATOM   16106 O O   . GLY   K  1 189 ? 18.69093  19.95640  41.92610  1.000 96.92000  ?  189 GLY   K O   1 
ATOM   16107 N N   . ARG   K  1 190 ? 19.76247  17.99509  41.65667  1.000 98.45605  ?  190 ARG   K N   1 
ATOM   16108 C CA  . ARG   K  1 190 ? 19.18484  17.43566  42.87588  1.000 86.61759  ?  190 ARG   K CA  1 
ATOM   16109 C C   . ARG   K  1 190 ? 19.74318  18.12752  44.12862  1.000 93.73293  ?  190 ARG   K C   1 
ATOM   16110 O O   . ARG   K  1 190 ? 20.88550  18.60799  44.16558  1.000 104.41951 ?  190 ARG   K O   1 
ATOM   16111 C CB  . ARG   K  1 190 ? 19.43521  15.93076  42.95245  1.000 93.82740  ?  190 ARG   K CB  1 
ATOM   16112 C CG  . ARG   K  1 190 ? 19.05109  15.15901  41.70688  1.000 88.48356  ?  190 ARG   K CG  1 
ATOM   16113 C CD  . ARG   K  1 190 ? 17.84860  14.25511  41.96165  1.000 78.98956  ?  190 ARG   K CD  1 
ATOM   16114 N NE  . ARG   K  1 190 ? 18.13529  13.13994  42.85951  1.000 93.64618  ?  190 ARG   K NE  1 
ATOM   16115 C CZ  . ARG   K  1 190 ? 17.21664  12.52133  43.58838  1.000 110.62646 ?  190 ARG   K CZ  1 
ATOM   16116 N NH1 . ARG   K  1 190 ? 15.95344  12.91226  43.58139  1.000 106.88312 ?  190 ARG   K NH1 1 
ATOM   16117 N NH2 . ARG   K  1 190 ? 17.57415  11.49261  44.35126  1.000 96.28071  ?  190 ARG   K NH2 1 
ATOM   16118 N N   . ALA   K  1 191 ? 18.91578  18.17157  45.16261  1.000 95.14666  ?  191 ALA   K N   1 
ATOM   16119 C CA  . ALA   K  1 191 ? 19.22646  18.89103  46.38702  1.000 82.94195  ?  191 ALA   K CA  1 
ATOM   16120 C C   . ALA   K  1 191 ? 19.83324  17.95176  47.42425  1.000 145.97921 ?  191 ALA   K C   1 
ATOM   16121 O O   . ALA   K  1 191 ? 19.70913  16.72466  47.33479  1.000 84.19720  ?  191 ALA   K O   1 
ATOM   16122 C CB  . ALA   K  1 191 ? 17.96599  19.53894  46.96315  1.000 95.25851  ?  191 ALA   K CB  1 
ATOM   16123 N N   . PHE   K  1 192 ? 20.45391  18.55681  48.44439  1.000 77.09848  ?  192 PHE   K N   1 
ATOM   16124 C CA  . PHE   K  1 192 ? 21.21699  17.79678  49.43266  1.000 80.97122  ?  192 PHE   K CA  1 
ATOM   16125 C C   . PHE   K  1 192 ? 20.39418  16.66766  50.05370  1.000 104.81745 ?  192 PHE   K C   1 
ATOM   16126 O O   . PHE   K  1 192 ? 20.85914  15.52192  50.14380  1.000 94.40721  ?  192 PHE   K O   1 
ATOM   16127 C CB  . PHE   K  1 192 ? 21.75041  18.74856  50.50675  1.000 82.50954  ?  192 PHE   K CB  1 
ATOM   16128 C CG  . PHE   K  1 192 ? 22.64237  18.08665  51.52142  1.000 89.96975  ?  192 PHE   K CG  1 
ATOM   16129 C CD1 . PHE   K  1 192 ? 22.10305  17.36615  52.58062  1.000 99.11607  ?  192 PHE   K CD1 1 
ATOM   16130 C CD2 . PHE   K  1 192 ? 24.02212  18.18986  51.42175  1.000 98.06506  ?  192 PHE   K CD2 1 
ATOM   16131 C CE1 . PHE   K  1 192 ? 22.91580  16.75275  53.51714  1.000 79.70880  ?  192 PHE   K CE1 1 
ATOM   16132 C CE2 . PHE   K  1 192 ? 24.84739  17.57903  52.35984  1.000 104.16693 ?  192 PHE   K CE2 1 
ATOM   16133 C CZ  . PHE   K  1 192 ? 24.28804  16.86361  53.41115  1.000 87.61102  ?  192 PHE   K CZ  1 
ATOM   16134 N N   . ASP   K  1 193 ? 19.17083  16.97311  50.49467  1.000 108.38057 ?  193 ASP   K N   1 
ATOM   16135 C CA  . ASP   K  1 193 ? 18.33180  15.98536  51.17151  1.000 88.47773  ?  193 ASP   K CA  1 
ATOM   16136 C C   . ASP   K  1 193 ? 17.71466  14.96200  50.21528  1.000 114.97114 ?  193 ASP   K C   1 
ATOM   16137 O O   . ASP   K  1 193 ? 17.23362  13.91475  50.66774  1.000 75.85783  ?  193 ASP   K O   1 
ATOM   16138 C CB  . ASP   K  1 193 ? 17.23824  16.70184  51.96876  1.000 101.36821 ?  193 ASP   K CB  1 
ATOM   16139 C CG  . ASP   K  1 193 ? 16.32898  17.53101  51.08489  1.000 144.24949 ?  193 ASP   K CG  1 
ATOM   16140 O OD1 . ASP   K  1 193 ? 16.79581  18.54917  50.53096  1.000 104.96607 ?  193 ASP   K OD1 1 
ATOM   16141 O OD2 . ASP   K  1 193 ? 15.15528  17.13608  50.91689  1.000 103.46406 -1 193 ASP   K OD2 1 
ATOM   16142 N N   . GLU   K  1 194 ? 17.71355  15.23099  48.90997  1.000 84.75372  ?  194 GLU   K N   1 
ATOM   16143 C CA  . GLU   K  1 194 ? 17.39816  14.19092  47.93500  1.000 111.72490 ?  194 GLU   K CA  1 
ATOM   16144 C C   . GLU   K  1 194 ? 18.57302  13.23649  47.75621  1.000 116.10185 ?  194 GLU   K C   1 
ATOM   16145 O O   . GLU   K  1 194 ? 18.39550  12.01156  47.78642  1.000 104.59550 ?  194 GLU   K O   1 
ATOM   16146 C CB  . GLU   K  1 194 ? 17.03596  14.81865  46.59121  1.000 103.48770 ?  194 GLU   K CB  1 
ATOM   16147 C CG  . GLU   K  1 194 ? 15.85655  15.78759  46.63365  1.000 89.26446  ?  194 GLU   K CG  1 
ATOM   16148 C CD  . GLU   K  1 194 ? 15.58429  16.41516  45.26955  1.000 146.83854 ?  194 GLU   K CD  1 
ATOM   16149 O OE1 . GLU   K  1 194 ? 16.38239  17.28517  44.85805  1.000 121.44945 ?  194 GLU   K OE1 1 
ATOM   16150 O OE2 . GLU   K  1 194 ? 14.59646  16.02573  44.59888  1.000 119.00196 -1 194 GLU   K OE2 1 
ATOM   16151 N N   . VAL   K  1 195 ? 19.78181  13.79762  47.58968  1.000 101.09446 ?  195 VAL   K N   1 
ATOM   16152 C CA  . VAL   K  1 195 ? 20.97988  13.01278  47.28735  1.000 68.89439  ?  195 VAL   K CA  1 
ATOM   16153 C C   . VAL   K  1 195 ? 21.40302  12.16333  48.48656  1.000 130.32039 ?  195 VAL   K C   1 
ATOM   16154 O O   . VAL   K  1 195 ? 21.64351  10.95590  48.36367  1.000 82.10989  ?  195 VAL   K O   1 
ATOM   16155 C CB  . VAL   K  1 195 ? 22.11835  13.94562  46.84441  1.000 104.12970 ?  195 VAL   K CB  1 
ATOM   16156 C CG1 . VAL   K  1 195 ? 23.40279  13.15298  46.63526  1.000 73.80086  ?  195 VAL   K CG1 1 
ATOM   16157 C CG2 . VAL   K  1 195 ? 21.72468  14.71420  45.58734  1.000 78.79778  ?  195 VAL   K CG2 1 
ATOM   16158 N N   . PHE   K  1 196 ? 21.52741  12.77699  49.65479  1.000 76.48462  ?  196 PHE   K N   1 
ATOM   16159 C CA  . PHE   K  1 196 ? 22.04572  12.08464  50.82038  1.000 108.40488 ?  196 PHE   K CA  1 
ATOM   16160 C C   . PHE   K  1 196 ? 20.91164  11.73778  51.77745  1.000 88.89945  ?  196 PHE   K C   1 
ATOM   16161 O O   . PHE   K  1 196 ? 19.89998  12.43723  51.84651  1.000 91.16034  ?  196 PHE   K O   1 
ATOM   16162 C CB  . PHE   K  1 196 ? 23.10247  12.94179  51.52285  1.000 81.14676  ?  196 PHE   K CB  1 
ATOM   16163 C CG  . PHE   K  1 196 ? 24.21656  13.36415  50.62380  1.000 98.60286  ?  196 PHE   K CG  1 
ATOM   16164 C CD1 . PHE   K  1 196 ? 25.09610  12.42586  50.10379  1.000 82.30742  ?  196 PHE   K CD1 1 
ATOM   16165 C CD2 . PHE   K  1 196 ? 24.37646  14.69336  50.27441  1.000 75.72075  ?  196 PHE   K CD2 1 
ATOM   16166 C CE1 . PHE   K  1 196 ? 26.12694  12.81573  49.24953  1.000 86.32310  ?  196 PHE   K CE1 1 
ATOM   16167 C CE2 . PHE   K  1 196 ? 25.41085  15.09314  49.42762  1.000 93.90578  ?  196 PHE   K CE2 1 
ATOM   16168 C CZ  . PHE   K  1 196 ? 26.28917  14.15463  48.91713  1.000 85.29416  ?  196 PHE   K CZ  1 
ATOM   16169 N N   . LEU   K  1 197 ? 21.09454  10.64282  52.51335  1.000 76.00908  ?  197 LEU   K N   1 
ATOM   16170 C CA  . LEU   K  1 197 ? 20.10809  10.14565  53.47097  1.000 78.83553  ?  197 LEU   K CA  1 
ATOM   16171 C C   . LEU   K  1 197 ? 20.15204  11.00462  54.72728  1.000 97.42937  ?  197 LEU   K C   1 
ATOM   16172 O O   . LEU   K  1 197 ? 21.09476  10.91634  55.51925  1.000 72.82838  ?  197 LEU   K O   1 
ATOM   16173 C CB  . LEU   K  1 197 ? 20.40591  8.69008   53.80838  1.000 76.36854  ?  197 LEU   K CB  1 
ATOM   16174 C CG  . LEU   K  1 197 ? 19.39189  7.77718   54.48268  1.000 73.06462  ?  197 LEU   K CG  1 
ATOM   16175 C CD1 . LEU   K  1 197 ? 20.00314  6.41202   54.42642  1.000 81.30950  ?  197 LEU   K CD1 1 
ATOM   16176 C CD2 . LEU   K  1 197 ? 19.14460  8.13438   55.92726  1.000 120.26529 ?  197 LEU   K CD2 1 
ATOM   16177 N N   . CYS   K  1 198 ? 19.12393  11.81237  54.93414  1.000 84.33763  ?  198 CYS   K N   1 
ATOM   16178 C CA  . CYS   K  1 198 ? 19.05275  12.64646  56.11571  1.000 83.51166  ?  198 CYS   K CA  1 
ATOM   16179 C C   . CYS   K  1 198 ? 17.58630  12.95958  56.36631  1.000 87.14245  ?  198 CYS   K C   1 
ATOM   16180 O O   . CYS   K  1 198 ? 16.69399  12.37397  55.74344  1.000 94.23934  ?  198 CYS   K O   1 
ATOM   16181 C CB  . CYS   K  1 198 ? 19.88972  13.91498  55.92323  1.000 76.96583  ?  198 CYS   K CB  1 
ATOM   16182 S SG  . CYS   K  1 198 ? 19.42216  14.83594  54.41057  1.000 85.70204  ?  198 CYS   K SG  1 
ATOM   16183 N N   . ASP   K  1 199 ? 17.34373  13.90502  57.27049  1.000 87.21603  ?  199 ASP   K N   1 
ATOM   16184 C CA  . ASP   K  1 199 ? 16.00866  14.41257  57.57128  1.000 75.69024  ?  199 ASP   K CA  1 
ATOM   16185 C C   . ASP   K  1 199 ? 16.07512  15.93804  57.55068  1.000 110.30647 ?  199 ASP   K C   1 
ATOM   16186 O O   . ASP   K  1 199 ? 16.56413  16.54912  58.50866  1.000 75.44565  ?  199 ASP   K O   1 
ATOM   16187 C CB  . ASP   K  1 199 ? 15.53701  13.88859  58.92851  1.000 77.49507  ?  199 ASP   K CB  1 
ATOM   16188 C CG  . ASP   K  1 199 ? 14.13680  14.36310  59.30309  1.000 178.84385 ?  199 ASP   K CG  1 
ATOM   16189 O OD1 . ASP   K  1 199 ? 13.55248  15.23061  58.59867  1.000 80.33122  ?  199 ASP   K OD1 1 
ATOM   16190 O OD2 . ASP   K  1 199 ? 13.63206  13.83983  60.32407  1.000 88.03125  -1 199 ASP   K OD2 1 
ATOM   16191 N N   . LYS   K  1 200 ? 15.58234  16.56141  56.46834  1.000 63.60780  ?  200 LYS   K N   1 
ATOM   16192 C CA  . LYS   K  1 200 ? 15.71416  18.01430  56.34215  1.000 89.06858  ?  200 LYS   K CA  1 
ATOM   16193 C C   . LYS   K  1 200 ? 14.89216  18.77077  57.37630  1.000 85.81286  ?  200 LYS   K C   1 
ATOM   16194 O O   . LYS   K  1 200 ? 15.12773  19.96668  57.56592  1.000 77.52964  ?  200 LYS   K O   1 
ATOM   16195 C CB  . LYS   K  1 200 ? 15.32656  18.48694  54.93402  1.000 63.42311  ?  200 LYS   K CB  1 
ATOM   16196 C CG  . LYS   K  1 200 ? 13.83651  18.51223  54.65571  1.000 86.21263  ?  200 LYS   K CG  1 
ATOM   16197 C CD  . LYS   K  1 200 ? 13.52790  18.94078  53.21693  1.000 106.72258 ?  200 LYS   K CD  1 
ATOM   16198 C CE  . LYS   K  1 200 ? 13.88136  20.40532  52.94029  1.000 90.00094  ?  200 LYS   K CE  1 
ATOM   16199 N NZ  . LYS   K  1 200 ? 13.21100  20.90392  51.69046  1.000 84.58073  ?  200 LYS   K NZ  1 
ATOM   16200 N N   . ASN   K  1 201 ? 13.96245  18.10493  58.06008  1.000 77.08560  ?  201 ASN   K N   1 
ATOM   16201 C CA  . ASN   K  1 201 ? 13.12248  18.72881  59.07093  1.000 100.24730 ?  201 ASN   K CA  1 
ATOM   16202 C C   . ASN   K  1 201 ? 13.62398  18.49747  60.48150  1.000 75.99226  ?  201 ASN   K C   1 
ATOM   16203 O O   . ASN   K  1 201 ? 13.07828  19.07612  61.42466  1.000 108.03291 ?  201 ASN   K O   1 
ATOM   16204 C CB  . ASN   K  1 201 ? 11.69697  18.20775  58.94091  1.000 74.24516  ?  201 ASN   K CB  1 
ATOM   16205 C CG  . ASN   K  1 201 ? 11.12692  18.48884  57.58674  1.000 111.70892 ?  201 ASN   K CG  1 
ATOM   16206 O OD1 . ASN   K  1 201 ? 11.30502  19.59263  57.04379  1.000 64.94150  ?  201 ASN   K OD1 1 
ATOM   16207 N ND2 . ASN   K  1 201 ? 10.47841  17.48905  57.00000  1.000 79.82342  ?  201 ASN   K ND2 1 
ATOM   16208 N N   . ALA   K  1 202 ? 14.58795  17.71471  60.63904  1.000 126.67741 ?  202 ALA   K N   1 
ATOM   16209 C CA  . ALA   K  1 202 ? 15.11292  17.44787  61.96213  1.000 79.17308  ?  202 ALA   K CA  1 
ATOM   16210 C C   . ALA   K  1 202 ? 16.22907  18.43005  62.29368  1.000 72.40395  ?  202 ALA   K C   1 
ATOM   16211 O O   . ALA   K  1 202 ? 16.84495  19.01383  61.39177  1.000 84.15809  ?  202 ALA   K O   1 
ATOM   16212 C CB  . ALA   K  1 202 ? 15.63630  16.02155  62.04398  1.000 56.54142  ?  202 ALA   K CB  1 
ATOM   16213 N N   . PRO   K  1 203 ? 16.47599  18.67430  63.57715  1.000 103.60654 ?  203 PRO   K N   1 
ATOM   16214 C CA  . PRO   K  1 203 ? 17.67902  19.42715  63.94899  1.000 98.42679  ?  203 PRO   K CA  1 
ATOM   16215 C C   . PRO   K  1 203 ? 18.92182  18.64887  63.54347  1.000 88.25182  ?  203 PRO   K C   1 
ATOM   16216 O O   . PRO   K  1 203 ? 18.97847  17.41572  63.66338  1.000 68.50864  ?  203 PRO   K O   1 
ATOM   16217 C CB  . PRO   K  1 203 ? 17.56536  19.58049  65.47313  1.000 75.70969  ?  203 PRO   K CB  1 
ATOM   16218 C CG  . PRO   K  1 203 ? 16.56582  18.53867  65.91050  1.000 66.41819  ?  203 PRO   K CG  1 
ATOM   16219 C CD  . PRO   K  1 203 ? 15.64529  18.30931  64.73859  1.000 54.55151  ?  203 PRO   K CD  1 
ATOM   16220 N N   . TYR   K  1 204 ? 19.90746  19.38649  63.02232  1.000 72.10697  ?  204 TYR   K N   1 
ATOM   16221 C CA  . TYR   K  1 204 ? 21.15321  18.82552  62.50909  1.000 83.17659  ?  204 TYR   K CA  1 
ATOM   16222 C C   . TYR   K  1 204 ? 20.92133  17.89957  61.33147  1.000 76.88546  ?  204 TYR   K C   1 
ATOM   16223 O O   . TYR   K  1 204 ? 21.70213  16.97001  61.11584  1.000 81.23878  ?  204 TYR   K O   1 
ATOM   16224 C CB  . TYR   K  1 204 ? 21.91832  18.07908  63.60868  1.000 70.58290  ?  204 TYR   K CB  1 
ATOM   16225 C CG  . TYR   K  1 204 ? 21.92019  18.83320  64.91459  1.000 74.85848  ?  204 TYR   K CG  1 
ATOM   16226 C CD1 . TYR   K  1 204 ? 22.45162  20.12374  64.98346  1.000 69.61991  ?  204 TYR   K CD1 1 
ATOM   16227 C CD2 . TYR   K  1 204 ? 21.38566  18.26951  66.07513  1.000 65.80735  ?  204 TYR   K CD2 1 
ATOM   16228 C CE1 . TYR   K  1 204 ? 22.45315  20.84217  66.16941  1.000 52.33529  ?  204 TYR   K CE1 1 
ATOM   16229 C CE2 . TYR   K  1 204 ? 21.38508  18.97438  67.27136  1.000 62.85022  ?  204 TYR   K CE2 1 
ATOM   16230 C CZ  . TYR   K  1 204 ? 21.91356  20.26517  67.30479  1.000 76.06348  ?  204 TYR   K CZ  1 
ATOM   16231 O OH  . TYR   K  1 204 ? 21.93179  20.98730  68.47377  1.000 78.07341  ?  204 TYR   K OH  1 
ATOM   16232 N N   . TYR   K  1 205 ? 19.83377  18.10934  60.59195  1.000 63.38773  ?  205 TYR   K N   1 
ATOM   16233 C CA  . TYR   K  1 205 ? 19.43912  17.23776  59.48972  1.000 61.34773  ?  205 TYR   K CA  1 
ATOM   16234 C C   . TYR   K  1 205 ? 19.40286  15.75891  59.89614  1.000 68.77076  ?  205 TYR   K C   1 
ATOM   16235 O O   . TYR   K  1 205 ? 19.50434  14.86443  59.04336  1.000 66.75426  ?  205 TYR   K O   1 
ATOM   16236 C CB  . TYR   K  1 205 ? 20.35556  17.42914  58.28212  1.000 68.46618  ?  205 TYR   K CB  1 
ATOM   16237 C CG  . TYR   K  1 205 ? 19.83454  18.36676  57.22956  1.000 82.17294  ?  205 TYR   K CG  1 
ATOM   16238 C CD1 . TYR   K  1 205 ? 19.06410  19.47145  57.55871  1.000 74.42395  ?  205 TYR   K CD1 1 
ATOM   16239 C CD2 . TYR   K  1 205 ? 20.10808  18.13537  55.88665  1.000 69.67651  ?  205 TYR   K CD2 1 
ATOM   16240 C CE1 . TYR   K  1 205 ? 18.58955  20.33935  56.55677  1.000 59.30160  ?  205 TYR   K CE1 1 
ATOM   16241 C CE2 . TYR   K  1 205 ? 19.64307  18.98551  54.89204  1.000 83.30201  ?  205 TYR   K CE2 1 
ATOM   16242 C CZ  . TYR   K  1 205 ? 18.88674  20.08214  55.23068  1.000 103.19584 ?  205 TYR   K CZ  1 
ATOM   16243 O OH  . TYR   K  1 205 ? 18.44140  20.90445  54.22930  1.000 73.78362  ?  205 TYR   K OH  1 
ATOM   16244 N N   . GLY   K  1 206 ? 19.26629  15.47207  61.18782  1.000 59.89583  ?  206 GLY   K N   1 
ATOM   16245 C CA  . GLY   K  1 206 ? 19.16790  14.10726  61.64768  1.000 58.78325  ?  206 GLY   K CA  1 
ATOM   16246 C C   . GLY   K  1 206 ? 20.48517  13.41259  61.91857  1.000 72.57217  ?  206 GLY   K C   1 
ATOM   16247 O O   . GLY   K  1 206 ? 20.47633  12.30115  62.45991  1.000 64.58825  ?  206 GLY   K O   1 
ATOM   16248 N N   . PHE   K  1 207 ? 21.61437  14.01806  61.56473  1.000 57.43357  ?  207 PHE   K N   1 
ATOM   16249 C CA  . PHE   K  1 207 ? 22.90278  13.40254  61.85117  1.000 69.49287  ?  207 PHE   K CA  1 
ATOM   16250 C C   . PHE   K  1 207 ? 23.19807  13.47982  63.34439  1.000 64.95688  ?  207 PHE   K C   1 
ATOM   16251 O O   . PHE   K  1 207 ? 22.88449  14.47788  63.99857  1.000 74.99859  ?  207 PHE   K O   1 
ATOM   16252 C CB  . PHE   K  1 207 ? 24.00381  14.09910  61.05533  1.000 56.82860  ?  207 PHE   K CB  1 
ATOM   16253 C CG  . PHE   K  1 207 ? 23.81989  14.02905  59.56666  1.000 72.47666  ?  207 PHE   K CG  1 
ATOM   16254 C CD1 . PHE   K  1 207 ? 24.07433  12.84865  58.88220  1.000 46.25432  ?  207 PHE   K CD1 1 
ATOM   16255 C CD2 . PHE   K  1 207 ? 23.41631  15.14919  58.84354  1.000 50.63071  ?  207 PHE   K CD2 1 
ATOM   16256 C CE1 . PHE   K  1 207 ? 23.92262  12.78329  57.50422  1.000 66.56100  ?  207 PHE   K CE1 1 
ATOM   16257 C CE2 . PHE   K  1 207 ? 23.26440  15.09258  57.45767  1.000 54.28630  ?  207 PHE   K CE2 1 
ATOM   16258 C CZ  . PHE   K  1 207 ? 23.51693  13.90835  56.79127  1.000 71.24321  ?  207 PHE   K CZ  1 
ATOM   16259 N N   . ASN   K  1 208 ? 23.80143  12.42099  63.89272  1.000 55.62273  ?  208 ASN   K N   1 
ATOM   16260 C CA  . ASN   K  1 208 ? 24.06000  12.36731  65.32979  1.000 78.13609  ?  208 ASN   K CA  1 
ATOM   16261 C C   . ASN   K  1 208 ? 25.45927  12.82012  65.73072  1.000 47.76058  ?  208 ASN   K C   1 
ATOM   16262 O O   . ASN   K  1 208 ? 25.78826  12.77287  66.92478  1.000 105.93499 ?  208 ASN   K O   1 
ATOM   16263 C CB  . ASN   K  1 208 ? 23.80078  10.95851  65.88514  1.000 48.21059  ?  208 ASN   K CB  1 
ATOM   16264 C CG  . ASN   K  1 208 ? 24.33858  9.86966   65.01026  1.000 104.67979 ?  208 ASN   K CG  1 
ATOM   16265 O OD1 . ASN   K  1 208 ? 25.55140  9.77033   64.77988  1.000 159.72896 ?  208 ASN   K OD1 1 
ATOM   16266 N ND2 . ASN   K  1 208 ? 23.44024  9.01064   64.53844  1.000 81.65532  ?  208 ASN   K ND2 1 
ATOM   16267 N N   . SER   K  1 209 ? 26.27209  13.28125  64.78239  1.000 78.02926  ?  209 SER   K N   1 
ATOM   16268 C CA  . SER   K  1 209 ? 27.62104  13.77661  65.04646  1.000 61.49330  ?  209 SER   K CA  1 
ATOM   16269 C C   . SER   K  1 209 ? 28.15757  14.33850  63.74787  1.000 83.64067  ?  209 SER   K C   1 
ATOM   16270 O O   . SER   K  1 209 ? 27.57198  14.14298  62.67791  1.000 58.87359  ?  209 SER   K O   1 
ATOM   16271 C CB  . SER   K  1 209 ? 28.57964  12.69163  65.53822  1.000 72.48586  ?  209 SER   K CB  1 
ATOM   16272 O OG  . SER   K  1 209 ? 28.85552  11.78946  64.47956  1.000 51.80975  ?  209 SER   K OG  1 
ATOM   16273 N N   . TYR   K  1 210 ? 29.30843  15.00611  63.84795  1.000 60.07265  ?  210 TYR   K N   1 
ATOM   16274 C CA  . TYR   K  1 210 ? 29.92885  15.52458  62.63783  1.000 48.18597  ?  210 TYR   K CA  1 
ATOM   16275 C C   . TYR   K  1 210 ? 30.38773  14.38754  61.73144  1.000 61.19430  ?  210 TYR   K C   1 
ATOM   16276 O O   . TYR   K  1 210 ? 30.14808  14.41534  60.51766  1.000 54.14059  ?  210 TYR   K O   1 
ATOM   16277 C CB  . TYR   K  1 210 ? 31.09322  16.44823  62.99268  1.000 37.59067  ?  210 TYR   K CB  1 
ATOM   16278 C CG  . TYR   K  1 210 ? 31.86055  16.87635  61.77510  1.000 70.66395  ?  210 TYR   K CG  1 
ATOM   16279 C CD1 . TYR   K  1 210 ? 31.36619  17.87251  60.94378  1.000 47.68653  ?  210 TYR   K CD1 1 
ATOM   16280 C CD2 . TYR   K  1 210 ? 33.05706  16.26134  61.43002  1.000 63.10009  ?  210 TYR   K CD2 1 
ATOM   16281 C CE1 . TYR   K  1 210 ? 32.04279  18.26319  59.79861  1.000 51.30932  ?  210 TYR   K CE1 1 
ATOM   16282 C CE2 . TYR   K  1 210 ? 33.74538  16.64263  60.28980  1.000 64.86975  ?  210 TYR   K CE2 1 
ATOM   16283 C CZ  . TYR   K  1 210 ? 33.23056  17.64571  59.48324  1.000 73.86494  ?  210 TYR   K CZ  1 
ATOM   16284 O OH  . TYR   K  1 210 ? 33.90302  18.03521  58.36224  1.000 55.64110  ?  210 TYR   K OH  1 
ATOM   16285 N N   . ASP   K  1 211 ? 31.03203  13.37285  62.31112  1.000 59.09295  ?  211 ASP   K N   1 
ATOM   16286 C CA  . ASP   K  1 211 ? 31.48521  12.22716  61.53010  1.000 53.81671  ?  211 ASP   K CA  1 
ATOM   16287 C C   . ASP   K  1 211 ? 30.33008  11.56651  60.79667  1.000 75.20542  ?  211 ASP   K C   1 
ATOM   16288 O O   . ASP   K  1 211 ? 30.48868  11.10839  59.65348  1.000 56.08771  ?  211 ASP   K O   1 
ATOM   16289 C CB  . ASP   K  1 211 ? 32.18074  11.20492  62.43362  1.000 56.95633  ?  211 ASP   K CB  1 
ATOM   16290 C CG  . ASP   K  1 211 ? 32.69627  10.00726  61.65415  1.000 57.49963  ?  211 ASP   K CG  1 
ATOM   16291 O OD1 . ASP   K  1 211 ? 33.63280  10.18939  60.83351  1.000 62.25097  ?  211 ASP   K OD1 1 
ATOM   16292 O OD2 . ASP   K  1 211 ? 32.16203  8.89046   61.85105  1.000 80.16615  -1 211 ASP   K OD2 1 
ATOM   16293 N N   . ASP   K  1 212 ? 29.16698  11.48456  61.45322  1.000 64.21997  ?  212 ASP   K N   1 
ATOM   16294 C CA  . ASP   K  1 212 ? 27.97489  10.95601  60.79591  1.000 73.73784  ?  212 ASP   K CA  1 
ATOM   16295 C C   . ASP   K  1 212 ? 27.63838  11.76617  59.54294  1.000 66.00161  ?  212 ASP   K C   1 
ATOM   16296 O O   . ASP   K  1 212 ? 27.33406  11.20197  58.48176  1.000 66.68856  ?  212 ASP   K O   1 
ATOM   16297 C CB  . ASP   K  1 212 ? 26.81208  10.95448  61.79211  1.000 75.21642  ?  212 ASP   K CB  1 
ATOM   16298 C CG  . ASP   K  1 212 ? 25.58438  10.21866  61.27801  1.000 83.33701  ?  212 ASP   K CG  1 
ATOM   16299 O OD1 . ASP   K  1 212 ? 25.73975  9.32619   60.41616  1.000 98.33727  ?  212 ASP   K OD1 1 
ATOM   16300 O OD2 . ASP   K  1 212 ? 24.46206  10.55646  61.73116  1.000 84.20968  -1 212 ASP   K OD2 1 
ATOM   16301 N N   . PHE   K  1 213 ? 27.71899  13.09167  59.64041  1.000 49.84164  ?  213 PHE   K N   1 
ATOM   16302 C CA  . PHE   K  1 213 ? 27.46416  13.94183  58.48302  1.000 47.11186  ?  213 PHE   K CA  1 
ATOM   16303 C C   . PHE   K  1 213 ? 28.55348  13.77983  57.42779  1.000 84.02081  ?  213 PHE   K C   1 
ATOM   16304 O O   . PHE   K  1 213 ? 28.26164  13.69809  56.22147  1.000 58.51800  ?  213 PHE   K O   1 
ATOM   16305 C CB  . PHE   K  1 213 ? 27.36261  15.40109  58.93880  1.000 53.79009  ?  213 PHE   K CB  1 
ATOM   16306 C CG  . PHE   K  1 213 ? 27.53821  16.37591  57.84069  1.000 66.48965  ?  213 PHE   K CG  1 
ATOM   16307 C CD1 . PHE   K  1 213 ? 26.47377  16.68642  56.99654  1.000 69.97146  ?  213 PHE   K CD1 1 
ATOM   16308 C CD2 . PHE   K  1 213 ? 28.76825  16.98062  57.63183  1.000 54.69542  ?  213 PHE   K CD2 1 
ATOM   16309 C CE1 . PHE   K  1 213 ? 26.63427  17.59703  55.96010  1.000 79.44662  ?  213 PHE   K CE1 1 
ATOM   16310 C CE2 . PHE   K  1 213 ? 28.93571  17.89049  56.60194  1.000 82.38776  ?  213 PHE   K CE2 1 
ATOM   16311 C CZ  . PHE   K  1 213 ? 27.86668  18.19846  55.76260  1.000 71.84056  ?  213 PHE   K CZ  1 
ATOM   16312 N N   . PHE   K  1 214 ? 29.81487  13.75563  57.87590  1.000 48.27041  ?  214 PHE   K N   1 
ATOM   16313 C CA  . PHE   K  1 214 ? 30.95826  13.60279  56.98245  1.000 46.56316  ?  214 PHE   K CA  1 
ATOM   16314 C C   . PHE   K  1 214 ? 30.85500  12.31958  56.15537  1.000 45.36882  ?  214 PHE   K C   1 
ATOM   16315 O O   . PHE   K  1 214 ? 31.19555  12.30651  54.96198  1.000 72.99176  ?  214 PHE   K O   1 
ATOM   16316 C CB  . PHE   K  1 214 ? 32.23683  13.62611  57.82474  1.000 55.29733  ?  214 PHE   K CB  1 
ATOM   16317 C CG  . PHE   K  1 214 ? 33.50746  13.57309  57.02700  1.000 53.50804  ?  214 PHE   K CG  1 
ATOM   16318 C CD1 . PHE   K  1 214 ? 33.98992  14.70684  56.39415  1.000 52.04674  ?  214 PHE   K CD1 1 
ATOM   16319 C CD2 . PHE   K  1 214 ? 34.23971  12.39684  56.93662  1.000 60.94103  ?  214 PHE   K CD2 1 
ATOM   16320 C CE1 . PHE   K  1 214 ? 35.15887  14.67232  55.65937  1.000 48.49165  ?  214 PHE   K CE1 1 
ATOM   16321 C CE2 . PHE   K  1 214 ? 35.42566  12.35347  56.20714  1.000 60.33221  ?  214 PHE   K CE2 1 
ATOM   16322 C CZ  . PHE   K  1 214 ? 35.89105  13.49731  55.56987  1.000 54.25242  ?  214 PHE   K CZ  1 
ATOM   16323 N N   . ASN   K  1 215 ? 30.36107  11.23890  56.76292  1.000 44.97794  ?  215 ASN   K N   1 
ATOM   16324 C CA  . ASN   K  1 215 ? 30.20574  9.95118   56.09118  1.000 52.63665  ?  215 ASN   K CA  1 
ATOM   16325 C C   . ASN   K  1 215 ? 28.74822  9.63785   55.76109  1.000 62.41921  ?  215 ASN   K C   1 
ATOM   16326 O O   . ASN   K  1 215 ? 28.31348  8.48430   55.82909  1.000 56.16288  ?  215 ASN   K O   1 
ATOM   16327 C CB  . ASN   K  1 215 ? 30.82330  8.83718   56.92692  1.000 52.48392  ?  215 ASN   K CB  1 
ATOM   16328 C CG  . ASN   K  1 215 ? 32.33512  8.85922   56.85857  1.000 75.60584  ?  215 ASN   K CG  1 
ATOM   16329 O OD1 . ASN   K  1 215 ? 32.92361  9.00390   55.77961  1.000 54.26627  ?  215 ASN   K OD1 1 
ATOM   16330 N ND2 . ASN   K  1 215 ? 32.97339  8.75237   58.01005  1.000 50.99414  ?  215 ASN   K ND2 1 
ATOM   16331 N N   . ARG   K  1 216 ? 27.98825  10.67222  55.38987  1.000 53.91280  ?  216 ARG   K N   1 
ATOM   16332 C CA  . ARG   K  1 216 ? 26.59602  10.50818  55.00785  1.000 62.79349  ?  216 ARG   K CA  1 
ATOM   16333 C C   . ARG   K  1 216 ? 26.46621  9.53636   53.83460  1.000 85.83684  ?  216 ARG   K C   1 
ATOM   16334 O O   . ARG   K  1 216 ? 27.30249  9.51239   52.92651  1.000 62.02124  ?  216 ARG   K O   1 
ATOM   16335 C CB  . ARG   K  1 216 ? 26.01676  11.87523  54.64519  1.000 59.07636  ?  216 ARG   K CB  1 
ATOM   16336 C CG  . ARG   K  1 216 ? 26.70730  12.53003  53.47029  1.000 58.36767  ?  216 ARG   K CG  1 
ATOM   16337 C CD  . ARG   K  1 216 ? 26.30515  13.97561  53.32244  1.000 68.68168  ?  216 ARG   K CD  1 
ATOM   16338 N NE  . ARG   K  1 216 ? 27.12891  14.66160  52.33097  1.000 57.62200  ?  216 ARG   K NE  1 
ATOM   16339 C CZ  . ARG   K  1 216 ? 28.33911  15.14265  52.58439  1.000 82.40112  ?  216 ARG   K CZ  1 
ATOM   16340 N NH1 . ARG   K  1 216 ? 28.88270  15.04517  53.79007  1.000 61.21426  ?  216 ARG   K NH1 1 
ATOM   16341 N NH2 . ARG   K  1 216 ? 29.02382  15.72674  51.60553  1.000 65.69862  ?  216 ARG   K NH2 1 
ATOM   16342 N N   . ARG   K  1 217 ? 25.44330  8.69080   53.86319  1.000 130.56676 ?  217 ARG   K N   1 
ATOM   16343 C CA  . ARG   K  1 217 ? 25.26327  7.71833   52.78629  1.000 90.66183  ?  217 ARG   K CA  1 
ATOM   16344 C C   . ARG   K  1 217 ? 24.37713  8.34191   51.69450  1.000 103.94096 ?  217 ARG   K C   1 
ATOM   16345 O O   . ARG   K  1 217 ? 23.80705  9.41418   51.87755  1.000 49.27501  ?  217 ARG   K O   1 
ATOM   16346 C CB  . ARG   K  1 217 ? 24.68627  6.40017   53.34797  1.000 59.11836  ?  217 ARG   K CB  1 
ATOM   16347 C CG  . ARG   K  1 217 ? 25.48407  5.83317   54.55657  1.000 66.56075  ?  217 ARG   K CG  1 
ATOM   16348 C CD  . ARG   K  1 217 ? 24.84750  4.60403   55.20969  1.000 54.71557  ?  217 ARG   K CD  1 
ATOM   16349 N NE  . ARG   K  1 217 ? 25.74983  3.50953   55.58545  1.000 25.30169  ?  217 ARG   K NE  1 
ATOM   16350 C CZ  . ARG   K  1 217 ? 26.25185  2.61081   54.72810  1.000 113.87875 ?  217 ARG   K CZ  1 
ATOM   16351 N NH1 . ARG   K  1 217 ? 26.07165  2.72617   53.40832  1.000 73.97480  ?  217 ARG   K NH1 1 
ATOM   16352 N NH2 . ARG   K  1 217 ? 26.94908  1.56982   55.20242  1.000 67.77598  ?  217 ARG   K NH2 1 
ATOM   16353 N N   . PHE   K  1 218 ? 24.33954  7.70848   50.51681  1.000 84.68068  ?  218 PHE   K N   1 
ATOM   16354 C CA  . PHE   K  1 218 ? 23.44077  8.14491   49.44937  1.000 73.54851  ?  218 PHE   K CA  1 
ATOM   16355 C C   . PHE   K  1 218 ? 22.01879  7.66777   49.73672  1.000 103.99881 ?  218 PHE   K C   1 
ATOM   16356 O O   . PHE   K  1 218 ? 21.81035  6.52139   50.14234  1.000 75.75959  ?  218 PHE   K O   1 
ATOM   16357 C CB  . PHE   K  1 218 ? 23.89159  7.60487   48.09726  1.000 64.39943  ?  218 PHE   K CB  1 
ATOM   16358 C CG  . PHE   K  1 218 ? 25.12350  8.26226   47.55554  1.000 84.05525  ?  218 PHE   K CG  1 
ATOM   16359 C CD1 . PHE   K  1 218 ? 25.13311  9.62959   47.26534  1.000 66.06735  ?  218 PHE   K CD1 1 
ATOM   16360 C CD2 . PHE   K  1 218 ? 26.27585  7.50805   47.31348  1.000 74.72802  ?  218 PHE   K CD2 1 
ATOM   16361 C CE1 . PHE   K  1 218 ? 26.27214  10.24247  46.74962  1.000 91.31720  ?  218 PHE   K CE1 1 
ATOM   16362 C CE2 . PHE   K  1 218 ? 27.41713  8.10734   46.80444  1.000 73.99520  ?  218 PHE   K CE2 1 
ATOM   16363 C CZ  . PHE   K  1 218 ? 27.41645  9.48105   46.52167  1.000 67.25081  ?  218 PHE   K CZ  1 
ATOM   16364 N N   . ARG   K  1 219 ? 21.03260  8.53913   49.51401  1.000 106.00831 ?  219 ARG   K N   1 
ATOM   16365 C CA  . ARG   K  1 219 ? 19.64347  8.12636   49.69938  1.000 110.33963 ?  219 ARG   K CA  1 
ATOM   16366 C C   . ARG   K  1 219 ? 19.20491  7.13631   48.63022  1.000 107.27883 ?  219 ARG   K C   1 
ATOM   16367 O O   . ARG   K  1 219 ? 18.38698  6.24987   48.89532  1.000 105.81480 ?  219 ARG   K O   1 
ATOM   16368 C CB  . ARG   K  1 219 ? 18.71413  9.33685   49.67803  1.000 103.12682 ?  219 ARG   K CB  1 
ATOM   16369 C CG  . ARG   K  1 219 ? 17.27534  8.94346   50.02783  1.000 119.56653 ?  219 ARG   K CG  1 
ATOM   16370 C CD  . ARG   K  1 219 ? 16.29560  10.07856  49.85231  1.000 109.47068 ?  219 ARG   K CD  1 
ATOM   16371 N NE  . ARG   K  1 219 ? 16.55012  11.17736  50.77337  1.000 95.59767  ?  219 ARG   K NE  1 
ATOM   16372 C CZ  . ARG   K  1 219 ? 16.30499  11.12425  52.07553  1.000 163.50469 ?  219 ARG   K CZ  1 
ATOM   16373 N NH1 . ARG   K  1 219 ? 15.79244  10.04560  52.64212  1.000 95.85171  ?  219 ARG   K NH1 1 
ATOM   16374 N NH2 . ARG   K  1 219 ? 16.58349  12.17830  52.83133  1.000 87.66719  ?  219 ARG   K NH2 1 
ATOM   16375 N N   . ASN   K  1 220 ? 19.73432  7.27000   47.42255  1.000 101.49898 ?  220 ASN   K N   1 
ATOM   16376 C CA  . ASN   K  1 220 ? 19.28248  6.45193   46.31293  1.000 107.54593 ?  220 ASN   K CA  1 
ATOM   16377 C C   . ASN   K  1 220 ? 20.34902  6.46520   45.22744  1.000 104.43389 ?  220 ASN   K C   1 
ATOM   16378 O O   . ASN   K  1 220 ? 20.26233  7.25024   44.27184  1.000 109.87598 ?  220 ASN   K O   1 
ATOM   16379 C CB  . ASN   K  1 220 ? 17.94943  6.98627   45.78523  1.000 115.45729 ?  220 ASN   K CB  1 
ATOM   16380 C CG  . ASN   K  1 220 ? 17.26016  6.02209   44.84481  1.000 140.74028 ?  220 ASN   K CG  1 
ATOM   16381 O OD1 . ASN   K  1 220 ? 17.88068  5.11259   44.28034  1.000 115.98840 ?  220 ASN   K OD1 1 
ATOM   16382 N ND2 . ASN   K  1 220 ? 15.96547  6.22061   44.66416  1.000 117.27304 ?  220 ASN   K ND2 1 
ATOM   16383 N N   . ARG   K  1 221 ? 21.35955  5.60229   45.36265  1.000 85.86086  ?  221 ARG   K N   1 
ATOM   16384 C CA  . ARG   K  1 221 ? 22.48145  5.66190   44.42870  1.000 89.20292  ?  221 ARG   K CA  1 
ATOM   16385 C C   . ARG   K  1 221 ? 22.03975  5.37440   42.99619  1.000 97.89353  ?  221 ARG   K C   1 
ATOM   16386 O O   . ARG   K  1 221 ? 22.62365  5.92585   42.05882  1.000 87.82643  ?  221 ARG   K O   1 
ATOM   16387 C CB  . ARG   K  1 221 ? 23.60161  4.70612   44.86704  1.000 76.67916  ?  221 ARG   K CB  1 
ATOM   16388 C CG  . ARG   K  1 221 ? 23.26029  3.21395   44.77811  1.000 77.20354  ?  221 ARG   K CG  1 
ATOM   16389 C CD  . ARG   K  1 221 ? 23.82339  2.56582   43.50419  1.000 88.90303  ?  221 ARG   K CD  1 
ATOM   16390 N NE  . ARG   K  1 221 ? 23.43565  1.16104   43.39077  1.000 83.93344  ?  221 ARG   K NE  1 
ATOM   16391 C CZ  . ARG   K  1 221 ? 24.12379  0.13643   43.88428  1.000 95.46258  ?  221 ARG   K CZ  1 
ATOM   16392 N NH1 . ARG   K  1 221 ? 25.25786  0.30666   44.54788  1.000 89.83398  ?  221 ARG   K NH1 1 
ATOM   16393 N NH2 . ARG   K  1 221 ? 23.66897  -1.09478  43.70013  1.000 80.55296  ?  221 ARG   K NH2 1 
ATOM   16394 N N   . ASP   K  1 222 ? 20.99164  4.55763   42.80208  1.000 77.39014  ?  222 ASP   K N   1 
ATOM   16395 C CA  . ASP   K  1 222 ? 20.53621  4.25006   41.44490  1.000 94.37297  ?  222 ASP   K CA  1 
ATOM   16396 C C   . ASP   K  1 222 ? 20.02456  5.47893   40.68754  1.000 97.09921  ?  222 ASP   K C   1 
ATOM   16397 O O   . ASP   K  1 222 ? 20.01634  5.47123   39.44843  1.000 83.92184  ?  222 ASP   K O   1 
ATOM   16398 C CB  . ASP   K  1 222 ? 19.45312  3.17142   41.47619  1.000 71.89566  ?  222 ASP   K CB  1 
ATOM   16399 C CG  . ASP   K  1 222 ? 19.96393  1.83524   42.04663  1.000 90.88776  ?  222 ASP   K CG  1 
ATOM   16400 O OD1 . ASP   K  1 222 ? 20.82595  1.16370   41.42501  1.000 97.85243  ?  222 ASP   K OD1 1 
ATOM   16401 O OD2 . ASP   K  1 222 ? 19.50839  1.48147   43.15059  1.000 106.98644 -1 222 ASP   K OD2 1 
ATOM   16402 N N   . ILE   K  1 223 ? 19.61889  6.53978   41.38396  1.000 92.75179  ?  223 ILE   K N   1 
ATOM   16403 C CA  . ILE   K  1 223 ? 19.31912  7.79274   40.69539  1.000 102.30800 ?  223 ILE   K CA  1 
ATOM   16404 C C   . ILE   K  1 223 ? 20.59042  8.61345   40.48671  1.000 113.51687 ?  223 ILE   K C   1 
ATOM   16405 O O   . ILE   K  1 223 ? 20.95016  8.95357   39.35324  1.000 116.04385 ?  223 ILE   K O   1 
ATOM   16406 C CB  . ILE   K  1 223 ? 18.24471  8.58402   41.46683  1.000 114.93714 ?  223 ILE   K CB  1 
ATOM   16407 C CG1 . ILE   K  1 223 ? 16.89963  7.86724   41.39409  1.000 95.95382  ?  223 ILE   K CG1 1 
ATOM   16408 C CG2 . ILE   K  1 223 ? 18.09131  9.99273   40.92096  1.000 83.74226  ?  223 ILE   K CG2 1 
ATOM   16409 C CD1 . ILE   K  1 223 ? 15.87039  8.50041   42.28293  1.000 98.98214  ?  223 ILE   K CD1 1 
ATOM   16410 N N   . ASP   K  1 224 ? 21.30595  8.91208   41.57785  1.000 91.62316  ?  224 ASP   K N   1 
ATOM   16411 C CA  . ASP   K  1 224 ? 22.37134  9.91488   41.57713  1.000 92.72870  ?  224 ASP   K CA  1 
ATOM   16412 C C   . ASP   K  1 224 ? 23.75826  9.39222   41.20607  1.000 93.60546  ?  224 ASP   K C   1 
ATOM   16413 O O   . ASP   K  1 224 ? 24.54732  10.14390  40.61827  1.000 89.19718  ?  224 ASP   K O   1 
ATOM   16414 C CB  . ASP   K  1 224 ? 22.44625  10.57120  42.95168  1.000 88.63881  ?  224 ASP   K CB  1 
ATOM   16415 C CG  . ASP   K  1 224 ? 21.12417  11.16682  43.37490  1.000 102.00746 ?  224 ASP   K CG  1 
ATOM   16416 O OD1 . ASP   K  1 224 ? 20.69543  12.13945  42.72016  1.000 105.13763 ?  224 ASP   K OD1 1 
ATOM   16417 O OD2 . ASP   K  1 224 ? 20.51844  10.65125  44.34197  1.000 101.65949 -1 224 ASP   K OD2 1 
ATOM   16418 N N   . ARG   K  1 225 ? 24.09735  8.15183   41.55724  1.000 86.00768  ?  225 ARG   K N   1 
ATOM   16419 C CA  . ARG   K  1 225 ? 25.43233  7.59197   41.31203  1.000 76.68159  ?  225 ARG   K CA  1 
ATOM   16420 C C   . ARG   K  1 225 ? 25.28003  6.13162   40.92237  1.000 91.77983  ?  225 ARG   K C   1 
ATOM   16421 O O   . ARG   K  1 225 ? 25.67060  5.22024   41.66333  1.000 85.81714  ?  225 ARG   K O   1 
ATOM   16422 C CB  . ARG   K  1 225 ? 26.32315  7.73982   42.55169  1.000 77.73357  ?  225 ARG   K CB  1 
ATOM   16423 N N   . PRO   K  1 226 ? 24.68608  5.86658   39.76506  1.000 89.83726  ?  226 PRO   K N   1 
ATOM   16424 C CA  . PRO   K  1 226 ? 24.39191  4.47618   39.39363  1.000 71.63947  ?  226 PRO   K CA  1 
ATOM   16425 C C   . PRO   K  1 226 ? 25.65491  3.68068   39.10749  1.000 96.17586  ?  226 PRO   K C   1 
ATOM   16426 O O   . PRO   K  1 226 ? 26.65894  4.21229   38.62950  1.000 79.40720  ?  226 PRO   K O   1 
ATOM   16427 C CB  . PRO   K  1 226 ? 23.54530  4.61986   38.12117  1.000 70.75471  ?  226 PRO   K CB  1 
ATOM   16428 C CG  . PRO   K  1 226 ? 23.95190  5.97324   37.54695  1.000 69.53146  ?  226 PRO   K CG  1 
ATOM   16429 C CD  . PRO   K  1 226 ? 24.23736  6.83984   38.74591  1.000 72.73400  ?  226 PRO   K CD  1 
ATOM   16430 N N   . VAL   K  1 227 ? 25.58436  2.38143   39.39458  1.000 75.25859  ?  227 VAL   K N   1 
ATOM   16431 C CA  . VAL   K  1 227 ? 26.61520  1.43673   38.98189  1.000 72.28252  ?  227 VAL   K CA  1 
ATOM   16432 C C   . VAL   K  1 227 ? 26.51767  1.27459   37.47091  1.000 84.71850  ?  227 VAL   K C   1 
ATOM   16433 O O   . VAL   K  1 227 ? 25.80733  0.38981   36.98058  1.000 85.70892  ?  227 VAL   K O   1 
ATOM   16434 C CB  . VAL   K  1 227 ? 26.46124  0.08532   39.70675  1.000 75.45430  ?  227 VAL   K CB  1 
ATOM   16435 C CG1 . VAL   K  1 227 ? 27.57217  -0.88048  39.31448  1.000 76.61298  ?  227 VAL   K CG1 1 
ATOM   16436 C CG2 . VAL   K  1 227 ? 26.44629  0.30063   41.21246  1.000 70.67825  ?  227 VAL   K CG2 1 
ATOM   16437 N N   . VAL   K  1 228 ? 27.23480  2.13178   36.73137  1.000 81.99859  ?  228 VAL   K N   1 
ATOM   16438 C CA  . VAL   K  1 228 ? 27.05890  2.25895   35.28792  1.000 69.59045  ?  228 VAL   K CA  1 
ATOM   16439 C C   . VAL   K  1 228 ? 27.25923  0.91868   34.59869  1.000 109.87611 ?  228 VAL   K C   1 
ATOM   16440 O O   . VAL   K  1 228 ? 28.24469  0.21234   34.83986  1.000 80.14715  ?  228 VAL   K O   1 
ATOM   16441 C CB  . VAL   K  1 228 ? 28.01709  3.32745   34.74521  1.000 88.00695  ?  228 VAL   K CB  1 
ATOM   16442 C CG1 . VAL   K  1 228 ? 27.87342  3.46295   33.23880  1.000 74.40145  ?  228 VAL   K CG1 1 
ATOM   16443 C CG2 . VAL   K  1 228 ? 27.75190  4.65418   35.45026  1.000 69.01631  ?  228 VAL   K CG2 1 
ATOM   16444 N N   . GLY   K  1 229 ? 26.31167  0.56393   33.72951  1.000 94.74052  ?  229 GLY   K N   1 
ATOM   16445 C CA  . GLY   K  1 229 ? 26.32353  -0.71159  33.04222  1.000 78.64674  ?  229 GLY   K CA  1 
ATOM   16446 C C   . GLY   K  1 229 ? 25.75696  -1.86965  33.83605  1.000 85.66317  ?  229 GLY   K C   1 
ATOM   16447 O O   . GLY   K  1 229 ? 25.58178  -2.96399  33.27286  1.000 100.86486 ?  229 GLY   K O   1 
ATOM   16448 N N   . GLY   K  1 230 ? 25.48524  -1.67121  35.11942  1.000 100.41980 ?  230 GLY   K N   1 
ATOM   16449 C CA  . GLY   K  1 230 ? 24.88052  -2.67361  35.98832  1.000 71.47382  ?  230 GLY   K CA  1 
ATOM   16450 C C   . GLY   K  1 230 ? 25.89089  -3.64354  36.57275  1.000 119.02905 ?  230 GLY   K C   1 
ATOM   16451 O O   . GLY   K  1 230 ? 26.88573  -4.01716  35.94412  1.000 89.03648  ?  230 GLY   K O   1 
ATOM   16452 N N   . VAL   K  1 231 ? 25.60031  -4.08186  37.80262  1.000 81.47988  ?  231 VAL   K N   1 
ATOM   16453 C CA  . VAL   K  1 231 ? 26.46175  -4.98435  38.55832  1.000 121.82442 ?  231 VAL   K CA  1 
ATOM   16454 C C   . VAL   K  1 231 ? 26.76294  -6.26815  37.79211  1.000 81.68831  ?  231 VAL   K C   1 
ATOM   16455 O O   . VAL   K  1 231 ? 27.78675  -6.91749  38.04371  1.000 116.80139 ?  231 VAL   K O   1 
ATOM   16456 C CB  . VAL   K  1 231 ? 25.79700  -5.26555  39.91904  1.000 74.28720  ?  231 VAL   K CB  1 
ATOM   16457 C CG1 . VAL   K  1 231 ? 24.42570  -5.83120  39.69978  1.000 129.09408 ?  231 VAL   K CG1 1 
ATOM   16458 C CG2 . VAL   K  1 231 ? 26.60063  -6.22900  40.73370  1.000 101.64225 ?  231 VAL   K CG2 1 
ATOM   16459 N N   . ASN   K  1 232 ? 25.92928  -6.61655  36.81138  1.000 110.40317 ?  232 ASN   K N   1 
ATOM   16460 C CA  . ASN   K  1 232 ? 26.10156  -7.85691  36.05950  1.000 99.37944  ?  232 ASN   K CA  1 
ATOM   16461 C C   . ASN   K  1 232 ? 27.15579  -7.77551  34.96251  1.000 111.06273 ?  232 ASN   K C   1 
ATOM   16462 O O   . ASN   K  1 232 ? 27.60865  -8.82570  34.49159  1.000 106.27060 ?  232 ASN   K O   1 
ATOM   16463 C CB  . ASN   K  1 232 ? 24.77937  -8.27652  35.43035  1.000 116.12357 ?  232 ASN   K CB  1 
ATOM   16464 C CG  . ASN   K  1 232 ? 23.94335  -9.11580  36.35939  1.000 115.74475 ?  232 ASN   K CG  1 
ATOM   16465 O OD1 . ASN   K  1 232 ? 24.20727  -9.17270  37.56761  1.000 116.75022 ?  232 ASN   K OD1 1 
ATOM   16466 N ND2 . ASN   K  1 232 ? 22.92827  -9.78113  35.80741  1.000 191.87710 ?  232 ASN   K ND2 1 
ATOM   16467 N N   . ASN   K  1 233 ? 27.53764  -6.57793  34.51880  1.000 90.73368  ?  233 ASN   K N   1 
ATOM   16468 C CA  . ASN   K  1 233 ? 28.57413  -6.43483  33.50446  1.000 98.43296  ?  233 ASN   K CA  1 
ATOM   16469 C C   . ASN   K  1 233 ? 29.91513  -6.39214  34.23390  1.000 150.90156 ?  233 ASN   K C   1 
ATOM   16470 O O   . ASN   K  1 233 ? 30.26024  -5.38598  34.87385  1.000 96.18117  ?  233 ASN   K O   1 
ATOM   16471 C CB  . ASN   K  1 233 ? 28.34076  -5.17689  32.66993  1.000 78.34665  ?  233 ASN   K CB  1 
ATOM   16472 C CG  . ASN   K  1 233 ? 29.30383  -5.06408  31.50869  1.000 115.73674 ?  233 ASN   K CG  1 
ATOM   16473 O OD1 . ASN   K  1 233 ? 30.42041  -5.58813  31.54747  1.000 108.79959 ?  233 ASN   K OD1 1 
ATOM   16474 N ND2 . ASN   K  1 233 ? 28.88139  -4.36289  30.46872  1.000 104.48625 ?  233 ASN   K ND2 1 
ATOM   16475 N N   . THR   K  1 234 ? 30.66390  -7.48823  34.16627  1.000 88.59761  ?  234 THR   K N   1 
ATOM   16476 C CA  . THR   K  1 234 ? 31.90599  -7.57591  34.92192  1.000 103.93205 ?  234 THR   K CA  1 
ATOM   16477 C C   . THR   K  1 234 ? 33.11153  -7.11023  34.11715  1.000 84.16619  ?  234 THR   K C   1 
ATOM   16478 O O   . THR   K  1 234 ? 34.24338  -7.21251  34.60038  1.000 134.66385 ?  234 THR   K O   1 
ATOM   16479 C CB  . THR   K  1 234 ? 32.11918  -9.00073  35.45040  1.000 89.82860  ?  234 THR   K CB  1 
ATOM   16480 O OG1 . THR   K  1 234 ? 32.37004  -9.90116  34.37063  1.000 100.01240 ?  234 THR   K OG1 1 
ATOM   16481 C CG2 . THR   K  1 234 ? 30.89533  -9.47151  36.21679  1.000 79.81668  ?  234 THR   K CG2 1 
ATOM   16482 N N   . THR   K  1 235 ? 32.88718  -6.55524  32.93102  1.000 115.50052 ?  235 THR   K N   1 
ATOM   16483 C CA  . THR   K  1 235 ? 33.96037  -5.97906  32.13618  1.000 97.71093  ?  235 THR   K CA  1 
ATOM   16484 C C   . THR   K  1 235 ? 34.25625  -4.53268  32.50605  1.000 117.81530 ?  235 THR   K C   1 
ATOM   16485 O O   . THR   K  1 235 ? 35.13795  -3.92151  31.88788  1.000 101.07118 ?  235 THR   K O   1 
ATOM   16486 C CB  . THR   K  1 235 ? 33.60535  -6.06108  30.65085  1.000 132.86132 ?  235 THR   K CB  1 
ATOM   16487 O OG1 . THR   K  1 235 ? 32.69436  -5.00046  30.30618  1.000 94.05066  ?  235 THR   K OG1 1 
ATOM   16488 C CG2 . THR   K  1 235 ? 32.93730  -7.38424  30.36099  1.000 104.01912 ?  235 THR   K CG2 1 
ATOM   16489 N N   . LEU   K  1 236 ? 33.55114  -3.97546  33.49464  1.000 95.52465  ?  236 LEU   K N   1 
ATOM   16490 C CA  . LEU   K  1 236 ? 33.65593  -2.56549  33.85314  1.000 95.99630  ?  236 LEU   K CA  1 
ATOM   16491 C C   . LEU   K  1 236 ? 34.21310  -2.43064  35.25811  1.000 89.61454  ?  236 LEU   K C   1 
ATOM   16492 O O   . LEU   K  1 236 ? 33.87882  -3.22304  36.14613  1.000 91.33283  ?  236 LEU   K O   1 
ATOM   16493 C CB  . LEU   K  1 236 ? 32.29850  -1.86778  33.78701  1.000 89.52258  ?  236 LEU   K CB  1 
ATOM   16494 C CG  . LEU   K  1 236 ? 31.53441  -2.09722  32.48571  1.000 96.81567  ?  236 LEU   K CG  1 
ATOM   16495 C CD1 . LEU   K  1 236 ? 30.06376  -1.71966  32.67093  1.000 88.76651  ?  236 LEU   K CD1 1 
ATOM   16496 C CD2 . LEU   K  1 236 ? 32.19526  -1.32647  31.34272  1.000 79.24215  ?  236 LEU   K CD2 1 
ATOM   16497 N N   . ILE   K  1 237 ? 35.06587  -1.42654  35.45115  1.000 93.42136  ?  237 ILE   K N   1 
ATOM   16498 C CA  . ILE   K  1 237 ? 35.63292  -1.10777  36.75618  1.000 86.74788  ?  237 ILE   K CA  1 
ATOM   16499 C C   . ILE   K  1 237 ? 35.14151  0.27901   37.14937  1.000 97.98429  ?  237 ILE   K C   1 
ATOM   16500 O O   . ILE   K  1 237 ? 35.33793  1.25399   36.40105  1.000 84.90728  ?  237 ILE   K O   1 
ATOM   16501 C CB  . ILE   K  1 237 ? 37.17077  -1.17097  36.75484  1.000 85.57110  ?  237 ILE   K CB  1 
ATOM   16502 C CG1 . ILE   K  1 237 ? 37.65600  -2.56088  36.32458  1.000 82.49353  ?  237 ILE   K CG1 1 
ATOM   16503 C CG2 . ILE   K  1 237 ? 37.70668  -0.83070  38.15416  1.000 83.44041  ?  237 ILE   K CG2 1 
ATOM   16504 C CD1 . ILE   K  1 237 ? 39.17765  -2.72933  36.32175  1.000 84.38829  ?  237 ILE   K CD1 1 
ATOM   16505 N N   . SER   K  1 238 ? 34.51736  0.36279   38.33284  1.000 76.04311  ?  238 SER   K N   1 
ATOM   16506 C CA  . SER   K  1 238 ? 33.90921  1.59223   38.83762  1.000 82.81212  ?  238 SER   K CA  1 
ATOM   16507 C C   . SER   K  1 238 ? 34.88583  2.41562   39.66526  1.000 91.55813  ?  238 SER   K C   1 
ATOM   16508 O O   . SER   K  1 238 ? 35.78943  1.88100   40.31454  1.000 76.53031  ?  238 SER   K O   1 
ATOM   16509 C CB  . SER   K  1 238 ? 32.68456  1.28575   39.70553  1.000 81.27467  ?  238 SER   K CB  1 
ATOM   16510 O OG  . SER   K  1 238 ? 31.52636  1.12938   38.91287  1.000 95.05598  ?  238 SER   K OG  1 
ATOM   16511 N N   . ALA   K  1 239 ? 34.66334  3.72967   39.66295  1.000 76.07854  ?  239 ALA   K N   1 
ATOM   16512 C CA  . ALA   K  1 239 ? 35.36288  4.62671   40.57434  1.000 84.13373  ?  239 ALA   K CA  1 
ATOM   16513 C C   . ALA   K  1 239 ? 35.00359  4.30943   42.01705  1.000 60.33425  ?  239 ALA   K C   1 
ATOM   16514 O O   . ALA   K  1 239 ? 33.82392  4.23016   42.36357  1.000 75.76698  ?  239 ALA   K O   1 
ATOM   16515 C CB  . ALA   K  1 239 ? 34.99523  6.07131   40.26193  1.000 56.70896  ?  239 ALA   K CB  1 
ATOM   16516 N N   . ALA   K  1 240 ? 36.02403  4.16330   42.87208  1.000 66.00607  ?  240 ALA   K N   1 
ATOM   16517 C CA  . ALA   K  1 240 ? 35.78149  3.79463   44.26833  1.000 59.62564  ?  240 ALA   K CA  1 
ATOM   16518 C C   . ALA   K  1 240 ? 35.40432  4.97784   45.15264  1.000 66.09525  ?  240 ALA   K C   1 
ATOM   16519 O O   . ALA   K  1 240 ? 34.80982  4.77190   46.22072  1.000 61.41075  ?  240 ALA   K O   1 
ATOM   16520 C CB  . ALA   K  1 240 ? 37.01265  3.10911   44.86009  1.000 51.35564  ?  240 ALA   K CB  1 
ATOM   16521 N N   . CYS   K  1 241 ? 35.75298  6.20013   44.74717  1.000 42.20050  ?  241 CYS   K N   1 
ATOM   16522 C CA  . CYS   K  1 241 ? 35.52640  7.38930   45.55444  1.000 52.10655  ?  241 CYS   K CA  1 
ATOM   16523 C C   . CYS   K  1 241 ? 35.01887  8.50696   44.66089  1.000 52.41637  ?  241 CYS   K C   1 
ATOM   16524 O O   . CYS   K  1 241 ? 35.50128  8.68504   43.53463  1.000 51.41882  ?  241 CYS   K O   1 
ATOM   16525 C CB  . CYS   K  1 241 ? 36.80045  7.86861   46.26741  1.000 53.74403  ?  241 CYS   K CB  1 
ATOM   16526 S SG  . CYS   K  1 241 ? 37.45424  6.70974   47.48447  1.000 54.00036  ?  241 CYS   K SG  1 
ATOM   16527 N N   . GLU   K  1 242 ? 34.03309  9.24772   45.17395  1.000 69.59987  ?  242 GLU   K N   1 
ATOM   16528 C CA  . GLU   K  1 242 ? 33.65067  10.53435  44.61092  1.000 53.26769  ?  242 GLU   K CA  1 
ATOM   16529 C C   . GLU   K  1 242 ? 34.83512  11.49193  44.67417  1.000 56.16948  ?  242 GLU   K C   1 
ATOM   16530 O O   . GLU   K  1 242 ? 35.24614  11.90023  45.76900  1.000 78.75012  ?  242 GLU   K O   1 
ATOM   16531 C CB  . GLU   K  1 242 ? 32.45985  11.09652  45.38453  1.000 64.14870  ?  242 GLU   K CB  1 
ATOM   16532 C CG  . GLU   K  1 242 ? 31.92718  12.42820  44.86883  1.000 58.48178  ?  242 GLU   K CG  1 
ATOM   16533 C CD  . GLU   K  1 242 ? 31.12238  12.30388  43.57974  1.000 82.48635  ?  242 GLU   K CD  1 
ATOM   16534 O OE1 . GLU   K  1 242 ? 30.67453  11.17790  43.21667  1.000 61.96247  ?  242 GLU   K OE1 1 
ATOM   16535 O OE2 . GLU   K  1 242 ? 30.94226  13.36182  42.93439  1.000 68.50733  -1 242 GLU   K OE2 1 
ATOM   16536 N N   . SER   K  1 243 ? 35.39524  11.86852  43.52720  1.000 58.74588  ?  243 SER   K N   1 
ATOM   16537 C CA  . SER   K  1 243 ? 36.68691  12.54562  43.54455  1.000 70.22934  ?  243 SER   K CA  1 
ATOM   16538 C C   . SER   K  1 243 ? 36.87841  13.33386  42.25596  1.000 60.46151  ?  243 SER   K C   1 
ATOM   16539 O O   . SER   K  1 243 ? 36.04069  13.30500  41.34730  1.000 64.96557  ?  243 SER   K O   1 
ATOM   16540 C CB  . SER   K  1 243 ? 37.82750  11.52903  43.72405  1.000 59.45924  ?  243 SER   K CB  1 
ATOM   16541 O OG  . SER   K  1 243 ? 37.78390  10.56044  42.67899  1.000 66.95544  ?  243 SER   K OG  1 
ATOM   16542 N N   . LEU   K  1 244 ? 38.01989  14.02256  42.18818  1.000 52.99907  ?  244 LEU   K N   1 
ATOM   16543 C CA  . LEU   K  1 244 ? 38.54921  14.62104  40.97025  1.000 58.53438  ?  244 LEU   K CA  1 
ATOM   16544 C C   . LEU   K  1 244 ? 39.76221  13.82170  40.50313  1.000 56.03750  ?  244 LEU   K C   1 
ATOM   16545 O O   . LEU   K  1 244 ? 40.57218  13.37887  41.32548  1.000 62.31883  ?  244 LEU   K O   1 
ATOM   16546 C CB  . LEU   K  1 244 ? 38.94331  16.07533  41.21311  1.000 43.40237  ?  244 LEU   K CB  1 
ATOM   16547 C CG  . LEU   K  1 244 ? 37.79990  17.01435  41.59441  1.000 61.84032  ?  244 LEU   K CG  1 
ATOM   16548 C CD1 . LEU   K  1 244 ? 38.33573  18.30818  42.16040  1.000 55.80111  ?  244 LEU   K CD1 1 
ATOM   16549 C CD2 . LEU   K  1 244 ? 36.99617  17.26658  40.35869  1.000 49.02940  ?  244 LEU   K CD2 1 
ATOM   16550 N N   . SER   K  1 245 ? 39.85822  13.60243  39.19344  1.000 88.04825  ?  245 SER   K N   1 
ATOM   16551 C CA  . SER   K  1 245 ? 41.06044  13.06298  38.56883  1.000 48.67008  ?  245 SER   K CA  1 
ATOM   16552 C C   . SER   K  1 245 ? 42.30555  13.78719  39.08391  1.000 48.71571  ?  245 SER   K C   1 
ATOM   16553 O O   . SER   K  1 245 ? 42.34279  15.02342  39.12227  1.000 57.67870  ?  245 SER   K O   1 
ATOM   16554 C CB  . SER   K  1 245 ? 40.92184  13.24453  37.05497  1.000 51.41041  ?  245 SER   K CB  1 
ATOM   16555 O OG  . SER   K  1 245 ? 42.05198  12.78021  36.36878  1.000 96.98321  ?  245 SER   K OG  1 
ATOM   16556 N N   . TYR   K  1 246 ? 43.32932  13.02816  39.49674  1.000 45.45314  ?  246 TYR   K N   1 
ATOM   16557 C CA  . TYR   K  1 246 ? 44.57188  13.68173  39.91863  1.000 35.58975  ?  246 TYR   K CA  1 
ATOM   16558 C C   . TYR   K  1 246 ? 45.78784  13.29312  39.08742  1.000 37.20490  ?  246 TYR   K C   1 
ATOM   16559 O O   . TYR   K  1 246 ? 46.59406  14.16949  38.73502  1.000 40.26524  ?  246 TYR   K O   1 
ATOM   16560 C CB  . TYR   K  1 246 ? 44.87663  13.42298  41.40331  1.000 25.96207  ?  246 TYR   K CB  1 
ATOM   16561 C CG  . TYR   K  1 246 ? 46.09186  14.20177  41.85581  1.000 42.14302  ?  246 TYR   K CG  1 
ATOM   16562 C CD1 . TYR   K  1 246 ? 47.39017  13.69951  41.67624  1.000 35.24772  ?  246 TYR   K CD1 1 
ATOM   16563 C CD2 . TYR   K  1 246 ? 45.94669  15.45157  42.44659  1.000 21.35643  ?  246 TYR   K CD2 1 
ATOM   16564 C CE1 . TYR   K  1 246 ? 48.49097  14.43632  42.06646  1.000 28.98560  ?  246 TYR   K CE1 1 
ATOM   16565 C CE2 . TYR   K  1 246 ? 47.04709  16.19475  42.85193  1.000 47.64890  ?  246 TYR   K CE2 1 
ATOM   16566 C CZ  . TYR   K  1 246 ? 48.30868  15.68626  42.65554  1.000 38.66864  ?  246 TYR   K CZ  1 
ATOM   16567 O OH  . TYR   K  1 246 ? 49.37337  16.44114  43.05787  1.000 54.76616  ?  246 TYR   K OH  1 
ATOM   16568 N N   . ASN   K  1 247 ? 45.98863  12.00068  38.82930  1.000 33.89748  ?  247 ASN   K N   1 
ATOM   16569 C CA  . ASN   K  1 247 ? 47.11070  11.53100  38.02525  1.000 26.28145  ?  247 ASN   K CA  1 
ATOM   16570 C C   . ASN   K  1 247 ? 46.76550  10.14966  37.49347  1.000 33.35652  ?  247 ASN   K C   1 
ATOM   16571 O O   . ASN   K  1 247 ? 46.06970  9.37303   38.15784  1.000 36.59146  ?  247 ASN   K O   1 
ATOM   16572 C CB  . ASN   K  1 247 ? 48.41992  11.46697  38.82174  1.000 36.51950  ?  247 ASN   K CB  1 
ATOM   16573 C CG  . ASN   K  1 247 ? 49.54159  10.79422  38.03899  1.000 34.16857  ?  247 ASN   K CG  1 
ATOM   16574 O OD1 . ASN   K  1 247 ? 50.12144  11.40357  37.13717  1.000 51.64665  ?  247 ASN   K OD1 1 
ATOM   16575 N ND2 . ASN   K  1 247 ? 49.83319  9.52442   38.35704  1.000 32.61014  ?  247 ASN   K ND2 1 
ATOM   16576 N N   . VAL   K  1 248 ? 47.23601  9.86151   36.27823  1.000 42.83819  ?  248 VAL   K N   1 
ATOM   16577 C CA  . VAL   K  1 248 ? 47.30153  8.49913   35.76310  1.000 48.62940  ?  248 VAL   K CA  1 
ATOM   16578 C C   . VAL   K  1 248 ? 48.73974  8.22160   35.36416  1.000 40.16478  ?  248 VAL   K C   1 
ATOM   16579 O O   . VAL   K  1 248 ? 49.39483  9.07530   34.75701  1.000 47.67318  ?  248 VAL   K O   1 
ATOM   16580 C CB  . VAL   K  1 248 ? 46.35909  8.28588   34.56863  1.000 44.17876  ?  248 VAL   K CB  1 
ATOM   16581 C CG1 . VAL   K  1 248 ? 46.68484  6.96623   33.86311  1.000 36.97462  ?  248 VAL   K CG1 1 
ATOM   16582 C CG2 . VAL   K  1 248 ? 44.91502  8.32890   35.03977  1.000 42.27480  ?  248 VAL   K CG2 1 
ATOM   16583 N N   . SER   K  1 249 ? 49.24905  7.05197   35.74488  1.000 45.98715  ?  249 SER   K N   1 
ATOM   16584 C CA  . SER   K  1 249 ? 50.59950  6.66315   35.36405  1.000 33.35882  ?  249 SER   K CA  1 
ATOM   16585 C C   . SER   K  1 249 ? 50.56605  5.27204   34.76723  1.000 45.93822  ?  249 SER   K C   1 
ATOM   16586 O O   . SER   K  1 249 ? 49.86315  4.38526   35.26789  1.000 35.74001  ?  249 SER   K O   1 
ATOM   16587 C CB  . SER   K  1 249 ? 51.56574  6.69581   36.54342  1.000 32.94687  ?  249 SER   K CB  1 
ATOM   16588 O OG  . SER   K  1 249 ? 51.87000  8.03201   36.89302  1.000 38.64016  ?  249 SER   K OG  1 
ATOM   16589 N N   . TYR   K  1 250 ? 51.32483  5.09331   33.69219  1.000 40.66537  ?  250 TYR   K N   1 
ATOM   16590 C CA  . TYR   K  1 250 ? 51.47237  3.80495   33.04189  1.000 66.81240  ?  250 TYR   K CA  1 
ATOM   16591 C C   . TYR   K  1 250 ? 52.87679  3.27282   33.28151  1.000 38.06609  ?  250 TYR   K C   1 
ATOM   16592 O O   . TYR   K  1 250 ? 53.81247  4.03491   33.57122  1.000 47.17403  ?  250 TYR   K O   1 
ATOM   16593 C CB  . TYR   K  1 250 ? 51.19972  3.91817   31.53943  1.000 37.49775  ?  250 TYR   K CB  1 
ATOM   16594 C CG  . TYR   K  1 250 ? 49.82568  4.42537   31.20519  1.000 53.03333  ?  250 TYR   K CG  1 
ATOM   16595 C CD1 . TYR   K  1 250 ? 48.72891  3.56593   31.20900  1.000 39.41349  ?  250 TYR   K CD1 1 
ATOM   16596 C CD2 . TYR   K  1 250 ? 49.61345  5.76013   30.90010  1.000 35.53170  ?  250 TYR   K CD2 1 
ATOM   16597 C CE1 . TYR   K  1 250 ? 47.44508  4.03153   30.90040  1.000 51.26419  ?  250 TYR   K CE1 1 
ATOM   16598 C CE2 . TYR   K  1 250 ? 48.34688  6.23047   30.59446  1.000 46.61427  ?  250 TYR   K CE2 1 
ATOM   16599 C CZ  . TYR   K  1 250 ? 47.26177  5.36870   30.59291  1.000 58.52032  ?  250 TYR   K CZ  1 
ATOM   16600 O OH  . TYR   K  1 250 ? 45.98981  5.84098   30.28823  1.000 64.03939  ?  250 TYR   K OH  1 
ATOM   16601 N N   . ASP   K  1 251 ? 53.00134  1.94699   33.16039  1.000 57.31334  ?  251 ASP   K N   1 
ATOM   16602 C CA  . ASP   K  1 251 ? 54.27491  1.24819   33.31192  1.000 57.57156  ?  251 ASP   K CA  1 
ATOM   16603 C C   . ASP   K  1 251 ? 54.95890  1.64870   34.62246  1.000 76.22555  ?  251 ASP   K C   1 
ATOM   16604 O O   . ASP   K  1 251 ? 56.08465  2.15352   34.64946  1.000 61.09180  ?  251 ASP   K O   1 
ATOM   16605 C CB  . ASP   K  1 251 ? 55.17643  1.53537   32.10963  1.000 56.90251  ?  251 ASP   K CB  1 
ATOM   16606 C CG  . ASP   K  1 251 ? 56.39324  0.63401   32.05723  1.000 79.11264  ?  251 ASP   K CG  1 
ATOM   16607 O OD1 . ASP   K  1 251 ? 56.23028  -0.57688  32.33281  1.000 65.54583  ?  251 ASP   K OD1 1 
ATOM   16608 O OD2 . ASP   K  1 251 ? 57.49729  1.14314   31.72595  1.000 65.08862  -1 251 ASP   K OD2 1 
ATOM   16609 N N   . VAL   K  1 252 ? 54.23647  1.45240   35.72474  1.000 45.02550  ?  252 VAL   K N   1 
ATOM   16610 C CA  . VAL   K  1 252 ? 54.74922  1.87260   37.02499  1.000 47.31460  ?  252 VAL   K CA  1 
ATOM   16611 C C   . VAL   K  1 252 ? 55.80684  0.89279   37.51896  1.000 48.28049  ?  252 VAL   K C   1 
ATOM   16612 O O   . VAL   K  1 252 ? 55.84180  -0.28581  37.14401  1.000 49.93428  ?  252 VAL   K O   1 
ATOM   16613 C CB  . VAL   K  1 252 ? 53.61720  2.02659   38.05168  1.000 50.16209  ?  252 VAL   K CB  1 
ATOM   16614 C CG1 . VAL   K  1 252 ? 52.67647  3.15283   37.62646  1.000 38.15716  ?  252 VAL   K CG1 1 
ATOM   16615 C CG2 . VAL   K  1 252 ? 52.89486  0.68357   38.25986  1.000 38.54764  ?  252 VAL   K CG2 1 
ATOM   16616 N N   . GLN   K  1 253 ? 56.65326  1.39215   38.41360  1.000 43.39598  ?  253 GLN   K N   1 
ATOM   16617 C CA  . GLN   K  1 253 ? 57.85987  0.69683   38.82345  1.000 49.16242  ?  253 GLN   K CA  1 
ATOM   16618 C C   . GLN   K  1 253 ? 58.13935  0.95931   40.30641  1.000 61.01925  ?  253 GLN   K C   1 
ATOM   16619 O O   . GLN   K  1 253 ? 57.42147  1.70759   40.98538  1.000 48.44907  ?  253 GLN   K O   1 
ATOM   16620 C CB  . GLN   K  1 253 ? 59.02866  1.16238   37.95713  1.000 37.79267  ?  253 GLN   K CB  1 
ATOM   16621 C CG  . GLN   K  1 253 ? 59.20179  2.66737   38.04975  1.000 75.36902  ?  253 GLN   K CG  1 
ATOM   16622 C CD  . GLN   K  1 253 ? 60.35070  3.16731   37.22950  1.000 66.63297  ?  253 GLN   K CD  1 
ATOM   16623 O OE1 . GLN   K  1 253 ? 60.41167  4.34840   36.88228  1.000 67.51353  ?  253 GLN   K OE1 1 
ATOM   16624 N NE2 . GLN   K  1 253 ? 61.28064  2.27592   36.91601  1.000 74.74327  ?  253 GLN   K NE2 1 
ATOM   16625 N N   . SER   K  1 254 ? 59.21224  0.35012   40.80915  1.000 63.77963  ?  254 SER   K N   1 
ATOM   16626 C CA  . SER   K  1 254 ? 59.68523  0.61573   42.15787  1.000 43.72487  ?  254 SER   K CA  1 
ATOM   16627 C C   . SER   K  1 254 ? 60.97415  1.43809   42.13350  1.000 45.81511  ?  254 SER   K C   1 
ATOM   16628 O O   . SER   K  1 254 ? 61.79260  1.34364   41.21153  1.000 57.57267  ?  254 SER   K O   1 
ATOM   16629 C CB  . SER   K  1 254 ? 59.88820  -0.68553  42.92729  1.000 54.49203  ?  254 SER   K CB  1 
ATOM   16630 O OG  . SER   K  1 254 ? 58.65099  -1.38209  43.04124  1.000 46.06379  ?  254 SER   K OG  1 
ATOM   16631 N N   . LEU   K  1 255 ? 61.12201  2.27883   43.14944  1.000 44.36046  ?  255 LEU   K N   1 
ATOM   16632 C CA  . LEU   K  1 255 ? 62.28740  3.12576   43.32115  1.000 46.72213  ?  255 LEU   K CA  1 
ATOM   16633 C C   . LEU   K  1 255 ? 63.02238  2.74463   44.60388  1.000 48.26145  ?  255 LEU   K C   1 
ATOM   16634 O O   . LEU   K  1 255 ? 62.42270  2.25256   45.56499  1.000 49.50983  ?  255 LEU   K O   1 
ATOM   16635 C CB  . LEU   K  1 255 ? 61.86995  4.59396   43.36593  1.000 49.44053  ?  255 LEU   K CB  1 
ATOM   16636 C CG  . LEU   K  1 255 ? 61.01274  4.96479   42.15819  1.000 50.71249  ?  255 LEU   K CG  1 
ATOM   16637 C CD1 . LEU   K  1 255 ? 60.45552  6.37372   42.27131  1.000 49.49886  ?  255 LEU   K CD1 1 
ATOM   16638 C CD2 . LEU   K  1 255 ? 61.82673  4.80356   40.89189  1.000 39.32947  ?  255 LEU   K CD2 1 
ATOM   16639 N N   . ASP   K  1 256 ? 64.33654  2.97252   44.62377  1.000 59.65396  ?  256 ASP   K N   1 
ATOM   16640 C CA  . ASP   K  1 256 ? 65.07858  2.69077   45.84920  1.000 45.02730  ?  256 ASP   K CA  1 
ATOM   16641 C C   . ASP   K  1 256 ? 64.95639  3.82722   46.86496  1.000 67.56315  ?  256 ASP   K C   1 
ATOM   16642 O O   . ASP   K  1 256 ? 64.94784  3.55167   48.07299  1.000 47.56592  ?  256 ASP   K O   1 
ATOM   16643 C CB  . ASP   K  1 256 ? 66.54369  2.38634   45.52622  1.000 55.05253  ?  256 ASP   K CB  1 
ATOM   16644 C CG  . ASP   K  1 256 ? 66.71517  1.05085   44.80108  1.000 81.77648  ?  256 ASP   K CG  1 
ATOM   16645 O OD1 . ASP   K  1 256 ? 66.53933  -0.04182  45.40503  1.000 55.58654  ?  256 ASP   K OD1 1 
ATOM   16646 O OD2 . ASP   K  1 256 ? 67.02379  1.09395   43.60362  1.000 56.26679  -1 256 ASP   K OD2 1 
ATOM   16647 N N   . THR   K  1 257 ? 64.83856  5.08559   46.40715  1.000 55.48702  ?  257 THR   K N   1 
ATOM   16648 C CA  . THR   K  1 257 ? 64.53226  6.22261   47.27085  1.000 83.67770  ?  257 THR   K CA  1 
ATOM   16649 C C   . THR   K  1 257 ? 63.52514  7.13034   46.58364  1.000 49.79499  ?  257 THR   K C   1 
ATOM   16650 O O   . THR   K  1 257 ? 63.39114  7.12645   45.35711  1.000 71.77350  ?  257 THR   K O   1 
ATOM   16651 C CB  . THR   K  1 257 ? 65.77876  7.04965   47.60945  1.000 56.82989  ?  257 THR   K CB  1 
ATOM   16652 O OG1 . THR   K  1 257 ? 66.37625  7.52257   46.39361  1.000 79.54247  ?  257 THR   K OG1 1 
ATOM   16653 C CG2 . THR   K  1 257 ? 66.77021  6.22540   48.34517  1.000 68.41574  ?  257 THR   K CG2 1 
ATOM   16654 N N   . LEU   K  1 258 ? 62.84604  7.94203   47.39429  1.000 59.22491  ?  258 LEU   K N   1 
ATOM   16655 C CA  . LEU   K  1 258 ? 61.88756  8.93436   46.88906  1.000 44.67027  ?  258 LEU   K CA  1 
ATOM   16656 C C   . LEU   K  1 258 ? 62.51514  10.32802  46.92896  1.000 71.90785  ?  258 LEU   K C   1 
ATOM   16657 O O   . LEU   K  1 258 ? 62.13398  11.21147  47.71593  1.000 75.21688  ?  258 LEU   K O   1 
ATOM   16658 C CB  . LEU   K  1 258 ? 60.59623  8.89507   47.70597  1.000 44.80076  ?  258 LEU   K CB  1 
ATOM   16659 C CG  . LEU   K  1 258 ? 60.05823  7.51029   48.03264  1.000 40.65872  ?  258 LEU   K CG  1 
ATOM   16660 C CD1 . LEU   K  1 258 ? 58.89139  7.67947   48.95848  1.000 47.84813  ?  258 LEU   K CD1 1 
ATOM   16661 C CD2 . LEU   K  1 258 ? 59.67322  6.73905   46.76810  1.000 37.07135  ?  258 LEU   K CD2 1 
ATOM   16662 N N   . VAL   K  1 259 ? 63.51207  10.50458  46.06506  1.000 72.40821  ?  259 VAL   K N   1 
ATOM   16663 C CA  . VAL   K  1 259 ? 64.32977  11.71327  46.00767  1.000 75.74593  ?  259 VAL   K CA  1 
ATOM   16664 C C   . VAL   K  1 259 ? 64.48767  12.09364  44.54873  1.000 139.89434 ?  259 VAL   K C   1 
ATOM   16665 O O   . VAL   K  1 259 ? 64.85861  11.24041  43.72515  1.000 71.40127  ?  259 VAL   K O   1 
ATOM   16666 C CB  . VAL   K  1 259 ? 65.73773  11.52031  46.60974  1.000 95.42513  ?  259 VAL   K CB  1 
ATOM   16667 C CG1 . VAL   K  1 259 ? 66.38804  12.86808  46.86305  1.000 57.55286  ?  259 VAL   K CG1 1 
ATOM   16668 C CG2 . VAL   K  1 259 ? 65.74839  10.62648  47.85240  1.000 81.93037  ?  259 VAL   K CG2 1 
ATOM   16669 N N   . PHE   K  1 260 ? 64.24481  13.37594  44.23524  1.000 82.05984  ?  260 PHE   K N   1 
ATOM   16670 C CA  . PHE   K  1 260 ? 64.54382  13.95422  42.91981  1.000 142.59306 ?  260 PHE   K CA  1 
ATOM   16671 C C   . PHE   K  1 260 ? 63.70552  13.31560  41.83589  1.000 99.67123  ?  260 PHE   K C   1 
ATOM   16672 O O   . PHE   K  1 260 ? 63.95761  13.51889  40.64106  1.000 176.00921 ?  260 PHE   K O   1 
ATOM   16673 C CB  . PHE   K  1 260 ? 66.03058  13.82050  42.52499  1.000 95.17185  ?  260 PHE   K CB  1 
ATOM   16674 C CG  . PHE   K  1 260 ? 66.97990  14.51752  43.45318  1.000 112.89674 ?  260 PHE   K CG  1 
ATOM   16675 C CD1 . PHE   K  1 260 ? 66.64820  15.74078  44.00824  1.000 90.44475  ?  260 PHE   K CD1 1 
ATOM   16676 C CD2 . PHE   K  1 260 ? 68.20068  13.94843  43.77261  1.000 106.06484 ?  260 PHE   K CD2 1 
ATOM   16677 C CE1 . PHE   K  1 260 ? 67.51164  16.38974  44.87135  1.000 189.45835 ?  260 PHE   K CE1 1 
ATOM   16678 C CE2 . PHE   K  1 260 ? 69.07478  14.59658  44.63743  1.000 107.60712 ?  260 PHE   K CE2 1 
ATOM   16679 C CZ  . PHE   K  1 260 ? 68.72460  15.82216  45.18777  1.000 124.28936 ?  260 PHE   K CZ  1 
ATOM   16680 N N   . LYS   K  1 261 ? 62.79989  12.45142  42.30983  1.000 94.99286  ?  261 LYS   K N   1 
ATOM   16681 C CA  . LYS   K  1 261 ? 61.82249  11.60241  41.67505  1.000 104.95673 ?  261 LYS   K CA  1 
ATOM   16682 C C   . LYS   K  1 261 ? 60.40718  12.01191  42.10969  1.000 99.74860  ?  261 LYS   K C   1 
ATOM   16683 O O   . LYS   K  1 261 ? 59.51752  11.16241  42.14302  1.000 62.92211  ?  261 LYS   K O   1 
ATOM   16684 C CB  . LYS   K  1 261 ? 62.10990  10.14258  42.06893  1.000 91.51480  ?  261 LYS   K CB  1 
ATOM   16685 C CG  . LYS   K  1 261 ? 63.10406  9.37887   41.16502  1.000 114.28015 ?  261 LYS   K CG  1 
ATOM   16686 C CD  . LYS   K  1 261 ? 63.16030  7.91633   41.61307  1.000 86.80588  ?  261 LYS   K CD  1 
ATOM   16687 C CE  . LYS   K  1 261 ? 64.46850  7.15670   41.40013  1.000 92.62993  ?  261 LYS   K CE  1 
ATOM   16688 N NZ  . LYS   K  1 261 ? 65.19427  7.02256   42.70332  1.000 47.44564  ?  261 LYS   K NZ  1 
ATOM   16689 N N   . GLY   K  1 262 ? 60.20413  13.30758  42.51336  1.000 101.65195 ?  262 GLY   K N   1 
ATOM   16690 C CA  . GLY   K  1 262 ? 58.93291  13.66924  43.11098  1.000 46.24568  ?  262 GLY   K CA  1 
ATOM   16691 C C   . GLY   K  1 262 ? 57.77605  13.46310  42.16809  1.000 103.10730 ?  262 GLY   K C   1 
ATOM   16692 O O   . GLY   K  1 262 ? 57.89580  13.66116  40.96324  1.000 96.43124  ?  262 GLY   K O   1 
ATOM   16693 N N   . GLU   K  1 263 ? 56.65821  13.01949  42.71705  1.000 58.42936  ?  263 GLU   K N   1 
ATOM   16694 C CA  . GLU   K  1 263 ? 55.44750  12.82742  41.91397  1.000 92.83152  ?  263 GLU   K CA  1 
ATOM   16695 C C   . GLU   K  1 263 ? 55.62354  11.65930  40.94658  1.000 102.93740 ?  263 GLU   K C   1 
ATOM   16696 O O   . GLU   K  1 263 ? 55.08624  11.66249  39.82785  1.000 67.76831  ?  263 GLU   K O   1 
ATOM   16697 C CB  . GLU   K  1 263 ? 55.04197  14.11398  41.16487  1.000 56.85144  ?  263 GLU   K CB  1 
ATOM   16698 C CG  . GLU   K  1 263 ? 53.54384  14.35030  41.01766  1.000 92.48268  ?  263 GLU   K CG  1 
ATOM   16699 C CD  . GLU   K  1 263 ? 52.84121  14.73935  42.34738  1.000 85.73181  ?  263 GLU   K CD  1 
ATOM   16700 O OE1 . GLU   K  1 263 ? 53.49949  14.70896  43.41690  1.000 56.07822  ?  263 GLU   K OE1 1 
ATOM   16701 O OE2 . GLU   K  1 263 ? 51.62375  15.07575  42.32154  1.000 69.91192  -1 263 GLU   K OE2 1 
ATOM   16702 N N   . THR   K  1 264 ? 56.41001  10.67084  41.38521  1.000 46.44592  ?  264 THR   K N   1 
ATOM   16703 C CA  . THR   K  1 264 ? 56.47175  9.35442   40.77406  1.000 31.97504  ?  264 THR   K CA  1 
ATOM   16704 C C   . THR   K  1 264 ? 56.04670  8.31803   41.80016  1.000 47.22377  ?  264 THR   K C   1 
ATOM   16705 O O   . THR   K  1 264 ? 56.44262  8.39808   42.96605  1.000 38.30417  ?  264 THR   K O   1 
ATOM   16706 C CB  . THR   K  1 264 ? 57.88279  9.03155   40.31602  1.000 52.82095  ?  264 THR   K CB  1 
ATOM   16707 O OG1 . THR   K  1 264 ? 58.38015  10.11359  39.52588  1.000 103.89179 ?  264 THR   K OG1 1 
ATOM   16708 C CG2 . THR   K  1 264 ? 57.89648  7.72314   39.52936  1.000 39.80865  ?  264 THR   K CG2 1 
ATOM   16709 N N   . TYR   K  1 265 ? 55.24475  7.34539   41.37927  1.000 43.31139  ?  265 TYR   K N   1 
ATOM   16710 C CA  . TYR   K  1 265 ? 54.97321  6.22241   42.26676  1.000 33.82565  ?  265 TYR   K CA  1 
ATOM   16711 C C   . TYR   K  1 265 ? 56.19784  5.32311   42.37643  1.000 38.66437  ?  265 TYR   K C   1 
ATOM   16712 O O   . TYR   K  1 265 ? 56.99511  5.19621   41.43659  1.000 46.68367  ?  265 TYR   K O   1 
ATOM   16713 C CB  . TYR   K  1 265 ? 53.79253  5.37942   41.77743  1.000 29.90010  ?  265 TYR   K CB  1 
ATOM   16714 C CG  . TYR   K  1 265 ? 52.50068  6.13235   41.59929  1.000 48.75830  ?  265 TYR   K CG  1 
ATOM   16715 C CD1 . TYR   K  1 265 ? 51.82947  6.66128   42.68337  1.000 40.10811  ?  265 TYR   K CD1 1 
ATOM   16716 C CD2 . TYR   K  1 265 ? 51.94528  6.29380   40.34079  1.000 37.67124  ?  265 TYR   K CD2 1 
ATOM   16717 C CE1 . TYR   K  1 265 ? 50.62907  7.34617   42.51622  1.000 48.01891  ?  265 TYR   K CE1 1 
ATOM   16718 C CE2 . TYR   K  1 265 ? 50.76324  6.97221   40.15919  1.000 46.25330  ?  265 TYR   K CE2 1 
ATOM   16719 C CZ  . TYR   K  1 265 ? 50.10528  7.50064   41.25117  1.000 40.16433  ?  265 TYR   K CZ  1 
ATOM   16720 O OH  . TYR   K  1 265 ? 48.92527  8.18589   41.05952  1.000 43.49596  ?  265 TYR   K OH  1 
ATOM   16721 N N   . SER   K  1 266 ? 56.33399  4.69626   43.54810  1.000 44.77914  ?  266 SER   K N   1 
ATOM   16722 C CA  . SER   K  1 266 ? 57.24675  3.57721   43.76755  1.000 33.83741  ?  266 SER   K CA  1 
ATOM   16723 C C   . SER   K  1 266 ? 56.40580  2.44107   44.34842  1.000 47.34565  ?  266 SER   K C   1 
ATOM   16724 O O   . SER   K  1 266 ? 56.01034  2.49644   45.51880  1.000 37.88715  ?  266 SER   K O   1 
ATOM   16725 C CB  . SER   K  1 266 ? 58.39832  3.97136   44.69263  1.000 35.59867  ?  266 SER   K CB  1 
ATOM   16726 O OG  . SER   K  1 266 ? 59.11330  2.82566   45.12526  1.000 46.14864  ?  266 SER   K OG  1 
ATOM   16727 N N   . LEU   K  1 267 ? 56.11844  1.42409   43.52427  1.000 40.97899  ?  267 LEU   K N   1 
ATOM   16728 C CA  . LEU   K  1 267 ? 55.23901  0.33093   43.94363  1.000 50.56466  ?  267 LEU   K CA  1 
ATOM   16729 C C   . LEU   K  1 267 ? 55.66720  -0.26174  45.27961  1.000 40.34338  ?  267 LEU   K C   1 
ATOM   16730 O O   . LEU   K  1 267 ? 54.83866  -0.46647  46.17477  1.000 55.93985  ?  267 LEU   K O   1 
ATOM   16731 C CB  . LEU   K  1 267 ? 55.22406  -0.76615  42.88738  1.000 34.02237  ?  267 LEU   K CB  1 
ATOM   16732 C CG  . LEU   K  1 267 ? 54.36391  -0.60332  41.65170  1.000 53.62276  ?  267 LEU   K CG  1 
ATOM   16733 C CD1 . LEU   K  1 267 ? 54.54336  -1.88256  40.91338  1.000 45.69933  ?  267 LEU   K CD1 1 
ATOM   16734 C CD2 . LEU   K  1 267 ? 52.86936  -0.36148  42.00036  1.000 39.98499  ?  267 LEU   K CD2 1 
ATOM   16735 N N   . LYS   K  1 268 ? 56.96719  -0.56941  45.41025  1.000 61.18010  ?  268 LYS   K N   1 
ATOM   16736 C CA  . LYS   K  1 268 ? 57.52791  -1.11032  46.64926  1.000 40.03573  ?  268 LYS   K CA  1 
ATOM   16737 C C   . LYS   K  1 268 ? 57.12768  -0.26150  47.86430  1.000 58.96829  ?  268 LYS   K C   1 
ATOM   16738 O O   . LYS   K  1 268 ? 56.78180  -0.80506  48.92048  1.000 38.08901  ?  268 LYS   K O   1 
ATOM   16739 C CB  . LYS   K  1 268 ? 59.05310  -1.20980  46.48798  1.000 46.44269  ?  268 LYS   K CB  1 
ATOM   16740 C CG  . LYS   K  1 268 ? 59.88701  -1.37467  47.74656  1.000 59.35762  ?  268 LYS   K CG  1 
ATOM   16741 C CD  . LYS   K  1 268 ? 61.33346  -0.87372  47.50744  1.000 52.95865  ?  268 LYS   K CD  1 
ATOM   16742 C CE  . LYS   K  1 268 ? 62.17900  -0.90725  48.81743  1.000 65.54207  ?  268 LYS   K CE  1 
ATOM   16743 N NZ  . LYS   K  1 268 ? 63.35524  0.06021   48.75421  1.000 62.32415  ?  268 LYS   K NZ  1 
ATOM   16744 N N   . HIS   K  1 269 ? 57.11951  1.07258   47.71755  1.000 39.48357  ?  269 HIS   K N   1 
ATOM   16745 C CA  . HIS   K  1 269 ? 56.71821  1.96515   48.80506  1.000 23.98592  ?  269 HIS   K CA  1 
ATOM   16746 C C   . HIS   K  1 269 ? 55.20204  2.04149   48.93571  1.000 48.91669  ?  269 HIS   K C   1 
ATOM   16747 O O   . HIS   K  1 269 ? 54.65265  1.75538   50.00614  1.000 31.65302  ?  269 HIS   K O   1 
ATOM   16748 C CB  . HIS   K  1 269 ? 57.27503  3.37194   48.58299  1.000 31.64818  ?  269 HIS   K CB  1 
ATOM   16749 C CG  . HIS   K  1 269 ? 58.75886  3.46492   48.70840  1.000 35.69511  ?  269 HIS   K CG  1 
ATOM   16750 N ND1 . HIS   K  1 269 ? 59.61835  3.06874   47.70790  1.000 57.05927  ?  269 HIS   K ND1 1 
ATOM   16751 C CD2 . HIS   K  1 269 ? 59.53974  3.91835   49.71681  1.000 42.97012  ?  269 HIS   K CD2 1 
ATOM   16752 C CE1 . HIS   K  1 269 ? 60.86598  3.26551   48.09841  1.000 32.28115  ?  269 HIS   K CE1 1 
ATOM   16753 N NE2 . HIS   K  1 269 ? 60.84576  3.77997   49.31402  1.000 47.82781  ?  269 HIS   K NE2 1 
ATOM   16754 N N   . LEU   K  1 270 ? 54.51730  2.46885   47.85994  1.000 37.94169  ?  270 LEU   K N   1 
ATOM   16755 C CA  . LEU   K  1 270 ? 53.05298  2.54645   47.85945  1.000 33.19653  ?  270 LEU   K CA  1 
ATOM   16756 C C   . LEU   K  1 270 ? 52.42368  1.31128   48.50795  1.000 36.88439  ?  270 LEU   K C   1 
ATOM   16757 O O   . LEU   K  1 270 ? 51.63425  1.42760   49.45510  1.000 40.44058  ?  270 LEU   K O   1 
ATOM   16758 C CB  . LEU   K  1 270 ? 52.53491  2.71996   46.42800  1.000 39.91791  ?  270 LEU   K CB  1 
ATOM   16759 C CG  . LEU   K  1 270 ? 51.01786  2.79382   46.27005  1.000 36.98027  ?  270 LEU   K CG  1 
ATOM   16760 C CD1 . LEU   K  1 270 ? 50.44507  4.13747   46.76335  1.000 34.71526  ?  270 LEU   K CD1 1 
ATOM   16761 C CD2 . LEU   K  1 270 ? 50.62384  2.50809   44.82936  1.000 42.71051  ?  270 LEU   K CD2 1 
ATOM   16762 N N   . LEU   K  1 271 ? 52.80563  0.11604   48.04899  1.000 44.51064  ?  271 LEU   K N   1 
ATOM   16763 C CA  . LEU   K  1 271 ? 52.23824  -1.12988  48.55594  1.000 41.13753  ?  271 LEU   K CA  1 
ATOM   16764 C C   . LEU   K  1 271 ? 52.99685  -1.69663  49.74878  1.000 49.57019  ?  271 LEU   K C   1 
ATOM   16765 O O   . LEU   K  1 271 ? 52.71377  -2.82959  50.16053  1.000 39.13247  ?  271 LEU   K O   1 
ATOM   16766 C CB  . LEU   K  1 271 ? 52.17661  -2.17744  47.44319  1.000 31.60032  ?  271 LEU   K CB  1 
ATOM   16767 C CG  . LEU   K  1 271 ? 51.40379  -1.71463  46.20330  1.000 44.68968  ?  271 LEU   K CG  1 
ATOM   16768 C CD1 . LEU   K  1 271 ? 51.49826  -2.80255  45.16176  1.000 35.80650  ?  271 LEU   K CD1 1 
ATOM   16769 C CD2 . LEU   K  1 271 ? 49.93876  -1.34793  46.51955  1.000 29.33276  ?  271 LEU   K CD2 1 
ATOM   16770 N N   . ASN   K  1 272 ? 53.95404  -0.94559  50.30809  1.000 44.56095  ?  272 ASN   K N   1 
ATOM   16771 C CA  . ASN   K  1 272 ? 54.60852  -1.31905  51.57057  1.000 36.56144  ?  272 ASN   K CA  1 
ATOM   16772 C C   . ASN   K  1 272 ? 55.24533  -2.71300  51.48432  1.000 48.69833  ?  272 ASN   K C   1 
ATOM   16773 O O   . ASN   K  1 272 ? 55.10421  -3.54008  52.38373  1.000 55.49242  ?  272 ASN   K O   1 
ATOM   16774 C CB  . ASN   K  1 272 ? 53.61398  -1.23652  52.73676  1.000 58.47156  ?  272 ASN   K CB  1 
ATOM   16775 C CG  . ASN   K  1 272 ? 54.28718  -1.29692  54.09902  1.000 48.96256  ?  272 ASN   K CG  1 
ATOM   16776 O OD1 . ASN   K  1 272 ? 55.33382  -0.67303  54.33446  1.000 48.76639  ?  272 ASN   K OD1 1 
ATOM   16777 N ND2 . ASN   K  1 272 ? 53.68343  -2.05658  55.01084  1.000 55.19439  ?  272 ASN   K ND2 1 
ATOM   16778 N N   . ASN   K  1 273 ? 55.94085  -2.97383  50.36869  1.000 49.57684  ?  273 ASN   K N   1 
ATOM   16779 C CA  . ASN   K  1 273 ? 56.68878  -4.22205  50.14272  1.000 58.68323  ?  273 ASN   K CA  1 
ATOM   16780 C C   . ASN   K  1 273 ? 55.80867  -5.46399  50.21585  1.000 46.69247  ?  273 ASN   K C   1 
ATOM   16781 O O   . ASN   K  1 273 ? 56.26989  -6.52377  50.64262  1.000 55.48797  ?  273 ASN   K O   1 
ATOM   16782 C CB  . ASN   K  1 273 ? 57.85905  -4.36537  51.12042  1.000 53.17239  ?  273 ASN   K CB  1 
ATOM   16783 C CG  . ASN   K  1 273 ? 59.08098  -3.62953  50.65769  1.000 89.67593  ?  273 ASN   K CG  1 
ATOM   16784 O OD1 . ASN   K  1 273 ? 59.66382  -3.97215  49.62174  1.000 95.11278  ?  273 ASN   K OD1 1 
ATOM   16785 N ND2 . ASN   K  1 273 ? 59.47554  -2.59682  51.40578  1.000 92.33729  ?  273 ASN   K ND2 1 
ATOM   16786 N N   . ASP   K  1 274 ? 54.54809  -5.36754  49.79118  1.000 65.44843  ?  274 ASP   K N   1 
ATOM   16787 C CA  . ASP   K  1 274 ? 53.68280  -6.54063  49.84889  1.000 62.66701  ?  274 ASP   K CA  1 
ATOM   16788 C C   . ASP   K  1 274 ? 54.20466  -7.63568  48.91661  1.000 57.06456  ?  274 ASP   K C   1 
ATOM   16789 O O   . ASP   K  1 274 ? 54.71994  -7.33598  47.82753  1.000 57.89414  ?  274 ASP   K O   1 
ATOM   16790 C CB  . ASP   K  1 274 ? 52.24377  -6.18048  49.46797  1.000 59.25786  ?  274 ASP   K CB  1 
ATOM   16791 C CG  . ASP   K  1 274 ? 51.25950  -7.27295  49.83958  1.000 68.88865  ?  274 ASP   K CG  1 
ATOM   16792 O OD1 . ASP   K  1 274 ? 51.11667  -8.26317  49.07604  1.000 77.35775  ?  274 ASP   K OD1 1 
ATOM   16793 O OD2 . ASP   K  1 274 ? 50.65278  -7.15546  50.92840  1.000 91.08123  -1 274 ASP   K OD2 1 
ATOM   16794 N N   . PRO   K  1 275 ? 54.07478  -8.91026  49.29435  1.000 78.48368  ?  275 PRO   K N   1 
ATOM   16795 C CA  . PRO   K  1 275 ? 54.38128  -9.99524  48.33892  1.000 58.45667  ?  275 PRO   K CA  1 
ATOM   16796 C C   . PRO   K  1 275 ? 53.69589  -9.85909  46.98212  1.000 68.05844  ?  275 PRO   K C   1 
ATOM   16797 O O   . PRO   K  1 275 ? 54.28485  -10.29518 45.98779  1.000 81.37381  ?  275 PRO   K O   1 
ATOM   16798 C CB  . PRO   K  1 275 ? 53.92724  -11.25626 49.08088  1.000 60.68259  ?  275 PRO   K CB  1 
ATOM   16799 C CG  . PRO   K  1 275 ? 54.01130  -10.88111 50.53209  1.000 62.72900  ?  275 PRO   K CG  1 
ATOM   16800 C CD  . PRO   K  1 275 ? 53.70985  -9.41312  50.62716  1.000 66.66600  ?  275 PRO   K CD  1 
ATOM   16801 N N   . PHE   K  1 276 ? 52.49965  -9.24589  46.88802  1.000 63.03898  ?  276 PHE   K N   1 
ATOM   16802 C CA  . PHE   K  1 276 ? 51.86801  -9.03410  45.57800  1.000 53.37145  ?  276 PHE   K CA  1 
ATOM   16803 C C   . PHE   K  1 276 ? 52.56166  -7.97336  44.72926  1.000 70.46206  ?  276 PHE   K C   1 
ATOM   16804 O O   . PHE   K  1 276 ? 52.27104  -7.88702  43.52756  1.000 66.32035  ?  276 PHE   K O   1 
ATOM   16805 C CB  . PHE   K  1 276 ? 50.40161  -8.62180  45.71286  1.000 54.60970  ?  276 PHE   K CB  1 
ATOM   16806 C CG  . PHE   K  1 276 ? 49.52362  -9.66959  46.32291  1.000 70.12211  ?  276 PHE   K CG  1 
ATOM   16807 C CD1 . PHE   K  1 276 ? 49.75365  -11.01279 46.09202  1.000 63.12885  ?  276 PHE   K CD1 1 
ATOM   16808 C CD2 . PHE   K  1 276 ? 48.45575  -9.30580  47.12876  1.000 60.19503  ?  276 PHE   K CD2 1 
ATOM   16809 C CE1 . PHE   K  1 276 ? 48.92458  -11.97476 46.65325  1.000 74.90829  ?  276 PHE   K CE1 1 
ATOM   16810 C CE2 . PHE   K  1 276 ? 47.62493  -10.26019 47.70037  1.000 78.72127  ?  276 PHE   K CE2 1 
ATOM   16811 C CZ  . PHE   K  1 276 ? 47.86121  -11.59382 47.46729  1.000 69.21600  ?  276 PHE   K CZ  1 
ATOM   16812 N N   . THR   K  1 277 ? 53.44656  -7.16316  45.31380  1.000 57.39602  ?  277 THR   K N   1 
ATOM   16813 C CA  . THR   K  1 277 ? 54.03968  -6.04092  44.58430  1.000 63.11971  ?  277 THR   K CA  1 
ATOM   16814 C C   . THR   K  1 277 ? 54.56367  -6.40816  43.19934  1.000 54.69691  ?  277 THR   K C   1 
ATOM   16815 O O   . THR   K  1 277 ? 54.28321  -5.66224  42.24941  1.000 60.75804  ?  277 THR   K O   1 
ATOM   16816 C CB  . THR   K  1 277 ? 55.15857  -5.40730  45.42550  1.000 51.86364  ?  277 THR   K CB  1 
ATOM   16817 O OG1 . THR   K  1 277 ? 54.65191  -5.08466  46.72419  1.000 58.10028  ?  277 THR   K OG1 1 
ATOM   16818 C CG2 . THR   K  1 277 ? 55.66435  -4.12891  44.76967  1.000 41.85927  ?  277 THR   K CG2 1 
ATOM   16819 N N   . PRO   K  1 278 ? 55.30288  -7.51058  43.00325  1.000 81.01209  ?  278 PRO   K N   1 
ATOM   16820 C CA  . PRO   K  1 278 ? 55.83452  -7.78831  41.65629  1.000 53.70419  ?  278 PRO   K CA  1 
ATOM   16821 C C   . PRO   K  1 278 ? 54.76235  -7.92585  40.58788  1.000 67.71110  ?  278 PRO   K C   1 
ATOM   16822 O O   . PRO   K  1 278 ? 55.03373  -7.59129  39.42580  1.000 56.27354  ?  278 PRO   K O   1 
ATOM   16823 C CB  . PRO   K  1 278 ? 56.59971  -9.10715  41.83898  1.000 46.43938  ?  278 PRO   K CB  1 
ATOM   16824 C CG  . PRO   K  1 278 ? 56.86892  -9.21856  43.26442  1.000 50.21425  ?  278 PRO   K CG  1 
ATOM   16825 C CD  . PRO   K  1 278 ? 55.74587  -8.52499  43.97811  1.000 53.12418  ?  278 PRO   K CD  1 
ATOM   16826 N N   . GLN   K  1 279 ? 53.55580  -8.40584  40.94228  1.000 46.40128  ?  279 GLN   K N   1 
ATOM   16827 C CA  . GLN   K  1 279 ? 52.48626  -8.58073  39.95492  1.000 44.21545  ?  279 GLN   K CA  1 
ATOM   16828 C C   . GLN   K  1 279 ? 52.04817  -7.26213  39.31748  1.000 57.61757  ?  279 GLN   K C   1 
ATOM   16829 O O   . GLN   K  1 279 ? 51.47610  -7.27648  38.21650  1.000 56.00867  ?  279 GLN   K O   1 
ATOM   16830 C CB  . GLN   K  1 279 ? 51.26535  -9.26262  40.58773  1.000 41.65310  ?  279 GLN   K CB  1 
ATOM   16831 C CG  . GLN   K  1 279 ? 51.51432  -10.67713 41.11075  1.000 33.15567  ?  279 GLN   K CG  1 
ATOM   16832 C CD  . GLN   K  1 279 ? 50.23461  -11.38384 41.53232  1.000 72.68181  ?  279 GLN   K CD  1 
ATOM   16833 O OE1 . GLN   K  1 279 ? 49.24665  -11.41334 40.79039  1.000 58.51275  ?  279 GLN   K OE1 1 
ATOM   16834 N NE2 . GLN   K  1 279 ? 50.24965  -11.96017 42.72830  1.000 49.53665  ?  279 GLN   K NE2 1 
ATOM   16835 N N   . PHE   K  1 280 ? 52.29582  -6.13116  39.98543  1.000 52.74229  ?  280 PHE   K N   1 
ATOM   16836 C CA  . PHE   K  1 280 ? 51.86393  -4.82313  39.51441  1.000 54.32009  ?  280 PHE   K CA  1 
ATOM   16837 C C   . PHE   K  1 280 ? 52.98709  -4.04592  38.86393  1.000 52.64253  ?  280 PHE   K C   1 
ATOM   16838 O O   . PHE   K  1 280 ? 52.75355  -2.92802  38.37855  1.000 55.31602  ?  280 PHE   K O   1 
ATOM   16839 C CB  . PHE   K  1 280 ? 51.24534  -4.02453  40.66800  1.000 36.23383  ?  280 PHE   K CB  1 
ATOM   16840 C CG  . PHE   K  1 280 ? 49.93216  -4.57098  41.08607  1.000 66.15966  ?  280 PHE   K CG  1 
ATOM   16841 C CD1 . PHE   K  1 280 ? 48.76394  -4.19267  40.42694  1.000 46.85973  ?  280 PHE   K CD1 1 
ATOM   16842 C CD2 . PHE   K  1 280 ? 49.86482  -5.54415  42.06659  1.000 37.18395  ?  280 PHE   K CD2 1 
ATOM   16843 C CE1 . PHE   K  1 280 ? 47.55014  -4.74560  40.78710  1.000 61.57722  ?  280 PHE   K CE1 1 
ATOM   16844 C CE2 . PHE   K  1 280 ? 48.64789  -6.09903  42.43050  1.000 60.88851  ?  280 PHE   K CE2 1 
ATOM   16845 C CZ  . PHE   K  1 280 ? 47.49158  -5.70039  41.78757  1.000 53.26286  ?  280 PHE   K CZ  1 
ATOM   16846 N N   . GLU   K  1 281 ? 54.19157  -4.61485  38.84027  1.000 49.73094  ?  281 GLU   K N   1 
ATOM   16847 C CA  . GLU   K  1 281 ? 55.28365  -4.02882  38.08386  1.000 62.57512  ?  281 GLU   K CA  1 
ATOM   16848 C C   . GLU   K  1 281 ? 54.86614  -3.87148  36.62255  1.000 39.82249  ?  281 GLU   K C   1 
ATOM   16849 O O   . GLU   K  1 281 ? 54.28100  -4.78637  36.03664  1.000 59.51988  ?  281 GLU   K O   1 
ATOM   16850 C CB  . GLU   K  1 281 ? 56.52112  -4.91484  38.22310  1.000 43.09053  ?  281 GLU   K CB  1 
ATOM   16851 C CG  . GLU   K  1 281 ? 57.81820  -4.15132  38.21281  1.000 75.06832  ?  281 GLU   K CG  1 
ATOM   16852 C CD  . GLU   K  1 281 ? 58.05070  -3.36293  39.48835  1.000 143.27537 ?  281 GLU   K CD  1 
ATOM   16853 O OE1 . GLU   K  1 281 ? 57.75465  -3.86617  40.60753  1.000 62.41984  ?  281 GLU   K OE1 1 
ATOM   16854 O OE2 . GLU   K  1 281 ? 58.54600  -2.22517  39.35631  1.000 78.39393  -1 281 GLU   K OE2 1 
ATOM   16855 N N   . HIS   K  1 282 ? 55.10737  -2.68343  36.05824  1.000 57.69866  ?  282 HIS   K N   1 
ATOM   16856 C CA  . HIS   K  1 282 ? 54.73495  -2.29488  34.69761  1.000 81.28405  ?  282 HIS   K CA  1 
ATOM   16857 C C   . HIS   K  1 282 ? 53.23663  -2.06949  34.51708  1.000 68.86568  ?  282 HIS   K C   1 
ATOM   16858 O O   . HIS   K  1 282 ? 52.80004  -1.81428  33.38969  1.000 74.09190  ?  282 HIS   K O   1 
ATOM   16859 C CB  . HIS   K  1 282 ? 55.17289  -3.32254  33.64976  1.000 48.79146  ?  282 HIS   K CB  1 
ATOM   16860 C CG  . HIS   K  1 282 ? 56.64561  -3.56570  33.61575  1.000 95.53063  ?  282 HIS   K CG  1 
ATOM   16861 N ND1 . HIS   K  1 282 ? 57.54020  -2.64714  33.10754  1.000 80.24113  ?  282 HIS   K ND1 1 
ATOM   16862 C CD2 . HIS   K  1 282 ? 57.38173  -4.62906  34.01863  1.000 55.79874  ?  282 HIS   K CD2 1 
ATOM   16863 C CE1 . HIS   K  1 282 ? 58.76637  -3.12892  33.20804  1.000 64.13992  ?  282 HIS   K CE1 1 
ATOM   16864 N NE2 . HIS   K  1 282 ? 58.69864  -4.33094  33.75712  1.000 76.09873  ?  282 HIS   K NE2 1 
ATOM   16865 N N   . GLY   K  1 283 ? 52.43252  -2.16062  35.57952  1.000 56.00888  ?  283 GLY   K N   1 
ATOM   16866 C CA  . GLY   K  1 283 ? 51.00249  -1.92533  35.48683  1.000 35.56666  ?  283 GLY   K CA  1 
ATOM   16867 C C   . GLY   K  1 283 ? 50.65874  -0.44746  35.46017  1.000 47.74214  ?  283 GLY   K C   1 
ATOM   16868 O O   . GLY   K  1 283 ? 51.52313  0.38775   35.16627  1.000 46.78428  ?  283 GLY   K O   1 
ATOM   16869 N N   . SER   K  1 284 ? 49.41119  -0.09751  35.77109  1.000 46.27775  ?  284 SER   K N   1 
ATOM   16870 C CA  . SER   K  1 284 ? 48.98785  1.29755   35.69101  1.000 54.98347  ?  284 SER   K CA  1 
ATOM   16871 C C   . SER   K  1 284 ? 48.20807  1.66930   36.94073  1.000 48.99019  ?  284 SER   K C   1 
ATOM   16872 O O   . SER   K  1 284 ? 47.62200  0.81421   37.62154  1.000 41.92605  ?  284 SER   K O   1 
ATOM   16873 C CB  . SER   K  1 284 ? 48.13403  1.56912   34.43555  1.000 38.02862  ?  284 SER   K CB  1 
ATOM   16874 O OG  . SER   K  1 284 ? 47.15565  0.54202   34.27137  1.000 56.74935  ?  284 SER   K OG  1 
ATOM   16875 N N   . ILE   K  1 285 ? 48.19056  2.97015   37.22081  1.000 39.41845  ?  285 ILE   K N   1 
ATOM   16876 C CA  . ILE   K  1 285 ? 47.57917  3.51251   38.42749  1.000 38.16065  ?  285 ILE   K CA  1 
ATOM   16877 C C   . ILE   K  1 285 ? 46.77421  4.74946   38.04977  1.000 34.31816  ?  285 ILE   K C   1 
ATOM   16878 O O   . ILE   K  1 285 ? 47.28194  5.64164   37.35569  1.000 53.31302  ?  285 ILE   K O   1 
ATOM   16879 C CB  . ILE   K  1 285 ? 48.63683  3.88133   39.49405  1.000 41.56498  ?  285 ILE   K CB  1 
ATOM   16880 C CG1 . ILE   K  1 285 ? 49.37744  2.64794   40.03223  1.000 38.05456  ?  285 ILE   K CG1 1 
ATOM   16881 C CG2 . ILE   K  1 285 ? 47.99705  4.67504   40.60461  1.000 33.99720  ?  285 ILE   K CG2 1 
ATOM   16882 C CD1 . ILE   K  1 285 ? 50.58447  3.00095   40.90666  1.000 46.34398  ?  285 ILE   K CD1 1 
ATOM   16883 N N   . LEU   K  1 286 ? 45.52799  4.80334   38.51749  1.000 53.16049  ?  286 LEU   K N   1 
ATOM   16884 C CA  . LEU   K  1 286 ? 44.69216  5.99714   38.48690  1.000 36.02950  ?  286 LEU   K CA  1 
ATOM   16885 C C   . LEU   K  1 286 ? 44.50634  6.47796   39.92123  1.000 42.92945  ?  286 LEU   K C   1 
ATOM   16886 O O   . LEU   K  1 286 ? 44.16890  5.67600   40.80307  1.000 47.64437  ?  286 LEU   K O   1 
ATOM   16887 C CB  . LEU   K  1 286 ? 43.32575  5.70168   37.83329  1.000 51.21582  ?  286 LEU   K CB  1 
ATOM   16888 C CG  . LEU   K  1 286 ? 42.18374  6.66573   38.21800  1.000 46.87815  ?  286 LEU   K CG  1 
ATOM   16889 C CD1 . LEU   K  1 286 ? 42.42268  8.03249   37.62521  1.000 41.83830  ?  286 LEU   K CD1 1 
ATOM   16890 C CD2 . LEU   K  1 286 ? 40.81333  6.15921   37.80203  1.000 47.07586  ?  286 LEU   K CD2 1 
ATOM   16891 N N   . GLN   K  1 287 ? 44.71536  7.77711   40.15247  1.000 31.24930  ?  287 GLN   K N   1 
ATOM   16892 C CA  . GLN   K  1 287 ? 44.62277  8.35939   41.48841  1.000 45.31164  ?  287 GLN   K CA  1 
ATOM   16893 C C   . GLN   K  1 287 ? 43.66764  9.54831   41.47639  1.000 45.99173  ?  287 GLN   K C   1 
ATOM   16894 O O   . GLN   K  1 287 ? 43.77849  10.43910  40.62115  1.000 39.55930  ?  287 GLN   K O   1 
ATOM   16895 C CB  . GLN   K  1 287 ? 46.00307  8.79918   42.01368  1.000 34.35532  ?  287 GLN   K CB  1 
ATOM   16896 C CG  . GLN   K  1 287 ? 45.95070  9.47605   43.37477  1.000 42.26489  ?  287 GLN   K CG  1 
ATOM   16897 C CD  . GLN   K  1 287 ? 47.32066  9.73267   43.99613  1.000 39.52504  ?  287 GLN   K CD  1 
ATOM   16898 O OE1 . GLN   K  1 287 ? 48.36192  9.53384   43.36519  1.000 41.66364  ?  287 GLN   K OE1 1 
ATOM   16899 N NE2 . GLN   K  1 287 ? 47.31928  10.18438  45.25285  1.000 35.64087  ?  287 GLN   K NE2 1 
ATOM   16900 N N   . GLY   K  1 288 ? 42.74043  9.56421   42.43578  1.000 38.49965  ?  288 GLY   K N   1 
ATOM   16901 C CA  . GLY   K  1 288 ? 41.79968  10.66051  42.60027  1.000 30.32891  ?  288 GLY   K CA  1 
ATOM   16902 C C   . GLY   K  1 288 ? 41.97241  11.44320  43.89807  1.000 34.94669  ?  288 GLY   K C   1 
ATOM   16903 O O   . GLY   K  1 288 ? 42.55375  10.95928  44.87785  1.000 49.98374  ?  288 GLY   K O   1 
ATOM   16904 N N   . PHE   K  1 289 ? 41.47834  12.67364  43.90613  1.000 39.01987  ?  289 PHE   K N   1 
ATOM   16905 C CA  . PHE   K  1 289 ? 41.50477  13.54161  45.07283  1.000 45.57265  ?  289 PHE   K CA  1 
ATOM   16906 C C   . PHE   K  1 289 ? 40.07103  13.84720  45.47499  1.000 40.87270  ?  289 PHE   K C   1 
ATOM   16907 O O   . PHE   K  1 289 ? 39.26022  14.22426  44.62515  1.000 43.26563  ?  289 PHE   K O   1 
ATOM   16908 C CB  . PHE   K  1 289 ? 42.25921  14.83285  44.75756  1.000 34.61328  ?  289 PHE   K CB  1 
ATOM   16909 C CG  . PHE   K  1 289 ? 42.03311  15.94149  45.75311  1.000 40.29682  ?  289 PHE   K CG  1 
ATOM   16910 C CD1 . PHE   K  1 289 ? 42.39438  15.78477  47.08432  1.000 29.08398  ?  289 PHE   K CD1 1 
ATOM   16911 C CD2 . PHE   K  1 289 ? 41.48764  17.15314  45.35580  1.000 39.73743  ?  289 PHE   K CD2 1 
ATOM   16912 C CE1 . PHE   K  1 289 ? 42.20640  16.82416  48.01322  1.000 47.72663  ?  289 PHE   K CE1 1 
ATOM   16913 C CE2 . PHE   K  1 289 ? 41.30277  18.19157  46.27567  1.000 43.09282  ?  289 PHE   K CE2 1 
ATOM   16914 C CZ  . PHE   K  1 289 ? 41.66810  18.02518  47.60544  1.000 41.39261  ?  289 PHE   K CZ  1 
ATOM   16915 N N   . LEU   K  1 290 ? 39.76159  13.67245  46.75894  1.000 46.11148  ?  290 LEU   K N   1 
ATOM   16916 C CA  . LEU   K  1 290 ? 38.44513  13.98092  47.30639  1.000 45.48181  ?  290 LEU   K CA  1 
ATOM   16917 C C   . LEU   K  1 290 ? 38.47711  15.37377  47.94115  1.000 49.84986  ?  290 LEU   K C   1 
ATOM   16918 O O   . LEU   K  1 290 ? 39.26455  15.60742  48.86300  1.000 69.47547  ?  290 LEU   K O   1 
ATOM   16919 C CB  . LEU   K  1 290 ? 38.04296  12.92440  48.34027  1.000 38.61914  ?  290 LEU   K CB  1 
ATOM   16920 C CG  . LEU   K  1 290 ? 37.76851  11.45637  47.95723  1.000 46.37290  ?  290 LEU   K CG  1 
ATOM   16921 C CD1 . LEU   K  1 290 ? 39.04428  10.69669  47.61349  1.000 44.02036  ?  290 LEU   K CD1 1 
ATOM   16922 C CD2 . LEU   K  1 290 ? 36.99294  10.70341  49.05805  1.000 38.44279  ?  290 LEU   K CD2 1 
ATOM   16923 N N   . ASN   K  1 291 ? 37.62826  16.29661  47.45738  1.000 64.75743  ?  291 ASN   K N   1 
ATOM   16924 C CA  . ASN   K  1 291 ? 37.48995  17.61976  48.09057  1.000 52.17842  ?  291 ASN   K CA  1 
ATOM   16925 C C   . ASN   K  1 291 ? 36.98338  17.47857  49.51694  1.000 56.69864  ?  291 ASN   K C   1 
ATOM   16926 O O   . ASN   K  1 291 ? 36.44660  16.43815  49.91787  1.000 56.31654  ?  291 ASN   K O   1 
ATOM   16927 C CB  . ASN   K  1 291 ? 36.49749  18.53237  47.35698  1.000 79.23701  ?  291 ASN   K CB  1 
ATOM   16928 C CG  . ASN   K  1 291 ? 36.54550  18.36813  45.87193  1.000 90.20660  ?  291 ASN   K CG  1 
ATOM   16929 O OD1 . ASN   K  1 291 ? 35.95827  17.43284  45.31917  1.000 136.00913 ?  291 ASN   K OD1 1 
ATOM   16930 N ND2 . ASN   K  1 291 ? 37.24675  19.27452  45.20307  1.000 90.92229  ?  291 ASN   K ND2 1 
ATOM   16931 N N   . VAL   K  1 292 ? 37.11479  18.56531  50.28181  1.000 50.91119  ?  292 VAL   K N   1 
ATOM   16932 C CA  . VAL   K  1 292 ? 36.71287  18.47626  51.67916  1.000 78.88327  ?  292 VAL   K CA  1 
ATOM   16933 C C   . VAL   K  1 292 ? 35.20393  18.29338  51.80514  1.000 79.62416  ?  292 VAL   K C   1 
ATOM   16934 O O   . VAL   K  1 292 ? 34.72812  17.69339  52.77966  1.000 61.99910  ?  292 VAL   K O   1 
ATOM   16935 C CB  . VAL   K  1 292 ? 37.20207  19.69872  52.46579  1.000 77.20324  ?  292 VAL   K CB  1 
ATOM   16936 C CG1 . VAL   K  1 292 ? 37.36431  19.31018  53.93518  1.000 70.06160  ?  292 VAL   K CG1 1 
ATOM   16937 C CG2 . VAL   K  1 292 ? 38.51075  20.24269  51.85452  1.000 61.98085  ?  292 VAL   K CG2 1 
ATOM   16938 N N   . THR   K  1 293 ? 34.42962  18.76455  50.82281  1.000 55.45320  ?  293 THR   K N   1 
ATOM   16939 C CA  . THR   K  1 293 ? 32.97528  18.63286  50.85102  1.000 61.84206  ?  293 THR   K CA  1 
ATOM   16940 C C   . THR   K  1 293 ? 32.44556  17.38360  50.14113  1.000 89.10424  ?  293 THR   K C   1 
ATOM   16941 O O   . THR   K  1 293 ? 31.22544  17.25375  49.98508  1.000 76.35397  ?  293 THR   K O   1 
ATOM   16942 C CB  . THR   K  1 293 ? 32.31657  19.85196  50.20469  1.000 86.41386  ?  293 THR   K CB  1 
ATOM   16943 O OG1 . THR   K  1 293 ? 32.80121  20.00921  48.85380  1.000 64.43752  ?  293 THR   K OG1 1 
ATOM   16944 C CG2 . THR   K  1 293 ? 32.58837  21.09108  51.02466  1.000 55.11115  ?  293 THR   K CG2 1 
ATOM   16945 N N   . ALA   K  1 294 ? 33.31203  16.47629  49.69707  1.000 66.62285  ?  294 ALA   K N   1 
ATOM   16946 C CA  . ALA   K  1 294 ? 32.84850  15.34657  48.90610  1.000 59.97942  ?  294 ALA   K CA  1 
ATOM   16947 C C   . ALA   K  1 294 ? 32.33803  14.20267  49.79068  1.000 59.42810  ?  294 ALA   K C   1 
ATOM   16948 O O   . ALA   K  1 294 ? 32.61447  14.11104  50.99085  1.000 76.90319  ?  294 ALA   K O   1 
ATOM   16949 C CB  . ALA   K  1 294 ? 33.95516  14.83676  47.97722  1.000 58.32779  ?  294 ALA   K CB  1 
ATOM   16950 N N   . TYR   K  1 295 ? 31.52935  13.35406  49.17639  1.000 61.31453  ?  295 TYR   K N   1 
ATOM   16951 C CA  . TYR   K  1 295 ? 31.18535  12.07944  49.77389  1.000 68.76129  ?  295 TYR   K CA  1 
ATOM   16952 C C   . TYR   K  1 295 ? 32.47752  11.32611  50.08116  1.000 66.68799  ?  295 TYR   K C   1 
ATOM   16953 O O   . TYR   K  1 295 ? 33.37190  11.23920  49.23563  1.000 63.61310  ?  295 TYR   K O   1 
ATOM   16954 C CB  . TYR   K  1 295 ? 30.28978  11.33568  48.78152  1.000 41.97194  ?  295 TYR   K CB  1 
ATOM   16955 C CG  . TYR   K  1 295 ? 29.85678  9.92654   49.11089  1.000 71.76615  ?  295 TYR   K CG  1 
ATOM   16956 C CD1 . TYR   K  1 295 ? 28.68321  9.67539   49.84183  1.000 60.02042  ?  295 TYR   K CD1 1 
ATOM   16957 C CD2 . TYR   K  1 295 ? 30.57078  8.84207   48.61683  1.000 55.88387  ?  295 TYR   K CD2 1 
ATOM   16958 C CE1 . TYR   K  1 295 ? 28.26679  8.36149   50.11050  1.000 52.91858  ?  295 TYR   K CE1 1 
ATOM   16959 C CE2 . TYR   K  1 295 ? 30.17414  7.54371   48.87242  1.000 50.94144  ?  295 TYR   K CE2 1 
ATOM   16960 C CZ  . TYR   K  1 295 ? 29.02153  7.29726   49.61818  1.000 65.22962  ?  295 TYR   K CZ  1 
ATOM   16961 O OH  . TYR   K  1 295 ? 28.64070  5.98861   49.86818  1.000 56.23605  ?  295 TYR   K OH  1 
ATOM   16962 N N   . HIS   K  1 296 ? 32.61241  10.82097  51.30756  1.000 58.30437  ?  296 HIS   K N   1 
ATOM   16963 C CA  . HIS   K  1 296 ? 33.88800  10.24622  51.73265  1.000 66.53262  ?  296 HIS   K CA  1 
ATOM   16964 C C   . HIS   K  1 296 ? 33.82643  8.74512   52.02242  1.000 51.12119  ?  296 HIS   K C   1 
ATOM   16965 O O   . HIS   K  1 296 ? 34.70193  8.22171   52.73120  1.000 57.02176  ?  296 HIS   K O   1 
ATOM   16966 C CB  . HIS   K  1 296 ? 34.44467  11.00785  52.94469  1.000 55.51969  ?  296 HIS   K CB  1 
ATOM   16967 C CG  . HIS   K  1 296 ? 35.44605  12.06162  52.56713  1.000 65.41348  ?  296 HIS   K CG  1 
ATOM   16968 N ND1 . HIS   K  1 296 ? 35.07711  13.30536  52.10200  1.000 73.22938  ?  296 HIS   K ND1 1 
ATOM   16969 C CD2 . HIS   K  1 296 ? 36.80005  12.03367  52.52404  1.000 64.85979  ?  296 HIS   K CD2 1 
ATOM   16970 C CE1 . HIS   K  1 296 ? 36.15818  14.00341  51.80414  1.000 65.26186  ?  296 HIS   K CE1 1 
ATOM   16971 N NE2 . HIS   K  1 296 ? 37.21792  13.25578  52.05419  1.000 79.16805  ?  296 HIS   K NE2 1 
ATOM   16972 N N   . ARG   K  1 297 ? 32.84370  8.02904   51.47717  1.000 58.22072  ?  297 ARG   K N   1 
ATOM   16973 C CA  . ARG   K  1 297 ? 32.85007  6.58027   51.63098  1.000 53.64558  ?  297 ARG   K CA  1 
ATOM   16974 C C   . ARG   K  1 297 ? 33.51207  5.92626   50.42411  1.000 70.62287  ?  297 ARG   K C   1 
ATOM   16975 O O   . ARG   K  1 297 ? 33.73894  6.56393   49.39267  1.000 60.26897  ?  297 ARG   K O   1 
ATOM   16976 C CB  . ARG   K  1 297 ? 31.44206  6.03917   51.81567  1.000 57.52688  ?  297 ARG   K CB  1 
ATOM   16977 C CG  . ARG   K  1 297 ? 30.64370  6.76308   52.86911  1.000 62.54620  ?  297 ARG   K CG  1 
ATOM   16978 C CD  . ARG   K  1 297 ? 29.31385  6.05771   53.04746  1.000 59.40991  ?  297 ARG   K CD  1 
ATOM   16979 N NE  . ARG   K  1 297 ? 28.98500  5.90976   54.45981  1.000 76.91687  ?  297 ARG   K NE  1 
ATOM   16980 C CZ  . ARG   K  1 297 ? 28.97924  4.74961   55.09761  1.000 69.23727  ?  297 ARG   K CZ  1 
ATOM   16981 N NH1 . ARG   K  1 297 ? 29.22012  3.61016   54.45742  1.000 77.61245  ?  297 ARG   K NH1 1 
ATOM   16982 N NH2 . ARG   K  1 297 ? 28.72003  4.73046   56.40401  1.000 112.91443 ?  297 ARG   K NH2 1 
ATOM   16983 N N   . TRP   K  1 298 ? 33.85063  4.64326   50.57995  1.000 54.48023  ?  298 TRP   K N   1 
ATOM   16984 C CA  . TRP   K  1 298 ? 34.47248  3.84709   49.53399  1.000 52.32860  ?  298 TRP   K CA  1 
ATOM   16985 C C   . TRP   K  1 298 ? 33.46578  2.83551   49.00540  1.000 60.24837  ?  298 TRP   K C   1 
ATOM   16986 O O   . TRP   K  1 298 ? 32.75355  2.18722   49.78199  1.000 64.28606  ?  298 TRP   K O   1 
ATOM   16987 C CB  . TRP   K  1 298 ? 35.70252  3.07517   50.03797  1.000 46.50749  ?  298 TRP   K CB  1 
ATOM   16988 C CG  . TRP   K  1 298 ? 36.65366  3.80406   50.94435  1.000 57.23893  ?  298 TRP   K CG  1 
ATOM   16989 C CD1 . TRP   K  1 298 ? 36.85517  5.16009   51.03647  1.000 52.50936  ?  298 TRP   K CD1 1 
ATOM   16990 C CD2 . TRP   K  1 298 ? 37.54678  3.20015   51.89766  1.000 46.62141  ?  298 TRP   K CD2 1 
ATOM   16991 N NE1 . TRP   K  1 298 ? 37.80790  5.43107   52.00113  1.000 43.91830  ?  298 TRP   K NE1 1 
ATOM   16992 C CE2 . TRP   K  1 298 ? 38.25122  4.24545   52.53388  1.000 50.21625  ?  298 TRP   K CE2 1 
ATOM   16993 C CE3 . TRP   K  1 298 ? 37.80272  1.87658   52.28597  1.000 39.68436  ?  298 TRP   K CE3 1 
ATOM   16994 C CZ2 . TRP   K  1 298 ? 39.19676  4.00439   53.53293  1.000 55.34179  ?  298 TRP   K CZ2 1 
ATOM   16995 C CZ3 . TRP   K  1 298 ? 38.73992  1.64112   53.26458  1.000 61.58794  ?  298 TRP   K CZ3 1 
ATOM   16996 C CH2 . TRP   K  1 298 ? 39.42808  2.69900   53.87996  1.000 53.14331  ?  298 TRP   K CH2 1 
ATOM   16997 N N   . HIS   K  1 299 ? 33.44337  2.67381   47.68903  1.000 66.92644  ?  299 HIS   K N   1 
ATOM   16998 C CA  . HIS   K  1 299 ? 32.62201  1.67297   47.03079  1.000 75.80450  ?  299 HIS   K CA  1 
ATOM   16999 C C   . HIS   K  1 299 ? 33.51520  0.66137   46.32641  1.000 65.95952  ?  299 HIS   K C   1 
ATOM   17000 O O   . HIS   K  1 299 ? 34.63230  0.98650   45.90817  1.000 68.05312  ?  299 HIS   K O   1 
ATOM   17001 C CB  . HIS   K  1 299 ? 31.65901  2.30371   46.01272  1.000 55.13686  ?  299 HIS   K CB  1 
ATOM   17002 C CG  . HIS   K  1 299 ? 30.59073  3.15419   46.63090  1.000 72.05537  ?  299 HIS   K CG  1 
ATOM   17003 N ND1 . HIS   K  1 299 ? 29.62882  3.80371   45.88582  1.000 65.10013  ?  299 HIS   K ND1 1 
ATOM   17004 C CD2 . HIS   K  1 299 ? 30.34449  3.47146   47.92417  1.000 65.40207  ?  299 HIS   K CD2 1 
ATOM   17005 C CE1 . HIS   K  1 299 ? 28.83586  4.48319   46.69539  1.000 78.83034  ?  299 HIS   K CE1 1 
ATOM   17006 N NE2 . HIS   K  1 299 ? 29.24924  4.29750   47.93771  1.000 67.19127  ?  299 HIS   K NE2 1 
ATOM   17007 N N   . ALA   K  1 300 ? 33.00537  -0.56787  46.18854  1.000 67.79669  ?  300 ALA   K N   1 
ATOM   17008 C CA  . ALA   K  1 300 ? 33.77177  -1.63161  45.54194  1.000 72.83220  ?  300 ALA   K CA  1 
ATOM   17009 C C   . ALA   K  1 300 ? 33.86837  -1.36495  44.04488  1.000 65.81710  ?  300 ALA   K C   1 
ATOM   17010 O O   . ALA   K  1 300 ? 32.84332  -1.11731  43.39773  1.000 76.01715  ?  300 ALA   K O   1 
ATOM   17011 C CB  . ALA   K  1 300 ? 33.12297  -2.98741  45.78893  1.000 61.37164  ?  300 ALA   K CB  1 
ATOM   17012 N N   . PRO   K  1 301 ? 35.07155  -1.39202  43.46100  1.000 85.96368  ?  301 PRO   K N   1 
ATOM   17013 C CA  . PRO   K  1 301 ? 35.21444  -1.06585  42.02892  1.000 71.80445  ?  301 PRO   K CA  1 
ATOM   17014 C C   . PRO   K  1 301 ? 34.87423  -2.21397  41.08685  1.000 92.59077  ?  301 PRO   K C   1 
ATOM   17015 O O   . PRO   K  1 301 ? 34.73239  -1.97585  39.87814  1.000 76.99036  ?  301 PRO   K O   1 
ATOM   17016 C CB  . PRO   K  1 301 ? 36.69800  -0.67555  41.91187  1.000 80.70221  ?  301 PRO   K CB  1 
ATOM   17017 C CG  . PRO   K  1 301 ? 37.37274  -1.47068  42.99134  1.000 77.95178  ?  301 PRO   K CG  1 
ATOM   17018 C CD  . PRO   K  1 301 ? 36.36720  -1.63437  44.12321  1.000 63.26176  ?  301 PRO   K CD  1 
ATOM   17019 N N   . VAL   K  1 302 ? 34.74369  -3.44075  41.60237  1.000 77.02891  ?  302 VAL   K N   1 
ATOM   17020 C CA  . VAL   K  1 302 ? 34.45997  -4.63376  40.80839  1.000 101.86122 ?  302 VAL   K CA  1 
ATOM   17021 C C   . VAL   K  1 302 ? 33.64178  -5.59843  41.65772  1.000 76.27397  ?  302 VAL   K C   1 
ATOM   17022 O O   . VAL   K  1 302 ? 33.58994  -5.48808  42.88326  1.000 92.94606  ?  302 VAL   K O   1 
ATOM   17023 C CB  . VAL   K  1 302 ? 35.74749  -5.35113  40.33155  1.000 76.03178  ?  302 VAL   K CB  1 
ATOM   17024 C CG1 . VAL   K  1 302 ? 36.55611  -4.46243  39.40351  1.000 100.29905 ?  302 VAL   K CG1 1 
ATOM   17025 C CG2 . VAL   K  1 302 ? 36.57458  -5.82521  41.54354  1.000 74.71953  ?  302 VAL   K CG2 1 
ATOM   17026 N N   . ASN   K  1 303 ? 33.00040  -6.56163  40.99722  1.000 90.23293  ?  303 ASN   K N   1 
ATOM   17027 C CA  . ASN   K  1 303 ? 32.54860  -7.75309  41.70710  1.000 75.10476  ?  303 ASN   K CA  1 
ATOM   17028 C C   . ASN   K  1 303 ? 33.76930  -8.61035  42.01070  1.000 94.40742  ?  303 ASN   K C   1 
ATOM   17029 O O   . ASN   K  1 303 ? 34.55412  -8.92566  41.10513  1.000 89.90936  ?  303 ASN   K O   1 
ATOM   17030 C CB  . ASN   K  1 303 ? 31.54869  -8.55952  40.87470  1.000 93.93200  ?  303 ASN   K CB  1 
ATOM   17031 C CG  . ASN   K  1 303 ? 30.35869  -7.73720  40.39504  1.000 86.67113  ?  303 ASN   K CG  1 
ATOM   17032 O OD1 . ASN   K  1 303 ? 30.10280  -6.61666  40.85405  1.000 91.37838  ?  303 ASN   K OD1 1 
ATOM   17033 N ND2 . ASN   K  1 303 ? 29.61918  -8.30636  39.45878  1.000 89.43106  ?  303 ASN   K ND2 1 
ATOM   17034 N N   . GLY   K  1 304 ? 33.95958  -8.97048  43.27375  1.000 75.21594  ?  304 GLY   K N   1 
ATOM   17035 C CA  . GLY   K  1 304 ? 35.13135  -9.76297  43.58102  1.000 61.98816  ?  304 GLY   K CA  1 
ATOM   17036 C C   . GLY   K  1 304 ? 35.24635  -10.06635 45.05446  1.000 78.51470  ?  304 GLY   K C   1 
ATOM   17037 O O   . GLY   K  1 304 ? 34.33489  -9.80295  45.84764  1.000 81.33043  ?  304 GLY   K O   1 
ATOM   17038 N N   . THR   K  1 305 ? 36.40556  -10.61921 45.40165  1.000 89.19413  ?  305 THR   K N   1 
ATOM   17039 C CA  . THR   K  1 305 ? 36.70417  -11.06853 46.75352  1.000 90.49292  ?  305 THR   K CA  1 
ATOM   17040 C C   . THR   K  1 305 ? 37.81490  -10.21673 47.35820  1.000 112.42535 ?  305 THR   K C   1 
ATOM   17041 O O   . THR   K  1 305 ? 38.81431  -9.90601  46.68914  1.000 77.29894  ?  305 THR   K O   1 
ATOM   17042 C CB  . THR   K  1 305 ? 37.12447  -12.53984 46.74584  1.000 80.11279  ?  305 THR   K CB  1 
ATOM   17043 O OG1 . THR   K  1 305 ? 36.25701  -13.26428 45.86445  1.000 97.18425  ?  305 THR   K OG1 1 
ATOM   17044 C CG2 . THR   K  1 305 ? 37.03855  -13.12070 48.14706  1.000 79.89986  ?  305 THR   K CG2 1 
ATOM   17045 N N   . ILE   K  1 306 ? 37.63335  -9.83099  48.62008  1.000 74.82449  ?  306 ILE   K N   1 
ATOM   17046 C CA  . ILE   K  1 306 ? 38.67368  -9.09293  49.32136  1.000 87.64984  ?  306 ILE   K CA  1 
ATOM   17047 C C   . ILE   K  1 306 ? 39.78833  -10.07246 49.63619  1.000 88.28904  ?  306 ILE   K C   1 
ATOM   17048 O O   . ILE   K  1 306 ? 39.58031  -11.04751 50.36560  1.000 91.34439  ?  306 ILE   K O   1 
ATOM   17049 C CB  . ILE   K  1 306 ? 38.13407  -8.44250  50.60060  1.000 83.91884  ?  306 ILE   K CB  1 
ATOM   17050 C CG1 . ILE   K  1 306 ? 36.84191  -7.65913  50.32514  1.000 71.32154  ?  306 ILE   K CG1 1 
ATOM   17051 C CG2 . ILE   K  1 306 ? 39.22034  -7.56797  51.23882  1.000 79.61265  ?  306 ILE   K CG2 1 
ATOM   17052 C CD1 . ILE   K  1 306 ? 36.94624  -6.59748  49.22437  1.000 78.07921  ?  306 ILE   K CD1 1 
ATOM   17053 N N   . VAL   K  1 307 ? 40.96263  -9.84013  49.06649  1.000 67.95169  ?  307 VAL   K N   1 
ATOM   17054 C CA  . VAL   K  1 307 ? 42.06689  -10.75836 49.28494  1.000 61.83670  ?  307 VAL   K CA  1 
ATOM   17055 C C   . VAL   K  1 307 ? 42.84210  -10.40383 50.54865  1.000 70.55394  ?  307 VAL   K C   1 
ATOM   17056 O O   . VAL   K  1 307 ? 43.17352  -11.29223 51.33859  1.000 69.05744  ?  307 VAL   K O   1 
ATOM   17057 C CB  . VAL   K  1 307 ? 42.98137  -10.79473 48.04802  1.000 77.75931  ?  307 VAL   K CB  1 
ATOM   17058 C CG1 . VAL   K  1 307 ? 44.13769  -11.75146 48.28317  1.000 51.73430  ?  307 VAL   K CG1 1 
ATOM   17059 C CG2 . VAL   K  1 307 ? 42.19338  -11.18900 46.79917  1.000 62.80576  ?  307 VAL   K CG2 1 
ATOM   17060 N N   . LYS   K  1 308 ? 43.09095  -9.11159  50.77949  1.000 78.72142  ?  308 LYS   K N   1 
ATOM   17061 C CA  . LYS   K  1 308 ? 44.04186  -8.67930  51.80030  1.000 69.34035  ?  308 LYS   K CA  1 
ATOM   17062 C C   . LYS   K  1 308 ? 43.85248  -7.19646  52.08437  1.000 82.86399  ?  308 LYS   K C   1 
ATOM   17063 O O   . LYS   K  1 308 ? 43.78460  -6.38722  51.15026  1.000 66.03424  ?  308 LYS   K O   1 
ATOM   17064 C CB  . LYS   K  1 308 ? 45.47004  -8.93790  51.32750  1.000 66.15640  ?  308 LYS   K CB  1 
ATOM   17065 C CG  . LYS   K  1 308 ? 46.55795  -8.91879  52.38652  1.000 57.49751  ?  308 LYS   K CG  1 
ATOM   17066 C CD  . LYS   K  1 308 ? 47.88524  -9.01618  51.63048  1.000 68.35494  ?  308 LYS   K CD  1 
ATOM   17067 C CE  . LYS   K  1 308 ? 49.05862  -9.45828  52.49331  1.000 88.29803  ?  308 LYS   K CE  1 
ATOM   17068 N NZ  . LYS   K  1 308 ? 50.17450  -9.86146  51.56537  1.000 99.94390  ?  308 LYS   K NZ  1 
ATOM   17069 N N   . ILE   K  1 309 ? 43.78464  -6.84866  53.36843  1.000 56.01709  ?  309 ILE   K N   1 
ATOM   17070 C CA  . ILE   K  1 309 ? 43.66889  -5.47050  53.83116  1.000 63.09552  ?  309 ILE   K CA  1 
ATOM   17071 C C   . ILE   K  1 309 ? 44.85426  -5.19728  54.74290  1.000 55.54327  ?  309 ILE   K C   1 
ATOM   17072 O O   . ILE   K  1 309 ? 45.04012  -5.91049  55.73482  1.000 64.11824  ?  309 ILE   K O   1 
ATOM   17073 C CB  . ILE   K  1 309 ? 42.36090  -5.22725  54.59296  1.000 47.54590  ?  309 ILE   K CB  1 
ATOM   17074 C CG1 . ILE   K  1 309 ? 41.14800  -5.52608  53.72491  1.000 68.23589  ?  309 ILE   K CG1 1 
ATOM   17075 C CG2 . ILE   K  1 309 ? 42.32559  -3.79407  55.11595  1.000 50.20096  ?  309 ILE   K CG2 1 
ATOM   17076 C CD1 . ILE   K  1 309 ? 39.88373  -5.62859  54.53042  1.000 48.93344  ?  309 ILE   K CD1 1 
ATOM   17077 N N   . ILE   K  1 310 ? 45.64685  -4.16844  54.42352  1.000 53.62119  ?  310 ILE   K N   1 
ATOM   17078 C CA  . ILE   K  1 310 ? 46.82869  -3.82212  55.20765  1.000 37.49907  ?  310 ILE   K CA  1 
ATOM   17079 C C   . ILE   K  1 310 ? 46.75581  -2.36076  55.61706  1.000 54.91085  ?  310 ILE   K C   1 
ATOM   17080 O O   . ILE   K  1 310 ? 46.56985  -1.48010  54.76768  1.000 47.90504  ?  310 ILE   K O   1 
ATOM   17081 C CB  . ILE   K  1 310 ? 48.13754  -4.06471  54.43878  1.000 54.88844  ?  310 ILE   K CB  1 
ATOM   17082 C CG1 . ILE   K  1 310 ? 48.16480  -5.46403  53.83317  1.000 55.97917  ?  310 ILE   K CG1 1 
ATOM   17083 C CG2 . ILE   K  1 310 ? 49.30520  -3.82804  55.36756  1.000 42.32446  ?  310 ILE   K CG2 1 
ATOM   17084 C CD1 . ILE   K  1 310 ? 48.18919  -5.45443  52.32019  1.000 60.35045  ?  310 ILE   K CD1 1 
ATOM   17085 N N   . ASN   K  1 311 ? 46.95908  -2.09271  56.90095  1.000 45.89440  ?  311 ASN   K N   1 
ATOM   17086 C CA  . ASN   K  1 311 ? 46.97348  -0.72302  57.39158  1.000 42.70658  ?  311 ASN   K CA  1 
ATOM   17087 C C   . ASN   K  1 311 ? 48.40978  -0.30501  57.65835  1.000 32.06331  ?  311 ASN   K C   1 
ATOM   17088 O O   . ASN   K  1 311 ? 49.13142  -0.96670  58.40955  1.000 59.07626  ?  311 ASN   K O   1 
ATOM   17089 C CB  . ASN   K  1 311 ? 46.09230  -0.57205  58.62498  1.000 27.46129  ?  311 ASN   K CB  1 
ATOM   17090 C CG  . ASN   K  1 311 ? 44.61780  -0.44936  58.24955  1.000 73.18430  ?  311 ASN   K CG  1 
ATOM   17091 O OD1 . ASN   K  1 311 ? 44.20836  0.52878   57.60855  1.000 53.17539  ?  311 ASN   K OD1 1 
ATOM   17092 N ND2 . ASN   K  1 311 ? 43.82567  -1.45452  58.60974  1.000 55.37894  ?  311 ASN   K ND2 1 
ATOM   17093 N N   . VAL   K  1 312 ? 48.83362  0.76996   57.00507  1.000 35.43472  ?  312 VAL   K N   1 
ATOM   17094 C CA  . VAL   K  1 312 ? 50.22861  1.17394   56.99585  1.000 33.88042  ?  312 VAL   K CA  1 
ATOM   17095 C C   . VAL   K  1 312 ? 50.35771  2.51818   57.70758  1.000 32.72626  ?  312 VAL   K C   1 
ATOM   17096 O O   . VAL   K  1 312 ? 49.75710  3.50930   57.27949  1.000 57.62942  ?  312 VAL   K O   1 
ATOM   17097 C CB  . VAL   K  1 312 ? 50.79153  1.24880   55.56555  1.000 37.44631  ?  312 VAL   K CB  1 
ATOM   17098 C CG1 . VAL   K  1 312 ? 52.32343  1.38311   55.61351  1.000 23.74316  ?  312 VAL   K CG1 1 
ATOM   17099 C CG2 . VAL   K  1 312 ? 50.40074  0.00036   54.78230  1.000 30.14240  ?  312 VAL   K CG2 1 
ATOM   17100 N N   . PRO   K  1 313 ? 51.11054  2.59800   58.79776  1.000 46.31844  ?  313 PRO   K N   1 
ATOM   17101 C CA  . PRO   K  1 313 ? 51.40453  3.90670   59.40150  1.000 42.00126  ?  313 PRO   K CA  1 
ATOM   17102 C C   . PRO   K  1 313 ? 52.28505  4.72776   58.47448  1.000 45.68133  ?  313 PRO   K C   1 
ATOM   17103 O O   . PRO   K  1 313 ? 53.09100  4.18676   57.70968  1.000 40.91963  ?  313 PRO   K O   1 
ATOM   17104 C CB  . PRO   K  1 313 ? 52.15909  3.55517   60.69475  1.000 25.04035  ?  313 PRO   K CB  1 
ATOM   17105 C CG  . PRO   K  1 313 ? 51.98222  2.03617   60.88234  1.000 30.88900  ?  313 PRO   K CG  1 
ATOM   17106 C CD  . PRO   K  1 313 ? 51.73609  1.47245   59.50975  1.000 27.05994  ?  313 PRO   K CD  1 
ATOM   17107 N N   . GLY   K  1 314 ? 52.13465  6.04629   58.54985  1.000 38.39275  ?  314 GLY   K N   1 
ATOM   17108 C CA  . GLY   K  1 314 ? 52.90315  6.89966   57.67398  1.000 30.85420  ?  314 GLY   K CA  1 
ATOM   17109 C C   . GLY   K  1 314 ? 52.86380  8.36128   58.05021  1.000 47.81701  ?  314 GLY   K C   1 
ATOM   17110 O O   . GLY   K  1 314 ? 52.63228  8.72186   59.20709  1.000 39.06805  ?  314 GLY   K O   1 
ATOM   17111 N N   . THR   K  1 315 ? 53.11166  9.20451   57.05229  1.000 30.28050  ?  315 THR   K N   1 
ATOM   17112 C CA  . THR   K  1 315 ? 53.10796  10.64443  57.23698  1.000 32.63211  ?  315 THR   K CA  1 
ATOM   17113 C C   . THR   K  1 315 ? 51.67723  11.19708  57.22111  1.000 40.96257  ?  315 THR   K C   1 
ATOM   17114 O O   . THR   K  1 315 ? 50.71881  10.52909  56.81770  1.000 33.14596  ?  315 THR   K O   1 
ATOM   17115 C CB  . THR   K  1 315 ? 53.94343  11.32291  56.14549  1.000 32.25457  ?  315 THR   K CB  1 
ATOM   17116 O OG1 . THR   K  1 315 ? 53.29304  11.19091  54.86520  1.000 26.03387  ?  315 THR   K OG1 1 
ATOM   17117 C CG2 . THR   K  1 315 ? 55.26542  10.66667  56.04559  1.000 22.74588  ?  315 THR   K CG2 1 
ATOM   17118 N N   . TYR   K  1 316 ? 51.56014  12.44580  57.66548  1.000 33.46166  ?  316 TYR   K N   1 
ATOM   17119 C CA  . TYR   K  1 316 ? 50.39303  13.32773  57.65995  1.000 33.02146  ?  316 TYR   K CA  1 
ATOM   17120 C C   . TYR   K  1 316 ? 50.69712  14.66522  56.99905  1.000 28.04640  ?  316 TYR   K C   1 
ATOM   17121 O O   . TYR   K  1 316 ? 49.83772  15.22047  56.30818  1.000 37.90842  ?  316 TYR   K O   1 
ATOM   17122 C CB  . TYR   K  1 316 ? 49.87492  13.57359  59.11042  1.000 27.96692  ?  316 TYR   K CB  1 
ATOM   17123 C CG  . TYR   K  1 316 ? 49.51008  12.29211  59.80946  1.000 38.71310  ?  316 TYR   K CG  1 
ATOM   17124 C CD1 . TYR   K  1 316 ? 48.27745  11.67392  59.57280  1.000 40.09225  ?  316 TYR   K CD1 1 
ATOM   17125 C CD2 . TYR   K  1 316 ? 50.41553  11.66722  60.66326  1.000 32.81178  ?  316 TYR   K CD2 1 
ATOM   17126 C CE1 . TYR   K  1 316 ? 47.94056  10.47058  60.18491  1.000 31.73098  ?  316 TYR   K CE1 1 
ATOM   17127 C CE2 . TYR   K  1 316 ? 50.09702  10.46391  61.29170  1.000 24.99998  ?  316 TYR   K CE2 1 
ATOM   17128 C CZ  . TYR   K  1 316 ? 48.85856  9.87268   61.04866  1.000 42.78430  ?  316 TYR   K CZ  1 
ATOM   17129 O OH  . TYR   K  1 316 ? 48.55512  8.68081   61.66958  1.000 34.05763  ?  316 TYR   K OH  1 
ATOM   17130 N N   . PHE   K  1 317 ? 51.91250  15.19564  57.17702  1.000 48.42883  ?  317 PHE   K N   1 
ATOM   17131 C CA  . PHE   K  1 317 ? 52.20299  16.56722  56.77887  1.000 29.67847  ?  317 PHE   K CA  1 
ATOM   17132 C C   . PHE   K  1 317 ? 53.40310  16.66029  55.84634  1.000 51.34834  ?  317 PHE   K C   1 
ATOM   17133 O O   . PHE   K  1 317 ? 54.05569  17.71218  55.78451  1.000 39.27973  ?  317 PHE   K O   1 
ATOM   17134 C CB  . PHE   K  1 317 ? 52.41935  17.44024  58.01464  1.000 29.55770  ?  317 PHE   K CB  1 
ATOM   17135 C CG  . PHE   K  1 317 ? 51.20195  17.54769  58.88239  1.000 49.70080  ?  317 PHE   K CG  1 
ATOM   17136 C CD1 . PHE   K  1 317 ? 50.10541  18.28903  58.46185  1.000 30.35806  ?  317 PHE   K CD1 1 
ATOM   17137 C CD2 . PHE   K  1 317 ? 51.14152  16.88536  60.10477  1.000 45.46419  ?  317 PHE   K CD2 1 
ATOM   17138 C CE1 . PHE   K  1 317 ? 48.97507  18.39009  59.25289  1.000 45.66707  ?  317 PHE   K CE1 1 
ATOM   17139 C CE2 . PHE   K  1 317 ? 50.01716  16.97856  60.89716  1.000 38.25665  ?  317 PHE   K CE2 1 
ATOM   17140 C CZ  . PHE   K  1 317 ? 48.92794  17.73221  60.46641  1.000 39.66327  ?  317 PHE   K CZ  1 
ATOM   17141 N N   . ALA   K  1 318 ? 53.69792  15.58652  55.10221  1.000 26.18768  ?  318 ALA   K N   1 
ATOM   17142 C CA  . ALA   K  1 318 ? 54.84473  15.56160  54.19271  1.000 23.06322  ?  318 ALA   K CA  1 
ATOM   17143 C C   . ALA   K  1 318 ? 54.39669  15.95730  52.79286  1.000 27.87894  ?  318 ALA   K C   1 
ATOM   17144 O O   . ALA   K  1 318 ? 53.63246  15.22797  52.15529  1.000 32.79576  ?  318 ALA   K O   1 
ATOM   17145 C CB  . ALA   K  1 318 ? 55.48663  14.17774  54.16529  1.000 16.58517  ?  318 ALA   K CB  1 
ATOM   17146 N N   . GLN   K  1 319 ? 54.88063  17.09884  52.30224  1.000 35.31003  ?  319 GLN   K N   1 
ATOM   17147 C CA  . GLN   K  1 319 ? 54.70870  17.41223  50.89103  1.000 31.79115  ?  319 GLN   K CA  1 
ATOM   17148 C C   . GLN   K  1 319 ? 55.93039  16.91316  50.11901  1.000 29.88630  ?  319 GLN   K C   1 
ATOM   17149 O O   . GLN   K  1 319 ? 56.90754  16.42857  50.70105  1.000 44.15937  ?  319 GLN   K O   1 
ATOM   17150 C CB  . GLN   K  1 319 ? 54.47971  18.90694  50.68119  1.000 31.27700  ?  319 GLN   K CB  1 
ATOM   17151 C CG  . GLN   K  1 319 ? 55.66526  19.73681  51.07803  1.000 39.37947  ?  319 GLN   K CG  1 
ATOM   17152 C CD  . GLN   K  1 319 ? 55.34660  21.21245  51.08273  1.000 28.39188  ?  319 GLN   K CD  1 
ATOM   17153 O OE1 . GLN   K  1 319 ? 54.65603  21.71295  51.98067  1.000 51.71249  ?  319 GLN   K OE1 1 
ATOM   17154 N NE2 . GLN   K  1 319 ? 55.86058  21.92528  50.08921  1.000 37.19908  ?  319 GLN   K NE2 1 
ATOM   17155 N N   . ALA   K  1 320 ? 55.87276  17.00946  48.79344  1.000 38.32098  ?  320 ALA   K N   1 
ATOM   17156 C CA  . ALA   K  1 320 ? 56.99863  16.56597  47.97555  1.000 39.06639  ?  320 ALA   K CA  1 
ATOM   17157 C C   . ALA   K  1 320 ? 58.18294  17.51564  48.15893  1.000 38.80920  ?  320 ALA   K C   1 
ATOM   17158 O O   . ALA   K  1 320 ? 58.01785  18.73680  48.03164  1.000 40.34740  ?  320 ALA   K O   1 
ATOM   17159 C CB  . ALA   K  1 320 ? 56.60194  16.48766  46.50595  1.000 22.80889  ?  320 ALA   K CB  1 
ATOM   17160 N N   . PRO   K  1 321 ? 59.38532  16.99889  48.43590  1.000 46.56576  ?  321 PRO   K N   1 
ATOM   17161 C CA  . PRO   K  1 321 ? 60.53978  17.88602  48.67950  1.000 32.46473  ?  321 PRO   K CA  1 
ATOM   17162 C C   . PRO   K  1 321 ? 60.81209  18.86617  47.53981  1.000 38.14999  ?  321 PRO   K C   1 
ATOM   17163 O O   . PRO   K  1 321 ? 61.21304  20.00590  47.80797  1.000 42.91649  ?  321 PRO   K O   1 
ATOM   17164 C CB  . PRO   K  1 321 ? 61.70457  16.90100  48.87540  1.000 25.66131  ?  321 PRO   K CB  1 
ATOM   17165 C CG  . PRO   K  1 321 ? 61.08650  15.53885  49.01946  1.000 46.82146  ?  321 PRO   K CG  1 
ATOM   17166 C CD  . PRO   K  1 321 ? 59.77529  15.58385  48.31055  1.000 29.11123  ?  321 PRO   K CD  1 
ATOM   17167 N N   . SER   K  1 322 ? 60.56651  18.46771  46.28254  1.000 43.36990  ?  322 SER   K N   1 
ATOM   17168 C CA  . SER   K  1 322 ? 60.71772  19.36911  45.13742  1.000 42.85212  ?  322 SER   K CA  1 
ATOM   17169 C C   . SER   K  1 322 ? 59.83262  20.61324  45.21744  1.000 42.45610  ?  322 SER   K C   1 
ATOM   17170 O O   . SER   K  1 322 ? 60.11715  21.59674  44.52247  1.000 61.83587  ?  322 SER   K O   1 
ATOM   17171 C CB  . SER   K  1 322 ? 60.41515  18.62725  43.82568  1.000 33.91635  ?  322 SER   K CB  1 
ATOM   17172 O OG  . SER   K  1 322 ? 59.32337  17.72263  43.95742  1.000 59.00869  ?  322 SER   K OG  1 
ATOM   17173 N N   . THR   K  1 323 ? 58.75645  20.59202  46.01362  1.000 48.43088  ?  323 THR   K N   1 
ATOM   17174 C CA  . THR   K  1 323 ? 57.86693  21.74415  46.13583  1.000 30.77519  ?  323 THR   K CA  1 
ATOM   17175 C C   . THR   K  1 323 ? 58.17215  22.60519  47.34866  1.000 46.24979  ?  323 THR   K C   1 
ATOM   17176 O O   . THR   K  1 323 ? 57.51408  23.63024  47.53316  1.000 29.16116  ?  323 THR   K O   1 
ATOM   17177 C CB  . THR   K  1 323 ? 56.39409  21.30873  46.21072  1.000 37.50950  ?  323 THR   K CB  1 
ATOM   17178 O OG1 . THR   K  1 323 ? 56.09215  20.82907  47.53285  1.000 39.04482  ?  323 THR   K OG1 1 
ATOM   17179 C CG2 . THR   K  1 323 ? 56.11228  20.21891  45.21358  1.000 19.45977  ?  323 THR   K CG2 1 
ATOM   17180 N N   . ILE   K  1 324 ? 59.12826  22.21025  48.18972  1.000 38.34360  ?  324 ILE   K N   1 
ATOM   17181 C CA  . ILE   K  1 324 ? 59.40981  22.98246  49.39318  1.000 40.08940  ?  324 ILE   K CA  1 
ATOM   17182 C C   . ILE   K  1 324 ? 59.85675  24.37657  48.98731  1.000 58.63891  ?  324 ILE   K C   1 
ATOM   17183 O O   . ILE   K  1 324 ? 60.80840  24.54033  48.21254  1.000 51.30922  ?  324 ILE   K O   1 
ATOM   17184 C CB  . ILE   K  1 324 ? 60.45836  22.27828  50.24929  1.000 28.09846  ?  324 ILE   K CB  1 
ATOM   17185 C CG1 . ILE   K  1 324 ? 59.87535  20.97885  50.80261  1.000 41.47689  ?  324 ILE   K CG1 1 
ATOM   17186 C CG2 . ILE   K  1 324 ? 60.92071  23.20401  51.37517  1.000 30.64089  ?  324 ILE   K CG2 1 
ATOM   17187 C CD1 . ILE   K  1 324 ? 60.83774  20.18450  51.59177  1.000 34.97998  ?  324 ILE   K CD1 1 
ATOM   17188 N N   . GLY   K  1 325 ? 59.14446  25.39108  49.47820  1.000 44.83818  ?  325 GLY   K N   1 
ATOM   17189 C CA  . GLY   K  1 325 ? 59.43834  26.76858  49.14732  1.000 40.05781  ?  325 GLY   K CA  1 
ATOM   17190 C C   . GLY   K  1 325 ? 58.53998  27.40074  48.09787  1.000 49.08875  ?  325 GLY   K C   1 
ATOM   17191 O O   . GLY   K  1 325 ? 58.50844  28.63314  48.00553  1.000 54.26022  ?  325 GLY   K O   1 
ATOM   17192 N N   . ASP   K  1 326 ? 57.83371  26.60160  47.29551  1.000 38.12668  ?  326 ASP   K N   1 
ATOM   17193 C CA  . ASP   K  1 326 ? 56.87976  27.14236  46.33220  1.000 45.33104  ?  326 ASP   K CA  1 
ATOM   17194 C C   . ASP   K  1 326 ? 55.85859  28.05403  47.02007  1.000 36.50551  ?  326 ASP   K C   1 
ATOM   17195 O O   . ASP   K  1 326 ? 55.57227  27.90329  48.21316  1.000 46.87351  ?  326 ASP   K O   1 
ATOM   17196 C CB  . ASP   K  1 326 ? 56.13804  26.01286  45.61641  1.000 27.76305  ?  326 ASP   K CB  1 
ATOM   17197 C CG  . ASP   K  1 326 ? 57.03452  25.19415  44.70773  1.000 64.43580  ?  326 ASP   K CG  1 
ATOM   17198 O OD1 . ASP   K  1 326 ? 58.22251  25.56502  44.51829  1.000 50.03691  ?  326 ASP   K OD1 1 
ATOM   17199 O OD2 . ASP   K  1 326 ? 56.52750  24.17062  44.18207  1.000 52.63037  -1 326 ASP   K OD2 1 
ATOM   17200 N N   . PRO   K  1 327 ? 55.28417  29.00310  46.29021  1.000 62.52734  ?  327 PRO   K N   1 
ATOM   17201 C CA  . PRO   K  1 327 ? 54.30855  29.90906  46.91072  1.000 47.98470  ?  327 PRO   K CA  1 
ATOM   17202 C C   . PRO   K  1 327 ? 53.04638  29.17940  47.36451  1.000 42.70317  ?  327 PRO   K C   1 
ATOM   17203 O O   . PRO   K  1 327 ? 52.56250  28.26058  46.69882  1.000 55.68583  ?  327 PRO   K O   1 
ATOM   17204 C CB  . PRO   K  1 327 ? 54.00612  30.91960  45.79520  1.000 27.87572  ?  327 PRO   K CB  1 
ATOM   17205 C CG  . PRO   K  1 327 ? 54.50726  30.29850  44.52698  1.000 42.54477  ?  327 PRO   K CG  1 
ATOM   17206 C CD  . PRO   K  1 327 ? 55.65097  29.41752  44.92303  1.000 45.45988  ?  327 PRO   K CD  1 
ATOM   17207 N N   . ILE   K  1 328 ? 52.52149  29.59231  48.51628  1.000 47.38866  ?  328 ILE   K N   1 
ATOM   17208 C CA  . ILE   K  1 328 ? 51.21745  29.11724  48.97927  1.000 47.18797  ?  328 ILE   K CA  1 
ATOM   17209 C C   . ILE   K  1 328 ? 50.15339  30.13879  48.59482  1.000 49.48369  ?  328 ILE   K C   1 
ATOM   17210 O O   . ILE   K  1 328 ? 49.99569  31.15410  49.28987  1.000 58.52458  ?  328 ILE   K O   1 
ATOM   17211 C CB  . ILE   K  1 328 ? 51.20612  28.85911  50.49609  1.000 52.41285  ?  328 ILE   K CB  1 
ATOM   17212 C CG1 . ILE   K  1 328 ? 52.31000  27.87276  50.88522  1.000 39.86944  ?  328 ILE   K CG1 1 
ATOM   17213 C CG2 . ILE   K  1 328 ? 49.85547  28.30011  50.94411  1.000 41.59392  ?  328 ILE   K CG2 1 
ATOM   17214 C CD1 . ILE   K  1 328 ? 52.33865  27.54736  52.37949  1.000 35.87923  ?  328 ILE   K CD1 1 
ATOM   17215 N N   . PRO   K  1 329 ? 49.38978  29.90288  47.52372  1.000 68.66246  ?  329 PRO   K N   1 
ATOM   17216 C CA  . PRO   K  1 329 ? 48.44789  30.91990  47.03100  1.000 54.13467  ?  329 PRO   K CA  1 
ATOM   17217 C C   . PRO   K  1 329 ? 47.43123  31.32226  48.08910  1.000 56.38757  ?  329 PRO   K C   1 
ATOM   17218 O O   . PRO   K  1 329 ? 47.00758  30.51093  48.92012  1.000 88.73792  ?  329 PRO   K O   1 
ATOM   17219 C CB  . PRO   K  1 329 ? 47.76913  30.23493  45.83869  1.000 40.99547  ?  329 PRO   K CB  1 
ATOM   17220 C CG  . PRO   K  1 329 ? 48.73447  29.13197  45.43155  1.000 51.70385  ?  329 PRO   K CG  1 
ATOM   17221 C CD  . PRO   K  1 329 ? 49.41268  28.69688  46.68036  1.000 56.59509  ?  329 PRO   K CD  1 
ATOM   17222 N N   . ASP   K  1 330 ? 47.08524  32.61239  48.07562  1.000 84.74886  ?  330 ASP   K N   1 
ATOM   17223 C CA  . ASP   K  1 330 ? 46.07557  33.18001  48.96165  1.000 94.82077  ?  330 ASP   K CA  1 
ATOM   17224 C C   . ASP   K  1 330 ? 44.67830  33.21187  48.34058  1.000 73.51408  ?  330 ASP   K C   1 
ATOM   17225 O O   . ASP   K  1 330 ? 43.84008  34.01838  48.78412  1.000 102.23903 ?  330 ASP   K O   1 
ATOM   17226 C CB  . ASP   K  1 330 ? 46.49724  34.59082  49.41494  1.000 66.05500  ?  330 ASP   K CB  1 
ATOM   17227 C CG  . ASP   K  1 330 ? 46.38521  34.67234  51.09996  1.000 56.46372  ?  330 ASP   K CG  1 
ATOM   17228 O OD1 . ASP   K  1 330 ? 46.53893  33.63356  51.71828  1.000 91.13062  ?  330 ASP   K OD1 1 
ATOM   17229 O OD2 . ASP   K  1 330 ? 46.05113  35.62423  51.73285  1.000 106.67752 ?  330 ASP   K OD2 1 
ATOM   17230 N N   . ASN   K  1 331 ? 44.42140  32.33389  47.36451  1.000 81.10387  ?  331 ASN   K N   1 
ATOM   17231 C CA  . ASN   K  1 331 ? 43.15268  32.19274  46.66796  1.000 81.22895  ?  331 ASN   K CA  1 
ATOM   17232 C C   . ASN   K  1 331 ? 42.72855  30.72900  46.75881  1.000 63.89733  ?  331 ASN   K C   1 
ATOM   17233 O O   . ASN   K  1 331 ? 43.30954  29.96974  47.52359  1.000 107.60728 ?  331 ASN   K O   1 
ATOM   17234 C CB  . ASN   K  1 331 ? 43.31635  32.66963  45.23278  1.000 59.15322  ?  331 ASN   K CB  1 
ATOM   17235 C CG  . ASN   K  1 331 ? 44.20931  31.80015  44.40813  1.000 70.24438  ?  331 ASN   K CG  1 
ATOM   17236 O OD1 . ASN   K  1 331 ? 44.11407  30.57552  44.32402  1.000 139.75761 ?  331 ASN   K OD1 1 
ATOM   17237 N ND2 . ASN   K  1 331 ? 45.19008  32.46288  43.85192  1.000 74.41410  ?  331 ASN   K ND2 1 
ATOM   17238 N N   . ASP   K  1 332 ? 41.73695  30.31966  46.01339  1.000 98.72986  ?  332 ASP   K N   1 
ATOM   17239 C CA  . ASP   K  1 332 ? 41.58238  28.97475  45.45078  1.000 26.31425  ?  332 ASP   K CA  1 
ATOM   17240 C C   . ASP   K  1 332 ? 41.92955  28.88076  43.96247  1.000 90.67588  ?  332 ASP   K C   1 
ATOM   17241 O O   . ASP   K  1 332 ? 41.77190  27.81150  43.38457  1.000 38.00979  ?  332 ASP   K O   1 
ATOM   17242 C CB  . ASP   K  1 332 ? 40.16121  28.44425  45.62258  1.000 121.52697 ?  332 ASP   K CB  1 
ATOM   17243 C CG  . ASP   K  1 332 ? 39.14319  29.22888  44.82098  1.000 77.49855  ?  332 ASP   K CG  1 
ATOM   17244 O OD1 . ASP   K  1 332 ? 39.43959  30.40296  44.47157  1.000 87.69123  ?  332 ASP   K OD1 1 
ATOM   17245 O OD2 . ASP   K  1 332 ? 38.02832  28.71138  44.59079  1.000 59.36486  ?  332 ASP   K OD2 1 
ATOM   17246 N N   . TYR   K  1 333 ? 42.32531  29.96713  43.33456  1.000 113.95246 ?  333 TYR   K N   1 
ATOM   17247 C CA  . TYR   K  1 333 ? 42.68539  29.94970  41.92190  1.000 57.38135  ?  333 TYR   K CA  1 
ATOM   17248 C C   . TYR   K  1 333 ? 43.78724  28.90129  41.62120  1.000 103.75222 ?  333 TYR   K C   1 
ATOM   17249 O O   . TYR   K  1 333 ? 43.99003  28.55888  40.43848  1.000 54.62205  ?  333 TYR   K O   1 
ATOM   17250 C CB  . TYR   K  1 333 ? 43.09424  31.39028  41.54365  1.000 21.39934  ?  333 TYR   K CB  1 
ATOM   17251 C CG  . TYR   K  1 333 ? 43.34550  31.80571  40.08235  1.000 78.42847  ?  333 TYR   K CG  1 
ATOM   17252 C CD1 . TYR   K  1 333 ? 42.28726  31.94672  39.17559  1.000 70.05527  ?  333 TYR   K CD1 1 
ATOM   17253 C CD2 . TYR   K  1 333 ? 44.64236  32.12096  39.62176  1.000 71.46913  ?  333 TYR   K CD2 1 
ATOM   17254 C CE1 . TYR   K  1 333 ? 42.52166  32.31340  37.83909  1.000 47.09245  ?  333 TYR   K CE1 1 
ATOM   17255 C CE2 . TYR   K  1 333 ? 44.89018  32.46441  38.29942  1.000 66.61138  ?  333 TYR   K CE2 1 
ATOM   17256 C CZ  . TYR   K  1 333 ? 43.83367  32.56405  37.41449  1.000 82.82332  ?  333 TYR   K CZ  1 
ATOM   17257 O OH  . TYR   K  1 333 ? 44.10301  32.91742  36.11780  1.000 59.45553  ?  333 TYR   K OH  1 
ATOM   17258 N N   . ASP   K  1 334 ? 44.43349  28.29941  42.65509  1.000 72.54154  ?  334 ASP   K N   1 
ATOM   17259 C CA  . ASP   K  1 334 ? 45.80587  27.81614  42.49022  1.000 70.61626  ?  334 ASP   K CA  1 
ATOM   17260 C C   . ASP   K  1 334 ? 46.18062  26.79710  43.56269  1.000 80.05663  ?  334 ASP   K C   1 
ATOM   17261 O O   . ASP   K  1 334 ? 46.04792  27.08334  44.76548  1.000 45.78419  ?  334 ASP   K O   1 
ATOM   17262 C CB  . ASP   K  1 334 ? 46.79295  28.97111  42.53231  1.000 99.41832  ?  334 ASP   K CB  1 
ATOM   17263 C CG  . ASP   K  1 334 ? 46.71720  29.83582  41.30220  1.000 114.03965 ?  334 ASP   K CG  1 
ATOM   17264 O OD1 . ASP   K  1 334 ? 46.40161  29.29354  40.20600  1.000 70.24529  ?  334 ASP   K OD1 1 
ATOM   17265 O OD2 . ASP   K  1 334 ? 46.97957  31.04915  41.41331  1.000 81.56950  -1 334 ASP   K OD2 1 
ATOM   17266 N N   . PRO   K  1 335 ? 46.66485  25.61937  43.16891  1.000 74.70581  ?  335 PRO   K N   1 
ATOM   17267 C CA  . PRO   K  1 335 ? 46.97751  24.57614  44.14635  1.000 54.51227  ?  335 PRO   K CA  1 
ATOM   17268 C C   . PRO   K  1 335 ? 48.20632  24.93785  44.95101  1.000 38.54181  ?  335 PRO   K C   1 
ATOM   17269 O O   . PRO   K  1 335 ? 49.23771  25.35752  44.39079  1.000 67.48340  ?  335 PRO   K O   1 
ATOM   17270 C CB  . PRO   K  1 335 ? 47.23290  23.33810  43.27302  1.000 60.29106  ?  335 PRO   K CB  1 
ATOM   17271 C CG  . PRO   K  1 335 ? 46.78838  23.72184  41.88821  1.000 73.15169  ?  335 PRO   K CG  1 
ATOM   17272 C CD  . PRO   K  1 335 ? 46.92228  25.18887  41.79067  1.000 46.72774  ?  335 PRO   K CD  1 
ATOM   17273 N N   . PRO   K  1 336 ? 48.15166  24.78353  46.27548  1.000 60.83296  ?  336 PRO   K N   1 
ATOM   17274 C CA  . PRO   K  1 336 ? 49.34932  24.96974  47.11066  1.000 25.24808  ?  336 PRO   K CA  1 
ATOM   17275 C C   . PRO   K  1 336 ? 50.27325  23.76499  47.00062  1.000 91.54033  ?  336 PRO   K C   1 
ATOM   17276 O O   . PRO   K  1 336 ? 49.89747  22.72567  46.42931  1.000 30.60657  ?  336 PRO   K O   1 
ATOM   17277 C CB  . PRO   K  1 336 ? 48.76418  25.12500  48.52024  1.000 44.23112  ?  336 PRO   K CB  1 
ATOM   17278 C CG  . PRO   K  1 336 ? 47.49510  24.31437  48.48417  1.000 41.20769  ?  336 PRO   K CG  1 
ATOM   17279 C CD  . PRO   K  1 336 ? 46.99600  24.28921  47.05482  1.000 25.23073  ?  336 PRO   K CD  1 
ATOM   17280 N N   . PRO   K  1 337 ? 51.50808  23.86650  47.50378  1.000 33.94820  ?  337 PRO   K N   1 
ATOM   17281 C CA  . PRO   K  1 337 ? 52.48063  22.76854  47.27759  1.000 49.55968  ?  337 PRO   K CA  1 
ATOM   17282 C C   . PRO   K  1 337 ? 51.99344  21.38953  47.72216  1.000 38.11325  ?  337 PRO   K C   1 
ATOM   17283 O O   . PRO   K  1 337 ? 52.17750  20.40637  46.99196  1.000 35.95897  ?  337 PRO   K O   1 
ATOM   17284 C CB  . PRO   K  1 337 ? 53.70714  23.21805  48.08164  1.000 36.08236  ?  337 PRO   K CB  1 
ATOM   17285 C CG  . PRO   K  1 337 ? 53.58176  24.67877  48.20053  1.000 44.46504  ?  337 PRO   K CG  1 
ATOM   17286 C CD  . PRO   K  1 337 ? 52.10733  24.99682  48.22803  1.000 53.13978  ?  337 PRO   K CD  1 
ATOM   17287 N N   . TYR   K  1 338 ? 51.35168  21.29605  48.88903  1.000 38.73580  ?  338 TYR   K N   1 
ATOM   17288 C CA  . TYR   K  1 338 ? 50.82815  20.01571  49.35284  1.000 41.32091  ?  338 TYR   K CA  1 
ATOM   17289 C C   . TYR   K  1 338 ? 49.87542  19.39088  48.33623  1.000 35.13330  ?  338 TYR   K C   1 
ATOM   17290 O O   . TYR   K  1 338 ? 49.98090  18.19326  48.03823  1.000 36.46143  ?  338 TYR   K O   1 
ATOM   17291 C CB  . TYR   K  1 338 ? 50.13850  20.19781  50.70563  1.000 28.83865  ?  338 TYR   K CB  1 
ATOM   17292 C CG  . TYR   K  1 338 ? 49.70584  18.91393  51.38332  1.000 41.91510  ?  338 TYR   K CG  1 
ATOM   17293 C CD1 . TYR   K  1 338 ? 50.62506  17.90407  51.68778  1.000 34.64284  ?  338 TYR   K CD1 1 
ATOM   17294 C CD2 . TYR   K  1 338 ? 48.38295  18.72239  51.74407  1.000 32.48335  ?  338 TYR   K CD2 1 
ATOM   17295 C CE1 . TYR   K  1 338 ? 50.21846  16.72937  52.33183  1.000 37.35525  ?  338 TYR   K CE1 1 
ATOM   17296 C CE2 . TYR   K  1 338 ? 47.97003  17.56405  52.37937  1.000 26.39195  ?  338 TYR   K CE2 1 
ATOM   17297 C CZ  . TYR   K  1 338 ? 48.88199  16.56827  52.66698  1.000 46.63680  ?  338 TYR   K CZ  1 
ATOM   17298 O OH  . TYR   K  1 338 ? 48.43886  15.42580  53.30082  1.000 35.18540  ?  338 TYR   K OH  1 
ATOM   17299 N N   . LEU   K  1 339 ? 48.93099  20.17837  47.79138  1.000 36.76490  ?  339 LEU   K N   1 
ATOM   17300 C CA  . LEU   K  1 339 ? 47.99608  19.60524  46.81022  1.000 27.92627  ?  339 LEU   K CA  1 
ATOM   17301 C C   . LEU   K  1 339 ? 48.63172  19.35483  45.44846  1.000 39.91139  ?  339 LEU   K C   1 
ATOM   17302 O O   . LEU   K  1 339 ? 47.96213  18.79226  44.57550  1.000 41.60295  ?  339 LEU   K O   1 
ATOM   17303 C CB  . LEU   K  1 339 ? 46.76233  20.48853  46.63038  1.000 28.74931  ?  339 LEU   K CB  1 
ATOM   17304 C CG  . LEU   K  1 339 ? 45.94237  20.60887  47.92321  1.000 50.76457  ?  339 LEU   K CG  1 
ATOM   17305 C CD1 . LEU   K  1 339 ? 44.65670  21.37068  47.68647  1.000 34.59008  ?  339 LEU   K CD1 1 
ATOM   17306 C CD2 . LEU   K  1 339 ? 45.64138  19.24564  48.50664  1.000 35.94412  ?  339 LEU   K CD2 1 
ATOM   17307 N N   . LYS   K  1 340 ? 49.88913  19.74654  45.23913  1.000 29.95168  ?  340 LYS   K N   1 
ATOM   17308 C CA  . LYS   K  1 340 ? 50.66125  19.27429  44.09676  1.000 49.77032  ?  340 LYS   K CA  1 
ATOM   17309 C C   . LYS   K  1 340 ? 51.54577  18.06338  44.43242  1.000 31.98232  ?  340 LYS   K C   1 
ATOM   17310 O O   . LYS   K  1 340 ? 52.40781  17.70763  43.62632  1.000 38.37362  ?  340 LYS   K O   1 
ATOM   17311 C CB  . LYS   K  1 340 ? 51.52153  20.41051  43.53318  1.000 32.63237  ?  340 LYS   K CB  1 
ATOM   17312 C CG  . LYS   K  1 340 ? 50.75305  21.63628  43.00363  1.000 79.88337  ?  340 LYS   K CG  1 
ATOM   17313 C CD  . LYS   K  1 340 ? 51.72376  22.63290  42.40553  1.000 90.26112  ?  340 LYS   K CD  1 
ATOM   17314 C CE  . LYS   K  1 340 ? 51.15484  23.34110  41.19588  1.000 113.03779 ?  340 LYS   K CE  1 
ATOM   17315 N NZ  . LYS   K  1 340 ? 50.58295  22.42365  40.16493  1.000 108.11652 ?  340 LYS   K NZ  1 
ATOM   17316 N N   . SER   K  1 341 ? 51.33225  17.40882  45.58786  1.000 37.67169  ?  341 SER   K N   1 
ATOM   17317 C CA  . SER   K  1 341 ? 52.20607  16.34891  46.08546  1.000 30.82674  ?  341 SER   K CA  1 
ATOM   17318 C C   . SER   K  1 341 ? 51.54194  14.97709  46.20935  1.000 35.71237  ?  341 SER   K C   1 
ATOM   17319 O O   . SER   K  1 341 ? 52.17451  14.04704  46.73724  1.000 46.26103  ?  341 SER   K O   1 
ATOM   17320 C CB  . SER   K  1 341 ? 52.77128  16.73584  47.46442  1.000 37.37232  ?  341 SER   K CB  1 
ATOM   17321 O OG  . SER   K  1 341 ? 53.58849  17.89123  47.40537  1.000 37.13423  ?  341 SER   K OG  1 
ATOM   17322 N N   . LEU   K  1 342 ? 50.30027  14.81860  45.74623  1.000 36.04308  ?  342 LEU   K N   1 
ATOM   17323 C CA  . LEU   K  1 342 ? 49.53145  13.61837  46.06757  1.000 47.23234  ?  342 LEU   K CA  1 
ATOM   17324 C C   . LEU   K  1 342 ? 50.19197  12.35017  45.53586  1.000 35.83483  ?  342 LEU   K C   1 
ATOM   17325 O O   . LEU   K  1 342 ? 50.12471  11.29759  46.18016  1.000 41.75123  ?  342 LEU   K O   1 
ATOM   17326 C CB  . LEU   K  1 342 ? 48.10948  13.72918  45.52041  1.000 30.09780  ?  342 LEU   K CB  1 
ATOM   17327 C CG  . LEU   K  1 342 ? 47.03870  14.29496  46.44313  1.000 48.36396  ?  342 LEU   K CG  1 
ATOM   17328 C CD1 . LEU   K  1 342 ? 47.34296  15.75277  46.79302  1.000 28.54087  ?  342 LEU   K CD1 1 
ATOM   17329 C CD2 . LEU   K  1 342 ? 45.66504  14.14925  45.76245  1.000 24.15206  ?  342 LEU   K CD2 1 
ATOM   17330 N N   . VAL   K  1 343 ? 50.81439  12.40417  44.35711  1.000 44.90416  ?  343 VAL   K N   1 
ATOM   17331 C CA  . VAL   K  1 343 ? 51.48445  11.19635  43.88123  1.000 39.19822  ?  343 VAL   K CA  1 
ATOM   17332 C C   . VAL   K  1 343 ? 52.66068  10.86399  44.78747  1.000 52.11234  ?  343 VAL   K C   1 
ATOM   17333 O O   . VAL   K  1 343 ? 52.81164  9.72257   45.23662  1.000 36.44088  ?  343 VAL   K O   1 
ATOM   17334 C CB  . VAL   K  1 343 ? 51.92379  11.33456  42.41301  1.000 40.07886  ?  343 VAL   K CB  1 
ATOM   17335 C CG1 . VAL   K  1 343 ? 52.83250  10.16673  42.03070  1.000 26.29420  ?  343 VAL   K CG1 1 
ATOM   17336 C CG2 . VAL   K  1 343 ? 50.71012  11.33744  41.50340  1.000 33.64187  ?  343 VAL   K CG2 1 
ATOM   17337 N N   . TYR   K  1 344 ? 53.48077  11.86719  45.10609  1.000 26.58694  ?  344 TYR   K N   1 
ATOM   17338 C CA  . TYR   K  1 344 ? 54.62897  11.64649  45.97834  1.000 44.04272  ?  344 TYR   K CA  1 
ATOM   17339 C C   . TYR   K  1 344 ? 54.22604  10.98658  47.29227  1.000 45.57592  ?  344 TYR   K C   1 
ATOM   17340 O O   . TYR   K  1 344 ? 54.76016  9.93192   47.65028  1.000 35.56100  ?  344 TYR   K O   1 
ATOM   17341 C CB  . TYR   K  1 344 ? 55.35570  12.96392  46.25555  1.000 30.94341  ?  344 TYR   K CB  1 
ATOM   17342 C CG  . TYR   K  1 344 ? 56.47343  12.83150  47.26962  1.000 51.32800  ?  344 TYR   K CG  1 
ATOM   17343 C CD1 . TYR   K  1 344 ? 57.72696  12.36346  46.89182  1.000 34.07961  ?  344 TYR   K CD1 1 
ATOM   17344 C CD2 . TYR   K  1 344 ? 56.27587  13.17038  48.60562  1.000 43.30527  ?  344 TYR   K CD2 1 
ATOM   17345 C CE1 . TYR   K  1 344 ? 58.75881  12.23381  47.81286  1.000 34.27868  ?  344 TYR   K CE1 1 
ATOM   17346 C CE2 . TYR   K  1 344 ? 57.30597  13.04745  49.54442  1.000 33.37592  ?  344 TYR   K CE2 1 
ATOM   17347 C CZ  . TYR   K  1 344 ? 58.53931  12.58038  49.13628  1.000 51.64561  ?  344 TYR   K CZ  1 
ATOM   17348 O OH  . TYR   K  1 344 ? 59.55963  12.46374  50.04588  1.000 46.68508  ?  344 TYR   K OH  1 
ATOM   17349 N N   . PHE   K  1 345 ? 53.28538  11.59379  48.03185  1.000 26.79437  ?  345 PHE   K N   1 
ATOM   17350 C CA  . PHE   K  1 345 ? 53.06167  11.12572  49.39758  1.000 35.84272  ?  345 PHE   K CA  1 
ATOM   17351 C C   . PHE   K  1 345 ? 52.11094  9.93511   49.47559  1.000 41.02210  ?  345 PHE   K C   1 
ATOM   17352 O O   . PHE   K  1 345 ? 51.96198  9.35236   50.55691  1.000 37.36526  ?  345 PHE   K O   1 
ATOM   17353 C CB  . PHE   K  1 345 ? 52.61878  12.27870  50.34231  1.000 26.34374  ?  345 PHE   K CB  1 
ATOM   17354 C CG  . PHE   K  1 345 ? 51.23866  12.87214  50.08134  1.000 39.54878  ?  345 PHE   K CG  1 
ATOM   17355 C CD1 . PHE   K  1 345 ? 50.07598  12.13207  50.26278  1.000 44.75890  ?  345 PHE   K CD1 1 
ATOM   17356 C CD2 . PHE   K  1 345 ? 51.11122  14.22293  49.76816  1.000 33.09743  ?  345 PHE   K CD2 1 
ATOM   17357 C CE1 . PHE   K  1 345 ? 48.81347  12.71383  50.05666  1.000 28.94184  ?  345 PHE   K CE1 1 
ATOM   17358 C CE2 . PHE   K  1 345 ? 49.85428  14.82211  49.56453  1.000 34.56457  ?  345 PHE   K CE2 1 
ATOM   17359 C CZ  . PHE   K  1 345 ? 48.70456  14.07070  49.70829  1.000 36.86231  ?  345 PHE   K CZ  1 
ATOM   17360 N N   . SER   K  1 346 ? 51.51908  9.51356   48.35868  1.000 20.37517  ?  346 SER   K N   1 
ATOM   17361 C CA  . SER   K  1 346 ? 50.88051  8.20335   48.34003  1.000 42.58244  ?  346 SER   K CA  1 
ATOM   17362 C C   . SER   K  1 346 ? 51.88218  7.11548   48.70945  1.000 29.95447  ?  346 SER   K C   1 
ATOM   17363 O O   . SER   K  1 346 ? 51.49702  6.06020   49.23109  1.000 29.95739  ?  346 SER   K O   1 
ATOM   17364 C CB  . SER   K  1 346 ? 50.28250  7.92557   46.96247  1.000 29.35995  ?  346 SER   K CB  1 
ATOM   17365 O OG  . SER   K  1 346 ? 51.31195  7.59008   46.04317  1.000 25.96641  ?  346 SER   K OG  1 
ATOM   17366 N N   . ASN   K  1 347 ? 53.17519  7.37344   48.47101  1.000 35.98037  ?  347 ASN   K N   1 
ATOM   17367 C CA  . ASN   K  1 347 ? 54.22085  6.41218   48.80380  1.000 17.08151  ?  347 ASN   K CA  1 
ATOM   17368 C C   . ASN   K  1 347 ? 54.44472  6.27858   50.30840  1.000 33.95339  ?  347 ASN   K C   1 
ATOM   17369 O O   . ASN   K  1 347 ? 54.89930  5.22003   50.76493  1.000 34.29595  ?  347 ASN   K O   1 
ATOM   17370 C CB  . ASN   K  1 347 ? 55.53131  6.80949   48.12077  1.000 24.60162  ?  347 ASN   K CB  1 
ATOM   17371 C CG  . ASN   K  1 347 ? 55.46020  6.69237   46.61386  1.000 39.74702  ?  347 ASN   K CG  1 
ATOM   17372 O OD1 . ASN   K  1 347 ? 55.25245  5.60236   46.06780  1.000 30.88239  ?  347 ASN   K OD1 1 
ATOM   17373 N ND2 . ASN   K  1 347 ? 55.64381  7.81125   45.92886  1.000 21.61356  ?  347 ASN   K ND2 1 
ATOM   17374 N N   . ILE   K  1 348 ? 54.14288  7.32217   51.09298  1.000 34.52327  ?  348 ILE   K N   1 
ATOM   17375 C CA  . ILE   K  1 348 ? 54.59428  7.35903   52.48635  1.000 27.51865  ?  348 ILE   K CA  1 
ATOM   17376 C C   . ILE   K  1 348 ? 53.51106  7.74223   53.49597  1.000 38.59797  ?  348 ILE   K C   1 
ATOM   17377 O O   . ILE   K  1 348 ? 53.71941  7.62078   54.70920  1.000 42.06956  ?  348 ILE   K O   1 
ATOM   17378 C CB  . ILE   K  1 348 ? 55.79062  8.31499   52.61696  1.000 36.50222  ?  348 ILE   K CB  1 
ATOM   17379 C CG1 . ILE   K  1 348 ? 55.39223  9.71166   52.13249  1.000 25.03266  ?  348 ILE   K CG1 1 
ATOM   17380 C CG2 . ILE   K  1 348 ? 56.99237  7.77603   51.83633  1.000 22.93935  ?  348 ILE   K CG2 1 
ATOM   17381 C CD1 . ILE   K  1 348 ? 56.41883  10.77655  52.49232  1.000 47.58697  ?  348 ILE   K CD1 1 
ATOM   17382 N N   . ALA   K  1 349 ? 52.36329  8.21823   53.02227  1.000 30.58573  ?  349 ALA   K N   1 
ATOM   17383 C CA  . ALA   K  1 349 ? 51.32624  8.68158   53.93802  1.000 31.04850  ?  349 ALA   K CA  1 
ATOM   17384 C C   . ALA   K  1 349 ? 50.63692  7.50964   54.63133  1.000 34.23049  ?  349 ALA   K C   1 
ATOM   17385 O O   . ALA   K  1 349 ? 50.55321  6.39796   54.09291  1.000 39.16629  ?  349 ALA   K O   1 
ATOM   17386 C CB  . ALA   K  1 349 ? 50.27285  9.50699   53.19204  1.000 16.24918  ?  349 ALA   K CB  1 
ATOM   17387 N N   . ALA   K  1 350 ? 50.13332  7.76705   55.83957  1.000 34.38331  ?  350 ALA   K N   1 
ATOM   17388 C CA  . ALA   K  1 350 ? 49.21693  6.82091   56.46866  1.000 36.86967  ?  350 ALA   K CA  1 
ATOM   17389 C C   . ALA   K  1 350 ? 48.11215  6.42889   55.48912  1.000 42.80897  ?  350 ALA   K C   1 
ATOM   17390 O O   . ALA   K  1 350 ? 47.44001  7.28818   54.90891  1.000 36.33855  ?  350 ALA   K O   1 
ATOM   17391 C CB  . ALA   K  1 350 ? 48.61369  7.43615   57.72587  1.000 22.74330  ?  350 ALA   K CB  1 
ATOM   17392 N N   . ARG   K  1 351 ? 47.94141  5.12627   55.29374  1.000 31.91588  ?  351 ARG   K N   1 
ATOM   17393 C CA  . ARG   K  1 351 ? 47.13582  4.64276   54.18483  1.000 42.17003  ?  351 ARG   K CA  1 
ATOM   17394 C C   . ARG   K  1 351 ? 46.70704  3.21008   54.46601  1.000 34.50689  ?  351 ARG   K C   1 
ATOM   17395 O O   . ARG   K  1 351 ? 47.27245  2.52357   55.32993  1.000 48.74221  ?  351 ARG   K O   1 
ATOM   17396 C CB  . ARG   K  1 351 ? 47.90940  4.73929   52.85490  1.000 27.89017  ?  351 ARG   K CB  1 
ATOM   17397 C CG  . ARG   K  1 351 ? 49.14783  3.87251   52.80279  1.000 27.89591  ?  351 ARG   K CG  1 
ATOM   17398 C CD  . ARG   K  1 351 ? 50.09998  4.31342   51.70289  1.000 35.81100  ?  351 ARG   K CD  1 
ATOM   17399 N NE  . ARG   K  1 351 ? 51.25700  3.42922   51.60778  1.000 37.37509  ?  351 ARG   K NE  1 
ATOM   17400 C CZ  . ARG   K  1 351 ? 52.32519  3.49768   52.39505  1.000 58.89655  ?  351 ARG   K CZ  1 
ATOM   17401 N NH1 . ARG   K  1 351 ? 52.42950  4.40398   53.35722  1.000 37.64542  ?  351 ARG   K NH1 1 
ATOM   17402 N NH2 . ARG   K  1 351 ? 53.31950  2.63641   52.21099  1.000 33.01235  ?  351 ARG   K NH2 1 
ATOM   17403 N N   . GLN   K  1 352 ? 45.67716  2.77625   53.73722  1.000 46.57485  ?  352 GLN   K N   1 
ATOM   17404 C CA  . GLN   K  1 352 ? 45.23236  1.38899   53.77150  1.000 39.93450  ?  352 GLN   K CA  1 
ATOM   17405 C C   . GLN   K  1 352 ? 45.29147  0.82769   52.36247  1.000 52.11072  ?  352 GLN   K C   1 
ATOM   17406 O O   . GLN   K  1 352 ? 44.81876  1.46713   51.41081  1.000 50.98937  ?  352 GLN   K O   1 
ATOM   17407 C CB  . GLN   K  1 352 ? 43.82334  1.24346   54.32584  1.000 50.09951  ?  352 GLN   K CB  1 
ATOM   17408 C CG  . GLN   K  1 352 ? 43.33010  -0.19436  54.30407  1.000 45.15302  ?  352 GLN   K CG  1 
ATOM   17409 C CD  . GLN   K  1 352 ? 41.88031  -0.29767  54.75449  1.000 53.49934  ?  352 GLN   K CD  1 
ATOM   17410 O OE1 . GLN   K  1 352 ? 40.97939  -0.49384  53.94227  1.000 55.55827  ?  352 GLN   K OE1 1 
ATOM   17411 N NE2 . GLN   K  1 352 ? 41.65080  -0.14843  56.05325  1.000 42.66452  ?  352 GLN   K NE2 1 
ATOM   17412 N N   . ILE   K  1 353 ? 45.92138  -0.33658  52.23303  1.000 50.35015  ?  353 ILE   K N   1 
ATOM   17413 C CA  . ILE   K  1 353 ? 46.05794  -1.04646  50.96706  1.000 53.17316  ?  353 ILE   K CA  1 
ATOM   17414 C C   . ILE   K  1 353 ? 45.02749  -2.15798  50.96056  1.000 46.19012  ?  353 ILE   K C   1 
ATOM   17415 O O   . ILE   K  1 353 ? 44.91098  -2.90578  51.94316  1.000 60.28043  ?  353 ILE   K O   1 
ATOM   17416 C CB  . ILE   K  1 353 ? 47.46914  -1.63554  50.81070  1.000 51.07519  ?  353 ILE   K CB  1 
ATOM   17417 C CG1 . ILE   K  1 353 ? 48.53592  -0.53738  50.86078  1.000 58.31698  ?  353 ILE   K CG1 1 
ATOM   17418 C CG2 . ILE   K  1 353 ? 47.53673  -2.49903  49.55428  1.000 41.93880  ?  353 ILE   K CG2 1 
ATOM   17419 C CD1 . ILE   K  1 353 ? 49.89407  -1.05024  51.27107  1.000 38.48835  ?  353 ILE   K CD1 1 
ATOM   17420 N N   . MET   K  1 354 ? 44.27773  -2.28031  49.87115  1.000 58.34864  ?  354 MET   K N   1 
ATOM   17421 C CA  . MET   K  1 354 ? 43.27554  -3.33575  49.76638  1.000 63.65544  ?  354 MET   K CA  1 
ATOM   17422 C C   . MET   K  1 354 ? 43.44789  -4.05274  48.43503  1.000 68.74983  ?  354 MET   K C   1 
ATOM   17423 O O   . MET   K  1 354 ? 43.37246  -3.42248  47.37241  1.000 70.22002  ?  354 MET   K O   1 
ATOM   17424 C CB  . MET   K  1 354 ? 41.86714  -2.76384  49.91357  1.000 52.67156  ?  354 MET   K CB  1 
ATOM   17425 C CG  . MET   K  1 354 ? 40.76743  -3.80596  50.05877  1.000 74.51402  ?  354 MET   K CG  1 
ATOM   17426 S SD  . MET   K  1 354 ? 39.15387  -3.02320  50.21376  1.000 71.75300  ?  354 MET   K SD  1 
ATOM   17427 C CE  . MET   K  1 354 ? 39.27174  -2.41862  51.90317  1.000 69.95937  ?  354 MET   K CE  1 
ATOM   17428 N N   . PHE   K  1 355 ? 43.72022  -5.35726  48.49170  1.000 72.71315  ?  355 PHE   K N   1 
ATOM   17429 C CA  . PHE   K  1 355 ? 43.83904  -6.18569  47.29416  1.000 74.34417  ?  355 PHE   K CA  1 
ATOM   17430 C C   . PHE   K  1 355 ? 42.52103  -6.89852  47.04463  1.000 73.08395  ?  355 PHE   K C   1 
ATOM   17431 O O   . PHE   K  1 355 ? 41.95475  -7.50804  47.96203  1.000 77.69503  ?  355 PHE   K O   1 
ATOM   17432 C CB  . PHE   K  1 355 ? 44.96611  -7.20844  47.43886  1.000 78.20234  ?  355 PHE   K CB  1 
ATOM   17433 C CG  . PHE   K  1 355 ? 46.31675  -6.59694  47.43299  1.000 80.06174  ?  355 PHE   K CG  1 
ATOM   17434 C CD1 . PHE   K  1 355 ? 46.89842  -6.20496  46.23657  1.000 67.10513  ?  355 PHE   K CD1 1 
ATOM   17435 C CD2 . PHE   K  1 355 ? 46.99900  -6.38816  48.61667  1.000 75.79930  ?  355 PHE   K CD2 1 
ATOM   17436 C CE1 . PHE   K  1 355 ? 48.15365  -5.62267  46.20988  1.000 79.98321  ?  355 PHE   K CE1 1 
ATOM   17437 C CE2 . PHE   K  1 355 ? 48.25134  -5.80900  48.60347  1.000 62.96409  ?  355 PHE   K CE2 1 
ATOM   17438 C CZ  . PHE   K  1 355 ? 48.83673  -5.42913  47.39360  1.000 64.52280  ?  355 PHE   K CZ  1 
ATOM   17439 N N   . ILE   K  1 356 ? 42.02643  -6.81832  45.81663  1.000 70.67834  ?  356 ILE   K N   1 
ATOM   17440 C CA  . ILE   K  1 356 ? 40.76359  -7.45385  45.46715  1.000 74.03751  ?  356 ILE   K CA  1 
ATOM   17441 C C   . ILE   K  1 356 ? 40.98256  -8.36654  44.27691  1.000 86.97798  ?  356 ILE   K C   1 
ATOM   17442 O O   . ILE   K  1 356 ? 41.68088  -7.99864  43.32230  1.000 73.71821  ?  356 ILE   K O   1 
ATOM   17443 C CB  . ILE   K  1 356 ? 39.66290  -6.42067  45.16964  1.000 68.11856  ?  356 ILE   K CB  1 
ATOM   17444 C CG1 . ILE   K  1 356 ? 39.44732  -5.53779  46.41356  1.000 67.41888  ?  356 ILE   K CG1 1 
ATOM   17445 C CG2 . ILE   K  1 356 ? 38.38402  -7.14740  44.73640  1.000 71.15723  ?  356 ILE   K CG2 1 
ATOM   17446 C CD1 . ILE   K  1 356 ? 38.47644  -4.37226  46.19836  1.000 61.52392  ?  356 ILE   K CD1 1 
ATOM   17447 N N   . GLU   K  1 357 ? 40.39811  -9.56743  44.34365  1.000 74.60954  ?  357 GLU   K N   1 
ATOM   17448 C CA  . GLU   K  1 357 ? 40.39855  -10.49297 43.21451  1.000 89.60229  ?  357 GLU   K CA  1 
ATOM   17449 C C   . GLU   K  1 357 ? 39.06202  -10.37331 42.47586  1.000 87.80816  ?  357 GLU   K C   1 
ATOM   17450 O O   . GLU   K  1 357 ? 38.02898  -10.86709 42.95209  1.000 86.49614  ?  357 GLU   K O   1 
ATOM   17451 C CB  . GLU   K  1 357 ? 40.65567  -11.91817 43.68703  1.000 80.11755  ?  357 GLU   K CB  1 
ATOM   17452 C CG  . GLU   K  1 357 ? 40.67802  -12.96002 42.56205  1.000 78.89758  ?  357 GLU   K CG  1 
ATOM   17453 C CD  . GLU   K  1 357 ? 41.96112  -12.94972 41.74143  1.000 132.19755 ?  357 GLU   K CD  1 
ATOM   17454 O OE1 . GLU   K  1 357 ? 43.05892  -12.83381 42.34265  1.000 114.72692 ?  357 GLU   K OE1 1 
ATOM   17455 O OE2 . GLU   K  1 357 ? 41.86858  -13.07677 40.49376  1.000 101.80617 -1 357 GLU   K OE2 1 
ATOM   17456 N N   . ALA   K  1 358 ? 39.09269  -9.70319  41.31863  1.000 80.88615  ?  358 ALA   K N   1 
ATOM   17457 C CA  . ALA   K  1 358 ? 37.90364  -9.51802  40.49099  1.000 99.74782  ?  358 ALA   K CA  1 
ATOM   17458 C C   . ALA   K  1 358 ? 37.36063  -10.85836 40.02685  1.000 94.17539  ?  358 ALA   K C   1 
ATOM   17459 O O   . ALA   K  1 358 ? 38.12271  -11.74388 39.62866  1.000 120.17006 ?  358 ALA   K O   1 
ATOM   17460 C CB  . ALA   K  1 358 ? 38.23071  -8.66135  39.26431  1.000 88.38827  ?  358 ALA   K CB  1 
ATOM   17461 N N   . ASP   K  1 359 ? 36.03127  -11.00158 40.07800  1.000 102.60069 ?  359 ASP   K N   1 
ATOM   17462 C CA  . ASP   K  1 359 ? 35.39356  -12.20712 39.54939  1.000 97.91216  ?  359 ASP   K CA  1 
ATOM   17463 C C   . ASP   K  1 359 ? 35.76128  -12.42605 38.08402  1.000 80.06530  ?  359 ASP   K C   1 
ATOM   17464 O O   . ASP   K  1 359 ? 35.94808  -13.56643 37.64382  1.000 86.82883  ?  359 ASP   K O   1 
ATOM   17465 C CB  . ASP   K  1 359 ? 33.86928  -12.13266 39.71126  1.000 76.97543  ?  359 ASP   K CB  1 
ATOM   17466 C CG  . ASP   K  1 359 ? 33.41672  -12.18622 41.17719  1.000 114.26455 ?  359 ASP   K CG  1 
ATOM   17467 O OD1 . ASP   K  1 359 ? 34.23928  -12.54210 42.05270  1.000 94.28905  ?  359 ASP   K OD1 1 
ATOM   17468 O OD2 . ASP   K  1 359 ? 32.23593  -11.85065 41.45685  1.000 87.99938  -1 359 ASP   K OD2 1 
ATOM   17469 N N   . ASN   K  1 360 ? 35.88564  -11.35228 37.31760  1.000 85.41396  ?  360 ASN   K N   1 
ATOM   17470 C CA  . ASN   K  1 360 ? 36.28670  -11.46858 35.92067  1.000 76.66598  ?  360 ASN   K CA  1 
ATOM   17471 C C   . ASN   K  1 360 ? 37.78869  -11.74474 35.85204  1.000 87.63101  ?  360 ASN   K C   1 
ATOM   17472 O O   . ASN   K  1 360 ? 38.60390  -10.86008 36.14700  1.000 98.30382  ?  360 ASN   K O   1 
ATOM   17473 C CB  . ASN   K  1 360 ? 35.91663  -10.19494 35.16271  1.000 77.94652  ?  360 ASN   K CB  1 
ATOM   17474 C CG  . ASN   K  1 360 ? 36.08219  -10.34298 33.67987  1.000 96.73247  ?  360 ASN   K CG  1 
ATOM   17475 O OD1 . ASN   K  1 360 ? 37.08504  -10.88745 33.20262  1.000 99.83683  ?  360 ASN   K OD1 1 
ATOM   17476 N ND2 . ASN   K  1 360 ? 35.08861  -9.87389  32.92797  1.000 102.69550 ?  360 ASN   K ND2 1 
ATOM   17477 N N   . LYS   K  1 361 ? 38.15331  -12.96221 35.43298  1.000 80.45475  ?  361 LYS   K N   1 
ATOM   17478 C CA  . LYS   K  1 361 ? 39.55554  -13.37319 35.40665  1.000 88.22362  ?  361 LYS   K CA  1 
ATOM   17479 C C   . LYS   K  1 361 ? 40.41696  -12.48114 34.51759  1.000 60.54073  ?  361 LYS   K C   1 
ATOM   17480 O O   . LYS   K  1 361 ? 41.63097  -12.38855 34.74443  1.000 110.92402 ?  361 LYS   K O   1 
ATOM   17481 C CB  . LYS   K  1 361 ? 39.66624  -14.83603 34.95747  1.000 64.69727  ?  361 LYS   K CB  1 
ATOM   17482 N N   . GLU   K  1 362 ? 39.82051  -11.80812 33.53367  1.000 81.04329  ?  362 GLU   K N   1 
ATOM   17483 C CA  . GLU   K  1 362 ? 40.56025  -10.89712 32.66425  1.000 76.50691  ?  362 GLU   K CA  1 
ATOM   17484 C C   . GLU   K  1 362 ? 40.92850  -9.58888  33.35630  1.000 96.78915  ?  362 GLU   K C   1 
ATOM   17485 O O   . GLU   K  1 362 ? 41.72942  -8.81565  32.81064  1.000 89.05164  ?  362 GLU   K O   1 
ATOM   17486 C CB  . GLU   K  1 362 ? 39.74716  -10.59580 31.39634  1.000 85.36549  ?  362 GLU   K CB  1 
ATOM   17487 N N   . ILE   K  1 363 ? 40.33243  -9.31139  34.51300  1.000 76.59501  ?  363 ILE   K N   1 
ATOM   17488 C CA  . ILE   K  1 363 ? 40.70735  -8.18278  35.34903  1.000 94.56302  ?  363 ILE   K CA  1 
ATOM   17489 C C   . ILE   K  1 363 ? 41.59028  -8.64011  36.50200  1.000 83.05451  ?  363 ILE   K C   1 
ATOM   17490 O O   . ILE   K  1 363 ? 42.63704  -8.04779  36.77314  1.000 91.40763  ?  363 ILE   K O   1 
ATOM   17491 C CB  . ILE   K  1 363 ? 39.42586  -7.46540  35.84251  1.000 84.79951  ?  363 ILE   K CB  1 
ATOM   17492 C CG1 . ILE   K  1 363 ? 38.74097  -6.73820  34.68104  1.000 78.70684  ?  363 ILE   K CG1 1 
ATOM   17493 C CG2 . ILE   K  1 363 ? 39.73155  -6.45880  36.93198  1.000 64.58271  ?  363 ILE   K CG2 1 
ATOM   17494 C CD1 . ILE   K  1 363 ? 37.41530  -6.08252  35.06002  1.000 82.10835  ?  363 ILE   K CD1 1 
ATOM   17495 N N   . GLY   K  1 364 ? 41.18895  -9.72818  37.14689  1.000 78.74385  ?  364 GLY   K N   1 
ATOM   17496 C CA  . GLY   K  1 364 ? 42.04485  -10.42213 38.05989  1.000 66.63960  ?  364 GLY   K CA  1 
ATOM   17497 C C   . GLY   K  1 364 ? 42.32601  -9.63920  39.32593  1.000 111.88253 ?  364 GLY   K C   1 
ATOM   17498 O O   . GLY   K  1 364 ? 41.45722  -8.95886  39.88911  1.000 76.47332  ?  364 GLY   K O   1 
ATOM   17499 N N   . LEU   K  1 365 ? 43.56757  -9.75997  39.78770  1.000 83.26689  ?  365 LEU   K N   1 
ATOM   17500 C CA  . LEU   K  1 365 ? 43.97729  -9.08055  41.00450  1.000 60.15484  ?  365 LEU   K CA  1 
ATOM   17501 C C   . LEU   K  1 365 ? 44.13464  -7.59183  40.72046  1.000 84.81049  ?  365 LEU   K C   1 
ATOM   17502 O O   . LEU   K  1 365 ? 44.79225  -7.20024  39.74937  1.000 72.11167  ?  365 LEU   K O   1 
ATOM   17503 C CB  . LEU   K  1 365 ? 45.28770  -9.67511  41.52568  1.000 74.25769  ?  365 LEU   K CB  1 
ATOM   17504 C CG  . LEU   K  1 365 ? 45.68780  -9.22762  42.93402  1.000 77.81618  ?  365 LEU   K CG  1 
ATOM   17505 C CD1 . LEU   K  1 365 ? 44.62118  -9.66701  43.94215  1.000 65.05067  ?  365 LEU   K CD1 1 
ATOM   17506 C CD2 . LEU   K  1 365 ? 47.05535  -9.76732  43.29123  1.000 64.08799  ?  365 LEU   K CD2 1 
ATOM   17507 N N   . ILE   K  1 366 ? 43.48816  -6.76319  41.54013  1.000 57.09747  ?  366 ILE   K N   1 
ATOM   17508 C CA  . ILE   K  1 366 ? 43.64742  -5.31789  41.48126  1.000 71.42577  ?  366 ILE   K CA  1 
ATOM   17509 C C   . ILE   K  1 366 ? 44.03153  -4.86211  42.87714  1.000 73.73775  ?  366 ILE   K C   1 
ATOM   17510 O O   . ILE   K  1 366 ? 43.93285  -5.61560  43.84957  1.000 69.26228  ?  366 ILE   K O   1 
ATOM   17511 C CB  . ILE   K  1 366 ? 42.37397  -4.57474  41.00602  1.000 64.78785  ?  366 ILE   K CB  1 
ATOM   17512 C CG1 . ILE   K  1 366 ? 41.25295  -4.72565  42.02600  1.000 68.31224  ?  366 ILE   K CG1 1 
ATOM   17513 C CG2 . ILE   K  1 366 ? 41.90822  -5.05800  39.64952  1.000 56.73127  ?  366 ILE   K CG2 1 
ATOM   17514 C CD1 . ILE   K  1 366 ? 40.17381  -3.69955  41.84990  1.000 69.08242  ?  366 ILE   K CD1 1 
ATOM   17515 N N   . PHE   K  1 367 ? 44.46888  -3.61265  42.98073  1.000 57.21266  ?  367 PHE   K N   1 
ATOM   17516 C CA  . PHE   K  1 367 ? 44.63951  -3.04214  44.30549  1.000 54.18109  ?  367 PHE   K CA  1 
ATOM   17517 C C   . PHE   K  1 367 ? 43.98301  -1.67079  44.37528  1.000 63.45602  ?  367 PHE   K C   1 
ATOM   17518 O O   . PHE   K  1 367 ? 43.78650  -0.98308  43.36754  1.000 58.96247  ?  367 PHE   K O   1 
ATOM   17519 C CB  . PHE   K  1 367 ? 46.14567  -3.00126  44.76181  1.000 53.14913  ?  367 PHE   K CB  1 
ATOM   17520 C CG  . PHE   K  1 367 ? 47.00424  -1.93035  44.10597  1.000 45.15411  ?  367 PHE   K CG  1 
ATOM   17521 C CD1 . PHE   K  1 367 ? 46.81943  -0.57491  44.39558  1.000 61.44706  ?  367 PHE   K CD1 1 
ATOM   17522 C CD2 . PHE   K  1 367 ? 48.07117  -2.29089  43.28233  1.000 56.59565  ?  367 PHE   K CD2 1 
ATOM   17523 C CE1 . PHE   K  1 367 ? 47.63097  0.40523   43.82150  1.000 45.60299  ?  367 PHE   K CE1 1 
ATOM   17524 C CE2 . PHE   K  1 367 ? 48.90846  -1.31394  42.70631  1.000 54.65693  ?  367 PHE   K CE2 1 
ATOM   17525 C CZ  . PHE   K  1 367 ? 48.69525  0.03295   42.97537  1.000 51.37909  ?  367 PHE   K CZ  1 
ATOM   17526 N N   . LEU   K  1 368 ? 43.60210  -1.32111  45.58996  1.000 60.46733  ?  368 LEU   K N   1 
ATOM   17527 C CA  . LEU   K  1 368 ? 43.17355  0.00855   45.96868  1.000 51.42331  ?  368 LEU   K CA  1 
ATOM   17528 C C   . LEU   K  1 368 ? 44.08354  0.46874   47.10138  1.000 52.17224  ?  368 LEU   K C   1 
ATOM   17529 O O   . LEU   K  1 368 ? 44.41911  -0.32219  47.99241  1.000 60.68396  ?  368 LEU   K O   1 
ATOM   17530 C CB  . LEU   K  1 368 ? 41.71077  -0.01299  46.42346  1.000 49.08801  ?  368 LEU   K CB  1 
ATOM   17531 C CG  . LEU   K  1 368 ? 40.66950  -0.19082  45.32625  1.000 59.68427  ?  368 LEU   K CG  1 
ATOM   17532 C CD1 . LEU   K  1 368 ? 39.34640  -0.60475  45.94188  1.000 55.46522  ?  368 LEU   K CD1 1 
ATOM   17533 C CD2 . LEU   K  1 368 ? 40.49820  1.11062   44.54118  1.000 57.11913  ?  368 LEU   K CD2 1 
ATOM   17534 N N   . VAL   K  1 369 ? 44.50975  1.72840   47.06511  1.000 35.92602  ?  369 VAL   K N   1 
ATOM   17535 C CA  . VAL   K  1 369 ? 45.16473  2.35344   48.21119  1.000 38.26595  ?  369 VAL   K CA  1 
ATOM   17536 C C   . VAL   K  1 369 ? 44.34405  3.57595   48.60801  1.000 35.75014  ?  369 VAL   K C   1 
ATOM   17537 O O   . VAL   K  1 369 ? 44.14545  4.48797   47.79282  1.000 45.19708  ?  369 VAL   K O   1 
ATOM   17538 C CB  . VAL   K  1 369 ? 46.62281  2.74768   47.91774  1.000 44.49749  ?  369 VAL   K CB  1 
ATOM   17539 C CG1 . VAL   K  1 369 ? 47.27220  3.32121   49.19400  1.000 34.26499  ?  369 VAL   K CG1 1 
ATOM   17540 C CG2 . VAL   K  1 369 ? 47.40704  1.56126   47.39903  1.000 41.65880  ?  369 VAL   K CG2 1 
ATOM   17541 N N   . PHE   K  1 370 ? 43.88104  3.60733   49.85605  1.000 54.70534  ?  370 PHE   K N   1 
ATOM   17542 C CA  . PHE   K  1 370 ? 43.19726  4.78153   50.38815  1.000 36.35040  ?  370 PHE   K CA  1 
ATOM   17543 C C   . PHE   K  1 370 ? 44.20409  5.62836   51.16699  1.000 50.19116  ?  370 PHE   K C   1 
ATOM   17544 O O   . PHE   K  1 370 ? 44.81557  5.15348   52.13363  1.000 48.41388  ?  370 PHE   K O   1 
ATOM   17545 C CB  . PHE   K  1 370 ? 41.99891  4.35363   51.23687  1.000 43.83421  ?  370 PHE   K CB  1 
ATOM   17546 C CG  . PHE   K  1 370 ? 40.98536  3.58825   50.44864  1.000 53.84178  ?  370 PHE   K CG  1 
ATOM   17547 C CD1 . PHE   K  1 370 ? 40.11855  4.25385   49.58781  1.000 44.36664  ?  370 PHE   K CD1 1 
ATOM   17548 C CD2 . PHE   K  1 370 ? 40.94076  2.19939   50.50231  1.000 58.62912  ?  370 PHE   K CD2 1 
ATOM   17549 C CE1 . PHE   K  1 370 ? 39.19923  3.55036   48.80779  1.000 54.52574  ?  370 PHE   K CE1 1 
ATOM   17550 C CE2 . PHE   K  1 370 ? 40.00942  1.48065   49.72845  1.000 43.01132  ?  370 PHE   K CE2 1 
ATOM   17551 C CZ  . PHE   K  1 370 ? 39.14859  2.15729   48.87546  1.000 54.01931  ?  370 PHE   K CZ  1 
ATOM   17552 N N   . ILE   K  1 371 ? 44.39585  6.86958   50.72689  1.000 39.36578  ?  371 ILE   K N   1 
ATOM   17553 C CA  . ILE   K  1 371 ? 45.55252  7.68318   51.10522  1.000 35.14449  ?  371 ILE   K CA  1 
ATOM   17554 C C   . ILE   K  1 371 ? 45.08350  8.82695   52.00036  1.000 36.06422  ?  371 ILE   K C   1 
ATOM   17555 O O   . ILE   K  1 371 ? 44.26625  9.66140   51.58608  1.000 45.97150  ?  371 ILE   K O   1 
ATOM   17556 C CB  . ILE   K  1 371 ? 46.28444  8.21225   49.85971  1.000 44.25996  ?  371 ILE   K CB  1 
ATOM   17557 C CG1 . ILE   K  1 371 ? 46.64254  7.04545   48.92307  1.000 33.84768  ?  371 ILE   K CG1 1 
ATOM   17558 C CG2 . ILE   K  1 371 ? 47.53055  9.01896   50.25114  1.000 29.73283  ?  371 ILE   K CG2 1 
ATOM   17559 C CD1 . ILE   K  1 371 ? 46.70406  7.44893   47.46298  1.000 31.71484  ?  371 ILE   K CD1 1 
ATOM   17560 N N   . GLY   K  1 372 ? 45.60326  8.86830   53.23157  1.000 33.80827  ?  372 GLY   K N   1 
ATOM   17561 C CA  . GLY   K  1 372 ? 45.27348  9.95292   54.13514  1.000 25.10589  ?  372 GLY   K CA  1 
ATOM   17562 C C   . GLY   K  1 372 ? 45.90914  11.26952  53.72262  1.000 33.43463  ?  372 GLY   K C   1 
ATOM   17563 O O   . GLY   K  1 372 ? 46.88242  11.32023  52.96978  1.000 33.60679  ?  372 GLY   K O   1 
ATOM   17564 N N   . MET   K  1 373 ? 45.31718  12.35314  54.21324  1.000 32.55305  ?  373 MET   K N   1 
ATOM   17565 C CA  . MET   K  1 373 ? 45.84239  13.69917  54.01453  1.000 45.58855  ?  373 MET   K CA  1 
ATOM   17566 C C   . MET   K  1 373 ? 45.60267  14.48004  55.28994  1.000 43.34040  ?  373 MET   K C   1 
ATOM   17567 O O   . MET   K  1 373 ? 44.44693  14.63688  55.70513  1.000 38.63250  ?  373 MET   K O   1 
ATOM   17568 C CB  . MET   K  1 373 ? 45.17851  14.40390  52.83511  1.000 25.59222  ?  373 MET   K CB  1 
ATOM   17569 C CG  . MET   K  1 373 ? 45.44680  13.71610  51.52894  1.000 47.41623  ?  373 MET   K CG  1 
ATOM   17570 S SD  . MET   K  1 373 ? 44.55495  14.46637  50.13510  1.000 40.92629  ?  373 MET   K SD  1 
ATOM   17571 C CE  . MET   K  1 373 ? 45.01220  16.19036  50.31562  1.000 16.70769  ?  373 MET   K CE  1 
ATOM   17572 N N   . THR   K  1 374 ? 46.69418  14.97447  55.88924  1.000 32.97206  ?  374 THR   K N   1 
ATOM   17573 C CA  . THR   K  1 374 ? 46.68888  15.68078  57.17136  1.000 34.34375  ?  374 THR   K CA  1 
ATOM   17574 C C   . THR   K  1 374 ? 45.71152  15.02111  58.14527  1.000 31.25233  ?  374 THR   K C   1 
ATOM   17575 O O   . THR   K  1 374 ? 45.79782  13.81224  58.37540  1.000 41.87383  ?  374 THR   K O   1 
ATOM   17576 C CB  . THR   K  1 374 ? 46.40523  17.18841  56.96505  1.000 43.32155  ?  374 THR   K CB  1 
ATOM   17577 O OG1 . THR   K  1 374 ? 45.08892  17.41716  56.43220  1.000 38.27402  ?  374 THR   K OG1 1 
ATOM   17578 C CG2 . THR   K  1 374 ? 47.41814  17.77526  55.99593  1.000 27.89451  ?  374 THR   K CG2 1 
ATOM   17579 N N   . GLU   K  1 375 ? 44.76935  15.77458  58.70687  1.000 41.91118  ?  375 GLU   K N   1 
ATOM   17580 C CA  . GLU   K  1 375 ? 43.90365  15.21290  59.74394  1.000 29.44262  ?  375 GLU   K CA  1 
ATOM   17581 C C   . GLU   K  1 375 ? 42.82593  14.25692  59.21547  1.000 44.28972  ?  375 GLU   K C   1 
ATOM   17582 O O   . GLU   K  1 375 ? 42.17481  13.58024  60.02467  1.000 30.38329  ?  375 GLU   K O   1 
ATOM   17583 C CB  . GLU   K  1 375 ? 43.23107  16.34208  60.52883  1.000 42.30034  ?  375 GLU   K CB  1 
ATOM   17584 C CG  . GLU   K  1 375 ? 42.33709  17.25639  59.65510  1.000 30.95657  ?  375 GLU   K CG  1 
ATOM   17585 C CD  . GLU   K  1 375 ? 43.02790  18.58440  59.28350  1.000 41.31803  ?  375 GLU   K CD  1 
ATOM   17586 O OE1 . GLU   K  1 375 ? 44.04992  18.55464  58.55786  1.000 46.65185  ?  375 GLU   K OE1 1 
ATOM   17587 O OE2 . GLU   K  1 375 ? 42.54479  19.65995  59.72414  1.000 45.69458  -1 375 GLU   K OE2 1 
ATOM   17588 N N   . ILE   K  1 376 ? 42.59418  14.18456  57.90202  1.000 30.07982  ?  376 ILE   K N   1 
ATOM   17589 C CA  . ILE   K  1 376 ? 41.65876  13.18867  57.38207  1.000 30.30553  ?  376 ILE   K CA  1 
ATOM   17590 C C   . ILE   K  1 376 ? 42.45415  11.97509  56.90927  1.000 34.17625  ?  376 ILE   K C   1 
ATOM   17591 O O   . ILE   K  1 376 ? 42.70309  11.80158  55.71105  1.000 41.73477  ?  376 ILE   K O   1 
ATOM   17592 C CB  . ILE   K  1 376 ? 40.77810  13.77407  56.26344  1.000 41.22541  ?  376 ILE   K CB  1 
ATOM   17593 C CG1 . ILE   K  1 376 ? 40.08250  15.04543  56.77444  1.000 30.65791  ?  376 ILE   K CG1 1 
ATOM   17594 C CG2 . ILE   K  1 376 ? 39.77185  12.72724  55.75852  1.000 19.29865  ?  376 ILE   K CG2 1 
ATOM   17595 C CD1 . ILE   K  1 376 ? 39.40496  15.86563  55.67764  1.000 51.48740  ?  376 ILE   K CD1 1 
ATOM   17596 N N   . SER   K  1 377 ? 42.87231  11.12968  57.85297  1.000 36.24866  ?  377 SER   K N   1 
ATOM   17597 C CA  . SER   K  1 377 ? 43.82195  10.06956  57.54627  1.000 49.78753  ?  377 SER   K CA  1 
ATOM   17598 C C   . SER   K  1 377 ? 43.43981  8.71419   58.12147  1.000 33.77413  ?  377 SER   K C   1 
ATOM   17599 O O   . SER   K  1 377 ? 44.20393  7.75542   57.96409  1.000 58.00919  ?  377 SER   K O   1 
ATOM   17600 C CB  . SER   K  1 377 ? 45.22613  10.45898  58.02975  1.000 27.62730  ?  377 SER   K CB  1 
ATOM   17601 O OG  . SER   K  1 377 ? 45.74066  11.48270  57.19223  1.000 33.70495  ?  377 SER   K OG  1 
ATOM   17602 N N   . THR   K  1 378 ? 42.28355  8.60055   58.76127  1.000 57.01190  ?  378 THR   K N   1 
ATOM   17603 C CA  . THR   K  1 378 ? 41.80102  7.30554   59.21625  1.000 43.13744  ?  378 THR   K CA  1 
ATOM   17604 C C   . THR   K  1 378 ? 41.06440  6.57377   58.08958  1.000 58.49756  ?  378 THR   K C   1 
ATOM   17605 O O   . THR   K  1 378 ? 40.16605  7.13241   57.43879  1.000 50.23178  ?  378 THR   K O   1 
ATOM   17606 C CB  . THR   K  1 378 ? 40.89562  7.47557   60.43517  1.000 55.66022  ?  378 THR   K CB  1 
ATOM   17607 O OG1 . THR   K  1 378 ? 41.68165  7.92530   61.54719  1.000 50.45432  ?  378 THR   K OG1 1 
ATOM   17608 C CG2 . THR   K  1 378 ? 40.27523  6.15584   60.78971  1.000 30.87194  ?  378 THR   K CG2 1 
ATOM   17609 N N   . CYS   K  1 379 ? 41.45068  5.31615   57.86636  1.000 43.27607  ?  379 CYS   K N   1 
ATOM   17610 C CA  . CYS   K  1 379 ? 40.92682  4.48848   56.78013  1.000 41.55823  ?  379 CYS   K CA  1 
ATOM   17611 C C   . CYS   K  1 379 ? 40.24160  3.28587   57.41757  1.000 49.62828  ?  379 CYS   K C   1 
ATOM   17612 O O   . CYS   K  1 379 ? 40.90048  2.31781   57.81217  1.000 54.99087  ?  379 CYS   K O   1 
ATOM   17613 C CB  . CYS   K  1 379 ? 42.04404  4.05699   55.83242  1.000 42.13952  ?  379 CYS   K CB  1 
ATOM   17614 S SG  . CYS   K  1 379 ? 42.93912  5.44589   55.07971  1.000 53.66474  ?  379 CYS   K SG  1 
ATOM   17615 N N   . GLU   K  1 380 ? 38.92058  3.34426   57.53046  1.000 56.04003  ?  380 GLU   K N   1 
ATOM   17616 C CA  . GLU   K  1 380 ? 38.15287  2.23526   58.07726  1.000 41.54384  ?  380 GLU   K CA  1 
ATOM   17617 C C   . GLU   K  1 380 ? 37.61514  1.36966   56.94400  1.000 57.83652  ?  380 GLU   K C   1 
ATOM   17618 O O   . GLU   K  1 380 ? 36.80850  1.83699   56.12641  1.000 56.69622  ?  380 GLU   K O   1 
ATOM   17619 C CB  . GLU   K  1 380 ? 36.99644  2.71313   58.94712  1.000 53.02042  ?  380 GLU   K CB  1 
ATOM   17620 C CG  . GLU   K  1 380 ? 36.19554  1.53158   59.42590  1.000 65.79124  ?  380 GLU   K CG  1 
ATOM   17621 C CD  . GLU   K  1 380 ? 34.95925  1.90455   60.18832  1.000 61.56568  ?  380 GLU   K CD  1 
ATOM   17622 O OE1 . GLU   K  1 380 ? 34.59733  3.10375   60.19070  1.000 66.59163  ?  380 GLU   K OE1 1 
ATOM   17623 O OE2 . GLU   K  1 380 ? 34.35552  0.97936   60.77526  1.000 73.68205  -1 380 GLU   K OE2 1 
ATOM   17624 N N   . ALA   K  1 381 ? 38.06575  0.11376   56.90127  1.000 55.06667  ?  381 ALA   K N   1 
ATOM   17625 C CA  . ALA   K  1 381 ? 37.41949  -0.90477  56.08234  1.000 73.56483  ?  381 ALA   K CA  1 
ATOM   17626 C C   . ALA   K  1 381 ? 36.18855  -1.44305  56.81224  1.000 63.95461  ?  381 ALA   K C   1 
ATOM   17627 O O   . ALA   K  1 381 ? 36.24448  -1.74360  58.01292  1.000 64.57014  ?  381 ALA   K O   1 
ATOM   17628 C CB  . ALA   K  1 381 ? 38.39550  -2.04552  55.77325  1.000 54.04646  ?  381 ALA   K CB  1 
ATOM   17629 N N   . THR   K  1 382 ? 35.07274  -1.55474  56.09267  1.000 57.58936  ?  382 THR   K N   1 
ATOM   17630 C CA  . THR   K  1 382 ? 33.89160  -2.24853  56.60163  1.000 57.17141  ?  382 THR   K CA  1 
ATOM   17631 C C   . THR   K  1 382 ? 33.66927  -3.59861  55.91871  1.000 52.30462  ?  382 THR   K C   1 
ATOM   17632 O O   . THR   K  1 382 ? 32.56682  -4.15290  55.98005  1.000 79.84670  ?  382 THR   K O   1 
ATOM   17633 C CB  . THR   K  1 382 ? 32.65973  -1.36296  56.45145  1.000 46.88386  ?  382 THR   K CB  1 
ATOM   17634 O OG1 . THR   K  1 382 ? 32.47791  -1.01317  55.06343  1.000 55.77557  ?  382 THR   K OG1 1 
ATOM   17635 C CG2 . THR   K  1 382 ? 32.83004  -0.09552  57.29294  1.000 57.67150  ?  382 THR   K CG2 1 
ATOM   17636 N N   . VAL   K  1 383 ? 34.68909  -4.11297  55.23533  1.000 60.70975  ?  383 VAL   K N   1 
ATOM   17637 C CA  . VAL   K  1 383 ? 34.67213  -5.44602  54.65784  1.000 50.04797  ?  383 VAL   K CA  1 
ATOM   17638 C C   . VAL   K  1 383 ? 35.80468  -6.24105  55.29562  1.000 64.04998  ?  383 VAL   K C   1 
ATOM   17639 O O   . VAL   K  1 383 ? 36.70457  -5.68964  55.93344  1.000 59.80179  ?  383 VAL   K O   1 
ATOM   17640 C CB  . VAL   K  1 383 ? 34.81214  -5.44150  53.12286  1.000 70.76035  ?  383 VAL   K CB  1 
ATOM   17641 C CG1 . VAL   K  1 383 ? 33.62551  -4.76842  52.48456  1.000 50.81363  ?  383 VAL   K CG1 1 
ATOM   17642 C CG2 . VAL   K  1 383 ? 36.11169  -4.76612  52.70958  1.000 55.52269  ?  383 VAL   K CG2 1 
ATOM   17643 N N   . SER   K  1 384 ? 35.74460  -7.55556  55.12157  1.000 72.03733  ?  384 SER   K N   1 
ATOM   17644 C CA  . SER   K  1 384 ? 36.70162  -8.46235  55.73774  1.000 52.55825  ?  384 SER   K CA  1 
ATOM   17645 C C   . SER   K  1 384 ? 37.43593  -9.23813  54.65752  1.000 76.95559  ?  384 SER   K C   1 
ATOM   17646 O O   . SER   K  1 384 ? 36.91646  -9.44074  53.54916  1.000 65.72169  ?  384 SER   K O   1 
ATOM   17647 C CB  . SER   K  1 384 ? 36.00307  -9.43148  56.69385  1.000 54.95500  ?  384 SER   K CB  1 
ATOM   17648 O OG  . SER   K  1 384 ? 35.19277  -8.70960  57.61263  1.000 82.16069  ?  384 SER   K OG  1 
ATOM   17649 N N   . GLU   K  1 385 ? 38.65495  -9.66524  54.97378  1.000 77.86183  ?  385 GLU   K N   1 
ATOM   17650 C CA  . GLU   K  1 385 ? 39.35018  -10.53162 54.03218  1.000 86.59015  ?  385 GLU   K CA  1 
ATOM   17651 C C   . GLU   K  1 385 ? 38.50047  -11.77814 53.78040  1.000 86.20734  ?  385 GLU   K C   1 
ATOM   17652 O O   . GLU   K  1 385 ? 37.85419  -12.31415 54.68939  1.000 84.16331  ?  385 GLU   K O   1 
ATOM   17653 C CB  . GLU   K  1 385 ? 40.73595  -10.89401 54.56319  1.000 64.53017  ?  385 GLU   K CB  1 
ATOM   17654 C CG  . GLU   K  1 385 ? 41.60965  -9.67763  54.89130  1.000 78.32982  ?  385 GLU   K CG  1 
ATOM   17655 C CD  . GLU   K  1 385 ? 43.05033  -10.05428 55.23322  1.000 95.23917  ?  385 GLU   K CD  1 
ATOM   17656 O OE1 . GLU   K  1 385 ? 43.27129  -11.22434 55.62767  1.000 93.62823  ?  385 GLU   K OE1 1 
ATOM   17657 O OE2 . GLU   K  1 385 ? 43.95824  -9.18908  55.09763  1.000 80.78989  -1 385 GLU   K OE2 1 
ATOM   17658 N N   . GLY   K  1 386 ? 38.43828  -12.19200 52.52117  1.000 86.42608  ?  386 GLY   K N   1 
ATOM   17659 C CA  . GLY   K  1 386 ? 37.64219  -13.33318 52.12380  1.000 72.58274  ?  386 GLY   K CA  1 
ATOM   17660 C C   . GLY   K  1 386 ? 36.21492  -13.01661 51.71596  1.000 91.29193  ?  386 GLY   K C   1 
ATOM   17661 O O   . GLY   K  1 386 ? 35.59277  -13.81041 51.00745  1.000 85.87672  ?  386 GLY   K O   1 
ATOM   17662 N N   . GLN   K  1 387 ? 35.68337  -11.88408 52.14199  1.000 73.05710  ?  387 GLN   K N   1 
ATOM   17663 C CA  . GLN   K  1 387 ? 34.32182  -11.49707 51.80729  1.000 69.74782  ?  387 GLN   K CA  1 
ATOM   17664 C C   . GLN   K  1 387 ? 34.16584  -11.21282 50.31104  1.000 88.98301  ?  387 GLN   K C   1 
ATOM   17665 O O   . GLN   K  1 387 ? 35.10390  -10.76733 49.63681  1.000 82.11948  ?  387 GLN   K O   1 
ATOM   17666 C CB  . GLN   K  1 387 ? 33.95371  -10.26421 52.62536  1.000 68.60350  ?  387 GLN   K CB  1 
ATOM   17667 C CG  . GLN   K  1 387 ? 32.61187  -9.68662  52.37558  1.000 69.16721  ?  387 GLN   K CG  1 
ATOM   17668 C CD  . GLN   K  1 387 ? 32.36332  -8.52585  53.29950  1.000 77.16767  ?  387 GLN   K CD  1 
ATOM   17669 O OE1 . GLN   K  1 387 ? 33.07211  -8.34974  54.30389  1.000 82.13084  ?  387 GLN   K OE1 1 
ATOM   17670 N NE2 . GLN   K  1 387 ? 31.37496  -7.70485  52.95928  1.000 70.54783  ?  387 GLN   K NE2 1 
ATOM   17671 N N   . HIS   K  1 388 ? 32.96580  -11.48768 49.78646  1.000 64.84400  ?  388 HIS   K N   1 
ATOM   17672 C CA  . HIS   K  1 388 ? 32.62032  -11.13365 48.41352  1.000 76.13783  ?  388 HIS   K CA  1 
ATOM   17673 C C   . HIS   K  1 388 ? 31.82244  -9.83706  48.40264  1.000 89.78747  ?  388 HIS   K C   1 
ATOM   17674 O O   . HIS   K  1 388 ? 31.04225  -9.56423  49.32295  1.000 63.87053  ?  388 HIS   K O   1 
ATOM   17675 C CB  . HIS   K  1 388 ? 31.80958  -12.22937 47.73428  1.000 54.15493  ?  388 HIS   K CB  1 
ATOM   17676 C CG  . HIS   K  1 388 ? 31.50779  -11.95785 46.29368  1.000 71.48750  ?  388 HIS   K CG  1 
ATOM   17677 N ND1 . HIS   K  1 388 ? 30.38716  -11.26221 45.88030  1.000 72.44596  ?  388 HIS   K ND1 1 
ATOM   17678 C CD2 . HIS   K  1 388 ? 32.18016  -12.29354 45.16623  1.000 60.41875  ?  388 HIS   K CD2 1 
ATOM   17679 C CE1 . HIS   K  1 388 ? 30.38829  -11.17510 44.56077  1.000 68.76167  ?  388 HIS   K CE1 1 
ATOM   17680 N NE2 . HIS   K  1 388 ? 31.46305  -11.79605 44.10203  1.000 64.70273  ?  388 HIS   K NE2 1 
ATOM   17681 N N   . VAL   K  1 389 ? 32.04073  -9.02970  47.36518  1.000 69.99581  ?  389 VAL   K N   1 
ATOM   17682 C CA  . VAL   K  1 389 ? 31.34094  -7.76122  47.19061  1.000 82.39900  ?  389 VAL   K CA  1 
ATOM   17683 C C   . VAL   K  1 389 ? 31.00850  -7.59225  45.71543  1.000 81.34259  ?  389 VAL   K C   1 
ATOM   17684 O O   . VAL   K  1 389 ? 31.67355  -8.15236  44.83219  1.000 95.47609  ?  389 VAL   K O   1 
ATOM   17685 C CB  . VAL   K  1 389 ? 32.15597  -6.53831  47.70343  1.000 87.58586  ?  389 VAL   K CB  1 
ATOM   17686 C CG1 . VAL   K  1 389 ? 32.41460  -6.63698  49.22527  1.000 72.38464  ?  389 VAL   K CG1 1 
ATOM   17687 C CG2 . VAL   K  1 389 ? 33.46332  -6.38573  46.94273  1.000 66.67204  ?  389 VAL   K CG2 1 
ATOM   17688 N N   . ASN   K  1 390 ? 29.95682  -6.81725  45.46292  1.000 75.97960  ?  390 ASN   K N   1 
ATOM   17689 C CA  . ASN   K  1 390 ? 29.56813  -6.39192  44.12462  1.000 79.44296  ?  390 ASN   K CA  1 
ATOM   17690 C C   . ASN   K  1 390 ? 29.97014  -4.94413  43.90745  1.000 104.80585 ?  390 ASN   K C   1 
ATOM   17691 O O   . ASN   K  1 390 ? 29.97548  -4.13457  44.84308  1.000 82.27972  ?  390 ASN   K O   1 
ATOM   17692 C CB  . ASN   K  1 390 ? 28.05770  -6.53681  43.90100  1.000 92.14346  ?  390 ASN   K CB  1 
ATOM   17693 C CG  . ASN   K  1 390 ? 27.61360  -7.99016  43.86380  1.000 85.69140  ?  390 ASN   K CG  1 
ATOM   17694 O OD1 . ASN   K  1 390 ? 28.26054  -8.84478  43.23840  1.000 96.17550  ?  390 ASN   K OD1 1 
ATOM   17695 N ND2 . ASN   K  1 390 ? 26.52693  -8.28428  44.55927  1.000 95.62828  ?  390 ASN   K ND2 1 
ATOM   17696 N N   . ARG   K  1 391 ? 30.32731  -4.63811  42.66179  1.000 81.41767  ?  391 ARG   K N   1 
ATOM   17697 C CA  . ARG   K  1 391 ? 30.60883  -3.27516  42.23590  1.000 92.01235  ?  391 ARG   K CA  1 
ATOM   17698 C C   . ARG   K  1 391 ? 29.55907  -2.31094  42.79012  1.000 80.01968  ?  391 ARG   K C   1 
ATOM   17699 O O   . ARG   K  1 391 ? 28.35544  -2.50620  42.59326  1.000 90.69931  ?  391 ARG   K O   1 
ATOM   17700 C CB  . ARG   K  1 391 ? 30.64352  -3.24611  40.70402  1.000 71.38938  ?  391 ARG   K CB  1 
ATOM   17701 C CG  . ARG   K  1 391 ? 31.22214  -1.99919  40.05429  1.000 81.05945  ?  391 ARG   K CG  1 
ATOM   17702 C CD  . ARG   K  1 391 ? 31.67558  -2.28384  38.62211  1.000 90.64732  ?  391 ARG   K CD  1 
ATOM   17703 N NE  . ARG   K  1 391 ? 30.58812  -2.60897  37.70520  1.000 83.00762  ?  391 ARG   K NE  1 
ATOM   17704 C CZ  . ARG   K  1 391 ? 29.99128  -1.71728  36.92333  1.000 124.57716 ?  391 ARG   K CZ  1 
ATOM   17705 N NH1 . ARG   K  1 391 ? 30.30406  -0.43409  36.97136  1.000 83.97260  ?  391 ARG   K NH1 1 
ATOM   17706 N NH2 . ARG   K  1 391 ? 29.05695  -2.11844  36.07020  1.000 84.92044  ?  391 ARG   K NH2 1 
ATOM   17707 N N   . GLY   K  1 392 ? 30.01436  -1.31592  43.56949  1.000 79.99099  ?  392 GLY   K N   1 
ATOM   17708 C CA  . GLY   K  1 392 ? 29.15491  -0.30740  44.17254  1.000 76.41882  ?  392 GLY   K CA  1 
ATOM   17709 C C   . GLY   K  1 392 ? 28.83653  -0.50676  45.64535  1.000 85.19981  ?  392 GLY   K C   1 
ATOM   17710 O O   . GLY   K  1 392 ? 28.28670  0.41690   46.27269  1.000 83.77554  ?  392 GLY   K O   1 
ATOM   17711 N N   . ASP   K  1 393 ? 29.17033  -1.67081  46.21751  1.000 73.88793  ?  393 ASP   K N   1 
ATOM   17712 C CA  . ASP   K  1 393 ? 28.95577  -1.91882  47.64404  1.000 86.57817  ?  393 ASP   K CA  1 
ATOM   17713 C C   . ASP   K  1 393 ? 29.96036  -1.13418  48.49290  1.000 81.13361  ?  393 ASP   K C   1 
ATOM   17714 O O   . ASP   K  1 393 ? 31.02251  -0.71785  48.01636  1.000 100.18849 ?  393 ASP   K O   1 
ATOM   17715 C CB  . ASP   K  1 393 ? 29.08360  -3.41505  47.96177  1.000 77.21783  ?  393 ASP   K CB  1 
ATOM   17716 C CG  . ASP   K  1 393 ? 28.05612  -4.28580  47.21894  1.000 106.10571 ?  393 ASP   K CG  1 
ATOM   17717 O OD1 . ASP   K  1 393 ? 27.13835  -3.75535  46.54318  1.000 102.70777 ?  393 ASP   K OD1 1 
ATOM   17718 O OD2 . ASP   K  1 393 ? 28.17663  -5.52606  47.31664  1.000 90.80851  -1 393 ASP   K OD2 1 
ATOM   17719 N N   . ASP   K  1 394 ? 29.62932  -0.95329  49.77554  1.000 95.05476  ?  394 ASP   K N   1 
ATOM   17720 C CA  . ASP   K  1 394 ? 30.55501  -0.27896  50.68749  1.000 70.77148  ?  394 ASP   K CA  1 
ATOM   17721 C C   . ASP   K  1 394 ? 31.83594  -1.09507  50.85950  1.000 97.45382  ?  394 ASP   K C   1 
ATOM   17722 O O   . ASP   K  1 394 ? 31.77990  -2.30822  51.08523  1.000 80.27874  ?  394 ASP   K O   1 
ATOM   17723 C CB  . ASP   K  1 394 ? 29.90578  -0.05375  52.05754  1.000 90.26969  ?  394 ASP   K CB  1 
ATOM   17724 C CG  . ASP   K  1 394 ? 28.64592  0.79282   51.99127  1.000 79.77161  ?  394 ASP   K CG  1 
ATOM   17725 O OD1 . ASP   K  1 394 ? 28.58542  1.75276   51.17812  1.000 124.13065 ?  394 ASP   K OD1 1 
ATOM   17726 O OD2 . ASP   K  1 394 ? 27.72196  0.50812   52.78372  1.000 119.38076 -1 394 ASP   K OD2 1 
ATOM   17727 N N   . LEU   K  1 395 ? 32.99594  -0.43821  50.74130  1.000 64.25587  ?  395 LEU   K N   1 
ATOM   17728 C CA  . LEU   K  1 395 ? 34.23702  -1.04734  51.21743  1.000 83.19714  ?  395 LEU   K CA  1 
ATOM   17729 C C   . LEU   K  1 395 ? 34.66230  -0.49257  52.55853  1.000 76.13222  ?  395 LEU   K C   1 
ATOM   17730 O O   . LEU   K  1 395 ? 35.33726  -1.18836  53.33339  1.000 73.59731  ?  395 LEU   K O   1 
ATOM   17731 C CB  . LEU   K  1 395 ? 35.39417  -0.82957  50.23800  1.000 60.66686  ?  395 LEU   K CB  1 
ATOM   17732 C CG  . LEU   K  1 395 ? 35.41211  -1.54893  48.90299  1.000 75.14147  ?  395 LEU   K CG  1 
ATOM   17733 C CD1 . LEU   K  1 395 ? 36.67163  -1.13415  48.21152  1.000 60.13851  ?  395 LEU   K CD1 1 
ATOM   17734 C CD2 . LEU   K  1 395 ? 35.34502  -3.05541  49.09046  1.000 70.16874  ?  395 LEU   K CD2 1 
ATOM   17735 N N   . GLY   K  1 396 ? 34.28235  0.74773   52.83012  1.000 52.11115  ?  396 GLY   K N   1 
ATOM   17736 C CA  . GLY   K  1 396 ? 34.69804  1.41934   54.04349  1.000 60.50976  ?  396 GLY   K CA  1 
ATOM   17737 C C   . GLY   K  1 396 ? 34.58216  2.91257   53.83050  1.000 56.67789  ?  396 GLY   K C   1 
ATOM   17738 O O   . GLY   K  1 396 ? 33.82140  3.36939   52.97118  1.000 60.12898  ?  396 GLY   K O   1 
ATOM   17739 N N   . MET   K  1 397 ? 35.37184  3.65695   54.60121  1.000 59.08831  ?  397 MET   K N   1 
ATOM   17740 C CA  . MET   K  1 397 ? 35.26760  5.10692   54.51858  1.000 57.96521  ?  397 MET   K CA  1 
ATOM   17741 C C   . MET   K  1 397 ? 36.46563  5.76524   55.18489  1.000 73.47557  ?  397 MET   K C   1 
ATOM   17742 O O   . MET   K  1 397 ? 37.22598  5.13144   55.92581  1.000 62.70441  ?  397 MET   K O   1 
ATOM   17743 C CB  . MET   K  1 397 ? 33.97597  5.59390   55.16647  1.000 55.78952  ?  397 MET   K CB  1 
ATOM   17744 C CG  . MET   K  1 397 ? 34.05654  5.67973   56.67999  1.000 60.27038  ?  397 MET   K CG  1 
ATOM   17745 S SD  . MET   K  1 397 ? 32.41487  5.42856   57.32169  1.000 70.67140  ?  397 MET   K SD  1 
ATOM   17746 C CE  . MET   K  1 397 ? 32.23940  3.67038   57.08628  1.000 48.91704  ?  397 MET   K CE  1 
ATOM   17747 N N   . PHE   K  1 398 ? 36.61310  7.05992   54.89857  1.000 48.21467  ?  398 PHE   K N   1 
ATOM   17748 C CA  . PHE   K  1 398 ? 37.55908  7.93935   55.56610  1.000 41.49702  ?  398 PHE   K CA  1 
ATOM   17749 C C   . PHE   K  1 398 ? 36.94411  8.55782   56.82729  1.000 51.27640  ?  398 PHE   K C   1 
ATOM   17750 O O   . PHE   K  1 398 ? 35.73805  8.79567   56.90425  1.000 60.98685  ?  398 PHE   K O   1 
ATOM   17751 C CB  . PHE   K  1 398 ? 37.98635  9.07261   54.62931  1.000 41.57887  ?  398 PHE   K CB  1 
ATOM   17752 C CG  . PHE   K  1 398 ? 38.84231  8.64650   53.47923  1.000 55.22501  ?  398 PHE   K CG  1 
ATOM   17753 C CD1 . PHE   K  1 398 ? 40.19081  8.32316   53.67842  1.000 41.89281  ?  398 PHE   K CD1 1 
ATOM   17754 C CD2 . PHE   K  1 398 ? 38.32685  8.63557   52.17828  1.000 48.65096  ?  398 PHE   K CD2 1 
ATOM   17755 C CE1 . PHE   K  1 398 ? 41.00726  7.95372   52.59868  1.000 53.93287  ?  398 PHE   K CE1 1 
ATOM   17756 C CE2 . PHE   K  1 398 ? 39.13500  8.27244   51.08089  1.000 44.69566  ?  398 PHE   K CE2 1 
ATOM   17757 C CZ  . PHE   K  1 398 ? 40.47375  7.93141   51.29026  1.000 52.03172  ?  398 PHE   K CZ  1 
ATOM   17758 N N   . HIS   K  1 399 ? 37.79418  8.85642   57.80798  1.000 55.28576  ?  399 HIS   K N   1 
ATOM   17759 C CA  . HIS   K  1 399 ? 37.38932  9.65998   58.95614  1.000 63.67947  ?  399 HIS   K CA  1 
ATOM   17760 C C   . HIS   K  1 399 ? 38.48823  10.65652  59.28266  1.000 42.13872  ?  399 HIS   K C   1 
ATOM   17761 O O   . HIS   K  1 399 ? 39.66975  10.40116  59.03625  1.000 70.53729  ?  399 HIS   K O   1 
ATOM   17762 C CB  . HIS   K  1 399 ? 37.13640  8.84843   60.25944  1.000 39.63954  ?  399 HIS   K CB  1 
ATOM   17763 C CG  . HIS   K  1 399 ? 36.15700  7.72263   60.12390  1.000 43.39333  ?  399 HIS   K CG  1 
ATOM   17764 N ND1 . HIS   K  1 399 ? 34.79942  7.88760   60.30112  1.000 51.43825  ?  399 HIS   K ND1 1 
ATOM   17765 C CD2 . HIS   K  1 399 ? 36.34636  6.40474   59.86221  1.000 58.82155  ?  399 HIS   K CD2 1 
ATOM   17766 C CE1 . HIS   K  1 399 ? 34.19239  6.72540   60.13053  1.000 69.09132  ?  399 HIS   K CE1 1 
ATOM   17767 N NE2 . HIS   K  1 399 ? 35.10873  5.80752   59.87269  1.000 40.30228  ?  399 HIS   K NE2 1 
ATOM   17768 N N   . PHE   K  1 400 ? 38.09242  11.77291  59.89173  1.000 56.44738  ?  400 PHE   K N   1 
ATOM   17769 C CA  . PHE   K  1 400 ? 39.04088  12.54790  60.67671  1.000 37.91648  ?  400 PHE   K CA  1 
ATOM   17770 C C   . PHE   K  1 400 ? 39.67772  11.62714  61.71345  1.000 46.54703  ?  400 PHE   K C   1 
ATOM   17771 O O   . PHE   K  1 400 ? 38.97987  10.89520  62.42530  1.000 57.03710  ?  400 PHE   K O   1 
ATOM   17772 C CB  . PHE   K  1 400 ? 38.33405  13.72553  61.35593  1.000 55.59424  ?  400 PHE   K CB  1 
ATOM   17773 C CG  . PHE   K  1 400 ? 38.10424  14.90113  60.45173  1.000 35.52123  ?  400 PHE   K CG  1 
ATOM   17774 C CD1 . PHE   K  1 400 ? 37.14390  14.84475  59.44023  1.000 54.56547  ?  400 PHE   K CD1 1 
ATOM   17775 C CD2 . PHE   K  1 400 ? 38.85337  16.06617  60.59865  1.000 55.55853  ?  400 PHE   K CD2 1 
ATOM   17776 C CE1 . PHE   K  1 400 ? 36.94630  15.92029  58.58309  1.000 39.23339  ?  400 PHE   K CE1 1 
ATOM   17777 C CE2 . PHE   K  1 400 ? 38.65099  17.16060  59.74988  1.000 51.40444  ?  400 PHE   K CE2 1 
ATOM   17778 C CZ  . PHE   K  1 400 ? 37.70112  17.08089  58.74245  1.000 54.31949  ?  400 PHE   K CZ  1 
ATOM   17779 N N   . GLY   K  1 401 ? 40.99778  11.63022  61.76277  1.000 37.50490  ?  401 GLY   K N   1 
ATOM   17780 C CA  . GLY   K  1 401 ? 41.72646  10.77145  62.67643  1.000 33.43342  ?  401 GLY   K CA  1 
ATOM   17781 C C   . GLY   K  1 401 ? 43.08772  10.43791  62.10570  1.000 43.89261  ?  401 GLY   K C   1 
ATOM   17782 O O   . GLY   K  1 401 ? 43.46982  10.90670  61.03363  1.000 50.08544  ?  401 GLY   K O   1 
ATOM   17783 N N   . GLY   K  1 402 ? 43.81449  9.60492   62.85206  1.000 37.10160  ?  402 GLY   K N   1 
ATOM   17784 C CA  . GLY   K  1 402 ? 45.15940  9.19350   62.45875  1.000 29.70727  ?  402 GLY   K CA  1 
ATOM   17785 C C   . GLY   K  1 402 ? 45.19790  7.95414   61.57057  1.000 58.94540  ?  402 GLY   K C   1 
ATOM   17786 O O   . GLY   K  1 402 ? 46.23049  7.56115   60.98574  1.000 40.56349  ?  402 GLY   K O   1 
ATOM   17787 O OXT . GLY   K  1 402 ? 44.16075  7.30245   61.40601  1.000 49.74683  -1 402 GLY   K OXT 1 
ATOM   17788 N N   . SER   L  2 1   ? 42.47934  11.05565  49.57281  1.000 33.64456  ?  404 SER   L N   1 
ATOM   17789 C CA  . SER   L  2 1   ? 42.88581  10.65412  48.21897  1.000 28.76422  ?  404 SER   L CA  1 
ATOM   17790 C C   . SER   L  2 1   ? 42.79021  9.13498   48.03189  1.000 40.18943  ?  404 SER   L C   1 
ATOM   17791 O O   . SER   L  2 1   ? 42.80494  8.39081   49.00838  1.000 43.70486  ?  404 SER   L O   1 
ATOM   17792 C CB  . SER   L  2 1   ? 44.31649  11.14994  47.92241  1.000 35.03943  ?  404 SER   L CB  1 
ATOM   17793 O OG  . SER   L  2 1   ? 44.72788  10.84276  46.59619  1.000 37.77773  ?  404 SER   L OG  1 
ATOM   17794 N N   . PHE   L  2 2   ? 42.68555  8.66336   46.78679  1.000 40.41396  ?  405 PHE   L N   1 
ATOM   17795 C CA  . PHE   L  2 2   ? 42.62922  7.22493   46.53853  1.000 46.68874  ?  405 PHE   L CA  1 
ATOM   17796 C C   . PHE   L  2 2   ? 43.33972  6.89805   45.22964  1.000 44.35964  ?  405 PHE   L C   1 
ATOM   17797 O O   . PHE   L  2 2   ? 43.43252  7.74154   44.32649  1.000 53.65776  ?  405 PHE   L O   1 
ATOM   17798 C CB  . PHE   L  2 2   ? 41.18157  6.70356   46.49640  1.000 47.36956  ?  405 PHE   L CB  1 
ATOM   17799 C CG  . PHE   L  2 2   ? 40.57721  6.70638   45.12185  1.000 49.84194  ?  405 PHE   L CG  1 
ATOM   17800 C CD1 . PHE   L  2 2   ? 40.02876  7.87596   44.58419  1.000 56.13523  ?  405 PHE   L CD1 1 
ATOM   17801 C CD2 . PHE   L  2 2   ? 40.57122  5.53875   44.35506  1.000 53.27729  ?  405 PHE   L CD2 1 
ATOM   17802 C CE1 . PHE   L  2 2   ? 39.47728  7.88818   43.30318  1.000 49.86394  ?  405 PHE   L CE1 1 
ATOM   17803 C CE2 . PHE   L  2 2   ? 40.02460  5.53324   43.06678  1.000 46.00129  ?  405 PHE   L CE2 1 
ATOM   17804 C CZ  . PHE   L  2 2   ? 39.46343  6.72346   42.54202  1.000 52.18923  ?  405 PHE   L CZ  1 
ATOM   17805 N N   . ALA   L  2 3   ? 43.81977  5.65062   45.12543  1.000 37.36587  ?  406 ALA   L N   1 
ATOM   17806 C CA  . ALA   L  2 3   ? 44.46509  5.17984   43.91011  1.000 41.61776  ?  406 ALA   L CA  1 
ATOM   17807 C C   . ALA   L  2 3   ? 43.97878  3.78412   43.55567  1.000 44.75797  ?  406 ALA   L C   1 
ATOM   17808 O O   . ALA   L  2 3   ? 43.85737  2.91138   44.42675  1.000 43.66657  ?  406 ALA   L O   1 
ATOM   17809 C CB  . ALA   L  2 3   ? 45.98383  5.17881   44.03759  1.000 25.41778  ?  406 ALA   L CB  1 
ATOM   17810 N N   . LEU   L  2 4   ? 43.70814  3.59334   42.26069  1.000 59.07731  ?  407 LEU   L N   1 
ATOM   17811 C CA  . LEU   L  2 4   ? 43.34561  2.30890   41.67807  1.000 58.35501  ?  407 LEU   L CA  1 
ATOM   17812 C C   . LEU   L  2 4   ? 44.54875  1.76859   40.91765  1.000 43.57335  ?  407 LEU   L C   1 
ATOM   17813 O O   . LEU   L  2 4   ? 45.15891  2.49821   40.12914  1.000 63.13057  ?  407 LEU   L O   1 
ATOM   17814 C CB  . LEU   L  2 4   ? 42.14344  2.45974   40.74104  1.000 47.30313  ?  407 LEU   L CB  1 
ATOM   17815 C CG  . LEU   L  2 4   ? 41.85639  1.26045   39.83375  1.000 59.03184  ?  407 LEU   L CG  1 
ATOM   17816 C CD1 . LEU   L  2 4   ? 41.35450  0.06555   40.66393  1.000 45.42658  ?  407 LEU   L CD1 1 
ATOM   17817 C CD2 . LEU   L  2 4   ? 40.86949  1.65197   38.75410  1.000 51.37404  ?  407 LEU   L CD2 1 
ATOM   17818 N N   . GLY   L  2 5   ? 44.89570  0.50061   41.16695  1.000 67.53713  ?  408 GLY   L N   1 
ATOM   17819 C CA  . GLY   L  2 5   ? 46.03412  -0.13845  40.51641  1.000 44.24951  ?  408 GLY   L CA  1 
ATOM   17820 C C   . GLY   L  2 5   ? 45.66233  -1.32204  39.63489  1.000 59.77406  ?  408 GLY   L C   1 
ATOM   17821 O O   . GLY   L  2 5   ? 44.95025  -2.24377  40.06553  1.000 66.09876  ?  408 GLY   L O   1 
ATOM   17822 N N   . LEU   L  2 6   ? 46.14027  -1.30071  38.38896  1.000 53.07815  ?  409 LEU   L N   1 
ATOM   17823 C CA  . LEU   L  2 6   ? 45.90337  -2.36231  37.41614  1.000 72.43365  ?  409 LEU   L CA  1 
ATOM   17824 C C   . LEU   L  2 6   ? 47.22493  -2.98876  36.99236  1.000 65.82976  ?  409 LEU   L C   1 
ATOM   17825 O O   . LEU   L  2 6   ? 48.21249  -2.27740  36.75972  1.000 70.89523  ?  409 LEU   L O   1 
ATOM   17826 C CB  . LEU   L  2 6   ? 45.18152  -1.82444  36.17744  1.000 63.71540  ?  409 LEU   L CB  1 
ATOM   17827 C CG  . LEU   L  2 6   ? 43.90361  -1.04103  36.48631  1.000 70.59051  ?  409 LEU   L CG  1 
ATOM   17828 C CD1 . LEU   L  2 6   ? 43.27849  -0.50526  35.20828  1.000 56.67307  ?  409 LEU   L CD1 1 
ATOM   17829 C CD2 . LEU   L  2 6   ? 42.90133  -1.88841  37.29966  1.000 52.22431  ?  409 LEU   L CD2 1 
ATOM   17830 N N   . ARG   L  2 7   ? 47.22872  -4.31699  36.87749  1.000 66.50215  ?  410 ARG   L N   1 
ATOM   17831 C CA  . ARG   L  2 7   ? 48.37281  -5.06544  36.36319  1.000 65.22941  ?  410 ARG   L CA  1 
ATOM   17832 C C   . ARG   L  2 7   ? 48.54856  -4.84178  34.85099  1.000 71.12824  ?  410 ARG   L C   1 
ATOM   17833 O O   . ARG   L  2 7   ? 47.60060  -4.49128  34.13684  1.000 82.39088  ?  410 ARG   L O   1 
ATOM   17834 C CB  . ARG   L  2 7   ? 48.18567  -6.55612  36.67526  1.000 52.07900  ?  410 ARG   L CB  1 
ATOM   17835 C CG  . ARG   L  2 7   ? 48.04251  -6.82570  38.16374  1.000 54.08720  ?  410 ARG   L CG  1 
ATOM   17836 C CD  . ARG   L  2 7   ? 47.71503  -8.26329  38.50994  1.000 65.33263  ?  410 ARG   L CD  1 
ATOM   17837 N NE  . ARG   L  2 7   ? 46.37746  -8.64316  38.08007  1.000 84.42608  ?  410 ARG   L NE  1 
ATOM   17838 C CZ  . ARG   L  2 7   ? 46.10910  -9.33140  36.97731  1.000 75.28630  ?  410 ARG   L CZ  1 
ATOM   17839 N NH1 . ARG   L  2 7   ? 47.07223  -9.80531  36.20426  1.000 78.65029  ?  410 ARG   L NH1 1 
ATOM   17840 N NH2 . ARG   L  2 7   ? 44.84124  -9.53905  36.63408  1.000 84.51402  ?  410 ARG   L NH2 1 
ATOM   17841 N N   . LYS   L  2 8   ? 49.78663  -5.04036  34.35858  1.000 72.93799  ?  411 LYS   L N   1 
ATOM   17842 C CA  . LYS   L  2 8   ? 50.03137  -4.94284  32.91382  1.000 90.99866  ?  411 LYS   L CA  1 
ATOM   17843 C C   . LYS   L  2 8   ? 49.23910  -5.99527  32.15591  1.000 83.22367  ?  411 LYS   L C   1 
ATOM   17844 O O   . LYS   L  2 8   ? 48.61332  -5.69413  31.13128  1.000 80.13529  ?  411 LYS   L O   1 
ATOM   17845 C CB  . LYS   L  2 8   ? 51.52063  -5.08470  32.58511  1.000 63.11867  ?  411 LYS   L CB  1 
ATOM   17846 N N   . ASP   L  2 9   ? 49.23486  -7.23414  32.66235  1.000 70.68637  ?  412 ASP   L N   1 
ATOM   17847 C CA  . ASP   L  2 9   ? 48.46129  -8.33280  32.08844  1.000 122.11484 ?  412 ASP   L CA  1 
ATOM   17848 C C   . ASP   L  2 9   ? 46.95120  -8.12969  32.17198  1.000 77.43171  ?  412 ASP   L C   1 
ATOM   17849 O O   . ASP   L  2 9   ? 46.19216  -8.97865  31.68509  1.000 108.00890 ?  412 ASP   L O   1 
ATOM   17850 C CB  . ASP   L  2 9   ? 48.84207  -9.63747  32.78604  1.000 95.67037  ?  412 ASP   L CB  1 
ATOM   17851 C CG  . ASP   L  2 9   ? 50.22044  -10.12435 32.38521  1.000 105.10365 ?  412 ASP   L CG  1 
ATOM   17852 O OD1 . ASP   L  2 9   ? 50.80145  -9.56081  31.42482  1.000 107.69336 ?  412 ASP   L OD1 1 
ATOM   17853 O OD2 . ASP   L  2 9   ? 50.72135  -11.06974 33.02715  1.000 130.35470 -1 412 ASP   L OD2 1 
ATOM   17854 N N   . CYS   L  2 10  ? 46.49178  -7.06214  32.80166  1.000 102.69022 ?  413 CYS   L N   1 
ATOM   17855 C CA  . CYS   L  2 10  ? 45.06936  -6.78966  32.86497  1.000 79.61291  ?  413 CYS   L CA  1 
ATOM   17856 C C   . CYS   L  2 10  ? 44.65303  -6.12156  31.56063  1.000 90.16077  ?  413 CYS   L C   1 
ATOM   17857 O O   . CYS   L  2 10  ? 45.22583  -5.09524  31.16511  1.000 88.16483  ?  413 CYS   L O   1 
ATOM   17858 C CB  . CYS   L  2 10  ? 44.75723  -5.92070  34.08112  1.000 71.10035  ?  413 CYS   L CB  1 
ATOM   17859 S SG  . CYS   L  2 10  ? 43.12225  -5.15364  34.10253  1.000 82.97628  ?  413 CYS   L SG  1 
ATOM   17860 N N   . ARG   L  2 11  ? 43.67372  -6.72373  30.88511  1.000 82.41511  ?  414 ARG   L N   1 
ATOM   17861 C CA  . ARG   L  2 11  ? 43.16939  -6.25296  29.60254  1.000 104.78035 ?  414 ARG   L CA  1 
ATOM   17862 C C   . ARG   L  2 11  ? 42.25335  -5.01362  29.73244  1.000 116.11040 ?  414 ARG   L C   1 
ATOM   17863 O O   . ARG   L  2 11  ? 41.69870  -4.54869  28.72968  1.000 88.65443  ?  414 ARG   L O   1 
ATOM   17864 C CB  . ARG   L  2 11  ? 42.45102  -7.41240  28.89611  1.000 76.43052  ?  414 ARG   L CB  1 
ATOM   17865 N N   . ALA   L  2 12  ? 42.09433  -4.45376  30.93131  1.000 93.27886  ?  415 ALA   L N   1 
ATOM   17866 C CA  . ALA   L  2 12  ? 41.31905  -3.23470  31.11709  1.000 82.17919  ?  415 ALA   L CA  1 
ATOM   17867 C C   . ALA   L  2 12  ? 42.21613  -2.01689  30.95675  1.000 76.05800  ?  415 ALA   L C   1 
ATOM   17868 O O   . ALA   L  2 12  ? 43.40475  -2.05026  31.30249  1.000 103.70816 ?  415 ALA   L O   1 
ATOM   17869 C CB  . ALA   L  2 12  ? 40.65679  -3.21000  32.49422  1.000 61.85753  ?  415 ALA   L CB  1 
ATOM   17870 N N   . GLU   L  2 13  ? 41.63595  -0.93800  30.44175  1.000 53.18462  ?  416 GLU   L N   1 
ATOM   17871 C CA  . GLU   L  2 13  ? 42.37754  0.27389   30.12605  1.000 66.86806  ?  416 GLU   L CA  1 
ATOM   17872 C C   . GLU   L  2 13  ? 41.66761  1.46717   30.75612  1.000 69.16814  ?  416 GLU   L C   1 
ATOM   17873 O O   . GLU   L  2 13  ? 40.45291  1.63470   30.59861  1.000 74.33619  ?  416 GLU   L O   1 
ATOM   17874 C CB  . GLU   L  2 13  ? 42.53144  0.46017   28.60476  1.000 56.14644  ?  416 GLU   L CB  1 
ATOM   17875 N N   . ILE   L  2 14  ? 42.43175  2.27722   31.49050  1.000 66.35759  ?  417 ILE   L N   1 
ATOM   17876 C CA  . ILE   L  2 14  ? 41.89736  3.49105   32.08488  1.000 74.08344  ?  417 ILE   L CA  1 
ATOM   17877 C C   . ILE   L  2 14  ? 41.26278  4.36802   31.00644  1.000 64.22530  ?  417 ILE   L C   1 
ATOM   17878 O O   . ILE   L  2 14  ? 41.79180  4.53131   29.90313  1.000 72.56383  ?  417 ILE   L O   1 
ATOM   17879 C CB  . ILE   L  2 14  ? 43.01829  4.22644   32.84337  1.000 54.44582  ?  417 ILE   L CB  1 
ATOM   17880 C CG1 . ILE   L  2 14  ? 43.55375  3.34487   33.97124  1.000 57.81648  ?  417 ILE   L CG1 1 
ATOM   17881 C CG2 . ILE   L  2 14  ? 42.53712  5.58776   33.38489  1.000 61.46291  ?  417 ILE   L CG2 1 
ATOM   17882 C CD1 . ILE   L  2 14  ? 44.74832  3.94745   34.70319  1.000 67.88320  ?  417 ILE   L CD1 1 
ATOM   17883 N N   . VAL   L  2 15  ? 40.11037  4.93383   31.33553  1.000 73.64235  ?  418 VAL   L N   1 
ATOM   17884 C CA  . VAL   L  2 15  ? 39.38480  5.77659   30.40145  1.000 55.34196  ?  418 VAL   L CA  1 
ATOM   17885 C C   . VAL   L  2 15  ? 40.14138  7.08482   30.20272  1.000 59.13713  ?  418 VAL   L C   1 
ATOM   17886 O O   . VAL   L  2 15  ? 40.44344  7.79555   31.17202  1.000 79.24073  ?  418 VAL   L O   1 
ATOM   17887 C CB  . VAL   L  2 15  ? 37.95603  5.99662   30.92293  1.000 78.70567  ?  418 VAL   L CB  1 
ATOM   17888 C CG1 . VAL   L  2 15  ? 37.20655  7.04112   30.09805  1.000 47.01850  ?  418 VAL   L CG1 1 
ATOM   17889 C CG2 . VAL   L  2 15  ? 37.21768  4.65298   30.95973  1.000 45.28667  ?  418 VAL   L CG2 1 
ATOM   17890 N N   . GLU   L  2 16  ? 40.41549  7.42424   28.93145  1.000 66.24010  ?  419 GLU   L N   1 
ATOM   17891 C CA  . GLU   L  2 16  ? 41.39584  8.46425   28.60617  1.000 55.71135  ?  419 GLU   L CA  1 
ATOM   17892 C C   . GLU   L  2 16  ? 41.04748  9.82210   29.20236  1.000 66.15228  ?  419 GLU   L C   1 
ATOM   17893 O O   . GLU   L  2 16  ? 41.96414  10.58572  29.52923  1.000 66.27215  ?  419 GLU   L O   1 
ATOM   17894 C CB  . GLU   L  2 16  ? 41.57578  8.61945   27.08501  1.000 56.40434  ?  419 GLU   L CB  1 
ATOM   17895 C CG  . GLU   L  2 16  ? 41.80302  7.27461   26.35127  1.000 161.04329 ?  419 GLU   L CG  1 
ATOM   17896 C CD  . GLU   L  2 16  ? 43.26721  6.80255   26.28871  1.000 174.09552 ?  419 GLU   L CD  1 
ATOM   17897 O OE1 . GLU   L  2 16  ? 44.18456  7.51541   26.77189  1.000 170.89142 ?  419 GLU   L OE1 1 
ATOM   17898 O OE2 . GLU   L  2 16  ? 43.50089  5.70498   25.73134  1.000 184.98691 ?  419 GLU   L OE2 1 
ATOM   17899 N N   . LYS   L  2 17  ? 39.75681  10.16490  29.34324  1.000 61.84853  ?  420 LYS   L N   1 
ATOM   17900 C CA  . LYS   L  2 17  ? 39.46476  11.52361  29.81106  1.000 64.10512  ?  420 LYS   L CA  1 
ATOM   17901 C C   . LYS   L  2 17  ? 40.01675  11.77250  31.20936  1.000 70.62391  ?  420 LYS   L C   1 
ATOM   17902 O O   . LYS   L  2 17  ? 40.26222  12.92994  31.57976  1.000 69.02492  ?  420 LYS   L O   1 
ATOM   17903 C CB  . LYS   L  2 17  ? 37.95321  11.84454  29.77203  1.000 46.57898  ?  420 LYS   L CB  1 
ATOM   17904 C CG  . LYS   L  2 17  ? 37.00337  11.10680  30.75521  1.000 51.57910  ?  420 LYS   L CG  1 
ATOM   17905 C CD  . LYS   L  2 17  ? 35.91886  12.09576  31.23381  1.000 72.71574  ?  420 LYS   L CD  1 
ATOM   17906 C CE  . LYS   L  2 17  ? 34.61488  11.43494  31.66725  1.000 82.51203  ?  420 LYS   L CE  1 
ATOM   17907 N NZ  . LYS   L  2 17  ? 34.05506  10.61428  30.56216  1.000 105.40712 ?  420 LYS   L NZ  1 
ATOM   17908 N N   . PHE   L  2 18  ? 40.24037  10.70992  31.98729  1.000 71.30905  ?  421 PHE   L N   1 
ATOM   17909 C CA  . PHE   L  2 18  ? 40.75653  10.86279  33.33959  1.000 94.98695  ?  421 PHE   L CA  1 
ATOM   17910 C C   . PHE   L  2 18  ? 42.26529  11.04910  33.38798  1.000 82.19429  ?  421 PHE   L C   1 
ATOM   17911 O O   . PHE   L  2 18  ? 42.79636  11.36712  34.45527  1.000 76.90797  ?  421 PHE   L O   1 
ATOM   17912 C CB  . PHE   L  2 18  ? 40.34190  9.66757   34.18333  1.000 60.13509  ?  421 PHE   L CB  1 
ATOM   17913 C CG  . PHE   L  2 18  ? 38.86099  9.51133   34.27279  1.000 71.36514  ?  421 PHE   L CG  1 
ATOM   17914 C CD1 . PHE   L  2 18  ? 38.07871  10.55349  34.76921  1.000 70.80444  ?  421 PHE   L CD1 1 
ATOM   17915 C CD2 . PHE   L  2 18  ? 38.23395  8.35174   33.83468  1.000 88.19047  ?  421 PHE   L CD2 1 
ATOM   17916 C CE1 . PHE   L  2 18  ? 36.70659  10.43143  34.84185  1.000 63.11901  ?  421 PHE   L CE1 1 
ATOM   17917 C CE2 . PHE   L  2 18  ? 36.85292  8.22169   33.90250  1.000 78.57622  ?  421 PHE   L CE2 1 
ATOM   17918 C CZ  . PHE   L  2 18  ? 36.09105  9.26404   34.40101  1.000 84.24814  ?  421 PHE   L CZ  1 
ATOM   17919 N N   . THR   L  2 19  ? 42.97399  10.90170  32.26872  1.000 62.21279  ?  422 THR   L N   1 
ATOM   17920 C CA  . THR   L  2 19  ? 44.37745  11.28467  32.30345  1.000 52.43464  ?  422 THR   L CA  1 
ATOM   17921 C C   . THR   L  2 19  ? 44.57062  12.80010  32.34354  1.000 60.48239  ?  422 THR   L C   1 
ATOM   17922 O O   . THR   L  2 19  ? 45.70192  13.24845  32.56125  1.000 58.61781  ?  422 THR   L O   1 
ATOM   17923 C CB  . THR   L  2 19  ? 45.11891  10.69461  31.10580  1.000 64.05924  ?  422 THR   L CB  1 
ATOM   17924 O OG1 . THR   L  2 19  ? 44.77644  11.42634  29.93090  1.000 60.26283  ?  422 THR   L OG1 1 
ATOM   17925 C CG2 . THR   L  2 19  ? 44.73490  9.23805   30.89621  1.000 65.98066  ?  422 THR   L CG2 1 
ATOM   17926 N N   . GLU   L  2 20  ? 43.50540  13.60160  32.15846  1.000 68.71428  ?  423 GLU   L N   1 
ATOM   17927 C CA  . GLU   L  2 20  ? 43.62158  15.05009  32.32428  1.000 67.00424  ?  423 GLU   L CA  1 
ATOM   17928 C C   . GLU   L  2 20  ? 43.32907  15.41480  33.77664  1.000 57.45391  ?  423 GLU   L C   1 
ATOM   17929 O O   . GLU   L  2 20  ? 42.20016  15.20003  34.24909  1.000 73.22654  ?  423 GLU   L O   1 
ATOM   17930 C CB  . GLU   L  2 20  ? 42.68127  15.80441  31.38629  1.000 53.27834  ?  423 GLU   L CB  1 
ATOM   17931 N N   . PRO   L  2 21  ? 44.30932  15.91236  34.51938  1.000 58.55119  ?  424 PRO   L N   1 
ATOM   17932 C CA  . PRO   L  2 21  ? 44.05444  16.33906  35.89957  1.000 71.99119  ?  424 PRO   L CA  1 
ATOM   17933 C C   . PRO   L  2 21  ? 42.88354  17.30524  35.95450  1.000 57.60577  ?  424 PRO   L C   1 
ATOM   17934 O O   . PRO   L  2 21  ? 42.67919  18.10944  35.04516  1.000 66.30327  ?  424 PRO   L O   1 
ATOM   17935 C CB  . PRO   L  2 21  ? 45.36009  17.03336  36.30590  1.000 40.49732  ?  424 PRO   L CB  1 
ATOM   17936 C CG  . PRO   L  2 21  ? 46.40341  16.43474  35.42071  1.000 55.61596  ?  424 PRO   L CG  1 
ATOM   17937 C CD  . PRO   L  2 21  ? 45.71978  16.02839  34.12937  1.000 54.30693  ?  424 PRO   L CD  1 
ATOM   17938 N N   . GLY   L  2 22  ? 42.11056  17.21730  37.03731  1.000 63.47913  ?  425 GLY   L N   1 
ATOM   17939 C CA  . GLY   L  2 22  ? 40.98848  18.09964  37.25976  1.000 46.15627  ?  425 GLY   L CA  1 
ATOM   17940 C C   . GLY   L  2 22  ? 39.65390  17.58677  36.74968  1.000 54.79592  ?  425 GLY   L C   1 
ATOM   17941 O O   . GLY   L  2 22  ? 38.61886  18.16389  37.09406  1.000 60.67438  ?  425 GLY   L O   1 
ATOM   17942 N N   . THR   L  2 23  ? 39.64327  16.52550  35.94667  1.000 61.81339  ?  426 THR   L N   1 
ATOM   17943 C CA  . THR   L  2 23  ? 38.39279  15.96201  35.45048  1.000 59.48247  ?  426 THR   L CA  1 
ATOM   17944 C C   . THR   L  2 23  ? 37.53787  15.41546  36.59703  1.000 59.45562  ?  426 THR   L C   1 
ATOM   17945 O O   . THR   L  2 23  ? 38.03693  14.75733  37.51306  1.000 88.72633  ?  426 THR   L O   1 
ATOM   17946 C CB  . THR   L  2 23  ? 38.70208  14.85343  34.43518  1.000 68.15435  ?  426 THR   L CB  1 
ATOM   17947 O OG1 . THR   L  2 23  ? 39.46019  15.39290  33.34280  1.000 76.45332  ?  426 THR   L OG1 1 
ATOM   17948 C CG2 . THR   L  2 23  ? 37.42958  14.18570  33.91136  1.000 58.59390  ?  426 THR   L CG2 1 
ATOM   17949 N N   . VAL   L  2 24  ? 36.23579  15.68364  36.53641  1.000 82.49791  ?  427 VAL   L N   1 
ATOM   17950 C CA  . VAL   L  2 24  ? 35.32844  15.22490  37.57899  1.000 63.66235  ?  427 VAL   L CA  1 
ATOM   17951 C C   . VAL   L  2 24  ? 35.15398  13.71260  37.49389  1.000 58.11781  ?  427 VAL   L C   1 
ATOM   17952 O O   . VAL   L  2 24  ? 34.90157  13.15254  36.41679  1.000 82.97241  ?  427 VAL   L O   1 
ATOM   17953 C CB  . VAL   L  2 24  ? 33.98632  15.96226  37.46784  1.000 56.53063  ?  427 VAL   L CB  1 
ATOM   17954 C CG1 . VAL   L  2 24  ? 32.91970  15.27102  38.29469  1.000 49.27005  ?  427 VAL   L CG1 1 
ATOM   17955 C CG2 . VAL   L  2 24  ? 34.16773  17.38943  37.93186  1.000 56.47711  ?  427 VAL   L CG2 1 
ATOM   17956 N N   . ILE   L  2 25  ? 35.29143  13.04444  38.63773  1.000 89.26220  ?  428 ILE   L N   1 
ATOM   17957 C CA  . ILE   L  2 25  ? 35.11249  11.59843  38.75837  1.000 58.15890  ?  428 ILE   L CA  1 
ATOM   17958 C C   . ILE   L  2 25  ? 33.86342  11.37607  39.60679  1.000 79.57090  ?  428 ILE   L C   1 
ATOM   17959 O O   . ILE   L  2 25  ? 33.87673  11.57436  40.82950  1.000 70.87140  ?  428 ILE   L O   1 
ATOM   17960 C CB  . ILE   L  2 25  ? 36.33808  10.90137  39.37581  1.000 76.56528  ?  428 ILE   L CB  1 
ATOM   17961 C CG1 . ILE   L  2 25  ? 37.58940  11.06149  38.49800  1.000 67.43393  ?  428 ILE   L CG1 1 
ATOM   17962 C CG2 . ILE   L  2 25  ? 36.03595  9.43590   39.59684  1.000 55.39779  ?  428 ILE   L CG2 1 
ATOM   17963 C CD1 . ILE   L  2 25  ? 38.79926  10.24287  38.96581  1.000 62.06278  ?  428 ILE   L CD1 1 
ATOM   17964 N N   . ARG   L  2 26  ? 32.77152  10.98088  38.96215  1.000 69.48242  ?  429 ARG   L N   1 
ATOM   17965 C CA  . ARG   L  2 26  ? 31.54554  10.65723  39.67804  1.000 68.29479  ?  429 ARG   L CA  1 
ATOM   17966 C C   . ARG   L  2 26  ? 31.66567  9.24021   40.20403  1.000 68.82498  ?  429 ARG   L C   1 
ATOM   17967 O O   . ARG   L  2 26  ? 31.90262  8.30811   39.42675  1.000 67.86462  ?  429 ARG   L O   1 
ATOM   17968 C CB  . ARG   L  2 26  ? 30.32760  10.79904  38.76671  1.000 76.30964  ?  429 ARG   L CB  1 
ATOM   17969 C CG  . ARG   L  2 26  ? 30.10983  12.21638  38.31516  1.000 70.08770  ?  429 ARG   L CG  1 
ATOM   17970 C CD  . ARG   L  2 26  ? 29.02110  12.33141  37.27965  1.000 83.71019  ?  429 ARG   L CD  1 
ATOM   17971 N NE  . ARG   L  2 26  ? 28.30858  13.59122  37.45704  1.000 69.49277  ?  429 ARG   L NE  1 
ATOM   17972 C CZ  . ARG   L  2 26  ? 28.76722  14.76859  37.04896  1.000 201.99659 ?  429 ARG   L CZ  1 
ATOM   17973 N NH1 . ARG   L  2 26  ? 29.90060  14.87627  36.36283  1.000 65.13046  ?  429 ARG   L NH1 1 
ATOM   17974 N NH2 . ARG   L  2 26  ? 28.07784  15.86790  37.34103  1.000 71.95707  ?  429 ARG   L NH2 1 
ATOM   17975 N N   . ILE   L  2 27  ? 31.50873  9.07544   41.51922  1.000 60.81827  ?  430 ILE   L N   1 
ATOM   17976 C CA  . ILE   L  2 27  ? 31.64115  7.74846   42.10087  1.000 78.21176  ?  430 ILE   L CA  1 
ATOM   17977 C C   . ILE   L  2 27  ? 30.69443  6.77961   41.38524  1.000 65.84315  ?  430 ILE   L C   1 
ATOM   17978 O O   . ILE   L  2 27  ? 29.60828  7.15769   40.93094  1.000 92.64513  ?  430 ILE   L O   1 
ATOM   17979 C CB  . ILE   L  2 27  ? 31.39687  7.81103   43.62089  1.000 71.71580  ?  430 ILE   L CB  1 
ATOM   17980 C CG1 . ILE   L  2 27  ? 31.92853  6.53546   44.30262  1.000 66.20017  ?  430 ILE   L CG1 1 
ATOM   17981 C CG2 . ILE   L  2 27  ? 29.91018  8.11357   43.92839  1.000 69.83036  ?  430 ILE   L CG2 1 
ATOM   17982 C CD1 . ILE   L  2 27  ? 31.90319  6.61901   45.82693  1.000 63.38365  ?  430 ILE   L CD1 1 
ATOM   17983 N N   . ASN   L  2 28  ? 31.14583  5.52993   41.25095  1.000 103.46788 ?  431 ASN   L N   1 
ATOM   17984 C CA  . ASN   L  2 28  ? 30.47542  4.44671   40.53325  1.000 82.91995  ?  431 ASN   L CA  1 
ATOM   17985 C C   . ASN   L  2 28  ? 30.52928  4.60709   39.01749  1.000 94.48801  ?  431 ASN   L C   1 
ATOM   17986 O O   . ASN   L  2 28  ? 30.11710  3.68514   38.30843  1.000 85.03298  ?  431 ASN   L O   1 
ATOM   17987 C CB  . ASN   L  2 28  ? 29.00110  4.29217   40.94652  1.000 78.58970  ?  431 ASN   L CB  1 
ATOM   17988 C CG  . ASN   L  2 28  ? 28.83073  3.94756   42.41327  1.000 90.49881  ?  431 ASN   L CG  1 
ATOM   17989 O OD1 . ASN   L  2 28  ? 29.73416  3.41078   43.05566  1.000 95.44947  ?  431 ASN   L OD1 1 
ATOM   17990 N ND2 . ASN   L  2 28  ? 27.66088  4.26556   42.95453  1.000 82.64667  ?  431 ASN   L ND2 1 
ATOM   17991 N N   . GLU   L  2 29  ? 30.99360  5.74167   38.48844  1.000 68.47285  ?  432 GLU   L N   1 
ATOM   17992 C CA  . GLU   L  2 29  ? 31.07802  5.82265   37.03359  1.000 77.11841  ?  432 GLU   L CA  1 
ATOM   17993 C C   . GLU   L  2 29  ? 32.29793  5.02691   36.53623  1.000 72.89574  ?  432 GLU   L C   1 
ATOM   17994 O O   . GLU   L  2 29  ? 33.16233  4.61119   37.31552  1.000 88.35831  ?  432 GLU   L O   1 
ATOM   17995 C CB  . GLU   L  2 29  ? 31.09820  7.28935   36.57857  1.000 61.29486  ?  432 GLU   L CB  1 
ATOM   17996 C CG  . GLU   L  2 29  ? 32.46081  7.90163   36.30600  1.000 74.57620  ?  432 GLU   L CG  1 
ATOM   17997 C CD  . GLU   L  2 29  ? 32.38092  9.27750   35.62670  1.000 98.95493  ?  432 GLU   L CD  1 
ATOM   17998 O OE1 . GLU   L  2 29  ? 32.31250  10.30322  36.34102  1.000 83.96905  ?  432 GLU   L OE1 1 
ATOM   17999 O OE2 . GLU   L  2 29  ? 32.40639  9.33695   34.37123  1.000 90.22183  -1 432 GLU   L OE2 1 
ATOM   18000 N N   . VAL   L  2 30  ? 32.33504  4.75947   35.23334  1.000 91.08763  ?  433 VAL   L N   1 
ATOM   18001 C CA  . VAL   L  2 30  ? 33.35477  3.87657   34.66128  1.000 66.40460  ?  433 VAL   L CA  1 
ATOM   18002 C C   . VAL   L  2 30  ? 34.67575  4.63017   34.54233  1.000 86.50680  ?  433 VAL   L C   1 
ATOM   18003 O O   . VAL   L  2 30  ? 34.75090  5.65276   33.84998  1.000 77.34330  ?  433 VAL   L O   1 
ATOM   18004 C CB  . VAL   L  2 30  ? 32.90949  3.34385   33.28839  1.000 87.35647  ?  433 VAL   L CB  1 
ATOM   18005 C CG1 . VAL   L  2 30  ? 33.97679  2.43214   32.67000  1.000 77.18406  ?  433 VAL   L CG1 1 
ATOM   18006 C CG2 . VAL   L  2 30  ? 31.55717  2.62455   33.38282  1.000 71.95970  ?  433 VAL   L CG2 1 
ATOM   18007 N N   . VAL   L  2 31  ? 35.72658  4.11906   35.19796  1.000 68.20824  ?  434 VAL   L N   1 
ATOM   18008 C CA  . VAL   L  2 31  ? 37.06533  4.68686   35.04474  1.000 79.28972  ?  434 VAL   L CA  1 
ATOM   18009 C C   . VAL   L  2 31  ? 38.01229  3.76661   34.27700  1.000 66.88649  ?  434 VAL   L C   1 
ATOM   18010 O O   . VAL   L  2 31  ? 39.04893  4.24328   33.78433  1.000 66.06816  ?  434 VAL   L O   1 
ATOM   18011 C CB  . VAL   L  2 31  ? 37.69646  5.09521   36.39923  1.000 69.60982  ?  434 VAL   L CB  1 
ATOM   18012 C CG1 . VAL   L  2 31  ? 36.92933  6.24655   37.03585  1.000 53.37420  ?  434 VAL   L CG1 1 
ATOM   18013 C CG2 . VAL   L  2 31  ? 37.78960  3.89795   37.37769  1.000 55.95314  ?  434 VAL   L CG2 1 
ATOM   18014 N N   . ALA   L  2 32  ? 37.69575  2.48316   34.14386  1.000 76.17936  ?  435 ALA   L N   1 
ATOM   18015 C CA  . ALA   L  2 32  ? 38.47295  1.59558   33.28861  1.000 79.45699  ?  435 ALA   L CA  1 
ATOM   18016 C C   . ALA   L  2 32  ? 37.54500  0.51194   32.75656  1.000 89.39938  ?  435 ALA   L C   1 
ATOM   18017 O O   . ALA   L  2 32  ? 36.57515  0.12403   33.42180  1.000 81.46925  ?  435 ALA   L O   1 
ATOM   18018 C CB  . ALA   L  2 32  ? 39.66107  0.96384   34.02792  1.000 73.15462  ?  435 ALA   L CB  1 
ATOM   18019 N N   . ALA   L  2 33  ? 37.85708  0.02120   31.55562  1.000 85.56566  ?  436 ALA   L N   1 
ATOM   18020 C CA  . ALA   L  2 33  ? 37.02279  -0.96002  30.87312  1.000 94.56406  ?  436 ALA   L CA  1 
ATOM   18021 C C   . ALA   L  2 33  ? 37.89015  -1.85306  30.00021  1.000 114.18625 ?  436 ALA   L C   1 
ATOM   18022 O O   . ALA   L  2 33  ? 38.94864  -1.43530  29.52006  1.000 91.58249  ?  436 ALA   L O   1 
ATOM   18023 C CB  . ALA   L  2 33  ? 35.95816  -0.29322  30.00434  1.000 78.66679  ?  436 ALA   L CB  1 
ATOM   18024 N N   . LEU   L  2 34  ? 37.41582  -3.07890  29.78413  1.000 75.65303  ?  437 LEU   L N   1 
ATOM   18025 C CA  . LEU   L  2 34  ? 38.09943  -4.06009  28.94054  1.000 105.37747 ?  437 LEU   L CA  1 
ATOM   18026 C C   . LEU   L  2 34  ? 38.16467  -3.65298  27.46439  1.000 73.24765  ?  437 LEU   L C   1 
ATOM   18027 O O   . LEU   L  2 34  ? 37.15499  -3.31071  26.85758  1.000 79.98540  ?  437 LEU   L O   1 
ATOM   18028 C CB  . LEU   L  2 34  ? 37.41010  -5.42439  29.06699  1.000 72.06921  ?  437 LEU   L CB  1 
ATOM   18029 C CG  . LEU   L  2 34  ? 37.66446  -6.21717  30.35826  1.000 97.19220  ?  437 LEU   L CG  1 
ATOM   18030 C CD1 . LEU   L  2 34  ? 36.83658  -7.52844  30.42165  1.000 78.34693  ?  437 LEU   L CD1 1 
ATOM   18031 C CD2 . LEU   L  2 34  ? 39.16939  -6.47403  30.55637  1.000 99.94648  ?  437 LEU   L CD2 1 
HETATM 18032 C C   . A1LWG M  3 .   ? 18.14299  14.68587  -30.63807 1.000 17.17884  ?  501 A1LWG J C   1 
HETATM 18033 C CA  . A1LWG M  3 .   ? 18.25736  16.17645  -30.26381 1.000 22.81116  ?  501 A1LWG J CA  1 
HETATM 18034 C CB  . A1LWG M  3 .   ? 19.66547  16.36576  -29.62659 1.000 17.52725  ?  501 A1LWG J CB  1 
HETATM 18035 C C06 . A1LWG M  3 .   ? 17.18131  18.26302  -31.40474 1.000 25.68580  ?  501 A1LWG J C06 1 
HETATM 18036 C C07 . A1LWG M  3 .   ? 17.06642  19.14536  -32.68068 1.000 56.04771  ?  501 A1LWG J C07 1 
HETATM 18037 C C08 . A1LWG M  3 .   ? 18.35415  19.80384  -33.30590 1.000 84.69303  ?  501 A1LWG J C08 1 
HETATM 18038 C C09 . A1LWG M  3 .   ? 19.51309  20.17561  -32.61359 1.000 92.29074  ?  501 A1LWG J C09 1 
HETATM 18039 C C11 . A1LWG M  3 .   ? 19.88943  20.70665  -34.76216 1.000 81.41205  ?  501 A1LWG J C11 1 
HETATM 18040 C C12 . A1LWG M  3 .   ? 18.59081  20.15590  -34.67484 1.000 89.01114  ?  501 A1LWG J C12 1 
HETATM 18041 C C13 . A1LWG M  3 .   ? 17.84174  20.05324  -35.86191 1.000 96.98128  ?  501 A1LWG J C13 1 
HETATM 18042 C C14 . A1LWG M  3 .   ? 18.35681  20.48716  -37.10679 1.000 45.24655  ?  501 A1LWG J C14 1 
HETATM 18043 C C15 . A1LWG M  3 .   ? 19.64737  21.03528  -37.17659 1.000 35.78583  ?  501 A1LWG J C15 1 
HETATM 18044 C C16 . A1LWG M  3 .   ? 20.41789  21.13858  -36.00033 1.000 54.31128  ?  501 A1LWG J C16 1 
HETATM 18045 N N   . A1LWG M  3 .   ? 18.14282  17.07176  -31.50881 1.000 70.37550  ?  501 A1LWG J N   1 
HETATM 18046 N N10 . A1LWG M  3 .   ? 20.41258  20.70561  -33.50790 1.000 91.30877  ?  501 A1LWG J N10 1 
HETATM 18047 O O   . A1LWG M  3 .   ? 17.56602  14.34105  -31.70103 1.000 28.50110  ?  501 A1LWG J O   1 
HETATM 18048 C C   . A1LWG N  3 .   ? 7.08482   25.37511  6.86397   1.000 55.36216  ?  501 A1LWG H C   1 
HETATM 18049 C CA  . A1LWG N  3 .   ? 7.03915   24.03832  7.59059   1.000 29.72608  ?  501 A1LWG H CA  1 
HETATM 18050 C CB  . A1LWG N  3 .   ? 5.59402   24.07586  8.18959   1.000 16.94035  ?  501 A1LWG H CB  1 
HETATM 18051 C C06 . A1LWG N  3 .   ? 7.85895   21.58267  7.02901   1.000 89.52644  ?  501 A1LWG H C06 1 
HETATM 18052 C C07 . A1LWG N  3 .   ? 8.14883   20.52190  5.91288   1.000 17.46691  ?  501 A1LWG H C07 1 
HETATM 18053 C C08 . A1LWG N  3 .   ? 6.87134   19.75453  5.36472   1.000 58.75272  ?  501 A1LWG H C08 1 
HETATM 18054 C C09 . A1LWG N  3 .   ? 5.67191   19.57061  6.07007   1.000 65.24620  ?  501 A1LWG H C09 1 
HETATM 18055 C C11 . A1LWG N  3 .   ? 5.34236   18.58187  4.08102   1.000 88.43126  ?  501 A1LWG H C11 1 
HETATM 18056 C C12 . A1LWG N  3 .   ? 6.66329   19.10950  4.09317   1.000 90.74434  ?  501 A1LWG H C12 1 
HETATM 18057 C C13 . A1LWG N  3 .   ? 7.45656   18.90717  2.94205   1.000 39.11667  ?  501 A1LWG H C13 1 
HETATM 18058 C C14 . A1LWG N  3 .   ? 6.95011   18.22377  1.80908   1.000 50.66977  ?  501 A1LWG H C14 1 
HETATM 18059 C C15 . A1LWG N  3 .   ? 5.62774   17.69737  1.79304   1.000 25.98295  ?  501 A1LWG H C15 1 
HETATM 18060 C C16 . A1LWG N  3 .   ? 4.82873   17.87934  2.94032   1.000 35.96600  ?  501 A1LWG H C16 1 
HETATM 18061 N N   . A1LWG N  3 .   ? 7.21847   22.90301  6.57781   1.000 89.76404  ?  501 A1LWG H N   1 
HETATM 18062 N N10 . A1LWG N  3 .   ? 4.77714   18.87853  5.29043   1.000 33.62445  ?  501 A1LWG H N10 1 
HETATM 18063 O O   . A1LWG N  3 .   ? 7.51599   25.42343  5.72156   1.000 19.70346  ?  501 A1LWG H O   1 
HETATM 18064 C C   . A1LWG O  3 .   ? 24.37259  59.78679  36.11607  1.000 23.86033  ?  501 A1LWG B C   1 
HETATM 18065 C CA  . A1LWG O  3 .   ? 24.37382  58.30936  36.45920  1.000 16.21383  ?  501 A1LWG B CA  1 
HETATM 18066 C CB  . A1LWG O  3 .   ? 25.74242  57.74384  35.99335  1.000 17.87334  ?  501 A1LWG B CB  1 
HETATM 18067 C C06 . A1LWG O  3 .   ? 23.82396  56.95525  38.59477  1.000 122.49141 ?  501 A1LWG B C06 1 
HETATM 18068 C C07 . A1LWG O  3 .   ? 23.63331  57.00964  40.11963  1.000 98.74895  ?  501 A1LWG B C07 1 
HETATM 18069 C C08 . A1LWG O  3 .   ? 24.90296  56.89528  41.01001  1.000 94.48751  ?  501 A1LWG B C08 1 
HETATM 18070 C C09 . A1LWG O  3 .   ? 26.09330  56.26531  40.63701  1.000 124.21485 ?  501 A1LWG B C09 1 
HETATM 18071 C C11 . A1LWG O  3 .   ? 26.42450  57.03524  42.71079  1.000 110.14728 ?  501 A1LWG B C11 1 
HETATM 18072 C C12 . A1LWG O  3 .   ? 25.10105  57.38245  42.33347  1.000 81.64504  ?  501 A1LWG B C12 1 
HETATM 18073 C C13 . A1LWG O  3 .   ? 24.31149  58.08983  43.26733  1.000 48.72013  ?  501 A1LWG B C13 1 
HETATM 18074 C C14 . A1LWG O  3 .   ? 24.78724  58.45074  44.55786  1.000 21.47710  ?  501 A1LWG B C14 1 
HETATM 18075 C C15 . A1LWG O  3 .   ? 26.11741  58.10069  44.91078  1.000 60.50701  ?  501 A1LWG B C15 1 
HETATM 18076 C C16 . A1LWG O  3 .   ? 26.94283  57.41188  43.98775  1.000 19.72591  ?  501 A1LWG B C16 1 
HETATM 18077 N N   . A1LWG O  3 .   ? 24.08218  58.30671  37.96131  1.000 107.19285 ?  501 A1LWG B N   1 
HETATM 18078 N N10 . A1LWG O  3 .   ? 26.99065  56.36388  41.66595  1.000 85.98356  ?  501 A1LWG B N10 1 
HETATM 18079 O O   . A1LWG O  3 .   ? 23.74371  60.60384  36.82434  1.000 17.09846  ?  501 A1LWG B O   1 
HETATM 18080 C C   . A1LWG P  3 .   ? 49.32621  39.34554  -1.95863  1.000 68.66281  ?  501 A1LWG D C   1 
HETATM 18081 C CA  . A1LWG P  3 .   ? 49.33094  40.62320  -2.80694  1.000 41.36380  ?  501 A1LWG D CA  1 
HETATM 18082 C CB  . A1LWG P  3 .   ? 50.77213  41.23823  -2.75527  1.000 18.88106  ?  501 A1LWG D CB  1 
HETATM 18083 C C06 . A1LWG P  3 .   ? 48.38982  41.20968  -5.18417  1.000 30.98038  ?  501 A1LWG D C06 1 
HETATM 18084 C C07 . A1LWG P  3 .   ? 48.33223  40.74774  -6.65722  1.000 97.11491  ?  501 A1LWG D C07 1 
HETATM 18085 C C08 . A1LWG P  3 .   ? 49.63182  40.65084  -7.52033  1.000 88.27915  ?  501 A1LWG D C08 1 
HETATM 18086 C C09 . A1LWG P  3 .   ? 50.83280  41.36533  -7.34892  1.000 102.61785 ?  501 A1LWG D C09 1 
HETATM 18087 C C11 . A1LWG P  3 .   ? 51.16221  40.04153  -9.15402  1.000 128.42974 ?  501 A1LWG D C11 1 
HETATM 18088 C C12 . A1LWG P  3 .   ? 49.83191  39.81834  -8.66510  1.000 123.94409 ?  501 A1LWG D C12 1 
HETATM 18089 C C13 . A1LWG P  3 .   ? 49.01802  38.88221  -9.33561  1.000 59.80944  ?  501 A1LWG D C13 1 
HETATM 18090 C C14 . A1LWG P  3 .   ? 49.51367  38.16534  -10.46372 1.000 33.89575  ?  501 A1LWG D C14 1 
HETATM 18091 C C15 . A1LWG P  3 .   ? 50.83291  38.38243  -10.95029 1.000 41.09598  ?  501 A1LWG D C15 1 
HETATM 18092 C C16 . A1LWG P  3 .   ? 51.65942  39.32493  -10.29994 1.000 48.74371  ?  501 A1LWG D C16 1 
HETATM 18093 N N   . A1LWG P  3 .   ? 48.97761  40.17890  -4.22434  1.000 116.74111 ?  501 A1LWG D N   1 
HETATM 18094 N N10 . A1LWG P  3 .   ? 51.73444  40.99452  -8.32965  1.000 22.53153  ?  501 A1LWG D N10 1 
HETATM 18095 O O   . A1LWG P  3 .   ? 48.80799  38.35984  -2.51052  1.000 17.09465  ?  501 A1LWG D O   1 
HETATM 18096 C C   . A1LWG Q  3 .   ? -1.22803  -4.96096  53.28111  1.000 28.88055  ?  501 A1LWG F C   1 
HETATM 18097 C CA  . A1LWG Q  3 .   ? -0.54170  -5.73527  52.11988  1.000 38.90057  ?  501 A1LWG F CA  1 
HETATM 18098 C CB  . A1LWG Q  3 .   ? -1.69040  -5.95685  51.06719  1.000 24.99091  ?  501 A1LWG F CB  1 
HETATM 18099 C C06 . A1LWG Q  3 .   ? 1.26826   -5.41888  50.26832  1.000 73.03108  ?  501 A1LWG F C06 1 
HETATM 18100 C C07 . A1LWG Q  3 .   ? 2.20790   -4.41039  49.57597  1.000 32.88332  ?  501 A1LWG F C07 1 
HETATM 18101 C C08 . A1LWG Q  3 .   ? 1.51928   -3.51928  48.50160  1.000 126.91343 ?  501 A1LWG F C08 1 
HETATM 18102 C C09 . A1LWG Q  3 .   ? 0.32327   -3.82308  47.83829  1.000 118.05057 ?  501 A1LWG F C09 1 
HETATM 18103 C C11 . A1LWG Q  3 .   ? 0.95066   -1.83898  47.03272  1.000 122.28724 ?  501 A1LWG F C11 1 
HETATM 18104 C C12 . A1LWG Q  3 .   ? 1.92906   -2.25489  47.99001  1.000 146.40709 ?  501 A1LWG F C12 1 
HETATM 18105 C C13 . A1LWG Q  3 .   ? 3.03043   -1.42935  48.24501  1.000 25.77985  ?  501 A1LWG F C13 1 
HETATM 18106 C C14 . A1LWG Q  3 .   ? 3.15939   -0.20155  47.55737  1.000 88.73670  ?  501 A1LWG F C14 1 
HETATM 18107 C C15 . A1LWG Q  3 .   ? 2.18101   0.21296   46.61613  1.000 30.95291  ?  501 A1LWG F C15 1 
HETATM 18108 C C16 . A1LWG Q  3 .   ? 1.07635   -0.59871  46.35165  1.000 41.76188  ?  501 A1LWG F C16 1 
HETATM 18109 N N   . A1LWG Q  3 .   ? 0.70025   -4.98157  51.60577  1.000 105.18450 ?  501 A1LWG F N   1 
HETATM 18110 N N10 . A1LWG Q  3 .   ? -0.01445  -2.80723  46.96313  1.000 24.73837  ?  501 A1LWG F N10 1 
HETATM 18111 O O   . A1LWG Q  3 .   ? -0.68921  -3.96232  53.75298  1.000 36.47247  ?  501 A1LWG F O   1 
HETATM 18112 C C   . A1LWG R  3 .   ? 41.35165  11.91704  49.74345  1.000 46.41424  ?  501 A1LWG L C   1 
HETATM 18113 C CA  . A1LWG R  3 .   ? 40.95583  12.59507  51.03578  1.000 23.39793  ?  501 A1LWG L CA  1 
HETATM 18114 C CB  . A1LWG R  3 .   ? 42.09740  12.27523  52.07451  1.000 45.39833  ?  501 A1LWG L CB  1 
HETATM 18115 C C06 . A1LWG R  3 .   ? 40.23351  14.94231  51.82925  1.000 127.87336 ?  501 A1LWG L C06 1 
HETATM 18116 C C07 . A1LWG R  3 .   ? 40.47156  16.45276  51.65939  1.000 59.98400  ?  501 A1LWG L C07 1 
HETATM 18117 C C08 . A1LWG R  3 .   ? 41.70762  17.01337  52.43306  1.000 95.61828  ?  501 A1LWG L C08 1 
HETATM 18118 C C09 . A1LWG R  3 .   ? 42.31345  16.44833  53.56635  1.000 72.44043  ?  501 A1LWG L C09 1 
HETATM 18119 C C11 . A1LWG R  3 .   ? 43.47276  18.29258  53.10615  1.000 70.22882  ?  501 A1LWG L C11 1 
HETATM 18120 C C12 . A1LWG R  3 .   ? 42.43457  18.19573  52.14119  1.000 118.67494 ?  501 A1LWG L C12 1 
HETATM 18121 C C13 . A1LWG R  3 .   ? 42.31128  19.18588  51.14147  1.000 87.21136  ?  501 A1LWG L C13 1 
HETATM 18122 C C14 . A1LWG R  3 .   ? 43.21786  20.27505  51.08350  1.000 60.92487  ?  501 A1LWG L C14 1 
HETATM 18123 C C15 . A1LWG R  3 .   ? 44.25431  20.37621  52.04560  1.000 59.26784  ?  501 A1LWG L C15 1 
HETATM 18124 C C16 . A1LWG R  3 .   ? 44.38538  19.37669  53.04625  1.000 38.78650  ?  501 A1LWG L C16 1 
HETATM 18125 N N   . A1LWG R  3 .   ? 40.86218  14.08952  50.74462  1.000 130.41859 ?  501 A1LWG L N   1 
HETATM 18126 N N10 . A1LWG R  3 .   ? 43.36289  17.23827  53.95942  1.000 38.46408  ?  501 A1LWG L N10 1 
HETATM 18127 O O   . A1LWG R  3 .   ? 41.74731  12.57729  48.76340  1.000 32.85201  ?  501 A1LWG L O   1 
HETATM 18128 O O   . HOH   S  4 .   ? -3.27175  18.79344  -30.87821 1.000 33.72837  ?  501 HOH   I O   1 
HETATM 18129 O O   . HOH   S  4 .   ? 34.87207  23.21931  -22.52302 1.000 31.76289  ?  502 HOH   I O   1 
HETATM 18130 O O   . HOH   S  4 .   ? 20.61265  26.47952  -48.53232 1.000 45.79296  ?  503 HOH   I O   1 
HETATM 18131 O O   . HOH   S  4 .   ? 45.60634  19.04486  -26.43131 1.000 44.03562  ?  504 HOH   I O   1 
HETATM 18132 O O   . HOH   S  4 .   ? 9.66418   -3.88760  -20.07500 1.000 36.15916  ?  505 HOH   I O   1 
HETATM 18133 O O   . HOH   S  4 .   ? 11.74062  13.11694  -25.65006 1.000 34.04589  ?  506 HOH   I O   1 
HETATM 18134 O O   . HOH   S  4 .   ? 31.60345  24.68872  -19.56185 1.000 44.19579  ?  507 HOH   I O   1 
HETATM 18135 O O   . HOH   S  4 .   ? 6.11418   19.60800  -28.66037 1.000 36.28071  ?  508 HOH   I O   1 
HETATM 18136 O O   . HOH   S  4 .   ? 43.58637  21.01593  -41.95803 1.000 27.53791  ?  509 HOH   I O   1 
HETATM 18137 O O   . HOH   S  4 .   ? 25.95661  21.51884  -43.15250 1.000 36.58995  ?  510 HOH   I O   1 
HETATM 18138 O O   . HOH   S  4 .   ? 30.65361  10.86195  -17.29424 1.000 34.03872  ?  511 HOH   I O   1 
HETATM 18139 O O   . HOH   S  4 .   ? 9.30250   -2.84978  -18.04415 1.000 43.57098  ?  512 HOH   I O   1 
HETATM 18140 O O   . HOH   S  4 .   ? 13.44702  3.30611   -26.06562 1.000 32.19143  ?  513 HOH   I O   1 
HETATM 18141 O O   . HOH   S  4 .   ? -1.18998  20.75652  -34.96556 1.000 37.13341  ?  514 HOH   I O   1 
HETATM 18142 O O   . HOH   S  4 .   ? 9.61238   40.64968  -41.93480 1.000 39.97799  ?  515 HOH   I O   1 
HETATM 18143 O O   . HOH   S  4 .   ? 36.55016  40.27404  -34.38878 1.000 65.58352  ?  516 HOH   I O   1 
HETATM 18144 O O   . HOH   S  4 .   ? 7.98792   10.45044  -16.63088 1.000 32.45781  ?  517 HOH   I O   1 
HETATM 18145 O O   . HOH   S  4 .   ? 24.97576  25.99127  -18.71442 1.000 27.29429  ?  518 HOH   I O   1 
HETATM 18146 O O   . HOH   S  4 .   ? 33.97729  -5.36850  -37.30307 1.000 23.91972  ?  519 HOH   I O   1 
HETATM 18147 O O   . HOH   S  4 .   ? 49.94883  23.66712  -35.88468 1.000 38.17143  ?  520 HOH   I O   1 
HETATM 18148 O O   . HOH   S  4 .   ? 2.54398   6.45571   -25.52656 1.000 28.71317  ?  521 HOH   I O   1 
HETATM 18149 O O   . HOH   S  4 .   ? 5.76536   15.45291  -30.77612 1.000 24.98641  ?  522 HOH   I O   1 
HETATM 18150 O O   . HOH   S  4 .   ? 24.68248  -8.55983  -28.74955 1.000 30.89269  ?  523 HOH   I O   1 
HETATM 18151 O O   . HOH   S  4 .   ? 24.92978  -10.52916 -21.79833 1.000 47.95391  ?  524 HOH   I O   1 
HETATM 18152 O O   . HOH   S  4 .   ? -3.22760  13.02152  -26.96540 1.000 35.99265  ?  525 HOH   I O   1 
HETATM 18153 O O   . HOH   S  4 .   ? 32.13245  19.91852  -33.59087 1.000 29.41624  ?  526 HOH   I O   1 
HETATM 18154 O O   . HOH   S  4 .   ? 28.65650  16.14107  -34.78714 1.000 26.53569  ?  527 HOH   I O   1 
HETATM 18155 O O   . HOH   S  4 .   ? 21.12305  -3.81596  -40.36135 1.000 36.56533  ?  528 HOH   I O   1 
HETATM 18156 O O   . HOH   S  4 .   ? 27.84418  -1.77339  -36.82579 1.000 24.77749  ?  529 HOH   I O   1 
HETATM 18157 O O   . HOH   S  4 .   ? 40.70247  -4.50665  -35.08974 1.000 21.98389  ?  530 HOH   I O   1 
HETATM 18158 O O   . HOH   S  4 .   ? 32.39124  -6.93228  -40.76966 1.000 33.87270  ?  531 HOH   I O   1 
HETATM 18159 O O   . HOH   S  4 .   ? 33.57378  11.51725  -28.67355 1.000 22.03217  ?  532 HOH   I O   1 
HETATM 18160 O O   . HOH   S  4 .   ? 5.75423   9.32880   -18.92479 1.000 23.63056  ?  533 HOH   I O   1 
HETATM 18161 O O   . HOH   S  4 .   ? 31.23919  18.64025  -40.31156 1.000 36.65448  ?  534 HOH   I O   1 
HETATM 18162 O O   . HOH   S  4 .   ? 6.31944   14.42954  -18.57340 1.000 24.28665  ?  535 HOH   I O   1 
HETATM 18163 O O   . HOH   S  4 .   ? 10.01508  18.93557  -23.16224 1.000 31.36084  ?  536 HOH   I O   1 
HETATM 18164 O O   . HOH   S  4 .   ? 12.50673  9.34431   -12.38050 1.000 46.69964  ?  537 HOH   I O   1 
HETATM 18165 O O   . HOH   S  4 .   ? 0.34046   12.23152  -36.35161 1.000 47.28195  ?  538 HOH   I O   1 
HETATM 18166 O O   . HOH   S  4 .   ? 26.71445  17.45379  -30.69660 1.000 31.04247  ?  539 HOH   I O   1 
HETATM 18167 O O   . HOH   S  4 .   ? 25.40898  0.17217   -38.40837 1.000 36.98951  ?  540 HOH   I O   1 
HETATM 18168 O O   . HOH   S  4 .   ? 7.00722   12.45253  -32.59084 1.000 26.83559  ?  541 HOH   I O   1 
HETATM 18169 O O   . HOH   S  4 .   ? 26.48245  16.20920  -33.27497 1.000 21.59284  ?  542 HOH   I O   1 
HETATM 18170 O O   . HOH   S  4 .   ? -0.29898  4.37446   -19.30493 1.000 30.48292  ?  543 HOH   I O   1 
HETATM 18171 O O   . HOH   S  4 .   ? 17.61993  -9.18724  -15.65995 1.000 46.83392  ?  544 HOH   I O   1 
HETATM 18172 O O   . HOH   S  4 .   ? 12.99765  6.16750   -8.75972  1.000 37.73612  ?  545 HOH   I O   1 
HETATM 18173 O O   . HOH   S  4 .   ? 7.71957   15.94096  -36.32007 1.000 43.94410  ?  546 HOH   I O   1 
HETATM 18174 O O   . HOH   S  4 .   ? 6.16394   16.79631  -28.59635 1.000 30.13346  ?  547 HOH   I O   1 
HETATM 18175 O O   . HOH   S  4 .   ? 12.56046  39.11427  -17.02537 1.000 41.79383  ?  548 HOH   I O   1 
HETATM 18176 O O   . HOH   S  4 .   ? 24.94532  8.23454   -10.26064 1.000 38.13186  ?  549 HOH   I O   1 
HETATM 18177 O O   . HOH   S  4 .   ? 11.73092  -5.08998  -17.67284 1.000 34.38630  ?  550 HOH   I O   1 
HETATM 18178 O O   . HOH   S  4 .   ? 36.66526  17.79716  -26.33760 1.000 20.53772  ?  551 HOH   I O   1 
HETATM 18179 O O   . HOH   S  4 .   ? 34.40420  8.27290   -30.37950 1.000 34.66872  ?  552 HOH   I O   1 
HETATM 18180 O O   . HOH   S  4 .   ? 24.61900  34.74076  -21.98411 1.000 35.47585  ?  553 HOH   I O   1 
HETATM 18181 O O   . HOH   S  4 .   ? 4.96764   -9.09204  -17.59309 1.000 24.85529  ?  554 HOH   I O   1 
HETATM 18182 O O   . HOH   S  4 .   ? 1.89006   13.42893  -16.49330 1.000 24.26511  ?  555 HOH   I O   1 
HETATM 18183 O O   . HOH   S  4 .   ? 15.45172  3.43135   -6.48770  1.000 26.25623  ?  556 HOH   I O   1 
HETATM 18184 O O   . HOH   S  4 .   ? 26.57364  33.00204  -49.85730 1.000 91.04803  ?  557 HOH   I O   1 
HETATM 18185 O O   . HOH   S  4 .   ? 38.92373  -1.30795  -25.12589 1.000 42.46130  ?  558 HOH   I O   1 
HETATM 18186 O O   . HOH   S  4 .   ? 25.11234  23.24780  -19.02953 1.000 41.70307  ?  559 HOH   I O   1 
HETATM 18187 O O   . HOH   S  4 .   ? 5.71615   11.88106  -17.92528 1.000 27.76366  ?  560 HOH   I O   1 
HETATM 18188 O O   . HOH   S  4 .   ? 34.41842  18.99225  -25.15769 1.000 30.63511  ?  561 HOH   I O   1 
HETATM 18189 O O   . HOH   S  4 .   ? 5.28815   -10.08330 -15.40844 1.000 37.63484  ?  562 HOH   I O   1 
HETATM 18190 O O   . HOH   S  4 .   ? 4.23044   12.29817  -15.80070 1.000 29.59472  ?  563 HOH   I O   1 
HETATM 18191 O O   . HOH   S  4 .   ? 39.74533  -6.59240  -33.88793 1.000 24.02570  ?  564 HOH   I O   1 
HETATM 18192 O O   . HOH   T  4 .   ? 8.97815   -6.67084  -34.52600 1.000 46.07834  ?  601 HOH   J O   1 
HETATM 18193 O O   . HOH   T  4 .   ? 3.78701   0.96337   -31.54390 1.000 35.87455  ?  602 HOH   J O   1 
HETATM 18194 O O   . HOH   U  4 .   ? 28.14636  15.54528  14.40997  1.000 31.43820  ?  501 HOH   G O   1 
HETATM 18195 O O   . HOH   U  4 .   ? 28.74469  27.82875  9.75827   1.000 40.91024  ?  502 HOH   G O   1 
HETATM 18196 O O   . HOH   U  4 .   ? 8.01165   10.38052  5.25299   1.000 30.32911  ?  503 HOH   G O   1 
HETATM 18197 O O   . HOH   U  4 .   ? 8.73691   15.24453  -6.25445  1.000 34.46537  ?  504 HOH   G O   1 
HETATM 18198 O O   . HOH   U  4 .   ? 28.41886  24.16132  23.23482  1.000 31.89380  ?  505 HOH   G O   1 
HETATM 18199 O O   . HOH   U  4 .   ? 11.64758  37.39562  8.44903   1.000 29.30238  ?  506 HOH   G O   1 
HETATM 18200 O O   . HOH   U  4 .   ? -4.06132  22.71408  3.49951   1.000 16.52471  ?  507 HOH   G O   1 
HETATM 18201 O O   . HOH   U  4 .   ? -6.33346  27.59692  -7.62404  1.000 35.31356  ?  508 HOH   G O   1 
HETATM 18202 O O   . HOH   U  4 .   ? -1.01428  7.24160   -0.60671  1.000 20.04482  ?  509 HOH   G O   1 
HETATM 18203 O O   . HOH   U  4 .   ? 1.27001   20.89222  -10.13003 1.000 35.41098  ?  510 HOH   G O   1 
HETATM 18204 O O   . HOH   U  4 .   ? -1.51904  16.02746  -4.10895  1.000 24.77102  ?  511 HOH   G O   1 
HETATM 18205 O O   . HOH   U  4 .   ? 25.55656  27.11030  16.01020  1.000 19.55904  ?  512 HOH   G O   1 
HETATM 18206 O O   . HOH   U  4 .   ? 17.91691  11.83701  -6.53527  1.000 44.56661  ?  513 HOH   G O   1 
HETATM 18207 O O   . HOH   U  4 .   ? 15.00083  46.18427  12.13164  1.000 31.04448  ?  514 HOH   G O   1 
HETATM 18208 O O   . HOH   U  4 .   ? 0.66505   36.76141  24.93482  1.000 25.80120  ?  515 HOH   G O   1 
HETATM 18209 O O   . HOH   U  4 .   ? -9.15142  42.36489  -4.80357  1.000 21.99631  ?  516 HOH   G O   1 
HETATM 18210 O O   . HOH   U  4 .   ? -0.32423  9.34820   -2.17551  1.000 30.07840  ?  517 HOH   G O   1 
HETATM 18211 O O   . HOH   U  4 .   ? 15.62614  45.58332  14.46074  1.000 25.11347  ?  518 HOH   G O   1 
HETATM 18212 O O   . HOH   U  4 .   ? 5.43122   47.21603  7.60624   1.000 16.87512  ?  519 HOH   G O   1 
HETATM 18213 O O   . HOH   U  4 .   ? 19.25412  24.71997  6.53072   1.000 22.60101  ?  520 HOH   G O   1 
HETATM 18214 O O   . HOH   U  4 .   ? 13.47154  27.97093  11.02371  1.000 23.22001  ?  521 HOH   G O   1 
HETATM 18215 O O   . HOH   U  4 .   ? 12.63383  39.11373  25.05588  1.000 34.51659  ?  522 HOH   G O   1 
HETATM 18216 O O   . HOH   U  4 .   ? 19.57723  33.74799  16.81369  1.000 23.18474  ?  523 HOH   G O   1 
HETATM 18217 O O   . HOH   U  4 .   ? -7.19567  19.71629  5.66640   1.000 14.73739  ?  524 HOH   G O   1 
HETATM 18218 O O   . HOH   U  4 .   ? 0.45969   50.90479  12.64756  1.000 33.85639  ?  525 HOH   G O   1 
HETATM 18219 O O   . HOH   U  4 .   ? 4.75259   13.74160  -3.28971  1.000 30.00187  ?  526 HOH   G O   1 
HETATM 18220 O O   . HOH   U  4 .   ? 22.45079  34.71210  9.31918   1.000 28.24190  ?  527 HOH   G O   1 
HETATM 18221 O O   . HOH   U  4 .   ? 18.30556  45.13116  14.56802  1.000 31.28909  ?  528 HOH   G O   1 
HETATM 18222 O O   . HOH   U  4 .   ? -13.12351 4.21600   0.73476   1.000 36.21304  ?  529 HOH   G O   1 
HETATM 18223 O O   . HOH   U  4 .   ? 12.44139  35.12042  23.05081  1.000 28.59224  ?  530 HOH   G O   1 
HETATM 18224 O O   . HOH   U  4 .   ? 19.14556  23.89646  9.17617   1.000 31.64514  ?  531 HOH   G O   1 
HETATM 18225 O O   . HOH   U  4 .   ? 22.79147  50.10890  7.51256   1.000 38.38648  ?  532 HOH   G O   1 
HETATM 18226 O O   . HOH   U  4 .   ? -3.08066  39.76859  -3.00703  1.000 30.51909  ?  533 HOH   G O   1 
HETATM 18227 O O   . HOH   U  4 .   ? 18.00133  27.27863  4.11504   1.000 22.11365  ?  534 HOH   G O   1 
HETATM 18228 O O   . HOH   U  4 .   ? 19.17788  21.51800  20.71875  1.000 22.96170  ?  535 HOH   G O   1 
HETATM 18229 O O   . HOH   U  4 .   ? 0.19529   17.34580  21.52261  1.000 32.54060  ?  536 HOH   G O   1 
HETATM 18230 O O   . HOH   U  4 .   ? 10.10254  33.66714  -4.08752  1.000 28.01321  ?  537 HOH   G O   1 
HETATM 18231 O O   . HOH   U  4 .   ? 11.08594  42.91979  -7.24493  1.000 33.23407  ?  538 HOH   G O   1 
HETATM 18232 O O   . HOH   U  4 .   ? -1.69801  22.65387  7.60679   1.000 17.79026  ?  539 HOH   G O   1 
HETATM 18233 O O   . HOH   U  4 .   ? 12.22211  55.16626  14.70958  1.000 28.08081  ?  540 HOH   G O   1 
HETATM 18234 O O   . HOH   U  4 .   ? -5.13865  39.02353  21.36771  1.000 26.57972  ?  541 HOH   G O   1 
HETATM 18235 O O   . HOH   U  4 .   ? 15.31867  23.01796  15.01677  1.000 25.69569  ?  542 HOH   G O   1 
HETATM 18236 O O   . HOH   U  4 .   ? 18.76421  28.40677  18.39404  1.000 26.26480  ?  543 HOH   G O   1 
HETATM 18237 O O   . HOH   U  4 .   ? -8.84329  29.35879  8.51129   1.000 19.58846  ?  544 HOH   G O   1 
HETATM 18238 O O   . HOH   U  4 .   ? 10.70484  34.79233  25.61675  1.000 31.89262  ?  545 HOH   G O   1 
HETATM 18239 O O   . HOH   U  4 .   ? 26.73113  49.87855  18.17020  1.000 34.62381  ?  546 HOH   G O   1 
HETATM 18240 O O   . HOH   U  4 .   ? -10.57151 12.40520  16.43776  1.000 37.03476  ?  547 HOH   G O   1 
HETATM 18241 O O   . HOH   U  4 .   ? 9.87852   42.26324  27.31642  1.000 34.16012  ?  548 HOH   G O   1 
HETATM 18242 O O   . HOH   U  4 .   ? -9.17970  31.93657  6.15822   1.000 18.24034  ?  549 HOH   G O   1 
HETATM 18243 O O   . HOH   U  4 .   ? 0.60204   50.42644  15.04243  1.000 29.61114  ?  550 HOH   G O   1 
HETATM 18244 O O   . HOH   U  4 .   ? -6.17196  48.93519  11.21298  1.000 32.80471  ?  551 HOH   G O   1 
HETATM 18245 O O   . HOH   U  4 .   ? 1.19922   16.85088  -3.82896  1.000 30.20286  ?  552 HOH   G O   1 
HETATM 18246 O O   . HOH   U  4 .   ? -20.61756 16.80781  8.92575   1.000 20.25692  ?  553 HOH   G O   1 
HETATM 18247 O O   . HOH   U  4 .   ? 21.55325  22.69534  5.74921   1.000 22.57784  ?  554 HOH   G O   1 
HETATM 18248 O O   . HOH   U  4 .   ? -3.77921  26.77796  14.49268  1.000 25.99584  ?  555 HOH   G O   1 
HETATM 18249 O O   . HOH   U  4 .   ? 3.53387   40.43724  -7.09832  1.000 30.80105  ?  556 HOH   G O   1 
HETATM 18250 O O   . HOH   U  4 .   ? -6.81813  23.70466  13.05195  1.000 22.80428  ?  557 HOH   G O   1 
HETATM 18251 O O   . HOH   U  4 .   ? 19.03226  35.60410  21.14446  1.000 42.04759  ?  558 HOH   G O   1 
HETATM 18252 O O   . HOH   U  4 .   ? -0.23287  51.51540  8.52369   1.000 19.65258  ?  559 HOH   G O   1 
HETATM 18253 O O   . HOH   U  4 .   ? -12.70195 12.80064  -6.88093  1.000 30.35418  ?  560 HOH   G O   1 
HETATM 18254 O O   . HOH   U  4 .   ? -17.01944 10.92434  15.81503  1.000 21.94095  ?  561 HOH   G O   1 
HETATM 18255 O O   . HOH   U  4 .   ? -1.64860  23.18130  4.95264   1.000 22.98001  ?  562 HOH   G O   1 
HETATM 18256 O O   . HOH   U  4 .   ? 14.49755  42.47907  24.76294  1.000 40.50655  ?  563 HOH   G O   1 
HETATM 18257 O O   . HOH   U  4 .   ? -11.37037 23.16184  12.07717  1.000 22.70114  ?  564 HOH   G O   1 
HETATM 18258 O O   . HOH   U  4 .   ? -12.94839 28.09777  13.07122  1.000 30.87826  ?  565 HOH   G O   1 
HETATM 18259 O O   . HOH   U  4 .   ? 8.97327   44.94782  -0.59870  1.000 22.79978  ?  566 HOH   G O   1 
HETATM 18260 O O   . HOH   U  4 .   ? 23.52353  30.13903  19.79764  1.000 24.70966  ?  567 HOH   G O   1 
HETATM 18261 O O   . HOH   U  4 .   ? 0.64366   9.61745   22.28482  1.000 21.49195  ?  568 HOH   G O   1 
HETATM 18262 O O   . HOH   U  4 .   ? -8.96988  32.54212  15.68228  1.000 34.75344  ?  569 HOH   G O   1 
HETATM 18263 O O   . HOH   U  4 .   ? 24.57994  42.03398  17.68599  1.000 26.34311  ?  570 HOH   G O   1 
HETATM 18264 O O   . HOH   U  4 .   ? -12.21562 42.21196  13.16026  1.000 36.84173  ?  571 HOH   G O   1 
HETATM 18265 O O   . HOH   U  4 .   ? 1.21713   29.47904  21.11489  1.000 23.19991  ?  572 HOH   G O   1 
HETATM 18266 O O   . HOH   U  4 .   ? -0.28873  51.59970  5.36335   1.000 38.46765  ?  573 HOH   G O   1 
HETATM 18267 O O   . HOH   U  4 .   ? 16.23979  34.33489  22.47662  1.000 29.62155  ?  574 HOH   G O   1 
HETATM 18268 O O   . HOH   U  4 .   ? -1.14852  25.26067  16.66692  1.000 30.51590  ?  575 HOH   G O   1 
HETATM 18269 O O   . HOH   U  4 .   ? 0.04528   31.64346  21.54278  1.000 30.23214  ?  576 HOH   G O   1 
HETATM 18270 O O   . HOH   U  4 .   ? 1.37962   5.36050   -0.42597  1.000 27.93545  ?  577 HOH   G O   1 
HETATM 18271 O O   . HOH   U  4 .   ? 15.88368  40.73672  24.62990  1.000 34.50481  ?  578 HOH   G O   1 
HETATM 18272 O O   . HOH   U  4 .   ? 5.86371   7.12043   11.13683  1.000 35.77620  ?  579 HOH   G O   1 
HETATM 18273 O O   . HOH   U  4 .   ? 19.36744  31.04854  17.94757  1.000 21.29530  ?  580 HOH   G O   1 
HETATM 18274 O O   . HOH   U  4 .   ? -14.37852 16.17695  17.08680  1.000 41.65667  ?  581 HOH   G O   1 
HETATM 18275 O O   . HOH   U  4 .   ? -12.45122 25.08042  13.73101  1.000 20.67246  ?  582 HOH   G O   1 
HETATM 18276 O O   . HOH   U  4 .   ? -22.64692 18.24298  3.68627   1.000 33.33087  ?  583 HOH   G O   1 
HETATM 18277 O O   . HOH   U  4 .   ? 1.55158   39.20105  -7.53540  1.000 41.51740  ?  584 HOH   G O   1 
HETATM 18278 O O   . HOH   U  4 .   ? -15.05470 24.24092  14.05127  1.000 36.18838  ?  585 HOH   G O   1 
HETATM 18279 O O   . HOH   U  4 .   ? -9.32266  22.59973  13.76261  1.000 17.75019  ?  586 HOH   G O   1 
HETATM 18280 O O   . HOH   U  4 .   ? 35.84455  26.56295  13.52540  1.000 18.56803  ?  587 HOH   G O   1 
HETATM 18281 O O   . HOH   U  4 .   ? -6.18722  49.09205  14.29406  1.000 38.29905  ?  588 HOH   G O   1 
HETATM 18282 O O   . HOH   U  4 .   ? 34.61048  28.55012  12.82432  1.000 30.72373  ?  589 HOH   G O   1 
HETATM 18283 O O   . HOH   U  4 .   ? 18.69777  33.43674  21.53773  1.000 31.67309  ?  590 HOH   G O   1 
HETATM 18284 O O   . HOH   U  4 .   ? 34.99988  26.88731  11.00651  1.000 36.90156  ?  591 HOH   G O   1 
HETATM 18285 O O   . HOH   U  4 .   ? 21.22404  31.88812  20.40939  1.000 36.59395  ?  592 HOH   G O   1 
HETATM 18286 O O   . HOH   U  4 .   ? 7.20634   6.29638   8.93005   1.000 34.87344  ?  593 HOH   G O   1 
HETATM 18287 O O   . HOH   U  4 .   ? 8.47009   47.18047  -2.55446  1.000 32.56995  ?  594 HOH   G O   1 
HETATM 18288 O O   . HOH   U  4 .   ? -9.83375  22.10887  18.62273  1.000 24.62807  ?  595 HOH   G O   1 
HETATM 18289 O O   . HOH   U  4 .   ? -12.84313 16.45004  19.20202  1.000 42.46604  ?  596 HOH   G O   1 
HETATM 18290 O O   . HOH   U  4 .   ? -9.55606  23.78022  16.63550  1.000 26.83563  ?  597 HOH   G O   1 
HETATM 18291 O O   . HOH   U  4 .   ? -11.67222 25.26484  16.28723  1.000 29.01543  ?  598 HOH   G O   1 
HETATM 18292 O O   . HOH   U  4 .   ? -15.46533 23.95344  16.52892  1.000 44.21324  ?  599 HOH   G O   1 
HETATM 18293 O O   . HOH   V  4 .   ? 17.30287  52.60279  1.27916   1.000 36.38575  ?  601 HOH   H O   1 
HETATM 18294 O O   . HOH   V  4 .   ? 20.75286  38.98988  2.58255   1.000 31.68089  ?  602 HOH   H O   1 
HETATM 18295 O O   . HOH   V  4 .   ? 21.97660  39.04475  4.91488   1.000 24.39467  ?  603 HOH   H O   1 
HETATM 18296 O O   . HOH   V  4 .   ? 6.81904   55.08553  3.16265   1.000 35.67909  ?  604 HOH   H O   1 
HETATM 18297 O O   . HOH   V  4 .   ? 21.27836  33.22083  -0.31834  1.000 36.85569  ?  605 HOH   H O   1 
HETATM 18298 O O   . HOH   V  4 .   ? 8.48810   34.88849  -6.27913  1.000 26.18528  ?  606 HOH   H O   1 
HETATM 18299 O O   . HOH   V  4 .   ? 20.58791  30.22522  -3.14905  1.000 19.67160  ?  607 HOH   H O   1 
HETATM 18300 O O   . HOH   V  4 .   ? 24.84142  27.20637  0.22734   1.000 33.67291  ?  608 HOH   H O   1 
HETATM 18301 O O   . HOH   W  4 .   ? 3.38384   47.71379  38.37884  1.000 41.81367  ?  501 HOH   A O   1 
HETATM 18302 O O   . HOH   W  4 .   ? 11.41156  58.24643  23.12032  1.000 24.70105  ?  502 HOH   A O   1 
HETATM 18303 O O   . HOH   W  4 .   ? 20.15476  80.14916  29.00976  1.000 19.19214  ?  503 HOH   A O   1 
HETATM 18304 O O   . HOH   W  4 .   ? 28.69479  67.79041  53.55155  1.000 43.15953  ?  504 HOH   A O   1 
HETATM 18305 O O   . HOH   W  4 .   ? 5.86799   54.20968  28.55987  1.000 33.51753  ?  505 HOH   A O   1 
HETATM 18306 O O   . HOH   W  4 .   ? 6.40300   61.40686  21.07054  1.000 32.37319  ?  506 HOH   A O   1 
HETATM 18307 O O   . HOH   W  4 .   ? 3.22072   59.43713  33.16543  1.000 45.97453  ?  507 HOH   A O   1 
HETATM 18308 O O   . HOH   W  4 .   ? 11.80236  59.87486  18.46709  1.000 28.33831  ?  508 HOH   A O   1 
HETATM 18309 O O   . HOH   W  4 .   ? 20.91511  73.20076  37.66109  1.000 32.64155  ?  509 HOH   A O   1 
HETATM 18310 O O   . HOH   W  4 .   ? 32.73979  54.85133  28.20694  1.000 24.47932  ?  510 HOH   A O   1 
HETATM 18311 O O   . HOH   W  4 .   ? 44.70886  49.84147  55.13105  1.000 35.46800  ?  511 HOH   A O   1 
HETATM 18312 O O   . HOH   W  4 .   ? 17.96768  58.15221  31.31584  1.000 18.57210  ?  512 HOH   A O   1 
HETATM 18313 O O   . HOH   W  4 .   ? 37.94489  71.80151  44.03482  1.000 33.00443  ?  513 HOH   A O   1 
HETATM 18314 O O   . HOH   W  4 .   ? 11.71856  46.39426  29.66542  1.000 42.59239  ?  514 HOH   A O   1 
HETATM 18315 O O   . HOH   W  4 .   ? 32.95684  61.44163  49.93950  1.000 32.37816  ?  515 HOH   A O   1 
HETATM 18316 O O   . HOH   W  4 .   ? 27.67484  72.12351  13.01855  1.000 38.47320  ?  516 HOH   A O   1 
HETATM 18317 O O   . HOH   W  4 .   ? 32.65393  59.31851  39.02041  1.000 24.55118  ?  517 HOH   A O   1 
HETATM 18318 O O   . HOH   W  4 .   ? 55.01380  53.92805  53.59676  1.000 26.43654  ?  518 HOH   A O   1 
HETATM 18319 O O   . HOH   W  4 .   ? 36.62456  70.36562  53.58871  1.000 45.81654  ?  519 HOH   A O   1 
HETATM 18320 O O   . HOH   W  4 .   ? 13.36824  62.89643  36.49518  1.000 20.00765  ?  520 HOH   A O   1 
HETATM 18321 O O   . HOH   W  4 .   ? 40.51771  65.04074  31.90680  1.000 23.33369  ?  521 HOH   A O   1 
HETATM 18322 O O   . HOH   W  4 .   ? 15.93423  46.16845  29.26387  1.000 31.95169  ?  522 HOH   A O   1 
HETATM 18323 O O   . HOH   W  4 .   ? 38.78064  56.66632  40.87240  1.000 15.51322  ?  523 HOH   A O   1 
HETATM 18324 O O   . HOH   W  4 .   ? 12.11759  55.33235  37.44061  1.000 36.25494  ?  524 HOH   A O   1 
HETATM 18325 O O   . HOH   W  4 .   ? 40.06559  75.02550  23.50119  1.000 41.57123  ?  525 HOH   A O   1 
HETATM 18326 O O   . HOH   W  4 .   ? 50.37274  60.48226  48.13852  1.000 35.56470  ?  526 HOH   A O   1 
HETATM 18327 O O   . HOH   W  4 .   ? 12.38208  57.48398  35.66541  1.000 26.33722  ?  527 HOH   A O   1 
HETATM 18328 O O   . HOH   W  4 .   ? 35.25454  60.70384  39.97556  1.000 22.80517  ?  528 HOH   A O   1 
HETATM 18329 O O   . HOH   W  4 .   ? 42.38023  68.68793  51.16927  1.000 40.66242  ?  529 HOH   A O   1 
HETATM 18330 O O   . HOH   W  4 .   ? 31.17549  47.04429  31.62756  1.000 33.09654  ?  530 HOH   A O   1 
HETATM 18331 O O   . HOH   W  4 .   ? 31.61425  55.05834  53.77382  1.000 34.18112  ?  531 HOH   A O   1 
HETATM 18332 O O   . HOH   W  4 .   ? 37.12474  72.07592  15.82854  1.000 30.18052  ?  532 HOH   A O   1 
HETATM 18333 O O   . HOH   W  4 .   ? 6.24563   71.77564  17.22338  1.000 29.60800  ?  533 HOH   A O   1 
HETATM 18334 O O   . HOH   W  4 .   ? 55.22481  54.63859  51.25234  1.000 29.21745  ?  534 HOH   A O   1 
HETATM 18335 O O   . HOH   W  4 .   ? 24.10165  47.30309  35.12942  1.000 31.25798  ?  535 HOH   A O   1 
HETATM 18336 O O   . HOH   W  4 .   ? 52.22553  52.15510  40.26078  1.000 30.31600  ?  536 HOH   A O   1 
HETATM 18337 O O   . HOH   W  4 .   ? 29.69611  67.67985  11.23896  1.000 42.29265  ?  537 HOH   A O   1 
HETATM 18338 O O   . HOH   W  4 .   ? 48.23875  45.45112  37.80321  1.000 31.03088  ?  538 HOH   A O   1 
HETATM 18339 O O   . HOH   W  4 .   ? 51.75166  54.13967  58.03125  1.000 34.90175  ?  539 HOH   A O   1 
HETATM 18340 O O   . HOH   W  4 .   ? 14.25404  61.18728  38.71121  1.000 32.06593  ?  540 HOH   A O   1 
HETATM 18341 O O   . HOH   W  4 .   ? 30.49785  61.31367  49.49889  1.000 29.83676  ?  541 HOH   A O   1 
HETATM 18342 O O   . HOH   W  4 .   ? 37.82432  61.37195  46.18746  1.000 26.10706  ?  542 HOH   A O   1 
HETATM 18343 O O   . HOH   W  4 .   ? 15.90192  69.12609  17.06248  1.000 37.99767  ?  543 HOH   A O   1 
HETATM 18344 O O   . HOH   W  4 .   ? 27.16630  80.23891  34.06319  1.000 21.89836  ?  544 HOH   A O   1 
HETATM 18345 O O   . HOH   W  4 .   ? 26.39753  44.38755  31.74250  1.000 36.09304  ?  545 HOH   A O   1 
HETATM 18346 O O   . HOH   W  4 .   ? 16.27714  52.13730  32.32937  1.000 34.92566  ?  546 HOH   A O   1 
HETATM 18347 O O   . HOH   W  4 .   ? 44.42046  61.66311  54.03646  1.000 22.67312  ?  547 HOH   A O   1 
HETATM 18348 O O   . HOH   W  4 .   ? 33.08991  57.26377  37.20050  1.000 22.59412  ?  548 HOH   A O   1 
HETATM 18349 O O   . HOH   W  4 .   ? 34.25176  76.65403  31.85139  1.000 22.57898  ?  549 HOH   A O   1 
HETATM 18350 O O   . HOH   W  4 .   ? 47.77961  55.53878  32.20152  1.000 33.63535  ?  550 HOH   A O   1 
HETATM 18351 O O   . HOH   W  4 .   ? 20.34274  51.02714  45.93168  1.000 38.54456  ?  551 HOH   A O   1 
HETATM 18352 O O   . HOH   W  4 .   ? 9.97724   59.01613  38.66767  1.000 25.03670  ?  552 HOH   A O   1 
HETATM 18353 O O   . HOH   W  4 .   ? 45.46348  69.40608  34.04163  1.000 33.31424  ?  553 HOH   A O   1 
HETATM 18354 O O   . HOH   W  4 .   ? 47.12035  78.10274  28.82815  1.000 27.30227  ?  554 HOH   A O   1 
HETATM 18355 O O   . HOH   W  4 .   ? 42.40019  58.32982  30.26594  1.000 26.84803  ?  555 HOH   A O   1 
HETATM 18356 O O   . HOH   W  4 .   ? 33.35055  70.69966  12.42869  1.000 35.68222  ?  556 HOH   A O   1 
HETATM 18357 O O   . HOH   W  4 .   ? 24.09041  71.27767  42.21729  1.000 34.25475  ?  557 HOH   A O   1 
HETATM 18358 O O   . HOH   W  4 .   ? 32.24892  52.61842  29.37053  1.000 23.17503  ?  558 HOH   A O   1 
HETATM 18359 O O   . HOH   W  4 .   ? 30.59653  70.48843  12.22245  1.000 33.70883  ?  559 HOH   A O   1 
HETATM 18360 O O   . HOH   W  4 .   ? 42.28556  43.50746  38.72705  1.000 32.64334  ?  560 HOH   A O   1 
HETATM 18361 O O   . HOH   W  4 .   ? 8.79099   76.08162  17.72222  1.000 29.15093  ?  561 HOH   A O   1 
HETATM 18362 O O   . HOH   W  4 .   ? 20.06146  66.74445  26.39713  1.000 19.11292  ?  562 HOH   A O   1 
HETATM 18363 O O   . HOH   W  4 .   ? 28.60331  51.84755  19.15274  1.000 31.54745  ?  563 HOH   A O   1 
HETATM 18364 O O   . HOH   W  4 .   ? 40.09298  61.22643  31.74302  1.000 29.41855  ?  564 HOH   A O   1 
HETATM 18365 O O   . HOH   W  4 .   ? 40.18587  58.49999  57.44725  1.000 32.90613  ?  565 HOH   A O   1 
HETATM 18366 O O   . HOH   W  4 .   ? 41.66320  47.35942  32.99012  1.000 25.17500  ?  566 HOH   A O   1 
HETATM 18367 O O   . HOH   W  4 .   ? 25.69581  43.98908  45.89627  1.000 31.65158  ?  567 HOH   A O   1 
HETATM 18368 O O   . HOH   W  4 .   ? 48.35769  42.62230  40.27168  1.000 36.96731  ?  568 HOH   A O   1 
HETATM 18369 O O   . HOH   W  4 .   ? 30.17861  84.26600  25.70386  1.000 33.43748  ?  569 HOH   A O   1 
HETATM 18370 O O   . HOH   W  4 .   ? 32.12174  76.13047  35.01419  1.000 26.83199  ?  570 HOH   A O   1 
HETATM 18371 O O   . HOH   W  4 .   ? 51.53851  57.89425  50.02187  1.000 35.98029  ?  571 HOH   A O   1 
HETATM 18372 O O   . HOH   W  4 .   ? 44.66739  68.91033  37.03881  1.000 15.89536  ?  572 HOH   A O   1 
HETATM 18373 O O   . HOH   W  4 .   ? 41.20146  72.24333  16.47840  1.000 30.91668  ?  573 HOH   A O   1 
HETATM 18374 O O   . HOH   W  4 .   ? 18.47360  54.85561  17.37082  1.000 22.66974  ?  574 HOH   A O   1 
HETATM 18375 O O   . HOH   W  4 .   ? 32.22138  72.37371  54.89323  1.000 49.10299  ?  575 HOH   A O   1 
HETATM 18376 O O   . HOH   W  4 .   ? 33.93140  54.21763  30.93404  1.000 29.05351  ?  576 HOH   A O   1 
HETATM 18377 O O   . HOH   W  4 .   ? 46.89326  62.88986  41.76729  1.000 30.57695  ?  577 HOH   A O   1 
HETATM 18378 O O   . HOH   W  4 .   ? 29.97736  51.82994  23.18195  1.000 35.51611  ?  578 HOH   A O   1 
HETATM 18379 O O   . HOH   W  4 .   ? 13.62532  63.13527  42.64991  1.000 36.38694  ?  579 HOH   A O   1 
HETATM 18380 O O   . HOH   W  4 .   ? 49.47625  59.00445  51.47572  1.000 30.08483  ?  580 HOH   A O   1 
HETATM 18381 O O   . HOH   W  4 .   ? 48.11896  61.09222  42.60481  1.000 34.79954  ?  581 HOH   A O   1 
HETATM 18382 O O   . HOH   W  4 .   ? 7.50826   46.26497  55.56577  1.000 48.05092  ?  582 HOH   A O   1 
HETATM 18383 O O   . HOH   W  4 .   ? 24.25734  76.08779  39.87389  1.000 36.91477  ?  583 HOH   A O   1 
HETATM 18384 O O   . HOH   W  4 .   ? 50.92037  44.12636  40.85796  1.000 32.98893  ?  584 HOH   A O   1 
HETATM 18385 O O   . HOH   W  4 .   ? 29.69891  49.33331  22.47848  1.000 36.62074  ?  585 HOH   A O   1 
HETATM 18386 O O   . HOH   W  4 .   ? 54.04293  57.01549  50.85167  1.000 29.85105  ?  586 HOH   A O   1 
HETATM 18387 O O   . HOH   W  4 .   ? 48.46735  61.19560  50.91189  1.000 45.06493  ?  587 HOH   A O   1 
HETATM 18388 O O   . HOH   W  4 .   ? 42.19335  63.69059  33.51202  1.000 25.37867  ?  588 HOH   A O   1 
HETATM 18389 O O   . HOH   W  4 .   ? 41.98030  73.73995  23.19801  1.000 40.64821  ?  589 HOH   A O   1 
HETATM 18390 O O   . HOH   W  4 .   ? 32.56264  68.31241  10.90051  1.000 36.29868  ?  590 HOH   A O   1 
HETATM 18391 O O   . HOH   X  4 .   ? 30.94666  78.10853  20.94451  1.000 40.28850  ?  601 HOH   B O   1 
HETATM 18392 O O   . HOH   X  4 .   ? 9.15033   63.84457  27.85449  1.000 40.01480  ?  602 HOH   B O   1 
HETATM 18393 O O   . HOH   X  4 .   ? 14.23286  82.37189  19.42787  1.000 43.71849  ?  603 HOH   B O   1 
HETATM 18394 O O   . HOH   X  4 .   ? 15.38629  79.01432  25.37668  1.000 37.33168  ?  604 HOH   B O   1 
HETATM 18395 O O   . HOH   X  4 .   ? 13.63046  73.05860  41.06573  1.000 38.05651  ?  605 HOH   B O   1 
HETATM 18396 O O   . HOH   X  4 .   ? 25.29420  78.54561  23.66829  1.000 33.15836  ?  606 HOH   B O   1 
HETATM 18397 O O   . HOH   X  4 .   ? 22.97717  75.96647  37.79427  1.000 23.59217  ?  607 HOH   B O   1 
HETATM 18398 O O   . HOH   X  4 .   ? 9.35257   70.55369  27.41720  1.000 25.76053  ?  608 HOH   B O   1 
HETATM 18399 O O   . HOH   X  4 .   ? 11.49155  70.53931  39.96617  1.000 39.20237  ?  609 HOH   B O   1 
HETATM 18400 O O   . HOH   Y  4 .   ? 44.33123  49.66045  18.48821  1.000 26.16602  ?  501 HOH   C O   1 
HETATM 18401 O O   . HOH   Y  4 .   ? 48.25046  41.38958  24.20241  1.000 31.86992  ?  502 HOH   C O   1 
HETATM 18402 O O   . HOH   Y  4 .   ? 72.89444  27.42783  6.86356   1.000 35.57495  ?  503 HOH   C O   1 
HETATM 18403 O O   . HOH   Y  4 .   ? 49.60437  29.77554  23.98471  1.000 24.48608  ?  504 HOH   C O   1 
HETATM 18404 O O   . HOH   Y  4 .   ? 38.11204  36.73897  -1.18974  1.000 34.83414  ?  505 HOH   C O   1 
HETATM 18405 O O   . HOH   Y  4 .   ? 30.95669  33.94484  19.26375  1.000 36.01940  ?  506 HOH   C O   1 
HETATM 18406 O O   . HOH   Y  4 .   ? 66.58951  58.29434  -9.42396  1.000 51.11191  ?  507 HOH   C O   1 
HETATM 18407 O O   . HOH   Y  4 .   ? 26.59257  54.36865  -3.40714  1.000 41.85309  ?  508 HOH   C O   1 
HETATM 18408 O O   . HOH   Y  4 .   ? 27.78012  41.07820  -4.85968  1.000 32.70117  ?  509 HOH   C O   1 
HETATM 18409 O O   . HOH   Y  4 .   ? 54.16409  51.42030  12.88804  1.000 44.29905  ?  510 HOH   C O   1 
HETATM 18410 O O   . HOH   Y  4 .   ? 42.95505  42.36734  2.27584   1.000 22.75061  ?  511 HOH   C O   1 
HETATM 18411 O O   . HOH   Y  4 .   ? 45.61813  26.06797  0.90638   1.000 30.94421  ?  512 HOH   C O   1 
HETATM 18412 O O   . HOH   Y  4 .   ? 27.94510  41.20924  1.35065   1.000 28.48003  ?  513 HOH   C O   1 
HETATM 18413 O O   . HOH   Y  4 .   ? 67.12745  53.45875  -9.98284  1.000 36.11722  ?  514 HOH   C O   1 
HETATM 18414 O O   . HOH   Y  4 .   ? 65.56245  38.40964  -0.06545  1.000 26.92508  ?  515 HOH   C O   1 
HETATM 18415 O O   . HOH   Y  4 .   ? 49.24149  35.66298  25.62582  1.000 38.96681  ?  516 HOH   C O   1 
HETATM 18416 O O   . HOH   Y  4 .   ? 56.31382  39.10892  -20.41663 1.000 36.98607  ?  517 HOH   C O   1 
HETATM 18417 O O   . HOH   Y  4 .   ? 37.59291  37.92628  19.18806  1.000 42.03432  ?  518 HOH   C O   1 
HETATM 18418 O O   . HOH   Y  4 .   ? 36.69698  44.92603  9.92258   1.000 28.70598  ?  519 HOH   C O   1 
HETATM 18419 O O   . HOH   Y  4 .   ? 65.39583  21.63030  8.39671   1.000 26.84442  ?  520 HOH   C O   1 
HETATM 18420 O O   . HOH   Y  4 .   ? 63.49154  40.89347  -7.67658  1.000 22.24462  ?  521 HOH   C O   1 
HETATM 18421 O O   . HOH   Y  4 .   ? 56.73851  29.90762  21.82231  1.000 36.55178  ?  522 HOH   C O   1 
HETATM 18422 O O   . HOH   Y  4 .   ? 63.82555  18.29813  7.42901   1.000 28.67146  ?  523 HOH   C O   1 
HETATM 18423 O O   . HOH   Y  4 .   ? 56.00992  50.72247  15.89677  1.000 28.14209  ?  524 HOH   C O   1 
HETATM 18424 O O   . HOH   Y  4 .   ? 60.08741  37.12918  -5.84093  1.000 25.09838  ?  525 HOH   C O   1 
HETATM 18425 O O   . HOH   Y  4 .   ? 64.80622  23.61672  11.22941  1.000 28.47305  ?  526 HOH   C O   1 
HETATM 18426 O O   . HOH   Y  4 .   ? 57.50643  38.71528  -4.83964  1.000 20.63617  ?  527 HOH   C O   1 
HETATM 18427 O O   . HOH   Y  4 .   ? 39.05206  47.52926  10.05430  1.000 35.49781  ?  528 HOH   C O   1 
HETATM 18428 O O   . HOH   Y  4 .   ? 50.86744  30.57438  17.96465  1.000 27.61831  ?  529 HOH   C O   1 
HETATM 18429 O O   . HOH   Y  4 .   ? 28.24781  50.21763  -8.12658  1.000 32.71833  ?  530 HOH   C O   1 
HETATM 18430 O O   . HOH   Y  4 .   ? 51.85590  61.93607  -4.76270  1.000 48.19708  ?  531 HOH   C O   1 
HETATM 18431 O O   . HOH   Y  4 .   ? 37.72112  48.89915  5.62769   1.000 34.10253  ?  532 HOH   C O   1 
HETATM 18432 O O   . HOH   Y  4 .   ? 72.36642  23.67644  9.61363   1.000 16.32030  ?  533 HOH   C O   1 
HETATM 18433 O O   . HOH   Y  4 .   ? 51.16978  55.23022  17.51744  1.000 35.71318  ?  534 HOH   C O   1 
HETATM 18434 O O   . HOH   Y  4 .   ? 52.23603  20.25559  5.84682   1.000 24.86233  ?  535 HOH   C O   1 
HETATM 18435 O O   . HOH   Y  4 .   ? 61.81148  47.21945  10.43531  1.000 34.87248  ?  536 HOH   C O   1 
HETATM 18436 O O   . HOH   Y  4 .   ? 63.15554  45.38222  -1.17893  1.000 26.93130  ?  537 HOH   C O   1 
HETATM 18437 O O   . HOH   Y  4 .   ? 37.31320  41.98295  -2.33428  1.000 30.09144  ?  538 HOH   C O   1 
HETATM 18438 O O   . HOH   Y  4 .   ? 70.27559  30.72131  2.40976   1.000 25.25921  ?  539 HOH   C O   1 
HETATM 18439 O O   . HOH   Y  4 .   ? 32.85868  49.22483  7.62500   1.000 45.39948  ?  540 HOH   C O   1 
HETATM 18440 O O   . HOH   Y  4 .   ? 57.94228  41.27099  -3.96686  1.000 16.70279  ?  541 HOH   C O   1 
HETATM 18441 O O   . HOH   Y  4 .   ? 56.83349  27.67797  21.08614  1.000 38.46374  ?  542 HOH   C O   1 
HETATM 18442 O O   . HOH   Y  4 .   ? 55.87343  59.00764  -12.47937 1.000 32.62237  ?  543 HOH   C O   1 
HETATM 18443 O O   . HOH   Y  4 .   ? 40.40792  40.87372  24.63994  1.000 37.77678  ?  544 HOH   C O   1 
HETATM 18444 O O   . HOH   Y  4 .   ? 65.64045  35.85540  3.13314   1.000 21.92281  ?  545 HOH   C O   1 
HETATM 18445 O O   . HOH   Y  4 .   ? 37.18184  39.73026  -3.00805  1.000 30.78526  ?  546 HOH   C O   1 
HETATM 18446 O O   . HOH   Y  4 .   ? 42.14437  46.93912  -4.94497  1.000 35.16387  ?  547 HOH   C O   1 
HETATM 18447 O O   . HOH   Y  4 .   ? 55.46728  33.55773  23.66339  1.000 32.18183  ?  548 HOH   C O   1 
HETATM 18448 O O   . HOH   Y  4 .   ? 54.99843  50.66194  7.62267   1.000 26.34240  ?  549 HOH   C O   1 
HETATM 18449 O O   . HOH   Y  4 .   ? 62.17480  33.25785  21.07344  1.000 29.95282  ?  550 HOH   C O   1 
HETATM 18450 O O   . HOH   Y  4 .   ? 55.93998  36.17546  23.76203  1.000 38.09240  ?  551 HOH   C O   1 
HETATM 18451 O O   . HOH   Y  4 .   ? 53.93172  23.30930  -0.18830  1.000 49.06363  ?  552 HOH   C O   1 
HETATM 18452 O O   . HOH   Y  4 .   ? 29.50934  38.48444  1.42263   1.000 35.23244  ?  553 HOH   C O   1 
HETATM 18453 O O   . HOH   Y  4 .   ? 45.09931  35.53132  9.26423   1.000 24.89964  ?  554 HOH   C O   1 
HETATM 18454 O O   . HOH   Y  4 .   ? 38.10811  63.07467  -6.62570  1.000 35.11163  ?  555 HOH   C O   1 
HETATM 18455 O O   . HOH   Y  4 .   ? 59.77011  45.50821  2.56520   1.000 35.31936  ?  556 HOH   C O   1 
HETATM 18456 O O   . HOH   Y  4 .   ? 25.23009  53.33272  -1.66495  1.000 55.21450  ?  557 HOH   C O   1 
HETATM 18457 O O   . HOH   Y  4 .   ? 47.17871  24.39233  12.76414  1.000 33.37258  ?  558 HOH   C O   1 
HETATM 18458 O O   . HOH   Y  4 .   ? 45.55418  30.70033  -4.76734  1.000 31.07615  ?  559 HOH   C O   1 
HETATM 18459 O O   . HOH   Y  4 .   ? 33.87580  29.32785  21.00763  1.000 28.96198  ?  560 HOH   C O   1 
HETATM 18460 O O   . HOH   Y  4 .   ? 63.16151  25.56058  18.38557  1.000 26.93531  ?  561 HOH   C O   1 
HETATM 18461 O O   . HOH   Y  4 .   ? 56.29736  59.87402  -10.40139 1.000 48.45765  ?  562 HOH   C O   1 
HETATM 18462 O O   . HOH   Y  4 .   ? 56.74843  23.89820  3.73235   1.000 23.97493  ?  563 HOH   C O   1 
HETATM 18463 O O   . HOH   Y  4 .   ? 57.57693  46.96499  2.72684   1.000 35.67431  ?  564 HOH   C O   1 
HETATM 18464 O O   . HOH   Y  4 .   ? 62.04370  47.34931  0.41734   1.000 31.95008  ?  565 HOH   C O   1 
HETATM 18465 O O   . HOH   Y  4 .   ? 69.46587  30.45353  -0.52888  1.000 6.73357   ?  566 HOH   C O   1 
HETATM 18466 O O   . HOH   Y  4 .   ? 65.22266  46.83633  -1.71407  1.000 29.27936  ?  567 HOH   C O   1 
HETATM 18467 O O   . HOH   Y  4 .   ? 20.69446  45.68809  2.14308   1.000 33.53043  ?  568 HOH   C O   1 
HETATM 18468 O O   . HOH   Y  4 .   ? 31.43670  49.97333  9.76501   1.000 51.13382  ?  569 HOH   C O   1 
HETATM 18469 O O   . HOH   Y  4 .   ? 21.71086  43.76111  2.99477   1.000 29.93052  ?  570 HOH   C O   1 
HETATM 18470 O O   . HOH   Y  4 .   ? 56.88321  38.55618  23.67407  1.000 27.67388  ?  571 HOH   C O   1 
HETATM 18471 O O   . HOH   Y  4 .   ? 25.14340  38.16014  4.83794   1.000 35.88625  ?  572 HOH   C O   1 
HETATM 18472 O O   . HOH   Y  4 .   ? 62.93556  30.81386  22.35205  1.000 33.24464  ?  573 HOH   C O   1 
HETATM 18473 O O   . HOH   Y  4 .   ? 44.51286  31.33354  -7.37559  1.000 42.94153  ?  574 HOH   C O   1 
HETATM 18474 O O   . HOH   Z  4 .   ? 55.87970  25.95923  17.68808  1.000 31.02303  ?  601 HOH   D O   1 
HETATM 18475 O O   . HOH   Z  4 .   ? 38.38515  22.74407  20.03528  1.000 39.27871  ?  602 HOH   D O   1 
HETATM 18476 O O   . HOH   Z  4 .   ? 35.22536  29.97691  8.16321   1.000 33.95077  ?  603 HOH   D O   1 
HETATM 18477 O O   . HOH   Z  4 .   ? 33.94437  38.00627  7.38354   1.000 20.80168  ?  604 HOH   D O   1 
HETATM 18478 O O   . HOH   Z  4 .   ? 55.29612  26.13669  20.25862  1.000 40.43051  ?  605 HOH   D O   1 
HETATM 18479 O O   . HOH   Z  4 .   ? 53.23372  20.82369  21.51335  1.000 39.89688  ?  606 HOH   D O   1 
HETATM 18480 O O   . HOH   Z  4 .   ? 47.59321  23.54337  0.63862   1.000 26.96118  ?  607 HOH   D O   1 
HETATM 18481 O O   . HOH   Z  4 .   ? 49.90196  24.78930  15.35407  1.000 34.13140  ?  608 HOH   D O   1 
HETATM 18482 O O   . HOH   Z  4 .   ? 36.69999  24.27669  21.50345  1.000 43.19588  ?  609 HOH   D O   1 
HETATM 18483 O O   . HOH   AA 4 .   ? 2.59081   13.06030  47.12238  1.000 50.84246  ?  501 HOH   E O   1 
HETATM 18484 O O   . HOH   AA 4 .   ? -22.32287 1.92681   63.71368  1.000 54.90265  ?  502 HOH   E O   1 
HETATM 18485 O O   . HOH   AA 4 .   ? 7.59920   7.38111   47.09234  1.000 68.50768  ?  503 HOH   E O   1 
HETATM 18486 O O   . HOH   AA 4 .   ? 6.74273   7.79910   44.73648  1.000 47.55624  ?  504 HOH   E O   1 
HETATM 18487 O O   . HOH   AA 4 .   ? -14.10298 11.00763  69.45611  1.000 42.04124  ?  505 HOH   E O   1 
HETATM 18488 O O   . HOH   AA 4 .   ? -14.90833 -14.18498 75.42087  1.000 30.81755  ?  506 HOH   E O   1 
HETATM 18489 O O   . HOH   AA 4 .   ? -3.44737  17.49907  45.25139  1.000 46.44951  ?  507 HOH   E O   1 
HETATM 18490 O O   . HOH   AA 4 .   ? -12.83442 -18.31933 72.46420  1.000 31.93005  ?  508 HOH   E O   1 
HETATM 18491 O O   . HOH   AA 4 .   ? -2.48463  -22.59240 76.71530  1.000 54.66870  ?  509 HOH   E O   1 
HETATM 18492 O O   . HOH   AA 4 .   ? -4.04528  3.28012   73.60897  1.000 32.21394  ?  510 HOH   E O   1 
HETATM 18493 O O   . HOH   AA 4 .   ? -1.76419  -15.67294 74.91514  1.000 28.57476  ?  511 HOH   E O   1 
HETATM 18494 O O   . HOH   AA 4 .   ? 18.97715  -9.91863  60.10666  1.000 38.27677  ?  512 HOH   E O   1 
HETATM 18495 O O   . HOH   AA 4 .   ? 0.69999   -10.25461 81.54035  1.000 36.75526  ?  513 HOH   E O   1 
HETATM 18496 O O   . HOH   AA 4 .   ? 9.83521   -7.64248  58.24430  1.000 28.99605  ?  514 HOH   E O   1 
HETATM 18497 O O   . HOH   AA 4 .   ? 0.81626   -20.09215 68.29170  1.000 16.17087  ?  515 HOH   E O   1 
HETATM 18498 O O   . HOH   AA 4 .   ? 8.17056   -6.92267  39.06148  1.000 43.95510  ?  516 HOH   E O   1 
HETATM 18499 O O   . HOH   AA 4 .   ? -6.13495  4.95624   22.26461  1.000 40.52617  ?  517 HOH   E O   1 
HETATM 18500 O O   . HOH   AA 4 .   ? -13.41239 -7.42770  44.35339  1.000 19.76710  ?  518 HOH   E O   1 
HETATM 18501 O O   . HOH   AA 4 .   ? -10.28329 -14.15182 44.44621  1.000 32.82793  ?  519 HOH   E O   1 
HETATM 18502 O O   . HOH   AA 4 .   ? -12.89902 -5.75342  71.66054  1.000 39.18837  ?  520 HOH   E O   1 
HETATM 18503 O O   . HOH   AA 4 .   ? -10.54024 0.03535   42.07096  1.000 29.93578  ?  521 HOH   E O   1 
HETATM 18504 O O   . HOH   AA 4 .   ? -8.58204  0.88988   46.72241  1.000 27.04931  ?  522 HOH   E O   1 
HETATM 18505 O O   . HOH   AA 4 .   ? -26.88823 -1.39757  58.74781  1.000 40.83644  ?  523 HOH   E O   1 
HETATM 18506 O O   . HOH   AA 4 .   ? 8.33283   -4.66438  57.61586  1.000 42.08453  ?  524 HOH   E O   1 
HETATM 18507 O O   . HOH   AA 4 .   ? 2.46111   -10.57685 57.98271  1.000 23.19934  ?  525 HOH   E O   1 
HETATM 18508 O O   . HOH   AA 4 .   ? -1.43829  11.51522  37.09364  1.000 34.55658  ?  526 HOH   E O   1 
HETATM 18509 O O   . HOH   AA 4 .   ? 10.10300  -4.32137  41.10399  1.000 40.69221  ?  527 HOH   E O   1 
HETATM 18510 O O   . HOH   AA 4 .   ? 5.46224   -19.13777 59.91356  1.000 15.97034  ?  528 HOH   E O   1 
HETATM 18511 O O   . HOH   AA 4 .   ? -17.84501 -0.01507  51.97202  1.000 35.90417  ?  529 HOH   E O   1 
HETATM 18512 O O   . HOH   AA 4 .   ? 5.46950   -14.76315 53.68341  1.000 31.80394  ?  530 HOH   E O   1 
HETATM 18513 O O   . HOH   AA 4 .   ? -7.95843  6.55173   42.64908  1.000 28.08318  ?  531 HOH   E O   1 
HETATM 18514 O O   . HOH   AA 4 .   ? 3.84477   -17.85789 64.93757  1.000 28.21759  ?  532 HOH   E O   1 
HETATM 18515 O O   . HOH   AA 4 .   ? -7.07462  -20.03304 76.42277  1.000 32.12637  ?  533 HOH   E O   1 
HETATM 18516 O O   . HOH   AA 4 .   ? -7.51289  -3.71903  46.96630  1.000 15.95329  ?  534 HOH   E O   1 
HETATM 18517 O O   . HOH   AA 4 .   ? -19.10717 -19.04755 65.10298  1.000 37.91334  ?  535 HOH   E O   1 
HETATM 18518 O O   . HOH   AA 4 .   ? -19.08610 -4.77865  48.02605  1.000 34.14475  ?  536 HOH   E O   1 
HETATM 18519 O O   . HOH   AA 4 .   ? -16.66261 -2.57946  49.05646  1.000 33.57233  ?  537 HOH   E O   1 
HETATM 18520 O O   . HOH   AA 4 .   ? 10.47516  -10.25574 55.08337  1.000 35.76719  ?  538 HOH   E O   1 
HETATM 18521 O O   . HOH   AA 4 .   ? 8.31185   -21.77850 53.67128  1.000 21.97348  ?  539 HOH   E O   1 
HETATM 18522 O O   . HOH   AA 4 .   ? -10.99586 7.32633   62.01695  1.000 35.22950  ?  540 HOH   E O   1 
HETATM 18523 O O   . HOH   AA 4 .   ? 7.93953   -4.97645  59.92576  1.000 31.82211  ?  541 HOH   E O   1 
HETATM 18524 O O   . HOH   AA 4 .   ? 23.30460  -12.73703 45.09726  1.000 33.64813  ?  542 HOH   E O   1 
HETATM 18525 O O   . HOH   AA 4 .   ? -7.15505  -0.85585  47.82326  1.000 21.91325  ?  543 HOH   E O   1 
HETATM 18526 O O   . HOH   AA 4 .   ? 20.09984  -13.41121 54.01785  1.000 26.18484  ?  544 HOH   E O   1 
HETATM 18527 O O   . HOH   AA 4 .   ? -10.81051 -17.52398 52.50712  1.000 29.30471  ?  545 HOH   E O   1 
HETATM 18528 O O   . HOH   AA 4 .   ? 4.06449   11.53396  31.37636  1.000 45.23235  ?  546 HOH   E O   1 
HETATM 18529 O O   . HOH   AA 4 .   ? -12.02662 -14.37289 38.63139  1.000 29.11485  ?  547 HOH   E O   1 
HETATM 18530 O O   . HOH   AA 4 .   ? 14.30786  -14.35984 70.65638  1.000 29.70423  ?  548 HOH   E O   1 
HETATM 18531 O O   . HOH   AA 4 .   ? -1.77084  7.08338   64.27024  1.000 30.12779  ?  549 HOH   E O   1 
HETATM 18532 O O   . HOH   AA 4 .   ? 5.39731   -2.36180  36.11147  1.000 30.55806  ?  550 HOH   E O   1 
HETATM 18533 O O   . HOH   AA 4 .   ? -16.06905 -3.42347  43.66391  1.000 34.69369  ?  551 HOH   E O   1 
HETATM 18534 O O   . HOH   AA 4 .   ? -8.54000  9.03583   67.06049  1.000 44.05805  ?  552 HOH   E O   1 
HETATM 18535 O O   . HOH   AA 4 .   ? 19.22100  -23.02019 56.87403  1.000 32.24113  ?  553 HOH   E O   1 
HETATM 18536 O O   . HOH   AA 4 .   ? -4.30552  -14.78029 74.17598  1.000 35.92648  ?  554 HOH   E O   1 
HETATM 18537 O O   . HOH   AA 4 .   ? -21.60581 -11.14822 69.73343  1.000 36.17570  ?  555 HOH   E O   1 
HETATM 18538 O O   . HOH   AA 4 .   ? -3.13817  -15.19622 81.56642  1.000 34.55612  ?  556 HOH   E O   1 
HETATM 18539 O O   . HOH   AA 4 .   ? 14.54909  -26.27984 60.20525  1.000 33.38178  ?  557 HOH   E O   1 
HETATM 18540 O O   . HOH   AA 4 .   ? 12.70445  -7.46059  57.29703  1.000 30.13126  ?  558 HOH   E O   1 
HETATM 18541 O O   . HOH   AA 4 .   ? 2.21293   -20.38186 62.72990  1.000 41.16215  ?  559 HOH   E O   1 
HETATM 18542 O O   . HOH   AA 4 .   ? -11.44307 4.14404   72.11961  1.000 49.80719  ?  560 HOH   E O   1 
HETATM 18543 O O   . HOH   AA 4 .   ? -20.28575 -15.22069 56.19154  1.000 37.69038  ?  561 HOH   E O   1 
HETATM 18544 O O   . HOH   AA 4 .   ? 20.51741  -16.16799 52.58538  1.000 38.83478  ?  562 HOH   E O   1 
HETATM 18545 O O   . HOH   AA 4 .   ? -20.82861 -8.25632  56.83067  1.000 36.25732  ?  563 HOH   E O   1 
HETATM 18546 O O   . HOH   AA 4 .   ? 0.23820   12.08834  38.72944  1.000 35.47438  ?  564 HOH   E O   1 
HETATM 18547 O O   . HOH   AA 4 .   ? -8.25152  -17.46916 79.12692  1.000 35.84401  ?  565 HOH   E O   1 
HETATM 18548 O O   . HOH   AA 4 .   ? 4.43815   -18.99274 62.72449  1.000 18.60932  ?  566 HOH   E O   1 
HETATM 18549 O O   . HOH   AA 4 .   ? -27.49109 7.65538   60.46442  1.000 31.89535  ?  567 HOH   E O   1 
HETATM 18550 O O   . HOH   AA 4 .   ? -15.42266 -6.93378  42.48651  1.000 38.14504  ?  568 HOH   E O   1 
HETATM 18551 O O   . HOH   AA 4 .   ? -15.20120 -16.87672 76.46189  1.000 41.76726  ?  569 HOH   E O   1 
HETATM 18552 O O   . HOH   AA 4 .   ? -9.58251  -16.36445 80.76006  1.000 44.34596  ?  570 HOH   E O   1 
HETATM 18553 O O   . HOH   AA 4 .   ? -9.79022  -6.62100  22.44825  1.000 49.10804  ?  571 HOH   E O   1 
HETATM 18554 O O   . HOH   AA 4 .   ? -19.85919 -14.22193 53.60609  1.000 28.80793  ?  572 HOH   E O   1 
HETATM 18555 O O   . HOH   AA 4 .   ? 2.73525   9.23380   34.51434  1.000 32.53113  ?  573 HOH   E O   1 
HETATM 18556 O O   . HOH   BA 4 .   ? 8.93233   3.25108   59.24339  1.000 38.38741  ?  601 HOH   F O   1 
HETATM 18557 O O   . HOH   BA 4 .   ? 5.58180   -4.86258  71.84717  1.000 34.57692  ?  602 HOH   F O   1 
HETATM 18558 O O   . HOH   BA 4 .   ? -3.59658  -4.82666  83.87345  1.000 47.45628  ?  603 HOH   F O   1 
HETATM 18559 O O   . HOH   BA 4 .   ? 7.51862   -11.17329 68.01568  1.000 30.55010  ?  604 HOH   F O   1 
HETATM 18560 O O   . HOH   CA 4 .   ? 27.19278  13.47574  39.92077  1.000 57.14500  ?  501 HOH   K O   1 
HETATM 18561 O O   . HOH   CA 4 .   ? 31.84688  2.52071   37.18716  1.000 79.00004  ?  502 HOH   K O   1 
HETATM 18562 O O   . HOH   CA 4 .   ? 49.78781  6.78055   60.81445  1.000 30.73530  ?  503 HOH   K O   1 
HETATM 18563 O O   . HOH   CA 4 .   ? 65.84380  22.55515  62.00216  1.000 36.20339  ?  504 HOH   K O   1 
HETATM 18564 O O   . HOH   CA 4 .   ? 35.86600  11.98767  60.97856  1.000 46.15768  ?  505 HOH   K O   1 
HETATM 18565 O O   . HOH   CA 4 .   ? 63.35820  3.33566   49.98788  1.000 35.90733  ?  506 HOH   K O   1 
HETATM 18566 O O   . HOH   CA 4 .   ? 52.29725  7.17839   32.71625  1.000 40.69112  ?  507 HOH   K O   1 
HETATM 18567 O O   . HOH   CA 4 .   ? 60.30142  15.61035  44.87127  1.000 23.67618  ?  508 HOH   K O   1 
HETATM 18568 O O   . HOH   CA 4 .   ? 35.16540  19.96838  73.02446  1.000 31.13524  ?  509 HOH   K O   1 
HETATM 18569 O O   . HOH   CA 4 .   ? 36.49136  -16.15173 51.23087  1.000 56.24926  ?  510 HOH   K O   1 
HETATM 18570 O O   . HOH   CA 4 .   ? 56.44268  19.01694  54.30311  1.000 30.60683  ?  511 HOH   K O   1 
HETATM 18571 O O   . HOH   CA 4 .   ? 48.36841  11.24959  55.93995  1.000 31.10219  ?  512 HOH   K O   1 
HETATM 18572 O O   . HOH   CA 4 .   ? 52.69874  23.41804  52.32097  1.000 30.96784  ?  513 HOH   K O   1 
HETATM 18573 O O   . HOH   CA 4 .   ? 52.06689  13.33085  53.96662  1.000 30.42305  ?  514 HOH   K O   1 
HETATM 18574 O O   . HOH   CA 4 .   ? 61.09622  8.57500   64.07081  1.000 33.68249  ?  515 HOH   K O   1 
HETATM 18575 O O   . HOH   CA 4 .   ? 46.22394  27.97731  48.57070  1.000 49.10252  ?  516 HOH   K O   1 
HETATM 18576 O O   . HOH   CA 4 .   ? 50.18664  23.15936  50.68025  1.000 31.05230  ?  517 HOH   K O   1 
HETATM 18577 O O   . HOH   CA 4 .   ? 53.65060  13.82324  58.82416  1.000 24.34195  ?  518 HOH   K O   1 
HETATM 18578 O O   . HOH   CA 4 .   ? 34.57848  -9.11441  38.19317  1.000 64.51668  ?  519 HOH   K O   1 
HETATM 18579 O O   . HOH   CA 4 .   ? 49.35732  12.85083  53.56779  1.000 15.80989  ?  520 HOH   K O   1 
HETATM 18580 O O   . HOH   CA 4 .   ? 60.87988  -6.05114  33.60864  1.000 88.83466  ?  521 HOH   K O   1 
HETATM 18581 O O   . HOH   CA 4 .   ? 47.96988  35.74918  63.66670  1.000 47.77537  ?  522 HOH   K O   1 
HETATM 18582 O O   . HOH   CA 4 .   ? 24.56400  -3.19059  47.66834  1.000 51.89948  ?  523 HOH   K O   1 
HETATM 18583 O O   . HOH   CA 4 .   ? 63.21309  25.72805  54.07126  1.000 34.31343  ?  524 HOH   K O   1 
HETATM 18584 O O   . HOH   CA 4 .   ? 50.03782  27.42304  42.50472  1.000 44.98571  ?  525 HOH   K O   1 
HETATM 18585 O O   . HOH   CA 4 .   ? 52.69104  11.63956  35.52643  1.000 40.68141  ?  526 HOH   K O   1 
HETATM 18586 O O   . HOH   CA 4 .   ? 57.87803  3.45425   64.19890  1.000 47.74425  ?  527 HOH   K O   1 
HETATM 18587 O O   . HOH   CA 4 .   ? 36.20018  24.02881  54.73252  1.000 32.81387  ?  528 HOH   K O   1 
HETATM 18588 O O   . HOH   CA 4 .   ? 45.93272  33.00809  62.66307  1.000 34.07423  ?  529 HOH   K O   1 
HETATM 18589 O O   . HOH   CA 4 .   ? 55.41877  19.24710  77.77335  1.000 41.09674  ?  530 HOH   K O   1 
HETATM 18590 O O   . HOH   CA 4 .   ? 62.69879  11.79963  66.12935  1.000 35.80227  ?  531 HOH   K O   1 
HETATM 18591 O O   . HOH   CA 4 .   ? 36.82908  22.16373  56.60865  1.000 47.39886  ?  532 HOH   K O   1 
HETATM 18592 O O   . HOH   CA 4 .   ? 46.16237  30.35821  59.78350  1.000 43.63721  ?  533 HOH   K O   1 
HETATM 18593 O O   . HOH   CA 4 .   ? 48.15718  31.44160  58.74555  1.000 34.24727  ?  534 HOH   K O   1 
HETATM 18594 O O   . HOH   DA 4 .   ? 38.44800  -1.53653  25.53088  1.000 53.44414  ?  601 HOH   L O   1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1     N N   . LEU   A  57  ? 0.74600 0.74600 0.74600 0.00000  0.00000  0.00000  57  LEU   I N   
2     C CA  . LEU   A  57  ? 0.70670 0.70670 0.70670 -0.00000 0.00000  0.00000  57  LEU   I CA  
3     C C   . LEU   A  57  ? 0.91114 0.91114 0.91114 -0.00000 0.00000  0.00000  57  LEU   I C   
4     O O   . LEU   A  57  ? 0.93639 0.93639 0.93639 0.00000  0.00000  0.00000  57  LEU   I O   
5     C CB  . LEU   A  57  ? 0.66421 0.66421 0.66421 -0.00000 0.00000  0.00000  57  LEU   I CB  
6     C CG  . LEU   A  57  ? 0.87019 0.87019 0.87019 0.00000  0.00000  0.00000  57  LEU   I CG  
7     C CD1 . LEU   A  57  ? 0.77376 0.77376 0.77376 0.00000  0.00000  0.00000  57  LEU   I CD1 
8     C CD2 . LEU   A  57  ? 0.85075 0.85075 0.85075 0.00000  0.00000  0.00000  57  LEU   I CD2 
9     N N   . MET   A  58  ? 0.88342 0.88342 0.88342 -0.00000 0.00000  0.00000  58  MET   I N   
10    C CA  . MET   A  58  ? 0.86948 0.86948 0.86948 -0.00000 0.00000  0.00000  58  MET   I CA  
11    C C   . MET   A  58  ? 0.75180 0.75180 0.75180 -0.00000 0.00000  0.00000  58  MET   I C   
12    O O   . MET   A  58  ? 1.01353 1.01353 1.01353 0.00000  0.00000  0.00000  58  MET   I O   
13    C CB  . MET   A  58  ? 0.78009 0.78009 0.78009 -0.00000 -0.00000 0.00000  58  MET   I CB  
14    C CG  . MET   A  58  ? 0.97389 0.97389 0.97389 0.00000  -0.00000 0.00000  58  MET   I CG  
15    S SD  . MET   A  58  ? 1.04817 1.04817 1.04817 0.00000  0.00000  0.00000  58  MET   I SD  
16    C CE  . MET   A  58  ? 0.75215 0.75215 0.75215 -0.00000 0.00000  0.00000  58  MET   I CE  
17    N N   . GLN   A  59  ? 0.79535 0.79535 0.79535 0.00000  0.00000  0.00000  59  GLN   I N   
18    C CA  . GLN   A  59  ? 0.65398 0.65398 0.65398 -0.00000 0.00000  0.00000  59  GLN   I CA  
19    C C   . GLN   A  59  ? 0.77721 0.77721 0.77721 0.00000  0.00000  0.00000  59  GLN   I C   
20    O O   . GLN   A  59  ? 0.70186 0.70186 0.70186 0.00000  0.00000  0.00000  59  GLN   I O   
21    C CB  . GLN   A  59  ? 0.57483 0.57483 0.57483 0.00000  0.00000  0.00000  59  GLN   I CB  
22    C CG  . GLN   A  59  ? 0.94910 0.94910 0.94910 -0.00000 0.00000  0.00000  59  GLN   I CG  
23    C CD  . GLN   A  59  ? 1.23523 1.23523 1.23523 -0.00000 0.00000  0.00000  59  GLN   I CD  
24    O OE1 . GLN   A  59  ? 1.38194 1.38194 1.38194 -0.00000 -0.00000 0.00000  59  GLN   I OE1 
25    N NE2 . GLN   A  59  ? 1.04053 1.04053 1.04053 -0.00000 0.00000  0.00000  59  GLN   I NE2 
26    N N   . PRO   A  60  ? 0.89038 0.89038 0.89038 0.00000  0.00000  0.00000  60  PRO   I N   
27    C CA  . PRO   A  60  ? 0.65886 0.65886 0.65886 0.00000  0.00000  0.00000  60  PRO   I CA  
28    C C   . PRO   A  60  ? 0.96394 0.96394 0.96394 0.00000  0.00000  0.00000  60  PRO   I C   
29    O O   . PRO   A  60  ? 0.69928 0.69928 0.69928 0.00000  0.00000  0.00000  60  PRO   I O   
30    C CB  . PRO   A  60  ? 0.66853 0.66853 0.66853 0.00000  0.00000  0.00000  60  PRO   I CB  
31    C CG  . PRO   A  60  ? 0.75705 0.75705 0.75705 -0.00000 0.00000  0.00000  60  PRO   I CG  
32    C CD  . PRO   A  60  ? 0.60860 0.60860 0.60860 0.00000  0.00000  0.00000  60  PRO   I CD  
33    N N   . ILE   A  61  ? 0.57784 0.57784 0.57784 0.00000  0.00000  0.00000  61  ILE   I N   
34    C CA  . ILE   A  61  ? 0.88603 0.88603 0.88603 -0.00000 0.00000  0.00000  61  ILE   I CA  
35    C C   . ILE   A  61  ? 0.71276 0.71276 0.71276 -0.00000 0.00000  0.00000  61  ILE   I C   
36    O O   . ILE   A  61  ? 0.76765 0.76765 0.76765 0.00000  0.00000  0.00000  61  ILE   I O   
37    C CB  . ILE   A  61  ? 0.70733 0.70733 0.70733 -0.00000 0.00000  0.00000  61  ILE   I CB  
38    C CG1 . ILE   A  61  ? 0.58767 0.58767 0.58767 0.00000  0.00000  0.00000  61  ILE   I CG1 
39    C CG2 . ILE   A  61  ? 0.56407 0.56407 0.56407 0.00000  0.00000  0.00000  61  ILE   I CG2 
40    C CD1 . ILE   A  61  ? 0.67111 0.67111 0.67111 -0.00000 0.00000  0.00000  61  ILE   I CD1 
41    N N   . GLN   A  62  ? 0.42381 0.42381 0.42381 0.00000  0.00000  0.00000  62  GLN   I N   
42    C CA  . GLN   A  62  ? 0.73107 0.73107 0.73107 -0.00000 0.00000  0.00000  62  GLN   I CA  
43    C C   . GLN   A  62  ? 1.36954 1.36954 1.36954 0.00000  0.00000  0.00000  62  GLN   I C   
44    O O   . GLN   A  62  ? 0.83345 0.83345 0.83345 0.00000  0.00000  0.00000  62  GLN   I O   
45    C CB  . GLN   A  62  ? 0.56757 0.56757 0.56757 0.00000  0.00000  0.00000  62  GLN   I CB  
46    C CG  . GLN   A  62  ? 1.29142 1.29142 1.29142 0.00000  0.00000  0.00000  62  GLN   I CG  
47    C CD  . GLN   A  62  ? 1.37439 1.37439 1.37439 0.00000  0.00000  0.00000  62  GLN   I CD  
48    O OE1 . GLN   A  62  ? 1.42197 1.42197 1.42197 0.00000  0.00000  0.00000  62  GLN   I OE1 
49    N NE2 . GLN   A  62  ? 1.53908 1.53908 1.53908 0.00000  0.00000  0.00000  62  GLN   I NE2 
50    N N   . GLU   A  63  ? 0.55897 0.55897 0.55897 -0.00000 0.00000  0.00000  63  GLU   I N   
51    C CA  . GLU   A  63  ? 0.75955 0.75955 0.75955 -0.00000 0.00000  0.00000  63  GLU   I CA  
52    C C   . GLU   A  63  ? 0.78766 0.78766 0.78766 0.00000  0.00000  0.00000  63  GLU   I C   
53    O O   . GLU   A  63  ? 0.70306 0.70306 0.70306 -0.00000 0.00000  0.00000  63  GLU   I O   
54    C CB  . GLU   A  63  ? 0.55842 0.55842 0.55842 0.00000  0.00000  0.00000  63  GLU   I CB  
55    C CG  . GLU   A  63  ? 1.03431 1.03431 1.03431 0.00000  0.00000  0.00000  63  GLU   I CG  
56    C CD  . GLU   A  63  ? 0.86704 0.86704 0.86704 0.00000  0.00000  0.00000  63  GLU   I CD  
57    O OE1 . GLU   A  63  ? 1.45545 1.45545 1.45545 0.00000  0.00000  0.00000  63  GLU   I OE1 
58    O OE2 . GLU   A  63  ? 1.80493 1.80493 1.80493 0.00000  0.00000  0.00000  63  GLU   I OE2 
59    N N   . PHE   A  64  ? 0.57204 0.57204 0.57204 -0.00000 0.00000  0.00000  64  PHE   I N   
60    C CA  . PHE   A  64  ? 0.48907 0.48907 0.48907 -0.00000 0.00000  0.00000  64  PHE   I CA  
61    C C   . PHE   A  64  ? 0.66684 0.66684 0.66684 0.00000  0.00000  0.00000  64  PHE   I C   
62    O O   . PHE   A  64  ? 0.59793 0.59793 0.59793 0.00000  0.00000  0.00000  64  PHE   I O   
63    C CB  . PHE   A  64  ? 0.52825 0.52825 0.52825 -0.00000 0.00000  0.00000  64  PHE   I CB  
64    C CG  . PHE   A  64  ? 0.59377 0.59377 0.59377 0.00000  0.00000  0.00000  64  PHE   I CG  
65    C CD1 . PHE   A  64  ? 0.69439 0.69439 0.69439 0.00000  0.00000  0.00000  64  PHE   I CD1 
66    C CD2 . PHE   A  64  ? 0.45489 0.45489 0.45489 -0.00000 0.00000  0.00000  64  PHE   I CD2 
67    C CE1 . PHE   A  64  ? 0.51698 0.51698 0.51698 0.00000  0.00000  0.00000  64  PHE   I CE1 
68    C CE2 . PHE   A  64  ? 0.43273 0.43273 0.43273 -0.00000 0.00000  0.00000  64  PHE   I CE2 
69    C CZ  . PHE   A  64  ? 0.54339 0.54339 0.54339 0.00000  0.00000  0.00000  64  PHE   I CZ  
70    N N   . LYS   A  65  ? 0.69475 0.69475 0.69475 0.00000  0.00000  0.00000  65  LYS   I N   
71    C CA  . LYS   A  65  ? 0.63062 0.63062 0.63062 0.00000  0.00000  0.00000  65  LYS   I CA  
72    C C   . LYS   A  65  ? 0.88628 0.88628 0.88628 0.00000  0.00000  0.00000  65  LYS   I C   
73    O O   . LYS   A  65  ? 0.77933 0.77933 0.77933 -0.00000 0.00000  0.00000  65  LYS   I O   
74    C CB  . LYS   A  65  ? 0.72253 0.72253 0.72253 0.00000  0.00000  0.00000  65  LYS   I CB  
75    C CG  . LYS   A  65  ? 0.73564 0.73564 0.73564 -0.00000 0.00000  0.00000  65  LYS   I CG  
76    C CD  . LYS   A  65  ? 0.86906 0.86906 0.86906 0.00000  0.00000  0.00000  65  LYS   I CD  
77    C CE  . LYS   A  65  ? 0.96725 0.96725 0.96725 0.00000  0.00000  0.00000  65  LYS   I CE  
78    N NZ  . LYS   A  65  ? 1.10739 1.10739 1.10739 -0.00000 0.00000  -0.00000 65  LYS   I NZ  
79    N N   . ALA   A  66  ? 0.76217 0.76217 0.76217 -0.00000 0.00000  0.00000  66  ALA   I N   
80    C CA  . ALA   A  66  ? 0.80313 0.80313 0.80313 -0.00000 0.00000  0.00000  66  ALA   I CA  
81    C C   . ALA   A  66  ? 0.93376 0.93376 0.93376 0.00000  0.00000  0.00000  66  ALA   I C   
82    O O   . ALA   A  66  ? 0.73648 0.73648 0.73648 0.00000  0.00000  0.00000  66  ALA   I O   
83    C CB  . ALA   A  66  ? 0.51554 0.51554 0.51554 0.00000  0.00000  0.00000  66  ALA   I CB  
84    N N   . PHE   A  67  ? 0.89328 0.89328 0.89328 -0.00000 0.00000  0.00000  67  PHE   I N   
85    C CA  . PHE   A  67  ? 0.62034 0.62034 0.62034 -0.00000 0.00000  0.00000  67  PHE   I CA  
86    C C   . PHE   A  67  ? 0.82279 0.82279 0.82279 0.00000  0.00000  0.00000  67  PHE   I C   
87    O O   . PHE   A  67  ? 0.77556 0.77556 0.77556 0.00000  0.00000  0.00000  67  PHE   I O   
88    C CB  . PHE   A  67  ? 0.63575 0.63575 0.63575 0.00000  0.00000  0.00000  67  PHE   I CB  
89    C CG  . PHE   A  67  ? 0.64809 0.64809 0.64809 0.00000  0.00000  0.00000  67  PHE   I CG  
90    C CD1 . PHE   A  67  ? 0.47566 0.47566 0.47566 -0.00000 0.00000  0.00000  67  PHE   I CD1 
91    C CD2 . PHE   A  67  ? 0.57160 0.57160 0.57160 -0.00000 0.00000  0.00000  67  PHE   I CD2 
92    C CE1 . PHE   A  67  ? 0.56606 0.56606 0.56606 -0.00000 0.00000  0.00000  67  PHE   I CE1 
93    C CE2 . PHE   A  67  ? 0.69683 0.69683 0.69683 0.00000  0.00000  0.00000  67  PHE   I CE2 
94    C CZ  . PHE   A  67  ? 0.53288 0.53288 0.53288 -0.00000 0.00000  0.00000  67  PHE   I CZ  
95    N N   . ILE   A  68  ? 0.65654 0.65654 0.65654 0.00000  0.00000  0.00000  68  ILE   I N   
96    C CA  . ILE   A  68  ? 0.68418 0.68418 0.68418 0.00000  0.00000  0.00000  68  ILE   I CA  
97    C C   . ILE   A  68  ? 0.76127 0.76127 0.76127 -0.00000 -0.00000 0.00000  68  ILE   I C   
98    O O   . ILE   A  68  ? 0.73128 0.73128 0.73128 -0.00000 0.00000  0.00000  68  ILE   I O   
99    C CB  . ILE   A  68  ? 0.55648 0.55648 0.55648 0.00000  0.00000  0.00000  68  ILE   I CB  
100   C CG1 . ILE   A  68  ? 0.64638 0.64638 0.64638 0.00000  0.00000  0.00000  68  ILE   I CG1 
101   C CG2 . ILE   A  68  ? 0.62475 0.62475 0.62475 0.00000  0.00000  0.00000  68  ILE   I CG2 
102   C CD1 . ILE   A  68  ? 0.55745 0.55745 0.55745 0.00000  0.00000  0.00000  68  ILE   I CD1 
103   N N   . GLU   A  69  ? 1.08434 1.08434 1.08434 0.00000  0.00000  0.00000  69  GLU   I N   
104   C CA  . GLU   A  69  ? 0.76218 0.76218 0.76218 -0.00000 0.00000  0.00000  69  GLU   I CA  
105   C C   . GLU   A  69  ? 0.88061 0.88061 0.88061 -0.00000 -0.00000 0.00000  69  GLU   I C   
106   O O   . GLU   A  69  ? 0.88703 0.88703 0.88703 0.00000  0.00000  0.00000  69  GLU   I O   
107   C CB  . GLU   A  69  ? 0.84248 0.84248 0.84248 0.00000  0.00000  0.00000  69  GLU   I CB  
108   C CG  . GLU   A  69  ? 0.66526 0.66526 0.66526 -0.00000 0.00000  0.00000  69  GLU   I CG  
109   C CD  . GLU   A  69  ? 1.18720 1.18720 1.18720 0.00000  0.00000  0.00000  69  GLU   I CD  
110   O OE1 . GLU   A  69  ? 0.83824 0.83824 0.83824 0.00000  0.00000  0.00000  69  GLU   I OE1 
111   O OE2 . GLU   A  69  ? 0.92445 0.92445 0.92445 -0.00000 0.00000  0.00000  69  GLU   I OE2 
112   N N   . SER   A  70  ? 0.88934 0.88934 0.88934 -0.00000 0.00000  0.00000  70  SER   I N   
113   C CA  . SER   A  70  ? 0.53195 0.53195 0.53195 -0.00000 0.00000  0.00000  70  SER   I CA  
114   C C   . SER   A  70  ? 0.89623 0.89623 0.89623 0.00000  0.00000  0.00000  70  SER   I C   
115   O O   . SER   A  70  ? 0.70287 0.70287 0.70287 0.00000  0.00000  0.00000  70  SER   I O   
116   C CB  . SER   A  70  ? 0.69152 0.69152 0.69152 -0.00000 0.00000  -0.00000 70  SER   I CB  
117   O OG  . SER   A  70  ? 0.96176 0.96176 0.96176 0.00000  0.00000  0.00000  70  SER   I OG  
118   N N   . ASP   A  71  ? 0.59668 0.59668 0.59668 0.00000  0.00000  0.00000  71  ASP   I N   
119   C CA  . ASP   A  71  ? 0.53693 0.53693 0.53693 0.00000  0.00000  0.00000  71  ASP   I CA  
120   C C   . ASP   A  71  ? 0.61633 0.61633 0.61633 0.00000  0.00000  0.00000  71  ASP   I C   
121   O O   . ASP   A  71  ? 0.61510 0.61510 0.61510 -0.00000 0.00000  0.00000  71  ASP   I O   
122   C CB  . ASP   A  71  ? 0.65301 0.65301 0.65301 0.00000  0.00000  0.00000  71  ASP   I CB  
123   C CG  . ASP   A  71  ? 1.15024 1.15024 1.15024 0.00000  0.00000  0.00000  71  ASP   I CG  
124   O OD1 . ASP   A  71  ? 0.69334 0.69334 0.69334 -0.00000 0.00000  0.00000  71  ASP   I OD1 
125   O OD2 . ASP   A  71  ? 0.86945 0.86945 0.86945 0.00000  -0.00000 0.00000  71  ASP   I OD2 
126   N N   . PRO   A  72  ? 0.71811 0.71811 0.71811 0.00000  0.00000  0.00000  72  PRO   I N   
127   C CA  . PRO   A  72  ? 0.69593 0.69593 0.69593 0.00000  0.00000  0.00000  72  PRO   I CA  
128   C C   . PRO   A  72  ? 0.58008 0.58008 0.58008 0.00000  0.00000  0.00000  72  PRO   I C   
129   O O   . PRO   A  72  ? 0.65277 0.65277 0.65277 -0.00000 0.00000  0.00000  72  PRO   I O   
130   C CB  . PRO   A  72  ? 0.52138 0.52138 0.52138 -0.00000 0.00000  0.00000  72  PRO   I CB  
131   C CG  . PRO   A  72  ? 0.59540 0.59540 0.59540 0.00000  0.00000  0.00000  72  PRO   I CG  
132   C CD  . PRO   A  72  ? 0.41752 0.41752 0.41752 0.00000  0.00000  0.00000  72  PRO   I CD  
133   N N   . VAL   A  73  ? 0.70484 0.70484 0.70484 -0.00000 0.00000  0.00000  73  VAL   I N   
134   C CA  . VAL   A  73  ? 0.84398 0.84398 0.84398 0.00000  0.00000  0.00000  73  VAL   I CA  
135   C C   . VAL   A  73  ? 0.94017 0.94017 0.94017 -0.00000 0.00000  0.00000  73  VAL   I C   
136   O O   . VAL   A  73  ? 0.57312 0.57312 0.57312 0.00000  0.00000  0.00000  73  VAL   I O   
137   C CB  . VAL   A  73  ? 0.80274 0.80274 0.80274 0.00000  -0.00000 0.00000  73  VAL   I CB  
138   C CG1 . VAL   A  73  ? 0.51209 0.51209 0.51209 0.00000  0.00000  0.00000  73  VAL   I CG1 
139   C CG2 . VAL   A  73  ? 0.48471 0.48471 0.48471 0.00000  0.00000  0.00000  73  VAL   I CG2 
140   N N   . VAL   A  74  ? 0.70775 0.70775 0.70775 0.00000  0.00000  0.00000  74  VAL   I N   
141   C CA  . VAL   A  74  ? 0.58866 0.58866 0.58866 0.00000  0.00000  0.00000  74  VAL   I CA  
142   C C   . VAL   A  74  ? 0.72586 0.72586 0.72586 -0.00000 0.00000  0.00000  74  VAL   I C   
143   O O   . VAL   A  74  ? 0.78449 0.78449 0.78449 0.00000  0.00000  0.00000  74  VAL   I O   
144   C CB  . VAL   A  74  ? 0.61560 0.61560 0.61560 -0.00000 0.00000  0.00000  74  VAL   I CB  
145   C CG1 . VAL   A  74  ? 0.39938 0.39938 0.39938 -0.00000 -0.00000 0.00000  74  VAL   I CG1 
146   C CG2 . VAL   A  74  ? 0.48596 0.48596 0.48596 -0.00000 0.00000  0.00000  74  VAL   I CG2 
147   N N   . HIS   A  75  ? 0.78480 0.78480 0.78480 -0.00000 0.00000  0.00000  75  HIS   I N   
148   C CA  . HIS   A  75  ? 0.69235 0.69235 0.69235 0.00000  0.00000  0.00000  75  HIS   I CA  
149   C C   . HIS   A  75  ? 0.55101 0.55101 0.55101 0.00000  0.00000  0.00000  75  HIS   I C   
150   O O   . HIS   A  75  ? 0.63859 0.63859 0.63859 -0.00000 0.00000  0.00000  75  HIS   I O   
151   C CB  . HIS   A  75  ? 0.58562 0.58562 0.58562 -0.00000 0.00000  0.00000  75  HIS   I CB  
152   C CG  . HIS   A  75  ? 1.00138 1.00138 1.00138 0.00000  0.00000  0.00000  75  HIS   I CG  
153   N ND1 . HIS   A  75  ? 1.12104 1.12104 1.12104 -0.00000 0.00000  0.00000  75  HIS   I ND1 
154   C CD2 . HIS   A  75  ? 1.01972 1.01972 1.01972 -0.00000 0.00000  0.00000  75  HIS   I CD2 
155   C CE1 . HIS   A  75  ? 0.96263 0.96263 0.96263 0.00000  0.00000  0.00000  75  HIS   I CE1 
156   N NE2 . HIS   A  75  ? 0.79393 0.79393 0.79393 0.00000  0.00000  0.00000  75  HIS   I NE2 
157   N N   . GLN   A  76  ? 0.75299 0.75299 0.75299 -0.00000 0.00000  0.00000  76  GLN   I N   
158   C CA  . GLN   A  76  ? 0.48290 0.48290 0.48290 0.00000  0.00000  0.00000  76  GLN   I CA  
159   C C   . GLN   A  76  ? 0.77666 0.77666 0.77666 -0.00000 0.00000  0.00000  76  GLN   I C   
160   O O   . GLN   A  76  ? 0.64072 0.64072 0.64072 0.00000  0.00000  0.00000  76  GLN   I O   
161   C CB  . GLN   A  76  ? 0.80486 0.80486 0.80486 -0.00000 0.00000  0.00000  76  GLN   I CB  
162   C CG  . GLN   A  76  ? 0.50062 0.50062 0.50062 0.00000  0.00000  0.00000  76  GLN   I CG  
163   C CD  . GLN   A  76  ? 1.23861 1.23861 1.23861 0.00000  0.00000  0.00000  76  GLN   I CD  
164   O OE1 . GLN   A  76  ? 0.72752 0.72752 0.72752 0.00000  0.00000  0.00000  76  GLN   I OE1 
165   N NE2 . GLN   A  76  ? 0.62716 0.62716 0.62716 0.00000  0.00000  0.00000  76  GLN   I NE2 
166   N N   . GLU   A  77  ? 0.65107 0.65107 0.65107 0.00000  0.00000  0.00000  77  GLU   I N   
167   C CA  . GLU   A  77  ? 0.53701 0.53701 0.53701 -0.00000 0.00000  0.00000  77  GLU   I CA  
168   C C   . GLU   A  77  ? 0.88353 0.88353 0.88353 0.00000  0.00000  0.00000  77  GLU   I C   
169   O O   . GLU   A  77  ? 0.46059 0.46059 0.46059 0.00000  0.00000  0.00000  77  GLU   I O   
170   C CB  . GLU   A  77  ? 0.53119 0.53119 0.53119 0.00000  0.00000  0.00000  77  GLU   I CB  
171   C CG  . GLU   A  77  ? 0.46908 0.46908 0.46908 0.00000  0.00000  0.00000  77  GLU   I CG  
172   C CD  . GLU   A  77  ? 0.87929 0.87929 0.87929 0.00000  0.00000  0.00000  77  GLU   I CD  
173   O OE1 . GLU   A  77  ? 0.64700 0.64700 0.64700 0.00000  0.00000  0.00000  77  GLU   I OE1 
174   O OE2 . GLU   A  77  ? 0.56794 0.56794 0.56794 0.00000  0.00000  0.00000  77  GLU   I OE2 
175   N N   . PHE   A  78  ? 0.59359 0.59359 0.59359 0.00000  0.00000  0.00000  78  PHE   I N   
176   C CA  . PHE   A  78  ? 0.86041 0.86041 0.86041 0.00000  0.00000  0.00000  78  PHE   I CA  
177   C C   . PHE   A  78  ? 0.85113 0.85113 0.85113 0.00000  0.00000  0.00000  78  PHE   I C   
178   O O   . PHE   A  78  ? 0.94816 0.94816 0.94816 0.00000  0.00000  0.00000  78  PHE   I O   
179   C CB  . PHE   A  78  ? 0.61442 0.61442 0.61442 0.00000  0.00000  0.00000  78  PHE   I CB  
180   C CG  . PHE   A  78  ? 0.84821 0.84821 0.84821 -0.00000 0.00000  0.00000  78  PHE   I CG  
181   C CD1 . PHE   A  78  ? 0.67518 0.67518 0.67518 -0.00000 0.00000  0.00000  78  PHE   I CD1 
182   C CD2 . PHE   A  78  ? 0.52891 0.52891 0.52891 -0.00000 0.00000  0.00000  78  PHE   I CD2 
183   C CE1 . PHE   A  78  ? 0.64859 0.64859 0.64859 0.00000  0.00000  0.00000  78  PHE   I CE1 
184   C CE2 . PHE   A  78  ? 0.77947 0.77947 0.77947 0.00000  0.00000  0.00000  78  PHE   I CE2 
185   C CZ  . PHE   A  78  ? 0.61998 0.61998 0.61998 0.00000  0.00000  0.00000  78  PHE   I CZ  
186   N N   . ILE   A  79  ? 0.67804 0.67804 0.67804 0.00000  0.00000  0.00000  79  ILE   I N   
187   C CA  . ILE   A  79  ? 0.59762 0.59762 0.59762 0.00000  0.00000  0.00000  79  ILE   I CA  
188   C C   . ILE   A  79  ? 0.80957 0.80957 0.80957 0.00000  0.00000  0.00000  79  ILE   I C   
189   O O   . ILE   A  79  ? 0.50984 0.50984 0.50984 -0.00000 0.00000  0.00000  79  ILE   I O   
190   C CB  . ILE   A  79  ? 0.70862 0.70862 0.70862 0.00000  0.00000  0.00000  79  ILE   I CB  
191   C CG1 . ILE   A  79  ? 0.53697 0.53697 0.53697 0.00000  0.00000  0.00000  79  ILE   I CG1 
192   C CG2 . ILE   A  79  ? 0.54714 0.54714 0.54714 0.00000  0.00000  0.00000  79  ILE   I CG2 
193   C CD1 . ILE   A  79  ? 0.50213 0.50213 0.50213 0.00000  0.00000  0.00000  79  ILE   I CD1 
194   N N   . ASP   A  80  ? 0.52186 0.52186 0.52186 -0.00000 -0.00000 0.00000  80  ASP   I N   
195   C CA  . ASP   A  80  ? 0.72577 0.72577 0.72577 0.00000  0.00000  0.00000  80  ASP   I CA  
196   C C   . ASP   A  80  ? 0.61402 0.61402 0.61402 0.00000  0.00000  0.00000  80  ASP   I C   
197   O O   . ASP   A  80  ? 0.72995 0.72995 0.72995 0.00000  0.00000  0.00000  80  ASP   I O   
198   C CB  . ASP   A  80  ? 0.64725 0.64725 0.64725 0.00000  0.00000  0.00000  80  ASP   I CB  
199   C CG  . ASP   A  80  ? 0.87891 0.87891 0.87891 0.00000  0.00000  0.00000  80  ASP   I CG  
200   O OD1 . ASP   A  80  ? 0.85593 0.85593 0.85593 0.00000  -0.00000 0.00000  80  ASP   I OD1 
201   O OD2 . ASP   A  80  ? 0.95335 0.95335 0.95335 -0.00000 0.00000  0.00000  80  ASP   I OD2 
202   N N   . MET   A  81  ? 0.68736 0.68736 0.68736 -0.00000 0.00000  0.00000  81  MET   I N   
203   C CA  . MET   A  81  ? 0.60764 0.60764 0.60764 -0.00000 0.00000  0.00000  81  MET   I CA  
204   C C   . MET   A  81  ? 0.89608 0.89608 0.89608 0.00000  0.00000  0.00000  81  MET   I C   
205   O O   . MET   A  81  ? 0.73601 0.73601 0.73601 -0.00000 0.00000  0.00000  81  MET   I O   
206   C CB  . MET   A  81  ? 0.60770 0.60770 0.60770 0.00000  0.00000  0.00000  81  MET   I CB  
207   C CG  . MET   A  81  ? 0.68955 0.68955 0.68955 0.00000  -0.00000 -0.00000 81  MET   I CG  
208   S SD  . MET   A  81  ? 0.68808 0.68808 0.68808 0.00000  0.00000  0.00000  81  MET   I SD  
209   C CE  . MET   A  81  ? 0.64525 0.64525 0.64525 0.00000  0.00000  0.00000  81  MET   I CE  
210   N N   . PHE   A  82  ? 0.63247 0.63247 0.63247 0.00000  0.00000  0.00000  82  PHE   I N   
211   C CA  . PHE   A  82  ? 0.95417 0.95417 0.95417 -0.00000 0.00000  0.00000  82  PHE   I CA  
212   C C   . PHE   A  82  ? 0.61045 0.61045 0.61045 -0.00000 0.00000  0.00000  82  PHE   I C   
213   O O   . PHE   A  82  ? 1.41319 1.41319 1.41319 -0.00000 0.00000  0.00000  82  PHE   I O   
214   C CB  . PHE   A  82  ? 0.64378 0.64378 0.64378 0.00000  0.00000  0.00000  82  PHE   I CB  
215   C CG  . PHE   A  82  ? 1.19034 1.19034 1.19034 0.00000  0.00000  0.00000  82  PHE   I CG  
216   C CD1 . PHE   A  82  ? 0.60680 0.60680 0.60680 -0.00000 -0.00000 0.00000  82  PHE   I CD1 
217   C CD2 . PHE   A  82  ? 0.63988 0.63988 0.63988 -0.00000 0.00000  0.00000  82  PHE   I CD2 
218   C CE1 . PHE   A  82  ? 0.84443 0.84443 0.84443 -0.00000 -0.00000 0.00000  82  PHE   I CE1 
219   C CE2 . PHE   A  82  ? 0.86048 0.86048 0.86048 -0.00000 0.00000  0.00000  82  PHE   I CE2 
220   C CZ  . PHE   A  82  ? 0.55277 0.55277 0.55277 -0.00000 0.00000  0.00000  82  PHE   I CZ  
221   N N   . GLU   A  83  ? 0.89114 0.89114 0.89114 0.00000  0.00000  0.00000  83  GLU   I N   
222   C CA  . GLU   A  83  ? 0.95148 0.95148 0.95148 -0.00000 0.00000  0.00000  83  GLU   I CA  
223   C C   . GLU   A  83  ? 1.05697 1.05697 1.05697 0.00000  0.00000  0.00000  83  GLU   I C   
224   O O   . GLU   A  83  ? 0.75635 0.75635 0.75635 -0.00000 0.00000  0.00000  83  GLU   I O   
225   C CB  . GLU   A  83  ? 0.63908 0.63908 0.63908 0.00000  0.00000  0.00000  83  GLU   I CB  
226   N N   . GLY   A  84  ? 1.19584 1.19584 1.19584 0.00000  0.00000  0.00000  84  GLY   I N   
227   C CA  . GLY   A  84  ? 0.74442 0.74442 0.74442 0.00000  0.00000  0.00000  84  GLY   I CA  
228   C C   . GLY   A  84  ? 1.16345 1.16345 1.16345 0.00000  0.00000  0.00000  84  GLY   I C   
229   O O   . GLY   A  84  ? 0.97496 0.97496 0.97496 0.00000  0.00000  0.00000  84  GLY   I O   
230   N N   . ILE   A  85  ? 1.28338 1.28338 1.28338 0.00000  0.00000  0.00000  85  ILE   I N   
231   C CA  . ILE   A  85  ? 1.02513 1.02513 1.02513 0.00000  0.00000  0.00000  85  ILE   I CA  
232   C C   . ILE   A  85  ? 1.15444 1.15444 1.15444 0.00000  0.00000  0.00000  85  ILE   I C   
233   O O   . ILE   A  85  ? 1.08030 1.08030 1.08030 0.00000  0.00000  0.00000  85  ILE   I O   
234   C CB  . ILE   A  85  ? 0.94175 0.94175 0.94175 0.00000  -0.00000 -0.00000 85  ILE   I CB  
235   C CG1 . ILE   A  85  ? 1.13520 1.13520 1.13520 0.00000  0.00000  0.00000  85  ILE   I CG1 
236   C CG2 . ILE   A  85  ? 0.96855 0.96855 0.96855 0.00000  0.00000  0.00000  85  ILE   I CG2 
237   C CD1 . ILE   A  85  ? 1.03269 1.03269 1.03269 0.00000  0.00000  0.00000  85  ILE   I CD1 
238   N N   . GLN   A  86  ? 1.13424 1.13424 1.13424 0.00000  0.00000  0.00000  86  GLN   I N   
239   C CA  . GLN   A  86  ? 1.53465 1.53465 1.53465 0.00000  0.00000  0.00000  86  GLN   I CA  
240   C C   . GLN   A  86  ? 0.91202 0.91202 0.91202 0.00000  0.00000  0.00000  86  GLN   I C   
241   O O   . GLN   A  86  ? 1.50344 1.50344 1.50344 0.00000  0.00000  0.00000  86  GLN   I O   
242   C CB  . GLN   A  86  ? 1.08042 1.08042 1.08042 -0.00000 0.00000  0.00000  86  GLN   I CB  
243   N N   . ASP   A  87  ? 1.36273 1.36273 1.36273 -0.00000 0.00000  0.00000  87  ASP   I N   
244   C CA  . ASP   A  87  ? 0.93557 0.93557 0.93557 0.00000  0.00000  0.00000  87  ASP   I CA  
245   C C   . ASP   A  87  ? 0.79817 0.79817 0.79817 0.00000  0.00000  0.00000  87  ASP   I C   
246   O O   . ASP   A  87  ? 1.05639 1.05639 1.05639 0.00000  0.00000  0.00000  87  ASP   I O   
247   C CB  . ASP   A  87  ? 0.83747 0.83747 0.83747 -0.00000 0.00000  0.00000  87  ASP   I CB  
248   C CG  . ASP   A  87  ? 1.75905 1.75905 1.75905 0.00000  0.00000  0.00000  87  ASP   I CG  
249   O OD1 . ASP   A  87  ? 1.50899 1.50899 1.50899 0.00000  0.00000  0.00000  87  ASP   I OD1 
250   O OD2 . ASP   A  87  ? 1.48416 1.48416 1.48416 -0.00000 0.00000  0.00000  87  ASP   I OD2 
251   N N   . SER   A  88  ? 0.85972 0.85972 0.85972 -0.00000 0.00000  0.00000  88  SER   I N   
252   C CA  . SER   A  88  ? 0.72138 0.72138 0.72138 -0.00000 0.00000  0.00000  88  SER   I CA  
253   C C   . SER   A  88  ? 1.25824 1.25824 1.25824 -0.00000 0.00000  0.00000  88  SER   I C   
254   O O   . SER   A  88  ? 0.84662 0.84662 0.84662 0.00000  0.00000  0.00000  88  SER   I O   
255   C CB  . SER   A  88  ? 0.73467 0.73467 0.73467 -0.00000 0.00000  0.00000  88  SER   I CB  
256   O OG  . SER   A  88  ? 0.93896 0.93896 0.93896 0.00000  0.00000  0.00000  88  SER   I OG  
257   N N   . PRO   A  89  ? 1.05064 1.05064 1.05064 0.00000  -0.00000 0.00000  89  PRO   I N   
258   C CA  . PRO   A  89  ? 0.75322 0.75322 0.75322 0.00000  0.00000  0.00000  89  PRO   I CA  
259   C C   . PRO   A  89  ? 1.10411 1.10411 1.10411 0.00000  0.00000  0.00000  89  PRO   I C   
260   O O   . PRO   A  89  ? 0.88371 0.88371 0.88371 -0.00000 -0.00000 0.00000  89  PRO   I O   
261   C CB  . PRO   A  89  ? 1.03652 1.03652 1.03652 -0.00000 0.00000  0.00000  89  PRO   I CB  
262   C CG  . PRO   A  89  ? 1.00700 1.00700 1.00700 0.00000  0.00000  -0.00000 89  PRO   I CG  
263   C CD  . PRO   A  89  ? 0.93857 0.93857 0.93857 0.00000  0.00000  0.00000  89  PRO   I CD  
264   N N   . ARG   A  90  ? 0.93561 0.93561 0.93561 0.00000  0.00000  0.00000  90  ARG   I N   
265   C CA  . ARG   A  90  ? 1.15090 1.15090 1.15090 -0.00000 0.00000  0.00000  90  ARG   I CA  
266   C C   . ARG   A  90  ? 1.03293 1.03293 1.03293 0.00000  0.00000  0.00000  90  ARG   I C   
267   O O   . ARG   A  90  ? 1.02770 1.02770 1.02770 0.00000  0.00000  0.00000  90  ARG   I O   
268   C CB  . ARG   A  90  ? 0.95321 0.95321 0.95321 0.00000  0.00000  0.00000  90  ARG   I CB  
269   N N   . ASN   A  91  ? 0.74235 0.74235 0.74235 0.00000  0.00000  0.00000  91  ASN   I N   
270   C CA  . ASN   A  91  ? 0.79910 0.79910 0.79910 0.00000  0.00000  0.00000  91  ASN   I CA  
271   C C   . ASN   A  91  ? 0.78170 0.78170 0.78170 -0.00000 0.00000  0.00000  91  ASN   I C   
272   O O   . ASN   A  91  ? 0.86470 0.86470 0.86470 0.00000  0.00000  0.00000  91  ASN   I O   
273   C CB  . ASN   A  91  ? 0.69779 0.69779 0.69779 0.00000  0.00000  0.00000  91  ASN   I CB  
274   C CG  . ASN   A  91  ? 0.83302 0.83302 0.83302 0.00000  0.00000  0.00000  91  ASN   I CG  
275   O OD1 . ASN   A  91  ? 0.96208 0.96208 0.96208 0.00000  0.00000  0.00000  91  ASN   I OD1 
276   N ND2 . ASN   A  91  ? 0.78269 0.78269 0.78269 0.00000  0.00000  0.00000  91  ASN   I ND2 
277   N N   . TYR   A  92  ? 0.79960 0.79960 0.79960 0.00000  0.00000  0.00000  92  TYR   I N   
278   C CA  . TYR   A  92  ? 0.72034 0.72034 0.72034 0.00000  0.00000  0.00000  92  TYR   I CA  
279   C C   . TYR   A  92  ? 0.77219 0.77219 0.77219 0.00000  -0.00000 -0.00000 92  TYR   I C   
280   O O   . TYR   A  92  ? 0.83192 0.83192 0.83192 0.00000  -0.00000 -0.00000 92  TYR   I O   
281   C CB  . TYR   A  92  ? 0.58377 0.58377 0.58377 0.00000  0.00000  0.00000  92  TYR   I CB  
282   C CG  . TYR   A  92  ? 0.65300 0.65300 0.65300 0.00000  0.00000  0.00000  92  TYR   I CG  
283   C CD1 . TYR   A  92  ? 0.63043 0.63043 0.63043 0.00000  0.00000  0.00000  92  TYR   I CD1 
284   C CD2 . TYR   A  92  ? 0.73449 0.73449 0.73449 -0.00000 -0.00000 0.00000  92  TYR   I CD2 
285   C CE1 . TYR   A  92  ? 0.87083 0.87083 0.87083 0.00000  0.00000  0.00000  92  TYR   I CE1 
286   C CE2 . TYR   A  92  ? 0.83404 0.83404 0.83404 0.00000  -0.00000 0.00000  92  TYR   I CE2 
287   C CZ  . TYR   A  92  ? 0.77759 0.77759 0.77759 -0.00000 0.00000  0.00000  92  TYR   I CZ  
288   O OH  . TYR   A  92  ? 0.98982 0.98982 0.98982 0.00000  0.00000  0.00000  92  TYR   I OH  
289   N N   . GLN   A  93  ? 0.69763 0.69763 0.69763 -0.00000 0.00000  0.00000  93  GLN   I N   
290   C CA  . GLN   A  93  ? 0.85731 0.85731 0.85731 0.00000  0.00000  0.00000  93  GLN   I CA  
291   C C   . GLN   A  93  ? 0.68061 0.68061 0.68061 0.00000  0.00000  0.00000  93  GLN   I C   
292   O O   . GLN   A  93  ? 0.74913 0.74913 0.74913 0.00000  -0.00000 0.00000  93  GLN   I O   
293   C CB  . GLN   A  93  ? 0.61507 0.61507 0.61507 0.00000  0.00000  0.00000  93  GLN   I CB  
294   C CG  . GLN   A  93  ? 0.82696 0.82696 0.82696 -0.00000 0.00000  0.00000  93  GLN   I CG  
295   C CD  . GLN   A  93  ? 2.33800 2.33800 2.33800 0.00000  0.00000  0.00000  93  GLN   I CD  
296   O OE1 . GLN   A  93  ? 0.79630 0.79630 0.79630 0.00000  0.00000  0.00000  93  GLN   I OE1 
297   N NE2 . GLN   A  93  ? 0.82441 0.82441 0.82441 0.00000  0.00000  0.00000  93  GLN   I NE2 
298   N N   . GLU   A  94  ? 0.86954 0.86954 0.86954 0.00000  0.00000  0.00000  94  GLU   I N   
299   C CA  . GLU   A  94  ? 0.51926 0.51926 0.51926 0.00000  -0.00000 0.00000  94  GLU   I CA  
300   C C   . GLU   A  94  ? 0.95627 0.95627 0.95627 0.00000  0.00000  0.00000  94  GLU   I C   
301   O O   . GLU   A  94  ? 0.91902 0.91902 0.91902 0.00000  0.00000  0.00000  94  GLU   I O   
302   C CB  . GLU   A  94  ? 0.91746 0.91746 0.91746 -0.00000 -0.00000 -0.00000 94  GLU   I CB  
303   C CG  . GLU   A  94  ? 1.19031 1.19031 1.19031 -0.00000 0.00000  -0.00000 94  GLU   I CG  
304   C CD  . GLU   A  94  ? 1.98440 1.98440 1.98440 0.00000  0.00000  0.00000  94  GLU   I CD  
305   O OE1 . GLU   A  94  ? 0.82510 0.82510 0.82510 -0.00000 0.00000  0.00000  94  GLU   I OE1 
306   O OE2 . GLU   A  94  ? 1.50531 1.50531 1.50531 0.00000  0.00000  0.00000  94  GLU   I OE2 
307   N N   . LEU   A  95  ? 0.96604 0.96604 0.96604 0.00000  -0.00000 0.00000  95  LEU   I N   
308   C CA  . LEU   A  95  ? 0.72594 0.72594 0.72594 0.00000  0.00000  0.00000  95  LEU   I CA  
309   C C   . LEU   A  95  ? 0.77823 0.77823 0.77823 0.00000  0.00000  0.00000  95  LEU   I C   
310   O O   . LEU   A  95  ? 0.72769 0.72769 0.72769 -0.00000 0.00000  0.00000  95  LEU   I O   
311   C CB  . LEU   A  95  ? 0.81598 0.81598 0.81598 0.00000  0.00000  0.00000  95  LEU   I CB  
312   C CG  . LEU   A  95  ? 0.81683 0.81683 0.81683 0.00000  0.00000  0.00000  95  LEU   I CG  
313   C CD1 . LEU   A  95  ? 0.74450 0.74450 0.74450 -0.00000 0.00000  0.00000  95  LEU   I CD1 
314   C CD2 . LEU   A  95  ? 0.63302 0.63302 0.63302 0.00000  0.00000  0.00000  95  LEU   I CD2 
315   N N   . CYS   A  96  ? 0.63193 0.63193 0.63193 -0.00000 0.00000  0.00000  96  CYS   I N   
316   C CA  . CYS   A  96  ? 0.76857 0.76857 0.76857 -0.00000 0.00000  0.00000  96  CYS   I CA  
317   C C   . CYS   A  96  ? 0.77109 0.77109 0.77109 0.00000  0.00000  0.00000  96  CYS   I C   
318   O O   . CYS   A  96  ? 1.01603 1.01603 1.01603 -0.00000 0.00000  0.00000  96  CYS   I O   
319   C CB  . CYS   A  96  ? 0.68667 0.68667 0.68667 -0.00000 0.00000  0.00000  96  CYS   I CB  
320   S SG  . CYS   A  96  ? 0.88557 0.88557 0.88557 0.00000  0.00000  0.00000  96  CYS   I SG  
321   N N   . ASN   A  97  ? 0.83914 0.83914 0.83914 -0.00000 0.00000  0.00000  97  ASN   I N   
322   C CA  . ASN   A  97  ? 0.71591 0.71591 0.71591 0.00000  0.00000  0.00000  97  ASN   I CA  
323   C C   . ASN   A  97  ? 1.03038 1.03038 1.03038 0.00000  0.00000  0.00000  97  ASN   I C   
324   O O   . ASN   A  97  ? 0.79497 0.79497 0.79497 0.00000  0.00000  -0.00000 97  ASN   I O   
325   C CB  . ASN   A  97  ? 0.86190 0.86190 0.86190 -0.00000 0.00000  0.00000  97  ASN   I CB  
326   C CG  . ASN   A  97  ? 1.36185 1.36185 1.36185 0.00000  0.00000  0.00000  97  ASN   I CG  
327   O OD1 . ASN   A  97  ? 1.01439 1.01439 1.01439 -0.00000 0.00000  0.00000  97  ASN   I OD1 
328   N ND2 . ASN   A  97  ? 0.82449 0.82449 0.82449 -0.00000 0.00000  0.00000  97  ASN   I ND2 
329   N N   . MET   A  98  ? 0.53210 0.53210 0.53210 -0.00000 0.00000  0.00000  98  MET   I N   
330   C CA  . MET   A  98  ? 0.48561 0.48561 0.48561 0.00000  0.00000  0.00000  98  MET   I CA  
331   C C   . MET   A  98  ? 0.96747 0.96747 0.96747 -0.00000 0.00000  0.00000  98  MET   I C   
332   O O   . MET   A  98  ? 0.71238 0.71238 0.71238 -0.00000 0.00000  0.00000  98  MET   I O   
333   C CB  . MET   A  98  ? 0.57246 0.57246 0.57246 0.00000  -0.00000 0.00000  98  MET   I CB  
334   C CG  . MET   A  98  ? 0.43306 0.43306 0.43306 0.00000  0.00000  0.00000  98  MET   I CG  
335   S SD  . MET   A  98  ? 0.82701 0.82701 0.82701 0.00000  0.00000  0.00000  98  MET   I SD  
336   C CE  . MET   A  98  ? 0.65854 0.65854 0.65854 -0.00000 0.00000  0.00000  98  MET   I CE  
337   N N   . PHE   A  99  ? 0.67913 0.67913 0.67913 0.00000  0.00000  0.00000  99  PHE   I N   
338   C CA  . PHE   A  99  ? 0.62883 0.62883 0.62883 -0.00000 0.00000  0.00000  99  PHE   I CA  
339   C C   . PHE   A  99  ? 0.74722 0.74722 0.74722 -0.00000 -0.00000 -0.00000 99  PHE   I C   
340   O O   . PHE   A  99  ? 0.73285 0.73285 0.73285 -0.00000 0.00000  0.00000  99  PHE   I O   
341   C CB  . PHE   A  99  ? 0.60953 0.60953 0.60953 0.00000  0.00000  0.00000  99  PHE   I CB  
342   C CG  . PHE   A  99  ? 0.71354 0.71354 0.71354 0.00000  -0.00000 0.00000  99  PHE   I CG  
343   C CD1 . PHE   A  99  ? 0.58468 0.58468 0.58468 0.00000  0.00000  0.00000  99  PHE   I CD1 
344   C CD2 . PHE   A  99  ? 0.69645 0.69645 0.69645 -0.00000 0.00000  0.00000  99  PHE   I CD2 
345   C CE1 . PHE   A  99  ? 0.78157 0.78157 0.78157 0.00000  0.00000  0.00000  99  PHE   I CE1 
346   C CE2 . PHE   A  99  ? 0.57378 0.57378 0.57378 -0.00000 0.00000  0.00000  99  PHE   I CE2 
347   C CZ  . PHE   A  99  ? 0.62576 0.62576 0.62576 0.00000  0.00000  0.00000  99  PHE   I CZ  
348   N N   . ASN   A  100 ? 0.66511 0.66511 0.66511 0.00000  0.00000  0.00000  100 ASN   I N   
349   C CA  . ASN   A  100 ? 0.71898 0.71898 0.71898 -0.00000 0.00000  0.00000  100 ASN   I CA  
350   C C   . ASN   A  100 ? 0.76691 0.76691 0.76691 0.00000  0.00000  0.00000  100 ASN   I C   
351   O O   . ASN   A  100 ? 0.85881 0.85881 0.85881 -0.00000 0.00000  0.00000  100 ASN   I O   
352   C CB  . ASN   A  100 ? 0.71249 0.71249 0.71249 0.00000  0.00000  0.00000  100 ASN   I CB  
353   C CG  . ASN   A  100 ? 0.85753 0.85753 0.85753 -0.00000 0.00000  0.00000  100 ASN   I CG  
354   O OD1 . ASN   A  100 ? 1.01770 1.01770 1.01770 -0.00000 0.00000  0.00000  100 ASN   I OD1 
355   N ND2 . ASN   A  100 ? 0.85348 0.85348 0.85348 0.00000  0.00000  0.00000  100 ASN   I ND2 
356   N N   . ASP   A  101 ? 0.68283 0.68283 0.68283 0.00000  0.00000  0.00000  101 ASP   I N   
357   C CA  . ASP   A  101 ? 0.60337 0.60337 0.60337 0.00000  0.00000  0.00000  101 ASP   I CA  
358   C C   . ASP   A  101 ? 0.89037 0.89037 0.89037 0.00000  0.00000  0.00000  101 ASP   I C   
359   O O   . ASP   A  101 ? 0.78492 0.78492 0.78492 0.00000  0.00000  0.00000  101 ASP   I O   
360   C CB  . ASP   A  101 ? 0.60432 0.60432 0.60432 -0.00000 0.00000  0.00000  101 ASP   I CB  
361   C CG  . ASP   A  101 ? 1.65249 1.65249 1.65249 -0.00000 0.00000  0.00000  101 ASP   I CG  
362   O OD1 . ASP   A  101 ? 0.83292 0.83292 0.83292 0.00000  0.00000  0.00000  101 ASP   I OD1 
363   O OD2 . ASP   A  101 ? 0.95523 0.95523 0.95523 0.00000  0.00000  0.00000  101 ASP   I OD2 
364   N N   . ILE   A  102 ? 0.77583 0.77583 0.77583 0.00000  0.00000  0.00000  102 ILE   I N   
365   C CA  . ILE   A  102 ? 0.57896 0.57896 0.57896 0.00000  0.00000  0.00000  102 ILE   I CA  
366   C C   . ILE   A  102 ? 0.90270 0.90270 0.90270 0.00000  0.00000  0.00000  102 ILE   I C   
367   O O   . ILE   A  102 ? 0.69421 0.69421 0.69421 -0.00000 0.00000  0.00000  102 ILE   I O   
368   C CB  . ILE   A  102 ? 0.61479 0.61479 0.61479 0.00000  0.00000  0.00000  102 ILE   I CB  
369   C CG1 . ILE   A  102 ? 0.42250 0.42250 0.42250 0.00000  0.00000  0.00000  102 ILE   I CG1 
370   C CG2 . ILE   A  102 ? 0.47841 0.47841 0.47841 0.00000  -0.00000 0.00000  102 ILE   I CG2 
371   C CD1 . ILE   A  102 ? 0.68955 0.68955 0.68955 0.00000  0.00000  0.00000  102 ILE   I CD1 
372   N N   . PHE   A  103 ? 0.59019 0.59019 0.59019 -0.00000 0.00000  0.00000  103 PHE   I N   
373   C CA  . PHE   A  103 ? 0.90066 0.90066 0.90066 0.00000  0.00000  0.00000  103 PHE   I CA  
374   C C   . PHE   A  103 ? 0.62056 0.62056 0.62056 0.00000  0.00000  0.00000  103 PHE   I C   
375   O O   . PHE   A  103 ? 0.72645 0.72645 0.72645 -0.00000 -0.00000 0.00000  103 PHE   I O   
376   C CB  . PHE   A  103 ? 0.48787 0.48787 0.48787 0.00000  0.00000  0.00000  103 PHE   I CB  
377   C CG  . PHE   A  103 ? 0.70645 0.70645 0.70645 -0.00000 0.00000  -0.00000 103 PHE   I CG  
378   C CD1 . PHE   A  103 ? 0.65548 0.65548 0.65548 0.00000  0.00000  0.00000  103 PHE   I CD1 
379   C CD2 . PHE   A  103 ? 0.55486 0.55486 0.55486 -0.00000 0.00000  0.00000  103 PHE   I CD2 
380   C CE1 . PHE   A  103 ? 0.81060 0.81060 0.81060 0.00000  -0.00000 0.00000  103 PHE   I CE1 
381   C CE2 . PHE   A  103 ? 0.70851 0.70851 0.70851 -0.00000 0.00000  0.00000  103 PHE   I CE2 
382   C CZ  . PHE   A  103 ? 0.69943 0.69943 0.69943 0.00000  0.00000  0.00000  103 PHE   I CZ  
383   N N   . ARG   A  104 ? 0.96170 0.96170 0.96170 0.00000  0.00000  0.00000  104 ARG   I N   
384   C CA  . ARG   A  104 ? 0.82983 0.82983 0.82983 0.00000  0.00000  0.00000  104 ARG   I CA  
385   C C   . ARG   A  104 ? 0.54990 0.54990 0.54990 0.00000  0.00000  0.00000  104 ARG   I C   
386   O O   . ARG   A  104 ? 0.90168 0.90168 0.90168 0.00000  0.00000  0.00000  104 ARG   I O   
387   C CB  . ARG   A  104 ? 0.57143 0.57143 0.57143 0.00000  0.00000  0.00000  104 ARG   I CB  
388   C CG  . ARG   A  104 ? 0.56374 0.56374 0.56374 0.00000  0.00000  0.00000  104 ARG   I CG  
389   C CD  . ARG   A  104 ? 0.81695 0.81695 0.81695 -0.00000 0.00000  0.00000  104 ARG   I CD  
390   N NE  . ARG   A  104 ? 0.88522 0.88522 0.88522 0.00000  0.00000  0.00000  104 ARG   I NE  
391   C CZ  . ARG   A  104 ? 1.23107 1.23107 1.23107 -0.00000 -0.00000 0.00000  104 ARG   I CZ  
392   N NH1 . ARG   A  104 ? 0.83465 0.83465 0.83465 0.00000  0.00000  0.00000  104 ARG   I NH1 
393   N NH2 . ARG   A  104 ? 0.71381 0.71381 0.71381 -0.00000 0.00000  0.00000  104 ARG   I NH2 
394   N N   . LYS   A  105 ? 0.61761 0.61761 0.61761 0.00000  0.00000  0.00000  105 LYS   I N   
395   C CA  . LYS   A  105 ? 0.88025 0.88025 0.88025 0.00000  0.00000  0.00000  105 LYS   I CA  
396   C C   . LYS   A  105 ? 0.65900 0.65900 0.65900 -0.00000 0.00000  0.00000  105 LYS   I C   
397   O O   . LYS   A  105 ? 0.71760 0.71760 0.71760 0.00000  0.00000  0.00000  105 LYS   I O   
398   C CB  . LYS   A  105 ? 0.75635 0.75635 0.75635 0.00000  0.00000  0.00000  105 LYS   I CB  
399   C CG  . LYS   A  105 ? 0.62900 0.62900 0.62900 -0.00000 0.00000  0.00000  105 LYS   I CG  
400   C CD  . LYS   A  105 ? 0.63489 0.63489 0.63489 -0.00000 0.00000  0.00000  105 LYS   I CD  
401   C CE  . LYS   A  105 ? 1.01747 1.01747 1.01747 -0.00000 0.00000  0.00000  105 LYS   I CE  
402   N NZ  . LYS   A  105 ? 1.18025 1.18025 1.18025 0.00000  0.00000  0.00000  105 LYS   I NZ  
403   N N   . ALA   A  106 ? 0.66037 0.66037 0.66037 0.00000  0.00000  0.00000  106 ALA   I N   
404   C CA  . ALA   A  106 ? 0.57503 0.57503 0.57503 0.00000  0.00000  0.00000  106 ALA   I CA  
405   C C   . ALA   A  106 ? 0.36467 0.36467 0.36467 -0.00000 0.00000  0.00000  106 ALA   I C   
406   O O   . ALA   A  106 ? 0.60974 0.60974 0.60974 -0.00000 0.00000  0.00000  106 ALA   I O   
407   C CB  . ALA   A  106 ? 0.40161 0.40161 0.40161 0.00000  0.00000  0.00000  106 ALA   I CB  
408   N N   . PRO   A  107 ? 0.77583 0.77583 0.77583 0.00000  -0.00000 -0.00000 107 PRO   I N   
409   C CA  . PRO   A  107 ? 0.55207 0.55207 0.55207 0.00000  0.00000  0.00000  107 PRO   I CA  
410   C C   . PRO   A  107 ? 0.67724 0.67724 0.67724 0.00000  0.00000  0.00000  107 PRO   I C   
411   O O   . PRO   A  107 ? 0.61725 0.61725 0.61725 0.00000  -0.00000 0.00000  107 PRO   I O   
412   C CB  . PRO   A  107 ? 0.52745 0.52745 0.52745 0.00000  0.00000  0.00000  107 PRO   I CB  
413   C CG  . PRO   A  107 ? 0.48453 0.48453 0.48453 0.00000  0.00000  0.00000  107 PRO   I CG  
414   C CD  . PRO   A  107 ? 0.40636 0.40636 0.40636 0.00000  0.00000  0.00000  107 PRO   I CD  
415   N N   . VAL   A  108 ? 0.54489 0.54489 0.54489 0.00000  0.00000  0.00000  108 VAL   I N   
416   C CA  . VAL   A  108 ? 0.49253 0.49253 0.49253 -0.00000 0.00000  0.00000  108 VAL   I CA  
417   C C   . VAL   A  108 ? 0.63478 0.63478 0.63478 0.00000  0.00000  0.00000  108 VAL   I C   
418   O O   . VAL   A  108 ? 0.64257 0.64257 0.64257 0.00000  0.00000  0.00000  108 VAL   I O   
419   C CB  . VAL   A  108 ? 0.62216 0.62216 0.62216 0.00000  0.00000  0.00000  108 VAL   I CB  
420   C CG1 . VAL   A  108 ? 0.38181 0.38181 0.38181 -0.00000 0.00000  0.00000  108 VAL   I CG1 
421   C CG2 . VAL   A  108 ? 0.37859 0.37859 0.37859 0.00000  0.00000  0.00000  108 VAL   I CG2 
422   N N   . TYR   A  109 ? 0.43770 0.43770 0.43770 0.00000  0.00000  0.00000  109 TYR   I N   
423   C CA  . TYR   A  109 ? 0.81073 0.81073 0.81073 0.00000  0.00000  0.00000  109 TYR   I CA  
424   C C   . TYR   A  109 ? 0.43411 0.43411 0.43411 0.00000  0.00000  0.00000  109 TYR   I C   
425   O O   . TYR   A  109 ? 0.61047 0.61047 0.61047 0.00000  0.00000  0.00000  109 TYR   I O   
426   C CB  . TYR   A  109 ? 0.36007 0.36007 0.36007 0.00000  0.00000  0.00000  109 TYR   I CB  
427   C CG  . TYR   A  109 ? 0.77555 0.77555 0.77555 0.00000  0.00000  0.00000  109 TYR   I CG  
428   C CD1 . TYR   A  109 ? 0.37649 0.37649 0.37649 -0.00000 0.00000  0.00000  109 TYR   I CD1 
429   C CD2 . TYR   A  109 ? 0.42688 0.42688 0.42688 0.00000  0.00000  0.00000  109 TYR   I CD2 
430   C CE1 . TYR   A  109 ? 0.90427 0.90427 0.90427 0.00000  0.00000  0.00000  109 TYR   I CE1 
431   C CE2 . TYR   A  109 ? 0.69464 0.69464 0.69464 0.00000  0.00000  0.00000  109 TYR   I CE2 
432   C CZ  . TYR   A  109 ? 0.39342 0.39342 0.39342 0.00000  0.00000  0.00000  109 TYR   I CZ  
433   O OH  . TYR   A  109 ? 0.72613 0.72613 0.72613 0.00000  0.00000  0.00000  109 TYR   I OH  
434   N N   . GLY   A  110 ? 0.77287 0.77287 0.77287 -0.00000 0.00000  0.00000  110 GLY   I N   
435   C CA  . GLY   A  110 ? 0.32958 0.32958 0.32958 0.00000  0.00000  0.00000  110 GLY   I CA  
436   C C   . GLY   A  110 ? 0.75635 0.75635 0.75635 0.00000  0.00000  0.00000  110 GLY   I C   
437   O O   . GLY   A  110 ? 0.68039 0.68039 0.68039 0.00000  0.00000  0.00000  110 GLY   I O   
438   N N   . ASP   A  111 ? 0.76401 0.76401 0.76401 -0.00000 0.00000  0.00000  111 ASP   I N   
439   C CA  . ASP   A  111 ? 0.64469 0.64469 0.64469 0.00000  0.00000  0.00000  111 ASP   I CA  
440   C C   . ASP   A  111 ? 0.44264 0.44264 0.44264 -0.00000 0.00000  0.00000  111 ASP   I C   
441   O O   . ASP   A  111 ? 0.61149 0.61149 0.61149 0.00000  0.00000  0.00000  111 ASP   I O   
442   C CB  . ASP   A  111 ? 0.80594 0.80594 0.80594 0.00000  0.00000  0.00000  111 ASP   I CB  
443   C CG  . ASP   A  111 ? 0.78962 0.78962 0.78962 0.00000  0.00000  0.00000  111 ASP   I CG  
444   O OD1 . ASP   A  111 ? 0.98995 0.98995 0.98995 -0.00000 0.00000  0.00000  111 ASP   I OD1 
445   O OD2 . ASP   A  111 ? 1.22892 1.22892 1.22892 0.00000  -0.00000 0.00000  111 ASP   I OD2 
446   N N   . LEU   A  112 ? 1.36024 1.36024 1.36024 0.00000  0.00000  0.00000  112 LEU   I N   
447   C CA  . LEU   A  112 ? 0.21902 0.21902 0.21902 0.00000  0.00000  0.00000  112 LEU   I CA  
448   C C   . LEU   A  112 ? 0.75276 0.75276 0.75276 0.00000  0.00000  0.00000  112 LEU   I C   
449   O O   . LEU   A  112 ? 0.64977 0.64977 0.64977 -0.00000 0.00000  0.00000  112 LEU   I O   
450   C CB  . LEU   A  112 ? 0.75320 0.75320 0.75320 0.00000  -0.00000 0.00000  112 LEU   I CB  
451   C CG  . LEU   A  112 ? 1.07803 1.07803 1.07803 0.00000  0.00000  0.00000  112 LEU   I CG  
452   C CD1 . LEU   A  112 ? 1.19711 1.19711 1.19711 0.00000  0.00000  0.00000  112 LEU   I CD1 
453   C CD2 . LEU   A  112 ? 1.56640 1.56640 1.56640 0.00000  0.00000  0.00000  112 LEU   I CD2 
454   N N   . GLY   A  113 ? 0.50686 0.50686 0.50686 -0.00000 0.00000  0.00000  113 GLY   I N   
455   C CA  . GLY   A  113 ? 0.48760 0.48760 0.48760 -0.00000 0.00000  0.00000  113 GLY   I CA  
456   C C   . GLY   A  113 ? 0.53306 0.53306 0.53306 0.00000  0.00000  0.00000  113 GLY   I C   
457   O O   . GLY   A  113 ? 0.51329 0.51329 0.51329 0.00000  0.00000  0.00000  113 GLY   I O   
458   N N   . PRO   A  114 ? 0.49421 0.49421 0.49421 -0.00000 0.00000  0.00000  114 PRO   I N   
459   C CA  . PRO   A  114 ? 0.40959 0.40959 0.40959 -0.00000 0.00000  0.00000  114 PRO   I CA  
460   C C   . PRO   A  114 ? 0.44708 0.44708 0.44708 -0.00000 0.00000  0.00000  114 PRO   I C   
461   O O   . PRO   A  114 ? 0.50367 0.50367 0.50367 0.00000  0.00000  0.00000  114 PRO   I O   
462   C CB  . PRO   A  114 ? 0.47305 0.47305 0.47305 0.00000  0.00000  0.00000  114 PRO   I CB  
463   C CG  . PRO   A  114 ? 0.43450 0.43450 0.43450 -0.00000 0.00000  0.00000  114 PRO   I CG  
464   C CD  . PRO   A  114 ? 0.44824 0.44824 0.44824 -0.00000 0.00000  0.00000  114 PRO   I CD  
465   N N   . PRO   A  115 ? 0.49465 0.49465 0.49465 -0.00000 0.00000  0.00000  115 PRO   I N   
466   C CA  . PRO   A  115 ? 0.63378 0.63378 0.63378 0.00000  0.00000  0.00000  115 PRO   I CA  
467   C C   . PRO   A  115 ? 0.53371 0.53371 0.53371 -0.00000 0.00000  0.00000  115 PRO   I C   
468   O O   . PRO   A  115 ? 0.59821 0.59821 0.59821 -0.00000 0.00000  0.00000  115 PRO   I O   
469   C CB  . PRO   A  115 ? 0.40293 0.40293 0.40293 -0.00000 0.00000  0.00000  115 PRO   I CB  
470   C CG  . PRO   A  115 ? 0.43533 0.43533 0.43533 0.00000  -0.00000 0.00000  115 PRO   I CG  
471   C CD  . PRO   A  115 ? 0.56157 0.56157 0.56157 0.00000  0.00000  0.00000  115 PRO   I CD  
472   N N   . VAL   A  116 ? 0.54446 0.54446 0.54446 0.00000  -0.00000 0.00000  116 VAL   I N   
473   C CA  . VAL   A  116 ? 0.42112 0.42112 0.42112 -0.00000 0.00000  0.00000  116 VAL   I CA  
474   C C   . VAL   A  116 ? 0.45254 0.45254 0.45254 -0.00000 0.00000  0.00000  116 VAL   I C   
475   O O   . VAL   A  116 ? 0.49780 0.49780 0.49780 0.00000  0.00000  0.00000  116 VAL   I O   
476   C CB  . VAL   A  116 ? 0.51193 0.51193 0.51193 0.00000  0.00000  0.00000  116 VAL   I CB  
477   C CG1 . VAL   A  116 ? 0.41155 0.41155 0.41155 0.00000  0.00000  0.00000  116 VAL   I CG1 
478   C CG2 . VAL   A  116 ? 0.30972 0.30972 0.30972 0.00000  0.00000  0.00000  116 VAL   I CG2 
479   N N   . TYR   A  117 ? 0.48754 0.48754 0.48754 -0.00000 0.00000  0.00000  117 TYR   I N   
480   C CA  . TYR   A  117 ? 0.65894 0.65894 0.65894 0.00000  0.00000  0.00000  117 TYR   I CA  
481   C C   . TYR   A  117 ? 0.58321 0.58321 0.58321 -0.00000 0.00000  0.00000  117 TYR   I C   
482   O O   . TYR   A  117 ? 0.64668 0.64668 0.64668 0.00000  0.00000  0.00000  117 TYR   I O   
483   C CB  . TYR   A  117 ? 0.47637 0.47637 0.47637 -0.00000 0.00000  0.00000  117 TYR   I CB  
484   C CG  . TYR   A  117 ? 0.56845 0.56845 0.56845 -0.00000 0.00000  0.00000  117 TYR   I CG  
485   C CD1 . TYR   A  117 ? 0.52069 0.52069 0.52069 0.00000  0.00000  0.00000  117 TYR   I CD1 
486   C CD2 . TYR   A  117 ? 0.73232 0.73232 0.73232 0.00000  0.00000  0.00000  117 TYR   I CD2 
487   C CE1 . TYR   A  117 ? 0.52616 0.52616 0.52616 -0.00000 0.00000  0.00000  117 TYR   I CE1 
488   C CE2 . TYR   A  117 ? 0.44628 0.44628 0.44628 0.00000  0.00000  0.00000  117 TYR   I CE2 
489   C CZ  . TYR   A  117 ? 0.65434 0.65434 0.65434 0.00000  0.00000  0.00000  117 TYR   I CZ  
490   O OH  . TYR   A  117 ? 0.52444 0.52444 0.52444 -0.00000 0.00000  0.00000  117 TYR   I OH  
491   N N   . MET   A  118 ? 0.60662 0.60662 0.60662 -0.00000 0.00000  0.00000  118 MET   I N   
492   C CA  . MET   A  118 ? 0.47784 0.47784 0.47784 0.00000  0.00000  0.00000  118 MET   I CA  
493   C C   . MET   A  118 ? 0.67567 0.67567 0.67567 0.00000  0.00000  0.00000  118 MET   I C   
494   O O   . MET   A  118 ? 0.57647 0.57647 0.57647 0.00000  0.00000  0.00000  118 MET   I O   
495   C CB  . MET   A  118 ? 0.51671 0.51671 0.51671 0.00000  0.00000  0.00000  118 MET   I CB  
496   C CG  . MET   A  118 ? 0.38589 0.38589 0.38589 0.00000  0.00000  0.00000  118 MET   I CG  
497   S SD  . MET   A  118 ? 0.61659 0.61659 0.61659 -0.00000 0.00000  0.00000  118 MET   I SD  
498   C CE  . MET   A  118 ? 0.67449 0.67449 0.67449 0.00000  0.00000  0.00000  118 MET   I CE  
499   N N   . ILE   A  119 ? 0.43506 0.43506 0.43506 -0.00000 0.00000  0.00000  119 ILE   I N   
500   C CA  . ILE   A  119 ? 0.58045 0.58045 0.58045 0.00000  0.00000  0.00000  119 ILE   I CA  
501   C C   . ILE   A  119 ? 0.58596 0.58596 0.58596 0.00000  0.00000  0.00000  119 ILE   I C   
502   O O   . ILE   A  119 ? 0.64500 0.64500 0.64500 0.00000  0.00000  0.00000  119 ILE   I O   
503   C CB  . ILE   A  119 ? 0.47877 0.47877 0.47877 0.00000  0.00000  -0.00000 119 ILE   I CB  
504   C CG1 . ILE   A  119 ? 0.50777 0.50777 0.50777 0.00000  0.00000  0.00000  119 ILE   I CG1 
505   C CG2 . ILE   A  119 ? 0.57388 0.57388 0.57388 0.00000  0.00000  0.00000  119 ILE   I CG2 
506   C CD1 . ILE   A  119 ? 0.56955 0.56955 0.56955 0.00000  0.00000  0.00000  119 ILE   I CD1 
507   N N   . MET   A  120 ? 0.52741 0.52741 0.52741 -0.00000 0.00000  0.00000  120 MET   I N   
508   C CA  . MET   A  120 ? 0.50206 0.50206 0.50206 0.00000  0.00000  0.00000  120 MET   I CA  
509   C C   . MET   A  120 ? 0.57591 0.57591 0.57591 -0.00000 0.00000  0.00000  120 MET   I C   
510   O O   . MET   A  120 ? 0.57090 0.57090 0.57090 -0.00000 0.00000  0.00000  120 MET   I O   
511   C CB  . MET   A  120 ? 0.34533 0.34533 0.34533 0.00000  0.00000  0.00000  120 MET   I CB  
512   C CG  . MET   A  120 ? 0.44527 0.44527 0.44527 0.00000  0.00000  0.00000  120 MET   I CG  
513   S SD  . MET   A  120 ? 0.64942 0.64942 0.64942 0.00000  0.00000  0.00000  120 MET   I SD  
514   C CE  . MET   A  120 ? 0.45489 0.45489 0.45489 0.00000  0.00000  0.00000  120 MET   I CE  
515   N N   . ALA   A  121 ? 0.43206 0.43206 0.43206 0.00000  -0.00000 0.00000  121 ALA   I N   
516   C CA  . ALA   A  121 ? 0.50533 0.50533 0.50533 0.00000  0.00000  0.00000  121 ALA   I CA  
517   C C   . ALA   A  121 ? 0.51009 0.51009 0.51009 -0.00000 0.00000  0.00000  121 ALA   I C   
518   O O   . ALA   A  121 ? 0.59841 0.59841 0.59841 0.00000  0.00000  0.00000  121 ALA   I O   
519   C CB  . ALA   A  121 ? 0.40294 0.40294 0.40294 0.00000  0.00000  0.00000  121 ALA   I CB  
520   N N   . LYS   A  122 ? 0.60773 0.60773 0.60773 0.00000  0.00000  0.00000  122 LYS   I N   
521   C CA  . LYS   A  122 ? 0.51321 0.51321 0.51321 0.00000  0.00000  0.00000  122 LYS   I CA  
522   C C   . LYS   A  122 ? 0.69337 0.69337 0.69337 0.00000  0.00000  0.00000  122 LYS   I C   
523   O O   . LYS   A  122 ? 0.61526 0.61526 0.61526 0.00000  0.00000  0.00000  122 LYS   I O   
524   C CB  . LYS   A  122 ? 0.50580 0.50580 0.50580 -0.00000 0.00000  0.00000  122 LYS   I CB  
525   N N   . LEU   A  123 ? 0.58149 0.58149 0.58149 0.00000  0.00000  0.00000  123 LEU   I N   
526   C CA  . LEU   A  123 ? 0.57516 0.57516 0.57516 0.00000  0.00000  0.00000  123 LEU   I CA  
527   C C   . LEU   A  123 ? 0.89166 0.89166 0.89166 0.00000  0.00000  0.00000  123 LEU   I C   
528   O O   . LEU   A  123 ? 0.47471 0.47471 0.47471 -0.00000 0.00000  0.00000  123 LEU   I O   
529   C CB  . LEU   A  123 ? 0.46228 0.46228 0.46228 0.00000  0.00000  0.00000  123 LEU   I CB  
530   C CG  . LEU   A  123 ? 0.57553 0.57553 0.57553 -0.00000 0.00000  0.00000  123 LEU   I CG  
531   C CD1 . LEU   A  123 ? 0.50150 0.50150 0.50150 0.00000  0.00000  0.00000  123 LEU   I CD1 
532   C CD2 . LEU   A  123 ? 0.49934 0.49934 0.49934 0.00000  0.00000  0.00000  123 LEU   I CD2 
533   N N   . MET   A  124 ? 0.55252 0.55252 0.55252 0.00000  0.00000  0.00000  124 MET   I N   
534   C CA  . MET   A  124 ? 0.69679 0.69679 0.69679 0.00000  0.00000  0.00000  124 MET   I CA  
535   C C   . MET   A  124 ? 0.60265 0.60265 0.60265 -0.00000 -0.00000 0.00000  124 MET   I C   
536   O O   . MET   A  124 ? 0.59188 0.59188 0.59188 0.00000  0.00000  0.00000  124 MET   I O   
537   C CB  . MET   A  124 ? 0.41288 0.41288 0.41288 0.00000  0.00000  0.00000  124 MET   I CB  
538   C CG  . MET   A  124 ? 0.66928 0.66928 0.66928 -0.00000 0.00000  0.00000  124 MET   I CG  
539   S SD  . MET   A  124 ? 0.69317 0.69317 0.69317 0.00000  0.00000  0.00000  124 MET   I SD  
540   C CE  . MET   A  124 ? 0.38505 0.38505 0.38505 0.00000  0.00000  0.00000  124 MET   I CE  
541   N N   . ASN   A  125 ? 0.63572 0.63572 0.63572 0.00000  0.00000  0.00000  125 ASN   I N   
542   C CA  . ASN   A  125 ? 0.55824 0.55824 0.55824 -0.00000 0.00000  0.00000  125 ASN   I CA  
543   C C   . ASN   A  125 ? 0.62946 0.62946 0.62946 -0.00000 0.00000  0.00000  125 ASN   I C   
544   O O   . ASN   A  125 ? 0.67997 0.67997 0.67997 -0.00000 0.00000  0.00000  125 ASN   I O   
545   C CB  . ASN   A  125 ? 0.53906 0.53906 0.53906 0.00000  0.00000  0.00000  125 ASN   I CB  
546   C CG  . ASN   A  125 ? 0.51539 0.51539 0.51539 0.00000  0.00000  0.00000  125 ASN   I CG  
547   O OD1 . ASN   A  125 ? 0.59345 0.59345 0.59345 0.00000  0.00000  0.00000  125 ASN   I OD1 
548   N ND2 . ASN   A  125 ? 0.73466 0.73466 0.73466 0.00000  0.00000  0.00000  125 ASN   I ND2 
549   N N   . THR   A  126 ? 0.61107 0.61107 0.61107 0.00000  0.00000  0.00000  126 THR   I N   
550   C CA  . THR   A  126 ? 0.72619 0.72619 0.72619 -0.00000 0.00000  0.00000  126 THR   I CA  
551   C C   . THR   A  126 ? 0.45858 0.45858 0.45858 0.00000  0.00000  0.00000  126 THR   I C   
552   O O   . THR   A  126 ? 0.69824 0.69824 0.69824 0.00000  0.00000  0.00000  126 THR   I O   
553   C CB  . THR   A  126 ? 0.53305 0.53305 0.53305 0.00000  0.00000  0.00000  126 THR   I CB  
554   O OG1 . THR   A  126 ? 0.52573 0.52573 0.52573 0.00000  0.00000  0.00000  126 THR   I OG1 
555   C CG2 . THR   A  126 ? 0.34333 0.34333 0.34333 -0.00000 0.00000  0.00000  126 THR   I CG2 
556   N N   . ARG   A  127 ? 1.47424 1.47424 1.47424 0.00000  0.00000  0.00000  127 ARG   I N   
557   C CA  . ARG   A  127 ? 0.23603 0.23603 0.23603 0.00000  0.00000  0.00000  127 ARG   I CA  
558   C C   . ARG   A  127 ? 0.33347 0.33347 0.33347 -0.00000 0.00000  0.00000  127 ARG   I C   
559   O O   . ARG   A  127 ? 0.74060 0.74060 0.74060 0.00000  0.00000  0.00000  127 ARG   I O   
560   C CB  . ARG   A  127 ? 0.24953 0.24953 0.24953 0.00000  0.00000  0.00000  127 ARG   I CB  
561   C CG  . ARG   A  127 ? 1.57370 1.57370 1.57370 0.00000  0.00000  0.00000  127 ARG   I CG  
562   C CD  . ARG   A  127 ? 0.30501 0.30501 0.30501 0.00000  0.00000  0.00000  127 ARG   I CD  
563   N NE  . ARG   A  127 ? 0.70898 0.70898 0.70898 0.00000  0.00000  0.00000  127 ARG   I NE  
564   C CZ  . ARG   A  127 ? 1.46529 1.46529 1.46529 -0.00000 0.00000  0.00000  127 ARG   I CZ  
565   N NH1 . ARG   A  127 ? 1.30100 1.30100 1.30100 -0.00000 0.00000  0.00000  127 ARG   I NH1 
566   N NH2 . ARG   A  127 ? 1.06164 1.06164 1.06164 0.00000  0.00000  0.00000  127 ARG   I NH2 
567   N N   . ALA   A  128 ? 0.38226 0.38226 0.38226 -0.00000 0.00000  0.00000  128 ALA   I N   
568   C CA  . ALA   A  128 ? 0.54655 0.54655 0.54655 0.00000  0.00000  -0.00000 128 ALA   I CA  
569   C C   . ALA   A  128 ? 0.43169 0.43169 0.43169 0.00000  0.00000  0.00000  128 ALA   I C   
570   O O   . ALA   A  128 ? 0.56898 0.56898 0.56898 -0.00000 0.00000  0.00000  128 ALA   I O   
571   C CB  . ALA   A  128 ? 0.40429 0.40429 0.40429 0.00000  0.00000  0.00000  128 ALA   I CB  
572   N N   . GLY   A  129 ? 0.73768 0.73768 0.73768 -0.00000 0.00000  0.00000  129 GLY   I N   
573   C CA  . GLY   A  129 ? 0.33251 0.33251 0.33251 -0.00000 0.00000  0.00000  129 GLY   I CA  
574   C C   . GLY   A  129 ? 0.64277 0.64277 0.64277 -0.00000 0.00000  0.00000  129 GLY   I C   
575   O O   . GLY   A  129 ? 0.51416 0.51416 0.51416 0.00000  0.00000  0.00000  129 GLY   I O   
576   N N   . PHE   A  130 ? 0.42494 0.42494 0.42494 -0.00000 0.00000  0.00000  130 PHE   I N   
577   C CA  . PHE   A  130 ? 0.42603 0.42603 0.42603 -0.00000 0.00000  0.00000  130 PHE   I CA  
578   C C   . PHE   A  130 ? 0.69113 0.69113 0.69113 0.00000  0.00000  0.00000  130 PHE   I C   
579   O O   . PHE   A  130 ? 0.57910 0.57910 0.57910 -0.00000 0.00000  0.00000  130 PHE   I O   
580   C CB  . PHE   A  130 ? 0.28155 0.28155 0.28155 -0.00000 0.00000  0.00000  130 PHE   I CB  
581   C CG  . PHE   A  130 ? 0.45183 0.45183 0.45183 0.00000  0.00000  0.00000  130 PHE   I CG  
582   C CD1 . PHE   A  130 ? 0.45178 0.45178 0.45178 -0.00000 0.00000  0.00000  130 PHE   I CD1 
583   C CD2 . PHE   A  130 ? 0.37074 0.37074 0.37074 0.00000  0.00000  0.00000  130 PHE   I CD2 
584   C CE1 . PHE   A  130 ? 0.43700 0.43700 0.43700 0.00000  0.00000  0.00000  130 PHE   I CE1 
585   C CE2 . PHE   A  130 ? 0.54583 0.54583 0.54583 0.00000  0.00000  0.00000  130 PHE   I CE2 
586   C CZ  . PHE   A  130 ? 0.37420 0.37420 0.37420 0.00000  0.00000  0.00000  130 PHE   I CZ  
587   N N   . SER   A  131 ? 0.42549 0.42549 0.42549 -0.00000 0.00000  0.00000  131 SER   I N   
588   C CA  . SER   A  131 ? 0.64933 0.64933 0.64933 -0.00000 -0.00000 0.00000  131 SER   I CA  
589   C C   . SER   A  131 ? 0.49303 0.49303 0.49303 0.00000  0.00000  0.00000  131 SER   I C   
590   O O   . SER   A  131 ? 0.63040 0.63040 0.63040 -0.00000 0.00000  0.00000  131 SER   I O   
591   C CB  . SER   A  131 ? 0.28489 0.28489 0.28489 -0.00000 0.00000  0.00000  131 SER   I CB  
592   O OG  . SER   A  131 ? 1.19510 1.19510 1.19510 -0.00000 0.00000  0.00000  131 SER   I OG  
593   N N   . ALA   A  132 ? 0.41101 0.41101 0.41101 0.00000  0.00000  0.00000  132 ALA   I N   
594   C CA  . ALA   A  132 ? 0.33834 0.33834 0.33834 0.00000  0.00000  0.00000  132 ALA   I CA  
595   C C   . ALA   A  132 ? 0.51933 0.51933 0.51933 0.00000  0.00000  0.00000  132 ALA   I C   
596   O O   . ALA   A  132 ? 0.44035 0.44035 0.44035 -0.00000 0.00000  0.00000  132 ALA   I O   
597   C CB  . ALA   A  132 ? 0.34749 0.34749 0.34749 0.00000  -0.00000 0.00000  132 ALA   I CB  
598   N N   . PHE   A  133 ? 0.38861 0.38861 0.38861 0.00000  0.00000  0.00000  133 PHE   I N   
599   C CA  . PHE   A  133 ? 0.52254 0.52254 0.52254 -0.00000 0.00000  0.00000  133 PHE   I CA  
600   C C   . PHE   A  133 ? 0.61055 0.61055 0.61055 -0.00000 0.00000  0.00000  133 PHE   I C   
601   O O   . PHE   A  133 ? 0.47772 0.47772 0.47772 -0.00000 0.00000  0.00000  133 PHE   I O   
602   C CB  . PHE   A  133 ? 0.42399 0.42399 0.42399 0.00000  0.00000  0.00000  133 PHE   I CB  
603   C CG  . PHE   A  133 ? 0.56268 0.56268 0.56268 0.00000  0.00000  0.00000  133 PHE   I CG  
604   C CD1 . PHE   A  133 ? 0.50634 0.50634 0.50634 -0.00000 0.00000  0.00000  133 PHE   I CD1 
605   C CD2 . PHE   A  133 ? 0.43938 0.43938 0.43938 0.00000  0.00000  0.00000  133 PHE   I CD2 
606   C CE1 . PHE   A  133 ? 0.40331 0.40331 0.40331 0.00000  0.00000  0.00000  133 PHE   I CE1 
607   C CE2 . PHE   A  133 ? 0.43207 0.43207 0.43207 0.00000  0.00000  0.00000  133 PHE   I CE2 
608   C CZ  . PHE   A  133 ? 0.35345 0.35345 0.35345 0.00000  0.00000  0.00000  133 PHE   I CZ  
609   N N   . THR   A  134 ? 0.36846 0.36846 0.36846 0.00000  -0.00000 0.00000  134 THR   I N   
610   C CA  . THR   A  134 ? 0.42746 0.42746 0.42746 0.00000  0.00000  0.00000  134 THR   I CA  
611   C C   . THR   A  134 ? 0.39994 0.39994 0.39994 0.00000  -0.00000 0.00000  134 THR   I C   
612   O O   . THR   A  134 ? 0.50065 0.50065 0.50065 0.00000  0.00000  0.00000  134 THR   I O   
613   C CB  . THR   A  134 ? 0.42768 0.42768 0.42768 -0.00000 0.00000  0.00000  134 THR   I CB  
614   O OG1 . THR   A  134 ? 0.49972 0.49972 0.49972 0.00000  0.00000  0.00000  134 THR   I OG1 
615   C CG2 . THR   A  134 ? 0.33896 0.33896 0.33896 0.00000  0.00000  0.00000  134 THR   I CG2 
616   N N   . ARG   A  135 ? 0.43658 0.43658 0.43658 -0.00000 0.00000  0.00000  135 ARG   I N   
617   C CA  . ARG   A  135 ? 0.43884 0.43884 0.43884 0.00000  0.00000  0.00000  135 ARG   I CA  
618   C C   . ARG   A  135 ? 0.61140 0.61140 0.61140 -0.00000 0.00000  0.00000  135 ARG   I C   
619   O O   . ARG   A  135 ? 0.44180 0.44180 0.44180 -0.00000 0.00000  0.00000  135 ARG   I O   
620   C CB  . ARG   A  135 ? 0.32255 0.32255 0.32255 0.00000  0.00000  0.00000  135 ARG   I CB  
621   C CG  . ARG   A  135 ? 0.37581 0.37581 0.37581 -0.00000 0.00000  0.00000  135 ARG   I CG  
622   C CD  . ARG   A  135 ? 0.41046 0.41046 0.41046 -0.00000 0.00000  0.00000  135 ARG   I CD  
623   N NE  . ARG   A  135 ? 0.65483 0.65483 0.65483 0.00000  0.00000  0.00000  135 ARG   I NE  
624   C CZ  . ARG   A  135 ? 0.70316 0.70316 0.70316 -0.00000 -0.00000 0.00000  135 ARG   I CZ  
625   N NH1 . ARG   A  135 ? 0.59139 0.59139 0.59139 -0.00000 0.00000  0.00000  135 ARG   I NH1 
626   N NH2 . ARG   A  135 ? 0.56517 0.56517 0.56517 -0.00000 0.00000  0.00000  135 ARG   I NH2 
627   N N   . GLN   A  136 ? 0.39285 0.39285 0.39285 -0.00000 0.00000  0.00000  136 GLN   I N   
628   C CA  . GLN   A  136 ? 0.41841 0.41841 0.41841 0.00000  0.00000  0.00000  136 GLN   I CA  
629   C C   . GLN   A  136 ? 0.38503 0.38503 0.38503 0.00000  0.00000  0.00000  136 GLN   I C   
630   O O   . GLN   A  136 ? 0.60660 0.60660 0.60660 0.00000  0.00000  0.00000  136 GLN   I O   
631   C CB  . GLN   A  136 ? 0.39375 0.39375 0.39375 0.00000  0.00000  0.00000  136 GLN   I CB  
632   C CG  . GLN   A  136 ? 0.33337 0.33337 0.33337 -0.00000 0.00000  0.00000  136 GLN   I CG  
633   C CD  . GLN   A  136 ? 0.65327 0.65327 0.65327 0.00000  0.00000  0.00000  136 GLN   I CD  
634   O OE1 . GLN   A  136 ? 0.50028 0.50028 0.50028 0.00000  0.00000  0.00000  136 GLN   I OE1 
635   N NE2 . GLN   A  136 ? 0.33974 0.33974 0.33974 -0.00000 0.00000  0.00000  136 GLN   I NE2 
636   N N   . ARG   A  137 ? 0.76799 0.76799 0.76799 0.00000  0.00000  0.00000  137 ARG   I N   
637   C CA  . ARG   A  137 ? 0.33481 0.33481 0.33481 0.00000  0.00000  0.00000  137 ARG   I CA  
638   C C   . ARG   A  137 ? 0.57619 0.57619 0.57619 0.00000  0.00000  0.00000  137 ARG   I C   
639   O O   . ARG   A  137 ? 0.44365 0.44365 0.44365 0.00000  0.00000  0.00000  137 ARG   I O   
640   C CB  . ARG   A  137 ? 0.76297 0.76297 0.76297 0.00000  0.00000  0.00000  137 ARG   I CB  
641   C CG  . ARG   A  137 ? 0.30554 0.30554 0.30554 -0.00000 -0.00000 -0.00000 137 ARG   I CG  
642   C CD  . ARG   A  137 ? 0.33003 0.33003 0.33003 0.00000  0.00000  0.00000  137 ARG   I CD  
643   N NE  . ARG   A  137 ? 0.98027 0.98027 0.98027 0.00000  0.00000  0.00000  137 ARG   I NE  
644   C CZ  . ARG   A  137 ? 0.99191 0.99191 0.99191 0.00000  0.00000  0.00000  137 ARG   I CZ  
645   N NH1 . ARG   A  137 ? 0.45390 0.45390 0.45390 0.00000  0.00000  0.00000  137 ARG   I NH1 
646   N NH2 . ARG   A  137 ? 0.36443 0.36443 0.36443 0.00000  0.00000  0.00000  137 ARG   I NH2 
647   N N   . LEU   A  138 ? 0.38946 0.38946 0.38946 0.00000  0.00000  0.00000  138 LEU   I N   
648   C CA  . LEU   A  138 ? 0.55483 0.55483 0.55483 -0.00000 0.00000  0.00000  138 LEU   I CA  
649   C C   . LEU   A  138 ? 0.67438 0.67438 0.67438 0.00000  0.00000  0.00000  138 LEU   I C   
650   O O   . LEU   A  138 ? 0.54202 0.54202 0.54202 -0.00000 0.00000  0.00000  138 LEU   I O   
651   C CB  . LEU   A  138 ? 0.47610 0.47610 0.47610 0.00000  0.00000  0.00000  138 LEU   I CB  
652   C CG  . LEU   A  138 ? 0.65189 0.65189 0.65189 0.00000  0.00000  0.00000  138 LEU   I CG  
653   C CD1 . LEU   A  138 ? 0.48064 0.48064 0.48064 0.00000  0.00000  0.00000  138 LEU   I CD1 
654   C CD2 . LEU   A  138 ? 0.44686 0.44686 0.44686 0.00000  0.00000  -0.00000 138 LEU   I CD2 
655   N N   . ASN   A  139 ? 0.43344 0.43344 0.43344 -0.00000 0.00000  0.00000  139 ASN   I N   
656   C CA  . ASN   A  139 ? 0.63865 0.63865 0.63865 0.00000  0.00000  0.00000  139 ASN   I CA  
657   C C   . ASN   A  139 ? 0.46903 0.46903 0.46903 -0.00000 0.00000  0.00000  139 ASN   I C   
658   O O   . ASN   A  139 ? 0.64510 0.64510 0.64510 0.00000  0.00000  0.00000  139 ASN   I O   
659   C CB  . ASN   A  139 ? 0.33850 0.33850 0.33850 -0.00000 0.00000  0.00000  139 ASN   I CB  
660   C CG  . ASN   A  139 ? 0.55156 0.55156 0.55156 0.00000  0.00000  0.00000  139 ASN   I CG  
661   O OD1 . ASN   A  139 ? 0.44490 0.44490 0.44490 0.00000  0.00000  -0.00000 139 ASN   I OD1 
662   N ND2 . ASN   A  139 ? 0.40464 0.40464 0.40464 0.00000  0.00000  0.00000  139 ASN   I ND2 
663   N N   . LEU   A  140 ? 0.53217 0.53217 0.53217 -0.00000 0.00000  0.00000  140 LEU   I N   
664   C CA  . LEU   A  140 ? 0.38211 0.38211 0.38211 0.00000  0.00000  0.00000  140 LEU   I CA  
665   C C   . LEU   A  140 ? 0.66429 0.66429 0.66429 0.00000  0.00000  0.00000  140 LEU   I C   
666   O O   . LEU   A  140 ? 0.39738 0.39738 0.39738 0.00000  0.00000  0.00000  140 LEU   I O   
667   C CB  . LEU   A  140 ? 0.37627 0.37627 0.37627 0.00000  0.00000  0.00000  140 LEU   I CB  
668   C CG  . LEU   A  140 ? 0.58196 0.58196 0.58196 0.00000  -0.00000 0.00000  140 LEU   I CG  
669   C CD1 . LEU   A  140 ? 0.30293 0.30293 0.30293 0.00000  0.00000  0.00000  140 LEU   I CD1 
670   C CD2 . LEU   A  140 ? 0.22510 0.22510 0.22510 0.00000  0.00000  0.00000  140 LEU   I CD2 
671   N N   . HIS   A  141 ? 0.53281 0.53281 0.53281 -0.00000 0.00000  0.00000  141 HIS   I N   
672   C CA  . HIS   A  141 ? 0.50620 0.50620 0.50620 -0.00000 0.00000  0.00000  141 HIS   I CA  
673   C C   . HIS   A  141 ? 0.52111 0.52111 0.52111 0.00000  0.00000  0.00000  141 HIS   I C   
674   O O   . HIS   A  141 ? 0.60580 0.60580 0.60580 0.00000  0.00000  0.00000  141 HIS   I O   
675   C CB  . HIS   A  141 ? 0.37924 0.37924 0.37924 0.00000  0.00000  0.00000  141 HIS   I CB  
676   C CG  . HIS   A  141 ? 0.72818 0.72818 0.72818 -0.00000 0.00000  0.00000  141 HIS   I CG  
677   N ND1 . HIS   A  141 ? 0.70079 0.70079 0.70079 -0.00000 -0.00000 0.00000  141 HIS   I ND1 
678   C CD2 . HIS   A  141 ? 0.64153 0.64153 0.64153 0.00000  0.00000  0.00000  141 HIS   I CD2 
679   C CE1 . HIS   A  141 ? 0.54276 0.54276 0.54276 0.00000  0.00000  0.00000  141 HIS   I CE1 
680   N NE2 . HIS   A  141 ? 0.71055 0.71055 0.71055 0.00000  0.00000  0.00000  141 HIS   I NE2 
681   N N   . PHE   A  142 ? 0.54175 0.54175 0.54175 0.00000  0.00000  0.00000  142 PHE   I N   
682   C CA  . PHE   A  142 ? 0.70937 0.70937 0.70937 -0.00000 0.00000  0.00000  142 PHE   I CA  
683   C C   . PHE   A  142 ? 0.54339 0.54339 0.54339 0.00000  0.00000  0.00000  142 PHE   I C   
684   O O   . PHE   A  142 ? 0.56821 0.56821 0.56821 0.00000  0.00000  0.00000  142 PHE   I O   
685   C CB  . PHE   A  142 ? 0.53163 0.53163 0.53163 0.00000  0.00000  0.00000  142 PHE   I CB  
686   C CG  . PHE   A  142 ? 0.62262 0.62262 0.62262 0.00000  -0.00000 0.00000  142 PHE   I CG  
687   C CD1 . PHE   A  142 ? 0.55717 0.55717 0.55717 -0.00000 0.00000  0.00000  142 PHE   I CD1 
688   C CD2 . PHE   A  142 ? 0.57605 0.57605 0.57605 0.00000  0.00000  0.00000  142 PHE   I CD2 
689   C CE1 . PHE   A  142 ? 0.54550 0.54550 0.54550 -0.00000 0.00000  0.00000  142 PHE   I CE1 
690   C CE2 . PHE   A  142 ? 0.59005 0.59005 0.59005 -0.00000 0.00000  0.00000  142 PHE   I CE2 
691   C CZ  . PHE   A  142 ? 0.52947 0.52947 0.52947 -0.00000 0.00000  0.00000  142 PHE   I CZ  
692   N N   . LYS   A  143 ? 0.52583 0.52583 0.52583 0.00000  0.00000  0.00000  143 LYS   I N   
693   C CA  . LYS   A  143 ? 0.47095 0.47095 0.47095 0.00000  0.00000  0.00000  143 LYS   I CA  
694   C C   . LYS   A  143 ? 0.51243 0.51243 0.51243 0.00000  0.00000  0.00000  143 LYS   I C   
695   O O   . LYS   A  143 ? 0.55501 0.55501 0.55501 -0.00000 0.00000  0.00000  143 LYS   I O   
696   C CB  . LYS   A  143 ? 0.51595 0.51595 0.51595 -0.00000 0.00000  0.00000  143 LYS   I CB  
697   C CG  . LYS   A  143 ? 0.34579 0.34579 0.34579 0.00000  0.00000  0.00000  143 LYS   I CG  
698   C CD  . LYS   A  143 ? 0.44916 0.44916 0.44916 0.00000  0.00000  0.00000  143 LYS   I CD  
699   C CE  . LYS   A  143 ? 0.53222 0.53222 0.53222 0.00000  0.00000  0.00000  143 LYS   I CE  
700   N NZ  . LYS   A  143 ? 0.59059 0.59059 0.59059 -0.00000 0.00000  0.00000  143 LYS   I NZ  
701   N N   . LYS   A  144 ? 0.71602 0.71602 0.71602 -0.00000 0.00000  0.00000  144 LYS   I N   
702   C CA  . LYS   A  144 ? 0.59905 0.59905 0.59905 -0.00000 0.00000  0.00000  144 LYS   I CA  
703   C C   . LYS   A  144 ? 0.68643 0.68643 0.68643 0.00000  0.00000  0.00000  144 LYS   I C   
704   O O   . LYS   A  144 ? 0.41557 0.41557 0.41557 0.00000  0.00000  0.00000  144 LYS   I O   
705   C CB  . LYS   A  144 ? 0.22656 0.22656 0.22656 -0.00000 0.00000  0.00000  144 LYS   I CB  
706   C CG  . LYS   A  144 ? 0.63131 0.63131 0.63131 0.00000  0.00000  0.00000  144 LYS   I CG  
707   C CD  . LYS   A  144 ? 1.07803 1.07803 1.07803 -0.00000 0.00000  0.00000  144 LYS   I CD  
708   C CE  . LYS   A  144 ? 1.03693 1.03693 1.03693 -0.00000 -0.00000 -0.00000 144 LYS   I CE  
709   N NZ  . LYS   A  144 ? 1.59559 1.59559 1.59559 0.00000  0.00000  0.00000  144 LYS   I NZ  
710   N N   . LEU   A  145 ? 0.44392 0.44392 0.44392 0.00000  0.00000  0.00000  145 LEU   I N   
711   C CA  . LEU   A  145 ? 0.37335 0.37335 0.37335 0.00000  0.00000  0.00000  145 LEU   I CA  
712   C C   . LEU   A  145 ? 0.62869 0.62869 0.62869 0.00000  0.00000  0.00000  145 LEU   I C   
713   O O   . LEU   A  145 ? 0.60624 0.60624 0.60624 -0.00000 0.00000  0.00000  145 LEU   I O   
714   C CB  . LEU   A  145 ? 0.51059 0.51059 0.51059 0.00000  0.00000  0.00000  145 LEU   I CB  
715   C CG  . LEU   A  145 ? 0.54417 0.54417 0.54417 0.00000  0.00000  0.00000  145 LEU   I CG  
716   C CD1 . LEU   A  145 ? 0.46439 0.46439 0.46439 0.00000  0.00000  0.00000  145 LEU   I CD1 
717   C CD2 . LEU   A  145 ? 0.45654 0.45654 0.45654 0.00000  0.00000  0.00000  145 LEU   I CD2 
718   N N   . PHE   A  146 ? 0.41498 0.41498 0.41498 0.00000  0.00000  0.00000  146 PHE   I N   
719   C CA  . PHE   A  146 ? 0.46506 0.46506 0.46506 -0.00000 0.00000  0.00000  146 PHE   I CA  
720   C C   . PHE   A  146 ? 0.56942 0.56942 0.56942 0.00000  0.00000  0.00000  146 PHE   I C   
721   O O   . PHE   A  146 ? 0.57840 0.57840 0.57840 -0.00000 -0.00000 0.00000  146 PHE   I O   
722   C CB  . PHE   A  146 ? 0.46796 0.46796 0.46796 0.00000  0.00000  0.00000  146 PHE   I CB  
723   C CG  . PHE   A  146 ? 0.51322 0.51322 0.51322 0.00000  0.00000  0.00000  146 PHE   I CG  
724   C CD1 . PHE   A  146 ? 0.51377 0.51377 0.51377 -0.00000 0.00000  0.00000  146 PHE   I CD1 
725   C CD2 . PHE   A  146 ? 0.42594 0.42594 0.42594 -0.00000 0.00000  0.00000  146 PHE   I CD2 
726   C CE1 . PHE   A  146 ? 0.51523 0.51523 0.51523 0.00000  0.00000  0.00000  146 PHE   I CE1 
727   C CE2 . PHE   A  146 ? 0.47132 0.47132 0.47132 -0.00000 0.00000  0.00000  146 PHE   I CE2 
728   C CZ  . PHE   A  146 ? 0.54298 0.54298 0.54298 -0.00000 -0.00000 0.00000  146 PHE   I CZ  
729   N N   . ASP   A  147 ? 0.53861 0.53861 0.53861 0.00000  0.00000  -0.00000 147 ASP   I N   
730   C CA  . ASP   A  147 ? 0.45791 0.45791 0.45791 -0.00000 0.00000  0.00000  147 ASP   I CA  
731   C C   . ASP   A  147 ? 0.57905 0.57905 0.57905 0.00000  0.00000  0.00000  147 ASP   I C   
732   O O   . ASP   A  147 ? 0.55769 0.55769 0.55769 0.00000  0.00000  0.00000  147 ASP   I O   
733   C CB  . ASP   A  147 ? 0.36224 0.36224 0.36224 -0.00000 -0.00000 0.00000  147 ASP   I CB  
734   C CG  . ASP   A  147 ? 0.78118 0.78118 0.78118 0.00000  0.00000  0.00000  147 ASP   I CG  
735   O OD1 . ASP   A  147 ? 0.68133 0.68133 0.68133 0.00000  0.00000  -0.00000 147 ASP   I OD1 
736   O OD2 . ASP   A  147 ? 0.73427 0.73427 0.73427 0.00000  0.00000  0.00000  147 ASP   I OD2 
737   N N   . THR   A  148 ? 0.48210 0.48210 0.48210 0.00000  0.00000  -0.00000 148 THR   I N   
738   C CA  . THR   A  148 ? 0.60177 0.60177 0.60177 0.00000  -0.00000 -0.00000 148 THR   I CA  
739   C C   . THR   A  148 ? 0.56258 0.56258 0.56258 -0.00000 0.00000  0.00000  148 THR   I C   
740   O O   . THR   A  148 ? 0.63877 0.63877 0.63877 -0.00000 0.00000  0.00000  148 THR   I O   
741   C CB  . THR   A  148 ? 0.53668 0.53668 0.53668 0.00000  0.00000  0.00000  148 THR   I CB  
742   O OG1 . THR   A  148 ? 0.54767 0.54767 0.54767 0.00000  0.00000  0.00000  148 THR   I OG1 
743   C CG2 . THR   A  148 ? 0.40121 0.40121 0.40121 0.00000  0.00000  0.00000  148 THR   I CG2 
744   N N   . TRP   A  149 ? 0.50862 0.50862 0.50862 -0.00000 0.00000  0.00000  149 TRP   I N   
745   C CA  . TRP   A  149 ? 0.42131 0.42131 0.42131 0.00000  0.00000  0.00000  149 TRP   I CA  
746   C C   . TRP   A  149 ? 0.72561 0.72561 0.72561 0.00000  0.00000  0.00000  149 TRP   I C   
747   O O   . TRP   A  149 ? 0.53334 0.53334 0.53334 0.00000  0.00000  0.00000  149 TRP   I O   
748   C CB  . TRP   A  149 ? 0.39054 0.39054 0.39054 0.00000  0.00000  0.00000  149 TRP   I CB  
749   C CG  . TRP   A  149 ? 0.53017 0.53017 0.53017 -0.00000 0.00000  0.00000  149 TRP   I CG  
750   C CD1 . TRP   A  149 ? 0.45826 0.45826 0.45826 -0.00000 0.00000  0.00000  149 TRP   I CD1 
751   C CD2 . TRP   A  149 ? 0.66111 0.66111 0.66111 0.00000  0.00000  0.00000  149 TRP   I CD2 
752   N NE1 . TRP   A  149 ? 0.61293 0.61293 0.61293 -0.00000 0.00000  0.00000  149 TRP   I NE1 
753   C CE2 . TRP   A  149 ? 0.43914 0.43914 0.43914 0.00000  0.00000  0.00000  149 TRP   I CE2 
754   C CE3 . TRP   A  149 ? 0.42797 0.42797 0.42797 -0.00000 0.00000  0.00000  149 TRP   I CE3 
755   C CZ2 . TRP   A  149 ? 0.55877 0.55877 0.55877 -0.00000 0.00000  0.00000  149 TRP   I CZ2 
756   C CZ3 . TRP   A  149 ? 0.46422 0.46422 0.46422 0.00000  0.00000  0.00000  149 TRP   I CZ3 
757   C CH2 . TRP   A  149 ? 0.55563 0.55563 0.55563 0.00000  0.00000  0.00000  149 TRP   I CH2 
758   N N   . GLY   A  150 ? 0.57247 0.57247 0.57247 -0.00000 0.00000  0.00000  150 GLY   I N   
759   C CA  . GLY   A  150 ? 0.43768 0.43768 0.43768 0.00000  0.00000  0.00000  150 GLY   I CA  
760   C C   . GLY   A  150 ? 0.70735 0.70735 0.70735 -0.00000 0.00000  0.00000  150 GLY   I C   
761   O O   . GLY   A  150 ? 0.86001 0.86001 0.86001 0.00000  0.00000  0.00000  150 GLY   I O   
762   N N   . LEU   A  151 ? 0.51826 0.51826 0.51826 0.00000  0.00000  0.00000  151 LEU   I N   
763   C CA  . LEU   A  151 ? 0.45136 0.45136 0.45136 0.00000  0.00000  0.00000  151 LEU   I CA  
764   C C   . LEU   A  151 ? 0.95088 0.95088 0.95088 -0.00000 0.00000  0.00000  151 LEU   I C   
765   O O   . LEU   A  151 ? 0.60965 0.60965 0.60965 -0.00000 0.00000  0.00000  151 LEU   I O   
766   C CB  . LEU   A  151 ? 0.60582 0.60582 0.60582 -0.00000 0.00000  0.00000  151 LEU   I CB  
767   C CG  . LEU   A  151 ? 0.87301 0.87301 0.87301 0.00000  0.00000  0.00000  151 LEU   I CG  
768   C CD1 . LEU   A  151 ? 0.43193 0.43193 0.43193 0.00000  0.00000  0.00000  151 LEU   I CD1 
769   C CD2 . LEU   A  151 ? 0.28657 0.28657 0.28657 0.00000  0.00000  0.00000  151 LEU   I CD2 
770   N N   . PHE   A  152 ? 0.47150 0.47150 0.47150 0.00000  0.00000  0.00000  152 PHE   I N   
771   C CA  . PHE   A  152 ? 0.63299 0.63299 0.63299 -0.00000 0.00000  0.00000  152 PHE   I CA  
772   C C   . PHE   A  152 ? 0.80059 0.80059 0.80059 0.00000  0.00000  0.00000  152 PHE   I C   
773   O O   . PHE   A  152 ? 0.70503 0.70503 0.70503 0.00000  0.00000  0.00000  152 PHE   I O   
774   C CB  . PHE   A  152 ? 0.40835 0.40835 0.40835 0.00000  0.00000  0.00000  152 PHE   I CB  
775   C CG  . PHE   A  152 ? 0.74091 0.74091 0.74091 -0.00000 0.00000  0.00000  152 PHE   I CG  
776   C CD1 . PHE   A  152 ? 0.52497 0.52497 0.52497 0.00000  0.00000  0.00000  152 PHE   I CD1 
777   C CD2 . PHE   A  152 ? 0.62461 0.62461 0.62461 -0.00000 0.00000  0.00000  152 PHE   I CD2 
778   C CE1 . PHE   A  152 ? 0.61356 0.61356 0.61356 0.00000  0.00000  0.00000  152 PHE   I CE1 
779   C CE2 . PHE   A  152 ? 0.74593 0.74593 0.74593 0.00000  0.00000  0.00000  152 PHE   I CE2 
780   C CZ  . PHE   A  152 ? 0.64143 0.64143 0.64143 0.00000  0.00000  0.00000  152 PHE   I CZ  
781   N N   . LEU   A  153 ? 0.58697 0.58697 0.58697 0.00000  0.00000  0.00000  153 LEU   I N   
782   C CA  . LEU   A  153 ? 0.61112 0.61112 0.61112 0.00000  0.00000  0.00000  153 LEU   I CA  
783   C C   . LEU   A  153 ? 0.60587 0.60587 0.60587 -0.00000 0.00000  0.00000  153 LEU   I C   
784   O O   . LEU   A  153 ? 0.66154 0.66154 0.66154 0.00000  0.00000  0.00000  153 LEU   I O   
785   C CB  . LEU   A  153 ? 0.51893 0.51893 0.51893 0.00000  -0.00000 0.00000  153 LEU   I CB  
786   C CG  . LEU   A  153 ? 0.68443 0.68443 0.68443 0.00000  0.00000  0.00000  153 LEU   I CG  
787   C CD1 . LEU   A  153 ? 0.45872 0.45872 0.45872 0.00000  0.00000  0.00000  153 LEU   I CD1 
788   C CD2 . LEU   A  153 ? 0.45892 0.45892 0.45892 -0.00000 0.00000  0.00000  153 LEU   I CD2 
789   N N   . SER   A  154 ? 0.60112 0.60112 0.60112 0.00000  0.00000  -0.00000 154 SER   I N   
790   C CA  . SER   A  154 ? 0.57263 0.57263 0.57263 0.00000  0.00000  0.00000  154 SER   I CA  
791   C C   . SER   A  154 ? 0.70032 0.70032 0.70032 -0.00000 0.00000  0.00000  154 SER   I C   
792   O O   . SER   A  154 ? 0.75404 0.75404 0.75404 0.00000  0.00000  0.00000  154 SER   I O   
793   C CB  . SER   A  154 ? 0.41048 0.41048 0.41048 -0.00000 0.00000  0.00000  154 SER   I CB  
794   O OG  . SER   A  154 ? 1.43172 1.43172 1.43172 -0.00000 0.00000  0.00000  154 SER   I OG  
795   N N   . SER   A  155 ? 0.60447 0.60447 0.60447 0.00000  0.00000  0.00000  155 SER   I N   
796   C CA  . SER   A  155 ? 0.61237 0.61237 0.61237 0.00000  0.00000  0.00000  155 SER   I CA  
797   C C   . SER   A  155 ? 1.43060 1.43060 1.43060 0.00000  0.00000  0.00000  155 SER   I C   
798   O O   . SER   A  155 ? 0.58818 0.58818 0.58818 0.00000  0.00000  -0.00000 155 SER   I O   
799   C CB  . SER   A  155 ? 0.57124 0.57124 0.57124 -0.00000 0.00000  0.00000  155 SER   I CB  
800   O OG  . SER   A  155 ? 0.69852 0.69852 0.69852 0.00000  0.00000  0.00000  155 SER   I OG  
801   N N   . LYS   A  156 ? 0.77562 0.77562 0.77562 0.00000  0.00000  0.00000  156 LYS   I N   
802   C CA  . LYS   A  156 ? 0.98862 0.98862 0.98862 -0.00000 0.00000  0.00000  156 LYS   I CA  
803   C C   . LYS   A  156 ? 0.65199 0.65199 0.65199 0.00000  0.00000  0.00000  156 LYS   I C   
804   O O   . LYS   A  156 ? 0.85266 0.85266 0.85266 0.00000  0.00000  0.00000  156 LYS   I O   
805   C CB  . LYS   A  156 ? 0.55973 0.55973 0.55973 -0.00000 -0.00000 0.00000  156 LYS   I CB  
806   N N   . ASP   A  157 ? 0.70572 0.70572 0.70572 0.00000  0.00000  0.00000  157 ASP   I N   
807   C CA  . ASP   A  157 ? 0.69270 0.69270 0.69270 -0.00000 0.00000  0.00000  157 ASP   I CA  
808   C C   . ASP   A  157 ? 0.72461 0.72461 0.72461 0.00000  0.00000  0.00000  157 ASP   I C   
809   O O   . ASP   A  157 ? 0.67250 0.67250 0.67250 -0.00000 0.00000  0.00000  157 ASP   I O   
810   C CB  . ASP   A  157 ? 0.83647 0.83647 0.83647 -0.00000 0.00000  0.00000  157 ASP   I CB  
811   C CG  . ASP   A  157 ? 0.84962 0.84962 0.84962 0.00000  0.00000  0.00000  157 ASP   I CG  
812   O OD1 . ASP   A  157 ? 0.98389 0.98389 0.98389 0.00000  0.00000  0.00000  157 ASP   I OD1 
813   O OD2 . ASP   A  157 ? 1.22076 1.22076 1.22076 0.00000  0.00000  0.00000  157 ASP   I OD2 
814   N N   . SER   A  158 ? 0.88590 0.88590 0.88590 0.00000  0.00000  0.00000  158 SER   I N   
815   C CA  . SER   A  158 ? 0.70136 0.70136 0.70136 -0.00000 0.00000  0.00000  158 SER   I CA  
816   C C   . SER   A  158 ? 0.73739 0.73739 0.73739 0.00000  0.00000  0.00000  158 SER   I C   
817   O O   . SER   A  158 ? 0.67481 0.67481 0.67481 -0.00000 0.00000  0.00000  158 SER   I O   
818   C CB  . SER   A  158 ? 0.61850 0.61850 0.61850 0.00000  0.00000  0.00000  158 SER   I CB  
819   O OG  . SER   A  158 ? 0.61164 0.61164 0.61164 0.00000  0.00000  0.00000  158 SER   I OG  
820   N N   . ARG   A  159 ? 0.63274 0.63274 0.63274 0.00000  0.00000  0.00000  159 ARG   I N   
821   C CA  . ARG   A  159 ? 0.72414 0.72414 0.72414 0.00000  -0.00000 0.00000  159 ARG   I CA  
822   C C   . ARG   A  159 ? 0.73372 0.73372 0.73372 0.00000  0.00000  0.00000  159 ARG   I C   
823   O O   . ARG   A  159 ? 0.66302 0.66302 0.66302 -0.00000 0.00000  0.00000  159 ARG   I O   
824   C CB  . ARG   A  159 ? 0.50418 0.50418 0.50418 0.00000  0.00000  0.00000  159 ARG   I CB  
825   C CG  . ARG   A  159 ? 0.95974 0.95974 0.95974 -0.00000 0.00000  0.00000  159 ARG   I CG  
826   C CD  . ARG   A  159 ? 0.75815 0.75815 0.75815 -0.00000 0.00000  0.00000  159 ARG   I CD  
827   N NE  . ARG   A  159 ? 0.93372 0.93372 0.93372 0.00000  0.00000  0.00000  159 ARG   I NE  
828   C CZ  . ARG   A  159 ? 0.82186 0.82186 0.82186 -0.00000 0.00000  0.00000  159 ARG   I CZ  
829   N NH1 . ARG   A  159 ? 0.72651 0.72651 0.72651 0.00000  0.00000  0.00000  159 ARG   I NH1 
830   N NH2 . ARG   A  159 ? 0.69131 0.69131 0.69131 0.00000  0.00000  0.00000  159 ARG   I NH2 
831   N N   . ASN   A  160 ? 0.67462 0.67462 0.67462 -0.00000 0.00000  0.00000  160 ASN   I N   
832   C CA  . ASN   A  160 ? 0.72965 0.72965 0.72965 0.00000  0.00000  0.00000  160 ASN   I CA  
833   C C   . ASN   A  160 ? 0.63375 0.63375 0.63375 0.00000  0.00000  0.00000  160 ASN   I C   
834   O O   . ASN   A  160 ? 1.01081 1.01081 1.01081 0.00000  0.00000  0.00000  160 ASN   I O   
835   C CB  . ASN   A  160 ? 0.70495 0.70495 0.70495 0.00000  0.00000  0.00000  160 ASN   I CB  
836   C CG  . ASN   A  160 ? 0.85914 0.85914 0.85914 -0.00000 0.00000  0.00000  160 ASN   I CG  
837   O OD1 . ASN   A  160 ? 1.02957 1.02957 1.02957 -0.00000 0.00000  -0.00000 160 ASN   I OD1 
838   N ND2 . ASN   A  160 ? 0.91225 0.91225 0.91225 0.00000  0.00000  0.00000  160 ASN   I ND2 
839   N N   . VAL   A  161 ? 0.75941 0.75941 0.75941 0.00000  0.00000  0.00000  161 VAL   I N   
840   C CA  . VAL   A  161 ? 0.79493 0.79493 0.79493 0.00000  -0.00000 0.00000  161 VAL   I CA  
841   C C   . VAL   A  161 ? 0.82913 0.82913 0.82913 0.00000  0.00000  0.00000  161 VAL   I C   
842   O O   . VAL   A  161 ? 0.61007 0.61007 0.61007 0.00000  0.00000  0.00000  161 VAL   I O   
843   C CB  . VAL   A  161 ? 0.71826 0.71826 0.71826 0.00000  0.00000  0.00000  161 VAL   I CB  
844   C CG1 . VAL   A  161 ? 0.57724 0.57724 0.57724 0.00000  0.00000  0.00000  161 VAL   I CG1 
845   C CG2 . VAL   A  161 ? 0.51255 0.51255 0.51255 0.00000  0.00000  0.00000  161 VAL   I CG2 
846   N N   . LEU   A  162 ? 0.59350 0.59350 0.59350 0.00000  0.00000  0.00000  162 LEU   I N   
847   C CA  . LEU   A  162 ? 0.72580 0.72580 0.72580 0.00000  0.00000  0.00000  162 LEU   I CA  
848   C C   . LEU   A  162 ? 0.96555 0.96555 0.96555 -0.00000 0.00000  0.00000  162 LEU   I C   
849   O O   . LEU   A  162 ? 0.74513 0.74513 0.74513 0.00000  -0.00000 0.00000  162 LEU   I O   
850   C CB  . LEU   A  162 ? 0.68346 0.68346 0.68346 -0.00000 0.00000  0.00000  162 LEU   I CB  
851   C CG  . LEU   A  162 ? 0.53957 0.53957 0.53957 -0.00000 0.00000  0.00000  162 LEU   I CG  
852   C CD1 . LEU   A  162 ? 0.48503 0.48503 0.48503 0.00000  0.00000  0.00000  162 LEU   I CD1 
853   C CD2 . LEU   A  162 ? 0.47038 0.47038 0.47038 0.00000  -0.00000 0.00000  162 LEU   I CD2 
854   N N   . VAL   A  163 ? 0.55172 0.55172 0.55172 -0.00000 0.00000  0.00000  163 VAL   I N   
855   C CA  . VAL   A  163 ? 0.51429 0.51429 0.51429 0.00000  0.00000  0.00000  163 VAL   I CA  
856   C C   . VAL   A  163 ? 0.77298 0.77298 0.77298 -0.00000 -0.00000 0.00000  163 VAL   I C   
857   O O   . VAL   A  163 ? 0.67904 0.67904 0.67904 -0.00000 0.00000  0.00000  163 VAL   I O   
858   C CB  . VAL   A  163 ? 0.53912 0.53912 0.53912 0.00000  0.00000  0.00000  163 VAL   I CB  
859   C CG1 . VAL   A  163 ? 0.45787 0.45787 0.45787 0.00000  0.00000  0.00000  163 VAL   I CG1 
860   C CG2 . VAL   A  163 ? 0.45190 0.45190 0.45190 0.00000  0.00000  0.00000  163 VAL   I CG2 
861   N N   . ALA   A  164 ? 0.71012 0.71012 0.71012 0.00000  -0.00000 0.00000  164 ALA   I N   
862   C CA  . ALA   A  164 ? 0.80645 0.80645 0.80645 0.00000  0.00000  0.00000  164 ALA   I CA  
863   C C   . ALA   A  164 ? 0.69247 0.69247 0.69247 0.00000  0.00000  0.00000  164 ALA   I C   
864   O O   . ALA   A  164 ? 0.66606 0.66606 0.66606 0.00000  0.00000  0.00000  164 ALA   I O   
865   C CB  . ALA   A  164 ? 0.43734 0.43734 0.43734 -0.00000 -0.00000 0.00000  164 ALA   I CB  
866   N N   . ASP   A  165 ? 0.65482 0.65482 0.65482 0.00000  0.00000  0.00000  165 ASP   I N   
867   C CA  . ASP   A  165 ? 0.63373 0.63373 0.63373 0.00000  0.00000  0.00000  165 ASP   I CA  
868   C C   . ASP   A  165 ? 0.63196 0.63196 0.63196 0.00000  0.00000  0.00000  165 ASP   I C   
869   O O   . ASP   A  165 ? 1.07552 1.07552 1.07552 0.00000  0.00000  0.00000  165 ASP   I O   
870   C CB  . ASP   A  165 ? 0.72588 0.72588 0.72588 0.00000  0.00000  0.00000  165 ASP   I CB  
871   C CG  . ASP   A  165 ? 0.57330 0.57330 0.57330 0.00000  0.00000  0.00000  165 ASP   I CG  
872   O OD1 . ASP   A  165 ? 1.15908 1.15908 1.15908 -0.00000 0.00000  0.00000  165 ASP   I OD1 
873   O OD2 . ASP   A  165 ? 1.19325 1.19325 1.19325 0.00000  0.00000  0.00000  165 ASP   I OD2 
874   N N   . GLN   A  166 ? 0.73000 0.73000 0.73000 0.00000  0.00000  0.00000  166 GLN   I N   
875   C CA  . GLN   A  166 ? 0.91324 0.91324 0.91324 -0.00000 0.00000  0.00000  166 GLN   I CA  
876   C C   . GLN   A  166 ? 0.43525 0.43525 0.43525 0.00000  0.00000  0.00000  166 GLN   I C   
877   O O   . GLN   A  166 ? 1.36742 1.36742 1.36742 0.00000  0.00000  0.00000  166 GLN   I O   
878   C CB  . GLN   A  166 ? 0.40139 0.40139 0.40139 -0.00000 0.00000  0.00000  166 GLN   I CB  
879   C CG  . GLN   A  166 ? 0.86387 0.86387 0.86387 -0.00000 0.00000  0.00000  166 GLN   I CG  
880   C CD  . GLN   A  166 ? 1.61642 1.61642 1.61642 0.00000  0.00000  0.00000  166 GLN   I CD  
881   O OE1 . GLN   A  166 ? 1.04352 1.04352 1.04352 -0.00000 0.00000  0.00000  166 GLN   I OE1 
882   N NE2 . GLN   A  166 ? 0.87132 0.87132 0.87132 0.00000  0.00000  0.00000  166 GLN   I NE2 
883   N N   . PHE   A  167 ? 0.83456 0.83456 0.83456 0.00000  0.00000  0.00000  167 PHE   I N   
884   C CA  . PHE   A  167 ? 0.82137 0.82137 0.82137 0.00000  0.00000  0.00000  167 PHE   I CA  
885   C C   . PHE   A  167 ? 0.84041 0.84041 0.84041 -0.00000 0.00000  0.00000  167 PHE   I C   
886   O O   . PHE   A  167 ? 0.78949 0.78949 0.78949 0.00000  0.00000  0.00000  167 PHE   I O   
887   C CB  . PHE   A  167 ? 0.69600 0.69600 0.69600 0.00000  0.00000  0.00000  167 PHE   I CB  
888   C CG  . PHE   A  167 ? 0.76561 0.76561 0.76561 0.00000  0.00000  0.00000  167 PHE   I CG  
889   C CD1 . PHE   A  167 ? 0.61634 0.61634 0.61634 0.00000  0.00000  0.00000  167 PHE   I CD1 
890   C CD2 . PHE   A  167 ? 0.50372 0.50372 0.50372 -0.00000 0.00000  0.00000  167 PHE   I CD2 
891   C CE1 . PHE   A  167 ? 1.51207 1.51207 1.51207 0.00000  0.00000  0.00000  167 PHE   I CE1 
892   C CE2 . PHE   A  167 ? 1.37048 1.37048 1.37048 0.00000  0.00000  0.00000  167 PHE   I CE2 
893   C CZ  . PHE   A  167 ? 0.34817 0.34817 0.34817 -0.00000 0.00000  0.00000  167 PHE   I CZ  
894   N N   . ASP   A  168 ? 0.86139 0.86139 0.86139 0.00000  0.00000  0.00000  168 ASP   I N   
895   C CA  . ASP   A  168 ? 0.42158 0.42158 0.42158 0.00000  0.00000  0.00000  168 ASP   I CA  
896   C C   . ASP   A  168 ? 1.07143 1.07143 1.07143 -0.00000 0.00000  0.00000  168 ASP   I C   
897   O O   . ASP   A  168 ? 0.73612 0.73612 0.73612 0.00000  0.00000  0.00000  168 ASP   I O   
898   C CB  . ASP   A  168 ? 0.59990 0.59990 0.59990 0.00000  0.00000  0.00000  168 ASP   I CB  
899   C CG  . ASP   A  168 ? 0.91383 0.91383 0.91383 -0.00000 0.00000  0.00000  168 ASP   I CG  
900   O OD1 . ASP   A  168 ? 0.73438 0.73438 0.73438 0.00000  0.00000  0.00000  168 ASP   I OD1 
901   O OD2 . ASP   A  168 ? 0.88541 0.88541 0.88541 -0.00000 0.00000  0.00000  168 ASP   I OD2 
902   N N   . ASP   A  169 ? 0.86405 0.86405 0.86405 -0.00000 0.00000  0.00000  169 ASP   I N   
903   C CA  . ASP   A  169 ? 0.91334 0.91334 0.91334 0.00000  0.00000  0.00000  169 ASP   I CA  
904   C C   . ASP   A  169 ? 1.12672 1.12672 1.12672 -0.00000 0.00000  0.00000  169 ASP   I C   
905   O O   . ASP   A  169 ? 0.97257 0.97257 0.97257 0.00000  0.00000  0.00000  169 ASP   I O   
906   C CB  . ASP   A  169 ? 0.64209 0.64209 0.64209 0.00000  0.00000  0.00000  169 ASP   I CB  
907   N N   . ARG   A  170 ? 1.78967 1.78967 1.78967 0.00000  0.00000  -0.00000 170 ARG   I N   
908   C CA  . ARG   A  170 ? 0.66121 0.66121 0.66121 -0.00000 0.00000  0.00000  170 ARG   I CA  
909   C C   . ARG   A  170 ? 0.89278 0.89278 0.89278 0.00000  0.00000  0.00000  170 ARG   I C   
910   O O   . ARG   A  170 ? 0.77900 0.77900 0.77900 0.00000  0.00000  0.00000  170 ARG   I O   
911   C CB  . ARG   A  170 ? 0.73534 0.73534 0.73534 0.00000  0.00000  0.00000  170 ARG   I CB  
912   N N   . HIS   A  171 ? 0.83515 0.83515 0.83515 -0.00000 0.00000  0.00000  171 HIS   I N   
913   C CA  . HIS   A  171 ? 0.87606 0.87606 0.87606 -0.00000 0.00000  0.00000  171 HIS   I CA  
914   C C   . HIS   A  171 ? 0.45245 0.45245 0.45245 0.00000  0.00000  0.00000  171 HIS   I C   
915   O O   . HIS   A  171 ? 1.35520 1.35520 1.35520 0.00000  0.00000  -0.00000 171 HIS   I O   
916   C CB  . HIS   A  171 ? 0.91114 0.91114 0.91114 0.00000  0.00000  0.00000  171 HIS   I CB  
917   C CG  . HIS   A  171 ? 0.85014 0.85014 0.85014 -0.00000 0.00000  0.00000  171 HIS   I CG  
918   N ND1 . HIS   A  171 ? 0.92186 0.92186 0.92186 0.00000  0.00000  -0.00000 171 HIS   I ND1 
919   C CD2 . HIS   A  171 ? 0.85302 0.85302 0.85302 0.00000  0.00000  -0.00000 171 HIS   I CD2 
920   C CE1 . HIS   A  171 ? 0.60212 0.60212 0.60212 -0.00000 0.00000  0.00000  171 HIS   I CE1 
921   N NE2 . HIS   A  171 ? 1.55534 1.55534 1.55534 0.00000  0.00000  0.00000  171 HIS   I NE2 
922   N N   . CYS   A  172 ? 0.93459 0.93459 0.93459 -0.00000 0.00000  0.00000  172 CYS   I N   
923   C CA  . CYS   A  172 ? 0.54610 0.54610 0.54610 0.00000  0.00000  0.00000  172 CYS   I CA  
924   C C   . CYS   A  172 ? 0.55951 0.55951 0.55951 -0.00000 0.00000  0.00000  172 CYS   I C   
925   O O   . CYS   A  172 ? 0.84991 0.84991 0.84991 0.00000  0.00000  0.00000  172 CYS   I O   
926   C CB  . CYS   A  172 ? 0.66155 0.66155 0.66155 0.00000  0.00000  0.00000  172 CYS   I CB  
927   S SG  . CYS   A  172 ? 0.76254 0.76254 0.76254 0.00000  0.00000  0.00000  172 CYS   I SG  
928   N N   . GLY   A  173 ? 0.71654 0.71654 0.71654 0.00000  0.00000  0.00000  173 GLY   I N   
929   C CA  . GLY   A  173 ? 0.52216 0.52216 0.52216 -0.00000 0.00000  0.00000  173 GLY   I CA  
930   C C   . GLY   A  173 ? 0.70667 0.70667 0.70667 0.00000  0.00000  0.00000  173 GLY   I C   
931   O O   . GLY   A  173 ? 0.70737 0.70737 0.70737 0.00000  0.00000  0.00000  173 GLY   I O   
932   N N   . TRP   A  174 ? 0.48289 0.48289 0.48289 -0.00000 0.00000  0.00000  174 TRP   I N   
933   C CA  . TRP   A  174 ? 0.80683 0.80683 0.80683 0.00000  0.00000  0.00000  174 TRP   I CA  
934   C C   . TRP   A  174 ? 0.91554 0.91554 0.91554 0.00000  0.00000  0.00000  174 TRP   I C   
935   O O   . TRP   A  174 ? 0.71519 0.71519 0.71519 0.00000  0.00000  0.00000  174 TRP   I O   
936   C CB  . TRP   A  174 ? 0.52509 0.52509 0.52509 0.00000  0.00000  0.00000  174 TRP   I CB  
937   C CG  . TRP   A  174 ? 0.90568 0.90568 0.90568 0.00000  0.00000  0.00000  174 TRP   I CG  
938   C CD1 . TRP   A  174 ? 0.62643 0.62643 0.62643 0.00000  0.00000  0.00000  174 TRP   I CD1 
939   C CD2 . TRP   A  174 ? 0.73677 0.73677 0.73677 -0.00000 0.00000  0.00000  174 TRP   I CD2 
940   N NE1 . TRP   A  174 ? 0.65785 0.65785 0.65785 0.00000  0.00000  0.00000  174 TRP   I NE1 
941   C CE2 . TRP   A  174 ? 0.55728 0.55728 0.55728 0.00000  0.00000  0.00000  174 TRP   I CE2 
942   C CE3 . TRP   A  174 ? 0.58537 0.58537 0.58537 0.00000  0.00000  0.00000  174 TRP   I CE3 
943   C CZ2 . TRP   A  174 ? 0.46117 0.46117 0.46117 0.00000  0.00000  0.00000  174 TRP   I CZ2 
944   C CZ3 . TRP   A  174 ? 0.61114 0.61114 0.61114 0.00000  0.00000  0.00000  174 TRP   I CZ3 
945   C CH2 . TRP   A  174 ? 0.49909 0.49909 0.49909 0.00000  0.00000  0.00000  174 TRP   I CH2 
946   N N   . LEU   A  175 ? 0.65545 0.65545 0.65545 0.00000  0.00000  0.00000  175 LEU   I N   
947   C CA  . LEU   A  175 ? 0.59154 0.59154 0.59154 -0.00000 0.00000  0.00000  175 LEU   I CA  
948   C C   . LEU   A  175 ? 0.71435 0.71435 0.71435 0.00000  0.00000  0.00000  175 LEU   I C   
949   O O   . LEU   A  175 ? 0.82643 0.82643 0.82643 0.00000  0.00000  0.00000  175 LEU   I O   
950   C CB  . LEU   A  175 ? 0.52817 0.52817 0.52817 0.00000  0.00000  0.00000  175 LEU   I CB  
951   C CG  . LEU   A  175 ? 0.66257 0.66257 0.66257 0.00000  0.00000  0.00000  175 LEU   I CG  
952   C CD1 . LEU   A  175 ? 0.54283 0.54283 0.54283 0.00000  0.00000  0.00000  175 LEU   I CD1 
953   C CD2 . LEU   A  175 ? 0.50414 0.50414 0.50414 -0.00000 0.00000  0.00000  175 LEU   I CD2 
954   N N   . ASN   A  176 ? 0.41278 0.41278 0.41278 0.00000  0.00000  0.00000  176 ASN   I N   
955   C CA  . ASN   A  176 ? 0.35692 0.35692 0.35692 -0.00000 0.00000  0.00000  176 ASN   I CA  
956   C C   . ASN   A  176 ? 0.56474 0.56474 0.56474 -0.00000 0.00000  0.00000  176 ASN   I C   
957   O O   . ASN   A  176 ? 0.74060 0.74060 0.74060 0.00000  0.00000  0.00000  176 ASN   I O   
958   C CB  . ASN   A  176 ? 0.69790 0.69790 0.69790 0.00000  0.00000  0.00000  176 ASN   I CB  
959   C CG  . ASN   A  176 ? 0.67651 0.67651 0.67651 0.00000  0.00000  0.00000  176 ASN   I CG  
960   O OD1 . ASN   A  176 ? 0.50156 0.50156 0.50156 0.00000  0.00000  0.00000  176 ASN   I OD1 
961   N ND2 . ASN   A  176 ? 0.51855 0.51855 0.51855 -0.00000 0.00000  0.00000  176 ASN   I ND2 
962   N N   . GLU   A  177 ? 0.65437 0.65437 0.65437 0.00000  0.00000  0.00000  177 GLU   I N   
963   C CA  . GLU   A  177 ? 0.62016 0.62016 0.62016 0.00000  0.00000  0.00000  177 GLU   I CA  
964   C C   . GLU   A  177 ? 0.54126 0.54126 0.54126 0.00000  0.00000  0.00000  177 GLU   I C   
965   O O   . GLU   A  177 ? 0.65838 0.65838 0.65838 0.00000  0.00000  0.00000  177 GLU   I O   
966   C CB  . GLU   A  177 ? 0.38905 0.38905 0.38905 0.00000  0.00000  0.00000  177 GLU   I CB  
967   N N   . ARG   A  178 ? 0.52647 0.52647 0.52647 0.00000  0.00000  0.00000  178 ARG   I N   
968   C CA  . ARG   A  178 ? 0.82490 0.82490 0.82490 0.00000  0.00000  0.00000  178 ARG   I CA  
969   C C   . ARG   A  178 ? 0.77647 0.77647 0.77647 -0.00000 0.00000  0.00000  178 ARG   I C   
970   O O   . ARG   A  178 ? 0.75696 0.75696 0.75696 0.00000  0.00000  0.00000  178 ARG   I O   
971   C CB  . ARG   A  178 ? 0.38395 0.38395 0.38395 -0.00000 0.00000  0.00000  178 ARG   I CB  
972   C CG  . ARG   A  178 ? 0.88713 0.88713 0.88713 0.00000  0.00000  0.00000  178 ARG   I CG  
973   C CD  . ARG   A  178 ? 0.82266 0.82266 0.82266 0.00000  0.00000  0.00000  178 ARG   I CD  
974   N NE  . ARG   A  178 ? 1.25012 1.25012 1.25012 0.00000  0.00000  0.00000  178 ARG   I NE  
975   C CZ  . ARG   A  178 ? 1.30582 1.30582 1.30582 0.00000  0.00000  0.00000  178 ARG   I CZ  
976   N NH1 . ARG   A  178 ? 0.78558 0.78558 0.78558 0.00000  0.00000  0.00000  178 ARG   I NH1 
977   N NH2 . ARG   A  178 ? 1.26222 1.26222 1.26222 -0.00000 0.00000  0.00000  178 ARG   I NH2 
978   N N   . ALA   A  179 ? 0.63721 0.63721 0.63721 0.00000  0.00000  0.00000  179 ALA   I N   
979   C CA  . ALA   A  179 ? 0.62031 0.62031 0.62031 0.00000  0.00000  0.00000  179 ALA   I CA  
980   C C   . ALA   A  179 ? 0.47864 0.47864 0.47864 -0.00000 0.00000  0.00000  179 ALA   I C   
981   O O   . ALA   A  179 ? 0.57547 0.57547 0.57547 0.00000  0.00000  0.00000  179 ALA   I O   
982   C CB  . ALA   A  179 ? 0.31431 0.31431 0.31431 0.00000  0.00000  0.00000  179 ALA   I CB  
983   N N   . LEU   A  180 ? 0.57708 0.57708 0.57708 0.00000  0.00000  0.00000  180 LEU   I N   
984   C CA  . LEU   A  180 ? 0.41187 0.41187 0.41187 0.00000  0.00000  0.00000  180 LEU   I CA  
985   C C   . LEU   A  180 ? 0.61930 0.61930 0.61930 0.00000  0.00000  0.00000  180 LEU   I C   
986   O O   . LEU   A  180 ? 0.62083 0.62083 0.62083 0.00000  0.00000  0.00000  180 LEU   I O   
987   C CB  . LEU   A  180 ? 0.35278 0.35278 0.35278 -0.00000 0.00000  0.00000  180 LEU   I CB  
988   C CG  . LEU   A  180 ? 0.66709 0.66709 0.66709 0.00000  0.00000  0.00000  180 LEU   I CG  
989   C CD1 . LEU   A  180 ? 0.63709 0.63709 0.63709 -0.00000 0.00000  0.00000  180 LEU   I CD1 
990   C CD2 . LEU   A  180 ? 0.51099 0.51099 0.51099 -0.00000 0.00000  0.00000  180 LEU   I CD2 
991   N N   . SER   A  181 ? 0.59820 0.59820 0.59820 0.00000  0.00000  0.00000  181 SER   I N   
992   C CA  . SER   A  181 ? 0.64774 0.64774 0.64774 -0.00000 0.00000  0.00000  181 SER   I CA  
993   C C   . SER   A  181 ? 0.49194 0.49194 0.49194 0.00000  -0.00000 0.00000  181 SER   I C   
994   O O   . SER   A  181 ? 0.63522 0.63522 0.63522 -0.00000 0.00000  0.00000  181 SER   I O   
995   C CB  . SER   A  181 ? 0.42458 0.42458 0.42458 0.00000  -0.00000 -0.00000 181 SER   I CB  
996   O OG  . SER   A  181 ? 1.28860 1.28860 1.28860 0.00000  0.00000  0.00000  181 SER   I OG  
997   N N   . ALA   A  182 ? 0.69094 0.69094 0.69094 0.00000  0.00000  0.00000  182 ALA   I N   
998   C CA  . ALA   A  182 ? 0.96538 0.96538 0.96538 -0.00000 0.00000  0.00000  182 ALA   I CA  
999   C C   . ALA   A  182 ? 0.70586 0.70586 0.70586 0.00000  0.00000  0.00000  182 ALA   I C   
1000  O O   . ALA   A  182 ? 0.55168 0.55168 0.55168 -0.00000 0.00000  0.00000  182 ALA   I O   
1001  C CB  . ALA   A  182 ? 0.44009 0.44009 0.44009 0.00000  0.00000  0.00000  182 ALA   I CB  
1002  N N   . MET   A  183 ? 0.48232 0.48232 0.48232 0.00000  0.00000  0.00000  183 MET   I N   
1003  C CA  . MET   A  183 ? 0.68657 0.68657 0.68657 0.00000  0.00000  0.00000  183 MET   I CA  
1004  C C   . MET   A  183 ? 0.50090 0.50090 0.50090 0.00000  0.00000  0.00000  183 MET   I C   
1005  O O   . MET   A  183 ? 0.73641 0.73641 0.73641 0.00000  0.00000  0.00000  183 MET   I O   
1006  C CB  . MET   A  183 ? 0.49228 0.49228 0.49228 0.00000  0.00000  0.00000  183 MET   I CB  
1007  C CG  . MET   A  183 ? 0.51890 0.51890 0.51890 0.00000  0.00000  0.00000  183 MET   I CG  
1008  S SD  . MET   A  183 ? 0.63555 0.63555 0.63555 0.00000  0.00000  0.00000  183 MET   I SD  
1009  C CE  . MET   A  183 ? 0.58810 0.58810 0.58810 0.00000  0.00000  0.00000  183 MET   I CE  
1010  N N   . VAL   A  184 ? 0.55684 0.55684 0.55684 0.00000  0.00000  0.00000  184 VAL   I N   
1011  C CA  . VAL   A  184 ? 0.64370 0.64370 0.64370 -0.00000 0.00000  0.00000  184 VAL   I CA  
1012  C C   . VAL   A  184 ? 0.40995 0.40995 0.40995 0.00000  0.00000  0.00000  184 VAL   I C   
1013  O O   . VAL   A  184 ? 0.54830 0.54830 0.54830 0.00000  -0.00000 0.00000  184 VAL   I O   
1014  C CB  . VAL   A  184 ? 0.38296 0.38296 0.38296 0.00000  0.00000  0.00000  184 VAL   I CB  
1015  C CG1 . VAL   A  184 ? 0.45277 0.45277 0.45277 -0.00000 0.00000  0.00000  184 VAL   I CG1 
1016  C CG2 . VAL   A  184 ? 0.39702 0.39702 0.39702 0.00000  0.00000  0.00000  184 VAL   I CG2 
1017  N N   . LYS   A  185 ? 0.52869 0.52869 0.52869 0.00000  0.00000  0.00000  185 LYS   I N   
1018  C CA  . LYS   A  185 ? 0.56511 0.56511 0.56511 0.00000  0.00000  0.00000  185 LYS   I CA  
1019  C C   . LYS   A  185 ? 0.25762 0.25762 0.25762 -0.00000 0.00000  0.00000  185 LYS   I C   
1020  O O   . LYS   A  185 ? 0.99762 0.99762 0.99762 -0.00000 0.00000  0.00000  185 LYS   I O   
1021  C CB  . LYS   A  185 ? 0.42098 0.42098 0.42098 0.00000  0.00000  0.00000  185 LYS   I CB  
1022  C CG  . LYS   A  185 ? 0.49955 0.49955 0.49955 0.00000  0.00000  0.00000  185 LYS   I CG  
1023  C CD  . LYS   A  185 ? 0.82171 0.82171 0.82171 0.00000  0.00000  0.00000  185 LYS   I CD  
1024  C CE  . LYS   A  185 ? 0.82988 0.82988 0.82988 0.00000  0.00000  0.00000  185 LYS   I CE  
1025  N NZ  . LYS   A  185 ? 1.00370 1.00370 1.00370 0.00000  0.00000  0.00000  185 LYS   I NZ  
1026  N N   . HIS   A  186 ? 0.65931 0.65931 0.65931 -0.00000 0.00000  0.00000  186 HIS   I N   
1027  C CA  . HIS   A  186 ? 0.43247 0.43247 0.43247 0.00000  0.00000  -0.00000 186 HIS   I CA  
1028  C C   . HIS   A  186 ? 0.67613 0.67613 0.67613 0.00000  0.00000  0.00000  186 HIS   I C   
1029  O O   . HIS   A  186 ? 0.50076 0.50076 0.50076 0.00000  0.00000  0.00000  186 HIS   I O   
1030  C CB  . HIS   A  186 ? 0.53944 0.53944 0.53944 0.00000  0.00000  0.00000  186 HIS   I CB  
1031  C CG  . HIS   A  186 ? 0.86929 0.86929 0.86929 0.00000  0.00000  0.00000  186 HIS   I CG  
1032  N ND1 . HIS   A  186 ? 0.70436 0.70436 0.70436 0.00000  0.00000  -0.00000 186 HIS   I ND1 
1033  C CD2 . HIS   A  186 ? 0.35810 0.35810 0.35810 0.00000  0.00000  0.00000  186 HIS   I CD2 
1034  C CE1 . HIS   A  186 ? 0.54958 0.54958 0.54958 -0.00000 0.00000  0.00000  186 HIS   I CE1 
1035  N NE2 . HIS   A  186 ? 0.75293 0.75293 0.75293 0.00000  0.00000  0.00000  186 HIS   I NE2 
1036  N N   . TYR   A  187 ? 0.54361 0.54361 0.54361 0.00000  0.00000  0.00000  187 TYR   I N   
1037  C CA  . TYR   A  187 ? 0.64441 0.64441 0.64441 -0.00000 0.00000  0.00000  187 TYR   I CA  
1038  C C   . TYR   A  187 ? 1.09893 1.09893 1.09893 0.00000  0.00000  0.00000  187 TYR   I C   
1039  O O   . TYR   A  187 ? 0.56131 0.56131 0.56131 0.00000  0.00000  0.00000  187 TYR   I O   
1040  C CB  . TYR   A  187 ? 0.70154 0.70154 0.70154 -0.00000 0.00000  0.00000  187 TYR   I CB  
1041  C CG  . TYR   A  187 ? 0.49899 0.49899 0.49899 0.00000  -0.00000 0.00000  187 TYR   I CG  
1042  C CD1 . TYR   A  187 ? 0.60569 0.60569 0.60569 0.00000  0.00000  0.00000  187 TYR   I CD1 
1043  C CD2 . TYR   A  187 ? 0.68551 0.68551 0.68551 -0.00000 0.00000  0.00000  187 TYR   I CD2 
1044  C CE1 . TYR   A  187 ? 0.55393 0.55393 0.55393 0.00000  0.00000  0.00000  187 TYR   I CE1 
1045  C CE2 . TYR   A  187 ? 0.33287 0.33287 0.33287 0.00000  0.00000  0.00000  187 TYR   I CE2 
1046  C CZ  . TYR   A  187 ? 0.67964 0.67964 0.67964 -0.00000 -0.00000 0.00000  187 TYR   I CZ  
1047  O OH  . TYR   A  187 ? 0.59595 0.59595 0.59595 0.00000  0.00000  0.00000  187 TYR   I OH  
1048  N N   . ASN   A  188 ? 0.48868 0.48868 0.48868 -0.00000 0.00000  0.00000  188 ASN   I N   
1049  C CA  . ASN   A  188 ? 1.11825 1.11825 1.11825 -0.00000 0.00000  0.00000  188 ASN   I CA  
1050  C C   . ASN   A  188 ? 0.47562 0.47562 0.47562 0.00000  0.00000  0.00000  188 ASN   I C   
1051  O O   . ASN   A  188 ? 0.89970 0.89970 0.89970 0.00000  0.00000  0.00000  188 ASN   I O   
1052  C CB  . ASN   A  188 ? 0.62104 0.62104 0.62104 0.00000  0.00000  0.00000  188 ASN   I CB  
1053  C CG  . ASN   A  188 ? 1.11886 1.11886 1.11886 0.00000  0.00000  0.00000  188 ASN   I CG  
1054  O OD1 . ASN   A  188 ? 1.47158 1.47158 1.47158 -0.00000 0.00000  0.00000  188 ASN   I OD1 
1055  N ND2 . ASN   A  188 ? 1.28149 1.28149 1.28149 0.00000  0.00000  0.00000  188 ASN   I ND2 
1056  N N   . GLY   A  189 ? 0.78224 0.78224 0.78224 -0.00000 0.00000  0.00000  189 GLY   I N   
1057  C CA  . GLY   A  189 ? 0.36324 0.36324 0.36324 0.00000  0.00000  0.00000  189 GLY   I CA  
1058  C C   . GLY   A  189 ? 0.41599 0.41599 0.41599 -0.00000 0.00000  0.00000  189 GLY   I C   
1059  O O   . GLY   A  189 ? 0.83263 0.83263 0.83263 0.00000  0.00000  0.00000  189 GLY   I O   
1060  N N   . ARG   A  190 ? 0.53313 0.53313 0.53313 0.00000  0.00000  0.00000  190 ARG   I N   
1061  C CA  . ARG   A  190 ? 0.38320 0.38320 0.38320 0.00000  0.00000  0.00000  190 ARG   I CA  
1062  C C   . ARG   A  190 ? 0.47331 0.47331 0.47331 0.00000  0.00000  0.00000  190 ARG   I C   
1063  O O   . ARG   A  190 ? 0.60866 0.60866 0.60866 0.00000  0.00000  0.00000  190 ARG   I O   
1064  C CB  . ARG   A  190 ? 0.47451 0.47451 0.47451 0.00000  0.00000  0.00000  190 ARG   I CB  
1065  C CG  . ARG   A  190 ? 0.40683 0.40683 0.40683 0.00000  0.00000  0.00000  190 ARG   I CG  
1066  C CD  . ARG   A  190 ? 0.28659 0.28659 0.28659 0.00000  0.00000  0.00000  190 ARG   I CD  
1067  N NE  . ARG   A  190 ? 0.47221 0.47221 0.47221 0.00000  -0.00000 -0.00000 190 ARG   I NE  
1068  C CZ  . ARG   A  190 ? 0.68727 0.68727 0.68727 0.00000  0.00000  0.00000  190 ARG   I CZ  
1069  N NH1 . ARG   A  190 ? 0.63986 0.63986 0.63986 0.00000  0.00000  0.00000  190 ARG   I NH1 
1070  N NH2 . ARG   A  190 ? 0.50558 0.50558 0.50558 0.00000  0.00000  0.00000  190 ARG   I NH2 
1071  N N   . ALA   A  191 ? 0.53286 0.53286 0.53286 0.00000  0.00000  0.00000  191 ALA   I N   
1072  C CA  . ALA   A  191 ? 0.37829 0.37829 0.37829 0.00000  0.00000  0.00000  191 ALA   I CA  
1073  C C   . ALA   A  191 ? 1.17666 1.17666 1.17666 -0.00000 0.00000  0.00000  191 ALA   I C   
1074  O O   . ALA   A  191 ? 0.39419 0.39419 0.39419 0.00000  0.00000  0.00000  191 ALA   I O   
1075  C CB  . ALA   A  191 ? 0.53428 0.53428 0.53428 0.00000  0.00000  0.00000  191 ALA   I CB  
1076  N N   . PHE   A  192 ? 0.40303 0.40303 0.40303 0.00000  0.00000  0.00000  192 PHE   I N   
1077  C CA  . PHE   A  192 ? 0.45208 0.45208 0.45208 0.00000  0.00000  0.00000  192 PHE   I CA  
1078  C C   . PHE   A  192 ? 0.75410 0.75410 0.75410 0.00000  0.00000  0.00000  192 PHE   I C   
1079  O O   . PHE   A  192 ? 0.62225 0.62225 0.62225 0.00000  0.00000  0.00000  192 PHE   I O   
1080  C CB  . PHE   A  192 ? 0.47157 0.47157 0.47157 0.00000  0.00000  0.00000  192 PHE   I CB  
1081  C CG  . PHE   A  192 ? 0.56605 0.56605 0.56605 0.00000  -0.00000 -0.00000 192 PHE   I CG  
1082  C CD1 . PHE   A  192 ? 0.68189 0.68189 0.68189 -0.00000 0.00000  0.00000  192 PHE   I CD1 
1083  C CD2 . PHE   A  192 ? 0.66858 0.66858 0.66858 0.00000  0.00000  0.00000  192 PHE   I CD2 
1084  C CE1 . PHE   A  192 ? 0.43609 0.43609 0.43609 0.00000  0.00000  0.00000  192 PHE   I CE1 
1085  C CE2 . PHE   A  192 ? 0.74586 0.74586 0.74586 0.00000  -0.00000 0.00000  192 PHE   I CE2 
1086  C CZ  . PHE   A  192 ? 0.53618 0.53618 0.53618 0.00000  0.00000  0.00000  192 PHE   I CZ  
1087  N N   . ASP   A  193 ? 0.65344 0.65344 0.65344 -0.00000 0.00000  0.00000  193 ASP   I N   
1088  C CA  . ASP   A  193 ? 0.40137 0.40137 0.40137 0.00000  0.00000  0.00000  193 ASP   I CA  
1089  C C   . ASP   A  193 ? 0.73691 0.73691 0.73691 0.00000  0.00000  0.00000  193 ASP   I C   
1090  O O   . ASP   A  193 ? 0.24153 0.24153 0.24153 0.00000  0.00000  0.00000  193 ASP   I O   
1091  C CB  . ASP   A  193 ? 0.56462 0.56462 0.56462 -0.00000 0.00000  0.00000  193 ASP   I CB  
1092  C CG  . ASP   A  193 ? 1.10772 1.10772 1.10772 -0.00000 0.00000  0.00000  193 ASP   I CG  
1093  O OD1 . ASP   A  193 ? 0.61019 0.61019 0.61019 0.00000  0.00000  0.00000  193 ASP   I OD1 
1094  O OD2 . ASP   A  193 ? 0.59117 0.59117 0.59117 -0.00000 -0.00000 -0.00000 193 ASP   I OD2 
1095  N N   . GLU   A  194 ? 0.29521 0.29521 0.29521 0.00000  0.00000  0.00000  194 GLU   I N   
1096  C CA  . GLU   A  194 ? 0.63680 0.63680 0.63680 0.00000  0.00000  0.00000  194 GLU   I CA  
1097  C C   . GLU   A  194 ? 0.69224 0.69224 0.69224 -0.00000 0.00000  0.00000  194 GLU   I C   
1098  O O   . GLU   A  194 ? 0.54651 0.54651 0.54651 0.00000  0.00000  0.00000  194 GLU   I O   
1099  C CB  . GLU   A  194 ? 0.53248 0.53248 0.53248 0.00000  0.00000  0.00000  194 GLU   I CB  
1100  C CG  . GLU   A  194 ? 0.35234 0.35234 0.35234 -0.00000 0.00000  0.00000  194 GLU   I CG  
1101  C CD  . GLU   A  194 ? 1.08152 1.08152 1.08152 -0.00000 0.00000  0.00000  194 GLU   I CD  
1102  O OE1 . GLU   A  194 ? 0.75996 0.75996 0.75996 -0.00000 0.00000  0.00000  194 GLU   I OE1 
1103  O OE2 . GLU   A  194 ? 0.72897 0.72897 0.72897 0.00000  0.00000  0.00000  194 GLU   I OE2 
1104  N N   . VAL   A  195 ? 0.67936 0.67936 0.67936 -0.00000 0.00000  0.00000  195 VAL   I N   
1105  C CA  . VAL   A  195 ? 0.27154 0.27154 0.27154 0.00000  0.00000  0.00000  195 VAL   I CA  
1106  C C   . VAL   A  195 ? 1.04951 1.04951 1.04951 -0.00000 -0.00000 0.00000  195 VAL   I C   
1107  O O   . VAL   A  195 ? 0.43892 0.43892 0.43892 -0.00000 0.00000  0.00000  195 VAL   I O   
1108  C CB  . VAL   A  195 ? 0.71780 0.71780 0.71780 0.00000  0.00000  0.00000  195 VAL   I CB  
1109  C CG1 . VAL   A  195 ? 0.33368 0.33368 0.33368 0.00000  0.00000  0.00000  195 VAL   I CG1 
1110  C CG2 . VAL   A  195 ? 0.39697 0.39697 0.39697 0.00000  0.00000  0.00000  195 VAL   I CG2 
1111  N N   . PHE   A  196 ? 0.32483 0.32483 0.32483 -0.00000 0.00000  0.00000  196 PHE   I N   
1112  C CA  . PHE   A  196 ? 0.72911 0.72911 0.72911 0.00000  0.00000  0.00000  196 PHE   I CA  
1113  C C   . PHE   A  196 ? 0.48207 0.48207 0.48207 0.00000  0.00000  0.00000  196 PHE   I C   
1114  O O   . PHE   A  196 ? 0.51070 0.51070 0.51070 -0.00000 0.00000  0.00000  196 PHE   I O   
1115  C CB  . PHE   A  196 ? 0.38388 0.38388 0.38388 0.00000  0.00000  0.00000  196 PHE   I CB  
1116  C CG  . PHE   A  196 ? 0.60496 0.60496 0.60496 -0.00000 0.00000  0.00000  196 PHE   I CG  
1117  C CD1 . PHE   A  196 ? 0.39858 0.39858 0.39858 -0.00000 0.00000  0.00000  196 PHE   I CD1 
1118  C CD2 . PHE   A  196 ? 0.31516 0.31516 0.31516 0.00000  0.00000  0.00000  196 PHE   I CD2 
1119  C CE1 . PHE   A  196 ? 0.44944 0.44944 0.44944 -0.00000 0.00000  0.00000  196 PHE   I CE1 
1120  C CE2 . PHE   A  196 ? 0.54547 0.54547 0.54547 0.00000  0.00000  0.00000  196 PHE   I CE2 
1121  C CZ  . PHE   A  196 ? 0.43641 0.43641 0.43641 0.00000  0.00000  0.00000  196 PHE   I CZ  
1122  N N   . LEU   A  197 ? 0.55828 0.55828 0.55828 -0.00000 0.00000  0.00000  197 LEU   I N   
1123  C CA  . LEU   A  197 ? 0.59408 0.59408 0.59408 -0.00000 0.00000  0.00000  197 LEU   I CA  
1124  C C   . LEU   A  197 ? 0.82957 0.82957 0.82957 0.00000  0.00000  0.00000  197 LEU   I C   
1125  O O   . LEU   A  197 ? 0.51799 0.51799 0.51799 -0.00000 0.00000  0.00000  197 LEU   I O   
1126  C CB  . LEU   A  197 ? 0.56283 0.56283 0.56283 0.00000  0.00000  0.00000  197 LEU   I CB  
1127  C CG  . LEU   A  197 ? 0.52099 0.52099 0.52099 -0.00000 0.00000  0.00000  197 LEU   I CG  
1128  C CD1 . LEU   A  197 ? 0.62541 0.62541 0.62541 0.00000  0.00000  0.00000  197 LEU   I CD1 
1129  C CD2 . LEU   A  197 ? 1.11879 1.11879 1.11879 0.00000  0.00000  0.00000  197 LEU   I CD2 
1130  N N   . CYS   A  198 ? 0.64989 0.64989 0.64989 0.00000  0.00000  0.00000  198 CYS   I N   
1131  C CA  . CYS   A  198 ? 0.63943 0.63943 0.63943 -0.00000 0.00000  0.00000  198 CYS   I CA  
1132  C C   . CYS   A  198 ? 0.68542 0.68542 0.68542 -0.00000 0.00000  0.00000  198 CYS   I C   
1133  O O   . CYS   A  198 ? 0.77530 0.77530 0.77530 -0.00000 0.00000  0.00000  198 CYS   I O   
1134  C CB  . CYS   A  198 ? 0.55653 0.55653 0.55653 0.00000  0.00000  0.00000  198 CYS   I CB  
1135  S SG  . CYS   A  198 ? 0.66717 0.66717 0.66717 0.00000  0.00000  0.00000  198 CYS   I SG  
1136  N N   . ASP   A  199 ? 0.68791 0.68791 0.68791 0.00000  0.00000  0.00000  199 ASP   I N   
1137  C CA  . ASP   A  199 ? 0.54193 0.54193 0.54193 -0.00000 0.00000  0.00000  199 ASP   I CA  
1138  C C   . ASP   A  199 ? 0.98035 0.98035 0.98035 0.00000  0.00000  0.00000  199 ASP   I C   
1139  O O   . ASP   A  199 ? 0.53883 0.53883 0.53883 0.00000  0.00000  0.00000  199 ASP   I O   
1140  C CB  . ASP   A  199 ? 0.56479 0.56479 0.56479 0.00000  0.00000  0.00000  199 ASP   I CB  
1141  C CG  . ASP   A  199 ? 1.84839 1.84839 1.84839 0.00000  0.00000  -0.00000 199 ASP   I CG  
1142  O OD1 . ASP   A  199 ? 0.60071 0.60071 0.60071 -0.00000 0.00000  0.00000  199 ASP   I OD1 
1143  O OD2 . ASP   A  199 ? 0.69823 0.69823 0.69823 0.00000  0.00000  0.00000  199 ASP   I OD2 
1144  N N   . LYS   A  200 ? 0.56888 0.56888 0.56888 0.00000  -0.00000 0.00000  200 LYS   I N   
1145  C CA  . LYS   A  200 ? 0.89135 0.89135 0.89135 0.00000  0.00000  0.00000  200 LYS   I CA  
1146  C C   . LYS   A  200 ? 0.85011 0.85011 0.85011 0.00000  0.00000  0.00000  200 LYS   I C   
1147  O O   . LYS   A  200 ? 0.74520 0.74520 0.74520 -0.00000 0.00000  0.00000  200 LYS   I O   
1148  C CB  . LYS   A  200 ? 0.56654 0.56654 0.56654 0.00000  0.00000  0.00000  200 LYS   I CB  
1149  C CG  . LYS   A  200 ? 0.85518 0.85518 0.85518 0.00000  0.00000  0.00000  200 LYS   I CG  
1150  C CD  . LYS   A  200 ? 1.11494 1.11494 1.11494 0.00000  0.00000  0.00000  200 LYS   I CD  
1151  C CE  . LYS   A  200 ? 0.90316 0.90316 0.90316 0.00000  0.00000  0.00000  200 LYS   I CE  
1152  N NZ  . LYS   A  200 ? 0.83451 0.83451 0.83451 0.00000  0.00000  0.00000  200 LYS   I NZ  
1153  N N   . ASN   A  201 ? 0.68944 0.68944 0.68944 0.00000  0.00000  0.00000  201 ASN   I N   
1154  C CA  . ASN   A  201 ? 0.98278 0.98278 0.98278 0.00000  0.00000  0.00000  201 ASN   I CA  
1155  C C   . ASN   A  201 ? 0.67559 0.67559 0.67559 0.00000  0.00000  0.00000  201 ASN   I C   
1156  O O   . ASN   A  201 ? 1.08139 1.08139 1.08139 0.00000  0.00000  -0.00000 201 ASN   I O   
1157  C CB  . ASN   A  201 ? 0.65346 0.65346 0.65346 0.00000  0.00000  0.00000  201 ASN   I CB  
1158  C CG  . ASN   A  201 ? 1.12795 1.12795 1.12795 0.00000  0.00000  0.00000  201 ASN   I CG  
1159  O OD1 . ASN   A  201 ? 0.53563 0.53563 0.53563 -0.00000 0.00000  0.00000  201 ASN   I OD1 
1160  N ND2 . ASN   A  201 ? 0.72411 0.72411 0.72411 0.00000  0.00000  0.00000  201 ASN   I ND2 
1161  N N   . ALA   A  202 ? 1.34015 1.34015 1.34015 0.00000  0.00000  -0.00000 202 ALA   I N   
1162  C CA  . ALA   A  202 ? 0.73850 0.73850 0.73850 0.00000  -0.00000 0.00000  202 ALA   I CA  
1163  C C   . ALA   A  202 ? 0.65277 0.65277 0.65277 0.00000  0.00000  0.00000  202 ALA   I C   
1164  O O   . ALA   A  202 ? 0.80164 0.80164 0.80164 0.00000  0.00000  0.00000  202 ALA   I O   
1165  C CB  . ALA   A  202 ? 0.45187 0.45187 0.45187 0.00000  0.00000  0.00000  202 ALA   I CB  
1166  N N   . PRO   A  203 ? 1.08327 1.08327 1.08327 0.00000  0.00000  0.00000  203 PRO   I N   
1167  C CA  . PRO   A  203 ? 1.01767 1.01767 1.01767 0.00000  0.00000  0.00000  203 PRO   I CA  
1168  C C   . PRO   A  203 ? 0.88880 0.88880 0.88880 0.00000  0.00000  -0.00000 203 PRO   I C   
1169  O O   . PRO   A  203 ? 0.63875 0.63875 0.63875 0.00000  0.00000  0.00000  203 PRO   I O   
1170  C CB  . PRO   A  203 ? 0.72995 0.72995 0.72995 -0.00000 0.00000  0.00000  203 PRO   I CB  
1171  C CG  . PRO   A  203 ? 0.61227 0.61227 0.61227 0.00000  0.00000  0.00000  203 PRO   I CG  
1172  C CD  . PRO   A  203 ? 0.46198 0.46198 0.46198 0.00000  0.00000  0.00000  203 PRO   I CD  
1173  N N   . TYR   A  204 ? 0.68062 0.68062 0.68062 0.00000  0.00000  0.00000  204 TYR   I N   
1174  C CA  . TYR   A  204 ? 0.82082 0.82082 0.82082 0.00000  0.00000  0.00000  204 TYR   I CA  
1175  C C   . TYR   A  204 ? 0.74114 0.74114 0.74114 -0.00000 0.00000  0.00000  204 TYR   I C   
1176  O O   . TYR   A  204 ? 0.79627 0.79627 0.79627 0.00000  0.00000  0.00000  204 TYR   I O   
1177  C CB  . TYR   A  204 ? 0.66131 0.66131 0.66131 0.00000  0.00000  0.00000  204 TYR   I CB  
1178  C CG  . TYR   A  204 ? 0.71547 0.71547 0.71547 -0.00000 -0.00000 0.00000  204 TYR   I CG  
1179  C CD1 . TYR   A  204 ? 0.64912 0.64912 0.64912 -0.00000 -0.00000 0.00000  204 TYR   I CD1 
1180  C CD2 . TYR   A  204 ? 0.60083 0.60083 0.60083 0.00000  0.00000  0.00000  204 TYR   I CD2 
1181  C CE1 . TYR   A  204 ? 0.43021 0.43021 0.43021 0.00000  0.00000  0.00000  204 TYR   I CE1 
1182  C CE2 . TYR   A  204 ? 0.56338 0.56338 0.56338 -0.00000 0.00000  0.00000  204 TYR   I CE2 
1183  C CZ  . TYR   A  204 ? 0.73073 0.73073 0.73073 -0.00000 0.00000  0.00000  204 TYR   I CZ  
1184  O OH  . TYR   A  204 ? 0.75618 0.75618 0.75618 0.00000  0.00000  0.00000  204 TYR   I OH  
1185  N N   . TYR   A  205 ? 0.50320 0.50320 0.50320 0.00000  0.00000  0.00000  205 TYR   I N   
1186  C CA  . TYR   A  205 ? 0.47737 0.47737 0.47737 0.00000  0.00000  0.00000  205 TYR   I CA  
1187  C C   . TYR   A  205 ? 0.57138 0.57138 0.57138 -0.00000 0.00000  0.00000  205 TYR   I C   
1188  O O   . TYR   A  205 ? 0.54584 0.54584 0.54584 0.00000  0.00000  0.00000  205 TYR   I O   
1189  C CB  . TYR   A  205 ? 0.56752 0.56752 0.56752 0.00000  0.00000  0.00000  205 TYR   I CB  
1190  C CG  . TYR   A  205 ? 0.74112 0.74112 0.74112 0.00000  0.00000  0.00000  205 TYR   I CG  
1191  C CD1 . TYR   A  205 ? 0.64298 0.64298 0.64298 0.00000  -0.00000 0.00000  205 TYR   I CD1 
1192  C CD2 . TYR   A  205 ? 0.58285 0.58285 0.58285 0.00000  0.00000  -0.00000 205 TYR   I CD2 
1193  C CE1 . TYR   A  205 ? 0.45145 0.45145 0.45145 0.00000  0.00000  0.00000  205 TYR   I CE1 
1194  C CE2 . TYR   A  205 ? 0.75542 0.75542 0.75542 -0.00000 0.00000  0.00000  205 TYR   I CE2 
1195  C CZ  . TYR   A  205 ? 1.00738 1.00738 1.00738 -0.00000 0.00000  0.00000  205 TYR   I CZ  
1196  O OH  . TYR   A  205 ? 0.63487 0.63487 0.63487 0.00000  0.00000  0.00000  205 TYR   I OH  
1197  N N   . GLY   A  206 ? 0.44270 0.44270 0.44270 0.00000  0.00000  0.00000  206 GLY   I N   
1198  C CA  . GLY   A  206 ? 0.42861 0.42861 0.42861 0.00000  -0.00000 0.00000  206 GLY   I CA  
1199  C C   . GLY   A  206 ? 0.60324 0.60324 0.60324 0.00000  0.00000  0.00000  206 GLY   I C   
1200  O O   . GLY   A  206 ? 0.50213 0.50213 0.50213 -0.00000 0.00000  0.00000  206 GLY   I O   
1201  N N   . PHE   A  207 ? 0.54527 0.54527 0.54527 0.00000  0.00000  0.00000  207 PHE   I N   
1202  C CA  . PHE   A  207 ? 0.69800 0.69800 0.69800 0.00000  0.00000  0.00000  207 PHE   I CA  
1203  C C   . PHE   A  207 ? 0.64055 0.64055 0.64055 0.00000  0.00000  0.00000  207 PHE   I C   
1204  O O   . PHE   A  207 ? 0.76773 0.76773 0.76773 0.00000  0.00000  0.00000  207 PHE   I O   
1205  C CB  . PHE   A  207 ? 0.53760 0.53760 0.53760 -0.00000 0.00000  0.00000  207 PHE   I CB  
1206  C CG  . PHE   A  207 ? 0.73579 0.73579 0.73579 0.00000  0.00000  0.00000  207 PHE   I CG  
1207  C CD1 . PHE   A  207 ? 0.40368 0.40368 0.40368 0.00000  0.00000  0.00000  207 PHE   I CD1 
1208  C CD2 . PHE   A  207 ? 0.45911 0.45911 0.45911 -0.00000 0.00000  0.00000  207 PHE   I CD2 
1209  C CE1 . PHE   A  207 ? 0.66087 0.66087 0.66087 0.00000  0.00000  0.00000  207 PHE   I CE1 
1210  C CE2 . PHE   A  207 ? 0.50541 0.50541 0.50541 0.00000  0.00000  0.00000  207 PHE   I CE2 
1211  C CZ  . PHE   A  207 ? 0.72017 0.72017 0.72017 -0.00000 0.00000  0.00000  207 PHE   I CZ  
1212  N N   . ASN   A  208 ? 0.56470 0.56470 0.56470 0.00000  0.00000  0.00000  208 ASN   I N   
1213  C CA  . ASN   A  208 ? 0.84983 0.84983 0.84983 -0.00000 0.00000  0.00000  208 ASN   I CA  
1214  C C   . ASN   A  208 ? 0.46512 0.46512 0.46512 0.00000  0.00000  0.00000  208 ASN   I C   
1215  O O   . ASN   A  208 ? 1.20191 1.20191 1.20191 0.00000  0.00000  0.00000  208 ASN   I O   
1216  C CB  . ASN   A  208 ? 0.47082 0.47082 0.47082 0.00000  0.00000  0.00000  208 ASN   I CB  
1217  C CG  . ASN   A  208 ? 1.18601 1.18601 1.18601 0.00000  0.00000  0.00000  208 ASN   I CG  
1218  O OD1 . ASN   A  208 ? 1.88322 1.88322 1.88322 -0.00000 0.00000  0.00000  208 ASN   I OD1 
1219  N ND2 . ASN   A  208 ? 0.89440 0.89440 0.89440 0.00000  0.00000  0.00000  208 ASN   I ND2 
1220  N N   . SER   A  209 ? 0.75299 0.75299 0.75299 0.00000  0.00000  0.00000  209 SER   I N   
1221  C CA  . SER   A  209 ? 0.54356 0.54356 0.54356 0.00000  0.00000  -0.00000 209 SER   I CA  
1222  C C   . SER   A  209 ? 0.82406 0.82406 0.82406 0.00000  0.00000  0.00000  209 SER   I C   
1223  O O   . SER   A  209 ? 0.51039 0.51039 0.51039 0.00000  0.00000  0.00000  209 SER   I O   
1224  C CB  . SER   A  209 ? 0.68279 0.68279 0.68279 -0.00000 0.00000  0.00000  209 SER   I CB  
1225  O OG  . SER   A  209 ? 0.42092 0.42092 0.42092 0.00000  -0.00000 0.00000  209 SER   I OG  
1226  N N   . TYR   A  210 ? 0.58182 0.58182 0.58182 0.00000  0.00000  0.00000  210 TYR   I N   
1227  C CA  . TYR   A  210 ? 0.43127 0.43127 0.43127 0.00000  0.00000  0.00000  210 TYR   I CA  
1228  C C   . TYR   A  210 ? 0.59602 0.59602 0.59602 0.00000  0.00000  0.00000  210 TYR   I C   
1229  O O   . TYR   A  210 ? 0.50669 0.50669 0.50669 0.00000  0.00000  0.00000  210 TYR   I O   
1230  C CB  . TYR   A  210 ? 0.29708 0.29708 0.29708 0.00000  0.00000  0.00000  210 TYR   I CB  
1231  C CG  . TYR   A  210 ? 0.71596 0.71596 0.71596 0.00000  0.00000  0.00000  210 TYR   I CG  
1232  C CD1 . TYR   A  210 ? 0.42494 0.42494 0.42494 0.00000  0.00000  0.00000  210 TYR   I CD1 
1233  C CD2 . TYR   A  210 ? 0.62016 0.62016 0.62016 0.00000  0.00000  0.00000  210 TYR   I CD2 
1234  C CE1 . TYR   A  210 ? 0.47083 0.47083 0.47083 0.00000  0.00000  0.00000  210 TYR   I CE1 
1235  C CE2 . TYR   A  210 ? 0.64257 0.64257 0.64257 0.00000  0.00000  0.00000  210 TYR   I CE2 
1236  C CZ  . TYR   A  210 ? 0.75650 0.75650 0.75650 -0.00000 0.00000  0.00000  210 TYR   I CZ  
1237  O OH  . TYR   A  210 ? 0.52569 0.52569 0.52569 0.00000  0.00000  0.00000  210 TYR   I OH  
1238  N N   . ASP   A  211 ? 0.49499 0.49499 0.49499 -0.00000 0.00000  0.00000  211 ASP   I N   
1239  C CA  . ASP   A  211 ? 0.42817 0.42817 0.42817 -0.00000 0.00000  0.00000  211 ASP   I CA  
1240  C C   . ASP   A  211 ? 0.69906 0.69906 0.69906 -0.00000 0.00000  0.00000  211 ASP   I C   
1241  O O   . ASP   A  211 ? 0.45693 0.45693 0.45693 0.00000  0.00000  0.00000  211 ASP   I O   
1242  C CB  . ASP   A  211 ? 0.46793 0.46793 0.46793 0.00000  0.00000  0.00000  211 ASP   I CB  
1243  C CG  . ASP   A  211 ? 0.47481 0.47481 0.47481 0.00000  0.00000  0.00000  211 ASP   I CG  
1244  O OD1 . ASP   A  211 ? 0.53499 0.53499 0.53499 0.00000  0.00000  0.00000  211 ASP   I OD1 
1245  O OD2 . ASP   A  211 ? 0.76189 0.76189 0.76189 -0.00000 0.00000  -0.00000 211 ASP   I OD2 
1246  N N   . ASP   A  212 ? 0.53035 0.53035 0.53035 0.00000  0.00000  0.00000  212 ASP   I N   
1247  C CA  . ASP   A  212 ? 0.65090 0.65090 0.65090 0.00000  0.00000  0.00000  212 ASP   I CA  
1248  C C   . ASP   A  212 ? 0.55292 0.55292 0.55292 -0.00000 0.00000  0.00000  212 ASP   I C   
1249  O O   . ASP   A  212 ? 0.56162 0.56162 0.56162 -0.00000 0.00000  0.00000  212 ASP   I O   
1250  C CB  . ASP   A  212 ? 0.66963 0.66963 0.66963 0.00000  0.00000  0.00000  212 ASP   I CB  
1251  C CG  . ASP   A  212 ? 0.77247 0.77247 0.77247 0.00000  -0.00000 0.00000  212 ASP   I CG  
1252  O OD1 . ASP   A  212 ? 0.96246 0.96246 0.96246 0.00000  0.00000  -0.00000 212 ASP   I OD1 
1253  O OD2 . ASP   A  212 ? 0.78353 0.78353 0.78353 0.00000  0.00000  0.00000  212 ASP   I OD2 
1254  N N   . PHE   A  213 ? 0.38463 0.38463 0.38463 -0.00000 0.00000  0.00000  213 PHE   I N   
1255  C CA  . PHE   A  213 ? 0.35005 0.35005 0.35005 -0.00000 0.00000  -0.00000 213 PHE   I CA  
1256  C C   . PHE   A  213 ? 0.81751 0.81751 0.81751 -0.00000 0.00000  -0.00000 213 PHE   I C   
1257  O O   . PHE   A  213 ? 0.49451 0.49451 0.49451 -0.00000 0.00000  0.00000  213 PHE   I O   
1258  C CB  . PHE   A  213 ? 0.43463 0.43463 0.43463 -0.00000 0.00000  0.00000  213 PHE   I CB  
1259  C CG  . PHE   A  213 ? 0.59548 0.59548 0.59548 0.00000  -0.00000 0.00000  213 PHE   I CG  
1260  C CD1 . PHE   A  213 ? 0.63957 0.63957 0.63957 -0.00000 0.00000  0.00000  213 PHE   I CD1 
1261  C CD2 . PHE   A  213 ? 0.44610 0.44610 0.44610 0.00000  0.00000  0.00000  213 PHE   I CD2 
1262  C CE1 . PHE   A  213 ? 0.75958 0.75958 0.75958 0.00000  0.00000  0.00000  213 PHE   I CE1 
1263  C CE2 . PHE   A  213 ? 0.79683 0.79683 0.79683 -0.00000 0.00000  0.00000  213 PHE   I CE2 
1264  C CZ  . PHE   A  213 ? 0.66325 0.66325 0.66325 -0.00000 0.00000  0.00000  213 PHE   I CZ  
1265  N N   . PHE   A  214 ? 0.43262 0.43262 0.43262 0.00000  0.00000  0.00000  214 PHE   I N   
1266  C CA  . PHE   A  214 ? 0.41100 0.41100 0.41100 -0.00000 0.00000  0.00000  214 PHE   I CA  
1267  C C   . PHE   A  214 ? 0.39587 0.39587 0.39587 -0.00000 0.00000  0.00000  214 PHE   I C   
1268  O O   . PHE   A  214 ? 0.74572 0.74572 0.74572 0.00000  0.00000  0.00000  214 PHE   I O   
1269  C CB  . PHE   A  214 ? 0.52161 0.52161 0.52161 0.00000  0.00000  0.00000  214 PHE   I CB  
1270  C CG  . PHE   A  214 ? 0.49895 0.49895 0.49895 0.00000  0.00000  0.00000  214 PHE   I CG  
1271  C CD1 . PHE   A  214 ? 0.48045 0.48045 0.48045 -0.00000 0.00000  0.00000  214 PHE   I CD1 
1272  C CD2 . PHE   A  214 ? 0.59309 0.59309 0.59309 0.00000  0.00000  -0.00000 214 PHE   I CD2 
1273  C CE1 . PHE   A  214 ? 0.43542 0.43542 0.43542 0.00000  0.00000  0.00000  214 PHE   I CE1 
1274  C CE2 . PHE   A  214 ? 0.58538 0.58538 0.58538 -0.00000 0.00000  0.00000  214 PHE   I CE2 
1275  C CZ  . PHE   A  214 ? 0.50838 0.50838 0.50838 0.00000  0.00000  0.00000  214 PHE   I CZ  
1276  N N   . ASN   A  215 ? 0.29857 0.29857 0.29857 0.00000  0.00000  0.00000  215 ASN   I N   
1277  C CA  . ASN   A  215 ? 0.39557 0.39557 0.39557 -0.00000 0.00000  0.00000  215 ASN   I CA  
1278  C C   . ASN   A  215 ? 0.51947 0.51947 0.51947 0.00000  0.00000  0.00000  215 ASN   I C   
1279  O O   . ASN   A  215 ? 0.44023 0.44023 0.44023 0.00000  0.00000  0.00000  215 ASN   I O   
1280  C CB  . ASN   A  215 ? 0.39364 0.39364 0.39364 0.00000  0.00000  0.00000  215 ASN   I CB  
1281  C CG  . ASN   A  215 ? 0.68648 0.68648 0.68648 0.00000  0.00000  0.00000  215 ASN   I CG  
1282  O OD1 . ASN   A  215 ? 0.41621 0.41621 0.41621 0.00000  0.00000  0.00000  215 ASN   I OD1 
1283  N ND2 . ASN   A  215 ? 0.37477 0.37477 0.37477 0.00000  0.00000  0.00000  215 ASN   I ND2 
1284  N N   . ARG   A  216 ? 0.28284 0.28284 0.28284 -0.00000 0.00000  0.00000  216 ARG   I N   
1285  C CA  . ARG   A  216 ? 0.39532 0.39532 0.39532 -0.00000 0.00000  0.00000  216 ARG   I CA  
1286  C C   . ARG   A  216 ? 0.68716 0.68716 0.68716 -0.00000 0.00000  0.00000  216 ARG   I C   
1287  O O   . ARG   A  216 ? 0.38554 0.38554 0.38554 -0.00000 0.00000  0.00000  216 ARG   I O   
1288  C CB  . ARG   A  216 ? 0.34824 0.34824 0.34824 0.00000  0.00000  0.00000  216 ARG   I CB  
1289  C CG  . ARG   A  216 ? 0.33926 0.33926 0.33926 -0.00000 0.00000  0.00000  216 ARG   I CG  
1290  C CD  . ARG   A  216 ? 0.46989 0.46989 0.46989 -0.00000 0.00000  0.00000  216 ARG   I CD  
1291  N NE  . ARG   A  216 ? 0.32982 0.32982 0.32982 0.00000  0.00000  0.00000  216 ARG   I NE  
1292  C CZ  . ARG   A  216 ? 0.64365 0.64365 0.64365 0.00000  0.00000  -0.00000 216 ARG   I CZ  
1293  N NH1 . ARG   A  216 ? 0.37532 0.37532 0.37532 -0.00000 0.00000  0.00000  216 ARG   I NH1 
1294  N NH2 . ARG   A  216 ? 0.43211 0.43211 0.43211 0.00000  0.00000  0.00000  216 ARG   I NH2 
1295  N N   . ARG   A  217 ? 0.63160 0.63160 0.63160 0.00000  0.00000  0.00000  217 ARG   I N   
1296  C CA  . ARG   A  217 ? 0.47371 0.47371 0.47371 0.00000  0.00000  0.00000  217 ARG   I CA  
1297  C C   . ARG   A  217 ? 0.28866 0.28866 0.28866 0.00000  0.00000  0.00000  217 ARG   I C   
1298  O O   . ARG   A  217 ? 0.47139 0.47139 0.47139 -0.00000 0.00000  0.00000  217 ARG   I O   
1299  C CB  . ARG   A  217 ? 0.30082 0.30082 0.30082 0.00000  0.00000  0.00000  217 ARG   I CB  
1300  C CG  . ARG   A  217 ? 0.77089 0.77089 0.77089 0.00000  0.00000  0.00000  217 ARG   I CG  
1301  C CD  . ARG   A  217 ? 0.58542 0.58542 0.58542 -0.00000 0.00000  0.00000  217 ARG   I CD  
1302  N NE  . ARG   A  217 ? 1.01853 1.01853 1.01853 0.00000  0.00000  0.00000  217 ARG   I NE  
1303  C CZ  . ARG   A  217 ? 1.04037 1.04037 1.04037 0.00000  0.00000  0.00000  217 ARG   I CZ  
1304  N NH1 . ARG   A  217 ? 1.17087 1.17087 1.17087 0.00000  0.00000  0.00000  217 ARG   I NH1 
1305  N NH2 . ARG   A  217 ? 1.41888 1.41888 1.41888 -0.00000 -0.00000 0.00000  217 ARG   I NH2 
1306  N N   . PHE   A  218 ? 0.48566 0.48566 0.48566 0.00000  0.00000  -0.00000 218 PHE   I N   
1307  C CA  . PHE   A  218 ? 0.34467 0.34467 0.34467 0.00000  0.00000  0.00000  218 PHE   I CA  
1308  C C   . PHE   A  218 ? 0.73033 0.73033 0.73033 -0.00000 0.00000  0.00000  218 PHE   I C   
1309  O O   . PHE   A  218 ? 0.37267 0.37267 0.37267 0.00000  0.00000  0.00000  218 PHE   I O   
1310  C CB  . PHE   A  218 ? 0.22879 0.22879 0.22879 0.00000  0.00000  0.00000  218 PHE   I CB  
1311  C CG  . PHE   A  218 ? 0.47774 0.47774 0.47774 -0.00000 0.00000  0.00000  218 PHE   I CG  
1312  C CD1 . PHE   A  218 ? 0.24992 0.24992 0.24992 0.00000  0.00000  0.00000  218 PHE   I CD1 
1313  C CD2 . PHE   A  218 ? 0.35961 0.35961 0.35961 0.00000  0.00000  -0.00000 218 PHE   I CD2 
1314  C CE1 . PHE   A  218 ? 0.56971 0.56971 0.56971 0.00000  0.00000  0.00000  218 PHE   I CE1 
1315  C CE2 . PHE   A  218 ? 0.35033 0.35033 0.35033 0.00000  0.00000  0.00000  218 PHE   I CE2 
1316  C CZ  . PHE   A  218 ? 0.26491 0.26491 0.26491 0.00000  0.00000  0.00000  218 PHE   I CZ  
1317  N N   . ARG   A  219 ? 0.51988 0.51988 0.51988 0.00000  0.00000  0.00000  219 ARG   I N   
1318  C CA  . ARG   A  219 ? 0.57473 0.57473 0.57473 0.00000  0.00000  0.00000  219 ARG   I CA  
1319  C C   . ARG   A  219 ? 0.53597 0.53597 0.53597 0.00000  0.00000  0.00000  219 ARG   I C   
1320  O O   . ARG   A  219 ? 0.51743 0.51743 0.51743 0.00000  0.00000  0.00000  219 ARG   I O   
1321  C CB  . ARG   A  219 ? 0.48338 0.48338 0.48338 0.00000  0.00000  0.00000  219 ARG   I CB  
1322  C CG  . ARG   A  219 ? 0.69159 0.69159 0.69159 0.00000  0.00000  0.00000  219 ARG   I CG  
1323  C CD  . ARG   A  219 ? 0.56373 0.56373 0.56373 -0.00000 0.00000  0.00000  219 ARG   I CD  
1324  N NE  . ARG   A  219 ? 0.38802 0.38802 0.38802 0.00000  0.00000  0.00000  219 ARG   I NE  
1325  C CZ  . ARG   A  219 ? 1.24808 1.24808 1.24808 -0.00000 0.00000  0.00000  219 ARG   I CZ  
1326  N NH1 . ARG   A  219 ? 0.39124 0.39124 0.39124 0.00000  0.00000  0.00000  219 ARG   I NH1 
1327  N NH2 . ARG   A  219 ? 0.28758 0.28758 0.28758 -0.00000 0.00000  0.00000  219 ARG   I NH2 
1328  N N   . ASN   A  220 ? 0.45601 0.45601 0.45601 0.00000  0.00000  0.00000  220 ASN   I N   
1329  C CA  . ASN   A  220 ? 0.53259 0.53259 0.53259 -0.00000 0.00000  0.00000  220 ASN   I CA  
1330  C C   . ASN   A  220 ? 0.49318 0.49318 0.49318 0.00000  0.00000  0.00000  220 ASN   I C   
1331  O O   . ASN   A  220 ? 0.56210 0.56210 0.56210 0.00000  0.00000  0.00000  220 ASN   I O   
1332  C CB  . ASN   A  220 ? 0.63279 0.63279 0.63279 0.00000  0.00000  0.00000  220 ASN   I CB  
1333  C CG  . ASN   A  220 ? 0.95300 0.95300 0.95300 -0.00000 -0.00000 0.00000  220 ASN   I CG  
1334  O OD1 . ASN   A  220 ? 0.63952 0.63952 0.63952 0.00000  -0.00000 0.00000  220 ASN   I OD1 
1335  N ND2 . ASN   A  220 ? 0.65579 0.65579 0.65579 -0.00000 0.00000  0.00000  220 ASN   I ND2 
1336  N N   . ARG   A  221 ? 0.44107 0.44107 0.44107 0.00000  0.00000  0.00000  221 ARG   I N   
1337  C CA  . ARG   A  221 ? 0.48340 0.48340 0.48340 0.00000  0.00000  0.00000  221 ARG   I CA  
1338  C C   . ARG   A  221 ? 0.59347 0.59347 0.59347 -0.00000 0.00000  0.00000  221 ARG   I C   
1339  O O   . ARG   A  221 ? 0.46597 0.46597 0.46597 -0.00000 0.00000  0.00000  221 ARG   I O   
1340  C CB  . ARG   A  221 ? 0.32479 0.32479 0.32479 -0.00000 0.00000  0.00000  221 ARG   I CB  
1341  C CG  . ARG   A  221 ? 0.33143 0.33143 0.33143 -0.00000 0.00000  0.00000  221 ARG   I CG  
1342  C CD  . ARG   A  221 ? 0.47960 0.47960 0.47960 0.00000  0.00000  0.00000  221 ARG   I CD  
1343  N NE  . ARG   A  221 ? 0.41666 0.41666 0.41666 0.00000  0.00000  0.00000  221 ARG   I NE  
1344  C CZ  . ARG   A  221 ? 0.56268 0.56268 0.56268 -0.00000 0.00000  0.00000  221 ARG   I CZ  
1345  N NH1 . ARG   A  221 ? 0.49139 0.49139 0.49139 0.00000  0.00000  0.00000  221 ARG   I NH1 
1346  N NH2 . ARG   A  221 ? 0.37385 0.37385 0.37385 0.00000  0.00000  0.00000  221 ARG   I NH2 
1347  N N   . ASP   A  222 ? 0.43435 0.43435 0.43435 0.00000  0.00000  0.00000  222 ASP   I N   
1348  C CA  . ASP   A  222 ? 0.64944 0.64944 0.64944 -0.00000 0.00000  0.00000  222 ASP   I CA  
1349  C C   . ASP   A  222 ? 0.68397 0.68397 0.68397 0.00000  0.00000  -0.00000 222 ASP   I C   
1350  O O   . ASP   A  222 ? 0.51707 0.51707 0.51707 -0.00000 0.00000  0.00000  222 ASP   I O   
1351  C CB  . ASP   A  222 ? 0.36476 0.36476 0.36476 0.00000  0.00000  0.00000  222 ASP   I CB  
1352  C CG  . ASP   A  222 ? 0.60530 0.60530 0.60530 0.00000  0.00000  0.00000  222 ASP   I CG  
1353  O OD1 . ASP   A  222 ? 0.69351 0.69351 0.69351 0.00000  0.00000  0.00000  222 ASP   I OD1 
1354  O OD2 . ASP   A  222 ? 0.80919 0.80919 0.80919 0.00000  0.00000  0.00000  222 ASP   I OD2 
1355  N N   . ILE   A  223 ? 0.34374 0.34374 0.34374 0.00000  0.00000  0.00000  223 ILE   I N   
1356  C CA  . ILE   A  223 ? 0.46477 0.46477 0.46477 0.00000  0.00000  0.00000  223 ILE   I CA  
1357  C C   . ILE   A  223 ? 0.60673 0.60673 0.60673 -0.00000 0.00000  0.00000  223 ILE   I C   
1358  O O   . ILE   A  223 ? 0.63873 0.63873 0.63873 -0.00000 0.00000  0.00000  223 ILE   I O   
1359  C CB  . ILE   A  223 ? 0.62472 0.62472 0.62472 0.00000  -0.00000 0.00000  223 ILE   I CB  
1360  C CG1 . ILE   A  223 ? 0.38429 0.38429 0.38429 0.00000  0.00000  0.00000  223 ILE   I CG1 
1361  C CG2 . ILE   A  223 ? 0.22963 0.22963 0.22963 0.00000  0.00000  0.00000  223 ILE   I CG2 
1362  C CD1 . ILE   A  223 ? 0.42264 0.42264 0.42264 0.00000  0.00000  0.00000  223 ILE   I CD1 
1363  N N   . ASP   A  224 ? 0.49842 0.49842 0.49842 -0.00000 0.00000  0.00000  224 ASP   I N   
1364  C CA  . ASP   A  224 ? 0.51242 0.51242 0.51242 0.00000  0.00000  0.00000  224 ASP   I CA  
1365  C C   . ASP   A  224 ? 0.52353 0.52353 0.52353 0.00000  0.00000  0.00000  224 ASP   I C   
1366  O O   . ASP   A  224 ? 0.46770 0.46770 0.46770 0.00000  0.00000  0.00000  224 ASP   I O   
1367  C CB  . ASP   A  224 ? 0.46063 0.46063 0.46063 0.00000  0.00000  0.00000  224 ASP   I CB  
1368  C CG  . ASP   A  224 ? 0.62994 0.62994 0.62994 0.00000  0.00000  0.00000  224 ASP   I CG  
1369  O OD1 . ASP   A  224 ? 0.66959 0.66959 0.66959 -0.00000 0.00000  0.00000  224 ASP   I OD1 
1370  O OD2 . ASP   A  224 ? 0.62553 0.62553 0.62553 0.00000  -0.00000 0.00000  224 ASP   I OD2 
1371  N N   . ARG   A  225 ? 0.53913 0.53913 0.53913 0.00000  0.00000  -0.00000 225 ARG   I N   
1372  C CA  . ARG   A  225 ? 0.42102 0.42102 0.42102 -0.00000 0.00000  0.00000  225 ARG   I CA  
1373  C C   . ARG   A  225 ? 0.61224 0.61224 0.61224 0.00000  -0.00000 0.00000  225 ARG   I C   
1374  O O   . ARG   A  225 ? 0.53672 0.53672 0.53672 0.00000  0.00000  0.00000  225 ARG   I O   
1375  C CB  . ARG   A  225 ? 0.43434 0.43434 0.43434 0.00000  0.00000  0.00000  225 ARG   I CB  
1376  C CG  . ARG   A  225 ? 0.28518 0.28518 0.28518 0.00000  0.00000  0.00000  225 ARG   I CG  
1377  C CD  . ARG   A  225 ? 0.18435 0.18435 0.18435 0.00000  0.00000  0.00000  225 ARG   I CD  
1378  N NE  . ARG   A  225 ? 0.62998 0.62998 0.62998 0.00000  0.00000  0.00000  225 ARG   I NE  
1379  C CZ  . ARG   A  225 ? 0.43023 0.43023 0.43023 0.00000  0.00000  0.00000  225 ARG   I CZ  
1380  N NH1 . ARG   A  225 ? 0.60372 0.60372 0.60372 0.00000  0.00000  0.00000  225 ARG   I NH1 
1381  N NH2 . ARG   A  225 ? 0.32391 0.32391 0.32391 0.00000  0.00000  0.00000  225 ARG   I NH2 
1382  N N   . PRO   A  226 ? 0.53890 0.53890 0.53890 0.00000  0.00000  0.00000  226 PRO   I N   
1383  C CA  . PRO   A  226 ? 0.30842 0.30842 0.30842 0.00000  0.00000  0.00000  226 PRO   I CA  
1384  C C   . PRO   A  226 ? 0.61917 0.61917 0.61917 0.00000  0.00000  0.00000  226 PRO   I C   
1385  O O   . PRO   A  226 ? 0.40680 0.40680 0.40680 0.00000  0.00000  0.00000  226 PRO   I O   
1386  C CB  . PRO   A  226 ? 0.29721 0.29721 0.29721 -0.00000 0.00000  0.00000  226 PRO   I CB  
1387  C CG  . PRO   A  226 ? 0.28172 0.28172 0.28172 -0.00000 0.00000  0.00000  226 PRO   I CG  
1388  C CD  . PRO   A  226 ? 0.32228 0.32228 0.32228 -0.00000 0.00000  0.00000  226 PRO   I CD  
1389  N N   . VAL   A  227 ? 0.40934 0.40934 0.40934 -0.00000 0.00000  0.00000  227 VAL   I N   
1390  C CA  . VAL   A  227 ? 0.37165 0.37165 0.37165 0.00000  -0.00000 0.00000  227 VAL   I CA  
1391  C C   . VAL   A  227 ? 0.52916 0.52916 0.52916 0.00000  0.00000  0.00000  227 VAL   I C   
1392  O O   . VAL   A  227 ? 0.54170 0.54170 0.54170 -0.00000 0.00000  0.00000  227 VAL   I O   
1393  C CB  . VAL   A  227 ? 0.41182 0.41182 0.41182 -0.00000 0.00000  0.00000  227 VAL   I CB  
1394  C CG1 . VAL   A  227 ? 0.42650 0.42650 0.42650 0.00000  0.00000  0.00000  227 VAL   I CG1 
1395  C CG2 . VAL   A  227 ? 0.35133 0.35133 0.35133 0.00000  0.00000  0.00000  227 VAL   I CG2 
1396  N N   . VAL   A  228 ? 0.42056 0.42056 0.42056 0.00000  0.00000  0.00000  228 VAL   I N   
1397  C CA  . VAL   A  228 ? 0.26341 0.26341 0.26341 0.00000  0.00000  0.00000  228 VAL   I CA  
1398  C C   . VAL   A  228 ? 0.77363 0.77363 0.77363 0.00000  0.00000  0.00000  228 VAL   I C   
1399  O O   . VAL   A  228 ? 0.39711 0.39711 0.39711 0.00000  0.00000  0.00000  228 VAL   I O   
1400  C CB  . VAL   A  228 ? 0.49665 0.49665 0.49665 0.00000  0.00000  -0.00000 228 VAL   I CB  
1401  C CG1 . VAL   A  228 ? 0.32434 0.32434 0.32434 0.00000  0.00000  0.00000  228 VAL   I CG1 
1402  C CG2 . VAL   A  228 ? 0.25614 0.25614 0.25614 0.00000  0.00000  0.00000  228 VAL   I CG2 
1403  N N   . GLY   A  229 ? 0.47736 0.47736 0.47736 0.00000  0.00000  0.00000  229 GLY   I N   
1404  C CA  . GLY   A  229 ? 0.27353 0.27353 0.27353 0.00000  0.00000  0.00000  229 GLY   I CA  
1405  C C   . GLY   A  229 ? 0.36240 0.36240 0.36240 -0.00000 0.00000  0.00000  229 GLY   I C   
1406  O O   . GLY   A  229 ? 0.55493 0.55493 0.55493 0.00000  -0.00000 0.00000  229 GLY   I O   
1407  N N   . GLY   A  230 ? 0.56056 0.56056 0.56056 0.00000  0.00000  0.00000  230 GLY   I N   
1408  C CA  . GLY   A  230 ? 0.19395 0.19395 0.19395 0.00000  0.00000  0.00000  230 GLY   I CA  
1409  C C   . GLY   A  230 ? 0.79625 0.79625 0.79625 -0.00000 0.00000  0.00000  230 GLY   I C   
1410  O O   . GLY   A  230 ? 0.41639 0.41639 0.41639 -0.00000 0.00000  0.00000  230 GLY   I O   
1411  N N   . VAL   A  231 ? 0.41035 0.41035 0.41035 0.00000  0.00000  0.00000  231 VAL   I N   
1412  C CA  . VAL   A  231 ? 0.92132 0.92132 0.92132 -0.00000 0.00000  0.00000  231 VAL   I CA  
1413  C C   . VAL   A  231 ? 0.41299 0.41299 0.41299 0.00000  0.00000  0.00000  231 VAL   I C   
1414  O O   . VAL   A  231 ? 0.85770 0.85770 0.85770 -0.00000 0.00000  0.00000  231 VAL   I O   
1415  C CB  . VAL   A  231 ? 0.31926 0.31926 0.31926 -0.00000 0.00000  0.00000  231 VAL   I CB  
1416  C CG1 . VAL   A  231 ? 1.01339 1.01339 1.01339 0.00000  0.00000  0.00000  231 VAL   I CG1 
1417  C CG2 . VAL   A  231 ? 0.66571 0.66571 0.66571 0.00000  0.00000  0.00000  231 VAL   I CG2 
1418  N N   . ASN   A  232 ? 0.61198 0.61198 0.61198 -0.00000 -0.00000 0.00000  232 ASN   I N   
1419  C CA  . ASN   A  232 ? 0.47237 0.47237 0.47237 -0.00000 0.00000  0.00000  232 ASN   I CA  
1420  C C   . ASN   A  232 ? 0.62034 0.62034 0.62034 -0.00000 0.00000  0.00000  232 ASN   I C   
1421  O O   . ASN   A  232 ? 0.55964 0.55964 0.55964 -0.00000 0.00000  0.00000  232 ASN   I O   
1422  C CB  . ASN   A  232 ? 0.68443 0.68443 0.68443 0.00000  0.00000  0.00000  232 ASN   I CB  
1423  C CG  . ASN   A  232 ? 0.67964 0.67964 0.67964 -0.00000 0.00000  0.00000  232 ASN   I CG  
1424  O OD1 . ASN   A  232 ? 0.69237 0.69237 0.69237 0.00000  0.00000  0.00000  232 ASN   I OD1 
1425  N ND2 . ASN   A  232 ? 1.64386 1.64386 1.64386 0.00000  0.00000  0.00000  232 ASN   I ND2 
1426  N N   . ASN   A  233 ? 0.34161 0.34161 0.34161 0.00000  0.00000  0.00000  233 ASN   I N   
1427  C CA  . ASN   A  233 ? 0.43913 0.43913 0.43913 0.00000  0.00000  0.00000  233 ASN   I CA  
1428  C C   . ASN   A  233 ? 1.10365 1.10365 1.10365 -0.00000 0.00000  0.00000  233 ASN   I C   
1429  O O   . ASN   A  233 ? 0.41061 0.41061 0.41061 0.00000  0.00000  0.00000  233 ASN   I O   
1430  C CB  . ASN   A  233 ? 0.18473 0.18473 0.18473 0.00000  0.00000  0.00000  233 ASN   I CB  
1431  C CG  . ASN   A  233 ? 0.65828 0.65828 0.65828 -0.00000 0.00000  0.00000  233 ASN   I CG  
1432  O OD1 . ASN   A  233 ? 0.57042 0.57042 0.57042 -0.00000 0.00000  0.00000  233 ASN   I OD1 
1433  N ND2 . ASN   A  233 ? 0.51579 0.51579 0.51579 0.00000  0.00000  0.00000  233 ASN   I ND2 
1434  N N   . THR   A  234 ? 0.47861 0.47861 0.47861 0.00000  0.00000  0.00000  234 THR   I N   
1435  C CA  . THR   A  234 ? 0.67282 0.67282 0.67282 0.00000  -0.00000 0.00000  234 THR   I CA  
1436  C C   . THR   A  234 ? 0.42249 0.42249 0.42249 -0.00000 0.00000  -0.00000 234 THR   I C   
1437  O O   . THR   A  234 ? 1.06205 1.06205 1.06205 0.00000  0.00000  0.00000  234 THR   I O   
1438  C CB  . THR   A  234 ? 0.49420 0.49420 0.49420 0.00000  0.00000  0.00000  234 THR   I CB  
1439  O OG1 . THR   A  234 ? 0.62318 0.62318 0.62318 -0.00000 0.00000  0.00000  234 THR   I OG1 
1440  C CG2 . THR   A  234 ? 0.36740 0.36740 0.36740 0.00000  0.00000  0.00000  234 THR   I CG2 
1441  N N   . THR   A  235 ? 0.71927 0.71927 0.71927 0.00000  0.00000  0.00000  235 THR   I N   
1442  C CA  . THR   A  235 ? 0.49396 0.49396 0.49396 -0.00000 0.00000  0.00000  235 THR   I CA  
1443  C C   . THR   A  235 ? 0.74858 0.74858 0.74858 0.00000  0.00000  0.00000  235 THR   I C   
1444  O O   . THR   A  235 ? 0.53652 0.53652 0.53652 0.00000  0.00000  0.00000  235 THR   I O   
1445  C CB  . THR   A  235 ? 0.93914 0.93914 0.93914 0.00000  0.00000  0.00000  235 THR   I CB  
1446  O OG1 . THR   A  235 ? 0.44760 0.44760 0.44760 0.00000  0.00000  0.00000  235 THR   I OG1 
1447  C CG2 . THR   A  235 ? 0.57385 0.57385 0.57385 -0.00000 0.00000  0.00000  235 THR   I CG2 
1448  N N   . LEU   A  236 ? 0.55586 0.55586 0.55586 -0.00000 -0.00000 0.00000  236 LEU   I N   
1449  C CA  . LEU   A  236 ? 0.56184 0.56184 0.56184 0.00000  0.00000  0.00000  236 LEU   I CA  
1450  C C   . LEU   A  236 ? 0.48101 0.48101 0.48101 0.00000  0.00000  0.00000  236 LEU   I C   
1451  O O   . LEU   A  236 ? 0.50277 0.50277 0.50277 0.00000  -0.00000 0.00000  236 LEU   I O   
1452  C CB  . LEU   A  236 ? 0.47985 0.47985 0.47985 0.00000  0.00000  0.00000  236 LEU   I CB  
1453  C CG  . LEU   A  236 ? 0.57221 0.57221 0.57221 0.00000  0.00000  0.00000  236 LEU   I CG  
1454  C CD1 . LEU   A  236 ? 0.47027 0.47027 0.47027 0.00000  0.00000  0.00000  236 LEU   I CD1 
1455  C CD2 . LEU   A  236 ? 0.34964 0.34964 0.34964 -0.00000 0.00000  0.00000  236 LEU   I CD2 
1456  N N   . ILE   A  237 ? 0.45191 0.45191 0.45191 -0.00000 0.00000  0.00000  237 ILE   I N   
1457  C CA  . ILE   A  237 ? 0.36739 0.36739 0.36739 -0.00000 0.00000  0.00000  237 ILE   I CA  
1458  C C   . ILE   A  237 ? 0.50970 0.50970 0.50970 -0.00000 0.00000  0.00000  237 ILE   I C   
1459  O O   . ILE   A  237 ? 0.34407 0.34407 0.34407 0.00000  0.00000  0.00000  237 ILE   I O   
1460  C CB  . ILE   A  237 ? 0.35248 0.35248 0.35248 0.00000  0.00000  0.00000  237 ILE   I CB  
1461  C CG1 . ILE   A  237 ? 0.31350 0.31350 0.31350 0.00000  0.00000  0.00000  237 ILE   I CG1 
1462  C CG2 . ILE   A  237 ? 0.32550 0.32550 0.32550 -0.00000 0.00000  0.00000  237 ILE   I CG2 
1463  C CD1 . ILE   A  237 ? 0.33750 0.33750 0.33750 0.00000  0.00000  0.00000  237 ILE   I CD1 
1464  N N   . SER   A  238 ? 0.29057 0.29057 0.29057 0.00000  0.00000  0.00000  238 SER   I N   
1465  C CA  . SER   A  238 ? 0.37630 0.37630 0.37630 -0.00000 0.00000  0.00000  238 SER   I CA  
1466  C C   . SER   A  238 ? 0.48707 0.48707 0.48707 0.00000  0.00000  0.00000  238 SER   I C   
1467  O O   . SER   A  238 ? 0.29674 0.29674 0.29674 0.00000  0.00000  0.00000  238 SER   I O   
1468  C CB  . SER   A  238 ? 0.35683 0.35683 0.35683 0.00000  0.00000  0.00000  238 SER   I CB  
1469  O OG  . SER   A  238 ? 0.53137 0.53137 0.53137 0.00000  0.00000  0.00000  238 SER   I OG  
1470  N N   . ALA   A  239 ? 0.43485 0.43485 0.43485 -0.00000 0.00000  0.00000  239 ALA   I N   
1471  C CA  . ALA   A  239 ? 0.53687 0.53687 0.53687 -0.00000 -0.00000 0.00000  239 ALA   I CA  
1472  C C   . ALA   A  239 ? 0.23545 0.23545 0.23545 0.00000  0.00000  0.00000  239 ALA   I C   
1473  O O   . ALA   A  239 ? 0.43090 0.43090 0.43090 -0.00000 0.00000  0.00000  239 ALA   I O   
1474  C CB  . ALA   A  239 ? 0.18953 0.18953 0.18953 0.00000  0.00000  0.00000  239 ALA   I CB  
1475  N N   . ALA   A  240 ? 0.49195 0.49195 0.49195 0.00000  -0.00000 0.00000  240 ALA   I N   
1476  C CA  . ALA   A  240 ? 0.41114 0.41114 0.41114 0.00000  0.00000  0.00000  240 ALA   I CA  
1477  C C   . ALA   A  240 ? 0.49307 0.49307 0.49307 0.00000  0.00000  0.00000  240 ALA   I C   
1478  O O   . ALA   A  240 ? 0.43374 0.43374 0.43374 0.00000  0.00000  0.00000  240 ALA   I O   
1479  C CB  . ALA   A  240 ? 0.30640 0.30640 0.30640 0.00000  0.00000  0.00000  240 ALA   I CB  
1480  N N   . CYS   A  241 ? 0.30249 0.30249 0.30249 0.00000  0.00000  0.00000  241 CYS   I N   
1481  C CA  . CYS   A  241 ? 0.42795 0.42795 0.42795 0.00000  0.00000  0.00000  241 CYS   I CA  
1482  C C   . CYS   A  241 ? 0.43188 0.43188 0.43188 -0.00000 0.00000  0.00000  241 CYS   I C   
1483  O O   . CYS   A  241 ? 0.41924 0.41924 0.41924 0.00000  0.00000  0.00000  241 CYS   I O   
1484  C CB  . CYS   A  241 ? 0.44869 0.44869 0.44869 0.00000  -0.00000 0.00000  241 CYS   I CB  
1485  S SG  . CYS   A  241 ? 0.45194 0.45194 0.45194 0.00000  0.00000  0.00000  241 CYS   I SG  
1486  N N   . GLU   A  242 ? 0.49193 0.49193 0.49193 0.00000  0.00000  0.00000  242 GLU   I N   
1487  C CA  . GLU   A  242 ? 0.28508 0.28508 0.28508 -0.00000 0.00000  0.00000  242 GLU   I CA  
1488  C C   . GLU   A  242 ? 0.32184 0.32184 0.32184 0.00000  -0.00000 0.00000  242 GLU   I C   
1489  O O   . GLU   A  242 ? 0.60782 0.60782 0.60782 -0.00000 0.00000  0.00000  242 GLU   I O   
1490  C CB  . GLU   A  242 ? 0.42289 0.42289 0.42289 -0.00000 0.00000  0.00000  242 GLU   I CB  
1491  C CG  . GLU   A  242 ? 0.35112 0.35112 0.35112 0.00000  0.00000  0.00000  242 GLU   I CG  
1492  C CD  . GLU   A  242 ? 0.65514 0.65514 0.65514 0.00000  0.00000  0.00000  242 GLU   I CD  
1493  O OE1 . GLU   A  242 ? 0.39521 0.39521 0.39521 0.00000  0.00000  0.00000  242 GLU   I OE1 
1494  O OE2 . GLU   A  242 ? 0.47810 0.47810 0.47810 -0.00000 0.00000  0.00000  242 GLU   I OE2 
1495  N N   . SER   A  243 ? 0.38689 0.38689 0.38689 -0.00000 0.00000  0.00000  243 SER   I N   
1496  C CA  . SER   A  243 ? 0.53233 0.53233 0.53233 0.00000  0.00000  0.00000  243 SER   I CA  
1497  C C   . SER   A  243 ? 0.40862 0.40862 0.40862 0.00000  0.00000  0.00000  243 SER   I C   
1498  O O   . SER   A  243 ? 0.46566 0.46566 0.46566 0.00000  0.00000  0.00000  243 SER   I O   
1499  C CB  . SER   A  243 ? 0.39592 0.39592 0.39592 -0.00000 0.00000  0.00000  243 SER   I CB  
1500  O OG  . SER   A  243 ? 0.49086 0.49086 0.49086 0.00000  0.00000  0.00000  243 SER   I OG  
1501  N N   . LEU   A  244 ? 0.44406 0.44406 0.44406 0.00000  0.00000  0.00000  244 LEU   I N   
1502  C CA  . LEU   A  244 ? 0.51417 0.51417 0.51417 -0.00000 0.00000  0.00000  244 LEU   I CA  
1503  C C   . LEU   A  244 ? 0.48254 0.48254 0.48254 0.00000  0.00000  0.00000  244 LEU   I C   
1504  O O   . LEU   A  244 ? 0.56210 0.56210 0.56210 0.00000  0.00000  0.00000  244 LEU   I O   
1505  C CB  . LEU   A  244 ? 0.32252 0.32252 0.32252 -0.00000 0.00000  0.00000  244 LEU   I CB  
1506  C CG  . LEU   A  244 ? 0.55604 0.55604 0.55604 -0.00000 0.00000  0.00000  244 LEU   I CG  
1507  C CD1 . LEU   A  244 ? 0.47955 0.47955 0.47955 0.00000  0.00000  0.00000  244 LEU   I CD1 
1508  C CD2 . LEU   A  244 ? 0.39378 0.39378 0.39378 -0.00000 0.00000  0.00000  244 LEU   I CD2 
1509  N N   . SER   A  245 ? 0.87418 0.87418 0.87418 0.00000  0.00000  0.00000  245 SER   I N   
1510  C CA  . SER   A  245 ? 0.37545 0.37545 0.37545 -0.00000 0.00000  0.00000  245 SER   I CA  
1511  C C   . SER   A  245 ? 0.37603 0.37603 0.37603 0.00000  0.00000  0.00000  245 SER   I C   
1512  O O   . SER   A  245 ? 0.48955 0.48955 0.48955 0.00000  0.00000  0.00000  245 SER   I O   
1513  C CB  . SER   A  245 ? 0.41016 0.41016 0.41016 0.00000  -0.00000 0.00000  245 SER   I CB  
1514  O OG  . SER   A  245 ? 0.98734 0.98734 0.98734 0.00000  -0.00000 0.00000  245 SER   I OG  
1515  N N   . TYR   A  246 ? 0.54954 0.54954 0.54954 0.00000  0.00000  0.00000  246 TYR   I N   
1516  C CA  . TYR   A  246 ? 0.42462 0.42462 0.42462 -0.00000 0.00000  0.00000  246 TYR   I CA  
1517  C C   . TYR   A  246 ? 0.44507 0.44507 0.44507 0.00000  0.00000  0.00000  246 TYR   I C   
1518  O O   . TYR   A  246 ? 0.48383 0.48383 0.48383 0.00000  0.00000  0.00000  246 TYR   I O   
1519  C CB  . TYR   A  246 ? 0.30268 0.30268 0.30268 0.00000  0.00000  0.00000  246 TYR   I CB  
1520  C CG  . TYR   A  246 ? 0.50761 0.50761 0.50761 0.00000  0.00000  0.00000  246 TYR   I CG  
1521  C CD1 . TYR   A  246 ? 0.42028 0.42028 0.42028 0.00000  0.00000  0.00000  246 TYR   I CD1 
1522  C CD2 . TYR   A  246 ? 0.24435 0.24435 0.24435 0.00000  0.00000  0.00000  246 TYR   I CD2 
1523  C CE1 . TYR   A  246 ? 0.34097 0.34097 0.34097 -0.00000 0.00000  0.00000  246 TYR   I CE1 
1524  C CE2 . TYR   A  246 ? 0.57735 0.57735 0.57735 -0.00000 0.00000  0.00000  246 TYR   I CE2 
1525  C CZ  . TYR   A  246 ? 0.46361 0.46361 0.46361 0.00000  0.00000  0.00000  246 TYR   I CZ  
1526  O OH  . TYR   A  246 ? 0.66749 0.66749 0.66749 0.00000  0.00000  0.00000  246 TYR   I OH  
1527  N N   . ASN   A  247 ? 0.39875 0.39875 0.39875 -0.00000 0.00000  0.00000  247 ASN   I N   
1528  C CA  . ASN   A  247 ? 0.30229 0.30229 0.30229 0.00000  0.00000  0.00000  247 ASN   I CA  
1529  C C   . ASN   A  247 ? 0.39190 0.39190 0.39190 0.00000  -0.00000 0.00000  247 ASN   I C   
1530  O O   . ASN   A  247 ? 0.43287 0.43287 0.43287 -0.00000 0.00000  0.00000  247 ASN   I O   
1531  C CB  . ASN   A  247 ? 0.43196 0.43196 0.43196 -0.00000 0.00000  0.00000  247 ASN   I CB  
1532  C CG  . ASN   A  247 ? 0.40218 0.40218 0.40218 0.00000  -0.00000 0.00000  247 ASN   I CG  
1533  O OD1 . ASN   A  247 ? 0.62355 0.62355 0.62355 0.00000  0.00000  0.00000  247 ASN   I OD1 
1534  N ND2 . ASN   A  247 ? 0.38245 0.38245 0.38245 0.00000  0.00000  0.00000  247 ASN   I ND2 
1535  N N   . VAL   A  248 ? 0.43326 0.43326 0.43326 0.00000  -0.00000 0.00000  248 VAL   I N   
1536  C CA  . VAL   A  248 ? 0.50661 0.50661 0.50661 -0.00000 0.00000  0.00000  248 VAL   I CA  
1537  C C   . VAL   A  248 ? 0.39940 0.39940 0.39940 0.00000  0.00000  0.00000  248 VAL   I C   
1538  O O   . VAL   A  248 ? 0.49450 0.49450 0.49450 -0.00000 0.00000  0.00000  248 VAL   I O   
1539  C CB  . VAL   A  248 ? 0.45024 0.45024 0.45024 0.00000  0.00000  0.00000  248 VAL   I CB  
1540  C CG1 . VAL   A  248 ? 0.35900 0.35900 0.35900 0.00000  0.00000  0.00000  248 VAL   I CG1 
1541  C CG2 . VAL   A  248 ? 0.42613 0.42613 0.42613 0.00000  0.00000  0.00000  248 VAL   I CG2 
1542  N N   . SER   A  249 ? 0.49664 0.49664 0.49664 -0.00000 0.00000  0.00000  249 SER   I N   
1543  C CA  . SER   A  249 ? 0.33670 0.33670 0.33670 0.00000  0.00000  0.00000  249 SER   I CA  
1544  C C   . SER   A  249 ? 0.49602 0.49602 0.49602 0.00000  0.00000  0.00000  249 SER   I C   
1545  O O   . SER   A  249 ? 0.36686 0.36686 0.36686 0.00000  0.00000  0.00000  249 SER   I O   
1546  C CB  . SER   A  249 ? 0.33149 0.33149 0.33149 -0.00000 0.00000  0.00000  249 SER   I CB  
1547  O OG  . SER   A  249 ? 0.40359 0.40359 0.40359 -0.00000 -0.00000 0.00000  249 SER   I OG  
1548  N N   . TYR   A  250 ? 0.42291 0.42291 0.42291 -0.00000 0.00000  0.00000  250 TYR   I N   
1549  C CA  . TYR   A  250 ? 0.75407 0.75407 0.75407 -0.00000 0.00000  0.00000  250 TYR   I CA  
1550  C C   . TYR   A  250 ? 0.38999 0.38999 0.38999 0.00000  0.00000  0.00000  250 TYR   I C   
1551  O O   . TYR   A  250 ? 0.50534 0.50534 0.50534 0.00000  0.00000  0.00000  250 TYR   I O   
1552  C CB  . TYR   A  250 ? 0.38279 0.38279 0.38279 -0.00000 0.00000  0.00000  250 TYR   I CB  
1553  C CG  . TYR   A  250 ? 0.57955 0.57955 0.57955 0.00000  0.00000  0.00000  250 TYR   I CG  
1554  C CD1 . TYR   A  250 ? 0.40705 0.40705 0.40705 0.00000  0.00000  0.00000  250 TYR   I CD1 
1555  C CD2 . TYR   A  250 ? 0.35789 0.35789 0.35789 0.00000  0.00000  0.00000  250 TYR   I CD2 
1556  C CE1 . TYR   A  250 ? 0.55715 0.55715 0.55715 0.00000  0.00000  0.00000  250 TYR   I CE1 
1557  C CE2 . TYR   A  250 ? 0.49825 0.49825 0.49825 0.00000  0.00000  0.00000  250 TYR   I CE2 
1558  C CZ  . TYR   A  250 ? 0.64905 0.64905 0.64905 0.00000  -0.00000 0.00000  250 TYR   I CZ  
1559  O OH  . TYR   A  250 ? 0.71895 0.71895 0.71895 -0.00000 0.00000  0.00000  250 TYR   I OH  
1560  N N   . ASP   A  251 ? 0.46608 0.46608 0.46608 0.00000  0.00000  0.00000  251 ASP   I N   
1561  C CA  . ASP   A  251 ? 0.46935 0.46935 0.46935 0.00000  0.00000  0.00000  251 ASP   I CA  
1562  C C   . ASP   A  251 ? 0.70560 0.70560 0.70560 0.00000  0.00000  0.00000  251 ASP   I C   
1563  O O   . ASP   A  251 ? 0.51393 0.51393 0.51393 0.00000  0.00000  0.00000  251 ASP   I O   
1564  C CB  . ASP   A  251 ? 0.46087 0.46087 0.46087 0.00000  0.00000  0.00000  251 ASP   I CB  
1565  C CG  . ASP   A  251 ? 0.74217 0.74217 0.74217 0.00000  0.00000  0.00000  251 ASP   I CG  
1566  O OD1 . ASP   A  251 ? 0.57034 0.57034 0.57034 0.00000  0.00000  0.00000  251 ASP   I OD1 
1567  O OD2 . ASP   A  251 ? 0.56455 0.56455 0.56455 0.00000  0.00000  0.00000  251 ASP   I OD2 
1568  N N   . VAL   A  252 ? 0.50829 0.50829 0.50829 0.00000  0.00000  0.00000  252 VAL   I N   
1569  C CA  . VAL   A  252 ? 0.53728 0.53728 0.53728 -0.00000 0.00000  0.00000  252 VAL   I CA  
1570  C C   . VAL   A  252 ? 0.54951 0.54951 0.54951 -0.00000 0.00000  0.00000  252 VAL   I C   
1571  O O   . VAL   A  252 ? 0.57046 0.57046 0.57046 0.00000  0.00000  0.00000  252 VAL   I O   
1572  C CB  . VAL   A  252 ? 0.57334 0.57334 0.57334 0.00000  0.00000  0.00000  252 VAL   I CB  
1573  C CG1 . VAL   A  252 ? 0.42130 0.42130 0.42130 0.00000  0.00000  0.00000  252 VAL   I CG1 
1574  C CG2 . VAL   A  252 ? 0.42624 0.42624 0.42624 0.00000  0.00000  0.00000  252 VAL   I CG2 
1575  N N   . GLN   A  253 ? 0.41372 0.41372 0.41372 0.00000  0.00000  0.00000  253 GLN   I N   
1576  C CA  . GLN   A  253 ? 0.48676 0.48676 0.48676 0.00000  0.00000  0.00000  253 GLN   I CA  
1577  C C   . GLN   A  253 ? 0.63692 0.63692 0.63692 -0.00000 0.00000  0.00000  253 GLN   I C   
1578  O O   . GLN   A  253 ? 0.47772 0.47772 0.47772 -0.00000 0.00000  0.00000  253 GLN   I O   
1579  C CB  . GLN   A  253 ? 0.34276 0.34276 0.34276 -0.00000 0.00000  0.00000  253 GLN   I CB  
1580  C CG  . GLN   A  253 ? 0.81867 0.81867 0.81867 -0.00000 0.00000  0.00000  253 GLN   I CG  
1581  C CD  . GLN   A  253 ? 0.70802 0.70802 0.70802 -0.00000 0.00000  0.00000  253 GLN   I CD  
1582  O OE1 . GLN   A  253 ? 0.71918 0.71918 0.71918 0.00000  -0.00000 -0.00000 253 GLN   I OE1 
1583  N NE2 . GLN   A  253 ? 0.81074 0.81074 0.81074 0.00000  0.00000  0.00000  253 GLN   I NE2 
1584  N N   . SER   A  254 ? 0.60395 0.60395 0.60395 -0.00000 0.00000  0.00000  254 SER   I N   
1585  C CA  . SER   A  254 ? 0.34996 0.34996 0.34996 -0.00000 0.00000  0.00000  254 SER   I CA  
1586  C C   . SER   A  254 ? 0.37643 0.37643 0.37643 0.00000  0.00000  0.00000  254 SER   I C   
1587  O O   . SER   A  254 ? 0.52534 0.52534 0.52534 0.00000  0.00000  0.00000  254 SER   I O   
1588  C CB  . SER   A  254 ? 0.48632 0.48632 0.48632 -0.00000 0.00000  0.00000  254 SER   I CB  
1589  O OG  . SER   A  254 ? 0.37958 0.37958 0.37958 0.00000  0.00000  0.00000  254 SER   I OG  
1590  N N   . LEU   A  255 ? 0.42205 0.42205 0.42205 -0.00000 0.00000  0.00000  255 LEU   I N   
1591  C CA  . LEU   A  255 ? 0.45196 0.45196 0.45196 0.00000  0.00000  0.00000  255 LEU   I CA  
1592  C C   . LEU   A  255 ? 0.47145 0.47145 0.47145 0.00000  0.00000  0.00000  255 LEU   I C   
1593  O O   . LEU   A  255 ? 0.48726 0.48726 0.48726 0.00000  0.00000  0.00000  255 LEU   I O   
1594  C CB  . LEU   A  255 ? 0.48639 0.48639 0.48639 -0.00000 0.00000  0.00000  255 LEU   I CB  
1595  C CG  . LEU   A  255 ? 0.50250 0.50250 0.50250 -0.00000 0.00000  0.00000  255 LEU   I CG  
1596  C CD1 . LEU   A  255 ? 0.48712 0.48712 0.48712 -0.00000 0.00000  0.00000  255 LEU   I CD1 
1597  C CD2 . LEU   A  255 ? 0.35833 0.35833 0.35833 0.00000  0.00000  0.00000  255 LEU   I CD2 
1598  N N   . ASP   A  256 ? 0.47823 0.47823 0.47823 0.00000  0.00000  0.00000  256 ASP   I N   
1599  C CA  . ASP   A  256 ? 0.29298 0.29298 0.29298 0.00000  -0.00000 0.00000  256 ASP   I CA  
1600  C C   . ASP   A  256 ? 0.57840 0.57840 0.57840 0.00000  0.00000  0.00000  256 ASP   I C   
1601  O O   . ASP   A  256 ? 0.32513 0.32513 0.32513 0.00000  0.00000  0.00000  256 ASP   I O   
1602  C CB  . ASP   A  256 ? 0.41995 0.41995 0.41995 0.00000  0.00000  0.00000  256 ASP   I CB  
1603  C CG  . ASP   A  256 ? 0.75841 0.75841 0.75841 0.00000  0.00000  0.00000  256 ASP   I CG  
1604  O OD1 . ASP   A  256 ? 0.42671 0.42671 0.42671 -0.00000 0.00000  -0.00000 256 ASP   I OD1 
1605  O OD2 . ASP   A  256 ? 0.43533 0.43533 0.43533 -0.00000 0.00000  0.00000  256 ASP   I OD2 
1606  N N   . THR   A  257 ? 0.37448 0.37448 0.37448 0.00000  0.00000  0.00000  257 THR   I N   
1607  C CA  . THR   A  257 ? 0.73152 0.73152 0.73152 0.00000  0.00000  0.00000  257 THR   I CA  
1608  C C   . THR   A  257 ? 0.30239 0.30239 0.30239 0.00000  0.00000  0.00000  257 THR   I C   
1609  O O   . THR   A  257 ? 0.58075 0.58075 0.58075 0.00000  0.00000  0.00000  257 THR   I O   
1610  C CB  . THR   A  257 ? 0.39149 0.39149 0.39149 0.00000  0.00000  0.00000  257 THR   I CB  
1611  O OG1 . THR   A  257 ? 0.67915 0.67915 0.67915 0.00000  0.00000  0.00000  257 THR   I OG1 
1612  C CG2 . THR   A  257 ? 0.53822 0.53822 0.53822 -0.00000 0.00000  0.00000  257 THR   I CG2 
1613  N N   . LEU   A  258 ? 0.57002 0.57002 0.57002 -0.00000 0.00000  0.00000  258 LEU   I N   
1614  C CA  . LEU   A  258 ? 0.38568 0.38568 0.38568 0.00000  0.00000  0.00000  258 LEU   I CA  
1615  C C   . LEU   A  258 ? 0.73065 0.73065 0.73065 -0.00000 0.00000  0.00000  258 LEU   I C   
1616  O O   . LEU   A  258 ? 0.77256 0.77256 0.77256 0.00000  0.00000  0.00000  258 LEU   I O   
1617  C CB  . LEU   A  258 ? 0.38733 0.38733 0.38733 -0.00000 0.00000  0.00000  258 LEU   I CB  
1618  C CG  . LEU   A  258 ? 0.33487 0.33487 0.33487 -0.00000 0.00000  0.00000  258 LEU   I CG  
1619  C CD1 . LEU   A  258 ? 0.42593 0.42593 0.42593 0.00000  0.00000  0.00000  258 LEU   I CD1 
1620  C CD2 . LEU   A  258 ? 0.28944 0.28944 0.28944 -0.00000 0.00000  0.00000  258 LEU   I CD2 
1621  N N   . VAL   A  259 ? 0.58054 0.58054 0.58054 -0.00000 0.00000  0.00000  259 VAL   I N   
1622  C CA  . VAL   A  259 ? 0.62281 0.62281 0.62281 -0.00000 0.00000  0.00000  259 VAL   I CA  
1623  C C   . VAL   A  259 ? 1.43526 1.43526 1.43526 -0.00000 0.00000  0.00000  259 VAL   I C   
1624  O O   . VAL   A  259 ? 0.56778 0.56778 0.56778 0.00000  0.00000  0.00000  259 VAL   I O   
1625  C CB  . VAL   A  259 ? 0.87205 0.87205 0.87205 -0.00000 0.00000  0.00000  259 VAL   I CB  
1626  C CG1 . VAL   A  259 ? 0.39239 0.39239 0.39239 0.00000  -0.00000 0.00000  259 VAL   I CG1 
1627  C CG2 . VAL   A  259 ? 0.70114 0.70114 0.70114 0.00000  0.00000  0.00000  259 VAL   I CG2 
1628  N N   . PHE   A  260 ? 0.46685 0.46685 0.46685 -0.00000 0.00000  0.00000  260 PHE   I N   
1629  C CA  . PHE   A  260 ? 1.23351 1.23351 1.23351 0.00000  0.00000  0.00000  260 PHE   I CA  
1630  C C   . PHE   A  260 ? 0.68990 0.68990 0.68990 -0.00000 0.00000  0.00000  260 PHE   I C   
1631  O O   . PHE   A  260 ? 1.65673 1.65673 1.65673 0.00000  0.00000  0.00000  260 PHE   I O   
1632  C CB  . PHE   A  260 ? 0.63292 0.63292 0.63292 0.00000  0.00000  0.00000  260 PHE   I CB  
1633  C CG  . PHE   A  260 ? 0.85741 0.85741 0.85741 0.00000  0.00000  0.00000  260 PHE   I CG  
1634  C CD1 . PHE   A  260 ? 0.57305 0.57305 0.57305 0.00000  -0.00000 0.00000  260 PHE   I CD1 
1635  C CD2 . PHE   A  260 ? 0.77088 0.77088 0.77088 0.00000  0.00000  0.00000  260 PHE   I CD2 
1636  C CE1 . PHE   A  260 ? 1.82707 1.82707 1.82707 0.00000  0.00000  0.00000  260 PHE   I CE1 
1637  C CE2 . PHE   A  260 ? 0.79041 0.79041 0.79041 0.00000  0.00000  0.00000  260 PHE   I CE2 
1638  C CZ  . PHE   A  260 ? 1.00169 1.00169 1.00169 0.00000  0.00000  0.00000  260 PHE   I CZ  
1639  N N   . LYS   A  261 ? 1.17126 1.17126 1.17126 0.00000  0.00000  0.00000  261 LYS   I N   
1640  C CA  . LYS   A  261 ? 1.41126 1.41126 1.41126 0.00000  0.00000  0.00000  261 LYS   I CA  
1641  C C   . LYS   A  261 ? 1.36305 1.36305 1.36305 -0.00000 0.00000  0.00000  261 LYS   I C   
1642  O O   . LYS   A  261 ? 1.67845 1.67845 1.67845 -0.00000 0.00000  0.00000  261 LYS   I O   
1643  C CB  . LYS   A  261 ? 0.98891 0.98891 0.98891 -0.00000 0.00000  0.00000  261 LYS   I CB  
1644  C CG  . LYS   A  261 ? 0.48438 0.48438 0.48438 -0.00000 0.00000  0.00000  261 LYS   I CG  
1645  C CD  . LYS   A  261 ? 1.39834 1.39834 1.39834 -0.00000 0.00000  0.00000  261 LYS   I CD  
1646  C CE  . LYS   A  261 ? 1.21846 1.21846 1.21846 0.00000  0.00000  0.00000  261 LYS   I CE  
1647  N NZ  . LYS   A  261 ? 0.75082 0.75082 0.75082 0.00000  0.00000  0.00000  261 LYS   I NZ  
1648  N N   . GLY   A  262 ? 1.19472 1.19472 1.19472 0.00000  0.00000  0.00000  262 GLY   I N   
1649  C CA  . GLY   A  262 ? 0.49299 0.49299 0.49299 0.00000  0.00000  0.00000  262 GLY   I CA  
1650  C C   . GLY   A  262 ? 1.21315 1.21315 1.21315 0.00000  0.00000  0.00000  262 GLY   I C   
1651  O O   . GLY   A  262 ? 1.12860 1.12860 1.12860 -0.00000 0.00000  0.00000  262 GLY   I O   
1652  N N   . GLU   A  263 ? 0.68377 0.68377 0.68377 0.00000  0.00000  0.00000  263 GLU   I N   
1653  C CA  . GLU   A  263 ? 1.11948 1.11948 1.11948 0.00000  -0.00000 0.00000  263 GLU   I CA  
1654  C C   . GLU   A  263 ? 1.24747 1.24747 1.24747 0.00000  0.00000  0.00000  263 GLU   I C   
1655  O O   . GLU   A  263 ? 0.80205 0.80205 0.80205 0.00000  0.00000  0.00000  263 GLU   I O   
1656  C CB  . GLU   A  263 ? 0.66379 0.66379 0.66379 0.00000  0.00000  0.00000  263 GLU   I CB  
1657  C CG  . GLU   A  263 ? 1.11506 1.11506 1.11506 -0.00000 0.00000  0.00000  263 GLU   I CG  
1658  C CD  . GLU   A  263 ? 1.02956 1.02956 1.02956 0.00000  0.00000  0.00000  263 GLU   I CD  
1659  O OE1 . GLU   A  263 ? 0.65399 0.65399 0.65399 0.00000  0.00000  0.00000  263 GLU   I OE1 
1660  O OE2 . GLU   A  263 ? 0.82920 0.82920 0.82920 0.00000  0.00000  0.00000  263 GLU   I OE2 
1661  N N   . THR   A  264 ? 0.55509 0.55509 0.55509 -0.00000 0.00000  0.00000  264 THR   I N   
1662  C CA  . THR   A  264 ? 0.37181 0.37181 0.37181 0.00000  0.00000  0.00000  264 THR   I CA  
1663  C C   . THR   A  264 ? 0.56494 0.56494 0.56494 0.00000  0.00000  0.00000  264 THR   I C   
1664  O O   . THR   A  264 ? 0.45197 0.45197 0.45197 -0.00000 0.00000  0.00000  264 THR   I O   
1665  C CB  . THR   A  264 ? 0.63583 0.63583 0.63583 0.00000  0.00000  0.00000  264 THR   I CB  
1666  O OG1 . THR   A  264 ? 1.28265 1.28265 1.28265 -0.00000 0.00000  0.00000  264 THR   I OG1 
1667  C CG2 . THR   A  264 ? 0.47103 0.47103 0.47103 -0.00000 0.00000  0.00000  264 THR   I CG2 
1668  N N   . TYR   A  265 ? 0.44494 0.44494 0.44494 0.00000  0.00000  0.00000  265 TYR   I N   
1669  C CA  . TYR   A  265 ? 0.32480 0.32480 0.32480 0.00000  0.00000  0.00000  265 TYR   I CA  
1670  C C   . TYR   A  265 ? 0.38608 0.38608 0.38608 -0.00000 0.00000  0.00000  265 TYR   I C   
1671  O O   . TYR   A  265 ? 0.48765 0.48765 0.48765 -0.00000 0.00000  0.00000  265 TYR   I O   
1672  C CB  . TYR   A  265 ? 0.27508 0.27508 0.27508 -0.00000 0.00000  0.00000  265 TYR   I CB  
1673  C CG  . TYR   A  265 ? 0.51392 0.51392 0.51392 -0.00000 0.00000  0.00000  265 TYR   I CG  
1674  C CD1 . TYR   A  265 ? 0.40437 0.40437 0.40437 -0.00000 0.00000  0.00000  265 TYR   I CD1 
1675  C CD2 . TYR   A  265 ? 0.37350 0.37350 0.37350 -0.00000 0.00000  0.00000  265 TYR   I CD2 
1676  C CE1 . TYR   A  265 ? 0.50456 0.50456 0.50456 0.00000  0.00000  0.00000  265 TYR   I CE1 
1677  C CE2 . TYR   A  265 ? 0.48220 0.48220 0.48220 -0.00000 0.00000  0.00000  265 TYR   I CE2 
1678  C CZ  . TYR   A  265 ? 0.40508 0.40508 0.40508 0.00000  0.00000  0.00000  265 TYR   I CZ  
1679  O OH  . TYR   A  265 ? 0.44728 0.44728 0.44728 0.00000  0.00000  0.00000  265 TYR   I OH  
1680  N N   . SER   A  266 ? 0.37664 0.37664 0.37664 0.00000  0.00000  0.00000  266 SER   I N   
1681  C CA  . SER   A  266 ? 0.23806 0.23806 0.23806 -0.00000 0.00000  0.00000  266 SER   I CA  
1682  C C   . SER   A  266 ? 0.40914 0.40914 0.40914 0.00000  0.00000  0.00000  266 SER   I C   
1683  O O   . SER   A  266 ? 0.28935 0.28935 0.28935 0.00000  0.00000  0.00000  266 SER   I O   
1684  C CB  . SER   A  266 ? 0.26037 0.26037 0.26037 -0.00000 0.00000  0.00000  266 SER   I CB  
1685  O OG  . SER   A  266 ? 0.39398 0.39398 0.39398 0.00000  0.00000  0.00000  266 SER   I OG  
1686  N N   . LEU   A  267 ? 0.28737 0.28737 0.28737 0.00000  -0.00000 0.00000  267 LEU   I N   
1687  C CA  . LEU   A  267 ? 0.40877 0.40877 0.40877 -0.00000 0.00000  0.00000  267 LEU   I CA  
1688  C C   . LEU   A  267 ? 0.27932 0.27932 0.27932 0.00000  0.00000  0.00000  267 LEU   I C   
1689  O O   . LEU   A  267 ? 0.47685 0.47685 0.47685 0.00000  0.00000  0.00000  267 LEU   I O   
1690  C CB  . LEU   A  267 ? 0.19926 0.19926 0.19926 -0.00000 0.00000  0.00000  267 LEU   I CB  
1691  C CG  . LEU   A  267 ? 0.44750 0.44750 0.44750 0.00000  0.00000  0.00000  267 LEU   I CG  
1692  C CD1 . LEU   A  267 ? 0.34715 0.34715 0.34715 -0.00000 0.00000  0.00000  267 LEU   I CD1 
1693  C CD2 . LEU   A  267 ? 0.27478 0.27478 0.27478 -0.00000 0.00000  0.00000  267 LEU   I CD2 
1694  N N   . LYS   A  268 ? 0.53870 0.53870 0.53870 -0.00000 0.00000  0.00000  268 LYS   I N   
1695  C CA  . LYS   A  268 ? 0.27090 0.27090 0.27090 0.00000  0.00000  0.00000  268 LYS   I CA  
1696  C C   . LYS   A  268 ? 0.51068 0.51068 0.51068 0.00000  0.00000  0.00000  268 LYS   I C   
1697  O O   . LYS   A  268 ? 0.24625 0.24625 0.24625 0.00000  0.00000  0.00000  268 LYS   I O   
1698  C CB  . LYS   A  268 ? 0.35205 0.35205 0.35205 0.00000  0.00000  0.00000  268 LYS   I CB  
1699  C CG  . LYS   A  268 ? 0.51562 0.51562 0.51562 0.00000  0.00000  0.00000  268 LYS   I CG  
1700  C CD  . LYS   A  268 ? 0.43457 0.43457 0.43457 0.00000  0.00000  0.00000  268 LYS   I CD  
1701  C CE  . LYS   A  268 ? 0.59394 0.59394 0.59394 -0.00000 0.00000  0.00000  268 LYS   I CE  
1702  N NZ  . LYS   A  268 ? 0.55319 0.55319 0.55319 -0.00000 0.00000  0.00000  268 LYS   I NZ  
1703  N N   . HIS   A  269 ? 0.38679 0.38679 0.38679 -0.00000 0.00000  0.00000  269 HIS   I N   
1704  C CA  . HIS   A  269 ? 0.19051 0.19051 0.19051 0.00000  0.00000  0.00000  269 HIS   I CA  
1705  C C   . HIS   A  269 ? 0.50626 0.50626 0.50626 -0.00000 0.00000  0.00000  269 HIS   I C   
1706  O O   . HIS   A  269 ? 0.28761 0.28761 0.28761 0.00000  0.00000  0.00000  269 HIS   I O   
1707  C CB  . HIS   A  269 ? 0.28755 0.28755 0.28755 0.00000  0.00000  0.00000  269 HIS   I CB  
1708  C CG  . HIS   A  269 ? 0.33880 0.33880 0.33880 0.00000  -0.00000 -0.00000 269 HIS   I CG  
1709  N ND1 . HIS   A  269 ? 0.60939 0.60939 0.60939 0.00000  0.00000  0.00000  269 HIS   I ND1 
1710  C CD2 . HIS   A  269 ? 0.43094 0.43094 0.43094 0.00000  0.00000  0.00000  269 HIS   I CD2 
1711  C CE1 . HIS   A  269 ? 0.29557 0.29557 0.29557 -0.00000 0.00000  0.00000  269 HIS   I CE1 
1712  N NE2 . HIS   A  269 ? 0.49247 0.49247 0.49247 -0.00000 0.00000  0.00000  269 HIS   I NE2 
1713  N N   . LEU   A  270 ? 0.30020 0.30020 0.30020 0.00000  0.00000  0.00000  270 LEU   I N   
1714  C CA  . LEU   A  270 ? 0.24010 0.24010 0.24010 -0.00000 0.00000  0.00000  270 LEU   I CA  
1715  C C   . LEU   A  270 ? 0.28681 0.28681 0.28681 0.00000  0.00000  0.00000  270 LEU   I C   
1716  O O   . LEU   A  270 ? 0.33185 0.33185 0.33185 -0.00000 0.00000  0.00000  270 LEU   I O   
1717  C CB  . LEU   A  270 ? 0.32523 0.32523 0.32523 0.00000  0.00000  0.00000  270 LEU   I CB  
1718  C CG  . LEU   A  270 ? 0.28802 0.28802 0.28802 0.00000  0.00000  0.00000  270 LEU   I CG  
1719  C CD1 . LEU   A  270 ? 0.25933 0.25933 0.25933 -0.00000 -0.00000 0.00000  270 LEU   I CD1 
1720  C CD2 . LEU   A  270 ? 0.36059 0.36059 0.36059 -0.00000 0.00000  0.00000  270 LEU   I CD2 
1721  N N   . LEU   A  271 ? 0.35187 0.35187 0.35187 0.00000  0.00000  0.00000  271 LEU   I N   
1722  C CA  . LEU   A  271 ? 0.30915 0.30915 0.30915 0.00000  -0.00000 0.00000  271 LEU   I CA  
1723  C C   . LEU   A  271 ? 0.41595 0.41595 0.41595 -0.00000 0.00000  0.00000  271 LEU   I C   
1724  O O   . LEU   A  271 ? 0.28376 0.28376 0.28376 0.00000  0.00000  0.00000  271 LEU   I O   
1725  C CB  . LEU   A  271 ? 0.18836 0.18836 0.18836 -0.00000 0.00000  0.00000  271 LEU   I CB  
1726  C CG  . LEU   A  271 ? 0.35414 0.35414 0.35414 -0.00000 0.00000  0.00000  271 LEU   I CG  
1727  C CD1 . LEU   A  271 ? 0.24163 0.24163 0.24163 0.00000  0.00000  0.00000  271 LEU   I CD1 
1728  C CD2 . LEU   A  271 ? 0.15964 0.15964 0.15964 -0.00000 0.00000  0.00000  271 LEU   I CD2 
1729  N N   . ASN   A  272 ? 0.34992 0.34992 0.34992 0.00000  0.00000  0.00000  272 ASN   I N   
1730  C CA  . ASN   A  272 ? 0.24861 0.24861 0.24861 0.00000  0.00000  0.00000  272 ASN   I CA  
1731  C C   . ASN   A  272 ? 0.40232 0.40232 0.40232 0.00000  0.00000  0.00000  272 ASN   I C   
1732  O O   . ASN   A  272 ? 0.48837 0.48837 0.48837 0.00000  0.00000  0.00000  272 ASN   I O   
1733  C CB  . ASN   A  272 ? 0.52610 0.52610 0.52610 -0.00000 0.00000  0.00000  272 ASN   I CB  
1734  C CG  . ASN   A  272 ? 0.40567 0.40567 0.40567 0.00000  0.00000  0.00000  272 ASN   I CG  
1735  O OD1 . ASN   A  272 ? 0.40318 0.40318 0.40318 0.00000  0.00000  0.00000  272 ASN   I OD1 
1736  N ND2 . ASN   A  272 ? 0.48460 0.48460 0.48460 0.00000  -0.00000 0.00000  272 ASN   I ND2 
1737  N N   . ASN   A  273 ? 0.40671 0.40671 0.40671 0.00000  -0.00000 0.00000  273 ASN   I N   
1738  C CA  . ASN   A  273 ? 0.52205 0.52205 0.52205 0.00000  0.00000  0.00000  273 ASN   I CA  
1739  C C   . ASN   A  273 ? 0.37018 0.37018 0.37018 0.00000  0.00000  0.00000  273 ASN   I C   
1740  O O   . ASN   A  273 ? 0.48158 0.48158 0.48158 0.00000  0.00000  0.00000  273 ASN   I O   
1741  C CB  . ASN   A  273 ? 0.45225 0.45225 0.45225 0.00000  0.00000  0.00000  273 ASN   I CB  
1742  C CG  . ASN   A  273 ? 0.91457 0.91457 0.91457 0.00000  0.00000  0.00000  273 ASN   I CG  
1743  O OD1 . ASN   A  273 ? 0.98343 0.98343 0.98343 0.00000  0.00000  0.00000  273 ASN   I OD1 
1744  N ND2 . ASN   A  273 ? 0.94828 0.94828 0.94828 0.00000  0.00000  0.00000  273 ASN   I ND2 
1745  N N   . ASP   A  274 ? 0.44249 0.44249 0.44249 0.00000  0.00000  0.00000  274 ASP   I N   
1746  C CA  . ASP   A  274 ? 0.40726 0.40726 0.40726 0.00000  0.00000  0.00000  274 ASP   I CA  
1747  C C   . ASP   A  274 ? 0.33631 0.33631 0.33631 -0.00000 0.00000  0.00000  274 ASP   I C   
1748  O O   . ASP   A  274 ? 0.34682 0.34682 0.34682 0.00000  0.00000  0.00000  274 ASP   I O   
1749  C CB  . ASP   A  274 ? 0.36409 0.36409 0.36409 -0.00000 0.00000  0.00000  274 ASP   I CB  
1750  C CG  . ASP   A  274 ? 0.48606 0.48606 0.48606 0.00000  0.00000  0.00000  274 ASP   I CG  
1751  O OD1 . ASP   A  274 ? 0.59333 0.59333 0.59333 0.00000  0.00000  0.00000  274 ASP   I OD1 
1752  O OD2 . ASP   A  274 ? 0.76714 0.76714 0.76714 -0.00000 -0.00000 0.00000  274 ASP   I OD2 
1753  N N   . PRO   A  275 ? 0.49969 0.49969 0.49969 -0.00000 0.00000  0.00000  275 PRO   I N   
1754  C CA  . PRO   A  275 ? 0.24604 0.24604 0.24604 0.00000  0.00000  0.00000  275 PRO   I CA  
1755  C C   . PRO   A  275 ? 0.36765 0.36765 0.36765 0.00000  0.00000  0.00000  275 PRO   I C   
1756  O O   . PRO   A  275 ? 0.53629 0.53629 0.53629 0.00000  0.00000  0.00000  275 PRO   I O   
1757  C CB  . PRO   A  275 ? 0.27424 0.27424 0.27424 0.00000  0.00000  0.00000  275 PRO   I CB  
1758  C CG  . PRO   A  275 ? 0.30015 0.30015 0.30015 0.00000  0.00000  0.00000  275 PRO   I CG  
1759  C CD  . PRO   A  275 ? 0.35002 0.35002 0.35002 0.00000  0.00000  -0.00000 275 PRO   I CD  
1760  N N   . PHE   A  276 ? 0.43018 0.43018 0.43018 0.00000  0.00000  0.00000  276 PHE   I N   
1761  C CA  . PHE   A  276 ? 0.30774 0.30774 0.30774 -0.00000 0.00000  0.00000  276 PHE   I CA  
1762  C C   . PHE   A  276 ? 0.52419 0.52419 0.52419 0.00000  0.00000  0.00000  276 PHE   I C   
1763  O O   . PHE   A  276 ? 0.47174 0.47174 0.47174 0.00000  0.00000  0.00000  276 PHE   I O   
1764  C CB  . PHE   A  276 ? 0.32342 0.32342 0.32342 0.00000  0.00000  0.00000  276 PHE   I CB  
1765  C CG  . PHE   A  276 ? 0.51989 0.51989 0.51989 -0.00000 0.00000  0.00000  276 PHE   I CG  
1766  C CD1 . PHE   A  276 ? 0.43132 0.43132 0.43132 -0.00000 0.00000  0.00000  276 PHE   I CD1 
1767  C CD2 . PHE   A  276 ? 0.39416 0.39416 0.39416 0.00000  0.00000  0.00000  276 PHE   I CD2 
1768  C CE1 . PHE   A  276 ? 0.58050 0.58050 0.58050 0.00000  0.00000  0.00000  276 PHE   I CE1 
1769  C CE2 . PHE   A  276 ? 0.62880 0.62880 0.62880 -0.00000 0.00000  0.00000  276 PHE   I CE2 
1770  C CZ  . PHE   A  276 ? 0.50841 0.50841 0.50841 0.00000  0.00000  0.00000  276 PHE   I CZ  
1771  N N   . THR   A  277 ? 0.40457 0.40457 0.40457 0.00000  0.00000  0.00000  277 THR   I N   
1772  C CA  . THR   A  277 ? 0.47706 0.47706 0.47706 -0.00000 0.00000  0.00000  277 THR   I CA  
1773  C C   . THR   A  277 ? 0.37039 0.37039 0.37039 0.00000  0.00000  0.00000  277 THR   I C   
1774  O O   . THR   A  277 ? 0.44715 0.44715 0.44715 -0.00000 0.00000  0.00000  277 THR   I O   
1775  C CB  . THR   A  277 ? 0.33450 0.33450 0.33450 -0.00000 0.00000  0.00000  277 THR   I CB  
1776  O OG1 . THR   A  277 ? 0.41349 0.41349 0.41349 -0.00000 0.00000  0.00000  277 THR   I OG1 
1777  C CG2 . THR   A  277 ? 0.20780 0.20780 0.20780 -0.00000 0.00000  0.00000  277 THR   I CG2 
1778  N N   . PRO   A  278 ? 0.69185 0.69185 0.69185 0.00000  0.00000  0.00000  278 PRO   I N   
1779  C CA  . PRO   A  278 ? 0.34599 0.34599 0.34599 -0.00000 0.00000  0.00000  278 PRO   I CA  
1780  C C   . PRO   A  278 ? 0.52339 0.52339 0.52339 0.00000  0.00000  0.00000  278 PRO   I C   
1781  O O   . PRO   A  278 ? 0.37853 0.37853 0.37853 0.00000  0.00000  0.00000  278 PRO   I O   
1782  C CB  . PRO   A  278 ? 0.25398 0.25398 0.25398 0.00000  0.00000  0.00000  278 PRO   I CB  
1783  C CG  . PRO   A  278 ? 0.30179 0.30179 0.30179 0.00000  0.00000  0.00000  278 PRO   I CG  
1784  C CD  . PRO   A  278 ? 0.33864 0.33864 0.33864 0.00000  0.00000  0.00000  278 PRO   I CD  
1785  N N   . GLN   A  279 ? 0.40994 0.40994 0.40994 -0.00000 -0.00000 0.00000  279 GLN   I N   
1786  C CA  . GLN   A  279 ? 0.38225 0.38225 0.38225 0.00000  0.00000  0.00000  279 GLN   I CA  
1787  C C   . GLN   A  279 ? 0.55199 0.55199 0.55199 -0.00000 -0.00000 0.00000  279 GLN   I C   
1788  O O   . GLN   A  279 ? 0.53161 0.53161 0.53161 -0.00000 0.00000  0.00000  279 GLN   I O   
1789  C CB  . GLN   A  279 ? 0.34980 0.34980 0.34980 -0.00000 -0.00000 -0.00000 279 GLN   I CB  
1790  C CG  . GLN   A  279 ? 0.24218 0.24218 0.24218 0.00000  0.00000  0.00000  279 GLN   I CG  
1791  C CD  . GLN   A  279 ? 0.74278 0.74278 0.74278 -0.00000 0.00000  0.00000  279 GLN   I CD  
1792  O OE1 . GLN   A  279 ? 0.56333 0.56333 0.56333 -0.00000 0.00000  0.00000  279 GLN   I OE1 
1793  N NE2 . GLN   A  279 ? 0.44965 0.44965 0.44965 0.00000  0.00000  0.00000  279 GLN   I NE2 
1794  N N   . PHE   A  280 ? 0.40014 0.40014 0.40014 -0.00000 0.00000  0.00000  280 PHE   I N   
1795  C CA  . PHE   A  280 ? 0.42012 0.42012 0.42012 -0.00000 0.00000  0.00000  280 PHE   I CA  
1796  C C   . PHE   A  280 ? 0.39887 0.39887 0.39887 0.00000  0.00000  0.00000  280 PHE   I C   
1797  O O   . PHE   A  280 ? 0.43273 0.43273 0.43273 -0.00000 0.00000  0.00000  280 PHE   I O   
1798  C CB  . PHE   A  280 ? 0.19106 0.19106 0.19106 -0.00000 0.00000  0.00000  280 PHE   I CB  
1799  C CG  . PHE   A  280 ? 0.57007 0.57007 0.57007 0.00000  0.00000  0.00000  280 PHE   I CG  
1800  C CD1 . PHE   A  280 ? 0.32563 0.32563 0.32563 0.00000  -0.00000 0.00000  280 PHE   I CD1 
1801  C CD2 . PHE   A  280 ? 0.20309 0.20309 0.20309 0.00000  0.00000  0.00000  280 PHE   I CD2 
1802  C CE1 . PHE   A  280 ? 0.51203 0.51203 0.51203 0.00000  0.00000  0.00000  280 PHE   I CE1 
1803  C CE2 . PHE   A  280 ? 0.50331 0.50331 0.50331 -0.00000 0.00000  0.00000  280 PHE   I CE2 
1804  C CZ  . PHE   A  280 ? 0.40673 0.40673 0.40673 0.00000  0.00000  0.00000  280 PHE   I CZ  
1805  N N   . GLU   A  281 ? 0.40285 0.40285 0.40285 0.00000  0.00000  0.00000  281 GLU   I N   
1806  C CA  . GLU   A  281 ? 0.56553 0.56553 0.56553 -0.00000 0.00000  0.00000  281 GLU   I CA  
1807  C C   . GLU   A  281 ? 0.27736 0.27736 0.27736 -0.00000 0.00000  0.00000  281 GLU   I C   
1808  O O   . GLU   A  281 ? 0.52683 0.52683 0.52683 0.00000  -0.00000 0.00000  281 GLU   I O   
1809  C CB  . GLU   A  281 ? 0.31875 0.31875 0.31875 0.00000  0.00000  0.00000  281 GLU   I CB  
1810  C CG  . GLU   A  281 ? 0.72376 0.72376 0.72376 0.00000  0.00000  0.00000  281 GLU   I CG  
1811  C CD  . GLU   A  281 ? 1.58761 1.58761 1.58761 0.00000  0.00000  0.00000  281 GLU   I CD  
1812  O OE1 . GLU   A  281 ? 0.56356 0.56356 0.56356 0.00000  0.00000  0.00000  281 GLU   I OE1 
1813  O OE2 . GLU   A  281 ? 0.76588 0.76588 0.76588 0.00000  0.00000  0.00000  281 GLU   I OE2 
1814  N N   . HIS   A  282 ? 0.42638 0.42638 0.42638 0.00000  0.00000  0.00000  282 HIS   I N   
1815  C CA  . HIS   A  282 ? 0.72509 0.72509 0.72509 -0.00000 0.00000  0.00000  282 HIS   I CA  
1816  C C   . HIS   A  282 ? 0.56781 0.56781 0.56781 0.00000  0.00000  0.00000  282 HIS   I C   
1817  O O   . HIS   A  282 ? 0.63400 0.63400 0.63400 0.00000  0.00000  0.00000  282 HIS   I O   
1818  C CB  . HIS   A  282 ? 0.31357 0.31357 0.31357 0.00000  0.00000  0.00000  282 HIS   I CB  
1819  C CG  . HIS   A  282 ? 0.90552 0.90552 0.90552 -0.00000 0.00000  0.00000  282 HIS   I CG  
1820  N ND1 . HIS   A  282 ? 0.71188 0.71188 0.71188 -0.00000 0.00000  0.00000  282 HIS   I ND1 
1821  C CD2 . HIS   A  282 ? 0.40231 0.40231 0.40231 0.00000  0.00000  0.00000  282 HIS   I CD2 
1822  C CE1 . HIS   A  282 ? 0.50796 0.50796 0.50796 0.00000  0.00000  0.00000  282 HIS   I CE1 
1823  N NE2 . HIS   A  282 ? 0.65942 0.65942 0.65942 0.00000  0.00000  0.00000  282 HIS   I NE2 
1824  N N   . GLY   A  283 ? 0.57595 0.57595 0.57595 -0.00000 -0.00000 0.00000  283 GLY   I N   
1825  C CA  . GLY   A  283 ? 0.31705 0.31705 0.31705 0.00000  0.00000  0.00000  283 GLY   I CA  
1826  C C   . GLY   A  283 ? 0.47125 0.47125 0.47125 0.00000  0.00000  0.00000  283 GLY   I C   
1827  O O   . GLY   A  283 ? 0.45912 0.45912 0.45912 0.00000  0.00000  0.00000  283 GLY   I O   
1828  N N   . SER   A  284 ? 0.36283 0.36283 0.36283 -0.00000 0.00000  0.00000  284 SER   I N   
1829  C CA  . SER   A  284 ? 0.47309 0.47309 0.47309 0.00000  0.00000  0.00000  284 SER   I CA  
1830  C C   . SER   A  284 ? 0.39719 0.39719 0.39719 0.00000  0.00000  0.00000  284 SER   I C   
1831  O O   . SER   A  284 ? 0.30772 0.30772 0.30772 0.00000  0.00000  0.00000  284 SER   I O   
1832  C CB  . SER   A  284 ? 0.25836 0.25836 0.25836 -0.00000 0.00000  0.00000  284 SER   I CB  
1833  O OG  . SER   A  284 ? 0.49546 0.49546 0.49546 0.00000  0.00000  0.00000  284 SER   I OG  
1834  N N   . ILE   A  285 ? 0.28074 0.28074 0.28074 0.00000  0.00000  0.00000  285 ILE   I N   
1835  C CA  . ILE   A  285 ? 0.26481 0.26481 0.26481 -0.00000 0.00000  0.00000  285 ILE   I CA  
1836  C C   . ILE   A  285 ? 0.21614 0.21614 0.21614 -0.00000 0.00000  0.00000  285 ILE   I C   
1837  O O   . ILE   A  285 ? 0.45672 0.45672 0.45672 0.00000  0.00000  0.00000  285 ILE   I O   
1838  C CB  . ILE   A  285 ? 0.30793 0.30793 0.30793 -0.00000 -0.00000 0.00000  285 ILE   I CB  
1839  C CG1 . ILE   A  285 ? 0.26347 0.26347 0.26347 0.00000  0.00000  0.00000  285 ILE   I CG1 
1840  C CG2 . ILE   A  285 ? 0.21208 0.21208 0.21208 0.00000  0.00000  0.00000  285 ILE   I CG2 
1841  C CD1 . ILE   A  285 ? 0.36845 0.36845 0.36845 -0.00000 0.00000  0.00000  285 ILE   I CD1 
1842  N N   . LEU   A  286 ? 0.43095 0.43095 0.43095 0.00000  -0.00000 0.00000  286 LEU   I N   
1843  C CA  . LEU   A  286 ? 0.21399 0.21399 0.21399 0.00000  0.00000  0.00000  286 LEU   I CA  
1844  C C   . LEU   A  286 ? 0.30138 0.30138 0.30138 0.00000  0.00000  0.00000  286 LEU   I C   
1845  O O   . LEU   A  286 ? 0.36109 0.36109 0.36109 -0.00000 0.00000  0.00000  286 LEU   I O   
1846  C CB  . LEU   A  286 ? 0.40632 0.40632 0.40632 0.00000  0.00000  0.00000  286 LEU   I CB  
1847  C CG  . LEU   A  286 ? 0.35139 0.35139 0.35139 0.00000  0.00000  0.00000  286 LEU   I CG  
1848  C CD1 . LEU   A  286 ? 0.28756 0.28756 0.28756 -0.00000 0.00000  0.00000  286 LEU   I CD1 
1849  C CD2 . LEU   A  286 ? 0.35389 0.35389 0.35389 0.00000  0.00000  0.00000  286 LEU   I CD2 
1850  N N   . GLN   A  287 ? 0.24737 0.24737 0.24737 0.00000  0.00000  0.00000  287 GLN   I N   
1851  C CA  . GLN   A  287 ? 0.42547 0.42547 0.42547 -0.00000 0.00000  0.00000  287 GLN   I CA  
1852  C C   . GLN   A  287 ? 0.43409 0.43409 0.43409 0.00000  0.00000  0.00000  287 GLN   I C   
1853  O O   . GLN   A  287 ? 0.35262 0.35262 0.35262 -0.00000 0.00000  0.00000  287 GLN   I O   
1854  C CB  . GLN   A  287 ? 0.28671 0.28671 0.28671 0.00000  0.00000  0.00000  287 GLN   I CB  
1855  C CG  . GLN   A  287 ? 0.38689 0.38689 0.38689 0.00000  0.00000  0.00000  287 GLN   I CG  
1856  C CD  . GLN   A  287 ? 0.35219 0.35219 0.35219 0.00000  0.00000  0.00000  287 GLN   I CD  
1857  O OE1 . GLN   A  287 ? 0.37927 0.37927 0.37927 0.00000  0.00000  0.00000  287 GLN   I OE1 
1858  N NE2 . GLN   A  287 ? 0.30299 0.30299 0.30299 0.00000  0.00000  0.00000  287 GLN   I NE2 
1859  N N   . GLY   A  288 ? 0.39706 0.39706 0.39706 -0.00000 0.00000  0.00000  288 GLY   I N   
1860  C CA  . GLY   A  288 ? 0.29358 0.29358 0.29358 0.00000  0.00000  0.00000  288 GLY   I CA  
1861  C C   . GLY   A  288 ? 0.35206 0.35206 0.35206 -0.00000 0.00000  0.00000  288 GLY   I C   
1862  O O   . GLY   A  288 ? 0.54251 0.54251 0.54251 -0.00000 0.00000  0.00000  288 GLY   I O   
1863  N N   . PHE   A  289 ? 0.44482 0.44482 0.44482 0.00000  0.00000  0.00000  289 PHE   I N   
1864  C CA  . PHE   A  289 ? 0.52781 0.52781 0.52781 0.00000  0.00000  0.00000  289 PHE   I CA  
1865  C C   . PHE   A  289 ? 0.46829 0.46829 0.46829 0.00000  0.00000  0.00000  289 PHE   I C   
1866  O O   . PHE   A  289 ? 0.49859 0.49859 0.49859 0.00000  0.00000  0.00000  289 PHE   I O   
1867  C CB  . PHE   A  289 ? 0.38901 0.38901 0.38901 0.00000  0.00000  0.00000  289 PHE   I CB  
1868  C CG  . PHE   A  289 ? 0.46099 0.46099 0.46099 -0.00000 0.00000  0.00000  289 PHE   I CG  
1869  C CD1 . PHE   A  289 ? 0.31898 0.31898 0.31898 0.00000  -0.00000 0.00000  289 PHE   I CD1 
1870  C CD2 . PHE   A  289 ? 0.45391 0.45391 0.45391 -0.00000 0.00000  0.00000  289 PHE   I CD2 
1871  C CE1 . PHE   A  289 ? 0.55509 0.55509 0.55509 0.00000  0.00000  0.00000  289 PHE   I CE1 
1872  C CE2 . PHE   A  289 ? 0.49641 0.49641 0.49641 -0.00000 -0.00000 0.00000  289 PHE   I CE2 
1873  C CZ  . PHE   A  289 ? 0.47487 0.47487 0.47487 -0.00000 0.00000  0.00000  289 PHE   I CZ  
1874  N N   . LEU   A  290 ? 0.42864 0.42864 0.42864 0.00000  0.00000  0.00000  290 LEU   I N   
1875  C CA  . LEU   A  290 ? 0.42067 0.42067 0.42067 -0.00000 0.00000  0.00000  290 LEU   I CA  
1876  C C   . LEU   A  290 ? 0.47599 0.47599 0.47599 -0.00000 0.00000  0.00000  290 LEU   I C   
1877  O O   . LEU   A  290 ? 0.72455 0.72455 0.72455 0.00000  0.00000  0.00000  290 LEU   I O   
1878  C CB  . LEU   A  290 ? 0.33375 0.33375 0.33375 0.00000  0.00000  0.00000  290 LEU   I CB  
1879  C CG  . LEU   A  290 ? 0.43196 0.43196 0.43196 0.00000  0.00000  0.00000  290 LEU   I CG  
1880  C CD1 . LEU   A  290 ? 0.40216 0.40216 0.40216 0.00000  0.00000  0.00000  290 LEU   I CD1 
1881  C CD2 . LEU   A  290 ? 0.33152 0.33152 0.33152 0.00000  0.00000  0.00000  290 LEU   I CD2 
1882  N N   . ASN   A  291 ? 0.56633 0.56633 0.56633 0.00000  0.00000  0.00000  291 ASN   I N   
1883  C CA  . ASN   A  291 ? 0.40701 0.40701 0.40701 0.00000  0.00000  0.00000  291 ASN   I CA  
1884  C C   . ASN   A  291 ? 0.46426 0.46426 0.46426 -0.00000 0.00000  0.00000  291 ASN   I C   
1885  O O   . ASN   A  291 ? 0.45942 0.45942 0.45942 -0.00000 0.00000  0.00000  291 ASN   I O   
1886  C CB  . ASN   A  291 ? 0.74972 0.74972 0.74972 0.00000  0.00000  0.00000  291 ASN   I CB  
1887  C CG  . ASN   A  291 ? 0.88865 0.88865 0.88865 0.00000  0.00000  0.00000  291 ASN   I CG  
1888  O OD1 . ASN   A  291 ? 1.46874 1.46874 1.46874 -0.00000 0.00000  0.00000  291 ASN   I OD1 
1889  N ND2 . ASN   A  291 ? 0.89771 0.89771 0.89771 -0.00000 0.00000  0.00000  291 ASN   I ND2 
1890  N N   . VAL   A  292 ? 0.49024 0.49024 0.49024 0.00000  0.00000  0.00000  292 VAL   I N   
1891  C CA  . VAL   A  292 ? 0.84451 0.84451 0.84451 0.00000  0.00000  0.00000  292 VAL   I CA  
1892  C C   . VAL   A  292 ? 0.85389 0.85389 0.85389 0.00000  0.00000  0.00000  292 VAL   I C   
1893  O O   . VAL   A  292 ? 0.63067 0.63067 0.63067 -0.00000 0.00000  0.00000  292 VAL   I O   
1894  C CB  . VAL   A  292 ? 0.82323 0.82323 0.82323 -0.00000 0.00000  0.00000  292 VAL   I CB  
1895  C CG1 . VAL   A  292 ? 0.73278 0.73278 0.73278 0.00000  0.00000  0.00000  292 VAL   I CG1 
1896  C CG2 . VAL   A  292 ? 0.63044 0.63044 0.63044 -0.00000 0.00000  -0.00000 292 VAL   I CG2 
1897  N N   . THR   A  293 ? 0.56161 0.56161 0.56161 0.00000  0.00000  -0.00000 293 THR   I N   
1898  C CA  . THR   A  293 ? 0.64253 0.64253 0.64253 0.00000  0.00000  0.00000  293 THR   I CA  
1899  C C   . THR   A  293 ? 0.98781 0.98781 0.98781 0.00000  0.00000  0.00000  293 THR   I C   
1900  O O   . THR   A  293 ? 0.82633 0.82633 0.82633 0.00000  0.00000  0.00000  293 THR   I O   
1901  C CB  . THR   A  293 ? 0.95374 0.95374 0.95374 0.00000  0.00000  0.00000  293 THR   I CB  
1902  O OG1 . THR   A  293 ? 0.67540 0.67540 0.67540 0.00000  0.00000  0.00000  293 THR   I OG1 
1903  C CG2 . THR   A  293 ? 0.55728 0.55728 0.55728 -0.00000 0.00000  0.00000  293 THR   I CG2 
1904  N N   . ALA   A  294 ? 0.48919 0.48919 0.48919 -0.00000 0.00000  0.00000  294 ALA   I N   
1905  C CA  . ALA   A  294 ? 0.40505 0.40505 0.40505 0.00000  0.00000  0.00000  294 ALA   I CA  
1906  C C   . ALA   A  294 ? 0.39807 0.39807 0.39807 0.00000  0.00000  0.00000  294 ALA   I C   
1907  O O   . ALA   A  294 ? 0.61940 0.61940 0.61940 -0.00000 0.00000  0.00000  294 ALA   I O   
1908  C CB  . ALA   A  294 ? 0.38414 0.38414 0.38414 0.00000  0.00000  0.00000  294 ALA   I CB  
1909  N N   . TYR   A  295 ? 0.49016 0.49016 0.49016 0.00000  0.00000  0.00000  295 TYR   I N   
1910  C CA  . TYR   A  295 ? 0.58448 0.58448 0.58448 0.00000  0.00000  0.00000  295 TYR   I CA  
1911  C C   . TYR   A  295 ? 0.55822 0.55822 0.55822 -0.00000 -0.00000 0.00000  295 TYR   I C   
1912  O O   . TYR   A  295 ? 0.51927 0.51927 0.51927 0.00000  0.00000  0.00000  295 TYR   I O   
1913  C CB  . TYR   A  295 ? 0.24519 0.24519 0.24519 0.00000  0.00000  0.00000  295 TYR   I CB  
1914  C CG  . TYR   A  295 ? 0.62253 0.62253 0.62253 -0.00000 -0.00000 0.00000  295 TYR   I CG  
1915  C CD1 . TYR   A  295 ? 0.47377 0.47377 0.47377 -0.00000 0.00000  0.00000  295 TYR   I CD1 
1916  C CD2 . TYR   A  295 ? 0.42138 0.42138 0.42138 0.00000  0.00000  0.00000  295 TYR   I CD2 
1917  C CE1 . TYR   A  295 ? 0.38383 0.38383 0.38383 -0.00000 0.00000  0.00000  295 TYR   I CE1 
1918  C CE2 . TYR   A  295 ? 0.35879 0.35879 0.35879 0.00000  -0.00000 0.00000  295 TYR   I CE2 
1919  C CZ  . TYR   A  295 ? 0.53975 0.53975 0.53975 0.00000  0.00000  0.00000  295 TYR   I CZ  
1920  O OH  . TYR   A  295 ? 0.42584 0.42584 0.42584 0.00000  0.00000  0.00000  295 TYR   I OH  
1921  N N   . HIS   A  296 ? 0.43388 0.43388 0.43388 -0.00000 0.00000  0.00000  296 HIS   I N   
1922  C CA  . HIS   A  296 ? 0.53809 0.53809 0.53809 0.00000  0.00000  0.00000  296 HIS   I CA  
1923  C C   . HIS   A  296 ? 0.34290 0.34290 0.34290 0.00000  0.00000  0.00000  296 HIS   I C   
1924  O O   . HIS   A  296 ? 0.41763 0.41763 0.41763 0.00000  0.00000  0.00000  296 HIS   I O   
1925  C CB  . HIS   A  296 ? 0.39861 0.39861 0.39861 -0.00000 0.00000  0.00000  296 HIS   I CB  
1926  C CG  . HIS   A  296 ? 0.52391 0.52391 0.52391 0.00000  0.00000  0.00000  296 HIS   I CG  
1927  N ND1 . HIS   A  296 ? 0.62290 0.62290 0.62290 0.00000  0.00000  0.00000  296 HIS   I ND1 
1928  C CD2 . HIS   A  296 ? 0.51690 0.51690 0.51690 0.00000  0.00000  0.00000  296 HIS   I CD2 
1929  C CE1 . HIS   A  296 ? 0.52199 0.52199 0.52199 -0.00000 0.00000  0.00000  296 HIS   I CE1 
1930  N NE2 . HIS   A  296 ? 0.69812 0.69812 0.69812 0.00000  0.00000  0.00000  296 HIS   I NE2 
1931  N N   . ARG   A  297 ? 0.37792 0.37792 0.37792 -0.00000 0.00000  0.00000  297 ARG   I N   
1932  C CA  . ARG   A  297 ? 0.31997 0.31997 0.31997 0.00000  0.00000  0.00000  297 ARG   I CA  
1933  C C   . ARG   A  297 ? 0.53499 0.53499 0.53499 -0.00000 0.00000  0.00000  297 ARG   I C   
1934  O O   . ARG   A  297 ? 0.40386 0.40386 0.40386 0.00000  0.00000  0.00000  297 ARG   I O   
1935  C CB  . ARG   A  297 ? 0.36913 0.36913 0.36913 0.00000  0.00000  0.00000  297 ARG   I CB  
1936  C CG  . ARG   A  297 ? 0.43270 0.43270 0.43270 0.00000  0.00000  0.00000  297 ARG   I CG  
1937  C CD  . ARG   A  297 ? 0.39298 0.39298 0.39298 0.00000  0.00000  0.00000  297 ARG   I CD  
1938  N NE  . ARG   A  297 ? 0.61471 0.61471 0.61471 0.00000  0.00000  0.00000  297 ARG   I NE  
1939  C CZ  . ARG   A  297 ? 0.51744 0.51744 0.51744 0.00000  0.00000  0.00000  297 ARG   I CZ  
1940  N NH1 . ARG   A  297 ? 0.62352 0.62352 0.62352 -0.00000 0.00000  0.00000  297 ARG   I NH1 
1941  N NH2 . ARG   A  297 ? 1.07062 1.07062 1.07062 0.00000  0.00000  -0.00000 297 ARG   I NH2 
1942  N N   . TRP   A  298 ? 0.36621 0.36621 0.36621 0.00000  0.00000  0.00000  298 TRP   I N   
1943  C CA  . TRP   A  298 ? 0.33896 0.33896 0.33896 -0.00000 0.00000  0.00000  298 TRP   I CA  
1944  C C   . TRP   A  298 ? 0.43927 0.43927 0.43927 0.00000  0.00000  0.00000  298 TRP   I C   
1945  O O   . TRP   A  298 ? 0.49040 0.49040 0.49040 0.00000  0.00000  0.00000  298 TRP   I O   
1946  C CB  . TRP   A  298 ? 0.26524 0.26524 0.26524 -0.00000 0.00000  0.00000  298 TRP   I CB  
1947  C CG  . TRP   A  298 ? 0.40115 0.40115 0.40115 0.00000  0.00000  0.00000  298 TRP   I CG  
1948  C CD1 . TRP   A  298 ? 0.34125 0.34125 0.34125 0.00000  0.00000  0.00000  298 TRP   I CD1 
1949  C CD2 . TRP   A  298 ? 0.26668 0.26668 0.26668 0.00000  0.00000  0.00000  298 TRP   I CD2 
1950  N NE1 . TRP   A  298 ? 0.23244 0.23244 0.23244 0.00000  0.00000  0.00000  298 TRP   I NE1 
1951  C CE2 . TRP   A  298 ? 0.31221 0.31221 0.31221 0.00000  0.00000  0.00000  298 TRP   I CE2 
1952  C CE3 . TRP   A  298 ? 0.17882 0.17882 0.17882 -0.00000 0.00000  0.00000  298 TRP   I CE3 
1953  C CZ2 . TRP   A  298 ? 0.37712 0.37712 0.37712 0.00000  0.00000  0.00000  298 TRP   I CZ2 
1954  C CZ3 . TRP   A  298 ? 0.45623 0.45623 0.45623 0.00000  -0.00000 0.00000  298 TRP   I CZ3 
1955  C CH2 . TRP   A  298 ? 0.34928 0.34928 0.34928 -0.00000 0.00000  0.00000  298 TRP   I CH2 
1956  N N   . HIS   A  299 ? 0.35499 0.35499 0.35499 0.00000  0.00000  0.00000  299 HIS   I N   
1957  C CA  . HIS   A  299 ? 0.46743 0.46743 0.46743 -0.00000 0.00000  0.00000  299 HIS   I CA  
1958  C C   . HIS   A  299 ? 0.34274 0.34274 0.34274 0.00000  0.00000  0.00000  299 HIS   I C   
1959  O O   . HIS   A  299 ? 0.36926 0.36926 0.36926 -0.00000 0.00000  0.00000  299 HIS   I O   
1960  C CB  . HIS   A  299 ? 0.20567 0.20567 0.20567 0.00000  0.00000  -0.00000 299 HIS   I CB  
1961  C CG  . HIS   A  299 ? 0.41994 0.41994 0.41994 -0.00000 0.00000  0.00000  299 HIS   I CG  
1962  N ND1 . HIS   A  299 ? 0.33186 0.33186 0.33186 0.00000  0.00000  0.00000  299 HIS   I ND1 
1963  C CD2 . HIS   A  299 ? 0.33568 0.33568 0.33568 -0.00000 0.00000  0.00000  299 HIS   I CD2 
1964  C CE1 . HIS   A  299 ? 0.50575 0.50575 0.50575 0.00000  0.00000  0.00000  299 HIS   I CE1 
1965  N NE2 . HIS   A  299 ? 0.35834 0.35834 0.35834 0.00000  0.00000  0.00000  299 HIS   I NE2 
1966  N N   . ALA   A  300 ? 0.36989 0.36989 0.36989 -0.00000 0.00000  0.00000  300 ALA   I N   
1967  C CA  . ALA   A  300 ? 0.43366 0.43366 0.43366 0.00000  0.00000  0.00000  300 ALA   I CA  
1968  C C   . ALA   A  300 ? 0.34481 0.34481 0.34481 0.00000  0.00000  0.00000  300 ALA   I C   
1969  O O   . ALA   A  300 ? 0.47400 0.47400 0.47400 0.00000  0.00000  0.00000  300 ALA   I O   
1970  C CB  . ALA   A  300 ? 0.28851 0.28851 0.28851 0.00000  0.00000  0.00000  300 ALA   I CB  
1971  N N   . PRO   A  301 ? 0.51246 0.51246 0.51246 -0.00000 0.00000  0.00000  301 PRO   I N   
1972  C CA  . PRO   A  301 ? 0.33313 0.33313 0.33313 0.00000  0.00000  0.00000  301 PRO   I CA  
1973  C C   . PRO   A  301 ? 0.59639 0.59639 0.59639 0.00000  0.00000  0.00000  301 PRO   I C   
1974  O O   . PRO   A  301 ? 0.39881 0.39881 0.39881 0.00000  0.00000  0.00000  301 PRO   I O   
1975  C CB  . PRO   A  301 ? 0.44582 0.44582 0.44582 0.00000  0.00000  0.00000  301 PRO   I CB  
1976  C CG  . PRO   A  301 ? 0.41099 0.41099 0.41099 0.00000  0.00000  0.00000  301 PRO   I CG  
1977  C CD  . PRO   A  301 ? 0.22494 0.22494 0.22494 0.00000  0.00000  0.00000  301 PRO   I CD  
1978  N N   . VAL   A  302 ? 0.32895 0.32895 0.32895 -0.00000 0.00000  0.00000  302 VAL   I N   
1979  C CA  . VAL   A  302 ? 0.64345 0.64345 0.64345 0.00000  0.00000  0.00000  302 VAL   I CA  
1980  C C   . VAL   A  302 ? 0.31939 0.31939 0.31939 0.00000  0.00000  0.00000  302 VAL   I C   
1981  O O   . VAL   A  302 ? 0.53054 0.53054 0.53054 0.00000  0.00000  0.00000  302 VAL   I O   
1982  C CB  . VAL   A  302 ? 0.31632 0.31632 0.31632 -0.00000 0.00000  0.00000  302 VAL   I CB  
1983  C CG1 . VAL   A  302 ? 0.62367 0.62367 0.62367 -0.00000 0.00000  0.00000  302 VAL   I CG1 
1984  C CG2 . VAL   A  302 ? 0.29970 0.29970 0.29970 0.00000  0.00000  0.00000  302 VAL   I CG2 
1985  N N   . ASN   A  303 ? 0.57032 0.57032 0.57032 -0.00000 0.00000  0.00000  303 ASN   I N   
1986  C CA  . ASN   A  303 ? 0.37872 0.37872 0.37872 -0.00000 0.00000  0.00000  303 ASN   I CA  
1987  C C   . ASN   A  303 ? 0.62319 0.62319 0.62319 0.00000  0.00000  0.00000  303 ASN   I C   
1988  O O   . ASN   A  303 ? 0.56622 0.56622 0.56622 0.00000  -0.00000 0.00000  303 ASN   I O   
1989  C CB  . ASN   A  303 ? 0.61717 0.61717 0.61717 -0.00000 0.00000  0.00000  303 ASN   I CB  
1990  C CG  . ASN   A  303 ? 0.52521 0.52521 0.52521 -0.00000 0.00000  0.00000  303 ASN   I CG  
1991  O OD1 . ASN   A  303 ? 0.58482 0.58482 0.58482 -0.00000 0.00000  0.00000  303 ASN   I OD1 
1992  N ND2 . ASN   A  303 ? 0.56016 0.56016 0.56016 0.00000  0.00000  0.00000  303 ASN   I ND2 
1993  N N   . GLY   A  304 ? 0.47400 0.47400 0.47400 -0.00000 0.00000  0.00000  304 GLY   I N   
1994  C CA  . GLY   A  304 ? 0.30647 0.30647 0.30647 0.00000  0.00000  0.00000  304 GLY   I CA  
1995  C C   . GLY   A  304 ? 0.51578 0.51578 0.51578 0.00000  0.00000  0.00000  304 GLY   I C   
1996  O O   . GLY   A  304 ? 0.55144 0.55144 0.55144 0.00000  0.00000  0.00000  304 GLY   I O   
1997  N N   . THR   A  305 ? 0.44573 0.44573 0.44573 0.00000  0.00000  0.00000  305 THR   I N   
1998  C CA  . THR   A  305 ? 0.46218 0.46218 0.46218 0.00000  0.00000  0.00000  305 THR   I CA  
1999  C C   . THR   A  305 ? 0.73996 0.73996 0.73996 0.00000  0.00000  0.00000  305 THR   I C   
2000  O O   . THR   A  305 ? 0.29507 0.29507 0.29507 0.00000  0.00000  0.00000  305 THR   I O   
2001  C CB  . THR   A  305 ? 0.33071 0.33071 0.33071 0.00000  0.00000  0.00000  305 THR   I CB  
2002  O OG1 . THR   A  305 ? 0.54692 0.54692 0.54692 -0.00000 -0.00000 0.00000  305 THR   I OG1 
2003  C CG2 . THR   A  305 ? 0.32802 0.32802 0.32802 -0.00000 0.00000  0.00000  305 THR   I CG2 
2004  N N   . ILE   A  306 ? 0.29321 0.29321 0.29321 0.00000  0.00000  0.00000  306 ILE   I N   
2005  C CA  . ILE   A  306 ? 0.45564 0.45564 0.45564 0.00000  -0.00000 0.00000  306 ILE   I CA  
2006  C C   . ILE   A  306 ? 0.46374 0.46374 0.46374 0.00000  0.00000  0.00000  306 ILE   I C   
2007  O O   . ILE   A  306 ? 0.50244 0.50244 0.50244 -0.00000 0.00000  0.00000  306 ILE   I O   
2008  C CB  . ILE   A  306 ? 0.40839 0.40839 0.40839 -0.00000 0.00000  0.00000  306 ILE   I CB  
2009  C CG1 . ILE   A  306 ? 0.24884 0.24884 0.24884 0.00000  0.00000  0.00000  306 ILE   I CG1 
2010  C CG2 . ILE   A  306 ? 0.35385 0.35385 0.35385 -0.00000 0.00000  0.00000  306 ILE   I CG2 
2011  C CD1 . ILE   A  306 ? 0.33443 0.33443 0.33443 0.00000  0.00000  0.00000  306 ILE   I CD1 
2012  N N   . VAL   A  307 ? 0.42000 0.42000 0.42000 -0.00000 0.00000  0.00000  307 VAL   I N   
2013  C CA  . VAL   A  307 ? 0.34255 0.34255 0.34255 0.00000  0.00000  0.00000  307 VAL   I CA  
2014  C C   . VAL   A  307 ? 0.45296 0.45296 0.45296 0.00000  0.00000  0.00000  307 VAL   I C   
2015  O O   . VAL   A  307 ? 0.43400 0.43400 0.43400 0.00000  0.00000  0.00000  307 VAL   I O   
2016  C CB  . VAL   A  307 ? 0.54421 0.54421 0.54421 0.00000  0.00000  0.00000  307 VAL   I CB  
2017  C CG1 . VAL   A  307 ? 0.21460 0.21460 0.21460 -0.00000 0.00000  0.00000  307 VAL   I CG1 
2018  C CG2 . VAL   A  307 ? 0.35482 0.35482 0.35482 0.00000  0.00000  0.00000  307 VAL   I CG2 
2019  N N   . LYS   A  308 ? 0.59153 0.59153 0.59153 0.00000  0.00000  0.00000  308 LYS   I N   
2020  C CA  . LYS   A  308 ? 0.47272 0.47272 0.47272 0.00000  0.00000  0.00000  308 LYS   I CA  
2021  C C   . LYS   A  308 ? 0.64400 0.64400 0.64400 0.00000  0.00000  0.00000  308 LYS   I C   
2022  O O   . LYS   A  308 ? 0.43085 0.43085 0.43085 0.00000  0.00000  0.00000  308 LYS   I O   
2023  C CB  . LYS   A  308 ? 0.43240 0.43240 0.43240 0.00000  0.00000  0.00000  308 LYS   I CB  
2024  C CG  . LYS   A  308 ? 0.32273 0.32273 0.32273 0.00000  -0.00000 0.00000  308 LYS   I CG  
2025  C CD  . LYS   A  308 ? 0.46024 0.46024 0.46024 0.00000  0.00000  0.00000  308 LYS   I CD  
2026  C CE  . LYS   A  308 ? 0.71282 0.71282 0.71282 0.00000  0.00000  0.00000  308 LYS   I CE  
2027  N NZ  . LYS   A  308 ? 0.86032 0.86032 0.86032 -0.00000 0.00000  0.00000  308 LYS   I NZ  
2028  N N   . ILE   A  309 ? 0.37122 0.37122 0.37122 -0.00000 0.00000  0.00000  309 ILE   I N   
2029  C CA  . ILE   A  309 ? 0.46087 0.46087 0.46087 0.00000  0.00000  0.00000  309 ILE   I CA  
2030  C C   . ILE   A  309 ? 0.36522 0.36522 0.36522 0.00000  0.00000  0.00000  309 ILE   I C   
2031  O O   . ILE   A  309 ? 0.47382 0.47382 0.47382 -0.00000 0.00000  0.00000  309 ILE   I O   
2032  C CB  . ILE   A  309 ? 0.26393 0.26393 0.26393 0.00000  0.00000  0.00000  309 ILE   I CB  
2033  C CG1 . ILE   A  309 ? 0.52597 0.52597 0.52597 -0.00000 0.00000  0.00000  309 ILE   I CG1 
2034  C CG2 . ILE   A  309 ? 0.29756 0.29756 0.29756 0.00000  0.00000  0.00000  309 ILE   I CG2 
2035  C CD1 . ILE   A  309 ? 0.28150 0.28150 0.28150 0.00000  0.00000  0.00000  309 ILE   I CD1 
2036  N N   . ILE   A  310 ? 0.43200 0.43200 0.43200 0.00000  0.00000  0.00000  310 ILE   I N   
2037  C CA  . ILE   A  310 ? 0.22781 0.22781 0.22781 0.00000  0.00000  0.00000  310 ILE   I CA  
2038  C C   . ILE   A  310 ? 0.44833 0.44833 0.44833 0.00000  0.00000  0.00000  310 ILE   I C   
2039  O O   . ILE   A  310 ? 0.35960 0.35960 0.35960 -0.00000 0.00000  0.00000  310 ILE   I O   
2040  C CB  . ILE   A  310 ? 0.44805 0.44805 0.44805 0.00000  0.00000  0.00000  310 ILE   I CB  
2041  C CG1 . ILE   A  310 ? 0.46186 0.46186 0.46186 0.00000  0.00000  0.00000  310 ILE   I CG1 
2042  C CG2 . ILE   A  310 ? 0.28892 0.28892 0.28892 -0.00000 0.00000  0.00000  310 ILE   I CG2 
2043  C CD1 . ILE   A  310 ? 0.51722 0.51722 0.51722 -0.00000 0.00000  0.00000  310 ILE   I CD1 
2044  N N   . ASN   A  311 ? 0.43150 0.43150 0.43150 -0.00000 0.00000  0.00000  311 ASN   I N   
2045  C CA  . ASN   A  311 ? 0.39112 0.39112 0.39112 0.00000  0.00000  0.00000  311 ASN   I CA  
2046  C C   . ASN   A  311 ? 0.25633 0.25633 0.25633 0.00000  0.00000  0.00000  311 ASN   I C   
2047  O O   . ASN   A  311 ? 0.59845 0.59845 0.59845 0.00000  0.00000  0.00000  311 ASN   I O   
2048  C CB  . ASN   A  311 ? 0.19804 0.19804 0.19804 0.00000  0.00000  0.00000  311 ASN   I CB  
2049  C CG  . ASN   A  311 ? 0.77713 0.77713 0.77713 -0.00000 0.00000  0.00000  311 ASN   I CG  
2050  O OD1 . ASN   A  311 ? 0.52371 0.52371 0.52371 0.00000  0.00000  0.00000  311 ASN   I OD1 
2051  N ND2 . ASN   A  311 ? 0.55162 0.55162 0.55162 0.00000  0.00000  0.00000  311 ASN   I ND2 
2052  N N   . VAL   A  312 ? 0.31948 0.31948 0.31948 -0.00000 0.00000  0.00000  312 VAL   I N   
2053  C CA  . VAL   A  312 ? 0.29979 0.29979 0.29979 0.00000  0.00000  0.00000  312 VAL   I CA  
2054  C C   . VAL   A  312 ? 0.28518 0.28518 0.28518 0.00000  0.00000  0.00000  312 VAL   I C   
2055  O O   . VAL   A  312 ? 0.60058 0.60058 0.60058 0.00000  0.00000  0.00000  312 VAL   I O   
2056  C CB  . VAL   A  312 ? 0.34496 0.34496 0.34496 0.00000  0.00000  0.00000  312 VAL   I CB  
2057  C CG1 . VAL   A  312 ? 0.17141 0.17141 0.17141 -0.00000 0.00000  0.00000  312 VAL   I CG1 
2058  C CG2 . VAL   A  312 ? 0.25245 0.25245 0.25245 0.00000  0.00000  0.00000  312 VAL   I CG2 
2059  N N   . PRO   A  313 ? 0.43291 0.43291 0.43291 0.00000  0.00000  0.00000  313 PRO   I N   
2060  C CA  . PRO   A  313 ? 0.37824 0.37824 0.37824 0.00000  0.00000  0.00000  313 PRO   I CA  
2061  C C   . PRO   A  313 ? 0.42484 0.42484 0.42484 -0.00000 0.00000  0.00000  313 PRO   I C   
2062  O O   . PRO   A  313 ? 0.36454 0.36454 0.36454 0.00000  0.00000  0.00000  313 PRO   I O   
2063  C CB  . PRO   A  313 ? 0.16342 0.16342 0.16342 0.00000  0.00000  0.00000  313 PRO   I CB  
2064  C CG  . PRO   A  313 ? 0.23750 0.23750 0.23750 0.00000  -0.00000 0.00000  313 PRO   I CG  
2065  C CD  . PRO   A  313 ? 0.18900 0.18900 0.18900 0.00000  0.00000  0.00000  313 PRO   I CD  
2066  N N   . GLY   A  314 ? 0.35902 0.35902 0.35902 -0.00000 0.00000  0.00000  314 GLY   I N   
2067  C CA  . GLY   A  314 ? 0.26355 0.26355 0.26355 0.00000  0.00000  0.00000  314 GLY   I CA  
2068  C C   . GLY   A  314 ? 0.47838 0.47838 0.47838 -0.00000 0.00000  0.00000  314 GLY   I C   
2069  O O   . GLY   A  314 ? 0.36758 0.36758 0.36758 -0.00000 0.00000  0.00000  314 GLY   I O   
2070  N N   . THR   A  315 ? 0.41824 0.41824 0.41824 -0.00000 0.00000  0.00000  315 THR   I N   
2071  C CA  . THR   A  315 ? 0.44802 0.44802 0.44802 0.00000  0.00000  0.00000  315 THR   I CA  
2072  C C   . THR   A  315 ? 0.55353 0.55353 0.55353 -0.00000 0.00000  0.00000  315 THR   I C   
2073  O O   . THR   A  315 ? 0.45453 0.45453 0.45453 0.00000  0.00000  0.00000  315 THR   I O   
2074  C CB  . THR   A  315 ? 0.44324 0.44324 0.44324 -0.00000 0.00000  0.00000  315 THR   I CB  
2075  O OG1 . THR   A  315 ? 0.36445 0.36445 0.36445 0.00000  0.00000  0.00000  315 THR   I OG1 
2076  C CG2 . THR   A  315 ? 0.32281 0.32281 0.32281 0.00000  0.00000  0.00000  315 THR   I CG2 
2077  N N   . TYR   A  316 ? 0.46608 0.46608 0.46608 0.00000  0.00000  0.00000  316 TYR   I N   
2078  C CA  . TYR   A  316 ? 0.46051 0.46051 0.46051 -0.00000 0.00000  0.00000  316 TYR   I CA  
2079  C C   . TYR   A  316 ? 0.39750 0.39750 0.39750 0.00000  0.00000  0.00000  316 TYR   I C   
2080  O O   . TYR   A  316 ? 0.52240 0.52240 0.52240 -0.00000 0.00000  0.00000  316 TYR   I O   
2081  C CB  . TYR   A  316 ? 0.39649 0.39649 0.39649 0.00000  0.00000  0.00000  316 TYR   I CB  
2082  C CG  . TYR   A  316 ? 0.53259 0.53259 0.53259 0.00000  0.00000  0.00000  316 TYR   I CG  
2083  C CD1 . TYR   A  316 ? 0.55006 0.55006 0.55006 -0.00000 0.00000  0.00000  316 TYR   I CD1 
2084  C CD2 . TYR   A  316 ? 0.45785 0.45785 0.45785 0.00000  0.00000  0.00000  316 TYR   I CD2 
2085  C CE1 . TYR   A  316 ? 0.44416 0.44416 0.44416 -0.00000 0.00000  0.00000  316 TYR   I CE1 
2086  C CE2 . TYR   A  316 ? 0.35891 0.35891 0.35891 0.00000  0.00000  0.00000  316 TYR   I CE2 
2087  C CZ  . TYR   A  316 ? 0.58415 0.58415 0.58415 0.00000  0.00000  0.00000  316 TYR   I CZ  
2088  O OH  . TYR   A  316 ? 0.47363 0.47363 0.47363 -0.00000 0.00000  0.00000  316 TYR   I OH  
2089  N N   . PHE   A  317 ? 0.54214 0.54214 0.54214 0.00000  0.00000  0.00000  317 PHE   I N   
2090  C CA  . PHE   A  317 ? 0.30466 0.30466 0.30466 -0.00000 0.00000  0.00000  317 PHE   I CA  
2091  C C   . PHE   A  317 ? 0.57911 0.57911 0.57911 -0.00000 0.00000  0.00000  317 PHE   I C   
2092  O O   . PHE   A  317 ? 0.42626 0.42626 0.42626 0.00000  0.00000  0.00000  317 PHE   I O   
2093  C CB  . PHE   A  317 ? 0.30313 0.30313 0.30313 -0.00000 0.00000  0.00000  317 PHE   I CB  
2094  C CG  . PHE   A  317 ? 0.55825 0.55825 0.55825 0.00000  0.00000  0.00000  317 PHE   I CG  
2095  C CD1 . PHE   A  317 ? 0.31327 0.31327 0.31327 0.00000  0.00000  0.00000  317 PHE   I CD1 
2096  C CD2 . PHE   A  317 ? 0.50459 0.50459 0.50459 0.00000  0.00000  0.00000  317 PHE   I CD2 
2097  C CE1 . PHE   A  317 ? 0.50716 0.50716 0.50716 -0.00000 0.00000  0.00000  317 PHE   I CE1 
2098  C CE2 . PHE   A  317 ? 0.41330 0.41330 0.41330 0.00000  0.00000  0.00000  317 PHE   I CE2 
2099  C CZ  . PHE   A  317 ? 0.43112 0.43112 0.43112 0.00000  0.00000  0.00000  317 PHE   I CZ  
2100  N N   . ALA   A  318 ? 0.38678 0.38678 0.38678 0.00000  0.00000  0.00000  318 ALA   I N   
2101  C CA  . ALA   A  318 ? 0.34720 0.34720 0.34720 -0.00000 0.00000  0.00000  318 ALA   I CA  
2102  C C   . ALA   A  318 ? 0.40820 0.40820 0.40820 -0.00000 0.00000  0.00000  318 ALA   I C   
2103  O O   . ALA   A  318 ? 0.47047 0.47047 0.47047 -0.00000 0.00000  0.00000  318 ALA   I O   
2104  C CB  . ALA   A  318 ? 0.26516 0.26516 0.26516 -0.00000 0.00000  0.00000  318 ALA   I CB  
2105  N N   . GLN   A  319 ? 0.47143 0.47143 0.47143 -0.00000 0.00000  0.00000  319 GLN   I N   
2106  C CA  . GLN   A  319 ? 0.42686 0.42686 0.42686 0.00000  0.00000  0.00000  319 GLN   I CA  
2107  C C   . GLN   A  319 ? 0.40274 0.40274 0.40274 0.00000  0.00000  -0.00000 319 GLN   I C   
2108  O O   . GLN   A  319 ? 0.58351 0.58351 0.58351 0.00000  0.00000  0.00000  319 GLN   I O   
2109  C CB  . GLN   A  319 ? 0.42035 0.42035 0.42035 0.00000  0.00000  0.00000  319 GLN   I CB  
2110  C CG  . GLN   A  319 ? 0.52297 0.52297 0.52297 0.00000  0.00000  0.00000  319 GLN   I CG  
2111  C CD  . GLN   A  319 ? 0.38381 0.38381 0.38381 0.00000  0.00000  0.00000  319 GLN   I CD  
2112  O OE1 . GLN   A  319 ? 0.67917 0.67917 0.67917 0.00000  0.00000  0.00000  319 GLN   I OE1 
2113  N NE2 . GLN   A  319 ? 0.49535 0.49535 0.49535 0.00000  0.00000  0.00000  319 GLN   I NE2 
2114  N N   . ALA   A  320 ? 0.43200 0.43200 0.43200 -0.00000 0.00000  0.00000  320 ALA   I N   
2115  C CA  . ALA   A  320 ? 0.44144 0.44144 0.44144 -0.00000 0.00000  0.00000  320 ALA   I CA  
2116  C C   . ALA   A  320 ? 0.43818 0.43818 0.43818 0.00000  0.00000  0.00000  320 ALA   I C   
2117  O O   . ALA   A  320 ? 0.45766 0.45766 0.45766 0.00000  0.00000  0.00000  320 ALA   I O   
2118  C CB  . ALA   A  320 ? 0.23553 0.23553 0.23553 -0.00000 0.00000  0.00000  320 ALA   I CB  
2119  N N   . PRO   A  321 ? 0.62948 0.62948 0.62948 0.00000  0.00000  0.00000  321 PRO   I N   
2120  C CA  . PRO   A  321 ? 0.45089 0.45089 0.45089 -0.00000 0.00000  0.00000  321 PRO   I CA  
2121  C C   . PRO   A  321 ? 0.52289 0.52289 0.52289 0.00000  0.00000  0.00000  321 PRO   I C   
2122  O O   . PRO   A  321 ? 0.58326 0.58326 0.58326 0.00000  0.00000  0.00000  321 PRO   I O   
2123  C CB  . PRO   A  321 ? 0.36472 0.36472 0.36472 -0.00000 0.00000  0.00000  321 PRO   I CB  
2124  C CG  . PRO   A  321 ? 0.63272 0.63272 0.63272 0.00000  0.00000  0.00000  321 PRO   I CG  
2125  C CD  . PRO   A  321 ? 0.40841 0.40841 0.40841 0.00000  0.00000  0.00000  321 PRO   I CD  
2126  N N   . SER   A  322 ? 0.55863 0.55863 0.55863 0.00000  0.00000  0.00000  322 SER   I N   
2127  C CA  . SER   A  322 ? 0.55207 0.55207 0.55207 0.00000  0.00000  0.00000  322 SER   I CA  
2128  C C   . SER   A  322 ? 0.54705 0.54705 0.54705 0.00000  0.00000  0.00000  322 SER   I C   
2129  O O   . SER   A  322 ? 0.79250 0.79250 0.79250 0.00000  0.00000  0.00000  322 SER   I O   
2130  C CB  . SER   A  322 ? 0.43890 0.43890 0.43890 0.00000  0.00000  0.00000  322 SER   I CB  
2131  O OG  . SER   A  322 ? 0.75669 0.75669 0.75669 0.00000  0.00000  0.00000  322 SER   I OG  
2132  N N   . THR   A  323 ? 0.81364 0.81364 0.81364 0.00000  0.00000  0.00000  323 THR   I N   
2133  C CA  . THR   A  323 ? 0.59002 0.59002 0.59002 0.00000  0.00000  0.00000  323 THR   I CA  
2134  C C   . THR   A  323 ? 0.78601 0.78601 0.78601 0.00000  -0.00000 0.00000  323 THR   I C   
2135  O O   . THR   A  323 ? 0.56958 0.56958 0.56958 0.00000  0.00000  0.00000  323 THR   I O   
2136  C CB  . THR   A  323 ? 0.67532 0.67532 0.67532 0.00000  0.00000  0.00000  323 THR   I CB  
2137  O OG1 . THR   A  323 ? 0.69476 0.69476 0.69476 0.00000  0.00000  0.00000  323 THR   I OG1 
2138  C CG2 . THR   A  323 ? 0.44671 0.44671 0.44671 -0.00000 0.00000  0.00000  323 THR   I CG2 
2139  N N   . ILE   A  324 ? 0.53958 0.53958 0.53958 0.00000  0.00000  0.00000  324 ILE   I N   
2140  C CA  . ILE   A  324 ? 0.56169 0.56169 0.56169 0.00000  0.00000  0.00000  324 ILE   I CA  
2141  C C   . ILE   A  324 ? 0.79662 0.79662 0.79662 0.00000  0.00000  0.00000  324 ILE   I C   
2142  O O   . ILE   A  324 ? 0.70379 0.70379 0.70379 0.00000  0.00000  0.00000  324 ILE   I O   
2143  C CB  . ILE   A  324 ? 0.40982 0.40982 0.40982 0.00000  -0.00000 0.00000  324 ILE   I CB  
2144  C CG1 . ILE   A  324 ? 0.57926 0.57926 0.57926 0.00000  0.00000  0.00000  324 ILE   I CG1 
2145  C CG2 . ILE   A  324 ? 0.44202 0.44202 0.44202 0.00000  0.00000  0.00000  324 ILE   I CG2 
2146  C CD1 . ILE   A  324 ? 0.49698 0.49698 0.49698 0.00000  0.00000  0.00000  324 ILE   I CD1 
2147  N N   . GLY   A  325 ? 0.62673 0.62673 0.62673 -0.00000 0.00000  0.00000  325 GLY   I N   
2148  C CA  . GLY   A  325 ? 0.56619 0.56619 0.56619 -0.00000 0.00000  0.00000  325 GLY   I CA  
2149  C C   . GLY   A  325 ? 0.68057 0.68057 0.68057 -0.00000 0.00000  0.00000  325 GLY   I C   
2150  O O   . GLY   A  325 ? 0.74606 0.74606 0.74606 -0.00000 0.00000  0.00000  325 GLY   I O   
2151  N N   . ASP   A  326 ? 0.65269 0.65269 0.65269 -0.00000 0.00000  0.00000  326 ASP   I N   
2152  C CA  . ASP   A  326 ? 0.74393 0.74393 0.74393 0.00000  -0.00000 0.00000  326 ASP   I CA  
2153  C C   . ASP   A  326 ? 0.63216 0.63216 0.63216 -0.00000 0.00000  0.00000  326 ASP   I C   
2154  O O   . ASP   A  326 ? 0.76347 0.76347 0.76347 -0.00000 0.00000  0.00000  326 ASP   I O   
2155  C CB  . ASP   A  326 ? 0.52143 0.52143 0.52143 0.00000  0.00000  0.00000  326 ASP   I CB  
2156  C CG  . ASP   A  326 ? 0.98590 0.98590 0.98590 -0.00000 0.00000  0.00000  326 ASP   I CG  
2157  O OD1 . ASP   A  326 ? 0.80353 0.80353 0.80353 0.00000  0.00000  0.00000  326 ASP   I OD1 
2158  O OD2 . ASP   A  326 ? 0.83638 0.83638 0.83638 0.00000  0.00000  0.00000  326 ASP   I OD2 
2159  N N   . PRO   A  327 ? 0.88452 0.88452 0.88452 0.00000  0.00000  0.00000  327 PRO   I N   
2160  C CA  . PRO   A  327 ? 0.70033 0.70033 0.70033 -0.00000 0.00000  0.00000  327 PRO   I CA  
2161  C C   . PRO   A  327 ? 0.63344 0.63344 0.63344 -0.00000 0.00000  -0.00000 327 PRO   I C   
2162  O O   . PRO   A  327 ? 0.79787 0.79787 0.79787 0.00000  0.00000  0.00000  327 PRO   I O   
2163  C CB  . PRO   A  327 ? 0.44565 0.44565 0.44565 0.00000  0.00000  0.00000  327 PRO   I CB  
2164  C CG  . PRO   A  327 ? 0.63143 0.63143 0.63143 -0.00000 0.00000  0.00000  327 PRO   I CG  
2165  C CD  . PRO   A  327 ? 0.66835 0.66835 0.66835 -0.00000 0.00000  0.00000  327 PRO   I CD  
2166  N N   . ILE   A  328 ? 0.50459 0.50459 0.50459 0.00000  0.00000  0.00000  328 ILE   I N   
2167  C CA  . ILE   A  328 ? 0.50205 0.50205 0.50205 0.00000  0.00000  0.00000  328 ILE   I CA  
2168  C C   . ILE   A  328 ? 0.53112 0.53112 0.53112 -0.00000 0.00000  0.00000  328 ILE   I C   
2169  O O   . ILE   A  328 ? 0.64563 0.64563 0.64563 0.00000  -0.00000 -0.00000 328 ILE   I O   
2170  C CB  . ILE   A  328 ? 0.56822 0.56822 0.56822 -0.00000 0.00000  0.00000  328 ILE   I CB  
2171  C CG1 . ILE   A  328 ? 0.40936 0.40936 0.40936 0.00000  0.00000  0.00000  328 ILE   I CG1 
2172  C CG2 . ILE   A  328 ? 0.43120 0.43120 0.43120 0.00000  0.00000  0.00000  328 ILE   I CG2 
2173  C CD1 . ILE   A  328 ? 0.35882 0.35882 0.35882 -0.00000 0.00000  0.00000  328 ILE   I CD1 
2174  N N   . PRO   A  329 ? 0.87830 0.87830 0.87830 0.00000  0.00000  0.00000  329 PRO   I N   
2175  C CA  . PRO   A  329 ? 0.69430 0.69430 0.69430 -0.00000 0.00000  0.00000  329 PRO   I CA  
2176  C C   . PRO   A  329 ? 0.72283 0.72283 0.72283 0.00000  0.00000  0.00000  329 PRO   I C   
2177  O O   . PRO   A  329 ? 1.13256 1.13256 1.13256 -0.00000 0.00000  0.00000  329 PRO   I O   
2178  C CB  . PRO   A  329 ? 0.52789 0.52789 0.52789 0.00000  0.00000  -0.00000 329 PRO   I CB  
2179  C CG  . PRO   A  329 ? 0.66351 0.66351 0.66351 -0.00000 0.00000  0.00000  329 PRO   I CG  
2180  C CD  . PRO   A  329 ? 0.72546 0.72546 0.72546 -0.00000 0.00000  0.00000  329 PRO   I CD  
2181  N N   . ASP   A  330 ? 0.99972 0.99972 0.99972 -0.00000 0.00000  0.00000  330 ASP   I N   
2182  C CA  . ASP   A  330 ? 1.12729 1.12729 1.12729 -0.00000 0.00000  0.00000  330 ASP   I CA  
2183  C C   . ASP   A  330 ? 0.85743 0.85743 0.85743 0.00000  0.00000  0.00000  330 ASP   I C   
2184  O O   . ASP   A  330 ? 1.22124 1.22124 1.22124 0.00000  0.00000  0.00000  330 ASP   I O   
2185  C CB  . ASP   A  330 ? 0.76296 0.76296 0.76296 -0.00000 0.00000  0.00000  330 ASP   I CB  
2186  N N   . ASN   A  331 ? 1.04201 1.04201 1.04201 0.00000  0.00000  0.00000  331 ASN   I N   
2187  C CA  . ASN   A  331 ? 1.04360 1.04360 1.04360 0.00000  0.00000  0.00000  331 ASN   I CA  
2188  C C   . ASN   A  331 ? 0.82409 0.82409 0.82409 0.00000  0.00000  0.00000  331 ASN   I C   
2189  O O   . ASN   A  331 ? 1.37768 1.37768 1.37768 -0.00000 0.00000  0.00000  331 ASN   I O   
2190  C CB  . ASN   A  331 ? 0.76401 0.76401 0.76401 -0.00000 0.00000  0.00000  331 ASN   I CB  
2191  C CG  . ASN   A  331 ? 0.90448 0.90448 0.90448 0.00000  0.00000  0.00000  331 ASN   I CG  
2192  O OD1 . ASN   A  331 ? 1.78487 1.78487 1.78487 0.00000  0.00000  0.00000  331 ASN   I OD1 
2193  N ND2 . ASN   A  331 ? 0.95729 0.95729 0.95729 -0.00000 0.00000  0.00000  331 ASN   I ND2 
2194  N N   . ASP   A  332 ? 0.99285 0.99285 0.99285 0.00000  0.00000  0.00000  332 ASP   I N   
2195  C CA  . ASP   A  332 ? 1.10050 1.10050 1.10050 0.00000  0.00000  0.00000  332 ASP   I CA  
2196  C C   . ASP   A  332 ? 0.75439 0.75439 0.75439 -0.00000 -0.00000 0.00000  332 ASP   I C   
2197  O O   . ASP   A  332 ? 0.82386 0.82386 0.82386 -0.00000 0.00000  0.00000  332 ASP   I O   
2198  C CB  . ASP   A  332 ? 1.14425 1.14425 1.14425 -0.00000 0.00000  0.00000  332 ASP   I CB  
2199  C CG  . ASP   A  332 ? 1.25643 1.25643 1.25643 0.00000  0.00000  0.00000  332 ASP   I CG  
2200  O OD1 . ASP   A  332 ? 1.25886 1.25886 1.25886 0.00000  0.00000  0.00000  332 ASP   I OD1 
2201  O OD2 . ASP   A  332 ? 1.08495 1.08495 1.08495 0.00000  0.00000  0.00000  332 ASP   I OD2 
2202  N N   . TYR   A  333 ? 1.30467 1.30467 1.30467 0.00000  -0.00000 0.00000  333 TYR   I N   
2203  C CA  . TYR   A  333 ? 1.26611 1.26611 1.26611 0.00000  0.00000  0.00000  333 TYR   I CA  
2204  C C   . TYR   A  333 ? 1.43275 1.43275 1.43275 0.00000  0.00000  0.00000  333 TYR   I C   
2205  O O   . TYR   A  333 ? 0.53803 0.53803 0.53803 0.00000  0.00000  0.00000  333 TYR   I O   
2206  C CB  . TYR   A  333 ? 0.44437 0.44437 0.44437 0.00000  0.00000  0.00000  333 TYR   I CB  
2207  C CG  . TYR   A  333 ? 0.89783 0.89783 0.89783 0.00000  0.00000  0.00000  333 TYR   I CG  
2208  C CD1 . TYR   A  333 ? 1.47839 1.47839 1.47839 0.00000  0.00000  0.00000  333 TYR   I CD1 
2209  C CD2 . TYR   A  333 ? 1.03870 1.03870 1.03870 -0.00000 -0.00000 0.00000  333 TYR   I CD2 
2210  C CE1 . TYR   A  333 ? 1.58918 1.58918 1.58918 0.00000  0.00000  0.00000  333 TYR   I CE1 
2211  C CE2 . TYR   A  333 ? 1.07981 1.07981 1.07981 -0.00000 0.00000  0.00000  333 TYR   I CE2 
2212  C CZ  . TYR   A  333 ? 1.11776 1.11776 1.11776 -0.00000 0.00000  0.00000  333 TYR   I CZ  
2213  O OH  . TYR   A  333 ? 1.06489 1.06489 1.06489 0.00000  0.00000  0.00000  333 TYR   I OH  
2214  N N   . ASP   A  334 ? 0.86877 0.86877 0.86877 0.00000  0.00000  0.00000  334 ASP   I N   
2215  C CA  . ASP   A  334 ? 0.84438 0.84438 0.84438 -0.00000 0.00000  0.00000  334 ASP   I CA  
2216  C C   . ASP   A  334 ? 0.96395 0.96395 0.96395 -0.00000 0.00000  0.00000  334 ASP   I C   
2217  O O   . ASP   A  334 ? 0.52988 0.52988 0.52988 0.00000  0.00000  0.00000  334 ASP   I O   
2218  C CB  . ASP   A  334 ? 1.20917 1.20917 1.20917 0.00000  0.00000  -0.00000 334 ASP   I CB  
2219  C CG  . ASP   A  334 ? 1.39435 1.39435 1.39435 -0.00000 0.00000  0.00000  334 ASP   I CG  
2220  O OD1 . ASP   A  334 ? 0.83969 0.83969 0.83969 0.00000  0.00000  0.00000  334 ASP   I OD1 
2221  O OD2 . ASP   A  334 ? 0.98311 0.98311 0.98311 0.00000  0.00000  0.00000  334 ASP   I OD2 
2222  N N   . PRO   A  335 ? 0.85559 0.85559 0.85559 0.00000  0.00000  0.00000  335 PRO   I N   
2223  C CA  . PRO   A  335 ? 0.59984 0.59984 0.59984 -0.00000 0.00000  -0.00000 335 PRO   I CA  
2224  C C   . PRO   A  335 ? 0.39757 0.39757 0.39757 0.00000  0.00000  0.00000  335 PRO   I C   
2225  O O   . PRO   A  335 ? 0.76412 0.76412 0.76412 -0.00000 0.00000  0.00000  335 PRO   I O   
2226  C CB  . PRO   A  335 ? 0.67303 0.67303 0.67303 -0.00000 0.00000  0.00000  335 PRO   I CB  
2227  C CG  . PRO   A  335 ? 0.83591 0.83591 0.83591 0.00000  0.00000  -0.00000 335 PRO   I CG  
2228  C CD  . PRO   A  335 ? 0.50124 0.50124 0.50124 0.00000  0.00000  0.00000  335 PRO   I CD  
2229  N N   . PRO   A  336 ? 0.76643 0.76643 0.76643 -0.00000 0.00000  0.00000  336 PRO   I N   
2230  C CA  . PRO   A  336 ? 0.31574 0.31574 0.31574 -0.00000 0.00000  0.00000  336 PRO   I CA  
2231  C C   . PRO   A  336 ? 1.15534 1.15534 1.15534 -0.00000 0.00000  0.00000  336 PRO   I C   
2232  O O   . PRO   A  336 ? 0.38361 0.38361 0.38361 0.00000  0.00000  0.00000  336 PRO   I O   
2233  C CB  . PRO   A  336 ? 0.55617 0.55617 0.55617 0.00000  0.00000  0.00000  336 PRO   I CB  
2234  C CG  . PRO   A  336 ? 0.51787 0.51787 0.51787 0.00000  0.00000  0.00000  336 PRO   I CG  
2235  C CD  . PRO   A  336 ? 0.31552 0.31552 0.31552 0.00000  0.00000  0.00000  336 PRO   I CD  
2236  N N   . PRO   A  337 ? 0.55637 0.55637 0.55637 0.00000  0.00000  0.00000  337 PRO   I N   
2237  C CA  . PRO   A  337 ? 0.75409 0.75409 0.75409 0.00000  0.00000  0.00000  337 PRO   I CA  
2238  C C   . PRO   A  337 ? 0.60912 0.60912 0.60912 0.00000  0.00000  0.00000  337 PRO   I C   
2239  O O   . PRO   A  337 ? 0.58184 0.58184 0.58184 0.00000  0.00000  0.00000  337 PRO   I O   
2240  C CB  . PRO   A  337 ? 0.58340 0.58340 0.58340 -0.00000 0.00000  0.00000  337 PRO   I CB  
2241  C CG  . PRO   A  337 ? 0.68957 0.68957 0.68957 0.00000  0.00000  0.00000  337 PRO   I CG  
2242  C CD  . PRO   A  337 ? 0.79944 0.79944 0.79944 0.00000  0.00000  0.00000  337 PRO   I CD  
2243  N N   . TYR   A  338 ? 0.56849 0.56849 0.56849 0.00000  0.00000  0.00000  338 TYR   I N   
2244  C CA  . TYR   A  338 ? 0.60124 0.60124 0.60124 -0.00000 0.00000  0.00000  338 TYR   I CA  
2245  C C   . TYR   A  338 ? 0.52287 0.52287 0.52287 -0.00000 0.00000  0.00000  338 TYR   I C   
2246  O O   . TYR   A  338 ? 0.53969 0.53969 0.53969 0.00000  0.00000  0.00000  338 TYR   I O   
2247  C CB  . TYR   A  338 ? 0.44315 0.44315 0.44315 -0.00000 0.00000  0.00000  338 TYR   I CB  
2248  C CG  . TYR   A  338 ? 0.60876 0.60876 0.60876 0.00000  0.00000  0.00000  338 TYR   I CG  
2249  C CD1 . TYR   A  338 ? 0.51666 0.51666 0.51666 0.00000  0.00000  0.00000  338 TYR   I CD1 
2250  C CD2 . TYR   A  338 ? 0.48931 0.48931 0.48931 0.00000  0.00000  0.00000  338 TYR   I CD2 
2251  C CE1 . TYR   A  338 ? 0.55101 0.55101 0.55101 0.00000  0.00000  0.00000  338 TYR   I CE1 
2252  C CE2 . TYR   A  338 ? 0.41216 0.41216 0.41216 0.00000  0.00000  0.00000  338 TYR   I CE2 
2253  C CZ  . TYR   A  338 ? 0.66856 0.66856 0.66856 -0.00000 0.00000  0.00000  338 TYR   I CZ  
2254  O OH  . TYR   A  338 ? 0.52353 0.52353 0.52353 -0.00000 0.00000  0.00000  338 TYR   I OH  
2255  N N   . LEU   A  339 ? 0.48550 0.48550 0.48550 0.00000  0.00000  0.00000  339 LEU   I N   
2256  C CA  . LEU   A  339 ? 0.37356 0.37356 0.37356 0.00000  0.00000  0.00000  339 LEU   I CA  
2257  C C   . LEU   A  339 ? 0.52535 0.52535 0.52535 0.00000  0.00000  0.00000  339 LEU   I C   
2258  O O   . LEU   A  339 ? 0.54678 0.54678 0.54678 0.00000  0.00000  0.00000  339 LEU   I O   
2259  C CB  . LEU   A  339 ? 0.38398 0.38398 0.38398 0.00000  0.00000  0.00000  339 LEU   I CB  
2260  C CG  . LEU   A  339 ? 0.66281 0.66281 0.66281 0.00000  0.00000  0.00000  339 LEU   I CG  
2261  C CD1 . LEU   A  339 ? 0.45796 0.45796 0.45796 0.00000  0.00000  0.00000  339 LEU   I CD1 
2262  C CD2 . LEU   A  339 ? 0.47511 0.47511 0.47511 0.00000  0.00000  0.00000  339 LEU   I CD2 
2263  N N   . LYS   A  340 ? 0.41327 0.41327 0.41327 0.00000  0.00000  0.00000  340 LYS   I N   
2264  C CA  . LYS   A  340 ? 0.66427 0.66427 0.66427 -0.00000 0.00000  0.00000  340 LYS   I CA  
2265  C C   . LYS   A  340 ? 0.43898 0.43898 0.43898 0.00000  0.00000  0.00000  340 LYS   I C   
2266  O O   . LYS   A  340 ? 0.51993 0.51993 0.51993 0.00000  0.00000  0.00000  340 LYS   I O   
2267  C CB  . LYS   A  340 ? 0.44722 0.44722 0.44722 -0.00000 0.00000  0.00000  340 LYS   I CB  
2268  C CG  . LYS   A  340 ? 1.26280 1.26280 1.26280 -0.00000 0.00000  0.00000  340 LYS   I CG  
2269  C CD  . LYS   A  340 ? 1.39557 1.39557 1.39557 0.00000  0.00000  0.00000  340 LYS   I CD  
2270  C CE  . LYS   A  340 ? 1.53939 1.53939 1.53939 0.00000  -0.00000 0.00000  340 LYS   I CE  
2271  N NZ  . LYS   A  340 ? 1.17144 1.17144 1.17144 0.00000  0.00000  0.00000  340 LYS   I NZ  
2272  N N   . SER   A  341 ? 0.49137 0.49137 0.49137 0.00000  0.00000  0.00000  341 SER   I N   
2273  C CA  . SER   A  341 ? 0.40468 0.40468 0.40468 -0.00000 0.00000  0.00000  341 SER   I CA  
2274  C C   . SER   A  341 ? 0.46656 0.46656 0.46656 -0.00000 0.00000  0.00000  341 SER   I C   
2275  O O   . SER   A  341 ? 0.60016 0.60016 0.60016 0.00000  -0.00000 0.00000  341 SER   I O   
2276  C CB  . SER   A  341 ? 0.48758 0.48758 0.48758 -0.00000 0.00000  0.00000  341 SER   I CB  
2277  O OG  . SER   A  341 ? 0.48457 0.48457 0.48457 0.00000  0.00000  0.00000  341 SER   I OG  
2278  N N   . LEU   A  342 ? 0.42476 0.42476 0.42476 0.00000  0.00000  0.00000  342 LEU   I N   
2279  C CA  . LEU   A  342 ? 0.56647 0.56647 0.56647 -0.00000 0.00000  0.00000  342 LEU   I CA  
2280  C C   . LEU   A  342 ? 0.42212 0.42212 0.42212 0.00000  0.00000  -0.00000 342 LEU   I C   
2281  O O   . LEU   A  342 ? 0.49705 0.49705 0.49705 0.00000  0.00000  0.00000  342 LEU   I O   
2282  C CB  . LEU   A  342 ? 0.34946 0.34946 0.34946 -0.00000 0.00000  0.00000  342 LEU   I CB  
2283  C CG  . LEU   A  342 ? 0.58081 0.58081 0.58081 -0.00000 0.00000  0.00000  342 LEU   I CG  
2284  C CD1 . LEU   A  342 ? 0.32974 0.32974 0.32974 0.00000  0.00000  0.00000  342 LEU   I CD1 
2285  C CD2 . LEU   A  342 ? 0.27416 0.27416 0.27416 0.00000  0.00000  0.00000  342 LEU   I CD2 
2286  N N   . VAL   A  343 ? 0.52039 0.52039 0.52039 -0.00000 0.00000  0.00000  343 VAL   I N   
2287  C CA  . VAL   A  343 ? 0.44812 0.44812 0.44812 0.00000  0.00000  0.00000  343 VAL   I CA  
2288  C C   . VAL   A  343 ? 0.61168 0.61168 0.61168 0.00000  0.00000  0.00000  343 VAL   I C   
2289  O O   . VAL   A  343 ? 0.41320 0.41320 0.41320 0.00000  0.00000  0.00000  343 VAL   I O   
2290  C CB  . VAL   A  343 ? 0.45928 0.45928 0.45928 -0.00000 0.00000  0.00000  343 VAL   I CB  
2291  C CG1 . VAL   A  343 ? 0.28469 0.28469 0.28469 -0.00000 0.00000  0.00000  343 VAL   I CG1 
2292  C CG2 . VAL   A  343 ? 0.37775 0.37775 0.37775 0.00000  0.00000  0.00000  343 VAL   I CG2 
2293  N N   . TYR   A  344 ? 0.32438 0.32438 0.32438 -0.00000 0.00000  0.00000  344 TYR   I N   
2294  C CA  . TYR   A  344 ? 0.54546 0.54546 0.54546 0.00000  0.00000  0.00000  344 TYR   I CA  
2295  C C   . TYR   A  344 ? 0.56488 0.56488 0.56488 -0.00000 -0.00000 -0.00000 344 TYR   I C   
2296  O O   . TYR   A  344 ? 0.43804 0.43804 0.43804 0.00000  0.00000  0.00000  344 TYR   I O   
2297  C CB  . TYR   A  344 ? 0.37956 0.37956 0.37956 -0.00000 0.00000  0.00000  344 TYR   I CB  
2298  C CG  . TYR   A  344 ? 0.63773 0.63773 0.63773 -0.00000 0.00000  0.00000  344 TYR   I CG  
2299  C CD1 . TYR   A  344 ? 0.41928 0.41928 0.41928 0.00000  0.00000  0.00000  344 TYR   I CD1 
2300  C CD2 . TYR   A  344 ? 0.53612 0.53612 0.53612 0.00000  0.00000  0.00000  344 TYR   I CD2 
2301  C CE1 . TYR   A  344 ? 0.42180 0.42180 0.42180 0.00000  0.00000  0.00000  344 TYR   I CE1 
2302  C CE2 . TYR   A  344 ? 0.41037 0.41037 0.41037 0.00000  0.00000  0.00000  344 TYR   I CE2 
2303  C CZ  . TYR   A  344 ? 0.64176 0.64176 0.64176 0.00000  -0.00000 0.00000  344 TYR   I CZ  
2304  O OH  . TYR   A  344 ? 0.57893 0.57893 0.57893 0.00000  0.00000  0.00000  344 TYR   I OH  
2305  N N   . PHE   A  345 ? 0.30277 0.30277 0.30277 -0.00000 0.00000  0.00000  345 PHE   I N   
2306  C CA  . PHE   A  345 ? 0.41737 0.41737 0.41737 0.00000  0.00000  0.00000  345 PHE   I CA  
2307  C C   . PHE   A  345 ? 0.48297 0.48297 0.48297 0.00000  0.00000  0.00000  345 PHE   I C   
2308  O O   . PHE   A  345 ? 0.43666 0.43666 0.43666 0.00000  0.00000  0.00000  345 PHE   I O   
2309  C CB  . PHE   A  345 ? 0.29707 0.29707 0.29707 0.00000  0.00000  0.00000  345 PHE   I CB  
2310  C CG  . PHE   A  345 ? 0.46431 0.46431 0.46431 0.00000  0.00000  0.00000  345 PHE   I CG  
2311  C CD1 . PHE   A  345 ? 0.53030 0.53030 0.53030 0.00000  0.00000  0.00000  345 PHE   I CD1 
2312  C CD2 . PHE   A  345 ? 0.38260 0.38260 0.38260 -0.00000 0.00000  0.00000  345 PHE   I CD2 
2313  C CE1 . PHE   A  345 ? 0.32997 0.32997 0.32997 0.00000  0.00000  0.00000  345 PHE   I CE1 
2314  C CE2 . PHE   A  345 ? 0.40118 0.40118 0.40118 -0.00000 0.00000  0.00000  345 PHE   I CE2 
2315  C CZ  . PHE   A  345 ? 0.43029 0.43029 0.43029 0.00000  0.00000  0.00000  345 PHE   I CZ  
2316  N N   . SER   A  346 ? 0.25503 0.25503 0.25503 0.00000  0.00000  0.00000  346 SER   I N   
2317  C CA  . SER   A  346 ? 0.53629 0.53629 0.53629 -0.00000 0.00000  0.00000  346 SER   I CA  
2318  C C   . SER   A  346 ? 0.37635 0.37635 0.37635 0.00000  0.00000  0.00000  346 SER   I C   
2319  O O   . SER   A  346 ? 0.37639 0.37639 0.37639 -0.00000 0.00000  0.00000  346 SER   I O   
2320  C CB  . SER   A  346 ? 0.36882 0.36882 0.36882 0.00000  0.00000  0.00000  346 SER   I CB  
2321  O OG  . SER   A  346 ? 0.32585 0.32585 0.32585 0.00000  0.00000  0.00000  346 SER   I OG  
2322  N N   . ASN   A  347 ? 0.45190 0.45190 0.45190 0.00000  0.00000  0.00000  347 ASN   I N   
2323  C CA  . ASN   A  347 ? 0.21255 0.21255 0.21255 0.00000  0.00000  0.00000  347 ASN   I CA  
2324  C C   . ASN   A  347 ? 0.42623 0.42623 0.42623 0.00000  0.00000  0.00000  347 ASN   I C   
2325  O O   . ASN   A  347 ? 0.43057 0.43057 0.43057 0.00000  0.00000  0.00000  347 ASN   I O   
2326  C CB  . ASN   A  347 ? 0.30779 0.30779 0.30779 0.00000  0.00000  0.00000  347 ASN   I CB  
2327  C CG  . ASN   A  347 ? 0.49961 0.49961 0.49961 -0.00000 0.00000  0.00000  347 ASN   I CG  
2328  O OD1 . ASN   A  347 ? 0.38734 0.38734 0.38734 -0.00000 0.00000  0.00000  347 ASN   I OD1 
2329  N ND2 . ASN   A  347 ? 0.26995 0.26995 0.26995 0.00000  -0.00000 0.00000  347 ASN   I ND2 
2330  N N   . ILE   A  348 ? 0.36102 0.36102 0.36102 0.00000  0.00000  0.00000  348 ILE   I N   
2331  C CA  . ILE   A  348 ? 0.27230 0.27230 0.27230 0.00000  0.00000  0.00000  348 ILE   I CA  
2332  C C   . ILE   A  348 ? 0.41263 0.41263 0.41263 0.00000  0.00000  0.00000  348 ILE   I C   
2333  O O   . ILE   A  348 ? 0.45659 0.45659 0.45659 0.00000  0.00000  0.00000  348 ILE   I O   
2334  C CB  . ILE   A  348 ? 0.38608 0.38608 0.38608 0.00000  0.00000  0.00000  348 ILE   I CB  
2335  C CG1 . ILE   A  348 ? 0.24082 0.24082 0.24082 0.00000  0.00000  0.00000  348 ILE   I CG1 
2336  C CG2 . ILE   A  348 ? 0.21431 0.21431 0.21431 -0.00000 0.00000  0.00000  348 ILE   I CG2 
2337  C CD1 . ILE   A  348 ? 0.52647 0.52647 0.52647 0.00000  0.00000  0.00000  348 ILE   I CD1 
2338  N N   . ALA   A  349 ? 0.33884 0.33884 0.33884 -0.00000 0.00000  0.00000  349 ALA   I N   
2339  C CA  . ALA   A  349 ? 0.34470 0.34470 0.34470 -0.00000 0.00000  0.00000  349 ALA   I CA  
2340  C C   . ALA   A  349 ? 0.38500 0.38500 0.38500 0.00000  -0.00000 -0.00000 349 ALA   I C   
2341  O O   . ALA   A  349 ? 0.44751 0.44751 0.44751 -0.00000 0.00000  0.00000  349 ALA   I O   
2342  C CB  . ALA   A  349 ? 0.15726 0.15726 0.15726 0.00000  0.00000  0.00000  349 ALA   I CB  
2343  N N   . ALA   A  350 ? 0.33691 0.33691 0.33691 0.00000  0.00000  0.00000  350 ALA   I N   
2344  C CA  . ALA   A  350 ? 0.36840 0.36840 0.36840 0.00000  0.00000  0.00000  350 ALA   I CA  
2345  C C   . ALA   A  350 ? 0.44362 0.44362 0.44362 0.00000  0.00000  0.00000  350 ALA   I C   
2346  O O   . ALA   A  350 ? 0.36168 0.36168 0.36168 -0.00000 0.00000  0.00000  350 ALA   I O   
2347  C CB  . ALA   A  350 ? 0.18949 0.18949 0.18949 0.00000  0.00000  0.00000  350 ALA   I CB  
2348  N N   . ARG   A  351 ? 0.25343 0.25343 0.25343 -0.00000 0.00000  0.00000  351 ARG   I N   
2349  C CA  . ARG   A  351 ? 0.38331 0.38331 0.38331 -0.00000 0.00000  -0.00000 351 ARG   I CA  
2350  C C   . ARG   A  351 ? 0.28625 0.28625 0.28625 0.00000  0.00000  0.00000  351 ARG   I C   
2351  O O   . ARG   A  351 ? 0.46654 0.46654 0.46654 0.00000  0.00000  0.00000  351 ARG   I O   
2352  C CB  . ARG   A  351 ? 0.20245 0.20245 0.20245 -0.00000 0.00000  0.00000  351 ARG   I CB  
2353  C CG  . ARG   A  351 ? 0.20252 0.20252 0.20252 -0.00000 0.00000  0.00000  351 ARG   I CG  
2354  C CD  . ARG   A  351 ? 0.30277 0.30277 0.30277 0.00000  0.00000  0.00000  351 ARG   I CD  
2355  N NE  . ARG   A  351 ? 0.32258 0.32258 0.32258 0.00000  0.00000  0.00000  351 ARG   I NE  
2356  C CZ  . ARG   A  351 ? 0.59515 0.59515 0.59515 0.00000  0.00000  0.00000  351 ARG   I CZ  
2357  N NH1 . ARG   A  351 ? 0.32600 0.32600 0.32600 0.00000  0.00000  0.00000  351 ARG   I NH1 
2358  N NH2 . ARG   A  351 ? 0.26732 0.26732 0.26732 0.00000  0.00000  0.00000  351 ARG   I NH2 
2359  N N   . GLN   A  352 ? 0.38192 0.38192 0.38192 0.00000  0.00000  0.00000  352 GLN   I N   
2360  C CA  . GLN   A  352 ? 0.29782 0.29782 0.29782 0.00000  0.00000  0.00000  352 GLN   I CA  
2361  C C   . GLN   A  352 ? 0.45204 0.45204 0.45204 0.00000  0.00000  0.00000  352 GLN   I C   
2362  O O   . GLN   A  352 ? 0.43783 0.43783 0.43783 0.00000  0.00000  0.00000  352 GLN   I O   
2363  C CB  . GLN   A  352 ? 0.42656 0.42656 0.42656 0.00000  0.00000  0.00000  352 GLN   I CB  
2364  C CG  . GLN   A  352 ? 0.36392 0.36392 0.36392 0.00000  0.00000  0.00000  352 GLN   I CG  
2365  C CD  . GLN   A  352 ? 0.46962 0.46962 0.46962 0.00000  0.00000  0.00000  352 GLN   I CD  
2366  O OE1 . GLN   A  352 ? 0.49570 0.49570 0.49570 0.00000  -0.00000 0.00000  352 GLN   I OE1 
2367  N NE2 . GLN   A  352 ? 0.33240 0.33240 0.33240 0.00000  0.00000  0.00000  352 GLN   I NE2 
2368  N N   . ILE   A  353 ? 0.34579 0.34579 0.34579 -0.00000 0.00000  0.00000  353 ILE   I N   
2369  C CA  . ILE   A  353 ? 0.38154 0.38154 0.38154 0.00000  0.00000  0.00000  353 ILE   I CA  
2370  C C   . ILE   A  353 ? 0.29310 0.29310 0.29310 0.00000  0.00000  0.00000  353 ILE   I C   
2371  O O   . ILE   A  353 ? 0.47156 0.47156 0.47156 0.00000  0.00000  0.00000  353 ILE   I O   
2372  C CB  . ILE   A  353 ? 0.35497 0.35497 0.35497 0.00000  0.00000  0.00000  353 ILE   I CB  
2373  C CG1 . ILE   A  353 ? 0.44669 0.44669 0.44669 -0.00000 0.00000  0.00000  353 ILE   I CG1 
2374  C CG2 . ILE   A  353 ? 0.23926 0.23926 0.23926 0.00000  0.00000  0.00000  353 ILE   I CG2 
2375  C CD1 . ILE   A  353 ? 0.19556 0.19556 0.19556 -0.00000 0.00000  0.00000  353 ILE   I CD1 
2376  N N   . MET   A  354 ? 0.25367 0.25367 0.25367 0.00000  0.00000  0.00000  354 MET   I N   
2377  C CA  . MET   A  354 ? 0.32089 0.32089 0.32089 0.00000  0.00000  0.00000  354 MET   I CA  
2378  C C   . MET   A  354 ? 0.38541 0.38541 0.38541 -0.00000 0.00000  0.00000  354 MET   I C   
2379  O O   . MET   A  354 ? 0.40403 0.40403 0.40403 0.00000  0.00000  0.00000  354 MET   I O   
2380  C CB  . MET   A  354 ? 0.18177 0.18177 0.18177 0.00000  -0.00000 0.00000  354 MET   I CB  
2381  C CG  . MET   A  354 ? 0.45841 0.45841 0.45841 0.00000  0.00000  0.00000  354 MET   I CG  
2382  S SD  . MET   A  354 ? 0.42344 0.42344 0.42344 -0.00000 0.00000  0.00000  354 MET   I SD  
2383  C CE  . MET   A  354 ? 0.40073 0.40073 0.40073 -0.00000 0.00000  0.00000  354 MET   I CE  
2384  N N   . PHE   A  355 ? 0.35539 0.35539 0.35539 0.00000  0.00000  0.00000  355 PHE   I N   
2385  C CA  . PHE   A  355 ? 0.37604 0.37604 0.37604 0.00000  -0.00000 0.00000  355 PHE   I CA  
2386  C C   . PHE   A  355 ? 0.36008 0.36008 0.36008 0.00000  0.00000  0.00000  355 PHE   I C   
2387  O O   . PHE   A  355 ? 0.41848 0.41848 0.41848 -0.00000 0.00000  0.00000  355 PHE   I O   
2388  C CB  . PHE   A  355 ? 0.42491 0.42491 0.42491 0.00000  0.00000  0.00000  355 PHE   I CB  
2389  C CG  . PHE   A  355 ? 0.44846 0.44846 0.44846 -0.00000 0.00000  0.00000  355 PHE   I CG  
2390  C CD1 . PHE   A  355 ? 0.28436 0.28436 0.28436 -0.00000 0.00000  0.00000  355 PHE   I CD1 
2391  C CD2 . PHE   A  355 ? 0.39447 0.39447 0.39447 -0.00000 0.00000  0.00000  355 PHE   I CD2 
2392  C CE1 . PHE   A  355 ? 0.44746 0.44746 0.44746 -0.00000 0.00000  0.00000  355 PHE   I CE1 
2393  C CE2 . PHE   A  355 ? 0.23191 0.23191 0.23191 0.00000  0.00000  0.00000  355 PHE   I CE2 
2394  C CZ  . PHE   A  355 ? 0.25166 0.25166 0.25166 0.00000  0.00000  0.00000  355 PHE   I CZ  
2395  N N   . ILE   A  356 ? 0.36775 0.36775 0.36775 0.00000  0.00000  0.00000  356 ILE   I N   
2396  C CA  . ILE   A  356 ? 0.41029 0.41029 0.41029 0.00000  0.00000  0.00000  356 ILE   I CA  
2397  C C   . ILE   A  356 ? 0.57419 0.57419 0.57419 0.00000  0.00000  0.00000  356 ILE   I C   
2398  O O   . ILE   A  356 ? 0.40625 0.40625 0.40625 0.00000  0.00000  0.00000  356 ILE   I O   
2399  C CB  . ILE   A  356 ? 0.33533 0.33533 0.33533 0.00000  0.00000  0.00000  356 ILE   I CB  
2400  C CG1 . ILE   A  356 ? 0.32647 0.32647 0.32647 0.00000  0.00000  0.00000  356 ILE   I CG1 
2401  C CG2 . ILE   A  356 ? 0.37382 0.37382 0.37382 0.00000  0.00000  0.00000  356 ILE   I CG2 
2402  C CD1 . ILE   A  356 ? 0.25181 0.25181 0.25181 0.00000  0.00000  -0.00000 356 ILE   I CD1 
2403  N N   . GLU   A  357 ? 0.27510 0.27510 0.27510 -0.00000 0.00000  0.00000  357 GLU   I N   
2404  C CA  . GLU   A  357 ? 0.46498 0.46498 0.46498 0.00000  -0.00000 0.00000  357 GLU   I CA  
2405  C C   . GLU   A  357 ? 0.44226 0.44226 0.44226 0.00000  0.00000  0.00000  357 GLU   I C   
2406  O O   . GLU   A  357 ? 0.42564 0.42564 0.42564 -0.00000 0.00000  0.00000  357 GLU   I O   
2407  C CB  . GLU   A  357 ? 0.34486 0.34486 0.34486 -0.00000 0.00000  0.00000  357 GLU   I CB  
2408  C CG  . GLU   A  357 ? 0.32940 0.32940 0.32940 0.00000  0.00000  0.00000  357 GLU   I CG  
2409  C CD  . GLU   A  357 ? 1.00446 1.00446 1.00446 0.00000  0.00000  0.00000  357 GLU   I CD  
2410  O OE1 . GLU   A  357 ? 0.78319 0.78319 0.78319 0.00000  0.00000  0.00000  357 GLU   I OE1 
2411  O OE2 . GLU   A  357 ? 0.61954 0.61954 0.61954 -0.00000 0.00000  0.00000  357 GLU   I OE2 
2412  N N   . ALA   A  358 ? 0.29649 0.29649 0.29649 0.00000  0.00000  0.00000  358 ALA   I N   
2413  C CA  . ALA   A  358 ? 0.53537 0.53537 0.53537 0.00000  0.00000  0.00000  358 ALA   I CA  
2414  C C   . ALA   A  358 ? 0.46480 0.46480 0.46480 -0.00000 0.00000  0.00000  358 ALA   I C   
2415  O O   . ALA   A  358 ? 0.79402 0.79402 0.79402 0.00000  0.00000  0.00000  358 ALA   I O   
2416  C CB  . ALA   A  358 ? 0.39150 0.39150 0.39150 0.00000  -0.00000 0.00000  358 ALA   I CB  
2417  N N   . ASP   A  359 ? 0.65416 0.65416 0.65416 0.00000  0.00000  0.00000  359 ASP   I N   
2418  C CA  . ASP   A  359 ? 0.59478 0.59478 0.59478 -0.00000 0.00000  0.00000  359 ASP   I CA  
2419  C C   . ASP   A  359 ? 0.36875 0.36875 0.36875 -0.00000 0.00000  0.00000  359 ASP   I C   
2420  O O   . ASP   A  359 ? 0.45441 0.45441 0.45441 0.00000  0.00000  0.00000  359 ASP   I O   
2421  C CB  . ASP   A  359 ? 0.32962 0.32962 0.32962 0.00000  0.00000  -0.00000 359 ASP   I CB  
2422  C CG  . ASP   A  359 ? 0.80189 0.80189 0.80189 0.00000  0.00000  0.00000  359 ASP   I CG  
2423  O OD1 . ASP   A  359 ? 0.54889 0.54889 0.54889 -0.00000 0.00000  0.00000  359 ASP   I OD1 
2424  O OD2 . ASP   A  359 ? 0.46924 0.46924 0.46924 -0.00000 0.00000  0.00000  359 ASP   I OD2 
2425  N N   . ASN   A  360 ? 0.46414 0.46414 0.46414 -0.00000 0.00000  0.00000  360 ASN   I N   
2426  C CA  . ASN   A  360 ? 0.35335 0.35335 0.35335 0.00000  0.00000  0.00000  360 ASN   I CA  
2427  C C   . ASN   A  360 ? 0.49222 0.49222 0.49222 0.00000  0.00000  0.00000  360 ASN   I C   
2428  O O   . ASN   A  360 ? 0.62740 0.62740 0.62740 -0.00000 0.00000  0.00000  360 ASN   I O   
2429  C CB  . ASN   A  360 ? 0.36957 0.36957 0.36957 0.00000  0.00000  0.00000  360 ASN   I CB  
2430  C CG  . ASN   A  360 ? 0.60750 0.60750 0.60750 -0.00000 0.00000  0.00000  360 ASN   I CG  
2431  O OD1 . ASN   A  360 ? 0.64681 0.64681 0.64681 0.00000  0.00000  0.00000  360 ASN   I OD1 
2432  N ND2 . ASN   A  360 ? 0.68302 0.68302 0.68302 0.00000  0.00000  0.00000  360 ASN   I ND2 
2433  N N   . LYS   A  361 ? 0.59005 0.59005 0.59005 -0.00000 0.00000  0.00000  361 LYS   I N   
2434  C CA  . LYS   A  361 ? 0.68844 0.68844 0.68844 -0.00000 0.00000  0.00000  361 LYS   I CA  
2435  C C   . LYS   A  361 ? 0.33784 0.33784 0.33784 0.00000  0.00000  0.00000  361 LYS   I C   
2436  O O   . LYS   A  361 ? 0.97595 0.97595 0.97595 0.00000  0.00000  0.00000  361 LYS   I O   
2437  C CB  . LYS   A  361 ? 0.39048 0.39048 0.39048 0.00000  0.00000  0.00000  361 LYS   I CB  
2438  C CG  . LYS   A  361 ? 1.28868 1.28868 1.28868 0.00000  0.00000  0.00000  361 LYS   I CG  
2439  C CD  . LYS   A  361 ? 1.52633 1.52633 1.52633 0.00000  0.00000  0.00000  361 LYS   I CD  
2440  C CE  . LYS   A  361 ? 1.74250 1.74250 1.74250 -0.00000 0.00000  0.00000  361 LYS   I CE  
2441  N NZ  . LYS   A  361 ? 1.49710 1.49710 1.49710 0.00000  0.00000  0.00000  361 LYS   I NZ  
2442  N N   . GLU   A  362 ? 0.53347 0.53347 0.53347 0.00000  0.00000  0.00000  362 GLU   I N   
2443  C CA  . GLU   A  362 ? 0.47602 0.47602 0.47602 0.00000  0.00000  0.00000  362 GLU   I CA  
2444  C C   . GLU   A  362 ? 0.73289 0.73289 0.73289 0.00000  0.00000  0.00000  362 GLU   I C   
2445  O O   . GLU   A  362 ? 0.63490 0.63490 0.63490 -0.00000 0.00000  0.00000  362 GLU   I O   
2446  C CB  . GLU   A  362 ? 0.58821 0.58821 0.58821 0.00000  0.00000  0.00000  362 GLU   I CB  
2447  N N   . ILE   A  363 ? 0.40776 0.40776 0.40776 -0.00000 0.00000  0.00000  363 ILE   I N   
2448  C CA  . ILE   A  363 ? 0.63533 0.63533 0.63533 -0.00000 0.00000  0.00000  363 ILE   I CA  
2449  C C   . ILE   A  363 ? 0.48957 0.48957 0.48957 0.00000  0.00000  -0.00000 363 ILE   I C   
2450  O O   . ILE   A  363 ? 0.59537 0.59537 0.59537 0.00000  0.00000  0.00000  363 ILE   I O   
2451  C CB  . ILE   A  363 ? 0.51167 0.51167 0.51167 0.00000  0.00000  0.00000  363 ILE   I CB  
2452  C CG1 . ILE   A  363 ? 0.43451 0.43451 0.43451 0.00000  0.00000  0.00000  363 ILE   I CG1 
2453  C CG2 . ILE   A  363 ? 0.25562 0.25562 0.25562 0.00000  0.00000  0.00000  363 ILE   I CG2 
2454  C CD1 . ILE   A  363 ? 0.47759 0.47759 0.47759 0.00000  0.00000  0.00000  363 ILE   I CD1 
2455  N N   . GLY   A  364 ? 0.48141 0.48141 0.48141 0.00000  0.00000  0.00000  364 GLY   I N   
2456  C CA  . GLY   A  364 ? 0.32811 0.32811 0.32811 0.00000  0.00000  0.00000  364 GLY   I CA  
2457  C C   . GLY   A  364 ? 0.90112 0.90112 0.90112 0.00000  0.00000  0.00000  364 GLY   I C   
2458  O O   . GLY   A  364 ? 0.45265 0.45265 0.45265 0.00000  0.00000  0.00000  364 GLY   I O   
2459  N N   . LEU   A  365 ? 0.59304 0.59304 0.59304 -0.00000 0.00000  0.00000  365 LEU   I N   
2460  C CA  . LEU   A  365 ? 0.30032 0.30032 0.30032 0.00000  0.00000  0.00000  365 LEU   I CA  
2461  C C   . LEU   A  365 ? 0.61259 0.61259 0.61259 0.00000  0.00000  0.00000  365 LEU   I C   
2462  O O   . LEU   A  365 ? 0.45175 0.45175 0.45175 0.00000  0.00000  0.00000  365 LEU   I O   
2463  C CB  . LEU   A  365 ? 0.47893 0.47893 0.47893 0.00000  0.00000  0.00000  365 LEU   I CB  
2464  C CG  . LEU   A  365 ? 0.52400 0.52400 0.52400 0.00000  0.00000  0.00000  365 LEU   I CG  
2465  C CD1 . LEU   A  365 ? 0.36233 0.36233 0.36233 0.00000  0.00000  0.00000  365 LEU   I CD1 
2466  C CD2 . LEU   A  365 ? 0.35013 0.35013 0.35013 0.00000  0.00000  0.00000  365 LEU   I CD2 
2467  N N   . ILE   A  366 ? 0.26109 0.26109 0.26109 0.00000  0.00000  0.00000  366 ILE   I N   
2468  C CA  . ILE   A  366 ? 0.44256 0.44256 0.44256 0.00000  0.00000  0.00000  366 ILE   I CA  
2469  C C   . ILE   A  366 ? 0.47184 0.47184 0.47184 0.00000  0.00000  0.00000  366 ILE   I C   
2470  O O   . ILE   A  366 ? 0.41516 0.41516 0.41516 -0.00000 0.00000  0.00000  366 ILE   I O   
2471  C CB  . ILE   A  366 ? 0.35849 0.35849 0.35849 0.00000  0.00000  0.00000  366 ILE   I CB  
2472  C CG1 . ILE   A  366 ? 0.40312 0.40312 0.40312 0.00000  0.00000  0.00000  366 ILE   I CG1 
2473  C CG2 . ILE   A  366 ? 0.25645 0.25645 0.25645 0.00000  -0.00000 0.00000  366 ILE   I CG2 
2474  C CD1 . ILE   A  366 ? 0.41288 0.41288 0.41288 0.00000  0.00000  0.00000  366 ILE   I CD1 
2475  N N   . PHE   A  367 ? 0.37976 0.37976 0.37976 -0.00000 0.00000  0.00000  367 PHE   I N   
2476  C CA  . PHE   A  367 ? 0.34136 0.34136 0.34136 0.00000  0.00000  0.00000  367 PHE   I CA  
2477  C C   . PHE   A  367 ? 0.45883 0.45883 0.45883 0.00000  0.00000  0.00000  367 PHE   I C   
2478  O O   . PHE   A  367 ? 0.40192 0.40192 0.40192 0.00000  0.00000  0.00000  367 PHE   I O   
2479  C CB  . PHE   A  367 ? 0.32829 0.32829 0.32829 0.00000  0.00000  0.00000  367 PHE   I CB  
2480  C CG  . PHE   A  367 ? 0.22703 0.22703 0.22703 0.00000  0.00000  0.00000  367 PHE   I CG  
2481  C CD1 . PHE   A  367 ? 0.43339 0.43339 0.43339 0.00000  0.00000  0.00000  367 PHE   I CD1 
2482  C CD2 . PHE   A  367 ? 0.37194 0.37194 0.37194 0.00000  0.00000  0.00000  367 PHE   I CD2 
2483  C CE1 . PHE   A  367 ? 0.23272 0.23272 0.23272 -0.00000 0.00000  0.00000  367 PHE   I CE1 
2484  C CE2 . PHE   A  367 ? 0.34739 0.34739 0.34739 0.00000  0.00000  0.00000  367 PHE   I CE2 
2485  C CZ  . PHE   A  367 ? 0.30587 0.30587 0.30587 0.00000  0.00000  0.00000  367 PHE   I CZ  
2486  N N   . LEU   A  368 ? 0.38021 0.38021 0.38021 0.00000  0.00000  0.00000  368 LEU   I N   
2487  C CA  . LEU   A  368 ? 0.26567 0.26567 0.26567 -0.00000 0.00000  0.00000  368 LEU   I CA  
2488  C C   . LEU   A  368 ? 0.27515 0.27515 0.27515 0.00000  0.00000  0.00000  368 LEU   I C   
2489  O O   . LEU   A  368 ? 0.38295 0.38295 0.38295 0.00000  0.00000  0.00000  368 LEU   I O   
2490  C CB  . LEU   A  368 ? 0.23609 0.23609 0.23609 0.00000  -0.00000 0.00000  368 LEU   I CB  
2491  C CG  . LEU   A  368 ? 0.37029 0.37029 0.37029 0.00000  0.00000  0.00000  368 LEU   I CG  
2492  C CD1 . LEU   A  368 ? 0.31686 0.31686 0.31686 -0.00000 0.00000  0.00000  368 LEU   I CD1 
2493  C CD2 . LEU   A  368 ? 0.33780 0.33780 0.33780 0.00000  0.00000  0.00000  368 LEU   I CD2 
2494  N N   . VAL   A  369 ? 0.28894 0.28894 0.28894 0.00000  0.00000  0.00000  369 VAL   I N   
2495  C CA  . VAL   A  369 ? 0.31857 0.31857 0.31857 0.00000  0.00000  0.00000  369 VAL   I CA  
2496  C C   . VAL   A  369 ? 0.28671 0.28671 0.28671 0.00000  0.00000  0.00000  369 VAL   I C   
2497  O O   . VAL   A  369 ? 0.40636 0.40636 0.40636 0.00000  0.00000  0.00000  369 VAL   I O   
2498  C CB  . VAL   A  369 ? 0.39750 0.39750 0.39750 0.00000  0.00000  0.00000  369 VAL   I CB  
2499  C CG1 . VAL   A  369 ? 0.26790 0.26790 0.26790 -0.00000 0.00000  0.00000  369 VAL   I CG1 
2500  C CG2 . VAL   A  369 ? 0.36154 0.36154 0.36154 -0.00000 0.00000  0.00000  369 VAL   I CG2 
2501  N N   . PHE   A  370 ? 0.38535 0.38535 0.38535 0.00000  0.00000  0.00000  370 PHE   I N   
2502  C CA  . PHE   A  370 ? 0.15288 0.15288 0.15288 0.00000  0.00000  0.00000  370 PHE   I CA  
2503  C C   . PHE   A  370 ? 0.32817 0.32817 0.32817 0.00000  0.00000  0.00000  370 PHE   I C   
2504  O O   . PHE   A  370 ? 0.30566 0.30566 0.30566 0.00000  0.00000  0.00000  370 PHE   I O   
2505  C CB  . PHE   A  370 ? 0.24766 0.24766 0.24766 0.00000  0.00000  0.00000  370 PHE   I CB  
2506  C CG  . PHE   A  370 ? 0.37441 0.37441 0.37441 0.00000  0.00000  0.00000  370 PHE   I CG  
2507  C CD1 . PHE   A  370 ? 0.25440 0.25440 0.25440 0.00000  0.00000  0.00000  370 PHE   I CD1 
2508  C CD2 . PHE   A  370 ? 0.43504 0.43504 0.43504 -0.00000 0.00000  0.00000  370 PHE   I CD2 
2509  C CE1 . PHE   A  370 ? 0.38307 0.38307 0.38307 0.00000  0.00000  0.00000  370 PHE   I CE1 
2510  C CE2 . PHE   A  370 ? 0.23724 0.23724 0.23724 0.00000  0.00000  0.00000  370 PHE   I CE2 
2511  C CZ  . PHE   A  370 ? 0.37666 0.37666 0.37666 0.00000  0.00000  0.00000  370 PHE   I CZ  
2512  N N   . ILE   A  371 ? 0.38394 0.38394 0.38394 -0.00000 0.00000  0.00000  371 ILE   I N   
2513  C CA  . ILE   A  371 ? 0.33048 0.33048 0.33048 0.00000  0.00000  0.00000  371 ILE   I CA  
2514  C C   . ILE   A  371 ? 0.34213 0.34213 0.34213 -0.00000 0.00000  0.00000  371 ILE   I C   
2515  O O   . ILE   A  371 ? 0.46761 0.46761 0.46761 0.00000  0.00000  -0.00000 371 ILE   I O   
2516  C CB  . ILE   A  371 ? 0.44593 0.44593 0.44593 0.00000  0.00000  0.00000  371 ILE   I CB  
2517  C CG1 . ILE   A  371 ? 0.31406 0.31406 0.31406 0.00000  0.00000  0.00000  371 ILE   I CG1 
2518  C CG2 . ILE   A  371 ? 0.26194 0.26194 0.26194 0.00000  0.00000  0.00000  371 ILE   I CG2 
2519  C CD1 . ILE   A  371 ? 0.28704 0.28704 0.28704 0.00000  -0.00000 0.00000  371 ILE   I CD1 
2520  N N   . GLY   A  372 ? 0.45487 0.45487 0.45487 0.00000  0.00000  -0.00000 372 GLY   I N   
2521  C CA  . GLY   A  372 ? 0.34465 0.34465 0.34465 0.00000  -0.00000 0.00000  372 GLY   I CA  
2522  C C   . GLY   A  372 ? 0.45014 0.45014 0.45014 0.00000  0.00000  0.00000  372 GLY   I C   
2523  O O   . GLY   A  372 ? 0.45232 0.45232 0.45232 -0.00000 0.00000  0.00000  372 GLY   I O   
2524  N N   . MET   A  373 ? 0.35778 0.35778 0.35778 -0.00000 0.00000  0.00000  373 MET   I N   
2525  C CA  . MET   A  373 ? 0.52287 0.52287 0.52287 0.00000  0.00000  0.00000  373 MET   I CA  
2526  C C   . MET   A  373 ? 0.49440 0.49440 0.49440 0.00000  0.00000  0.00000  373 MET   I C   
2527  O O   . MET   A  373 ? 0.43477 0.43477 0.43477 0.00000  0.00000  0.00000  373 MET   I O   
2528  C CB  . MET   A  373 ? 0.26962 0.26962 0.26962 0.00000  0.00000  0.00000  373 MET   I CB  
2529  C CG  . MET   A  373 ? 0.54602 0.54602 0.54602 0.00000  -0.00000 0.00000  373 MET   I CG  
2530  S SD  . MET   A  373 ? 0.46383 0.46383 0.46383 0.00000  0.00000  0.00000  373 MET   I SD  
2531  C CE  . MET   A  373 ? 0.15709 0.15709 0.15709 0.00000  0.00000  0.00000  373 MET   I CE  
2532  N N   . THR   A  374 ? 0.41599 0.41599 0.41599 -0.00000 0.00000  0.00000  374 THR   I N   
2533  C CA  . THR   A  374 ? 0.43336 0.43336 0.43336 -0.00000 0.00000  0.00000  374 THR   I CA  
2534  C C   . THR   A  374 ? 0.39421 0.39421 0.39421 -0.00000 0.00000  0.00000  374 THR   I C   
2535  O O   . THR   A  374 ? 0.52873 0.52873 0.52873 -0.00000 0.00000  0.00000  374 THR   I O   
2536  C CB  . THR   A  374 ? 0.54706 0.54706 0.54706 0.00000  0.00000  0.00000  374 THR   I CB  
2537  O OG1 . THR   A  374 ? 0.48314 0.48314 0.48314 0.00000  0.00000  0.00000  374 THR   I OG1 
2538  C CG2 . THR   A  374 ? 0.35168 0.35168 0.35168 -0.00000 0.00000  0.00000  374 THR   I CG2 
2539  N N   . GLU   A  375 ? 0.50794 0.50794 0.50794 0.00000  0.00000  0.00000  375 GLU   I N   
2540  C CA  . GLU   A  375 ? 0.35002 0.35002 0.35002 -0.00000 0.00000  0.00000  375 GLU   I CA  
2541  C C   . GLU   A  375 ? 0.53806 0.53806 0.53806 0.00000  0.00000  0.00000  375 GLU   I C   
2542  O O   . GLU   A  375 ? 0.36193 0.36193 0.36193 0.00000  0.00000  0.00000  375 GLU   I O   
2543  C CB  . GLU   A  375 ? 0.51287 0.51287 0.51287 0.00000  0.00000  0.00000  375 GLU   I CB  
2544  C CG  . GLU   A  375 ? 0.36919 0.36919 0.36919 -0.00000 0.00000  0.00000  375 GLU   I CG  
2545  C CD  . GLU   A  375 ? 0.50042 0.50042 0.50042 -0.00000 0.00000  0.00000  375 GLU   I CD  
2546  O OE1 . GLU   A  375 ? 0.56798 0.56798 0.56798 0.00000  0.00000  0.00000  375 GLU   I OE1 
2547  O OE2 . GLU   A  375 ? 0.55585 0.55585 0.55585 0.00000  0.00000  0.00000  375 GLU   I OE2 
2548  N N   . ILE   A  376 ? 0.32954 0.32954 0.32954 -0.00000 0.00000  0.00000  376 ILE   I N   
2549  C CA  . ILE   A  376 ? 0.33240 0.33240 0.33240 -0.00000 0.00000  0.00000  376 ILE   I CA  
2550  C C   . ILE   A  376 ? 0.38142 0.38142 0.38142 0.00000  0.00000  0.00000  376 ILE   I C   
2551  O O   . ILE   A  376 ? 0.47715 0.47715 0.47715 0.00000  -0.00000 0.00000  376 ILE   I O   
2552  C CB  . ILE   A  376 ? 0.47070 0.47070 0.47070 0.00000  0.00000  0.00000  376 ILE   I CB  
2553  C CG1 . ILE   A  376 ? 0.33686 0.33686 0.33686 -0.00000 -0.00000 0.00000  376 ILE   I CG1 
2554  C CG2 . ILE   A  376 ? 0.19299 0.19299 0.19299 0.00000  0.00000  0.00000  376 ILE   I CG2 
2555  C CD1 . ILE   A  376 ? 0.60067 0.60067 0.60067 0.00000  0.00000  0.00000  376 ILE   I CD1 
2556  N N   . SER   A  377 ? 0.35317 0.35317 0.35317 0.00000  0.00000  0.00000  377 SER   I N   
2557  C CA  . SER   A  377 ? 0.52465 0.52465 0.52465 0.00000  0.00000  0.00000  377 SER   I CA  
2558  C C   . SER   A  377 ? 0.32183 0.32183 0.32183 0.00000  0.00000  0.00000  377 SER   I C   
2559  O O   . SER   A  377 ? 0.62877 0.62877 0.62877 0.00000  0.00000  0.00000  377 SER   I O   
2560  C CB  . SER   A  377 ? 0.24398 0.24398 0.24398 0.00000  0.00000  0.00000  377 SER   I CB  
2561  O OG  . SER   A  377 ? 0.32096 0.32096 0.32096 0.00000  0.00000  0.00000  377 SER   I OG  
2562  N N   . THR   A  378 ? 0.48729 0.48729 0.48729 -0.00000 0.00000  0.00000  378 THR   I N   
2563  C CA  . THR   A  378 ? 0.31157 0.31157 0.31157 0.00000  0.00000  0.00000  378 THR   I CA  
2564  C C   . THR   A  378 ? 0.50610 0.50610 0.50610 0.00000  0.00000  0.00000  378 THR   I C   
2565  O O   . THR   A  378 ? 0.40142 0.40142 0.40142 0.00000  0.00000  0.00000  378 THR   I O   
2566  C CB  . THR   A  378 ? 0.47017 0.47017 0.47017 0.00000  0.00000  0.00000  378 THR   I CB  
2567  O OG1 . THR   A  378 ? 0.40423 0.40423 0.40423 0.00000  0.00000  0.00000  378 THR   I OG1 
2568  C CG2 . THR   A  378 ? 0.15622 0.15622 0.15622 0.00000  0.00000  0.00000  378 THR   I CG2 
2569  N N   . CYS   A  379 ? 0.30588 0.30588 0.30588 0.00000  0.00000  0.00000  379 CYS   I N   
2570  C CA  . CYS   A  379 ? 0.28412 0.28412 0.28412 -0.00000 0.00000  0.00000  379 CYS   I CA  
2571  C C   . CYS   A  379 ? 0.38633 0.38633 0.38633 -0.00000 0.00000  0.00000  379 CYS   I C   
2572  O O   . CYS   A  379 ? 0.45425 0.45425 0.45425 0.00000  0.00000  0.00000  379 CYS   I O   
2573  C CB  . CYS   A  379 ? 0.29148 0.29148 0.29148 0.00000  0.00000  0.00000  379 CYS   I CB  
2574  S SG  . CYS   A  379 ? 0.43745 0.43745 0.43745 -0.00000 0.00000  0.00000  379 CYS   I SG  
2575  N N   . GLU   A  380 ? 0.42112 0.42112 0.42112 0.00000  0.00000  0.00000  380 GLU   I N   
2576  C CA  . GLU   A  380 ? 0.23753 0.23753 0.23753 0.00000  0.00000  0.00000  380 GLU   I CA  
2577  C C   . GLU   A  380 ? 0.44388 0.44388 0.44388 0.00000  0.00000  0.00000  380 GLU   I C   
2578  O O   . GLU   A  380 ? 0.42944 0.42944 0.42944 0.00000  0.00000  0.00000  380 GLU   I O   
2579  C CB  . GLU   A  380 ? 0.38288 0.38288 0.38288 0.00000  0.00000  0.00000  380 GLU   I CB  
2580  C CG  . GLU   A  380 ? 0.54462 0.54462 0.54462 0.00000  0.00000  0.00000  380 GLU   I CG  
2581  C CD  . GLU   A  380 ? 0.49111 0.49111 0.49111 0.00000  0.00000  0.00000  380 GLU   I CD  
2582  O OE1 . GLU   A  380 ? 0.55476 0.55476 0.55476 -0.00000 0.00000  0.00000  380 GLU   I OE1 
2583  O OE2 . GLU   A  380 ? 0.64456 0.64456 0.64456 0.00000  0.00000  0.00000  380 GLU   I OE2 
2584  N N   . ALA   A  381 ? 0.32848 0.32848 0.32848 0.00000  0.00000  0.00000  381 ALA   I N   
2585  C CA  . ALA   A  381 ? 0.56276 0.56276 0.56276 0.00000  0.00000  0.00000  381 ALA   I CA  
2586  C C   . ALA   A  381 ? 0.44105 0.44105 0.44105 0.00000  0.00000  0.00000  381 ALA   I C   
2587  O O   . ALA   A  381 ? 0.44884 0.44884 0.44884 0.00000  0.00000  0.00000  381 ALA   I O   
2588  C CB  . ALA   A  381 ? 0.31556 0.31556 0.31556 -0.00000 0.00000  0.00000  381 ALA   I CB  
2589  N N   . THR   A  382 ? 0.39958 0.39958 0.39958 0.00000  0.00000  0.00000  382 THR   I N   
2590  C CA  . THR   A  382 ? 0.39429 0.39429 0.39429 0.00000  0.00000  0.00000  382 THR   I CA  
2591  C C   . THR   A  382 ? 0.33265 0.33265 0.33265 0.00000  0.00000  0.00000  382 THR   I C   
2592  O O   . THR   A  382 ? 0.68148 0.68148 0.68148 0.00000  0.00000  0.00000  382 THR   I O   
2593  C CB  . THR   A  382 ? 0.26400 0.26400 0.26400 -0.00000 0.00000  0.00000  382 THR   I CB  
2594  O OG1 . THR   A  382 ? 0.37661 0.37661 0.37661 -0.00000 0.00000  0.00000  382 THR   I OG1 
2595  C CG2 . THR   A  382 ? 0.40062 0.40062 0.40062 0.00000  0.00000  0.00000  382 THR   I CG2 
2596  N N   . VAL   A  383 ? 0.45975 0.45975 0.45975 -0.00000 0.00000  0.00000  383 VAL   I N   
2597  C CA  . VAL   A  383 ? 0.32472 0.32472 0.32472 0.00000  0.00000  0.00000  383 VAL   I CA  
2598  C C   . VAL   A  383 ? 0.50206 0.50206 0.50206 0.00000  0.00000  0.00000  383 VAL   I C   
2599  O O   . VAL   A  383 ? 0.44825 0.44825 0.44825 0.00000  0.00000  0.00000  383 VAL   I O   
2600  C CB  . VAL   A  383 ? 0.58705 0.58705 0.58705 -0.00000 0.00000  0.00000  383 VAL   I CB  
2601  C CG1 . VAL   A  383 ? 0.33442 0.33442 0.33442 0.00000  0.00000  0.00000  383 VAL   I CG1 
2602  C CG2 . VAL   A  383 ? 0.39406 0.39406 0.39406 0.00000  0.00000  0.00000  383 VAL   I CG2 
2603  N N   . SER   A  384 ? 0.57435 0.57435 0.57435 -0.00000 0.00000  0.00000  384 SER   I N   
2604  C CA  . SER   A  384 ? 0.32764 0.32764 0.32764 0.00000  0.00000  0.00000  384 SER   I CA  
2605  C C   . SER   A  384 ? 0.63664 0.63664 0.63664 -0.00000 0.00000  0.00000  384 SER   I C   
2606  O O   . SER   A  384 ? 0.49436 0.49436 0.49436 -0.00000 0.00000  0.00000  384 SER   I O   
2607  C CB  . SER   A  384 ? 0.35800 0.35800 0.35800 0.00000  0.00000  0.00000  384 SER   I CB  
2608  O OG  . SER   A  384 ? 0.70256 0.70256 0.70256 -0.00000 0.00000  0.00000  384 SER   I OG  
2609  N N   . GLU   A  385 ? 0.43864 0.43864 0.43864 0.00000  0.00000  0.00000  385 GLU   I N   
2610  C CA  . GLU   A  385 ? 0.54919 0.54919 0.54919 0.00000  0.00000  0.00000  385 GLU   I CA  
2611  C C   . GLU   A  385 ? 0.54434 0.54434 0.54434 0.00000  0.00000  0.00000  385 GLU   I C   
2612  O O   . GLU   A  385 ? 0.51845 0.51845 0.51845 0.00000  0.00000  0.00000  385 GLU   I O   
2613  C CB  . GLU   A  385 ? 0.26980 0.26980 0.26980 0.00000  0.00000  0.00000  385 GLU   I CB  
2614  C CG  . GLU   A  385 ? 0.44457 0.44457 0.44457 0.00000  0.00000  -0.00000 385 GLU   I CG  
2615  C CD  . GLU   A  385 ? 0.65873 0.65873 0.65873 0.00000  0.00000  0.00000  385 GLU   I CD  
2616  O OE1 . GLU   A  385 ? 0.63833 0.63833 0.63833 0.00000  0.00000  -0.00000 385 GLU   I OE1 
2617  O OE2 . GLU   A  385 ? 0.47573 0.47573 0.47573 0.00000  0.00000  0.00000  385 GLU   I OE2 
2618  N N   . GLY   A  386 ? 0.51363 0.51363 0.51363 0.00000  0.00000  0.00000  386 GLY   I N   
2619  C CA  . GLY   A  386 ? 0.33830 0.33830 0.33830 0.00000  0.00000  0.00000  386 GLY   I CA  
2620  C C   . GLY   A  386 ? 0.57526 0.57526 0.57526 0.00000  -0.00000 0.00000  386 GLY   I C   
2621  O O   . GLY   A  386 ? 0.50667 0.50667 0.50667 0.00000  0.00000  0.00000  386 GLY   I O   
2622  N N   . GLN   A  387 ? 0.45758 0.45758 0.45758 0.00000  0.00000  0.00000  387 GLN   I N   
2623  C CA  . GLN   A  387 ? 0.41567 0.41567 0.41567 0.00000  0.00000  0.00000  387 GLN   I CA  
2624  C C   . GLN   A  387 ? 0.65928 0.65928 0.65928 0.00000  0.00000  0.00000  387 GLN   I C   
2625  O O   . GLN   A  387 ? 0.57236 0.57236 0.57236 0.00000  0.00000  0.00000  387 GLN   I O   
2626  C CB  . GLN   A  387 ? 0.40117 0.40117 0.40117 0.00000  0.00000  0.00000  387 GLN   I CB  
2627  C CG  . GLN   A  387 ? 0.40831 0.40831 0.40831 0.00000  0.00000  0.00000  387 GLN   I CG  
2628  C CD  . GLN   A  387 ? 0.50964 0.50964 0.50964 0.00000  0.00000  0.00000  387 GLN   I CD  
2629  O OE1 . GLN   A  387 ? 0.57250 0.57250 0.57250 0.00000  0.00000  0.00000  387 GLN   I OE1 
2630  N NE2 . GLN   A  387 ? 0.42580 0.42580 0.42580 -0.00000 0.00000  0.00000  387 GLN   I NE2 
2631  N N   . HIS   A  388 ? 0.38423 0.38423 0.38423 0.00000  0.00000  0.00000  388 HIS   I N   
2632  C CA  . HIS   A  388 ? 0.52727 0.52727 0.52727 -0.00000 0.00000  0.00000  388 HIS   I CA  
2633  C C   . HIS   A  388 ? 0.70014 0.70014 0.70014 -0.00000 0.00000  0.00000  388 HIS   I C   
2634  O O   . HIS   A  388 ? 0.37190 0.37190 0.37190 0.00000  0.00000  0.00000  388 HIS   I O   
2635  C CB  . HIS   A  388 ? 0.24885 0.24885 0.24885 -0.00000 0.00000  0.00000  388 HIS   I CB  
2636  C CG  . HIS   A  388 ? 0.46837 0.46837 0.46837 0.00000  0.00000  0.00000  388 HIS   I CG  
2637  N ND1 . HIS   A  388 ? 0.48051 0.48051 0.48051 0.00000  0.00000  0.00000  388 HIS   I ND1 
2638  C CD2 . HIS   A  388 ? 0.32818 0.32818 0.32818 -0.00000 0.00000  0.00000  388 HIS   I CD2 
2639  C CE1 . HIS   A  388 ? 0.43385 0.43385 0.43385 -0.00000 0.00000  0.00000  388 HIS   I CE1 
2640  N NE2 . HIS   A  388 ? 0.38244 0.38244 0.38244 0.00000  0.00000  0.00000  388 HIS   I NE2 
2641  N N   . VAL   A  389 ? 0.31564 0.31564 0.31564 0.00000  -0.00000 0.00000  389 VAL   I N   
2642  C CA  . VAL   A  389 ? 0.47273 0.47273 0.47273 0.00000  0.00000  0.00000  389 VAL   I CA  
2643  C C   . VAL   A  389 ? 0.45935 0.45935 0.45935 0.00000  0.00000  0.00000  389 VAL   I C   
2644  O O   . VAL   A  389 ? 0.63835 0.63835 0.63835 0.00000  0.00000  0.00000  389 VAL   I O   
2645  C CB  . VAL   A  389 ? 0.53842 0.53842 0.53842 -0.00000 0.00000  0.00000  389 VAL   I CB  
2646  C CG1 . VAL   A  389 ? 0.34590 0.34590 0.34590 -0.00000 0.00000  0.00000  389 VAL   I CG1 
2647  C CG2 . VAL   A  389 ? 0.27355 0.27355 0.27355 -0.00000 -0.00000 0.00000  389 VAL   I CG2 
2648  N N   . ASN   A  390 ? 0.31976 0.31976 0.31976 0.00000  0.00000  0.00000  390 ASN   I N   
2649  C CA  . ASN   A  390 ? 0.36362 0.36362 0.36362 0.00000  0.00000  0.00000  390 ASN   I CA  
2650  C C   . ASN   A  390 ? 0.68484 0.68484 0.68484 0.00000  0.00000  0.00000  390 ASN   I C   
2651  O O   . ASN   A  390 ? 0.39955 0.39955 0.39955 -0.00000 0.00000  0.00000  390 ASN   I O   
2652  C CB  . ASN   A  390 ? 0.52447 0.52447 0.52447 0.00000  0.00000  0.00000  390 ASN   I CB  
2653  C CG  . ASN   A  390 ? 0.44276 0.44276 0.44276 0.00000  0.00000  0.00000  390 ASN   I CG  
2654  O OD1 . ASN   A  390 ? 0.57554 0.57554 0.57554 0.00000  0.00000  0.00000  390 ASN   I OD1 
2655  N ND2 . ASN   A  390 ? 0.56861 0.56861 0.56861 -0.00000 0.00000  0.00000  390 ASN   I ND2 
2656  N N   . ARG   A  391 ? 0.41475 0.41475 0.41475 -0.00000 0.00000  0.00000  391 ARG   I N   
2657  C CA  . ARG   A  391 ? 0.54894 0.54894 0.54894 -0.00000 0.00000  0.00000  391 ARG   I CA  
2658  C C   . ARG   A  391 ? 0.39705 0.39705 0.39705 0.00000  0.00000  0.00000  391 ARG   I C   
2659  O O   . ARG   A  391 ? 0.53231 0.53231 0.53231 0.00000  0.00000  0.00000  391 ARG   I O   
2660  C CB  . ARG   A  391 ? 0.28774 0.28774 0.28774 0.00000  0.00000  -0.00000 391 ARG   I CB  
2661  C CG  . ARG   A  391 ? 0.41022 0.41022 0.41022 -0.00000 -0.00000 0.00000  391 ARG   I CG  
2662  C CD  . ARG   A  391 ? 0.53165 0.53165 0.53165 -0.00000 0.00000  0.00000  391 ARG   I CD  
2663  N NE  . ARG   A  391 ? 0.43489 0.43489 0.43489 0.00000  -0.00000 0.00000  391 ARG   I NE  
2664  C CZ  . ARG   A  391 ? 0.96138 0.96138 0.96138 0.00000  0.00000  -0.00000 391 ARG   I CZ  
2665  N NH1 . ARG   A  391 ? 0.44711 0.44711 0.44711 0.00000  0.00000  0.00000  391 ARG   I NH1 
2666  N NH2 . ARG   A  391 ? 0.45912 0.45912 0.45912 -0.00000 0.00000  0.00000  391 ARG   I NH2 
2667  N N   . GLY   A  392 ? 0.31330 0.31330 0.31330 -0.00000 0.00000  0.00000  392 GLY   I N   
2668  C CA  . GLY   A  392 ? 0.26806 0.26806 0.26806 0.00000  0.00000  0.00000  392 GLY   I CA  
2669  C C   . GLY   A  392 ? 0.37927 0.37927 0.37927 0.00000  0.00000  0.00000  392 GLY   I C   
2670  O O   . GLY   A  392 ? 0.36123 0.36123 0.36123 -0.00000 0.00000  0.00000  392 GLY   I O   
2671  N N   . ASP   A  393 ? 0.28115 0.28115 0.28115 0.00000  0.00000  0.00000  393 ASP   I N   
2672  C CA  . ASP   A  393 ? 0.44188 0.44188 0.44188 0.00000  0.00000  0.00000  393 ASP   I CA  
2673  C C   . ASP   A  393 ? 0.37292 0.37292 0.37292 0.00000  0.00000  0.00000  393 ASP   I C   
2674  O O   . ASP   A  393 ? 0.61425 0.61425 0.61425 -0.00000 0.00000  0.00000  393 ASP   I O   
2675  C CB  . ASP   A  393 ? 0.32333 0.32333 0.32333 0.00000  0.00000  0.00000  393 ASP   I CB  
2676  C CG  . ASP   A  393 ? 0.68919 0.68919 0.68919 0.00000  0.00000  0.00000  393 ASP   I CG  
2677  O OD1 . ASP   A  393 ? 0.64616 0.64616 0.64616 0.00000  0.00000  0.00000  393 ASP   I OD1 
2678  O OD2 . ASP   A  393 ? 0.49545 0.49545 0.49545 0.00000  -0.00000 0.00000  393 ASP   I OD2 
2679  N N   . ASP   A  394 ? 0.57633 0.57633 0.57633 0.00000  0.00000  0.00000  394 ASP   I N   
2680  C CA  . ASP   A  394 ? 0.26878 0.26878 0.26878 0.00000  0.00000  0.00000  394 ASP   I CA  
2681  C C   . ASP   A  394 ? 0.60672 0.60672 0.60672 0.00000  0.00000  0.00000  394 ASP   I C   
2682  O O   . ASP   A  394 ? 0.38919 0.38919 0.38919 -0.00000 0.00000  0.00000  394 ASP   I O   
2683  C CB  . ASP   A  394 ? 0.51573 0.51573 0.51573 0.00000  0.00000  0.00000  394 ASP   I CB  
2684  C CG  . ASP   A  394 ? 0.38277 0.38277 0.38277 -0.00000 0.00000  0.00000  394 ASP   I CG  
2685  O OD1 . ASP   A  394 ? 0.94458 0.94458 0.94458 -0.00000 0.00000  0.00000  394 ASP   I OD1 
2686  O OD2 . ASP   A  394 ? 0.88442 0.88442 0.88442 -0.00000 0.00000  0.00000  394 ASP   I OD2 
2687  N N   . LEU   A  395 ? 0.31774 0.31774 0.31774 0.00000  0.00000  0.00000  395 LEU   I N   
2688  C CA  . LEU   A  395 ? 0.55764 0.55764 0.55764 -0.00000 0.00000  0.00000  395 LEU   I CA  
2689  C C   . LEU   A  395 ? 0.46816 0.46816 0.46816 0.00000  0.00000  0.00000  395 LEU   I C   
2690  O O   . LEU   A  395 ? 0.43605 0.43605 0.43605 0.00000  0.00000  0.00000  395 LEU   I O   
2691  C CB  . LEU   A  395 ? 0.27229 0.27229 0.27229 0.00000  0.00000  0.00000  395 LEU   I CB  
2692  C CG  . LEU   A  395 ? 0.45561 0.45561 0.45561 -0.00000 -0.00000 0.00000  395 LEU   I CG  
2693  C CD1 . LEU   A  395 ? 0.26559 0.26559 0.26559 -0.00000 0.00000  0.00000  395 LEU   I CD1 
2694  C CD2 . LEU   A  395 ? 0.39263 0.39263 0.39263 0.00000  0.00000  0.00000  395 LEU   I CD2 
2695  N N   . GLY   A  396 ? 0.41337 0.41337 0.41337 0.00000  0.00000  0.00000  396 GLY   I N   
2696  C CA  . GLY   A  396 ? 0.51974 0.51974 0.51974 0.00000  0.00000  0.00000  396 GLY   I CA  
2697  C C   . GLY   A  396 ? 0.47121 0.47121 0.47121 0.00000  0.00000  0.00000  396 GLY   I C   
2698  O O   . GLY   A  396 ? 0.51492 0.51492 0.51492 0.00000  0.00000  0.00000  396 GLY   I O   
2699  N N   . MET   A  397 ? 0.41468 0.41468 0.41468 0.00000  0.00000  0.00000  397 MET   I N   
2700  C CA  . MET   A  397 ? 0.40046 0.40046 0.40046 0.00000  0.00000  0.00000  397 MET   I CA  
2701  C C   . MET   A  397 ? 0.59690 0.59690 0.59690 0.00000  0.00000  0.00000  397 MET   I C   
2702  O O   . MET   A  397 ? 0.46048 0.46048 0.46048 -0.00000 0.00000  0.00000  397 MET   I O   
2703  C CB  . MET   A  397 ? 0.37290 0.37290 0.37290 0.00000  0.00000  0.00000  397 MET   I CB  
2704  C CG  . MET   A  397 ? 0.42965 0.42965 0.42965 0.00000  0.00000  0.00000  397 MET   I CG  
2705  S SD  . MET   A  397 ? 0.56138 0.56138 0.56138 -0.00000 0.00000  0.00000  397 MET   I SD  
2706  C CE  . MET   A  397 ? 0.28586 0.28586 0.28586 0.00000  -0.00000 0.00000  397 MET   I CE  
2707  N N   . PHE   A  398 ? 0.36902 0.36902 0.36902 -0.00000 0.00000  0.00000  398 PHE   I N   
2708  C CA  . PHE   A  398 ? 0.28394 0.28394 0.28394 -0.00000 0.00000  0.00000  398 PHE   I CA  
2709  C C   . PHE   A  398 ? 0.40780 0.40780 0.40780 0.00000  -0.00000 0.00000  398 PHE   I C   
2710  O O   . PHE   A  398 ? 0.53078 0.53078 0.53078 0.00000  0.00000  0.00000  398 PHE   I O   
2711  C CB  . PHE   A  398 ? 0.28498 0.28498 0.28498 0.00000  0.00000  0.00000  398 PHE   I CB  
2712  C CG  . PHE   A  398 ? 0.45781 0.45781 0.45781 0.00000  0.00000  0.00000  398 PHE   I CG  
2713  C CD1 . PHE   A  398 ? 0.28895 0.28895 0.28895 0.00000  0.00000  0.00000  398 PHE   I CD1 
2714  C CD2 . PHE   A  398 ? 0.37455 0.37455 0.37455 -0.00000 0.00000  0.00000  398 PHE   I CD2 
2715  C CE1 . PHE   A  398 ? 0.44144 0.44144 0.44144 -0.00000 0.00000  0.00000  398 PHE   I CE1 
2716  C CE2 . PHE   A  398 ? 0.32445 0.32445 0.32445 0.00000  0.00000  0.00000  398 PHE   I CE2 
2717  C CZ  . PHE   A  398 ? 0.41736 0.41736 0.41736 0.00000  0.00000  0.00000  398 PHE   I CZ  
2718  N N   . HIS   A  399 ? 0.49253 0.49253 0.49253 0.00000  0.00000  0.00000  399 HIS   I N   
2719  C CA  . HIS   A  399 ? 0.59884 0.59884 0.59884 0.00000  0.00000  0.00000  399 HIS   I CA  
2720  C C   . HIS   A  399 ? 0.32602 0.32602 0.32602 0.00000  0.00000  0.00000  399 HIS   I C   
2721  O O   . HIS   A  399 ? 0.68570 0.68570 0.68570 0.00000  0.00000  0.00000  399 HIS   I O   
2722  C CB  . HIS   A  399 ? 0.29437 0.29437 0.29437 0.00000  0.00000  0.00000  399 HIS   I CB  
2723  C CG  . HIS   A  399 ? 0.34191 0.34191 0.34191 -0.00000 0.00000  0.00000  399 HIS   I CG  
2724  N ND1 . HIS   A  399 ? 0.44380 0.44380 0.44380 0.00000  0.00000  0.00000  399 HIS   I ND1 
2725  C CD2 . HIS   A  399 ? 0.53732 0.53732 0.53732 -0.00000 0.00000  0.00000  399 HIS   I CD2 
2726  C CE1 . HIS   A  399 ? 0.66738 0.66738 0.66738 0.00000  0.00000  0.00000  399 HIS   I CE1 
2727  N NE2 . HIS   A  399 ? 0.30277 0.30277 0.30277 0.00000  0.00000  -0.00000 399 HIS   I NE2 
2728  N N   . PHE   A  400 ? 0.54617 0.54617 0.54617 -0.00000 0.00000  0.00000  400 PHE   I N   
2729  C CA  . PHE   A  400 ? 0.31147 0.31147 0.31147 -0.00000 0.00000  0.00000  400 PHE   I CA  
2730  C C   . PHE   A  400 ? 0.42078 0.42078 0.42078 0.00000  0.00000  0.00000  400 PHE   I C   
2731  O O   . PHE   A  400 ? 0.55364 0.55364 0.55364 0.00000  0.00000  0.00000  400 PHE   I O   
2732  C CB  . PHE   A  400 ? 0.53537 0.53537 0.53537 -0.00000 -0.00000 0.00000  400 PHE   I CB  
2733  C CG  . PHE   A  400 ? 0.28114 0.28114 0.28114 -0.00000 0.00000  0.00000  400 PHE   I CG  
2734  C CD1 . PHE   A  400 ? 0.52234 0.52234 0.52234 -0.00000 0.00000  0.00000  400 PHE   I CD1 
2735  C CD2 . PHE   A  400 ? 0.53491 0.53491 0.53491 0.00000  0.00000  0.00000  400 PHE   I CD2 
2736  C CE1 . PHE   A  400 ? 0.32815 0.32815 0.32815 0.00000  0.00000  0.00000  400 PHE   I CE1 
2737  C CE2 . PHE   A  400 ? 0.48230 0.48230 0.48230 -0.00000 0.00000  0.00000  400 PHE   I CE2 
2738  C CZ  . PHE   A  400 ? 0.51922 0.51922 0.51922 0.00000  0.00000  0.00000  400 PHE   I CZ  
2739  N N   . GLY   A  401 ? 0.36541 0.36541 0.36541 -0.00000 0.00000  -0.00000 401 GLY   I N   
2740  C CA  . GLY   A  401 ? 0.31384 0.31384 0.31384 0.00000  0.00000  0.00000  401 GLY   I CA  
2741  C C   . GLY   A  401 ? 0.44631 0.44631 0.44631 -0.00000 0.00000  0.00000  401 GLY   I C   
2742  O O   . GLY   A  401 ? 0.52474 0.52474 0.52474 0.00000  0.00000  0.00000  401 GLY   I O   
2743  N N   . GLY   A  402 ? 0.43277 0.43277 0.43277 0.00000  0.00000  0.00000  402 GLY   I N   
2744  C CA  . GLY   A  402 ? 0.33912 0.33912 0.33912 0.00000  0.00000  0.00000  402 GLY   I CA  
2745  C C   . GLY   A  402 ? 0.70942 0.70942 0.70942 0.00000  0.00000  0.00000  402 GLY   I C   
2746  O O   . GLY   A  402 ? 0.47661 0.47661 0.47661 0.00000  0.00000  0.00000  402 GLY   I O   
2747  O OXT . GLY   A  402 ? 0.59292 0.59292 0.59292 -0.00000 0.00000  0.00000  402 GLY   I OXT 
2748  N N   . SER   B  1   ? 0.32026 0.32026 0.32026 0.00000  0.00000  0.00000  404 SER   J N   
2749  C CA  . SER   B  1   ? 0.25845 0.25845 0.25845 0.00000  0.00000  0.00000  404 SER   J CA  
2750  C C   . SER   B  1   ? 0.40315 0.40315 0.40315 0.00000  0.00000  0.00000  404 SER   J C   
2751  O O   . SER   B  1   ? 0.44767 0.44767 0.44767 0.00000  0.00000  0.00000  404 SER   J O   
2752  C CB  . SER   B  1   ? 0.33792 0.33792 0.33792 0.00000  0.00000  0.00000  404 SER   J CB  
2753  O OG  . SER   B  1   ? 0.37260 0.37260 0.37260 0.00000  0.00000  0.00000  404 SER   J OG  
2754  N N   . PHE   B  2   ? 0.24197 0.24197 0.24197 -0.00000 0.00000  0.00000  405 PHE   J N   
2755  C CA  . PHE   B  2   ? 0.32144 0.32144 0.32144 0.00000  0.00000  0.00000  405 PHE   J CA  
2756  C C   . PHE   B  2   ? 0.29194 0.29194 0.29194 0.00000  0.00000  0.00000  405 PHE   J C   
2757  O O   . PHE   B  2   ? 0.40970 0.40970 0.40970 0.00000  0.00000  0.00000  405 PHE   J O   
2758  C CB  . PHE   B  2   ? 0.33006 0.33006 0.33006 -0.00000 -0.00000 0.00000  405 PHE   J CB  
2759  C CG  . PHE   B  2   ? 0.36137 0.36137 0.36137 -0.00000 -0.00000 -0.00000 405 PHE   J CG  
2760  C CD1 . PHE   B  2   ? 0.44108 0.44108 0.44108 -0.00000 0.00000  0.00000  405 PHE   J CD1 
2761  C CD2 . PHE   B  2   ? 0.40488 0.40488 0.40488 0.00000  0.00000  0.00000  405 PHE   J CD2 
2762  C CE1 . PHE   B  2   ? 0.36165 0.36165 0.36165 0.00000  0.00000  0.00000  405 PHE   J CE1 
2763  C CE2 . PHE   B  2   ? 0.31273 0.31273 0.31273 -0.00000 0.00000  0.00000  405 PHE   J CE2 
2764  C CZ  . PHE   B  2   ? 0.39110 0.39110 0.39110 0.00000  0.00000  0.00000  405 PHE   J CZ  
2765  N N   . ALA   B  3   ? 0.31459 0.31459 0.31459 -0.00000 0.00000  0.00000  406 ALA   J N   
2766  C CA  . ALA   B  3   ? 0.36844 0.36844 0.36844 0.00000  0.00000  0.00000  406 ALA   J CA  
2767  C C   . ALA   B  3   ? 0.40821 0.40821 0.40821 0.00000  0.00000  0.00000  406 ALA   J C   
2768  O O   . ALA   B  3   ? 0.39439 0.39439 0.39439 0.00000  0.00000  0.00000  406 ALA   J O   
2769  C CB  . ALA   B  3   ? 0.16326 0.16326 0.16326 0.00000  -0.00000 0.00000  406 ALA   J CB  
2770  N N   . LEU   B  4   ? 0.43352 0.43352 0.43352 0.00000  0.00000  0.00000  407 LEU   J N   
2771  C CA  . LEU   B  4   ? 0.42437 0.42437 0.42437 0.00000  0.00000  0.00000  407 LEU   J CA  
2772  C C   . LEU   B  4   ? 0.23716 0.23716 0.23716 0.00000  -0.00000 0.00000  407 LEU   J C   
2773  O O   . LEU   B  4   ? 0.48485 0.48485 0.48485 0.00000  0.00000  0.00000  407 LEU   J O   
2774  C CB  . LEU   B  4   ? 0.28440 0.28440 0.28440 0.00000  0.00000  0.00000  407 LEU   J CB  
2775  C CG  . LEU   B  4   ? 0.43294 0.43294 0.43294 0.00000  0.00000  0.00000  407 LEU   J CG  
2776  C CD1 . LEU   B  4   ? 0.26063 0.26063 0.26063 -0.00000 0.00000  0.00000  407 LEU   J CD1 
2777  C CD2 . LEU   B  4   ? 0.33596 0.33596 0.33596 0.00000  0.00000  0.00000  407 LEU   J CD2 
2778  N N   . GLY   B  5   ? 0.47960 0.47960 0.47960 -0.00000 0.00000  0.00000  408 GLY   J N   
2779  C CA  . GLY   B  5   ? 0.18465 0.18465 0.18465 0.00000  0.00000  0.00000  408 GLY   J CA  
2780  C C   . GLY   B  5   ? 0.38127 0.38127 0.38127 0.00000  0.00000  0.00000  408 GLY   J C   
2781  O O   . GLY   B  5   ? 0.46138 0.46138 0.46138 0.00000  0.00000  0.00000  408 GLY   J O   
2782  N N   . LEU   B  6   ? 0.33189 0.33189 0.33189 -0.00000 0.00000  0.00000  409 LEU   J N   
2783  C CA  . LEU   B  6   ? 0.57704 0.57704 0.57704 0.00000  0.00000  0.00000  409 LEU   J CA  
2784  C C   . LEU   B  6   ? 0.49340 0.49340 0.49340 0.00000  0.00000  0.00000  409 LEU   J C   
2785  O O   . LEU   B  6   ? 0.55755 0.55755 0.55755 0.00000  0.00000  0.00000  409 LEU   J O   
2786  C CB  . LEU   B  6   ? 0.46662 0.46662 0.46662 -0.00000 0.00000  0.00000  409 LEU   J CB  
2787  C CG  . LEU   B  6   ? 0.55369 0.55369 0.55369 0.00000  0.00000  0.00000  409 LEU   J CG  
2788  C CD1 . LEU   B  6   ? 0.37742 0.37742 0.37742 0.00000  -0.00000 -0.00000 409 LEU   J CD1 
2789  C CD2 . LEU   B  6   ? 0.32108 0.32108 0.32108 -0.00000 0.00000  0.00000  409 LEU   J CD2 
2790  N N   . ARG   B  7   ? 0.46837 0.46837 0.46837 0.00000  0.00000  0.00000  410 ARG   J N   
2791  C CA  . ARG   B  7   ? 0.45225 0.45225 0.45225 -0.00000 0.00000  0.00000  410 ARG   J CA  
2792  C C   . ARG   B  7   ? 0.52696 0.52696 0.52696 0.00000  0.00000  0.00000  410 ARG   J C   
2793  O O   . ARG   B  7   ? 0.66961 0.66961 0.66961 0.00000  -0.00000 0.00000  410 ARG   J O   
2794  C CB  . ARG   B  7   ? 0.28570 0.28570 0.28570 0.00000  0.00000  0.00000  410 ARG   J CB  
2795  C CG  . ARG   B  7   ? 0.31114 0.31114 0.31114 0.00000  0.00000  0.00000  410 ARG   J CG  
2796  C CD  . ARG   B  7   ? 0.45356 0.45356 0.45356 0.00000  0.00000  0.00000  410 ARG   J CD  
2797  N NE  . ARG   B  7   ? 0.69538 0.69538 0.69538 0.00000  0.00000  0.00000  410 ARG   J NE  
2798  C CZ  . ARG   B  7   ? 0.57963 0.57963 0.57963 0.00000  0.00000  0.00000  410 ARG   J CZ  
2799  N NH1 . ARG   B  7   ? 0.62223 0.62223 0.62223 0.00000  0.00000  0.00000  410 ARG   J NH1 
2800  N NH2 . ARG   B  7   ? 0.69650 0.69650 0.69650 0.00000  -0.00000 0.00000  410 ARG   J NH2 
2801  N N   . LYS   B  8   ? 0.50754 0.50754 0.50754 0.00000  0.00000  0.00000  411 LYS   J N   
2802  C CA  . LYS   B  8   ? 0.73628 0.73628 0.73628 0.00000  0.00000  0.00000  411 LYS   J CA  
2803  C C   . LYS   B  8   ? 0.63781 0.63781 0.63781 -0.00000 0.00000  0.00000  411 LYS   J C   
2804  O O   . LYS   B  8   ? 0.59869 0.59869 0.59869 0.00000  0.00000  0.00000  411 LYS   J O   
2805  C CB  . LYS   B  8   ? 0.38318 0.38318 0.38318 0.00000  0.00000  0.00000  411 LYS   J CB  
2806  N N   . ASP   B  9   ? 0.46973 0.46973 0.46973 -0.00000 -0.00000 -0.00000 412 ASP   J N   
2807  C CA  . ASP   B  9   ? 1.12108 1.12108 1.12108 0.00000  0.00000  0.00000  412 ASP   J CA  
2808  C C   . ASP   B  9   ? 0.55516 0.55516 0.55516 0.00000  0.00000  0.00000  412 ASP   J C   
2809  O O   . ASP   B  9   ? 0.94242 0.94242 0.94242 0.00000  -0.00000 -0.00000 412 ASP   J O   
2810  C CB  . ASP   B  9   ? 0.78616 0.78616 0.78616 -0.00000 -0.00000 0.00000  412 ASP   J CB  
2811  C CG  . ASP   B  9   ? 0.90563 0.90563 0.90563 0.00000  0.00000  0.00000  412 ASP   J CG  
2812  O OD1 . ASP   B  9   ? 0.93843 0.93843 0.93843 0.00000  0.00000  0.00000  412 ASP   J OD1 
2813  O OD2 . ASP   B  9   ? 1.22544 1.22544 1.22544 0.00000  0.00000  0.00000  412 ASP   J OD2 
2814  N N   . CYS   B  10  ? 0.99183 0.99183 0.99183 0.00000  0.00000  0.00000  413 CYS   J N   
2815  C CA  . CYS   B  10  ? 0.69955 0.69955 0.69955 0.00000  0.00000  0.00000  413 CYS   J CA  
2816  C C   . CYS   B  10  ? 0.83314 0.83314 0.83314 0.00000  0.00000  0.00000  413 CYS   J C   
2817  O O   . CYS   B  10  ? 0.80787 0.80787 0.80787 0.00000  0.00000  0.00000  413 CYS   J O   
2818  C CB  . CYS   B  10  ? 0.59174 0.59174 0.59174 0.00000  0.00000  0.00000  413 CYS   J CB  
2819  S SG  . CYS   B  10  ? 0.74215 0.74215 0.74215 -0.00000 0.00000  0.00000  413 CYS   J SG  
2820  N N   . ARG   B  11  ? 0.80729 0.80729 0.80729 0.00000  0.00000  0.00000  414 ARG   J N   
2821  C CA  . ARG   B  11  ? 1.09055 1.09055 1.09055 0.00000  0.00000  0.00000  414 ARG   J CA  
2822  C C   . ARG   B  11  ? 1.23405 1.23405 1.23405 0.00000  0.00000  0.00000  414 ARG   J C   
2823  O O   . ARG   B  11  ? 0.88631 0.88631 0.88631 0.00000  0.00000  0.00000  414 ARG   J O   
2824  C CB  . ARG   B  11  ? 0.73150 0.73150 0.73150 0.00000  0.00000  0.00000  414 ARG   J CB  
2825  N N   . ALA   B  12  ? 0.98492 0.98492 0.98492 0.00000  0.00000  0.00000  415 ALA   J N   
2826  C CA  . ALA   B  12  ? 0.84434 0.84434 0.84434 0.00000  0.00000  0.00000  415 ALA   J CA  
2827  C C   . ALA   B  12  ? 0.76681 0.76681 0.76681 -0.00000 0.00000  0.00000  415 ALA   J C   
2828  O O   . ALA   B  12  ? 1.11700 1.11700 1.11700 0.00000  0.00000  0.00000  415 ALA   J O   
2829  C CB  . ALA   B  12  ? 0.58696 0.58696 0.58696 -0.00000 0.00000  0.00000  415 ALA   J CB  
2830  N N   . GLU   B  13  ? 0.49691 0.49691 0.49691 0.00000  0.00000  0.00000  416 GLU   J N   
2831  C CA  . GLU   B  13  ? 0.67022 0.67022 0.67022 0.00000  0.00000  0.00000  416 GLU   J CA  
2832  C C   . GLU   B  13  ? 0.69935 0.69935 0.69935 0.00000  0.00000  0.00000  416 GLU   J C   
2833  O O   . GLU   B  13  ? 0.76480 0.76480 0.76480 0.00000  0.00000  0.00000  416 GLU   J O   
2834  C CB  . GLU   B  13  ? 0.53443 0.53443 0.53443 0.00000  0.00000  0.00000  416 GLU   J CB  
2835  N N   . ILE   B  14  ? 0.62904 0.62904 0.62904 0.00000  0.00000  0.00000  417 ILE   J N   
2836  C CA  . ILE   B  14  ? 0.72689 0.72689 0.72689 0.00000  0.00000  0.00000  417 ILE   J CA  
2837  C C   . ILE   B  14  ? 0.60203 0.60203 0.60203 0.00000  0.00000  0.00000  417 ILE   J C   
2838  O O   . ILE   B  14  ? 0.70764 0.70764 0.70764 0.00000  0.00000  0.00000  417 ILE   J O   
2839  C CB  . ILE   B  14  ? 0.47817 0.47817 0.47817 0.00000  0.00000  0.00000  417 ILE   J CB  
2840  C CG1 . ILE   B  14  ? 0.52086 0.52086 0.52086 0.00000  0.00000  0.00000  417 ILE   J CG1 
2841  C CG2 . ILE   B  14  ? 0.56705 0.56705 0.56705 0.00000  0.00000  0.00000  417 ILE   J CG2 
2842  C CD1 . ILE   B  14  ? 0.64836 0.64836 0.64836 0.00000  0.00000  0.00000  417 ILE   J CD1 
2843  N N   . VAL   B  15  ? 0.68262 0.68262 0.68262 0.00000  0.00000  0.00000  418 VAL   J N   
2844  C CA  . VAL   B  15  ? 0.45084 0.45084 0.45084 0.00000  0.00000  0.00000  418 VAL   J CA  
2845  C C   . VAL   B  15  ? 0.49891 0.49891 0.49891 0.00000  0.00000  0.00000  418 VAL   J C   
2846  O O   . VAL   B  15  ? 0.75352 0.75352 0.75352 -0.00000 0.00000  0.00000  418 VAL   J O   
2847  C CB  . VAL   B  15  ? 0.74674 0.74674 0.74674 0.00000  0.00000  0.00000  418 VAL   J CB  
2848  C CG1 . VAL   B  15  ? 0.34542 0.34542 0.34542 -0.00000 0.00000  0.00000  418 VAL   J CG1 
2849  C CG2 . VAL   B  15  ? 0.32349 0.32349 0.32349 0.00000  0.00000  0.00000  418 VAL   J CG2 
2850  N N   . GLU   B  16  ? 0.69936 0.69936 0.69936 0.00000  0.00000  0.00000  419 GLU   J N   
2851  C CA  . GLU   B  16  ? 0.56601 0.56601 0.56601 -0.00000 0.00000  0.00000  419 GLU   J CA  
2852  C C   . GLU   B  16  ? 0.69825 0.69825 0.69825 0.00000  0.00000  0.00000  419 GLU   J C   
2853  O O   . GLU   B  16  ? 0.69977 0.69977 0.69977 0.00000  0.00000  0.00000  419 GLU   J O   
2854  C CB  . GLU   B  16  ? 0.57479 0.57479 0.57479 0.00000  0.00000  0.00000  419 GLU   J CB  
2855  N N   . LYS   B  17  ? 0.56556 0.56556 0.56556 0.00000  0.00000  0.00000  420 LYS   J N   
2856  C CA  . LYS   B  17  ? 0.59414 0.59414 0.59414 0.00000  0.00000  0.00000  420 LYS   J CA  
2857  C C   . LYS   B  17  ? 0.67670 0.67670 0.67670 -0.00000 0.00000  0.00000  420 LYS   J C   
2858  O O   . LYS   B  17  ? 0.65645 0.65645 0.65645 0.00000  0.00000  0.00000  420 LYS   J O   
2859  C CB  . LYS   B  17  ? 0.37217 0.37217 0.37217 -0.00000 0.00000  0.00000  420 LYS   J CB  
2860  C CG  . LYS   B  17  ? 0.43549 0.43549 0.43549 0.00000  0.00000  0.00000  420 LYS   J CG  
2861  C CD  . LYS   B  17  ? 0.70319 0.70319 0.70319 0.00000  0.00000  0.00000  420 LYS   J CD  
2862  C CE  . LYS   B  17  ? 0.82726 0.82726 0.82726 0.00000  0.00000  0.00000  420 LYS   J CE  
2863  N NZ  . LYS   B  17  ? 1.11723 1.11723 1.11723 -0.00000 0.00000  0.00000  420 LYS   J NZ  
2864  N N   . PHE   B  18  ? 0.52987 0.52987 0.52987 0.00000  0.00000  0.00000  421 PHE   J N   
2865  C CA  . PHE   B  18  ? 0.82975 0.82975 0.82975 -0.00000 0.00000  0.00000  421 PHE   J CA  
2866  C C   . PHE   B  18  ? 0.66773 0.66773 0.66773 -0.00000 0.00000  0.00000  421 PHE   J C   
2867  O O   . PHE   B  18  ? 0.60078 0.60078 0.60078 -0.00000 0.00000  0.00000  421 PHE   J O   
2868  C CB  . PHE   B  18  ? 0.38835 0.38835 0.38835 -0.00000 0.00000  0.00000  421 PHE   J CB  
2869  C CG  . PHE   B  18  ? 0.53058 0.53058 0.53058 -0.00000 0.00000  0.00000  421 PHE   J CG  
2870  C CD1 . PHE   B  18  ? 0.52348 0.52348 0.52348 0.00000  0.00000  0.00000  421 PHE   J CD1 
2871  C CD2 . PHE   B  18  ? 0.74368 0.74368 0.74368 -0.00000 0.00000  0.00000  421 PHE   J CD2 
2872  C CE1 . PHE   B  18  ? 0.42614 0.42614 0.42614 0.00000  0.00000  0.00000  421 PHE   J CE1 
2873  C CE2 . PHE   B  18  ? 0.62191 0.62191 0.62191 -0.00000 0.00000  0.00000  421 PHE   J CE2 
2874  C CZ  . PHE   B  18  ? 0.69375 0.69375 0.69375 0.00000  0.00000  0.00000  421 PHE   J CZ  
2875  N N   . THR   B  19  ? 0.52479 0.52479 0.52479 0.00000  -0.00000 0.00000  422 THR   J N   
2876  C CA  . THR   B  19  ? 0.40094 0.40094 0.40094 0.00000  0.00000  0.00000  422 THR   J CA  
2877  C C   . THR   B  19  ? 0.50287 0.50287 0.50287 0.00000  0.00000  0.00000  422 THR   J C   
2878  O O   . THR   B  19  ? 0.47925 0.47925 0.47925 -0.00000 0.00000  0.00000  422 THR   J O   
2879  C CB  . THR   B  19  ? 0.54817 0.54817 0.54817 0.00000  -0.00000 0.00000  422 THR   J CB  
2880  O OG1 . THR   B  19  ? 0.50009 0.50009 0.50009 -0.00000 0.00000  0.00000  422 THR   J OG1 
2881  C CG2 . THR   B  19  ? 0.57251 0.57251 0.57251 0.00000  0.00000  0.00000  422 THR   J CG2 
2882  N N   . GLU   B  20  ? 0.65832 0.65832 0.65832 0.00000  0.00000  0.00000  423 GLU   J N   
2883  C CA  . GLU   B  20  ? 0.63666 0.63666 0.63666 0.00000  0.00000  0.00000  423 GLU   J CA  
2884  C C   . GLU   B  20  ? 0.51571 0.51571 0.51571 0.00000  0.00000  0.00000  423 GLU   J C   
2885  O O   . GLU   B  20  ? 0.71547 0.71547 0.71547 -0.00000 -0.00000 0.00000  423 GLU   J O   
2886  C CB  . GLU   B  20  ? 0.46282 0.46282 0.46282 0.00000  0.00000  0.00000  423 GLU   J CB  
2887  N N   . PRO   B  21  ? 0.45794 0.45794 0.45794 0.00000  0.00000  0.00000  424 PRO   J N   
2888  C CA  . PRO   B  21  ? 0.62816 0.62816 0.62816 -0.00000 0.00000  0.00000  424 PRO   J CA  
2889  C C   . PRO   B  21  ? 0.44596 0.44596 0.44596 0.00000  0.00000  0.00000  424 PRO   J C   
2890  O O   . PRO   B  21  ? 0.55612 0.55612 0.55612 0.00000  0.00000  -0.00000 424 PRO   J O   
2891  C CB  . PRO   B  21  ? 0.22928 0.22928 0.22928 0.00000  0.00000  0.00000  424 PRO   J CB  
2892  C CG  . PRO   B  21  ? 0.42076 0.42076 0.42076 -0.00000 0.00000  0.00000  424 PRO   J CG  
2893  C CD  . PRO   B  21  ? 0.40418 0.40418 0.40418 0.00000  0.00000  0.00000  424 PRO   J CD  
2894  N N   . GLY   B  22  ? 0.49146 0.49146 0.49146 -0.00000 0.00000  0.00000  425 GLY   J N   
2895  C CA  . GLY   B  22  ? 0.27206 0.27206 0.27206 -0.00000 0.00000  0.00000  425 GLY   J CA  
2896  C C   . GLY   B  22  ? 0.38148 0.38148 0.38148 0.00000  0.00000  0.00000  425 GLY   J C   
2897  O O   . GLY   B  22  ? 0.45593 0.45593 0.45593 0.00000  0.00000  0.00000  425 GLY   J O   
2898  N N   . THR   B  23  ? 0.36670 0.36670 0.36670 0.00000  0.00000  0.00000  426 THR   J N   
2899  C CA  . THR   B  23  ? 0.33718 0.33718 0.33718 -0.00000 0.00000  0.00000  426 THR   J CA  
2900  C C   . THR   B  23  ? 0.33684 0.33684 0.33684 -0.00000 0.00000  0.00000  426 THR   J C   
2901  O O   . THR   B  23  ? 0.70756 0.70756 0.70756 -0.00000 -0.00000 0.00000  426 THR   J O   
2902  C CB  . THR   B  23  ? 0.44701 0.44701 0.44701 -0.00000 0.00000  0.00000  426 THR   J CB  
2903  O OG1 . THR   B  23  ? 0.55212 0.55212 0.55212 -0.00000 0.00000  0.00000  426 THR   J OG1 
2904  C CG2 . THR   B  23  ? 0.32592 0.32592 0.32592 0.00000  0.00000  0.00000  426 THR   J CG2 
2905  N N   . VAL   B  24  ? 0.72843 0.72843 0.72843 0.00000  0.00000  0.00000  427 VAL   J N   
2906  C CA  . VAL   B  24  ? 0.48987 0.48987 0.48987 0.00000  0.00000  0.00000  427 VAL   J CA  
2907  C C   . VAL   B  24  ? 0.41965 0.41965 0.41965 -0.00000 0.00000  0.00000  427 VAL   J C   
2908  O O   . VAL   B  24  ? 0.73444 0.73444 0.73444 0.00000  0.00000  0.00000  427 VAL   J O   
2909  C CB  . VAL   B  24  ? 0.39955 0.39955 0.39955 0.00000  0.00000  0.00000  427 VAL   J CB  
2910  C CG1 . VAL   B  24  ? 0.30759 0.30759 0.30759 0.00000  0.00000  0.00000  427 VAL   J CG1 
2911  C CG2 . VAL   B  24  ? 0.39887 0.39887 0.39887 0.00000  0.00000  0.00000  427 VAL   J CG2 
2912  N N   . ILE   B  25  ? 0.67785 0.67785 0.67785 0.00000  0.00000  0.00000  428 ILE   J N   
2913  C CA  . ILE   B  25  ? 0.28392 0.28392 0.28392 0.00000  -0.00000 0.00000  428 ILE   J CA  
2914  C C   . ILE   B  25  ? 0.55510 0.55510 0.55510 -0.00000 0.00000  0.00000  428 ILE   J C   
2915  O O   . ILE   B  25  ? 0.44492 0.44492 0.44492 -0.00000 0.00000  0.00000  428 ILE   J O   
2916  C CB  . ILE   B  25  ? 0.51704 0.51704 0.51704 -0.00000 0.00000  0.00000  428 ILE   J CB  
2917  C CG1 . ILE   B  25  ? 0.40139 0.40139 0.40139 0.00000  0.00000  0.00000  428 ILE   J CG1 
2918  C CG2 . ILE   B  25  ? 0.24895 0.24895 0.24895 0.00000  0.00000  0.00000  428 ILE   J CG2 
2919  C CD1 . ILE   B  25  ? 0.33336 0.33336 0.33336 0.00000  0.00000  0.00000  428 ILE   J CD1 
2920  N N   . ARG   B  26  ? 0.44628 0.44628 0.44628 -0.00000 0.00000  0.00000  429 ARG   J N   
2921  C CA  . ARG   B  26  ? 0.43124 0.43124 0.43124 0.00000  0.00000  0.00000  429 ARG   J CA  
2922  C C   . ARG   B  26  ? 0.43795 0.43795 0.43795 0.00000  0.00000  0.00000  429 ARG   J C   
2923  O O   . ARG   B  26  ? 0.42579 0.42579 0.42579 -0.00000 0.00000  0.00000  429 ARG   J O   
2924  C CB  . ARG   B  26  ? 0.53274 0.53274 0.53274 -0.00000 0.00000  0.00000  429 ARG   J CB  
2925  C CG  . ARG   B  26  ? 0.45394 0.45394 0.45394 -0.00000 0.00000  0.00000  429 ARG   J CG  
2926  C CD  . ARG   B  26  ? 0.62647 0.62647 0.62647 -0.00000 0.00000  0.00000  429 ARG   J CD  
2927  N NE  . ARG   B  26  ? 0.44641 0.44641 0.44641 -0.00000 0.00000  0.00000  429 ARG   J NE  
2928  C CZ  . ARG   B  26  ? 2.12459 2.12459 2.12459 0.00000  0.00000  0.00000  429 ARG   J CZ  
2929  N NH1 . ARG   B  26  ? 0.39116 0.39116 0.39116 0.00000  0.00000  0.00000  429 ARG   J NH1 
2930  N NH2 . ARG   B  26  ? 0.47762 0.47762 0.47762 0.00000  -0.00000 0.00000  429 ARG   J NH2 
2931  N N   . ILE   B  27  ? 0.21653 0.21653 0.21653 -0.00000 -0.00000 0.00000  430 ILE   J N   
2932  C CA  . ILE   B  27  ? 0.43682 0.43682 0.43682 -0.00000 0.00000  0.00000  430 ILE   J CA  
2933  C C   . ILE   B  27  ? 0.28017 0.28017 0.28017 0.00000  0.00000  0.00000  430 ILE   J C   
2934  O O   . ILE   B  27  ? 0.61962 0.61962 0.61962 0.00000  -0.00000 0.00000  430 ILE   J O   
2935  C CB  . ILE   B  27  ? 0.35455 0.35455 0.35455 0.00000  0.00000  0.00000  430 ILE   J CB  
2936  C CG1 . ILE   B  27  ? 0.28469 0.28469 0.28469 0.00000  0.00000  0.00000  430 ILE   J CG1 
2937  C CG2 . ILE   B  27  ? 0.33067 0.33067 0.33067 -0.00000 0.00000  0.00000  430 ILE   J CG2 
2938  C CD1 . ILE   B  27  ? 0.24902 0.24902 0.24902 -0.00000 0.00000  0.00000  430 ILE   J CD1 
2939  N N   . ASN   B  28  ? 0.59695 0.59695 0.59695 -0.00000 0.00000  0.00000  431 ASN   J N   
2940  C CA  . ASN   B  28  ? 0.33671 0.33671 0.33671 0.00000  0.00000  0.00000  431 ASN   J CA  
2941  C C   . ASN   B  28  ? 0.48322 0.48322 0.48322 0.00000  0.00000  0.00000  431 ASN   J C   
2942  O O   . ASN   B  28  ? 0.36347 0.36347 0.36347 -0.00000 0.00000  0.00000  431 ASN   J O   
2943  C CB  . ASN   B  28  ? 0.28186 0.28186 0.28186 0.00000  0.00000  0.00000  431 ASN   J CB  
2944  C CG  . ASN   B  28  ? 0.43270 0.43270 0.43270 0.00000  0.00000  0.00000  431 ASN   J CG  
2945  O OD1 . ASN   B  28  ? 0.49540 0.49540 0.49540 0.00000  0.00000  0.00000  431 ASN   J OD1 
2946  N ND2 . ASN   B  28  ? 0.33325 0.33325 0.33325 -0.00000 0.00000  0.00000  431 ASN   J ND2 
2947  N N   . GLU   B  29  ? 0.28387 0.28387 0.28387 0.00000  0.00000  0.00000  432 GLU   J N   
2948  C CA  . GLU   B  29  ? 0.39337 0.39337 0.39337 0.00000  0.00000  0.00000  432 GLU   J CA  
2949  C C   . GLU   B  29  ? 0.33989 0.33989 0.33989 -0.00000 0.00000  0.00000  432 GLU   J C   
2950  O O   . GLU   B  29  ? 0.53572 0.53572 0.53572 -0.00000 0.00000  0.00000  432 GLU   J O   
2951  C CB  . GLU   B  29  ? 0.19296 0.19296 0.19296 0.00000  0.00000  0.00000  432 GLU   J CB  
2952  C CG  . GLU   B  29  ? 0.36117 0.36117 0.36117 -0.00000 0.00000  0.00000  432 GLU   J CG  
2953  C CD  . GLU   B  29  ? 0.66993 0.66993 0.66993 0.00000  0.00000  0.00000  432 GLU   J CD  
2954  O OE1 . GLU   B  29  ? 0.48013 0.48013 0.48013 0.00000  0.00000  0.00000  432 GLU   J OE1 
2955  O OE2 . GLU   B  29  ? 0.55933 0.55933 0.55933 -0.00000 0.00000  0.00000  432 GLU   J OE2 
2956  N N   . VAL   B  30  ? 0.59866 0.59866 0.59866 -0.00000 0.00000  0.00000  433 VAL   J N   
2957  C CA  . VAL   B  30  ? 0.28604 0.28604 0.28604 0.00000  0.00000  0.00000  433 VAL   J CA  
2958  C C   . VAL   B  30  ? 0.54064 0.54064 0.54064 0.00000  0.00000  0.00000  433 VAL   J C   
2959  O O   . VAL   B  30  ? 0.42458 0.42458 0.42458 0.00000  0.00000  0.00000  433 VAL   J O   
2960  C CB  . VAL   B  30  ? 0.55140 0.55140 0.55140 -0.00000 0.00000  0.00000  433 VAL   J CB  
2961  C CG1 . VAL   B  30  ? 0.42257 0.42257 0.42257 -0.00000 0.00000  0.00000  433 VAL   J CG1 
2962  C CG2 . VAL   B  30  ? 0.35640 0.35640 0.35640 -0.00000 0.00000  0.00000  433 VAL   J CG2 
2963  N N   . VAL   B  31  ? 0.45693 0.45693 0.45693 0.00000  0.00000  0.00000  434 VAL   J N   
2964  C CA  . VAL   B  31  ? 0.59727 0.59727 0.59727 0.00000  0.00000  0.00000  434 VAL   J CA  
2965  C C   . VAL   B  31  ? 0.44019 0.44019 0.44019 0.00000  0.00000  0.00000  434 VAL   J C   
2966  O O   . VAL   B  31  ? 0.42982 0.42982 0.42982 0.00000  0.00000  0.00000  434 VAL   J O   
2967  C CB  . VAL   B  31  ? 0.47468 0.47468 0.47468 0.00000  0.00000  -0.00000 434 VAL   J CB  
2968  C CG1 . VAL   B  31  ? 0.26905 0.26905 0.26905 0.00000  0.00000  -0.00000 434 VAL   J CG1 
2969  C CG2 . VAL   B  31  ? 0.30171 0.30171 0.30171 -0.00000 0.00000  0.00000  434 VAL   J CG2 
2970  N N   . ALA   B  32  ? 0.35563 0.35563 0.35563 0.00000  0.00000  0.00000  435 ALA   J N   
2971  C CA  . ALA   B  32  ? 0.39714 0.39714 0.39714 0.00000  0.00000  0.00000  435 ALA   J CA  
2972  C C   . ALA   B  32  ? 0.52307 0.52307 0.52307 0.00000  0.00000  0.00000  435 ALA   J C   
2973  O O   . ALA   B  32  ? 0.42263 0.42263 0.42263 0.00000  0.00000  0.00000  435 ALA   J O   
2974  C CB  . ALA   B  32  ? 0.31732 0.31732 0.31732 0.00000  0.00000  0.00000  435 ALA   J CB  
2975  N N   . ALA   B  33  ? 0.41006 0.41006 0.41006 0.00000  0.00000  0.00000  436 ALA   J N   
2976  C CA  . ALA   B  33  ? 0.52402 0.52402 0.52402 0.00000  0.00000  0.00000  436 ALA   J CA  
2977  C C   . ALA   B  33  ? 0.77254 0.77254 0.77254 0.00000  0.00000  0.00000  436 ALA   J C   
2978  O O   . ALA   B  33  ? 0.48626 0.48626 0.48626 -0.00000 0.00000  0.00000  436 ALA   J O   
2979  C CB  . ALA   B  33  ? 0.32268 0.32268 0.32268 0.00000  0.00000  0.00000  436 ALA   J CB  
2980  N N   . LEU   B  34  ? 0.51578 0.51578 0.51578 0.00000  0.00000  0.00000  437 LEU   J N   
2981  C CA  . LEU   B  34  ? 0.89225 0.89225 0.89225 -0.00000 0.00000  0.00000  437 LEU   J CA  
2982  C C   . LEU   B  34  ? 0.48532 0.48532 0.48532 0.00000  0.00000  0.00000  437 LEU   J C   
2983  O O   . LEU   B  34  ? 0.57065 0.57065 0.57065 0.00000  0.00000  0.00000  437 LEU   J O   
2984  C CB  . LEU   B  34  ? 0.47039 0.47039 0.47039 -0.00000 0.00000  0.00000  437 LEU   J CB  
2985  C CG  . LEU   B  34  ? 0.78858 0.78858 0.78858 -0.00000 0.00000  0.00000  437 LEU   J CG  
2986  C CD1 . LEU   B  34  ? 0.54990 0.54990 0.54990 0.00000  0.00000  0.00000  437 LEU   J CD1 
2987  C CD2 . LEU   B  34  ? 0.82346 0.82346 0.82346 -0.00000 0.00000  0.00000  437 LEU   J CD2 
2988  N N   . LEU   C  57  ? 0.41381 0.41381 0.41381 0.00000  0.00000  0.00000  57  LEU   G N   
2989  C CA  . LEU   C  57  ? 0.37452 0.37452 0.37452 -0.00000 0.00000  0.00000  57  LEU   G CA  
2990  C C   . LEU   C  57  ? 0.57896 0.57896 0.57896 -0.00000 0.00000  0.00000  57  LEU   G C   
2991  O O   . LEU   C  57  ? 0.60421 0.60421 0.60421 0.00000  0.00000  0.00000  57  LEU   G O   
2992  C CB  . LEU   C  57  ? 0.33203 0.33203 0.33203 -0.00000 0.00000  0.00000  57  LEU   G CB  
2993  C CG  . LEU   C  57  ? 0.53801 0.53801 0.53801 0.00000  0.00000  0.00000  57  LEU   G CG  
2994  C CD1 . LEU   C  57  ? 0.44158 0.44158 0.44158 0.00000  0.00000  0.00000  57  LEU   G CD1 
2995  C CD2 . LEU   C  57  ? 0.51857 0.51857 0.51857 0.00000  0.00000  0.00000  57  LEU   G CD2 
2996  N N   . MET   C  58  ? 0.62694 0.62694 0.62694 -0.00000 0.00000  0.00000  58  MET   G N   
2997  C CA  . MET   C  58  ? 0.61299 0.61299 0.61299 -0.00000 0.00000  0.00000  58  MET   G CA  
2998  C C   . MET   C  58  ? 0.49531 0.49531 0.49531 -0.00000 0.00000  0.00000  58  MET   G C   
2999  O O   . MET   C  58  ? 0.75704 0.75704 0.75704 0.00000  0.00000  0.00000  58  MET   G O   
3000  C CB  . MET   C  58  ? 0.52361 0.52361 0.52361 -0.00000 -0.00000 0.00000  58  MET   G CB  
3001  C CG  . MET   C  58  ? 0.71741 0.71741 0.71741 0.00000  -0.00000 0.00000  58  MET   G CG  
3002  S SD  . MET   C  58  ? 0.79169 0.79169 0.79169 0.00000  0.00000  0.00000  58  MET   G SD  
3003  C CE  . MET   C  58  ? 0.49566 0.49566 0.49566 -0.00000 0.00000  0.00000  58  MET   G CE  
3004  N N   . GLN   C  59  ? 0.64116 0.64116 0.64116 0.00000  0.00000  0.00000  59  GLN   G N   
3005  C CA  . GLN   C  59  ? 0.49979 0.49979 0.49979 -0.00000 0.00000  0.00000  59  GLN   G CA  
3006  C C   . GLN   C  59  ? 0.62302 0.62302 0.62302 0.00000  0.00000  0.00000  59  GLN   G C   
3007  O O   . GLN   C  59  ? 0.54767 0.54767 0.54767 0.00000  0.00000  0.00000  59  GLN   G O   
3008  C CB  . GLN   C  59  ? 0.42064 0.42064 0.42064 0.00000  0.00000  0.00000  59  GLN   G CB  
3009  C CG  . GLN   C  59  ? 0.79492 0.79492 0.79492 -0.00000 0.00000  0.00000  59  GLN   G CG  
3010  C CD  . GLN   C  59  ? 1.08105 1.08105 1.08105 -0.00000 0.00000  0.00000  59  GLN   G CD  
3011  O OE1 . GLN   C  59  ? 1.22775 1.22775 1.22775 -0.00000 -0.00000 0.00000  59  GLN   G OE1 
3012  N NE2 . GLN   C  59  ? 0.88634 0.88634 0.88634 -0.00000 0.00000  0.00000  59  GLN   G NE2 
3013  N N   . PRO   C  60  ? 0.64490 0.64490 0.64490 0.00000  0.00000  0.00000  60  PRO   G N   
3014  C CA  . PRO   C  60  ? 0.41338 0.41338 0.41338 0.00000  0.00000  0.00000  60  PRO   G CA  
3015  C C   . PRO   C  60  ? 0.71846 0.71846 0.71846 0.00000  0.00000  0.00000  60  PRO   G C   
3016  O O   . PRO   C  60  ? 0.45380 0.45380 0.45380 0.00000  0.00000  0.00000  60  PRO   G O   
3017  C CB  . PRO   C  60  ? 0.42305 0.42305 0.42305 0.00000  0.00000  0.00000  60  PRO   G CB  
3018  C CG  . PRO   C  60  ? 0.51156 0.51156 0.51156 -0.00000 0.00000  0.00000  60  PRO   G CG  
3019  C CD  . PRO   C  60  ? 0.36311 0.36311 0.36311 0.00000  0.00000  0.00000  60  PRO   G CD  
3020  N N   . ILE   C  61  ? 0.31651 0.31651 0.31651 0.00000  0.00000  0.00000  61  ILE   G N   
3021  C CA  . ILE   C  61  ? 0.62470 0.62470 0.62470 -0.00000 0.00000  0.00000  61  ILE   G CA  
3022  C C   . ILE   C  61  ? 0.45143 0.45143 0.45143 -0.00000 0.00000  0.00000  61  ILE   G C   
3023  O O   . ILE   C  61  ? 0.50632 0.50632 0.50632 0.00000  0.00000  0.00000  61  ILE   G O   
3024  C CB  . ILE   C  61  ? 0.44600 0.44600 0.44600 -0.00000 0.00000  0.00000  61  ILE   G CB  
3025  C CG1 . ILE   C  61  ? 0.32634 0.32634 0.32634 0.00000  0.00000  0.00000  61  ILE   G CG1 
3026  C CG2 . ILE   C  61  ? 0.30275 0.30275 0.30275 0.00000  0.00000  0.00000  61  ILE   G CG2 
3027  C CD1 . ILE   C  61  ? 0.40979 0.40979 0.40979 -0.00000 0.00000  0.00000  61  ILE   G CD1 
3028  N N   . GLN   C  62  ? 0.88211 0.88211 0.88211 -0.00000 0.00000  0.00000  62  GLN   G N   
3029  C CA  . GLN   C  62  ? 0.29670 0.29670 0.29670 0.00000  0.00000  0.00000  62  GLN   G CA  
3030  C C   . GLN   C  62  ? 0.85069 0.85069 0.85069 -0.00000 0.00000  0.00000  62  GLN   G C   
3031  O O   . GLN   C  62  ? 0.22262 0.22262 0.22262 -0.00000 0.00000  0.00000  62  GLN   G O   
3032  C CB  . GLN   C  62  ? 0.28859 0.28859 0.28859 -0.00000 0.00000  0.00000  62  GLN   G CB  
3033  C CG  . GLN   C  62  ? 1.07573 1.07573 1.07573 -0.00000 0.00000  0.00000  62  GLN   G CG  
3034  C CD  . GLN   C  62  ? 1.47610 1.47610 1.47610 0.00000  0.00000  0.00000  62  GLN   G CD  
3035  O OE1 . GLN   C  62  ? 0.85415 0.85415 0.85415 -0.00000 0.00000  0.00000  62  GLN   G OE1 
3036  N NE2 . GLN   C  62  ? 1.34850 1.34850 1.34850 0.00000  0.00000  0.00000  62  GLN   G NE2 
3037  N N   . GLU   C  63  ? 0.36891 0.36891 0.36891 -0.00000 0.00000  0.00000  63  GLU   G N   
3038  C CA  . GLU   C  63  ? 0.56948 0.56948 0.56948 -0.00000 0.00000  0.00000  63  GLU   G CA  
3039  C C   . GLU   C  63  ? 0.59759 0.59759 0.59759 0.00000  0.00000  0.00000  63  GLU   G C   
3040  O O   . GLU   C  63  ? 0.51299 0.51299 0.51299 -0.00000 0.00000  0.00000  63  GLU   G O   
3041  C CB  . GLU   C  63  ? 0.36835 0.36835 0.36835 0.00000  0.00000  0.00000  63  GLU   G CB  
3042  C CG  . GLU   C  63  ? 0.84425 0.84425 0.84425 0.00000  0.00000  0.00000  63  GLU   G CG  
3043  C CD  . GLU   C  63  ? 0.67697 0.67697 0.67697 0.00000  0.00000  0.00000  63  GLU   G CD  
3044  O OE1 . GLU   C  63  ? 1.26539 1.26539 1.26539 0.00000  0.00000  0.00000  63  GLU   G OE1 
3045  O OE2 . GLU   C  63  ? 1.61486 1.61486 1.61486 0.00000  0.00000  0.00000  63  GLU   G OE2 
3046  N N   . PHE   C  64  ? 0.43582 0.43582 0.43582 -0.00000 0.00000  0.00000  64  PHE   G N   
3047  C CA  . PHE   C  64  ? 0.35285 0.35285 0.35285 -0.00000 0.00000  0.00000  64  PHE   G CA  
3048  C C   . PHE   C  64  ? 0.53063 0.53063 0.53063 0.00000  0.00000  0.00000  64  PHE   G C   
3049  O O   . PHE   C  64  ? 0.46172 0.46172 0.46172 0.00000  0.00000  0.00000  64  PHE   G O   
3050  C CB  . PHE   C  64  ? 0.39204 0.39204 0.39204 -0.00000 0.00000  0.00000  64  PHE   G CB  
3051  C CG  . PHE   C  64  ? 0.45755 0.45755 0.45755 0.00000  0.00000  0.00000  64  PHE   G CG  
3052  C CD1 . PHE   C  64  ? 0.55817 0.55817 0.55817 0.00000  0.00000  0.00000  64  PHE   G CD1 
3053  C CD2 . PHE   C  64  ? 0.31867 0.31867 0.31867 -0.00000 0.00000  0.00000  64  PHE   G CD2 
3054  C CE1 . PHE   C  64  ? 0.38076 0.38076 0.38076 0.00000  0.00000  0.00000  64  PHE   G CE1 
3055  C CE2 . PHE   C  64  ? 0.29651 0.29651 0.29651 -0.00000 0.00000  0.00000  64  PHE   G CE2 
3056  C CZ  . PHE   C  64  ? 0.40718 0.40718 0.40718 0.00000  0.00000  0.00000  64  PHE   G CZ  
3057  N N   . LYS   C  65  ? 0.40555 0.40555 0.40555 0.00000  0.00000  0.00000  65  LYS   G N   
3058  C CA  . LYS   C  65  ? 0.34142 0.34142 0.34142 0.00000  0.00000  0.00000  65  LYS   G CA  
3059  C C   . LYS   C  65  ? 0.59708 0.59708 0.59708 0.00000  0.00000  0.00000  65  LYS   G C   
3060  O O   . LYS   C  65  ? 0.49013 0.49013 0.49013 -0.00000 0.00000  0.00000  65  LYS   G O   
3061  C CB  . LYS   C  65  ? 0.43333 0.43333 0.43333 0.00000  0.00000  0.00000  65  LYS   G CB  
3062  C CG  . LYS   C  65  ? 0.44644 0.44644 0.44644 -0.00000 0.00000  0.00000  65  LYS   G CG  
3063  C CD  . LYS   C  65  ? 0.57986 0.57986 0.57986 0.00000  0.00000  0.00000  65  LYS   G CD  
3064  C CE  . LYS   C  65  ? 0.67805 0.67805 0.67805 0.00000  0.00000  0.00000  65  LYS   G CE  
3065  N NZ  . LYS   C  65  ? 0.81819 0.81819 0.81819 -0.00000 0.00000  -0.00000 65  LYS   G NZ  
3066  N N   . ALA   C  66  ? 0.47548 0.47548 0.47548 -0.00000 0.00000  0.00000  66  ALA   G N   
3067  C CA  . ALA   C  66  ? 0.51644 0.51644 0.51644 -0.00000 0.00000  0.00000  66  ALA   G CA  
3068  C C   . ALA   C  66  ? 0.64707 0.64707 0.64707 0.00000  0.00000  0.00000  66  ALA   G C   
3069  O O   . ALA   C  66  ? 0.44980 0.44980 0.44980 0.00000  0.00000  0.00000  66  ALA   G O   
3070  C CB  . ALA   C  66  ? 0.22886 0.22886 0.22886 0.00000  0.00000  0.00000  66  ALA   G CB  
3071  N N   . PHE   C  67  ? 0.60345 0.60345 0.60345 -0.00000 0.00000  0.00000  67  PHE   G N   
3072  C CA  . PHE   C  67  ? 0.33051 0.33051 0.33051 -0.00000 0.00000  0.00000  67  PHE   G CA  
3073  C C   . PHE   C  67  ? 0.53297 0.53297 0.53297 0.00000  0.00000  0.00000  67  PHE   G C   
3074  O O   . PHE   C  67  ? 0.48573 0.48573 0.48573 0.00000  0.00000  0.00000  67  PHE   G O   
3075  C CB  . PHE   C  67  ? 0.34592 0.34592 0.34592 0.00000  0.00000  0.00000  67  PHE   G CB  
3076  C CG  . PHE   C  67  ? 0.35826 0.35826 0.35826 0.00000  0.00000  0.00000  67  PHE   G CG  
3077  C CD1 . PHE   C  67  ? 0.18583 0.18583 0.18583 -0.00000 0.00000  0.00000  67  PHE   G CD1 
3078  C CD2 . PHE   C  67  ? 0.28177 0.28177 0.28177 -0.00000 0.00000  0.00000  67  PHE   G CD2 
3079  C CE1 . PHE   C  67  ? 0.27624 0.27624 0.27624 -0.00000 0.00000  0.00000  67  PHE   G CE1 
3080  C CE2 . PHE   C  67  ? 0.40700 0.40700 0.40700 0.00000  0.00000  0.00000  67  PHE   G CE2 
3081  C CZ  . PHE   C  67  ? 0.24305 0.24305 0.24305 -0.00000 0.00000  0.00000  67  PHE   G CZ  
3082  N N   . ILE   C  68  ? 0.46638 0.46638 0.46638 0.00000  0.00000  0.00000  68  ILE   G N   
3083  C CA  . ILE   C  68  ? 0.49402 0.49402 0.49402 0.00000  0.00000  0.00000  68  ILE   G CA  
3084  C C   . ILE   C  68  ? 0.57111 0.57111 0.57111 -0.00000 -0.00000 0.00000  68  ILE   G C   
3085  O O   . ILE   C  68  ? 0.54112 0.54112 0.54112 -0.00000 0.00000  0.00000  68  ILE   G O   
3086  C CB  . ILE   C  68  ? 0.36632 0.36632 0.36632 0.00000  0.00000  0.00000  68  ILE   G CB  
3087  C CG1 . ILE   C  68  ? 0.45622 0.45622 0.45622 0.00000  0.00000  0.00000  68  ILE   G CG1 
3088  C CG2 . ILE   C  68  ? 0.43459 0.43459 0.43459 0.00000  0.00000  0.00000  68  ILE   G CG2 
3089  C CD1 . ILE   C  68  ? 0.36729 0.36729 0.36729 0.00000  0.00000  0.00000  68  ILE   G CD1 
3090  N N   . GLU   C  69  ? 0.76768 0.76768 0.76768 0.00000  0.00000  0.00000  69  GLU   G N   
3091  C CA  . GLU   C  69  ? 0.44552 0.44552 0.44552 -0.00000 0.00000  0.00000  69  GLU   G CA  
3092  C C   . GLU   C  69  ? 0.56395 0.56395 0.56395 -0.00000 -0.00000 0.00000  69  GLU   G C   
3093  O O   . GLU   C  69  ? 0.57037 0.57037 0.57037 0.00000  0.00000  0.00000  69  GLU   G O   
3094  C CB  . GLU   C  69  ? 0.52582 0.52582 0.52582 0.00000  0.00000  0.00000  69  GLU   G CB  
3095  C CG  . GLU   C  69  ? 0.34860 0.34860 0.34860 -0.00000 0.00000  0.00000  69  GLU   G CG  
3096  C CD  . GLU   C  69  ? 0.87054 0.87054 0.87054 0.00000  0.00000  0.00000  69  GLU   G CD  
3097  O OE1 . GLU   C  69  ? 0.52159 0.52159 0.52159 0.00000  0.00000  0.00000  69  GLU   G OE1 
3098  O OE2 . GLU   C  69  ? 0.60779 0.60779 0.60779 -0.00000 0.00000  0.00000  69  GLU   G OE2 
3099  N N   . SER   C  70  ? 0.59951 0.59951 0.59951 -0.00000 0.00000  0.00000  70  SER   G N   
3100  C CA  . SER   C  70  ? 0.24212 0.24212 0.24212 -0.00000 0.00000  0.00000  70  SER   G CA  
3101  C C   . SER   C  70  ? 0.60640 0.60640 0.60640 0.00000  0.00000  0.00000  70  SER   G C   
3102  O O   . SER   C  70  ? 0.41304 0.41304 0.41304 0.00000  0.00000  0.00000  70  SER   G O   
3103  C CB  . SER   C  70  ? 0.40169 0.40169 0.40169 -0.00000 0.00000  -0.00000 70  SER   G CB  
3104  O OG  . SER   C  70  ? 0.67193 0.67193 0.67193 0.00000  0.00000  0.00000  70  SER   G OG  
3105  N N   . ASP   C  71  ? 0.44333 0.44333 0.44333 0.00000  0.00000  0.00000  71  ASP   G N   
3106  C CA  . ASP   C  71  ? 0.38358 0.38358 0.38358 0.00000  0.00000  0.00000  71  ASP   G CA  
3107  C C   . ASP   C  71  ? 0.46298 0.46298 0.46298 0.00000  0.00000  0.00000  71  ASP   G C   
3108  O O   . ASP   C  71  ? 0.46175 0.46175 0.46175 -0.00000 0.00000  0.00000  71  ASP   G O   
3109  C CB  . ASP   C  71  ? 0.49966 0.49966 0.49966 0.00000  0.00000  0.00000  71  ASP   G CB  
3110  C CG  . ASP   C  71  ? 0.99690 0.99690 0.99690 0.00000  0.00000  0.00000  71  ASP   G CG  
3111  O OD1 . ASP   C  71  ? 0.53999 0.53999 0.53999 -0.00000 0.00000  0.00000  71  ASP   G OD1 
3112  O OD2 . ASP   C  71  ? 0.71610 0.71610 0.71610 0.00000  -0.00000 0.00000  71  ASP   G OD2 
3113  N N   . PRO   C  72  ? 0.57770 0.57770 0.57770 0.00000  0.00000  0.00000  72  PRO   G N   
3114  C CA  . PRO   C  72  ? 0.55552 0.55552 0.55552 0.00000  0.00000  0.00000  72  PRO   G CA  
3115  C C   . PRO   C  72  ? 0.43967 0.43967 0.43967 0.00000  0.00000  0.00000  72  PRO   G C   
3116  O O   . PRO   C  72  ? 0.51236 0.51236 0.51236 -0.00000 0.00000  0.00000  72  PRO   G O   
3117  C CB  . PRO   C  72  ? 0.38097 0.38097 0.38097 -0.00000 0.00000  0.00000  72  PRO   G CB  
3118  C CG  . PRO   C  72  ? 0.45499 0.45499 0.45499 0.00000  0.00000  0.00000  72  PRO   G CG  
3119  C CD  . PRO   C  72  ? 0.27711 0.27711 0.27711 0.00000  0.00000  0.00000  72  PRO   G CD  
3120  N N   . VAL   C  73  ? 0.51180 0.51180 0.51180 -0.00000 0.00000  0.00000  73  VAL   G N   
3121  C CA  . VAL   C  73  ? 0.65094 0.65094 0.65094 0.00000  0.00000  0.00000  73  VAL   G CA  
3122  C C   . VAL   C  73  ? 0.74713 0.74713 0.74713 -0.00000 0.00000  0.00000  73  VAL   G C   
3123  O O   . VAL   C  73  ? 0.38009 0.38009 0.38009 0.00000  0.00000  0.00000  73  VAL   G O   
3124  C CB  . VAL   C  73  ? 0.60970 0.60970 0.60970 0.00000  -0.00000 0.00000  73  VAL   G CB  
3125  C CG1 . VAL   C  73  ? 0.31905 0.31905 0.31905 0.00000  0.00000  0.00000  73  VAL   G CG1 
3126  C CG2 . VAL   C  73  ? 0.29168 0.29168 0.29168 0.00000  0.00000  0.00000  73  VAL   G CG2 
3127  N N   . VAL   C  74  ? 0.52885 0.52885 0.52885 0.00000  0.00000  0.00000  74  VAL   G N   
3128  C CA  . VAL   C  74  ? 0.40976 0.40976 0.40976 0.00000  0.00000  0.00000  74  VAL   G CA  
3129  C C   . VAL   C  74  ? 0.54695 0.54695 0.54695 -0.00000 0.00000  0.00000  74  VAL   G C   
3130  O O   . VAL   C  74  ? 0.60559 0.60559 0.60559 0.00000  0.00000  0.00000  74  VAL   G O   
3131  C CB  . VAL   C  74  ? 0.43669 0.43669 0.43669 -0.00000 0.00000  0.00000  74  VAL   G CB  
3132  C CG1 . VAL   C  74  ? 0.22048 0.22048 0.22048 -0.00000 -0.00000 0.00000  74  VAL   G CG1 
3133  C CG2 . VAL   C  74  ? 0.30706 0.30706 0.30706 -0.00000 0.00000  0.00000  74  VAL   G CG2 
3134  N N   . HIS   C  75  ? 0.57605 0.57605 0.57605 -0.00000 0.00000  0.00000  75  HIS   G N   
3135  C CA  . HIS   C  75  ? 0.48360 0.48360 0.48360 0.00000  0.00000  0.00000  75  HIS   G CA  
3136  C C   . HIS   C  75  ? 0.34226 0.34226 0.34226 0.00000  0.00000  0.00000  75  HIS   G C   
3137  O O   . HIS   C  75  ? 0.42984 0.42984 0.42984 -0.00000 0.00000  0.00000  75  HIS   G O   
3138  C CB  . HIS   C  75  ? 0.37687 0.37687 0.37687 -0.00000 0.00000  0.00000  75  HIS   G CB  
3139  C CG  . HIS   C  75  ? 0.79263 0.79263 0.79263 0.00000  0.00000  0.00000  75  HIS   G CG  
3140  N ND1 . HIS   C  75  ? 0.91229 0.91229 0.91229 -0.00000 0.00000  0.00000  75  HIS   G ND1 
3141  C CD2 . HIS   C  75  ? 0.81096 0.81096 0.81096 -0.00000 0.00000  0.00000  75  HIS   G CD2 
3142  C CE1 . HIS   C  75  ? 0.75388 0.75388 0.75388 0.00000  0.00000  0.00000  75  HIS   G CE1 
3143  N NE2 . HIS   C  75  ? 0.58518 0.58518 0.58518 0.00000  0.00000  0.00000  75  HIS   G NE2 
3144  N N   . GLN   C  76  ? 0.58081 0.58081 0.58081 -0.00000 0.00000  0.00000  76  GLN   G N   
3145  C CA  . GLN   C  76  ? 0.31073 0.31073 0.31073 0.00000  0.00000  0.00000  76  GLN   G CA  
3146  C C   . GLN   C  76  ? 0.60448 0.60448 0.60448 -0.00000 0.00000  0.00000  76  GLN   G C   
3147  O O   . GLN   C  76  ? 0.46855 0.46855 0.46855 0.00000  0.00000  0.00000  76  GLN   G O   
3148  C CB  . GLN   C  76  ? 0.63269 0.63269 0.63269 -0.00000 0.00000  0.00000  76  GLN   G CB  
3149  C CG  . GLN   C  76  ? 0.32845 0.32845 0.32845 0.00000  0.00000  0.00000  76  GLN   G CG  
3150  C CD  . GLN   C  76  ? 1.06643 1.06643 1.06643 0.00000  0.00000  0.00000  76  GLN   G CD  
3151  O OE1 . GLN   C  76  ? 0.55535 0.55535 0.55535 0.00000  0.00000  0.00000  76  GLN   G OE1 
3152  N NE2 . GLN   C  76  ? 0.45498 0.45498 0.45498 0.00000  0.00000  0.00000  76  GLN   G NE2 
3153  N N   . GLU   C  77  ? 0.52491 0.52491 0.52491 0.00000  0.00000  0.00000  77  GLU   G N   
3154  C CA  . GLU   C  77  ? 0.41085 0.41085 0.41085 -0.00000 0.00000  0.00000  77  GLU   G CA  
3155  C C   . GLU   C  77  ? 0.75738 0.75738 0.75738 0.00000  0.00000  0.00000  77  GLU   G C   
3156  O O   . GLU   C  77  ? 0.33443 0.33443 0.33443 0.00000  0.00000  0.00000  77  GLU   G O   
3157  C CB  . GLU   C  77  ? 0.40504 0.40504 0.40504 0.00000  0.00000  0.00000  77  GLU   G CB  
3158  C CG  . GLU   C  77  ? 0.34292 0.34292 0.34292 0.00000  0.00000  0.00000  77  GLU   G CG  
3159  C CD  . GLU   C  77  ? 0.75313 0.75313 0.75313 0.00000  0.00000  0.00000  77  GLU   G CD  
3160  O OE1 . GLU   C  77  ? 0.52084 0.52084 0.52084 0.00000  0.00000  0.00000  77  GLU   G OE1 
3161  O OE2 . GLU   C  77  ? 0.44179 0.44179 0.44179 0.00000  0.00000  0.00000  77  GLU   G OE2 
3162  N N   . PHE   C  78  ? 0.32958 0.32958 0.32958 0.00000  0.00000  0.00000  78  PHE   G N   
3163  C CA  . PHE   C  78  ? 0.59639 0.59639 0.59639 0.00000  0.00000  0.00000  78  PHE   G CA  
3164  C C   . PHE   C  78  ? 0.58711 0.58711 0.58711 0.00000  0.00000  0.00000  78  PHE   G C   
3165  O O   . PHE   C  78  ? 0.68415 0.68415 0.68415 0.00000  0.00000  0.00000  78  PHE   G O   
3166  C CB  . PHE   C  78  ? 0.35041 0.35041 0.35041 0.00000  0.00000  0.00000  78  PHE   G CB  
3167  C CG  . PHE   C  78  ? 0.58420 0.58420 0.58420 -0.00000 0.00000  0.00000  78  PHE   G CG  
3168  C CD1 . PHE   C  78  ? 0.41117 0.41117 0.41117 -0.00000 0.00000  0.00000  78  PHE   G CD1 
3169  C CD2 . PHE   C  78  ? 0.26490 0.26490 0.26490 -0.00000 0.00000  0.00000  78  PHE   G CD2 
3170  C CE1 . PHE   C  78  ? 0.38457 0.38457 0.38457 0.00000  0.00000  0.00000  78  PHE   G CE1 
3171  C CE2 . PHE   C  78  ? 0.51546 0.51546 0.51546 0.00000  0.00000  0.00000  78  PHE   G CE2 
3172  C CZ  . PHE   C  78  ? 0.35597 0.35597 0.35597 0.00000  0.00000  0.00000  78  PHE   G CZ  
3173  N N   . ILE   C  79  ? 0.57489 0.57489 0.57489 0.00000  0.00000  0.00000  79  ILE   G N   
3174  C CA  . ILE   C  79  ? 0.49446 0.49446 0.49446 0.00000  0.00000  0.00000  79  ILE   G CA  
3175  C C   . ILE   C  79  ? 0.70642 0.70642 0.70642 0.00000  0.00000  0.00000  79  ILE   G C   
3176  O O   . ILE   C  79  ? 0.40669 0.40669 0.40669 -0.00000 0.00000  0.00000  79  ILE   G O   
3177  C CB  . ILE   C  79  ? 0.60547 0.60547 0.60547 0.00000  0.00000  0.00000  79  ILE   G CB  
3178  C CG1 . ILE   C  79  ? 0.43382 0.43382 0.43382 0.00000  0.00000  0.00000  79  ILE   G CG1 
3179  C CG2 . ILE   C  79  ? 0.44399 0.44399 0.44399 0.00000  0.00000  0.00000  79  ILE   G CG2 
3180  C CD1 . ILE   C  79  ? 0.39897 0.39897 0.39897 0.00000  0.00000  0.00000  79  ILE   G CD1 
3181  N N   . ASP   C  80  ? 0.31891 0.31891 0.31891 -0.00000 -0.00000 0.00000  80  ASP   G N   
3182  C CA  . ASP   C  80  ? 0.52282 0.52282 0.52282 0.00000  0.00000  0.00000  80  ASP   G CA  
3183  C C   . ASP   C  80  ? 0.41107 0.41107 0.41107 0.00000  0.00000  0.00000  80  ASP   G C   
3184  O O   . ASP   C  80  ? 0.52700 0.52700 0.52700 0.00000  0.00000  0.00000  80  ASP   G O   
3185  C CB  . ASP   C  80  ? 0.44430 0.44430 0.44430 0.00000  0.00000  0.00000  80  ASP   G CB  
3186  C CG  . ASP   C  80  ? 0.67596 0.67596 0.67596 0.00000  0.00000  0.00000  80  ASP   G CG  
3187  O OD1 . ASP   C  80  ? 0.65299 0.65299 0.65299 0.00000  -0.00000 0.00000  80  ASP   G OD1 
3188  O OD2 . ASP   C  80  ? 0.75040 0.75040 0.75040 -0.00000 0.00000  0.00000  80  ASP   G OD2 
3189  N N   . MET   C  81  ? 0.46606 0.46606 0.46606 -0.00000 0.00000  0.00000  81  MET   G N   
3190  C CA  . MET   C  81  ? 0.38633 0.38633 0.38633 -0.00000 0.00000  0.00000  81  MET   G CA  
3191  C C   . MET   C  81  ? 0.67477 0.67477 0.67477 0.00000  0.00000  0.00000  81  MET   G C   
3192  O O   . MET   C  81  ? 0.51471 0.51471 0.51471 -0.00000 0.00000  0.00000  81  MET   G O   
3193  C CB  . MET   C  81  ? 0.38640 0.38640 0.38640 0.00000  0.00000  0.00000  81  MET   G CB  
3194  C CG  . MET   C  81  ? 0.46824 0.46824 0.46824 0.00000  -0.00000 -0.00000 81  MET   G CG  
3195  S SD  . MET   C  81  ? 0.46678 0.46678 0.46678 0.00000  0.00000  0.00000  81  MET   G SD  
3196  C CE  . MET   C  81  ? 0.42395 0.42395 0.42395 0.00000  0.00000  0.00000  81  MET   G CE  
3197  N N   . PHE   C  82  ? 0.45933 0.45933 0.45933 0.00000  0.00000  0.00000  82  PHE   G N   
3198  C CA  . PHE   C  82  ? 0.78102 0.78102 0.78102 -0.00000 0.00000  0.00000  82  PHE   G CA  
3199  C C   . PHE   C  82  ? 0.43731 0.43731 0.43731 -0.00000 0.00000  0.00000  82  PHE   G C   
3200  O O   . PHE   C  82  ? 1.24004 1.24004 1.24004 -0.00000 0.00000  0.00000  82  PHE   G O   
3201  C CB  . PHE   C  82  ? 0.47063 0.47063 0.47063 0.00000  0.00000  0.00000  82  PHE   G CB  
3202  C CG  . PHE   C  82  ? 1.01720 1.01720 1.01720 0.00000  0.00000  0.00000  82  PHE   G CG  
3203  C CD1 . PHE   C  82  ? 0.43365 0.43365 0.43365 -0.00000 -0.00000 0.00000  82  PHE   G CD1 
3204  C CD2 . PHE   C  82  ? 0.46674 0.46674 0.46674 -0.00000 0.00000  0.00000  82  PHE   G CD2 
3205  C CE1 . PHE   C  82  ? 0.67129 0.67129 0.67129 -0.00000 -0.00000 0.00000  82  PHE   G CE1 
3206  C CE2 . PHE   C  82  ? 0.68733 0.68733 0.68733 -0.00000 0.00000  0.00000  82  PHE   G CE2 
3207  C CZ  . PHE   C  82  ? 0.37962 0.37962 0.37962 -0.00000 0.00000  0.00000  82  PHE   G CZ  
3208  N N   . GLU   C  83  ? 0.82513 0.82513 0.82513 0.00000  0.00000  0.00000  83  GLU   G N   
3209  C CA  . GLU   C  83  ? 0.88547 0.88547 0.88547 -0.00000 0.00000  0.00000  83  GLU   G CA  
3210  C C   . GLU   C  83  ? 0.99096 0.99096 0.99096 0.00000  0.00000  0.00000  83  GLU   G C   
3211  O O   . GLU   C  83  ? 0.69034 0.69034 0.69034 -0.00000 0.00000  0.00000  83  GLU   G O   
3212  C CB  . GLU   C  83  ? 0.57307 0.57307 0.57307 0.00000  0.00000  0.00000  83  GLU   G CB  
3213  C CG  . GLU   C  83  ? 1.41309 1.41309 1.41309 0.00000  0.00000  0.00000  83  GLU   G CG  
3214  C CD  . GLU   C  83  ? 1.99511 1.99511 1.99511 0.00000  0.00000  0.00000  83  GLU   G CD  
3215  O OE1 . GLU   C  83  ? 1.07713 1.07713 1.07713 0.00000  0.00000  -0.00000 83  GLU   G OE1 
3216  O OE2 . GLU   C  83  ? 1.30544 1.30544 1.30544 -0.00000 0.00000  0.00000  83  GLU   G OE2 
3217  N N   . GLY   C  84  ? 1.19364 1.19364 1.19364 0.00000  0.00000  0.00000  84  GLY   G N   
3218  C CA  . GLY   C  84  ? 0.74222 0.74222 0.74222 0.00000  0.00000  0.00000  84  GLY   G CA  
3219  C C   . GLY   C  84  ? 1.16126 1.16126 1.16126 0.00000  0.00000  0.00000  84  GLY   G C   
3220  O O   . GLY   C  84  ? 0.97276 0.97276 0.97276 0.00000  0.00000  0.00000  84  GLY   G O   
3221  N N   . ILE   C  85  ? 1.25082 1.25082 1.25082 0.00000  0.00000  0.00000  85  ILE   G N   
3222  C CA  . ILE   C  85  ? 0.99257 0.99257 0.99257 0.00000  0.00000  0.00000  85  ILE   G CA  
3223  C C   . ILE   C  85  ? 1.12187 1.12187 1.12187 0.00000  0.00000  0.00000  85  ILE   G C   
3224  O O   . ILE   C  85  ? 1.04774 1.04774 1.04774 0.00000  0.00000  0.00000  85  ILE   G O   
3225  C CB  . ILE   C  85  ? 0.90918 0.90918 0.90918 0.00000  -0.00000 -0.00000 85  ILE   G CB  
3226  C CG1 . ILE   C  85  ? 1.10264 1.10264 1.10264 0.00000  0.00000  0.00000  85  ILE   G CG1 
3227  C CG2 . ILE   C  85  ? 0.93599 0.93599 0.93599 0.00000  0.00000  0.00000  85  ILE   G CG2 
3228  C CD1 . ILE   C  85  ? 1.00012 1.00012 1.00012 0.00000  0.00000  0.00000  85  ILE   G CD1 
3229  N N   . GLN   C  86  ? 1.04889 1.04889 1.04889 0.00000  0.00000  0.00000  86  GLN   G N   
3230  C CA  . GLN   C  86  ? 1.44930 1.44930 1.44930 0.00000  0.00000  0.00000  86  GLN   G CA  
3231  C C   . GLN   C  86  ? 0.82667 0.82667 0.82667 0.00000  0.00000  0.00000  86  GLN   G C   
3232  O O   . GLN   C  86  ? 1.41809 1.41809 1.41809 0.00000  0.00000  0.00000  86  GLN   G O   
3233  C CB  . GLN   C  86  ? 0.99507 0.99507 0.99507 -0.00000 0.00000  0.00000  86  GLN   G CB  
3234  N N   . ASP   C  87  ? 1.27313 1.27313 1.27313 -0.00000 0.00000  0.00000  87  ASP   G N   
3235  C CA  . ASP   C  87  ? 0.84596 0.84596 0.84596 0.00000  0.00000  0.00000  87  ASP   G CA  
3236  C C   . ASP   C  87  ? 0.70857 0.70857 0.70857 0.00000  0.00000  0.00000  87  ASP   G C   
3237  O O   . ASP   C  87  ? 0.96678 0.96678 0.96678 0.00000  0.00000  0.00000  87  ASP   G O   
3238  C CB  . ASP   C  87  ? 0.74786 0.74786 0.74786 -0.00000 0.00000  0.00000  87  ASP   G CB  
3239  C CG  . ASP   C  87  ? 1.66945 1.66945 1.66945 0.00000  0.00000  0.00000  87  ASP   G CG  
3240  O OD1 . ASP   C  87  ? 1.41938 1.41938 1.41938 0.00000  0.00000  0.00000  87  ASP   G OD1 
3241  O OD2 . ASP   C  87  ? 1.39455 1.39455 1.39455 -0.00000 0.00000  0.00000  87  ASP   G OD2 
3242  N N   . SER   C  88  ? 0.68940 0.68940 0.68940 -0.00000 0.00000  0.00000  88  SER   G N   
3243  C CA  . SER   C  88  ? 0.55106 0.55106 0.55106 -0.00000 0.00000  0.00000  88  SER   G CA  
3244  C C   . SER   C  88  ? 1.08792 1.08792 1.08792 -0.00000 0.00000  0.00000  88  SER   G C   
3245  O O   . SER   C  88  ? 0.67630 0.67630 0.67630 0.00000  0.00000  0.00000  88  SER   G O   
3246  C CB  . SER   C  88  ? 0.56435 0.56435 0.56435 -0.00000 0.00000  0.00000  88  SER   G CB  
3247  O OG  . SER   C  88  ? 0.76864 0.76864 0.76864 0.00000  0.00000  0.00000  88  SER   G OG  
3248  N N   . PRO   C  89  ? 0.72886 0.72886 0.72886 0.00000  -0.00000 0.00000  89  PRO   G N   
3249  C CA  . PRO   C  89  ? 0.43144 0.43144 0.43144 0.00000  0.00000  0.00000  89  PRO   G CA  
3250  C C   . PRO   C  89  ? 0.78233 0.78233 0.78233 0.00000  0.00000  0.00000  89  PRO   G C   
3251  O O   . PRO   C  89  ? 0.56193 0.56193 0.56193 -0.00000 -0.00000 0.00000  89  PRO   G O   
3252  C CB  . PRO   C  89  ? 0.71474 0.71474 0.71474 -0.00000 0.00000  0.00000  89  PRO   G CB  
3253  C CG  . PRO   C  89  ? 0.68523 0.68523 0.68523 0.00000  0.00000  -0.00000 89  PRO   G CG  
3254  C CD  . PRO   C  89  ? 0.61679 0.61679 0.61679 0.00000  0.00000  0.00000  89  PRO   G CD  
3255  N N   . ARG   C  90  ? 0.40072 0.40072 0.40072 0.00000  0.00000  0.00000  90  ARG   G N   
3256  C CA  . ARG   C  90  ? 0.61601 0.61601 0.61601 -0.00000 0.00000  0.00000  90  ARG   G CA  
3257  C C   . ARG   C  90  ? 0.49804 0.49804 0.49804 0.00000  0.00000  0.00000  90  ARG   G C   
3258  O O   . ARG   C  90  ? 0.49281 0.49281 0.49281 0.00000  0.00000  0.00000  90  ARG   G O   
3259  C CB  . ARG   C  90  ? 0.41832 0.41832 0.41832 0.00000  0.00000  0.00000  90  ARG   G CB  
3260  N N   . ASN   C  91  ? 0.49424 0.49424 0.49424 0.00000  0.00000  0.00000  91  ASN   G N   
3261  C CA  . ASN   C  91  ? 0.55098 0.55098 0.55098 0.00000  0.00000  0.00000  91  ASN   G CA  
3262  C C   . ASN   C  91  ? 0.53358 0.53358 0.53358 -0.00000 0.00000  0.00000  91  ASN   G C   
3263  O O   . ASN   C  91  ? 0.61658 0.61658 0.61658 0.00000  0.00000  0.00000  91  ASN   G O   
3264  C CB  . ASN   C  91  ? 0.44968 0.44968 0.44968 0.00000  0.00000  0.00000  91  ASN   G CB  
3265  C CG  . ASN   C  91  ? 0.58491 0.58491 0.58491 0.00000  0.00000  0.00000  91  ASN   G CG  
3266  O OD1 . ASN   C  91  ? 0.71397 0.71397 0.71397 0.00000  0.00000  0.00000  91  ASN   G OD1 
3267  N ND2 . ASN   C  91  ? 0.53457 0.53457 0.53457 0.00000  0.00000  0.00000  91  ASN   G ND2 
3268  N N   . TYR   C  92  ? 0.51222 0.51222 0.51222 0.00000  0.00000  0.00000  92  TYR   G N   
3269  C CA  . TYR   C  92  ? 0.43295 0.43295 0.43295 0.00000  0.00000  0.00000  92  TYR   G CA  
3270  C C   . TYR   C  92  ? 0.48480 0.48480 0.48480 0.00000  -0.00000 -0.00000 92  TYR   G C   
3271  O O   . TYR   C  92  ? 0.54454 0.54454 0.54454 0.00000  -0.00000 -0.00000 92  TYR   G O   
3272  C CB  . TYR   C  92  ? 0.29639 0.29639 0.29639 0.00000  0.00000  0.00000  92  TYR   G CB  
3273  C CG  . TYR   C  92  ? 0.36562 0.36562 0.36562 0.00000  0.00000  0.00000  92  TYR   G CG  
3274  C CD1 . TYR   C  92  ? 0.34305 0.34305 0.34305 0.00000  0.00000  0.00000  92  TYR   G CD1 
3275  C CD2 . TYR   C  92  ? 0.44710 0.44710 0.44710 -0.00000 -0.00000 0.00000  92  TYR   G CD2 
3276  C CE1 . TYR   C  92  ? 0.58345 0.58345 0.58345 0.00000  0.00000  0.00000  92  TYR   G CE1 
3277  C CE2 . TYR   C  92  ? 0.54665 0.54665 0.54665 0.00000  -0.00000 0.00000  92  TYR   G CE2 
3278  C CZ  . TYR   C  92  ? 0.49021 0.49021 0.49021 -0.00000 0.00000  0.00000  92  TYR   G CZ  
3279  O OH  . TYR   C  92  ? 0.70243 0.70243 0.70243 0.00000  0.00000  0.00000  92  TYR   G OH  
3280  N N   . GLN   C  93  ? 0.51852 0.51852 0.51852 -0.00000 0.00000  0.00000  93  GLN   G N   
3281  C CA  . GLN   C  93  ? 0.67820 0.67820 0.67820 0.00000  0.00000  0.00000  93  GLN   G CA  
3282  C C   . GLN   C  93  ? 0.50150 0.50150 0.50150 0.00000  0.00000  0.00000  93  GLN   G C   
3283  O O   . GLN   C  93  ? 0.57002 0.57002 0.57002 0.00000  -0.00000 0.00000  93  GLN   G O   
3284  C CB  . GLN   C  93  ? 0.43596 0.43596 0.43596 0.00000  0.00000  0.00000  93  GLN   G CB  
3285  C CG  . GLN   C  93  ? 0.64785 0.64785 0.64785 -0.00000 0.00000  0.00000  93  GLN   G CG  
3286  C CD  . GLN   C  93  ? 2.15889 2.15889 2.15889 0.00000  0.00000  0.00000  93  GLN   G CD  
3287  O OE1 . GLN   C  93  ? 0.61719 0.61719 0.61719 0.00000  0.00000  0.00000  93  GLN   G OE1 
3288  N NE2 . GLN   C  93  ? 0.64530 0.64530 0.64530 0.00000  0.00000  0.00000  93  GLN   G NE2 
3289  N N   . GLU   C  94  ? 0.67974 0.67974 0.67974 0.00000  0.00000  0.00000  94  GLU   G N   
3290  C CA  . GLU   C  94  ? 0.32945 0.32945 0.32945 0.00000  -0.00000 0.00000  94  GLU   G CA  
3291  C C   . GLU   C  94  ? 0.76647 0.76647 0.76647 0.00000  0.00000  0.00000  94  GLU   G C   
3292  O O   . GLU   C  94  ? 0.72921 0.72921 0.72921 0.00000  0.00000  0.00000  94  GLU   G O   
3293  C CB  . GLU   C  94  ? 0.72766 0.72766 0.72766 -0.00000 -0.00000 -0.00000 94  GLU   G CB  
3294  C CG  . GLU   C  94  ? 1.00050 1.00050 1.00050 -0.00000 0.00000  -0.00000 94  GLU   G CG  
3295  C CD  . GLU   C  94  ? 1.79459 1.79459 1.79459 0.00000  0.00000  0.00000  94  GLU   G CD  
3296  O OE1 . GLU   C  94  ? 0.63529 0.63529 0.63529 -0.00000 0.00000  0.00000  94  GLU   G OE1 
3297  O OE2 . GLU   C  94  ? 1.31550 1.31550 1.31550 0.00000  0.00000  0.00000  94  GLU   G OE2 
3298  N N   . LEU   C  95  ? 0.61267 0.61267 0.61267 0.00000  -0.00000 0.00000  95  LEU   G N   
3299  C CA  . LEU   C  95  ? 0.37258 0.37258 0.37258 0.00000  0.00000  0.00000  95  LEU   G CA  
3300  C C   . LEU   C  95  ? 0.42487 0.42487 0.42487 0.00000  0.00000  0.00000  95  LEU   G C   
3301  O O   . LEU   C  95  ? 0.37433 0.37433 0.37433 -0.00000 0.00000  0.00000  95  LEU   G O   
3302  C CB  . LEU   C  95  ? 0.46262 0.46262 0.46262 0.00000  0.00000  0.00000  95  LEU   G CB  
3303  C CG  . LEU   C  95  ? 0.46347 0.46347 0.46347 0.00000  0.00000  0.00000  95  LEU   G CG  
3304  C CD1 . LEU   C  95  ? 0.39113 0.39113 0.39113 -0.00000 0.00000  0.00000  95  LEU   G CD1 
3305  C CD2 . LEU   C  95  ? 0.27966 0.27966 0.27966 0.00000  0.00000  0.00000  95  LEU   G CD2 
3306  N N   . CYS   C  96  ? 0.30380 0.30380 0.30380 -0.00000 0.00000  0.00000  96  CYS   G N   
3307  C CA  . CYS   C  96  ? 0.44044 0.44044 0.44044 -0.00000 0.00000  0.00000  96  CYS   G CA  
3308  C C   . CYS   C  96  ? 0.44296 0.44296 0.44296 0.00000  0.00000  0.00000  96  CYS   G C   
3309  O O   . CYS   C  96  ? 0.68790 0.68790 0.68790 -0.00000 0.00000  0.00000  96  CYS   G O   
3310  C CB  . CYS   C  96  ? 0.35854 0.35854 0.35854 -0.00000 0.00000  0.00000  96  CYS   G CB  
3311  S SG  . CYS   C  96  ? 0.55744 0.55744 0.55744 0.00000  0.00000  0.00000  96  CYS   G SG  
3312  N N   . ASN   C  97  ? 0.56428 0.56428 0.56428 -0.00000 0.00000  0.00000  97  ASN   G N   
3313  C CA  . ASN   C  97  ? 0.44105 0.44105 0.44105 0.00000  0.00000  0.00000  97  ASN   G CA  
3314  C C   . ASN   C  97  ? 0.75552 0.75552 0.75552 0.00000  0.00000  0.00000  97  ASN   G C   
3315  O O   . ASN   C  97  ? 0.52011 0.52011 0.52011 0.00000  0.00000  -0.00000 97  ASN   G O   
3316  C CB  . ASN   C  97  ? 0.58704 0.58704 0.58704 -0.00000 0.00000  0.00000  97  ASN   G CB  
3317  C CG  . ASN   C  97  ? 1.08699 1.08699 1.08699 0.00000  0.00000  0.00000  97  ASN   G CG  
3318  O OD1 . ASN   C  97  ? 0.73953 0.73953 0.73953 -0.00000 0.00000  0.00000  97  ASN   G OD1 
3319  N ND2 . ASN   C  97  ? 0.54962 0.54962 0.54962 -0.00000 0.00000  0.00000  97  ASN   G ND2 
3320  N N   . MET   C  98  ? 0.35870 0.35870 0.35870 -0.00000 0.00000  0.00000  98  MET   G N   
3321  C CA  . MET   C  98  ? 0.31221 0.31221 0.31221 0.00000  0.00000  0.00000  98  MET   G CA  
3322  C C   . MET   C  98  ? 0.79406 0.79406 0.79406 -0.00000 0.00000  0.00000  98  MET   G C   
3323  O O   . MET   C  98  ? 0.53897 0.53897 0.53897 -0.00000 0.00000  0.00000  98  MET   G O   
3324  C CB  . MET   C  98  ? 0.39905 0.39905 0.39905 0.00000  -0.00000 0.00000  98  MET   G CB  
3325  C CG  . MET   C  98  ? 0.25966 0.25966 0.25966 0.00000  0.00000  0.00000  98  MET   G CG  
3326  S SD  . MET   C  98  ? 0.65361 0.65361 0.65361 0.00000  0.00000  0.00000  98  MET   G SD  
3327  C CE  . MET   C  98  ? 0.48513 0.48513 0.48513 -0.00000 0.00000  0.00000  98  MET   G CE  
3328  N N   . PHE   C  99  ? 0.44339 0.44339 0.44339 0.00000  0.00000  0.00000  99  PHE   G N   
3329  C CA  . PHE   C  99  ? 0.39309 0.39309 0.39309 -0.00000 0.00000  0.00000  99  PHE   G CA  
3330  C C   . PHE   C  99  ? 0.51148 0.51148 0.51148 -0.00000 -0.00000 -0.00000 99  PHE   G C   
3331  O O   . PHE   C  99  ? 0.49711 0.49711 0.49711 -0.00000 0.00000  0.00000  99  PHE   G O   
3332  C CB  . PHE   C  99  ? 0.37379 0.37379 0.37379 0.00000  0.00000  0.00000  99  PHE   G CB  
3333  C CG  . PHE   C  99  ? 0.47780 0.47780 0.47780 0.00000  -0.00000 0.00000  99  PHE   G CG  
3334  C CD1 . PHE   C  99  ? 0.34894 0.34894 0.34894 0.00000  0.00000  0.00000  99  PHE   G CD1 
3335  C CD2 . PHE   C  99  ? 0.46071 0.46071 0.46071 -0.00000 0.00000  0.00000  99  PHE   G CD2 
3336  C CE1 . PHE   C  99  ? 0.54583 0.54583 0.54583 0.00000  0.00000  0.00000  99  PHE   G CE1 
3337  C CE2 . PHE   C  99  ? 0.33804 0.33804 0.33804 -0.00000 0.00000  0.00000  99  PHE   G CE2 
3338  C CZ  . PHE   C  99  ? 0.39001 0.39001 0.39001 0.00000  0.00000  0.00000  99  PHE   G CZ  
3339  N N   . ASN   C  100 ? 0.42223 0.42223 0.42223 0.00000  0.00000  0.00000  100 ASN   G N   
3340  C CA  . ASN   C  100 ? 0.47609 0.47609 0.47609 -0.00000 0.00000  0.00000  100 ASN   G CA  
3341  C C   . ASN   C  100 ? 0.52403 0.52403 0.52403 0.00000  0.00000  0.00000  100 ASN   G C   
3342  O O   . ASN   C  100 ? 0.61592 0.61592 0.61592 -0.00000 0.00000  0.00000  100 ASN   G O   
3343  C CB  . ASN   C  100 ? 0.46961 0.46961 0.46961 0.00000  0.00000  0.00000  100 ASN   G CB  
3344  C CG  . ASN   C  100 ? 0.61465 0.61465 0.61465 -0.00000 0.00000  0.00000  100 ASN   G CG  
3345  O OD1 . ASN   C  100 ? 0.77482 0.77482 0.77482 -0.00000 0.00000  0.00000  100 ASN   G OD1 
3346  N ND2 . ASN   C  100 ? 0.61059 0.61059 0.61059 0.00000  0.00000  0.00000  100 ASN   G ND2 
3347  N N   . ASP   C  101 ? 0.47646 0.47646 0.47646 0.00000  0.00000  0.00000  101 ASP   G N   
3348  C CA  . ASP   C  101 ? 0.39700 0.39700 0.39700 0.00000  0.00000  0.00000  101 ASP   G CA  
3349  C C   . ASP   C  101 ? 0.68400 0.68400 0.68400 0.00000  0.00000  0.00000  101 ASP   G C   
3350  O O   . ASP   C  101 ? 0.57856 0.57856 0.57856 0.00000  0.00000  0.00000  101 ASP   G O   
3351  C CB  . ASP   C  101 ? 0.39795 0.39795 0.39795 -0.00000 0.00000  0.00000  101 ASP   G CB  
3352  C CG  . ASP   C  101 ? 1.44612 1.44612 1.44612 -0.00000 0.00000  0.00000  101 ASP   G CG  
3353  O OD1 . ASP   C  101 ? 0.62656 0.62656 0.62656 0.00000  0.00000  0.00000  101 ASP   G OD1 
3354  O OD2 . ASP   C  101 ? 0.74886 0.74886 0.74886 0.00000  0.00000  0.00000  101 ASP   G OD2 
3355  N N   . ILE   C  102 ? 0.51869 0.51869 0.51869 0.00000  0.00000  0.00000  102 ILE   G N   
3356  C CA  . ILE   C  102 ? 0.32182 0.32182 0.32182 0.00000  0.00000  0.00000  102 ILE   G CA  
3357  C C   . ILE   C  102 ? 0.64556 0.64556 0.64556 0.00000  0.00000  0.00000  102 ILE   G C   
3358  O O   . ILE   C  102 ? 0.43707 0.43707 0.43707 -0.00000 0.00000  0.00000  102 ILE   G O   
3359  C CB  . ILE   C  102 ? 0.35765 0.35765 0.35765 0.00000  0.00000  0.00000  102 ILE   G CB  
3360  C CG1 . ILE   C  102 ? 0.16536 0.16536 0.16536 0.00000  0.00000  0.00000  102 ILE   G CG1 
3361  C CG2 . ILE   C  102 ? 0.22127 0.22127 0.22127 0.00000  -0.00000 0.00000  102 ILE   G CG2 
3362  C CD1 . ILE   C  102 ? 0.43241 0.43241 0.43241 0.00000  0.00000  0.00000  102 ILE   G CD1 
3363  N N   . PHE   C  103 ? 0.32961 0.32961 0.32961 -0.00000 0.00000  0.00000  103 PHE   G N   
3364  C CA  . PHE   C  103 ? 0.64007 0.64007 0.64007 0.00000  0.00000  0.00000  103 PHE   G CA  
3365  C C   . PHE   C  103 ? 0.35997 0.35997 0.35997 0.00000  0.00000  0.00000  103 PHE   G C   
3366  O O   . PHE   C  103 ? 0.46586 0.46586 0.46586 -0.00000 -0.00000 0.00000  103 PHE   G O   
3367  C CB  . PHE   C  103 ? 0.22729 0.22729 0.22729 0.00000  0.00000  0.00000  103 PHE   G CB  
3368  C CG  . PHE   C  103 ? 0.44586 0.44586 0.44586 -0.00000 0.00000  -0.00000 103 PHE   G CG  
3369  C CD1 . PHE   C  103 ? 0.39489 0.39489 0.39489 0.00000  0.00000  0.00000  103 PHE   G CD1 
3370  C CD2 . PHE   C  103 ? 0.29427 0.29427 0.29427 -0.00000 0.00000  0.00000  103 PHE   G CD2 
3371  C CE1 . PHE   C  103 ? 0.55001 0.55001 0.55001 0.00000  -0.00000 0.00000  103 PHE   G CE1 
3372  C CE2 . PHE   C  103 ? 0.44793 0.44793 0.44793 -0.00000 0.00000  0.00000  103 PHE   G CE2 
3373  C CZ  . PHE   C  103 ? 0.43884 0.43884 0.43884 0.00000  0.00000  0.00000  103 PHE   G CZ  
3374  N N   . ARG   C  104 ? 0.52028 0.52028 0.52028 0.00000  0.00000  0.00000  104 ARG   G N   
3375  C CA  . ARG   C  104 ? 0.40966 0.40966 0.40966 0.00000  0.00000  0.00000  104 ARG   G CA  
3376  C C   . ARG   C  104 ? 0.43272 0.43272 0.43272 0.00000  0.00000  0.00000  104 ARG   G C   
3377  O O   . ARG   C  104 ? 0.34163 0.34163 0.34163 0.00000  0.00000  0.00000  104 ARG   G O   
3378  C CB  . ARG   C  104 ? 0.64332 0.64332 0.64332 0.00000  0.00000  0.00000  104 ARG   G CB  
3379  C CG  . ARG   C  104 ? 0.88295 0.88295 0.88295 0.00000  0.00000  0.00000  104 ARG   G CG  
3380  C CD  . ARG   C  104 ? 0.54296 0.54296 0.54296 0.00000  -0.00000 -0.00000 104 ARG   G CD  
3381  N NE  . ARG   C  104 ? 1.56179 1.56179 1.56179 -0.00000 0.00000  0.00000  104 ARG   G NE  
3382  C CZ  . ARG   C  104 ? 1.60515 1.60515 1.60515 0.00000  0.00000  0.00000  104 ARG   G CZ  
3383  N NH1 . ARG   C  104 ? 1.89043 1.89043 1.89043 0.00000  0.00000  0.00000  104 ARG   G NH1 
3384  N NH2 . ARG   C  104 ? 1.42335 1.42335 1.42335 0.00000  0.00000  0.00000  104 ARG   G NH2 
3385  N N   . LYS   C  105 ? 0.37409 0.37409 0.37409 0.00000  0.00000  0.00000  105 LYS   G N   
3386  C CA  . LYS   C  105 ? 0.63673 0.63673 0.63673 0.00000  0.00000  0.00000  105 LYS   G CA  
3387  C C   . LYS   C  105 ? 0.41548 0.41548 0.41548 -0.00000 0.00000  0.00000  105 LYS   G C   
3388  O O   . LYS   C  105 ? 0.47409 0.47409 0.47409 0.00000  0.00000  0.00000  105 LYS   G O   
3389  C CB  . LYS   C  105 ? 0.51283 0.51283 0.51283 0.00000  0.00000  0.00000  105 LYS   G CB  
3390  C CG  . LYS   C  105 ? 0.38548 0.38548 0.38548 -0.00000 0.00000  0.00000  105 LYS   G CG  
3391  C CD  . LYS   C  105 ? 0.39137 0.39137 0.39137 -0.00000 0.00000  0.00000  105 LYS   G CD  
3392  C CE  . LYS   C  105 ? 0.77395 0.77395 0.77395 -0.00000 0.00000  0.00000  105 LYS   G CE  
3393  N NZ  . LYS   C  105 ? 0.93673 0.93673 0.93673 0.00000  0.00000  0.00000  105 LYS   G NZ  
3394  N N   . ALA   C  106 ? 0.63154 0.63154 0.63154 0.00000  0.00000  0.00000  106 ALA   G N   
3395  C CA  . ALA   C  106 ? 0.54619 0.54619 0.54619 0.00000  0.00000  0.00000  106 ALA   G CA  
3396  C C   . ALA   C  106 ? 0.33583 0.33583 0.33583 -0.00000 0.00000  0.00000  106 ALA   G C   
3397  O O   . ALA   C  106 ? 0.58090 0.58090 0.58090 -0.00000 0.00000  0.00000  106 ALA   G O   
3398  C CB  . ALA   C  106 ? 0.37277 0.37277 0.37277 0.00000  0.00000  0.00000  106 ALA   G CB  
3399  N N   . PRO   C  107 ? 0.64616 0.64616 0.64616 0.00000  -0.00000 -0.00000 107 PRO   G N   
3400  C CA  . PRO   C  107 ? 0.42240 0.42240 0.42240 0.00000  0.00000  0.00000  107 PRO   G CA  
3401  C C   . PRO   C  107 ? 0.54757 0.54757 0.54757 0.00000  0.00000  0.00000  107 PRO   G C   
3402  O O   . PRO   C  107 ? 0.48758 0.48758 0.48758 0.00000  -0.00000 0.00000  107 PRO   G O   
3403  C CB  . PRO   C  107 ? 0.39778 0.39778 0.39778 0.00000  0.00000  0.00000  107 PRO   G CB  
3404  C CG  . PRO   C  107 ? 0.35486 0.35486 0.35486 0.00000  0.00000  0.00000  107 PRO   G CG  
3405  C CD  . PRO   C  107 ? 0.27670 0.27670 0.27670 0.00000  0.00000  0.00000  107 PRO   G CD  
3406  N N   . VAL   C  108 ? 0.51562 0.51562 0.51562 0.00000  0.00000  0.00000  108 VAL   G N   
3407  C CA  . VAL   C  108 ? 0.46327 0.46327 0.46327 -0.00000 0.00000  0.00000  108 VAL   G CA  
3408  C C   . VAL   C  108 ? 0.60552 0.60552 0.60552 0.00000  0.00000  0.00000  108 VAL   G C   
3409  O O   . VAL   C  108 ? 0.61331 0.61331 0.61331 0.00000  0.00000  0.00000  108 VAL   G O   
3410  C CB  . VAL   C  108 ? 0.59290 0.59290 0.59290 0.00000  0.00000  0.00000  108 VAL   G CB  
3411  C CG1 . VAL   C  108 ? 0.35255 0.35255 0.35255 -0.00000 0.00000  0.00000  108 VAL   G CG1 
3412  C CG2 . VAL   C  108 ? 0.34933 0.34933 0.34933 0.00000  0.00000  0.00000  108 VAL   G CG2 
3413  N N   . TYR   C  109 ? 0.43270 0.43270 0.43270 0.00000  0.00000  0.00000  109 TYR   G N   
3414  C CA  . TYR   C  109 ? 0.80573 0.80573 0.80573 0.00000  0.00000  0.00000  109 TYR   G CA  
3415  C C   . TYR   C  109 ? 0.42911 0.42911 0.42911 0.00000  0.00000  0.00000  109 TYR   G C   
3416  O O   . TYR   C  109 ? 0.60547 0.60547 0.60547 0.00000  0.00000  0.00000  109 TYR   G O   
3417  C CB  . TYR   C  109 ? 0.35507 0.35507 0.35507 0.00000  0.00000  0.00000  109 TYR   G CB  
3418  C CG  . TYR   C  109 ? 0.77055 0.77055 0.77055 0.00000  0.00000  0.00000  109 TYR   G CG  
3419  C CD1 . TYR   C  109 ? 0.37149 0.37149 0.37149 -0.00000 0.00000  0.00000  109 TYR   G CD1 
3420  C CD2 . TYR   C  109 ? 0.42188 0.42188 0.42188 0.00000  0.00000  0.00000  109 TYR   G CD2 
3421  C CE1 . TYR   C  109 ? 0.89927 0.89927 0.89927 0.00000  0.00000  0.00000  109 TYR   G CE1 
3422  C CE2 . TYR   C  109 ? 0.68964 0.68964 0.68964 0.00000  0.00000  0.00000  109 TYR   G CE2 
3423  C CZ  . TYR   C  109 ? 0.38842 0.38842 0.38842 0.00000  0.00000  0.00000  109 TYR   G CZ  
3424  O OH  . TYR   C  109 ? 0.72113 0.72113 0.72113 0.00000  0.00000  0.00000  109 TYR   G OH  
3425  N N   . GLY   C  110 ? 0.62628 0.62628 0.62628 -0.00000 0.00000  0.00000  110 GLY   G N   
3426  C CA  . GLY   C  110 ? 0.18299 0.18299 0.18299 0.00000  0.00000  0.00000  110 GLY   G CA  
3427  C C   . GLY   C  110 ? 0.60977 0.60977 0.60977 0.00000  0.00000  0.00000  110 GLY   G C   
3428  O O   . GLY   C  110 ? 0.53381 0.53381 0.53381 0.00000  0.00000  0.00000  110 GLY   G O   
3429  N N   . ASP   C  111 ? 0.75925 0.75925 0.75925 -0.00000 0.00000  0.00000  111 ASP   G N   
3430  C CA  . ASP   C  111 ? 0.63993 0.63993 0.63993 0.00000  0.00000  0.00000  111 ASP   G CA  
3431  C C   . ASP   C  111 ? 0.43788 0.43788 0.43788 -0.00000 0.00000  0.00000  111 ASP   G C   
3432  O O   . ASP   C  111 ? 0.60673 0.60673 0.60673 0.00000  0.00000  0.00000  111 ASP   G O   
3433  C CB  . ASP   C  111 ? 0.80118 0.80118 0.80118 0.00000  0.00000  0.00000  111 ASP   G CB  
3434  C CG  . ASP   C  111 ? 0.78485 0.78485 0.78485 0.00000  0.00000  0.00000  111 ASP   G CG  
3435  O OD1 . ASP   C  111 ? 0.98518 0.98518 0.98518 -0.00000 0.00000  0.00000  111 ASP   G OD1 
3436  O OD2 . ASP   C  111 ? 1.22415 1.22415 1.22415 0.00000  -0.00000 0.00000  111 ASP   G OD2 
3437  N N   . LEU   C  112 ? 0.81840 0.81840 0.81840 0.00000  0.00000  0.00000  112 LEU   G N   
3438  C CA  . LEU   C  112 ? 0.16872 0.16872 0.16872 0.00000  0.00000  0.00000  112 LEU   G CA  
3439  C C   . LEU   C  112 ? 0.93143 0.93143 0.93143 0.00000  0.00000  0.00000  112 LEU   G C   
3440  O O   . LEU   C  112 ? 0.43989 0.43989 0.43989 -0.00000 0.00000  0.00000  112 LEU   G O   
3441  C CB  . LEU   C  112 ? 0.91014 0.91014 0.91014 -0.00000 0.00000  0.00000  112 LEU   G CB  
3442  C CG  . LEU   C  112 ? 1.77479 1.77479 1.77479 0.00000  0.00000  0.00000  112 LEU   G CG  
3443  C CD1 . LEU   C  112 ? 1.01595 1.01595 1.01595 0.00000  0.00000  0.00000  112 LEU   G CD1 
3444  C CD2 . LEU   C  112 ? 1.82998 1.82998 1.82998 0.00000  0.00000  0.00000  112 LEU   G CD2 
3445  N N   . GLY   C  113 ? 0.43399 0.43399 0.43399 -0.00000 0.00000  0.00000  113 GLY   G N   
3446  C CA  . GLY   C  113 ? 0.41472 0.41472 0.41472 -0.00000 0.00000  0.00000  113 GLY   G CA  
3447  C C   . GLY   C  113 ? 0.46018 0.46018 0.46018 0.00000  0.00000  0.00000  113 GLY   G C   
3448  O O   . GLY   C  113 ? 0.44041 0.44041 0.44041 0.00000  0.00000  0.00000  113 GLY   G O   
3449  N N   . PRO   C  114 ? 0.43443 0.43443 0.43443 -0.00000 0.00000  0.00000  114 PRO   G N   
3450  C CA  . PRO   C  114 ? 0.34980 0.34980 0.34980 -0.00000 0.00000  0.00000  114 PRO   G CA  
3451  C C   . PRO   C  114 ? 0.38729 0.38729 0.38729 -0.00000 0.00000  0.00000  114 PRO   G C   
3452  O O   . PRO   C  114 ? 0.44389 0.44389 0.44389 0.00000  0.00000  0.00000  114 PRO   G O   
3453  C CB  . PRO   C  114 ? 0.41327 0.41327 0.41327 0.00000  0.00000  0.00000  114 PRO   G CB  
3454  C CG  . PRO   C  114 ? 0.37471 0.37471 0.37471 -0.00000 0.00000  0.00000  114 PRO   G CG  
3455  C CD  . PRO   C  114 ? 0.38846 0.38846 0.38846 -0.00000 0.00000  0.00000  114 PRO   G CD  
3456  N N   . PRO   C  115 ? 0.36023 0.36023 0.36023 -0.00000 0.00000  0.00000  115 PRO   G N   
3457  C CA  . PRO   C  115 ? 0.49936 0.49936 0.49936 0.00000  0.00000  0.00000  115 PRO   G CA  
3458  C C   . PRO   C  115 ? 0.39929 0.39929 0.39929 -0.00000 0.00000  0.00000  115 PRO   G C   
3459  O O   . PRO   C  115 ? 0.46380 0.46380 0.46380 -0.00000 0.00000  0.00000  115 PRO   G O   
3460  C CB  . PRO   C  115 ? 0.26851 0.26851 0.26851 -0.00000 0.00000  0.00000  115 PRO   G CB  
3461  C CG  . PRO   C  115 ? 0.30091 0.30091 0.30091 0.00000  -0.00000 0.00000  115 PRO   G CG  
3462  C CD  . PRO   C  115 ? 0.42715 0.42715 0.42715 0.00000  0.00000  0.00000  115 PRO   G CD  
3463  N N   . VAL   C  116 ? 0.45711 0.45711 0.45711 0.00000  -0.00000 0.00000  116 VAL   G N   
3464  C CA  . VAL   C  116 ? 0.33376 0.33376 0.33376 -0.00000 0.00000  0.00000  116 VAL   G CA  
3465  C C   . VAL   C  116 ? 0.36519 0.36519 0.36519 -0.00000 0.00000  0.00000  116 VAL   G C   
3466  O O   . VAL   C  116 ? 0.41045 0.41045 0.41045 0.00000  0.00000  0.00000  116 VAL   G O   
3467  C CB  . VAL   C  116 ? 0.42458 0.42458 0.42458 0.00000  0.00000  0.00000  116 VAL   G CB  
3468  C CG1 . VAL   C  116 ? 0.32420 0.32420 0.32420 0.00000  0.00000  0.00000  116 VAL   G CG1 
3469  C CG2 . VAL   C  116 ? 0.22236 0.22236 0.22236 0.00000  0.00000  0.00000  116 VAL   G CG2 
3470  N N   . TYR   C  117 ? 0.33824 0.33824 0.33824 -0.00000 0.00000  0.00000  117 TYR   G N   
3471  C CA  . TYR   C  117 ? 0.50964 0.50964 0.50964 0.00000  0.00000  0.00000  117 TYR   G CA  
3472  C C   . TYR   C  117 ? 0.43391 0.43391 0.43391 -0.00000 0.00000  0.00000  117 TYR   G C   
3473  O O   . TYR   C  117 ? 0.49738 0.49738 0.49738 0.00000  0.00000  0.00000  117 TYR   G O   
3474  C CB  . TYR   C  117 ? 0.32707 0.32707 0.32707 -0.00000 0.00000  0.00000  117 TYR   G CB  
3475  C CG  . TYR   C  117 ? 0.41915 0.41915 0.41915 -0.00000 0.00000  0.00000  117 TYR   G CG  
3476  C CD1 . TYR   C  117 ? 0.37139 0.37139 0.37139 0.00000  0.00000  0.00000  117 TYR   G CD1 
3477  C CD2 . TYR   C  117 ? 0.58302 0.58302 0.58302 0.00000  0.00000  0.00000  117 TYR   G CD2 
3478  C CE1 . TYR   C  117 ? 0.37686 0.37686 0.37686 -0.00000 0.00000  0.00000  117 TYR   G CE1 
3479  C CE2 . TYR   C  117 ? 0.29698 0.29698 0.29698 0.00000  0.00000  0.00000  117 TYR   G CE2 
3480  C CZ  . TYR   C  117 ? 0.50504 0.50504 0.50504 0.00000  0.00000  0.00000  117 TYR   G CZ  
3481  O OH  . TYR   C  117 ? 0.37514 0.37514 0.37514 -0.00000 0.00000  0.00000  117 TYR   G OH  
3482  N N   . MET   C  118 ? 0.45225 0.45225 0.45225 -0.00000 0.00000  0.00000  118 MET   G N   
3483  C CA  . MET   C  118 ? 0.32347 0.32347 0.32347 0.00000  0.00000  0.00000  118 MET   G CA  
3484  C C   . MET   C  118 ? 0.52131 0.52131 0.52131 0.00000  0.00000  0.00000  118 MET   G C   
3485  O O   . MET   C  118 ? 0.42211 0.42211 0.42211 0.00000  0.00000  0.00000  118 MET   G O   
3486  C CB  . MET   C  118 ? 0.36234 0.36234 0.36234 0.00000  0.00000  0.00000  118 MET   G CB  
3487  C CG  . MET   C  118 ? 0.23152 0.23152 0.23152 0.00000  0.00000  0.00000  118 MET   G CG  
3488  S SD  . MET   C  118 ? 0.46222 0.46222 0.46222 -0.00000 0.00000  0.00000  118 MET   G SD  
3489  C CE  . MET   C  118 ? 0.52013 0.52013 0.52013 0.00000  0.00000  0.00000  118 MET   G CE  
3490  N N   . ILE   C  119 ? 0.40624 0.40624 0.40624 -0.00000 0.00000  0.00000  119 ILE   G N   
3491  C CA  . ILE   C  119 ? 0.55163 0.55163 0.55163 0.00000  0.00000  0.00000  119 ILE   G CA  
3492  C C   . ILE   C  119 ? 0.55714 0.55714 0.55714 0.00000  0.00000  0.00000  119 ILE   G C   
3493  O O   . ILE   C  119 ? 0.61618 0.61618 0.61618 0.00000  0.00000  0.00000  119 ILE   G O   
3494  C CB  . ILE   C  119 ? 0.44995 0.44995 0.44995 0.00000  0.00000  -0.00000 119 ILE   G CB  
3495  C CG1 . ILE   C  119 ? 0.47895 0.47895 0.47895 0.00000  0.00000  0.00000  119 ILE   G CG1 
3496  C CG2 . ILE   C  119 ? 0.54506 0.54506 0.54506 0.00000  0.00000  0.00000  119 ILE   G CG2 
3497  C CD1 . ILE   C  119 ? 0.54073 0.54073 0.54073 0.00000  0.00000  0.00000  119 ILE   G CD1 
3498  N N   . MET   C  120 ? 0.32943 0.32943 0.32943 -0.00000 0.00000  0.00000  120 MET   G N   
3499  C CA  . MET   C  120 ? 0.30408 0.30408 0.30408 0.00000  0.00000  0.00000  120 MET   G CA  
3500  C C   . MET   C  120 ? 0.37793 0.37793 0.37793 -0.00000 0.00000  0.00000  120 MET   G C   
3501  O O   . MET   C  120 ? 0.37293 0.37293 0.37293 -0.00000 0.00000  0.00000  120 MET   G O   
3502  C CB  . MET   C  120 ? 0.14735 0.14735 0.14735 0.00000  0.00000  0.00000  120 MET   G CB  
3503  C CG  . MET   C  120 ? 0.24730 0.24730 0.24730 0.00000  0.00000  0.00000  120 MET   G CG  
3504  S SD  . MET   C  120 ? 0.45145 0.45145 0.45145 0.00000  0.00000  0.00000  120 MET   G SD  
3505  C CE  . MET   C  120 ? 0.25691 0.25691 0.25691 0.00000  0.00000  0.00000  120 MET   G CE  
3506  N N   . ALA   C  121 ? 0.34136 0.34136 0.34136 0.00000  -0.00000 0.00000  121 ALA   G N   
3507  C CA  . ALA   C  121 ? 0.41463 0.41463 0.41463 0.00000  0.00000  0.00000  121 ALA   G CA  
3508  C C   . ALA   C  121 ? 0.41938 0.41938 0.41938 -0.00000 0.00000  0.00000  121 ALA   G C   
3509  O O   . ALA   C  121 ? 0.50770 0.50770 0.50770 0.00000  0.00000  0.00000  121 ALA   G O   
3510  C CB  . ALA   C  121 ? 0.31224 0.31224 0.31224 0.00000  0.00000  0.00000  121 ALA   G CB  
3511  N N   . LYS   C  122 ? 0.36404 0.36404 0.36404 0.00000  0.00000  0.00000  122 LYS   G N   
3512  C CA  . LYS   C  122 ? 0.26952 0.26952 0.26952 0.00000  0.00000  0.00000  122 LYS   G CA  
3513  C C   . LYS   C  122 ? 0.44968 0.44968 0.44968 0.00000  0.00000  0.00000  122 LYS   G C   
3514  O O   . LYS   C  122 ? 0.37157 0.37157 0.37157 0.00000  0.00000  0.00000  122 LYS   G O   
3515  C CB  . LYS   C  122 ? 0.26210 0.26210 0.26210 -0.00000 0.00000  0.00000  122 LYS   G CB  
3516  N N   . LEU   C  123 ? 0.39959 0.39959 0.39959 0.00000  0.00000  0.00000  123 LEU   G N   
3517  C CA  . LEU   C  123 ? 0.39327 0.39327 0.39327 0.00000  0.00000  0.00000  123 LEU   G CA  
3518  C C   . LEU   C  123 ? 0.70976 0.70976 0.70976 0.00000  0.00000  0.00000  123 LEU   G C   
3519  O O   . LEU   C  123 ? 0.29282 0.29282 0.29282 -0.00000 0.00000  0.00000  123 LEU   G O   
3520  C CB  . LEU   C  123 ? 0.28038 0.28038 0.28038 0.00000  0.00000  0.00000  123 LEU   G CB  
3521  C CG  . LEU   C  123 ? 0.39364 0.39364 0.39364 -0.00000 0.00000  0.00000  123 LEU   G CG  
3522  C CD1 . LEU   C  123 ? 0.31960 0.31960 0.31960 0.00000  0.00000  0.00000  123 LEU   G CD1 
3523  C CD2 . LEU   C  123 ? 0.31744 0.31744 0.31744 0.00000  0.00000  0.00000  123 LEU   G CD2 
3524  N N   . MET   C  124 ? 0.33373 0.33373 0.33373 0.00000  0.00000  0.00000  124 MET   G N   
3525  C CA  . MET   C  124 ? 0.47801 0.47801 0.47801 0.00000  0.00000  0.00000  124 MET   G CA  
3526  C C   . MET   C  124 ? 0.38386 0.38386 0.38386 -0.00000 -0.00000 0.00000  124 MET   G C   
3527  O O   . MET   C  124 ? 0.37309 0.37309 0.37309 0.00000  0.00000  0.00000  124 MET   G O   
3528  C CB  . MET   C  124 ? 0.19409 0.19409 0.19409 0.00000  0.00000  0.00000  124 MET   G CB  
3529  C CG  . MET   C  124 ? 0.45050 0.45050 0.45050 -0.00000 0.00000  0.00000  124 MET   G CG  
3530  S SD  . MET   C  124 ? 0.47438 0.47438 0.47438 0.00000  0.00000  0.00000  124 MET   G SD  
3531  C CE  . MET   C  124 ? 0.16627 0.16627 0.16627 0.00000  0.00000  0.00000  124 MET   G CE  
3532  N N   . ASN   C  125 ? 0.45646 0.45646 0.45646 0.00000  0.00000  0.00000  125 ASN   G N   
3533  C CA  . ASN   C  125 ? 0.37898 0.37898 0.37898 -0.00000 0.00000  0.00000  125 ASN   G CA  
3534  C C   . ASN   C  125 ? 0.45021 0.45021 0.45021 -0.00000 0.00000  0.00000  125 ASN   G C   
3535  O O   . ASN   C  125 ? 0.50072 0.50072 0.50072 -0.00000 0.00000  0.00000  125 ASN   G O   
3536  C CB  . ASN   C  125 ? 0.35981 0.35981 0.35981 0.00000  0.00000  0.00000  125 ASN   G CB  
3537  C CG  . ASN   C  125 ? 0.33613 0.33613 0.33613 0.00000  0.00000  0.00000  125 ASN   G CG  
3538  O OD1 . ASN   C  125 ? 0.41419 0.41419 0.41419 0.00000  0.00000  0.00000  125 ASN   G OD1 
3539  N ND2 . ASN   C  125 ? 0.55541 0.55541 0.55541 0.00000  0.00000  0.00000  125 ASN   G ND2 
3540  N N   . THR   C  126 ? 0.43698 0.43698 0.43698 0.00000  0.00000  0.00000  126 THR   G N   
3541  C CA  . THR   C  126 ? 0.55210 0.55210 0.55210 -0.00000 0.00000  0.00000  126 THR   G CA  
3542  C C   . THR   C  126 ? 0.28450 0.28450 0.28450 0.00000  0.00000  0.00000  126 THR   G C   
3543  O O   . THR   C  126 ? 0.52415 0.52415 0.52415 0.00000  0.00000  0.00000  126 THR   G O   
3544  C CB  . THR   C  126 ? 0.35896 0.35896 0.35896 0.00000  0.00000  0.00000  126 THR   G CB  
3545  O OG1 . THR   C  126 ? 0.35165 0.35165 0.35165 0.00000  0.00000  0.00000  126 THR   G OG1 
3546  C CG2 . THR   C  126 ? 0.16924 0.16924 0.16924 -0.00000 0.00000  0.00000  126 THR   G CG2 
3547  N N   . ARG   C  127 ? 0.40059 0.40059 0.40059 -0.00000 0.00000  0.00000  127 ARG   G N   
3548  C CA  . ARG   C  127 ? 0.30210 0.30210 0.30210 -0.00000 0.00000  0.00000  127 ARG   G CA  
3549  C C   . ARG   C  127 ? 0.58342 0.58342 0.58342 0.00000  0.00000  0.00000  127 ARG   G C   
3550  O O   . ARG   C  127 ? 0.40288 0.40288 0.40288 0.00000  0.00000  0.00000  127 ARG   G O   
3551  C CB  . ARG   C  127 ? 0.11255 0.11255 0.11255 0.00000  0.00000  0.00000  127 ARG   G CB  
3552  C CG  . ARG   C  127 ? 1.39710 1.39710 1.39710 0.00000  0.00000  0.00000  127 ARG   G CG  
3553  C CD  . ARG   C  127 ? 0.76430 0.76430 0.76430 0.00000  0.00000  0.00000  127 ARG   G CD  
3554  N NE  . ARG   C  127 ? 1.61257 1.61257 1.61257 0.00000  0.00000  0.00000  127 ARG   G NE  
3555  C CZ  . ARG   C  127 ? 0.95134 0.95134 0.95134 0.00000  0.00000  0.00000  127 ARG   G CZ  
3556  N NH1 . ARG   C  127 ? 0.82935 0.82935 0.82935 0.00000  0.00000  0.00000  127 ARG   G NH1 
3557  N NH2 . ARG   C  127 ? 1.22390 1.22390 1.22390 0.00000  0.00000  0.00000  127 ARG   G NH2 
3558  N N   . ALA   C  128 ? 0.23956 0.23956 0.23956 -0.00000 0.00000  0.00000  128 ALA   G N   
3559  C CA  . ALA   C  128 ? 0.40384 0.40384 0.40384 0.00000  0.00000  -0.00000 128 ALA   G CA  
3560  C C   . ALA   C  128 ? 0.28898 0.28898 0.28898 0.00000  0.00000  0.00000  128 ALA   G C   
3561  O O   . ALA   C  128 ? 0.42627 0.42627 0.42627 -0.00000 0.00000  0.00000  128 ALA   G O   
3562  C CB  . ALA   C  128 ? 0.26159 0.26159 0.26159 0.00000  0.00000  0.00000  128 ALA   G CB  
3563  N N   . GLY   C  129 ? 0.57447 0.57447 0.57447 -0.00000 0.00000  0.00000  129 GLY   G N   
3564  C CA  . GLY   C  129 ? 0.16930 0.16930 0.16930 -0.00000 0.00000  0.00000  129 GLY   G CA  
3565  C C   . GLY   C  129 ? 0.47956 0.47956 0.47956 -0.00000 0.00000  0.00000  129 GLY   G C   
3566  O O   . GLY   C  129 ? 0.35095 0.35095 0.35095 0.00000  0.00000  0.00000  129 GLY   G O   
3567  N N   . PHE   C  130 ? 0.31624 0.31624 0.31624 -0.00000 0.00000  0.00000  130 PHE   G N   
3568  C CA  . PHE   C  130 ? 0.31734 0.31734 0.31734 -0.00000 0.00000  0.00000  130 PHE   G CA  
3569  C C   . PHE   C  130 ? 0.58244 0.58244 0.58244 0.00000  0.00000  0.00000  130 PHE   G C   
3570  O O   . PHE   C  130 ? 0.47041 0.47041 0.47041 -0.00000 0.00000  0.00000  130 PHE   G O   
3571  C CB  . PHE   C  130 ? 0.17285 0.17285 0.17285 -0.00000 0.00000  0.00000  130 PHE   G CB  
3572  C CG  . PHE   C  130 ? 0.34313 0.34313 0.34313 0.00000  0.00000  0.00000  130 PHE   G CG  
3573  C CD1 . PHE   C  130 ? 0.34308 0.34308 0.34308 -0.00000 0.00000  0.00000  130 PHE   G CD1 
3574  C CD2 . PHE   C  130 ? 0.26204 0.26204 0.26204 0.00000  0.00000  0.00000  130 PHE   G CD2 
3575  C CE1 . PHE   C  130 ? 0.32830 0.32830 0.32830 0.00000  0.00000  0.00000  130 PHE   G CE1 
3576  C CE2 . PHE   C  130 ? 0.43714 0.43714 0.43714 0.00000  0.00000  0.00000  130 PHE   G CE2 
3577  C CZ  . PHE   C  130 ? 0.26550 0.26550 0.26550 0.00000  0.00000  0.00000  130 PHE   G CZ  
3578  N N   . SER   C  131 ? 0.30503 0.30503 0.30503 -0.00000 0.00000  0.00000  131 SER   G N   
3579  C CA  . SER   C  131 ? 0.52887 0.52887 0.52887 -0.00000 -0.00000 0.00000  131 SER   G CA  
3580  C C   . SER   C  131 ? 0.37257 0.37257 0.37257 0.00000  0.00000  0.00000  131 SER   G C   
3581  O O   . SER   C  131 ? 0.50994 0.50994 0.50994 -0.00000 0.00000  0.00000  131 SER   G O   
3582  C CB  . SER   C  131 ? 0.16443 0.16443 0.16443 -0.00000 0.00000  0.00000  131 SER   G CB  
3583  O OG  . SER   C  131 ? 1.07463 1.07463 1.07463 -0.00000 0.00000  0.00000  131 SER   G OG  
3584  N N   . ALA   C  132 ? 0.34445 0.34445 0.34445 0.00000  0.00000  0.00000  132 ALA   G N   
3585  C CA  . ALA   C  132 ? 0.27178 0.27178 0.27178 0.00000  0.00000  0.00000  132 ALA   G CA  
3586  C C   . ALA   C  132 ? 0.45277 0.45277 0.45277 0.00000  0.00000  0.00000  132 ALA   G C   
3587  O O   . ALA   C  132 ? 0.37379 0.37379 0.37379 -0.00000 0.00000  0.00000  132 ALA   G O   
3588  C CB  . ALA   C  132 ? 0.28093 0.28093 0.28093 0.00000  -0.00000 0.00000  132 ALA   G CB  
3589  N N   . PHE   C  133 ? 0.27942 0.27942 0.27942 0.00000  0.00000  0.00000  133 PHE   G N   
3590  C CA  . PHE   C  133 ? 0.41335 0.41335 0.41335 -0.00000 0.00000  0.00000  133 PHE   G CA  
3591  C C   . PHE   C  133 ? 0.50135 0.50135 0.50135 -0.00000 0.00000  0.00000  133 PHE   G C   
3592  O O   . PHE   C  133 ? 0.36853 0.36853 0.36853 -0.00000 0.00000  0.00000  133 PHE   G O   
3593  C CB  . PHE   C  133 ? 0.31480 0.31480 0.31480 0.00000  0.00000  0.00000  133 PHE   G CB  
3594  C CG  . PHE   C  133 ? 0.45348 0.45348 0.45348 0.00000  0.00000  0.00000  133 PHE   G CG  
3595  C CD1 . PHE   C  133 ? 0.39715 0.39715 0.39715 -0.00000 0.00000  0.00000  133 PHE   G CD1 
3596  C CD2 . PHE   C  133 ? 0.33018 0.33018 0.33018 0.00000  0.00000  0.00000  133 PHE   G CD2 
3597  C CE1 . PHE   C  133 ? 0.29411 0.29411 0.29411 0.00000  0.00000  0.00000  133 PHE   G CE1 
3598  C CE2 . PHE   C  133 ? 0.32287 0.32287 0.32287 0.00000  0.00000  0.00000  133 PHE   G CE2 
3599  C CZ  . PHE   C  133 ? 0.24426 0.24426 0.24426 0.00000  0.00000  0.00000  133 PHE   G CZ  
3600  N N   . THR   C  134 ? 0.28456 0.28456 0.28456 0.00000  -0.00000 0.00000  134 THR   G N   
3601  C CA  . THR   C  134 ? 0.34357 0.34357 0.34357 0.00000  0.00000  0.00000  134 THR   G CA  
3602  C C   . THR   C  134 ? 0.31604 0.31604 0.31604 0.00000  -0.00000 0.00000  134 THR   G C   
3603  O O   . THR   C  134 ? 0.41675 0.41675 0.41675 0.00000  0.00000  0.00000  134 THR   G O   
3604  C CB  . THR   C  134 ? 0.34378 0.34378 0.34378 -0.00000 0.00000  0.00000  134 THR   G CB  
3605  O OG1 . THR   C  134 ? 0.41582 0.41582 0.41582 0.00000  0.00000  0.00000  134 THR   G OG1 
3606  C CG2 . THR   C  134 ? 0.25506 0.25506 0.25506 0.00000  0.00000  0.00000  134 THR   G CG2 
3607  N N   . ARG   C  135 ? 0.34242 0.34242 0.34242 -0.00000 0.00000  0.00000  135 ARG   G N   
3608  C CA  . ARG   C  135 ? 0.34468 0.34468 0.34468 0.00000  0.00000  0.00000  135 ARG   G CA  
3609  C C   . ARG   C  135 ? 0.51724 0.51724 0.51724 -0.00000 0.00000  0.00000  135 ARG   G C   
3610  O O   . ARG   C  135 ? 0.34764 0.34764 0.34764 -0.00000 0.00000  0.00000  135 ARG   G O   
3611  C CB  . ARG   C  135 ? 0.22839 0.22839 0.22839 0.00000  0.00000  0.00000  135 ARG   G CB  
3612  C CG  . ARG   C  135 ? 0.28165 0.28165 0.28165 -0.00000 0.00000  0.00000  135 ARG   G CG  
3613  C CD  . ARG   C  135 ? 0.31630 0.31630 0.31630 -0.00000 0.00000  0.00000  135 ARG   G CD  
3614  N NE  . ARG   C  135 ? 0.56067 0.56067 0.56067 0.00000  0.00000  0.00000  135 ARG   G NE  
3615  C CZ  . ARG   C  135 ? 0.60900 0.60900 0.60900 -0.00000 -0.00000 0.00000  135 ARG   G CZ  
3616  N NH1 . ARG   C  135 ? 0.49723 0.49723 0.49723 -0.00000 0.00000  0.00000  135 ARG   G NH1 
3617  N NH2 . ARG   C  135 ? 0.47101 0.47101 0.47101 -0.00000 0.00000  0.00000  135 ARG   G NH2 
3618  N N   . GLN   C  136 ? 0.32644 0.32644 0.32644 -0.00000 0.00000  0.00000  136 GLN   G N   
3619  C CA  . GLN   C  136 ? 0.35200 0.35200 0.35200 0.00000  0.00000  0.00000  136 GLN   G CA  
3620  C C   . GLN   C  136 ? 0.31862 0.31862 0.31862 0.00000  0.00000  0.00000  136 GLN   G C   
3621  O O   . GLN   C  136 ? 0.54019 0.54019 0.54019 0.00000  0.00000  0.00000  136 GLN   G O   
3622  C CB  . GLN   C  136 ? 0.32734 0.32734 0.32734 0.00000  0.00000  0.00000  136 GLN   G CB  
3623  C CG  . GLN   C  136 ? 0.26696 0.26696 0.26696 -0.00000 0.00000  0.00000  136 GLN   G CG  
3624  C CD  . GLN   C  136 ? 0.58686 0.58686 0.58686 0.00000  0.00000  0.00000  136 GLN   G CD  
3625  O OE1 . GLN   C  136 ? 0.43386 0.43386 0.43386 0.00000  0.00000  0.00000  136 GLN   G OE1 
3626  N NE2 . GLN   C  136 ? 0.27332 0.27332 0.27332 -0.00000 0.00000  0.00000  136 GLN   G NE2 
3627  N N   . ARG   C  137 ? 0.31092 0.31092 0.31092 0.00000  0.00000  0.00000  137 ARG   G N   
3628  C CA  . ARG   C  137 ? 0.30119 0.30119 0.30119 0.00000  0.00000  0.00000  137 ARG   G CA  
3629  C C   . ARG   C  137 ? 0.23974 0.23974 0.23974 0.00000  0.00000  0.00000  137 ARG   G C   
3630  O O   . ARG   C  137 ? 0.47300 0.47300 0.47300 0.00000  0.00000  0.00000  137 ARG   G O   
3631  C CB  . ARG   C  137 ? 0.20945 0.20945 0.20945 0.00000  0.00000  0.00000  137 ARG   G CB  
3632  C CG  . ARG   C  137 ? 0.23472 0.23472 0.23472 -0.00000 0.00000  0.00000  137 ARG   G CG  
3633  C CD  . ARG   C  137 ? 0.33397 0.33397 0.33397 -0.00000 0.00000  0.00000  137 ARG   G CD  
3634  N NE  . ARG   C  137 ? 0.36621 0.36621 0.36621 0.00000  -0.00000 0.00000  137 ARG   G NE  
3635  C CZ  . ARG   C  137 ? 0.60122 0.60122 0.60122 0.00000  0.00000  0.00000  137 ARG   G CZ  
3636  N NH1 . ARG   C  137 ? 0.19776 0.19776 0.19776 -0.00000 0.00000  0.00000  137 ARG   G NH1 
3637  N NH2 . ARG   C  137 ? 0.38916 0.38916 0.38916 0.00000  0.00000  0.00000  137 ARG   G NH2 
3638  N N   . LEU   C  138 ? 0.17587 0.17587 0.17587 0.00000  0.00000  0.00000  138 LEU   G N   
3639  C CA  . LEU   C  138 ? 0.34124 0.34124 0.34124 -0.00000 0.00000  0.00000  138 LEU   G CA  
3640  C C   . LEU   C  138 ? 0.46079 0.46079 0.46079 0.00000  0.00000  0.00000  138 LEU   G C   
3641  O O   . LEU   C  138 ? 0.32843 0.32843 0.32843 -0.00000 0.00000  0.00000  138 LEU   G O   
3642  C CB  . LEU   C  138 ? 0.26251 0.26251 0.26251 0.00000  0.00000  0.00000  138 LEU   G CB  
3643  C CG  . LEU   C  138 ? 0.43830 0.43830 0.43830 0.00000  0.00000  0.00000  138 LEU   G CG  
3644  C CD1 . LEU   C  138 ? 0.26705 0.26705 0.26705 0.00000  0.00000  0.00000  138 LEU   G CD1 
3645  C CD2 . LEU   C  138 ? 0.23327 0.23327 0.23327 0.00000  0.00000  -0.00000 138 LEU   G CD2 
3646  N N   . ASN   C  139 ? 0.25378 0.25378 0.25378 -0.00000 0.00000  0.00000  139 ASN   G N   
3647  C CA  . ASN   C  139 ? 0.45899 0.45899 0.45899 0.00000  0.00000  0.00000  139 ASN   G CA  
3648  C C   . ASN   C  139 ? 0.28937 0.28937 0.28937 -0.00000 0.00000  0.00000  139 ASN   G C   
3649  O O   . ASN   C  139 ? 0.46544 0.46544 0.46544 0.00000  0.00000  0.00000  139 ASN   G O   
3650  C CB  . ASN   C  139 ? 0.15884 0.15884 0.15884 -0.00000 0.00000  0.00000  139 ASN   G CB  
3651  C CG  . ASN   C  139 ? 0.37190 0.37190 0.37190 0.00000  0.00000  0.00000  139 ASN   G CG  
3652  O OD1 . ASN   C  139 ? 0.26525 0.26525 0.26525 0.00000  0.00000  -0.00000 139 ASN   G OD1 
3653  N ND2 . ASN   C  139 ? 0.22498 0.22498 0.22498 0.00000  0.00000  0.00000  139 ASN   G ND2 
3654  N N   . LEU   C  140 ? 0.45683 0.45683 0.45683 -0.00000 0.00000  0.00000  140 LEU   G N   
3655  C CA  . LEU   C  140 ? 0.30677 0.30677 0.30677 0.00000  0.00000  0.00000  140 LEU   G CA  
3656  C C   . LEU   C  140 ? 0.58895 0.58895 0.58895 0.00000  0.00000  0.00000  140 LEU   G C   
3657  O O   . LEU   C  140 ? 0.32203 0.32203 0.32203 0.00000  0.00000  0.00000  140 LEU   G O   
3658  C CB  . LEU   C  140 ? 0.30092 0.30092 0.30092 0.00000  0.00000  0.00000  140 LEU   G CB  
3659  C CG  . LEU   C  140 ? 0.50662 0.50662 0.50662 0.00000  -0.00000 0.00000  140 LEU   G CG  
3660  C CD1 . LEU   C  140 ? 0.22758 0.22758 0.22758 0.00000  0.00000  0.00000  140 LEU   G CD1 
3661  C CD2 . LEU   C  140 ? 0.14976 0.14976 0.14976 0.00000  0.00000  0.00000  140 LEU   G CD2 
3662  N N   . HIS   C  141 ? 0.35554 0.35554 0.35554 -0.00000 0.00000  0.00000  141 HIS   G N   
3663  C CA  . HIS   C  141 ? 0.32892 0.32892 0.32892 -0.00000 0.00000  0.00000  141 HIS   G CA  
3664  C C   . HIS   C  141 ? 0.34383 0.34383 0.34383 0.00000  0.00000  0.00000  141 HIS   G C   
3665  O O   . HIS   C  141 ? 0.42852 0.42852 0.42852 0.00000  0.00000  0.00000  141 HIS   G O   
3666  C CB  . HIS   C  141 ? 0.20197 0.20197 0.20197 0.00000  0.00000  0.00000  141 HIS   G CB  
3667  C CG  . HIS   C  141 ? 0.55090 0.55090 0.55090 -0.00000 0.00000  0.00000  141 HIS   G CG  
3668  N ND1 . HIS   C  141 ? 0.52351 0.52351 0.52351 -0.00000 -0.00000 0.00000  141 HIS   G ND1 
3669  C CD2 . HIS   C  141 ? 0.46425 0.46425 0.46425 0.00000  0.00000  0.00000  141 HIS   G CD2 
3670  C CE1 . HIS   C  141 ? 0.36548 0.36548 0.36548 0.00000  0.00000  0.00000  141 HIS   G CE1 
3671  N NE2 . HIS   C  141 ? 0.53327 0.53327 0.53327 0.00000  0.00000  0.00000  141 HIS   G NE2 
3672  N N   . PHE   C  142 ? 0.40068 0.40068 0.40068 0.00000  0.00000  0.00000  142 PHE   G N   
3673  C CA  . PHE   C  142 ? 0.56830 0.56830 0.56830 -0.00000 0.00000  0.00000  142 PHE   G CA  
3674  C C   . PHE   C  142 ? 0.40232 0.40232 0.40232 0.00000  0.00000  0.00000  142 PHE   G C   
3675  O O   . PHE   C  142 ? 0.42713 0.42713 0.42713 0.00000  0.00000  0.00000  142 PHE   G O   
3676  C CB  . PHE   C  142 ? 0.39056 0.39056 0.39056 0.00000  0.00000  0.00000  142 PHE   G CB  
3677  C CG  . PHE   C  142 ? 0.48155 0.48155 0.48155 0.00000  -0.00000 0.00000  142 PHE   G CG  
3678  C CD1 . PHE   C  142 ? 0.41609 0.41609 0.41609 -0.00000 0.00000  0.00000  142 PHE   G CD1 
3679  C CD2 . PHE   C  142 ? 0.43498 0.43498 0.43498 0.00000  0.00000  0.00000  142 PHE   G CD2 
3680  C CE1 . PHE   C  142 ? 0.40443 0.40443 0.40443 -0.00000 0.00000  0.00000  142 PHE   G CE1 
3681  C CE2 . PHE   C  142 ? 0.44898 0.44898 0.44898 -0.00000 0.00000  0.00000  142 PHE   G CE2 
3682  C CZ  . PHE   C  142 ? 0.38840 0.38840 0.38840 -0.00000 0.00000  0.00000  142 PHE   G CZ  
3683  N N   . LYS   C  143 ? 0.42588 0.42588 0.42588 0.00000  0.00000  0.00000  143 LYS   G N   
3684  C CA  . LYS   C  143 ? 0.37100 0.37100 0.37100 0.00000  0.00000  0.00000  143 LYS   G CA  
3685  C C   . LYS   C  143 ? 0.41249 0.41249 0.41249 0.00000  0.00000  0.00000  143 LYS   G C   
3686  O O   . LYS   C  143 ? 0.45506 0.45506 0.45506 -0.00000 0.00000  0.00000  143 LYS   G O   
3687  C CB  . LYS   C  143 ? 0.41600 0.41600 0.41600 -0.00000 0.00000  0.00000  143 LYS   G CB  
3688  C CG  . LYS   C  143 ? 0.24584 0.24584 0.24584 0.00000  0.00000  0.00000  143 LYS   G CG  
3689  C CD  . LYS   C  143 ? 0.34921 0.34921 0.34921 0.00000  0.00000  0.00000  143 LYS   G CD  
3690  C CE  . LYS   C  143 ? 0.43227 0.43227 0.43227 0.00000  0.00000  0.00000  143 LYS   G CE  
3691  N NZ  . LYS   C  143 ? 0.49065 0.49065 0.49065 -0.00000 0.00000  0.00000  143 LYS   G NZ  
3692  N N   . LYS   C  144 ? 0.51052 0.51052 0.51052 0.00000  -0.00000 0.00000  144 LYS   G N   
3693  C CA  . LYS   C  144 ? 0.33254 0.33254 0.33254 0.00000  0.00000  0.00000  144 LYS   G CA  
3694  C C   . LYS   C  144 ? 0.60397 0.60397 0.60397 0.00000  0.00000  0.00000  144 LYS   G C   
3695  O O   . LYS   C  144 ? 0.23649 0.23649 0.23649 0.00000  0.00000  0.00000  144 LYS   G O   
3696  C CB  . LYS   C  144 ? 0.26632 0.26632 0.26632 0.00000  0.00000  0.00000  144 LYS   G CB  
3697  C CG  . LYS   C  144 ? 0.23392 0.23392 0.23392 0.00000  0.00000  0.00000  144 LYS   G CG  
3698  C CD  . LYS   C  144 ? 1.38438 1.38438 1.38438 0.00000  -0.00000 0.00000  144 LYS   G CD  
3699  C CE  . LYS   C  144 ? 1.29440 1.29440 1.29440 0.00000  0.00000  0.00000  144 LYS   G CE  
3700  N NZ  . LYS   C  144 ? 1.18269 1.18269 1.18269 -0.00000 0.00000  0.00000  144 LYS   G NZ  
3701  N N   . LEU   C  145 ? 0.32754 0.32754 0.32754 0.00000  0.00000  0.00000  145 LEU   G N   
3702  C CA  . LEU   C  145 ? 0.25697 0.25697 0.25697 0.00000  0.00000  0.00000  145 LEU   G CA  
3703  C C   . LEU   C  145 ? 0.51231 0.51231 0.51231 0.00000  0.00000  0.00000  145 LEU   G C   
3704  O O   . LEU   C  145 ? 0.48986 0.48986 0.48986 -0.00000 0.00000  0.00000  145 LEU   G O   
3705  C CB  . LEU   C  145 ? 0.39421 0.39421 0.39421 0.00000  0.00000  0.00000  145 LEU   G CB  
3706  C CG  . LEU   C  145 ? 0.42779 0.42779 0.42779 0.00000  0.00000  0.00000  145 LEU   G CG  
3707  C CD1 . LEU   C  145 ? 0.34801 0.34801 0.34801 0.00000  0.00000  0.00000  145 LEU   G CD1 
3708  C CD2 . LEU   C  145 ? 0.34016 0.34016 0.34016 0.00000  0.00000  0.00000  145 LEU   G CD2 
3709  N N   . PHE   C  146 ? 0.27366 0.27366 0.27366 0.00000  0.00000  0.00000  146 PHE   G N   
3710  C CA  . PHE   C  146 ? 0.32374 0.32374 0.32374 -0.00000 0.00000  0.00000  146 PHE   G CA  
3711  C C   . PHE   C  146 ? 0.42809 0.42809 0.42809 0.00000  0.00000  0.00000  146 PHE   G C   
3712  O O   . PHE   C  146 ? 0.43708 0.43708 0.43708 -0.00000 -0.00000 0.00000  146 PHE   G O   
3713  C CB  . PHE   C  146 ? 0.32663 0.32663 0.32663 0.00000  0.00000  0.00000  146 PHE   G CB  
3714  C CG  . PHE   C  146 ? 0.37189 0.37189 0.37189 0.00000  0.00000  0.00000  146 PHE   G CG  
3715  C CD1 . PHE   C  146 ? 0.37244 0.37244 0.37244 -0.00000 0.00000  0.00000  146 PHE   G CD1 
3716  C CD2 . PHE   C  146 ? 0.28461 0.28461 0.28461 -0.00000 0.00000  0.00000  146 PHE   G CD2 
3717  C CE1 . PHE   C  146 ? 0.37390 0.37390 0.37390 0.00000  0.00000  0.00000  146 PHE   G CE1 
3718  C CE2 . PHE   C  146 ? 0.32999 0.32999 0.32999 -0.00000 0.00000  0.00000  146 PHE   G CE2 
3719  C CZ  . PHE   C  146 ? 0.40165 0.40165 0.40165 -0.00000 -0.00000 0.00000  146 PHE   G CZ  
3720  N N   . ASP   C  147 ? 0.37836 0.37836 0.37836 0.00000  0.00000  -0.00000 147 ASP   G N   
3721  C CA  . ASP   C  147 ? 0.29766 0.29766 0.29766 -0.00000 0.00000  0.00000  147 ASP   G CA  
3722  C C   . ASP   C  147 ? 0.41879 0.41879 0.41879 0.00000  0.00000  0.00000  147 ASP   G C   
3723  O O   . ASP   C  147 ? 0.39744 0.39744 0.39744 0.00000  0.00000  0.00000  147 ASP   G O   
3724  C CB  . ASP   C  147 ? 0.20199 0.20199 0.20199 -0.00000 -0.00000 0.00000  147 ASP   G CB  
3725  C CG  . ASP   C  147 ? 0.62093 0.62093 0.62093 0.00000  0.00000  0.00000  147 ASP   G CG  
3726  O OD1 . ASP   C  147 ? 0.52108 0.52108 0.52108 0.00000  0.00000  -0.00000 147 ASP   G OD1 
3727  O OD2 . ASP   C  147 ? 0.57402 0.57402 0.57402 0.00000  0.00000  0.00000  147 ASP   G OD2 
3728  N N   . THR   C  148 ? 0.34537 0.34537 0.34537 0.00000  0.00000  -0.00000 148 THR   G N   
3729  C CA  . THR   C  148 ? 0.46504 0.46504 0.46504 0.00000  -0.00000 -0.00000 148 THR   G CA  
3730  C C   . THR   C  148 ? 0.42585 0.42585 0.42585 -0.00000 0.00000  0.00000  148 THR   G C   
3731  O O   . THR   C  148 ? 0.50204 0.50204 0.50204 -0.00000 0.00000  0.00000  148 THR   G O   
3732  C CB  . THR   C  148 ? 0.39995 0.39995 0.39995 0.00000  0.00000  0.00000  148 THR   G CB  
3733  O OG1 . THR   C  148 ? 0.41094 0.41094 0.41094 0.00000  0.00000  0.00000  148 THR   G OG1 
3734  C CG2 . THR   C  148 ? 0.26448 0.26448 0.26448 0.00000  0.00000  0.00000  148 THR   G CG2 
3735  N N   . TRP   C  149 ? 0.38999 0.38999 0.38999 -0.00000 0.00000  0.00000  149 TRP   G N   
3736  C CA  . TRP   C  149 ? 0.30267 0.30267 0.30267 0.00000  0.00000  0.00000  149 TRP   G CA  
3737  C C   . TRP   C  149 ? 0.60697 0.60697 0.60697 0.00000  0.00000  0.00000  149 TRP   G C   
3738  O O   . TRP   C  149 ? 0.41470 0.41470 0.41470 0.00000  0.00000  0.00000  149 TRP   G O   
3739  C CB  . TRP   C  149 ? 0.27191 0.27191 0.27191 0.00000  0.00000  0.00000  149 TRP   G CB  
3740  C CG  . TRP   C  149 ? 0.41154 0.41154 0.41154 -0.00000 0.00000  0.00000  149 TRP   G CG  
3741  C CD1 . TRP   C  149 ? 0.33963 0.33963 0.33963 -0.00000 0.00000  0.00000  149 TRP   G CD1 
3742  C CD2 . TRP   C  149 ? 0.54248 0.54248 0.54248 0.00000  0.00000  0.00000  149 TRP   G CD2 
3743  N NE1 . TRP   C  149 ? 0.49429 0.49429 0.49429 -0.00000 0.00000  0.00000  149 TRP   G NE1 
3744  C CE2 . TRP   C  149 ? 0.32051 0.32051 0.32051 0.00000  0.00000  0.00000  149 TRP   G CE2 
3745  C CE3 . TRP   C  149 ? 0.30933 0.30933 0.30933 -0.00000 0.00000  0.00000  149 TRP   G CE3 
3746  C CZ2 . TRP   C  149 ? 0.44014 0.44014 0.44014 -0.00000 0.00000  0.00000  149 TRP   G CZ2 
3747  C CZ3 . TRP   C  149 ? 0.34558 0.34558 0.34558 0.00000  0.00000  0.00000  149 TRP   G CZ3 
3748  C CH2 . TRP   C  149 ? 0.43699 0.43699 0.43699 0.00000  0.00000  0.00000  149 TRP   G CH2 
3749  N N   . GLY   C  150 ? 0.40005 0.40005 0.40005 -0.00000 0.00000  0.00000  150 GLY   G N   
3750  C CA  . GLY   C  150 ? 0.26526 0.26526 0.26526 0.00000  0.00000  0.00000  150 GLY   G CA  
3751  C C   . GLY   C  150 ? 0.53493 0.53493 0.53493 -0.00000 0.00000  0.00000  150 GLY   G C   
3752  O O   . GLY   C  150 ? 0.68759 0.68759 0.68759 0.00000  0.00000  0.00000  150 GLY   G O   
3753  N N   . LEU   C  151 ? 0.54063 0.54063 0.54063 0.00000  0.00000  0.00000  151 LEU   G N   
3754  C CA  . LEU   C  151 ? 0.47374 0.47374 0.47374 0.00000  0.00000  0.00000  151 LEU   G CA  
3755  C C   . LEU   C  151 ? 0.97326 0.97326 0.97326 -0.00000 0.00000  0.00000  151 LEU   G C   
3756  O O   . LEU   C  151 ? 0.63203 0.63203 0.63203 -0.00000 0.00000  0.00000  151 LEU   G O   
3757  C CB  . LEU   C  151 ? 0.62820 0.62820 0.62820 -0.00000 0.00000  0.00000  151 LEU   G CB  
3758  C CG  . LEU   C  151 ? 0.89539 0.89539 0.89539 0.00000  0.00000  0.00000  151 LEU   G CG  
3759  C CD1 . LEU   C  151 ? 0.45430 0.45430 0.45430 0.00000  0.00000  0.00000  151 LEU   G CD1 
3760  C CD2 . LEU   C  151 ? 0.30895 0.30895 0.30895 0.00000  0.00000  0.00000  151 LEU   G CD2 
3761  N N   . PHE   C  152 ? 0.30022 0.30022 0.30022 0.00000  0.00000  0.00000  152 PHE   G N   
3762  C CA  . PHE   C  152 ? 0.46170 0.46170 0.46170 -0.00000 0.00000  0.00000  152 PHE   G CA  
3763  C C   . PHE   C  152 ? 0.62931 0.62931 0.62931 0.00000  0.00000  0.00000  152 PHE   G C   
3764  O O   . PHE   C  152 ? 0.53375 0.53375 0.53375 0.00000  0.00000  0.00000  152 PHE   G O   
3765  C CB  . PHE   C  152 ? 0.23707 0.23707 0.23707 0.00000  0.00000  0.00000  152 PHE   G CB  
3766  C CG  . PHE   C  152 ? 0.56962 0.56962 0.56962 -0.00000 0.00000  0.00000  152 PHE   G CG  
3767  C CD1 . PHE   C  152 ? 0.35369 0.35369 0.35369 0.00000  0.00000  0.00000  152 PHE   G CD1 
3768  C CD2 . PHE   C  152 ? 0.45333 0.45333 0.45333 -0.00000 0.00000  0.00000  152 PHE   G CD2 
3769  C CE1 . PHE   C  152 ? 0.44228 0.44228 0.44228 0.00000  0.00000  0.00000  152 PHE   G CE1 
3770  C CE2 . PHE   C  152 ? 0.57465 0.57465 0.57465 0.00000  0.00000  0.00000  152 PHE   G CE2 
3771  C CZ  . PHE   C  152 ? 0.47014 0.47014 0.47014 0.00000  0.00000  0.00000  152 PHE   G CZ  
3772  N N   . LEU   C  153 ? 0.38186 0.38186 0.38186 0.00000  0.00000  0.00000  153 LEU   G N   
3773  C CA  . LEU   C  153 ? 0.40601 0.40601 0.40601 0.00000  0.00000  0.00000  153 LEU   G CA  
3774  C C   . LEU   C  153 ? 0.40076 0.40076 0.40076 -0.00000 0.00000  0.00000  153 LEU   G C   
3775  O O   . LEU   C  153 ? 0.45642 0.45642 0.45642 0.00000  0.00000  0.00000  153 LEU   G O   
3776  C CB  . LEU   C  153 ? 0.31381 0.31381 0.31381 0.00000  -0.00000 0.00000  153 LEU   G CB  
3777  C CG  . LEU   C  153 ? 0.47932 0.47932 0.47932 0.00000  0.00000  0.00000  153 LEU   G CG  
3778  C CD1 . LEU   C  153 ? 0.25360 0.25360 0.25360 0.00000  0.00000  0.00000  153 LEU   G CD1 
3779  C CD2 . LEU   C  153 ? 0.25381 0.25381 0.25381 -0.00000 0.00000  0.00000  153 LEU   G CD2 
3780  N N   . SER   C  154 ? 0.53124 0.53124 0.53124 0.00000  0.00000  -0.00000 154 SER   G N   
3781  C CA  . SER   C  154 ? 0.50276 0.50276 0.50276 0.00000  0.00000  0.00000  154 SER   G CA  
3782  C C   . SER   C  154 ? 0.63045 0.63045 0.63045 -0.00000 0.00000  0.00000  154 SER   G C   
3783  O O   . SER   C  154 ? 0.68417 0.68417 0.68417 0.00000  0.00000  0.00000  154 SER   G O   
3784  C CB  . SER   C  154 ? 0.34060 0.34060 0.34060 -0.00000 0.00000  0.00000  154 SER   G CB  
3785  O OG  . SER   C  154 ? 1.36185 1.36185 1.36185 -0.00000 0.00000  0.00000  154 SER   G OG  
3786  N N   . SER   C  155 ? 0.36286 0.36286 0.36286 0.00000  0.00000  0.00000  155 SER   G N   
3787  C CA  . SER   C  155 ? 0.37076 0.37076 0.37076 0.00000  0.00000  0.00000  155 SER   G CA  
3788  C C   . SER   C  155 ? 1.18898 1.18898 1.18898 0.00000  0.00000  0.00000  155 SER   G C   
3789  O O   . SER   C  155 ? 0.34656 0.34656 0.34656 0.00000  0.00000  -0.00000 155 SER   G O   
3790  C CB  . SER   C  155 ? 0.32963 0.32963 0.32963 -0.00000 0.00000  0.00000  155 SER   G CB  
3791  O OG  . SER   C  155 ? 0.45691 0.45691 0.45691 0.00000  0.00000  0.00000  155 SER   G OG  
3792  N N   . LYS   C  156 ? 0.45661 0.45661 0.45661 0.00000  0.00000  0.00000  156 LYS   G N   
3793  C CA  . LYS   C  156 ? 0.66962 0.66962 0.66962 -0.00000 0.00000  0.00000  156 LYS   G CA  
3794  C C   . LYS   C  156 ? 0.33299 0.33299 0.33299 0.00000  0.00000  0.00000  156 LYS   G C   
3795  O O   . LYS   C  156 ? 0.53366 0.53366 0.53366 0.00000  0.00000  0.00000  156 LYS   G O   
3796  C CB  . LYS   C  156 ? 0.24073 0.24073 0.24073 -0.00000 -0.00000 0.00000  156 LYS   G CB  
3797  N N   . ASP   C  157 ? 0.53261 0.53261 0.53261 0.00000  0.00000  0.00000  157 ASP   G N   
3798  C CA  . ASP   C  157 ? 0.51959 0.51959 0.51959 -0.00000 0.00000  0.00000  157 ASP   G CA  
3799  C C   . ASP   C  157 ? 0.55150 0.55150 0.55150 0.00000  0.00000  0.00000  157 ASP   G C   
3800  O O   . ASP   C  157 ? 0.49939 0.49939 0.49939 -0.00000 0.00000  0.00000  157 ASP   G O   
3801  C CB  . ASP   C  157 ? 0.66336 0.66336 0.66336 -0.00000 0.00000  0.00000  157 ASP   G CB  
3802  C CG  . ASP   C  157 ? 0.67651 0.67651 0.67651 0.00000  0.00000  0.00000  157 ASP   G CG  
3803  O OD1 . ASP   C  157 ? 0.81077 0.81077 0.81077 0.00000  0.00000  0.00000  157 ASP   G OD1 
3804  O OD2 . ASP   C  157 ? 1.04765 1.04765 1.04765 0.00000  0.00000  0.00000  157 ASP   G OD2 
3805  N N   . SER   C  158 ? 0.72384 0.72384 0.72384 0.00000  0.00000  0.00000  158 SER   G N   
3806  C CA  . SER   C  158 ? 0.53930 0.53930 0.53930 -0.00000 0.00000  0.00000  158 SER   G CA  
3807  C C   . SER   C  158 ? 0.57533 0.57533 0.57533 0.00000  0.00000  0.00000  158 SER   G C   
3808  O O   . SER   C  158 ? 0.51275 0.51275 0.51275 -0.00000 0.00000  0.00000  158 SER   G O   
3809  C CB  . SER   C  158 ? 0.45643 0.45643 0.45643 0.00000  0.00000  0.00000  158 SER   G CB  
3810  O OG  . SER   C  158 ? 0.44958 0.44958 0.44958 0.00000  0.00000  0.00000  158 SER   G OG  
3811  N N   . ARG   C  159 ? 0.38085 0.38085 0.38085 0.00000  0.00000  0.00000  159 ARG   G N   
3812  C CA  . ARG   C  159 ? 0.47224 0.47224 0.47224 0.00000  -0.00000 0.00000  159 ARG   G CA  
3813  C C   . ARG   C  159 ? 0.48182 0.48182 0.48182 0.00000  0.00000  0.00000  159 ARG   G C   
3814  O O   . ARG   C  159 ? 0.41112 0.41112 0.41112 -0.00000 0.00000  0.00000  159 ARG   G O   
3815  C CB  . ARG   C  159 ? 0.25228 0.25228 0.25228 0.00000  0.00000  0.00000  159 ARG   G CB  
3816  C CG  . ARG   C  159 ? 0.70784 0.70784 0.70784 -0.00000 0.00000  0.00000  159 ARG   G CG  
3817  C CD  . ARG   C  159 ? 0.50625 0.50625 0.50625 -0.00000 0.00000  0.00000  159 ARG   G CD  
3818  N NE  . ARG   C  159 ? 0.68182 0.68182 0.68182 0.00000  0.00000  0.00000  159 ARG   G NE  
3819  C CZ  . ARG   C  159 ? 0.56996 0.56996 0.56996 -0.00000 0.00000  0.00000  159 ARG   G CZ  
3820  N NH1 . ARG   C  159 ? 0.47461 0.47461 0.47461 0.00000  0.00000  0.00000  159 ARG   G NH1 
3821  N NH2 . ARG   C  159 ? 0.43941 0.43941 0.43941 0.00000  0.00000  0.00000  159 ARG   G NH2 
3822  N N   . ASN   C  160 ? 0.42653 0.42653 0.42653 -0.00000 0.00000  0.00000  160 ASN   G N   
3823  C CA  . ASN   C  160 ? 0.48157 0.48157 0.48157 0.00000  0.00000  0.00000  160 ASN   G CA  
3824  C C   . ASN   C  160 ? 0.38566 0.38566 0.38566 0.00000  0.00000  0.00000  160 ASN   G C   
3825  O O   . ASN   C  160 ? 0.76273 0.76273 0.76273 0.00000  0.00000  0.00000  160 ASN   G O   
3826  C CB  . ASN   C  160 ? 0.45687 0.45687 0.45687 0.00000  0.00000  0.00000  160 ASN   G CB  
3827  C CG  . ASN   C  160 ? 0.61106 0.61106 0.61106 -0.00000 0.00000  0.00000  160 ASN   G CG  
3828  O OD1 . ASN   C  160 ? 0.78148 0.78148 0.78148 -0.00000 0.00000  -0.00000 160 ASN   G OD1 
3829  N ND2 . ASN   C  160 ? 0.66417 0.66417 0.66417 0.00000  0.00000  0.00000  160 ASN   G ND2 
3830  N N   . VAL   C  161 ? 0.54335 0.54335 0.54335 0.00000  0.00000  0.00000  161 VAL   G N   
3831  C CA  . VAL   C  161 ? 0.57888 0.57888 0.57888 0.00000  -0.00000 0.00000  161 VAL   G CA  
3832  C C   . VAL   C  161 ? 0.61307 0.61307 0.61307 0.00000  0.00000  0.00000  161 VAL   G C   
3833  O O   . VAL   C  161 ? 0.39402 0.39402 0.39402 0.00000  0.00000  0.00000  161 VAL   G O   
3834  C CB  . VAL   C  161 ? 0.50221 0.50221 0.50221 0.00000  0.00000  0.00000  161 VAL   G CB  
3835  C CG1 . VAL   C  161 ? 0.36119 0.36119 0.36119 0.00000  0.00000  0.00000  161 VAL   G CG1 
3836  C CG2 . VAL   C  161 ? 0.29649 0.29649 0.29649 0.00000  0.00000  0.00000  161 VAL   G CG2 
3837  N N   . LEU   C  162 ? 0.39973 0.39973 0.39973 0.00000  0.00000  0.00000  162 LEU   G N   
3838  C CA  . LEU   C  162 ? 0.53202 0.53202 0.53202 0.00000  0.00000  0.00000  162 LEU   G CA  
3839  C C   . LEU   C  162 ? 0.77178 0.77178 0.77178 -0.00000 0.00000  0.00000  162 LEU   G C   
3840  O O   . LEU   C  162 ? 0.55136 0.55136 0.55136 0.00000  -0.00000 0.00000  162 LEU   G O   
3841  C CB  . LEU   C  162 ? 0.48968 0.48968 0.48968 -0.00000 0.00000  0.00000  162 LEU   G CB  
3842  C CG  . LEU   C  162 ? 0.34580 0.34580 0.34580 -0.00000 0.00000  0.00000  162 LEU   G CG  
3843  C CD1 . LEU   C  162 ? 0.29126 0.29126 0.29126 0.00000  0.00000  0.00000  162 LEU   G CD1 
3844  C CD2 . LEU   C  162 ? 0.27661 0.27661 0.27661 0.00000  -0.00000 0.00000  162 LEU   G CD2 
3845  N N   . VAL   C  163 ? 0.41054 0.41054 0.41054 -0.00000 0.00000  0.00000  163 VAL   G N   
3846  C CA  . VAL   C  163 ? 0.37311 0.37311 0.37311 0.00000  0.00000  0.00000  163 VAL   G CA  
3847  C C   . VAL   C  163 ? 0.63180 0.63180 0.63180 -0.00000 -0.00000 0.00000  163 VAL   G C   
3848  O O   . VAL   C  163 ? 0.53786 0.53786 0.53786 -0.00000 0.00000  0.00000  163 VAL   G O   
3849  C CB  . VAL   C  163 ? 0.39794 0.39794 0.39794 0.00000  0.00000  0.00000  163 VAL   G CB  
3850  C CG1 . VAL   C  163 ? 0.31669 0.31669 0.31669 0.00000  0.00000  0.00000  163 VAL   G CG1 
3851  C CG2 . VAL   C  163 ? 0.31072 0.31072 0.31072 0.00000  0.00000  0.00000  163 VAL   G CG2 
3852  N N   . ALA   C  164 ? 0.53114 0.53114 0.53114 0.00000  -0.00000 0.00000  164 ALA   G N   
3853  C CA  . ALA   C  164 ? 0.62747 0.62747 0.62747 0.00000  0.00000  0.00000  164 ALA   G CA  
3854  C C   . ALA   C  164 ? 0.51349 0.51349 0.51349 0.00000  0.00000  0.00000  164 ALA   G C   
3855  O O   . ALA   C  164 ? 0.48708 0.48708 0.48708 0.00000  0.00000  0.00000  164 ALA   G O   
3856  C CB  . ALA   C  164 ? 0.25836 0.25836 0.25836 -0.00000 -0.00000 0.00000  164 ALA   G CB  
3857  N N   . ASP   C  165 ? 0.53287 0.53287 0.53287 0.00000  0.00000  0.00000  165 ASP   G N   
3858  C CA  . ASP   C  165 ? 0.51177 0.51177 0.51177 0.00000  0.00000  0.00000  165 ASP   G CA  
3859  C C   . ASP   C  165 ? 0.51000 0.51000 0.51000 0.00000  0.00000  0.00000  165 ASP   G C   
3860  O O   . ASP   C  165 ? 0.95356 0.95356 0.95356 0.00000  0.00000  0.00000  165 ASP   G O   
3861  C CB  . ASP   C  165 ? 0.60392 0.60392 0.60392 0.00000  0.00000  0.00000  165 ASP   G CB  
3862  C CG  . ASP   C  165 ? 0.45135 0.45135 0.45135 0.00000  0.00000  0.00000  165 ASP   G CG  
3863  O OD1 . ASP   C  165 ? 1.03712 1.03712 1.03712 -0.00000 0.00000  0.00000  165 ASP   G OD1 
3864  O OD2 . ASP   C  165 ? 1.07129 1.07129 1.07129 0.00000  0.00000  0.00000  165 ASP   G OD2 
3865  N N   . GLN   C  166 ? 0.89314 0.89314 0.89314 0.00000  0.00000  0.00000  166 GLN   G N   
3866  C CA  . GLN   C  166 ? 1.07638 1.07638 1.07638 -0.00000 0.00000  0.00000  166 GLN   G CA  
3867  C C   . GLN   C  166 ? 0.59839 0.59839 0.59839 0.00000  0.00000  0.00000  166 GLN   G C   
3868  O O   . GLN   C  166 ? 1.53056 1.53056 1.53056 0.00000  0.00000  0.00000  166 GLN   G O   
3869  C CB  . GLN   C  166 ? 0.56453 0.56453 0.56453 -0.00000 0.00000  0.00000  166 GLN   G CB  
3870  C CG  . GLN   C  166 ? 1.02701 1.02701 1.02701 -0.00000 0.00000  0.00000  166 GLN   G CG  
3871  C CD  . GLN   C  166 ? 1.77956 1.77956 1.77956 0.00000  0.00000  0.00000  166 GLN   G CD  
3872  O OE1 . GLN   C  166 ? 1.20666 1.20666 1.20666 -0.00000 0.00000  0.00000  166 GLN   G OE1 
3873  N NE2 . GLN   C  166 ? 1.03446 1.03446 1.03446 0.00000  0.00000  0.00000  166 GLN   G NE2 
3874  N N   . PHE   C  167 ? 1.17178 1.17178 1.17178 0.00000  0.00000  0.00000  167 PHE   G N   
3875  C CA  . PHE   C  167 ? 1.15858 1.15858 1.15858 0.00000  0.00000  0.00000  167 PHE   G CA  
3876  C C   . PHE   C  167 ? 1.17763 1.17763 1.17763 -0.00000 0.00000  0.00000  167 PHE   G C   
3877  O O   . PHE   C  167 ? 1.12671 1.12671 1.12671 0.00000  0.00000  0.00000  167 PHE   G O   
3878  C CB  . PHE   C  167 ? 1.03322 1.03322 1.03322 0.00000  0.00000  0.00000  167 PHE   G CB  
3879  C CG  . PHE   C  167 ? 1.10283 1.10283 1.10283 0.00000  0.00000  0.00000  167 PHE   G CG  
3880  C CD1 . PHE   C  167 ? 0.95356 0.95356 0.95356 0.00000  0.00000  0.00000  167 PHE   G CD1 
3881  C CD2 . PHE   C  167 ? 0.84094 0.84094 0.84094 -0.00000 0.00000  0.00000  167 PHE   G CD2 
3882  C CE1 . PHE   C  167 ? 1.84928 1.84928 1.84928 0.00000  0.00000  0.00000  167 PHE   G CE1 
3883  C CE2 . PHE   C  167 ? 1.70770 1.70770 1.70770 0.00000  0.00000  0.00000  167 PHE   G CE2 
3884  C CZ  . PHE   C  167 ? 0.68538 0.68538 0.68538 -0.00000 0.00000  0.00000  167 PHE   G CZ  
3885  N N   . ASP   C  168 ? 1.42933 1.42933 1.42933 0.00000  0.00000  0.00000  168 ASP   G N   
3886  C CA  . ASP   C  168 ? 0.98952 0.98952 0.98952 0.00000  0.00000  0.00000  168 ASP   G CA  
3887  C C   . ASP   C  168 ? 1.63937 1.63937 1.63937 -0.00000 0.00000  0.00000  168 ASP   G C   
3888  O O   . ASP   C  168 ? 1.30405 1.30405 1.30405 0.00000  0.00000  0.00000  168 ASP   G O   
3889  C CB  . ASP   C  168 ? 1.16783 1.16783 1.16783 0.00000  0.00000  0.00000  168 ASP   G CB  
3890  C CG  . ASP   C  168 ? 1.48177 1.48177 1.48177 -0.00000 0.00000  0.00000  168 ASP   G CG  
3891  O OD1 . ASP   C  168 ? 1.30232 1.30232 1.30232 0.00000  0.00000  0.00000  168 ASP   G OD1 
3892  O OD2 . ASP   C  168 ? 1.45335 1.45335 1.45335 -0.00000 0.00000  0.00000  168 ASP   G OD2 
3893  N N   . ASP   C  169 ? 1.33038 1.33038 1.33038 -0.00000 0.00000  0.00000  169 ASP   G N   
3894  C CA  . ASP   C  169 ? 1.37967 1.37967 1.37967 0.00000  0.00000  0.00000  169 ASP   G CA  
3895  C C   . ASP   C  169 ? 1.59305 1.59305 1.59305 -0.00000 0.00000  0.00000  169 ASP   G C   
3896  O O   . ASP   C  169 ? 1.43890 1.43890 1.43890 0.00000  0.00000  0.00000  169 ASP   G O   
3897  C CB  . ASP   C  169 ? 1.10842 1.10842 1.10842 0.00000  0.00000  0.00000  169 ASP   G CB  
3898  N N   . ARG   C  170 ? 1.92416 1.92416 1.92416 0.00000  0.00000  -0.00000 170 ARG   G N   
3899  C CA  . ARG   C  170 ? 0.79570 0.79570 0.79570 -0.00000 0.00000  0.00000  170 ARG   G CA  
3900  C C   . ARG   C  170 ? 1.02727 1.02727 1.02727 0.00000  0.00000  0.00000  170 ARG   G C   
3901  O O   . ARG   C  170 ? 0.91349 0.91349 0.91349 0.00000  0.00000  0.00000  170 ARG   G O   
3902  C CB  . ARG   C  170 ? 0.86983 0.86983 0.86983 0.00000  0.00000  0.00000  170 ARG   G CB  
3903  N N   . HIS   C  171 ? 0.84839 0.84839 0.84839 -0.00000 0.00000  0.00000  171 HIS   G N   
3904  C CA  . HIS   C  171 ? 0.88930 0.88930 0.88930 -0.00000 0.00000  0.00000  171 HIS   G CA  
3905  C C   . HIS   C  171 ? 0.46568 0.46568 0.46568 0.00000  0.00000  0.00000  171 HIS   G C   
3906  O O   . HIS   C  171 ? 1.36844 1.36844 1.36844 0.00000  0.00000  -0.00000 171 HIS   G O   
3907  C CB  . HIS   C  171 ? 0.92437 0.92437 0.92437 0.00000  0.00000  0.00000  171 HIS   G CB  
3908  C CG  . HIS   C  171 ? 0.86337 0.86337 0.86337 -0.00000 0.00000  0.00000  171 HIS   G CG  
3909  N ND1 . HIS   C  171 ? 0.93510 0.93510 0.93510 0.00000  0.00000  -0.00000 171 HIS   G ND1 
3910  C CD2 . HIS   C  171 ? 0.86625 0.86625 0.86625 0.00000  0.00000  -0.00000 171 HIS   G CD2 
3911  C CE1 . HIS   C  171 ? 0.61536 0.61536 0.61536 -0.00000 0.00000  0.00000  171 HIS   G CE1 
3912  N NE2 . HIS   C  171 ? 1.56858 1.56858 1.56858 0.00000  0.00000  0.00000  171 HIS   G NE2 
3913  N N   . CYS   C  172 ? 0.90748 0.90748 0.90748 -0.00000 0.00000  0.00000  172 CYS   G N   
3914  C CA  . CYS   C  172 ? 0.51899 0.51899 0.51899 0.00000  0.00000  0.00000  172 CYS   G CA  
3915  C C   . CYS   C  172 ? 0.53240 0.53240 0.53240 -0.00000 0.00000  0.00000  172 CYS   G C   
3916  O O   . CYS   C  172 ? 0.82280 0.82280 0.82280 0.00000  0.00000  0.00000  172 CYS   G O   
3917  C CB  . CYS   C  172 ? 0.63444 0.63444 0.63444 0.00000  0.00000  0.00000  172 CYS   G CB  
3918  S SG  . CYS   C  172 ? 0.73543 0.73543 0.73543 0.00000  0.00000  0.00000  172 CYS   G SG  
3919  N N   . GLY   C  173 ? 0.72196 0.72196 0.72196 0.00000  0.00000  0.00000  173 GLY   G N   
3920  C CA  . GLY   C  173 ? 0.52758 0.52758 0.52758 -0.00000 0.00000  0.00000  173 GLY   G CA  
3921  C C   . GLY   C  173 ? 0.71209 0.71209 0.71209 0.00000  0.00000  0.00000  173 GLY   G C   
3922  O O   . GLY   C  173 ? 0.71279 0.71279 0.71279 0.00000  0.00000  0.00000  173 GLY   G O   
3923  N N   . TRP   C  174 ? 0.37605 0.37605 0.37605 -0.00000 0.00000  0.00000  174 TRP   G N   
3924  C CA  . TRP   C  174 ? 0.69999 0.69999 0.69999 0.00000  0.00000  0.00000  174 TRP   G CA  
3925  C C   . TRP   C  174 ? 0.80870 0.80870 0.80870 0.00000  0.00000  0.00000  174 TRP   G C   
3926  O O   . TRP   C  174 ? 0.60835 0.60835 0.60835 0.00000  0.00000  0.00000  174 TRP   G O   
3927  C CB  . TRP   C  174 ? 0.41825 0.41825 0.41825 0.00000  0.00000  0.00000  174 TRP   G CB  
3928  C CG  . TRP   C  174 ? 0.79884 0.79884 0.79884 0.00000  0.00000  0.00000  174 TRP   G CG  
3929  C CD1 . TRP   C  174 ? 0.51959 0.51959 0.51959 0.00000  0.00000  0.00000  174 TRP   G CD1 
3930  C CD2 . TRP   C  174 ? 0.62993 0.62993 0.62993 -0.00000 0.00000  0.00000  174 TRP   G CD2 
3931  N NE1 . TRP   C  174 ? 0.55101 0.55101 0.55101 0.00000  0.00000  0.00000  174 TRP   G NE1 
3932  C CE2 . TRP   C  174 ? 0.45044 0.45044 0.45044 0.00000  0.00000  0.00000  174 TRP   G CE2 
3933  C CE3 . TRP   C  174 ? 0.47852 0.47852 0.47852 0.00000  0.00000  0.00000  174 TRP   G CE3 
3934  C CZ2 . TRP   C  174 ? 0.35433 0.35433 0.35433 0.00000  0.00000  0.00000  174 TRP   G CZ2 
3935  C CZ3 . TRP   C  174 ? 0.50430 0.50430 0.50430 0.00000  0.00000  0.00000  174 TRP   G CZ3 
3936  C CH2 . TRP   C  174 ? 0.39225 0.39225 0.39225 0.00000  0.00000  0.00000  174 TRP   G CH2 
3937  N N   . LEU   C  175 ? 0.52637 0.52637 0.52637 0.00000  0.00000  0.00000  175 LEU   G N   
3938  C CA  . LEU   C  175 ? 0.46245 0.46245 0.46245 -0.00000 0.00000  0.00000  175 LEU   G CA  
3939  C C   . LEU   C  175 ? 0.58527 0.58527 0.58527 0.00000  0.00000  0.00000  175 LEU   G C   
3940  O O   . LEU   C  175 ? 0.69734 0.69734 0.69734 0.00000  0.00000  0.00000  175 LEU   G O   
3941  C CB  . LEU   C  175 ? 0.39909 0.39909 0.39909 0.00000  0.00000  0.00000  175 LEU   G CB  
3942  C CG  . LEU   C  175 ? 0.53348 0.53348 0.53348 0.00000  0.00000  0.00000  175 LEU   G CG  
3943  C CD1 . LEU   C  175 ? 0.41375 0.41375 0.41375 0.00000  0.00000  0.00000  175 LEU   G CD1 
3944  C CD2 . LEU   C  175 ? 0.37506 0.37506 0.37506 -0.00000 0.00000  0.00000  175 LEU   G CD2 
3945  N N   . ASN   C  176 ? 0.43813 0.43813 0.43813 0.00000  0.00000  0.00000  176 ASN   G N   
3946  C CA  . ASN   C  176 ? 0.38227 0.38227 0.38227 -0.00000 0.00000  0.00000  176 ASN   G CA  
3947  C C   . ASN   C  176 ? 0.59009 0.59009 0.59009 -0.00000 0.00000  0.00000  176 ASN   G C   
3948  O O   . ASN   C  176 ? 0.76595 0.76595 0.76595 0.00000  0.00000  0.00000  176 ASN   G O   
3949  C CB  . ASN   C  176 ? 0.72325 0.72325 0.72325 0.00000  0.00000  0.00000  176 ASN   G CB  
3950  C CG  . ASN   C  176 ? 0.70186 0.70186 0.70186 0.00000  0.00000  0.00000  176 ASN   G CG  
3951  O OD1 . ASN   C  176 ? 0.52692 0.52692 0.52692 0.00000  0.00000  0.00000  176 ASN   G OD1 
3952  N ND2 . ASN   C  176 ? 0.54390 0.54390 0.54390 -0.00000 0.00000  0.00000  176 ASN   G ND2 
3953  N N   . GLU   C  177 ? 0.59534 0.59534 0.59534 0.00000  0.00000  0.00000  177 GLU   G N   
3954  C CA  . GLU   C  177 ? 0.56113 0.56113 0.56113 0.00000  0.00000  0.00000  177 GLU   G CA  
3955  C C   . GLU   C  177 ? 0.48223 0.48223 0.48223 0.00000  0.00000  0.00000  177 GLU   G C   
3956  O O   . GLU   C  177 ? 0.59934 0.59934 0.59934 0.00000  0.00000  0.00000  177 GLU   G O   
3957  C CB  . GLU   C  177 ? 0.33001 0.33001 0.33001 0.00000  0.00000  0.00000  177 GLU   G CB  
3958  N N   . ARG   C  178 ? 0.52403 0.52403 0.52403 0.00000  0.00000  0.00000  178 ARG   G N   
3959  C CA  . ARG   C  178 ? 0.82245 0.82245 0.82245 0.00000  0.00000  0.00000  178 ARG   G CA  
3960  C C   . ARG   C  178 ? 0.77402 0.77402 0.77402 -0.00000 0.00000  0.00000  178 ARG   G C   
3961  O O   . ARG   C  178 ? 0.75451 0.75451 0.75451 0.00000  0.00000  0.00000  178 ARG   G O   
3962  C CB  . ARG   C  178 ? 0.38150 0.38150 0.38150 -0.00000 0.00000  0.00000  178 ARG   G CB  
3963  C CG  . ARG   C  178 ? 0.84884 0.84884 0.84884 0.00000  -0.00000 0.00000  178 ARG   G CG  
3964  C CD  . ARG   C  178 ? 0.61856 0.61856 0.61856 0.00000  0.00000  0.00000  178 ARG   G CD  
3965  N NE  . ARG   C  178 ? 1.22121 1.22121 1.22121 0.00000  0.00000  0.00000  178 ARG   G NE  
3966  C CZ  . ARG   C  178 ? 1.47513 1.47513 1.47513 -0.00000 0.00000  0.00000  178 ARG   G CZ  
3967  N NH1 . ARG   C  178 ? 0.91293 0.91293 0.91293 0.00000  0.00000  -0.00000 178 ARG   G NH1 
3968  N NH2 . ARG   C  178 ? 1.31017 1.31017 1.31017 0.00000  0.00000  0.00000  178 ARG   G NH2 
3969  N N   . ALA   C  179 ? 0.65019 0.65019 0.65019 0.00000  0.00000  0.00000  179 ALA   G N   
3970  C CA  . ALA   C  179 ? 0.63329 0.63329 0.63329 0.00000  0.00000  0.00000  179 ALA   G CA  
3971  C C   . ALA   C  179 ? 0.49163 0.49163 0.49163 -0.00000 0.00000  0.00000  179 ALA   G C   
3972  O O   . ALA   C  179 ? 0.58846 0.58846 0.58846 0.00000  0.00000  0.00000  179 ALA   G O   
3973  C CB  . ALA   C  179 ? 0.32729 0.32729 0.32729 0.00000  0.00000  0.00000  179 ALA   G CB  
3974  N N   . LEU   C  180 ? 0.50745 0.50745 0.50745 0.00000  0.00000  0.00000  180 LEU   G N   
3975  C CA  . LEU   C  180 ? 0.34224 0.34224 0.34224 0.00000  0.00000  0.00000  180 LEU   G CA  
3976  C C   . LEU   C  180 ? 0.54967 0.54967 0.54967 0.00000  0.00000  0.00000  180 LEU   G C   
3977  O O   . LEU   C  180 ? 0.55119 0.55119 0.55119 0.00000  0.00000  0.00000  180 LEU   G O   
3978  C CB  . LEU   C  180 ? 0.28315 0.28315 0.28315 -0.00000 0.00000  0.00000  180 LEU   G CB  
3979  C CG  . LEU   C  180 ? 0.59746 0.59746 0.59746 0.00000  0.00000  0.00000  180 LEU   G CG  
3980  C CD1 . LEU   C  180 ? 0.56746 0.56746 0.56746 -0.00000 0.00000  0.00000  180 LEU   G CD1 
3981  C CD2 . LEU   C  180 ? 0.44136 0.44136 0.44136 -0.00000 0.00000  0.00000  180 LEU   G CD2 
3982  N N   . SER   C  181 ? 0.57016 0.57016 0.57016 0.00000  0.00000  0.00000  181 SER   G N   
3983  C CA  . SER   C  181 ? 0.61970 0.61970 0.61970 -0.00000 0.00000  0.00000  181 SER   G CA  
3984  C C   . SER   C  181 ? 0.46390 0.46390 0.46390 0.00000  -0.00000 0.00000  181 SER   G C   
3985  O O   . SER   C  181 ? 0.60719 0.60719 0.60719 -0.00000 0.00000  0.00000  181 SER   G O   
3986  C CB  . SER   C  181 ? 0.39654 0.39654 0.39654 0.00000  -0.00000 -0.00000 181 SER   G CB  
3987  O OG  . SER   C  181 ? 1.26056 1.26056 1.26056 0.00000  0.00000  0.00000  181 SER   G OG  
3988  N N   . ALA   C  182 ? 0.65163 0.65163 0.65163 0.00000  0.00000  0.00000  182 ALA   G N   
3989  C CA  . ALA   C  182 ? 0.92607 0.92607 0.92607 -0.00000 0.00000  0.00000  182 ALA   G CA  
3990  C C   . ALA   C  182 ? 0.66655 0.66655 0.66655 0.00000  0.00000  0.00000  182 ALA   G C   
3991  O O   . ALA   C  182 ? 0.51237 0.51237 0.51237 -0.00000 0.00000  0.00000  182 ALA   G O   
3992  C CB  . ALA   C  182 ? 0.40078 0.40078 0.40078 0.00000  0.00000  0.00000  182 ALA   G CB  
3993  N N   . MET   C  183 ? 0.31188 0.31188 0.31188 0.00000  0.00000  0.00000  183 MET   G N   
3994  C CA  . MET   C  183 ? 0.51613 0.51613 0.51613 0.00000  0.00000  0.00000  183 MET   G CA  
3995  C C   . MET   C  183 ? 0.33046 0.33046 0.33046 0.00000  0.00000  0.00000  183 MET   G C   
3996  O O   . MET   C  183 ? 0.56597 0.56597 0.56597 0.00000  0.00000  0.00000  183 MET   G O   
3997  C CB  . MET   C  183 ? 0.32184 0.32184 0.32184 0.00000  0.00000  0.00000  183 MET   G CB  
3998  C CG  . MET   C  183 ? 0.34846 0.34846 0.34846 0.00000  0.00000  0.00000  183 MET   G CG  
3999  S SD  . MET   C  183 ? 0.46511 0.46511 0.46511 0.00000  0.00000  0.00000  183 MET   G SD  
4000  C CE  . MET   C  183 ? 0.41766 0.41766 0.41766 0.00000  0.00000  0.00000  183 MET   G CE  
4001  N N   . VAL   C  184 ? 0.44366 0.44366 0.44366 0.00000  0.00000  0.00000  184 VAL   G N   
4002  C CA  . VAL   C  184 ? 0.53052 0.53052 0.53052 -0.00000 0.00000  0.00000  184 VAL   G CA  
4003  C C   . VAL   C  184 ? 0.29677 0.29677 0.29677 0.00000  0.00000  0.00000  184 VAL   G C   
4004  O O   . VAL   C  184 ? 0.43512 0.43512 0.43512 0.00000  -0.00000 0.00000  184 VAL   G O   
4005  C CB  . VAL   C  184 ? 0.26978 0.26978 0.26978 0.00000  0.00000  0.00000  184 VAL   G CB  
4006  C CG1 . VAL   C  184 ? 0.33958 0.33958 0.33958 -0.00000 0.00000  0.00000  184 VAL   G CG1 
4007  C CG2 . VAL   C  184 ? 0.28384 0.28384 0.28384 0.00000  0.00000  0.00000  184 VAL   G CG2 
4008  N N   . LYS   C  185 ? 0.55794 0.55794 0.55794 0.00000  0.00000  0.00000  185 LYS   G N   
4009  C CA  . LYS   C  185 ? 0.59436 0.59436 0.59436 0.00000  0.00000  0.00000  185 LYS   G CA  
4010  C C   . LYS   C  185 ? 0.28687 0.28687 0.28687 -0.00000 0.00000  0.00000  185 LYS   G C   
4011  O O   . LYS   C  185 ? 1.02687 1.02687 1.02687 -0.00000 0.00000  0.00000  185 LYS   G O   
4012  C CB  . LYS   C  185 ? 0.45022 0.45022 0.45022 0.00000  0.00000  0.00000  185 LYS   G CB  
4013  C CG  . LYS   C  185 ? 0.52880 0.52880 0.52880 0.00000  0.00000  0.00000  185 LYS   G CG  
4014  C CD  . LYS   C  185 ? 0.85096 0.85096 0.85096 0.00000  0.00000  0.00000  185 LYS   G CD  
4015  C CE  . LYS   C  185 ? 0.85912 0.85912 0.85912 0.00000  0.00000  0.00000  185 LYS   G CE  
4016  N NZ  . LYS   C  185 ? 1.03295 1.03295 1.03295 0.00000  0.00000  0.00000  185 LYS   G NZ  
4017  N N   . HIS   C  186 ? 0.57487 0.57487 0.57487 -0.00000 0.00000  0.00000  186 HIS   G N   
4018  C CA  . HIS   C  186 ? 0.34803 0.34803 0.34803 0.00000  0.00000  -0.00000 186 HIS   G CA  
4019  C C   . HIS   C  186 ? 0.59169 0.59169 0.59169 0.00000  0.00000  0.00000  186 HIS   G C   
4020  O O   . HIS   C  186 ? 0.41632 0.41632 0.41632 0.00000  0.00000  0.00000  186 HIS   G O   
4021  C CB  . HIS   C  186 ? 0.45500 0.45500 0.45500 0.00000  0.00000  0.00000  186 HIS   G CB  
4022  C CG  . HIS   C  186 ? 0.78485 0.78485 0.78485 0.00000  0.00000  0.00000  186 HIS   G CG  
4023  N ND1 . HIS   C  186 ? 0.61992 0.61992 0.61992 0.00000  0.00000  -0.00000 186 HIS   G ND1 
4024  C CD2 . HIS   C  186 ? 0.27366 0.27366 0.27366 0.00000  0.00000  0.00000  186 HIS   G CD2 
4025  C CE1 . HIS   C  186 ? 0.46514 0.46514 0.46514 -0.00000 0.00000  0.00000  186 HIS   G CE1 
4026  N NE2 . HIS   C  186 ? 0.66849 0.66849 0.66849 0.00000  0.00000  0.00000  186 HIS   G NE2 
4027  N N   . TYR   C  187 ? 0.40948 0.40948 0.40948 0.00000  0.00000  0.00000  187 TYR   G N   
4028  C CA  . TYR   C  187 ? 0.51029 0.51029 0.51029 -0.00000 0.00000  0.00000  187 TYR   G CA  
4029  C C   . TYR   C  187 ? 0.96481 0.96481 0.96481 0.00000  0.00000  0.00000  187 TYR   G C   
4030  O O   . TYR   C  187 ? 0.42719 0.42719 0.42719 0.00000  0.00000  0.00000  187 TYR   G O   
4031  C CB  . TYR   C  187 ? 0.56742 0.56742 0.56742 -0.00000 0.00000  0.00000  187 TYR   G CB  
4032  C CG  . TYR   C  187 ? 0.36487 0.36487 0.36487 0.00000  -0.00000 0.00000  187 TYR   G CG  
4033  C CD1 . TYR   C  187 ? 0.47157 0.47157 0.47157 0.00000  0.00000  0.00000  187 TYR   G CD1 
4034  C CD2 . TYR   C  187 ? 0.55138 0.55138 0.55138 -0.00000 0.00000  0.00000  187 TYR   G CD2 
4035  C CE1 . TYR   C  187 ? 0.41981 0.41981 0.41981 0.00000  0.00000  0.00000  187 TYR   G CE1 
4036  C CE2 . TYR   C  187 ? 0.19875 0.19875 0.19875 0.00000  0.00000  0.00000  187 TYR   G CE2 
4037  C CZ  . TYR   C  187 ? 0.54552 0.54552 0.54552 -0.00000 -0.00000 0.00000  187 TYR   G CZ  
4038  O OH  . TYR   C  187 ? 0.46183 0.46183 0.46183 0.00000  0.00000  0.00000  187 TYR   G OH  
4039  N N   . ASN   C  188 ? 0.41702 0.41702 0.41702 -0.00000 0.00000  0.00000  188 ASN   G N   
4040  C CA  . ASN   C  188 ? 1.04659 1.04659 1.04659 -0.00000 0.00000  0.00000  188 ASN   G CA  
4041  C C   . ASN   C  188 ? 0.40396 0.40396 0.40396 0.00000  0.00000  0.00000  188 ASN   G C   
4042  O O   . ASN   C  188 ? 0.82803 0.82803 0.82803 0.00000  0.00000  0.00000  188 ASN   G O   
4043  C CB  . ASN   C  188 ? 0.54937 0.54937 0.54937 0.00000  0.00000  0.00000  188 ASN   G CB  
4044  C CG  . ASN   C  188 ? 1.04720 1.04720 1.04720 0.00000  0.00000  0.00000  188 ASN   G CG  
4045  O OD1 . ASN   C  188 ? 1.39992 1.39992 1.39992 -0.00000 0.00000  0.00000  188 ASN   G OD1 
4046  N ND2 . ASN   C  188 ? 1.20983 1.20983 1.20983 0.00000  0.00000  0.00000  188 ASN   G ND2 
4047  N N   . GLY   C  189 ? 0.64855 0.64855 0.64855 -0.00000 0.00000  0.00000  189 GLY   G N   
4048  C CA  . GLY   C  189 ? 0.22954 0.22954 0.22954 0.00000  0.00000  0.00000  189 GLY   G CA  
4049  C C   . GLY   C  189 ? 0.28230 0.28230 0.28230 -0.00000 0.00000  0.00000  189 GLY   G C   
4050  O O   . GLY   C  189 ? 0.69893 0.69893 0.69893 0.00000  0.00000  0.00000  189 GLY   G O   
4051  N N   . ARG   C  190 ? 0.54281 0.54281 0.54281 0.00000  0.00000  0.00000  190 ARG   G N   
4052  C CA  . ARG   C  190 ? 0.39288 0.39288 0.39288 0.00000  0.00000  0.00000  190 ARG   G CA  
4053  C C   . ARG   C  190 ? 0.48299 0.48299 0.48299 0.00000  0.00000  0.00000  190 ARG   G C   
4054  O O   . ARG   C  190 ? 0.61834 0.61834 0.61834 0.00000  0.00000  0.00000  190 ARG   G O   
4055  C CB  . ARG   C  190 ? 0.48419 0.48419 0.48419 0.00000  0.00000  0.00000  190 ARG   G CB  
4056  C CG  . ARG   C  190 ? 0.41651 0.41651 0.41651 0.00000  0.00000  0.00000  190 ARG   G CG  
4057  C CD  . ARG   C  190 ? 0.29627 0.29627 0.29627 0.00000  0.00000  0.00000  190 ARG   G CD  
4058  N NE  . ARG   C  190 ? 0.48189 0.48189 0.48189 0.00000  -0.00000 -0.00000 190 ARG   G NE  
4059  C CZ  . ARG   C  190 ? 0.69695 0.69695 0.69695 0.00000  0.00000  0.00000  190 ARG   G CZ  
4060  N NH1 . ARG   C  190 ? 0.64954 0.64954 0.64954 0.00000  0.00000  0.00000  190 ARG   G NH1 
4061  N NH2 . ARG   C  190 ? 0.51526 0.51526 0.51526 0.00000  0.00000  0.00000  190 ARG   G NH2 
4062  N N   . ALA   C  191 ? 0.50578 0.50578 0.50578 0.00000  0.00000  0.00000  191 ALA   G N   
4063  C CA  . ALA   C  191 ? 0.35120 0.35120 0.35120 0.00000  0.00000  0.00000  191 ALA   G CA  
4064  C C   . ALA   C  191 ? 1.14958 1.14958 1.14958 -0.00000 0.00000  0.00000  191 ALA   G C   
4065  O O   . ALA   C  191 ? 0.36710 0.36710 0.36710 0.00000  0.00000  0.00000  191 ALA   G O   
4066  C CB  . ALA   C  191 ? 0.50720 0.50720 0.50720 0.00000  0.00000  0.00000  191 ALA   G CB  
4067  N N   . PHE   C  192 ? 0.34799 0.34799 0.34799 0.00000  0.00000  0.00000  192 PHE   G N   
4068  C CA  . PHE   C  192 ? 0.39704 0.39704 0.39704 0.00000  0.00000  0.00000  192 PHE   G CA  
4069  C C   . PHE   C  192 ? 0.69905 0.69905 0.69905 0.00000  0.00000  0.00000  192 PHE   G C   
4070  O O   . PHE   C  192 ? 0.56721 0.56721 0.56721 0.00000  0.00000  0.00000  192 PHE   G O   
4071  C CB  . PHE   C  192 ? 0.41652 0.41652 0.41652 0.00000  0.00000  0.00000  192 PHE   G CB  
4072  C CG  . PHE   C  192 ? 0.51101 0.51101 0.51101 0.00000  -0.00000 -0.00000 192 PHE   G CG  
4073  C CD1 . PHE   C  192 ? 0.62685 0.62685 0.62685 -0.00000 0.00000  0.00000  192 PHE   G CD1 
4074  C CD2 . PHE   C  192 ? 0.61353 0.61353 0.61353 0.00000  0.00000  0.00000  192 PHE   G CD2 
4075  C CE1 . PHE   C  192 ? 0.38105 0.38105 0.38105 0.00000  0.00000  0.00000  192 PHE   G CE1 
4076  C CE2 . PHE   C  192 ? 0.69082 0.69082 0.69082 0.00000  -0.00000 0.00000  192 PHE   G CE2 
4077  C CZ  . PHE   C  192 ? 0.48113 0.48113 0.48113 0.00000  0.00000  0.00000  192 PHE   G CZ  
4078  N N   . ASP   C  193 ? 0.63024 0.63024 0.63024 -0.00000 0.00000  0.00000  193 ASP   G N   
4079  C CA  . ASP   C  193 ? 0.37817 0.37817 0.37817 0.00000  0.00000  0.00000  193 ASP   G CA  
4080  C C   . ASP   C  193 ? 0.71371 0.71371 0.71371 0.00000  0.00000  0.00000  193 ASP   G C   
4081  O O   . ASP   C  193 ? 0.21833 0.21833 0.21833 0.00000  0.00000  0.00000  193 ASP   G O   
4082  C CB  . ASP   C  193 ? 0.54143 0.54143 0.54143 -0.00000 0.00000  0.00000  193 ASP   G CB  
4083  C CG  . ASP   C  193 ? 1.08452 1.08452 1.08452 -0.00000 0.00000  0.00000  193 ASP   G CG  
4084  O OD1 . ASP   C  193 ? 0.58699 0.58699 0.58699 0.00000  0.00000  0.00000  193 ASP   G OD1 
4085  O OD2 . ASP   C  193 ? 0.56797 0.56797 0.56797 -0.00000 -0.00000 -0.00000 193 ASP   G OD2 
4086  N N   . GLU   C  194 ? 0.34039 0.34039 0.34039 0.00000  0.00000  0.00000  194 GLU   G N   
4087  C CA  . GLU   C  194 ? 0.68198 0.68198 0.68198 0.00000  0.00000  0.00000  194 GLU   G CA  
4088  C C   . GLU   C  194 ? 0.73742 0.73742 0.73742 -0.00000 0.00000  0.00000  194 GLU   G C   
4089  O O   . GLU   C  194 ? 0.59169 0.59169 0.59169 0.00000  0.00000  0.00000  194 GLU   G O   
4090  C CB  . GLU   C  194 ? 0.57766 0.57766 0.57766 0.00000  0.00000  0.00000  194 GLU   G CB  
4091  C CG  . GLU   C  194 ? 0.39752 0.39752 0.39752 -0.00000 0.00000  0.00000  194 GLU   G CG  
4092  C CD  . GLU   C  194 ? 1.12670 1.12670 1.12670 -0.00000 0.00000  0.00000  194 GLU   G CD  
4093  O OE1 . GLU   C  194 ? 0.80514 0.80514 0.80514 -0.00000 0.00000  0.00000  194 GLU   G OE1 
4094  O OE2 . GLU   C  194 ? 0.77415 0.77415 0.77415 0.00000  0.00000  0.00000  194 GLU   G OE2 
4095  N N   . VAL   C  195 ? 0.67361 0.67361 0.67361 -0.00000 0.00000  0.00000  195 VAL   G N   
4096  C CA  . VAL   C  195 ? 0.26579 0.26579 0.26579 0.00000  0.00000  0.00000  195 VAL   G CA  
4097  C C   . VAL   C  195 ? 1.04376 1.04376 1.04376 -0.00000 -0.00000 0.00000  195 VAL   G C   
4098  O O   . VAL   C  195 ? 0.43317 0.43317 0.43317 -0.00000 0.00000  0.00000  195 VAL   G O   
4099  C CB  . VAL   C  195 ? 0.71205 0.71205 0.71205 0.00000  0.00000  0.00000  195 VAL   G CB  
4100  C CG1 . VAL   C  195 ? 0.32793 0.32793 0.32793 0.00000  0.00000  0.00000  195 VAL   G CG1 
4101  C CG2 . VAL   C  195 ? 0.39122 0.39122 0.39122 0.00000  0.00000  0.00000  195 VAL   G CG2 
4102  N N   . PHE   C  196 ? 0.29791 0.29791 0.29791 -0.00000 0.00000  0.00000  196 PHE   G N   
4103  C CA  . PHE   C  196 ? 0.70219 0.70219 0.70219 0.00000  0.00000  0.00000  196 PHE   G CA  
4104  C C   . PHE   C  196 ? 0.45515 0.45515 0.45515 0.00000  0.00000  0.00000  196 PHE   G C   
4105  O O   . PHE   C  196 ? 0.48378 0.48378 0.48378 -0.00000 0.00000  0.00000  196 PHE   G O   
4106  C CB  . PHE   C  196 ? 0.35696 0.35696 0.35696 0.00000  0.00000  0.00000  196 PHE   G CB  
4107  C CG  . PHE   C  196 ? 0.57804 0.57804 0.57804 -0.00000 0.00000  0.00000  196 PHE   G CG  
4108  C CD1 . PHE   C  196 ? 0.37166 0.37166 0.37166 -0.00000 0.00000  0.00000  196 PHE   G CD1 
4109  C CD2 . PHE   C  196 ? 0.28824 0.28824 0.28824 0.00000  0.00000  0.00000  196 PHE   G CD2 
4110  C CE1 . PHE   C  196 ? 0.42252 0.42252 0.42252 -0.00000 0.00000  0.00000  196 PHE   G CE1 
4111  C CE2 . PHE   C  196 ? 0.51855 0.51855 0.51855 0.00000  0.00000  0.00000  196 PHE   G CE2 
4112  C CZ  . PHE   C  196 ? 0.40949 0.40949 0.40949 0.00000  0.00000  0.00000  196 PHE   G CZ  
4113  N N   . LEU   C  197 ? 0.48683 0.48683 0.48683 -0.00000 0.00000  0.00000  197 LEU   G N   
4114  C CA  . LEU   C  197 ? 0.52263 0.52263 0.52263 -0.00000 0.00000  0.00000  197 LEU   G CA  
4115  C C   . LEU   C  197 ? 0.75813 0.75813 0.75813 0.00000  0.00000  0.00000  197 LEU   G C   
4116  O O   . LEU   C  197 ? 0.44655 0.44655 0.44655 -0.00000 0.00000  0.00000  197 LEU   G O   
4117  C CB  . LEU   C  197 ? 0.49139 0.49139 0.49139 0.00000  0.00000  0.00000  197 LEU   G CB  
4118  C CG  . LEU   C  197 ? 0.44954 0.44954 0.44954 -0.00000 0.00000  0.00000  197 LEU   G CG  
4119  C CD1 . LEU   C  197 ? 0.55397 0.55397 0.55397 0.00000  0.00000  0.00000  197 LEU   G CD1 
4120  C CD2 . LEU   C  197 ? 1.04735 1.04735 1.04735 0.00000  0.00000  0.00000  197 LEU   G CD2 
4121  N N   . CYS   C  198 ? 0.51107 0.51107 0.51107 0.00000  0.00000  0.00000  198 CYS   G N   
4122  C CA  . CYS   C  198 ? 0.50061 0.50061 0.50061 -0.00000 0.00000  0.00000  198 CYS   G CA  
4123  C C   . CYS   C  198 ? 0.54660 0.54660 0.54660 -0.00000 0.00000  0.00000  198 CYS   G C   
4124  O O   . CYS   C  198 ? 0.63648 0.63648 0.63648 -0.00000 0.00000  0.00000  198 CYS   G O   
4125  C CB  . CYS   C  198 ? 0.41771 0.41771 0.41771 0.00000  0.00000  0.00000  198 CYS   G CB  
4126  S SG  . CYS   C  198 ? 0.52835 0.52835 0.52835 0.00000  0.00000  0.00000  198 CYS   G SG  
4127  N N   . ASP   C  199 ? 0.49702 0.49702 0.49702 0.00000  0.00000  0.00000  199 ASP   G N   
4128  C CA  . ASP   C  199 ? 0.35104 0.35104 0.35104 -0.00000 0.00000  0.00000  199 ASP   G CA  
4129  C C   . ASP   C  199 ? 0.78946 0.78946 0.78946 0.00000  0.00000  0.00000  199 ASP   G C   
4130  O O   . ASP   C  199 ? 0.34795 0.34795 0.34795 0.00000  0.00000  0.00000  199 ASP   G O   
4131  C CB  . ASP   C  199 ? 0.37390 0.37390 0.37390 0.00000  0.00000  0.00000  199 ASP   G CB  
4132  C CG  . ASP   C  199 ? 1.65750 1.65750 1.65750 0.00000  0.00000  -0.00000 199 ASP   G CG  
4133  O OD1 . ASP   C  199 ? 0.40982 0.40982 0.40982 -0.00000 0.00000  0.00000  199 ASP   G OD1 
4134  O OD2 . ASP   C  199 ? 0.50735 0.50735 0.50735 0.00000  0.00000  0.00000  199 ASP   G OD2 
4135  N N   . LYS   C  200 ? 0.45991 0.45991 0.45991 0.00000  -0.00000 0.00000  200 LYS   G N   
4136  C CA  . LYS   C  200 ? 0.78238 0.78238 0.78238 0.00000  0.00000  0.00000  200 LYS   G CA  
4137  C C   . LYS   C  200 ? 0.74114 0.74114 0.74114 0.00000  0.00000  0.00000  200 LYS   G C   
4138  O O   . LYS   C  200 ? 0.63624 0.63624 0.63624 -0.00000 0.00000  0.00000  200 LYS   G O   
4139  C CB  . LYS   C  200 ? 0.45758 0.45758 0.45758 0.00000  0.00000  0.00000  200 LYS   G CB  
4140  C CG  . LYS   C  200 ? 0.74621 0.74621 0.74621 0.00000  0.00000  0.00000  200 LYS   G CG  
4141  C CD  . LYS   C  200 ? 1.00597 1.00597 1.00597 0.00000  0.00000  0.00000  200 LYS   G CD  
4142  C CE  . LYS   C  200 ? 0.79419 0.79419 0.79419 0.00000  0.00000  0.00000  200 LYS   G CE  
4143  N NZ  . LYS   C  200 ? 0.72554 0.72554 0.72554 0.00000  0.00000  0.00000  200 LYS   G NZ  
4144  N N   . ASN   C  201 ? 0.61502 0.61502 0.61502 0.00000  0.00000  0.00000  201 ASN   G N   
4145  C CA  . ASN   C  201 ? 0.90837 0.90837 0.90837 0.00000  0.00000  0.00000  201 ASN   G CA  
4146  C C   . ASN   C  201 ? 0.60118 0.60118 0.60118 0.00000  0.00000  0.00000  201 ASN   G C   
4147  O O   . ASN   C  201 ? 1.00698 1.00698 1.00698 0.00000  0.00000  -0.00000 201 ASN   G O   
4148  C CB  . ASN   C  201 ? 0.57905 0.57905 0.57905 0.00000  0.00000  0.00000  201 ASN   G CB  
4149  C CG  . ASN   C  201 ? 1.05353 1.05353 1.05353 0.00000  0.00000  0.00000  201 ASN   G CG  
4150  O OD1 . ASN   C  201 ? 0.46122 0.46122 0.46122 -0.00000 0.00000  0.00000  201 ASN   G OD1 
4151  N ND2 . ASN   C  201 ? 0.64970 0.64970 0.64970 0.00000  0.00000  0.00000  201 ASN   G ND2 
4152  N N   . ALA   C  202 ? 1.18515 1.18515 1.18515 0.00000  0.00000  -0.00000 202 ALA   G N   
4153  C CA  . ALA   C  202 ? 0.58350 0.58350 0.58350 0.00000  -0.00000 0.00000  202 ALA   G CA  
4154  C C   . ALA   C  202 ? 0.49777 0.49777 0.49777 0.00000  0.00000  0.00000  202 ALA   G C   
4155  O O   . ALA   C  202 ? 0.64664 0.64664 0.64664 0.00000  0.00000  0.00000  202 ALA   G O   
4156  C CB  . ALA   C  202 ? 0.29687 0.29687 0.29687 0.00000  0.00000  0.00000  202 ALA   G CB  
4157  N N   . PRO   C  203 ? 0.94763 0.94763 0.94763 0.00000  0.00000  0.00000  203 PRO   G N   
4158  C CA  . PRO   C  203 ? 0.88203 0.88203 0.88203 0.00000  0.00000  0.00000  203 PRO   G CA  
4159  C C   . PRO   C  203 ? 0.75316 0.75316 0.75316 0.00000  0.00000  -0.00000 203 PRO   G C   
4160  O O   . PRO   C  203 ? 0.50311 0.50311 0.50311 0.00000  0.00000  0.00000  203 PRO   G O   
4161  C CB  . PRO   C  203 ? 0.59431 0.59431 0.59431 -0.00000 0.00000  0.00000  203 PRO   G CB  
4162  C CG  . PRO   C  203 ? 0.47663 0.47663 0.47663 0.00000  0.00000  0.00000  203 PRO   G CG  
4163  C CD  . PRO   C  203 ? 0.32634 0.32634 0.32634 0.00000  0.00000  0.00000  203 PRO   G CD  
4164  N N   . TYR   C  204 ? 0.46335 0.46335 0.46335 0.00000  0.00000  0.00000  204 TYR   G N   
4165  C CA  . TYR   C  204 ? 0.60355 0.60355 0.60355 0.00000  0.00000  0.00000  204 TYR   G CA  
4166  C C   . TYR   C  204 ? 0.52387 0.52387 0.52387 -0.00000 0.00000  0.00000  204 TYR   G C   
4167  O O   . TYR   C  204 ? 0.57901 0.57901 0.57901 0.00000  0.00000  0.00000  204 TYR   G O   
4168  C CB  . TYR   C  204 ? 0.44405 0.44405 0.44405 0.00000  0.00000  0.00000  204 TYR   G CB  
4169  C CG  . TYR   C  204 ? 0.49820 0.49820 0.49820 -0.00000 -0.00000 0.00000  204 TYR   G CG  
4170  C CD1 . TYR   C  204 ? 0.43185 0.43185 0.43185 -0.00000 -0.00000 0.00000  204 TYR   G CD1 
4171  C CD2 . TYR   C  204 ? 0.38357 0.38357 0.38357 0.00000  0.00000  0.00000  204 TYR   G CD2 
4172  C CE1 . TYR   C  204 ? 0.21294 0.21294 0.21294 0.00000  0.00000  0.00000  204 TYR   G CE1 
4173  C CE2 . TYR   C  204 ? 0.34611 0.34611 0.34611 -0.00000 0.00000  0.00000  204 TYR   G CE2 
4174  C CZ  . TYR   C  204 ? 0.51346 0.51346 0.51346 -0.00000 0.00000  0.00000  204 TYR   G CZ  
4175  O OH  . TYR   C  204 ? 0.53892 0.53892 0.53892 0.00000  0.00000  0.00000  204 TYR   G OH  
4176  N N   . TYR   C  205 ? 0.37734 0.37734 0.37734 0.00000  0.00000  0.00000  205 TYR   G N   
4177  C CA  . TYR   C  205 ? 0.35150 0.35150 0.35150 0.00000  0.00000  0.00000  205 TYR   G CA  
4178  C C   . TYR   C  205 ? 0.44552 0.44552 0.44552 -0.00000 0.00000  0.00000  205 TYR   G C   
4179  O O   . TYR   C  205 ? 0.41998 0.41998 0.41998 0.00000  0.00000  0.00000  205 TYR   G O   
4180  C CB  . TYR   C  205 ? 0.44166 0.44166 0.44166 0.00000  0.00000  0.00000  205 TYR   G CB  
4181  C CG  . TYR   C  205 ? 0.61526 0.61526 0.61526 0.00000  0.00000  0.00000  205 TYR   G CG  
4182  C CD1 . TYR   C  205 ? 0.51712 0.51712 0.51712 0.00000  -0.00000 0.00000  205 TYR   G CD1 
4183  C CD2 . TYR   C  205 ? 0.45699 0.45699 0.45699 0.00000  0.00000  -0.00000 205 TYR   G CD2 
4184  C CE1 . TYR   C  205 ? 0.32559 0.32559 0.32559 0.00000  0.00000  0.00000  205 TYR   G CE1 
4185  C CE2 . TYR   C  205 ? 0.62956 0.62956 0.62956 -0.00000 0.00000  0.00000  205 TYR   G CE2 
4186  C CZ  . TYR   C  205 ? 0.88152 0.88152 0.88152 -0.00000 0.00000  0.00000  205 TYR   G CZ  
4187  O OH  . TYR   C  205 ? 0.50901 0.50901 0.50901 0.00000  0.00000  0.00000  205 TYR   G OH  
4188  N N   . GLY   C  206 ? 0.31973 0.31973 0.31973 0.00000  0.00000  0.00000  206 GLY   G N   
4189  C CA  . GLY   C  206 ? 0.30564 0.30564 0.30564 0.00000  -0.00000 0.00000  206 GLY   G CA  
4190  C C   . GLY   C  206 ? 0.48028 0.48028 0.48028 0.00000  0.00000  0.00000  206 GLY   G C   
4191  O O   . GLY   C  206 ? 0.37916 0.37916 0.37916 -0.00000 0.00000  0.00000  206 GLY   G O   
4192  N N   . PHE   C  207 ? 0.33738 0.33738 0.33738 0.00000  0.00000  0.00000  207 PHE   G N   
4193  C CA  . PHE   C  207 ? 0.49012 0.49012 0.49012 0.00000  0.00000  0.00000  207 PHE   G CA  
4194  C C   . PHE   C  207 ? 0.43267 0.43267 0.43267 0.00000  0.00000  0.00000  207 PHE   G C   
4195  O O   . PHE   C  207 ? 0.55985 0.55985 0.55985 0.00000  0.00000  0.00000  207 PHE   G O   
4196  C CB  . PHE   C  207 ? 0.32972 0.32972 0.32972 -0.00000 0.00000  0.00000  207 PHE   G CB  
4197  C CG  . PHE   C  207 ? 0.52791 0.52791 0.52791 0.00000  0.00000  0.00000  207 PHE   G CG  
4198  C CD1 . PHE   C  207 ? 0.19580 0.19580 0.19580 0.00000  0.00000  0.00000  207 PHE   G CD1 
4199  C CD2 . PHE   C  207 ? 0.25122 0.25122 0.25122 -0.00000 0.00000  0.00000  207 PHE   G CD2 
4200  C CE1 . PHE   C  207 ? 0.45298 0.45298 0.45298 0.00000  0.00000  0.00000  207 PHE   G CE1 
4201  C CE2 . PHE   C  207 ? 0.29752 0.29752 0.29752 0.00000  0.00000  0.00000  207 PHE   G CE2 
4202  C CZ  . PHE   C  207 ? 0.51228 0.51228 0.51228 -0.00000 0.00000  0.00000  207 PHE   G CZ  
4203  N N   . ASN   C  208 ? 0.49459 0.49459 0.49459 0.00000  0.00000  0.00000  208 ASN   G N   
4204  C CA  . ASN   C  208 ? 0.77972 0.77972 0.77972 -0.00000 0.00000  0.00000  208 ASN   G CA  
4205  C C   . ASN   C  208 ? 0.39501 0.39501 0.39501 0.00000  0.00000  0.00000  208 ASN   G C   
4206  O O   . ASN   C  208 ? 1.13180 1.13180 1.13180 0.00000  0.00000  0.00000  208 ASN   G O   
4207  C CB  . ASN   C  208 ? 0.40071 0.40071 0.40071 0.00000  0.00000  0.00000  208 ASN   G CB  
4208  C CG  . ASN   C  208 ? 1.11590 1.11590 1.11590 0.00000  0.00000  0.00000  208 ASN   G CG  
4209  O OD1 . ASN   C  208 ? 1.81311 1.81311 1.81311 -0.00000 0.00000  0.00000  208 ASN   G OD1 
4210  N ND2 . ASN   C  208 ? 0.82429 0.82429 0.82429 0.00000  0.00000  0.00000  208 ASN   G ND2 
4211  N N   . SER   C  209 ? 0.63596 0.63596 0.63596 0.00000  0.00000  0.00000  209 SER   G N   
4212  C CA  . SER   C  209 ? 0.42653 0.42653 0.42653 0.00000  0.00000  -0.00000 209 SER   G CA  
4213  C C   . SER   C  209 ? 0.70703 0.70703 0.70703 0.00000  0.00000  0.00000  209 SER   G C   
4214  O O   . SER   C  209 ? 0.39335 0.39335 0.39335 0.00000  0.00000  0.00000  209 SER   G O   
4215  C CB  . SER   C  209 ? 0.56575 0.56575 0.56575 -0.00000 0.00000  0.00000  209 SER   G CB  
4216  O OG  . SER   C  209 ? 0.30388 0.30388 0.30388 0.00000  -0.00000 0.00000  209 SER   G OG  
4217  N N   . TYR   C  210 ? 0.42992 0.42992 0.42992 0.00000  0.00000  0.00000  210 TYR   G N   
4218  C CA  . TYR   C  210 ? 0.27937 0.27937 0.27937 0.00000  0.00000  0.00000  210 TYR   G CA  
4219  C C   . TYR   C  210 ? 0.44412 0.44412 0.44412 0.00000  0.00000  0.00000  210 TYR   G C   
4220  O O   . TYR   C  210 ? 0.35479 0.35479 0.35479 0.00000  0.00000  0.00000  210 TYR   G O   
4221  C CB  . TYR   C  210 ? 0.14518 0.14518 0.14518 0.00000  0.00000  0.00000  210 TYR   G CB  
4222  C CG  . TYR   C  210 ? 0.56406 0.56406 0.56406 0.00000  0.00000  0.00000  210 TYR   G CG  
4223  C CD1 . TYR   C  210 ? 0.27305 0.27305 0.27305 0.00000  0.00000  0.00000  210 TYR   G CD1 
4224  C CD2 . TYR   C  210 ? 0.46826 0.46826 0.46826 0.00000  0.00000  0.00000  210 TYR   G CD2 
4225  C CE1 . TYR   C  210 ? 0.31893 0.31893 0.31893 0.00000  0.00000  0.00000  210 TYR   G CE1 
4226  C CE2 . TYR   C  210 ? 0.49067 0.49067 0.49067 0.00000  0.00000  0.00000  210 TYR   G CE2 
4227  C CZ  . TYR   C  210 ? 0.60460 0.60460 0.60460 -0.00000 0.00000  0.00000  210 TYR   G CZ  
4228  O OH  . TYR   C  210 ? 0.37379 0.37379 0.37379 0.00000  0.00000  0.00000  210 TYR   G OH  
4229  N N   . ASP   C  211 ? 0.40581 0.40581 0.40581 -0.00000 0.00000  0.00000  211 ASP   G N   
4230  C CA  . ASP   C  211 ? 0.33898 0.33898 0.33898 -0.00000 0.00000  0.00000  211 ASP   G CA  
4231  C C   . ASP   C  211 ? 0.60988 0.60988 0.60988 -0.00000 0.00000  0.00000  211 ASP   G C   
4232  O O   . ASP   C  211 ? 0.36775 0.36775 0.36775 0.00000  0.00000  0.00000  211 ASP   G O   
4233  C CB  . ASP   C  211 ? 0.37875 0.37875 0.37875 0.00000  0.00000  0.00000  211 ASP   G CB  
4234  C CG  . ASP   C  211 ? 0.38563 0.38563 0.38563 0.00000  0.00000  0.00000  211 ASP   G CG  
4235  O OD1 . ASP   C  211 ? 0.44581 0.44581 0.44581 0.00000  0.00000  0.00000  211 ASP   G OD1 
4236  O OD2 . ASP   C  211 ? 0.67270 0.67270 0.67270 -0.00000 0.00000  -0.00000 211 ASP   G OD2 
4237  N N   . ASP   C  212 ? 0.39442 0.39442 0.39442 0.00000  0.00000  0.00000  212 ASP   G N   
4238  C CA  . ASP   C  212 ? 0.51497 0.51497 0.51497 0.00000  0.00000  0.00000  212 ASP   G CA  
4239  C C   . ASP   C  212 ? 0.41699 0.41699 0.41699 -0.00000 0.00000  0.00000  212 ASP   G C   
4240  O O   . ASP   C  212 ? 0.42569 0.42569 0.42569 -0.00000 0.00000  0.00000  212 ASP   G O   
4241  C CB  . ASP   C  212 ? 0.53369 0.53369 0.53369 0.00000  0.00000  0.00000  212 ASP   G CB  
4242  C CG  . ASP   C  212 ? 0.63654 0.63654 0.63654 0.00000  -0.00000 0.00000  212 ASP   G CG  
4243  O OD1 . ASP   C  212 ? 0.82652 0.82652 0.82652 0.00000  0.00000  -0.00000 212 ASP   G OD1 
4244  O OD2 . ASP   C  212 ? 0.64759 0.64759 0.64759 0.00000  0.00000  0.00000  212 ASP   G OD2 
4245  N N   . PHE   C  213 ? 0.23294 0.23294 0.23294 -0.00000 0.00000  0.00000  213 PHE   G N   
4246  C CA  . PHE   C  213 ? 0.19837 0.19837 0.19837 -0.00000 0.00000  -0.00000 213 PHE   G CA  
4247  C C   . PHE   C  213 ? 0.66582 0.66582 0.66582 -0.00000 0.00000  -0.00000 213 PHE   G C   
4248  O O   . PHE   C  213 ? 0.34283 0.34283 0.34283 -0.00000 0.00000  0.00000  213 PHE   G O   
4249  C CB  . PHE   C  213 ? 0.28295 0.28295 0.28295 -0.00000 0.00000  0.00000  213 PHE   G CB  
4250  C CG  . PHE   C  213 ? 0.44379 0.44379 0.44379 0.00000  -0.00000 0.00000  213 PHE   G CG  
4251  C CD1 . PHE   C  213 ? 0.48789 0.48789 0.48789 -0.00000 0.00000  0.00000  213 PHE   G CD1 
4252  C CD2 . PHE   C  213 ? 0.29441 0.29441 0.29441 0.00000  0.00000  0.00000  213 PHE   G CD2 
4253  C CE1 . PHE   C  213 ? 0.60789 0.60789 0.60789 0.00000  0.00000  0.00000  213 PHE   G CE1 
4254  C CE2 . PHE   C  213 ? 0.64514 0.64514 0.64514 -0.00000 0.00000  0.00000  213 PHE   G CE2 
4255  C CZ  . PHE   C  213 ? 0.51156 0.51156 0.51156 -0.00000 0.00000  0.00000  213 PHE   G CZ  
4256  N N   . PHE   C  214 ? 0.28857 0.28857 0.28857 0.00000  0.00000  0.00000  214 PHE   G N   
4257  C CA  . PHE   C  214 ? 0.26695 0.26695 0.26695 -0.00000 0.00000  0.00000  214 PHE   G CA  
4258  C C   . PHE   C  214 ? 0.25182 0.25182 0.25182 -0.00000 0.00000  0.00000  214 PHE   G C   
4259  O O   . PHE   C  214 ? 0.60167 0.60167 0.60167 0.00000  0.00000  0.00000  214 PHE   G O   
4260  C CB  . PHE   C  214 ? 0.37757 0.37757 0.37757 0.00000  0.00000  0.00000  214 PHE   G CB  
4261  C CG  . PHE   C  214 ? 0.35491 0.35491 0.35491 0.00000  0.00000  0.00000  214 PHE   G CG  
4262  C CD1 . PHE   C  214 ? 0.33640 0.33640 0.33640 -0.00000 0.00000  0.00000  214 PHE   G CD1 
4263  C CD2 . PHE   C  214 ? 0.44905 0.44905 0.44905 0.00000  0.00000  -0.00000 214 PHE   G CD2 
4264  C CE1 . PHE   C  214 ? 0.29137 0.29137 0.29137 0.00000  0.00000  0.00000  214 PHE   G CE1 
4265  C CE2 . PHE   C  214 ? 0.44133 0.44133 0.44133 -0.00000 0.00000  0.00000  214 PHE   G CE2 
4266  C CZ  . PHE   C  214 ? 0.36433 0.36433 0.36433 0.00000  0.00000  0.00000  214 PHE   G CZ  
4267  N N   . ASN   C  215 ? 0.23003 0.23003 0.23003 0.00000  0.00000  0.00000  215 ASN   G N   
4268  C CA  . ASN   C  215 ? 0.32703 0.32703 0.32703 -0.00000 0.00000  0.00000  215 ASN   G CA  
4269  C C   . ASN   C  215 ? 0.45092 0.45092 0.45092 0.00000  0.00000  0.00000  215 ASN   G C   
4270  O O   . ASN   C  215 ? 0.37169 0.37169 0.37169 0.00000  0.00000  0.00000  215 ASN   G O   
4271  C CB  . ASN   C  215 ? 0.32509 0.32509 0.32509 0.00000  0.00000  0.00000  215 ASN   G CB  
4272  C CG  . ASN   C  215 ? 0.61793 0.61793 0.61793 0.00000  0.00000  0.00000  215 ASN   G CG  
4273  O OD1 . ASN   C  215 ? 0.34767 0.34767 0.34767 0.00000  0.00000  0.00000  215 ASN   G OD1 
4274  N ND2 . ASN   C  215 ? 0.30622 0.30622 0.30622 0.00000  0.00000  0.00000  215 ASN   G ND2 
4275  N N   . ARG   C  216 ? 0.25825 0.25825 0.25825 -0.00000 0.00000  0.00000  216 ARG   G N   
4276  C CA  . ARG   C  216 ? 0.37072 0.37072 0.37072 -0.00000 0.00000  0.00000  216 ARG   G CA  
4277  C C   . ARG   C  216 ? 0.66257 0.66257 0.66257 -0.00000 0.00000  0.00000  216 ARG   G C   
4278  O O   . ARG   C  216 ? 0.36094 0.36094 0.36094 -0.00000 0.00000  0.00000  216 ARG   G O   
4279  C CB  . ARG   C  216 ? 0.32365 0.32365 0.32365 0.00000  0.00000  0.00000  216 ARG   G CB  
4280  C CG  . ARG   C  216 ? 0.31467 0.31467 0.31467 -0.00000 0.00000  0.00000  216 ARG   G CG  
4281  C CD  . ARG   C  216 ? 0.44530 0.44530 0.44530 -0.00000 0.00000  0.00000  216 ARG   G CD  
4282  N NE  . ARG   C  216 ? 0.30523 0.30523 0.30523 0.00000  0.00000  0.00000  216 ARG   G NE  
4283  C CZ  . ARG   C  216 ? 0.61906 0.61906 0.61906 0.00000  0.00000  -0.00000 216 ARG   G CZ  
4284  N NH1 . ARG   C  216 ? 0.35072 0.35072 0.35072 -0.00000 0.00000  0.00000  216 ARG   G NH1 
4285  N NH2 . ARG   C  216 ? 0.40752 0.40752 0.40752 0.00000  0.00000  0.00000  216 ARG   G NH2 
4286  N N   . ARG   C  217 ? 0.31889 0.31889 0.31889 -0.00000 -0.00000 -0.00000 217 ARG   G N   
4287  C CA  . ARG   C  217 ? 0.37882 0.37882 0.37882 0.00000  -0.00000 0.00000  217 ARG   G CA  
4288  C C   . ARG   C  217 ? 0.42480 0.42480 0.42480 0.00000  0.00000  0.00000  217 ARG   G C   
4289  O O   . ARG   C  217 ? 0.64052 0.64052 0.64052 0.00000  0.00000  0.00000  217 ARG   G O   
4290  C CB  . ARG   C  217 ? 0.14076 0.14076 0.14076 0.00000  0.00000  0.00000  217 ARG   G CB  
4291  C CG  . ARG   C  217 ? 0.23596 0.23596 0.23596 -0.00000 0.00000  0.00000  217 ARG   G CG  
4292  C CD  . ARG   C  217 ? 0.71603 0.71603 0.71603 0.00000  0.00000  0.00000  217 ARG   G CD  
4293  N NE  . ARG   C  217 ? 1.38580 1.38580 1.38580 -0.00000 0.00000  0.00000  217 ARG   G NE  
4294  C CZ  . ARG   C  217 ? 0.86905 0.86905 0.86905 0.00000  0.00000  0.00000  217 ARG   G CZ  
4295  N NH1 . ARG   C  217 ? 1.21384 1.21384 1.21384 -0.00000 0.00000  0.00000  217 ARG   G NH1 
4296  N NH2 . ARG   C  217 ? 1.58175 1.58175 1.58175 0.00000  0.00000  0.00000  217 ARG   G NH2 
4297  N N   . PHE   C  218 ? 0.41581 0.41581 0.41581 0.00000  0.00000  -0.00000 218 PHE   G N   
4298  C CA  . PHE   C  218 ? 0.27482 0.27482 0.27482 0.00000  0.00000  0.00000  218 PHE   G CA  
4299  C C   . PHE   C  218 ? 0.66048 0.66048 0.66048 -0.00000 0.00000  0.00000  218 PHE   G C   
4300  O O   . PHE   C  218 ? 0.30282 0.30282 0.30282 0.00000  0.00000  0.00000  218 PHE   G O   
4301  C CB  . PHE   C  218 ? 0.15894 0.15894 0.15894 0.00000  0.00000  0.00000  218 PHE   G CB  
4302  C CG  . PHE   C  218 ? 0.40789 0.40789 0.40789 -0.00000 0.00000  0.00000  218 PHE   G CG  
4303  C CD1 . PHE   C  218 ? 0.18007 0.18007 0.18007 0.00000  0.00000  0.00000  218 PHE   G CD1 
4304  C CD2 . PHE   C  218 ? 0.28976 0.28976 0.28976 0.00000  0.00000  -0.00000 218 PHE   G CD2 
4305  C CE1 . PHE   C  218 ? 0.49986 0.49986 0.49986 0.00000  0.00000  0.00000  218 PHE   G CE1 
4306  C CE2 . PHE   C  218 ? 0.28048 0.28048 0.28048 0.00000  0.00000  0.00000  218 PHE   G CE2 
4307  C CZ  . PHE   C  218 ? 0.19506 0.19506 0.19506 0.00000  0.00000  0.00000  218 PHE   G CZ  
4308  N N   . ARG   C  219 ? 0.39945 0.39945 0.39945 0.00000  0.00000  0.00000  219 ARG   G N   
4309  C CA  . ARG   C  219 ? 0.45430 0.45430 0.45430 0.00000  0.00000  0.00000  219 ARG   G CA  
4310  C C   . ARG   C  219 ? 0.41554 0.41554 0.41554 0.00000  0.00000  0.00000  219 ARG   G C   
4311  O O   . ARG   C  219 ? 0.39700 0.39700 0.39700 0.00000  0.00000  0.00000  219 ARG   G O   
4312  C CB  . ARG   C  219 ? 0.36295 0.36295 0.36295 0.00000  0.00000  0.00000  219 ARG   G CB  
4313  C CG  . ARG   C  219 ? 0.57116 0.57116 0.57116 0.00000  0.00000  0.00000  219 ARG   G CG  
4314  C CD  . ARG   C  219 ? 0.44330 0.44330 0.44330 -0.00000 0.00000  0.00000  219 ARG   G CD  
4315  N NE  . ARG   C  219 ? 0.26759 0.26759 0.26759 0.00000  0.00000  0.00000  219 ARG   G NE  
4316  C CZ  . ARG   C  219 ? 1.12765 1.12765 1.12765 -0.00000 0.00000  0.00000  219 ARG   G CZ  
4317  N NH1 . ARG   C  219 ? 0.27081 0.27081 0.27081 0.00000  0.00000  0.00000  219 ARG   G NH1 
4318  N NH2 . ARG   C  219 ? 0.16715 0.16715 0.16715 -0.00000 0.00000  0.00000  219 ARG   G NH2 
4319  N N   . ASN   C  220 ? 0.37915 0.37915 0.37915 0.00000  0.00000  0.00000  220 ASN   G N   
4320  C CA  . ASN   C  220 ? 0.45573 0.45573 0.45573 -0.00000 0.00000  0.00000  220 ASN   G CA  
4321  C C   . ASN   C  220 ? 0.41632 0.41632 0.41632 0.00000  0.00000  0.00000  220 ASN   G C   
4322  O O   . ASN   C  220 ? 0.48524 0.48524 0.48524 0.00000  0.00000  0.00000  220 ASN   G O   
4323  C CB  . ASN   C  220 ? 0.55593 0.55593 0.55593 0.00000  0.00000  0.00000  220 ASN   G CB  
4324  C CG  . ASN   C  220 ? 0.87614 0.87614 0.87614 -0.00000 -0.00000 0.00000  220 ASN   G CG  
4325  O OD1 . ASN   C  220 ? 0.56266 0.56266 0.56266 0.00000  -0.00000 0.00000  220 ASN   G OD1 
4326  N ND2 . ASN   C  220 ? 0.57893 0.57893 0.57893 -0.00000 0.00000  0.00000  220 ASN   G ND2 
4327  N N   . ARG   C  221 ? 0.39198 0.39198 0.39198 0.00000  0.00000  0.00000  221 ARG   G N   
4328  C CA  . ARG   C  221 ? 0.43431 0.43431 0.43431 0.00000  0.00000  0.00000  221 ARG   G CA  
4329  C C   . ARG   C  221 ? 0.54438 0.54438 0.54438 -0.00000 0.00000  0.00000  221 ARG   G C   
4330  O O   . ARG   C  221 ? 0.41687 0.41687 0.41687 -0.00000 0.00000  0.00000  221 ARG   G O   
4331  C CB  . ARG   C  221 ? 0.27569 0.27569 0.27569 -0.00000 0.00000  0.00000  221 ARG   G CB  
4332  C CG  . ARG   C  221 ? 0.28233 0.28233 0.28233 -0.00000 0.00000  0.00000  221 ARG   G CG  
4333  C CD  . ARG   C  221 ? 0.43051 0.43051 0.43051 0.00000  0.00000  0.00000  221 ARG   G CD  
4334  N NE  . ARG   C  221 ? 0.36757 0.36757 0.36757 0.00000  0.00000  0.00000  221 ARG   G NE  
4335  C CZ  . ARG   C  221 ? 0.51359 0.51359 0.51359 -0.00000 0.00000  0.00000  221 ARG   G CZ  
4336  N NH1 . ARG   C  221 ? 0.44230 0.44230 0.44230 0.00000  0.00000  0.00000  221 ARG   G NH1 
4337  N NH2 . ARG   C  221 ? 0.32475 0.32475 0.32475 0.00000  0.00000  0.00000  221 ARG   G NH2 
4338  N N   . ASP   C  222 ? 0.37202 0.37202 0.37202 0.00000  0.00000  0.00000  222 ASP   G N   
4339  C CA  . ASP   C  222 ? 0.58711 0.58711 0.58711 -0.00000 0.00000  0.00000  222 ASP   G CA  
4340  C C   . ASP   C  222 ? 0.62164 0.62164 0.62164 0.00000  0.00000  -0.00000 222 ASP   G C   
4341  O O   . ASP   C  222 ? 0.45475 0.45475 0.45475 -0.00000 0.00000  0.00000  222 ASP   G O   
4342  C CB  . ASP   C  222 ? 0.30243 0.30243 0.30243 0.00000  0.00000  0.00000  222 ASP   G CB  
4343  C CG  . ASP   C  222 ? 0.54297 0.54297 0.54297 0.00000  0.00000  0.00000  222 ASP   G CG  
4344  O OD1 . ASP   C  222 ? 0.63118 0.63118 0.63118 0.00000  0.00000  0.00000  222 ASP   G OD1 
4345  O OD2 . ASP   C  222 ? 0.74686 0.74686 0.74686 0.00000  0.00000  0.00000  222 ASP   G OD2 
4346  N N   . ILE   C  223 ? 0.34456 0.34456 0.34456 0.00000  0.00000  0.00000  223 ILE   G N   
4347  C CA  . ILE   C  223 ? 0.46559 0.46559 0.46559 0.00000  0.00000  0.00000  223 ILE   G CA  
4348  C C   . ILE   C  223 ? 0.60755 0.60755 0.60755 -0.00000 0.00000  0.00000  223 ILE   G C   
4349  O O   . ILE   C  223 ? 0.63956 0.63956 0.63956 -0.00000 0.00000  0.00000  223 ILE   G O   
4350  C CB  . ILE   C  223 ? 0.62554 0.62554 0.62554 0.00000  -0.00000 0.00000  223 ILE   G CB  
4351  C CG1 . ILE   C  223 ? 0.38511 0.38511 0.38511 0.00000  0.00000  0.00000  223 ILE   G CG1 
4352  C CG2 . ILE   C  223 ? 0.23045 0.23045 0.23045 0.00000  0.00000  0.00000  223 ILE   G CG2 
4353  C CD1 . ILE   C  223 ? 0.42347 0.42347 0.42347 0.00000  0.00000  0.00000  223 ILE   G CD1 
4354  N N   . ASP   C  224 ? 0.41588 0.41588 0.41588 -0.00000 0.00000  0.00000  224 ASP   G N   
4355  C CA  . ASP   C  224 ? 0.42988 0.42988 0.42988 0.00000  0.00000  0.00000  224 ASP   G CA  
4356  C C   . ASP   C  224 ? 0.44099 0.44099 0.44099 0.00000  0.00000  0.00000  224 ASP   G C   
4357  O O   . ASP   C  224 ? 0.38516 0.38516 0.38516 0.00000  0.00000  0.00000  224 ASP   G O   
4358  C CB  . ASP   C  224 ? 0.37809 0.37809 0.37809 0.00000  0.00000  0.00000  224 ASP   G CB  
4359  C CG  . ASP   C  224 ? 0.54740 0.54740 0.54740 0.00000  0.00000  0.00000  224 ASP   G CG  
4360  O OD1 . ASP   C  224 ? 0.58705 0.58705 0.58705 -0.00000 0.00000  0.00000  224 ASP   G OD1 
4361  O OD2 . ASP   C  224 ? 0.54299 0.54299 0.54299 0.00000  -0.00000 0.00000  224 ASP   G OD2 
4362  N N   . ARG   C  225 ? 0.54939 0.54939 0.54939 0.00000  0.00000  -0.00000 225 ARG   G N   
4363  C CA  . ARG   C  225 ? 0.43127 0.43127 0.43127 -0.00000 0.00000  0.00000  225 ARG   G CA  
4364  C C   . ARG   C  225 ? 0.62250 0.62250 0.62250 0.00000  -0.00000 0.00000  225 ARG   G C   
4365  O O   . ARG   C  225 ? 0.54698 0.54698 0.54698 0.00000  0.00000  0.00000  225 ARG   G O   
4366  C CB  . ARG   C  225 ? 0.44460 0.44460 0.44460 0.00000  0.00000  0.00000  225 ARG   G CB  
4367  C CG  . ARG   C  225 ? 0.26497 0.26497 0.26497 0.00000  0.00000  0.00000  225 ARG   G CG  
4368  C CD  . ARG   C  225 ? 0.23183 0.23183 0.23183 0.00000  0.00000  0.00000  225 ARG   G CD  
4369  N NE  . ARG   C  225 ? 0.86859 0.86859 0.86859 0.00000  0.00000  0.00000  225 ARG   G NE  
4370  C CZ  . ARG   C  225 ? 0.36031 0.36031 0.36031 0.00000  0.00000  0.00000  225 ARG   G CZ  
4371  N NH1 . ARG   C  225 ? 0.17835 0.17835 0.17835 0.00000  0.00000  0.00000  225 ARG   G NH1 
4372  N NH2 . ARG   C  225 ? 0.41261 0.41261 0.41261 0.00000  0.00000  0.00000  225 ARG   G NH2 
4373  N N   . PRO   C  226 ? 0.53477 0.53477 0.53477 0.00000  0.00000  0.00000  226 PRO   G N   
4374  C CA  . PRO   C  226 ? 0.30430 0.30430 0.30430 0.00000  0.00000  0.00000  226 PRO   G CA  
4375  C C   . PRO   C  226 ? 0.61505 0.61505 0.61505 0.00000  0.00000  0.00000  226 PRO   G C   
4376  O O   . PRO   C  226 ? 0.40268 0.40268 0.40268 0.00000  0.00000  0.00000  226 PRO   G O   
4377  C CB  . PRO   C  226 ? 0.29309 0.29309 0.29309 -0.00000 0.00000  0.00000  226 PRO   G CB  
4378  C CG  . PRO   C  226 ? 0.27760 0.27760 0.27760 -0.00000 0.00000  0.00000  226 PRO   G CG  
4379  C CD  . PRO   C  226 ? 0.31816 0.31816 0.31816 -0.00000 0.00000  0.00000  226 PRO   G CD  
4380  N N   . VAL   C  227 ? 0.25478 0.25478 0.25478 -0.00000 0.00000  0.00000  227 VAL   G N   
4381  C CA  . VAL   C  227 ? 0.21709 0.21709 0.21709 0.00000  -0.00000 0.00000  227 VAL   G CA  
4382  C C   . VAL   C  227 ? 0.37459 0.37459 0.37459 0.00000  0.00000  0.00000  227 VAL   G C   
4383  O O   . VAL   C  227 ? 0.38714 0.38714 0.38714 -0.00000 0.00000  0.00000  227 VAL   G O   
4384  C CB  . VAL   C  227 ? 0.25726 0.25726 0.25726 -0.00000 0.00000  0.00000  227 VAL   G CB  
4385  C CG1 . VAL   C  227 ? 0.27194 0.27194 0.27194 0.00000  0.00000  0.00000  227 VAL   G CG1 
4386  C CG2 . VAL   C  227 ? 0.19677 0.19677 0.19677 0.00000  0.00000  0.00000  227 VAL   G CG2 
4387  N N   . VAL   C  228 ? 0.32587 0.32587 0.32587 0.00000  0.00000  0.00000  228 VAL   G N   
4388  C CA  . VAL   C  228 ? 0.16872 0.16872 0.16872 0.00000  0.00000  0.00000  228 VAL   G CA  
4389  C C   . VAL   C  228 ? 0.67894 0.67894 0.67894 0.00000  0.00000  0.00000  228 VAL   G C   
4390  O O   . VAL   C  228 ? 0.30242 0.30242 0.30242 0.00000  0.00000  0.00000  228 VAL   G O   
4391  C CB  . VAL   C  228 ? 0.40196 0.40196 0.40196 0.00000  0.00000  -0.00000 228 VAL   G CB  
4392  C CG1 . VAL   C  228 ? 0.22965 0.22965 0.22965 0.00000  0.00000  0.00000  228 VAL   G CG1 
4393  C CG2 . VAL   C  228 ? 0.16144 0.16144 0.16144 0.00000  0.00000  0.00000  228 VAL   G CG2 
4394  N N   . GLY   C  229 ? 0.38102 0.38102 0.38102 0.00000  0.00000  0.00000  229 GLY   G N   
4395  C CA  . GLY   C  229 ? 0.17719 0.17719 0.17719 0.00000  0.00000  0.00000  229 GLY   G CA  
4396  C C   . GLY   C  229 ? 0.26606 0.26606 0.26606 -0.00000 0.00000  0.00000  229 GLY   G C   
4397  O O   . GLY   C  229 ? 0.45859 0.45859 0.45859 0.00000  -0.00000 0.00000  229 GLY   G O   
4398  N N   . GLY   C  230 ? 0.45769 0.45769 0.45769 0.00000  0.00000  0.00000  230 GLY   G N   
4399  C CA  . GLY   C  230 ? 0.10455 0.10455 0.10455 0.00000  0.00000  0.00000  230 GLY   G CA  
4400  C C   . GLY   C  230 ? 0.69338 0.69338 0.69338 -0.00000 0.00000  0.00000  230 GLY   G C   
4401  O O   . GLY   C  230 ? 0.31352 0.31352 0.31352 -0.00000 0.00000  0.00000  230 GLY   G O   
4402  N N   . VAL   C  231 ? 0.32642 0.32642 0.32642 0.00000  0.00000  0.00000  231 VAL   G N   
4403  C CA  . VAL   C  231 ? 0.83739 0.83739 0.83739 -0.00000 0.00000  0.00000  231 VAL   G CA  
4404  C C   . VAL   C  231 ? 0.32906 0.32906 0.32906 0.00000  0.00000  0.00000  231 VAL   G C   
4405  O O   . VAL   C  231 ? 0.77377 0.77377 0.77377 -0.00000 0.00000  0.00000  231 VAL   G O   
4406  C CB  . VAL   C  231 ? 0.23533 0.23533 0.23533 -0.00000 0.00000  0.00000  231 VAL   G CB  
4407  C CG1 . VAL   C  231 ? 0.92946 0.92946 0.92946 0.00000  0.00000  0.00000  231 VAL   G CG1 
4408  C CG2 . VAL   C  231 ? 0.58178 0.58178 0.58178 0.00000  0.00000  0.00000  231 VAL   G CG2 
4409  N N   . ASN   C  232 ? 0.47669 0.47669 0.47669 -0.00000 -0.00000 0.00000  232 ASN   G N   
4410  C CA  . ASN   C  232 ? 0.33707 0.33707 0.33707 -0.00000 0.00000  0.00000  232 ASN   G CA  
4411  C C   . ASN   C  232 ? 0.48504 0.48504 0.48504 -0.00000 0.00000  0.00000  232 ASN   G C   
4412  O O   . ASN   C  232 ? 0.42435 0.42435 0.42435 -0.00000 0.00000  0.00000  232 ASN   G O   
4413  C CB  . ASN   C  232 ? 0.54914 0.54914 0.54914 0.00000  0.00000  0.00000  232 ASN   G CB  
4414  C CG  . ASN   C  232 ? 0.54434 0.54434 0.54434 -0.00000 0.00000  0.00000  232 ASN   G CG  
4415  O OD1 . ASN   C  232 ? 0.55707 0.55707 0.55707 0.00000  0.00000  0.00000  232 ASN   G OD1 
4416  N ND2 . ASN   C  232 ? 1.50857 1.50857 1.50857 0.00000  0.00000  0.00000  232 ASN   G ND2 
4417  N N   . ASN   C  233 ? 0.30682 0.30682 0.30682 0.00000  0.00000  0.00000  233 ASN   G N   
4418  C CA  . ASN   C  233 ? 0.40433 0.40433 0.40433 0.00000  0.00000  0.00000  233 ASN   G CA  
4419  C C   . ASN   C  233 ? 1.06885 1.06885 1.06885 -0.00000 0.00000  0.00000  233 ASN   G C   
4420  O O   . ASN   C  233 ? 0.37581 0.37581 0.37581 0.00000  0.00000  0.00000  233 ASN   G O   
4421  C CB  . ASN   C  233 ? 0.14994 0.14994 0.14994 0.00000  0.00000  0.00000  233 ASN   G CB  
4422  C CG  . ASN   C  233 ? 0.62349 0.62349 0.62349 -0.00000 0.00000  0.00000  233 ASN   G CG  
4423  O OD1 . ASN   C  233 ? 0.53563 0.53563 0.53563 -0.00000 0.00000  0.00000  233 ASN   G OD1 
4424  N ND2 . ASN   C  233 ? 0.48100 0.48100 0.48100 0.00000  0.00000  0.00000  233 ASN   G ND2 
4425  N N   . THR   C  234 ? 0.33594 0.33594 0.33594 0.00000  0.00000  0.00000  234 THR   G N   
4426  C CA  . THR   C  234 ? 0.53015 0.53015 0.53015 0.00000  -0.00000 0.00000  234 THR   G CA  
4427  C C   . THR   C  234 ? 0.27982 0.27982 0.27982 -0.00000 0.00000  -0.00000 234 THR   G C   
4428  O O   . THR   C  234 ? 0.91938 0.91938 0.91938 0.00000  0.00000  0.00000  234 THR   G O   
4429  C CB  . THR   C  234 ? 0.35153 0.35153 0.35153 0.00000  0.00000  0.00000  234 THR   G CB  
4430  O OG1 . THR   C  234 ? 0.48051 0.48051 0.48051 -0.00000 0.00000  0.00000  234 THR   G OG1 
4431  C CG2 . THR   C  234 ? 0.22473 0.22473 0.22473 0.00000  0.00000  0.00000  234 THR   G CG2 
4432  N N   . THR   C  235 ? 0.53100 0.53100 0.53100 0.00000  0.00000  0.00000  235 THR   G N   
4433  C CA  . THR   C  235 ? 0.30569 0.30569 0.30569 -0.00000 0.00000  0.00000  235 THR   G CA  
4434  C C   . THR   C  235 ? 0.56032 0.56032 0.56032 0.00000  0.00000  0.00000  235 THR   G C   
4435  O O   . THR   C  235 ? 0.34825 0.34825 0.34825 0.00000  0.00000  0.00000  235 THR   G O   
4436  C CB  . THR   C  235 ? 0.75088 0.75088 0.75088 0.00000  0.00000  0.00000  235 THR   G CB  
4437  O OG1 . THR   C  235 ? 0.25934 0.25934 0.25934 0.00000  0.00000  0.00000  235 THR   G OG1 
4438  C CG2 . THR   C  235 ? 0.38559 0.38559 0.38559 -0.00000 0.00000  0.00000  235 THR   G CG2 
4439  N N   . LEU   C  236 ? 0.46435 0.46435 0.46435 -0.00000 -0.00000 0.00000  236 LEU   G N   
4440  C CA  . LEU   C  236 ? 0.47032 0.47032 0.47032 0.00000  0.00000  0.00000  236 LEU   G CA  
4441  C C   . LEU   C  236 ? 0.38949 0.38949 0.38949 0.00000  0.00000  0.00000  236 LEU   G C   
4442  O O   . LEU   C  236 ? 0.41126 0.41126 0.41126 0.00000  -0.00000 0.00000  236 LEU   G O   
4443  C CB  . LEU   C  236 ? 0.38833 0.38833 0.38833 0.00000  0.00000  0.00000  236 LEU   G CB  
4444  C CG  . LEU   C  236 ? 0.48070 0.48070 0.48070 0.00000  0.00000  0.00000  236 LEU   G CG  
4445  C CD1 . LEU   C  236 ? 0.37875 0.37875 0.37875 0.00000  0.00000  0.00000  236 LEU   G CD1 
4446  C CD2 . LEU   C  236 ? 0.25813 0.25813 0.25813 -0.00000 0.00000  0.00000  236 LEU   G CD2 
4447  N N   . ILE   C  237 ? 0.44067 0.44067 0.44067 -0.00000 0.00000  0.00000  237 ILE   G N   
4448  C CA  . ILE   C  237 ? 0.35615 0.35615 0.35615 -0.00000 0.00000  0.00000  237 ILE   G CA  
4449  C C   . ILE   C  237 ? 0.49846 0.49846 0.49846 -0.00000 0.00000  0.00000  237 ILE   G C   
4450  O O   . ILE   C  237 ? 0.33284 0.33284 0.33284 0.00000  0.00000  0.00000  237 ILE   G O   
4451  C CB  . ILE   C  237 ? 0.34125 0.34125 0.34125 0.00000  0.00000  0.00000  237 ILE   G CB  
4452  C CG1 . ILE   C  237 ? 0.30227 0.30227 0.30227 0.00000  0.00000  0.00000  237 ILE   G CG1 
4453  C CG2 . ILE   C  237 ? 0.31426 0.31426 0.31426 -0.00000 0.00000  0.00000  237 ILE   G CG2 
4454  C CD1 . ILE   C  237 ? 0.32627 0.32627 0.32627 0.00000  0.00000  0.00000  237 ILE   G CD1 
4455  N N   . SER   C  238 ? 0.27916 0.27916 0.27916 0.00000  0.00000  0.00000  238 SER   G N   
4456  C CA  . SER   C  238 ? 0.36489 0.36489 0.36489 -0.00000 0.00000  0.00000  238 SER   G CA  
4457  C C   . SER   C  238 ? 0.47566 0.47566 0.47566 0.00000  0.00000  0.00000  238 SER   G C   
4458  O O   . SER   C  238 ? 0.28533 0.28533 0.28533 0.00000  0.00000  0.00000  238 SER   G O   
4459  C CB  . SER   C  238 ? 0.34542 0.34542 0.34542 0.00000  0.00000  0.00000  238 SER   G CB  
4460  O OG  . SER   C  238 ? 0.51996 0.51996 0.51996 0.00000  0.00000  0.00000  238 SER   G OG  
4461  N N   . ALA   C  239 ? 0.40653 0.40653 0.40653 -0.00000 0.00000  0.00000  239 ALA   G N   
4462  C CA  . ALA   C  239 ? 0.50855 0.50855 0.50855 -0.00000 -0.00000 0.00000  239 ALA   G CA  
4463  C C   . ALA   C  239 ? 0.20712 0.20712 0.20712 0.00000  0.00000  0.00000  239 ALA   G C   
4464  O O   . ALA   C  239 ? 0.40258 0.40258 0.40258 -0.00000 0.00000  0.00000  239 ALA   G O   
4465  C CB  . ALA   C  239 ? 0.16121 0.16121 0.16121 0.00000  0.00000  0.00000  239 ALA   G CB  
4466  N N   . ALA   C  240 ? 0.35326 0.35326 0.35326 0.00000  -0.00000 0.00000  240 ALA   G N   
4467  C CA  . ALA   C  240 ? 0.27245 0.27245 0.27245 0.00000  0.00000  0.00000  240 ALA   G CA  
4468  C C   . ALA   C  240 ? 0.35439 0.35439 0.35439 0.00000  0.00000  0.00000  240 ALA   G C   
4469  O O   . ALA   C  240 ? 0.29506 0.29506 0.29506 0.00000  0.00000  0.00000  240 ALA   G O   
4470  C CB  . ALA   C  240 ? 0.16771 0.16771 0.16771 0.00000  0.00000  0.00000  240 ALA   G CB  
4471  N N   . CYS   C  241 ? 0.24661 0.24661 0.24661 0.00000  0.00000  0.00000  241 CYS   G N   
4472  C CA  . CYS   C  241 ? 0.37207 0.37207 0.37207 0.00000  0.00000  0.00000  241 CYS   G CA  
4473  C C   . CYS   C  241 ? 0.37599 0.37599 0.37599 -0.00000 0.00000  0.00000  241 CYS   G C   
4474  O O   . CYS   C  241 ? 0.36336 0.36336 0.36336 0.00000  0.00000  0.00000  241 CYS   G O   
4475  C CB  . CYS   C  241 ? 0.39281 0.39281 0.39281 0.00000  -0.00000 0.00000  241 CYS   G CB  
4476  S SG  . CYS   C  241 ? 0.39606 0.39606 0.39606 0.00000  0.00000  0.00000  241 CYS   G SG  
4477  N N   . GLU   C  242 ? 0.43060 0.43060 0.43060 0.00000  0.00000  0.00000  242 GLU   G N   
4478  C CA  . GLU   C  242 ? 0.22375 0.22375 0.22375 -0.00000 0.00000  0.00000  242 GLU   G CA  
4479  C C   . GLU   C  242 ? 0.26050 0.26050 0.26050 0.00000  -0.00000 0.00000  242 GLU   G C   
4480  O O   . GLU   C  242 ? 0.54649 0.54649 0.54649 -0.00000 0.00000  0.00000  242 GLU   G O   
4481  C CB  . GLU   C  242 ? 0.36156 0.36156 0.36156 -0.00000 0.00000  0.00000  242 GLU   G CB  
4482  C CG  . GLU   C  242 ? 0.28978 0.28978 0.28978 0.00000  0.00000  0.00000  242 GLU   G CG  
4483  C CD  . GLU   C  242 ? 0.59381 0.59381 0.59381 0.00000  0.00000  0.00000  242 GLU   G CD  
4484  O OE1 . GLU   C  242 ? 0.33387 0.33387 0.33387 0.00000  0.00000  0.00000  242 GLU   G OE1 
4485  O OE2 . GLU   C  242 ? 0.41676 0.41676 0.41676 -0.00000 0.00000  0.00000  242 GLU   G OE2 
4486  N N   . SER   C  243 ? 0.28947 0.28947 0.28947 -0.00000 0.00000  0.00000  243 SER   G N   
4487  C CA  . SER   C  243 ? 0.43491 0.43491 0.43491 0.00000  0.00000  0.00000  243 SER   G CA  
4488  C C   . SER   C  243 ? 0.31120 0.31120 0.31120 0.00000  0.00000  0.00000  243 SER   G C   
4489  O O   . SER   C  243 ? 0.36824 0.36824 0.36824 0.00000  0.00000  0.00000  243 SER   G O   
4490  C CB  . SER   C  243 ? 0.29851 0.29851 0.29851 -0.00000 0.00000  0.00000  243 SER   G CB  
4491  O OG  . SER   C  243 ? 0.39345 0.39345 0.39345 0.00000  0.00000  0.00000  243 SER   G OG  
4492  N N   . LEU   C  244 ? 0.35226 0.35226 0.35226 0.00000  0.00000  0.00000  244 LEU   G N   
4493  C CA  . LEU   C  244 ? 0.42236 0.42236 0.42236 -0.00000 0.00000  0.00000  244 LEU   G CA  
4494  C C   . LEU   C  244 ? 0.39074 0.39074 0.39074 0.00000  0.00000  0.00000  244 LEU   G C   
4495  O O   . LEU   C  244 ? 0.47029 0.47029 0.47029 0.00000  0.00000  0.00000  244 LEU   G O   
4496  C CB  . LEU   C  244 ? 0.23071 0.23071 0.23071 -0.00000 0.00000  0.00000  244 LEU   G CB  
4497  C CG  . LEU   C  244 ? 0.46423 0.46423 0.46423 -0.00000 0.00000  0.00000  244 LEU   G CG  
4498  C CD1 . LEU   C  244 ? 0.38774 0.38774 0.38774 0.00000  0.00000  0.00000  244 LEU   G CD1 
4499  C CD2 . LEU   C  244 ? 0.30198 0.30198 0.30198 -0.00000 0.00000  0.00000  244 LEU   G CD2 
4500  N N   . SER   C  245 ? 0.80307 0.80307 0.80307 0.00000  0.00000  0.00000  245 SER   G N   
4501  C CA  . SER   C  245 ? 0.30434 0.30434 0.30434 -0.00000 0.00000  0.00000  245 SER   G CA  
4502  C C   . SER   C  245 ? 0.30492 0.30492 0.30492 0.00000  0.00000  0.00000  245 SER   G C   
4503  O O   . SER   C  245 ? 0.41844 0.41844 0.41844 0.00000  0.00000  0.00000  245 SER   G O   
4504  C CB  . SER   C  245 ? 0.33905 0.33905 0.33905 0.00000  -0.00000 0.00000  245 SER   G CB  
4505  O OG  . SER   C  245 ? 0.91623 0.91623 0.91623 0.00000  -0.00000 0.00000  245 SER   G OG  
4506  N N   . TYR   C  246 ? 0.42225 0.42225 0.42225 0.00000  0.00000  0.00000  246 TYR   G N   
4507  C CA  . TYR   C  246 ? 0.29733 0.29733 0.29733 -0.00000 0.00000  0.00000  246 TYR   G CA  
4508  C C   . TYR   C  246 ? 0.31779 0.31779 0.31779 0.00000  0.00000  0.00000  246 TYR   G C   
4509  O O   . TYR   C  246 ? 0.35655 0.35655 0.35655 0.00000  0.00000  0.00000  246 TYR   G O   
4510  C CB  . TYR   C  246 ? 0.17539 0.17539 0.17539 0.00000  0.00000  0.00000  246 TYR   G CB  
4511  C CG  . TYR   C  246 ? 0.38033 0.38033 0.38033 0.00000  0.00000  0.00000  246 TYR   G CG  
4512  C CD1 . TYR   C  246 ? 0.29300 0.29300 0.29300 0.00000  0.00000  0.00000  246 TYR   G CD1 
4513  C CD2 . TYR   C  246 ? 0.11706 0.11706 0.11706 0.00000  0.00000  0.00000  246 TYR   G CD2 
4514  C CE1 . TYR   C  246 ? 0.21369 0.21369 0.21369 -0.00000 0.00000  0.00000  246 TYR   G CE1 
4515  C CE2 . TYR   C  246 ? 0.45006 0.45006 0.45006 -0.00000 0.00000  0.00000  246 TYR   G CE2 
4516  C CZ  . TYR   C  246 ? 0.33632 0.33632 0.33632 0.00000  0.00000  0.00000  246 TYR   G CZ  
4517  O OH  . TYR   C  246 ? 0.54020 0.54020 0.54020 0.00000  0.00000  0.00000  246 TYR   G OH  
4518  N N   . ASN   C  247 ? 0.28289 0.28289 0.28289 -0.00000 0.00000  0.00000  247 ASN   G N   
4519  C CA  . ASN   C  247 ? 0.18643 0.18643 0.18643 0.00000  0.00000  0.00000  247 ASN   G CA  
4520  C C   . ASN   C  247 ? 0.27604 0.27604 0.27604 0.00000  -0.00000 0.00000  247 ASN   G C   
4521  O O   . ASN   C  247 ? 0.31701 0.31701 0.31701 -0.00000 0.00000  0.00000  247 ASN   G O   
4522  C CB  . ASN   C  247 ? 0.31610 0.31610 0.31610 -0.00000 0.00000  0.00000  247 ASN   G CB  
4523  C CG  . ASN   C  247 ? 0.28632 0.28632 0.28632 0.00000  -0.00000 0.00000  247 ASN   G CG  
4524  O OD1 . ASN   C  247 ? 0.50769 0.50769 0.50769 0.00000  0.00000  0.00000  247 ASN   G OD1 
4525  N ND2 . ASN   C  247 ? 0.26659 0.26659 0.26659 0.00000  0.00000  0.00000  247 ASN   G ND2 
4526  N N   . VAL   C  248 ? 0.28103 0.28103 0.28103 0.00000  -0.00000 0.00000  248 VAL   G N   
4527  C CA  . VAL   C  248 ? 0.35437 0.35437 0.35437 -0.00000 0.00000  0.00000  248 VAL   G CA  
4528  C C   . VAL   C  248 ? 0.24717 0.24717 0.24717 0.00000  0.00000  0.00000  248 VAL   G C   
4529  O O   . VAL   C  248 ? 0.34226 0.34226 0.34226 -0.00000 0.00000  0.00000  248 VAL   G O   
4530  C CB  . VAL   C  248 ? 0.29801 0.29801 0.29801 0.00000  0.00000  0.00000  248 VAL   G CB  
4531  C CG1 . VAL   C  248 ? 0.20676 0.20676 0.20676 0.00000  0.00000  0.00000  248 VAL   G CG1 
4532  C CG2 . VAL   C  248 ? 0.27389 0.27389 0.27389 0.00000  0.00000  0.00000  248 VAL   G CG2 
4533  N N   . SER   C  249 ? 0.43113 0.43113 0.43113 -0.00000 0.00000  0.00000  249 SER   G N   
4534  C CA  . SER   C  249 ? 0.27119 0.27119 0.27119 0.00000  0.00000  0.00000  249 SER   G CA  
4535  C C   . SER   C  249 ? 0.43051 0.43051 0.43051 0.00000  0.00000  0.00000  249 SER   G C   
4536  O O   . SER   C  249 ? 0.30135 0.30135 0.30135 0.00000  0.00000  0.00000  249 SER   G O   
4537  C CB  . SER   C  249 ? 0.26597 0.26597 0.26597 -0.00000 0.00000  0.00000  249 SER   G CB  
4538  O OG  . SER   C  249 ? 0.33808 0.33808 0.33808 -0.00000 -0.00000 0.00000  249 SER   G OG  
4539  N N   . TYR   C  250 ? 0.31193 0.31193 0.31193 -0.00000 0.00000  0.00000  250 TYR   G N   
4540  C CA  . TYR   C  250 ? 0.64309 0.64309 0.64309 -0.00000 0.00000  0.00000  250 TYR   G CA  
4541  C C   . TYR   C  250 ? 0.27901 0.27901 0.27901 0.00000  0.00000  0.00000  250 TYR   G C   
4542  O O   . TYR   C  250 ? 0.39437 0.39437 0.39437 0.00000  0.00000  0.00000  250 TYR   G O   
4543  C CB  . TYR   C  250 ? 0.27181 0.27181 0.27181 -0.00000 0.00000  0.00000  250 TYR   G CB  
4544  C CG  . TYR   C  250 ? 0.46857 0.46857 0.46857 0.00000  0.00000  0.00000  250 TYR   G CG  
4545  C CD1 . TYR   C  250 ? 0.29608 0.29608 0.29608 0.00000  0.00000  0.00000  250 TYR   G CD1 
4546  C CD2 . TYR   C  250 ? 0.24691 0.24691 0.24691 0.00000  0.00000  0.00000  250 TYR   G CD2 
4547  C CE1 . TYR   C  250 ? 0.44617 0.44617 0.44617 0.00000  0.00000  0.00000  250 TYR   G CE1 
4548  C CE2 . TYR   C  250 ? 0.38728 0.38728 0.38728 0.00000  0.00000  0.00000  250 TYR   G CE2 
4549  C CZ  . TYR   C  250 ? 0.53807 0.53807 0.53807 0.00000  -0.00000 0.00000  250 TYR   G CZ  
4550  O OH  . TYR   C  250 ? 0.60797 0.60797 0.60797 -0.00000 0.00000  0.00000  250 TYR   G OH  
4551  N N   . ASP   C  251 ? 0.36741 0.36741 0.36741 0.00000  0.00000  0.00000  251 ASP   G N   
4552  C CA  . ASP   C  251 ? 0.37068 0.37068 0.37068 0.00000  0.00000  0.00000  251 ASP   G CA  
4553  C C   . ASP   C  251 ? 0.60693 0.60693 0.60693 0.00000  0.00000  0.00000  251 ASP   G C   
4554  O O   . ASP   C  251 ? 0.41526 0.41526 0.41526 0.00000  0.00000  0.00000  251 ASP   G O   
4555  C CB  . ASP   C  251 ? 0.36220 0.36220 0.36220 0.00000  0.00000  0.00000  251 ASP   G CB  
4556  C CG  . ASP   C  251 ? 0.64350 0.64350 0.64350 0.00000  0.00000  0.00000  251 ASP   G CG  
4557  O OD1 . ASP   C  251 ? 0.47167 0.47167 0.47167 0.00000  0.00000  0.00000  251 ASP   G OD1 
4558  O OD2 . ASP   C  251 ? 0.46588 0.46588 0.46588 0.00000  0.00000  0.00000  251 ASP   G OD2 
4559  N N   . VAL   C  252 ? 0.37806 0.37806 0.37806 0.00000  0.00000  0.00000  252 VAL   G N   
4560  C CA  . VAL   C  252 ? 0.40705 0.40705 0.40705 -0.00000 0.00000  0.00000  252 VAL   G CA  
4561  C C   . VAL   C  252 ? 0.41928 0.41928 0.41928 -0.00000 0.00000  0.00000  252 VAL   G C   
4562  O O   . VAL   C  252 ? 0.44023 0.44023 0.44023 0.00000  0.00000  0.00000  252 VAL   G O   
4563  C CB  . VAL   C  252 ? 0.44311 0.44311 0.44311 0.00000  0.00000  0.00000  252 VAL   G CB  
4564  C CG1 . VAL   C  252 ? 0.29107 0.29107 0.29107 0.00000  0.00000  0.00000  252 VAL   G CG1 
4565  C CG2 . VAL   C  252 ? 0.29601 0.29601 0.29601 0.00000  0.00000  0.00000  252 VAL   G CG2 
4566  N N   . GLN   C  253 ? 0.30973 0.30973 0.30973 0.00000  0.00000  0.00000  253 GLN   G N   
4567  C CA  . GLN   C  253 ? 0.38276 0.38276 0.38276 0.00000  0.00000  0.00000  253 GLN   G CA  
4568  C C   . GLN   C  253 ? 0.53293 0.53293 0.53293 -0.00000 0.00000  0.00000  253 GLN   G C   
4569  O O   . GLN   C  253 ? 0.37372 0.37372 0.37372 -0.00000 0.00000  0.00000  253 GLN   G O   
4570  C CB  . GLN   C  253 ? 0.23876 0.23876 0.23876 -0.00000 0.00000  0.00000  253 GLN   G CB  
4571  C CG  . GLN   C  253 ? 0.71467 0.71467 0.71467 -0.00000 0.00000  0.00000  253 GLN   G CG  
4572  C CD  . GLN   C  253 ? 0.60403 0.60403 0.60403 -0.00000 0.00000  0.00000  253 GLN   G CD  
4573  O OE1 . GLN   C  253 ? 0.61518 0.61518 0.61518 0.00000  -0.00000 -0.00000 253 GLN   G OE1 
4574  N NE2 . GLN   C  253 ? 0.70674 0.70674 0.70674 0.00000  0.00000  0.00000  253 GLN   G NE2 
4575  N N   . SER   C  254 ? 0.55935 0.55935 0.55935 -0.00000 0.00000  0.00000  254 SER   G N   
4576  C CA  . SER   C  254 ? 0.30536 0.30536 0.30536 -0.00000 0.00000  0.00000  254 SER   G CA  
4577  C C   . SER   C  254 ? 0.33183 0.33183 0.33183 0.00000  0.00000  0.00000  254 SER   G C   
4578  O O   . SER   C  254 ? 0.48074 0.48074 0.48074 0.00000  0.00000  0.00000  254 SER   G O   
4579  C CB  . SER   C  254 ? 0.44172 0.44172 0.44172 -0.00000 0.00000  0.00000  254 SER   G CB  
4580  O OG  . SER   C  254 ? 0.33498 0.33498 0.33498 0.00000  0.00000  0.00000  254 SER   G OG  
4581  N N   . LEU   C  255 ? 0.37970 0.37970 0.37970 -0.00000 0.00000  0.00000  255 LEU   G N   
4582  C CA  . LEU   C  255 ? 0.40961 0.40961 0.40961 0.00000  0.00000  0.00000  255 LEU   G CA  
4583  C C   . LEU   C  255 ? 0.42910 0.42910 0.42910 0.00000  0.00000  0.00000  255 LEU   G C   
4584  O O   . LEU   C  255 ? 0.44491 0.44491 0.44491 0.00000  0.00000  0.00000  255 LEU   G O   
4585  C CB  . LEU   C  255 ? 0.44404 0.44404 0.44404 -0.00000 0.00000  0.00000  255 LEU   G CB  
4586  C CG  . LEU   C  255 ? 0.46015 0.46015 0.46015 -0.00000 0.00000  0.00000  255 LEU   G CG  
4587  C CD1 . LEU   C  255 ? 0.44478 0.44478 0.44478 -0.00000 0.00000  0.00000  255 LEU   G CD1 
4588  C CD2 . LEU   C  255 ? 0.31598 0.31598 0.31598 0.00000  0.00000  0.00000  255 LEU   G CD2 
4589  N N   . ASP   C  256 ? 0.52627 0.52627 0.52627 0.00000  0.00000  0.00000  256 ASP   G N   
4590  C CA  . ASP   C  256 ? 0.34102 0.34102 0.34102 0.00000  -0.00000 0.00000  256 ASP   G CA  
4591  C C   . ASP   C  256 ? 0.62644 0.62644 0.62644 0.00000  0.00000  0.00000  256 ASP   G C   
4592  O O   . ASP   C  256 ? 0.37317 0.37317 0.37317 0.00000  0.00000  0.00000  256 ASP   G O   
4593  C CB  . ASP   C  256 ? 0.46799 0.46799 0.46799 0.00000  0.00000  0.00000  256 ASP   G CB  
4594  C CG  . ASP   C  256 ? 0.80645 0.80645 0.80645 0.00000  0.00000  0.00000  256 ASP   G CG  
4595  O OD1 . ASP   C  256 ? 0.47475 0.47475 0.47475 -0.00000 0.00000  -0.00000 256 ASP   G OD1 
4596  O OD2 . ASP   C  256 ? 0.48337 0.48337 0.48337 -0.00000 0.00000  0.00000  256 ASP   G OD2 
4597  N N   . THR   C  257 ? 0.34147 0.34147 0.34147 0.00000  0.00000  0.00000  257 THR   G N   
4598  C CA  . THR   C  257 ? 0.69850 0.69850 0.69850 0.00000  0.00000  0.00000  257 THR   G CA  
4599  C C   . THR   C  257 ? 0.26937 0.26937 0.26937 0.00000  0.00000  0.00000  257 THR   G C   
4600  O O   . THR   C  257 ? 0.54774 0.54774 0.54774 0.00000  0.00000  0.00000  257 THR   G O   
4601  C CB  . THR   C  257 ? 0.35847 0.35847 0.35847 0.00000  0.00000  0.00000  257 THR   G CB  
4602  O OG1 . THR   C  257 ? 0.64613 0.64613 0.64613 0.00000  0.00000  0.00000  257 THR   G OG1 
4603  C CG2 . THR   C  257 ? 0.50521 0.50521 0.50521 -0.00000 0.00000  0.00000  257 THR   G CG2 
4604  N N   . LEU   C  258 ? 0.53629 0.53629 0.53629 -0.00000 0.00000  0.00000  258 LEU   G N   
4605  C CA  . LEU   C  258 ? 0.35196 0.35196 0.35196 0.00000  0.00000  0.00000  258 LEU   G CA  
4606  C C   . LEU   C  258 ? 0.69693 0.69693 0.69693 -0.00000 0.00000  0.00000  258 LEU   G C   
4607  O O   . LEU   C  258 ? 0.73883 0.73883 0.73883 0.00000  0.00000  0.00000  258 LEU   G O   
4608  C CB  . LEU   C  258 ? 0.35361 0.35361 0.35361 -0.00000 0.00000  0.00000  258 LEU   G CB  
4609  C CG  . LEU   C  258 ? 0.30115 0.30115 0.30115 -0.00000 0.00000  0.00000  258 LEU   G CG  
4610  C CD1 . LEU   C  258 ? 0.39221 0.39221 0.39221 0.00000  0.00000  0.00000  258 LEU   G CD1 
4611  C CD2 . LEU   C  258 ? 0.25572 0.25572 0.25572 -0.00000 0.00000  0.00000  258 LEU   G CD2 
4612  N N   . VAL   C  259 ? 0.62797 0.62797 0.62797 -0.00000 0.00000  0.00000  259 VAL   G N   
4613  C CA  . VAL   C  259 ? 0.67025 0.67025 0.67025 -0.00000 0.00000  0.00000  259 VAL   G CA  
4614  C C   . VAL   C  259 ? 1.48270 1.48270 1.48270 -0.00000 0.00000  0.00000  259 VAL   G C   
4615  O O   . VAL   C  259 ? 0.61522 0.61522 0.61522 0.00000  0.00000  0.00000  259 VAL   G O   
4616  C CB  . VAL   C  259 ? 0.91949 0.91949 0.91949 -0.00000 0.00000  0.00000  259 VAL   G CB  
4617  C CG1 . VAL   C  259 ? 0.43983 0.43983 0.43983 0.00000  -0.00000 0.00000  259 VAL   G CG1 
4618  C CG2 . VAL   C  259 ? 0.74857 0.74857 0.74857 0.00000  0.00000  0.00000  259 VAL   G CG2 
4619  N N   . PHE   C  260 ? 0.38769 0.38769 0.38769 -0.00000 0.00000  0.00000  260 PHE   G N   
4620  C CA  . PHE   C  260 ? 1.15435 1.15435 1.15435 0.00000  0.00000  0.00000  260 PHE   G CA  
4621  C C   . PHE   C  260 ? 0.61074 0.61074 0.61074 -0.00000 0.00000  0.00000  260 PHE   G C   
4622  O O   . PHE   C  260 ? 1.57757 1.57757 1.57757 0.00000  0.00000  0.00000  260 PHE   G O   
4623  C CB  . PHE   C  260 ? 0.55376 0.55376 0.55376 0.00000  0.00000  0.00000  260 PHE   G CB  
4624  C CG  . PHE   C  260 ? 0.77824 0.77824 0.77824 0.00000  0.00000  0.00000  260 PHE   G CG  
4625  C CD1 . PHE   C  260 ? 0.49389 0.49389 0.49389 0.00000  -0.00000 0.00000  260 PHE   G CD1 
4626  C CD2 . PHE   C  260 ? 0.69172 0.69172 0.69172 0.00000  0.00000  0.00000  260 PHE   G CD2 
4627  C CE1 . PHE   C  260 ? 1.74791 1.74791 1.74791 0.00000  0.00000  0.00000  260 PHE   G CE1 
4628  C CE2 . PHE   C  260 ? 0.71125 0.71125 0.71125 0.00000  0.00000  0.00000  260 PHE   G CE2 
4629  C CZ  . PHE   C  260 ? 0.92253 0.92253 0.92253 0.00000  0.00000  0.00000  260 PHE   G CZ  
4630  N N   . LYS   C  261 ? 0.76281 0.76281 0.76281 -0.00000 0.00000  0.00000  261 LYS   G N   
4631  C CA  . LYS   C  261 ? 1.22047 1.22047 1.22047 0.00000  0.00000  0.00000  261 LYS   G CA  
4632  C C   . LYS   C  261 ? 0.78336 0.78336 0.78336 0.00000  0.00000  0.00000  261 LYS   G C   
4633  O O   . LYS   C  261 ? 0.43193 0.43193 0.43193 0.00000  0.00000  0.00000  261 LYS   G O   
4634  C CB  . LYS   C  261 ? 0.78705 0.78705 0.78705 0.00000  0.00000  0.00000  261 LYS   G CB  
4635  C CG  . LYS   C  261 ? 0.85363 0.85363 0.85363 0.00000  0.00000  0.00000  261 LYS   G CG  
4636  C CD  . LYS   C  261 ? 0.68413 0.68413 0.68413 0.00000  0.00000  0.00000  261 LYS   G CD  
4637  C CE  . LYS   C  261 ? 0.97301 0.97301 0.97301 -0.00000 0.00000  0.00000  261 LYS   G CE  
4638  N NZ  . LYS   C  261 ? 0.74331 0.74331 0.74331 0.00000  0.00000  0.00000  261 LYS   G NZ  
4639  N N   . GLY   C  262 ? 1.01277 1.01277 1.01277 0.00000  0.00000  0.00000  262 GLY   G N   
4640  C CA  . GLY   C  262 ? 0.31104 0.31104 0.31104 0.00000  0.00000  0.00000  262 GLY   G CA  
4641  C C   . GLY   C  262 ? 1.03120 1.03120 1.03120 0.00000  0.00000  0.00000  262 GLY   G C   
4642  O O   . GLY   C  262 ? 0.94665 0.94665 0.94665 -0.00000 0.00000  0.00000  262 GLY   G O   
4643  N N   . GLU   C  263 ? 0.46527 0.46527 0.46527 0.00000  0.00000  0.00000  263 GLU   G N   
4644  C CA  . GLU   C  263 ? 0.90098 0.90098 0.90098 0.00000  -0.00000 0.00000  263 GLU   G CA  
4645  C C   . GLU   C  263 ? 1.02897 1.02897 1.02897 0.00000  0.00000  0.00000  263 GLU   G C   
4646  O O   . GLU   C  263 ? 0.58355 0.58355 0.58355 0.00000  0.00000  0.00000  263 GLU   G O   
4647  C CB  . GLU   C  263 ? 0.44528 0.44528 0.44528 0.00000  0.00000  0.00000  263 GLU   G CB  
4648  C CG  . GLU   C  263 ? 0.89656 0.89656 0.89656 -0.00000 0.00000  0.00000  263 GLU   G CG  
4649  C CD  . GLU   C  263 ? 0.81106 0.81106 0.81106 0.00000  0.00000  0.00000  263 GLU   G CD  
4650  O OE1 . GLU   C  263 ? 0.43549 0.43549 0.43549 0.00000  0.00000  0.00000  263 GLU   G OE1 
4651  O OE2 . GLU   C  263 ? 0.61070 0.61070 0.61070 0.00000  0.00000  0.00000  263 GLU   G OE2 
4652  N N   . THR   C  264 ? 0.51805 0.51805 0.51805 -0.00000 0.00000  0.00000  264 THR   G N   
4653  C CA  . THR   C  264 ? 0.33478 0.33478 0.33478 0.00000  0.00000  0.00000  264 THR   G CA  
4654  C C   . THR   C  264 ? 0.52790 0.52790 0.52790 0.00000  0.00000  0.00000  264 THR   G C   
4655  O O   . THR   C  264 ? 0.41494 0.41494 0.41494 -0.00000 0.00000  0.00000  264 THR   G O   
4656  C CB  . THR   C  264 ? 0.59879 0.59879 0.59879 0.00000  0.00000  0.00000  264 THR   G CB  
4657  O OG1 . THR   C  264 ? 1.24561 1.24561 1.24561 -0.00000 0.00000  0.00000  264 THR   G OG1 
4658  C CG2 . THR   C  264 ? 0.43399 0.43399 0.43399 -0.00000 0.00000  0.00000  264 THR   G CG2 
4659  N N   . TYR   C  265 ? 0.40986 0.40986 0.40986 0.00000  0.00000  0.00000  265 TYR   G N   
4660  C CA  . TYR   C  265 ? 0.28972 0.28972 0.28972 0.00000  0.00000  0.00000  265 TYR   G CA  
4661  C C   . TYR   C  265 ? 0.35101 0.35101 0.35101 -0.00000 0.00000  0.00000  265 TYR   G C   
4662  O O   . TYR   C  265 ? 0.45257 0.45257 0.45257 -0.00000 0.00000  0.00000  265 TYR   G O   
4663  C CB  . TYR   C  265 ? 0.24000 0.24000 0.24000 -0.00000 0.00000  0.00000  265 TYR   G CB  
4664  C CG  . TYR   C  265 ? 0.47885 0.47885 0.47885 -0.00000 0.00000  0.00000  265 TYR   G CG  
4665  C CD1 . TYR   C  265 ? 0.36929 0.36929 0.36929 -0.00000 0.00000  0.00000  265 TYR   G CD1 
4666  C CD2 . TYR   C  265 ? 0.33843 0.33843 0.33843 -0.00000 0.00000  0.00000  265 TYR   G CD2 
4667  C CE1 . TYR   C  265 ? 0.46948 0.46948 0.46948 0.00000  0.00000  0.00000  265 TYR   G CE1 
4668  C CE2 . TYR   C  265 ? 0.44712 0.44712 0.44712 -0.00000 0.00000  0.00000  265 TYR   G CE2 
4669  C CZ  . TYR   C  265 ? 0.37000 0.37000 0.37000 0.00000  0.00000  0.00000  265 TYR   G CZ  
4670  O OH  . TYR   C  265 ? 0.41220 0.41220 0.41220 0.00000  0.00000  0.00000  265 TYR   G OH  
4671  N N   . SER   C  266 ? 0.33368 0.33368 0.33368 0.00000  0.00000  0.00000  266 SER   G N   
4672  C CA  . SER   C  266 ? 0.19510 0.19510 0.19510 -0.00000 0.00000  0.00000  266 SER   G CA  
4673  C C   . SER   C  266 ? 0.36619 0.36619 0.36619 0.00000  0.00000  0.00000  266 SER   G C   
4674  O O   . SER   C  266 ? 0.24639 0.24639 0.24639 0.00000  0.00000  0.00000  266 SER   G O   
4675  C CB  . SER   C  266 ? 0.21741 0.21741 0.21741 -0.00000 0.00000  0.00000  266 SER   G CB  
4676  O OG  . SER   C  266 ? 0.35103 0.35103 0.35103 0.00000  0.00000  0.00000  266 SER   G OG  
4677  N N   . LEU   C  267 ? 0.28379 0.28379 0.28379 0.00000  -0.00000 0.00000  267 LEU   G N   
4678  C CA  . LEU   C  267 ? 0.40520 0.40520 0.40520 -0.00000 0.00000  0.00000  267 LEU   G CA  
4679  C C   . LEU   C  267 ? 0.27574 0.27574 0.27574 0.00000  0.00000  0.00000  267 LEU   G C   
4680  O O   . LEU   C  267 ? 0.47328 0.47328 0.47328 0.00000  0.00000  0.00000  267 LEU   G O   
4681  C CB  . LEU   C  267 ? 0.19569 0.19569 0.19569 -0.00000 0.00000  0.00000  267 LEU   G CB  
4682  C CG  . LEU   C  267 ? 0.44393 0.44393 0.44393 0.00000  0.00000  0.00000  267 LEU   G CG  
4683  C CD1 . LEU   C  267 ? 0.34358 0.34358 0.34358 -0.00000 0.00000  0.00000  267 LEU   G CD1 
4684  C CD2 . LEU   C  267 ? 0.27121 0.27121 0.27121 -0.00000 0.00000  0.00000  267 LEU   G CD2 
4685  N N   . LYS   C  268 ? 0.57407 0.57407 0.57407 -0.00000 0.00000  0.00000  268 LYS   G N   
4686  C CA  . LYS   C  268 ? 0.30628 0.30628 0.30628 0.00000  0.00000  0.00000  268 LYS   G CA  
4687  C C   . LYS   C  268 ? 0.54606 0.54606 0.54606 0.00000  0.00000  0.00000  268 LYS   G C   
4688  O O   . LYS   C  268 ? 0.28162 0.28162 0.28162 0.00000  0.00000  0.00000  268 LYS   G O   
4689  C CB  . LYS   C  268 ? 0.38742 0.38742 0.38742 0.00000  0.00000  0.00000  268 LYS   G CB  
4690  C CG  . LYS   C  268 ? 0.55099 0.55099 0.55099 0.00000  0.00000  0.00000  268 LYS   G CG  
4691  C CD  . LYS   C  268 ? 0.46995 0.46995 0.46995 0.00000  0.00000  0.00000  268 LYS   G CD  
4692  C CE  . LYS   C  268 ? 0.62932 0.62932 0.62932 -0.00000 0.00000  0.00000  268 LYS   G CE  
4693  N NZ  . LYS   C  268 ? 0.58856 0.58856 0.58856 -0.00000 0.00000  0.00000  268 LYS   G NZ  
4694  N N   . HIS   C  269 ? 0.32950 0.32950 0.32950 -0.00000 0.00000  0.00000  269 HIS   G N   
4695  C CA  . HIS   C  269 ? 0.13322 0.13322 0.13322 0.00000  0.00000  0.00000  269 HIS   G CA  
4696  C C   . HIS   C  269 ? 0.44898 0.44898 0.44898 -0.00000 0.00000  0.00000  269 HIS   G C   
4697  O O   . HIS   C  269 ? 0.23033 0.23033 0.23033 0.00000  0.00000  0.00000  269 HIS   G O   
4698  C CB  . HIS   C  269 ? 0.23027 0.23027 0.23027 0.00000  0.00000  0.00000  269 HIS   G CB  
4699  C CG  . HIS   C  269 ? 0.28152 0.28152 0.28152 0.00000  -0.00000 -0.00000 269 HIS   G CG  
4700  N ND1 . HIS   C  269 ? 0.55210 0.55210 0.55210 0.00000  0.00000  0.00000  269 HIS   G ND1 
4701  C CD2 . HIS   C  269 ? 0.37366 0.37366 0.37366 0.00000  0.00000  0.00000  269 HIS   G CD2 
4702  C CE1 . HIS   C  269 ? 0.23828 0.23828 0.23828 -0.00000 0.00000  0.00000  269 HIS   G CE1 
4703  N NE2 . HIS   C  269 ? 0.43519 0.43519 0.43519 -0.00000 0.00000  0.00000  269 HIS   G NE2 
4704  N N   . LEU   C  270 ? 0.28461 0.28461 0.28461 0.00000  0.00000  0.00000  270 LEU   G N   
4705  C CA  . LEU   C  270 ? 0.22451 0.22451 0.22451 -0.00000 0.00000  0.00000  270 LEU   G CA  
4706  C C   . LEU   C  270 ? 0.27122 0.27122 0.27122 0.00000  0.00000  0.00000  270 LEU   G C   
4707  O O   . LEU   C  270 ? 0.31626 0.31626 0.31626 -0.00000 0.00000  0.00000  270 LEU   G O   
4708  C CB  . LEU   C  270 ? 0.30964 0.30964 0.30964 0.00000  0.00000  0.00000  270 LEU   G CB  
4709  C CG  . LEU   C  270 ? 0.27243 0.27243 0.27243 0.00000  0.00000  0.00000  270 LEU   G CG  
4710  C CD1 . LEU   C  270 ? 0.24375 0.24375 0.24375 -0.00000 -0.00000 0.00000  270 LEU   G CD1 
4711  C CD2 . LEU   C  270 ? 0.34501 0.34501 0.34501 -0.00000 0.00000  0.00000  270 LEU   G CD2 
4712  N N   . LEU   C  271 ? 0.36125 0.36125 0.36125 0.00000  0.00000  0.00000  271 LEU   G N   
4713  C CA  . LEU   C  271 ? 0.31853 0.31853 0.31853 0.00000  -0.00000 0.00000  271 LEU   G CA  
4714  C C   . LEU   C  271 ? 0.42533 0.42533 0.42533 -0.00000 0.00000  0.00000  271 LEU   G C   
4715  O O   . LEU   C  271 ? 0.29314 0.29314 0.29314 0.00000  0.00000  0.00000  271 LEU   G O   
4716  C CB  . LEU   C  271 ? 0.19774 0.19774 0.19774 -0.00000 0.00000  0.00000  271 LEU   G CB  
4717  C CG  . LEU   C  271 ? 0.36352 0.36352 0.36352 -0.00000 0.00000  0.00000  271 LEU   G CG  
4718  C CD1 . LEU   C  271 ? 0.25101 0.25101 0.25101 0.00000  0.00000  0.00000  271 LEU   G CD1 
4719  C CD2 . LEU   C  271 ? 0.16902 0.16902 0.16902 -0.00000 0.00000  0.00000  271 LEU   G CD2 
4720  N N   . ASN   C  272 ? 0.25106 0.25106 0.25106 0.00000  0.00000  0.00000  272 ASN   G N   
4721  C CA  . ASN   C  272 ? 0.14975 0.14975 0.14975 0.00000  0.00000  0.00000  272 ASN   G CA  
4722  C C   . ASN   C  272 ? 0.30347 0.30347 0.30347 0.00000  0.00000  0.00000  272 ASN   G C   
4723  O O   . ASN   C  272 ? 0.38951 0.38951 0.38951 0.00000  0.00000  0.00000  272 ASN   G O   
4724  C CB  . ASN   C  272 ? 0.42724 0.42724 0.42724 -0.00000 0.00000  0.00000  272 ASN   G CB  
4725  C CG  . ASN   C  272 ? 0.30681 0.30681 0.30681 0.00000  0.00000  0.00000  272 ASN   G CG  
4726  O OD1 . ASN   C  272 ? 0.30433 0.30433 0.30433 0.00000  0.00000  0.00000  272 ASN   G OD1 
4727  N ND2 . ASN   C  272 ? 0.38574 0.38574 0.38574 0.00000  -0.00000 0.00000  272 ASN   G ND2 
4728  N N   . ASN   C  273 ? 0.26051 0.26051 0.26051 0.00000  -0.00000 0.00000  273 ASN   G N   
4729  C CA  . ASN   C  273 ? 0.37585 0.37585 0.37585 0.00000  0.00000  0.00000  273 ASN   G CA  
4730  C C   . ASN   C  273 ? 0.22398 0.22398 0.22398 0.00000  0.00000  0.00000  273 ASN   G C   
4731  O O   . ASN   C  273 ? 0.33538 0.33538 0.33538 0.00000  0.00000  0.00000  273 ASN   G O   
4732  C CB  . ASN   C  273 ? 0.30605 0.30605 0.30605 0.00000  0.00000  0.00000  273 ASN   G CB  
4733  C CG  . ASN   C  273 ? 0.76837 0.76837 0.76837 0.00000  0.00000  0.00000  273 ASN   G CG  
4734  O OD1 . ASN   C  273 ? 0.83723 0.83723 0.83723 0.00000  0.00000  0.00000  273 ASN   G OD1 
4735  N ND2 . ASN   C  273 ? 0.80208 0.80208 0.80208 0.00000  0.00000  0.00000  273 ASN   G ND2 
4736  N N   . ASP   C  274 ? 0.42018 0.42018 0.42018 0.00000  0.00000  0.00000  274 ASP   G N   
4737  C CA  . ASP   C  274 ? 0.38495 0.38495 0.38495 0.00000  0.00000  0.00000  274 ASP   G CA  
4738  C C   . ASP   C  274 ? 0.31400 0.31400 0.31400 -0.00000 0.00000  0.00000  274 ASP   G C   
4739  O O   . ASP   C  274 ? 0.32451 0.32451 0.32451 0.00000  0.00000  0.00000  274 ASP   G O   
4740  C CB  . ASP   C  274 ? 0.34178 0.34178 0.34178 -0.00000 0.00000  0.00000  274 ASP   G CB  
4741  C CG  . ASP   C  274 ? 0.46375 0.46375 0.46375 0.00000  0.00000  0.00000  274 ASP   G CG  
4742  O OD1 . ASP   C  274 ? 0.57101 0.57101 0.57101 0.00000  0.00000  0.00000  274 ASP   G OD1 
4743  O OD2 . ASP   C  274 ? 0.74482 0.74482 0.74482 -0.00000 -0.00000 0.00000  274 ASP   G OD2 
4744  N N   . PRO   C  275 ? 0.45635 0.45635 0.45635 -0.00000 0.00000  0.00000  275 PRO   G N   
4745  C CA  . PRO   C  275 ? 0.20271 0.20271 0.20271 0.00000  0.00000  0.00000  275 PRO   G CA  
4746  C C   . PRO   C  275 ? 0.32431 0.32431 0.32431 0.00000  0.00000  0.00000  275 PRO   G C   
4747  O O   . PRO   C  275 ? 0.49296 0.49296 0.49296 0.00000  0.00000  0.00000  275 PRO   G O   
4748  C CB  . PRO   C  275 ? 0.23090 0.23090 0.23090 0.00000  0.00000  0.00000  275 PRO   G CB  
4749  C CG  . PRO   C  275 ? 0.25682 0.25682 0.25682 0.00000  0.00000  0.00000  275 PRO   G CG  
4750  C CD  . PRO   C  275 ? 0.30668 0.30668 0.30668 0.00000  0.00000  -0.00000 275 PRO   G CD  
4751  N N   . PHE   C  276 ? 0.41355 0.41355 0.41355 0.00000  0.00000  0.00000  276 PHE   G N   
4752  C CA  . PHE   C  276 ? 0.29111 0.29111 0.29111 -0.00000 0.00000  0.00000  276 PHE   G CA  
4753  C C   . PHE   C  276 ? 0.50756 0.50756 0.50756 0.00000  0.00000  0.00000  276 PHE   G C   
4754  O O   . PHE   C  276 ? 0.45511 0.45511 0.45511 0.00000  0.00000  0.00000  276 PHE   G O   
4755  C CB  . PHE   C  276 ? 0.30679 0.30679 0.30679 0.00000  0.00000  0.00000  276 PHE   G CB  
4756  C CG  . PHE   C  276 ? 0.50326 0.50326 0.50326 -0.00000 0.00000  0.00000  276 PHE   G CG  
4757  C CD1 . PHE   C  276 ? 0.41469 0.41469 0.41469 -0.00000 0.00000  0.00000  276 PHE   G CD1 
4758  C CD2 . PHE   C  276 ? 0.37753 0.37753 0.37753 0.00000  0.00000  0.00000  276 PHE   G CD2 
4759  C CE1 . PHE   C  276 ? 0.56387 0.56387 0.56387 0.00000  0.00000  0.00000  276 PHE   G CE1 
4760  C CE2 . PHE   C  276 ? 0.61217 0.61217 0.61217 -0.00000 0.00000  0.00000  276 PHE   G CE2 
4761  C CZ  . PHE   C  276 ? 0.49178 0.49178 0.49178 0.00000  0.00000  0.00000  276 PHE   G CZ  
4762  N N   . THR   C  277 ? 0.35960 0.35960 0.35960 0.00000  0.00000  0.00000  277 THR   G N   
4763  C CA  . THR   C  277 ? 0.43210 0.43210 0.43210 -0.00000 0.00000  0.00000  277 THR   G CA  
4764  C C   . THR   C  277 ? 0.32542 0.32542 0.32542 0.00000  0.00000  0.00000  277 THR   G C   
4765  O O   . THR   C  277 ? 0.40218 0.40218 0.40218 -0.00000 0.00000  0.00000  277 THR   G O   
4766  C CB  . THR   C  277 ? 0.28954 0.28954 0.28954 -0.00000 0.00000  0.00000  277 THR   G CB  
4767  O OG1 . THR   C  277 ? 0.36852 0.36852 0.36852 -0.00000 0.00000  0.00000  277 THR   G OG1 
4768  C CG2 . THR   C  277 ? 0.16283 0.16283 0.16283 -0.00000 0.00000  0.00000  277 THR   G CG2 
4769  N N   . PRO   C  278 ? 0.66915 0.66915 0.66915 0.00000  0.00000  0.00000  278 PRO   G N   
4770  C CA  . PRO   C  278 ? 0.32330 0.32330 0.32330 -0.00000 0.00000  0.00000  278 PRO   G CA  
4771  C C   . PRO   C  278 ? 0.50069 0.50069 0.50069 0.00000  0.00000  0.00000  278 PRO   G C   
4772  O O   . PRO   C  278 ? 0.35584 0.35584 0.35584 0.00000  0.00000  0.00000  278 PRO   G O   
4773  C CB  . PRO   C  278 ? 0.23129 0.23129 0.23129 0.00000  0.00000  0.00000  278 PRO   G CB  
4774  C CG  . PRO   C  278 ? 0.27909 0.27909 0.27909 0.00000  0.00000  0.00000  278 PRO   G CG  
4775  C CD  . PRO   C  278 ? 0.31595 0.31595 0.31595 0.00000  0.00000  0.00000  278 PRO   G CD  
4776  N N   . GLN   C  279 ? 0.35850 0.35850 0.35850 -0.00000 -0.00000 0.00000  279 GLN   G N   
4777  C CA  . GLN   C  279 ? 0.33082 0.33082 0.33082 0.00000  0.00000  0.00000  279 GLN   G CA  
4778  C C   . GLN   C  279 ? 0.50056 0.50056 0.50056 -0.00000 -0.00000 0.00000  279 GLN   G C   
4779  O O   . GLN   C  279 ? 0.48018 0.48018 0.48018 -0.00000 0.00000  0.00000  279 GLN   G O   
4780  C CB  . GLN   C  279 ? 0.29836 0.29836 0.29836 -0.00000 -0.00000 -0.00000 279 GLN   G CB  
4781  C CG  . GLN   C  279 ? 0.19074 0.19074 0.19074 0.00000  0.00000  0.00000  279 GLN   G CG  
4782  C CD  . GLN   C  279 ? 0.69135 0.69135 0.69135 -0.00000 0.00000  0.00000  279 GLN   G CD  
4783  O OE1 . GLN   C  279 ? 0.51189 0.51189 0.51189 -0.00000 0.00000  0.00000  279 GLN   G OE1 
4784  N NE2 . GLN   C  279 ? 0.39821 0.39821 0.39821 0.00000  0.00000  0.00000  279 GLN   G NE2 
4785  N N   . PHE   C  280 ? 0.35379 0.35379 0.35379 -0.00000 0.00000  0.00000  280 PHE   G N   
4786  C CA  . PHE   C  280 ? 0.37377 0.37377 0.37377 -0.00000 0.00000  0.00000  280 PHE   G CA  
4787  C C   . PHE   C  280 ? 0.35252 0.35252 0.35252 0.00000  0.00000  0.00000  280 PHE   G C   
4788  O O   . PHE   C  280 ? 0.38638 0.38638 0.38638 -0.00000 0.00000  0.00000  280 PHE   G O   
4789  C CB  . PHE   C  280 ? 0.14470 0.14470 0.14470 -0.00000 0.00000  0.00000  280 PHE   G CB  
4790  C CG  . PHE   C  280 ? 0.52372 0.52372 0.52372 0.00000  0.00000  0.00000  280 PHE   G CG  
4791  C CD1 . PHE   C  280 ? 0.27928 0.27928 0.27928 0.00000  -0.00000 0.00000  280 PHE   G CD1 
4792  C CD2 . PHE   C  280 ? 0.15674 0.15674 0.15674 0.00000  0.00000  0.00000  280 PHE   G CD2 
4793  C CE1 . PHE   C  280 ? 0.46568 0.46568 0.46568 0.00000  0.00000  0.00000  280 PHE   G CE1 
4794  C CE2 . PHE   C  280 ? 0.45696 0.45696 0.45696 -0.00000 0.00000  0.00000  280 PHE   G CE2 
4795  C CZ  . PHE   C  280 ? 0.36038 0.36038 0.36038 0.00000  0.00000  0.00000  280 PHE   G CZ  
4796  N N   . GLU   C  281 ? 0.40431 0.40431 0.40431 0.00000  0.00000  0.00000  281 GLU   G N   
4797  C CA  . GLU   C  281 ? 0.56698 0.56698 0.56698 -0.00000 0.00000  0.00000  281 GLU   G CA  
4798  C C   . GLU   C  281 ? 0.27882 0.27882 0.27882 -0.00000 0.00000  0.00000  281 GLU   G C   
4799  O O   . GLU   C  281 ? 0.52829 0.52829 0.52829 0.00000  -0.00000 0.00000  281 GLU   G O   
4800  C CB  . GLU   C  281 ? 0.32021 0.32021 0.32021 0.00000  0.00000  0.00000  281 GLU   G CB  
4801  C CG  . GLU   C  281 ? 0.72521 0.72521 0.72521 0.00000  0.00000  0.00000  281 GLU   G CG  
4802  C CD  . GLU   C  281 ? 1.58906 1.58906 1.58906 0.00000  0.00000  0.00000  281 GLU   G CD  
4803  O OE1 . GLU   C  281 ? 0.56502 0.56502 0.56502 0.00000  0.00000  0.00000  281 GLU   G OE1 
4804  O OE2 . GLU   C  281 ? 0.76733 0.76733 0.76733 0.00000  0.00000  0.00000  281 GLU   G OE2 
4805  N N   . HIS   C  282 ? 0.26115 0.26115 0.26115 0.00000  0.00000  0.00000  282 HIS   G N   
4806  C CA  . HIS   C  282 ? 0.55987 0.55987 0.55987 -0.00000 0.00000  0.00000  282 HIS   G CA  
4807  C C   . HIS   C  282 ? 0.40259 0.40259 0.40259 0.00000  0.00000  0.00000  282 HIS   G C   
4808  O O   . HIS   C  282 ? 0.46878 0.46878 0.46878 0.00000  0.00000  0.00000  282 HIS   G O   
4809  C CB  . HIS   C  282 ? 0.14834 0.14834 0.14834 0.00000  0.00000  0.00000  282 HIS   G CB  
4810  C CG  . HIS   C  282 ? 0.74030 0.74030 0.74030 -0.00000 0.00000  0.00000  282 HIS   G CG  
4811  N ND1 . HIS   C  282 ? 0.54666 0.54666 0.54666 -0.00000 0.00000  0.00000  282 HIS   G ND1 
4812  C CD2 . HIS   C  282 ? 0.23709 0.23709 0.23709 0.00000  0.00000  0.00000  282 HIS   G CD2 
4813  C CE1 . HIS   C  282 ? 0.34273 0.34273 0.34273 0.00000  0.00000  0.00000  282 HIS   G CE1 
4814  N NE2 . HIS   C  282 ? 0.49419 0.49419 0.49419 0.00000  0.00000  0.00000  282 HIS   G NE2 
4815  N N   . GLY   C  283 ? 0.52325 0.52325 0.52325 -0.00000 -0.00000 0.00000  283 GLY   G N   
4816  C CA  . GLY   C  283 ? 0.26434 0.26434 0.26434 0.00000  0.00000  0.00000  283 GLY   G CA  
4817  C C   . GLY   C  283 ? 0.41855 0.41855 0.41855 0.00000  0.00000  0.00000  283 GLY   G C   
4818  O O   . GLY   C  283 ? 0.40642 0.40642 0.40642 0.00000  0.00000  0.00000  283 GLY   G O   
4819  N N   . SER   C  284 ? 0.29190 0.29190 0.29190 -0.00000 0.00000  0.00000  284 SER   G N   
4820  C CA  . SER   C  284 ? 0.40216 0.40216 0.40216 0.00000  0.00000  0.00000  284 SER   G CA  
4821  C C   . SER   C  284 ? 0.32626 0.32626 0.32626 0.00000  0.00000  0.00000  284 SER   G C   
4822  O O   . SER   C  284 ? 0.23679 0.23679 0.23679 0.00000  0.00000  0.00000  284 SER   G O   
4823  C CB  . SER   C  284 ? 0.18743 0.18743 0.18743 -0.00000 0.00000  0.00000  284 SER   G CB  
4824  O OG  . SER   C  284 ? 0.42453 0.42453 0.42453 0.00000  0.00000  0.00000  284 SER   G OG  
4825  N N   . ILE   C  285 ? 0.31342 0.31342 0.31342 0.00000  0.00000  0.00000  285 ILE   G N   
4826  C CA  . ILE   C  285 ? 0.29749 0.29749 0.29749 -0.00000 0.00000  0.00000  285 ILE   G CA  
4827  C C   . ILE   C  285 ? 0.24882 0.24882 0.24882 -0.00000 0.00000  0.00000  285 ILE   G C   
4828  O O   . ILE   C  285 ? 0.48939 0.48939 0.48939 0.00000  0.00000  0.00000  285 ILE   G O   
4829  C CB  . ILE   C  285 ? 0.34060 0.34060 0.34060 -0.00000 -0.00000 0.00000  285 ILE   G CB  
4830  C CG1 . ILE   C  285 ? 0.29614 0.29614 0.29614 0.00000  0.00000  0.00000  285 ILE   G CG1 
4831  C CG2 . ILE   C  285 ? 0.24476 0.24476 0.24476 0.00000  0.00000  0.00000  285 ILE   G CG2 
4832  C CD1 . ILE   C  285 ? 0.40113 0.40113 0.40113 -0.00000 0.00000  0.00000  285 ILE   G CD1 
4833  N N   . LEU   C  286 ? 0.42926 0.42926 0.42926 0.00000  -0.00000 0.00000  286 LEU   G N   
4834  C CA  . LEU   C  286 ? 0.21230 0.21230 0.21230 0.00000  0.00000  0.00000  286 LEU   G CA  
4835  C C   . LEU   C  286 ? 0.29969 0.29969 0.29969 0.00000  0.00000  0.00000  286 LEU   G C   
4836  O O   . LEU   C  286 ? 0.35940 0.35940 0.35940 -0.00000 0.00000  0.00000  286 LEU   G O   
4837  C CB  . LEU   C  286 ? 0.40464 0.40464 0.40464 0.00000  0.00000  0.00000  286 LEU   G CB  
4838  C CG  . LEU   C  286 ? 0.34970 0.34970 0.34970 0.00000  0.00000  0.00000  286 LEU   G CG  
4839  C CD1 . LEU   C  286 ? 0.28587 0.28587 0.28587 -0.00000 0.00000  0.00000  286 LEU   G CD1 
4840  C CD2 . LEU   C  286 ? 0.35220 0.35220 0.35220 0.00000  0.00000  0.00000  286 LEU   G CD2 
4841  N N   . GLN   C  287 ? 0.20626 0.20626 0.20626 0.00000  0.00000  0.00000  287 GLN   G N   
4842  C CA  . GLN   C  287 ? 0.38436 0.38436 0.38436 -0.00000 0.00000  0.00000  287 GLN   G CA  
4843  C C   . GLN   C  287 ? 0.39297 0.39297 0.39297 0.00000  0.00000  0.00000  287 GLN   G C   
4844  O O   . GLN   C  287 ? 0.31151 0.31151 0.31151 -0.00000 0.00000  0.00000  287 GLN   G O   
4845  C CB  . GLN   C  287 ? 0.24560 0.24560 0.24560 0.00000  0.00000  0.00000  287 GLN   G CB  
4846  C CG  . GLN   C  287 ? 0.34577 0.34577 0.34577 0.00000  0.00000  0.00000  287 GLN   G CG  
4847  C CD  . GLN   C  287 ? 0.31107 0.31107 0.31107 0.00000  0.00000  0.00000  287 GLN   G CD  
4848  O OE1 . GLN   C  287 ? 0.33816 0.33816 0.33816 0.00000  0.00000  0.00000  287 GLN   G OE1 
4849  N NE2 . GLN   C  287 ? 0.26188 0.26188 0.26188 0.00000  0.00000  0.00000  287 GLN   G NE2 
4850  N N   . GLY   C  288 ? 0.34410 0.34410 0.34410 -0.00000 0.00000  0.00000  288 GLY   G N   
4851  C CA  . GLY   C  288 ? 0.24062 0.24062 0.24062 0.00000  0.00000  0.00000  288 GLY   G CA  
4852  C C   . GLY   C  288 ? 0.29910 0.29910 0.29910 -0.00000 0.00000  0.00000  288 GLY   G C   
4853  O O   . GLY   C  288 ? 0.48955 0.48955 0.48955 -0.00000 0.00000  0.00000  288 GLY   G O   
4854  N N   . PHE   C  289 ? 0.36294 0.36294 0.36294 0.00000  0.00000  0.00000  289 PHE   G N   
4855  C CA  . PHE   C  289 ? 0.44593 0.44593 0.44593 0.00000  0.00000  0.00000  289 PHE   G CA  
4856  C C   . PHE   C  289 ? 0.38641 0.38641 0.38641 0.00000  0.00000  0.00000  289 PHE   G C   
4857  O O   . PHE   C  289 ? 0.41671 0.41671 0.41671 0.00000  0.00000  0.00000  289 PHE   G O   
4858  C CB  . PHE   C  289 ? 0.30713 0.30713 0.30713 0.00000  0.00000  0.00000  289 PHE   G CB  
4859  C CG  . PHE   C  289 ? 0.37911 0.37911 0.37911 -0.00000 0.00000  0.00000  289 PHE   G CG  
4860  C CD1 . PHE   C  289 ? 0.23710 0.23710 0.23710 0.00000  -0.00000 0.00000  289 PHE   G CD1 
4861  C CD2 . PHE   C  289 ? 0.37203 0.37203 0.37203 -0.00000 0.00000  0.00000  289 PHE   G CD2 
4862  C CE1 . PHE   C  289 ? 0.47321 0.47321 0.47321 0.00000  0.00000  0.00000  289 PHE   G CE1 
4863  C CE2 . PHE   C  289 ? 0.41453 0.41453 0.41453 -0.00000 -0.00000 0.00000  289 PHE   G CE2 
4864  C CZ  . PHE   C  289 ? 0.39299 0.39299 0.39299 -0.00000 0.00000  0.00000  289 PHE   G CZ  
4865  N N   . LEU   C  290 ? 0.32894 0.32894 0.32894 0.00000  0.00000  0.00000  290 LEU   G N   
4866  C CA  . LEU   C  290 ? 0.32097 0.32097 0.32097 -0.00000 0.00000  0.00000  290 LEU   G CA  
4867  C C   . LEU   C  290 ? 0.37629 0.37629 0.37629 -0.00000 0.00000  0.00000  290 LEU   G C   
4868  O O   . LEU   C  290 ? 0.62485 0.62485 0.62485 0.00000  0.00000  0.00000  290 LEU   G O   
4869  C CB  . LEU   C  290 ? 0.23405 0.23405 0.23405 0.00000  0.00000  0.00000  290 LEU   G CB  
4870  C CG  . LEU   C  290 ? 0.33225 0.33225 0.33225 0.00000  0.00000  0.00000  290 LEU   G CG  
4871  C CD1 . LEU   C  290 ? 0.30246 0.30246 0.30246 0.00000  0.00000  0.00000  290 LEU   G CD1 
4872  C CD2 . LEU   C  290 ? 0.23182 0.23182 0.23182 0.00000  0.00000  0.00000  290 LEU   G CD2 
4873  N N   . ASN   C  291 ? 0.53726 0.53726 0.53726 0.00000  0.00000  0.00000  291 ASN   G N   
4874  C CA  . ASN   C  291 ? 0.37794 0.37794 0.37794 0.00000  0.00000  0.00000  291 ASN   G CA  
4875  C C   . ASN   C  291 ? 0.43519 0.43519 0.43519 -0.00000 0.00000  0.00000  291 ASN   G C   
4876  O O   . ASN   C  291 ? 0.43035 0.43035 0.43035 -0.00000 0.00000  0.00000  291 ASN   G O   
4877  C CB  . ASN   C  291 ? 0.72065 0.72065 0.72065 0.00000  0.00000  0.00000  291 ASN   G CB  
4878  C CG  . ASN   C  291 ? 0.85958 0.85958 0.85958 0.00000  0.00000  0.00000  291 ASN   G CG  
4879  O OD1 . ASN   C  291 ? 1.43967 1.43967 1.43967 -0.00000 0.00000  0.00000  291 ASN   G OD1 
4880  N ND2 . ASN   C  291 ? 0.86864 0.86864 0.86864 -0.00000 0.00000  0.00000  291 ASN   G ND2 
4881  N N   . VAL   C  292 ? 0.38026 0.38026 0.38026 0.00000  0.00000  0.00000  292 VAL   G N   
4882  C CA  . VAL   C  292 ? 0.73454 0.73454 0.73454 0.00000  0.00000  0.00000  292 VAL   G CA  
4883  C C   . VAL   C  292 ? 0.74392 0.74392 0.74392 0.00000  0.00000  0.00000  292 VAL   G C   
4884  O O   . VAL   C  292 ? 0.52069 0.52069 0.52069 -0.00000 0.00000  0.00000  292 VAL   G O   
4885  C CB  . VAL   C  292 ? 0.71326 0.71326 0.71326 -0.00000 0.00000  0.00000  292 VAL   G CB  
4886  C CG1 . VAL   C  292 ? 0.62281 0.62281 0.62281 0.00000  0.00000  0.00000  292 VAL   G CG1 
4887  C CG2 . VAL   C  292 ? 0.52046 0.52046 0.52046 -0.00000 0.00000  -0.00000 292 VAL   G CG2 
4888  N N   . THR   C  293 ? 0.35751 0.35751 0.35751 0.00000  0.00000  -0.00000 293 THR   G N   
4889  C CA  . THR   C  293 ? 0.43843 0.43843 0.43843 0.00000  0.00000  0.00000  293 THR   G CA  
4890  C C   . THR   C  293 ? 0.78371 0.78371 0.78371 0.00000  0.00000  0.00000  293 THR   G C   
4891  O O   . THR   C  293 ? 0.62222 0.62222 0.62222 0.00000  0.00000  0.00000  293 THR   G O   
4892  C CB  . THR   C  293 ? 0.74963 0.74963 0.74963 0.00000  0.00000  0.00000  293 THR   G CB  
4893  O OG1 . THR   C  293 ? 0.47130 0.47130 0.47130 0.00000  0.00000  0.00000  293 THR   G OG1 
4894  C CG2 . THR   C  293 ? 0.35318 0.35318 0.35318 -0.00000 0.00000  0.00000  293 THR   G CG2 
4895  N N   . ALA   C  294 ? 0.48933 0.48933 0.48933 -0.00000 0.00000  0.00000  294 ALA   G N   
4896  C CA  . ALA   C  294 ? 0.40519 0.40519 0.40519 0.00000  0.00000  0.00000  294 ALA   G CA  
4897  C C   . ALA   C  294 ? 0.39820 0.39820 0.39820 0.00000  0.00000  0.00000  294 ALA   G C   
4898  O O   . ALA   C  294 ? 0.61953 0.61953 0.61953 -0.00000 0.00000  0.00000  294 ALA   G O   
4899  C CB  . ALA   C  294 ? 0.38427 0.38427 0.38427 0.00000  0.00000  0.00000  294 ALA   G CB  
4900  N N   . TYR   C  295 ? 0.34890 0.34890 0.34890 0.00000  0.00000  0.00000  295 TYR   G N   
4901  C CA  . TYR   C  295 ? 0.44321 0.44321 0.44321 0.00000  0.00000  0.00000  295 TYR   G CA  
4902  C C   . TYR   C  295 ? 0.41695 0.41695 0.41695 -0.00000 -0.00000 0.00000  295 TYR   G C   
4903  O O   . TYR   C  295 ? 0.37801 0.37801 0.37801 0.00000  0.00000  0.00000  295 TYR   G O   
4904  C CB  . TYR   C  295 ? 0.10392 0.10392 0.10392 0.00000  0.00000  0.00000  295 TYR   G CB  
4905  C CG  . TYR   C  295 ? 0.48127 0.48127 0.48127 -0.00000 -0.00000 0.00000  295 TYR   G CG  
4906  C CD1 . TYR   C  295 ? 0.33251 0.33251 0.33251 -0.00000 0.00000  0.00000  295 TYR   G CD1 
4907  C CD2 . TYR   C  295 ? 0.28012 0.28012 0.28012 0.00000  0.00000  0.00000  295 TYR   G CD2 
4908  C CE1 . TYR   C  295 ? 0.24256 0.24256 0.24256 -0.00000 0.00000  0.00000  295 TYR   G CE1 
4909  C CE2 . TYR   C  295 ? 0.21752 0.21752 0.21752 0.00000  -0.00000 0.00000  295 TYR   G CE2 
4910  C CZ  . TYR   C  295 ? 0.39848 0.39848 0.39848 0.00000  0.00000  0.00000  295 TYR   G CZ  
4911  O OH  . TYR   C  295 ? 0.28458 0.28458 0.28458 0.00000  0.00000  0.00000  295 TYR   G OH  
4912  N N   . HIS   C  296 ? 0.39678 0.39678 0.39678 -0.00000 0.00000  0.00000  296 HIS   G N   
4913  C CA  . HIS   C  296 ? 0.50099 0.50099 0.50099 0.00000  0.00000  0.00000  296 HIS   G CA  
4914  C C   . HIS   C  296 ? 0.30581 0.30581 0.30581 0.00000  0.00000  0.00000  296 HIS   G C   
4915  O O   . HIS   C  296 ? 0.38054 0.38054 0.38054 0.00000  0.00000  0.00000  296 HIS   G O   
4916  C CB  . HIS   C  296 ? 0.36151 0.36151 0.36151 -0.00000 0.00000  0.00000  296 HIS   G CB  
4917  C CG  . HIS   C  296 ? 0.48682 0.48682 0.48682 0.00000  0.00000  0.00000  296 HIS   G CG  
4918  N ND1 . HIS   C  296 ? 0.58581 0.58581 0.58581 0.00000  0.00000  0.00000  296 HIS   G ND1 
4919  C CD2 . HIS   C  296 ? 0.47981 0.47981 0.47981 0.00000  0.00000  0.00000  296 HIS   G CD2 
4920  C CE1 . HIS   C  296 ? 0.48490 0.48490 0.48490 -0.00000 0.00000  0.00000  296 HIS   G CE1 
4921  N NE2 . HIS   C  296 ? 0.66102 0.66102 0.66102 0.00000  0.00000  0.00000  296 HIS   G NE2 
4922  N N   . ARG   C  297 ? 0.31631 0.31631 0.31631 -0.00000 0.00000  0.00000  297 ARG   G N   
4923  C CA  . ARG   C  297 ? 0.25836 0.25836 0.25836 0.00000  0.00000  0.00000  297 ARG   G CA  
4924  C C   . ARG   C  297 ? 0.47338 0.47338 0.47338 -0.00000 0.00000  0.00000  297 ARG   G C   
4925  O O   . ARG   C  297 ? 0.34225 0.34225 0.34225 0.00000  0.00000  0.00000  297 ARG   G O   
4926  C CB  . ARG   C  297 ? 0.30752 0.30752 0.30752 0.00000  0.00000  0.00000  297 ARG   G CB  
4927  C CG  . ARG   C  297 ? 0.37109 0.37109 0.37109 0.00000  0.00000  0.00000  297 ARG   G CG  
4928  C CD  . ARG   C  297 ? 0.33137 0.33137 0.33137 0.00000  0.00000  0.00000  297 ARG   G CD  
4929  N NE  . ARG   C  297 ? 0.55310 0.55310 0.55310 0.00000  0.00000  0.00000  297 ARG   G NE  
4930  C CZ  . ARG   C  297 ? 0.45583 0.45583 0.45583 0.00000  0.00000  0.00000  297 ARG   G CZ  
4931  N NH1 . ARG   C  297 ? 0.56190 0.56190 0.56190 -0.00000 0.00000  0.00000  297 ARG   G NH1 
4932  N NH2 . ARG   C  297 ? 1.00901 1.00901 1.00901 0.00000  0.00000  -0.00000 297 ARG   G NH2 
4933  N N   . TRP   C  298 ? 0.36375 0.36375 0.36375 0.00000  0.00000  0.00000  298 TRP   G N   
4934  C CA  . TRP   C  298 ? 0.33650 0.33650 0.33650 -0.00000 0.00000  0.00000  298 TRP   G CA  
4935  C C   . TRP   C  298 ? 0.43681 0.43681 0.43681 0.00000  0.00000  0.00000  298 TRP   G C   
4936  O O   . TRP   C  298 ? 0.48795 0.48795 0.48795 0.00000  0.00000  0.00000  298 TRP   G O   
4937  C CB  . TRP   C  298 ? 0.26278 0.26278 0.26278 -0.00000 0.00000  0.00000  298 TRP   G CB  
4938  C CG  . TRP   C  298 ? 0.39869 0.39869 0.39869 0.00000  0.00000  0.00000  298 TRP   G CG  
4939  C CD1 . TRP   C  298 ? 0.33879 0.33879 0.33879 0.00000  0.00000  0.00000  298 TRP   G CD1 
4940  C CD2 . TRP   C  298 ? 0.26422 0.26422 0.26422 0.00000  0.00000  0.00000  298 TRP   G CD2 
4941  N NE1 . TRP   C  298 ? 0.22999 0.22999 0.22999 0.00000  0.00000  0.00000  298 TRP   G NE1 
4942  C CE2 . TRP   C  298 ? 0.30975 0.30975 0.30975 0.00000  0.00000  0.00000  298 TRP   G CE2 
4943  C CE3 . TRP   C  298 ? 0.17636 0.17636 0.17636 -0.00000 0.00000  0.00000  298 TRP   G CE3 
4944  C CZ2 . TRP   C  298 ? 0.37467 0.37467 0.37467 0.00000  0.00000  0.00000  298 TRP   G CZ2 
4945  C CZ3 . TRP   C  298 ? 0.45378 0.45378 0.45378 0.00000  -0.00000 0.00000  298 TRP   G CZ3 
4946  C CH2 . TRP   C  298 ? 0.34682 0.34682 0.34682 -0.00000 0.00000  0.00000  298 TRP   G CH2 
4947  N N   . HIS   C  299 ? 0.35289 0.35289 0.35289 0.00000  0.00000  0.00000  299 HIS   G N   
4948  C CA  . HIS   C  299 ? 0.46534 0.46534 0.46534 -0.00000 0.00000  0.00000  299 HIS   G CA  
4949  C C   . HIS   C  299 ? 0.34065 0.34065 0.34065 0.00000  0.00000  0.00000  299 HIS   G C   
4950  O O   . HIS   C  299 ? 0.36716 0.36716 0.36716 -0.00000 0.00000  0.00000  299 HIS   G O   
4951  C CB  . HIS   C  299 ? 0.20358 0.20358 0.20358 0.00000  0.00000  -0.00000 299 HIS   G CB  
4952  C CG  . HIS   C  299 ? 0.41785 0.41785 0.41785 -0.00000 0.00000  0.00000  299 HIS   G CG  
4953  N ND1 . HIS   C  299 ? 0.32976 0.32976 0.32976 0.00000  0.00000  0.00000  299 HIS   G ND1 
4954  C CD2 . HIS   C  299 ? 0.33359 0.33359 0.33359 -0.00000 0.00000  0.00000  299 HIS   G CD2 
4955  C CE1 . HIS   C  299 ? 0.50366 0.50366 0.50366 0.00000  0.00000  0.00000  299 HIS   G CE1 
4956  N NE2 . HIS   C  299 ? 0.35625 0.35625 0.35625 0.00000  0.00000  0.00000  299 HIS   G NE2 
4957  N N   . ALA   C  300 ? 0.29593 0.29593 0.29593 -0.00000 0.00000  0.00000  300 ALA   G N   
4958  C CA  . ALA   C  300 ? 0.35971 0.35971 0.35971 0.00000  0.00000  0.00000  300 ALA   G CA  
4959  C C   . ALA   C  300 ? 0.27086 0.27086 0.27086 0.00000  0.00000  0.00000  300 ALA   G C   
4960  O O   . ALA   C  300 ? 0.40005 0.40005 0.40005 0.00000  0.00000  0.00000  300 ALA   G O   
4961  C CB  . ALA   C  300 ? 0.21456 0.21456 0.21456 0.00000  0.00000  0.00000  300 ALA   G CB  
4962  N N   . PRO   C  301 ? 0.44925 0.44925 0.44925 -0.00000 0.00000  0.00000  301 PRO   G N   
4963  C CA  . PRO   C  301 ? 0.26992 0.26992 0.26992 0.00000  0.00000  0.00000  301 PRO   G CA  
4964  C C   . PRO   C  301 ? 0.53318 0.53318 0.53318 0.00000  0.00000  0.00000  301 PRO   G C   
4965  O O   . PRO   C  301 ? 0.33560 0.33560 0.33560 0.00000  0.00000  0.00000  301 PRO   G O   
4966  C CB  . PRO   C  301 ? 0.38261 0.38261 0.38261 0.00000  0.00000  0.00000  301 PRO   G CB  
4967  C CG  . PRO   C  301 ? 0.34778 0.34778 0.34778 0.00000  0.00000  0.00000  301 PRO   G CG  
4968  C CD  . PRO   C  301 ? 0.16173 0.16173 0.16173 0.00000  0.00000  0.00000  301 PRO   G CD  
4969  N N   . VAL   C  302 ? 0.23009 0.23009 0.23009 -0.00000 0.00000  0.00000  302 VAL   G N   
4970  C CA  . VAL   C  302 ? 0.54459 0.54459 0.54459 0.00000  0.00000  0.00000  302 VAL   G CA  
4971  C C   . VAL   C  302 ? 0.22053 0.22053 0.22053 0.00000  0.00000  0.00000  302 VAL   G C   
4972  O O   . VAL   C  302 ? 0.43168 0.43168 0.43168 0.00000  0.00000  0.00000  302 VAL   G O   
4973  C CB  . VAL   C  302 ? 0.21746 0.21746 0.21746 -0.00000 0.00000  0.00000  302 VAL   G CB  
4974  C CG1 . VAL   C  302 ? 0.52481 0.52481 0.52481 -0.00000 0.00000  0.00000  302 VAL   G CG1 
4975  C CG2 . VAL   C  302 ? 0.20084 0.20084 0.20084 0.00000  0.00000  0.00000  302 VAL   G CG2 
4976  N N   . ASN   C  303 ? 0.45056 0.45056 0.45056 -0.00000 0.00000  0.00000  303 ASN   G N   
4977  C CA  . ASN   C  303 ? 0.25896 0.25896 0.25896 -0.00000 0.00000  0.00000  303 ASN   G CA  
4978  C C   . ASN   C  303 ? 0.50343 0.50343 0.50343 0.00000  0.00000  0.00000  303 ASN   G C   
4979  O O   . ASN   C  303 ? 0.44646 0.44646 0.44646 0.00000  -0.00000 0.00000  303 ASN   G O   
4980  C CB  . ASN   C  303 ? 0.49741 0.49741 0.49741 -0.00000 0.00000  0.00000  303 ASN   G CB  
4981  C CG  . ASN   C  303 ? 0.40545 0.40545 0.40545 -0.00000 0.00000  0.00000  303 ASN   G CG  
4982  O OD1 . ASN   C  303 ? 0.46507 0.46507 0.46507 -0.00000 0.00000  0.00000  303 ASN   G OD1 
4983  N ND2 . ASN   C  303 ? 0.44041 0.44041 0.44041 0.00000  0.00000  0.00000  303 ASN   G ND2 
4984  N N   . GLY   C  304 ? 0.38846 0.38846 0.38846 -0.00000 0.00000  0.00000  304 GLY   G N   
4985  C CA  . GLY   C  304 ? 0.22093 0.22093 0.22093 0.00000  0.00000  0.00000  304 GLY   G CA  
4986  C C   . GLY   C  304 ? 0.43024 0.43024 0.43024 0.00000  0.00000  0.00000  304 GLY   G C   
4987  O O   . GLY   C  304 ? 0.46590 0.46590 0.46590 0.00000  0.00000  0.00000  304 GLY   G O   
4988  N N   . THR   C  305 ? 0.36801 0.36801 0.36801 0.00000  0.00000  0.00000  305 THR   G N   
4989  C CA  . THR   C  305 ? 0.38446 0.38446 0.38446 0.00000  0.00000  0.00000  305 THR   G CA  
4990  C C   . THR   C  305 ? 0.66224 0.66224 0.66224 0.00000  0.00000  0.00000  305 THR   G C   
4991  O O   . THR   C  305 ? 0.21736 0.21736 0.21736 0.00000  0.00000  0.00000  305 THR   G O   
4992  C CB  . THR   C  305 ? 0.25300 0.25300 0.25300 0.00000  0.00000  0.00000  305 THR   G CB  
4993  O OG1 . THR   C  305 ? 0.46921 0.46921 0.46921 -0.00000 -0.00000 0.00000  305 THR   G OG1 
4994  C CG2 . THR   C  305 ? 0.25030 0.25030 0.25030 -0.00000 0.00000  0.00000  305 THR   G CG2 
4995  N N   . ILE   C  306 ? 0.21529 0.21529 0.21529 0.00000  0.00000  0.00000  306 ILE   G N   
4996  C CA  . ILE   C  306 ? 0.37772 0.37772 0.37772 0.00000  -0.00000 0.00000  306 ILE   G CA  
4997  C C   . ILE   C  306 ? 0.38582 0.38582 0.38582 0.00000  0.00000  0.00000  306 ILE   G C   
4998  O O   . ILE   C  306 ? 0.42451 0.42451 0.42451 -0.00000 0.00000  0.00000  306 ILE   G O   
4999  C CB  . ILE   C  306 ? 0.33047 0.33047 0.33047 -0.00000 0.00000  0.00000  306 ILE   G CB  
5000  C CG1 . ILE   C  306 ? 0.17092 0.17092 0.17092 0.00000  0.00000  0.00000  306 ILE   G CG1 
5001  C CG2 . ILE   C  306 ? 0.27593 0.27593 0.27593 -0.00000 0.00000  0.00000  306 ILE   G CG2 
5002  C CD1 . ILE   C  306 ? 0.25651 0.25651 0.25651 0.00000  0.00000  0.00000  306 ILE   G CD1 
5003  N N   . VAL   C  307 ? 0.33930 0.33930 0.33930 -0.00000 0.00000  0.00000  307 VAL   G N   
5004  C CA  . VAL   C  307 ? 0.26186 0.26186 0.26186 0.00000  0.00000  0.00000  307 VAL   G CA  
5005  C C   . VAL   C  307 ? 0.37226 0.37226 0.37226 0.00000  0.00000  0.00000  307 VAL   G C   
5006  O O   . VAL   C  307 ? 0.35331 0.35331 0.35331 0.00000  0.00000  0.00000  307 VAL   G O   
5007  C CB  . VAL   C  307 ? 0.46352 0.46352 0.46352 0.00000  0.00000  0.00000  307 VAL   G CB  
5008  C CG1 . VAL   C  307 ? 0.13391 0.13391 0.13391 -0.00000 0.00000  0.00000  307 VAL   G CG1 
5009  C CG2 . VAL   C  307 ? 0.27413 0.27413 0.27413 0.00000  0.00000  0.00000  307 VAL   G CG2 
5010  N N   . LYS   C  308 ? 0.51945 0.51945 0.51945 0.00000  0.00000  0.00000  308 LYS   G N   
5011  C CA  . LYS   C  308 ? 0.40063 0.40063 0.40063 0.00000  0.00000  0.00000  308 LYS   G CA  
5012  C C   . LYS   C  308 ? 0.57191 0.57191 0.57191 0.00000  0.00000  0.00000  308 LYS   G C   
5013  O O   . LYS   C  308 ? 0.35876 0.35876 0.35876 0.00000  0.00000  0.00000  308 LYS   G O   
5014  C CB  . LYS   C  308 ? 0.36031 0.36031 0.36031 0.00000  0.00000  0.00000  308 LYS   G CB  
5015  C CG  . LYS   C  308 ? 0.25064 0.25064 0.25064 0.00000  -0.00000 0.00000  308 LYS   G CG  
5016  C CD  . LYS   C  308 ? 0.38815 0.38815 0.38815 0.00000  0.00000  0.00000  308 LYS   G CD  
5017  C CE  . LYS   C  308 ? 0.64074 0.64074 0.64074 0.00000  0.00000  0.00000  308 LYS   G CE  
5018  N NZ  . LYS   C  308 ? 0.78823 0.78823 0.78823 -0.00000 0.00000  0.00000  308 LYS   G NZ  
5019  N N   . ILE   C  309 ? 0.32892 0.32892 0.32892 -0.00000 0.00000  0.00000  309 ILE   G N   
5020  C CA  . ILE   C  309 ? 0.41857 0.41857 0.41857 0.00000  0.00000  0.00000  309 ILE   G CA  
5021  C C   . ILE   C  309 ? 0.32292 0.32292 0.32292 0.00000  0.00000  0.00000  309 ILE   G C   
5022  O O   . ILE   C  309 ? 0.43152 0.43152 0.43152 -0.00000 0.00000  0.00000  309 ILE   G O   
5023  C CB  . ILE   C  309 ? 0.22163 0.22163 0.22163 0.00000  0.00000  0.00000  309 ILE   G CB  
5024  C CG1 . ILE   C  309 ? 0.48367 0.48367 0.48367 -0.00000 0.00000  0.00000  309 ILE   G CG1 
5025  C CG2 . ILE   C  309 ? 0.25526 0.25526 0.25526 0.00000  0.00000  0.00000  309 ILE   G CG2 
5026  C CD1 . ILE   C  309 ? 0.23920 0.23920 0.23920 0.00000  0.00000  0.00000  309 ILE   G CD1 
5027  N N   . ILE   C  310 ? 0.33557 0.33557 0.33557 0.00000  0.00000  0.00000  310 ILE   G N   
5028  C CA  . ILE   C  310 ? 0.13138 0.13138 0.13138 0.00000  0.00000  0.00000  310 ILE   G CA  
5029  C C   . ILE   C  310 ? 0.35190 0.35190 0.35190 0.00000  0.00000  0.00000  310 ILE   G C   
5030  O O   . ILE   C  310 ? 0.26317 0.26317 0.26317 -0.00000 0.00000  0.00000  310 ILE   G O   
5031  C CB  . ILE   C  310 ? 0.35162 0.35162 0.35162 0.00000  0.00000  0.00000  310 ILE   G CB  
5032  C CG1 . ILE   C  310 ? 0.36543 0.36543 0.36543 0.00000  0.00000  0.00000  310 ILE   G CG1 
5033  C CG2 . ILE   C  310 ? 0.19249 0.19249 0.19249 -0.00000 0.00000  0.00000  310 ILE   G CG2 
5034  C CD1 . ILE   C  310 ? 0.42079 0.42079 0.42079 -0.00000 0.00000  0.00000  310 ILE   G CD1 
5035  N N   . ASN   C  311 ? 0.33027 0.33027 0.33027 -0.00000 0.00000  0.00000  311 ASN   G N   
5036  C CA  . ASN   C  311 ? 0.28989 0.28989 0.28989 0.00000  0.00000  0.00000  311 ASN   G CA  
5037  C C   . ASN   C  311 ? 0.15510 0.15510 0.15510 0.00000  0.00000  0.00000  311 ASN   G C   
5038  O O   . ASN   C  311 ? 0.49722 0.49722 0.49722 0.00000  0.00000  0.00000  311 ASN   G O   
5039  C CB  . ASN   C  311 ? 0.09681 0.09681 0.09681 0.00000  0.00000  0.00000  311 ASN   G CB  
5040  C CG  . ASN   C  311 ? 0.67590 0.67590 0.67590 -0.00000 0.00000  0.00000  311 ASN   G CG  
5041  O OD1 . ASN   C  311 ? 0.42248 0.42248 0.42248 0.00000  0.00000  0.00000  311 ASN   G OD1 
5042  N ND2 . ASN   C  311 ? 0.45039 0.45039 0.45039 0.00000  0.00000  0.00000  311 ASN   G ND2 
5043  N N   . VAL   C  312 ? 0.30960 0.30960 0.30960 -0.00000 0.00000  0.00000  312 VAL   G N   
5044  C CA  . VAL   C  312 ? 0.28991 0.28991 0.28991 0.00000  0.00000  0.00000  312 VAL   G CA  
5045  C C   . VAL   C  312 ? 0.27530 0.27530 0.27530 0.00000  0.00000  0.00000  312 VAL   G C   
5046  O O   . VAL   C  312 ? 0.59070 0.59070 0.59070 0.00000  0.00000  0.00000  312 VAL   G O   
5047  C CB  . VAL   C  312 ? 0.33508 0.33508 0.33508 0.00000  0.00000  0.00000  312 VAL   G CB  
5048  C CG1 . VAL   C  312 ? 0.16152 0.16152 0.16152 -0.00000 0.00000  0.00000  312 VAL   G CG1 
5049  C CG2 . VAL   C  312 ? 0.24257 0.24257 0.24257 0.00000  0.00000  0.00000  312 VAL   G CG2 
5050  N N   . PRO   C  313 ? 0.45334 0.45334 0.45334 0.00000  0.00000  0.00000  313 PRO   G N   
5051  C CA  . PRO   C  313 ? 0.39866 0.39866 0.39866 0.00000  0.00000  0.00000  313 PRO   G CA  
5052  C C   . PRO   C  313 ? 0.44527 0.44527 0.44527 -0.00000 0.00000  0.00000  313 PRO   G C   
5053  O O   . PRO   C  313 ? 0.38496 0.38496 0.38496 0.00000  0.00000  0.00000  313 PRO   G O   
5054  C CB  . PRO   C  313 ? 0.18385 0.18385 0.18385 0.00000  0.00000  0.00000  313 PRO   G CB  
5055  C CG  . PRO   C  313 ? 0.25792 0.25792 0.25792 0.00000  -0.00000 0.00000  313 PRO   G CG  
5056  C CD  . PRO   C  313 ? 0.20943 0.20943 0.20943 0.00000  0.00000  0.00000  313 PRO   G CD  
5057  N N   . GLY   C  314 ? 0.29738 0.29738 0.29738 -0.00000 0.00000  0.00000  314 GLY   G N   
5058  C CA  . GLY   C  314 ? 0.20190 0.20190 0.20190 0.00000  0.00000  0.00000  314 GLY   G CA  
5059  C C   . GLY   C  314 ? 0.41674 0.41674 0.41674 -0.00000 0.00000  0.00000  314 GLY   G C   
5060  O O   . GLY   C  314 ? 0.30593 0.30593 0.30593 -0.00000 0.00000  0.00000  314 GLY   G O   
5061  N N   . THR   C  315 ? 0.22783 0.22783 0.22783 -0.00000 0.00000  0.00000  315 THR   G N   
5062  C CA  . THR   C  315 ? 0.25761 0.25761 0.25761 0.00000  0.00000  0.00000  315 THR   G CA  
5063  C C   . THR   C  315 ? 0.36312 0.36312 0.36312 -0.00000 0.00000  0.00000  315 THR   G C   
5064  O O   . THR   C  315 ? 0.26412 0.26412 0.26412 0.00000  0.00000  0.00000  315 THR   G O   
5065  C CB  . THR   C  315 ? 0.25283 0.25283 0.25283 -0.00000 0.00000  0.00000  315 THR   G CB  
5066  O OG1 . THR   C  315 ? 0.17404 0.17404 0.17404 0.00000  0.00000  0.00000  315 THR   G OG1 
5067  C CG2 . THR   C  315 ? 0.13240 0.13240 0.13240 0.00000  0.00000  0.00000  315 THR   G CG2 
5068  N N   . TYR   C  316 ? 0.30276 0.30276 0.30276 0.00000  0.00000  0.00000  316 TYR   G N   
5069  C CA  . TYR   C  316 ? 0.29718 0.29718 0.29718 -0.00000 0.00000  0.00000  316 TYR   G CA  
5070  C C   . TYR   C  316 ? 0.23417 0.23417 0.23417 0.00000  0.00000  0.00000  316 TYR   G C   
5071  O O   . TYR   C  316 ? 0.35908 0.35908 0.35908 -0.00000 0.00000  0.00000  316 TYR   G O   
5072  C CB  . TYR   C  316 ? 0.23317 0.23317 0.23317 0.00000  0.00000  0.00000  316 TYR   G CB  
5073  C CG  . TYR   C  316 ? 0.36927 0.36927 0.36927 0.00000  0.00000  0.00000  316 TYR   G CG  
5074  C CD1 . TYR   C  316 ? 0.38674 0.38674 0.38674 -0.00000 0.00000  0.00000  316 TYR   G CD1 
5075  C CD2 . TYR   C  316 ? 0.29453 0.29453 0.29453 0.00000  0.00000  0.00000  316 TYR   G CD2 
5076  C CE1 . TYR   C  316 ? 0.28084 0.28084 0.28084 -0.00000 0.00000  0.00000  316 TYR   G CE1 
5077  C CE2 . TYR   C  316 ? 0.19559 0.19559 0.19559 0.00000  0.00000  0.00000  316 TYR   G CE2 
5078  C CZ  . TYR   C  316 ? 0.42083 0.42083 0.42083 0.00000  0.00000  0.00000  316 TYR   G CZ  
5079  O OH  . TYR   C  316 ? 0.31031 0.31031 0.31031 -0.00000 0.00000  0.00000  316 TYR   G OH  
5080  N N   . PHE   C  317 ? 0.45659 0.45659 0.45659 0.00000  0.00000  0.00000  317 PHE   G N   
5081  C CA  . PHE   C  317 ? 0.21911 0.21911 0.21911 -0.00000 0.00000  0.00000  317 PHE   G CA  
5082  C C   . PHE   C  317 ? 0.49357 0.49357 0.49357 -0.00000 0.00000  0.00000  317 PHE   G C   
5083  O O   . PHE   C  317 ? 0.34072 0.34072 0.34072 0.00000  0.00000  0.00000  317 PHE   G O   
5084  C CB  . PHE   C  317 ? 0.21758 0.21758 0.21758 -0.00000 0.00000  0.00000  317 PHE   G CB  
5085  C CG  . PHE   C  317 ? 0.47270 0.47270 0.47270 0.00000  0.00000  0.00000  317 PHE   G CG  
5086  C CD1 . PHE   C  317 ? 0.22772 0.22772 0.22772 0.00000  0.00000  0.00000  317 PHE   G CD1 
5087  C CD2 . PHE   C  317 ? 0.41904 0.41904 0.41904 0.00000  0.00000  0.00000  317 PHE   G CD2 
5088  C CE1 . PHE   C  317 ? 0.42161 0.42161 0.42161 -0.00000 0.00000  0.00000  317 PHE   G CE1 
5089  C CE2 . PHE   C  317 ? 0.32776 0.32776 0.32776 0.00000  0.00000  0.00000  317 PHE   G CE2 
5090  C CZ  . PHE   C  317 ? 0.34557 0.34557 0.34557 0.00000  0.00000  0.00000  317 PHE   G CZ  
5091  N N   . ALA   C  318 ? 0.28452 0.28452 0.28452 0.00000  0.00000  0.00000  318 ALA   G N   
5092  C CA  . ALA   C  318 ? 0.24495 0.24495 0.24495 -0.00000 0.00000  0.00000  318 ALA   G CA  
5093  C C   . ALA   C  318 ? 0.30594 0.30594 0.30594 -0.00000 0.00000  0.00000  318 ALA   G C   
5094  O O   . ALA   C  318 ? 0.36822 0.36822 0.36822 -0.00000 0.00000  0.00000  318 ALA   G O   
5095  C CB  . ALA   C  318 ? 0.16291 0.16291 0.16291 -0.00000 0.00000  0.00000  318 ALA   G CB  
5096  N N   . GLN   C  319 ? 0.32389 0.32389 0.32389 -0.00000 0.00000  0.00000  319 GLN   G N   
5097  C CA  . GLN   C  319 ? 0.27932 0.27932 0.27932 0.00000  0.00000  0.00000  319 GLN   G CA  
5098  C C   . GLN   C  319 ? 0.25520 0.25520 0.25520 0.00000  0.00000  -0.00000 319 GLN   G C   
5099  O O   . GLN   C  319 ? 0.43597 0.43597 0.43597 0.00000  0.00000  0.00000  319 GLN   G O   
5100  C CB  . GLN   C  319 ? 0.27281 0.27281 0.27281 0.00000  0.00000  0.00000  319 GLN   G CB  
5101  C CG  . GLN   C  319 ? 0.37543 0.37543 0.37543 0.00000  0.00000  0.00000  319 GLN   G CG  
5102  C CD  . GLN   C  319 ? 0.23627 0.23627 0.23627 0.00000  0.00000  0.00000  319 GLN   G CD  
5103  O OE1 . GLN   C  319 ? 0.53163 0.53163 0.53163 0.00000  0.00000  0.00000  319 GLN   G OE1 
5104  N NE2 . GLN   C  319 ? 0.34782 0.34782 0.34782 0.00000  0.00000  0.00000  319 GLN   G NE2 
5105  N N   . ALA   C  320 ? 0.34421 0.34421 0.34421 -0.00000 0.00000  0.00000  320 ALA   G N   
5106  C CA  . ALA   C  320 ? 0.35365 0.35365 0.35365 -0.00000 0.00000  0.00000  320 ALA   G CA  
5107  C C   . ALA   C  320 ? 0.35039 0.35039 0.35039 0.00000  0.00000  0.00000  320 ALA   G C   
5108  O O   . ALA   C  320 ? 0.36987 0.36987 0.36987 0.00000  0.00000  0.00000  320 ALA   G O   
5109  C CB  . ALA   C  320 ? 0.14774 0.14774 0.14774 -0.00000 0.00000  0.00000  320 ALA   G CB  
5110  N N   . PRO   C  321 ? 0.51551 0.51551 0.51551 0.00000  0.00000  0.00000  321 PRO   G N   
5111  C CA  . PRO   C  321 ? 0.33691 0.33691 0.33691 -0.00000 0.00000  0.00000  321 PRO   G CA  
5112  C C   . PRO   C  321 ? 0.40892 0.40892 0.40892 0.00000  0.00000  0.00000  321 PRO   G C   
5113  O O   . PRO   C  321 ? 0.46929 0.46929 0.46929 0.00000  0.00000  0.00000  321 PRO   G O   
5114  C CB  . PRO   C  321 ? 0.25075 0.25075 0.25075 -0.00000 0.00000  0.00000  321 PRO   G CB  
5115  C CG  . PRO   C  321 ? 0.51874 0.51874 0.51874 0.00000  0.00000  0.00000  321 PRO   G CG  
5116  C CD  . PRO   C  321 ? 0.29444 0.29444 0.29444 0.00000  0.00000  0.00000  321 PRO   G CD  
5117  N N   . SER   C  322 ? 0.47909 0.47909 0.47909 0.00000  0.00000  0.00000  322 SER   G N   
5118  C CA  . SER   C  322 ? 0.47253 0.47253 0.47253 0.00000  0.00000  0.00000  322 SER   G CA  
5119  C C   . SER   C  322 ? 0.46751 0.46751 0.46751 0.00000  0.00000  0.00000  322 SER   G C   
5120  O O   . SER   C  322 ? 0.71296 0.71296 0.71296 0.00000  0.00000  0.00000  322 SER   G O   
5121  C CB  . SER   C  322 ? 0.35936 0.35936 0.35936 0.00000  0.00000  0.00000  322 SER   G CB  
5122  O OG  . SER   C  322 ? 0.67715 0.67715 0.67715 0.00000  0.00000  0.00000  322 SER   G OG  
5123  N N   . THR   C  323 ? 0.57173 0.57173 0.57173 0.00000  0.00000  0.00000  323 THR   G N   
5124  C CA  . THR   C  323 ? 0.34812 0.34812 0.34812 0.00000  0.00000  0.00000  323 THR   G CA  
5125  C C   . THR   C  323 ? 0.54411 0.54411 0.54411 0.00000  -0.00000 0.00000  323 THR   G C   
5126  O O   . THR   C  323 ? 0.32768 0.32768 0.32768 0.00000  0.00000  0.00000  323 THR   G O   
5127  C CB  . THR   C  323 ? 0.43341 0.43341 0.43341 0.00000  0.00000  0.00000  323 THR   G CB  
5128  O OG1 . THR   C  323 ? 0.45286 0.45286 0.45286 0.00000  0.00000  0.00000  323 THR   G OG1 
5129  C CG2 . THR   C  323 ? 0.20481 0.20481 0.20481 -0.00000 0.00000  0.00000  323 THR   G CG2 
5130  N N   . ILE   C  324 ? 0.41837 0.41837 0.41837 0.00000  0.00000  0.00000  324 ILE   G N   
5131  C CA  . ILE   C  324 ? 0.44048 0.44048 0.44048 0.00000  0.00000  0.00000  324 ILE   G CA  
5132  C C   . ILE   C  324 ? 0.67541 0.67541 0.67541 0.00000  0.00000  0.00000  324 ILE   G C   
5133  O O   . ILE   C  324 ? 0.58258 0.58258 0.58258 0.00000  0.00000  0.00000  324 ILE   G O   
5134  C CB  . ILE   C  324 ? 0.28861 0.28861 0.28861 0.00000  -0.00000 0.00000  324 ILE   G CB  
5135  C CG1 . ILE   C  324 ? 0.45805 0.45805 0.45805 0.00000  0.00000  0.00000  324 ILE   G CG1 
5136  C CG2 . ILE   C  324 ? 0.32082 0.32082 0.32082 0.00000  0.00000  0.00000  324 ILE   G CG2 
5137  C CD1 . ILE   C  324 ? 0.37577 0.37577 0.37577 0.00000  0.00000  0.00000  324 ILE   G CD1 
5138  N N   . GLY   C  325 ? 0.44695 0.44695 0.44695 -0.00000 0.00000  0.00000  325 GLY   G N   
5139  C CA  . GLY   C  325 ? 0.38640 0.38640 0.38640 -0.00000 0.00000  0.00000  325 GLY   G CA  
5140  C C   . GLY   C  325 ? 0.50078 0.50078 0.50078 -0.00000 0.00000  0.00000  325 GLY   G C   
5141  O O   . GLY   C  325 ? 0.56628 0.56628 0.56628 -0.00000 0.00000  0.00000  325 GLY   G O   
5142  N N   . ASP   C  326 ? 0.43071 0.43071 0.43071 -0.00000 0.00000  0.00000  326 ASP   G N   
5143  C CA  . ASP   C  326 ? 0.52195 0.52195 0.52195 0.00000  -0.00000 0.00000  326 ASP   G CA  
5144  C C   . ASP   C  326 ? 0.41018 0.41018 0.41018 -0.00000 0.00000  0.00000  326 ASP   G C   
5145  O O   . ASP   C  326 ? 0.54149 0.54149 0.54149 -0.00000 0.00000  0.00000  326 ASP   G O   
5146  C CB  . ASP   C  326 ? 0.29945 0.29945 0.29945 0.00000  0.00000  0.00000  326 ASP   G CB  
5147  C CG  . ASP   C  326 ? 0.76392 0.76392 0.76392 -0.00000 0.00000  0.00000  326 ASP   G CG  
5148  O OD1 . ASP   C  326 ? 0.58155 0.58155 0.58155 0.00000  0.00000  0.00000  326 ASP   G OD1 
5149  O OD2 . ASP   C  326 ? 0.61440 0.61440 0.61440 0.00000  0.00000  0.00000  326 ASP   G OD2 
5150  N N   . PRO   C  327 ? 0.64856 0.64856 0.64856 0.00000  0.00000  0.00000  327 PRO   G N   
5151  C CA  . PRO   C  327 ? 0.46437 0.46437 0.46437 -0.00000 0.00000  0.00000  327 PRO   G CA  
5152  C C   . PRO   C  327 ? 0.39748 0.39748 0.39748 -0.00000 0.00000  -0.00000 327 PRO   G C   
5153  O O   . PRO   C  327 ? 0.56191 0.56191 0.56191 0.00000  0.00000  0.00000  327 PRO   G O   
5154  C CB  . PRO   C  327 ? 0.20969 0.20969 0.20969 0.00000  0.00000  0.00000  327 PRO   G CB  
5155  C CG  . PRO   C  327 ? 0.39547 0.39547 0.39547 -0.00000 0.00000  0.00000  327 PRO   G CG  
5156  C CD  . PRO   C  327 ? 0.43239 0.43239 0.43239 -0.00000 0.00000  0.00000  327 PRO   G CD  
5157  N N   . ILE   C  328 ? 0.42349 0.42349 0.42349 0.00000  0.00000  0.00000  328 ILE   G N   
5158  C CA  . ILE   C  328 ? 0.42094 0.42094 0.42094 0.00000  0.00000  0.00000  328 ILE   G CA  
5159  C C   . ILE   C  328 ? 0.45002 0.45002 0.45002 -0.00000 0.00000  0.00000  328 ILE   G C   
5160  O O   . ILE   C  328 ? 0.56452 0.56452 0.56452 0.00000  -0.00000 -0.00000 328 ILE   G O   
5161  C CB  . ILE   C  328 ? 0.48712 0.48712 0.48712 -0.00000 0.00000  0.00000  328 ILE   G CB  
5162  C CG1 . ILE   C  328 ? 0.32825 0.32825 0.32825 0.00000  0.00000  0.00000  328 ILE   G CG1 
5163  C CG2 . ILE   C  328 ? 0.35010 0.35010 0.35010 0.00000  0.00000  0.00000  328 ILE   G CG2 
5164  C CD1 . ILE   C  328 ? 0.27772 0.27772 0.27772 -0.00000 0.00000  0.00000  328 ILE   G CD1 
5165  N N   . PRO   C  329 ? 0.56593 0.56593 0.56593 0.00000  0.00000  0.00000  329 PRO   G N   
5166  C CA  . PRO   C  329 ? 0.38193 0.38193 0.38193 -0.00000 0.00000  0.00000  329 PRO   G CA  
5167  C C   . PRO   C  329 ? 0.41046 0.41046 0.41046 0.00000  0.00000  0.00000  329 PRO   G C   
5168  O O   . PRO   C  329 ? 0.82019 0.82019 0.82019 -0.00000 0.00000  0.00000  329 PRO   G O   
5169  C CB  . PRO   C  329 ? 0.21552 0.21552 0.21552 0.00000  0.00000  -0.00000 329 PRO   G CB  
5170  C CG  . PRO   C  329 ? 0.35114 0.35114 0.35114 -0.00000 0.00000  0.00000  329 PRO   G CG  
5171  C CD  . PRO   C  329 ? 0.41309 0.41309 0.41309 -0.00000 0.00000  0.00000  329 PRO   G CD  
5172  N N   . ASP   C  330 ? 0.72300 0.72300 0.72300 -0.00000 0.00000  0.00000  330 ASP   G N   
5173  C CA  . ASP   C  330 ? 0.85057 0.85057 0.85057 -0.00000 0.00000  0.00000  330 ASP   G CA  
5174  C C   . ASP   C  330 ? 0.58071 0.58071 0.58071 0.00000  0.00000  0.00000  330 ASP   G C   
5175  O O   . ASP   C  330 ? 0.94452 0.94452 0.94452 0.00000  0.00000  0.00000  330 ASP   G O   
5176  C CB  . ASP   C  330 ? 0.48624 0.48624 0.48624 -0.00000 0.00000  0.00000  330 ASP   G CB  
5177  C CG  . ASP   C  330 ? 0.77468 0.77468 0.77468 0.00000  0.00000  0.00000  330 ASP   G CG  
5178  O OD1 . ASP   C  330 ? 1.49015 1.49015 1.49015 -0.00000 0.00000  0.00000  330 ASP   G OD1 
5179  O OD2 . ASP   C  330 ? 1.06604 1.06604 1.06604 -0.00000 0.00000  0.00000  330 ASP   G OD2 
5180  N N   . ASN   C  331 ? 0.83084 0.83084 0.83084 0.00000  0.00000  0.00000  331 ASN   G N   
5181  C CA  . ASN   C  331 ? 0.83243 0.83243 0.83243 0.00000  0.00000  0.00000  331 ASN   G CA  
5182  C C   . ASN   C  331 ? 0.61292 0.61292 0.61292 0.00000  0.00000  0.00000  331 ASN   G C   
5183  O O   . ASN   C  331 ? 1.16651 1.16651 1.16651 -0.00000 0.00000  0.00000  331 ASN   G O   
5184  C CB  . ASN   C  331 ? 0.55284 0.55284 0.55284 -0.00000 0.00000  0.00000  331 ASN   G CB  
5185  C CG  . ASN   C  331 ? 0.69331 0.69331 0.69331 0.00000  0.00000  0.00000  331 ASN   G CG  
5186  O OD1 . ASN   C  331 ? 1.57370 1.57370 1.57370 0.00000  0.00000  0.00000  331 ASN   G OD1 
5187  N ND2 . ASN   C  331 ? 0.74612 0.74612 0.74612 -0.00000 0.00000  0.00000  331 ASN   G ND2 
5188  N N   . ASP   C  332 ? 1.50106 1.50106 1.50106 0.00000  0.00000  0.00000  332 ASP   G N   
5189  C CA  . ASP   C  332 ? 0.24275 0.24275 0.24275 0.00000  0.00000  0.00000  332 ASP   G CA  
5190  C C   . ASP   C  332 ? 0.95962 0.95962 0.95962 -0.00000 0.00000  0.00000  332 ASP   G C   
5191  O O   . ASP   C  332 ? 0.72277 0.72277 0.72277 0.00000  0.00000  0.00000  332 ASP   G O   
5192  C CB  . ASP   C  332 ? 1.05488 1.05488 1.05488 0.00000  -0.00000 0.00000  332 ASP   G CB  
5193  C CG  . ASP   C  332 ? 1.74772 1.74772 1.74772 0.00000  0.00000  0.00000  332 ASP   G CG  
5194  O OD1 . ASP   C  332 ? 1.82504 1.82504 1.82504 0.00000  0.00000  0.00000  332 ASP   G OD1 
5195  O OD2 . ASP   C  332 ? 1.51966 1.51966 1.51966 -0.00000 0.00000  0.00000  332 ASP   G OD2 
5196  N N   . TYR   C  333 ? 0.87729 0.87729 0.87729 -0.00000 0.00000  0.00000  333 TYR   G N   
5197  C CA  . TYR   C  333 ? 0.88650 0.88650 0.88650 -0.00000 0.00000  0.00000  333 TYR   G CA  
5198  C C   . TYR   C  333 ? 1.08176 1.08176 1.08176 0.00000  0.00000  0.00000  333 TYR   G C   
5199  O O   . TYR   C  333 ? 1.05532 1.05532 1.05532 -0.00000 -0.00000 0.00000  333 TYR   G O   
5200  C CB  . TYR   C  333 ? 0.16180 0.16180 0.16180 0.00000  0.00000  0.00000  333 TYR   G CB  
5201  C CG  . TYR   C  333 ? 1.14498 1.14498 1.14498 0.00000  0.00000  0.00000  333 TYR   G CG  
5202  C CD1 . TYR   C  333 ? 0.54759 0.54759 0.54759 -0.00000 0.00000  0.00000  333 TYR   G CD1 
5203  C CD2 . TYR   C  333 ? 0.67196 0.67196 0.67196 0.00000  0.00000  0.00000  333 TYR   G CD2 
5204  C CE1 . TYR   C  333 ? 0.82894 0.82894 0.82894 0.00000  -0.00000 0.00000  333 TYR   G CE1 
5205  C CE2 . TYR   C  333 ? 0.78141 0.78141 0.78141 0.00000  0.00000  0.00000  333 TYR   G CE2 
5206  C CZ  . TYR   C  333 ? 1.24662 1.24662 1.24662 -0.00000 0.00000  0.00000  333 TYR   G CZ  
5207  O OH  . TYR   C  333 ? 0.22320 0.22320 0.22320 0.00000  0.00000  0.00000  333 TYR   G OH  
5208  N N   . ASP   C  334 ? 0.81242 0.81242 0.81242 0.00000  0.00000  0.00000  334 ASP   G N   
5209  C CA  . ASP   C  334 ? 0.78804 0.78804 0.78804 -0.00000 0.00000  0.00000  334 ASP   G CA  
5210  C C   . ASP   C  334 ? 0.90760 0.90760 0.90760 -0.00000 0.00000  0.00000  334 ASP   G C   
5211  O O   . ASP   C  334 ? 0.47354 0.47354 0.47354 0.00000  0.00000  0.00000  334 ASP   G O   
5212  C CB  . ASP   C  334 ? 1.15282 1.15282 1.15282 0.00000  0.00000  -0.00000 334 ASP   G CB  
5213  C CG  . ASP   C  334 ? 1.33800 1.33800 1.33800 -0.00000 0.00000  0.00000  334 ASP   G CG  
5214  O OD1 . ASP   C  334 ? 0.78334 0.78334 0.78334 0.00000  0.00000  0.00000  334 ASP   G OD1 
5215  O OD2 . ASP   C  334 ? 0.92676 0.92676 0.92676 0.00000  0.00000  0.00000  334 ASP   G OD2 
5216  N N   . PRO   C  335 ? 0.78171 0.78171 0.78171 0.00000  0.00000  0.00000  335 PRO   G N   
5217  C CA  . PRO   C  335 ? 0.52595 0.52595 0.52595 -0.00000 0.00000  -0.00000 335 PRO   G CA  
5218  C C   . PRO   C  335 ? 0.32368 0.32368 0.32368 0.00000  0.00000  0.00000  335 PRO   G C   
5219  O O   . PRO   C  335 ? 0.69023 0.69023 0.69023 -0.00000 0.00000  0.00000  335 PRO   G O   
5220  C CB  . PRO   C  335 ? 0.59914 0.59914 0.59914 -0.00000 0.00000  0.00000  335 PRO   G CB  
5221  C CG  . PRO   C  335 ? 0.76202 0.76202 0.76202 0.00000  0.00000  -0.00000 335 PRO   G CG  
5222  C CD  . PRO   C  335 ? 0.42736 0.42736 0.42736 0.00000  0.00000  0.00000  335 PRO   G CD  
5223  N N   . PRO   C  336 ? 0.69415 0.69415 0.69415 -0.00000 0.00000  0.00000  336 PRO   G N   
5224  C CA  . PRO   C  336 ? 0.24346 0.24346 0.24346 -0.00000 0.00000  0.00000  336 PRO   G CA  
5225  C C   . PRO   C  336 ? 1.08306 1.08306 1.08306 -0.00000 0.00000  0.00000  336 PRO   G C   
5226  O O   . PRO   C  336 ? 0.31133 0.31133 0.31133 0.00000  0.00000  0.00000  336 PRO   G O   
5227  C CB  . PRO   C  336 ? 0.48388 0.48388 0.48388 0.00000  0.00000  0.00000  336 PRO   G CB  
5228  C CG  . PRO   C  336 ? 0.44559 0.44559 0.44559 0.00000  0.00000  0.00000  336 PRO   G CG  
5229  C CD  . PRO   C  336 ? 0.24324 0.24324 0.24324 0.00000  0.00000  0.00000  336 PRO   G CD  
5230  N N   . PRO   C  337 ? 0.30891 0.30891 0.30891 0.00000  0.00000  0.00000  337 PRO   G N   
5231  C CA  . PRO   C  337 ? 0.50663 0.50663 0.50663 0.00000  0.00000  0.00000  337 PRO   G CA  
5232  C C   . PRO   C  337 ? 0.36166 0.36166 0.36166 0.00000  0.00000  0.00000  337 PRO   G C   
5233  O O   . PRO   C  337 ? 0.33438 0.33438 0.33438 0.00000  0.00000  0.00000  337 PRO   G O   
5234  C CB  . PRO   C  337 ? 0.33594 0.33594 0.33594 -0.00000 0.00000  0.00000  337 PRO   G CB  
5235  C CG  . PRO   C  337 ? 0.44211 0.44211 0.44211 0.00000  0.00000  0.00000  337 PRO   G CG  
5236  C CD  . PRO   C  337 ? 0.55198 0.55198 0.55198 0.00000  0.00000  0.00000  337 PRO   G CD  
5237  N N   . TYR   C  338 ? 0.34590 0.34590 0.34590 0.00000  0.00000  0.00000  338 TYR   G N   
5238  C CA  . TYR   C  338 ? 0.37864 0.37864 0.37864 -0.00000 0.00000  0.00000  338 TYR   G CA  
5239  C C   . TYR   C  338 ? 0.30027 0.30027 0.30027 -0.00000 0.00000  0.00000  338 TYR   G C   
5240  O O   . TYR   C  338 ? 0.31709 0.31709 0.31709 0.00000  0.00000  0.00000  338 TYR   G O   
5241  C CB  . TYR   C  338 ? 0.22055 0.22055 0.22055 -0.00000 0.00000  0.00000  338 TYR   G CB  
5242  C CG  . TYR   C  338 ? 0.38616 0.38616 0.38616 0.00000  0.00000  0.00000  338 TYR   G CG  
5243  C CD1 . TYR   C  338 ? 0.29406 0.29406 0.29406 0.00000  0.00000  0.00000  338 TYR   G CD1 
5244  C CD2 . TYR   C  338 ? 0.26671 0.26671 0.26671 0.00000  0.00000  0.00000  338 TYR   G CD2 
5245  C CE1 . TYR   C  338 ? 0.32841 0.32841 0.32841 0.00000  0.00000  0.00000  338 TYR   G CE1 
5246  C CE2 . TYR   C  338 ? 0.18956 0.18956 0.18956 0.00000  0.00000  0.00000  338 TYR   G CE2 
5247  C CZ  . TYR   C  338 ? 0.44596 0.44596 0.44596 -0.00000 0.00000  0.00000  338 TYR   G CZ  
5248  O OH  . TYR   C  338 ? 0.30093 0.30093 0.30093 -0.00000 0.00000  0.00000  338 TYR   G OH  
5249  N N   . LEU   C  339 ? 0.36974 0.36974 0.36974 0.00000  0.00000  0.00000  339 LEU   G N   
5250  C CA  . LEU   C  339 ? 0.25780 0.25780 0.25780 0.00000  0.00000  0.00000  339 LEU   G CA  
5251  C C   . LEU   C  339 ? 0.40959 0.40959 0.40959 0.00000  0.00000  0.00000  339 LEU   G C   
5252  O O   . LEU   C  339 ? 0.43102 0.43102 0.43102 0.00000  0.00000  0.00000  339 LEU   G O   
5253  C CB  . LEU   C  339 ? 0.26822 0.26822 0.26822 0.00000  0.00000  0.00000  339 LEU   G CB  
5254  C CG  . LEU   C  339 ? 0.54705 0.54705 0.54705 0.00000  0.00000  0.00000  339 LEU   G CG  
5255  C CD1 . LEU   C  339 ? 0.34220 0.34220 0.34220 0.00000  0.00000  0.00000  339 LEU   G CD1 
5256  C CD2 . LEU   C  339 ? 0.35935 0.35935 0.35935 0.00000  0.00000  0.00000  339 LEU   G CD2 
5257  N N   . LYS   C  340 ? 0.26724 0.26724 0.26724 0.00000  0.00000  0.00000  340 LYS   G N   
5258  C CA  . LYS   C  340 ? 0.51824 0.51824 0.51824 -0.00000 0.00000  0.00000  340 LYS   G CA  
5259  C C   . LYS   C  340 ? 0.29296 0.29296 0.29296 0.00000  0.00000  0.00000  340 LYS   G C   
5260  O O   . LYS   C  340 ? 0.37390 0.37390 0.37390 0.00000  0.00000  0.00000  340 LYS   G O   
5261  C CB  . LYS   C  340 ? 0.30119 0.30119 0.30119 -0.00000 0.00000  0.00000  340 LYS   G CB  
5262  N N   . SER   C  341 ? 0.40163 0.40163 0.40163 0.00000  0.00000  0.00000  341 SER   G N   
5263  C CA  . SER   C  341 ? 0.31494 0.31494 0.31494 -0.00000 0.00000  0.00000  341 SER   G CA  
5264  C C   . SER   C  341 ? 0.37681 0.37681 0.37681 -0.00000 0.00000  0.00000  341 SER   G C   
5265  O O   . SER   C  341 ? 0.51041 0.51041 0.51041 0.00000  -0.00000 0.00000  341 SER   G O   
5266  C CB  . SER   C  341 ? 0.39784 0.39784 0.39784 -0.00000 0.00000  0.00000  341 SER   G CB  
5267  O OG  . SER   C  341 ? 0.39482 0.39482 0.39482 0.00000  0.00000  0.00000  341 SER   G OG  
5268  N N   . LEU   C  342 ? 0.37971 0.37971 0.37971 0.00000  0.00000  0.00000  342 LEU   G N   
5269  C CA  . LEU   C  342 ? 0.52143 0.52143 0.52143 -0.00000 0.00000  0.00000  342 LEU   G CA  
5270  C C   . LEU   C  342 ? 0.37708 0.37708 0.37708 0.00000  0.00000  -0.00000 342 LEU   G C   
5271  O O   . LEU   C  342 ? 0.45201 0.45201 0.45201 0.00000  0.00000  0.00000  342 LEU   G O   
5272  C CB  . LEU   C  342 ? 0.30442 0.30442 0.30442 -0.00000 0.00000  0.00000  342 LEU   G CB  
5273  C CG  . LEU   C  342 ? 0.53576 0.53576 0.53576 -0.00000 0.00000  0.00000  342 LEU   G CG  
5274  C CD1 . LEU   C  342 ? 0.28470 0.28470 0.28470 0.00000  0.00000  0.00000  342 LEU   G CD1 
5275  C CD2 . LEU   C  342 ? 0.22911 0.22911 0.22911 0.00000  0.00000  0.00000  342 LEU   G CD2 
5276  N N   . VAL   C  343 ? 0.46763 0.46763 0.46763 -0.00000 0.00000  0.00000  343 VAL   G N   
5277  C CA  . VAL   C  343 ? 0.39536 0.39536 0.39536 0.00000  0.00000  0.00000  343 VAL   G CA  
5278  C C   . VAL   C  343 ? 0.55892 0.55892 0.55892 0.00000  0.00000  0.00000  343 VAL   G C   
5279  O O   . VAL   C  343 ? 0.36044 0.36044 0.36044 0.00000  0.00000  0.00000  343 VAL   G O   
5280  C CB  . VAL   C  343 ? 0.40652 0.40652 0.40652 -0.00000 0.00000  0.00000  343 VAL   G CB  
5281  C CG1 . VAL   C  343 ? 0.23193 0.23193 0.23193 -0.00000 0.00000  0.00000  343 VAL   G CG1 
5282  C CG2 . VAL   C  343 ? 0.32499 0.32499 0.32499 0.00000  0.00000  0.00000  343 VAL   G CG2 
5283  N N   . TYR   C  344 ? 0.23559 0.23559 0.23559 -0.00000 0.00000  0.00000  344 TYR   G N   
5284  C CA  . TYR   C  344 ? 0.45668 0.45668 0.45668 0.00000  0.00000  0.00000  344 TYR   G CA  
5285  C C   . TYR   C  344 ? 0.47609 0.47609 0.47609 -0.00000 -0.00000 -0.00000 344 TYR   G C   
5286  O O   . TYR   C  344 ? 0.34925 0.34925 0.34925 0.00000  0.00000  0.00000  344 TYR   G O   
5287  C CB  . TYR   C  344 ? 0.29077 0.29077 0.29077 -0.00000 0.00000  0.00000  344 TYR   G CB  
5288  C CG  . TYR   C  344 ? 0.54894 0.54894 0.54894 -0.00000 0.00000  0.00000  344 TYR   G CG  
5289  C CD1 . TYR   C  344 ? 0.33049 0.33049 0.33049 0.00000  0.00000  0.00000  344 TYR   G CD1 
5290  C CD2 . TYR   C  344 ? 0.44734 0.44734 0.44734 0.00000  0.00000  0.00000  344 TYR   G CD2 
5291  C CE1 . TYR   C  344 ? 0.33301 0.33301 0.33301 0.00000  0.00000  0.00000  344 TYR   G CE1 
5292  C CE2 . TYR   C  344 ? 0.32158 0.32158 0.32158 0.00000  0.00000  0.00000  344 TYR   G CE2 
5293  C CZ  . TYR   C  344 ? 0.55297 0.55297 0.55297 0.00000  -0.00000 0.00000  344 TYR   G CZ  
5294  O OH  . TYR   C  344 ? 0.49014 0.49014 0.49014 0.00000  0.00000  0.00000  344 TYR   G OH  
5295  N N   . PHE   C  345 ? 0.23760 0.23760 0.23760 -0.00000 0.00000  0.00000  345 PHE   G N   
5296  C CA  . PHE   C  345 ? 0.35219 0.35219 0.35219 0.00000  0.00000  0.00000  345 PHE   G CA  
5297  C C   . PHE   C  345 ? 0.41779 0.41779 0.41779 0.00000  0.00000  0.00000  345 PHE   G C   
5298  O O   . PHE   C  345 ? 0.37148 0.37148 0.37148 0.00000  0.00000  0.00000  345 PHE   G O   
5299  C CB  . PHE   C  345 ? 0.23189 0.23189 0.23189 0.00000  0.00000  0.00000  345 PHE   G CB  
5300  C CG  . PHE   C  345 ? 0.39913 0.39913 0.39913 0.00000  0.00000  0.00000  345 PHE   G CG  
5301  C CD1 . PHE   C  345 ? 0.46512 0.46512 0.46512 0.00000  0.00000  0.00000  345 PHE   G CD1 
5302  C CD2 . PHE   C  345 ? 0.31743 0.31743 0.31743 -0.00000 0.00000  0.00000  345 PHE   G CD2 
5303  C CE1 . PHE   C  345 ? 0.26479 0.26479 0.26479 0.00000  0.00000  0.00000  345 PHE   G CE1 
5304  C CE2 . PHE   C  345 ? 0.33601 0.33601 0.33601 -0.00000 0.00000  0.00000  345 PHE   G CE2 
5305  C CZ  . PHE   C  345 ? 0.36511 0.36511 0.36511 0.00000  0.00000  0.00000  345 PHE   G CZ  
5306  N N   . SER   C  346 ? 0.21033 0.21033 0.21033 0.00000  0.00000  0.00000  346 SER   G N   
5307  C CA  . SER   C  346 ? 0.49159 0.49159 0.49159 -0.00000 0.00000  0.00000  346 SER   G CA  
5308  C C   . SER   C  346 ? 0.33165 0.33165 0.33165 0.00000  0.00000  0.00000  346 SER   G C   
5309  O O   . SER   C  346 ? 0.33169 0.33169 0.33169 -0.00000 0.00000  0.00000  346 SER   G O   
5310  C CB  . SER   C  346 ? 0.32412 0.32412 0.32412 0.00000  0.00000  0.00000  346 SER   G CB  
5311  O OG  . SER   C  346 ? 0.28114 0.28114 0.28114 0.00000  0.00000  0.00000  346 SER   G OG  
5312  N N   . ASN   C  347 ? 0.43086 0.43086 0.43086 0.00000  0.00000  0.00000  347 ASN   G N   
5313  C CA  . ASN   C  347 ? 0.19150 0.19150 0.19150 0.00000  0.00000  0.00000  347 ASN   G CA  
5314  C C   . ASN   C  347 ? 0.40519 0.40519 0.40519 0.00000  0.00000  0.00000  347 ASN   G C   
5315  O O   . ASN   C  347 ? 0.40952 0.40952 0.40952 0.00000  0.00000  0.00000  347 ASN   G O   
5316  C CB  . ASN   C  347 ? 0.28674 0.28674 0.28674 0.00000  0.00000  0.00000  347 ASN   G CB  
5317  C CG  . ASN   C  347 ? 0.47856 0.47856 0.47856 -0.00000 0.00000  0.00000  347 ASN   G CG  
5318  O OD1 . ASN   C  347 ? 0.36629 0.36629 0.36629 -0.00000 0.00000  0.00000  347 ASN   G OD1 
5319  N ND2 . ASN   C  347 ? 0.24890 0.24890 0.24890 0.00000  -0.00000 0.00000  347 ASN   G ND2 
5320  N N   . ILE   C  348 ? 0.31373 0.31373 0.31373 0.00000  0.00000  0.00000  348 ILE   G N   
5321  C CA  . ILE   C  348 ? 0.22501 0.22501 0.22501 0.00000  0.00000  0.00000  348 ILE   G CA  
5322  C C   . ILE   C  348 ? 0.36534 0.36534 0.36534 0.00000  0.00000  0.00000  348 ILE   G C   
5323  O O   . ILE   C  348 ? 0.40930 0.40930 0.40930 0.00000  0.00000  0.00000  348 ILE   G O   
5324  C CB  . ILE   C  348 ? 0.33879 0.33879 0.33879 0.00000  0.00000  0.00000  348 ILE   G CB  
5325  C CG1 . ILE   C  348 ? 0.19353 0.19353 0.19353 0.00000  0.00000  0.00000  348 ILE   G CG1 
5326  C CG2 . ILE   C  348 ? 0.16702 0.16702 0.16702 -0.00000 0.00000  0.00000  348 ILE   G CG2 
5327  C CD1 . ILE   C  348 ? 0.47918 0.47918 0.47918 0.00000  0.00000  0.00000  348 ILE   G CD1 
5328  N N   . ALA   C  349 ? 0.31306 0.31306 0.31306 -0.00000 0.00000  0.00000  349 ALA   G N   
5329  C CA  . ALA   C  349 ? 0.31892 0.31892 0.31892 -0.00000 0.00000  0.00000  349 ALA   G CA  
5330  C C   . ALA   C  349 ? 0.35922 0.35922 0.35922 0.00000  -0.00000 -0.00000 349 ALA   G C   
5331  O O   . ALA   C  349 ? 0.42174 0.42174 0.42174 -0.00000 0.00000  0.00000  349 ALA   G O   
5332  C CB  . ALA   C  349 ? 0.13149 0.13149 0.13149 0.00000  0.00000  0.00000  349 ALA   G CB  
5333  N N   . ALA   C  350 ? 0.27516 0.27516 0.27516 0.00000  0.00000  0.00000  350 ALA   G N   
5334  C CA  . ALA   C  350 ? 0.30665 0.30665 0.30665 0.00000  0.00000  0.00000  350 ALA   G CA  
5335  C C   . ALA   C  350 ? 0.38187 0.38187 0.38187 0.00000  0.00000  0.00000  350 ALA   G C   
5336  O O   . ALA   C  350 ? 0.29992 0.29992 0.29992 -0.00000 0.00000  0.00000  350 ALA   G O   
5337  C CB  . ALA   C  350 ? 0.12774 0.12774 0.12774 0.00000  0.00000  0.00000  350 ALA   G CB  
5338  N N   . ARG   C  351 ? 0.22874 0.22874 0.22874 -0.00000 0.00000  0.00000  351 ARG   G N   
5339  C CA  . ARG   C  351 ? 0.35861 0.35861 0.35861 -0.00000 0.00000  -0.00000 351 ARG   G CA  
5340  C C   . ARG   C  351 ? 0.26156 0.26156 0.26156 0.00000  0.00000  0.00000  351 ARG   G C   
5341  O O   . ARG   C  351 ? 0.44185 0.44185 0.44185 0.00000  0.00000  0.00000  351 ARG   G O   
5342  C CB  . ARG   C  351 ? 0.17776 0.17776 0.17776 -0.00000 0.00000  0.00000  351 ARG   G CB  
5343  C CG  . ARG   C  351 ? 0.17783 0.17783 0.17783 -0.00000 0.00000  0.00000  351 ARG   G CG  
5344  C CD  . ARG   C  351 ? 0.27807 0.27807 0.27807 0.00000  0.00000  0.00000  351 ARG   G CD  
5345  N NE  . ARG   C  351 ? 0.29788 0.29788 0.29788 0.00000  0.00000  0.00000  351 ARG   G NE  
5346  C CZ  . ARG   C  351 ? 0.57046 0.57046 0.57046 0.00000  0.00000  0.00000  351 ARG   G CZ  
5347  N NH1 . ARG   C  351 ? 0.30131 0.30131 0.30131 0.00000  0.00000  0.00000  351 ARG   G NH1 
5348  N NH2 . ARG   C  351 ? 0.24263 0.24263 0.24263 0.00000  0.00000  0.00000  351 ARG   G NH2 
5349  N N   . GLN   C  352 ? 0.26698 0.26698 0.26698 0.00000  0.00000  0.00000  352 GLN   G N   
5350  C CA  . GLN   C  352 ? 0.18288 0.18288 0.18288 0.00000  0.00000  0.00000  352 GLN   G CA  
5351  C C   . GLN   C  352 ? 0.33709 0.33709 0.33709 0.00000  0.00000  0.00000  352 GLN   G C   
5352  O O   . GLN   C  352 ? 0.32289 0.32289 0.32289 0.00000  0.00000  0.00000  352 GLN   G O   
5353  C CB  . GLN   C  352 ? 0.31162 0.31162 0.31162 0.00000  0.00000  0.00000  352 GLN   G CB  
5354  C CG  . GLN   C  352 ? 0.24897 0.24897 0.24897 0.00000  0.00000  0.00000  352 GLN   G CG  
5355  C CD  . GLN   C  352 ? 0.35468 0.35468 0.35468 0.00000  0.00000  0.00000  352 GLN   G CD  
5356  O OE1 . GLN   C  352 ? 0.38076 0.38076 0.38076 0.00000  -0.00000 0.00000  352 GLN   G OE1 
5357  N NE2 . GLN   C  352 ? 0.21746 0.21746 0.21746 0.00000  0.00000  0.00000  352 GLN   G NE2 
5358  N N   . ILE   C  353 ? 0.29949 0.29949 0.29949 -0.00000 0.00000  0.00000  353 ILE   G N   
5359  C CA  . ILE   C  353 ? 0.33524 0.33524 0.33524 0.00000  0.00000  0.00000  353 ILE   G CA  
5360  C C   . ILE   C  353 ? 0.24680 0.24680 0.24680 0.00000  0.00000  0.00000  353 ILE   G C   
5361  O O   . ILE   C  353 ? 0.42526 0.42526 0.42526 0.00000  0.00000  0.00000  353 ILE   G O   
5362  C CB  . ILE   C  353 ? 0.30867 0.30867 0.30867 0.00000  0.00000  0.00000  353 ILE   G CB  
5363  C CG1 . ILE   C  353 ? 0.40039 0.40039 0.40039 -0.00000 0.00000  0.00000  353 ILE   G CG1 
5364  C CG2 . ILE   C  353 ? 0.19296 0.19296 0.19296 0.00000  0.00000  0.00000  353 ILE   G CG2 
5365  C CD1 . ILE   C  353 ? 0.14926 0.14926 0.14926 -0.00000 0.00000  0.00000  353 ILE   G CD1 
5366  N N   . MET   C  354 ? 0.25446 0.25446 0.25446 0.00000  0.00000  0.00000  354 MET   G N   
5367  C CA  . MET   C  354 ? 0.32168 0.32168 0.32168 0.00000  0.00000  0.00000  354 MET   G CA  
5368  C C   . MET   C  354 ? 0.38620 0.38620 0.38620 -0.00000 0.00000  0.00000  354 MET   G C   
5369  O O   . MET   C  354 ? 0.40482 0.40482 0.40482 0.00000  0.00000  0.00000  354 MET   G O   
5370  C CB  . MET   C  354 ? 0.18256 0.18256 0.18256 0.00000  -0.00000 0.00000  354 MET   G CB  
5371  C CG  . MET   C  354 ? 0.45920 0.45920 0.45920 0.00000  0.00000  0.00000  354 MET   G CG  
5372  S SD  . MET   C  354 ? 0.42423 0.42423 0.42423 -0.00000 0.00000  0.00000  354 MET   G SD  
5373  C CE  . MET   C  354 ? 0.40152 0.40152 0.40152 -0.00000 0.00000  0.00000  354 MET   G CE  
5374  N N   . PHE   C  355 ? 0.36517 0.36517 0.36517 0.00000  0.00000  0.00000  355 PHE   G N   
5375  C CA  . PHE   C  355 ? 0.38583 0.38583 0.38583 0.00000  -0.00000 0.00000  355 PHE   G CA  
5376  C C   . PHE   C  355 ? 0.36987 0.36987 0.36987 0.00000  0.00000  0.00000  355 PHE   G C   
5377  O O   . PHE   C  355 ? 0.42827 0.42827 0.42827 -0.00000 0.00000  0.00000  355 PHE   G O   
5378  C CB  . PHE   C  355 ? 0.43469 0.43469 0.43469 0.00000  0.00000  0.00000  355 PHE   G CB  
5379  C CG  . PHE   C  355 ? 0.45824 0.45824 0.45824 -0.00000 0.00000  0.00000  355 PHE   G CG  
5380  C CD1 . PHE   C  355 ? 0.29415 0.29415 0.29415 -0.00000 0.00000  0.00000  355 PHE   G CD1 
5381  C CD2 . PHE   C  355 ? 0.40426 0.40426 0.40426 -0.00000 0.00000  0.00000  355 PHE   G CD2 
5382  C CE1 . PHE   C  355 ? 0.45725 0.45725 0.45725 -0.00000 0.00000  0.00000  355 PHE   G CE1 
5383  C CE2 . PHE   C  355 ? 0.24170 0.24170 0.24170 0.00000  0.00000  0.00000  355 PHE   G CE2 
5384  C CZ  . PHE   C  355 ? 0.26144 0.26144 0.26144 0.00000  0.00000  0.00000  355 PHE   G CZ  
5385  N N   . ILE   C  356 ? 0.30837 0.30837 0.30837 0.00000  0.00000  0.00000  356 ILE   G N   
5386  C CA  . ILE   C  356 ? 0.35092 0.35092 0.35092 0.00000  0.00000  0.00000  356 ILE   G CA  
5387  C C   . ILE   C  356 ? 0.51481 0.51481 0.51481 0.00000  0.00000  0.00000  356 ILE   G C   
5388  O O   . ILE   C  356 ? 0.34687 0.34687 0.34687 0.00000  0.00000  0.00000  356 ILE   G O   
5389  C CB  . ILE   C  356 ? 0.27595 0.27595 0.27595 0.00000  0.00000  0.00000  356 ILE   G CB  
5390  C CG1 . ILE   C  356 ? 0.26709 0.26709 0.26709 0.00000  0.00000  0.00000  356 ILE   G CG1 
5391  C CG2 . ILE   C  356 ? 0.31444 0.31444 0.31444 0.00000  0.00000  0.00000  356 ILE   G CG2 
5392  C CD1 . ILE   C  356 ? 0.19243 0.19243 0.19243 0.00000  0.00000  -0.00000 356 ILE   G CD1 
5393  N N   . GLU   C  357 ? 0.21008 0.21008 0.21008 -0.00000 0.00000  0.00000  357 GLU   G N   
5394  C CA  . GLU   C  357 ? 0.39997 0.39997 0.39997 0.00000  -0.00000 0.00000  357 GLU   G CA  
5395  C C   . GLU   C  357 ? 0.37725 0.37725 0.37725 0.00000  0.00000  0.00000  357 GLU   G C   
5396  O O   . GLU   C  357 ? 0.36063 0.36063 0.36063 -0.00000 0.00000  0.00000  357 GLU   G O   
5397  C CB  . GLU   C  357 ? 0.27984 0.27984 0.27984 -0.00000 0.00000  0.00000  357 GLU   G CB  
5398  C CG  . GLU   C  357 ? 0.26439 0.26439 0.26439 0.00000  0.00000  0.00000  357 GLU   G CG  
5399  C CD  . GLU   C  357 ? 0.93945 0.93945 0.93945 0.00000  0.00000  0.00000  357 GLU   G CD  
5400  O OE1 . GLU   C  357 ? 0.71818 0.71818 0.71818 0.00000  0.00000  0.00000  357 GLU   G OE1 
5401  O OE2 . GLU   C  357 ? 0.55453 0.55453 0.55453 -0.00000 0.00000  0.00000  357 GLU   G OE2 
5402  N N   . ALA   C  358 ? 0.21059 0.21059 0.21059 0.00000  0.00000  0.00000  358 ALA   G N   
5403  C CA  . ALA   C  358 ? 0.44947 0.44947 0.44947 0.00000  0.00000  0.00000  358 ALA   G CA  
5404  C C   . ALA   C  358 ? 0.37890 0.37890 0.37890 -0.00000 0.00000  0.00000  358 ALA   G C   
5405  O O   . ALA   C  358 ? 0.70812 0.70812 0.70812 0.00000  0.00000  0.00000  358 ALA   G O   
5406  C CB  . ALA   C  358 ? 0.30560 0.30560 0.30560 0.00000  -0.00000 0.00000  358 ALA   G CB  
5407  N N   . ASP   C  359 ? 0.54801 0.54801 0.54801 0.00000  0.00000  0.00000  359 ASP   G N   
5408  C CA  . ASP   C  359 ? 0.48863 0.48863 0.48863 -0.00000 0.00000  0.00000  359 ASP   G CA  
5409  C C   . ASP   C  359 ? 0.26259 0.26259 0.26259 -0.00000 0.00000  0.00000  359 ASP   G C   
5410  O O   . ASP   C  359 ? 0.34825 0.34825 0.34825 0.00000  0.00000  0.00000  359 ASP   G O   
5411  C CB  . ASP   C  359 ? 0.22346 0.22346 0.22346 0.00000  0.00000  -0.00000 359 ASP   G CB  
5412  C CG  . ASP   C  359 ? 0.69573 0.69573 0.69573 0.00000  0.00000  0.00000  359 ASP   G CG  
5413  O OD1 . ASP   C  359 ? 0.44274 0.44274 0.44274 -0.00000 0.00000  0.00000  359 ASP   G OD1 
5414  O OD2 . ASP   C  359 ? 0.36308 0.36308 0.36308 -0.00000 0.00000  0.00000  359 ASP   G OD2 
5415  N N   . ASN   C  360 ? 0.33796 0.33796 0.33796 -0.00000 0.00000  0.00000  360 ASN   G N   
5416  C CA  . ASN   C  360 ? 0.22716 0.22716 0.22716 0.00000  0.00000  0.00000  360 ASN   G CA  
5417  C C   . ASN   C  360 ? 0.36604 0.36604 0.36604 0.00000  0.00000  0.00000  360 ASN   G C   
5418  O O   . ASN   C  360 ? 0.50121 0.50121 0.50121 -0.00000 0.00000  0.00000  360 ASN   G O   
5419  C CB  . ASN   C  360 ? 0.24338 0.24338 0.24338 0.00000  0.00000  0.00000  360 ASN   G CB  
5420  C CG  . ASN   C  360 ? 0.48131 0.48131 0.48131 -0.00000 0.00000  0.00000  360 ASN   G CG  
5421  O OD1 . ASN   C  360 ? 0.52063 0.52063 0.52063 0.00000  0.00000  0.00000  360 ASN   G OD1 
5422  N ND2 . ASN   C  360 ? 0.55683 0.55683 0.55683 0.00000  0.00000  0.00000  360 ASN   G ND2 
5423  N N   . LYS   C  361 ? 0.49069 0.49069 0.49069 -0.00000 0.00000  0.00000  361 LYS   G N   
5424  C CA  . LYS   C  361 ? 0.58909 0.58909 0.58909 -0.00000 0.00000  0.00000  361 LYS   G CA  
5425  C C   . LYS   C  361 ? 0.23848 0.23848 0.23848 0.00000  0.00000  0.00000  361 LYS   G C   
5426  O O   . LYS   C  361 ? 0.87659 0.87659 0.87659 0.00000  0.00000  0.00000  361 LYS   G O   
5427  C CB  . LYS   C  361 ? 0.29112 0.29112 0.29112 0.00000  0.00000  0.00000  361 LYS   G CB  
5428  C CG  . LYS   C  361 ? 0.33866 0.33866 0.33866 -0.00000 0.00000  0.00000  361 LYS   G CG  
5429  C CD  . LYS   C  361 ? 0.11110 0.11110 0.11110 -0.00000 0.00000  0.00000  361 LYS   G CD  
5430  C CE  . LYS   C  361 ? 1.15112 1.15112 1.15112 0.00000  0.00000  0.00000  361 LYS   G CE  
5431  N NZ  . LYS   C  361 ? 1.25372 1.25372 1.25372 0.00000  0.00000  0.00000  361 LYS   G NZ  
5432  N N   . GLU   C  362 ? 0.39609 0.39609 0.39609 0.00000  0.00000  0.00000  362 GLU   G N   
5433  C CA  . GLU   C  362 ? 0.33864 0.33864 0.33864 0.00000  0.00000  0.00000  362 GLU   G CA  
5434  C C   . GLU   C  362 ? 0.59552 0.59552 0.59552 0.00000  0.00000  0.00000  362 GLU   G C   
5435  O O   . GLU   C  362 ? 0.49752 0.49752 0.49752 -0.00000 0.00000  0.00000  362 GLU   G O   
5436  C CB  . GLU   C  362 ? 0.45084 0.45084 0.45084 0.00000  0.00000  0.00000  362 GLU   G CB  
5437  C CG  . GLU   C  362 ? 0.30250 0.30250 0.30250 0.00000  0.00000  0.00000  362 GLU   G CG  
5438  C CD  . GLU   C  362 ? 1.30575 1.30575 1.30575 0.00000  0.00000  0.00000  362 GLU   G CD  
5439  O OE1 . GLU   C  362 ? 1.28627 1.28627 1.28627 -0.00000 0.00000  0.00000  362 GLU   G OE1 
5440  O OE2 . GLU   C  362 ? 1.26061 1.26061 1.26061 0.00000  0.00000  0.00000  362 GLU   G OE2 
5441  N N   . ILE   C  363 ? 0.35793 0.35793 0.35793 -0.00000 0.00000  0.00000  363 ILE   G N   
5442  C CA  . ILE   C  363 ? 0.58549 0.58549 0.58549 -0.00000 0.00000  0.00000  363 ILE   G CA  
5443  C C   . ILE   C  363 ? 0.43974 0.43974 0.43974 0.00000  0.00000  -0.00000 363 ILE   G C   
5444  O O   . ILE   C  363 ? 0.54553 0.54553 0.54553 0.00000  0.00000  0.00000  363 ILE   G O   
5445  C CB  . ILE   C  363 ? 0.46184 0.46184 0.46184 0.00000  0.00000  0.00000  363 ILE   G CB  
5446  C CG1 . ILE   C  363 ? 0.38467 0.38467 0.38467 0.00000  0.00000  0.00000  363 ILE   G CG1 
5447  C CG2 . ILE   C  363 ? 0.20579 0.20579 0.20579 0.00000  0.00000  0.00000  363 ILE   G CG2 
5448  C CD1 . ILE   C  363 ? 0.42775 0.42775 0.42775 0.00000  0.00000  0.00000  363 ILE   G CD1 
5449  N N   . GLY   C  364 ? 0.37873 0.37873 0.37873 0.00000  0.00000  0.00000  364 GLY   G N   
5450  C CA  . GLY   C  364 ? 0.22543 0.22543 0.22543 0.00000  0.00000  0.00000  364 GLY   G CA  
5451  C C   . GLY   C  364 ? 0.79844 0.79844 0.79844 0.00000  0.00000  0.00000  364 GLY   G C   
5452  O O   . GLY   C  364 ? 0.34998 0.34998 0.34998 0.00000  0.00000  0.00000  364 GLY   G O   
5453  N N   . LEU   C  365 ? 0.52349 0.52349 0.52349 -0.00000 0.00000  0.00000  365 LEU   G N   
5454  C CA  . LEU   C  365 ? 0.23077 0.23077 0.23077 0.00000  0.00000  0.00000  365 LEU   G CA  
5455  C C   . LEU   C  365 ? 0.54304 0.54304 0.54304 0.00000  0.00000  0.00000  365 LEU   G C   
5456  O O   . LEU   C  365 ? 0.38220 0.38220 0.38220 0.00000  0.00000  0.00000  365 LEU   G O   
5457  C CB  . LEU   C  365 ? 0.40938 0.40938 0.40938 0.00000  0.00000  0.00000  365 LEU   G CB  
5458  C CG  . LEU   C  365 ? 0.45445 0.45445 0.45445 0.00000  0.00000  0.00000  365 LEU   G CG  
5459  C CD1 . LEU   C  365 ? 0.29278 0.29278 0.29278 0.00000  0.00000  0.00000  365 LEU   G CD1 
5460  C CD2 . LEU   C  365 ? 0.28058 0.28058 0.28058 0.00000  0.00000  0.00000  365 LEU   G CD2 
5461  N N   . ILE   C  366 ? 0.17129 0.17129 0.17129 0.00000  0.00000  0.00000  366 ILE   G N   
5462  C CA  . ILE   C  366 ? 0.35276 0.35276 0.35276 0.00000  0.00000  0.00000  366 ILE   G CA  
5463  C C   . ILE   C  366 ? 0.38205 0.38205 0.38205 0.00000  0.00000  0.00000  366 ILE   G C   
5464  O O   . ILE   C  366 ? 0.32536 0.32536 0.32536 -0.00000 0.00000  0.00000  366 ILE   G O   
5465  C CB  . ILE   C  366 ? 0.26869 0.26869 0.26869 0.00000  0.00000  0.00000  366 ILE   G CB  
5466  C CG1 . ILE   C  366 ? 0.31333 0.31333 0.31333 0.00000  0.00000  0.00000  366 ILE   G CG1 
5467  C CG2 . ILE   C  366 ? 0.16666 0.16666 0.16666 0.00000  -0.00000 0.00000  366 ILE   G CG2 
5468  C CD1 . ILE   C  366 ? 0.32309 0.32309 0.32309 0.00000  0.00000  0.00000  366 ILE   G CD1 
5469  N N   . PHE   C  367 ? 0.32687 0.32687 0.32687 -0.00000 0.00000  0.00000  367 PHE   G N   
5470  C CA  . PHE   C  367 ? 0.28847 0.28847 0.28847 0.00000  0.00000  0.00000  367 PHE   G CA  
5471  C C   . PHE   C  367 ? 0.40594 0.40594 0.40594 0.00000  0.00000  0.00000  367 PHE   G C   
5472  O O   . PHE   C  367 ? 0.34903 0.34903 0.34903 0.00000  0.00000  0.00000  367 PHE   G O   
5473  C CB  . PHE   C  367 ? 0.27540 0.27540 0.27540 0.00000  0.00000  0.00000  367 PHE   G CB  
5474  C CG  . PHE   C  367 ? 0.17415 0.17415 0.17415 0.00000  0.00000  0.00000  367 PHE   G CG  
5475  C CD1 . PHE   C  367 ? 0.38050 0.38050 0.38050 0.00000  0.00000  0.00000  367 PHE   G CD1 
5476  C CD2 . PHE   C  367 ? 0.31905 0.31905 0.31905 0.00000  0.00000  0.00000  367 PHE   G CD2 
5477  C CE1 . PHE   C  367 ? 0.17983 0.17983 0.17983 -0.00000 0.00000  0.00000  367 PHE   G CE1 
5478  C CE2 . PHE   C  367 ? 0.29450 0.29450 0.29450 0.00000  0.00000  0.00000  367 PHE   G CE2 
5479  C CZ  . PHE   C  367 ? 0.25299 0.25299 0.25299 0.00000  0.00000  0.00000  367 PHE   G CZ  
5480  N N   . LEU   C  368 ? 0.35972 0.35972 0.35972 0.00000  0.00000  0.00000  368 LEU   G N   
5481  C CA  . LEU   C  368 ? 0.24518 0.24518 0.24518 -0.00000 0.00000  0.00000  368 LEU   G CA  
5482  C C   . LEU   C  368 ? 0.25466 0.25466 0.25466 0.00000  0.00000  0.00000  368 LEU   G C   
5483  O O   . LEU   C  368 ? 0.36247 0.36247 0.36247 0.00000  0.00000  0.00000  368 LEU   G O   
5484  C CB  . LEU   C  368 ? 0.21560 0.21560 0.21560 0.00000  -0.00000 0.00000  368 LEU   G CB  
5485  C CG  . LEU   C  368 ? 0.34980 0.34980 0.34980 0.00000  0.00000  0.00000  368 LEU   G CG  
5486  C CD1 . LEU   C  368 ? 0.29637 0.29637 0.29637 -0.00000 0.00000  0.00000  368 LEU   G CD1 
5487  C CD2 . LEU   C  368 ? 0.31732 0.31732 0.31732 0.00000  0.00000  0.00000  368 LEU   G CD2 
5488  N N   . VAL   C  369 ? 0.25273 0.25273 0.25273 0.00000  0.00000  0.00000  369 VAL   G N   
5489  C CA  . VAL   C  369 ? 0.28236 0.28236 0.28236 0.00000  0.00000  0.00000  369 VAL   G CA  
5490  C C   . VAL   C  369 ? 0.25050 0.25050 0.25050 0.00000  0.00000  0.00000  369 VAL   G C   
5491  O O   . VAL   C  369 ? 0.37015 0.37015 0.37015 0.00000  0.00000  0.00000  369 VAL   G O   
5492  C CB  . VAL   C  369 ? 0.36129 0.36129 0.36129 0.00000  0.00000  0.00000  369 VAL   G CB  
5493  C CG1 . VAL   C  369 ? 0.23169 0.23169 0.23169 -0.00000 0.00000  0.00000  369 VAL   G CG1 
5494  C CG2 . VAL   C  369 ? 0.32534 0.32534 0.32534 -0.00000 0.00000  0.00000  369 VAL   G CG2 
5495  N N   . PHE   C  370 ? 0.36145 0.36145 0.36145 0.00000  0.00000  0.00000  370 PHE   G N   
5496  C CA  . PHE   C  370 ? 0.12898 0.12898 0.12898 0.00000  0.00000  0.00000  370 PHE   G CA  
5497  C C   . PHE   C  370 ? 0.30427 0.30427 0.30427 0.00000  0.00000  0.00000  370 PHE   G C   
5498  O O   . PHE   C  370 ? 0.28177 0.28177 0.28177 0.00000  0.00000  0.00000  370 PHE   G O   
5499  C CB  . PHE   C  370 ? 0.22376 0.22376 0.22376 0.00000  0.00000  0.00000  370 PHE   G CB  
5500  C CG  . PHE   C  370 ? 0.35051 0.35051 0.35051 0.00000  0.00000  0.00000  370 PHE   G CG  
5501  C CD1 . PHE   C  370 ? 0.23051 0.23051 0.23051 0.00000  0.00000  0.00000  370 PHE   G CD1 
5502  C CD2 . PHE   C  370 ? 0.41114 0.41114 0.41114 -0.00000 0.00000  0.00000  370 PHE   G CD2 
5503  C CE1 . PHE   C  370 ? 0.35917 0.35917 0.35917 0.00000  0.00000  0.00000  370 PHE   G CE1 
5504  C CE2 . PHE   C  370 ? 0.21334 0.21334 0.21334 0.00000  0.00000  0.00000  370 PHE   G CE2 
5505  C CZ  . PHE   C  370 ? 0.35276 0.35276 0.35276 0.00000  0.00000  0.00000  370 PHE   G CZ  
5506  N N   . ILE   C  371 ? 0.30205 0.30205 0.30205 -0.00000 0.00000  0.00000  371 ILE   G N   
5507  C CA  . ILE   C  371 ? 0.24858 0.24858 0.24858 0.00000  0.00000  0.00000  371 ILE   G CA  
5508  C C   . ILE   C  371 ? 0.26023 0.26023 0.26023 -0.00000 0.00000  0.00000  371 ILE   G C   
5509  O O   . ILE   C  371 ? 0.38571 0.38571 0.38571 0.00000  0.00000  -0.00000 371 ILE   G O   
5510  C CB  . ILE   C  371 ? 0.36403 0.36403 0.36403 0.00000  0.00000  0.00000  371 ILE   G CB  
5511  C CG1 . ILE   C  371 ? 0.23216 0.23216 0.23216 0.00000  0.00000  0.00000  371 ILE   G CG1 
5512  C CG2 . ILE   C  371 ? 0.18004 0.18004 0.18004 0.00000  0.00000  0.00000  371 ILE   G CG2 
5513  C CD1 . ILE   C  371 ? 0.20515 0.20515 0.20515 0.00000  -0.00000 0.00000  371 ILE   G CD1 
5514  N N   . GLY   C  372 ? 0.36183 0.36183 0.36183 0.00000  0.00000  -0.00000 372 GLY   G N   
5515  C CA  . GLY   C  372 ? 0.25161 0.25161 0.25161 0.00000  -0.00000 0.00000  372 GLY   G CA  
5516  C C   . GLY   C  372 ? 0.35709 0.35709 0.35709 0.00000  0.00000  0.00000  372 GLY   G C   
5517  O O   . GLY   C  372 ? 0.35927 0.35927 0.35927 -0.00000 0.00000  0.00000  372 GLY   G O   
5518  N N   . MET   C  373 ? 0.27841 0.27841 0.27841 -0.00000 0.00000  0.00000  373 MET   G N   
5519  C CA  . MET   C  373 ? 0.44351 0.44351 0.44351 0.00000  0.00000  0.00000  373 MET   G CA  
5520  C C   . MET   C  373 ? 0.41503 0.41503 0.41503 0.00000  0.00000  0.00000  373 MET   G C   
5521  O O   . MET   C  373 ? 0.35541 0.35541 0.35541 0.00000  0.00000  0.00000  373 MET   G O   
5522  C CB  . MET   C  373 ? 0.19025 0.19025 0.19025 0.00000  0.00000  0.00000  373 MET   G CB  
5523  C CG  . MET   C  373 ? 0.46666 0.46666 0.46666 0.00000  -0.00000 0.00000  373 MET   G CG  
5524  S SD  . MET   C  373 ? 0.38446 0.38446 0.38446 0.00000  0.00000  0.00000  373 MET   G SD  
5525  C CE  . MET   C  373 ? 0.07773 0.07773 0.07773 0.00000  0.00000  0.00000  373 MET   G CE  
5526  N N   . THR   C  374 ? 0.26018 0.26018 0.26018 -0.00000 0.00000  0.00000  374 THR   G N   
5527  C CA  . THR   C  374 ? 0.27755 0.27755 0.27755 -0.00000 0.00000  0.00000  374 THR   G CA  
5528  C C   . THR   C  374 ? 0.23840 0.23840 0.23840 -0.00000 0.00000  0.00000  374 THR   G C   
5529  O O   . THR   C  374 ? 0.37292 0.37292 0.37292 -0.00000 0.00000  0.00000  374 THR   G O   
5530  C CB  . THR   C  374 ? 0.39126 0.39126 0.39126 0.00000  0.00000  0.00000  374 THR   G CB  
5531  O OG1 . THR   C  374 ? 0.32733 0.32733 0.32733 0.00000  0.00000  0.00000  374 THR   G OG1 
5532  C CG2 . THR   C  374 ? 0.19587 0.19587 0.19587 -0.00000 0.00000  0.00000  374 THR   G CG2 
5533  N N   . GLU   C  375 ? 0.39969 0.39969 0.39969 0.00000  0.00000  0.00000  375 GLU   G N   
5534  C CA  . GLU   C  375 ? 0.24178 0.24178 0.24178 -0.00000 0.00000  0.00000  375 GLU   G CA  
5535  C C   . GLU   C  375 ? 0.42982 0.42982 0.42982 0.00000  0.00000  0.00000  375 GLU   G C   
5536  O O   . GLU   C  375 ? 0.25369 0.25369 0.25369 0.00000  0.00000  0.00000  375 GLU   G O   
5537  C CB  . GLU   C  375 ? 0.40462 0.40462 0.40462 0.00000  0.00000  0.00000  375 GLU   G CB  
5538  C CG  . GLU   C  375 ? 0.26095 0.26095 0.26095 -0.00000 0.00000  0.00000  375 GLU   G CG  
5539  C CD  . GLU   C  375 ? 0.39218 0.39218 0.39218 -0.00000 0.00000  0.00000  375 GLU   G CD  
5540  O OE1 . GLU   C  375 ? 0.45973 0.45973 0.45973 0.00000  0.00000  0.00000  375 GLU   G OE1 
5541  O OE2 . GLU   C  375 ? 0.44761 0.44761 0.44761 0.00000  0.00000  0.00000  375 GLU   G OE2 
5542  N N   . ILE   C  376 ? 0.24153 0.24153 0.24153 -0.00000 0.00000  0.00000  376 ILE   G N   
5543  C CA  . ILE   C  376 ? 0.24439 0.24439 0.24439 -0.00000 0.00000  0.00000  376 ILE   G CA  
5544  C C   . ILE   C  376 ? 0.29341 0.29341 0.29341 0.00000  0.00000  0.00000  376 ILE   G C   
5545  O O   . ILE   C  376 ? 0.38914 0.38914 0.38914 0.00000  -0.00000 0.00000  376 ILE   G O   
5546  C CB  . ILE   C  376 ? 0.38269 0.38269 0.38269 0.00000  0.00000  0.00000  376 ILE   G CB  
5547  C CG1 . ILE   C  376 ? 0.24885 0.24885 0.24885 -0.00000 -0.00000 0.00000  376 ILE   G CG1 
5548  C CG2 . ILE   C  376 ? 0.10499 0.10499 0.10499 0.00000  0.00000  0.00000  376 ILE   G CG2 
5549  C CD1 . ILE   C  376 ? 0.51266 0.51266 0.51266 0.00000  0.00000  0.00000  376 ILE   G CD1 
5550  N N   . SER   C  377 ? 0.25442 0.25442 0.25442 0.00000  0.00000  0.00000  377 SER   G N   
5551  C CA  . SER   C  377 ? 0.42589 0.42589 0.42589 0.00000  0.00000  0.00000  377 SER   G CA  
5552  C C   . SER   C  377 ? 0.22308 0.22308 0.22308 0.00000  0.00000  0.00000  377 SER   G C   
5553  O O   . SER   C  377 ? 0.53002 0.53002 0.53002 0.00000  0.00000  0.00000  377 SER   G O   
5554  C CB  . SER   C  377 ? 0.14523 0.14523 0.14523 0.00000  0.00000  0.00000  377 SER   G CB  
5555  O OG  . SER   C  377 ? 0.22220 0.22220 0.22220 0.00000  0.00000  0.00000  377 SER   G OG  
5556  N N   . THR   C  378 ? 0.41453 0.41453 0.41453 -0.00000 0.00000  0.00000  378 THR   G N   
5557  C CA  . THR   C  378 ? 0.23881 0.23881 0.23881 0.00000  0.00000  0.00000  378 THR   G CA  
5558  C C   . THR   C  378 ? 0.43335 0.43335 0.43335 0.00000  0.00000  0.00000  378 THR   G C   
5559  O O   . THR   C  378 ? 0.32866 0.32866 0.32866 0.00000  0.00000  0.00000  378 THR   G O   
5560  C CB  . THR   C  378 ? 0.39741 0.39741 0.39741 0.00000  0.00000  0.00000  378 THR   G CB  
5561  O OG1 . THR   C  378 ? 0.33148 0.33148 0.33148 0.00000  0.00000  0.00000  378 THR   G OG1 
5562  C CG2 . THR   C  378 ? 0.08347 0.08347 0.08347 0.00000  0.00000  0.00000  378 THR   G CG2 
5563  N N   . CYS   C  379 ? 0.30433 0.30433 0.30433 0.00000  0.00000  0.00000  379 CYS   G N   
5564  C CA  . CYS   C  379 ? 0.28257 0.28257 0.28257 -0.00000 0.00000  0.00000  379 CYS   G CA  
5565  C C   . CYS   C  379 ? 0.38478 0.38478 0.38478 -0.00000 0.00000  0.00000  379 CYS   G C   
5566  O O   . CYS   C  379 ? 0.45270 0.45270 0.45270 0.00000  0.00000  0.00000  379 CYS   G O   
5567  C CB  . CYS   C  379 ? 0.28993 0.28993 0.28993 0.00000  0.00000  0.00000  379 CYS   G CB  
5568  S SG  . CYS   C  379 ? 0.43590 0.43590 0.43590 -0.00000 0.00000  0.00000  379 CYS   G SG  
5569  N N   . GLU   C  380 ? 0.32495 0.32495 0.32495 0.00000  0.00000  0.00000  380 GLU   G N   
5570  C CA  . GLU   C  380 ? 0.14136 0.14136 0.14136 0.00000  0.00000  0.00000  380 GLU   G CA  
5571  C C   . GLU   C  380 ? 0.34771 0.34771 0.34771 0.00000  0.00000  0.00000  380 GLU   G C   
5572  O O   . GLU   C  380 ? 0.33327 0.33327 0.33327 0.00000  0.00000  0.00000  380 GLU   G O   
5573  C CB  . GLU   C  380 ? 0.28671 0.28671 0.28671 0.00000  0.00000  0.00000  380 GLU   G CB  
5574  C CG  . GLU   C  380 ? 0.44846 0.44846 0.44846 0.00000  0.00000  0.00000  380 GLU   G CG  
5575  C CD  . GLU   C  380 ? 0.39494 0.39494 0.39494 0.00000  0.00000  0.00000  380 GLU   G CD  
5576  O OE1 . GLU   C  380 ? 0.45859 0.45859 0.45859 -0.00000 0.00000  0.00000  380 GLU   G OE1 
5577  O OE2 . GLU   C  380 ? 0.54839 0.54839 0.54839 0.00000  0.00000  0.00000  380 GLU   G OE2 
5578  N N   . ALA   C  381 ? 0.24320 0.24320 0.24320 0.00000  0.00000  0.00000  381 ALA   G N   
5579  C CA  . ALA   C  381 ? 0.47748 0.47748 0.47748 0.00000  0.00000  0.00000  381 ALA   G CA  
5580  C C   . ALA   C  381 ? 0.35577 0.35577 0.35577 0.00000  0.00000  0.00000  381 ALA   G C   
5581  O O   . ALA   C  381 ? 0.36356 0.36356 0.36356 0.00000  0.00000  0.00000  381 ALA   G O   
5582  C CB  . ALA   C  381 ? 0.23028 0.23028 0.23028 -0.00000 0.00000  0.00000  381 ALA   G CB  
5583  N N   . THR   C  382 ? 0.30083 0.30083 0.30083 0.00000  0.00000  0.00000  382 THR   G N   
5584  C CA  . THR   C  382 ? 0.29554 0.29554 0.29554 0.00000  0.00000  0.00000  382 THR   G CA  
5585  C C   . THR   C  382 ? 0.23390 0.23390 0.23390 0.00000  0.00000  0.00000  382 THR   G C   
5586  O O   . THR   C  382 ? 0.58272 0.58272 0.58272 0.00000  0.00000  0.00000  382 THR   G O   
5587  C CB  . THR   C  382 ? 0.16524 0.16524 0.16524 -0.00000 0.00000  0.00000  382 THR   G CB  
5588  O OG1 . THR   C  382 ? 0.27786 0.27786 0.27786 -0.00000 0.00000  0.00000  382 THR   G OG1 
5589  C CG2 . THR   C  382 ? 0.30187 0.30187 0.30187 0.00000  0.00000  0.00000  382 THR   G CG2 
5590  N N   . VAL   C  383 ? 0.36903 0.36903 0.36903 -0.00000 0.00000  0.00000  383 VAL   G N   
5591  C CA  . VAL   C  383 ? 0.23400 0.23400 0.23400 0.00000  0.00000  0.00000  383 VAL   G CA  
5592  C C   . VAL   C  383 ? 0.41134 0.41134 0.41134 0.00000  0.00000  0.00000  383 VAL   G C   
5593  O O   . VAL   C  383 ? 0.35754 0.35754 0.35754 0.00000  0.00000  0.00000  383 VAL   G O   
5594  C CB  . VAL   C  383 ? 0.49633 0.49633 0.49633 -0.00000 0.00000  0.00000  383 VAL   G CB  
5595  C CG1 . VAL   C  383 ? 0.24370 0.24370 0.24370 0.00000  0.00000  0.00000  383 VAL   G CG1 
5596  C CG2 . VAL   C  383 ? 0.30334 0.30334 0.30334 0.00000  0.00000  0.00000  383 VAL   G CG2 
5597  N N   . SER   C  384 ? 0.49605 0.49605 0.49605 -0.00000 0.00000  0.00000  384 SER   G N   
5598  C CA  . SER   C  384 ? 0.24934 0.24934 0.24934 0.00000  0.00000  0.00000  384 SER   G CA  
5599  C C   . SER   C  384 ? 0.55834 0.55834 0.55834 -0.00000 0.00000  0.00000  384 SER   G C   
5600  O O   . SER   C  384 ? 0.41606 0.41606 0.41606 -0.00000 0.00000  0.00000  384 SER   G O   
5601  C CB  . SER   C  384 ? 0.27970 0.27970 0.27970 0.00000  0.00000  0.00000  384 SER   G CB  
5602  O OG  . SER   C  384 ? 0.62426 0.62426 0.62426 -0.00000 0.00000  0.00000  384 SER   G OG  
5603  N N   . GLU   C  385 ? 0.34345 0.34345 0.34345 0.00000  0.00000  0.00000  385 GLU   G N   
5604  C CA  . GLU   C  385 ? 0.45400 0.45400 0.45400 0.00000  0.00000  0.00000  385 GLU   G CA  
5605  C C   . GLU   C  385 ? 0.44915 0.44915 0.44915 0.00000  0.00000  0.00000  385 GLU   G C   
5606  O O   . GLU   C  385 ? 0.42326 0.42326 0.42326 0.00000  0.00000  0.00000  385 GLU   G O   
5607  C CB  . GLU   C  385 ? 0.17461 0.17461 0.17461 0.00000  0.00000  0.00000  385 GLU   G CB  
5608  C CG  . GLU   C  385 ? 0.34938 0.34938 0.34938 0.00000  0.00000  -0.00000 385 GLU   G CG  
5609  C CD  . GLU   C  385 ? 0.56354 0.56354 0.56354 0.00000  0.00000  0.00000  385 GLU   G CD  
5610  O OE1 . GLU   C  385 ? 0.54314 0.54314 0.54314 0.00000  0.00000  -0.00000 385 GLU   G OE1 
5611  O OE2 . GLU   C  385 ? 0.38054 0.38054 0.38054 0.00000  0.00000  0.00000  385 GLU   G OE2 
5612  N N   . GLY   C  386 ? 0.43378 0.43378 0.43378 0.00000  0.00000  0.00000  386 GLY   G N   
5613  C CA  . GLY   C  386 ? 0.25845 0.25845 0.25845 0.00000  0.00000  0.00000  386 GLY   G CA  
5614  C C   . GLY   C  386 ? 0.49541 0.49541 0.49541 0.00000  -0.00000 0.00000  386 GLY   G C   
5615  O O   . GLY   C  386 ? 0.42682 0.42682 0.42682 0.00000  0.00000  0.00000  386 GLY   G O   
5616  N N   . GLN   C  387 ? 0.40138 0.40138 0.40138 0.00000  0.00000  0.00000  387 GLN   G N   
5617  C CA  . GLN   C  387 ? 0.35946 0.35946 0.35946 0.00000  0.00000  0.00000  387 GLN   G CA  
5618  C C   . GLN   C  387 ? 0.60308 0.60308 0.60308 0.00000  0.00000  0.00000  387 GLN   G C   
5619  O O   . GLN   C  387 ? 0.51615 0.51615 0.51615 0.00000  0.00000  0.00000  387 GLN   G O   
5620  C CB  . GLN   C  387 ? 0.34497 0.34497 0.34497 0.00000  0.00000  0.00000  387 GLN   G CB  
5621  C CG  . GLN   C  387 ? 0.35211 0.35211 0.35211 0.00000  0.00000  0.00000  387 GLN   G CG  
5622  C CD  . GLN   C  387 ? 0.45344 0.45344 0.45344 0.00000  0.00000  0.00000  387 GLN   G CD  
5623  O OE1 . GLN   C  387 ? 0.51630 0.51630 0.51630 0.00000  0.00000  0.00000  387 GLN   G OE1 
5624  N NE2 . GLN   C  387 ? 0.36960 0.36960 0.36960 -0.00000 0.00000  0.00000  387 GLN   G NE2 
5625  N N   . HIS   C  388 ? 0.34009 0.34009 0.34009 0.00000  0.00000  0.00000  388 HIS   G N   
5626  C CA  . HIS   C  388 ? 0.48313 0.48313 0.48313 -0.00000 0.00000  0.00000  388 HIS   G CA  
5627  C C   . HIS   C  388 ? 0.65600 0.65600 0.65600 -0.00000 0.00000  0.00000  388 HIS   G C   
5628  O O   . HIS   C  388 ? 0.32776 0.32776 0.32776 0.00000  0.00000  0.00000  388 HIS   G O   
5629  C CB  . HIS   C  388 ? 0.20471 0.20471 0.20471 -0.00000 0.00000  0.00000  388 HIS   G CB  
5630  C CG  . HIS   C  388 ? 0.42423 0.42423 0.42423 0.00000  0.00000  0.00000  388 HIS   G CG  
5631  N ND1 . HIS   C  388 ? 0.43637 0.43637 0.43637 0.00000  0.00000  0.00000  388 HIS   G ND1 
5632  C CD2 . HIS   C  388 ? 0.28404 0.28404 0.28404 -0.00000 0.00000  0.00000  388 HIS   G CD2 
5633  C CE1 . HIS   C  388 ? 0.38971 0.38971 0.38971 -0.00000 0.00000  0.00000  388 HIS   G CE1 
5634  N NE2 . HIS   C  388 ? 0.33830 0.33830 0.33830 0.00000  0.00000  0.00000  388 HIS   G NE2 
5635  N N   . VAL   C  389 ? 0.20616 0.20616 0.20616 0.00000  -0.00000 0.00000  389 VAL   G N   
5636  C CA  . VAL   C  389 ? 0.36325 0.36325 0.36325 0.00000  0.00000  0.00000  389 VAL   G CA  
5637  C C   . VAL   C  389 ? 0.34987 0.34987 0.34987 0.00000  0.00000  0.00000  389 VAL   G C   
5638  O O   . VAL   C  389 ? 0.52887 0.52887 0.52887 0.00000  0.00000  0.00000  389 VAL   G O   
5639  C CB  . VAL   C  389 ? 0.42894 0.42894 0.42894 -0.00000 0.00000  0.00000  389 VAL   G CB  
5640  C CG1 . VAL   C  389 ? 0.23641 0.23641 0.23641 -0.00000 0.00000  0.00000  389 VAL   G CG1 
5641  C CG2 . VAL   C  389 ? 0.16406 0.16406 0.16406 -0.00000 -0.00000 0.00000  389 VAL   G CG2 
5642  N N   . ASN   C  390 ? 0.24433 0.24433 0.24433 0.00000  0.00000  0.00000  390 ASN   G N   
5643  C CA  . ASN   C  390 ? 0.28819 0.28819 0.28819 0.00000  0.00000  0.00000  390 ASN   G CA  
5644  C C   . ASN   C  390 ? 0.60942 0.60942 0.60942 0.00000  0.00000  0.00000  390 ASN   G C   
5645  O O   . ASN   C  390 ? 0.32412 0.32412 0.32412 -0.00000 0.00000  0.00000  390 ASN   G O   
5646  C CB  . ASN   C  390 ? 0.44905 0.44905 0.44905 0.00000  0.00000  0.00000  390 ASN   G CB  
5647  C CG  . ASN   C  390 ? 0.36733 0.36733 0.36733 0.00000  0.00000  0.00000  390 ASN   G CG  
5648  O OD1 . ASN   C  390 ? 0.50011 0.50011 0.50011 0.00000  0.00000  0.00000  390 ASN   G OD1 
5649  N ND2 . ASN   C  390 ? 0.49318 0.49318 0.49318 -0.00000 0.00000  0.00000  390 ASN   G ND2 
5650  N N   . ARG   C  391 ? 0.29044 0.29044 0.29044 -0.00000 0.00000  0.00000  391 ARG   G N   
5651  C CA  . ARG   C  391 ? 0.42463 0.42463 0.42463 -0.00000 0.00000  0.00000  391 ARG   G CA  
5652  C C   . ARG   C  391 ? 0.27274 0.27274 0.27274 0.00000  0.00000  0.00000  391 ARG   G C   
5653  O O   . ARG   C  391 ? 0.40800 0.40800 0.40800 0.00000  0.00000  0.00000  391 ARG   G O   
5654  C CB  . ARG   C  391 ? 0.16343 0.16343 0.16343 0.00000  0.00000  -0.00000 391 ARG   G CB  
5655  C CG  . ARG   C  391 ? 0.28591 0.28591 0.28591 -0.00000 -0.00000 0.00000  391 ARG   G CG  
5656  C CD  . ARG   C  391 ? 0.40734 0.40734 0.40734 -0.00000 0.00000  0.00000  391 ARG   G CD  
5657  N NE  . ARG   C  391 ? 0.31058 0.31058 0.31058 0.00000  -0.00000 0.00000  391 ARG   G NE  
5658  C CZ  . ARG   C  391 ? 0.83706 0.83706 0.83706 0.00000  0.00000  -0.00000 391 ARG   G CZ  
5659  N NH1 . ARG   C  391 ? 0.32280 0.32280 0.32280 0.00000  0.00000  0.00000  391 ARG   G NH1 
5660  N NH2 . ARG   C  391 ? 0.33481 0.33481 0.33481 -0.00000 0.00000  0.00000  391 ARG   G NH2 
5661  N N   . GLY   C  392 ? 0.28610 0.28610 0.28610 -0.00000 0.00000  0.00000  392 GLY   G N   
5662  C CA  . GLY   C  392 ? 0.24086 0.24086 0.24086 0.00000  0.00000  0.00000  392 GLY   G CA  
5663  C C   . GLY   C  392 ? 0.35207 0.35207 0.35207 0.00000  0.00000  0.00000  392 GLY   G C   
5664  O O   . GLY   C  392 ? 0.33404 0.33404 0.33404 -0.00000 0.00000  0.00000  392 GLY   G O   
5665  N N   . ASP   C  393 ? 0.22034 0.22034 0.22034 0.00000  0.00000  0.00000  393 ASP   G N   
5666  C CA  . ASP   C  393 ? 0.38106 0.38106 0.38106 0.00000  0.00000  0.00000  393 ASP   G CA  
5667  C C   . ASP   C  393 ? 0.31210 0.31210 0.31210 0.00000  0.00000  0.00000  393 ASP   G C   
5668  O O   . ASP   C  393 ? 0.55344 0.55344 0.55344 -0.00000 0.00000  0.00000  393 ASP   G O   
5669  C CB  . ASP   C  393 ? 0.26251 0.26251 0.26251 0.00000  0.00000  0.00000  393 ASP   G CB  
5670  C CG  . ASP   C  393 ? 0.62838 0.62838 0.62838 0.00000  0.00000  0.00000  393 ASP   G CG  
5671  O OD1 . ASP   C  393 ? 0.58534 0.58534 0.58534 0.00000  0.00000  0.00000  393 ASP   G OD1 
5672  O OD2 . ASP   C  393 ? 0.43464 0.43464 0.43464 0.00000  -0.00000 0.00000  393 ASP   G OD2 
5673  N N   . ASP   C  394 ? 0.55990 0.55990 0.55990 0.00000  0.00000  0.00000  394 ASP   G N   
5674  C CA  . ASP   C  394 ? 0.25235 0.25235 0.25235 0.00000  0.00000  0.00000  394 ASP   G CA  
5675  C C   . ASP   C  394 ? 0.59029 0.59029 0.59029 0.00000  0.00000  0.00000  394 ASP   G C   
5676  O O   . ASP   C  394 ? 0.37276 0.37276 0.37276 -0.00000 0.00000  0.00000  394 ASP   G O   
5677  C CB  . ASP   C  394 ? 0.49930 0.49930 0.49930 0.00000  0.00000  0.00000  394 ASP   G CB  
5678  C CG  . ASP   C  394 ? 0.36634 0.36634 0.36634 -0.00000 0.00000  0.00000  394 ASP   G CG  
5679  O OD1 . ASP   C  394 ? 0.92815 0.92815 0.92815 -0.00000 0.00000  0.00000  394 ASP   G OD1 
5680  O OD2 . ASP   C  394 ? 0.86799 0.86799 0.86799 -0.00000 0.00000  0.00000  394 ASP   G OD2 
5681  N N   . LEU   C  395 ? 0.32886 0.32886 0.32886 0.00000  0.00000  0.00000  395 LEU   G N   
5682  C CA  . LEU   C  395 ? 0.56875 0.56875 0.56875 -0.00000 0.00000  0.00000  395 LEU   G CA  
5683  C C   . LEU   C  395 ? 0.47927 0.47927 0.47927 0.00000  0.00000  0.00000  395 LEU   G C   
5684  O O   . LEU   C  395 ? 0.44717 0.44717 0.44717 0.00000  0.00000  0.00000  395 LEU   G O   
5685  C CB  . LEU   C  395 ? 0.28340 0.28340 0.28340 0.00000  0.00000  0.00000  395 LEU   G CB  
5686  C CG  . LEU   C  395 ? 0.46673 0.46673 0.46673 -0.00000 -0.00000 0.00000  395 LEU   G CG  
5687  C CD1 . LEU   C  395 ? 0.27671 0.27671 0.27671 -0.00000 0.00000  0.00000  395 LEU   G CD1 
5688  C CD2 . LEU   C  395 ? 0.40375 0.40375 0.40375 0.00000  0.00000  0.00000  395 LEU   G CD2 
5689  N N   . GLY   C  396 ? 0.31484 0.31484 0.31484 0.00000  0.00000  0.00000  396 GLY   G N   
5690  C CA  . GLY   C  396 ? 0.42121 0.42121 0.42121 0.00000  0.00000  0.00000  396 GLY   G CA  
5691  C C   . GLY   C  396 ? 0.37268 0.37268 0.37268 0.00000  0.00000  0.00000  396 GLY   G C   
5692  O O   . GLY   C  396 ? 0.41638 0.41638 0.41638 0.00000  0.00000  0.00000  396 GLY   G O   
5693  N N   . MET   C  397 ? 0.31912 0.31912 0.31912 0.00000  0.00000  0.00000  397 MET   G N   
5694  C CA  . MET   C  397 ? 0.30490 0.30490 0.30490 0.00000  0.00000  0.00000  397 MET   G CA  
5695  C C   . MET   C  397 ? 0.50134 0.50134 0.50134 0.00000  0.00000  0.00000  397 MET   G C   
5696  O O   . MET   C  397 ? 0.36492 0.36492 0.36492 -0.00000 0.00000  0.00000  397 MET   G O   
5697  C CB  . MET   C  397 ? 0.27735 0.27735 0.27735 0.00000  0.00000  0.00000  397 MET   G CB  
5698  C CG  . MET   C  397 ? 0.33410 0.33410 0.33410 0.00000  0.00000  0.00000  397 MET   G CG  
5699  S SD  . MET   C  397 ? 0.46583 0.46583 0.46583 -0.00000 0.00000  0.00000  397 MET   G SD  
5700  C CE  . MET   C  397 ? 0.19030 0.19030 0.19030 0.00000  -0.00000 0.00000  397 MET   G CE  
5701  N N   . PHE   C  398 ? 0.34001 0.34001 0.34001 -0.00000 0.00000  0.00000  398 PHE   G N   
5702  C CA  . PHE   C  398 ? 0.25493 0.25493 0.25493 -0.00000 0.00000  0.00000  398 PHE   G CA  
5703  C C   . PHE   C  398 ? 0.37879 0.37879 0.37879 0.00000  -0.00000 0.00000  398 PHE   G C   
5704  O O   . PHE   C  398 ? 0.50178 0.50178 0.50178 0.00000  0.00000  0.00000  398 PHE   G O   
5705  C CB  . PHE   C  398 ? 0.25597 0.25597 0.25597 0.00000  0.00000  0.00000  398 PHE   G CB  
5706  C CG  . PHE   C  398 ? 0.42880 0.42880 0.42880 0.00000  0.00000  0.00000  398 PHE   G CG  
5707  C CD1 . PHE   C  398 ? 0.25995 0.25995 0.25995 0.00000  0.00000  0.00000  398 PHE   G CD1 
5708  C CD2 . PHE   C  398 ? 0.34554 0.34554 0.34554 -0.00000 0.00000  0.00000  398 PHE   G CD2 
5709  C CE1 . PHE   C  398 ? 0.41244 0.41244 0.41244 -0.00000 0.00000  0.00000  398 PHE   G CE1 
5710  C CE2 . PHE   C  398 ? 0.29545 0.29545 0.29545 0.00000  0.00000  0.00000  398 PHE   G CE2 
5711  C CZ  . PHE   C  398 ? 0.38836 0.38836 0.38836 0.00000  0.00000  0.00000  398 PHE   G CZ  
5712  N N   . HIS   C  399 ? 0.36524 0.36524 0.36524 0.00000  0.00000  0.00000  399 HIS   G N   
5713  C CA  . HIS   C  399 ? 0.47155 0.47155 0.47155 0.00000  0.00000  0.00000  399 HIS   G CA  
5714  C C   . HIS   C  399 ? 0.19873 0.19873 0.19873 0.00000  0.00000  0.00000  399 HIS   G C   
5715  O O   . HIS   C  399 ? 0.55840 0.55840 0.55840 0.00000  0.00000  0.00000  399 HIS   G O   
5716  C CB  . HIS   C  399 ? 0.16708 0.16708 0.16708 0.00000  0.00000  0.00000  399 HIS   G CB  
5717  C CG  . HIS   C  399 ? 0.21462 0.21462 0.21462 -0.00000 0.00000  0.00000  399 HIS   G CG  
5718  N ND1 . HIS   C  399 ? 0.31651 0.31651 0.31651 0.00000  0.00000  0.00000  399 HIS   G ND1 
5719  C CD2 . HIS   C  399 ? 0.41002 0.41002 0.41002 -0.00000 0.00000  0.00000  399 HIS   G CD2 
5720  C CE1 . HIS   C  399 ? 0.54009 0.54009 0.54009 0.00000  0.00000  0.00000  399 HIS   G CE1 
5721  N NE2 . HIS   C  399 ? 0.17547 0.17547 0.17547 0.00000  0.00000  -0.00000 399 HIS   G NE2 
5722  N N   . PHE   C  400 ? 0.44709 0.44709 0.44709 -0.00000 0.00000  0.00000  400 PHE   G N   
5723  C CA  . PHE   C  400 ? 0.21239 0.21239 0.21239 -0.00000 0.00000  0.00000  400 PHE   G CA  
5724  C C   . PHE   C  400 ? 0.32170 0.32170 0.32170 0.00000  0.00000  0.00000  400 PHE   G C   
5725  O O   . PHE   C  400 ? 0.45455 0.45455 0.45455 0.00000  0.00000  0.00000  400 PHE   G O   
5726  C CB  . PHE   C  400 ? 0.43628 0.43628 0.43628 -0.00000 -0.00000 0.00000  400 PHE   G CB  
5727  C CG  . PHE   C  400 ? 0.18205 0.18205 0.18205 -0.00000 0.00000  0.00000  400 PHE   G CG  
5728  C CD1 . PHE   C  400 ? 0.42325 0.42325 0.42325 -0.00000 0.00000  0.00000  400 PHE   G CD1 
5729  C CD2 . PHE   C  400 ? 0.43583 0.43583 0.43583 0.00000  0.00000  0.00000  400 PHE   G CD2 
5730  C CE1 . PHE   C  400 ? 0.22907 0.22907 0.22907 0.00000  0.00000  0.00000  400 PHE   G CE1 
5731  C CE2 . PHE   C  400 ? 0.38322 0.38322 0.38322 -0.00000 0.00000  0.00000  400 PHE   G CE2 
5732  C CZ  . PHE   C  400 ? 0.42014 0.42014 0.42014 0.00000  0.00000  0.00000  400 PHE   G CZ  
5733  N N   . GLY   C  401 ? 0.28448 0.28448 0.28448 -0.00000 0.00000  -0.00000 401 GLY   G N   
5734  C CA  . GLY   C  401 ? 0.23291 0.23291 0.23291 0.00000  0.00000  0.00000  401 GLY   G CA  
5735  C C   . GLY   C  401 ? 0.36538 0.36538 0.36538 -0.00000 0.00000  0.00000  401 GLY   G C   
5736  O O   . GLY   C  401 ? 0.44382 0.44382 0.44382 0.00000  0.00000  0.00000  401 GLY   G O   
5737  N N   . GLY   C  402 ? 0.38763 0.38763 0.38763 0.00000  0.00000  0.00000  402 GLY   G N   
5738  C CA  . GLY   C  402 ? 0.29398 0.29398 0.29398 0.00000  0.00000  0.00000  402 GLY   G CA  
5739  C C   . GLY   C  402 ? 0.66429 0.66429 0.66429 0.00000  0.00000  0.00000  402 GLY   G C   
5740  O O   . GLY   C  402 ? 0.43148 0.43148 0.43148 0.00000  0.00000  0.00000  402 GLY   G O   
5741  O OXT . GLY   C  402 ? 0.54779 0.54779 0.54779 -0.00000 0.00000  0.00000  402 GLY   G OXT 
5742  N N   . SER   D  1   ? 0.25979 0.25979 0.25979 0.00000  0.00000  0.00000  404 SER   H N   
5743  C CA  . SER   D  1   ? 0.19798 0.19798 0.19798 0.00000  0.00000  0.00000  404 SER   H CA  
5744  C C   . SER   D  1   ? 0.34268 0.34268 0.34268 0.00000  0.00000  0.00000  404 SER   H C   
5745  O O   . SER   D  1   ? 0.38720 0.38720 0.38720 0.00000  0.00000  0.00000  404 SER   H O   
5746  C CB  . SER   D  1   ? 0.27745 0.27745 0.27745 0.00000  0.00000  0.00000  404 SER   H CB  
5747  O OG  . SER   D  1   ? 0.31213 0.31213 0.31213 0.00000  0.00000  0.00000  404 SER   H OG  
5748  N N   . PHE   D  2   ? 0.21198 0.21198 0.21198 -0.00000 0.00000  0.00000  405 PHE   H N   
5749  C CA  . PHE   D  2   ? 0.29145 0.29145 0.29145 0.00000  0.00000  0.00000  405 PHE   H CA  
5750  C C   . PHE   D  2   ? 0.26195 0.26195 0.26195 0.00000  0.00000  0.00000  405 PHE   H C   
5751  O O   . PHE   D  2   ? 0.37972 0.37972 0.37972 0.00000  0.00000  0.00000  405 PHE   H O   
5752  C CB  . PHE   D  2   ? 0.30007 0.30007 0.30007 -0.00000 -0.00000 0.00000  405 PHE   H CB  
5753  C CG  . PHE   D  2   ? 0.33139 0.33139 0.33139 -0.00000 -0.00000 -0.00000 405 PHE   H CG  
5754  C CD1 . PHE   D  2   ? 0.41109 0.41109 0.41109 -0.00000 0.00000  0.00000  405 PHE   H CD1 
5755  C CD2 . PHE   D  2   ? 0.37490 0.37490 0.37490 0.00000  0.00000  0.00000  405 PHE   H CD2 
5756  C CE1 . PHE   D  2   ? 0.33167 0.33167 0.33167 0.00000  0.00000  0.00000  405 PHE   H CE1 
5757  C CE2 . PHE   D  2   ? 0.28275 0.28275 0.28275 -0.00000 0.00000  0.00000  405 PHE   H CE2 
5758  C CZ  . PHE   D  2   ? 0.36112 0.36112 0.36112 0.00000  0.00000  0.00000  405 PHE   H CZ  
5759  N N   . ALA   D  3   ? 0.29408 0.29408 0.29408 -0.00000 0.00000  0.00000  406 ALA   H N   
5760  C CA  . ALA   D  3   ? 0.34793 0.34793 0.34793 0.00000  0.00000  0.00000  406 ALA   H CA  
5761  C C   . ALA   D  3   ? 0.38770 0.38770 0.38770 0.00000  0.00000  0.00000  406 ALA   H C   
5762  O O   . ALA   D  3   ? 0.37388 0.37388 0.37388 0.00000  0.00000  0.00000  406 ALA   H O   
5763  C CB  . ALA   D  3   ? 0.14276 0.14276 0.14276 0.00000  -0.00000 0.00000  406 ALA   H CB  
5764  N N   . LEU   D  4   ? 0.37520 0.37520 0.37520 0.00000  0.00000  0.00000  407 LEU   H N   
5765  C CA  . LEU   D  4   ? 0.36605 0.36605 0.36605 0.00000  0.00000  0.00000  407 LEU   H CA  
5766  C C   . LEU   D  4   ? 0.17884 0.17884 0.17884 0.00000  -0.00000 0.00000  407 LEU   H C   
5767  O O   . LEU   D  4   ? 0.42654 0.42654 0.42654 0.00000  0.00000  0.00000  407 LEU   H O   
5768  C CB  . LEU   D  4   ? 0.22608 0.22608 0.22608 0.00000  0.00000  0.00000  407 LEU   H CB  
5769  C CG  . LEU   D  4   ? 0.37463 0.37463 0.37463 0.00000  0.00000  0.00000  407 LEU   H CG  
5770  C CD1 . LEU   D  4   ? 0.20231 0.20231 0.20231 -0.00000 0.00000  0.00000  407 LEU   H CD1 
5771  C CD2 . LEU   D  4   ? 0.27764 0.27764 0.27764 0.00000  0.00000  0.00000  407 LEU   H CD2 
5772  N N   . GLY   D  5   ? 0.46138 0.46138 0.46138 -0.00000 0.00000  0.00000  408 GLY   H N   
5773  C CA  . GLY   D  5   ? 0.16644 0.16644 0.16644 0.00000  0.00000  0.00000  408 GLY   H CA  
5774  C C   . GLY   D  5   ? 0.36306 0.36306 0.36306 0.00000  0.00000  0.00000  408 GLY   H C   
5775  O O   . GLY   D  5   ? 0.44316 0.44316 0.44316 0.00000  0.00000  0.00000  408 GLY   H O   
5776  N N   . LEU   D  6   ? 0.17553 0.17553 0.17553 -0.00000 0.00000  0.00000  409 LEU   H N   
5777  C CA  . LEU   D  6   ? 0.42067 0.42067 0.42067 0.00000  0.00000  0.00000  409 LEU   H CA  
5778  C C   . LEU   D  6   ? 0.33703 0.33703 0.33703 0.00000  0.00000  0.00000  409 LEU   H C   
5779  O O   . LEU   D  6   ? 0.40119 0.40119 0.40119 0.00000  0.00000  0.00000  409 LEU   H O   
5780  C CB  . LEU   D  6   ? 0.31025 0.31025 0.31025 -0.00000 0.00000  0.00000  409 LEU   H CB  
5781  C CG  . LEU   D  6   ? 0.39733 0.39733 0.39733 0.00000  0.00000  0.00000  409 LEU   H CG  
5782  C CD1 . LEU   D  6   ? 0.22106 0.22106 0.22106 0.00000  -0.00000 -0.00000 409 LEU   H CD1 
5783  C CD2 . LEU   D  6   ? 0.16472 0.16472 0.16472 -0.00000 0.00000  0.00000  409 LEU   H CD2 
5784  N N   . ARG   D  7   ? 0.35212 0.35212 0.35212 0.00000  0.00000  0.00000  410 ARG   H N   
5785  C CA  . ARG   D  7   ? 0.33600 0.33600 0.33600 -0.00000 0.00000  0.00000  410 ARG   H CA  
5786  C C   . ARG   D  7   ? 0.41071 0.41071 0.41071 0.00000  0.00000  0.00000  410 ARG   H C   
5787  O O   . ARG   D  7   ? 0.55336 0.55336 0.55336 0.00000  -0.00000 0.00000  410 ARG   H O   
5788  C CB  . ARG   D  7   ? 0.16945 0.16945 0.16945 0.00000  0.00000  0.00000  410 ARG   H CB  
5789  C CG  . ARG   D  7   ? 0.19489 0.19489 0.19489 0.00000  0.00000  0.00000  410 ARG   H CG  
5790  C CD  . ARG   D  7   ? 0.33731 0.33731 0.33731 0.00000  0.00000  0.00000  410 ARG   H CD  
5791  N NE  . ARG   D  7   ? 0.57913 0.57913 0.57913 0.00000  0.00000  0.00000  410 ARG   H NE  
5792  C CZ  . ARG   D  7   ? 0.46338 0.46338 0.46338 0.00000  0.00000  0.00000  410 ARG   H CZ  
5793  N NH1 . ARG   D  7   ? 0.50598 0.50598 0.50598 0.00000  0.00000  0.00000  410 ARG   H NH1 
5794  N NH2 . ARG   D  7   ? 0.58025 0.58025 0.58025 0.00000  -0.00000 0.00000  410 ARG   H NH2 
5795  N N   . LYS   D  8   ? 0.57174 0.57174 0.57174 0.00000  0.00000  0.00000  411 LYS   H N   
5796  C CA  . LYS   D  8   ? 0.80048 0.80048 0.80048 0.00000  0.00000  0.00000  411 LYS   H CA  
5797  C C   . LYS   D  8   ? 0.70201 0.70201 0.70201 -0.00000 0.00000  0.00000  411 LYS   H C   
5798  O O   . LYS   D  8   ? 0.66290 0.66290 0.66290 0.00000  0.00000  0.00000  411 LYS   H O   
5799  C CB  . LYS   D  8   ? 0.44738 0.44738 0.44738 0.00000  0.00000  0.00000  411 LYS   H CB  
5800  C CG  . LYS   D  8   ? 0.94545 0.94545 0.94545 0.00000  -0.00000 0.00000  411 LYS   H CG  
5801  C CD  . LYS   D  8   ? 0.92241 0.92241 0.92241 0.00000  0.00000  0.00000  411 LYS   H CD  
5802  C CE  . LYS   D  8   ? 1.27548 1.27548 1.27548 0.00000  0.00000  0.00000  411 LYS   H CE  
5803  N NZ  . LYS   D  8   ? 1.19365 1.19365 1.19365 -0.00000 0.00000  0.00000  411 LYS   H NZ  
5804  N N   . ASP   D  9   ? 0.48225 0.48225 0.48225 -0.00000 -0.00000 -0.00000 412 ASP   H N   
5805  C CA  . ASP   D  9   ? 1.13360 1.13360 1.13360 0.00000  0.00000  0.00000  412 ASP   H CA  
5806  C C   . ASP   D  9   ? 0.56768 0.56768 0.56768 0.00000  0.00000  0.00000  412 ASP   H C   
5807  O O   . ASP   D  9   ? 0.95494 0.95494 0.95494 0.00000  -0.00000 -0.00000 412 ASP   H O   
5808  C CB  . ASP   D  9   ? 0.79867 0.79867 0.79867 -0.00000 -0.00000 0.00000  412 ASP   H CB  
5809  C CG  . ASP   D  9   ? 0.91815 0.91815 0.91815 0.00000  0.00000  0.00000  412 ASP   H CG  
5810  O OD1 . ASP   D  9   ? 0.95095 0.95095 0.95095 0.00000  0.00000  0.00000  412 ASP   H OD1 
5811  O OD2 . ASP   D  9   ? 1.23795 1.23795 1.23795 0.00000  0.00000  0.00000  412 ASP   H OD2 
5812  N N   . CYS   D  10  ? 0.86493 0.86493 0.86493 0.00000  0.00000  0.00000  413 CYS   H N   
5813  C CA  . CYS   D  10  ? 0.57265 0.57265 0.57265 0.00000  0.00000  0.00000  413 CYS   H CA  
5814  C C   . CYS   D  10  ? 0.70624 0.70624 0.70624 0.00000  0.00000  0.00000  413 CYS   H C   
5815  O O   . CYS   D  10  ? 0.68096 0.68096 0.68096 0.00000  0.00000  0.00000  413 CYS   H O   
5816  C CB  . CYS   D  10  ? 0.46484 0.46484 0.46484 0.00000  0.00000  0.00000  413 CYS   H CB  
5817  S SG  . CYS   D  10  ? 0.61525 0.61525 0.61525 -0.00000 0.00000  0.00000  413 CYS   H SG  
5818  N N   . ARG   D  11  ? 0.59073 0.59073 0.59073 0.00000  0.00000  0.00000  414 ARG   H N   
5819  C CA  . ARG   D  11  ? 0.87399 0.87399 0.87399 0.00000  0.00000  0.00000  414 ARG   H CA  
5820  C C   . ARG   D  11  ? 1.01749 1.01749 1.01749 0.00000  0.00000  0.00000  414 ARG   H C   
5821  O O   . ARG   D  11  ? 0.66975 0.66975 0.66975 0.00000  0.00000  0.00000  414 ARG   H O   
5822  C CB  . ARG   D  11  ? 0.51493 0.51493 0.51493 0.00000  0.00000  0.00000  414 ARG   H CB  
5823  N N   . ALA   D  12  ? 0.72009 0.72009 0.72009 0.00000  0.00000  0.00000  415 ALA   H N   
5824  C CA  . ALA   D  12  ? 0.57951 0.57951 0.57951 0.00000  0.00000  0.00000  415 ALA   H CA  
5825  C C   . ALA   D  12  ? 0.50199 0.50199 0.50199 -0.00000 0.00000  0.00000  415 ALA   H C   
5826  O O   . ALA   D  12  ? 0.85218 0.85218 0.85218 0.00000  0.00000  0.00000  415 ALA   H O   
5827  C CB  . ALA   D  12  ? 0.32214 0.32214 0.32214 -0.00000 0.00000  0.00000  415 ALA   H CB  
5828  N N   . GLU   D  13  ? 0.31966 0.31966 0.31966 0.00000  0.00000  0.00000  416 GLU   H N   
5829  C CA  . GLU   D  13  ? 0.49296 0.49296 0.49296 0.00000  0.00000  0.00000  416 GLU   H CA  
5830  C C   . GLU   D  13  ? 0.52209 0.52209 0.52209 0.00000  0.00000  0.00000  416 GLU   H C   
5831  O O   . GLU   D  13  ? 0.58755 0.58755 0.58755 0.00000  0.00000  0.00000  416 GLU   H O   
5832  C CB  . GLU   D  13  ? 0.35717 0.35717 0.35717 0.00000  0.00000  0.00000  416 GLU   H CB  
5833  N N   . ILE   D  14  ? 0.49238 0.49238 0.49238 0.00000  0.00000  0.00000  417 ILE   H N   
5834  C CA  . ILE   D  14  ? 0.59023 0.59023 0.59023 0.00000  0.00000  0.00000  417 ILE   H CA  
5835  C C   . ILE   D  14  ? 0.46538 0.46538 0.46538 0.00000  0.00000  0.00000  417 ILE   H C   
5836  O O   . ILE   D  14  ? 0.57099 0.57099 0.57099 0.00000  0.00000  0.00000  417 ILE   H O   
5837  C CB  . ILE   D  14  ? 0.34152 0.34152 0.34152 0.00000  0.00000  0.00000  417 ILE   H CB  
5838  C CG1 . ILE   D  14  ? 0.38421 0.38421 0.38421 0.00000  0.00000  0.00000  417 ILE   H CG1 
5839  C CG2 . ILE   D  14  ? 0.43039 0.43039 0.43039 0.00000  0.00000  0.00000  417 ILE   H CG2 
5840  C CD1 . ILE   D  14  ? 0.51171 0.51171 0.51171 0.00000  0.00000  0.00000  417 ILE   H CD1 
5841  N N   . VAL   D  15  ? 0.56265 0.56265 0.56265 0.00000  0.00000  0.00000  418 VAL   H N   
5842  C CA  . VAL   D  15  ? 0.33088 0.33088 0.33088 0.00000  0.00000  0.00000  418 VAL   H CA  
5843  C C   . VAL   D  15  ? 0.37894 0.37894 0.37894 0.00000  0.00000  0.00000  418 VAL   H C   
5844  O O   . VAL   D  15  ? 0.63356 0.63356 0.63356 -0.00000 0.00000  0.00000  418 VAL   H O   
5845  C CB  . VAL   D  15  ? 0.62678 0.62678 0.62678 0.00000  0.00000  0.00000  418 VAL   H CB  
5846  C CG1 . VAL   D  15  ? 0.22546 0.22546 0.22546 -0.00000 0.00000  0.00000  418 VAL   H CG1 
5847  C CG2 . VAL   D  15  ? 0.20353 0.20353 0.20353 0.00000  0.00000  0.00000  418 VAL   H CG2 
5848  N N   . GLU   D  16  ? 0.57935 0.57935 0.57935 0.00000  0.00000  0.00000  419 GLU   H N   
5849  C CA  . GLU   D  16  ? 0.44600 0.44600 0.44600 -0.00000 0.00000  0.00000  419 GLU   H CA  
5850  C C   . GLU   D  16  ? 0.57823 0.57823 0.57823 0.00000  0.00000  0.00000  419 GLU   H C   
5851  O O   . GLU   D  16  ? 0.57975 0.57975 0.57975 0.00000  0.00000  0.00000  419 GLU   H O   
5852  C CB  . GLU   D  16  ? 0.45478 0.45478 0.45478 0.00000  0.00000  0.00000  419 GLU   H CB  
5853  N N   . LYS   D  17  ? 0.48867 0.48867 0.48867 0.00000  0.00000  0.00000  420 LYS   H N   
5854  C CA  . LYS   D  17  ? 0.51725 0.51725 0.51725 0.00000  0.00000  0.00000  420 LYS   H CA  
5855  C C   . LYS   D  17  ? 0.59981 0.59981 0.59981 -0.00000 0.00000  0.00000  420 LYS   H C   
5856  O O   . LYS   D  17  ? 0.57956 0.57956 0.57956 0.00000  0.00000  0.00000  420 LYS   H O   
5857  C CB  . LYS   D  17  ? 0.29528 0.29528 0.29528 -0.00000 0.00000  0.00000  420 LYS   H CB  
5858  C CG  . LYS   D  17  ? 0.35861 0.35861 0.35861 0.00000  0.00000  0.00000  420 LYS   H CG  
5859  C CD  . LYS   D  17  ? 0.62631 0.62631 0.62631 0.00000  0.00000  0.00000  420 LYS   H CD  
5860  C CE  . LYS   D  17  ? 0.75038 0.75038 0.75038 0.00000  0.00000  0.00000  420 LYS   H CE  
5861  N NZ  . LYS   D  17  ? 1.04035 1.04035 1.04035 -0.00000 0.00000  0.00000  420 LYS   H NZ  
5862  N N   . PHE   D  18  ? 0.42389 0.42389 0.42389 0.00000  0.00000  0.00000  421 PHE   H N   
5863  C CA  . PHE   D  18  ? 0.72377 0.72377 0.72377 -0.00000 0.00000  0.00000  421 PHE   H CA  
5864  C C   . PHE   D  18  ? 0.56175 0.56175 0.56175 -0.00000 0.00000  0.00000  421 PHE   H C   
5865  O O   . PHE   D  18  ? 0.49480 0.49480 0.49480 -0.00000 0.00000  0.00000  421 PHE   H O   
5866  C CB  . PHE   D  18  ? 0.28237 0.28237 0.28237 -0.00000 0.00000  0.00000  421 PHE   H CB  
5867  C CG  . PHE   D  18  ? 0.42460 0.42460 0.42460 -0.00000 0.00000  0.00000  421 PHE   H CG  
5868  C CD1 . PHE   D  18  ? 0.41750 0.41750 0.41750 0.00000  0.00000  0.00000  421 PHE   H CD1 
5869  C CD2 . PHE   D  18  ? 0.63769 0.63769 0.63769 -0.00000 0.00000  0.00000  421 PHE   H CD2 
5870  C CE1 . PHE   D  18  ? 0.32016 0.32016 0.32016 0.00000  0.00000  0.00000  421 PHE   H CE1 
5871  C CE2 . PHE   D  18  ? 0.51593 0.51593 0.51593 -0.00000 0.00000  0.00000  421 PHE   H CE2 
5872  C CZ  . PHE   D  18  ? 0.58776 0.58776 0.58776 0.00000  0.00000  0.00000  421 PHE   H CZ  
5873  N N   . THR   D  19  ? 0.52623 0.52623 0.52623 0.00000  -0.00000 0.00000  422 THR   H N   
5874  C CA  . THR   D  19  ? 0.40239 0.40239 0.40239 0.00000  0.00000  0.00000  422 THR   H CA  
5875  C C   . THR   D  19  ? 0.50431 0.50431 0.50431 0.00000  0.00000  0.00000  422 THR   H C   
5876  O O   . THR   D  19  ? 0.48070 0.48070 0.48070 -0.00000 0.00000  0.00000  422 THR   H O   
5877  C CB  . THR   D  19  ? 0.54961 0.54961 0.54961 0.00000  -0.00000 0.00000  422 THR   H CB  
5878  O OG1 . THR   D  19  ? 0.50153 0.50153 0.50153 -0.00000 0.00000  0.00000  422 THR   H OG1 
5879  C CG2 . THR   D  19  ? 0.57395 0.57395 0.57395 0.00000  0.00000  0.00000  422 THR   H CG2 
5880  N N   . GLU   D  20  ? 0.56103 0.56103 0.56103 0.00000  0.00000  0.00000  423 GLU   H N   
5881  C CA  . GLU   D  20  ? 0.53938 0.53938 0.53938 0.00000  0.00000  0.00000  423 GLU   H CA  
5882  C C   . GLU   D  20  ? 0.41842 0.41842 0.41842 0.00000  0.00000  0.00000  423 GLU   H C   
5883  O O   . GLU   D  20  ? 0.61818 0.61818 0.61818 -0.00000 -0.00000 0.00000  423 GLU   H O   
5884  C CB  . GLU   D  20  ? 0.36554 0.36554 0.36554 0.00000  0.00000  0.00000  423 GLU   H CB  
5885  N N   . PRO   D  21  ? 0.36472 0.36472 0.36472 0.00000  0.00000  0.00000  424 PRO   H N   
5886  C CA  . PRO   D  21  ? 0.53494 0.53494 0.53494 -0.00000 0.00000  0.00000  424 PRO   H CA  
5887  C C   . PRO   D  21  ? 0.35274 0.35274 0.35274 0.00000  0.00000  0.00000  424 PRO   H C   
5888  O O   . PRO   D  21  ? 0.46290 0.46290 0.46290 0.00000  0.00000  -0.00000 424 PRO   H O   
5889  C CB  . PRO   D  21  ? 0.13606 0.13606 0.13606 0.00000  0.00000  0.00000  424 PRO   H CB  
5890  C CG  . PRO   D  21  ? 0.32754 0.32754 0.32754 -0.00000 0.00000  0.00000  424 PRO   H CG  
5891  C CD  . PRO   D  21  ? 0.31096 0.31096 0.31096 0.00000  0.00000  0.00000  424 PRO   H CD  
5892  N N   . GLY   D  22  ? 0.42373 0.42373 0.42373 -0.00000 0.00000  0.00000  425 GLY   H N   
5893  C CA  . GLY   D  22  ? 0.20434 0.20434 0.20434 -0.00000 0.00000  0.00000  425 GLY   H CA  
5894  C C   . GLY   D  22  ? 0.31376 0.31376 0.31376 0.00000  0.00000  0.00000  425 GLY   H C   
5895  O O   . GLY   D  22  ? 0.38821 0.38821 0.38821 0.00000  0.00000  0.00000  425 GLY   H O   
5896  N N   . THR   D  23  ? 0.39279 0.39279 0.39279 0.00000  0.00000  0.00000  426 THR   H N   
5897  C CA  . THR   D  23  ? 0.36327 0.36327 0.36327 -0.00000 0.00000  0.00000  426 THR   H CA  
5898  C C   . THR   D  23  ? 0.36293 0.36293 0.36293 -0.00000 0.00000  0.00000  426 THR   H C   
5899  O O   . THR   D  23  ? 0.73365 0.73365 0.73365 -0.00000 -0.00000 0.00000  426 THR   H O   
5900  C CB  . THR   D  23  ? 0.47310 0.47310 0.47310 -0.00000 0.00000  0.00000  426 THR   H CB  
5901  O OG1 . THR   D  23  ? 0.57821 0.57821 0.57821 -0.00000 0.00000  0.00000  426 THR   H OG1 
5902  C CG2 . THR   D  23  ? 0.35202 0.35202 0.35202 0.00000  0.00000  0.00000  426 THR   H CG2 
5903  N N   . VAL   D  24  ? 0.63249 0.63249 0.63249 0.00000  0.00000  0.00000  427 VAL   H N   
5904  C CA  . VAL   D  24  ? 0.39393 0.39393 0.39393 0.00000  0.00000  0.00000  427 VAL   H CA  
5905  C C   . VAL   D  24  ? 0.32371 0.32371 0.32371 -0.00000 0.00000  0.00000  427 VAL   H C   
5906  O O   . VAL   D  24  ? 0.63850 0.63850 0.63850 0.00000  0.00000  0.00000  427 VAL   H O   
5907  C CB  . VAL   D  24  ? 0.30361 0.30361 0.30361 0.00000  0.00000  0.00000  427 VAL   H CB  
5908  C CG1 . VAL   D  24  ? 0.21165 0.21165 0.21165 0.00000  0.00000  0.00000  427 VAL   H CG1 
5909  C CG2 . VAL   D  24  ? 0.30293 0.30293 0.30293 0.00000  0.00000  0.00000  427 VAL   H CG2 
5910  N N   . ILE   D  25  ? 0.61373 0.61373 0.61373 0.00000  0.00000  0.00000  428 ILE   H N   
5911  C CA  . ILE   D  25  ? 0.21980 0.21980 0.21980 0.00000  -0.00000 0.00000  428 ILE   H CA  
5912  C C   . ILE   D  25  ? 0.49099 0.49099 0.49099 -0.00000 0.00000  0.00000  428 ILE   H C   
5913  O O   . ILE   D  25  ? 0.38081 0.38081 0.38081 -0.00000 0.00000  0.00000  428 ILE   H O   
5914  C CB  . ILE   D  25  ? 0.45292 0.45292 0.45292 -0.00000 0.00000  0.00000  428 ILE   H CB  
5915  C CG1 . ILE   D  25  ? 0.33727 0.33727 0.33727 0.00000  0.00000  0.00000  428 ILE   H CG1 
5916  C CG2 . ILE   D  25  ? 0.18484 0.18484 0.18484 0.00000  0.00000  0.00000  428 ILE   H CG2 
5917  C CD1 . ILE   D  25  ? 0.26925 0.26925 0.26925 0.00000  0.00000  0.00000  428 ILE   H CD1 
5918  N N   . ARG   D  26  ? 0.35236 0.35236 0.35236 -0.00000 0.00000  0.00000  429 ARG   H N   
5919  C CA  . ARG   D  26  ? 0.33731 0.33731 0.33731 0.00000  0.00000  0.00000  429 ARG   H CA  
5920  C C   . ARG   D  26  ? 0.34403 0.34403 0.34403 0.00000  0.00000  0.00000  429 ARG   H C   
5921  O O   . ARG   D  26  ? 0.33187 0.33187 0.33187 -0.00000 0.00000  0.00000  429 ARG   H O   
5922  C CB  . ARG   D  26  ? 0.43882 0.43882 0.43882 -0.00000 0.00000  0.00000  429 ARG   H CB  
5923  C CG  . ARG   D  26  ? 0.36002 0.36002 0.36002 -0.00000 0.00000  0.00000  429 ARG   H CG  
5924  C CD  . ARG   D  26  ? 0.53255 0.53255 0.53255 -0.00000 0.00000  0.00000  429 ARG   H CD  
5925  N NE  . ARG   D  26  ? 0.35249 0.35249 0.35249 -0.00000 0.00000  0.00000  429 ARG   H NE  
5926  C CZ  . ARG   D  26  ? 2.03067 2.03067 2.03067 0.00000  0.00000  0.00000  429 ARG   H CZ  
5927  N NH1 . ARG   D  26  ? 0.29724 0.29724 0.29724 0.00000  0.00000  0.00000  429 ARG   H NH1 
5928  N NH2 . ARG   D  26  ? 0.38370 0.38370 0.38370 0.00000  -0.00000 0.00000  429 ARG   H NH2 
5929  N N   . ILE   D  27  ? 0.20221 0.20221 0.20221 -0.00000 -0.00000 0.00000  430 ILE   H N   
5930  C CA  . ILE   D  27  ? 0.42250 0.42250 0.42250 -0.00000 0.00000  0.00000  430 ILE   H CA  
5931  C C   . ILE   D  27  ? 0.26585 0.26585 0.26585 0.00000  0.00000  0.00000  430 ILE   H C   
5932  O O   . ILE   D  27  ? 0.60530 0.60530 0.60530 0.00000  -0.00000 0.00000  430 ILE   H O   
5933  C CB  . ILE   D  27  ? 0.34023 0.34023 0.34023 0.00000  0.00000  0.00000  430 ILE   H CB  
5934  C CG1 . ILE   D  27  ? 0.27037 0.27037 0.27037 0.00000  0.00000  0.00000  430 ILE   H CG1 
5935  C CG2 . ILE   D  27  ? 0.31635 0.31635 0.31635 -0.00000 0.00000  0.00000  430 ILE   H CG2 
5936  C CD1 . ILE   D  27  ? 0.23470 0.23470 0.23470 -0.00000 0.00000  0.00000  430 ILE   H CD1 
5937  N N   . ASN   D  28  ? 0.56885 0.56885 0.56885 -0.00000 0.00000  0.00000  431 ASN   H N   
5938  C CA  . ASN   D  28  ? 0.30861 0.30861 0.30861 0.00000  0.00000  0.00000  431 ASN   H CA  
5939  C C   . ASN   D  28  ? 0.45512 0.45512 0.45512 0.00000  0.00000  0.00000  431 ASN   H C   
5940  O O   . ASN   D  28  ? 0.33537 0.33537 0.33537 -0.00000 0.00000  0.00000  431 ASN   H O   
5941  C CB  . ASN   D  28  ? 0.25377 0.25377 0.25377 0.00000  0.00000  0.00000  431 ASN   H CB  
5942  C CG  . ASN   D  28  ? 0.40460 0.40460 0.40460 0.00000  0.00000  0.00000  431 ASN   H CG  
5943  O OD1 . ASN   D  28  ? 0.46730 0.46730 0.46730 0.00000  0.00000  0.00000  431 ASN   H OD1 
5944  N ND2 . ASN   D  28  ? 0.30515 0.30515 0.30515 -0.00000 0.00000  0.00000  431 ASN   H ND2 
5945  N N   . GLU   D  29  ? 0.29964 0.29964 0.29964 0.00000  0.00000  0.00000  432 GLU   H N   
5946  C CA  . GLU   D  29  ? 0.40913 0.40913 0.40913 0.00000  0.00000  0.00000  432 GLU   H CA  
5947  C C   . GLU   D  29  ? 0.35565 0.35565 0.35565 -0.00000 0.00000  0.00000  432 GLU   H C   
5948  O O   . GLU   D  29  ? 0.55149 0.55149 0.55149 -0.00000 0.00000  0.00000  432 GLU   H O   
5949  C CB  . GLU   D  29  ? 0.20873 0.20873 0.20873 0.00000  0.00000  0.00000  432 GLU   H CB  
5950  C CG  . GLU   D  29  ? 0.37694 0.37694 0.37694 -0.00000 0.00000  0.00000  432 GLU   H CG  
5951  C CD  . GLU   D  29  ? 0.68570 0.68570 0.68570 0.00000  0.00000  0.00000  432 GLU   H CD  
5952  O OE1 . GLU   D  29  ? 0.49590 0.49590 0.49590 0.00000  0.00000  0.00000  432 GLU   H OE1 
5953  O OE2 . GLU   D  29  ? 0.57509 0.57509 0.57509 -0.00000 0.00000  0.00000  432 GLU   H OE2 
5954  N N   . VAL   D  30  ? 0.54466 0.54466 0.54466 -0.00000 0.00000  0.00000  433 VAL   H N   
5955  C CA  . VAL   D  30  ? 0.23204 0.23204 0.23204 0.00000  0.00000  0.00000  433 VAL   H CA  
5956  C C   . VAL   D  30  ? 0.48664 0.48664 0.48664 0.00000  0.00000  0.00000  433 VAL   H C   
5957  O O   . VAL   D  30  ? 0.37058 0.37058 0.37058 0.00000  0.00000  0.00000  433 VAL   H O   
5958  C CB  . VAL   D  30  ? 0.49740 0.49740 0.49740 -0.00000 0.00000  0.00000  433 VAL   H CB  
5959  C CG1 . VAL   D  30  ? 0.36857 0.36857 0.36857 -0.00000 0.00000  0.00000  433 VAL   H CG1 
5960  C CG2 . VAL   D  30  ? 0.30240 0.30240 0.30240 -0.00000 0.00000  0.00000  433 VAL   H CG2 
5961  N N   . VAL   D  31  ? 0.41873 0.41873 0.41873 0.00000  0.00000  0.00000  434 VAL   H N   
5962  C CA  . VAL   D  31  ? 0.55908 0.55908 0.55908 0.00000  0.00000  0.00000  434 VAL   H CA  
5963  C C   . VAL   D  31  ? 0.40199 0.40199 0.40199 0.00000  0.00000  0.00000  434 VAL   H C   
5964  O O   . VAL   D  31  ? 0.39163 0.39163 0.39163 0.00000  0.00000  0.00000  434 VAL   H O   
5965  C CB  . VAL   D  31  ? 0.43648 0.43648 0.43648 0.00000  0.00000  -0.00000 434 VAL   H CB  
5966  C CG1 . VAL   D  31  ? 0.23086 0.23086 0.23086 0.00000  0.00000  -0.00000 434 VAL   H CG1 
5967  C CG2 . VAL   D  31  ? 0.26352 0.26352 0.26352 -0.00000 0.00000  0.00000  434 VAL   H CG2 
5968  N N   . ALA   D  32  ? 0.33193 0.33193 0.33193 0.00000  0.00000  0.00000  435 ALA   H N   
5969  C CA  . ALA   D  32  ? 0.37344 0.37344 0.37344 0.00000  0.00000  0.00000  435 ALA   H CA  
5970  C C   . ALA   D  32  ? 0.49936 0.49936 0.49936 0.00000  0.00000  0.00000  435 ALA   H C   
5971  O O   . ALA   D  32  ? 0.39892 0.39892 0.39892 0.00000  0.00000  0.00000  435 ALA   H O   
5972  C CB  . ALA   D  32  ? 0.29362 0.29362 0.29362 0.00000  0.00000  0.00000  435 ALA   H CB  
5973  N N   . ALA   D  33  ? 0.43845 0.43845 0.43845 0.00000  0.00000  0.00000  436 ALA   H N   
5974  C CA  . ALA   D  33  ? 0.55241 0.55241 0.55241 0.00000  0.00000  0.00000  436 ALA   H CA  
5975  C C   . ALA   D  33  ? 0.80093 0.80093 0.80093 0.00000  0.00000  0.00000  436 ALA   H C   
5976  O O   . ALA   D  33  ? 0.51465 0.51465 0.51465 -0.00000 0.00000  0.00000  436 ALA   H O   
5977  C CB  . ALA   D  33  ? 0.35107 0.35107 0.35107 0.00000  0.00000  0.00000  436 ALA   H CB  
5978  N N   . LEU   D  34  ? 0.39110 0.39110 0.39110 0.00000  0.00000  0.00000  437 LEU   H N   
5979  C CA  . LEU   D  34  ? 0.76756 0.76756 0.76756 -0.00000 0.00000  0.00000  437 LEU   H CA  
5980  C C   . LEU   D  34  ? 0.36063 0.36063 0.36063 0.00000  0.00000  0.00000  437 LEU   H C   
5981  O O   . LEU   D  34  ? 0.44597 0.44597 0.44597 0.00000  0.00000  0.00000  437 LEU   H O   
5982  C CB  . LEU   D  34  ? 0.34571 0.34571 0.34571 -0.00000 0.00000  0.00000  437 LEU   H CB  
5983  C CG  . LEU   D  34  ? 0.66390 0.66390 0.66390 -0.00000 0.00000  0.00000  437 LEU   H CG  
5984  C CD1 . LEU   D  34  ? 0.42522 0.42522 0.42522 0.00000  0.00000  0.00000  437 LEU   H CD1 
5985  C CD2 . LEU   D  34  ? 0.69878 0.69878 0.69878 -0.00000 0.00000  0.00000  437 LEU   H CD2 
5986  N N   . ASN   E  53  ? 0.21429 0.21429 0.21429 0.00000  0.00000  0.00000  53  ASN   A N   
5987  C CA  . ASN   E  53  ? 1.25712 1.25712 1.25712 0.00000  0.00000  0.00000  53  ASN   A CA  
5988  C C   . ASN   E  53  ? 1.64520 1.64520 1.64520 0.00000  0.00000  0.00000  53  ASN   A C   
5989  O O   . ASN   E  53  ? 1.68137 1.68137 1.68137 0.00000  0.00000  0.00000  53  ASN   A O   
5990  C CB  . ASN   E  53  ? 1.03253 1.03253 1.03253 0.00000  0.00000  0.00000  53  ASN   A CB  
5991  C CG  . ASN   E  53  ? 1.14208 1.14208 1.14208 -0.00000 0.00000  0.00000  53  ASN   A CG  
5992  O OD1 . ASN   E  53  ? 1.15503 1.15503 1.15503 0.00000  0.00000  0.00000  53  ASN   A OD1 
5993  N ND2 . ASN   E  53  ? 1.54785 1.54785 1.54785 0.00000  0.00000  0.00000  53  ASN   A ND2 
5994  N N   . GLU   E  54  ? 0.96075 0.96075 0.96075 0.00000  0.00000  0.00000  54  GLU   A N   
5995  C CA  . GLU   E  54  ? 1.40710 1.40710 1.40710 0.00000  0.00000  0.00000  54  GLU   A CA  
5996  C C   . GLU   E  54  ? 0.67729 0.67729 0.67729 0.00000  0.00000  0.00000  54  GLU   A C   
5997  O O   . GLU   E  54  ? 0.48502 0.48502 0.48502 0.00000  0.00000  0.00000  54  GLU   A O   
5998  C CB  . GLU   E  54  ? 1.15113 1.15113 1.15113 0.00000  -0.00000 0.00000  54  GLU   A CB  
5999  C CG  . GLU   E  54  ? 0.90676 0.90676 0.90676 -0.00000 0.00000  0.00000  54  GLU   A CG  
6000  C CD  . GLU   E  54  ? 1.67126 1.67126 1.67126 0.00000  0.00000  0.00000  54  GLU   A CD  
6001  O OE1 . GLU   E  54  ? 1.94568 1.94568 1.94568 0.00000  0.00000  0.00000  54  GLU   A OE1 
6002  O OE2 . GLU   E  54  ? 1.64929 1.64929 1.64929 0.00000  0.00000  0.00000  54  GLU   A OE2 
6003  N N   . PHE   E  55  ? 1.25706 1.25706 1.25706 0.00000  0.00000  0.00000  55  PHE   A N   
6004  C CA  . PHE   E  55  ? 0.73654 0.73654 0.73654 0.00000  0.00000  0.00000  55  PHE   A CA  
6005  C C   . PHE   E  55  ? 0.91731 0.91731 0.91731 -0.00000 0.00000  0.00000  55  PHE   A C   
6006  O O   . PHE   E  55  ? 1.75814 1.75814 1.75814 -0.00000 0.00000  0.00000  55  PHE   A O   
6007  C CB  . PHE   E  55  ? 0.42517 0.42517 0.42517 0.00000  0.00000  0.00000  55  PHE   A CB  
6008  C CG  . PHE   E  55  ? 0.75643 0.75643 0.75643 0.00000  0.00000  0.00000  55  PHE   A CG  
6009  C CD1 . PHE   E  55  ? 1.07857 1.07857 1.07857 0.00000  -0.00000 0.00000  55  PHE   A CD1 
6010  C CD2 . PHE   E  55  ? 0.38749 0.38749 0.38749 -0.00000 0.00000  0.00000  55  PHE   A CD2 
6011  C CE1 . PHE   E  55  ? 0.96479 0.96479 0.96479 -0.00000 0.00000  0.00000  55  PHE   A CE1 
6012  C CE2 . PHE   E  55  ? 0.22256 0.22256 0.22256 0.00000  0.00000  0.00000  55  PHE   A CE2 
6013  C CZ  . PHE   E  55  ? 0.99723 0.99723 0.99723 0.00000  0.00000  0.00000  55  PHE   A CZ  
6014  N N   . GLY   E  56  ? 0.52590 0.52590 0.52590 0.00000  0.00000  0.00000  56  GLY   A N   
6015  C CA  . GLY   E  56  ? 0.27260 0.27260 0.27260 0.00000  -0.00000 0.00000  56  GLY   A CA  
6016  C C   . GLY   E  56  ? 1.28624 1.28624 1.28624 0.00000  0.00000  0.00000  56  GLY   A C   
6017  O O   . GLY   E  56  ? 1.32714 1.32714 1.32714 0.00000  0.00000  0.00000  56  GLY   A O   
6018  N N   . LEU   E  57  ? 0.41951 0.41951 0.41951 0.00000  0.00000  0.00000  57  LEU   A N   
6019  C CA  . LEU   E  57  ? 0.38021 0.38021 0.38021 -0.00000 0.00000  0.00000  57  LEU   A CA  
6020  C C   . LEU   E  57  ? 0.58466 0.58466 0.58466 -0.00000 0.00000  0.00000  57  LEU   A C   
6021  O O   . LEU   E  57  ? 0.60991 0.60991 0.60991 0.00000  0.00000  0.00000  57  LEU   A O   
6022  C CB  . LEU   E  57  ? 0.33773 0.33773 0.33773 -0.00000 0.00000  0.00000  57  LEU   A CB  
6023  C CG  . LEU   E  57  ? 0.54371 0.54371 0.54371 0.00000  0.00000  0.00000  57  LEU   A CG  
6024  C CD1 . LEU   E  57  ? 0.44728 0.44728 0.44728 0.00000  0.00000  0.00000  57  LEU   A CD1 
6025  C CD2 . LEU   E  57  ? 0.52426 0.52426 0.52426 0.00000  0.00000  0.00000  57  LEU   A CD2 
6026  N N   . MET   E  58  ? 0.48511 0.48511 0.48511 -0.00000 0.00000  0.00000  58  MET   A N   
6027  C CA  . MET   E  58  ? 0.47116 0.47116 0.47116 -0.00000 0.00000  0.00000  58  MET   A CA  
6028  C C   . MET   E  58  ? 0.35348 0.35348 0.35348 -0.00000 0.00000  0.00000  58  MET   A C   
6029  O O   . MET   E  58  ? 0.61521 0.61521 0.61521 0.00000  0.00000  0.00000  58  MET   A O   
6030  C CB  . MET   E  58  ? 0.38178 0.38178 0.38178 -0.00000 -0.00000 0.00000  58  MET   A CB  
6031  C CG  . MET   E  58  ? 0.57558 0.57558 0.57558 0.00000  -0.00000 0.00000  58  MET   A CG  
6032  S SD  . MET   E  58  ? 0.64986 0.64986 0.64986 0.00000  0.00000  0.00000  58  MET   A SD  
6033  C CE  . MET   E  58  ? 0.35383 0.35383 0.35383 -0.00000 0.00000  0.00000  58  MET   A CE  
6034  N N   . GLN   E  59  ? 0.56021 0.56021 0.56021 0.00000  0.00000  0.00000  59  GLN   A N   
6035  C CA  . GLN   E  59  ? 0.41885 0.41885 0.41885 -0.00000 0.00000  0.00000  59  GLN   A CA  
6036  C C   . GLN   E  59  ? 0.54207 0.54207 0.54207 0.00000  0.00000  0.00000  59  GLN   A C   
6037  O O   . GLN   E  59  ? 0.46672 0.46672 0.46672 0.00000  0.00000  0.00000  59  GLN   A O   
6038  C CB  . GLN   E  59  ? 0.33969 0.33969 0.33969 0.00000  0.00000  0.00000  59  GLN   A CB  
6039  C CG  . GLN   E  59  ? 0.71397 0.71397 0.71397 -0.00000 0.00000  0.00000  59  GLN   A CG  
6040  C CD  . GLN   E  59  ? 1.00010 1.00010 1.00010 -0.00000 0.00000  0.00000  59  GLN   A CD  
6041  O OE1 . GLN   E  59  ? 1.14681 1.14681 1.14681 -0.00000 -0.00000 0.00000  59  GLN   A OE1 
6042  N NE2 . GLN   E  59  ? 0.80539 0.80539 0.80539 -0.00000 0.00000  0.00000  59  GLN   A NE2 
6043  N N   . PRO   E  60  ? 0.67381 0.67381 0.67381 0.00000  0.00000  0.00000  60  PRO   A N   
6044  C CA  . PRO   E  60  ? 0.44228 0.44228 0.44228 0.00000  0.00000  0.00000  60  PRO   A CA  
6045  C C   . PRO   E  60  ? 0.74736 0.74736 0.74736 0.00000  0.00000  0.00000  60  PRO   A C   
6046  O O   . PRO   E  60  ? 0.48271 0.48271 0.48271 0.00000  0.00000  0.00000  60  PRO   A O   
6047  C CB  . PRO   E  60  ? 0.45196 0.45196 0.45196 0.00000  0.00000  0.00000  60  PRO   A CB  
6048  C CG  . PRO   E  60  ? 0.54047 0.54047 0.54047 -0.00000 0.00000  0.00000  60  PRO   A CG  
6049  C CD  . PRO   E  60  ? 0.39202 0.39202 0.39202 0.00000  0.00000  0.00000  60  PRO   A CD  
6050  N N   . ILE   E  61  ? 0.30992 0.30992 0.30992 0.00000  0.00000  0.00000  61  ILE   A N   
6051  C CA  . ILE   E  61  ? 0.61811 0.61811 0.61811 -0.00000 0.00000  0.00000  61  ILE   A CA  
6052  C C   . ILE   E  61  ? 0.44484 0.44484 0.44484 -0.00000 0.00000  0.00000  61  ILE   A C   
6053  O O   . ILE   E  61  ? 0.49973 0.49973 0.49973 0.00000  0.00000  0.00000  61  ILE   A O   
6054  C CB  . ILE   E  61  ? 0.43941 0.43941 0.43941 -0.00000 0.00000  0.00000  61  ILE   A CB  
6055  C CG1 . ILE   E  61  ? 0.31975 0.31975 0.31975 0.00000  0.00000  0.00000  61  ILE   A CG1 
6056  C CG2 . ILE   E  61  ? 0.29616 0.29616 0.29616 0.00000  0.00000  0.00000  61  ILE   A CG2 
6057  C CD1 . ILE   E  61  ? 0.40320 0.40320 0.40320 -0.00000 0.00000  0.00000  61  ILE   A CD1 
6058  N N   . GLN   E  62  ? 0.33014 0.33014 0.33014 0.00000  0.00000  0.00000  62  GLN   A N   
6059  C CA  . GLN   E  62  ? 0.43479 0.43479 0.43479 -0.00000 0.00000  0.00000  62  GLN   A CA  
6060  C C   . GLN   E  62  ? 0.24966 0.24966 0.24966 0.00000  0.00000  0.00000  62  GLN   A C   
6061  O O   . GLN   E  62  ? 1.23844 1.23844 1.23844 0.00000  0.00000  0.00000  62  GLN   A O   
6062  C CB  . GLN   E  62  ? 0.38355 0.38355 0.38355 0.00000  0.00000  0.00000  62  GLN   A CB  
6063  C CG  . GLN   E  62  ? 0.54679 0.54679 0.54679 0.00000  0.00000  0.00000  62  GLN   A CG  
6064  C CD  . GLN   E  62  ? 1.24352 1.24352 1.24352 0.00000  0.00000  0.00000  62  GLN   A CD  
6065  O OE1 . GLN   E  62  ? 0.62784 0.62784 0.62784 -0.00000 0.00000  0.00000  62  GLN   A OE1 
6066  N NE2 . GLN   E  62  ? 1.30964 1.30964 1.30964 0.00000  0.00000  0.00000  62  GLN   A NE2 
6067  N N   . GLU   E  63  ? 0.32822 0.32822 0.32822 -0.00000 0.00000  0.00000  63  GLU   A N   
6068  C CA  . GLU   E  63  ? 0.52880 0.52880 0.52880 -0.00000 0.00000  0.00000  63  GLU   A CA  
6069  C C   . GLU   E  63  ? 0.55691 0.55691 0.55691 0.00000  0.00000  0.00000  63  GLU   A C   
6070  O O   . GLU   E  63  ? 0.47231 0.47231 0.47231 -0.00000 0.00000  0.00000  63  GLU   A O   
6071  C CB  . GLU   E  63  ? 0.32767 0.32767 0.32767 0.00000  0.00000  0.00000  63  GLU   A CB  
6072  C CG  . GLU   E  63  ? 0.80356 0.80356 0.80356 0.00000  0.00000  0.00000  63  GLU   A CG  
6073  C CD  . GLU   E  63  ? 0.63628 0.63628 0.63628 0.00000  0.00000  0.00000  63  GLU   A CD  
6074  O OE1 . GLU   E  63  ? 1.22470 1.22470 1.22470 0.00000  0.00000  0.00000  63  GLU   A OE1 
6075  O OE2 . GLU   E  63  ? 1.57418 1.57418 1.57418 0.00000  0.00000  0.00000  63  GLU   A OE2 
6076  N N   . PHE   E  64  ? 0.43190 0.43190 0.43190 -0.00000 0.00000  0.00000  64  PHE   A N   
6077  C CA  . PHE   E  64  ? 0.34893 0.34893 0.34893 -0.00000 0.00000  0.00000  64  PHE   A CA  
6078  C C   . PHE   E  64  ? 0.52671 0.52671 0.52671 0.00000  0.00000  0.00000  64  PHE   A C   
6079  O O   . PHE   E  64  ? 0.45780 0.45780 0.45780 0.00000  0.00000  0.00000  64  PHE   A O   
6080  C CB  . PHE   E  64  ? 0.38811 0.38811 0.38811 -0.00000 0.00000  0.00000  64  PHE   A CB  
6081  C CG  . PHE   E  64  ? 0.45363 0.45363 0.45363 0.00000  0.00000  0.00000  64  PHE   A CG  
6082  C CD1 . PHE   E  64  ? 0.55425 0.55425 0.55425 0.00000  0.00000  0.00000  64  PHE   A CD1 
6083  C CD2 . PHE   E  64  ? 0.31475 0.31475 0.31475 -0.00000 0.00000  0.00000  64  PHE   A CD2 
6084  C CE1 . PHE   E  64  ? 0.37684 0.37684 0.37684 0.00000  0.00000  0.00000  64  PHE   A CE1 
6085  C CE2 . PHE   E  64  ? 0.29259 0.29259 0.29259 -0.00000 0.00000  0.00000  64  PHE   A CE2 
6086  C CZ  . PHE   E  64  ? 0.40326 0.40326 0.40326 0.00000  0.00000  0.00000  64  PHE   A CZ  
6087  N N   . LYS   E  65  ? 0.39870 0.39870 0.39870 0.00000  0.00000  0.00000  65  LYS   A N   
6088  C CA  . LYS   E  65  ? 0.33458 0.33458 0.33458 0.00000  0.00000  0.00000  65  LYS   A CA  
6089  C C   . LYS   E  65  ? 0.59024 0.59024 0.59024 0.00000  0.00000  0.00000  65  LYS   A C   
6090  O O   . LYS   E  65  ? 0.48329 0.48329 0.48329 -0.00000 0.00000  0.00000  65  LYS   A O   
6091  C CB  . LYS   E  65  ? 0.42649 0.42649 0.42649 0.00000  0.00000  0.00000  65  LYS   A CB  
6092  C CG  . LYS   E  65  ? 0.43960 0.43960 0.43960 -0.00000 0.00000  0.00000  65  LYS   A CG  
6093  C CD  . LYS   E  65  ? 0.57302 0.57302 0.57302 0.00000  0.00000  0.00000  65  LYS   A CD  
6094  C CE  . LYS   E  65  ? 0.67121 0.67121 0.67121 0.00000  0.00000  0.00000  65  LYS   A CE  
6095  N NZ  . LYS   E  65  ? 0.81135 0.81135 0.81135 -0.00000 0.00000  -0.00000 65  LYS   A NZ  
6096  N N   . ALA   E  66  ? 0.52312 0.52312 0.52312 -0.00000 0.00000  0.00000  66  ALA   A N   
6097  C CA  . ALA   E  66  ? 0.56408 0.56408 0.56408 -0.00000 0.00000  0.00000  66  ALA   A CA  
6098  C C   . ALA   E  66  ? 0.69471 0.69471 0.69471 0.00000  0.00000  0.00000  66  ALA   A C   
6099  O O   . ALA   E  66  ? 0.49744 0.49744 0.49744 0.00000  0.00000  0.00000  66  ALA   A O   
6100  C CB  . ALA   E  66  ? 0.27650 0.27650 0.27650 0.00000  0.00000  0.00000  66  ALA   A CB  
6101  N N   . PHE   E  67  ? 0.61961 0.61961 0.61961 -0.00000 0.00000  0.00000  67  PHE   A N   
6102  C CA  . PHE   E  67  ? 0.34667 0.34667 0.34667 -0.00000 0.00000  0.00000  67  PHE   A CA  
6103  C C   . PHE   E  67  ? 0.54912 0.54912 0.54912 0.00000  0.00000  0.00000  67  PHE   A C   
6104  O O   . PHE   E  67  ? 0.50189 0.50189 0.50189 0.00000  0.00000  0.00000  67  PHE   A O   
6105  C CB  . PHE   E  67  ? 0.36207 0.36207 0.36207 0.00000  0.00000  0.00000  67  PHE   A CB  
6106  C CG  . PHE   E  67  ? 0.37442 0.37442 0.37442 0.00000  0.00000  0.00000  67  PHE   A CG  
6107  C CD1 . PHE   E  67  ? 0.20198 0.20198 0.20198 -0.00000 0.00000  0.00000  67  PHE   A CD1 
6108  C CD2 . PHE   E  67  ? 0.29793 0.29793 0.29793 -0.00000 0.00000  0.00000  67  PHE   A CD2 
6109  C CE1 . PHE   E  67  ? 0.29239 0.29239 0.29239 -0.00000 0.00000  0.00000  67  PHE   A CE1 
6110  C CE2 . PHE   E  67  ? 0.42316 0.42316 0.42316 0.00000  0.00000  0.00000  67  PHE   A CE2 
6111  C CZ  . PHE   E  67  ? 0.25921 0.25921 0.25921 -0.00000 0.00000  0.00000  67  PHE   A CZ  
6112  N N   . ILE   E  68  ? 0.44848 0.44848 0.44848 0.00000  0.00000  0.00000  68  ILE   A N   
6113  C CA  . ILE   E  68  ? 0.47612 0.47612 0.47612 0.00000  0.00000  0.00000  68  ILE   A CA  
6114  C C   . ILE   E  68  ? 0.55321 0.55321 0.55321 -0.00000 -0.00000 0.00000  68  ILE   A C   
6115  O O   . ILE   E  68  ? 0.52322 0.52322 0.52322 -0.00000 0.00000  0.00000  68  ILE   A O   
6116  C CB  . ILE   E  68  ? 0.34842 0.34842 0.34842 0.00000  0.00000  0.00000  68  ILE   A CB  
6117  C CG1 . ILE   E  68  ? 0.43832 0.43832 0.43832 0.00000  0.00000  0.00000  68  ILE   A CG1 
6118  C CG2 . ILE   E  68  ? 0.41669 0.41669 0.41669 0.00000  0.00000  0.00000  68  ILE   A CG2 
6119  C CD1 . ILE   E  68  ? 0.34939 0.34939 0.34939 0.00000  0.00000  0.00000  68  ILE   A CD1 
6120  N N   . GLU   E  69  ? 0.73143 0.73143 0.73143 0.00000  0.00000  0.00000  69  GLU   A N   
6121  C CA  . GLU   E  69  ? 0.40927 0.40927 0.40927 -0.00000 0.00000  0.00000  69  GLU   A CA  
6122  C C   . GLU   E  69  ? 0.52769 0.52769 0.52769 -0.00000 -0.00000 0.00000  69  GLU   A C   
6123  O O   . GLU   E  69  ? 0.53412 0.53412 0.53412 0.00000  0.00000  0.00000  69  GLU   A O   
6124  C CB  . GLU   E  69  ? 0.48957 0.48957 0.48957 0.00000  0.00000  0.00000  69  GLU   A CB  
6125  C CG  . GLU   E  69  ? 0.31235 0.31235 0.31235 -0.00000 0.00000  0.00000  69  GLU   A CG  
6126  C CD  . GLU   E  69  ? 0.83428 0.83428 0.83428 0.00000  0.00000  0.00000  69  GLU   A CD  
6127  O OE1 . GLU   E  69  ? 0.48533 0.48533 0.48533 0.00000  0.00000  0.00000  69  GLU   A OE1 
6128  O OE2 . GLU   E  69  ? 0.57154 0.57154 0.57154 -0.00000 0.00000  0.00000  69  GLU   A OE2 
6129  N N   . SER   E  70  ? 0.61775 0.61775 0.61775 -0.00000 0.00000  0.00000  70  SER   A N   
6130  C CA  . SER   E  70  ? 0.26036 0.26036 0.26036 -0.00000 0.00000  0.00000  70  SER   A CA  
6131  C C   . SER   E  70  ? 0.62464 0.62464 0.62464 0.00000  0.00000  0.00000  70  SER   A C   
6132  O O   . SER   E  70  ? 0.43128 0.43128 0.43128 0.00000  0.00000  0.00000  70  SER   A O   
6133  C CB  . SER   E  70  ? 0.41993 0.41993 0.41993 -0.00000 0.00000  -0.00000 70  SER   A CB  
6134  O OG  . SER   E  70  ? 0.69017 0.69017 0.69017 0.00000  0.00000  0.00000  70  SER   A OG  
6135  N N   . ASP   E  71  ? 0.44291 0.44291 0.44291 0.00000  0.00000  0.00000  71  ASP   A N   
6136  C CA  . ASP   E  71  ? 0.38316 0.38316 0.38316 0.00000  0.00000  0.00000  71  ASP   A CA  
6137  C C   . ASP   E  71  ? 0.46256 0.46256 0.46256 0.00000  0.00000  0.00000  71  ASP   A C   
6138  O O   . ASP   E  71  ? 0.46133 0.46133 0.46133 -0.00000 0.00000  0.00000  71  ASP   A O   
6139  C CB  . ASP   E  71  ? 0.49924 0.49924 0.49924 0.00000  0.00000  0.00000  71  ASP   A CB  
6140  C CG  . ASP   E  71  ? 0.99648 0.99648 0.99648 0.00000  0.00000  0.00000  71  ASP   A CG  
6141  O OD1 . ASP   E  71  ? 0.53957 0.53957 0.53957 -0.00000 0.00000  0.00000  71  ASP   A OD1 
6142  O OD2 . ASP   E  71  ? 0.71568 0.71568 0.71568 0.00000  -0.00000 0.00000  71  ASP   A OD2 
6143  N N   . PRO   E  72  ? 0.57124 0.57124 0.57124 0.00000  0.00000  0.00000  72  PRO   A N   
6144  C CA  . PRO   E  72  ? 0.54906 0.54906 0.54906 0.00000  0.00000  0.00000  72  PRO   A CA  
6145  C C   . PRO   E  72  ? 0.43321 0.43321 0.43321 0.00000  0.00000  0.00000  72  PRO   A C   
6146  O O   . PRO   E  72  ? 0.50590 0.50590 0.50590 -0.00000 0.00000  0.00000  72  PRO   A O   
6147  C CB  . PRO   E  72  ? 0.37451 0.37451 0.37451 -0.00000 0.00000  0.00000  72  PRO   A CB  
6148  C CG  . PRO   E  72  ? 0.44853 0.44853 0.44853 0.00000  0.00000  0.00000  72  PRO   A CG  
6149  C CD  . PRO   E  72  ? 0.27065 0.27065 0.27065 0.00000  0.00000  0.00000  72  PRO   A CD  
6150  N N   . VAL   E  73  ? 0.46898 0.46898 0.46898 -0.00000 0.00000  0.00000  73  VAL   A N   
6151  C CA  . VAL   E  73  ? 0.60811 0.60811 0.60811 0.00000  0.00000  0.00000  73  VAL   A CA  
6152  C C   . VAL   E  73  ? 0.70431 0.70431 0.70431 -0.00000 0.00000  0.00000  73  VAL   A C   
6153  O O   . VAL   E  73  ? 0.33726 0.33726 0.33726 0.00000  0.00000  0.00000  73  VAL   A O   
6154  C CB  . VAL   E  73  ? 0.56687 0.56687 0.56687 0.00000  -0.00000 0.00000  73  VAL   A CB  
6155  C CG1 . VAL   E  73  ? 0.27623 0.27623 0.27623 0.00000  0.00000  0.00000  73  VAL   A CG1 
6156  C CG2 . VAL   E  73  ? 0.24885 0.24885 0.24885 0.00000  0.00000  0.00000  73  VAL   A CG2 
6157  N N   . VAL   E  74  ? 0.52095 0.52095 0.52095 0.00000  0.00000  0.00000  74  VAL   A N   
6158  C CA  . VAL   E  74  ? 0.40186 0.40186 0.40186 0.00000  0.00000  0.00000  74  VAL   A CA  
6159  C C   . VAL   E  74  ? 0.53906 0.53906 0.53906 -0.00000 0.00000  0.00000  74  VAL   A C   
6160  O O   . VAL   E  74  ? 0.59770 0.59770 0.59770 0.00000  0.00000  0.00000  74  VAL   A O   
6161  C CB  . VAL   E  74  ? 0.42880 0.42880 0.42880 -0.00000 0.00000  0.00000  74  VAL   A CB  
6162  C CG1 . VAL   E  74  ? 0.21258 0.21258 0.21258 -0.00000 -0.00000 0.00000  74  VAL   A CG1 
6163  C CG2 . VAL   E  74  ? 0.29917 0.29917 0.29917 -0.00000 0.00000  0.00000  74  VAL   A CG2 
6164  N N   . HIS   E  75  ? 0.55317 0.55317 0.55317 -0.00000 0.00000  0.00000  75  HIS   A N   
6165  C CA  . HIS   E  75  ? 0.46072 0.46072 0.46072 0.00000  0.00000  0.00000  75  HIS   A CA  
6166  C C   . HIS   E  75  ? 0.31938 0.31938 0.31938 0.00000  0.00000  0.00000  75  HIS   A C   
6167  O O   . HIS   E  75  ? 0.40696 0.40696 0.40696 -0.00000 0.00000  0.00000  75  HIS   A O   
6168  C CB  . HIS   E  75  ? 0.35399 0.35399 0.35399 -0.00000 0.00000  0.00000  75  HIS   A CB  
6169  C CG  . HIS   E  75  ? 0.76975 0.76975 0.76975 0.00000  0.00000  0.00000  75  HIS   A CG  
6170  N ND1 . HIS   E  75  ? 0.88941 0.88941 0.88941 -0.00000 0.00000  0.00000  75  HIS   A ND1 
6171  C CD2 . HIS   E  75  ? 0.78808 0.78808 0.78808 -0.00000 0.00000  0.00000  75  HIS   A CD2 
6172  C CE1 . HIS   E  75  ? 0.73100 0.73100 0.73100 0.00000  0.00000  0.00000  75  HIS   A CE1 
6173  N NE2 . HIS   E  75  ? 0.56230 0.56230 0.56230 0.00000  0.00000  0.00000  75  HIS   A NE2 
6174  N N   . GLN   E  76  ? 0.48842 0.48842 0.48842 -0.00000 0.00000  0.00000  76  GLN   A N   
6175  C CA  . GLN   E  76  ? 0.21833 0.21833 0.21833 0.00000  0.00000  0.00000  76  GLN   A CA  
6176  C C   . GLN   E  76  ? 0.51209 0.51209 0.51209 -0.00000 0.00000  0.00000  76  GLN   A C   
6177  O O   . GLN   E  76  ? 0.37615 0.37615 0.37615 0.00000  0.00000  0.00000  76  GLN   A O   
6178  C CB  . GLN   E  76  ? 0.54029 0.54029 0.54029 -0.00000 0.00000  0.00000  76  GLN   A CB  
6179  C CG  . GLN   E  76  ? 0.23605 0.23605 0.23605 0.00000  0.00000  0.00000  76  GLN   A CG  
6180  C CD  . GLN   E  76  ? 0.97404 0.97404 0.97404 0.00000  0.00000  0.00000  76  GLN   A CD  
6181  O OE1 . GLN   E  76  ? 0.46295 0.46295 0.46295 0.00000  0.00000  0.00000  76  GLN   A OE1 
6182  N NE2 . GLN   E  76  ? 0.36259 0.36259 0.36259 0.00000  0.00000  0.00000  76  GLN   A NE2 
6183  N N   . GLU   E  77  ? 0.49284 0.49284 0.49284 0.00000  0.00000  0.00000  77  GLU   A N   
6184  C CA  . GLU   E  77  ? 0.37877 0.37877 0.37877 -0.00000 0.00000  0.00000  77  GLU   A CA  
6185  C C   . GLU   E  77  ? 0.72530 0.72530 0.72530 0.00000  0.00000  0.00000  77  GLU   A C   
6186  O O   . GLU   E  77  ? 0.30236 0.30236 0.30236 0.00000  0.00000  0.00000  77  GLU   A O   
6187  C CB  . GLU   E  77  ? 0.37296 0.37296 0.37296 0.00000  0.00000  0.00000  77  GLU   A CB  
6188  C CG  . GLU   E  77  ? 0.31085 0.31085 0.31085 0.00000  0.00000  0.00000  77  GLU   A CG  
6189  C CD  . GLU   E  77  ? 0.72106 0.72106 0.72106 0.00000  0.00000  0.00000  77  GLU   A CD  
6190  O OE1 . GLU   E  77  ? 0.48877 0.48877 0.48877 0.00000  0.00000  0.00000  77  GLU   A OE1 
6191  O OE2 . GLU   E  77  ? 0.40971 0.40971 0.40971 0.00000  0.00000  0.00000  77  GLU   A OE2 
6192  N N   . PHE   E  78  ? 0.31121 0.31121 0.31121 0.00000  0.00000  0.00000  78  PHE   A N   
6193  C CA  . PHE   E  78  ? 0.57802 0.57802 0.57802 0.00000  0.00000  0.00000  78  PHE   A CA  
6194  C C   . PHE   E  78  ? 0.56874 0.56874 0.56874 0.00000  0.00000  0.00000  78  PHE   A C   
6195  O O   . PHE   E  78  ? 0.66578 0.66578 0.66578 0.00000  0.00000  0.00000  78  PHE   A O   
6196  C CB  . PHE   E  78  ? 0.33204 0.33204 0.33204 0.00000  0.00000  0.00000  78  PHE   A CB  
6197  C CG  . PHE   E  78  ? 0.56582 0.56582 0.56582 -0.00000 0.00000  0.00000  78  PHE   A CG  
6198  C CD1 . PHE   E  78  ? 0.39279 0.39279 0.39279 -0.00000 0.00000  0.00000  78  PHE   A CD1 
6199  C CD2 . PHE   E  78  ? 0.24652 0.24652 0.24652 -0.00000 0.00000  0.00000  78  PHE   A CD2 
6200  C CE1 . PHE   E  78  ? 0.36620 0.36620 0.36620 0.00000  0.00000  0.00000  78  PHE   A CE1 
6201  C CE2 . PHE   E  78  ? 0.49709 0.49709 0.49709 0.00000  0.00000  0.00000  78  PHE   A CE2 
6202  C CZ  . PHE   E  78  ? 0.33759 0.33759 0.33759 0.00000  0.00000  0.00000  78  PHE   A CZ  
6203  N N   . ILE   E  79  ? 0.47270 0.47270 0.47270 0.00000  0.00000  0.00000  79  ILE   A N   
6204  C CA  . ILE   E  79  ? 0.39227 0.39227 0.39227 0.00000  0.00000  0.00000  79  ILE   A CA  
6205  C C   . ILE   E  79  ? 0.60423 0.60423 0.60423 0.00000  0.00000  0.00000  79  ILE   A C   
6206  O O   . ILE   E  79  ? 0.30450 0.30450 0.30450 -0.00000 0.00000  0.00000  79  ILE   A O   
6207  C CB  . ILE   E  79  ? 0.50328 0.50328 0.50328 0.00000  0.00000  0.00000  79  ILE   A CB  
6208  C CG1 . ILE   E  79  ? 0.33163 0.33163 0.33163 0.00000  0.00000  0.00000  79  ILE   A CG1 
6209  C CG2 . ILE   E  79  ? 0.34180 0.34180 0.34180 0.00000  0.00000  0.00000  79  ILE   A CG2 
6210  C CD1 . ILE   E  79  ? 0.29678 0.29678 0.29678 0.00000  0.00000  0.00000  79  ILE   A CD1 
6211  N N   . ASP   E  80  ? 0.28054 0.28054 0.28054 -0.00000 -0.00000 0.00000  80  ASP   A N   
6212  C CA  . ASP   E  80  ? 0.48445 0.48445 0.48445 0.00000  0.00000  0.00000  80  ASP   A CA  
6213  C C   . ASP   E  80  ? 0.37271 0.37271 0.37271 0.00000  0.00000  0.00000  80  ASP   A C   
6214  O O   . ASP   E  80  ? 0.48864 0.48864 0.48864 0.00000  0.00000  0.00000  80  ASP   A O   
6215  C CB  . ASP   E  80  ? 0.40594 0.40594 0.40594 0.00000  0.00000  0.00000  80  ASP   A CB  
6216  C CG  . ASP   E  80  ? 0.63760 0.63760 0.63760 0.00000  0.00000  0.00000  80  ASP   A CG  
6217  O OD1 . ASP   E  80  ? 0.61462 0.61462 0.61462 0.00000  -0.00000 0.00000  80  ASP   A OD1 
6218  O OD2 . ASP   E  80  ? 0.71203 0.71203 0.71203 -0.00000 0.00000  0.00000  80  ASP   A OD2 
6219  N N   . MET   E  81  ? 0.42893 0.42893 0.42893 -0.00000 0.00000  0.00000  81  MET   A N   
6220  C CA  . MET   E  81  ? 0.34921 0.34921 0.34921 -0.00000 0.00000  0.00000  81  MET   A CA  
6221  C C   . MET   E  81  ? 0.63765 0.63765 0.63765 0.00000  0.00000  0.00000  81  MET   A C   
6222  O O   . MET   E  81  ? 0.47759 0.47759 0.47759 -0.00000 0.00000  0.00000  81  MET   A O   
6223  C CB  . MET   E  81  ? 0.34928 0.34928 0.34928 0.00000  0.00000  0.00000  81  MET   A CB  
6224  C CG  . MET   E  81  ? 0.43112 0.43112 0.43112 0.00000  -0.00000 -0.00000 81  MET   A CG  
6225  S SD  . MET   E  81  ? 0.42966 0.42966 0.42966 0.00000  0.00000  0.00000  81  MET   A SD  
6226  C CE  . MET   E  81  ? 0.38683 0.38683 0.38683 0.00000  0.00000  0.00000  81  MET   A CE  
6227  N N   . PHE   E  82  ? 0.32320 0.32320 0.32320 0.00000  0.00000  0.00000  82  PHE   A N   
6228  C CA  . PHE   E  82  ? 0.64490 0.64490 0.64490 -0.00000 0.00000  0.00000  82  PHE   A CA  
6229  C C   . PHE   E  82  ? 0.30118 0.30118 0.30118 -0.00000 0.00000  0.00000  82  PHE   A C   
6230  O O   . PHE   E  82  ? 1.10392 1.10392 1.10392 -0.00000 0.00000  0.00000  82  PHE   A O   
6231  C CB  . PHE   E  82  ? 0.33451 0.33451 0.33451 0.00000  0.00000  0.00000  82  PHE   A CB  
6232  C CG  . PHE   E  82  ? 0.88107 0.88107 0.88107 0.00000  0.00000  0.00000  82  PHE   A CG  
6233  C CD1 . PHE   E  82  ? 0.29753 0.29753 0.29753 -0.00000 -0.00000 0.00000  82  PHE   A CD1 
6234  C CD2 . PHE   E  82  ? 0.33061 0.33061 0.33061 -0.00000 0.00000  0.00000  82  PHE   A CD2 
6235  C CE1 . PHE   E  82  ? 0.53516 0.53516 0.53516 -0.00000 -0.00000 0.00000  82  PHE   A CE1 
6236  C CE2 . PHE   E  82  ? 0.55121 0.55121 0.55121 -0.00000 0.00000  0.00000  82  PHE   A CE2 
6237  C CZ  . PHE   E  82  ? 0.24350 0.24350 0.24350 -0.00000 0.00000  0.00000  82  PHE   A CZ  
6238  N N   . GLU   E  83  ? 0.67976 0.67976 0.67976 0.00000  0.00000  0.00000  83  GLU   A N   
6239  C CA  . GLU   E  83  ? 0.74010 0.74010 0.74010 -0.00000 0.00000  0.00000  83  GLU   A CA  
6240  C C   . GLU   E  83  ? 0.84558 0.84558 0.84558 0.00000  0.00000  0.00000  83  GLU   A C   
6241  O O   . GLU   E  83  ? 0.54497 0.54497 0.54497 -0.00000 0.00000  0.00000  83  GLU   A O   
6242  C CB  . GLU   E  83  ? 0.42770 0.42770 0.42770 0.00000  0.00000  0.00000  83  GLU   A CB  
6243  C CG  . GLU   E  83  ? 0.45088 0.45088 0.45088 0.00000  0.00000  0.00000  83  GLU   A CG  
6244  C CD  . GLU   E  83  ? 0.30951 0.30951 0.30951 -0.00000 0.00000  0.00000  83  GLU   A CD  
6245  O OE1 . GLU   E  83  ? 1.32622 1.32622 1.32622 -0.00000 0.00000  0.00000  83  GLU   A OE1 
6246  O OE2 . GLU   E  83  ? 0.81273 0.81273 0.81273 0.00000  0.00000  0.00000  83  GLU   A OE2 
6247  N N   . GLY   E  84  ? 0.98381 0.98381 0.98381 0.00000  0.00000  0.00000  84  GLY   A N   
6248  C CA  . GLY   E  84  ? 0.53239 0.53239 0.53239 0.00000  0.00000  0.00000  84  GLY   A CA  
6249  C C   . GLY   E  84  ? 0.95143 0.95143 0.95143 0.00000  0.00000  0.00000  84  GLY   A C   
6250  O O   . GLY   E  84  ? 0.76294 0.76294 0.76294 0.00000  0.00000  0.00000  84  GLY   A O   
6251  N N   . ILE   E  85  ? 0.96208 0.96208 0.96208 0.00000  0.00000  0.00000  85  ILE   A N   
6252  C CA  . ILE   E  85  ? 0.70384 0.70384 0.70384 0.00000  0.00000  0.00000  85  ILE   A CA  
6253  C C   . ILE   E  85  ? 0.83314 0.83314 0.83314 0.00000  0.00000  0.00000  85  ILE   A C   
6254  O O   . ILE   E  85  ? 0.75901 0.75901 0.75901 0.00000  0.00000  0.00000  85  ILE   A O   
6255  C CB  . ILE   E  85  ? 0.62045 0.62045 0.62045 0.00000  -0.00000 -0.00000 85  ILE   A CB  
6256  C CG1 . ILE   E  85  ? 0.81391 0.81391 0.81391 0.00000  0.00000  0.00000  85  ILE   A CG1 
6257  C CG2 . ILE   E  85  ? 0.64725 0.64725 0.64725 0.00000  0.00000  0.00000  85  ILE   A CG2 
6258  C CD1 . ILE   E  85  ? 0.71139 0.71139 0.71139 0.00000  0.00000  0.00000  85  ILE   A CD1 
6259  N N   . GLN   E  86  ? 0.82137 0.82137 0.82137 0.00000  0.00000  0.00000  86  GLN   A N   
6260  C CA  . GLN   E  86  ? 1.22178 1.22178 1.22178 0.00000  0.00000  0.00000  86  GLN   A CA  
6261  C C   . GLN   E  86  ? 0.59916 0.59916 0.59916 0.00000  0.00000  0.00000  86  GLN   A C   
6262  O O   . GLN   E  86  ? 1.19058 1.19058 1.19058 0.00000  0.00000  0.00000  86  GLN   A O   
6263  C CB  . GLN   E  86  ? 0.76755 0.76755 0.76755 -0.00000 0.00000  0.00000  86  GLN   A CB  
6264  N N   . ASP   E  87  ? 1.06699 1.06699 1.06699 -0.00000 0.00000  0.00000  87  ASP   A N   
6265  C CA  . ASP   E  87  ? 0.63983 0.63983 0.63983 0.00000  0.00000  0.00000  87  ASP   A CA  
6266  C C   . ASP   E  87  ? 0.50243 0.50243 0.50243 0.00000  0.00000  0.00000  87  ASP   A C   
6267  O O   . ASP   E  87  ? 0.76065 0.76065 0.76065 0.00000  0.00000  0.00000  87  ASP   A O   
6268  C CB  . ASP   E  87  ? 0.54173 0.54173 0.54173 -0.00000 0.00000  0.00000  87  ASP   A CB  
6269  C CG  . ASP   E  87  ? 1.46332 1.46332 1.46332 0.00000  0.00000  0.00000  87  ASP   A CG  
6270  O OD1 . ASP   E  87  ? 1.21325 1.21325 1.21325 0.00000  0.00000  0.00000  87  ASP   A OD1 
6271  O OD2 . ASP   E  87  ? 1.18842 1.18842 1.18842 -0.00000 0.00000  0.00000  87  ASP   A OD2 
6272  N N   . SER   E  88  ? 0.55897 0.55897 0.55897 -0.00000 0.00000  0.00000  88  SER   A N   
6273  C CA  . SER   E  88  ? 0.42064 0.42064 0.42064 -0.00000 0.00000  0.00000  88  SER   A CA  
6274  C C   . SER   E  88  ? 0.95749 0.95749 0.95749 -0.00000 0.00000  0.00000  88  SER   A C   
6275  O O   . SER   E  88  ? 0.54588 0.54588 0.54588 0.00000  0.00000  0.00000  88  SER   A O   
6276  C CB  . SER   E  88  ? 0.43392 0.43392 0.43392 -0.00000 0.00000  0.00000  88  SER   A CB  
6277  O OG  . SER   E  88  ? 0.63822 0.63822 0.63822 0.00000  0.00000  0.00000  88  SER   A OG  
6278  N N   . PRO   E  89  ? 0.60217 0.60217 0.60217 0.00000  -0.00000 0.00000  89  PRO   A N   
6279  C CA  . PRO   E  89  ? 0.30474 0.30474 0.30474 0.00000  0.00000  0.00000  89  PRO   A CA  
6280  C C   . PRO   E  89  ? 0.65563 0.65563 0.65563 0.00000  0.00000  0.00000  89  PRO   A C   
6281  O O   . PRO   E  89  ? 0.43524 0.43524 0.43524 -0.00000 -0.00000 0.00000  89  PRO   A O   
6282  C CB  . PRO   E  89  ? 0.58805 0.58805 0.58805 -0.00000 0.00000  0.00000  89  PRO   A CB  
6283  C CG  . PRO   E  89  ? 0.55853 0.55853 0.55853 0.00000  0.00000  -0.00000 89  PRO   A CG  
6284  C CD  . PRO   E  89  ? 0.49009 0.49009 0.49009 0.00000  0.00000  0.00000  89  PRO   A CD  
6285  N N   . ARG   E  90  ? 0.48030 0.48030 0.48030 0.00000  0.00000  0.00000  90  ARG   A N   
6286  C CA  . ARG   E  90  ? 0.69560 0.69560 0.69560 -0.00000 0.00000  0.00000  90  ARG   A CA  
6287  C C   . ARG   E  90  ? 0.57762 0.57762 0.57762 0.00000  0.00000  0.00000  90  ARG   A C   
6288  O O   . ARG   E  90  ? 0.57239 0.57239 0.57239 0.00000  0.00000  0.00000  90  ARG   A O   
6289  C CB  . ARG   E  90  ? 0.49791 0.49791 0.49791 0.00000  0.00000  0.00000  90  ARG   A CB  
6290  C CG  . ARG   E  90  ? 1.45588 1.45588 1.45588 -0.00000 0.00000  -0.00000 90  ARG   A CG  
6291  C CD  . ARG   E  90  ? 0.24447 0.24447 0.24447 0.00000  0.00000  0.00000  90  ARG   A CD  
6292  N NE  . ARG   E  90  ? 1.06310 1.06310 1.06310 -0.00000 0.00000  0.00000  90  ARG   A NE  
6293  C CZ  . ARG   E  90  ? 1.54477 1.54477 1.54477 0.00000  0.00000  0.00000  90  ARG   A CZ  
6294  N NH1 . ARG   E  90  ? 1.25601 1.25601 1.25601 0.00000  0.00000  0.00000  90  ARG   A NH1 
6295  N NH2 . ARG   E  90  ? 0.62770 0.62770 0.62770 -0.00000 0.00000  0.00000  90  ARG   A NH2 
6296  N N   . ASN   E  91  ? 0.44148 0.44148 0.44148 0.00000  0.00000  0.00000  91  ASN   A N   
6297  C CA  . ASN   E  91  ? 0.49822 0.49822 0.49822 0.00000  0.00000  0.00000  91  ASN   A CA  
6298  C C   . ASN   E  91  ? 0.48083 0.48083 0.48083 -0.00000 0.00000  0.00000  91  ASN   A C   
6299  O O   . ASN   E  91  ? 0.56383 0.56383 0.56383 0.00000  0.00000  0.00000  91  ASN   A O   
6300  C CB  . ASN   E  91  ? 0.39692 0.39692 0.39692 0.00000  0.00000  0.00000  91  ASN   A CB  
6301  C CG  . ASN   E  91  ? 0.53215 0.53215 0.53215 0.00000  0.00000  0.00000  91  ASN   A CG  
6302  O OD1 . ASN   E  91  ? 0.66121 0.66121 0.66121 0.00000  0.00000  0.00000  91  ASN   A OD1 
6303  N ND2 . ASN   E  91  ? 0.48182 0.48182 0.48182 0.00000  0.00000  0.00000  91  ASN   A ND2 
6304  N N   . TYR   E  92  ? 0.52094 0.52094 0.52094 0.00000  0.00000  0.00000  92  TYR   A N   
6305  C CA  . TYR   E  92  ? 0.44168 0.44168 0.44168 0.00000  0.00000  0.00000  92  TYR   A CA  
6306  C C   . TYR   E  92  ? 0.49353 0.49353 0.49353 0.00000  -0.00000 -0.00000 92  TYR   A C   
6307  O O   . TYR   E  92  ? 0.55327 0.55327 0.55327 0.00000  -0.00000 -0.00000 92  TYR   A O   
6308  C CB  . TYR   E  92  ? 0.30511 0.30511 0.30511 0.00000  0.00000  0.00000  92  TYR   A CB  
6309  C CG  . TYR   E  92  ? 0.37435 0.37435 0.37435 0.00000  0.00000  0.00000  92  TYR   A CG  
6310  C CD1 . TYR   E  92  ? 0.35178 0.35178 0.35178 0.00000  0.00000  0.00000  92  TYR   A CD1 
6311  C CD2 . TYR   E  92  ? 0.45583 0.45583 0.45583 -0.00000 -0.00000 0.00000  92  TYR   A CD2 
6312  C CE1 . TYR   E  92  ? 0.59218 0.59218 0.59218 0.00000  0.00000  0.00000  92  TYR   A CE1 
6313  C CE2 . TYR   E  92  ? 0.55538 0.55538 0.55538 0.00000  -0.00000 0.00000  92  TYR   A CE2 
6314  C CZ  . TYR   E  92  ? 0.49894 0.49894 0.49894 -0.00000 0.00000  0.00000  92  TYR   A CZ  
6315  O OH  . TYR   E  92  ? 0.71116 0.71116 0.71116 0.00000  0.00000  0.00000  92  TYR   A OH  
6316  N N   . GLN   E  93  ? 0.42992 0.42992 0.42992 -0.00000 0.00000  0.00000  93  GLN   A N   
6317  C CA  . GLN   E  93  ? 0.58960 0.58960 0.58960 0.00000  0.00000  0.00000  93  GLN   A CA  
6318  C C   . GLN   E  93  ? 0.41290 0.41290 0.41290 0.00000  0.00000  0.00000  93  GLN   A C   
6319  O O   . GLN   E  93  ? 0.48142 0.48142 0.48142 0.00000  -0.00000 0.00000  93  GLN   A O   
6320  C CB  . GLN   E  93  ? 0.34736 0.34736 0.34736 0.00000  0.00000  0.00000  93  GLN   A CB  
6321  C CG  . GLN   E  93  ? 0.55925 0.55925 0.55925 -0.00000 0.00000  0.00000  93  GLN   A CG  
6322  C CD  . GLN   E  93  ? 2.07029 2.07029 2.07029 0.00000  0.00000  0.00000  93  GLN   A CD  
6323  O OE1 . GLN   E  93  ? 0.52860 0.52860 0.52860 0.00000  0.00000  0.00000  93  GLN   A OE1 
6324  N NE2 . GLN   E  93  ? 0.55670 0.55670 0.55670 0.00000  0.00000  0.00000  93  GLN   A NE2 
6325  N N   . GLU   E  94  ? 0.60624 0.60624 0.60624 0.00000  0.00000  0.00000  94  GLU   A N   
6326  C CA  . GLU   E  94  ? 0.25596 0.25596 0.25596 0.00000  -0.00000 0.00000  94  GLU   A CA  
6327  C C   . GLU   E  94  ? 0.69297 0.69297 0.69297 0.00000  0.00000  0.00000  94  GLU   A C   
6328  O O   . GLU   E  94  ? 0.65572 0.65572 0.65572 0.00000  0.00000  0.00000  94  GLU   A O   
6329  C CB  . GLU   E  94  ? 0.65416 0.65416 0.65416 -0.00000 -0.00000 -0.00000 94  GLU   A CB  
6330  C CG  . GLU   E  94  ? 0.92701 0.92701 0.92701 -0.00000 0.00000  -0.00000 94  GLU   A CG  
6331  C CD  . GLU   E  94  ? 1.72110 1.72110 1.72110 0.00000  0.00000  0.00000  94  GLU   A CD  
6332  O OE1 . GLU   E  94  ? 0.56180 0.56180 0.56180 -0.00000 0.00000  0.00000  94  GLU   A OE1 
6333  O OE2 . GLU   E  94  ? 1.24201 1.24201 1.24201 0.00000  0.00000  0.00000  94  GLU   A OE2 
6334  N N   . LEU   E  95  ? 0.67124 0.67124 0.67124 0.00000  -0.00000 0.00000  95  LEU   A N   
6335  C CA  . LEU   E  95  ? 0.43115 0.43115 0.43115 0.00000  0.00000  0.00000  95  LEU   A CA  
6336  C C   . LEU   E  95  ? 0.48344 0.48344 0.48344 0.00000  0.00000  0.00000  95  LEU   A C   
6337  O O   . LEU   E  95  ? 0.43290 0.43290 0.43290 -0.00000 0.00000  0.00000  95  LEU   A O   
6338  C CB  . LEU   E  95  ? 0.52119 0.52119 0.52119 0.00000  0.00000  0.00000  95  LEU   A CB  
6339  C CG  . LEU   E  95  ? 0.52204 0.52204 0.52204 0.00000  0.00000  0.00000  95  LEU   A CG  
6340  C CD1 . LEU   E  95  ? 0.44970 0.44970 0.44970 -0.00000 0.00000  0.00000  95  LEU   A CD1 
6341  C CD2 . LEU   E  95  ? 0.33823 0.33823 0.33823 0.00000  0.00000  0.00000  95  LEU   A CD2 
6342  N N   . CYS   E  96  ? 0.31404 0.31404 0.31404 -0.00000 0.00000  0.00000  96  CYS   A N   
6343  C CA  . CYS   E  96  ? 0.45068 0.45068 0.45068 -0.00000 0.00000  0.00000  96  CYS   A CA  
6344  C C   . CYS   E  96  ? 0.45320 0.45320 0.45320 0.00000  0.00000  0.00000  96  CYS   A C   
6345  O O   . CYS   E  96  ? 0.69814 0.69814 0.69814 -0.00000 0.00000  0.00000  96  CYS   A O   
6346  C CB  . CYS   E  96  ? 0.36878 0.36878 0.36878 -0.00000 0.00000  0.00000  96  CYS   A CB  
6347  S SG  . CYS   E  96  ? 0.56768 0.56768 0.56768 0.00000  0.00000  0.00000  96  CYS   A SG  
6348  N N   . ASN   E  97  ? 0.47398 0.47398 0.47398 -0.00000 0.00000  0.00000  97  ASN   A N   
6349  C CA  . ASN   E  97  ? 0.35075 0.35075 0.35075 0.00000  0.00000  0.00000  97  ASN   A CA  
6350  C C   . ASN   E  97  ? 0.66522 0.66522 0.66522 0.00000  0.00000  0.00000  97  ASN   A C   
6351  O O   . ASN   E  97  ? 0.42980 0.42980 0.42980 0.00000  0.00000  -0.00000 97  ASN   A O   
6352  C CB  . ASN   E  97  ? 0.49673 0.49673 0.49673 -0.00000 0.00000  0.00000  97  ASN   A CB  
6353  C CG  . ASN   E  97  ? 0.99669 0.99669 0.99669 0.00000  0.00000  0.00000  97  ASN   A CG  
6354  O OD1 . ASN   E  97  ? 0.64923 0.64923 0.64923 -0.00000 0.00000  0.00000  97  ASN   A OD1 
6355  N ND2 . ASN   E  97  ? 0.45932 0.45932 0.45932 -0.00000 0.00000  0.00000  97  ASN   A ND2 
6356  N N   . MET   E  98  ? 0.34133 0.34133 0.34133 -0.00000 0.00000  0.00000  98  MET   A N   
6357  C CA  . MET   E  98  ? 0.29484 0.29484 0.29484 0.00000  0.00000  0.00000  98  MET   A CA  
6358  C C   . MET   E  98  ? 0.77670 0.77670 0.77670 -0.00000 0.00000  0.00000  98  MET   A C   
6359  O O   . MET   E  98  ? 0.52161 0.52161 0.52161 -0.00000 0.00000  0.00000  98  MET   A O   
6360  C CB  . MET   E  98  ? 0.38169 0.38169 0.38169 0.00000  -0.00000 0.00000  98  MET   A CB  
6361  C CG  . MET   E  98  ? 0.24229 0.24229 0.24229 0.00000  0.00000  0.00000  98  MET   A CG  
6362  S SD  . MET   E  98  ? 0.63624 0.63624 0.63624 0.00000  0.00000  0.00000  98  MET   A SD  
6363  C CE  . MET   E  98  ? 0.46777 0.46777 0.46777 -0.00000 0.00000  0.00000  98  MET   A CE  
6364  N N   . PHE   E  99  ? 0.38257 0.38257 0.38257 0.00000  0.00000  0.00000  99  PHE   A N   
6365  C CA  . PHE   E  99  ? 0.33227 0.33227 0.33227 -0.00000 0.00000  0.00000  99  PHE   A CA  
6366  C C   . PHE   E  99  ? 0.45066 0.45066 0.45066 -0.00000 -0.00000 -0.00000 99  PHE   A C   
6367  O O   . PHE   E  99  ? 0.43628 0.43628 0.43628 -0.00000 0.00000  0.00000  99  PHE   A O   
6368  C CB  . PHE   E  99  ? 0.31297 0.31297 0.31297 0.00000  0.00000  0.00000  99  PHE   A CB  
6369  C CG  . PHE   E  99  ? 0.41698 0.41698 0.41698 0.00000  -0.00000 0.00000  99  PHE   A CG  
6370  C CD1 . PHE   E  99  ? 0.28812 0.28812 0.28812 0.00000  0.00000  0.00000  99  PHE   A CD1 
6371  C CD2 . PHE   E  99  ? 0.39989 0.39989 0.39989 -0.00000 0.00000  0.00000  99  PHE   A CD2 
6372  C CE1 . PHE   E  99  ? 0.48501 0.48501 0.48501 0.00000  0.00000  0.00000  99  PHE   A CE1 
6373  C CE2 . PHE   E  99  ? 0.27722 0.27722 0.27722 -0.00000 0.00000  0.00000  99  PHE   A CE2 
6374  C CZ  . PHE   E  99  ? 0.32919 0.32919 0.32919 0.00000  0.00000  0.00000  99  PHE   A CZ  
6375  N N   . ASN   E  100 ? 0.33950 0.33950 0.33950 0.00000  0.00000  0.00000  100 ASN   A N   
6376  C CA  . ASN   E  100 ? 0.39336 0.39336 0.39336 -0.00000 0.00000  0.00000  100 ASN   A CA  
6377  C C   . ASN   E  100 ? 0.44129 0.44129 0.44129 0.00000  0.00000  0.00000  100 ASN   A C   
6378  O O   . ASN   E  100 ? 0.53319 0.53319 0.53319 -0.00000 0.00000  0.00000  100 ASN   A O   
6379  C CB  . ASN   E  100 ? 0.38688 0.38688 0.38688 0.00000  0.00000  0.00000  100 ASN   A CB  
6380  C CG  . ASN   E  100 ? 0.53192 0.53192 0.53192 -0.00000 0.00000  0.00000  100 ASN   A CG  
6381  O OD1 . ASN   E  100 ? 0.69209 0.69209 0.69209 -0.00000 0.00000  0.00000  100 ASN   A OD1 
6382  N ND2 . ASN   E  100 ? 0.52786 0.52786 0.52786 0.00000  0.00000  0.00000  100 ASN   A ND2 
6383  N N   . ASP   E  101 ? 0.41375 0.41375 0.41375 0.00000  0.00000  0.00000  101 ASP   A N   
6384  C CA  . ASP   E  101 ? 0.33429 0.33429 0.33429 0.00000  0.00000  0.00000  101 ASP   A CA  
6385  C C   . ASP   E  101 ? 0.62130 0.62130 0.62130 0.00000  0.00000  0.00000  101 ASP   A C   
6386  O O   . ASP   E  101 ? 0.51585 0.51585 0.51585 0.00000  0.00000  0.00000  101 ASP   A O   
6387  C CB  . ASP   E  101 ? 0.33525 0.33525 0.33525 -0.00000 0.00000  0.00000  101 ASP   A CB  
6388  C CG  . ASP   E  101 ? 1.38342 1.38342 1.38342 -0.00000 0.00000  0.00000  101 ASP   A CG  
6389  O OD1 . ASP   E  101 ? 0.56385 0.56385 0.56385 0.00000  0.00000  0.00000  101 ASP   A OD1 
6390  O OD2 . ASP   E  101 ? 0.68615 0.68615 0.68615 0.00000  0.00000  0.00000  101 ASP   A OD2 
6391  N N   . ILE   E  102 ? 0.54776 0.54776 0.54776 0.00000  0.00000  0.00000  102 ILE   A N   
6392  C CA  . ILE   E  102 ? 0.35089 0.35089 0.35089 0.00000  0.00000  0.00000  102 ILE   A CA  
6393  C C   . ILE   E  102 ? 0.67464 0.67464 0.67464 0.00000  0.00000  0.00000  102 ILE   A C   
6394  O O   . ILE   E  102 ? 0.46614 0.46614 0.46614 -0.00000 0.00000  0.00000  102 ILE   A O   
6395  C CB  . ILE   E  102 ? 0.38672 0.38672 0.38672 0.00000  0.00000  0.00000  102 ILE   A CB  
6396  C CG1 . ILE   E  102 ? 0.19443 0.19443 0.19443 0.00000  0.00000  0.00000  102 ILE   A CG1 
6397  C CG2 . ILE   E  102 ? 0.25034 0.25034 0.25034 0.00000  -0.00000 0.00000  102 ILE   A CG2 
6398  C CD1 . ILE   E  102 ? 0.46148 0.46148 0.46148 0.00000  0.00000  0.00000  102 ILE   A CD1 
6399  N N   . PHE   E  103 ? 0.37696 0.37696 0.37696 -0.00000 0.00000  0.00000  103 PHE   A N   
6400  C CA  . PHE   E  103 ? 0.68743 0.68743 0.68743 0.00000  0.00000  0.00000  103 PHE   A CA  
6401  C C   . PHE   E  103 ? 0.40733 0.40733 0.40733 0.00000  0.00000  0.00000  103 PHE   A C   
6402  O O   . PHE   E  103 ? 0.51322 0.51322 0.51322 -0.00000 -0.00000 0.00000  103 PHE   A O   
6403  C CB  . PHE   E  103 ? 0.27464 0.27464 0.27464 0.00000  0.00000  0.00000  103 PHE   A CB  
6404  C CG  . PHE   E  103 ? 0.49322 0.49322 0.49322 -0.00000 0.00000  -0.00000 103 PHE   A CG  
6405  C CD1 . PHE   E  103 ? 0.44225 0.44225 0.44225 0.00000  0.00000  0.00000  103 PHE   A CD1 
6406  C CD2 . PHE   E  103 ? 0.34162 0.34162 0.34162 -0.00000 0.00000  0.00000  103 PHE   A CD2 
6407  C CE1 . PHE   E  103 ? 0.59737 0.59737 0.59737 0.00000  -0.00000 0.00000  103 PHE   A CE1 
6408  C CE2 . PHE   E  103 ? 0.49528 0.49528 0.49528 -0.00000 0.00000  0.00000  103 PHE   A CE2 
6409  C CZ  . PHE   E  103 ? 0.48620 0.48620 0.48620 0.00000  0.00000  0.00000  103 PHE   A CZ  
6410  N N   . ARG   E  104 ? 0.45008 0.45008 0.45008 0.00000  0.00000  0.00000  104 ARG   A N   
6411  C CA  . ARG   E  104 ? 0.22873 0.22873 0.22873 0.00000  0.00000  0.00000  104 ARG   A CA  
6412  C C   . ARG   E  104 ? 0.48188 0.48188 0.48188 -0.00000 0.00000  0.00000  104 ARG   A C   
6413  O O   . ARG   E  104 ? 0.65736 0.65736 0.65736 -0.00000 0.00000  0.00000  104 ARG   A O   
6414  C CB  . ARG   E  104 ? 0.35470 0.35470 0.35470 0.00000  0.00000  0.00000  104 ARG   A CB  
6415  C CG  . ARG   E  104 ? 0.23889 0.23889 0.23889 0.00000  0.00000  0.00000  104 ARG   A CG  
6416  C CD  . ARG   E  104 ? 0.76358 0.76358 0.76358 -0.00000 0.00000  -0.00000 104 ARG   A CD  
6417  N NE  . ARG   E  104 ? 0.78129 0.78129 0.78129 -0.00000 0.00000  0.00000  104 ARG   A NE  
6418  C CZ  . ARG   E  104 ? 1.15875 1.15875 1.15875 0.00000  0.00000  0.00000  104 ARG   A CZ  
6419  N NH1 . ARG   E  104 ? 1.34254 1.34254 1.34254 -0.00000 0.00000  0.00000  104 ARG   A NH1 
6420  N NH2 . ARG   E  104 ? 1.04677 1.04677 1.04677 -0.00000 0.00000  0.00000  104 ARG   A NH2 
6421  N N   . LYS   E  105 ? 0.40353 0.40353 0.40353 0.00000  0.00000  0.00000  105 LYS   A N   
6422  C CA  . LYS   E  105 ? 0.66617 0.66617 0.66617 0.00000  0.00000  0.00000  105 LYS   A CA  
6423  C C   . LYS   E  105 ? 0.44492 0.44492 0.44492 -0.00000 0.00000  0.00000  105 LYS   A C   
6424  O O   . LYS   E  105 ? 0.50353 0.50353 0.50353 0.00000  0.00000  0.00000  105 LYS   A O   
6425  C CB  . LYS   E  105 ? 0.54227 0.54227 0.54227 0.00000  0.00000  0.00000  105 LYS   A CB  
6426  C CG  . LYS   E  105 ? 0.41492 0.41492 0.41492 -0.00000 0.00000  0.00000  105 LYS   A CG  
6427  C CD  . LYS   E  105 ? 0.42081 0.42081 0.42081 -0.00000 0.00000  0.00000  105 LYS   A CD  
6428  C CE  . LYS   E  105 ? 0.80339 0.80339 0.80339 -0.00000 0.00000  0.00000  105 LYS   A CE  
6429  N NZ  . LYS   E  105 ? 0.96617 0.96617 0.96617 0.00000  0.00000  0.00000  105 LYS   A NZ  
6430  N N   . ALA   E  106 ? 0.65376 0.65376 0.65376 0.00000  0.00000  0.00000  106 ALA   A N   
6431  C CA  . ALA   E  106 ? 0.56842 0.56842 0.56842 0.00000  0.00000  0.00000  106 ALA   A CA  
6432  C C   . ALA   E  106 ? 0.35806 0.35806 0.35806 -0.00000 0.00000  0.00000  106 ALA   A C   
6433  O O   . ALA   E  106 ? 0.60313 0.60313 0.60313 -0.00000 0.00000  0.00000  106 ALA   A O   
6434  C CB  . ALA   E  106 ? 0.39500 0.39500 0.39500 0.00000  0.00000  0.00000  106 ALA   A CB  
6435  N N   . PRO   E  107 ? 0.65657 0.65657 0.65657 0.00000  -0.00000 -0.00000 107 PRO   A N   
6436  C CA  . PRO   E  107 ? 0.43280 0.43280 0.43280 0.00000  0.00000  0.00000  107 PRO   A CA  
6437  C C   . PRO   E  107 ? 0.55797 0.55797 0.55797 0.00000  0.00000  0.00000  107 PRO   A C   
6438  O O   . PRO   E  107 ? 0.49798 0.49798 0.49798 0.00000  -0.00000 0.00000  107 PRO   A O   
6439  C CB  . PRO   E  107 ? 0.40818 0.40818 0.40818 0.00000  0.00000  0.00000  107 PRO   A CB  
6440  C CG  . PRO   E  107 ? 0.36526 0.36526 0.36526 0.00000  0.00000  0.00000  107 PRO   A CG  
6441  C CD  . PRO   E  107 ? 0.28710 0.28710 0.28710 0.00000  0.00000  0.00000  107 PRO   A CD  
6442  N N   . VAL   E  108 ? 0.46417 0.46417 0.46417 0.00000  0.00000  0.00000  108 VAL   A N   
6443  C CA  . VAL   E  108 ? 0.41181 0.41181 0.41181 -0.00000 0.00000  0.00000  108 VAL   A CA  
6444  C C   . VAL   E  108 ? 0.55407 0.55407 0.55407 0.00000  0.00000  0.00000  108 VAL   A C   
6445  O O   . VAL   E  108 ? 0.56186 0.56186 0.56186 0.00000  0.00000  0.00000  108 VAL   A O   
6446  C CB  . VAL   E  108 ? 0.54145 0.54145 0.54145 0.00000  0.00000  0.00000  108 VAL   A CB  
6447  C CG1 . VAL   E  108 ? 0.30110 0.30110 0.30110 -0.00000 0.00000  0.00000  108 VAL   A CG1 
6448  C CG2 . VAL   E  108 ? 0.29788 0.29788 0.29788 0.00000  0.00000  0.00000  108 VAL   A CG2 
6449  N N   . TYR   E  109 ? 0.47649 0.47649 0.47649 0.00000  0.00000  0.00000  109 TYR   A N   
6450  C CA  . TYR   E  109 ? 0.84952 0.84952 0.84952 0.00000  0.00000  0.00000  109 TYR   A CA  
6451  C C   . TYR   E  109 ? 0.47290 0.47290 0.47290 0.00000  0.00000  0.00000  109 TYR   A C   
6452  O O   . TYR   E  109 ? 0.64926 0.64926 0.64926 0.00000  0.00000  0.00000  109 TYR   A O   
6453  C CB  . TYR   E  109 ? 0.39887 0.39887 0.39887 0.00000  0.00000  0.00000  109 TYR   A CB  
6454  C CG  . TYR   E  109 ? 0.81435 0.81435 0.81435 0.00000  0.00000  0.00000  109 TYR   A CG  
6455  C CD1 . TYR   E  109 ? 0.41528 0.41528 0.41528 -0.00000 0.00000  0.00000  109 TYR   A CD1 
6456  C CD2 . TYR   E  109 ? 0.46567 0.46567 0.46567 0.00000  0.00000  0.00000  109 TYR   A CD2 
6457  C CE1 . TYR   E  109 ? 0.94306 0.94306 0.94306 0.00000  0.00000  0.00000  109 TYR   A CE1 
6458  C CE2 . TYR   E  109 ? 0.73343 0.73343 0.73343 0.00000  0.00000  0.00000  109 TYR   A CE2 
6459  C CZ  . TYR   E  109 ? 0.43221 0.43221 0.43221 0.00000  0.00000  0.00000  109 TYR   A CZ  
6460  O OH  . TYR   E  109 ? 0.76493 0.76493 0.76493 0.00000  0.00000  0.00000  109 TYR   A OH  
6461  N N   . GLY   E  110 ? 0.63226 0.63226 0.63226 -0.00000 0.00000  0.00000  110 GLY   A N   
6462  C CA  . GLY   E  110 ? 0.18897 0.18897 0.18897 0.00000  0.00000  0.00000  110 GLY   A CA  
6463  C C   . GLY   E  110 ? 0.61575 0.61575 0.61575 0.00000  0.00000  0.00000  110 GLY   A C   
6464  O O   . GLY   E  110 ? 0.53978 0.53978 0.53978 0.00000  0.00000  0.00000  110 GLY   A O   
6465  N N   . ASP   E  111 ? 0.65077 0.65077 0.65077 -0.00000 0.00000  0.00000  111 ASP   A N   
6466  C CA  . ASP   E  111 ? 0.53145 0.53145 0.53145 0.00000  0.00000  0.00000  111 ASP   A CA  
6467  C C   . ASP   E  111 ? 0.32940 0.32940 0.32940 -0.00000 0.00000  0.00000  111 ASP   A C   
6468  O O   . ASP   E  111 ? 0.49825 0.49825 0.49825 0.00000  0.00000  0.00000  111 ASP   A O   
6469  C CB  . ASP   E  111 ? 0.69270 0.69270 0.69270 0.00000  0.00000  0.00000  111 ASP   A CB  
6470  C CG  . ASP   E  111 ? 0.67637 0.67637 0.67637 0.00000  0.00000  0.00000  111 ASP   A CG  
6471  O OD1 . ASP   E  111 ? 0.87670 0.87670 0.87670 -0.00000 0.00000  0.00000  111 ASP   A OD1 
6472  O OD2 . ASP   E  111 ? 1.11567 1.11567 1.11567 0.00000  -0.00000 0.00000  111 ASP   A OD2 
6473  N N   . LEU   E  112 ? 0.42178 0.42178 0.42178 -0.00000 0.00000  0.00000  112 LEU   A N   
6474  C CA  . LEU   E  112 ? 0.20779 0.20779 0.20779 0.00000  0.00000  0.00000  112 LEU   A CA  
6475  C C   . LEU   E  112 ? 0.67087 0.67087 0.67087 -0.00000 0.00000  0.00000  112 LEU   A C   
6476  O O   . LEU   E  112 ? 0.35147 0.35147 0.35147 -0.00000 0.00000  0.00000  112 LEU   A O   
6477  C CB  . LEU   E  112 ? 0.91495 0.91495 0.91495 -0.00000 0.00000  0.00000  112 LEU   A CB  
6478  C CG  . LEU   E  112 ? 0.96729 0.96729 0.96729 -0.00000 0.00000  0.00000  112 LEU   A CG  
6479  C CD1 . LEU   E  112 ? 1.16862 1.16862 1.16862 0.00000  0.00000  0.00000  112 LEU   A CD1 
6480  C CD2 . LEU   E  112 ? 1.22068 1.22068 1.22068 0.00000  0.00000  0.00000  112 LEU   A CD2 
6481  N N   . GLY   E  113 ? 0.40726 0.40726 0.40726 -0.00000 0.00000  0.00000  113 GLY   A N   
6482  C CA  . GLY   E  113 ? 0.38799 0.38799 0.38799 -0.00000 0.00000  0.00000  113 GLY   A CA  
6483  C C   . GLY   E  113 ? 0.43346 0.43346 0.43346 0.00000  0.00000  0.00000  113 GLY   A C   
6484  O O   . GLY   E  113 ? 0.41368 0.41368 0.41368 0.00000  0.00000  0.00000  113 GLY   A O   
6485  N N   . PRO   E  114 ? 0.36109 0.36109 0.36109 -0.00000 0.00000  0.00000  114 PRO   A N   
6486  C CA  . PRO   E  114 ? 0.27646 0.27646 0.27646 -0.00000 0.00000  0.00000  114 PRO   A CA  
6487  C C   . PRO   E  114 ? 0.31395 0.31395 0.31395 -0.00000 0.00000  0.00000  114 PRO   A C   
6488  O O   . PRO   E  114 ? 0.37055 0.37055 0.37055 0.00000  0.00000  0.00000  114 PRO   A O   
6489  C CB  . PRO   E  114 ? 0.33993 0.33993 0.33993 0.00000  0.00000  0.00000  114 PRO   A CB  
6490  C CG  . PRO   E  114 ? 0.30137 0.30137 0.30137 -0.00000 0.00000  0.00000  114 PRO   A CG  
6491  C CD  . PRO   E  114 ? 0.31512 0.31512 0.31512 -0.00000 0.00000  0.00000  114 PRO   A CD  
6492  N N   . PRO   E  115 ? 0.37536 0.37536 0.37536 -0.00000 0.00000  0.00000  115 PRO   A N   
6493  C CA  . PRO   E  115 ? 0.51449 0.51449 0.51449 0.00000  0.00000  0.00000  115 PRO   A CA  
6494  C C   . PRO   E  115 ? 0.41442 0.41442 0.41442 -0.00000 0.00000  0.00000  115 PRO   A C   
6495  O O   . PRO   E  115 ? 0.47893 0.47893 0.47893 -0.00000 0.00000  0.00000  115 PRO   A O   
6496  C CB  . PRO   E  115 ? 0.28364 0.28364 0.28364 -0.00000 0.00000  0.00000  115 PRO   A CB  
6497  C CG  . PRO   E  115 ? 0.31604 0.31604 0.31604 0.00000  -0.00000 0.00000  115 PRO   A CG  
6498  C CD  . PRO   E  115 ? 0.44228 0.44228 0.44228 0.00000  0.00000  0.00000  115 PRO   A CD  
6499  N N   . VAL   E  116 ? 0.51078 0.51078 0.51078 0.00000  -0.00000 0.00000  116 VAL   A N   
6500  C CA  . VAL   E  116 ? 0.38744 0.38744 0.38744 -0.00000 0.00000  0.00000  116 VAL   A CA  
6501  C C   . VAL   E  116 ? 0.41886 0.41886 0.41886 -0.00000 0.00000  0.00000  116 VAL   A C   
6502  O O   . VAL   E  116 ? 0.46412 0.46412 0.46412 0.00000  0.00000  0.00000  116 VAL   A O   
6503  C CB  . VAL   E  116 ? 0.47825 0.47825 0.47825 0.00000  0.00000  0.00000  116 VAL   A CB  
6504  C CG1 . VAL   E  116 ? 0.37787 0.37787 0.37787 0.00000  0.00000  0.00000  116 VAL   A CG1 
6505  C CG2 . VAL   E  116 ? 0.27604 0.27604 0.27604 0.00000  0.00000  0.00000  116 VAL   A CG2 
6506  N N   . TYR   E  117 ? 0.28577 0.28577 0.28577 -0.00000 0.00000  0.00000  117 TYR   A N   
6507  C CA  . TYR   E  117 ? 0.45717 0.45717 0.45717 0.00000  0.00000  0.00000  117 TYR   A CA  
6508  C C   . TYR   E  117 ? 0.38144 0.38144 0.38144 -0.00000 0.00000  0.00000  117 TYR   A C   
6509  O O   . TYR   E  117 ? 0.44491 0.44491 0.44491 0.00000  0.00000  0.00000  117 TYR   A O   
6510  C CB  . TYR   E  117 ? 0.27460 0.27460 0.27460 -0.00000 0.00000  0.00000  117 TYR   A CB  
6511  C CG  . TYR   E  117 ? 0.36668 0.36668 0.36668 -0.00000 0.00000  0.00000  117 TYR   A CG  
6512  C CD1 . TYR   E  117 ? 0.31892 0.31892 0.31892 0.00000  0.00000  0.00000  117 TYR   A CD1 
6513  C CD2 . TYR   E  117 ? 0.53055 0.53055 0.53055 0.00000  0.00000  0.00000  117 TYR   A CD2 
6514  C CE1 . TYR   E  117 ? 0.32439 0.32439 0.32439 -0.00000 0.00000  0.00000  117 TYR   A CE1 
6515  C CE2 . TYR   E  117 ? 0.24451 0.24451 0.24451 0.00000  0.00000  0.00000  117 TYR   A CE2 
6516  C CZ  . TYR   E  117 ? 0.45257 0.45257 0.45257 0.00000  0.00000  0.00000  117 TYR   A CZ  
6517  O OH  . TYR   E  117 ? 0.32267 0.32267 0.32267 -0.00000 0.00000  0.00000  117 TYR   A OH  
6518  N N   . MET   E  118 ? 0.45933 0.45933 0.45933 -0.00000 0.00000  0.00000  118 MET   A N   
6519  C CA  . MET   E  118 ? 0.33055 0.33055 0.33055 0.00000  0.00000  0.00000  118 MET   A CA  
6520  C C   . MET   E  118 ? 0.52839 0.52839 0.52839 0.00000  0.00000  0.00000  118 MET   A C   
6521  O O   . MET   E  118 ? 0.42919 0.42919 0.42919 0.00000  0.00000  0.00000  118 MET   A O   
6522  C CB  . MET   E  118 ? 0.36942 0.36942 0.36942 0.00000  0.00000  0.00000  118 MET   A CB  
6523  C CG  . MET   E  118 ? 0.23860 0.23860 0.23860 0.00000  0.00000  0.00000  118 MET   A CG  
6524  S SD  . MET   E  118 ? 0.46930 0.46930 0.46930 -0.00000 0.00000  0.00000  118 MET   A SD  
6525  C CE  . MET   E  118 ? 0.52721 0.52721 0.52721 0.00000  0.00000  0.00000  118 MET   A CE  
6526  N N   . ILE   E  119 ? 0.31564 0.31564 0.31564 -0.00000 0.00000  0.00000  119 ILE   A N   
6527  C CA  . ILE   E  119 ? 0.46102 0.46102 0.46102 0.00000  0.00000  0.00000  119 ILE   A CA  
6528  C C   . ILE   E  119 ? 0.46653 0.46653 0.46653 0.00000  0.00000  0.00000  119 ILE   A C   
6529  O O   . ILE   E  119 ? 0.52558 0.52558 0.52558 0.00000  0.00000  0.00000  119 ILE   A O   
6530  C CB  . ILE   E  119 ? 0.35935 0.35935 0.35935 0.00000  0.00000  -0.00000 119 ILE   A CB  
6531  C CG1 . ILE   E  119 ? 0.38835 0.38835 0.38835 0.00000  0.00000  0.00000  119 ILE   A CG1 
6532  C CG2 . ILE   E  119 ? 0.45446 0.45446 0.45446 0.00000  0.00000  0.00000  119 ILE   A CG2 
6533  C CD1 . ILE   E  119 ? 0.45013 0.45013 0.45013 0.00000  0.00000  0.00000  119 ILE   A CD1 
6534  N N   . MET   E  120 ? 0.37637 0.37637 0.37637 -0.00000 0.00000  0.00000  120 MET   A N   
6535  C CA  . MET   E  120 ? 0.35102 0.35102 0.35102 0.00000  0.00000  0.00000  120 MET   A CA  
6536  C C   . MET   E  120 ? 0.42487 0.42487 0.42487 -0.00000 0.00000  0.00000  120 MET   A C   
6537  O O   . MET   E  120 ? 0.41987 0.41987 0.41987 -0.00000 0.00000  0.00000  120 MET   A O   
6538  C CB  . MET   E  120 ? 0.19429 0.19429 0.19429 0.00000  0.00000  0.00000  120 MET   A CB  
6539  C CG  . MET   E  120 ? 0.29423 0.29423 0.29423 0.00000  0.00000  0.00000  120 MET   A CG  
6540  S SD  . MET   E  120 ? 0.49838 0.49838 0.49838 0.00000  0.00000  0.00000  120 MET   A SD  
6541  C CE  . MET   E  120 ? 0.30385 0.30385 0.30385 0.00000  0.00000  0.00000  120 MET   A CE  
6542  N N   . ALA   E  121 ? 0.36424 0.36424 0.36424 0.00000  -0.00000 0.00000  121 ALA   A N   
6543  C CA  . ALA   E  121 ? 0.43750 0.43750 0.43750 0.00000  0.00000  0.00000  121 ALA   A CA  
6544  C C   . ALA   E  121 ? 0.44226 0.44226 0.44226 -0.00000 0.00000  0.00000  121 ALA   A C   
6545  O O   . ALA   E  121 ? 0.53058 0.53058 0.53058 0.00000  0.00000  0.00000  121 ALA   A O   
6546  C CB  . ALA   E  121 ? 0.33512 0.33512 0.33512 0.00000  0.00000  0.00000  121 ALA   A CB  
6547  N N   . LYS   E  122 ? 0.41306 0.41306 0.41306 0.00000  0.00000  0.00000  122 LYS   A N   
6548  C CA  . LYS   E  122 ? 0.31854 0.31854 0.31854 0.00000  0.00000  0.00000  122 LYS   A CA  
6549  C C   . LYS   E  122 ? 0.49870 0.49870 0.49870 0.00000  0.00000  0.00000  122 LYS   A C   
6550  O O   . LYS   E  122 ? 0.42058 0.42058 0.42058 0.00000  0.00000  0.00000  122 LYS   A O   
6551  C CB  . LYS   E  122 ? 0.31112 0.31112 0.31112 -0.00000 0.00000  0.00000  122 LYS   A CB  
6552  N N   . LEU   E  123 ? 0.46317 0.46317 0.46317 0.00000  0.00000  0.00000  123 LEU   A N   
6553  C CA  . LEU   E  123 ? 0.45685 0.45685 0.45685 0.00000  0.00000  0.00000  123 LEU   A CA  
6554  C C   . LEU   E  123 ? 0.77334 0.77334 0.77334 0.00000  0.00000  0.00000  123 LEU   A C   
6555  O O   . LEU   E  123 ? 0.35640 0.35640 0.35640 -0.00000 0.00000  0.00000  123 LEU   A O   
6556  C CB  . LEU   E  123 ? 0.34396 0.34396 0.34396 0.00000  0.00000  0.00000  123 LEU   A CB  
6557  C CG  . LEU   E  123 ? 0.45722 0.45722 0.45722 -0.00000 0.00000  0.00000  123 LEU   A CG  
6558  C CD1 . LEU   E  123 ? 0.38318 0.38318 0.38318 0.00000  0.00000  0.00000  123 LEU   A CD1 
6559  C CD2 . LEU   E  123 ? 0.38102 0.38102 0.38102 0.00000  0.00000  0.00000  123 LEU   A CD2 
6560  N N   . MET   E  124 ? 0.34731 0.34731 0.34731 0.00000  0.00000  0.00000  124 MET   A N   
6561  C CA  . MET   E  124 ? 0.49158 0.49158 0.49158 0.00000  0.00000  0.00000  124 MET   A CA  
6562  C C   . MET   E  124 ? 0.39744 0.39744 0.39744 -0.00000 -0.00000 0.00000  124 MET   A C   
6563  O O   . MET   E  124 ? 0.38667 0.38667 0.38667 0.00000  0.00000  0.00000  124 MET   A O   
6564  C CB  . MET   E  124 ? 0.20767 0.20767 0.20767 0.00000  0.00000  0.00000  124 MET   A CB  
6565  C CG  . MET   E  124 ? 0.46407 0.46407 0.46407 -0.00000 0.00000  0.00000  124 MET   A CG  
6566  S SD  . MET   E  124 ? 0.48796 0.48796 0.48796 0.00000  0.00000  0.00000  124 MET   A SD  
6567  C CE  . MET   E  124 ? 0.17984 0.17984 0.17984 0.00000  0.00000  0.00000  124 MET   A CE  
6568  N N   . ASN   E  125 ? 0.43382 0.43382 0.43382 0.00000  0.00000  0.00000  125 ASN   A N   
6569  C CA  . ASN   E  125 ? 0.35633 0.35633 0.35633 -0.00000 0.00000  0.00000  125 ASN   A CA  
6570  C C   . ASN   E  125 ? 0.42756 0.42756 0.42756 -0.00000 0.00000  0.00000  125 ASN   A C   
6571  O O   . ASN   E  125 ? 0.47807 0.47807 0.47807 -0.00000 0.00000  0.00000  125 ASN   A O   
6572  C CB  . ASN   E  125 ? 0.33716 0.33716 0.33716 0.00000  0.00000  0.00000  125 ASN   A CB  
6573  C CG  . ASN   E  125 ? 0.31349 0.31349 0.31349 0.00000  0.00000  0.00000  125 ASN   A CG  
6574  O OD1 . ASN   E  125 ? 0.39154 0.39154 0.39154 0.00000  0.00000  0.00000  125 ASN   A OD1 
6575  N ND2 . ASN   E  125 ? 0.53276 0.53276 0.53276 0.00000  0.00000  0.00000  125 ASN   A ND2 
6576  N N   . THR   E  126 ? 0.40816 0.40816 0.40816 0.00000  0.00000  0.00000  126 THR   A N   
6577  C CA  . THR   E  126 ? 0.52328 0.52328 0.52328 -0.00000 0.00000  0.00000  126 THR   A CA  
6578  C C   . THR   E  126 ? 0.25567 0.25567 0.25567 0.00000  0.00000  0.00000  126 THR   A C   
6579  O O   . THR   E  126 ? 0.49533 0.49533 0.49533 0.00000  0.00000  0.00000  126 THR   A O   
6580  C CB  . THR   E  126 ? 0.33014 0.33014 0.33014 0.00000  0.00000  0.00000  126 THR   A CB  
6581  O OG1 . THR   E  126 ? 0.32282 0.32282 0.32282 0.00000  0.00000  0.00000  126 THR   A OG1 
6582  C CG2 . THR   E  126 ? 0.14042 0.14042 0.14042 -0.00000 0.00000  0.00000  126 THR   A CG2 
6583  N N   . ARG   E  127 ? 0.62867 0.62867 0.62867 0.00000  0.00000  0.00000  127 ARG   A N   
6584  C CA  . ARG   E  127 ? 0.29952 0.29952 0.29952 0.00000  0.00000  0.00000  127 ARG   A CA  
6585  C C   . ARG   E  127 ? 0.40500 0.40500 0.40500 -0.00000 0.00000  0.00000  127 ARG   A C   
6586  O O   . ARG   E  127 ? 0.21397 0.21397 0.21397 0.00000  0.00000  0.00000  127 ARG   A O   
6587  C CB  . ARG   E  127 ? 0.44084 0.44084 0.44084 0.00000  0.00000  0.00000  127 ARG   A CB  
6588  C CG  . ARG   E  127 ? 1.02580 1.02580 1.02580 0.00000  0.00000  0.00000  127 ARG   A CG  
6589  C CD  . ARG   E  127 ? 0.75324 0.75324 0.75324 0.00000  0.00000  -0.00000 127 ARG   A CD  
6590  N NE  . ARG   E  127 ? 1.54469 1.54469 1.54469 -0.00000 0.00000  0.00000  127 ARG   A NE  
6591  C CZ  . ARG   E  127 ? 1.34765 1.34765 1.34765 0.00000  0.00000  0.00000  127 ARG   A CZ  
6592  N NH1 . ARG   E  127 ? 1.05293 1.05293 1.05293 0.00000  0.00000  0.00000  127 ARG   A NH1 
6593  N NH2 . ARG   E  127 ? 1.28456 1.28456 1.28456 -0.00000 0.00000  0.00000  127 ARG   A NH2 
6594  N N   . ALA   E  128 ? 0.24940 0.24940 0.24940 -0.00000 0.00000  0.00000  128 ALA   A N   
6595  C CA  . ALA   E  128 ? 0.41368 0.41368 0.41368 0.00000  0.00000  -0.00000 128 ALA   A CA  
6596  C C   . ALA   E  128 ? 0.29883 0.29883 0.29883 0.00000  0.00000  0.00000  128 ALA   A C   
6597  O O   . ALA   E  128 ? 0.43611 0.43611 0.43611 -0.00000 0.00000  0.00000  128 ALA   A O   
6598  C CB  . ALA   E  128 ? 0.27143 0.27143 0.27143 0.00000  0.00000  0.00000  128 ALA   A CB  
6599  N N   . GLY   E  129 ? 0.61203 0.61203 0.61203 -0.00000 0.00000  0.00000  129 GLY   A N   
6600  C CA  . GLY   E  129 ? 0.20687 0.20687 0.20687 -0.00000 0.00000  0.00000  129 GLY   A CA  
6601  C C   . GLY   E  129 ? 0.51712 0.51712 0.51712 -0.00000 0.00000  0.00000  129 GLY   A C   
6602  O O   . GLY   E  129 ? 0.38851 0.38851 0.38851 0.00000  0.00000  0.00000  129 GLY   A O   
6603  N N   . PHE   E  130 ? 0.32510 0.32510 0.32510 -0.00000 0.00000  0.00000  130 PHE   A N   
6604  C CA  . PHE   E  130 ? 0.32619 0.32619 0.32619 -0.00000 0.00000  0.00000  130 PHE   A CA  
6605  C C   . PHE   E  130 ? 0.59129 0.59129 0.59129 0.00000  0.00000  0.00000  130 PHE   A C   
6606  O O   . PHE   E  130 ? 0.47927 0.47927 0.47927 -0.00000 0.00000  0.00000  130 PHE   A O   
6607  C CB  . PHE   E  130 ? 0.18171 0.18171 0.18171 -0.00000 0.00000  0.00000  130 PHE   A CB  
6608  C CG  . PHE   E  130 ? 0.35199 0.35199 0.35199 0.00000  0.00000  0.00000  130 PHE   A CG  
6609  C CD1 . PHE   E  130 ? 0.35194 0.35194 0.35194 -0.00000 0.00000  0.00000  130 PHE   A CD1 
6610  C CD2 . PHE   E  130 ? 0.27090 0.27090 0.27090 0.00000  0.00000  0.00000  130 PHE   A CD2 
6611  C CE1 . PHE   E  130 ? 0.33716 0.33716 0.33716 0.00000  0.00000  0.00000  130 PHE   A CE1 
6612  C CE2 . PHE   E  130 ? 0.44599 0.44599 0.44599 0.00000  0.00000  0.00000  130 PHE   A CE2 
6613  C CZ  . PHE   E  130 ? 0.27436 0.27436 0.27436 0.00000  0.00000  0.00000  130 PHE   A CZ  
6614  N N   . SER   E  131 ? 0.27307 0.27307 0.27307 -0.00000 0.00000  0.00000  131 SER   A N   
6615  C CA  . SER   E  131 ? 0.49691 0.49691 0.49691 -0.00000 -0.00000 0.00000  131 SER   A CA  
6616  C C   . SER   E  131 ? 0.34061 0.34061 0.34061 0.00000  0.00000  0.00000  131 SER   A C   
6617  O O   . SER   E  131 ? 0.47798 0.47798 0.47798 -0.00000 0.00000  0.00000  131 SER   A O   
6618  C CB  . SER   E  131 ? 0.13247 0.13247 0.13247 -0.00000 0.00000  0.00000  131 SER   A CB  
6619  O OG  . SER   E  131 ? 1.04267 1.04267 1.04267 -0.00000 0.00000  0.00000  131 SER   A OG  
6620  N N   . ALA   E  132 ? 0.36300 0.36300 0.36300 0.00000  0.00000  0.00000  132 ALA   A N   
6621  C CA  . ALA   E  132 ? 0.29033 0.29033 0.29033 0.00000  0.00000  0.00000  132 ALA   A CA  
6622  C C   . ALA   E  132 ? 0.47132 0.47132 0.47132 0.00000  0.00000  0.00000  132 ALA   A C   
6623  O O   . ALA   E  132 ? 0.39234 0.39234 0.39234 -0.00000 0.00000  0.00000  132 ALA   A O   
6624  C CB  . ALA   E  132 ? 0.29948 0.29948 0.29948 0.00000  -0.00000 0.00000  132 ALA   A CB  
6625  N N   . PHE   E  133 ? 0.25235 0.25235 0.25235 0.00000  0.00000  0.00000  133 PHE   A N   
6626  C CA  . PHE   E  133 ? 0.38628 0.38628 0.38628 -0.00000 0.00000  0.00000  133 PHE   A CA  
6627  C C   . PHE   E  133 ? 0.47429 0.47429 0.47429 -0.00000 0.00000  0.00000  133 PHE   A C   
6628  O O   . PHE   E  133 ? 0.34146 0.34146 0.34146 -0.00000 0.00000  0.00000  133 PHE   A O   
6629  C CB  . PHE   E  133 ? 0.28773 0.28773 0.28773 0.00000  0.00000  0.00000  133 PHE   A CB  
6630  C CG  . PHE   E  133 ? 0.42641 0.42641 0.42641 0.00000  0.00000  0.00000  133 PHE   A CG  
6631  C CD1 . PHE   E  133 ? 0.37008 0.37008 0.37008 -0.00000 0.00000  0.00000  133 PHE   A CD1 
6632  C CD2 . PHE   E  133 ? 0.30311 0.30311 0.30311 0.00000  0.00000  0.00000  133 PHE   A CD2 
6633  C CE1 . PHE   E  133 ? 0.26704 0.26704 0.26704 0.00000  0.00000  0.00000  133 PHE   A CE1 
6634  C CE2 . PHE   E  133 ? 0.29581 0.29581 0.29581 0.00000  0.00000  0.00000  133 PHE   A CE2 
6635  C CZ  . PHE   E  133 ? 0.21719 0.21719 0.21719 0.00000  0.00000  0.00000  133 PHE   A CZ  
6636  N N   . THR   E  134 ? 0.28438 0.28438 0.28438 0.00000  -0.00000 0.00000  134 THR   A N   
6637  C CA  . THR   E  134 ? 0.34339 0.34339 0.34339 0.00000  0.00000  0.00000  134 THR   A CA  
6638  C C   . THR   E  134 ? 0.31586 0.31586 0.31586 0.00000  -0.00000 0.00000  134 THR   A C   
6639  O O   . THR   E  134 ? 0.41657 0.41657 0.41657 0.00000  0.00000  0.00000  134 THR   A O   
6640  C CB  . THR   E  134 ? 0.34360 0.34360 0.34360 -0.00000 0.00000  0.00000  134 THR   A CB  
6641  O OG1 . THR   E  134 ? 0.41564 0.41564 0.41564 0.00000  0.00000  0.00000  134 THR   A OG1 
6642  C CG2 . THR   E  134 ? 0.25488 0.25488 0.25488 0.00000  0.00000  0.00000  134 THR   A CG2 
6643  N N   . ARG   E  135 ? 0.42826 0.42826 0.42826 -0.00000 0.00000  0.00000  135 ARG   A N   
6644  C CA  . ARG   E  135 ? 0.43052 0.43052 0.43052 0.00000  0.00000  0.00000  135 ARG   A CA  
6645  C C   . ARG   E  135 ? 0.60308 0.60308 0.60308 -0.00000 0.00000  0.00000  135 ARG   A C   
6646  O O   . ARG   E  135 ? 0.43348 0.43348 0.43348 -0.00000 0.00000  0.00000  135 ARG   A O   
6647  C CB  . ARG   E  135 ? 0.31423 0.31423 0.31423 0.00000  0.00000  0.00000  135 ARG   A CB  
6648  C CG  . ARG   E  135 ? 0.36749 0.36749 0.36749 -0.00000 0.00000  0.00000  135 ARG   A CG  
6649  C CD  . ARG   E  135 ? 0.40214 0.40214 0.40214 -0.00000 0.00000  0.00000  135 ARG   A CD  
6650  N NE  . ARG   E  135 ? 0.64651 0.64651 0.64651 0.00000  0.00000  0.00000  135 ARG   A NE  
6651  C CZ  . ARG   E  135 ? 0.69484 0.69484 0.69484 -0.00000 -0.00000 0.00000  135 ARG   A CZ  
6652  N NH1 . ARG   E  135 ? 0.58307 0.58307 0.58307 -0.00000 0.00000  0.00000  135 ARG   A NH1 
6653  N NH2 . ARG   E  135 ? 0.55685 0.55685 0.55685 -0.00000 0.00000  0.00000  135 ARG   A NH2 
6654  N N   . GLN   E  136 ? 0.33711 0.33711 0.33711 -0.00000 0.00000  0.00000  136 GLN   A N   
6655  C CA  . GLN   E  136 ? 0.36267 0.36267 0.36267 0.00000  0.00000  0.00000  136 GLN   A CA  
6656  C C   . GLN   E  136 ? 0.32929 0.32929 0.32929 0.00000  0.00000  0.00000  136 GLN   A C   
6657  O O   . GLN   E  136 ? 0.55085 0.55085 0.55085 0.00000  0.00000  0.00000  136 GLN   A O   
6658  C CB  . GLN   E  136 ? 0.33800 0.33800 0.33800 0.00000  0.00000  0.00000  136 GLN   A CB  
6659  C CG  . GLN   E  136 ? 0.27763 0.27763 0.27763 -0.00000 0.00000  0.00000  136 GLN   A CG  
6660  C CD  . GLN   E  136 ? 0.59753 0.59753 0.59753 0.00000  0.00000  0.00000  136 GLN   A CD  
6661  O OE1 . GLN   E  136 ? 0.44453 0.44453 0.44453 0.00000  0.00000  0.00000  136 GLN   A OE1 
6662  N NE2 . GLN   E  136 ? 0.28399 0.28399 0.28399 -0.00000 0.00000  0.00000  136 GLN   A NE2 
6663  N N   . ARG   E  137 ? 0.33378 0.33378 0.33378 0.00000  0.00000  0.00000  137 ARG   A N   
6664  C CA  . ARG   E  137 ? 0.20934 0.20934 0.20934 0.00000  0.00000  0.00000  137 ARG   A CA  
6665  C C   . ARG   E  137 ? 0.71665 0.71665 0.71665 0.00000  -0.00000 0.00000  137 ARG   A C   
6666  O O   . ARG   E  137 ? 0.35165 0.35165 0.35165 0.00000  0.00000  0.00000  137 ARG   A O   
6667  C CB  . ARG   E  137 ? 0.48403 0.48403 0.48403 0.00000  0.00000  0.00000  137 ARG   A CB  
6668  C CG  . ARG   E  137 ? 0.09530 0.09530 0.09530 0.00000  0.00000  0.00000  137 ARG   A CG  
6669  C CD  . ARG   E  137 ? 0.63822 0.63822 0.63822 0.00000  0.00000  0.00000  137 ARG   A CD  
6670  N NE  . ARG   E  137 ? 0.74614 0.74614 0.74614 0.00000  0.00000  0.00000  137 ARG   A NE  
6671  C CZ  . ARG   E  137 ? 0.41420 0.41420 0.41420 0.00000  0.00000  -0.00000 137 ARG   A CZ  
6672  N NH1 . ARG   E  137 ? 0.33260 0.33260 0.33260 0.00000  0.00000  -0.00000 137 ARG   A NH1 
6673  N NH2 . ARG   E  137 ? 0.57500 0.57500 0.57500 0.00000  0.00000  0.00000  137 ARG   A NH2 
6674  N N   . LEU   E  138 ? 0.21292 0.21292 0.21292 0.00000  0.00000  0.00000  138 LEU   A N   
6675  C CA  . LEU   E  138 ? 0.37829 0.37829 0.37829 -0.00000 0.00000  0.00000  138 LEU   A CA  
6676  C C   . LEU   E  138 ? 0.49784 0.49784 0.49784 0.00000  0.00000  0.00000  138 LEU   A C   
6677  O O   . LEU   E  138 ? 0.36548 0.36548 0.36548 -0.00000 0.00000  0.00000  138 LEU   A O   
6678  C CB  . LEU   E  138 ? 0.29956 0.29956 0.29956 0.00000  0.00000  0.00000  138 LEU   A CB  
6679  C CG  . LEU   E  138 ? 0.47535 0.47535 0.47535 0.00000  0.00000  0.00000  138 LEU   A CG  
6680  C CD1 . LEU   E  138 ? 0.30410 0.30410 0.30410 0.00000  0.00000  0.00000  138 LEU   A CD1 
6681  C CD2 . LEU   E  138 ? 0.27032 0.27032 0.27032 0.00000  0.00000  -0.00000 138 LEU   A CD2 
6682  N N   . ASN   E  139 ? 0.31722 0.31722 0.31722 -0.00000 0.00000  0.00000  139 ASN   A N   
6683  C CA  . ASN   E  139 ? 0.52242 0.52242 0.52242 0.00000  0.00000  0.00000  139 ASN   A CA  
6684  C C   . ASN   E  139 ? 0.35280 0.35280 0.35280 -0.00000 0.00000  0.00000  139 ASN   A C   
6685  O O   . ASN   E  139 ? 0.52888 0.52888 0.52888 0.00000  0.00000  0.00000  139 ASN   A O   
6686  C CB  . ASN   E  139 ? 0.22227 0.22227 0.22227 -0.00000 0.00000  0.00000  139 ASN   A CB  
6687  C CG  . ASN   E  139 ? 0.43533 0.43533 0.43533 0.00000  0.00000  0.00000  139 ASN   A CG  
6688  O OD1 . ASN   E  139 ? 0.32868 0.32868 0.32868 0.00000  0.00000  -0.00000 139 ASN   A OD1 
6689  N ND2 . ASN   E  139 ? 0.28841 0.28841 0.28841 0.00000  0.00000  0.00000  139 ASN   A ND2 
6690  N N   . LEU   E  140 ? 0.44276 0.44276 0.44276 -0.00000 0.00000  0.00000  140 LEU   A N   
6691  C CA  . LEU   E  140 ? 0.29270 0.29270 0.29270 0.00000  0.00000  0.00000  140 LEU   A CA  
6692  C C   . LEU   E  140 ? 0.57488 0.57488 0.57488 0.00000  0.00000  0.00000  140 LEU   A C   
6693  O O   . LEU   E  140 ? 0.30797 0.30797 0.30797 0.00000  0.00000  0.00000  140 LEU   A O   
6694  C CB  . LEU   E  140 ? 0.28686 0.28686 0.28686 0.00000  0.00000  0.00000  140 LEU   A CB  
6695  C CG  . LEU   E  140 ? 0.49255 0.49255 0.49255 0.00000  -0.00000 0.00000  140 LEU   A CG  
6696  C CD1 . LEU   E  140 ? 0.21351 0.21351 0.21351 0.00000  0.00000  0.00000  140 LEU   A CD1 
6697  C CD2 . LEU   E  140 ? 0.13569 0.13569 0.13569 0.00000  0.00000  0.00000  140 LEU   A CD2 
6698  N N   . HIS   E  141 ? 0.32363 0.32363 0.32363 -0.00000 0.00000  0.00000  141 HIS   A N   
6699  C CA  . HIS   E  141 ? 0.29702 0.29702 0.29702 -0.00000 0.00000  0.00000  141 HIS   A CA  
6700  C C   . HIS   E  141 ? 0.31192 0.31192 0.31192 0.00000  0.00000  0.00000  141 HIS   A C   
6701  O O   . HIS   E  141 ? 0.39662 0.39662 0.39662 0.00000  0.00000  0.00000  141 HIS   A O   
6702  C CB  . HIS   E  141 ? 0.17006 0.17006 0.17006 0.00000  0.00000  0.00000  141 HIS   A CB  
6703  C CG  . HIS   E  141 ? 0.51900 0.51900 0.51900 -0.00000 0.00000  0.00000  141 HIS   A CG  
6704  N ND1 . HIS   E  141 ? 0.49161 0.49161 0.49161 -0.00000 -0.00000 0.00000  141 HIS   A ND1 
6705  C CD2 . HIS   E  141 ? 0.43235 0.43235 0.43235 0.00000  0.00000  0.00000  141 HIS   A CD2 
6706  C CE1 . HIS   E  141 ? 0.33357 0.33357 0.33357 0.00000  0.00000  0.00000  141 HIS   A CE1 
6707  N NE2 . HIS   E  141 ? 0.50137 0.50137 0.50137 0.00000  0.00000  0.00000  141 HIS   A NE2 
6708  N N   . PHE   E  142 ? 0.32159 0.32159 0.32159 0.00000  0.00000  0.00000  142 PHE   A N   
6709  C CA  . PHE   E  142 ? 0.48921 0.48921 0.48921 -0.00000 0.00000  0.00000  142 PHE   A CA  
6710  C C   . PHE   E  142 ? 0.32323 0.32323 0.32323 0.00000  0.00000  0.00000  142 PHE   A C   
6711  O O   . PHE   E  142 ? 0.34805 0.34805 0.34805 0.00000  0.00000  0.00000  142 PHE   A O   
6712  C CB  . PHE   E  142 ? 0.31147 0.31147 0.31147 0.00000  0.00000  0.00000  142 PHE   A CB  
6713  C CG  . PHE   E  142 ? 0.40246 0.40246 0.40246 0.00000  -0.00000 0.00000  142 PHE   A CG  
6714  C CD1 . PHE   E  142 ? 0.33701 0.33701 0.33701 -0.00000 0.00000  0.00000  142 PHE   A CD1 
6715  C CD2 . PHE   E  142 ? 0.35589 0.35589 0.35589 0.00000  0.00000  0.00000  142 PHE   A CD2 
6716  C CE1 . PHE   E  142 ? 0.32534 0.32534 0.32534 -0.00000 0.00000  0.00000  142 PHE   A CE1 
6717  C CE2 . PHE   E  142 ? 0.36989 0.36989 0.36989 -0.00000 0.00000  0.00000  142 PHE   A CE2 
6718  C CZ  . PHE   E  142 ? 0.30931 0.30931 0.30931 -0.00000 0.00000  0.00000  142 PHE   A CZ  
6719  N N   . LYS   E  143 ? 0.44617 0.44617 0.44617 0.00000  0.00000  0.00000  143 LYS   A N   
6720  C CA  . LYS   E  143 ? 0.39129 0.39129 0.39129 0.00000  0.00000  0.00000  143 LYS   A CA  
6721  C C   . LYS   E  143 ? 0.43278 0.43278 0.43278 0.00000  0.00000  0.00000  143 LYS   A C   
6722  O O   . LYS   E  143 ? 0.47535 0.47535 0.47535 -0.00000 0.00000  0.00000  143 LYS   A O   
6723  C CB  . LYS   E  143 ? 0.43629 0.43629 0.43629 -0.00000 0.00000  0.00000  143 LYS   A CB  
6724  C CG  . LYS   E  143 ? 0.26613 0.26613 0.26613 0.00000  0.00000  0.00000  143 LYS   A CG  
6725  C CD  . LYS   E  143 ? 0.36950 0.36950 0.36950 0.00000  0.00000  0.00000  143 LYS   A CD  
6726  C CE  . LYS   E  143 ? 0.45256 0.45256 0.45256 0.00000  0.00000  0.00000  143 LYS   A CE  
6727  N NZ  . LYS   E  143 ? 0.51094 0.51094 0.51094 -0.00000 0.00000  0.00000  143 LYS   A NZ  
6728  N N   . LYS   E  144 ? 0.42491 0.42491 0.42491 0.00000  0.00000  0.00000  144 LYS   A N   
6729  C CA  . LYS   E  144 ? 0.72549 0.72549 0.72549 0.00000  0.00000  0.00000  144 LYS   A CA  
6730  C C   . LYS   E  144 ? 0.46073 0.46073 0.46073 0.00000  0.00000  0.00000  144 LYS   A C   
6731  O O   . LYS   E  144 ? 0.44175 0.44175 0.44175 0.00000  0.00000  0.00000  144 LYS   A O   
6732  C CB  . LYS   E  144 ? 0.33083 0.33083 0.33083 0.00000  0.00000  0.00000  144 LYS   A CB  
6733  C CG  . LYS   E  144 ? 0.20584 0.20584 0.20584 -0.00000 0.00000  0.00000  144 LYS   A CG  
6734  C CD  . LYS   E  144 ? 1.31357 1.31357 1.31357 0.00000  0.00000  0.00000  144 LYS   A CD  
6735  C CE  . LYS   E  144 ? 1.61970 1.61970 1.61970 -0.00000 0.00000  0.00000  144 LYS   A CE  
6736  N NZ  . LYS   E  144 ? 0.33250 0.33250 0.33250 0.00000  0.00000  0.00000  144 LYS   A NZ  
6737  N N   . LEU   E  145 ? 0.30167 0.30167 0.30167 0.00000  0.00000  0.00000  145 LEU   A N   
6738  C CA  . LEU   E  145 ? 0.23110 0.23110 0.23110 0.00000  0.00000  0.00000  145 LEU   A CA  
6739  C C   . LEU   E  145 ? 0.48644 0.48644 0.48644 0.00000  0.00000  0.00000  145 LEU   A C   
6740  O O   . LEU   E  145 ? 0.46399 0.46399 0.46399 -0.00000 0.00000  0.00000  145 LEU   A O   
6741  C CB  . LEU   E  145 ? 0.36834 0.36834 0.36834 0.00000  0.00000  0.00000  145 LEU   A CB  
6742  C CG  . LEU   E  145 ? 0.40192 0.40192 0.40192 0.00000  0.00000  0.00000  145 LEU   A CG  
6743  C CD1 . LEU   E  145 ? 0.32214 0.32214 0.32214 0.00000  0.00000  0.00000  145 LEU   A CD1 
6744  C CD2 . LEU   E  145 ? 0.31429 0.31429 0.31429 0.00000  0.00000  0.00000  145 LEU   A CD2 
6745  N N   . PHE   E  146 ? 0.29283 0.29283 0.29283 0.00000  0.00000  0.00000  146 PHE   A N   
6746  C CA  . PHE   E  146 ? 0.34291 0.34291 0.34291 -0.00000 0.00000  0.00000  146 PHE   A CA  
6747  C C   . PHE   E  146 ? 0.44727 0.44727 0.44727 0.00000  0.00000  0.00000  146 PHE   A C   
6748  O O   . PHE   E  146 ? 0.45625 0.45625 0.45625 -0.00000 -0.00000 0.00000  146 PHE   A O   
6749  C CB  . PHE   E  146 ? 0.34581 0.34581 0.34581 0.00000  0.00000  0.00000  146 PHE   A CB  
6750  C CG  . PHE   E  146 ? 0.39107 0.39107 0.39107 0.00000  0.00000  0.00000  146 PHE   A CG  
6751  C CD1 . PHE   E  146 ? 0.39162 0.39162 0.39162 -0.00000 0.00000  0.00000  146 PHE   A CD1 
6752  C CD2 . PHE   E  146 ? 0.30379 0.30379 0.30379 -0.00000 0.00000  0.00000  146 PHE   A CD2 
6753  C CE1 . PHE   E  146 ? 0.39308 0.39308 0.39308 0.00000  0.00000  0.00000  146 PHE   A CE1 
6754  C CE2 . PHE   E  146 ? 0.34917 0.34917 0.34917 -0.00000 0.00000  0.00000  146 PHE   A CE2 
6755  C CZ  . PHE   E  146 ? 0.42083 0.42083 0.42083 -0.00000 -0.00000 0.00000  146 PHE   A CZ  
6756  N N   . ASP   E  147 ? 0.36954 0.36954 0.36954 0.00000  0.00000  -0.00000 147 ASP   A N   
6757  C CA  . ASP   E  147 ? 0.28884 0.28884 0.28884 -0.00000 0.00000  0.00000  147 ASP   A CA  
6758  C C   . ASP   E  147 ? 0.40998 0.40998 0.40998 0.00000  0.00000  0.00000  147 ASP   A C   
6759  O O   . ASP   E  147 ? 0.38862 0.38862 0.38862 0.00000  0.00000  0.00000  147 ASP   A O   
6760  C CB  . ASP   E  147 ? 0.19317 0.19317 0.19317 -0.00000 -0.00000 0.00000  147 ASP   A CB  
6761  C CG  . ASP   E  147 ? 0.61211 0.61211 0.61211 0.00000  0.00000  0.00000  147 ASP   A CG  
6762  O OD1 . ASP   E  147 ? 0.51226 0.51226 0.51226 0.00000  0.00000  -0.00000 147 ASP   A OD1 
6763  O OD2 . ASP   E  147 ? 0.56521 0.56521 0.56521 0.00000  0.00000  0.00000  147 ASP   A OD2 
6764  N N   . THR   E  148 ? 0.38323 0.38323 0.38323 0.00000  0.00000  -0.00000 148 THR   A N   
6765  C CA  . THR   E  148 ? 0.50290 0.50290 0.50290 0.00000  -0.00000 -0.00000 148 THR   A CA  
6766  C C   . THR   E  148 ? 0.46371 0.46371 0.46371 -0.00000 0.00000  0.00000  148 THR   A C   
6767  O O   . THR   E  148 ? 0.53990 0.53990 0.53990 -0.00000 0.00000  0.00000  148 THR   A O   
6768  C CB  . THR   E  148 ? 0.43782 0.43782 0.43782 0.00000  0.00000  0.00000  148 THR   A CB  
6769  O OG1 . THR   E  148 ? 0.44880 0.44880 0.44880 0.00000  0.00000  0.00000  148 THR   A OG1 
6770  C CG2 . THR   E  148 ? 0.30234 0.30234 0.30234 0.00000  0.00000  0.00000  148 THR   A CG2 
6771  N N   . TRP   E  149 ? 0.36025 0.36025 0.36025 -0.00000 0.00000  0.00000  149 TRP   A N   
6772  C CA  . TRP   E  149 ? 0.27293 0.27293 0.27293 0.00000  0.00000  0.00000  149 TRP   A CA  
6773  C C   . TRP   E  149 ? 0.57723 0.57723 0.57723 0.00000  0.00000  0.00000  149 TRP   A C   
6774  O O   . TRP   E  149 ? 0.38496 0.38496 0.38496 0.00000  0.00000  0.00000  149 TRP   A O   
6775  C CB  . TRP   E  149 ? 0.24217 0.24217 0.24217 0.00000  0.00000  0.00000  149 TRP   A CB  
6776  C CG  . TRP   E  149 ? 0.38180 0.38180 0.38180 -0.00000 0.00000  0.00000  149 TRP   A CG  
6777  C CD1 . TRP   E  149 ? 0.30989 0.30989 0.30989 -0.00000 0.00000  0.00000  149 TRP   A CD1 
6778  C CD2 . TRP   E  149 ? 0.51274 0.51274 0.51274 0.00000  0.00000  0.00000  149 TRP   A CD2 
6779  N NE1 . TRP   E  149 ? 0.46455 0.46455 0.46455 -0.00000 0.00000  0.00000  149 TRP   A NE1 
6780  C CE2 . TRP   E  149 ? 0.29077 0.29077 0.29077 0.00000  0.00000  0.00000  149 TRP   A CE2 
6781  C CE3 . TRP   E  149 ? 0.27959 0.27959 0.27959 -0.00000 0.00000  0.00000  149 TRP   A CE3 
6782  C CZ2 . TRP   E  149 ? 0.41040 0.41040 0.41040 -0.00000 0.00000  0.00000  149 TRP   A CZ2 
6783  C CZ3 . TRP   E  149 ? 0.31584 0.31584 0.31584 0.00000  0.00000  0.00000  149 TRP   A CZ3 
6784  C CH2 . TRP   E  149 ? 0.40725 0.40725 0.40725 0.00000  0.00000  0.00000  149 TRP   A CH2 
6785  N N   . GLY   E  150 ? 0.36793 0.36793 0.36793 -0.00000 0.00000  0.00000  150 GLY   A N   
6786  C CA  . GLY   E  150 ? 0.23313 0.23313 0.23313 0.00000  0.00000  0.00000  150 GLY   A CA  
6787  C C   . GLY   E  150 ? 0.50281 0.50281 0.50281 -0.00000 0.00000  0.00000  150 GLY   A C   
6788  O O   . GLY   E  150 ? 0.65547 0.65547 0.65547 0.00000  0.00000  0.00000  150 GLY   A O   
6789  N N   . LEU   E  151 ? 0.44906 0.44906 0.44906 0.00000  0.00000  0.00000  151 LEU   A N   
6790  C CA  . LEU   E  151 ? 0.38216 0.38216 0.38216 0.00000  0.00000  0.00000  151 LEU   A CA  
6791  C C   . LEU   E  151 ? 0.88169 0.88169 0.88169 -0.00000 0.00000  0.00000  151 LEU   A C   
6792  O O   . LEU   E  151 ? 0.54046 0.54046 0.54046 -0.00000 0.00000  0.00000  151 LEU   A O   
6793  C CB  . LEU   E  151 ? 0.53662 0.53662 0.53662 -0.00000 0.00000  0.00000  151 LEU   A CB  
6794  C CG  . LEU   E  151 ? 0.80381 0.80381 0.80381 0.00000  0.00000  0.00000  151 LEU   A CG  
6795  C CD1 . LEU   E  151 ? 0.36273 0.36273 0.36273 0.00000  0.00000  0.00000  151 LEU   A CD1 
6796  C CD2 . LEU   E  151 ? 0.21737 0.21737 0.21737 0.00000  0.00000  0.00000  151 LEU   A CD2 
6797  N N   . PHE   E  152 ? 0.31883 0.31883 0.31883 0.00000  0.00000  0.00000  152 PHE   A N   
6798  C CA  . PHE   E  152 ? 0.48032 0.48032 0.48032 -0.00000 0.00000  0.00000  152 PHE   A CA  
6799  C C   . PHE   E  152 ? 0.64792 0.64792 0.64792 0.00000  0.00000  0.00000  152 PHE   A C   
6800  O O   . PHE   E  152 ? 0.55236 0.55236 0.55236 0.00000  0.00000  0.00000  152 PHE   A O   
6801  C CB  . PHE   E  152 ? 0.25568 0.25568 0.25568 0.00000  0.00000  0.00000  152 PHE   A CB  
6802  C CG  . PHE   E  152 ? 0.58824 0.58824 0.58824 -0.00000 0.00000  0.00000  152 PHE   A CG  
6803  C CD1 . PHE   E  152 ? 0.37231 0.37231 0.37231 0.00000  0.00000  0.00000  152 PHE   A CD1 
6804  C CD2 . PHE   E  152 ? 0.47194 0.47194 0.47194 -0.00000 0.00000  0.00000  152 PHE   A CD2 
6805  C CE1 . PHE   E  152 ? 0.46089 0.46089 0.46089 0.00000  0.00000  0.00000  152 PHE   A CE1 
6806  C CE2 . PHE   E  152 ? 0.59326 0.59326 0.59326 0.00000  0.00000  0.00000  152 PHE   A CE2 
6807  C CZ  . PHE   E  152 ? 0.48876 0.48876 0.48876 0.00000  0.00000  0.00000  152 PHE   A CZ  
6808  N N   . LEU   E  153 ? 0.41890 0.41890 0.41890 0.00000  0.00000  0.00000  153 LEU   A N   
6809  C CA  . LEU   E  153 ? 0.44305 0.44305 0.44305 0.00000  0.00000  0.00000  153 LEU   A CA  
6810  C C   . LEU   E  153 ? 0.43780 0.43780 0.43780 -0.00000 0.00000  0.00000  153 LEU   A C   
6811  O O   . LEU   E  153 ? 0.49346 0.49346 0.49346 0.00000  0.00000  0.00000  153 LEU   A O   
6812  C CB  . LEU   E  153 ? 0.35085 0.35085 0.35085 0.00000  -0.00000 0.00000  153 LEU   A CB  
6813  C CG  . LEU   E  153 ? 0.51636 0.51636 0.51636 0.00000  0.00000  0.00000  153 LEU   A CG  
6814  C CD1 . LEU   E  153 ? 0.29064 0.29064 0.29064 0.00000  0.00000  0.00000  153 LEU   A CD1 
6815  C CD2 . LEU   E  153 ? 0.29085 0.29085 0.29085 -0.00000 0.00000  0.00000  153 LEU   A CD2 
6816  N N   . SER   E  154 ? 0.46276 0.46276 0.46276 0.00000  0.00000  -0.00000 154 SER   A N   
6817  C CA  . SER   E  154 ? 0.43428 0.43428 0.43428 0.00000  0.00000  0.00000  154 SER   A CA  
6818  C C   . SER   E  154 ? 0.56197 0.56197 0.56197 -0.00000 0.00000  0.00000  154 SER   A C   
6819  O O   . SER   E  154 ? 0.61569 0.61569 0.61569 0.00000  0.00000  0.00000  154 SER   A O   
6820  C CB  . SER   E  154 ? 0.27212 0.27212 0.27212 -0.00000 0.00000  0.00000  154 SER   A CB  
6821  O OG  . SER   E  154 ? 1.29337 1.29337 1.29337 -0.00000 0.00000  0.00000  154 SER   A OG  
6822  N N   . SER   E  155 ? 0.44389 0.44389 0.44389 0.00000  0.00000  0.00000  155 SER   A N   
6823  C CA  . SER   E  155 ? 0.45179 0.45179 0.45179 0.00000  0.00000  0.00000  155 SER   A CA  
6824  C C   . SER   E  155 ? 1.27002 1.27002 1.27002 0.00000  0.00000  0.00000  155 SER   A C   
6825  O O   . SER   E  155 ? 0.42760 0.42760 0.42760 0.00000  0.00000  -0.00000 155 SER   A O   
6826  C CB  . SER   E  155 ? 0.41066 0.41066 0.41066 -0.00000 0.00000  0.00000  155 SER   A CB  
6827  O OG  . SER   E  155 ? 0.53794 0.53794 0.53794 0.00000  0.00000  0.00000  155 SER   A OG  
6828  N N   . LYS   E  156 ? 0.53304 0.53304 0.53304 0.00000  0.00000  0.00000  156 LYS   A N   
6829  C CA  . LYS   E  156 ? 0.74604 0.74604 0.74604 -0.00000 0.00000  0.00000  156 LYS   A CA  
6830  C C   . LYS   E  156 ? 0.40941 0.40941 0.40941 0.00000  0.00000  0.00000  156 LYS   A C   
6831  O O   . LYS   E  156 ? 0.61008 0.61008 0.61008 0.00000  0.00000  0.00000  156 LYS   A O   
6832  C CB  . LYS   E  156 ? 0.31715 0.31715 0.31715 -0.00000 -0.00000 0.00000  156 LYS   A CB  
6833  N N   . ASP   E  157 ? 0.58933 0.58933 0.58933 0.00000  0.00000  0.00000  157 ASP   A N   
6834  C CA  . ASP   E  157 ? 0.57631 0.57631 0.57631 -0.00000 0.00000  0.00000  157 ASP   A CA  
6835  C C   . ASP   E  157 ? 0.60822 0.60822 0.60822 0.00000  0.00000  0.00000  157 ASP   A C   
6836  O O   . ASP   E  157 ? 0.55611 0.55611 0.55611 -0.00000 0.00000  0.00000  157 ASP   A O   
6837  C CB  . ASP   E  157 ? 0.72008 0.72008 0.72008 -0.00000 0.00000  0.00000  157 ASP   A CB  
6838  C CG  . ASP   E  157 ? 0.73323 0.73323 0.73323 0.00000  0.00000  0.00000  157 ASP   A CG  
6839  O OD1 . ASP   E  157 ? 0.86749 0.86749 0.86749 0.00000  0.00000  0.00000  157 ASP   A OD1 
6840  O OD2 . ASP   E  157 ? 1.10437 1.10437 1.10437 0.00000  0.00000  0.00000  157 ASP   A OD2 
6841  N N   . SER   E  158 ? 0.71995 0.71995 0.71995 0.00000  0.00000  0.00000  158 SER   A N   
6842  C CA  . SER   E  158 ? 0.53541 0.53541 0.53541 -0.00000 0.00000  0.00000  158 SER   A CA  
6843  C C   . SER   E  158 ? 0.57144 0.57144 0.57144 0.00000  0.00000  0.00000  158 SER   A C   
6844  O O   . SER   E  158 ? 0.50886 0.50886 0.50886 -0.00000 0.00000  0.00000  158 SER   A O   
6845  C CB  . SER   E  158 ? 0.45254 0.45254 0.45254 0.00000  0.00000  0.00000  158 SER   A CB  
6846  O OG  . SER   E  158 ? 0.44569 0.44569 0.44569 0.00000  0.00000  0.00000  158 SER   A OG  
6847  N N   . ARG   E  159 ? 0.41422 0.41422 0.41422 0.00000  0.00000  0.00000  159 ARG   A N   
6848  C CA  . ARG   E  159 ? 0.50561 0.50561 0.50561 0.00000  -0.00000 0.00000  159 ARG   A CA  
6849  C C   . ARG   E  159 ? 0.51520 0.51520 0.51520 0.00000  0.00000  0.00000  159 ARG   A C   
6850  O O   . ARG   E  159 ? 0.44450 0.44450 0.44450 -0.00000 0.00000  0.00000  159 ARG   A O   
6851  C CB  . ARG   E  159 ? 0.28565 0.28565 0.28565 0.00000  0.00000  0.00000  159 ARG   A CB  
6852  C CG  . ARG   E  159 ? 0.74122 0.74122 0.74122 -0.00000 0.00000  0.00000  159 ARG   A CG  
6853  C CD  . ARG   E  159 ? 0.53963 0.53963 0.53963 -0.00000 0.00000  0.00000  159 ARG   A CD  
6854  N NE  . ARG   E  159 ? 0.71520 0.71520 0.71520 0.00000  0.00000  0.00000  159 ARG   A NE  
6855  C CZ  . ARG   E  159 ? 0.60333 0.60333 0.60333 -0.00000 0.00000  0.00000  159 ARG   A CZ  
6856  N NH1 . ARG   E  159 ? 0.50799 0.50799 0.50799 0.00000  0.00000  0.00000  159 ARG   A NH1 
6857  N NH2 . ARG   E  159 ? 0.47279 0.47279 0.47279 0.00000  0.00000  0.00000  159 ARG   A NH2 
6858  N N   . ASN   E  160 ? 0.41945 0.41945 0.41945 -0.00000 0.00000  0.00000  160 ASN   A N   
6859  C CA  . ASN   E  160 ? 0.47449 0.47449 0.47449 0.00000  0.00000  0.00000  160 ASN   A CA  
6860  C C   . ASN   E  160 ? 0.37858 0.37858 0.37858 0.00000  0.00000  0.00000  160 ASN   A C   
6861  O O   . ASN   E  160 ? 0.75565 0.75565 0.75565 0.00000  0.00000  0.00000  160 ASN   A O   
6862  C CB  . ASN   E  160 ? 0.44979 0.44979 0.44979 0.00000  0.00000  0.00000  160 ASN   A CB  
6863  C CG  . ASN   E  160 ? 0.60398 0.60398 0.60398 -0.00000 0.00000  0.00000  160 ASN   A CG  
6864  O OD1 . ASN   E  160 ? 0.77440 0.77440 0.77440 -0.00000 0.00000  -0.00000 160 ASN   A OD1 
6865  N ND2 . ASN   E  160 ? 0.65709 0.65709 0.65709 0.00000  0.00000  0.00000  160 ASN   A ND2 
6866  N N   . VAL   E  161 ? 0.53547 0.53547 0.53547 0.00000  0.00000  0.00000  161 VAL   A N   
6867  C CA  . VAL   E  161 ? 0.57100 0.57100 0.57100 0.00000  -0.00000 0.00000  161 VAL   A CA  
6868  C C   . VAL   E  161 ? 0.60519 0.60519 0.60519 0.00000  0.00000  0.00000  161 VAL   A C   
6869  O O   . VAL   E  161 ? 0.38614 0.38614 0.38614 0.00000  0.00000  0.00000  161 VAL   A O   
6870  C CB  . VAL   E  161 ? 0.49433 0.49433 0.49433 0.00000  0.00000  0.00000  161 VAL   A CB  
6871  C CG1 . VAL   E  161 ? 0.35331 0.35331 0.35331 0.00000  0.00000  0.00000  161 VAL   A CG1 
6872  C CG2 . VAL   E  161 ? 0.28861 0.28861 0.28861 0.00000  0.00000  0.00000  161 VAL   A CG2 
6873  N N   . LEU   E  162 ? 0.36218 0.36218 0.36218 0.00000  0.00000  0.00000  162 LEU   A N   
6874  C CA  . LEU   E  162 ? 0.49447 0.49447 0.49447 0.00000  0.00000  0.00000  162 LEU   A CA  
6875  C C   . LEU   E  162 ? 0.73423 0.73423 0.73423 -0.00000 0.00000  0.00000  162 LEU   A C   
6876  O O   . LEU   E  162 ? 0.51381 0.51381 0.51381 0.00000  -0.00000 0.00000  162 LEU   A O   
6877  C CB  . LEU   E  162 ? 0.45213 0.45213 0.45213 -0.00000 0.00000  0.00000  162 LEU   A CB  
6878  C CG  . LEU   E  162 ? 0.30825 0.30825 0.30825 -0.00000 0.00000  0.00000  162 LEU   A CG  
6879  C CD1 . LEU   E  162 ? 0.25371 0.25371 0.25371 0.00000  0.00000  0.00000  162 LEU   A CD1 
6880  C CD2 . LEU   E  162 ? 0.23906 0.23906 0.23906 0.00000  -0.00000 0.00000  162 LEU   A CD2 
6881  N N   . VAL   E  163 ? 0.41057 0.41057 0.41057 -0.00000 0.00000  0.00000  163 VAL   A N   
6882  C CA  . VAL   E  163 ? 0.37315 0.37315 0.37315 0.00000  0.00000  0.00000  163 VAL   A CA  
6883  C C   . VAL   E  163 ? 0.63184 0.63184 0.63184 -0.00000 -0.00000 0.00000  163 VAL   A C   
6884  O O   . VAL   E  163 ? 0.53790 0.53790 0.53790 -0.00000 0.00000  0.00000  163 VAL   A O   
6885  C CB  . VAL   E  163 ? 0.39798 0.39798 0.39798 0.00000  0.00000  0.00000  163 VAL   A CB  
6886  C CG1 . VAL   E  163 ? 0.31672 0.31672 0.31672 0.00000  0.00000  0.00000  163 VAL   A CG1 
6887  C CG2 . VAL   E  163 ? 0.31075 0.31075 0.31075 0.00000  0.00000  0.00000  163 VAL   A CG2 
6888  N N   . ALA   E  164 ? 0.62141 0.62141 0.62141 0.00000  -0.00000 0.00000  164 ALA   A N   
6889  C CA  . ALA   E  164 ? 0.71774 0.71774 0.71774 0.00000  0.00000  0.00000  164 ALA   A CA  
6890  C C   . ALA   E  164 ? 0.60376 0.60376 0.60376 0.00000  0.00000  0.00000  164 ALA   A C   
6891  O O   . ALA   E  164 ? 0.57735 0.57735 0.57735 0.00000  0.00000  0.00000  164 ALA   A O   
6892  C CB  . ALA   E  164 ? 0.34863 0.34863 0.34863 -0.00000 -0.00000 0.00000  164 ALA   A CB  
6893  N N   . ASP   E  165 ? 0.55675 0.55675 0.55675 0.00000  0.00000  0.00000  165 ASP   A N   
6894  C CA  . ASP   E  165 ? 0.53566 0.53566 0.53566 0.00000  0.00000  0.00000  165 ASP   A CA  
6895  C C   . ASP   E  165 ? 0.53389 0.53389 0.53389 0.00000  0.00000  0.00000  165 ASP   A C   
6896  O O   . ASP   E  165 ? 0.97745 0.97745 0.97745 0.00000  0.00000  0.00000  165 ASP   A O   
6897  C CB  . ASP   E  165 ? 0.62781 0.62781 0.62781 0.00000  0.00000  0.00000  165 ASP   A CB  
6898  C CG  . ASP   E  165 ? 0.47523 0.47523 0.47523 0.00000  0.00000  0.00000  165 ASP   A CG  
6899  O OD1 . ASP   E  165 ? 1.06101 1.06101 1.06101 -0.00000 0.00000  0.00000  165 ASP   A OD1 
6900  O OD2 . ASP   E  165 ? 1.09518 1.09518 1.09518 0.00000  0.00000  0.00000  165 ASP   A OD2 
6901  N N   . GLN   E  166 ? 0.81431 0.81431 0.81431 0.00000  0.00000  0.00000  166 GLN   A N   
6902  C CA  . GLN   E  166 ? 0.99756 0.99756 0.99756 -0.00000 0.00000  0.00000  166 GLN   A CA  
6903  C C   . GLN   E  166 ? 0.51956 0.51956 0.51956 0.00000  0.00000  0.00000  166 GLN   A C   
6904  O O   . GLN   E  166 ? 1.45174 1.45174 1.45174 0.00000  0.00000  0.00000  166 GLN   A O   
6905  C CB  . GLN   E  166 ? 0.48570 0.48570 0.48570 -0.00000 0.00000  0.00000  166 GLN   A CB  
6906  C CG  . GLN   E  166 ? 0.94818 0.94818 0.94818 -0.00000 0.00000  0.00000  166 GLN   A CG  
6907  C CD  . GLN   E  166 ? 1.70074 1.70074 1.70074 0.00000  0.00000  0.00000  166 GLN   A CD  
6908  O OE1 . GLN   E  166 ? 1.12783 1.12783 1.12783 -0.00000 0.00000  0.00000  166 GLN   A OE1 
6909  N NE2 . GLN   E  166 ? 0.95563 0.95563 0.95563 0.00000  0.00000  0.00000  166 GLN   A NE2 
6910  N N   . PHE   E  167 ? 0.94343 0.94343 0.94343 0.00000  0.00000  0.00000  167 PHE   A N   
6911  C CA  . PHE   E  167 ? 0.93023 0.93023 0.93023 0.00000  0.00000  0.00000  167 PHE   A CA  
6912  C C   . PHE   E  167 ? 0.94928 0.94928 0.94928 -0.00000 0.00000  0.00000  167 PHE   A C   
6913  O O   . PHE   E  167 ? 0.89836 0.89836 0.89836 0.00000  0.00000  0.00000  167 PHE   A O   
6914  C CB  . PHE   E  167 ? 0.80487 0.80487 0.80487 0.00000  0.00000  0.00000  167 PHE   A CB  
6915  C CG  . PHE   E  167 ? 0.87448 0.87448 0.87448 0.00000  0.00000  0.00000  167 PHE   A CG  
6916  C CD1 . PHE   E  167 ? 0.72521 0.72521 0.72521 0.00000  0.00000  0.00000  167 PHE   A CD1 
6917  C CD2 . PHE   E  167 ? 0.61259 0.61259 0.61259 -0.00000 0.00000  0.00000  167 PHE   A CD2 
6918  C CE1 . PHE   E  167 ? 1.62093 1.62093 1.62093 0.00000  0.00000  0.00000  167 PHE   A CE1 
6919  C CE2 . PHE   E  167 ? 1.47935 1.47935 1.47935 0.00000  0.00000  0.00000  167 PHE   A CE2 
6920  C CZ  . PHE   E  167 ? 0.45703 0.45703 0.45703 -0.00000 0.00000  0.00000  167 PHE   A CZ  
6921  N N   . ASP   E  168 ? 1.00816 1.00816 1.00816 0.00000  0.00000  0.00000  168 ASP   A N   
6922  C CA  . ASP   E  168 ? 0.56835 0.56835 0.56835 0.00000  0.00000  0.00000  168 ASP   A CA  
6923  C C   . ASP   E  168 ? 1.21820 1.21820 1.21820 -0.00000 0.00000  0.00000  168 ASP   A C   
6924  O O   . ASP   E  168 ? 0.88289 0.88289 0.88289 0.00000  0.00000  0.00000  168 ASP   A O   
6925  C CB  . ASP   E  168 ? 0.74667 0.74667 0.74667 0.00000  0.00000  0.00000  168 ASP   A CB  
6926  C CG  . ASP   E  168 ? 1.06060 1.06060 1.06060 -0.00000 0.00000  0.00000  168 ASP   A CG  
6927  O OD1 . ASP   E  168 ? 0.88115 0.88115 0.88115 0.00000  0.00000  0.00000  168 ASP   A OD1 
6928  O OD2 . ASP   E  168 ? 1.03218 1.03218 1.03218 -0.00000 0.00000  0.00000  168 ASP   A OD2 
6929  N N   . ASP   E  169 ? 0.87056 0.87056 0.87056 -0.00000 0.00000  0.00000  169 ASP   A N   
6930  C CA  . ASP   E  169 ? 0.91985 0.91985 0.91985 0.00000  0.00000  0.00000  169 ASP   A CA  
6931  C C   . ASP   E  169 ? 1.13323 1.13323 1.13323 -0.00000 0.00000  0.00000  169 ASP   A C   
6932  O O   . ASP   E  169 ? 0.97908 0.97908 0.97908 0.00000  0.00000  0.00000  169 ASP   A O   
6933  C CB  . ASP   E  169 ? 0.64860 0.64860 0.64860 0.00000  0.00000  0.00000  169 ASP   A CB  
6934  N N   . ARG   E  170 ? 1.76665 1.76665 1.76665 0.00000  0.00000  -0.00000 170 ARG   A N   
6935  C CA  . ARG   E  170 ? 0.63819 0.63819 0.63819 -0.00000 0.00000  0.00000  170 ARG   A CA  
6936  C C   . ARG   E  170 ? 0.86976 0.86976 0.86976 0.00000  0.00000  0.00000  170 ARG   A C   
6937  O O   . ARG   E  170 ? 0.75598 0.75598 0.75598 0.00000  0.00000  0.00000  170 ARG   A O   
6938  C CB  . ARG   E  170 ? 0.71232 0.71232 0.71232 0.00000  0.00000  0.00000  170 ARG   A CB  
6939  N N   . HIS   E  171 ? 0.79818 0.79818 0.79818 -0.00000 0.00000  0.00000  171 HIS   A N   
6940  C CA  . HIS   E  171 ? 0.83910 0.83910 0.83910 -0.00000 0.00000  0.00000  171 HIS   A CA  
6941  C C   . HIS   E  171 ? 0.41548 0.41548 0.41548 0.00000  0.00000  0.00000  171 HIS   A C   
6942  O O   . HIS   E  171 ? 1.31823 1.31823 1.31823 0.00000  0.00000  -0.00000 171 HIS   A O   
6943  C CB  . HIS   E  171 ? 0.87417 0.87417 0.87417 0.00000  0.00000  0.00000  171 HIS   A CB  
6944  C CG  . HIS   E  171 ? 0.81317 0.81317 0.81317 -0.00000 0.00000  0.00000  171 HIS   A CG  
6945  N ND1 . HIS   E  171 ? 0.88490 0.88490 0.88490 0.00000  0.00000  -0.00000 171 HIS   A ND1 
6946  C CD2 . HIS   E  171 ? 0.81605 0.81605 0.81605 0.00000  0.00000  -0.00000 171 HIS   A CD2 
6947  C CE1 . HIS   E  171 ? 0.56515 0.56515 0.56515 -0.00000 0.00000  0.00000  171 HIS   A CE1 
6948  N NE2 . HIS   E  171 ? 1.51837 1.51837 1.51837 0.00000  0.00000  0.00000  171 HIS   A NE2 
6949  N N   . CYS   E  172 ? 0.83512 0.83512 0.83512 -0.00000 0.00000  0.00000  172 CYS   A N   
6950  C CA  . CYS   E  172 ? 0.44663 0.44663 0.44663 0.00000  0.00000  0.00000  172 CYS   A CA  
6951  C C   . CYS   E  172 ? 0.46004 0.46004 0.46004 -0.00000 0.00000  0.00000  172 CYS   A C   
6952  O O   . CYS   E  172 ? 0.75045 0.75045 0.75045 0.00000  0.00000  0.00000  172 CYS   A O   
6953  C CB  . CYS   E  172 ? 0.56208 0.56208 0.56208 0.00000  0.00000  0.00000  172 CYS   A CB  
6954  S SG  . CYS   E  172 ? 0.66308 0.66308 0.66308 0.00000  0.00000  0.00000  172 CYS   A SG  
6955  N N   . GLY   E  173 ? 0.57550 0.57550 0.57550 0.00000  0.00000  0.00000  173 GLY   A N   
6956  C CA  . GLY   E  173 ? 0.38112 0.38112 0.38112 -0.00000 0.00000  0.00000  173 GLY   A CA  
6957  C C   . GLY   E  173 ? 0.56563 0.56563 0.56563 0.00000  0.00000  0.00000  173 GLY   A C   
6958  O O   . GLY   E  173 ? 0.56633 0.56633 0.56633 0.00000  0.00000  0.00000  173 GLY   A O   
6959  N N   . TRP   E  174 ? 0.33713 0.33713 0.33713 -0.00000 0.00000  0.00000  174 TRP   A N   
6960  C CA  . TRP   E  174 ? 0.66107 0.66107 0.66107 0.00000  0.00000  0.00000  174 TRP   A CA  
6961  C C   . TRP   E  174 ? 0.76978 0.76978 0.76978 0.00000  0.00000  0.00000  174 TRP   A C   
6962  O O   . TRP   E  174 ? 0.56943 0.56943 0.56943 0.00000  0.00000  0.00000  174 TRP   A O   
6963  C CB  . TRP   E  174 ? 0.37933 0.37933 0.37933 0.00000  0.00000  0.00000  174 TRP   A CB  
6964  C CG  . TRP   E  174 ? 0.75992 0.75992 0.75992 0.00000  0.00000  0.00000  174 TRP   A CG  
6965  C CD1 . TRP   E  174 ? 0.48067 0.48067 0.48067 0.00000  0.00000  0.00000  174 TRP   A CD1 
6966  C CD2 . TRP   E  174 ? 0.59101 0.59101 0.59101 -0.00000 0.00000  0.00000  174 TRP   A CD2 
6967  N NE1 . TRP   E  174 ? 0.51209 0.51209 0.51209 0.00000  0.00000  0.00000  174 TRP   A NE1 
6968  C CE2 . TRP   E  174 ? 0.41152 0.41152 0.41152 0.00000  0.00000  0.00000  174 TRP   A CE2 
6969  C CE3 . TRP   E  174 ? 0.43961 0.43961 0.43961 0.00000  0.00000  0.00000  174 TRP   A CE3 
6970  C CZ2 . TRP   E  174 ? 0.31541 0.31541 0.31541 0.00000  0.00000  0.00000  174 TRP   A CZ2 
6971  C CZ3 . TRP   E  174 ? 0.46538 0.46538 0.46538 0.00000  0.00000  0.00000  174 TRP   A CZ3 
6972  C CH2 . TRP   E  174 ? 0.35333 0.35333 0.35333 0.00000  0.00000  0.00000  174 TRP   A CH2 
6973  N N   . LEU   E  175 ? 0.53391 0.53391 0.53391 0.00000  0.00000  0.00000  175 LEU   A N   
6974  C CA  . LEU   E  175 ? 0.47000 0.47000 0.47000 -0.00000 0.00000  0.00000  175 LEU   A CA  
6975  C C   . LEU   E  175 ? 0.59281 0.59281 0.59281 0.00000  0.00000  0.00000  175 LEU   A C   
6976  O O   . LEU   E  175 ? 0.70489 0.70489 0.70489 0.00000  0.00000  0.00000  175 LEU   A O   
6977  C CB  . LEU   E  175 ? 0.40663 0.40663 0.40663 0.00000  0.00000  0.00000  175 LEU   A CB  
6978  C CG  . LEU   E  175 ? 0.54103 0.54103 0.54103 0.00000  0.00000  0.00000  175 LEU   A CG  
6979  C CD1 . LEU   E  175 ? 0.42129 0.42129 0.42129 0.00000  0.00000  0.00000  175 LEU   A CD1 
6980  C CD2 . LEU   E  175 ? 0.38260 0.38260 0.38260 -0.00000 0.00000  0.00000  175 LEU   A CD2 
6981  N N   . ASN   E  176 ? 0.50758 0.50758 0.50758 0.00000  0.00000  0.00000  176 ASN   A N   
6982  C CA  . ASN   E  176 ? 0.45173 0.45173 0.45173 -0.00000 0.00000  0.00000  176 ASN   A CA  
6983  C C   . ASN   E  176 ? 0.65955 0.65955 0.65955 -0.00000 0.00000  0.00000  176 ASN   A C   
6984  O O   . ASN   E  176 ? 0.83540 0.83540 0.83540 0.00000  0.00000  0.00000  176 ASN   A O   
6985  C CB  . ASN   E  176 ? 0.79271 0.79271 0.79271 0.00000  0.00000  0.00000  176 ASN   A CB  
6986  C CG  . ASN   E  176 ? 0.77132 0.77132 0.77132 0.00000  0.00000  0.00000  176 ASN   A CG  
6987  O OD1 . ASN   E  176 ? 0.59637 0.59637 0.59637 0.00000  0.00000  0.00000  176 ASN   A OD1 
6988  N ND2 . ASN   E  176 ? 0.61336 0.61336 0.61336 -0.00000 0.00000  0.00000  176 ASN   A ND2 
6989  N N   . GLU   E  177 ? 0.73745 0.73745 0.73745 0.00000  0.00000  0.00000  177 GLU   A N   
6990  C CA  . GLU   E  177 ? 0.70324 0.70324 0.70324 0.00000  0.00000  0.00000  177 GLU   A CA  
6991  C C   . GLU   E  177 ? 0.62434 0.62434 0.62434 0.00000  0.00000  0.00000  177 GLU   A C   
6992  O O   . GLU   E  177 ? 0.74146 0.74146 0.74146 0.00000  0.00000  0.00000  177 GLU   A O   
6993  C CB  . GLU   E  177 ? 0.47213 0.47213 0.47213 0.00000  0.00000  0.00000  177 GLU   A CB  
6994  N N   . ARG   E  178 ? 0.54740 0.54740 0.54740 0.00000  0.00000  0.00000  178 ARG   A N   
6995  C CA  . ARG   E  178 ? 0.84583 0.84583 0.84583 0.00000  0.00000  0.00000  178 ARG   A CA  
6996  C C   . ARG   E  178 ? 0.79740 0.79740 0.79740 -0.00000 0.00000  0.00000  178 ARG   A C   
6997  O O   . ARG   E  178 ? 0.77789 0.77789 0.77789 0.00000  0.00000  0.00000  178 ARG   A O   
6998  C CB  . ARG   E  178 ? 0.40488 0.40488 0.40488 -0.00000 0.00000  0.00000  178 ARG   A CB  
6999  C CG  . ARG   E  178 ? 0.88094 0.88094 0.88094 -0.00000 0.00000  0.00000  178 ARG   A CG  
7000  C CD  . ARG   E  178 ? 0.77890 0.77890 0.77890 -0.00000 0.00000  0.00000  178 ARG   A CD  
7001  N NE  . ARG   E  178 ? 1.04436 1.04436 1.04436 -0.00000 0.00000  0.00000  178 ARG   A NE  
7002  C CZ  . ARG   E  178 ? 1.67068 1.67068 1.67068 0.00000  0.00000  0.00000  178 ARG   A CZ  
7003  N NH1 . ARG   E  178 ? 1.75834 1.75834 1.75834 -0.00000 0.00000  0.00000  178 ARG   A NH1 
7004  N NH2 . ARG   E  178 ? 0.68740 0.68740 0.68740 0.00000  0.00000  0.00000  178 ARG   A NH2 
7005  N N   . ALA   E  179 ? 0.76841 0.76841 0.76841 0.00000  0.00000  0.00000  179 ALA   A N   
7006  C CA  . ALA   E  179 ? 0.75151 0.75151 0.75151 0.00000  0.00000  0.00000  179 ALA   A CA  
7007  C C   . ALA   E  179 ? 0.60985 0.60985 0.60985 -0.00000 0.00000  0.00000  179 ALA   A C   
7008  O O   . ALA   E  179 ? 0.70668 0.70668 0.70668 0.00000  0.00000  0.00000  179 ALA   A O   
7009  C CB  . ALA   E  179 ? 0.44551 0.44551 0.44551 0.00000  0.00000  0.00000  179 ALA   A CB  
7010  N N   . LEU   E  180 ? 0.64502 0.64502 0.64502 0.00000  0.00000  0.00000  180 LEU   A N   
7011  C CA  . LEU   E  180 ? 0.47980 0.47980 0.47980 0.00000  0.00000  0.00000  180 LEU   A CA  
7012  C C   . LEU   E  180 ? 0.68724 0.68724 0.68724 0.00000  0.00000  0.00000  180 LEU   A C   
7013  O O   . LEU   E  180 ? 0.68876 0.68876 0.68876 0.00000  0.00000  0.00000  180 LEU   A O   
7014  C CB  . LEU   E  180 ? 0.42072 0.42072 0.42072 -0.00000 0.00000  0.00000  180 LEU   A CB  
7015  C CG  . LEU   E  180 ? 0.73502 0.73502 0.73502 0.00000  0.00000  0.00000  180 LEU   A CG  
7016  C CD1 . LEU   E  180 ? 0.70502 0.70502 0.70502 -0.00000 0.00000  0.00000  180 LEU   A CD1 
7017  C CD2 . LEU   E  180 ? 0.57892 0.57892 0.57892 -0.00000 0.00000  0.00000  180 LEU   A CD2 
7018  N N   . SER   E  181 ? 0.62281 0.62281 0.62281 0.00000  0.00000  0.00000  181 SER   A N   
7019  C CA  . SER   E  181 ? 0.67235 0.67235 0.67235 -0.00000 0.00000  0.00000  181 SER   A CA  
7020  C C   . SER   E  181 ? 0.51655 0.51655 0.51655 0.00000  -0.00000 0.00000  181 SER   A C   
7021  O O   . SER   E  181 ? 0.65983 0.65983 0.65983 -0.00000 0.00000  0.00000  181 SER   A O   
7022  C CB  . SER   E  181 ? 0.44919 0.44919 0.44919 0.00000  -0.00000 -0.00000 181 SER   A CB  
7023  O OG  . SER   E  181 ? 1.31321 1.31321 1.31321 0.00000  0.00000  0.00000  181 SER   A OG  
7024  N N   . ALA   E  182 ? 0.57740 0.57740 0.57740 0.00000  0.00000  0.00000  182 ALA   A N   
7025  C CA  . ALA   E  182 ? 0.85184 0.85184 0.85184 -0.00000 0.00000  0.00000  182 ALA   A CA  
7026  C C   . ALA   E  182 ? 0.59232 0.59232 0.59232 0.00000  0.00000  0.00000  182 ALA   A C   
7027  O O   . ALA   E  182 ? 0.43814 0.43814 0.43814 -0.00000 0.00000  0.00000  182 ALA   A O   
7028  C CB  . ALA   E  182 ? 0.32655 0.32655 0.32655 0.00000  0.00000  0.00000  182 ALA   A CB  
7029  N N   . MET   E  183 ? 0.36730 0.36730 0.36730 0.00000  0.00000  0.00000  183 MET   A N   
7030  C CA  . MET   E  183 ? 0.57155 0.57155 0.57155 0.00000  0.00000  0.00000  183 MET   A CA  
7031  C C   . MET   E  183 ? 0.38588 0.38588 0.38588 0.00000  0.00000  0.00000  183 MET   A C   
7032  O O   . MET   E  183 ? 0.62139 0.62139 0.62139 0.00000  0.00000  0.00000  183 MET   A O   
7033  C CB  . MET   E  183 ? 0.37726 0.37726 0.37726 0.00000  0.00000  0.00000  183 MET   A CB  
7034  C CG  . MET   E  183 ? 0.40388 0.40388 0.40388 0.00000  0.00000  0.00000  183 MET   A CG  
7035  S SD  . MET   E  183 ? 0.52053 0.52053 0.52053 0.00000  0.00000  0.00000  183 MET   A SD  
7036  C CE  . MET   E  183 ? 0.47308 0.47308 0.47308 0.00000  0.00000  0.00000  183 MET   A CE  
7037  N N   . VAL   E  184 ? 0.44010 0.44010 0.44010 0.00000  0.00000  0.00000  184 VAL   A N   
7038  C CA  . VAL   E  184 ? 0.52696 0.52696 0.52696 -0.00000 0.00000  0.00000  184 VAL   A CA  
7039  C C   . VAL   E  184 ? 0.29321 0.29321 0.29321 0.00000  0.00000  0.00000  184 VAL   A C   
7040  O O   . VAL   E  184 ? 0.43156 0.43156 0.43156 0.00000  -0.00000 0.00000  184 VAL   A O   
7041  C CB  . VAL   E  184 ? 0.26622 0.26622 0.26622 0.00000  0.00000  0.00000  184 VAL   A CB  
7042  C CG1 . VAL   E  184 ? 0.33602 0.33602 0.33602 -0.00000 0.00000  0.00000  184 VAL   A CG1 
7043  C CG2 . VAL   E  184 ? 0.28028 0.28028 0.28028 0.00000  0.00000  0.00000  184 VAL   A CG2 
7044  N N   . LYS   E  185 ? 0.46017 0.46017 0.46017 0.00000  0.00000  0.00000  185 LYS   A N   
7045  C CA  . LYS   E  185 ? 0.49659 0.49659 0.49659 0.00000  0.00000  0.00000  185 LYS   A CA  
7046  C C   . LYS   E  185 ? 0.18910 0.18910 0.18910 -0.00000 0.00000  0.00000  185 LYS   A C   
7047  O O   . LYS   E  185 ? 0.92910 0.92910 0.92910 -0.00000 0.00000  0.00000  185 LYS   A O   
7048  C CB  . LYS   E  185 ? 0.35246 0.35246 0.35246 0.00000  0.00000  0.00000  185 LYS   A CB  
7049  C CG  . LYS   E  185 ? 0.43103 0.43103 0.43103 0.00000  0.00000  0.00000  185 LYS   A CG  
7050  C CD  . LYS   E  185 ? 0.75319 0.75319 0.75319 0.00000  0.00000  0.00000  185 LYS   A CD  
7051  C CE  . LYS   E  185 ? 0.76136 0.76136 0.76136 0.00000  0.00000  0.00000  185 LYS   A CE  
7052  N NZ  . LYS   E  185 ? 0.93519 0.93519 0.93519 0.00000  0.00000  0.00000  185 LYS   A NZ  
7053  N N   . HIS   E  186 ? 0.54018 0.54018 0.54018 -0.00000 0.00000  0.00000  186 HIS   A N   
7054  C CA  . HIS   E  186 ? 0.31334 0.31334 0.31334 0.00000  0.00000  -0.00000 186 HIS   A CA  
7055  C C   . HIS   E  186 ? 0.55700 0.55700 0.55700 0.00000  0.00000  0.00000  186 HIS   A C   
7056  O O   . HIS   E  186 ? 0.38163 0.38163 0.38163 0.00000  0.00000  0.00000  186 HIS   A O   
7057  C CB  . HIS   E  186 ? 0.42031 0.42031 0.42031 0.00000  0.00000  0.00000  186 HIS   A CB  
7058  C CG  . HIS   E  186 ? 0.75016 0.75016 0.75016 0.00000  0.00000  0.00000  186 HIS   A CG  
7059  N ND1 . HIS   E  186 ? 0.58523 0.58523 0.58523 0.00000  0.00000  -0.00000 186 HIS   A ND1 
7060  C CD2 . HIS   E  186 ? 0.23897 0.23897 0.23897 0.00000  0.00000  0.00000  186 HIS   A CD2 
7061  C CE1 . HIS   E  186 ? 0.43045 0.43045 0.43045 -0.00000 0.00000  0.00000  186 HIS   A CE1 
7062  N NE2 . HIS   E  186 ? 0.63380 0.63380 0.63380 0.00000  0.00000  0.00000  186 HIS   A NE2 
7063  N N   . TYR   E  187 ? 0.44565 0.44565 0.44565 0.00000  0.00000  0.00000  187 TYR   A N   
7064  C CA  . TYR   E  187 ? 0.54645 0.54645 0.54645 -0.00000 0.00000  0.00000  187 TYR   A CA  
7065  C C   . TYR   E  187 ? 1.00097 1.00097 1.00097 0.00000  0.00000  0.00000  187 TYR   A C   
7066  O O   . TYR   E  187 ? 0.46336 0.46336 0.46336 0.00000  0.00000  0.00000  187 TYR   A O   
7067  C CB  . TYR   E  187 ? 0.60358 0.60358 0.60358 -0.00000 0.00000  0.00000  187 TYR   A CB  
7068  C CG  . TYR   E  187 ? 0.40103 0.40103 0.40103 0.00000  -0.00000 0.00000  187 TYR   A CG  
7069  C CD1 . TYR   E  187 ? 0.50773 0.50773 0.50773 0.00000  0.00000  0.00000  187 TYR   A CD1 
7070  C CD2 . TYR   E  187 ? 0.58755 0.58755 0.58755 -0.00000 0.00000  0.00000  187 TYR   A CD2 
7071  C CE1 . TYR   E  187 ? 0.45597 0.45597 0.45597 0.00000  0.00000  0.00000  187 TYR   A CE1 
7072  C CE2 . TYR   E  187 ? 0.23491 0.23491 0.23491 0.00000  0.00000  0.00000  187 TYR   A CE2 
7073  C CZ  . TYR   E  187 ? 0.58168 0.58168 0.58168 -0.00000 -0.00000 0.00000  187 TYR   A CZ  
7074  O OH  . TYR   E  187 ? 0.49799 0.49799 0.49799 0.00000  0.00000  0.00000  187 TYR   A OH  
7075  N N   . ASN   E  188 ? 0.45700 0.45700 0.45700 -0.00000 0.00000  0.00000  188 ASN   A N   
7076  C CA  . ASN   E  188 ? 1.08657 1.08657 1.08657 -0.00000 0.00000  0.00000  188 ASN   A CA  
7077  C C   . ASN   E  188 ? 0.44394 0.44394 0.44394 0.00000  0.00000  0.00000  188 ASN   A C   
7078  O O   . ASN   E  188 ? 0.86801 0.86801 0.86801 0.00000  0.00000  0.00000  188 ASN   A O   
7079  C CB  . ASN   E  188 ? 0.58935 0.58935 0.58935 0.00000  0.00000  0.00000  188 ASN   A CB  
7080  C CG  . ASN   E  188 ? 1.08718 1.08718 1.08718 0.00000  0.00000  0.00000  188 ASN   A CG  
7081  O OD1 . ASN   E  188 ? 1.43990 1.43990 1.43990 -0.00000 0.00000  0.00000  188 ASN   A OD1 
7082  N ND2 . ASN   E  188 ? 1.24981 1.24981 1.24981 0.00000  0.00000  0.00000  188 ASN   A ND2 
7083  N N   . GLY   E  189 ? 0.79120 0.79120 0.79120 -0.00000 0.00000  0.00000  189 GLY   A N   
7084  C CA  . GLY   E  189 ? 0.37219 0.37219 0.37219 0.00000  0.00000  0.00000  189 GLY   A CA  
7085  C C   . GLY   E  189 ? 0.42495 0.42495 0.42495 -0.00000 0.00000  0.00000  189 GLY   A C   
7086  O O   . GLY   E  189 ? 0.84158 0.84158 0.84158 0.00000  0.00000  0.00000  189 GLY   A O   
7087  N N   . ARG   E  190 ? 0.56234 0.56234 0.56234 0.00000  0.00000  0.00000  190 ARG   A N   
7088  C CA  . ARG   E  190 ? 0.41240 0.41240 0.41240 0.00000  0.00000  0.00000  190 ARG   A CA  
7089  C C   . ARG   E  190 ? 0.50252 0.50252 0.50252 0.00000  0.00000  0.00000  190 ARG   A C   
7090  O O   . ARG   E  190 ? 0.63787 0.63787 0.63787 0.00000  0.00000  0.00000  190 ARG   A O   
7091  C CB  . ARG   E  190 ? 0.50372 0.50372 0.50372 0.00000  0.00000  0.00000  190 ARG   A CB  
7092  C CG  . ARG   E  190 ? 0.43604 0.43604 0.43604 0.00000  0.00000  0.00000  190 ARG   A CG  
7093  C CD  . ARG   E  190 ? 0.31579 0.31579 0.31579 0.00000  0.00000  0.00000  190 ARG   A CD  
7094  N NE  . ARG   E  190 ? 0.50142 0.50142 0.50142 0.00000  -0.00000 -0.00000 190 ARG   A NE  
7095  C CZ  . ARG   E  190 ? 0.71648 0.71648 0.71648 0.00000  0.00000  0.00000  190 ARG   A CZ  
7096  N NH1 . ARG   E  190 ? 0.66907 0.66907 0.66907 0.00000  0.00000  0.00000  190 ARG   A NH1 
7097  N NH2 . ARG   E  190 ? 0.53479 0.53479 0.53479 0.00000  0.00000  0.00000  190 ARG   A NH2 
7098  N N   . ALA   E  191 ? 0.48905 0.48905 0.48905 0.00000  0.00000  0.00000  191 ALA   A N   
7099  C CA  . ALA   E  191 ? 0.33448 0.33448 0.33448 0.00000  0.00000  0.00000  191 ALA   A CA  
7100  C C   . ALA   E  191 ? 1.13285 1.13285 1.13285 -0.00000 0.00000  0.00000  191 ALA   A C   
7101  O O   . ALA   E  191 ? 0.35037 0.35037 0.35037 0.00000  0.00000  0.00000  191 ALA   A O   
7102  C CB  . ALA   E  191 ? 0.49047 0.49047 0.49047 0.00000  0.00000  0.00000  191 ALA   A CB  
7103  N N   . PHE   E  192 ? 0.31703 0.31703 0.31703 0.00000  0.00000  0.00000  192 PHE   A N   
7104  C CA  . PHE   E  192 ? 0.36608 0.36608 0.36608 0.00000  0.00000  0.00000  192 PHE   A CA  
7105  C C   . PHE   E  192 ? 0.66810 0.66810 0.66810 0.00000  0.00000  0.00000  192 PHE   A C   
7106  O O   . PHE   E  192 ? 0.53625 0.53625 0.53625 0.00000  0.00000  0.00000  192 PHE   A O   
7107  C CB  . PHE   E  192 ? 0.38557 0.38557 0.38557 0.00000  0.00000  0.00000  192 PHE   A CB  
7108  C CG  . PHE   E  192 ? 0.48005 0.48005 0.48005 0.00000  -0.00000 -0.00000 192 PHE   A CG  
7109  C CD1 . PHE   E  192 ? 0.59589 0.59589 0.59589 -0.00000 0.00000  0.00000  192 PHE   A CD1 
7110  C CD2 . PHE   E  192 ? 0.58258 0.58258 0.58258 0.00000  0.00000  0.00000  192 PHE   A CD2 
7111  C CE1 . PHE   E  192 ? 0.35009 0.35009 0.35009 0.00000  0.00000  0.00000  192 PHE   A CE1 
7112  C CE2 . PHE   E  192 ? 0.65986 0.65986 0.65986 0.00000  -0.00000 0.00000  192 PHE   A CE2 
7113  C CZ  . PHE   E  192 ? 0.45018 0.45018 0.45018 0.00000  0.00000  0.00000  192 PHE   A CZ  
7114  N N   . ASP   E  193 ? 0.63161 0.63161 0.63161 -0.00000 0.00000  0.00000  193 ASP   A N   
7115  C CA  . ASP   E  193 ? 0.37954 0.37954 0.37954 0.00000  0.00000  0.00000  193 ASP   A CA  
7116  C C   . ASP   E  193 ? 0.71508 0.71508 0.71508 0.00000  0.00000  0.00000  193 ASP   A C   
7117  O O   . ASP   E  193 ? 0.21971 0.21971 0.21971 0.00000  0.00000  0.00000  193 ASP   A O   
7118  C CB  . ASP   E  193 ? 0.54280 0.54280 0.54280 -0.00000 0.00000  0.00000  193 ASP   A CB  
7119  C CG  . ASP   E  193 ? 1.08590 1.08590 1.08590 -0.00000 0.00000  0.00000  193 ASP   A CG  
7120  O OD1 . ASP   E  193 ? 0.58837 0.58837 0.58837 0.00000  0.00000  0.00000  193 ASP   A OD1 
7121  O OD2 . ASP   E  193 ? 0.56934 0.56934 0.56934 -0.00000 -0.00000 -0.00000 193 ASP   A OD2 
7122  N N   . GLU   E  194 ? 0.26302 0.26302 0.26302 0.00000  0.00000  0.00000  194 GLU   A N   
7123  C CA  . GLU   E  194 ? 0.60462 0.60462 0.60462 0.00000  0.00000  0.00000  194 GLU   A CA  
7124  C C   . GLU   E  194 ? 0.66005 0.66005 0.66005 -0.00000 0.00000  0.00000  194 GLU   A C   
7125  O O   . GLU   E  194 ? 0.51432 0.51432 0.51432 0.00000  0.00000  0.00000  194 GLU   A O   
7126  C CB  . GLU   E  194 ? 0.50029 0.50029 0.50029 0.00000  0.00000  0.00000  194 GLU   A CB  
7127  C CG  . GLU   E  194 ? 0.32015 0.32015 0.32015 -0.00000 0.00000  0.00000  194 GLU   A CG  
7128  C CD  . GLU   E  194 ? 1.04934 1.04934 1.04934 -0.00000 0.00000  0.00000  194 GLU   A CD  
7129  O OE1 . GLU   E  194 ? 0.72778 0.72778 0.72778 -0.00000 0.00000  0.00000  194 GLU   A OE1 
7130  O OE2 . GLU   E  194 ? 0.69678 0.69678 0.69678 0.00000  0.00000  0.00000  194 GLU   A OE2 
7131  N N   . VAL   E  195 ? 0.63453 0.63453 0.63453 -0.00000 0.00000  0.00000  195 VAL   A N   
7132  C CA  . VAL   E  195 ? 0.22671 0.22671 0.22671 0.00000  0.00000  0.00000  195 VAL   A CA  
7133  C C   . VAL   E  195 ? 1.00468 1.00468 1.00468 -0.00000 -0.00000 0.00000  195 VAL   A C   
7134  O O   . VAL   E  195 ? 0.39409 0.39409 0.39409 -0.00000 0.00000  0.00000  195 VAL   A O   
7135  C CB  . VAL   E  195 ? 0.67297 0.67297 0.67297 0.00000  0.00000  0.00000  195 VAL   A CB  
7136  C CG1 . VAL   E  195 ? 0.28885 0.28885 0.28885 0.00000  0.00000  0.00000  195 VAL   A CG1 
7137  C CG2 . VAL   E  195 ? 0.35214 0.35214 0.35214 0.00000  0.00000  0.00000  195 VAL   A CG2 
7138  N N   . PHE   E  196 ? 0.23998 0.23998 0.23998 -0.00000 0.00000  0.00000  196 PHE   A N   
7139  C CA  . PHE   E  196 ? 0.64425 0.64425 0.64425 0.00000  0.00000  0.00000  196 PHE   A CA  
7140  C C   . PHE   E  196 ? 0.39721 0.39721 0.39721 0.00000  0.00000  0.00000  196 PHE   A C   
7141  O O   . PHE   E  196 ? 0.42585 0.42585 0.42585 -0.00000 0.00000  0.00000  196 PHE   A O   
7142  C CB  . PHE   E  196 ? 0.29902 0.29902 0.29902 0.00000  0.00000  0.00000  196 PHE   A CB  
7143  C CG  . PHE   E  196 ? 0.52011 0.52011 0.52011 -0.00000 0.00000  0.00000  196 PHE   A CG  
7144  C CD1 . PHE   E  196 ? 0.31372 0.31372 0.31372 -0.00000 0.00000  0.00000  196 PHE   A CD1 
7145  C CD2 . PHE   E  196 ? 0.23030 0.23030 0.23030 0.00000  0.00000  0.00000  196 PHE   A CD2 
7146  C CE1 . PHE   E  196 ? 0.36458 0.36458 0.36458 -0.00000 0.00000  0.00000  196 PHE   A CE1 
7147  C CE2 . PHE   E  196 ? 0.46062 0.46062 0.46062 0.00000  0.00000  0.00000  196 PHE   A CE2 
7148  C CZ  . PHE   E  196 ? 0.35155 0.35155 0.35155 0.00000  0.00000  0.00000  196 PHE   A CZ  
7149  N N   . LEU   E  197 ? 0.37151 0.37151 0.37151 -0.00000 0.00000  0.00000  197 LEU   A N   
7150  C CA  . LEU   E  197 ? 0.40730 0.40730 0.40730 -0.00000 0.00000  0.00000  197 LEU   A CA  
7151  C C   . LEU   E  197 ? 0.64280 0.64280 0.64280 0.00000  0.00000  0.00000  197 LEU   A C   
7152  O O   . LEU   E  197 ? 0.33122 0.33122 0.33122 -0.00000 0.00000  0.00000  197 LEU   A O   
7153  C CB  . LEU   E  197 ? 0.37606 0.37606 0.37606 0.00000  0.00000  0.00000  197 LEU   A CB  
7154  C CG  . LEU   E  197 ? 0.33422 0.33422 0.33422 -0.00000 0.00000  0.00000  197 LEU   A CG  
7155  C CD1 . LEU   E  197 ? 0.43864 0.43864 0.43864 0.00000  0.00000  0.00000  197 LEU   A CD1 
7156  C CD2 . LEU   E  197 ? 0.93202 0.93202 0.93202 0.00000  0.00000  0.00000  197 LEU   A CD2 
7157  N N   . CYS   E  198 ? 0.52211 0.52211 0.52211 0.00000  0.00000  0.00000  198 CYS   A N   
7158  C CA  . CYS   E  198 ? 0.51165 0.51165 0.51165 -0.00000 0.00000  0.00000  198 CYS   A CA  
7159  C C   . CYS   E  198 ? 0.55763 0.55763 0.55763 -0.00000 0.00000  0.00000  198 CYS   A C   
7160  O O   . CYS   E  198 ? 0.64752 0.64752 0.64752 -0.00000 0.00000  0.00000  198 CYS   A O   
7161  C CB  . CYS   E  198 ? 0.42875 0.42875 0.42875 0.00000  0.00000  0.00000  198 CYS   A CB  
7162  S SG  . CYS   E  198 ? 0.53939 0.53939 0.53939 0.00000  0.00000  0.00000  198 CYS   A SG  
7163  N N   . ASP   E  199 ? 0.55648 0.55648 0.55648 0.00000  0.00000  0.00000  199 ASP   A N   
7164  C CA  . ASP   E  199 ? 0.41050 0.41050 0.41050 -0.00000 0.00000  0.00000  199 ASP   A CA  
7165  C C   . ASP   E  199 ? 0.84892 0.84892 0.84892 0.00000  0.00000  0.00000  199 ASP   A C   
7166  O O   . ASP   E  199 ? 0.40741 0.40741 0.40741 0.00000  0.00000  0.00000  199 ASP   A O   
7167  C CB  . ASP   E  199 ? 0.43336 0.43336 0.43336 0.00000  0.00000  0.00000  199 ASP   A CB  
7168  C CG  . ASP   E  199 ? 1.71696 1.71696 1.71696 0.00000  0.00000  -0.00000 199 ASP   A CG  
7169  O OD1 . ASP   E  199 ? 0.46928 0.46928 0.46928 -0.00000 0.00000  0.00000  199 ASP   A OD1 
7170  O OD2 . ASP   E  199 ? 0.56680 0.56680 0.56680 0.00000  0.00000  0.00000  199 ASP   A OD2 
7171  N N   . LYS   E  200 ? 0.43175 0.43175 0.43175 0.00000  -0.00000 0.00000  200 LYS   A N   
7172  C CA  . LYS   E  200 ? 0.75421 0.75421 0.75421 0.00000  0.00000  0.00000  200 LYS   A CA  
7173  C C   . LYS   E  200 ? 0.71298 0.71298 0.71298 0.00000  0.00000  0.00000  200 LYS   A C   
7174  O O   . LYS   E  200 ? 0.60807 0.60807 0.60807 -0.00000 0.00000  0.00000  200 LYS   A O   
7175  C CB  . LYS   E  200 ? 0.42941 0.42941 0.42941 0.00000  0.00000  0.00000  200 LYS   A CB  
7176  C CG  . LYS   E  200 ? 0.71804 0.71804 0.71804 0.00000  0.00000  0.00000  200 LYS   A CG  
7177  C CD  . LYS   E  200 ? 0.97780 0.97780 0.97780 0.00000  0.00000  0.00000  200 LYS   A CD  
7178  C CE  . LYS   E  200 ? 0.76602 0.76602 0.76602 0.00000  0.00000  0.00000  200 LYS   A CE  
7179  N NZ  . LYS   E  200 ? 0.69737 0.69737 0.69737 0.00000  0.00000  0.00000  200 LYS   A NZ  
7180  N N   . ASN   E  201 ? 0.58347 0.58347 0.58347 0.00000  0.00000  0.00000  201 ASN   A N   
7181  C CA  . ASN   E  201 ? 0.87682 0.87682 0.87682 0.00000  0.00000  0.00000  201 ASN   A CA  
7182  C C   . ASN   E  201 ? 0.56963 0.56963 0.56963 0.00000  0.00000  0.00000  201 ASN   A C   
7183  O O   . ASN   E  201 ? 0.97542 0.97542 0.97542 0.00000  0.00000  -0.00000 201 ASN   A O   
7184  C CB  . ASN   E  201 ? 0.54750 0.54750 0.54750 0.00000  0.00000  0.00000  201 ASN   A CB  
7185  C CG  . ASN   E  201 ? 1.02198 1.02198 1.02198 0.00000  0.00000  0.00000  201 ASN   A CG  
7186  O OD1 . ASN   E  201 ? 0.42967 0.42967 0.42967 -0.00000 0.00000  0.00000  201 ASN   A OD1 
7187  N ND2 . ASN   E  201 ? 0.61815 0.61815 0.61815 0.00000  0.00000  0.00000  201 ASN   A ND2 
7188  N N   . ALA   E  202 ? 1.18963 1.18963 1.18963 0.00000  0.00000  -0.00000 202 ALA   A N   
7189  C CA  . ALA   E  202 ? 0.58798 0.58798 0.58798 0.00000  -0.00000 0.00000  202 ALA   A CA  
7190  C C   . ALA   E  202 ? 0.50224 0.50224 0.50224 0.00000  0.00000  0.00000  202 ALA   A C   
7191  O O   . ALA   E  202 ? 0.65111 0.65111 0.65111 0.00000  0.00000  0.00000  202 ALA   A O   
7192  C CB  . ALA   E  202 ? 0.30134 0.30134 0.30134 0.00000  0.00000  0.00000  202 ALA   A CB  
7193  N N   . PRO   E  203 ? 1.00826 1.00826 1.00826 0.00000  0.00000  0.00000  203 PRO   A N   
7194  C CA  . PRO   E  203 ? 0.94266 0.94266 0.94266 0.00000  0.00000  0.00000  203 PRO   A CA  
7195  C C   . PRO   E  203 ? 0.81379 0.81379 0.81379 0.00000  0.00000  -0.00000 203 PRO   A C   
7196  O O   . PRO   E  203 ? 0.56374 0.56374 0.56374 0.00000  0.00000  0.00000  203 PRO   A O   
7197  C CB  . PRO   E  203 ? 0.65494 0.65494 0.65494 -0.00000 0.00000  0.00000  203 PRO   A CB  
7198  C CG  . PRO   E  203 ? 0.53726 0.53726 0.53726 0.00000  0.00000  0.00000  203 PRO   A CG  
7199  C CD  . PRO   E  203 ? 0.38697 0.38697 0.38697 0.00000  0.00000  0.00000  203 PRO   A CD  
7200  N N   . TYR   E  204 ? 0.49879 0.49879 0.49879 0.00000  0.00000  0.00000  204 TYR   A N   
7201  C CA  . TYR   E  204 ? 0.63899 0.63899 0.63899 0.00000  0.00000  0.00000  204 TYR   A CA  
7202  C C   . TYR   E  204 ? 0.55931 0.55931 0.55931 -0.00000 0.00000  0.00000  204 TYR   A C   
7203  O O   . TYR   E  204 ? 0.61444 0.61444 0.61444 0.00000  0.00000  0.00000  204 TYR   A O   
7204  C CB  . TYR   E  204 ? 0.47949 0.47949 0.47949 0.00000  0.00000  0.00000  204 TYR   A CB  
7205  C CG  . TYR   E  204 ? 0.53364 0.53364 0.53364 -0.00000 -0.00000 0.00000  204 TYR   A CG  
7206  C CD1 . TYR   E  204 ? 0.46729 0.46729 0.46729 -0.00000 -0.00000 0.00000  204 TYR   A CD1 
7207  C CD2 . TYR   E  204 ? 0.41900 0.41900 0.41900 0.00000  0.00000  0.00000  204 TYR   A CD2 
7208  C CE1 . TYR   E  204 ? 0.24838 0.24838 0.24838 0.00000  0.00000  0.00000  204 TYR   A CE1 
7209  C CE2 . TYR   E  204 ? 0.38155 0.38155 0.38155 -0.00000 0.00000  0.00000  204 TYR   A CE2 
7210  C CZ  . TYR   E  204 ? 0.54890 0.54890 0.54890 -0.00000 0.00000  0.00000  204 TYR   A CZ  
7211  O OH  . TYR   E  204 ? 0.57435 0.57435 0.57435 0.00000  0.00000  0.00000  204 TYR   A OH  
7212  N N   . TYR   E  205 ? 0.38146 0.38146 0.38146 0.00000  0.00000  0.00000  205 TYR   A N   
7213  C CA  . TYR   E  205 ? 0.35562 0.35562 0.35562 0.00000  0.00000  0.00000  205 TYR   A CA  
7214  C C   . TYR   E  205 ? 0.44963 0.44963 0.44963 -0.00000 0.00000  0.00000  205 TYR   A C   
7215  O O   . TYR   E  205 ? 0.42409 0.42409 0.42409 0.00000  0.00000  0.00000  205 TYR   A O   
7216  C CB  . TYR   E  205 ? 0.44578 0.44578 0.44578 0.00000  0.00000  0.00000  205 TYR   A CB  
7217  C CG  . TYR   E  205 ? 0.61937 0.61937 0.61937 0.00000  0.00000  0.00000  205 TYR   A CG  
7218  C CD1 . TYR   E  205 ? 0.52123 0.52123 0.52123 0.00000  -0.00000 0.00000  205 TYR   A CD1 
7219  C CD2 . TYR   E  205 ? 0.46110 0.46110 0.46110 0.00000  0.00000  -0.00000 205 TYR   A CD2 
7220  C CE1 . TYR   E  205 ? 0.32970 0.32970 0.32970 0.00000  0.00000  0.00000  205 TYR   A CE1 
7221  C CE2 . TYR   E  205 ? 0.63367 0.63367 0.63367 -0.00000 0.00000  0.00000  205 TYR   A CE2 
7222  C CZ  . TYR   E  205 ? 0.88563 0.88563 0.88563 -0.00000 0.00000  0.00000  205 TYR   A CZ  
7223  O OH  . TYR   E  205 ? 0.51312 0.51312 0.51312 0.00000  0.00000  0.00000  205 TYR   A OH  
7224  N N   . GLY   E  206 ? 0.48214 0.48214 0.48214 0.00000  0.00000  0.00000  206 GLY   A N   
7225  C CA  . GLY   E  206 ? 0.46805 0.46805 0.46805 0.00000  -0.00000 0.00000  206 GLY   A CA  
7226  C C   . GLY   E  206 ? 0.64269 0.64269 0.64269 0.00000  0.00000  0.00000  206 GLY   A C   
7227  O O   . GLY   E  206 ? 0.54157 0.54157 0.54157 -0.00000 0.00000  0.00000  206 GLY   A O   
7228  N N   . PHE   E  207 ? 0.37028 0.37028 0.37028 0.00000  0.00000  0.00000  207 PHE   A N   
7229  C CA  . PHE   E  207 ? 0.52301 0.52301 0.52301 0.00000  0.00000  0.00000  207 PHE   A CA  
7230  C C   . PHE   E  207 ? 0.46557 0.46557 0.46557 0.00000  0.00000  0.00000  207 PHE   A C   
7231  O O   . PHE   E  207 ? 0.59275 0.59275 0.59275 0.00000  0.00000  0.00000  207 PHE   A O   
7232  C CB  . PHE   E  207 ? 0.36262 0.36262 0.36262 -0.00000 0.00000  0.00000  207 PHE   A CB  
7233  C CG  . PHE   E  207 ? 0.56080 0.56080 0.56080 0.00000  0.00000  0.00000  207 PHE   A CG  
7234  C CD1 . PHE   E  207 ? 0.22869 0.22869 0.22869 0.00000  0.00000  0.00000  207 PHE   A CD1 
7235  C CD2 . PHE   E  207 ? 0.28412 0.28412 0.28412 -0.00000 0.00000  0.00000  207 PHE   A CD2 
7236  C CE1 . PHE   E  207 ? 0.48588 0.48588 0.48588 0.00000  0.00000  0.00000  207 PHE   A CE1 
7237  C CE2 . PHE   E  207 ? 0.33042 0.33042 0.33042 0.00000  0.00000  0.00000  207 PHE   A CE2 
7238  C CZ  . PHE   E  207 ? 0.54518 0.54518 0.54518 -0.00000 0.00000  0.00000  207 PHE   A CZ  
7239  N N   . ASN   E  208 ? 0.42163 0.42163 0.42163 0.00000  0.00000  0.00000  208 ASN   A N   
7240  C CA  . ASN   E  208 ? 0.70676 0.70676 0.70676 -0.00000 0.00000  0.00000  208 ASN   A CA  
7241  C C   . ASN   E  208 ? 0.32205 0.32205 0.32205 0.00000  0.00000  0.00000  208 ASN   A C   
7242  O O   . ASN   E  208 ? 1.05884 1.05884 1.05884 0.00000  0.00000  0.00000  208 ASN   A O   
7243  C CB  . ASN   E  208 ? 0.32775 0.32775 0.32775 0.00000  0.00000  0.00000  208 ASN   A CB  
7244  C CG  . ASN   E  208 ? 1.04294 1.04294 1.04294 0.00000  0.00000  0.00000  208 ASN   A CG  
7245  O OD1 . ASN   E  208 ? 1.74015 1.74015 1.74015 -0.00000 0.00000  0.00000  208 ASN   A OD1 
7246  N ND2 . ASN   E  208 ? 0.75133 0.75133 0.75133 0.00000  0.00000  0.00000  208 ASN   A ND2 
7247  N N   . SER   E  209 ? 0.60436 0.60436 0.60436 0.00000  0.00000  0.00000  209 SER   A N   
7248  C CA  . SER   E  209 ? 0.39493 0.39493 0.39493 0.00000  0.00000  -0.00000 209 SER   A CA  
7249  C C   . SER   E  209 ? 0.67543 0.67543 0.67543 0.00000  0.00000  0.00000  209 SER   A C   
7250  O O   . SER   E  209 ? 0.36175 0.36175 0.36175 0.00000  0.00000  0.00000  209 SER   A O   
7251  C CB  . SER   E  209 ? 0.53415 0.53415 0.53415 -0.00000 0.00000  0.00000  209 SER   A CB  
7252  O OG  . SER   E  209 ? 0.27229 0.27229 0.27229 0.00000  -0.00000 0.00000  209 SER   A OG  
7253  N N   . TYR   E  210 ? 0.43575 0.43575 0.43575 0.00000  0.00000  0.00000  210 TYR   A N   
7254  C CA  . TYR   E  210 ? 0.28521 0.28521 0.28521 0.00000  0.00000  0.00000  210 TYR   A CA  
7255  C C   . TYR   E  210 ? 0.44996 0.44996 0.44996 0.00000  0.00000  0.00000  210 TYR   A C   
7256  O O   . TYR   E  210 ? 0.36062 0.36062 0.36062 0.00000  0.00000  0.00000  210 TYR   A O   
7257  C CB  . TYR   E  210 ? 0.15102 0.15102 0.15102 0.00000  0.00000  0.00000  210 TYR   A CB  
7258  C CG  . TYR   E  210 ? 0.56989 0.56989 0.56989 0.00000  0.00000  0.00000  210 TYR   A CG  
7259  C CD1 . TYR   E  210 ? 0.27888 0.27888 0.27888 0.00000  0.00000  0.00000  210 TYR   A CD1 
7260  C CD2 . TYR   E  210 ? 0.47410 0.47410 0.47410 0.00000  0.00000  0.00000  210 TYR   A CD2 
7261  C CE1 . TYR   E  210 ? 0.32477 0.32477 0.32477 0.00000  0.00000  0.00000  210 TYR   A CE1 
7262  C CE2 . TYR   E  210 ? 0.49651 0.49651 0.49651 0.00000  0.00000  0.00000  210 TYR   A CE2 
7263  C CZ  . TYR   E  210 ? 0.61044 0.61044 0.61044 -0.00000 0.00000  0.00000  210 TYR   A CZ  
7264  O OH  . TYR   E  210 ? 0.37963 0.37963 0.37963 0.00000  0.00000  0.00000  210 TYR   A OH  
7265  N N   . ASP   E  211 ? 0.36881 0.36881 0.36881 -0.00000 0.00000  0.00000  211 ASP   A N   
7266  C CA  . ASP   E  211 ? 0.30199 0.30199 0.30199 -0.00000 0.00000  0.00000  211 ASP   A CA  
7267  C C   . ASP   E  211 ? 0.57288 0.57288 0.57288 -0.00000 0.00000  0.00000  211 ASP   A C   
7268  O O   . ASP   E  211 ? 0.33075 0.33075 0.33075 0.00000  0.00000  0.00000  211 ASP   A O   
7269  C CB  . ASP   E  211 ? 0.34175 0.34175 0.34175 0.00000  0.00000  0.00000  211 ASP   A CB  
7270  C CG  . ASP   E  211 ? 0.34863 0.34863 0.34863 0.00000  0.00000  0.00000  211 ASP   A CG  
7271  O OD1 . ASP   E  211 ? 0.40881 0.40881 0.40881 0.00000  0.00000  0.00000  211 ASP   A OD1 
7272  O OD2 . ASP   E  211 ? 0.63571 0.63571 0.63571 -0.00000 0.00000  -0.00000 211 ASP   A OD2 
7273  N N   . ASP   E  212 ? 0.31565 0.31565 0.31565 0.00000  0.00000  0.00000  212 ASP   A N   
7274  C CA  . ASP   E  212 ? 0.43620 0.43620 0.43620 0.00000  0.00000  0.00000  212 ASP   A CA  
7275  C C   . ASP   E  212 ? 0.33822 0.33822 0.33822 -0.00000 0.00000  0.00000  212 ASP   A C   
7276  O O   . ASP   E  212 ? 0.34692 0.34692 0.34692 -0.00000 0.00000  0.00000  212 ASP   A O   
7277  C CB  . ASP   E  212 ? 0.45493 0.45493 0.45493 0.00000  0.00000  0.00000  212 ASP   A CB  
7278  C CG  . ASP   E  212 ? 0.55777 0.55777 0.55777 0.00000  -0.00000 0.00000  212 ASP   A CG  
7279  O OD1 . ASP   E  212 ? 0.74775 0.74775 0.74775 0.00000  0.00000  -0.00000 212 ASP   A OD1 
7280  O OD2 . ASP   E  212 ? 0.56883 0.56883 0.56883 0.00000  0.00000  0.00000  212 ASP   A OD2 
7281  N N   . PHE   E  213 ? 0.21132 0.21132 0.21132 -0.00000 0.00000  0.00000  213 PHE   A N   
7282  C CA  . PHE   E  213 ? 0.17674 0.17674 0.17674 -0.00000 0.00000  -0.00000 213 PHE   A CA  
7283  C C   . PHE   E  213 ? 0.64420 0.64420 0.64420 -0.00000 0.00000  -0.00000 213 PHE   A C   
7284  O O   . PHE   E  213 ? 0.32121 0.32121 0.32121 -0.00000 0.00000  0.00000  213 PHE   A O   
7285  C CB  . PHE   E  213 ? 0.26133 0.26133 0.26133 -0.00000 0.00000  0.00000  213 PHE   A CB  
7286  C CG  . PHE   E  213 ? 0.42217 0.42217 0.42217 0.00000  -0.00000 0.00000  213 PHE   A CG  
7287  C CD1 . PHE   E  213 ? 0.46626 0.46626 0.46626 -0.00000 0.00000  0.00000  213 PHE   A CD1 
7288  C CD2 . PHE   E  213 ? 0.27279 0.27279 0.27279 0.00000  0.00000  0.00000  213 PHE   A CD2 
7289  C CE1 . PHE   E  213 ? 0.58627 0.58627 0.58627 0.00000  0.00000  0.00000  213 PHE   A CE1 
7290  C CE2 . PHE   E  213 ? 0.62352 0.62352 0.62352 -0.00000 0.00000  0.00000  213 PHE   A CE2 
7291  C CZ  . PHE   E  213 ? 0.48994 0.48994 0.48994 -0.00000 0.00000  0.00000  213 PHE   A CZ  
7292  N N   . PHE   E  214 ? 0.24102 0.24102 0.24102 0.00000  0.00000  0.00000  214 PHE   A N   
7293  C CA  . PHE   E  214 ? 0.21940 0.21940 0.21940 -0.00000 0.00000  0.00000  214 PHE   A CA  
7294  C C   . PHE   E  214 ? 0.20427 0.20427 0.20427 -0.00000 0.00000  0.00000  214 PHE   A C   
7295  O O   . PHE   E  214 ? 0.55412 0.55412 0.55412 0.00000  0.00000  0.00000  214 PHE   A O   
7296  C CB  . PHE   E  214 ? 0.33002 0.33002 0.33002 0.00000  0.00000  0.00000  214 PHE   A CB  
7297  C CG  . PHE   E  214 ? 0.30736 0.30736 0.30736 0.00000  0.00000  0.00000  214 PHE   A CG  
7298  C CD1 . PHE   E  214 ? 0.28885 0.28885 0.28885 -0.00000 0.00000  0.00000  214 PHE   A CD1 
7299  C CD2 . PHE   E  214 ? 0.40150 0.40150 0.40150 0.00000  0.00000  -0.00000 214 PHE   A CD2 
7300  C CE1 . PHE   E  214 ? 0.24382 0.24382 0.24382 0.00000  0.00000  0.00000  214 PHE   A CE1 
7301  C CE2 . PHE   E  214 ? 0.39379 0.39379 0.39379 -0.00000 0.00000  0.00000  214 PHE   A CE2 
7302  C CZ  . PHE   E  214 ? 0.31678 0.31678 0.31678 0.00000  0.00000  0.00000  214 PHE   A CZ  
7303  N N   . ASN   E  215 ? 0.27021 0.27021 0.27021 0.00000  0.00000  0.00000  215 ASN   A N   
7304  C CA  . ASN   E  215 ? 0.36721 0.36721 0.36721 -0.00000 0.00000  0.00000  215 ASN   A CA  
7305  C C   . ASN   E  215 ? 0.49110 0.49110 0.49110 0.00000  0.00000  0.00000  215 ASN   A C   
7306  O O   . ASN   E  215 ? 0.41187 0.41187 0.41187 0.00000  0.00000  0.00000  215 ASN   A O   
7307  C CB  . ASN   E  215 ? 0.36527 0.36527 0.36527 0.00000  0.00000  0.00000  215 ASN   A CB  
7308  C CG  . ASN   E  215 ? 0.65811 0.65811 0.65811 0.00000  0.00000  0.00000  215 ASN   A CG  
7309  O OD1 . ASN   E  215 ? 0.38784 0.38784 0.38784 0.00000  0.00000  0.00000  215 ASN   A OD1 
7310  N ND2 . ASN   E  215 ? 0.34640 0.34640 0.34640 0.00000  0.00000  0.00000  215 ASN   A ND2 
7311  N N   . ARG   E  216 ? 0.24224 0.24224 0.24224 -0.00000 0.00000  0.00000  216 ARG   A N   
7312  C CA  . ARG   E  216 ? 0.35472 0.35472 0.35472 -0.00000 0.00000  0.00000  216 ARG   A CA  
7313  C C   . ARG   E  216 ? 0.64656 0.64656 0.64656 -0.00000 0.00000  0.00000  216 ARG   A C   
7314  O O   . ARG   E  216 ? 0.34494 0.34494 0.34494 -0.00000 0.00000  0.00000  216 ARG   A O   
7315  C CB  . ARG   E  216 ? 0.30764 0.30764 0.30764 0.00000  0.00000  0.00000  216 ARG   A CB  
7316  C CG  . ARG   E  216 ? 0.29866 0.29866 0.29866 -0.00000 0.00000  0.00000  216 ARG   A CG  
7317  C CD  . ARG   E  216 ? 0.42929 0.42929 0.42929 -0.00000 0.00000  0.00000  216 ARG   A CD  
7318  N NE  . ARG   E  216 ? 0.28922 0.28922 0.28922 0.00000  0.00000  0.00000  216 ARG   A NE  
7319  C CZ  . ARG   E  216 ? 0.60305 0.60305 0.60305 0.00000  0.00000  -0.00000 216 ARG   A CZ  
7320  N NH1 . ARG   E  216 ? 0.33471 0.33471 0.33471 -0.00000 0.00000  0.00000  216 ARG   A NH1 
7321  N NH2 . ARG   E  216 ? 0.39151 0.39151 0.39151 0.00000  0.00000  0.00000  216 ARG   A NH2 
7322  N N   . ARG   E  217 ? 0.39576 0.39576 0.39576 0.00000  0.00000  0.00000  217 ARG   A N   
7323  C CA  . ARG   E  217 ? 0.34947 0.34947 0.34947 0.00000  0.00000  0.00000  217 ARG   A CA  
7324  C C   . ARG   E  217 ? 1.39570 1.39570 1.39570 0.00000  0.00000  0.00000  217 ARG   A C   
7325  O O   . ARG   E  217 ? 0.24588 0.24588 0.24588 0.00000  0.00000  0.00000  217 ARG   A O   
7326  C CB  . ARG   E  217 ? 0.38487 0.38487 0.38487 0.00000  0.00000  0.00000  217 ARG   A CB  
7327  C CG  . ARG   E  217 ? 0.71206 0.71206 0.71206 0.00000  0.00000  0.00000  217 ARG   A CG  
7328  C CD  . ARG   E  217 ? 0.38867 0.38867 0.38867 0.00000  0.00000  0.00000  217 ARG   A CD  
7329  N NE  . ARG   E  217 ? 0.57179 0.57179 0.57179 0.00000  0.00000  0.00000  217 ARG   A NE  
7330  C CZ  . ARG   E  217 ? 0.28682 0.28682 0.28682 0.00000  0.00000  0.00000  217 ARG   A CZ  
7331  N NH1 . ARG   E  217 ? 0.42023 0.42023 0.42023 0.00000  0.00000  0.00000  217 ARG   A NH1 
7332  N NH2 . ARG   E  217 ? 0.98028 0.98028 0.98028 0.00000  0.00000  0.00000  217 ARG   A NH2 
7333  N N   . PHE   E  218 ? 0.45142 0.45142 0.45142 0.00000  0.00000  -0.00000 218 PHE   A N   
7334  C CA  . PHE   E  218 ? 0.31043 0.31043 0.31043 0.00000  0.00000  0.00000  218 PHE   A CA  
7335  C C   . PHE   E  218 ? 0.69609 0.69609 0.69609 -0.00000 0.00000  0.00000  218 PHE   A C   
7336  O O   . PHE   E  218 ? 0.33843 0.33843 0.33843 0.00000  0.00000  0.00000  218 PHE   A O   
7337  C CB  . PHE   E  218 ? 0.19455 0.19455 0.19455 0.00000  0.00000  0.00000  218 PHE   A CB  
7338  C CG  . PHE   E  218 ? 0.44350 0.44350 0.44350 -0.00000 0.00000  0.00000  218 PHE   A CG  
7339  C CD1 . PHE   E  218 ? 0.21568 0.21568 0.21568 0.00000  0.00000  0.00000  218 PHE   A CD1 
7340  C CD2 . PHE   E  218 ? 0.32537 0.32537 0.32537 0.00000  0.00000  -0.00000 218 PHE   A CD2 
7341  C CE1 . PHE   E  218 ? 0.53547 0.53547 0.53547 0.00000  0.00000  0.00000  218 PHE   A CE1 
7342  C CE2 . PHE   E  218 ? 0.31609 0.31609 0.31609 0.00000  0.00000  0.00000  218 PHE   A CE2 
7343  C CZ  . PHE   E  218 ? 0.23067 0.23067 0.23067 0.00000  0.00000  0.00000  218 PHE   A CZ  
7344  N N   . ARG   E  219 ? 0.44205 0.44205 0.44205 0.00000  0.00000  0.00000  219 ARG   A N   
7345  C CA  . ARG   E  219 ? 0.49690 0.49690 0.49690 0.00000  0.00000  0.00000  219 ARG   A CA  
7346  C C   . ARG   E  219 ? 0.45814 0.45814 0.45814 0.00000  0.00000  0.00000  219 ARG   A C   
7347  O O   . ARG   E  219 ? 0.43960 0.43960 0.43960 0.00000  0.00000  0.00000  219 ARG   A O   
7348  C CB  . ARG   E  219 ? 0.40555 0.40555 0.40555 0.00000  0.00000  0.00000  219 ARG   A CB  
7349  C CG  . ARG   E  219 ? 0.61376 0.61376 0.61376 0.00000  0.00000  0.00000  219 ARG   A CG  
7350  C CD  . ARG   E  219 ? 0.48590 0.48590 0.48590 -0.00000 0.00000  0.00000  219 ARG   A CD  
7351  N NE  . ARG   E  219 ? 0.31019 0.31019 0.31019 0.00000  0.00000  0.00000  219 ARG   A NE  
7352  C CZ  . ARG   E  219 ? 1.17025 1.17025 1.17025 -0.00000 0.00000  0.00000  219 ARG   A CZ  
7353  N NH1 . ARG   E  219 ? 0.31341 0.31341 0.31341 0.00000  0.00000  0.00000  219 ARG   A NH1 
7354  N NH2 . ARG   E  219 ? 0.20975 0.20975 0.20975 -0.00000 0.00000  0.00000  219 ARG   A NH2 
7355  N N   . ASN   E  220 ? 0.39567 0.39567 0.39567 0.00000  0.00000  0.00000  220 ASN   A N   
7356  C CA  . ASN   E  220 ? 0.47226 0.47226 0.47226 -0.00000 0.00000  0.00000  220 ASN   A CA  
7357  C C   . ASN   E  220 ? 0.43284 0.43284 0.43284 0.00000  0.00000  0.00000  220 ASN   A C   
7358  O O   . ASN   E  220 ? 0.50177 0.50177 0.50177 0.00000  0.00000  0.00000  220 ASN   A O   
7359  C CB  . ASN   E  220 ? 0.57245 0.57245 0.57245 0.00000  0.00000  0.00000  220 ASN   A CB  
7360  C CG  . ASN   E  220 ? 0.89267 0.89267 0.89267 -0.00000 -0.00000 0.00000  220 ASN   A CG  
7361  O OD1 . ASN   E  220 ? 0.57918 0.57918 0.57918 0.00000  -0.00000 0.00000  220 ASN   A OD1 
7362  N ND2 . ASN   E  220 ? 0.59545 0.59545 0.59545 -0.00000 0.00000  0.00000  220 ASN   A ND2 
7363  N N   . ARG   E  221 ? 0.44179 0.44179 0.44179 0.00000  0.00000  0.00000  221 ARG   A N   
7364  C CA  . ARG   E  221 ? 0.48412 0.48412 0.48412 0.00000  0.00000  0.00000  221 ARG   A CA  
7365  C C   . ARG   E  221 ? 0.59419 0.59419 0.59419 -0.00000 0.00000  0.00000  221 ARG   A C   
7366  O O   . ARG   E  221 ? 0.46669 0.46669 0.46669 -0.00000 0.00000  0.00000  221 ARG   A O   
7367  C CB  . ARG   E  221 ? 0.32550 0.32550 0.32550 -0.00000 0.00000  0.00000  221 ARG   A CB  
7368  C CG  . ARG   E  221 ? 0.33215 0.33215 0.33215 -0.00000 0.00000  0.00000  221 ARG   A CG  
7369  C CD  . ARG   E  221 ? 0.48032 0.48032 0.48032 0.00000  0.00000  0.00000  221 ARG   A CD  
7370  N NE  . ARG   E  221 ? 0.41738 0.41738 0.41738 0.00000  0.00000  0.00000  221 ARG   A NE  
7371  C CZ  . ARG   E  221 ? 0.56340 0.56340 0.56340 -0.00000 0.00000  0.00000  221 ARG   A CZ  
7372  N NH1 . ARG   E  221 ? 0.49211 0.49211 0.49211 0.00000  0.00000  0.00000  221 ARG   A NH1 
7373  N NH2 . ARG   E  221 ? 0.37457 0.37457 0.37457 0.00000  0.00000  0.00000  221 ARG   A NH2 
7374  N N   . ASP   E  222 ? 0.42211 0.42211 0.42211 0.00000  0.00000  0.00000  222 ASP   A N   
7375  C CA  . ASP   E  222 ? 0.63720 0.63720 0.63720 -0.00000 0.00000  0.00000  222 ASP   A CA  
7376  C C   . ASP   E  222 ? 0.67173 0.67173 0.67173 0.00000  0.00000  -0.00000 222 ASP   A C   
7377  O O   . ASP   E  222 ? 0.50483 0.50483 0.50483 -0.00000 0.00000  0.00000  222 ASP   A O   
7378  C CB  . ASP   E  222 ? 0.35252 0.35252 0.35252 0.00000  0.00000  0.00000  222 ASP   A CB  
7379  C CG  . ASP   E  222 ? 0.59306 0.59306 0.59306 0.00000  0.00000  0.00000  222 ASP   A CG  
7380  O OD1 . ASP   E  222 ? 0.68127 0.68127 0.68127 0.00000  0.00000  0.00000  222 ASP   A OD1 
7381  O OD2 . ASP   E  222 ? 0.79695 0.79695 0.79695 0.00000  0.00000  0.00000  222 ASP   A OD2 
7382  N N   . ILE   E  223 ? 0.29087 0.29087 0.29087 0.00000  0.00000  0.00000  223 ILE   A N   
7383  C CA  . ILE   E  223 ? 0.41190 0.41190 0.41190 0.00000  0.00000  0.00000  223 ILE   A CA  
7384  C C   . ILE   E  223 ? 0.55387 0.55387 0.55387 -0.00000 0.00000  0.00000  223 ILE   A C   
7385  O O   . ILE   E  223 ? 0.58587 0.58587 0.58587 -0.00000 0.00000  0.00000  223 ILE   A O   
7386  C CB  . ILE   E  223 ? 0.57185 0.57185 0.57185 0.00000  -0.00000 0.00000  223 ILE   A CB  
7387  C CG1 . ILE   E  223 ? 0.33143 0.33143 0.33143 0.00000  0.00000  0.00000  223 ILE   A CG1 
7388  C CG2 . ILE   E  223 ? 0.17677 0.17677 0.17677 0.00000  0.00000  0.00000  223 ILE   A CG2 
7389  C CD1 . ILE   E  223 ? 0.36978 0.36978 0.36978 0.00000  0.00000  0.00000  223 ILE   A CD1 
7390  N N   . ASP   E  224 ? 0.41713 0.41713 0.41713 -0.00000 0.00000  0.00000  224 ASP   A N   
7391  C CA  . ASP   E  224 ? 0.43113 0.43113 0.43113 0.00000  0.00000  0.00000  224 ASP   A CA  
7392  C C   . ASP   E  224 ? 0.44223 0.44223 0.44223 0.00000  0.00000  0.00000  224 ASP   A C   
7393  O O   . ASP   E  224 ? 0.38640 0.38640 0.38640 0.00000  0.00000  0.00000  224 ASP   A O   
7394  C CB  . ASP   E  224 ? 0.37933 0.37933 0.37933 0.00000  0.00000  0.00000  224 ASP   A CB  
7395  C CG  . ASP   E  224 ? 0.54865 0.54865 0.54865 0.00000  0.00000  0.00000  224 ASP   A CG  
7396  O OD1 . ASP   E  224 ? 0.58829 0.58829 0.58829 -0.00000 0.00000  0.00000  224 ASP   A OD1 
7397  O OD2 . ASP   E  224 ? 0.54424 0.54424 0.54424 0.00000  -0.00000 0.00000  224 ASP   A OD2 
7398  N N   . ARG   E  225 ? 0.54886 0.54886 0.54886 0.00000  0.00000  -0.00000 225 ARG   A N   
7399  C CA  . ARG   E  225 ? 0.43074 0.43074 0.43074 -0.00000 0.00000  0.00000  225 ARG   A CA  
7400  C C   . ARG   E  225 ? 0.62197 0.62197 0.62197 0.00000  -0.00000 0.00000  225 ARG   A C   
7401  O O   . ARG   E  225 ? 0.54645 0.54645 0.54645 0.00000  0.00000  0.00000  225 ARG   A O   
7402  C CB  . ARG   E  225 ? 0.44407 0.44407 0.44407 0.00000  0.00000  0.00000  225 ARG   A CB  
7403  C CG  . ARG   E  225 ? 0.19481 0.19481 0.19481 0.00000  0.00000  -0.00000 225 ARG   A CG  
7404  C CD  . ARG   E  225 ? 0.17111 0.17111 0.17111 0.00000  0.00000  -0.00000 225 ARG   A CD  
7405  N NE  . ARG   E  225 ? 0.58214 0.58214 0.58214 0.00000  0.00000  0.00000  225 ARG   A NE  
7406  C CZ  . ARG   E  225 ? 0.34062 0.34062 0.34062 0.00000  0.00000  0.00000  225 ARG   A CZ  
7407  N NH1 . ARG   E  225 ? 0.62857 0.62857 0.62857 -0.00000 0.00000  0.00000  225 ARG   A NH1 
7408  N NH2 . ARG   E  225 ? 0.13401 0.13401 0.13401 0.00000  0.00000  0.00000  225 ARG   A NH2 
7409  N N   . PRO   E  226 ? 0.49270 0.49270 0.49270 0.00000  0.00000  0.00000  226 PRO   A N   
7410  C CA  . PRO   E  226 ? 0.26222 0.26222 0.26222 0.00000  0.00000  0.00000  226 PRO   A CA  
7411  C C   . PRO   E  226 ? 0.57298 0.57298 0.57298 0.00000  0.00000  0.00000  226 PRO   A C   
7412  O O   . PRO   E  226 ? 0.36060 0.36060 0.36060 0.00000  0.00000  0.00000  226 PRO   A O   
7413  C CB  . PRO   E  226 ? 0.25102 0.25102 0.25102 -0.00000 0.00000  0.00000  226 PRO   A CB  
7414  C CG  . PRO   E  226 ? 0.23553 0.23553 0.23553 -0.00000 0.00000  0.00000  226 PRO   A CG  
7415  C CD  . PRO   E  226 ? 0.27609 0.27609 0.27609 -0.00000 0.00000  0.00000  226 PRO   A CD  
7416  N N   . VAL   E  227 ? 0.32822 0.32822 0.32822 -0.00000 0.00000  0.00000  227 VAL   A N   
7417  C CA  . VAL   E  227 ? 0.29053 0.29053 0.29053 0.00000  -0.00000 0.00000  227 VAL   A CA  
7418  C C   . VAL   E  227 ? 0.44803 0.44803 0.44803 0.00000  0.00000  0.00000  227 VAL   A C   
7419  O O   . VAL   E  227 ? 0.46057 0.46057 0.46057 -0.00000 0.00000  0.00000  227 VAL   A O   
7420  C CB  . VAL   E  227 ? 0.33070 0.33070 0.33070 -0.00000 0.00000  0.00000  227 VAL   A CB  
7421  C CG1 . VAL   E  227 ? 0.34537 0.34537 0.34537 0.00000  0.00000  0.00000  227 VAL   A CG1 
7422  C CG2 . VAL   E  227 ? 0.27021 0.27021 0.27021 0.00000  0.00000  0.00000  227 VAL   A CG2 
7423  N N   . VAL   E  228 ? 0.34116 0.34116 0.34116 0.00000  0.00000  0.00000  228 VAL   A N   
7424  C CA  . VAL   E  228 ? 0.18401 0.18401 0.18401 0.00000  0.00000  0.00000  228 VAL   A CA  
7425  C C   . VAL   E  228 ? 0.69423 0.69423 0.69423 0.00000  0.00000  0.00000  228 VAL   A C   
7426  O O   . VAL   E  228 ? 0.31771 0.31771 0.31771 0.00000  0.00000  0.00000  228 VAL   A O   
7427  C CB  . VAL   E  228 ? 0.41725 0.41725 0.41725 0.00000  0.00000  -0.00000 228 VAL   A CB  
7428  C CG1 . VAL   E  228 ? 0.24494 0.24494 0.24494 0.00000  0.00000  0.00000  228 VAL   A CG1 
7429  C CG2 . VAL   E  228 ? 0.17673 0.17673 0.17673 0.00000  0.00000  0.00000  228 VAL   A CG2 
7430  N N   . GLY   E  229 ? 0.46567 0.46567 0.46567 0.00000  0.00000  0.00000  229 GLY   A N   
7431  C CA  . GLY   E  229 ? 0.26184 0.26184 0.26184 0.00000  0.00000  0.00000  229 GLY   A CA  
7432  C C   . GLY   E  229 ? 0.35070 0.35070 0.35070 -0.00000 0.00000  0.00000  229 GLY   A C   
7433  O O   . GLY   E  229 ? 0.54323 0.54323 0.54323 0.00000  -0.00000 0.00000  229 GLY   A O   
7434  N N   . GLY   E  230 ? 0.45102 0.45102 0.45102 0.00000  0.00000  0.00000  230 GLY   A N   
7435  C CA  . GLY   E  230 ? 0.10455 0.10455 0.10455 0.00000  0.00000  0.00000  230 GLY   A CA  
7436  C C   . GLY   E  230 ? 0.68671 0.68671 0.68671 -0.00000 0.00000  0.00000  230 GLY   A C   
7437  O O   . GLY   E  230 ? 0.30685 0.30685 0.30685 -0.00000 0.00000  0.00000  230 GLY   A O   
7438  N N   . VAL   E  231 ? 0.25805 0.25805 0.25805 0.00000  0.00000  0.00000  231 VAL   A N   
7439  C CA  . VAL   E  231 ? 0.76902 0.76902 0.76902 -0.00000 0.00000  0.00000  231 VAL   A CA  
7440  C C   . VAL   E  231 ? 0.26069 0.26069 0.26069 0.00000  0.00000  0.00000  231 VAL   A C   
7441  O O   . VAL   E  231 ? 0.70540 0.70540 0.70540 -0.00000 0.00000  0.00000  231 VAL   A O   
7442  C CB  . VAL   E  231 ? 0.16696 0.16696 0.16696 -0.00000 0.00000  0.00000  231 VAL   A CB  
7443  C CG1 . VAL   E  231 ? 0.86109 0.86109 0.86109 0.00000  0.00000  0.00000  231 VAL   A CG1 
7444  C CG2 . VAL   E  231 ? 0.51341 0.51341 0.51341 0.00000  0.00000  0.00000  231 VAL   A CG2 
7445  N N   . ASN   E  232 ? 0.54167 0.54167 0.54167 -0.00000 -0.00000 0.00000  232 ASN   A N   
7446  C CA  . ASN   E  232 ? 0.40205 0.40205 0.40205 -0.00000 0.00000  0.00000  232 ASN   A CA  
7447  C C   . ASN   E  232 ? 0.55002 0.55002 0.55002 -0.00000 0.00000  0.00000  232 ASN   A C   
7448  O O   . ASN   E  232 ? 0.48933 0.48933 0.48933 -0.00000 0.00000  0.00000  232 ASN   A O   
7449  C CB  . ASN   E  232 ? 0.61412 0.61412 0.61412 0.00000  0.00000  0.00000  232 ASN   A CB  
7450  C CG  . ASN   E  232 ? 0.60932 0.60932 0.60932 -0.00000 0.00000  0.00000  232 ASN   A CG  
7451  O OD1 . ASN   E  232 ? 0.62206 0.62206 0.62206 0.00000  0.00000  0.00000  232 ASN   A OD1 
7452  N ND2 . ASN   E  232 ? 1.57355 1.57355 1.57355 0.00000  0.00000  0.00000  232 ASN   A ND2 
7453  N N   . ASN   E  233 ? 0.32875 0.32875 0.32875 0.00000  0.00000  0.00000  233 ASN   A N   
7454  C CA  . ASN   E  233 ? 0.42627 0.42627 0.42627 0.00000  0.00000  0.00000  233 ASN   A CA  
7455  C C   . ASN   E  233 ? 1.09079 1.09079 1.09079 -0.00000 0.00000  0.00000  233 ASN   A C   
7456  O O   . ASN   E  233 ? 0.39775 0.39775 0.39775 0.00000  0.00000  0.00000  233 ASN   A O   
7457  C CB  . ASN   E  233 ? 0.17187 0.17187 0.17187 0.00000  0.00000  0.00000  233 ASN   A CB  
7458  C CG  . ASN   E  233 ? 0.64542 0.64542 0.64542 -0.00000 0.00000  0.00000  233 ASN   A CG  
7459  O OD1 . ASN   E  233 ? 0.55756 0.55756 0.55756 -0.00000 0.00000  0.00000  233 ASN   A OD1 
7460  N ND2 . ASN   E  233 ? 0.50293 0.50293 0.50293 0.00000  0.00000  0.00000  233 ASN   A ND2 
7461  N N   . THR   E  234 ? 0.32247 0.32247 0.32247 0.00000  0.00000  0.00000  234 THR   A N   
7462  C CA  . THR   E  234 ? 0.51668 0.51668 0.51668 0.00000  -0.00000 0.00000  234 THR   A CA  
7463  C C   . THR   E  234 ? 0.26634 0.26634 0.26634 -0.00000 0.00000  -0.00000 234 THR   A C   
7464  O O   . THR   E  234 ? 0.90590 0.90590 0.90590 0.00000  0.00000  0.00000  234 THR   A O   
7465  C CB  . THR   E  234 ? 0.33806 0.33806 0.33806 0.00000  0.00000  0.00000  234 THR   A CB  
7466  O OG1 . THR   E  234 ? 0.46704 0.46704 0.46704 -0.00000 0.00000  0.00000  234 THR   A OG1 
7467  C CG2 . THR   E  234 ? 0.21125 0.21125 0.21125 0.00000  0.00000  0.00000  234 THR   A CG2 
7468  N N   . THR   E  235 ? 0.56499 0.56499 0.56499 0.00000  0.00000  0.00000  235 THR   A N   
7469  C CA  . THR   E  235 ? 0.33968 0.33968 0.33968 -0.00000 0.00000  0.00000  235 THR   A CA  
7470  C C   . THR   E  235 ? 0.59430 0.59430 0.59430 0.00000  0.00000  0.00000  235 THR   A C   
7471  O O   . THR   E  235 ? 0.38224 0.38224 0.38224 0.00000  0.00000  0.00000  235 THR   A O   
7472  C CB  . THR   E  235 ? 0.78486 0.78486 0.78486 0.00000  0.00000  0.00000  235 THR   A CB  
7473  O OG1 . THR   E  235 ? 0.29332 0.29332 0.29332 0.00000  0.00000  0.00000  235 THR   A OG1 
7474  C CG2 . THR   E  235 ? 0.41957 0.41957 0.41957 -0.00000 0.00000  0.00000  235 THR   A CG2 
7475  N N   . LEU   E  236 ? 0.53536 0.53536 0.53536 -0.00000 -0.00000 0.00000  236 LEU   A N   
7476  C CA  . LEU   E  236 ? 0.54133 0.54133 0.54133 0.00000  0.00000  0.00000  236 LEU   A CA  
7477  C C   . LEU   E  236 ? 0.46050 0.46050 0.46050 0.00000  0.00000  0.00000  236 LEU   A C   
7478  O O   . LEU   E  236 ? 0.48227 0.48227 0.48227 0.00000  -0.00000 0.00000  236 LEU   A O   
7479  C CB  . LEU   E  236 ? 0.45934 0.45934 0.45934 0.00000  0.00000  0.00000  236 LEU   A CB  
7480  C CG  . LEU   E  236 ? 0.55171 0.55171 0.55171 0.00000  0.00000  0.00000  236 LEU   A CG  
7481  C CD1 . LEU   E  236 ? 0.44976 0.44976 0.44976 0.00000  0.00000  0.00000  236 LEU   A CD1 
7482  C CD2 . LEU   E  236 ? 0.32914 0.32914 0.32914 -0.00000 0.00000  0.00000  236 LEU   A CD2 
7483  N N   . ILE   E  237 ? 0.42074 0.42074 0.42074 -0.00000 0.00000  0.00000  237 ILE   A N   
7484  C CA  . ILE   E  237 ? 0.33622 0.33622 0.33622 -0.00000 0.00000  0.00000  237 ILE   A CA  
7485  C C   . ILE   E  237 ? 0.47853 0.47853 0.47853 -0.00000 0.00000  0.00000  237 ILE   A C   
7486  O O   . ILE   E  237 ? 0.31291 0.31291 0.31291 0.00000  0.00000  0.00000  237 ILE   A O   
7487  C CB  . ILE   E  237 ? 0.32132 0.32132 0.32132 0.00000  0.00000  0.00000  237 ILE   A CB  
7488  C CG1 . ILE   E  237 ? 0.28234 0.28234 0.28234 0.00000  0.00000  0.00000  237 ILE   A CG1 
7489  C CG2 . ILE   E  237 ? 0.29433 0.29433 0.29433 -0.00000 0.00000  0.00000  237 ILE   A CG2 
7490  C CD1 . ILE   E  237 ? 0.30634 0.30634 0.30634 0.00000  0.00000  0.00000  237 ILE   A CD1 
7491  N N   . SER   E  238 ? 0.26785 0.26785 0.26785 0.00000  0.00000  0.00000  238 SER   A N   
7492  C CA  . SER   E  238 ? 0.35358 0.35358 0.35358 -0.00000 0.00000  0.00000  238 SER   A CA  
7493  C C   . SER   E  238 ? 0.46435 0.46435 0.46435 0.00000  0.00000  0.00000  238 SER   A C   
7494  O O   . SER   E  238 ? 0.27402 0.27402 0.27402 0.00000  0.00000  0.00000  238 SER   A O   
7495  C CB  . SER   E  238 ? 0.33411 0.33411 0.33411 0.00000  0.00000  0.00000  238 SER   A CB  
7496  O OG  . SER   E  238 ? 0.50865 0.50865 0.50865 0.00000  0.00000  0.00000  238 SER   A OG  
7497  N N   . ALA   E  239 ? 0.50106 0.50106 0.50106 -0.00000 0.00000  0.00000  239 ALA   A N   
7498  C CA  . ALA   E  239 ? 0.60308 0.60308 0.60308 -0.00000 -0.00000 0.00000  239 ALA   A CA  
7499  C C   . ALA   E  239 ? 0.30165 0.30165 0.30165 0.00000  0.00000  0.00000  239 ALA   A C   
7500  O O   . ALA   E  239 ? 0.49711 0.49711 0.49711 -0.00000 0.00000  0.00000  239 ALA   A O   
7501  C CB  . ALA   E  239 ? 0.25574 0.25574 0.25574 0.00000  0.00000  0.00000  239 ALA   A CB  
7502  N N   . ALA   E  240 ? 0.45807 0.45807 0.45807 0.00000  -0.00000 0.00000  240 ALA   A N   
7503  C CA  . ALA   E  240 ? 0.37726 0.37726 0.37726 0.00000  0.00000  0.00000  240 ALA   A CA  
7504  C C   . ALA   E  240 ? 0.45920 0.45920 0.45920 0.00000  0.00000  0.00000  240 ALA   A C   
7505  O O   . ALA   E  240 ? 0.39987 0.39987 0.39987 0.00000  0.00000  0.00000  240 ALA   A O   
7506  C CB  . ALA   E  240 ? 0.27252 0.27252 0.27252 0.00000  0.00000  0.00000  240 ALA   A CB  
7507  N N   . CYS   E  241 ? 0.22163 0.22163 0.22163 0.00000  0.00000  0.00000  241 CYS   A N   
7508  C CA  . CYS   E  241 ? 0.34709 0.34709 0.34709 0.00000  0.00000  0.00000  241 CYS   A CA  
7509  C C   . CYS   E  241 ? 0.35101 0.35101 0.35101 -0.00000 0.00000  0.00000  241 CYS   A C   
7510  O O   . CYS   E  241 ? 0.33838 0.33838 0.33838 0.00000  0.00000  0.00000  241 CYS   A O   
7511  C CB  . CYS   E  241 ? 0.36783 0.36783 0.36783 0.00000  -0.00000 0.00000  241 CYS   A CB  
7512  S SG  . CYS   E  241 ? 0.37107 0.37107 0.37107 0.00000  0.00000  0.00000  241 CYS   A SG  
7513  N N   . GLU   E  242 ? 0.38374 0.38374 0.38374 0.00000  0.00000  0.00000  242 GLU   A N   
7514  C CA  . GLU   E  242 ? 0.17689 0.17689 0.17689 -0.00000 0.00000  0.00000  242 GLU   A CA  
7515  C C   . GLU   E  242 ? 0.21364 0.21364 0.21364 0.00000  -0.00000 0.00000  242 GLU   A C   
7516  O O   . GLU   E  242 ? 0.49963 0.49963 0.49963 -0.00000 0.00000  0.00000  242 GLU   A O   
7517  C CB  . GLU   E  242 ? 0.31470 0.31470 0.31470 -0.00000 0.00000  0.00000  242 GLU   A CB  
7518  C CG  . GLU   E  242 ? 0.24293 0.24293 0.24293 0.00000  0.00000  0.00000  242 GLU   A CG  
7519  C CD  . GLU   E  242 ? 0.54695 0.54695 0.54695 0.00000  0.00000  0.00000  242 GLU   A CD  
7520  O OE1 . GLU   E  242 ? 0.28701 0.28701 0.28701 0.00000  0.00000  0.00000  242 GLU   A OE1 
7521  O OE2 . GLU   E  242 ? 0.36990 0.36990 0.36990 -0.00000 0.00000  0.00000  242 GLU   A OE2 
7522  N N   . SER   E  243 ? 0.30199 0.30199 0.30199 -0.00000 0.00000  0.00000  243 SER   A N   
7523  C CA  . SER   E  243 ? 0.44743 0.44743 0.44743 0.00000  0.00000  0.00000  243 SER   A CA  
7524  C C   . SER   E  243 ? 0.32372 0.32372 0.32372 0.00000  0.00000  0.00000  243 SER   A C   
7525  O O   . SER   E  243 ? 0.38077 0.38077 0.38077 0.00000  0.00000  0.00000  243 SER   A O   
7526  C CB  . SER   E  243 ? 0.31103 0.31103 0.31103 -0.00000 0.00000  0.00000  243 SER   A CB  
7527  O OG  . SER   E  243 ? 0.40597 0.40597 0.40597 0.00000  0.00000  0.00000  243 SER   A OG  
7528  N N   . LEU   E  244 ? 0.37372 0.37372 0.37372 0.00000  0.00000  0.00000  244 LEU   A N   
7529  C CA  . LEU   E  244 ? 0.44383 0.44383 0.44383 -0.00000 0.00000  0.00000  244 LEU   A CA  
7530  C C   . LEU   E  244 ? 0.41221 0.41221 0.41221 0.00000  0.00000  0.00000  244 LEU   A C   
7531  O O   . LEU   E  244 ? 0.49176 0.49176 0.49176 0.00000  0.00000  0.00000  244 LEU   A O   
7532  C CB  . LEU   E  244 ? 0.25218 0.25218 0.25218 -0.00000 0.00000  0.00000  244 LEU   A CB  
7533  C CG  . LEU   E  244 ? 0.48570 0.48570 0.48570 -0.00000 0.00000  0.00000  244 LEU   A CG  
7534  C CD1 . LEU   E  244 ? 0.40921 0.40921 0.40921 0.00000  0.00000  0.00000  244 LEU   A CD1 
7535  C CD2 . LEU   E  244 ? 0.32345 0.32345 0.32345 -0.00000 0.00000  0.00000  244 LEU   A CD2 
7536  N N   . SER   E  245 ? 0.75179 0.75179 0.75179 0.00000  0.00000  0.00000  245 SER   A N   
7537  C CA  . SER   E  245 ? 0.25306 0.25306 0.25306 -0.00000 0.00000  0.00000  245 SER   A CA  
7538  C C   . SER   E  245 ? 0.25364 0.25364 0.25364 0.00000  0.00000  0.00000  245 SER   A C   
7539  O O   . SER   E  245 ? 0.36715 0.36715 0.36715 0.00000  0.00000  0.00000  245 SER   A O   
7540  C CB  . SER   E  245 ? 0.28777 0.28777 0.28777 0.00000  -0.00000 0.00000  245 SER   A CB  
7541  O OG  . SER   E  245 ? 0.86495 0.86495 0.86495 0.00000  -0.00000 0.00000  245 SER   A OG  
7542  N N   . TYR   E  246 ? 0.44678 0.44678 0.44678 0.00000  0.00000  0.00000  246 TYR   A N   
7543  C CA  . TYR   E  246 ? 0.32185 0.32185 0.32185 -0.00000 0.00000  0.00000  246 TYR   A CA  
7544  C C   . TYR   E  246 ? 0.34231 0.34231 0.34231 0.00000  0.00000  0.00000  246 TYR   A C   
7545  O O   . TYR   E  246 ? 0.38107 0.38107 0.38107 0.00000  0.00000  0.00000  246 TYR   A O   
7546  C CB  . TYR   E  246 ? 0.19992 0.19992 0.19992 0.00000  0.00000  0.00000  246 TYR   A CB  
7547  C CG  . TYR   E  246 ? 0.40485 0.40485 0.40485 0.00000  0.00000  0.00000  246 TYR   A CG  
7548  C CD1 . TYR   E  246 ? 0.31752 0.31752 0.31752 0.00000  0.00000  0.00000  246 TYR   A CD1 
7549  C CD2 . TYR   E  246 ? 0.14159 0.14159 0.14159 0.00000  0.00000  0.00000  246 TYR   A CD2 
7550  C CE1 . TYR   E  246 ? 0.23821 0.23821 0.23821 -0.00000 0.00000  0.00000  246 TYR   A CE1 
7551  C CE2 . TYR   E  246 ? 0.47459 0.47459 0.47459 -0.00000 0.00000  0.00000  246 TYR   A CE2 
7552  C CZ  . TYR   E  246 ? 0.36085 0.36085 0.36085 0.00000  0.00000  0.00000  246 TYR   A CZ  
7553  O OH  . TYR   E  246 ? 0.56473 0.56473 0.56473 0.00000  0.00000  0.00000  246 TYR   A OH  
7554  N N   . ASN   E  247 ? 0.33283 0.33283 0.33283 -0.00000 0.00000  0.00000  247 ASN   A N   
7555  C CA  . ASN   E  247 ? 0.23637 0.23637 0.23637 0.00000  0.00000  0.00000  247 ASN   A CA  
7556  C C   . ASN   E  247 ? 0.32598 0.32598 0.32598 0.00000  -0.00000 0.00000  247 ASN   A C   
7557  O O   . ASN   E  247 ? 0.36695 0.36695 0.36695 -0.00000 0.00000  0.00000  247 ASN   A O   
7558  C CB  . ASN   E  247 ? 0.36604 0.36604 0.36604 -0.00000 0.00000  0.00000  247 ASN   A CB  
7559  C CG  . ASN   E  247 ? 0.33626 0.33626 0.33626 0.00000  -0.00000 0.00000  247 ASN   A CG  
7560  O OD1 . ASN   E  247 ? 0.55762 0.55762 0.55762 0.00000  0.00000  0.00000  247 ASN   A OD1 
7561  N ND2 . ASN   E  247 ? 0.31652 0.31652 0.31652 0.00000  0.00000  0.00000  247 ASN   A ND2 
7562  N N   . VAL   E  248 ? 0.32022 0.32022 0.32022 0.00000  -0.00000 0.00000  248 VAL   A N   
7563  C CA  . VAL   E  248 ? 0.39356 0.39356 0.39356 -0.00000 0.00000  0.00000  248 VAL   A CA  
7564  C C   . VAL   E  248 ? 0.28636 0.28636 0.28636 0.00000  0.00000  0.00000  248 VAL   A C   
7565  O O   . VAL   E  248 ? 0.38145 0.38145 0.38145 -0.00000 0.00000  0.00000  248 VAL   A O   
7566  C CB  . VAL   E  248 ? 0.33719 0.33719 0.33719 0.00000  0.00000  0.00000  248 VAL   A CB  
7567  C CG1 . VAL   E  248 ? 0.24595 0.24595 0.24595 0.00000  0.00000  0.00000  248 VAL   A CG1 
7568  C CG2 . VAL   E  248 ? 0.31308 0.31308 0.31308 0.00000  0.00000  0.00000  248 VAL   A CG2 
7569  N N   . SER   E  249 ? 0.51101 0.51101 0.51101 -0.00000 0.00000  0.00000  249 SER   A N   
7570  C CA  . SER   E  249 ? 0.35107 0.35107 0.35107 0.00000  0.00000  0.00000  249 SER   A CA  
7571  C C   . SER   E  249 ? 0.51039 0.51039 0.51039 0.00000  0.00000  0.00000  249 SER   A C   
7572  O O   . SER   E  249 ? 0.38123 0.38123 0.38123 0.00000  0.00000  0.00000  249 SER   A O   
7573  C CB  . SER   E  249 ? 0.34585 0.34585 0.34585 -0.00000 0.00000  0.00000  249 SER   A CB  
7574  O OG  . SER   E  249 ? 0.41796 0.41796 0.41796 -0.00000 -0.00000 0.00000  249 SER   A OG  
7575  N N   . TYR   E  250 ? 0.30754 0.30754 0.30754 -0.00000 0.00000  0.00000  250 TYR   A N   
7576  C CA  . TYR   E  250 ? 0.63870 0.63870 0.63870 -0.00000 0.00000  0.00000  250 TYR   A CA  
7577  C C   . TYR   E  250 ? 0.27462 0.27462 0.27462 0.00000  0.00000  0.00000  250 TYR   A C   
7578  O O   . TYR   E  250 ? 0.38998 0.38998 0.38998 0.00000  0.00000  0.00000  250 TYR   A O   
7579  C CB  . TYR   E  250 ? 0.26743 0.26743 0.26743 -0.00000 0.00000  0.00000  250 TYR   A CB  
7580  C CG  . TYR   E  250 ? 0.46419 0.46419 0.46419 0.00000  0.00000  0.00000  250 TYR   A CG  
7581  C CD1 . TYR   E  250 ? 0.29169 0.29169 0.29169 0.00000  0.00000  0.00000  250 TYR   A CD1 
7582  C CD2 . TYR   E  250 ? 0.24253 0.24253 0.24253 0.00000  0.00000  0.00000  250 TYR   A CD2 
7583  C CE1 . TYR   E  250 ? 0.44178 0.44178 0.44178 0.00000  0.00000  0.00000  250 TYR   A CE1 
7584  C CE2 . TYR   E  250 ? 0.38289 0.38289 0.38289 0.00000  0.00000  0.00000  250 TYR   A CE2 
7585  C CZ  . TYR   E  250 ? 0.53368 0.53368 0.53368 0.00000  -0.00000 0.00000  250 TYR   A CZ  
7586  O OH  . TYR   E  250 ? 0.60358 0.60358 0.60358 -0.00000 0.00000  0.00000  250 TYR   A OH  
7587  N N   . ASP   E  251 ? 0.37964 0.37964 0.37964 0.00000  0.00000  0.00000  251 ASP   A N   
7588  C CA  . ASP   E  251 ? 0.38291 0.38291 0.38291 0.00000  0.00000  0.00000  251 ASP   A CA  
7589  C C   . ASP   E  251 ? 0.61917 0.61917 0.61917 0.00000  0.00000  0.00000  251 ASP   A C   
7590  O O   . ASP   E  251 ? 0.42750 0.42750 0.42750 0.00000  0.00000  0.00000  251 ASP   A O   
7591  C CB  . ASP   E  251 ? 0.37444 0.37444 0.37444 0.00000  0.00000  0.00000  251 ASP   A CB  
7592  C CG  . ASP   E  251 ? 0.65573 0.65573 0.65573 0.00000  0.00000  0.00000  251 ASP   A CG  
7593  O OD1 . ASP   E  251 ? 0.48391 0.48391 0.48391 0.00000  0.00000  0.00000  251 ASP   A OD1 
7594  O OD2 . ASP   E  251 ? 0.47812 0.47812 0.47812 0.00000  0.00000  0.00000  251 ASP   A OD2 
7595  N N   . VAL   E  252 ? 0.37637 0.37637 0.37637 0.00000  0.00000  0.00000  252 VAL   A N   
7596  C CA  . VAL   E  252 ? 0.40536 0.40536 0.40536 -0.00000 0.00000  0.00000  252 VAL   A CA  
7597  C C   . VAL   E  252 ? 0.41759 0.41759 0.41759 -0.00000 0.00000  0.00000  252 VAL   A C   
7598  O O   . VAL   E  252 ? 0.43854 0.43854 0.43854 0.00000  0.00000  0.00000  252 VAL   A O   
7599  C CB  . VAL   E  252 ? 0.44142 0.44142 0.44142 0.00000  0.00000  0.00000  252 VAL   A CB  
7600  C CG1 . VAL   E  252 ? 0.28938 0.28938 0.28938 0.00000  0.00000  0.00000  252 VAL   A CG1 
7601  C CG2 . VAL   E  252 ? 0.29433 0.29433 0.29433 0.00000  0.00000  0.00000  252 VAL   A CG2 
7602  N N   . GLN   E  253 ? 0.35730 0.35730 0.35730 0.00000  0.00000  0.00000  253 GLN   A N   
7603  C CA  . GLN   E  253 ? 0.43034 0.43034 0.43034 0.00000  0.00000  0.00000  253 GLN   A CA  
7604  C C   . GLN   E  253 ? 0.58050 0.58050 0.58050 -0.00000 0.00000  0.00000  253 GLN   A C   
7605  O O   . GLN   E  253 ? 0.42130 0.42130 0.42130 -0.00000 0.00000  0.00000  253 GLN   A O   
7606  C CB  . GLN   E  253 ? 0.28634 0.28634 0.28634 -0.00000 0.00000  0.00000  253 GLN   A CB  
7607  C CG  . GLN   E  253 ? 0.76225 0.76225 0.76225 -0.00000 0.00000  0.00000  253 GLN   A CG  
7608  C CD  . GLN   E  253 ? 0.65160 0.65160 0.65160 -0.00000 0.00000  0.00000  253 GLN   A CD  
7609  O OE1 . GLN   E  253 ? 0.66276 0.66276 0.66276 0.00000  -0.00000 -0.00000 253 GLN   A OE1 
7610  N NE2 . GLN   E  253 ? 0.75432 0.75432 0.75432 0.00000  0.00000  0.00000  253 GLN   A NE2 
7611  N N   . SER   E  254 ? 0.52942 0.52942 0.52942 -0.00000 0.00000  0.00000  254 SER   A N   
7612  C CA  . SER   E  254 ? 0.27542 0.27542 0.27542 -0.00000 0.00000  0.00000  254 SER   A CA  
7613  C C   . SER   E  254 ? 0.30189 0.30189 0.30189 0.00000  0.00000  0.00000  254 SER   A C   
7614  O O   . SER   E  254 ? 0.45080 0.45080 0.45080 0.00000  0.00000  0.00000  254 SER   A O   
7615  C CB  . SER   E  254 ? 0.41179 0.41179 0.41179 -0.00000 0.00000  0.00000  254 SER   A CB  
7616  O OG  . SER   E  254 ? 0.30504 0.30504 0.30504 0.00000  0.00000  0.00000  254 SER   A OG  
7617  N N   . LEU   E  255 ? 0.38208 0.38208 0.38208 -0.00000 0.00000  0.00000  255 LEU   A N   
7618  C CA  . LEU   E  255 ? 0.41199 0.41199 0.41199 0.00000  0.00000  0.00000  255 LEU   A CA  
7619  C C   . LEU   E  255 ? 0.43148 0.43148 0.43148 0.00000  0.00000  0.00000  255 LEU   A C   
7620  O O   . LEU   E  255 ? 0.44729 0.44729 0.44729 0.00000  0.00000  0.00000  255 LEU   A O   
7621  C CB  . LEU   E  255 ? 0.44642 0.44642 0.44642 -0.00000 0.00000  0.00000  255 LEU   A CB  
7622  C CG  . LEU   E  255 ? 0.46253 0.46253 0.46253 -0.00000 0.00000  0.00000  255 LEU   A CG  
7623  C CD1 . LEU   E  255 ? 0.44716 0.44716 0.44716 -0.00000 0.00000  0.00000  255 LEU   A CD1 
7624  C CD2 . LEU   E  255 ? 0.31836 0.31836 0.31836 0.00000  0.00000  0.00000  255 LEU   A CD2 
7625  N N   . ASP   E  256 ? 0.50181 0.50181 0.50181 0.00000  0.00000  0.00000  256 ASP   A N   
7626  C CA  . ASP   E  256 ? 0.31656 0.31656 0.31656 0.00000  -0.00000 0.00000  256 ASP   A CA  
7627  C C   . ASP   E  256 ? 0.60198 0.60198 0.60198 0.00000  0.00000  0.00000  256 ASP   A C   
7628  O O   . ASP   E  256 ? 0.34871 0.34871 0.34871 0.00000  0.00000  0.00000  256 ASP   A O   
7629  C CB  . ASP   E  256 ? 0.44353 0.44353 0.44353 0.00000  0.00000  0.00000  256 ASP   A CB  
7630  C CG  . ASP   E  256 ? 0.78199 0.78199 0.78199 0.00000  0.00000  0.00000  256 ASP   A CG  
7631  O OD1 . ASP   E  256 ? 0.45029 0.45029 0.45029 -0.00000 0.00000  -0.00000 256 ASP   A OD1 
7632  O OD2 . ASP   E  256 ? 0.45891 0.45891 0.45891 -0.00000 0.00000  0.00000  256 ASP   A OD2 
7633  N N   . THR   E  257 ? 0.38736 0.38736 0.38736 0.00000  0.00000  0.00000  257 THR   A N   
7634  C CA  . THR   E  257 ? 0.74440 0.74440 0.74440 0.00000  0.00000  0.00000  257 THR   A CA  
7635  C C   . THR   E  257 ? 0.31527 0.31527 0.31527 0.00000  0.00000  0.00000  257 THR   A C   
7636  O O   . THR   E  257 ? 0.59363 0.59363 0.59363 0.00000  0.00000  0.00000  257 THR   A O   
7637  C CB  . THR   E  257 ? 0.40436 0.40436 0.40436 0.00000  0.00000  0.00000  257 THR   A CB  
7638  O OG1 . THR   E  257 ? 0.69202 0.69202 0.69202 0.00000  0.00000  0.00000  257 THR   A OG1 
7639  C CG2 . THR   E  257 ? 0.55110 0.55110 0.55110 -0.00000 0.00000  0.00000  257 THR   A CG2 
7640  N N   . LEU   E  258 ? 0.58077 0.58077 0.58077 -0.00000 0.00000  0.00000  258 LEU   A N   
7641  C CA  . LEU   E  258 ? 0.39644 0.39644 0.39644 0.00000  0.00000  0.00000  258 LEU   A CA  
7642  C C   . LEU   E  258 ? 0.74141 0.74141 0.74141 -0.00000 0.00000  0.00000  258 LEU   A C   
7643  O O   . LEU   E  258 ? 0.78331 0.78331 0.78331 0.00000  0.00000  0.00000  258 LEU   A O   
7644  C CB  . LEU   E  258 ? 0.39809 0.39809 0.39809 -0.00000 0.00000  0.00000  258 LEU   A CB  
7645  C CG  . LEU   E  258 ? 0.34563 0.34563 0.34563 -0.00000 0.00000  0.00000  258 LEU   A CG  
7646  C CD1 . LEU   E  258 ? 0.43669 0.43669 0.43669 0.00000  0.00000  0.00000  258 LEU   A CD1 
7647  C CD2 . LEU   E  258 ? 0.30020 0.30020 0.30020 -0.00000 0.00000  0.00000  258 LEU   A CD2 
7648  N N   . VAL   E  259 ? 0.68690 0.68690 0.68690 -0.00000 0.00000  0.00000  259 VAL   A N   
7649  C CA  . VAL   E  259 ? 0.72917 0.72917 0.72917 -0.00000 0.00000  0.00000  259 VAL   A CA  
7650  C C   . VAL   E  259 ? 1.54162 1.54162 1.54162 -0.00000 0.00000  0.00000  259 VAL   A C   
7651  O O   . VAL   E  259 ? 0.67414 0.67414 0.67414 0.00000  0.00000  0.00000  259 VAL   A O   
7652  C CB  . VAL   E  259 ? 0.97841 0.97841 0.97841 -0.00000 0.00000  0.00000  259 VAL   A CB  
7653  C CG1 . VAL   E  259 ? 0.49875 0.49875 0.49875 0.00000  -0.00000 0.00000  259 VAL   A CG1 
7654  C CG2 . VAL   E  259 ? 0.80749 0.80749 0.80749 0.00000  0.00000  0.00000  259 VAL   A CG2 
7655  N N   . PHE   E  260 ? 0.45819 0.45819 0.45819 -0.00000 0.00000  0.00000  260 PHE   A N   
7656  C CA  . PHE   E  260 ? 1.22485 1.22485 1.22485 0.00000  0.00000  0.00000  260 PHE   A CA  
7657  C C   . PHE   E  260 ? 0.68124 0.68124 0.68124 -0.00000 0.00000  0.00000  260 PHE   A C   
7658  O O   . PHE   E  260 ? 1.64807 1.64807 1.64807 0.00000  0.00000  0.00000  260 PHE   A O   
7659  C CB  . PHE   E  260 ? 0.62425 0.62425 0.62425 0.00000  0.00000  0.00000  260 PHE   A CB  
7660  C CG  . PHE   E  260 ? 0.84874 0.84874 0.84874 0.00000  0.00000  0.00000  260 PHE   A CG  
7661  C CD1 . PHE   E  260 ? 0.56438 0.56438 0.56438 0.00000  -0.00000 0.00000  260 PHE   A CD1 
7662  C CD2 . PHE   E  260 ? 0.76222 0.76222 0.76222 0.00000  0.00000  0.00000  260 PHE   A CD2 
7663  C CE1 . PHE   E  260 ? 1.81841 1.81841 1.81841 0.00000  0.00000  0.00000  260 PHE   A CE1 
7664  C CE2 . PHE   E  260 ? 0.78175 0.78175 0.78175 0.00000  0.00000  0.00000  260 PHE   A CE2 
7665  C CZ  . PHE   E  260 ? 0.99303 0.99303 0.99303 0.00000  0.00000  0.00000  260 PHE   A CZ  
7666  N N   . LYS   E  261 ? 0.34569 0.34569 0.34569 -0.00000 0.00000  0.00000  261 LYS   A N   
7667  C CA  . LYS   E  261 ? 0.97640 0.97640 0.97640 0.00000  -0.00000 0.00000  261 LYS   A CA  
7668  C C   . LYS   E  261 ? 1.64423 1.64423 1.64423 0.00000  0.00000  0.00000  261 LYS   A C   
7669  O O   . LYS   E  261 ? 1.75351 1.75351 1.75351 0.00000  0.00000  0.00000  261 LYS   A O   
7670  C CB  . LYS   E  261 ? 1.52120 1.52120 1.52120 0.00000  0.00000  0.00000  261 LYS   A CB  
7671  C CG  . LYS   E  261 ? 1.19783 1.19783 1.19783 -0.00000 -0.00000 0.00000  261 LYS   A CG  
7672  C CD  . LYS   E  261 ? 1.17789 1.17789 1.17789 0.00000  0.00000  0.00000  261 LYS   A CD  
7673  C CE  . LYS   E  261 ? 0.73586 0.73586 0.73586 -0.00000 0.00000  0.00000  261 LYS   A CE  
7674  N NZ  . LYS   E  261 ? 0.33452 0.33452 0.33452 0.00000  0.00000  0.00000  261 LYS   A NZ  
7675  N N   . GLY   E  262 ? 1.08023 1.08023 1.08023 0.00000  0.00000  0.00000  262 GLY   A N   
7676  C CA  . GLY   E  262 ? 0.37850 0.37850 0.37850 0.00000  0.00000  0.00000  262 GLY   A CA  
7677  C C   . GLY   E  262 ? 1.09867 1.09867 1.09867 0.00000  0.00000  0.00000  262 GLY   A C   
7678  O O   . GLY   E  262 ? 1.01411 1.01411 1.01411 -0.00000 0.00000  0.00000  262 GLY   A O   
7679  N N   . GLU   E  263 ? 0.54125 0.54125 0.54125 0.00000  0.00000  0.00000  263 GLU   A N   
7680  C CA  . GLU   E  263 ? 0.97696 0.97696 0.97696 0.00000  -0.00000 0.00000  263 GLU   A CA  
7681  C C   . GLU   E  263 ? 1.10495 1.10495 1.10495 0.00000  0.00000  0.00000  263 GLU   A C   
7682  O O   . GLU   E  263 ? 0.65953 0.65953 0.65953 0.00000  0.00000  0.00000  263 GLU   A O   
7683  C CB  . GLU   E  263 ? 0.52126 0.52126 0.52126 0.00000  0.00000  0.00000  263 GLU   A CB  
7684  C CG  . GLU   E  263 ? 0.97254 0.97254 0.97254 -0.00000 0.00000  0.00000  263 GLU   A CG  
7685  C CD  . GLU   E  263 ? 0.88704 0.88704 0.88704 0.00000  0.00000  0.00000  263 GLU   A CD  
7686  O OE1 . GLU   E  263 ? 0.51147 0.51147 0.51147 0.00000  0.00000  0.00000  263 GLU   A OE1 
7687  O OE2 . GLU   E  263 ? 0.68668 0.68668 0.68668 0.00000  0.00000  0.00000  263 GLU   A OE2 
7688  N N   . THR   E  264 ? 0.56200 0.56200 0.56200 -0.00000 0.00000  0.00000  264 THR   A N   
7689  C CA  . THR   E  264 ? 0.37872 0.37872 0.37872 0.00000  0.00000  0.00000  264 THR   A CA  
7690  C C   . THR   E  264 ? 0.57185 0.57185 0.57185 0.00000  0.00000  0.00000  264 THR   A C   
7691  O O   . THR   E  264 ? 0.45888 0.45888 0.45888 -0.00000 0.00000  0.00000  264 THR   A O   
7692  C CB  . THR   E  264 ? 0.64274 0.64274 0.64274 0.00000  0.00000  0.00000  264 THR   A CB  
7693  O OG1 . THR   E  264 ? 1.28956 1.28956 1.28956 -0.00000 0.00000  0.00000  264 THR   A OG1 
7694  C CG2 . THR   E  264 ? 0.47794 0.47794 0.47794 -0.00000 0.00000  0.00000  264 THR   A CG2 
7695  N N   . TYR   E  265 ? 0.42939 0.42939 0.42939 0.00000  0.00000  0.00000  265 TYR   A N   
7696  C CA  . TYR   E  265 ? 0.30925 0.30925 0.30925 0.00000  0.00000  0.00000  265 TYR   A CA  
7697  C C   . TYR   E  265 ? 0.37053 0.37053 0.37053 -0.00000 0.00000  0.00000  265 TYR   A C   
7698  O O   . TYR   E  265 ? 0.47210 0.47210 0.47210 -0.00000 0.00000  0.00000  265 TYR   A O   
7699  C CB  . TYR   E  265 ? 0.25953 0.25953 0.25953 -0.00000 0.00000  0.00000  265 TYR   A CB  
7700  C CG  . TYR   E  265 ? 0.49837 0.49837 0.49837 -0.00000 0.00000  0.00000  265 TYR   A CG  
7701  C CD1 . TYR   E  265 ? 0.38882 0.38882 0.38882 -0.00000 0.00000  0.00000  265 TYR   A CD1 
7702  C CD2 . TYR   E  265 ? 0.35795 0.35795 0.35795 -0.00000 0.00000  0.00000  265 TYR   A CD2 
7703  C CE1 . TYR   E  265 ? 0.48901 0.48901 0.48901 0.00000  0.00000  0.00000  265 TYR   A CE1 
7704  C CE2 . TYR   E  265 ? 0.46665 0.46665 0.46665 -0.00000 0.00000  0.00000  265 TYR   A CE2 
7705  C CZ  . TYR   E  265 ? 0.38953 0.38953 0.38953 0.00000  0.00000  0.00000  265 TYR   A CZ  
7706  O OH  . TYR   E  265 ? 0.43172 0.43172 0.43172 0.00000  0.00000  0.00000  265 TYR   A OH  
7707  N N   . SER   E  266 ? 0.36245 0.36245 0.36245 0.00000  0.00000  0.00000  266 SER   A N   
7708  C CA  . SER   E  266 ? 0.22387 0.22387 0.22387 -0.00000 0.00000  0.00000  266 SER   A CA  
7709  C C   . SER   E  266 ? 0.39496 0.39496 0.39496 0.00000  0.00000  0.00000  266 SER   A C   
7710  O O   . SER   E  266 ? 0.27516 0.27516 0.27516 0.00000  0.00000  0.00000  266 SER   A O   
7711  C CB  . SER   E  266 ? 0.24618 0.24618 0.24618 -0.00000 0.00000  0.00000  266 SER   A CB  
7712  O OG  . SER   E  266 ? 0.37980 0.37980 0.37980 0.00000  0.00000  0.00000  266 SER   A OG  
7713  N N   . LEU   E  267 ? 0.30750 0.30750 0.30750 0.00000  -0.00000 0.00000  267 LEU   A N   
7714  C CA  . LEU   E  267 ? 0.42890 0.42890 0.42890 -0.00000 0.00000  0.00000  267 LEU   A CA  
7715  C C   . LEU   E  267 ? 0.29945 0.29945 0.29945 0.00000  0.00000  0.00000  267 LEU   A C   
7716  O O   . LEU   E  267 ? 0.49698 0.49698 0.49698 0.00000  0.00000  0.00000  267 LEU   A O   
7717  C CB  . LEU   E  267 ? 0.21939 0.21939 0.21939 -0.00000 0.00000  0.00000  267 LEU   A CB  
7718  C CG  . LEU   E  267 ? 0.46763 0.46763 0.46763 0.00000  0.00000  0.00000  267 LEU   A CG  
7719  C CD1 . LEU   E  267 ? 0.36728 0.36728 0.36728 -0.00000 0.00000  0.00000  267 LEU   A CD1 
7720  C CD2 . LEU   E  267 ? 0.29491 0.29491 0.29491 -0.00000 0.00000  0.00000  267 LEU   A CD2 
7721  N N   . LYS   E  268 ? 0.54135 0.54135 0.54135 -0.00000 0.00000  0.00000  268 LYS   A N   
7722  C CA  . LYS   E  268 ? 0.27355 0.27355 0.27355 0.00000  0.00000  0.00000  268 LYS   A CA  
7723  C C   . LYS   E  268 ? 0.51334 0.51334 0.51334 0.00000  0.00000  0.00000  268 LYS   A C   
7724  O O   . LYS   E  268 ? 0.24890 0.24890 0.24890 0.00000  0.00000  0.00000  268 LYS   A O   
7725  C CB  . LYS   E  268 ? 0.35470 0.35470 0.35470 0.00000  0.00000  0.00000  268 LYS   A CB  
7726  C CG  . LYS   E  268 ? 0.51827 0.51827 0.51827 0.00000  0.00000  0.00000  268 LYS   A CG  
7727  C CD  . LYS   E  268 ? 0.43722 0.43722 0.43722 0.00000  0.00000  0.00000  268 LYS   A CD  
7728  C CE  . LYS   E  268 ? 0.59659 0.59659 0.59659 -0.00000 0.00000  0.00000  268 LYS   A CE  
7729  N NZ  . LYS   E  268 ? 0.55584 0.55584 0.55584 -0.00000 0.00000  0.00000  268 LYS   A NZ  
7730  N N   . HIS   E  269 ? 0.38553 0.38553 0.38553 -0.00000 0.00000  0.00000  269 HIS   A N   
7731  C CA  . HIS   E  269 ? 0.18925 0.18925 0.18925 0.00000  0.00000  0.00000  269 HIS   A CA  
7732  C C   . HIS   E  269 ? 0.50500 0.50500 0.50500 -0.00000 0.00000  0.00000  269 HIS   A C   
7733  O O   . HIS   E  269 ? 0.28636 0.28636 0.28636 0.00000  0.00000  0.00000  269 HIS   A O   
7734  C CB  . HIS   E  269 ? 0.28629 0.28629 0.28629 0.00000  0.00000  0.00000  269 HIS   A CB  
7735  C CG  . HIS   E  269 ? 0.33755 0.33755 0.33755 0.00000  -0.00000 -0.00000 269 HIS   A CG  
7736  N ND1 . HIS   E  269 ? 0.60813 0.60813 0.60813 0.00000  0.00000  0.00000  269 HIS   A ND1 
7737  C CD2 . HIS   E  269 ? 0.42969 0.42969 0.42969 0.00000  0.00000  0.00000  269 HIS   A CD2 
7738  C CE1 . HIS   E  269 ? 0.29431 0.29431 0.29431 -0.00000 0.00000  0.00000  269 HIS   A CE1 
7739  N NE2 . HIS   E  269 ? 0.49121 0.49121 0.49121 -0.00000 0.00000  0.00000  269 HIS   A NE2 
7740  N N   . LEU   E  270 ? 0.32349 0.32349 0.32349 0.00000  0.00000  0.00000  270 LEU   A N   
7741  C CA  . LEU   E  270 ? 0.26340 0.26340 0.26340 -0.00000 0.00000  0.00000  270 LEU   A CA  
7742  C C   . LEU   E  270 ? 0.31010 0.31010 0.31010 0.00000  0.00000  0.00000  270 LEU   A C   
7743  O O   . LEU   E  270 ? 0.35514 0.35514 0.35514 -0.00000 0.00000  0.00000  270 LEU   A O   
7744  C CB  . LEU   E  270 ? 0.34852 0.34852 0.34852 0.00000  0.00000  0.00000  270 LEU   A CB  
7745  C CG  . LEU   E  270 ? 0.31132 0.31132 0.31132 0.00000  0.00000  0.00000  270 LEU   A CG  
7746  C CD1 . LEU   E  270 ? 0.28263 0.28263 0.28263 -0.00000 -0.00000 0.00000  270 LEU   A CD1 
7747  C CD2 . LEU   E  270 ? 0.38389 0.38389 0.38389 -0.00000 0.00000  0.00000  270 LEU   A CD2 
7748  N N   . LEU   E  271 ? 0.40121 0.40121 0.40121 0.00000  0.00000  0.00000  271 LEU   A N   
7749  C CA  . LEU   E  271 ? 0.35849 0.35849 0.35849 0.00000  -0.00000 0.00000  271 LEU   A CA  
7750  C C   . LEU   E  271 ? 0.46529 0.46529 0.46529 -0.00000 0.00000  0.00000  271 LEU   A C   
7751  O O   . LEU   E  271 ? 0.33310 0.33310 0.33310 0.00000  0.00000  0.00000  271 LEU   A O   
7752  C CB  . LEU   E  271 ? 0.23770 0.23770 0.23770 -0.00000 0.00000  0.00000  271 LEU   A CB  
7753  C CG  . LEU   E  271 ? 0.40348 0.40348 0.40348 -0.00000 0.00000  0.00000  271 LEU   A CG  
7754  C CD1 . LEU   E  271 ? 0.29097 0.29097 0.29097 0.00000  0.00000  0.00000  271 LEU   A CD1 
7755  C CD2 . LEU   E  271 ? 0.20898 0.20898 0.20898 -0.00000 0.00000  0.00000  271 LEU   A CD2 
7756  N N   . ASN   E  272 ? 0.32064 0.32064 0.32064 0.00000  0.00000  0.00000  272 ASN   A N   
7757  C CA  . ASN   E  272 ? 0.21933 0.21933 0.21933 0.00000  0.00000  0.00000  272 ASN   A CA  
7758  C C   . ASN   E  272 ? 0.37304 0.37304 0.37304 0.00000  0.00000  0.00000  272 ASN   A C   
7759  O O   . ASN   E  272 ? 0.45909 0.45909 0.45909 0.00000  0.00000  0.00000  272 ASN   A O   
7760  C CB  . ASN   E  272 ? 0.49682 0.49682 0.49682 -0.00000 0.00000  0.00000  272 ASN   A CB  
7761  C CG  . ASN   E  272 ? 0.37639 0.37639 0.37639 0.00000  0.00000  0.00000  272 ASN   A CG  
7762  O OD1 . ASN   E  272 ? 0.37391 0.37391 0.37391 0.00000  0.00000  0.00000  272 ASN   A OD1 
7763  N ND2 . ASN   E  272 ? 0.45532 0.45532 0.45532 0.00000  -0.00000 0.00000  272 ASN   A ND2 
7764  N N   . ASN   E  273 ? 0.30262 0.30262 0.30262 0.00000  -0.00000 0.00000  273 ASN   A N   
7765  C CA  . ASN   E  273 ? 0.41796 0.41796 0.41796 0.00000  0.00000  0.00000  273 ASN   A CA  
7766  C C   . ASN   E  273 ? 0.26609 0.26609 0.26609 0.00000  0.00000  0.00000  273 ASN   A C   
7767  O O   . ASN   E  273 ? 0.37749 0.37749 0.37749 0.00000  0.00000  0.00000  273 ASN   A O   
7768  C CB  . ASN   E  273 ? 0.34816 0.34816 0.34816 0.00000  0.00000  0.00000  273 ASN   A CB  
7769  C CG  . ASN   E  273 ? 0.81048 0.81048 0.81048 0.00000  0.00000  0.00000  273 ASN   A CG  
7770  O OD1 . ASN   E  273 ? 0.87934 0.87934 0.87934 0.00000  0.00000  0.00000  273 ASN   A OD1 
7771  N ND2 . ASN   E  273 ? 0.84419 0.84419 0.84419 0.00000  0.00000  0.00000  273 ASN   A ND2 
7772  N N   . ASP   E  274 ? 0.35961 0.35961 0.35961 0.00000  0.00000  0.00000  274 ASP   A N   
7773  C CA  . ASP   E  274 ? 0.32438 0.32438 0.32438 0.00000  0.00000  0.00000  274 ASP   A CA  
7774  C C   . ASP   E  274 ? 0.25343 0.25343 0.25343 -0.00000 0.00000  0.00000  274 ASP   A C   
7775  O O   . ASP   E  274 ? 0.26393 0.26393 0.26393 0.00000  0.00000  0.00000  274 ASP   A O   
7776  C CB  . ASP   E  274 ? 0.28120 0.28120 0.28120 -0.00000 0.00000  0.00000  274 ASP   A CB  
7777  C CG  . ASP   E  274 ? 0.40318 0.40318 0.40318 0.00000  0.00000  0.00000  274 ASP   A CG  
7778  O OD1 . ASP   E  274 ? 0.51044 0.51044 0.51044 0.00000  0.00000  0.00000  274 ASP   A OD1 
7779  O OD2 . ASP   E  274 ? 0.68425 0.68425 0.68425 -0.00000 -0.00000 0.00000  274 ASP   A OD2 
7780  N N   . PRO   E  275 ? 0.38156 0.38156 0.38156 -0.00000 0.00000  0.00000  275 PRO   A N   
7781  C CA  . PRO   E  275 ? 0.12791 0.12791 0.12791 0.00000  0.00000  0.00000  275 PRO   A CA  
7782  C C   . PRO   E  275 ? 0.24952 0.24952 0.24952 0.00000  0.00000  0.00000  275 PRO   A C   
7783  O O   . PRO   E  275 ? 0.41816 0.41816 0.41816 0.00000  0.00000  0.00000  275 PRO   A O   
7784  C CB  . PRO   E  275 ? 0.15610 0.15610 0.15610 0.00000  0.00000  0.00000  275 PRO   A CB  
7785  C CG  . PRO   E  275 ? 0.18202 0.18202 0.18202 0.00000  0.00000  0.00000  275 PRO   A CG  
7786  C CD  . PRO   E  275 ? 0.23188 0.23188 0.23188 0.00000  0.00000  -0.00000 275 PRO   A CD  
7787  N N   . PHE   E  276 ? 0.31099 0.31099 0.31099 0.00000  0.00000  0.00000  276 PHE   A N   
7788  C CA  . PHE   E  276 ? 0.18855 0.18855 0.18855 -0.00000 0.00000  0.00000  276 PHE   A CA  
7789  C C   . PHE   E  276 ? 0.40501 0.40501 0.40501 0.00000  0.00000  0.00000  276 PHE   A C   
7790  O O   . PHE   E  276 ? 0.35255 0.35255 0.35255 0.00000  0.00000  0.00000  276 PHE   A O   
7791  C CB  . PHE   E  276 ? 0.20423 0.20423 0.20423 0.00000  0.00000  0.00000  276 PHE   A CB  
7792  C CG  . PHE   E  276 ? 0.40070 0.40070 0.40070 -0.00000 0.00000  0.00000  276 PHE   A CG  
7793  C CD1 . PHE   E  276 ? 0.31213 0.31213 0.31213 -0.00000 0.00000  0.00000  276 PHE   A CD1 
7794  C CD2 . PHE   E  276 ? 0.27497 0.27497 0.27497 0.00000  0.00000  0.00000  276 PHE   A CD2 
7795  C CE1 . PHE   E  276 ? 0.46132 0.46132 0.46132 0.00000  0.00000  0.00000  276 PHE   A CE1 
7796  C CE2 . PHE   E  276 ? 0.50961 0.50961 0.50961 -0.00000 0.00000  0.00000  276 PHE   A CE2 
7797  C CZ  . PHE   E  276 ? 0.38923 0.38923 0.38923 0.00000  0.00000  0.00000  276 PHE   A CZ  
7798  N N   . THR   E  277 ? 0.36654 0.36654 0.36654 0.00000  0.00000  0.00000  277 THR   A N   
7799  C CA  . THR   E  277 ? 0.43903 0.43903 0.43903 -0.00000 0.00000  0.00000  277 THR   A CA  
7800  C C   . THR   E  277 ? 0.33235 0.33235 0.33235 0.00000  0.00000  0.00000  277 THR   A C   
7801  O O   . THR   E  277 ? 0.40912 0.40912 0.40912 -0.00000 0.00000  0.00000  277 THR   A O   
7802  C CB  . THR   E  277 ? 0.29647 0.29647 0.29647 -0.00000 0.00000  0.00000  277 THR   A CB  
7803  O OG1 . THR   E  277 ? 0.37546 0.37546 0.37546 -0.00000 0.00000  0.00000  277 THR   A OG1 
7804  C CG2 . THR   E  277 ? 0.16976 0.16976 0.16976 -0.00000 0.00000  0.00000  277 THR   A CG2 
7805  N N   . PRO   E  278 ? 0.65071 0.65071 0.65071 0.00000  0.00000  0.00000  278 PRO   A N   
7806  C CA  . PRO   E  278 ? 0.30485 0.30485 0.30485 -0.00000 0.00000  0.00000  278 PRO   A CA  
7807  C C   . PRO   E  278 ? 0.48225 0.48225 0.48225 0.00000  0.00000  0.00000  278 PRO   A C   
7808  O O   . PRO   E  278 ? 0.33739 0.33739 0.33739 0.00000  0.00000  0.00000  278 PRO   A O   
7809  C CB  . PRO   E  278 ? 0.21284 0.21284 0.21284 0.00000  0.00000  0.00000  278 PRO   A CB  
7810  C CG  . PRO   E  278 ? 0.26065 0.26065 0.26065 0.00000  0.00000  0.00000  278 PRO   A CG  
7811  C CD  . PRO   E  278 ? 0.29751 0.29751 0.29751 0.00000  0.00000  0.00000  278 PRO   A CD  
7812  N N   . GLN   E  279 ? 0.39532 0.39532 0.39532 -0.00000 -0.00000 0.00000  279 GLN   A N   
7813  C CA  . GLN   E  279 ? 0.36763 0.36763 0.36763 0.00000  0.00000  0.00000  279 GLN   A CA  
7814  C C   . GLN   E  279 ? 0.53737 0.53737 0.53737 -0.00000 -0.00000 0.00000  279 GLN   A C   
7815  O O   . GLN   E  279 ? 0.51700 0.51700 0.51700 -0.00000 0.00000  0.00000  279 GLN   A O   
7816  C CB  . GLN   E  279 ? 0.33518 0.33518 0.33518 -0.00000 -0.00000 -0.00000 279 GLN   A CB  
7817  C CG  . GLN   E  279 ? 0.22756 0.22756 0.22756 0.00000  0.00000  0.00000  279 GLN   A CG  
7818  C CD  . GLN   E  279 ? 0.72816 0.72816 0.72816 -0.00000 0.00000  0.00000  279 GLN   A CD  
7819  O OE1 . GLN   E  279 ? 0.54871 0.54871 0.54871 -0.00000 0.00000  0.00000  279 GLN   A OE1 
7820  N NE2 . GLN   E  279 ? 0.43503 0.43503 0.43503 0.00000  0.00000  0.00000  279 GLN   A NE2 
7821  N N   . PHE   E  280 ? 0.40923 0.40923 0.40923 -0.00000 0.00000  0.00000  280 PHE   A N   
7822  C CA  . PHE   E  280 ? 0.42921 0.42921 0.42921 -0.00000 0.00000  0.00000  280 PHE   A CA  
7823  C C   . PHE   E  280 ? 0.40796 0.40796 0.40796 0.00000  0.00000  0.00000  280 PHE   A C   
7824  O O   . PHE   E  280 ? 0.44182 0.44182 0.44182 -0.00000 0.00000  0.00000  280 PHE   A O   
7825  C CB  . PHE   E  280 ? 0.20015 0.20015 0.20015 -0.00000 0.00000  0.00000  280 PHE   A CB  
7826  C CG  . PHE   E  280 ? 0.57916 0.57916 0.57916 0.00000  0.00000  0.00000  280 PHE   A CG  
7827  C CD1 . PHE   E  280 ? 0.33472 0.33472 0.33472 0.00000  -0.00000 0.00000  280 PHE   A CD1 
7828  C CD2 . PHE   E  280 ? 0.21218 0.21218 0.21218 0.00000  0.00000  0.00000  280 PHE   A CD2 
7829  C CE1 . PHE   E  280 ? 0.52112 0.52112 0.52112 0.00000  0.00000  0.00000  280 PHE   A CE1 
7830  C CE2 . PHE   E  280 ? 0.51240 0.51240 0.51240 -0.00000 0.00000  0.00000  280 PHE   A CE2 
7831  C CZ  . PHE   E  280 ? 0.41582 0.41582 0.41582 0.00000  0.00000  0.00000  280 PHE   A CZ  
7832  N N   . GLU   E  281 ? 0.35597 0.35597 0.35597 0.00000  0.00000  0.00000  281 GLU   A N   
7833  C CA  . GLU   E  281 ? 0.51864 0.51864 0.51864 -0.00000 0.00000  0.00000  281 GLU   A CA  
7834  C C   . GLU   E  281 ? 0.23048 0.23048 0.23048 -0.00000 0.00000  0.00000  281 GLU   A C   
7835  O O   . GLU   E  281 ? 0.47995 0.47995 0.47995 0.00000  -0.00000 0.00000  281 GLU   A O   
7836  C CB  . GLU   E  281 ? 0.27187 0.27187 0.27187 0.00000  0.00000  0.00000  281 GLU   A CB  
7837  C CG  . GLU   E  281 ? 0.67687 0.67687 0.67687 0.00000  0.00000  0.00000  281 GLU   A CG  
7838  C CD  . GLU   E  281 ? 1.54072 1.54072 1.54072 0.00000  0.00000  0.00000  281 GLU   A CD  
7839  O OE1 . GLU   E  281 ? 0.51667 0.51667 0.51667 0.00000  0.00000  0.00000  281 GLU   A OE1 
7840  O OE2 . GLU   E  281 ? 0.71899 0.71899 0.71899 0.00000  0.00000  0.00000  281 GLU   A OE2 
7841  N N   . HIS   E  282 ? 0.35802 0.35802 0.35802 0.00000  0.00000  0.00000  282 HIS   A N   
7842  C CA  . HIS   E  282 ? 0.65673 0.65673 0.65673 -0.00000 0.00000  0.00000  282 HIS   A CA  
7843  C C   . HIS   E  282 ? 0.49945 0.49945 0.49945 0.00000  0.00000  0.00000  282 HIS   A C   
7844  O O   . HIS   E  282 ? 0.56564 0.56564 0.56564 0.00000  0.00000  0.00000  282 HIS   A O   
7845  C CB  . HIS   E  282 ? 0.24521 0.24521 0.24521 0.00000  0.00000  0.00000  282 HIS   A CB  
7846  C CG  . HIS   E  282 ? 0.83717 0.83717 0.83717 -0.00000 0.00000  0.00000  282 HIS   A CG  
7847  N ND1 . HIS   E  282 ? 0.64352 0.64352 0.64352 -0.00000 0.00000  0.00000  282 HIS   A ND1 
7848  C CD2 . HIS   E  282 ? 0.33396 0.33396 0.33396 0.00000  0.00000  0.00000  282 HIS   A CD2 
7849  C CE1 . HIS   E  282 ? 0.43960 0.43960 0.43960 0.00000  0.00000  0.00000  282 HIS   A CE1 
7850  N NE2 . HIS   E  282 ? 0.59106 0.59106 0.59106 0.00000  0.00000  0.00000  282 HIS   A NE2 
7851  N N   . GLY   E  283 ? 0.56364 0.56364 0.56364 -0.00000 -0.00000 0.00000  283 GLY   A N   
7852  C CA  . GLY   E  283 ? 0.30474 0.30474 0.30474 0.00000  0.00000  0.00000  283 GLY   A CA  
7853  C C   . GLY   E  283 ? 0.45894 0.45894 0.45894 0.00000  0.00000  0.00000  283 GLY   A C   
7854  O O   . GLY   E  283 ? 0.44681 0.44681 0.44681 0.00000  0.00000  0.00000  283 GLY   A O   
7855  N N   . SER   E  284 ? 0.31110 0.31110 0.31110 -0.00000 0.00000  0.00000  284 SER   A N   
7856  C CA  . SER   E  284 ? 0.42136 0.42136 0.42136 0.00000  0.00000  0.00000  284 SER   A CA  
7857  C C   . SER   E  284 ? 0.34546 0.34546 0.34546 0.00000  0.00000  0.00000  284 SER   A C   
7858  O O   . SER   E  284 ? 0.25599 0.25599 0.25599 0.00000  0.00000  0.00000  284 SER   A O   
7859  C CB  . SER   E  284 ? 0.20663 0.20663 0.20663 -0.00000 0.00000  0.00000  284 SER   A CB  
7860  O OG  . SER   E  284 ? 0.44373 0.44373 0.44373 0.00000  0.00000  0.00000  284 SER   A OG  
7861  N N   . ILE   E  285 ? 0.26580 0.26580 0.26580 0.00000  0.00000  0.00000  285 ILE   A N   
7862  C CA  . ILE   E  285 ? 0.24987 0.24987 0.24987 -0.00000 0.00000  0.00000  285 ILE   A CA  
7863  C C   . ILE   E  285 ? 0.20121 0.20121 0.20121 -0.00000 0.00000  0.00000  285 ILE   A C   
7864  O O   . ILE   E  285 ? 0.44178 0.44178 0.44178 0.00000  0.00000  0.00000  285 ILE   A O   
7865  C CB  . ILE   E  285 ? 0.29299 0.29299 0.29299 -0.00000 -0.00000 0.00000  285 ILE   A CB  
7866  C CG1 . ILE   E  285 ? 0.24853 0.24853 0.24853 0.00000  0.00000  0.00000  285 ILE   A CG1 
7867  C CG2 . ILE   E  285 ? 0.19714 0.19714 0.19714 0.00000  0.00000  0.00000  285 ILE   A CG2 
7868  C CD1 . ILE   E  285 ? 0.35352 0.35352 0.35352 -0.00000 0.00000  0.00000  285 ILE   A CD1 
7869  N N   . LEU   E  286 ? 0.41316 0.41316 0.41316 0.00000  -0.00000 0.00000  286 LEU   A N   
7870  C CA  . LEU   E  286 ? 0.19620 0.19620 0.19620 0.00000  0.00000  0.00000  286 LEU   A CA  
7871  C C   . LEU   E  286 ? 0.28359 0.28359 0.28359 0.00000  0.00000  0.00000  286 LEU   A C   
7872  O O   . LEU   E  286 ? 0.34330 0.34330 0.34330 -0.00000 0.00000  0.00000  286 LEU   A O   
7873  C CB  . LEU   E  286 ? 0.38853 0.38853 0.38853 0.00000  0.00000  0.00000  286 LEU   A CB  
7874  C CG  . LEU   E  286 ? 0.33360 0.33360 0.33360 0.00000  0.00000  0.00000  286 LEU   A CG  
7875  C CD1 . LEU   E  286 ? 0.26977 0.26977 0.26977 -0.00000 0.00000  0.00000  286 LEU   A CD1 
7876  C CD2 . LEU   E  286 ? 0.33610 0.33610 0.33610 0.00000  0.00000  0.00000  286 LEU   A CD2 
7877  N N   . GLN   E  287 ? 0.22943 0.22943 0.22943 0.00000  0.00000  0.00000  287 GLN   A N   
7878  C CA  . GLN   E  287 ? 0.40753 0.40753 0.40753 -0.00000 0.00000  0.00000  287 GLN   A CA  
7879  C C   . GLN   E  287 ? 0.41615 0.41615 0.41615 0.00000  0.00000  0.00000  287 GLN   A C   
7880  O O   . GLN   E  287 ? 0.33468 0.33468 0.33468 -0.00000 0.00000  0.00000  287 GLN   A O   
7881  C CB  . GLN   E  287 ? 0.26877 0.26877 0.26877 0.00000  0.00000  0.00000  287 GLN   A CB  
7882  C CG  . GLN   E  287 ? 0.36895 0.36895 0.36895 0.00000  0.00000  0.00000  287 GLN   A CG  
7883  C CD  . GLN   E  287 ? 0.33425 0.33425 0.33425 0.00000  0.00000  0.00000  287 GLN   A CD  
7884  O OE1 . GLN   E  287 ? 0.36133 0.36133 0.36133 0.00000  0.00000  0.00000  287 GLN   A OE1 
7885  N NE2 . GLN   E  287 ? 0.28505 0.28505 0.28505 0.00000  0.00000  0.00000  287 GLN   A NE2 
7886  N N   . GLY   E  288 ? 0.33158 0.33158 0.33158 -0.00000 0.00000  0.00000  288 GLY   A N   
7887  C CA  . GLY   E  288 ? 0.22810 0.22810 0.22810 0.00000  0.00000  0.00000  288 GLY   A CA  
7888  C C   . GLY   E  288 ? 0.28658 0.28658 0.28658 -0.00000 0.00000  0.00000  288 GLY   A C   
7889  O O   . GLY   E  288 ? 0.47703 0.47703 0.47703 -0.00000 0.00000  0.00000  288 GLY   A O   
7890  N N   . PHE   E  289 ? 0.28731 0.28731 0.28731 0.00000  0.00000  0.00000  289 PHE   A N   
7891  C CA  . PHE   E  289 ? 0.37030 0.37030 0.37030 0.00000  0.00000  0.00000  289 PHE   A CA  
7892  C C   . PHE   E  289 ? 0.31078 0.31078 0.31078 0.00000  0.00000  0.00000  289 PHE   A C   
7893  O O   . PHE   E  289 ? 0.34108 0.34108 0.34108 0.00000  0.00000  0.00000  289 PHE   A O   
7894  C CB  . PHE   E  289 ? 0.23150 0.23150 0.23150 0.00000  0.00000  0.00000  289 PHE   A CB  
7895  C CG  . PHE   E  289 ? 0.30348 0.30348 0.30348 -0.00000 0.00000  0.00000  289 PHE   A CG  
7896  C CD1 . PHE   E  289 ? 0.16147 0.16147 0.16147 0.00000  -0.00000 0.00000  289 PHE   A CD1 
7897  C CD2 . PHE   E  289 ? 0.29640 0.29640 0.29640 -0.00000 0.00000  0.00000  289 PHE   A CD2 
7898  C CE1 . PHE   E  289 ? 0.39758 0.39758 0.39758 0.00000  0.00000  0.00000  289 PHE   A CE1 
7899  C CE2 . PHE   E  289 ? 0.33889 0.33889 0.33889 -0.00000 -0.00000 0.00000  289 PHE   A CE2 
7900  C CZ  . PHE   E  289 ? 0.31736 0.31736 0.31736 -0.00000 0.00000  0.00000  289 PHE   A CZ  
7901  N N   . LEU   E  290 ? 0.29076 0.29076 0.29076 0.00000  0.00000  0.00000  290 LEU   A N   
7902  C CA  . LEU   E  290 ? 0.28279 0.28279 0.28279 -0.00000 0.00000  0.00000  290 LEU   A CA  
7903  C C   . LEU   E  290 ? 0.33811 0.33811 0.33811 -0.00000 0.00000  0.00000  290 LEU   A C   
7904  O O   . LEU   E  290 ? 0.58667 0.58667 0.58667 0.00000  0.00000  0.00000  290 LEU   A O   
7905  C CB  . LEU   E  290 ? 0.19587 0.19587 0.19587 0.00000  0.00000  0.00000  290 LEU   A CB  
7906  C CG  . LEU   E  290 ? 0.29407 0.29407 0.29407 0.00000  0.00000  0.00000  290 LEU   A CG  
7907  C CD1 . LEU   E  290 ? 0.26428 0.26428 0.26428 0.00000  0.00000  0.00000  290 LEU   A CD1 
7908  C CD2 . LEU   E  290 ? 0.19364 0.19364 0.19364 0.00000  0.00000  0.00000  290 LEU   A CD2 
7909  N N   . ASN   E  291 ? 0.51436 0.51436 0.51436 0.00000  0.00000  0.00000  291 ASN   A N   
7910  C CA  . ASN   E  291 ? 0.35505 0.35505 0.35505 0.00000  0.00000  0.00000  291 ASN   A CA  
7911  C C   . ASN   E  291 ? 0.41230 0.41230 0.41230 -0.00000 0.00000  0.00000  291 ASN   A C   
7912  O O   . ASN   E  291 ? 0.40746 0.40746 0.40746 -0.00000 0.00000  0.00000  291 ASN   A O   
7913  C CB  . ASN   E  291 ? 0.69775 0.69775 0.69775 0.00000  0.00000  0.00000  291 ASN   A CB  
7914  C CG  . ASN   E  291 ? 0.83668 0.83668 0.83668 0.00000  0.00000  0.00000  291 ASN   A CG  
7915  O OD1 . ASN   E  291 ? 1.41677 1.41677 1.41677 -0.00000 0.00000  0.00000  291 ASN   A OD1 
7916  N ND2 . ASN   E  291 ? 0.84574 0.84574 0.84574 -0.00000 0.00000  0.00000  291 ASN   A ND2 
7917  N N   . VAL   E  292 ? 0.31417 0.31417 0.31417 0.00000  0.00000  0.00000  292 VAL   A N   
7918  C CA  . VAL   E  292 ? 0.66844 0.66844 0.66844 0.00000  0.00000  0.00000  292 VAL   A CA  
7919  C C   . VAL   E  292 ? 0.67782 0.67782 0.67782 0.00000  0.00000  0.00000  292 VAL   A C   
7920  O O   . VAL   E  292 ? 0.45460 0.45460 0.45460 -0.00000 0.00000  0.00000  292 VAL   A O   
7921  C CB  . VAL   E  292 ? 0.64716 0.64716 0.64716 -0.00000 0.00000  0.00000  292 VAL   A CB  
7922  C CG1 . VAL   E  292 ? 0.55671 0.55671 0.55671 0.00000  0.00000  0.00000  292 VAL   A CG1 
7923  C CG2 . VAL   E  292 ? 0.45437 0.45437 0.45437 -0.00000 0.00000  -0.00000 292 VAL   A CG2 
7924  N N   . THR   E  293 ? 0.42257 0.42257 0.42257 0.00000  0.00000  -0.00000 293 THR   A N   
7925  C CA  . THR   E  293 ? 0.50348 0.50348 0.50348 0.00000  0.00000  0.00000  293 THR   A CA  
7926  C C   . THR   E  293 ? 0.84876 0.84876 0.84876 0.00000  0.00000  0.00000  293 THR   A C   
7927  O O   . THR   E  293 ? 0.68728 0.68728 0.68728 0.00000  0.00000  0.00000  293 THR   A O   
7928  C CB  . THR   E  293 ? 0.81469 0.81469 0.81469 0.00000  0.00000  0.00000  293 THR   A CB  
7929  O OG1 . THR   E  293 ? 0.53635 0.53635 0.53635 0.00000  0.00000  0.00000  293 THR   A OG1 
7930  C CG2 . THR   E  293 ? 0.41823 0.41823 0.41823 -0.00000 0.00000  0.00000  293 THR   A CG2 
7931  N N   . ALA   E  294 ? 0.43449 0.43449 0.43449 -0.00000 0.00000  0.00000  294 ALA   A N   
7932  C CA  . ALA   E  294 ? 0.35035 0.35035 0.35035 0.00000  0.00000  0.00000  294 ALA   A CA  
7933  C C   . ALA   E  294 ? 0.34337 0.34337 0.34337 0.00000  0.00000  0.00000  294 ALA   A C   
7934  O O   . ALA   E  294 ? 0.56469 0.56469 0.56469 -0.00000 0.00000  0.00000  294 ALA   A O   
7935  C CB  . ALA   E  294 ? 0.32943 0.32943 0.32943 0.00000  0.00000  0.00000  294 ALA   A CB  
7936  N N   . TYR   E  295 ? 0.37880 0.37880 0.37880 0.00000  0.00000  0.00000  295 TYR   A N   
7937  C CA  . TYR   E  295 ? 0.47311 0.47311 0.47311 0.00000  0.00000  0.00000  295 TYR   A CA  
7938  C C   . TYR   E  295 ? 0.44685 0.44685 0.44685 -0.00000 -0.00000 0.00000  295 TYR   A C   
7939  O O   . TYR   E  295 ? 0.40791 0.40791 0.40791 0.00000  0.00000  0.00000  295 TYR   A O   
7940  C CB  . TYR   E  295 ? 0.13382 0.13382 0.13382 0.00000  0.00000  0.00000  295 TYR   A CB  
7941  C CG  . TYR   E  295 ? 0.51117 0.51117 0.51117 -0.00000 -0.00000 0.00000  295 TYR   A CG  
7942  C CD1 . TYR   E  295 ? 0.36241 0.36241 0.36241 -0.00000 0.00000  0.00000  295 TYR   A CD1 
7943  C CD2 . TYR   E  295 ? 0.31002 0.31002 0.31002 0.00000  0.00000  0.00000  295 TYR   A CD2 
7944  C CE1 . TYR   E  295 ? 0.27246 0.27246 0.27246 -0.00000 0.00000  0.00000  295 TYR   A CE1 
7945  C CE2 . TYR   E  295 ? 0.24742 0.24742 0.24742 0.00000  -0.00000 0.00000  295 TYR   A CE2 
7946  C CZ  . TYR   E  295 ? 0.42838 0.42838 0.42838 0.00000  0.00000  0.00000  295 TYR   A CZ  
7947  O OH  . TYR   E  295 ? 0.31448 0.31448 0.31448 0.00000  0.00000  0.00000  295 TYR   A OH  
7948  N N   . HIS   E  296 ? 0.40036 0.40036 0.40036 -0.00000 0.00000  0.00000  296 HIS   A N   
7949  C CA  . HIS   E  296 ? 0.50457 0.50457 0.50457 0.00000  0.00000  0.00000  296 HIS   A CA  
7950  C C   . HIS   E  296 ? 0.30938 0.30938 0.30938 0.00000  0.00000  0.00000  296 HIS   A C   
7951  O O   . HIS   E  296 ? 0.38411 0.38411 0.38411 0.00000  0.00000  0.00000  296 HIS   A O   
7952  C CB  . HIS   E  296 ? 0.36509 0.36509 0.36509 -0.00000 0.00000  0.00000  296 HIS   A CB  
7953  C CG  . HIS   E  296 ? 0.49039 0.49039 0.49039 0.00000  0.00000  0.00000  296 HIS   A CG  
7954  N ND1 . HIS   E  296 ? 0.58938 0.58938 0.58938 0.00000  0.00000  0.00000  296 HIS   A ND1 
7955  C CD2 . HIS   E  296 ? 0.48338 0.48338 0.48338 0.00000  0.00000  0.00000  296 HIS   A CD2 
7956  C CE1 . HIS   E  296 ? 0.48847 0.48847 0.48847 -0.00000 0.00000  0.00000  296 HIS   A CE1 
7957  N NE2 . HIS   E  296 ? 0.66460 0.66460 0.66460 0.00000  0.00000  0.00000  296 HIS   A NE2 
7958  N N   . ARG   E  297 ? 0.32196 0.32196 0.32196 -0.00000 0.00000  0.00000  297 ARG   A N   
7959  C CA  . ARG   E  297 ? 0.26401 0.26401 0.26401 0.00000  0.00000  0.00000  297 ARG   A CA  
7960  C C   . ARG   E  297 ? 0.47903 0.47903 0.47903 -0.00000 0.00000  0.00000  297 ARG   A C   
7961  O O   . ARG   E  297 ? 0.34790 0.34790 0.34790 0.00000  0.00000  0.00000  297 ARG   A O   
7962  C CB  . ARG   E  297 ? 0.31317 0.31317 0.31317 0.00000  0.00000  0.00000  297 ARG   A CB  
7963  C CG  . ARG   E  297 ? 0.37674 0.37674 0.37674 0.00000  0.00000  0.00000  297 ARG   A CG  
7964  C CD  . ARG   E  297 ? 0.33702 0.33702 0.33702 0.00000  0.00000  0.00000  297 ARG   A CD  
7965  N NE  . ARG   E  297 ? 0.55875 0.55875 0.55875 0.00000  0.00000  0.00000  297 ARG   A NE  
7966  C CZ  . ARG   E  297 ? 0.46149 0.46149 0.46149 0.00000  0.00000  0.00000  297 ARG   A CZ  
7967  N NH1 . ARG   E  297 ? 0.56756 0.56756 0.56756 -0.00000 0.00000  0.00000  297 ARG   A NH1 
7968  N NH2 . ARG   E  297 ? 1.01466 1.01466 1.01466 0.00000  0.00000  -0.00000 297 ARG   A NH2 
7969  N N   . TRP   E  298 ? 0.36301 0.36301 0.36301 0.00000  0.00000  0.00000  298 TRP   A N   
7970  C CA  . TRP   E  298 ? 0.33576 0.33576 0.33576 -0.00000 0.00000  0.00000  298 TRP   A CA  
7971  C C   . TRP   E  298 ? 0.43607 0.43607 0.43607 0.00000  0.00000  0.00000  298 TRP   A C   
7972  O O   . TRP   E  298 ? 0.48721 0.48721 0.48721 0.00000  0.00000  0.00000  298 TRP   A O   
7973  C CB  . TRP   E  298 ? 0.26204 0.26204 0.26204 -0.00000 0.00000  0.00000  298 TRP   A CB  
7974  C CG  . TRP   E  298 ? 0.39795 0.39795 0.39795 0.00000  0.00000  0.00000  298 TRP   A CG  
7975  C CD1 . TRP   E  298 ? 0.33805 0.33805 0.33805 0.00000  0.00000  0.00000  298 TRP   A CD1 
7976  C CD2 . TRP   E  298 ? 0.26348 0.26348 0.26348 0.00000  0.00000  0.00000  298 TRP   A CD2 
7977  N NE1 . TRP   E  298 ? 0.22924 0.22924 0.22924 0.00000  0.00000  0.00000  298 TRP   A NE1 
7978  C CE2 . TRP   E  298 ? 0.30901 0.30901 0.30901 0.00000  0.00000  0.00000  298 TRP   A CE2 
7979  C CE3 . TRP   E  298 ? 0.17562 0.17562 0.17562 -0.00000 0.00000  0.00000  298 TRP   A CE3 
7980  C CZ2 . TRP   E  298 ? 0.37392 0.37392 0.37392 0.00000  0.00000  0.00000  298 TRP   A CZ2 
7981  C CZ3 . TRP   E  298 ? 0.45303 0.45303 0.45303 0.00000  -0.00000 0.00000  298 TRP   A CZ3 
7982  C CH2 . TRP   E  298 ? 0.34608 0.34608 0.34608 -0.00000 0.00000  0.00000  298 TRP   A CH2 
7983  N N   . HIS   E  299 ? 0.40797 0.40797 0.40797 0.00000  0.00000  0.00000  299 HIS   A N   
7984  C CA  . HIS   E  299 ? 0.52042 0.52042 0.52042 -0.00000 0.00000  0.00000  299 HIS   A CA  
7985  C C   . HIS   E  299 ? 0.39573 0.39573 0.39573 0.00000  0.00000  0.00000  299 HIS   A C   
7986  O O   . HIS   E  299 ? 0.42224 0.42224 0.42224 -0.00000 0.00000  0.00000  299 HIS   A O   
7987  C CB  . HIS   E  299 ? 0.25866 0.25866 0.25866 0.00000  0.00000  -0.00000 299 HIS   A CB  
7988  C CG  . HIS   E  299 ? 0.47293 0.47293 0.47293 -0.00000 0.00000  0.00000  299 HIS   A CG  
7989  N ND1 . HIS   E  299 ? 0.38484 0.38484 0.38484 0.00000  0.00000  0.00000  299 HIS   A ND1 
7990  C CD2 . HIS   E  299 ? 0.38867 0.38867 0.38867 -0.00000 0.00000  0.00000  299 HIS   A CD2 
7991  C CE1 . HIS   E  299 ? 0.55874 0.55874 0.55874 0.00000  0.00000  0.00000  299 HIS   A CE1 
7992  N NE2 . HIS   E  299 ? 0.41133 0.41133 0.41133 0.00000  0.00000  0.00000  299 HIS   A NE2 
7993  N N   . ALA   E  300 ? 0.37997 0.37997 0.37997 -0.00000 0.00000  0.00000  300 ALA   A N   
7994  C CA  . ALA   E  300 ? 0.44374 0.44374 0.44374 0.00000  0.00000  0.00000  300 ALA   A CA  
7995  C C   . ALA   E  300 ? 0.35490 0.35490 0.35490 0.00000  0.00000  0.00000  300 ALA   A C   
7996  O O   . ALA   E  300 ? 0.48408 0.48408 0.48408 0.00000  0.00000  0.00000  300 ALA   A O   
7997  C CB  . ALA   E  300 ? 0.29859 0.29859 0.29859 0.00000  0.00000  0.00000  300 ALA   A CB  
7998  N N   . PRO   E  301 ? 0.46486 0.46486 0.46486 -0.00000 0.00000  0.00000  301 PRO   A N   
7999  C CA  . PRO   E  301 ? 0.28553 0.28553 0.28553 0.00000  0.00000  0.00000  301 PRO   A CA  
8000  C C   . PRO   E  301 ? 0.54879 0.54879 0.54879 0.00000  0.00000  0.00000  301 PRO   A C   
8001  O O   . PRO   E  301 ? 0.35121 0.35121 0.35121 0.00000  0.00000  0.00000  301 PRO   A O   
8002  C CB  . PRO   E  301 ? 0.39822 0.39822 0.39822 0.00000  0.00000  0.00000  301 PRO   A CB  
8003  C CG  . PRO   E  301 ? 0.36338 0.36338 0.36338 0.00000  0.00000  0.00000  301 PRO   A CG  
8004  C CD  . PRO   E  301 ? 0.17733 0.17733 0.17733 0.00000  0.00000  0.00000  301 PRO   A CD  
8005  N N   . VAL   E  302 ? 0.28336 0.28336 0.28336 -0.00000 0.00000  0.00000  302 VAL   A N   
8006  C CA  . VAL   E  302 ? 0.59787 0.59787 0.59787 0.00000  0.00000  0.00000  302 VAL   A CA  
8007  C C   . VAL   E  302 ? 0.27380 0.27380 0.27380 0.00000  0.00000  0.00000  302 VAL   A C   
8008  O O   . VAL   E  302 ? 0.48496 0.48496 0.48496 0.00000  0.00000  0.00000  302 VAL   A O   
8009  C CB  . VAL   E  302 ? 0.27073 0.27073 0.27073 -0.00000 0.00000  0.00000  302 VAL   A CB  
8010  C CG1 . VAL   E  302 ? 0.57808 0.57808 0.57808 -0.00000 0.00000  0.00000  302 VAL   A CG1 
8011  C CG2 . VAL   E  302 ? 0.25411 0.25411 0.25411 0.00000  0.00000  0.00000  302 VAL   A CG2 
8012  N N   . ASN   E  303 ? 0.50448 0.50448 0.50448 -0.00000 0.00000  0.00000  303 ASN   A N   
8013  C CA  . ASN   E  303 ? 0.31288 0.31288 0.31288 -0.00000 0.00000  0.00000  303 ASN   A CA  
8014  C C   . ASN   E  303 ? 0.55735 0.55735 0.55735 0.00000  0.00000  0.00000  303 ASN   A C   
8015  O O   . ASN   E  303 ? 0.50038 0.50038 0.50038 0.00000  -0.00000 0.00000  303 ASN   A O   
8016  C CB  . ASN   E  303 ? 0.55133 0.55133 0.55133 -0.00000 0.00000  0.00000  303 ASN   A CB  
8017  C CG  . ASN   E  303 ? 0.45937 0.45937 0.45937 -0.00000 0.00000  0.00000  303 ASN   A CG  
8018  O OD1 . ASN   E  303 ? 0.51899 0.51899 0.51899 -0.00000 0.00000  0.00000  303 ASN   A OD1 
8019  N ND2 . ASN   E  303 ? 0.49432 0.49432 0.49432 0.00000  0.00000  0.00000  303 ASN   A ND2 
8020  N N   . GLY   E  304 ? 0.53794 0.53794 0.53794 -0.00000 0.00000  0.00000  304 GLY   A N   
8021  C CA  . GLY   E  304 ? 0.37041 0.37041 0.37041 0.00000  0.00000  0.00000  304 GLY   A CA  
8022  C C   . GLY   E  304 ? 0.57972 0.57972 0.57972 0.00000  0.00000  0.00000  304 GLY   A C   
8023  O O   . GLY   E  304 ? 0.61538 0.61538 0.61538 0.00000  0.00000  0.00000  304 GLY   A O   
8024  N N   . THR   E  305 ? 0.50877 0.50877 0.50877 0.00000  0.00000  0.00000  305 THR   A N   
8025  C CA  . THR   E  305 ? 0.52522 0.52522 0.52522 0.00000  0.00000  0.00000  305 THR   A CA  
8026  C C   . THR   E  305 ? 0.80299 0.80299 0.80299 0.00000  0.00000  0.00000  305 THR   A C   
8027  O O   . THR   E  305 ? 0.35811 0.35811 0.35811 0.00000  0.00000  0.00000  305 THR   A O   
8028  C CB  . THR   E  305 ? 0.39375 0.39375 0.39375 0.00000  0.00000  0.00000  305 THR   A CB  
8029  O OG1 . THR   E  305 ? 0.60996 0.60996 0.60996 -0.00000 -0.00000 0.00000  305 THR   A OG1 
8030  C CG2 . THR   E  305 ? 0.39105 0.39105 0.39105 -0.00000 0.00000  0.00000  305 THR   A CG2 
8031  N N   . ILE   E  306 ? 0.31326 0.31326 0.31326 0.00000  0.00000  0.00000  306 ILE   A N   
8032  C CA  . ILE   E  306 ? 0.47570 0.47570 0.47570 0.00000  -0.00000 0.00000  306 ILE   A CA  
8033  C C   . ILE   E  306 ? 0.48380 0.48380 0.48380 0.00000  0.00000  0.00000  306 ILE   A C   
8034  O O   . ILE   E  306 ? 0.52249 0.52249 0.52249 -0.00000 0.00000  0.00000  306 ILE   A O   
8035  C CB  . ILE   E  306 ? 0.42845 0.42845 0.42845 -0.00000 0.00000  0.00000  306 ILE   A CB  
8036  C CG1 . ILE   E  306 ? 0.26890 0.26890 0.26890 0.00000  0.00000  0.00000  306 ILE   A CG1 
8037  C CG2 . ILE   E  306 ? 0.37391 0.37391 0.37391 -0.00000 0.00000  0.00000  306 ILE   A CG2 
8038  C CD1 . ILE   E  306 ? 0.35449 0.35449 0.35449 0.00000  0.00000  0.00000  306 ILE   A CD1 
8039  N N   . VAL   E  307 ? 0.43455 0.43455 0.43455 -0.00000 0.00000  0.00000  307 VAL   A N   
8040  C CA  . VAL   E  307 ? 0.35710 0.35710 0.35710 0.00000  0.00000  0.00000  307 VAL   A CA  
8041  C C   . VAL   E  307 ? 0.46751 0.46751 0.46751 0.00000  0.00000  0.00000  307 VAL   A C   
8042  O O   . VAL   E  307 ? 0.44855 0.44855 0.44855 0.00000  0.00000  0.00000  307 VAL   A O   
8043  C CB  . VAL   E  307 ? 0.55876 0.55876 0.55876 0.00000  0.00000  0.00000  307 VAL   A CB  
8044  C CG1 . VAL   E  307 ? 0.22915 0.22915 0.22915 -0.00000 0.00000  0.00000  307 VAL   A CG1 
8045  C CG2 . VAL   E  307 ? 0.36937 0.36937 0.36937 0.00000  0.00000  0.00000  307 VAL   A CG2 
8046  N N   . LYS   E  308 ? 0.49635 0.49635 0.49635 0.00000  0.00000  0.00000  308 LYS   A N   
8047  C CA  . LYS   E  308 ? 0.37754 0.37754 0.37754 0.00000  0.00000  0.00000  308 LYS   A CA  
8048  C C   . LYS   E  308 ? 0.54882 0.54882 0.54882 0.00000  0.00000  0.00000  308 LYS   A C   
8049  O O   . LYS   E  308 ? 0.33567 0.33567 0.33567 0.00000  0.00000  0.00000  308 LYS   A O   
8050  C CB  . LYS   E  308 ? 0.33721 0.33721 0.33721 0.00000  0.00000  0.00000  308 LYS   A CB  
8051  C CG  . LYS   E  308 ? 0.22755 0.22755 0.22755 0.00000  -0.00000 0.00000  308 LYS   A CG  
8052  C CD  . LYS   E  308 ? 0.36506 0.36506 0.36506 0.00000  0.00000  0.00000  308 LYS   A CD  
8053  C CE  . LYS   E  308 ? 0.61764 0.61764 0.61764 0.00000  0.00000  0.00000  308 LYS   A CE  
8054  N NZ  . LYS   E  308 ? 0.76514 0.76514 0.76514 -0.00000 0.00000  0.00000  308 LYS   A NZ  
8055  N N   . ILE   E  309 ? 0.34953 0.34953 0.34953 -0.00000 0.00000  0.00000  309 ILE   A N   
8056  C CA  . ILE   E  309 ? 0.43918 0.43918 0.43918 0.00000  0.00000  0.00000  309 ILE   A CA  
8057  C C   . ILE   E  309 ? 0.34353 0.34353 0.34353 0.00000  0.00000  0.00000  309 ILE   A C   
8058  O O   . ILE   E  309 ? 0.45213 0.45213 0.45213 -0.00000 0.00000  0.00000  309 ILE   A O   
8059  C CB  . ILE   E  309 ? 0.24224 0.24224 0.24224 0.00000  0.00000  0.00000  309 ILE   A CB  
8060  C CG1 . ILE   E  309 ? 0.50428 0.50428 0.50428 -0.00000 0.00000  0.00000  309 ILE   A CG1 
8061  C CG2 . ILE   E  309 ? 0.27587 0.27587 0.27587 0.00000  0.00000  0.00000  309 ILE   A CG2 
8062  C CD1 . ILE   E  309 ? 0.25981 0.25981 0.25981 0.00000  0.00000  0.00000  309 ILE   A CD1 
8063  N N   . ILE   E  310 ? 0.39443 0.39443 0.39443 0.00000  0.00000  0.00000  310 ILE   A N   
8064  C CA  . ILE   E  310 ? 0.19024 0.19024 0.19024 0.00000  0.00000  0.00000  310 ILE   A CA  
8065  C C   . ILE   E  310 ? 0.41076 0.41076 0.41076 0.00000  0.00000  0.00000  310 ILE   A C   
8066  O O   . ILE   E  310 ? 0.32203 0.32203 0.32203 -0.00000 0.00000  0.00000  310 ILE   A O   
8067  C CB  . ILE   E  310 ? 0.41048 0.41048 0.41048 0.00000  0.00000  0.00000  310 ILE   A CB  
8068  C CG1 . ILE   E  310 ? 0.42429 0.42429 0.42429 0.00000  0.00000  0.00000  310 ILE   A CG1 
8069  C CG2 . ILE   E  310 ? 0.25135 0.25135 0.25135 -0.00000 0.00000  0.00000  310 ILE   A CG2 
8070  C CD1 . ILE   E  310 ? 0.47966 0.47966 0.47966 -0.00000 0.00000  0.00000  310 ILE   A CD1 
8071  N N   . ASN   E  311 ? 0.35101 0.35101 0.35101 -0.00000 0.00000  0.00000  311 ASN   A N   
8072  C CA  . ASN   E  311 ? 0.31064 0.31064 0.31064 0.00000  0.00000  0.00000  311 ASN   A CA  
8073  C C   . ASN   E  311 ? 0.17584 0.17584 0.17584 0.00000  0.00000  0.00000  311 ASN   A C   
8074  O O   . ASN   E  311 ? 0.51796 0.51796 0.51796 0.00000  0.00000  0.00000  311 ASN   A O   
8075  C CB  . ASN   E  311 ? 0.11755 0.11755 0.11755 0.00000  0.00000  0.00000  311 ASN   A CB  
8076  C CG  . ASN   E  311 ? 0.69664 0.69664 0.69664 -0.00000 0.00000  0.00000  311 ASN   A CG  
8077  O OD1 . ASN   E  311 ? 0.44322 0.44322 0.44322 0.00000  0.00000  0.00000  311 ASN   A OD1 
8078  N ND2 . ASN   E  311 ? 0.47113 0.47113 0.47113 0.00000  0.00000  0.00000  311 ASN   A ND2 
8079  N N   . VAL   E  312 ? 0.27384 0.27384 0.27384 -0.00000 0.00000  0.00000  312 VAL   A N   
8080  C CA  . VAL   E  312 ? 0.25415 0.25415 0.25415 0.00000  0.00000  0.00000  312 VAL   A CA  
8081  C C   . VAL   E  312 ? 0.23954 0.23954 0.23954 0.00000  0.00000  0.00000  312 VAL   A C   
8082  O O   . VAL   E  312 ? 0.55494 0.55494 0.55494 0.00000  0.00000  0.00000  312 VAL   A O   
8083  C CB  . VAL   E  312 ? 0.29932 0.29932 0.29932 0.00000  0.00000  0.00000  312 VAL   A CB  
8084  C CG1 . VAL   E  312 ? 0.12576 0.12576 0.12576 -0.00000 0.00000  0.00000  312 VAL   A CG1 
8085  C CG2 . VAL   E  312 ? 0.20681 0.20681 0.20681 0.00000  0.00000  0.00000  312 VAL   A CG2 
8086  N N   . PRO   E  313 ? 0.43462 0.43462 0.43462 0.00000  0.00000  0.00000  313 PRO   A N   
8087  C CA  . PRO   E  313 ? 0.37994 0.37994 0.37994 0.00000  0.00000  0.00000  313 PRO   A CA  
8088  C C   . PRO   E  313 ? 0.42655 0.42655 0.42655 -0.00000 0.00000  0.00000  313 PRO   A C   
8089  O O   . PRO   E  313 ? 0.36624 0.36624 0.36624 0.00000  0.00000  0.00000  313 PRO   A O   
8090  C CB  . PRO   E  313 ? 0.16513 0.16513 0.16513 0.00000  0.00000  0.00000  313 PRO   A CB  
8091  C CG  . PRO   E  313 ? 0.23920 0.23920 0.23920 0.00000  -0.00000 0.00000  313 PRO   A CG  
8092  C CD  . PRO   E  313 ? 0.19070 0.19070 0.19070 0.00000  0.00000  0.00000  313 PRO   A CD  
8093  N N   . GLY   E  314 ? 0.28210 0.28210 0.28210 -0.00000 0.00000  0.00000  314 GLY   A N   
8094  C CA  . GLY   E  314 ? 0.18663 0.18663 0.18663 0.00000  0.00000  0.00000  314 GLY   A CA  
8095  C C   . GLY   E  314 ? 0.40146 0.40146 0.40146 -0.00000 0.00000  0.00000  314 GLY   A C   
8096  O O   . GLY   E  314 ? 0.29066 0.29066 0.29066 -0.00000 0.00000  0.00000  314 GLY   A O   
8097  N N   . THR   E  315 ? 0.36409 0.36409 0.36409 -0.00000 0.00000  0.00000  315 THR   A N   
8098  C CA  . THR   E  315 ? 0.39388 0.39388 0.39388 0.00000  0.00000  0.00000  315 THR   A CA  
8099  C C   . THR   E  315 ? 0.49938 0.49938 0.49938 -0.00000 0.00000  0.00000  315 THR   A C   
8100  O O   . THR   E  315 ? 0.40038 0.40038 0.40038 0.00000  0.00000  0.00000  315 THR   A O   
8101  C CB  . THR   E  315 ? 0.38910 0.38910 0.38910 -0.00000 0.00000  0.00000  315 THR   A CB  
8102  O OG1 . THR   E  315 ? 0.31031 0.31031 0.31031 0.00000  0.00000  0.00000  315 THR   A OG1 
8103  C CG2 . THR   E  315 ? 0.26867 0.26867 0.26867 0.00000  0.00000  0.00000  315 THR   A CG2 
8104  N N   . TYR   E  316 ? 0.32653 0.32653 0.32653 0.00000  0.00000  0.00000  316 TYR   A N   
8105  C CA  . TYR   E  316 ? 0.32095 0.32095 0.32095 -0.00000 0.00000  0.00000  316 TYR   A CA  
8106  C C   . TYR   E  316 ? 0.25794 0.25794 0.25794 0.00000  0.00000  0.00000  316 TYR   A C   
8107  O O   . TYR   E  316 ? 0.38285 0.38285 0.38285 -0.00000 0.00000  0.00000  316 TYR   A O   
8108  C CB  . TYR   E  316 ? 0.25693 0.25693 0.25693 0.00000  0.00000  0.00000  316 TYR   A CB  
8109  C CG  . TYR   E  316 ? 0.39304 0.39304 0.39304 0.00000  0.00000  0.00000  316 TYR   A CG  
8110  C CD1 . TYR   E  316 ? 0.41050 0.41050 0.41050 -0.00000 0.00000  0.00000  316 TYR   A CD1 
8111  C CD2 . TYR   E  316 ? 0.31830 0.31830 0.31830 0.00000  0.00000  0.00000  316 TYR   A CD2 
8112  C CE1 . TYR   E  316 ? 0.30461 0.30461 0.30461 -0.00000 0.00000  0.00000  316 TYR   A CE1 
8113  C CE2 . TYR   E  316 ? 0.21936 0.21936 0.21936 0.00000  0.00000  0.00000  316 TYR   A CE2 
8114  C CZ  . TYR   E  316 ? 0.44460 0.44460 0.44460 0.00000  0.00000  0.00000  316 TYR   A CZ  
8115  O OH  . TYR   E  316 ? 0.33407 0.33407 0.33407 -0.00000 0.00000  0.00000  316 TYR   A OH  
8116  N N   . PHE   E  317 ? 0.45572 0.45572 0.45572 0.00000  0.00000  0.00000  317 PHE   A N   
8117  C CA  . PHE   E  317 ? 0.21824 0.21824 0.21824 -0.00000 0.00000  0.00000  317 PHE   A CA  
8118  C C   . PHE   E  317 ? 0.49269 0.49269 0.49269 -0.00000 0.00000  0.00000  317 PHE   A C   
8119  O O   . PHE   E  317 ? 0.33984 0.33984 0.33984 0.00000  0.00000  0.00000  317 PHE   A O   
8120  C CB  . PHE   E  317 ? 0.21671 0.21671 0.21671 -0.00000 0.00000  0.00000  317 PHE   A CB  
8121  C CG  . PHE   E  317 ? 0.47183 0.47183 0.47183 0.00000  0.00000  0.00000  317 PHE   A CG  
8122  C CD1 . PHE   E  317 ? 0.22685 0.22685 0.22685 0.00000  0.00000  0.00000  317 PHE   A CD1 
8123  C CD2 . PHE   E  317 ? 0.41817 0.41817 0.41817 0.00000  0.00000  0.00000  317 PHE   A CD2 
8124  C CE1 . PHE   E  317 ? 0.42074 0.42074 0.42074 -0.00000 0.00000  0.00000  317 PHE   A CE1 
8125  C CE2 . PHE   E  317 ? 0.32689 0.32689 0.32689 0.00000  0.00000  0.00000  317 PHE   A CE2 
8126  C CZ  . PHE   E  317 ? 0.34470 0.34470 0.34470 0.00000  0.00000  0.00000  317 PHE   A CZ  
8127  N N   . ALA   E  318 ? 0.26946 0.26946 0.26946 0.00000  0.00000  0.00000  318 ALA   A N   
8128  C CA  . ALA   E  318 ? 0.22988 0.22988 0.22988 -0.00000 0.00000  0.00000  318 ALA   A CA  
8129  C C   . ALA   E  318 ? 0.29088 0.29088 0.29088 -0.00000 0.00000  0.00000  318 ALA   A C   
8130  O O   . ALA   E  318 ? 0.35315 0.35315 0.35315 -0.00000 0.00000  0.00000  318 ALA   A O   
8131  C CB  . ALA   E  318 ? 0.14784 0.14784 0.14784 -0.00000 0.00000  0.00000  318 ALA   A CB  
8132  N N   . GLN   E  319 ? 0.34047 0.34047 0.34047 -0.00000 0.00000  0.00000  319 GLN   A N   
8133  C CA  . GLN   E  319 ? 0.29590 0.29590 0.29590 0.00000  0.00000  0.00000  319 GLN   A CA  
8134  C C   . GLN   E  319 ? 0.27177 0.27177 0.27177 0.00000  0.00000  -0.00000 319 GLN   A C   
8135  O O   . GLN   E  319 ? 0.45254 0.45254 0.45254 0.00000  0.00000  0.00000  319 GLN   A O   
8136  C CB  . GLN   E  319 ? 0.28939 0.28939 0.28939 0.00000  0.00000  0.00000  319 GLN   A CB  
8137  C CG  . GLN   E  319 ? 0.39201 0.39201 0.39201 0.00000  0.00000  0.00000  319 GLN   A CG  
8138  C CD  . GLN   E  319 ? 0.25285 0.25285 0.25285 0.00000  0.00000  0.00000  319 GLN   A CD  
8139  O OE1 . GLN   E  319 ? 0.54821 0.54821 0.54821 0.00000  0.00000  0.00000  319 GLN   A OE1 
8140  N NE2 . GLN   E  319 ? 0.36439 0.36439 0.36439 0.00000  0.00000  0.00000  319 GLN   A NE2 
8141  N N   . ALA   E  320 ? 0.41282 0.41282 0.41282 -0.00000 0.00000  0.00000  320 ALA   A N   
8142  C CA  . ALA   E  320 ? 0.42226 0.42226 0.42226 -0.00000 0.00000  0.00000  320 ALA   A CA  
8143  C C   . ALA   E  320 ? 0.41900 0.41900 0.41900 0.00000  0.00000  0.00000  320 ALA   A C   
8144  O O   . ALA   E  320 ? 0.43849 0.43849 0.43849 0.00000  0.00000  0.00000  320 ALA   A O   
8145  C CB  . ALA   E  320 ? 0.21636 0.21636 0.21636 -0.00000 0.00000  0.00000  320 ALA   A CB  
8146  N N   . PRO   E  321 ? 0.50273 0.50273 0.50273 0.00000  0.00000  0.00000  321 PRO   A N   
8147  C CA  . PRO   E  321 ? 0.32414 0.32414 0.32414 -0.00000 0.00000  0.00000  321 PRO   A CA  
8148  C C   . PRO   E  321 ? 0.39615 0.39615 0.39615 0.00000  0.00000  0.00000  321 PRO   A C   
8149  O O   . PRO   E  321 ? 0.45652 0.45652 0.45652 0.00000  0.00000  0.00000  321 PRO   A O   
8150  C CB  . PRO   E  321 ? 0.23798 0.23798 0.23798 -0.00000 0.00000  0.00000  321 PRO   A CB  
8151  C CG  . PRO   E  321 ? 0.50597 0.50597 0.50597 0.00000  0.00000  0.00000  321 PRO   A CG  
8152  C CD  . PRO   E  321 ? 0.28167 0.28167 0.28167 0.00000  0.00000  0.00000  321 PRO   A CD  
8153  N N   . SER   E  322 ? 0.37759 0.37759 0.37759 0.00000  0.00000  0.00000  322 SER   A N   
8154  C CA  . SER   E  322 ? 0.37103 0.37103 0.37103 0.00000  0.00000  0.00000  322 SER   A CA  
8155  C C   . SER   E  322 ? 0.36601 0.36601 0.36601 0.00000  0.00000  0.00000  322 SER   A C   
8156  O O   . SER   E  322 ? 0.61146 0.61146 0.61146 0.00000  0.00000  0.00000  322 SER   A O   
8157  C CB  . SER   E  322 ? 0.25786 0.25786 0.25786 0.00000  0.00000  0.00000  322 SER   A CB  
8158  O OG  . SER   E  322 ? 0.57566 0.57566 0.57566 0.00000  0.00000  0.00000  322 SER   A OG  
8159  N N   . THR   E  323 ? 0.60472 0.60472 0.60472 0.00000  0.00000  0.00000  323 THR   A N   
8160  C CA  . THR   E  323 ? 0.38111 0.38111 0.38111 0.00000  0.00000  0.00000  323 THR   A CA  
8161  C C   . THR   E  323 ? 0.57709 0.57709 0.57709 0.00000  -0.00000 0.00000  323 THR   A C   
8162  O O   . THR   E  323 ? 0.36066 0.36066 0.36066 0.00000  0.00000  0.00000  323 THR   A O   
8163  C CB  . THR   E  323 ? 0.46640 0.46640 0.46640 0.00000  0.00000  0.00000  323 THR   A CB  
8164  O OG1 . THR   E  323 ? 0.48584 0.48584 0.48584 0.00000  0.00000  0.00000  323 THR   A OG1 
8165  C CG2 . THR   E  323 ? 0.23779 0.23779 0.23779 -0.00000 0.00000  0.00000  323 THR   A CG2 
8166  N N   . ILE   E  324 ? 0.40981 0.40981 0.40981 0.00000  0.00000  0.00000  324 ILE   A N   
8167  C CA  . ILE   E  324 ? 0.43192 0.43192 0.43192 0.00000  0.00000  0.00000  324 ILE   A CA  
8168  C C   . ILE   E  324 ? 0.66685 0.66685 0.66685 0.00000  0.00000  0.00000  324 ILE   A C   
8169  O O   . ILE   E  324 ? 0.57402 0.57402 0.57402 0.00000  0.00000  0.00000  324 ILE   A O   
8170  C CB  . ILE   E  324 ? 0.28005 0.28005 0.28005 0.00000  -0.00000 0.00000  324 ILE   A CB  
8171  C CG1 . ILE   E  324 ? 0.44949 0.44949 0.44949 0.00000  0.00000  0.00000  324 ILE   A CG1 
8172  C CG2 . ILE   E  324 ? 0.31225 0.31225 0.31225 0.00000  0.00000  0.00000  324 ILE   A CG2 
8173  C CD1 . ILE   E  324 ? 0.36721 0.36721 0.36721 0.00000  0.00000  0.00000  324 ILE   A CD1 
8174  N N   . GLY   E  325 ? 0.44728 0.44728 0.44728 -0.00000 0.00000  0.00000  325 GLY   A N   
8175  C CA  . GLY   E  325 ? 0.38673 0.38673 0.38673 -0.00000 0.00000  0.00000  325 GLY   A CA  
8176  C C   . GLY   E  325 ? 0.50111 0.50111 0.50111 -0.00000 0.00000  0.00000  325 GLY   A C   
8177  O O   . GLY   E  325 ? 0.56661 0.56661 0.56661 -0.00000 0.00000  0.00000  325 GLY   A O   
8178  N N   . ASP   E  326 ? 0.41943 0.41943 0.41943 -0.00000 0.00000  0.00000  326 ASP   A N   
8179  C CA  . ASP   E  326 ? 0.51068 0.51068 0.51068 0.00000  -0.00000 0.00000  326 ASP   A CA  
8180  C C   . ASP   E  326 ? 0.39890 0.39890 0.39890 -0.00000 0.00000  0.00000  326 ASP   A C   
8181  O O   . ASP   E  326 ? 0.53021 0.53021 0.53021 -0.00000 0.00000  0.00000  326 ASP   A O   
8182  C CB  . ASP   E  326 ? 0.28818 0.28818 0.28818 0.00000  0.00000  0.00000  326 ASP   A CB  
8183  C CG  . ASP   E  326 ? 0.75264 0.75264 0.75264 -0.00000 0.00000  0.00000  326 ASP   A CG  
8184  O OD1 . ASP   E  326 ? 0.57028 0.57028 0.57028 0.00000  0.00000  0.00000  326 ASP   A OD1 
8185  O OD2 . ASP   E  326 ? 0.60313 0.60313 0.60313 0.00000  0.00000  0.00000  326 ASP   A OD2 
8186  N N   . PRO   E  327 ? 0.59247 0.59247 0.59247 0.00000  0.00000  0.00000  327 PRO   A N   
8187  C CA  . PRO   E  327 ? 0.40828 0.40828 0.40828 -0.00000 0.00000  0.00000  327 PRO   A CA  
8188  C C   . PRO   E  327 ? 0.34139 0.34139 0.34139 -0.00000 0.00000  -0.00000 327 PRO   A C   
8189  O O   . PRO   E  327 ? 0.50582 0.50582 0.50582 0.00000  0.00000  0.00000  327 PRO   A O   
8190  C CB  . PRO   E  327 ? 0.15897 0.15897 0.15897 0.00000  0.00000  0.00000  327 PRO   A CB  
8191  C CG  . PRO   E  327 ? 0.33939 0.33939 0.33939 -0.00000 0.00000  0.00000  327 PRO   A CG  
8192  C CD  . PRO   E  327 ? 0.37631 0.37631 0.37631 -0.00000 0.00000  0.00000  327 PRO   A CD  
8193  N N   . ILE   E  328 ? 0.37346 0.37346 0.37346 0.00000  0.00000  0.00000  328 ILE   A N   
8194  C CA  . ILE   E  328 ? 0.37092 0.37092 0.37092 0.00000  0.00000  0.00000  328 ILE   A CA  
8195  C C   . ILE   E  328 ? 0.39999 0.39999 0.39999 -0.00000 0.00000  0.00000  328 ILE   A C   
8196  O O   . ILE   E  328 ? 0.51450 0.51450 0.51450 0.00000  -0.00000 -0.00000 328 ILE   A O   
8197  C CB  . ILE   E  328 ? 0.43709 0.43709 0.43709 -0.00000 0.00000  0.00000  328 ILE   A CB  
8198  C CG1 . ILE   E  328 ? 0.27823 0.27823 0.27823 0.00000  0.00000  0.00000  328 ILE   A CG1 
8199  C CG2 . ILE   E  328 ? 0.30007 0.30007 0.30007 0.00000  0.00000  0.00000  328 ILE   A CG2 
8200  C CD1 . ILE   E  328 ? 0.22769 0.22769 0.22769 -0.00000 0.00000  0.00000  328 ILE   A CD1 
8201  N N   . PRO   E  329 ? 0.59334 0.59334 0.59334 0.00000  0.00000  0.00000  329 PRO   A N   
8202  C CA  . PRO   E  329 ? 0.40934 0.40934 0.40934 -0.00000 0.00000  0.00000  329 PRO   A CA  
8203  C C   . PRO   E  329 ? 0.43787 0.43787 0.43787 0.00000  0.00000  0.00000  329 PRO   A C   
8204  O O   . PRO   E  329 ? 0.84760 0.84760 0.84760 -0.00000 0.00000  0.00000  329 PRO   A O   
8205  C CB  . PRO   E  329 ? 0.24293 0.24293 0.24293 0.00000  0.00000  -0.00000 329 PRO   A CB  
8206  C CG  . PRO   E  329 ? 0.37855 0.37855 0.37855 -0.00000 0.00000  0.00000  329 PRO   A CG  
8207  C CD  . PRO   E  329 ? 0.44050 0.44050 0.44050 -0.00000 0.00000  0.00000  329 PRO   A CD  
8208  N N   . ASP   E  330 ? 0.78299 0.78299 0.78299 -0.00000 0.00000  0.00000  330 ASP   A N   
8209  C CA  . ASP   E  330 ? 0.91055 0.91055 0.91055 -0.00000 0.00000  0.00000  330 ASP   A CA  
8210  C C   . ASP   E  330 ? 0.64070 0.64070 0.64070 0.00000  0.00000  0.00000  330 ASP   A C   
8211  O O   . ASP   E  330 ? 1.00450 1.00450 1.00450 0.00000  0.00000  0.00000  330 ASP   A O   
8212  C CB  . ASP   E  330 ? 0.54622 0.54622 0.54622 -0.00000 0.00000  0.00000  330 ASP   A CB  
8213  C CG  . ASP   E  330 ? 0.78719 0.78719 0.78719 0.00000  0.00000  -0.00000 330 ASP   A CG  
8214  O OD1 . ASP   E  330 ? 1.18114 1.18114 1.18114 0.00000  0.00000  0.00000  330 ASP   A OD1 
8215  O OD2 . ASP   E  330 ? 0.67990 0.67990 0.67990 -0.00000 0.00000  -0.00000 330 ASP   A OD2 
8216  N N   . ASN   E  331 ? 1.01341 1.01341 1.01341 0.00000  0.00000  0.00000  331 ASN   A N   
8217  C CA  . ASN   E  331 ? 1.01499 1.01499 1.01499 0.00000  0.00000  0.00000  331 ASN   A CA  
8218  C C   . ASN   E  331 ? 0.79548 0.79548 0.79548 0.00000  0.00000  0.00000  331 ASN   A C   
8219  O O   . ASN   E  331 ? 1.34908 1.34908 1.34908 -0.00000 0.00000  0.00000  331 ASN   A O   
8220  C CB  . ASN   E  331 ? 0.73540 0.73540 0.73540 -0.00000 0.00000  0.00000  331 ASN   A CB  
8221  C CG  . ASN   E  331 ? 0.87587 0.87587 0.87587 0.00000  0.00000  0.00000  331 ASN   A CG  
8222  O OD1 . ASN   E  331 ? 1.75627 1.75627 1.75627 0.00000  0.00000  0.00000  331 ASN   A OD1 
8223  N ND2 . ASN   E  331 ? 0.92868 0.92868 0.92868 -0.00000 0.00000  0.00000  331 ASN   A ND2 
8224  N N   . ASP   E  332 ? 2.02596 2.02596 2.02596 0.00000  0.00000  0.00000  332 ASP   A N   
8225  C CA  . ASP   E  332 ? 0.35569 0.35569 0.35569 0.00000  0.00000  0.00000  332 ASP   A CA  
8226  C C   . ASP   E  332 ? 0.98241 0.98241 0.98241 0.00000  0.00000  0.00000  332 ASP   A C   
8227  O O   . ASP   E  332 ? 1.29382 1.29382 1.29382 -0.00000 0.00000  0.00000  332 ASP   A O   
8228  C CB  . ASP   E  332 ? 0.73847 0.73847 0.73847 -0.00000 0.00000  -0.00000 332 ASP   A CB  
8229  C CG  . ASP   E  332 ? 1.59542 1.59542 1.59542 -0.00000 0.00000  0.00000  332 ASP   A CG  
8230  O OD1 . ASP   E  332 ? 1.63302 1.63302 1.63302 -0.00000 0.00000  0.00000  332 ASP   A OD1 
8231  O OD2 . ASP   E  332 ? 1.66662 1.66662 1.66662 0.00000  0.00000  0.00000  332 ASP   A OD2 
8232  N N   . TYR   E  333 ? 1.25591 1.25591 1.25591 -0.00000 0.00000  0.00000  333 TYR   A N   
8233  C CA  . TYR   E  333 ? 0.94756 0.94756 0.94756 -0.00000 0.00000  0.00000  333 TYR   A CA  
8234  C C   . TYR   E  333 ? 1.56690 1.56690 1.56690 0.00000  0.00000  0.00000  333 TYR   A C   
8235  O O   . TYR   E  333 ? 1.49082 1.49082 1.49082 0.00000  0.00000  0.00000  333 TYR   A O   
8236  C CB  . TYR   E  333 ? 0.25602 0.25602 0.25602 0.00000  0.00000  0.00000  333 TYR   A CB  
8237  C CG  . TYR   E  333 ? 1.28888 1.28888 1.28888 0.00000  0.00000  0.00000  333 TYR   A CG  
8238  C CD1 . TYR   E  333 ? 1.27393 1.27393 1.27393 -0.00000 0.00000  0.00000  333 TYR   A CD1 
8239  C CD2 . TYR   E  333 ? 1.44212 1.44212 1.44212 0.00000  -0.00000 0.00000  333 TYR   A CD2 
8240  C CE1 . TYR   E  333 ? 1.29436 1.29436 1.29436 0.00000  0.00000  0.00000  333 TYR   A CE1 
8241  C CE2 . TYR   E  333 ? 1.58852 1.58852 1.58852 -0.00000 0.00000  0.00000  333 TYR   A CE2 
8242  C CZ  . TYR   E  333 ? 1.50085 1.50085 1.50085 -0.00000 0.00000  0.00000  333 TYR   A CZ  
8243  O OH  . TYR   E  333 ? 0.40539 0.40539 0.40539 -0.00000 0.00000  0.00000  333 TYR   A OH  
8244  N N   . ASP   E  334 ? 0.87686 0.87686 0.87686 0.00000  0.00000  0.00000  334 ASP   A N   
8245  C CA  . ASP   E  334 ? 0.85247 0.85247 0.85247 -0.00000 0.00000  0.00000  334 ASP   A CA  
8246  C C   . ASP   E  334 ? 0.97204 0.97204 0.97204 -0.00000 0.00000  0.00000  334 ASP   A C   
8247  O O   . ASP   E  334 ? 0.53797 0.53797 0.53797 0.00000  0.00000  0.00000  334 ASP   A O   
8248  C CB  . ASP   E  334 ? 1.21726 1.21726 1.21726 0.00000  0.00000  -0.00000 334 ASP   A CB  
8249  C CG  . ASP   E  334 ? 1.40244 1.40244 1.40244 -0.00000 0.00000  0.00000  334 ASP   A CG  
8250  O OD1 . ASP   E  334 ? 0.84778 0.84778 0.84778 0.00000  0.00000  0.00000  334 ASP   A OD1 
8251  O OD2 . ASP   E  334 ? 0.99120 0.99120 0.99120 0.00000  0.00000  0.00000  334 ASP   A OD2 
8252  N N   . PRO   E  335 ? 0.74607 0.74607 0.74607 0.00000  0.00000  0.00000  335 PRO   A N   
8253  C CA  . PRO   E  335 ? 0.49032 0.49032 0.49032 -0.00000 0.00000  -0.00000 335 PRO   A CA  
8254  C C   . PRO   E  335 ? 0.28805 0.28805 0.28805 0.00000  0.00000  0.00000  335 PRO   A C   
8255  O O   . PRO   E  335 ? 0.65460 0.65460 0.65460 -0.00000 0.00000  0.00000  335 PRO   A O   
8256  C CB  . PRO   E  335 ? 0.56350 0.56350 0.56350 -0.00000 0.00000  0.00000  335 PRO   A CB  
8257  C CG  . PRO   E  335 ? 0.72639 0.72639 0.72639 0.00000  0.00000  -0.00000 335 PRO   A CG  
8258  C CD  . PRO   E  335 ? 0.39172 0.39172 0.39172 0.00000  0.00000  0.00000  335 PRO   A CD  
8259  N N   . PRO   E  336 ? 0.68168 0.68168 0.68168 -0.00000 0.00000  0.00000  336 PRO   A N   
8260  C CA  . PRO   E  336 ? 0.23100 0.23100 0.23100 -0.00000 0.00000  0.00000  336 PRO   A CA  
8261  C C   . PRO   E  336 ? 1.07060 1.07060 1.07060 -0.00000 0.00000  0.00000  336 PRO   A C   
8262  O O   . PRO   E  336 ? 0.29886 0.29886 0.29886 0.00000  0.00000  0.00000  336 PRO   A O   
8263  C CB  . PRO   E  336 ? 0.47142 0.47142 0.47142 0.00000  0.00000  0.00000  336 PRO   A CB  
8264  C CG  . PRO   E  336 ? 0.43313 0.43313 0.43313 0.00000  0.00000  0.00000  336 PRO   A CG  
8265  C CD  . PRO   E  336 ? 0.23078 0.23078 0.23078 0.00000  0.00000  0.00000  336 PRO   A CD  
8266  N N   . PRO   E  337 ? 0.31845 0.31845 0.31845 0.00000  0.00000  0.00000  337 PRO   A N   
8267  C CA  . PRO   E  337 ? 0.51618 0.51618 0.51618 0.00000  0.00000  0.00000  337 PRO   A CA  
8268  C C   . PRO   E  337 ? 0.37121 0.37121 0.37121 0.00000  0.00000  0.00000  337 PRO   A C   
8269  O O   . PRO   E  337 ? 0.34392 0.34392 0.34392 0.00000  0.00000  0.00000  337 PRO   A O   
8270  C CB  . PRO   E  337 ? 0.34548 0.34548 0.34548 -0.00000 0.00000  0.00000  337 PRO   A CB  
8271  C CG  . PRO   E  337 ? 0.45165 0.45165 0.45165 0.00000  0.00000  0.00000  337 PRO   A CG  
8272  C CD  . PRO   E  337 ? 0.56152 0.56152 0.56152 0.00000  0.00000  0.00000  337 PRO   A CD  
8273  N N   . TYR   E  338 ? 0.38860 0.38860 0.38860 0.00000  0.00000  0.00000  338 TYR   A N   
8274  C CA  . TYR   E  338 ? 0.42134 0.42134 0.42134 -0.00000 0.00000  0.00000  338 TYR   A CA  
8275  C C   . TYR   E  338 ? 0.34297 0.34297 0.34297 -0.00000 0.00000  0.00000  338 TYR   A C   
8276  O O   . TYR   E  338 ? 0.35979 0.35979 0.35979 0.00000  0.00000  0.00000  338 TYR   A O   
8277  C CB  . TYR   E  338 ? 0.26325 0.26325 0.26325 -0.00000 0.00000  0.00000  338 TYR   A CB  
8278  C CG  . TYR   E  338 ? 0.42887 0.42887 0.42887 0.00000  0.00000  0.00000  338 TYR   A CG  
8279  C CD1 . TYR   E  338 ? 0.33676 0.33676 0.33676 0.00000  0.00000  0.00000  338 TYR   A CD1 
8280  C CD2 . TYR   E  338 ? 0.30941 0.30941 0.30941 0.00000  0.00000  0.00000  338 TYR   A CD2 
8281  C CE1 . TYR   E  338 ? 0.37111 0.37111 0.37111 0.00000  0.00000  0.00000  338 TYR   A CE1 
8282  C CE2 . TYR   E  338 ? 0.23226 0.23226 0.23226 0.00000  0.00000  0.00000  338 TYR   A CE2 
8283  C CZ  . TYR   E  338 ? 0.48867 0.48867 0.48867 -0.00000 0.00000  0.00000  338 TYR   A CZ  
8284  O OH  . TYR   E  338 ? 0.34363 0.34363 0.34363 -0.00000 0.00000  0.00000  338 TYR   A OH  
8285  N N   . LEU   E  339 ? 0.40618 0.40618 0.40618 0.00000  0.00000  0.00000  339 LEU   A N   
8286  C CA  . LEU   E  339 ? 0.29423 0.29423 0.29423 0.00000  0.00000  0.00000  339 LEU   A CA  
8287  C C   . LEU   E  339 ? 0.44603 0.44603 0.44603 0.00000  0.00000  0.00000  339 LEU   A C   
8288  O O   . LEU   E  339 ? 0.46745 0.46745 0.46745 0.00000  0.00000  0.00000  339 LEU   A O   
8289  C CB  . LEU   E  339 ? 0.30466 0.30466 0.30466 0.00000  0.00000  0.00000  339 LEU   A CB  
8290  C CG  . LEU   E  339 ? 0.58348 0.58348 0.58348 0.00000  0.00000  0.00000  339 LEU   A CG  
8291  C CD1 . LEU   E  339 ? 0.37863 0.37863 0.37863 0.00000  0.00000  0.00000  339 LEU   A CD1 
8292  C CD2 . LEU   E  339 ? 0.39578 0.39578 0.39578 0.00000  0.00000  0.00000  339 LEU   A CD2 
8293  N N   . LYS   E  340 ? 0.25945 0.25945 0.25945 0.00000  0.00000  0.00000  340 LYS   A N   
8294  C CA  . LYS   E  340 ? 0.51046 0.51046 0.51046 -0.00000 0.00000  0.00000  340 LYS   A CA  
8295  C C   . LYS   E  340 ? 0.28517 0.28517 0.28517 0.00000  0.00000  0.00000  340 LYS   A C   
8296  O O   . LYS   E  340 ? 0.36612 0.36612 0.36612 0.00000  0.00000  0.00000  340 LYS   A O   
8297  C CB  . LYS   E  340 ? 0.29341 0.29341 0.29341 -0.00000 0.00000  0.00000  340 LYS   A CB  
8298  C CG  . LYS   E  340 ? 0.25520 0.25520 0.25520 -0.00000 0.00000  0.00000  340 LYS   A CG  
8299  C CD  . LYS   E  340 ? 0.83965 0.83965 0.83965 -0.00000 0.00000  0.00000  340 LYS   A CD  
8300  C CE  . LYS   E  340 ? 0.83376 0.83376 0.83376 0.00000  0.00000  0.00000  340 LYS   A CE  
8301  N NZ  . LYS   E  340 ? 0.87015 0.87015 0.87015 -0.00000 0.00000  0.00000  340 LYS   A NZ  
8302  N N   . SER   E  341 ? 0.34126 0.34126 0.34126 0.00000  0.00000  0.00000  341 SER   A N   
8303  C CA  . SER   E  341 ? 0.25456 0.25456 0.25456 -0.00000 0.00000  0.00000  341 SER   A CA  
8304  C C   . SER   E  341 ? 0.31644 0.31644 0.31644 -0.00000 0.00000  0.00000  341 SER   A C   
8305  O O   . SER   E  341 ? 0.45004 0.45004 0.45004 0.00000  -0.00000 0.00000  341 SER   A O   
8306  C CB  . SER   E  341 ? 0.33746 0.33746 0.33746 -0.00000 0.00000  0.00000  341 SER   A CB  
8307  O OG  . SER   E  341 ? 0.33445 0.33445 0.33445 0.00000  0.00000  0.00000  341 SER   A OG  
8308  N N   . LEU   E  342 ? 0.35663 0.35663 0.35663 0.00000  0.00000  0.00000  342 LEU   A N   
8309  C CA  . LEU   E  342 ? 0.49834 0.49834 0.49834 -0.00000 0.00000  0.00000  342 LEU   A CA  
8310  C C   . LEU   E  342 ? 0.35399 0.35399 0.35399 0.00000  0.00000  -0.00000 342 LEU   A C   
8311  O O   . LEU   E  342 ? 0.42892 0.42892 0.42892 0.00000  0.00000  0.00000  342 LEU   A O   
8312  C CB  . LEU   E  342 ? 0.28133 0.28133 0.28133 -0.00000 0.00000  0.00000  342 LEU   A CB  
8313  C CG  . LEU   E  342 ? 0.51268 0.51268 0.51268 -0.00000 0.00000  0.00000  342 LEU   A CG  
8314  C CD1 . LEU   E  342 ? 0.26161 0.26161 0.26161 0.00000  0.00000  0.00000  342 LEU   A CD1 
8315  C CD2 . LEU   E  342 ? 0.20603 0.20603 0.20603 0.00000  0.00000  0.00000  342 LEU   A CD2 
8316  N N   . VAL   E  343 ? 0.46555 0.46555 0.46555 -0.00000 0.00000  0.00000  343 VAL   A N   
8317  C CA  . VAL   E  343 ? 0.39328 0.39328 0.39328 0.00000  0.00000  0.00000  343 VAL   A CA  
8318  C C   . VAL   E  343 ? 0.55684 0.55684 0.55684 0.00000  0.00000  0.00000  343 VAL   A C   
8319  O O   . VAL   E  343 ? 0.35836 0.35836 0.35836 0.00000  0.00000  0.00000  343 VAL   A O   
8320  C CB  . VAL   E  343 ? 0.40443 0.40443 0.40443 -0.00000 0.00000  0.00000  343 VAL   A CB  
8321  C CG1 . VAL   E  343 ? 0.22985 0.22985 0.22985 -0.00000 0.00000  0.00000  343 VAL   A CG1 
8322  C CG2 . VAL   E  343 ? 0.32291 0.32291 0.32291 0.00000  0.00000  0.00000  343 VAL   A CG2 
8323  N N   . TYR   E  344 ? 0.26587 0.26587 0.26587 -0.00000 0.00000  0.00000  344 TYR   A N   
8324  C CA  . TYR   E  344 ? 0.48695 0.48695 0.48695 0.00000  0.00000  0.00000  344 TYR   A CA  
8325  C C   . TYR   E  344 ? 0.50637 0.50637 0.50637 -0.00000 -0.00000 -0.00000 344 TYR   A C   
8326  O O   . TYR   E  344 ? 0.37953 0.37953 0.37953 0.00000  0.00000  0.00000  344 TYR   A O   
8327  C CB  . TYR   E  344 ? 0.32105 0.32105 0.32105 -0.00000 0.00000  0.00000  344 TYR   A CB  
8328  C CG  . TYR   E  344 ? 0.57922 0.57922 0.57922 -0.00000 0.00000  0.00000  344 TYR   A CG  
8329  C CD1 . TYR   E  344 ? 0.36077 0.36077 0.36077 0.00000  0.00000  0.00000  344 TYR   A CD1 
8330  C CD2 . TYR   E  344 ? 0.47761 0.47761 0.47761 0.00000  0.00000  0.00000  344 TYR   A CD2 
8331  C CE1 . TYR   E  344 ? 0.36329 0.36329 0.36329 0.00000  0.00000  0.00000  344 TYR   A CE1 
8332  C CE2 . TYR   E  344 ? 0.35185 0.35185 0.35185 0.00000  0.00000  0.00000  344 TYR   A CE2 
8333  C CZ  . TYR   E  344 ? 0.58324 0.58324 0.58324 0.00000  -0.00000 0.00000  344 TYR   A CZ  
8334  O OH  . TYR   E  344 ? 0.52042 0.52042 0.52042 0.00000  0.00000  0.00000  344 TYR   A OH  
8335  N N   . PHE   E  345 ? 0.23897 0.23897 0.23897 -0.00000 0.00000  0.00000  345 PHE   A N   
8336  C CA  . PHE   E  345 ? 0.35357 0.35357 0.35357 0.00000  0.00000  0.00000  345 PHE   A CA  
8337  C C   . PHE   E  345 ? 0.41917 0.41917 0.41917 0.00000  0.00000  0.00000  345 PHE   A C   
8338  O O   . PHE   E  345 ? 0.37286 0.37286 0.37286 0.00000  0.00000  0.00000  345 PHE   A O   
8339  C CB  . PHE   E  345 ? 0.23327 0.23327 0.23327 0.00000  0.00000  0.00000  345 PHE   A CB  
8340  C CG  . PHE   E  345 ? 0.40051 0.40051 0.40051 0.00000  0.00000  0.00000  345 PHE   A CG  
8341  C CD1 . PHE   E  345 ? 0.46650 0.46650 0.46650 0.00000  0.00000  0.00000  345 PHE   A CD1 
8342  C CD2 . PHE   E  345 ? 0.31880 0.31880 0.31880 -0.00000 0.00000  0.00000  345 PHE   A CD2 
8343  C CE1 . PHE   E  345 ? 0.26617 0.26617 0.26617 0.00000  0.00000  0.00000  345 PHE   A CE1 
8344  C CE2 . PHE   E  345 ? 0.33738 0.33738 0.33738 -0.00000 0.00000  0.00000  345 PHE   A CE2 
8345  C CZ  . PHE   E  345 ? 0.36648 0.36648 0.36648 0.00000  0.00000  0.00000  345 PHE   A CZ  
8346  N N   . SER   E  346 ? 0.21252 0.21252 0.21252 0.00000  0.00000  0.00000  346 SER   A N   
8347  C CA  . SER   E  346 ? 0.49378 0.49378 0.49378 -0.00000 0.00000  0.00000  346 SER   A CA  
8348  C C   . SER   E  346 ? 0.33385 0.33385 0.33385 0.00000  0.00000  0.00000  346 SER   A C   
8349  O O   . SER   E  346 ? 0.33388 0.33388 0.33388 -0.00000 0.00000  0.00000  346 SER   A O   
8350  C CB  . SER   E  346 ? 0.32632 0.32632 0.32632 0.00000  0.00000  0.00000  346 SER   A CB  
8351  O OG  . SER   E  346 ? 0.28334 0.28334 0.28334 0.00000  0.00000  0.00000  346 SER   A OG  
8352  N N   . ASN   E  347 ? 0.39800 0.39800 0.39800 0.00000  0.00000  0.00000  347 ASN   A N   
8353  C CA  . ASN   E  347 ? 0.15864 0.15864 0.15864 0.00000  0.00000  0.00000  347 ASN   A CA  
8354  C C   . ASN   E  347 ? 0.37233 0.37233 0.37233 0.00000  0.00000  0.00000  347 ASN   A C   
8355  O O   . ASN   E  347 ? 0.37667 0.37667 0.37667 0.00000  0.00000  0.00000  347 ASN   A O   
8356  C CB  . ASN   E  347 ? 0.25389 0.25389 0.25389 0.00000  0.00000  0.00000  347 ASN   A CB  
8357  C CG  . ASN   E  347 ? 0.44570 0.44570 0.44570 -0.00000 0.00000  0.00000  347 ASN   A CG  
8358  O OD1 . ASN   E  347 ? 0.33343 0.33343 0.33343 -0.00000 0.00000  0.00000  347 ASN   A OD1 
8359  N ND2 . ASN   E  347 ? 0.21604 0.21604 0.21604 0.00000  -0.00000 0.00000  347 ASN   A ND2 
8360  N N   . ILE   E  348 ? 0.34121 0.34121 0.34121 0.00000  0.00000  0.00000  348 ILE   A N   
8361  C CA  . ILE   E  348 ? 0.25250 0.25250 0.25250 0.00000  0.00000  0.00000  348 ILE   A CA  
8362  C C   . ILE   E  348 ? 0.39282 0.39282 0.39282 0.00000  0.00000  0.00000  348 ILE   A C   
8363  O O   . ILE   E  348 ? 0.43679 0.43679 0.43679 0.00000  0.00000  0.00000  348 ILE   A O   
8364  C CB  . ILE   E  348 ? 0.36627 0.36627 0.36627 0.00000  0.00000  0.00000  348 ILE   A CB  
8365  C CG1 . ILE   E  348 ? 0.22101 0.22101 0.22101 0.00000  0.00000  0.00000  348 ILE   A CG1 
8366  C CG2 . ILE   E  348 ? 0.19450 0.19450 0.19450 -0.00000 0.00000  0.00000  348 ILE   A CG2 
8367  C CD1 . ILE   E  348 ? 0.50666 0.50666 0.50666 0.00000  0.00000  0.00000  348 ILE   A CD1 
8368  N N   . ALA   E  349 ? 0.33698 0.33698 0.33698 -0.00000 0.00000  0.00000  349 ALA   A N   
8369  C CA  . ALA   E  349 ? 0.34284 0.34284 0.34284 -0.00000 0.00000  0.00000  349 ALA   A CA  
8370  C C   . ALA   E  349 ? 0.38314 0.38314 0.38314 0.00000  -0.00000 -0.00000 349 ALA   A C   
8371  O O   . ALA   E  349 ? 0.44565 0.44565 0.44565 -0.00000 0.00000  0.00000  349 ALA   A O   
8372  C CB  . ALA   E  349 ? 0.15540 0.15540 0.15540 0.00000  0.00000  0.00000  349 ALA   A CB  
8373  N N   . ALA   E  350 ? 0.30293 0.30293 0.30293 0.00000  0.00000  0.00000  350 ALA   A N   
8374  C CA  . ALA   E  350 ? 0.33442 0.33442 0.33442 0.00000  0.00000  0.00000  350 ALA   A CA  
8375  C C   . ALA   E  350 ? 0.40964 0.40964 0.40964 0.00000  0.00000  0.00000  350 ALA   A C   
8376  O O   . ALA   E  350 ? 0.32769 0.32769 0.32769 -0.00000 0.00000  0.00000  350 ALA   A O   
8377  C CB  . ALA   E  350 ? 0.15550 0.15550 0.15550 0.00000  0.00000  0.00000  350 ALA   A CB  
8378  N N   . ARG   E  351 ? 0.22521 0.22521 0.22521 -0.00000 0.00000  0.00000  351 ARG   A N   
8379  C CA  . ARG   E  351 ? 0.35508 0.35508 0.35508 -0.00000 0.00000  -0.00000 351 ARG   A CA  
8380  C C   . ARG   E  351 ? 0.25803 0.25803 0.25803 0.00000  0.00000  0.00000  351 ARG   A C   
8381  O O   . ARG   E  351 ? 0.43832 0.43832 0.43832 0.00000  0.00000  0.00000  351 ARG   A O   
8382  C CB  . ARG   E  351 ? 0.17423 0.17423 0.17423 -0.00000 0.00000  0.00000  351 ARG   A CB  
8383  C CG  . ARG   E  351 ? 0.17430 0.17430 0.17430 -0.00000 0.00000  0.00000  351 ARG   A CG  
8384  C CD  . ARG   E  351 ? 0.27455 0.27455 0.27455 0.00000  0.00000  0.00000  351 ARG   A CD  
8385  N NE  . ARG   E  351 ? 0.29435 0.29435 0.29435 0.00000  0.00000  0.00000  351 ARG   A NE  
8386  C CZ  . ARG   E  351 ? 0.56693 0.56693 0.56693 0.00000  0.00000  0.00000  351 ARG   A CZ  
8387  N NH1 . ARG   E  351 ? 0.29778 0.29778 0.29778 0.00000  0.00000  0.00000  351 ARG   A NH1 
8388  N NH2 . ARG   E  351 ? 0.23910 0.23910 0.23910 0.00000  0.00000  0.00000  351 ARG   A NH2 
8389  N N   . GLN   E  352 ? 0.32267 0.32267 0.32267 0.00000  0.00000  0.00000  352 GLN   A N   
8390  C CA  . GLN   E  352 ? 0.23857 0.23857 0.23857 0.00000  0.00000  0.00000  352 GLN   A CA  
8391  C C   . GLN   E  352 ? 0.39278 0.39278 0.39278 0.00000  0.00000  0.00000  352 GLN   A C   
8392  O O   . GLN   E  352 ? 0.37858 0.37858 0.37858 0.00000  0.00000  0.00000  352 GLN   A O   
8393  C CB  . GLN   E  352 ? 0.36731 0.36731 0.36731 0.00000  0.00000  0.00000  352 GLN   A CB  
8394  C CG  . GLN   E  352 ? 0.30466 0.30466 0.30466 0.00000  0.00000  0.00000  352 GLN   A CG  
8395  C CD  . GLN   E  352 ? 0.41037 0.41037 0.41037 0.00000  0.00000  0.00000  352 GLN   A CD  
8396  O OE1 . GLN   E  352 ? 0.43645 0.43645 0.43645 0.00000  -0.00000 0.00000  352 GLN   A OE1 
8397  N NE2 . GLN   E  352 ? 0.27315 0.27315 0.27315 0.00000  0.00000  0.00000  352 GLN   A NE2 
8398  N N   . ILE   E  353 ? 0.31912 0.31912 0.31912 -0.00000 0.00000  0.00000  353 ILE   A N   
8399  C CA  . ILE   E  353 ? 0.35487 0.35487 0.35487 0.00000  0.00000  0.00000  353 ILE   A CA  
8400  C C   . ILE   E  353 ? 0.26643 0.26643 0.26643 0.00000  0.00000  0.00000  353 ILE   A C   
8401  O O   . ILE   E  353 ? 0.44489 0.44489 0.44489 0.00000  0.00000  0.00000  353 ILE   A O   
8402  C CB  . ILE   E  353 ? 0.32830 0.32830 0.32830 0.00000  0.00000  0.00000  353 ILE   A CB  
8403  C CG1 . ILE   E  353 ? 0.42002 0.42002 0.42002 -0.00000 0.00000  0.00000  353 ILE   A CG1 
8404  C CG2 . ILE   E  353 ? 0.21259 0.21259 0.21259 0.00000  0.00000  0.00000  353 ILE   A CG2 
8405  C CD1 . ILE   E  353 ? 0.16889 0.16889 0.16889 -0.00000 0.00000  0.00000  353 ILE   A CD1 
8406  N N   . MET   E  354 ? 0.25708 0.25708 0.25708 0.00000  0.00000  0.00000  354 MET   A N   
8407  C CA  . MET   E  354 ? 0.32429 0.32429 0.32429 0.00000  0.00000  0.00000  354 MET   A CA  
8408  C C   . MET   E  354 ? 0.38881 0.38881 0.38881 -0.00000 0.00000  0.00000  354 MET   A C   
8409  O O   . MET   E  354 ? 0.40743 0.40743 0.40743 0.00000  0.00000  0.00000  354 MET   A O   
8410  C CB  . MET   E  354 ? 0.18518 0.18518 0.18518 0.00000  -0.00000 0.00000  354 MET   A CB  
8411  C CG  . MET   E  354 ? 0.46182 0.46182 0.46182 0.00000  0.00000  0.00000  354 MET   A CG  
8412  S SD  . MET   E  354 ? 0.42685 0.42685 0.42685 -0.00000 0.00000  0.00000  354 MET   A SD  
8413  C CE  . MET   E  354 ? 0.40413 0.40413 0.40413 -0.00000 0.00000  0.00000  354 MET   A CE  
8414  N N   . PHE   E  355 ? 0.41479 0.41479 0.41479 0.00000  0.00000  0.00000  355 PHE   A N   
8415  C CA  . PHE   E  355 ? 0.43545 0.43545 0.43545 0.00000  -0.00000 0.00000  355 PHE   A CA  
8416  C C   . PHE   E  355 ? 0.41949 0.41949 0.41949 0.00000  0.00000  0.00000  355 PHE   A C   
8417  O O   . PHE   E  355 ? 0.47789 0.47789 0.47789 -0.00000 0.00000  0.00000  355 PHE   A O   
8418  C CB  . PHE   E  355 ? 0.48431 0.48431 0.48431 0.00000  0.00000  0.00000  355 PHE   A CB  
8419  C CG  . PHE   E  355 ? 0.50786 0.50786 0.50786 -0.00000 0.00000  0.00000  355 PHE   A CG  
8420  C CD1 . PHE   E  355 ? 0.34377 0.34377 0.34377 -0.00000 0.00000  0.00000  355 PHE   A CD1 
8421  C CD2 . PHE   E  355 ? 0.45388 0.45388 0.45388 -0.00000 0.00000  0.00000  355 PHE   A CD2 
8422  C CE1 . PHE   E  355 ? 0.50687 0.50687 0.50687 -0.00000 0.00000  0.00000  355 PHE   A CE1 
8423  C CE2 . PHE   E  355 ? 0.29132 0.29132 0.29132 0.00000  0.00000  0.00000  355 PHE   A CE2 
8424  C CZ  . PHE   E  355 ? 0.31106 0.31106 0.31106 0.00000  0.00000  0.00000  355 PHE   A CZ  
8425  N N   . ILE   E  356 ? 0.39515 0.39515 0.39515 0.00000  0.00000  0.00000  356 ILE   A N   
8426  C CA  . ILE   E  356 ? 0.43769 0.43769 0.43769 0.00000  0.00000  0.00000  356 ILE   A CA  
8427  C C   . ILE   E  356 ? 0.60158 0.60158 0.60158 0.00000  0.00000  0.00000  356 ILE   A C   
8428  O O   . ILE   E  356 ? 0.43365 0.43365 0.43365 0.00000  0.00000  0.00000  356 ILE   A O   
8429  C CB  . ILE   E  356 ? 0.36273 0.36273 0.36273 0.00000  0.00000  0.00000  356 ILE   A CB  
8430  C CG1 . ILE   E  356 ? 0.35386 0.35386 0.35386 0.00000  0.00000  0.00000  356 ILE   A CG1 
8431  C CG2 . ILE   E  356 ? 0.40121 0.40121 0.40121 0.00000  0.00000  0.00000  356 ILE   A CG2 
8432  C CD1 . ILE   E  356 ? 0.27920 0.27920 0.27920 0.00000  0.00000  -0.00000 356 ILE   A CD1 
8433  N N   . GLU   E  357 ? 0.27303 0.27303 0.27303 -0.00000 0.00000  0.00000  357 GLU   A N   
8434  C CA  . GLU   E  357 ? 0.46291 0.46291 0.46291 0.00000  -0.00000 0.00000  357 GLU   A CA  
8435  C C   . GLU   E  357 ? 0.44019 0.44019 0.44019 0.00000  0.00000  0.00000  357 GLU   A C   
8436  O O   . GLU   E  357 ? 0.42357 0.42357 0.42357 -0.00000 0.00000  0.00000  357 GLU   A O   
8437  C CB  . GLU   E  357 ? 0.34279 0.34279 0.34279 -0.00000 0.00000  0.00000  357 GLU   A CB  
8438  C CG  . GLU   E  357 ? 0.32734 0.32734 0.32734 0.00000  0.00000  0.00000  357 GLU   A CG  
8439  C CD  . GLU   E  357 ? 1.00239 1.00239 1.00239 0.00000  0.00000  0.00000  357 GLU   A CD  
8440  O OE1 . GLU   E  357 ? 0.78112 0.78112 0.78112 0.00000  0.00000  0.00000  357 GLU   A OE1 
8441  O OE2 . GLU   E  357 ? 0.61748 0.61748 0.61748 -0.00000 0.00000  0.00000  357 GLU   A OE2 
8442  N N   . ALA   E  358 ? 0.24211 0.24211 0.24211 0.00000  0.00000  0.00000  358 ALA   A N   
8443  C CA  . ALA   E  358 ? 0.48099 0.48099 0.48099 0.00000  0.00000  0.00000  358 ALA   A CA  
8444  C C   . ALA   E  358 ? 0.41042 0.41042 0.41042 -0.00000 0.00000  0.00000  358 ALA   A C   
8445  O O   . ALA   E  358 ? 0.73964 0.73964 0.73964 0.00000  0.00000  0.00000  358 ALA   A O   
8446  C CB  . ALA   E  358 ? 0.33712 0.33712 0.33712 0.00000  -0.00000 0.00000  358 ALA   A CB  
8447  N N   . ASP   E  359 ? 0.59698 0.59698 0.59698 0.00000  0.00000  0.00000  359 ASP   A N   
8448  C CA  . ASP   E  359 ? 0.53760 0.53760 0.53760 -0.00000 0.00000  0.00000  359 ASP   A CA  
8449  C C   . ASP   E  359 ? 0.31157 0.31157 0.31157 -0.00000 0.00000  0.00000  359 ASP   A C   
8450  O O   . ASP   E  359 ? 0.39723 0.39723 0.39723 0.00000  0.00000  0.00000  359 ASP   A O   
8451  C CB  . ASP   E  359 ? 0.27243 0.27243 0.27243 0.00000  0.00000  -0.00000 359 ASP   A CB  
8452  C CG  . ASP   E  359 ? 0.74470 0.74470 0.74470 0.00000  0.00000  0.00000  359 ASP   A CG  
8453  O OD1 . ASP   E  359 ? 0.49171 0.49171 0.49171 -0.00000 0.00000  0.00000  359 ASP   A OD1 
8454  O OD2 . ASP   E  359 ? 0.41205 0.41205 0.41205 -0.00000 0.00000  0.00000  359 ASP   A OD2 
8455  N N   . ASN   E  360 ? 0.45497 0.45497 0.45497 -0.00000 0.00000  0.00000  360 ASN   A N   
8456  C CA  . ASN   E  360 ? 0.34418 0.34418 0.34418 0.00000  0.00000  0.00000  360 ASN   A CA  
8457  C C   . ASN   E  360 ? 0.48305 0.48305 0.48305 0.00000  0.00000  0.00000  360 ASN   A C   
8458  O O   . ASN   E  360 ? 0.61822 0.61822 0.61822 -0.00000 0.00000  0.00000  360 ASN   A O   
8459  C CB  . ASN   E  360 ? 0.36040 0.36040 0.36040 0.00000  0.00000  0.00000  360 ASN   A CB  
8460  C CG  . ASN   E  360 ? 0.59832 0.59832 0.59832 -0.00000 0.00000  0.00000  360 ASN   A CG  
8461  O OD1 . ASN   E  360 ? 0.63764 0.63764 0.63764 0.00000  0.00000  0.00000  360 ASN   A OD1 
8462  N ND2 . ASN   E  360 ? 0.67385 0.67385 0.67385 0.00000  0.00000  0.00000  360 ASN   A ND2 
8463  N N   . LYS   E  361 ? 0.52572 0.52572 0.52572 -0.00000 0.00000  0.00000  361 LYS   A N   
8464  C CA  . LYS   E  361 ? 0.62412 0.62412 0.62412 -0.00000 0.00000  0.00000  361 LYS   A CA  
8465  C C   . LYS   E  361 ? 0.27351 0.27351 0.27351 0.00000  0.00000  0.00000  361 LYS   A C   
8466  O O   . LYS   E  361 ? 0.91162 0.91162 0.91162 0.00000  0.00000  0.00000  361 LYS   A O   
8467  C CB  . LYS   E  361 ? 0.32615 0.32615 0.32615 0.00000  0.00000  0.00000  361 LYS   A CB  
8468  C CG  . LYS   E  361 ? 0.87442 0.87442 0.87442 0.00000  0.00000  0.00000  361 LYS   A CG  
8469  C CD  . LYS   E  361 ? 0.21420 0.21420 0.21420 -0.00000 0.00000  0.00000  361 LYS   A CD  
8470  C CE  . LYS   E  361 ? 1.17034 1.17034 1.17034 -0.00000 0.00000  0.00000  361 LYS   A CE  
8471  N NZ  . LYS   E  361 ? 1.21598 1.21598 1.21598 0.00000  0.00000  0.00000  361 LYS   A NZ  
8472  N N   . GLU   E  362 ? 0.54480 0.54480 0.54480 0.00000  0.00000  0.00000  362 GLU   A N   
8473  C CA  . GLU   E  362 ? 0.48735 0.48735 0.48735 0.00000  0.00000  0.00000  362 GLU   A CA  
8474  C C   . GLU   E  362 ? 0.74423 0.74423 0.74423 0.00000  0.00000  0.00000  362 GLU   A C   
8475  O O   . GLU   E  362 ? 0.64623 0.64623 0.64623 -0.00000 0.00000  0.00000  362 GLU   A O   
8476  C CB  . GLU   E  362 ? 0.59955 0.59955 0.59955 0.00000  0.00000  0.00000  362 GLU   A CB  
8477  N N   . ILE   E  363 ? 0.47439 0.47439 0.47439 -0.00000 0.00000  0.00000  363 ILE   A N   
8478  C CA  . ILE   E  363 ? 0.70196 0.70196 0.70196 -0.00000 0.00000  0.00000  363 ILE   A CA  
8479  C C   . ILE   E  363 ? 0.55621 0.55621 0.55621 0.00000  0.00000  -0.00000 363 ILE   A C   
8480  O O   . ILE   E  363 ? 0.66200 0.66200 0.66200 0.00000  0.00000  0.00000  363 ILE   A O   
8481  C CB  . ILE   E  363 ? 0.57831 0.57831 0.57831 0.00000  0.00000  0.00000  363 ILE   A CB  
8482  C CG1 . ILE   E  363 ? 0.50114 0.50114 0.50114 0.00000  0.00000  0.00000  363 ILE   A CG1 
8483  C CG2 . ILE   E  363 ? 0.32226 0.32226 0.32226 0.00000  0.00000  0.00000  363 ILE   A CG2 
8484  C CD1 . ILE   E  363 ? 0.54422 0.54422 0.54422 0.00000  0.00000  0.00000  363 ILE   A CD1 
8485  N N   . GLY   E  364 ? 0.46693 0.46693 0.46693 0.00000  0.00000  0.00000  364 GLY   A N   
8486  C CA  . GLY   E  364 ? 0.31362 0.31362 0.31362 0.00000  0.00000  0.00000  364 GLY   A CA  
8487  C C   . GLY   E  364 ? 0.88663 0.88663 0.88663 0.00000  0.00000  0.00000  364 GLY   A C   
8488  O O   . GLY   E  364 ? 0.43817 0.43817 0.43817 0.00000  0.00000  0.00000  364 GLY   A O   
8489  N N   . LEU   E  365 ? 0.55837 0.55837 0.55837 -0.00000 0.00000  0.00000  365 LEU   A N   
8490  C CA  . LEU   E  365 ? 0.26565 0.26565 0.26565 0.00000  0.00000  0.00000  365 LEU   A CA  
8491  C C   . LEU   E  365 ? 0.57792 0.57792 0.57792 0.00000  0.00000  0.00000  365 LEU   A C   
8492  O O   . LEU   E  365 ? 0.41709 0.41709 0.41709 0.00000  0.00000  0.00000  365 LEU   A O   
8493  C CB  . LEU   E  365 ? 0.44427 0.44427 0.44427 0.00000  0.00000  0.00000  365 LEU   A CB  
8494  C CG  . LEU   E  365 ? 0.48933 0.48933 0.48933 0.00000  0.00000  0.00000  365 LEU   A CG  
8495  C CD1 . LEU   E  365 ? 0.32766 0.32766 0.32766 0.00000  0.00000  0.00000  365 LEU   A CD1 
8496  C CD2 . LEU   E  365 ? 0.31546 0.31546 0.31546 0.00000  0.00000  0.00000  365 LEU   A CD2 
8497  N N   . ILE   E  366 ? 0.27256 0.27256 0.27256 0.00000  0.00000  0.00000  366 ILE   A N   
8498  C CA  . ILE   E  366 ? 0.45403 0.45403 0.45403 0.00000  0.00000  0.00000  366 ILE   A CA  
8499  C C   . ILE   E  366 ? 0.48331 0.48331 0.48331 0.00000  0.00000  0.00000  366 ILE   A C   
8500  O O   . ILE   E  366 ? 0.42662 0.42662 0.42662 -0.00000 0.00000  0.00000  366 ILE   A O   
8501  C CB  . ILE   E  366 ? 0.36996 0.36996 0.36996 0.00000  0.00000  0.00000  366 ILE   A CB  
8502  C CG1 . ILE   E  366 ? 0.41459 0.41459 0.41459 0.00000  0.00000  0.00000  366 ILE   A CG1 
8503  C CG2 . ILE   E  366 ? 0.26792 0.26792 0.26792 0.00000  -0.00000 0.00000  366 ILE   A CG2 
8504  C CD1 . ILE   E  366 ? 0.42435 0.42435 0.42435 0.00000  0.00000  0.00000  366 ILE   A CD1 
8505  N N   . PHE   E  367 ? 0.36018 0.36018 0.36018 -0.00000 0.00000  0.00000  367 PHE   A N   
8506  C CA  . PHE   E  367 ? 0.32179 0.32179 0.32179 0.00000  0.00000  0.00000  367 PHE   A CA  
8507  C C   . PHE   E  367 ? 0.43925 0.43925 0.43925 0.00000  0.00000  0.00000  367 PHE   A C   
8508  O O   . PHE   E  367 ? 0.38234 0.38234 0.38234 0.00000  0.00000  0.00000  367 PHE   A O   
8509  C CB  . PHE   E  367 ? 0.30872 0.30872 0.30872 0.00000  0.00000  0.00000  367 PHE   A CB  
8510  C CG  . PHE   E  367 ? 0.20746 0.20746 0.20746 0.00000  0.00000  0.00000  367 PHE   A CG  
8511  C CD1 . PHE   E  367 ? 0.41381 0.41381 0.41381 0.00000  0.00000  0.00000  367 PHE   A CD1 
8512  C CD2 . PHE   E  367 ? 0.35237 0.35237 0.35237 0.00000  0.00000  0.00000  367 PHE   A CD2 
8513  C CE1 . PHE   E  367 ? 0.21314 0.21314 0.21314 -0.00000 0.00000  0.00000  367 PHE   A CE1 
8514  C CE2 . PHE   E  367 ? 0.32781 0.32781 0.32781 0.00000  0.00000  0.00000  367 PHE   A CE2 
8515  C CZ  . PHE   E  367 ? 0.28630 0.28630 0.28630 0.00000  0.00000  0.00000  367 PHE   A CZ  
8516  N N   . LEU   E  368 ? 0.31198 0.31198 0.31198 0.00000  0.00000  0.00000  368 LEU   A N   
8517  C CA  . LEU   E  368 ? 0.19744 0.19744 0.19744 -0.00000 0.00000  0.00000  368 LEU   A CA  
8518  C C   . LEU   E  368 ? 0.20692 0.20692 0.20692 0.00000  0.00000  0.00000  368 LEU   A C   
8519  O O   . LEU   E  368 ? 0.31473 0.31473 0.31473 0.00000  0.00000  0.00000  368 LEU   A O   
8520  C CB  . LEU   E  368 ? 0.16786 0.16786 0.16786 0.00000  -0.00000 0.00000  368 LEU   A CB  
8521  C CG  . LEU   E  368 ? 0.30207 0.30207 0.30207 0.00000  0.00000  0.00000  368 LEU   A CG  
8522  C CD1 . LEU   E  368 ? 0.24863 0.24863 0.24863 -0.00000 0.00000  0.00000  368 LEU   A CD1 
8523  C CD2 . LEU   E  368 ? 0.26958 0.26958 0.26958 0.00000  0.00000  0.00000  368 LEU   A CD2 
8524  N N   . VAL   E  369 ? 0.27698 0.27698 0.27698 0.00000  0.00000  0.00000  369 VAL   A N   
8525  C CA  . VAL   E  369 ? 0.30661 0.30661 0.30661 0.00000  0.00000  0.00000  369 VAL   A CA  
8526  C C   . VAL   E  369 ? 0.27475 0.27475 0.27475 0.00000  0.00000  0.00000  369 VAL   A C   
8527  O O   . VAL   E  369 ? 0.39440 0.39440 0.39440 0.00000  0.00000  0.00000  369 VAL   A O   
8528  C CB  . VAL   E  369 ? 0.38554 0.38554 0.38554 0.00000  0.00000  0.00000  369 VAL   A CB  
8529  C CG1 . VAL   E  369 ? 0.25594 0.25594 0.25594 -0.00000 0.00000  0.00000  369 VAL   A CG1 
8530  C CG2 . VAL   E  369 ? 0.34958 0.34958 0.34958 -0.00000 0.00000  0.00000  369 VAL   A CG2 
8531  N N   . PHE   E  370 ? 0.38777 0.38777 0.38777 0.00000  0.00000  0.00000  370 PHE   A N   
8532  C CA  . PHE   E  370 ? 0.15530 0.15530 0.15530 0.00000  0.00000  0.00000  370 PHE   A CA  
8533  C C   . PHE   E  370 ? 0.33060 0.33060 0.33060 0.00000  0.00000  0.00000  370 PHE   A C   
8534  O O   . PHE   E  370 ? 0.30809 0.30809 0.30809 0.00000  0.00000  0.00000  370 PHE   A O   
8535  C CB  . PHE   E  370 ? 0.25008 0.25008 0.25008 0.00000  0.00000  0.00000  370 PHE   A CB  
8536  C CG  . PHE   E  370 ? 0.37683 0.37683 0.37683 0.00000  0.00000  0.00000  370 PHE   A CG  
8537  C CD1 . PHE   E  370 ? 0.25683 0.25683 0.25683 0.00000  0.00000  0.00000  370 PHE   A CD1 
8538  C CD2 . PHE   E  370 ? 0.43746 0.43746 0.43746 -0.00000 0.00000  0.00000  370 PHE   A CD2 
8539  C CE1 . PHE   E  370 ? 0.38549 0.38549 0.38549 0.00000  0.00000  0.00000  370 PHE   A CE1 
8540  C CE2 . PHE   E  370 ? 0.23966 0.23966 0.23966 0.00000  0.00000  0.00000  370 PHE   A CE2 
8541  C CZ  . PHE   E  370 ? 0.37908 0.37908 0.37908 0.00000  0.00000  0.00000  370 PHE   A CZ  
8542  N N   . ILE   E  371 ? 0.39420 0.39420 0.39420 -0.00000 0.00000  0.00000  371 ILE   A N   
8543  C CA  . ILE   E  371 ? 0.34073 0.34073 0.34073 0.00000  0.00000  0.00000  371 ILE   A CA  
8544  C C   . ILE   E  371 ? 0.35238 0.35238 0.35238 -0.00000 0.00000  0.00000  371 ILE   A C   
8545  O O   . ILE   E  371 ? 0.47786 0.47786 0.47786 0.00000  0.00000  -0.00000 371 ILE   A O   
8546  C CB  . ILE   E  371 ? 0.45618 0.45618 0.45618 0.00000  0.00000  0.00000  371 ILE   A CB  
8547  C CG1 . ILE   E  371 ? 0.32431 0.32431 0.32431 0.00000  0.00000  0.00000  371 ILE   A CG1 
8548  C CG2 . ILE   E  371 ? 0.27219 0.27219 0.27219 0.00000  0.00000  0.00000  371 ILE   A CG2 
8549  C CD1 . ILE   E  371 ? 0.29730 0.29730 0.29730 0.00000  -0.00000 0.00000  371 ILE   A CD1 
8550  N N   . GLY   E  372 ? 0.34079 0.34079 0.34079 0.00000  0.00000  -0.00000 372 GLY   A N   
8551  C CA  . GLY   E  372 ? 0.23058 0.23058 0.23058 0.00000  -0.00000 0.00000  372 GLY   A CA  
8552  C C   . GLY   E  372 ? 0.33606 0.33606 0.33606 0.00000  0.00000  0.00000  372 GLY   A C   
8553  O O   . GLY   E  372 ? 0.33824 0.33824 0.33824 -0.00000 0.00000  0.00000  372 GLY   A O   
8554  N N   . MET   E  373 ? 0.29984 0.29984 0.29984 -0.00000 0.00000  0.00000  373 MET   A N   
8555  C CA  . MET   E  373 ? 0.46494 0.46494 0.46494 0.00000  0.00000  0.00000  373 MET   A CA  
8556  C C   . MET   E  373 ? 0.43647 0.43647 0.43647 0.00000  0.00000  0.00000  373 MET   A C   
8557  O O   . MET   E  373 ? 0.37684 0.37684 0.37684 0.00000  0.00000  0.00000  373 MET   A O   
8558  C CB  . MET   E  373 ? 0.21168 0.21168 0.21168 0.00000  0.00000  0.00000  373 MET   A CB  
8559  C CG  . MET   E  373 ? 0.48809 0.48809 0.48809 0.00000  -0.00000 0.00000  373 MET   A CG  
8560  S SD  . MET   E  373 ? 0.40589 0.40589 0.40589 0.00000  0.00000  0.00000  373 MET   A SD  
8561  C CE  . MET   E  373 ? 0.09916 0.09916 0.09916 0.00000  0.00000  0.00000  373 MET   A CE  
8562  N N   . THR   E  374 ? 0.29651 0.29651 0.29651 -0.00000 0.00000  0.00000  374 THR   A N   
8563  C CA  . THR   E  374 ? 0.31388 0.31388 0.31388 -0.00000 0.00000  0.00000  374 THR   A CA  
8564  C C   . THR   E  374 ? 0.27473 0.27473 0.27473 -0.00000 0.00000  0.00000  374 THR   A C   
8565  O O   . THR   E  374 ? 0.40925 0.40925 0.40925 -0.00000 0.00000  0.00000  374 THR   A O   
8566  C CB  . THR   E  374 ? 0.42758 0.42758 0.42758 0.00000  0.00000  0.00000  374 THR   A CB  
8567  O OG1 . THR   E  374 ? 0.36366 0.36366 0.36366 0.00000  0.00000  0.00000  374 THR   A OG1 
8568  C CG2 . THR   E  374 ? 0.23220 0.23220 0.23220 -0.00000 0.00000  0.00000  374 THR   A CG2 
8569  N N   . GLU   E  375 ? 0.41043 0.41043 0.41043 0.00000  0.00000  0.00000  375 GLU   A N   
8570  C CA  . GLU   E  375 ? 0.25252 0.25252 0.25252 -0.00000 0.00000  0.00000  375 GLU   A CA  
8571  C C   . GLU   E  375 ? 0.44056 0.44056 0.44056 0.00000  0.00000  0.00000  375 GLU   A C   
8572  O O   . GLU   E  375 ? 0.26443 0.26443 0.26443 0.00000  0.00000  0.00000  375 GLU   A O   
8573  C CB  . GLU   E  375 ? 0.41536 0.41536 0.41536 0.00000  0.00000  0.00000  375 GLU   A CB  
8574  C CG  . GLU   E  375 ? 0.27169 0.27169 0.27169 -0.00000 0.00000  0.00000  375 GLU   A CG  
8575  C CD  . GLU   E  375 ? 0.40292 0.40292 0.40292 -0.00000 0.00000  0.00000  375 GLU   A CD  
8576  O OE1 . GLU   E  375 ? 0.47047 0.47047 0.47047 0.00000  0.00000  0.00000  375 GLU   A OE1 
8577  O OE2 . GLU   E  375 ? 0.45835 0.45835 0.45835 0.00000  0.00000  0.00000  375 GLU   A OE2 
8578  N N   . ILE   E  376 ? 0.28319 0.28319 0.28319 -0.00000 0.00000  0.00000  376 ILE   A N   
8579  C CA  . ILE   E  376 ? 0.28605 0.28605 0.28605 -0.00000 0.00000  0.00000  376 ILE   A CA  
8580  C C   . ILE   E  376 ? 0.33507 0.33507 0.33507 0.00000  0.00000  0.00000  376 ILE   A C   
8581  O O   . ILE   E  376 ? 0.43080 0.43080 0.43080 0.00000  -0.00000 0.00000  376 ILE   A O   
8582  C CB  . ILE   E  376 ? 0.42435 0.42435 0.42435 0.00000  0.00000  0.00000  376 ILE   A CB  
8583  C CG1 . ILE   E  376 ? 0.29051 0.29051 0.29051 -0.00000 -0.00000 0.00000  376 ILE   A CG1 
8584  C CG2 . ILE   E  376 ? 0.14664 0.14664 0.14664 0.00000  0.00000  0.00000  376 ILE   A CG2 
8585  C CD1 . ILE   E  376 ? 0.55432 0.55432 0.55432 0.00000  0.00000  0.00000  376 ILE   A CD1 
8586  N N   . SER   E  377 ? 0.37126 0.37126 0.37126 0.00000  0.00000  0.00000  377 SER   A N   
8587  C CA  . SER   E  377 ? 0.54273 0.54273 0.54273 0.00000  0.00000  0.00000  377 SER   A CA  
8588  C C   . SER   E  377 ? 0.33992 0.33992 0.33992 0.00000  0.00000  0.00000  377 SER   A C   
8589  O O   . SER   E  377 ? 0.64686 0.64686 0.64686 0.00000  0.00000  0.00000  377 SER   A O   
8590  C CB  . SER   E  377 ? 0.26207 0.26207 0.26207 0.00000  0.00000  0.00000  377 SER   A CB  
8591  O OG  . SER   E  377 ? 0.33905 0.33905 0.33905 0.00000  0.00000  0.00000  377 SER   A OG  
8592  N N   . THR   E  378 ? 0.50871 0.50871 0.50871 -0.00000 0.00000  0.00000  378 THR   A N   
8593  C CA  . THR   E  378 ? 0.33299 0.33299 0.33299 0.00000  0.00000  0.00000  378 THR   A CA  
8594  C C   . THR   E  378 ? 0.52753 0.52753 0.52753 0.00000  0.00000  0.00000  378 THR   A C   
8595  O O   . THR   E  378 ? 0.42284 0.42284 0.42284 0.00000  0.00000  0.00000  378 THR   A O   
8596  C CB  . THR   E  378 ? 0.49159 0.49159 0.49159 0.00000  0.00000  0.00000  378 THR   A CB  
8597  O OG1 . THR   E  378 ? 0.42566 0.42566 0.42566 0.00000  0.00000  0.00000  378 THR   A OG1 
8598  C CG2 . THR   E  378 ? 0.17764 0.17764 0.17764 0.00000  0.00000  0.00000  378 THR   A CG2 
8599  N N   . CYS   E  379 ? 0.30293 0.30293 0.30293 0.00000  0.00000  0.00000  379 CYS   A N   
8600  C CA  . CYS   E  379 ? 0.28117 0.28117 0.28117 -0.00000 0.00000  0.00000  379 CYS   A CA  
8601  C C   . CYS   E  379 ? 0.38338 0.38338 0.38338 -0.00000 0.00000  0.00000  379 CYS   A C   
8602  O O   . CYS   E  379 ? 0.45130 0.45130 0.45130 0.00000  0.00000  0.00000  379 CYS   A O   
8603  C CB  . CYS   E  379 ? 0.28853 0.28853 0.28853 0.00000  0.00000  0.00000  379 CYS   A CB  
8604  S SG  . CYS   E  379 ? 0.43450 0.43450 0.43450 -0.00000 0.00000  0.00000  379 CYS   A SG  
8605  N N   . GLU   E  380 ? 0.37988 0.37988 0.37988 0.00000  0.00000  0.00000  380 GLU   A N   
8606  C CA  . GLU   E  380 ? 0.19628 0.19628 0.19628 0.00000  0.00000  0.00000  380 GLU   A CA  
8607  C C   . GLU   E  380 ? 0.40263 0.40263 0.40263 0.00000  0.00000  0.00000  380 GLU   A C   
8608  O O   . GLU   E  380 ? 0.38819 0.38819 0.38819 0.00000  0.00000  0.00000  380 GLU   A O   
8609  C CB  . GLU   E  380 ? 0.34163 0.34163 0.34163 0.00000  0.00000  0.00000  380 GLU   A CB  
8610  C CG  . GLU   E  380 ? 0.50338 0.50338 0.50338 0.00000  0.00000  0.00000  380 GLU   A CG  
8611  C CD  . GLU   E  380 ? 0.44986 0.44986 0.44986 0.00000  0.00000  0.00000  380 GLU   A CD  
8612  O OE1 . GLU   E  380 ? 0.51352 0.51352 0.51352 -0.00000 0.00000  0.00000  380 GLU   A OE1 
8613  O OE2 . GLU   E  380 ? 0.60332 0.60332 0.60332 0.00000  0.00000  0.00000  380 GLU   A OE2 
8614  N N   . ALA   E  381 ? 0.29350 0.29350 0.29350 0.00000  0.00000  0.00000  381 ALA   A N   
8615  C CA  . ALA   E  381 ? 0.52778 0.52778 0.52778 0.00000  0.00000  0.00000  381 ALA   A CA  
8616  C C   . ALA   E  381 ? 0.40606 0.40606 0.40606 0.00000  0.00000  0.00000  381 ALA   A C   
8617  O O   . ALA   E  381 ? 0.41386 0.41386 0.41386 0.00000  0.00000  0.00000  381 ALA   A O   
8618  C CB  . ALA   E  381 ? 0.28058 0.28058 0.28058 -0.00000 0.00000  0.00000  381 ALA   A CB  
8619  N N   . THR   E  382 ? 0.39960 0.39960 0.39960 0.00000  0.00000  0.00000  382 THR   A N   
8620  C CA  . THR   E  382 ? 0.39430 0.39430 0.39430 0.00000  0.00000  0.00000  382 THR   A CA  
8621  C C   . THR   E  382 ? 0.33266 0.33266 0.33266 0.00000  0.00000  0.00000  382 THR   A C   
8622  O O   . THR   E  382 ? 0.68149 0.68149 0.68149 0.00000  0.00000  0.00000  382 THR   A O   
8623  C CB  . THR   E  382 ? 0.26401 0.26401 0.26401 -0.00000 0.00000  0.00000  382 THR   A CB  
8624  O OG1 . THR   E  382 ? 0.37662 0.37662 0.37662 -0.00000 0.00000  0.00000  382 THR   A OG1 
8625  C CG2 . THR   E  382 ? 0.40064 0.40064 0.40064 0.00000  0.00000  0.00000  382 THR   A CG2 
8626  N N   . VAL   E  383 ? 0.35665 0.35665 0.35665 -0.00000 0.00000  0.00000  383 VAL   A N   
8627  C CA  . VAL   E  383 ? 0.22162 0.22162 0.22162 0.00000  0.00000  0.00000  383 VAL   A CA  
8628  C C   . VAL   E  383 ? 0.39896 0.39896 0.39896 0.00000  0.00000  0.00000  383 VAL   A C   
8629  O O   . VAL   E  383 ? 0.34515 0.34515 0.34515 0.00000  0.00000  0.00000  383 VAL   A O   
8630  C CB  . VAL   E  383 ? 0.48395 0.48395 0.48395 -0.00000 0.00000  0.00000  383 VAL   A CB  
8631  C CG1 . VAL   E  383 ? 0.23132 0.23132 0.23132 0.00000  0.00000  0.00000  383 VAL   A CG1 
8632  C CG2 . VAL   E  383 ? 0.29096 0.29096 0.29096 0.00000  0.00000  0.00000  383 VAL   A CG2 
8633  N N   . SER   E  384 ? 0.52519 0.52519 0.52519 -0.00000 0.00000  0.00000  384 SER   A N   
8634  C CA  . SER   E  384 ? 0.27848 0.27848 0.27848 0.00000  0.00000  0.00000  384 SER   A CA  
8635  C C   . SER   E  384 ? 0.58748 0.58748 0.58748 -0.00000 0.00000  0.00000  384 SER   A C   
8636  O O   . SER   E  384 ? 0.44520 0.44520 0.44520 -0.00000 0.00000  0.00000  384 SER   A O   
8637  C CB  . SER   E  384 ? 0.30884 0.30884 0.30884 0.00000  0.00000  0.00000  384 SER   A CB  
8638  O OG  . SER   E  384 ? 0.65340 0.65340 0.65340 -0.00000 0.00000  0.00000  384 SER   A OG  
8639  N N   . GLU   E  385 ? 0.46773 0.46773 0.46773 0.00000  0.00000  0.00000  385 GLU   A N   
8640  C CA  . GLU   E  385 ? 0.57828 0.57828 0.57828 0.00000  0.00000  0.00000  385 GLU   A CA  
8641  C C   . GLU   E  385 ? 0.57343 0.57343 0.57343 0.00000  0.00000  0.00000  385 GLU   A C   
8642  O O   . GLU   E  385 ? 0.54754 0.54754 0.54754 0.00000  0.00000  0.00000  385 GLU   A O   
8643  C CB  . GLU   E  385 ? 0.29888 0.29888 0.29888 0.00000  0.00000  0.00000  385 GLU   A CB  
8644  C CG  . GLU   E  385 ? 0.47366 0.47366 0.47366 0.00000  0.00000  -0.00000 385 GLU   A CG  
8645  C CD  . GLU   E  385 ? 0.68782 0.68782 0.68782 0.00000  0.00000  0.00000  385 GLU   A CD  
8646  O OE1 . GLU   E  385 ? 0.66741 0.66741 0.66741 0.00000  0.00000  -0.00000 385 GLU   A OE1 
8647  O OE2 . GLU   E  385 ? 0.50481 0.50481 0.50481 0.00000  0.00000  0.00000  385 GLU   A OE2 
8648  N N   . GLY   E  386 ? 0.34503 0.34503 0.34503 0.00000  0.00000  0.00000  386 GLY   A N   
8649  C CA  . GLY   E  386 ? 0.16970 0.16970 0.16970 0.00000  0.00000  0.00000  386 GLY   A CA  
8650  C C   . GLY   E  386 ? 0.40666 0.40666 0.40666 0.00000  -0.00000 0.00000  386 GLY   A C   
8651  O O   . GLY   E  386 ? 0.33807 0.33807 0.33807 0.00000  0.00000  0.00000  386 GLY   A O   
8652  N N   . GLN   E  387 ? 0.34794 0.34794 0.34794 0.00000  0.00000  0.00000  387 GLN   A N   
8653  C CA  . GLN   E  387 ? 0.30603 0.30603 0.30603 0.00000  0.00000  0.00000  387 GLN   A CA  
8654  C C   . GLN   E  387 ? 0.54965 0.54965 0.54965 0.00000  0.00000  0.00000  387 GLN   A C   
8655  O O   . GLN   E  387 ? 0.46272 0.46272 0.46272 0.00000  0.00000  0.00000  387 GLN   A O   
8656  C CB  . GLN   E  387 ? 0.29154 0.29154 0.29154 0.00000  0.00000  0.00000  387 GLN   A CB  
8657  C CG  . GLN   E  387 ? 0.29868 0.29868 0.29868 0.00000  0.00000  0.00000  387 GLN   A CG  
8658  C CD  . GLN   E  387 ? 0.40000 0.40000 0.40000 0.00000  0.00000  0.00000  387 GLN   A CD  
8659  O OE1 . GLN   E  387 ? 0.46286 0.46286 0.46286 0.00000  0.00000  0.00000  387 GLN   A OE1 
8660  N NE2 . GLN   E  387 ? 0.31616 0.31616 0.31616 -0.00000 0.00000  0.00000  387 GLN   A NE2 
8661  N N   . HIS   E  388 ? 0.37635 0.37635 0.37635 0.00000  0.00000  0.00000  388 HIS   A N   
8662  C CA  . HIS   E  388 ? 0.51939 0.51939 0.51939 -0.00000 0.00000  0.00000  388 HIS   A CA  
8663  C C   . HIS   E  388 ? 0.69226 0.69226 0.69226 -0.00000 0.00000  0.00000  388 HIS   A C   
8664  O O   . HIS   E  388 ? 0.36402 0.36402 0.36402 0.00000  0.00000  0.00000  388 HIS   A O   
8665  C CB  . HIS   E  388 ? 0.24097 0.24097 0.24097 -0.00000 0.00000  0.00000  388 HIS   A CB  
8666  C CG  . HIS   E  388 ? 0.46049 0.46049 0.46049 0.00000  0.00000  0.00000  388 HIS   A CG  
8667  N ND1 . HIS   E  388 ? 0.47263 0.47263 0.47263 0.00000  0.00000  0.00000  388 HIS   A ND1 
8668  C CD2 . HIS   E  388 ? 0.32030 0.32030 0.32030 -0.00000 0.00000  0.00000  388 HIS   A CD2 
8669  C CE1 . HIS   E  388 ? 0.42597 0.42597 0.42597 -0.00000 0.00000  0.00000  388 HIS   A CE1 
8670  N NE2 . HIS   E  388 ? 0.37456 0.37456 0.37456 0.00000  0.00000  0.00000  388 HIS   A NE2 
8671  N N   . VAL   E  389 ? 0.26106 0.26106 0.26106 0.00000  -0.00000 0.00000  389 VAL   A N   
8672  C CA  . VAL   E  389 ? 0.41815 0.41815 0.41815 0.00000  0.00000  0.00000  389 VAL   A CA  
8673  C C   . VAL   E  389 ? 0.40477 0.40477 0.40477 0.00000  0.00000  0.00000  389 VAL   A C   
8674  O O   . VAL   E  389 ? 0.58377 0.58377 0.58377 0.00000  0.00000  0.00000  389 VAL   A O   
8675  C CB  . VAL   E  389 ? 0.48384 0.48384 0.48384 -0.00000 0.00000  0.00000  389 VAL   A CB  
8676  C CG1 . VAL   E  389 ? 0.29131 0.29131 0.29131 -0.00000 0.00000  0.00000  389 VAL   A CG1 
8677  C CG2 . VAL   E  389 ? 0.21896 0.21896 0.21896 -0.00000 -0.00000 0.00000  389 VAL   A CG2 
8678  N N   . ASN   E  390 ? 0.30872 0.30872 0.30872 0.00000  0.00000  0.00000  390 ASN   A N   
8679  C CA  . ASN   E  390 ? 0.35259 0.35259 0.35259 0.00000  0.00000  0.00000  390 ASN   A CA  
8680  C C   . ASN   E  390 ? 0.67381 0.67381 0.67381 0.00000  0.00000  0.00000  390 ASN   A C   
8681  O O   . ASN   E  390 ? 0.38852 0.38852 0.38852 -0.00000 0.00000  0.00000  390 ASN   A O   
8682  C CB  . ASN   E  390 ? 0.51344 0.51344 0.51344 0.00000  0.00000  0.00000  390 ASN   A CB  
8683  C CG  . ASN   E  390 ? 0.43172 0.43172 0.43172 0.00000  0.00000  0.00000  390 ASN   A CG  
8684  O OD1 . ASN   E  390 ? 0.56451 0.56451 0.56451 0.00000  0.00000  0.00000  390 ASN   A OD1 
8685  N ND2 . ASN   E  390 ? 0.55758 0.55758 0.55758 -0.00000 0.00000  0.00000  390 ASN   A ND2 
8686  N N   . ARG   E  391 ? 0.34996 0.34996 0.34996 -0.00000 0.00000  0.00000  391 ARG   A N   
8687  C CA  . ARG   E  391 ? 0.48414 0.48414 0.48414 -0.00000 0.00000  0.00000  391 ARG   A CA  
8688  C C   . ARG   E  391 ? 0.33225 0.33225 0.33225 0.00000  0.00000  0.00000  391 ARG   A C   
8689  O O   . ARG   E  391 ? 0.46751 0.46751 0.46751 0.00000  0.00000  0.00000  391 ARG   A O   
8690  C CB  . ARG   E  391 ? 0.22295 0.22295 0.22295 0.00000  0.00000  -0.00000 391 ARG   A CB  
8691  C CG  . ARG   E  391 ? 0.34542 0.34542 0.34542 -0.00000 -0.00000 0.00000  391 ARG   A CG  
8692  C CD  . ARG   E  391 ? 0.46685 0.46685 0.46685 -0.00000 0.00000  0.00000  391 ARG   A CD  
8693  N NE  . ARG   E  391 ? 0.37009 0.37009 0.37009 0.00000  -0.00000 0.00000  391 ARG   A NE  
8694  C CZ  . ARG   E  391 ? 0.89658 0.89658 0.89658 0.00000  0.00000  -0.00000 391 ARG   A CZ  
8695  N NH1 . ARG   E  391 ? 0.38231 0.38231 0.38231 0.00000  0.00000  0.00000  391 ARG   A NH1 
8696  N NH2 . ARG   E  391 ? 0.39432 0.39432 0.39432 -0.00000 0.00000  0.00000  391 ARG   A NH2 
8697  N N   . GLY   E  392 ? 0.33537 0.33537 0.33537 -0.00000 0.00000  0.00000  392 GLY   A N   
8698  C CA  . GLY   E  392 ? 0.29013 0.29013 0.29013 0.00000  0.00000  0.00000  392 GLY   A CA  
8699  C C   . GLY   E  392 ? 0.40134 0.40134 0.40134 0.00000  0.00000  0.00000  392 GLY   A C   
8700  O O   . GLY   E  392 ? 0.38330 0.38330 0.38330 -0.00000 0.00000  0.00000  392 GLY   A O   
8701  N N   . ASP   E  393 ? 0.28289 0.28289 0.28289 0.00000  0.00000  0.00000  393 ASP   A N   
8702  C CA  . ASP   E  393 ? 0.44361 0.44361 0.44361 0.00000  0.00000  0.00000  393 ASP   A CA  
8703  C C   . ASP   E  393 ? 0.37466 0.37466 0.37466 0.00000  0.00000  0.00000  393 ASP   A C   
8704  O O   . ASP   E  393 ? 0.61599 0.61599 0.61599 -0.00000 0.00000  0.00000  393 ASP   A O   
8705  C CB  . ASP   E  393 ? 0.32506 0.32506 0.32506 0.00000  0.00000  0.00000  393 ASP   A CB  
8706  C CG  . ASP   E  393 ? 0.69093 0.69093 0.69093 0.00000  0.00000  0.00000  393 ASP   A CG  
8707  O OD1 . ASP   E  393 ? 0.64790 0.64790 0.64790 0.00000  0.00000  0.00000  393 ASP   A OD1 
8708  O OD2 . ASP   E  393 ? 0.49719 0.49719 0.49719 0.00000  -0.00000 0.00000  393 ASP   A OD2 
8709  N N   . ASP   E  394 ? 0.59616 0.59616 0.59616 0.00000  0.00000  0.00000  394 ASP   A N   
8710  C CA  . ASP   E  394 ? 0.28861 0.28861 0.28861 0.00000  0.00000  0.00000  394 ASP   A CA  
8711  C C   . ASP   E  394 ? 0.62654 0.62654 0.62654 0.00000  0.00000  0.00000  394 ASP   A C   
8712  O O   . ASP   E  394 ? 0.40902 0.40902 0.40902 -0.00000 0.00000  0.00000  394 ASP   A O   
8713  C CB  . ASP   E  394 ? 0.53555 0.53555 0.53555 0.00000  0.00000  0.00000  394 ASP   A CB  
8714  C CG  . ASP   E  394 ? 0.40259 0.40259 0.40259 -0.00000 0.00000  0.00000  394 ASP   A CG  
8715  O OD1 . ASP   E  394 ? 0.96441 0.96441 0.96441 -0.00000 0.00000  0.00000  394 ASP   A OD1 
8716  O OD2 . ASP   E  394 ? 0.90425 0.90425 0.90425 -0.00000 0.00000  0.00000  394 ASP   A OD2 
8717  N N   . LEU   E  395 ? 0.29811 0.29811 0.29811 0.00000  0.00000  0.00000  395 LEU   A N   
8718  C CA  . LEU   E  395 ? 0.53800 0.53800 0.53800 -0.00000 0.00000  0.00000  395 LEU   A CA  
8719  C C   . LEU   E  395 ? 0.44852 0.44852 0.44852 0.00000  0.00000  0.00000  395 LEU   A C   
8720  O O   . LEU   E  395 ? 0.41642 0.41642 0.41642 0.00000  0.00000  0.00000  395 LEU   A O   
8721  C CB  . LEU   E  395 ? 0.25265 0.25265 0.25265 0.00000  0.00000  0.00000  395 LEU   A CB  
8722  C CG  . LEU   E  395 ? 0.43597 0.43597 0.43597 -0.00000 -0.00000 0.00000  395 LEU   A CG  
8723  C CD1 . LEU   E  395 ? 0.24596 0.24596 0.24596 -0.00000 0.00000  0.00000  395 LEU   A CD1 
8724  C CD2 . LEU   E  395 ? 0.37299 0.37299 0.37299 0.00000  0.00000  0.00000  395 LEU   A CD2 
8725  N N   . GLY   E  396 ? 0.26713 0.26713 0.26713 0.00000  0.00000  0.00000  396 GLY   A N   
8726  C CA  . GLY   E  396 ? 0.37350 0.37350 0.37350 0.00000  0.00000  0.00000  396 GLY   A CA  
8727  C C   . GLY   E  396 ? 0.32497 0.32497 0.32497 0.00000  0.00000  0.00000  396 GLY   A C   
8728  O O   . GLY   E  396 ? 0.36868 0.36868 0.36868 0.00000  0.00000  0.00000  396 GLY   A O   
8729  N N   . MET   E  397 ? 0.31666 0.31666 0.31666 0.00000  0.00000  0.00000  397 MET   A N   
8730  C CA  . MET   E  397 ? 0.30244 0.30244 0.30244 0.00000  0.00000  0.00000  397 MET   A CA  
8731  C C   . MET   E  397 ? 0.49888 0.49888 0.49888 0.00000  0.00000  0.00000  397 MET   A C   
8732  O O   . MET   E  397 ? 0.36246 0.36246 0.36246 -0.00000 0.00000  0.00000  397 MET   A O   
8733  C CB  . MET   E  397 ? 0.27488 0.27488 0.27488 0.00000  0.00000  0.00000  397 MET   A CB  
8734  C CG  . MET   E  397 ? 0.33163 0.33163 0.33163 0.00000  0.00000  0.00000  397 MET   A CG  
8735  S SD  . MET   E  397 ? 0.46336 0.46336 0.46336 -0.00000 0.00000  0.00000  397 MET   A SD  
8736  C CE  . MET   E  397 ? 0.18784 0.18784 0.18784 0.00000  -0.00000 0.00000  397 MET   A CE  
8737  N N   . PHE   E  398 ? 0.32436 0.32436 0.32436 -0.00000 0.00000  0.00000  398 PHE   A N   
8738  C CA  . PHE   E  398 ? 0.23928 0.23928 0.23928 -0.00000 0.00000  0.00000  398 PHE   A CA  
8739  C C   . PHE   E  398 ? 0.36313 0.36313 0.36313 0.00000  -0.00000 0.00000  398 PHE   A C   
8740  O O   . PHE   E  398 ? 0.48612 0.48612 0.48612 0.00000  0.00000  0.00000  398 PHE   A O   
8741  C CB  . PHE   E  398 ? 0.24031 0.24031 0.24031 0.00000  0.00000  0.00000  398 PHE   A CB  
8742  C CG  . PHE   E  398 ? 0.41314 0.41314 0.41314 0.00000  0.00000  0.00000  398 PHE   A CG  
8743  C CD1 . PHE   E  398 ? 0.24429 0.24429 0.24429 0.00000  0.00000  0.00000  398 PHE   A CD1 
8744  C CD2 . PHE   E  398 ? 0.32988 0.32988 0.32988 -0.00000 0.00000  0.00000  398 PHE   A CD2 
8745  C CE1 . PHE   E  398 ? 0.39678 0.39678 0.39678 -0.00000 0.00000  0.00000  398 PHE   A CE1 
8746  C CE2 . PHE   E  398 ? 0.27979 0.27979 0.27979 0.00000  0.00000  0.00000  398 PHE   A CE2 
8747  C CZ  . PHE   E  398 ? 0.37270 0.37270 0.37270 0.00000  0.00000  0.00000  398 PHE   A CZ  
8748  N N   . HIS   E  399 ? 0.47640 0.47640 0.47640 0.00000  0.00000  0.00000  399 HIS   A N   
8749  C CA  . HIS   E  399 ? 0.58270 0.58270 0.58270 0.00000  0.00000  0.00000  399 HIS   A CA  
8750  C C   . HIS   E  399 ? 0.30989 0.30989 0.30989 0.00000  0.00000  0.00000  399 HIS   A C   
8751  O O   . HIS   E  399 ? 0.66956 0.66956 0.66956 0.00000  0.00000  0.00000  399 HIS   A O   
8752  C CB  . HIS   E  399 ? 0.27823 0.27823 0.27823 0.00000  0.00000  0.00000  399 HIS   A CB  
8753  C CG  . HIS   E  399 ? 0.32578 0.32578 0.32578 -0.00000 0.00000  0.00000  399 HIS   A CG  
8754  N ND1 . HIS   E  399 ? 0.42767 0.42767 0.42767 0.00000  0.00000  0.00000  399 HIS   A ND1 
8755  C CD2 . HIS   E  399 ? 0.52118 0.52118 0.52118 -0.00000 0.00000  0.00000  399 HIS   A CD2 
8756  C CE1 . HIS   E  399 ? 0.65125 0.65125 0.65125 0.00000  0.00000  0.00000  399 HIS   A CE1 
8757  N NE2 . HIS   E  399 ? 0.28663 0.28663 0.28663 0.00000  0.00000  -0.00000 399 HIS   A NE2 
8758  N N   . PHE   E  400 ? 0.47911 0.47911 0.47911 -0.00000 0.00000  0.00000  400 PHE   A N   
8759  C CA  . PHE   E  400 ? 0.24441 0.24441 0.24441 -0.00000 0.00000  0.00000  400 PHE   A CA  
8760  C C   . PHE   E  400 ? 0.35372 0.35372 0.35372 0.00000  0.00000  0.00000  400 PHE   A C   
8761  O O   . PHE   E  400 ? 0.48658 0.48658 0.48658 0.00000  0.00000  0.00000  400 PHE   A O   
8762  C CB  . PHE   E  400 ? 0.46831 0.46831 0.46831 -0.00000 -0.00000 0.00000  400 PHE   A CB  
8763  C CG  . PHE   E  400 ? 0.21408 0.21408 0.21408 -0.00000 0.00000  0.00000  400 PHE   A CG  
8764  C CD1 . PHE   E  400 ? 0.45528 0.45528 0.45528 -0.00000 0.00000  0.00000  400 PHE   A CD1 
8765  C CD2 . PHE   E  400 ? 0.46785 0.46785 0.46785 0.00000  0.00000  0.00000  400 PHE   A CD2 
8766  C CE1 . PHE   E  400 ? 0.26109 0.26109 0.26109 0.00000  0.00000  0.00000  400 PHE   A CE1 
8767  C CE2 . PHE   E  400 ? 0.41524 0.41524 0.41524 -0.00000 0.00000  0.00000  400 PHE   A CE2 
8768  C CZ  . PHE   E  400 ? 0.45216 0.45216 0.45216 0.00000  0.00000  0.00000  400 PHE   A CZ  
8769  N N   . GLY   E  401 ? 0.43056 0.43056 0.43056 -0.00000 0.00000  -0.00000 401 GLY   A N   
8770  C CA  . GLY   E  401 ? 0.37899 0.37899 0.37899 0.00000  0.00000  0.00000  401 GLY   A CA  
8771  C C   . GLY   E  401 ? 0.51146 0.51146 0.51146 -0.00000 0.00000  0.00000  401 GLY   A C   
8772  O O   . GLY   E  401 ? 0.58989 0.58989 0.58989 0.00000  0.00000  0.00000  401 GLY   A O   
8773  N N   . GLY   E  402 ? 0.38130 0.38130 0.38130 0.00000  0.00000  0.00000  402 GLY   A N   
8774  C CA  . GLY   E  402 ? 0.28765 0.28765 0.28765 0.00000  0.00000  0.00000  402 GLY   A CA  
8775  C C   . GLY   E  402 ? 0.65796 0.65796 0.65796 0.00000  0.00000  0.00000  402 GLY   A C   
8776  O O   . GLY   E  402 ? 0.42515 0.42515 0.42515 0.00000  0.00000  0.00000  402 GLY   A O   
8777  O OXT . GLY   E  402 ? 0.54146 0.54146 0.54146 -0.00000 0.00000  0.00000  402 GLY   A OXT 
8778  N N   . SER   F  1   ? 0.21969 0.21969 0.21969 0.00000  0.00000  0.00000  404 SER   B N   
8779  C CA  . SER   F  1   ? 0.15788 0.15788 0.15788 0.00000  0.00000  0.00000  404 SER   B CA  
8780  C C   . SER   F  1   ? 0.30258 0.30258 0.30258 0.00000  0.00000  0.00000  404 SER   B C   
8781  O O   . SER   F  1   ? 0.34710 0.34710 0.34710 0.00000  0.00000  0.00000  404 SER   B O   
8782  C CB  . SER   F  1   ? 0.23735 0.23735 0.23735 0.00000  0.00000  0.00000  404 SER   B CB  
8783  O OG  . SER   F  1   ? 0.27203 0.27203 0.27203 0.00000  0.00000  0.00000  404 SER   B OG  
8784  N N   . PHE   F  2   ? 0.21792 0.21792 0.21792 -0.00000 0.00000  0.00000  405 PHE   B N   
8785  C CA  . PHE   F  2   ? 0.29739 0.29739 0.29739 0.00000  0.00000  0.00000  405 PHE   B CA  
8786  C C   . PHE   F  2   ? 0.26790 0.26790 0.26790 0.00000  0.00000  0.00000  405 PHE   B C   
8787  O O   . PHE   F  2   ? 0.38566 0.38566 0.38566 0.00000  0.00000  0.00000  405 PHE   B O   
8788  C CB  . PHE   F  2   ? 0.30602 0.30602 0.30602 -0.00000 -0.00000 0.00000  405 PHE   B CB  
8789  C CG  . PHE   F  2   ? 0.33733 0.33733 0.33733 -0.00000 -0.00000 -0.00000 405 PHE   B CG  
8790  C CD1 . PHE   F  2   ? 0.41704 0.41704 0.41704 -0.00000 0.00000  0.00000  405 PHE   B CD1 
8791  C CD2 . PHE   F  2   ? 0.38084 0.38084 0.38084 0.00000  0.00000  0.00000  405 PHE   B CD2 
8792  C CE1 . PHE   F  2   ? 0.33761 0.33761 0.33761 0.00000  0.00000  0.00000  405 PHE   B CE1 
8793  C CE2 . PHE   F  2   ? 0.28869 0.28869 0.28869 -0.00000 0.00000  0.00000  405 PHE   B CE2 
8794  C CZ  . PHE   F  2   ? 0.36706 0.36706 0.36706 0.00000  0.00000  0.00000  405 PHE   B CZ  
8795  N N   . ALA   F  3   ? 0.25304 0.25304 0.25304 -0.00000 0.00000  0.00000  406 ALA   B N   
8796  C CA  . ALA   F  3   ? 0.30689 0.30689 0.30689 0.00000  0.00000  0.00000  406 ALA   B CA  
8797  C C   . ALA   F  3   ? 0.34666 0.34666 0.34666 0.00000  0.00000  0.00000  406 ALA   B C   
8798  O O   . ALA   F  3   ? 0.33284 0.33284 0.33284 0.00000  0.00000  0.00000  406 ALA   B O   
8799  C CB  . ALA   F  3   ? 0.10171 0.10171 0.10171 0.00000  -0.00000 0.00000  406 ALA   B CB  
8800  N N   . LEU   F  4   ? 0.43637 0.43637 0.43637 0.00000  0.00000  0.00000  407 LEU   B N   
8801  C CA  . LEU   F  4   ? 0.42722 0.42722 0.42722 0.00000  0.00000  0.00000  407 LEU   B CA  
8802  C C   . LEU   F  4   ? 0.24001 0.24001 0.24001 0.00000  -0.00000 0.00000  407 LEU   B C   
8803  O O   . LEU   F  4   ? 0.48771 0.48771 0.48771 0.00000  0.00000  0.00000  407 LEU   B O   
8804  C CB  . LEU   F  4   ? 0.28725 0.28725 0.28725 0.00000  0.00000  0.00000  407 LEU   B CB  
8805  C CG  . LEU   F  4   ? 0.43580 0.43580 0.43580 0.00000  0.00000  0.00000  407 LEU   B CG  
8806  C CD1 . LEU   F  4   ? 0.26348 0.26348 0.26348 -0.00000 0.00000  0.00000  407 LEU   B CD1 
8807  C CD2 . LEU   F  4   ? 0.33881 0.33881 0.33881 0.00000  0.00000  0.00000  407 LEU   B CD2 
8808  N N   . GLY   F  5   ? 0.48012 0.48012 0.48012 -0.00000 0.00000  0.00000  408 GLY   B N   
8809  C CA  . GLY   F  5   ? 0.18518 0.18518 0.18518 0.00000  0.00000  0.00000  408 GLY   B CA  
8810  C C   . GLY   F  5   ? 0.38180 0.38180 0.38180 0.00000  0.00000  0.00000  408 GLY   B C   
8811  O O   . GLY   F  5   ? 0.46190 0.46190 0.46190 0.00000  0.00000  0.00000  408 GLY   B O   
8812  N N   . LEU   F  6   ? 0.26504 0.26504 0.26504 -0.00000 0.00000  0.00000  409 LEU   B N   
8813  C CA  . LEU   F  6   ? 0.51018 0.51018 0.51018 0.00000  0.00000  0.00000  409 LEU   B CA  
8814  C C   . LEU   F  6   ? 0.42654 0.42654 0.42654 0.00000  0.00000  0.00000  409 LEU   B C   
8815  O O   . LEU   F  6   ? 0.49070 0.49070 0.49070 0.00000  0.00000  0.00000  409 LEU   B O   
8816  C CB  . LEU   F  6   ? 0.39976 0.39976 0.39976 -0.00000 0.00000  0.00000  409 LEU   B CB  
8817  C CG  . LEU   F  6   ? 0.48684 0.48684 0.48684 0.00000  0.00000  0.00000  409 LEU   B CG  
8818  C CD1 . LEU   F  6   ? 0.31057 0.31057 0.31057 0.00000  -0.00000 -0.00000 409 LEU   B CD1 
8819  C CD2 . LEU   F  6   ? 0.25423 0.25423 0.25423 -0.00000 0.00000  0.00000  409 LEU   B CD2 
8820  N N   . ARG   F  7   ? 0.42794 0.42794 0.42794 0.00000  0.00000  0.00000  410 ARG   B N   
8821  C CA  . ARG   F  7   ? 0.41182 0.41182 0.41182 -0.00000 0.00000  0.00000  410 ARG   B CA  
8822  C C   . ARG   F  7   ? 0.48653 0.48653 0.48653 0.00000  0.00000  0.00000  410 ARG   B C   
8823  O O   . ARG   F  7   ? 0.62917 0.62917 0.62917 0.00000  -0.00000 0.00000  410 ARG   B O   
8824  C CB  . ARG   F  7   ? 0.24527 0.24527 0.24527 0.00000  0.00000  0.00000  410 ARG   B CB  
8825  C CG  . ARG   F  7   ? 0.27070 0.27070 0.27070 0.00000  0.00000  0.00000  410 ARG   B CG  
8826  C CD  . ARG   F  7   ? 0.41313 0.41313 0.41313 0.00000  0.00000  0.00000  410 ARG   B CD  
8827  N NE  . ARG   F  7   ? 0.65495 0.65495 0.65495 0.00000  0.00000  0.00000  410 ARG   B NE  
8828  C CZ  . ARG   F  7   ? 0.53919 0.53919 0.53919 0.00000  0.00000  0.00000  410 ARG   B CZ  
8829  N NH1 . ARG   F  7   ? 0.58180 0.58180 0.58180 0.00000  0.00000  0.00000  410 ARG   B NH1 
8830  N NH2 . ARG   F  7   ? 0.65606 0.65606 0.65606 0.00000  -0.00000 0.00000  410 ARG   B NH2 
8831  N N   . LYS   F  8   ? 0.72534 0.72534 0.72534 0.00000  0.00000  0.00000  411 LYS   B N   
8832  C CA  . LYS   F  8   ? 0.95408 0.95408 0.95408 0.00000  0.00000  0.00000  411 LYS   B CA  
8833  C C   . LYS   F  8   ? 0.85561 0.85561 0.85561 -0.00000 0.00000  0.00000  411 LYS   B C   
8834  O O   . LYS   F  8   ? 0.81649 0.81649 0.81649 0.00000  0.00000  0.00000  411 LYS   B O   
8835  C CB  . LYS   F  8   ? 0.60098 0.60098 0.60098 0.00000  0.00000  0.00000  411 LYS   B CB  
8836  N N   . ASP   F  9   ? 0.58541 0.58541 0.58541 -0.00000 -0.00000 -0.00000 412 ASP   B N   
8837  C CA  . ASP   F  9   ? 1.23676 1.23676 1.23676 0.00000  0.00000  0.00000  412 ASP   B CA  
8838  C C   . ASP   F  9   ? 0.67084 0.67084 0.67084 0.00000  0.00000  0.00000  412 ASP   B C   
8839  O O   . ASP   F  9   ? 1.05811 1.05811 1.05811 0.00000  -0.00000 -0.00000 412 ASP   B O   
8840  C CB  . ASP   F  9   ? 0.90184 0.90184 0.90184 -0.00000 -0.00000 0.00000  412 ASP   B CB  
8841  C CG  . ASP   F  9   ? 1.02131 1.02131 1.02131 0.00000  0.00000  0.00000  412 ASP   B CG  
8842  O OD1 . ASP   F  9   ? 1.05411 1.05411 1.05411 0.00000  0.00000  0.00000  412 ASP   B OD1 
8843  O OD2 . ASP   F  9   ? 1.34112 1.34112 1.34112 0.00000  0.00000  0.00000  412 ASP   B OD2 
8844  N N   . CYS   F  10  ? 1.01397 1.01397 1.01397 0.00000  0.00000  0.00000  413 CYS   B N   
8845  C CA  . CYS   F  10  ? 0.72170 0.72170 0.72170 0.00000  0.00000  0.00000  413 CYS   B CA  
8846  C C   . CYS   F  10  ? 0.85529 0.85529 0.85529 0.00000  0.00000  0.00000  413 CYS   B C   
8847  O O   . CYS   F  10  ? 0.83001 0.83001 0.83001 0.00000  0.00000  0.00000  413 CYS   B O   
8848  C CB  . CYS   F  10  ? 0.61388 0.61388 0.61388 0.00000  0.00000  0.00000  413 CYS   B CB  
8849  S SG  . CYS   F  10  ? 0.76429 0.76429 0.76429 -0.00000 0.00000  0.00000  413 CYS   B SG  
8850  N N   . ARG   F  11  ? 0.63336 0.63336 0.63336 0.00000  0.00000  0.00000  414 ARG   B N   
8851  C CA  . ARG   F  11  ? 0.91662 0.91662 0.91662 0.00000  0.00000  0.00000  414 ARG   B CA  
8852  C C   . ARG   F  11  ? 1.06011 1.06011 1.06011 0.00000  0.00000  0.00000  414 ARG   B C   
8853  O O   . ARG   F  11  ? 0.71238 0.71238 0.71238 0.00000  0.00000  0.00000  414 ARG   B O   
8854  C CB  . ARG   F  11  ? 0.55756 0.55756 0.55756 0.00000  0.00000  0.00000  414 ARG   B CB  
8855  N N   . ALA   F  12  ? 0.72188 0.72188 0.72188 0.00000  0.00000  0.00000  415 ALA   B N   
8856  C CA  . ALA   F  12  ? 0.58130 0.58130 0.58130 0.00000  0.00000  0.00000  415 ALA   B CA  
8857  C C   . ALA   F  12  ? 0.50377 0.50377 0.50377 -0.00000 0.00000  0.00000  415 ALA   B C   
8858  O O   . ALA   F  12  ? 0.85397 0.85397 0.85397 0.00000  0.00000  0.00000  415 ALA   B O   
8859  C CB  . ALA   F  12  ? 0.32392 0.32392 0.32392 -0.00000 0.00000  0.00000  415 ALA   B CB  
8860  N N   . GLU   F  13  ? 0.42674 0.42674 0.42674 0.00000  0.00000  0.00000  416 GLU   B N   
8861  C CA  . GLU   F  13  ? 0.60005 0.60005 0.60005 0.00000  0.00000  0.00000  416 GLU   B CA  
8862  C C   . GLU   F  13  ? 0.62918 0.62918 0.62918 0.00000  0.00000  0.00000  416 GLU   B C   
8863  O O   . GLU   F  13  ? 0.69463 0.69463 0.69463 0.00000  0.00000  0.00000  416 GLU   B O   
8864  C CB  . GLU   F  13  ? 0.46425 0.46425 0.46425 0.00000  0.00000  0.00000  416 GLU   B CB  
8865  N N   . ILE   F  14  ? 0.49055 0.49055 0.49055 0.00000  0.00000  0.00000  417 ILE   B N   
8866  C CA  . ILE   F  14  ? 0.58840 0.58840 0.58840 0.00000  0.00000  0.00000  417 ILE   B CA  
8867  C C   . ILE   F  14  ? 0.46355 0.46355 0.46355 0.00000  0.00000  0.00000  417 ILE   B C   
8868  O O   . ILE   F  14  ? 0.56916 0.56916 0.56916 0.00000  0.00000  0.00000  417 ILE   B O   
8869  C CB  . ILE   F  14  ? 0.33969 0.33969 0.33969 0.00000  0.00000  0.00000  417 ILE   B CB  
8870  C CG1 . ILE   F  14  ? 0.38238 0.38238 0.38238 0.00000  0.00000  0.00000  417 ILE   B CG1 
8871  C CG2 . ILE   F  14  ? 0.42856 0.42856 0.42856 0.00000  0.00000  0.00000  417 ILE   B CG2 
8872  C CD1 . ILE   F  14  ? 0.50987 0.50987 0.50987 0.00000  0.00000  0.00000  417 ILE   B CD1 
8873  N N   . VAL   F  15  ? 0.61909 0.61909 0.61909 0.00000  0.00000  0.00000  418 VAL   B N   
8874  C CA  . VAL   F  15  ? 0.38732 0.38732 0.38732 0.00000  0.00000  0.00000  418 VAL   B CA  
8875  C C   . VAL   F  15  ? 0.43538 0.43538 0.43538 0.00000  0.00000  0.00000  418 VAL   B C   
8876  O O   . VAL   F  15  ? 0.69000 0.69000 0.69000 -0.00000 0.00000  0.00000  418 VAL   B O   
8877  C CB  . VAL   F  15  ? 0.68322 0.68322 0.68322 0.00000  0.00000  0.00000  418 VAL   B CB  
8878  C CG1 . VAL   F  15  ? 0.28190 0.28190 0.28190 -0.00000 0.00000  0.00000  418 VAL   B CG1 
8879  C CG2 . VAL   F  15  ? 0.25997 0.25997 0.25997 0.00000  0.00000  0.00000  418 VAL   B CG2 
8880  N N   . GLU   F  16  ? 0.52974 0.52974 0.52974 0.00000  0.00000  0.00000  419 GLU   B N   
8881  C CA  . GLU   F  16  ? 0.39639 0.39639 0.39639 -0.00000 0.00000  0.00000  419 GLU   B CA  
8882  C C   . GLU   F  16  ? 0.52863 0.52863 0.52863 0.00000  0.00000  0.00000  419 GLU   B C   
8883  O O   . GLU   F  16  ? 0.53015 0.53015 0.53015 0.00000  0.00000  0.00000  419 GLU   B O   
8884  C CB  . GLU   F  16  ? 0.40517 0.40517 0.40517 0.00000  0.00000  0.00000  419 GLU   B CB  
8885  N N   . LYS   F  17  ? 0.45006 0.45006 0.45006 0.00000  0.00000  0.00000  420 LYS   B N   
8886  C CA  . LYS   F  17  ? 0.47864 0.47864 0.47864 0.00000  0.00000  0.00000  420 LYS   B CA  
8887  C C   . LYS   F  17  ? 0.56120 0.56120 0.56120 -0.00000 0.00000  0.00000  420 LYS   B C   
8888  O O   . LYS   F  17  ? 0.54095 0.54095 0.54095 0.00000  0.00000  0.00000  420 LYS   B O   
8889  C CB  . LYS   F  17  ? 0.25667 0.25667 0.25667 -0.00000 0.00000  0.00000  420 LYS   B CB  
8890  C CG  . LYS   F  17  ? 0.32000 0.32000 0.32000 0.00000  0.00000  0.00000  420 LYS   B CG  
8891  C CD  . LYS   F  17  ? 0.58770 0.58770 0.58770 0.00000  0.00000  0.00000  420 LYS   B CD  
8892  C CE  . LYS   F  17  ? 0.71177 0.71177 0.71177 0.00000  0.00000  0.00000  420 LYS   B CE  
8893  N NZ  . LYS   F  17  ? 1.00174 1.00174 1.00174 -0.00000 0.00000  0.00000  420 LYS   B NZ  
8894  N N   . PHE   F  18  ? 0.44981 0.44981 0.44981 0.00000  0.00000  0.00000  421 PHE   B N   
8895  C CA  . PHE   F  18  ? 0.74969 0.74969 0.74969 -0.00000 0.00000  0.00000  421 PHE   B CA  
8896  C C   . PHE   F  18  ? 0.58767 0.58767 0.58767 -0.00000 0.00000  0.00000  421 PHE   B C   
8897  O O   . PHE   F  18  ? 0.52072 0.52072 0.52072 -0.00000 0.00000  0.00000  421 PHE   B O   
8898  C CB  . PHE   F  18  ? 0.30829 0.30829 0.30829 -0.00000 0.00000  0.00000  421 PHE   B CB  
8899  C CG  . PHE   F  18  ? 0.45052 0.45052 0.45052 -0.00000 0.00000  0.00000  421 PHE   B CG  
8900  C CD1 . PHE   F  18  ? 0.44342 0.44342 0.44342 0.00000  0.00000  0.00000  421 PHE   B CD1 
8901  C CD2 . PHE   F  18  ? 0.66361 0.66361 0.66361 -0.00000 0.00000  0.00000  421 PHE   B CD2 
8902  C CE1 . PHE   F  18  ? 0.34608 0.34608 0.34608 0.00000  0.00000  0.00000  421 PHE   B CE1 
8903  C CE2 . PHE   F  18  ? 0.54185 0.54185 0.54185 -0.00000 0.00000  0.00000  421 PHE   B CE2 
8904  C CZ  . PHE   F  18  ? 0.61368 0.61368 0.61368 0.00000  0.00000  0.00000  421 PHE   B CZ  
8905  N N   . THR   F  19  ? 0.44101 0.44101 0.44101 0.00000  -0.00000 0.00000  422 THR   B N   
8906  C CA  . THR   F  19  ? 0.31717 0.31717 0.31717 0.00000  0.00000  0.00000  422 THR   B CA  
8907  C C   . THR   F  19  ? 0.41909 0.41909 0.41909 0.00000  0.00000  0.00000  422 THR   B C   
8908  O O   . THR   F  19  ? 0.39548 0.39548 0.39548 -0.00000 0.00000  0.00000  422 THR   B O   
8909  C CB  . THR   F  19  ? 0.46439 0.46439 0.46439 0.00000  -0.00000 0.00000  422 THR   B CB  
8910  O OG1 . THR   F  19  ? 0.41631 0.41631 0.41631 -0.00000 0.00000  0.00000  422 THR   B OG1 
8911  C CG2 . THR   F  19  ? 0.48873 0.48873 0.48873 0.00000  0.00000  0.00000  422 THR   B CG2 
8912  N N   . GLU   F  20  ? 0.53002 0.53002 0.53002 0.00000  0.00000  0.00000  423 GLU   B N   
8913  C CA  . GLU   F  20  ? 0.50836 0.50836 0.50836 0.00000  0.00000  0.00000  423 GLU   B CA  
8914  C C   . GLU   F  20  ? 0.38740 0.38740 0.38740 0.00000  0.00000  0.00000  423 GLU   B C   
8915  O O   . GLU   F  20  ? 0.58716 0.58716 0.58716 -0.00000 -0.00000 0.00000  423 GLU   B O   
8916  C CB  . GLU   F  20  ? 0.33452 0.33452 0.33452 0.00000  0.00000  0.00000  423 GLU   B CB  
8917  N N   . PRO   F  21  ? 0.47114 0.47114 0.47114 0.00000  0.00000  0.00000  424 PRO   B N   
8918  C CA  . PRO   F  21  ? 0.64136 0.64136 0.64136 -0.00000 0.00000  0.00000  424 PRO   B CA  
8919  C C   . PRO   F  21  ? 0.45917 0.45917 0.45917 0.00000  0.00000  0.00000  424 PRO   B C   
8920  O O   . PRO   F  21  ? 0.56932 0.56932 0.56932 0.00000  0.00000  -0.00000 424 PRO   B O   
8921  C CB  . PRO   F  21  ? 0.24249 0.24249 0.24249 0.00000  0.00000  0.00000  424 PRO   B CB  
8922  C CG  . PRO   F  21  ? 0.43397 0.43397 0.43397 -0.00000 0.00000  0.00000  424 PRO   B CG  
8923  C CD  . PRO   F  21  ? 0.41739 0.41739 0.41739 0.00000  0.00000  0.00000  424 PRO   B CD  
8924  N N   . GLY   F  22  ? 0.55395 0.55395 0.55395 -0.00000 0.00000  0.00000  425 GLY   B N   
8925  C CA  . GLY   F  22  ? 0.33455 0.33455 0.33455 -0.00000 0.00000  0.00000  425 GLY   B CA  
8926  C C   . GLY   F  22  ? 0.44397 0.44397 0.44397 0.00000  0.00000  0.00000  425 GLY   B C   
8927  O O   . GLY   F  22  ? 0.51842 0.51842 0.51842 0.00000  0.00000  0.00000  425 GLY   B O   
8928  N N   . THR   F  23  ? 0.36426 0.36426 0.36426 0.00000  0.00000  0.00000  426 THR   B N   
8929  C CA  . THR   F  23  ? 0.33474 0.33474 0.33474 -0.00000 0.00000  0.00000  426 THR   B CA  
8930  C C   . THR   F  23  ? 0.33440 0.33440 0.33440 -0.00000 0.00000  0.00000  426 THR   B C   
8931  O O   . THR   F  23  ? 0.70511 0.70511 0.70511 -0.00000 -0.00000 0.00000  426 THR   B O   
8932  C CB  . THR   F  23  ? 0.44457 0.44457 0.44457 -0.00000 0.00000  0.00000  426 THR   B CB  
8933  O OG1 . THR   F  23  ? 0.54968 0.54968 0.54968 -0.00000 0.00000  0.00000  426 THR   B OG1 
8934  C CG2 . THR   F  23  ? 0.32348 0.32348 0.32348 0.00000  0.00000  0.00000  426 THR   B CG2 
8935  N N   . VAL   F  24  ? 0.62559 0.62559 0.62559 0.00000  0.00000  0.00000  427 VAL   B N   
8936  C CA  . VAL   F  24  ? 0.38703 0.38703 0.38703 0.00000  0.00000  0.00000  427 VAL   B CA  
8937  C C   . VAL   F  24  ? 0.31681 0.31681 0.31681 -0.00000 0.00000  0.00000  427 VAL   B C   
8938  O O   . VAL   F  24  ? 0.63160 0.63160 0.63160 0.00000  0.00000  0.00000  427 VAL   B O   
8939  C CB  . VAL   F  24  ? 0.29671 0.29671 0.29671 0.00000  0.00000  0.00000  427 VAL   B CB  
8940  C CG1 . VAL   F  24  ? 0.20475 0.20475 0.20475 0.00000  0.00000  0.00000  427 VAL   B CG1 
8941  C CG2 . VAL   F  24  ? 0.29603 0.29603 0.29603 0.00000  0.00000  0.00000  427 VAL   B CG2 
8942  N N   . ILE   F  25  ? 0.67045 0.67045 0.67045 0.00000  0.00000  0.00000  428 ILE   B N   
8943  C CA  . ILE   F  25  ? 0.27652 0.27652 0.27652 0.00000  -0.00000 0.00000  428 ILE   B CA  
8944  C C   . ILE   F  25  ? 0.54770 0.54770 0.54770 -0.00000 0.00000  0.00000  428 ILE   B C   
8945  O O   . ILE   F  25  ? 0.43752 0.43752 0.43752 -0.00000 0.00000  0.00000  428 ILE   B O   
8946  C CB  . ILE   F  25  ? 0.50964 0.50964 0.50964 -0.00000 0.00000  0.00000  428 ILE   B CB  
8947  C CG1 . ILE   F  25  ? 0.39399 0.39399 0.39399 0.00000  0.00000  0.00000  428 ILE   B CG1 
8948  C CG2 . ILE   F  25  ? 0.24155 0.24155 0.24155 0.00000  0.00000  0.00000  428 ILE   B CG2 
8949  C CD1 . ILE   F  25  ? 0.32596 0.32596 0.32596 0.00000  0.00000  0.00000  428 ILE   B CD1 
8950  N N   . ARG   F  26  ? 0.38341 0.38341 0.38341 -0.00000 0.00000  0.00000  429 ARG   B N   
8951  C CA  . ARG   F  26  ? 0.36837 0.36837 0.36837 0.00000  0.00000  0.00000  429 ARG   B CA  
8952  C C   . ARG   F  26  ? 0.37508 0.37508 0.37508 0.00000  0.00000  0.00000  429 ARG   B C   
8953  O O   . ARG   F  26  ? 0.36292 0.36292 0.36292 -0.00000 0.00000  0.00000  429 ARG   B O   
8954  C CB  . ARG   F  26  ? 0.46988 0.46988 0.46988 -0.00000 0.00000  0.00000  429 ARG   B CB  
8955  C CG  . ARG   F  26  ? 0.39108 0.39108 0.39108 -0.00000 0.00000  0.00000  429 ARG   B CG  
8956  C CD  . ARG   F  26  ? 0.56361 0.56361 0.56361 -0.00000 0.00000  0.00000  429 ARG   B CD  
8957  N NE  . ARG   F  26  ? 0.38354 0.38354 0.38354 -0.00000 0.00000  0.00000  429 ARG   B NE  
8958  C CZ  . ARG   F  26  ? 2.06172 2.06172 2.06172 0.00000  0.00000  0.00000  429 ARG   B CZ  
8959  N NH1 . ARG   F  26  ? 0.32829 0.32829 0.32829 0.00000  0.00000  0.00000  429 ARG   B NH1 
8960  N NH2 . ARG   F  26  ? 0.41475 0.41475 0.41475 0.00000  -0.00000 0.00000  429 ARG   B NH2 
8961  N N   . ILE   F  27  ? 0.21710 0.21710 0.21710 -0.00000 -0.00000 0.00000  430 ILE   B N   
8962  C CA  . ILE   F  27  ? 0.43739 0.43739 0.43739 -0.00000 0.00000  0.00000  430 ILE   B CA  
8963  C C   . ILE   F  27  ? 0.28074 0.28074 0.28074 0.00000  0.00000  0.00000  430 ILE   B C   
8964  O O   . ILE   F  27  ? 0.62019 0.62019 0.62019 0.00000  -0.00000 0.00000  430 ILE   B O   
8965  C CB  . ILE   F  27  ? 0.35511 0.35511 0.35511 0.00000  0.00000  0.00000  430 ILE   B CB  
8966  C CG1 . ILE   F  27  ? 0.28526 0.28526 0.28526 0.00000  0.00000  0.00000  430 ILE   B CG1 
8967  C CG2 . ILE   F  27  ? 0.33123 0.33123 0.33123 -0.00000 0.00000  0.00000  430 ILE   B CG2 
8968  C CD1 . ILE   F  27  ? 0.24959 0.24959 0.24959 -0.00000 0.00000  0.00000  430 ILE   B CD1 
8969  N N   . ASN   F  28  ? 0.52647 0.52647 0.52647 -0.00000 0.00000  0.00000  431 ASN   B N   
8970  C CA  . ASN   F  28  ? 0.26623 0.26623 0.26623 0.00000  0.00000  0.00000  431 ASN   B CA  
8971  C C   . ASN   F  28  ? 0.41274 0.41274 0.41274 0.00000  0.00000  0.00000  431 ASN   B C   
8972  O O   . ASN   F  28  ? 0.29299 0.29299 0.29299 -0.00000 0.00000  0.00000  431 ASN   B O   
8973  C CB  . ASN   F  28  ? 0.21138 0.21138 0.21138 0.00000  0.00000  0.00000  431 ASN   B CB  
8974  C CG  . ASN   F  28  ? 0.36221 0.36221 0.36221 0.00000  0.00000  0.00000  431 ASN   B CG  
8975  O OD1 . ASN   F  28  ? 0.42492 0.42492 0.42492 0.00000  0.00000  0.00000  431 ASN   B OD1 
8976  N ND2 . ASN   F  28  ? 0.26277 0.26277 0.26277 -0.00000 0.00000  0.00000  431 ASN   B ND2 
8977  N N   . GLU   F  29  ? 0.33810 0.33810 0.33810 0.00000  0.00000  0.00000  432 GLU   B N   
8978  C CA  . GLU   F  29  ? 0.44760 0.44760 0.44760 0.00000  0.00000  0.00000  432 GLU   B CA  
8979  C C   . GLU   F  29  ? 0.39412 0.39412 0.39412 -0.00000 0.00000  0.00000  432 GLU   B C   
8980  O O   . GLU   F  29  ? 0.58996 0.58996 0.58996 -0.00000 0.00000  0.00000  432 GLU   B O   
8981  C CB  . GLU   F  29  ? 0.24719 0.24719 0.24719 0.00000  0.00000  0.00000  432 GLU   B CB  
8982  C CG  . GLU   F  29  ? 0.41540 0.41540 0.41540 -0.00000 0.00000  0.00000  432 GLU   B CG  
8983  C CD  . GLU   F  29  ? 0.72416 0.72416 0.72416 0.00000  0.00000  0.00000  432 GLU   B CD  
8984  O OE1 . GLU   F  29  ? 0.53437 0.53437 0.53437 0.00000  0.00000  0.00000  432 GLU   B OE1 
8985  O OE2 . GLU   F  29  ? 0.61356 0.61356 0.61356 -0.00000 0.00000  0.00000  432 GLU   B OE2 
8986  N N   . VAL   F  30  ? 0.55634 0.55634 0.55634 -0.00000 0.00000  0.00000  433 VAL   B N   
8987  C CA  . VAL   F  30  ? 0.24373 0.24373 0.24373 0.00000  0.00000  0.00000  433 VAL   B CA  
8988  C C   . VAL   F  30  ? 0.49833 0.49833 0.49833 0.00000  0.00000  0.00000  433 VAL   B C   
8989  O O   . VAL   F  30  ? 0.38227 0.38227 0.38227 0.00000  0.00000  0.00000  433 VAL   B O   
8990  C CB  . VAL   F  30  ? 0.50909 0.50909 0.50909 -0.00000 0.00000  0.00000  433 VAL   B CB  
8991  C CG1 . VAL   F  30  ? 0.38025 0.38025 0.38025 -0.00000 0.00000  0.00000  433 VAL   B CG1 
8992  C CG2 . VAL   F  30  ? 0.31409 0.31409 0.31409 -0.00000 0.00000  0.00000  433 VAL   B CG2 
8993  N N   . VAL   F  31  ? 0.41241 0.41241 0.41241 0.00000  0.00000  0.00000  434 VAL   B N   
8994  C CA  . VAL   F  31  ? 0.55276 0.55276 0.55276 0.00000  0.00000  0.00000  434 VAL   B CA  
8995  C C   . VAL   F  31  ? 0.39567 0.39567 0.39567 0.00000  0.00000  0.00000  434 VAL   B C   
8996  O O   . VAL   F  31  ? 0.38531 0.38531 0.38531 0.00000  0.00000  0.00000  434 VAL   B O   
8997  C CB  . VAL   F  31  ? 0.43017 0.43017 0.43017 0.00000  0.00000  -0.00000 434 VAL   B CB  
8998  C CG1 . VAL   F  31  ? 0.22454 0.22454 0.22454 0.00000  0.00000  -0.00000 434 VAL   B CG1 
8999  C CG2 . VAL   F  31  ? 0.25720 0.25720 0.25720 -0.00000 0.00000  0.00000  434 VAL   B CG2 
9000  N N   . ALA   F  32  ? 0.39196 0.39196 0.39196 0.00000  0.00000  0.00000  435 ALA   B N   
9001  C CA  . ALA   F  32  ? 0.43347 0.43347 0.43347 0.00000  0.00000  0.00000  435 ALA   B CA  
9002  C C   . ALA   F  32  ? 0.55939 0.55939 0.55939 0.00000  0.00000  0.00000  435 ALA   B C   
9003  O O   . ALA   F  32  ? 0.45895 0.45895 0.45895 0.00000  0.00000  0.00000  435 ALA   B O   
9004  C CB  . ALA   F  32  ? 0.35365 0.35365 0.35365 0.00000  0.00000  0.00000  435 ALA   B CB  
9005  N N   . ALA   F  33  ? 0.38816 0.38816 0.38816 0.00000  0.00000  0.00000  436 ALA   B N   
9006  C CA  . ALA   F  33  ? 0.50213 0.50213 0.50213 0.00000  0.00000  0.00000  436 ALA   B CA  
9007  C C   . ALA   F  33  ? 0.75064 0.75064 0.75064 0.00000  0.00000  0.00000  436 ALA   B C   
9008  O O   . ALA   F  33  ? 0.46436 0.46436 0.46436 -0.00000 0.00000  0.00000  436 ALA   B O   
9009  C CB  . ALA   F  33  ? 0.30079 0.30079 0.30079 0.00000  0.00000  0.00000  436 ALA   B CB  
9010  N N   . LEU   F  34  ? 0.43444 0.43444 0.43444 0.00000  0.00000  0.00000  437 LEU   B N   
9011  C CA  . LEU   F  34  ? 0.81091 0.81091 0.81091 -0.00000 0.00000  0.00000  437 LEU   B CA  
9012  C C   . LEU   F  34  ? 0.40398 0.40398 0.40398 0.00000  0.00000  0.00000  437 LEU   B C   
9013  O O   . LEU   F  34  ? 0.48931 0.48931 0.48931 0.00000  0.00000  0.00000  437 LEU   B O   
9014  C CB  . LEU   F  34  ? 0.38905 0.38905 0.38905 -0.00000 0.00000  0.00000  437 LEU   B CB  
9015  C CG  . LEU   F  34  ? 0.70724 0.70724 0.70724 -0.00000 0.00000  0.00000  437 LEU   B CG  
9016  C CD1 . LEU   F  34  ? 0.46856 0.46856 0.46856 0.00000  0.00000  0.00000  437 LEU   B CD1 
9017  C CD2 . LEU   F  34  ? 0.74212 0.74212 0.74212 -0.00000 0.00000  0.00000  437 LEU   B CD2 
9018  N N   . LEU   G  57  ? 0.46203 0.46203 0.46203 0.00000  0.00000  0.00000  57  LEU   C N   
9019  C CA  . LEU   G  57  ? 0.42274 0.42274 0.42274 -0.00000 0.00000  0.00000  57  LEU   C CA  
9020  C C   . LEU   G  57  ? 0.62718 0.62718 0.62718 -0.00000 0.00000  0.00000  57  LEU   C C   
9021  O O   . LEU   G  57  ? 0.65243 0.65243 0.65243 0.00000  0.00000  0.00000  57  LEU   C O   
9022  C CB  . LEU   G  57  ? 0.38025 0.38025 0.38025 -0.00000 0.00000  0.00000  57  LEU   C CB  
9023  C CG  . LEU   G  57  ? 0.58623 0.58623 0.58623 0.00000  0.00000  0.00000  57  LEU   C CG  
9024  C CD1 . LEU   G  57  ? 0.48980 0.48980 0.48980 0.00000  0.00000  0.00000  57  LEU   C CD1 
9025  C CD2 . LEU   G  57  ? 0.56679 0.56679 0.56679 0.00000  0.00000  0.00000  57  LEU   C CD2 
9026  N N   . MET   G  58  ? 0.66078 0.66078 0.66078 -0.00000 0.00000  0.00000  58  MET   C N   
9027  C CA  . MET   G  58  ? 0.64683 0.64683 0.64683 -0.00000 0.00000  0.00000  58  MET   C CA  
9028  C C   . MET   G  58  ? 0.52915 0.52915 0.52915 -0.00000 0.00000  0.00000  58  MET   C C   
9029  O O   . MET   G  58  ? 0.79089 0.79089 0.79089 0.00000  0.00000  0.00000  58  MET   C O   
9030  C CB  . MET   G  58  ? 0.55745 0.55745 0.55745 -0.00000 -0.00000 0.00000  58  MET   C CB  
9031  C CG  . MET   G  58  ? 0.75125 0.75125 0.75125 0.00000  -0.00000 0.00000  58  MET   C CG  
9032  S SD  . MET   G  58  ? 0.82553 0.82553 0.82553 0.00000  0.00000  0.00000  58  MET   C SD  
9033  C CE  . MET   G  58  ? 0.52950 0.52950 0.52950 -0.00000 0.00000  0.00000  58  MET   C CE  
9034  N N   . GLN   G  59  ? 0.57723 0.57723 0.57723 0.00000  0.00000  0.00000  59  GLN   C N   
9035  C CA  . GLN   G  59  ? 0.43587 0.43587 0.43587 -0.00000 0.00000  0.00000  59  GLN   C CA  
9036  C C   . GLN   G  59  ? 0.55909 0.55909 0.55909 0.00000  0.00000  0.00000  59  GLN   C C   
9037  O O   . GLN   G  59  ? 0.48374 0.48374 0.48374 0.00000  0.00000  0.00000  59  GLN   C O   
9038  C CB  . GLN   G  59  ? 0.35671 0.35671 0.35671 0.00000  0.00000  0.00000  59  GLN   C CB  
9039  C CG  . GLN   G  59  ? 0.73099 0.73099 0.73099 -0.00000 0.00000  0.00000  59  GLN   C CG  
9040  C CD  . GLN   G  59  ? 1.01712 1.01712 1.01712 -0.00000 0.00000  0.00000  59  GLN   C CD  
9041  O OE1 . GLN   G  59  ? 1.16383 1.16383 1.16383 -0.00000 -0.00000 0.00000  59  GLN   C OE1 
9042  N NE2 . GLN   G  59  ? 0.82241 0.82241 0.82241 -0.00000 0.00000  0.00000  59  GLN   C NE2 
9043  N N   . PRO   G  60  ? 0.66361 0.66361 0.66361 0.00000  0.00000  0.00000  60  PRO   C N   
9044  C CA  . PRO   G  60  ? 0.43209 0.43209 0.43209 0.00000  0.00000  0.00000  60  PRO   C CA  
9045  C C   . PRO   G  60  ? 0.73717 0.73717 0.73717 0.00000  0.00000  0.00000  60  PRO   C C   
9046  O O   . PRO   G  60  ? 0.47251 0.47251 0.47251 0.00000  0.00000  0.00000  60  PRO   C O   
9047  C CB  . PRO   G  60  ? 0.44176 0.44176 0.44176 0.00000  0.00000  0.00000  60  PRO   C CB  
9048  C CG  . PRO   G  60  ? 0.53027 0.53027 0.53027 -0.00000 0.00000  0.00000  60  PRO   C CG  
9049  C CD  . PRO   G  60  ? 0.38183 0.38183 0.38183 0.00000  0.00000  0.00000  60  PRO   C CD  
9050  N N   . ILE   G  61  ? 0.37292 0.37292 0.37292 0.00000  0.00000  0.00000  61  ILE   C N   
9051  C CA  . ILE   G  61  ? 0.68111 0.68111 0.68111 -0.00000 0.00000  0.00000  61  ILE   C CA  
9052  C C   . ILE   G  61  ? 0.50784 0.50784 0.50784 -0.00000 0.00000  0.00000  61  ILE   C C   
9053  O O   . ILE   G  61  ? 0.56273 0.56273 0.56273 0.00000  0.00000  0.00000  61  ILE   C O   
9054  C CB  . ILE   G  61  ? 0.50241 0.50241 0.50241 -0.00000 0.00000  0.00000  61  ILE   C CB  
9055  C CG1 . ILE   G  61  ? 0.38275 0.38275 0.38275 0.00000  0.00000  0.00000  61  ILE   C CG1 
9056  C CG2 . ILE   G  61  ? 0.35915 0.35915 0.35915 0.00000  0.00000  0.00000  61  ILE   C CG2 
9057  C CD1 . ILE   G  61  ? 0.46619 0.46619 0.46619 -0.00000 0.00000  0.00000  61  ILE   C CD1 
9058  N N   . GLN   G  62  ? 1.01487 1.01487 1.01487 0.00000  0.00000  0.00000  62  GLN   C N   
9059  C CA  . GLN   G  62  ? 0.15517 0.15517 0.15517 -0.00000 0.00000  0.00000  62  GLN   C CA  
9060  C C   . GLN   G  62  ? 0.93404 0.93404 0.93404 0.00000  0.00000  0.00000  62  GLN   C C   
9061  O O   . GLN   G  62  ? 0.59548 0.59548 0.59548 0.00000  0.00000  0.00000  62  GLN   C O   
9062  C CB  . GLN   G  62  ? 0.69517 0.69517 0.69517 0.00000  -0.00000 0.00000  62  GLN   C CB  
9063  C CG  . GLN   G  62  ? 0.92362 0.92362 0.92362 0.00000  0.00000  0.00000  62  GLN   C CG  
9064  C CD  . GLN   G  62  ? 1.09438 1.09438 1.09438 0.00000  0.00000  0.00000  62  GLN   C CD  
9065  O OE1 . GLN   G  62  ? 1.48270 1.48270 1.48270 0.00000  0.00000  0.00000  62  GLN   C OE1 
9066  N NE2 . GLN   G  62  ? 1.56479 1.56479 1.56479 0.00000  -0.00000 0.00000  62  GLN   C NE2 
9067  N N   . GLU   G  63  ? 0.37296 0.37296 0.37296 -0.00000 0.00000  0.00000  63  GLU   C N   
9068  C CA  . GLU   G  63  ? 0.57353 0.57353 0.57353 -0.00000 0.00000  0.00000  63  GLU   C CA  
9069  C C   . GLU   G  63  ? 0.60164 0.60164 0.60164 0.00000  0.00000  0.00000  63  GLU   C C   
9070  O O   . GLU   G  63  ? 0.51705 0.51705 0.51705 -0.00000 0.00000  0.00000  63  GLU   C O   
9071  C CB  . GLU   G  63  ? 0.37241 0.37241 0.37241 0.00000  0.00000  0.00000  63  GLU   C CB  
9072  C CG  . GLU   G  63  ? 0.84830 0.84830 0.84830 0.00000  0.00000  0.00000  63  GLU   C CG  
9073  C CD  . GLU   G  63  ? 0.68102 0.68102 0.68102 0.00000  0.00000  0.00000  63  GLU   C CD  
9074  O OE1 . GLU   G  63  ? 1.26944 1.26944 1.26944 0.00000  0.00000  0.00000  63  GLU   C OE1 
9075  O OE2 . GLU   G  63  ? 1.61891 1.61891 1.61891 0.00000  0.00000  0.00000  63  GLU   C OE2 
9076  N N   . PHE   G  64  ? 0.49517 0.49517 0.49517 -0.00000 0.00000  0.00000  64  PHE   C N   
9077  C CA  . PHE   G  64  ? 0.41220 0.41220 0.41220 -0.00000 0.00000  0.00000  64  PHE   C CA  
9078  C C   . PHE   G  64  ? 0.58998 0.58998 0.58998 0.00000  0.00000  0.00000  64  PHE   C C   
9079  O O   . PHE   G  64  ? 0.52107 0.52107 0.52107 0.00000  0.00000  0.00000  64  PHE   C O   
9080  C CB  . PHE   G  64  ? 0.45139 0.45139 0.45139 -0.00000 0.00000  0.00000  64  PHE   C CB  
9081  C CG  . PHE   G  64  ? 0.51690 0.51690 0.51690 0.00000  0.00000  0.00000  64  PHE   C CG  
9082  C CD1 . PHE   G  64  ? 0.61753 0.61753 0.61753 0.00000  0.00000  0.00000  64  PHE   C CD1 
9083  C CD2 . PHE   G  64  ? 0.37802 0.37802 0.37802 -0.00000 0.00000  0.00000  64  PHE   C CD2 
9084  C CE1 . PHE   G  64  ? 0.44011 0.44011 0.44011 0.00000  0.00000  0.00000  64  PHE   C CE1 
9085  C CE2 . PHE   G  64  ? 0.35587 0.35587 0.35587 -0.00000 0.00000  0.00000  64  PHE   C CE2 
9086  C CZ  . PHE   G  64  ? 0.46653 0.46653 0.46653 0.00000  0.00000  0.00000  64  PHE   C CZ  
9087  N N   . LYS   G  65  ? 0.48649 0.48649 0.48649 0.00000  0.00000  0.00000  65  LYS   C N   
9088  C CA  . LYS   G  65  ? 0.42236 0.42236 0.42236 0.00000  0.00000  0.00000  65  LYS   C CA  
9089  C C   . LYS   G  65  ? 0.67803 0.67803 0.67803 0.00000  0.00000  0.00000  65  LYS   C C   
9090  O O   . LYS   G  65  ? 0.57108 0.57108 0.57108 -0.00000 0.00000  0.00000  65  LYS   C O   
9091  C CB  . LYS   G  65  ? 0.51428 0.51428 0.51428 0.00000  0.00000  0.00000  65  LYS   C CB  
9092  C CG  . LYS   G  65  ? 0.52739 0.52739 0.52739 -0.00000 0.00000  0.00000  65  LYS   C CG  
9093  C CD  . LYS   G  65  ? 0.66080 0.66080 0.66080 0.00000  0.00000  0.00000  65  LYS   C CD  
9094  C CE  . LYS   G  65  ? 0.75900 0.75900 0.75900 0.00000  0.00000  0.00000  65  LYS   C CE  
9095  N NZ  . LYS   G  65  ? 0.89914 0.89914 0.89914 -0.00000 0.00000  -0.00000 65  LYS   C NZ  
9096  N N   . ALA   G  66  ? 0.54163 0.54163 0.54163 -0.00000 0.00000  0.00000  66  ALA   C N   
9097  C CA  . ALA   G  66  ? 0.58259 0.58259 0.58259 -0.00000 0.00000  0.00000  66  ALA   C CA  
9098  C C   . ALA   G  66  ? 0.71322 0.71322 0.71322 0.00000  0.00000  0.00000  66  ALA   C C   
9099  O O   . ALA   G  66  ? 0.51594 0.51594 0.51594 0.00000  0.00000  0.00000  66  ALA   C O   
9100  C CB  . ALA   G  66  ? 0.29500 0.29500 0.29500 0.00000  0.00000  0.00000  66  ALA   C CB  
9101  N N   . PHE   G  67  ? 0.70823 0.70823 0.70823 -0.00000 0.00000  0.00000  67  PHE   C N   
9102  C CA  . PHE   G  67  ? 0.43528 0.43528 0.43528 -0.00000 0.00000  0.00000  67  PHE   C CA  
9103  C C   . PHE   G  67  ? 0.63774 0.63774 0.63774 0.00000  0.00000  0.00000  67  PHE   C C   
9104  O O   . PHE   G  67  ? 0.59051 0.59051 0.59051 0.00000  0.00000  0.00000  67  PHE   C O   
9105  C CB  . PHE   G  67  ? 0.45069 0.45069 0.45069 0.00000  0.00000  0.00000  67  PHE   C CB  
9106  C CG  . PHE   G  67  ? 0.46304 0.46304 0.46304 0.00000  0.00000  0.00000  67  PHE   C CG  
9107  C CD1 . PHE   G  67  ? 0.29060 0.29060 0.29060 -0.00000 0.00000  0.00000  67  PHE   C CD1 
9108  C CD2 . PHE   G  67  ? 0.38654 0.38654 0.38654 -0.00000 0.00000  0.00000  67  PHE   C CD2 
9109  C CE1 . PHE   G  67  ? 0.38101 0.38101 0.38101 -0.00000 0.00000  0.00000  67  PHE   C CE1 
9110  C CE2 . PHE   G  67  ? 0.51177 0.51177 0.51177 0.00000  0.00000  0.00000  67  PHE   C CE2 
9111  C CZ  . PHE   G  67  ? 0.34782 0.34782 0.34782 -0.00000 0.00000  0.00000  67  PHE   C CZ  
9112  N N   . ILE   G  68  ? 0.45296 0.45296 0.45296 0.00000  0.00000  0.00000  68  ILE   C N   
9113  C CA  . ILE   G  68  ? 0.48059 0.48059 0.48059 0.00000  0.00000  0.00000  68  ILE   C CA  
9114  C C   . ILE   G  68  ? 0.55769 0.55769 0.55769 -0.00000 -0.00000 0.00000  68  ILE   C C   
9115  O O   . ILE   G  68  ? 0.52770 0.52770 0.52770 -0.00000 0.00000  0.00000  68  ILE   C O   
9116  C CB  . ILE   G  68  ? 0.35289 0.35289 0.35289 0.00000  0.00000  0.00000  68  ILE   C CB  
9117  C CG1 . ILE   G  68  ? 0.44280 0.44280 0.44280 0.00000  0.00000  0.00000  68  ILE   C CG1 
9118  C CG2 . ILE   G  68  ? 0.42117 0.42117 0.42117 0.00000  0.00000  0.00000  68  ILE   C CG2 
9119  C CD1 . ILE   G  68  ? 0.35387 0.35387 0.35387 0.00000  0.00000  0.00000  68  ILE   C CD1 
9120  N N   . GLU   G  69  ? 0.95655 0.95655 0.95655 0.00000  0.00000  0.00000  69  GLU   C N   
9121  C CA  . GLU   G  69  ? 0.63439 0.63439 0.63439 -0.00000 0.00000  0.00000  69  GLU   C CA  
9122  C C   . GLU   G  69  ? 0.75282 0.75282 0.75282 -0.00000 -0.00000 0.00000  69  GLU   C C   
9123  O O   . GLU   G  69  ? 0.75924 0.75924 0.75924 0.00000  0.00000  0.00000  69  GLU   C O   
9124  C CB  . GLU   G  69  ? 0.71469 0.71469 0.71469 0.00000  0.00000  0.00000  69  GLU   C CB  
9125  C CG  . GLU   G  69  ? 0.53747 0.53747 0.53747 -0.00000 0.00000  0.00000  69  GLU   C CG  
9126  C CD  . GLU   G  69  ? 1.05941 1.05941 1.05941 0.00000  0.00000  0.00000  69  GLU   C CD  
9127  O OE1 . GLU   G  69  ? 0.71045 0.71045 0.71045 0.00000  0.00000  0.00000  69  GLU   C OE1 
9128  O OE2 . GLU   G  69  ? 0.79666 0.79666 0.79666 -0.00000 0.00000  0.00000  69  GLU   C OE2 
9129  N N   . SER   G  70  ? 0.59948 0.59948 0.59948 -0.00000 0.00000  0.00000  70  SER   C N   
9130  C CA  . SER   G  70  ? 0.24210 0.24210 0.24210 -0.00000 0.00000  0.00000  70  SER   C CA  
9131  C C   . SER   G  70  ? 0.60637 0.60637 0.60637 0.00000  0.00000  0.00000  70  SER   C C   
9132  O O   . SER   G  70  ? 0.41301 0.41301 0.41301 0.00000  0.00000  0.00000  70  SER   C O   
9133  C CB  . SER   G  70  ? 0.40166 0.40166 0.40166 -0.00000 0.00000  -0.00000 70  SER   C CB  
9134  O OG  . SER   G  70  ? 0.67190 0.67190 0.67190 0.00000  0.00000  0.00000  70  SER   C OG  
9135  N N   . ASP   G  71  ? 0.62641 0.62641 0.62641 0.00000  0.00000  0.00000  71  ASP   C N   
9136  C CA  . ASP   G  71  ? 0.56666 0.56666 0.56666 0.00000  0.00000  0.00000  71  ASP   C CA  
9137  C C   . ASP   G  71  ? 0.64606 0.64606 0.64606 0.00000  0.00000  0.00000  71  ASP   C C   
9138  O O   . ASP   G  71  ? 0.64483 0.64483 0.64483 -0.00000 0.00000  0.00000  71  ASP   C O   
9139  C CB  . ASP   G  71  ? 0.68275 0.68275 0.68275 0.00000  0.00000  0.00000  71  ASP   C CB  
9140  C CG  . ASP   G  71  ? 1.17998 1.17998 1.17998 0.00000  0.00000  0.00000  71  ASP   C CG  
9141  O OD1 . ASP   G  71  ? 0.72307 0.72307 0.72307 -0.00000 0.00000  0.00000  71  ASP   C OD1 
9142  O OD2 . ASP   G  71  ? 0.89918 0.89918 0.89918 0.00000  -0.00000 0.00000  71  ASP   C OD2 
9143  N N   . PRO   G  72  ? 0.69444 0.69444 0.69444 0.00000  0.00000  0.00000  72  PRO   C N   
9144  C CA  . PRO   G  72  ? 0.67226 0.67226 0.67226 0.00000  0.00000  0.00000  72  PRO   C CA  
9145  C C   . PRO   G  72  ? 0.55641 0.55641 0.55641 0.00000  0.00000  0.00000  72  PRO   C C   
9146  O O   . PRO   G  72  ? 0.62910 0.62910 0.62910 -0.00000 0.00000  0.00000  72  PRO   C O   
9147  C CB  . PRO   G  72  ? 0.49771 0.49771 0.49771 -0.00000 0.00000  0.00000  72  PRO   C CB  
9148  C CG  . PRO   G  72  ? 0.57173 0.57173 0.57173 0.00000  0.00000  0.00000  72  PRO   C CG  
9149  C CD  . PRO   G  72  ? 0.39385 0.39385 0.39385 0.00000  0.00000  0.00000  72  PRO   C CD  
9150  N N   . VAL   G  73  ? 0.62989 0.62989 0.62989 -0.00000 0.00000  0.00000  73  VAL   C N   
9151  C CA  . VAL   G  73  ? 0.76903 0.76903 0.76903 0.00000  0.00000  0.00000  73  VAL   C CA  
9152  C C   . VAL   G  73  ? 0.86522 0.86522 0.86522 -0.00000 0.00000  0.00000  73  VAL   C C   
9153  O O   . VAL   G  73  ? 0.49818 0.49818 0.49818 0.00000  0.00000  0.00000  73  VAL   C O   
9154  C CB  . VAL   G  73  ? 0.72779 0.72779 0.72779 0.00000  -0.00000 0.00000  73  VAL   C CB  
9155  C CG1 . VAL   G  73  ? 0.43714 0.43714 0.43714 0.00000  0.00000  0.00000  73  VAL   C CG1 
9156  C CG2 . VAL   G  73  ? 0.40977 0.40977 0.40977 0.00000  0.00000  0.00000  73  VAL   C CG2 
9157  N N   . VAL   G  74  ? 0.65105 0.65105 0.65105 0.00000  0.00000  0.00000  74  VAL   C N   
9158  C CA  . VAL   G  74  ? 0.53197 0.53197 0.53197 0.00000  0.00000  0.00000  74  VAL   C CA  
9159  C C   . VAL   G  74  ? 0.66916 0.66916 0.66916 -0.00000 0.00000  0.00000  74  VAL   C C   
9160  O O   . VAL   G  74  ? 0.72780 0.72780 0.72780 0.00000  0.00000  0.00000  74  VAL   C O   
9161  C CB  . VAL   G  74  ? 0.55890 0.55890 0.55890 -0.00000 0.00000  0.00000  74  VAL   C CB  
9162  C CG1 . VAL   G  74  ? 0.34268 0.34268 0.34268 -0.00000 -0.00000 0.00000  74  VAL   C CG1 
9163  C CG2 . VAL   G  74  ? 0.42927 0.42927 0.42927 -0.00000 0.00000  0.00000  74  VAL   C CG2 
9164  N N   . HIS   G  75  ? 0.70075 0.70075 0.70075 -0.00000 0.00000  0.00000  75  HIS   C N   
9165  C CA  . HIS   G  75  ? 0.60830 0.60830 0.60830 0.00000  0.00000  0.00000  75  HIS   C CA  
9166  C C   . HIS   G  75  ? 0.46696 0.46696 0.46696 0.00000  0.00000  0.00000  75  HIS   C C   
9167  O O   . HIS   G  75  ? 0.55454 0.55454 0.55454 -0.00000 0.00000  0.00000  75  HIS   C O   
9168  C CB  . HIS   G  75  ? 0.50157 0.50157 0.50157 -0.00000 0.00000  0.00000  75  HIS   C CB  
9169  C CG  . HIS   G  75  ? 0.91733 0.91733 0.91733 0.00000  0.00000  0.00000  75  HIS   C CG  
9170  N ND1 . HIS   G  75  ? 1.03699 1.03699 1.03699 -0.00000 0.00000  0.00000  75  HIS   C ND1 
9171  C CD2 . HIS   G  75  ? 0.93566 0.93566 0.93566 -0.00000 0.00000  0.00000  75  HIS   C CD2 
9172  C CE1 . HIS   G  75  ? 0.87858 0.87858 0.87858 0.00000  0.00000  0.00000  75  HIS   C CE1 
9173  N NE2 . HIS   G  75  ? 0.70988 0.70988 0.70988 0.00000  0.00000  0.00000  75  HIS   C NE2 
9174  N N   . GLN   G  76  ? 0.72945 0.72945 0.72945 -0.00000 0.00000  0.00000  76  GLN   C N   
9175  C CA  . GLN   G  76  ? 0.45936 0.45936 0.45936 0.00000  0.00000  0.00000  76  GLN   C CA  
9176  C C   . GLN   G  76  ? 0.75312 0.75312 0.75312 -0.00000 0.00000  0.00000  76  GLN   C C   
9177  O O   . GLN   G  76  ? 0.61719 0.61719 0.61719 0.00000  0.00000  0.00000  76  GLN   C O   
9178  C CB  . GLN   G  76  ? 0.78132 0.78132 0.78132 -0.00000 0.00000  0.00000  76  GLN   C CB  
9179  C CG  . GLN   G  76  ? 0.47708 0.47708 0.47708 0.00000  0.00000  0.00000  76  GLN   C CG  
9180  C CD  . GLN   G  76  ? 1.21507 1.21507 1.21507 0.00000  0.00000  0.00000  76  GLN   C CD  
9181  O OE1 . GLN   G  76  ? 0.70398 0.70398 0.70398 0.00000  0.00000  0.00000  76  GLN   C OE1 
9182  N NE2 . GLN   G  76  ? 0.60362 0.60362 0.60362 0.00000  0.00000  0.00000  76  GLN   C NE2 
9183  N N   . GLU   G  77  ? 0.65066 0.65066 0.65066 0.00000  0.00000  0.00000  77  GLU   C N   
9184  C CA  . GLU   G  77  ? 0.53659 0.53659 0.53659 -0.00000 0.00000  0.00000  77  GLU   C CA  
9185  C C   . GLU   G  77  ? 0.88312 0.88312 0.88312 0.00000  0.00000  0.00000  77  GLU   C C   
9186  O O   . GLU   G  77  ? 0.46018 0.46018 0.46018 0.00000  0.00000  0.00000  77  GLU   C O   
9187  C CB  . GLU   G  77  ? 0.53078 0.53078 0.53078 0.00000  0.00000  0.00000  77  GLU   C CB  
9188  C CG  . GLU   G  77  ? 0.46866 0.46866 0.46866 0.00000  0.00000  0.00000  77  GLU   C CG  
9189  C CD  . GLU   G  77  ? 0.87887 0.87887 0.87887 0.00000  0.00000  0.00000  77  GLU   C CD  
9190  O OE1 . GLU   G  77  ? 0.64658 0.64658 0.64658 0.00000  0.00000  0.00000  77  GLU   C OE1 
9191  O OE2 . GLU   G  77  ? 0.56753 0.56753 0.56753 0.00000  0.00000  0.00000  77  GLU   C OE2 
9192  N N   . PHE   G  78  ? 0.42285 0.42285 0.42285 0.00000  0.00000  0.00000  78  PHE   C N   
9193  C CA  . PHE   G  78  ? 0.68966 0.68966 0.68966 0.00000  0.00000  0.00000  78  PHE   C CA  
9194  C C   . PHE   G  78  ? 0.68038 0.68038 0.68038 0.00000  0.00000  0.00000  78  PHE   C C   
9195  O O   . PHE   G  78  ? 0.77741 0.77741 0.77741 0.00000  0.00000  0.00000  78  PHE   C O   
9196  C CB  . PHE   G  78  ? 0.44368 0.44368 0.44368 0.00000  0.00000  0.00000  78  PHE   C CB  
9197  C CG  . PHE   G  78  ? 0.67746 0.67746 0.67746 -0.00000 0.00000  0.00000  78  PHE   C CG  
9198  C CD1 . PHE   G  78  ? 0.50443 0.50443 0.50443 -0.00000 0.00000  0.00000  78  PHE   C CD1 
9199  C CD2 . PHE   G  78  ? 0.35816 0.35816 0.35816 -0.00000 0.00000  0.00000  78  PHE   C CD2 
9200  C CE1 . PHE   G  78  ? 0.47784 0.47784 0.47784 0.00000  0.00000  0.00000  78  PHE   C CE1 
9201  C CE2 . PHE   G  78  ? 0.60873 0.60873 0.60873 0.00000  0.00000  0.00000  78  PHE   C CE2 
9202  C CZ  . PHE   G  78  ? 0.44923 0.44923 0.44923 0.00000  0.00000  0.00000  78  PHE   C CZ  
9203  N N   . ILE   G  79  ? 0.66431 0.66431 0.66431 0.00000  0.00000  0.00000  79  ILE   C N   
9204  C CA  . ILE   G  79  ? 0.58388 0.58388 0.58388 0.00000  0.00000  0.00000  79  ILE   C CA  
9205  C C   . ILE   G  79  ? 0.79584 0.79584 0.79584 0.00000  0.00000  0.00000  79  ILE   C C   
9206  O O   . ILE   G  79  ? 0.49611 0.49611 0.49611 -0.00000 0.00000  0.00000  79  ILE   C O   
9207  C CB  . ILE   G  79  ? 0.69489 0.69489 0.69489 0.00000  0.00000  0.00000  79  ILE   C CB  
9208  C CG1 . ILE   G  79  ? 0.52324 0.52324 0.52324 0.00000  0.00000  0.00000  79  ILE   C CG1 
9209  C CG2 . ILE   G  79  ? 0.53341 0.53341 0.53341 0.00000  0.00000  0.00000  79  ILE   C CG2 
9210  C CD1 . ILE   G  79  ? 0.48840 0.48840 0.48840 0.00000  0.00000  0.00000  79  ILE   C CD1 
9211  N N   . ASP   G  80  ? 0.48064 0.48064 0.48064 -0.00000 -0.00000 0.00000  80  ASP   C N   
9212  C CA  . ASP   G  80  ? 0.68455 0.68455 0.68455 0.00000  0.00000  0.00000  80  ASP   C CA  
9213  C C   . ASP   G  80  ? 0.57280 0.57280 0.57280 0.00000  0.00000  0.00000  80  ASP   C C   
9214  O O   . ASP   G  80  ? 0.68873 0.68873 0.68873 0.00000  0.00000  0.00000  80  ASP   C O   
9215  C CB  . ASP   G  80  ? 0.60603 0.60603 0.60603 0.00000  0.00000  0.00000  80  ASP   C CB  
9216  C CG  . ASP   G  80  ? 0.83769 0.83769 0.83769 0.00000  0.00000  0.00000  80  ASP   C CG  
9217  O OD1 . ASP   G  80  ? 0.81472 0.81472 0.81472 0.00000  -0.00000 0.00000  80  ASP   C OD1 
9218  O OD2 . ASP   G  80  ? 0.91213 0.91213 0.91213 -0.00000 0.00000  0.00000  80  ASP   C OD2 
9219  N N   . MET   G  81  ? 0.60612 0.60612 0.60612 -0.00000 0.00000  0.00000  81  MET   C N   
9220  C CA  . MET   G  81  ? 0.52640 0.52640 0.52640 -0.00000 0.00000  0.00000  81  MET   C CA  
9221  C C   . MET   G  81  ? 0.81484 0.81484 0.81484 0.00000  0.00000  0.00000  81  MET   C C   
9222  O O   . MET   G  81  ? 0.65477 0.65477 0.65477 -0.00000 0.00000  0.00000  81  MET   C O   
9223  C CB  . MET   G  81  ? 0.52646 0.52646 0.52646 0.00000  0.00000  0.00000  81  MET   C CB  
9224  C CG  . MET   G  81  ? 0.60831 0.60831 0.60831 0.00000  -0.00000 -0.00000 81  MET   C CG  
9225  S SD  . MET   G  81  ? 0.60684 0.60684 0.60684 0.00000  0.00000  0.00000  81  MET   C SD  
9226  C CE  . MET   G  81  ? 0.56401 0.56401 0.56401 0.00000  0.00000  0.00000  81  MET   C CE  
9227  N N   . PHE   G  82  ? 0.49089 0.49089 0.49089 0.00000  0.00000  0.00000  82  PHE   C N   
9228  C CA  . PHE   G  82  ? 0.81259 0.81259 0.81259 -0.00000 0.00000  0.00000  82  PHE   C CA  
9229  C C   . PHE   G  82  ? 0.46887 0.46887 0.46887 -0.00000 0.00000  0.00000  82  PHE   C C   
9230  O O   . PHE   G  82  ? 1.27161 1.27161 1.27161 -0.00000 0.00000  0.00000  82  PHE   C O   
9231  C CB  . PHE   G  82  ? 0.50220 0.50220 0.50220 0.00000  0.00000  0.00000  82  PHE   C CB  
9232  C CG  . PHE   G  82  ? 1.04876 1.04876 1.04876 0.00000  0.00000  0.00000  82  PHE   C CG  
9233  C CD1 . PHE   G  82  ? 0.46522 0.46522 0.46522 -0.00000 -0.00000 0.00000  82  PHE   C CD1 
9234  C CD2 . PHE   G  82  ? 0.49830 0.49830 0.49830 -0.00000 0.00000  0.00000  82  PHE   C CD2 
9235  C CE1 . PHE   G  82  ? 0.70285 0.70285 0.70285 -0.00000 -0.00000 0.00000  82  PHE   C CE1 
9236  C CE2 . PHE   G  82  ? 0.71890 0.71890 0.71890 -0.00000 0.00000  0.00000  82  PHE   C CE2 
9237  C CZ  . PHE   G  82  ? 0.41119 0.41119 0.41119 -0.00000 0.00000  0.00000  82  PHE   C CZ  
9238  N N   . GLU   G  83  ? 0.78850 0.78850 0.78850 0.00000  0.00000  0.00000  83  GLU   C N   
9239  C CA  . GLU   G  83  ? 0.84885 0.84885 0.84885 -0.00000 0.00000  0.00000  83  GLU   C CA  
9240  C C   . GLU   G  83  ? 0.95433 0.95433 0.95433 0.00000  0.00000  0.00000  83  GLU   C C   
9241  O O   . GLU   G  83  ? 0.65372 0.65372 0.65372 -0.00000 0.00000  0.00000  83  GLU   C O   
9242  C CB  . GLU   G  83  ? 0.53645 0.53645 0.53645 0.00000  0.00000  0.00000  83  GLU   C CB  
9243  C CG  . GLU   G  83  ? 1.35654 1.35654 1.35654 0.00000  0.00000  0.00000  83  GLU   C CG  
9244  C CD  . GLU   G  83  ? 1.31873 1.31873 1.31873 0.00000  0.00000  0.00000  83  GLU   C CD  
9245  O OE1 . GLU   G  83  ? 1.40507 1.40507 1.40507 0.00000  0.00000  0.00000  83  GLU   C OE1 
9246  O OE2 . GLU   G  83  ? 0.50818 0.50818 0.50818 0.00000  0.00000  0.00000  83  GLU   C OE2 
9247  N N   . GLY   G  84  ? 1.04309 1.04309 1.04309 0.00000  0.00000  0.00000  84  GLY   C N   
9248  C CA  . GLY   G  84  ? 0.59167 0.59167 0.59167 0.00000  0.00000  0.00000  84  GLY   C CA  
9249  C C   . GLY   G  84  ? 1.01071 1.01071 1.01071 0.00000  0.00000  0.00000  84  GLY   C C   
9250  O O   . GLY   G  84  ? 0.82221 0.82221 0.82221 0.00000  0.00000  0.00000  84  GLY   C O   
9251  N N   . ILE   G  85  ? 1.13293 1.13293 1.13293 0.00000  0.00000  0.00000  85  ILE   C N   
9252  C CA  . ILE   G  85  ? 0.87469 0.87469 0.87469 0.00000  0.00000  0.00000  85  ILE   C CA  
9253  C C   . ILE   G  85  ? 1.00399 1.00399 1.00399 0.00000  0.00000  0.00000  85  ILE   C C   
9254  O O   . ILE   G  85  ? 0.92986 0.92986 0.92986 0.00000  0.00000  0.00000  85  ILE   C O   
9255  C CB  . ILE   G  85  ? 0.79130 0.79130 0.79130 0.00000  -0.00000 -0.00000 85  ILE   C CB  
9256  C CG1 . ILE   G  85  ? 0.98476 0.98476 0.98476 0.00000  0.00000  0.00000  85  ILE   C CG1 
9257  C CG2 . ILE   G  85  ? 0.81810 0.81810 0.81810 0.00000  0.00000  0.00000  85  ILE   C CG2 
9258  C CD1 . ILE   G  85  ? 0.88224 0.88224 0.88224 0.00000  0.00000  0.00000  85  ILE   C CD1 
9259  N N   . GLN   G  86  ? 0.85675 0.85675 0.85675 0.00000  0.00000  0.00000  86  GLN   C N   
9260  C CA  . GLN   G  86  ? 1.25716 1.25716 1.25716 0.00000  0.00000  0.00000  86  GLN   C CA  
9261  C C   . GLN   G  86  ? 0.63453 0.63453 0.63453 0.00000  0.00000  0.00000  86  GLN   C C   
9262  O O   . GLN   G  86  ? 1.22595 1.22595 1.22595 0.00000  0.00000  0.00000  86  GLN   C O   
9263  C CB  . GLN   G  86  ? 0.80293 0.80293 0.80293 -0.00000 0.00000  0.00000  86  GLN   C CB  
9264  C CG  . GLN   G  86  ? 1.73341 1.73341 1.73341 0.00000  0.00000  0.00000  86  GLN   C CG  
9265  C CD  . GLN   G  86  ? 2.15696 2.15696 2.15696 -0.00000 0.00000  -0.00000 86  GLN   C CD  
9266  O OE1 . GLN   G  86  ? 2.04736 2.04736 2.04736 -0.00000 0.00000  0.00000  86  GLN   C OE1 
9267  N NE2 . GLN   G  86  ? 1.95579 1.95579 1.95579 -0.00000 0.00000  0.00000  86  GLN   C NE2 
9268  N N   . ASP   G  87  ? 1.26722 1.26722 1.26722 -0.00000 0.00000  0.00000  87  ASP   C N   
9269  C CA  . ASP   G  87  ? 0.84005 0.84005 0.84005 0.00000  0.00000  0.00000  87  ASP   C CA  
9270  C C   . ASP   G  87  ? 0.70266 0.70266 0.70266 0.00000  0.00000  0.00000  87  ASP   C C   
9271  O O   . ASP   G  87  ? 0.96087 0.96087 0.96087 0.00000  0.00000  0.00000  87  ASP   C O   
9272  C CB  . ASP   G  87  ? 0.74195 0.74195 0.74195 -0.00000 0.00000  0.00000  87  ASP   C CB  
9273  C CG  . ASP   G  87  ? 1.66354 1.66354 1.66354 0.00000  0.00000  0.00000  87  ASP   C CG  
9274  O OD1 . ASP   G  87  ? 1.41347 1.41347 1.41347 0.00000  0.00000  0.00000  87  ASP   C OD1 
9275  O OD2 . ASP   G  87  ? 1.38864 1.38864 1.38864 -0.00000 0.00000  0.00000  87  ASP   C OD2 
9276  N N   . SER   G  88  ? 0.78124 0.78124 0.78124 -0.00000 0.00000  0.00000  88  SER   C N   
9277  C CA  . SER   G  88  ? 0.64290 0.64290 0.64290 -0.00000 0.00000  0.00000  88  SER   C CA  
9278  C C   . SER   G  88  ? 1.17976 1.17976 1.17976 -0.00000 0.00000  0.00000  88  SER   C C   
9279  O O   . SER   G  88  ? 0.76815 0.76815 0.76815 0.00000  0.00000  0.00000  88  SER   C O   
9280  C CB  . SER   G  88  ? 0.65619 0.65619 0.65619 -0.00000 0.00000  0.00000  88  SER   C CB  
9281  O OG  . SER   G  88  ? 0.86048 0.86048 0.86048 0.00000  0.00000  0.00000  88  SER   C OG  
9282  N N   . PRO   G  89  ? 0.72391 0.72391 0.72391 0.00000  -0.00000 0.00000  89  PRO   C N   
9283  C CA  . PRO   G  89  ? 0.42649 0.42649 0.42649 0.00000  0.00000  0.00000  89  PRO   C CA  
9284  C C   . PRO   G  89  ? 0.77738 0.77738 0.77738 0.00000  0.00000  0.00000  89  PRO   C C   
9285  O O   . PRO   G  89  ? 0.55699 0.55699 0.55699 -0.00000 -0.00000 0.00000  89  PRO   C O   
9286  C CB  . PRO   G  89  ? 0.70980 0.70980 0.70980 -0.00000 0.00000  0.00000  89  PRO   C CB  
9287  C CG  . PRO   G  89  ? 0.68028 0.68028 0.68028 0.00000  0.00000  -0.00000 89  PRO   C CG  
9288  C CD  . PRO   G  89  ? 0.61184 0.61184 0.61184 0.00000  0.00000  0.00000  89  PRO   C CD  
9289  N N   . ARG   G  90  ? 0.45685 0.45685 0.45685 0.00000  0.00000  0.00000  90  ARG   C N   
9290  C CA  . ARG   G  90  ? 0.67215 0.67215 0.67215 -0.00000 0.00000  0.00000  90  ARG   C CA  
9291  C C   . ARG   G  90  ? 0.55417 0.55417 0.55417 0.00000  0.00000  0.00000  90  ARG   C C   
9292  O O   . ARG   G  90  ? 0.54894 0.54894 0.54894 0.00000  0.00000  0.00000  90  ARG   C O   
9293  C CB  . ARG   G  90  ? 0.47446 0.47446 0.47446 0.00000  0.00000  0.00000  90  ARG   C CB  
9294  C CG  . ARG   G  90  ? 1.08185 1.08185 1.08185 -0.00000 0.00000  0.00000  90  ARG   C CG  
9295  C CD  . ARG   G  90  ? 1.18765 1.18765 1.18765 0.00000  0.00000  0.00000  90  ARG   C CD  
9296  N NE  . ARG   G  90  ? 1.58541 1.58541 1.58541 -0.00000 0.00000  0.00000  90  ARG   C NE  
9297  C CZ  . ARG   G  90  ? 1.41229 1.41229 1.41229 -0.00000 0.00000  0.00000  90  ARG   C CZ  
9298  N NH1 . ARG   G  90  ? 1.06952 1.06952 1.06952 -0.00000 0.00000  0.00000  90  ARG   C NH1 
9299  N NH2 . ARG   G  90  ? 1.47289 1.47289 1.47289 0.00000  0.00000  0.00000  90  ARG   C NH2 
9300  N N   . ASN   G  91  ? 0.50308 0.50308 0.50308 0.00000  0.00000  0.00000  91  ASN   C N   
9301  C CA  . ASN   G  91  ? 0.55982 0.55982 0.55982 0.00000  0.00000  0.00000  91  ASN   C CA  
9302  C C   . ASN   G  91  ? 0.54243 0.54243 0.54243 -0.00000 0.00000  0.00000  91  ASN   C C   
9303  O O   . ASN   G  91  ? 0.62543 0.62543 0.62543 0.00000  0.00000  0.00000  91  ASN   C O   
9304  C CB  . ASN   G  91  ? 0.45852 0.45852 0.45852 0.00000  0.00000  0.00000  91  ASN   C CB  
9305  C CG  . ASN   G  91  ? 0.59375 0.59375 0.59375 0.00000  0.00000  0.00000  91  ASN   C CG  
9306  O OD1 . ASN   G  91  ? 0.72281 0.72281 0.72281 0.00000  0.00000  0.00000  91  ASN   C OD1 
9307  N ND2 . ASN   G  91  ? 0.54342 0.54342 0.54342 0.00000  0.00000  0.00000  91  ASN   C ND2 
9308  N N   . TYR   G  92  ? 0.61669 0.61669 0.61669 0.00000  0.00000  0.00000  92  TYR   C N   
9309  C CA  . TYR   G  92  ? 0.53743 0.53743 0.53743 0.00000  0.00000  0.00000  92  TYR   C CA  
9310  C C   . TYR   G  92  ? 0.58928 0.58928 0.58928 0.00000  -0.00000 -0.00000 92  TYR   C C   
9311  O O   . TYR   G  92  ? 0.64901 0.64901 0.64901 0.00000  -0.00000 -0.00000 92  TYR   C O   
9312  C CB  . TYR   G  92  ? 0.40086 0.40086 0.40086 0.00000  0.00000  0.00000  92  TYR   C CB  
9313  C CG  . TYR   G  92  ? 0.47009 0.47009 0.47009 0.00000  0.00000  0.00000  92  TYR   C CG  
9314  C CD1 . TYR   G  92  ? 0.44752 0.44752 0.44752 0.00000  0.00000  0.00000  92  TYR   C CD1 
9315  C CD2 . TYR   G  92  ? 0.55158 0.55158 0.55158 -0.00000 -0.00000 0.00000  92  TYR   C CD2 
9316  C CE1 . TYR   G  92  ? 0.68792 0.68792 0.68792 0.00000  0.00000  0.00000  92  TYR   C CE1 
9317  C CE2 . TYR   G  92  ? 0.65113 0.65113 0.65113 0.00000  -0.00000 0.00000  92  TYR   C CE2 
9318  C CZ  . TYR   G  92  ? 0.59469 0.59469 0.59469 -0.00000 0.00000  0.00000  92  TYR   C CZ  
9319  O OH  . TYR   G  92  ? 0.80691 0.80691 0.80691 0.00000  0.00000  0.00000  92  TYR   C OH  
9320  N N   . GLN   G  93  ? 0.57175 0.57175 0.57175 -0.00000 0.00000  0.00000  93  GLN   C N   
9321  C CA  . GLN   G  93  ? 0.73143 0.73143 0.73143 0.00000  0.00000  0.00000  93  GLN   C CA  
9322  C C   . GLN   G  93  ? 0.55473 0.55473 0.55473 0.00000  0.00000  0.00000  93  GLN   C C   
9323  O O   . GLN   G  93  ? 0.62325 0.62325 0.62325 0.00000  -0.00000 0.00000  93  GLN   C O   
9324  C CB  . GLN   G  93  ? 0.48919 0.48919 0.48919 0.00000  0.00000  0.00000  93  GLN   C CB  
9325  C CG  . GLN   G  93  ? 0.70108 0.70108 0.70108 -0.00000 0.00000  0.00000  93  GLN   C CG  
9326  C CD  . GLN   G  93  ? 2.21212 2.21212 2.21212 0.00000  0.00000  0.00000  93  GLN   C CD  
9327  O OE1 . GLN   G  93  ? 0.67043 0.67043 0.67043 0.00000  0.00000  0.00000  93  GLN   C OE1 
9328  N NE2 . GLN   G  93  ? 0.69853 0.69853 0.69853 0.00000  0.00000  0.00000  93  GLN   C NE2 
9329  N N   . GLU   G  94  ? 0.61448 0.61448 0.61448 0.00000  0.00000  0.00000  94  GLU   C N   
9330  C CA  . GLU   G  94  ? 0.26419 0.26419 0.26419 0.00000  -0.00000 0.00000  94  GLU   C CA  
9331  C C   . GLU   G  94  ? 0.70121 0.70121 0.70121 0.00000  0.00000  0.00000  94  GLU   C C   
9332  O O   . GLU   G  94  ? 0.66396 0.66396 0.66396 0.00000  0.00000  0.00000  94  GLU   C O   
9333  C CB  . GLU   G  94  ? 0.66240 0.66240 0.66240 -0.00000 -0.00000 -0.00000 94  GLU   C CB  
9334  C CG  . GLU   G  94  ? 0.93524 0.93524 0.93524 -0.00000 0.00000  -0.00000 94  GLU   C CG  
9335  C CD  . GLU   G  94  ? 1.72933 1.72933 1.72933 0.00000  0.00000  0.00000  94  GLU   C CD  
9336  O OE1 . GLU   G  94  ? 0.57004 0.57004 0.57004 -0.00000 0.00000  0.00000  94  GLU   C OE1 
9337  O OE2 . GLU   G  94  ? 1.25025 1.25025 1.25025 0.00000  0.00000  0.00000  94  GLU   C OE2 
9338  N N   . LEU   G  95  ? 0.76099 0.76099 0.76099 0.00000  -0.00000 0.00000  95  LEU   C N   
9339  C CA  . LEU   G  95  ? 0.52089 0.52089 0.52089 0.00000  0.00000  0.00000  95  LEU   C CA  
9340  C C   . LEU   G  95  ? 0.57318 0.57318 0.57318 0.00000  0.00000  0.00000  95  LEU   C C   
9341  O O   . LEU   G  95  ? 0.52264 0.52264 0.52264 -0.00000 0.00000  0.00000  95  LEU   C O   
9342  C CB  . LEU   G  95  ? 0.61093 0.61093 0.61093 0.00000  0.00000  0.00000  95  LEU   C CB  
9343  C CG  . LEU   G  95  ? 0.61178 0.61178 0.61178 0.00000  0.00000  0.00000  95  LEU   C CG  
9344  C CD1 . LEU   G  95  ? 0.53945 0.53945 0.53945 -0.00000 0.00000  0.00000  95  LEU   C CD1 
9345  C CD2 . LEU   G  95  ? 0.42798 0.42798 0.42798 0.00000  0.00000  0.00000  95  LEU   C CD2 
9346  N N   . CYS   G  96  ? 0.32652 0.32652 0.32652 -0.00000 0.00000  0.00000  96  CYS   C N   
9347  C CA  . CYS   G  96  ? 0.46317 0.46317 0.46317 -0.00000 0.00000  0.00000  96  CYS   C CA  
9348  C C   . CYS   G  96  ? 0.46569 0.46569 0.46569 0.00000  0.00000  0.00000  96  CYS   C C   
9349  O O   . CYS   G  96  ? 0.71062 0.71062 0.71062 -0.00000 0.00000  0.00000  96  CYS   C O   
9350  C CB  . CYS   G  96  ? 0.38127 0.38127 0.38127 -0.00000 0.00000  0.00000  96  CYS   C CB  
9351  S SG  . CYS   G  96  ? 0.58016 0.58016 0.58016 0.00000  0.00000  0.00000  96  CYS   C SG  
9352  N N   . ASN   G  97  ? 0.45958 0.45958 0.45958 -0.00000 0.00000  0.00000  97  ASN   C N   
9353  C CA  . ASN   G  97  ? 0.33635 0.33635 0.33635 0.00000  0.00000  0.00000  97  ASN   C CA  
9354  C C   . ASN   G  97  ? 0.65082 0.65082 0.65082 0.00000  0.00000  0.00000  97  ASN   C C   
9355  O O   . ASN   G  97  ? 0.41540 0.41540 0.41540 0.00000  0.00000  -0.00000 97  ASN   C O   
9356  C CB  . ASN   G  97  ? 0.48233 0.48233 0.48233 -0.00000 0.00000  0.00000  97  ASN   C CB  
9357  C CG  . ASN   G  97  ? 0.98229 0.98229 0.98229 0.00000  0.00000  0.00000  97  ASN   C CG  
9358  O OD1 . ASN   G  97  ? 0.63483 0.63483 0.63483 -0.00000 0.00000  0.00000  97  ASN   C OD1 
9359  N ND2 . ASN   G  97  ? 0.44492 0.44492 0.44492 -0.00000 0.00000  0.00000  97  ASN   C ND2 
9360  N N   . MET   G  98  ? 0.35760 0.35760 0.35760 -0.00000 0.00000  0.00000  98  MET   C N   
9361  C CA  . MET   G  98  ? 0.31112 0.31112 0.31112 0.00000  0.00000  0.00000  98  MET   C CA  
9362  C C   . MET   G  98  ? 0.79297 0.79297 0.79297 -0.00000 0.00000  0.00000  98  MET   C C   
9363  O O   . MET   G  98  ? 0.53788 0.53788 0.53788 -0.00000 0.00000  0.00000  98  MET   C O   
9364  C CB  . MET   G  98  ? 0.39796 0.39796 0.39796 0.00000  -0.00000 0.00000  98  MET   C CB  
9365  C CG  . MET   G  98  ? 0.25857 0.25857 0.25857 0.00000  0.00000  0.00000  98  MET   C CG  
9366  S SD  . MET   G  98  ? 0.65251 0.65251 0.65251 0.00000  0.00000  0.00000  98  MET   C SD  
9367  C CE  . MET   G  98  ? 0.48404 0.48404 0.48404 -0.00000 0.00000  0.00000  98  MET   C CE  
9368  N N   . PHE   G  99  ? 0.45029 0.45029 0.45029 0.00000  0.00000  0.00000  99  PHE   C N   
9369  C CA  . PHE   G  99  ? 0.39999 0.39999 0.39999 -0.00000 0.00000  0.00000  99  PHE   C CA  
9370  C C   . PHE   G  99  ? 0.51838 0.51838 0.51838 -0.00000 -0.00000 -0.00000 99  PHE   C C   
9371  O O   . PHE   G  99  ? 0.50400 0.50400 0.50400 -0.00000 0.00000  0.00000  99  PHE   C O   
9372  C CB  . PHE   G  99  ? 0.38068 0.38068 0.38068 0.00000  0.00000  0.00000  99  PHE   C CB  
9373  C CG  . PHE   G  99  ? 0.48470 0.48470 0.48470 0.00000  -0.00000 0.00000  99  PHE   C CG  
9374  C CD1 . PHE   G  99  ? 0.35584 0.35584 0.35584 0.00000  0.00000  0.00000  99  PHE   C CD1 
9375  C CD2 . PHE   G  99  ? 0.46761 0.46761 0.46761 -0.00000 0.00000  0.00000  99  PHE   C CD2 
9376  C CE1 . PHE   G  99  ? 0.55272 0.55272 0.55272 0.00000  0.00000  0.00000  99  PHE   C CE1 
9377  C CE2 . PHE   G  99  ? 0.34493 0.34493 0.34493 -0.00000 0.00000  0.00000  99  PHE   C CE2 
9378  C CZ  . PHE   G  99  ? 0.39691 0.39691 0.39691 0.00000  0.00000  0.00000  99  PHE   C CZ  
9379  N N   . ASN   G  100 ? 0.40812 0.40812 0.40812 0.00000  0.00000  0.00000  100 ASN   C N   
9380  C CA  . ASN   G  100 ? 0.46198 0.46198 0.46198 -0.00000 0.00000  0.00000  100 ASN   C CA  
9381  C C   . ASN   G  100 ? 0.50992 0.50992 0.50992 0.00000  0.00000  0.00000  100 ASN   C C   
9382  O O   . ASN   G  100 ? 0.60181 0.60181 0.60181 -0.00000 0.00000  0.00000  100 ASN   C O   
9383  C CB  . ASN   G  100 ? 0.45550 0.45550 0.45550 0.00000  0.00000  0.00000  100 ASN   C CB  
9384  C CG  . ASN   G  100 ? 0.60054 0.60054 0.60054 -0.00000 0.00000  0.00000  100 ASN   C CG  
9385  O OD1 . ASN   G  100 ? 0.76071 0.76071 0.76071 -0.00000 0.00000  0.00000  100 ASN   C OD1 
9386  N ND2 . ASN   G  100 ? 0.59648 0.59648 0.59648 0.00000  0.00000  0.00000  100 ASN   C ND2 
9387  N N   . ASP   G  101 ? 0.48525 0.48525 0.48525 0.00000  0.00000  0.00000  101 ASP   C N   
9388  C CA  . ASP   G  101 ? 0.40579 0.40579 0.40579 0.00000  0.00000  0.00000  101 ASP   C CA  
9389  C C   . ASP   G  101 ? 0.69279 0.69279 0.69279 0.00000  0.00000  0.00000  101 ASP   C C   
9390  O O   . ASP   G  101 ? 0.58734 0.58734 0.58734 0.00000  0.00000  0.00000  101 ASP   C O   
9391  C CB  . ASP   G  101 ? 0.40674 0.40674 0.40674 -0.00000 0.00000  0.00000  101 ASP   C CB  
9392  C CG  . ASP   G  101 ? 1.45491 1.45491 1.45491 -0.00000 0.00000  0.00000  101 ASP   C CG  
9393  O OD1 . ASP   G  101 ? 0.63534 0.63534 0.63534 0.00000  0.00000  0.00000  101 ASP   C OD1 
9394  O OD2 . ASP   G  101 ? 0.75765 0.75765 0.75765 0.00000  0.00000  0.00000  101 ASP   C OD2 
9395  N N   . ILE   G  102 ? 0.54703 0.54703 0.54703 0.00000  0.00000  0.00000  102 ILE   C N   
9396  C CA  . ILE   G  102 ? 0.35017 0.35017 0.35017 0.00000  0.00000  0.00000  102 ILE   C CA  
9397  C C   . ILE   G  102 ? 0.67391 0.67391 0.67391 0.00000  0.00000  0.00000  102 ILE   C C   
9398  O O   . ILE   G  102 ? 0.46541 0.46541 0.46541 -0.00000 0.00000  0.00000  102 ILE   C O   
9399  C CB  . ILE   G  102 ? 0.38599 0.38599 0.38599 0.00000  0.00000  0.00000  102 ILE   C CB  
9400  C CG1 . ILE   G  102 ? 0.19370 0.19370 0.19370 0.00000  0.00000  0.00000  102 ILE   C CG1 
9401  C CG2 . ILE   G  102 ? 0.24961 0.24961 0.24961 0.00000  -0.00000 0.00000  102 ILE   C CG2 
9402  C CD1 . ILE   G  102 ? 0.46075 0.46075 0.46075 0.00000  0.00000  0.00000  102 ILE   C CD1 
9403  N N   . PHE   G  103 ? 0.38185 0.38185 0.38185 -0.00000 0.00000  0.00000  103 PHE   C N   
9404  C CA  . PHE   G  103 ? 0.69231 0.69231 0.69231 0.00000  0.00000  0.00000  103 PHE   C CA  
9405  C C   . PHE   G  103 ? 0.41221 0.41221 0.41221 0.00000  0.00000  0.00000  103 PHE   C C   
9406  O O   . PHE   G  103 ? 0.51810 0.51810 0.51810 -0.00000 -0.00000 0.00000  103 PHE   C O   
9407  C CB  . PHE   G  103 ? 0.27953 0.27953 0.27953 0.00000  0.00000  0.00000  103 PHE   C CB  
9408  C CG  . PHE   G  103 ? 0.49810 0.49810 0.49810 -0.00000 0.00000  -0.00000 103 PHE   C CG  
9409  C CD1 . PHE   G  103 ? 0.44713 0.44713 0.44713 0.00000  0.00000  0.00000  103 PHE   C CD1 
9410  C CD2 . PHE   G  103 ? 0.34651 0.34651 0.34651 -0.00000 0.00000  0.00000  103 PHE   C CD2 
9411  C CE1 . PHE   G  103 ? 0.60225 0.60225 0.60225 0.00000  -0.00000 0.00000  103 PHE   C CE1 
9412  C CE2 . PHE   G  103 ? 0.50016 0.50016 0.50016 -0.00000 0.00000  0.00000  103 PHE   C CE2 
9413  C CZ  . PHE   G  103 ? 0.49108 0.49108 0.49108 0.00000  0.00000  0.00000  103 PHE   C CZ  
9414  N N   . ARG   G  104 ? 0.53094 0.53094 0.53094 0.00000  0.00000  0.00000  104 ARG   C N   
9415  C CA  . ARG   G  104 ? 0.53265 0.53265 0.53265 -0.00000 -0.00000 -0.00000 104 ARG   C CA  
9416  C C   . ARG   G  104 ? 0.32548 0.32548 0.32548 0.00000  0.00000  0.00000  104 ARG   C C   
9417  O O   . ARG   G  104 ? 0.86841 0.86841 0.86841 -0.00000 0.00000  0.00000  104 ARG   C O   
9418  C CB  . ARG   G  104 ? 0.79987 0.79987 0.79987 0.00000  0.00000  0.00000  104 ARG   C CB  
9419  C CG  . ARG   G  104 ? 1.10170 1.10170 1.10170 -0.00000 0.00000  0.00000  104 ARG   C CG  
9420  C CD  . ARG   G  104 ? 1.13253 1.13253 1.13253 0.00000  0.00000  0.00000  104 ARG   C CD  
9421  N NE  . ARG   G  104 ? 0.33557 0.33557 0.33557 0.00000  0.00000  0.00000  104 ARG   C NE  
9422  C CZ  . ARG   G  104 ? 1.34616 1.34616 1.34616 -0.00000 0.00000  0.00000  104 ARG   C CZ  
9423  N NH1 . ARG   G  104 ? 1.32030 1.32030 1.32030 0.00000  0.00000  0.00000  104 ARG   C NH1 
9424  N NH2 . ARG   G  104 ? 1.07093 1.07093 1.07093 0.00000  0.00000  0.00000  104 ARG   C NH2 
9425  N N   . LYS   G  105 ? 0.48430 0.48430 0.48430 0.00000  0.00000  0.00000  105 LYS   C N   
9426  C CA  . LYS   G  105 ? 0.74694 0.74694 0.74694 0.00000  0.00000  0.00000  105 LYS   C CA  
9427  C C   . LYS   G  105 ? 0.52569 0.52569 0.52569 -0.00000 0.00000  0.00000  105 LYS   C C   
9428  O O   . LYS   G  105 ? 0.58430 0.58430 0.58430 0.00000  0.00000  0.00000  105 LYS   C O   
9429  C CB  . LYS   G  105 ? 0.62304 0.62304 0.62304 0.00000  0.00000  0.00000  105 LYS   C CB  
9430  C CG  . LYS   G  105 ? 0.49569 0.49569 0.49569 -0.00000 0.00000  0.00000  105 LYS   C CG  
9431  C CD  . LYS   G  105 ? 0.50158 0.50158 0.50158 -0.00000 0.00000  0.00000  105 LYS   C CD  
9432  C CE  . LYS   G  105 ? 0.88416 0.88416 0.88416 -0.00000 0.00000  0.00000  105 LYS   C CE  
9433  N NZ  . LYS   G  105 ? 1.04694 1.04694 1.04694 0.00000  0.00000  0.00000  105 LYS   C NZ  
9434  N N   . ALA   G  106 ? 0.64325 0.64325 0.64325 0.00000  0.00000  0.00000  106 ALA   C N   
9435  C CA  . ALA   G  106 ? 0.55791 0.55791 0.55791 0.00000  0.00000  0.00000  106 ALA   C CA  
9436  C C   . ALA   G  106 ? 0.34755 0.34755 0.34755 -0.00000 0.00000  0.00000  106 ALA   C C   
9437  O O   . ALA   G  106 ? 0.59262 0.59262 0.59262 -0.00000 0.00000  0.00000  106 ALA   C O   
9438  C CB  . ALA   G  106 ? 0.38449 0.38449 0.38449 0.00000  0.00000  0.00000  106 ALA   C CB  
9439  N N   . PRO   G  107 ? 0.71003 0.71003 0.71003 0.00000  -0.00000 -0.00000 107 PRO   C N   
9440  C CA  . PRO   G  107 ? 0.48627 0.48627 0.48627 0.00000  0.00000  0.00000  107 PRO   C CA  
9441  C C   . PRO   G  107 ? 0.61143 0.61143 0.61143 0.00000  0.00000  0.00000  107 PRO   C C   
9442  O O   . PRO   G  107 ? 0.55144 0.55144 0.55144 0.00000  -0.00000 0.00000  107 PRO   C O   
9443  C CB  . PRO   G  107 ? 0.46164 0.46164 0.46164 0.00000  0.00000  0.00000  107 PRO   C CB  
9444  C CG  . PRO   G  107 ? 0.41872 0.41872 0.41872 0.00000  0.00000  0.00000  107 PRO   C CG  
9445  C CD  . PRO   G  107 ? 0.34056 0.34056 0.34056 0.00000  0.00000  0.00000  107 PRO   C CD  
9446  N N   . VAL   G  108 ? 0.52780 0.52780 0.52780 0.00000  0.00000  0.00000  108 VAL   C N   
9447  C CA  . VAL   G  108 ? 0.47545 0.47545 0.47545 -0.00000 0.00000  0.00000  108 VAL   C CA  
9448  C C   . VAL   G  108 ? 0.61770 0.61770 0.61770 0.00000  0.00000  0.00000  108 VAL   C C   
9449  O O   . VAL   G  108 ? 0.62549 0.62549 0.62549 0.00000  0.00000  0.00000  108 VAL   C O   
9450  C CB  . VAL   G  108 ? 0.60508 0.60508 0.60508 0.00000  0.00000  0.00000  108 VAL   C CB  
9451  C CG1 . VAL   G  108 ? 0.36473 0.36473 0.36473 -0.00000 0.00000  0.00000  108 VAL   C CG1 
9452  C CG2 . VAL   G  108 ? 0.36151 0.36151 0.36151 0.00000  0.00000  0.00000  108 VAL   C CG2 
9453  N N   . TYR   G  109 ? 0.49830 0.49830 0.49830 0.00000  0.00000  0.00000  109 TYR   C N   
9454  C CA  . TYR   G  109 ? 0.87133 0.87133 0.87133 0.00000  0.00000  0.00000  109 TYR   C CA  
9455  C C   . TYR   G  109 ? 0.49471 0.49471 0.49471 0.00000  0.00000  0.00000  109 TYR   C C   
9456  O O   . TYR   G  109 ? 0.67107 0.67107 0.67107 0.00000  0.00000  0.00000  109 TYR   C O   
9457  C CB  . TYR   G  109 ? 0.42067 0.42067 0.42067 0.00000  0.00000  0.00000  109 TYR   C CB  
9458  C CG  . TYR   G  109 ? 0.83615 0.83615 0.83615 0.00000  0.00000  0.00000  109 TYR   C CG  
9459  C CD1 . TYR   G  109 ? 0.43709 0.43709 0.43709 -0.00000 0.00000  0.00000  109 TYR   C CD1 
9460  C CD2 . TYR   G  109 ? 0.48748 0.48748 0.48748 0.00000  0.00000  0.00000  109 TYR   C CD2 
9461  C CE1 . TYR   G  109 ? 0.96487 0.96487 0.96487 0.00000  0.00000  0.00000  109 TYR   C CE1 
9462  C CE2 . TYR   G  109 ? 0.75524 0.75524 0.75524 0.00000  0.00000  0.00000  109 TYR   C CE2 
9463  C CZ  . TYR   G  109 ? 0.45402 0.45402 0.45402 0.00000  0.00000  0.00000  109 TYR   C CZ  
9464  O OH  . TYR   G  109 ? 0.78674 0.78674 0.78674 0.00000  0.00000  0.00000  109 TYR   C OH  
9465  N N   . GLY   G  110 ? 0.67631 0.67631 0.67631 -0.00000 0.00000  0.00000  110 GLY   C N   
9466  C CA  . GLY   G  110 ? 0.23302 0.23302 0.23302 0.00000  0.00000  0.00000  110 GLY   C CA  
9467  C C   . GLY   G  110 ? 0.65980 0.65980 0.65980 0.00000  0.00000  0.00000  110 GLY   C C   
9468  O O   . GLY   G  110 ? 0.58383 0.58383 0.58383 0.00000  0.00000  0.00000  110 GLY   C O   
9469  N N   . ASP   G  111 ? 0.77557 0.77557 0.77557 -0.00000 0.00000  0.00000  111 ASP   C N   
9470  C CA  . ASP   G  111 ? 0.65625 0.65625 0.65625 0.00000  0.00000  0.00000  111 ASP   C CA  
9471  C C   . ASP   G  111 ? 0.45420 0.45420 0.45420 -0.00000 0.00000  0.00000  111 ASP   C C   
9472  O O   . ASP   G  111 ? 0.62305 0.62305 0.62305 0.00000  0.00000  0.00000  111 ASP   C O   
9473  C CB  . ASP   G  111 ? 0.81750 0.81750 0.81750 0.00000  0.00000  0.00000  111 ASP   C CB  
9474  C CG  . ASP   G  111 ? 0.80117 0.80117 0.80117 0.00000  0.00000  0.00000  111 ASP   C CG  
9475  O OD1 . ASP   G  111 ? 1.00150 1.00150 1.00150 -0.00000 0.00000  0.00000  111 ASP   C OD1 
9476  O OD2 . ASP   G  111 ? 1.24047 1.24047 1.24047 0.00000  -0.00000 0.00000  111 ASP   C OD2 
9477  N N   . LEU   G  112 ? 0.91759 0.91759 0.91759 0.00000  0.00000  0.00000  112 LEU   C N   
9478  C CA  . LEU   G  112 ? 0.50998 0.50998 0.50998 -0.00000 0.00000  0.00000  112 LEU   C CA  
9479  C C   . LEU   G  112 ? 0.99525 0.99525 0.99525 -0.00000 0.00000  0.00000  112 LEU   C C   
9480  O O   . LEU   G  112 ? 0.53394 0.53394 0.53394 0.00000  -0.00000 0.00000  112 LEU   C O   
9481  C CB  . LEU   G  112 ? 0.48017 0.48017 0.48017 -0.00000 0.00000  0.00000  112 LEU   C CB  
9482  C CG  . LEU   G  112 ? 1.74359 1.74359 1.74359 0.00000  0.00000  0.00000  112 LEU   C CG  
9483  C CD1 . LEU   G  112 ? 1.80883 1.80883 1.80883 0.00000  0.00000  0.00000  112 LEU   C CD1 
9484  C CD2 . LEU   G  112 ? 1.48640 1.48640 1.48640 -0.00000 0.00000  0.00000  112 LEU   C CD2 
9485  N N   . GLY   G  113 ? 0.51426 0.51426 0.51426 -0.00000 0.00000  0.00000  113 GLY   C N   
9486  C CA  . GLY   G  113 ? 0.49499 0.49499 0.49499 -0.00000 0.00000  0.00000  113 GLY   C CA  
9487  C C   . GLY   G  113 ? 0.54046 0.54046 0.54046 0.00000  0.00000  0.00000  113 GLY   C C   
9488  O O   . GLY   G  113 ? 0.52068 0.52068 0.52068 0.00000  0.00000  0.00000  113 GLY   C O   
9489  N N   . PRO   G  114 ? 0.46648 0.46648 0.46648 -0.00000 0.00000  0.00000  114 PRO   C N   
9490  C CA  . PRO   G  114 ? 0.38185 0.38185 0.38185 -0.00000 0.00000  0.00000  114 PRO   C CA  
9491  C C   . PRO   G  114 ? 0.41935 0.41935 0.41935 -0.00000 0.00000  0.00000  114 PRO   C C   
9492  O O   . PRO   G  114 ? 0.47594 0.47594 0.47594 0.00000  0.00000  0.00000  114 PRO   C O   
9493  C CB  . PRO   G  114 ? 0.44532 0.44532 0.44532 0.00000  0.00000  0.00000  114 PRO   C CB  
9494  C CG  . PRO   G  114 ? 0.40676 0.40676 0.40676 -0.00000 0.00000  0.00000  114 PRO   C CG  
9495  C CD  . PRO   G  114 ? 0.42051 0.42051 0.42051 -0.00000 0.00000  0.00000  114 PRO   C CD  
9496  N N   . PRO   G  115 ? 0.34362 0.34362 0.34362 -0.00000 0.00000  0.00000  115 PRO   C N   
9497  C CA  . PRO   G  115 ? 0.48274 0.48274 0.48274 0.00000  0.00000  0.00000  115 PRO   C CA  
9498  C C   . PRO   G  115 ? 0.38267 0.38267 0.38267 -0.00000 0.00000  0.00000  115 PRO   C C   
9499  O O   . PRO   G  115 ? 0.44718 0.44718 0.44718 -0.00000 0.00000  0.00000  115 PRO   C O   
9500  C CB  . PRO   G  115 ? 0.25189 0.25189 0.25189 -0.00000 0.00000  0.00000  115 PRO   C CB  
9501  C CG  . PRO   G  115 ? 0.28429 0.28429 0.28429 0.00000  -0.00000 0.00000  115 PRO   C CG  
9502  C CD  . PRO   G  115 ? 0.41054 0.41054 0.41054 0.00000  0.00000  0.00000  115 PRO   C CD  
9503  N N   . VAL   G  116 ? 0.57104 0.57104 0.57104 0.00000  -0.00000 0.00000  116 VAL   C N   
9504  C CA  . VAL   G  116 ? 0.44770 0.44770 0.44770 -0.00000 0.00000  0.00000  116 VAL   C CA  
9505  C C   . VAL   G  116 ? 0.47912 0.47912 0.47912 -0.00000 0.00000  0.00000  116 VAL   C C   
9506  O O   . VAL   G  116 ? 0.52438 0.52438 0.52438 0.00000  0.00000  0.00000  116 VAL   C O   
9507  C CB  . VAL   G  116 ? 0.53851 0.53851 0.53851 0.00000  0.00000  0.00000  116 VAL   C CB  
9508  C CG1 . VAL   G  116 ? 0.43813 0.43813 0.43813 0.00000  0.00000  0.00000  116 VAL   C CG1 
9509  C CG2 . VAL   G  116 ? 0.33630 0.33630 0.33630 0.00000  0.00000  0.00000  116 VAL   C CG2 
9510  N N   . TYR   G  117 ? 0.38917 0.38917 0.38917 -0.00000 0.00000  0.00000  117 TYR   C N   
9511  C CA  . TYR   G  117 ? 0.56057 0.56057 0.56057 0.00000  0.00000  0.00000  117 TYR   C CA  
9512  C C   . TYR   G  117 ? 0.48484 0.48484 0.48484 -0.00000 0.00000  0.00000  117 TYR   C C   
9513  O O   . TYR   G  117 ? 0.54831 0.54831 0.54831 0.00000  0.00000  0.00000  117 TYR   C O   
9514  C CB  . TYR   G  117 ? 0.37800 0.37800 0.37800 -0.00000 0.00000  0.00000  117 TYR   C CB  
9515  C CG  . TYR   G  117 ? 0.47008 0.47008 0.47008 -0.00000 0.00000  0.00000  117 TYR   C CG  
9516  C CD1 . TYR   G  117 ? 0.42232 0.42232 0.42232 0.00000  0.00000  0.00000  117 TYR   C CD1 
9517  C CD2 . TYR   G  117 ? 0.63395 0.63395 0.63395 0.00000  0.00000  0.00000  117 TYR   C CD2 
9518  C CE1 . TYR   G  117 ? 0.42779 0.42779 0.42779 -0.00000 0.00000  0.00000  117 TYR   C CE1 
9519  C CE2 . TYR   G  117 ? 0.34791 0.34791 0.34791 0.00000  0.00000  0.00000  117 TYR   C CE2 
9520  C CZ  . TYR   G  117 ? 0.55597 0.55597 0.55597 0.00000  0.00000  0.00000  117 TYR   C CZ  
9521  O OH  . TYR   G  117 ? 0.42607 0.42607 0.42607 -0.00000 0.00000  0.00000  117 TYR   C OH  
9522  N N   . MET   G  118 ? 0.52976 0.52976 0.52976 -0.00000 0.00000  0.00000  118 MET   C N   
9523  C CA  . MET   G  118 ? 0.40098 0.40098 0.40098 0.00000  0.00000  0.00000  118 MET   C CA  
9524  C C   . MET   G  118 ? 0.59882 0.59882 0.59882 0.00000  0.00000  0.00000  118 MET   C C   
9525  O O   . MET   G  118 ? 0.49962 0.49962 0.49962 0.00000  0.00000  0.00000  118 MET   C O   
9526  C CB  . MET   G  118 ? 0.43985 0.43985 0.43985 0.00000  0.00000  0.00000  118 MET   C CB  
9527  C CG  . MET   G  118 ? 0.30903 0.30903 0.30903 0.00000  0.00000  0.00000  118 MET   C CG  
9528  S SD  . MET   G  118 ? 0.53973 0.53973 0.53973 -0.00000 0.00000  0.00000  118 MET   C SD  
9529  C CE  . MET   G  118 ? 0.59764 0.59764 0.59764 0.00000  0.00000  0.00000  118 MET   C CE  
9530  N N   . ILE   G  119 ? 0.36391 0.36391 0.36391 -0.00000 0.00000  0.00000  119 ILE   C N   
9531  C CA  . ILE   G  119 ? 0.50929 0.50929 0.50929 0.00000  0.00000  0.00000  119 ILE   C CA  
9532  C C   . ILE   G  119 ? 0.51481 0.51481 0.51481 0.00000  0.00000  0.00000  119 ILE   C C   
9533  O O   . ILE   G  119 ? 0.57385 0.57385 0.57385 0.00000  0.00000  0.00000  119 ILE   C O   
9534  C CB  . ILE   G  119 ? 0.40762 0.40762 0.40762 0.00000  0.00000  -0.00000 119 ILE   C CB  
9535  C CG1 . ILE   G  119 ? 0.43662 0.43662 0.43662 0.00000  0.00000  0.00000  119 ILE   C CG1 
9536  C CG2 . ILE   G  119 ? 0.50273 0.50273 0.50273 0.00000  0.00000  0.00000  119 ILE   C CG2 
9537  C CD1 . ILE   G  119 ? 0.49840 0.49840 0.49840 0.00000  0.00000  0.00000  119 ILE   C CD1 
9538  N N   . MET   G  120 ? 0.41920 0.41920 0.41920 -0.00000 0.00000  0.00000  120 MET   C N   
9539  C CA  . MET   G  120 ? 0.39385 0.39385 0.39385 0.00000  0.00000  0.00000  120 MET   C CA  
9540  C C   . MET   G  120 ? 0.46770 0.46770 0.46770 -0.00000 0.00000  0.00000  120 MET   C C   
9541  O O   . MET   G  120 ? 0.46269 0.46269 0.46269 -0.00000 0.00000  0.00000  120 MET   C O   
9542  C CB  . MET   G  120 ? 0.23712 0.23712 0.23712 0.00000  0.00000  0.00000  120 MET   C CB  
9543  C CG  . MET   G  120 ? 0.33706 0.33706 0.33706 0.00000  0.00000  0.00000  120 MET   C CG  
9544  S SD  . MET   G  120 ? 0.54121 0.54121 0.54121 0.00000  0.00000  0.00000  120 MET   C SD  
9545  C CE  . MET   G  120 ? 0.34668 0.34668 0.34668 0.00000  0.00000  0.00000  120 MET   C CE  
9546  N N   . ALA   G  121 ? 0.40330 0.40330 0.40330 0.00000  -0.00000 0.00000  121 ALA   C N   
9547  C CA  . ALA   G  121 ? 0.47656 0.47656 0.47656 0.00000  0.00000  0.00000  121 ALA   C CA  
9548  C C   . ALA   G  121 ? 0.48132 0.48132 0.48132 -0.00000 0.00000  0.00000  121 ALA   C C   
9549  O O   . ALA   G  121 ? 0.56964 0.56964 0.56964 0.00000  0.00000  0.00000  121 ALA   C O   
9550  C CB  . ALA   G  121 ? 0.37418 0.37418 0.37418 0.00000  0.00000  0.00000  121 ALA   C CB  
9551  N N   . LYS   G  122 ? 0.52923 0.52923 0.52923 0.00000  0.00000  0.00000  122 LYS   C N   
9552  C CA  . LYS   G  122 ? 0.43470 0.43470 0.43470 0.00000  0.00000  0.00000  122 LYS   C CA  
9553  C C   . LYS   G  122 ? 0.61487 0.61487 0.61487 0.00000  0.00000  0.00000  122 LYS   C C   
9554  O O   . LYS   G  122 ? 0.53675 0.53675 0.53675 0.00000  0.00000  0.00000  122 LYS   C O   
9555  C CB  . LYS   G  122 ? 0.42729 0.42729 0.42729 -0.00000 0.00000  0.00000  122 LYS   C CB  
9556  C CG  . LYS   G  122 ? 1.53043 1.53043 1.53043 -0.00000 0.00000  0.00000  122 LYS   C CG  
9557  C CD  . LYS   G  122 ? 1.29569 1.29569 1.29569 0.00000  0.00000  0.00000  122 LYS   C CD  
9558  C CE  . LYS   G  122 ? 1.25565 1.25565 1.25565 0.00000  0.00000  0.00000  122 LYS   C CE  
9559  N NZ  . LYS   G  122 ? 0.93623 0.93623 0.93623 0.00000  0.00000  0.00000  122 LYS   C NZ  
9560  N N   . LEU   G  123 ? 0.52403 0.52403 0.52403 0.00000  0.00000  0.00000  123 LEU   C N   
9561  C CA  . LEU   G  123 ? 0.51770 0.51770 0.51770 0.00000  0.00000  0.00000  123 LEU   C CA  
9562  C C   . LEU   G  123 ? 0.83420 0.83420 0.83420 0.00000  0.00000  0.00000  123 LEU   C C   
9563  O O   . LEU   G  123 ? 0.41725 0.41725 0.41725 -0.00000 0.00000  0.00000  123 LEU   C O   
9564  C CB  . LEU   G  123 ? 0.40482 0.40482 0.40482 0.00000  0.00000  0.00000  123 LEU   C CB  
9565  C CG  . LEU   G  123 ? 0.51807 0.51807 0.51807 -0.00000 0.00000  0.00000  123 LEU   C CG  
9566  C CD1 . LEU   G  123 ? 0.44404 0.44404 0.44404 0.00000  0.00000  0.00000  123 LEU   C CD1 
9567  C CD2 . LEU   G  123 ? 0.44188 0.44188 0.44188 0.00000  0.00000  0.00000  123 LEU   C CD2 
9568  N N   . MET   G  124 ? 0.42919 0.42919 0.42919 0.00000  0.00000  0.00000  124 MET   C N   
9569  C CA  . MET   G  124 ? 0.57347 0.57347 0.57347 0.00000  0.00000  0.00000  124 MET   C CA  
9570  C C   . MET   G  124 ? 0.47932 0.47932 0.47932 -0.00000 -0.00000 0.00000  124 MET   C C   
9571  O O   . MET   G  124 ? 0.46855 0.46855 0.46855 0.00000  0.00000  0.00000  124 MET   C O   
9572  C CB  . MET   G  124 ? 0.28955 0.28955 0.28955 0.00000  0.00000  0.00000  124 MET   C CB  
9573  C CG  . MET   G  124 ? 0.54596 0.54596 0.54596 -0.00000 0.00000  0.00000  124 MET   C CG  
9574  S SD  . MET   G  124 ? 0.56984 0.56984 0.56984 0.00000  0.00000  0.00000  124 MET   C SD  
9575  C CE  . MET   G  124 ? 0.26173 0.26173 0.26173 0.00000  0.00000  0.00000  124 MET   C CE  
9576  N N   . ASN   G  125 ? 0.57034 0.57034 0.57034 0.00000  0.00000  0.00000  125 ASN   C N   
9577  C CA  . ASN   G  125 ? 0.49285 0.49285 0.49285 -0.00000 0.00000  0.00000  125 ASN   C CA  
9578  C C   . ASN   G  125 ? 0.56408 0.56408 0.56408 -0.00000 0.00000  0.00000  125 ASN   C C   
9579  O O   . ASN   G  125 ? 0.61459 0.61459 0.61459 -0.00000 0.00000  0.00000  125 ASN   C O   
9580  C CB  . ASN   G  125 ? 0.47368 0.47368 0.47368 0.00000  0.00000  0.00000  125 ASN   C CB  
9581  C CG  . ASN   G  125 ? 0.45001 0.45001 0.45001 0.00000  0.00000  0.00000  125 ASN   C CG  
9582  O OD1 . ASN   G  125 ? 0.52807 0.52807 0.52807 0.00000  0.00000  0.00000  125 ASN   C OD1 
9583  N ND2 . ASN   G  125 ? 0.66928 0.66928 0.66928 0.00000  0.00000  0.00000  125 ASN   C ND2 
9584  N N   . THR   G  126 ? 0.55932 0.55932 0.55932 0.00000  0.00000  0.00000  126 THR   C N   
9585  C CA  . THR   G  126 ? 0.67444 0.67444 0.67444 -0.00000 0.00000  0.00000  126 THR   C CA  
9586  C C   . THR   G  126 ? 0.40683 0.40683 0.40683 0.00000  0.00000  0.00000  126 THR   C C   
9587  O O   . THR   G  126 ? 0.64649 0.64649 0.64649 0.00000  0.00000  0.00000  126 THR   C O   
9588  C CB  . THR   G  126 ? 0.48130 0.48130 0.48130 0.00000  0.00000  0.00000  126 THR   C CB  
9589  O OG1 . THR   G  126 ? 0.47398 0.47398 0.47398 0.00000  0.00000  0.00000  126 THR   C OG1 
9590  C CG2 . THR   G  126 ? 0.29158 0.29158 0.29158 -0.00000 0.00000  0.00000  126 THR   C CG2 
9591  N N   . ARG   G  127 ? 0.82866 0.82866 0.82866 -0.00000 0.00000  0.00000  127 ARG   C N   
9592  C CA  . ARG   G  127 ? 0.34630 0.34630 0.34630 0.00000  0.00000  0.00000  127 ARG   C CA  
9593  C C   . ARG   G  127 ? 1.08639 1.08639 1.08639 0.00000  0.00000  0.00000  127 ARG   C C   
9594  O O   . ARG   G  127 ? 0.58758 0.58758 0.58758 0.00000  0.00000  0.00000  127 ARG   C O   
9595  C CB  . ARG   G  127 ? 0.17392 0.17392 0.17392 -0.00000 0.00000  0.00000  127 ARG   C CB  
9596  C CG  . ARG   G  127 ? 0.85341 0.85341 0.85341 -0.00000 0.00000  0.00000  127 ARG   C CG  
9597  C CD  . ARG   G  127 ? 1.75204 1.75204 1.75204 -0.00000 0.00000  0.00000  127 ARG   C CD  
9598  N NE  . ARG   G  127 ? 1.73397 1.73397 1.73397 0.00000  0.00000  0.00000  127 ARG   C NE  
9599  C CZ  . ARG   G  127 ? 1.59627 1.59627 1.59627 0.00000  0.00000  0.00000  127 ARG   C CZ  
9600  N NH1 . ARG   G  127 ? 0.37709 0.37709 0.37709 0.00000  -0.00000 0.00000  127 ARG   C NH1 
9601  N NH2 . ARG   G  127 ? 0.89438 0.89438 0.89438 0.00000  0.00000  0.00000  127 ARG   C NH2 
9602  N N   . ALA   G  128 ? 0.41557 0.41557 0.41557 -0.00000 0.00000  0.00000  128 ALA   C N   
9603  C CA  . ALA   G  128 ? 0.57986 0.57986 0.57986 0.00000  0.00000  -0.00000 128 ALA   C CA  
9604  C C   . ALA   G  128 ? 0.46500 0.46500 0.46500 0.00000  0.00000  0.00000  128 ALA   C C   
9605  O O   . ALA   G  128 ? 0.60229 0.60229 0.60229 -0.00000 0.00000  0.00000  128 ALA   C O   
9606  C CB  . ALA   G  128 ? 0.43760 0.43760 0.43760 0.00000  0.00000  0.00000  128 ALA   C CB  
9607  N N   . GLY   G  129 ? 0.64560 0.64560 0.64560 -0.00000 0.00000  0.00000  129 GLY   C N   
9608  C CA  . GLY   G  129 ? 0.24044 0.24044 0.24044 -0.00000 0.00000  0.00000  129 GLY   C CA  
9609  C C   . GLY   G  129 ? 0.55069 0.55069 0.55069 -0.00000 0.00000  0.00000  129 GLY   C C   
9610  O O   . GLY   G  129 ? 0.42208 0.42208 0.42208 0.00000  0.00000  0.00000  129 GLY   C O   
9611  N N   . PHE   G  130 ? 0.38085 0.38085 0.38085 -0.00000 0.00000  0.00000  130 PHE   C N   
9612  C CA  . PHE   G  130 ? 0.38194 0.38194 0.38194 -0.00000 0.00000  0.00000  130 PHE   C CA  
9613  C C   . PHE   G  130 ? 0.64705 0.64705 0.64705 0.00000  0.00000  0.00000  130 PHE   C C   
9614  O O   . PHE   G  130 ? 0.53502 0.53502 0.53502 -0.00000 0.00000  0.00000  130 PHE   C O   
9615  C CB  . PHE   G  130 ? 0.23746 0.23746 0.23746 -0.00000 0.00000  0.00000  130 PHE   C CB  
9616  C CG  . PHE   G  130 ? 0.40774 0.40774 0.40774 0.00000  0.00000  0.00000  130 PHE   C CG  
9617  C CD1 . PHE   G  130 ? 0.40769 0.40769 0.40769 -0.00000 0.00000  0.00000  130 PHE   C CD1 
9618  C CD2 . PHE   G  130 ? 0.32665 0.32665 0.32665 0.00000  0.00000  0.00000  130 PHE   C CD2 
9619  C CE1 . PHE   G  130 ? 0.39291 0.39291 0.39291 0.00000  0.00000  0.00000  130 PHE   C CE1 
9620  C CE2 . PHE   G  130 ? 0.50174 0.50174 0.50174 0.00000  0.00000  0.00000  130 PHE   C CE2 
9621  C CZ  . PHE   G  130 ? 0.33011 0.33011 0.33011 0.00000  0.00000  0.00000  130 PHE   C CZ  
9622  N N   . SER   G  131 ? 0.36447 0.36447 0.36447 -0.00000 0.00000  0.00000  131 SER   C N   
9623  C CA  . SER   G  131 ? 0.58830 0.58830 0.58830 -0.00000 -0.00000 0.00000  131 SER   C CA  
9624  C C   . SER   G  131 ? 0.43200 0.43200 0.43200 0.00000  0.00000  0.00000  131 SER   C C   
9625  O O   . SER   G  131 ? 0.56938 0.56938 0.56938 -0.00000 0.00000  0.00000  131 SER   C O   
9626  C CB  . SER   G  131 ? 0.22386 0.22386 0.22386 -0.00000 0.00000  0.00000  131 SER   C CB  
9627  O OG  . SER   G  131 ? 1.13407 1.13407 1.13407 -0.00000 0.00000  0.00000  131 SER   C OG  
9628  N N   . ALA   G  132 ? 0.38304 0.38304 0.38304 0.00000  0.00000  0.00000  132 ALA   C N   
9629  C CA  . ALA   G  132 ? 0.31037 0.31037 0.31037 0.00000  0.00000  0.00000  132 ALA   C CA  
9630  C C   . ALA   G  132 ? 0.49135 0.49135 0.49135 0.00000  0.00000  0.00000  132 ALA   C C   
9631  O O   . ALA   G  132 ? 0.41238 0.41238 0.41238 -0.00000 0.00000  0.00000  132 ALA   C O   
9632  C CB  . ALA   G  132 ? 0.31951 0.31951 0.31951 0.00000  -0.00000 0.00000  132 ALA   C CB  
9633  N N   . PHE   G  133 ? 0.31679 0.31679 0.31679 0.00000  0.00000  0.00000  133 PHE   C N   
9634  C CA  . PHE   G  133 ? 0.45072 0.45072 0.45072 -0.00000 0.00000  0.00000  133 PHE   C CA  
9635  C C   . PHE   G  133 ? 0.53873 0.53873 0.53873 -0.00000 0.00000  0.00000  133 PHE   C C   
9636  O O   . PHE   G  133 ? 0.40590 0.40590 0.40590 -0.00000 0.00000  0.00000  133 PHE   C O   
9637  C CB  . PHE   G  133 ? 0.35217 0.35217 0.35217 0.00000  0.00000  0.00000  133 PHE   C CB  
9638  C CG  . PHE   G  133 ? 0.49085 0.49085 0.49085 0.00000  0.00000  0.00000  133 PHE   C CG  
9639  C CD1 . PHE   G  133 ? 0.43452 0.43452 0.43452 -0.00000 0.00000  0.00000  133 PHE   C CD1 
9640  C CD2 . PHE   G  133 ? 0.36755 0.36755 0.36755 0.00000  0.00000  0.00000  133 PHE   C CD2 
9641  C CE1 . PHE   G  133 ? 0.33148 0.33148 0.33148 0.00000  0.00000  0.00000  133 PHE   C CE1 
9642  C CE2 . PHE   G  133 ? 0.36025 0.36025 0.36025 0.00000  0.00000  0.00000  133 PHE   C CE2 
9643  C CZ  . PHE   G  133 ? 0.28163 0.28163 0.28163 0.00000  0.00000  0.00000  133 PHE   C CZ  
9644  N N   . THR   G  134 ? 0.36188 0.36188 0.36188 0.00000  -0.00000 0.00000  134 THR   C N   
9645  C CA  . THR   G  134 ? 0.42088 0.42088 0.42088 0.00000  0.00000  0.00000  134 THR   C CA  
9646  C C   . THR   G  134 ? 0.39335 0.39335 0.39335 0.00000  -0.00000 0.00000  134 THR   C C   
9647  O O   . THR   G  134 ? 0.49406 0.49406 0.49406 0.00000  0.00000  0.00000  134 THR   C O   
9648  C CB  . THR   G  134 ? 0.42109 0.42109 0.42109 -0.00000 0.00000  0.00000  134 THR   C CB  
9649  O OG1 . THR   G  134 ? 0.49313 0.49313 0.49313 0.00000  0.00000  0.00000  134 THR   C OG1 
9650  C CG2 . THR   G  134 ? 0.33237 0.33237 0.33237 0.00000  0.00000  0.00000  134 THR   C CG2 
9651  N N   . ARG   G  135 ? 0.39149 0.39149 0.39149 -0.00000 0.00000  0.00000  135 ARG   C N   
9652  C CA  . ARG   G  135 ? 0.39374 0.39374 0.39374 0.00000  0.00000  0.00000  135 ARG   C CA  
9653  C C   . ARG   G  135 ? 0.56631 0.56631 0.56631 -0.00000 0.00000  0.00000  135 ARG   C C   
9654  O O   . ARG   G  135 ? 0.39671 0.39671 0.39671 -0.00000 0.00000  0.00000  135 ARG   C O   
9655  C CB  . ARG   G  135 ? 0.27745 0.27745 0.27745 0.00000  0.00000  0.00000  135 ARG   C CB  
9656  C CG  . ARG   G  135 ? 0.33072 0.33072 0.33072 -0.00000 0.00000  0.00000  135 ARG   C CG  
9657  C CD  . ARG   G  135 ? 0.36537 0.36537 0.36537 -0.00000 0.00000  0.00000  135 ARG   C CD  
9658  N NE  . ARG   G  135 ? 0.60974 0.60974 0.60974 0.00000  0.00000  0.00000  135 ARG   C NE  
9659  C CZ  . ARG   G  135 ? 0.65807 0.65807 0.65807 -0.00000 -0.00000 0.00000  135 ARG   C CZ  
9660  N NH1 . ARG   G  135 ? 0.54629 0.54629 0.54629 -0.00000 0.00000  0.00000  135 ARG   C NH1 
9661  N NH2 . ARG   G  135 ? 0.52008 0.52008 0.52008 -0.00000 0.00000  0.00000  135 ARG   C NH2 
9662  N N   . GLN   G  136 ? 0.34071 0.34071 0.34071 -0.00000 0.00000  0.00000  136 GLN   C N   
9663  C CA  . GLN   G  136 ? 0.36627 0.36627 0.36627 0.00000  0.00000  0.00000  136 GLN   C CA  
9664  C C   . GLN   G  136 ? 0.33289 0.33289 0.33289 0.00000  0.00000  0.00000  136 GLN   C C   
9665  O O   . GLN   G  136 ? 0.55446 0.55446 0.55446 0.00000  0.00000  0.00000  136 GLN   C O   
9666  C CB  . GLN   G  136 ? 0.34161 0.34161 0.34161 0.00000  0.00000  0.00000  136 GLN   C CB  
9667  C CG  . GLN   G  136 ? 0.28123 0.28123 0.28123 -0.00000 0.00000  0.00000  136 GLN   C CG  
9668  C CD  . GLN   G  136 ? 0.60113 0.60113 0.60113 0.00000  0.00000  0.00000  136 GLN   C CD  
9669  O OE1 . GLN   G  136 ? 0.44813 0.44813 0.44813 0.00000  0.00000  0.00000  136 GLN   C OE1 
9670  N NE2 . GLN   G  136 ? 0.28759 0.28759 0.28759 -0.00000 0.00000  0.00000  136 GLN   C NE2 
9671  N N   . ARG   G  137 ? 0.28613 0.28613 0.28613 -0.00000 0.00000  0.00000  137 ARG   C N   
9672  C CA  . ARG   G  137 ? 0.39953 0.39953 0.39953 0.00000  0.00000  0.00000  137 ARG   C CA  
9673  C C   . ARG   G  137 ? 0.25037 0.25037 0.25037 0.00000  0.00000  0.00000  137 ARG   C C   
9674  O O   . ARG   G  137 ? 0.48459 0.48459 0.48459 -0.00000 0.00000  0.00000  137 ARG   C O   
9675  C CB  . ARG   G  137 ? 0.41471 0.41471 0.41471 0.00000  0.00000  0.00000  137 ARG   C CB  
9676  C CG  . ARG   G  137 ? 0.30714 0.30714 0.30714 -0.00000 0.00000  0.00000  137 ARG   C CG  
9677  C CD  . ARG   G  137 ? 0.35584 0.35584 0.35584 0.00000  0.00000  0.00000  137 ARG   C CD  
9678  N NE  . ARG   G  137 ? 0.32710 0.32710 0.32710 0.00000  0.00000  0.00000  137 ARG   C NE  
9679  C CZ  . ARG   G  137 ? 0.48450 0.48450 0.48450 0.00000  0.00000  0.00000  137 ARG   C CZ  
9680  N NH1 . ARG   G  137 ? 0.30651 0.30651 0.30651 0.00000  0.00000  0.00000  137 ARG   C NH1 
9681  N NH2 . ARG   G  137 ? 0.31810 0.31810 0.31810 0.00000  0.00000  0.00000  137 ARG   C NH2 
9682  N N   . LEU   G  138 ? 0.24634 0.24634 0.24634 0.00000  0.00000  0.00000  138 LEU   C N   
9683  C CA  . LEU   G  138 ? 0.41171 0.41171 0.41171 -0.00000 0.00000  0.00000  138 LEU   C CA  
9684  C C   . LEU   G  138 ? 0.53126 0.53126 0.53126 0.00000  0.00000  0.00000  138 LEU   C C   
9685  O O   . LEU   G  138 ? 0.39890 0.39890 0.39890 -0.00000 0.00000  0.00000  138 LEU   C O   
9686  C CB  . LEU   G  138 ? 0.33298 0.33298 0.33298 0.00000  0.00000  0.00000  138 LEU   C CB  
9687  C CG  . LEU   G  138 ? 0.50877 0.50877 0.50877 0.00000  0.00000  0.00000  138 LEU   C CG  
9688  C CD1 . LEU   G  138 ? 0.33752 0.33752 0.33752 0.00000  0.00000  0.00000  138 LEU   C CD1 
9689  C CD2 . LEU   G  138 ? 0.30374 0.30374 0.30374 0.00000  0.00000  -0.00000 138 LEU   C CD2 
9690  N N   . ASN   G  139 ? 0.33168 0.33168 0.33168 -0.00000 0.00000  0.00000  139 ASN   C N   
9691  C CA  . ASN   G  139 ? 0.53688 0.53688 0.53688 0.00000  0.00000  0.00000  139 ASN   C CA  
9692  C C   . ASN   G  139 ? 0.36726 0.36726 0.36726 -0.00000 0.00000  0.00000  139 ASN   C C   
9693  O O   . ASN   G  139 ? 0.54334 0.54334 0.54334 0.00000  0.00000  0.00000  139 ASN   C O   
9694  C CB  . ASN   G  139 ? 0.23673 0.23673 0.23673 -0.00000 0.00000  0.00000  139 ASN   C CB  
9695  C CG  . ASN   G  139 ? 0.44979 0.44979 0.44979 0.00000  0.00000  0.00000  139 ASN   C CG  
9696  O OD1 . ASN   G  139 ? 0.34314 0.34314 0.34314 0.00000  0.00000  -0.00000 139 ASN   C OD1 
9697  N ND2 . ASN   G  139 ? 0.30287 0.30287 0.30287 0.00000  0.00000  0.00000  139 ASN   C ND2 
9698  N N   . LEU   G  140 ? 0.48421 0.48421 0.48421 -0.00000 0.00000  0.00000  140 LEU   C N   
9699  C CA  . LEU   G  140 ? 0.33414 0.33414 0.33414 0.00000  0.00000  0.00000  140 LEU   C CA  
9700  C C   . LEU   G  140 ? 0.61633 0.61633 0.61633 0.00000  0.00000  0.00000  140 LEU   C C   
9701  O O   . LEU   G  140 ? 0.34941 0.34941 0.34941 0.00000  0.00000  0.00000  140 LEU   C O   
9702  C CB  . LEU   G  140 ? 0.32830 0.32830 0.32830 0.00000  0.00000  0.00000  140 LEU   C CB  
9703  C CG  . LEU   G  140 ? 0.53400 0.53400 0.53400 0.00000  -0.00000 0.00000  140 LEU   C CG  
9704  C CD1 . LEU   G  140 ? 0.25496 0.25496 0.25496 0.00000  0.00000  0.00000  140 LEU   C CD1 
9705  C CD2 . LEU   G  140 ? 0.17714 0.17714 0.17714 0.00000  0.00000  0.00000  140 LEU   C CD2 
9706  N N   . HIS   G  141 ? 0.37951 0.37951 0.37951 -0.00000 0.00000  0.00000  141 HIS   C N   
9707  C CA  . HIS   G  141 ? 0.35290 0.35290 0.35290 -0.00000 0.00000  0.00000  141 HIS   C CA  
9708  C C   . HIS   G  141 ? 0.36780 0.36780 0.36780 0.00000  0.00000  0.00000  141 HIS   C C   
9709  O O   . HIS   G  141 ? 0.45250 0.45250 0.45250 0.00000  0.00000  0.00000  141 HIS   C O   
9710  C CB  . HIS   G  141 ? 0.22594 0.22594 0.22594 0.00000  0.00000  0.00000  141 HIS   C CB  
9711  C CG  . HIS   G  141 ? 0.57487 0.57487 0.57487 -0.00000 0.00000  0.00000  141 HIS   C CG  
9712  N ND1 . HIS   G  141 ? 0.54749 0.54749 0.54749 -0.00000 -0.00000 0.00000  141 HIS   C ND1 
9713  C CD2 . HIS   G  141 ? 0.48823 0.48823 0.48823 0.00000  0.00000  0.00000  141 HIS   C CD2 
9714  C CE1 . HIS   G  141 ? 0.38945 0.38945 0.38945 0.00000  0.00000  0.00000  141 HIS   C CE1 
9715  N NE2 . HIS   G  141 ? 0.55724 0.55724 0.55724 0.00000  0.00000  0.00000  141 HIS   C NE2 
9716  N N   . PHE   G  142 ? 0.34774 0.34774 0.34774 0.00000  0.00000  0.00000  142 PHE   C N   
9717  C CA  . PHE   G  142 ? 0.51537 0.51537 0.51537 -0.00000 0.00000  0.00000  142 PHE   C CA  
9718  C C   . PHE   G  142 ? 0.34939 0.34939 0.34939 0.00000  0.00000  0.00000  142 PHE   C C   
9719  O O   . PHE   G  142 ? 0.37420 0.37420 0.37420 0.00000  0.00000  0.00000  142 PHE   C O   
9720  C CB  . PHE   G  142 ? 0.33762 0.33762 0.33762 0.00000  0.00000  0.00000  142 PHE   C CB  
9721  C CG  . PHE   G  142 ? 0.42861 0.42861 0.42861 0.00000  -0.00000 0.00000  142 PHE   C CG  
9722  C CD1 . PHE   G  142 ? 0.36316 0.36316 0.36316 -0.00000 0.00000  0.00000  142 PHE   C CD1 
9723  C CD2 . PHE   G  142 ? 0.38204 0.38204 0.38204 0.00000  0.00000  0.00000  142 PHE   C CD2 
9724  C CE1 . PHE   G  142 ? 0.35149 0.35149 0.35149 -0.00000 0.00000  0.00000  142 PHE   C CE1 
9725  C CE2 . PHE   G  142 ? 0.39604 0.39604 0.39604 -0.00000 0.00000  0.00000  142 PHE   C CE2 
9726  C CZ  . PHE   G  142 ? 0.33546 0.33546 0.33546 -0.00000 0.00000  0.00000  142 PHE   C CZ  
9727  N N   . LYS   G  143 ? 0.42444 0.42444 0.42444 0.00000  0.00000  0.00000  143 LYS   C N   
9728  C CA  . LYS   G  143 ? 0.36957 0.36957 0.36957 0.00000  0.00000  0.00000  143 LYS   C CA  
9729  C C   . LYS   G  143 ? 0.41105 0.41105 0.41105 0.00000  0.00000  0.00000  143 LYS   C C   
9730  O O   . LYS   G  143 ? 0.45363 0.45363 0.45363 -0.00000 0.00000  0.00000  143 LYS   C O   
9731  C CB  . LYS   G  143 ? 0.41457 0.41457 0.41457 -0.00000 0.00000  0.00000  143 LYS   C CB  
9732  C CG  . LYS   G  143 ? 0.24441 0.24441 0.24441 0.00000  0.00000  0.00000  143 LYS   C CG  
9733  C CD  . LYS   G  143 ? 0.34778 0.34778 0.34778 0.00000  0.00000  0.00000  143 LYS   C CD  
9734  C CE  . LYS   G  143 ? 0.43084 0.43084 0.43084 0.00000  0.00000  0.00000  143 LYS   C CE  
9735  N NZ  . LYS   G  143 ? 0.48921 0.48921 0.48921 -0.00000 0.00000  0.00000  143 LYS   C NZ  
9736  N N   . LYS   G  144 ? 0.25543 0.25543 0.25543 0.00000  0.00000  0.00000  144 LYS   C N   
9737  C CA  . LYS   G  144 ? 0.39011 0.39011 0.39011 -0.00000 0.00000  0.00000  144 LYS   C CA  
9738  C C   . LYS   G  144 ? 0.22172 0.22172 0.22172 -0.00000 0.00000  0.00000  144 LYS   C C   
9739  O O   . LYS   G  144 ? 0.41685 0.41685 0.41685 0.00000  0.00000  0.00000  144 LYS   C O   
9740  C CB  . LYS   G  144 ? 0.14292 0.14292 0.14292 0.00000  -0.00000 -0.00000 144 LYS   C CB  
9741  C CG  . LYS   G  144 ? 0.75479 0.75479 0.75479 0.00000  0.00000  0.00000  144 LYS   C CG  
9742  C CD  . LYS   G  144 ? 1.30587 1.30587 1.30587 0.00000  0.00000  0.00000  144 LYS   C CD  
9743  C CE  . LYS   G  144 ? 1.61745 1.61745 1.61745 -0.00000 0.00000  0.00000  144 LYS   C CE  
9744  N NZ  . LYS   G  144 ? 0.59489 0.59489 0.59489 0.00000  0.00000  0.00000  144 LYS   C NZ  
9745  N N   . LEU   G  145 ? 0.32125 0.32125 0.32125 0.00000  0.00000  0.00000  145 LEU   C N   
9746  C CA  . LEU   G  145 ? 0.25068 0.25068 0.25068 0.00000  0.00000  0.00000  145 LEU   C CA  
9747  C C   . LEU   G  145 ? 0.50602 0.50602 0.50602 0.00000  0.00000  0.00000  145 LEU   C C   
9748  O O   . LEU   G  145 ? 0.48356 0.48356 0.48356 -0.00000 0.00000  0.00000  145 LEU   C O   
9749  C CB  . LEU   G  145 ? 0.38792 0.38792 0.38792 0.00000  0.00000  0.00000  145 LEU   C CB  
9750  C CG  . LEU   G  145 ? 0.42150 0.42150 0.42150 0.00000  0.00000  0.00000  145 LEU   C CG  
9751  C CD1 . LEU   G  145 ? 0.34172 0.34172 0.34172 0.00000  0.00000  0.00000  145 LEU   C CD1 
9752  C CD2 . LEU   G  145 ? 0.33387 0.33387 0.33387 0.00000  0.00000  0.00000  145 LEU   C CD2 
9753  N N   . PHE   G  146 ? 0.34569 0.34569 0.34569 0.00000  0.00000  0.00000  146 PHE   C N   
9754  C CA  . PHE   G  146 ? 0.39577 0.39577 0.39577 -0.00000 0.00000  0.00000  146 PHE   C CA  
9755  C C   . PHE   G  146 ? 0.50012 0.50012 0.50012 0.00000  0.00000  0.00000  146 PHE   C C   
9756  O O   . PHE   G  146 ? 0.50911 0.50911 0.50911 -0.00000 -0.00000 0.00000  146 PHE   C O   
9757  C CB  . PHE   G  146 ? 0.39867 0.39867 0.39867 0.00000  0.00000  0.00000  146 PHE   C CB  
9758  C CG  . PHE   G  146 ? 0.44393 0.44393 0.44393 0.00000  0.00000  0.00000  146 PHE   C CG  
9759  C CD1 . PHE   G  146 ? 0.44448 0.44448 0.44448 -0.00000 0.00000  0.00000  146 PHE   C CD1 
9760  C CD2 . PHE   G  146 ? 0.35665 0.35665 0.35665 -0.00000 0.00000  0.00000  146 PHE   C CD2 
9761  C CE1 . PHE   G  146 ? 0.44594 0.44594 0.44594 0.00000  0.00000  0.00000  146 PHE   C CE1 
9762  C CE2 . PHE   G  146 ? 0.40203 0.40203 0.40203 -0.00000 0.00000  0.00000  146 PHE   C CE2 
9763  C CZ  . PHE   G  146 ? 0.47369 0.47369 0.47369 -0.00000 -0.00000 0.00000  146 PHE   C CZ  
9764  N N   . ASP   G  147 ? 0.40628 0.40628 0.40628 0.00000  0.00000  -0.00000 147 ASP   C N   
9765  C CA  . ASP   G  147 ? 0.32558 0.32558 0.32558 -0.00000 0.00000  0.00000  147 ASP   C CA  
9766  C C   . ASP   G  147 ? 0.44672 0.44672 0.44672 0.00000  0.00000  0.00000  147 ASP   C C   
9767  O O   . ASP   G  147 ? 0.42536 0.42536 0.42536 0.00000  0.00000  0.00000  147 ASP   C O   
9768  C CB  . ASP   G  147 ? 0.22991 0.22991 0.22991 -0.00000 -0.00000 0.00000  147 ASP   C CB  
9769  C CG  . ASP   G  147 ? 0.64885 0.64885 0.64885 0.00000  0.00000  0.00000  147 ASP   C CG  
9770  O OD1 . ASP   G  147 ? 0.54900 0.54900 0.54900 0.00000  0.00000  -0.00000 147 ASP   C OD1 
9771  O OD2 . ASP   G  147 ? 0.60195 0.60195 0.60195 0.00000  0.00000  0.00000  147 ASP   C OD2 
9772  N N   . THR   G  148 ? 0.36490 0.36490 0.36490 0.00000  0.00000  -0.00000 148 THR   C N   
9773  C CA  . THR   G  148 ? 0.48457 0.48457 0.48457 0.00000  -0.00000 -0.00000 148 THR   C CA  
9774  C C   . THR   G  148 ? 0.44539 0.44539 0.44539 -0.00000 0.00000  0.00000  148 THR   C C   
9775  O O   . THR   G  148 ? 0.52157 0.52157 0.52157 -0.00000 0.00000  0.00000  148 THR   C O   
9776  C CB  . THR   G  148 ? 0.41949 0.41949 0.41949 0.00000  0.00000  0.00000  148 THR   C CB  
9777  O OG1 . THR   G  148 ? 0.43048 0.43048 0.43048 0.00000  0.00000  0.00000  148 THR   C OG1 
9778  C CG2 . THR   G  148 ? 0.28402 0.28402 0.28402 0.00000  0.00000  0.00000  148 THR   C CG2 
9779  N N   . TRP   G  149 ? 0.46291 0.46291 0.46291 -0.00000 0.00000  0.00000  149 TRP   C N   
9780  C CA  . TRP   G  149 ? 0.37559 0.37559 0.37559 0.00000  0.00000  0.00000  149 TRP   C CA  
9781  C C   . TRP   G  149 ? 0.67989 0.67989 0.67989 0.00000  0.00000  0.00000  149 TRP   C C   
9782  O O   . TRP   G  149 ? 0.48762 0.48762 0.48762 0.00000  0.00000  0.00000  149 TRP   C O   
9783  C CB  . TRP   G  149 ? 0.34483 0.34483 0.34483 0.00000  0.00000  0.00000  149 TRP   C CB  
9784  C CG  . TRP   G  149 ? 0.48446 0.48446 0.48446 -0.00000 0.00000  0.00000  149 TRP   C CG  
9785  C CD1 . TRP   G  149 ? 0.41254 0.41254 0.41254 -0.00000 0.00000  0.00000  149 TRP   C CD1 
9786  C CD2 . TRP   G  149 ? 0.61540 0.61540 0.61540 0.00000  0.00000  0.00000  149 TRP   C CD2 
9787  N NE1 . TRP   G  149 ? 0.56721 0.56721 0.56721 -0.00000 0.00000  0.00000  149 TRP   C NE1 
9788  C CE2 . TRP   G  149 ? 0.39342 0.39342 0.39342 0.00000  0.00000  0.00000  149 TRP   C CE2 
9789  C CE3 . TRP   G  149 ? 0.38225 0.38225 0.38225 -0.00000 0.00000  0.00000  149 TRP   C CE3 
9790  C CZ2 . TRP   G  149 ? 0.51305 0.51305 0.51305 -0.00000 0.00000  0.00000  149 TRP   C CZ2 
9791  C CZ3 . TRP   G  149 ? 0.41850 0.41850 0.41850 0.00000  0.00000  0.00000  149 TRP   C CZ3 
9792  C CH2 . TRP   G  149 ? 0.50991 0.50991 0.50991 0.00000  0.00000  0.00000  149 TRP   C CH2 
9793  N N   . GLY   G  150 ? 0.43223 0.43223 0.43223 -0.00000 0.00000  0.00000  150 GLY   C N   
9794  C CA  . GLY   G  150 ? 0.29744 0.29744 0.29744 0.00000  0.00000  0.00000  150 GLY   C CA  
9795  C C   . GLY   G  150 ? 0.56711 0.56711 0.56711 -0.00000 0.00000  0.00000  150 GLY   C C   
9796  O O   . GLY   G  150 ? 0.71977 0.71977 0.71977 0.00000  0.00000  0.00000  150 GLY   C O   
9797  N N   . LEU   G  151 ? 0.51329 0.51329 0.51329 0.00000  0.00000  0.00000  151 LEU   C N   
9798  C CA  . LEU   G  151 ? 0.44640 0.44640 0.44640 0.00000  0.00000  0.00000  151 LEU   C CA  
9799  C C   . LEU   G  151 ? 0.94592 0.94592 0.94592 -0.00000 0.00000  0.00000  151 LEU   C C   
9800  O O   . LEU   G  151 ? 0.60469 0.60469 0.60469 -0.00000 0.00000  0.00000  151 LEU   C O   
9801  C CB  . LEU   G  151 ? 0.60086 0.60086 0.60086 -0.00000 0.00000  0.00000  151 LEU   C CB  
9802  C CG  . LEU   G  151 ? 0.86805 0.86805 0.86805 0.00000  0.00000  0.00000  151 LEU   C CG  
9803  C CD1 . LEU   G  151 ? 0.42696 0.42696 0.42696 0.00000  0.00000  0.00000  151 LEU   C CD1 
9804  C CD2 . LEU   G  151 ? 0.28161 0.28161 0.28161 0.00000  0.00000  0.00000  151 LEU   C CD2 
9805  N N   . PHE   G  152 ? 0.33133 0.33133 0.33133 0.00000  0.00000  0.00000  152 PHE   C N   
9806  C CA  . PHE   G  152 ? 0.49282 0.49282 0.49282 -0.00000 0.00000  0.00000  152 PHE   C CA  
9807  C C   . PHE   G  152 ? 0.66042 0.66042 0.66042 0.00000  0.00000  0.00000  152 PHE   C C   
9808  O O   . PHE   G  152 ? 0.56486 0.56486 0.56486 0.00000  0.00000  0.00000  152 PHE   C O   
9809  C CB  . PHE   G  152 ? 0.26818 0.26818 0.26818 0.00000  0.00000  0.00000  152 PHE   C CB  
9810  C CG  . PHE   G  152 ? 0.60074 0.60074 0.60074 -0.00000 0.00000  0.00000  152 PHE   C CG  
9811  C CD1 . PHE   G  152 ? 0.38481 0.38481 0.38481 0.00000  0.00000  0.00000  152 PHE   C CD1 
9812  C CD2 . PHE   G  152 ? 0.48445 0.48445 0.48445 -0.00000 0.00000  0.00000  152 PHE   C CD2 
9813  C CE1 . PHE   G  152 ? 0.47339 0.47339 0.47339 0.00000  0.00000  0.00000  152 PHE   C CE1 
9814  C CE2 . PHE   G  152 ? 0.60576 0.60576 0.60576 0.00000  0.00000  0.00000  152 PHE   C CE2 
9815  C CZ  . PHE   G  152 ? 0.50126 0.50126 0.50126 0.00000  0.00000  0.00000  152 PHE   C CZ  
9816  N N   . LEU   G  153 ? 0.49542 0.49542 0.49542 0.00000  0.00000  0.00000  153 LEU   C N   
9817  C CA  . LEU   G  153 ? 0.51957 0.51957 0.51957 0.00000  0.00000  0.00000  153 LEU   C CA  
9818  C C   . LEU   G  153 ? 0.51432 0.51432 0.51432 -0.00000 0.00000  0.00000  153 LEU   C C   
9819  O O   . LEU   G  153 ? 0.56998 0.56998 0.56998 0.00000  0.00000  0.00000  153 LEU   C O   
9820  C CB  . LEU   G  153 ? 0.42737 0.42737 0.42737 0.00000  -0.00000 0.00000  153 LEU   C CB  
9821  C CG  . LEU   G  153 ? 0.59288 0.59288 0.59288 0.00000  0.00000  0.00000  153 LEU   C CG  
9822  C CD1 . LEU   G  153 ? 0.36716 0.36716 0.36716 0.00000  0.00000  0.00000  153 LEU   C CD1 
9823  C CD2 . LEU   G  153 ? 0.36737 0.36737 0.36737 -0.00000 0.00000  0.00000  153 LEU   C CD2 
9824  N N   . SER   G  154 ? 0.53328 0.53328 0.53328 0.00000  0.00000  -0.00000 154 SER   C N   
9825  C CA  . SER   G  154 ? 0.50480 0.50480 0.50480 0.00000  0.00000  0.00000  154 SER   C CA  
9826  C C   . SER   G  154 ? 0.63249 0.63249 0.63249 -0.00000 0.00000  0.00000  154 SER   C C   
9827  O O   . SER   G  154 ? 0.68621 0.68621 0.68621 0.00000  0.00000  0.00000  154 SER   C O   
9828  C CB  . SER   G  154 ? 0.34264 0.34264 0.34264 -0.00000 0.00000  0.00000  154 SER   C CB  
9829  O OG  . SER   G  154 ? 1.36388 1.36388 1.36388 -0.00000 0.00000  0.00000  154 SER   C OG  
9830  N N   . SER   G  155 ? 0.51545 0.51545 0.51545 0.00000  0.00000  0.00000  155 SER   C N   
9831  C CA  . SER   G  155 ? 0.52335 0.52335 0.52335 0.00000  0.00000  0.00000  155 SER   C CA  
9832  C C   . SER   G  155 ? 1.34158 1.34158 1.34158 0.00000  0.00000  0.00000  155 SER   C C   
9833  O O   . SER   G  155 ? 0.49916 0.49916 0.49916 0.00000  0.00000  -0.00000 155 SER   C O   
9834  C CB  . SER   G  155 ? 0.48222 0.48222 0.48222 -0.00000 0.00000  0.00000  155 SER   C CB  
9835  O OG  . SER   G  155 ? 0.60950 0.60950 0.60950 0.00000  0.00000  0.00000  155 SER   C OG  
9836  N N   . LYS   G  156 ? 0.64403 0.64403 0.64403 0.00000  0.00000  0.00000  156 LYS   C N   
9837  C CA  . LYS   G  156 ? 0.85703 0.85703 0.85703 -0.00000 0.00000  0.00000  156 LYS   C CA  
9838  C C   . LYS   G  156 ? 0.52040 0.52040 0.52040 0.00000  0.00000  0.00000  156 LYS   C C   
9839  O O   . LYS   G  156 ? 0.72107 0.72107 0.72107 0.00000  0.00000  0.00000  156 LYS   C O   
9840  C CB  . LYS   G  156 ? 0.42814 0.42814 0.42814 -0.00000 -0.00000 0.00000  156 LYS   C CB  
9841  C CG  . LYS   G  156 ? 1.26215 1.26215 1.26215 0.00000  0.00000  0.00000  156 LYS   C CG  
9842  C CD  . LYS   G  156 ? 1.71421 1.71421 1.71421 0.00000  0.00000  0.00000  156 LYS   C CD  
9843  C CE  . LYS   G  156 ? 1.69684 1.69684 1.69684 0.00000  0.00000  0.00000  156 LYS   C CE  
9844  N NZ  . LYS   G  156 ? 1.25521 1.25521 1.25521 0.00000  0.00000  0.00000  156 LYS   C NZ  
9845  N N   . ASP   G  157 ? 0.59788 0.59788 0.59788 0.00000  0.00000  0.00000  157 ASP   C N   
9846  C CA  . ASP   G  157 ? 0.58487 0.58487 0.58487 -0.00000 0.00000  0.00000  157 ASP   C CA  
9847  C C   . ASP   G  157 ? 0.61677 0.61677 0.61677 0.00000  0.00000  0.00000  157 ASP   C C   
9848  O O   . ASP   G  157 ? 0.56467 0.56467 0.56467 -0.00000 0.00000  0.00000  157 ASP   C O   
9849  C CB  . ASP   G  157 ? 0.72864 0.72864 0.72864 -0.00000 0.00000  0.00000  157 ASP   C CB  
9850  C CG  . ASP   G  157 ? 0.74178 0.74178 0.74178 0.00000  0.00000  0.00000  157 ASP   C CG  
9851  O OD1 . ASP   G  157 ? 0.87605 0.87605 0.87605 0.00000  0.00000  0.00000  157 ASP   C OD1 
9852  O OD2 . ASP   G  157 ? 1.11292 1.11292 1.11292 0.00000  0.00000  0.00000  157 ASP   C OD2 
9853  N N   . SER   G  158 ? 0.81915 0.81915 0.81915 0.00000  0.00000  0.00000  158 SER   C N   
9854  C CA  . SER   G  158 ? 0.63461 0.63461 0.63461 -0.00000 0.00000  0.00000  158 SER   C CA  
9855  C C   . SER   G  158 ? 0.67064 0.67064 0.67064 0.00000  0.00000  0.00000  158 SER   C C   
9856  O O   . SER   G  158 ? 0.60806 0.60806 0.60806 -0.00000 0.00000  0.00000  158 SER   C O   
9857  C CB  . SER   G  158 ? 0.55175 0.55175 0.55175 0.00000  0.00000  0.00000  158 SER   C CB  
9858  O OG  . SER   G  158 ? 0.54489 0.54489 0.54489 0.00000  0.00000  0.00000  158 SER   C OG  
9859  N N   . ARG   G  159 ? 0.59379 0.59379 0.59379 0.00000  0.00000  0.00000  159 ARG   C N   
9860  C CA  . ARG   G  159 ? 0.68518 0.68518 0.68518 0.00000  -0.00000 0.00000  159 ARG   C CA  
9861  C C   . ARG   G  159 ? 0.69476 0.69476 0.69476 0.00000  0.00000  0.00000  159 ARG   C C   
9862  O O   . ARG   G  159 ? 0.62406 0.62406 0.62406 -0.00000 0.00000  0.00000  159 ARG   C O   
9863  C CB  . ARG   G  159 ? 0.46522 0.46522 0.46522 0.00000  0.00000  0.00000  159 ARG   C CB  
9864  C CG  . ARG   G  159 ? 0.92078 0.92078 0.92078 -0.00000 0.00000  0.00000  159 ARG   C CG  
9865  C CD  . ARG   G  159 ? 0.71919 0.71919 0.71919 -0.00000 0.00000  0.00000  159 ARG   C CD  
9866  N NE  . ARG   G  159 ? 0.89477 0.89477 0.89477 0.00000  0.00000  0.00000  159 ARG   C NE  
9867  C CZ  . ARG   G  159 ? 0.78290 0.78290 0.78290 -0.00000 0.00000  0.00000  159 ARG   C CZ  
9868  N NH1 . ARG   G  159 ? 0.68755 0.68755 0.68755 0.00000  0.00000  0.00000  159 ARG   C NH1 
9869  N NH2 . ARG   G  159 ? 0.65235 0.65235 0.65235 0.00000  0.00000  0.00000  159 ARG   C NH2 
9870  N N   . ASN   G  160 ? 0.58084 0.58084 0.58084 -0.00000 0.00000  0.00000  160 ASN   C N   
9871  C CA  . ASN   G  160 ? 0.63588 0.63588 0.63588 0.00000  0.00000  0.00000  160 ASN   C CA  
9872  C C   . ASN   G  160 ? 0.53997 0.53997 0.53997 0.00000  0.00000  0.00000  160 ASN   C C   
9873  O O   . ASN   G  160 ? 0.91704 0.91704 0.91704 0.00000  0.00000  0.00000  160 ASN   C O   
9874  C CB  . ASN   G  160 ? 0.61117 0.61117 0.61117 0.00000  0.00000  0.00000  160 ASN   C CB  
9875  C CG  . ASN   G  160 ? 0.76536 0.76536 0.76536 -0.00000 0.00000  0.00000  160 ASN   C CG  
9876  O OD1 . ASN   G  160 ? 0.93579 0.93579 0.93579 -0.00000 0.00000  -0.00000 160 ASN   C OD1 
9877  N ND2 . ASN   G  160 ? 0.81847 0.81847 0.81847 0.00000  0.00000  0.00000  160 ASN   C ND2 
9878  N N   . VAL   G  161 ? 0.63472 0.63472 0.63472 0.00000  0.00000  0.00000  161 VAL   C N   
9879  C CA  . VAL   G  161 ? 0.67024 0.67024 0.67024 0.00000  -0.00000 0.00000  161 VAL   C CA  
9880  C C   . VAL   G  161 ? 0.70444 0.70444 0.70444 0.00000  0.00000  0.00000  161 VAL   C C   
9881  O O   . VAL   G  161 ? 0.48538 0.48538 0.48538 0.00000  0.00000  0.00000  161 VAL   C O   
9882  C CB  . VAL   G  161 ? 0.59357 0.59357 0.59357 0.00000  0.00000  0.00000  161 VAL   C CB  
9883  C CG1 . VAL   G  161 ? 0.45255 0.45255 0.45255 0.00000  0.00000  0.00000  161 VAL   C CG1 
9884  C CG2 . VAL   G  161 ? 0.38786 0.38786 0.38786 0.00000  0.00000  0.00000  161 VAL   C CG2 
9885  N N   . LEU   G  162 ? 0.51669 0.51669 0.51669 0.00000  0.00000  0.00000  162 LEU   C N   
9886  C CA  . LEU   G  162 ? 0.64899 0.64899 0.64899 0.00000  0.00000  0.00000  162 LEU   C CA  
9887  C C   . LEU   G  162 ? 0.88875 0.88875 0.88875 -0.00000 0.00000  0.00000  162 LEU   C C   
9888  O O   . LEU   G  162 ? 0.66833 0.66833 0.66833 0.00000  -0.00000 0.00000  162 LEU   C O   
9889  C CB  . LEU   G  162 ? 0.60665 0.60665 0.60665 -0.00000 0.00000  0.00000  162 LEU   C CB  
9890  C CG  . LEU   G  162 ? 0.46277 0.46277 0.46277 -0.00000 0.00000  0.00000  162 LEU   C CG  
9891  C CD1 . LEU   G  162 ? 0.40823 0.40823 0.40823 0.00000  0.00000  0.00000  162 LEU   C CD1 
9892  C CD2 . LEU   G  162 ? 0.39357 0.39357 0.39357 0.00000  -0.00000 0.00000  162 LEU   C CD2 
9893  N N   . VAL   G  163 ? 0.66896 0.66896 0.66896 -0.00000 0.00000  0.00000  163 VAL   C N   
9894  C CA  . VAL   G  163 ? 0.63153 0.63153 0.63153 0.00000  0.00000  0.00000  163 VAL   C CA  
9895  C C   . VAL   G  163 ? 0.89022 0.89022 0.89022 -0.00000 -0.00000 0.00000  163 VAL   C C   
9896  O O   . VAL   G  163 ? 0.79628 0.79628 0.79628 -0.00000 0.00000  0.00000  163 VAL   C O   
9897  C CB  . VAL   G  163 ? 0.65636 0.65636 0.65636 0.00000  0.00000  0.00000  163 VAL   C CB  
9898  C CG1 . VAL   G  163 ? 0.57511 0.57511 0.57511 0.00000  0.00000  0.00000  163 VAL   C CG1 
9899  C CG2 . VAL   G  163 ? 0.56914 0.56914 0.56914 0.00000  0.00000  0.00000  163 VAL   C CG2 
9900  N N   . ALA   G  164 ? 0.69254 0.69254 0.69254 0.00000  -0.00000 0.00000  164 ALA   C N   
9901  C CA  . ALA   G  164 ? 0.78887 0.78887 0.78887 0.00000  0.00000  0.00000  164 ALA   C CA  
9902  C C   . ALA   G  164 ? 0.67489 0.67489 0.67489 0.00000  0.00000  0.00000  164 ALA   C C   
9903  O O   . ALA   G  164 ? 0.64848 0.64848 0.64848 0.00000  0.00000  0.00000  164 ALA   C O   
9904  C CB  . ALA   G  164 ? 0.41976 0.41976 0.41976 -0.00000 -0.00000 0.00000  164 ALA   C CB  
9905  N N   . ASP   G  165 ? 0.72260 0.72260 0.72260 0.00000  0.00000  0.00000  165 ASP   C N   
9906  C CA  . ASP   G  165 ? 0.70150 0.70150 0.70150 0.00000  0.00000  0.00000  165 ASP   C CA  
9907  C C   . ASP   G  165 ? 0.69974 0.69974 0.69974 0.00000  0.00000  0.00000  165 ASP   C C   
9908  O O   . ASP   G  165 ? 1.14329 1.14329 1.14329 0.00000  0.00000  0.00000  165 ASP   C O   
9909  C CB  . ASP   G  165 ? 0.79365 0.79365 0.79365 0.00000  0.00000  0.00000  165 ASP   C CB  
9910  C CG  . ASP   G  165 ? 0.64108 0.64108 0.64108 0.00000  0.00000  0.00000  165 ASP   C CG  
9911  O OD1 . ASP   G  165 ? 1.22685 1.22685 1.22685 -0.00000 0.00000  0.00000  165 ASP   C OD1 
9912  O OD2 . ASP   G  165 ? 1.26102 1.26102 1.26102 0.00000  0.00000  0.00000  165 ASP   C OD2 
9913  N N   . GLN   G  166 ? 0.86289 0.86289 0.86289 0.00000  0.00000  0.00000  166 GLN   C N   
9914  C CA  . GLN   G  166 ? 1.04614 1.04614 1.04614 -0.00000 0.00000  0.00000  166 GLN   C CA  
9915  C C   . GLN   G  166 ? 0.56814 0.56814 0.56814 0.00000  0.00000  0.00000  166 GLN   C C   
9916  O O   . GLN   G  166 ? 1.50032 1.50032 1.50032 0.00000  0.00000  0.00000  166 GLN   C O   
9917  C CB  . GLN   G  166 ? 0.53428 0.53428 0.53428 -0.00000 0.00000  0.00000  166 GLN   C CB  
9918  C CG  . GLN   G  166 ? 0.99676 0.99676 0.99676 -0.00000 0.00000  0.00000  166 GLN   C CG  
9919  C CD  . GLN   G  166 ? 1.74932 1.74932 1.74932 0.00000  0.00000  0.00000  166 GLN   C CD  
9920  O OE1 . GLN   G  166 ? 1.17641 1.17641 1.17641 -0.00000 0.00000  0.00000  166 GLN   C OE1 
9921  N NE2 . GLN   G  166 ? 1.00421 1.00421 1.00421 0.00000  0.00000  0.00000  166 GLN   C NE2 
9922  N N   . PHE   G  167 ? 0.87672 0.87672 0.87672 0.00000  0.00000  0.00000  167 PHE   C N   
9923  C CA  . PHE   G  167 ? 0.86352 0.86352 0.86352 0.00000  0.00000  0.00000  167 PHE   C CA  
9924  C C   . PHE   G  167 ? 0.88257 0.88257 0.88257 -0.00000 0.00000  0.00000  167 PHE   C C   
9925  O O   . PHE   G  167 ? 0.83165 0.83165 0.83165 0.00000  0.00000  0.00000  167 PHE   C O   
9926  C CB  . PHE   G  167 ? 0.73816 0.73816 0.73816 0.00000  0.00000  0.00000  167 PHE   C CB  
9927  C CG  . PHE   G  167 ? 0.80777 0.80777 0.80777 0.00000  0.00000  0.00000  167 PHE   C CG  
9928  C CD1 . PHE   G  167 ? 0.65850 0.65850 0.65850 0.00000  0.00000  0.00000  167 PHE   C CD1 
9929  C CD2 . PHE   G  167 ? 0.54588 0.54588 0.54588 -0.00000 0.00000  0.00000  167 PHE   C CD2 
9930  C CE1 . PHE   G  167 ? 1.55422 1.55422 1.55422 0.00000  0.00000  0.00000  167 PHE   C CE1 
9931  C CE2 . PHE   G  167 ? 1.41264 1.41264 1.41264 0.00000  0.00000  0.00000  167 PHE   C CE2 
9932  C CZ  . PHE   G  167 ? 0.39032 0.39032 0.39032 -0.00000 0.00000  0.00000  167 PHE   C CZ  
9933  N N   . ASP   G  168 ? 1.03148 1.03148 1.03148 0.00000  0.00000  0.00000  168 ASP   C N   
9934  C CA  . ASP   G  168 ? 0.59166 0.59166 0.59166 0.00000  0.00000  0.00000  168 ASP   C CA  
9935  C C   . ASP   G  168 ? 1.24152 1.24152 1.24152 -0.00000 0.00000  0.00000  168 ASP   C C   
9936  O O   . ASP   G  168 ? 0.90620 0.90620 0.90620 0.00000  0.00000  0.00000  168 ASP   C O   
9937  C CB  . ASP   G  168 ? 0.76998 0.76998 0.76998 0.00000  0.00000  0.00000  168 ASP   C CB  
9938  C CG  . ASP   G  168 ? 1.08392 1.08392 1.08392 -0.00000 0.00000  0.00000  168 ASP   C CG  
9939  O OD1 . ASP   G  168 ? 0.90446 0.90446 0.90446 0.00000  0.00000  0.00000  168 ASP   C OD1 
9940  O OD2 . ASP   G  168 ? 1.05549 1.05549 1.05549 -0.00000 0.00000  0.00000  168 ASP   C OD2 
9941  N N   . ASP   G  169 ? 0.83032 0.83032 0.83032 -0.00000 0.00000  0.00000  169 ASP   C N   
9942  C CA  . ASP   G  169 ? 0.87961 0.87961 0.87961 0.00000  0.00000  0.00000  169 ASP   C CA  
9943  C C   . ASP   G  169 ? 1.09299 1.09299 1.09299 -0.00000 0.00000  0.00000  169 ASP   C C   
9944  O O   . ASP   G  169 ? 0.93884 0.93884 0.93884 0.00000  0.00000  0.00000  169 ASP   C O   
9945  C CB  . ASP   G  169 ? 0.60836 0.60836 0.60836 0.00000  0.00000  0.00000  169 ASP   C CB  
9946  N N   . ARG   G  170 ? 1.67771 1.67771 1.67771 0.00000  0.00000  -0.00000 170 ARG   C N   
9947  C CA  . ARG   G  170 ? 0.54924 0.54924 0.54924 -0.00000 0.00000  0.00000  170 ARG   C CA  
9948  C C   . ARG   G  170 ? 0.78081 0.78081 0.78081 0.00000  0.00000  0.00000  170 ARG   C C   
9949  O O   . ARG   G  170 ? 0.66703 0.66703 0.66703 0.00000  0.00000  0.00000  170 ARG   C O   
9950  C CB  . ARG   G  170 ? 0.62337 0.62337 0.62337 0.00000  0.00000  0.00000  170 ARG   C CB  
9951  N N   . HIS   G  171 ? 0.79306 0.79306 0.79306 -0.00000 0.00000  0.00000  171 HIS   C N   
9952  C CA  . HIS   G  171 ? 0.83397 0.83397 0.83397 -0.00000 0.00000  0.00000  171 HIS   C CA  
9953  C C   . HIS   G  171 ? 0.41035 0.41035 0.41035 0.00000  0.00000  0.00000  171 HIS   C C   
9954  O O   . HIS   G  171 ? 1.31311 1.31311 1.31311 0.00000  0.00000  -0.00000 171 HIS   C O   
9955  C CB  . HIS   G  171 ? 0.86904 0.86904 0.86904 0.00000  0.00000  0.00000  171 HIS   C CB  
9956  C CG  . HIS   G  171 ? 0.80804 0.80804 0.80804 -0.00000 0.00000  0.00000  171 HIS   C CG  
9957  N ND1 . HIS   G  171 ? 0.87977 0.87977 0.87977 0.00000  0.00000  -0.00000 171 HIS   C ND1 
9958  C CD2 . HIS   G  171 ? 0.81092 0.81092 0.81092 0.00000  0.00000  -0.00000 171 HIS   C CD2 
9959  C CE1 . HIS   G  171 ? 0.56003 0.56003 0.56003 -0.00000 0.00000  0.00000  171 HIS   C CE1 
9960  N NE2 . HIS   G  171 ? 1.51325 1.51325 1.51325 0.00000  0.00000  0.00000  171 HIS   C NE2 
9961  N N   . CYS   G  172 ? 0.91163 0.91163 0.91163 -0.00000 0.00000  0.00000  172 CYS   C N   
9962  C CA  . CYS   G  172 ? 0.52314 0.52314 0.52314 0.00000  0.00000  0.00000  172 CYS   C CA  
9963  C C   . CYS   G  172 ? 0.53655 0.53655 0.53655 -0.00000 0.00000  0.00000  172 CYS   C C   
9964  O O   . CYS   G  172 ? 0.82696 0.82696 0.82696 0.00000  0.00000  0.00000  172 CYS   C O   
9965  C CB  . CYS   G  172 ? 0.63859 0.63859 0.63859 0.00000  0.00000  0.00000  172 CYS   C CB  
9966  S SG  . CYS   G  172 ? 0.73959 0.73959 0.73959 0.00000  0.00000  0.00000  172 CYS   C SG  
9967  N N   . GLY   G  173 ? 0.78850 0.78850 0.78850 0.00000  0.00000  0.00000  173 GLY   C N   
9968  C CA  . GLY   G  173 ? 0.59412 0.59412 0.59412 -0.00000 0.00000  0.00000  173 GLY   C CA  
9969  C C   . GLY   G  173 ? 0.77863 0.77863 0.77863 0.00000  0.00000  0.00000  173 GLY   C C   
9970  O O   . GLY   G  173 ? 0.77933 0.77933 0.77933 0.00000  0.00000  0.00000  173 GLY   C O   
9971  N N   . TRP   G  174 ? 0.46574 0.46574 0.46574 -0.00000 0.00000  0.00000  174 TRP   C N   
9972  C CA  . TRP   G  174 ? 0.78969 0.78969 0.78969 0.00000  0.00000  0.00000  174 TRP   C CA  
9973  C C   . TRP   G  174 ? 0.89839 0.89839 0.89839 0.00000  0.00000  0.00000  174 TRP   C C   
9974  O O   . TRP   G  174 ? 0.69804 0.69804 0.69804 0.00000  0.00000  0.00000  174 TRP   C O   
9975  C CB  . TRP   G  174 ? 0.50794 0.50794 0.50794 0.00000  0.00000  0.00000  174 TRP   C CB  
9976  C CG  . TRP   G  174 ? 0.88853 0.88853 0.88853 0.00000  0.00000  0.00000  174 TRP   C CG  
9977  C CD1 . TRP   G  174 ? 0.60928 0.60928 0.60928 0.00000  0.00000  0.00000  174 TRP   C CD1 
9978  C CD2 . TRP   G  174 ? 0.71963 0.71963 0.71963 -0.00000 0.00000  0.00000  174 TRP   C CD2 
9979  N NE1 . TRP   G  174 ? 0.64070 0.64070 0.64070 0.00000  0.00000  0.00000  174 TRP   C NE1 
9980  C CE2 . TRP   G  174 ? 0.54013 0.54013 0.54013 0.00000  0.00000  0.00000  174 TRP   C CE2 
9981  C CE3 . TRP   G  174 ? 0.56822 0.56822 0.56822 0.00000  0.00000  0.00000  174 TRP   C CE3 
9982  C CZ2 . TRP   G  174 ? 0.44402 0.44402 0.44402 0.00000  0.00000  0.00000  174 TRP   C CZ2 
9983  C CZ3 . TRP   G  174 ? 0.59400 0.59400 0.59400 0.00000  0.00000  0.00000  174 TRP   C CZ3 
9984  C CH2 . TRP   G  174 ? 0.48194 0.48194 0.48194 0.00000  0.00000  0.00000  174 TRP   C CH2 
9985  N N   . LEU   G  175 ? 0.62983 0.62983 0.62983 0.00000  0.00000  0.00000  175 LEU   C N   
9986  C CA  . LEU   G  175 ? 0.56592 0.56592 0.56592 -0.00000 0.00000  0.00000  175 LEU   C CA  
9987  C C   . LEU   G  175 ? 0.68873 0.68873 0.68873 0.00000  0.00000  0.00000  175 LEU   C C   
9988  O O   . LEU   G  175 ? 0.80081 0.80081 0.80081 0.00000  0.00000  0.00000  175 LEU   C O   
9989  C CB  . LEU   G  175 ? 0.50256 0.50256 0.50256 0.00000  0.00000  0.00000  175 LEU   C CB  
9990  C CG  . LEU   G  175 ? 0.63695 0.63695 0.63695 0.00000  0.00000  0.00000  175 LEU   C CG  
9991  C CD1 . LEU   G  175 ? 0.51722 0.51722 0.51722 0.00000  0.00000  0.00000  175 LEU   C CD1 
9992  C CD2 . LEU   G  175 ? 0.47852 0.47852 0.47852 -0.00000 0.00000  0.00000  175 LEU   C CD2 
9993  N N   . ASN   G  176 ? 0.65631 0.65631 0.65631 0.00000  0.00000  0.00000  176 ASN   C N   
9994  C CA  . ASN   G  176 ? 0.60045 0.60045 0.60045 -0.00000 0.00000  0.00000  176 ASN   C CA  
9995  C C   . ASN   G  176 ? 0.80827 0.80827 0.80827 -0.00000 0.00000  0.00000  176 ASN   C C   
9996  O O   . ASN   G  176 ? 0.98413 0.98413 0.98413 0.00000  0.00000  0.00000  176 ASN   C O   
9997  C CB  . ASN   G  176 ? 0.94143 0.94143 0.94143 0.00000  0.00000  0.00000  176 ASN   C CB  
9998  C CG  . ASN   G  176 ? 0.92004 0.92004 0.92004 0.00000  0.00000  0.00000  176 ASN   C CG  
9999  O OD1 . ASN   G  176 ? 0.74509 0.74509 0.74509 0.00000  0.00000  0.00000  176 ASN   C OD1 
10000 N ND2 . ASN   G  176 ? 0.76208 0.76208 0.76208 -0.00000 0.00000  0.00000  176 ASN   C ND2 
10001 N N   . GLU   G  177 ? 0.76293 0.76293 0.76293 0.00000  0.00000  0.00000  177 GLU   C N   
10002 C CA  . GLU   G  177 ? 0.72872 0.72872 0.72872 0.00000  0.00000  0.00000  177 GLU   C CA  
10003 C C   . GLU   G  177 ? 0.64982 0.64982 0.64982 0.00000  0.00000  0.00000  177 GLU   C C   
10004 O O   . GLU   G  177 ? 0.76694 0.76694 0.76694 0.00000  0.00000  0.00000  177 GLU   C O   
10005 C CB  . GLU   G  177 ? 0.49761 0.49761 0.49761 0.00000  0.00000  0.00000  177 GLU   C CB  
10006 N N   . ARG   G  178 ? 0.59097 0.59097 0.59097 0.00000  0.00000  0.00000  178 ARG   C N   
10007 C CA  . ARG   G  178 ? 0.88939 0.88939 0.88939 0.00000  0.00000  0.00000  178 ARG   C CA  
10008 C C   . ARG   G  178 ? 0.84096 0.84096 0.84096 -0.00000 0.00000  0.00000  178 ARG   C C   
10009 O O   . ARG   G  178 ? 0.82145 0.82145 0.82145 0.00000  0.00000  0.00000  178 ARG   C O   
10010 C CB  . ARG   G  178 ? 0.44844 0.44844 0.44844 -0.00000 0.00000  0.00000  178 ARG   C CB  
10011 C CG  . ARG   G  178 ? 0.96092 0.96092 0.96092 -0.00000 0.00000  0.00000  178 ARG   C CG  
10012 C CD  . ARG   G  178 ? 1.14518 1.14518 1.14518 0.00000  -0.00000 0.00000  178 ARG   C CD  
10013 N NE  . ARG   G  178 ? 1.50339 1.50339 1.50339 0.00000  0.00000  0.00000  178 ARG   C NE  
10014 N N   . ALA   G  179 ? 0.70351 0.70351 0.70351 0.00000  0.00000  0.00000  179 ALA   C N   
10015 C CA  . ALA   G  179 ? 0.68661 0.68661 0.68661 0.00000  0.00000  0.00000  179 ALA   C CA  
10016 C C   . ALA   G  179 ? 0.54494 0.54494 0.54494 -0.00000 0.00000  0.00000  179 ALA   C C   
10017 O O   . ALA   G  179 ? 0.64177 0.64177 0.64177 0.00000  0.00000  0.00000  179 ALA   C O   
10018 C CB  . ALA   G  179 ? 0.38061 0.38061 0.38061 0.00000  0.00000  0.00000  179 ALA   C CB  
10019 N N   . LEU   G  180 ? 0.62430 0.62430 0.62430 0.00000  0.00000  0.00000  180 LEU   C N   
10020 C CA  . LEU   G  180 ? 0.45909 0.45909 0.45909 0.00000  0.00000  0.00000  180 LEU   C CA  
10021 C C   . LEU   G  180 ? 0.66652 0.66652 0.66652 0.00000  0.00000  0.00000  180 LEU   C C   
10022 O O   . LEU   G  180 ? 0.66804 0.66804 0.66804 0.00000  0.00000  0.00000  180 LEU   C O   
10023 C CB  . LEU   G  180 ? 0.40000 0.40000 0.40000 -0.00000 0.00000  0.00000  180 LEU   C CB  
10024 C CG  . LEU   G  180 ? 0.71431 0.71431 0.71431 0.00000  0.00000  0.00000  180 LEU   C CG  
10025 C CD1 . LEU   G  180 ? 0.68431 0.68431 0.68431 -0.00000 0.00000  0.00000  180 LEU   C CD1 
10026 C CD2 . LEU   G  180 ? 0.55821 0.55821 0.55821 -0.00000 0.00000  0.00000  180 LEU   C CD2 
10027 N N   . SER   G  181 ? 0.61170 0.61170 0.61170 0.00000  0.00000  0.00000  181 SER   C N   
10028 C CA  . SER   G  181 ? 0.66124 0.66124 0.66124 -0.00000 0.00000  0.00000  181 SER   C CA  
10029 C C   . SER   G  181 ? 0.50545 0.50545 0.50545 0.00000  -0.00000 0.00000  181 SER   C C   
10030 O O   . SER   G  181 ? 0.64873 0.64873 0.64873 -0.00000 0.00000  0.00000  181 SER   C O   
10031 C CB  . SER   G  181 ? 0.43808 0.43808 0.43808 0.00000  -0.00000 -0.00000 181 SER   C CB  
10032 O OG  . SER   G  181 ? 1.30210 1.30210 1.30210 0.00000  0.00000  0.00000  181 SER   C OG  
10033 N N   . ALA   G  182 ? 0.66013 0.66013 0.66013 0.00000  0.00000  0.00000  182 ALA   C N   
10034 C CA  . ALA   G  182 ? 0.93457 0.93457 0.93457 -0.00000 0.00000  0.00000  182 ALA   C CA  
10035 C C   . ALA   G  182 ? 0.67505 0.67505 0.67505 0.00000  0.00000  0.00000  182 ALA   C C   
10036 O O   . ALA   G  182 ? 0.52087 0.52087 0.52087 -0.00000 0.00000  0.00000  182 ALA   C O   
10037 C CB  . ALA   G  182 ? 0.40928 0.40928 0.40928 0.00000  0.00000  0.00000  182 ALA   C CB  
10038 N N   . MET   G  183 ? 0.46957 0.46957 0.46957 0.00000  0.00000  0.00000  183 MET   C N   
10039 C CA  . MET   G  183 ? 0.67381 0.67381 0.67381 0.00000  0.00000  0.00000  183 MET   C CA  
10040 C C   . MET   G  183 ? 0.48815 0.48815 0.48815 0.00000  0.00000  0.00000  183 MET   C C   
10041 O O   . MET   G  183 ? 0.72365 0.72365 0.72365 0.00000  0.00000  0.00000  183 MET   C O   
10042 C CB  . MET   G  183 ? 0.47953 0.47953 0.47953 0.00000  0.00000  0.00000  183 MET   C CB  
10043 C CG  . MET   G  183 ? 0.50614 0.50614 0.50614 0.00000  0.00000  0.00000  183 MET   C CG  
10044 S SD  . MET   G  183 ? 0.62279 0.62279 0.62279 0.00000  0.00000  0.00000  183 MET   C SD  
10045 C CE  . MET   G  183 ? 0.57535 0.57535 0.57535 0.00000  0.00000  0.00000  183 MET   C CE  
10046 N N   . VAL   G  184 ? 0.53257 0.53257 0.53257 0.00000  0.00000  0.00000  184 VAL   C N   
10047 C CA  . VAL   G  184 ? 0.61943 0.61943 0.61943 -0.00000 0.00000  0.00000  184 VAL   C CA  
10048 C C   . VAL   G  184 ? 0.38567 0.38567 0.38567 0.00000  0.00000  0.00000  184 VAL   C C   
10049 O O   . VAL   G  184 ? 0.52402 0.52402 0.52402 0.00000  -0.00000 0.00000  184 VAL   C O   
10050 C CB  . VAL   G  184 ? 0.35868 0.35868 0.35868 0.00000  0.00000  0.00000  184 VAL   C CB  
10051 C CG1 . VAL   G  184 ? 0.42849 0.42849 0.42849 -0.00000 0.00000  0.00000  184 VAL   C CG1 
10052 C CG2 . VAL   G  184 ? 0.37274 0.37274 0.37274 0.00000  0.00000  0.00000  184 VAL   C CG2 
10053 N N   . LYS   G  185 ? 0.51811 0.51811 0.51811 0.00000  0.00000  0.00000  185 LYS   C N   
10054 C CA  . LYS   G  185 ? 0.55453 0.55453 0.55453 0.00000  0.00000  0.00000  185 LYS   C CA  
10055 C C   . LYS   G  185 ? 0.24704 0.24704 0.24704 -0.00000 0.00000  0.00000  185 LYS   C C   
10056 O O   . LYS   G  185 ? 0.98704 0.98704 0.98704 -0.00000 0.00000  0.00000  185 LYS   C O   
10057 C CB  . LYS   G  185 ? 0.41039 0.41039 0.41039 0.00000  0.00000  0.00000  185 LYS   C CB  
10058 C CG  . LYS   G  185 ? 0.48897 0.48897 0.48897 0.00000  0.00000  0.00000  185 LYS   C CG  
10059 C CD  . LYS   G  185 ? 0.81113 0.81113 0.81113 0.00000  0.00000  0.00000  185 LYS   C CD  
10060 C CE  . LYS   G  185 ? 0.81929 0.81929 0.81929 0.00000  0.00000  0.00000  185 LYS   C CE  
10061 N NZ  . LYS   G  185 ? 0.99312 0.99312 0.99312 0.00000  0.00000  0.00000  185 LYS   C NZ  
10062 N N   . HIS   G  186 ? 0.62931 0.62931 0.62931 -0.00000 0.00000  0.00000  186 HIS   C N   
10063 C CA  . HIS   G  186 ? 0.40247 0.40247 0.40247 0.00000  0.00000  -0.00000 186 HIS   C CA  
10064 C C   . HIS   G  186 ? 0.64613 0.64613 0.64613 0.00000  0.00000  0.00000  186 HIS   C C   
10065 O O   . HIS   G  186 ? 0.47076 0.47076 0.47076 0.00000  0.00000  0.00000  186 HIS   C O   
10066 C CB  . HIS   G  186 ? 0.50944 0.50944 0.50944 0.00000  0.00000  0.00000  186 HIS   C CB  
10067 C CG  . HIS   G  186 ? 0.83929 0.83929 0.83929 0.00000  0.00000  0.00000  186 HIS   C CG  
10068 N ND1 . HIS   G  186 ? 0.67436 0.67436 0.67436 0.00000  0.00000  -0.00000 186 HIS   C ND1 
10069 C CD2 . HIS   G  186 ? 0.32810 0.32810 0.32810 0.00000  0.00000  0.00000  186 HIS   C CD2 
10070 C CE1 . HIS   G  186 ? 0.51958 0.51958 0.51958 -0.00000 0.00000  0.00000  186 HIS   C CE1 
10071 N NE2 . HIS   G  186 ? 0.72293 0.72293 0.72293 0.00000  0.00000  0.00000  186 HIS   C NE2 
10072 N N   . TYR   G  187 ? 0.55253 0.55253 0.55253 0.00000  0.00000  0.00000  187 TYR   C N   
10073 C CA  . TYR   G  187 ? 0.65334 0.65334 0.65334 -0.00000 0.00000  0.00000  187 TYR   C CA  
10074 C C   . TYR   G  187 ? 1.10786 1.10786 1.10786 0.00000  0.00000  0.00000  187 TYR   C C   
10075 O O   . TYR   G  187 ? 0.57024 0.57024 0.57024 0.00000  0.00000  0.00000  187 TYR   C O   
10076 C CB  . TYR   G  187 ? 0.71047 0.71047 0.71047 -0.00000 0.00000  0.00000  187 TYR   C CB  
10077 C CG  . TYR   G  187 ? 0.50792 0.50792 0.50792 0.00000  -0.00000 0.00000  187 TYR   C CG  
10078 C CD1 . TYR   G  187 ? 0.61462 0.61462 0.61462 0.00000  0.00000  0.00000  187 TYR   C CD1 
10079 C CD2 . TYR   G  187 ? 0.69443 0.69443 0.69443 -0.00000 0.00000  0.00000  187 TYR   C CD2 
10080 C CE1 . TYR   G  187 ? 0.56286 0.56286 0.56286 0.00000  0.00000  0.00000  187 TYR   C CE1 
10081 C CE2 . TYR   G  187 ? 0.34180 0.34180 0.34180 0.00000  0.00000  0.00000  187 TYR   C CE2 
10082 C CZ  . TYR   G  187 ? 0.68857 0.68857 0.68857 -0.00000 -0.00000 0.00000  187 TYR   C CZ  
10083 O OH  . TYR   G  187 ? 0.60488 0.60488 0.60488 0.00000  0.00000  0.00000  187 TYR   C OH  
10084 N N   . ASN   G  188 ? 0.44351 0.44351 0.44351 -0.00000 0.00000  0.00000  188 ASN   C N   
10085 C CA  . ASN   G  188 ? 1.07308 1.07308 1.07308 -0.00000 0.00000  0.00000  188 ASN   C CA  
10086 C C   . ASN   G  188 ? 0.43045 0.43045 0.43045 0.00000  0.00000  0.00000  188 ASN   C C   
10087 O O   . ASN   G  188 ? 0.85452 0.85452 0.85452 0.00000  0.00000  0.00000  188 ASN   C O   
10088 C CB  . ASN   G  188 ? 0.57586 0.57586 0.57586 0.00000  0.00000  0.00000  188 ASN   C CB  
10089 C CG  . ASN   G  188 ? 1.07369 1.07369 1.07369 0.00000  0.00000  0.00000  188 ASN   C CG  
10090 O OD1 . ASN   G  188 ? 1.42640 1.42640 1.42640 -0.00000 0.00000  0.00000  188 ASN   C OD1 
10091 N ND2 . ASN   G  188 ? 1.23631 1.23631 1.23631 0.00000  0.00000  0.00000  188 ASN   C ND2 
10092 N N   . GLY   G  189 ? 0.84402 0.84402 0.84402 -0.00000 0.00000  0.00000  189 GLY   C N   
10093 C CA  . GLY   G  189 ? 0.42502 0.42502 0.42502 0.00000  0.00000  0.00000  189 GLY   C CA  
10094 C C   . GLY   G  189 ? 0.47777 0.47777 0.47777 -0.00000 0.00000  0.00000  189 GLY   C C   
10095 O O   . GLY   G  189 ? 0.89441 0.89441 0.89441 0.00000  0.00000  0.00000  189 GLY   C O   
10096 N N   . ARG   G  190 ? 0.63487 0.63487 0.63487 0.00000  0.00000  0.00000  190 ARG   C N   
10097 C CA  . ARG   G  190 ? 0.48493 0.48493 0.48493 0.00000  0.00000  0.00000  190 ARG   C CA  
10098 C C   . ARG   G  190 ? 0.57505 0.57505 0.57505 0.00000  0.00000  0.00000  190 ARG   C C   
10099 O O   . ARG   G  190 ? 0.71040 0.71040 0.71040 0.00000  0.00000  0.00000  190 ARG   C O   
10100 C CB  . ARG   G  190 ? 0.57625 0.57625 0.57625 0.00000  0.00000  0.00000  190 ARG   C CB  
10101 C CG  . ARG   G  190 ? 0.50857 0.50857 0.50857 0.00000  0.00000  0.00000  190 ARG   C CG  
10102 C CD  . ARG   G  190 ? 0.38832 0.38832 0.38832 0.00000  0.00000  0.00000  190 ARG   C CD  
10103 N NE  . ARG   G  190 ? 0.57395 0.57395 0.57395 0.00000  -0.00000 -0.00000 190 ARG   C NE  
10104 C CZ  . ARG   G  190 ? 0.78901 0.78901 0.78901 0.00000  0.00000  0.00000  190 ARG   C CZ  
10105 N NH1 . ARG   G  190 ? 0.74160 0.74160 0.74160 0.00000  0.00000  0.00000  190 ARG   C NH1 
10106 N NH2 . ARG   G  190 ? 0.60732 0.60732 0.60732 0.00000  0.00000  0.00000  190 ARG   C NH2 
10107 N N   . ALA   G  191 ? 0.59701 0.59701 0.59701 0.00000  0.00000  0.00000  191 ALA   C N   
10108 C CA  . ALA   G  191 ? 0.44243 0.44243 0.44243 0.00000  0.00000  0.00000  191 ALA   C CA  
10109 C C   . ALA   G  191 ? 1.24081 1.24081 1.24081 -0.00000 0.00000  0.00000  191 ALA   C C   
10110 O O   . ALA   G  191 ? 0.45833 0.45833 0.45833 0.00000  0.00000  0.00000  191 ALA   C O   
10111 C CB  . ALA   G  191 ? 0.59842 0.59842 0.59842 0.00000  0.00000  0.00000  191 ALA   C CB  
10112 N N   . PHE   G  192 ? 0.42658 0.42658 0.42658 0.00000  0.00000  0.00000  192 PHE   C N   
10113 C CA  . PHE   G  192 ? 0.47563 0.47563 0.47563 0.00000  0.00000  0.00000  192 PHE   C CA  
10114 C C   . PHE   G  192 ? 0.77764 0.77764 0.77764 0.00000  0.00000  0.00000  192 PHE   C C   
10115 O O   . PHE   G  192 ? 0.64579 0.64579 0.64579 0.00000  0.00000  0.00000  192 PHE   C O   
10116 C CB  . PHE   G  192 ? 0.49511 0.49511 0.49511 0.00000  0.00000  0.00000  192 PHE   C CB  
10117 C CG  . PHE   G  192 ? 0.58959 0.58959 0.58959 0.00000  -0.00000 -0.00000 192 PHE   C CG  
10118 C CD1 . PHE   G  192 ? 0.70543 0.70543 0.70543 -0.00000 0.00000  0.00000  192 PHE   C CD1 
10119 C CD2 . PHE   G  192 ? 0.69212 0.69212 0.69212 0.00000  0.00000  0.00000  192 PHE   C CD2 
10120 C CE1 . PHE   G  192 ? 0.45964 0.45964 0.45964 0.00000  0.00000  0.00000  192 PHE   C CE1 
10121 C CE2 . PHE   G  192 ? 0.76940 0.76940 0.76940 0.00000  -0.00000 0.00000  192 PHE   C CE2 
10122 C CZ  . PHE   G  192 ? 0.55972 0.55972 0.55972 0.00000  0.00000  0.00000  192 PHE   C CZ  
10123 N N   . ASP   G  193 ? 0.72481 0.72481 0.72481 -0.00000 0.00000  0.00000  193 ASP   C N   
10124 C CA  . ASP   G  193 ? 0.47274 0.47274 0.47274 0.00000  0.00000  0.00000  193 ASP   C CA  
10125 C C   . ASP   G  193 ? 0.80829 0.80829 0.80829 0.00000  0.00000  0.00000  193 ASP   C C   
10126 O O   . ASP   G  193 ? 0.31291 0.31291 0.31291 0.00000  0.00000  0.00000  193 ASP   C O   
10127 C CB  . ASP   G  193 ? 0.63600 0.63600 0.63600 -0.00000 0.00000  0.00000  193 ASP   C CB  
10128 C CG  . ASP   G  193 ? 1.17910 1.17910 1.17910 -0.00000 0.00000  0.00000  193 ASP   C CG  
10129 O OD1 . ASP   G  193 ? 0.68157 0.68157 0.68157 0.00000  0.00000  0.00000  193 ASP   C OD1 
10130 O OD2 . ASP   G  193 ? 0.66255 0.66255 0.66255 -0.00000 -0.00000 -0.00000 193 ASP   C OD2 
10131 N N   . GLU   G  194 ? 0.40064 0.40064 0.40064 0.00000  0.00000  0.00000  194 GLU   C N   
10132 C CA  . GLU   G  194 ? 0.74224 0.74224 0.74224 0.00000  0.00000  0.00000  194 GLU   C CA  
10133 C C   . GLU   G  194 ? 0.79767 0.79767 0.79767 -0.00000 0.00000  0.00000  194 GLU   C C   
10134 O O   . GLU   G  194 ? 0.65194 0.65194 0.65194 0.00000  0.00000  0.00000  194 GLU   C O   
10135 C CB  . GLU   G  194 ? 0.63791 0.63791 0.63791 0.00000  0.00000  0.00000  194 GLU   C CB  
10136 C CG  . GLU   G  194 ? 0.45777 0.45777 0.45777 -0.00000 0.00000  0.00000  194 GLU   C CG  
10137 C CD  . GLU   G  194 ? 1.18696 1.18696 1.18696 -0.00000 0.00000  0.00000  194 GLU   C CD  
10138 O OE1 . GLU   G  194 ? 0.86540 0.86540 0.86540 -0.00000 0.00000  0.00000  194 GLU   C OE1 
10139 O OE2 . GLU   G  194 ? 0.83440 0.83440 0.83440 0.00000  0.00000  0.00000  194 GLU   C OE2 
10140 N N   . VAL   G  195 ? 0.72438 0.72438 0.72438 -0.00000 0.00000  0.00000  195 VAL   C N   
10141 C CA  . VAL   G  195 ? 0.31657 0.31657 0.31657 0.00000  0.00000  0.00000  195 VAL   C CA  
10142 C C   . VAL   G  195 ? 1.09453 1.09453 1.09453 -0.00000 -0.00000 0.00000  195 VAL   C C   
10143 O O   . VAL   G  195 ? 0.48394 0.48394 0.48394 -0.00000 0.00000  0.00000  195 VAL   C O   
10144 C CB  . VAL   G  195 ? 0.76283 0.76283 0.76283 0.00000  0.00000  0.00000  195 VAL   C CB  
10145 C CG1 . VAL   G  195 ? 0.37871 0.37871 0.37871 0.00000  0.00000  0.00000  195 VAL   C CG1 
10146 C CG2 . VAL   G  195 ? 0.44199 0.44199 0.44199 0.00000  0.00000  0.00000  195 VAL   C CG2 
10147 N N   . PHE   G  196 ? 0.38286 0.38286 0.38286 -0.00000 0.00000  0.00000  196 PHE   C N   
10148 C CA  . PHE   G  196 ? 0.78713 0.78713 0.78713 0.00000  0.00000  0.00000  196 PHE   C CA  
10149 C C   . PHE   G  196 ? 0.54010 0.54010 0.54010 0.00000  0.00000  0.00000  196 PHE   C C   
10150 O O   . PHE   G  196 ? 0.56873 0.56873 0.56873 -0.00000 0.00000  0.00000  196 PHE   C O   
10151 C CB  . PHE   G  196 ? 0.44191 0.44191 0.44191 0.00000  0.00000  0.00000  196 PHE   C CB  
10152 C CG  . PHE   G  196 ? 0.66299 0.66299 0.66299 -0.00000 0.00000  0.00000  196 PHE   C CG  
10153 C CD1 . PHE   G  196 ? 0.45661 0.45661 0.45661 -0.00000 0.00000  0.00000  196 PHE   C CD1 
10154 C CD2 . PHE   G  196 ? 0.37319 0.37319 0.37319 0.00000  0.00000  0.00000  196 PHE   C CD2 
10155 C CE1 . PHE   G  196 ? 0.50747 0.50747 0.50747 -0.00000 0.00000  0.00000  196 PHE   C CE1 
10156 C CE2 . PHE   G  196 ? 0.60350 0.60350 0.60350 0.00000  0.00000  0.00000  196 PHE   C CE2 
10157 C CZ  . PHE   G  196 ? 0.49443 0.49443 0.49443 0.00000  0.00000  0.00000  196 PHE   C CZ  
10158 N N   . LEU   G  197 ? 0.61242 0.61242 0.61242 -0.00000 0.00000  0.00000  197 LEU   C N   
10159 C CA  . LEU   G  197 ? 0.64822 0.64822 0.64822 -0.00000 0.00000  0.00000  197 LEU   C CA  
10160 C C   . LEU   G  197 ? 0.88371 0.88371 0.88371 0.00000  0.00000  0.00000  197 LEU   C C   
10161 O O   . LEU   G  197 ? 0.57214 0.57214 0.57214 -0.00000 0.00000  0.00000  197 LEU   C O   
10162 C CB  . LEU   G  197 ? 0.61697 0.61697 0.61697 0.00000  0.00000  0.00000  197 LEU   C CB  
10163 C CG  . LEU   G  197 ? 0.57513 0.57513 0.57513 -0.00000 0.00000  0.00000  197 LEU   C CG  
10164 C CD1 . LEU   G  197 ? 0.67955 0.67955 0.67955 0.00000  0.00000  0.00000  197 LEU   C CD1 
10165 C CD2 . LEU   G  197 ? 1.17293 1.17293 1.17293 0.00000  0.00000  0.00000  197 LEU   C CD2 
10166 N N   . CYS   G  198 ? 0.77740 0.77740 0.77740 0.00000  0.00000  0.00000  198 CYS   C N   
10167 C CA  . CYS   G  198 ? 0.76694 0.76694 0.76694 -0.00000 0.00000  0.00000  198 CYS   C CA  
10168 C C   . CYS   G  198 ? 0.81293 0.81293 0.81293 -0.00000 0.00000  0.00000  198 CYS   C C   
10169 O O   . CYS   G  198 ? 0.90281 0.90281 0.90281 -0.00000 0.00000  0.00000  198 CYS   C O   
10170 C CB  . CYS   G  198 ? 0.68404 0.68404 0.68404 0.00000  0.00000  0.00000  198 CYS   C CB  
10171 S SG  . CYS   G  198 ? 0.79468 0.79468 0.79468 0.00000  0.00000  0.00000  198 CYS   C SG  
10172 N N   . ASP   G  199 ? 0.69194 0.69194 0.69194 0.00000  0.00000  0.00000  199 ASP   C N   
10173 C CA  . ASP   G  199 ? 0.54596 0.54596 0.54596 -0.00000 0.00000  0.00000  199 ASP   C CA  
10174 C C   . ASP   G  199 ? 0.98438 0.98438 0.98438 0.00000  0.00000  0.00000  199 ASP   C C   
10175 O O   . ASP   G  199 ? 0.54286 0.54286 0.54286 0.00000  0.00000  0.00000  199 ASP   C O   
10176 C CB  . ASP   G  199 ? 0.56882 0.56882 0.56882 0.00000  0.00000  0.00000  199 ASP   C CB  
10177 C CG  . ASP   G  199 ? 1.85242 1.85242 1.85242 0.00000  0.00000  -0.00000 199 ASP   C CG  
10178 O OD1 . ASP   G  199 ? 0.60474 0.60474 0.60474 -0.00000 0.00000  0.00000  199 ASP   C OD1 
10179 O OD2 . ASP   G  199 ? 0.70226 0.70226 0.70226 0.00000  0.00000  0.00000  199 ASP   C OD2 
10180 N N   . LYS   G  200 ? 0.64539 0.64539 0.64539 0.00000  -0.00000 0.00000  200 LYS   C N   
10181 C CA  . LYS   G  200 ? 0.96786 0.96786 0.96786 0.00000  0.00000  0.00000  200 LYS   C CA  
10182 C C   . LYS   G  200 ? 0.92662 0.92662 0.92662 0.00000  0.00000  0.00000  200 LYS   C C   
10183 O O   . LYS   G  200 ? 0.82171 0.82171 0.82171 -0.00000 0.00000  0.00000  200 LYS   C O   
10184 C CB  . LYS   G  200 ? 0.64305 0.64305 0.64305 0.00000  0.00000  0.00000  200 LYS   C CB  
10185 C CG  . LYS   G  200 ? 0.93168 0.93168 0.93168 0.00000  0.00000  0.00000  200 LYS   C CG  
10186 C CD  . LYS   G  200 ? 1.19145 1.19145 1.19145 0.00000  0.00000  0.00000  200 LYS   C CD  
10187 C CE  . LYS   G  200 ? 0.97966 0.97966 0.97966 0.00000  0.00000  0.00000  200 LYS   C CE  
10188 N NZ  . LYS   G  200 ? 0.91102 0.91102 0.91102 0.00000  0.00000  0.00000  200 LYS   C NZ  
10189 N N   . ASN   G  201 ? 0.70186 0.70186 0.70186 0.00000  0.00000  0.00000  201 ASN   C N   
10190 C CA  . ASN   G  201 ? 0.99520 0.99520 0.99520 0.00000  0.00000  0.00000  201 ASN   C CA  
10191 C C   . ASN   G  201 ? 0.68801 0.68801 0.68801 0.00000  0.00000  0.00000  201 ASN   C C   
10192 O O   . ASN   G  201 ? 1.09381 1.09381 1.09381 0.00000  0.00000  -0.00000 201 ASN   C O   
10193 C CB  . ASN   G  201 ? 0.66588 0.66588 0.66588 0.00000  0.00000  0.00000  201 ASN   C CB  
10194 C CG  . ASN   G  201 ? 1.14037 1.14037 1.14037 0.00000  0.00000  0.00000  201 ASN   C CG  
10195 O OD1 . ASN   G  201 ? 0.54805 0.54805 0.54805 -0.00000 0.00000  0.00000  201 ASN   C OD1 
10196 N ND2 . ASN   G  201 ? 0.73653 0.73653 0.73653 0.00000  0.00000  0.00000  201 ASN   C ND2 
10197 N N   . ALA   G  202 ? 1.28672 1.28672 1.28672 0.00000  0.00000  -0.00000 202 ALA   C N   
10198 C CA  . ALA   G  202 ? 0.68507 0.68507 0.68507 0.00000  -0.00000 0.00000  202 ALA   C CA  
10199 C C   . ALA   G  202 ? 0.59934 0.59934 0.59934 0.00000  0.00000  0.00000  202 ALA   C C   
10200 O O   . ALA   G  202 ? 0.74820 0.74820 0.74820 0.00000  0.00000  0.00000  202 ALA   C O   
10201 C CB  . ALA   G  202 ? 0.39843 0.39843 0.39843 0.00000  0.00000  0.00000  202 ALA   C CB  
10202 N N   . PRO   G  203 ? 1.00256 1.00256 1.00256 0.00000  0.00000  0.00000  203 PRO   C N   
10203 C CA  . PRO   G  203 ? 0.93696 0.93696 0.93696 0.00000  0.00000  0.00000  203 PRO   C CA  
10204 C C   . PRO   G  203 ? 0.80809 0.80809 0.80809 0.00000  0.00000  -0.00000 203 PRO   C C   
10205 O O   . PRO   G  203 ? 0.55804 0.55804 0.55804 0.00000  0.00000  0.00000  203 PRO   C O   
10206 C CB  . PRO   G  203 ? 0.64924 0.64924 0.64924 -0.00000 0.00000  0.00000  203 PRO   C CB  
10207 C CG  . PRO   G  203 ? 0.53157 0.53157 0.53157 0.00000  0.00000  0.00000  203 PRO   C CG  
10208 C CD  . PRO   G  203 ? 0.38127 0.38127 0.38127 0.00000  0.00000  0.00000  203 PRO   C CD  
10209 N N   . TYR   G  204 ? 0.62966 0.62966 0.62966 0.00000  0.00000  0.00000  204 TYR   C N   
10210 C CA  . TYR   G  204 ? 0.76986 0.76986 0.76986 0.00000  0.00000  0.00000  204 TYR   C CA  
10211 C C   . TYR   G  204 ? 0.69018 0.69018 0.69018 -0.00000 0.00000  0.00000  204 TYR   C C   
10212 O O   . TYR   G  204 ? 0.74532 0.74532 0.74532 0.00000  0.00000  0.00000  204 TYR   C O   
10213 C CB  . TYR   G  204 ? 0.61036 0.61036 0.61036 0.00000  0.00000  0.00000  204 TYR   C CB  
10214 C CG  . TYR   G  204 ? 0.66451 0.66451 0.66451 -0.00000 -0.00000 0.00000  204 TYR   C CG  
10215 C CD1 . TYR   G  204 ? 0.59816 0.59816 0.59816 -0.00000 -0.00000 0.00000  204 TYR   C CD1 
10216 C CD2 . TYR   G  204 ? 0.54988 0.54988 0.54988 0.00000  0.00000  0.00000  204 TYR   C CD2 
10217 C CE1 . TYR   G  204 ? 0.37925 0.37925 0.37925 0.00000  0.00000  0.00000  204 TYR   C CE1 
10218 C CE2 . TYR   G  204 ? 0.51242 0.51242 0.51242 -0.00000 0.00000  0.00000  204 TYR   C CE2 
10219 C CZ  . TYR   G  204 ? 0.67977 0.67977 0.67977 -0.00000 0.00000  0.00000  204 TYR   C CZ  
10220 O OH  . TYR   G  204 ? 0.70523 0.70523 0.70523 0.00000  0.00000  0.00000  204 TYR   C OH  
10221 N N   . TYR   G  205 ? 0.51636 0.51636 0.51636 0.00000  0.00000  0.00000  205 TYR   C N   
10222 C CA  . TYR   G  205 ? 0.49053 0.49053 0.49053 0.00000  0.00000  0.00000  205 TYR   C CA  
10223 C C   . TYR   G  205 ? 0.58454 0.58454 0.58454 -0.00000 0.00000  0.00000  205 TYR   C C   
10224 O O   . TYR   G  205 ? 0.55900 0.55900 0.55900 0.00000  0.00000  0.00000  205 TYR   C O   
10225 C CB  . TYR   G  205 ? 0.58068 0.58068 0.58068 0.00000  0.00000  0.00000  205 TYR   C CB  
10226 C CG  . TYR   G  205 ? 0.75428 0.75428 0.75428 0.00000  0.00000  0.00000  205 TYR   C CG  
10227 C CD1 . TYR   G  205 ? 0.65614 0.65614 0.65614 0.00000  -0.00000 0.00000  205 TYR   C CD1 
10228 C CD2 . TYR   G  205 ? 0.59601 0.59601 0.59601 0.00000  0.00000  -0.00000 205 TYR   C CD2 
10229 C CE1 . TYR   G  205 ? 0.46461 0.46461 0.46461 0.00000  0.00000  0.00000  205 TYR   C CE1 
10230 C CE2 . TYR   G  205 ? 0.76858 0.76858 0.76858 -0.00000 0.00000  0.00000  205 TYR   C CE2 
10231 C CZ  . TYR   G  205 ? 1.02054 1.02054 1.02054 -0.00000 0.00000  0.00000  205 TYR   C CZ  
10232 O OH  . TYR   G  205 ? 0.64803 0.64803 0.64803 0.00000  0.00000  0.00000  205 TYR   C OH  
10233 N N   . GLY   G  206 ? 0.52984 0.52984 0.52984 0.00000  0.00000  0.00000  206 GLY   C N   
10234 C CA  . GLY   G  206 ? 0.51574 0.51574 0.51574 0.00000  -0.00000 0.00000  206 GLY   C CA  
10235 C C   . GLY   G  206 ? 0.69038 0.69038 0.69038 0.00000  0.00000  0.00000  206 GLY   C C   
10236 O O   . GLY   G  206 ? 0.58927 0.58927 0.58927 -0.00000 0.00000  0.00000  206 GLY   C O   
10237 N N   . PHE   G  207 ? 0.53744 0.53744 0.53744 0.00000  0.00000  0.00000  207 PHE   C N   
10238 C CA  . PHE   G  207 ? 0.69017 0.69017 0.69017 0.00000  0.00000  0.00000  207 PHE   C CA  
10239 C C   . PHE   G  207 ? 0.63272 0.63272 0.63272 0.00000  0.00000  0.00000  207 PHE   C C   
10240 O O   . PHE   G  207 ? 0.75990 0.75990 0.75990 0.00000  0.00000  0.00000  207 PHE   C O   
10241 C CB  . PHE   G  207 ? 0.52978 0.52978 0.52978 -0.00000 0.00000  0.00000  207 PHE   C CB  
10242 C CG  . PHE   G  207 ? 0.72796 0.72796 0.72796 0.00000  0.00000  0.00000  207 PHE   C CG  
10243 C CD1 . PHE   G  207 ? 0.39585 0.39585 0.39585 0.00000  0.00000  0.00000  207 PHE   C CD1 
10244 C CD2 . PHE   G  207 ? 0.45128 0.45128 0.45128 -0.00000 0.00000  0.00000  207 PHE   C CD2 
10245 C CE1 . PHE   G  207 ? 0.65304 0.65304 0.65304 0.00000  0.00000  0.00000  207 PHE   C CE1 
10246 C CE2 . PHE   G  207 ? 0.49758 0.49758 0.49758 0.00000  0.00000  0.00000  207 PHE   C CE2 
10247 C CZ  . PHE   G  207 ? 0.71234 0.71234 0.71234 -0.00000 0.00000  0.00000  207 PHE   C CZ  
10248 N N   . ASN   G  208 ? 0.56310 0.56310 0.56310 0.00000  0.00000  0.00000  208 ASN   C N   
10249 C CA  . ASN   G  208 ? 0.84824 0.84824 0.84824 -0.00000 0.00000  0.00000  208 ASN   C CA  
10250 C C   . ASN   G  208 ? 0.46353 0.46353 0.46353 0.00000  0.00000  0.00000  208 ASN   C C   
10251 O O   . ASN   G  208 ? 1.20031 1.20031 1.20031 0.00000  0.00000  0.00000  208 ASN   C O   
10252 C CB  . ASN   G  208 ? 0.46923 0.46923 0.46923 0.00000  0.00000  0.00000  208 ASN   C CB  
10253 C CG  . ASN   G  208 ? 1.18442 1.18442 1.18442 0.00000  0.00000  0.00000  208 ASN   C CG  
10254 O OD1 . ASN   G  208 ? 1.88162 1.88162 1.88162 -0.00000 0.00000  0.00000  208 ASN   C OD1 
10255 N ND2 . ASN   G  208 ? 0.89281 0.89281 0.89281 0.00000  0.00000  0.00000  208 ASN   C ND2 
10256 N N   . SER   G  209 ? 0.67724 0.67724 0.67724 0.00000  0.00000  0.00000  209 SER   C N   
10257 C CA  . SER   G  209 ? 0.46781 0.46781 0.46781 0.00000  0.00000  -0.00000 209 SER   C CA  
10258 C C   . SER   G  209 ? 0.74831 0.74831 0.74831 0.00000  0.00000  0.00000  209 SER   C C   
10259 O O   . SER   G  209 ? 0.43463 0.43463 0.43463 0.00000  0.00000  0.00000  209 SER   C O   
10260 C CB  . SER   G  209 ? 0.60704 0.60704 0.60704 -0.00000 0.00000  0.00000  209 SER   C CB  
10261 O OG  . SER   G  209 ? 0.34517 0.34517 0.34517 0.00000  -0.00000 0.00000  209 SER   C OG  
10262 N N   . TYR   G  210 ? 0.57042 0.57042 0.57042 0.00000  0.00000  0.00000  210 TYR   C N   
10263 C CA  . TYR   G  210 ? 0.41988 0.41988 0.41988 0.00000  0.00000  0.00000  210 TYR   C CA  
10264 C C   . TYR   G  210 ? 0.58463 0.58463 0.58463 0.00000  0.00000  0.00000  210 TYR   C C   
10265 O O   . TYR   G  210 ? 0.49529 0.49529 0.49529 0.00000  0.00000  0.00000  210 TYR   C O   
10266 C CB  . TYR   G  210 ? 0.28569 0.28569 0.28569 0.00000  0.00000  0.00000  210 TYR   C CB  
10267 C CG  . TYR   G  210 ? 0.70456 0.70456 0.70456 0.00000  0.00000  0.00000  210 TYR   C CG  
10268 C CD1 . TYR   G  210 ? 0.41355 0.41355 0.41355 0.00000  0.00000  0.00000  210 TYR   C CD1 
10269 C CD2 . TYR   G  210 ? 0.60877 0.60877 0.60877 0.00000  0.00000  0.00000  210 TYR   C CD2 
10270 C CE1 . TYR   G  210 ? 0.45943 0.45943 0.45943 0.00000  0.00000  0.00000  210 TYR   C CE1 
10271 C CE2 . TYR   G  210 ? 0.63118 0.63118 0.63118 0.00000  0.00000  0.00000  210 TYR   C CE2 
10272 C CZ  . TYR   G  210 ? 0.74511 0.74511 0.74511 -0.00000 0.00000  0.00000  210 TYR   C CZ  
10273 O OH  . TYR   G  210 ? 0.51430 0.51430 0.51430 0.00000  0.00000  0.00000  210 TYR   C OH  
10274 N N   . ASP   G  211 ? 0.48519 0.48519 0.48519 -0.00000 0.00000  0.00000  211 ASP   C N   
10275 C CA  . ASP   G  211 ? 0.41837 0.41837 0.41837 -0.00000 0.00000  0.00000  211 ASP   C CA  
10276 C C   . ASP   G  211 ? 0.68926 0.68926 0.68926 -0.00000 0.00000  0.00000  211 ASP   C C   
10277 O O   . ASP   G  211 ? 0.44713 0.44713 0.44713 0.00000  0.00000  0.00000  211 ASP   C O   
10278 C CB  . ASP   G  211 ? 0.45813 0.45813 0.45813 0.00000  0.00000  0.00000  211 ASP   C CB  
10279 C CG  . ASP   G  211 ? 0.46501 0.46501 0.46501 0.00000  0.00000  0.00000  211 ASP   C CG  
10280 O OD1 . ASP   G  211 ? 0.52519 0.52519 0.52519 0.00000  0.00000  0.00000  211 ASP   C OD1 
10281 O OD2 . ASP   G  211 ? 0.75209 0.75209 0.75209 -0.00000 0.00000  -0.00000 211 ASP   C OD2 
10282 N N   . ASP   G  212 ? 0.43590 0.43590 0.43590 0.00000  0.00000  0.00000  212 ASP   C N   
10283 C CA  . ASP   G  212 ? 0.55644 0.55644 0.55644 0.00000  0.00000  0.00000  212 ASP   C CA  
10284 C C   . ASP   G  212 ? 0.45846 0.45846 0.45846 -0.00000 0.00000  0.00000  212 ASP   C C   
10285 O O   . ASP   G  212 ? 0.46716 0.46716 0.46716 -0.00000 0.00000  0.00000  212 ASP   C O   
10286 C CB  . ASP   G  212 ? 0.57517 0.57517 0.57517 0.00000  0.00000  0.00000  212 ASP   C CB  
10287 C CG  . ASP   G  212 ? 0.67802 0.67802 0.67802 0.00000  -0.00000 0.00000  212 ASP   C CG  
10288 O OD1 . ASP   G  212 ? 0.86800 0.86800 0.86800 0.00000  0.00000  -0.00000 212 ASP   C OD1 
10289 O OD2 . ASP   G  212 ? 0.68907 0.68907 0.68907 0.00000  0.00000  0.00000  212 ASP   C OD2 
10290 N N   . PHE   G  213 ? 0.37790 0.37790 0.37790 -0.00000 0.00000  0.00000  213 PHE   C N   
10291 C CA  . PHE   G  213 ? 0.34333 0.34333 0.34333 -0.00000 0.00000  -0.00000 213 PHE   C CA  
10292 C C   . PHE   G  213 ? 0.81079 0.81079 0.81079 -0.00000 0.00000  -0.00000 213 PHE   C C   
10293 O O   . PHE   G  213 ? 0.48779 0.48779 0.48779 -0.00000 0.00000  0.00000  213 PHE   C O   
10294 C CB  . PHE   G  213 ? 0.42791 0.42791 0.42791 -0.00000 0.00000  0.00000  213 PHE   C CB  
10295 C CG  . PHE   G  213 ? 0.58875 0.58875 0.58875 0.00000  -0.00000 0.00000  213 PHE   C CG  
10296 C CD1 . PHE   G  213 ? 0.63285 0.63285 0.63285 -0.00000 0.00000  0.00000  213 PHE   C CD1 
10297 C CD2 . PHE   G  213 ? 0.43938 0.43938 0.43938 0.00000  0.00000  0.00000  213 PHE   C CD2 
10298 C CE1 . PHE   G  213 ? 0.75285 0.75285 0.75285 0.00000  0.00000  0.00000  213 PHE   C CE1 
10299 C CE2 . PHE   G  213 ? 0.79010 0.79010 0.79010 -0.00000 0.00000  0.00000  213 PHE   C CE2 
10300 C CZ  . PHE   G  213 ? 0.65652 0.65652 0.65652 -0.00000 0.00000  0.00000  213 PHE   C CZ  
10301 N N   . PHE   G  214 ? 0.43435 0.43435 0.43435 0.00000  0.00000  0.00000  214 PHE   C N   
10302 C CA  . PHE   G  214 ? 0.41273 0.41273 0.41273 -0.00000 0.00000  0.00000  214 PHE   C CA  
10303 C C   . PHE   G  214 ? 0.39760 0.39760 0.39760 -0.00000 0.00000  0.00000  214 PHE   C C   
10304 O O   . PHE   G  214 ? 0.74745 0.74745 0.74745 0.00000  0.00000  0.00000  214 PHE   C O   
10305 C CB  . PHE   G  214 ? 0.52334 0.52334 0.52334 0.00000  0.00000  0.00000  214 PHE   C CB  
10306 C CG  . PHE   G  214 ? 0.50068 0.50068 0.50068 0.00000  0.00000  0.00000  214 PHE   C CG  
10307 C CD1 . PHE   G  214 ? 0.48218 0.48218 0.48218 -0.00000 0.00000  0.00000  214 PHE   C CD1 
10308 C CD2 . PHE   G  214 ? 0.59482 0.59482 0.59482 0.00000  0.00000  -0.00000 214 PHE   C CD2 
10309 C CE1 . PHE   G  214 ? 0.43715 0.43715 0.43715 0.00000  0.00000  0.00000  214 PHE   C CE1 
10310 C CE2 . PHE   G  214 ? 0.58711 0.58711 0.58711 -0.00000 0.00000  0.00000  214 PHE   C CE2 
10311 C CZ  . PHE   G  214 ? 0.51011 0.51011 0.51011 0.00000  0.00000  0.00000  214 PHE   C CZ  
10312 N N   . ASN   G  215 ? 0.36343 0.36343 0.36343 0.00000  0.00000  0.00000  215 ASN   C N   
10313 C CA  . ASN   G  215 ? 0.46043 0.46043 0.46043 -0.00000 0.00000  0.00000  215 ASN   C CA  
10314 C C   . ASN   G  215 ? 0.58433 0.58433 0.58433 0.00000  0.00000  0.00000  215 ASN   C C   
10315 O O   . ASN   G  215 ? 0.50509 0.50509 0.50509 0.00000  0.00000  0.00000  215 ASN   C O   
10316 C CB  . ASN   G  215 ? 0.45849 0.45849 0.45849 0.00000  0.00000  0.00000  215 ASN   C CB  
10317 C CG  . ASN   G  215 ? 0.75134 0.75134 0.75134 0.00000  0.00000  0.00000  215 ASN   C CG  
10318 O OD1 . ASN   G  215 ? 0.48107 0.48107 0.48107 0.00000  0.00000  0.00000  215 ASN   C OD1 
10319 N ND2 . ASN   G  215 ? 0.43963 0.43963 0.43963 0.00000  0.00000  0.00000  215 ASN   C ND2 
10320 N N   . ARG   G  216 ? 0.31518 0.31518 0.31518 -0.00000 0.00000  0.00000  216 ARG   C N   
10321 C CA  . ARG   G  216 ? 0.42765 0.42765 0.42765 -0.00000 0.00000  0.00000  216 ARG   C CA  
10322 C C   . ARG   G  216 ? 0.71950 0.71950 0.71950 -0.00000 0.00000  0.00000  216 ARG   C C   
10323 O O   . ARG   G  216 ? 0.41787 0.41787 0.41787 -0.00000 0.00000  0.00000  216 ARG   C O   
10324 C CB  . ARG   G  216 ? 0.38057 0.38057 0.38057 0.00000  0.00000  0.00000  216 ARG   C CB  
10325 C CG  . ARG   G  216 ? 0.37160 0.37160 0.37160 -0.00000 0.00000  0.00000  216 ARG   C CG  
10326 C CD  . ARG   G  216 ? 0.50223 0.50223 0.50223 -0.00000 0.00000  0.00000  216 ARG   C CD  
10327 N NE  . ARG   G  216 ? 0.36215 0.36215 0.36215 0.00000  0.00000  0.00000  216 ARG   C NE  
10328 C CZ  . ARG   G  216 ? 0.67599 0.67599 0.67599 0.00000  0.00000  -0.00000 216 ARG   C CZ  
10329 N NH1 . ARG   G  216 ? 0.40765 0.40765 0.40765 -0.00000 0.00000  0.00000  216 ARG   C NH1 
10330 N NH2 . ARG   G  216 ? 0.46445 0.46445 0.46445 0.00000  0.00000  0.00000  216 ARG   C NH2 
10331 N N   . ARG   G  217 ? 0.40542 0.40542 0.40542 -0.00000 0.00000  0.00000  217 ARG   C N   
10332 C CA  . ARG   G  217 ? 0.60519 0.60519 0.60519 -0.00000 0.00000  0.00000  217 ARG   C CA  
10333 C C   . ARG   G  217 ? 0.42518 0.42518 0.42518 -0.00000 0.00000  0.00000  217 ARG   C C   
10334 O O   . ARG   G  217 ? 0.64055 0.64055 0.64055 0.00000  0.00000  0.00000  217 ARG   C O   
10335 C CB  . ARG   G  217 ? 0.48033 0.48033 0.48033 -0.00000 0.00000  0.00000  217 ARG   C CB  
10336 C CG  . ARG   G  217 ? 0.23363 0.23363 0.23363 0.00000  0.00000  0.00000  217 ARG   C CG  
10337 C CD  . ARG   G  217 ? 0.43713 0.43713 0.43713 0.00000  0.00000  0.00000  217 ARG   C CD  
10338 N NE  . ARG   G  217 ? 1.17126 1.17126 1.17126 -0.00000 0.00000  0.00000  217 ARG   C NE  
10339 C CZ  . ARG   G  217 ? 1.50272 1.50272 1.50272 0.00000  0.00000  0.00000  217 ARG   C CZ  
10340 N NH1 . ARG   G  217 ? 1.18654 1.18654 1.18654 0.00000  0.00000  0.00000  217 ARG   C NH1 
10341 N NH2 . ARG   G  217 ? 1.42561 1.42561 1.42561 0.00000  0.00000  0.00000  217 ARG   C NH2 
10342 N N   . PHE   G  218 ? 0.54226 0.54226 0.54226 0.00000  0.00000  -0.00000 218 PHE   C N   
10343 C CA  . PHE   G  218 ? 0.40126 0.40126 0.40126 0.00000  0.00000  0.00000  218 PHE   C CA  
10344 C C   . PHE   G  218 ? 0.78692 0.78692 0.78692 -0.00000 0.00000  0.00000  218 PHE   C C   
10345 O O   . PHE   G  218 ? 0.42927 0.42927 0.42927 0.00000  0.00000  0.00000  218 PHE   C O   
10346 C CB  . PHE   G  218 ? 0.28539 0.28539 0.28539 0.00000  0.00000  0.00000  218 PHE   C CB  
10347 C CG  . PHE   G  218 ? 0.53433 0.53433 0.53433 -0.00000 0.00000  0.00000  218 PHE   C CG  
10348 C CD1 . PHE   G  218 ? 0.30651 0.30651 0.30651 0.00000  0.00000  0.00000  218 PHE   C CD1 
10349 C CD2 . PHE   G  218 ? 0.41620 0.41620 0.41620 0.00000  0.00000  -0.00000 218 PHE   C CD2 
10350 C CE1 . PHE   G  218 ? 0.62631 0.62631 0.62631 0.00000  0.00000  0.00000  218 PHE   C CE1 
10351 C CE2 . PHE   G  218 ? 0.40692 0.40692 0.40692 0.00000  0.00000  0.00000  218 PHE   C CE2 
10352 C CZ  . PHE   G  218 ? 0.32150 0.32150 0.32150 0.00000  0.00000  0.00000  218 PHE   C CZ  
10353 N N   . ARG   G  219 ? 0.58751 0.58751 0.58751 0.00000  0.00000  0.00000  219 ARG   C N   
10354 C CA  . ARG   G  219 ? 0.64237 0.64237 0.64237 0.00000  0.00000  0.00000  219 ARG   C CA  
10355 C C   . ARG   G  219 ? 0.60360 0.60360 0.60360 0.00000  0.00000  0.00000  219 ARG   C C   
10356 O O   . ARG   G  219 ? 0.58506 0.58506 0.58506 0.00000  0.00000  0.00000  219 ARG   C O   
10357 C CB  . ARG   G  219 ? 0.55102 0.55102 0.55102 0.00000  0.00000  0.00000  219 ARG   C CB  
10358 C CG  . ARG   G  219 ? 0.75923 0.75923 0.75923 0.00000  0.00000  0.00000  219 ARG   C CG  
10359 C CD  . ARG   G  219 ? 0.63136 0.63136 0.63136 -0.00000 0.00000  0.00000  219 ARG   C CD  
10360 N NE  . ARG   G  219 ? 0.45566 0.45566 0.45566 0.00000  0.00000  0.00000  219 ARG   C NE  
10361 C CZ  . ARG   G  219 ? 1.31571 1.31571 1.31571 -0.00000 0.00000  0.00000  219 ARG   C CZ  
10362 N NH1 . ARG   G  219 ? 0.45888 0.45888 0.45888 0.00000  0.00000  0.00000  219 ARG   C NH1 
10363 N NH2 . ARG   G  219 ? 0.35522 0.35522 0.35522 -0.00000 0.00000  0.00000  219 ARG   C NH2 
10364 N N   . ASN   G  220 ? 0.55004 0.55004 0.55004 0.00000  0.00000  0.00000  220 ASN   C N   
10365 C CA  . ASN   G  220 ? 0.62662 0.62662 0.62662 -0.00000 0.00000  0.00000  220 ASN   C CA  
10366 C C   . ASN   G  220 ? 0.58721 0.58721 0.58721 0.00000  0.00000  0.00000  220 ASN   C C   
10367 O O   . ASN   G  220 ? 0.65613 0.65613 0.65613 0.00000  0.00000  0.00000  220 ASN   C O   
10368 C CB  . ASN   G  220 ? 0.72682 0.72682 0.72682 0.00000  0.00000  0.00000  220 ASN   C CB  
10369 C CG  . ASN   G  220 ? 1.04703 1.04703 1.04703 -0.00000 -0.00000 0.00000  220 ASN   C CG  
10370 O OD1 . ASN   G  220 ? 0.73355 0.73355 0.73355 0.00000  -0.00000 0.00000  220 ASN   C OD1 
10371 N ND2 . ASN   G  220 ? 0.74982 0.74982 0.74982 -0.00000 0.00000  0.00000  220 ASN   C ND2 
10372 N N   . ARG   G  221 ? 0.56098 0.56098 0.56098 0.00000  0.00000  0.00000  221 ARG   C N   
10373 C CA  . ARG   G  221 ? 0.60330 0.60330 0.60330 0.00000  0.00000  0.00000  221 ARG   C CA  
10374 C C   . ARG   G  221 ? 0.71337 0.71337 0.71337 -0.00000 0.00000  0.00000  221 ARG   C C   
10375 O O   . ARG   G  221 ? 0.58587 0.58587 0.58587 -0.00000 0.00000  0.00000  221 ARG   C O   
10376 C CB  . ARG   G  221 ? 0.44469 0.44469 0.44469 -0.00000 0.00000  0.00000  221 ARG   C CB  
10377 C CG  . ARG   G  221 ? 0.45133 0.45133 0.45133 -0.00000 0.00000  0.00000  221 ARG   C CG  
10378 C CD  . ARG   G  221 ? 0.59951 0.59951 0.59951 0.00000  0.00000  0.00000  221 ARG   C CD  
10379 N NE  . ARG   G  221 ? 0.53657 0.53657 0.53657 0.00000  0.00000  0.00000  221 ARG   C NE  
10380 C CZ  . ARG   G  221 ? 0.68258 0.68258 0.68258 -0.00000 0.00000  0.00000  221 ARG   C CZ  
10381 N NH1 . ARG   G  221 ? 0.61130 0.61130 0.61130 0.00000  0.00000  0.00000  221 ARG   C NH1 
10382 N NH2 . ARG   G  221 ? 0.49375 0.49375 0.49375 0.00000  0.00000  0.00000  221 ARG   C NH2 
10383 N N   . ASP   G  222 ? 0.46663 0.46663 0.46663 0.00000  0.00000  0.00000  222 ASP   C N   
10384 C CA  . ASP   G  222 ? 0.68172 0.68172 0.68172 -0.00000 0.00000  0.00000  222 ASP   C CA  
10385 C C   . ASP   G  222 ? 0.71625 0.71625 0.71625 0.00000  0.00000  -0.00000 222 ASP   C C   
10386 O O   . ASP   G  222 ? 0.54935 0.54935 0.54935 -0.00000 0.00000  0.00000  222 ASP   C O   
10387 C CB  . ASP   G  222 ? 0.39704 0.39704 0.39704 0.00000  0.00000  0.00000  222 ASP   C CB  
10388 C CG  . ASP   G  222 ? 0.63758 0.63758 0.63758 0.00000  0.00000  0.00000  222 ASP   C CG  
10389 O OD1 . ASP   G  222 ? 0.72579 0.72579 0.72579 0.00000  0.00000  0.00000  222 ASP   C OD1 
10390 O OD2 . ASP   G  222 ? 0.84147 0.84147 0.84147 0.00000  0.00000  0.00000  222 ASP   C OD2 
10391 N N   . ILE   G  223 ? 0.37444 0.37444 0.37444 0.00000  0.00000  0.00000  223 ILE   C N   
10392 C CA  . ILE   G  223 ? 0.49547 0.49547 0.49547 0.00000  0.00000  0.00000  223 ILE   C CA  
10393 C C   . ILE   G  223 ? 0.63743 0.63743 0.63743 -0.00000 0.00000  0.00000  223 ILE   C C   
10394 O O   . ILE   G  223 ? 0.66944 0.66944 0.66944 -0.00000 0.00000  0.00000  223 ILE   C O   
10395 C CB  . ILE   G  223 ? 0.65542 0.65542 0.65542 0.00000  -0.00000 0.00000  223 ILE   C CB  
10396 C CG1 . ILE   G  223 ? 0.41500 0.41500 0.41500 0.00000  0.00000  0.00000  223 ILE   C CG1 
10397 C CG2 . ILE   G  223 ? 0.26033 0.26033 0.26033 0.00000  0.00000  0.00000  223 ILE   C CG2 
10398 C CD1 . ILE   G  223 ? 0.45335 0.45335 0.45335 0.00000  0.00000  0.00000  223 ILE   C CD1 
10399 N N   . ASP   G  224 ? 0.55380 0.55380 0.55380 -0.00000 0.00000  0.00000  224 ASP   C N   
10400 C CA  . ASP   G  224 ? 0.56780 0.56780 0.56780 0.00000  0.00000  0.00000  224 ASP   C CA  
10401 C C   . ASP   G  224 ? 0.57891 0.57891 0.57891 0.00000  0.00000  0.00000  224 ASP   C C   
10402 O O   . ASP   G  224 ? 0.52308 0.52308 0.52308 0.00000  0.00000  0.00000  224 ASP   C O   
10403 C CB  . ASP   G  224 ? 0.51601 0.51601 0.51601 0.00000  0.00000  0.00000  224 ASP   C CB  
10404 C CG  . ASP   G  224 ? 0.68532 0.68532 0.68532 0.00000  0.00000  0.00000  224 ASP   C CG  
10405 O OD1 . ASP   G  224 ? 0.72497 0.72497 0.72497 -0.00000 0.00000  0.00000  224 ASP   C OD1 
10406 O OD2 . ASP   G  224 ? 0.68091 0.68091 0.68091 0.00000  -0.00000 0.00000  224 ASP   C OD2 
10407 N N   . ARG   G  225 ? 0.52702 0.52702 0.52702 0.00000  0.00000  -0.00000 225 ARG   C N   
10408 C CA  . ARG   G  225 ? 0.40891 0.40891 0.40891 -0.00000 0.00000  0.00000  225 ARG   C CA  
10409 C C   . ARG   G  225 ? 0.60013 0.60013 0.60013 0.00000  -0.00000 0.00000  225 ARG   C C   
10410 O O   . ARG   G  225 ? 0.52461 0.52461 0.52461 0.00000  0.00000  0.00000  225 ARG   C O   
10411 C CB  . ARG   G  225 ? 0.42223 0.42223 0.42223 0.00000  0.00000  0.00000  225 ARG   C CB  
10412 C CG  . ARG   G  225 ? 0.24515 0.24515 0.24515 0.00000  0.00000  0.00000  225 ARG   C CG  
10413 C CD  . ARG   G  225 ? 0.13270 0.13270 0.13270 0.00000  0.00000  0.00000  225 ARG   C CD  
10414 N NE  . ARG   G  225 ? 0.66995 0.66995 0.66995 -0.00000 0.00000  0.00000  225 ARG   C NE  
10415 C CZ  . ARG   G  225 ? 0.41863 0.41863 0.41863 -0.00000 0.00000  0.00000  225 ARG   C CZ  
10416 N NH1 . ARG   G  225 ? 0.74718 0.74718 0.74718 0.00000  0.00000  0.00000  225 ARG   C NH1 
10417 N NH2 . ARG   G  225 ? 0.80636 0.80636 0.80636 0.00000  0.00000  0.00000  225 ARG   C NH2 
10418 N N   . PRO   G  226 ? 0.57916 0.57916 0.57916 0.00000  0.00000  0.00000  226 PRO   C N   
10419 C CA  . PRO   G  226 ? 0.34869 0.34869 0.34869 0.00000  0.00000  0.00000  226 PRO   C CA  
10420 C C   . PRO   G  226 ? 0.65944 0.65944 0.65944 0.00000  0.00000  0.00000  226 PRO   C C   
10421 O O   . PRO   G  226 ? 0.44707 0.44707 0.44707 0.00000  0.00000  0.00000  226 PRO   C O   
10422 C CB  . PRO   G  226 ? 0.33748 0.33748 0.33748 -0.00000 0.00000  0.00000  226 PRO   C CB  
10423 C CG  . PRO   G  226 ? 0.32199 0.32199 0.32199 -0.00000 0.00000  0.00000  226 PRO   C CG  
10424 C CD  . PRO   G  226 ? 0.36255 0.36255 0.36255 -0.00000 0.00000  0.00000  226 PRO   C CD  
10425 N N   . VAL   G  227 ? 0.38406 0.38406 0.38406 -0.00000 0.00000  0.00000  227 VAL   C N   
10426 C CA  . VAL   G  227 ? 0.34637 0.34637 0.34637 0.00000  -0.00000 0.00000  227 VAL   C CA  
10427 C C   . VAL   G  227 ? 0.50388 0.50388 0.50388 0.00000  0.00000  0.00000  227 VAL   C C   
10428 O O   . VAL   G  227 ? 0.51642 0.51642 0.51642 -0.00000 0.00000  0.00000  227 VAL   C O   
10429 C CB  . VAL   G  227 ? 0.38654 0.38654 0.38654 -0.00000 0.00000  0.00000  227 VAL   C CB  
10430 C CG1 . VAL   G  227 ? 0.40122 0.40122 0.40122 0.00000  0.00000  0.00000  227 VAL   C CG1 
10431 C CG2 . VAL   G  227 ? 0.32605 0.32605 0.32605 0.00000  0.00000  0.00000  227 VAL   C CG2 
10432 N N   . VAL   G  228 ? 0.32704 0.32704 0.32704 0.00000  0.00000  0.00000  228 VAL   C N   
10433 C CA  . VAL   G  228 ? 0.16989 0.16989 0.16989 0.00000  0.00000  0.00000  228 VAL   C CA  
10434 C C   . VAL   G  228 ? 0.68011 0.68011 0.68011 0.00000  0.00000  0.00000  228 VAL   C C   
10435 O O   . VAL   G  228 ? 0.30359 0.30359 0.30359 0.00000  0.00000  0.00000  228 VAL   C O   
10436 C CB  . VAL   G  228 ? 0.40313 0.40313 0.40313 0.00000  0.00000  -0.00000 228 VAL   C CB  
10437 C CG1 . VAL   G  228 ? 0.23082 0.23082 0.23082 0.00000  0.00000  0.00000  228 VAL   C CG1 
10438 C CG2 . VAL   G  228 ? 0.16261 0.16261 0.16261 0.00000  0.00000  0.00000  228 VAL   C CG2 
10439 N N   . GLY   G  229 ? 0.44805 0.44805 0.44805 0.00000  0.00000  0.00000  229 GLY   C N   
10440 C CA  . GLY   G  229 ? 0.24422 0.24422 0.24422 0.00000  0.00000  0.00000  229 GLY   C CA  
10441 C C   . GLY   G  229 ? 0.33308 0.33308 0.33308 -0.00000 0.00000  0.00000  229 GLY   C C   
10442 O O   . GLY   G  229 ? 0.52561 0.52561 0.52561 0.00000  -0.00000 0.00000  229 GLY   C O   
10443 N N   . GLY   G  230 ? 0.56895 0.56895 0.56895 0.00000  0.00000  0.00000  230 GLY   C N   
10444 C CA  . GLY   G  230 ? 0.20234 0.20234 0.20234 0.00000  0.00000  0.00000  230 GLY   C CA  
10445 C C   . GLY   G  230 ? 0.80464 0.80464 0.80464 -0.00000 0.00000  0.00000  230 GLY   C C   
10446 O O   . GLY   G  230 ? 0.42478 0.42478 0.42478 -0.00000 0.00000  0.00000  230 GLY   C O   
10447 N N   . VAL   G  231 ? 0.42595 0.42595 0.42595 0.00000  0.00000  0.00000  231 VAL   C N   
10448 C CA  . VAL   G  231 ? 0.93692 0.93692 0.93692 -0.00000 0.00000  0.00000  231 VAL   C CA  
10449 C C   . VAL   G  231 ? 0.42859 0.42859 0.42859 0.00000  0.00000  0.00000  231 VAL   C C   
10450 O O   . VAL   G  231 ? 0.87330 0.87330 0.87330 -0.00000 0.00000  0.00000  231 VAL   C O   
10451 C CB  . VAL   G  231 ? 0.33485 0.33485 0.33485 -0.00000 0.00000  0.00000  231 VAL   C CB  
10452 C CG1 . VAL   G  231 ? 1.02899 1.02899 1.02899 0.00000  0.00000  0.00000  231 VAL   C CG1 
10453 C CG2 . VAL   G  231 ? 0.68131 0.68131 0.68131 0.00000  0.00000  0.00000  231 VAL   C CG2 
10454 N N   . ASN   G  232 ? 0.61206 0.61206 0.61206 -0.00000 -0.00000 0.00000  232 ASN   C N   
10455 C CA  . ASN   G  232 ? 0.47244 0.47244 0.47244 -0.00000 0.00000  0.00000  232 ASN   C CA  
10456 C C   . ASN   G  232 ? 0.62041 0.62041 0.62041 -0.00000 0.00000  0.00000  232 ASN   C C   
10457 O O   . ASN   G  232 ? 0.55972 0.55972 0.55972 -0.00000 0.00000  0.00000  232 ASN   C O   
10458 C CB  . ASN   G  232 ? 0.68451 0.68451 0.68451 0.00000  0.00000  0.00000  232 ASN   C CB  
10459 C CG  . ASN   G  232 ? 0.67971 0.67971 0.67971 -0.00000 0.00000  0.00000  232 ASN   C CG  
10460 O OD1 . ASN   G  232 ? 0.69245 0.69245 0.69245 0.00000  0.00000  0.00000  232 ASN   C OD1 
10461 N ND2 . ASN   G  232 ? 1.64394 1.64394 1.64394 0.00000  0.00000  0.00000  232 ASN   C ND2 
10462 N N   . ASN   G  233 ? 0.43522 0.43522 0.43522 0.00000  0.00000  0.00000  233 ASN   C N   
10463 C CA  . ASN   G  233 ? 0.53274 0.53274 0.53274 0.00000  0.00000  0.00000  233 ASN   C CA  
10464 C C   . ASN   G  233 ? 1.19726 1.19726 1.19726 -0.00000 0.00000  0.00000  233 ASN   C C   
10465 O O   . ASN   G  233 ? 0.50422 0.50422 0.50422 0.00000  0.00000  0.00000  233 ASN   C O   
10466 C CB  . ASN   G  233 ? 0.27834 0.27834 0.27834 0.00000  0.00000  0.00000  233 ASN   C CB  
10467 C CG  . ASN   G  233 ? 0.75189 0.75189 0.75189 -0.00000 0.00000  0.00000  233 ASN   C CG  
10468 O OD1 . ASN   G  233 ? 0.66403 0.66403 0.66403 -0.00000 0.00000  0.00000  233 ASN   C OD1 
10469 N ND2 . ASN   G  233 ? 0.60940 0.60940 0.60940 0.00000  0.00000  0.00000  233 ASN   C ND2 
10470 N N   . THR   G  234 ? 0.48707 0.48707 0.48707 0.00000  0.00000  0.00000  234 THR   C N   
10471 C CA  . THR   G  234 ? 0.68128 0.68128 0.68128 0.00000  -0.00000 0.00000  234 THR   C CA  
10472 C C   . THR   G  234 ? 0.43094 0.43094 0.43094 -0.00000 0.00000  -0.00000 234 THR   C C   
10473 O O   . THR   G  234 ? 1.07050 1.07050 1.07050 0.00000  0.00000  0.00000  234 THR   C O   
10474 C CB  . THR   G  234 ? 0.50266 0.50266 0.50266 0.00000  0.00000  0.00000  234 THR   C CB  
10475 O OG1 . THR   G  234 ? 0.63164 0.63164 0.63164 -0.00000 0.00000  0.00000  234 THR   C OG1 
10476 C CG2 . THR   G  234 ? 0.37586 0.37586 0.37586 0.00000  0.00000  0.00000  234 THR   C CG2 
10477 N N   . THR   G  235 ? 0.67695 0.67695 0.67695 0.00000  0.00000  0.00000  235 THR   C N   
10478 C CA  . THR   G  235 ? 0.45164 0.45164 0.45164 -0.00000 0.00000  0.00000  235 THR   C CA  
10479 C C   . THR   G  235 ? 0.70627 0.70627 0.70627 0.00000  0.00000  0.00000  235 THR   C C   
10480 O O   . THR   G  235 ? 0.49420 0.49420 0.49420 0.00000  0.00000  0.00000  235 THR   C O   
10481 C CB  . THR   G  235 ? 0.89683 0.89683 0.89683 0.00000  0.00000  0.00000  235 THR   C CB  
10482 O OG1 . THR   G  235 ? 0.40528 0.40528 0.40528 0.00000  0.00000  0.00000  235 THR   C OG1 
10483 C CG2 . THR   G  235 ? 0.53153 0.53153 0.53153 -0.00000 0.00000  0.00000  235 THR   C CG2 
10484 N N   . LEU   G  236 ? 0.55444 0.55444 0.55444 -0.00000 -0.00000 0.00000  236 LEU   C N   
10485 C CA  . LEU   G  236 ? 0.56041 0.56041 0.56041 0.00000  0.00000  0.00000  236 LEU   C CA  
10486 C C   . LEU   G  236 ? 0.47959 0.47959 0.47959 0.00000  0.00000  0.00000  236 LEU   C C   
10487 O O   . LEU   G  236 ? 0.50135 0.50135 0.50135 0.00000  -0.00000 0.00000  236 LEU   C O   
10488 C CB  . LEU   G  236 ? 0.47842 0.47842 0.47842 0.00000  0.00000  0.00000  236 LEU   C CB  
10489 C CG  . LEU   G  236 ? 0.57079 0.57079 0.57079 0.00000  0.00000  0.00000  236 LEU   C CG  
10490 C CD1 . LEU   G  236 ? 0.46885 0.46885 0.46885 0.00000  0.00000  0.00000  236 LEU   C CD1 
10491 C CD2 . LEU   G  236 ? 0.34822 0.34822 0.34822 -0.00000 0.00000  0.00000  236 LEU   C CD2 
10492 N N   . ILE   G  237 ? 0.54080 0.54080 0.54080 -0.00000 0.00000  0.00000  237 ILE   C N   
10493 C CA  . ILE   G  237 ? 0.45628 0.45628 0.45628 -0.00000 0.00000  0.00000  237 ILE   C CA  
10494 C C   . ILE   G  237 ? 0.59859 0.59859 0.59859 -0.00000 0.00000  0.00000  237 ILE   C C   
10495 O O   . ILE   G  237 ? 0.43297 0.43297 0.43297 0.00000  0.00000  0.00000  237 ILE   C O   
10496 C CB  . ILE   G  237 ? 0.44138 0.44138 0.44138 0.00000  0.00000  0.00000  237 ILE   C CB  
10497 C CG1 . ILE   G  237 ? 0.40240 0.40240 0.40240 0.00000  0.00000  0.00000  237 ILE   C CG1 
10498 C CG2 . ILE   G  237 ? 0.41439 0.41439 0.41439 -0.00000 0.00000  0.00000  237 ILE   C CG2 
10499 C CD1 . ILE   G  237 ? 0.42640 0.42640 0.42640 0.00000  0.00000  0.00000  237 ILE   C CD1 
10500 N N   . SER   G  238 ? 0.39116 0.39116 0.39116 0.00000  0.00000  0.00000  238 SER   C N   
10501 C CA  . SER   G  238 ? 0.47689 0.47689 0.47689 -0.00000 0.00000  0.00000  238 SER   C CA  
10502 C C   . SER   G  238 ? 0.58766 0.58766 0.58766 0.00000  0.00000  0.00000  238 SER   C C   
10503 O O   . SER   G  238 ? 0.39733 0.39733 0.39733 0.00000  0.00000  0.00000  238 SER   C O   
10504 C CB  . SER   G  238 ? 0.45742 0.45742 0.45742 0.00000  0.00000  0.00000  238 SER   C CB  
10505 O OG  . SER   G  238 ? 0.63196 0.63196 0.63196 0.00000  0.00000  0.00000  238 SER   C OG  
10506 N N   . ALA   G  239 ? 0.51636 0.51636 0.51636 -0.00000 0.00000  0.00000  239 ALA   C N   
10507 C CA  . ALA   G  239 ? 0.61838 0.61838 0.61838 -0.00000 -0.00000 0.00000  239 ALA   C CA  
10508 C C   . ALA   G  239 ? 0.31695 0.31695 0.31695 0.00000  0.00000  0.00000  239 ALA   C C   
10509 O O   . ALA   G  239 ? 0.51241 0.51241 0.51241 -0.00000 0.00000  0.00000  239 ALA   C O   
10510 C CB  . ALA   G  239 ? 0.27104 0.27104 0.27104 0.00000  0.00000  0.00000  239 ALA   C CB  
10511 N N   . ALA   G  240 ? 0.40318 0.40318 0.40318 0.00000  -0.00000 0.00000  240 ALA   C N   
10512 C CA  . ALA   G  240 ? 0.32238 0.32238 0.32238 0.00000  0.00000  0.00000  240 ALA   C CA  
10513 C C   . ALA   G  240 ? 0.40431 0.40431 0.40431 0.00000  0.00000  0.00000  240 ALA   C C   
10514 O O   . ALA   G  240 ? 0.34498 0.34498 0.34498 0.00000  0.00000  0.00000  240 ALA   C O   
10515 C CB  . ALA   G  240 ? 0.21763 0.21763 0.21763 0.00000  0.00000  0.00000  240 ALA   C CB  
10516 N N   . CYS   G  241 ? 0.36964 0.36964 0.36964 0.00000  0.00000  0.00000  241 CYS   C N   
10517 C CA  . CYS   G  241 ? 0.49510 0.49510 0.49510 0.00000  0.00000  0.00000  241 CYS   C CA  
10518 C C   . CYS   G  241 ? 0.49902 0.49902 0.49902 -0.00000 0.00000  0.00000  241 CYS   C C   
10519 O O   . CYS   G  241 ? 0.48639 0.48639 0.48639 0.00000  0.00000  0.00000  241 CYS   C O   
10520 C CB  . CYS   G  241 ? 0.51584 0.51584 0.51584 0.00000  -0.00000 0.00000  241 CYS   C CB  
10521 S SG  . CYS   G  241 ? 0.51909 0.51909 0.51909 0.00000  0.00000  0.00000  241 CYS   C SG  
10522 N N   . GLU   G  242 ? 0.53280 0.53280 0.53280 0.00000  0.00000  0.00000  242 GLU   C N   
10523 C CA  . GLU   G  242 ? 0.32595 0.32595 0.32595 -0.00000 0.00000  0.00000  242 GLU   C CA  
10524 C C   . GLU   G  242 ? 0.36270 0.36270 0.36270 0.00000  -0.00000 0.00000  242 GLU   C C   
10525 O O   . GLU   G  242 ? 0.64869 0.64869 0.64869 -0.00000 0.00000  0.00000  242 GLU   C O   
10526 C CB  . GLU   G  242 ? 0.46376 0.46376 0.46376 -0.00000 0.00000  0.00000  242 GLU   C CB  
10527 C CG  . GLU   G  242 ? 0.39199 0.39199 0.39199 0.00000  0.00000  0.00000  242 GLU   C CG  
10528 C CD  . GLU   G  242 ? 0.69601 0.69601 0.69601 0.00000  0.00000  0.00000  242 GLU   C CD  
10529 O OE1 . GLU   G  242 ? 0.43607 0.43607 0.43607 0.00000  0.00000  0.00000  242 GLU   C OE1 
10530 O OE2 . GLU   G  242 ? 0.51896 0.51896 0.51896 -0.00000 0.00000  0.00000  242 GLU   C OE2 
10531 N N   . SER   G  243 ? 0.37730 0.37730 0.37730 -0.00000 0.00000  0.00000  243 SER   C N   
10532 C CA  . SER   G  243 ? 0.52274 0.52274 0.52274 0.00000  0.00000  0.00000  243 SER   C CA  
10533 C C   . SER   G  243 ? 0.39903 0.39903 0.39903 0.00000  0.00000  0.00000  243 SER   C C   
10534 O O   . SER   G  243 ? 0.45608 0.45608 0.45608 0.00000  0.00000  0.00000  243 SER   C O   
10535 C CB  . SER   G  243 ? 0.38634 0.38634 0.38634 -0.00000 0.00000  0.00000  243 SER   C CB  
10536 O OG  . SER   G  243 ? 0.48128 0.48128 0.48128 0.00000  0.00000  0.00000  243 SER   C OG  
10537 N N   . LEU   G  244 ? 0.43817 0.43817 0.43817 0.00000  0.00000  0.00000  244 LEU   C N   
10538 C CA  . LEU   G  244 ? 0.50828 0.50828 0.50828 -0.00000 0.00000  0.00000  244 LEU   C CA  
10539 C C   . LEU   G  244 ? 0.47666 0.47666 0.47666 0.00000  0.00000  0.00000  244 LEU   C C   
10540 O O   . LEU   G  244 ? 0.55621 0.55621 0.55621 0.00000  0.00000  0.00000  244 LEU   C O   
10541 C CB  . LEU   G  244 ? 0.31663 0.31663 0.31663 -0.00000 0.00000  0.00000  244 LEU   C CB  
10542 C CG  . LEU   G  244 ? 0.55015 0.55015 0.55015 -0.00000 0.00000  0.00000  244 LEU   C CG  
10543 C CD1 . LEU   G  244 ? 0.47366 0.47366 0.47366 0.00000  0.00000  0.00000  244 LEU   C CD1 
10544 C CD2 . LEU   G  244 ? 0.38790 0.38790 0.38790 -0.00000 0.00000  0.00000  244 LEU   C CD2 
10545 N N   . SER   G  245 ? 0.79155 0.79155 0.79155 0.00000  0.00000  0.00000  245 SER   C N   
10546 C CA  . SER   G  245 ? 0.29282 0.29282 0.29282 -0.00000 0.00000  0.00000  245 SER   C CA  
10547 C C   . SER   G  245 ? 0.29340 0.29340 0.29340 0.00000  0.00000  0.00000  245 SER   C C   
10548 O O   . SER   G  245 ? 0.40692 0.40692 0.40692 0.00000  0.00000  0.00000  245 SER   C O   
10549 C CB  . SER   G  245 ? 0.32753 0.32753 0.32753 0.00000  -0.00000 0.00000  245 SER   C CB  
10550 O OG  . SER   G  245 ? 0.90471 0.90471 0.90471 0.00000  -0.00000 0.00000  245 SER   C OG  
10551 N N   . TYR   G  246 ? 0.49131 0.49131 0.49131 0.00000  0.00000  0.00000  246 TYR   C N   
10552 C CA  . TYR   G  246 ? 0.36639 0.36639 0.36639 -0.00000 0.00000  0.00000  246 TYR   C CA  
10553 C C   . TYR   G  246 ? 0.38684 0.38684 0.38684 0.00000  0.00000  0.00000  246 TYR   C C   
10554 O O   . TYR   G  246 ? 0.42560 0.42560 0.42560 0.00000  0.00000  0.00000  246 TYR   C O   
10555 C CB  . TYR   G  246 ? 0.24445 0.24445 0.24445 0.00000  0.00000  0.00000  246 TYR   C CB  
10556 C CG  . TYR   G  246 ? 0.44938 0.44938 0.44938 0.00000  0.00000  0.00000  246 TYR   C CG  
10557 C CD1 . TYR   G  246 ? 0.36205 0.36205 0.36205 0.00000  0.00000  0.00000  246 TYR   C CD1 
10558 C CD2 . TYR   G  246 ? 0.18612 0.18612 0.18612 0.00000  0.00000  0.00000  246 TYR   C CD2 
10559 C CE1 . TYR   G  246 ? 0.28274 0.28274 0.28274 -0.00000 0.00000  0.00000  246 TYR   C CE1 
10560 C CE2 . TYR   G  246 ? 0.51912 0.51912 0.51912 -0.00000 0.00000  0.00000  246 TYR   C CE2 
10561 C CZ  . TYR   G  246 ? 0.40538 0.40538 0.40538 0.00000  0.00000  0.00000  246 TYR   C CZ  
10562 O OH  . TYR   G  246 ? 0.60926 0.60926 0.60926 0.00000  0.00000  0.00000  246 TYR   C OH  
10563 N N   . ASN   G  247 ? 0.35266 0.35266 0.35266 -0.00000 0.00000  0.00000  247 ASN   C N   
10564 C CA  . ASN   G  247 ? 0.25620 0.25620 0.25620 0.00000  0.00000  0.00000  247 ASN   C CA  
10565 C C   . ASN   G  247 ? 0.34580 0.34580 0.34580 0.00000  -0.00000 0.00000  247 ASN   C C   
10566 O O   . ASN   G  247 ? 0.38678 0.38678 0.38678 -0.00000 0.00000  0.00000  247 ASN   C O   
10567 C CB  . ASN   G  247 ? 0.38586 0.38586 0.38586 -0.00000 0.00000  0.00000  247 ASN   C CB  
10568 C CG  . ASN   G  247 ? 0.35609 0.35609 0.35609 0.00000  -0.00000 0.00000  247 ASN   C CG  
10569 O OD1 . ASN   G  247 ? 0.57745 0.57745 0.57745 0.00000  0.00000  0.00000  247 ASN   C OD1 
10570 N ND2 . ASN   G  247 ? 0.33635 0.33635 0.33635 0.00000  0.00000  0.00000  247 ASN   C ND2 
10571 N N   . VAL   G  248 ? 0.35041 0.35041 0.35041 0.00000  -0.00000 0.00000  248 VAL   C N   
10572 C CA  . VAL   G  248 ? 0.42375 0.42375 0.42375 -0.00000 0.00000  0.00000  248 VAL   C CA  
10573 C C   . VAL   G  248 ? 0.31655 0.31655 0.31655 0.00000  0.00000  0.00000  248 VAL   C C   
10574 O O   . VAL   G  248 ? 0.41164 0.41164 0.41164 -0.00000 0.00000  0.00000  248 VAL   C O   
10575 C CB  . VAL   G  248 ? 0.36739 0.36739 0.36739 0.00000  0.00000  0.00000  248 VAL   C CB  
10576 C CG1 . VAL   G  248 ? 0.27614 0.27614 0.27614 0.00000  0.00000  0.00000  248 VAL   C CG1 
10577 C CG2 . VAL   G  248 ? 0.34327 0.34327 0.34327 0.00000  0.00000  0.00000  248 VAL   C CG2 
10578 N N   . SER   G  249 ? 0.52204 0.52204 0.52204 -0.00000 0.00000  0.00000  249 SER   C N   
10579 C CA  . SER   G  249 ? 0.36210 0.36210 0.36210 0.00000  0.00000  0.00000  249 SER   C CA  
10580 C C   . SER   G  249 ? 0.52142 0.52142 0.52142 0.00000  0.00000  0.00000  249 SER   C C   
10581 O O   . SER   G  249 ? 0.39226 0.39226 0.39226 0.00000  0.00000  0.00000  249 SER   C O   
10582 C CB  . SER   G  249 ? 0.35688 0.35688 0.35688 -0.00000 0.00000  0.00000  249 SER   C CB  
10583 O OG  . SER   G  249 ? 0.42899 0.42899 0.42899 -0.00000 -0.00000 0.00000  249 SER   C OG  
10584 N N   . TYR   G  250 ? 0.37046 0.37046 0.37046 -0.00000 0.00000  0.00000  250 TYR   C N   
10585 C CA  . TYR   G  250 ? 0.70161 0.70161 0.70161 -0.00000 0.00000  0.00000  250 TYR   C CA  
10586 C C   . TYR   G  250 ? 0.33754 0.33754 0.33754 0.00000  0.00000  0.00000  250 TYR   C C   
10587 O O   . TYR   G  250 ? 0.45289 0.45289 0.45289 0.00000  0.00000  0.00000  250 TYR   C O   
10588 C CB  . TYR   G  250 ? 0.33034 0.33034 0.33034 -0.00000 0.00000  0.00000  250 TYR   C CB  
10589 C CG  . TYR   G  250 ? 0.52710 0.52710 0.52710 0.00000  0.00000  0.00000  250 TYR   C CG  
10590 C CD1 . TYR   G  250 ? 0.35460 0.35460 0.35460 0.00000  0.00000  0.00000  250 TYR   C CD1 
10591 C CD2 . TYR   G  250 ? 0.30544 0.30544 0.30544 0.00000  0.00000  0.00000  250 TYR   C CD2 
10592 C CE1 . TYR   G  250 ? 0.50469 0.50469 0.50469 0.00000  0.00000  0.00000  250 TYR   C CE1 
10593 C CE2 . TYR   G  250 ? 0.44580 0.44580 0.44580 0.00000  0.00000  0.00000  250 TYR   C CE2 
10594 C CZ  . TYR   G  250 ? 0.59659 0.59659 0.59659 0.00000  -0.00000 0.00000  250 TYR   C CZ  
10595 O OH  . TYR   G  250 ? 0.66649 0.66649 0.66649 -0.00000 0.00000  0.00000  250 TYR   C OH  
10596 N N   . ASP   G  251 ? 0.37396 0.37396 0.37396 0.00000  0.00000  0.00000  251 ASP   C N   
10597 C CA  . ASP   G  251 ? 0.37723 0.37723 0.37723 0.00000  0.00000  0.00000  251 ASP   C CA  
10598 C C   . ASP   G  251 ? 0.61348 0.61348 0.61348 0.00000  0.00000  0.00000  251 ASP   C C   
10599 O O   . ASP   G  251 ? 0.42181 0.42181 0.42181 0.00000  0.00000  0.00000  251 ASP   C O   
10600 C CB  . ASP   G  251 ? 0.36875 0.36875 0.36875 0.00000  0.00000  0.00000  251 ASP   C CB  
10601 C CG  . ASP   G  251 ? 0.65005 0.65005 0.65005 0.00000  0.00000  0.00000  251 ASP   C CG  
10602 O OD1 . ASP   G  251 ? 0.47822 0.47822 0.47822 0.00000  0.00000  0.00000  251 ASP   C OD1 
10603 O OD2 . ASP   G  251 ? 0.47243 0.47243 0.47243 0.00000  0.00000  0.00000  251 ASP   C OD2 
10604 N N   . VAL   G  252 ? 0.35567 0.35567 0.35567 0.00000  0.00000  0.00000  252 VAL   C N   
10605 C CA  . VAL   G  252 ? 0.38466 0.38466 0.38466 -0.00000 0.00000  0.00000  252 VAL   C CA  
10606 C C   . VAL   G  252 ? 0.39690 0.39690 0.39690 -0.00000 0.00000  0.00000  252 VAL   C C   
10607 O O   . VAL   G  252 ? 0.41784 0.41784 0.41784 0.00000  0.00000  0.00000  252 VAL   C O   
10608 C CB  . VAL   G  252 ? 0.42073 0.42073 0.42073 0.00000  0.00000  0.00000  252 VAL   C CB  
10609 C CG1 . VAL   G  252 ? 0.26868 0.26868 0.26868 0.00000  0.00000  0.00000  252 VAL   C CG1 
10610 C CG2 . VAL   G  252 ? 0.27363 0.27363 0.27363 0.00000  0.00000  0.00000  252 VAL   C CG2 
10611 N N   . GLN   G  253 ? 0.23953 0.23953 0.23953 0.00000  0.00000  0.00000  253 GLN   C N   
10612 C CA  . GLN   G  253 ? 0.31256 0.31256 0.31256 0.00000  0.00000  0.00000  253 GLN   C CA  
10613 C C   . GLN   G  253 ? 0.46273 0.46273 0.46273 -0.00000 0.00000  0.00000  253 GLN   C C   
10614 O O   . GLN   G  253 ? 0.30353 0.30353 0.30353 -0.00000 0.00000  0.00000  253 GLN   C O   
10615 C CB  . GLN   G  253 ? 0.16856 0.16856 0.16856 -0.00000 0.00000  0.00000  253 GLN   C CB  
10616 C CG  . GLN   G  253 ? 0.64447 0.64447 0.64447 -0.00000 0.00000  0.00000  253 GLN   C CG  
10617 C CD  . GLN   G  253 ? 0.53383 0.53383 0.53383 -0.00000 0.00000  0.00000  253 GLN   C CD  
10618 O OE1 . GLN   G  253 ? 0.54498 0.54498 0.54498 0.00000  -0.00000 -0.00000 253 GLN   C OE1 
10619 N NE2 . GLN   G  253 ? 0.63655 0.63655 0.63655 0.00000  0.00000  0.00000  253 GLN   C NE2 
10620 N N   . SER   G  254 ? 0.48347 0.48347 0.48347 -0.00000 0.00000  0.00000  254 SER   C N   
10621 C CA  . SER   G  254 ? 0.22948 0.22948 0.22948 -0.00000 0.00000  0.00000  254 SER   C CA  
10622 C C   . SER   G  254 ? 0.25595 0.25595 0.25595 0.00000  0.00000  0.00000  254 SER   C C   
10623 O O   . SER   G  254 ? 0.40486 0.40486 0.40486 0.00000  0.00000  0.00000  254 SER   C O   
10624 C CB  . SER   G  254 ? 0.36585 0.36585 0.36585 -0.00000 0.00000  0.00000  254 SER   C CB  
10625 O OG  . SER   G  254 ? 0.25910 0.25910 0.25910 0.00000  0.00000  0.00000  254 SER   C OG  
10626 N N   . LEU   G  255 ? 0.31997 0.31997 0.31997 -0.00000 0.00000  0.00000  255 LEU   C N   
10627 C CA  . LEU   G  255 ? 0.34988 0.34988 0.34988 0.00000  0.00000  0.00000  255 LEU   C CA  
10628 C C   . LEU   G  255 ? 0.36938 0.36938 0.36938 0.00000  0.00000  0.00000  255 LEU   C C   
10629 O O   . LEU   G  255 ? 0.38519 0.38519 0.38519 0.00000  0.00000  0.00000  255 LEU   C O   
10630 C CB  . LEU   G  255 ? 0.38431 0.38431 0.38431 -0.00000 0.00000  0.00000  255 LEU   C CB  
10631 C CG  . LEU   G  255 ? 0.40042 0.40042 0.40042 -0.00000 0.00000  0.00000  255 LEU   C CG  
10632 C CD1 . LEU   G  255 ? 0.38505 0.38505 0.38505 -0.00000 0.00000  0.00000  255 LEU   C CD1 
10633 C CD2 . LEU   G  255 ? 0.25625 0.25625 0.25625 0.00000  0.00000  0.00000  255 LEU   C CD2 
10634 N N   . ASP   G  256 ? 0.43603 0.43603 0.43603 0.00000  0.00000  0.00000  256 ASP   C N   
10635 C CA  . ASP   G  256 ? 0.25078 0.25078 0.25078 0.00000  -0.00000 0.00000  256 ASP   C CA  
10636 C C   . ASP   G  256 ? 0.53620 0.53620 0.53620 0.00000  0.00000  0.00000  256 ASP   C C   
10637 O O   . ASP   G  256 ? 0.28293 0.28293 0.28293 0.00000  0.00000  0.00000  256 ASP   C O   
10638 C CB  . ASP   G  256 ? 0.37775 0.37775 0.37775 0.00000  0.00000  0.00000  256 ASP   C CB  
10639 C CG  . ASP   G  256 ? 0.71621 0.71621 0.71621 0.00000  0.00000  0.00000  256 ASP   C CG  
10640 O OD1 . ASP   G  256 ? 0.38451 0.38451 0.38451 -0.00000 0.00000  -0.00000 256 ASP   C OD1 
10641 O OD2 . ASP   G  256 ? 0.39313 0.39313 0.39313 -0.00000 0.00000  0.00000  256 ASP   C OD2 
10642 N N   . THR   G  257 ? 0.31099 0.31099 0.31099 0.00000  0.00000  0.00000  257 THR   C N   
10643 C CA  . THR   G  257 ? 0.66803 0.66803 0.66803 0.00000  0.00000  0.00000  257 THR   C CA  
10644 C C   . THR   G  257 ? 0.23890 0.23890 0.23890 0.00000  0.00000  0.00000  257 THR   C C   
10645 O O   . THR   G  257 ? 0.51726 0.51726 0.51726 0.00000  0.00000  0.00000  257 THR   C O   
10646 C CB  . THR   G  257 ? 0.32800 0.32800 0.32800 0.00000  0.00000  0.00000  257 THR   C CB  
10647 O OG1 . THR   G  257 ? 0.61566 0.61566 0.61566 0.00000  0.00000  0.00000  257 THR   C OG1 
10648 C CG2 . THR   G  257 ? 0.47473 0.47473 0.47473 -0.00000 0.00000  0.00000  257 THR   C CG2 
10649 N N   . LEU   G  258 ? 0.50677 0.50677 0.50677 -0.00000 0.00000  0.00000  258 LEU   C N   
10650 C CA  . LEU   G  258 ? 0.32243 0.32243 0.32243 0.00000  0.00000  0.00000  258 LEU   C CA  
10651 C C   . LEU   G  258 ? 0.66740 0.66740 0.66740 -0.00000 0.00000  0.00000  258 LEU   C C   
10652 O O   . LEU   G  258 ? 0.70931 0.70931 0.70931 0.00000  0.00000  0.00000  258 LEU   C O   
10653 C CB  . LEU   G  258 ? 0.32408 0.32408 0.32408 -0.00000 0.00000  0.00000  258 LEU   C CB  
10654 C CG  . LEU   G  258 ? 0.27162 0.27162 0.27162 -0.00000 0.00000  0.00000  258 LEU   C CG  
10655 C CD1 . LEU   G  258 ? 0.36268 0.36268 0.36268 0.00000  0.00000  0.00000  258 LEU   C CD1 
10656 C CD2 . LEU   G  258 ? 0.22619 0.22619 0.22619 -0.00000 0.00000  0.00000  258 LEU   C CD2 
10657 N N   . VAL   G  259 ? 0.49544 0.49544 0.49544 -0.00000 0.00000  0.00000  259 VAL   C N   
10658 C CA  . VAL   G  259 ? 0.53771 0.53771 0.53771 -0.00000 0.00000  0.00000  259 VAL   C CA  
10659 C C   . VAL   G  259 ? 1.35016 1.35016 1.35016 -0.00000 0.00000  0.00000  259 VAL   C C   
10660 O O   . VAL   G  259 ? 0.48269 0.48269 0.48269 0.00000  0.00000  0.00000  259 VAL   C O   
10661 C CB  . VAL   G  259 ? 0.78695 0.78695 0.78695 -0.00000 0.00000  0.00000  259 VAL   C CB  
10662 C CG1 . VAL   G  259 ? 0.30730 0.30730 0.30730 0.00000  -0.00000 0.00000  259 VAL   C CG1 
10663 C CG2 . VAL   G  259 ? 0.61604 0.61604 0.61604 0.00000  0.00000  0.00000  259 VAL   C CG2 
10664 N N   . PHE   G  260 ? 0.37487 0.37487 0.37487 -0.00000 0.00000  0.00000  260 PHE   C N   
10665 C CA  . PHE   G  260 ? 1.14153 1.14153 1.14153 0.00000  0.00000  0.00000  260 PHE   C CA  
10666 C C   . PHE   G  260 ? 0.59792 0.59792 0.59792 -0.00000 0.00000  0.00000  260 PHE   C C   
10667 O O   . PHE   G  260 ? 1.56475 1.56475 1.56475 0.00000  0.00000  0.00000  260 PHE   C O   
10668 C CB  . PHE   G  260 ? 0.54093 0.54093 0.54093 0.00000  0.00000  0.00000  260 PHE   C CB  
10669 C CG  . PHE   G  260 ? 0.76542 0.76542 0.76542 0.00000  0.00000  0.00000  260 PHE   C CG  
10670 C CD1 . PHE   G  260 ? 0.48107 0.48107 0.48107 0.00000  -0.00000 0.00000  260 PHE   C CD1 
10671 C CD2 . PHE   G  260 ? 0.67890 0.67890 0.67890 0.00000  0.00000  0.00000  260 PHE   C CD2 
10672 C CE1 . PHE   G  260 ? 1.73509 1.73509 1.73509 0.00000  0.00000  0.00000  260 PHE   C CE1 
10673 C CE2 . PHE   G  260 ? 0.69843 0.69843 0.69843 0.00000  0.00000  0.00000  260 PHE   C CE2 
10674 C CZ  . PHE   G  260 ? 0.90971 0.90971 0.90971 0.00000  0.00000  0.00000  260 PHE   C CZ  
10675 N N   . LYS   G  261 ? 0.52982 0.52982 0.52982 0.00000  0.00000  0.00000  261 LYS   C N   
10676 C CA  . LYS   G  261 ? 1.35893 1.35893 1.35893 -0.00000 0.00000  0.00000  261 LYS   C CA  
10677 C C   . LYS   G  261 ? 1.06979 1.06979 1.06979 0.00000  0.00000  0.00000  261 LYS   C C   
10678 O O   . LYS   G  261 ? 0.51424 0.51424 0.51424 0.00000  0.00000  0.00000  261 LYS   C O   
10679 C CB  . LYS   G  261 ? 1.07342 1.07342 1.07342 -0.00000 0.00000  0.00000  261 LYS   C CB  
10680 C CG  . LYS   G  261 ? 1.42940 1.42940 1.42940 0.00000  0.00000  0.00000  261 LYS   C CG  
10681 C CD  . LYS   G  261 ? 1.21929 1.21929 1.21929 -0.00000 0.00000  0.00000  261 LYS   C CD  
10682 C CE  . LYS   G  261 ? 0.38174 0.38174 0.38174 -0.00000 0.00000  0.00000  261 LYS   C CE  
10683 N NZ  . LYS   G  261 ? 0.55765 0.55765 0.55765 -0.00000 0.00000  0.00000  261 LYS   C NZ  
10684 N N   . GLY   G  262 ? 1.09648 1.09648 1.09648 0.00000  0.00000  0.00000  262 GLY   C N   
10685 C CA  . GLY   G  262 ? 0.39475 0.39475 0.39475 0.00000  0.00000  0.00000  262 GLY   C CA  
10686 C C   . GLY   G  262 ? 1.11491 1.11491 1.11491 0.00000  0.00000  0.00000  262 GLY   C C   
10687 O O   . GLY   G  262 ? 1.03036 1.03036 1.03036 -0.00000 0.00000  0.00000  262 GLY   C O   
10688 N N   . GLU   G  263 ? 0.50489 0.50489 0.50489 0.00000  0.00000  0.00000  263 GLU   C N   
10689 C CA  . GLU   G  263 ? 0.94060 0.94060 0.94060 0.00000  -0.00000 0.00000  263 GLU   C CA  
10690 C C   . GLU   G  263 ? 1.06859 1.06859 1.06859 0.00000  0.00000  0.00000  263 GLU   C C   
10691 O O   . GLU   G  263 ? 0.62317 0.62317 0.62317 0.00000  0.00000  0.00000  263 GLU   C O   
10692 C CB  . GLU   G  263 ? 0.48490 0.48490 0.48490 0.00000  0.00000  0.00000  263 GLU   C CB  
10693 C CG  . GLU   G  263 ? 0.93618 0.93618 0.93618 -0.00000 0.00000  0.00000  263 GLU   C CG  
10694 C CD  . GLU   G  263 ? 0.85068 0.85068 0.85068 0.00000  0.00000  0.00000  263 GLU   C CD  
10695 O OE1 . GLU   G  263 ? 0.47511 0.47511 0.47511 0.00000  0.00000  0.00000  263 GLU   C OE1 
10696 O OE2 . GLU   G  263 ? 0.65032 0.65032 0.65032 0.00000  0.00000  0.00000  263 GLU   C OE2 
10697 N N   . THR   G  264 ? 0.49308 0.49308 0.49308 -0.00000 0.00000  0.00000  264 THR   C N   
10698 C CA  . THR   G  264 ? 0.30980 0.30980 0.30980 0.00000  0.00000  0.00000  264 THR   C CA  
10699 C C   . THR   G  264 ? 0.50293 0.50293 0.50293 0.00000  0.00000  0.00000  264 THR   C C   
10700 O O   . THR   G  264 ? 0.38996 0.38996 0.38996 -0.00000 0.00000  0.00000  264 THR   C O   
10701 C CB  . THR   G  264 ? 0.57382 0.57382 0.57382 0.00000  0.00000  0.00000  264 THR   C CB  
10702 O OG1 . THR   G  264 ? 1.22064 1.22064 1.22064 -0.00000 0.00000  0.00000  264 THR   C OG1 
10703 C CG2 . THR   G  264 ? 0.40902 0.40902 0.40902 -0.00000 0.00000  0.00000  264 THR   C CG2 
10704 N N   . TYR   G  265 ? 0.38731 0.38731 0.38731 0.00000  0.00000  0.00000  265 TYR   C N   
10705 C CA  . TYR   G  265 ? 0.26717 0.26717 0.26717 0.00000  0.00000  0.00000  265 TYR   C CA  
10706 C C   . TYR   G  265 ? 0.32845 0.32845 0.32845 -0.00000 0.00000  0.00000  265 TYR   C C   
10707 O O   . TYR   G  265 ? 0.43002 0.43002 0.43002 -0.00000 0.00000  0.00000  265 TYR   C O   
10708 C CB  . TYR   G  265 ? 0.21745 0.21745 0.21745 -0.00000 0.00000  0.00000  265 TYR   C CB  
10709 C CG  . TYR   G  265 ? 0.45629 0.45629 0.45629 -0.00000 0.00000  0.00000  265 TYR   C CG  
10710 C CD1 . TYR   G  265 ? 0.34674 0.34674 0.34674 -0.00000 0.00000  0.00000  265 TYR   C CD1 
10711 C CD2 . TYR   G  265 ? 0.31588 0.31588 0.31588 -0.00000 0.00000  0.00000  265 TYR   C CD2 
10712 C CE1 . TYR   G  265 ? 0.44693 0.44693 0.44693 0.00000  0.00000  0.00000  265 TYR   C CE1 
10713 C CE2 . TYR   G  265 ? 0.42457 0.42457 0.42457 -0.00000 0.00000  0.00000  265 TYR   C CE2 
10714 C CZ  . TYR   G  265 ? 0.34745 0.34745 0.34745 0.00000  0.00000  0.00000  265 TYR   C CZ  
10715 O OH  . TYR   G  265 ? 0.38965 0.38965 0.38965 0.00000  0.00000  0.00000  265 TYR   C OH  
10716 N N   . SER   G  266 ? 0.36844 0.36844 0.36844 0.00000  0.00000  0.00000  266 SER   C N   
10717 C CA  . SER   G  266 ? 0.22986 0.22986 0.22986 -0.00000 0.00000  0.00000  266 SER   C CA  
10718 C C   . SER   G  266 ? 0.40094 0.40094 0.40094 0.00000  0.00000  0.00000  266 SER   C C   
10719 O O   . SER   G  266 ? 0.28115 0.28115 0.28115 0.00000  0.00000  0.00000  266 SER   C O   
10720 C CB  . SER   G  266 ? 0.25216 0.25216 0.25216 -0.00000 0.00000  0.00000  266 SER   C CB  
10721 O OG  . SER   G  266 ? 0.38578 0.38578 0.38578 0.00000  0.00000  0.00000  266 SER   C OG  
10722 N N   . LEU   G  267 ? 0.29149 0.29149 0.29149 0.00000  -0.00000 0.00000  267 LEU   C N   
10723 C CA  . LEU   G  267 ? 0.41290 0.41290 0.41290 -0.00000 0.00000  0.00000  267 LEU   C CA  
10724 C C   . LEU   G  267 ? 0.28344 0.28344 0.28344 0.00000  0.00000  0.00000  267 LEU   C C   
10725 O O   . LEU   G  267 ? 0.48098 0.48098 0.48098 0.00000  0.00000  0.00000  267 LEU   C O   
10726 C CB  . LEU   G  267 ? 0.20339 0.20339 0.20339 -0.00000 0.00000  0.00000  267 LEU   C CB  
10727 C CG  . LEU   G  267 ? 0.45163 0.45163 0.45163 0.00000  0.00000  0.00000  267 LEU   C CG  
10728 C CD1 . LEU   G  267 ? 0.35128 0.35128 0.35128 -0.00000 0.00000  0.00000  267 LEU   C CD1 
10729 C CD2 . LEU   G  267 ? 0.27890 0.27890 0.27890 -0.00000 0.00000  0.00000  267 LEU   C CD2 
10730 N N   . LYS   G  268 ? 0.49951 0.49951 0.49951 -0.00000 0.00000  0.00000  268 LYS   C N   
10731 C CA  . LYS   G  268 ? 0.23171 0.23171 0.23171 0.00000  0.00000  0.00000  268 LYS   C CA  
10732 C C   . LYS   G  268 ? 0.47149 0.47149 0.47149 0.00000  0.00000  0.00000  268 LYS   C C   
10733 O O   . LYS   G  268 ? 0.20706 0.20706 0.20706 0.00000  0.00000  0.00000  268 LYS   C O   
10734 C CB  . LYS   G  268 ? 0.31286 0.31286 0.31286 0.00000  0.00000  0.00000  268 LYS   C CB  
10735 C CG  . LYS   G  268 ? 0.47643 0.47643 0.47643 0.00000  0.00000  0.00000  268 LYS   C CG  
10736 C CD  . LYS   G  268 ? 0.39538 0.39538 0.39538 0.00000  0.00000  0.00000  268 LYS   C CD  
10737 C CE  . LYS   G  268 ? 0.55475 0.55475 0.55475 -0.00000 0.00000  0.00000  268 LYS   C CE  
10738 N NZ  . LYS   G  268 ? 0.51400 0.51400 0.51400 -0.00000 0.00000  0.00000  268 LYS   C NZ  
10739 N N   . HIS   G  269 ? 0.36231 0.36231 0.36231 -0.00000 0.00000  0.00000  269 HIS   C N   
10740 C CA  . HIS   G  269 ? 0.16603 0.16603 0.16603 0.00000  0.00000  0.00000  269 HIS   C CA  
10741 C C   . HIS   G  269 ? 0.48178 0.48178 0.48178 -0.00000 0.00000  0.00000  269 HIS   C C   
10742 O O   . HIS   G  269 ? 0.26314 0.26314 0.26314 0.00000  0.00000  0.00000  269 HIS   C O   
10743 C CB  . HIS   G  269 ? 0.26308 0.26308 0.26308 0.00000  0.00000  0.00000  269 HIS   C CB  
10744 C CG  . HIS   G  269 ? 0.31433 0.31433 0.31433 0.00000  -0.00000 -0.00000 269 HIS   C CG  
10745 N ND1 . HIS   G  269 ? 0.58491 0.58491 0.58491 0.00000  0.00000  0.00000  269 HIS   C ND1 
10746 C CD2 . HIS   G  269 ? 0.40647 0.40647 0.40647 0.00000  0.00000  0.00000  269 HIS   C CD2 
10747 C CE1 . HIS   G  269 ? 0.27109 0.27109 0.27109 -0.00000 0.00000  0.00000  269 HIS   C CE1 
10748 N NE2 . HIS   G  269 ? 0.46799 0.46799 0.46799 -0.00000 0.00000  0.00000  269 HIS   C NE2 
10749 N N   . LEU   G  270 ? 0.30731 0.30731 0.30731 0.00000  0.00000  0.00000  270 LEU   C N   
10750 C CA  . LEU   G  270 ? 0.24722 0.24722 0.24722 -0.00000 0.00000  0.00000  270 LEU   C CA  
10751 C C   . LEU   G  270 ? 0.29392 0.29392 0.29392 0.00000  0.00000  0.00000  270 LEU   C C   
10752 O O   . LEU   G  270 ? 0.33896 0.33896 0.33896 -0.00000 0.00000  0.00000  270 LEU   C O   
10753 C CB  . LEU   G  270 ? 0.33234 0.33234 0.33234 0.00000  0.00000  0.00000  270 LEU   C CB  
10754 C CG  . LEU   G  270 ? 0.29514 0.29514 0.29514 0.00000  0.00000  0.00000  270 LEU   C CG  
10755 C CD1 . LEU   G  270 ? 0.26645 0.26645 0.26645 -0.00000 -0.00000 0.00000  270 LEU   C CD1 
10756 C CD2 . LEU   G  270 ? 0.36771 0.36771 0.36771 -0.00000 0.00000  0.00000  270 LEU   C CD2 
10757 N N   . LEU   G  271 ? 0.36925 0.36925 0.36925 0.00000  0.00000  0.00000  271 LEU   C N   
10758 C CA  . LEU   G  271 ? 0.32653 0.32653 0.32653 0.00000  -0.00000 0.00000  271 LEU   C CA  
10759 C C   . LEU   G  271 ? 0.43333 0.43333 0.43333 -0.00000 0.00000  0.00000  271 LEU   C C   
10760 O O   . LEU   G  271 ? 0.30113 0.30113 0.30113 0.00000  0.00000  0.00000  271 LEU   C O   
10761 C CB  . LEU   G  271 ? 0.20574 0.20574 0.20574 -0.00000 0.00000  0.00000  271 LEU   C CB  
10762 C CG  . LEU   G  271 ? 0.37151 0.37151 0.37151 -0.00000 0.00000  0.00000  271 LEU   C CG  
10763 C CD1 . LEU   G  271 ? 0.25901 0.25901 0.25901 0.00000  0.00000  0.00000  271 LEU   C CD1 
10764 C CD2 . LEU   G  271 ? 0.17702 0.17702 0.17702 -0.00000 0.00000  0.00000  271 LEU   C CD2 
10765 N N   . ASN   G  272 ? 0.30884 0.30884 0.30884 0.00000  0.00000  0.00000  272 ASN   C N   
10766 C CA  . ASN   G  272 ? 0.20753 0.20753 0.20753 0.00000  0.00000  0.00000  272 ASN   C CA  
10767 C C   . ASN   G  272 ? 0.36124 0.36124 0.36124 0.00000  0.00000  0.00000  272 ASN   C C   
10768 O O   . ASN   G  272 ? 0.44729 0.44729 0.44729 0.00000  0.00000  0.00000  272 ASN   C O   
10769 C CB  . ASN   G  272 ? 0.48502 0.48502 0.48502 -0.00000 0.00000  0.00000  272 ASN   C CB  
10770 C CG  . ASN   G  272 ? 0.36459 0.36459 0.36459 0.00000  0.00000  0.00000  272 ASN   C CG  
10771 O OD1 . ASN   G  272 ? 0.36210 0.36210 0.36210 0.00000  0.00000  0.00000  272 ASN   C OD1 
10772 N ND2 . ASN   G  272 ? 0.44352 0.44352 0.44352 0.00000  -0.00000 0.00000  272 ASN   C ND2 
10773 N N   . ASN   G  273 ? 0.36364 0.36364 0.36364 0.00000  -0.00000 0.00000  273 ASN   C N   
10774 C CA  . ASN   G  273 ? 0.47897 0.47897 0.47897 0.00000  0.00000  0.00000  273 ASN   C CA  
10775 C C   . ASN   G  273 ? 0.32711 0.32711 0.32711 0.00000  0.00000  0.00000  273 ASN   C C   
10776 O O   . ASN   G  273 ? 0.43850 0.43850 0.43850 0.00000  0.00000  0.00000  273 ASN   C O   
10777 C CB  . ASN   G  273 ? 0.40917 0.40917 0.40917 0.00000  0.00000  0.00000  273 ASN   C CB  
10778 C CG  . ASN   G  273 ? 0.87150 0.87150 0.87150 0.00000  0.00000  0.00000  273 ASN   C CG  
10779 O OD1 . ASN   G  273 ? 0.94036 0.94036 0.94036 0.00000  0.00000  0.00000  273 ASN   C OD1 
10780 N ND2 . ASN   G  273 ? 0.90520 0.90520 0.90520 0.00000  0.00000  0.00000  273 ASN   C ND2 
10781 N N   . ASP   G  274 ? 0.36029 0.36029 0.36029 0.00000  0.00000  0.00000  274 ASP   C N   
10782 C CA  . ASP   G  274 ? 0.32506 0.32506 0.32506 0.00000  0.00000  0.00000  274 ASP   C CA  
10783 C C   . ASP   G  274 ? 0.25410 0.25410 0.25410 -0.00000 0.00000  0.00000  274 ASP   C C   
10784 O O   . ASP   G  274 ? 0.26461 0.26461 0.26461 0.00000  0.00000  0.00000  274 ASP   C O   
10785 C CB  . ASP   G  274 ? 0.28188 0.28188 0.28188 -0.00000 0.00000  0.00000  274 ASP   C CB  
10786 C CG  . ASP   G  274 ? 0.40386 0.40386 0.40386 0.00000  0.00000  0.00000  274 ASP   C CG  
10787 O OD1 . ASP   G  274 ? 0.51112 0.51112 0.51112 0.00000  0.00000  0.00000  274 ASP   C OD1 
10788 O OD2 . ASP   G  274 ? 0.68493 0.68493 0.68493 -0.00000 -0.00000 0.00000  274 ASP   C OD2 
10789 N N   . PRO   G  275 ? 0.44643 0.44643 0.44643 -0.00000 0.00000  0.00000  275 PRO   C N   
10790 C CA  . PRO   G  275 ? 0.19278 0.19278 0.19278 0.00000  0.00000  0.00000  275 PRO   C CA  
10791 C C   . PRO   G  275 ? 0.31439 0.31439 0.31439 0.00000  0.00000  0.00000  275 PRO   C C   
10792 O O   . PRO   G  275 ? 0.48303 0.48303 0.48303 0.00000  0.00000  0.00000  275 PRO   C O   
10793 C CB  . PRO   G  275 ? 0.22098 0.22098 0.22098 0.00000  0.00000  0.00000  275 PRO   C CB  
10794 C CG  . PRO   G  275 ? 0.24689 0.24689 0.24689 0.00000  0.00000  0.00000  275 PRO   C CG  
10795 C CD  . PRO   G  275 ? 0.29676 0.29676 0.29676 0.00000  0.00000  -0.00000 275 PRO   C CD  
10796 N N   . PHE   G  276 ? 0.35636 0.35636 0.35636 0.00000  0.00000  0.00000  276 PHE   C N   
10797 C CA  . PHE   G  276 ? 0.23392 0.23392 0.23392 -0.00000 0.00000  0.00000  276 PHE   C CA  
10798 C C   . PHE   G  276 ? 0.45037 0.45037 0.45037 0.00000  0.00000  0.00000  276 PHE   C C   
10799 O O   . PHE   G  276 ? 0.39792 0.39792 0.39792 0.00000  0.00000  0.00000  276 PHE   C O   
10800 C CB  . PHE   G  276 ? 0.24960 0.24960 0.24960 0.00000  0.00000  0.00000  276 PHE   C CB  
10801 C CG  . PHE   G  276 ? 0.44607 0.44607 0.44607 -0.00000 0.00000  0.00000  276 PHE   C CG  
10802 C CD1 . PHE   G  276 ? 0.35750 0.35750 0.35750 -0.00000 0.00000  0.00000  276 PHE   C CD1 
10803 C CD2 . PHE   G  276 ? 0.32034 0.32034 0.32034 0.00000  0.00000  0.00000  276 PHE   C CD2 
10804 C CE1 . PHE   G  276 ? 0.50669 0.50669 0.50669 0.00000  0.00000  0.00000  276 PHE   C CE1 
10805 C CE2 . PHE   G  276 ? 0.55498 0.55498 0.55498 -0.00000 0.00000  0.00000  276 PHE   C CE2 
10806 C CZ  . PHE   G  276 ? 0.43459 0.43459 0.43459 0.00000  0.00000  0.00000  276 PHE   C CZ  
10807 N N   . THR   G  277 ? 0.33770 0.33770 0.33770 0.00000  0.00000  0.00000  277 THR   C N   
10808 C CA  . THR   G  277 ? 0.41019 0.41019 0.41019 -0.00000 0.00000  0.00000  277 THR   C CA  
10809 C C   . THR   G  277 ? 0.30352 0.30352 0.30352 0.00000  0.00000  0.00000  277 THR   C C   
10810 O O   . THR   G  277 ? 0.38028 0.38028 0.38028 -0.00000 0.00000  0.00000  277 THR   C O   
10811 C CB  . THR   G  277 ? 0.26763 0.26763 0.26763 -0.00000 0.00000  0.00000  277 THR   C CB  
10812 O OG1 . THR   G  277 ? 0.34662 0.34662 0.34662 -0.00000 0.00000  0.00000  277 THR   C OG1 
10813 C CG2 . THR   G  277 ? 0.14093 0.14093 0.14093 -0.00000 0.00000  0.00000  277 THR   C CG2 
10814 N N   . PRO   G  278 ? 0.61889 0.61889 0.61889 0.00000  0.00000  0.00000  278 PRO   C N   
10815 C CA  . PRO   G  278 ? 0.27303 0.27303 0.27303 -0.00000 0.00000  0.00000  278 PRO   C CA  
10816 C C   . PRO   G  278 ? 0.45043 0.45043 0.45043 0.00000  0.00000  0.00000  278 PRO   C C   
10817 O O   . PRO   G  278 ? 0.30557 0.30557 0.30557 0.00000  0.00000  0.00000  278 PRO   C O   
10818 C CB  . PRO   G  278 ? 0.18102 0.18102 0.18102 0.00000  0.00000  0.00000  278 PRO   C CB  
10819 C CG  . PRO   G  278 ? 0.22883 0.22883 0.22883 0.00000  0.00000  0.00000  278 PRO   C CG  
10820 C CD  . PRO   G  278 ? 0.26568 0.26568 0.26568 0.00000  0.00000  0.00000  278 PRO   C CD  
10821 N N   . GLN   G  279 ? 0.33561 0.33561 0.33561 -0.00000 -0.00000 0.00000  279 GLN   C N   
10822 C CA  . GLN   G  279 ? 0.30792 0.30792 0.30792 0.00000  0.00000  0.00000  279 GLN   C CA  
10823 C C   . GLN   G  279 ? 0.47766 0.47766 0.47766 -0.00000 -0.00000 0.00000  279 GLN   C C   
10824 O O   . GLN   G  279 ? 0.45728 0.45728 0.45728 -0.00000 0.00000  0.00000  279 GLN   C O   
10825 C CB  . GLN   G  279 ? 0.27547 0.27547 0.27547 -0.00000 -0.00000 -0.00000 279 GLN   C CB  
10826 C CG  . GLN   G  279 ? 0.16785 0.16785 0.16785 0.00000  0.00000  0.00000  279 GLN   C CG  
10827 C CD  . GLN   G  279 ? 0.66845 0.66845 0.66845 -0.00000 0.00000  0.00000  279 GLN   C CD  
10828 O OE1 . GLN   G  279 ? 0.48900 0.48900 0.48900 -0.00000 0.00000  0.00000  279 GLN   C OE1 
10829 N NE2 . GLN   G  279 ? 0.37532 0.37532 0.37532 0.00000  0.00000  0.00000  279 GLN   C NE2 
10830 N N   . PHE   G  280 ? 0.36575 0.36575 0.36575 -0.00000 0.00000  0.00000  280 PHE   C N   
10831 C CA  . PHE   G  280 ? 0.38574 0.38574 0.38574 -0.00000 0.00000  0.00000  280 PHE   C CA  
10832 C C   . PHE   G  280 ? 0.36449 0.36449 0.36449 0.00000  0.00000  0.00000  280 PHE   C C   
10833 O O   . PHE   G  280 ? 0.39835 0.39835 0.39835 -0.00000 0.00000  0.00000  280 PHE   C O   
10834 C CB  . PHE   G  280 ? 0.15667 0.15667 0.15667 -0.00000 0.00000  0.00000  280 PHE   C CB  
10835 C CG  . PHE   G  280 ? 0.53569 0.53569 0.53569 0.00000  0.00000  0.00000  280 PHE   C CG  
10836 C CD1 . PHE   G  280 ? 0.29125 0.29125 0.29125 0.00000  -0.00000 0.00000  280 PHE   C CD1 
10837 C CD2 . PHE   G  280 ? 0.16870 0.16870 0.16870 0.00000  0.00000  0.00000  280 PHE   C CD2 
10838 C CE1 . PHE   G  280 ? 0.47765 0.47765 0.47765 0.00000  0.00000  0.00000  280 PHE   C CE1 
10839 C CE2 . PHE   G  280 ? 0.46893 0.46893 0.46893 -0.00000 0.00000  0.00000  280 PHE   C CE2 
10840 C CZ  . PHE   G  280 ? 0.37235 0.37235 0.37235 0.00000  0.00000  0.00000  280 PHE   C CZ  
10841 N N   . GLU   G  281 ? 0.37521 0.37521 0.37521 0.00000  0.00000  0.00000  281 GLU   C N   
10842 C CA  . GLU   G  281 ? 0.53789 0.53789 0.53789 -0.00000 0.00000  0.00000  281 GLU   C CA  
10843 C C   . GLU   G  281 ? 0.24972 0.24972 0.24972 -0.00000 0.00000  0.00000  281 GLU   C C   
10844 O O   . GLU   G  281 ? 0.49919 0.49919 0.49919 0.00000  -0.00000 0.00000  281 GLU   C O   
10845 C CB  . GLU   G  281 ? 0.29111 0.29111 0.29111 0.00000  0.00000  0.00000  281 GLU   C CB  
10846 C CG  . GLU   G  281 ? 0.69611 0.69611 0.69611 0.00000  0.00000  0.00000  281 GLU   C CG  
10847 C CD  . GLU   G  281 ? 1.55997 1.55997 1.55997 0.00000  0.00000  0.00000  281 GLU   C CD  
10848 O OE1 . GLU   G  281 ? 0.53592 0.53592 0.53592 0.00000  0.00000  0.00000  281 GLU   C OE1 
10849 O OE2 . GLU   G  281 ? 0.73823 0.73823 0.73823 0.00000  0.00000  0.00000  281 GLU   C OE2 
10850 N N   . HIS   G  282 ? 0.27185 0.27185 0.27185 0.00000  0.00000  0.00000  282 HIS   C N   
10851 C CA  . HIS   G  282 ? 0.57056 0.57056 0.57056 -0.00000 0.00000  0.00000  282 HIS   C CA  
10852 C C   . HIS   G  282 ? 0.41328 0.41328 0.41328 0.00000  0.00000  0.00000  282 HIS   C C   
10853 O O   . HIS   G  282 ? 0.47947 0.47947 0.47947 0.00000  0.00000  0.00000  282 HIS   C O   
10854 C CB  . HIS   G  282 ? 0.15903 0.15903 0.15903 0.00000  0.00000  0.00000  282 HIS   C CB  
10855 C CG  . HIS   G  282 ? 0.75099 0.75099 0.75099 -0.00000 0.00000  0.00000  282 HIS   C CG  
10856 N ND1 . HIS   G  282 ? 0.55735 0.55735 0.55735 -0.00000 0.00000  0.00000  282 HIS   C ND1 
10857 C CD2 . HIS   G  282 ? 0.24778 0.24778 0.24778 0.00000  0.00000  0.00000  282 HIS   C CD2 
10858 C CE1 . HIS   G  282 ? 0.35343 0.35343 0.35343 0.00000  0.00000  0.00000  282 HIS   C CE1 
10859 N NE2 . HIS   G  282 ? 0.50489 0.50489 0.50489 0.00000  0.00000  0.00000  282 HIS   C NE2 
10860 N N   . GLY   G  283 ? 0.48089 0.48089 0.48089 -0.00000 -0.00000 0.00000  283 GLY   C N   
10861 C CA  . GLY   G  283 ? 0.22199 0.22199 0.22199 0.00000  0.00000  0.00000  283 GLY   C CA  
10862 C C   . GLY   G  283 ? 0.37619 0.37619 0.37619 0.00000  0.00000  0.00000  283 GLY   C C   
10863 O O   . GLY   G  283 ? 0.36406 0.36406 0.36406 0.00000  0.00000  0.00000  283 GLY   C O   
10864 N N   . SER   G  284 ? 0.37223 0.37223 0.37223 -0.00000 0.00000  0.00000  284 SER   C N   
10865 C CA  . SER   G  284 ? 0.48249 0.48249 0.48249 0.00000  0.00000  0.00000  284 SER   C CA  
10866 C C   . SER   G  284 ? 0.40658 0.40658 0.40658 0.00000  0.00000  0.00000  284 SER   C C   
10867 O O   . SER   G  284 ? 0.31712 0.31712 0.31712 0.00000  0.00000  0.00000  284 SER   C O   
10868 C CB  . SER   G  284 ? 0.26775 0.26775 0.26775 -0.00000 0.00000  0.00000  284 SER   C CB  
10869 O OG  . SER   G  284 ? 0.50486 0.50486 0.50486 0.00000  0.00000  0.00000  284 SER   C OG  
10870 N N   . ILE   G  285 ? 0.29971 0.29971 0.29971 0.00000  0.00000  0.00000  285 ILE   C N   
10871 C CA  . ILE   G  285 ? 0.28378 0.28378 0.28378 -0.00000 0.00000  0.00000  285 ILE   C CA  
10872 C C   . ILE   G  285 ? 0.23511 0.23511 0.23511 -0.00000 0.00000  0.00000  285 ILE   C C   
10873 O O   . ILE   G  285 ? 0.47569 0.47569 0.47569 0.00000  0.00000  0.00000  285 ILE   C O   
10874 C CB  . ILE   G  285 ? 0.32690 0.32690 0.32690 -0.00000 -0.00000 0.00000  285 ILE   C CB  
10875 C CG1 . ILE   G  285 ? 0.28244 0.28244 0.28244 0.00000  0.00000  0.00000  285 ILE   C CG1 
10876 C CG2 . ILE   G  285 ? 0.23105 0.23105 0.23105 0.00000  0.00000  0.00000  285 ILE   C CG2 
10877 C CD1 . ILE   G  285 ? 0.38742 0.38742 0.38742 -0.00000 0.00000  0.00000  285 ILE   C CD1 
10878 N N   . LEU   G  286 ? 0.46755 0.46755 0.46755 0.00000  -0.00000 0.00000  286 LEU   C N   
10879 C CA  . LEU   G  286 ? 0.25058 0.25058 0.25058 0.00000  0.00000  0.00000  286 LEU   C CA  
10880 C C   . LEU   G  286 ? 0.33797 0.33797 0.33797 0.00000  0.00000  0.00000  286 LEU   C C   
10881 O O   . LEU   G  286 ? 0.39769 0.39769 0.39769 -0.00000 0.00000  0.00000  286 LEU   C O   
10882 C CB  . LEU   G  286 ? 0.44292 0.44292 0.44292 0.00000  0.00000  0.00000  286 LEU   C CB  
10883 C CG  . LEU   G  286 ? 0.38798 0.38798 0.38798 0.00000  0.00000  0.00000  286 LEU   C CG  
10884 C CD1 . LEU   G  286 ? 0.32415 0.32415 0.32415 -0.00000 0.00000  0.00000  286 LEU   C CD1 
10885 C CD2 . LEU   G  286 ? 0.39049 0.39049 0.39049 0.00000  0.00000  0.00000  286 LEU   C CD2 
10886 N N   . GLN   G  287 ? 0.23674 0.23674 0.23674 0.00000  0.00000  0.00000  287 GLN   C N   
10887 C CA  . GLN   G  287 ? 0.41484 0.41484 0.41484 -0.00000 0.00000  0.00000  287 GLN   C CA  
10888 C C   . GLN   G  287 ? 0.42346 0.42346 0.42346 0.00000  0.00000  0.00000  287 GLN   C C   
10889 O O   . GLN   G  287 ? 0.34199 0.34199 0.34199 -0.00000 0.00000  0.00000  287 GLN   C O   
10890 C CB  . GLN   G  287 ? 0.27608 0.27608 0.27608 0.00000  0.00000  0.00000  287 GLN   C CB  
10891 C CG  . GLN   G  287 ? 0.37626 0.37626 0.37626 0.00000  0.00000  0.00000  287 GLN   C CG  
10892 C CD  . GLN   G  287 ? 0.34156 0.34156 0.34156 0.00000  0.00000  0.00000  287 GLN   C CD  
10893 O OE1 . GLN   G  287 ? 0.36864 0.36864 0.36864 0.00000  0.00000  0.00000  287 GLN   C OE1 
10894 N NE2 . GLN   G  287 ? 0.29236 0.29236 0.29236 0.00000  0.00000  0.00000  287 GLN   C NE2 
10895 N N   . GLY   G  288 ? 0.37726 0.37726 0.37726 -0.00000 0.00000  0.00000  288 GLY   C N   
10896 C CA  . GLY   G  288 ? 0.27378 0.27378 0.27378 0.00000  0.00000  0.00000  288 GLY   C CA  
10897 C C   . GLY   G  288 ? 0.33226 0.33226 0.33226 -0.00000 0.00000  0.00000  288 GLY   C C   
10898 O O   . GLY   G  288 ? 0.52271 0.52271 0.52271 -0.00000 0.00000  0.00000  288 GLY   C O   
10899 N N   . PHE   G  289 ? 0.44513 0.44513 0.44513 0.00000  0.00000  0.00000  289 PHE   C N   
10900 C CA  . PHE   G  289 ? 0.52812 0.52812 0.52812 0.00000  0.00000  0.00000  289 PHE   C CA  
10901 C C   . PHE   G  289 ? 0.46860 0.46860 0.46860 0.00000  0.00000  0.00000  289 PHE   C C   
10902 O O   . PHE   G  289 ? 0.49891 0.49891 0.49891 0.00000  0.00000  0.00000  289 PHE   C O   
10903 C CB  . PHE   G  289 ? 0.38932 0.38932 0.38932 0.00000  0.00000  0.00000  289 PHE   C CB  
10904 C CG  . PHE   G  289 ? 0.46130 0.46130 0.46130 -0.00000 0.00000  0.00000  289 PHE   C CG  
10905 C CD1 . PHE   G  289 ? 0.31929 0.31929 0.31929 0.00000  -0.00000 0.00000  289 PHE   C CD1 
10906 C CD2 . PHE   G  289 ? 0.45422 0.45422 0.45422 -0.00000 0.00000  0.00000  289 PHE   C CD2 
10907 C CE1 . PHE   G  289 ? 0.55540 0.55540 0.55540 0.00000  0.00000  0.00000  289 PHE   C CE1 
10908 C CE2 . PHE   G  289 ? 0.49672 0.49672 0.49672 -0.00000 -0.00000 0.00000  289 PHE   C CE2 
10909 C CZ  . PHE   G  289 ? 0.47518 0.47518 0.47518 -0.00000 0.00000  0.00000  289 PHE   C CZ  
10910 N N   . LEU   G  290 ? 0.37316 0.37316 0.37316 0.00000  0.00000  0.00000  290 LEU   C N   
10911 C CA  . LEU   G  290 ? 0.36518 0.36518 0.36518 -0.00000 0.00000  0.00000  290 LEU   C CA  
10912 C C   . LEU   G  290 ? 0.42050 0.42050 0.42050 -0.00000 0.00000  0.00000  290 LEU   C C   
10913 O O   . LEU   G  290 ? 0.66907 0.66907 0.66907 0.00000  0.00000  0.00000  290 LEU   C O   
10914 C CB  . LEU   G  290 ? 0.27827 0.27827 0.27827 0.00000  0.00000  0.00000  290 LEU   C CB  
10915 C CG  . LEU   G  290 ? 0.37647 0.37647 0.37647 0.00000  0.00000  0.00000  290 LEU   C CG  
10916 C CD1 . LEU   G  290 ? 0.34667 0.34667 0.34667 0.00000  0.00000  0.00000  290 LEU   C CD1 
10917 C CD2 . LEU   G  290 ? 0.27603 0.27603 0.27603 0.00000  0.00000  0.00000  290 LEU   C CD2 
10918 N N   . ASN   G  291 ? 0.72050 0.72050 0.72050 0.00000  0.00000  0.00000  291 ASN   C N   
10919 C CA  . ASN   G  291 ? 0.56118 0.56118 0.56118 0.00000  0.00000  0.00000  291 ASN   C CA  
10920 C C   . ASN   G  291 ? 0.61843 0.61843 0.61843 -0.00000 0.00000  0.00000  291 ASN   C C   
10921 O O   . ASN   G  291 ? 0.61359 0.61359 0.61359 -0.00000 0.00000  0.00000  291 ASN   C O   
10922 C CB  . ASN   G  291 ? 0.90388 0.90388 0.90388 0.00000  0.00000  0.00000  291 ASN   C CB  
10923 C CG  . ASN   G  291 ? 1.04282 1.04282 1.04282 0.00000  0.00000  0.00000  291 ASN   C CG  
10924 O OD1 . ASN   G  291 ? 1.62291 1.62291 1.62291 -0.00000 0.00000  0.00000  291 ASN   C OD1 
10925 N ND2 . ASN   G  291 ? 1.05188 1.05188 1.05188 -0.00000 0.00000  0.00000  291 ASN   C ND2 
10926 N N   . VAL   G  292 ? 0.52369 0.52369 0.52369 0.00000  0.00000  0.00000  292 VAL   C N   
10927 C CA  . VAL   G  292 ? 0.87796 0.87796 0.87796 0.00000  0.00000  0.00000  292 VAL   C CA  
10928 C C   . VAL   G  292 ? 0.88734 0.88734 0.88734 0.00000  0.00000  0.00000  292 VAL   C C   
10929 O O   . VAL   G  292 ? 0.66412 0.66412 0.66412 -0.00000 0.00000  0.00000  292 VAL   C O   
10930 C CB  . VAL   G  292 ? 0.85668 0.85668 0.85668 -0.00000 0.00000  0.00000  292 VAL   C CB  
10931 C CG1 . VAL   G  292 ? 0.76623 0.76623 0.76623 0.00000  0.00000  0.00000  292 VAL   C CG1 
10932 C CG2 . VAL   G  292 ? 0.66389 0.66389 0.66389 -0.00000 0.00000  -0.00000 292 VAL   C CG2 
10933 N N   . THR   G  293 ? 0.55142 0.55142 0.55142 0.00000  0.00000  -0.00000 293 THR   C N   
10934 C CA  . THR   G  293 ? 0.63233 0.63233 0.63233 0.00000  0.00000  0.00000  293 THR   C CA  
10935 C C   . THR   G  293 ? 0.97761 0.97761 0.97761 0.00000  0.00000  0.00000  293 THR   C C   
10936 O O   . THR   G  293 ? 0.81613 0.81613 0.81613 0.00000  0.00000  0.00000  293 THR   C O   
10937 C CB  . THR   G  293 ? 0.94354 0.94354 0.94354 0.00000  0.00000  0.00000  293 THR   C CB  
10938 O OG1 . THR   G  293 ? 0.66520 0.66520 0.66520 0.00000  0.00000  0.00000  293 THR   C OG1 
10939 C CG2 . THR   G  293 ? 0.54709 0.54709 0.54709 -0.00000 0.00000  0.00000  293 THR   C CG2 
10940 N N   . ALA   G  294 ? 0.53460 0.53460 0.53460 -0.00000 0.00000  0.00000  294 ALA   C N   
10941 C CA  . ALA   G  294 ? 0.45046 0.45046 0.45046 0.00000  0.00000  0.00000  294 ALA   C CA  
10942 C C   . ALA   G  294 ? 0.44348 0.44348 0.44348 0.00000  0.00000  0.00000  294 ALA   C C   
10943 O O   . ALA   G  294 ? 0.66481 0.66481 0.66481 -0.00000 0.00000  0.00000  294 ALA   C O   
10944 C CB  . ALA   G  294 ? 0.42955 0.42955 0.42955 0.00000  0.00000  0.00000  294 ALA   C CB  
10945 N N   . TYR   G  295 ? 0.43732 0.43732 0.43732 0.00000  0.00000  0.00000  295 TYR   C N   
10946 C CA  . TYR   G  295 ? 0.53163 0.53163 0.53163 0.00000  0.00000  0.00000  295 TYR   C CA  
10947 C C   . TYR   G  295 ? 0.50538 0.50538 0.50538 -0.00000 -0.00000 0.00000  295 TYR   C C   
10948 O O   . TYR   G  295 ? 0.46643 0.46643 0.46643 0.00000  0.00000  0.00000  295 TYR   C O   
10949 C CB  . TYR   G  295 ? 0.19234 0.19234 0.19234 0.00000  0.00000  0.00000  295 TYR   C CB  
10950 C CG  . TYR   G  295 ? 0.56969 0.56969 0.56969 -0.00000 -0.00000 0.00000  295 TYR   C CG  
10951 C CD1 . TYR   G  295 ? 0.42093 0.42093 0.42093 -0.00000 0.00000  0.00000  295 TYR   C CD1 
10952 C CD2 . TYR   G  295 ? 0.36854 0.36854 0.36854 0.00000  0.00000  0.00000  295 TYR   C CD2 
10953 C CE1 . TYR   G  295 ? 0.33098 0.33098 0.33098 -0.00000 0.00000  0.00000  295 TYR   C CE1 
10954 C CE2 . TYR   G  295 ? 0.30594 0.30594 0.30594 0.00000  -0.00000 0.00000  295 TYR   C CE2 
10955 C CZ  . TYR   G  295 ? 0.48691 0.48691 0.48691 0.00000  0.00000  0.00000  295 TYR   C CZ  
10956 O OH  . TYR   G  295 ? 0.37300 0.37300 0.37300 0.00000  0.00000  0.00000  295 TYR   C OH  
10957 N N   . HIS   G  296 ? 0.40855 0.40855 0.40855 -0.00000 0.00000  0.00000  296 HIS   C N   
10958 C CA  . HIS   G  296 ? 0.51276 0.51276 0.51276 0.00000  0.00000  0.00000  296 HIS   C CA  
10959 C C   . HIS   G  296 ? 0.31757 0.31757 0.31757 0.00000  0.00000  0.00000  296 HIS   C C   
10960 O O   . HIS   G  296 ? 0.39230 0.39230 0.39230 0.00000  0.00000  0.00000  296 HIS   C O   
10961 C CB  . HIS   G  296 ? 0.37328 0.37328 0.37328 -0.00000 0.00000  0.00000  296 HIS   C CB  
10962 C CG  . HIS   G  296 ? 0.49858 0.49858 0.49858 0.00000  0.00000  0.00000  296 HIS   C CG  
10963 N ND1 . HIS   G  296 ? 0.59757 0.59757 0.59757 0.00000  0.00000  0.00000  296 HIS   C ND1 
10964 C CD2 . HIS   G  296 ? 0.49157 0.49157 0.49157 0.00000  0.00000  0.00000  296 HIS   C CD2 
10965 C CE1 . HIS   G  296 ? 0.49666 0.49666 0.49666 -0.00000 0.00000  0.00000  296 HIS   C CE1 
10966 N NE2 . HIS   G  296 ? 0.67279 0.67279 0.67279 0.00000  0.00000  0.00000  296 HIS   C NE2 
10967 N N   . ARG   G  297 ? 0.38943 0.38943 0.38943 -0.00000 0.00000  0.00000  297 ARG   C N   
10968 C CA  . ARG   G  297 ? 0.33149 0.33149 0.33149 0.00000  0.00000  0.00000  297 ARG   C CA  
10969 C C   . ARG   G  297 ? 0.54651 0.54651 0.54651 -0.00000 0.00000  0.00000  297 ARG   C C   
10970 O O   . ARG   G  297 ? 0.41537 0.41537 0.41537 0.00000  0.00000  0.00000  297 ARG   C O   
10971 C CB  . ARG   G  297 ? 0.38064 0.38064 0.38064 0.00000  0.00000  0.00000  297 ARG   C CB  
10972 C CG  . ARG   G  297 ? 0.44421 0.44421 0.44421 0.00000  0.00000  0.00000  297 ARG   C CG  
10973 C CD  . ARG   G  297 ? 0.40449 0.40449 0.40449 0.00000  0.00000  0.00000  297 ARG   C CD  
10974 N NE  . ARG   G  297 ? 0.62622 0.62622 0.62622 0.00000  0.00000  0.00000  297 ARG   C NE  
10975 C CZ  . ARG   G  297 ? 0.52896 0.52896 0.52896 0.00000  0.00000  0.00000  297 ARG   C CZ  
10976 N NH1 . ARG   G  297 ? 0.63503 0.63503 0.63503 -0.00000 0.00000  0.00000  297 ARG   C NH1 
10977 N NH2 . ARG   G  297 ? 1.08213 1.08213 1.08213 0.00000  0.00000  -0.00000 297 ARG   C NH2 
10978 N N   . TRP   G  298 ? 0.43361 0.43361 0.43361 0.00000  0.00000  0.00000  298 TRP   C N   
10979 C CA  . TRP   G  298 ? 0.40636 0.40636 0.40636 -0.00000 0.00000  0.00000  298 TRP   C CA  
10980 C C   . TRP   G  298 ? 0.50667 0.50667 0.50667 0.00000  0.00000  0.00000  298 TRP   C C   
10981 O O   . TRP   G  298 ? 0.55780 0.55780 0.55780 0.00000  0.00000  0.00000  298 TRP   C O   
10982 C CB  . TRP   G  298 ? 0.33264 0.33264 0.33264 -0.00000 0.00000  0.00000  298 TRP   C CB  
10983 C CG  . TRP   G  298 ? 0.46855 0.46855 0.46855 0.00000  0.00000  0.00000  298 TRP   C CG  
10984 C CD1 . TRP   G  298 ? 0.40865 0.40865 0.40865 0.00000  0.00000  0.00000  298 TRP   C CD1 
10985 C CD2 . TRP   G  298 ? 0.33408 0.33408 0.33408 0.00000  0.00000  0.00000  298 TRP   C CD2 
10986 N NE1 . TRP   G  298 ? 0.29984 0.29984 0.29984 0.00000  0.00000  0.00000  298 TRP   C NE1 
10987 C CE2 . TRP   G  298 ? 0.37961 0.37961 0.37961 0.00000  0.00000  0.00000  298 TRP   C CE2 
10988 C CE3 . TRP   G  298 ? 0.24622 0.24622 0.24622 -0.00000 0.00000  0.00000  298 TRP   C CE3 
10989 C CZ2 . TRP   G  298 ? 0.44452 0.44452 0.44452 0.00000  0.00000  0.00000  298 TRP   C CZ2 
10990 C CZ3 . TRP   G  298 ? 0.52363 0.52363 0.52363 0.00000  -0.00000 0.00000  298 TRP   C CZ3 
10991 C CH2 . TRP   G  298 ? 0.41668 0.41668 0.41668 -0.00000 0.00000  0.00000  298 TRP   C CH2 
10992 N N   . HIS   G  299 ? 0.47181 0.47181 0.47181 0.00000  0.00000  0.00000  299 HIS   C N   
10993 C CA  . HIS   G  299 ? 0.58425 0.58425 0.58425 -0.00000 0.00000  0.00000  299 HIS   C CA  
10994 C C   . HIS   G  299 ? 0.45957 0.45957 0.45957 0.00000  0.00000  0.00000  299 HIS   C C   
10995 O O   . HIS   G  299 ? 0.48608 0.48608 0.48608 -0.00000 0.00000  0.00000  299 HIS   C O   
10996 C CB  . HIS   G  299 ? 0.32249 0.32249 0.32249 0.00000  0.00000  -0.00000 299 HIS   C CB  
10997 C CG  . HIS   G  299 ? 0.53677 0.53677 0.53677 -0.00000 0.00000  0.00000  299 HIS   C CG  
10998 N ND1 . HIS   G  299 ? 0.44868 0.44868 0.44868 0.00000  0.00000  0.00000  299 HIS   C ND1 
10999 C CD2 . HIS   G  299 ? 0.45250 0.45250 0.45250 -0.00000 0.00000  0.00000  299 HIS   C CD2 
11000 C CE1 . HIS   G  299 ? 0.62258 0.62258 0.62258 0.00000  0.00000  0.00000  299 HIS   C CE1 
11001 N NE2 . HIS   G  299 ? 0.47517 0.47517 0.47517 0.00000  0.00000  0.00000  299 HIS   C NE2 
11002 N N   . ALA   G  300 ? 0.41668 0.41668 0.41668 -0.00000 0.00000  0.00000  300 ALA   C N   
11003 C CA  . ALA   G  300 ? 0.48046 0.48046 0.48046 0.00000  0.00000  0.00000  300 ALA   C CA  
11004 C C   . ALA   G  300 ? 0.39161 0.39161 0.39161 0.00000  0.00000  0.00000  300 ALA   C C   
11005 O O   . ALA   G  300 ? 0.52079 0.52079 0.52079 0.00000  0.00000  0.00000  300 ALA   C O   
11006 C CB  . ALA   G  300 ? 0.33531 0.33531 0.33531 0.00000  0.00000  0.00000  300 ALA   C CB  
11007 N N   . PRO   G  301 ? 0.50670 0.50670 0.50670 -0.00000 0.00000  0.00000  301 PRO   C N   
11008 C CA  . PRO   G  301 ? 0.32738 0.32738 0.32738 0.00000  0.00000  0.00000  301 PRO   C CA  
11009 C C   . PRO   G  301 ? 0.59064 0.59064 0.59064 0.00000  0.00000  0.00000  301 PRO   C C   
11010 O O   . PRO   G  301 ? 0.39306 0.39306 0.39306 0.00000  0.00000  0.00000  301 PRO   C O   
11011 C CB  . PRO   G  301 ? 0.44007 0.44007 0.44007 0.00000  0.00000  0.00000  301 PRO   C CB  
11012 C CG  . PRO   G  301 ? 0.40523 0.40523 0.40523 0.00000  0.00000  0.00000  301 PRO   C CG  
11013 C CD  . PRO   G  301 ? 0.21918 0.21918 0.21918 0.00000  0.00000  0.00000  301 PRO   C CD  
11014 N N   . VAL   G  302 ? 0.33925 0.33925 0.33925 -0.00000 0.00000  0.00000  302 VAL   C N   
11015 C CA  . VAL   G  302 ? 0.65375 0.65375 0.65375 0.00000  0.00000  0.00000  302 VAL   C CA  
11016 C C   . VAL   G  302 ? 0.32969 0.32969 0.32969 0.00000  0.00000  0.00000  302 VAL   C C   
11017 O O   . VAL   G  302 ? 0.54084 0.54084 0.54084 0.00000  0.00000  0.00000  302 VAL   C O   
11018 C CB  . VAL   G  302 ? 0.32662 0.32662 0.32662 -0.00000 0.00000  0.00000  302 VAL   C CB  
11019 C CG1 . VAL   G  302 ? 0.63397 0.63397 0.63397 -0.00000 0.00000  0.00000  302 VAL   C CG1 
11020 C CG2 . VAL   G  302 ? 0.31000 0.31000 0.31000 0.00000  0.00000  0.00000  302 VAL   C CG2 
11021 N N   . ASN   G  303 ? 0.63691 0.63691 0.63691 -0.00000 0.00000  0.00000  303 ASN   C N   
11022 C CA  . ASN   G  303 ? 0.44531 0.44531 0.44531 -0.00000 0.00000  0.00000  303 ASN   C CA  
11023 C C   . ASN   G  303 ? 0.68978 0.68978 0.68978 0.00000  0.00000  0.00000  303 ASN   C C   
11024 O O   . ASN   G  303 ? 0.63281 0.63281 0.63281 0.00000  -0.00000 0.00000  303 ASN   C O   
11025 C CB  . ASN   G  303 ? 0.68375 0.68375 0.68375 -0.00000 0.00000  0.00000  303 ASN   C CB  
11026 C CG  . ASN   G  303 ? 0.59179 0.59179 0.59179 -0.00000 0.00000  0.00000  303 ASN   C CG  
11027 O OD1 . ASN   G  303 ? 0.65141 0.65141 0.65141 -0.00000 0.00000  0.00000  303 ASN   C OD1 
11028 N ND2 . ASN   G  303 ? 0.62675 0.62675 0.62675 0.00000  0.00000  0.00000  303 ASN   C ND2 
11029 N N   . GLY   G  304 ? 0.53067 0.53067 0.53067 -0.00000 0.00000  0.00000  304 GLY   C N   
11030 C CA  . GLY   G  304 ? 0.36314 0.36314 0.36314 0.00000  0.00000  0.00000  304 GLY   C CA  
11031 C C   . GLY   G  304 ? 0.57245 0.57245 0.57245 0.00000  0.00000  0.00000  304 GLY   C C   
11032 O O   . GLY   G  304 ? 0.60811 0.60811 0.60811 0.00000  0.00000  0.00000  304 GLY   C O   
11033 N N   . THR   G  305 ? 0.50636 0.50636 0.50636 0.00000  0.00000  0.00000  305 THR   C N   
11034 C CA  . THR   G  305 ? 0.52281 0.52281 0.52281 0.00000  0.00000  0.00000  305 THR   C CA  
11035 C C   . THR   G  305 ? 0.80058 0.80058 0.80058 0.00000  0.00000  0.00000  305 THR   C C   
11036 O O   . THR   G  305 ? 0.35570 0.35570 0.35570 0.00000  0.00000  0.00000  305 THR   C O   
11037 C CB  . THR   G  305 ? 0.39134 0.39134 0.39134 0.00000  0.00000  0.00000  305 THR   C CB  
11038 O OG1 . THR   G  305 ? 0.60755 0.60755 0.60755 -0.00000 -0.00000 0.00000  305 THR   C OG1 
11039 C CG2 . THR   G  305 ? 0.38864 0.38864 0.38864 -0.00000 0.00000  0.00000  305 THR   C CG2 
11040 N N   . ILE   G  306 ? 0.38108 0.38108 0.38108 0.00000  0.00000  0.00000  306 ILE   C N   
11041 C CA  . ILE   G  306 ? 0.54351 0.54351 0.54351 0.00000  -0.00000 0.00000  306 ILE   C CA  
11042 C C   . ILE   G  306 ? 0.55161 0.55161 0.55161 0.00000  0.00000  0.00000  306 ILE   C C   
11043 O O   . ILE   G  306 ? 0.59031 0.59031 0.59031 -0.00000 0.00000  0.00000  306 ILE   C O   
11044 C CB  . ILE   G  306 ? 0.49626 0.49626 0.49626 -0.00000 0.00000  0.00000  306 ILE   C CB  
11045 C CG1 . ILE   G  306 ? 0.33671 0.33671 0.33671 0.00000  0.00000  0.00000  306 ILE   C CG1 
11046 C CG2 . ILE   G  306 ? 0.44172 0.44172 0.44172 -0.00000 0.00000  0.00000  306 ILE   C CG2 
11047 C CD1 . ILE   G  306 ? 0.42230 0.42230 0.42230 0.00000  0.00000  0.00000  306 ILE   C CD1 
11048 N N   . VAL   G  307 ? 0.47194 0.47194 0.47194 -0.00000 0.00000  0.00000  307 VAL   C N   
11049 C CA  . VAL   G  307 ? 0.39449 0.39449 0.39449 0.00000  0.00000  0.00000  307 VAL   C CA  
11050 C C   . VAL   G  307 ? 0.50490 0.50490 0.50490 0.00000  0.00000  0.00000  307 VAL   C C   
11051 O O   . VAL   G  307 ? 0.48594 0.48594 0.48594 0.00000  0.00000  0.00000  307 VAL   C O   
11052 C CB  . VAL   G  307 ? 0.59615 0.59615 0.59615 0.00000  0.00000  0.00000  307 VAL   C CB  
11053 C CG1 . VAL   G  307 ? 0.26654 0.26654 0.26654 -0.00000 0.00000  0.00000  307 VAL   C CG1 
11054 C CG2 . VAL   G  307 ? 0.40676 0.40676 0.40676 0.00000  0.00000  0.00000  307 VAL   C CG2 
11055 N N   . LYS   G  308 ? 0.54873 0.54873 0.54873 0.00000  0.00000  0.00000  308 LYS   C N   
11056 C CA  . LYS   G  308 ? 0.42992 0.42992 0.42992 0.00000  0.00000  0.00000  308 LYS   C CA  
11057 C C   . LYS   G  308 ? 0.60120 0.60120 0.60120 0.00000  0.00000  0.00000  308 LYS   C C   
11058 O O   . LYS   G  308 ? 0.38805 0.38805 0.38805 0.00000  0.00000  0.00000  308 LYS   C O   
11059 C CB  . LYS   G  308 ? 0.38960 0.38960 0.38960 0.00000  0.00000  0.00000  308 LYS   C CB  
11060 C CG  . LYS   G  308 ? 0.27993 0.27993 0.27993 0.00000  -0.00000 0.00000  308 LYS   C CG  
11061 C CD  . LYS   G  308 ? 0.41744 0.41744 0.41744 0.00000  0.00000  0.00000  308 LYS   C CD  
11062 C CE  . LYS   G  308 ? 0.67002 0.67002 0.67002 0.00000  0.00000  0.00000  308 LYS   C CE  
11063 N NZ  . LYS   G  308 ? 0.81752 0.81752 0.81752 -0.00000 0.00000  0.00000  308 LYS   C NZ  
11064 N N   . ILE   G  309 ? 0.38416 0.38416 0.38416 -0.00000 0.00000  0.00000  309 ILE   C N   
11065 C CA  . ILE   G  309 ? 0.47381 0.47381 0.47381 0.00000  0.00000  0.00000  309 ILE   C CA  
11066 C C   . ILE   G  309 ? 0.37816 0.37816 0.37816 0.00000  0.00000  0.00000  309 ILE   C C   
11067 O O   . ILE   G  309 ? 0.48677 0.48677 0.48677 -0.00000 0.00000  0.00000  309 ILE   C O   
11068 C CB  . ILE   G  309 ? 0.27688 0.27688 0.27688 0.00000  0.00000  0.00000  309 ILE   C CB  
11069 C CG1 . ILE   G  309 ? 0.53892 0.53892 0.53892 -0.00000 0.00000  0.00000  309 ILE   C CG1 
11070 C CG2 . ILE   G  309 ? 0.31050 0.31050 0.31050 0.00000  0.00000  0.00000  309 ILE   C CG2 
11071 C CD1 . ILE   G  309 ? 0.29445 0.29445 0.29445 0.00000  0.00000  0.00000  309 ILE   C CD1 
11072 N N   . ILE   G  310 ? 0.43069 0.43069 0.43069 0.00000  0.00000  0.00000  310 ILE   C N   
11073 C CA  . ILE   G  310 ? 0.22651 0.22651 0.22651 0.00000  0.00000  0.00000  310 ILE   C CA  
11074 C C   . ILE   G  310 ? 0.44703 0.44703 0.44703 0.00000  0.00000  0.00000  310 ILE   C C   
11075 O O   . ILE   G  310 ? 0.35830 0.35830 0.35830 -0.00000 0.00000  0.00000  310 ILE   C O   
11076 C CB  . ILE   G  310 ? 0.44674 0.44674 0.44674 0.00000  0.00000  0.00000  310 ILE   C CB  
11077 C CG1 . ILE   G  310 ? 0.46056 0.46056 0.46056 0.00000  0.00000  0.00000  310 ILE   C CG1 
11078 C CG2 . ILE   G  310 ? 0.28762 0.28762 0.28762 -0.00000 0.00000  0.00000  310 ILE   C CG2 
11079 C CD1 . ILE   G  310 ? 0.51592 0.51592 0.51592 -0.00000 0.00000  0.00000  310 ILE   C CD1 
11080 N N   . ASN   G  311 ? 0.44059 0.44059 0.44059 -0.00000 0.00000  0.00000  311 ASN   C N   
11081 C CA  . ASN   G  311 ? 0.40022 0.40022 0.40022 0.00000  0.00000  0.00000  311 ASN   C CA  
11082 C C   . ASN   G  311 ? 0.26542 0.26542 0.26542 0.00000  0.00000  0.00000  311 ASN   C C   
11083 O O   . ASN   G  311 ? 0.60755 0.60755 0.60755 0.00000  0.00000  0.00000  311 ASN   C O   
11084 C CB  . ASN   G  311 ? 0.20714 0.20714 0.20714 0.00000  0.00000  0.00000  311 ASN   C CB  
11085 C CG  . ASN   G  311 ? 0.78623 0.78623 0.78623 -0.00000 0.00000  0.00000  311 ASN   C CG  
11086 O OD1 . ASN   G  311 ? 0.53281 0.53281 0.53281 0.00000  0.00000  0.00000  311 ASN   C OD1 
11087 N ND2 . ASN   G  311 ? 0.56072 0.56072 0.56072 0.00000  0.00000  0.00000  311 ASN   C ND2 
11088 N N   . VAL   G  312 ? 0.36468 0.36468 0.36468 -0.00000 0.00000  0.00000  312 VAL   C N   
11089 C CA  . VAL   G  312 ? 0.34500 0.34500 0.34500 0.00000  0.00000  0.00000  312 VAL   C CA  
11090 C C   . VAL   G  312 ? 0.33038 0.33038 0.33038 0.00000  0.00000  0.00000  312 VAL   C C   
11091 O O   . VAL   G  312 ? 0.64578 0.64578 0.64578 0.00000  0.00000  0.00000  312 VAL   C O   
11092 C CB  . VAL   G  312 ? 0.39016 0.39016 0.39016 0.00000  0.00000  0.00000  312 VAL   C CB  
11093 C CG1 . VAL   G  312 ? 0.21661 0.21661 0.21661 -0.00000 0.00000  0.00000  312 VAL   C CG1 
11094 C CG2 . VAL   G  312 ? 0.29765 0.29765 0.29765 0.00000  0.00000  0.00000  312 VAL   C CG2 
11095 N N   . PRO   G  313 ? 0.46684 0.46684 0.46684 0.00000  0.00000  0.00000  313 PRO   C N   
11096 C CA  . PRO   G  313 ? 0.41216 0.41216 0.41216 0.00000  0.00000  0.00000  313 PRO   C CA  
11097 C C   . PRO   G  313 ? 0.45877 0.45877 0.45877 -0.00000 0.00000  0.00000  313 PRO   C C   
11098 O O   . PRO   G  313 ? 0.39846 0.39846 0.39846 0.00000  0.00000  0.00000  313 PRO   C O   
11099 C CB  . PRO   G  313 ? 0.19735 0.19735 0.19735 0.00000  0.00000  0.00000  313 PRO   C CB  
11100 C CG  . PRO   G  313 ? 0.27142 0.27142 0.27142 0.00000  -0.00000 0.00000  313 PRO   C CG  
11101 C CD  . PRO   G  313 ? 0.22293 0.22293 0.22293 0.00000  0.00000  0.00000  313 PRO   C CD  
11102 N N   . GLY   G  314 ? 0.32362 0.32362 0.32362 -0.00000 0.00000  0.00000  314 GLY   C N   
11103 C CA  . GLY   G  314 ? 0.22815 0.22815 0.22815 0.00000  0.00000  0.00000  314 GLY   C CA  
11104 C C   . GLY   G  314 ? 0.44298 0.44298 0.44298 -0.00000 0.00000  0.00000  314 GLY   C C   
11105 O O   . GLY   G  314 ? 0.33218 0.33218 0.33218 -0.00000 0.00000  0.00000  314 GLY   C O   
11106 N N   . THR   G  315 ? 0.29709 0.29709 0.29709 -0.00000 0.00000  0.00000  315 THR   C N   
11107 C CA  . THR   G  315 ? 0.32688 0.32688 0.32688 0.00000  0.00000  0.00000  315 THR   C CA  
11108 C C   . THR   G  315 ? 0.43238 0.43238 0.43238 -0.00000 0.00000  0.00000  315 THR   C C   
11109 O O   . THR   G  315 ? 0.33338 0.33338 0.33338 0.00000  0.00000  0.00000  315 THR   C O   
11110 C CB  . THR   G  315 ? 0.32209 0.32209 0.32209 -0.00000 0.00000  0.00000  315 THR   C CB  
11111 O OG1 . THR   G  315 ? 0.24331 0.24331 0.24331 0.00000  0.00000  0.00000  315 THR   C OG1 
11112 C CG2 . THR   G  315 ? 0.20167 0.20167 0.20167 0.00000  0.00000  0.00000  315 THR   C CG2 
11113 N N   . TYR   G  316 ? 0.35714 0.35714 0.35714 0.00000  0.00000  0.00000  316 TYR   C N   
11114 C CA  . TYR   G  316 ? 0.35156 0.35156 0.35156 -0.00000 0.00000  0.00000  316 TYR   C CA  
11115 C C   . TYR   G  316 ? 0.28855 0.28855 0.28855 0.00000  0.00000  0.00000  316 TYR   C C   
11116 O O   . TYR   G  316 ? 0.41346 0.41346 0.41346 -0.00000 0.00000  0.00000  316 TYR   C O   
11117 C CB  . TYR   G  316 ? 0.28755 0.28755 0.28755 0.00000  0.00000  0.00000  316 TYR   C CB  
11118 C CG  . TYR   G  316 ? 0.42365 0.42365 0.42365 0.00000  0.00000  0.00000  316 TYR   C CG  
11119 C CD1 . TYR   G  316 ? 0.44112 0.44112 0.44112 -0.00000 0.00000  0.00000  316 TYR   C CD1 
11120 C CD2 . TYR   G  316 ? 0.34891 0.34891 0.34891 0.00000  0.00000  0.00000  316 TYR   C CD2 
11121 C CE1 . TYR   G  316 ? 0.33522 0.33522 0.33522 -0.00000 0.00000  0.00000  316 TYR   C CE1 
11122 C CE2 . TYR   G  316 ? 0.24997 0.24997 0.24997 0.00000  0.00000  0.00000  316 TYR   C CE2 
11123 C CZ  . TYR   G  316 ? 0.47521 0.47521 0.47521 0.00000  0.00000  0.00000  316 TYR   C CZ  
11124 O OH  . TYR   G  316 ? 0.36469 0.36469 0.36469 -0.00000 0.00000  0.00000  316 TYR   C OH  
11125 N N   . PHE   G  317 ? 0.55672 0.55672 0.55672 0.00000  0.00000  0.00000  317 PHE   C N   
11126 C CA  . PHE   G  317 ? 0.31925 0.31925 0.31925 -0.00000 0.00000  0.00000  317 PHE   C CA  
11127 C C   . PHE   G  317 ? 0.59370 0.59370 0.59370 -0.00000 0.00000  0.00000  317 PHE   C C   
11128 O O   . PHE   G  317 ? 0.44085 0.44085 0.44085 0.00000  0.00000  0.00000  317 PHE   C O   
11129 C CB  . PHE   G  317 ? 0.31772 0.31772 0.31772 -0.00000 0.00000  0.00000  317 PHE   C CB  
11130 C CG  . PHE   G  317 ? 0.57283 0.57283 0.57283 0.00000  0.00000  0.00000  317 PHE   C CG  
11131 C CD1 . PHE   G  317 ? 0.32786 0.32786 0.32786 0.00000  0.00000  0.00000  317 PHE   C CD1 
11132 C CD2 . PHE   G  317 ? 0.51918 0.51918 0.51918 0.00000  0.00000  0.00000  317 PHE   C CD2 
11133 C CE1 . PHE   G  317 ? 0.52175 0.52175 0.52175 -0.00000 0.00000  0.00000  317 PHE   C CE1 
11134 C CE2 . PHE   G  317 ? 0.42789 0.42789 0.42789 0.00000  0.00000  0.00000  317 PHE   C CE2 
11135 C CZ  . PHE   G  317 ? 0.44571 0.44571 0.44571 0.00000  0.00000  0.00000  317 PHE   C CZ  
11136 N N   . ALA   G  318 ? 0.39389 0.39389 0.39389 0.00000  0.00000  0.00000  318 ALA   C N   
11137 C CA  . ALA   G  318 ? 0.35432 0.35432 0.35432 -0.00000 0.00000  0.00000  318 ALA   C CA  
11138 C C   . ALA   G  318 ? 0.41531 0.41531 0.41531 -0.00000 0.00000  0.00000  318 ALA   C C   
11139 O O   . ALA   G  318 ? 0.47758 0.47758 0.47758 -0.00000 0.00000  0.00000  318 ALA   C O   
11140 C CB  . ALA   G  318 ? 0.27227 0.27227 0.27227 -0.00000 0.00000  0.00000  318 ALA   C CB  
11141 N N   . GLN   G  319 ? 0.47366 0.47366 0.47366 -0.00000 0.00000  0.00000  319 GLN   C N   
11142 C CA  . GLN   G  319 ? 0.42909 0.42909 0.42909 0.00000  0.00000  0.00000  319 GLN   C CA  
11143 C C   . GLN   G  319 ? 0.40497 0.40497 0.40497 0.00000  0.00000  -0.00000 319 GLN   C C   
11144 O O   . GLN   G  319 ? 0.58574 0.58574 0.58574 0.00000  0.00000  0.00000  319 GLN   C O   
11145 C CB  . GLN   G  319 ? 0.42258 0.42258 0.42258 0.00000  0.00000  0.00000  319 GLN   C CB  
11146 C CG  . GLN   G  319 ? 0.52520 0.52520 0.52520 0.00000  0.00000  0.00000  319 GLN   C CG  
11147 C CD  . GLN   G  319 ? 0.38604 0.38604 0.38604 0.00000  0.00000  0.00000  319 GLN   C CD  
11148 O OE1 . GLN   G  319 ? 0.68140 0.68140 0.68140 0.00000  0.00000  0.00000  319 GLN   C OE1 
11149 N NE2 . GLN   G  319 ? 0.49759 0.49759 0.49759 0.00000  0.00000  0.00000  319 GLN   C NE2 
11150 N N   . ALA   G  320 ? 0.48107 0.48107 0.48107 -0.00000 0.00000  0.00000  320 ALA   C N   
11151 C CA  . ALA   G  320 ? 0.49051 0.49051 0.49051 -0.00000 0.00000  0.00000  320 ALA   C CA  
11152 C C   . ALA   G  320 ? 0.48726 0.48726 0.48726 0.00000  0.00000  0.00000  320 ALA   C C   
11153 O O   . ALA   G  320 ? 0.50674 0.50674 0.50674 0.00000  0.00000  0.00000  320 ALA   C O   
11154 C CB  . ALA   G  320 ? 0.28461 0.28461 0.28461 -0.00000 0.00000  0.00000  320 ALA   C CB  
11155 N N   . PRO   G  321 ? 0.58679 0.58679 0.58679 0.00000  0.00000  0.00000  321 PRO   C N   
11156 C CA  . PRO   G  321 ? 0.40820 0.40820 0.40820 -0.00000 0.00000  0.00000  321 PRO   C CA  
11157 C C   . PRO   G  321 ? 0.48021 0.48021 0.48021 0.00000  0.00000  0.00000  321 PRO   C C   
11158 O O   . PRO   G  321 ? 0.54057 0.54057 0.54057 0.00000  0.00000  0.00000  321 PRO   C O   
11159 C CB  . PRO   G  321 ? 0.32204 0.32204 0.32204 -0.00000 0.00000  0.00000  321 PRO   C CB  
11160 C CG  . PRO   G  321 ? 0.59003 0.59003 0.59003 0.00000  0.00000  0.00000  321 PRO   C CG  
11161 C CD  . PRO   G  321 ? 0.36573 0.36573 0.36573 0.00000  0.00000  0.00000  321 PRO   C CD  
11162 N N   . SER   G  322 ? 0.56819 0.56819 0.56819 0.00000  0.00000  0.00000  322 SER   C N   
11163 C CA  . SER   G  322 ? 0.56164 0.56164 0.56164 0.00000  0.00000  0.00000  322 SER   C CA  
11164 C C   . SER   G  322 ? 0.55662 0.55662 0.55662 0.00000  0.00000  0.00000  322 SER   C C   
11165 O O   . SER   G  322 ? 0.80207 0.80207 0.80207 0.00000  0.00000  0.00000  322 SER   C O   
11166 C CB  . SER   G  322 ? 0.44846 0.44846 0.44846 0.00000  0.00000  0.00000  322 SER   C CB  
11167 O OG  . SER   G  322 ? 0.76626 0.76626 0.76626 0.00000  0.00000  0.00000  322 SER   C OG  
11168 N N   . THR   G  323 ? 0.69880 0.69880 0.69880 0.00000  0.00000  0.00000  323 THR   C N   
11169 C CA  . THR   G  323 ? 0.47519 0.47519 0.47519 0.00000  0.00000  0.00000  323 THR   C CA  
11170 C C   . THR   G  323 ? 0.67118 0.67118 0.67118 0.00000  -0.00000 0.00000  323 THR   C C   
11171 O O   . THR   G  323 ? 0.45475 0.45475 0.45475 0.00000  0.00000  0.00000  323 THR   C O   
11172 C CB  . THR   G  323 ? 0.56048 0.56048 0.56048 0.00000  0.00000  0.00000  323 THR   C CB  
11173 O OG1 . THR   G  323 ? 0.57993 0.57993 0.57993 0.00000  0.00000  0.00000  323 THR   C OG1 
11174 C CG2 . THR   G  323 ? 0.33188 0.33188 0.33188 -0.00000 0.00000  0.00000  323 THR   C CG2 
11175 N N   . ILE   G  324 ? 0.52485 0.52485 0.52485 0.00000  0.00000  0.00000  324 ILE   C N   
11176 C CA  . ILE   G  324 ? 0.54696 0.54696 0.54696 0.00000  0.00000  0.00000  324 ILE   C CA  
11177 C C   . ILE   G  324 ? 0.78189 0.78189 0.78189 0.00000  0.00000  0.00000  324 ILE   C C   
11178 O O   . ILE   G  324 ? 0.68906 0.68906 0.68906 0.00000  0.00000  0.00000  324 ILE   C O   
11179 C CB  . ILE   G  324 ? 0.39510 0.39510 0.39510 0.00000  -0.00000 0.00000  324 ILE   C CB  
11180 C CG1 . ILE   G  324 ? 0.56454 0.56454 0.56454 0.00000  0.00000  0.00000  324 ILE   C CG1 
11181 C CG2 . ILE   G  324 ? 0.42730 0.42730 0.42730 0.00000  0.00000  0.00000  324 ILE   C CG2 
11182 C CD1 . ILE   G  324 ? 0.48225 0.48225 0.48225 0.00000  0.00000  0.00000  324 ILE   C CD1 
11183 N N   . GLY   G  325 ? 0.54547 0.54547 0.54547 -0.00000 0.00000  0.00000  325 GLY   C N   
11184 C CA  . GLY   G  325 ? 0.48493 0.48493 0.48493 -0.00000 0.00000  0.00000  325 GLY   C CA  
11185 C C   . GLY   G  325 ? 0.59931 0.59931 0.59931 -0.00000 0.00000  0.00000  325 GLY   C C   
11186 O O   . GLY   G  325 ? 0.66480 0.66480 0.66480 -0.00000 0.00000  0.00000  325 GLY   C O   
11187 N N   . ASP   G  326 ? 0.57730 0.57730 0.57730 -0.00000 0.00000  0.00000  326 ASP   C N   
11188 C CA  . ASP   G  326 ? 0.66854 0.66854 0.66854 0.00000  -0.00000 0.00000  326 ASP   C CA  
11189 C C   . ASP   G  326 ? 0.55677 0.55677 0.55677 -0.00000 0.00000  0.00000  326 ASP   C C   
11190 O O   . ASP   G  326 ? 0.68808 0.68808 0.68808 -0.00000 0.00000  0.00000  326 ASP   C O   
11191 C CB  . ASP   G  326 ? 0.44604 0.44604 0.44604 0.00000  0.00000  0.00000  326 ASP   C CB  
11192 C CG  . ASP   G  326 ? 0.91051 0.91051 0.91051 -0.00000 0.00000  0.00000  326 ASP   C CG  
11193 O OD1 . ASP   G  326 ? 0.72814 0.72814 0.72814 0.00000  0.00000  0.00000  326 ASP   C OD1 
11194 O OD2 . ASP   G  326 ? 0.76099 0.76099 0.76099 0.00000  0.00000  0.00000  326 ASP   C OD2 
11195 N N   . PRO   G  327 ? 0.92040 0.92040 0.92040 0.00000  0.00000  0.00000  327 PRO   C N   
11196 C CA  . PRO   G  327 ? 0.73622 0.73622 0.73622 -0.00000 0.00000  0.00000  327 PRO   C CA  
11197 C C   . PRO   G  327 ? 0.66932 0.66932 0.66932 -0.00000 0.00000  -0.00000 327 PRO   C C   
11198 O O   . PRO   G  327 ? 0.83375 0.83375 0.83375 0.00000  0.00000  0.00000  327 PRO   C O   
11199 C CB  . PRO   G  327 ? 0.48153 0.48153 0.48153 0.00000  0.00000  0.00000  327 PRO   C CB  
11200 C CG  . PRO   G  327 ? 0.66732 0.66732 0.66732 -0.00000 0.00000  0.00000  327 PRO   C CG  
11201 C CD  . PRO   G  327 ? 0.70424 0.70424 0.70424 -0.00000 0.00000  0.00000  327 PRO   C CD  
11202 N N   . ILE   G  328 ? 0.61794 0.61794 0.61794 0.00000  0.00000  0.00000  328 ILE   C N   
11203 C CA  . ILE   G  328 ? 0.61540 0.61540 0.61540 0.00000  0.00000  0.00000  328 ILE   C CA  
11204 C C   . ILE   G  328 ? 0.64448 0.64448 0.64448 -0.00000 0.00000  0.00000  328 ILE   C C   
11205 O O   . ILE   G  328 ? 0.75898 0.75898 0.75898 0.00000  -0.00000 -0.00000 328 ILE   C O   
11206 C CB  . ILE   G  328 ? 0.68158 0.68158 0.68158 -0.00000 0.00000  0.00000  328 ILE   C CB  
11207 C CG1 . ILE   G  328 ? 0.52271 0.52271 0.52271 0.00000  0.00000  0.00000  328 ILE   C CG1 
11208 C CG2 . ILE   G  328 ? 0.54455 0.54455 0.54455 0.00000  0.00000  0.00000  328 ILE   C CG2 
11209 C CD1 . ILE   G  328 ? 0.47217 0.47217 0.47217 -0.00000 0.00000  0.00000  328 ILE   C CD1 
11210 N N   . PRO   G  329 ? 0.84987 0.84987 0.84987 0.00000  0.00000  0.00000  329 PRO   C N   
11211 C CA  . PRO   G  329 ? 0.66587 0.66587 0.66587 -0.00000 0.00000  0.00000  329 PRO   C CA  
11212 C C   . PRO   G  329 ? 0.69440 0.69440 0.69440 0.00000  0.00000  0.00000  329 PRO   C C   
11213 O O   . PRO   G  329 ? 1.10413 1.10413 1.10413 -0.00000 0.00000  0.00000  329 PRO   C O   
11214 C CB  . PRO   G  329 ? 0.49946 0.49946 0.49946 0.00000  0.00000  -0.00000 329 PRO   C CB  
11215 C CG  . PRO   G  329 ? 0.63508 0.63508 0.63508 -0.00000 0.00000  0.00000  329 PRO   C CG  
11216 C CD  . PRO   G  329 ? 0.69703 0.69703 0.69703 -0.00000 0.00000  0.00000  329 PRO   C CD  
11217 N N   . ASP   G  330 ? 1.00399 1.00399 1.00399 -0.00000 0.00000  0.00000  330 ASP   C N   
11218 C CA  . ASP   G  330 ? 1.13156 1.13156 1.13156 -0.00000 0.00000  0.00000  330 ASP   C CA  
11219 C C   . ASP   G  330 ? 0.86170 0.86170 0.86170 0.00000  0.00000  0.00000  330 ASP   C C   
11220 O O   . ASP   G  330 ? 1.22551 1.22551 1.22551 0.00000  0.00000  0.00000  330 ASP   C O   
11221 C CB  . ASP   G  330 ? 0.76723 0.76723 0.76723 -0.00000 0.00000  0.00000  330 ASP   C CB  
11222 N N   . ASN   G  331 ? 1.09626 1.09626 1.09626 0.00000  0.00000  0.00000  331 ASN   C N   
11223 C CA  . ASN   G  331 ? 1.09785 1.09785 1.09785 0.00000  0.00000  0.00000  331 ASN   C CA  
11224 C C   . ASN   G  331 ? 0.87834 0.87834 0.87834 0.00000  0.00000  0.00000  331 ASN   C C   
11225 O O   . ASN   G  331 ? 1.43193 1.43193 1.43193 -0.00000 0.00000  0.00000  331 ASN   C O   
11226 C CB  . ASN   G  331 ? 0.81826 0.81826 0.81826 -0.00000 0.00000  0.00000  331 ASN   C CB  
11227 C CG  . ASN   G  331 ? 0.95873 0.95873 0.95873 0.00000  0.00000  0.00000  331 ASN   C CG  
11228 O OD1 . ASN   G  331 ? 1.83912 1.83912 1.83912 0.00000  0.00000  0.00000  331 ASN   C OD1 
11229 N ND2 . ASN   G  331 ? 1.01154 1.01154 1.01154 -0.00000 0.00000  0.00000  331 ASN   C ND2 
11230 N N   . ASP   G  332 ? 1.40971 1.40971 1.40971 0.00000  0.00000  0.00000  332 ASP   C N   
11231 C CA  . ASP   G  332 ? 1.18988 1.18988 1.18988 -0.00000 0.00000  0.00000  332 ASP   C CA  
11232 C C   . ASP   G  332 ? 1.19247 1.19247 1.19247 0.00000  0.00000  0.00000  332 ASP   C C   
11233 O O   . ASP   G  332 ? 0.45531 0.45531 0.45531 0.00000  -0.00000 0.00000  332 ASP   C O   
11234 C CB  . ASP   G  332 ? 1.32048 1.32048 1.32048 0.00000  0.00000  0.00000  332 ASP   C CB  
11235 N N   . TYR   G  333 ? 1.01898 1.01898 1.01898 -0.00000 0.00000  0.00000  333 TYR   C N   
11236 C CA  . TYR   G  333 ? 1.26313 1.26313 1.26313 0.00000  0.00000  0.00000  333 TYR   C CA  
11237 C C   . TYR   G  333 ? 0.82389 0.82389 0.82389 0.00000  0.00000  0.00000  333 TYR   C C   
11238 O O   . TYR   G  333 ? 1.06724 1.06724 1.06724 0.00000  0.00000  0.00000  333 TYR   C O   
11239 C CB  . TYR   G  333 ? 1.55720 1.55720 1.55720 0.00000  0.00000  0.00000  333 TYR   C CB  
11240 C CG  . TYR   G  333 ? 0.96770 0.96770 0.96770 0.00000  0.00000  0.00000  333 TYR   C CG  
11241 C CD1 . TYR   G  333 ? 0.91152 0.91152 0.91152 0.00000  0.00000  0.00000  333 TYR   C CD1 
11242 C CD2 . TYR   G  333 ? 0.84620 0.84620 0.84620 -0.00000 0.00000  0.00000  333 TYR   C CD2 
11243 C CE1 . TYR   G  333 ? 1.26773 1.26773 1.26773 0.00000  0.00000  0.00000  333 TYR   C CE1 
11244 C CE2 . TYR   G  333 ? 1.25771 1.25771 1.25771 0.00000  0.00000  0.00000  333 TYR   C CE2 
11245 C CZ  . TYR   G  333 ? 1.33591 1.33591 1.33591 -0.00000 0.00000  -0.00000 333 TYR   C CZ  
11246 O OH  . TYR   G  333 ? 1.10765 1.10765 1.10765 0.00000  0.00000  0.00000  333 TYR   C OH  
11247 N N   . ASP   G  334 ? 0.88120 0.88120 0.88120 0.00000  0.00000  0.00000  334 ASP   C N   
11248 C CA  . ASP   G  334 ? 0.85681 0.85681 0.85681 -0.00000 0.00000  0.00000  334 ASP   C CA  
11249 C C   . ASP   G  334 ? 0.97638 0.97638 0.97638 -0.00000 0.00000  0.00000  334 ASP   C C   
11250 O O   . ASP   G  334 ? 0.54231 0.54231 0.54231 0.00000  0.00000  0.00000  334 ASP   C O   
11251 C CB  . ASP   G  334 ? 1.22160 1.22160 1.22160 0.00000  0.00000  -0.00000 334 ASP   C CB  
11252 C CG  . ASP   G  334 ? 1.40678 1.40678 1.40678 -0.00000 0.00000  0.00000  334 ASP   C CG  
11253 O OD1 . ASP   G  334 ? 0.85212 0.85212 0.85212 0.00000  0.00000  0.00000  334 ASP   C OD1 
11254 O OD2 . ASP   G  334 ? 0.99554 0.99554 0.99554 0.00000  0.00000  0.00000  334 ASP   C OD2 
11255 N N   . PRO   G  335 ? 0.84744 0.84744 0.84744 0.00000  0.00000  0.00000  335 PRO   C N   
11256 C CA  . PRO   G  335 ? 0.59168 0.59168 0.59168 -0.00000 0.00000  -0.00000 335 PRO   C CA  
11257 C C   . PRO   G  335 ? 0.38942 0.38942 0.38942 0.00000  0.00000  0.00000  335 PRO   C C   
11258 O O   . PRO   G  335 ? 0.75597 0.75597 0.75597 -0.00000 0.00000  0.00000  335 PRO   C O   
11259 C CB  . PRO   G  335 ? 0.66487 0.66487 0.66487 -0.00000 0.00000  0.00000  335 PRO   C CB  
11260 C CG  . PRO   G  335 ? 0.82776 0.82776 0.82776 0.00000  0.00000  -0.00000 335 PRO   C CG  
11261 C CD  . PRO   G  335 ? 0.49309 0.49309 0.49309 0.00000  0.00000  0.00000  335 PRO   C CD  
11262 N N   . PRO   G  336 ? 0.70430 0.70430 0.70430 -0.00000 0.00000  0.00000  336 PRO   C N   
11263 C CA  . PRO   G  336 ? 0.25361 0.25361 0.25361 -0.00000 0.00000  0.00000  336 PRO   C CA  
11264 C C   . PRO   G  336 ? 1.09321 1.09321 1.09321 -0.00000 0.00000  0.00000  336 PRO   C C   
11265 O O   . PRO   G  336 ? 0.32147 0.32147 0.32147 0.00000  0.00000  0.00000  336 PRO   C O   
11266 C CB  . PRO   G  336 ? 0.49403 0.49403 0.49403 0.00000  0.00000  0.00000  336 PRO   C CB  
11267 C CG  . PRO   G  336 ? 0.45574 0.45574 0.45574 0.00000  0.00000  0.00000  336 PRO   C CG  
11268 C CD  . PRO   G  336 ? 0.25339 0.25339 0.25339 0.00000  0.00000  0.00000  336 PRO   C CD  
11269 N N   . PRO   G  337 ? 0.37117 0.37117 0.37117 0.00000  0.00000  0.00000  337 PRO   C N   
11270 C CA  . PRO   G  337 ? 0.56890 0.56890 0.56890 0.00000  0.00000  0.00000  337 PRO   C CA  
11271 C C   . PRO   G  337 ? 0.42393 0.42393 0.42393 0.00000  0.00000  0.00000  337 PRO   C C   
11272 O O   . PRO   G  337 ? 0.39664 0.39664 0.39664 0.00000  0.00000  0.00000  337 PRO   C O   
11273 C CB  . PRO   G  337 ? 0.39820 0.39820 0.39820 -0.00000 0.00000  0.00000  337 PRO   C CB  
11274 C CG  . PRO   G  337 ? 0.50437 0.50437 0.50437 0.00000  0.00000  0.00000  337 PRO   C CG  
11275 C CD  . PRO   G  337 ? 0.61424 0.61424 0.61424 0.00000  0.00000  0.00000  337 PRO   C CD  
11276 N N   . TYR   G  338 ? 0.41933 0.41933 0.41933 0.00000  0.00000  0.00000  338 TYR   C N   
11277 C CA  . TYR   G  338 ? 0.45207 0.45207 0.45207 -0.00000 0.00000  0.00000  338 TYR   C CA  
11278 C C   . TYR   G  338 ? 0.37371 0.37371 0.37371 -0.00000 0.00000  0.00000  338 TYR   C C   
11279 O O   . TYR   G  338 ? 0.39053 0.39053 0.39053 0.00000  0.00000  0.00000  338 TYR   C O   
11280 C CB  . TYR   G  338 ? 0.29398 0.29398 0.29398 -0.00000 0.00000  0.00000  338 TYR   C CB  
11281 C CG  . TYR   G  338 ? 0.45960 0.45960 0.45960 0.00000  0.00000  0.00000  338 TYR   C CG  
11282 C CD1 . TYR   G  338 ? 0.36749 0.36749 0.36749 0.00000  0.00000  0.00000  338 TYR   C CD1 
11283 C CD2 . TYR   G  338 ? 0.34014 0.34014 0.34014 0.00000  0.00000  0.00000  338 TYR   C CD2 
11284 C CE1 . TYR   G  338 ? 0.40185 0.40185 0.40185 0.00000  0.00000  0.00000  338 TYR   C CE1 
11285 C CE2 . TYR   G  338 ? 0.26300 0.26300 0.26300 0.00000  0.00000  0.00000  338 TYR   C CE2 
11286 C CZ  . TYR   G  338 ? 0.51940 0.51940 0.51940 -0.00000 0.00000  0.00000  338 TYR   C CZ  
11287 O OH  . TYR   G  338 ? 0.37437 0.37437 0.37437 -0.00000 0.00000  0.00000  338 TYR   C OH  
11288 N N   . LEU   G  339 ? 0.49045 0.49045 0.49045 0.00000  0.00000  0.00000  339 LEU   C N   
11289 C CA  . LEU   G  339 ? 0.37851 0.37851 0.37851 0.00000  0.00000  0.00000  339 LEU   C CA  
11290 C C   . LEU   G  339 ? 0.53030 0.53030 0.53030 0.00000  0.00000  0.00000  339 LEU   C C   
11291 O O   . LEU   G  339 ? 0.55173 0.55173 0.55173 0.00000  0.00000  0.00000  339 LEU   C O   
11292 C CB  . LEU   G  339 ? 0.38893 0.38893 0.38893 0.00000  0.00000  0.00000  339 LEU   C CB  
11293 C CG  . LEU   G  339 ? 0.66776 0.66776 0.66776 0.00000  0.00000  0.00000  339 LEU   C CG  
11294 C CD1 . LEU   G  339 ? 0.46291 0.46291 0.46291 0.00000  0.00000  0.00000  339 LEU   C CD1 
11295 C CD2 . LEU   G  339 ? 0.48006 0.48006 0.48006 0.00000  0.00000  0.00000  339 LEU   C CD2 
11296 N N   . LYS   G  340 ? 0.38119 0.38119 0.38119 0.00000  0.00000  0.00000  340 LYS   C N   
11297 C CA  . LYS   G  340 ? 0.63220 0.63220 0.63220 -0.00000 0.00000  0.00000  340 LYS   C CA  
11298 C C   . LYS   G  340 ? 0.40691 0.40691 0.40691 0.00000  0.00000  0.00000  340 LYS   C C   
11299 O O   . LYS   G  340 ? 0.48786 0.48786 0.48786 0.00000  0.00000  0.00000  340 LYS   C O   
11300 C CB  . LYS   G  340 ? 0.41514 0.41514 0.41514 -0.00000 0.00000  0.00000  340 LYS   C CB  
11301 C CG  . LYS   G  340 ? 0.59277 0.59277 0.59277 -0.00000 0.00000  0.00000  340 LYS   C CG  
11302 C CD  . LYS   G  340 ? 1.43901 1.43901 1.43901 -0.00000 0.00000  0.00000  340 LYS   C CD  
11303 C CE  . LYS   G  340 ? 1.48549 1.48549 1.48549 0.00000  0.00000  0.00000  340 LYS   C CE  
11304 N NZ  . LYS   G  340 ? 0.75407 0.75407 0.75407 0.00000  0.00000  0.00000  340 LYS   C NZ  
11305 N N   . SER   G  341 ? 0.40184 0.40184 0.40184 0.00000  0.00000  0.00000  341 SER   C N   
11306 C CA  . SER   G  341 ? 0.31514 0.31514 0.31514 -0.00000 0.00000  0.00000  341 SER   C CA  
11307 C C   . SER   G  341 ? 0.37702 0.37702 0.37702 -0.00000 0.00000  0.00000  341 SER   C C   
11308 O O   . SER   G  341 ? 0.51062 0.51062 0.51062 0.00000  -0.00000 0.00000  341 SER   C O   
11309 C CB  . SER   G  341 ? 0.39805 0.39805 0.39805 -0.00000 0.00000  0.00000  341 SER   C CB  
11310 O OG  . SER   G  341 ? 0.39503 0.39503 0.39503 0.00000  0.00000  0.00000  341 SER   C OG  
11311 N N   . LEU   G  342 ? 0.37581 0.37581 0.37581 0.00000  0.00000  0.00000  342 LEU   C N   
11312 C CA  . LEU   G  342 ? 0.51752 0.51752 0.51752 -0.00000 0.00000  0.00000  342 LEU   C CA  
11313 C C   . LEU   G  342 ? 0.37317 0.37317 0.37317 0.00000  0.00000  -0.00000 342 LEU   C C   
11314 O O   . LEU   G  342 ? 0.44810 0.44810 0.44810 0.00000  0.00000  0.00000  342 LEU   C O   
11315 C CB  . LEU   G  342 ? 0.30051 0.30051 0.30051 -0.00000 0.00000  0.00000  342 LEU   C CB  
11316 C CG  . LEU   G  342 ? 0.53185 0.53185 0.53185 -0.00000 0.00000  0.00000  342 LEU   C CG  
11317 C CD1 . LEU   G  342 ? 0.28079 0.28079 0.28079 0.00000  0.00000  0.00000  342 LEU   C CD1 
11318 C CD2 . LEU   G  342 ? 0.22521 0.22521 0.22521 0.00000  0.00000  0.00000  342 LEU   C CD2 
11319 N N   . VAL   G  343 ? 0.46249 0.46249 0.46249 -0.00000 0.00000  0.00000  343 VAL   C N   
11320 C CA  . VAL   G  343 ? 0.39022 0.39022 0.39022 0.00000  0.00000  0.00000  343 VAL   C CA  
11321 C C   . VAL   G  343 ? 0.55378 0.55378 0.55378 0.00000  0.00000  0.00000  343 VAL   C C   
11322 O O   . VAL   G  343 ? 0.35530 0.35530 0.35530 0.00000  0.00000  0.00000  343 VAL   C O   
11323 C CB  . VAL   G  343 ? 0.40138 0.40138 0.40138 -0.00000 0.00000  0.00000  343 VAL   C CB  
11324 C CG1 . VAL   G  343 ? 0.22679 0.22679 0.22679 -0.00000 0.00000  0.00000  343 VAL   C CG1 
11325 C CG2 . VAL   G  343 ? 0.31985 0.31985 0.31985 0.00000  0.00000  0.00000  343 VAL   C CG2 
11326 N N   . TYR   G  344 ? 0.25247 0.25247 0.25247 -0.00000 0.00000  0.00000  344 TYR   C N   
11327 C CA  . TYR   G  344 ? 0.47355 0.47355 0.47355 0.00000  0.00000  0.00000  344 TYR   C CA  
11328 C C   . TYR   G  344 ? 0.49296 0.49296 0.49296 -0.00000 -0.00000 -0.00000 344 TYR   C C   
11329 O O   . TYR   G  344 ? 0.36612 0.36612 0.36612 0.00000  0.00000  0.00000  344 TYR   C O   
11330 C CB  . TYR   G  344 ? 0.30764 0.30764 0.30764 -0.00000 0.00000  0.00000  344 TYR   C CB  
11331 C CG  . TYR   G  344 ? 0.56582 0.56582 0.56582 -0.00000 0.00000  0.00000  344 TYR   C CG  
11332 C CD1 . TYR   G  344 ? 0.34736 0.34736 0.34736 0.00000  0.00000  0.00000  344 TYR   C CD1 
11333 C CD2 . TYR   G  344 ? 0.46421 0.46421 0.46421 0.00000  0.00000  0.00000  344 TYR   C CD2 
11334 C CE1 . TYR   G  344 ? 0.34988 0.34988 0.34988 0.00000  0.00000  0.00000  344 TYR   C CE1 
11335 C CE2 . TYR   G  344 ? 0.33845 0.33845 0.33845 0.00000  0.00000  0.00000  344 TYR   C CE2 
11336 C CZ  . TYR   G  344 ? 0.56984 0.56984 0.56984 0.00000  -0.00000 0.00000  344 TYR   C CZ  
11337 O OH  . TYR   G  344 ? 0.50701 0.50701 0.50701 0.00000  0.00000  0.00000  344 TYR   C OH  
11338 N N   . PHE   G  345 ? 0.24831 0.24831 0.24831 -0.00000 0.00000  0.00000  345 PHE   C N   
11339 C CA  . PHE   G  345 ? 0.36291 0.36291 0.36291 0.00000  0.00000  0.00000  345 PHE   C CA  
11340 C C   . PHE   G  345 ? 0.42850 0.42850 0.42850 0.00000  0.00000  0.00000  345 PHE   C C   
11341 O O   . PHE   G  345 ? 0.38219 0.38219 0.38219 0.00000  0.00000  0.00000  345 PHE   C O   
11342 C CB  . PHE   G  345 ? 0.24260 0.24260 0.24260 0.00000  0.00000  0.00000  345 PHE   C CB  
11343 C CG  . PHE   G  345 ? 0.40984 0.40984 0.40984 0.00000  0.00000  0.00000  345 PHE   C CG  
11344 C CD1 . PHE   G  345 ? 0.47583 0.47583 0.47583 0.00000  0.00000  0.00000  345 PHE   C CD1 
11345 C CD2 . PHE   G  345 ? 0.32814 0.32814 0.32814 -0.00000 0.00000  0.00000  345 PHE   C CD2 
11346 C CE1 . PHE   G  345 ? 0.27551 0.27551 0.27551 0.00000  0.00000  0.00000  345 PHE   C CE1 
11347 C CE2 . PHE   G  345 ? 0.34672 0.34672 0.34672 -0.00000 0.00000  0.00000  345 PHE   C CE2 
11348 C CZ  . PHE   G  345 ? 0.37582 0.37582 0.37582 0.00000  0.00000  0.00000  345 PHE   C CZ  
11349 N N   . SER   G  346 ? 0.23092 0.23092 0.23092 0.00000  0.00000  0.00000  346 SER   C N   
11350 C CA  . SER   G  346 ? 0.51218 0.51218 0.51218 -0.00000 0.00000  0.00000  346 SER   C CA  
11351 C C   . SER   G  346 ? 0.35225 0.35225 0.35225 0.00000  0.00000  0.00000  346 SER   C C   
11352 O O   . SER   G  346 ? 0.35228 0.35228 0.35228 -0.00000 0.00000  0.00000  346 SER   C O   
11353 C CB  . SER   G  346 ? 0.34472 0.34472 0.34472 0.00000  0.00000  0.00000  346 SER   C CB  
11354 O OG  . SER   G  346 ? 0.30174 0.30174 0.30174 0.00000  0.00000  0.00000  346 SER   C OG  
11355 N N   . ASN   G  347 ? 0.43139 0.43139 0.43139 0.00000  0.00000  0.00000  347 ASN   C N   
11356 C CA  . ASN   G  347 ? 0.19203 0.19203 0.19203 0.00000  0.00000  0.00000  347 ASN   C CA  
11357 C C   . ASN   G  347 ? 0.40572 0.40572 0.40572 0.00000  0.00000  0.00000  347 ASN   C C   
11358 O O   . ASN   G  347 ? 0.41006 0.41006 0.41006 0.00000  0.00000  0.00000  347 ASN   C O   
11359 C CB  . ASN   G  347 ? 0.28728 0.28728 0.28728 0.00000  0.00000  0.00000  347 ASN   C CB  
11360 C CG  . ASN   G  347 ? 0.47909 0.47909 0.47909 -0.00000 0.00000  0.00000  347 ASN   C CG  
11361 O OD1 . ASN   G  347 ? 0.36682 0.36682 0.36682 -0.00000 0.00000  0.00000  347 ASN   C OD1 
11362 N ND2 . ASN   G  347 ? 0.24943 0.24943 0.24943 0.00000  -0.00000 0.00000  347 ASN   C ND2 
11363 N N   . ILE   G  348 ? 0.25689 0.25689 0.25689 0.00000  0.00000  0.00000  348 ILE   C N   
11364 C CA  . ILE   G  348 ? 0.16817 0.16817 0.16817 0.00000  0.00000  0.00000  348 ILE   C CA  
11365 C C   . ILE   G  348 ? 0.30849 0.30849 0.30849 0.00000  0.00000  0.00000  348 ILE   C C   
11366 O O   . ILE   G  348 ? 0.35246 0.35246 0.35246 0.00000  0.00000  0.00000  348 ILE   C O   
11367 C CB  . ILE   G  348 ? 0.28195 0.28195 0.28195 0.00000  0.00000  0.00000  348 ILE   C CB  
11368 C CG1 . ILE   G  348 ? 0.13669 0.13669 0.13669 0.00000  0.00000  0.00000  348 ILE   C CG1 
11369 C CG2 . ILE   G  348 ? 0.11018 0.11018 0.11018 -0.00000 0.00000  0.00000  348 ILE   C CG2 
11370 C CD1 . ILE   G  348 ? 0.42234 0.42234 0.42234 0.00000  0.00000  0.00000  348 ILE   C CD1 
11371 N N   . ALA   G  349 ? 0.34090 0.34090 0.34090 -0.00000 0.00000  0.00000  349 ALA   C N   
11372 C CA  . ALA   G  349 ? 0.34676 0.34676 0.34676 -0.00000 0.00000  0.00000  349 ALA   C CA  
11373 C C   . ALA   G  349 ? 0.38706 0.38706 0.38706 0.00000  -0.00000 -0.00000 349 ALA   C C   
11374 O O   . ALA   G  349 ? 0.44957 0.44957 0.44957 -0.00000 0.00000  0.00000  349 ALA   C O   
11375 C CB  . ALA   G  349 ? 0.15932 0.15932 0.15932 0.00000  0.00000  0.00000  349 ALA   C CB  
11376 N N   . ALA   G  350 ? 0.26633 0.26633 0.26633 0.00000  0.00000  0.00000  350 ALA   C N   
11377 C CA  . ALA   G  350 ? 0.29782 0.29782 0.29782 0.00000  0.00000  0.00000  350 ALA   C CA  
11378 C C   . ALA   G  350 ? 0.37304 0.37304 0.37304 0.00000  0.00000  0.00000  350 ALA   C C   
11379 O O   . ALA   G  350 ? 0.29109 0.29109 0.29109 -0.00000 0.00000  0.00000  350 ALA   C O   
11380 C CB  . ALA   G  350 ? 0.11891 0.11891 0.11891 0.00000  0.00000  0.00000  350 ALA   C CB  
11381 N N   . ARG   G  351 ? 0.24399 0.24399 0.24399 -0.00000 0.00000  0.00000  351 ARG   C N   
11382 C CA  . ARG   G  351 ? 0.37386 0.37386 0.37386 -0.00000 0.00000  -0.00000 351 ARG   C CA  
11383 C C   . ARG   G  351 ? 0.27681 0.27681 0.27681 0.00000  0.00000  0.00000  351 ARG   C C   
11384 O O   . ARG   G  351 ? 0.45710 0.45710 0.45710 0.00000  0.00000  0.00000  351 ARG   C O   
11385 C CB  . ARG   G  351 ? 0.19300 0.19300 0.19300 -0.00000 0.00000  0.00000  351 ARG   C CB  
11386 C CG  . ARG   G  351 ? 0.19308 0.19308 0.19308 -0.00000 0.00000  0.00000  351 ARG   C CG  
11387 C CD  . ARG   G  351 ? 0.29332 0.29332 0.29332 0.00000  0.00000  0.00000  351 ARG   C CD  
11388 N NE  . ARG   G  351 ? 0.31313 0.31313 0.31313 0.00000  0.00000  0.00000  351 ARG   C NE  
11389 C CZ  . ARG   G  351 ? 0.58571 0.58571 0.58571 0.00000  0.00000  0.00000  351 ARG   C CZ  
11390 N NH1 . ARG   G  351 ? 0.31656 0.31656 0.31656 0.00000  0.00000  0.00000  351 ARG   C NH1 
11391 N NH2 . ARG   G  351 ? 0.25788 0.25788 0.25788 0.00000  0.00000  0.00000  351 ARG   C NH2 
11392 N N   . GLN   G  352 ? 0.33989 0.33989 0.33989 0.00000  0.00000  0.00000  352 GLN   C N   
11393 C CA  . GLN   G  352 ? 0.25579 0.25579 0.25579 0.00000  0.00000  0.00000  352 GLN   C CA  
11394 C C   . GLN   G  352 ? 0.41001 0.41001 0.41001 0.00000  0.00000  0.00000  352 GLN   C C   
11395 O O   . GLN   G  352 ? 0.39581 0.39581 0.39581 0.00000  0.00000  0.00000  352 GLN   C O   
11396 C CB  . GLN   G  352 ? 0.38454 0.38454 0.38454 0.00000  0.00000  0.00000  352 GLN   C CB  
11397 C CG  . GLN   G  352 ? 0.32189 0.32189 0.32189 0.00000  0.00000  0.00000  352 GLN   C CG  
11398 C CD  . GLN   G  352 ? 0.42759 0.42759 0.42759 0.00000  0.00000  0.00000  352 GLN   C CD  
11399 O OE1 . GLN   G  352 ? 0.45367 0.45367 0.45367 0.00000  -0.00000 0.00000  352 GLN   C OE1 
11400 N NE2 . GLN   G  352 ? 0.29037 0.29037 0.29037 0.00000  0.00000  0.00000  352 GLN   C NE2 
11401 N N   . ILE   G  353 ? 0.30841 0.30841 0.30841 -0.00000 0.00000  0.00000  353 ILE   C N   
11402 C CA  . ILE   G  353 ? 0.34416 0.34416 0.34416 0.00000  0.00000  0.00000  353 ILE   C CA  
11403 C C   . ILE   G  353 ? 0.25572 0.25572 0.25572 0.00000  0.00000  0.00000  353 ILE   C C   
11404 O O   . ILE   G  353 ? 0.43418 0.43418 0.43418 0.00000  0.00000  0.00000  353 ILE   C O   
11405 C CB  . ILE   G  353 ? 0.31759 0.31759 0.31759 0.00000  0.00000  0.00000  353 ILE   C CB  
11406 C CG1 . ILE   G  353 ? 0.40931 0.40931 0.40931 -0.00000 0.00000  0.00000  353 ILE   C CG1 
11407 C CG2 . ILE   G  353 ? 0.20188 0.20188 0.20188 0.00000  0.00000  0.00000  353 ILE   C CG2 
11408 C CD1 . ILE   G  353 ? 0.15818 0.15818 0.15818 -0.00000 0.00000  0.00000  353 ILE   C CD1 
11409 N N   . MET   G  354 ? 0.25821 0.25821 0.25821 0.00000  0.00000  0.00000  354 MET   C N   
11410 C CA  . MET   G  354 ? 0.32543 0.32543 0.32543 0.00000  0.00000  0.00000  354 MET   C CA  
11411 C C   . MET   G  354 ? 0.38995 0.38995 0.38995 -0.00000 0.00000  0.00000  354 MET   C C   
11412 O O   . MET   G  354 ? 0.40857 0.40857 0.40857 0.00000  0.00000  0.00000  354 MET   C O   
11413 C CB  . MET   G  354 ? 0.18631 0.18631 0.18631 0.00000  -0.00000 0.00000  354 MET   C CB  
11414 C CG  . MET   G  354 ? 0.46295 0.46295 0.46295 0.00000  0.00000  0.00000  354 MET   C CG  
11415 S SD  . MET   G  354 ? 0.42798 0.42798 0.42798 -0.00000 0.00000  0.00000  354 MET   C SD  
11416 C CE  . MET   G  354 ? 0.40527 0.40527 0.40527 -0.00000 0.00000  0.00000  354 MET   C CE  
11417 N N   . PHE   G  355 ? 0.37168 0.37168 0.37168 0.00000  0.00000  0.00000  355 PHE   C N   
11418 C CA  . PHE   G  355 ? 0.39233 0.39233 0.39233 0.00000  -0.00000 0.00000  355 PHE   C CA  
11419 C C   . PHE   G  355 ? 0.37637 0.37637 0.37637 0.00000  0.00000  0.00000  355 PHE   C C   
11420 O O   . PHE   G  355 ? 0.43477 0.43477 0.43477 -0.00000 0.00000  0.00000  355 PHE   C O   
11421 C CB  . PHE   G  355 ? 0.44120 0.44120 0.44120 0.00000  0.00000  0.00000  355 PHE   C CB  
11422 C CG  . PHE   G  355 ? 0.46475 0.46475 0.46475 -0.00000 0.00000  0.00000  355 PHE   C CG  
11423 C CD1 . PHE   G  355 ? 0.30065 0.30065 0.30065 -0.00000 0.00000  0.00000  355 PHE   C CD1 
11424 C CD2 . PHE   G  355 ? 0.41076 0.41076 0.41076 -0.00000 0.00000  0.00000  355 PHE   C CD2 
11425 C CE1 . PHE   G  355 ? 0.46375 0.46375 0.46375 -0.00000 0.00000  0.00000  355 PHE   C CE1 
11426 C CE2 . PHE   G  355 ? 0.24820 0.24820 0.24820 0.00000  0.00000  0.00000  355 PHE   C CE2 
11427 C CZ  . PHE   G  355 ? 0.26794 0.26794 0.26794 0.00000  0.00000  0.00000  355 PHE   C CZ  
11428 N N   . ILE   G  356 ? 0.34037 0.34037 0.34037 0.00000  0.00000  0.00000  356 ILE   C N   
11429 C CA  . ILE   G  356 ? 0.38291 0.38291 0.38291 0.00000  0.00000  0.00000  356 ILE   C CA  
11430 C C   . ILE   G  356 ? 0.54680 0.54680 0.54680 0.00000  0.00000  0.00000  356 ILE   C C   
11431 O O   . ILE   G  356 ? 0.37887 0.37887 0.37887 0.00000  0.00000  0.00000  356 ILE   C O   
11432 C CB  . ILE   G  356 ? 0.30795 0.30795 0.30795 0.00000  0.00000  0.00000  356 ILE   C CB  
11433 C CG1 . ILE   G  356 ? 0.29909 0.29909 0.29909 0.00000  0.00000  0.00000  356 ILE   C CG1 
11434 C CG2 . ILE   G  356 ? 0.34643 0.34643 0.34643 0.00000  0.00000  0.00000  356 ILE   C CG2 
11435 C CD1 . ILE   G  356 ? 0.22443 0.22443 0.22443 0.00000  0.00000  -0.00000 356 ILE   C CD1 
11436 N N   . GLU   G  357 ? 0.32191 0.32191 0.32191 -0.00000 0.00000  0.00000  357 GLU   C N   
11437 C CA  . GLU   G  357 ? 0.51179 0.51179 0.51179 0.00000  -0.00000 0.00000  357 GLU   C CA  
11438 C C   . GLU   G  357 ? 0.48907 0.48907 0.48907 0.00000  0.00000  0.00000  357 GLU   C C   
11439 O O   . GLU   G  357 ? 0.47245 0.47245 0.47245 -0.00000 0.00000  0.00000  357 GLU   C O   
11440 C CB  . GLU   G  357 ? 0.39167 0.39167 0.39167 -0.00000 0.00000  0.00000  357 GLU   C CB  
11441 C CG  . GLU   G  357 ? 0.37622 0.37622 0.37622 0.00000  0.00000  0.00000  357 GLU   C CG  
11442 C CD  . GLU   G  357 ? 1.05127 1.05127 1.05127 0.00000  0.00000  0.00000  357 GLU   C CD  
11443 O OE1 . GLU   G  357 ? 0.83000 0.83000 0.83000 0.00000  0.00000  0.00000  357 GLU   C OE1 
11444 O OE2 . GLU   G  357 ? 0.66636 0.66636 0.66636 -0.00000 0.00000  0.00000  357 GLU   C OE2 
11445 N N   . ALA   G  358 ? 0.30760 0.30760 0.30760 0.00000  0.00000  0.00000  358 ALA   C N   
11446 C CA  . ALA   G  358 ? 0.54649 0.54649 0.54649 0.00000  0.00000  0.00000  358 ALA   C CA  
11447 C C   . ALA   G  358 ? 0.47591 0.47591 0.47591 -0.00000 0.00000  0.00000  358 ALA   C C   
11448 O O   . ALA   G  358 ? 0.80514 0.80514 0.80514 0.00000  0.00000  0.00000  358 ALA   C O   
11449 C CB  . ALA   G  358 ? 0.40262 0.40262 0.40262 0.00000  -0.00000 0.00000  358 ALA   C CB  
11450 N N   . ASP   G  359 ? 0.63239 0.63239 0.63239 0.00000  0.00000  0.00000  359 ASP   C N   
11451 C CA  . ASP   G  359 ? 0.57301 0.57301 0.57301 -0.00000 0.00000  0.00000  359 ASP   C CA  
11452 C C   . ASP   G  359 ? 0.34698 0.34698 0.34698 -0.00000 0.00000  0.00000  359 ASP   C C   
11453 O O   . ASP   G  359 ? 0.43264 0.43264 0.43264 0.00000  0.00000  0.00000  359 ASP   C O   
11454 C CB  . ASP   G  359 ? 0.30784 0.30784 0.30784 0.00000  0.00000  -0.00000 359 ASP   C CB  
11455 C CG  . ASP   G  359 ? 0.78012 0.78012 0.78012 0.00000  0.00000  0.00000  359 ASP   C CG  
11456 O OD1 . ASP   G  359 ? 0.52712 0.52712 0.52712 -0.00000 0.00000  0.00000  359 ASP   C OD1 
11457 O OD2 . ASP   G  359 ? 0.44746 0.44746 0.44746 -0.00000 0.00000  0.00000  359 ASP   C OD2 
11458 N N   . ASN   G  360 ? 0.40980 0.40980 0.40980 -0.00000 0.00000  0.00000  360 ASN   C N   
11459 C CA  . ASN   G  360 ? 0.29901 0.29901 0.29901 0.00000  0.00000  0.00000  360 ASN   C CA  
11460 C C   . ASN   G  360 ? 0.43788 0.43788 0.43788 0.00000  0.00000  0.00000  360 ASN   C C   
11461 O O   . ASN   G  360 ? 0.57305 0.57305 0.57305 -0.00000 0.00000  0.00000  360 ASN   C O   
11462 C CB  . ASN   G  360 ? 0.31523 0.31523 0.31523 0.00000  0.00000  0.00000  360 ASN   C CB  
11463 C CG  . ASN   G  360 ? 0.55315 0.55315 0.55315 -0.00000 0.00000  0.00000  360 ASN   C CG  
11464 O OD1 . ASN   G  360 ? 0.59247 0.59247 0.59247 0.00000  0.00000  0.00000  360 ASN   C OD1 
11465 N ND2 . ASN   G  360 ? 0.62868 0.62868 0.62868 0.00000  0.00000  0.00000  360 ASN   C ND2 
11466 N N   . LYS   G  361 ? 0.51590 0.51590 0.51590 -0.00000 0.00000  0.00000  361 LYS   C N   
11467 C CA  . LYS   G  361 ? 0.61429 0.61429 0.61429 -0.00000 0.00000  0.00000  361 LYS   C CA  
11468 C C   . LYS   G  361 ? 0.26368 0.26368 0.26368 0.00000  0.00000  0.00000  361 LYS   C C   
11469 O O   . LYS   G  361 ? 0.90180 0.90180 0.90180 0.00000  0.00000  0.00000  361 LYS   C O   
11470 C CB  . LYS   G  361 ? 0.31633 0.31633 0.31633 0.00000  0.00000  0.00000  361 LYS   C CB  
11471 N N   . GLU   G  362 ? 0.39654 0.39654 0.39654 0.00000  0.00000  0.00000  362 GLU   C N   
11472 C CA  . GLU   G  362 ? 0.33909 0.33909 0.33909 0.00000  0.00000  0.00000  362 GLU   C CA  
11473 C C   . GLU   G  362 ? 0.59597 0.59597 0.59597 0.00000  0.00000  0.00000  362 GLU   C C   
11474 O O   . GLU   G  362 ? 0.49797 0.49797 0.49797 -0.00000 0.00000  0.00000  362 GLU   C O   
11475 C CB  . GLU   G  362 ? 0.45129 0.45129 0.45129 0.00000  0.00000  0.00000  362 GLU   C CB  
11476 C CG  . GLU   G  362 ? 0.41379 0.41379 0.41379 -0.00000 0.00000  0.00000  362 GLU   C CG  
11477 C CD  . GLU   G  362 ? 1.48175 1.48175 1.48175 0.00000  0.00000  0.00000  362 GLU   C CD  
11478 O OE1 . GLU   G  362 ? 1.47611 1.47611 1.47611 -0.00000 0.00000  0.00000  362 GLU   C OE1 
11479 O OE2 . GLU   G  362 ? 1.35917 1.35917 1.35917 -0.00000 0.00000  0.00000  362 GLU   C OE2 
11480 N N   . ILE   G  363 ? 0.46409 0.46409 0.46409 -0.00000 0.00000  0.00000  363 ILE   C N   
11481 C CA  . ILE   G  363 ? 0.69166 0.69166 0.69166 -0.00000 0.00000  0.00000  363 ILE   C CA  
11482 C C   . ILE   G  363 ? 0.54590 0.54590 0.54590 0.00000  0.00000  -0.00000 363 ILE   C C   
11483 O O   . ILE   G  363 ? 0.65170 0.65170 0.65170 0.00000  0.00000  0.00000  363 ILE   C O   
11484 C CB  . ILE   G  363 ? 0.56800 0.56800 0.56800 0.00000  0.00000  0.00000  363 ILE   C CB  
11485 C CG1 . ILE   G  363 ? 0.49084 0.49084 0.49084 0.00000  0.00000  0.00000  363 ILE   C CG1 
11486 C CG2 . ILE   G  363 ? 0.31195 0.31195 0.31195 0.00000  0.00000  0.00000  363 ILE   C CG2 
11487 C CD1 . ILE   G  363 ? 0.53392 0.53392 0.53392 0.00000  0.00000  0.00000  363 ILE   C CD1 
11488 N N   . GLY   G  364 ? 0.44992 0.44992 0.44992 0.00000  0.00000  0.00000  364 GLY   C N   
11489 C CA  . GLY   G  364 ? 0.29662 0.29662 0.29662 0.00000  0.00000  0.00000  364 GLY   C CA  
11490 C C   . GLY   G  364 ? 0.86962 0.86962 0.86962 0.00000  0.00000  0.00000  364 GLY   C C   
11491 O O   . GLY   G  364 ? 0.42116 0.42116 0.42116 0.00000  0.00000  0.00000  364 GLY   C O   
11492 N N   . LEU   G  365 ? 0.52013 0.52013 0.52013 -0.00000 0.00000  0.00000  365 LEU   C N   
11493 C CA  . LEU   G  365 ? 0.22741 0.22741 0.22741 0.00000  0.00000  0.00000  365 LEU   C CA  
11494 C C   . LEU   G  365 ? 0.53968 0.53968 0.53968 0.00000  0.00000  0.00000  365 LEU   C C   
11495 O O   . LEU   G  365 ? 0.37885 0.37885 0.37885 0.00000  0.00000  0.00000  365 LEU   C O   
11496 C CB  . LEU   G  365 ? 0.40602 0.40602 0.40602 0.00000  0.00000  0.00000  365 LEU   C CB  
11497 C CG  . LEU   G  365 ? 0.45109 0.45109 0.45109 0.00000  0.00000  0.00000  365 LEU   C CG  
11498 C CD1 . LEU   G  365 ? 0.28942 0.28942 0.28942 0.00000  0.00000  0.00000  365 LEU   C CD1 
11499 C CD2 . LEU   G  365 ? 0.27722 0.27722 0.27722 0.00000  0.00000  0.00000  365 LEU   C CD2 
11500 N N   . ILE   G  366 ? 0.22699 0.22699 0.22699 0.00000  0.00000  0.00000  366 ILE   C N   
11501 C CA  . ILE   G  366 ? 0.40846 0.40846 0.40846 0.00000  0.00000  0.00000  366 ILE   C CA  
11502 C C   . ILE   G  366 ? 0.43774 0.43774 0.43774 0.00000  0.00000  0.00000  366 ILE   C C   
11503 O O   . ILE   G  366 ? 0.38106 0.38106 0.38106 -0.00000 0.00000  0.00000  366 ILE   C O   
11504 C CB  . ILE   G  366 ? 0.32439 0.32439 0.32439 0.00000  0.00000  0.00000  366 ILE   C CB  
11505 C CG1 . ILE   G  366 ? 0.36902 0.36902 0.36902 0.00000  0.00000  0.00000  366 ILE   C CG1 
11506 C CG2 . ILE   G  366 ? 0.22235 0.22235 0.22235 0.00000  -0.00000 0.00000  366 ILE   C CG2 
11507 C CD1 . ILE   G  366 ? 0.37878 0.37878 0.37878 0.00000  0.00000  0.00000  366 ILE   C CD1 
11508 N N   . PHE   G  367 ? 0.31531 0.31531 0.31531 -0.00000 0.00000  0.00000  367 PHE   C N   
11509 C CA  . PHE   G  367 ? 0.27691 0.27691 0.27691 0.00000  0.00000  0.00000  367 PHE   C CA  
11510 C C   . PHE   G  367 ? 0.39438 0.39438 0.39438 0.00000  0.00000  0.00000  367 PHE   C C   
11511 O O   . PHE   G  367 ? 0.33747 0.33747 0.33747 0.00000  0.00000  0.00000  367 PHE   C O   
11512 C CB  . PHE   G  367 ? 0.26384 0.26384 0.26384 0.00000  0.00000  0.00000  367 PHE   C CB  
11513 C CG  . PHE   G  367 ? 0.16258 0.16258 0.16258 0.00000  0.00000  0.00000  367 PHE   C CG  
11514 C CD1 . PHE   G  367 ? 0.36894 0.36894 0.36894 0.00000  0.00000  0.00000  367 PHE   C CD1 
11515 C CD2 . PHE   G  367 ? 0.30749 0.30749 0.30749 0.00000  0.00000  0.00000  367 PHE   C CD2 
11516 C CE1 . PHE   G  367 ? 0.16827 0.16827 0.16827 -0.00000 0.00000  0.00000  367 PHE   C CE1 
11517 C CE2 . PHE   G  367 ? 0.28294 0.28294 0.28294 0.00000  0.00000  0.00000  367 PHE   C CE2 
11518 C CZ  . PHE   G  367 ? 0.24142 0.24142 0.24142 0.00000  0.00000  0.00000  367 PHE   C CZ  
11519 N N   . LEU   G  368 ? 0.39271 0.39271 0.39271 0.00000  0.00000  0.00000  368 LEU   C N   
11520 C CA  . LEU   G  368 ? 0.27817 0.27817 0.27817 -0.00000 0.00000  0.00000  368 LEU   C CA  
11521 C C   . LEU   G  368 ? 0.28765 0.28765 0.28765 0.00000  0.00000  0.00000  368 LEU   C C   
11522 O O   . LEU   G  368 ? 0.39546 0.39546 0.39546 0.00000  0.00000  0.00000  368 LEU   C O   
11523 C CB  . LEU   G  368 ? 0.24859 0.24859 0.24859 0.00000  -0.00000 0.00000  368 LEU   C CB  
11524 C CG  . LEU   G  368 ? 0.38279 0.38279 0.38279 0.00000  0.00000  0.00000  368 LEU   C CG  
11525 C CD1 . LEU   G  368 ? 0.32936 0.32936 0.32936 -0.00000 0.00000  0.00000  368 LEU   C CD1 
11526 C CD2 . LEU   G  368 ? 0.35031 0.35031 0.35031 0.00000  0.00000  0.00000  368 LEU   C CD2 
11527 N N   . VAL   G  369 ? 0.21293 0.21293 0.21293 0.00000  0.00000  0.00000  369 VAL   C N   
11528 C CA  . VAL   G  369 ? 0.24257 0.24257 0.24257 0.00000  0.00000  0.00000  369 VAL   C CA  
11529 C C   . VAL   G  369 ? 0.21071 0.21071 0.21071 0.00000  0.00000  0.00000  369 VAL   C C   
11530 O O   . VAL   G  369 ? 0.33035 0.33035 0.33035 0.00000  0.00000  0.00000  369 VAL   C O   
11531 C CB  . VAL   G  369 ? 0.32149 0.32149 0.32149 0.00000  0.00000  0.00000  369 VAL   C CB  
11532 C CG1 . VAL   G  369 ? 0.19190 0.19190 0.19190 -0.00000 0.00000  0.00000  369 VAL   C CG1 
11533 C CG2 . VAL   G  369 ? 0.28554 0.28554 0.28554 -0.00000 0.00000  0.00000  369 VAL   C CG2 
11534 N N   . PHE   G  370 ? 0.39633 0.39633 0.39633 0.00000  0.00000  0.00000  370 PHE   C N   
11535 C CA  . PHE   G  370 ? 0.16386 0.16386 0.16386 0.00000  0.00000  0.00000  370 PHE   C CA  
11536 C C   . PHE   G  370 ? 0.33916 0.33916 0.33916 0.00000  0.00000  0.00000  370 PHE   C C   
11537 O O   . PHE   G  370 ? 0.31665 0.31665 0.31665 0.00000  0.00000  0.00000  370 PHE   C O   
11538 C CB  . PHE   G  370 ? 0.25865 0.25865 0.25865 0.00000  0.00000  0.00000  370 PHE   C CB  
11539 C CG  . PHE   G  370 ? 0.38539 0.38539 0.38539 0.00000  0.00000  0.00000  370 PHE   C CG  
11540 C CD1 . PHE   G  370 ? 0.26539 0.26539 0.26539 0.00000  0.00000  0.00000  370 PHE   C CD1 
11541 C CD2 . PHE   G  370 ? 0.44602 0.44602 0.44602 -0.00000 0.00000  0.00000  370 PHE   C CD2 
11542 C CE1 . PHE   G  370 ? 0.39405 0.39405 0.39405 0.00000  0.00000  0.00000  370 PHE   C CE1 
11543 C CE2 . PHE   G  370 ? 0.24822 0.24822 0.24822 0.00000  0.00000  0.00000  370 PHE   C CE2 
11544 C CZ  . PHE   G  370 ? 0.38764 0.38764 0.38764 0.00000  0.00000  0.00000  370 PHE   C CZ  
11545 N N   . ILE   G  371 ? 0.28636 0.28636 0.28636 -0.00000 0.00000  0.00000  371 ILE   C N   
11546 C CA  . ILE   G  371 ? 0.23290 0.23290 0.23290 0.00000  0.00000  0.00000  371 ILE   C CA  
11547 C C   . ILE   G  371 ? 0.24454 0.24454 0.24454 -0.00000 0.00000  0.00000  371 ILE   C C   
11548 O O   . ILE   G  371 ? 0.37002 0.37002 0.37002 0.00000  0.00000  -0.00000 371 ILE   C O   
11549 C CB  . ILE   G  371 ? 0.34834 0.34834 0.34834 0.00000  0.00000  0.00000  371 ILE   C CB  
11550 C CG1 . ILE   G  371 ? 0.21647 0.21647 0.21647 0.00000  0.00000  0.00000  371 ILE   C CG1 
11551 C CG2 . ILE   G  371 ? 0.16436 0.16436 0.16436 0.00000  0.00000  0.00000  371 ILE   C CG2 
11552 C CD1 . ILE   G  371 ? 0.18946 0.18946 0.18946 0.00000  -0.00000 0.00000  371 ILE   C CD1 
11553 N N   . GLY   G  372 ? 0.30832 0.30832 0.30832 0.00000  0.00000  -0.00000 372 GLY   C N   
11554 C CA  . GLY   G  372 ? 0.19811 0.19811 0.19811 0.00000  -0.00000 0.00000  372 GLY   C CA  
11555 C C   . GLY   G  372 ? 0.30359 0.30359 0.30359 0.00000  0.00000  0.00000  372 GLY   C C   
11556 O O   . GLY   G  372 ? 0.30577 0.30577 0.30577 -0.00000 0.00000  0.00000  372 GLY   C O   
11557 N N   . MET   G  373 ? 0.35319 0.35319 0.35319 -0.00000 0.00000  0.00000  373 MET   C N   
11558 C CA  . MET   G  373 ? 0.51829 0.51829 0.51829 0.00000  0.00000  0.00000  373 MET   C CA  
11559 C C   . MET   G  373 ? 0.48981 0.48981 0.48981 0.00000  0.00000  0.00000  373 MET   C C   
11560 O O   . MET   G  373 ? 0.43019 0.43019 0.43019 0.00000  0.00000  0.00000  373 MET   C O   
11561 C CB  . MET   G  373 ? 0.26503 0.26503 0.26503 0.00000  0.00000  0.00000  373 MET   C CB  
11562 C CG  . MET   G  373 ? 0.54143 0.54143 0.54143 0.00000  -0.00000 0.00000  373 MET   C CG  
11563 S SD  . MET   G  373 ? 0.45924 0.45924 0.45924 0.00000  0.00000  0.00000  373 MET   C SD  
11564 C CE  . MET   G  373 ? 0.15251 0.15251 0.15251 0.00000  0.00000  0.00000  373 MET   C CE  
11565 N N   . THR   G  374 ? 0.32564 0.32564 0.32564 -0.00000 0.00000  0.00000  374 THR   C N   
11566 C CA  . THR   G  374 ? 0.34301 0.34301 0.34301 -0.00000 0.00000  0.00000  374 THR   C CA  
11567 C C   . THR   G  374 ? 0.30386 0.30386 0.30386 -0.00000 0.00000  0.00000  374 THR   C C   
11568 O O   . THR   G  374 ? 0.43838 0.43838 0.43838 -0.00000 0.00000  0.00000  374 THR   C O   
11569 C CB  . THR   G  374 ? 0.45672 0.45672 0.45672 0.00000  0.00000  0.00000  374 THR   C CB  
11570 O OG1 . THR   G  374 ? 0.39279 0.39279 0.39279 0.00000  0.00000  0.00000  374 THR   C OG1 
11571 C CG2 . THR   G  374 ? 0.26133 0.26133 0.26133 -0.00000 0.00000  0.00000  374 THR   C CG2 
11572 N N   . GLU   G  375 ? 0.43089 0.43089 0.43089 0.00000  0.00000  0.00000  375 GLU   C N   
11573 C CA  . GLU   G  375 ? 0.27298 0.27298 0.27298 -0.00000 0.00000  0.00000  375 GLU   C CA  
11574 C C   . GLU   G  375 ? 0.46102 0.46102 0.46102 0.00000  0.00000  0.00000  375 GLU   C C   
11575 O O   . GLU   G  375 ? 0.28489 0.28489 0.28489 0.00000  0.00000  0.00000  375 GLU   C O   
11576 C CB  . GLU   G  375 ? 0.43582 0.43582 0.43582 0.00000  0.00000  0.00000  375 GLU   C CB  
11577 C CG  . GLU   G  375 ? 0.29215 0.29215 0.29215 -0.00000 0.00000  0.00000  375 GLU   C CG  
11578 C CD  . GLU   G  375 ? 0.42338 0.42338 0.42338 -0.00000 0.00000  0.00000  375 GLU   C CD  
11579 O OE1 . GLU   G  375 ? 0.49093 0.49093 0.49093 0.00000  0.00000  0.00000  375 GLU   C OE1 
11580 O OE2 . GLU   G  375 ? 0.47881 0.47881 0.47881 0.00000  0.00000  0.00000  375 GLU   C OE2 
11581 N N   . ILE   G  376 ? 0.36341 0.36341 0.36341 -0.00000 0.00000  0.00000  376 ILE   C N   
11582 C CA  . ILE   G  376 ? 0.36627 0.36627 0.36627 -0.00000 0.00000  0.00000  376 ILE   C CA  
11583 C C   . ILE   G  376 ? 0.41529 0.41529 0.41529 0.00000  0.00000  0.00000  376 ILE   C C   
11584 O O   . ILE   G  376 ? 0.51102 0.51102 0.51102 0.00000  -0.00000 0.00000  376 ILE   C O   
11585 C CB  . ILE   G  376 ? 0.50457 0.50457 0.50457 0.00000  0.00000  0.00000  376 ILE   C CB  
11586 C CG1 . ILE   G  376 ? 0.37073 0.37073 0.37073 -0.00000 -0.00000 0.00000  376 ILE   C CG1 
11587 C CG2 . ILE   G  376 ? 0.22686 0.22686 0.22686 0.00000  0.00000  0.00000  376 ILE   C CG2 
11588 C CD1 . ILE   G  376 ? 0.63454 0.63454 0.63454 0.00000  0.00000  0.00000  376 ILE   C CD1 
11589 N N   . SER   G  377 ? 0.36891 0.36891 0.36891 0.00000  0.00000  0.00000  377 SER   C N   
11590 C CA  . SER   G  377 ? 0.54038 0.54038 0.54038 0.00000  0.00000  0.00000  377 SER   C CA  
11591 C C   . SER   G  377 ? 0.33757 0.33757 0.33757 0.00000  0.00000  0.00000  377 SER   C C   
11592 O O   . SER   G  377 ? 0.64451 0.64451 0.64451 0.00000  0.00000  0.00000  377 SER   C O   
11593 C CB  . SER   G  377 ? 0.25972 0.25972 0.25972 0.00000  0.00000  0.00000  377 SER   C CB  
11594 O OG  . SER   G  377 ? 0.33669 0.33669 0.33669 0.00000  0.00000  0.00000  377 SER   C OG  
11595 N N   . THR   G  378 ? 0.45890 0.45890 0.45890 -0.00000 0.00000  0.00000  378 THR   C N   
11596 C CA  . THR   G  378 ? 0.28318 0.28318 0.28318 0.00000  0.00000  0.00000  378 THR   C CA  
11597 C C   . THR   G  378 ? 0.47772 0.47772 0.47772 0.00000  0.00000  0.00000  378 THR   C C   
11598 O O   . THR   G  378 ? 0.37303 0.37303 0.37303 0.00000  0.00000  0.00000  378 THR   C O   
11599 C CB  . THR   G  378 ? 0.44178 0.44178 0.44178 0.00000  0.00000  0.00000  378 THR   C CB  
11600 O OG1 . THR   G  378 ? 0.37585 0.37585 0.37585 0.00000  0.00000  0.00000  378 THR   C OG1 
11601 C CG2 . THR   G  378 ? 0.12784 0.12784 0.12784 0.00000  0.00000  0.00000  378 THR   C CG2 
11602 N N   . CYS   G  379 ? 0.28831 0.28831 0.28831 0.00000  0.00000  0.00000  379 CYS   C N   
11603 C CA  . CYS   G  379 ? 0.26655 0.26655 0.26655 -0.00000 0.00000  0.00000  379 CYS   C CA  
11604 C C   . CYS   G  379 ? 0.36876 0.36876 0.36876 -0.00000 0.00000  0.00000  379 CYS   C C   
11605 O O   . CYS   G  379 ? 0.43668 0.43668 0.43668 0.00000  0.00000  0.00000  379 CYS   C O   
11606 C CB  . CYS   G  379 ? 0.27391 0.27391 0.27391 0.00000  0.00000  0.00000  379 CYS   C CB  
11607 S SG  . CYS   G  379 ? 0.41988 0.41988 0.41988 -0.00000 0.00000  0.00000  379 CYS   C SG  
11608 N N   . GLU   G  380 ? 0.39755 0.39755 0.39755 0.00000  0.00000  0.00000  380 GLU   C N   
11609 C CA  . GLU   G  380 ? 0.21396 0.21396 0.21396 0.00000  0.00000  0.00000  380 GLU   C CA  
11610 C C   . GLU   G  380 ? 0.42031 0.42031 0.42031 0.00000  0.00000  0.00000  380 GLU   C C   
11611 O O   . GLU   G  380 ? 0.40586 0.40586 0.40586 0.00000  0.00000  0.00000  380 GLU   C O   
11612 C CB  . GLU   G  380 ? 0.35931 0.35931 0.35931 0.00000  0.00000  0.00000  380 GLU   C CB  
11613 C CG  . GLU   G  380 ? 0.52105 0.52105 0.52105 0.00000  0.00000  0.00000  380 GLU   C CG  
11614 C CD  . GLU   G  380 ? 0.46754 0.46754 0.46754 0.00000  0.00000  0.00000  380 GLU   C CD  
11615 O OE1 . GLU   G  380 ? 0.53119 0.53119 0.53119 -0.00000 0.00000  0.00000  380 GLU   C OE1 
11616 O OE2 . GLU   G  380 ? 0.62099 0.62099 0.62099 0.00000  0.00000  0.00000  380 GLU   C OE2 
11617 N N   . ALA   G  381 ? 0.28905 0.28905 0.28905 0.00000  0.00000  0.00000  381 ALA   C N   
11618 C CA  . ALA   G  381 ? 0.52333 0.52333 0.52333 0.00000  0.00000  0.00000  381 ALA   C CA  
11619 C C   . ALA   G  381 ? 0.40161 0.40161 0.40161 0.00000  0.00000  0.00000  381 ALA   C C   
11620 O O   . ALA   G  381 ? 0.40941 0.40941 0.40941 0.00000  0.00000  0.00000  381 ALA   C O   
11621 C CB  . ALA   G  381 ? 0.27612 0.27612 0.27612 -0.00000 0.00000  0.00000  381 ALA   C CB  
11622 N N   . THR   G  382 ? 0.39150 0.39150 0.39150 0.00000  0.00000  0.00000  382 THR   C N   
11623 C CA  . THR   G  382 ? 0.38621 0.38621 0.38621 0.00000  0.00000  0.00000  382 THR   C CA  
11624 C C   . THR   G  382 ? 0.32457 0.32457 0.32457 0.00000  0.00000  0.00000  382 THR   C C   
11625 O O   . THR   G  382 ? 0.67339 0.67339 0.67339 0.00000  0.00000  0.00000  382 THR   C O   
11626 C CB  . THR   G  382 ? 0.25591 0.25591 0.25591 -0.00000 0.00000  0.00000  382 THR   C CB  
11627 O OG1 . THR   G  382 ? 0.36853 0.36853 0.36853 -0.00000 0.00000  0.00000  382 THR   C OG1 
11628 C CG2 . THR   G  382 ? 0.39254 0.39254 0.39254 0.00000  0.00000  0.00000  382 THR   C CG2 
11629 N N   . VAL   G  383 ? 0.44124 0.44124 0.44124 -0.00000 0.00000  0.00000  383 VAL   C N   
11630 C CA  . VAL   G  383 ? 0.30620 0.30620 0.30620 0.00000  0.00000  0.00000  383 VAL   C CA  
11631 C C   . VAL   G  383 ? 0.48354 0.48354 0.48354 0.00000  0.00000  0.00000  383 VAL   C C   
11632 O O   . VAL   G  383 ? 0.42974 0.42974 0.42974 0.00000  0.00000  0.00000  383 VAL   C O   
11633 C CB  . VAL   G  383 ? 0.56853 0.56853 0.56853 -0.00000 0.00000  0.00000  383 VAL   C CB  
11634 C CG1 . VAL   G  383 ? 0.31590 0.31590 0.31590 0.00000  0.00000  0.00000  383 VAL   C CG1 
11635 C CG2 . VAL   G  383 ? 0.37554 0.37554 0.37554 0.00000  0.00000  0.00000  383 VAL   C CG2 
11636 N N   . SER   G  384 ? 0.57020 0.57020 0.57020 -0.00000 0.00000  0.00000  384 SER   C N   
11637 C CA  . SER   G  384 ? 0.32350 0.32350 0.32350 0.00000  0.00000  0.00000  384 SER   C CA  
11638 C C   . SER   G  384 ? 0.63249 0.63249 0.63249 -0.00000 0.00000  0.00000  384 SER   C C   
11639 O O   . SER   G  384 ? 0.49021 0.49021 0.49021 -0.00000 0.00000  0.00000  384 SER   C O   
11640 C CB  . SER   G  384 ? 0.35385 0.35385 0.35385 0.00000  0.00000  0.00000  384 SER   C CB  
11641 O OG  . SER   G  384 ? 0.69842 0.69842 0.69842 -0.00000 0.00000  0.00000  384 SER   C OG  
11642 N N   . GLU   G  385 ? 0.46591 0.46591 0.46591 0.00000  0.00000  0.00000  385 GLU   C N   
11643 C CA  . GLU   G  385 ? 0.57646 0.57646 0.57646 0.00000  0.00000  0.00000  385 GLU   C CA  
11644 C C   . GLU   G  385 ? 0.57161 0.57161 0.57161 0.00000  0.00000  0.00000  385 GLU   C C   
11645 O O   . GLU   G  385 ? 0.54572 0.54572 0.54572 0.00000  0.00000  0.00000  385 GLU   C O   
11646 C CB  . GLU   G  385 ? 0.29707 0.29707 0.29707 0.00000  0.00000  0.00000  385 GLU   C CB  
11647 C CG  . GLU   G  385 ? 0.47184 0.47184 0.47184 0.00000  0.00000  -0.00000 385 GLU   C CG  
11648 C CD  . GLU   G  385 ? 0.68600 0.68600 0.68600 0.00000  0.00000  0.00000  385 GLU   C CD  
11649 O OE1 . GLU   G  385 ? 0.66560 0.66560 0.66560 0.00000  0.00000  -0.00000 385 GLU   C OE1 
11650 O OE2 . GLU   G  385 ? 0.50300 0.50300 0.50300 0.00000  0.00000  0.00000  385 GLU   C OE2 
11651 N N   . GLY   G  386 ? 0.45458 0.45458 0.45458 0.00000  0.00000  0.00000  386 GLY   C N   
11652 C CA  . GLY   G  386 ? 0.27925 0.27925 0.27925 0.00000  0.00000  0.00000  386 GLY   C CA  
11653 C C   . GLY   G  386 ? 0.51620 0.51620 0.51620 0.00000  -0.00000 0.00000  386 GLY   C C   
11654 O O   . GLY   G  386 ? 0.44762 0.44762 0.44762 0.00000  0.00000  0.00000  386 GLY   C O   
11655 N N   . GLN   G  387 ? 0.44998 0.44998 0.44998 0.00000  0.00000  0.00000  387 GLN   C N   
11656 C CA  . GLN   G  387 ? 0.40807 0.40807 0.40807 0.00000  0.00000  0.00000  387 GLN   C CA  
11657 C C   . GLN   G  387 ? 0.65169 0.65169 0.65169 0.00000  0.00000  0.00000  387 GLN   C C   
11658 O O   . GLN   G  387 ? 0.56476 0.56476 0.56476 0.00000  0.00000  0.00000  387 GLN   C O   
11659 C CB  . GLN   G  387 ? 0.39358 0.39358 0.39358 0.00000  0.00000  0.00000  387 GLN   C CB  
11660 C CG  . GLN   G  387 ? 0.40072 0.40072 0.40072 0.00000  0.00000  0.00000  387 GLN   C CG  
11661 C CD  . GLN   G  387 ? 0.50204 0.50204 0.50204 0.00000  0.00000  0.00000  387 GLN   C CD  
11662 O OE1 . GLN   G  387 ? 0.56490 0.56490 0.56490 0.00000  0.00000  0.00000  387 GLN   C OE1 
11663 N NE2 . GLN   G  387 ? 0.41820 0.41820 0.41820 -0.00000 0.00000  0.00000  387 GLN   C NE2 
11664 N N   . HIS   G  388 ? 0.40917 0.40917 0.40917 0.00000  0.00000  0.00000  388 HIS   C N   
11665 C CA  . HIS   G  388 ? 0.55221 0.55221 0.55221 -0.00000 0.00000  0.00000  388 HIS   C CA  
11666 C C   . HIS   G  388 ? 0.72509 0.72509 0.72509 -0.00000 0.00000  0.00000  388 HIS   C C   
11667 O O   . HIS   G  388 ? 0.39684 0.39684 0.39684 0.00000  0.00000  0.00000  388 HIS   C O   
11668 C CB  . HIS   G  388 ? 0.27379 0.27379 0.27379 -0.00000 0.00000  0.00000  388 HIS   C CB  
11669 C CG  . HIS   G  388 ? 0.49331 0.49331 0.49331 0.00000  0.00000  0.00000  388 HIS   C CG  
11670 N ND1 . HIS   G  388 ? 0.50545 0.50545 0.50545 0.00000  0.00000  0.00000  388 HIS   C ND1 
11671 C CD2 . HIS   G  388 ? 0.35313 0.35313 0.35313 -0.00000 0.00000  0.00000  388 HIS   C CD2 
11672 C CE1 . HIS   G  388 ? 0.45879 0.45879 0.45879 -0.00000 0.00000  0.00000  388 HIS   C CE1 
11673 N NE2 . HIS   G  388 ? 0.40738 0.40738 0.40738 0.00000  0.00000  0.00000  388 HIS   C NE2 
11674 N N   . VAL   G  389 ? 0.34481 0.34481 0.34481 0.00000  -0.00000 0.00000  389 VAL   C N   
11675 C CA  . VAL   G  389 ? 0.50190 0.50190 0.50190 0.00000  0.00000  0.00000  389 VAL   C CA  
11676 C C   . VAL   G  389 ? 0.48852 0.48852 0.48852 0.00000  0.00000  0.00000  389 VAL   C C   
11677 O O   . VAL   G  389 ? 0.66752 0.66752 0.66752 0.00000  0.00000  0.00000  389 VAL   C O   
11678 C CB  . VAL   G  389 ? 0.56759 0.56759 0.56759 -0.00000 0.00000  0.00000  389 VAL   C CB  
11679 C CG1 . VAL   G  389 ? 0.37507 0.37507 0.37507 -0.00000 0.00000  0.00000  389 VAL   C CG1 
11680 C CG2 . VAL   G  389 ? 0.30271 0.30271 0.30271 -0.00000 -0.00000 0.00000  389 VAL   C CG2 
11681 N N   . ASN   G  390 ? 0.38057 0.38057 0.38057 0.00000  0.00000  0.00000  390 ASN   C N   
11682 C CA  . ASN   G  390 ? 0.42443 0.42443 0.42443 0.00000  0.00000  0.00000  390 ASN   C CA  
11683 C C   . ASN   G  390 ? 0.74565 0.74565 0.74565 0.00000  0.00000  0.00000  390 ASN   C C   
11684 O O   . ASN   G  390 ? 0.46036 0.46036 0.46036 -0.00000 0.00000  0.00000  390 ASN   C O   
11685 C CB  . ASN   G  390 ? 0.58528 0.58528 0.58528 0.00000  0.00000  0.00000  390 ASN   C CB  
11686 C CG  . ASN   G  390 ? 0.50357 0.50357 0.50357 0.00000  0.00000  0.00000  390 ASN   C CG  
11687 O OD1 . ASN   G  390 ? 0.63635 0.63635 0.63635 0.00000  0.00000  0.00000  390 ASN   C OD1 
11688 N ND2 . ASN   G  390 ? 0.62942 0.62942 0.62942 -0.00000 0.00000  0.00000  390 ASN   C ND2 
11689 N N   . ARG   G  391 ? 0.38764 0.38764 0.38764 -0.00000 0.00000  0.00000  391 ARG   C N   
11690 C CA  . ARG   G  391 ? 0.52182 0.52182 0.52182 -0.00000 0.00000  0.00000  391 ARG   C CA  
11691 C C   . ARG   G  391 ? 0.36993 0.36993 0.36993 0.00000  0.00000  0.00000  391 ARG   C C   
11692 O O   . ARG   G  391 ? 0.50519 0.50519 0.50519 0.00000  0.00000  0.00000  391 ARG   C O   
11693 C CB  . ARG   G  391 ? 0.26063 0.26063 0.26063 0.00000  0.00000  -0.00000 391 ARG   C CB  
11694 C CG  . ARG   G  391 ? 0.38310 0.38310 0.38310 -0.00000 -0.00000 0.00000  391 ARG   C CG  
11695 C CD  . ARG   G  391 ? 0.50453 0.50453 0.50453 -0.00000 0.00000  0.00000  391 ARG   C CD  
11696 N NE  . ARG   G  391 ? 0.40778 0.40778 0.40778 0.00000  -0.00000 0.00000  391 ARG   C NE  
11697 C CZ  . ARG   G  391 ? 0.93426 0.93426 0.93426 0.00000  0.00000  -0.00000 391 ARG   C CZ  
11698 N NH1 . ARG   G  391 ? 0.42000 0.42000 0.42000 0.00000  0.00000  0.00000  391 ARG   C NH1 
11699 N NH2 . ARG   G  391 ? 0.43200 0.43200 0.43200 -0.00000 0.00000  0.00000  391 ARG   C NH2 
11700 N N   . GLY   G  392 ? 0.45223 0.45223 0.45223 -0.00000 0.00000  0.00000  392 GLY   C N   
11701 C CA  . GLY   G  392 ? 0.40698 0.40698 0.40698 0.00000  0.00000  0.00000  392 GLY   C CA  
11702 C C   . GLY   G  392 ? 0.51820 0.51820 0.51820 0.00000  0.00000  0.00000  392 GLY   C C   
11703 O O   . GLY   G  392 ? 0.50016 0.50016 0.50016 -0.00000 0.00000  0.00000  392 GLY   C O   
11704 N N   . ASP   G  393 ? 0.30408 0.30408 0.30408 0.00000  0.00000  0.00000  393 ASP   C N   
11705 C CA  . ASP   G  393 ? 0.46481 0.46481 0.46481 0.00000  0.00000  0.00000  393 ASP   C CA  
11706 C C   . ASP   G  393 ? 0.39585 0.39585 0.39585 0.00000  0.00000  0.00000  393 ASP   C C   
11707 O O   . ASP   G  393 ? 0.63718 0.63718 0.63718 -0.00000 0.00000  0.00000  393 ASP   C O   
11708 C CB  . ASP   G  393 ? 0.34626 0.34626 0.34626 0.00000  0.00000  0.00000  393 ASP   C CB  
11709 C CG  . ASP   G  393 ? 0.71212 0.71212 0.71212 0.00000  0.00000  0.00000  393 ASP   C CG  
11710 O OD1 . ASP   G  393 ? 0.66909 0.66909 0.66909 0.00000  0.00000  0.00000  393 ASP   C OD1 
11711 O OD2 . ASP   G  393 ? 0.51838 0.51838 0.51838 0.00000  -0.00000 0.00000  393 ASP   C OD2 
11712 N N   . ASP   G  394 ? 0.62008 0.62008 0.62008 0.00000  0.00000  0.00000  394 ASP   C N   
11713 C CA  . ASP   G  394 ? 0.31253 0.31253 0.31253 0.00000  0.00000  0.00000  394 ASP   C CA  
11714 C C   . ASP   G  394 ? 0.65046 0.65046 0.65046 0.00000  0.00000  0.00000  394 ASP   C C   
11715 O O   . ASP   G  394 ? 0.43294 0.43294 0.43294 -0.00000 0.00000  0.00000  394 ASP   C O   
11716 C CB  . ASP   G  394 ? 0.55947 0.55947 0.55947 0.00000  0.00000  0.00000  394 ASP   C CB  
11717 C CG  . ASP   G  394 ? 0.42651 0.42651 0.42651 -0.00000 0.00000  0.00000  394 ASP   C CG  
11718 O OD1 . ASP   G  394 ? 0.98833 0.98833 0.98833 -0.00000 0.00000  0.00000  394 ASP   C OD1 
11719 O OD2 . ASP   G  394 ? 0.92817 0.92817 0.92817 -0.00000 0.00000  0.00000  394 ASP   C OD2 
11720 N N   . LEU   G  395 ? 0.31491 0.31491 0.31491 0.00000  0.00000  0.00000  395 LEU   C N   
11721 C CA  . LEU   G  395 ? 0.55481 0.55481 0.55481 -0.00000 0.00000  0.00000  395 LEU   C CA  
11722 C C   . LEU   G  395 ? 0.46533 0.46533 0.46533 0.00000  0.00000  0.00000  395 LEU   C C   
11723 O O   . LEU   G  395 ? 0.43322 0.43322 0.43322 0.00000  0.00000  0.00000  395 LEU   C O   
11724 C CB  . LEU   G  395 ? 0.26946 0.26946 0.26946 0.00000  0.00000  0.00000  395 LEU   C CB  
11725 C CG  . LEU   G  395 ? 0.45278 0.45278 0.45278 -0.00000 -0.00000 0.00000  395 LEU   C CG  
11726 C CD1 . LEU   G  395 ? 0.26277 0.26277 0.26277 -0.00000 0.00000  0.00000  395 LEU   C CD1 
11727 C CD2 . LEU   G  395 ? 0.38980 0.38980 0.38980 0.00000  0.00000  0.00000  395 LEU   C CD2 
11728 N N   . GLY   G  396 ? 0.34625 0.34625 0.34625 0.00000  0.00000  0.00000  396 GLY   C N   
11729 C CA  . GLY   G  396 ? 0.45261 0.45261 0.45261 0.00000  0.00000  0.00000  396 GLY   C CA  
11730 C C   . GLY   G  396 ? 0.40408 0.40408 0.40408 0.00000  0.00000  0.00000  396 GLY   C C   
11731 O O   . GLY   G  396 ? 0.44779 0.44779 0.44779 0.00000  0.00000  0.00000  396 GLY   C O   
11732 N N   . MET   G  397 ? 0.43247 0.43247 0.43247 0.00000  0.00000  0.00000  397 MET   C N   
11733 C CA  . MET   G  397 ? 0.41824 0.41824 0.41824 0.00000  0.00000  0.00000  397 MET   C CA  
11734 C C   . MET   G  397 ? 0.61468 0.61468 0.61468 0.00000  0.00000  0.00000  397 MET   C C   
11735 O O   . MET   G  397 ? 0.47827 0.47827 0.47827 -0.00000 0.00000  0.00000  397 MET   C O   
11736 C CB  . MET   G  397 ? 0.39069 0.39069 0.39069 0.00000  0.00000  0.00000  397 MET   C CB  
11737 C CG  . MET   G  397 ? 0.44744 0.44744 0.44744 0.00000  0.00000  0.00000  397 MET   C CG  
11738 S SD  . MET   G  397 ? 0.57917 0.57917 0.57917 -0.00000 0.00000  0.00000  397 MET   C SD  
11739 C CE  . MET   G  397 ? 0.30365 0.30365 0.30365 0.00000  -0.00000 0.00000  397 MET   C CE  
11740 N N   . PHE   G  398 ? 0.39617 0.39617 0.39617 -0.00000 0.00000  0.00000  398 PHE   C N   
11741 C CA  . PHE   G  398 ? 0.31109 0.31109 0.31109 -0.00000 0.00000  0.00000  398 PHE   C CA  
11742 C C   . PHE   G  398 ? 0.43495 0.43495 0.43495 0.00000  -0.00000 0.00000  398 PHE   C C   
11743 O O   . PHE   G  398 ? 0.55793 0.55793 0.55793 0.00000  0.00000  0.00000  398 PHE   C O   
11744 C CB  . PHE   G  398 ? 0.31213 0.31213 0.31213 0.00000  0.00000  0.00000  398 PHE   C CB  
11745 C CG  . PHE   G  398 ? 0.48496 0.48496 0.48496 0.00000  0.00000  0.00000  398 PHE   C CG  
11746 C CD1 . PHE   G  398 ? 0.31610 0.31610 0.31610 0.00000  0.00000  0.00000  398 PHE   C CD1 
11747 C CD2 . PHE   G  398 ? 0.40170 0.40170 0.40170 -0.00000 0.00000  0.00000  398 PHE   C CD2 
11748 C CE1 . PHE   G  398 ? 0.46859 0.46859 0.46859 -0.00000 0.00000  0.00000  398 PHE   C CE1 
11749 C CE2 . PHE   G  398 ? 0.35160 0.35160 0.35160 0.00000  0.00000  0.00000  398 PHE   C CE2 
11750 C CZ  . PHE   G  398 ? 0.44452 0.44452 0.44452 0.00000  0.00000  0.00000  398 PHE   C CZ  
11751 N N   . HIS   G  399 ? 0.47792 0.47792 0.47792 0.00000  0.00000  0.00000  399 HIS   C N   
11752 C CA  . HIS   G  399 ? 0.58423 0.58423 0.58423 0.00000  0.00000  0.00000  399 HIS   C CA  
11753 C C   . HIS   G  399 ? 0.31141 0.31141 0.31141 0.00000  0.00000  0.00000  399 HIS   C C   
11754 O O   . HIS   G  399 ? 0.67108 0.67108 0.67108 0.00000  0.00000  0.00000  399 HIS   C O   
11755 C CB  . HIS   G  399 ? 0.27976 0.27976 0.27976 0.00000  0.00000  0.00000  399 HIS   C CB  
11756 C CG  . HIS   G  399 ? 0.32730 0.32730 0.32730 -0.00000 0.00000  0.00000  399 HIS   C CG  
11757 N ND1 . HIS   G  399 ? 0.42919 0.42919 0.42919 0.00000  0.00000  0.00000  399 HIS   C ND1 
11758 C CD2 . HIS   G  399 ? 0.52270 0.52270 0.52270 -0.00000 0.00000  0.00000  399 HIS   C CD2 
11759 C CE1 . HIS   G  399 ? 0.65277 0.65277 0.65277 0.00000  0.00000  0.00000  399 HIS   C CE1 
11760 N NE2 . HIS   G  399 ? 0.28815 0.28815 0.28815 0.00000  0.00000  -0.00000 399 HIS   C NE2 
11761 N N   . PHE   G  400 ? 0.52840 0.52840 0.52840 -0.00000 0.00000  0.00000  400 PHE   C N   
11762 C CA  . PHE   G  400 ? 0.29370 0.29370 0.29370 -0.00000 0.00000  0.00000  400 PHE   C CA  
11763 C C   . PHE   G  400 ? 0.40301 0.40301 0.40301 0.00000  0.00000  0.00000  400 PHE   C C   
11764 O O   . PHE   G  400 ? 0.53586 0.53586 0.53586 0.00000  0.00000  0.00000  400 PHE   C O   
11765 C CB  . PHE   G  400 ? 0.51759 0.51759 0.51759 -0.00000 -0.00000 0.00000  400 PHE   C CB  
11766 C CG  . PHE   G  400 ? 0.26336 0.26336 0.26336 -0.00000 0.00000  0.00000  400 PHE   C CG  
11767 C CD1 . PHE   G  400 ? 0.50456 0.50456 0.50456 -0.00000 0.00000  0.00000  400 PHE   C CD1 
11768 C CD2 . PHE   G  400 ? 0.51714 0.51714 0.51714 0.00000  0.00000  0.00000  400 PHE   C CD2 
11769 C CE1 . PHE   G  400 ? 0.31038 0.31038 0.31038 0.00000  0.00000  0.00000  400 PHE   C CE1 
11770 C CE2 . PHE   G  400 ? 0.46453 0.46453 0.46453 -0.00000 0.00000  0.00000  400 PHE   C CE2 
11771 C CZ  . PHE   G  400 ? 0.50145 0.50145 0.50145 0.00000  0.00000  0.00000  400 PHE   C CZ  
11772 N N   . GLY   G  401 ? 0.36214 0.36214 0.36214 -0.00000 0.00000  -0.00000 401 GLY   C N   
11773 C CA  . GLY   G  401 ? 0.31057 0.31057 0.31057 0.00000  0.00000  0.00000  401 GLY   C CA  
11774 C C   . GLY   G  401 ? 0.44304 0.44304 0.44304 -0.00000 0.00000  0.00000  401 GLY   C C   
11775 O O   . GLY   G  401 ? 0.52147 0.52147 0.52147 0.00000  0.00000  0.00000  401 GLY   C O   
11776 N N   . GLY   G  402 ? 0.39924 0.39924 0.39924 0.00000  0.00000  0.00000  402 GLY   C N   
11777 C CA  . GLY   G  402 ? 0.30558 0.30558 0.30558 0.00000  0.00000  0.00000  402 GLY   C CA  
11778 C C   . GLY   G  402 ? 0.67589 0.67589 0.67589 0.00000  0.00000  0.00000  402 GLY   C C   
11779 O O   . GLY   G  402 ? 0.44308 0.44308 0.44308 0.00000  0.00000  0.00000  402 GLY   C O   
11780 O OXT . GLY   G  402 ? 0.55939 0.55939 0.55939 -0.00000 0.00000  0.00000  402 GLY   C OXT 
11781 N N   . SER   H  1   ? 0.25721 0.25721 0.25721 0.00000  0.00000  0.00000  404 SER   D N   
11782 C CA  . SER   H  1   ? 0.19540 0.19540 0.19540 0.00000  0.00000  0.00000  404 SER   D CA  
11783 C C   . SER   H  1   ? 0.34010 0.34010 0.34010 0.00000  0.00000  0.00000  404 SER   D C   
11784 O O   . SER   H  1   ? 0.38462 0.38462 0.38462 0.00000  0.00000  0.00000  404 SER   D O   
11785 C CB  . SER   H  1   ? 0.27487 0.27487 0.27487 0.00000  0.00000  0.00000  404 SER   D CB  
11786 O OG  . SER   H  1   ? 0.30956 0.30956 0.30956 0.00000  0.00000  0.00000  404 SER   D OG  
11787 N N   . PHE   H  2   ? 0.22800 0.22800 0.22800 -0.00000 0.00000  0.00000  405 PHE   D N   
11788 C CA  . PHE   H  2   ? 0.30747 0.30747 0.30747 0.00000  0.00000  0.00000  405 PHE   D CA  
11789 C C   . PHE   H  2   ? 0.27798 0.27798 0.27798 0.00000  0.00000  0.00000  405 PHE   D C   
11790 O O   . PHE   H  2   ? 0.39574 0.39574 0.39574 0.00000  0.00000  0.00000  405 PHE   D O   
11791 C CB  . PHE   H  2   ? 0.31610 0.31610 0.31610 -0.00000 -0.00000 0.00000  405 PHE   D CB  
11792 C CG  . PHE   H  2   ? 0.34741 0.34741 0.34741 -0.00000 -0.00000 -0.00000 405 PHE   D CG  
11793 C CD1 . PHE   H  2   ? 0.42712 0.42712 0.42712 -0.00000 0.00000  0.00000  405 PHE   D CD1 
11794 C CD2 . PHE   H  2   ? 0.39092 0.39092 0.39092 0.00000  0.00000  0.00000  405 PHE   D CD2 
11795 C CE1 . PHE   H  2   ? 0.34769 0.34769 0.34769 0.00000  0.00000  0.00000  405 PHE   D CE1 
11796 C CE2 . PHE   H  2   ? 0.29877 0.29877 0.29877 -0.00000 0.00000  0.00000  405 PHE   D CE2 
11797 C CZ  . PHE   H  2   ? 0.37714 0.37714 0.37714 0.00000  0.00000  0.00000  405 PHE   D CZ  
11798 N N   . ALA   H  3   ? 0.27306 0.27306 0.27306 -0.00000 0.00000  0.00000  406 ALA   D N   
11799 C CA  . ALA   H  3   ? 0.32691 0.32691 0.32691 0.00000  0.00000  0.00000  406 ALA   D CA  
11800 C C   . ALA   H  3   ? 0.36668 0.36668 0.36668 0.00000  0.00000  0.00000  406 ALA   D C   
11801 O O   . ALA   H  3   ? 0.35286 0.35286 0.35286 0.00000  0.00000  0.00000  406 ALA   D O   
11802 C CB  . ALA   H  3   ? 0.12174 0.12174 0.12174 0.00000  -0.00000 0.00000  406 ALA   D CB  
11803 N N   . LEU   H  4   ? 0.37591 0.37591 0.37591 0.00000  0.00000  0.00000  407 LEU   D N   
11804 C CA  . LEU   H  4   ? 0.36676 0.36676 0.36676 0.00000  0.00000  0.00000  407 LEU   D CA  
11805 C C   . LEU   H  4   ? 0.17955 0.17955 0.17955 0.00000  -0.00000 0.00000  407 LEU   D C   
11806 O O   . LEU   H  4   ? 0.42725 0.42725 0.42725 0.00000  0.00000  0.00000  407 LEU   D O   
11807 C CB  . LEU   H  4   ? 0.22679 0.22679 0.22679 0.00000  0.00000  0.00000  407 LEU   D CB  
11808 C CG  . LEU   H  4   ? 0.37534 0.37534 0.37534 0.00000  0.00000  0.00000  407 LEU   D CG  
11809 C CD1 . LEU   H  4   ? 0.20302 0.20302 0.20302 -0.00000 0.00000  0.00000  407 LEU   D CD1 
11810 C CD2 . LEU   H  4   ? 0.27835 0.27835 0.27835 0.00000  0.00000  0.00000  407 LEU   D CD2 
11811 N N   . GLY   H  5   ? 0.49069 0.49069 0.49069 -0.00000 0.00000  0.00000  408 GLY   D N   
11812 C CA  . GLY   H  5   ? 0.19575 0.19575 0.19575 0.00000  0.00000  0.00000  408 GLY   D CA  
11813 C C   . GLY   H  5   ? 0.39237 0.39237 0.39237 0.00000  0.00000  0.00000  408 GLY   D C   
11814 O O   . GLY   H  5   ? 0.47247 0.47247 0.47247 0.00000  0.00000  0.00000  408 GLY   D O   
11815 N N   . LEU   H  6   ? 0.16249 0.16249 0.16249 -0.00000 0.00000  0.00000  409 LEU   D N   
11816 C CA  . LEU   H  6   ? 0.40763 0.40763 0.40763 0.00000  0.00000  0.00000  409 LEU   D CA  
11817 C C   . LEU   H  6   ? 0.32399 0.32399 0.32399 0.00000  0.00000  0.00000  409 LEU   D C   
11818 O O   . LEU   H  6   ? 0.38815 0.38815 0.38815 0.00000  0.00000  0.00000  409 LEU   D O   
11819 C CB  . LEU   H  6   ? 0.29721 0.29721 0.29721 -0.00000 0.00000  0.00000  409 LEU   D CB  
11820 C CG  . LEU   H  6   ? 0.38429 0.38429 0.38429 0.00000  0.00000  0.00000  409 LEU   D CG  
11821 C CD1 . LEU   H  6   ? 0.20802 0.20802 0.20802 0.00000  -0.00000 -0.00000 409 LEU   D CD1 
11822 C CD2 . LEU   H  6   ? 0.15168 0.15168 0.15168 -0.00000 0.00000  0.00000  409 LEU   D CD2 
11823 N N   . ARG   H  7   ? 0.39480 0.39480 0.39480 0.00000  0.00000  0.00000  410 ARG   D N   
11824 C CA  . ARG   H  7   ? 0.37868 0.37868 0.37868 -0.00000 0.00000  0.00000  410 ARG   D CA  
11825 C C   . ARG   H  7   ? 0.45339 0.45339 0.45339 0.00000  0.00000  0.00000  410 ARG   D C   
11826 O O   . ARG   H  7   ? 0.59603 0.59603 0.59603 0.00000  -0.00000 0.00000  410 ARG   D O   
11827 C CB  . ARG   H  7   ? 0.21213 0.21213 0.21213 0.00000  0.00000  0.00000  410 ARG   D CB  
11828 C CG  . ARG   H  7   ? 0.23756 0.23756 0.23756 0.00000  0.00000  0.00000  410 ARG   D CG  
11829 C CD  . ARG   H  7   ? 0.37999 0.37999 0.37999 0.00000  0.00000  0.00000  410 ARG   D CD  
11830 N NE  . ARG   H  7   ? 0.62181 0.62181 0.62181 0.00000  0.00000  0.00000  410 ARG   D NE  
11831 C CZ  . ARG   H  7   ? 0.50605 0.50605 0.50605 0.00000  0.00000  0.00000  410 ARG   D CZ  
11832 N NH1 . ARG   H  7   ? 0.54866 0.54866 0.54866 0.00000  0.00000  0.00000  410 ARG   D NH1 
11833 N NH2 . ARG   H  7   ? 0.62292 0.62292 0.62292 0.00000  -0.00000 0.00000  410 ARG   D NH2 
11834 N N   . LYS   H  8   ? 0.46712 0.46712 0.46712 0.00000  0.00000  0.00000  411 LYS   D N   
11835 C CA  . LYS   H  8   ? 0.69586 0.69586 0.69586 0.00000  0.00000  0.00000  411 LYS   D CA  
11836 C C   . LYS   H  8   ? 0.59739 0.59739 0.59739 -0.00000 0.00000  0.00000  411 LYS   D C   
11837 O O   . LYS   H  8   ? 0.55828 0.55828 0.55828 0.00000  0.00000  0.00000  411 LYS   D O   
11838 C CB  . LYS   H  8   ? 0.34276 0.34276 0.34276 0.00000  0.00000  0.00000  411 LYS   D CB  
11839 N N   . ASP   H  9   ? 0.52339 0.52339 0.52339 -0.00000 -0.00000 -0.00000 412 ASP   D N   
11840 C CA  . ASP   H  9   ? 1.17474 1.17474 1.17474 0.00000  0.00000  0.00000  412 ASP   D CA  
11841 C C   . ASP   H  9   ? 0.60882 0.60882 0.60882 0.00000  0.00000  0.00000  412 ASP   D C   
11842 O O   . ASP   H  9   ? 0.99608 0.99608 0.99608 0.00000  -0.00000 -0.00000 412 ASP   D O   
11843 C CB  . ASP   H  9   ? 0.83981 0.83981 0.83981 -0.00000 -0.00000 0.00000  412 ASP   D CB  
11844 C CG  . ASP   H  9   ? 0.95929 0.95929 0.95929 0.00000  0.00000  0.00000  412 ASP   D CG  
11845 O OD1 . ASP   H  9   ? 0.99209 0.99209 0.99209 0.00000  0.00000  0.00000  412 ASP   D OD1 
11846 O OD2 . ASP   H  9   ? 1.27910 1.27910 1.27910 0.00000  0.00000  0.00000  412 ASP   D OD2 
11847 N N   . CYS   H  10  ? 0.95793 0.95793 0.95793 0.00000  0.00000  0.00000  413 CYS   D N   
11848 C CA  . CYS   H  10  ? 0.66565 0.66565 0.66565 0.00000  0.00000  0.00000  413 CYS   D CA  
11849 C C   . CYS   H  10  ? 0.79924 0.79924 0.79924 0.00000  0.00000  0.00000  413 CYS   D C   
11850 O O   . CYS   H  10  ? 0.77396 0.77396 0.77396 0.00000  0.00000  0.00000  413 CYS   D O   
11851 C CB  . CYS   H  10  ? 0.55784 0.55784 0.55784 0.00000  0.00000  0.00000  413 CYS   D CB  
11852 S SG  . CYS   H  10  ? 0.70825 0.70825 0.70825 -0.00000 0.00000  0.00000  413 CYS   D SG  
11853 N N   . ARG   H  11  ? 0.62772 0.62772 0.62772 0.00000  0.00000  0.00000  414 ARG   D N   
11854 C CA  . ARG   H  11  ? 0.91098 0.91098 0.91098 0.00000  0.00000  0.00000  414 ARG   D CA  
11855 C C   . ARG   H  11  ? 1.05447 1.05447 1.05447 0.00000  0.00000  0.00000  414 ARG   D C   
11856 O O   . ARG   H  11  ? 0.70674 0.70674 0.70674 0.00000  0.00000  0.00000  414 ARG   D O   
11857 C CB  . ARG   H  11  ? 0.55192 0.55192 0.55192 0.00000  0.00000  0.00000  414 ARG   D CB  
11858 N N   . ALA   H  12  ? 0.71732 0.71732 0.71732 0.00000  0.00000  0.00000  415 ALA   D N   
11859 C CA  . ALA   H  12  ? 0.57674 0.57674 0.57674 0.00000  0.00000  0.00000  415 ALA   D CA  
11860 C C   . ALA   H  12  ? 0.49922 0.49922 0.49922 -0.00000 0.00000  0.00000  415 ALA   D C   
11861 O O   . ALA   H  12  ? 0.84941 0.84941 0.84941 0.00000  0.00000  0.00000  415 ALA   D O   
11862 C CB  . ALA   H  12  ? 0.31937 0.31937 0.31937 -0.00000 0.00000  0.00000  415 ALA   D CB  
11863 N N   . GLU   H  13  ? 0.42071 0.42071 0.42071 0.00000  0.00000  0.00000  416 GLU   D N   
11864 C CA  . GLU   H  13  ? 0.59402 0.59402 0.59402 0.00000  0.00000  0.00000  416 GLU   D CA  
11865 C C   . GLU   H  13  ? 0.62315 0.62315 0.62315 0.00000  0.00000  0.00000  416 GLU   D C   
11866 O O   . GLU   H  13  ? 0.68860 0.68860 0.68860 0.00000  0.00000  0.00000  416 GLU   D O   
11867 C CB  . GLU   H  13  ? 0.45823 0.45823 0.45823 0.00000  0.00000  0.00000  416 GLU   D CB  
11868 C CG  . GLU   H  13  ? 0.81453 0.81453 0.81453 0.00000  0.00000  0.00000  416 GLU   D CG  
11869 C CD  . GLU   H  13  ? 1.41443 1.41443 1.41443 0.00000  0.00000  0.00000  416 GLU   D CD  
11870 O OE1 . GLU   H  13  ? 1.47014 1.47014 1.47014 -0.00000 -0.00000 0.00000  416 GLU   D OE1 
11871 O OE2 . GLU   H  13  ? 1.46043 1.46043 1.46043 0.00000  0.00000  0.00000  416 GLU   D OE2 
11872 N N   . ILE   H  14  ? 0.47683 0.47683 0.47683 0.00000  0.00000  0.00000  417 ILE   D N   
11873 C CA  . ILE   H  14  ? 0.57468 0.57468 0.57468 0.00000  0.00000  0.00000  417 ILE   D CA  
11874 C C   . ILE   H  14  ? 0.44983 0.44983 0.44983 0.00000  0.00000  0.00000  417 ILE   D C   
11875 O O   . ILE   H  14  ? 0.55543 0.55543 0.55543 0.00000  0.00000  0.00000  417 ILE   D O   
11876 C CB  . ILE   H  14  ? 0.32597 0.32597 0.32597 0.00000  0.00000  0.00000  417 ILE   D CB  
11877 C CG1 . ILE   H  14  ? 0.36866 0.36866 0.36866 0.00000  0.00000  0.00000  417 ILE   D CG1 
11878 C CG2 . ILE   H  14  ? 0.41484 0.41484 0.41484 0.00000  0.00000  0.00000  417 ILE   D CG2 
11879 C CD1 . ILE   H  14  ? 0.49615 0.49615 0.49615 0.00000  0.00000  0.00000  417 ILE   D CD1 
11880 N N   . VAL   H  15  ? 0.59232 0.59232 0.59232 0.00000  0.00000  0.00000  418 VAL   D N   
11881 C CA  . VAL   H  15  ? 0.36054 0.36054 0.36054 0.00000  0.00000  0.00000  418 VAL   D CA  
11882 C C   . VAL   H  15  ? 0.40861 0.40861 0.40861 0.00000  0.00000  0.00000  418 VAL   D C   
11883 O O   . VAL   H  15  ? 0.66322 0.66322 0.66322 -0.00000 0.00000  0.00000  418 VAL   D O   
11884 C CB  . VAL   H  15  ? 0.65644 0.65644 0.65644 0.00000  0.00000  0.00000  418 VAL   D CB  
11885 C CG1 . VAL   H  15  ? 0.25512 0.25512 0.25512 -0.00000 0.00000  0.00000  418 VAL   D CG1 
11886 C CG2 . VAL   H  15  ? 0.23319 0.23319 0.23319 0.00000  0.00000  0.00000  418 VAL   D CG2 
11887 N N   . GLU   H  16  ? 0.53408 0.53408 0.53408 0.00000  0.00000  0.00000  419 GLU   D N   
11888 C CA  . GLU   H  16  ? 0.40073 0.40073 0.40073 -0.00000 0.00000  0.00000  419 GLU   D CA  
11889 C C   . GLU   H  16  ? 0.53297 0.53297 0.53297 0.00000  0.00000  0.00000  419 GLU   D C   
11890 O O   . GLU   H  16  ? 0.53449 0.53449 0.53449 0.00000  0.00000  0.00000  419 GLU   D O   
11891 C CB  . GLU   H  16  ? 0.40951 0.40951 0.40951 0.00000  0.00000  0.00000  419 GLU   D CB  
11892 N N   . LYS   H  17  ? 0.43816 0.43816 0.43816 0.00000  0.00000  0.00000  420 LYS   D N   
11893 C CA  . LYS   H  17  ? 0.46674 0.46674 0.46674 0.00000  0.00000  0.00000  420 LYS   D CA  
11894 C C   . LYS   H  17  ? 0.54930 0.54930 0.54930 -0.00000 0.00000  0.00000  420 LYS   D C   
11895 O O   . LYS   H  17  ? 0.52905 0.52905 0.52905 0.00000  0.00000  0.00000  420 LYS   D O   
11896 C CB  . LYS   H  17  ? 0.24477 0.24477 0.24477 -0.00000 0.00000  0.00000  420 LYS   D CB  
11897 C CG  . LYS   H  17  ? 0.30809 0.30809 0.30809 0.00000  0.00000  0.00000  420 LYS   D CG  
11898 C CD  . LYS   H  17  ? 0.57579 0.57579 0.57579 0.00000  0.00000  0.00000  420 LYS   D CD  
11899 C CE  . LYS   H  17  ? 0.69986 0.69986 0.69986 0.00000  0.00000  0.00000  420 LYS   D CE  
11900 N NZ  . LYS   H  17  ? 0.98983 0.98983 0.98983 -0.00000 0.00000  0.00000  420 LYS   D NZ  
11901 N N   . PHE   H  18  ? 0.41126 0.41126 0.41126 0.00000  0.00000  0.00000  421 PHE   D N   
11902 C CA  . PHE   H  18  ? 0.71115 0.71115 0.71115 -0.00000 0.00000  0.00000  421 PHE   D CA  
11903 C C   . PHE   H  18  ? 0.54912 0.54912 0.54912 -0.00000 0.00000  0.00000  421 PHE   D C   
11904 O O   . PHE   H  18  ? 0.48217 0.48217 0.48217 -0.00000 0.00000  0.00000  421 PHE   D O   
11905 C CB  . PHE   H  18  ? 0.26974 0.26974 0.26974 -0.00000 0.00000  0.00000  421 PHE   D CB  
11906 C CG  . PHE   H  18  ? 0.41197 0.41197 0.41197 -0.00000 0.00000  0.00000  421 PHE   D CG  
11907 C CD1 . PHE   H  18  ? 0.40487 0.40487 0.40487 0.00000  0.00000  0.00000  421 PHE   D CD1 
11908 C CD2 . PHE   H  18  ? 0.62507 0.62507 0.62507 -0.00000 0.00000  0.00000  421 PHE   D CD2 
11909 C CE1 . PHE   H  18  ? 0.30753 0.30753 0.30753 0.00000  0.00000  0.00000  421 PHE   D CE1 
11910 C CE2 . PHE   H  18  ? 0.50330 0.50330 0.50330 -0.00000 0.00000  0.00000  421 PHE   D CE2 
11911 C CZ  . PHE   H  18  ? 0.57514 0.57514 0.57514 0.00000  0.00000  0.00000  421 PHE   D CZ  
11912 N N   . THR   H  19  ? 0.47486 0.47486 0.47486 0.00000  -0.00000 0.00000  422 THR   D N   
11913 C CA  . THR   H  19  ? 0.35102 0.35102 0.35102 0.00000  0.00000  0.00000  422 THR   D CA  
11914 C C   . THR   H  19  ? 0.45295 0.45295 0.45295 0.00000  0.00000  0.00000  422 THR   D C   
11915 O O   . THR   H  19  ? 0.42933 0.42933 0.42933 -0.00000 0.00000  0.00000  422 THR   D O   
11916 C CB  . THR   H  19  ? 0.49825 0.49825 0.49825 0.00000  -0.00000 0.00000  422 THR   D CB  
11917 O OG1 . THR   H  19  ? 0.45017 0.45017 0.45017 -0.00000 0.00000  0.00000  422 THR   D OG1 
11918 C CG2 . THR   H  19  ? 0.52258 0.52258 0.52258 0.00000  0.00000  0.00000  422 THR   D CG2 
11919 N N   . GLU   H  20  ? 0.49164 0.49164 0.49164 0.00000  0.00000  0.00000  423 GLU   D N   
11920 C CA  . GLU   H  20  ? 0.46998 0.46998 0.46998 0.00000  0.00000  0.00000  423 GLU   D CA  
11921 C C   . GLU   H  20  ? 0.34903 0.34903 0.34903 0.00000  0.00000  0.00000  423 GLU   D C   
11922 O O   . GLU   H  20  ? 0.54879 0.54879 0.54879 -0.00000 -0.00000 0.00000  423 GLU   D O   
11923 C CB  . GLU   H  20  ? 0.29614 0.29614 0.29614 0.00000  0.00000  0.00000  423 GLU   D CB  
11924 N N   . PRO   H  21  ? 0.45835 0.45835 0.45835 0.00000  0.00000  0.00000  424 PRO   D N   
11925 C CA  . PRO   H  21  ? 0.62857 0.62857 0.62857 -0.00000 0.00000  0.00000  424 PRO   D CA  
11926 C C   . PRO   H  21  ? 0.44637 0.44637 0.44637 0.00000  0.00000  0.00000  424 PRO   D C   
11927 O O   . PRO   H  21  ? 0.55653 0.55653 0.55653 0.00000  0.00000  -0.00000 424 PRO   D O   
11928 C CB  . PRO   H  21  ? 0.22969 0.22969 0.22969 0.00000  0.00000  0.00000  424 PRO   D CB  
11929 C CG  . PRO   H  21  ? 0.42117 0.42117 0.42117 -0.00000 0.00000  0.00000  424 PRO   D CG  
11930 C CD  . PRO   H  21  ? 0.40459 0.40459 0.40459 0.00000  0.00000  0.00000  424 PRO   D CD  
11931 N N   . GLY   H  22  ? 0.47433 0.47433 0.47433 -0.00000 0.00000  0.00000  425 GLY   D N   
11932 C CA  . GLY   H  22  ? 0.25494 0.25494 0.25494 -0.00000 0.00000  0.00000  425 GLY   D CA  
11933 C C   . GLY   H  22  ? 0.36436 0.36436 0.36436 0.00000  0.00000  0.00000  425 GLY   D C   
11934 O O   . GLY   H  22  ? 0.43881 0.43881 0.43881 0.00000  0.00000  0.00000  425 GLY   D O   
11935 N N   . THR   H  23  ? 0.40587 0.40587 0.40587 0.00000  0.00000  0.00000  426 THR   D N   
11936 C CA  . THR   H  23  ? 0.37635 0.37635 0.37635 -0.00000 0.00000  0.00000  426 THR   D CA  
11937 C C   . THR   H  23  ? 0.37601 0.37601 0.37601 -0.00000 0.00000  0.00000  426 THR   D C   
11938 O O   . THR   H  23  ? 0.74673 0.74673 0.74673 -0.00000 -0.00000 0.00000  426 THR   D O   
11939 C CB  . THR   H  23  ? 0.48618 0.48618 0.48618 -0.00000 0.00000  0.00000  426 THR   D CB  
11940 O OG1 . THR   H  23  ? 0.59129 0.59129 0.59129 -0.00000 0.00000  0.00000  426 THR   D OG1 
11941 C CG2 . THR   H  23  ? 0.36510 0.36510 0.36510 0.00000  0.00000  0.00000  426 THR   D CG2 
11942 N N   . VAL   H  24  ? 0.63872 0.63872 0.63872 0.00000  0.00000  0.00000  427 VAL   D N   
11943 C CA  . VAL   H  24  ? 0.40017 0.40017 0.40017 0.00000  0.00000  0.00000  427 VAL   D CA  
11944 C C   . VAL   H  24  ? 0.32994 0.32994 0.32994 -0.00000 0.00000  0.00000  427 VAL   D C   
11945 O O   . VAL   H  24  ? 0.64473 0.64473 0.64473 0.00000  0.00000  0.00000  427 VAL   D O   
11946 C CB  . VAL   H  24  ? 0.30984 0.30984 0.30984 0.00000  0.00000  0.00000  427 VAL   D CB  
11947 C CG1 . VAL   H  24  ? 0.21789 0.21789 0.21789 0.00000  0.00000  0.00000  427 VAL   D CG1 
11948 C CG2 . VAL   H  24  ? 0.30916 0.30916 0.30916 0.00000  0.00000  0.00000  427 VAL   D CG2 
11949 N N   . ILE   H  25  ? 0.69609 0.69609 0.69609 0.00000  0.00000  0.00000  428 ILE   D N   
11950 C CA  . ILE   H  25  ? 0.30217 0.30217 0.30217 0.00000  -0.00000 0.00000  428 ILE   D CA  
11951 C C   . ILE   H  25  ? 0.57335 0.57335 0.57335 -0.00000 0.00000  0.00000  428 ILE   D C   
11952 O O   . ILE   H  25  ? 0.46317 0.46317 0.46317 -0.00000 0.00000  0.00000  428 ILE   D O   
11953 C CB  . ILE   H  25  ? 0.53529 0.53529 0.53529 -0.00000 0.00000  0.00000  428 ILE   D CB  
11954 C CG1 . ILE   H  25  ? 0.41964 0.41964 0.41964 0.00000  0.00000  0.00000  428 ILE   D CG1 
11955 C CG2 . ILE   H  25  ? 0.26720 0.26720 0.26720 0.00000  0.00000  0.00000  428 ILE   D CG2 
11956 C CD1 . ILE   H  25  ? 0.35161 0.35161 0.35161 0.00000  0.00000  0.00000  428 ILE   D CD1 
11957 N N   . ARG   H  26  ? 0.49204 0.49204 0.49204 -0.00000 0.00000  0.00000  429 ARG   D N   
11958 C CA  . ARG   H  26  ? 0.47699 0.47699 0.47699 0.00000  0.00000  0.00000  429 ARG   D CA  
11959 C C   . ARG   H  26  ? 0.48371 0.48371 0.48371 0.00000  0.00000  0.00000  429 ARG   D C   
11960 O O   . ARG   H  26  ? 0.47155 0.47155 0.47155 -0.00000 0.00000  0.00000  429 ARG   D O   
11961 C CB  . ARG   H  26  ? 0.57850 0.57850 0.57850 -0.00000 0.00000  0.00000  429 ARG   D CB  
11962 C CG  . ARG   H  26  ? 0.49970 0.49970 0.49970 -0.00000 0.00000  0.00000  429 ARG   D CG  
11963 C CD  . ARG   H  26  ? 0.67223 0.67223 0.67223 -0.00000 0.00000  0.00000  429 ARG   D CD  
11964 N NE  . ARG   H  26  ? 0.49217 0.49217 0.49217 -0.00000 0.00000  0.00000  429 ARG   D NE  
11965 C CZ  . ARG   H  26  ? 2.17035 2.17035 2.17035 0.00000  0.00000  0.00000  429 ARG   D CZ  
11966 N NH1 . ARG   H  26  ? 0.43692 0.43692 0.43692 0.00000  0.00000  0.00000  429 ARG   D NH1 
11967 N NH2 . ARG   H  26  ? 0.52338 0.52338 0.52338 0.00000  -0.00000 0.00000  429 ARG   D NH2 
11968 N N   . ILE   H  27  ? 0.27311 0.27311 0.27311 -0.00000 -0.00000 0.00000  430 ILE   D N   
11969 C CA  . ILE   H  27  ? 0.49340 0.49340 0.49340 -0.00000 0.00000  0.00000  430 ILE   D CA  
11970 C C   . ILE   H  27  ? 0.33675 0.33675 0.33675 0.00000  0.00000  0.00000  430 ILE   D C   
11971 O O   . ILE   H  27  ? 0.67620 0.67620 0.67620 0.00000  -0.00000 0.00000  430 ILE   D O   
11972 C CB  . ILE   H  27  ? 0.41113 0.41113 0.41113 0.00000  0.00000  0.00000  430 ILE   D CB  
11973 C CG1 . ILE   H  27  ? 0.34127 0.34127 0.34127 0.00000  0.00000  0.00000  430 ILE   D CG1 
11974 C CG2 . ILE   H  27  ? 0.38725 0.38725 0.38725 -0.00000 0.00000  0.00000  430 ILE   D CG2 
11975 C CD1 . ILE   H  27  ? 0.30560 0.30560 0.30560 -0.00000 0.00000  0.00000  430 ILE   D CD1 
11976 N N   . ASN   H  28  ? 0.67796 0.67796 0.67796 -0.00000 0.00000  0.00000  431 ASN   D N   
11977 C CA  . ASN   H  28  ? 0.41772 0.41772 0.41772 0.00000  0.00000  0.00000  431 ASN   D CA  
11978 C C   . ASN   H  28  ? 0.56423 0.56423 0.56423 0.00000  0.00000  0.00000  431 ASN   D C   
11979 O O   . ASN   H  28  ? 0.44448 0.44448 0.44448 -0.00000 0.00000  0.00000  431 ASN   D O   
11980 C CB  . ASN   H  28  ? 0.36288 0.36288 0.36288 0.00000  0.00000  0.00000  431 ASN   D CB  
11981 C CG  . ASN   H  28  ? 0.51371 0.51371 0.51371 0.00000  0.00000  0.00000  431 ASN   D CG  
11982 O OD1 . ASN   H  28  ? 0.57641 0.57641 0.57641 0.00000  0.00000  0.00000  431 ASN   D OD1 
11983 N ND2 . ASN   H  28  ? 0.41426 0.41426 0.41426 -0.00000 0.00000  0.00000  431 ASN   D ND2 
11984 N N   . GLU   H  29  ? 0.41821 0.41821 0.41821 0.00000  0.00000  0.00000  432 GLU   D N   
11985 C CA  . GLU   H  29  ? 0.52771 0.52771 0.52771 0.00000  0.00000  0.00000  432 GLU   D CA  
11986 C C   . GLU   H  29  ? 0.47423 0.47423 0.47423 -0.00000 0.00000  0.00000  432 GLU   D C   
11987 O O   . GLU   H  29  ? 0.67007 0.67007 0.67007 -0.00000 0.00000  0.00000  432 GLU   D O   
11988 C CB  . GLU   H  29  ? 0.32730 0.32730 0.32730 0.00000  0.00000  0.00000  432 GLU   D CB  
11989 C CG  . GLU   H  29  ? 0.49551 0.49551 0.49551 -0.00000 0.00000  0.00000  432 GLU   D CG  
11990 C CD  . GLU   H  29  ? 0.80427 0.80427 0.80427 0.00000  0.00000  0.00000  432 GLU   D CD  
11991 O OE1 . GLU   H  29  ? 0.61447 0.61447 0.61447 0.00000  0.00000  0.00000  432 GLU   D OE1 
11992 O OE2 . GLU   H  29  ? 0.69367 0.69367 0.69367 -0.00000 0.00000  0.00000  432 GLU   D OE2 
11993 N N   . VAL   H  30  ? 0.52654 0.52654 0.52654 -0.00000 0.00000  0.00000  433 VAL   D N   
11994 C CA  . VAL   H  30  ? 0.21393 0.21393 0.21393 0.00000  0.00000  0.00000  433 VAL   D CA  
11995 C C   . VAL   H  30  ? 0.46853 0.46853 0.46853 0.00000  0.00000  0.00000  433 VAL   D C   
11996 O O   . VAL   H  30  ? 0.35247 0.35247 0.35247 0.00000  0.00000  0.00000  433 VAL   D O   
11997 C CB  . VAL   H  30  ? 0.47929 0.47929 0.47929 -0.00000 0.00000  0.00000  433 VAL   D CB  
11998 C CG1 . VAL   H  30  ? 0.35045 0.35045 0.35045 -0.00000 0.00000  0.00000  433 VAL   D CG1 
11999 C CG2 . VAL   H  30  ? 0.28429 0.28429 0.28429 -0.00000 0.00000  0.00000  433 VAL   D CG2 
12000 N N   . VAL   H  31  ? 0.39920 0.39920 0.39920 0.00000  0.00000  0.00000  434 VAL   D N   
12001 C CA  . VAL   H  31  ? 0.53955 0.53955 0.53955 0.00000  0.00000  0.00000  434 VAL   D CA  
12002 C C   . VAL   H  31  ? 0.38246 0.38246 0.38246 0.00000  0.00000  0.00000  434 VAL   D C   
12003 O O   . VAL   H  31  ? 0.37209 0.37209 0.37209 0.00000  0.00000  0.00000  434 VAL   D O   
12004 C CB  . VAL   H  31  ? 0.41695 0.41695 0.41695 0.00000  0.00000  -0.00000 434 VAL   D CB  
12005 C CG1 . VAL   H  31  ? 0.21132 0.21132 0.21132 0.00000  0.00000  -0.00000 434 VAL   D CG1 
12006 C CG2 . VAL   H  31  ? 0.24398 0.24398 0.24398 -0.00000 0.00000  0.00000  434 VAL   D CG2 
12007 N N   . ALA   H  32  ? 0.43307 0.43307 0.43307 0.00000  0.00000  0.00000  435 ALA   D N   
12008 C CA  . ALA   H  32  ? 0.47458 0.47458 0.47458 0.00000  0.00000  0.00000  435 ALA   D CA  
12009 C C   . ALA   H  32  ? 0.60050 0.60050 0.60050 0.00000  0.00000  0.00000  435 ALA   D C   
12010 O O   . ALA   H  32  ? 0.50007 0.50007 0.50007 0.00000  0.00000  0.00000  435 ALA   D O   
12011 C CB  . ALA   H  32  ? 0.39476 0.39476 0.39476 0.00000  0.00000  0.00000  435 ALA   D CB  
12012 N N   . ALA   H  33  ? 0.38315 0.38315 0.38315 0.00000  0.00000  0.00000  436 ALA   D N   
12013 C CA  . ALA   H  33  ? 0.49712 0.49712 0.49712 0.00000  0.00000  0.00000  436 ALA   D CA  
12014 C C   . ALA   H  33  ? 0.74564 0.74564 0.74564 0.00000  0.00000  0.00000  436 ALA   D C   
12015 O O   . ALA   H  33  ? 0.45936 0.45936 0.45936 -0.00000 0.00000  0.00000  436 ALA   D O   
12016 C CB  . ALA   H  33  ? 0.29578 0.29578 0.29578 0.00000  0.00000  0.00000  436 ALA   D CB  
12017 N N   . LEU   H  34  ? 0.44065 0.44065 0.44065 0.00000  0.00000  0.00000  437 LEU   D N   
12018 C CA  . LEU   H  34  ? 0.81711 0.81711 0.81711 -0.00000 0.00000  0.00000  437 LEU   D CA  
12019 C C   . LEU   H  34  ? 0.41018 0.41018 0.41018 0.00000  0.00000  0.00000  437 LEU   D C   
12020 O O   . LEU   H  34  ? 0.49552 0.49552 0.49552 0.00000  0.00000  0.00000  437 LEU   D O   
12021 C CB  . LEU   H  34  ? 0.39526 0.39526 0.39526 -0.00000 0.00000  0.00000  437 LEU   D CB  
12022 C CG  . LEU   H  34  ? 0.71345 0.71345 0.71345 -0.00000 0.00000  0.00000  437 LEU   D CG  
12023 C CD1 . LEU   H  34  ? 0.47477 0.47477 0.47477 0.00000  0.00000  0.00000  437 LEU   D CD1 
12024 C CD2 . LEU   H  34  ? 0.74833 0.74833 0.74833 -0.00000 0.00000  0.00000  437 LEU   D CD2 
12025 N N   . LEU   I  57  ? 0.74203 0.74203 0.74203 0.00000  0.00000  0.00000  57  LEU   E N   
12026 C CA  . LEU   I  57  ? 0.70273 0.70273 0.70273 -0.00000 0.00000  0.00000  57  LEU   E CA  
12027 C C   . LEU   I  57  ? 0.90717 0.90717 0.90717 -0.00000 0.00000  0.00000  57  LEU   E C   
12028 O O   . LEU   I  57  ? 0.93243 0.93243 0.93243 0.00000  0.00000  0.00000  57  LEU   E O   
12029 C CB  . LEU   I  57  ? 0.66024 0.66024 0.66024 -0.00000 0.00000  0.00000  57  LEU   E CB  
12030 C CG  . LEU   I  57  ? 0.86622 0.86622 0.86622 0.00000  0.00000  0.00000  57  LEU   E CG  
12031 C CD1 . LEU   I  57  ? 0.76979 0.76979 0.76979 0.00000  0.00000  0.00000  57  LEU   E CD1 
12032 C CD2 . LEU   I  57  ? 0.84678 0.84678 0.84678 0.00000  0.00000  0.00000  57  LEU   E CD2 
12033 N N   . MET   I  58  ? 0.82118 0.82118 0.82118 -0.00000 0.00000  0.00000  58  MET   E N   
12034 C CA  . MET   I  58  ? 0.80723 0.80723 0.80723 -0.00000 0.00000  0.00000  58  MET   E CA  
12035 C C   . MET   I  58  ? 0.68955 0.68955 0.68955 -0.00000 0.00000  0.00000  58  MET   E C   
12036 O O   . MET   I  58  ? 0.95128 0.95128 0.95128 0.00000  0.00000  0.00000  58  MET   E O   
12037 C CB  . MET   I  58  ? 0.71784 0.71784 0.71784 -0.00000 -0.00000 0.00000  58  MET   E CB  
12038 C CG  . MET   I  58  ? 0.91164 0.91164 0.91164 0.00000  -0.00000 0.00000  58  MET   E CG  
12039 S SD  . MET   I  58  ? 0.98592 0.98592 0.98592 0.00000  0.00000  0.00000  58  MET   E SD  
12040 C CE  . MET   I  58  ? 0.68990 0.68990 0.68990 -0.00000 0.00000  0.00000  58  MET   E CE  
12041 N N   . GLN   I  59  ? 0.85982 0.85982 0.85982 0.00000  0.00000  0.00000  59  GLN   E N   
12042 C CA  . GLN   I  59  ? 0.71845 0.71845 0.71845 -0.00000 0.00000  0.00000  59  GLN   E CA  
12043 C C   . GLN   I  59  ? 0.84168 0.84168 0.84168 0.00000  0.00000  0.00000  59  GLN   E C   
12044 O O   . GLN   I  59  ? 0.76633 0.76633 0.76633 0.00000  0.00000  0.00000  59  GLN   E O   
12045 C CB  . GLN   I  59  ? 0.63930 0.63930 0.63930 0.00000  0.00000  0.00000  59  GLN   E CB  
12046 C CG  . GLN   I  59  ? 1.01358 1.01358 1.01358 -0.00000 0.00000  0.00000  59  GLN   E CG  
12047 C CD  . GLN   I  59  ? 1.29971 1.29971 1.29971 -0.00000 0.00000  0.00000  59  GLN   E CD  
12048 O OE1 . GLN   I  59  ? 1.44641 1.44641 1.44641 -0.00000 -0.00000 0.00000  59  GLN   E OE1 
12049 N NE2 . GLN   I  59  ? 1.10500 1.10500 1.10500 -0.00000 0.00000  0.00000  59  GLN   E NE2 
12050 N N   . PRO   I  60  ? 0.70601 0.70601 0.70601 0.00000  0.00000  0.00000  60  PRO   E N   
12051 C CA  . PRO   I  60  ? 0.47449 0.47449 0.47449 0.00000  0.00000  0.00000  60  PRO   E CA  
12052 C C   . PRO   I  60  ? 0.77957 0.77957 0.77957 0.00000  0.00000  0.00000  60  PRO   E C   
12053 O O   . PRO   I  60  ? 0.51491 0.51491 0.51491 0.00000  0.00000  0.00000  60  PRO   E O   
12054 C CB  . PRO   I  60  ? 0.48416 0.48416 0.48416 0.00000  0.00000  0.00000  60  PRO   E CB  
12055 C CG  . PRO   I  60  ? 0.57267 0.57267 0.57267 -0.00000 0.00000  0.00000  60  PRO   E CG  
12056 C CD  . PRO   I  60  ? 0.42422 0.42422 0.42422 0.00000  0.00000  0.00000  60  PRO   E CD  
12057 N N   . ILE   I  61  ? 0.49613 0.49613 0.49613 0.00000  0.00000  0.00000  61  ILE   E N   
12058 C CA  . ILE   I  61  ? 0.80432 0.80432 0.80432 -0.00000 0.00000  0.00000  61  ILE   E CA  
12059 C C   . ILE   I  61  ? 0.63105 0.63105 0.63105 -0.00000 0.00000  0.00000  61  ILE   E C   
12060 O O   . ILE   I  61  ? 0.68594 0.68594 0.68594 0.00000  0.00000  0.00000  61  ILE   E O   
12061 C CB  . ILE   I  61  ? 0.62563 0.62563 0.62563 -0.00000 0.00000  0.00000  61  ILE   E CB  
12062 C CG1 . ILE   I  61  ? 0.50596 0.50596 0.50596 0.00000  0.00000  0.00000  61  ILE   E CG1 
12063 C CG2 . ILE   I  61  ? 0.48237 0.48237 0.48237 0.00000  0.00000  0.00000  61  ILE   E CG2 
12064 C CD1 . ILE   I  61  ? 0.58941 0.58941 0.58941 -0.00000 0.00000  0.00000  61  ILE   E CD1 
12065 N N   . GLN   I  62  ? 0.78791 0.78791 0.78791 0.00000  0.00000  0.00000  62  GLN   E N   
12066 C CA  . GLN   I  62  ? 0.40241 0.40241 0.40241 -0.00000 0.00000  0.00000  62  GLN   E CA  
12067 C C   . GLN   I  62  ? 1.09864 1.09864 1.09864 -0.00000 0.00000  0.00000  62  GLN   E C   
12068 O O   . GLN   I  62  ? 0.37313 0.37313 0.37313 -0.00000 0.00000  0.00000  62  GLN   E O   
12069 C CB  . GLN   I  62  ? 1.03550 1.03550 1.03550 -0.00000 0.00000  0.00000  62  GLN   E CB  
12070 C CG  . GLN   I  62  ? 1.28478 1.28478 1.28478 0.00000  0.00000  0.00000  62  GLN   E CG  
12071 C CD  . GLN   I  62  ? 1.85825 1.85825 1.85825 -0.00000 0.00000  0.00000  62  GLN   E CD  
12072 O OE1 . GLN   I  62  ? 1.88547 1.88547 1.88547 -0.00000 0.00000  0.00000  62  GLN   E OE1 
12073 N NE2 . GLN   I  62  ? 1.88318 1.88318 1.88318 0.00000  0.00000  0.00000  62  GLN   E NE2 
12074 N N   . GLU   I  63  ? 0.56693 0.56693 0.56693 -0.00000 0.00000  0.00000  63  GLU   E N   
12075 C CA  . GLU   I  63  ? 0.76750 0.76750 0.76750 -0.00000 0.00000  0.00000  63  GLU   E CA  
12076 C C   . GLU   I  63  ? 0.79561 0.79561 0.79561 0.00000  0.00000  0.00000  63  GLU   E C   
12077 O O   . GLU   I  63  ? 0.71101 0.71101 0.71101 -0.00000 0.00000  0.00000  63  GLU   E O   
12078 C CB  . GLU   I  63  ? 0.56637 0.56637 0.56637 0.00000  0.00000  0.00000  63  GLU   E CB  
12079 C CG  . GLU   I  63  ? 1.04226 1.04226 1.04226 0.00000  0.00000  0.00000  63  GLU   E CG  
12080 C CD  . GLU   I  63  ? 0.87499 0.87499 0.87499 0.00000  0.00000  0.00000  63  GLU   E CD  
12081 O OE1 . GLU   I  63  ? 1.46340 1.46340 1.46340 0.00000  0.00000  0.00000  63  GLU   E OE1 
12082 O OE2 . GLU   I  63  ? 1.81288 1.81288 1.81288 0.00000  0.00000  0.00000  63  GLU   E OE2 
12083 N N   . PHE   I  64  ? 0.64863 0.64863 0.64863 -0.00000 0.00000  0.00000  64  PHE   E N   
12084 C CA  . PHE   I  64  ? 0.56565 0.56565 0.56565 -0.00000 0.00000  0.00000  64  PHE   E CA  
12085 C C   . PHE   I  64  ? 0.74343 0.74343 0.74343 0.00000  0.00000  0.00000  64  PHE   E C   
12086 O O   . PHE   I  64  ? 0.67452 0.67452 0.67452 0.00000  0.00000  0.00000  64  PHE   E O   
12087 C CB  . PHE   I  64  ? 0.60484 0.60484 0.60484 -0.00000 0.00000  0.00000  64  PHE   E CB  
12088 C CG  . PHE   I  64  ? 0.67035 0.67035 0.67035 0.00000  0.00000  0.00000  64  PHE   E CG  
12089 C CD1 . PHE   I  64  ? 0.77098 0.77098 0.77098 0.00000  0.00000  0.00000  64  PHE   E CD1 
12090 C CD2 . PHE   I  64  ? 0.53148 0.53148 0.53148 -0.00000 0.00000  0.00000  64  PHE   E CD2 
12091 C CE1 . PHE   I  64  ? 0.59357 0.59357 0.59357 0.00000  0.00000  0.00000  64  PHE   E CE1 
12092 C CE2 . PHE   I  64  ? 0.50932 0.50932 0.50932 -0.00000 0.00000  0.00000  64  PHE   E CE2 
12093 C CZ  . PHE   I  64  ? 0.61998 0.61998 0.61998 0.00000  0.00000  0.00000  64  PHE   E CZ  
12094 N N   . LYS   I  65  ? 0.59075 0.59075 0.59075 0.00000  0.00000  0.00000  65  LYS   E N   
12095 C CA  . LYS   I  65  ? 0.52662 0.52662 0.52662 0.00000  0.00000  0.00000  65  LYS   E CA  
12096 C C   . LYS   I  65  ? 0.78228 0.78228 0.78228 0.00000  0.00000  0.00000  65  LYS   E C   
12097 O O   . LYS   I  65  ? 0.67533 0.67533 0.67533 -0.00000 0.00000  0.00000  65  LYS   E O   
12098 C CB  . LYS   I  65  ? 0.61853 0.61853 0.61853 0.00000  0.00000  0.00000  65  LYS   E CB  
12099 C CG  . LYS   I  65  ? 0.63164 0.63164 0.63164 -0.00000 0.00000  0.00000  65  LYS   E CG  
12100 C CD  . LYS   I  65  ? 0.76506 0.76506 0.76506 0.00000  0.00000  0.00000  65  LYS   E CD  
12101 C CE  . LYS   I  65  ? 0.86325 0.86325 0.86325 0.00000  0.00000  0.00000  65  LYS   E CE  
12102 N NZ  . LYS   I  65  ? 1.00339 1.00339 1.00339 -0.00000 0.00000  -0.00000 65  LYS   E NZ  
12103 N N   . ALA   I  66  ? 0.67905 0.67905 0.67905 -0.00000 0.00000  0.00000  66  ALA   E N   
12104 C CA  . ALA   I  66  ? 0.72001 0.72001 0.72001 -0.00000 0.00000  0.00000  66  ALA   E CA  
12105 C C   . ALA   I  66  ? 0.85065 0.85065 0.85065 0.00000  0.00000  0.00000  66  ALA   E C   
12106 O O   . ALA   I  66  ? 0.65337 0.65337 0.65337 0.00000  0.00000  0.00000  66  ALA   E O   
12107 C CB  . ALA   I  66  ? 0.43243 0.43243 0.43243 0.00000  0.00000  0.00000  66  ALA   E CB  
12108 N N   . PHE   I  67  ? 0.88831 0.88831 0.88831 -0.00000 0.00000  0.00000  67  PHE   E N   
12109 C CA  . PHE   I  67  ? 0.61537 0.61537 0.61537 -0.00000 0.00000  0.00000  67  PHE   E CA  
12110 C C   . PHE   I  67  ? 0.81782 0.81782 0.81782 0.00000  0.00000  0.00000  67  PHE   E C   
12111 O O   . PHE   I  67  ? 0.77059 0.77059 0.77059 0.00000  0.00000  0.00000  67  PHE   E O   
12112 C CB  . PHE   I  67  ? 0.63077 0.63077 0.63077 0.00000  0.00000  0.00000  67  PHE   E CB  
12113 C CG  . PHE   I  67  ? 0.64312 0.64312 0.64312 0.00000  0.00000  0.00000  67  PHE   E CG  
12114 C CD1 . PHE   I  67  ? 0.47068 0.47068 0.47068 -0.00000 0.00000  0.00000  67  PHE   E CD1 
12115 C CD2 . PHE   I  67  ? 0.56663 0.56663 0.56663 -0.00000 0.00000  0.00000  67  PHE   E CD2 
12116 C CE1 . PHE   I  67  ? 0.56109 0.56109 0.56109 -0.00000 0.00000  0.00000  67  PHE   E CE1 
12117 C CE2 . PHE   I  67  ? 0.69186 0.69186 0.69186 0.00000  0.00000  0.00000  67  PHE   E CE2 
12118 C CZ  . PHE   I  67  ? 0.52791 0.52791 0.52791 -0.00000 0.00000  0.00000  67  PHE   E CZ  
12119 N N   . ILE   I  68  ? 0.66262 0.66262 0.66262 0.00000  0.00000  0.00000  68  ILE   E N   
12120 C CA  . ILE   I  68  ? 0.69026 0.69026 0.69026 0.00000  0.00000  0.00000  68  ILE   E CA  
12121 C C   . ILE   I  68  ? 0.76736 0.76736 0.76736 -0.00000 -0.00000 0.00000  68  ILE   E C   
12122 O O   . ILE   I  68  ? 0.73737 0.73737 0.73737 -0.00000 0.00000  0.00000  68  ILE   E O   
12123 C CB  . ILE   I  68  ? 0.56256 0.56256 0.56256 0.00000  0.00000  0.00000  68  ILE   E CB  
12124 C CG1 . ILE   I  68  ? 0.65247 0.65247 0.65247 0.00000  0.00000  0.00000  68  ILE   E CG1 
12125 C CG2 . ILE   I  68  ? 0.63084 0.63084 0.63084 0.00000  0.00000  0.00000  68  ILE   E CG2 
12126 C CD1 . ILE   I  68  ? 0.56354 0.56354 0.56354 0.00000  0.00000  0.00000  68  ILE   E CD1 
12127 N N   . GLU   I  69  ? 1.02669 1.02669 1.02669 0.00000  0.00000  0.00000  69  GLU   E N   
12128 C CA  . GLU   I  69  ? 0.70453 0.70453 0.70453 -0.00000 0.00000  0.00000  69  GLU   E CA  
12129 C C   . GLU   I  69  ? 0.82295 0.82295 0.82295 -0.00000 -0.00000 0.00000  69  GLU   E C   
12130 O O   . GLU   I  69  ? 0.82938 0.82938 0.82938 0.00000  0.00000  0.00000  69  GLU   E O   
12131 C CB  . GLU   I  69  ? 0.78482 0.78482 0.78482 0.00000  0.00000  0.00000  69  GLU   E CB  
12132 C CG  . GLU   I  69  ? 0.60761 0.60761 0.60761 -0.00000 0.00000  0.00000  69  GLU   E CG  
12133 C CD  . GLU   I  69  ? 1.12954 1.12954 1.12954 0.00000  0.00000  0.00000  69  GLU   E CD  
12134 O OE1 . GLU   I  69  ? 0.78059 0.78059 0.78059 0.00000  0.00000  0.00000  69  GLU   E OE1 
12135 O OE2 . GLU   I  69  ? 0.86680 0.86680 0.86680 -0.00000 0.00000  0.00000  69  GLU   E OE2 
12136 N N   . SER   I  70  ? 0.83606 0.83606 0.83606 -0.00000 0.00000  0.00000  70  SER   E N   
12137 C CA  . SER   I  70  ? 0.47867 0.47867 0.47867 -0.00000 0.00000  0.00000  70  SER   E CA  
12138 C C   . SER   I  70  ? 0.84295 0.84295 0.84295 0.00000  0.00000  0.00000  70  SER   E C   
12139 O O   . SER   I  70  ? 0.64959 0.64959 0.64959 0.00000  0.00000  0.00000  70  SER   E O   
12140 C CB  . SER   I  70  ? 0.63824 0.63824 0.63824 -0.00000 0.00000  -0.00000 70  SER   E CB  
12141 O OG  . SER   I  70  ? 0.90848 0.90848 0.90848 0.00000  0.00000  0.00000  70  SER   E OG  
12142 N N   . ASP   I  71  ? 0.59131 0.59131 0.59131 0.00000  0.00000  0.00000  71  ASP   E N   
12143 C CA  . ASP   I  71  ? 0.53156 0.53156 0.53156 0.00000  0.00000  0.00000  71  ASP   E CA  
12144 C C   . ASP   I  71  ? 0.61096 0.61096 0.61096 0.00000  0.00000  0.00000  71  ASP   E C   
12145 O O   . ASP   I  71  ? 0.60973 0.60973 0.60973 -0.00000 0.00000  0.00000  71  ASP   E O   
12146 C CB  . ASP   I  71  ? 0.64764 0.64764 0.64764 0.00000  0.00000  0.00000  71  ASP   E CB  
12147 C CG  . ASP   I  71  ? 1.14487 1.14487 1.14487 0.00000  0.00000  0.00000  71  ASP   E CG  
12148 O OD1 . ASP   I  71  ? 0.68797 0.68797 0.68797 -0.00000 0.00000  0.00000  71  ASP   E OD1 
12149 O OD2 . ASP   I  71  ? 0.86408 0.86408 0.86408 0.00000  -0.00000 0.00000  71  ASP   E OD2 
12150 N N   . PRO   I  72  ? 0.74664 0.74664 0.74664 0.00000  0.00000  0.00000  72  PRO   E N   
12151 C CA  . PRO   I  72  ? 0.72446 0.72446 0.72446 0.00000  0.00000  0.00000  72  PRO   E CA  
12152 C C   . PRO   I  72  ? 0.60861 0.60861 0.60861 0.00000  0.00000  0.00000  72  PRO   E C   
12153 O O   . PRO   I  72  ? 0.68130 0.68130 0.68130 -0.00000 0.00000  0.00000  72  PRO   E O   
12154 C CB  . PRO   I  72  ? 0.54991 0.54991 0.54991 -0.00000 0.00000  0.00000  72  PRO   E CB  
12155 C CG  . PRO   I  72  ? 0.62393 0.62393 0.62393 0.00000  0.00000  0.00000  72  PRO   E CG  
12156 C CD  . PRO   I  72  ? 0.44606 0.44606 0.44606 0.00000  0.00000  0.00000  72  PRO   E CD  
12157 N N   . VAL   I  73  ? 0.64640 0.64640 0.64640 -0.00000 0.00000  0.00000  73  VAL   E N   
12158 C CA  . VAL   I  73  ? 0.78553 0.78553 0.78553 0.00000  0.00000  0.00000  73  VAL   E CA  
12159 C C   . VAL   I  73  ? 0.88173 0.88173 0.88173 -0.00000 0.00000  0.00000  73  VAL   E C   
12160 O O   . VAL   I  73  ? 0.51468 0.51468 0.51468 0.00000  0.00000  0.00000  73  VAL   E O   
12161 C CB  . VAL   I  73  ? 0.74429 0.74429 0.74429 0.00000  -0.00000 0.00000  73  VAL   E CB  
12162 C CG1 . VAL   I  73  ? 0.45365 0.45365 0.45365 0.00000  0.00000  0.00000  73  VAL   E CG1 
12163 C CG2 . VAL   I  73  ? 0.42627 0.42627 0.42627 0.00000  0.00000  0.00000  73  VAL   E CG2 
12164 N N   . VAL   I  74  ? 0.69189 0.69189 0.69189 0.00000  0.00000  0.00000  74  VAL   E N   
12165 C CA  . VAL   I  74  ? 0.57280 0.57280 0.57280 0.00000  0.00000  0.00000  74  VAL   E CA  
12166 C C   . VAL   I  74  ? 0.71000 0.71000 0.71000 -0.00000 0.00000  0.00000  74  VAL   E C   
12167 O O   . VAL   I  74  ? 0.76863 0.76863 0.76863 0.00000  0.00000  0.00000  74  VAL   E O   
12168 C CB  . VAL   I  74  ? 0.59974 0.59974 0.59974 -0.00000 0.00000  0.00000  74  VAL   E CB  
12169 C CG1 . VAL   I  74  ? 0.38352 0.38352 0.38352 -0.00000 -0.00000 0.00000  74  VAL   E CG1 
12170 C CG2 . VAL   I  74  ? 0.47010 0.47010 0.47010 -0.00000 0.00000  0.00000  74  VAL   E CG2 
12171 N N   . HIS   I  75  ? 0.79677 0.79677 0.79677 -0.00000 0.00000  0.00000  75  HIS   E N   
12172 C CA  . HIS   I  75  ? 0.70432 0.70432 0.70432 0.00000  0.00000  0.00000  75  HIS   E CA  
12173 C C   . HIS   I  75  ? 0.56299 0.56299 0.56299 0.00000  0.00000  0.00000  75  HIS   E C   
12174 O O   . HIS   I  75  ? 0.65056 0.65056 0.65056 -0.00000 0.00000  0.00000  75  HIS   E O   
12175 C CB  . HIS   I  75  ? 0.59759 0.59759 0.59759 -0.00000 0.00000  0.00000  75  HIS   E CB  
12176 C CG  . HIS   I  75  ? 1.01336 1.01336 1.01336 0.00000  0.00000  0.00000  75  HIS   E CG  
12177 N ND1 . HIS   I  75  ? 1.13302 1.13302 1.13302 -0.00000 0.00000  0.00000  75  HIS   E ND1 
12178 C CD2 . HIS   I  75  ? 1.03169 1.03169 1.03169 -0.00000 0.00000  0.00000  75  HIS   E CD2 
12179 C CE1 . HIS   I  75  ? 0.97461 0.97461 0.97461 0.00000  0.00000  0.00000  75  HIS   E CE1 
12180 N NE2 . HIS   I  75  ? 0.80591 0.80591 0.80591 0.00000  0.00000  0.00000  75  HIS   E NE2 
12181 N N   . GLN   I  76  ? 0.72813 0.72813 0.72813 -0.00000 0.00000  0.00000  76  GLN   E N   
12182 C CA  . GLN   I  76  ? 0.45805 0.45805 0.45805 0.00000  0.00000  0.00000  76  GLN   E CA  
12183 C C   . GLN   I  76  ? 0.75181 0.75181 0.75181 -0.00000 0.00000  0.00000  76  GLN   E C   
12184 O O   . GLN   I  76  ? 0.61587 0.61587 0.61587 0.00000  0.00000  0.00000  76  GLN   E O   
12185 C CB  . GLN   I  76  ? 0.78001 0.78001 0.78001 -0.00000 0.00000  0.00000  76  GLN   E CB  
12186 C CG  . GLN   I  76  ? 0.47577 0.47577 0.47577 0.00000  0.00000  0.00000  76  GLN   E CG  
12187 C CD  . GLN   I  76  ? 1.21375 1.21375 1.21375 0.00000  0.00000  0.00000  76  GLN   E CD  
12188 O OE1 . GLN   I  76  ? 0.70267 0.70267 0.70267 0.00000  0.00000  0.00000  76  GLN   E OE1 
12189 N NE2 . GLN   I  76  ? 0.60230 0.60230 0.60230 0.00000  0.00000  0.00000  76  GLN   E NE2 
12190 N N   . GLU   I  77  ? 0.65112 0.65112 0.65112 0.00000  0.00000  0.00000  77  GLU   E N   
12191 C CA  . GLU   I  77  ? 0.53705 0.53705 0.53705 -0.00000 0.00000  0.00000  77  GLU   E CA  
12192 C C   . GLU   I  77  ? 0.88358 0.88358 0.88358 0.00000  0.00000  0.00000  77  GLU   E C   
12193 O O   . GLU   I  77  ? 0.46064 0.46064 0.46064 0.00000  0.00000  0.00000  77  GLU   E O   
12194 C CB  . GLU   I  77  ? 0.53124 0.53124 0.53124 0.00000  0.00000  0.00000  77  GLU   E CB  
12195 C CG  . GLU   I  77  ? 0.46912 0.46912 0.46912 0.00000  0.00000  0.00000  77  GLU   E CG  
12196 C CD  . GLU   I  77  ? 0.87934 0.87934 0.87934 0.00000  0.00000  0.00000  77  GLU   E CD  
12197 O OE1 . GLU   I  77  ? 0.64704 0.64704 0.64704 0.00000  0.00000  0.00000  77  GLU   E OE1 
12198 O OE2 . GLU   I  77  ? 0.56799 0.56799 0.56799 0.00000  0.00000  0.00000  77  GLU   E OE2 
12199 N N   . PHE   I  78  ? 0.48700 0.48700 0.48700 0.00000  0.00000  0.00000  78  PHE   E N   
12200 C CA  . PHE   I  78  ? 0.75382 0.75382 0.75382 0.00000  0.00000  0.00000  78  PHE   E CA  
12201 C C   . PHE   I  78  ? 0.74454 0.74454 0.74454 0.00000  0.00000  0.00000  78  PHE   E C   
12202 O O   . PHE   I  78  ? 0.84157 0.84157 0.84157 0.00000  0.00000  0.00000  78  PHE   E O   
12203 C CB  . PHE   I  78  ? 0.50783 0.50783 0.50783 0.00000  0.00000  0.00000  78  PHE   E CB  
12204 C CG  . PHE   I  78  ? 0.74162 0.74162 0.74162 -0.00000 0.00000  0.00000  78  PHE   E CG  
12205 C CD1 . PHE   I  78  ? 0.56859 0.56859 0.56859 -0.00000 0.00000  0.00000  78  PHE   E CD1 
12206 C CD2 . PHE   I  78  ? 0.42232 0.42232 0.42232 -0.00000 0.00000  0.00000  78  PHE   E CD2 
12207 C CE1 . PHE   I  78  ? 0.54200 0.54200 0.54200 0.00000  0.00000  0.00000  78  PHE   E CE1 
12208 C CE2 . PHE   I  78  ? 0.67288 0.67288 0.67288 0.00000  0.00000  0.00000  78  PHE   E CE2 
12209 C CZ  . PHE   I  78  ? 0.51339 0.51339 0.51339 0.00000  0.00000  0.00000  78  PHE   E CZ  
12210 N N   . ILE   I  79  ? 0.63107 0.63107 0.63107 0.00000  0.00000  0.00000  79  ILE   E N   
12211 C CA  . ILE   I  79  ? 0.55064 0.55064 0.55064 0.00000  0.00000  0.00000  79  ILE   E CA  
12212 C C   . ILE   I  79  ? 0.76260 0.76260 0.76260 0.00000  0.00000  0.00000  79  ILE   E C   
12213 O O   . ILE   I  79  ? 0.46287 0.46287 0.46287 -0.00000 0.00000  0.00000  79  ILE   E O   
12214 C CB  . ILE   I  79  ? 0.66165 0.66165 0.66165 0.00000  0.00000  0.00000  79  ILE   E CB  
12215 C CG1 . ILE   I  79  ? 0.49000 0.49000 0.49000 0.00000  0.00000  0.00000  79  ILE   E CG1 
12216 C CG2 . ILE   I  79  ? 0.50017 0.50017 0.50017 0.00000  0.00000  0.00000  79  ILE   E CG2 
12217 C CD1 . ILE   I  79  ? 0.45515 0.45515 0.45515 0.00000  0.00000  0.00000  79  ILE   E CD1 
12218 N N   . ASP   I  80  ? 0.43098 0.43098 0.43098 -0.00000 -0.00000 0.00000  80  ASP   E N   
12219 C CA  . ASP   I  80  ? 0.63489 0.63489 0.63489 0.00000  0.00000  0.00000  80  ASP   E CA  
12220 C C   . ASP   I  80  ? 0.52314 0.52314 0.52314 0.00000  0.00000  0.00000  80  ASP   E C   
12221 O O   . ASP   I  80  ? 0.63907 0.63907 0.63907 0.00000  0.00000  0.00000  80  ASP   E O   
12222 C CB  . ASP   I  80  ? 0.55637 0.55637 0.55637 0.00000  0.00000  0.00000  80  ASP   E CB  
12223 C CG  . ASP   I  80  ? 0.78803 0.78803 0.78803 0.00000  0.00000  0.00000  80  ASP   E CG  
12224 O OD1 . ASP   I  80  ? 0.76505 0.76505 0.76505 0.00000  -0.00000 0.00000  80  ASP   E OD1 
12225 O OD2 . ASP   I  80  ? 0.86247 0.86247 0.86247 -0.00000 0.00000  0.00000  80  ASP   E OD2 
12226 N N   . MET   I  81  ? 0.54527 0.54527 0.54527 -0.00000 0.00000  0.00000  81  MET   E N   
12227 C CA  . MET   I  81  ? 0.46554 0.46554 0.46554 -0.00000 0.00000  0.00000  81  MET   E CA  
12228 C C   . MET   I  81  ? 0.75398 0.75398 0.75398 0.00000  0.00000  0.00000  81  MET   E C   
12229 O O   . MET   I  81  ? 0.59392 0.59392 0.59392 -0.00000 0.00000  0.00000  81  MET   E O   
12230 C CB  . MET   I  81  ? 0.46561 0.46561 0.46561 0.00000  0.00000  0.00000  81  MET   E CB  
12231 C CG  . MET   I  81  ? 0.54745 0.54745 0.54745 0.00000  -0.00000 -0.00000 81  MET   E CG  
12232 S SD  . MET   I  81  ? 0.54599 0.54599 0.54599 0.00000  0.00000  0.00000  81  MET   E SD  
12233 C CE  . MET   I  81  ? 0.50316 0.50316 0.50316 0.00000  0.00000  0.00000  81  MET   E CE  
12234 N N   . PHE   I  82  ? 0.46871 0.46871 0.46871 0.00000  0.00000  0.00000  82  PHE   E N   
12235 C CA  . PHE   I  82  ? 0.79041 0.79041 0.79041 -0.00000 0.00000  0.00000  82  PHE   E CA  
12236 C C   . PHE   I  82  ? 0.44669 0.44669 0.44669 -0.00000 0.00000  0.00000  82  PHE   E C   
12237 O O   . PHE   I  82  ? 1.24943 1.24943 1.24943 -0.00000 0.00000  0.00000  82  PHE   E O   
12238 C CB  . PHE   I  82  ? 0.48002 0.48002 0.48002 0.00000  0.00000  0.00000  82  PHE   E CB  
12239 C CG  . PHE   I  82  ? 1.02658 1.02658 1.02658 0.00000  0.00000  0.00000  82  PHE   E CG  
12240 C CD1 . PHE   I  82  ? 0.44304 0.44304 0.44304 -0.00000 -0.00000 0.00000  82  PHE   E CD1 
12241 C CD2 . PHE   I  82  ? 0.47612 0.47612 0.47612 -0.00000 0.00000  0.00000  82  PHE   E CD2 
12242 C CE1 . PHE   I  82  ? 0.68068 0.68068 0.68068 -0.00000 -0.00000 0.00000  82  PHE   E CE1 
12243 C CE2 . PHE   I  82  ? 0.69672 0.69672 0.69672 -0.00000 0.00000  0.00000  82  PHE   E CE2 
12244 C CZ  . PHE   I  82  ? 0.38901 0.38901 0.38901 -0.00000 0.00000  0.00000  82  PHE   E CZ  
12245 N N   . GLU   I  83  ? 0.85916 0.85916 0.85916 0.00000  0.00000  0.00000  83  GLU   E N   
12246 C CA  . GLU   I  83  ? 0.91950 0.91950 0.91950 -0.00000 0.00000  0.00000  83  GLU   E CA  
12247 C C   . GLU   I  83  ? 1.02499 1.02499 1.02499 0.00000  0.00000  0.00000  83  GLU   E C   
12248 O O   . GLU   I  83  ? 0.72437 0.72437 0.72437 -0.00000 0.00000  0.00000  83  GLU   E O   
12249 C CB  . GLU   I  83  ? 0.60710 0.60710 0.60710 0.00000  0.00000  0.00000  83  GLU   E CB  
12250 C CG  . GLU   I  83  ? 1.28168 1.28168 1.28168 0.00000  0.00000  0.00000  83  GLU   E CG  
12251 C CD  . GLU   I  83  ? 1.84478 1.84478 1.84478 0.00000  0.00000  0.00000  83  GLU   E CD  
12252 O OE1 . GLU   I  83  ? 2.01143 2.01143 2.01143 -0.00000 0.00000  0.00000  83  GLU   E OE1 
12253 O OE2 . GLU   I  83  ? 1.90263 1.90263 1.90263 -0.00000 0.00000  0.00000  83  GLU   E OE2 
12254 N N   . GLY   I  84  ? 0.99533 0.99533 0.99533 0.00000  0.00000  0.00000  84  GLY   E N   
12255 C CA  . GLY   I  84  ? 0.54391 0.54391 0.54391 0.00000  0.00000  0.00000  84  GLY   E CA  
12256 C C   . GLY   I  84  ? 0.96295 0.96295 0.96295 0.00000  0.00000  0.00000  84  GLY   E C   
12257 O O   . GLY   I  84  ? 0.77445 0.77445 0.77445 0.00000  0.00000  0.00000  84  GLY   E O   
12258 N N   . ILE   I  85  ? 0.93528 0.93528 0.93528 0.00000  0.00000  0.00000  85  ILE   E N   
12259 C CA  . ILE   I  85  ? 0.67703 0.67703 0.67703 0.00000  0.00000  0.00000  85  ILE   E CA  
12260 C C   . ILE   I  85  ? 0.80634 0.80634 0.80634 0.00000  0.00000  0.00000  85  ILE   E C   
12261 O O   . ILE   I  85  ? 0.73220 0.73220 0.73220 0.00000  0.00000  0.00000  85  ILE   E O   
12262 C CB  . ILE   I  85  ? 0.59365 0.59365 0.59365 0.00000  -0.00000 -0.00000 85  ILE   E CB  
12263 C CG1 . ILE   I  85  ? 0.78710 0.78710 0.78710 0.00000  0.00000  0.00000  85  ILE   E CG1 
12264 C CG2 . ILE   I  85  ? 0.62045 0.62045 0.62045 0.00000  0.00000  0.00000  85  ILE   E CG2 
12265 C CD1 . ILE   I  85  ? 0.68458 0.68458 0.68458 0.00000  0.00000  0.00000  85  ILE   E CD1 
12266 N N   . GLN   I  86  ? 0.75637 0.75637 0.75637 0.00000  0.00000  0.00000  86  GLN   E N   
12267 C CA  . GLN   I  86  ? 1.15678 1.15678 1.15678 0.00000  0.00000  0.00000  86  GLN   E CA  
12268 C C   . GLN   I  86  ? 0.53415 0.53415 0.53415 0.00000  0.00000  0.00000  86  GLN   E C   
12269 O O   . GLN   I  86  ? 1.12557 1.12557 1.12557 0.00000  0.00000  0.00000  86  GLN   E O   
12270 C CB  . GLN   I  86  ? 0.70255 0.70255 0.70255 -0.00000 0.00000  0.00000  86  GLN   E CB  
12271 C CG  . GLN   I  86  ? 1.58481 1.58481 1.58481 -0.00000 0.00000  0.00000  86  GLN   E CG  
12272 C CD  . GLN   I  86  ? 0.84999 0.84999 0.84999 -0.00000 0.00000  0.00000  86  GLN   E CD  
12273 O OE1 . GLN   I  86  ? 1.22230 1.22230 1.22230 0.00000  0.00000  0.00000  86  GLN   E OE1 
12274 N NE2 . GLN   I  86  ? 1.24041 1.24041 1.24041 -0.00000 0.00000  0.00000  86  GLN   E NE2 
12275 N N   . ASP   I  87  ? 1.31530 1.31530 1.31530 -0.00000 0.00000  0.00000  87  ASP   E N   
12276 C CA  . ASP   I  87  ? 0.88814 0.88814 0.88814 0.00000  0.00000  0.00000  87  ASP   E CA  
12277 C C   . ASP   I  87  ? 0.75075 0.75075 0.75075 0.00000  0.00000  0.00000  87  ASP   E C   
12278 O O   . ASP   I  87  ? 1.00896 1.00896 1.00896 0.00000  0.00000  0.00000  87  ASP   E O   
12279 C CB  . ASP   I  87  ? 0.79004 0.79004 0.79004 -0.00000 0.00000  0.00000  87  ASP   E CB  
12280 C CG  . ASP   I  87  ? 1.71163 1.71163 1.71163 0.00000  0.00000  0.00000  87  ASP   E CG  
12281 O OD1 . ASP   I  87  ? 1.46156 1.46156 1.46156 0.00000  0.00000  0.00000  87  ASP   E OD1 
12282 O OD2 . ASP   I  87  ? 1.43673 1.43673 1.43673 -0.00000 0.00000  0.00000  87  ASP   E OD2 
12283 N N   . SER   I  88  ? 0.65399 0.65399 0.65399 -0.00000 0.00000  0.00000  88  SER   E N   
12284 C CA  . SER   I  88  ? 0.51566 0.51566 0.51566 -0.00000 0.00000  0.00000  88  SER   E CA  
12285 C C   . SER   I  88  ? 1.05252 1.05252 1.05252 -0.00000 0.00000  0.00000  88  SER   E C   
12286 O O   . SER   I  88  ? 0.64090 0.64090 0.64090 0.00000  0.00000  0.00000  88  SER   E O   
12287 C CB  . SER   I  88  ? 0.52895 0.52895 0.52895 -0.00000 0.00000  0.00000  88  SER   E CB  
12288 O OG  . SER   I  88  ? 0.73324 0.73324 0.73324 0.00000  0.00000  0.00000  88  SER   E OG  
12289 N N   . PRO   I  89  ? 0.75271 0.75271 0.75271 0.00000  -0.00000 0.00000  89  PRO   E N   
12290 C CA  . PRO   I  89  ? 0.45529 0.45529 0.45529 0.00000  0.00000  0.00000  89  PRO   E CA  
12291 C C   . PRO   I  89  ? 0.80618 0.80618 0.80618 0.00000  0.00000  0.00000  89  PRO   E C   
12292 O O   . PRO   I  89  ? 0.58579 0.58579 0.58579 -0.00000 -0.00000 0.00000  89  PRO   E O   
12293 C CB  . PRO   I  89  ? 0.73859 0.73859 0.73859 -0.00000 0.00000  0.00000  89  PRO   E CB  
12294 C CG  . PRO   I  89  ? 0.70908 0.70908 0.70908 0.00000  0.00000  -0.00000 89  PRO   E CG  
12295 C CD  . PRO   I  89  ? 0.64064 0.64064 0.64064 0.00000  0.00000  0.00000  89  PRO   E CD  
12296 N N   . ARG   I  90  ? 0.58169 0.58169 0.58169 0.00000  0.00000  0.00000  90  ARG   E N   
12297 C CA  . ARG   I  90  ? 0.79699 0.79699 0.79699 -0.00000 0.00000  0.00000  90  ARG   E CA  
12298 C C   . ARG   I  90  ? 0.67901 0.67901 0.67901 0.00000  0.00000  0.00000  90  ARG   E C   
12299 O O   . ARG   I  90  ? 0.67378 0.67378 0.67378 0.00000  0.00000  0.00000  90  ARG   E O   
12300 C CB  . ARG   I  90  ? 0.59930 0.59930 0.59930 0.00000  0.00000  0.00000  90  ARG   E CB  
12301 C CG  . ARG   I  90  ? 0.52106 0.52106 0.52106 0.00000  0.00000  0.00000  90  ARG   E CG  
12302 C CD  . ARG   I  90  ? 0.48137 0.48137 0.48137 -0.00000 0.00000  0.00000  90  ARG   E CD  
12303 N NE  . ARG   I  90  ? 1.30294 1.30294 1.30294 -0.00000 0.00000  0.00000  90  ARG   E NE  
12304 C CZ  . ARG   I  90  ? 0.34433 0.34433 0.34433 0.00000  0.00000  0.00000  90  ARG   E CZ  
12305 N NH1 . ARG   I  90  ? 0.74955 0.74955 0.74955 0.00000  0.00000  0.00000  90  ARG   E NH1 
12306 N NH2 . ARG   I  90  ? 0.55815 0.55815 0.55815 0.00000  0.00000  0.00000  90  ARG   E NH2 
12307 N N   . ASN   I  91  ? 0.50979 0.50979 0.50979 0.00000  0.00000  0.00000  91  ASN   E N   
12308 C CA  . ASN   I  91  ? 0.56653 0.56653 0.56653 0.00000  0.00000  0.00000  91  ASN   E CA  
12309 C C   . ASN   I  91  ? 0.54914 0.54914 0.54914 -0.00000 0.00000  0.00000  91  ASN   E C   
12310 O O   . ASN   I  91  ? 0.63214 0.63214 0.63214 0.00000  0.00000  0.00000  91  ASN   E O   
12311 C CB  . ASN   I  91  ? 0.46523 0.46523 0.46523 0.00000  0.00000  0.00000  91  ASN   E CB  
12312 C CG  . ASN   I  91  ? 0.60046 0.60046 0.60046 0.00000  0.00000  0.00000  91  ASN   E CG  
12313 O OD1 . ASN   I  91  ? 0.72952 0.72952 0.72952 0.00000  0.00000  0.00000  91  ASN   E OD1 
12314 N ND2 . ASN   I  91  ? 0.55013 0.55013 0.55013 0.00000  0.00000  0.00000  91  ASN   E ND2 
12315 N N   . TYR   I  92  ? 0.69182 0.69182 0.69182 0.00000  0.00000  0.00000  92  TYR   E N   
12316 C CA  . TYR   I  92  ? 0.61256 0.61256 0.61256 0.00000  0.00000  0.00000  92  TYR   E CA  
12317 C C   . TYR   I  92  ? 0.66441 0.66441 0.66441 0.00000  -0.00000 -0.00000 92  TYR   E C   
12318 O O   . TYR   I  92  ? 0.72414 0.72414 0.72414 0.00000  -0.00000 -0.00000 92  TYR   E O   
12319 C CB  . TYR   I  92  ? 0.47599 0.47599 0.47599 0.00000  0.00000  0.00000  92  TYR   E CB  
12320 C CG  . TYR   I  92  ? 0.54522 0.54522 0.54522 0.00000  0.00000  0.00000  92  TYR   E CG  
12321 C CD1 . TYR   I  92  ? 0.52265 0.52265 0.52265 0.00000  0.00000  0.00000  92  TYR   E CD1 
12322 C CD2 . TYR   I  92  ? 0.62671 0.62671 0.62671 -0.00000 -0.00000 0.00000  92  TYR   E CD2 
12323 C CE1 . TYR   I  92  ? 0.76305 0.76305 0.76305 0.00000  0.00000  0.00000  92  TYR   E CE1 
12324 C CE2 . TYR   I  92  ? 0.72626 0.72626 0.72626 0.00000  -0.00000 0.00000  92  TYR   E CE2 
12325 C CZ  . TYR   I  92  ? 0.66981 0.66981 0.66981 -0.00000 0.00000  0.00000  92  TYR   E CZ  
12326 O OH  . TYR   I  92  ? 0.88204 0.88204 0.88204 0.00000  0.00000  0.00000  92  TYR   E OH  
12327 N N   . GLN   I  93  ? 0.57374 0.57374 0.57374 -0.00000 0.00000  0.00000  93  GLN   E N   
12328 C CA  . GLN   I  93  ? 0.73342 0.73342 0.73342 0.00000  0.00000  0.00000  93  GLN   E CA  
12329 C C   . GLN   I  93  ? 0.55672 0.55672 0.55672 0.00000  0.00000  0.00000  93  GLN   E C   
12330 O O   . GLN   I  93  ? 0.62524 0.62524 0.62524 0.00000  -0.00000 0.00000  93  GLN   E O   
12331 C CB  . GLN   I  93  ? 0.49118 0.49118 0.49118 0.00000  0.00000  0.00000  93  GLN   E CB  
12332 C CG  . GLN   I  93  ? 0.70307 0.70307 0.70307 -0.00000 0.00000  0.00000  93  GLN   E CG  
12333 C CD  . GLN   I  93  ? 2.21410 2.21410 2.21410 0.00000  0.00000  0.00000  93  GLN   E CD  
12334 O OE1 . GLN   I  93  ? 0.67241 0.67241 0.67241 0.00000  0.00000  0.00000  93  GLN   E OE1 
12335 N NE2 . GLN   I  93  ? 0.70052 0.70052 0.70052 0.00000  0.00000  0.00000  93  GLN   E NE2 
12336 N N   . GLU   I  94  ? 0.66806 0.66806 0.66806 0.00000  0.00000  0.00000  94  GLU   E N   
12337 C CA  . GLU   I  94  ? 0.31778 0.31778 0.31778 0.00000  -0.00000 0.00000  94  GLU   E CA  
12338 C C   . GLU   I  94  ? 0.75479 0.75479 0.75479 0.00000  0.00000  0.00000  94  GLU   E C   
12339 O O   . GLU   I  94  ? 0.71754 0.71754 0.71754 0.00000  0.00000  0.00000  94  GLU   E O   
12340 C CB  . GLU   I  94  ? 0.71598 0.71598 0.71598 -0.00000 -0.00000 -0.00000 94  GLU   E CB  
12341 C CG  . GLU   I  94  ? 0.98883 0.98883 0.98883 -0.00000 0.00000  -0.00000 94  GLU   E CG  
12342 C CD  . GLU   I  94  ? 1.78292 1.78292 1.78292 0.00000  0.00000  0.00000  94  GLU   E CD  
12343 O OE1 . GLU   I  94  ? 0.62362 0.62362 0.62362 -0.00000 0.00000  0.00000  94  GLU   E OE1 
12344 O OE2 . GLU   I  94  ? 1.30383 1.30383 1.30383 0.00000  0.00000  0.00000  94  GLU   E OE2 
12345 N N   . LEU   I  95  ? 0.65060 0.65060 0.65060 0.00000  -0.00000 0.00000  95  LEU   E N   
12346 C CA  . LEU   I  95  ? 0.41050 0.41050 0.41050 0.00000  0.00000  0.00000  95  LEU   E CA  
12347 C C   . LEU   I  95  ? 0.46279 0.46279 0.46279 0.00000  0.00000  0.00000  95  LEU   E C   
12348 O O   . LEU   I  95  ? 0.41225 0.41225 0.41225 -0.00000 0.00000  0.00000  95  LEU   E O   
12349 C CB  . LEU   I  95  ? 0.50054 0.50054 0.50054 0.00000  0.00000  0.00000  95  LEU   E CB  
12350 C CG  . LEU   I  95  ? 0.50139 0.50139 0.50139 0.00000  0.00000  0.00000  95  LEU   E CG  
12351 C CD1 . LEU   I  95  ? 0.42905 0.42905 0.42905 -0.00000 0.00000  0.00000  95  LEU   E CD1 
12352 C CD2 . LEU   I  95  ? 0.31758 0.31758 0.31758 0.00000  0.00000  0.00000  95  LEU   E CD2 
12353 N N   . CYS   I  96  ? 0.35851 0.35851 0.35851 -0.00000 0.00000  0.00000  96  CYS   E N   
12354 C CA  . CYS   I  96  ? 0.49515 0.49515 0.49515 -0.00000 0.00000  0.00000  96  CYS   E CA  
12355 C C   . CYS   I  96  ? 0.49767 0.49767 0.49767 0.00000  0.00000  0.00000  96  CYS   E C   
12356 O O   . CYS   I  96  ? 0.74261 0.74261 0.74261 -0.00000 0.00000  0.00000  96  CYS   E O   
12357 C CB  . CYS   I  96  ? 0.41325 0.41325 0.41325 -0.00000 0.00000  0.00000  96  CYS   E CB  
12358 S SG  . CYS   I  96  ? 0.61215 0.61215 0.61215 0.00000  0.00000  0.00000  96  CYS   E SG  
12359 N N   . ASN   I  97  ? 0.66294 0.66294 0.66294 -0.00000 0.00000  0.00000  97  ASN   E N   
12360 C CA  . ASN   I  97  ? 0.53971 0.53971 0.53971 0.00000  0.00000  0.00000  97  ASN   E CA  
12361 C C   . ASN   I  97  ? 0.85418 0.85418 0.85418 0.00000  0.00000  0.00000  97  ASN   E C   
12362 O O   . ASN   I  97  ? 0.61877 0.61877 0.61877 0.00000  0.00000  -0.00000 97  ASN   E O   
12363 C CB  . ASN   I  97  ? 0.68570 0.68570 0.68570 -0.00000 0.00000  0.00000  97  ASN   E CB  
12364 C CG  . ASN   I  97  ? 1.18565 1.18565 1.18565 0.00000  0.00000  0.00000  97  ASN   E CG  
12365 O OD1 . ASN   I  97  ? 0.83819 0.83819 0.83819 -0.00000 0.00000  0.00000  97  ASN   E OD1 
12366 N ND2 . ASN   I  97  ? 0.64828 0.64828 0.64828 -0.00000 0.00000  0.00000  97  ASN   E ND2 
12367 N N   . MET   I  98  ? 0.39797 0.39797 0.39797 -0.00000 0.00000  0.00000  98  MET   E N   
12368 C CA  . MET   I  98  ? 0.35149 0.35149 0.35149 0.00000  0.00000  0.00000  98  MET   E CA  
12369 C C   . MET   I  98  ? 0.83334 0.83334 0.83334 -0.00000 0.00000  0.00000  98  MET   E C   
12370 O O   . MET   I  98  ? 0.57825 0.57825 0.57825 -0.00000 0.00000  0.00000  98  MET   E O   
12371 C CB  . MET   I  98  ? 0.43833 0.43833 0.43833 0.00000  -0.00000 0.00000  98  MET   E CB  
12372 C CG  . MET   I  98  ? 0.29894 0.29894 0.29894 0.00000  0.00000  0.00000  98  MET   E CG  
12373 S SD  . MET   I  98  ? 0.69288 0.69288 0.69288 0.00000  0.00000  0.00000  98  MET   E SD  
12374 C CE  . MET   I  98  ? 0.52441 0.52441 0.52441 -0.00000 0.00000  0.00000  98  MET   E CE  
12375 N N   . PHE   I  99  ? 0.49816 0.49816 0.49816 0.00000  0.00000  0.00000  99  PHE   E N   
12376 C CA  . PHE   I  99  ? 0.44786 0.44786 0.44786 -0.00000 0.00000  0.00000  99  PHE   E CA  
12377 C C   . PHE   I  99  ? 0.56625 0.56625 0.56625 -0.00000 -0.00000 -0.00000 99  PHE   E C   
12378 O O   . PHE   I  99  ? 0.55188 0.55188 0.55188 -0.00000 0.00000  0.00000  99  PHE   E O   
12379 C CB  . PHE   I  99  ? 0.42856 0.42856 0.42856 0.00000  0.00000  0.00000  99  PHE   E CB  
12380 C CG  . PHE   I  99  ? 0.53257 0.53257 0.53257 0.00000  -0.00000 0.00000  99  PHE   E CG  
12381 C CD1 . PHE   I  99  ? 0.40371 0.40371 0.40371 0.00000  0.00000  0.00000  99  PHE   E CD1 
12382 C CD2 . PHE   I  99  ? 0.51548 0.51548 0.51548 -0.00000 0.00000  0.00000  99  PHE   E CD2 
12383 C CE1 . PHE   I  99  ? 0.60060 0.60060 0.60060 0.00000  0.00000  0.00000  99  PHE   E CE1 
12384 C CE2 . PHE   I  99  ? 0.39281 0.39281 0.39281 -0.00000 0.00000  0.00000  99  PHE   E CE2 
12385 C CZ  . PHE   I  99  ? 0.44479 0.44479 0.44479 0.00000  0.00000  0.00000  99  PHE   E CZ  
12386 N N   . ASN   I  100 ? 0.46395 0.46395 0.46395 0.00000  0.00000  0.00000  100 ASN   E N   
12387 C CA  . ASN   I  100 ? 0.51782 0.51782 0.51782 -0.00000 0.00000  0.00000  100 ASN   E CA  
12388 C C   . ASN   I  100 ? 0.56575 0.56575 0.56575 0.00000  0.00000  0.00000  100 ASN   E C   
12389 O O   . ASN   I  100 ? 0.65764 0.65764 0.65764 -0.00000 0.00000  0.00000  100 ASN   E O   
12390 C CB  . ASN   I  100 ? 0.51133 0.51133 0.51133 0.00000  0.00000  0.00000  100 ASN   E CB  
12391 C CG  . ASN   I  100 ? 0.65637 0.65637 0.65637 -0.00000 0.00000  0.00000  100 ASN   E CG  
12392 O OD1 . ASN   I  100 ? 0.81654 0.81654 0.81654 -0.00000 0.00000  0.00000  100 ASN   E OD1 
12393 N ND2 . ASN   I  100 ? 0.65232 0.65232 0.65232 0.00000  0.00000  0.00000  100 ASN   E ND2 
12394 N N   . ASP   I  101 ? 0.54985 0.54985 0.54985 0.00000  0.00000  0.00000  101 ASP   E N   
12395 C CA  . ASP   I  101 ? 0.47038 0.47038 0.47038 0.00000  0.00000  0.00000  101 ASP   E CA  
12396 C C   . ASP   I  101 ? 0.75739 0.75739 0.75739 0.00000  0.00000  0.00000  101 ASP   E C   
12397 O O   . ASP   I  101 ? 0.65194 0.65194 0.65194 0.00000  0.00000  0.00000  101 ASP   E O   
12398 C CB  . ASP   I  101 ? 0.47134 0.47134 0.47134 -0.00000 0.00000  0.00000  101 ASP   E CB  
12399 C CG  . ASP   I  101 ? 1.51951 1.51951 1.51951 -0.00000 0.00000  0.00000  101 ASP   E CG  
12400 O OD1 . ASP   I  101 ? 0.69994 0.69994 0.69994 0.00000  0.00000  0.00000  101 ASP   E OD1 
12401 O OD2 . ASP   I  101 ? 0.82225 0.82225 0.82225 0.00000  0.00000  0.00000  101 ASP   E OD2 
12402 N N   . ILE   I  102 ? 0.60060 0.60060 0.60060 0.00000  0.00000  0.00000  102 ILE   E N   
12403 C CA  . ILE   I  102 ? 0.40373 0.40373 0.40373 0.00000  0.00000  0.00000  102 ILE   E CA  
12404 C C   . ILE   I  102 ? 0.72747 0.72747 0.72747 0.00000  0.00000  0.00000  102 ILE   E C   
12405 O O   . ILE   I  102 ? 0.51898 0.51898 0.51898 -0.00000 0.00000  0.00000  102 ILE   E O   
12406 C CB  . ILE   I  102 ? 0.43956 0.43956 0.43956 0.00000  0.00000  0.00000  102 ILE   E CB  
12407 C CG1 . ILE   I  102 ? 0.24727 0.24727 0.24727 0.00000  0.00000  0.00000  102 ILE   E CG1 
12408 C CG2 . ILE   I  102 ? 0.30318 0.30318 0.30318 0.00000  -0.00000 0.00000  102 ILE   E CG2 
12409 C CD1 . ILE   I  102 ? 0.51432 0.51432 0.51432 0.00000  0.00000  0.00000  102 ILE   E CD1 
12410 N N   . PHE   I  103 ? 0.39385 0.39385 0.39385 -0.00000 0.00000  0.00000  103 PHE   E N   
12411 C CA  . PHE   I  103 ? 0.70432 0.70432 0.70432 0.00000  0.00000  0.00000  103 PHE   E CA  
12412 C C   . PHE   I  103 ? 0.42422 0.42422 0.42422 0.00000  0.00000  0.00000  103 PHE   E C   
12413 O O   . PHE   I  103 ? 0.53011 0.53011 0.53011 -0.00000 -0.00000 0.00000  103 PHE   E O   
12414 C CB  . PHE   I  103 ? 0.29153 0.29153 0.29153 0.00000  0.00000  0.00000  103 PHE   E CB  
12415 C CG  . PHE   I  103 ? 0.51011 0.51011 0.51011 -0.00000 0.00000  -0.00000 103 PHE   E CG  
12416 C CD1 . PHE   I  103 ? 0.45914 0.45914 0.45914 0.00000  0.00000  0.00000  103 PHE   E CD1 
12417 C CD2 . PHE   I  103 ? 0.35851 0.35851 0.35851 -0.00000 0.00000  0.00000  103 PHE   E CD2 
12418 C CE1 . PHE   I  103 ? 0.61426 0.61426 0.61426 0.00000  -0.00000 0.00000  103 PHE   E CE1 
12419 C CE2 . PHE   I  103 ? 0.51217 0.51217 0.51217 -0.00000 0.00000  0.00000  103 PHE   E CE2 
12420 C CZ  . PHE   I  103 ? 0.50309 0.50309 0.50309 0.00000  0.00000  0.00000  103 PHE   E CZ  
12421 N N   . ARG   I  104 ? 0.86743 0.86743 0.86743 0.00000  0.00000  0.00000  104 ARG   E N   
12422 C CA  . ARG   I  104 ? 0.33695 0.33695 0.33695 -0.00000 0.00000  0.00000  104 ARG   E CA  
12423 C C   . ARG   I  104 ? 1.21027 1.21027 1.21027 -0.00000 0.00000  0.00000  104 ARG   E C   
12424 O O   . ARG   I  104 ? 0.38486 0.38486 0.38486 0.00000  0.00000  0.00000  104 ARG   E O   
12425 C CB  . ARG   I  104 ? 0.58465 0.58465 0.58465 0.00000  0.00000  0.00000  104 ARG   E CB  
12426 C CG  . ARG   I  104 ? 0.44104 0.44104 0.44104 -0.00000 0.00000  0.00000  104 ARG   E CG  
12427 C CD  . ARG   I  104 ? 0.90756 0.90756 0.90756 0.00000  0.00000  0.00000  104 ARG   E CD  
12428 N NE  . ARG   I  104 ? 1.11494 1.11494 1.11494 0.00000  0.00000  0.00000  104 ARG   E NE  
12429 C CZ  . ARG   I  104 ? 1.55090 1.55090 1.55090 0.00000  0.00000  0.00000  104 ARG   E CZ  
12430 N NH1 . ARG   I  104 ? 1.58037 1.58037 1.58037 0.00000  0.00000  0.00000  104 ARG   E NH1 
12431 N NH2 . ARG   I  104 ? 1.76104 1.76104 1.76104 -0.00000 0.00000  0.00000  104 ARG   E NH2 
12432 N N   . LYS   I  105 ? 0.49689 0.49689 0.49689 0.00000  0.00000  0.00000  105 LYS   E N   
12433 C CA  . LYS   I  105 ? 0.75953 0.75953 0.75953 0.00000  0.00000  0.00000  105 LYS   E CA  
12434 C C   . LYS   I  105 ? 0.53828 0.53828 0.53828 -0.00000 0.00000  0.00000  105 LYS   E C   
12435 O O   . LYS   I  105 ? 0.59688 0.59688 0.59688 0.00000  0.00000  0.00000  105 LYS   E O   
12436 C CB  . LYS   I  105 ? 0.63563 0.63563 0.63563 0.00000  0.00000  0.00000  105 LYS   E CB  
12437 C CG  . LYS   I  105 ? 0.50828 0.50828 0.50828 -0.00000 0.00000  0.00000  105 LYS   E CG  
12438 C CD  . LYS   I  105 ? 0.51417 0.51417 0.51417 -0.00000 0.00000  0.00000  105 LYS   E CD  
12439 C CE  . LYS   I  105 ? 0.89674 0.89674 0.89674 -0.00000 0.00000  0.00000  105 LYS   E CE  
12440 N NZ  . LYS   I  105 ? 1.05953 1.05953 1.05953 0.00000  0.00000  0.00000  105 LYS   E NZ  
12441 N N   . ALA   I  106 ? 0.65241 0.65241 0.65241 0.00000  0.00000  0.00000  106 ALA   E N   
12442 C CA  . ALA   I  106 ? 0.56707 0.56707 0.56707 0.00000  0.00000  0.00000  106 ALA   E CA  
12443 C C   . ALA   I  106 ? 0.35671 0.35671 0.35671 -0.00000 0.00000  0.00000  106 ALA   E C   
12444 O O   . ALA   I  106 ? 0.60178 0.60178 0.60178 -0.00000 0.00000  0.00000  106 ALA   E O   
12445 C CB  . ALA   I  106 ? 0.39365 0.39365 0.39365 0.00000  0.00000  0.00000  106 ALA   E CB  
12446 N N   . PRO   I  107 ? 0.73409 0.73409 0.73409 0.00000  -0.00000 -0.00000 107 PRO   E N   
12447 C CA  . PRO   I  107 ? 0.51033 0.51033 0.51033 0.00000  0.00000  0.00000  107 PRO   E CA  
12448 C C   . PRO   I  107 ? 0.63549 0.63549 0.63549 0.00000  0.00000  0.00000  107 PRO   E C   
12449 O O   . PRO   I  107 ? 0.57550 0.57550 0.57550 0.00000  -0.00000 0.00000  107 PRO   E O   
12450 C CB  . PRO   I  107 ? 0.48570 0.48570 0.48570 0.00000  0.00000  0.00000  107 PRO   E CB  
12451 C CG  . PRO   I  107 ? 0.44278 0.44278 0.44278 0.00000  0.00000  0.00000  107 PRO   E CG  
12452 C CD  . PRO   I  107 ? 0.36462 0.36462 0.36462 0.00000  0.00000  0.00000  107 PRO   E CD  
12453 N N   . VAL   I  108 ? 0.67486 0.67486 0.67486 0.00000  0.00000  0.00000  108 VAL   E N   
12454 C CA  . VAL   I  108 ? 0.62250 0.62250 0.62250 -0.00000 0.00000  0.00000  108 VAL   E CA  
12455 C C   . VAL   I  108 ? 0.76476 0.76476 0.76476 0.00000  0.00000  0.00000  108 VAL   E C   
12456 O O   . VAL   I  108 ? 0.77255 0.77255 0.77255 0.00000  0.00000  0.00000  108 VAL   E O   
12457 C CB  . VAL   I  108 ? 0.75214 0.75214 0.75214 0.00000  0.00000  0.00000  108 VAL   E CB  
12458 C CG1 . VAL   I  108 ? 0.51179 0.51179 0.51179 -0.00000 0.00000  0.00000  108 VAL   E CG1 
12459 C CG2 . VAL   I  108 ? 0.50857 0.50857 0.50857 0.00000  0.00000  0.00000  108 VAL   E CG2 
12460 N N   . TYR   I  109 ? 0.55121 0.55121 0.55121 0.00000  0.00000  0.00000  109 TYR   E N   
12461 C CA  . TYR   I  109 ? 0.92424 0.92424 0.92424 0.00000  0.00000  0.00000  109 TYR   E CA  
12462 C C   . TYR   I  109 ? 0.54762 0.54762 0.54762 0.00000  0.00000  0.00000  109 TYR   E C   
12463 O O   . TYR   I  109 ? 0.72398 0.72398 0.72398 0.00000  0.00000  0.00000  109 TYR   E O   
12464 C CB  . TYR   I  109 ? 0.47358 0.47358 0.47358 0.00000  0.00000  0.00000  109 TYR   E CB  
12465 C CG  . TYR   I  109 ? 0.88906 0.88906 0.88906 0.00000  0.00000  0.00000  109 TYR   E CG  
12466 C CD1 . TYR   I  109 ? 0.49000 0.49000 0.49000 -0.00000 0.00000  0.00000  109 TYR   E CD1 
12467 C CD2 . TYR   I  109 ? 0.54039 0.54039 0.54039 0.00000  0.00000  0.00000  109 TYR   E CD2 
12468 C CE1 . TYR   I  109 ? 1.01778 1.01778 1.01778 0.00000  0.00000  0.00000  109 TYR   E CE1 
12469 C CE2 . TYR   I  109 ? 0.80815 0.80815 0.80815 0.00000  0.00000  0.00000  109 TYR   E CE2 
12470 C CZ  . TYR   I  109 ? 0.50693 0.50693 0.50693 0.00000  0.00000  0.00000  109 TYR   E CZ  
12471 O OH  . TYR   I  109 ? 0.83964 0.83964 0.83964 0.00000  0.00000  0.00000  109 TYR   E OH  
12472 N N   . GLY   I  110 ? 0.71383 0.71383 0.71383 -0.00000 0.00000  0.00000  110 GLY   E N   
12473 C CA  . GLY   I  110 ? 0.27054 0.27054 0.27054 0.00000  0.00000  0.00000  110 GLY   E CA  
12474 C C   . GLY   I  110 ? 0.69732 0.69732 0.69732 0.00000  0.00000  0.00000  110 GLY   E C   
12475 O O   . GLY   I  110 ? 0.62135 0.62135 0.62135 0.00000  0.00000  0.00000  110 GLY   E O   
12476 N N   . ASP   I  111 ? 0.65611 0.65611 0.65611 -0.00000 0.00000  0.00000  111 ASP   E N   
12477 C CA  . ASP   I  111 ? 0.53678 0.53678 0.53678 0.00000  0.00000  0.00000  111 ASP   E CA  
12478 C C   . ASP   I  111 ? 0.33473 0.33473 0.33473 -0.00000 0.00000  0.00000  111 ASP   E C   
12479 O O   . ASP   I  111 ? 0.50359 0.50359 0.50359 0.00000  0.00000  0.00000  111 ASP   E O   
12480 C CB  . ASP   I  111 ? 0.69803 0.69803 0.69803 0.00000  0.00000  0.00000  111 ASP   E CB  
12481 C CG  . ASP   I  111 ? 0.68171 0.68171 0.68171 0.00000  0.00000  0.00000  111 ASP   E CG  
12482 O OD1 . ASP   I  111 ? 0.88204 0.88204 0.88204 -0.00000 0.00000  0.00000  111 ASP   E OD1 
12483 O OD2 . ASP   I  111 ? 1.12101 1.12101 1.12101 0.00000  -0.00000 0.00000  111 ASP   E OD2 
12484 N N   . LEU   I  112 ? 0.91549 0.91549 0.91549 -0.00000 0.00000  0.00000  112 LEU   E N   
12485 C CA  . LEU   I  112 ? 0.38163 0.38163 0.38163 0.00000  0.00000  0.00000  112 LEU   E CA  
12486 C C   . LEU   I  112 ? 0.97403 0.97403 0.97403 -0.00000 0.00000  0.00000  112 LEU   E C   
12487 O O   . LEU   I  112 ? 0.50023 0.50023 0.50023 0.00000  0.00000  0.00000  112 LEU   E O   
12488 C CB  . LEU   I  112 ? 1.07640 1.07640 1.07640 0.00000  -0.00000 0.00000  112 LEU   E CB  
12489 C CG  . LEU   I  112 ? 1.57715 1.57715 1.57715 0.00000  0.00000  0.00000  112 LEU   E CG  
12490 C CD1 . LEU   I  112 ? 1.29501 1.29501 1.29501 0.00000  0.00000  0.00000  112 LEU   E CD1 
12491 C CD2 . LEU   I  112 ? 1.04646 1.04646 1.04646 -0.00000 0.00000  0.00000  112 LEU   E CD2 
12492 N N   . GLY   I  113 ? 0.52385 0.52385 0.52385 -0.00000 0.00000  0.00000  113 GLY   E N   
12493 C CA  . GLY   I  113 ? 0.50459 0.50459 0.50459 -0.00000 0.00000  0.00000  113 GLY   E CA  
12494 C C   . GLY   I  113 ? 0.55005 0.55005 0.55005 0.00000  0.00000  0.00000  113 GLY   E C   
12495 O O   . GLY   I  113 ? 0.53028 0.53028 0.53028 0.00000  0.00000  0.00000  113 GLY   E O   
12496 N N   . PRO   I  114 ? 0.47733 0.47733 0.47733 -0.00000 0.00000  0.00000  114 PRO   E N   
12497 C CA  . PRO   I  114 ? 0.39270 0.39270 0.39270 -0.00000 0.00000  0.00000  114 PRO   E CA  
12498 C C   . PRO   I  114 ? 0.43019 0.43019 0.43019 -0.00000 0.00000  0.00000  114 PRO   E C   
12499 O O   . PRO   I  114 ? 0.48679 0.48679 0.48679 0.00000  0.00000  0.00000  114 PRO   E O   
12500 C CB  . PRO   I  114 ? 0.45617 0.45617 0.45617 0.00000  0.00000  0.00000  114 PRO   E CB  
12501 C CG  . PRO   I  114 ? 0.41761 0.41761 0.41761 -0.00000 0.00000  0.00000  114 PRO   E CG  
12502 C CD  . PRO   I  114 ? 0.43136 0.43136 0.43136 -0.00000 0.00000  0.00000  114 PRO   E CD  
12503 N N   . PRO   I  115 ? 0.49915 0.49915 0.49915 -0.00000 0.00000  0.00000  115 PRO   E N   
12504 C CA  . PRO   I  115 ? 0.63828 0.63828 0.63828 0.00000  0.00000  0.00000  115 PRO   E CA  
12505 C C   . PRO   I  115 ? 0.53821 0.53821 0.53821 -0.00000 0.00000  0.00000  115 PRO   E C   
12506 O O   . PRO   I  115 ? 0.60271 0.60271 0.60271 -0.00000 0.00000  0.00000  115 PRO   E O   
12507 C CB  . PRO   I  115 ? 0.40742 0.40742 0.40742 -0.00000 0.00000  0.00000  115 PRO   E CB  
12508 C CG  . PRO   I  115 ? 0.43982 0.43982 0.43982 0.00000  -0.00000 0.00000  115 PRO   E CG  
12509 C CD  . PRO   I  115 ? 0.56607 0.56607 0.56607 0.00000  0.00000  0.00000  115 PRO   E CD  
12510 N N   . VAL   I  116 ? 0.53213 0.53213 0.53213 0.00000  -0.00000 0.00000  116 VAL   E N   
12511 C CA  . VAL   I  116 ? 0.40878 0.40878 0.40878 -0.00000 0.00000  0.00000  116 VAL   E CA  
12512 C C   . VAL   I  116 ? 0.44020 0.44020 0.44020 -0.00000 0.00000  0.00000  116 VAL   E C   
12513 O O   . VAL   I  116 ? 0.48547 0.48547 0.48547 0.00000  0.00000  0.00000  116 VAL   E O   
12514 C CB  . VAL   I  116 ? 0.49960 0.49960 0.49960 0.00000  0.00000  0.00000  116 VAL   E CB  
12515 C CG1 . VAL   I  116 ? 0.39922 0.39922 0.39922 0.00000  0.00000  0.00000  116 VAL   E CG1 
12516 C CG2 . VAL   I  116 ? 0.29738 0.29738 0.29738 0.00000  0.00000  0.00000  116 VAL   E CG2 
12517 N N   . TYR   I  117 ? 0.42998 0.42998 0.42998 -0.00000 0.00000  0.00000  117 TYR   E N   
12518 C CA  . TYR   I  117 ? 0.60137 0.60137 0.60137 0.00000  0.00000  0.00000  117 TYR   E CA  
12519 C C   . TYR   I  117 ? 0.52564 0.52564 0.52564 -0.00000 0.00000  0.00000  117 TYR   E C   
12520 O O   . TYR   I  117 ? 0.58912 0.58912 0.58912 0.00000  0.00000  0.00000  117 TYR   E O   
12521 C CB  . TYR   I  117 ? 0.41881 0.41881 0.41881 -0.00000 0.00000  0.00000  117 TYR   E CB  
12522 C CG  . TYR   I  117 ? 0.51088 0.51088 0.51088 -0.00000 0.00000  0.00000  117 TYR   E CG  
12523 C CD1 . TYR   I  117 ? 0.46312 0.46312 0.46312 0.00000  0.00000  0.00000  117 TYR   E CD1 
12524 C CD2 . TYR   I  117 ? 0.67476 0.67476 0.67476 0.00000  0.00000  0.00000  117 TYR   E CD2 
12525 C CE1 . TYR   I  117 ? 0.46859 0.46859 0.46859 -0.00000 0.00000  0.00000  117 TYR   E CE1 
12526 C CE2 . TYR   I  117 ? 0.38871 0.38871 0.38871 0.00000  0.00000  0.00000  117 TYR   E CE2 
12527 C CZ  . TYR   I  117 ? 0.59677 0.59677 0.59677 0.00000  0.00000  0.00000  117 TYR   E CZ  
12528 O OH  . TYR   I  117 ? 0.46687 0.46687 0.46687 -0.00000 0.00000  0.00000  117 TYR   E OH  
12529 N N   . MET   I  118 ? 0.56032 0.56032 0.56032 -0.00000 0.00000  0.00000  118 MET   E N   
12530 C CA  . MET   I  118 ? 0.43154 0.43154 0.43154 0.00000  0.00000  0.00000  118 MET   E CA  
12531 C C   . MET   I  118 ? 0.62938 0.62938 0.62938 0.00000  0.00000  0.00000  118 MET   E C   
12532 O O   . MET   I  118 ? 0.53018 0.53018 0.53018 0.00000  0.00000  0.00000  118 MET   E O   
12533 C CB  . MET   I  118 ? 0.47041 0.47041 0.47041 0.00000  0.00000  0.00000  118 MET   E CB  
12534 C CG  . MET   I  118 ? 0.33959 0.33959 0.33959 0.00000  0.00000  0.00000  118 MET   E CG  
12535 S SD  . MET   I  118 ? 0.57029 0.57029 0.57029 -0.00000 0.00000  0.00000  118 MET   E SD  
12536 C CE  . MET   I  118 ? 0.62820 0.62820 0.62820 0.00000  0.00000  0.00000  118 MET   E CE  
12537 N N   . ILE   I  119 ? 0.39035 0.39035 0.39035 -0.00000 0.00000  0.00000  119 ILE   E N   
12538 C CA  . ILE   I  119 ? 0.53574 0.53574 0.53574 0.00000  0.00000  0.00000  119 ILE   E CA  
12539 C C   . ILE   I  119 ? 0.54125 0.54125 0.54125 0.00000  0.00000  0.00000  119 ILE   E C   
12540 O O   . ILE   I  119 ? 0.60030 0.60030 0.60030 0.00000  0.00000  0.00000  119 ILE   E O   
12541 C CB  . ILE   I  119 ? 0.43407 0.43407 0.43407 0.00000  0.00000  -0.00000 119 ILE   E CB  
12542 C CG1 . ILE   I  119 ? 0.46306 0.46306 0.46306 0.00000  0.00000  0.00000  119 ILE   E CG1 
12543 C CG2 . ILE   I  119 ? 0.52917 0.52917 0.52917 0.00000  0.00000  0.00000  119 ILE   E CG2 
12544 C CD1 . ILE   I  119 ? 0.52485 0.52485 0.52485 0.00000  0.00000  0.00000  119 ILE   E CD1 
12545 N N   . MET   I  120 ? 0.48685 0.48685 0.48685 -0.00000 0.00000  0.00000  120 MET   E N   
12546 C CA  . MET   I  120 ? 0.46150 0.46150 0.46150 0.00000  0.00000  0.00000  120 MET   E CA  
12547 C C   . MET   I  120 ? 0.53535 0.53535 0.53535 -0.00000 0.00000  0.00000  120 MET   E C   
12548 O O   . MET   I  120 ? 0.53035 0.53035 0.53035 -0.00000 0.00000  0.00000  120 MET   E O   
12549 C CB  . MET   I  120 ? 0.30477 0.30477 0.30477 0.00000  0.00000  0.00000  120 MET   E CB  
12550 C CG  . MET   I  120 ? 0.40471 0.40471 0.40471 0.00000  0.00000  0.00000  120 MET   E CG  
12551 S SD  . MET   I  120 ? 0.60886 0.60886 0.60886 0.00000  0.00000  0.00000  120 MET   E SD  
12552 C CE  . MET   I  120 ? 0.41433 0.41433 0.41433 0.00000  0.00000  0.00000  120 MET   E CE  
12553 N N   . ALA   I  121 ? 0.39848 0.39848 0.39848 0.00000  -0.00000 0.00000  121 ALA   E N   
12554 C CA  . ALA   I  121 ? 0.47175 0.47175 0.47175 0.00000  0.00000  0.00000  121 ALA   E CA  
12555 C C   . ALA   I  121 ? 0.47650 0.47650 0.47650 -0.00000 0.00000  0.00000  121 ALA   E C   
12556 O O   . ALA   I  121 ? 0.56482 0.56482 0.56482 0.00000  0.00000  0.00000  121 ALA   E O   
12557 C CB  . ALA   I  121 ? 0.36936 0.36936 0.36936 0.00000  0.00000  0.00000  121 ALA   E CB  
12558 N N   . LYS   I  122 ? 0.48040 0.48040 0.48040 0.00000  0.00000  0.00000  122 LYS   E N   
12559 C CA  . LYS   I  122 ? 0.38588 0.38588 0.38588 0.00000  0.00000  0.00000  122 LYS   E CA  
12560 C C   . LYS   I  122 ? 0.56604 0.56604 0.56604 0.00000  0.00000  0.00000  122 LYS   E C   
12561 O O   . LYS   I  122 ? 0.48793 0.48793 0.48793 0.00000  0.00000  0.00000  122 LYS   E O   
12562 C CB  . LYS   I  122 ? 0.37847 0.37847 0.37847 -0.00000 0.00000  0.00000  122 LYS   E CB  
12563 N N   . LEU   I  123 ? 0.42572 0.42572 0.42572 0.00000  0.00000  0.00000  123 LEU   E N   
12564 C CA  . LEU   I  123 ? 0.41940 0.41940 0.41940 0.00000  0.00000  0.00000  123 LEU   E CA  
12565 C C   . LEU   I  123 ? 0.73589 0.73589 0.73589 0.00000  0.00000  0.00000  123 LEU   E C   
12566 O O   . LEU   I  123 ? 0.31895 0.31895 0.31895 -0.00000 0.00000  0.00000  123 LEU   E O   
12567 C CB  . LEU   I  123 ? 0.30651 0.30651 0.30651 0.00000  0.00000  0.00000  123 LEU   E CB  
12568 C CG  . LEU   I  123 ? 0.41977 0.41977 0.41977 -0.00000 0.00000  0.00000  123 LEU   E CG  
12569 C CD1 . LEU   I  123 ? 0.34574 0.34574 0.34574 0.00000  0.00000  0.00000  123 LEU   E CD1 
12570 C CD2 . LEU   I  123 ? 0.34358 0.34358 0.34358 0.00000  0.00000  0.00000  123 LEU   E CD2 
12571 N N   . MET   I  124 ? 0.45068 0.45068 0.45068 0.00000  0.00000  0.00000  124 MET   E N   
12572 C CA  . MET   I  124 ? 0.59495 0.59495 0.59495 0.00000  0.00000  0.00000  124 MET   E CA  
12573 C C   . MET   I  124 ? 0.50080 0.50080 0.50080 -0.00000 -0.00000 0.00000  124 MET   E C   
12574 O O   . MET   I  124 ? 0.49003 0.49003 0.49003 0.00000  0.00000  0.00000  124 MET   E O   
12575 C CB  . MET   I  124 ? 0.31103 0.31103 0.31103 0.00000  0.00000  0.00000  124 MET   E CB  
12576 C CG  . MET   I  124 ? 0.56744 0.56744 0.56744 -0.00000 0.00000  0.00000  124 MET   E CG  
12577 S SD  . MET   I  124 ? 0.59132 0.59132 0.59132 0.00000  0.00000  0.00000  124 MET   E SD  
12578 C CE  . MET   I  124 ? 0.28321 0.28321 0.28321 0.00000  0.00000  0.00000  124 MET   E CE  
12579 N N   . ASN   I  125 ? 0.64818 0.64818 0.64818 0.00000  0.00000  0.00000  125 ASN   E N   
12580 C CA  . ASN   I  125 ? 0.57070 0.57070 0.57070 -0.00000 0.00000  0.00000  125 ASN   E CA  
12581 C C   . ASN   I  125 ? 0.64192 0.64192 0.64192 -0.00000 0.00000  0.00000  125 ASN   E C   
12582 O O   . ASN   I  125 ? 0.69243 0.69243 0.69243 -0.00000 0.00000  0.00000  125 ASN   E O   
12583 C CB  . ASN   I  125 ? 0.55152 0.55152 0.55152 0.00000  0.00000  0.00000  125 ASN   E CB  
12584 C CG  . ASN   I  125 ? 0.52785 0.52785 0.52785 0.00000  0.00000  0.00000  125 ASN   E CG  
12585 O OD1 . ASN   I  125 ? 0.60591 0.60591 0.60591 0.00000  0.00000  0.00000  125 ASN   E OD1 
12586 N ND2 . ASN   I  125 ? 0.74712 0.74712 0.74712 0.00000  0.00000  0.00000  125 ASN   E ND2 
12587 N N   . THR   I  126 ? 0.63273 0.63273 0.63273 0.00000  0.00000  0.00000  126 THR   E N   
12588 C CA  . THR   I  126 ? 0.74786 0.74786 0.74786 -0.00000 0.00000  0.00000  126 THR   E CA  
12589 C C   . THR   I  126 ? 0.48025 0.48025 0.48025 0.00000  0.00000  0.00000  126 THR   E C   
12590 O O   . THR   I  126 ? 0.71991 0.71991 0.71991 0.00000  0.00000  0.00000  126 THR   E O   
12591 C CB  . THR   I  126 ? 0.55472 0.55472 0.55472 0.00000  0.00000  0.00000  126 THR   E CB  
12592 O OG1 . THR   I  126 ? 0.54740 0.54740 0.54740 0.00000  0.00000  0.00000  126 THR   E OG1 
12593 C CG2 . THR   I  126 ? 0.36500 0.36500 0.36500 -0.00000 0.00000  0.00000  126 THR   E CG2 
12594 N N   . ARG   I  127 ? 0.57965 0.57965 0.57965 0.00000  0.00000  0.00000  127 ARG   E N   
12595 C CA  . ARG   I  127 ? 0.37548 0.37548 0.37548 0.00000  0.00000  0.00000  127 ARG   E CA  
12596 C C   . ARG   I  127 ? 0.45737 0.45737 0.45737 0.00000  0.00000  0.00000  127 ARG   E C   
12597 O O   . ARG   I  127 ? 0.99851 0.99851 0.99851 0.00000  0.00000  0.00000  127 ARG   E O   
12598 C CB  . ARG   I  127 ? 0.37099 0.37099 0.37099 0.00000  0.00000  0.00000  127 ARG   E CB  
12599 C CG  . ARG   I  127 ? 1.44542 1.44542 1.44542 -0.00000 0.00000  0.00000  127 ARG   E CG  
12600 C CD  . ARG   I  127 ? 1.55018 1.55018 1.55018 0.00000  0.00000  0.00000  127 ARG   E CD  
12601 N NE  . ARG   I  127 ? 1.63631 1.63631 1.63631 0.00000  0.00000  0.00000  127 ARG   E NE  
12602 C CZ  . ARG   I  127 ? 1.87626 1.87626 1.87626 -0.00000 0.00000  0.00000  127 ARG   E CZ  
12603 N NH1 . ARG   I  127 ? 1.77880 1.77880 1.77880 0.00000  0.00000  0.00000  127 ARG   E NH1 
12604 N NH2 . ARG   I  127 ? 1.67479 1.67479 1.67479 0.00000  0.00000  0.00000  127 ARG   E NH2 
12605 N N   . ALA   I  128 ? 0.45887 0.45887 0.45887 -0.00000 0.00000  0.00000  128 ALA   E N   
12606 C CA  . ALA   I  128 ? 0.62316 0.62316 0.62316 0.00000  0.00000  -0.00000 128 ALA   E CA  
12607 C C   . ALA   I  128 ? 0.50830 0.50830 0.50830 0.00000  0.00000  0.00000  128 ALA   E C   
12608 O O   . ALA   I  128 ? 0.64559 0.64559 0.64559 -0.00000 0.00000  0.00000  128 ALA   E O   
12609 C CB  . ALA   I  128 ? 0.48091 0.48091 0.48091 0.00000  0.00000  0.00000  128 ALA   E CB  
12610 N N   . GLY   I  129 ? 0.68882 0.68882 0.68882 -0.00000 0.00000  0.00000  129 GLY   E N   
12611 C CA  . GLY   I  129 ? 0.28365 0.28365 0.28365 -0.00000 0.00000  0.00000  129 GLY   E CA  
12612 C C   . GLY   I  129 ? 0.59391 0.59391 0.59391 -0.00000 0.00000  0.00000  129 GLY   E C   
12613 O O   . GLY   I  129 ? 0.46530 0.46530 0.46530 0.00000  0.00000  0.00000  129 GLY   E O   
12614 N N   . PHE   I  130 ? 0.41864 0.41864 0.41864 -0.00000 0.00000  0.00000  130 PHE   E N   
12615 C CA  . PHE   I  130 ? 0.41974 0.41974 0.41974 -0.00000 0.00000  0.00000  130 PHE   E CA  
12616 C C   . PHE   I  130 ? 0.68484 0.68484 0.68484 0.00000  0.00000  0.00000  130 PHE   E C   
12617 O O   . PHE   I  130 ? 0.57281 0.57281 0.57281 -0.00000 0.00000  0.00000  130 PHE   E O   
12618 C CB  . PHE   I  130 ? 0.27525 0.27525 0.27525 -0.00000 0.00000  0.00000  130 PHE   E CB  
12619 C CG  . PHE   I  130 ? 0.44553 0.44553 0.44553 0.00000  0.00000  0.00000  130 PHE   E CG  
12620 C CD1 . PHE   I  130 ? 0.44548 0.44548 0.44548 -0.00000 0.00000  0.00000  130 PHE   E CD1 
12621 C CD2 . PHE   I  130 ? 0.36444 0.36444 0.36444 0.00000  0.00000  0.00000  130 PHE   E CD2 
12622 C CE1 . PHE   I  130 ? 0.43070 0.43070 0.43070 0.00000  0.00000  0.00000  130 PHE   E CE1 
12623 C CE2 . PHE   I  130 ? 0.53954 0.53954 0.53954 0.00000  0.00000  0.00000  130 PHE   E CE2 
12624 C CZ  . PHE   I  130 ? 0.36790 0.36790 0.36790 0.00000  0.00000  0.00000  130 PHE   E CZ  
12625 N N   . SER   I  131 ? 0.42288 0.42288 0.42288 -0.00000 0.00000  0.00000  131 SER   E N   
12626 C CA  . SER   I  131 ? 0.64672 0.64672 0.64672 -0.00000 -0.00000 0.00000  131 SER   E CA  
12627 C C   . SER   I  131 ? 0.49042 0.49042 0.49042 0.00000  0.00000  0.00000  131 SER   E C   
12628 O O   . SER   I  131 ? 0.62779 0.62779 0.62779 -0.00000 0.00000  0.00000  131 SER   E O   
12629 C CB  . SER   I  131 ? 0.28228 0.28228 0.28228 -0.00000 0.00000  0.00000  131 SER   E CB  
12630 O OG  . SER   I  131 ? 1.19249 1.19249 1.19249 -0.00000 0.00000  0.00000  131 SER   E OG  
12631 N N   . ALA   I  132 ? 0.45157 0.45157 0.45157 0.00000  0.00000  0.00000  132 ALA   E N   
12632 C CA  . ALA   I  132 ? 0.37890 0.37890 0.37890 0.00000  0.00000  0.00000  132 ALA   E CA  
12633 C C   . ALA   I  132 ? 0.55989 0.55989 0.55989 0.00000  0.00000  0.00000  132 ALA   E C   
12634 O O   . ALA   I  132 ? 0.48091 0.48091 0.48091 -0.00000 0.00000  0.00000  132 ALA   E O   
12635 C CB  . ALA   I  132 ? 0.38805 0.38805 0.38805 0.00000  -0.00000 0.00000  132 ALA   E CB  
12636 N N   . PHE   I  133 ? 0.40567 0.40567 0.40567 0.00000  0.00000  0.00000  133 PHE   E N   
12637 C CA  . PHE   I  133 ? 0.53960 0.53960 0.53960 -0.00000 0.00000  0.00000  133 PHE   E CA  
12638 C C   . PHE   I  133 ? 0.62761 0.62761 0.62761 -0.00000 0.00000  0.00000  133 PHE   E C   
12639 O O   . PHE   I  133 ? 0.49478 0.49478 0.49478 -0.00000 0.00000  0.00000  133 PHE   E O   
12640 C CB  . PHE   I  133 ? 0.44105 0.44105 0.44105 0.00000  0.00000  0.00000  133 PHE   E CB  
12641 C CG  . PHE   I  133 ? 0.57973 0.57973 0.57973 0.00000  0.00000  0.00000  133 PHE   E CG  
12642 C CD1 . PHE   I  133 ? 0.52340 0.52340 0.52340 -0.00000 0.00000  0.00000  133 PHE   E CD1 
12643 C CD2 . PHE   I  133 ? 0.45644 0.45644 0.45644 0.00000  0.00000  0.00000  133 PHE   E CD2 
12644 C CE1 . PHE   I  133 ? 0.42036 0.42036 0.42036 0.00000  0.00000  0.00000  133 PHE   E CE1 
12645 C CE2 . PHE   I  133 ? 0.44913 0.44913 0.44913 0.00000  0.00000  0.00000  133 PHE   E CE2 
12646 C CZ  . PHE   I  133 ? 0.37051 0.37051 0.37051 0.00000  0.00000  0.00000  133 PHE   E CZ  
12647 N N   . THR   I  134 ? 0.36994 0.36994 0.36994 0.00000  -0.00000 0.00000  134 THR   E N   
12648 C CA  . THR   I  134 ? 0.42894 0.42894 0.42894 0.00000  0.00000  0.00000  134 THR   E CA  
12649 C C   . THR   I  134 ? 0.40141 0.40141 0.40141 0.00000  -0.00000 0.00000  134 THR   E C   
12650 O O   . THR   I  134 ? 0.50212 0.50212 0.50212 0.00000  0.00000  0.00000  134 THR   E O   
12651 C CB  . THR   I  134 ? 0.42915 0.42915 0.42915 -0.00000 0.00000  0.00000  134 THR   E CB  
12652 O OG1 . THR   I  134 ? 0.50120 0.50120 0.50120 0.00000  0.00000  0.00000  134 THR   E OG1 
12653 C CG2 . THR   I  134 ? 0.34044 0.34044 0.34044 0.00000  0.00000  0.00000  134 THR   E CG2 
12654 N N   . ARG   I  135 ? 0.50530 0.50530 0.50530 -0.00000 0.00000  0.00000  135 ARG   E N   
12655 C CA  . ARG   I  135 ? 0.50756 0.50756 0.50756 0.00000  0.00000  0.00000  135 ARG   E CA  
12656 C C   . ARG   I  135 ? 0.68012 0.68012 0.68012 -0.00000 0.00000  0.00000  135 ARG   E C   
12657 O O   . ARG   I  135 ? 0.51052 0.51052 0.51052 -0.00000 0.00000  0.00000  135 ARG   E O   
12658 C CB  . ARG   I  135 ? 0.39127 0.39127 0.39127 0.00000  0.00000  0.00000  135 ARG   E CB  
12659 C CG  . ARG   I  135 ? 0.44453 0.44453 0.44453 -0.00000 0.00000  0.00000  135 ARG   E CG  
12660 C CD  . ARG   I  135 ? 0.47918 0.47918 0.47918 -0.00000 0.00000  0.00000  135 ARG   E CD  
12661 N NE  . ARG   I  135 ? 0.72355 0.72355 0.72355 0.00000  0.00000  0.00000  135 ARG   E NE  
12662 C CZ  . ARG   I  135 ? 0.77188 0.77188 0.77188 -0.00000 -0.00000 0.00000  135 ARG   E CZ  
12663 N NH1 . ARG   I  135 ? 0.66011 0.66011 0.66011 -0.00000 0.00000  0.00000  135 ARG   E NH1 
12664 N NH2 . ARG   I  135 ? 0.63389 0.63389 0.63389 -0.00000 0.00000  0.00000  135 ARG   E NH2 
12665 N N   . GLN   I  136 ? 0.49409 0.49409 0.49409 -0.00000 0.00000  0.00000  136 GLN   E N   
12666 C CA  . GLN   I  136 ? 0.51966 0.51966 0.51966 0.00000  0.00000  0.00000  136 GLN   E CA  
12667 C C   . GLN   I  136 ? 0.48627 0.48627 0.48627 0.00000  0.00000  0.00000  136 GLN   E C   
12668 O O   . GLN   I  136 ? 0.70784 0.70784 0.70784 0.00000  0.00000  0.00000  136 GLN   E O   
12669 C CB  . GLN   I  136 ? 0.49499 0.49499 0.49499 0.00000  0.00000  0.00000  136 GLN   E CB  
12670 C CG  . GLN   I  136 ? 0.43461 0.43461 0.43461 -0.00000 0.00000  0.00000  136 GLN   E CG  
12671 C CD  . GLN   I  136 ? 0.75451 0.75451 0.75451 0.00000  0.00000  0.00000  136 GLN   E CD  
12672 O OE1 . GLN   I  136 ? 0.60152 0.60152 0.60152 0.00000  0.00000  0.00000  136 GLN   E OE1 
12673 N NE2 . GLN   I  136 ? 0.44098 0.44098 0.44098 -0.00000 0.00000  0.00000  136 GLN   E NE2 
12674 N N   . ARG   I  137 ? 0.28110 0.28110 0.28110 0.00000  0.00000  -0.00000 137 ARG   E N   
12675 C CA  . ARG   I  137 ? 0.80874 0.80874 0.80874 0.00000  0.00000  0.00000  137 ARG   E CA  
12676 C C   . ARG   I  137 ? 0.62729 0.62729 0.62729 0.00000  0.00000  0.00000  137 ARG   E C   
12677 O O   . ARG   I  137 ? 0.32288 0.32288 0.32288 0.00000  0.00000  0.00000  137 ARG   E O   
12678 C CB  . ARG   I  137 ? 1.15871 1.15871 1.15871 -0.00000 0.00000  0.00000  137 ARG   E CB  
12679 C CG  . ARG   I  137 ? 1.14701 1.14701 1.14701 -0.00000 0.00000  0.00000  137 ARG   E CG  
12680 C CD  . ARG   I  137 ? 1.86103 1.86103 1.86103 -0.00000 0.00000  0.00000  137 ARG   E CD  
12681 N NE  . ARG   I  137 ? 2.05712 2.05712 2.05712 0.00000  0.00000  0.00000  137 ARG   E NE  
12682 C CZ  . ARG   I  137 ? 1.73622 1.73622 1.73622 0.00000  0.00000  0.00000  137 ARG   E CZ  
12683 N NH1 . ARG   I  137 ? 1.29948 1.29948 1.29948 0.00000  0.00000  0.00000  137 ARG   E NH1 
12684 N NH2 . ARG   I  137 ? 1.54878 1.54878 1.54878 -0.00000 -0.00000 0.00000  137 ARG   E NH2 
12685 N N   . LEU   I  138 ? 0.36618 0.36618 0.36618 0.00000  0.00000  0.00000  138 LEU   E N   
12686 C CA  . LEU   I  138 ? 0.53155 0.53155 0.53155 -0.00000 0.00000  0.00000  138 LEU   E CA  
12687 C C   . LEU   I  138 ? 0.65110 0.65110 0.65110 0.00000  0.00000  0.00000  138 LEU   E C   
12688 O O   . LEU   I  138 ? 0.51874 0.51874 0.51874 -0.00000 0.00000  0.00000  138 LEU   E O   
12689 C CB  . LEU   I  138 ? 0.45282 0.45282 0.45282 0.00000  0.00000  0.00000  138 LEU   E CB  
12690 C CG  . LEU   I  138 ? 0.62861 0.62861 0.62861 0.00000  0.00000  0.00000  138 LEU   E CG  
12691 C CD1 . LEU   I  138 ? 0.45736 0.45736 0.45736 0.00000  0.00000  0.00000  138 LEU   E CD1 
12692 C CD2 . LEU   I  138 ? 0.42358 0.42358 0.42358 0.00000  0.00000  -0.00000 138 LEU   E CD2 
12693 N N   . ASN   I  139 ? 0.47227 0.47227 0.47227 -0.00000 0.00000  0.00000  139 ASN   E N   
12694 C CA  . ASN   I  139 ? 0.67748 0.67748 0.67748 0.00000  0.00000  0.00000  139 ASN   E CA  
12695 C C   . ASN   I  139 ? 0.50786 0.50786 0.50786 -0.00000 0.00000  0.00000  139 ASN   E C   
12696 O O   . ASN   I  139 ? 0.68393 0.68393 0.68393 0.00000  0.00000  0.00000  139 ASN   E O   
12697 C CB  . ASN   I  139 ? 0.37733 0.37733 0.37733 -0.00000 0.00000  0.00000  139 ASN   E CB  
12698 C CG  . ASN   I  139 ? 0.59039 0.59039 0.59039 0.00000  0.00000  0.00000  139 ASN   E CG  
12699 O OD1 . ASN   I  139 ? 0.48373 0.48373 0.48373 0.00000  0.00000  -0.00000 139 ASN   E OD1 
12700 N ND2 . ASN   I  139 ? 0.44347 0.44347 0.44347 0.00000  0.00000  0.00000  139 ASN   E ND2 
12701 N N   . LEU   I  140 ? 0.62972 0.62972 0.62972 -0.00000 0.00000  0.00000  140 LEU   E N   
12702 C CA  . LEU   I  140 ? 0.47966 0.47966 0.47966 0.00000  0.00000  0.00000  140 LEU   E CA  
12703 C C   . LEU   I  140 ? 0.76184 0.76184 0.76184 0.00000  0.00000  0.00000  140 LEU   E C   
12704 O O   . LEU   I  140 ? 0.49493 0.49493 0.49493 0.00000  0.00000  0.00000  140 LEU   E O   
12705 C CB  . LEU   I  140 ? 0.47382 0.47382 0.47382 0.00000  0.00000  0.00000  140 LEU   E CB  
12706 C CG  . LEU   I  140 ? 0.67951 0.67951 0.67951 0.00000  -0.00000 0.00000  140 LEU   E CG  
12707 C CD1 . LEU   I  140 ? 0.40048 0.40048 0.40048 0.00000  0.00000  0.00000  140 LEU   E CD1 
12708 C CD2 . LEU   I  140 ? 0.32265 0.32265 0.32265 0.00000  0.00000  0.00000  140 LEU   E CD2 
12709 N N   . HIS   I  141 ? 0.46103 0.46103 0.46103 -0.00000 0.00000  0.00000  141 HIS   E N   
12710 C CA  . HIS   I  141 ? 0.43441 0.43441 0.43441 -0.00000 0.00000  0.00000  141 HIS   E CA  
12711 C C   . HIS   I  141 ? 0.44932 0.44932 0.44932 0.00000  0.00000  0.00000  141 HIS   E C   
12712 O O   . HIS   I  141 ? 0.53401 0.53401 0.53401 0.00000  0.00000  0.00000  141 HIS   E O   
12713 C CB  . HIS   I  141 ? 0.30746 0.30746 0.30746 0.00000  0.00000  0.00000  141 HIS   E CB  
12714 C CG  . HIS   I  141 ? 0.65639 0.65639 0.65639 -0.00000 0.00000  0.00000  141 HIS   E CG  
12715 N ND1 . HIS   I  141 ? 0.62900 0.62900 0.62900 -0.00000 -0.00000 0.00000  141 HIS   E ND1 
12716 C CD2 . HIS   I  141 ? 0.56975 0.56975 0.56975 0.00000  0.00000  0.00000  141 HIS   E CD2 
12717 C CE1 . HIS   I  141 ? 0.47097 0.47097 0.47097 0.00000  0.00000  0.00000  141 HIS   E CE1 
12718 N NE2 . HIS   I  141 ? 0.63876 0.63876 0.63876 0.00000  0.00000  0.00000  141 HIS   E NE2 
12719 N N   . PHE   I  142 ? 0.45251 0.45251 0.45251 0.00000  0.00000  0.00000  142 PHE   E N   
12720 C CA  . PHE   I  142 ? 0.62013 0.62013 0.62013 -0.00000 0.00000  0.00000  142 PHE   E CA  
12721 C C   . PHE   I  142 ? 0.45415 0.45415 0.45415 0.00000  0.00000  0.00000  142 PHE   E C   
12722 O O   . PHE   I  142 ? 0.47897 0.47897 0.47897 0.00000  0.00000  0.00000  142 PHE   E O   
12723 C CB  . PHE   I  142 ? 0.44239 0.44239 0.44239 0.00000  0.00000  0.00000  142 PHE   E CB  
12724 C CG  . PHE   I  142 ? 0.53338 0.53338 0.53338 0.00000  -0.00000 0.00000  142 PHE   E CG  
12725 C CD1 . PHE   I  142 ? 0.46793 0.46793 0.46793 -0.00000 0.00000  0.00000  142 PHE   E CD1 
12726 C CD2 . PHE   I  142 ? 0.48681 0.48681 0.48681 0.00000  0.00000  0.00000  142 PHE   E CD2 
12727 C CE1 . PHE   I  142 ? 0.45626 0.45626 0.45626 -0.00000 0.00000  0.00000  142 PHE   E CE1 
12728 C CE2 . PHE   I  142 ? 0.50081 0.50081 0.50081 -0.00000 0.00000  0.00000  142 PHE   E CE2 
12729 C CZ  . PHE   I  142 ? 0.44023 0.44023 0.44023 -0.00000 0.00000  0.00000  142 PHE   E CZ  
12730 N N   . LYS   I  143 ? 0.46077 0.46077 0.46077 0.00000  0.00000  0.00000  143 LYS   E N   
12731 C CA  . LYS   I  143 ? 0.40589 0.40589 0.40589 0.00000  0.00000  0.00000  143 LYS   E CA  
12732 C C   . LYS   I  143 ? 0.44738 0.44738 0.44738 0.00000  0.00000  0.00000  143 LYS   E C   
12733 O O   . LYS   I  143 ? 0.48995 0.48995 0.48995 -0.00000 0.00000  0.00000  143 LYS   E O   
12734 C CB  . LYS   I  143 ? 0.45089 0.45089 0.45089 -0.00000 0.00000  0.00000  143 LYS   E CB  
12735 C CG  . LYS   I  143 ? 0.28073 0.28073 0.28073 0.00000  0.00000  0.00000  143 LYS   E CG  
12736 C CD  . LYS   I  143 ? 0.38410 0.38410 0.38410 0.00000  0.00000  0.00000  143 LYS   E CD  
12737 C CE  . LYS   I  143 ? 0.46716 0.46716 0.46716 0.00000  0.00000  0.00000  143 LYS   E CE  
12738 N NZ  . LYS   I  143 ? 0.52554 0.52554 0.52554 -0.00000 0.00000  0.00000  143 LYS   E NZ  
12739 N N   . LYS   I  144 ? 0.33132 0.33132 0.33132 0.00000  0.00000  0.00000  144 LYS   E N   
12740 C CA  . LYS   I  144 ? 0.74063 0.74063 0.74063 -0.00000 0.00000  0.00000  144 LYS   E CA  
12741 C C   . LYS   I  144 ? 0.21607 0.21607 0.21607 -0.00000 0.00000  0.00000  144 LYS   E C   
12742 O O   . LYS   I  144 ? 0.99494 0.99494 0.99494 -0.00000 0.00000  0.00000  144 LYS   E O   
12743 C CB  . LYS   I  144 ? 0.37089 0.37089 0.37089 0.00000  0.00000  0.00000  144 LYS   E CB  
12744 C CG  . LYS   I  144 ? 0.51597 0.51597 0.51597 0.00000  0.00000  0.00000  144 LYS   E CG  
12745 C CD  . LYS   I  144 ? 1.18034 1.18034 1.18034 -0.00000 0.00000  0.00000  144 LYS   E CD  
12746 C CE  . LYS   I  144 ? 1.40226 1.40226 1.40226 0.00000  0.00000  0.00000  144 LYS   E CE  
12747 N NZ  . LYS   I  144 ? 1.14109 1.14109 1.14109 0.00000  -0.00000 -0.00000 144 LYS   E NZ  
12748 N N   . LEU   I  145 ? 0.34937 0.34937 0.34937 0.00000  0.00000  0.00000  145 LEU   E N   
12749 C CA  . LEU   I  145 ? 0.27880 0.27880 0.27880 0.00000  0.00000  0.00000  145 LEU   E CA  
12750 C C   . LEU   I  145 ? 0.53415 0.53415 0.53415 0.00000  0.00000  0.00000  145 LEU   E C   
12751 O O   . LEU   I  145 ? 0.51169 0.51169 0.51169 -0.00000 0.00000  0.00000  145 LEU   E O   
12752 C CB  . LEU   I  145 ? 0.41604 0.41604 0.41604 0.00000  0.00000  0.00000  145 LEU   E CB  
12753 C CG  . LEU   I  145 ? 0.44962 0.44962 0.44962 0.00000  0.00000  0.00000  145 LEU   E CG  
12754 C CD1 . LEU   I  145 ? 0.36985 0.36985 0.36985 0.00000  0.00000  0.00000  145 LEU   E CD1 
12755 C CD2 . LEU   I  145 ? 0.36199 0.36199 0.36199 0.00000  0.00000  0.00000  145 LEU   E CD2 
12756 N N   . PHE   I  146 ? 0.31332 0.31332 0.31332 0.00000  0.00000  0.00000  146 PHE   E N   
12757 C CA  . PHE   I  146 ? 0.36340 0.36340 0.36340 -0.00000 0.00000  0.00000  146 PHE   E CA  
12758 C C   . PHE   I  146 ? 0.46775 0.46775 0.46775 0.00000  0.00000  0.00000  146 PHE   E C   
12759 O O   . PHE   I  146 ? 0.47674 0.47674 0.47674 -0.00000 -0.00000 0.00000  146 PHE   E O   
12760 C CB  . PHE   I  146 ? 0.36630 0.36630 0.36630 0.00000  0.00000  0.00000  146 PHE   E CB  
12761 C CG  . PHE   I  146 ? 0.41156 0.41156 0.41156 0.00000  0.00000  0.00000  146 PHE   E CG  
12762 C CD1 . PHE   I  146 ? 0.41211 0.41211 0.41211 -0.00000 0.00000  0.00000  146 PHE   E CD1 
12763 C CD2 . PHE   I  146 ? 0.32427 0.32427 0.32427 -0.00000 0.00000  0.00000  146 PHE   E CD2 
12764 C CE1 . PHE   I  146 ? 0.41357 0.41357 0.41357 0.00000  0.00000  0.00000  146 PHE   E CE1 
12765 C CE2 . PHE   I  146 ? 0.36965 0.36965 0.36965 -0.00000 0.00000  0.00000  146 PHE   E CE2 
12766 C CZ  . PHE   I  146 ? 0.44132 0.44132 0.44132 -0.00000 -0.00000 0.00000  146 PHE   E CZ  
12767 N N   . ASP   I  147 ? 0.51606 0.51606 0.51606 0.00000  0.00000  -0.00000 147 ASP   E N   
12768 C CA  . ASP   I  147 ? 0.43536 0.43536 0.43536 -0.00000 0.00000  0.00000  147 ASP   E CA  
12769 C C   . ASP   I  147 ? 0.55650 0.55650 0.55650 0.00000  0.00000  0.00000  147 ASP   E C   
12770 O O   . ASP   I  147 ? 0.53514 0.53514 0.53514 0.00000  0.00000  0.00000  147 ASP   E O   
12771 C CB  . ASP   I  147 ? 0.33969 0.33969 0.33969 -0.00000 -0.00000 0.00000  147 ASP   E CB  
12772 C CG  . ASP   I  147 ? 0.75863 0.75863 0.75863 0.00000  0.00000  0.00000  147 ASP   E CG  
12773 O OD1 . ASP   I  147 ? 0.65878 0.65878 0.65878 0.00000  0.00000  -0.00000 147 ASP   E OD1 
12774 O OD2 . ASP   I  147 ? 0.71172 0.71172 0.71172 0.00000  0.00000  0.00000  147 ASP   E OD2 
12775 N N   . THR   I  148 ? 0.45984 0.45984 0.45984 0.00000  0.00000  -0.00000 148 THR   E N   
12776 C CA  . THR   I  148 ? 0.57951 0.57951 0.57951 0.00000  -0.00000 -0.00000 148 THR   E CA  
12777 C C   . THR   I  148 ? 0.54032 0.54032 0.54032 -0.00000 0.00000  0.00000  148 THR   E C   
12778 O O   . THR   I  148 ? 0.61651 0.61651 0.61651 -0.00000 0.00000  0.00000  148 THR   E O   
12779 C CB  . THR   I  148 ? 0.51443 0.51443 0.51443 0.00000  0.00000  0.00000  148 THR   E CB  
12780 O OG1 . THR   I  148 ? 0.52541 0.52541 0.52541 0.00000  0.00000  0.00000  148 THR   E OG1 
12781 C CG2 . THR   I  148 ? 0.37895 0.37895 0.37895 0.00000  0.00000  0.00000  148 THR   E CG2 
12782 N N   . TRP   I  149 ? 0.44225 0.44225 0.44225 -0.00000 0.00000  0.00000  149 TRP   E N   
12783 C CA  . TRP   I  149 ? 0.35493 0.35493 0.35493 0.00000  0.00000  0.00000  149 TRP   E CA  
12784 C C   . TRP   I  149 ? 0.65923 0.65923 0.65923 0.00000  0.00000  0.00000  149 TRP   E C   
12785 O O   . TRP   I  149 ? 0.46696 0.46696 0.46696 0.00000  0.00000  0.00000  149 TRP   E O   
12786 C CB  . TRP   I  149 ? 0.32417 0.32417 0.32417 0.00000  0.00000  0.00000  149 TRP   E CB  
12787 C CG  . TRP   I  149 ? 0.46380 0.46380 0.46380 -0.00000 0.00000  0.00000  149 TRP   E CG  
12788 C CD1 . TRP   I  149 ? 0.39189 0.39189 0.39189 -0.00000 0.00000  0.00000  149 TRP   E CD1 
12789 C CD2 . TRP   I  149 ? 0.59474 0.59474 0.59474 0.00000  0.00000  0.00000  149 TRP   E CD2 
12790 N NE1 . TRP   I  149 ? 0.54655 0.54655 0.54655 -0.00000 0.00000  0.00000  149 TRP   E NE1 
12791 C CE2 . TRP   I  149 ? 0.37277 0.37277 0.37277 0.00000  0.00000  0.00000  149 TRP   E CE2 
12792 C CE3 . TRP   I  149 ? 0.36159 0.36159 0.36159 -0.00000 0.00000  0.00000  149 TRP   E CE3 
12793 C CZ2 . TRP   I  149 ? 0.49240 0.49240 0.49240 -0.00000 0.00000  0.00000  149 TRP   E CZ2 
12794 C CZ3 . TRP   I  149 ? 0.39784 0.39784 0.39784 0.00000  0.00000  0.00000  149 TRP   E CZ3 
12795 C CH2 . TRP   I  149 ? 0.48925 0.48925 0.48925 0.00000  0.00000  0.00000  149 TRP   E CH2 
12796 N N   . GLY   I  150 ? 0.41022 0.41022 0.41022 -0.00000 0.00000  0.00000  150 GLY   E N   
12797 C CA  . GLY   I  150 ? 0.27542 0.27542 0.27542 0.00000  0.00000  0.00000  150 GLY   E CA  
12798 C C   . GLY   I  150 ? 0.54509 0.54509 0.54509 -0.00000 0.00000  0.00000  150 GLY   E C   
12799 O O   . GLY   I  150 ? 0.69775 0.69775 0.69775 0.00000  0.00000  0.00000  150 GLY   E O   
12800 N N   . LEU   I  151 ? 0.37809 0.37809 0.37809 0.00000  0.00000  0.00000  151 LEU   E N   
12801 C CA  . LEU   I  151 ? 0.31120 0.31120 0.31120 0.00000  0.00000  0.00000  151 LEU   E CA  
12802 C C   . LEU   I  151 ? 0.81072 0.81072 0.81072 -0.00000 0.00000  0.00000  151 LEU   E C   
12803 O O   . LEU   I  151 ? 0.46949 0.46949 0.46949 -0.00000 0.00000  0.00000  151 LEU   E O   
12804 C CB  . LEU   I  151 ? 0.46565 0.46565 0.46565 -0.00000 0.00000  0.00000  151 LEU   E CB  
12805 C CG  . LEU   I  151 ? 0.73285 0.73285 0.73285 0.00000  0.00000  0.00000  151 LEU   E CG  
12806 C CD1 . LEU   I  151 ? 0.29176 0.29176 0.29176 0.00000  0.00000  0.00000  151 LEU   E CD1 
12807 C CD2 . LEU   I  151 ? 0.14640 0.14640 0.14640 0.00000  0.00000  0.00000  151 LEU   E CD2 
12808 N N   . PHE   I  152 ? 0.41206 0.41206 0.41206 0.00000  0.00000  0.00000  152 PHE   E N   
12809 C CA  . PHE   I  152 ? 0.57355 0.57355 0.57355 -0.00000 0.00000  0.00000  152 PHE   E CA  
12810 C C   . PHE   I  152 ? 0.74115 0.74115 0.74115 0.00000  0.00000  0.00000  152 PHE   E C   
12811 O O   . PHE   I  152 ? 0.64559 0.64559 0.64559 0.00000  0.00000  0.00000  152 PHE   E O   
12812 C CB  . PHE   I  152 ? 0.34891 0.34891 0.34891 0.00000  0.00000  0.00000  152 PHE   E CB  
12813 C CG  . PHE   I  152 ? 0.68147 0.68147 0.68147 -0.00000 0.00000  0.00000  152 PHE   E CG  
12814 C CD1 . PHE   I  152 ? 0.46554 0.46554 0.46554 0.00000  0.00000  0.00000  152 PHE   E CD1 
12815 C CD2 . PHE   I  152 ? 0.56518 0.56518 0.56518 -0.00000 0.00000  0.00000  152 PHE   E CD2 
12816 C CE1 . PHE   I  152 ? 0.55412 0.55412 0.55412 0.00000  0.00000  0.00000  152 PHE   E CE1 
12817 C CE2 . PHE   I  152 ? 0.68649 0.68649 0.68649 0.00000  0.00000  0.00000  152 PHE   E CE2 
12818 C CZ  . PHE   I  152 ? 0.58199 0.58199 0.58199 0.00000  0.00000  0.00000  152 PHE   E CZ  
12819 N N   . LEU   I  153 ? 0.51164 0.51164 0.51164 0.00000  0.00000  0.00000  153 LEU   E N   
12820 C CA  . LEU   I  153 ? 0.53580 0.53580 0.53580 0.00000  0.00000  0.00000  153 LEU   E CA  
12821 C C   . LEU   I  153 ? 0.53055 0.53055 0.53055 -0.00000 0.00000  0.00000  153 LEU   E C   
12822 O O   . LEU   I  153 ? 0.58621 0.58621 0.58621 0.00000  0.00000  0.00000  153 LEU   E O   
12823 C CB  . LEU   I  153 ? 0.44360 0.44360 0.44360 0.00000  -0.00000 0.00000  153 LEU   E CB  
12824 C CG  . LEU   I  153 ? 0.60911 0.60911 0.60911 0.00000  0.00000  0.00000  153 LEU   E CG  
12825 C CD1 . LEU   I  153 ? 0.38339 0.38339 0.38339 0.00000  0.00000  0.00000  153 LEU   E CD1 
12826 C CD2 . LEU   I  153 ? 0.38360 0.38360 0.38360 -0.00000 0.00000  0.00000  153 LEU   E CD2 
12827 N N   . SER   I  154 ? 0.43788 0.43788 0.43788 0.00000  0.00000  -0.00000 154 SER   E N   
12828 C CA  . SER   I  154 ? 0.40940 0.40940 0.40940 0.00000  0.00000  0.00000  154 SER   E CA  
12829 C C   . SER   I  154 ? 0.53709 0.53709 0.53709 -0.00000 0.00000  0.00000  154 SER   E C   
12830 O O   . SER   I  154 ? 0.59081 0.59081 0.59081 0.00000  0.00000  0.00000  154 SER   E O   
12831 C CB  . SER   I  154 ? 0.24724 0.24724 0.24724 -0.00000 0.00000  0.00000  154 SER   E CB  
12832 O OG  . SER   I  154 ? 1.26849 1.26849 1.26849 -0.00000 0.00000  0.00000  154 SER   E OG  
12833 N N   . SER   I  155 ? 0.46401 0.46401 0.46401 0.00000  0.00000  0.00000  155 SER   E N   
12834 C CA  . SER   I  155 ? 0.47191 0.47191 0.47191 0.00000  0.00000  0.00000  155 SER   E CA  
12835 C C   . SER   I  155 ? 1.29014 1.29014 1.29014 0.00000  0.00000  0.00000  155 SER   E C   
12836 O O   . SER   I  155 ? 0.44772 0.44772 0.44772 0.00000  0.00000  -0.00000 155 SER   E O   
12837 C CB  . SER   I  155 ? 0.43078 0.43078 0.43078 -0.00000 0.00000  0.00000  155 SER   E CB  
12838 O OG  . SER   I  155 ? 0.55806 0.55806 0.55806 0.00000  0.00000  0.00000  155 SER   E OG  
12839 N N   . LYS   I  156 ? 0.54636 0.54636 0.54636 0.00000  0.00000  0.00000  156 LYS   E N   
12840 C CA  . LYS   I  156 ? 0.75937 0.75937 0.75937 -0.00000 0.00000  0.00000  156 LYS   E CA  
12841 C C   . LYS   I  156 ? 0.42274 0.42274 0.42274 0.00000  0.00000  0.00000  156 LYS   E C   
12842 O O   . LYS   I  156 ? 0.62341 0.62341 0.62341 0.00000  0.00000  0.00000  156 LYS   E O   
12843 C CB  . LYS   I  156 ? 0.33048 0.33048 0.33048 -0.00000 -0.00000 0.00000  156 LYS   E CB  
12844 N N   . ASP   I  157 ? 0.67801 0.67801 0.67801 0.00000  0.00000  0.00000  157 ASP   E N   
12845 C CA  . ASP   I  157 ? 0.66499 0.66499 0.66499 -0.00000 0.00000  0.00000  157 ASP   E CA  
12846 C C   . ASP   I  157 ? 0.69690 0.69690 0.69690 0.00000  0.00000  0.00000  157 ASP   E C   
12847 O O   . ASP   I  157 ? 0.64479 0.64479 0.64479 -0.00000 0.00000  0.00000  157 ASP   E O   
12848 C CB  . ASP   I  157 ? 0.80876 0.80876 0.80876 -0.00000 0.00000  0.00000  157 ASP   E CB  
12849 C CG  . ASP   I  157 ? 0.82191 0.82191 0.82191 0.00000  0.00000  0.00000  157 ASP   E CG  
12850 O OD1 . ASP   I  157 ? 0.95617 0.95617 0.95617 0.00000  0.00000  0.00000  157 ASP   E OD1 
12851 O OD2 . ASP   I  157 ? 1.19305 1.19305 1.19305 0.00000  0.00000  0.00000  157 ASP   E OD2 
12852 N N   . SER   I  158 ? 0.76188 0.76188 0.76188 0.00000  0.00000  0.00000  158 SER   E N   
12853 C CA  . SER   I  158 ? 0.57734 0.57734 0.57734 -0.00000 0.00000  0.00000  158 SER   E CA  
12854 C C   . SER   I  158 ? 0.61337 0.61337 0.61337 0.00000  0.00000  0.00000  158 SER   E C   
12855 O O   . SER   I  158 ? 0.55079 0.55079 0.55079 -0.00000 0.00000  0.00000  158 SER   E O   
12856 C CB  . SER   I  158 ? 0.49448 0.49448 0.49448 0.00000  0.00000  0.00000  158 SER   E CB  
12857 O OG  . SER   I  158 ? 0.48762 0.48762 0.48762 0.00000  0.00000  0.00000  158 SER   E OG  
12858 N N   . ARG   I  159 ? 0.51267 0.51267 0.51267 0.00000  0.00000  0.00000  159 ARG   E N   
12859 C CA  . ARG   I  159 ? 0.60406 0.60406 0.60406 0.00000  -0.00000 0.00000  159 ARG   E CA  
12860 C C   . ARG   I  159 ? 0.61364 0.61364 0.61364 0.00000  0.00000  0.00000  159 ARG   E C   
12861 O O   . ARG   I  159 ? 0.54295 0.54295 0.54295 -0.00000 0.00000  0.00000  159 ARG   E O   
12862 C CB  . ARG   I  159 ? 0.38410 0.38410 0.38410 0.00000  0.00000  0.00000  159 ARG   E CB  
12863 C CG  . ARG   I  159 ? 0.83966 0.83966 0.83966 -0.00000 0.00000  0.00000  159 ARG   E CG  
12864 C CD  . ARG   I  159 ? 0.63808 0.63808 0.63808 -0.00000 0.00000  0.00000  159 ARG   E CD  
12865 N NE  . ARG   I  159 ? 0.81365 0.81365 0.81365 0.00000  0.00000  0.00000  159 ARG   E NE  
12866 C CZ  . ARG   I  159 ? 0.70178 0.70178 0.70178 -0.00000 0.00000  0.00000  159 ARG   E CZ  
12867 N NH1 . ARG   I  159 ? 0.60644 0.60644 0.60644 0.00000  0.00000  0.00000  159 ARG   E NH1 
12868 N NH2 . ARG   I  159 ? 0.57123 0.57123 0.57123 0.00000  0.00000  0.00000  159 ARG   E NH2 
12869 N N   . ASN   I  160 ? 0.53469 0.53469 0.53469 -0.00000 0.00000  0.00000  160 ASN   E N   
12870 C CA  . ASN   I  160 ? 0.58973 0.58973 0.58973 0.00000  0.00000  0.00000  160 ASN   E CA  
12871 C C   . ASN   I  160 ? 0.49382 0.49382 0.49382 0.00000  0.00000  0.00000  160 ASN   E C   
12872 O O   . ASN   I  160 ? 0.87089 0.87089 0.87089 0.00000  0.00000  0.00000  160 ASN   E O   
12873 C CB  . ASN   I  160 ? 0.56502 0.56502 0.56502 0.00000  0.00000  0.00000  160 ASN   E CB  
12874 C CG  . ASN   I  160 ? 0.71922 0.71922 0.71922 -0.00000 0.00000  0.00000  160 ASN   E CG  
12875 O OD1 . ASN   I  160 ? 0.88964 0.88964 0.88964 -0.00000 0.00000  -0.00000 160 ASN   E OD1 
12876 N ND2 . ASN   I  160 ? 0.77233 0.77233 0.77233 0.00000  0.00000  0.00000  160 ASN   E ND2 
12877 N N   . VAL   I  161 ? 0.64959 0.64959 0.64959 0.00000  0.00000  0.00000  161 VAL   E N   
12878 C CA  . VAL   I  161 ? 0.68511 0.68511 0.68511 0.00000  -0.00000 0.00000  161 VAL   E CA  
12879 C C   . VAL   I  161 ? 0.71931 0.71931 0.71931 0.00000  0.00000  0.00000  161 VAL   E C   
12880 O O   . VAL   I  161 ? 0.50025 0.50025 0.50025 0.00000  0.00000  0.00000  161 VAL   E O   
12881 C CB  . VAL   I  161 ? 0.60845 0.60845 0.60845 0.00000  0.00000  0.00000  161 VAL   E CB  
12882 C CG1 . VAL   I  161 ? 0.46742 0.46742 0.46742 0.00000  0.00000  0.00000  161 VAL   E CG1 
12883 C CG2 . VAL   I  161 ? 0.40273 0.40273 0.40273 0.00000  0.00000  0.00000  161 VAL   E CG2 
12884 N N   . LEU   I  162 ? 0.46438 0.46438 0.46438 0.00000  0.00000  0.00000  162 LEU   E N   
12885 C CA  . LEU   I  162 ? 0.59668 0.59668 0.59668 0.00000  0.00000  0.00000  162 LEU   E CA  
12886 C C   . LEU   I  162 ? 0.83643 0.83643 0.83643 -0.00000 0.00000  0.00000  162 LEU   E C   
12887 O O   . LEU   I  162 ? 0.61601 0.61601 0.61601 0.00000  -0.00000 0.00000  162 LEU   E O   
12888 C CB  . LEU   I  162 ? 0.55434 0.55434 0.55434 -0.00000 0.00000  0.00000  162 LEU   E CB  
12889 C CG  . LEU   I  162 ? 0.41045 0.41045 0.41045 -0.00000 0.00000  0.00000  162 LEU   E CG  
12890 C CD1 . LEU   I  162 ? 0.35591 0.35591 0.35591 0.00000  0.00000  0.00000  162 LEU   E CD1 
12891 C CD2 . LEU   I  162 ? 0.34126 0.34126 0.34126 0.00000  -0.00000 0.00000  162 LEU   E CD2 
12892 N N   . VAL   I  163 ? 0.58930 0.58930 0.58930 -0.00000 0.00000  0.00000  163 VAL   E N   
12893 C CA  . VAL   I  163 ? 0.55187 0.55187 0.55187 0.00000  0.00000  0.00000  163 VAL   E CA  
12894 C C   . VAL   I  163 ? 0.81056 0.81056 0.81056 -0.00000 -0.00000 0.00000  163 VAL   E C   
12895 O O   . VAL   I  163 ? 0.71662 0.71662 0.71662 -0.00000 0.00000  0.00000  163 VAL   E O   
12896 C CB  . VAL   I  163 ? 0.57670 0.57670 0.57670 0.00000  0.00000  0.00000  163 VAL   E CB  
12897 C CG1 . VAL   I  163 ? 0.49545 0.49545 0.49545 0.00000  0.00000  0.00000  163 VAL   E CG1 
12898 C CG2 . VAL   I  163 ? 0.48948 0.48948 0.48948 0.00000  0.00000  0.00000  163 VAL   E CG2 
12899 N N   . ALA   I  164 ? 0.65846 0.65846 0.65846 0.00000  -0.00000 0.00000  164 ALA   E N   
12900 C CA  . ALA   I  164 ? 0.75479 0.75479 0.75479 0.00000  0.00000  0.00000  164 ALA   E CA  
12901 C C   . ALA   I  164 ? 0.64081 0.64081 0.64081 0.00000  0.00000  0.00000  164 ALA   E C   
12902 O O   . ALA   I  164 ? 0.61440 0.61440 0.61440 0.00000  0.00000  0.00000  164 ALA   E O   
12903 C CB  . ALA   I  164 ? 0.38568 0.38568 0.38568 -0.00000 -0.00000 0.00000  164 ALA   E CB  
12904 N N   . ASP   I  165 ? 0.58930 0.58930 0.58930 0.00000  0.00000  0.00000  165 ASP   E N   
12905 C CA  . ASP   I  165 ? 0.56820 0.56820 0.56820 0.00000  0.00000  0.00000  165 ASP   E CA  
12906 C C   . ASP   I  165 ? 0.56644 0.56644 0.56644 0.00000  0.00000  0.00000  165 ASP   E C   
12907 O O   . ASP   I  165 ? 1.00999 1.00999 1.00999 0.00000  0.00000  0.00000  165 ASP   E O   
12908 C CB  . ASP   I  165 ? 0.66035 0.66035 0.66035 0.00000  0.00000  0.00000  165 ASP   E CB  
12909 C CG  . ASP   I  165 ? 0.50778 0.50778 0.50778 0.00000  0.00000  0.00000  165 ASP   E CG  
12910 O OD1 . ASP   I  165 ? 1.09355 1.09355 1.09355 -0.00000 0.00000  0.00000  165 ASP   E OD1 
12911 O OD2 . ASP   I  165 ? 1.12772 1.12772 1.12772 0.00000  0.00000  0.00000  165 ASP   E OD2 
12912 N N   . GLN   I  166 ? 0.86827 0.86827 0.86827 0.00000  0.00000  0.00000  166 GLN   E N   
12913 C CA  . GLN   I  166 ? 1.05151 1.05151 1.05151 -0.00000 0.00000  0.00000  166 GLN   E CA  
12914 C C   . GLN   I  166 ? 0.57352 0.57352 0.57352 0.00000  0.00000  0.00000  166 GLN   E C   
12915 O O   . GLN   I  166 ? 1.50569 1.50569 1.50569 0.00000  0.00000  0.00000  166 GLN   E O   
12916 C CB  . GLN   I  166 ? 0.53966 0.53966 0.53966 -0.00000 0.00000  0.00000  166 GLN   E CB  
12917 C CG  . GLN   I  166 ? 1.00214 1.00214 1.00214 -0.00000 0.00000  0.00000  166 GLN   E CG  
12918 C CD  . GLN   I  166 ? 1.75469 1.75469 1.75469 0.00000  0.00000  0.00000  166 GLN   E CD  
12919 O OE1 . GLN   I  166 ? 1.18179 1.18179 1.18179 -0.00000 0.00000  0.00000  166 GLN   E OE1 
12920 N NE2 . GLN   I  166 ? 1.00959 1.00959 1.00959 0.00000  0.00000  0.00000  166 GLN   E NE2 
12921 N N   . PHE   I  167 ? 0.89549 0.89549 0.89549 0.00000  0.00000  0.00000  167 PHE   E N   
12922 C CA  . PHE   I  167 ? 0.88229 0.88229 0.88229 0.00000  0.00000  0.00000  167 PHE   E CA  
12923 C C   . PHE   I  167 ? 0.90134 0.90134 0.90134 -0.00000 0.00000  0.00000  167 PHE   E C   
12924 O O   . PHE   I  167 ? 0.85042 0.85042 0.85042 0.00000  0.00000  0.00000  167 PHE   E O   
12925 C CB  . PHE   I  167 ? 0.75693 0.75693 0.75693 0.00000  0.00000  0.00000  167 PHE   E CB  
12926 C CG  . PHE   I  167 ? 0.82653 0.82653 0.82653 0.00000  0.00000  0.00000  167 PHE   E CG  
12927 C CD1 . PHE   I  167 ? 0.67727 0.67727 0.67727 0.00000  0.00000  0.00000  167 PHE   E CD1 
12928 C CD2 . PHE   I  167 ? 0.56465 0.56465 0.56465 -0.00000 0.00000  0.00000  167 PHE   E CD2 
12929 C CE1 . PHE   I  167 ? 1.57299 1.57299 1.57299 0.00000  0.00000  0.00000  167 PHE   E CE1 
12930 C CE2 . PHE   I  167 ? 1.43141 1.43141 1.43141 0.00000  0.00000  0.00000  167 PHE   E CE2 
12931 C CZ  . PHE   I  167 ? 0.40909 0.40909 0.40909 -0.00000 0.00000  0.00000  167 PHE   E CZ  
12932 N N   . ASP   I  168 ? 1.18800 1.18800 1.18800 0.00000  0.00000  0.00000  168 ASP   E N   
12933 C CA  . ASP   I  168 ? 0.74819 0.74819 0.74819 0.00000  0.00000  0.00000  168 ASP   E CA  
12934 C C   . ASP   I  168 ? 1.39804 1.39804 1.39804 -0.00000 0.00000  0.00000  168 ASP   E C   
12935 O O   . ASP   I  168 ? 1.06273 1.06273 1.06273 0.00000  0.00000  0.00000  168 ASP   E O   
12936 C CB  . ASP   I  168 ? 0.92651 0.92651 0.92651 0.00000  0.00000  0.00000  168 ASP   E CB  
12937 C CG  . ASP   I  168 ? 1.24044 1.24044 1.24044 -0.00000 0.00000  0.00000  168 ASP   E CG  
12938 O OD1 . ASP   I  168 ? 1.06099 1.06099 1.06099 0.00000  0.00000  0.00000  168 ASP   E OD1 
12939 O OD2 . ASP   I  168 ? 1.21202 1.21202 1.21202 -0.00000 0.00000  0.00000  168 ASP   E OD2 
12940 N N   . ASP   I  169 ? 0.96695 0.96695 0.96695 -0.00000 0.00000  0.00000  169 ASP   E N   
12941 C CA  . ASP   I  169 ? 1.01624 1.01624 1.01624 0.00000  0.00000  0.00000  169 ASP   E CA  
12942 C C   . ASP   I  169 ? 1.22962 1.22962 1.22962 -0.00000 0.00000  0.00000  169 ASP   E C   
12943 O O   . ASP   I  169 ? 1.07547 1.07547 1.07547 0.00000  0.00000  0.00000  169 ASP   E O   
12944 C CB  . ASP   I  169 ? 0.74499 0.74499 0.74499 0.00000  0.00000  0.00000  169 ASP   E CB  
12945 N N   . ARG   I  170 ? 1.74112 1.74112 1.74112 0.00000  0.00000  -0.00000 170 ARG   E N   
12946 C CA  . ARG   I  170 ? 0.61266 0.61266 0.61266 -0.00000 0.00000  0.00000  170 ARG   E CA  
12947 C C   . ARG   I  170 ? 0.84422 0.84422 0.84422 0.00000  0.00000  0.00000  170 ARG   E C   
12948 O O   . ARG   I  170 ? 0.73045 0.73045 0.73045 0.00000  0.00000  0.00000  170 ARG   E O   
12949 C CB  . ARG   I  170 ? 0.68679 0.68679 0.68679 0.00000  0.00000  0.00000  170 ARG   E CB  
12950 N N   . HIS   I  171 ? 0.82051 0.82051 0.82051 -0.00000 0.00000  0.00000  171 HIS   E N   
12951 C CA  . HIS   I  171 ? 0.86143 0.86143 0.86143 -0.00000 0.00000  0.00000  171 HIS   E CA  
12952 C C   . HIS   I  171 ? 0.43781 0.43781 0.43781 0.00000  0.00000  0.00000  171 HIS   E C   
12953 O O   . HIS   I  171 ? 1.34056 1.34056 1.34056 0.00000  0.00000  -0.00000 171 HIS   E O   
12954 C CB  . HIS   I  171 ? 0.89650 0.89650 0.89650 0.00000  0.00000  0.00000  171 HIS   E CB  
12955 C CG  . HIS   I  171 ? 0.83550 0.83550 0.83550 -0.00000 0.00000  0.00000  171 HIS   E CG  
12956 N ND1 . HIS   I  171 ? 0.90723 0.90723 0.90723 0.00000  0.00000  -0.00000 171 HIS   E ND1 
12957 C CD2 . HIS   I  171 ? 0.83838 0.83838 0.83838 0.00000  0.00000  -0.00000 171 HIS   E CD2 
12958 C CE1 . HIS   I  171 ? 0.58748 0.58748 0.58748 -0.00000 0.00000  0.00000  171 HIS   E CE1 
12959 N NE2 . HIS   I  171 ? 1.54070 1.54070 1.54070 0.00000  0.00000  0.00000  171 HIS   E NE2 
12960 N N   . CYS   I  172 ? 0.85272 0.85272 0.85272 -0.00000 0.00000  0.00000  172 CYS   E N   
12961 C CA  . CYS   I  172 ? 0.46423 0.46423 0.46423 0.00000  0.00000  0.00000  172 CYS   E CA  
12962 C C   . CYS   I  172 ? 0.47763 0.47763 0.47763 -0.00000 0.00000  0.00000  172 CYS   E C   
12963 O O   . CYS   I  172 ? 0.76804 0.76804 0.76804 0.00000  0.00000  0.00000  172 CYS   E O   
12964 C CB  . CYS   I  172 ? 0.57968 0.57968 0.57968 0.00000  0.00000  0.00000  172 CYS   E CB  
12965 S SG  . CYS   I  172 ? 0.68067 0.68067 0.68067 0.00000  0.00000  0.00000  172 CYS   E SG  
12966 N N   . GLY   I  173 ? 0.63371 0.63371 0.63371 0.00000  0.00000  0.00000  173 GLY   E N   
12967 C CA  . GLY   I  173 ? 0.43933 0.43933 0.43933 -0.00000 0.00000  0.00000  173 GLY   E CA  
12968 C C   . GLY   I  173 ? 0.62384 0.62384 0.62384 0.00000  0.00000  0.00000  173 GLY   E C   
12969 O O   . GLY   I  173 ? 0.62454 0.62454 0.62454 0.00000  0.00000  0.00000  173 GLY   E O   
12970 N N   . TRP   I  174 ? 0.33319 0.33319 0.33319 -0.00000 0.00000  0.00000  174 TRP   E N   
12971 C CA  . TRP   I  174 ? 0.65714 0.65714 0.65714 0.00000  0.00000  0.00000  174 TRP   E CA  
12972 C C   . TRP   I  174 ? 0.76584 0.76584 0.76584 0.00000  0.00000  0.00000  174 TRP   E C   
12973 O O   . TRP   I  174 ? 0.56549 0.56549 0.56549 0.00000  0.00000  0.00000  174 TRP   E O   
12974 C CB  . TRP   I  174 ? 0.37539 0.37539 0.37539 0.00000  0.00000  0.00000  174 TRP   E CB  
12975 C CG  . TRP   I  174 ? 0.75598 0.75598 0.75598 0.00000  0.00000  0.00000  174 TRP   E CG  
12976 C CD1 . TRP   I  174 ? 0.47673 0.47673 0.47673 0.00000  0.00000  0.00000  174 TRP   E CD1 
12977 C CD2 . TRP   I  174 ? 0.58707 0.58707 0.58707 -0.00000 0.00000  0.00000  174 TRP   E CD2 
12978 N NE1 . TRP   I  174 ? 0.50815 0.50815 0.50815 0.00000  0.00000  0.00000  174 TRP   E NE1 
12979 C CE2 . TRP   I  174 ? 0.40758 0.40758 0.40758 0.00000  0.00000  0.00000  174 TRP   E CE2 
12980 C CE3 . TRP   I  174 ? 0.43567 0.43567 0.43567 0.00000  0.00000  0.00000  174 TRP   E CE3 
12981 C CZ2 . TRP   I  174 ? 0.31147 0.31147 0.31147 0.00000  0.00000  0.00000  174 TRP   E CZ2 
12982 C CZ3 . TRP   I  174 ? 0.46144 0.46144 0.46144 0.00000  0.00000  0.00000  174 TRP   E CZ3 
12983 C CH2 . TRP   I  174 ? 0.34939 0.34939 0.34939 0.00000  0.00000  0.00000  174 TRP   E CH2 
12984 N N   . LEU   I  175 ? 0.62358 0.62358 0.62358 0.00000  0.00000  0.00000  175 LEU   E N   
12985 C CA  . LEU   I  175 ? 0.55966 0.55966 0.55966 -0.00000 0.00000  0.00000  175 LEU   E CA  
12986 C C   . LEU   I  175 ? 0.68248 0.68248 0.68248 0.00000  0.00000  0.00000  175 LEU   E C   
12987 O O   . LEU   I  175 ? 0.79455 0.79455 0.79455 0.00000  0.00000  0.00000  175 LEU   E O   
12988 C CB  . LEU   I  175 ? 0.49630 0.49630 0.49630 0.00000  0.00000  0.00000  175 LEU   E CB  
12989 C CG  . LEU   I  175 ? 0.63069 0.63069 0.63069 0.00000  0.00000  0.00000  175 LEU   E CG  
12990 C CD1 . LEU   I  175 ? 0.51096 0.51096 0.51096 0.00000  0.00000  0.00000  175 LEU   E CD1 
12991 C CD2 . LEU   I  175 ? 0.47227 0.47227 0.47227 -0.00000 0.00000  0.00000  175 LEU   E CD2 
12992 N N   . ASN   I  176 ? 0.54929 0.54929 0.54929 0.00000  0.00000  0.00000  176 ASN   E N   
12993 C CA  . ASN   I  176 ? 0.49343 0.49343 0.49343 -0.00000 0.00000  0.00000  176 ASN   E CA  
12994 C C   . ASN   I  176 ? 0.70126 0.70126 0.70126 -0.00000 0.00000  0.00000  176 ASN   E C   
12995 O O   . ASN   I  176 ? 0.87711 0.87711 0.87711 0.00000  0.00000  0.00000  176 ASN   E O   
12996 C CB  . ASN   I  176 ? 0.83441 0.83441 0.83441 0.00000  0.00000  0.00000  176 ASN   E CB  
12997 C CG  . ASN   I  176 ? 0.81302 0.81302 0.81302 0.00000  0.00000  0.00000  176 ASN   E CG  
12998 O OD1 . ASN   I  176 ? 0.63808 0.63808 0.63808 0.00000  0.00000  0.00000  176 ASN   E OD1 
12999 N ND2 . ASN   I  176 ? 0.65507 0.65507 0.65507 -0.00000 0.00000  0.00000  176 ASN   E ND2 
13000 N N   . GLU   I  177 ? 0.60766 0.60766 0.60766 0.00000  0.00000  0.00000  177 GLU   E N   
13001 C CA  . GLU   I  177 ? 0.57345 0.57345 0.57345 0.00000  0.00000  0.00000  177 GLU   E CA  
13002 C C   . GLU   I  177 ? 0.49455 0.49455 0.49455 0.00000  0.00000  0.00000  177 GLU   E C   
13003 O O   . GLU   I  177 ? 0.61167 0.61167 0.61167 0.00000  0.00000  0.00000  177 GLU   E O   
13004 C CB  . GLU   I  177 ? 0.34234 0.34234 0.34234 0.00000  0.00000  0.00000  177 GLU   E CB  
13005 C CG  . GLU   I  177 ? 0.65550 0.65550 0.65550 -0.00000 0.00000  0.00000  177 GLU   E CG  
13006 C CD  . GLU   I  177 ? 1.19258 1.19258 1.19258 0.00000  0.00000  0.00000  177 GLU   E CD  
13007 O OE1 . GLU   I  177 ? 1.21971 1.21971 1.21971 0.00000  0.00000  0.00000  177 GLU   E OE1 
13008 O OE2 . GLU   I  177 ? 0.38850 0.38850 0.38850 0.00000  0.00000  0.00000  177 GLU   E OE2 
13009 N N   . ARG   I  178 ? 0.47005 0.47005 0.47005 0.00000  0.00000  0.00000  178 ARG   E N   
13010 C CA  . ARG   I  178 ? 0.76847 0.76847 0.76847 0.00000  0.00000  0.00000  178 ARG   E CA  
13011 C C   . ARG   I  178 ? 0.72004 0.72004 0.72004 -0.00000 0.00000  0.00000  178 ARG   E C   
13012 O O   . ARG   I  178 ? 0.70053 0.70053 0.70053 0.00000  0.00000  0.00000  178 ARG   E O   
13013 C CB  . ARG   I  178 ? 0.32752 0.32752 0.32752 -0.00000 0.00000  0.00000  178 ARG   E CB  
13014 N N   . ALA   I  179 ? 0.61859 0.61859 0.61859 0.00000  0.00000  0.00000  179 ALA   E N   
13015 C CA  . ALA   I  179 ? 0.60169 0.60169 0.60169 0.00000  0.00000  0.00000  179 ALA   E CA  
13016 C C   . ALA   I  179 ? 0.46002 0.46002 0.46002 -0.00000 0.00000  0.00000  179 ALA   E C   
13017 O O   . ALA   I  179 ? 0.55685 0.55685 0.55685 0.00000  0.00000  0.00000  179 ALA   E O   
13018 C CB  . ALA   I  179 ? 0.29569 0.29569 0.29569 0.00000  0.00000  0.00000  179 ALA   E CB  
13019 N N   . LEU   I  180 ? 0.54817 0.54817 0.54817 0.00000  0.00000  0.00000  180 LEU   E N   
13020 C CA  . LEU   I  180 ? 0.38296 0.38296 0.38296 0.00000  0.00000  0.00000  180 LEU   E CA  
13021 C C   . LEU   I  180 ? 0.59039 0.59039 0.59039 0.00000  0.00000  0.00000  180 LEU   E C   
13022 O O   . LEU   I  180 ? 0.59192 0.59192 0.59192 0.00000  0.00000  0.00000  180 LEU   E O   
13023 C CB  . LEU   I  180 ? 0.32387 0.32387 0.32387 -0.00000 0.00000  0.00000  180 LEU   E CB  
13024 C CG  . LEU   I  180 ? 0.63818 0.63818 0.63818 0.00000  0.00000  0.00000  180 LEU   E CG  
13025 C CD1 . LEU   I  180 ? 0.60818 0.60818 0.60818 -0.00000 0.00000  0.00000  180 LEU   E CD1 
13026 C CD2 . LEU   I  180 ? 0.48208 0.48208 0.48208 -0.00000 0.00000  0.00000  180 LEU   E CD2 
13027 N N   . SER   I  181 ? 0.59456 0.59456 0.59456 0.00000  0.00000  0.00000  181 SER   E N   
13028 C CA  . SER   I  181 ? 0.64410 0.64410 0.64410 -0.00000 0.00000  0.00000  181 SER   E CA  
13029 C C   . SER   I  181 ? 0.48831 0.48831 0.48831 0.00000  -0.00000 0.00000  181 SER   E C   
13030 O O   . SER   I  181 ? 0.63159 0.63159 0.63159 -0.00000 0.00000  0.00000  181 SER   E O   
13031 C CB  . SER   I  181 ? 0.42094 0.42094 0.42094 0.00000  -0.00000 -0.00000 181 SER   E CB  
13032 O OG  . SER   I  181 ? 1.28496 1.28496 1.28496 0.00000  0.00000  0.00000  181 SER   E OG  
13033 N N   . ALA   I  182 ? 0.56299 0.56299 0.56299 0.00000  0.00000  0.00000  182 ALA   E N   
13034 C CA  . ALA   I  182 ? 0.83743 0.83743 0.83743 -0.00000 0.00000  0.00000  182 ALA   E CA  
13035 C C   . ALA   I  182 ? 0.57792 0.57792 0.57792 0.00000  0.00000  0.00000  182 ALA   E C   
13036 O O   . ALA   I  182 ? 0.42374 0.42374 0.42374 -0.00000 0.00000  0.00000  182 ALA   E O   
13037 C CB  . ALA   I  182 ? 0.31214 0.31214 0.31214 0.00000  0.00000  0.00000  182 ALA   E CB  
13038 N N   . MET   I  183 ? 0.37441 0.37441 0.37441 0.00000  0.00000  0.00000  183 MET   E N   
13039 C CA  . MET   I  183 ? 0.57865 0.57865 0.57865 0.00000  0.00000  0.00000  183 MET   E CA  
13040 C C   . MET   I  183 ? 0.39299 0.39299 0.39299 0.00000  0.00000  0.00000  183 MET   E C   
13041 O O   . MET   I  183 ? 0.62849 0.62849 0.62849 0.00000  0.00000  0.00000  183 MET   E O   
13042 C CB  . MET   I  183 ? 0.38437 0.38437 0.38437 0.00000  0.00000  0.00000  183 MET   E CB  
13043 C CG  . MET   I  183 ? 0.41098 0.41098 0.41098 0.00000  0.00000  0.00000  183 MET   E CG  
13044 S SD  . MET   I  183 ? 0.52764 0.52764 0.52764 0.00000  0.00000  0.00000  183 MET   E SD  
13045 C CE  . MET   I  183 ? 0.48019 0.48019 0.48019 0.00000  0.00000  0.00000  183 MET   E CE  
13046 N N   . VAL   I  184 ? 0.59122 0.59122 0.59122 0.00000  0.00000  0.00000  184 VAL   E N   
13047 C CA  . VAL   I  184 ? 0.67808 0.67808 0.67808 -0.00000 0.00000  0.00000  184 VAL   E CA  
13048 C C   . VAL   I  184 ? 0.44433 0.44433 0.44433 0.00000  0.00000  0.00000  184 VAL   E C   
13049 O O   . VAL   I  184 ? 0.58267 0.58267 0.58267 0.00000  -0.00000 0.00000  184 VAL   E O   
13050 C CB  . VAL   I  184 ? 0.41734 0.41734 0.41734 0.00000  0.00000  0.00000  184 VAL   E CB  
13051 C CG1 . VAL   I  184 ? 0.48714 0.48714 0.48714 -0.00000 0.00000  0.00000  184 VAL   E CG1 
13052 C CG2 . VAL   I  184 ? 0.43140 0.43140 0.43140 0.00000  0.00000  0.00000  184 VAL   E CG2 
13053 N N   . LYS   I  185 ? 0.49899 0.49899 0.49899 0.00000  0.00000  0.00000  185 LYS   E N   
13054 C CA  . LYS   I  185 ? 0.53541 0.53541 0.53541 0.00000  0.00000  0.00000  185 LYS   E CA  
13055 C C   . LYS   I  185 ? 0.22791 0.22791 0.22791 -0.00000 0.00000  0.00000  185 LYS   E C   
13056 O O   . LYS   I  185 ? 0.96791 0.96791 0.96791 -0.00000 0.00000  0.00000  185 LYS   E O   
13057 C CB  . LYS   I  185 ? 0.39127 0.39127 0.39127 0.00000  0.00000  0.00000  185 LYS   E CB  
13058 C CG  . LYS   I  185 ? 0.46984 0.46984 0.46984 0.00000  0.00000  0.00000  185 LYS   E CG  
13059 C CD  . LYS   I  185 ? 0.79200 0.79200 0.79200 0.00000  0.00000  0.00000  185 LYS   E CD  
13060 C CE  . LYS   I  185 ? 0.80017 0.80017 0.80017 0.00000  0.00000  0.00000  185 LYS   E CE  
13061 N NZ  . LYS   I  185 ? 0.97400 0.97400 0.97400 0.00000  0.00000  0.00000  185 LYS   E NZ  
13062 N N   . HIS   I  186 ? 0.55338 0.55338 0.55338 -0.00000 0.00000  0.00000  186 HIS   E N   
13063 C CA  . HIS   I  186 ? 0.32654 0.32654 0.32654 0.00000  0.00000  -0.00000 186 HIS   E CA  
13064 C C   . HIS   I  186 ? 0.57020 0.57020 0.57020 0.00000  0.00000  0.00000  186 HIS   E C   
13065 O O   . HIS   I  186 ? 0.39483 0.39483 0.39483 0.00000  0.00000  0.00000  186 HIS   E O   
13066 C CB  . HIS   I  186 ? 0.43351 0.43351 0.43351 0.00000  0.00000  0.00000  186 HIS   E CB  
13067 C CG  . HIS   I  186 ? 0.76336 0.76336 0.76336 0.00000  0.00000  0.00000  186 HIS   E CG  
13068 N ND1 . HIS   I  186 ? 0.59843 0.59843 0.59843 0.00000  0.00000  -0.00000 186 HIS   E ND1 
13069 C CD2 . HIS   I  186 ? 0.25217 0.25217 0.25217 0.00000  0.00000  0.00000  186 HIS   E CD2 
13070 C CE1 . HIS   I  186 ? 0.44365 0.44365 0.44365 -0.00000 0.00000  0.00000  186 HIS   E CE1 
13071 N NE2 . HIS   I  186 ? 0.64700 0.64700 0.64700 0.00000  0.00000  0.00000  186 HIS   E NE2 
13072 N N   . TYR   I  187 ? 0.42638 0.42638 0.42638 0.00000  0.00000  0.00000  187 TYR   E N   
13073 C CA  . TYR   I  187 ? 0.52718 0.52718 0.52718 -0.00000 0.00000  0.00000  187 TYR   E CA  
13074 C C   . TYR   I  187 ? 0.98170 0.98170 0.98170 0.00000  0.00000  0.00000  187 TYR   E C   
13075 O O   . TYR   I  187 ? 0.44408 0.44408 0.44408 0.00000  0.00000  0.00000  187 TYR   E O   
13076 C CB  . TYR   I  187 ? 0.58431 0.58431 0.58431 -0.00000 0.00000  0.00000  187 TYR   E CB  
13077 C CG  . TYR   I  187 ? 0.38176 0.38176 0.38176 0.00000  -0.00000 0.00000  187 TYR   E CG  
13078 C CD1 . TYR   I  187 ? 0.48846 0.48846 0.48846 0.00000  0.00000  0.00000  187 TYR   E CD1 
13079 C CD2 . TYR   I  187 ? 0.56828 0.56828 0.56828 -0.00000 0.00000  0.00000  187 TYR   E CD2 
13080 C CE1 . TYR   I  187 ? 0.43670 0.43670 0.43670 0.00000  0.00000  0.00000  187 TYR   E CE1 
13081 C CE2 . TYR   I  187 ? 0.21564 0.21564 0.21564 0.00000  0.00000  0.00000  187 TYR   E CE2 
13082 C CZ  . TYR   I  187 ? 0.56241 0.56241 0.56241 -0.00000 -0.00000 0.00000  187 TYR   E CZ  
13083 O OH  . TYR   I  187 ? 0.47872 0.47872 0.47872 0.00000  0.00000  0.00000  187 TYR   E OH  
13084 N N   . ASN   I  188 ? 0.50138 0.50138 0.50138 -0.00000 0.00000  0.00000  188 ASN   E N   
13085 C CA  . ASN   I  188 ? 1.13095 1.13095 1.13095 -0.00000 0.00000  0.00000  188 ASN   E CA  
13086 C C   . ASN   I  188 ? 0.48832 0.48832 0.48832 0.00000  0.00000  0.00000  188 ASN   E C   
13087 O O   . ASN   I  188 ? 0.91239 0.91239 0.91239 0.00000  0.00000  0.00000  188 ASN   E O   
13088 C CB  . ASN   I  188 ? 0.63373 0.63373 0.63373 0.00000  0.00000  0.00000  188 ASN   E CB  
13089 C CG  . ASN   I  188 ? 1.13156 1.13156 1.13156 0.00000  0.00000  0.00000  188 ASN   E CG  
13090 O OD1 . ASN   I  188 ? 1.48428 1.48428 1.48428 -0.00000 0.00000  0.00000  188 ASN   E OD1 
13091 N ND2 . ASN   I  188 ? 1.29419 1.29419 1.29419 0.00000  0.00000  0.00000  188 ASN   E ND2 
13092 N N   . GLY   I  189 ? 0.88335 0.88335 0.88335 -0.00000 0.00000  0.00000  189 GLY   E N   
13093 C CA  . GLY   I  189 ? 0.46435 0.46435 0.46435 0.00000  0.00000  0.00000  189 GLY   E CA  
13094 C C   . GLY   I  189 ? 0.51710 0.51710 0.51710 -0.00000 0.00000  0.00000  189 GLY   E C   
13095 O O   . GLY   I  189 ? 0.93374 0.93374 0.93374 0.00000  0.00000  0.00000  189 GLY   E O   
13096 N N   . ARG   I  190 ? 0.59300 0.59300 0.59300 0.00000  0.00000  0.00000  190 ARG   E N   
13097 C CA  . ARG   I  190 ? 0.44307 0.44307 0.44307 0.00000  0.00000  0.00000  190 ARG   E CA  
13098 C C   . ARG   I  190 ? 0.53318 0.53318 0.53318 0.00000  0.00000  0.00000  190 ARG   E C   
13099 O O   . ARG   I  190 ? 0.66853 0.66853 0.66853 0.00000  0.00000  0.00000  190 ARG   E O   
13100 C CB  . ARG   I  190 ? 0.53438 0.53438 0.53438 0.00000  0.00000  0.00000  190 ARG   E CB  
13101 C CG  . ARG   I  190 ? 0.46670 0.46670 0.46670 0.00000  0.00000  0.00000  190 ARG   E CG  
13102 C CD  . ARG   I  190 ? 0.34646 0.34646 0.34646 0.00000  0.00000  0.00000  190 ARG   E CD  
13103 N NE  . ARG   I  190 ? 0.53208 0.53208 0.53208 0.00000  -0.00000 -0.00000 190 ARG   E NE  
13104 C CZ  . ARG   I  190 ? 0.74714 0.74714 0.74714 0.00000  0.00000  0.00000  190 ARG   E CZ  
13105 N NH1 . ARG   I  190 ? 0.69973 0.69973 0.69973 0.00000  0.00000  0.00000  190 ARG   E NH1 
13106 N NH2 . ARG   I  190 ? 0.56545 0.56545 0.56545 0.00000  0.00000  0.00000  190 ARG   E NH2 
13107 N N   . ALA   I  191 ? 0.52194 0.52194 0.52194 0.00000  0.00000  0.00000  191 ALA   E N   
13108 C CA  . ALA   I  191 ? 0.36736 0.36736 0.36736 0.00000  0.00000  0.00000  191 ALA   E CA  
13109 C C   . ALA   I  191 ? 1.16574 1.16574 1.16574 -0.00000 0.00000  0.00000  191 ALA   E C   
13110 O O   . ALA   I  191 ? 0.38326 0.38326 0.38326 0.00000  0.00000  0.00000  191 ALA   E O   
13111 C CB  . ALA   I  191 ? 0.52335 0.52335 0.52335 0.00000  0.00000  0.00000  191 ALA   E CB  
13112 N N   . PHE   I  192 ? 0.33988 0.33988 0.33988 0.00000  0.00000  0.00000  192 PHE   E N   
13113 C CA  . PHE   I  192 ? 0.38893 0.38893 0.38893 0.00000  0.00000  0.00000  192 PHE   E CA  
13114 C C   . PHE   I  192 ? 0.69094 0.69094 0.69094 0.00000  0.00000  0.00000  192 PHE   E C   
13115 O O   . PHE   I  192 ? 0.55910 0.55910 0.55910 0.00000  0.00000  0.00000  192 PHE   E O   
13116 C CB  . PHE   I  192 ? 0.40841 0.40841 0.40841 0.00000  0.00000  0.00000  192 PHE   E CB  
13117 C CG  . PHE   I  192 ? 0.50289 0.50289 0.50289 0.00000  -0.00000 -0.00000 192 PHE   E CG  
13118 C CD1 . PHE   I  192 ? 0.61873 0.61873 0.61873 -0.00000 0.00000  0.00000  192 PHE   E CD1 
13119 C CD2 . PHE   I  192 ? 0.60542 0.60542 0.60542 0.00000  0.00000  0.00000  192 PHE   E CD2 
13120 C CE1 . PHE   I  192 ? 0.37294 0.37294 0.37294 0.00000  0.00000  0.00000  192 PHE   E CE1 
13121 C CE2 . PHE   I  192 ? 0.68270 0.68270 0.68270 0.00000  -0.00000 0.00000  192 PHE   E CE2 
13122 C CZ  . PHE   I  192 ? 0.47302 0.47302 0.47302 0.00000  0.00000  0.00000  192 PHE   E CZ  
13123 N N   . ASP   I  193 ? 0.71184 0.71184 0.71184 -0.00000 0.00000  0.00000  193 ASP   E N   
13124 C CA  . ASP   I  193 ? 0.45977 0.45977 0.45977 0.00000  0.00000  0.00000  193 ASP   E CA  
13125 C C   . ASP   I  193 ? 0.79531 0.79531 0.79531 0.00000  0.00000  0.00000  193 ASP   E C   
13126 O O   . ASP   I  193 ? 0.29994 0.29994 0.29994 0.00000  0.00000  0.00000  193 ASP   E O   
13127 C CB  . ASP   I  193 ? 0.62303 0.62303 0.62303 -0.00000 0.00000  0.00000  193 ASP   E CB  
13128 C CG  . ASP   I  193 ? 1.16613 1.16613 1.16613 -0.00000 0.00000  0.00000  193 ASP   E CG  
13129 O OD1 . ASP   I  193 ? 0.66860 0.66860 0.66860 0.00000  0.00000  0.00000  193 ASP   E OD1 
13130 O OD2 . ASP   I  193 ? 0.64957 0.64957 0.64957 -0.00000 -0.00000 -0.00000 193 ASP   E OD2 
13131 N N   . GLU   I  194 ? 0.32707 0.32707 0.32707 0.00000  0.00000  0.00000  194 GLU   E N   
13132 C CA  . GLU   I  194 ? 0.66866 0.66866 0.66866 0.00000  0.00000  0.00000  194 GLU   E CA  
13133 C C   . GLU   I  194 ? 0.72410 0.72410 0.72410 -0.00000 0.00000  0.00000  194 GLU   E C   
13134 O O   . GLU   I  194 ? 0.57837 0.57837 0.57837 0.00000  0.00000  0.00000  194 GLU   E O   
13135 C CB  . GLU   I  194 ? 0.56434 0.56434 0.56434 0.00000  0.00000  0.00000  194 GLU   E CB  
13136 C CG  . GLU   I  194 ? 0.38420 0.38420 0.38420 -0.00000 0.00000  0.00000  194 GLU   E CG  
13137 C CD  . GLU   I  194 ? 1.11338 1.11338 1.11338 -0.00000 0.00000  0.00000  194 GLU   E CD  
13138 O OE1 . GLU   I  194 ? 0.79183 0.79183 0.79183 -0.00000 0.00000  0.00000  194 GLU   E OE1 
13139 O OE2 . GLU   I  194 ? 0.76083 0.76083 0.76083 0.00000  0.00000  0.00000  194 GLU   E OE2 
13140 N N   . VAL   I  195 ? 0.66752 0.66752 0.66752 -0.00000 0.00000  0.00000  195 VAL   E N   
13141 C CA  . VAL   I  195 ? 0.25970 0.25970 0.25970 0.00000  0.00000  0.00000  195 VAL   E CA  
13142 C C   . VAL   I  195 ? 1.03767 1.03767 1.03767 -0.00000 -0.00000 0.00000  195 VAL   E C   
13143 O O   . VAL   I  195 ? 0.42708 0.42708 0.42708 -0.00000 0.00000  0.00000  195 VAL   E O   
13144 C CB  . VAL   I  195 ? 0.70596 0.70596 0.70596 0.00000  0.00000  0.00000  195 VAL   E CB  
13145 C CG1 . VAL   I  195 ? 0.32184 0.32184 0.32184 0.00000  0.00000  0.00000  195 VAL   E CG1 
13146 C CG2 . VAL   I  195 ? 0.38513 0.38513 0.38513 0.00000  0.00000  0.00000  195 VAL   E CG2 
13147 N N   . PHE   I  196 ? 0.35924 0.35924 0.35924 -0.00000 0.00000  0.00000  196 PHE   E N   
13148 C CA  . PHE   I  196 ? 0.76351 0.76351 0.76351 0.00000  0.00000  0.00000  196 PHE   E CA  
13149 C C   . PHE   I  196 ? 0.51648 0.51648 0.51648 0.00000  0.00000  0.00000  196 PHE   E C   
13150 O O   . PHE   I  196 ? 0.54511 0.54511 0.54511 -0.00000 0.00000  0.00000  196 PHE   E O   
13151 C CB  . PHE   I  196 ? 0.41829 0.41829 0.41829 0.00000  0.00000  0.00000  196 PHE   E CB  
13152 C CG  . PHE   I  196 ? 0.63937 0.63937 0.63937 -0.00000 0.00000  0.00000  196 PHE   E CG  
13153 C CD1 . PHE   I  196 ? 0.43299 0.43299 0.43299 -0.00000 0.00000  0.00000  196 PHE   E CD1 
13154 C CD2 . PHE   I  196 ? 0.34957 0.34957 0.34957 0.00000  0.00000  0.00000  196 PHE   E CD2 
13155 C CE1 . PHE   I  196 ? 0.48385 0.48385 0.48385 -0.00000 0.00000  0.00000  196 PHE   E CE1 
13156 C CE2 . PHE   I  196 ? 0.57988 0.57988 0.57988 0.00000  0.00000  0.00000  196 PHE   E CE2 
13157 C CZ  . PHE   I  196 ? 0.47081 0.47081 0.47081 0.00000  0.00000  0.00000  196 PHE   E CZ  
13158 N N   . LEU   I  197 ? 0.46190 0.46190 0.46190 -0.00000 0.00000  0.00000  197 LEU   E N   
13159 C CA  . LEU   I  197 ? 0.49770 0.49770 0.49770 -0.00000 0.00000  0.00000  197 LEU   E CA  
13160 C C   . LEU   I  197 ? 0.73320 0.73320 0.73320 0.00000  0.00000  0.00000  197 LEU   E C   
13161 O O   . LEU   I  197 ? 0.42162 0.42162 0.42162 -0.00000 0.00000  0.00000  197 LEU   E O   
13162 C CB  . LEU   I  197 ? 0.46646 0.46646 0.46646 0.00000  0.00000  0.00000  197 LEU   E CB  
13163 C CG  . LEU   I  197 ? 0.42461 0.42461 0.42461 -0.00000 0.00000  0.00000  197 LEU   E CG  
13164 C CD1 . LEU   I  197 ? 0.52903 0.52903 0.52903 0.00000  0.00000  0.00000  197 LEU   E CD1 
13165 C CD2 . LEU   I  197 ? 1.02242 1.02242 1.02242 0.00000  0.00000  0.00000  197 LEU   E CD2 
13166 N N   . CYS   I  198 ? 0.55622 0.55622 0.55622 0.00000  0.00000  0.00000  198 CYS   E N   
13167 C CA  . CYS   I  198 ? 0.54576 0.54576 0.54576 -0.00000 0.00000  0.00000  198 CYS   E CA  
13168 C C   . CYS   I  198 ? 0.59174 0.59174 0.59174 -0.00000 0.00000  0.00000  198 CYS   E C   
13169 O O   . CYS   I  198 ? 0.68163 0.68163 0.68163 -0.00000 0.00000  0.00000  198 CYS   E O   
13170 C CB  . CYS   I  198 ? 0.46285 0.46285 0.46285 0.00000  0.00000  0.00000  198 CYS   E CB  
13171 S SG  . CYS   I  198 ? 0.57350 0.57350 0.57350 0.00000  0.00000  0.00000  198 CYS   E SG  
13172 N N   . ASP   I  199 ? 0.70824 0.70824 0.70824 0.00000  0.00000  0.00000  199 ASP   E N   
13173 C CA  . ASP   I  199 ? 0.56226 0.56226 0.56226 -0.00000 0.00000  0.00000  199 ASP   E CA  
13174 C C   . ASP   I  199 ? 1.00068 1.00068 1.00068 0.00000  0.00000  0.00000  199 ASP   E C   
13175 O O   . ASP   I  199 ? 0.55916 0.55916 0.55916 0.00000  0.00000  0.00000  199 ASP   E O   
13176 C CB  . ASP   I  199 ? 0.58512 0.58512 0.58512 0.00000  0.00000  0.00000  199 ASP   E CB  
13177 C CG  . ASP   I  199 ? 1.86872 1.86872 1.86872 0.00000  0.00000  -0.00000 199 ASP   E CG  
13178 O OD1 . ASP   I  199 ? 0.62104 0.62104 0.62104 -0.00000 0.00000  0.00000  199 ASP   E OD1 
13179 O OD2 . ASP   I  199 ? 0.71856 0.71856 0.71856 0.00000  0.00000  0.00000  199 ASP   E OD2 
13180 N N   . LYS   I  200 ? 0.55450 0.55450 0.55450 0.00000  -0.00000 0.00000  200 LYS   E N   
13181 C CA  . LYS   I  200 ? 0.87696 0.87696 0.87696 0.00000  0.00000  0.00000  200 LYS   E CA  
13182 C C   . LYS   I  200 ? 0.83573 0.83573 0.83573 0.00000  0.00000  0.00000  200 LYS   E C   
13183 O O   . LYS   I  200 ? 0.73082 0.73082 0.73082 -0.00000 0.00000  0.00000  200 LYS   E O   
13184 C CB  . LYS   I  200 ? 0.55216 0.55216 0.55216 0.00000  0.00000  0.00000  200 LYS   E CB  
13185 C CG  . LYS   I  200 ? 0.84079 0.84079 0.84079 0.00000  0.00000  0.00000  200 LYS   E CG  
13186 C CD  . LYS   I  200 ? 1.10055 1.10055 1.10055 0.00000  0.00000  0.00000  200 LYS   E CD  
13187 C CE  . LYS   I  200 ? 0.88877 0.88877 0.88877 0.00000  0.00000  0.00000  200 LYS   E CE  
13188 N NZ  . LYS   I  200 ? 0.82012 0.82012 0.82012 0.00000  0.00000  0.00000  200 LYS   E NZ  
13189 N N   . ASN   I  201 ? 0.66601 0.66601 0.66601 0.00000  0.00000  0.00000  201 ASN   E N   
13190 C CA  . ASN   I  201 ? 0.95935 0.95935 0.95935 0.00000  0.00000  0.00000  201 ASN   E CA  
13191 C C   . ASN   I  201 ? 0.65216 0.65216 0.65216 0.00000  0.00000  0.00000  201 ASN   E C   
13192 O O   . ASN   I  201 ? 1.05796 1.05796 1.05796 0.00000  0.00000  -0.00000 201 ASN   E O   
13193 C CB  . ASN   I  201 ? 0.63003 0.63003 0.63003 0.00000  0.00000  0.00000  201 ASN   E CB  
13194 C CG  . ASN   I  201 ? 1.10452 1.10452 1.10452 0.00000  0.00000  0.00000  201 ASN   E CG  
13195 O OD1 . ASN   I  201 ? 0.51220 0.51220 0.51220 -0.00000 0.00000  0.00000  201 ASN   E OD1 
13196 N ND2 . ASN   I  201 ? 0.70068 0.70068 0.70068 0.00000  0.00000  0.00000  201 ASN   E ND2 
13197 N N   . ALA   I  202 ? 1.22849 1.22849 1.22849 0.00000  0.00000  -0.00000 202 ALA   E N   
13198 C CA  . ALA   I  202 ? 0.62684 0.62684 0.62684 0.00000  -0.00000 0.00000  202 ALA   E CA  
13199 C C   . ALA   I  202 ? 0.54111 0.54111 0.54111 0.00000  0.00000  0.00000  202 ALA   E C   
13200 O O   . ALA   I  202 ? 0.68998 0.68998 0.68998 0.00000  0.00000  0.00000  202 ALA   E O   
13201 C CB  . ALA   I  202 ? 0.34021 0.34021 0.34021 0.00000  0.00000  0.00000  202 ALA   E CB  
13202 N N   . PRO   I  203 ? 0.89370 0.89370 0.89370 0.00000  0.00000  0.00000  203 PRO   E N   
13203 C CA  . PRO   I  203 ? 0.82810 0.82810 0.82810 0.00000  0.00000  0.00000  203 PRO   E CA  
13204 C C   . PRO   I  203 ? 0.69923 0.69923 0.69923 0.00000  0.00000  -0.00000 203 PRO   E C   
13205 O O   . PRO   I  203 ? 0.44918 0.44918 0.44918 0.00000  0.00000  0.00000  203 PRO   E O   
13206 C CB  . PRO   I  203 ? 0.54039 0.54039 0.54039 -0.00000 0.00000  0.00000  203 PRO   E CB  
13207 C CG  . PRO   I  203 ? 0.42271 0.42271 0.42271 0.00000  0.00000  0.00000  203 PRO   E CG  
13208 C CD  . PRO   I  203 ? 0.27242 0.27242 0.27242 0.00000  0.00000  0.00000  203 PRO   E CD  
13209 N N   . TYR   I  204 ? 0.61884 0.61884 0.61884 0.00000  0.00000  0.00000  204 TYR   E N   
13210 C CA  . TYR   I  204 ? 0.75904 0.75904 0.75904 0.00000  0.00000  0.00000  204 TYR   E CA  
13211 C C   . TYR   I  204 ? 0.67936 0.67936 0.67936 -0.00000 0.00000  0.00000  204 TYR   E C   
13212 O O   . TYR   I  204 ? 0.73449 0.73449 0.73449 0.00000  0.00000  0.00000  204 TYR   E O   
13213 C CB  . TYR   I  204 ? 0.59954 0.59954 0.59954 0.00000  0.00000  0.00000  204 TYR   E CB  
13214 C CG  . TYR   I  204 ? 0.65369 0.65369 0.65369 -0.00000 -0.00000 0.00000  204 TYR   E CG  
13215 C CD1 . TYR   I  204 ? 0.58734 0.58734 0.58734 -0.00000 -0.00000 0.00000  204 TYR   E CD1 
13216 C CD2 . TYR   I  204 ? 0.53905 0.53905 0.53905 0.00000  0.00000  0.00000  204 TYR   E CD2 
13217 C CE1 . TYR   I  204 ? 0.36843 0.36843 0.36843 0.00000  0.00000  0.00000  204 TYR   E CE1 
13218 C CE2 . TYR   I  204 ? 0.50160 0.50160 0.50160 -0.00000 0.00000  0.00000  204 TYR   E CE2 
13219 C CZ  . TYR   I  204 ? 0.66895 0.66895 0.66895 -0.00000 0.00000  0.00000  204 TYR   E CZ  
13220 O OH  . TYR   I  204 ? 0.69440 0.69440 0.69440 0.00000  0.00000  0.00000  204 TYR   E OH  
13221 N N   . TYR   I  205 ? 0.54693 0.54693 0.54693 0.00000  0.00000  0.00000  205 TYR   E N   
13222 C CA  . TYR   I  205 ? 0.52110 0.52110 0.52110 0.00000  0.00000  0.00000  205 TYR   E CA  
13223 C C   . TYR   I  205 ? 0.61511 0.61511 0.61511 -0.00000 0.00000  0.00000  205 TYR   E C   
13224 O O   . TYR   I  205 ? 0.58957 0.58957 0.58957 0.00000  0.00000  0.00000  205 TYR   E O   
13225 C CB  . TYR   I  205 ? 0.61125 0.61125 0.61125 0.00000  0.00000  0.00000  205 TYR   E CB  
13226 C CG  . TYR   I  205 ? 0.78485 0.78485 0.78485 0.00000  0.00000  0.00000  205 TYR   E CG  
13227 C CD1 . TYR   I  205 ? 0.68671 0.68671 0.68671 0.00000  -0.00000 0.00000  205 TYR   E CD1 
13228 C CD2 . TYR   I  205 ? 0.62658 0.62658 0.62658 0.00000  0.00000  -0.00000 205 TYR   E CD2 
13229 C CE1 . TYR   I  205 ? 0.49518 0.49518 0.49518 0.00000  0.00000  0.00000  205 TYR   E CE1 
13230 C CE2 . TYR   I  205 ? 0.79915 0.79915 0.79915 -0.00000 0.00000  0.00000  205 TYR   E CE2 
13231 C CZ  . TYR   I  205 ? 1.05111 1.05111 1.05111 -0.00000 0.00000  0.00000  205 TYR   E CZ  
13232 O OH  . TYR   I  205 ? 0.67860 0.67860 0.67860 0.00000  0.00000  0.00000  205 TYR   E OH  
13233 N N   . GLY   I  206 ? 0.50331 0.50331 0.50331 0.00000  0.00000  0.00000  206 GLY   E N   
13234 C CA  . GLY   I  206 ? 0.48922 0.48922 0.48922 0.00000  -0.00000 0.00000  206 GLY   E CA  
13235 C C   . GLY   I  206 ? 0.66386 0.66386 0.66386 0.00000  0.00000  0.00000  206 GLY   E C   
13236 O O   . GLY   I  206 ? 0.56274 0.56274 0.56274 -0.00000 0.00000  0.00000  206 GLY   E O   
13237 N N   . PHE   I  207 ? 0.49923 0.49923 0.49923 0.00000  0.00000  0.00000  207 PHE   E N   
13238 C CA  . PHE   I  207 ? 0.65197 0.65197 0.65197 0.00000  0.00000  0.00000  207 PHE   E CA  
13239 C C   . PHE   I  207 ? 0.59452 0.59452 0.59452 0.00000  0.00000  0.00000  207 PHE   E C   
13240 O O   . PHE   I  207 ? 0.72170 0.72170 0.72170 0.00000  0.00000  0.00000  207 PHE   E O   
13241 C CB  . PHE   I  207 ? 0.49157 0.49157 0.49157 -0.00000 0.00000  0.00000  207 PHE   E CB  
13242 C CG  . PHE   I  207 ? 0.68976 0.68976 0.68976 0.00000  0.00000  0.00000  207 PHE   E CG  
13243 C CD1 . PHE   I  207 ? 0.35765 0.35765 0.35765 0.00000  0.00000  0.00000  207 PHE   E CD1 
13244 C CD2 . PHE   I  207 ? 0.41308 0.41308 0.41308 -0.00000 0.00000  0.00000  207 PHE   E CD2 
13245 C CE1 . PHE   I  207 ? 0.61484 0.61484 0.61484 0.00000  0.00000  0.00000  207 PHE   E CE1 
13246 C CE2 . PHE   I  207 ? 0.45937 0.45937 0.45937 0.00000  0.00000  0.00000  207 PHE   E CE2 
13247 C CZ  . PHE   I  207 ? 0.67414 0.67414 0.67414 -0.00000 0.00000  0.00000  207 PHE   E CZ  
13248 N N   . ASN   I  208 ? 0.47294 0.47294 0.47294 0.00000  0.00000  0.00000  208 ASN   E N   
13249 C CA  . ASN   I  208 ? 0.75807 0.75807 0.75807 -0.00000 0.00000  0.00000  208 ASN   E CA  
13250 C C   . ASN   I  208 ? 0.37336 0.37336 0.37336 0.00000  0.00000  0.00000  208 ASN   E C   
13251 O O   . ASN   I  208 ? 1.11015 1.11015 1.11015 0.00000  0.00000  0.00000  208 ASN   E O   
13252 C CB  . ASN   I  208 ? 0.37906 0.37906 0.37906 0.00000  0.00000  0.00000  208 ASN   E CB  
13253 C CG  . ASN   I  208 ? 1.09425 1.09425 1.09425 0.00000  0.00000  0.00000  208 ASN   E CG  
13254 O OD1 . ASN   I  208 ? 1.79146 1.79146 1.79146 -0.00000 0.00000  0.00000  208 ASN   E OD1 
13255 N ND2 . ASN   I  208 ? 0.80265 0.80265 0.80265 0.00000  0.00000  0.00000  208 ASN   E ND2 
13256 N N   . SER   I  209 ? 0.64252 0.64252 0.64252 0.00000  0.00000  0.00000  209 SER   E N   
13257 C CA  . SER   I  209 ? 0.43309 0.43309 0.43309 0.00000  0.00000  -0.00000 209 SER   E CA  
13258 C C   . SER   I  209 ? 0.71359 0.71359 0.71359 0.00000  0.00000  0.00000  209 SER   E C   
13259 O O   . SER   I  209 ? 0.39991 0.39991 0.39991 0.00000  0.00000  0.00000  209 SER   E O   
13260 C CB  . SER   I  209 ? 0.57231 0.57231 0.57231 -0.00000 0.00000  0.00000  209 SER   E CB  
13261 O OG  . SER   I  209 ? 0.31045 0.31045 0.31045 0.00000  -0.00000 0.00000  209 SER   E OG  
13262 N N   . TYR   I  210 ? 0.45713 0.45713 0.45713 0.00000  0.00000  0.00000  210 TYR   E N   
13263 C CA  . TYR   I  210 ? 0.30658 0.30658 0.30658 0.00000  0.00000  0.00000  210 TYR   E CA  
13264 C C   . TYR   I  210 ? 0.47134 0.47134 0.47134 0.00000  0.00000  0.00000  210 TYR   E C   
13265 O O   . TYR   I  210 ? 0.38200 0.38200 0.38200 0.00000  0.00000  0.00000  210 TYR   E O   
13266 C CB  . TYR   I  210 ? 0.17239 0.17239 0.17239 0.00000  0.00000  0.00000  210 TYR   E CB  
13267 C CG  . TYR   I  210 ? 0.59127 0.59127 0.59127 0.00000  0.00000  0.00000  210 TYR   E CG  
13268 C CD1 . TYR   I  210 ? 0.30026 0.30026 0.30026 0.00000  0.00000  0.00000  210 TYR   E CD1 
13269 C CD2 . TYR   I  210 ? 0.49547 0.49547 0.49547 0.00000  0.00000  0.00000  210 TYR   E CD2 
13270 C CE1 . TYR   I  210 ? 0.34614 0.34614 0.34614 0.00000  0.00000  0.00000  210 TYR   E CE1 
13271 C CE2 . TYR   I  210 ? 0.51789 0.51789 0.51789 0.00000  0.00000  0.00000  210 TYR   E CE2 
13272 C CZ  . TYR   I  210 ? 0.63181 0.63181 0.63181 -0.00000 0.00000  0.00000  210 TYR   E CZ  
13273 O OH  . TYR   I  210 ? 0.40100 0.40100 0.40100 0.00000  0.00000  0.00000  210 TYR   E OH  
13274 N N   . ASP   I  211 ? 0.39311 0.39311 0.39311 -0.00000 0.00000  0.00000  211 ASP   E N   
13275 C CA  . ASP   I  211 ? 0.32628 0.32628 0.32628 -0.00000 0.00000  0.00000  211 ASP   E CA  
13276 C C   . ASP   I  211 ? 0.59717 0.59717 0.59717 -0.00000 0.00000  0.00000  211 ASP   E C   
13277 O O   . ASP   I  211 ? 0.35505 0.35505 0.35505 0.00000  0.00000  0.00000  211 ASP   E O   
13278 C CB  . ASP   I  211 ? 0.36605 0.36605 0.36605 0.00000  0.00000  0.00000  211 ASP   E CB  
13279 C CG  . ASP   I  211 ? 0.37293 0.37293 0.37293 0.00000  0.00000  0.00000  211 ASP   E CG  
13280 O OD1 . ASP   I  211 ? 0.43310 0.43310 0.43310 0.00000  0.00000  0.00000  211 ASP   E OD1 
13281 O OD2 . ASP   I  211 ? 0.66000 0.66000 0.66000 -0.00000 0.00000  -0.00000 211 ASP   E OD2 
13282 N N   . ASP   I  212 ? 0.36723 0.36723 0.36723 0.00000  0.00000  0.00000  212 ASP   E N   
13283 C CA  . ASP   I  212 ? 0.48778 0.48778 0.48778 0.00000  0.00000  0.00000  212 ASP   E CA  
13284 C C   . ASP   I  212 ? 0.38980 0.38980 0.38980 -0.00000 0.00000  0.00000  212 ASP   E C   
13285 O O   . ASP   I  212 ? 0.39850 0.39850 0.39850 -0.00000 0.00000  0.00000  212 ASP   E O   
13286 C CB  . ASP   I  212 ? 0.50650 0.50650 0.50650 0.00000  0.00000  0.00000  212 ASP   E CB  
13287 C CG  . ASP   I  212 ? 0.60935 0.60935 0.60935 0.00000  -0.00000 0.00000  212 ASP   E CG  
13288 O OD1 . ASP   I  212 ? 0.79933 0.79933 0.79933 0.00000  0.00000  -0.00000 212 ASP   E OD1 
13289 O OD2 . ASP   I  212 ? 0.62040 0.62040 0.62040 0.00000  0.00000  0.00000  212 ASP   E OD2 
13290 N N   . PHE   I  213 ? 0.32143 0.32143 0.32143 -0.00000 0.00000  0.00000  213 PHE   E N   
13291 C CA  . PHE   I  213 ? 0.28686 0.28686 0.28686 -0.00000 0.00000  -0.00000 213 PHE   E CA  
13292 C C   . PHE   I  213 ? 0.75432 0.75432 0.75432 -0.00000 0.00000  -0.00000 213 PHE   E C   
13293 O O   . PHE   I  213 ? 0.43132 0.43132 0.43132 -0.00000 0.00000  0.00000  213 PHE   E O   
13294 C CB  . PHE   I  213 ? 0.37144 0.37144 0.37144 -0.00000 0.00000  0.00000  213 PHE   E CB  
13295 C CG  . PHE   I  213 ? 0.53228 0.53228 0.53228 0.00000  -0.00000 0.00000  213 PHE   E CG  
13296 C CD1 . PHE   I  213 ? 0.57638 0.57638 0.57638 -0.00000 0.00000  0.00000  213 PHE   E CD1 
13297 C CD2 . PHE   I  213 ? 0.38291 0.38291 0.38291 0.00000  0.00000  0.00000  213 PHE   E CD2 
13298 C CE1 . PHE   I  213 ? 0.69639 0.69639 0.69639 0.00000  0.00000  0.00000  213 PHE   E CE1 
13299 C CE2 . PHE   I  213 ? 0.73364 0.73364 0.73364 -0.00000 0.00000  0.00000  213 PHE   E CE2 
13300 C CZ  . PHE   I  213 ? 0.60005 0.60005 0.60005 -0.00000 0.00000  0.00000  213 PHE   E CZ  
13301 N N   . PHE   I  214 ? 0.30786 0.30786 0.30786 0.00000  0.00000  0.00000  214 PHE   E N   
13302 C CA  . PHE   I  214 ? 0.28624 0.28624 0.28624 -0.00000 0.00000  0.00000  214 PHE   E CA  
13303 C C   . PHE   I  214 ? 0.27111 0.27111 0.27111 -0.00000 0.00000  0.00000  214 PHE   E C   
13304 O O   . PHE   I  214 ? 0.62096 0.62096 0.62096 0.00000  0.00000  0.00000  214 PHE   E O   
13305 C CB  . PHE   I  214 ? 0.39686 0.39686 0.39686 0.00000  0.00000  0.00000  214 PHE   E CB  
13306 C CG  . PHE   I  214 ? 0.37420 0.37420 0.37420 0.00000  0.00000  0.00000  214 PHE   E CG  
13307 C CD1 . PHE   I  214 ? 0.35569 0.35569 0.35569 -0.00000 0.00000  0.00000  214 PHE   E CD1 
13308 C CD2 . PHE   I  214 ? 0.46834 0.46834 0.46834 0.00000  0.00000  -0.00000 214 PHE   E CD2 
13309 C CE1 . PHE   I  214 ? 0.31067 0.31067 0.31067 0.00000  0.00000  0.00000  214 PHE   E CE1 
13310 C CE2 . PHE   I  214 ? 0.46063 0.46063 0.46063 -0.00000 0.00000  0.00000  214 PHE   E CE2 
13311 C CZ  . PHE   I  214 ? 0.38363 0.38363 0.38363 0.00000  0.00000  0.00000  214 PHE   E CZ  
13312 N N   . ASN   I  215 ? 0.28527 0.28527 0.28527 0.00000  0.00000  0.00000  215 ASN   E N   
13313 C CA  . ASN   I  215 ? 0.38227 0.38227 0.38227 -0.00000 0.00000  0.00000  215 ASN   E CA  
13314 C C   . ASN   I  215 ? 0.50617 0.50617 0.50617 0.00000  0.00000  0.00000  215 ASN   E C   
13315 O O   . ASN   I  215 ? 0.42693 0.42693 0.42693 0.00000  0.00000  0.00000  215 ASN   E O   
13316 C CB  . ASN   I  215 ? 0.38033 0.38033 0.38033 0.00000  0.00000  0.00000  215 ASN   E CB  
13317 C CG  . ASN   I  215 ? 0.67318 0.67318 0.67318 0.00000  0.00000  0.00000  215 ASN   E CG  
13318 O OD1 . ASN   I  215 ? 0.40291 0.40291 0.40291 0.00000  0.00000  0.00000  215 ASN   E OD1 
13319 N ND2 . ASN   I  215 ? 0.36147 0.36147 0.36147 0.00000  0.00000  0.00000  215 ASN   E ND2 
13320 N N   . ARG   I  216 ? 0.25829 0.25829 0.25829 -0.00000 0.00000  0.00000  216 ARG   E N   
13321 C CA  . ARG   I  216 ? 0.37076 0.37076 0.37076 -0.00000 0.00000  0.00000  216 ARG   E CA  
13322 C C   . ARG   I  216 ? 0.66261 0.66261 0.66261 -0.00000 0.00000  0.00000  216 ARG   E C   
13323 O O   . ARG   I  216 ? 0.36098 0.36098 0.36098 -0.00000 0.00000  0.00000  216 ARG   E O   
13324 C CB  . ARG   I  216 ? 0.32369 0.32369 0.32369 0.00000  0.00000  0.00000  216 ARG   E CB  
13325 C CG  . ARG   I  216 ? 0.31471 0.31471 0.31471 -0.00000 0.00000  0.00000  216 ARG   E CG  
13326 C CD  . ARG   I  216 ? 0.44534 0.44534 0.44534 -0.00000 0.00000  0.00000  216 ARG   E CD  
13327 N NE  . ARG   I  216 ? 0.30527 0.30527 0.30527 0.00000  0.00000  0.00000  216 ARG   E NE  
13328 C CZ  . ARG   I  216 ? 0.61910 0.61910 0.61910 0.00000  0.00000  -0.00000 216 ARG   E CZ  
13329 N NH1 . ARG   I  216 ? 0.35076 0.35076 0.35076 -0.00000 0.00000  0.00000  216 ARG   E NH1 
13330 N NH2 . ARG   I  216 ? 0.40756 0.40756 0.40756 0.00000  0.00000  0.00000  216 ARG   E NH2 
13331 N N   . ARG   I  217 ? 0.34624 0.34624 0.34624 -0.00000 0.00000  0.00000  217 ARG   E N   
13332 C CA  . ARG   I  217 ? 0.38054 0.38054 0.38054 0.00000  0.00000  0.00000  217 ARG   E CA  
13333 C C   . ARG   I  217 ? 0.39508 0.39508 0.39508 0.00000  0.00000  0.00000  217 ARG   E C   
13334 O O   . ARG   I  217 ? 0.58317 0.58317 0.58317 0.00000  0.00000  0.00000  217 ARG   E O   
13335 C CB  . ARG   I  217 ? 0.35317 0.35317 0.35317 0.00000  0.00000  0.00000  217 ARG   E CB  
13336 C CG  . ARG   I  217 ? 0.42672 0.42672 0.42672 -0.00000 0.00000  0.00000  217 ARG   E CG  
13337 C CD  . ARG   I  217 ? 0.79639 0.79639 0.79639 0.00000  0.00000  0.00000  217 ARG   E CD  
13338 N NE  . ARG   I  217 ? 1.76273 1.76273 1.76273 0.00000  -0.00000 0.00000  217 ARG   E NE  
13339 N N   . PHE   I  218 ? 0.48845 0.48845 0.48845 0.00000  0.00000  -0.00000 218 PHE   E N   
13340 C CA  . PHE   I  218 ? 0.34746 0.34746 0.34746 0.00000  0.00000  0.00000  218 PHE   E CA  
13341 C C   . PHE   I  218 ? 0.73312 0.73312 0.73312 -0.00000 0.00000  0.00000  218 PHE   E C   
13342 O O   . PHE   I  218 ? 0.37547 0.37547 0.37547 0.00000  0.00000  0.00000  218 PHE   E O   
13343 C CB  . PHE   I  218 ? 0.23159 0.23159 0.23159 0.00000  0.00000  0.00000  218 PHE   E CB  
13344 C CG  . PHE   I  218 ? 0.48053 0.48053 0.48053 -0.00000 0.00000  0.00000  218 PHE   E CG  
13345 C CD1 . PHE   I  218 ? 0.25271 0.25271 0.25271 0.00000  0.00000  0.00000  218 PHE   E CD1 
13346 C CD2 . PHE   I  218 ? 0.36240 0.36240 0.36240 0.00000  0.00000  -0.00000 218 PHE   E CD2 
13347 C CE1 . PHE   I  218 ? 0.57251 0.57251 0.57251 0.00000  0.00000  0.00000  218 PHE   E CE1 
13348 C CE2 . PHE   I  218 ? 0.35312 0.35312 0.35312 0.00000  0.00000  0.00000  218 PHE   E CE2 
13349 C CZ  . PHE   I  218 ? 0.26770 0.26770 0.26770 0.00000  0.00000  0.00000  218 PHE   E CZ  
13350 N N   . ARG   I  219 ? 0.44971 0.44971 0.44971 0.00000  0.00000  0.00000  219 ARG   E N   
13351 C CA  . ARG   I  219 ? 0.50456 0.50456 0.50456 0.00000  0.00000  0.00000  219 ARG   E CA  
13352 C C   . ARG   I  219 ? 0.46580 0.46580 0.46580 0.00000  0.00000  0.00000  219 ARG   E C   
13353 O O   . ARG   I  219 ? 0.44725 0.44725 0.44725 0.00000  0.00000  0.00000  219 ARG   E O   
13354 C CB  . ARG   I  219 ? 0.41321 0.41321 0.41321 0.00000  0.00000  0.00000  219 ARG   E CB  
13355 C CG  . ARG   I  219 ? 0.62142 0.62142 0.62142 0.00000  0.00000  0.00000  219 ARG   E CG  
13356 C CD  . ARG   I  219 ? 0.49356 0.49356 0.49356 -0.00000 0.00000  0.00000  219 ARG   E CD  
13357 N NE  . ARG   I  219 ? 0.31785 0.31785 0.31785 0.00000  0.00000  0.00000  219 ARG   E NE  
13358 C CZ  . ARG   I  219 ? 1.17791 1.17791 1.17791 -0.00000 0.00000  0.00000  219 ARG   E CZ  
13359 N NH1 . ARG   I  219 ? 0.32107 0.32107 0.32107 0.00000  0.00000  0.00000  219 ARG   E NH1 
13360 N NH2 . ARG   I  219 ? 0.21741 0.21741 0.21741 -0.00000 0.00000  0.00000  219 ARG   E NH2 
13361 N N   . ASN   I  220 ? 0.39595 0.39595 0.39595 0.00000  0.00000  0.00000  220 ASN   E N   
13362 C CA  . ASN   I  220 ? 0.47253 0.47253 0.47253 -0.00000 0.00000  0.00000  220 ASN   E CA  
13363 C C   . ASN   I  220 ? 0.43312 0.43312 0.43312 0.00000  0.00000  0.00000  220 ASN   E C   
13364 O O   . ASN   I  220 ? 0.50204 0.50204 0.50204 0.00000  0.00000  0.00000  220 ASN   E O   
13365 C CB  . ASN   I  220 ? 0.57273 0.57273 0.57273 0.00000  0.00000  0.00000  220 ASN   E CB  
13366 C CG  . ASN   I  220 ? 0.89294 0.89294 0.89294 -0.00000 -0.00000 0.00000  220 ASN   E CG  
13367 O OD1 . ASN   I  220 ? 0.57946 0.57946 0.57946 0.00000  -0.00000 0.00000  220 ASN   E OD1 
13368 N ND2 . ASN   I  220 ? 0.59573 0.59573 0.59573 -0.00000 0.00000  0.00000  220 ASN   E ND2 
13369 N N   . ARG   I  221 ? 0.39443 0.39443 0.39443 0.00000  0.00000  0.00000  221 ARG   E N   
13370 C CA  . ARG   I  221 ? 0.43676 0.43676 0.43676 0.00000  0.00000  0.00000  221 ARG   E CA  
13371 C C   . ARG   I  221 ? 0.54683 0.54683 0.54683 -0.00000 0.00000  0.00000  221 ARG   E C   
13372 O O   . ARG   I  221 ? 0.41933 0.41933 0.41933 -0.00000 0.00000  0.00000  221 ARG   E O   
13373 C CB  . ARG   I  221 ? 0.27815 0.27815 0.27815 -0.00000 0.00000  0.00000  221 ARG   E CB  
13374 C CG  . ARG   I  221 ? 0.28479 0.28479 0.28479 -0.00000 0.00000  0.00000  221 ARG   E CG  
13375 C CD  . ARG   I  221 ? 0.43296 0.43296 0.43296 0.00000  0.00000  0.00000  221 ARG   E CD  
13376 N NE  . ARG   I  221 ? 0.37002 0.37002 0.37002 0.00000  0.00000  0.00000  221 ARG   E NE  
13377 C CZ  . ARG   I  221 ? 0.51604 0.51604 0.51604 -0.00000 0.00000  0.00000  221 ARG   E CZ  
13378 N NH1 . ARG   I  221 ? 0.44475 0.44475 0.44475 0.00000  0.00000  0.00000  221 ARG   E NH1 
13379 N NH2 . ARG   I  221 ? 0.32721 0.32721 0.32721 0.00000  0.00000  0.00000  221 ARG   E NH2 
13380 N N   . ASP   I  222 ? 0.44859 0.44859 0.44859 0.00000  0.00000  0.00000  222 ASP   E N   
13381 C CA  . ASP   I  222 ? 0.66368 0.66368 0.66368 -0.00000 0.00000  0.00000  222 ASP   E CA  
13382 C C   . ASP   I  222 ? 0.69820 0.69820 0.69820 0.00000  0.00000  -0.00000 222 ASP   E C   
13383 O O   . ASP   I  222 ? 0.53131 0.53131 0.53131 -0.00000 0.00000  0.00000  222 ASP   E O   
13384 C CB  . ASP   I  222 ? 0.37900 0.37900 0.37900 0.00000  0.00000  0.00000  222 ASP   E CB  
13385 C CG  . ASP   I  222 ? 0.61954 0.61954 0.61954 0.00000  0.00000  0.00000  222 ASP   E CG  
13386 O OD1 . ASP   I  222 ? 0.70774 0.70774 0.70774 0.00000  0.00000  0.00000  222 ASP   E OD1 
13387 O OD2 . ASP   I  222 ? 0.82343 0.82343 0.82343 0.00000  0.00000  0.00000  222 ASP   E OD2 
13388 N N   . ILE   I  223 ? 0.43179 0.43179 0.43179 0.00000  0.00000  0.00000  223 ILE   E N   
13389 C CA  . ILE   I  223 ? 0.55282 0.55282 0.55282 0.00000  0.00000  0.00000  223 ILE   E CA  
13390 C C   . ILE   I  223 ? 0.69478 0.69478 0.69478 -0.00000 0.00000  0.00000  223 ILE   E C   
13391 O O   . ILE   I  223 ? 0.72678 0.72678 0.72678 -0.00000 0.00000  0.00000  223 ILE   E O   
13392 C CB  . ILE   I  223 ? 0.71277 0.71277 0.71277 0.00000  -0.00000 0.00000  223 ILE   E CB  
13393 C CG1 . ILE   I  223 ? 0.47234 0.47234 0.47234 0.00000  0.00000  0.00000  223 ILE   E CG1 
13394 C CG2 . ILE   I  223 ? 0.31768 0.31768 0.31768 0.00000  0.00000  0.00000  223 ILE   E CG2 
13395 C CD1 . ILE   I  223 ? 0.51070 0.51070 0.51070 0.00000  0.00000  0.00000  223 ILE   E CD1 
13396 N N   . ASP   I  224 ? 0.42204 0.42204 0.42204 -0.00000 0.00000  0.00000  224 ASP   E N   
13397 C CA  . ASP   I  224 ? 0.43604 0.43604 0.43604 0.00000  0.00000  0.00000  224 ASP   E CA  
13398 C C   . ASP   I  224 ? 0.44715 0.44715 0.44715 0.00000  0.00000  0.00000  224 ASP   E C   
13399 O O   . ASP   I  224 ? 0.39132 0.39132 0.39132 0.00000  0.00000  0.00000  224 ASP   E O   
13400 C CB  . ASP   I  224 ? 0.38424 0.38424 0.38424 0.00000  0.00000  0.00000  224 ASP   E CB  
13401 C CG  . ASP   I  224 ? 0.55356 0.55356 0.55356 0.00000  0.00000  0.00000  224 ASP   E CG  
13402 O OD1 . ASP   I  224 ? 0.59320 0.59320 0.59320 -0.00000 0.00000  0.00000  224 ASP   E OD1 
13403 O OD2 . ASP   I  224 ? 0.54915 0.54915 0.54915 0.00000  -0.00000 0.00000  224 ASP   E OD2 
13404 N N   . ARG   I  225 ? 0.53978 0.53978 0.53978 0.00000  0.00000  -0.00000 225 ARG   E N   
13405 C CA  . ARG   I  225 ? 0.42166 0.42166 0.42166 -0.00000 0.00000  0.00000  225 ARG   E CA  
13406 C C   . ARG   I  225 ? 0.61288 0.61288 0.61288 0.00000  -0.00000 0.00000  225 ARG   E C   
13407 O O   . ARG   I  225 ? 0.53736 0.53736 0.53736 0.00000  0.00000  0.00000  225 ARG   E O   
13408 C CB  . ARG   I  225 ? 0.43498 0.43498 0.43498 0.00000  0.00000  0.00000  225 ARG   E CB  
13409 C CG  . ARG   I  225 ? 0.13297 0.13297 0.13297 0.00000  0.00000  0.00000  225 ARG   E CG  
13410 C CD  . ARG   I  225 ? 0.26454 0.26454 0.26454 -0.00000 0.00000  0.00000  225 ARG   E CD  
13411 N NE  . ARG   I  225 ? 0.21978 0.21978 0.21978 0.00000  0.00000  0.00000  225 ARG   E NE  
13412 C CZ  . ARG   I  225 ? 0.37396 0.37396 0.37396 0.00000  0.00000  0.00000  225 ARG   E CZ  
13413 N NH1 . ARG   I  225 ? 0.19993 0.19993 0.19993 -0.00000 0.00000  0.00000  225 ARG   E NH1 
13414 N NH2 . ARG   I  225 ? 0.29507 0.29507 0.29507 0.00000  0.00000  0.00000  225 ARG   E NH2 
13415 N N   . PRO   I  226 ? 0.54974 0.54974 0.54974 0.00000  0.00000  0.00000  226 PRO   E N   
13416 C CA  . PRO   I  226 ? 0.31926 0.31926 0.31926 0.00000  0.00000  0.00000  226 PRO   E CA  
13417 C C   . PRO   I  226 ? 0.63002 0.63002 0.63002 0.00000  0.00000  0.00000  226 PRO   E C   
13418 O O   . PRO   I  226 ? 0.41764 0.41764 0.41764 0.00000  0.00000  0.00000  226 PRO   E O   
13419 C CB  . PRO   I  226 ? 0.30805 0.30805 0.30805 -0.00000 0.00000  0.00000  226 PRO   E CB  
13420 C CG  . PRO   I  226 ? 0.29256 0.29256 0.29256 -0.00000 0.00000  0.00000  226 PRO   E CG  
13421 C CD  . PRO   I  226 ? 0.33312 0.33312 0.33312 -0.00000 0.00000  0.00000  226 PRO   E CD  
13422 N N   . VAL   I  227 ? 0.36211 0.36211 0.36211 -0.00000 0.00000  0.00000  227 VAL   E N   
13423 C CA  . VAL   I  227 ? 0.32442 0.32442 0.32442 0.00000  -0.00000 0.00000  227 VAL   E CA  
13424 C C   . VAL   I  227 ? 0.48192 0.48192 0.48192 0.00000  0.00000  0.00000  227 VAL   E C   
13425 O O   . VAL   I  227 ? 0.49446 0.49446 0.49446 -0.00000 0.00000  0.00000  227 VAL   E O   
13426 C CB  . VAL   I  227 ? 0.36459 0.36459 0.36459 -0.00000 0.00000  0.00000  227 VAL   E CB  
13427 C CG1 . VAL   I  227 ? 0.37926 0.37926 0.37926 0.00000  0.00000  0.00000  227 VAL   E CG1 
13428 C CG2 . VAL   I  227 ? 0.30410 0.30410 0.30410 0.00000  0.00000  0.00000  227 VAL   E CG2 
13429 N N   . VAL   I  228 ? 0.47586 0.47586 0.47586 0.00000  0.00000  0.00000  228 VAL   E N   
13430 C CA  . VAL   I  228 ? 0.31871 0.31871 0.31871 0.00000  0.00000  0.00000  228 VAL   E CA  
13431 C C   . VAL   I  228 ? 0.82893 0.82893 0.82893 0.00000  0.00000  0.00000  228 VAL   E C   
13432 O O   . VAL   I  228 ? 0.45241 0.45241 0.45241 0.00000  0.00000  0.00000  228 VAL   E O   
13433 C CB  . VAL   I  228 ? 0.55195 0.55195 0.55195 0.00000  0.00000  -0.00000 228 VAL   E CB  
13434 C CG1 . VAL   I  228 ? 0.37964 0.37964 0.37964 0.00000  0.00000  0.00000  228 VAL   E CG1 
13435 C CG2 . VAL   I  228 ? 0.31144 0.31144 0.31144 0.00000  0.00000  0.00000  228 VAL   E CG2 
13436 N N   . GLY   I  229 ? 0.52014 0.52014 0.52014 0.00000  0.00000  0.00000  229 GLY   E N   
13437 C CA  . GLY   I  229 ? 0.31631 0.31631 0.31631 0.00000  0.00000  0.00000  229 GLY   E CA  
13438 C C   . GLY   I  229 ? 0.40517 0.40517 0.40517 -0.00000 0.00000  0.00000  229 GLY   E C   
13439 O O   . GLY   I  229 ? 0.59771 0.59771 0.59771 0.00000  -0.00000 0.00000  229 GLY   E O   
13440 N N   . GLY   I  230 ? 0.59717 0.59717 0.59717 0.00000  0.00000  0.00000  230 GLY   E N   
13441 C CA  . GLY   I  230 ? 0.23056 0.23056 0.23056 0.00000  0.00000  0.00000  230 GLY   E CA  
13442 C C   . GLY   I  230 ? 0.83286 0.83286 0.83286 -0.00000 0.00000  0.00000  230 GLY   E C   
13443 O O   . GLY   I  230 ? 0.45300 0.45300 0.45300 -0.00000 0.00000  0.00000  230 GLY   E O   
13444 N N   . VAL   I  231 ? 0.34996 0.34996 0.34996 0.00000  0.00000  0.00000  231 VAL   E N   
13445 C CA  . VAL   I  231 ? 0.86093 0.86093 0.86093 -0.00000 0.00000  0.00000  231 VAL   E CA  
13446 C C   . VAL   I  231 ? 0.35260 0.35260 0.35260 0.00000  0.00000  0.00000  231 VAL   E C   
13447 O O   . VAL   I  231 ? 0.79731 0.79731 0.79731 -0.00000 0.00000  0.00000  231 VAL   E O   
13448 C CB  . VAL   I  231 ? 0.25886 0.25886 0.25886 -0.00000 0.00000  0.00000  231 VAL   E CB  
13449 C CG1 . VAL   I  231 ? 0.95300 0.95300 0.95300 0.00000  0.00000  0.00000  231 VAL   E CG1 
13450 C CG2 . VAL   I  231 ? 0.60532 0.60532 0.60532 0.00000  0.00000  0.00000  231 VAL   E CG2 
13451 N N   . ASN   I  232 ? 0.49369 0.49369 0.49369 -0.00000 -0.00000 0.00000  232 ASN   E N   
13452 C CA  . ASN   I  232 ? 0.35407 0.35407 0.35407 -0.00000 0.00000  0.00000  232 ASN   E CA  
13453 C C   . ASN   I  232 ? 0.50205 0.50205 0.50205 -0.00000 0.00000  0.00000  232 ASN   E C   
13454 O O   . ASN   I  232 ? 0.44135 0.44135 0.44135 -0.00000 0.00000  0.00000  232 ASN   E O   
13455 C CB  . ASN   I  232 ? 0.56614 0.56614 0.56614 0.00000  0.00000  0.00000  232 ASN   E CB  
13456 C CG  . ASN   I  232 ? 0.56134 0.56134 0.56134 -0.00000 0.00000  0.00000  232 ASN   E CG  
13457 O OD1 . ASN   I  232 ? 0.57408 0.57408 0.57408 0.00000  0.00000  0.00000  232 ASN   E OD1 
13458 N ND2 . ASN   I  232 ? 1.52557 1.52557 1.52557 0.00000  0.00000  0.00000  232 ASN   E ND2 
13459 N N   . ASN   I  233 ? 0.32329 0.32329 0.32329 0.00000  0.00000  0.00000  233 ASN   E N   
13460 C CA  . ASN   I  233 ? 0.42080 0.42080 0.42080 0.00000  0.00000  0.00000  233 ASN   E CA  
13461 C C   . ASN   I  233 ? 1.08532 1.08532 1.08532 -0.00000 0.00000  0.00000  233 ASN   E C   
13462 O O   . ASN   I  233 ? 0.39228 0.39228 0.39228 0.00000  0.00000  0.00000  233 ASN   E O   
13463 C CB  . ASN   I  233 ? 0.16640 0.16640 0.16640 0.00000  0.00000  0.00000  233 ASN   E CB  
13464 C CG  . ASN   I  233 ? 0.63995 0.63995 0.63995 -0.00000 0.00000  0.00000  233 ASN   E CG  
13465 O OD1 . ASN   I  233 ? 0.55209 0.55209 0.55209 -0.00000 0.00000  0.00000  233 ASN   E OD1 
13466 N ND2 . ASN   I  233 ? 0.49746 0.49746 0.49746 0.00000  0.00000  0.00000  233 ASN   E ND2 
13467 N N   . THR   I  234 ? 0.45316 0.45316 0.45316 0.00000  0.00000  0.00000  234 THR   E N   
13468 C CA  . THR   I  234 ? 0.64737 0.64737 0.64737 0.00000  -0.00000 0.00000  234 THR   E CA  
13469 C C   . THR   I  234 ? 0.39703 0.39703 0.39703 -0.00000 0.00000  -0.00000 234 THR   E C   
13470 O O   . THR   I  234 ? 1.03660 1.03660 1.03660 0.00000  0.00000  0.00000  234 THR   E O   
13471 C CB  . THR   I  234 ? 0.46875 0.46875 0.46875 0.00000  0.00000  0.00000  234 THR   E CB  
13472 O OG1 . THR   I  234 ? 0.59773 0.59773 0.59773 -0.00000 0.00000  0.00000  234 THR   E OG1 
13473 C CG2 . THR   I  234 ? 0.34195 0.34195 0.34195 0.00000  0.00000  0.00000  234 THR   E CG2 
13474 N N   . THR   I  235 ? 0.62482 0.62482 0.62482 0.00000  0.00000  0.00000  235 THR   E N   
13475 C CA  . THR   I  235 ? 0.39952 0.39952 0.39952 -0.00000 0.00000  0.00000  235 THR   E CA  
13476 C C   . THR   I  235 ? 0.65414 0.65414 0.65414 0.00000  0.00000  0.00000  235 THR   E C   
13477 O O   . THR   I  235 ? 0.44207 0.44207 0.44207 0.00000  0.00000  0.00000  235 THR   E O   
13478 C CB  . THR   I  235 ? 0.84470 0.84470 0.84470 0.00000  0.00000  0.00000  235 THR   E CB  
13479 O OG1 . THR   I  235 ? 0.35316 0.35316 0.35316 0.00000  0.00000  0.00000  235 THR   E OG1 
13480 C CG2 . THR   I  235 ? 0.47941 0.47941 0.47941 -0.00000 0.00000  0.00000  235 THR   E CG2 
13481 N N   . LEU   I  236 ? 0.50471 0.50471 0.50471 -0.00000 -0.00000 0.00000  236 LEU   E N   
13482 C CA  . LEU   I  236 ? 0.51068 0.51068 0.51068 0.00000  0.00000  0.00000  236 LEU   E CA  
13483 C C   . LEU   I  236 ? 0.42986 0.42986 0.42986 0.00000  0.00000  0.00000  236 LEU   E C   
13484 O O   . LEU   I  236 ? 0.45162 0.45162 0.45162 0.00000  -0.00000 0.00000  236 LEU   E O   
13485 C CB  . LEU   I  236 ? 0.42869 0.42869 0.42869 0.00000  0.00000  0.00000  236 LEU   E CB  
13486 C CG  . LEU   I  236 ? 0.52106 0.52106 0.52106 0.00000  0.00000  0.00000  236 LEU   E CG  
13487 C CD1 . LEU   I  236 ? 0.41912 0.41912 0.41912 0.00000  0.00000  0.00000  236 LEU   E CD1 
13488 C CD2 . LEU   I  236 ? 0.29849 0.29849 0.29849 -0.00000 0.00000  0.00000  236 LEU   E CD2 
13489 N N   . ILE   I  237 ? 0.48188 0.48188 0.48188 -0.00000 0.00000  0.00000  237 ILE   E N   
13490 C CA  . ILE   I  237 ? 0.39736 0.39736 0.39736 -0.00000 0.00000  0.00000  237 ILE   E CA  
13491 C C   . ILE   I  237 ? 0.53967 0.53967 0.53967 -0.00000 0.00000  0.00000  237 ILE   E C   
13492 O O   . ILE   I  237 ? 0.37405 0.37405 0.37405 0.00000  0.00000  0.00000  237 ILE   E O   
13493 C CB  . ILE   I  237 ? 0.38246 0.38246 0.38246 0.00000  0.00000  0.00000  237 ILE   E CB  
13494 C CG1 . ILE   I  237 ? 0.34348 0.34348 0.34348 0.00000  0.00000  0.00000  237 ILE   E CG1 
13495 C CG2 . ILE   I  237 ? 0.35547 0.35547 0.35547 -0.00000 0.00000  0.00000  237 ILE   E CG2 
13496 C CD1 . ILE   I  237 ? 0.36748 0.36748 0.36748 0.00000  0.00000  0.00000  237 ILE   E CD1 
13497 N N   . SER   I  238 ? 0.33839 0.33839 0.33839 0.00000  0.00000  0.00000  238 SER   E N   
13498 C CA  . SER   I  238 ? 0.42412 0.42412 0.42412 -0.00000 0.00000  0.00000  238 SER   E CA  
13499 C C   . SER   I  238 ? 0.53489 0.53489 0.53489 0.00000  0.00000  0.00000  238 SER   E C   
13500 O O   . SER   I  238 ? 0.34456 0.34456 0.34456 0.00000  0.00000  0.00000  238 SER   E O   
13501 C CB  . SER   I  238 ? 0.40465 0.40465 0.40465 0.00000  0.00000  0.00000  238 SER   E CB  
13502 O OG  . SER   I  238 ? 0.57919 0.57919 0.57919 0.00000  0.00000  0.00000  238 SER   E OG  
13503 N N   . ALA   I  239 ? 0.47615 0.47615 0.47615 -0.00000 0.00000  0.00000  239 ALA   E N   
13504 C CA  . ALA   I  239 ? 0.57817 0.57817 0.57817 -0.00000 -0.00000 0.00000  239 ALA   E CA  
13505 C C   . ALA   I  239 ? 0.27674 0.27674 0.27674 0.00000  0.00000  0.00000  239 ALA   E C   
13506 O O   . ALA   I  239 ? 0.47220 0.47220 0.47220 -0.00000 0.00000  0.00000  239 ALA   E O   
13507 C CB  . ALA   I  239 ? 0.23083 0.23083 0.23083 0.00000  0.00000  0.00000  239 ALA   E CB  
13508 N N   . ALA   I  240 ? 0.47245 0.47245 0.47245 0.00000  -0.00000 0.00000  240 ALA   E N   
13509 C CA  . ALA   I  240 ? 0.39164 0.39164 0.39164 0.00000  0.00000  0.00000  240 ALA   E CA  
13510 C C   . ALA   I  240 ? 0.47357 0.47357 0.47357 0.00000  0.00000  0.00000  240 ALA   E C   
13511 O O   . ALA   I  240 ? 0.41424 0.41424 0.41424 0.00000  0.00000  0.00000  240 ALA   E O   
13512 C CB  . ALA   I  240 ? 0.28690 0.28690 0.28690 0.00000  0.00000  0.00000  240 ALA   E CB  
13513 N N   . CYS   I  241 ? 0.25569 0.25569 0.25569 0.00000  0.00000  0.00000  241 CYS   E N   
13514 C CA  . CYS   I  241 ? 0.38115 0.38115 0.38115 0.00000  0.00000  0.00000  241 CYS   E CA  
13515 C C   . CYS   I  241 ? 0.38508 0.38508 0.38508 -0.00000 0.00000  0.00000  241 CYS   E C   
13516 O O   . CYS   I  241 ? 0.37244 0.37244 0.37244 0.00000  0.00000  0.00000  241 CYS   E O   
13517 C CB  . CYS   I  241 ? 0.40189 0.40189 0.40189 0.00000  -0.00000 0.00000  241 CYS   E CB  
13518 S SG  . CYS   I  241 ? 0.40514 0.40514 0.40514 0.00000  0.00000  0.00000  241 CYS   E SG  
13519 N N   . GLU   I  242 ? 0.48424 0.48424 0.48424 0.00000  0.00000  0.00000  242 GLU   E N   
13520 C CA  . GLU   I  242 ? 0.27739 0.27739 0.27739 -0.00000 0.00000  0.00000  242 GLU   E CA  
13521 C C   . GLU   I  242 ? 0.31414 0.31414 0.31414 0.00000  -0.00000 0.00000  242 GLU   E C   
13522 O O   . GLU   I  242 ? 0.60013 0.60013 0.60013 -0.00000 0.00000  0.00000  242 GLU   E O   
13523 C CB  . GLU   I  242 ? 0.41520 0.41520 0.41520 -0.00000 0.00000  0.00000  242 GLU   E CB  
13524 C CG  . GLU   I  242 ? 0.34342 0.34342 0.34342 0.00000  0.00000  0.00000  242 GLU   E CG  
13525 C CD  . GLU   I  242 ? 0.64745 0.64745 0.64745 0.00000  0.00000  0.00000  242 GLU   E CD  
13526 O OE1 . GLU   I  242 ? 0.38751 0.38751 0.38751 0.00000  0.00000  0.00000  242 GLU   E OE1 
13527 O OE2 . GLU   I  242 ? 0.47040 0.47040 0.47040 -0.00000 0.00000  0.00000  242 GLU   E OE2 
13528 N N   . SER   I  243 ? 0.39220 0.39220 0.39220 -0.00000 0.00000  0.00000  243 SER   E N   
13529 C CA  . SER   I  243 ? 0.53764 0.53764 0.53764 0.00000  0.00000  0.00000  243 SER   E CA  
13530 C C   . SER   I  243 ? 0.41393 0.41393 0.41393 0.00000  0.00000  0.00000  243 SER   E C   
13531 O O   . SER   I  243 ? 0.47098 0.47098 0.47098 0.00000  0.00000  0.00000  243 SER   E O   
13532 C CB  . SER   I  243 ? 0.40124 0.40124 0.40124 -0.00000 0.00000  0.00000  243 SER   E CB  
13533 O OG  . SER   I  243 ? 0.49618 0.49618 0.49618 0.00000  0.00000  0.00000  243 SER   E OG  
13534 N N   . LEU   I  244 ? 0.42553 0.42553 0.42553 0.00000  0.00000  0.00000  244 LEU   E N   
13535 C CA  . LEU   I  244 ? 0.49563 0.49563 0.49563 -0.00000 0.00000  0.00000  244 LEU   E CA  
13536 C C   . LEU   I  244 ? 0.46401 0.46401 0.46401 0.00000  0.00000  0.00000  244 LEU   E C   
13537 O O   . LEU   I  244 ? 0.54356 0.54356 0.54356 0.00000  0.00000  0.00000  244 LEU   E O   
13538 C CB  . LEU   I  244 ? 0.30398 0.30398 0.30398 -0.00000 0.00000  0.00000  244 LEU   E CB  
13539 C CG  . LEU   I  244 ? 0.53750 0.53750 0.53750 -0.00000 0.00000  0.00000  244 LEU   E CG  
13540 C CD1 . LEU   I  244 ? 0.46101 0.46101 0.46101 0.00000  0.00000  0.00000  244 LEU   E CD1 
13541 C CD2 . LEU   I  244 ? 0.37525 0.37525 0.37525 -0.00000 0.00000  0.00000  244 LEU   E CD2 
13542 N N   . SER   I  245 ? 0.85406 0.85406 0.85406 0.00000  0.00000  0.00000  245 SER   E N   
13543 C CA  . SER   I  245 ? 0.35533 0.35533 0.35533 -0.00000 0.00000  0.00000  245 SER   E CA  
13544 C C   . SER   I  245 ? 0.35590 0.35590 0.35590 0.00000  0.00000  0.00000  245 SER   E C   
13545 O O   . SER   I  245 ? 0.46942 0.46942 0.46942 0.00000  0.00000  0.00000  245 SER   E O   
13546 C CB  . SER   I  245 ? 0.39003 0.39003 0.39003 0.00000  -0.00000 0.00000  245 SER   E CB  
13547 O OG  . SER   I  245 ? 0.96722 0.96722 0.96722 0.00000  -0.00000 0.00000  245 SER   E OG  
13548 N N   . TYR   I  246 ? 0.50676 0.50676 0.50676 0.00000  0.00000  0.00000  246 TYR   E N   
13549 C CA  . TYR   I  246 ? 0.38184 0.38184 0.38184 -0.00000 0.00000  0.00000  246 TYR   E CA  
13550 C C   . TYR   I  246 ? 0.40229 0.40229 0.40229 0.00000  0.00000  0.00000  246 TYR   E C   
13551 O O   . TYR   I  246 ? 0.44105 0.44105 0.44105 0.00000  0.00000  0.00000  246 TYR   E O   
13552 C CB  . TYR   I  246 ? 0.25990 0.25990 0.25990 0.00000  0.00000  0.00000  246 TYR   E CB  
13553 C CG  . TYR   I  246 ? 0.46484 0.46484 0.46484 0.00000  0.00000  0.00000  246 TYR   E CG  
13554 C CD1 . TYR   I  246 ? 0.37751 0.37751 0.37751 0.00000  0.00000  0.00000  246 TYR   E CD1 
13555 C CD2 . TYR   I  246 ? 0.20157 0.20157 0.20157 0.00000  0.00000  0.00000  246 TYR   E CD2 
13556 C CE1 . TYR   I  246 ? 0.29820 0.29820 0.29820 -0.00000 0.00000  0.00000  246 TYR   E CE1 
13557 C CE2 . TYR   I  246 ? 0.53457 0.53457 0.53457 -0.00000 0.00000  0.00000  246 TYR   E CE2 
13558 C CZ  . TYR   I  246 ? 0.42083 0.42083 0.42083 0.00000  0.00000  0.00000  246 TYR   E CZ  
13559 O OH  . TYR   I  246 ? 0.62471 0.62471 0.62471 0.00000  0.00000  0.00000  246 TYR   E OH  
13560 N N   . ASN   I  247 ? 0.36443 0.36443 0.36443 -0.00000 0.00000  0.00000  247 ASN   E N   
13561 C CA  . ASN   I  247 ? 0.26797 0.26797 0.26797 0.00000  0.00000  0.00000  247 ASN   E CA  
13562 C C   . ASN   I  247 ? 0.35758 0.35758 0.35758 0.00000  -0.00000 0.00000  247 ASN   E C   
13563 O O   . ASN   I  247 ? 0.39855 0.39855 0.39855 -0.00000 0.00000  0.00000  247 ASN   E O   
13564 C CB  . ASN   I  247 ? 0.39764 0.39764 0.39764 -0.00000 0.00000  0.00000  247 ASN   E CB  
13565 C CG  . ASN   I  247 ? 0.36787 0.36787 0.36787 0.00000  -0.00000 0.00000  247 ASN   E CG  
13566 O OD1 . ASN   I  247 ? 0.58923 0.58923 0.58923 0.00000  0.00000  0.00000  247 ASN   E OD1 
13567 N ND2 . ASN   I  247 ? 0.34813 0.34813 0.34813 0.00000  0.00000  0.00000  247 ASN   E ND2 
13568 N N   . VAL   I  248 ? 0.41094 0.41094 0.41094 0.00000  -0.00000 0.00000  248 VAL   E N   
13569 C CA  . VAL   I  248 ? 0.48429 0.48429 0.48429 -0.00000 0.00000  0.00000  248 VAL   E CA  
13570 C C   . VAL   I  248 ? 0.37708 0.37708 0.37708 0.00000  0.00000  0.00000  248 VAL   E C   
13571 O O   . VAL   I  248 ? 0.47218 0.47218 0.47218 -0.00000 0.00000  0.00000  248 VAL   E O   
13572 C CB  . VAL   I  248 ? 0.42792 0.42792 0.42792 0.00000  0.00000  0.00000  248 VAL   E CB  
13573 C CG1 . VAL   I  248 ? 0.33668 0.33668 0.33668 0.00000  0.00000  0.00000  248 VAL   E CG1 
13574 C CG2 . VAL   I  248 ? 0.40381 0.40381 0.40381 0.00000  0.00000  0.00000  248 VAL   E CG2 
13575 N N   . SER   I  249 ? 0.54727 0.54727 0.54727 -0.00000 0.00000  0.00000  249 SER   E N   
13576 C CA  . SER   I  249 ? 0.38733 0.38733 0.38733 0.00000  0.00000  0.00000  249 SER   E CA  
13577 C C   . SER   I  249 ? 0.54665 0.54665 0.54665 0.00000  0.00000  0.00000  249 SER   E C   
13578 O O   . SER   I  249 ? 0.41749 0.41749 0.41749 0.00000  0.00000  0.00000  249 SER   E O   
13579 C CB  . SER   I  249 ? 0.38211 0.38211 0.38211 -0.00000 0.00000  0.00000  249 SER   E CB  
13580 O OG  . SER   I  249 ? 0.45422 0.45422 0.45422 -0.00000 -0.00000 0.00000  249 SER   E OG  
13581 N N   . TYR   I  250 ? 0.37356 0.37356 0.37356 -0.00000 0.00000  0.00000  250 TYR   E N   
13582 C CA  . TYR   I  250 ? 0.70471 0.70471 0.70471 -0.00000 0.00000  0.00000  250 TYR   E CA  
13583 C C   . TYR   I  250 ? 0.34064 0.34064 0.34064 0.00000  0.00000  0.00000  250 TYR   E C   
13584 O O   . TYR   I  250 ? 0.45599 0.45599 0.45599 0.00000  0.00000  0.00000  250 TYR   E O   
13585 C CB  . TYR   I  250 ? 0.33344 0.33344 0.33344 -0.00000 0.00000  0.00000  250 TYR   E CB  
13586 C CG  . TYR   I  250 ? 0.53020 0.53020 0.53020 0.00000  0.00000  0.00000  250 TYR   E CG  
13587 C CD1 . TYR   I  250 ? 0.35770 0.35770 0.35770 0.00000  0.00000  0.00000  250 TYR   E CD1 
13588 C CD2 . TYR   I  250 ? 0.30854 0.30854 0.30854 0.00000  0.00000  0.00000  250 TYR   E CD2 
13589 C CE1 . TYR   I  250 ? 0.50779 0.50779 0.50779 0.00000  0.00000  0.00000  250 TYR   E CE1 
13590 C CE2 . TYR   I  250 ? 0.44890 0.44890 0.44890 0.00000  0.00000  0.00000  250 TYR   E CE2 
13591 C CZ  . TYR   I  250 ? 0.59969 0.59969 0.59969 0.00000  -0.00000 0.00000  250 TYR   E CZ  
13592 O OH  . TYR   I  250 ? 0.66959 0.66959 0.66959 -0.00000 0.00000  0.00000  250 TYR   E OH  
13593 N N   . ASP   I  251 ? 0.49036 0.49036 0.49036 0.00000  0.00000  0.00000  251 ASP   E N   
13594 C CA  . ASP   I  251 ? 0.49363 0.49363 0.49363 0.00000  0.00000  0.00000  251 ASP   E CA  
13595 C C   . ASP   I  251 ? 0.72988 0.72988 0.72988 0.00000  0.00000  0.00000  251 ASP   E C   
13596 O O   . ASP   I  251 ? 0.53821 0.53821 0.53821 0.00000  0.00000  0.00000  251 ASP   E O   
13597 C CB  . ASP   I  251 ? 0.48515 0.48515 0.48515 0.00000  0.00000  0.00000  251 ASP   E CB  
13598 C CG  . ASP   I  251 ? 0.76645 0.76645 0.76645 0.00000  0.00000  0.00000  251 ASP   E CG  
13599 O OD1 . ASP   I  251 ? 0.59462 0.59462 0.59462 0.00000  0.00000  0.00000  251 ASP   E OD1 
13600 O OD2 . ASP   I  251 ? 0.58883 0.58883 0.58883 0.00000  0.00000  0.00000  251 ASP   E OD2 
13601 N N   . VAL   I  252 ? 0.54812 0.54812 0.54812 0.00000  0.00000  0.00000  252 VAL   E N   
13602 C CA  . VAL   I  252 ? 0.57712 0.57712 0.57712 -0.00000 0.00000  0.00000  252 VAL   E CA  
13603 C C   . VAL   I  252 ? 0.58935 0.58935 0.58935 -0.00000 0.00000  0.00000  252 VAL   E C   
13604 O O   . VAL   I  252 ? 0.61029 0.61029 0.61029 0.00000  0.00000  0.00000  252 VAL   E O   
13605 C CB  . VAL   I  252 ? 0.61318 0.61318 0.61318 0.00000  0.00000  0.00000  252 VAL   E CB  
13606 C CG1 . VAL   I  252 ? 0.46114 0.46114 0.46114 0.00000  0.00000  0.00000  252 VAL   E CG1 
13607 C CG2 . VAL   I  252 ? 0.46608 0.46608 0.46608 0.00000  0.00000  0.00000  252 VAL   E CG2 
13608 N N   . GLN   I  253 ? 0.57124 0.57124 0.57124 0.00000  0.00000  0.00000  253 GLN   E N   
13609 C CA  . GLN   I  253 ? 0.64428 0.64428 0.64428 0.00000  0.00000  0.00000  253 GLN   E CA  
13610 C C   . GLN   I  253 ? 0.79444 0.79444 0.79444 -0.00000 0.00000  0.00000  253 GLN   E C   
13611 O O   . GLN   I  253 ? 0.63524 0.63524 0.63524 -0.00000 0.00000  0.00000  253 GLN   E O   
13612 C CB  . GLN   I  253 ? 0.50028 0.50028 0.50028 -0.00000 0.00000  0.00000  253 GLN   E CB  
13613 C CG  . GLN   I  253 ? 0.97619 0.97619 0.97619 -0.00000 0.00000  0.00000  253 GLN   E CG  
13614 C CD  . GLN   I  253 ? 0.86554 0.86554 0.86554 -0.00000 0.00000  0.00000  253 GLN   E CD  
13615 O OE1 . GLN   I  253 ? 0.87670 0.87670 0.87670 0.00000  -0.00000 -0.00000 253 GLN   E OE1 
13616 N NE2 . GLN   I  253 ? 0.96826 0.96826 0.96826 0.00000  0.00000  0.00000  253 GLN   E NE2 
13617 N N   . SER   I  254 ? 0.78895 0.78895 0.78895 -0.00000 0.00000  0.00000  254 SER   E N   
13618 C CA  . SER   I  254 ? 0.53496 0.53496 0.53496 -0.00000 0.00000  0.00000  254 SER   E CA  
13619 C C   . SER   I  254 ? 0.56143 0.56143 0.56143 0.00000  0.00000  0.00000  254 SER   E C   
13620 O O   . SER   I  254 ? 0.71034 0.71034 0.71034 0.00000  0.00000  0.00000  254 SER   E O   
13621 C CB  . SER   I  254 ? 0.67132 0.67132 0.67132 -0.00000 0.00000  0.00000  254 SER   E CB  
13622 O OG  . SER   I  254 ? 0.56458 0.56458 0.56458 0.00000  0.00000  0.00000  254 SER   E OG  
13623 N N   . LEU   I  255 ? 0.54935 0.54935 0.54935 -0.00000 0.00000  0.00000  255 LEU   E N   
13624 C CA  . LEU   I  255 ? 0.57926 0.57926 0.57926 0.00000  0.00000  0.00000  255 LEU   E CA  
13625 C C   . LEU   I  255 ? 0.59876 0.59876 0.59876 0.00000  0.00000  0.00000  255 LEU   E C   
13626 O O   . LEU   I  255 ? 0.61457 0.61457 0.61457 0.00000  0.00000  0.00000  255 LEU   E O   
13627 C CB  . LEU   I  255 ? 0.61369 0.61369 0.61369 -0.00000 0.00000  0.00000  255 LEU   E CB  
13628 C CG  . LEU   I  255 ? 0.62980 0.62980 0.62980 -0.00000 0.00000  0.00000  255 LEU   E CG  
13629 C CD1 . LEU   I  255 ? 0.61443 0.61443 0.61443 -0.00000 0.00000  0.00000  255 LEU   E CD1 
13630 C CD2 . LEU   I  255 ? 0.48563 0.48563 0.48563 0.00000  0.00000  0.00000  255 LEU   E CD2 
13631 N N   . ASP   I  256 ? 0.58980 0.58980 0.58980 0.00000  0.00000  0.00000  256 ASP   E N   
13632 C CA  . ASP   I  256 ? 0.40455 0.40455 0.40455 0.00000  -0.00000 0.00000  256 ASP   E CA  
13633 C C   . ASP   I  256 ? 0.68997 0.68997 0.68997 0.00000  0.00000  0.00000  256 ASP   E C   
13634 O O   . ASP   I  256 ? 0.43670 0.43670 0.43670 0.00000  0.00000  0.00000  256 ASP   E O   
13635 C CB  . ASP   I  256 ? 0.53152 0.53152 0.53152 0.00000  0.00000  0.00000  256 ASP   E CB  
13636 C CG  . ASP   I  256 ? 0.86998 0.86998 0.86998 0.00000  0.00000  0.00000  256 ASP   E CG  
13637 O OD1 . ASP   I  256 ? 0.53828 0.53828 0.53828 -0.00000 0.00000  -0.00000 256 ASP   E OD1 
13638 O OD2 . ASP   I  256 ? 0.54690 0.54690 0.54690 -0.00000 0.00000  0.00000  256 ASP   E OD2 
13639 N N   . THR   I  257 ? 0.59209 0.59209 0.59209 0.00000  0.00000  0.00000  257 THR   E N   
13640 C CA  . THR   I  257 ? 0.94913 0.94913 0.94913 0.00000  0.00000  0.00000  257 THR   E CA  
13641 C C   . THR   I  257 ? 0.52000 0.52000 0.52000 0.00000  0.00000  0.00000  257 THR   E C   
13642 O O   . THR   I  257 ? 0.79836 0.79836 0.79836 0.00000  0.00000  0.00000  257 THR   E O   
13643 C CB  . THR   I  257 ? 0.60909 0.60909 0.60909 0.00000  0.00000  0.00000  257 THR   E CB  
13644 O OG1 . THR   I  257 ? 0.89675 0.89675 0.89675 0.00000  0.00000  0.00000  257 THR   E OG1 
13645 C CG2 . THR   I  257 ? 0.75583 0.75583 0.75583 -0.00000 0.00000  0.00000  257 THR   E CG2 
13646 N N   . LEU   I  258 ? 0.82426 0.82426 0.82426 -0.00000 0.00000  0.00000  258 LEU   E N   
13647 C CA  . LEU   I  258 ? 0.63992 0.63992 0.63992 0.00000  0.00000  0.00000  258 LEU   E CA  
13648 C C   . LEU   I  258 ? 0.98489 0.98489 0.98489 -0.00000 0.00000  0.00000  258 LEU   E C   
13649 O O   . LEU   I  258 ? 1.02680 1.02680 1.02680 0.00000  0.00000  0.00000  258 LEU   E O   
13650 C CB  . LEU   I  258 ? 0.64157 0.64157 0.64157 -0.00000 0.00000  0.00000  258 LEU   E CB  
13651 C CG  . LEU   I  258 ? 0.58911 0.58911 0.58911 -0.00000 0.00000  0.00000  258 LEU   E CG  
13652 C CD1 . LEU   I  258 ? 0.68017 0.68017 0.68017 0.00000  0.00000  0.00000  258 LEU   E CD1 
13653 C CD2 . LEU   I  258 ? 0.54368 0.54368 0.54368 -0.00000 0.00000  0.00000  258 LEU   E CD2 
13654 N N   . VAL   I  259 ? 0.86098 0.86098 0.86098 -0.00000 0.00000  0.00000  259 VAL   E N   
13655 C CA  . VAL   I  259 ? 0.90325 0.90325 0.90325 -0.00000 0.00000  0.00000  259 VAL   E CA  
13656 C C   . VAL   I  259 ? 1.71570 1.71570 1.71570 -0.00000 0.00000  0.00000  259 VAL   E C   
13657 O O   . VAL   I  259 ? 0.84823 0.84823 0.84823 0.00000  0.00000  0.00000  259 VAL   E O   
13658 C CB  . VAL   I  259 ? 1.15249 1.15249 1.15249 -0.00000 0.00000  0.00000  259 VAL   E CB  
13659 C CG1 . VAL   I  259 ? 0.67284 0.67284 0.67284 0.00000  -0.00000 0.00000  259 VAL   E CG1 
13660 C CG2 . VAL   I  259 ? 0.98158 0.98158 0.98158 0.00000  0.00000  0.00000  259 VAL   E CG2 
13661 N N   . PHE   I  260 ? 0.94136 0.94136 0.94136 -0.00000 0.00000  0.00000  260 PHE   E N   
13662 C CA  . PHE   I  260 ? 1.70802 1.70802 1.70802 0.00000  0.00000  0.00000  260 PHE   E CA  
13663 C C   . PHE   I  260 ? 1.16441 1.16441 1.16441 -0.00000 0.00000  0.00000  260 PHE   E C   
13664 O O   . PHE   I  260 ? 2.13124 2.13124 2.13124 0.00000  0.00000  0.00000  260 PHE   E O   
13665 C CB  . PHE   I  260 ? 1.10742 1.10742 1.10742 0.00000  0.00000  0.00000  260 PHE   E CB  
13666 C CG  . PHE   I  260 ? 1.33191 1.33191 1.33191 0.00000  0.00000  0.00000  260 PHE   E CG  
13667 C CD1 . PHE   I  260 ? 1.04755 1.04755 1.04755 0.00000  -0.00000 0.00000  260 PHE   E CD1 
13668 C CD2 . PHE   I  260 ? 1.24538 1.24538 1.24538 0.00000  0.00000  0.00000  260 PHE   E CD2 
13669 C CE1 . PHE   I  260 ? 2.30157 2.30157 2.30157 0.00000  0.00000  0.00000  260 PHE   E CE1 
13670 C CE2 . PHE   I  260 ? 1.26492 1.26492 1.26492 0.00000  0.00000  0.00000  260 PHE   E CE2 
13671 C CZ  . PHE   I  260 ? 1.47620 1.47620 1.47620 0.00000  0.00000  0.00000  260 PHE   E CZ  
13672 N N   . LYS   I  261 ? 1.54800 1.54800 1.54800 -0.00000 0.00000  0.00000  261 LYS   E N   
13673 C CA  . LYS   I  261 ? 1.50245 1.50245 1.50245 0.00000  0.00000  0.00000  261 LYS   E CA  
13674 C C   . LYS   I  261 ? 1.65957 1.65957 1.65957 0.00000  -0.00000 0.00000  261 LYS   E C   
13675 O O   . LYS   I  261 ? 1.69304 1.69304 1.69304 -0.00000 0.00000  0.00000  261 LYS   E O   
13676 C CB  . LYS   I  261 ? 0.63608 0.63608 0.63608 0.00000  0.00000  0.00000  261 LYS   E CB  
13677 C CG  . LYS   I  261 ? 1.64381 1.64381 1.64381 -0.00000 0.00000  0.00000  261 LYS   E CG  
13678 C CD  . LYS   I  261 ? 1.78666 1.78666 1.78666 -0.00000 -0.00000 -0.00000 261 LYS   E CD  
13679 C CE  . LYS   I  261 ? 0.55359 0.55359 0.55359 0.00000  0.00000  0.00000  261 LYS   E CE  
13680 N NZ  . LYS   I  261 ? 0.30175 0.30175 0.30175 0.00000  0.00000  0.00000  261 LYS   E NZ  
13681 N N   . GLY   I  262 ? 1.29264 1.29264 1.29264 0.00000  0.00000  0.00000  262 GLY   E N   
13682 C CA  . GLY   I  262 ? 0.59091 0.59091 0.59091 0.00000  0.00000  0.00000  262 GLY   E CA  
13683 C C   . GLY   I  262 ? 1.31107 1.31107 1.31107 0.00000  0.00000  0.00000  262 GLY   E C   
13684 O O   . GLY   I  262 ? 1.22652 1.22652 1.22652 -0.00000 0.00000  0.00000  262 GLY   E O   
13685 N N   . GLU   I  263 ? 0.66668 0.66668 0.66668 0.00000  0.00000  0.00000  263 GLU   E N   
13686 C CA  . GLU   I  263 ? 1.10239 1.10239 1.10239 0.00000  -0.00000 0.00000  263 GLU   E CA  
13687 C C   . GLU   I  263 ? 1.23038 1.23038 1.23038 0.00000  0.00000  0.00000  263 GLU   E C   
13688 O O   . GLU   I  263 ? 0.78496 0.78496 0.78496 0.00000  0.00000  0.00000  263 GLU   E O   
13689 C CB  . GLU   I  263 ? 0.64670 0.64670 0.64670 0.00000  0.00000  0.00000  263 GLU   E CB  
13690 C CG  . GLU   I  263 ? 1.09797 1.09797 1.09797 -0.00000 0.00000  0.00000  263 GLU   E CG  
13691 C CD  . GLU   I  263 ? 1.01247 1.01247 1.01247 0.00000  0.00000  0.00000  263 GLU   E CD  
13692 O OE1 . GLU   I  263 ? 0.63691 0.63691 0.63691 0.00000  0.00000  0.00000  263 GLU   E OE1 
13693 O OE2 . GLU   I  263 ? 0.81211 0.81211 0.81211 0.00000  0.00000  0.00000  263 GLU   E OE2 
13694 N N   . THR   I  264 ? 0.64747 0.64747 0.64747 -0.00000 0.00000  0.00000  264 THR   E N   
13695 C CA  . THR   I  264 ? 0.46419 0.46419 0.46419 0.00000  0.00000  0.00000  264 THR   E CA  
13696 C C   . THR   I  264 ? 0.65732 0.65732 0.65732 0.00000  0.00000  0.00000  264 THR   E C   
13697 O O   . THR   I  264 ? 0.54435 0.54435 0.54435 -0.00000 0.00000  0.00000  264 THR   E O   
13698 C CB  . THR   I  264 ? 0.72821 0.72821 0.72821 0.00000  0.00000  0.00000  264 THR   E CB  
13699 O OG1 . THR   I  264 ? 1.37503 1.37503 1.37503 -0.00000 0.00000  0.00000  264 THR   E OG1 
13700 C CG2 . THR   I  264 ? 0.56341 0.56341 0.56341 -0.00000 0.00000  0.00000  264 THR   E CG2 
13701 N N   . TYR   I  265 ? 0.45048 0.45048 0.45048 0.00000  0.00000  0.00000  265 TYR   E N   
13702 C CA  . TYR   I  265 ? 0.33034 0.33034 0.33034 0.00000  0.00000  0.00000  265 TYR   E CA  
13703 C C   . TYR   I  265 ? 0.39162 0.39162 0.39162 -0.00000 0.00000  0.00000  265 TYR   E C   
13704 O O   . TYR   I  265 ? 0.49319 0.49319 0.49319 -0.00000 0.00000  0.00000  265 TYR   E O   
13705 C CB  . TYR   I  265 ? 0.28062 0.28062 0.28062 -0.00000 0.00000  0.00000  265 TYR   E CB  
13706 C CG  . TYR   I  265 ? 0.51946 0.51946 0.51946 -0.00000 0.00000  0.00000  265 TYR   E CG  
13707 C CD1 . TYR   I  265 ? 0.40991 0.40991 0.40991 -0.00000 0.00000  0.00000  265 TYR   E CD1 
13708 C CD2 . TYR   I  265 ? 0.37904 0.37904 0.37904 -0.00000 0.00000  0.00000  265 TYR   E CD2 
13709 C CE1 . TYR   I  265 ? 0.51010 0.51010 0.51010 0.00000  0.00000  0.00000  265 TYR   E CE1 
13710 C CE2 . TYR   I  265 ? 0.48774 0.48774 0.48774 -0.00000 0.00000  0.00000  265 TYR   E CE2 
13711 C CZ  . TYR   I  265 ? 0.41062 0.41062 0.41062 0.00000  0.00000  0.00000  265 TYR   E CZ  
13712 O OH  . TYR   I  265 ? 0.45281 0.45281 0.45281 0.00000  0.00000  0.00000  265 TYR   E OH  
13713 N N   . SER   I  266 ? 0.48051 0.48051 0.48051 0.00000  0.00000  0.00000  266 SER   E N   
13714 C CA  . SER   I  266 ? 0.34193 0.34193 0.34193 -0.00000 0.00000  0.00000  266 SER   E CA  
13715 C C   . SER   I  266 ? 0.51302 0.51302 0.51302 0.00000  0.00000  0.00000  266 SER   E C   
13716 O O   . SER   I  266 ? 0.39322 0.39322 0.39322 0.00000  0.00000  0.00000  266 SER   E O   
13717 C CB  . SER   I  266 ? 0.36424 0.36424 0.36424 -0.00000 0.00000  0.00000  266 SER   E CB  
13718 O OG  . SER   I  266 ? 0.49786 0.49786 0.49786 0.00000  0.00000  0.00000  266 SER   E OG  
13719 N N   . LEU   I  267 ? 0.42181 0.42181 0.42181 0.00000  -0.00000 0.00000  267 LEU   E N   
13720 C CA  . LEU   I  267 ? 0.54322 0.54322 0.54322 -0.00000 0.00000  0.00000  267 LEU   E CA  
13721 C C   . LEU   I  267 ? 0.41376 0.41376 0.41376 0.00000  0.00000  0.00000  267 LEU   E C   
13722 O O   . LEU   I  267 ? 0.61129 0.61129 0.61129 0.00000  0.00000  0.00000  267 LEU   E O   
13723 C CB  . LEU   I  267 ? 0.33371 0.33371 0.33371 -0.00000 0.00000  0.00000  267 LEU   E CB  
13724 C CG  . LEU   I  267 ? 0.58195 0.58195 0.58195 0.00000  0.00000  0.00000  267 LEU   E CG  
13725 C CD1 . LEU   I  267 ? 0.48160 0.48160 0.48160 -0.00000 0.00000  0.00000  267 LEU   E CD1 
13726 C CD2 . LEU   I  267 ? 0.40922 0.40922 0.40922 -0.00000 0.00000  0.00000  267 LEU   E CD2 
13727 N N   . LYS   I  268 ? 0.66154 0.66154 0.66154 -0.00000 0.00000  0.00000  268 LYS   E N   
13728 C CA  . LYS   I  268 ? 0.39375 0.39375 0.39375 0.00000  0.00000  0.00000  268 LYS   E CA  
13729 C C   . LYS   I  268 ? 0.63353 0.63353 0.63353 0.00000  0.00000  0.00000  268 LYS   E C   
13730 O O   . LYS   I  268 ? 0.36909 0.36909 0.36909 0.00000  0.00000  0.00000  268 LYS   E O   
13731 C CB  . LYS   I  268 ? 0.47489 0.47489 0.47489 0.00000  0.00000  0.00000  268 LYS   E CB  
13732 C CG  . LYS   I  268 ? 0.63846 0.63846 0.63846 0.00000  0.00000  0.00000  268 LYS   E CG  
13733 C CD  . LYS   I  268 ? 0.55742 0.55742 0.55742 0.00000  0.00000  0.00000  268 LYS   E CD  
13734 C CE  . LYS   I  268 ? 0.71679 0.71679 0.71679 -0.00000 0.00000  0.00000  268 LYS   E CE  
13735 N NZ  . LYS   I  268 ? 0.67603 0.67603 0.67603 -0.00000 0.00000  0.00000  268 LYS   E NZ  
13736 N N   . HIS   I  269 ? 0.47865 0.47865 0.47865 -0.00000 0.00000  0.00000  269 HIS   E N   
13737 C CA  . HIS   I  269 ? 0.28237 0.28237 0.28237 0.00000  0.00000  0.00000  269 HIS   E CA  
13738 C C   . HIS   I  269 ? 0.59813 0.59813 0.59813 -0.00000 0.00000  0.00000  269 HIS   E C   
13739 O O   . HIS   I  269 ? 0.37948 0.37948 0.37948 0.00000  0.00000  0.00000  269 HIS   E O   
13740 C CB  . HIS   I  269 ? 0.37942 0.37942 0.37942 0.00000  0.00000  0.00000  269 HIS   E CB  
13741 C CG  . HIS   I  269 ? 0.43067 0.43067 0.43067 0.00000  -0.00000 -0.00000 269 HIS   E CG  
13742 N ND1 . HIS   I  269 ? 0.70125 0.70125 0.70125 0.00000  0.00000  0.00000  269 HIS   E ND1 
13743 C CD2 . HIS   I  269 ? 0.52281 0.52281 0.52281 0.00000  0.00000  0.00000  269 HIS   E CD2 
13744 C CE1 . HIS   I  269 ? 0.38743 0.38743 0.38743 -0.00000 0.00000  0.00000  269 HIS   E CE1 
13745 N NE2 . HIS   I  269 ? 0.58434 0.58434 0.58434 -0.00000 0.00000  0.00000  269 HIS   E NE2 
13746 N N   . LEU   I  270 ? 0.35132 0.35132 0.35132 0.00000  0.00000  0.00000  270 LEU   E N   
13747 C CA  . LEU   I  270 ? 0.29123 0.29123 0.29123 -0.00000 0.00000  0.00000  270 LEU   E CA  
13748 C C   . LEU   I  270 ? 0.33793 0.33793 0.33793 0.00000  0.00000  0.00000  270 LEU   E C   
13749 O O   . LEU   I  270 ? 0.38297 0.38297 0.38297 -0.00000 0.00000  0.00000  270 LEU   E O   
13750 C CB  . LEU   I  270 ? 0.37635 0.37635 0.37635 0.00000  0.00000  0.00000  270 LEU   E CB  
13751 C CG  . LEU   I  270 ? 0.33915 0.33915 0.33915 0.00000  0.00000  0.00000  270 LEU   E CG  
13752 C CD1 . LEU   I  270 ? 0.31046 0.31046 0.31046 -0.00000 -0.00000 0.00000  270 LEU   E CD1 
13753 C CD2 . LEU   I  270 ? 0.41172 0.41172 0.41172 -0.00000 0.00000  0.00000  270 LEU   E CD2 
13754 N N   . LEU   I  271 ? 0.40248 0.40248 0.40248 0.00000  0.00000  0.00000  271 LEU   E N   
13755 C CA  . LEU   I  271 ? 0.35976 0.35976 0.35976 0.00000  -0.00000 0.00000  271 LEU   E CA  
13756 C C   . LEU   I  271 ? 0.46656 0.46656 0.46656 -0.00000 0.00000  0.00000  271 LEU   E C   
13757 O O   . LEU   I  271 ? 0.33436 0.33436 0.33436 0.00000  0.00000  0.00000  271 LEU   E O   
13758 C CB  . LEU   I  271 ? 0.23897 0.23897 0.23897 -0.00000 0.00000  0.00000  271 LEU   E CB  
13759 C CG  . LEU   I  271 ? 0.40475 0.40475 0.40475 -0.00000 0.00000  0.00000  271 LEU   E CG  
13760 C CD1 . LEU   I  271 ? 0.29224 0.29224 0.29224 0.00000  0.00000  0.00000  271 LEU   E CD1 
13761 C CD2 . LEU   I  271 ? 0.21025 0.21025 0.21025 -0.00000 0.00000  0.00000  271 LEU   E CD2 
13762 N N   . ASN   I  272 ? 0.37468 0.37468 0.37468 0.00000  0.00000  0.00000  272 ASN   E N   
13763 C CA  . ASN   I  272 ? 0.27337 0.27337 0.27337 0.00000  0.00000  0.00000  272 ASN   E CA  
13764 C C   . ASN   I  272 ? 0.42708 0.42708 0.42708 0.00000  0.00000  0.00000  272 ASN   E C   
13765 O O   . ASN   I  272 ? 0.51313 0.51313 0.51313 0.00000  0.00000  0.00000  272 ASN   E O   
13766 C CB  . ASN   I  272 ? 0.55086 0.55086 0.55086 -0.00000 0.00000  0.00000  272 ASN   E CB  
13767 C CG  . ASN   I  272 ? 0.43043 0.43043 0.43043 0.00000  0.00000  0.00000  272 ASN   E CG  
13768 O OD1 . ASN   I  272 ? 0.42794 0.42794 0.42794 0.00000  0.00000  0.00000  272 ASN   E OD1 
13769 N ND2 . ASN   I  272 ? 0.50935 0.50935 0.50935 0.00000  -0.00000 0.00000  272 ASN   E ND2 
13770 N N   . ASN   I  273 ? 0.40415 0.40415 0.40415 0.00000  -0.00000 0.00000  273 ASN   E N   
13771 C CA  . ASN   I  273 ? 0.51948 0.51948 0.51948 0.00000  0.00000  0.00000  273 ASN   E CA  
13772 C C   . ASN   I  273 ? 0.36762 0.36762 0.36762 0.00000  0.00000  0.00000  273 ASN   E C   
13773 O O   . ASN   I  273 ? 0.47902 0.47902 0.47902 0.00000  0.00000  0.00000  273 ASN   E O   
13774 C CB  . ASN   I  273 ? 0.44969 0.44969 0.44969 0.00000  0.00000  0.00000  273 ASN   E CB  
13775 C CG  . ASN   I  273 ? 0.91201 0.91201 0.91201 0.00000  0.00000  0.00000  273 ASN   E CG  
13776 O OD1 . ASN   I  273 ? 0.98087 0.98087 0.98087 0.00000  0.00000  0.00000  273 ASN   E OD1 
13777 N ND2 . ASN   I  273 ? 0.94572 0.94572 0.94572 0.00000  0.00000  0.00000  273 ASN   E ND2 
13778 N N   . ASP   I  274 ? 0.49377 0.49377 0.49377 0.00000  0.00000  0.00000  274 ASP   E N   
13779 C CA  . ASP   I  274 ? 0.45855 0.45855 0.45855 0.00000  0.00000  0.00000  274 ASP   E CA  
13780 C C   . ASP   I  274 ? 0.38759 0.38759 0.38759 -0.00000 0.00000  0.00000  274 ASP   E C   
13781 O O   . ASP   I  274 ? 0.39810 0.39810 0.39810 0.00000  0.00000  0.00000  274 ASP   E O   
13782 C CB  . ASP   I  274 ? 0.41537 0.41537 0.41537 -0.00000 0.00000  0.00000  274 ASP   E CB  
13783 C CG  . ASP   I  274 ? 0.53734 0.53734 0.53734 0.00000  0.00000  0.00000  274 ASP   E CG  
13784 O OD1 . ASP   I  274 ? 0.64461 0.64461 0.64461 0.00000  0.00000  0.00000  274 ASP   E OD1 
13785 O OD2 . ASP   I  274 ? 0.81842 0.81842 0.81842 -0.00000 -0.00000 0.00000  274 ASP   E OD2 
13786 N N   . PRO   I  275 ? 0.48936 0.48936 0.48936 -0.00000 0.00000  0.00000  275 PRO   E N   
13787 C CA  . PRO   I  275 ? 0.23571 0.23571 0.23571 0.00000  0.00000  0.00000  275 PRO   E CA  
13788 C C   . PRO   I  275 ? 0.35732 0.35732 0.35732 0.00000  0.00000  0.00000  275 PRO   E C   
13789 O O   . PRO   I  275 ? 0.52596 0.52596 0.52596 0.00000  0.00000  0.00000  275 PRO   E O   
13790 C CB  . PRO   I  275 ? 0.26391 0.26391 0.26391 0.00000  0.00000  0.00000  275 PRO   E CB  
13791 C CG  . PRO   I  275 ? 0.28982 0.28982 0.28982 0.00000  0.00000  0.00000  275 PRO   E CG  
13792 C CD  . PRO   I  275 ? 0.33969 0.33969 0.33969 0.00000  0.00000  -0.00000 275 PRO   E CD  
13793 N N   . PHE   I  276 ? 0.48920 0.48920 0.48920 0.00000  0.00000  0.00000  276 PHE   E N   
13794 C CA  . PHE   I  276 ? 0.36675 0.36675 0.36675 -0.00000 0.00000  0.00000  276 PHE   E CA  
13795 C C   . PHE   I  276 ? 0.58321 0.58321 0.58321 0.00000  0.00000  0.00000  276 PHE   E C   
13796 O O   . PHE   I  276 ? 0.53075 0.53075 0.53075 0.00000  0.00000  0.00000  276 PHE   E O   
13797 C CB  . PHE   I  276 ? 0.38244 0.38244 0.38244 0.00000  0.00000  0.00000  276 PHE   E CB  
13798 C CG  . PHE   I  276 ? 0.57890 0.57890 0.57890 -0.00000 0.00000  0.00000  276 PHE   E CG  
13799 C CD1 . PHE   I  276 ? 0.49033 0.49033 0.49033 -0.00000 0.00000  0.00000  276 PHE   E CD1 
13800 C CD2 . PHE   I  276 ? 0.45318 0.45318 0.45318 0.00000  0.00000  0.00000  276 PHE   E CD2 
13801 C CE1 . PHE   I  276 ? 0.63952 0.63952 0.63952 0.00000  0.00000  0.00000  276 PHE   E CE1 
13802 C CE2 . PHE   I  276 ? 0.68781 0.68781 0.68781 -0.00000 0.00000  0.00000  276 PHE   E CE2 
13803 C CZ  . PHE   I  276 ? 0.56743 0.56743 0.56743 0.00000  0.00000  0.00000  276 PHE   E CZ  
13804 N N   . THR   I  277 ? 0.42698 0.42698 0.42698 0.00000  0.00000  0.00000  277 THR   E N   
13805 C CA  . THR   I  277 ? 0.49947 0.49947 0.49947 -0.00000 0.00000  0.00000  277 THR   E CA  
13806 C C   . THR   I  277 ? 0.39279 0.39279 0.39279 0.00000  0.00000  0.00000  277 THR   E C   
13807 O O   . THR   I  277 ? 0.46956 0.46956 0.46956 -0.00000 0.00000  0.00000  277 THR   E O   
13808 C CB  . THR   I  277 ? 0.35691 0.35691 0.35691 -0.00000 0.00000  0.00000  277 THR   E CB  
13809 O OG1 . THR   I  277 ? 0.43590 0.43590 0.43590 -0.00000 0.00000  0.00000  277 THR   E OG1 
13810 C CG2 . THR   I  277 ? 0.23020 0.23020 0.23020 -0.00000 0.00000  0.00000  277 THR   E CG2 
13811 N N   . PRO   I  278 ? 0.71316 0.71316 0.71316 0.00000  0.00000  0.00000  278 PRO   E N   
13812 C CA  . PRO   I  278 ? 0.36730 0.36730 0.36730 -0.00000 0.00000  0.00000  278 PRO   E CA  
13813 C C   . PRO   I  278 ? 0.54470 0.54470 0.54470 0.00000  0.00000  0.00000  278 PRO   E C   
13814 O O   . PRO   I  278 ? 0.39985 0.39985 0.39985 0.00000  0.00000  0.00000  278 PRO   E O   
13815 C CB  . PRO   I  278 ? 0.27529 0.27529 0.27529 0.00000  0.00000  0.00000  278 PRO   E CB  
13816 C CG  . PRO   I  278 ? 0.32310 0.32310 0.32310 0.00000  0.00000  0.00000  278 PRO   E CG  
13817 C CD  . PRO   I  278 ? 0.35996 0.35996 0.35996 0.00000  0.00000  0.00000  278 PRO   E CD  
13818 N N   . GLN   I  279 ? 0.41785 0.41785 0.41785 -0.00000 -0.00000 0.00000  279 GLN   E N   
13819 C CA  . GLN   I  279 ? 0.39017 0.39017 0.39017 0.00000  0.00000  0.00000  279 GLN   E CA  
13820 C C   . GLN   I  279 ? 0.55991 0.55991 0.55991 -0.00000 -0.00000 0.00000  279 GLN   E C   
13821 O O   . GLN   I  279 ? 0.53953 0.53953 0.53953 -0.00000 0.00000  0.00000  279 GLN   E O   
13822 C CB  . GLN   I  279 ? 0.35772 0.35772 0.35772 -0.00000 -0.00000 -0.00000 279 GLN   E CB  
13823 C CG  . GLN   I  279 ? 0.25010 0.25010 0.25010 0.00000  0.00000  0.00000  279 GLN   E CG  
13824 C CD  . GLN   I  279 ? 0.75070 0.75070 0.75070 -0.00000 0.00000  0.00000  279 GLN   E CD  
13825 O OE1 . GLN   I  279 ? 0.57125 0.57125 0.57125 -0.00000 0.00000  0.00000  279 GLN   E OE1 
13826 N NE2 . GLN   I  279 ? 0.45756 0.45756 0.45756 0.00000  0.00000  0.00000  279 GLN   E NE2 
13827 N N   . PHE   I  280 ? 0.47375 0.47375 0.47375 -0.00000 0.00000  0.00000  280 PHE   E N   
13828 C CA  . PHE   I  280 ? 0.49373 0.49373 0.49373 -0.00000 0.00000  0.00000  280 PHE   E CA  
13829 C C   . PHE   I  280 ? 0.47249 0.47249 0.47249 0.00000  0.00000  0.00000  280 PHE   E C   
13830 O O   . PHE   I  280 ? 0.50635 0.50635 0.50635 -0.00000 0.00000  0.00000  280 PHE   E O   
13831 C CB  . PHE   I  280 ? 0.26467 0.26467 0.26467 -0.00000 0.00000  0.00000  280 PHE   E CB  
13832 C CG  . PHE   I  280 ? 0.64368 0.64368 0.64368 0.00000  0.00000  0.00000  280 PHE   E CG  
13833 C CD1 . PHE   I  280 ? 0.39925 0.39925 0.39925 0.00000  -0.00000 0.00000  280 PHE   E CD1 
13834 C CD2 . PHE   I  280 ? 0.27670 0.27670 0.27670 0.00000  0.00000  0.00000  280 PHE   E CD2 
13835 C CE1 . PHE   I  280 ? 0.58564 0.58564 0.58564 0.00000  0.00000  0.00000  280 PHE   E CE1 
13836 C CE2 . PHE   I  280 ? 0.57692 0.57692 0.57692 -0.00000 0.00000  0.00000  280 PHE   E CE2 
13837 C CZ  . PHE   I  280 ? 0.48034 0.48034 0.48034 0.00000  0.00000  0.00000  280 PHE   E CZ  
13838 N N   . GLU   I  281 ? 0.49752 0.49752 0.49752 0.00000  0.00000  0.00000  281 GLU   E N   
13839 C CA  . GLU   I  281 ? 0.66020 0.66020 0.66020 -0.00000 0.00000  0.00000  281 GLU   E CA  
13840 C C   . GLU   I  281 ? 0.37203 0.37203 0.37203 -0.00000 0.00000  0.00000  281 GLU   E C   
13841 O O   . GLU   I  281 ? 0.62150 0.62150 0.62150 0.00000  -0.00000 0.00000  281 GLU   E O   
13842 C CB  . GLU   I  281 ? 0.41342 0.41342 0.41342 0.00000  0.00000  0.00000  281 GLU   E CB  
13843 C CG  . GLU   I  281 ? 0.81842 0.81842 0.81842 0.00000  0.00000  0.00000  281 GLU   E CG  
13844 C CD  . GLU   I  281 ? 1.68228 1.68228 1.68228 0.00000  0.00000  0.00000  281 GLU   E CD  
13845 O OE1 . GLU   I  281 ? 0.65823 0.65823 0.65823 0.00000  0.00000  0.00000  281 GLU   E OE1 
13846 O OE2 . GLU   I  281 ? 0.86054 0.86054 0.86054 0.00000  0.00000  0.00000  281 GLU   E OE2 
13847 N N   . HIS   I  282 ? 0.52290 0.52290 0.52290 0.00000  0.00000  0.00000  282 HIS   E N   
13848 C CA  . HIS   I  282 ? 0.82161 0.82161 0.82161 -0.00000 0.00000  0.00000  282 HIS   E CA  
13849 C C   . HIS   I  282 ? 0.66433 0.66433 0.66433 0.00000  0.00000  0.00000  282 HIS   E C   
13850 O O   . HIS   I  282 ? 0.73052 0.73052 0.73052 0.00000  0.00000  0.00000  282 HIS   E O   
13851 C CB  . HIS   I  282 ? 0.41009 0.41009 0.41009 0.00000  0.00000  0.00000  282 HIS   E CB  
13852 C CG  . HIS   I  282 ? 1.00205 1.00205 1.00205 -0.00000 0.00000  0.00000  282 HIS   E CG  
13853 N ND1 . HIS   I  282 ? 0.80841 0.80841 0.80841 -0.00000 0.00000  0.00000  282 HIS   E ND1 
13854 C CD2 . HIS   I  282 ? 0.49884 0.49884 0.49884 0.00000  0.00000  0.00000  282 HIS   E CD2 
13855 C CE1 . HIS   I  282 ? 0.60448 0.60448 0.60448 0.00000  0.00000  0.00000  282 HIS   E CE1 
13856 N NE2 . HIS   I  282 ? 0.75594 0.75594 0.75594 0.00000  0.00000  0.00000  282 HIS   E NE2 
13857 N N   . GLY   I  283 ? 0.58286 0.58286 0.58286 -0.00000 -0.00000 0.00000  283 GLY   E N   
13858 C CA  . GLY   I  283 ? 0.32395 0.32395 0.32395 0.00000  0.00000  0.00000  283 GLY   E CA  
13859 C C   . GLY   I  283 ? 0.47816 0.47816 0.47816 0.00000  0.00000  0.00000  283 GLY   E C   
13860 O O   . GLY   I  283 ? 0.46603 0.46603 0.46603 0.00000  0.00000  0.00000  283 GLY   E O   
13861 N N   . SER   I  284 ? 0.38860 0.38860 0.38860 -0.00000 0.00000  0.00000  284 SER   E N   
13862 C CA  . SER   I  284 ? 0.49886 0.49886 0.49886 0.00000  0.00000  0.00000  284 SER   E CA  
13863 C C   . SER   I  284 ? 0.42296 0.42296 0.42296 0.00000  0.00000  0.00000  284 SER   E C   
13864 O O   . SER   I  284 ? 0.33349 0.33349 0.33349 0.00000  0.00000  0.00000  284 SER   E O   
13865 C CB  . SER   I  284 ? 0.28413 0.28413 0.28413 -0.00000 0.00000  0.00000  284 SER   E CB  
13866 O OG  . SER   I  284 ? 0.52123 0.52123 0.52123 0.00000  0.00000  0.00000  284 SER   E OG  
13867 N N   . ILE   I  285 ? 0.33386 0.33386 0.33386 0.00000  0.00000  0.00000  285 ILE   E N   
13868 C CA  . ILE   I  285 ? 0.31793 0.31793 0.31793 -0.00000 0.00000  0.00000  285 ILE   E CA  
13869 C C   . ILE   I  285 ? 0.26926 0.26926 0.26926 -0.00000 0.00000  0.00000  285 ILE   E C   
13870 O O   . ILE   I  285 ? 0.50983 0.50983 0.50983 0.00000  0.00000  0.00000  285 ILE   E O   
13871 C CB  . ILE   I  285 ? 0.36104 0.36104 0.36104 -0.00000 -0.00000 0.00000  285 ILE   E CB  
13872 C CG1 . ILE   I  285 ? 0.31658 0.31658 0.31658 0.00000  0.00000  0.00000  285 ILE   E CG1 
13873 C CG2 . ILE   I  285 ? 0.26520 0.26520 0.26520 0.00000  0.00000  0.00000  285 ILE   E CG2 
13874 C CD1 . ILE   I  285 ? 0.42157 0.42157 0.42157 -0.00000 0.00000  0.00000  285 ILE   E CD1 
13875 N N   . LEU   I  286 ? 0.48374 0.48374 0.48374 0.00000  -0.00000 0.00000  286 LEU   E N   
13876 C CA  . LEU   I  286 ? 0.26677 0.26677 0.26677 0.00000  0.00000  0.00000  286 LEU   E CA  
13877 C C   . LEU   I  286 ? 0.35416 0.35416 0.35416 0.00000  0.00000  0.00000  286 LEU   E C   
13878 O O   . LEU   I  286 ? 0.41388 0.41388 0.41388 -0.00000 0.00000  0.00000  286 LEU   E O   
13879 C CB  . LEU   I  286 ? 0.45911 0.45911 0.45911 0.00000  0.00000  0.00000  286 LEU   E CB  
13880 C CG  . LEU   I  286 ? 0.40417 0.40417 0.40417 0.00000  0.00000  0.00000  286 LEU   E CG  
13881 C CD1 . LEU   I  286 ? 0.34034 0.34034 0.34034 -0.00000 0.00000  0.00000  286 LEU   E CD1 
13882 C CD2 . LEU   I  286 ? 0.40668 0.40668 0.40668 0.00000  0.00000  0.00000  286 LEU   E CD2 
13883 N N   . GLN   I  287 ? 0.25877 0.25877 0.25877 0.00000  0.00000  0.00000  287 GLN   E N   
13884 C CA  . GLN   I  287 ? 0.43687 0.43687 0.43687 -0.00000 0.00000  0.00000  287 GLN   E CA  
13885 C C   . GLN   I  287 ? 0.44548 0.44548 0.44548 0.00000  0.00000  0.00000  287 GLN   E C   
13886 O O   . GLN   I  287 ? 0.36401 0.36401 0.36401 -0.00000 0.00000  0.00000  287 GLN   E O   
13887 C CB  . GLN   I  287 ? 0.29810 0.29810 0.29810 0.00000  0.00000  0.00000  287 GLN   E CB  
13888 C CG  . GLN   I  287 ? 0.39828 0.39828 0.39828 0.00000  0.00000  0.00000  287 GLN   E CG  
13889 C CD  . GLN   I  287 ? 0.36358 0.36358 0.36358 0.00000  0.00000  0.00000  287 GLN   E CD  
13890 O OE1 . GLN   I  287 ? 0.39067 0.39067 0.39067 0.00000  0.00000  0.00000  287 GLN   E OE1 
13891 N NE2 . GLN   I  287 ? 0.31439 0.31439 0.31439 0.00000  0.00000  0.00000  287 GLN   E NE2 
13892 N N   . GLY   I  288 ? 0.38289 0.38289 0.38289 -0.00000 0.00000  0.00000  288 GLY   E N   
13893 C CA  . GLY   I  288 ? 0.27941 0.27941 0.27941 0.00000  0.00000  0.00000  288 GLY   E CA  
13894 C C   . GLY   I  288 ? 0.33789 0.33789 0.33789 -0.00000 0.00000  0.00000  288 GLY   E C   
13895 O O   . GLY   I  288 ? 0.52834 0.52834 0.52834 -0.00000 0.00000  0.00000  288 GLY   E O   
13896 N N   . PHE   I  289 ? 0.43257 0.43257 0.43257 0.00000  0.00000  0.00000  289 PHE   E N   
13897 C CA  . PHE   I  289 ? 0.51556 0.51556 0.51556 0.00000  0.00000  0.00000  289 PHE   E CA  
13898 C C   . PHE   I  289 ? 0.45603 0.45603 0.45603 0.00000  0.00000  0.00000  289 PHE   E C   
13899 O O   . PHE   I  289 ? 0.48634 0.48634 0.48634 0.00000  0.00000  0.00000  289 PHE   E O   
13900 C CB  . PHE   I  289 ? 0.37676 0.37676 0.37676 0.00000  0.00000  0.00000  289 PHE   E CB  
13901 C CG  . PHE   I  289 ? 0.44874 0.44874 0.44874 -0.00000 0.00000  0.00000  289 PHE   E CG  
13902 C CD1 . PHE   I  289 ? 0.30673 0.30673 0.30673 0.00000  -0.00000 0.00000  289 PHE   E CD1 
13903 C CD2 . PHE   I  289 ? 0.44165 0.44165 0.44165 -0.00000 0.00000  0.00000  289 PHE   E CD2 
13904 C CE1 . PHE   I  289 ? 0.54284 0.54284 0.54284 0.00000  0.00000  0.00000  289 PHE   E CE1 
13905 C CE2 . PHE   I  289 ? 0.48415 0.48415 0.48415 -0.00000 -0.00000 0.00000  289 PHE   E CE2 
13906 C CZ  . PHE   I  289 ? 0.46262 0.46262 0.46262 -0.00000 0.00000  0.00000  289 PHE   E CZ  
13907 N N   . LEU   I  290 ? 0.40437 0.40437 0.40437 0.00000  0.00000  0.00000  290 LEU   E N   
13908 C CA  . LEU   I  290 ? 0.39640 0.39640 0.39640 -0.00000 0.00000  0.00000  290 LEU   E CA  
13909 C C   . LEU   I  290 ? 0.45172 0.45172 0.45172 -0.00000 0.00000  0.00000  290 LEU   E C   
13910 O O   . LEU   I  290 ? 0.70028 0.70028 0.70028 0.00000  0.00000  0.00000  290 LEU   E O   
13911 C CB  . LEU   I  290 ? 0.30948 0.30948 0.30948 0.00000  0.00000  0.00000  290 LEU   E CB  
13912 C CG  . LEU   I  290 ? 0.40768 0.40768 0.40768 0.00000  0.00000  0.00000  290 LEU   E CG  
13913 C CD1 . LEU   I  290 ? 0.37789 0.37789 0.37789 0.00000  0.00000  0.00000  290 LEU   E CD1 
13914 C CD2 . LEU   I  290 ? 0.30725 0.30725 0.30725 0.00000  0.00000  0.00000  290 LEU   E CD2 
13915 N N   . ASN   I  291 ? 0.56426 0.56426 0.56426 0.00000  0.00000  0.00000  291 ASN   E N   
13916 C CA  . ASN   I  291 ? 0.40494 0.40494 0.40494 0.00000  0.00000  0.00000  291 ASN   E CA  
13917 C C   . ASN   I  291 ? 0.46219 0.46219 0.46219 -0.00000 0.00000  0.00000  291 ASN   E C   
13918 O O   . ASN   I  291 ? 0.45735 0.45735 0.45735 -0.00000 0.00000  0.00000  291 ASN   E O   
13919 C CB  . ASN   I  291 ? 0.74764 0.74764 0.74764 0.00000  0.00000  0.00000  291 ASN   E CB  
13920 C CG  . ASN   I  291 ? 0.88658 0.88658 0.88658 0.00000  0.00000  0.00000  291 ASN   E CG  
13921 O OD1 . ASN   I  291 ? 1.46667 1.46667 1.46667 -0.00000 0.00000  0.00000  291 ASN   E OD1 
13922 N ND2 . ASN   I  291 ? 0.89564 0.89564 0.89564 -0.00000 0.00000  0.00000  291 ASN   E ND2 
13923 N N   . VAL   I  292 ? 0.37734 0.37734 0.37734 0.00000  0.00000  0.00000  292 VAL   E N   
13924 C CA  . VAL   I  292 ? 0.73162 0.73162 0.73162 0.00000  0.00000  0.00000  292 VAL   E CA  
13925 C C   . VAL   I  292 ? 0.74100 0.74100 0.74100 0.00000  0.00000  0.00000  292 VAL   E C   
13926 O O   . VAL   I  292 ? 0.51777 0.51777 0.51777 -0.00000 0.00000  0.00000  292 VAL   E O   
13927 C CB  . VAL   I  292 ? 0.71034 0.71034 0.71034 -0.00000 0.00000  0.00000  292 VAL   E CB  
13928 C CG1 . VAL   I  292 ? 0.61989 0.61989 0.61989 0.00000  0.00000  0.00000  292 VAL   E CG1 
13929 C CG2 . VAL   I  292 ? 0.51754 0.51754 0.51754 -0.00000 0.00000  -0.00000 292 VAL   E CG2 
13930 N N   . THR   I  293 ? 0.44052 0.44052 0.44052 0.00000  0.00000  -0.00000 293 THR   E N   
13931 C CA  . THR   I  293 ? 0.52144 0.52144 0.52144 0.00000  0.00000  0.00000  293 THR   E CA  
13932 C C   . THR   I  293 ? 0.86672 0.86672 0.86672 0.00000  0.00000  0.00000  293 THR   E C   
13933 O O   . THR   I  293 ? 0.70523 0.70523 0.70523 0.00000  0.00000  0.00000  293 THR   E O   
13934 C CB  . THR   I  293 ? 0.83264 0.83264 0.83264 0.00000  0.00000  0.00000  293 THR   E CB  
13935 O OG1 . THR   I  293 ? 0.55431 0.55431 0.55431 0.00000  0.00000  0.00000  293 THR   E OG1 
13936 C CG2 . THR   I  293 ? 0.43619 0.43619 0.43619 -0.00000 0.00000  0.00000  293 THR   E CG2 
13937 N N   . ALA   I  294 ? 0.47176 0.47176 0.47176 -0.00000 0.00000  0.00000  294 ALA   E N   
13938 C CA  . ALA   I  294 ? 0.38762 0.38762 0.38762 0.00000  0.00000  0.00000  294 ALA   E CA  
13939 C C   . ALA   I  294 ? 0.38063 0.38063 0.38063 0.00000  0.00000  0.00000  294 ALA   E C   
13940 O O   . ALA   I  294 ? 0.60196 0.60196 0.60196 -0.00000 0.00000  0.00000  294 ALA   E O   
13941 C CB  . ALA   I  294 ? 0.36670 0.36670 0.36670 0.00000  0.00000  0.00000  294 ALA   E CB  
13942 N N   . TYR   I  295 ? 0.40870 0.40870 0.40870 0.00000  0.00000  0.00000  295 TYR   E N   
13943 C CA  . TYR   I  295 ? 0.50301 0.50301 0.50301 0.00000  0.00000  0.00000  295 TYR   E CA  
13944 C C   . TYR   I  295 ? 0.47675 0.47675 0.47675 -0.00000 -0.00000 0.00000  295 TYR   E C   
13945 O O   . TYR   I  295 ? 0.43781 0.43781 0.43781 0.00000  0.00000  0.00000  295 TYR   E O   
13946 C CB  . TYR   I  295 ? 0.16372 0.16372 0.16372 0.00000  0.00000  0.00000  295 TYR   E CB  
13947 C CG  . TYR   I  295 ? 0.54107 0.54107 0.54107 -0.00000 -0.00000 0.00000  295 TYR   E CG  
13948 C CD1 . TYR   I  295 ? 0.39231 0.39231 0.39231 -0.00000 0.00000  0.00000  295 TYR   E CD1 
13949 C CD2 . TYR   I  295 ? 0.33992 0.33992 0.33992 0.00000  0.00000  0.00000  295 TYR   E CD2 
13950 C CE1 . TYR   I  295 ? 0.30236 0.30236 0.30236 -0.00000 0.00000  0.00000  295 TYR   E CE1 
13951 C CE2 . TYR   I  295 ? 0.27732 0.27732 0.27732 0.00000  -0.00000 0.00000  295 TYR   E CE2 
13952 C CZ  . TYR   I  295 ? 0.45828 0.45828 0.45828 0.00000  0.00000  0.00000  295 TYR   E CZ  
13953 O OH  . TYR   I  295 ? 0.34438 0.34438 0.34438 0.00000  0.00000  0.00000  295 TYR   E OH  
13954 N N   . HIS   I  296 ? 0.37446 0.37446 0.37446 -0.00000 0.00000  0.00000  296 HIS   E N   
13955 C CA  . HIS   I  296 ? 0.47867 0.47867 0.47867 0.00000  0.00000  0.00000  296 HIS   E CA  
13956 C C   . HIS   I  296 ? 0.28348 0.28348 0.28348 0.00000  0.00000  0.00000  296 HIS   E C   
13957 O O   . HIS   I  296 ? 0.35822 0.35822 0.35822 0.00000  0.00000  0.00000  296 HIS   E O   
13958 C CB  . HIS   I  296 ? 0.33919 0.33919 0.33919 -0.00000 0.00000  0.00000  296 HIS   E CB  
13959 C CG  . HIS   I  296 ? 0.46450 0.46450 0.46450 0.00000  0.00000  0.00000  296 HIS   E CG  
13960 N ND1 . HIS   I  296 ? 0.56349 0.56349 0.56349 0.00000  0.00000  0.00000  296 HIS   E ND1 
13961 C CD2 . HIS   I  296 ? 0.45748 0.45748 0.45748 0.00000  0.00000  0.00000  296 HIS   E CD2 
13962 C CE1 . HIS   I  296 ? 0.46258 0.46258 0.46258 -0.00000 0.00000  0.00000  296 HIS   E CE1 
13963 N NE2 . HIS   I  296 ? 0.63870 0.63870 0.63870 0.00000  0.00000  0.00000  296 HIS   E NE2 
13964 N N   . ARG   I  297 ? 0.36931 0.36931 0.36931 -0.00000 0.00000  0.00000  297 ARG   E N   
13965 C CA  . ARG   I  297 ? 0.31137 0.31137 0.31137 0.00000  0.00000  0.00000  297 ARG   E CA  
13966 C C   . ARG   I  297 ? 0.52639 0.52639 0.52639 -0.00000 0.00000  0.00000  297 ARG   E C   
13967 O O   . ARG   I  297 ? 0.39526 0.39526 0.39526 0.00000  0.00000  0.00000  297 ARG   E O   
13968 C CB  . ARG   I  297 ? 0.36053 0.36053 0.36053 0.00000  0.00000  0.00000  297 ARG   E CB  
13969 C CG  . ARG   I  297 ? 0.42410 0.42410 0.42410 0.00000  0.00000  0.00000  297 ARG   E CG  
13970 C CD  . ARG   I  297 ? 0.38438 0.38438 0.38438 0.00000  0.00000  0.00000  297 ARG   E CD  
13971 N NE  . ARG   I  297 ? 0.60610 0.60610 0.60610 0.00000  0.00000  0.00000  297 ARG   E NE  
13972 C CZ  . ARG   I  297 ? 0.50884 0.50884 0.50884 0.00000  0.00000  0.00000  297 ARG   E CZ  
13973 N NH1 . ARG   I  297 ? 0.61491 0.61491 0.61491 -0.00000 0.00000  0.00000  297 ARG   E NH1 
13974 N NH2 . ARG   I  297 ? 1.06202 1.06202 1.06202 0.00000  0.00000  -0.00000 297 ARG   E NH2 
13975 N N   . TRP   I  298 ? 0.37270 0.37270 0.37270 0.00000  0.00000  0.00000  298 TRP   E N   
13976 C CA  . TRP   I  298 ? 0.34545 0.34545 0.34545 -0.00000 0.00000  0.00000  298 TRP   E CA  
13977 C C   . TRP   I  298 ? 0.44576 0.44576 0.44576 0.00000  0.00000  0.00000  298 TRP   E C   
13978 O O   . TRP   I  298 ? 0.49690 0.49690 0.49690 0.00000  0.00000  0.00000  298 TRP   E O   
13979 C CB  . TRP   I  298 ? 0.27173 0.27173 0.27173 -0.00000 0.00000  0.00000  298 TRP   E CB  
13980 C CG  . TRP   I  298 ? 0.40764 0.40764 0.40764 0.00000  0.00000  0.00000  298 TRP   E CG  
13981 C CD1 . TRP   I  298 ? 0.34774 0.34774 0.34774 0.00000  0.00000  0.00000  298 TRP   E CD1 
13982 C CD2 . TRP   I  298 ? 0.27317 0.27317 0.27317 0.00000  0.00000  0.00000  298 TRP   E CD2 
13983 N NE1 . TRP   I  298 ? 0.23893 0.23893 0.23893 0.00000  0.00000  0.00000  298 TRP   E NE1 
13984 C CE2 . TRP   I  298 ? 0.31870 0.31870 0.31870 0.00000  0.00000  0.00000  298 TRP   E CE2 
13985 C CE3 . TRP   I  298 ? 0.18531 0.18531 0.18531 -0.00000 0.00000  0.00000  298 TRP   E CE3 
13986 C CZ2 . TRP   I  298 ? 0.38362 0.38362 0.38362 0.00000  0.00000  0.00000  298 TRP   E CZ2 
13987 C CZ3 . TRP   I  298 ? 0.46272 0.46272 0.46272 0.00000  -0.00000 0.00000  298 TRP   E CZ3 
13988 C CH2 . TRP   I  298 ? 0.35577 0.35577 0.35577 -0.00000 0.00000  0.00000  298 TRP   E CH2 
13989 N N   . HIS   I  299 ? 0.39980 0.39980 0.39980 0.00000  0.00000  0.00000  299 HIS   E N   
13990 C CA  . HIS   I  299 ? 0.51224 0.51224 0.51224 -0.00000 0.00000  0.00000  299 HIS   E CA  
13991 C C   . HIS   I  299 ? 0.38756 0.38756 0.38756 0.00000  0.00000  0.00000  299 HIS   E C   
13992 O O   . HIS   I  299 ? 0.41407 0.41407 0.41407 -0.00000 0.00000  0.00000  299 HIS   E O   
13993 C CB  . HIS   I  299 ? 0.25049 0.25049 0.25049 0.00000  0.00000  -0.00000 299 HIS   E CB  
13994 C CG  . HIS   I  299 ? 0.46476 0.46476 0.46476 -0.00000 0.00000  0.00000  299 HIS   E CG  
13995 N ND1 . HIS   I  299 ? 0.37667 0.37667 0.37667 0.00000  0.00000  0.00000  299 HIS   E ND1 
13996 C CD2 . HIS   I  299 ? 0.38050 0.38050 0.38050 -0.00000 0.00000  0.00000  299 HIS   E CD2 
13997 C CE1 . HIS   I  299 ? 0.55057 0.55057 0.55057 0.00000  0.00000  0.00000  299 HIS   E CE1 
13998 N NE2 . HIS   I  299 ? 0.40316 0.40316 0.40316 0.00000  0.00000  0.00000  299 HIS   E NE2 
13999 N N   . ALA   I  300 ? 0.37641 0.37641 0.37641 -0.00000 0.00000  0.00000  300 ALA   E N   
14000 C CA  . ALA   I  300 ? 0.44018 0.44018 0.44018 0.00000  0.00000  0.00000  300 ALA   E CA  
14001 C C   . ALA   I  300 ? 0.35133 0.35133 0.35133 0.00000  0.00000  0.00000  300 ALA   E C   
14002 O O   . ALA   I  300 ? 0.48052 0.48052 0.48052 0.00000  0.00000  0.00000  300 ALA   E O   
14003 C CB  . ALA   I  300 ? 0.29503 0.29503 0.29503 0.00000  0.00000  0.00000  300 ALA   E CB  
14004 N N   . PRO   I  301 ? 0.50109 0.50109 0.50109 -0.00000 0.00000  0.00000  301 PRO   E N   
14005 C CA  . PRO   I  301 ? 0.32177 0.32177 0.32177 0.00000  0.00000  0.00000  301 PRO   E CA  
14006 C C   . PRO   I  301 ? 0.58503 0.58503 0.58503 0.00000  0.00000  0.00000  301 PRO   E C   
14007 O O   . PRO   I  301 ? 0.38745 0.38745 0.38745 0.00000  0.00000  0.00000  301 PRO   E O   
14008 C CB  . PRO   I  301 ? 0.43446 0.43446 0.43446 0.00000  0.00000  0.00000  301 PRO   E CB  
14009 C CG  . PRO   I  301 ? 0.39962 0.39962 0.39962 0.00000  0.00000  0.00000  301 PRO   E CG  
14010 C CD  . PRO   I  301 ? 0.21357 0.21357 0.21357 0.00000  0.00000  0.00000  301 PRO   E CD  
14011 N N   . VAL   I  302 ? 0.29917 0.29917 0.29917 -0.00000 0.00000  0.00000  302 VAL   E N   
14012 C CA  . VAL   I  302 ? 0.61368 0.61368 0.61368 0.00000  0.00000  0.00000  302 VAL   E CA  
14013 C C   . VAL   I  302 ? 0.28961 0.28961 0.28961 0.00000  0.00000  0.00000  302 VAL   E C   
14014 O O   . VAL   I  302 ? 0.50076 0.50076 0.50076 0.00000  0.00000  0.00000  302 VAL   E O   
14015 C CB  . VAL   I  302 ? 0.28654 0.28654 0.28654 -0.00000 0.00000  0.00000  302 VAL   E CB  
14016 C CG1 . VAL   I  302 ? 0.59389 0.59389 0.59389 -0.00000 0.00000  0.00000  302 VAL   E CG1 
14017 C CG2 . VAL   I  302 ? 0.26992 0.26992 0.26992 0.00000  0.00000  0.00000  302 VAL   E CG2 
14018 N N   . ASN   I  303 ? 0.45850 0.45850 0.45850 -0.00000 0.00000  0.00000  303 ASN   E N   
14019 C CA  . ASN   I  303 ? 0.26690 0.26690 0.26690 -0.00000 0.00000  0.00000  303 ASN   E CA  
14020 C C   . ASN   I  303 ? 0.51137 0.51137 0.51137 0.00000  0.00000  0.00000  303 ASN   E C   
14021 O O   . ASN   I  303 ? 0.45440 0.45440 0.45440 0.00000  -0.00000 0.00000  303 ASN   E O   
14022 C CB  . ASN   I  303 ? 0.50535 0.50535 0.50535 -0.00000 0.00000  0.00000  303 ASN   E CB  
14023 C CG  . ASN   I  303 ? 0.41339 0.41339 0.41339 -0.00000 0.00000  0.00000  303 ASN   E CG  
14024 O OD1 . ASN   I  303 ? 0.47301 0.47301 0.47301 -0.00000 0.00000  0.00000  303 ASN   E OD1 
14025 N ND2 . ASN   I  303 ? 0.44834 0.44834 0.44834 0.00000  0.00000  0.00000  303 ASN   E ND2 
14026 N N   . GLY   I  304 ? 0.46978 0.46978 0.46978 -0.00000 0.00000  0.00000  304 GLY   E N   
14027 C CA  . GLY   I  304 ? 0.30225 0.30225 0.30225 0.00000  0.00000  0.00000  304 GLY   E CA  
14028 C C   . GLY   I  304 ? 0.51156 0.51156 0.51156 0.00000  0.00000  0.00000  304 GLY   E C   
14029 O O   . GLY   I  304 ? 0.54722 0.54722 0.54722 0.00000  0.00000  0.00000  304 GLY   E O   
14030 N N   . THR   I  305 ? 0.39044 0.39044 0.39044 0.00000  0.00000  0.00000  305 THR   E N   
14031 C CA  . THR   I  305 ? 0.40689 0.40689 0.40689 0.00000  0.00000  0.00000  305 THR   E CA  
14032 C C   . THR   I  305 ? 0.68467 0.68467 0.68467 0.00000  0.00000  0.00000  305 THR   E C   
14033 O O   . THR   I  305 ? 0.23979 0.23979 0.23979 0.00000  0.00000  0.00000  305 THR   E O   
14034 C CB  . THR   I  305 ? 0.27542 0.27542 0.27542 0.00000  0.00000  0.00000  305 THR   E CB  
14035 O OG1 . THR   I  305 ? 0.49164 0.49164 0.49164 -0.00000 -0.00000 0.00000  305 THR   E OG1 
14036 C CG2 . THR   I  305 ? 0.27273 0.27273 0.27273 -0.00000 0.00000  0.00000  305 THR   E CG2 
14037 N N   . ILE   I  306 ? 0.24492 0.24492 0.24492 0.00000  0.00000  0.00000  306 ILE   E N   
14038 C CA  . ILE   I  306 ? 0.40735 0.40735 0.40735 0.00000  -0.00000 0.00000  306 ILE   E CA  
14039 C C   . ILE   I  306 ? 0.41545 0.41545 0.41545 0.00000  0.00000  0.00000  306 ILE   E C   
14040 O O   . ILE   I  306 ? 0.45414 0.45414 0.45414 -0.00000 0.00000  0.00000  306 ILE   E O   
14041 C CB  . ILE   I  306 ? 0.36010 0.36010 0.36010 -0.00000 0.00000  0.00000  306 ILE   E CB  
14042 C CG1 . ILE   I  306 ? 0.20055 0.20055 0.20055 0.00000  0.00000  0.00000  306 ILE   E CG1 
14043 C CG2 . ILE   I  306 ? 0.30556 0.30556 0.30556 -0.00000 0.00000  0.00000  306 ILE   E CG2 
14044 C CD1 . ILE   I  306 ? 0.28614 0.28614 0.28614 0.00000  0.00000  0.00000  306 ILE   E CD1 
14045 N N   . VAL   I  307 ? 0.45171 0.45171 0.45171 -0.00000 0.00000  0.00000  307 VAL   E N   
14046 C CA  . VAL   I  307 ? 0.37426 0.37426 0.37426 0.00000  0.00000  0.00000  307 VAL   E CA  
14047 C C   . VAL   I  307 ? 0.48467 0.48467 0.48467 0.00000  0.00000  0.00000  307 VAL   E C   
14048 O O   . VAL   I  307 ? 0.46571 0.46571 0.46571 0.00000  0.00000  0.00000  307 VAL   E O   
14049 C CB  . VAL   I  307 ? 0.57592 0.57592 0.57592 0.00000  0.00000  0.00000  307 VAL   E CB  
14050 C CG1 . VAL   I  307 ? 0.24631 0.24631 0.24631 -0.00000 0.00000  0.00000  307 VAL   E CG1 
14051 C CG2 . VAL   I  307 ? 0.38653 0.38653 0.38653 0.00000  0.00000  0.00000  307 VAL   E CG2 
14052 N N   . LYS   I  308 ? 0.55382 0.55382 0.55382 0.00000  0.00000  0.00000  308 LYS   E N   
14053 C CA  . LYS   I  308 ? 0.43501 0.43501 0.43501 0.00000  0.00000  0.00000  308 LYS   E CA  
14054 C C   . LYS   I  308 ? 0.60629 0.60629 0.60629 0.00000  0.00000  0.00000  308 LYS   E C   
14055 O O   . LYS   I  308 ? 0.39314 0.39314 0.39314 0.00000  0.00000  0.00000  308 LYS   E O   
14056 C CB  . LYS   I  308 ? 0.39468 0.39468 0.39468 0.00000  0.00000  0.00000  308 LYS   E CB  
14057 C CG  . LYS   I  308 ? 0.28502 0.28502 0.28502 0.00000  -0.00000 0.00000  308 LYS   E CG  
14058 C CD  . LYS   I  308 ? 0.42253 0.42253 0.42253 0.00000  0.00000  0.00000  308 LYS   E CD  
14059 C CE  . LYS   I  308 ? 0.67511 0.67511 0.67511 0.00000  0.00000  0.00000  308 LYS   E CE  
14060 N NZ  . LYS   I  308 ? 0.82261 0.82261 0.82261 -0.00000 0.00000  0.00000  308 LYS   E NZ  
14061 N N   . ILE   I  309 ? 0.37873 0.37873 0.37873 -0.00000 0.00000  0.00000  309 ILE   E N   
14062 C CA  . ILE   I  309 ? 0.46838 0.46838 0.46838 0.00000  0.00000  0.00000  309 ILE   E CA  
14063 C C   . ILE   I  309 ? 0.37273 0.37273 0.37273 0.00000  0.00000  0.00000  309 ILE   E C   
14064 O O   . ILE   I  309 ? 0.48133 0.48133 0.48133 -0.00000 0.00000  0.00000  309 ILE   E O   
14065 C CB  . ILE   I  309 ? 0.27144 0.27144 0.27144 0.00000  0.00000  0.00000  309 ILE   E CB  
14066 C CG1 . ILE   I  309 ? 0.53349 0.53349 0.53349 -0.00000 0.00000  0.00000  309 ILE   E CG1 
14067 C CG2 . ILE   I  309 ? 0.30507 0.30507 0.30507 0.00000  0.00000  0.00000  309 ILE   E CG2 
14068 C CD1 . ILE   I  309 ? 0.28902 0.28902 0.28902 0.00000  0.00000  0.00000  309 ILE   E CD1 
14069 N N   . ILE   I  310 ? 0.46579 0.46579 0.46579 0.00000  0.00000  0.00000  310 ILE   E N   
14070 C CA  . ILE   I  310 ? 0.26160 0.26160 0.26160 0.00000  0.00000  0.00000  310 ILE   E CA  
14071 C C   . ILE   I  310 ? 0.48213 0.48213 0.48213 0.00000  0.00000  0.00000  310 ILE   E C   
14072 O O   . ILE   I  310 ? 0.39340 0.39340 0.39340 -0.00000 0.00000  0.00000  310 ILE   E O   
14073 C CB  . ILE   I  310 ? 0.48184 0.48184 0.48184 0.00000  0.00000  0.00000  310 ILE   E CB  
14074 C CG1 . ILE   I  310 ? 0.49566 0.49566 0.49566 0.00000  0.00000  0.00000  310 ILE   E CG1 
14075 C CG2 . ILE   I  310 ? 0.32272 0.32272 0.32272 -0.00000 0.00000  0.00000  310 ILE   E CG2 
14076 C CD1 . ILE   I  310 ? 0.55102 0.55102 0.55102 -0.00000 0.00000  0.00000  310 ILE   E CD1 
14077 N N   . ASN   I  311 ? 0.42868 0.42868 0.42868 -0.00000 0.00000  0.00000  311 ASN   E N   
14078 C CA  . ASN   I  311 ? 0.38830 0.38830 0.38830 0.00000  0.00000  0.00000  311 ASN   E CA  
14079 C C   . ASN   I  311 ? 0.25350 0.25350 0.25350 0.00000  0.00000  0.00000  311 ASN   E C   
14080 O O   . ASN   I  311 ? 0.59563 0.59563 0.59563 0.00000  0.00000  0.00000  311 ASN   E O   
14081 C CB  . ASN   I  311 ? 0.19522 0.19522 0.19522 0.00000  0.00000  0.00000  311 ASN   E CB  
14082 C CG  . ASN   I  311 ? 0.77431 0.77431 0.77431 -0.00000 0.00000  0.00000  311 ASN   E CG  
14083 O OD1 . ASN   I  311 ? 0.52089 0.52089 0.52089 0.00000  0.00000  0.00000  311 ASN   E OD1 
14084 N ND2 . ASN   I  311 ? 0.54880 0.54880 0.54880 0.00000  0.00000  0.00000  311 ASN   E ND2 
14085 N N   . VAL   I  312 ? 0.37495 0.37495 0.37495 -0.00000 0.00000  0.00000  312 VAL   E N   
14086 C CA  . VAL   I  312 ? 0.35526 0.35526 0.35526 0.00000  0.00000  0.00000  312 VAL   E CA  
14087 C C   . VAL   I  312 ? 0.34064 0.34064 0.34064 0.00000  0.00000  0.00000  312 VAL   E C   
14088 O O   . VAL   I  312 ? 0.65605 0.65605 0.65605 0.00000  0.00000  0.00000  312 VAL   E O   
14089 C CB  . VAL   I  312 ? 0.40042 0.40042 0.40042 0.00000  0.00000  0.00000  312 VAL   E CB  
14090 C CG1 . VAL   I  312 ? 0.22687 0.22687 0.22687 -0.00000 0.00000  0.00000  312 VAL   E CG1 
14091 C CG2 . VAL   I  312 ? 0.30792 0.30792 0.30792 0.00000  0.00000  0.00000  312 VAL   E CG2 
14092 N N   . PRO   I  313 ? 0.47859 0.47859 0.47859 0.00000  0.00000  0.00000  313 PRO   E N   
14093 C CA  . PRO   I  313 ? 0.42391 0.42391 0.42391 0.00000  0.00000  0.00000  313 PRO   E CA  
14094 C C   . PRO   I  313 ? 0.47052 0.47052 0.47052 -0.00000 0.00000  0.00000  313 PRO   E C   
14095 O O   . PRO   I  313 ? 0.41021 0.41021 0.41021 0.00000  0.00000  0.00000  313 PRO   E O   
14096 C CB  . PRO   I  313 ? 0.20910 0.20910 0.20910 0.00000  0.00000  0.00000  313 PRO   E CB  
14097 C CG  . PRO   I  313 ? 0.28317 0.28317 0.28317 0.00000  -0.00000 0.00000  313 PRO   E CG  
14098 C CD  . PRO   I  313 ? 0.23468 0.23468 0.23468 0.00000  0.00000  0.00000  313 PRO   E CD  
14099 N N   . GLY   I  314 ? 0.41918 0.41918 0.41918 -0.00000 0.00000  0.00000  314 GLY   E N   
14100 C CA  . GLY   I  314 ? 0.32370 0.32370 0.32370 0.00000  0.00000  0.00000  314 GLY   E CA  
14101 C C   . GLY   I  314 ? 0.53854 0.53854 0.53854 -0.00000 0.00000  0.00000  314 GLY   E C   
14102 O O   . GLY   I  314 ? 0.42773 0.42773 0.42773 -0.00000 0.00000  0.00000  314 GLY   E O   
14103 N N   . THR   I  315 ? 0.36394 0.36394 0.36394 -0.00000 0.00000  0.00000  315 THR   E N   
14104 C CA  . THR   I  315 ? 0.39372 0.39372 0.39372 0.00000  0.00000  0.00000  315 THR   E CA  
14105 C C   . THR   I  315 ? 0.49923 0.49923 0.49923 -0.00000 0.00000  0.00000  315 THR   E C   
14106 O O   . THR   I  315 ? 0.40023 0.40023 0.40023 0.00000  0.00000  0.00000  315 THR   E O   
14107 C CB  . THR   I  315 ? 0.38894 0.38894 0.38894 -0.00000 0.00000  0.00000  315 THR   E CB  
14108 O OG1 . THR   I  315 ? 0.31015 0.31015 0.31015 0.00000  0.00000  0.00000  315 THR   E OG1 
14109 C CG2 . THR   I  315 ? 0.26851 0.26851 0.26851 0.00000  0.00000  0.00000  315 THR   E CG2 
14110 N N   . TYR   I  316 ? 0.37768 0.37768 0.37768 0.00000  0.00000  0.00000  316 TYR   E N   
14111 C CA  . TYR   I  316 ? 0.37210 0.37210 0.37210 -0.00000 0.00000  0.00000  316 TYR   E CA  
14112 C C   . TYR   I  316 ? 0.30909 0.30909 0.30909 0.00000  0.00000  0.00000  316 TYR   E C   
14113 O O   . TYR   I  316 ? 0.43400 0.43400 0.43400 -0.00000 0.00000  0.00000  316 TYR   E O   
14114 C CB  . TYR   I  316 ? 0.30809 0.30809 0.30809 0.00000  0.00000  0.00000  316 TYR   E CB  
14115 C CG  . TYR   I  316 ? 0.44419 0.44419 0.44419 0.00000  0.00000  0.00000  316 TYR   E CG  
14116 C CD1 . TYR   I  316 ? 0.46166 0.46166 0.46166 -0.00000 0.00000  0.00000  316 TYR   E CD1 
14117 C CD2 . TYR   I  316 ? 0.36945 0.36945 0.36945 0.00000  0.00000  0.00000  316 TYR   E CD2 
14118 C CE1 . TYR   I  316 ? 0.35576 0.35576 0.35576 -0.00000 0.00000  0.00000  316 TYR   E CE1 
14119 C CE2 . TYR   I  316 ? 0.27051 0.27051 0.27051 0.00000  0.00000  0.00000  316 TYR   E CE2 
14120 C CZ  . TYR   I  316 ? 0.49575 0.49575 0.49575 0.00000  0.00000  0.00000  316 TYR   E CZ  
14121 O OH  . TYR   I  316 ? 0.38523 0.38523 0.38523 -0.00000 0.00000  0.00000  316 TYR   E OH  
14122 N N   . PHE   I  317 ? 0.54862 0.54862 0.54862 0.00000  0.00000  0.00000  317 PHE   E N   
14123 C CA  . PHE   I  317 ? 0.31114 0.31114 0.31114 -0.00000 0.00000  0.00000  317 PHE   E CA  
14124 C C   . PHE   I  317 ? 0.58559 0.58559 0.58559 -0.00000 0.00000  0.00000  317 PHE   E C   
14125 O O   . PHE   I  317 ? 0.43274 0.43274 0.43274 0.00000  0.00000  0.00000  317 PHE   E O   
14126 C CB  . PHE   I  317 ? 0.30961 0.30961 0.30961 -0.00000 0.00000  0.00000  317 PHE   E CB  
14127 C CG  . PHE   I  317 ? 0.56473 0.56473 0.56473 0.00000  0.00000  0.00000  317 PHE   E CG  
14128 C CD1 . PHE   I  317 ? 0.31975 0.31975 0.31975 0.00000  0.00000  0.00000  317 PHE   E CD1 
14129 C CD2 . PHE   I  317 ? 0.51107 0.51107 0.51107 0.00000  0.00000  0.00000  317 PHE   E CD2 
14130 C CE1 . PHE   I  317 ? 0.51364 0.51364 0.51364 -0.00000 0.00000  0.00000  317 PHE   E CE1 
14131 C CE2 . PHE   I  317 ? 0.41979 0.41979 0.41979 0.00000  0.00000  0.00000  317 PHE   E CE2 
14132 C CZ  . PHE   I  317 ? 0.43760 0.43760 0.43760 0.00000  0.00000  0.00000  317 PHE   E CZ  
14133 N N   . ALA   I  318 ? 0.43955 0.43955 0.43955 0.00000  0.00000  0.00000  318 ALA   E N   
14134 C CA  . ALA   I  318 ? 0.39997 0.39997 0.39997 -0.00000 0.00000  0.00000  318 ALA   E CA  
14135 C C   . ALA   I  318 ? 0.46097 0.46097 0.46097 -0.00000 0.00000  0.00000  318 ALA   E C   
14136 O O   . ALA   I  318 ? 0.52324 0.52324 0.52324 -0.00000 0.00000  0.00000  318 ALA   E O   
14137 C CB  . ALA   I  318 ? 0.31793 0.31793 0.31793 -0.00000 0.00000  0.00000  318 ALA   E CB  
14138 N N   . GLN   I  319 ? 0.49028 0.49028 0.49028 -0.00000 0.00000  0.00000  319 GLN   E N   
14139 C CA  . GLN   I  319 ? 0.44571 0.44571 0.44571 0.00000  0.00000  0.00000  319 GLN   E CA  
14140 C C   . GLN   I  319 ? 0.42159 0.42159 0.42159 0.00000  0.00000  -0.00000 319 GLN   E C   
14141 O O   . GLN   I  319 ? 0.60236 0.60236 0.60236 0.00000  0.00000  0.00000  319 GLN   E O   
14142 C CB  . GLN   I  319 ? 0.43920 0.43920 0.43920 0.00000  0.00000  0.00000  319 GLN   E CB  
14143 C CG  . GLN   I  319 ? 0.54182 0.54182 0.54182 0.00000  0.00000  0.00000  319 GLN   E CG  
14144 C CD  . GLN   I  319 ? 0.40266 0.40266 0.40266 0.00000  0.00000  0.00000  319 GLN   E CD  
14145 O OE1 . GLN   I  319 ? 0.69802 0.69802 0.69802 0.00000  0.00000  0.00000  319 GLN   E OE1 
14146 N NE2 . GLN   I  319 ? 0.51421 0.51421 0.51421 0.00000  0.00000  0.00000  319 GLN   E NE2 
14147 N N   . ALA   I  320 ? 0.52128 0.52128 0.52128 -0.00000 0.00000  0.00000  320 ALA   E N   
14148 C CA  . ALA   I  320 ? 0.53072 0.53072 0.53072 -0.00000 0.00000  0.00000  320 ALA   E CA  
14149 C C   . ALA   I  320 ? 0.52746 0.52746 0.52746 0.00000  0.00000  0.00000  320 ALA   E C   
14150 O O   . ALA   I  320 ? 0.54694 0.54694 0.54694 0.00000  0.00000  0.00000  320 ALA   E O   
14151 C CB  . ALA   I  320 ? 0.32482 0.32482 0.32482 -0.00000 0.00000  0.00000  320 ALA   E CB  
14152 N N   . PRO   I  321 ? 0.74194 0.74194 0.74194 0.00000  0.00000  0.00000  321 PRO   E N   
14153 C CA  . PRO   I  321 ? 0.56334 0.56334 0.56334 -0.00000 0.00000  0.00000  321 PRO   E CA  
14154 C C   . PRO   I  321 ? 0.63535 0.63535 0.63535 0.00000  0.00000  0.00000  321 PRO   E C   
14155 O O   . PRO   I  321 ? 0.69572 0.69572 0.69572 0.00000  0.00000  0.00000  321 PRO   E O   
14156 C CB  . PRO   I  321 ? 0.47718 0.47718 0.47718 -0.00000 0.00000  0.00000  321 PRO   E CB  
14157 C CG  . PRO   I  321 ? 0.74517 0.74517 0.74517 0.00000  0.00000  0.00000  321 PRO   E CG  
14158 C CD  . PRO   I  321 ? 0.52087 0.52087 0.52087 0.00000  0.00000  0.00000  321 PRO   E CD  
14159 N N   . SER   I  322 ? 0.59325 0.59325 0.59325 0.00000  0.00000  0.00000  322 SER   E N   
14160 C CA  . SER   I  322 ? 0.58669 0.58669 0.58669 0.00000  0.00000  0.00000  322 SER   E CA  
14161 C C   . SER   I  322 ? 0.58167 0.58167 0.58167 0.00000  0.00000  0.00000  322 SER   E C   
14162 O O   . SER   I  322 ? 0.82712 0.82712 0.82712 0.00000  0.00000  0.00000  322 SER   E O   
14163 C CB  . SER   I  322 ? 0.47352 0.47352 0.47352 0.00000  0.00000  0.00000  322 SER   E CB  
14164 O OG  . SER   I  322 ? 0.79131 0.79131 0.79131 0.00000  0.00000  0.00000  322 SER   E OG  
14165 N N   . THR   I  323 ? 0.72800 0.72800 0.72800 0.00000  0.00000  0.00000  323 THR   E N   
14166 C CA  . THR   I  323 ? 0.50439 0.50439 0.50439 0.00000  0.00000  0.00000  323 THR   E CA  
14167 C C   . THR   I  323 ? 0.70037 0.70037 0.70037 0.00000  -0.00000 0.00000  323 THR   E C   
14168 O O   . THR   I  323 ? 0.48394 0.48394 0.48394 0.00000  0.00000  0.00000  323 THR   E O   
14169 C CB  . THR   I  323 ? 0.58968 0.58968 0.58968 0.00000  0.00000  0.00000  323 THR   E CB  
14170 O OG1 . THR   I  323 ? 0.60912 0.60912 0.60912 0.00000  0.00000  0.00000  323 THR   E OG1 
14171 C CG2 . THR   I  323 ? 0.36107 0.36107 0.36107 -0.00000 0.00000  0.00000  323 THR   E CG2 
14172 N N   . ILE   I  324 ? 0.55183 0.55183 0.55183 0.00000  0.00000  0.00000  324 ILE   E N   
14173 C CA  . ILE   I  324 ? 0.57394 0.57394 0.57394 0.00000  0.00000  0.00000  324 ILE   E CA  
14174 C C   . ILE   I  324 ? 0.80887 0.80887 0.80887 0.00000  0.00000  0.00000  324 ILE   E C   
14175 O O   . ILE   I  324 ? 0.71604 0.71604 0.71604 0.00000  0.00000  0.00000  324 ILE   E O   
14176 C CB  . ILE   I  324 ? 0.42207 0.42207 0.42207 0.00000  -0.00000 0.00000  324 ILE   E CB  
14177 C CG1 . ILE   I  324 ? 0.59151 0.59151 0.59151 0.00000  0.00000  0.00000  324 ILE   E CG1 
14178 C CG2 . ILE   I  324 ? 0.45427 0.45427 0.45427 0.00000  0.00000  0.00000  324 ILE   E CG2 
14179 C CD1 . ILE   I  324 ? 0.50923 0.50923 0.50923 0.00000  0.00000  0.00000  324 ILE   E CD1 
14180 N N   . GLY   I  325 ? 0.63808 0.63808 0.63808 -0.00000 0.00000  0.00000  325 GLY   E N   
14181 C CA  . GLY   I  325 ? 0.57754 0.57754 0.57754 -0.00000 0.00000  0.00000  325 GLY   E CA  
14182 C C   . GLY   I  325 ? 0.69192 0.69192 0.69192 -0.00000 0.00000  0.00000  325 GLY   E C   
14183 O O   . GLY   I  325 ? 0.75741 0.75741 0.75741 -0.00000 0.00000  0.00000  325 GLY   E O   
14184 N N   . ASP   I  326 ? 0.59932 0.59932 0.59932 -0.00000 0.00000  0.00000  326 ASP   E N   
14185 C CA  . ASP   I  326 ? 0.69057 0.69057 0.69057 0.00000  -0.00000 0.00000  326 ASP   E CA  
14186 C C   . ASP   I  326 ? 0.57879 0.57879 0.57879 -0.00000 0.00000  0.00000  326 ASP   E C   
14187 O O   . ASP   I  326 ? 0.71010 0.71010 0.71010 -0.00000 0.00000  0.00000  326 ASP   E O   
14188 C CB  . ASP   I  326 ? 0.46807 0.46807 0.46807 0.00000  0.00000  0.00000  326 ASP   E CB  
14189 C CG  . ASP   I  326 ? 0.93253 0.93253 0.93253 -0.00000 0.00000  0.00000  326 ASP   E CG  
14190 O OD1 . ASP   I  326 ? 0.75017 0.75017 0.75017 0.00000  0.00000  0.00000  326 ASP   E OD1 
14191 O OD2 . ASP   I  326 ? 0.78301 0.78301 0.78301 0.00000  0.00000  0.00000  326 ASP   E OD2 
14192 N N   . PRO   I  327 ? 0.78264 0.78264 0.78264 0.00000  0.00000  0.00000  327 PRO   E N   
14193 C CA  . PRO   I  327 ? 0.59846 0.59846 0.59846 -0.00000 0.00000  0.00000  327 PRO   E CA  
14194 C C   . PRO   I  327 ? 0.53157 0.53157 0.53157 -0.00000 0.00000  -0.00000 327 PRO   E C   
14195 O O   . PRO   I  327 ? 0.69600 0.69600 0.69600 0.00000  0.00000  0.00000  327 PRO   E O   
14196 C CB  . PRO   I  327 ? 0.34378 0.34378 0.34378 0.00000  0.00000  0.00000  327 PRO   E CB  
14197 C CG  . PRO   I  327 ? 0.52956 0.52956 0.52956 -0.00000 0.00000  0.00000  327 PRO   E CG  
14198 C CD  . PRO   I  327 ? 0.56648 0.56648 0.56648 -0.00000 0.00000  0.00000  327 PRO   E CD  
14199 N N   . ILE   I  328 ? 0.63913 0.63913 0.63913 0.00000  0.00000  0.00000  328 ILE   E N   
14200 C CA  . ILE   I  328 ? 0.63659 0.63659 0.63659 0.00000  0.00000  0.00000  328 ILE   E CA  
14201 C C   . ILE   I  328 ? 0.66566 0.66566 0.66566 -0.00000 0.00000  0.00000  328 ILE   E C   
14202 O O   . ILE   I  328 ? 0.78017 0.78017 0.78017 0.00000  -0.00000 -0.00000 328 ILE   E O   
14203 C CB  . ILE   I  328 ? 0.70276 0.70276 0.70276 -0.00000 0.00000  0.00000  328 ILE   E CB  
14204 C CG1 . ILE   I  328 ? 0.54390 0.54390 0.54390 0.00000  0.00000  0.00000  328 ILE   E CG1 
14205 C CG2 . ILE   I  328 ? 0.56574 0.56574 0.56574 0.00000  0.00000  0.00000  328 ILE   E CG2 
14206 C CD1 . ILE   I  328 ? 0.49336 0.49336 0.49336 -0.00000 0.00000  0.00000  328 ILE   E CD1 
14207 N N   . PRO   I  329 ? 0.85098 0.85098 0.85098 0.00000  0.00000  0.00000  329 PRO   E N   
14208 C CA  . PRO   I  329 ? 0.66698 0.66698 0.66698 -0.00000 0.00000  0.00000  329 PRO   E CA  
14209 C C   . PRO   I  329 ? 0.69551 0.69551 0.69551 0.00000  0.00000  0.00000  329 PRO   E C   
14210 O O   . PRO   I  329 ? 1.10524 1.10524 1.10524 -0.00000 0.00000  0.00000  329 PRO   E O   
14211 C CB  . PRO   I  329 ? 0.50057 0.50057 0.50057 0.00000  0.00000  -0.00000 329 PRO   E CB  
14212 C CG  . PRO   I  329 ? 0.63619 0.63619 0.63619 -0.00000 0.00000  0.00000  329 PRO   E CG  
14213 C CD  . PRO   I  329 ? 0.69814 0.69814 0.69814 -0.00000 0.00000  0.00000  329 PRO   E CD  
14214 N N   . ASP   I  330 ? 0.87797 0.87797 0.87797 -0.00000 0.00000  0.00000  330 ASP   E N   
14215 C CA  . ASP   I  330 ? 1.00554 1.00554 1.00554 -0.00000 0.00000  0.00000  330 ASP   E CA  
14216 C C   . ASP   I  330 ? 0.73568 0.73568 0.73568 0.00000  0.00000  0.00000  330 ASP   E C   
14217 O O   . ASP   I  330 ? 1.09949 1.09949 1.09949 0.00000  0.00000  0.00000  330 ASP   E O   
14218 C CB  . ASP   I  330 ? 0.64121 0.64121 0.64121 -0.00000 0.00000  0.00000  330 ASP   E CB  
14219 N N   . ASN   I  331 ? 0.95643 0.95643 0.95643 0.00000  0.00000  0.00000  331 ASN   E N   
14220 C CA  . ASN   I  331 ? 0.95801 0.95801 0.95801 0.00000  0.00000  0.00000  331 ASN   E CA  
14221 C C   . ASN   I  331 ? 0.73850 0.73850 0.73850 0.00000  0.00000  0.00000  331 ASN   E C   
14222 O O   . ASN   I  331 ? 1.29210 1.29210 1.29210 -0.00000 0.00000  0.00000  331 ASN   E O   
14223 C CB  . ASN   I  331 ? 0.67842 0.67842 0.67842 -0.00000 0.00000  0.00000  331 ASN   E CB  
14224 C CG  . ASN   I  331 ? 0.81889 0.81889 0.81889 0.00000  0.00000  0.00000  331 ASN   E CG  
14225 O OD1 . ASN   I  331 ? 1.69929 1.69929 1.69929 0.00000  0.00000  0.00000  331 ASN   E OD1 
14226 N ND2 . ASN   I  331 ? 0.87170 0.87170 0.87170 -0.00000 0.00000  0.00000  331 ASN   E ND2 
14227 N N   . ASP   I  332 ? 1.39298 1.39298 1.39298 0.00000  0.00000  0.00000  332 ASP   E N   
14228 C CA  . ASP   I  332 ? 0.82195 0.82195 0.82195 0.00000  0.00000  0.00000  332 ASP   E CA  
14229 C C   . ASP   I  332 ? 1.03959 1.03959 1.03959 0.00000  0.00000  0.00000  332 ASP   E C   
14230 O O   . ASP   I  332 ? 1.01918 1.01918 1.01918 -0.00000 0.00000  0.00000  332 ASP   E O   
14231 C CB  . ASP   I  332 ? 0.38539 0.38539 0.38539 0.00000  0.00000  0.00000  332 ASP   E CB  
14232 N N   . TYR   I  333 ? 1.51074 1.51074 1.51074 -0.00000 0.00000  0.00000  333 TYR   E N   
14233 C CA  . TYR   I  333 ? 1.00985 1.00985 1.00985 0.00000  -0.00000 0.00000  333 TYR   E CA  
14234 C C   . TYR   I  333 ? 0.97835 0.97835 0.97835 -0.00000 0.00000  0.00000  333 TYR   E C   
14235 O O   . TYR   I  333 ? 0.76161 0.76161 0.76161 -0.00000 0.00000  0.00000  333 TYR   E O   
14236 C CB  . TYR   I  333 ? 1.05537 1.05537 1.05537 0.00000  0.00000  0.00000  333 TYR   E CB  
14237 C CG  . TYR   I  333 ? 1.73169 1.73169 1.73169 -0.00000 -0.00000 0.00000  333 TYR   E CG  
14238 C CD1 . TYR   I  333 ? 1.45350 1.45350 1.45350 0.00000  0.00000  0.00000  333 TYR   E CD1 
14239 C CD2 . TYR   I  333 ? 1.68884 1.68884 1.68884 0.00000  0.00000  0.00000  333 TYR   E CD2 
14240 C CE1 . TYR   I  333 ? 1.27461 1.27461 1.27461 0.00000  -0.00000 0.00000  333 TYR   E CE1 
14241 C CE2 . TYR   I  333 ? 0.77154 0.77154 0.77154 0.00000  0.00000  0.00000  333 TYR   E CE2 
14242 C CZ  . TYR   I  333 ? 1.07369 1.07369 1.07369 -0.00000 0.00000  0.00000  333 TYR   E CZ  
14243 O OH  . TYR   I  333 ? 1.31472 1.31472 1.31472 -0.00000 0.00000  0.00000  333 TYR   E OH  
14244 N N   . ASP   I  334 ? 0.94293 0.94293 0.94293 0.00000  0.00000  0.00000  334 ASP   E N   
14245 C CA  . ASP   I  334 ? 0.91855 0.91855 0.91855 -0.00000 0.00000  0.00000  334 ASP   E CA  
14246 C C   . ASP   I  334 ? 1.03811 1.03811 1.03811 -0.00000 0.00000  0.00000  334 ASP   E C   
14247 O O   . ASP   I  334 ? 0.60405 0.60405 0.60405 0.00000  0.00000  0.00000  334 ASP   E O   
14248 C CB  . ASP   I  334 ? 1.28333 1.28333 1.28333 0.00000  0.00000  -0.00000 334 ASP   E CB  
14249 C CG  . ASP   I  334 ? 1.46851 1.46851 1.46851 -0.00000 0.00000  0.00000  334 ASP   E CG  
14250 O OD1 . ASP   I  334 ? 0.91385 0.91385 0.91385 0.00000  0.00000  0.00000  334 ASP   E OD1 
14251 O OD2 . ASP   I  334 ? 1.05727 1.05727 1.05727 0.00000  0.00000  0.00000  334 ASP   E OD2 
14252 N N   . PRO   I  335 ? 0.84777 0.84777 0.84777 0.00000  0.00000  0.00000  335 PRO   E N   
14253 C CA  . PRO   I  335 ? 0.59201 0.59201 0.59201 -0.00000 0.00000  -0.00000 335 PRO   E CA  
14254 C C   . PRO   I  335 ? 0.38974 0.38974 0.38974 0.00000  0.00000  0.00000  335 PRO   E C   
14255 O O   . PRO   I  335 ? 0.75629 0.75629 0.75629 -0.00000 0.00000  0.00000  335 PRO   E O   
14256 C CB  . PRO   I  335 ? 0.66520 0.66520 0.66520 -0.00000 0.00000  0.00000  335 PRO   E CB  
14257 C CG  . PRO   I  335 ? 0.82808 0.82808 0.82808 0.00000  0.00000  -0.00000 335 PRO   E CG  
14258 C CD  . PRO   I  335 ? 0.49342 0.49342 0.49342 0.00000  0.00000  0.00000  335 PRO   E CD  
14259 N N   . PRO   I  336 ? 0.79102 0.79102 0.79102 -0.00000 0.00000  0.00000  336 PRO   E N   
14260 C CA  . PRO   I  336 ? 0.34033 0.34033 0.34033 -0.00000 0.00000  0.00000  336 PRO   E CA  
14261 C C   . PRO   I  336 ? 1.17993 1.17993 1.17993 -0.00000 0.00000  0.00000  336 PRO   E C   
14262 O O   . PRO   I  336 ? 0.40820 0.40820 0.40820 0.00000  0.00000  0.00000  336 PRO   E O   
14263 C CB  . PRO   I  336 ? 0.58076 0.58076 0.58076 0.00000  0.00000  0.00000  336 PRO   E CB  
14264 C CG  . PRO   I  336 ? 0.54246 0.54246 0.54246 0.00000  0.00000  0.00000  336 PRO   E CG  
14265 C CD  . PRO   I  336 ? 0.34011 0.34011 0.34011 0.00000  0.00000  0.00000  336 PRO   E CD  
14266 N N   . PRO   I  337 ? 0.42315 0.42315 0.42315 0.00000  0.00000  0.00000  337 PRO   E N   
14267 C CA  . PRO   I  337 ? 0.62088 0.62088 0.62088 0.00000  0.00000  0.00000  337 PRO   E CA  
14268 C C   . PRO   I  337 ? 0.47591 0.47591 0.47591 0.00000  0.00000  0.00000  337 PRO   E C   
14269 O O   . PRO   I  337 ? 0.44862 0.44862 0.44862 0.00000  0.00000  0.00000  337 PRO   E O   
14270 C CB  . PRO   I  337 ? 0.45018 0.45018 0.45018 -0.00000 0.00000  0.00000  337 PRO   E CB  
14271 C CG  . PRO   I  337 ? 0.55635 0.55635 0.55635 0.00000  0.00000  0.00000  337 PRO   E CG  
14272 C CD  . PRO   I  337 ? 0.66622 0.66622 0.66622 0.00000  0.00000  0.00000  337 PRO   E CD  
14273 N N   . TYR   I  338 ? 0.45953 0.45953 0.45953 0.00000  0.00000  0.00000  338 TYR   E N   
14274 C CA  . TYR   I  338 ? 0.49227 0.49227 0.49227 -0.00000 0.00000  0.00000  338 TYR   E CA  
14275 C C   . TYR   I  338 ? 0.41390 0.41390 0.41390 -0.00000 0.00000  0.00000  338 TYR   E C   
14276 O O   . TYR   I  338 ? 0.43072 0.43072 0.43072 0.00000  0.00000  0.00000  338 TYR   E O   
14277 C CB  . TYR   I  338 ? 0.33418 0.33418 0.33418 -0.00000 0.00000  0.00000  338 TYR   E CB  
14278 C CG  . TYR   I  338 ? 0.49979 0.49979 0.49979 0.00000  0.00000  0.00000  338 TYR   E CG  
14279 C CD1 . TYR   I  338 ? 0.40769 0.40769 0.40769 0.00000  0.00000  0.00000  338 TYR   E CD1 
14280 C CD2 . TYR   I  338 ? 0.38034 0.38034 0.38034 0.00000  0.00000  0.00000  338 TYR   E CD2 
14281 C CE1 . TYR   I  338 ? 0.44204 0.44204 0.44204 0.00000  0.00000  0.00000  338 TYR   E CE1 
14282 C CE2 . TYR   I  338 ? 0.30319 0.30319 0.30319 0.00000  0.00000  0.00000  338 TYR   E CE2 
14283 C CZ  . TYR   I  338 ? 0.55960 0.55960 0.55960 -0.00000 0.00000  0.00000  338 TYR   E CZ  
14284 O OH  . TYR   I  338 ? 0.41456 0.41456 0.41456 -0.00000 0.00000  0.00000  338 TYR   E OH  
14285 N N   . LEU   I  339 ? 0.42128 0.42128 0.42128 0.00000  0.00000  0.00000  339 LEU   E N   
14286 C CA  . LEU   I  339 ? 0.30934 0.30934 0.30934 0.00000  0.00000  0.00000  339 LEU   E CA  
14287 C C   . LEU   I  339 ? 0.46113 0.46113 0.46113 0.00000  0.00000  0.00000  339 LEU   E C   
14288 O O   . LEU   I  339 ? 0.48256 0.48256 0.48256 0.00000  0.00000  0.00000  339 LEU   E O   
14289 C CB  . LEU   I  339 ? 0.31976 0.31976 0.31976 0.00000  0.00000  0.00000  339 LEU   E CB  
14290 C CG  . LEU   I  339 ? 0.59859 0.59859 0.59859 0.00000  0.00000  0.00000  339 LEU   E CG  
14291 C CD1 . LEU   I  339 ? 0.39374 0.39374 0.39374 0.00000  0.00000  0.00000  339 LEU   E CD1 
14292 C CD2 . LEU   I  339 ? 0.41089 0.41089 0.41089 0.00000  0.00000  0.00000  339 LEU   E CD2 
14293 N N   . LYS   I  340 ? 0.35308 0.35308 0.35308 0.00000  0.00000  0.00000  340 LYS   E N   
14294 C CA  . LYS   I  340 ? 0.60409 0.60409 0.60409 -0.00000 0.00000  0.00000  340 LYS   E CA  
14295 C C   . LYS   I  340 ? 0.37880 0.37880 0.37880 0.00000  0.00000  0.00000  340 LYS   E C   
14296 O O   . LYS   I  340 ? 0.45975 0.45975 0.45975 0.00000  0.00000  0.00000  340 LYS   E O   
14297 C CB  . LYS   I  340 ? 0.38703 0.38703 0.38703 -0.00000 0.00000  0.00000  340 LYS   E CB  
14298 C CG  . LYS   I  340 ? 0.41372 0.41372 0.41372 0.00000  0.00000  0.00000  340 LYS   E CG  
14299 C CD  . LYS   I  340 ? 1.04489 1.04489 1.04489 0.00000  0.00000  0.00000  340 LYS   E CD  
14300 C CE  . LYS   I  340 ? 1.32615 1.32615 1.32615 0.00000  0.00000  0.00000  340 LYS   E CE  
14301 N NZ  . LYS   I  340 ? 1.08106 1.08106 1.08106 0.00000  0.00000  0.00000  340 LYS   E NZ  
14302 N N   . SER   I  341 ? 0.44502 0.44502 0.44502 0.00000  0.00000  0.00000  341 SER   E N   
14303 C CA  . SER   I  341 ? 0.35833 0.35833 0.35833 -0.00000 0.00000  0.00000  341 SER   E CA  
14304 C C   . SER   I  341 ? 0.42020 0.42020 0.42020 -0.00000 0.00000  0.00000  341 SER   E C   
14305 O O   . SER   I  341 ? 0.55380 0.55380 0.55380 0.00000  -0.00000 0.00000  341 SER   E O   
14306 C CB  . SER   I  341 ? 0.44123 0.44123 0.44123 -0.00000 0.00000  0.00000  341 SER   E CB  
14307 O OG  . SER   I  341 ? 0.43821 0.43821 0.43821 0.00000  0.00000  0.00000  341 SER   E OG  
14308 N N   . LEU   I  342 ? 0.39637 0.39637 0.39637 0.00000  0.00000  0.00000  342 LEU   E N   
14309 C CA  . LEU   I  342 ? 0.53809 0.53809 0.53809 -0.00000 0.00000  0.00000  342 LEU   E CA  
14310 C C   . LEU   I  342 ? 0.39373 0.39373 0.39373 0.00000  0.00000  -0.00000 342 LEU   E C   
14311 O O   . LEU   I  342 ? 0.46867 0.46867 0.46867 0.00000  0.00000  0.00000  342 LEU   E O   
14312 C CB  . LEU   I  342 ? 0.32107 0.32107 0.32107 -0.00000 0.00000  0.00000  342 LEU   E CB  
14313 C CG  . LEU   I  342 ? 0.55242 0.55242 0.55242 -0.00000 0.00000  0.00000  342 LEU   E CG  
14314 C CD1 . LEU   I  342 ? 0.30136 0.30136 0.30136 0.00000  0.00000  0.00000  342 LEU   E CD1 
14315 C CD2 . LEU   I  342 ? 0.24577 0.24577 0.24577 0.00000  0.00000  0.00000  342 LEU   E CD2 
14316 N N   . VAL   I  343 ? 0.54562 0.54562 0.54562 -0.00000 0.00000  0.00000  343 VAL   E N   
14317 C CA  . VAL   I  343 ? 0.47335 0.47335 0.47335 0.00000  0.00000  0.00000  343 VAL   E CA  
14318 C C   . VAL   I  343 ? 0.63691 0.63691 0.63691 0.00000  0.00000  0.00000  343 VAL   E C   
14319 O O   . VAL   I  343 ? 0.43843 0.43843 0.43843 0.00000  0.00000  0.00000  343 VAL   E O   
14320 C CB  . VAL   I  343 ? 0.48450 0.48450 0.48450 -0.00000 0.00000  0.00000  343 VAL   E CB  
14321 C CG1 . VAL   I  343 ? 0.30992 0.30992 0.30992 -0.00000 0.00000  0.00000  343 VAL   E CG1 
14322 C CG2 . VAL   I  343 ? 0.40298 0.40298 0.40298 0.00000  0.00000  0.00000  343 VAL   E CG2 
14323 N N   . TYR   I  344 ? 0.34405 0.34405 0.34405 -0.00000 0.00000  0.00000  344 TYR   E N   
14324 C CA  . TYR   I  344 ? 0.56513 0.56513 0.56513 0.00000  0.00000  0.00000  344 TYR   E CA  
14325 C C   . TYR   I  344 ? 0.58455 0.58455 0.58455 -0.00000 -0.00000 -0.00000 344 TYR   E C   
14326 O O   . TYR   I  344 ? 0.45771 0.45771 0.45771 0.00000  0.00000  0.00000  344 TYR   E O   
14327 C CB  . TYR   I  344 ? 0.39923 0.39923 0.39923 -0.00000 0.00000  0.00000  344 TYR   E CB  
14328 C CG  . TYR   I  344 ? 0.65740 0.65740 0.65740 -0.00000 0.00000  0.00000  344 TYR   E CG  
14329 C CD1 . TYR   I  344 ? 0.43895 0.43895 0.43895 0.00000  0.00000  0.00000  344 TYR   E CD1 
14330 C CD2 . TYR   I  344 ? 0.55579 0.55579 0.55579 0.00000  0.00000  0.00000  344 TYR   E CD2 
14331 C CE1 . TYR   I  344 ? 0.44147 0.44147 0.44147 0.00000  0.00000  0.00000  344 TYR   E CE1 
14332 C CE2 . TYR   I  344 ? 0.43003 0.43003 0.43003 0.00000  0.00000  0.00000  344 TYR   E CE2 
14333 C CZ  . TYR   I  344 ? 0.66142 0.66142 0.66142 0.00000  -0.00000 0.00000  344 TYR   E CZ  
14334 O OH  . TYR   I  344 ? 0.59860 0.59860 0.59860 0.00000  0.00000  0.00000  344 TYR   E OH  
14335 N N   . PHE   I  345 ? 0.31283 0.31283 0.31283 -0.00000 0.00000  0.00000  345 PHE   E N   
14336 C CA  . PHE   I  345 ? 0.42743 0.42743 0.42743 0.00000  0.00000  0.00000  345 PHE   E CA  
14337 C C   . PHE   I  345 ? 0.49303 0.49303 0.49303 0.00000  0.00000  0.00000  345 PHE   E C   
14338 O O   . PHE   I  345 ? 0.44671 0.44671 0.44671 0.00000  0.00000  0.00000  345 PHE   E O   
14339 C CB  . PHE   I  345 ? 0.30712 0.30712 0.30712 0.00000  0.00000  0.00000  345 PHE   E CB  
14340 C CG  . PHE   I  345 ? 0.47437 0.47437 0.47437 0.00000  0.00000  0.00000  345 PHE   E CG  
14341 C CD1 . PHE   I  345 ? 0.54035 0.54035 0.54035 0.00000  0.00000  0.00000  345 PHE   E CD1 
14342 C CD2 . PHE   I  345 ? 0.39266 0.39266 0.39266 -0.00000 0.00000  0.00000  345 PHE   E CD2 
14343 C CE1 . PHE   I  345 ? 0.34003 0.34003 0.34003 0.00000  0.00000  0.00000  345 PHE   E CE1 
14344 C CE2 . PHE   I  345 ? 0.41124 0.41124 0.41124 -0.00000 0.00000  0.00000  345 PHE   E CE2 
14345 C CZ  . PHE   I  345 ? 0.44034 0.44034 0.44034 0.00000  0.00000  0.00000  345 PHE   E CZ  
14346 N N   . SER   I  346 ? 0.25003 0.25003 0.25003 0.00000  0.00000  0.00000  346 SER   E N   
14347 C CA  . SER   I  346 ? 0.53129 0.53129 0.53129 -0.00000 0.00000  0.00000  346 SER   E CA  
14348 C C   . SER   I  346 ? 0.37135 0.37135 0.37135 0.00000  0.00000  0.00000  346 SER   E C   
14349 O O   . SER   I  346 ? 0.37139 0.37139 0.37139 -0.00000 0.00000  0.00000  346 SER   E O   
14350 C CB  . SER   I  346 ? 0.36382 0.36382 0.36382 0.00000  0.00000  0.00000  346 SER   E CB  
14351 O OG  . SER   I  346 ? 0.32084 0.32084 0.32084 0.00000  0.00000  0.00000  346 SER   E OG  
14352 N N   . ASN   I  347 ? 0.52299 0.52299 0.52299 0.00000  0.00000  0.00000  347 ASN   E N   
14353 C CA  . ASN   I  347 ? 0.28363 0.28363 0.28363 0.00000  0.00000  0.00000  347 ASN   E CA  
14354 C C   . ASN   I  347 ? 0.49731 0.49731 0.49731 0.00000  0.00000  0.00000  347 ASN   E C   
14355 O O   . ASN   I  347 ? 0.50165 0.50165 0.50165 0.00000  0.00000  0.00000  347 ASN   E O   
14356 C CB  . ASN   I  347 ? 0.37887 0.37887 0.37887 0.00000  0.00000  0.00000  347 ASN   E CB  
14357 C CG  . ASN   I  347 ? 0.57069 0.57069 0.57069 -0.00000 0.00000  0.00000  347 ASN   E CG  
14358 O OD1 . ASN   I  347 ? 0.45842 0.45842 0.45842 -0.00000 0.00000  0.00000  347 ASN   E OD1 
14359 N ND2 . ASN   I  347 ? 0.34103 0.34103 0.34103 0.00000  -0.00000 0.00000  347 ASN   E ND2 
14360 N N   . ILE   I  348 ? 0.46103 0.46103 0.46103 0.00000  0.00000  0.00000  348 ILE   E N   
14361 C CA  . ILE   I  348 ? 0.37231 0.37231 0.37231 0.00000  0.00000  0.00000  348 ILE   E CA  
14362 C C   . ILE   I  348 ? 0.51264 0.51264 0.51264 0.00000  0.00000  0.00000  348 ILE   E C   
14363 O O   . ILE   I  348 ? 0.55660 0.55660 0.55660 0.00000  0.00000  0.00000  348 ILE   E O   
14364 C CB  . ILE   I  348 ? 0.48609 0.48609 0.48609 0.00000  0.00000  0.00000  348 ILE   E CB  
14365 C CG1 . ILE   I  348 ? 0.34083 0.34083 0.34083 0.00000  0.00000  0.00000  348 ILE   E CG1 
14366 C CG2 . ILE   I  348 ? 0.31432 0.31432 0.31432 -0.00000 0.00000  0.00000  348 ILE   E CG2 
14367 C CD1 . ILE   I  348 ? 0.62648 0.62648 0.62648 0.00000  0.00000  0.00000  348 ILE   E CD1 
14368 N N   . ALA   I  349 ? 0.39986 0.39986 0.39986 -0.00000 0.00000  0.00000  349 ALA   E N   
14369 C CA  . ALA   I  349 ? 0.40572 0.40572 0.40572 -0.00000 0.00000  0.00000  349 ALA   E CA  
14370 C C   . ALA   I  349 ? 0.44602 0.44602 0.44602 0.00000  -0.00000 -0.00000 349 ALA   E C   
14371 O O   . ALA   I  349 ? 0.50853 0.50853 0.50853 -0.00000 0.00000  0.00000  349 ALA   E O   
14372 C CB  . ALA   I  349 ? 0.21828 0.21828 0.21828 0.00000  0.00000  0.00000  349 ALA   E CB  
14373 N N   . ALA   I  350 ? 0.34300 0.34300 0.34300 0.00000  0.00000  0.00000  350 ALA   E N   
14374 C CA  . ALA   I  350 ? 0.37449 0.37449 0.37449 0.00000  0.00000  0.00000  350 ALA   E CA  
14375 C C   . ALA   I  350 ? 0.44971 0.44971 0.44971 0.00000  0.00000  0.00000  350 ALA   E C   
14376 O O   . ALA   I  350 ? 0.36776 0.36776 0.36776 -0.00000 0.00000  0.00000  350 ALA   E O   
14377 C CB  . ALA   I  350 ? 0.19557 0.19557 0.19557 0.00000  0.00000  0.00000  350 ALA   E CB  
14378 N N   . ARG   I  351 ? 0.26281 0.26281 0.26281 -0.00000 0.00000  0.00000  351 ARG   E N   
14379 C CA  . ARG   I  351 ? 0.39268 0.39268 0.39268 -0.00000 0.00000  -0.00000 351 ARG   E CA  
14380 C C   . ARG   I  351 ? 0.29563 0.29563 0.29563 0.00000  0.00000  0.00000  351 ARG   E C   
14381 O O   . ARG   I  351 ? 0.47592 0.47592 0.47592 0.00000  0.00000  0.00000  351 ARG   E O   
14382 C CB  . ARG   I  351 ? 0.21183 0.21183 0.21183 -0.00000 0.00000  0.00000  351 ARG   E CB  
14383 C CG  . ARG   I  351 ? 0.21190 0.21190 0.21190 -0.00000 0.00000  0.00000  351 ARG   E CG  
14384 C CD  . ARG   I  351 ? 0.31214 0.31214 0.31214 0.00000  0.00000  0.00000  351 ARG   E CD  
14385 N NE  . ARG   I  351 ? 0.33195 0.33195 0.33195 0.00000  0.00000  0.00000  351 ARG   E NE  
14386 C CZ  . ARG   I  351 ? 0.60453 0.60453 0.60453 0.00000  0.00000  0.00000  351 ARG   E CZ  
14387 N NH1 . ARG   I  351 ? 0.33538 0.33538 0.33538 0.00000  0.00000  0.00000  351 ARG   E NH1 
14388 N NH2 . ARG   I  351 ? 0.27670 0.27670 0.27670 0.00000  0.00000  0.00000  351 ARG   E NH2 
14389 N N   . GLN   I  352 ? 0.35944 0.35944 0.35944 0.00000  0.00000  0.00000  352 GLN   E N   
14390 C CA  . GLN   I  352 ? 0.27534 0.27534 0.27534 0.00000  0.00000  0.00000  352 GLN   E CA  
14391 C C   . GLN   I  352 ? 0.42956 0.42956 0.42956 0.00000  0.00000  0.00000  352 GLN   E C   
14392 O O   . GLN   I  352 ? 0.41536 0.41536 0.41536 0.00000  0.00000  0.00000  352 GLN   E O   
14393 C CB  . GLN   I  352 ? 0.40409 0.40409 0.40409 0.00000  0.00000  0.00000  352 GLN   E CB  
14394 C CG  . GLN   I  352 ? 0.34144 0.34144 0.34144 0.00000  0.00000  0.00000  352 GLN   E CG  
14395 C CD  . GLN   I  352 ? 0.44714 0.44714 0.44714 0.00000  0.00000  0.00000  352 GLN   E CD  
14396 O OE1 . GLN   I  352 ? 0.47322 0.47322 0.47322 0.00000  -0.00000 0.00000  352 GLN   E OE1 
14397 N NE2 . GLN   I  352 ? 0.30992 0.30992 0.30992 0.00000  0.00000  0.00000  352 GLN   E NE2 
14398 N N   . ILE   I  353 ? 0.40182 0.40182 0.40182 -0.00000 0.00000  0.00000  353 ILE   E N   
14399 C CA  . ILE   I  353 ? 0.43758 0.43758 0.43758 0.00000  0.00000  0.00000  353 ILE   E CA  
14400 C C   . ILE   I  353 ? 0.34914 0.34914 0.34914 0.00000  0.00000  0.00000  353 ILE   E C   
14401 O O   . ILE   I  353 ? 0.52759 0.52759 0.52759 0.00000  0.00000  0.00000  353 ILE   E O   
14402 C CB  . ILE   I  353 ? 0.41101 0.41101 0.41101 0.00000  0.00000  0.00000  353 ILE   E CB  
14403 C CG1 . ILE   I  353 ? 0.50272 0.50272 0.50272 -0.00000 0.00000  0.00000  353 ILE   E CG1 
14404 C CG2 . ILE   I  353 ? 0.29529 0.29529 0.29529 0.00000  0.00000  0.00000  353 ILE   E CG2 
14405 C CD1 . ILE   I  353 ? 0.25159 0.25159 0.25159 -0.00000 0.00000  0.00000  353 ILE   E CD1 
14406 N N   . MET   I  354 ? 0.30298 0.30298 0.30298 0.00000  0.00000  0.00000  354 MET   E N   
14407 C CA  . MET   I  354 ? 0.37019 0.37019 0.37019 0.00000  0.00000  0.00000  354 MET   E CA  
14408 C C   . MET   I  354 ? 0.43471 0.43471 0.43471 -0.00000 0.00000  0.00000  354 MET   E C   
14409 O O   . MET   I  354 ? 0.45333 0.45333 0.45333 0.00000  0.00000  0.00000  354 MET   E O   
14410 C CB  . MET   I  354 ? 0.23108 0.23108 0.23108 0.00000  -0.00000 0.00000  354 MET   E CB  
14411 C CG  . MET   I  354 ? 0.50772 0.50772 0.50772 0.00000  0.00000  0.00000  354 MET   E CG  
14412 S SD  . MET   I  354 ? 0.47275 0.47275 0.47275 -0.00000 0.00000  0.00000  354 MET   E SD  
14413 C CE  . MET   I  354 ? 0.45003 0.45003 0.45003 -0.00000 0.00000  0.00000  354 MET   E CE  
14414 N N   . PHE   I  355 ? 0.36816 0.36816 0.36816 0.00000  0.00000  0.00000  355 PHE   E N   
14415 C CA  . PHE   I  355 ? 0.38882 0.38882 0.38882 0.00000  -0.00000 0.00000  355 PHE   E CA  
14416 C C   . PHE   I  355 ? 0.37286 0.37286 0.37286 0.00000  0.00000  0.00000  355 PHE   E C   
14417 O O   . PHE   I  355 ? 0.43126 0.43126 0.43126 -0.00000 0.00000  0.00000  355 PHE   E O   
14418 C CB  . PHE   I  355 ? 0.43768 0.43768 0.43768 0.00000  0.00000  0.00000  355 PHE   E CB  
14419 C CG  . PHE   I  355 ? 0.46123 0.46123 0.46123 -0.00000 0.00000  0.00000  355 PHE   E CG  
14420 C CD1 . PHE   I  355 ? 0.29713 0.29713 0.29713 -0.00000 0.00000  0.00000  355 PHE   E CD1 
14421 C CD2 . PHE   I  355 ? 0.40725 0.40725 0.40725 -0.00000 0.00000  0.00000  355 PHE   E CD2 
14422 C CE1 . PHE   I  355 ? 0.46024 0.46024 0.46024 -0.00000 0.00000  0.00000  355 PHE   E CE1 
14423 C CE2 . PHE   I  355 ? 0.24469 0.24469 0.24469 0.00000  0.00000  0.00000  355 PHE   E CE2 
14424 C CZ  . PHE   I  355 ? 0.26443 0.26443 0.26443 0.00000  0.00000  0.00000  355 PHE   E CZ  
14425 N N   . ILE   I  356 ? 0.33979 0.33979 0.33979 0.00000  0.00000  0.00000  356 ILE   E N   
14426 C CA  . ILE   I  356 ? 0.38233 0.38233 0.38233 0.00000  0.00000  0.00000  356 ILE   E CA  
14427 C C   . ILE   I  356 ? 0.54622 0.54622 0.54622 0.00000  0.00000  0.00000  356 ILE   E C   
14428 O O   . ILE   I  356 ? 0.37829 0.37829 0.37829 0.00000  0.00000  0.00000  356 ILE   E O   
14429 C CB  . ILE   I  356 ? 0.30737 0.30737 0.30737 0.00000  0.00000  0.00000  356 ILE   E CB  
14430 C CG1 . ILE   I  356 ? 0.29850 0.29850 0.29850 0.00000  0.00000  0.00000  356 ILE   E CG1 
14431 C CG2 . ILE   I  356 ? 0.34585 0.34585 0.34585 0.00000  0.00000  0.00000  356 ILE   E CG2 
14432 C CD1 . ILE   I  356 ? 0.22384 0.22384 0.22384 0.00000  0.00000  -0.00000 356 ILE   E CD1 
14433 N N   . GLU   I  357 ? 0.28312 0.28312 0.28312 -0.00000 0.00000  0.00000  357 GLU   E N   
14434 C CA  . GLU   I  357 ? 0.47301 0.47301 0.47301 0.00000  -0.00000 0.00000  357 GLU   E CA  
14435 C C   . GLU   I  357 ? 0.45029 0.45029 0.45029 0.00000  0.00000  0.00000  357 GLU   E C   
14436 O O   . GLU   I  357 ? 0.43367 0.43367 0.43367 -0.00000 0.00000  0.00000  357 GLU   E O   
14437 C CB  . GLU   I  357 ? 0.35288 0.35288 0.35288 -0.00000 0.00000  0.00000  357 GLU   E CB  
14438 C CG  . GLU   I  357 ? 0.33743 0.33743 0.33743 0.00000  0.00000  0.00000  357 GLU   E CG  
14439 C CD  . GLU   I  357 ? 1.01248 1.01248 1.01248 0.00000  0.00000  0.00000  357 GLU   E CD  
14440 O OE1 . GLU   I  357 ? 0.79122 0.79122 0.79122 0.00000  0.00000  0.00000  357 GLU   E OE1 
14441 O OE2 . GLU   I  357 ? 0.62757 0.62757 0.62757 -0.00000 0.00000  0.00000  357 GLU   E OE2 
14442 N N   . ALA   I  358 ? 0.23516 0.23516 0.23516 0.00000  0.00000  0.00000  358 ALA   E N   
14443 C CA  . ALA   I  358 ? 0.47404 0.47404 0.47404 0.00000  0.00000  0.00000  358 ALA   E CA  
14444 C C   . ALA   I  358 ? 0.40347 0.40347 0.40347 -0.00000 0.00000  0.00000  358 ALA   E C   
14445 O O   . ALA   I  358 ? 0.73269 0.73269 0.73269 0.00000  0.00000  0.00000  358 ALA   E O   
14446 C CB  . ALA   I  358 ? 0.33017 0.33017 0.33017 0.00000  -0.00000 0.00000  358 ALA   E CB  
14447 N N   . ASP   I  359 ? 0.68204 0.68204 0.68204 0.00000  0.00000  0.00000  359 ASP   E N   
14448 C CA  . ASP   I  359 ? 0.62266 0.62266 0.62266 -0.00000 0.00000  0.00000  359 ASP   E CA  
14449 C C   . ASP   I  359 ? 0.39662 0.39662 0.39662 -0.00000 0.00000  0.00000  359 ASP   E C   
14450 O O   . ASP   I  359 ? 0.48229 0.48229 0.48229 0.00000  0.00000  0.00000  359 ASP   E O   
14451 C CB  . ASP   I  359 ? 0.35749 0.35749 0.35749 0.00000  0.00000  -0.00000 359 ASP   E CB  
14452 C CG  . ASP   I  359 ? 0.82976 0.82976 0.82976 0.00000  0.00000  0.00000  359 ASP   E CG  
14453 O OD1 . ASP   I  359 ? 0.57677 0.57677 0.57677 -0.00000 0.00000  0.00000  359 ASP   E OD1 
14454 O OD2 . ASP   I  359 ? 0.49711 0.49711 0.49711 -0.00000 0.00000  0.00000  359 ASP   E OD2 
14455 N N   . ASN   I  360 ? 0.47694 0.47694 0.47694 -0.00000 0.00000  0.00000  360 ASN   E N   
14456 C CA  . ASN   I  360 ? 0.36614 0.36614 0.36614 0.00000  0.00000  0.00000  360 ASN   E CA  
14457 C C   . ASN   I  360 ? 0.50502 0.50502 0.50502 0.00000  0.00000  0.00000  360 ASN   E C   
14458 O O   . ASN   I  360 ? 0.64019 0.64019 0.64019 -0.00000 0.00000  0.00000  360 ASN   E O   
14459 C CB  . ASN   I  360 ? 0.38236 0.38236 0.38236 0.00000  0.00000  0.00000  360 ASN   E CB  
14460 C CG  . ASN   I  360 ? 0.62029 0.62029 0.62029 -0.00000 0.00000  0.00000  360 ASN   E CG  
14461 O OD1 . ASN   I  360 ? 0.65961 0.65961 0.65961 0.00000  0.00000  0.00000  360 ASN   E OD1 
14462 N ND2 . ASN   I  360 ? 0.69581 0.69581 0.69581 0.00000  0.00000  0.00000  360 ASN   E ND2 
14463 N N   . LYS   I  361 ? 0.48824 0.48824 0.48824 -0.00000 0.00000  0.00000  361 LYS   E N   
14464 C CA  . LYS   I  361 ? 0.58664 0.58664 0.58664 -0.00000 0.00000  0.00000  361 LYS   E CA  
14465 C C   . LYS   I  361 ? 0.23603 0.23603 0.23603 0.00000  0.00000  0.00000  361 LYS   E C   
14466 O O   . LYS   I  361 ? 0.87414 0.87414 0.87414 0.00000  0.00000  0.00000  361 LYS   E O   
14467 C CB  . LYS   I  361 ? 0.28867 0.28867 0.28867 0.00000  0.00000  0.00000  361 LYS   E CB  
14468 N N   . GLU   I  362 ? 0.36665 0.36665 0.36665 0.00000  0.00000  0.00000  362 GLU   E N   
14469 C CA  . GLU   I  362 ? 0.30919 0.30919 0.30919 0.00000  0.00000  0.00000  362 GLU   E CA  
14470 C C   . GLU   I  362 ? 0.56607 0.56607 0.56607 0.00000  0.00000  0.00000  362 GLU   E C   
14471 O O   . GLU   I  362 ? 0.46807 0.46807 0.46807 -0.00000 0.00000  0.00000  362 GLU   E O   
14472 C CB  . GLU   I  362 ? 0.42139 0.42139 0.42139 0.00000  0.00000  0.00000  362 GLU   E CB  
14473 C CG  . GLU   I  362 ? 1.28330 1.28330 1.28330 0.00000  0.00000  0.00000  362 GLU   E CG  
14474 C CD  . GLU   I  362 ? 1.68090 1.68090 1.68090 0.00000  0.00000  0.00000  362 GLU   E CD  
14475 O OE1 . GLU   I  362 ? 1.36672 1.36672 1.36672 -0.00000 0.00000  0.00000  362 GLU   E OE1 
14476 O OE2 . GLU   I  362 ? 1.44429 1.44429 1.44429 -0.00000 0.00000  0.00000  362 GLU   E OE2 
14477 N N   . ILE   I  363 ? 0.40403 0.40403 0.40403 -0.00000 0.00000  0.00000  363 ILE   E N   
14478 C CA  . ILE   I  363 ? 0.63160 0.63160 0.63160 -0.00000 0.00000  0.00000  363 ILE   E CA  
14479 C C   . ILE   I  363 ? 0.48584 0.48584 0.48584 0.00000  0.00000  -0.00000 363 ILE   E C   
14480 O O   . ILE   I  363 ? 0.59164 0.59164 0.59164 0.00000  0.00000  0.00000  363 ILE   E O   
14481 C CB  . ILE   I  363 ? 0.50794 0.50794 0.50794 0.00000  0.00000  0.00000  363 ILE   E CB  
14482 C CG1 . ILE   I  363 ? 0.43078 0.43078 0.43078 0.00000  0.00000  0.00000  363 ILE   E CG1 
14483 C CG2 . ILE   I  363 ? 0.25189 0.25189 0.25189 0.00000  0.00000  0.00000  363 ILE   E CG2 
14484 C CD1 . ILE   I  363 ? 0.47386 0.47386 0.47386 0.00000  0.00000  0.00000  363 ILE   E CD1 
14485 N N   . GLY   I  364 ? 0.47343 0.47343 0.47343 0.00000  0.00000  0.00000  364 GLY   E N   
14486 C CA  . GLY   I  364 ? 0.32013 0.32013 0.32013 0.00000  0.00000  0.00000  364 GLY   E CA  
14487 C C   . GLY   I  364 ? 0.89314 0.89314 0.89314 0.00000  0.00000  0.00000  364 GLY   E C   
14488 O O   . GLY   I  364 ? 0.44467 0.44467 0.44467 0.00000  0.00000  0.00000  364 GLY   E O   
14489 N N   . LEU   I  365 ? 0.63709 0.63709 0.63709 -0.00000 0.00000  0.00000  365 LEU   E N   
14490 C CA  . LEU   I  365 ? 0.34437 0.34437 0.34437 0.00000  0.00000  0.00000  365 LEU   E CA  
14491 C C   . LEU   I  365 ? 0.65664 0.65664 0.65664 0.00000  0.00000  0.00000  365 LEU   E C   
14492 O O   . LEU   I  365 ? 0.49580 0.49580 0.49580 0.00000  0.00000  0.00000  365 LEU   E O   
14493 C CB  . LEU   I  365 ? 0.52298 0.52298 0.52298 0.00000  0.00000  0.00000  365 LEU   E CB  
14494 C CG  . LEU   I  365 ? 0.56805 0.56805 0.56805 0.00000  0.00000  0.00000  365 LEU   E CG  
14495 C CD1 . LEU   I  365 ? 0.40638 0.40638 0.40638 0.00000  0.00000  0.00000  365 LEU   E CD1 
14496 C CD2 . LEU   I  365 ? 0.39418 0.39418 0.39418 0.00000  0.00000  0.00000  365 LEU   E CD2 
14497 N N   . ILE   I  366 ? 0.28967 0.28967 0.28967 0.00000  0.00000  0.00000  366 ILE   E N   
14498 C CA  . ILE   I  366 ? 0.47114 0.47114 0.47114 0.00000  0.00000  0.00000  366 ILE   E CA  
14499 C C   . ILE   I  366 ? 0.50043 0.50043 0.50043 0.00000  0.00000  0.00000  366 ILE   E C   
14500 O O   . ILE   I  366 ? 0.44374 0.44374 0.44374 -0.00000 0.00000  0.00000  366 ILE   E O   
14501 C CB  . ILE   I  366 ? 0.38707 0.38707 0.38707 0.00000  0.00000  0.00000  366 ILE   E CB  
14502 C CG1 . ILE   I  366 ? 0.43171 0.43171 0.43171 0.00000  0.00000  0.00000  366 ILE   E CG1 
14503 C CG2 . ILE   I  366 ? 0.28504 0.28504 0.28504 0.00000  -0.00000 0.00000  366 ILE   E CG2 
14504 C CD1 . ILE   I  366 ? 0.44147 0.44147 0.44147 0.00000  0.00000  0.00000  366 ILE   E CD1 
14505 N N   . PHE   I  367 ? 0.43345 0.43345 0.43345 -0.00000 0.00000  0.00000  367 PHE   E N   
14506 C CA  . PHE   I  367 ? 0.39506 0.39506 0.39506 0.00000  0.00000  0.00000  367 PHE   E CA  
14507 C C   . PHE   I  367 ? 0.51252 0.51252 0.51252 0.00000  0.00000  0.00000  367 PHE   E C   
14508 O O   . PHE   I  367 ? 0.45561 0.45561 0.45561 0.00000  0.00000  0.00000  367 PHE   E O   
14509 C CB  . PHE   I  367 ? 0.38199 0.38199 0.38199 0.00000  0.00000  0.00000  367 PHE   E CB  
14510 C CG  . PHE   I  367 ? 0.28073 0.28073 0.28073 0.00000  0.00000  0.00000  367 PHE   E CG  
14511 C CD1 . PHE   I  367 ? 0.48708 0.48708 0.48708 0.00000  0.00000  0.00000  367 PHE   E CD1 
14512 C CD2 . PHE   I  367 ? 0.42564 0.42564 0.42564 0.00000  0.00000  0.00000  367 PHE   E CD2 
14513 C CE1 . PHE   I  367 ? 0.28641 0.28641 0.28641 -0.00000 0.00000  0.00000  367 PHE   E CE1 
14514 C CE2 . PHE   I  367 ? 0.40108 0.40108 0.40108 0.00000  0.00000  0.00000  367 PHE   E CE2 
14515 C CZ  . PHE   I  367 ? 0.35957 0.35957 0.35957 0.00000  0.00000  0.00000  367 PHE   E CZ  
14516 N N   . LEU   I  368 ? 0.41705 0.41705 0.41705 0.00000  0.00000  0.00000  368 LEU   E N   
14517 C CA  . LEU   I  368 ? 0.30251 0.30251 0.30251 -0.00000 0.00000  0.00000  368 LEU   E CA  
14518 C C   . LEU   I  368 ? 0.31199 0.31199 0.31199 0.00000  0.00000  0.00000  368 LEU   E C   
14519 O O   . LEU   I  368 ? 0.41979 0.41979 0.41979 0.00000  0.00000  0.00000  368 LEU   E O   
14520 C CB  . LEU   I  368 ? 0.27293 0.27293 0.27293 0.00000  -0.00000 0.00000  368 LEU   E CB  
14521 C CG  . LEU   I  368 ? 0.40713 0.40713 0.40713 0.00000  0.00000  0.00000  368 LEU   E CG  
14522 C CD1 . LEU   I  368 ? 0.35370 0.35370 0.35370 -0.00000 0.00000  0.00000  368 LEU   E CD1 
14523 C CD2 . LEU   I  368 ? 0.37464 0.37464 0.37464 0.00000  0.00000  0.00000  368 LEU   E CD2 
14524 N N   . VAL   I  369 ? 0.33225 0.33225 0.33225 0.00000  0.00000  0.00000  369 VAL   E N   
14525 C CA  . VAL   I  369 ? 0.36189 0.36189 0.36189 0.00000  0.00000  0.00000  369 VAL   E CA  
14526 C C   . VAL   I  369 ? 0.33003 0.33003 0.33003 0.00000  0.00000  0.00000  369 VAL   E C   
14527 O O   . VAL   I  369 ? 0.44967 0.44967 0.44967 0.00000  0.00000  0.00000  369 VAL   E O   
14528 C CB  . VAL   I  369 ? 0.44081 0.44081 0.44081 0.00000  0.00000  0.00000  369 VAL   E CB  
14529 C CG1 . VAL   I  369 ? 0.31122 0.31122 0.31122 -0.00000 0.00000  0.00000  369 VAL   E CG1 
14530 C CG2 . VAL   I  369 ? 0.40486 0.40486 0.40486 -0.00000 0.00000  0.00000  369 VAL   E CG2 
14531 N N   . PHE   I  370 ? 0.44063 0.44063 0.44063 0.00000  0.00000  0.00000  370 PHE   E N   
14532 C CA  . PHE   I  370 ? 0.20816 0.20816 0.20816 0.00000  0.00000  0.00000  370 PHE   E CA  
14533 C C   . PHE   I  370 ? 0.38345 0.38345 0.38345 0.00000  0.00000  0.00000  370 PHE   E C   
14534 O O   . PHE   I  370 ? 0.36094 0.36094 0.36094 0.00000  0.00000  0.00000  370 PHE   E O   
14535 C CB  . PHE   I  370 ? 0.30294 0.30294 0.30294 0.00000  0.00000  0.00000  370 PHE   E CB  
14536 C CG  . PHE   I  370 ? 0.42969 0.42969 0.42969 0.00000  0.00000  0.00000  370 PHE   E CG  
14537 C CD1 . PHE   I  370 ? 0.30969 0.30969 0.30969 0.00000  0.00000  0.00000  370 PHE   E CD1 
14538 C CD2 . PHE   I  370 ? 0.49032 0.49032 0.49032 -0.00000 0.00000  0.00000  370 PHE   E CD2 
14539 C CE1 . PHE   I  370 ? 0.43835 0.43835 0.43835 0.00000  0.00000  0.00000  370 PHE   E CE1 
14540 C CE2 . PHE   I  370 ? 0.29252 0.29252 0.29252 0.00000  0.00000  0.00000  370 PHE   E CE2 
14541 C CZ  . PHE   I  370 ? 0.43194 0.43194 0.43194 0.00000  0.00000  0.00000  370 PHE   E CZ  
14542 N N   . ILE   I  371 ? 0.42641 0.42641 0.42641 -0.00000 0.00000  0.00000  371 ILE   E N   
14543 C CA  . ILE   I  371 ? 0.37295 0.37295 0.37295 0.00000  0.00000  0.00000  371 ILE   E CA  
14544 C C   . ILE   I  371 ? 0.38460 0.38460 0.38460 -0.00000 0.00000  0.00000  371 ILE   E C   
14545 O O   . ILE   I  371 ? 0.51008 0.51008 0.51008 0.00000  0.00000  -0.00000 371 ILE   E O   
14546 C CB  . ILE   I  371 ? 0.48840 0.48840 0.48840 0.00000  0.00000  0.00000  371 ILE   E CB  
14547 C CG1 . ILE   I  371 ? 0.35653 0.35653 0.35653 0.00000  0.00000  0.00000  371 ILE   E CG1 
14548 C CG2 . ILE   I  371 ? 0.30441 0.30441 0.30441 0.00000  0.00000  0.00000  371 ILE   E CG2 
14549 C CD1 . ILE   I  371 ? 0.32951 0.32951 0.32951 0.00000  -0.00000 0.00000  371 ILE   E CD1 
14550 N N   . GLY   I  372 ? 0.33669 0.33669 0.33669 0.00000  0.00000  -0.00000 372 GLY   E N   
14551 C CA  . GLY   I  372 ? 0.22647 0.22647 0.22647 0.00000  -0.00000 0.00000  372 GLY   E CA  
14552 C C   . GLY   I  372 ? 0.33195 0.33195 0.33195 0.00000  0.00000  0.00000  372 GLY   E C   
14553 O O   . GLY   I  372 ? 0.33414 0.33414 0.33414 -0.00000 0.00000  0.00000  372 GLY   E O   
14554 N N   . MET   I  373 ? 0.35434 0.35434 0.35434 -0.00000 0.00000  0.00000  373 MET   E N   
14555 C CA  . MET   I  373 ? 0.51944 0.51944 0.51944 0.00000  0.00000  0.00000  373 MET   E CA  
14556 C C   . MET   I  373 ? 0.49097 0.49097 0.49097 0.00000  0.00000  0.00000  373 MET   E C   
14557 O O   . MET   I  373 ? 0.43134 0.43134 0.43134 0.00000  0.00000  0.00000  373 MET   E O   
14558 C CB  . MET   I  373 ? 0.26618 0.26618 0.26618 0.00000  0.00000  0.00000  373 MET   E CB  
14559 C CG  . MET   I  373 ? 0.54259 0.54259 0.54259 0.00000  -0.00000 0.00000  373 MET   E CG  
14560 S SD  . MET   I  373 ? 0.46039 0.46039 0.46039 0.00000  0.00000  0.00000  373 MET   E SD  
14561 C CE  . MET   I  373 ? 0.15366 0.15366 0.15366 0.00000  0.00000  0.00000  373 MET   E CE  
14562 N N   . THR   I  374 ? 0.33471 0.33471 0.33471 -0.00000 0.00000  0.00000  374 THR   E N   
14563 C CA  . THR   I  374 ? 0.35209 0.35209 0.35209 -0.00000 0.00000  0.00000  374 THR   E CA  
14564 C C   . THR   I  374 ? 0.31293 0.31293 0.31293 -0.00000 0.00000  0.00000  374 THR   E C   
14565 O O   . THR   I  374 ? 0.44746 0.44746 0.44746 -0.00000 0.00000  0.00000  374 THR   E O   
14566 C CB  . THR   I  374 ? 0.46579 0.46579 0.46579 0.00000  0.00000  0.00000  374 THR   E CB  
14567 O OG1 . THR   I  374 ? 0.40186 0.40186 0.40186 0.00000  0.00000  0.00000  374 THR   E OG1 
14568 C CG2 . THR   I  374 ? 0.27041 0.27041 0.27041 -0.00000 0.00000  0.00000  374 THR   E CG2 
14569 N N   . GLU   I  375 ? 0.46173 0.46173 0.46173 0.00000  0.00000  0.00000  375 GLU   E N   
14570 C CA  . GLU   I  375 ? 0.30381 0.30381 0.30381 -0.00000 0.00000  0.00000  375 GLU   E CA  
14571 C C   . GLU   I  375 ? 0.49185 0.49185 0.49185 0.00000  0.00000  0.00000  375 GLU   E C   
14572 O O   . GLU   I  375 ? 0.31572 0.31572 0.31572 0.00000  0.00000  0.00000  375 GLU   E O   
14573 C CB  . GLU   I  375 ? 0.46666 0.46666 0.46666 0.00000  0.00000  0.00000  375 GLU   E CB  
14574 C CG  . GLU   I  375 ? 0.32299 0.32299 0.32299 -0.00000 0.00000  0.00000  375 GLU   E CG  
14575 C CD  . GLU   I  375 ? 0.45421 0.45421 0.45421 -0.00000 0.00000  0.00000  375 GLU   E CD  
14576 O OE1 . GLU   I  375 ? 0.52177 0.52177 0.52177 0.00000  0.00000  0.00000  375 GLU   E OE1 
14577 O OE2 . GLU   I  375 ? 0.50964 0.50964 0.50964 0.00000  0.00000  0.00000  375 GLU   E OE2 
14578 N N   . ILE   I  376 ? 0.35370 0.35370 0.35370 -0.00000 0.00000  0.00000  376 ILE   E N   
14579 C CA  . ILE   I  376 ? 0.35656 0.35656 0.35656 -0.00000 0.00000  0.00000  376 ILE   E CA  
14580 C C   . ILE   I  376 ? 0.40558 0.40558 0.40558 0.00000  0.00000  0.00000  376 ILE   E C   
14581 O O   . ILE   I  376 ? 0.50131 0.50131 0.50131 0.00000  -0.00000 0.00000  376 ILE   E O   
14582 C CB  . ILE   I  376 ? 0.49486 0.49486 0.49486 0.00000  0.00000  0.00000  376 ILE   E CB  
14583 C CG1 . ILE   I  376 ? 0.36102 0.36102 0.36102 -0.00000 -0.00000 0.00000  376 ILE   E CG1 
14584 C CG2 . ILE   I  376 ? 0.21715 0.21715 0.21715 0.00000  0.00000  0.00000  376 ILE   E CG2 
14585 C CD1 . ILE   I  376 ? 0.62483 0.62483 0.62483 0.00000  0.00000  0.00000  376 ILE   E CD1 
14586 N N   . SER   I  377 ? 0.29702 0.29702 0.29702 0.00000  0.00000  0.00000  377 SER   E N   
14587 C CA  . SER   I  377 ? 0.46849 0.46849 0.46849 0.00000  0.00000  0.00000  377 SER   E CA  
14588 C C   . SER   I  377 ? 0.26568 0.26568 0.26568 0.00000  0.00000  0.00000  377 SER   E C   
14589 O O   . SER   I  377 ? 0.57262 0.57262 0.57262 0.00000  0.00000  0.00000  377 SER   E O   
14590 C CB  . SER   I  377 ? 0.18783 0.18783 0.18783 0.00000  0.00000  0.00000  377 SER   E CB  
14591 O OG  . SER   I  377 ? 0.26480 0.26480 0.26480 0.00000  0.00000  0.00000  377 SER   E OG  
14592 N N   . THR   I  378 ? 0.44259 0.44259 0.44259 -0.00000 0.00000  0.00000  378 THR   E N   
14593 C CA  . THR   I  378 ? 0.26687 0.26687 0.26687 0.00000  0.00000  0.00000  378 THR   E CA  
14594 C C   . THR   I  378 ? 0.46141 0.46141 0.46141 0.00000  0.00000  0.00000  378 THR   E C   
14595 O O   . THR   I  378 ? 0.35672 0.35672 0.35672 0.00000  0.00000  0.00000  378 THR   E O   
14596 C CB  . THR   I  378 ? 0.42547 0.42547 0.42547 0.00000  0.00000  0.00000  378 THR   E CB  
14597 O OG1 . THR   I  378 ? 0.35954 0.35954 0.35954 0.00000  0.00000  0.00000  378 THR   E OG1 
14598 C CG2 . THR   I  378 ? 0.11152 0.11152 0.11152 0.00000  0.00000  0.00000  378 THR   E CG2 
14599 N N   . CYS   I  379 ? 0.28396 0.28396 0.28396 0.00000  0.00000  0.00000  379 CYS   E N   
14600 C CA  . CYS   I  379 ? 0.26221 0.26221 0.26221 -0.00000 0.00000  0.00000  379 CYS   E CA  
14601 C C   . CYS   I  379 ? 0.36442 0.36442 0.36442 -0.00000 0.00000  0.00000  379 CYS   E C   
14602 O O   . CYS   I  379 ? 0.43233 0.43233 0.43233 0.00000  0.00000  0.00000  379 CYS   E O   
14603 C CB  . CYS   I  379 ? 0.26957 0.26957 0.26957 0.00000  0.00000  0.00000  379 CYS   E CB  
14604 S SG  . CYS   I  379 ? 0.41554 0.41554 0.41554 -0.00000 0.00000  0.00000  379 CYS   E SG  
14605 N N   . GLU   I  380 ? 0.46777 0.46777 0.46777 0.00000  0.00000  0.00000  380 GLU   E N   
14606 C CA  . GLU   I  380 ? 0.28417 0.28417 0.28417 0.00000  0.00000  0.00000  380 GLU   E CA  
14607 C C   . GLU   I  380 ? 0.49052 0.49052 0.49052 0.00000  0.00000  0.00000  380 GLU   E C   
14608 O O   . GLU   I  380 ? 0.47608 0.47608 0.47608 0.00000  0.00000  0.00000  380 GLU   E O   
14609 C CB  . GLU   I  380 ? 0.42952 0.42952 0.42952 0.00000  0.00000  0.00000  380 GLU   E CB  
14610 C CG  . GLU   I  380 ? 0.59127 0.59127 0.59127 0.00000  0.00000  0.00000  380 GLU   E CG  
14611 C CD  . GLU   I  380 ? 0.53775 0.53775 0.53775 0.00000  0.00000  0.00000  380 GLU   E CD  
14612 O OE1 . GLU   I  380 ? 0.60140 0.60140 0.60140 -0.00000 0.00000  0.00000  380 GLU   E OE1 
14613 O OE2 . GLU   I  380 ? 0.69120 0.69120 0.69120 0.00000  0.00000  0.00000  380 GLU   E OE2 
14614 N N   . ALA   I  381 ? 0.29731 0.29731 0.29731 0.00000  0.00000  0.00000  381 ALA   E N   
14615 C CA  . ALA   I  381 ? 0.53159 0.53159 0.53159 0.00000  0.00000  0.00000  381 ALA   E CA  
14616 C C   . ALA   I  381 ? 0.40988 0.40988 0.40988 0.00000  0.00000  0.00000  381 ALA   E C   
14617 O O   . ALA   I  381 ? 0.41767 0.41767 0.41767 0.00000  0.00000  0.00000  381 ALA   E O   
14618 C CB  . ALA   I  381 ? 0.28439 0.28439 0.28439 -0.00000 0.00000  0.00000  381 ALA   E CB  
14619 N N   . THR   I  382 ? 0.35586 0.35586 0.35586 0.00000  0.00000  0.00000  382 THR   E N   
14620 C CA  . THR   I  382 ? 0.35057 0.35057 0.35057 0.00000  0.00000  0.00000  382 THR   E CA  
14621 C C   . THR   I  382 ? 0.28893 0.28893 0.28893 0.00000  0.00000  0.00000  382 THR   E C   
14622 O O   . THR   I  382 ? 0.63775 0.63775 0.63775 0.00000  0.00000  0.00000  382 THR   E O   
14623 C CB  . THR   I  382 ? 0.22027 0.22027 0.22027 -0.00000 0.00000  0.00000  382 THR   E CB  
14624 O OG1 . THR   I  382 ? 0.33289 0.33289 0.33289 -0.00000 0.00000  0.00000  382 THR   E OG1 
14625 C CG2 . THR   I  382 ? 0.35690 0.35690 0.35690 0.00000  0.00000  0.00000  382 THR   E CG2 
14626 N N   . VAL   I  383 ? 0.37733 0.37733 0.37733 -0.00000 0.00000  0.00000  383 VAL   E N   
14627 C CA  . VAL   I  383 ? 0.24230 0.24230 0.24230 0.00000  0.00000  0.00000  383 VAL   E CA  
14628 C C   . VAL   I  383 ? 0.41964 0.41964 0.41964 0.00000  0.00000  0.00000  383 VAL   E C   
14629 O O   . VAL   I  383 ? 0.36583 0.36583 0.36583 0.00000  0.00000  0.00000  383 VAL   E O   
14630 C CB  . VAL   I  383 ? 0.50462 0.50462 0.50462 -0.00000 0.00000  0.00000  383 VAL   E CB  
14631 C CG1 . VAL   I  383 ? 0.25199 0.25199 0.25199 0.00000  0.00000  0.00000  383 VAL   E CG1 
14632 C CG2 . VAL   I  383 ? 0.31164 0.31164 0.31164 0.00000  0.00000  0.00000  383 VAL   E CG2 
14633 N N   . SER   I  384 ? 0.60006 0.60006 0.60006 -0.00000 0.00000  0.00000  384 SER   E N   
14634 C CA  . SER   I  384 ? 0.35336 0.35336 0.35336 0.00000  0.00000  0.00000  384 SER   E CA  
14635 C C   . SER   I  384 ? 0.66235 0.66235 0.66235 -0.00000 0.00000  0.00000  384 SER   E C   
14636 O O   . SER   I  384 ? 0.52008 0.52008 0.52008 -0.00000 0.00000  0.00000  384 SER   E O   
14637 C CB  . SER   I  384 ? 0.38371 0.38371 0.38371 0.00000  0.00000  0.00000  384 SER   E CB  
14638 O OG  . SER   I  384 ? 0.72828 0.72828 0.72828 -0.00000 0.00000  0.00000  384 SER   E OG  
14639 N N   . GLU   I  385 ? 0.46398 0.46398 0.46398 0.00000  0.00000  0.00000  385 GLU   E N   
14640 C CA  . GLU   I  385 ? 0.57452 0.57452 0.57452 0.00000  0.00000  0.00000  385 GLU   E CA  
14641 C C   . GLU   I  385 ? 0.56967 0.56967 0.56967 0.00000  0.00000  0.00000  385 GLU   E C   
14642 O O   . GLU   I  385 ? 0.54378 0.54378 0.54378 0.00000  0.00000  0.00000  385 GLU   E O   
14643 C CB  . GLU   I  385 ? 0.29513 0.29513 0.29513 0.00000  0.00000  0.00000  385 GLU   E CB  
14644 C CG  . GLU   I  385 ? 0.46990 0.46990 0.46990 0.00000  0.00000  -0.00000 385 GLU   E CG  
14645 C CD  . GLU   I  385 ? 0.68406 0.68406 0.68406 0.00000  0.00000  0.00000  385 GLU   E CD  
14646 O OE1 . GLU   I  385 ? 0.66366 0.66366 0.66366 0.00000  0.00000  -0.00000 385 GLU   E OE1 
14647 O OE2 . GLU   I  385 ? 0.50106 0.50106 0.50106 0.00000  0.00000  0.00000  385 GLU   E OE2 
14648 N N   . GLY   I  386 ? 0.48617 0.48617 0.48617 0.00000  0.00000  0.00000  386 GLY   E N   
14649 C CA  . GLY   I  386 ? 0.31084 0.31084 0.31084 0.00000  0.00000  0.00000  386 GLY   E CA  
14650 C C   . GLY   I  386 ? 0.54780 0.54780 0.54780 0.00000  -0.00000 0.00000  386 GLY   E C   
14651 O O   . GLY   I  386 ? 0.47921 0.47921 0.47921 0.00000  0.00000  0.00000  386 GLY   E O   
14652 N N   . GLN   I  387 ? 0.39082 0.39082 0.39082 0.00000  0.00000  0.00000  387 GLN   E N   
14653 C CA  . GLN   I  387 ? 0.34890 0.34890 0.34890 0.00000  0.00000  0.00000  387 GLN   E CA  
14654 C C   . GLN   I  387 ? 0.59252 0.59252 0.59252 0.00000  0.00000  0.00000  387 GLN   E C   
14655 O O   . GLN   I  387 ? 0.50559 0.50559 0.50559 0.00000  0.00000  0.00000  387 GLN   E O   
14656 C CB  . GLN   I  387 ? 0.33441 0.33441 0.33441 0.00000  0.00000  0.00000  387 GLN   E CB  
14657 C CG  . GLN   I  387 ? 0.34155 0.34155 0.34155 0.00000  0.00000  0.00000  387 GLN   E CG  
14658 C CD  . GLN   I  387 ? 0.44288 0.44288 0.44288 0.00000  0.00000  0.00000  387 GLN   E CD  
14659 O OE1 . GLN   I  387 ? 0.50574 0.50574 0.50574 0.00000  0.00000  0.00000  387 GLN   E OE1 
14660 N NE2 . GLN   I  387 ? 0.35904 0.35904 0.35904 -0.00000 0.00000  0.00000  387 GLN   E NE2 
14661 N N   . HIS   I  388 ? 0.34312 0.34312 0.34312 0.00000  0.00000  0.00000  388 HIS   E N   
14662 C CA  . HIS   I  388 ? 0.48616 0.48616 0.48616 -0.00000 0.00000  0.00000  388 HIS   E CA  
14663 C C   . HIS   I  388 ? 0.65903 0.65903 0.65903 -0.00000 0.00000  0.00000  388 HIS   E C   
14664 O O   . HIS   I  388 ? 0.33079 0.33079 0.33079 0.00000  0.00000  0.00000  388 HIS   E O   
14665 C CB  . HIS   I  388 ? 0.20774 0.20774 0.20774 -0.00000 0.00000  0.00000  388 HIS   E CB  
14666 C CG  . HIS   I  388 ? 0.42726 0.42726 0.42726 0.00000  0.00000  0.00000  388 HIS   E CG  
14667 N ND1 . HIS   I  388 ? 0.43940 0.43940 0.43940 0.00000  0.00000  0.00000  388 HIS   E ND1 
14668 C CD2 . HIS   I  388 ? 0.28708 0.28708 0.28708 -0.00000 0.00000  0.00000  388 HIS   E CD2 
14669 C CE1 . HIS   I  388 ? 0.39274 0.39274 0.39274 -0.00000 0.00000  0.00000  388 HIS   E CE1 
14670 N NE2 . HIS   I  388 ? 0.34133 0.34133 0.34133 0.00000  0.00000  0.00000  388 HIS   E NE2 
14671 N N   . VAL   I  389 ? 0.23198 0.23198 0.23198 0.00000  -0.00000 0.00000  389 VAL   E N   
14672 C CA  . VAL   I  389 ? 0.38907 0.38907 0.38907 0.00000  0.00000  0.00000  389 VAL   E CA  
14673 C C   . VAL   I  389 ? 0.37569 0.37569 0.37569 0.00000  0.00000  0.00000  389 VAL   E C   
14674 O O   . VAL   I  389 ? 0.55469 0.55469 0.55469 0.00000  0.00000  0.00000  389 VAL   E O   
14675 C CB  . VAL   I  389 ? 0.45476 0.45476 0.45476 -0.00000 0.00000  0.00000  389 VAL   E CB  
14676 C CG1 . VAL   I  389 ? 0.26223 0.26223 0.26223 -0.00000 0.00000  0.00000  389 VAL   E CG1 
14677 C CG2 . VAL   I  389 ? 0.18988 0.18988 0.18988 -0.00000 -0.00000 0.00000  389 VAL   E CG2 
14678 N N   . ASN   I  390 ? 0.28880 0.28880 0.28880 0.00000  0.00000  0.00000  390 ASN   E N   
14679 C CA  . ASN   I  390 ? 0.33267 0.33267 0.33267 0.00000  0.00000  0.00000  390 ASN   E CA  
14680 C C   . ASN   I  390 ? 0.65389 0.65389 0.65389 0.00000  0.00000  0.00000  390 ASN   E C   
14681 O O   . ASN   I  390 ? 0.36860 0.36860 0.36860 -0.00000 0.00000  0.00000  390 ASN   E O   
14682 C CB  . ASN   I  390 ? 0.49352 0.49352 0.49352 0.00000  0.00000  0.00000  390 ASN   E CB  
14683 C CG  . ASN   I  390 ? 0.41181 0.41181 0.41181 0.00000  0.00000  0.00000  390 ASN   E CG  
14684 O OD1 . ASN   I  390 ? 0.54459 0.54459 0.54459 0.00000  0.00000  0.00000  390 ASN   E OD1 
14685 N ND2 . ASN   I  390 ? 0.53766 0.53766 0.53766 -0.00000 0.00000  0.00000  390 ASN   E ND2 
14686 N N   . ARG   I  391 ? 0.29697 0.29697 0.29697 -0.00000 0.00000  0.00000  391 ARG   E N   
14687 C CA  . ARG   I  391 ? 0.43115 0.43115 0.43115 -0.00000 0.00000  0.00000  391 ARG   E CA  
14688 C C   . ARG   I  391 ? 0.27927 0.27927 0.27927 0.00000  0.00000  0.00000  391 ARG   E C   
14689 O O   . ARG   I  391 ? 0.41453 0.41453 0.41453 0.00000  0.00000  0.00000  391 ARG   E O   
14690 C CB  . ARG   I  391 ? 0.16996 0.16996 0.16996 0.00000  0.00000  -0.00000 391 ARG   E CB  
14691 C CG  . ARG   I  391 ? 0.29243 0.29243 0.29243 -0.00000 -0.00000 0.00000  391 ARG   E CG  
14692 C CD  . ARG   I  391 ? 0.41387 0.41387 0.41387 -0.00000 0.00000  0.00000  391 ARG   E CD  
14693 N NE  . ARG   I  391 ? 0.31711 0.31711 0.31711 0.00000  -0.00000 0.00000  391 ARG   E NE  
14694 C CZ  . ARG   I  391 ? 0.84359 0.84359 0.84359 0.00000  0.00000  -0.00000 391 ARG   E CZ  
14695 N NH1 . ARG   I  391 ? 0.32933 0.32933 0.32933 0.00000  0.00000  0.00000  391 ARG   E NH1 
14696 N NH2 . ARG   I  391 ? 0.34133 0.34133 0.34133 -0.00000 0.00000  0.00000  391 ARG   E NH2 
14697 N N   . GLY   I  392 ? 0.35069 0.35069 0.35069 -0.00000 0.00000  0.00000  392 GLY   E N   
14698 C CA  . GLY   I  392 ? 0.30544 0.30544 0.30544 0.00000  0.00000  0.00000  392 GLY   E CA  
14699 C C   . GLY   I  392 ? 0.41666 0.41666 0.41666 0.00000  0.00000  0.00000  392 GLY   E C   
14700 O O   . GLY   I  392 ? 0.39862 0.39862 0.39862 -0.00000 0.00000  0.00000  392 GLY   E O   
14701 N N   . ASP   I  393 ? 0.26600 0.26600 0.26600 0.00000  0.00000  0.00000  393 ASP   E N   
14702 C CA  . ASP   I  393 ? 0.42672 0.42672 0.42672 0.00000  0.00000  0.00000  393 ASP   E CA  
14703 C C   . ASP   I  393 ? 0.35777 0.35777 0.35777 0.00000  0.00000  0.00000  393 ASP   E C   
14704 O O   . ASP   I  393 ? 0.59910 0.59910 0.59910 -0.00000 0.00000  0.00000  393 ASP   E O   
14705 C CB  . ASP   I  393 ? 0.30817 0.30817 0.30817 0.00000  0.00000  0.00000  393 ASP   E CB  
14706 C CG  . ASP   I  393 ? 0.67404 0.67404 0.67404 0.00000  0.00000  0.00000  393 ASP   E CG  
14707 O OD1 . ASP   I  393 ? 0.63100 0.63100 0.63100 0.00000  0.00000  0.00000  393 ASP   E OD1 
14708 O OD2 . ASP   I  393 ? 0.48030 0.48030 0.48030 0.00000  -0.00000 0.00000  393 ASP   E OD2 
14709 N N   . ASP   I  394 ? 0.62615 0.62615 0.62615 0.00000  0.00000  0.00000  394 ASP   E N   
14710 C CA  . ASP   I  394 ? 0.31860 0.31860 0.31860 0.00000  0.00000  0.00000  394 ASP   E CA  
14711 C C   . ASP   I  394 ? 0.65654 0.65654 0.65654 0.00000  0.00000  0.00000  394 ASP   E C   
14712 O O   . ASP   I  394 ? 0.43901 0.43901 0.43901 -0.00000 0.00000  0.00000  394 ASP   E O   
14713 C CB  . ASP   I  394 ? 0.56555 0.56555 0.56555 0.00000  0.00000  0.00000  394 ASP   E CB  
14714 C CG  . ASP   I  394 ? 0.43259 0.43259 0.43259 -0.00000 0.00000  0.00000  394 ASP   E CG  
14715 O OD1 . ASP   I  394 ? 0.99440 0.99440 0.99440 -0.00000 0.00000  0.00000  394 ASP   E OD1 
14716 O OD2 . ASP   I  394 ? 0.93424 0.93424 0.93424 -0.00000 0.00000  0.00000  394 ASP   E OD2 
14717 N N   . LEU   I  395 ? 0.37584 0.37584 0.37584 0.00000  0.00000  0.00000  395 LEU   E N   
14718 C CA  . LEU   I  395 ? 0.61573 0.61573 0.61573 -0.00000 0.00000  0.00000  395 LEU   E CA  
14719 C C   . LEU   I  395 ? 0.52625 0.52625 0.52625 0.00000  0.00000  0.00000  395 LEU   E C   
14720 O O   . LEU   I  395 ? 0.49415 0.49415 0.49415 0.00000  0.00000  0.00000  395 LEU   E O   
14721 C CB  . LEU   I  395 ? 0.33038 0.33038 0.33038 0.00000  0.00000  0.00000  395 LEU   E CB  
14722 C CG  . LEU   I  395 ? 0.51370 0.51370 0.51370 -0.00000 -0.00000 0.00000  395 LEU   E CG  
14723 C CD1 . LEU   I  395 ? 0.32369 0.32369 0.32369 -0.00000 0.00000  0.00000  395 LEU   E CD1 
14724 C CD2 . LEU   I  395 ? 0.45072 0.45072 0.45072 0.00000  0.00000  0.00000  395 LEU   E CD2 
14725 N N   . GLY   I  396 ? 0.31324 0.31324 0.31324 0.00000  0.00000  0.00000  396 GLY   E N   
14726 C CA  . GLY   I  396 ? 0.41961 0.41961 0.41961 0.00000  0.00000  0.00000  396 GLY   E CA  
14727 C C   . GLY   I  396 ? 0.37108 0.37108 0.37108 0.00000  0.00000  0.00000  396 GLY   E C   
14728 O O   . GLY   I  396 ? 0.41479 0.41479 0.41479 0.00000  0.00000  0.00000  396 GLY   E O   
14729 N N   . MET   I  397 ? 0.33881 0.33881 0.33881 0.00000  0.00000  0.00000  397 MET   E N   
14730 C CA  . MET   I  397 ? 0.32458 0.32458 0.32458 0.00000  0.00000  0.00000  397 MET   E CA  
14731 C C   . MET   I  397 ? 0.52102 0.52102 0.52102 0.00000  0.00000  0.00000  397 MET   E C   
14732 O O   . MET   I  397 ? 0.38461 0.38461 0.38461 -0.00000 0.00000  0.00000  397 MET   E O   
14733 C CB  . MET   I  397 ? 0.29703 0.29703 0.29703 0.00000  0.00000  0.00000  397 MET   E CB  
14734 C CG  . MET   I  397 ? 0.35378 0.35378 0.35378 0.00000  0.00000  0.00000  397 MET   E CG  
14735 S SD  . MET   I  397 ? 0.48551 0.48551 0.48551 -0.00000 0.00000  0.00000  397 MET   E SD  
14736 C CE  . MET   I  397 ? 0.20999 0.20999 0.20999 0.00000  -0.00000 0.00000  397 MET   E CE  
14737 N N   . PHE   I  398 ? 0.36536 0.36536 0.36536 -0.00000 0.00000  0.00000  398 PHE   E N   
14738 C CA  . PHE   I  398 ? 0.28028 0.28028 0.28028 -0.00000 0.00000  0.00000  398 PHE   E CA  
14739 C C   . PHE   I  398 ? 0.40414 0.40414 0.40414 0.00000  -0.00000 0.00000  398 PHE   E C   
14740 O O   . PHE   I  398 ? 0.52712 0.52712 0.52712 0.00000  0.00000  0.00000  398 PHE   E O   
14741 C CB  . PHE   I  398 ? 0.28132 0.28132 0.28132 0.00000  0.00000  0.00000  398 PHE   E CB  
14742 C CG  . PHE   I  398 ? 0.45415 0.45415 0.45415 0.00000  0.00000  0.00000  398 PHE   E CG  
14743 C CD1 . PHE   I  398 ? 0.28529 0.28529 0.28529 0.00000  0.00000  0.00000  398 PHE   E CD1 
14744 C CD2 . PHE   I  398 ? 0.37089 0.37089 0.37089 -0.00000 0.00000  0.00000  398 PHE   E CD2 
14745 C CE1 . PHE   I  398 ? 0.43778 0.43778 0.43778 -0.00000 0.00000  0.00000  398 PHE   E CE1 
14746 C CE2 . PHE   I  398 ? 0.32079 0.32079 0.32079 0.00000  0.00000  0.00000  398 PHE   E CE2 
14747 C CZ  . PHE   I  398 ? 0.41370 0.41370 0.41370 0.00000  0.00000  0.00000  398 PHE   E CZ  
14748 N N   . HIS   I  399 ? 0.46466 0.46466 0.46466 0.00000  0.00000  0.00000  399 HIS   E N   
14749 C CA  . HIS   I  399 ? 0.57097 0.57097 0.57097 0.00000  0.00000  0.00000  399 HIS   E CA  
14750 C C   . HIS   I  399 ? 0.29815 0.29815 0.29815 0.00000  0.00000  0.00000  399 HIS   E C   
14751 O O   . HIS   I  399 ? 0.65782 0.65782 0.65782 0.00000  0.00000  0.00000  399 HIS   E O   
14752 C CB  . HIS   I  399 ? 0.26650 0.26650 0.26650 0.00000  0.00000  0.00000  399 HIS   E CB  
14753 C CG  . HIS   I  399 ? 0.31404 0.31404 0.31404 -0.00000 0.00000  0.00000  399 HIS   E CG  
14754 N ND1 . HIS   I  399 ? 0.41593 0.41593 0.41593 0.00000  0.00000  0.00000  399 HIS   E ND1 
14755 C CD2 . HIS   I  399 ? 0.50944 0.50944 0.50944 -0.00000 0.00000  0.00000  399 HIS   E CD2 
14756 C CE1 . HIS   I  399 ? 0.63951 0.63951 0.63951 0.00000  0.00000  0.00000  399 HIS   E CE1 
14757 N NE2 . HIS   I  399 ? 0.27489 0.27489 0.27489 0.00000  0.00000  -0.00000 399 HIS   E NE2 
14758 N N   . PHE   I  400 ? 0.51941 0.51941 0.51941 -0.00000 0.00000  0.00000  400 PHE   E N   
14759 C CA  . PHE   I  400 ? 0.28471 0.28471 0.28471 -0.00000 0.00000  0.00000  400 PHE   E CA  
14760 C C   . PHE   I  400 ? 0.39402 0.39402 0.39402 0.00000  0.00000  0.00000  400 PHE   E C   
14761 O O   . PHE   I  400 ? 0.52688 0.52688 0.52688 0.00000  0.00000  0.00000  400 PHE   E O   
14762 C CB  . PHE   I  400 ? 0.50861 0.50861 0.50861 -0.00000 -0.00000 0.00000  400 PHE   E CB  
14763 C CG  . PHE   I  400 ? 0.25438 0.25438 0.25438 -0.00000 0.00000  0.00000  400 PHE   E CG  
14764 C CD1 . PHE   I  400 ? 0.49558 0.49558 0.49558 -0.00000 0.00000  0.00000  400 PHE   E CD1 
14765 C CD2 . PHE   I  400 ? 0.50815 0.50815 0.50815 0.00000  0.00000  0.00000  400 PHE   E CD2 
14766 C CE1 . PHE   I  400 ? 0.30139 0.30139 0.30139 0.00000  0.00000  0.00000  400 PHE   E CE1 
14767 C CE2 . PHE   I  400 ? 0.45554 0.45554 0.45554 -0.00000 0.00000  0.00000  400 PHE   E CE2 
14768 C CZ  . PHE   I  400 ? 0.49246 0.49246 0.49246 0.00000  0.00000  0.00000  400 PHE   E CZ  
14769 N N   . GLY   I  401 ? 0.30004 0.30004 0.30004 -0.00000 0.00000  -0.00000 401 GLY   E N   
14770 C CA  . GLY   I  401 ? 0.24847 0.24847 0.24847 0.00000  0.00000  0.00000  401 GLY   E CA  
14771 C C   . GLY   I  401 ? 0.38094 0.38094 0.38094 -0.00000 0.00000  0.00000  401 GLY   E C   
14772 O O   . GLY   I  401 ? 0.45937 0.45937 0.45937 0.00000  0.00000  0.00000  401 GLY   E O   
14773 N N   . GLY   I  402 ? 0.42269 0.42269 0.42269 0.00000  0.00000  0.00000  402 GLY   E N   
14774 C CA  . GLY   I  402 ? 0.32904 0.32904 0.32904 0.00000  0.00000  0.00000  402 GLY   E CA  
14775 C C   . GLY   I  402 ? 0.69935 0.69935 0.69935 0.00000  0.00000  0.00000  402 GLY   E C   
14776 O O   . GLY   I  402 ? 0.46654 0.46654 0.46654 0.00000  0.00000  0.00000  402 GLY   E O   
14777 O OXT . GLY   I  402 ? 0.58284 0.58284 0.58284 -0.00000 0.00000  0.00000  402 GLY   E OXT 
14778 N N   . SER   J  1   ? 0.27567 0.27567 0.27567 0.00000  0.00000  0.00000  404 SER   F N   
14779 C CA  . SER   J  1   ? 0.21386 0.21386 0.21386 0.00000  0.00000  0.00000  404 SER   F CA  
14780 C C   . SER   J  1   ? 0.35856 0.35856 0.35856 0.00000  0.00000  0.00000  404 SER   F C   
14781 O O   . SER   J  1   ? 0.40309 0.40309 0.40309 0.00000  0.00000  0.00000  404 SER   F O   
14782 C CB  . SER   J  1   ? 0.29334 0.29334 0.29334 0.00000  0.00000  0.00000  404 SER   F CB  
14783 O OG  . SER   J  1   ? 0.32802 0.32802 0.32802 0.00000  0.00000  0.00000  404 SER   F OG  
14784 N N   . PHE   J  2   ? 0.24126 0.24126 0.24126 -0.00000 0.00000  0.00000  405 PHE   F N   
14785 C CA  . PHE   J  2   ? 0.32073 0.32073 0.32073 0.00000  0.00000  0.00000  405 PHE   F CA  
14786 C C   . PHE   J  2   ? 0.29123 0.29123 0.29123 0.00000  0.00000  0.00000  405 PHE   F C   
14787 O O   . PHE   J  2   ? 0.40899 0.40899 0.40899 0.00000  0.00000  0.00000  405 PHE   F O   
14788 C CB  . PHE   J  2   ? 0.32935 0.32935 0.32935 -0.00000 -0.00000 0.00000  405 PHE   F CB  
14789 C CG  . PHE   J  2   ? 0.36066 0.36066 0.36066 -0.00000 -0.00000 -0.00000 405 PHE   F CG  
14790 C CD1 . PHE   J  2   ? 0.44037 0.44037 0.44037 -0.00000 0.00000  0.00000  405 PHE   F CD1 
14791 C CD2 . PHE   J  2   ? 0.40417 0.40417 0.40417 0.00000  0.00000  0.00000  405 PHE   F CD2 
14792 C CE1 . PHE   J  2   ? 0.36094 0.36094 0.36094 0.00000  0.00000  0.00000  405 PHE   F CE1 
14793 C CE2 . PHE   J  2   ? 0.31202 0.31202 0.31202 -0.00000 0.00000  0.00000  405 PHE   F CE2 
14794 C CZ  . PHE   J  2   ? 0.39039 0.39039 0.39039 0.00000  0.00000  0.00000  405 PHE   F CZ  
14795 N N   . ALA   J  3   ? 0.29508 0.29508 0.29508 -0.00000 0.00000  0.00000  406 ALA   F N   
14796 C CA  . ALA   J  3   ? 0.34893 0.34893 0.34893 0.00000  0.00000  0.00000  406 ALA   F CA  
14797 C C   . ALA   J  3   ? 0.38870 0.38870 0.38870 0.00000  0.00000  0.00000  406 ALA   F C   
14798 O O   . ALA   J  3   ? 0.37488 0.37488 0.37488 0.00000  0.00000  0.00000  406 ALA   F O   
14799 C CB  . ALA   J  3   ? 0.14376 0.14376 0.14376 0.00000  -0.00000 0.00000  406 ALA   F CB  
14800 N N   . LEU   J  4   ? 0.36773 0.36773 0.36773 0.00000  0.00000  0.00000  407 LEU   F N   
14801 C CA  . LEU   J  4   ? 0.35859 0.35859 0.35859 0.00000  0.00000  0.00000  407 LEU   F CA  
14802 C C   . LEU   J  4   ? 0.17137 0.17137 0.17137 0.00000  -0.00000 0.00000  407 LEU   F C   
14803 O O   . LEU   J  4   ? 0.41907 0.41907 0.41907 0.00000  0.00000  0.00000  407 LEU   F O   
14804 C CB  . LEU   J  4   ? 0.21861 0.21861 0.21861 0.00000  0.00000  0.00000  407 LEU   F CB  
14805 C CG  . LEU   J  4   ? 0.36716 0.36716 0.36716 0.00000  0.00000  0.00000  407 LEU   F CG  
14806 C CD1 . LEU   J  4   ? 0.19485 0.19485 0.19485 -0.00000 0.00000  0.00000  407 LEU   F CD1 
14807 C CD2 . LEU   J  4   ? 0.27017 0.27017 0.27017 0.00000  0.00000  0.00000  407 LEU   F CD2 
14808 N N   . GLY   J  5   ? 0.43505 0.43505 0.43505 -0.00000 0.00000  0.00000  408 GLY   F N   
14809 C CA  . GLY   J  5   ? 0.14011 0.14011 0.14011 0.00000  0.00000  0.00000  408 GLY   F CA  
14810 C C   . GLY   J  5   ? 0.33673 0.33673 0.33673 0.00000  0.00000  0.00000  408 GLY   F C   
14811 O O   . GLY   J  5   ? 0.41684 0.41684 0.41684 0.00000  0.00000  0.00000  408 GLY   F O   
14812 N N   . LEU   J  6   ? 0.33057 0.33057 0.33057 -0.00000 0.00000  0.00000  409 LEU   F N   
14813 C CA  . LEU   J  6   ? 0.57571 0.57571 0.57571 0.00000  0.00000  0.00000  409 LEU   F CA  
14814 C C   . LEU   J  6   ? 0.49207 0.49207 0.49207 0.00000  0.00000  0.00000  409 LEU   F C   
14815 O O   . LEU   J  6   ? 0.55623 0.55623 0.55623 0.00000  0.00000  0.00000  409 LEU   F O   
14816 C CB  . LEU   J  6   ? 0.46529 0.46529 0.46529 -0.00000 0.00000  0.00000  409 LEU   F CB  
14817 C CG  . LEU   J  6   ? 0.55237 0.55237 0.55237 0.00000  0.00000  0.00000  409 LEU   F CG  
14818 C CD1 . LEU   J  6   ? 0.37610 0.37610 0.37610 0.00000  -0.00000 -0.00000 409 LEU   F CD1 
14819 C CD2 . LEU   J  6   ? 0.31976 0.31976 0.31976 -0.00000 0.00000  0.00000  409 LEU   F CD2 
14820 N N   . ARG   J  7   ? 0.43979 0.43979 0.43979 0.00000  0.00000  0.00000  410 ARG   F N   
14821 C CA  . ARG   J  7   ? 0.42367 0.42367 0.42367 -0.00000 0.00000  0.00000  410 ARG   F CA  
14822 C C   . ARG   J  7   ? 0.49838 0.49838 0.49838 0.00000  0.00000  0.00000  410 ARG   F C   
14823 O O   . ARG   J  7   ? 0.64102 0.64102 0.64102 0.00000  -0.00000 0.00000  410 ARG   F O   
14824 C CB  . ARG   J  7   ? 0.25712 0.25712 0.25712 0.00000  0.00000  0.00000  410 ARG   F CB  
14825 C CG  . ARG   J  7   ? 0.28255 0.28255 0.28255 0.00000  0.00000  0.00000  410 ARG   F CG  
14826 C CD  . ARG   J  7   ? 0.42498 0.42498 0.42498 0.00000  0.00000  0.00000  410 ARG   F CD  
14827 N NE  . ARG   J  7   ? 0.66680 0.66680 0.66680 0.00000  0.00000  0.00000  410 ARG   F NE  
14828 C CZ  . ARG   J  7   ? 0.55104 0.55104 0.55104 0.00000  0.00000  0.00000  410 ARG   F CZ  
14829 N NH1 . ARG   J  7   ? 0.59365 0.59365 0.59365 0.00000  0.00000  0.00000  410 ARG   F NH1 
14830 N NH2 . ARG   J  7   ? 0.66791 0.66791 0.66791 0.00000  -0.00000 0.00000  410 ARG   F NH2 
14831 N N   . LYS   J  8   ? 0.44598 0.44598 0.44598 0.00000  0.00000  0.00000  411 LYS   F N   
14832 C CA  . LYS   J  8   ? 0.67472 0.67472 0.67472 0.00000  0.00000  0.00000  411 LYS   F CA  
14833 C C   . LYS   J  8   ? 0.57625 0.57625 0.57625 -0.00000 0.00000  0.00000  411 LYS   F C   
14834 O O   . LYS   J  8   ? 0.53714 0.53714 0.53714 0.00000  0.00000  0.00000  411 LYS   F O   
14835 C CB  . LYS   J  8   ? 0.32162 0.32162 0.32162 0.00000  0.00000  0.00000  411 LYS   F CB  
14836 N N   . ASP   J  9   ? 0.48034 0.48034 0.48034 -0.00000 -0.00000 -0.00000 412 ASP   F N   
14837 C CA  . ASP   J  9   ? 1.13169 1.13169 1.13169 0.00000  0.00000  0.00000  412 ASP   F CA  
14838 C C   . ASP   J  9   ? 0.56578 0.56578 0.56578 0.00000  0.00000  0.00000  412 ASP   F C   
14839 O O   . ASP   J  9   ? 0.95304 0.95304 0.95304 0.00000  -0.00000 -0.00000 412 ASP   F O   
14840 C CB  . ASP   J  9   ? 0.79677 0.79677 0.79677 -0.00000 -0.00000 0.00000  412 ASP   F CB  
14841 C CG  . ASP   J  9   ? 0.91624 0.91624 0.91624 0.00000  0.00000  0.00000  412 ASP   F CG  
14842 O OD1 . ASP   J  9   ? 0.94904 0.94904 0.94904 0.00000  0.00000  0.00000  412 ASP   F OD1 
14843 O OD2 . ASP   J  9   ? 1.23605 1.23605 1.23605 0.00000  0.00000  0.00000  412 ASP   F OD2 
14844 N N   . CYS   J  10  ? 0.85284 0.85284 0.85284 0.00000  0.00000  0.00000  413 CYS   F N   
14845 C CA  . CYS   J  10  ? 0.56056 0.56056 0.56056 0.00000  0.00000  0.00000  413 CYS   F CA  
14846 C C   . CYS   J  10  ? 0.69415 0.69415 0.69415 0.00000  0.00000  0.00000  413 CYS   F C   
14847 O O   . CYS   J  10  ? 0.66887 0.66887 0.66887 0.00000  0.00000  0.00000  413 CYS   F O   
14848 C CB  . CYS   J  10  ? 0.45275 0.45275 0.45275 0.00000  0.00000  0.00000  413 CYS   F CB  
14849 S SG  . CYS   J  10  ? 0.60316 0.60316 0.60316 -0.00000 0.00000  0.00000  413 CYS   F SG  
14850 N N   . ARG   J  11  ? 0.53329 0.53329 0.53329 0.00000  0.00000  0.00000  414 ARG   F N   
14851 C CA  . ARG   J  11  ? 0.81655 0.81655 0.81655 0.00000  0.00000  0.00000  414 ARG   F CA  
14852 C C   . ARG   J  11  ? 0.96004 0.96004 0.96004 0.00000  0.00000  0.00000  414 ARG   F C   
14853 O O   . ARG   J  11  ? 0.61231 0.61231 0.61231 0.00000  0.00000  0.00000  414 ARG   F O   
14854 C CB  . ARG   J  11  ? 0.45749 0.45749 0.45749 0.00000  0.00000  0.00000  414 ARG   F CB  
14855 N N   . ALA   J  12  ? 0.82458 0.82458 0.82458 0.00000  0.00000  0.00000  415 ALA   F N   
14856 C CA  . ALA   J  12  ? 0.68400 0.68400 0.68400 0.00000  0.00000  0.00000  415 ALA   F CA  
14857 C C   . ALA   J  12  ? 0.60648 0.60648 0.60648 -0.00000 0.00000  0.00000  415 ALA   F C   
14858 O O   . ALA   J  12  ? 0.95667 0.95667 0.95667 0.00000  0.00000  0.00000  415 ALA   F O   
14859 C CB  . ALA   J  12  ? 0.42663 0.42663 0.42663 -0.00000 0.00000  0.00000  415 ALA   F CB  
14860 N N   . GLU   J  13  ? 0.36576 0.36576 0.36576 0.00000  0.00000  0.00000  416 GLU   F N   
14861 C CA  . GLU   J  13  ? 0.53906 0.53906 0.53906 0.00000  0.00000  0.00000  416 GLU   F CA  
14862 C C   . GLU   J  13  ? 0.56819 0.56819 0.56819 0.00000  0.00000  0.00000  416 GLU   F C   
14863 O O   . GLU   J  13  ? 0.63364 0.63364 0.63364 0.00000  0.00000  0.00000  416 GLU   F O   
14864 C CB  . GLU   J  13  ? 0.40327 0.40327 0.40327 0.00000  0.00000  0.00000  416 GLU   F CB  
14865 N N   . ILE   J  14  ? 0.48688 0.48688 0.48688 0.00000  0.00000  0.00000  417 ILE   F N   
14866 C CA  . ILE   J  14  ? 0.58473 0.58473 0.58473 0.00000  0.00000  0.00000  417 ILE   F CA  
14867 C C   . ILE   J  14  ? 0.45988 0.45988 0.45988 0.00000  0.00000  0.00000  417 ILE   F C   
14868 O O   . ILE   J  14  ? 0.56548 0.56548 0.56548 0.00000  0.00000  0.00000  417 ILE   F O   
14869 C CB  . ILE   J  14  ? 0.33602 0.33602 0.33602 0.00000  0.00000  0.00000  417 ILE   F CB  
14870 C CG1 . ILE   J  14  ? 0.37871 0.37871 0.37871 0.00000  0.00000  0.00000  417 ILE   F CG1 
14871 C CG2 . ILE   J  14  ? 0.42489 0.42489 0.42489 0.00000  0.00000  0.00000  417 ILE   F CG2 
14872 C CD1 . ILE   J  14  ? 0.50620 0.50620 0.50620 0.00000  0.00000  0.00000  417 ILE   F CD1 
14873 N N   . VAL   J  15  ? 0.57779 0.57779 0.57779 0.00000  0.00000  0.00000  418 VAL   F N   
14874 C CA  . VAL   J  15  ? 0.34601 0.34601 0.34601 0.00000  0.00000  0.00000  418 VAL   F CA  
14875 C C   . VAL   J  15  ? 0.39407 0.39407 0.39407 0.00000  0.00000  0.00000  418 VAL   F C   
14876 O O   . VAL   J  15  ? 0.64869 0.64869 0.64869 -0.00000 0.00000  0.00000  418 VAL   F O   
14877 C CB  . VAL   J  15  ? 0.64191 0.64191 0.64191 0.00000  0.00000  0.00000  418 VAL   F CB  
14878 C CG1 . VAL   J  15  ? 0.24059 0.24059 0.24059 -0.00000 0.00000  0.00000  418 VAL   F CG1 
14879 C CG2 . VAL   J  15  ? 0.21866 0.21866 0.21866 0.00000  0.00000  0.00000  418 VAL   F CG2 
14880 N N   . GLU   J  16  ? 0.50052 0.50052 0.50052 0.00000  0.00000  0.00000  419 GLU   F N   
14881 C CA  . GLU   J  16  ? 0.36718 0.36718 0.36718 -0.00000 0.00000  0.00000  419 GLU   F CA  
14882 C C   . GLU   J  16  ? 0.49941 0.49941 0.49941 0.00000  0.00000  0.00000  419 GLU   F C   
14883 O O   . GLU   J  16  ? 0.50093 0.50093 0.50093 0.00000  0.00000  0.00000  419 GLU   F O   
14884 C CB  . GLU   J  16  ? 0.37595 0.37595 0.37595 0.00000  0.00000  0.00000  419 GLU   F CB  
14885 C CG  . GLU   J  16  ? 1.32853 1.32853 1.32853 -0.00000 0.00000  0.00000  419 GLU   F CG  
14886 C CD  . GLU   J  16  ? 1.61485 1.61485 1.61485 -0.00000 -0.00000 0.00000  419 GLU   F CD  
14887 O OE1 . GLU   J  16  ? 1.11968 1.11968 1.11968 0.00000  0.00000  0.00000  419 GLU   F OE1 
14888 O OE2 . GLU   J  16  ? 1.20321 1.20321 1.20321 0.00000  0.00000  -0.00000 419 GLU   F OE2 
14889 N N   . LYS   J  17  ? 0.41778 0.41778 0.41778 0.00000  0.00000  0.00000  420 LYS   F N   
14890 C CA  . LYS   J  17  ? 0.44636 0.44636 0.44636 0.00000  0.00000  0.00000  420 LYS   F CA  
14891 C C   . LYS   J  17  ? 0.52892 0.52892 0.52892 -0.00000 0.00000  0.00000  420 LYS   F C   
14892 O O   . LYS   J  17  ? 0.50867 0.50867 0.50867 0.00000  0.00000  0.00000  420 LYS   F O   
14893 C CB  . LYS   J  17  ? 0.22439 0.22439 0.22439 -0.00000 0.00000  0.00000  420 LYS   F CB  
14894 C CG  . LYS   J  17  ? 0.28772 0.28772 0.28772 0.00000  0.00000  0.00000  420 LYS   F CG  
14895 C CD  . LYS   J  17  ? 0.55542 0.55542 0.55542 0.00000  0.00000  0.00000  420 LYS   F CD  
14896 C CE  . LYS   J  17  ? 0.67949 0.67949 0.67949 0.00000  0.00000  0.00000  420 LYS   F CE  
14897 N NZ  . LYS   J  17  ? 0.96946 0.96946 0.96946 -0.00000 0.00000  0.00000  420 LYS   F NZ  
14898 N N   . PHE   J  18  ? 0.47236 0.47236 0.47236 0.00000  0.00000  0.00000  421 PHE   F N   
14899 C CA  . PHE   J  18  ? 0.77224 0.77224 0.77224 -0.00000 0.00000  0.00000  421 PHE   F CA  
14900 C C   . PHE   J  18  ? 0.61022 0.61022 0.61022 -0.00000 0.00000  0.00000  421 PHE   F C   
14901 O O   . PHE   J  18  ? 0.54327 0.54327 0.54327 -0.00000 0.00000  0.00000  421 PHE   F O   
14902 C CB  . PHE   J  18  ? 0.33084 0.33084 0.33084 -0.00000 0.00000  0.00000  421 PHE   F CB  
14903 C CG  . PHE   J  18  ? 0.47307 0.47307 0.47307 -0.00000 0.00000  0.00000  421 PHE   F CG  
14904 C CD1 . PHE   J  18  ? 0.46597 0.46597 0.46597 0.00000  0.00000  0.00000  421 PHE   F CD1 
14905 C CD2 . PHE   J  18  ? 0.68616 0.68616 0.68616 -0.00000 0.00000  0.00000  421 PHE   F CD2 
14906 C CE1 . PHE   J  18  ? 0.36863 0.36863 0.36863 0.00000  0.00000  0.00000  421 PHE   F CE1 
14907 C CE2 . PHE   J  18  ? 0.56440 0.56440 0.56440 -0.00000 0.00000  0.00000  421 PHE   F CE2 
14908 C CZ  . PHE   J  18  ? 0.63623 0.63623 0.63623 0.00000  0.00000  0.00000  421 PHE   F CZ  
14909 N N   . THR   J  19  ? 0.51621 0.51621 0.51621 0.00000  -0.00000 0.00000  422 THR   F N   
14910 C CA  . THR   J  19  ? 0.39237 0.39237 0.39237 0.00000  0.00000  0.00000  422 THR   F CA  
14911 C C   . THR   J  19  ? 0.49429 0.49429 0.49429 0.00000  0.00000  0.00000  422 THR   F C   
14912 O O   . THR   J  19  ? 0.47068 0.47068 0.47068 -0.00000 0.00000  0.00000  422 THR   F O   
14913 C CB  . THR   J  19  ? 0.53959 0.53959 0.53959 0.00000  -0.00000 0.00000  422 THR   F CB  
14914 O OG1 . THR   J  19  ? 0.49151 0.49151 0.49151 -0.00000 0.00000  0.00000  422 THR   F OG1 
14915 C CG2 . THR   J  19  ? 0.56393 0.56393 0.56393 0.00000  0.00000  0.00000  422 THR   F CG2 
14916 N N   . GLU   J  20  ? 0.56778 0.56778 0.56778 0.00000  0.00000  0.00000  423 GLU   F N   
14917 C CA  . GLU   J  20  ? 0.54612 0.54612 0.54612 0.00000  0.00000  0.00000  423 GLU   F CA  
14918 C C   . GLU   J  20  ? 0.42517 0.42517 0.42517 0.00000  0.00000  0.00000  423 GLU   F C   
14919 O O   . GLU   J  20  ? 0.62493 0.62493 0.62493 -0.00000 -0.00000 0.00000  423 GLU   F O   
14920 C CB  . GLU   J  20  ? 0.37228 0.37228 0.37228 0.00000  0.00000  0.00000  423 GLU   F CB  
14921 C CG  . GLU   J  20  ? 0.22462 0.22462 0.22462 0.00000  0.00000  0.00000  423 GLU   F CG  
14922 C CD  . GLU   J  20  ? 1.46815 1.46815 1.46815 -0.00000 0.00000  0.00000  423 GLU   F CD  
14923 O OE1 . GLU   J  20  ? 1.00925 1.00925 1.00925 0.00000  0.00000  0.00000  423 GLU   F OE1 
14924 O OE2 . GLU   J  20  ? 1.05680 1.05680 1.05680 0.00000  0.00000  0.00000  423 GLU   F OE2 
14925 N N   . PRO   J  21  ? 0.45108 0.45108 0.45108 0.00000  0.00000  0.00000  424 PRO   F N   
14926 C CA  . PRO   J  21  ? 0.62130 0.62130 0.62130 -0.00000 0.00000  0.00000  424 PRO   F CA  
14927 C C   . PRO   J  21  ? 0.43911 0.43911 0.43911 0.00000  0.00000  0.00000  424 PRO   F C   
14928 O O   . PRO   J  21  ? 0.54926 0.54926 0.54926 0.00000  0.00000  -0.00000 424 PRO   F O   
14929 C CB  . PRO   J  21  ? 0.22243 0.22243 0.22243 0.00000  0.00000  0.00000  424 PRO   F CB  
14930 C CG  . PRO   J  21  ? 0.41391 0.41391 0.41391 -0.00000 0.00000  0.00000  424 PRO   F CG  
14931 C CD  . PRO   J  21  ? 0.39733 0.39733 0.39733 0.00000  0.00000  0.00000  424 PRO   F CD  
14932 N N   . GLY   J  22  ? 0.51326 0.51326 0.51326 -0.00000 0.00000  0.00000  425 GLY   F N   
14933 C CA  . GLY   J  22  ? 0.29387 0.29387 0.29387 -0.00000 0.00000  0.00000  425 GLY   F CA  
14934 C C   . GLY   J  22  ? 0.40329 0.40329 0.40329 0.00000  0.00000  0.00000  425 GLY   F C   
14935 O O   . GLY   J  22  ? 0.47774 0.47774 0.47774 0.00000  0.00000  0.00000  425 GLY   F O   
14936 N N   . THR   J  23  ? 0.36460 0.36460 0.36460 0.00000  0.00000  0.00000  426 THR   F N   
14937 C CA  . THR   J  23  ? 0.33508 0.33508 0.33508 -0.00000 0.00000  0.00000  426 THR   F CA  
14938 C C   . THR   J  23  ? 0.33474 0.33474 0.33474 -0.00000 0.00000  0.00000  426 THR   F C   
14939 O O   . THR   J  23  ? 0.70546 0.70546 0.70546 -0.00000 -0.00000 0.00000  426 THR   F O   
14940 C CB  . THR   J  23  ? 0.44491 0.44491 0.44491 -0.00000 0.00000  0.00000  426 THR   F CB  
14941 O OG1 . THR   J  23  ? 0.55002 0.55002 0.55002 -0.00000 0.00000  0.00000  426 THR   F OG1 
14942 C CG2 . THR   J  23  ? 0.32382 0.32382 0.32382 0.00000  0.00000  0.00000  426 THR   F CG2 
14943 N N   . VAL   J  24  ? 0.62517 0.62517 0.62517 0.00000  0.00000  0.00000  427 VAL   F N   
14944 C CA  . VAL   J  24  ? 0.38661 0.38661 0.38661 0.00000  0.00000  0.00000  427 VAL   F CA  
14945 C C   . VAL   J  24  ? 0.31639 0.31639 0.31639 -0.00000 0.00000  0.00000  427 VAL   F C   
14946 O O   . VAL   J  24  ? 0.63118 0.63118 0.63118 0.00000  0.00000  0.00000  427 VAL   F O   
14947 C CB  . VAL   J  24  ? 0.29629 0.29629 0.29629 0.00000  0.00000  0.00000  427 VAL   F CB  
14948 C CG1 . VAL   J  24  ? 0.20433 0.20433 0.20433 0.00000  0.00000  0.00000  427 VAL   F CG1 
14949 C CG2 . VAL   J  24  ? 0.29561 0.29561 0.29561 0.00000  0.00000  0.00000  427 VAL   F CG2 
14950 N N   . ILE   J  25  ? 0.70418 0.70418 0.70418 0.00000  0.00000  0.00000  428 ILE   F N   
14951 C CA  . ILE   J  25  ? 0.31025 0.31025 0.31025 0.00000  -0.00000 0.00000  428 ILE   F CA  
14952 C C   . ILE   J  25  ? 0.58144 0.58144 0.58144 -0.00000 0.00000  0.00000  428 ILE   F C   
14953 O O   . ILE   J  25  ? 0.47126 0.47126 0.47126 -0.00000 0.00000  0.00000  428 ILE   F O   
14954 C CB  . ILE   J  25  ? 0.54337 0.54337 0.54337 -0.00000 0.00000  0.00000  428 ILE   F CB  
14955 C CG1 . ILE   J  25  ? 0.42772 0.42772 0.42772 0.00000  0.00000  0.00000  428 ILE   F CG1 
14956 C CG2 . ILE   J  25  ? 0.27528 0.27528 0.27528 0.00000  0.00000  0.00000  428 ILE   F CG2 
14957 C CD1 . ILE   J  25  ? 0.35970 0.35970 0.35970 0.00000  0.00000  0.00000  428 ILE   F CD1 
14958 N N   . ARG   J  26  ? 0.44038 0.44038 0.44038 -0.00000 0.00000  0.00000  429 ARG   F N   
14959 C CA  . ARG   J  26  ? 0.42534 0.42534 0.42534 0.00000  0.00000  0.00000  429 ARG   F CA  
14960 C C   . ARG   J  26  ? 0.43205 0.43205 0.43205 0.00000  0.00000  0.00000  429 ARG   F C   
14961 O O   . ARG   J  26  ? 0.41989 0.41989 0.41989 -0.00000 0.00000  0.00000  429 ARG   F O   
14962 C CB  . ARG   J  26  ? 0.52685 0.52685 0.52685 -0.00000 0.00000  0.00000  429 ARG   F CB  
14963 C CG  . ARG   J  26  ? 0.44804 0.44804 0.44804 -0.00000 0.00000  0.00000  429 ARG   F CG  
14964 C CD  . ARG   J  26  ? 0.62057 0.62057 0.62057 -0.00000 0.00000  0.00000  429 ARG   F CD  
14965 N NE  . ARG   J  26  ? 0.44051 0.44051 0.44051 -0.00000 0.00000  0.00000  429 ARG   F NE  
14966 C CZ  . ARG   J  26  ? 2.11869 2.11869 2.11869 0.00000  0.00000  0.00000  429 ARG   F CZ  
14967 N NH1 . ARG   J  26  ? 0.38526 0.38526 0.38526 0.00000  0.00000  0.00000  429 ARG   F NH1 
14968 N NH2 . ARG   J  26  ? 0.47172 0.47172 0.47172 0.00000  -0.00000 0.00000  429 ARG   F NH2 
14969 N N   . ILE   J  27  ? 0.26224 0.26224 0.26224 -0.00000 -0.00000 0.00000  430 ILE   F N   
14970 C CA  . ILE   J  27  ? 0.48253 0.48253 0.48253 -0.00000 0.00000  0.00000  430 ILE   F CA  
14971 C C   . ILE   J  27  ? 0.32588 0.32588 0.32588 0.00000  0.00000  0.00000  430 ILE   F C   
14972 O O   . ILE   J  27  ? 0.66534 0.66534 0.66534 0.00000  -0.00000 0.00000  430 ILE   F O   
14973 C CB  . ILE   J  27  ? 0.40026 0.40026 0.40026 0.00000  0.00000  0.00000  430 ILE   F CB  
14974 C CG1 . ILE   J  27  ? 0.33041 0.33041 0.33041 0.00000  0.00000  0.00000  430 ILE   F CG1 
14975 C CG2 . ILE   J  27  ? 0.37638 0.37638 0.37638 -0.00000 0.00000  0.00000  430 ILE   F CG2 
14976 C CD1 . ILE   J  27  ? 0.29473 0.29473 0.29473 -0.00000 0.00000  0.00000  430 ILE   F CD1 
14977 N N   . ASN   J  28  ? 0.66603 0.66603 0.66603 -0.00000 0.00000  0.00000  431 ASN   F N   
14978 C CA  . ASN   J  28  ? 0.40578 0.40578 0.40578 0.00000  0.00000  0.00000  431 ASN   F CA  
14979 C C   . ASN   J  28  ? 0.55229 0.55229 0.55229 0.00000  0.00000  0.00000  431 ASN   F C   
14980 O O   . ASN   J  28  ? 0.43254 0.43254 0.43254 -0.00000 0.00000  0.00000  431 ASN   F O   
14981 C CB  . ASN   J  28  ? 0.35094 0.35094 0.35094 0.00000  0.00000  0.00000  431 ASN   F CB  
14982 C CG  . ASN   J  28  ? 0.50177 0.50177 0.50177 0.00000  0.00000  0.00000  431 ASN   F CG  
14983 O OD1 . ASN   J  28  ? 0.56447 0.56447 0.56447 0.00000  0.00000  0.00000  431 ASN   F OD1 
14984 N ND2 . ASN   J  28  ? 0.40232 0.40232 0.40232 -0.00000 0.00000  0.00000  431 ASN   F ND2 
14985 N N   . GLU   J  29  ? 0.40545 0.40545 0.40545 0.00000  0.00000  0.00000  432 GLU   F N   
14986 C CA  . GLU   J  29  ? 0.51495 0.51495 0.51495 0.00000  0.00000  0.00000  432 GLU   F CA  
14987 C C   . GLU   J  29  ? 0.46147 0.46147 0.46147 -0.00000 0.00000  0.00000  432 GLU   F C   
14988 O O   . GLU   J  29  ? 0.65730 0.65730 0.65730 -0.00000 0.00000  0.00000  432 GLU   F O   
14989 C CB  . GLU   J  29  ? 0.31454 0.31454 0.31454 0.00000  0.00000  0.00000  432 GLU   F CB  
14990 C CG  . GLU   J  29  ? 0.48275 0.48275 0.48275 -0.00000 0.00000  0.00000  432 GLU   F CG  
14991 C CD  . GLU   J  29  ? 0.79151 0.79151 0.79151 0.00000  0.00000  0.00000  432 GLU   F CD  
14992 O OE1 . GLU   J  29  ? 0.60171 0.60171 0.60171 0.00000  0.00000  0.00000  432 GLU   F OE1 
14993 O OE2 . GLU   J  29  ? 0.68091 0.68091 0.68091 -0.00000 0.00000  0.00000  432 GLU   F OE2 
14994 N N   . VAL   J  30  ? 0.57752 0.57752 0.57752 -0.00000 0.00000  0.00000  433 VAL   F N   
14995 C CA  . VAL   J  30  ? 0.26490 0.26490 0.26490 0.00000  0.00000  0.00000  433 VAL   F CA  
14996 C C   . VAL   J  30  ? 0.51950 0.51950 0.51950 0.00000  0.00000  0.00000  433 VAL   F C   
14997 O O   . VAL   J  30  ? 0.40344 0.40344 0.40344 0.00000  0.00000  0.00000  433 VAL   F O   
14998 C CB  . VAL   J  30  ? 0.53026 0.53026 0.53026 -0.00000 0.00000  0.00000  433 VAL   F CB  
14999 C CG1 . VAL   J  30  ? 0.40143 0.40143 0.40143 -0.00000 0.00000  0.00000  433 VAL   F CG1 
15000 C CG2 . VAL   J  30  ? 0.33526 0.33526 0.33526 -0.00000 0.00000  0.00000  433 VAL   F CG2 
15001 N N   . VAL   J  31  ? 0.42632 0.42632 0.42632 0.00000  0.00000  0.00000  434 VAL   F N   
15002 C CA  . VAL   J  31  ? 0.56667 0.56667 0.56667 0.00000  0.00000  0.00000  434 VAL   F CA  
15003 C C   . VAL   J  31  ? 0.40958 0.40958 0.40958 0.00000  0.00000  0.00000  434 VAL   F C   
15004 O O   . VAL   J  31  ? 0.39922 0.39922 0.39922 0.00000  0.00000  0.00000  434 VAL   F O   
15005 C CB  . VAL   J  31  ? 0.44407 0.44407 0.44407 0.00000  0.00000  -0.00000 434 VAL   F CB  
15006 C CG1 . VAL   J  31  ? 0.23845 0.23845 0.23845 0.00000  0.00000  -0.00000 434 VAL   F CG1 
15007 C CG2 . VAL   J  31  ? 0.27111 0.27111 0.27111 -0.00000 0.00000  0.00000  434 VAL   F CG2 
15008 N N   . ALA   J  32  ? 0.38935 0.38935 0.38935 0.00000  0.00000  0.00000  435 ALA   F N   
15009 C CA  . ALA   J  32  ? 0.43086 0.43086 0.43086 0.00000  0.00000  0.00000  435 ALA   F CA  
15010 C C   . ALA   J  32  ? 0.55678 0.55678 0.55678 0.00000  0.00000  0.00000  435 ALA   F C   
15011 O O   . ALA   J  32  ? 0.45634 0.45634 0.45634 0.00000  0.00000  0.00000  435 ALA   F O   
15012 C CB  . ALA   J  32  ? 0.35104 0.35104 0.35104 0.00000  0.00000  0.00000  435 ALA   F CB  
15013 N N   . ALA   J  33  ? 0.44987 0.44987 0.44987 0.00000  0.00000  0.00000  436 ALA   F N   
15014 C CA  . ALA   J  33  ? 0.56384 0.56384 0.56384 0.00000  0.00000  0.00000  436 ALA   F CA  
15015 C C   . ALA   J  33  ? 0.81236 0.81236 0.81236 0.00000  0.00000  0.00000  436 ALA   F C   
15016 O O   . ALA   J  33  ? 0.52608 0.52608 0.52608 -0.00000 0.00000  0.00000  436 ALA   F O   
15017 C CB  . ALA   J  33  ? 0.36250 0.36250 0.36250 0.00000  0.00000  0.00000  436 ALA   F CB  
15018 N N   . LEU   J  34  ? 0.53390 0.53390 0.53390 0.00000  0.00000  0.00000  437 LEU   F N   
15019 C CA  . LEU   J  34  ? 0.91036 0.91036 0.91036 -0.00000 0.00000  0.00000  437 LEU   F CA  
15020 C C   . LEU   J  34  ? 0.50343 0.50343 0.50343 0.00000  0.00000  0.00000  437 LEU   F C   
15021 O O   . LEU   J  34  ? 0.58877 0.58877 0.58877 0.00000  0.00000  0.00000  437 LEU   F O   
15022 C CB  . LEU   J  34  ? 0.48851 0.48851 0.48851 -0.00000 0.00000  0.00000  437 LEU   F CB  
15023 C CG  . LEU   J  34  ? 0.80669 0.80669 0.80669 -0.00000 0.00000  0.00000  437 LEU   F CG  
15024 C CD1 . LEU   J  34  ? 0.56802 0.56802 0.56802 0.00000  0.00000  0.00000  437 LEU   F CD1 
15025 C CD2 . LEU   J  34  ? 0.84158 0.84158 0.84158 -0.00000 0.00000  0.00000  437 LEU   F CD2 
15026 N N   . GLY   K  56  ? 0.54333 0.54333 0.54333 0.00000  0.00000  0.00000  56  GLY   K N   
15027 C CA  . GLY   K  56  ? 0.81732 0.81732 0.81732 0.00000  0.00000  0.00000  56  GLY   K CA  
15028 C C   . GLY   K  56  ? 1.11176 1.11176 1.11176 0.00000  0.00000  0.00000  56  GLY   K C   
15029 O O   . GLY   K  56  ? 1.10109 1.10109 1.10109 0.00000  0.00000  0.00000  56  GLY   K O   
15030 N N   . LEU   K  57  ? 0.60307 0.60307 0.60307 0.00000  0.00000  0.00000  57  LEU   K N   
15031 C CA  . LEU   K  57  ? 0.56377 0.56377 0.56377 -0.00000 0.00000  0.00000  57  LEU   K CA  
15032 C C   . LEU   K  57  ? 0.76822 0.76822 0.76822 -0.00000 0.00000  0.00000  57  LEU   K C   
15033 O O   . LEU   K  57  ? 0.79347 0.79347 0.79347 0.00000  0.00000  0.00000  57  LEU   K O   
15034 C CB  . LEU   K  57  ? 0.52128 0.52128 0.52128 -0.00000 0.00000  0.00000  57  LEU   K CB  
15035 C CG  . LEU   K  57  ? 0.72727 0.72727 0.72727 0.00000  0.00000  0.00000  57  LEU   K CG  
15036 C CD1 . LEU   K  57  ? 0.63083 0.63083 0.63083 0.00000  0.00000  0.00000  57  LEU   K CD1 
15037 C CD2 . LEU   K  57  ? 0.70782 0.70782 0.70782 0.00000  0.00000  0.00000  57  LEU   K CD2 
15038 N N   . MET   K  58  ? 0.71795 0.71795 0.71795 -0.00000 0.00000  0.00000  58  MET   K N   
15039 C CA  . MET   K  58  ? 0.70400 0.70400 0.70400 -0.00000 0.00000  0.00000  58  MET   K CA  
15040 C C   . MET   K  58  ? 0.58632 0.58632 0.58632 -0.00000 0.00000  0.00000  58  MET   K C   
15041 O O   . MET   K  58  ? 0.84805 0.84805 0.84805 0.00000  0.00000  0.00000  58  MET   K O   
15042 C CB  . MET   K  58  ? 0.61462 0.61462 0.61462 -0.00000 -0.00000 0.00000  58  MET   K CB  
15043 C CG  . MET   K  58  ? 0.80842 0.80842 0.80842 0.00000  -0.00000 0.00000  58  MET   K CG  
15044 S SD  . MET   K  58  ? 0.88270 0.88270 0.88270 0.00000  0.00000  0.00000  58  MET   K SD  
15045 C CE  . MET   K  58  ? 0.58667 0.58667 0.58667 -0.00000 0.00000  0.00000  58  MET   K CE  
15046 N N   . GLN   K  59  ? 0.76182 0.76182 0.76182 0.00000  0.00000  0.00000  59  GLN   K N   
15047 C CA  . GLN   K  59  ? 0.62045 0.62045 0.62045 -0.00000 0.00000  0.00000  59  GLN   K CA  
15048 C C   . GLN   K  59  ? 0.74368 0.74368 0.74368 0.00000  0.00000  0.00000  59  GLN   K C   
15049 O O   . GLN   K  59  ? 0.66833 0.66833 0.66833 0.00000  0.00000  0.00000  59  GLN   K O   
15050 C CB  . GLN   K  59  ? 0.54129 0.54129 0.54129 0.00000  0.00000  0.00000  59  GLN   K CB  
15051 C CG  . GLN   K  59  ? 0.91557 0.91557 0.91557 -0.00000 0.00000  0.00000  59  GLN   K CG  
15052 C CD  . GLN   K  59  ? 1.20170 1.20170 1.20170 -0.00000 0.00000  0.00000  59  GLN   K CD  
15053 O OE1 . GLN   K  59  ? 1.34841 1.34841 1.34841 -0.00000 -0.00000 0.00000  59  GLN   K OE1 
15054 N NE2 . GLN   K  59  ? 1.00700 1.00700 1.00700 -0.00000 0.00000  0.00000  59  GLN   K NE2 
15055 N N   . PRO   K  60  ? 0.77788 0.77788 0.77788 0.00000  0.00000  0.00000  60  PRO   K N   
15056 C CA  . PRO   K  60  ? 0.54636 0.54636 0.54636 0.00000  0.00000  0.00000  60  PRO   K CA  
15057 C C   . PRO   K  60  ? 0.85144 0.85144 0.85144 0.00000  0.00000  0.00000  60  PRO   K C   
15058 O O   . PRO   K  60  ? 0.58678 0.58678 0.58678 0.00000  0.00000  0.00000  60  PRO   K O   
15059 C CB  . PRO   K  60  ? 0.55603 0.55603 0.55603 0.00000  0.00000  0.00000  60  PRO   K CB  
15060 C CG  . PRO   K  60  ? 0.64454 0.64454 0.64454 -0.00000 0.00000  0.00000  60  PRO   K CG  
15061 C CD  . PRO   K  60  ? 0.49609 0.49609 0.49609 0.00000  0.00000  0.00000  60  PRO   K CD  
15062 N N   . ILE   K  61  ? 0.40700 0.40700 0.40700 0.00000  0.00000  0.00000  61  ILE   K N   
15063 C CA  . ILE   K  61  ? 0.71519 0.71519 0.71519 -0.00000 0.00000  0.00000  61  ILE   K CA  
15064 C C   . ILE   K  61  ? 0.54192 0.54192 0.54192 -0.00000 0.00000  0.00000  61  ILE   K C   
15065 O O   . ILE   K  61  ? 0.59681 0.59681 0.59681 0.00000  0.00000  0.00000  61  ILE   K O   
15066 C CB  . ILE   K  61  ? 0.53649 0.53649 0.53649 -0.00000 0.00000  0.00000  61  ILE   K CB  
15067 C CG1 . ILE   K  61  ? 0.41683 0.41683 0.41683 0.00000  0.00000  0.00000  61  ILE   K CG1 
15068 C CG2 . ILE   K  61  ? 0.39324 0.39324 0.39324 0.00000  0.00000  0.00000  61  ILE   K CG2 
15069 C CD1 . ILE   K  61  ? 0.50028 0.50028 0.50028 -0.00000 0.00000  0.00000  61  ILE   K CD1 
15070 N N   . GLN   K  62  ? 0.87446 0.87446 0.87446 0.00000  0.00000  0.00000  62  GLN   K N   
15071 C CA  . GLN   K  62  ? 0.24162 0.24162 0.24162 0.00000  0.00000  0.00000  62  GLN   K CA  
15072 C C   . GLN   K  62  ? 0.44221 0.44221 0.44221 -0.00000 0.00000  0.00000  62  GLN   K C   
15073 O O   . GLN   K  62  ? 0.35365 0.35365 0.35365 0.00000  0.00000  0.00000  62  GLN   K O   
15074 C CB  . GLN   K  62  ? 0.90435 0.90435 0.90435 -0.00000 0.00000  0.00000  62  GLN   K CB  
15075 C CG  . GLN   K  62  ? 1.50622 1.50622 1.50622 -0.00000 0.00000  0.00000  62  GLN   K CG  
15076 C CD  . GLN   K  62  ? 1.44172 1.44172 1.44172 0.00000  0.00000  0.00000  62  GLN   K CD  
15077 O OE1 . GLN   K  62  ? 1.91643 1.91643 1.91643 0.00000  0.00000  0.00000  62  GLN   K OE1 
15078 N NE2 . GLN   K  62  ? 1.11417 1.11417 1.11417 -0.00000 0.00000  0.00000  62  GLN   K NE2 
15079 N N   . GLU   K  63  ? 0.43977 0.43977 0.43977 -0.00000 0.00000  0.00000  63  GLU   K N   
15080 C CA  . GLU   K  63  ? 0.64035 0.64035 0.64035 -0.00000 0.00000  0.00000  63  GLU   K CA  
15081 C C   . GLU   K  63  ? 0.66846 0.66846 0.66846 0.00000  0.00000  0.00000  63  GLU   K C   
15082 O O   . GLU   K  63  ? 0.58386 0.58386 0.58386 -0.00000 0.00000  0.00000  63  GLU   K O   
15083 C CB  . GLU   K  63  ? 0.43922 0.43922 0.43922 0.00000  0.00000  0.00000  63  GLU   K CB  
15084 C CG  . GLU   K  63  ? 0.91511 0.91511 0.91511 0.00000  0.00000  0.00000  63  GLU   K CG  
15085 C CD  . GLU   K  63  ? 0.74783 0.74783 0.74783 0.00000  0.00000  0.00000  63  GLU   K CD  
15086 O OE1 . GLU   K  63  ? 1.33625 1.33625 1.33625 0.00000  0.00000  0.00000  63  GLU   K OE1 
15087 O OE2 . GLU   K  63  ? 1.68573 1.68573 1.68573 0.00000  0.00000  0.00000  63  GLU   K OE2 
15088 N N   . PHE   K  64  ? 0.59075 0.59075 0.59075 -0.00000 0.00000  0.00000  64  PHE   K N   
15089 C CA  . PHE   K  64  ? 0.50778 0.50778 0.50778 -0.00000 0.00000  0.00000  64  PHE   K CA  
15090 C C   . PHE   K  64  ? 0.68555 0.68555 0.68555 0.00000  0.00000  0.00000  64  PHE   K C   
15091 O O   . PHE   K  64  ? 0.61664 0.61664 0.61664 0.00000  0.00000  0.00000  64  PHE   K O   
15092 C CB  . PHE   K  64  ? 0.54696 0.54696 0.54696 -0.00000 0.00000  0.00000  64  PHE   K CB  
15093 C CG  . PHE   K  64  ? 0.61248 0.61248 0.61248 0.00000  0.00000  0.00000  64  PHE   K CG  
15094 C CD1 . PHE   K  64  ? 0.71310 0.71310 0.71310 0.00000  0.00000  0.00000  64  PHE   K CD1 
15095 C CD2 . PHE   K  64  ? 0.47360 0.47360 0.47360 -0.00000 0.00000  0.00000  64  PHE   K CD2 
15096 C CE1 . PHE   K  64  ? 0.53569 0.53569 0.53569 0.00000  0.00000  0.00000  64  PHE   K CE1 
15097 C CE2 . PHE   K  64  ? 0.45144 0.45144 0.45144 -0.00000 0.00000  0.00000  64  PHE   K CE2 
15098 C CZ  . PHE   K  64  ? 0.56210 0.56210 0.56210 0.00000  0.00000  0.00000  64  PHE   K CZ  
15099 N N   . LYS   K  65  ? 0.53230 0.53230 0.53230 0.00000  0.00000  0.00000  65  LYS   K N   
15100 C CA  . LYS   K  65  ? 0.46817 0.46817 0.46817 0.00000  0.00000  0.00000  65  LYS   K CA  
15101 C C   . LYS   K  65  ? 0.72384 0.72384 0.72384 0.00000  0.00000  0.00000  65  LYS   K C   
15102 O O   . LYS   K  65  ? 0.61689 0.61689 0.61689 -0.00000 0.00000  0.00000  65  LYS   K O   
15103 C CB  . LYS   K  65  ? 0.56009 0.56009 0.56009 0.00000  0.00000  0.00000  65  LYS   K CB  
15104 C CG  . LYS   K  65  ? 0.57320 0.57320 0.57320 -0.00000 0.00000  0.00000  65  LYS   K CG  
15105 C CD  . LYS   K  65  ? 0.70661 0.70661 0.70661 0.00000  0.00000  0.00000  65  LYS   K CD  
15106 C CE  . LYS   K  65  ? 0.80481 0.80481 0.80481 0.00000  0.00000  0.00000  65  LYS   K CE  
15107 N NZ  . LYS   K  65  ? 0.94495 0.94495 0.94495 -0.00000 0.00000  -0.00000 65  LYS   K NZ  
15108 N N   . ALA   K  66  ? 0.62007 0.62007 0.62007 -0.00000 0.00000  0.00000  66  ALA   K N   
15109 C CA  . ALA   K  66  ? 0.66103 0.66103 0.66103 -0.00000 0.00000  0.00000  66  ALA   K CA  
15110 C C   . ALA   K  66  ? 0.79166 0.79166 0.79166 0.00000  0.00000  0.00000  66  ALA   K C   
15111 O O   . ALA   K  66  ? 0.59438 0.59438 0.59438 0.00000  0.00000  0.00000  66  ALA   K O   
15112 C CB  . ALA   K  66  ? 0.37344 0.37344 0.37344 0.00000  0.00000  0.00000  66  ALA   K CB  
15113 N N   . PHE   K  67  ? 0.88375 0.88375 0.88375 -0.00000 0.00000  0.00000  67  PHE   K N   
15114 C CA  . PHE   K  67  ? 0.61081 0.61081 0.61081 -0.00000 0.00000  0.00000  67  PHE   K CA  
15115 C C   . PHE   K  67  ? 0.81326 0.81326 0.81326 0.00000  0.00000  0.00000  67  PHE   K C   
15116 O O   . PHE   K  67  ? 0.76603 0.76603 0.76603 0.00000  0.00000  0.00000  67  PHE   K O   
15117 C CB  . PHE   K  67  ? 0.62621 0.62621 0.62621 0.00000  0.00000  0.00000  67  PHE   K CB  
15118 C CG  . PHE   K  67  ? 0.63856 0.63856 0.63856 0.00000  0.00000  0.00000  67  PHE   K CG  
15119 C CD1 . PHE   K  67  ? 0.46612 0.46612 0.46612 -0.00000 0.00000  0.00000  67  PHE   K CD1 
15120 C CD2 . PHE   K  67  ? 0.56207 0.56207 0.56207 -0.00000 0.00000  0.00000  67  PHE   K CD2 
15121 C CE1 . PHE   K  67  ? 0.55653 0.55653 0.55653 -0.00000 0.00000  0.00000  67  PHE   K CE1 
15122 C CE2 . PHE   K  67  ? 0.68730 0.68730 0.68730 0.00000  0.00000  0.00000  67  PHE   K CE2 
15123 C CZ  . PHE   K  67  ? 0.52335 0.52335 0.52335 -0.00000 0.00000  0.00000  67  PHE   K CZ  
15124 N N   . ILE   K  68  ? 0.48557 0.48557 0.48557 0.00000  0.00000  0.00000  68  ILE   K N   
15125 C CA  . ILE   K  68  ? 0.51321 0.51321 0.51321 0.00000  0.00000  0.00000  68  ILE   K CA  
15126 C C   . ILE   K  68  ? 0.59030 0.59030 0.59030 -0.00000 -0.00000 0.00000  68  ILE   K C   
15127 O O   . ILE   K  68  ? 0.56031 0.56031 0.56031 -0.00000 0.00000  0.00000  68  ILE   K O   
15128 C CB  . ILE   K  68  ? 0.38551 0.38551 0.38551 0.00000  0.00000  0.00000  68  ILE   K CB  
15129 C CG1 . ILE   K  68  ? 0.47541 0.47541 0.47541 0.00000  0.00000  0.00000  68  ILE   K CG1 
15130 C CG2 . ILE   K  68  ? 0.45378 0.45378 0.45378 0.00000  0.00000  0.00000  68  ILE   K CG2 
15131 C CD1 . ILE   K  68  ? 0.38648 0.38648 0.38648 0.00000  0.00000  0.00000  68  ILE   K CD1 
15132 N N   . GLU   K  69  ? 0.84544 0.84544 0.84544 0.00000  0.00000  0.00000  69  GLU   K N   
15133 C CA  . GLU   K  69  ? 0.52327 0.52327 0.52327 -0.00000 0.00000  0.00000  69  GLU   K CA  
15134 C C   . GLU   K  69  ? 0.64170 0.64170 0.64170 -0.00000 -0.00000 0.00000  69  GLU   K C   
15135 O O   . GLU   K  69  ? 0.64812 0.64812 0.64812 0.00000  0.00000  0.00000  69  GLU   K O   
15136 C CB  . GLU   K  69  ? 0.60357 0.60357 0.60357 0.00000  0.00000  0.00000  69  GLU   K CB  
15137 C CG  . GLU   K  69  ? 0.42635 0.42635 0.42635 -0.00000 0.00000  0.00000  69  GLU   K CG  
15138 C CD  . GLU   K  69  ? 0.94829 0.94829 0.94829 0.00000  0.00000  0.00000  69  GLU   K CD  
15139 O OE1 . GLU   K  69  ? 0.59934 0.59934 0.59934 0.00000  0.00000  0.00000  69  GLU   K OE1 
15140 O OE2 . GLU   K  69  ? 0.68554 0.68554 0.68554 -0.00000 0.00000  0.00000  69  GLU   K OE2 
15141 N N   . SER   K  70  ? 0.78217 0.78217 0.78217 -0.00000 0.00000  0.00000  70  SER   K N   
15142 C CA  . SER   K  70  ? 0.42478 0.42478 0.42478 -0.00000 0.00000  0.00000  70  SER   K CA  
15143 C C   . SER   K  70  ? 0.78906 0.78906 0.78906 0.00000  0.00000  0.00000  70  SER   K C   
15144 O O   . SER   K  70  ? 0.59570 0.59570 0.59570 0.00000  0.00000  0.00000  70  SER   K O   
15145 C CB  . SER   K  70  ? 0.58435 0.58435 0.58435 -0.00000 0.00000  -0.00000 70  SER   K CB  
15146 O OG  . SER   K  70  ? 0.85459 0.85459 0.85459 0.00000  0.00000  0.00000  70  SER   K OG  
15147 N N   . ASP   K  71  ? 0.57260 0.57260 0.57260 0.00000  0.00000  0.00000  71  ASP   K N   
15148 C CA  . ASP   K  71  ? 0.51285 0.51285 0.51285 0.00000  0.00000  0.00000  71  ASP   K CA  
15149 C C   . ASP   K  71  ? 0.59225 0.59225 0.59225 0.00000  0.00000  0.00000  71  ASP   K C   
15150 O O   . ASP   K  71  ? 0.59102 0.59102 0.59102 -0.00000 0.00000  0.00000  71  ASP   K O   
15151 C CB  . ASP   K  71  ? 0.62893 0.62893 0.62893 0.00000  0.00000  0.00000  71  ASP   K CB  
15152 C CG  . ASP   K  71  ? 1.12616 1.12616 1.12616 0.00000  0.00000  0.00000  71  ASP   K CG  
15153 O OD1 . ASP   K  71  ? 0.66926 0.66926 0.66926 -0.00000 0.00000  0.00000  71  ASP   K OD1 
15154 O OD2 . ASP   K  71  ? 0.84536 0.84536 0.84536 0.00000  -0.00000 0.00000  71  ASP   K OD2 
15155 N N   . PRO   K  72  ? 0.73010 0.73010 0.73010 0.00000  0.00000  0.00000  72  PRO   K N   
15156 C CA  . PRO   K  72  ? 0.70792 0.70792 0.70792 0.00000  0.00000  0.00000  72  PRO   K CA  
15157 C C   . PRO   K  72  ? 0.59207 0.59207 0.59207 0.00000  0.00000  0.00000  72  PRO   K C   
15158 O O   . PRO   K  72  ? 0.66476 0.66476 0.66476 -0.00000 0.00000  0.00000  72  PRO   K O   
15159 C CB  . PRO   K  72  ? 0.53337 0.53337 0.53337 -0.00000 0.00000  0.00000  72  PRO   K CB  
15160 C CG  . PRO   K  72  ? 0.60739 0.60739 0.60739 0.00000  0.00000  0.00000  72  PRO   K CG  
15161 C CD  . PRO   K  72  ? 0.42951 0.42951 0.42951 0.00000  0.00000  0.00000  72  PRO   K CD  
15162 N N   . VAL   K  73  ? 0.58455 0.58455 0.58455 -0.00000 0.00000  0.00000  73  VAL   K N   
15163 C CA  . VAL   K  73  ? 0.72369 0.72369 0.72369 0.00000  0.00000  0.00000  73  VAL   K CA  
15164 C C   . VAL   K  73  ? 0.81988 0.81988 0.81988 -0.00000 0.00000  0.00000  73  VAL   K C   
15165 O O   . VAL   K  73  ? 0.45283 0.45283 0.45283 0.00000  0.00000  0.00000  73  VAL   K O   
15166 C CB  . VAL   K  73  ? 0.68245 0.68245 0.68245 0.00000  -0.00000 0.00000  73  VAL   K CB  
15167 C CG1 . VAL   K  73  ? 0.39180 0.39180 0.39180 0.00000  0.00000  0.00000  73  VAL   K CG1 
15168 C CG2 . VAL   K  73  ? 0.36442 0.36442 0.36442 0.00000  0.00000  0.00000  73  VAL   K CG2 
15169 N N   . VAL   K  74  ? 0.61563 0.61563 0.61563 0.00000  0.00000  0.00000  74  VAL   K N   
15170 C CA  . VAL   K  74  ? 0.49654 0.49654 0.49654 0.00000  0.00000  0.00000  74  VAL   K CA  
15171 C C   . VAL   K  74  ? 0.63374 0.63374 0.63374 -0.00000 0.00000  0.00000  74  VAL   K C   
15172 O O   . VAL   K  74  ? 0.69237 0.69237 0.69237 0.00000  0.00000  0.00000  74  VAL   K O   
15173 C CB  . VAL   K  74  ? 0.52348 0.52348 0.52348 -0.00000 0.00000  0.00000  74  VAL   K CB  
15174 C CG1 . VAL   K  74  ? 0.30726 0.30726 0.30726 -0.00000 -0.00000 0.00000  74  VAL   K CG1 
15175 C CG2 . VAL   K  74  ? 0.39385 0.39385 0.39385 -0.00000 0.00000  0.00000  74  VAL   K CG2 
15176 N N   . HIS   K  75  ? 0.61094 0.61094 0.61094 -0.00000 0.00000  0.00000  75  HIS   K N   
15177 C CA  . HIS   K  75  ? 0.51849 0.51849 0.51849 0.00000  0.00000  0.00000  75  HIS   K CA  
15178 C C   . HIS   K  75  ? 0.37715 0.37715 0.37715 0.00000  0.00000  0.00000  75  HIS   K C   
15179 O O   . HIS   K  75  ? 0.46473 0.46473 0.46473 -0.00000 0.00000  0.00000  75  HIS   K O   
15180 C CB  . HIS   K  75  ? 0.41176 0.41176 0.41176 -0.00000 0.00000  0.00000  75  HIS   K CB  
15181 C CG  . HIS   K  75  ? 0.82752 0.82752 0.82752 0.00000  0.00000  0.00000  75  HIS   K CG  
15182 N ND1 . HIS   K  75  ? 0.94718 0.94718 0.94718 -0.00000 0.00000  0.00000  75  HIS   K ND1 
15183 C CD2 . HIS   K  75  ? 0.84585 0.84585 0.84585 -0.00000 0.00000  0.00000  75  HIS   K CD2 
15184 C CE1 . HIS   K  75  ? 0.78877 0.78877 0.78877 0.00000  0.00000  0.00000  75  HIS   K CE1 
15185 N NE2 . HIS   K  75  ? 0.62007 0.62007 0.62007 0.00000  0.00000  0.00000  75  HIS   K NE2 
15186 N N   . GLN   K  76  ? 0.61748 0.61748 0.61748 -0.00000 0.00000  0.00000  76  GLN   K N   
15187 C CA  . GLN   K  76  ? 0.34740 0.34740 0.34740 0.00000  0.00000  0.00000  76  GLN   K CA  
15188 C C   . GLN   K  76  ? 0.64116 0.64116 0.64116 -0.00000 0.00000  0.00000  76  GLN   K C   
15189 O O   . GLN   K  76  ? 0.50522 0.50522 0.50522 0.00000  0.00000  0.00000  76  GLN   K O   
15190 C CB  . GLN   K  76  ? 0.66936 0.66936 0.66936 -0.00000 0.00000  0.00000  76  GLN   K CB  
15191 C CG  . GLN   K  76  ? 0.36512 0.36512 0.36512 0.00000  0.00000  0.00000  76  GLN   K CG  
15192 C CD  . GLN   K  76  ? 1.10310 1.10310 1.10310 0.00000  0.00000  0.00000  76  GLN   K CD  
15193 O OE1 . GLN   K  76  ? 0.59202 0.59202 0.59202 0.00000  0.00000  0.00000  76  GLN   K OE1 
15194 N NE2 . GLN   K  76  ? 0.49165 0.49165 0.49165 0.00000  0.00000  0.00000  76  GLN   K NE2 
15195 N N   . GLU   K  77  ? 0.53693 0.53693 0.53693 0.00000  0.00000  0.00000  77  GLU   K N   
15196 C CA  . GLU   K  77  ? 0.42287 0.42287 0.42287 -0.00000 0.00000  0.00000  77  GLU   K CA  
15197 C C   . GLU   K  77  ? 0.76940 0.76940 0.76940 0.00000  0.00000  0.00000  77  GLU   K C   
15198 O O   . GLU   K  77  ? 0.34645 0.34645 0.34645 0.00000  0.00000  0.00000  77  GLU   K O   
15199 C CB  . GLU   K  77  ? 0.41705 0.41705 0.41705 0.00000  0.00000  0.00000  77  GLU   K CB  
15200 C CG  . GLU   K  77  ? 0.35494 0.35494 0.35494 0.00000  0.00000  0.00000  77  GLU   K CG  
15201 C CD  . GLU   K  77  ? 0.76515 0.76515 0.76515 0.00000  0.00000  0.00000  77  GLU   K CD  
15202 O OE1 . GLU   K  77  ? 0.53286 0.53286 0.53286 0.00000  0.00000  0.00000  77  GLU   K OE1 
15203 O OE2 . GLU   K  77  ? 0.45380 0.45380 0.45380 0.00000  0.00000  0.00000  77  GLU   K OE2 
15204 N N   . PHE   K  78  ? 0.37362 0.37362 0.37362 0.00000  0.00000  0.00000  78  PHE   K N   
15205 C CA  . PHE   K  78  ? 0.64044 0.64044 0.64044 0.00000  0.00000  0.00000  78  PHE   K CA  
15206 C C   . PHE   K  78  ? 0.63116 0.63116 0.63116 0.00000  0.00000  0.00000  78  PHE   K C   
15207 O O   . PHE   K  78  ? 0.72819 0.72819 0.72819 0.00000  0.00000  0.00000  78  PHE   K O   
15208 C CB  . PHE   K  78  ? 0.39446 0.39446 0.39446 0.00000  0.00000  0.00000  78  PHE   K CB  
15209 C CG  . PHE   K  78  ? 0.62824 0.62824 0.62824 -0.00000 0.00000  0.00000  78  PHE   K CG  
15210 C CD1 . PHE   K  78  ? 0.45521 0.45521 0.45521 -0.00000 0.00000  0.00000  78  PHE   K CD1 
15211 C CD2 . PHE   K  78  ? 0.30894 0.30894 0.30894 -0.00000 0.00000  0.00000  78  PHE   K CD2 
15212 C CE1 . PHE   K  78  ? 0.42862 0.42862 0.42862 0.00000  0.00000  0.00000  78  PHE   K CE1 
15213 C CE2 . PHE   K  78  ? 0.55951 0.55951 0.55951 0.00000  0.00000  0.00000  78  PHE   K CE2 
15214 C CZ  . PHE   K  78  ? 0.40001 0.40001 0.40001 0.00000  0.00000  0.00000  78  PHE   K CZ  
15215 N N   . ILE   K  79  ? 0.57457 0.57457 0.57457 0.00000  0.00000  0.00000  79  ILE   K N   
15216 C CA  . ILE   K  79  ? 0.49414 0.49414 0.49414 0.00000  0.00000  0.00000  79  ILE   K CA  
15217 C C   . ILE   K  79  ? 0.70610 0.70610 0.70610 0.00000  0.00000  0.00000  79  ILE   K C   
15218 O O   . ILE   K  79  ? 0.40637 0.40637 0.40637 -0.00000 0.00000  0.00000  79  ILE   K O   
15219 C CB  . ILE   K  79  ? 0.60515 0.60515 0.60515 0.00000  0.00000  0.00000  79  ILE   K CB  
15220 C CG1 . ILE   K  79  ? 0.43350 0.43350 0.43350 0.00000  0.00000  0.00000  79  ILE   K CG1 
15221 C CG2 . ILE   K  79  ? 0.44367 0.44367 0.44367 0.00000  0.00000  0.00000  79  ILE   K CG2 
15222 C CD1 . ILE   K  79  ? 0.39865 0.39865 0.39865 0.00000  0.00000  0.00000  79  ILE   K CD1 
15223 N N   . ASP   K  80  ? 0.40584 0.40584 0.40584 -0.00000 -0.00000 0.00000  80  ASP   K N   
15224 C CA  . ASP   K  80  ? 0.60975 0.60975 0.60975 0.00000  0.00000  0.00000  80  ASP   K CA  
15225 C C   . ASP   K  80  ? 0.49801 0.49801 0.49801 0.00000  0.00000  0.00000  80  ASP   K C   
15226 O O   . ASP   K  80  ? 0.61394 0.61394 0.61394 0.00000  0.00000  0.00000  80  ASP   K O   
15227 C CB  . ASP   K  80  ? 0.53124 0.53124 0.53124 0.00000  0.00000  0.00000  80  ASP   K CB  
15228 C CG  . ASP   K  80  ? 0.76290 0.76290 0.76290 0.00000  0.00000  0.00000  80  ASP   K CG  
15229 O OD1 . ASP   K  80  ? 0.73992 0.73992 0.73992 0.00000  -0.00000 0.00000  80  ASP   K OD1 
15230 O OD2 . ASP   K  80  ? 0.83733 0.83733 0.83733 -0.00000 0.00000  0.00000  80  ASP   K OD2 
15231 N N   . MET   K  81  ? 0.50657 0.50657 0.50657 -0.00000 0.00000  0.00000  81  MET   K N   
15232 C CA  . MET   K  81  ? 0.42685 0.42685 0.42685 -0.00000 0.00000  0.00000  81  MET   K CA  
15233 C C   . MET   K  81  ? 0.71529 0.71529 0.71529 0.00000  0.00000  0.00000  81  MET   K C   
15234 O O   . MET   K  81  ? 0.55522 0.55522 0.55522 -0.00000 0.00000  0.00000  81  MET   K O   
15235 C CB  . MET   K  81  ? 0.42691 0.42691 0.42691 0.00000  0.00000  0.00000  81  MET   K CB  
15236 C CG  . MET   K  81  ? 0.50876 0.50876 0.50876 0.00000  -0.00000 -0.00000 81  MET   K CG  
15237 S SD  . MET   K  81  ? 0.50730 0.50730 0.50730 0.00000  0.00000  0.00000  81  MET   K SD  
15238 C CE  . MET   K  81  ? 0.46446 0.46446 0.46446 0.00000  0.00000  0.00000  81  MET   K CE  
15239 N N   . PHE   K  82  ? 0.44539 0.44539 0.44539 0.00000  0.00000  0.00000  82  PHE   K N   
15240 C CA  . PHE   K  82  ? 0.76709 0.76709 0.76709 -0.00000 0.00000  0.00000  82  PHE   K CA  
15241 C C   . PHE   K  82  ? 0.42337 0.42337 0.42337 -0.00000 0.00000  0.00000  82  PHE   K C   
15242 O O   . PHE   K  82  ? 1.22611 1.22611 1.22611 -0.00000 0.00000  0.00000  82  PHE   K O   
15243 C CB  . PHE   K  82  ? 0.45670 0.45670 0.45670 0.00000  0.00000  0.00000  82  PHE   K CB  
15244 C CG  . PHE   K  82  ? 1.00326 1.00326 1.00326 0.00000  0.00000  0.00000  82  PHE   K CG  
15245 C CD1 . PHE   K  82  ? 0.41972 0.41972 0.41972 -0.00000 -0.00000 0.00000  82  PHE   K CD1 
15246 C CD2 . PHE   K  82  ? 0.45281 0.45281 0.45281 -0.00000 0.00000  0.00000  82  PHE   K CD2 
15247 C CE1 . PHE   K  82  ? 0.65736 0.65736 0.65736 -0.00000 -0.00000 0.00000  82  PHE   K CE1 
15248 C CE2 . PHE   K  82  ? 0.67340 0.67340 0.67340 -0.00000 0.00000  0.00000  82  PHE   K CE2 
15249 C CZ  . PHE   K  82  ? 0.36569 0.36569 0.36569 -0.00000 0.00000  0.00000  82  PHE   K CZ  
15250 N N   . GLU   K  83  ? 0.63484 0.63484 0.63484 0.00000  0.00000  0.00000  83  GLU   K N   
15251 C CA  . GLU   K  83  ? 0.69518 0.69518 0.69518 -0.00000 0.00000  0.00000  83  GLU   K CA  
15252 C C   . GLU   K  83  ? 0.80066 0.80066 0.80066 0.00000  0.00000  0.00000  83  GLU   K C   
15253 O O   . GLU   K  83  ? 0.50005 0.50005 0.50005 -0.00000 0.00000  0.00000  83  GLU   K O   
15254 C CB  . GLU   K  83  ? 0.38278 0.38278 0.38278 0.00000  0.00000  0.00000  83  GLU   K CB  
15255 C CG  . GLU   K  83  ? 0.50243 0.50243 0.50243 0.00000  0.00000  0.00000  83  GLU   K CG  
15256 C CD  . GLU   K  83  ? 1.22146 1.22146 1.22146 0.00000  0.00000  0.00000  83  GLU   K CD  
15257 O OE1 . GLU   K  83  ? 1.36479 1.36479 1.36479 -0.00000 0.00000  0.00000  83  GLU   K OE1 
15258 O OE2 . GLU   K  83  ? 1.52455 1.52455 1.52455 0.00000  -0.00000 0.00000  83  GLU   K OE2 
15259 N N   . GLY   K  84  ? 1.09543 1.09543 1.09543 0.00000  0.00000  0.00000  84  GLY   K N   
15260 C CA  . GLY   K  84  ? 0.64401 0.64401 0.64401 0.00000  0.00000  0.00000  84  GLY   K CA  
15261 C C   . GLY   K  84  ? 1.06305 1.06305 1.06305 0.00000  0.00000  0.00000  84  GLY   K C   
15262 O O   . GLY   K  84  ? 0.87455 0.87455 0.87455 0.00000  0.00000  0.00000  84  GLY   K O   
15263 N N   . ILE   K  85  ? 0.87112 0.87112 0.87112 0.00000  0.00000  0.00000  85  ILE   K N   
15264 C CA  . ILE   K  85  ? 0.61287 0.61287 0.61287 0.00000  0.00000  0.00000  85  ILE   K CA  
15265 C C   . ILE   K  85  ? 0.74217 0.74217 0.74217 0.00000  0.00000  0.00000  85  ILE   K C   
15266 O O   . ILE   K  85  ? 0.66804 0.66804 0.66804 0.00000  0.00000  0.00000  85  ILE   K O   
15267 C CB  . ILE   K  85  ? 0.52948 0.52948 0.52948 0.00000  -0.00000 -0.00000 85  ILE   K CB  
15268 C CG1 . ILE   K  85  ? 0.72294 0.72294 0.72294 0.00000  0.00000  0.00000  85  ILE   K CG1 
15269 C CG2 . ILE   K  85  ? 0.55629 0.55629 0.55629 0.00000  0.00000  0.00000  85  ILE   K CG2 
15270 C CD1 . ILE   K  85  ? 0.62042 0.62042 0.62042 0.00000  0.00000  0.00000  85  ILE   K CD1 
15271 N N   . GLN   K  86  ? 0.70836 0.70836 0.70836 0.00000  0.00000  0.00000  86  GLN   K N   
15272 C CA  . GLN   K  86  ? 1.10877 1.10877 1.10877 0.00000  0.00000  0.00000  86  GLN   K CA  
15273 C C   . GLN   K  86  ? 0.48614 0.48614 0.48614 0.00000  0.00000  0.00000  86  GLN   K C   
15274 O O   . GLN   K  86  ? 1.07756 1.07756 1.07756 0.00000  0.00000  0.00000  86  GLN   K O   
15275 C CB  . GLN   K  86  ? 0.65454 0.65454 0.65454 -0.00000 0.00000  0.00000  86  GLN   K CB  
15276 C CG  . GLN   K  86  ? 0.32779 0.32779 0.32779 -0.00000 0.00000  0.00000  86  GLN   K CG  
15277 C CD  . GLN   K  86  ? 0.63839 0.63839 0.63839 -0.00000 0.00000  0.00000  86  GLN   K CD  
15278 O OE1 . GLN   K  86  ? 0.45346 0.45346 0.45346 -0.00000 0.00000  0.00000  86  GLN   K OE1 
15279 N NE2 . GLN   K  86  ? 0.73177 0.73177 0.73177 0.00000  0.00000  0.00000  86  GLN   K NE2 
15280 N N   . ASP   K  87  ? 1.12635 1.12635 1.12635 -0.00000 0.00000  0.00000  87  ASP   K N   
15281 C CA  . ASP   K  87  ? 0.69919 0.69919 0.69919 0.00000  0.00000  0.00000  87  ASP   K CA  
15282 C C   . ASP   K  87  ? 0.56179 0.56179 0.56179 0.00000  0.00000  0.00000  87  ASP   K C   
15283 O O   . ASP   K  87  ? 0.82001 0.82001 0.82001 0.00000  0.00000  0.00000  87  ASP   K O   
15284 C CB  . ASP   K  87  ? 0.60109 0.60109 0.60109 -0.00000 0.00000  0.00000  87  ASP   K CB  
15285 C CG  . ASP   K  87  ? 1.52268 1.52268 1.52268 0.00000  0.00000  0.00000  87  ASP   K CG  
15286 O OD1 . ASP   K  87  ? 1.27261 1.27261 1.27261 0.00000  0.00000  0.00000  87  ASP   K OD1 
15287 O OD2 . ASP   K  87  ? 1.24778 1.24778 1.24778 -0.00000 0.00000  0.00000  87  ASP   K OD2 
15288 N N   . SER   K  88  ? 0.60246 0.60246 0.60246 -0.00000 0.00000  0.00000  88  SER   K N   
15289 C CA  . SER   K  88  ? 0.46413 0.46413 0.46413 -0.00000 0.00000  0.00000  88  SER   K CA  
15290 C C   . SER   K  88  ? 1.00099 1.00099 1.00099 -0.00000 0.00000  0.00000  88  SER   K C   
15291 O O   . SER   K  88  ? 0.58937 0.58937 0.58937 0.00000  0.00000  0.00000  88  SER   K O   
15292 C CB  . SER   K  88  ? 0.47742 0.47742 0.47742 -0.00000 0.00000  0.00000  88  SER   K CB  
15293 O OG  . SER   K  88  ? 0.68171 0.68171 0.68171 0.00000  0.00000  0.00000  88  SER   K OG  
15294 N N   . PRO   K  89  ? 0.69724 0.69724 0.69724 0.00000  -0.00000 0.00000  89  PRO   K N   
15295 C CA  . PRO   K  89  ? 0.39982 0.39982 0.39982 0.00000  0.00000  0.00000  89  PRO   K CA  
15296 C C   . PRO   K  89  ? 0.75071 0.75071 0.75071 0.00000  0.00000  0.00000  89  PRO   K C   
15297 O O   . PRO   K  89  ? 0.53031 0.53031 0.53031 -0.00000 -0.00000 0.00000  89  PRO   K O   
15298 C CB  . PRO   K  89  ? 0.68312 0.68312 0.68312 -0.00000 0.00000  0.00000  89  PRO   K CB  
15299 C CG  . PRO   K  89  ? 0.65361 0.65361 0.65361 0.00000  0.00000  -0.00000 89  PRO   K CG  
15300 C CD  . PRO   K  89  ? 0.58517 0.58517 0.58517 0.00000  0.00000  0.00000  89  PRO   K CD  
15301 N N   . ARG   K  90  ? 0.45504 0.45504 0.45504 0.00000  0.00000  0.00000  90  ARG   K N   
15302 C CA  . ARG   K  90  ? 0.67034 0.67034 0.67034 -0.00000 0.00000  0.00000  90  ARG   K CA  
15303 C C   . ARG   K  90  ? 0.55236 0.55236 0.55236 0.00000  0.00000  0.00000  90  ARG   K C   
15304 O O   . ARG   K  90  ? 0.54713 0.54713 0.54713 0.00000  0.00000  0.00000  90  ARG   K O   
15305 C CB  . ARG   K  90  ? 0.47265 0.47265 0.47265 0.00000  0.00000  0.00000  90  ARG   K CB  
15306 C CG  . ARG   K  90  ? 1.43661 1.43661 1.43661 0.00000  0.00000  0.00000  90  ARG   K CG  
15307 C CD  . ARG   K  90  ? 1.23146 1.23146 1.23146 -0.00000 0.00000  0.00000  90  ARG   K CD  
15308 N NE  . ARG   K  90  ? 1.24861 1.24861 1.24861 -0.00000 0.00000  0.00000  90  ARG   K NE  
15309 C CZ  . ARG   K  90  ? 0.51860 0.51860 0.51860 0.00000  0.00000  0.00000  90  ARG   K CZ  
15310 N NH1 . ARG   K  90  ? 1.26462 1.26462 1.26462 0.00000  0.00000  0.00000  90  ARG   K NH1 
15311 N NH2 . ARG   K  90  ? 0.74234 0.74234 0.74234 0.00000  0.00000  0.00000  90  ARG   K NH2 
15312 N N   . ASN   K  91  ? 0.54357 0.54357 0.54357 0.00000  0.00000  0.00000  91  ASN   K N   
15313 C CA  . ASN   K  91  ? 0.60032 0.60032 0.60032 0.00000  0.00000  0.00000  91  ASN   K CA  
15314 C C   . ASN   K  91  ? 0.58292 0.58292 0.58292 -0.00000 0.00000  0.00000  91  ASN   K C   
15315 O O   . ASN   K  91  ? 0.66592 0.66592 0.66592 0.00000  0.00000  0.00000  91  ASN   K O   
15316 C CB  . ASN   K  91  ? 0.49901 0.49901 0.49901 0.00000  0.00000  0.00000  91  ASN   K CB  
15317 C CG  . ASN   K  91  ? 0.63424 0.63424 0.63424 0.00000  0.00000  0.00000  91  ASN   K CG  
15318 O OD1 . ASN   K  91  ? 0.76330 0.76330 0.76330 0.00000  0.00000  0.00000  91  ASN   K OD1 
15319 N ND2 . ASN   K  91  ? 0.58391 0.58391 0.58391 0.00000  0.00000  0.00000  91  ASN   K ND2 
15320 N N   . TYR   K  92  ? 0.53307 0.53307 0.53307 0.00000  0.00000  0.00000  92  TYR   K N   
15321 C CA  . TYR   K  92  ? 0.45381 0.45381 0.45381 0.00000  0.00000  0.00000  92  TYR   K CA  
15322 C C   . TYR   K  92  ? 0.50566 0.50566 0.50566 0.00000  -0.00000 -0.00000 92  TYR   K C   
15323 O O   . TYR   K  92  ? 0.56539 0.56539 0.56539 0.00000  -0.00000 -0.00000 92  TYR   K O   
15324 C CB  . TYR   K  92  ? 0.31724 0.31724 0.31724 0.00000  0.00000  0.00000  92  TYR   K CB  
15325 C CG  . TYR   K  92  ? 0.38647 0.38647 0.38647 0.00000  0.00000  0.00000  92  TYR   K CG  
15326 C CD1 . TYR   K  92  ? 0.36390 0.36390 0.36390 0.00000  0.00000  0.00000  92  TYR   K CD1 
15327 C CD2 . TYR   K  92  ? 0.46796 0.46796 0.46796 -0.00000 -0.00000 0.00000  92  TYR   K CD2 
15328 C CE1 . TYR   K  92  ? 0.60430 0.60430 0.60430 0.00000  0.00000  0.00000  92  TYR   K CE1 
15329 C CE2 . TYR   K  92  ? 0.56751 0.56751 0.56751 0.00000  -0.00000 0.00000  92  TYR   K CE2 
15330 C CZ  . TYR   K  92  ? 0.51106 0.51106 0.51106 -0.00000 0.00000  0.00000  92  TYR   K CZ  
15331 O OH  . TYR   K  92  ? 0.72329 0.72329 0.72329 0.00000  0.00000  0.00000  92  TYR   K OH  
15332 N N   . GLN   K  93  ? 0.48657 0.48657 0.48657 -0.00000 0.00000  0.00000  93  GLN   K N   
15333 C CA  . GLN   K  93  ? 0.64625 0.64625 0.64625 0.00000  0.00000  0.00000  93  GLN   K CA  
15334 C C   . GLN   K  93  ? 0.46956 0.46956 0.46956 0.00000  0.00000  0.00000  93  GLN   K C   
15335 O O   . GLN   K  93  ? 0.53808 0.53808 0.53808 0.00000  -0.00000 0.00000  93  GLN   K O   
15336 C CB  . GLN   K  93  ? 0.40402 0.40402 0.40402 0.00000  0.00000  0.00000  93  GLN   K CB  
15337 C CG  . GLN   K  93  ? 0.61590 0.61590 0.61590 -0.00000 0.00000  0.00000  93  GLN   K CG  
15338 C CD  . GLN   K  93  ? 2.12694 2.12694 2.12694 0.00000  0.00000  0.00000  93  GLN   K CD  
15339 O OE1 . GLN   K  93  ? 0.58525 0.58525 0.58525 0.00000  0.00000  0.00000  93  GLN   K OE1 
15340 N NE2 . GLN   K  93  ? 0.61336 0.61336 0.61336 0.00000  0.00000  0.00000  93  GLN   K NE2 
15341 N N   . GLU   K  94  ? 0.60043 0.60043 0.60043 0.00000  0.00000  0.00000  94  GLU   K N   
15342 C CA  . GLU   K  94  ? 0.25014 0.25014 0.25014 0.00000  -0.00000 0.00000  94  GLU   K CA  
15343 C C   . GLU   K  94  ? 0.68716 0.68716 0.68716 0.00000  0.00000  0.00000  94  GLU   K C   
15344 O O   . GLU   K  94  ? 0.64990 0.64990 0.64990 0.00000  0.00000  0.00000  94  GLU   K O   
15345 C CB  . GLU   K  94  ? 0.64835 0.64835 0.64835 -0.00000 -0.00000 -0.00000 94  GLU   K CB  
15346 C CG  . GLU   K  94  ? 0.92119 0.92119 0.92119 -0.00000 0.00000  -0.00000 94  GLU   K CG  
15347 C CD  . GLU   K  94  ? 1.71528 1.71528 1.71528 0.00000  0.00000  0.00000  94  GLU   K CD  
15348 O OE1 . GLU   K  94  ? 0.55598 0.55598 0.55598 -0.00000 0.00000  0.00000  94  GLU   K OE1 
15349 O OE2 . GLU   K  94  ? 1.23619 1.23619 1.23619 0.00000  0.00000  0.00000  94  GLU   K OE2 
15350 N N   . LEU   K  95  ? 0.63018 0.63018 0.63018 0.00000  -0.00000 0.00000  95  LEU   K N   
15351 C CA  . LEU   K  95  ? 0.39009 0.39009 0.39009 0.00000  0.00000  0.00000  95  LEU   K CA  
15352 C C   . LEU   K  95  ? 0.44237 0.44237 0.44237 0.00000  0.00000  0.00000  95  LEU   K C   
15353 O O   . LEU   K  95  ? 0.39183 0.39183 0.39183 -0.00000 0.00000  0.00000  95  LEU   K O   
15354 C CB  . LEU   K  95  ? 0.48012 0.48012 0.48012 0.00000  0.00000  0.00000  95  LEU   K CB  
15355 C CG  . LEU   K  95  ? 0.48098 0.48098 0.48098 0.00000  0.00000  0.00000  95  LEU   K CG  
15356 C CD1 . LEU   K  95  ? 0.40864 0.40864 0.40864 -0.00000 0.00000  0.00000  95  LEU   K CD1 
15357 C CD2 . LEU   K  95  ? 0.29717 0.29717 0.29717 0.00000  0.00000  0.00000  95  LEU   K CD2 
15358 N N   . CYS   K  96  ? 0.32894 0.32894 0.32894 -0.00000 0.00000  0.00000  96  CYS   K N   
15359 C CA  . CYS   K  96  ? 0.46559 0.46559 0.46559 -0.00000 0.00000  0.00000  96  CYS   K CA  
15360 C C   . CYS   K  96  ? 0.46811 0.46811 0.46811 0.00000  0.00000  0.00000  96  CYS   K C   
15361 O O   . CYS   K  96  ? 0.71304 0.71304 0.71304 -0.00000 0.00000  0.00000  96  CYS   K O   
15362 C CB  . CYS   K  96  ? 0.38369 0.38369 0.38369 -0.00000 0.00000  0.00000  96  CYS   K CB  
15363 S SG  . CYS   K  96  ? 0.58259 0.58259 0.58259 0.00000  0.00000  0.00000  96  CYS   K SG  
15364 N N   . ASN   K  97  ? 0.61142 0.61142 0.61142 -0.00000 0.00000  0.00000  97  ASN   K N   
15365 C CA  . ASN   K  97  ? 0.48819 0.48819 0.48819 0.00000  0.00000  0.00000  97  ASN   K CA  
15366 C C   . ASN   K  97  ? 0.80266 0.80266 0.80266 0.00000  0.00000  0.00000  97  ASN   K C   
15367 O O   . ASN   K  97  ? 0.56724 0.56724 0.56724 0.00000  0.00000  -0.00000 97  ASN   K O   
15368 C CB  . ASN   K  97  ? 0.63417 0.63417 0.63417 -0.00000 0.00000  0.00000  97  ASN   K CB  
15369 C CG  . ASN   K  97  ? 1.13412 1.13412 1.13412 0.00000  0.00000  0.00000  97  ASN   K CG  
15370 O OD1 . ASN   K  97  ? 0.78667 0.78667 0.78667 -0.00000 0.00000  0.00000  97  ASN   K OD1 
15371 N ND2 . ASN   K  97  ? 0.59676 0.59676 0.59676 -0.00000 0.00000  0.00000  97  ASN   K ND2 
15372 N N   . MET   K  98  ? 0.36513 0.36513 0.36513 -0.00000 0.00000  0.00000  98  MET   K N   
15373 C CA  . MET   K  98  ? 0.31864 0.31864 0.31864 0.00000  0.00000  0.00000  98  MET   K CA  
15374 C C   . MET   K  98  ? 0.80050 0.80050 0.80050 -0.00000 0.00000  0.00000  98  MET   K C   
15375 O O   . MET   K  98  ? 0.54541 0.54541 0.54541 -0.00000 0.00000  0.00000  98  MET   K O   
15376 C CB  . MET   K  98  ? 0.40549 0.40549 0.40549 0.00000  -0.00000 0.00000  98  MET   K CB  
15377 C CG  . MET   K  98  ? 0.26609 0.26609 0.26609 0.00000  0.00000  0.00000  98  MET   K CG  
15378 S SD  . MET   K  98  ? 0.66004 0.66004 0.66004 0.00000  0.00000  0.00000  98  MET   K SD  
15379 C CE  . MET   K  98  ? 0.49157 0.49157 0.49157 -0.00000 0.00000  0.00000  98  MET   K CE  
15380 N N   . PHE   K  99  ? 0.49457 0.49457 0.49457 0.00000  0.00000  0.00000  99  PHE   K N   
15381 C CA  . PHE   K  99  ? 0.44427 0.44427 0.44427 -0.00000 0.00000  0.00000  99  PHE   K CA  
15382 C C   . PHE   K  99  ? 0.56266 0.56266 0.56266 -0.00000 -0.00000 -0.00000 99  PHE   K C   
15383 O O   . PHE   K  99  ? 0.54828 0.54828 0.54828 -0.00000 0.00000  0.00000  99  PHE   K O   
15384 C CB  . PHE   K  99  ? 0.42497 0.42497 0.42497 0.00000  0.00000  0.00000  99  PHE   K CB  
15385 C CG  . PHE   K  99  ? 0.52898 0.52898 0.52898 0.00000  -0.00000 0.00000  99  PHE   K CG  
15386 C CD1 . PHE   K  99  ? 0.40012 0.40012 0.40012 0.00000  0.00000  0.00000  99  PHE   K CD1 
15387 C CD2 . PHE   K  99  ? 0.51189 0.51189 0.51189 -0.00000 0.00000  0.00000  99  PHE   K CD2 
15388 C CE1 . PHE   K  99  ? 0.59701 0.59701 0.59701 0.00000  0.00000  0.00000  99  PHE   K CE1 
15389 C CE2 . PHE   K  99  ? 0.38922 0.38922 0.38922 -0.00000 0.00000  0.00000  99  PHE   K CE2 
15390 C CZ  . PHE   K  99  ? 0.44119 0.44119 0.44119 0.00000  0.00000  0.00000  99  PHE   K CZ  
15391 N N   . ASN   K  100 ? 0.48514 0.48514 0.48514 0.00000  0.00000  0.00000  100 ASN   K N   
15392 C CA  . ASN   K  100 ? 0.53900 0.53900 0.53900 -0.00000 0.00000  0.00000  100 ASN   K CA  
15393 C C   . ASN   K  100 ? 0.58694 0.58694 0.58694 0.00000  0.00000  0.00000  100 ASN   K C   
15394 O O   . ASN   K  100 ? 0.67883 0.67883 0.67883 -0.00000 0.00000  0.00000  100 ASN   K O   
15395 C CB  . ASN   K  100 ? 0.53252 0.53252 0.53252 0.00000  0.00000  0.00000  100 ASN   K CB  
15396 C CG  . ASN   K  100 ? 0.67756 0.67756 0.67756 -0.00000 0.00000  0.00000  100 ASN   K CG  
15397 O OD1 . ASN   K  100 ? 0.83773 0.83773 0.83773 -0.00000 0.00000  0.00000  100 ASN   K OD1 
15398 N ND2 . ASN   K  100 ? 0.67350 0.67350 0.67350 0.00000  0.00000  0.00000  100 ASN   K ND2 
15399 N N   . ASP   K  101 ? 0.55778 0.55778 0.55778 0.00000  0.00000  0.00000  101 ASP   K N   
15400 C CA  . ASP   K  101 ? 0.47832 0.47832 0.47832 0.00000  0.00000  0.00000  101 ASP   K CA  
15401 C C   . ASP   K  101 ? 0.76532 0.76532 0.76532 0.00000  0.00000  0.00000  101 ASP   K C   
15402 O O   . ASP   K  101 ? 0.65988 0.65988 0.65988 0.00000  0.00000  0.00000  101 ASP   K O   
15403 C CB  . ASP   K  101 ? 0.47927 0.47927 0.47927 -0.00000 0.00000  0.00000  101 ASP   K CB  
15404 C CG  . ASP   K  101 ? 1.52744 1.52744 1.52744 -0.00000 0.00000  0.00000  101 ASP   K CG  
15405 O OD1 . ASP   K  101 ? 0.70788 0.70788 0.70788 0.00000  0.00000  0.00000  101 ASP   K OD1 
15406 O OD2 . ASP   K  101 ? 0.83018 0.83018 0.83018 0.00000  0.00000  0.00000  101 ASP   K OD2 
15407 N N   . ILE   K  102 ? 0.63664 0.63664 0.63664 0.00000  0.00000  0.00000  102 ILE   K N   
15408 C CA  . ILE   K  102 ? 0.43978 0.43978 0.43978 0.00000  0.00000  0.00000  102 ILE   K CA  
15409 C C   . ILE   K  102 ? 0.76352 0.76352 0.76352 0.00000  0.00000  0.00000  102 ILE   K C   
15410 O O   . ILE   K  102 ? 0.55502 0.55502 0.55502 -0.00000 0.00000  0.00000  102 ILE   K O   
15411 C CB  . ILE   K  102 ? 0.47560 0.47560 0.47560 0.00000  0.00000  0.00000  102 ILE   K CB  
15412 C CG1 . ILE   K  102 ? 0.28331 0.28331 0.28331 0.00000  0.00000  0.00000  102 ILE   K CG1 
15413 C CG2 . ILE   K  102 ? 0.33922 0.33922 0.33922 0.00000  -0.00000 0.00000  102 ILE   K CG2 
15414 C CD1 . ILE   K  102 ? 0.55036 0.55036 0.55036 0.00000  0.00000  0.00000  102 ILE   K CD1 
15415 N N   . PHE   K  103 ? 0.44354 0.44354 0.44354 -0.00000 0.00000  0.00000  103 PHE   K N   
15416 C CA  . PHE   K  103 ? 0.75400 0.75400 0.75400 0.00000  0.00000  0.00000  103 PHE   K CA  
15417 C C   . PHE   K  103 ? 0.47390 0.47390 0.47390 0.00000  0.00000  0.00000  103 PHE   K C   
15418 O O   . PHE   K  103 ? 0.57979 0.57979 0.57979 -0.00000 -0.00000 0.00000  103 PHE   K O   
15419 C CB  . PHE   K  103 ? 0.34121 0.34121 0.34121 0.00000  0.00000  0.00000  103 PHE   K CB  
15420 C CG  . PHE   K  103 ? 0.55979 0.55979 0.55979 -0.00000 0.00000  -0.00000 103 PHE   K CG  
15421 C CD1 . PHE   K  103 ? 0.50882 0.50882 0.50882 0.00000  0.00000  0.00000  103 PHE   K CD1 
15422 C CD2 . PHE   K  103 ? 0.40820 0.40820 0.40820 -0.00000 0.00000  0.00000  103 PHE   K CD2 
15423 C CE1 . PHE   K  103 ? 0.66394 0.66394 0.66394 0.00000  -0.00000 0.00000  103 PHE   K CE1 
15424 C CE2 . PHE   K  103 ? 0.56185 0.56185 0.56185 -0.00000 0.00000  0.00000  103 PHE   K CE2 
15425 C CZ  . PHE   K  103 ? 0.55277 0.55277 0.55277 0.00000  0.00000  0.00000  103 PHE   K CZ  
15426 N N   . ARG   K  104 ? 1.54933 1.54933 1.54933 -0.00000 0.00000  0.00000  104 ARG   K N   
15427 C CA  . ARG   K  104 ? 0.17307 0.17307 0.17307 0.00000  0.00000  0.00000  104 ARG   K CA  
15428 C C   . ARG   K  104 ? 1.27104 1.27104 1.27104 -0.00000 -0.00000 0.00000  104 ARG   K C   
15429 O O   . ARG   K  104 ? 0.53321 0.53321 0.53321 -0.00000 0.00000  0.00000  104 ARG   K O   
15430 C CB  . ARG   K  104 ? 1.32511 1.32511 1.32511 0.00000  0.00000  0.00000  104 ARG   K CB  
15431 C CG  . ARG   K  104 ? 0.54192 0.54192 0.54192 0.00000  0.00000  0.00000  104 ARG   K CG  
15432 C CD  . ARG   K  104 ? 0.30546 0.30546 0.30546 0.00000  0.00000  0.00000  104 ARG   K CD  
15433 N NE  . ARG   K  104 ? 1.16668 1.16668 1.16668 -0.00000 0.00000  0.00000  104 ARG   K NE  
15434 C CZ  . ARG   K  104 ? 0.87059 0.87059 0.87059 0.00000  -0.00000 0.00000  104 ARG   K CZ  
15435 N NH1 . ARG   K  104 ? 1.40380 1.40380 1.40380 -0.00000 0.00000  0.00000  104 ARG   K NH1 
15436 N NH2 . ARG   K  104 ? 0.79479 0.79479 0.79479 0.00000  0.00000  0.00000  104 ARG   K NH2 
15437 N N   . LYS   K  105 ? 0.60813 0.60813 0.60813 0.00000  0.00000  0.00000  105 LYS   K N   
15438 C CA  . LYS   K  105 ? 0.87077 0.87077 0.87077 0.00000  0.00000  0.00000  105 LYS   K CA  
15439 C C   . LYS   K  105 ? 0.64952 0.64952 0.64952 -0.00000 0.00000  0.00000  105 LYS   K C   
15440 O O   . LYS   K  105 ? 0.70812 0.70812 0.70812 0.00000  0.00000  0.00000  105 LYS   K O   
15441 C CB  . LYS   K  105 ? 0.74687 0.74687 0.74687 0.00000  0.00000  0.00000  105 LYS   K CB  
15442 C CG  . LYS   K  105 ? 0.61952 0.61952 0.61952 -0.00000 0.00000  0.00000  105 LYS   K CG  
15443 C CD  . LYS   K  105 ? 0.62541 0.62541 0.62541 -0.00000 0.00000  0.00000  105 LYS   K CD  
15444 C CE  . LYS   K  105 ? 1.00798 1.00798 1.00798 -0.00000 0.00000  0.00000  105 LYS   K CE  
15445 N NZ  . LYS   K  105 ? 1.17077 1.17077 1.17077 0.00000  0.00000  0.00000  105 LYS   K NZ  
15446 N N   . ALA   K  106 ? 0.81752 0.81752 0.81752 0.00000  0.00000  0.00000  106 ALA   K N   
15447 C CA  . ALA   K  106 ? 0.73217 0.73217 0.73217 0.00000  0.00000  0.00000  106 ALA   K CA  
15448 C C   . ALA   K  106 ? 0.52181 0.52181 0.52181 -0.00000 0.00000  0.00000  106 ALA   K C   
15449 O O   . ALA   K  106 ? 0.76688 0.76688 0.76688 -0.00000 0.00000  0.00000  106 ALA   K O   
15450 C CB  . ALA   K  106 ? 0.55875 0.55875 0.55875 0.00000  0.00000  0.00000  106 ALA   K CB  
15451 N N   . PRO   K  107 ? 0.89890 0.89890 0.89890 0.00000  -0.00000 -0.00000 107 PRO   K N   
15452 C CA  . PRO   K  107 ? 0.67513 0.67513 0.67513 0.00000  0.00000  0.00000  107 PRO   K CA  
15453 C C   . PRO   K  107 ? 0.80030 0.80030 0.80030 0.00000  0.00000  0.00000  107 PRO   K C   
15454 O O   . PRO   K  107 ? 0.74031 0.74031 0.74031 0.00000  -0.00000 0.00000  107 PRO   K O   
15455 C CB  . PRO   K  107 ? 0.65051 0.65051 0.65051 0.00000  0.00000  0.00000  107 PRO   K CB  
15456 C CG  . PRO   K  107 ? 0.60759 0.60759 0.60759 0.00000  0.00000  0.00000  107 PRO   K CG  
15457 C CD  . PRO   K  107 ? 0.52943 0.52943 0.52943 0.00000  0.00000  0.00000  107 PRO   K CD  
15458 N N   . VAL   K  108 ? 0.69888 0.69888 0.69888 0.00000  0.00000  0.00000  108 VAL   K N   
15459 C CA  . VAL   K  108 ? 0.64652 0.64652 0.64652 -0.00000 0.00000  0.00000  108 VAL   K CA  
15460 C C   . VAL   K  108 ? 0.78877 0.78877 0.78877 0.00000  0.00000  0.00000  108 VAL   K C   
15461 O O   . VAL   K  108 ? 0.79657 0.79657 0.79657 0.00000  0.00000  0.00000  108 VAL   K O   
15462 C CB  . VAL   K  108 ? 0.77616 0.77616 0.77616 0.00000  0.00000  0.00000  108 VAL   K CB  
15463 C CG1 . VAL   K  108 ? 0.53581 0.53581 0.53581 -0.00000 0.00000  0.00000  108 VAL   K CG1 
15464 C CG2 . VAL   K  108 ? 0.53259 0.53259 0.53259 0.00000  0.00000  0.00000  108 VAL   K CG2 
15465 N N   . TYR   K  109 ? 0.58747 0.58747 0.58747 0.00000  0.00000  0.00000  109 TYR   K N   
15466 C CA  . TYR   K  109 ? 0.96050 0.96050 0.96050 0.00000  0.00000  0.00000  109 TYR   K CA  
15467 C C   . TYR   K  109 ? 0.58388 0.58388 0.58388 0.00000  0.00000  0.00000  109 TYR   K C   
15468 O O   . TYR   K  109 ? 0.76024 0.76024 0.76024 0.00000  0.00000  0.00000  109 TYR   K O   
15469 C CB  . TYR   K  109 ? 0.50984 0.50984 0.50984 0.00000  0.00000  0.00000  109 TYR   K CB  
15470 C CG  . TYR   K  109 ? 0.92532 0.92532 0.92532 0.00000  0.00000  0.00000  109 TYR   K CG  
15471 C CD1 . TYR   K  109 ? 0.52626 0.52626 0.52626 -0.00000 0.00000  0.00000  109 TYR   K CD1 
15472 C CD2 . TYR   K  109 ? 0.57665 0.57665 0.57665 0.00000  0.00000  0.00000  109 TYR   K CD2 
15473 C CE1 . TYR   K  109 ? 1.05404 1.05404 1.05404 0.00000  0.00000  0.00000  109 TYR   K CE1 
15474 C CE2 . TYR   K  109 ? 0.84441 0.84441 0.84441 0.00000  0.00000  0.00000  109 TYR   K CE2 
15475 C CZ  . TYR   K  109 ? 0.54319 0.54319 0.54319 0.00000  0.00000  0.00000  109 TYR   K CZ  
15476 O OH  . TYR   K  109 ? 0.87591 0.87591 0.87591 0.00000  0.00000  0.00000  109 TYR   K OH  
15477 N N   . GLY   K  110 ? 0.85913 0.85913 0.85913 -0.00000 0.00000  0.00000  110 GLY   K N   
15478 C CA  . GLY   K  110 ? 0.41584 0.41584 0.41584 0.00000  0.00000  0.00000  110 GLY   K CA  
15479 C C   . GLY   K  110 ? 0.84262 0.84262 0.84262 0.00000  0.00000  0.00000  110 GLY   K C   
15480 O O   . GLY   K  110 ? 0.76665 0.76665 0.76665 0.00000  0.00000  0.00000  110 GLY   K O   
15481 N N   . ASP   K  111 ? 0.70477 0.70477 0.70477 -0.00000 0.00000  0.00000  111 ASP   K N   
15482 C CA  . ASP   K  111 ? 0.58545 0.58545 0.58545 0.00000  0.00000  0.00000  111 ASP   K CA  
15483 C C   . ASP   K  111 ? 0.38340 0.38340 0.38340 -0.00000 0.00000  0.00000  111 ASP   K C   
15484 O O   . ASP   K  111 ? 0.55225 0.55225 0.55225 0.00000  0.00000  0.00000  111 ASP   K O   
15485 C CB  . ASP   K  111 ? 0.74670 0.74670 0.74670 0.00000  0.00000  0.00000  111 ASP   K CB  
15486 C CG  . ASP   K  111 ? 0.73037 0.73037 0.73037 0.00000  0.00000  0.00000  111 ASP   K CG  
15487 O OD1 . ASP   K  111 ? 0.93070 0.93070 0.93070 -0.00000 0.00000  0.00000  111 ASP   K OD1 
15488 O OD2 . ASP   K  111 ? 1.16967 1.16967 1.16967 0.00000  -0.00000 0.00000  111 ASP   K OD2 
15489 N N   . LEU   K  112 ? 0.60670 0.60670 0.60670 0.00000  0.00000  0.00000  112 LEU   K N   
15490 C CA  . LEU   K  112 ? 0.98313 0.98313 0.98313 -0.00000 0.00000  0.00000  112 LEU   K CA  
15491 C C   . LEU   K  112 ? 0.34455 0.34455 0.34455 -0.00000 0.00000  0.00000  112 LEU   K C   
15492 O O   . LEU   K  112 ? 0.41375 0.41375 0.41375 0.00000  0.00000  0.00000  112 LEU   K O   
15493 C CB  . LEU   K  112 ? 0.49477 0.49477 0.49477 0.00000  0.00000  0.00000  112 LEU   K CB  
15494 C CG  . LEU   K  112 ? 1.05993 1.05993 1.05993 0.00000  0.00000  -0.00000 112 LEU   K CG  
15495 C CD1 . LEU   K  112 ? 0.80454 0.80454 0.80454 0.00000  0.00000  0.00000  112 LEU   K CD1 
15496 C CD2 . LEU   K  112 ? 1.09175 1.09175 1.09175 -0.00000 0.00000  0.00000  112 LEU   K CD2 
15497 N N   . GLY   K  113 ? 0.52784 0.52784 0.52784 -0.00000 0.00000  0.00000  113 GLY   K N   
15498 C CA  . GLY   K  113 ? 0.50858 0.50858 0.50858 -0.00000 0.00000  0.00000  113 GLY   K CA  
15499 C C   . GLY   K  113 ? 0.55404 0.55404 0.55404 0.00000  0.00000  0.00000  113 GLY   K C   
15500 O O   . GLY   K  113 ? 0.53427 0.53427 0.53427 0.00000  0.00000  0.00000  113 GLY   K O   
15501 N N   . PRO   K  114 ? 0.52981 0.52981 0.52981 -0.00000 0.00000  0.00000  114 PRO   K N   
15502 C CA  . PRO   K  114 ? 0.44519 0.44519 0.44519 -0.00000 0.00000  0.00000  114 PRO   K CA  
15503 C C   . PRO   K  114 ? 0.48268 0.48268 0.48268 -0.00000 0.00000  0.00000  114 PRO   K C   
15504 O O   . PRO   K  114 ? 0.53927 0.53927 0.53927 0.00000  0.00000  0.00000  114 PRO   K O   
15505 C CB  . PRO   K  114 ? 0.50865 0.50865 0.50865 0.00000  0.00000  0.00000  114 PRO   K CB  
15506 C CG  . PRO   K  114 ? 0.47009 0.47009 0.47009 -0.00000 0.00000  0.00000  114 PRO   K CG  
15507 C CD  . PRO   K  114 ? 0.48384 0.48384 0.48384 -0.00000 0.00000  0.00000  114 PRO   K CD  
15508 N N   . PRO   K  115 ? 0.39126 0.39126 0.39126 -0.00000 0.00000  0.00000  115 PRO   K N   
15509 C CA  . PRO   K  115 ? 0.53038 0.53038 0.53038 0.00000  0.00000  0.00000  115 PRO   K CA  
15510 C C   . PRO   K  115 ? 0.43031 0.43031 0.43031 -0.00000 0.00000  0.00000  115 PRO   K C   
15511 O O   . PRO   K  115 ? 0.49482 0.49482 0.49482 -0.00000 0.00000  0.00000  115 PRO   K O   
15512 C CB  . PRO   K  115 ? 0.29953 0.29953 0.29953 -0.00000 0.00000  0.00000  115 PRO   K CB  
15513 C CG  . PRO   K  115 ? 0.33193 0.33193 0.33193 0.00000  -0.00000 0.00000  115 PRO   K CG  
15514 C CD  . PRO   K  115 ? 0.45818 0.45818 0.45818 0.00000  0.00000  0.00000  115 PRO   K CD  
15515 N N   . VAL   K  116 ? 0.51198 0.51198 0.51198 0.00000  -0.00000 0.00000  116 VAL   K N   
15516 C CA  . VAL   K  116 ? 0.38864 0.38864 0.38864 -0.00000 0.00000  0.00000  116 VAL   K CA  
15517 C C   . VAL   K  116 ? 0.42006 0.42006 0.42006 -0.00000 0.00000  0.00000  116 VAL   K C   
15518 O O   . VAL   K  116 ? 0.46532 0.46532 0.46532 0.00000  0.00000  0.00000  116 VAL   K O   
15519 C CB  . VAL   K  116 ? 0.47945 0.47945 0.47945 0.00000  0.00000  0.00000  116 VAL   K CB  
15520 C CG1 . VAL   K  116 ? 0.37907 0.37907 0.37907 0.00000  0.00000  0.00000  116 VAL   K CG1 
15521 C CG2 . VAL   K  116 ? 0.27724 0.27724 0.27724 0.00000  0.00000  0.00000  116 VAL   K CG2 
15522 N N   . TYR   K  117 ? 0.36195 0.36195 0.36195 -0.00000 0.00000  0.00000  117 TYR   K N   
15523 C CA  . TYR   K  117 ? 0.53334 0.53334 0.53334 0.00000  0.00000  0.00000  117 TYR   K CA  
15524 C C   . TYR   K  117 ? 0.45761 0.45761 0.45761 -0.00000 0.00000  0.00000  117 TYR   K C   
15525 O O   . TYR   K  117 ? 0.52109 0.52109 0.52109 0.00000  0.00000  0.00000  117 TYR   K O   
15526 C CB  . TYR   K  117 ? 0.35078 0.35078 0.35078 -0.00000 0.00000  0.00000  117 TYR   K CB  
15527 C CG  . TYR   K  117 ? 0.44285 0.44285 0.44285 -0.00000 0.00000  0.00000  117 TYR   K CG  
15528 C CD1 . TYR   K  117 ? 0.39509 0.39509 0.39509 0.00000  0.00000  0.00000  117 TYR   K CD1 
15529 C CD2 . TYR   K  117 ? 0.60673 0.60673 0.60673 0.00000  0.00000  0.00000  117 TYR   K CD2 
15530 C CE1 . TYR   K  117 ? 0.40056 0.40056 0.40056 -0.00000 0.00000  0.00000  117 TYR   K CE1 
15531 C CE2 . TYR   K  117 ? 0.32068 0.32068 0.32068 0.00000  0.00000  0.00000  117 TYR   K CE2 
15532 C CZ  . TYR   K  117 ? 0.52874 0.52874 0.52874 0.00000  0.00000  0.00000  117 TYR   K CZ  
15533 O OH  . TYR   K  117 ? 0.39884 0.39884 0.39884 -0.00000 0.00000  0.00000  117 TYR   K OH  
15534 N N   . MET   K  118 ? 0.54003 0.54003 0.54003 -0.00000 0.00000  0.00000  118 MET   K N   
15535 C CA  . MET   K  118 ? 0.41125 0.41125 0.41125 0.00000  0.00000  0.00000  118 MET   K CA  
15536 C C   . MET   K  118 ? 0.60909 0.60909 0.60909 0.00000  0.00000  0.00000  118 MET   K C   
15537 O O   . MET   K  118 ? 0.50989 0.50989 0.50989 0.00000  0.00000  0.00000  118 MET   K O   
15538 C CB  . MET   K  118 ? 0.45012 0.45012 0.45012 0.00000  0.00000  0.00000  118 MET   K CB  
15539 C CG  . MET   K  118 ? 0.31930 0.31930 0.31930 0.00000  0.00000  0.00000  118 MET   K CG  
15540 S SD  . MET   K  118 ? 0.55000 0.55000 0.55000 -0.00000 0.00000  0.00000  118 MET   K SD  
15541 C CE  . MET   K  118 ? 0.60791 0.60791 0.60791 0.00000  0.00000  0.00000  118 MET   K CE  
15542 N N   . ILE   K  119 ? 0.39233 0.39233 0.39233 -0.00000 0.00000  0.00000  119 ILE   K N   
15543 C CA  . ILE   K  119 ? 0.53772 0.53772 0.53772 0.00000  0.00000  0.00000  119 ILE   K CA  
15544 C C   . ILE   K  119 ? 0.54323 0.54323 0.54323 0.00000  0.00000  0.00000  119 ILE   K C   
15545 O O   . ILE   K  119 ? 0.60228 0.60228 0.60228 0.00000  0.00000  0.00000  119 ILE   K O   
15546 C CB  . ILE   K  119 ? 0.43605 0.43605 0.43605 0.00000  0.00000  -0.00000 119 ILE   K CB  
15547 C CG1 . ILE   K  119 ? 0.46504 0.46504 0.46504 0.00000  0.00000  0.00000  119 ILE   K CG1 
15548 C CG2 . ILE   K  119 ? 0.53115 0.53115 0.53115 0.00000  0.00000  0.00000  119 ILE   K CG2 
15549 C CD1 . ILE   K  119 ? 0.52683 0.52683 0.52683 0.00000  0.00000  0.00000  119 ILE   K CD1 
15550 N N   . MET   K  120 ? 0.41155 0.41155 0.41155 -0.00000 0.00000  0.00000  120 MET   K N   
15551 C CA  . MET   K  120 ? 0.38620 0.38620 0.38620 0.00000  0.00000  0.00000  120 MET   K CA  
15552 C C   . MET   K  120 ? 0.46005 0.46005 0.46005 -0.00000 0.00000  0.00000  120 MET   K C   
15553 O O   . MET   K  120 ? 0.45505 0.45505 0.45505 -0.00000 0.00000  0.00000  120 MET   K O   
15554 C CB  . MET   K  120 ? 0.22947 0.22947 0.22947 0.00000  0.00000  0.00000  120 MET   K CB  
15555 C CG  . MET   K  120 ? 0.32941 0.32941 0.32941 0.00000  0.00000  0.00000  120 MET   K CG  
15556 S SD  . MET   K  120 ? 0.53356 0.53356 0.53356 0.00000  0.00000  0.00000  120 MET   K SD  
15557 C CE  . MET   K  120 ? 0.33903 0.33903 0.33903 0.00000  0.00000  0.00000  120 MET   K CE  
15558 N N   . ALA   K  121 ? 0.34609 0.34609 0.34609 0.00000  -0.00000 0.00000  121 ALA   K N   
15559 C CA  . ALA   K  121 ? 0.41936 0.41936 0.41936 0.00000  0.00000  0.00000  121 ALA   K CA  
15560 C C   . ALA   K  121 ? 0.42411 0.42411 0.42411 -0.00000 0.00000  0.00000  121 ALA   K C   
15561 O O   . ALA   K  121 ? 0.51244 0.51244 0.51244 0.00000  0.00000  0.00000  121 ALA   K O   
15562 C CB  . ALA   K  121 ? 0.31697 0.31697 0.31697 0.00000  0.00000  0.00000  121 ALA   K CB  
15563 N N   . LYS   K  122 ? 0.50353 0.50353 0.50353 0.00000  0.00000  0.00000  122 LYS   K N   
15564 C CA  . LYS   K  122 ? 0.40901 0.40901 0.40901 0.00000  0.00000  0.00000  122 LYS   K CA  
15565 C C   . LYS   K  122 ? 0.58917 0.58917 0.58917 0.00000  0.00000  0.00000  122 LYS   K C   
15566 O O   . LYS   K  122 ? 0.51106 0.51106 0.51106 0.00000  0.00000  0.00000  122 LYS   K O   
15567 C CB  . LYS   K  122 ? 0.40159 0.40159 0.40159 -0.00000 0.00000  0.00000  122 LYS   K CB  
15568 C CG  . LYS   K  122 ? 0.25591 0.25591 0.25591 0.00000  0.00000  0.00000  122 LYS   K CG  
15569 C CD  . LYS   K  122 ? 0.26460 0.26460 0.26460 0.00000  0.00000  0.00000  122 LYS   K CD  
15570 C CE  . LYS   K  122 ? 1.58485 1.58485 1.58485 0.00000  0.00000  0.00000  122 LYS   K CE  
15571 N NZ  . LYS   K  122 ? 1.06671 1.06671 1.06671 0.00000  0.00000  0.00000  122 LYS   K NZ  
15572 N N   . LEU   K  123 ? 0.51753 0.51753 0.51753 0.00000  0.00000  0.00000  123 LEU   K N   
15573 C CA  . LEU   K  123 ? 0.51120 0.51120 0.51120 0.00000  0.00000  0.00000  123 LEU   K CA  
15574 C C   . LEU   K  123 ? 0.82770 0.82770 0.82770 0.00000  0.00000  0.00000  123 LEU   K C   
15575 O O   . LEU   K  123 ? 0.41076 0.41076 0.41076 -0.00000 0.00000  0.00000  123 LEU   K O   
15576 C CB  . LEU   K  123 ? 0.39832 0.39832 0.39832 0.00000  0.00000  0.00000  123 LEU   K CB  
15577 C CG  . LEU   K  123 ? 0.51158 0.51158 0.51158 -0.00000 0.00000  0.00000  123 LEU   K CG  
15578 C CD1 . LEU   K  123 ? 0.43754 0.43754 0.43754 0.00000  0.00000  0.00000  123 LEU   K CD1 
15579 C CD2 . LEU   K  123 ? 0.43538 0.43538 0.43538 0.00000  0.00000  0.00000  123 LEU   K CD2 
15580 N N   . MET   K  124 ? 0.40343 0.40343 0.40343 0.00000  0.00000  0.00000  124 MET   K N   
15581 C CA  . MET   K  124 ? 0.54770 0.54770 0.54770 0.00000  0.00000  0.00000  124 MET   K CA  
15582 C C   . MET   K  124 ? 0.45356 0.45356 0.45356 -0.00000 -0.00000 0.00000  124 MET   K C   
15583 O O   . MET   K  124 ? 0.44279 0.44279 0.44279 0.00000  0.00000  0.00000  124 MET   K O   
15584 C CB  . MET   K  124 ? 0.26379 0.26379 0.26379 0.00000  0.00000  0.00000  124 MET   K CB  
15585 C CG  . MET   K  124 ? 0.52019 0.52019 0.52019 -0.00000 0.00000  0.00000  124 MET   K CG  
15586 S SD  . MET   K  124 ? 0.54408 0.54408 0.54408 0.00000  0.00000  0.00000  124 MET   K SD  
15587 C CE  . MET   K  124 ? 0.23596 0.23596 0.23596 0.00000  0.00000  0.00000  124 MET   K CE  
15588 N N   . ASN   K  125 ? 0.48573 0.48573 0.48573 0.00000  0.00000  0.00000  125 ASN   K N   
15589 C CA  . ASN   K  125 ? 0.40825 0.40825 0.40825 -0.00000 0.00000  0.00000  125 ASN   K CA  
15590 C C   . ASN   K  125 ? 0.47947 0.47947 0.47947 -0.00000 0.00000  0.00000  125 ASN   K C   
15591 O O   . ASN   K  125 ? 0.52999 0.52999 0.52999 -0.00000 0.00000  0.00000  125 ASN   K O   
15592 C CB  . ASN   K  125 ? 0.38907 0.38907 0.38907 0.00000  0.00000  0.00000  125 ASN   K CB  
15593 C CG  . ASN   K  125 ? 0.36540 0.36540 0.36540 0.00000  0.00000  0.00000  125 ASN   K CG  
15594 O OD1 . ASN   K  125 ? 0.44346 0.44346 0.44346 0.00000  0.00000  0.00000  125 ASN   K OD1 
15595 N ND2 . ASN   K  125 ? 0.58467 0.58467 0.58467 0.00000  0.00000  0.00000  125 ASN   K ND2 
15596 N N   . THR   K  126 ? 0.43996 0.43996 0.43996 0.00000  0.00000  0.00000  126 THR   K N   
15597 C CA  . THR   K  126 ? 0.55508 0.55508 0.55508 -0.00000 0.00000  0.00000  126 THR   K CA  
15598 C C   . THR   K  126 ? 0.28747 0.28747 0.28747 0.00000  0.00000  0.00000  126 THR   K C   
15599 O O   . THR   K  126 ? 0.52713 0.52713 0.52713 0.00000  0.00000  0.00000  126 THR   K O   
15600 C CB  . THR   K  126 ? 0.36194 0.36194 0.36194 0.00000  0.00000  0.00000  126 THR   K CB  
15601 O OG1 . THR   K  126 ? 0.35462 0.35462 0.35462 0.00000  0.00000  0.00000  126 THR   K OG1 
15602 C CG2 . THR   K  126 ? 0.17222 0.17222 0.17222 -0.00000 0.00000  0.00000  126 THR   K CG2 
15603 N N   . ARG   K  127 ? 1.13330 1.13330 1.13330 0.00000  0.00000  0.00000  127 ARG   K N   
15604 C CA  . ARG   K  127 ? 0.20475 0.20475 0.20475 -0.00000 0.00000  0.00000  127 ARG   K CA  
15605 C C   . ARG   K  127 ? 0.21435 0.21435 0.21435 0.00000  0.00000  0.00000  127 ARG   K C   
15606 O O   . ARG   K  127 ? 0.52225 0.52225 0.52225 0.00000  0.00000  0.00000  127 ARG   K O   
15607 C CB  . ARG   K  127 ? 0.66600 0.66600 0.66600 0.00000  0.00000  0.00000  127 ARG   K CB  
15608 C CG  . ARG   K  127 ? 0.52312 0.52312 0.52312 0.00000  0.00000  0.00000  127 ARG   K CG  
15609 C CD  . ARG   K  127 ? 1.09795 1.09795 1.09795 -0.00000 0.00000  0.00000  127 ARG   K CD  
15610 N NE  . ARG   K  127 ? 1.89606 1.89606 1.89606 0.00000  0.00000  0.00000  127 ARG   K NE  
15611 C CZ  . ARG   K  127 ? 1.72775 1.72775 1.72775 0.00000  0.00000  0.00000  127 ARG   K CZ  
15612 N NH1 . ARG   K  127 ? 0.86363 0.86363 0.86363 -0.00000 -0.00000 0.00000  127 ARG   K NH1 
15613 N NH2 . ARG   K  127 ? 1.28040 1.28040 1.28040 -0.00000 0.00000  0.00000  127 ARG   K NH2 
15614 N N   . ALA   K  128 ? 0.33912 0.33912 0.33912 -0.00000 0.00000  0.00000  128 ALA   K N   
15615 C CA  . ALA   K  128 ? 0.50340 0.50340 0.50340 0.00000  0.00000  -0.00000 128 ALA   K CA  
15616 C C   . ALA   K  128 ? 0.38855 0.38855 0.38855 0.00000  0.00000  0.00000  128 ALA   K C   
15617 O O   . ALA   K  128 ? 0.52583 0.52583 0.52583 -0.00000 0.00000  0.00000  128 ALA   K O   
15618 C CB  . ALA   K  128 ? 0.36115 0.36115 0.36115 0.00000  0.00000  0.00000  128 ALA   K CB  
15619 N N   . GLY   K  129 ? 0.60257 0.60257 0.60257 -0.00000 0.00000  0.00000  129 GLY   K N   
15620 C CA  . GLY   K  129 ? 0.19741 0.19741 0.19741 -0.00000 0.00000  0.00000  129 GLY   K CA  
15621 C C   . GLY   K  129 ? 0.50766 0.50766 0.50766 -0.00000 0.00000  0.00000  129 GLY   K C   
15622 O O   . GLY   K  129 ? 0.37905 0.37905 0.37905 0.00000  0.00000  0.00000  129 GLY   K O   
15623 N N   . PHE   K  130 ? 0.43588 0.43588 0.43588 -0.00000 0.00000  0.00000  130 PHE   K N   
15624 C CA  . PHE   K  130 ? 0.43697 0.43697 0.43697 -0.00000 0.00000  0.00000  130 PHE   K CA  
15625 C C   . PHE   K  130 ? 0.70208 0.70208 0.70208 0.00000  0.00000  0.00000  130 PHE   K C   
15626 O O   . PHE   K  130 ? 0.59005 0.59005 0.59005 -0.00000 0.00000  0.00000  130 PHE   K O   
15627 C CB  . PHE   K  130 ? 0.29249 0.29249 0.29249 -0.00000 0.00000  0.00000  130 PHE   K CB  
15628 C CG  . PHE   K  130 ? 0.46277 0.46277 0.46277 0.00000  0.00000  0.00000  130 PHE   K CG  
15629 C CD1 . PHE   K  130 ? 0.46272 0.46272 0.46272 -0.00000 0.00000  0.00000  130 PHE   K CD1 
15630 C CD2 . PHE   K  130 ? 0.38168 0.38168 0.38168 0.00000  0.00000  0.00000  130 PHE   K CD2 
15631 C CE1 . PHE   K  130 ? 0.44794 0.44794 0.44794 0.00000  0.00000  0.00000  130 PHE   K CE1 
15632 C CE2 . PHE   K  130 ? 0.55677 0.55677 0.55677 0.00000  0.00000  0.00000  130 PHE   K CE2 
15633 C CZ  . PHE   K  130 ? 0.38514 0.38514 0.38514 0.00000  0.00000  0.00000  130 PHE   K CZ  
15634 N N   . SER   K  131 ? 0.35758 0.35758 0.35758 -0.00000 0.00000  0.00000  131 SER   K N   
15635 C CA  . SER   K  131 ? 0.58142 0.58142 0.58142 -0.00000 -0.00000 0.00000  131 SER   K CA  
15636 C C   . SER   K  131 ? 0.42512 0.42512 0.42512 0.00000  0.00000  0.00000  131 SER   K C   
15637 O O   . SER   K  131 ? 0.56249 0.56249 0.56249 -0.00000 0.00000  0.00000  131 SER   K O   
15638 C CB  . SER   K  131 ? 0.21698 0.21698 0.21698 -0.00000 0.00000  0.00000  131 SER   K CB  
15639 O OG  . SER   K  131 ? 1.12719 1.12719 1.12719 -0.00000 0.00000  0.00000  131 SER   K OG  
15640 N N   . ALA   K  132 ? 0.44359 0.44359 0.44359 0.00000  0.00000  0.00000  132 ALA   K N   
15641 C CA  . ALA   K  132 ? 0.37092 0.37092 0.37092 0.00000  0.00000  0.00000  132 ALA   K CA  
15642 C C   . ALA   K  132 ? 0.55191 0.55191 0.55191 0.00000  0.00000  0.00000  132 ALA   K C   
15643 O O   . ALA   K  132 ? 0.47293 0.47293 0.47293 -0.00000 0.00000  0.00000  132 ALA   K O   
15644 C CB  . ALA   K  132 ? 0.38007 0.38007 0.38007 0.00000  -0.00000 0.00000  132 ALA   K CB  
15645 N N   . PHE   K  133 ? 0.35295 0.35295 0.35295 0.00000  0.00000  0.00000  133 PHE   K N   
15646 C CA  . PHE   K  133 ? 0.48688 0.48688 0.48688 -0.00000 0.00000  0.00000  133 PHE   K CA  
15647 C C   . PHE   K  133 ? 0.57488 0.57488 0.57488 -0.00000 0.00000  0.00000  133 PHE   K C   
15648 O O   . PHE   K  133 ? 0.44206 0.44206 0.44206 -0.00000 0.00000  0.00000  133 PHE   K O   
15649 C CB  . PHE   K  133 ? 0.38833 0.38833 0.38833 0.00000  0.00000  0.00000  133 PHE   K CB  
15650 C CG  . PHE   K  133 ? 0.52701 0.52701 0.52701 0.00000  0.00000  0.00000  133 PHE   K CG  
15651 C CD1 . PHE   K  133 ? 0.47068 0.47068 0.47068 -0.00000 0.00000  0.00000  133 PHE   K CD1 
15652 C CD2 . PHE   K  133 ? 0.40371 0.40371 0.40371 0.00000  0.00000  0.00000  133 PHE   K CD2 
15653 C CE1 . PHE   K  133 ? 0.36764 0.36764 0.36764 0.00000  0.00000  0.00000  133 PHE   K CE1 
15654 C CE2 . PHE   K  133 ? 0.39640 0.39640 0.39640 0.00000  0.00000  0.00000  133 PHE   K CE2 
15655 C CZ  . PHE   K  133 ? 0.31778 0.31778 0.31778 0.00000  0.00000  0.00000  133 PHE   K CZ  
15656 N N   . THR   K  134 ? 0.40576 0.40576 0.40576 0.00000  -0.00000 0.00000  134 THR   K N   
15657 C CA  . THR   K  134 ? 0.46477 0.46477 0.46477 0.00000  0.00000  0.00000  134 THR   K CA  
15658 C C   . THR   K  134 ? 0.43724 0.43724 0.43724 0.00000  -0.00000 0.00000  134 THR   K C   
15659 O O   . THR   K  134 ? 0.53795 0.53795 0.53795 0.00000  0.00000  0.00000  134 THR   K O   
15660 C CB  . THR   K  134 ? 0.46498 0.46498 0.46498 -0.00000 0.00000  0.00000  134 THR   K CB  
15661 O OG1 . THR   K  134 ? 0.53702 0.53702 0.53702 0.00000  0.00000  0.00000  134 THR   K OG1 
15662 C CG2 . THR   K  134 ? 0.37626 0.37626 0.37626 0.00000  0.00000  0.00000  134 THR   K CG2 
15663 N N   . ARG   K  135 ? 0.38973 0.38973 0.38973 -0.00000 0.00000  0.00000  135 ARG   K N   
15664 C CA  . ARG   K  135 ? 0.39199 0.39199 0.39199 0.00000  0.00000  0.00000  135 ARG   K CA  
15665 C C   . ARG   K  135 ? 0.56455 0.56455 0.56455 -0.00000 0.00000  0.00000  135 ARG   K C   
15666 O O   . ARG   K  135 ? 0.39495 0.39495 0.39495 -0.00000 0.00000  0.00000  135 ARG   K O   
15667 C CB  . ARG   K  135 ? 0.27570 0.27570 0.27570 0.00000  0.00000  0.00000  135 ARG   K CB  
15668 C CG  . ARG   K  135 ? 0.32896 0.32896 0.32896 -0.00000 0.00000  0.00000  135 ARG   K CG  
15669 C CD  . ARG   K  135 ? 0.36361 0.36361 0.36361 -0.00000 0.00000  0.00000  135 ARG   K CD  
15670 N NE  . ARG   K  135 ? 0.60798 0.60798 0.60798 0.00000  0.00000  0.00000  135 ARG   K NE  
15671 C CZ  . ARG   K  135 ? 0.65631 0.65631 0.65631 -0.00000 -0.00000 0.00000  135 ARG   K CZ  
15672 N NH1 . ARG   K  135 ? 0.54454 0.54454 0.54454 -0.00000 0.00000  0.00000  135 ARG   K NH1 
15673 N NH2 . ARG   K  135 ? 0.51832 0.51832 0.51832 -0.00000 0.00000  0.00000  135 ARG   K NH2 
15674 N N   . GLN   K  136 ? 0.39744 0.39744 0.39744 -0.00000 0.00000  0.00000  136 GLN   K N   
15675 C CA  . GLN   K  136 ? 0.42300 0.42300 0.42300 0.00000  0.00000  0.00000  136 GLN   K CA  
15676 C C   . GLN   K  136 ? 0.38962 0.38962 0.38962 0.00000  0.00000  0.00000  136 GLN   K C   
15677 O O   . GLN   K  136 ? 0.61118 0.61118 0.61118 0.00000  0.00000  0.00000  136 GLN   K O   
15678 C CB  . GLN   K  136 ? 0.39833 0.39833 0.39833 0.00000  0.00000  0.00000  136 GLN   K CB  
15679 C CG  . GLN   K  136 ? 0.33796 0.33796 0.33796 -0.00000 0.00000  0.00000  136 GLN   K CG  
15680 C CD  . GLN   K  136 ? 0.65786 0.65786 0.65786 0.00000  0.00000  0.00000  136 GLN   K CD  
15681 O OE1 . GLN   K  136 ? 0.50486 0.50486 0.50486 0.00000  0.00000  0.00000  136 GLN   K OE1 
15682 N NE2 . GLN   K  136 ? 0.34432 0.34432 0.34432 -0.00000 0.00000  0.00000  136 GLN   K NE2 
15683 N N   . ARG   K  137 ? 0.46720 0.46720 0.46720 0.00000  0.00000  0.00000  137 ARG   K N   
15684 C CA  . ARG   K  137 ? 0.23562 0.23562 0.23562 -0.00000 0.00000  0.00000  137 ARG   K CA  
15685 C C   . ARG   K  137 ? 0.89890 0.89890 0.89890 0.00000  0.00000  0.00000  137 ARG   K C   
15686 O O   . ARG   K  137 ? 0.41423 0.41423 0.41423 -0.00000 0.00000  0.00000  137 ARG   K O   
15687 C CB  . ARG   K  137 ? 0.24316 0.24316 0.24316 0.00000  0.00000  0.00000  137 ARG   K CB  
15688 C CG  . ARG   K  137 ? 0.95710 0.95710 0.95710 -0.00000 0.00000  0.00000  137 ARG   K CG  
15689 C CD  . ARG   K  137 ? 1.01786 1.01786 1.01786 -0.00000 0.00000  0.00000  137 ARG   K CD  
15690 N NE  . ARG   K  137 ? 1.24964 1.24964 1.24964 0.00000  0.00000  0.00000  137 ARG   K NE  
15691 C CZ  . ARG   K  137 ? 1.17714 1.17714 1.17714 0.00000  0.00000  0.00000  137 ARG   K CZ  
15692 N NH1 . ARG   K  137 ? 0.71199 0.71199 0.71199 0.00000  0.00000  0.00000  137 ARG   K NH1 
15693 N NH2 . ARG   K  137 ? 1.47542 1.47542 1.47542 -0.00000 0.00000  0.00000  137 ARG   K NH2 
15694 N N   . LEU   K  138 ? 0.31174 0.31174 0.31174 0.00000  0.00000  0.00000  138 LEU   K N   
15695 C CA  . LEU   K  138 ? 0.47712 0.47712 0.47712 -0.00000 0.00000  0.00000  138 LEU   K CA  
15696 C C   . LEU   K  138 ? 0.59666 0.59666 0.59666 0.00000  0.00000  0.00000  138 LEU   K C   
15697 O O   . LEU   K  138 ? 0.46430 0.46430 0.46430 -0.00000 0.00000  0.00000  138 LEU   K O   
15698 C CB  . LEU   K  138 ? 0.39838 0.39838 0.39838 0.00000  0.00000  0.00000  138 LEU   K CB  
15699 C CG  . LEU   K  138 ? 0.57417 0.57417 0.57417 0.00000  0.00000  0.00000  138 LEU   K CG  
15700 C CD1 . LEU   K  138 ? 0.40292 0.40292 0.40292 0.00000  0.00000  0.00000  138 LEU   K CD1 
15701 C CD2 . LEU   K  138 ? 0.36914 0.36914 0.36914 0.00000  0.00000  -0.00000 138 LEU   K CD2 
15702 N N   . ASN   K  139 ? 0.36097 0.36097 0.36097 -0.00000 0.00000  0.00000  139 ASN   K N   
15703 C CA  . ASN   K  139 ? 0.56618 0.56618 0.56618 0.00000  0.00000  0.00000  139 ASN   K CA  
15704 C C   . ASN   K  139 ? 0.39656 0.39656 0.39656 -0.00000 0.00000  0.00000  139 ASN   K C   
15705 O O   . ASN   K  139 ? 0.57263 0.57263 0.57263 0.00000  0.00000  0.00000  139 ASN   K O   
15706 C CB  . ASN   K  139 ? 0.26603 0.26603 0.26603 -0.00000 0.00000  0.00000  139 ASN   K CB  
15707 C CG  . ASN   K  139 ? 0.47909 0.47909 0.47909 0.00000  0.00000  0.00000  139 ASN   K CG  
15708 O OD1 . ASN   K  139 ? 0.37243 0.37243 0.37243 0.00000  0.00000  -0.00000 139 ASN   K OD1 
15709 N ND2 . ASN   K  139 ? 0.33217 0.33217 0.33217 0.00000  0.00000  0.00000  139 ASN   K ND2 
15710 N N   . LEU   K  140 ? 0.56464 0.56464 0.56464 -0.00000 0.00000  0.00000  140 LEU   K N   
15711 C CA  . LEU   K  140 ? 0.41458 0.41458 0.41458 0.00000  0.00000  0.00000  140 LEU   K CA  
15712 C C   . LEU   K  140 ? 0.69676 0.69676 0.69676 0.00000  0.00000  0.00000  140 LEU   K C   
15713 O O   . LEU   K  140 ? 0.42985 0.42985 0.42985 0.00000  0.00000  0.00000  140 LEU   K O   
15714 C CB  . LEU   K  140 ? 0.40874 0.40874 0.40874 0.00000  0.00000  0.00000  140 LEU   K CB  
15715 C CG  . LEU   K  140 ? 0.61443 0.61443 0.61443 0.00000  -0.00000 0.00000  140 LEU   K CG  
15716 C CD1 . LEU   K  140 ? 0.33540 0.33540 0.33540 0.00000  0.00000  0.00000  140 LEU   K CD1 
15717 C CD2 . LEU   K  140 ? 0.25757 0.25757 0.25757 0.00000  0.00000  0.00000  140 LEU   K CD2 
15718 N N   . HIS   K  141 ? 0.47697 0.47697 0.47697 -0.00000 0.00000  0.00000  141 HIS   K N   
15719 C CA  . HIS   K  141 ? 0.45036 0.45036 0.45036 -0.00000 0.00000  0.00000  141 HIS   K CA  
15720 C C   . HIS   K  141 ? 0.46527 0.46527 0.46527 0.00000  0.00000  0.00000  141 HIS   K C   
15721 O O   . HIS   K  141 ? 0.54996 0.54996 0.54996 0.00000  0.00000  0.00000  141 HIS   K O   
15722 C CB  . HIS   K  141 ? 0.32340 0.32340 0.32340 0.00000  0.00000  0.00000  141 HIS   K CB  
15723 C CG  . HIS   K  141 ? 0.67234 0.67234 0.67234 -0.00000 0.00000  0.00000  141 HIS   K CG  
15724 N ND1 . HIS   K  141 ? 0.64495 0.64495 0.64495 -0.00000 -0.00000 0.00000  141 HIS   K ND1 
15725 C CD2 . HIS   K  141 ? 0.58569 0.58569 0.58569 0.00000  0.00000  0.00000  141 HIS   K CD2 
15726 C CE1 . HIS   K  141 ? 0.48692 0.48692 0.48692 0.00000  0.00000  0.00000  141 HIS   K CE1 
15727 N NE2 . HIS   K  141 ? 0.65471 0.65471 0.65471 0.00000  0.00000  0.00000  141 HIS   K NE2 
15728 N N   . PHE   K  142 ? 0.40254 0.40254 0.40254 0.00000  0.00000  0.00000  142 PHE   K N   
15729 C CA  . PHE   K  142 ? 0.57016 0.57016 0.57016 -0.00000 0.00000  0.00000  142 PHE   K CA  
15730 C C   . PHE   K  142 ? 0.40418 0.40418 0.40418 0.00000  0.00000  0.00000  142 PHE   K C   
15731 O O   . PHE   K  142 ? 0.42899 0.42899 0.42899 0.00000  0.00000  0.00000  142 PHE   K O   
15732 C CB  . PHE   K  142 ? 0.39241 0.39241 0.39241 0.00000  0.00000  0.00000  142 PHE   K CB  
15733 C CG  . PHE   K  142 ? 0.48341 0.48341 0.48341 0.00000  -0.00000 0.00000  142 PHE   K CG  
15734 C CD1 . PHE   K  142 ? 0.41795 0.41795 0.41795 -0.00000 0.00000  0.00000  142 PHE   K CD1 
15735 C CD2 . PHE   K  142 ? 0.43684 0.43684 0.43684 0.00000  0.00000  0.00000  142 PHE   K CD2 
15736 C CE1 . PHE   K  142 ? 0.40629 0.40629 0.40629 -0.00000 0.00000  0.00000  142 PHE   K CE1 
15737 C CE2 . PHE   K  142 ? 0.45084 0.45084 0.45084 -0.00000 0.00000  0.00000  142 PHE   K CE2 
15738 C CZ  . PHE   K  142 ? 0.39025 0.39025 0.39025 -0.00000 0.00000  0.00000  142 PHE   K CZ  
15739 N N   . LYS   K  143 ? 0.48364 0.48364 0.48364 0.00000  0.00000  0.00000  143 LYS   K N   
15740 C CA  . LYS   K  143 ? 0.42876 0.42876 0.42876 0.00000  0.00000  0.00000  143 LYS   K CA  
15741 C C   . LYS   K  143 ? 0.47025 0.47025 0.47025 0.00000  0.00000  0.00000  143 LYS   K C   
15742 O O   . LYS   K  143 ? 0.51282 0.51282 0.51282 -0.00000 0.00000  0.00000  143 LYS   K O   
15743 C CB  . LYS   K  143 ? 0.47376 0.47376 0.47376 -0.00000 0.00000  0.00000  143 LYS   K CB  
15744 C CG  . LYS   K  143 ? 0.30360 0.30360 0.30360 0.00000  0.00000  0.00000  143 LYS   K CG  
15745 C CD  . LYS   K  143 ? 0.40697 0.40697 0.40697 0.00000  0.00000  0.00000  143 LYS   K CD  
15746 C CE  . LYS   K  143 ? 0.49003 0.49003 0.49003 0.00000  0.00000  0.00000  143 LYS   K CE  
15747 N NZ  . LYS   K  143 ? 0.54841 0.54841 0.54841 -0.00000 0.00000  0.00000  143 LYS   K NZ  
15748 N N   . LYS   K  144 ? 0.24637 0.24637 0.24637 0.00000  -0.00000 0.00000  144 LYS   K N   
15749 C CA  . LYS   K  144 ? 0.73889 0.73889 0.73889 -0.00000 0.00000  0.00000  144 LYS   K CA  
15750 C C   . LYS   K  144 ? 0.72102 0.72102 0.72102 -0.00000 0.00000  0.00000  144 LYS   K C   
15751 O O   . LYS   K  144 ? 0.53988 0.53988 0.53988 0.00000  0.00000  0.00000  144 LYS   K O   
15752 C CB  . LYS   K  144 ? 0.22763 0.22763 0.22763 -0.00000 0.00000  0.00000  144 LYS   K CB  
15753 C CG  . LYS   K  144 ? 1.23684 1.23684 1.23684 -0.00000 0.00000  0.00000  144 LYS   K CG  
15754 C CD  . LYS   K  144 ? 1.28454 1.28454 1.28454 0.00000  0.00000  0.00000  144 LYS   K CD  
15755 C CE  . LYS   K  144 ? 1.31727 1.31727 1.31727 0.00000  -0.00000 0.00000  144 LYS   K CE  
15756 N NZ  . LYS   K  144 ? 1.02608 1.02608 1.02608 -0.00000 0.00000  0.00000  144 LYS   K NZ  
15757 N N   . LEU   K  145 ? 0.45620 0.45620 0.45620 0.00000  0.00000  0.00000  145 LEU   K N   
15758 C CA  . LEU   K  145 ? 0.38563 0.38563 0.38563 0.00000  0.00000  0.00000  145 LEU   K CA  
15759 C C   . LEU   K  145 ? 0.64097 0.64097 0.64097 0.00000  0.00000  0.00000  145 LEU   K C   
15760 O O   . LEU   K  145 ? 0.61852 0.61852 0.61852 -0.00000 0.00000  0.00000  145 LEU   K O   
15761 C CB  . LEU   K  145 ? 0.52287 0.52287 0.52287 0.00000  0.00000  0.00000  145 LEU   K CB  
15762 C CG  . LEU   K  145 ? 0.55645 0.55645 0.55645 0.00000  0.00000  0.00000  145 LEU   K CG  
15763 C CD1 . LEU   K  145 ? 0.47667 0.47667 0.47667 0.00000  0.00000  0.00000  145 LEU   K CD1 
15764 C CD2 . LEU   K  145 ? 0.46882 0.46882 0.46882 0.00000  0.00000  0.00000  145 LEU   K CD2 
15765 N N   . PHE   K  146 ? 0.36852 0.36852 0.36852 0.00000  0.00000  0.00000  146 PHE   K N   
15766 C CA  . PHE   K  146 ? 0.41860 0.41860 0.41860 -0.00000 0.00000  0.00000  146 PHE   K CA  
15767 C C   . PHE   K  146 ? 0.52295 0.52295 0.52295 0.00000  0.00000  0.00000  146 PHE   K C   
15768 O O   . PHE   K  146 ? 0.53194 0.53194 0.53194 -0.00000 -0.00000 0.00000  146 PHE   K O   
15769 C CB  . PHE   K  146 ? 0.42150 0.42150 0.42150 0.00000  0.00000  0.00000  146 PHE   K CB  
15770 C CG  . PHE   K  146 ? 0.46676 0.46676 0.46676 0.00000  0.00000  0.00000  146 PHE   K CG  
15771 C CD1 . PHE   K  146 ? 0.46731 0.46731 0.46731 -0.00000 0.00000  0.00000  146 PHE   K CD1 
15772 C CD2 . PHE   K  146 ? 0.37948 0.37948 0.37948 -0.00000 0.00000  0.00000  146 PHE   K CD2 
15773 C CE1 . PHE   K  146 ? 0.46877 0.46877 0.46877 0.00000  0.00000  0.00000  146 PHE   K CE1 
15774 C CE2 . PHE   K  146 ? 0.42485 0.42485 0.42485 -0.00000 0.00000  0.00000  146 PHE   K CE2 
15775 C CZ  . PHE   K  146 ? 0.49652 0.49652 0.49652 -0.00000 -0.00000 0.00000  146 PHE   K CZ  
15776 N N   . ASP   K  147 ? 0.52166 0.52166 0.52166 0.00000  0.00000  -0.00000 147 ASP   K N   
15777 C CA  . ASP   K  147 ? 0.44096 0.44096 0.44096 -0.00000 0.00000  0.00000  147 ASP   K CA  
15778 C C   . ASP   K  147 ? 0.56210 0.56210 0.56210 0.00000  0.00000  0.00000  147 ASP   K C   
15779 O O   . ASP   K  147 ? 0.54074 0.54074 0.54074 0.00000  0.00000  0.00000  147 ASP   K O   
15780 C CB  . ASP   K  147 ? 0.34529 0.34529 0.34529 -0.00000 -0.00000 0.00000  147 ASP   K CB  
15781 C CG  . ASP   K  147 ? 0.76423 0.76423 0.76423 0.00000  0.00000  0.00000  147 ASP   K CG  
15782 O OD1 . ASP   K  147 ? 0.66438 0.66438 0.66438 0.00000  0.00000  -0.00000 147 ASP   K OD1 
15783 O OD2 . ASP   K  147 ? 0.71733 0.71733 0.71733 0.00000  0.00000  0.00000  147 ASP   K OD2 
15784 N N   . THR   K  148 ? 0.52134 0.52134 0.52134 0.00000  0.00000  -0.00000 148 THR   K N   
15785 C CA  . THR   K  148 ? 0.64101 0.64101 0.64101 0.00000  -0.00000 -0.00000 148 THR   K CA  
15786 C C   . THR   K  148 ? 0.60182 0.60182 0.60182 -0.00000 0.00000  0.00000  148 THR   K C   
15787 O O   . THR   K  148 ? 0.67801 0.67801 0.67801 -0.00000 0.00000  0.00000  148 THR   K O   
15788 C CB  . THR   K  148 ? 0.57593 0.57593 0.57593 0.00000  0.00000  0.00000  148 THR   K CB  
15789 O OG1 . THR   K  148 ? 0.58692 0.58692 0.58692 0.00000  0.00000  0.00000  148 THR   K OG1 
15790 C CG2 . THR   K  148 ? 0.44045 0.44045 0.44045 0.00000  0.00000  0.00000  148 THR   K CG2 
15791 N N   . TRP   K  149 ? 0.58927 0.58927 0.58927 -0.00000 0.00000  0.00000  149 TRP   K N   
15792 C CA  . TRP   K  149 ? 0.50195 0.50195 0.50195 0.00000  0.00000  0.00000  149 TRP   K CA  
15793 C C   . TRP   K  149 ? 0.80625 0.80625 0.80625 0.00000  0.00000  0.00000  149 TRP   K C   
15794 O O   . TRP   K  149 ? 0.61398 0.61398 0.61398 0.00000  0.00000  0.00000  149 TRP   K O   
15795 C CB  . TRP   K  149 ? 0.47119 0.47119 0.47119 0.00000  0.00000  0.00000  149 TRP   K CB  
15796 C CG  . TRP   K  149 ? 0.61082 0.61082 0.61082 -0.00000 0.00000  0.00000  149 TRP   K CG  
15797 C CD1 . TRP   K  149 ? 0.53891 0.53891 0.53891 -0.00000 0.00000  0.00000  149 TRP   K CD1 
15798 C CD2 . TRP   K  149 ? 0.74176 0.74176 0.74176 0.00000  0.00000  0.00000  149 TRP   K CD2 
15799 N NE1 . TRP   K  149 ? 0.69357 0.69357 0.69357 -0.00000 0.00000  0.00000  149 TRP   K NE1 
15800 C CE2 . TRP   K  149 ? 0.51979 0.51979 0.51979 0.00000  0.00000  0.00000  149 TRP   K CE2 
15801 C CE3 . TRP   K  149 ? 0.50861 0.50861 0.50861 -0.00000 0.00000  0.00000  149 TRP   K CE3 
15802 C CZ2 . TRP   K  149 ? 0.63942 0.63942 0.63942 -0.00000 0.00000  0.00000  149 TRP   K CZ2 
15803 C CZ3 . TRP   K  149 ? 0.54486 0.54486 0.54486 0.00000  0.00000  0.00000  149 TRP   K CZ3 
15804 C CH2 . TRP   K  149 ? 0.63627 0.63627 0.63627 0.00000  0.00000  0.00000  149 TRP   K CH2 
15805 N N   . GLY   K  150 ? 0.53098 0.53098 0.53098 -0.00000 0.00000  0.00000  150 GLY   K N   
15806 C CA  . GLY   K  150 ? 0.39618 0.39618 0.39618 0.00000  0.00000  0.00000  150 GLY   K CA  
15807 C C   . GLY   K  150 ? 0.66585 0.66585 0.66585 -0.00000 0.00000  0.00000  150 GLY   K C   
15808 O O   . GLY   K  150 ? 0.81852 0.81852 0.81852 0.00000  0.00000  0.00000  150 GLY   K O   
15809 N N   . LEU   K  151 ? 0.57026 0.57026 0.57026 0.00000  0.00000  0.00000  151 LEU   K N   
15810 C CA  . LEU   K  151 ? 0.50337 0.50337 0.50337 0.00000  0.00000  0.00000  151 LEU   K CA  
15811 C C   . LEU   K  151 ? 1.00289 1.00289 1.00289 -0.00000 0.00000  0.00000  151 LEU   K C   
15812 O O   . LEU   K  151 ? 0.66166 0.66166 0.66166 -0.00000 0.00000  0.00000  151 LEU   K O   
15813 C CB  . LEU   K  151 ? 0.65782 0.65782 0.65782 -0.00000 0.00000  0.00000  151 LEU   K CB  
15814 C CG  . LEU   K  151 ? 0.92502 0.92502 0.92502 0.00000  0.00000  0.00000  151 LEU   K CG  
15815 C CD1 . LEU   K  151 ? 0.48393 0.48393 0.48393 0.00000  0.00000  0.00000  151 LEU   K CD1 
15816 C CD2 . LEU   K  151 ? 0.33857 0.33857 0.33857 0.00000  0.00000  0.00000  151 LEU   K CD2 
15817 N N   . PHE   K  152 ? 0.44915 0.44915 0.44915 0.00000  0.00000  0.00000  152 PHE   K N   
15818 C CA  . PHE   K  152 ? 0.61063 0.61063 0.61063 -0.00000 0.00000  0.00000  152 PHE   K CA  
15819 C C   . PHE   K  152 ? 0.77823 0.77823 0.77823 0.00000  0.00000  0.00000  152 PHE   K C   
15820 O O   . PHE   K  152 ? 0.68268 0.68268 0.68268 0.00000  0.00000  0.00000  152 PHE   K O   
15821 C CB  . PHE   K  152 ? 0.38599 0.38599 0.38599 0.00000  0.00000  0.00000  152 PHE   K CB  
15822 C CG  . PHE   K  152 ? 0.71855 0.71855 0.71855 -0.00000 0.00000  0.00000  152 PHE   K CG  
15823 C CD1 . PHE   K  152 ? 0.50262 0.50262 0.50262 0.00000  0.00000  0.00000  152 PHE   K CD1 
15824 C CD2 . PHE   K  152 ? 0.60226 0.60226 0.60226 -0.00000 0.00000  0.00000  152 PHE   K CD2 
15825 C CE1 . PHE   K  152 ? 0.59120 0.59120 0.59120 0.00000  0.00000  0.00000  152 PHE   K CE1 
15826 C CE2 . PHE   K  152 ? 0.72357 0.72357 0.72357 0.00000  0.00000  0.00000  152 PHE   K CE2 
15827 C CZ  . PHE   K  152 ? 0.61907 0.61907 0.61907 0.00000  0.00000  0.00000  152 PHE   K CZ  
15828 N N   . LEU   K  153 ? 0.60195 0.60195 0.60195 0.00000  0.00000  0.00000  153 LEU   K N   
15829 C CA  . LEU   K  153 ? 0.62610 0.62610 0.62610 0.00000  0.00000  0.00000  153 LEU   K CA  
15830 C C   . LEU   K  153 ? 0.62085 0.62085 0.62085 -0.00000 0.00000  0.00000  153 LEU   K C   
15831 O O   . LEU   K  153 ? 0.67651 0.67651 0.67651 0.00000  0.00000  0.00000  153 LEU   K O   
15832 C CB  . LEU   K  153 ? 0.53390 0.53390 0.53390 0.00000  -0.00000 0.00000  153 LEU   K CB  
15833 C CG  . LEU   K  153 ? 0.69941 0.69941 0.69941 0.00000  0.00000  0.00000  153 LEU   K CG  
15834 C CD1 . LEU   K  153 ? 0.47369 0.47369 0.47369 0.00000  0.00000  0.00000  153 LEU   K CD1 
15835 C CD2 . LEU   K  153 ? 0.47390 0.47390 0.47390 -0.00000 0.00000  0.00000  153 LEU   K CD2 
15836 N N   . SER   K  154 ? 0.68170 0.68170 0.68170 0.00000  0.00000  -0.00000 154 SER   K N   
15837 C CA  . SER   K  154 ? 0.65321 0.65321 0.65321 0.00000  0.00000  0.00000  154 SER   K CA  
15838 C C   . SER   K  154 ? 0.78090 0.78090 0.78090 -0.00000 0.00000  0.00000  154 SER   K C   
15839 O O   . SER   K  154 ? 0.83462 0.83462 0.83462 0.00000  0.00000  0.00000  154 SER   K O   
15840 C CB  . SER   K  154 ? 0.49106 0.49106 0.49106 -0.00000 0.00000  0.00000  154 SER   K CB  
15841 O OG  . SER   K  154 ? 1.51230 1.51230 1.51230 -0.00000 0.00000  0.00000  154 SER   K OG  
15842 N N   . SER   K  155 ? 0.67089 0.67089 0.67089 0.00000  0.00000  0.00000  155 SER   K N   
15843 C CA  . SER   K  155 ? 0.67879 0.67879 0.67879 0.00000  0.00000  0.00000  155 SER   K CA  
15844 C C   . SER   K  155 ? 1.49702 1.49702 1.49702 0.00000  0.00000  0.00000  155 SER   K C   
15845 O O   . SER   K  155 ? 0.65460 0.65460 0.65460 0.00000  0.00000  -0.00000 155 SER   K O   
15846 C CB  . SER   K  155 ? 0.63767 0.63767 0.63767 -0.00000 0.00000  0.00000  155 SER   K CB  
15847 O OG  . SER   K  155 ? 0.76494 0.76494 0.76494 0.00000  0.00000  0.00000  155 SER   K OG  
15848 N N   . LYS   K  156 ? 0.85900 0.85900 0.85900 0.00000  0.00000  0.00000  156 LYS   K N   
15849 C CA  . LYS   K  156 ? 1.07200 1.07200 1.07200 -0.00000 0.00000  0.00000  156 LYS   K CA  
15850 C C   . LYS   K  156 ? 0.73537 0.73537 0.73537 0.00000  0.00000  0.00000  156 LYS   K C   
15851 O O   . LYS   K  156 ? 0.93604 0.93604 0.93604 0.00000  0.00000  0.00000  156 LYS   K O   
15852 C CB  . LYS   K  156 ? 0.64311 0.64311 0.64311 -0.00000 -0.00000 0.00000  156 LYS   K CB  
15853 N N   . ASP   K  157 ? 0.72951 0.72951 0.72951 0.00000  0.00000  0.00000  157 ASP   K N   
15854 C CA  . ASP   K  157 ? 0.71650 0.71650 0.71650 -0.00000 0.00000  0.00000  157 ASP   K CA  
15855 C C   . ASP   K  157 ? 0.74840 0.74840 0.74840 0.00000  0.00000  0.00000  157 ASP   K C   
15856 O O   . ASP   K  157 ? 0.69629 0.69629 0.69629 -0.00000 0.00000  0.00000  157 ASP   K O   
15857 C CB  . ASP   K  157 ? 0.86026 0.86026 0.86026 -0.00000 0.00000  0.00000  157 ASP   K CB  
15858 C CG  . ASP   K  157 ? 0.87341 0.87341 0.87341 0.00000  0.00000  0.00000  157 ASP   K CG  
15859 O OD1 . ASP   K  157 ? 1.00768 1.00768 1.00768 0.00000  0.00000  0.00000  157 ASP   K OD1 
15860 O OD2 . ASP   K  157 ? 1.24455 1.24455 1.24455 0.00000  0.00000  0.00000  157 ASP   K OD2 
15861 N N   . SER   K  158 ? 0.99420 0.99420 0.99420 0.00000  0.00000  0.00000  158 SER   K N   
15862 C CA  . SER   K  158 ? 0.80965 0.80965 0.80965 -0.00000 0.00000  0.00000  158 SER   K CA  
15863 C C   . SER   K  158 ? 0.84568 0.84568 0.84568 0.00000  0.00000  0.00000  158 SER   K C   
15864 O O   . SER   K  158 ? 0.78310 0.78310 0.78310 -0.00000 0.00000  0.00000  158 SER   K O   
15865 C CB  . SER   K  158 ? 0.72679 0.72679 0.72679 0.00000  0.00000  0.00000  158 SER   K CB  
15866 O OG  . SER   K  158 ? 0.71993 0.71993 0.71993 0.00000  0.00000  0.00000  158 SER   K OG  
15867 N N   . ARG   K  159 ? 0.75625 0.75625 0.75625 0.00000  0.00000  0.00000  159 ARG   K N   
15868 C CA  . ARG   K  159 ? 0.84765 0.84765 0.84765 0.00000  -0.00000 0.00000  159 ARG   K CA  
15869 C C   . ARG   K  159 ? 0.85723 0.85723 0.85723 0.00000  0.00000  0.00000  159 ARG   K C   
15870 O O   . ARG   K  159 ? 0.78653 0.78653 0.78653 -0.00000 0.00000  0.00000  159 ARG   K O   
15871 C CB  . ARG   K  159 ? 0.62769 0.62769 0.62769 0.00000  0.00000  0.00000  159 ARG   K CB  
15872 C CG  . ARG   K  159 ? 1.08325 1.08325 1.08325 -0.00000 0.00000  0.00000  159 ARG   K CG  
15873 C CD  . ARG   K  159 ? 0.88166 0.88166 0.88166 -0.00000 0.00000  0.00000  159 ARG   K CD  
15874 N NE  . ARG   K  159 ? 1.05723 1.05723 1.05723 0.00000  0.00000  0.00000  159 ARG   K NE  
15875 C CZ  . ARG   K  159 ? 0.94537 0.94537 0.94537 -0.00000 0.00000  0.00000  159 ARG   K CZ  
15876 N NH1 . ARG   K  159 ? 0.85002 0.85002 0.85002 0.00000  0.00000  0.00000  159 ARG   K NH1 
15877 N NH2 . ARG   K  159 ? 0.81482 0.81482 0.81482 0.00000  0.00000  0.00000  159 ARG   K NH2 
15878 N N   . ASN   K  160 ? 0.63493 0.63493 0.63493 -0.00000 0.00000  0.00000  160 ASN   K N   
15879 C CA  . ASN   K  160 ? 0.68997 0.68997 0.68997 0.00000  0.00000  0.00000  160 ASN   K CA  
15880 C C   . ASN   K  160 ? 0.59406 0.59406 0.59406 0.00000  0.00000  0.00000  160 ASN   K C   
15881 O O   . ASN   K  160 ? 0.97113 0.97113 0.97113 0.00000  0.00000  0.00000  160 ASN   K O   
15882 C CB  . ASN   K  160 ? 0.66527 0.66527 0.66527 0.00000  0.00000  0.00000  160 ASN   K CB  
15883 C CG  . ASN   K  160 ? 0.81946 0.81946 0.81946 -0.00000 0.00000  0.00000  160 ASN   K CG  
15884 O OD1 . ASN   K  160 ? 0.98988 0.98988 0.98988 -0.00000 0.00000  -0.00000 160 ASN   K OD1 
15885 N ND2 . ASN   K  160 ? 0.87257 0.87257 0.87257 0.00000  0.00000  0.00000  160 ASN   K ND2 
15886 N N   . VAL   K  161 ? 0.87261 0.87261 0.87261 0.00000  0.00000  0.00000  161 VAL   K N   
15887 C CA  . VAL   K  161 ? 0.90813 0.90813 0.90813 0.00000  -0.00000 0.00000  161 VAL   K CA  
15888 C C   . VAL   K  161 ? 0.94233 0.94233 0.94233 0.00000  0.00000  0.00000  161 VAL   K C   
15889 O O   . VAL   K  161 ? 0.72327 0.72327 0.72327 0.00000  0.00000  0.00000  161 VAL   K O   
15890 C CB  . VAL   K  161 ? 0.83146 0.83146 0.83146 0.00000  0.00000  0.00000  161 VAL   K CB  
15891 C CG1 . VAL   K  161 ? 0.69044 0.69044 0.69044 0.00000  0.00000  0.00000  161 VAL   K CG1 
15892 C CG2 . VAL   K  161 ? 0.62575 0.62575 0.62575 0.00000  0.00000  0.00000  161 VAL   K CG2 
15893 N N   . LEU   K  162 ? 0.71321 0.71321 0.71321 0.00000  0.00000  0.00000  162 LEU   K N   
15894 C CA  . LEU   K  162 ? 0.84551 0.84551 0.84551 0.00000  0.00000  0.00000  162 LEU   K CA  
15895 C C   . LEU   K  162 ? 1.08526 1.08526 1.08526 -0.00000 0.00000  0.00000  162 LEU   K C   
15896 O O   . LEU   K  162 ? 0.86484 0.86484 0.86484 0.00000  -0.00000 0.00000  162 LEU   K O   
15897 C CB  . LEU   K  162 ? 0.80317 0.80317 0.80317 -0.00000 0.00000  0.00000  162 LEU   K CB  
15898 C CG  . LEU   K  162 ? 0.65928 0.65928 0.65928 -0.00000 0.00000  0.00000  162 LEU   K CG  
15899 C CD1 . LEU   K  162 ? 0.60474 0.60474 0.60474 0.00000  0.00000  0.00000  162 LEU   K CD1 
15900 C CD2 . LEU   K  162 ? 0.59009 0.59009 0.59009 0.00000  -0.00000 0.00000  162 LEU   K CD2 
15901 N N   . VAL   K  163 ? 0.82861 0.82861 0.82861 -0.00000 0.00000  0.00000  163 VAL   K N   
15902 C CA  . VAL   K  163 ? 0.79119 0.79119 0.79119 0.00000  0.00000  0.00000  163 VAL   K CA  
15903 C C   . VAL   K  163 ? 1.04988 1.04988 1.04988 -0.00000 -0.00000 0.00000  163 VAL   K C   
15904 O O   . VAL   K  163 ? 0.95594 0.95594 0.95594 -0.00000 0.00000  0.00000  163 VAL   K O   
15905 C CB  . VAL   K  163 ? 0.81602 0.81602 0.81602 0.00000  0.00000  0.00000  163 VAL   K CB  
15906 C CG1 . VAL   K  163 ? 0.73476 0.73476 0.73476 0.00000  0.00000  0.00000  163 VAL   K CG1 
15907 C CG2 . VAL   K  163 ? 0.72879 0.72879 0.72879 0.00000  0.00000  0.00000  163 VAL   K CG2 
15908 N N   . ALA   K  164 ? 0.91776 0.91776 0.91776 0.00000  -0.00000 0.00000  164 ALA   K N   
15909 C CA  . ALA   K  164 ? 1.01409 1.01409 1.01409 0.00000  0.00000  0.00000  164 ALA   K CA  
15910 C C   . ALA   K  164 ? 0.90011 0.90011 0.90011 0.00000  0.00000  0.00000  164 ALA   K C   
15911 O O   . ALA   K  164 ? 0.87370 0.87370 0.87370 0.00000  0.00000  0.00000  164 ALA   K O   
15912 C CB  . ALA   K  164 ? 0.64498 0.64498 0.64498 -0.00000 -0.00000 0.00000  164 ALA   K CB  
15913 N N   . ASP   K  165 ? 0.85265 0.85265 0.85265 0.00000  0.00000  0.00000  165 ASP   K N   
15914 C CA  . ASP   K  165 ? 0.83155 0.83155 0.83155 0.00000  0.00000  0.00000  165 ASP   K CA  
15915 C C   . ASP   K  165 ? 0.82978 0.82978 0.82978 0.00000  0.00000  0.00000  165 ASP   K C   
15916 O O   . ASP   K  165 ? 1.27334 1.27334 1.27334 0.00000  0.00000  0.00000  165 ASP   K O   
15917 C CB  . ASP   K  165 ? 0.92370 0.92370 0.92370 0.00000  0.00000  0.00000  165 ASP   K CB  
15918 C CG  . ASP   K  165 ? 0.77113 0.77113 0.77113 0.00000  0.00000  0.00000  165 ASP   K CG  
15919 O OD1 . ASP   K  165 ? 1.35690 1.35690 1.35690 -0.00000 0.00000  0.00000  165 ASP   K OD1 
15920 O OD2 . ASP   K  165 ? 1.39107 1.39107 1.39107 0.00000  0.00000  0.00000  165 ASP   K OD2 
15921 N N   . GLN   K  166 ? 1.09031 1.09031 1.09031 0.00000  0.00000  0.00000  166 GLN   K N   
15922 C CA  . GLN   K  166 ? 1.27355 1.27355 1.27355 -0.00000 0.00000  0.00000  166 GLN   K CA  
15923 C C   . GLN   K  166 ? 0.79556 0.79556 0.79556 0.00000  0.00000  0.00000  166 GLN   K C   
15924 O O   . GLN   K  166 ? 1.72773 1.72773 1.72773 0.00000  0.00000  0.00000  166 GLN   K O   
15925 C CB  . GLN   K  166 ? 0.76170 0.76170 0.76170 -0.00000 0.00000  0.00000  166 GLN   K CB  
15926 C CG  . GLN   K  166 ? 1.22418 1.22418 1.22418 -0.00000 0.00000  0.00000  166 GLN   K CG  
15927 C CD  . GLN   K  166 ? 1.97673 1.97673 1.97673 0.00000  0.00000  0.00000  166 GLN   K CD  
15928 O OE1 . GLN   K  166 ? 1.40382 1.40382 1.40382 -0.00000 0.00000  0.00000  166 GLN   K OE1 
15929 N NE2 . GLN   K  166 ? 1.23162 1.23162 1.23162 0.00000  0.00000  0.00000  166 GLN   K NE2 
15930 N N   . PHE   K  167 ? 1.01712 1.01712 1.01712 0.00000  0.00000  0.00000  167 PHE   K N   
15931 C CA  . PHE   K  167 ? 1.00392 1.00392 1.00392 0.00000  0.00000  0.00000  167 PHE   K CA  
15932 C C   . PHE   K  167 ? 1.02297 1.02297 1.02297 -0.00000 0.00000  0.00000  167 PHE   K C   
15933 O O   . PHE   K  167 ? 0.97205 0.97205 0.97205 0.00000  0.00000  0.00000  167 PHE   K O   
15934 C CB  . PHE   K  167 ? 0.87856 0.87856 0.87856 0.00000  0.00000  0.00000  167 PHE   K CB  
15935 C CG  . PHE   K  167 ? 0.94817 0.94817 0.94817 0.00000  0.00000  0.00000  167 PHE   K CG  
15936 C CD1 . PHE   K  167 ? 0.79890 0.79890 0.79890 0.00000  0.00000  0.00000  167 PHE   K CD1 
15937 C CD2 . PHE   K  167 ? 0.68628 0.68628 0.68628 -0.00000 0.00000  0.00000  167 PHE   K CD2 
15938 C CE1 . PHE   K  167 ? 1.69462 1.69462 1.69462 0.00000  0.00000  0.00000  167 PHE   K CE1 
15939 C CE2 . PHE   K  167 ? 1.55304 1.55304 1.55304 0.00000  0.00000  0.00000  167 PHE   K CE2 
15940 C CZ  . PHE   K  167 ? 0.53072 0.53072 0.53072 -0.00000 0.00000  0.00000  167 PHE   K CZ  
15941 N N   . ASP   K  168 ? 1.37474 1.37474 1.37474 0.00000  0.00000  0.00000  168 ASP   K N   
15942 C CA  . ASP   K  168 ? 0.93492 0.93492 0.93492 0.00000  0.00000  0.00000  168 ASP   K CA  
15943 C C   . ASP   K  168 ? 1.58478 1.58478 1.58478 -0.00000 0.00000  0.00000  168 ASP   K C   
15944 O O   . ASP   K  168 ? 1.24946 1.24946 1.24946 0.00000  0.00000  0.00000  168 ASP   K O   
15945 C CB  . ASP   K  168 ? 1.11324 1.11324 1.11324 0.00000  0.00000  0.00000  168 ASP   K CB  
15946 C CG  . ASP   K  168 ? 1.42718 1.42718 1.42718 -0.00000 0.00000  0.00000  168 ASP   K CG  
15947 O OD1 . ASP   K  168 ? 1.24773 1.24773 1.24773 0.00000  0.00000  0.00000  168 ASP   K OD1 
15948 O OD2 . ASP   K  168 ? 1.39875 1.39875 1.39875 -0.00000 0.00000  0.00000  168 ASP   K OD2 
15949 N N   . ASP   K  169 ? 1.12821 1.12821 1.12821 -0.00000 0.00000  0.00000  169 ASP   K N   
15950 C CA  . ASP   K  169 ? 1.17750 1.17750 1.17750 0.00000  0.00000  0.00000  169 ASP   K CA  
15951 C C   . ASP   K  169 ? 1.39088 1.39088 1.39088 -0.00000 0.00000  0.00000  169 ASP   K C   
15952 O O   . ASP   K  169 ? 1.23673 1.23673 1.23673 0.00000  0.00000  0.00000  169 ASP   K O   
15953 C CB  . ASP   K  169 ? 0.90625 0.90625 0.90625 0.00000  0.00000  0.00000  169 ASP   K CB  
15954 N N   . ARG   K  170 ? 1.96929 1.96929 1.96929 0.00000  0.00000  -0.00000 170 ARG   K N   
15955 C CA  . ARG   K  170 ? 0.84082 0.84082 0.84082 -0.00000 0.00000  0.00000  170 ARG   K CA  
15956 C C   . ARG   K  170 ? 1.07239 1.07239 1.07239 0.00000  0.00000  0.00000  170 ARG   K C   
15957 O O   . ARG   K  170 ? 0.95861 0.95861 0.95861 0.00000  0.00000  0.00000  170 ARG   K O   
15958 C CB  . ARG   K  170 ? 0.91495 0.91495 0.91495 0.00000  0.00000  0.00000  170 ARG   K CB  
15959 N N   . HIS   K  171 ? 1.05875 1.05875 1.05875 -0.00000 0.00000  0.00000  171 HIS   K N   
15960 C CA  . HIS   K  171 ? 1.09966 1.09966 1.09966 -0.00000 0.00000  0.00000  171 HIS   K CA  
15961 C C   . HIS   K  171 ? 0.67605 0.67605 0.67605 0.00000  0.00000  0.00000  171 HIS   K C   
15962 O O   . HIS   K  171 ? 1.57880 1.57880 1.57880 0.00000  0.00000  -0.00000 171 HIS   K O   
15963 C CB  . HIS   K  171 ? 1.13474 1.13474 1.13474 0.00000  0.00000  0.00000  171 HIS   K CB  
15964 C CG  . HIS   K  171 ? 1.07374 1.07374 1.07374 -0.00000 0.00000  0.00000  171 HIS   K CG  
15965 N ND1 . HIS   K  171 ? 1.14546 1.14546 1.14546 0.00000  0.00000  -0.00000 171 HIS   K ND1 
15966 C CD2 . HIS   K  171 ? 1.07662 1.07662 1.07662 0.00000  0.00000  -0.00000 171 HIS   K CD2 
15967 C CE1 . HIS   K  171 ? 0.82572 0.82572 0.82572 -0.00000 0.00000  0.00000  171 HIS   K CE1 
15968 N NE2 . HIS   K  171 ? 1.77894 1.77894 1.77894 0.00000  0.00000  0.00000  171 HIS   K NE2 
15969 N N   . CYS   K  172 ? 1.08478 1.08478 1.08478 -0.00000 0.00000  0.00000  172 CYS   K N   
15970 C CA  . CYS   K  172 ? 0.69629 0.69629 0.69629 0.00000  0.00000  0.00000  172 CYS   K CA  
15971 C C   . CYS   K  172 ? 0.70970 0.70970 0.70970 -0.00000 0.00000  0.00000  172 CYS   K C   
15972 O O   . CYS   K  172 ? 1.00010 1.00010 1.00010 0.00000  0.00000  0.00000  172 CYS   K O   
15973 C CB  . CYS   K  172 ? 0.81174 0.81174 0.81174 0.00000  0.00000  0.00000  172 CYS   K CB  
15974 S SG  . CYS   K  172 ? 0.91273 0.91273 0.91273 0.00000  0.00000  0.00000  172 CYS   K SG  
15975 N N   . GLY   K  173 ? 0.77626 0.77626 0.77626 0.00000  0.00000  0.00000  173 GLY   K N   
15976 C CA  . GLY   K  173 ? 0.58188 0.58188 0.58188 -0.00000 0.00000  0.00000  173 GLY   K CA  
15977 C C   . GLY   K  173 ? 0.76638 0.76638 0.76638 0.00000  0.00000  0.00000  173 GLY   K C   
15978 O O   . GLY   K  173 ? 0.76709 0.76709 0.76709 0.00000  0.00000  0.00000  173 GLY   K O   
15979 N N   . TRP   K  174 ? 0.64227 0.64227 0.64227 -0.00000 0.00000  0.00000  174 TRP   K N   
15980 C CA  . TRP   K  174 ? 0.96622 0.96622 0.96622 0.00000  0.00000  0.00000  174 TRP   K CA  
15981 C C   . TRP   K  174 ? 1.07492 1.07492 1.07492 0.00000  0.00000  0.00000  174 TRP   K C   
15982 O O   . TRP   K  174 ? 0.87457 0.87457 0.87457 0.00000  0.00000  0.00000  174 TRP   K O   
15983 C CB  . TRP   K  174 ? 0.68447 0.68447 0.68447 0.00000  0.00000  0.00000  174 TRP   K CB  
15984 C CG  . TRP   K  174 ? 1.06506 1.06506 1.06506 0.00000  0.00000  0.00000  174 TRP   K CG  
15985 C CD1 . TRP   K  174 ? 0.78581 0.78581 0.78581 0.00000  0.00000  0.00000  174 TRP   K CD1 
15986 C CD2 . TRP   K  174 ? 0.89616 0.89616 0.89616 -0.00000 0.00000  0.00000  174 TRP   K CD2 
15987 N NE1 . TRP   K  174 ? 0.81723 0.81723 0.81723 0.00000  0.00000  0.00000  174 TRP   K NE1 
15988 C CE2 . TRP   K  174 ? 0.71666 0.71666 0.71666 0.00000  0.00000  0.00000  174 TRP   K CE2 
15989 C CE3 . TRP   K  174 ? 0.74475 0.74475 0.74475 0.00000  0.00000  0.00000  174 TRP   K CE3 
15990 C CZ2 . TRP   K  174 ? 0.62055 0.62055 0.62055 0.00000  0.00000  0.00000  174 TRP   K CZ2 
15991 C CZ3 . TRP   K  174 ? 0.77052 0.77052 0.77052 0.00000  0.00000  0.00000  174 TRP   K CZ3 
15992 C CH2 . TRP   K  174 ? 0.65847 0.65847 0.65847 0.00000  0.00000  0.00000  174 TRP   K CH2 
15993 N N   . LEU   K  175 ? 0.88470 0.88470 0.88470 0.00000  0.00000  0.00000  175 LEU   K N   
15994 C CA  . LEU   K  175 ? 0.82079 0.82079 0.82079 -0.00000 0.00000  0.00000  175 LEU   K CA  
15995 C C   . LEU   K  175 ? 0.94360 0.94360 0.94360 0.00000  0.00000  0.00000  175 LEU   K C   
15996 O O   . LEU   K  175 ? 1.05568 1.05568 1.05568 0.00000  0.00000  0.00000  175 LEU   K O   
15997 C CB  . LEU   K  175 ? 0.75742 0.75742 0.75742 0.00000  0.00000  0.00000  175 LEU   K CB  
15998 C CG  . LEU   K  175 ? 0.89182 0.89182 0.89182 0.00000  0.00000  0.00000  175 LEU   K CG  
15999 C CD1 . LEU   K  175 ? 0.77208 0.77208 0.77208 0.00000  0.00000  0.00000  175 LEU   K CD1 
16000 C CD2 . LEU   K  175 ? 0.73339 0.73339 0.73339 -0.00000 0.00000  0.00000  175 LEU   K CD2 
16001 N N   . ASN   K  176 ? 0.67100 0.67100 0.67100 0.00000  0.00000  0.00000  176 ASN   K N   
16002 C CA  . ASN   K  176 ? 0.61514 0.61514 0.61514 -0.00000 0.00000  0.00000  176 ASN   K CA  
16003 C C   . ASN   K  176 ? 0.82296 0.82296 0.82296 -0.00000 0.00000  0.00000  176 ASN   K C   
16004 O O   . ASN   K  176 ? 0.99882 0.99882 0.99882 0.00000  0.00000  0.00000  176 ASN   K O   
16005 C CB  . ASN   K  176 ? 0.95612 0.95612 0.95612 0.00000  0.00000  0.00000  176 ASN   K CB  
16006 C CG  . ASN   K  176 ? 0.93473 0.93473 0.93473 0.00000  0.00000  0.00000  176 ASN   K CG  
16007 O OD1 . ASN   K  176 ? 0.75978 0.75978 0.75978 0.00000  0.00000  0.00000  176 ASN   K OD1 
16008 N ND2 . ASN   K  176 ? 0.77677 0.77677 0.77677 -0.00000 0.00000  0.00000  176 ASN   K ND2 
16009 N N   . GLU   K  177 ? 1.02699 1.02699 1.02699 0.00000  0.00000  0.00000  177 GLU   K N   
16010 C CA  . GLU   K  177 ? 0.99278 0.99278 0.99278 0.00000  0.00000  0.00000  177 GLU   K CA  
16011 C C   . GLU   K  177 ? 0.91388 0.91388 0.91388 0.00000  0.00000  0.00000  177 GLU   K C   
16012 O O   . GLU   K  177 ? 1.03100 1.03100 1.03100 0.00000  0.00000  0.00000  177 GLU   K O   
16013 C CB  . GLU   K  177 ? 0.76167 0.76167 0.76167 0.00000  0.00000  0.00000  177 GLU   K CB  
16014 N N   . ARG   K  178 ? 0.68411 0.68411 0.68411 0.00000  0.00000  0.00000  178 ARG   K N   
16015 C CA  . ARG   K  178 ? 0.98253 0.98253 0.98253 0.00000  0.00000  0.00000  178 ARG   K CA  
16016 C C   . ARG   K  178 ? 0.93410 0.93410 0.93410 -0.00000 0.00000  0.00000  178 ARG   K C   
16017 O O   . ARG   K  178 ? 0.91459 0.91459 0.91459 0.00000  0.00000  0.00000  178 ARG   K O   
16018 C CB  . ARG   K  178 ? 0.54158 0.54158 0.54158 -0.00000 0.00000  0.00000  178 ARG   K CB  
16019 C CG  . ARG   K  178 ? 1.22554 1.22554 1.22554 0.00000  0.00000  0.00000  178 ARG   K CG  
16020 C CD  . ARG   K  178 ? 1.47905 1.47905 1.47905 -0.00000 0.00000  0.00000  178 ARG   K CD  
16021 N NE  . ARG   K  178 ? 1.53650 1.53650 1.53650 0.00000  0.00000  0.00000  178 ARG   K NE  
16022 C CZ  . ARG   K  178 ? 2.16055 2.16055 2.16055 -0.00000 0.00000  0.00000  178 ARG   K CZ  
16023 N NH1 . ARG   K  178 ? 2.02341 2.02341 2.02341 0.00000  0.00000  0.00000  178 ARG   K NH1 
16024 N NH2 . ARG   K  178 ? 1.64376 1.64376 1.64376 -0.00000 0.00000  0.00000  178 ARG   K NH2 
16025 N N   . ALA   K  179 ? 1.03467 1.03467 1.03467 0.00000  0.00000  0.00000  179 ALA   K N   
16026 C CA  . ALA   K  179 ? 1.01777 1.01777 1.01777 0.00000  0.00000  0.00000  179 ALA   K CA  
16027 C C   . ALA   K  179 ? 0.87611 0.87611 0.87611 -0.00000 0.00000  0.00000  179 ALA   K C   
16028 O O   . ALA   K  179 ? 0.97294 0.97294 0.97294 0.00000  0.00000  0.00000  179 ALA   K O   
16029 C CB  . ALA   K  179 ? 0.71178 0.71178 0.71178 0.00000  0.00000  0.00000  179 ALA   K CB  
16030 N N   . LEU   K  180 ? 1.04866 1.04866 1.04866 0.00000  0.00000  0.00000  180 LEU   K N   
16031 C CA  . LEU   K  180 ? 0.88345 0.88345 0.88345 0.00000  0.00000  0.00000  180 LEU   K CA  
16032 C C   . LEU   K  180 ? 1.09088 1.09088 1.09088 0.00000  0.00000  0.00000  180 LEU   K C   
16033 O O   . LEU   K  180 ? 1.09240 1.09240 1.09240 0.00000  0.00000  0.00000  180 LEU   K O   
16034 C CB  . LEU   K  180 ? 0.82436 0.82436 0.82436 -0.00000 0.00000  0.00000  180 LEU   K CB  
16035 C CG  . LEU   K  180 ? 1.13867 1.13867 1.13867 0.00000  0.00000  0.00000  180 LEU   K CG  
16036 C CD1 . LEU   K  180 ? 1.10867 1.10867 1.10867 -0.00000 0.00000  0.00000  180 LEU   K CD1 
16037 C CD2 . LEU   K  180 ? 0.98257 0.98257 0.98257 -0.00000 0.00000  0.00000  180 LEU   K CD2 
16038 N N   . SER   K  181 ? 1.06123 1.06123 1.06123 0.00000  0.00000  0.00000  181 SER   K N   
16039 C CA  . SER   K  181 ? 1.11077 1.11077 1.11077 -0.00000 0.00000  0.00000  181 SER   K CA  
16040 C C   . SER   K  181 ? 0.95498 0.95498 0.95498 0.00000  -0.00000 0.00000  181 SER   K C   
16041 O O   . SER   K  181 ? 1.09826 1.09826 1.09826 -0.00000 0.00000  0.00000  181 SER   K O   
16042 C CB  . SER   K  181 ? 0.88761 0.88761 0.88761 0.00000  -0.00000 -0.00000 181 SER   K CB  
16043 O OG  . SER   K  181 ? 1.75163 1.75163 1.75163 0.00000  0.00000  0.00000  181 SER   K OG  
16044 N N   . ALA   K  182 ? 1.05479 1.05479 1.05479 0.00000  0.00000  0.00000  182 ALA   K N   
16045 C CA  . ALA   K  182 ? 1.32923 1.32923 1.32923 -0.00000 0.00000  0.00000  182 ALA   K CA  
16046 C C   . ALA   K  182 ? 1.06971 1.06971 1.06971 0.00000  0.00000  0.00000  182 ALA   K C   
16047 O O   . ALA   K  182 ? 0.91553 0.91553 0.91553 -0.00000 0.00000  0.00000  182 ALA   K O   
16048 C CB  . ALA   K  182 ? 0.80394 0.80394 0.80394 0.00000  0.00000  0.00000  182 ALA   K CB  
16049 N N   . MET   K  183 ? 0.81728 0.81728 0.81728 0.00000  0.00000  0.00000  183 MET   K N   
16050 C CA  . MET   K  183 ? 1.02153 1.02153 1.02153 0.00000  0.00000  0.00000  183 MET   K CA  
16051 C C   . MET   K  183 ? 0.83586 0.83586 0.83586 0.00000  0.00000  0.00000  183 MET   K C   
16052 O O   . MET   K  183 ? 1.07137 1.07137 1.07137 0.00000  0.00000  0.00000  183 MET   K O   
16053 C CB  . MET   K  183 ? 0.82724 0.82724 0.82724 0.00000  0.00000  0.00000  183 MET   K CB  
16054 C CG  . MET   K  183 ? 0.85386 0.85386 0.85386 0.00000  0.00000  0.00000  183 MET   K CG  
16055 S SD  . MET   K  183 ? 0.97051 0.97051 0.97051 0.00000  0.00000  0.00000  183 MET   K SD  
16056 C CE  . MET   K  183 ? 0.92306 0.92306 0.92306 0.00000  0.00000  0.00000  183 MET   K CE  
16057 N N   . VAL   K  184 ? 1.18370 1.18370 1.18370 0.00000  0.00000  0.00000  184 VAL   K N   
16058 C CA  . VAL   K  184 ? 1.27056 1.27056 1.27056 -0.00000 0.00000  0.00000  184 VAL   K CA  
16059 C C   . VAL   K  184 ? 1.03680 1.03680 1.03680 0.00000  0.00000  0.00000  184 VAL   K C   
16060 O O   . VAL   K  184 ? 1.17515 1.17515 1.17515 0.00000  -0.00000 0.00000  184 VAL   K O   
16061 C CB  . VAL   K  184 ? 1.00981 1.00981 1.00981 0.00000  0.00000  0.00000  184 VAL   K CB  
16062 C CG1 . VAL   K  184 ? 1.07962 1.07962 1.07962 -0.00000 0.00000  0.00000  184 VAL   K CG1 
16063 C CG2 . VAL   K  184 ? 1.02387 1.02387 1.02387 0.00000  0.00000  0.00000  184 VAL   K CG2 
16064 N N   . LYS   K  185 ? 1.09773 1.09773 1.09773 0.00000  0.00000  0.00000  185 LYS   K N   
16065 C CA  . LYS   K  185 ? 1.13415 1.13415 1.13415 0.00000  0.00000  0.00000  185 LYS   K CA  
16066 C C   . LYS   K  185 ? 0.82666 0.82666 0.82666 -0.00000 0.00000  0.00000  185 LYS   K C   
16067 O O   . LYS   K  185 ? 1.56666 1.56666 1.56666 -0.00000 0.00000  0.00000  185 LYS   K O   
16068 C CB  . LYS   K  185 ? 0.99001 0.99001 0.99001 0.00000  0.00000  0.00000  185 LYS   K CB  
16069 C CG  . LYS   K  185 ? 1.06859 1.06859 1.06859 0.00000  0.00000  0.00000  185 LYS   K CG  
16070 C CD  . LYS   K  185 ? 1.39075 1.39075 1.39075 0.00000  0.00000  0.00000  185 LYS   K CD  
16071 C CE  . LYS   K  185 ? 1.39891 1.39891 1.39891 0.00000  0.00000  0.00000  185 LYS   K CE  
16072 N NZ  . LYS   K  185 ? 1.57274 1.57274 1.57274 0.00000  0.00000  0.00000  185 LYS   K NZ  
16073 N N   . HIS   K  186 ? 1.10747 1.10747 1.10747 -0.00000 0.00000  0.00000  186 HIS   K N   
16074 C CA  . HIS   K  186 ? 0.88063 0.88063 0.88063 0.00000  0.00000  -0.00000 186 HIS   K CA  
16075 C C   . HIS   K  186 ? 1.12429 1.12429 1.12429 0.00000  0.00000  0.00000  186 HIS   K C   
16076 O O   . HIS   K  186 ? 0.94892 0.94892 0.94892 0.00000  0.00000  0.00000  186 HIS   K O   
16077 C CB  . HIS   K  186 ? 0.98760 0.98760 0.98760 0.00000  0.00000  0.00000  186 HIS   K CB  
16078 C CG  . HIS   K  186 ? 1.31745 1.31745 1.31745 0.00000  0.00000  0.00000  186 HIS   K CG  
16079 N ND1 . HIS   K  186 ? 1.15252 1.15252 1.15252 0.00000  0.00000  -0.00000 186 HIS   K ND1 
16080 C CD2 . HIS   K  186 ? 0.80626 0.80626 0.80626 0.00000  0.00000  0.00000  186 HIS   K CD2 
16081 C CE1 . HIS   K  186 ? 0.99774 0.99774 0.99774 -0.00000 0.00000  0.00000  186 HIS   K CE1 
16082 N NE2 . HIS   K  186 ? 1.20109 1.20109 1.20109 0.00000  0.00000  0.00000  186 HIS   K NE2 
16083 N N   . TYR   K  187 ? 1.08109 1.08109 1.08109 0.00000  0.00000  0.00000  187 TYR   K N   
16084 C CA  . TYR   K  187 ? 1.18190 1.18190 1.18190 -0.00000 0.00000  0.00000  187 TYR   K CA  
16085 C C   . TYR   K  187 ? 1.63642 1.63642 1.63642 0.00000  0.00000  0.00000  187 TYR   K C   
16086 O O   . TYR   K  187 ? 1.09880 1.09880 1.09880 0.00000  0.00000  0.00000  187 TYR   K O   
16087 C CB  . TYR   K  187 ? 1.23903 1.23903 1.23903 -0.00000 0.00000  0.00000  187 TYR   K CB  
16088 C CG  . TYR   K  187 ? 1.03648 1.03648 1.03648 0.00000  -0.00000 0.00000  187 TYR   K CG  
16089 C CD1 . TYR   K  187 ? 1.14317 1.14317 1.14317 0.00000  0.00000  0.00000  187 TYR   K CD1 
16090 C CD2 . TYR   K  187 ? 1.22299 1.22299 1.22299 -0.00000 0.00000  0.00000  187 TYR   K CD2 
16091 C CE1 . TYR   K  187 ? 1.09141 1.09141 1.09141 0.00000  0.00000  0.00000  187 TYR   K CE1 
16092 C CE2 . TYR   K  187 ? 0.87035 0.87035 0.87035 0.00000  0.00000  0.00000  187 TYR   K CE2 
16093 C CZ  . TYR   K  187 ? 1.21712 1.21712 1.21712 -0.00000 -0.00000 0.00000  187 TYR   K CZ  
16094 O OH  . TYR   K  187 ? 1.13343 1.13343 1.13343 0.00000  0.00000  0.00000  187 TYR   K OH  
16095 N N   . ASN   K  188 ? 1.22540 1.22540 1.22540 -0.00000 0.00000  0.00000  188 ASN   K N   
16096 C CA  . ASN   K  188 ? 1.85497 1.85497 1.85497 -0.00000 0.00000  0.00000  188 ASN   K CA  
16097 C C   . ASN   K  188 ? 1.21234 1.21234 1.21234 0.00000  0.00000  0.00000  188 ASN   K C   
16098 O O   . ASN   K  188 ? 1.63641 1.63641 1.63641 0.00000  0.00000  0.00000  188 ASN   K O   
16099 C CB  . ASN   K  188 ? 1.35776 1.35776 1.35776 0.00000  0.00000  0.00000  188 ASN   K CB  
16100 C CG  . ASN   K  188 ? 1.85558 1.85558 1.85558 0.00000  0.00000  0.00000  188 ASN   K CG  
16101 O OD1 . ASN   K  188 ? 2.20830 2.20830 2.20830 -0.00000 0.00000  0.00000  188 ASN   K OD1 
16102 N ND2 . ASN   K  188 ? 2.01821 2.01821 2.01821 0.00000  0.00000  0.00000  188 ASN   K ND2 
16103 N N   . GLY   K  189 ? 1.17712 1.17712 1.17712 -0.00000 0.00000  0.00000  189 GLY   K N   
16104 C CA  . GLY   K  189 ? 0.75812 0.75812 0.75812 0.00000  0.00000  0.00000  189 GLY   K CA  
16105 C C   . GLY   K  189 ? 0.81087 0.81087 0.81087 -0.00000 0.00000  0.00000  189 GLY   K C   
16106 O O   . GLY   K  189 ? 1.22751 1.22751 1.22751 0.00000  0.00000  0.00000  189 GLY   K O   
16107 N N   . ARG   K  190 ? 1.24696 1.24696 1.24696 0.00000  0.00000  0.00000  190 ARG   K N   
16108 C CA  . ARG   K  190 ? 1.09702 1.09702 1.09702 0.00000  0.00000  0.00000  190 ARG   K CA  
16109 C C   . ARG   K  190 ? 1.18714 1.18714 1.18714 0.00000  0.00000  0.00000  190 ARG   K C   
16110 O O   . ARG   K  190 ? 1.32249 1.32249 1.32249 0.00000  0.00000  0.00000  190 ARG   K O   
16111 C CB  . ARG   K  190 ? 1.18834 1.18834 1.18834 0.00000  0.00000  0.00000  190 ARG   K CB  
16112 C CG  . ARG   K  190 ? 1.12066 1.12066 1.12066 0.00000  0.00000  0.00000  190 ARG   K CG  
16113 C CD  . ARG   K  190 ? 1.00041 1.00041 1.00041 0.00000  0.00000  0.00000  190 ARG   K CD  
16114 N NE  . ARG   K  190 ? 1.18604 1.18604 1.18604 0.00000  -0.00000 -0.00000 190 ARG   K NE  
16115 C CZ  . ARG   K  190 ? 1.40110 1.40110 1.40110 0.00000  0.00000  0.00000  190 ARG   K CZ  
16116 N NH1 . ARG   K  190 ? 1.35369 1.35369 1.35369 0.00000  0.00000  0.00000  190 ARG   K NH1 
16117 N NH2 . ARG   K  190 ? 1.21941 1.21941 1.21941 0.00000  0.00000  0.00000  190 ARG   K NH2 
16118 N N   . ALA   K  191 ? 1.20505 1.20505 1.20505 0.00000  0.00000  0.00000  191 ALA   K N   
16119 C CA  . ALA   K  191 ? 1.05047 1.05047 1.05047 0.00000  0.00000  0.00000  191 ALA   K CA  
16120 C C   . ALA   K  191 ? 1.84885 1.84885 1.84885 -0.00000 0.00000  0.00000  191 ALA   K C   
16121 O O   . ALA   K  191 ? 1.06637 1.06637 1.06637 0.00000  0.00000  0.00000  191 ALA   K O   
16122 C CB  . ALA   K  191 ? 1.20646 1.20646 1.20646 0.00000  0.00000  0.00000  191 ALA   K CB  
16123 N N   . PHE   K  192 ? 0.97646 0.97646 0.97646 0.00000  0.00000  0.00000  192 PHE   K N   
16124 C CA  . PHE   K  192 ? 1.02551 1.02551 1.02551 0.00000  0.00000  0.00000  192 PHE   K CA  
16125 C C   . PHE   K  192 ? 1.32753 1.32753 1.32753 0.00000  0.00000  0.00000  192 PHE   K C   
16126 O O   . PHE   K  192 ? 1.19568 1.19568 1.19568 0.00000  0.00000  0.00000  192 PHE   K O   
16127 C CB  . PHE   K  192 ? 1.04500 1.04500 1.04500 0.00000  0.00000  0.00000  192 PHE   K CB  
16128 C CG  . PHE   K  192 ? 1.13948 1.13948 1.13948 0.00000  -0.00000 -0.00000 192 PHE   K CG  
16129 C CD1 . PHE   K  192 ? 1.25532 1.25532 1.25532 -0.00000 0.00000  0.00000  192 PHE   K CD1 
16130 C CD2 . PHE   K  192 ? 1.24201 1.24201 1.24201 0.00000  0.00000  0.00000  192 PHE   K CD2 
16131 C CE1 . PHE   K  192 ? 1.00952 1.00952 1.00952 0.00000  0.00000  0.00000  192 PHE   K CE1 
16132 C CE2 . PHE   K  192 ? 1.31929 1.31929 1.31929 0.00000  -0.00000 0.00000  192 PHE   K CE2 
16133 C CZ  . PHE   K  192 ? 1.10961 1.10961 1.10961 0.00000  0.00000  0.00000  192 PHE   K CZ  
16134 N N   . ASP   K  193 ? 1.37266 1.37266 1.37266 -0.00000 0.00000  0.00000  193 ASP   K N   
16135 C CA  . ASP   K  193 ? 1.12058 1.12058 1.12058 0.00000  0.00000  0.00000  193 ASP   K CA  
16136 C C   . ASP   K  193 ? 1.45613 1.45613 1.45613 0.00000  0.00000  0.00000  193 ASP   K C   
16137 O O   . ASP   K  193 ? 0.96075 0.96075 0.96075 0.00000  0.00000  0.00000  193 ASP   K O   
16138 C CB  . ASP   K  193 ? 1.28384 1.28384 1.28384 -0.00000 0.00000  0.00000  193 ASP   K CB  
16139 C CG  . ASP   K  193 ? 1.82694 1.82694 1.82694 -0.00000 0.00000  0.00000  193 ASP   K CG  
16140 O OD1 . ASP   K  193 ? 1.32941 1.32941 1.32941 0.00000  0.00000  0.00000  193 ASP   K OD1 
16141 O OD2 . ASP   K  193 ? 1.31039 1.31039 1.31039 -0.00000 -0.00000 -0.00000 193 ASP   K OD2 
16142 N N   . GLU   K  194 ? 1.07342 1.07342 1.07342 0.00000  0.00000  0.00000  194 GLU   K N   
16143 C CA  . GLU   K  194 ? 1.41501 1.41501 1.41501 0.00000  0.00000  0.00000  194 GLU   K CA  
16144 C C   . GLU   K  194 ? 1.47045 1.47045 1.47045 -0.00000 0.00000  0.00000  194 GLU   K C   
16145 O O   . GLU   K  194 ? 1.32472 1.32472 1.32472 0.00000  0.00000  0.00000  194 GLU   K O   
16146 C CB  . GLU   K  194 ? 1.31069 1.31069 1.31069 0.00000  0.00000  0.00000  194 GLU   K CB  
16147 C CG  . GLU   K  194 ? 1.13055 1.13055 1.13055 -0.00000 0.00000  0.00000  194 GLU   K CG  
16148 C CD  . GLU   K  194 ? 1.85973 1.85973 1.85973 -0.00000 0.00000  0.00000  194 GLU   K CD  
16149 O OE1 . GLU   K  194 ? 1.53818 1.53818 1.53818 -0.00000 0.00000  0.00000  194 GLU   K OE1 
16150 O OE2 . GLU   K  194 ? 1.50718 1.50718 1.50718 0.00000  0.00000  0.00000  194 GLU   K OE2 
16151 N N   . VAL   K  195 ? 1.28038 1.28038 1.28038 -0.00000 0.00000  0.00000  195 VAL   K N   
16152 C CA  . VAL   K  195 ? 0.87256 0.87256 0.87256 0.00000  0.00000  0.00000  195 VAL   K CA  
16153 C C   . VAL   K  195 ? 1.65053 1.65053 1.65053 -0.00000 -0.00000 0.00000  195 VAL   K C   
16154 O O   . VAL   K  195 ? 1.03993 1.03993 1.03993 -0.00000 0.00000  0.00000  195 VAL   K O   
16155 C CB  . VAL   K  195 ? 1.31882 1.31882 1.31882 0.00000  0.00000  0.00000  195 VAL   K CB  
16156 C CG1 . VAL   K  195 ? 0.93470 0.93470 0.93470 0.00000  0.00000  0.00000  195 VAL   K CG1 
16157 C CG2 . VAL   K  195 ? 0.99799 0.99799 0.99799 0.00000  0.00000  0.00000  195 VAL   K CG2 
16158 N N   . PHE   K  196 ? 0.96869 0.96869 0.96869 -0.00000 0.00000  0.00000  196 PHE   K N   
16159 C CA  . PHE   K  196 ? 1.37296 1.37296 1.37296 0.00000  0.00000  0.00000  196 PHE   K CA  
16160 C C   . PHE   K  196 ? 1.12592 1.12592 1.12592 0.00000  0.00000  0.00000  196 PHE   K C   
16161 O O   . PHE   K  196 ? 1.15456 1.15456 1.15456 -0.00000 0.00000  0.00000  196 PHE   K O   
16162 C CB  . PHE   K  196 ? 1.02774 1.02774 1.02774 0.00000  0.00000  0.00000  196 PHE   K CB  
16163 C CG  . PHE   K  196 ? 1.24882 1.24882 1.24882 -0.00000 0.00000  0.00000  196 PHE   K CG  
16164 C CD1 . PHE   K  196 ? 1.04244 1.04244 1.04244 -0.00000 0.00000  0.00000  196 PHE   K CD1 
16165 C CD2 . PHE   K  196 ? 0.95901 0.95901 0.95901 0.00000  0.00000  0.00000  196 PHE   K CD2 
16166 C CE1 . PHE   K  196 ? 1.09329 1.09329 1.09329 -0.00000 0.00000  0.00000  196 PHE   K CE1 
16167 C CE2 . PHE   K  196 ? 1.18933 1.18933 1.18933 0.00000  0.00000  0.00000  196 PHE   K CE2 
16168 C CZ  . PHE   K  196 ? 1.08026 1.08026 1.08026 0.00000  0.00000  0.00000  196 PHE   K CZ  
16169 N N   . LEU   K  197 ? 0.96267 0.96267 0.96267 -0.00000 0.00000  0.00000  197 LEU   K N   
16170 C CA  . LEU   K  197 ? 0.99846 0.99846 0.99846 -0.00000 0.00000  0.00000  197 LEU   K CA  
16171 C C   . LEU   K  197 ? 1.23396 1.23396 1.23396 0.00000  0.00000  0.00000  197 LEU   K C   
16172 O O   . LEU   K  197 ? 0.92238 0.92238 0.92238 -0.00000 0.00000  0.00000  197 LEU   K O   
16173 C CB  . LEU   K  197 ? 0.96722 0.96722 0.96722 0.00000  0.00000  0.00000  197 LEU   K CB  
16174 C CG  . LEU   K  197 ? 0.92537 0.92537 0.92537 -0.00000 0.00000  0.00000  197 LEU   K CG  
16175 C CD1 . LEU   K  197 ? 1.02980 1.02980 1.02980 0.00000  0.00000  0.00000  197 LEU   K CD1 
16176 C CD2 . LEU   K  197 ? 1.52318 1.52318 1.52318 0.00000  0.00000  0.00000  197 LEU   K CD2 
16177 N N   . CYS   K  198 ? 1.06815 1.06815 1.06815 0.00000  0.00000  0.00000  198 CYS   K N   
16178 C CA  . CYS   K  198 ? 1.05769 1.05769 1.05769 -0.00000 0.00000  0.00000  198 CYS   K CA  
16179 C C   . CYS   K  198 ? 1.10367 1.10367 1.10367 -0.00000 0.00000  0.00000  198 CYS   K C   
16180 O O   . CYS   K  198 ? 1.19356 1.19356 1.19356 -0.00000 0.00000  0.00000  198 CYS   K O   
16181 C CB  . CYS   K  198 ? 0.97478 0.97478 0.97478 0.00000  0.00000  0.00000  198 CYS   K CB  
16182 S SG  . CYS   K  198 ? 1.08543 1.08543 1.08543 0.00000  0.00000  0.00000  198 CYS   K SG  
16183 N N   . ASP   K  199 ? 1.10460 1.10460 1.10460 0.00000  0.00000  0.00000  199 ASP   K N   
16184 C CA  . ASP   K  199 ? 0.95863 0.95863 0.95863 -0.00000 0.00000  0.00000  199 ASP   K CA  
16185 C C   . ASP   K  199 ? 1.39705 1.39705 1.39705 0.00000  0.00000  0.00000  199 ASP   K C   
16186 O O   . ASP   K  199 ? 0.95553 0.95553 0.95553 0.00000  0.00000  0.00000  199 ASP   K O   
16187 C CB  . ASP   K  199 ? 0.98149 0.98149 0.98149 0.00000  0.00000  0.00000  199 ASP   K CB  
16188 C CG  . ASP   K  199 ? 2.26508 2.26508 2.26508 0.00000  0.00000  -0.00000 199 ASP   K CG  
16189 O OD1 . ASP   K  199 ? 1.01741 1.01741 1.01741 -0.00000 0.00000  0.00000  199 ASP   K OD1 
16190 O OD2 . ASP   K  199 ? 1.11493 1.11493 1.11493 0.00000  0.00000  0.00000  199 ASP   K OD2 
16191 N N   . LYS   K  200 ? 0.80560 0.80560 0.80560 0.00000  -0.00000 0.00000  200 LYS   K N   
16192 C CA  . LYS   K  200 ? 1.12807 1.12807 1.12807 0.00000  0.00000  0.00000  200 LYS   K CA  
16193 C C   . LYS   K  200 ? 1.08683 1.08683 1.08683 0.00000  0.00000  0.00000  200 LYS   K C   
16194 O O   . LYS   K  200 ? 0.98192 0.98192 0.98192 -0.00000 0.00000  0.00000  200 LYS   K O   
16195 C CB  . LYS   K  200 ? 0.80326 0.80326 0.80326 0.00000  0.00000  0.00000  200 LYS   K CB  
16196 C CG  . LYS   K  200 ? 1.09190 1.09190 1.09190 0.00000  0.00000  0.00000  200 LYS   K CG  
16197 C CD  . LYS   K  200 ? 1.35166 1.35166 1.35166 0.00000  0.00000  0.00000  200 LYS   K CD  
16198 C CE  . LYS   K  200 ? 1.13988 1.13988 1.13988 0.00000  0.00000  0.00000  200 LYS   K CE  
16199 N NZ  . LYS   K  200 ? 1.07123 1.07123 1.07123 0.00000  0.00000  0.00000  200 LYS   K NZ  
16200 N N   . ASN   K  201 ? 0.97630 0.97630 0.97630 0.00000  0.00000  0.00000  201 ASN   K N   
16201 C CA  . ASN   K  201 ? 1.26965 1.26965 1.26965 0.00000  0.00000  0.00000  201 ASN   K CA  
16202 C C   . ASN   K  201 ? 0.96245 0.96245 0.96245 0.00000  0.00000  0.00000  201 ASN   K C   
16203 O O   . ASN   K  201 ? 1.36825 1.36825 1.36825 0.00000  0.00000  -0.00000 201 ASN   K O   
16204 C CB  . ASN   K  201 ? 0.94033 0.94033 0.94033 0.00000  0.00000  0.00000  201 ASN   K CB  
16205 C CG  . ASN   K  201 ? 1.41481 1.41481 1.41481 0.00000  0.00000  0.00000  201 ASN   K CG  
16206 O OD1 . ASN   K  201 ? 0.82249 0.82249 0.82249 -0.00000 0.00000  0.00000  201 ASN   K OD1 
16207 N ND2 . ASN   K  201 ? 1.01098 1.01098 1.01098 0.00000  0.00000  0.00000  201 ASN   K ND2 
16208 N N   . ALA   K  202 ? 1.60439 1.60439 1.60439 0.00000  0.00000  -0.00000 202 ALA   K N   
16209 C CA  . ALA   K  202 ? 1.00274 1.00274 1.00274 0.00000  -0.00000 0.00000  202 ALA   K CA  
16210 C C   . ALA   K  202 ? 0.91701 0.91701 0.91701 0.00000  0.00000  0.00000  202 ALA   K C   
16211 O O   . ALA   K  202 ? 1.06587 1.06587 1.06587 0.00000  0.00000  0.00000  202 ALA   K O   
16212 C CB  . ALA   K  202 ? 0.71611 0.71611 0.71611 0.00000  0.00000  0.00000  202 ALA   K CB  
16213 N N   . PRO   K  203 ? 1.31219 1.31219 1.31219 0.00000  0.00000  0.00000  203 PRO   K N   
16214 C CA  . PRO   K  203 ? 1.24659 1.24659 1.24659 0.00000  0.00000  0.00000  203 PRO   K CA  
16215 C C   . PRO   K  203 ? 1.11772 1.11772 1.11772 0.00000  0.00000  -0.00000 203 PRO   K C   
16216 O O   . PRO   K  203 ? 0.86767 0.86767 0.86767 0.00000  0.00000  0.00000  203 PRO   K O   
16217 C CB  . PRO   K  203 ? 0.95887 0.95887 0.95887 -0.00000 0.00000  0.00000  203 PRO   K CB  
16218 C CG  . PRO   K  203 ? 0.84120 0.84120 0.84120 0.00000  0.00000  0.00000  203 PRO   K CG  
16219 C CD  . PRO   K  203 ? 0.69090 0.69090 0.69090 0.00000  0.00000  0.00000  203 PRO   K CD  
16220 N N   . TYR   K  204 ? 0.91325 0.91325 0.91325 0.00000  0.00000  0.00000  204 TYR   K N   
16221 C CA  . TYR   K  204 ? 1.05344 1.05344 1.05344 0.00000  0.00000  0.00000  204 TYR   K CA  
16222 C C   . TYR   K  204 ? 0.97377 0.97377 0.97377 -0.00000 0.00000  0.00000  204 TYR   K C   
16223 O O   . TYR   K  204 ? 1.02890 1.02890 1.02890 0.00000  0.00000  0.00000  204 TYR   K O   
16224 C CB  . TYR   K  204 ? 0.89394 0.89394 0.89394 0.00000  0.00000  0.00000  204 TYR   K CB  
16225 C CG  . TYR   K  204 ? 0.94809 0.94809 0.94809 -0.00000 -0.00000 0.00000  204 TYR   K CG  
16226 C CD1 . TYR   K  204 ? 0.88175 0.88175 0.88175 -0.00000 -0.00000 0.00000  204 TYR   K CD1 
16227 C CD2 . TYR   K  204 ? 0.83346 0.83346 0.83346 0.00000  0.00000  0.00000  204 TYR   K CD2 
16228 C CE1 . TYR   K  204 ? 0.66283 0.66283 0.66283 0.00000  0.00000  0.00000  204 TYR   K CE1 
16229 C CE2 . TYR   K  204 ? 0.79601 0.79601 0.79601 -0.00000 0.00000  0.00000  204 TYR   K CE2 
16230 C CZ  . TYR   K  204 ? 0.96336 0.96336 0.96336 -0.00000 0.00000  0.00000  204 TYR   K CZ  
16231 O OH  . TYR   K  204 ? 0.98881 0.98881 0.98881 0.00000  0.00000  0.00000  204 TYR   K OH  
16232 N N   . TYR   K  205 ? 0.80281 0.80281 0.80281 0.00000  0.00000  0.00000  205 TYR   K N   
16233 C CA  . TYR   K  205 ? 0.77698 0.77698 0.77698 0.00000  0.00000  0.00000  205 TYR   K CA  
16234 C C   . TYR   K  205 ? 0.87099 0.87099 0.87099 -0.00000 0.00000  0.00000  205 TYR   K C   
16235 O O   . TYR   K  205 ? 0.84545 0.84545 0.84545 0.00000  0.00000  0.00000  205 TYR   K O   
16236 C CB  . TYR   K  205 ? 0.86713 0.86713 0.86713 0.00000  0.00000  0.00000  205 TYR   K CB  
16237 C CG  . TYR   K  205 ? 1.04073 1.04073 1.04073 0.00000  0.00000  0.00000  205 TYR   K CG  
16238 C CD1 . TYR   K  205 ? 0.94259 0.94259 0.94259 0.00000  -0.00000 0.00000  205 TYR   K CD1 
16239 C CD2 . TYR   K  205 ? 0.88246 0.88246 0.88246 0.00000  0.00000  -0.00000 205 TYR   K CD2 
16240 C CE1 . TYR   K  205 ? 0.75106 0.75106 0.75106 0.00000  0.00000  0.00000  205 TYR   K CE1 
16241 C CE2 . TYR   K  205 ? 1.05503 1.05503 1.05503 -0.00000 0.00000  0.00000  205 TYR   K CE2 
16242 C CZ  . TYR   K  205 ? 1.30699 1.30699 1.30699 -0.00000 0.00000  0.00000  205 TYR   K CZ  
16243 O OH  . TYR   K  205 ? 0.93448 0.93448 0.93448 0.00000  0.00000  0.00000  205 TYR   K OH  
16244 N N   . GLY   K  206 ? 0.75859 0.75859 0.75859 0.00000  0.00000  0.00000  206 GLY   K N   
16245 C CA  . GLY   K  206 ? 0.74450 0.74450 0.74450 0.00000  -0.00000 0.00000  206 GLY   K CA  
16246 C C   . GLY   K  206 ? 0.91914 0.91914 0.91914 0.00000  0.00000  0.00000  206 GLY   K C   
16247 O O   . GLY   K  206 ? 0.81802 0.81802 0.81802 -0.00000 0.00000  0.00000  206 GLY   K O   
16248 N N   . PHE   K  207 ? 0.72740 0.72740 0.72740 0.00000  0.00000  0.00000  207 PHE   K N   
16249 C CA  . PHE   K  207 ? 0.88014 0.88014 0.88014 0.00000  0.00000  0.00000  207 PHE   K CA  
16250 C C   . PHE   K  207 ? 0.82269 0.82269 0.82269 0.00000  0.00000  0.00000  207 PHE   K C   
16251 O O   . PHE   K  207 ? 0.94987 0.94987 0.94987 0.00000  0.00000  0.00000  207 PHE   K O   
16252 C CB  . PHE   K  207 ? 0.71974 0.71974 0.71974 -0.00000 0.00000  0.00000  207 PHE   K CB  
16253 C CG  . PHE   K  207 ? 0.91793 0.91793 0.91793 0.00000  0.00000  0.00000  207 PHE   K CG  
16254 C CD1 . PHE   K  207 ? 0.58582 0.58582 0.58582 0.00000  0.00000  0.00000  207 PHE   K CD1 
16255 C CD2 . PHE   K  207 ? 0.64125 0.64125 0.64125 -0.00000 0.00000  0.00000  207 PHE   K CD2 
16256 C CE1 . PHE   K  207 ? 0.84300 0.84300 0.84300 0.00000  0.00000  0.00000  207 PHE   K CE1 
16257 C CE2 . PHE   K  207 ? 0.68754 0.68754 0.68754 0.00000  0.00000  0.00000  207 PHE   K CE2 
16258 C CZ  . PHE   K  207 ? 0.90231 0.90231 0.90231 -0.00000 0.00000  0.00000  207 PHE   K CZ  
16259 N N   . ASN   K  208 ? 0.70447 0.70447 0.70447 0.00000  0.00000  0.00000  208 ASN   K N   
16260 C CA  . ASN   K  208 ? 0.98961 0.98961 0.98961 -0.00000 0.00000  0.00000  208 ASN   K CA  
16261 C C   . ASN   K  208 ? 0.60489 0.60489 0.60489 0.00000  0.00000  0.00000  208 ASN   K C   
16262 O O   . ASN   K  208 ? 1.34168 1.34168 1.34168 0.00000  0.00000  0.00000  208 ASN   K O   
16263 C CB  . ASN   K  208 ? 0.61059 0.61059 0.61059 0.00000  0.00000  0.00000  208 ASN   K CB  
16264 C CG  . ASN   K  208 ? 1.32579 1.32579 1.32579 0.00000  0.00000  0.00000  208 ASN   K CG  
16265 O OD1 . ASN   K  208 ? 2.02299 2.02299 2.02299 -0.00000 0.00000  0.00000  208 ASN   K OD1 
16266 N ND2 . ASN   K  208 ? 1.03418 1.03418 1.03418 0.00000  0.00000  0.00000  208 ASN   K ND2 
16267 N N   . SER   K  209 ? 0.98825 0.98825 0.98825 0.00000  0.00000  0.00000  209 SER   K N   
16268 C CA  . SER   K  209 ? 0.77882 0.77882 0.77882 0.00000  0.00000  -0.00000 209 SER   K CA  
16269 C C   . SER   K  209 ? 1.05932 1.05932 1.05932 0.00000  0.00000  0.00000  209 SER   K C   
16270 O O   . SER   K  209 ? 0.74564 0.74564 0.74564 0.00000  0.00000  0.00000  209 SER   K O   
16271 C CB  . SER   K  209 ? 0.91804 0.91804 0.91804 -0.00000 0.00000  0.00000  209 SER   K CB  
16272 O OG  . SER   K  209 ? 0.65618 0.65618 0.65618 0.00000  -0.00000 0.00000  209 SER   K OG  
16273 N N   . TYR   K  210 ? 0.76083 0.76083 0.76083 0.00000  0.00000  0.00000  210 TYR   K N   
16274 C CA  . TYR   K  210 ? 0.61028 0.61028 0.61028 0.00000  0.00000  0.00000  210 TYR   K CA  
16275 C C   . TYR   K  210 ? 0.77503 0.77503 0.77503 0.00000  0.00000  0.00000  210 TYR   K C   
16276 O O   . TYR   K  210 ? 0.68570 0.68570 0.68570 0.00000  0.00000  0.00000  210 TYR   K O   
16277 C CB  . TYR   K  210 ? 0.47609 0.47609 0.47609 0.00000  0.00000  0.00000  210 TYR   K CB  
16278 C CG  . TYR   K  210 ? 0.89497 0.89497 0.89497 0.00000  0.00000  0.00000  210 TYR   K CG  
16279 C CD1 . TYR   K  210 ? 0.60396 0.60396 0.60396 0.00000  0.00000  0.00000  210 TYR   K CD1 
16280 C CD2 . TYR   K  210 ? 0.79917 0.79917 0.79917 0.00000  0.00000  0.00000  210 TYR   K CD2 
16281 C CE1 . TYR   K  210 ? 0.64984 0.64984 0.64984 0.00000  0.00000  0.00000  210 TYR   K CE1 
16282 C CE2 . TYR   K  210 ? 0.82158 0.82158 0.82158 0.00000  0.00000  0.00000  210 TYR   K CE2 
16283 C CZ  . TYR   K  210 ? 0.93551 0.93551 0.93551 -0.00000 0.00000  0.00000  210 TYR   K CZ  
16284 O OH  . TYR   K  210 ? 0.70470 0.70470 0.70470 0.00000  0.00000  0.00000  210 TYR   K OH  
16285 N N   . ASP   K  211 ? 0.74842 0.74842 0.74842 -0.00000 0.00000  0.00000  211 ASP   K N   
16286 C CA  . ASP   K  211 ? 0.68160 0.68160 0.68160 -0.00000 0.00000  0.00000  211 ASP   K CA  
16287 C C   . ASP   K  211 ? 0.95249 0.95249 0.95249 -0.00000 0.00000  0.00000  211 ASP   K C   
16288 O O   . ASP   K  211 ? 0.71036 0.71036 0.71036 0.00000  0.00000  0.00000  211 ASP   K O   
16289 C CB  . ASP   K  211 ? 0.72136 0.72136 0.72136 0.00000  0.00000  0.00000  211 ASP   K CB  
16290 C CG  . ASP   K  211 ? 0.72824 0.72824 0.72824 0.00000  0.00000  0.00000  211 ASP   K CG  
16291 O OD1 . ASP   K  211 ? 0.78842 0.78842 0.78842 0.00000  0.00000  0.00000  211 ASP   K OD1 
16292 O OD2 . ASP   K  211 ? 1.01532 1.01532 1.01532 -0.00000 0.00000  -0.00000 211 ASP   K OD2 
16293 N N   . ASP   K  212 ? 0.81336 0.81336 0.81336 0.00000  0.00000  0.00000  212 ASP   K N   
16294 C CA  . ASP   K  212 ? 0.93390 0.93390 0.93390 0.00000  0.00000  0.00000  212 ASP   K CA  
16295 C C   . ASP   K  212 ? 0.83592 0.83592 0.83592 -0.00000 0.00000  0.00000  212 ASP   K C   
16296 O O   . ASP   K  212 ? 0.84462 0.84462 0.84462 -0.00000 0.00000  0.00000  212 ASP   K O   
16297 C CB  . ASP   K  212 ? 0.95263 0.95263 0.95263 0.00000  0.00000  0.00000  212 ASP   K CB  
16298 C CG  . ASP   K  212 ? 1.05548 1.05548 1.05548 0.00000  -0.00000 0.00000  212 ASP   K CG  
16299 O OD1 . ASP   K  212 ? 1.24546 1.24546 1.24546 0.00000  0.00000  -0.00000 212 ASP   K OD1 
16300 O OD2 . ASP   K  212 ? 1.06653 1.06653 1.06653 0.00000  0.00000  0.00000  212 ASP   K OD2 
16301 N N   . PHE   K  213 ? 0.63125 0.63125 0.63125 -0.00000 0.00000  0.00000  213 PHE   K N   
16302 C CA  . PHE   K  213 ? 0.59668 0.59668 0.59668 -0.00000 0.00000  -0.00000 213 PHE   K CA  
16303 C C   . PHE   K  213 ? 1.06414 1.06414 1.06414 -0.00000 0.00000  -0.00000 213 PHE   K C   
16304 O O   . PHE   K  213 ? 0.74114 0.74114 0.74114 -0.00000 0.00000  0.00000  213 PHE   K O   
16305 C CB  . PHE   K  213 ? 0.68126 0.68126 0.68126 -0.00000 0.00000  0.00000  213 PHE   K CB  
16306 C CG  . PHE   K  213 ? 0.84210 0.84210 0.84210 0.00000  -0.00000 0.00000  213 PHE   K CG  
16307 C CD1 . PHE   K  213 ? 0.88620 0.88620 0.88620 -0.00000 0.00000  0.00000  213 PHE   K CD1 
16308 C CD2 . PHE   K  213 ? 0.69273 0.69273 0.69273 0.00000  0.00000  0.00000  213 PHE   K CD2 
16309 C CE1 . PHE   K  213 ? 1.00620 1.00620 1.00620 0.00000  0.00000  0.00000  213 PHE   K CE1 
16310 C CE2 . PHE   K  213 ? 1.04345 1.04345 1.04345 -0.00000 0.00000  0.00000  213 PHE   K CE2 
16311 C CZ  . PHE   K  213 ? 0.90987 0.90987 0.90987 -0.00000 0.00000  0.00000  213 PHE   K CZ  
16312 N N   . PHE   K  214 ? 0.61135 0.61135 0.61135 0.00000  0.00000  0.00000  214 PHE   K N   
16313 C CA  . PHE   K  214 ? 0.58973 0.58973 0.58973 -0.00000 0.00000  0.00000  214 PHE   K CA  
16314 C C   . PHE   K  214 ? 0.57460 0.57460 0.57460 -0.00000 0.00000  0.00000  214 PHE   K C   
16315 O O   . PHE   K  214 ? 0.92445 0.92445 0.92445 0.00000  0.00000  0.00000  214 PHE   K O   
16316 C CB  . PHE   K  214 ? 0.70035 0.70035 0.70035 0.00000  0.00000  0.00000  214 PHE   K CB  
16317 C CG  . PHE   K  214 ? 0.67769 0.67769 0.67769 0.00000  0.00000  0.00000  214 PHE   K CG  
16318 C CD1 . PHE   K  214 ? 0.65918 0.65918 0.65918 -0.00000 0.00000  0.00000  214 PHE   K CD1 
16319 C CD2 . PHE   K  214 ? 0.77183 0.77183 0.77183 0.00000  0.00000  -0.00000 214 PHE   K CD2 
16320 C CE1 . PHE   K  214 ? 0.61415 0.61415 0.61415 0.00000  0.00000  0.00000  214 PHE   K CE1 
16321 C CE2 . PHE   K  214 ? 0.76412 0.76412 0.76412 -0.00000 0.00000  0.00000  214 PHE   K CE2 
16322 C CZ  . PHE   K  214 ? 0.68711 0.68711 0.68711 0.00000  0.00000  0.00000  214 PHE   K CZ  
16323 N N   . ASN   K  215 ? 0.56965 0.56965 0.56965 0.00000  0.00000  0.00000  215 ASN   K N   
16324 C CA  . ASN   K  215 ? 0.66665 0.66665 0.66665 -0.00000 0.00000  0.00000  215 ASN   K CA  
16325 C C   . ASN   K  215 ? 0.79055 0.79055 0.79055 0.00000  0.00000  0.00000  215 ASN   K C   
16326 O O   . ASN   K  215 ? 0.71131 0.71131 0.71131 0.00000  0.00000  0.00000  215 ASN   K O   
16327 C CB  . ASN   K  215 ? 0.66472 0.66472 0.66472 0.00000  0.00000  0.00000  215 ASN   K CB  
16328 C CG  . ASN   K  215 ? 0.95756 0.95756 0.95756 0.00000  0.00000  0.00000  215 ASN   K CG  
16329 O OD1 . ASN   K  215 ? 0.68729 0.68729 0.68729 0.00000  0.00000  0.00000  215 ASN   K OD1 
16330 N ND2 . ASN   K  215 ? 0.64585 0.64585 0.64585 0.00000  0.00000  0.00000  215 ASN   K ND2 
16331 N N   . ARG   K  216 ? 0.68281 0.68281 0.68281 -0.00000 0.00000  0.00000  216 ARG   K N   
16332 C CA  . ARG   K  216 ? 0.79529 0.79529 0.79529 -0.00000 0.00000  0.00000  216 ARG   K CA  
16333 C C   . ARG   K  216 ? 1.08714 1.08714 1.08714 -0.00000 0.00000  0.00000  216 ARG   K C   
16334 O O   . ARG   K  216 ? 0.78551 0.78551 0.78551 -0.00000 0.00000  0.00000  216 ARG   K O   
16335 C CB  . ARG   K  216 ? 0.74821 0.74821 0.74821 0.00000  0.00000  0.00000  216 ARG   K CB  
16336 C CG  . ARG   K  216 ? 0.73924 0.73924 0.73924 -0.00000 0.00000  0.00000  216 ARG   K CG  
16337 C CD  . ARG   K  216 ? 0.86986 0.86986 0.86986 -0.00000 0.00000  0.00000  216 ARG   K CD  
16338 N NE  . ARG   K  216 ? 0.72979 0.72979 0.72979 0.00000  0.00000  0.00000  216 ARG   K NE  
16339 C CZ  . ARG   K  216 ? 1.04362 1.04362 1.04362 0.00000  0.00000  -0.00000 216 ARG   K CZ  
16340 N NH1 . ARG   K  216 ? 0.77529 0.77529 0.77529 -0.00000 0.00000  0.00000  216 ARG   K NH1 
16341 N NH2 . ARG   K  216 ? 0.83208 0.83208 0.83208 0.00000  0.00000  0.00000  216 ARG   K NH2 
16342 N N   . ARG   K  217 ? 1.65365 1.65365 1.65365 -0.00000 0.00000  0.00000  217 ARG   K N   
16343 C CA  . ARG   K  217 ? 1.14825 1.14825 1.14825 0.00000  0.00000  0.00000  217 ARG   K CA  
16344 C C   . ARG   K  217 ? 1.31643 1.31643 1.31643 0.00000  0.00000  0.00000  217 ARG   K C   
16345 O O   . ARG   K  217 ? 0.62408 0.62408 0.62408 0.00000  0.00000  0.00000  217 ARG   K O   
16346 C CB  . ARG   K  217 ? 0.74874 0.74874 0.74874 -0.00000 0.00000  0.00000  217 ARG   K CB  
16347 C CG  . ARG   K  217 ? 0.84300 0.84300 0.84300 0.00000  0.00000  0.00000  217 ARG   K CG  
16348 C CD  . ARG   K  217 ? 0.69298 0.69298 0.69298 0.00000  0.00000  0.00000  217 ARG   K CD  
16349 N NE  . ARG   K  217 ? 0.32045 0.32045 0.32045 0.00000  0.00000  0.00000  217 ARG   K NE  
16350 C CZ  . ARG   K  217 ? 1.44229 1.44229 1.44229 0.00000  0.00000  0.00000  217 ARG   K CZ  
16351 N NH1 . ARG   K  217 ? 0.93690 0.93690 0.93690 0.00000  0.00000  0.00000  217 ARG   K NH1 
16352 N NH2 . ARG   K  217 ? 0.85839 0.85839 0.85839 0.00000  0.00000  0.00000  217 ARG   K NH2 
16353 N N   . PHE   K  218 ? 1.07249 1.07249 1.07249 0.00000  0.00000  -0.00000 218 PHE   K N   
16354 C CA  . PHE   K  218 ? 0.93150 0.93150 0.93150 0.00000  0.00000  0.00000  218 PHE   K CA  
16355 C C   . PHE   K  218 ? 1.31716 1.31716 1.31716 -0.00000 0.00000  0.00000  218 PHE   K C   
16356 O O   . PHE   K  218 ? 0.95951 0.95951 0.95951 0.00000  0.00000  0.00000  218 PHE   K O   
16357 C CB  . PHE   K  218 ? 0.81563 0.81563 0.81563 0.00000  0.00000  0.00000  218 PHE   K CB  
16358 C CG  . PHE   K  218 ? 1.06457 1.06457 1.06457 -0.00000 0.00000  0.00000  218 PHE   K CG  
16359 C CD1 . PHE   K  218 ? 0.83675 0.83675 0.83675 0.00000  0.00000  0.00000  218 PHE   K CD1 
16360 C CD2 . PHE   K  218 ? 0.94644 0.94644 0.94644 0.00000  0.00000  -0.00000 218 PHE   K CD2 
16361 C CE1 . PHE   K  218 ? 1.15655 1.15655 1.15655 0.00000  0.00000  0.00000  218 PHE   K CE1 
16362 C CE2 . PHE   K  218 ? 0.93716 0.93716 0.93716 0.00000  0.00000  0.00000  218 PHE   K CE2 
16363 C CZ  . PHE   K  218 ? 0.85174 0.85174 0.85174 0.00000  0.00000  0.00000  218 PHE   K CZ  
16364 N N   . ARG   K  219 ? 1.34261 1.34261 1.34261 0.00000  0.00000  0.00000  219 ARG   K N   
16365 C CA  . ARG   K  219 ? 1.39747 1.39747 1.39747 0.00000  0.00000  0.00000  219 ARG   K CA  
16366 C C   . ARG   K  219 ? 1.35870 1.35870 1.35870 0.00000  0.00000  0.00000  219 ARG   K C   
16367 O O   . ARG   K  219 ? 1.34016 1.34016 1.34016 0.00000  0.00000  0.00000  219 ARG   K O   
16368 C CB  . ARG   K  219 ? 1.30612 1.30612 1.30612 0.00000  0.00000  0.00000  219 ARG   K CB  
16369 C CG  . ARG   K  219 ? 1.51433 1.51433 1.51433 0.00000  0.00000  0.00000  219 ARG   K CG  
16370 C CD  . ARG   K  219 ? 1.38646 1.38646 1.38646 -0.00000 0.00000  0.00000  219 ARG   K CD  
16371 N NE  . ARG   K  219 ? 1.21076 1.21076 1.21076 0.00000  0.00000  0.00000  219 ARG   K NE  
16372 C CZ  . ARG   K  219 ? 2.07081 2.07081 2.07081 -0.00000 0.00000  0.00000  219 ARG   K CZ  
16373 N NH1 . ARG   K  219 ? 1.21398 1.21398 1.21398 0.00000  0.00000  0.00000  219 ARG   K NH1 
16374 N NH2 . ARG   K  219 ? 1.11032 1.11032 1.11032 -0.00000 0.00000  0.00000  219 ARG   K NH2 
16375 N N   . ASN   K  220 ? 1.28550 1.28550 1.28550 0.00000  0.00000  0.00000  220 ASN   K N   
16376 C CA  . ASN   K  220 ? 1.36209 1.36209 1.36209 -0.00000 0.00000  0.00000  220 ASN   K CA  
16377 C C   . ASN   K  220 ? 1.32267 1.32267 1.32267 0.00000  0.00000  0.00000  220 ASN   K C   
16378 O O   . ASN   K  220 ? 1.39160 1.39160 1.39160 0.00000  0.00000  0.00000  220 ASN   K O   
16379 C CB  . ASN   K  220 ? 1.46228 1.46228 1.46228 0.00000  0.00000  0.00000  220 ASN   K CB  
16380 C CG  . ASN   K  220 ? 1.78250 1.78250 1.78250 -0.00000 -0.00000 0.00000  220 ASN   K CG  
16381 O OD1 . ASN   K  220 ? 1.46901 1.46901 1.46901 0.00000  -0.00000 0.00000  220 ASN   K OD1 
16382 N ND2 . ASN   K  220 ? 1.48528 1.48528 1.48528 -0.00000 0.00000  0.00000  220 ASN   K ND2 
16383 N N   . ARG   K  221 ? 1.08744 1.08744 1.08744 0.00000  0.00000  0.00000  221 ARG   K N   
16384 C CA  . ARG   K  221 ? 1.12977 1.12977 1.12977 0.00000  0.00000  0.00000  221 ARG   K CA  
16385 C C   . ARG   K  221 ? 1.23984 1.23984 1.23984 -0.00000 0.00000  0.00000  221 ARG   K C   
16386 O O   . ARG   K  221 ? 1.11233 1.11233 1.11233 -0.00000 0.00000  0.00000  221 ARG   K O   
16387 C CB  . ARG   K  221 ? 0.97115 0.97115 0.97115 -0.00000 0.00000  0.00000  221 ARG   K CB  
16388 C CG  . ARG   K  221 ? 0.97779 0.97779 0.97779 -0.00000 0.00000  0.00000  221 ARG   K CG  
16389 C CD  . ARG   K  221 ? 1.12597 1.12597 1.12597 0.00000  0.00000  0.00000  221 ARG   K CD  
16390 N NE  . ARG   K  221 ? 1.06303 1.06303 1.06303 0.00000  0.00000  0.00000  221 ARG   K NE  
16391 C CZ  . ARG   K  221 ? 1.20905 1.20905 1.20905 -0.00000 0.00000  0.00000  221 ARG   K CZ  
16392 N NH1 . ARG   K  221 ? 1.13776 1.13776 1.13776 0.00000  0.00000  0.00000  221 ARG   K NH1 
16393 N NH2 . ARG   K  221 ? 1.02022 1.02022 1.02022 0.00000  0.00000  0.00000  221 ARG   K NH2 
16394 N N   . ASP   K  222 ? 0.98016 0.98016 0.98016 0.00000  0.00000  0.00000  222 ASP   K N   
16395 C CA  . ASP   K  222 ? 1.19525 1.19525 1.19525 -0.00000 0.00000  0.00000  222 ASP   K CA  
16396 C C   . ASP   K  222 ? 1.22978 1.22978 1.22978 0.00000  0.00000  -0.00000 222 ASP   K C   
16397 O O   . ASP   K  222 ? 1.06288 1.06288 1.06288 -0.00000 0.00000  0.00000  222 ASP   K O   
16398 C CB  . ASP   K  222 ? 0.91057 0.91057 0.91057 0.00000  0.00000  0.00000  222 ASP   K CB  
16399 C CG  . ASP   K  222 ? 1.15111 1.15111 1.15111 0.00000  0.00000  0.00000  222 ASP   K CG  
16400 O OD1 . ASP   K  222 ? 1.23932 1.23932 1.23932 0.00000  0.00000  0.00000  222 ASP   K OD1 
16401 O OD2 . ASP   K  222 ? 1.35500 1.35500 1.35500 0.00000  0.00000  0.00000  222 ASP   K OD2 
16402 N N   . ILE   K  223 ? 1.17472 1.17472 1.17472 0.00000  0.00000  0.00000  223 ILE   K N   
16403 C CA  . ILE   K  223 ? 1.29575 1.29575 1.29575 0.00000  0.00000  0.00000  223 ILE   K CA  
16404 C C   . ILE   K  223 ? 1.43771 1.43771 1.43771 -0.00000 0.00000  0.00000  223 ILE   K C   
16405 O O   . ILE   K  223 ? 1.46971 1.46971 1.46971 -0.00000 0.00000  0.00000  223 ILE   K O   
16406 C CB  . ILE   K  223 ? 1.45570 1.45570 1.45570 0.00000  -0.00000 0.00000  223 ILE   K CB  
16407 C CG1 . ILE   K  223 ? 1.21527 1.21527 1.21527 0.00000  0.00000  0.00000  223 ILE   K CG1 
16408 C CG2 . ILE   K  223 ? 1.06061 1.06061 1.06061 0.00000  0.00000  0.00000  223 ILE   K CG2 
16409 C CD1 . ILE   K  223 ? 1.25362 1.25362 1.25362 0.00000  0.00000  0.00000  223 ILE   K CD1 
16410 N N   . ASP   K  224 ? 1.16042 1.16042 1.16042 -0.00000 0.00000  0.00000  224 ASP   K N   
16411 C CA  . ASP   K  224 ? 1.17442 1.17442 1.17442 0.00000  0.00000  0.00000  224 ASP   K CA  
16412 C C   . ASP   K  224 ? 1.18553 1.18553 1.18553 0.00000  0.00000  0.00000  224 ASP   K C   
16413 O O   . ASP   K  224 ? 1.12970 1.12970 1.12970 0.00000  0.00000  0.00000  224 ASP   K O   
16414 C CB  . ASP   K  224 ? 1.12262 1.12262 1.12262 0.00000  0.00000  0.00000  224 ASP   K CB  
16415 C CG  . ASP   K  224 ? 1.29194 1.29194 1.29194 0.00000  0.00000  0.00000  224 ASP   K CG  
16416 O OD1 . ASP   K  224 ? 1.33158 1.33158 1.33158 -0.00000 0.00000  0.00000  224 ASP   K OD1 
16417 O OD2 . ASP   K  224 ? 1.28753 1.28753 1.28753 0.00000  -0.00000 0.00000  224 ASP   K OD2 
16418 N N   . ARG   K  225 ? 1.08930 1.08930 1.08930 0.00000  0.00000  -0.00000 225 ARG   K N   
16419 C CA  . ARG   K  225 ? 0.97118 0.97118 0.97118 -0.00000 0.00000  0.00000  225 ARG   K CA  
16420 C C   . ARG   K  225 ? 1.16241 1.16241 1.16241 0.00000  -0.00000 0.00000  225 ARG   K C   
16421 O O   . ARG   K  225 ? 1.08689 1.08689 1.08689 0.00000  0.00000  0.00000  225 ARG   K O   
16422 C CB  . ARG   K  225 ? 0.98451 0.98451 0.98451 0.00000  0.00000  0.00000  225 ARG   K CB  
16423 N N   . PRO   K  226 ? 1.13780 1.13780 1.13780 0.00000  0.00000  0.00000  226 PRO   K N   
16424 C CA  . PRO   K  226 ? 0.90732 0.90732 0.90732 0.00000  0.00000  0.00000  226 PRO   K CA  
16425 C C   . PRO   K  226 ? 1.21808 1.21808 1.21808 0.00000  0.00000  0.00000  226 PRO   K C   
16426 O O   . PRO   K  226 ? 1.00570 1.00570 1.00570 0.00000  0.00000  0.00000  226 PRO   K O   
16427 C CB  . PRO   K  226 ? 0.89612 0.89612 0.89612 -0.00000 0.00000  0.00000  226 PRO   K CB  
16428 C CG  . PRO   K  226 ? 0.88063 0.88063 0.88063 -0.00000 0.00000  0.00000  226 PRO   K CG  
16429 C CD  . PRO   K  226 ? 0.92119 0.92119 0.92119 -0.00000 0.00000  0.00000  226 PRO   K CD  
16430 N N   . VAL   K  227 ? 0.95316 0.95316 0.95316 -0.00000 0.00000  0.00000  227 VAL   K N   
16431 C CA  . VAL   K  227 ? 0.91547 0.91547 0.91547 0.00000  -0.00000 0.00000  227 VAL   K CA  
16432 C C   . VAL   K  227 ? 1.07297 1.07297 1.07297 0.00000  0.00000  0.00000  227 VAL   K C   
16433 O O   . VAL   K  227 ? 1.08552 1.08552 1.08552 -0.00000 0.00000  0.00000  227 VAL   K O   
16434 C CB  . VAL   K  227 ? 0.95564 0.95564 0.95564 -0.00000 0.00000  0.00000  227 VAL   K CB  
16435 C CG1 . VAL   K  227 ? 0.97031 0.97031 0.97031 0.00000  0.00000  0.00000  227 VAL   K CG1 
16436 C CG2 . VAL   K  227 ? 0.89515 0.89515 0.89515 0.00000  0.00000  0.00000  227 VAL   K CG2 
16437 N N   . VAL   K  228 ? 1.03852 1.03852 1.03852 0.00000  0.00000  0.00000  228 VAL   K N   
16438 C CA  . VAL   K  228 ? 0.88137 0.88137 0.88137 0.00000  0.00000  0.00000  228 VAL   K CA  
16439 C C   . VAL   K  228 ? 1.39160 1.39160 1.39160 0.00000  0.00000  0.00000  228 VAL   K C   
16440 O O   . VAL   K  228 ? 1.01508 1.01508 1.01508 0.00000  0.00000  0.00000  228 VAL   K O   
16441 C CB  . VAL   K  228 ? 1.11462 1.11462 1.11462 0.00000  0.00000  -0.00000 228 VAL   K CB  
16442 C CG1 . VAL   K  228 ? 0.94231 0.94231 0.94231 0.00000  0.00000  0.00000  228 VAL   K CG1 
16443 C CG2 . VAL   K  228 ? 0.87410 0.87410 0.87410 0.00000  0.00000  0.00000  228 VAL   K CG2 
16444 N N   . GLY   K  229 ? 1.19990 1.19990 1.19990 0.00000  0.00000  0.00000  229 GLY   K N   
16445 C CA  . GLY   K  229 ? 0.99607 0.99607 0.99607 0.00000  0.00000  0.00000  229 GLY   K CA  
16446 C C   . GLY   K  229 ? 1.08494 1.08494 1.08494 -0.00000 0.00000  0.00000  229 GLY   K C   
16447 O O   . GLY   K  229 ? 1.27747 1.27747 1.27747 0.00000  -0.00000 0.00000  229 GLY   K O   
16448 N N   . GLY   K  230 ? 1.27183 1.27183 1.27183 0.00000  0.00000  0.00000  230 GLY   K N   
16449 C CA  . GLY   K  230 ? 0.90523 0.90523 0.90523 0.00000  0.00000  0.00000  230 GLY   K CA  
16450 C C   . GLY   K  230 ? 1.50752 1.50752 1.50752 -0.00000 0.00000  0.00000  230 GLY   K C   
16451 O O   . GLY   K  230 ? 1.12766 1.12766 1.12766 -0.00000 0.00000  0.00000  230 GLY   K O   
16452 N N   . VAL   K  231 ? 1.03195 1.03195 1.03195 0.00000  0.00000  0.00000  231 VAL   K N   
16453 C CA  . VAL   K  231 ? 1.54292 1.54292 1.54292 -0.00000 0.00000  0.00000  231 VAL   K CA  
16454 C C   . VAL   K  231 ? 1.03459 1.03459 1.03459 0.00000  0.00000  0.00000  231 VAL   K C   
16455 O O   . VAL   K  231 ? 1.47931 1.47931 1.47931 -0.00000 0.00000  0.00000  231 VAL   K O   
16456 C CB  . VAL   K  231 ? 0.94086 0.94086 0.94086 -0.00000 0.00000  0.00000  231 VAL   K CB  
16457 C CG1 . VAL   K  231 ? 1.63500 1.63500 1.63500 0.00000  0.00000  0.00000  231 VAL   K CG1 
16458 C CG2 . VAL   K  231 ? 1.28731 1.28731 1.28731 0.00000  0.00000  0.00000  231 VAL   K CG2 
16459 N N   . ASN   K  232 ? 1.39827 1.39827 1.39827 -0.00000 -0.00000 0.00000  232 ASN   K N   
16460 C CA  . ASN   K  232 ? 1.25866 1.25866 1.25866 -0.00000 0.00000  0.00000  232 ASN   K CA  
16461 C C   . ASN   K  232 ? 1.40663 1.40663 1.40663 -0.00000 0.00000  0.00000  232 ASN   K C   
16462 O O   . ASN   K  232 ? 1.34593 1.34593 1.34593 -0.00000 0.00000  0.00000  232 ASN   K O   
16463 C CB  . ASN   K  232 ? 1.47072 1.47072 1.47072 0.00000  0.00000  0.00000  232 ASN   K CB  
16464 C CG  . ASN   K  232 ? 1.46592 1.46592 1.46592 -0.00000 0.00000  0.00000  232 ASN   K CG  
16465 O OD1 . ASN   K  232 ? 1.47866 1.47866 1.47866 0.00000  0.00000  0.00000  232 ASN   K OD1 
16466 N ND2 . ASN   K  232 ? 2.43015 2.43015 2.43015 0.00000  0.00000  0.00000  232 ASN   K ND2 
16467 N N   . ASN   K  233 ? 1.14916 1.14916 1.14916 0.00000  0.00000  0.00000  233 ASN   K N   
16468 C CA  . ASN   K  233 ? 1.24667 1.24667 1.24667 0.00000  0.00000  0.00000  233 ASN   K CA  
16469 C C   . ASN   K  233 ? 1.91119 1.91119 1.91119 -0.00000 0.00000  0.00000  233 ASN   K C   
16470 O O   . ASN   K  233 ? 1.21815 1.21815 1.21815 0.00000  0.00000  0.00000  233 ASN   K O   
16471 C CB  . ASN   K  233 ? 0.99227 0.99227 0.99227 0.00000  0.00000  0.00000  233 ASN   K CB  
16472 C CG  . ASN   K  233 ? 1.46582 1.46582 1.46582 -0.00000 0.00000  0.00000  233 ASN   K CG  
16473 O OD1 . ASN   K  233 ? 1.37796 1.37796 1.37796 -0.00000 0.00000  0.00000  233 ASN   K OD1 
16474 N ND2 . ASN   K  233 ? 1.32333 1.32333 1.32333 0.00000  0.00000  0.00000  233 ASN   K ND2 
16475 N N   . THR   K  234 ? 1.12210 1.12210 1.12210 0.00000  0.00000  0.00000  234 THR   K N   
16476 C CA  . THR   K  234 ? 1.31631 1.31631 1.31631 0.00000  -0.00000 0.00000  234 THR   K CA  
16477 C C   . THR   K  234 ? 1.06598 1.06598 1.06598 -0.00000 0.00000  -0.00000 234 THR   K C   
16478 O O   . THR   K  234 ? 1.70554 1.70554 1.70554 0.00000  0.00000  0.00000  234 THR   K O   
16479 C CB  . THR   K  234 ? 1.13769 1.13769 1.13769 0.00000  0.00000  0.00000  234 THR   K CB  
16480 O OG1 . THR   K  234 ? 1.26667 1.26667 1.26667 -0.00000 0.00000  0.00000  234 THR   K OG1 
16481 C CG2 . THR   K  234 ? 1.01089 1.01089 1.01089 0.00000  0.00000  0.00000  234 THR   K CG2 
16482 N N   . THR   K  235 ? 1.46283 1.46283 1.46283 0.00000  0.00000  0.00000  235 THR   K N   
16483 C CA  . THR   K  235 ? 1.23752 1.23752 1.23752 -0.00000 0.00000  0.00000  235 THR   K CA  
16484 C C   . THR   K  235 ? 1.49215 1.49215 1.49215 0.00000  0.00000  0.00000  235 THR   K C   
16485 O O   . THR   K  235 ? 1.28008 1.28008 1.28008 0.00000  0.00000  0.00000  235 THR   K O   
16486 C CB  . THR   K  235 ? 1.68271 1.68271 1.68271 0.00000  0.00000  0.00000  235 THR   K CB  
16487 O OG1 . THR   K  235 ? 1.19117 1.19117 1.19117 0.00000  0.00000  0.00000  235 THR   K OG1 
16488 C CG2 . THR   K  235 ? 1.31742 1.31742 1.31742 -0.00000 0.00000  0.00000  235 THR   K CG2 
16489 N N   . LEU   K  236 ? 1.20983 1.20983 1.20983 -0.00000 -0.00000 0.00000  236 LEU   K N   
16490 C CA  . LEU   K  236 ? 1.21581 1.21581 1.21581 0.00000  0.00000  0.00000  236 LEU   K CA  
16491 C C   . LEU   K  236 ? 1.13498 1.13498 1.13498 0.00000  0.00000  0.00000  236 LEU   K C   
16492 O O   . LEU   K  236 ? 1.15674 1.15674 1.15674 0.00000  -0.00000 0.00000  236 LEU   K O   
16493 C CB  . LEU   K  236 ? 1.13382 1.13382 1.13382 0.00000  0.00000  0.00000  236 LEU   K CB  
16494 C CG  . LEU   K  236 ? 1.22618 1.22618 1.22618 0.00000  0.00000  0.00000  236 LEU   K CG  
16495 C CD1 . LEU   K  236 ? 1.12424 1.12424 1.12424 0.00000  0.00000  0.00000  236 LEU   K CD1 
16496 C CD2 . LEU   K  236 ? 1.00361 1.00361 1.00361 -0.00000 0.00000  0.00000  236 LEU   K CD2 
16497 N N   . ILE   K  237 ? 1.18320 1.18320 1.18320 -0.00000 0.00000  0.00000  237 ILE   K N   
16498 C CA  . ILE   K  237 ? 1.09867 1.09867 1.09867 -0.00000 0.00000  0.00000  237 ILE   K CA  
16499 C C   . ILE   K  237 ? 1.24099 1.24099 1.24099 -0.00000 0.00000  0.00000  237 ILE   K C   
16500 O O   . ILE   K  237 ? 1.07536 1.07536 1.07536 0.00000  0.00000  0.00000  237 ILE   K O   
16501 C CB  . ILE   K  237 ? 1.08377 1.08377 1.08377 0.00000  0.00000  0.00000  237 ILE   K CB  
16502 C CG1 . ILE   K  237 ? 1.04479 1.04479 1.04479 0.00000  0.00000  0.00000  237 ILE   K CG1 
16503 C CG2 . ILE   K  237 ? 1.05679 1.05679 1.05679 -0.00000 0.00000  0.00000  237 ILE   K CG2 
16504 C CD1 . ILE   K  237 ? 1.06879 1.06879 1.06879 0.00000  0.00000  0.00000  237 ILE   K CD1 
16505 N N   . SER   K  238 ? 0.96310 0.96310 0.96310 0.00000  0.00000  0.00000  238 SER   K N   
16506 C CA  . SER   K  238 ? 1.04883 1.04883 1.04883 -0.00000 0.00000  0.00000  238 SER   K CA  
16507 C C   . SER   K  238 ? 1.15960 1.15960 1.15960 0.00000  0.00000  0.00000  238 SER   K C   
16508 O O   . SER   K  238 ? 0.96927 0.96927 0.96927 0.00000  0.00000  0.00000  238 SER   K O   
16509 C CB  . SER   K  238 ? 1.02936 1.02936 1.02936 0.00000  0.00000  0.00000  238 SER   K CB  
16510 O OG  . SER   K  238 ? 1.20390 1.20390 1.20390 0.00000  0.00000  0.00000  238 SER   K OG  
16511 N N   . ALA   K  239 ? 0.96355 0.96355 0.96355 -0.00000 0.00000  0.00000  239 ALA   K N   
16512 C CA  . ALA   K  239 ? 1.06557 1.06557 1.06557 -0.00000 -0.00000 0.00000  239 ALA   K CA  
16513 C C   . ALA   K  239 ? 0.76414 0.76414 0.76414 0.00000  0.00000  0.00000  239 ALA   K C   
16514 O O   . ALA   K  239 ? 0.95960 0.95960 0.95960 -0.00000 0.00000  0.00000  239 ALA   K O   
16515 C CB  . ALA   K  239 ? 0.71823 0.71823 0.71823 0.00000  0.00000  0.00000  239 ALA   K CB  
16516 N N   . ALA   K  240 ? 0.83598 0.83598 0.83598 0.00000  -0.00000 0.00000  240 ALA   K N   
16517 C CA  . ALA   K  240 ? 0.75517 0.75517 0.75517 0.00000  0.00000  0.00000  240 ALA   K CA  
16518 C C   . ALA   K  240 ? 0.83711 0.83711 0.83711 0.00000  0.00000  0.00000  240 ALA   K C   
16519 O O   . ALA   K  240 ? 0.77778 0.77778 0.77778 0.00000  0.00000  0.00000  240 ALA   K O   
16520 C CB  . ALA   K  240 ? 0.65043 0.65043 0.65043 0.00000  0.00000  0.00000  240 ALA   K CB  
16521 N N   . CYS   K  241 ? 0.53448 0.53448 0.53448 0.00000  0.00000  0.00000  241 CYS   K N   
16522 C CA  . CYS   K  241 ? 0.65994 0.65994 0.65994 0.00000  0.00000  0.00000  241 CYS   K CA  
16523 C C   . CYS   K  241 ? 0.66386 0.66386 0.66386 -0.00000 0.00000  0.00000  241 CYS   K C   
16524 O O   . CYS   K  241 ? 0.65123 0.65123 0.65123 0.00000  0.00000  0.00000  241 CYS   K O   
16525 C CB  . CYS   K  241 ? 0.68068 0.68068 0.68068 0.00000  -0.00000 0.00000  241 CYS   K CB  
16526 S SG  . CYS   K  241 ? 0.68392 0.68392 0.68392 0.00000  0.00000  0.00000  241 CYS   K SG  
16527 N N   . GLU   K  242 ? 0.88149 0.88149 0.88149 0.00000  0.00000  0.00000  242 GLU   K N   
16528 C CA  . GLU   K  242 ? 0.67464 0.67464 0.67464 -0.00000 0.00000  0.00000  242 GLU   K CA  
16529 C C   . GLU   K  242 ? 0.71139 0.71139 0.71139 0.00000  -0.00000 0.00000  242 GLU   K C   
16530 O O   . GLU   K  242 ? 0.99738 0.99738 0.99738 -0.00000 0.00000  0.00000  242 GLU   K O   
16531 C CB  . GLU   K  242 ? 0.81245 0.81245 0.81245 -0.00000 0.00000  0.00000  242 GLU   K CB  
16532 C CG  . GLU   K  242 ? 0.74068 0.74068 0.74068 0.00000  0.00000  0.00000  242 GLU   K CG  
16533 C CD  . GLU   K  242 ? 1.04470 1.04470 1.04470 0.00000  0.00000  0.00000  242 GLU   K CD  
16534 O OE1 . GLU   K  242 ? 0.78476 0.78476 0.78476 0.00000  0.00000  0.00000  242 GLU   K OE1 
16535 O OE2 . GLU   K  242 ? 0.86766 0.86766 0.86766 -0.00000 0.00000  0.00000  242 GLU   K OE2 
16536 N N   . SER   K  243 ? 0.74403 0.74403 0.74403 -0.00000 0.00000  0.00000  243 SER   K N   
16537 C CA  . SER   K  243 ? 0.88946 0.88946 0.88946 0.00000  0.00000  0.00000  243 SER   K CA  
16538 C C   . SER   K  243 ? 0.76575 0.76575 0.76575 0.00000  0.00000  0.00000  243 SER   K C   
16539 O O   . SER   K  243 ? 0.82280 0.82280 0.82280 0.00000  0.00000  0.00000  243 SER   K O   
16540 C CB  . SER   K  243 ? 0.75306 0.75306 0.75306 -0.00000 0.00000  0.00000  243 SER   K CB  
16541 O OG  . SER   K  243 ? 0.84800 0.84800 0.84800 0.00000  0.00000  0.00000  243 SER   K OG  
16542 N N   . LEU   K  244 ? 0.67124 0.67124 0.67124 0.00000  0.00000  0.00000  244 LEU   K N   
16543 C CA  . LEU   K  244 ? 0.74135 0.74135 0.74135 -0.00000 0.00000  0.00000  244 LEU   K CA  
16544 C C   . LEU   K  244 ? 0.70972 0.70972 0.70972 0.00000  0.00000  0.00000  244 LEU   K C   
16545 O O   . LEU   K  244 ? 0.78928 0.78928 0.78928 0.00000  0.00000  0.00000  244 LEU   K O   
16546 C CB  . LEU   K  244 ? 0.54970 0.54970 0.54970 -0.00000 0.00000  0.00000  244 LEU   K CB  
16547 C CG  . LEU   K  244 ? 0.78322 0.78322 0.78322 -0.00000 0.00000  0.00000  244 LEU   K CG  
16548 C CD1 . LEU   K  244 ? 0.70673 0.70673 0.70673 0.00000  0.00000  0.00000  244 LEU   K CD1 
16549 C CD2 . LEU   K  244 ? 0.62096 0.62096 0.62096 -0.00000 0.00000  0.00000  244 LEU   K CD2 
16550 N N   . SER   K  245 ? 1.11514 1.11514 1.11514 0.00000  0.00000  0.00000  245 SER   K N   
16551 C CA  . SER   K  245 ? 0.61641 0.61641 0.61641 -0.00000 0.00000  0.00000  245 SER   K CA  
16552 C C   . SER   K  245 ? 0.61699 0.61699 0.61699 0.00000  0.00000  0.00000  245 SER   K C   
16553 O O   . SER   K  245 ? 0.73051 0.73051 0.73051 0.00000  0.00000  0.00000  245 SER   K O   
16554 C CB  . SER   K  245 ? 0.65112 0.65112 0.65112 0.00000  -0.00000 0.00000  245 SER   K CB  
16555 O OG  . SER   K  245 ? 1.22831 1.22831 1.22831 0.00000  -0.00000 0.00000  245 SER   K OG  
16556 N N   . TYR   K  246 ? 0.57567 0.57567 0.57567 0.00000  0.00000  0.00000  246 TYR   K N   
16557 C CA  . TYR   K  246 ? 0.45075 0.45075 0.45075 -0.00000 0.00000  0.00000  246 TYR   K CA  
16558 C C   . TYR   K  246 ? 0.47121 0.47121 0.47121 0.00000  0.00000  0.00000  246 TYR   K C   
16559 O O   . TYR   K  246 ? 0.50997 0.50997 0.50997 0.00000  0.00000  0.00000  246 TYR   K O   
16560 C CB  . TYR   K  246 ? 0.32881 0.32881 0.32881 0.00000  0.00000  0.00000  246 TYR   K CB  
16561 C CG  . TYR   K  246 ? 0.53375 0.53375 0.53375 0.00000  0.00000  0.00000  246 TYR   K CG  
16562 C CD1 . TYR   K  246 ? 0.44642 0.44642 0.44642 0.00000  0.00000  0.00000  246 TYR   K CD1 
16563 C CD2 . TYR   K  246 ? 0.27048 0.27048 0.27048 0.00000  0.00000  0.00000  246 TYR   K CD2 
16564 C CE1 . TYR   K  246 ? 0.36711 0.36711 0.36711 -0.00000 0.00000  0.00000  246 TYR   K CE1 
16565 C CE2 . TYR   K  246 ? 0.60348 0.60348 0.60348 -0.00000 0.00000  0.00000  246 TYR   K CE2 
16566 C CZ  . TYR   K  246 ? 0.48974 0.48974 0.48974 0.00000  0.00000  0.00000  246 TYR   K CZ  
16567 O OH  . TYR   K  246 ? 0.69362 0.69362 0.69362 0.00000  0.00000  0.00000  246 TYR   K OH  
16568 N N   . ASN   K  247 ? 0.42932 0.42932 0.42932 -0.00000 0.00000  0.00000  247 ASN   K N   
16569 C CA  . ASN   K  247 ? 0.33286 0.33286 0.33286 0.00000  0.00000  0.00000  247 ASN   K CA  
16570 C C   . ASN   K  247 ? 0.42247 0.42247 0.42247 0.00000  -0.00000 0.00000  247 ASN   K C   
16571 O O   . ASN   K  247 ? 0.46344 0.46344 0.46344 -0.00000 0.00000  0.00000  247 ASN   K O   
16572 C CB  . ASN   K  247 ? 0.46252 0.46252 0.46252 -0.00000 0.00000  0.00000  247 ASN   K CB  
16573 C CG  . ASN   K  247 ? 0.43275 0.43275 0.43275 0.00000  -0.00000 0.00000  247 ASN   K CG  
16574 O OD1 . ASN   K  247 ? 0.65411 0.65411 0.65411 0.00000  0.00000  0.00000  247 ASN   K OD1 
16575 N ND2 . ASN   K  247 ? 0.41301 0.41301 0.41301 0.00000  0.00000  0.00000  247 ASN   K ND2 
16576 N N   . VAL   K  248 ? 0.54255 0.54255 0.54255 0.00000  -0.00000 0.00000  248 VAL   K N   
16577 C CA  . VAL   K  248 ? 0.61590 0.61590 0.61590 -0.00000 0.00000  0.00000  248 VAL   K CA  
16578 C C   . VAL   K  248 ? 0.50869 0.50869 0.50869 0.00000  0.00000  0.00000  248 VAL   K C   
16579 O O   . VAL   K  248 ? 0.60379 0.60379 0.60379 -0.00000 0.00000  0.00000  248 VAL   K O   
16580 C CB  . VAL   K  248 ? 0.55953 0.55953 0.55953 0.00000  0.00000  0.00000  248 VAL   K CB  
16581 C CG1 . VAL   K  248 ? 0.46829 0.46829 0.46829 0.00000  0.00000  0.00000  248 VAL   K CG1 
16582 C CG2 . VAL   K  248 ? 0.53542 0.53542 0.53542 0.00000  0.00000  0.00000  248 VAL   K CG2 
16583 N N   . SER   K  249 ? 0.58243 0.58243 0.58243 -0.00000 0.00000  0.00000  249 SER   K N   
16584 C CA  . SER   K  249 ? 0.42249 0.42249 0.42249 0.00000  0.00000  0.00000  249 SER   K CA  
16585 C C   . SER   K  249 ? 0.58181 0.58181 0.58181 0.00000  0.00000  0.00000  249 SER   K C   
16586 O O   . SER   K  249 ? 0.45265 0.45265 0.45265 0.00000  0.00000  0.00000  249 SER   K O   
16587 C CB  . SER   K  249 ? 0.41728 0.41728 0.41728 -0.00000 0.00000  0.00000  249 SER   K CB  
16588 O OG  . SER   K  249 ? 0.48938 0.48938 0.48938 -0.00000 -0.00000 0.00000  249 SER   K OG  
16589 N N   . TYR   K  250 ? 0.51503 0.51503 0.51503 -0.00000 0.00000  0.00000  250 TYR   K N   
16590 C CA  . TYR   K  250 ? 0.84619 0.84619 0.84619 -0.00000 0.00000  0.00000  250 TYR   K CA  
16591 C C   . TYR   K  250 ? 0.48211 0.48211 0.48211 0.00000  0.00000  0.00000  250 TYR   K C   
16592 O O   . TYR   K  250 ? 0.59747 0.59747 0.59747 0.00000  0.00000  0.00000  250 TYR   K O   
16593 C CB  . TYR   K  250 ? 0.47491 0.47491 0.47491 -0.00000 0.00000  0.00000  250 TYR   K CB  
16594 C CG  . TYR   K  250 ? 0.67167 0.67167 0.67167 0.00000  0.00000  0.00000  250 TYR   K CG  
16595 C CD1 . TYR   K  250 ? 0.49918 0.49918 0.49918 0.00000  0.00000  0.00000  250 TYR   K CD1 
16596 C CD2 . TYR   K  250 ? 0.45001 0.45001 0.45001 0.00000  0.00000  0.00000  250 TYR   K CD2 
16597 C CE1 . TYR   K  250 ? 0.64927 0.64927 0.64927 0.00000  0.00000  0.00000  250 TYR   K CE1 
16598 C CE2 . TYR   K  250 ? 0.59038 0.59038 0.59038 0.00000  0.00000  0.00000  250 TYR   K CE2 
16599 C CZ  . TYR   K  250 ? 0.74117 0.74117 0.74117 0.00000  -0.00000 0.00000  250 TYR   K CZ  
16600 O OH  . TYR   K  250 ? 0.81107 0.81107 0.81107 -0.00000 0.00000  0.00000  250 TYR   K OH  
16601 N N   . ASP   K  251 ? 0.72588 0.72588 0.72588 0.00000  0.00000  0.00000  251 ASP   K N   
16602 C CA  . ASP   K  251 ? 0.72915 0.72915 0.72915 0.00000  0.00000  0.00000  251 ASP   K CA  
16603 C C   . ASP   K  251 ? 0.96541 0.96541 0.96541 0.00000  0.00000  0.00000  251 ASP   K C   
16604 O O   . ASP   K  251 ? 0.77374 0.77374 0.77374 0.00000  0.00000  0.00000  251 ASP   K O   
16605 C CB  . ASP   K  251 ? 0.72068 0.72068 0.72068 0.00000  0.00000  0.00000  251 ASP   K CB  
16606 C CG  . ASP   K  251 ? 1.00197 1.00197 1.00197 0.00000  0.00000  0.00000  251 ASP   K CG  
16607 O OD1 . ASP   K  251 ? 0.83015 0.83015 0.83015 0.00000  0.00000  0.00000  251 ASP   K OD1 
16608 O OD2 . ASP   K  251 ? 0.82436 0.82436 0.82436 0.00000  0.00000  0.00000  251 ASP   K OD2 
16609 N N   . VAL   K  252 ? 0.57025 0.57025 0.57025 0.00000  0.00000  0.00000  252 VAL   K N   
16610 C CA  . VAL   K  252 ? 0.59925 0.59925 0.59925 -0.00000 0.00000  0.00000  252 VAL   K CA  
16611 C C   . VAL   K  252 ? 0.61148 0.61148 0.61148 -0.00000 0.00000  0.00000  252 VAL   K C   
16612 O O   . VAL   K  252 ? 0.63243 0.63243 0.63243 0.00000  0.00000  0.00000  252 VAL   K O   
16613 C CB  . VAL   K  252 ? 0.63531 0.63531 0.63531 0.00000  0.00000  0.00000  252 VAL   K CB  
16614 C CG1 . VAL   K  252 ? 0.48327 0.48327 0.48327 0.00000  0.00000  0.00000  252 VAL   K CG1 
16615 C CG2 . VAL   K  252 ? 0.48821 0.48821 0.48821 0.00000  0.00000  0.00000  252 VAL   K CG2 
16616 N N   . GLN   K  253 ? 0.54962 0.54962 0.54962 0.00000  0.00000  0.00000  253 GLN   K N   
16617 C CA  . GLN   K  253 ? 0.62265 0.62265 0.62265 0.00000  0.00000  0.00000  253 GLN   K CA  
16618 C C   . GLN   K  253 ? 0.77282 0.77282 0.77282 -0.00000 0.00000  0.00000  253 GLN   K C   
16619 O O   . GLN   K  253 ? 0.61361 0.61361 0.61361 -0.00000 0.00000  0.00000  253 GLN   K O   
16620 C CB  . GLN   K  253 ? 0.47865 0.47865 0.47865 -0.00000 0.00000  0.00000  253 GLN   K CB  
16621 C CG  . GLN   K  253 ? 0.95456 0.95456 0.95456 -0.00000 0.00000  0.00000  253 GLN   K CG  
16622 C CD  . GLN   K  253 ? 0.84392 0.84392 0.84392 -0.00000 0.00000  0.00000  253 GLN   K CD  
16623 O OE1 . GLN   K  253 ? 0.85507 0.85507 0.85507 0.00000  -0.00000 -0.00000 253 GLN   K OE1 
16624 N NE2 . GLN   K  253 ? 0.94663 0.94663 0.94663 0.00000  0.00000  0.00000  253 GLN   K NE2 
16625 N N   . SER   K  254 ? 0.80778 0.80778 0.80778 -0.00000 0.00000  0.00000  254 SER   K N   
16626 C CA  . SER   K  254 ? 0.55378 0.55378 0.55378 -0.00000 0.00000  0.00000  254 SER   K CA  
16627 C C   . SER   K  254 ? 0.58026 0.58026 0.58026 0.00000  0.00000  0.00000  254 SER   K C   
16628 O O   . SER   K  254 ? 0.72917 0.72917 0.72917 0.00000  0.00000  0.00000  254 SER   K O   
16629 C CB  . SER   K  254 ? 0.69015 0.69015 0.69015 -0.00000 0.00000  0.00000  254 SER   K CB  
16630 O OG  . SER   K  254 ? 0.58340 0.58340 0.58340 0.00000  0.00000  0.00000  254 SER   K OG  
16631 N N   . LEU   K  255 ? 0.56183 0.56183 0.56183 -0.00000 0.00000  0.00000  255 LEU   K N   
16632 C CA  . LEU   K  255 ? 0.59174 0.59174 0.59174 0.00000  0.00000  0.00000  255 LEU   K CA  
16633 C C   . LEU   K  255 ? 0.61124 0.61124 0.61124 0.00000  0.00000  0.00000  255 LEU   K C   
16634 O O   . LEU   K  255 ? 0.62705 0.62705 0.62705 0.00000  0.00000  0.00000  255 LEU   K O   
16635 C CB  . LEU   K  255 ? 0.62617 0.62617 0.62617 -0.00000 0.00000  0.00000  255 LEU   K CB  
16636 C CG  . LEU   K  255 ? 0.64228 0.64228 0.64228 -0.00000 0.00000  0.00000  255 LEU   K CG  
16637 C CD1 . LEU   K  255 ? 0.62691 0.62691 0.62691 -0.00000 0.00000  0.00000  255 LEU   K CD1 
16638 C CD2 . LEU   K  255 ? 0.49811 0.49811 0.49811 0.00000  0.00000  0.00000  255 LEU   K CD2 
16639 N N   . ASP   K  256 ? 0.75553 0.75553 0.75553 0.00000  0.00000  0.00000  256 ASP   K N   
16640 C CA  . ASP   K  256 ? 0.57028 0.57028 0.57028 0.00000  -0.00000 0.00000  256 ASP   K CA  
16641 C C   . ASP   K  256 ? 0.85570 0.85570 0.85570 0.00000  0.00000  0.00000  256 ASP   K C   
16642 O O   . ASP   K  256 ? 0.60243 0.60243 0.60243 0.00000  0.00000  0.00000  256 ASP   K O   
16643 C CB  . ASP   K  256 ? 0.69725 0.69725 0.69725 0.00000  0.00000  0.00000  256 ASP   K CB  
16644 C CG  . ASP   K  256 ? 1.03571 1.03571 1.03571 0.00000  0.00000  0.00000  256 ASP   K CG  
16645 O OD1 . ASP   K  256 ? 0.70401 0.70401 0.70401 -0.00000 0.00000  -0.00000 256 ASP   K OD1 
16646 O OD2 . ASP   K  256 ? 0.71263 0.71263 0.71263 -0.00000 0.00000  0.00000  256 ASP   K OD2 
16647 N N   . THR   K  257 ? 0.70275 0.70275 0.70275 0.00000  0.00000  0.00000  257 THR   K N   
16648 C CA  . THR   K  257 ? 1.05979 1.05979 1.05979 0.00000  0.00000  0.00000  257 THR   K CA  
16649 C C   . THR   K  257 ? 0.63066 0.63066 0.63066 0.00000  0.00000  0.00000  257 THR   K C   
16650 O O   . THR   K  257 ? 0.90902 0.90902 0.90902 0.00000  0.00000  0.00000  257 THR   K O   
16651 C CB  . THR   K  257 ? 0.71976 0.71976 0.71976 0.00000  0.00000  0.00000  257 THR   K CB  
16652 O OG1 . THR   K  257 ? 1.00742 1.00742 1.00742 0.00000  0.00000  0.00000  257 THR   K OG1 
16653 C CG2 . THR   K  257 ? 0.86650 0.86650 0.86650 -0.00000 0.00000  0.00000  257 THR   K CG2 
16654 N N   . LEU   K  258 ? 0.75009 0.75009 0.75009 -0.00000 0.00000  0.00000  258 LEU   K N   
16655 C CA  . LEU   K  258 ? 0.56576 0.56576 0.56576 0.00000  0.00000  0.00000  258 LEU   K CA  
16656 C C   . LEU   K  258 ? 0.91072 0.91072 0.91072 -0.00000 0.00000  0.00000  258 LEU   K C   
16657 O O   . LEU   K  258 ? 0.95263 0.95263 0.95263 0.00000  0.00000  0.00000  258 LEU   K O   
16658 C CB  . LEU   K  258 ? 0.56741 0.56741 0.56741 -0.00000 0.00000  0.00000  258 LEU   K CB  
16659 C CG  . LEU   K  258 ? 0.51495 0.51495 0.51495 -0.00000 0.00000  0.00000  258 LEU   K CG  
16660 C CD1 . LEU   K  258 ? 0.60600 0.60600 0.60600 0.00000  0.00000  0.00000  258 LEU   K CD1 
16661 C CD2 . LEU   K  258 ? 0.46951 0.46951 0.46951 -0.00000 0.00000  0.00000  258 LEU   K CD2 
16662 N N   . VAL   K  259 ? 0.91706 0.91706 0.91706 -0.00000 0.00000  0.00000  259 VAL   K N   
16663 C CA  . VAL   K  259 ? 0.95933 0.95933 0.95933 -0.00000 0.00000  0.00000  259 VAL   K CA  
16664 C C   . VAL   K  259 ? 1.77178 1.77178 1.77178 -0.00000 0.00000  0.00000  259 VAL   K C   
16665 O O   . VAL   K  259 ? 0.90431 0.90431 0.90431 0.00000  0.00000  0.00000  259 VAL   K O   
16666 C CB  . VAL   K  259 ? 1.20857 1.20857 1.20857 -0.00000 0.00000  0.00000  259 VAL   K CB  
16667 C CG1 . VAL   K  259 ? 0.72892 0.72892 0.72892 0.00000  -0.00000 0.00000  259 VAL   K CG1 
16668 C CG2 . VAL   K  259 ? 1.03766 1.03766 1.03766 0.00000  0.00000  0.00000  259 VAL   K CG2 
16669 N N   . PHE   K  260 ? 1.03930 1.03930 1.03930 -0.00000 0.00000  0.00000  260 PHE   K N   
16670 C CA  . PHE   K  260 ? 1.80596 1.80596 1.80596 0.00000  0.00000  0.00000  260 PHE   K CA  
16671 C C   . PHE   K  260 ? 1.26235 1.26235 1.26235 -0.00000 0.00000  0.00000  260 PHE   K C   
16672 O O   . PHE   K  260 ? 2.22918 2.22918 2.22918 0.00000  0.00000  0.00000  260 PHE   K O   
16673 C CB  . PHE   K  260 ? 1.20537 1.20537 1.20537 0.00000  0.00000  0.00000  260 PHE   K CB  
16674 C CG  . PHE   K  260 ? 1.42985 1.42985 1.42985 0.00000  0.00000  0.00000  260 PHE   K CG  
16675 C CD1 . PHE   K  260 ? 1.14550 1.14550 1.14550 0.00000  -0.00000 0.00000  260 PHE   K CD1 
16676 C CD2 . PHE   K  260 ? 1.34333 1.34333 1.34333 0.00000  0.00000  0.00000  260 PHE   K CD2 
16677 C CE1 . PHE   K  260 ? 2.39952 2.39952 2.39952 0.00000  0.00000  0.00000  260 PHE   K CE1 
16678 C CE2 . PHE   K  260 ? 1.36286 1.36286 1.36286 0.00000  0.00000  0.00000  260 PHE   K CE2 
16679 C CZ  . PHE   K  260 ? 1.57414 1.57414 1.57414 0.00000  0.00000  0.00000  260 PHE   K CZ  
16680 N N   . LYS   K  261 ? 1.20310 1.20310 1.20310 0.00000  0.00000  0.00000  261 LYS   K N   
16681 C CA  . LYS   K  261 ? 1.32929 1.32929 1.32929 -0.00000 0.00000  0.00000  261 LYS   K CA  
16682 C C   . LYS   K  261 ? 1.26333 1.26333 1.26333 0.00000  0.00000  0.00000  261 LYS   K C   
16683 O O   . LYS   K  261 ? 0.79692 0.79692 0.79692 0.00000  0.00000  0.00000  261 LYS   K O   
16684 C CB  . LYS   K  261 ? 1.15905 1.15905 1.15905 0.00000  0.00000  0.00000  261 LYS   K CB  
16685 C CG  . LYS   K  261 ? 1.44738 1.44738 1.44738 0.00000  0.00000  0.00000  261 LYS   K CG  
16686 C CD  . LYS   K  261 ? 1.09941 1.09941 1.09941 -0.00000 0.00000  0.00000  261 LYS   K CD  
16687 C CE  . LYS   K  261 ? 1.17317 1.17317 1.17317 0.00000  0.00000  0.00000  261 LYS   K CE  
16688 N NZ  . LYS   K  261 ? 0.60091 0.60091 0.60091 0.00000  0.00000  0.00000  261 LYS   K NZ  
16689 N N   . GLY   K  262 ? 1.28744 1.28744 1.28744 0.00000  0.00000  0.00000  262 GLY   K N   
16690 C CA  . GLY   K  262 ? 0.58571 0.58571 0.58571 0.00000  0.00000  0.00000  262 GLY   K CA  
16691 C C   . GLY   K  262 ? 1.30587 1.30587 1.30587 0.00000  0.00000  0.00000  262 GLY   K C   
16692 O O   . GLY   K  262 ? 1.22132 1.22132 1.22132 -0.00000 0.00000  0.00000  262 GLY   K O   
16693 N N   . GLU   K  263 ? 0.74002 0.74002 0.74002 0.00000  0.00000  0.00000  263 GLU   K N   
16694 C CA  . GLU   K  263 ? 1.17572 1.17572 1.17572 0.00000  -0.00000 0.00000  263 GLU   K CA  
16695 C C   . GLU   K  263 ? 1.30372 1.30372 1.30372 0.00000  0.00000  0.00000  263 GLU   K C   
16696 O O   . GLU   K  263 ? 0.85830 0.85830 0.85830 0.00000  0.00000  0.00000  263 GLU   K O   
16697 C CB  . GLU   K  263 ? 0.72003 0.72003 0.72003 0.00000  0.00000  0.00000  263 GLU   K CB  
16698 C CG  . GLU   K  263 ? 1.17131 1.17131 1.17131 -0.00000 0.00000  0.00000  263 GLU   K CG  
16699 C CD  . GLU   K  263 ? 1.08581 1.08581 1.08581 0.00000  0.00000  0.00000  263 GLU   K CD  
16700 O OE1 . GLU   K  263 ? 0.71024 0.71024 0.71024 0.00000  0.00000  0.00000  263 GLU   K OE1 
16701 O OE2 . GLU   K  263 ? 0.88544 0.88544 0.88544 0.00000  0.00000  0.00000  263 GLU   K OE2 
16702 N N   . THR   K  264 ? 0.58824 0.58824 0.58824 -0.00000 0.00000  0.00000  264 THR   K N   
16703 C CA  . THR   K  264 ? 0.40497 0.40497 0.40497 0.00000  0.00000  0.00000  264 THR   K CA  
16704 C C   . THR   K  264 ? 0.59810 0.59810 0.59810 0.00000  0.00000  0.00000  264 THR   K C   
16705 O O   . THR   K  264 ? 0.48513 0.48513 0.48513 -0.00000 0.00000  0.00000  264 THR   K O   
16706 C CB  . THR   K  264 ? 0.66899 0.66899 0.66899 0.00000  0.00000  0.00000  264 THR   K CB  
16707 O OG1 . THR   K  264 ? 1.31580 1.31580 1.31580 -0.00000 0.00000  0.00000  264 THR   K OG1 
16708 C CG2 . THR   K  264 ? 0.50418 0.50418 0.50418 -0.00000 0.00000  0.00000  264 THR   K CG2 
16709 N N   . TYR   K  265 ? 0.54855 0.54855 0.54855 0.00000  0.00000  0.00000  265 TYR   K N   
16710 C CA  . TYR   K  265 ? 0.42841 0.42841 0.42841 0.00000  0.00000  0.00000  265 TYR   K CA  
16711 C C   . TYR   K  265 ? 0.48969 0.48969 0.48969 -0.00000 0.00000  0.00000  265 TYR   K C   
16712 O O   . TYR   K  265 ? 0.59126 0.59126 0.59126 -0.00000 0.00000  0.00000  265 TYR   K O   
16713 C CB  . TYR   K  265 ? 0.37869 0.37869 0.37869 -0.00000 0.00000  0.00000  265 TYR   K CB  
16714 C CG  . TYR   K  265 ? 0.61753 0.61753 0.61753 -0.00000 0.00000  0.00000  265 TYR   K CG  
16715 C CD1 . TYR   K  265 ? 0.50798 0.50798 0.50798 -0.00000 0.00000  0.00000  265 TYR   K CD1 
16716 C CD2 . TYR   K  265 ? 0.47711 0.47711 0.47711 -0.00000 0.00000  0.00000  265 TYR   K CD2 
16717 C CE1 . TYR   K  265 ? 0.60817 0.60817 0.60817 0.00000  0.00000  0.00000  265 TYR   K CE1 
16718 C CE2 . TYR   K  265 ? 0.58580 0.58580 0.58580 -0.00000 0.00000  0.00000  265 TYR   K CE2 
16719 C CZ  . TYR   K  265 ? 0.50869 0.50869 0.50869 0.00000  0.00000  0.00000  265 TYR   K CZ  
16720 O OH  . TYR   K  265 ? 0.55088 0.55088 0.55088 0.00000  0.00000  0.00000  265 TYR   K OH  
16721 N N   . SER   K  266 ? 0.56713 0.56713 0.56713 0.00000  0.00000  0.00000  266 SER   K N   
16722 C CA  . SER   K  266 ? 0.42856 0.42856 0.42856 -0.00000 0.00000  0.00000  266 SER   K CA  
16723 C C   . SER   K  266 ? 0.59964 0.59964 0.59964 0.00000  0.00000  0.00000  266 SER   K C   
16724 O O   . SER   K  266 ? 0.47985 0.47985 0.47985 0.00000  0.00000  0.00000  266 SER   K O   
16725 C CB  . SER   K  266 ? 0.45086 0.45086 0.45086 -0.00000 0.00000  0.00000  266 SER   K CB  
16726 O OG  . SER   K  266 ? 0.58448 0.58448 0.58448 0.00000  0.00000  0.00000  266 SER   K OG  
16727 N N   . LEU   K  267 ? 0.51901 0.51901 0.51901 0.00000  -0.00000 0.00000  267 LEU   K N   
16728 C CA  . LEU   K  267 ? 0.64041 0.64041 0.64041 -0.00000 0.00000  0.00000  267 LEU   K CA  
16729 C C   . LEU   K  267 ? 0.51095 0.51095 0.51095 0.00000  0.00000  0.00000  267 LEU   K C   
16730 O O   . LEU   K  267 ? 0.70849 0.70849 0.70849 0.00000  0.00000  0.00000  267 LEU   K O   
16731 C CB  . LEU   K  267 ? 0.43090 0.43090 0.43090 -0.00000 0.00000  0.00000  267 LEU   K CB  
16732 C CG  . LEU   K  267 ? 0.67914 0.67914 0.67914 0.00000  0.00000  0.00000  267 LEU   K CG  
16733 C CD1 . LEU   K  267 ? 0.57879 0.57879 0.57879 -0.00000 0.00000  0.00000  267 LEU   K CD1 
16734 C CD2 . LEU   K  267 ? 0.50642 0.50642 0.50642 -0.00000 0.00000  0.00000  267 LEU   K CD2 
16735 N N   . LYS   K  268 ? 0.77485 0.77485 0.77485 -0.00000 0.00000  0.00000  268 LYS   K N   
16736 C CA  . LYS   K  268 ? 0.50706 0.50706 0.50706 0.00000  0.00000  0.00000  268 LYS   K CA  
16737 C C   . LYS   K  268 ? 0.74684 0.74684 0.74684 0.00000  0.00000  0.00000  268 LYS   K C   
16738 O O   . LYS   K  268 ? 0.48240 0.48240 0.48240 0.00000  0.00000  0.00000  268 LYS   K O   
16739 C CB  . LYS   K  268 ? 0.58820 0.58820 0.58820 0.00000  0.00000  0.00000  268 LYS   K CB  
16740 C CG  . LYS   K  268 ? 0.75177 0.75177 0.75177 0.00000  0.00000  0.00000  268 LYS   K CG  
16741 C CD  . LYS   K  268 ? 0.67073 0.67073 0.67073 0.00000  0.00000  0.00000  268 LYS   K CD  
16742 C CE  . LYS   K  268 ? 0.83010 0.83010 0.83010 -0.00000 0.00000  0.00000  268 LYS   K CE  
16743 N NZ  . LYS   K  268 ? 0.78934 0.78934 0.78934 -0.00000 0.00000  0.00000  268 LYS   K NZ  
16744 N N   . HIS   K  269 ? 0.50007 0.50007 0.50007 -0.00000 0.00000  0.00000  269 HIS   K N   
16745 C CA  . HIS   K  269 ? 0.30379 0.30379 0.30379 0.00000  0.00000  0.00000  269 HIS   K CA  
16746 C C   . HIS   K  269 ? 0.61954 0.61954 0.61954 -0.00000 0.00000  0.00000  269 HIS   K C   
16747 O O   . HIS   K  269 ? 0.40089 0.40089 0.40089 0.00000  0.00000  0.00000  269 HIS   K O   
16748 C CB  . HIS   K  269 ? 0.40083 0.40083 0.40083 0.00000  0.00000  0.00000  269 HIS   K CB  
16749 C CG  . HIS   K  269 ? 0.45208 0.45208 0.45208 0.00000  -0.00000 -0.00000 269 HIS   K CG  
16750 N ND1 . HIS   K  269 ? 0.72266 0.72266 0.72266 0.00000  0.00000  0.00000  269 HIS   K ND1 
16751 C CD2 . HIS   K  269 ? 0.54422 0.54422 0.54422 0.00000  0.00000  0.00000  269 HIS   K CD2 
16752 C CE1 . HIS   K  269 ? 0.40885 0.40885 0.40885 -0.00000 0.00000  0.00000  269 HIS   K CE1 
16753 N NE2 . HIS   K  269 ? 0.60575 0.60575 0.60575 -0.00000 0.00000  0.00000  269 HIS   K NE2 
16754 N N   . LEU   K  270 ? 0.48054 0.48054 0.48054 0.00000  0.00000  0.00000  270 LEU   K N   
16755 C CA  . LEU   K  270 ? 0.42044 0.42044 0.42044 -0.00000 0.00000  0.00000  270 LEU   K CA  
16756 C C   . LEU   K  270 ? 0.46715 0.46715 0.46715 0.00000  0.00000  0.00000  270 LEU   K C   
16757 O O   . LEU   K  270 ? 0.51219 0.51219 0.51219 -0.00000 0.00000  0.00000  270 LEU   K O   
16758 C CB  . LEU   K  270 ? 0.50557 0.50557 0.50557 0.00000  0.00000  0.00000  270 LEU   K CB  
16759 C CG  . LEU   K  270 ? 0.46836 0.46836 0.46836 0.00000  0.00000  0.00000  270 LEU   K CG  
16760 C CD1 . LEU   K  270 ? 0.43967 0.43967 0.43967 -0.00000 -0.00000 0.00000  270 LEU   K CD1 
16761 C CD2 . LEU   K  270 ? 0.54093 0.54093 0.54093 -0.00000 0.00000  0.00000  270 LEU   K CD2 
16762 N N   . LEU   K  271 ? 0.56373 0.56373 0.56373 0.00000  0.00000  0.00000  271 LEU   K N   
16763 C CA  . LEU   K  271 ? 0.52101 0.52101 0.52101 0.00000  -0.00000 0.00000  271 LEU   K CA  
16764 C C   . LEU   K  271 ? 0.62781 0.62781 0.62781 -0.00000 0.00000  0.00000  271 LEU   K C   
16765 O O   . LEU   K  271 ? 0.49562 0.49562 0.49562 0.00000  0.00000  0.00000  271 LEU   K O   
16766 C CB  . LEU   K  271 ? 0.40022 0.40022 0.40022 -0.00000 0.00000  0.00000  271 LEU   K CB  
16767 C CG  . LEU   K  271 ? 0.56600 0.56600 0.56600 -0.00000 0.00000  0.00000  271 LEU   K CG  
16768 C CD1 . LEU   K  271 ? 0.45349 0.45349 0.45349 0.00000  0.00000  0.00000  271 LEU   K CD1 
16769 C CD2 . LEU   K  271 ? 0.37150 0.37150 0.37150 -0.00000 0.00000  0.00000  271 LEU   K CD2 
16770 N N   . ASN   K  272 ? 0.56437 0.56437 0.56437 0.00000  0.00000  0.00000  272 ASN   K N   
16771 C CA  . ASN   K  272 ? 0.46306 0.46306 0.46306 0.00000  0.00000  0.00000  272 ASN   K CA  
16772 C C   . ASN   K  272 ? 0.61677 0.61677 0.61677 0.00000  0.00000  0.00000  272 ASN   K C   
16773 O O   . ASN   K  272 ? 0.70282 0.70282 0.70282 0.00000  0.00000  0.00000  272 ASN   K O   
16774 C CB  . ASN   K  272 ? 0.74055 0.74055 0.74055 -0.00000 0.00000  0.00000  272 ASN   K CB  
16775 C CG  . ASN   K  272 ? 0.62012 0.62012 0.62012 0.00000  0.00000  0.00000  272 ASN   K CG  
16776 O OD1 . ASN   K  272 ? 0.61763 0.61763 0.61763 0.00000  0.00000  0.00000  272 ASN   K OD1 
16777 N ND2 . ASN   K  272 ? 0.69905 0.69905 0.69905 0.00000  -0.00000 0.00000  272 ASN   K ND2 
16778 N N   . ASN   K  273 ? 0.62790 0.62790 0.62790 0.00000  -0.00000 0.00000  273 ASN   K N   
16779 C CA  . ASN   K  273 ? 0.74323 0.74323 0.74323 0.00000  0.00000  0.00000  273 ASN   K CA  
16780 C C   . ASN   K  273 ? 0.59137 0.59137 0.59137 0.00000  0.00000  0.00000  273 ASN   K C   
16781 O O   . ASN   K  273 ? 0.70276 0.70276 0.70276 0.00000  0.00000  0.00000  273 ASN   K O   
16782 C CB  . ASN   K  273 ? 0.67344 0.67344 0.67344 0.00000  0.00000  0.00000  273 ASN   K CB  
16783 C CG  . ASN   K  273 ? 1.13576 1.13576 1.13576 0.00000  0.00000  0.00000  273 ASN   K CG  
16784 O OD1 . ASN   K  273 ? 1.20462 1.20462 1.20462 0.00000  0.00000  0.00000  273 ASN   K OD1 
16785 N ND2 . ASN   K  273 ? 1.16947 1.16947 1.16947 0.00000  0.00000  0.00000  273 ASN   K ND2 
16786 N N   . ASP   K  274 ? 0.82891 0.82891 0.82891 0.00000  0.00000  0.00000  274 ASP   K N   
16787 C CA  . ASP   K  274 ? 0.79369 0.79369 0.79369 0.00000  0.00000  0.00000  274 ASP   K CA  
16788 C C   . ASP   K  274 ? 0.72273 0.72273 0.72273 -0.00000 0.00000  0.00000  274 ASP   K C   
16789 O O   . ASP   K  274 ? 0.73324 0.73324 0.73324 0.00000  0.00000  0.00000  274 ASP   K O   
16790 C CB  . ASP   K  274 ? 0.75051 0.75051 0.75051 -0.00000 0.00000  0.00000  274 ASP   K CB  
16791 C CG  . ASP   K  274 ? 0.87248 0.87248 0.87248 0.00000  0.00000  0.00000  274 ASP   K CG  
16792 O OD1 . ASP   K  274 ? 0.97975 0.97975 0.97975 0.00000  0.00000  0.00000  274 ASP   K OD1 
16793 O OD2 . ASP   K  274 ? 1.15356 1.15356 1.15356 -0.00000 -0.00000 0.00000  274 ASP   K OD2 
16794 N N   . PRO   K  275 ? 0.99401 0.99401 0.99401 -0.00000 0.00000  0.00000  275 PRO   K N   
16795 C CA  . PRO   K  275 ? 0.74036 0.74036 0.74036 0.00000  0.00000  0.00000  275 PRO   K CA  
16796 C C   . PRO   K  275 ? 0.86197 0.86197 0.86197 0.00000  0.00000  0.00000  275 PRO   K C   
16797 O O   . PRO   K  275 ? 1.03061 1.03061 1.03061 0.00000  0.00000  0.00000  275 PRO   K O   
16798 C CB  . PRO   K  275 ? 0.76855 0.76855 0.76855 0.00000  0.00000  0.00000  275 PRO   K CB  
16799 C CG  . PRO   K  275 ? 0.79447 0.79447 0.79447 0.00000  0.00000  0.00000  275 PRO   K CG  
16800 C CD  . PRO   K  275 ? 0.84433 0.84433 0.84433 0.00000  0.00000  -0.00000 275 PRO   K CD  
16801 N N   . PHE   K  276 ? 0.79840 0.79840 0.79840 0.00000  0.00000  0.00000  276 PHE   K N   
16802 C CA  . PHE   K  276 ? 0.67596 0.67596 0.67596 -0.00000 0.00000  0.00000  276 PHE   K CA  
16803 C C   . PHE   K  276 ? 0.89241 0.89241 0.89241 0.00000  0.00000  0.00000  276 PHE   K C   
16804 O O   . PHE   K  276 ? 0.83996 0.83996 0.83996 0.00000  0.00000  0.00000  276 PHE   K O   
16805 C CB  . PHE   K  276 ? 0.69164 0.69164 0.69164 0.00000  0.00000  0.00000  276 PHE   K CB  
16806 C CG  . PHE   K  276 ? 0.88811 0.88811 0.88811 -0.00000 0.00000  0.00000  276 PHE   K CG  
16807 C CD1 . PHE   K  276 ? 0.79954 0.79954 0.79954 -0.00000 0.00000  0.00000  276 PHE   K CD1 
16808 C CD2 . PHE   K  276 ? 0.76238 0.76238 0.76238 0.00000  0.00000  0.00000  276 PHE   K CD2 
16809 C CE1 . PHE   K  276 ? 0.94872 0.94872 0.94872 0.00000  0.00000  0.00000  276 PHE   K CE1 
16810 C CE2 . PHE   K  276 ? 0.99702 0.99702 0.99702 -0.00000 0.00000  0.00000  276 PHE   K CE2 
16811 C CZ  . PHE   K  276 ? 0.87663 0.87663 0.87663 0.00000  0.00000  0.00000  276 PHE   K CZ  
16812 N N   . THR   K  277 ? 0.72693 0.72693 0.72693 0.00000  0.00000  0.00000  277 THR   K N   
16813 C CA  . THR   K  277 ? 0.79942 0.79942 0.79942 -0.00000 0.00000  0.00000  277 THR   K CA  
16814 C C   . THR   K  277 ? 0.69274 0.69274 0.69274 0.00000  0.00000  0.00000  277 THR   K C   
16815 O O   . THR   K  277 ? 0.76951 0.76951 0.76951 -0.00000 0.00000  0.00000  277 THR   K O   
16816 C CB  . THR   K  277 ? 0.65686 0.65686 0.65686 -0.00000 0.00000  0.00000  277 THR   K CB  
16817 O OG1 . THR   K  277 ? 0.73585 0.73585 0.73585 -0.00000 0.00000  0.00000  277 THR   K OG1 
16818 C CG2 . THR   K  277 ? 0.53015 0.53015 0.53015 -0.00000 0.00000  0.00000  277 THR   K CG2 
16819 N N   . PRO   K  278 ? 1.02603 1.02603 1.02603 0.00000  0.00000  0.00000  278 PRO   K N   
16820 C CA  . PRO   K  278 ? 0.68017 0.68017 0.68017 -0.00000 0.00000  0.00000  278 PRO   K CA  
16821 C C   . PRO   K  278 ? 0.85757 0.85757 0.85757 0.00000  0.00000  0.00000  278 PRO   K C   
16822 O O   . PRO   K  278 ? 0.71271 0.71271 0.71271 0.00000  0.00000  0.00000  278 PRO   K O   
16823 C CB  . PRO   K  278 ? 0.58816 0.58816 0.58816 0.00000  0.00000  0.00000  278 PRO   K CB  
16824 C CG  . PRO   K  278 ? 0.63597 0.63597 0.63597 0.00000  0.00000  0.00000  278 PRO   K CG  
16825 C CD  . PRO   K  278 ? 0.67283 0.67283 0.67283 0.00000  0.00000  0.00000  278 PRO   K CD  
16826 N N   . GLN   K  279 ? 0.58768 0.58768 0.58768 -0.00000 -0.00000 0.00000  279 GLN   K N   
16827 C CA  . GLN   K  279 ? 0.56000 0.56000 0.56000 0.00000  0.00000  0.00000  279 GLN   K CA  
16828 C C   . GLN   K  279 ? 0.72973 0.72973 0.72973 -0.00000 -0.00000 0.00000  279 GLN   K C   
16829 O O   . GLN   K  279 ? 0.70936 0.70936 0.70936 -0.00000 0.00000  0.00000  279 GLN   K O   
16830 C CB  . GLN   K  279 ? 0.52754 0.52754 0.52754 -0.00000 -0.00000 -0.00000 279 GLN   K CB  
16831 C CG  . GLN   K  279 ? 0.41992 0.41992 0.41992 0.00000  0.00000  0.00000  279 GLN   K CG  
16832 C CD  . GLN   K  279 ? 0.92053 0.92053 0.92053 -0.00000 0.00000  0.00000  279 GLN   K CD  
16833 O OE1 . GLN   K  279 ? 0.74107 0.74107 0.74107 -0.00000 0.00000  0.00000  279 GLN   K OE1 
16834 N NE2 . GLN   K  279 ? 0.62739 0.62739 0.62739 0.00000  0.00000  0.00000  279 GLN   K NE2 
16835 N N   . PHE   K  280 ? 0.66799 0.66799 0.66799 -0.00000 0.00000  0.00000  280 PHE   K N   
16836 C CA  . PHE   K  280 ? 0.68797 0.68797 0.68797 -0.00000 0.00000  0.00000  280 PHE   K CA  
16837 C C   . PHE   K  280 ? 0.66673 0.66673 0.66673 0.00000  0.00000  0.00000  280 PHE   K C   
16838 O O   . PHE   K  280 ? 0.70059 0.70059 0.70059 -0.00000 0.00000  0.00000  280 PHE   K O   
16839 C CB  . PHE   K  280 ? 0.45891 0.45891 0.45891 -0.00000 0.00000  0.00000  280 PHE   K CB  
16840 C CG  . PHE   K  280 ? 0.83792 0.83792 0.83792 0.00000  0.00000  0.00000  280 PHE   K CG  
16841 C CD1 . PHE   K  280 ? 0.59349 0.59349 0.59349 0.00000  -0.00000 0.00000  280 PHE   K CD1 
16842 C CD2 . PHE   K  280 ? 0.47094 0.47094 0.47094 0.00000  0.00000  0.00000  280 PHE   K CD2 
16843 C CE1 . PHE   K  280 ? 0.77988 0.77988 0.77988 0.00000  0.00000  0.00000  280 PHE   K CE1 
16844 C CE2 . PHE   K  280 ? 0.77116 0.77116 0.77116 -0.00000 0.00000  0.00000  280 PHE   K CE2 
16845 C CZ  . PHE   K  280 ? 0.67458 0.67458 0.67458 0.00000  0.00000  0.00000  280 PHE   K CZ  
16846 N N   . GLU   K  281 ? 0.62985 0.62985 0.62985 0.00000  0.00000  0.00000  281 GLU   K N   
16847 C CA  . GLU   K  281 ? 0.79252 0.79252 0.79252 -0.00000 0.00000  0.00000  281 GLU   K CA  
16848 C C   . GLU   K  281 ? 0.50436 0.50436 0.50436 -0.00000 0.00000  0.00000  281 GLU   K C   
16849 O O   . GLU   K  281 ? 0.75383 0.75383 0.75383 0.00000  -0.00000 0.00000  281 GLU   K O   
16850 C CB  . GLU   K  281 ? 0.54575 0.54575 0.54575 0.00000  0.00000  0.00000  281 GLU   K CB  
16851 C CG  . GLU   K  281 ? 0.95075 0.95075 0.95075 0.00000  0.00000  0.00000  281 GLU   K CG  
16852 C CD  . GLU   K  281 ? 1.81460 1.81460 1.81460 0.00000  0.00000  0.00000  281 GLU   K CD  
16853 O OE1 . GLU   K  281 ? 0.79056 0.79056 0.79056 0.00000  0.00000  0.00000  281 GLU   K OE1 
16854 O OE2 . GLU   K  281 ? 0.99287 0.99287 0.99287 0.00000  0.00000  0.00000  281 GLU   K OE2 
16855 N N   . HIS   K  282 ? 0.73076 0.73076 0.73076 0.00000  0.00000  0.00000  282 HIS   K N   
16856 C CA  . HIS   K  282 ? 1.02947 1.02947 1.02947 -0.00000 0.00000  0.00000  282 HIS   K CA  
16857 C C   . HIS   K  282 ? 0.87219 0.87219 0.87219 0.00000  0.00000  0.00000  282 HIS   K C   
16858 O O   . HIS   K  282 ? 0.93838 0.93838 0.93838 0.00000  0.00000  0.00000  282 HIS   K O   
16859 C CB  . HIS   K  282 ? 0.61795 0.61795 0.61795 0.00000  0.00000  0.00000  282 HIS   K CB  
16860 C CG  . HIS   K  282 ? 1.20991 1.20991 1.20991 -0.00000 0.00000  0.00000  282 HIS   K CG  
16861 N ND1 . HIS   K  282 ? 1.01627 1.01627 1.01627 -0.00000 0.00000  0.00000  282 HIS   K ND1 
16862 C CD2 . HIS   K  282 ? 0.70670 0.70670 0.70670 0.00000  0.00000  0.00000  282 HIS   K CD2 
16863 C CE1 . HIS   K  282 ? 0.81234 0.81234 0.81234 0.00000  0.00000  0.00000  282 HIS   K CE1 
16864 N NE2 . HIS   K  282 ? 0.96380 0.96380 0.96380 0.00000  0.00000  0.00000  282 HIS   K NE2 
16865 N N   . GLY   K  283 ? 0.70936 0.70936 0.70936 -0.00000 -0.00000 0.00000  283 GLY   K N   
16866 C CA  . GLY   K  283 ? 0.45046 0.45046 0.45046 0.00000  0.00000  0.00000  283 GLY   K CA  
16867 C C   . GLY   K  283 ? 0.60466 0.60466 0.60466 0.00000  0.00000  0.00000  283 GLY   K C   
16868 O O   . GLY   K  283 ? 0.59253 0.59253 0.59253 0.00000  0.00000  0.00000  283 GLY   K O   
16869 N N   . SER   K  284 ? 0.58611 0.58611 0.58611 -0.00000 0.00000  0.00000  284 SER   K N   
16870 C CA  . SER   K  284 ? 0.69637 0.69637 0.69637 0.00000  0.00000  0.00000  284 SER   K CA  
16871 C C   . SER   K  284 ? 0.62047 0.62047 0.62047 0.00000  0.00000  0.00000  284 SER   K C   
16872 O O   . SER   K  284 ? 0.53100 0.53100 0.53100 0.00000  0.00000  0.00000  284 SER   K O   
16873 C CB  . SER   K  284 ? 0.48164 0.48164 0.48164 -0.00000 0.00000  0.00000  284 SER   K CB  
16874 O OG  . SER   K  284 ? 0.71874 0.71874 0.71874 0.00000  0.00000  0.00000  284 SER   K OG  
16875 N N   . ILE   K  285 ? 0.49924 0.49924 0.49924 0.00000  0.00000  0.00000  285 ILE   K N   
16876 C CA  . ILE   K  285 ? 0.48331 0.48331 0.48331 -0.00000 0.00000  0.00000  285 ILE   K CA  
16877 C C   . ILE   K  285 ? 0.43464 0.43464 0.43464 -0.00000 0.00000  0.00000  285 ILE   K C   
16878 O O   . ILE   K  285 ? 0.67522 0.67522 0.67522 0.00000  0.00000  0.00000  285 ILE   K O   
16879 C CB  . ILE   K  285 ? 0.52643 0.52643 0.52643 -0.00000 -0.00000 0.00000  285 ILE   K CB  
16880 C CG1 . ILE   K  285 ? 0.48197 0.48197 0.48197 0.00000  0.00000  0.00000  285 ILE   K CG1 
16881 C CG2 . ILE   K  285 ? 0.43058 0.43058 0.43058 0.00000  0.00000  0.00000  285 ILE   K CG2 
16882 C CD1 . ILE   K  285 ? 0.58695 0.58695 0.58695 -0.00000 0.00000  0.00000  285 ILE   K CD1 
16883 N N   . LEU   K  286 ? 0.67329 0.67329 0.67329 0.00000  -0.00000 0.00000  286 LEU   K N   
16884 C CA  . LEU   K  286 ? 0.45632 0.45632 0.45632 0.00000  0.00000  0.00000  286 LEU   K CA  
16885 C C   . LEU   K  286 ? 0.54371 0.54371 0.54371 0.00000  0.00000  0.00000  286 LEU   K C   
16886 O O   . LEU   K  286 ? 0.60342 0.60342 0.60342 -0.00000 0.00000  0.00000  286 LEU   K O   
16887 C CB  . LEU   K  286 ? 0.64866 0.64866 0.64866 0.00000  0.00000  0.00000  286 LEU   K CB  
16888 C CG  . LEU   K  286 ? 0.59372 0.59372 0.59372 0.00000  0.00000  0.00000  286 LEU   K CG  
16889 C CD1 . LEU   K  286 ? 0.52989 0.52989 0.52989 -0.00000 0.00000  0.00000  286 LEU   K CD1 
16890 C CD2 . LEU   K  286 ? 0.59622 0.59622 0.59622 0.00000  0.00000  0.00000  286 LEU   K CD2 
16891 N N   . GLN   K  287 ? 0.39578 0.39578 0.39578 0.00000  0.00000  0.00000  287 GLN   K N   
16892 C CA  . GLN   K  287 ? 0.57388 0.57388 0.57388 -0.00000 0.00000  0.00000  287 GLN   K CA  
16893 C C   . GLN   K  287 ? 0.58249 0.58249 0.58249 0.00000  0.00000  0.00000  287 GLN   K C   
16894 O O   . GLN   K  287 ? 0.50102 0.50102 0.50102 -0.00000 0.00000  0.00000  287 GLN   K O   
16895 C CB  . GLN   K  287 ? 0.43512 0.43512 0.43512 0.00000  0.00000  0.00000  287 GLN   K CB  
16896 C CG  . GLN   K  287 ? 0.53529 0.53529 0.53529 0.00000  0.00000  0.00000  287 GLN   K CG  
16897 C CD  . GLN   K  287 ? 0.50059 0.50059 0.50059 0.00000  0.00000  0.00000  287 GLN   K CD  
16898 O OE1 . GLN   K  287 ? 0.52768 0.52768 0.52768 0.00000  0.00000  0.00000  287 GLN   K OE1 
16899 N NE2 . GLN   K  287 ? 0.45140 0.45140 0.45140 0.00000  0.00000  0.00000  287 GLN   K NE2 
16900 N N   . GLY   K  288 ? 0.48760 0.48760 0.48760 -0.00000 0.00000  0.00000  288 GLY   K N   
16901 C CA  . GLY   K  288 ? 0.38412 0.38412 0.38412 0.00000  0.00000  0.00000  288 GLY   K CA  
16902 C C   . GLY   K  288 ? 0.44261 0.44261 0.44261 -0.00000 0.00000  0.00000  288 GLY   K C   
16903 O O   . GLY   K  288 ? 0.63305 0.63305 0.63305 -0.00000 0.00000  0.00000  288 GLY   K O   
16904 N N   . PHE   K  289 ? 0.49419 0.49419 0.49419 0.00000  0.00000  0.00000  289 PHE   K N   
16905 C CA  . PHE   K  289 ? 0.57718 0.57718 0.57718 0.00000  0.00000  0.00000  289 PHE   K CA  
16906 C C   . PHE   K  289 ? 0.51766 0.51766 0.51766 0.00000  0.00000  0.00000  289 PHE   K C   
16907 O O   . PHE   K  289 ? 0.54797 0.54797 0.54797 0.00000  0.00000  0.00000  289 PHE   K O   
16908 C CB  . PHE   K  289 ? 0.43838 0.43838 0.43838 0.00000  0.00000  0.00000  289 PHE   K CB  
16909 C CG  . PHE   K  289 ? 0.51037 0.51037 0.51037 -0.00000 0.00000  0.00000  289 PHE   K CG  
16910 C CD1 . PHE   K  289 ? 0.36835 0.36835 0.36835 0.00000  -0.00000 0.00000  289 PHE   K CD1 
16911 C CD2 . PHE   K  289 ? 0.50328 0.50328 0.50328 -0.00000 0.00000  0.00000  289 PHE   K CD2 
16912 C CE1 . PHE   K  289 ? 0.60446 0.60446 0.60446 0.00000  0.00000  0.00000  289 PHE   K CE1 
16913 C CE2 . PHE   K  289 ? 0.54578 0.54578 0.54578 -0.00000 -0.00000 0.00000  289 PHE   K CE2 
16914 C CZ  . PHE   K  289 ? 0.52424 0.52424 0.52424 -0.00000 0.00000  0.00000  289 PHE   K CZ  
16915 N N   . LEU   K  290 ? 0.58401 0.58401 0.58401 0.00000  0.00000  0.00000  290 LEU   K N   
16916 C CA  . LEU   K  290 ? 0.57603 0.57603 0.57603 -0.00000 0.00000  0.00000  290 LEU   K CA  
16917 C C   . LEU   K  290 ? 0.63136 0.63136 0.63136 -0.00000 0.00000  0.00000  290 LEU   K C   
16918 O O   . LEU   K  290 ? 0.87992 0.87992 0.87992 0.00000  0.00000  0.00000  290 LEU   K O   
16919 C CB  . LEU   K  290 ? 0.48912 0.48912 0.48912 0.00000  0.00000  0.00000  290 LEU   K CB  
16920 C CG  . LEU   K  290 ? 0.58732 0.58732 0.58732 0.00000  0.00000  0.00000  290 LEU   K CG  
16921 C CD1 . LEU   K  290 ? 0.55752 0.55752 0.55752 0.00000  0.00000  0.00000  290 LEU   K CD1 
16922 C CD2 . LEU   K  290 ? 0.48688 0.48688 0.48688 0.00000  0.00000  0.00000  290 LEU   K CD2 
16923 N N   . ASN   K  291 ? 0.82016 0.82016 0.82016 0.00000  0.00000  0.00000  291 ASN   K N   
16924 C CA  . ASN   K  291 ? 0.66085 0.66085 0.66085 0.00000  0.00000  0.00000  291 ASN   K CA  
16925 C C   . ASN   K  291 ? 0.71810 0.71810 0.71810 -0.00000 0.00000  0.00000  291 ASN   K C   
16926 O O   . ASN   K  291 ? 0.71326 0.71326 0.71326 -0.00000 0.00000  0.00000  291 ASN   K O   
16927 C CB  . ASN   K  291 ? 1.00355 1.00355 1.00355 0.00000  0.00000  0.00000  291 ASN   K CB  
16928 C CG  . ASN   K  291 ? 1.14248 1.14248 1.14248 0.00000  0.00000  0.00000  291 ASN   K CG  
16929 O OD1 . ASN   K  291 ? 1.72258 1.72258 1.72258 -0.00000 0.00000  0.00000  291 ASN   K OD1 
16930 N ND2 . ASN   K  291 ? 1.15154 1.15154 1.15154 -0.00000 0.00000  0.00000  291 ASN   K ND2 
16931 N N   . VAL   K  292 ? 0.64480 0.64480 0.64480 0.00000  0.00000  0.00000  292 VAL   K N   
16932 C CA  . VAL   K  292 ? 0.99907 0.99907 0.99907 0.00000  0.00000  0.00000  292 VAL   K CA  
16933 C C   . VAL   K  292 ? 1.00845 1.00845 1.00845 0.00000  0.00000  0.00000  292 VAL   K C   
16934 O O   . VAL   K  292 ? 0.78523 0.78523 0.78523 -0.00000 0.00000  0.00000  292 VAL   K O   
16935 C CB  . VAL   K  292 ? 0.97779 0.97779 0.97779 -0.00000 0.00000  0.00000  292 VAL   K CB  
16936 C CG1 . VAL   K  292 ? 0.88734 0.88734 0.88734 0.00000  0.00000  0.00000  292 VAL   K CG1 
16937 C CG2 . VAL   K  292 ? 0.78500 0.78500 0.78500 -0.00000 0.00000  -0.00000 292 VAL   K CG2 
16938 N N   . THR   K  293 ? 0.70232 0.70232 0.70232 0.00000  0.00000  -0.00000 293 THR   K N   
16939 C CA  . THR   K  293 ? 0.78324 0.78324 0.78324 0.00000  0.00000  0.00000  293 THR   K CA  
16940 C C   . THR   K  293 ? 1.12852 1.12852 1.12852 0.00000  0.00000  0.00000  293 THR   K C   
16941 O O   . THR   K  293 ? 0.96703 0.96703 0.96703 0.00000  0.00000  0.00000  293 THR   K O   
16942 C CB  . THR   K  293 ? 1.09444 1.09444 1.09444 0.00000  0.00000  0.00000  293 THR   K CB  
16943 O OG1 . THR   K  293 ? 0.81611 0.81611 0.81611 0.00000  0.00000  0.00000  293 THR   K OG1 
16944 C CG2 . THR   K  293 ? 0.69799 0.69799 0.69799 -0.00000 0.00000  0.00000  293 THR   K CG2 
16945 N N   . ALA   K  294 ? 0.84379 0.84379 0.84379 -0.00000 0.00000  0.00000  294 ALA   K N   
16946 C CA  . ALA   K  294 ? 0.75965 0.75965 0.75965 0.00000  0.00000  0.00000  294 ALA   K CA  
16947 C C   . ALA   K  294 ? 0.75267 0.75267 0.75267 0.00000  0.00000  0.00000  294 ALA   K C   
16948 O O   . ALA   K  294 ? 0.97399 0.97399 0.97399 -0.00000 0.00000  0.00000  294 ALA   K O   
16949 C CB  . ALA   K  294 ? 0.73873 0.73873 0.73873 0.00000  0.00000  0.00000  294 ALA   K CB  
16950 N N   . TYR   K  295 ? 0.77656 0.77656 0.77656 0.00000  0.00000  0.00000  295 TYR   K N   
16951 C CA  . TYR   K  295 ? 0.87087 0.87087 0.87087 0.00000  0.00000  0.00000  295 TYR   K CA  
16952 C C   . TYR   K  295 ? 0.84461 0.84461 0.84461 -0.00000 -0.00000 0.00000  295 TYR   K C   
16953 O O   . TYR   K  295 ? 0.80567 0.80567 0.80567 0.00000  0.00000  0.00000  295 TYR   K O   
16954 C CB  . TYR   K  295 ? 0.53158 0.53158 0.53158 0.00000  0.00000  0.00000  295 TYR   K CB  
16955 C CG  . TYR   K  295 ? 0.90893 0.90893 0.90893 -0.00000 -0.00000 0.00000  295 TYR   K CG  
16956 C CD1 . TYR   K  295 ? 0.76017 0.76017 0.76017 -0.00000 0.00000  0.00000  295 TYR   K CD1 
16957 C CD2 . TYR   K  295 ? 0.70778 0.70778 0.70778 0.00000  0.00000  0.00000  295 TYR   K CD2 
16958 C CE1 . TYR   K  295 ? 0.67022 0.67022 0.67022 -0.00000 0.00000  0.00000  295 TYR   K CE1 
16959 C CE2 . TYR   K  295 ? 0.64518 0.64518 0.64518 0.00000  -0.00000 0.00000  295 TYR   K CE2 
16960 C CZ  . TYR   K  295 ? 0.82614 0.82614 0.82614 0.00000  0.00000  0.00000  295 TYR   K CZ  
16961 O OH  . TYR   K  295 ? 0.71224 0.71224 0.71224 0.00000  0.00000  0.00000  295 TYR   K OH  
16962 N N   . HIS   K  296 ? 0.73843 0.73843 0.73843 -0.00000 0.00000  0.00000  296 HIS   K N   
16963 C CA  . HIS   K  296 ? 0.84265 0.84265 0.84265 0.00000  0.00000  0.00000  296 HIS   K CA  
16964 C C   . HIS   K  296 ? 0.64746 0.64746 0.64746 0.00000  0.00000  0.00000  296 HIS   K C   
16965 O O   . HIS   K  296 ? 0.72219 0.72219 0.72219 0.00000  0.00000  0.00000  296 HIS   K O   
16966 C CB  . HIS   K  296 ? 0.70317 0.70317 0.70317 -0.00000 0.00000  0.00000  296 HIS   K CB  
16967 C CG  . HIS   K  296 ? 0.82847 0.82847 0.82847 0.00000  0.00000  0.00000  296 HIS   K CG  
16968 N ND1 . HIS   K  296 ? 0.92746 0.92746 0.92746 0.00000  0.00000  0.00000  296 HIS   K ND1 
16969 C CD2 . HIS   K  296 ? 0.82146 0.82146 0.82146 0.00000  0.00000  0.00000  296 HIS   K CD2 
16970 C CE1 . HIS   K  296 ? 0.82655 0.82655 0.82655 -0.00000 0.00000  0.00000  296 HIS   K CE1 
16971 N NE2 . HIS   K  296 ? 1.00268 1.00268 1.00268 0.00000  0.00000  0.00000  296 HIS   K NE2 
16972 N N   . ARG   K  297 ? 0.73737 0.73737 0.73737 -0.00000 0.00000  0.00000  297 ARG   K N   
16973 C CA  . ARG   K  297 ? 0.67943 0.67943 0.67943 0.00000  0.00000  0.00000  297 ARG   K CA  
16974 C C   . ARG   K  297 ? 0.89445 0.89445 0.89445 -0.00000 0.00000  0.00000  297 ARG   K C   
16975 O O   . ARG   K  297 ? 0.76332 0.76332 0.76332 0.00000  0.00000  0.00000  297 ARG   K O   
16976 C CB  . ARG   K  297 ? 0.72859 0.72859 0.72859 0.00000  0.00000  0.00000  297 ARG   K CB  
16977 C CG  . ARG   K  297 ? 0.79216 0.79216 0.79216 0.00000  0.00000  0.00000  297 ARG   K CG  
16978 C CD  . ARG   K  297 ? 0.75244 0.75244 0.75244 0.00000  0.00000  0.00000  297 ARG   K CD  
16979 N NE  . ARG   K  297 ? 0.97416 0.97416 0.97416 0.00000  0.00000  0.00000  297 ARG   K NE  
16980 C CZ  . ARG   K  297 ? 0.87690 0.87690 0.87690 0.00000  0.00000  0.00000  297 ARG   K CZ  
16981 N NH1 . ARG   K  297 ? 0.98297 0.98297 0.98297 -0.00000 0.00000  0.00000  297 ARG   K NH1 
16982 N NH2 . ARG   K  297 ? 1.43008 1.43008 1.43008 0.00000  0.00000  -0.00000 297 ARG   K NH2 
16983 N N   . TRP   K  298 ? 0.69000 0.69000 0.69000 0.00000  0.00000  0.00000  298 TRP   K N   
16984 C CA  . TRP   K  298 ? 0.66275 0.66275 0.66275 -0.00000 0.00000  0.00000  298 TRP   K CA  
16985 C C   . TRP   K  298 ? 0.76305 0.76305 0.76305 0.00000  0.00000  0.00000  298 TRP   K C   
16986 O O   . TRP   K  298 ? 0.81419 0.81419 0.81419 0.00000  0.00000  0.00000  298 TRP   K O   
16987 C CB  . TRP   K  298 ? 0.58902 0.58902 0.58902 -0.00000 0.00000  0.00000  298 TRP   K CB  
16988 C CG  . TRP   K  298 ? 0.72494 0.72494 0.72494 0.00000  0.00000  0.00000  298 TRP   K CG  
16989 C CD1 . TRP   K  298 ? 0.66504 0.66504 0.66504 0.00000  0.00000  0.00000  298 TRP   K CD1 
16990 C CD2 . TRP   K  298 ? 0.59047 0.59047 0.59047 0.00000  0.00000  0.00000  298 TRP   K CD2 
16991 N NE1 . TRP   K  298 ? 0.55623 0.55623 0.55623 0.00000  0.00000  0.00000  298 TRP   K NE1 
16992 C CE2 . TRP   K  298 ? 0.63600 0.63600 0.63600 0.00000  0.00000  0.00000  298 TRP   K CE2 
16993 C CE3 . TRP   K  298 ? 0.50261 0.50261 0.50261 -0.00000 0.00000  0.00000  298 TRP   K CE3 
16994 C CZ2 . TRP   K  298 ? 0.70091 0.70091 0.70091 0.00000  0.00000  0.00000  298 TRP   K CZ2 
16995 C CZ3 . TRP   K  298 ? 0.78002 0.78002 0.78002 0.00000  -0.00000 0.00000  298 TRP   K CZ3 
16996 C CH2 . TRP   K  298 ? 0.67307 0.67307 0.67307 -0.00000 0.00000  0.00000  298 TRP   K CH2 
16997 N N   . HIS   K  299 ? 0.84763 0.84763 0.84763 0.00000  0.00000  0.00000  299 HIS   K N   
16998 C CA  . HIS   K  299 ? 0.96008 0.96008 0.96008 -0.00000 0.00000  0.00000  299 HIS   K CA  
16999 C C   . HIS   K  299 ? 0.83539 0.83539 0.83539 0.00000  0.00000  0.00000  299 HIS   K C   
17000 O O   . HIS   K  299 ? 0.86190 0.86190 0.86190 -0.00000 0.00000  0.00000  299 HIS   K O   
17001 C CB  . HIS   K  299 ? 0.69832 0.69832 0.69832 0.00000  0.00000  -0.00000 299 HIS   K CB  
17002 C CG  . HIS   K  299 ? 0.91259 0.91259 0.91259 -0.00000 0.00000  0.00000  299 HIS   K CG  
17003 N ND1 . HIS   K  299 ? 0.82450 0.82450 0.82450 0.00000  0.00000  0.00000  299 HIS   K ND1 
17004 C CD2 . HIS   K  299 ? 0.82833 0.82833 0.82833 -0.00000 0.00000  0.00000  299 HIS   K CD2 
17005 C CE1 . HIS   K  299 ? 0.99840 0.99840 0.99840 0.00000  0.00000  0.00000  299 HIS   K CE1 
17006 N NE2 . HIS   K  299 ? 0.85099 0.85099 0.85099 0.00000  0.00000  0.00000  299 HIS   K NE2 
17007 N N   . ALA   K  300 ? 0.85866 0.85866 0.85866 -0.00000 0.00000  0.00000  300 ALA   K N   
17008 C CA  . ALA   K  300 ? 0.92243 0.92243 0.92243 0.00000  0.00000  0.00000  300 ALA   K CA  
17009 C C   . ALA   K  300 ? 0.83358 0.83358 0.83358 0.00000  0.00000  0.00000  300 ALA   K C   
17010 O O   . ALA   K  300 ? 0.96277 0.96277 0.96277 0.00000  0.00000  0.00000  300 ALA   K O   
17011 C CB  . ALA   K  300 ? 0.77728 0.77728 0.77728 0.00000  0.00000  0.00000  300 ALA   K CB  
17012 N N   . PRO   K  301 ? 1.08874 1.08874 1.08874 -0.00000 0.00000  0.00000  301 PRO   K N   
17013 C CA  . PRO   K  301 ? 0.90941 0.90941 0.90941 0.00000  0.00000  0.00000  301 PRO   K CA  
17014 C C   . PRO   K  301 ? 1.17268 1.17268 1.17268 0.00000  0.00000  0.00000  301 PRO   K C   
17015 O O   . PRO   K  301 ? 0.97509 0.97509 0.97509 0.00000  0.00000  0.00000  301 PRO   K O   
17016 C CB  . PRO   K  301 ? 1.02211 1.02211 1.02211 0.00000  0.00000  0.00000  301 PRO   K CB  
17017 C CG  . PRO   K  301 ? 0.98727 0.98727 0.98727 0.00000  0.00000  0.00000  301 PRO   K CG  
17018 C CD  . PRO   K  301 ? 0.80122 0.80122 0.80122 0.00000  0.00000  0.00000  301 PRO   K CD  
17019 N N   . VAL   K  302 ? 0.97558 0.97558 0.97558 -0.00000 0.00000  0.00000  302 VAL   K N   
17020 C CA  . VAL   K  302 ? 1.29009 1.29009 1.29009 0.00000  0.00000  0.00000  302 VAL   K CA  
17021 C C   . VAL   K  302 ? 0.96602 0.96602 0.96602 0.00000  0.00000  0.00000  302 VAL   K C   
17022 O O   . VAL   K  302 ? 1.17718 1.17718 1.17718 0.00000  0.00000  0.00000  302 VAL   K O   
17023 C CB  . VAL   K  302 ? 0.96295 0.96295 0.96295 -0.00000 0.00000  0.00000  302 VAL   K CB  
17024 C CG1 . VAL   K  302 ? 1.27030 1.27030 1.27030 -0.00000 0.00000  0.00000  302 VAL   K CG1 
17025 C CG2 . VAL   K  302 ? 0.94633 0.94633 0.94633 0.00000  0.00000  0.00000  302 VAL   K CG2 
17026 N N   . ASN   K  303 ? 1.14281 1.14281 1.14281 -0.00000 0.00000  0.00000  303 ASN   K N   
17027 C CA  . ASN   K  303 ? 0.95121 0.95121 0.95121 -0.00000 0.00000  0.00000  303 ASN   K CA  
17028 C C   . ASN   K  303 ? 1.19568 1.19568 1.19568 0.00000  0.00000  0.00000  303 ASN   K C   
17029 O O   . ASN   K  303 ? 1.13872 1.13872 1.13872 0.00000  -0.00000 0.00000  303 ASN   K O   
17030 C CB  . ASN   K  303 ? 1.18966 1.18966 1.18966 -0.00000 0.00000  0.00000  303 ASN   K CB  
17031 C CG  . ASN   K  303 ? 1.09770 1.09770 1.09770 -0.00000 0.00000  0.00000  303 ASN   K CG  
17032 O OD1 . ASN   K  303 ? 1.15732 1.15732 1.15732 -0.00000 0.00000  0.00000  303 ASN   K OD1 
17033 N ND2 . ASN   K  303 ? 1.13266 1.13266 1.13266 0.00000  0.00000  0.00000  303 ASN   K ND2 
17034 N N   . GLY   K  304 ? 0.95262 0.95262 0.95262 -0.00000 0.00000  0.00000  304 GLY   K N   
17035 C CA  . GLY   K  304 ? 0.78509 0.78509 0.78509 0.00000  0.00000  0.00000  304 GLY   K CA  
17036 C C   . GLY   K  304 ? 0.99440 0.99440 0.99440 0.00000  0.00000  0.00000  304 GLY   K C   
17037 O O   . GLY   K  304 ? 1.03006 1.03006 1.03006 0.00000  0.00000  0.00000  304 GLY   K O   
17038 N N   . THR   K  305 ? 1.12966 1.12966 1.12966 0.00000  0.00000  0.00000  305 THR   K N   
17039 C CA  . THR   K  305 ? 1.14611 1.14611 1.14611 0.00000  0.00000  0.00000  305 THR   K CA  
17040 C C   . THR   K  305 ? 1.42388 1.42388 1.42388 0.00000  0.00000  0.00000  305 THR   K C   
17041 O O   . THR   K  305 ? 0.97900 0.97900 0.97900 0.00000  0.00000  0.00000  305 THR   K O   
17042 C CB  . THR   K  305 ? 1.01464 1.01464 1.01464 0.00000  0.00000  0.00000  305 THR   K CB  
17043 O OG1 . THR   K  305 ? 1.23085 1.23085 1.23085 -0.00000 -0.00000 0.00000  305 THR   K OG1 
17044 C CG2 . THR   K  305 ? 1.01194 1.01194 1.01194 -0.00000 0.00000  0.00000  305 THR   K CG2 
17045 N N   . ILE   K  306 ? 0.94766 0.94766 0.94766 0.00000  0.00000  0.00000  306 ILE   K N   
17046 C CA  . ILE   K  306 ? 1.11010 1.11010 1.11010 0.00000  -0.00000 0.00000  306 ILE   K CA  
17047 C C   . ILE   K  306 ? 1.11819 1.11819 1.11819 0.00000  0.00000  0.00000  306 ILE   K C   
17048 O O   . ILE   K  306 ? 1.15689 1.15689 1.15689 -0.00000 0.00000  0.00000  306 ILE   K O   
17049 C CB  . ILE   K  306 ? 1.06284 1.06284 1.06284 -0.00000 0.00000  0.00000  306 ILE   K CB  
17050 C CG1 . ILE   K  306 ? 0.90330 0.90330 0.90330 0.00000  0.00000  0.00000  306 ILE   K CG1 
17051 C CG2 . ILE   K  306 ? 1.00831 1.00831 1.00831 -0.00000 0.00000  0.00000  306 ILE   K CG2 
17052 C CD1 . ILE   K  306 ? 0.98888 0.98888 0.98888 0.00000  0.00000  0.00000  306 ILE   K CD1 
17053 N N   . VAL   K  307 ? 0.86062 0.86062 0.86062 -0.00000 0.00000  0.00000  307 VAL   K N   
17054 C CA  . VAL   K  307 ? 0.78317 0.78317 0.78317 0.00000  0.00000  0.00000  307 VAL   K CA  
17055 C C   . VAL   K  307 ? 0.89358 0.89358 0.89358 0.00000  0.00000  0.00000  307 VAL   K C   
17056 O O   . VAL   K  307 ? 0.87462 0.87462 0.87462 0.00000  0.00000  0.00000  307 VAL   K O   
17057 C CB  . VAL   K  307 ? 0.98483 0.98483 0.98483 0.00000  0.00000  0.00000  307 VAL   K CB  
17058 C CG1 . VAL   K  307 ? 0.65522 0.65522 0.65522 -0.00000 0.00000  0.00000  307 VAL   K CG1 
17059 C CG2 . VAL   K  307 ? 0.79544 0.79544 0.79544 0.00000  0.00000  0.00000  307 VAL   K CG2 
17060 N N   . LYS   K  308 ? 0.99702 0.99702 0.99702 0.00000  0.00000  0.00000  308 LYS   K N   
17061 C CA  . LYS   K  308 ? 0.87821 0.87821 0.87821 0.00000  0.00000  0.00000  308 LYS   K CA  
17062 C C   . LYS   K  308 ? 1.04948 1.04948 1.04948 0.00000  0.00000  0.00000  308 LYS   K C   
17063 O O   . LYS   K  308 ? 0.83633 0.83633 0.83633 0.00000  0.00000  0.00000  308 LYS   K O   
17064 C CB  . LYS   K  308 ? 0.83788 0.83788 0.83788 0.00000  0.00000  0.00000  308 LYS   K CB  
17065 C CG  . LYS   K  308 ? 0.72821 0.72821 0.72821 0.00000  -0.00000 0.00000  308 LYS   K CG  
17066 C CD  . LYS   K  308 ? 0.86573 0.86573 0.86573 0.00000  0.00000  0.00000  308 LYS   K CD  
17067 C CE  . LYS   K  308 ? 1.11831 1.11831 1.11831 0.00000  0.00000  0.00000  308 LYS   K CE  
17068 N NZ  . LYS   K  308 ? 1.26580 1.26580 1.26580 -0.00000 0.00000  0.00000  308 LYS   K NZ  
17069 N N   . ILE   K  309 ? 0.70946 0.70946 0.70946 -0.00000 0.00000  0.00000  309 ILE   K N   
17070 C CA  . ILE   K  309 ? 0.79911 0.79911 0.79911 0.00000  0.00000  0.00000  309 ILE   K CA  
17071 C C   . ILE   K  309 ? 0.70346 0.70346 0.70346 0.00000  0.00000  0.00000  309 ILE   K C   
17072 O O   . ILE   K  309 ? 0.81207 0.81207 0.81207 -0.00000 0.00000  0.00000  309 ILE   K O   
17073 C CB  . ILE   K  309 ? 0.60218 0.60218 0.60218 0.00000  0.00000  0.00000  309 ILE   K CB  
17074 C CG1 . ILE   K  309 ? 0.86422 0.86422 0.86422 -0.00000 0.00000  0.00000  309 ILE   K CG1 
17075 C CG2 . ILE   K  309 ? 0.63580 0.63580 0.63580 0.00000  0.00000  0.00000  309 ILE   K CG2 
17076 C CD1 . ILE   K  309 ? 0.61975 0.61975 0.61975 0.00000  0.00000  0.00000  309 ILE   K CD1 
17077 N N   . ILE   K  310 ? 0.67912 0.67912 0.67912 0.00000  0.00000  0.00000  310 ILE   K N   
17078 C CA  . ILE   K  310 ? 0.47493 0.47493 0.47493 0.00000  0.00000  0.00000  310 ILE   K CA  
17079 C C   . ILE   K  310 ? 0.69545 0.69545 0.69545 0.00000  0.00000  0.00000  310 ILE   K C   
17080 O O   . ILE   K  310 ? 0.60672 0.60672 0.60672 -0.00000 0.00000  0.00000  310 ILE   K O   
17081 C CB  . ILE   K  310 ? 0.69517 0.69517 0.69517 0.00000  0.00000  0.00000  310 ILE   K CB  
17082 C CG1 . ILE   K  310 ? 0.70898 0.70898 0.70898 0.00000  0.00000  0.00000  310 ILE   K CG1 
17083 C CG2 . ILE   K  310 ? 0.53605 0.53605 0.53605 -0.00000 0.00000  0.00000  310 ILE   K CG2 
17084 C CD1 . ILE   K  310 ? 0.76435 0.76435 0.76435 -0.00000 0.00000  0.00000  310 ILE   K CD1 
17085 N N   . ASN   K  311 ? 0.58126 0.58126 0.58126 -0.00000 0.00000  0.00000  311 ASN   K N   
17086 C CA  . ASN   K  311 ? 0.54089 0.54089 0.54089 0.00000  0.00000  0.00000  311 ASN   K CA  
17087 C C   . ASN   K  311 ? 0.40609 0.40609 0.40609 0.00000  0.00000  0.00000  311 ASN   K C   
17088 O O   . ASN   K  311 ? 0.74821 0.74821 0.74821 0.00000  0.00000  0.00000  311 ASN   K O   
17089 C CB  . ASN   K  311 ? 0.34780 0.34780 0.34780 0.00000  0.00000  0.00000  311 ASN   K CB  
17090 C CG  . ASN   K  311 ? 0.92689 0.92689 0.92689 -0.00000 0.00000  0.00000  311 ASN   K CG  
17091 O OD1 . ASN   K  311 ? 0.67347 0.67347 0.67347 0.00000  0.00000  0.00000  311 ASN   K OD1 
17092 N ND2 . ASN   K  311 ? 0.70138 0.70138 0.70138 0.00000  0.00000  0.00000  311 ASN   K ND2 
17093 N N   . VAL   K  312 ? 0.44879 0.44879 0.44879 -0.00000 0.00000  0.00000  312 VAL   K N   
17094 C CA  . VAL   K  312 ? 0.42910 0.42910 0.42910 0.00000  0.00000  0.00000  312 VAL   K CA  
17095 C C   . VAL   K  312 ? 0.41448 0.41448 0.41448 0.00000  0.00000  0.00000  312 VAL   K C   
17096 O O   . VAL   K  312 ? 0.72989 0.72989 0.72989 0.00000  0.00000  0.00000  312 VAL   K O   
17097 C CB  . VAL   K  312 ? 0.47426 0.47426 0.47426 0.00000  0.00000  0.00000  312 VAL   K CB  
17098 C CG1 . VAL   K  312 ? 0.30071 0.30071 0.30071 -0.00000 0.00000  0.00000  312 VAL   K CG1 
17099 C CG2 . VAL   K  312 ? 0.38176 0.38176 0.38176 0.00000  0.00000  0.00000  312 VAL   K CG2 
17100 N N   . PRO   K  313 ? 0.58663 0.58663 0.58663 0.00000  0.00000  0.00000  313 PRO   K N   
17101 C CA  . PRO   K  313 ? 0.53195 0.53195 0.53195 0.00000  0.00000  0.00000  313 PRO   K CA  
17102 C C   . PRO   K  313 ? 0.57856 0.57856 0.57856 -0.00000 0.00000  0.00000  313 PRO   K C   
17103 O O   . PRO   K  313 ? 0.51825 0.51825 0.51825 0.00000  0.00000  0.00000  313 PRO   K O   
17104 C CB  . PRO   K  313 ? 0.31714 0.31714 0.31714 0.00000  0.00000  0.00000  313 PRO   K CB  
17105 C CG  . PRO   K  313 ? 0.39121 0.39121 0.39121 0.00000  -0.00000 0.00000  313 PRO   K CG  
17106 C CD  . PRO   K  313 ? 0.34272 0.34272 0.34272 0.00000  0.00000  0.00000  313 PRO   K CD  
17107 N N   . GLY   K  314 ? 0.48625 0.48625 0.48625 -0.00000 0.00000  0.00000  314 GLY   K N   
17108 C CA  . GLY   K  314 ? 0.39077 0.39077 0.39077 0.00000  0.00000  0.00000  314 GLY   K CA  
17109 C C   . GLY   K  314 ? 0.60561 0.60561 0.60561 -0.00000 0.00000  0.00000  314 GLY   K C   
17110 O O   . GLY   K  314 ? 0.49480 0.49480 0.49480 -0.00000 0.00000  0.00000  314 GLY   K O   
17111 N N   . THR   K  315 ? 0.38351 0.38351 0.38351 -0.00000 0.00000  0.00000  315 THR   K N   
17112 C CA  . THR   K  315 ? 0.41329 0.41329 0.41329 0.00000  0.00000  0.00000  315 THR   K CA  
17113 C C   . THR   K  315 ? 0.51880 0.51880 0.51880 -0.00000 0.00000  0.00000  315 THR   K C   
17114 O O   . THR   K  315 ? 0.41980 0.41980 0.41980 0.00000  0.00000  0.00000  315 THR   K O   
17115 C CB  . THR   K  315 ? 0.40851 0.40851 0.40851 -0.00000 0.00000  0.00000  315 THR   K CB  
17116 O OG1 . THR   K  315 ? 0.32972 0.32972 0.32972 0.00000  0.00000  0.00000  315 THR   K OG1 
17117 C CG2 . THR   K  315 ? 0.28808 0.28808 0.28808 0.00000  0.00000  0.00000  315 THR   K CG2 
17118 N N   . TYR   K  316 ? 0.42380 0.42380 0.42380 0.00000  0.00000  0.00000  316 TYR   K N   
17119 C CA  . TYR   K  316 ? 0.41822 0.41822 0.41822 -0.00000 0.00000  0.00000  316 TYR   K CA  
17120 C C   . TYR   K  316 ? 0.35521 0.35521 0.35521 0.00000  0.00000  0.00000  316 TYR   K C   
17121 O O   . TYR   K  316 ? 0.48012 0.48012 0.48012 -0.00000 0.00000  0.00000  316 TYR   K O   
17122 C CB  . TYR   K  316 ? 0.35421 0.35421 0.35421 0.00000  0.00000  0.00000  316 TYR   K CB  
17123 C CG  . TYR   K  316 ? 0.49031 0.49031 0.49031 0.00000  0.00000  0.00000  316 TYR   K CG  
17124 C CD1 . TYR   K  316 ? 0.50777 0.50777 0.50777 -0.00000 0.00000  0.00000  316 TYR   K CD1 
17125 C CD2 . TYR   K  316 ? 0.41557 0.41557 0.41557 0.00000  0.00000  0.00000  316 TYR   K CD2 
17126 C CE1 . TYR   K  316 ? 0.40188 0.40188 0.40188 -0.00000 0.00000  0.00000  316 TYR   K CE1 
17127 C CE2 . TYR   K  316 ? 0.31663 0.31663 0.31663 0.00000  0.00000  0.00000  316 TYR   K CE2 
17128 C CZ  . TYR   K  316 ? 0.54187 0.54187 0.54187 0.00000  0.00000  0.00000  316 TYR   K CZ  
17129 O OH  . TYR   K  316 ? 0.43134 0.43134 0.43134 -0.00000 0.00000  0.00000  316 TYR   K OH  
17130 N N   . PHE   K  317 ? 0.61336 0.61336 0.61336 0.00000  0.00000  0.00000  317 PHE   K N   
17131 C CA  . PHE   K  317 ? 0.37588 0.37588 0.37588 -0.00000 0.00000  0.00000  317 PHE   K CA  
17132 C C   . PHE   K  317 ? 0.65033 0.65033 0.65033 -0.00000 0.00000  0.00000  317 PHE   K C   
17133 O O   . PHE   K  317 ? 0.49748 0.49748 0.49748 0.00000  0.00000  0.00000  317 PHE   K O   
17134 C CB  . PHE   K  317 ? 0.37435 0.37435 0.37435 -0.00000 0.00000  0.00000  317 PHE   K CB  
17135 C CG  . PHE   K  317 ? 0.62947 0.62947 0.62947 0.00000  0.00000  0.00000  317 PHE   K CG  
17136 C CD1 . PHE   K  317 ? 0.38449 0.38449 0.38449 0.00000  0.00000  0.00000  317 PHE   K CD1 
17137 C CD2 . PHE   K  317 ? 0.57581 0.57581 0.57581 0.00000  0.00000  0.00000  317 PHE   K CD2 
17138 C CE1 . PHE   K  317 ? 0.57838 0.57838 0.57838 -0.00000 0.00000  0.00000  317 PHE   K CE1 
17139 C CE2 . PHE   K  317 ? 0.48453 0.48453 0.48453 0.00000  0.00000  0.00000  317 PHE   K CE2 
17140 C CZ  . PHE   K  317 ? 0.50234 0.50234 0.50234 0.00000  0.00000  0.00000  317 PHE   K CZ  
17141 N N   . ALA   K  318 ? 0.33167 0.33167 0.33167 0.00000  0.00000  0.00000  318 ALA   K N   
17142 C CA  . ALA   K  318 ? 0.29210 0.29210 0.29210 -0.00000 0.00000  0.00000  318 ALA   K CA  
17143 C C   . ALA   K  318 ? 0.35309 0.35309 0.35309 -0.00000 0.00000  0.00000  318 ALA   K C   
17144 O O   . ALA   K  318 ? 0.41536 0.41536 0.41536 -0.00000 0.00000  0.00000  318 ALA   K O   
17145 C CB  . ALA   K  318 ? 0.21005 0.21005 0.21005 -0.00000 0.00000  0.00000  318 ALA   K CB  
17146 N N   . GLN   K  319 ? 0.44721 0.44721 0.44721 -0.00000 0.00000  0.00000  319 GLN   K N   
17147 C CA  . GLN   K  319 ? 0.40264 0.40264 0.40264 0.00000  0.00000  0.00000  319 GLN   K CA  
17148 C C   . GLN   K  319 ? 0.37851 0.37851 0.37851 0.00000  0.00000  -0.00000 319 GLN   K C   
17149 O O   . GLN   K  319 ? 0.55928 0.55928 0.55928 0.00000  0.00000  0.00000  319 GLN   K O   
17150 C CB  . GLN   K  319 ? 0.39613 0.39613 0.39613 0.00000  0.00000  0.00000  319 GLN   K CB  
17151 C CG  . GLN   K  319 ? 0.49875 0.49875 0.49875 0.00000  0.00000  0.00000  319 GLN   K CG  
17152 C CD  . GLN   K  319 ? 0.35959 0.35959 0.35959 0.00000  0.00000  0.00000  319 GLN   K CD  
17153 O OE1 . GLN   K  319 ? 0.65495 0.65495 0.65495 0.00000  0.00000  0.00000  319 GLN   K OE1 
17154 N NE2 . GLN   K  319 ? 0.47113 0.47113 0.47113 0.00000  0.00000  0.00000  319 GLN   K NE2 
17155 N N   . ALA   K  320 ? 0.48534 0.48534 0.48534 -0.00000 0.00000  0.00000  320 ALA   K N   
17156 C CA  . ALA   K  320 ? 0.49478 0.49478 0.49478 -0.00000 0.00000  0.00000  320 ALA   K CA  
17157 C C   . ALA   K  320 ? 0.49152 0.49152 0.49152 0.00000  0.00000  0.00000  320 ALA   K C   
17158 O O   . ALA   K  320 ? 0.51101 0.51101 0.51101 0.00000  0.00000  0.00000  320 ALA   K O   
17159 C CB  . ALA   K  320 ? 0.28888 0.28888 0.28888 -0.00000 0.00000  0.00000  320 ALA   K CB  
17160 N N   . PRO   K  321 ? 0.58976 0.58976 0.58976 0.00000  0.00000  0.00000  321 PRO   K N   
17161 C CA  . PRO   K  321 ? 0.41117 0.41117 0.41117 -0.00000 0.00000  0.00000  321 PRO   K CA  
17162 C C   . PRO   K  321 ? 0.48318 0.48318 0.48318 0.00000  0.00000  0.00000  321 PRO   K C   
17163 O O   . PRO   K  321 ? 0.54354 0.54354 0.54354 0.00000  0.00000  0.00000  321 PRO   K O   
17164 C CB  . PRO   K  321 ? 0.32500 0.32500 0.32500 -0.00000 0.00000  0.00000  321 PRO   K CB  
17165 C CG  . PRO   K  321 ? 0.59300 0.59300 0.59300 0.00000  0.00000  0.00000  321 PRO   K CG  
17166 C CD  . PRO   K  321 ? 0.36870 0.36870 0.36870 0.00000  0.00000  0.00000  321 PRO   K CD  
17167 N N   . SER   K  322 ? 0.54929 0.54929 0.54929 0.00000  0.00000  0.00000  322 SER   K N   
17168 C CA  . SER   K  322 ? 0.54273 0.54273 0.54273 0.00000  0.00000  0.00000  322 SER   K CA  
17169 C C   . SER   K  322 ? 0.53771 0.53771 0.53771 0.00000  0.00000  0.00000  322 SER   K C   
17170 O O   . SER   K  322 ? 0.78316 0.78316 0.78316 0.00000  0.00000  0.00000  322 SER   K O   
17171 C CB  . SER   K  322 ? 0.42956 0.42956 0.42956 0.00000  0.00000  0.00000  322 SER   K CB  
17172 O OG  . SER   K  322 ? 0.74735 0.74735 0.74735 0.00000  0.00000  0.00000  322 SER   K OG  
17173 N N   . THR   K  323 ? 0.61338 0.61338 0.61338 0.00000  0.00000  0.00000  323 THR   K N   
17174 C CA  . THR   K  323 ? 0.38977 0.38977 0.38977 0.00000  0.00000  0.00000  323 THR   K CA  
17175 C C   . THR   K  323 ? 0.58576 0.58576 0.58576 0.00000  -0.00000 0.00000  323 THR   K C   
17176 O O   . THR   K  323 ? 0.36933 0.36933 0.36933 0.00000  0.00000  0.00000  323 THR   K O   
17177 C CB  . THR   K  323 ? 0.47506 0.47506 0.47506 0.00000  0.00000  0.00000  323 THR   K CB  
17178 O OG1 . THR   K  323 ? 0.49451 0.49451 0.49451 0.00000  0.00000  0.00000  323 THR   K OG1 
17179 C CG2 . THR   K  323 ? 0.24646 0.24646 0.24646 -0.00000 0.00000  0.00000  323 THR   K CG2 
17180 N N   . ILE   K  324 ? 0.48563 0.48563 0.48563 0.00000  0.00000  0.00000  324 ILE   K N   
17181 C CA  . ILE   K  324 ? 0.50774 0.50774 0.50774 0.00000  0.00000  0.00000  324 ILE   K CA  
17182 C C   . ILE   K  324 ? 0.74267 0.74267 0.74267 0.00000  0.00000  0.00000  324 ILE   K C   
17183 O O   . ILE   K  324 ? 0.64984 0.64984 0.64984 0.00000  0.00000  0.00000  324 ILE   K O   
17184 C CB  . ILE   K  324 ? 0.35587 0.35587 0.35587 0.00000  -0.00000 0.00000  324 ILE   K CB  
17185 C CG1 . ILE   K  324 ? 0.52531 0.52531 0.52531 0.00000  0.00000  0.00000  324 ILE   K CG1 
17186 C CG2 . ILE   K  324 ? 0.38807 0.38807 0.38807 0.00000  0.00000  0.00000  324 ILE   K CG2 
17187 C CD1 . ILE   K  324 ? 0.44303 0.44303 0.44303 0.00000  0.00000  0.00000  324 ILE   K CD1 
17188 N N   . GLY   K  325 ? 0.56788 0.56788 0.56788 -0.00000 0.00000  0.00000  325 GLY   K N   
17189 C CA  . GLY   K  325 ? 0.50734 0.50734 0.50734 -0.00000 0.00000  0.00000  325 GLY   K CA  
17190 C C   . GLY   K  325 ? 0.62172 0.62172 0.62172 -0.00000 0.00000  0.00000  325 GLY   K C   
17191 O O   . GLY   K  325 ? 0.68721 0.68721 0.68721 -0.00000 0.00000  0.00000  325 GLY   K O   
17192 N N   . ASP   K  326 ? 0.48288 0.48288 0.48288 -0.00000 0.00000  0.00000  326 ASP   K N   
17193 C CA  . ASP   K  326 ? 0.57412 0.57412 0.57412 0.00000  -0.00000 0.00000  326 ASP   K CA  
17194 C C   . ASP   K  326 ? 0.46235 0.46235 0.46235 -0.00000 0.00000  0.00000  326 ASP   K C   
17195 O O   . ASP   K  326 ? 0.59366 0.59366 0.59366 -0.00000 0.00000  0.00000  326 ASP   K O   
17196 C CB  . ASP   K  326 ? 0.35162 0.35162 0.35162 0.00000  0.00000  0.00000  326 ASP   K CB  
17197 C CG  . ASP   K  326 ? 0.81609 0.81609 0.81609 -0.00000 0.00000  0.00000  326 ASP   K CG  
17198 O OD1 . ASP   K  326 ? 0.63372 0.63372 0.63372 0.00000  0.00000  0.00000  326 ASP   K OD1 
17199 O OD2 . ASP   K  326 ? 0.66657 0.66657 0.66657 0.00000  0.00000  0.00000  326 ASP   K OD2 
17200 N N   . PRO   K  327 ? 0.79192 0.79192 0.79192 0.00000  0.00000  0.00000  327 PRO   K N   
17201 C CA  . PRO   K  327 ? 0.60773 0.60773 0.60773 -0.00000 0.00000  0.00000  327 PRO   K CA  
17202 C C   . PRO   K  327 ? 0.54084 0.54084 0.54084 -0.00000 0.00000  -0.00000 327 PRO   K C   
17203 O O   . PRO   K  327 ? 0.70527 0.70527 0.70527 0.00000  0.00000  0.00000  327 PRO   K O   
17204 C CB  . PRO   K  327 ? 0.35305 0.35305 0.35305 0.00000  0.00000  0.00000  327 PRO   K CB  
17205 C CG  . PRO   K  327 ? 0.53884 0.53884 0.53884 -0.00000 0.00000  0.00000  327 PRO   K CG  
17206 C CD  . PRO   K  327 ? 0.57576 0.57576 0.57576 -0.00000 0.00000  0.00000  327 PRO   K CD  
17207 N N   . ILE   K  328 ? 0.60018 0.60018 0.60018 0.00000  0.00000  0.00000  328 ILE   K N   
17208 C CA  . ILE   K  328 ? 0.59764 0.59764 0.59764 0.00000  0.00000  0.00000  328 ILE   K CA  
17209 C C   . ILE   K  328 ? 0.62672 0.62672 0.62672 -0.00000 0.00000  0.00000  328 ILE   K C   
17210 O O   . ILE   K  328 ? 0.74122 0.74122 0.74122 0.00000  -0.00000 -0.00000 328 ILE   K O   
17211 C CB  . ILE   K  328 ? 0.66382 0.66382 0.66382 -0.00000 0.00000  0.00000  328 ILE   K CB  
17212 C CG1 . ILE   K  328 ? 0.50495 0.50495 0.50495 0.00000  0.00000  0.00000  328 ILE   K CG1 
17213 C CG2 . ILE   K  328 ? 0.52679 0.52679 0.52679 0.00000  0.00000  0.00000  328 ILE   K CG2 
17214 C CD1 . ILE   K  328 ? 0.45442 0.45442 0.45442 -0.00000 0.00000  0.00000  328 ILE   K CD1 
17215 N N   . PRO   K  329 ? 0.86962 0.86962 0.86962 0.00000  0.00000  0.00000  329 PRO   K N   
17216 C CA  . PRO   K  329 ? 0.68562 0.68562 0.68562 -0.00000 0.00000  0.00000  329 PRO   K CA  
17217 C C   . PRO   K  329 ? 0.71416 0.71416 0.71416 0.00000  0.00000  0.00000  329 PRO   K C   
17218 O O   . PRO   K  329 ? 1.12388 1.12388 1.12388 -0.00000 0.00000  0.00000  329 PRO   K O   
17219 C CB  . PRO   K  329 ? 0.51921 0.51921 0.51921 0.00000  0.00000  -0.00000 329 PRO   K CB  
17220 C CG  . PRO   K  329 ? 0.65484 0.65484 0.65484 -0.00000 0.00000  0.00000  329 PRO   K CG  
17221 C CD  . PRO   K  329 ? 0.71679 0.71679 0.71679 -0.00000 0.00000  0.00000  329 PRO   K CD  
17222 N N   . ASP   K  330 ? 1.07336 1.07336 1.07336 -0.00000 0.00000  0.00000  330 ASP   K N   
17223 C CA  . ASP   K  330 ? 1.20092 1.20092 1.20092 -0.00000 0.00000  0.00000  330 ASP   K CA  
17224 C C   . ASP   K  330 ? 0.93107 0.93107 0.93107 0.00000  0.00000  0.00000  330 ASP   K C   
17225 O O   . ASP   K  330 ? 1.29487 1.29487 1.29487 0.00000  0.00000  0.00000  330 ASP   K O   
17226 C CB  . ASP   K  330 ? 0.83660 0.83660 0.83660 -0.00000 0.00000  0.00000  330 ASP   K CB  
17227 C CG  . ASP   K  330 ? 0.71512 0.71512 0.71512 0.00000  0.00000  0.00000  330 ASP   K CG  
17228 O OD1 . ASP   K  330 ? 1.15418 1.15418 1.15418 0.00000  -0.00000 0.00000  330 ASP   K OD1 
17229 O OD2 . ASP   K  330 ? 1.35109 1.35109 1.35109 0.00000  0.00000  0.00000  330 ASP   K OD2 
17230 N N   . ASN   K  331 ? 1.02719 1.02719 1.02719 0.00000  0.00000  0.00000  331 ASN   K N   
17231 C CA  . ASN   K  331 ? 1.02878 1.02878 1.02878 0.00000  0.00000  0.00000  331 ASN   K CA  
17232 C C   . ASN   K  331 ? 0.80927 0.80927 0.80927 0.00000  0.00000  0.00000  331 ASN   K C   
17233 O O   . ASN   K  331 ? 1.36286 1.36286 1.36286 -0.00000 0.00000  0.00000  331 ASN   K O   
17234 C CB  . ASN   K  331 ? 0.74918 0.74918 0.74918 -0.00000 0.00000  0.00000  331 ASN   K CB  
17235 C CG  . ASN   K  331 ? 0.88966 0.88966 0.88966 0.00000  0.00000  0.00000  331 ASN   K CG  
17236 O OD1 . ASN   K  331 ? 1.77005 1.77005 1.77005 0.00000  0.00000  0.00000  331 ASN   K OD1 
17237 N ND2 . ASN   K  331 ? 0.94247 0.94247 0.94247 -0.00000 0.00000  0.00000  331 ASN   K ND2 
17238 N N   . ASP   K  332 ? 1.25043 1.25043 1.25043 0.00000  0.00000  0.00000  332 ASP   K N   
17239 C CA  . ASP   K  332 ? 0.33327 0.33327 0.33327 0.00000  0.00000  0.00000  332 ASP   K CA  
17240 C C   . ASP   K  332 ? 1.14842 1.14842 1.14842 0.00000  0.00000  0.00000  332 ASP   K C   
17241 O O   . ASP   K  332 ? 0.48140 0.48140 0.48140 0.00000  0.00000  0.00000  332 ASP   K O   
17242 C CB  . ASP   K  332 ? 1.53916 1.53916 1.53916 0.00000  0.00000  0.00000  332 ASP   K CB  
17243 C CG  . ASP   K  332 ? 0.98153 0.98153 0.98153 0.00000  0.00000  0.00000  332 ASP   K CG  
17244 O OD1 . ASP   K  332 ? 1.11062 1.11062 1.11062 -0.00000 0.00000  0.00000  332 ASP   K OD1 
17245 O OD2 . ASP   K  332 ? 0.75186 0.75186 0.75186 0.00000  0.00000  0.00000  332 ASP   K OD2 
17246 N N   . TYR   K  333 ? 1.44322 1.44322 1.44322 0.00000  0.00000  0.00000  333 TYR   K N   
17247 C CA  . TYR   K  333 ? 0.72674 0.72674 0.72674 0.00000  0.00000  0.00000  333 TYR   K CA  
17248 C C   . TYR   K  333 ? 1.31404 1.31404 1.31404 0.00000  0.00000  0.00000  333 TYR   K C   
17249 O O   . TYR   K  333 ? 0.69180 0.69180 0.69180 -0.00000 0.00000  0.00000  333 TYR   K O   
17250 C CB  . TYR   K  333 ? 0.27103 0.27103 0.27103 0.00000  0.00000  0.00000  333 TYR   K CB  
17251 C CG  . TYR   K  333 ? 0.99331 0.99331 0.99331 0.00000  0.00000  0.00000  333 TYR   K CG  
17252 C CD1 . TYR   K  333 ? 0.88726 0.88726 0.88726 0.00000  0.00000  0.00000  333 TYR   K CD1 
17253 C CD2 . TYR   K  333 ? 0.90517 0.90517 0.90517 -0.00000 0.00000  0.00000  333 TYR   K CD2 
17254 C CE1 . TYR   K  333 ? 0.59643 0.59643 0.59643 0.00000  0.00000  0.00000  333 TYR   K CE1 
17255 C CE2 . TYR   K  333 ? 0.84364 0.84364 0.84364 -0.00000 0.00000  0.00000  333 TYR   K CE2 
17256 C CZ  . TYR   K  333 ? 1.04897 1.04897 1.04897 -0.00000 0.00000  0.00000  333 TYR   K CZ  
17257 O OH  . TYR   K  333 ? 0.75301 0.75301 0.75301 0.00000  0.00000  0.00000  333 TYR   K OH  
17258 N N   . ASP   K  334 ? 0.91875 0.91875 0.91875 0.00000  0.00000  0.00000  334 ASP   K N   
17259 C CA  . ASP   K  334 ? 0.89437 0.89437 0.89437 -0.00000 0.00000  0.00000  334 ASP   K CA  
17260 C C   . ASP   K  334 ? 1.01393 1.01393 1.01393 -0.00000 0.00000  0.00000  334 ASP   K C   
17261 O O   . ASP   K  334 ? 0.57986 0.57986 0.57986 0.00000  0.00000  0.00000  334 ASP   K O   
17262 C CB  . ASP   K  334 ? 1.25915 1.25915 1.25915 0.00000  0.00000  -0.00000 334 ASP   K CB  
17263 C CG  . ASP   K  334 ? 1.44433 1.44433 1.44433 -0.00000 0.00000  0.00000  334 ASP   K CG  
17264 O OD1 . ASP   K  334 ? 0.88967 0.88967 0.88967 0.00000  0.00000  0.00000  334 ASP   K OD1 
17265 O OD2 . ASP   K  334 ? 1.03309 1.03309 1.03309 0.00000  0.00000  0.00000  334 ASP   K OD2 
17266 N N   . PRO   K  335 ? 0.94616 0.94616 0.94616 0.00000  0.00000  0.00000  335 PRO   K N   
17267 C CA  . PRO   K  335 ? 0.69041 0.69041 0.69041 -0.00000 0.00000  -0.00000 335 PRO   K CA  
17268 C C   . PRO   K  335 ? 0.48814 0.48814 0.48814 0.00000  0.00000  0.00000  335 PRO   K C   
17269 O O   . PRO   K  335 ? 0.85469 0.85469 0.85469 -0.00000 0.00000  0.00000  335 PRO   K O   
17270 C CB  . PRO   K  335 ? 0.76360 0.76360 0.76360 -0.00000 0.00000  0.00000  335 PRO   K CB  
17271 C CG  . PRO   K  335 ? 0.92648 0.92648 0.92648 0.00000  0.00000  -0.00000 335 PRO   K CG  
17272 C CD  . PRO   K  335 ? 0.59181 0.59181 0.59181 0.00000  0.00000  0.00000  335 PRO   K CD  
17273 N N   . PRO   K  336 ? 0.77046 0.77046 0.77046 -0.00000 0.00000  0.00000  336 PRO   K N   
17274 C CA  . PRO   K  336 ? 0.31977 0.31977 0.31977 -0.00000 0.00000  0.00000  336 PRO   K CA  
17275 C C   . PRO   K  336 ? 1.15937 1.15937 1.15937 -0.00000 0.00000  0.00000  336 PRO   K C   
17276 O O   . PRO   K  336 ? 0.38764 0.38764 0.38764 0.00000  0.00000  0.00000  336 PRO   K O   
17277 C CB  . PRO   K  336 ? 0.56019 0.56019 0.56019 0.00000  0.00000  0.00000  336 PRO   K CB  
17278 C CG  . PRO   K  336 ? 0.52190 0.52190 0.52190 0.00000  0.00000  0.00000  336 PRO   K CG  
17279 C CD  . PRO   K  336 ? 0.31955 0.31955 0.31955 0.00000  0.00000  0.00000  336 PRO   K CD  
17280 N N   . PRO   K  337 ? 0.42996 0.42996 0.42996 0.00000  0.00000  0.00000  337 PRO   K N   
17281 C CA  . PRO   K  337 ? 0.62768 0.62768 0.62768 0.00000  0.00000  0.00000  337 PRO   K CA  
17282 C C   . PRO   K  337 ? 0.48271 0.48271 0.48271 0.00000  0.00000  0.00000  337 PRO   K C   
17283 O O   . PRO   K  337 ? 0.45543 0.45543 0.45543 0.00000  0.00000  0.00000  337 PRO   K O   
17284 C CB  . PRO   K  337 ? 0.45699 0.45699 0.45699 -0.00000 0.00000  0.00000  337 PRO   K CB  
17285 C CG  . PRO   K  337 ? 0.56316 0.56316 0.56316 0.00000  0.00000  0.00000  337 PRO   K CG  
17286 C CD  . PRO   K  337 ? 0.67302 0.67302 0.67302 0.00000  0.00000  0.00000  337 PRO   K CD  
17287 N N   . TYR   K  338 ? 0.49059 0.49059 0.49059 0.00000  0.00000  0.00000  338 TYR   K N   
17288 C CA  . TYR   K  338 ? 0.52334 0.52334 0.52334 -0.00000 0.00000  0.00000  338 TYR   K CA  
17289 C C   . TYR   K  338 ? 0.44497 0.44497 0.44497 -0.00000 0.00000  0.00000  338 TYR   K C   
17290 O O   . TYR   K  338 ? 0.46179 0.46179 0.46179 0.00000  0.00000  0.00000  338 TYR   K O   
17291 C CB  . TYR   K  338 ? 0.36525 0.36525 0.36525 -0.00000 0.00000  0.00000  338 TYR   K CB  
17292 C CG  . TYR   K  338 ? 0.53086 0.53086 0.53086 0.00000  0.00000  0.00000  338 TYR   K CG  
17293 C CD1 . TYR   K  338 ? 0.43876 0.43876 0.43876 0.00000  0.00000  0.00000  338 TYR   K CD1 
17294 C CD2 . TYR   K  338 ? 0.41141 0.41141 0.41141 0.00000  0.00000  0.00000  338 TYR   K CD2 
17295 C CE1 . TYR   K  338 ? 0.47311 0.47311 0.47311 0.00000  0.00000  0.00000  338 TYR   K CE1 
17296 C CE2 . TYR   K  338 ? 0.33426 0.33426 0.33426 0.00000  0.00000  0.00000  338 TYR   K CE2 
17297 C CZ  . TYR   K  338 ? 0.59066 0.59066 0.59066 -0.00000 0.00000  0.00000  338 TYR   K CZ  
17298 O OH  . TYR   K  338 ? 0.44563 0.44563 0.44563 -0.00000 0.00000  0.00000  338 TYR   K OH  
17299 N N   . LEU   K  339 ? 0.46563 0.46563 0.46563 0.00000  0.00000  0.00000  339 LEU   K N   
17300 C CA  . LEU   K  339 ? 0.35369 0.35369 0.35369 0.00000  0.00000  0.00000  339 LEU   K CA  
17301 C C   . LEU   K  339 ? 0.50548 0.50548 0.50548 0.00000  0.00000  0.00000  339 LEU   K C   
17302 O O   . LEU   K  339 ? 0.52691 0.52691 0.52691 0.00000  0.00000  0.00000  339 LEU   K O   
17303 C CB  . LEU   K  339 ? 0.36411 0.36411 0.36411 0.00000  0.00000  0.00000  339 LEU   K CB  
17304 C CG  . LEU   K  339 ? 0.64294 0.64294 0.64294 0.00000  0.00000  0.00000  339 LEU   K CG  
17305 C CD1 . LEU   K  339 ? 0.43809 0.43809 0.43809 0.00000  0.00000  0.00000  339 LEU   K CD1 
17306 C CD2 . LEU   K  339 ? 0.45524 0.45524 0.45524 0.00000  0.00000  0.00000  339 LEU   K CD2 
17307 N N   . LYS   K  340 ? 0.37934 0.37934 0.37934 0.00000  0.00000  0.00000  340 LYS   K N   
17308 C CA  . LYS   K  340 ? 0.63035 0.63035 0.63035 -0.00000 0.00000  0.00000  340 LYS   K CA  
17309 C C   . LYS   K  340 ? 0.40506 0.40506 0.40506 0.00000  0.00000  0.00000  340 LYS   K C   
17310 O O   . LYS   K  340 ? 0.48601 0.48601 0.48601 0.00000  0.00000  0.00000  340 LYS   K O   
17311 C CB  . LYS   K  340 ? 0.41329 0.41329 0.41329 -0.00000 0.00000  0.00000  340 LYS   K CB  
17312 C CG  . LYS   K  340 ? 1.01173 1.01173 1.01173 0.00000  0.00000  0.00000  340 LYS   K CG  
17313 C CD  . LYS   K  340 ? 1.14317 1.14317 1.14317 0.00000  0.00000  0.00000  340 LYS   K CD  
17314 C CE  . LYS   K  340 ? 1.43164 1.43164 1.43164 0.00000  0.00000  0.00000  340 LYS   K CE  
17315 N NZ  . LYS   K  340 ? 1.36931 1.36931 1.36931 0.00000  0.00000  0.00000  340 LYS   K NZ  
17316 N N   . SER   K  341 ? 0.47712 0.47712 0.47712 0.00000  0.00000  0.00000  341 SER   K N   
17317 C CA  . SER   K  341 ? 0.39043 0.39043 0.39043 -0.00000 0.00000  0.00000  341 SER   K CA  
17318 C C   . SER   K  341 ? 0.45230 0.45230 0.45230 -0.00000 0.00000  0.00000  341 SER   K C   
17319 O O   . SER   K  341 ? 0.58590 0.58590 0.58590 0.00000  -0.00000 0.00000  341 SER   K O   
17320 C CB  . SER   K  341 ? 0.47333 0.47333 0.47333 -0.00000 0.00000  0.00000  341 SER   K CB  
17321 O OG  . SER   K  341 ? 0.47031 0.47031 0.47031 0.00000  0.00000  0.00000  341 SER   K OG  
17322 N N   . LEU   K  342 ? 0.45649 0.45649 0.45649 0.00000  0.00000  0.00000  342 LEU   K N   
17323 C CA  . LEU   K  342 ? 0.59820 0.59820 0.59820 -0.00000 0.00000  0.00000  342 LEU   K CA  
17324 C C   . LEU   K  342 ? 0.45385 0.45385 0.45385 0.00000  0.00000  -0.00000 342 LEU   K C   
17325 O O   . LEU   K  342 ? 0.52879 0.52879 0.52879 0.00000  0.00000  0.00000  342 LEU   K O   
17326 C CB  . LEU   K  342 ? 0.38119 0.38119 0.38119 -0.00000 0.00000  0.00000  342 LEU   K CB  
17327 C CG  . LEU   K  342 ? 0.61254 0.61254 0.61254 -0.00000 0.00000  0.00000  342 LEU   K CG  
17328 C CD1 . LEU   K  342 ? 0.36147 0.36147 0.36147 0.00000  0.00000  0.00000  342 LEU   K CD1 
17329 C CD2 . LEU   K  342 ? 0.30589 0.30589 0.30589 0.00000  0.00000  0.00000  342 LEU   K CD2 
17330 N N   . VAL   K  343 ? 0.56872 0.56872 0.56872 -0.00000 0.00000  0.00000  343 VAL   K N   
17331 C CA  . VAL   K  343 ? 0.49645 0.49645 0.49645 0.00000  0.00000  0.00000  343 VAL   K CA  
17332 C C   . VAL   K  343 ? 0.66001 0.66001 0.66001 0.00000  0.00000  0.00000  343 VAL   K C   
17333 O O   . VAL   K  343 ? 0.46153 0.46153 0.46153 0.00000  0.00000  0.00000  343 VAL   K O   
17334 C CB  . VAL   K  343 ? 0.50760 0.50760 0.50760 -0.00000 0.00000  0.00000  343 VAL   K CB  
17335 C CG1 . VAL   K  343 ? 0.33302 0.33302 0.33302 -0.00000 0.00000  0.00000  343 VAL   K CG1 
17336 C CG2 . VAL   K  343 ? 0.42608 0.42608 0.42608 0.00000  0.00000  0.00000  343 VAL   K CG2 
17337 N N   . TYR   K  344 ? 0.33673 0.33673 0.33673 -0.00000 0.00000  0.00000  344 TYR   K N   
17338 C CA  . TYR   K  344 ? 0.55781 0.55781 0.55781 0.00000  0.00000  0.00000  344 TYR   K CA  
17339 C C   . TYR   K  344 ? 0.57723 0.57723 0.57723 -0.00000 -0.00000 -0.00000 344 TYR   K C   
17340 O O   . TYR   K  344 ? 0.45039 0.45039 0.45039 0.00000  0.00000  0.00000  344 TYR   K O   
17341 C CB  . TYR   K  344 ? 0.39190 0.39190 0.39190 -0.00000 0.00000  0.00000  344 TYR   K CB  
17342 C CG  . TYR   K  344 ? 0.65008 0.65008 0.65008 -0.00000 0.00000  0.00000  344 TYR   K CG  
17343 C CD1 . TYR   K  344 ? 0.43162 0.43162 0.43162 0.00000  0.00000  0.00000  344 TYR   K CD1 
17344 C CD2 . TYR   K  344 ? 0.54847 0.54847 0.54847 0.00000  0.00000  0.00000  344 TYR   K CD2 
17345 C CE1 . TYR   K  344 ? 0.43414 0.43414 0.43414 0.00000  0.00000  0.00000  344 TYR   K CE1 
17346 C CE2 . TYR   K  344 ? 0.42271 0.42271 0.42271 0.00000  0.00000  0.00000  344 TYR   K CE2 
17347 C CZ  . TYR   K  344 ? 0.65410 0.65410 0.65410 0.00000  -0.00000 0.00000  344 TYR   K CZ  
17348 O OH  . TYR   K  344 ? 0.59127 0.59127 0.59127 0.00000  0.00000  0.00000  344 TYR   K OH  
17349 N N   . PHE   K  345 ? 0.33935 0.33935 0.33935 -0.00000 0.00000  0.00000  345 PHE   K N   
17350 C CA  . PHE   K  345 ? 0.45395 0.45395 0.45395 0.00000  0.00000  0.00000  345 PHE   K CA  
17351 C C   . PHE   K  345 ? 0.51955 0.51955 0.51955 0.00000  0.00000  0.00000  345 PHE   K C   
17352 O O   . PHE   K  345 ? 0.47324 0.47324 0.47324 0.00000  0.00000  0.00000  345 PHE   K O   
17353 C CB  . PHE   K  345 ? 0.33365 0.33365 0.33365 0.00000  0.00000  0.00000  345 PHE   K CB  
17354 C CG  . PHE   K  345 ? 0.50089 0.50089 0.50089 0.00000  0.00000  0.00000  345 PHE   K CG  
17355 C CD1 . PHE   K  345 ? 0.56688 0.56688 0.56688 0.00000  0.00000  0.00000  345 PHE   K CD1 
17356 C CD2 . PHE   K  345 ? 0.41918 0.41918 0.41918 -0.00000 0.00000  0.00000  345 PHE   K CD2 
17357 C CE1 . PHE   K  345 ? 0.36655 0.36655 0.36655 0.00000  0.00000  0.00000  345 PHE   K CE1 
17358 C CE2 . PHE   K  345 ? 0.43777 0.43777 0.43777 -0.00000 0.00000  0.00000  345 PHE   K CE2 
17359 C CZ  . PHE   K  345 ? 0.46687 0.46687 0.46687 0.00000  0.00000  0.00000  345 PHE   K CZ  
17360 N N   . SER   K  346 ? 0.25805 0.25805 0.25805 0.00000  0.00000  0.00000  346 SER   K N   
17361 C CA  . SER   K  346 ? 0.53931 0.53931 0.53931 -0.00000 0.00000  0.00000  346 SER   K CA  
17362 C C   . SER   K  346 ? 0.37938 0.37938 0.37938 0.00000  0.00000  0.00000  346 SER   K C   
17363 O O   . SER   K  346 ? 0.37941 0.37941 0.37941 -0.00000 0.00000  0.00000  346 SER   K O   
17364 C CB  . SER   K  346 ? 0.37185 0.37185 0.37185 0.00000  0.00000  0.00000  346 SER   K CB  
17365 O OG  . SER   K  346 ? 0.32887 0.32887 0.32887 0.00000  0.00000  0.00000  346 SER   K OG  
17366 N N   . ASN   K  347 ? 0.45570 0.45570 0.45570 0.00000  0.00000  0.00000  347 ASN   K N   
17367 C CA  . ASN   K  347 ? 0.21634 0.21634 0.21634 0.00000  0.00000  0.00000  347 ASN   K CA  
17368 C C   . ASN   K  347 ? 0.43002 0.43002 0.43002 0.00000  0.00000  0.00000  347 ASN   K C   
17369 O O   . ASN   K  347 ? 0.43436 0.43436 0.43436 0.00000  0.00000  0.00000  347 ASN   K O   
17370 C CB  . ASN   K  347 ? 0.31158 0.31158 0.31158 0.00000  0.00000  0.00000  347 ASN   K CB  
17371 C CG  . ASN   K  347 ? 0.50340 0.50340 0.50340 -0.00000 0.00000  0.00000  347 ASN   K CG  
17372 O OD1 . ASN   K  347 ? 0.39113 0.39113 0.39113 -0.00000 0.00000  0.00000  347 ASN   K OD1 
17373 N ND2 . ASN   K  347 ? 0.27374 0.27374 0.27374 0.00000  -0.00000 0.00000  347 ASN   K ND2 
17374 N N   . ILE   K  348 ? 0.43724 0.43724 0.43724 0.00000  0.00000  0.00000  348 ILE   K N   
17375 C CA  . ILE   K  348 ? 0.34853 0.34853 0.34853 0.00000  0.00000  0.00000  348 ILE   K CA  
17376 C C   . ILE   K  348 ? 0.48885 0.48885 0.48885 0.00000  0.00000  0.00000  348 ILE   K C   
17377 O O   . ILE   K  348 ? 0.53282 0.53282 0.53282 0.00000  0.00000  0.00000  348 ILE   K O   
17378 C CB  . ILE   K  348 ? 0.46231 0.46231 0.46231 0.00000  0.00000  0.00000  348 ILE   K CB  
17379 C CG1 . ILE   K  348 ? 0.31704 0.31704 0.31704 0.00000  0.00000  0.00000  348 ILE   K CG1 
17380 C CG2 . ILE   K  348 ? 0.29053 0.29053 0.29053 -0.00000 0.00000  0.00000  348 ILE   K CG2 
17381 C CD1 . ILE   K  348 ? 0.60270 0.60270 0.60270 0.00000  0.00000  0.00000  348 ILE   K CD1 
17382 N N   . ALA   K  349 ? 0.38737 0.38737 0.38737 -0.00000 0.00000  0.00000  349 ALA   K N   
17383 C CA  . ALA   K  349 ? 0.39323 0.39323 0.39323 -0.00000 0.00000  0.00000  349 ALA   K CA  
17384 C C   . ALA   K  349 ? 0.43353 0.43353 0.43353 0.00000  -0.00000 -0.00000 349 ALA   K C   
17385 O O   . ALA   K  349 ? 0.49605 0.49605 0.49605 -0.00000 0.00000  0.00000  349 ALA   K O   
17386 C CB  . ALA   K  349 ? 0.20580 0.20580 0.20580 0.00000  0.00000  0.00000  349 ALA   K CB  
17387 N N   . ALA   K  350 ? 0.43547 0.43547 0.43547 0.00000  0.00000  0.00000  350 ALA   K N   
17388 C CA  . ALA   K  350 ? 0.46696 0.46696 0.46696 0.00000  0.00000  0.00000  350 ALA   K CA  
17389 C C   . ALA   K  350 ? 0.54218 0.54218 0.54218 0.00000  0.00000  0.00000  350 ALA   K C   
17390 O O   . ALA   K  350 ? 0.46023 0.46023 0.46023 -0.00000 0.00000  0.00000  350 ALA   K O   
17391 C CB  . ALA   K  350 ? 0.28805 0.28805 0.28805 0.00000  0.00000  0.00000  350 ALA   K CB  
17392 N N   . ARG   K  351 ? 0.40422 0.40422 0.40422 -0.00000 0.00000  0.00000  351 ARG   K N   
17393 C CA  . ARG   K  351 ? 0.53409 0.53409 0.53409 -0.00000 0.00000  -0.00000 351 ARG   K CA  
17394 C C   . ARG   K  351 ? 0.43703 0.43703 0.43703 0.00000  0.00000  0.00000  351 ARG   K C   
17395 O O   . ARG   K  351 ? 0.61733 0.61733 0.61733 0.00000  0.00000  0.00000  351 ARG   K O   
17396 C CB  . ARG   K  351 ? 0.35323 0.35323 0.35323 -0.00000 0.00000  0.00000  351 ARG   K CB  
17397 C CG  . ARG   K  351 ? 0.35331 0.35331 0.35331 -0.00000 0.00000  0.00000  351 ARG   K CG  
17398 C CD  . ARG   K  351 ? 0.45355 0.45355 0.45355 0.00000  0.00000  0.00000  351 ARG   K CD  
17399 N NE  . ARG   K  351 ? 0.47336 0.47336 0.47336 0.00000  0.00000  0.00000  351 ARG   K NE  
17400 C CZ  . ARG   K  351 ? 0.74593 0.74593 0.74593 0.00000  0.00000  0.00000  351 ARG   K CZ  
17401 N NH1 . ARG   K  351 ? 0.47678 0.47678 0.47678 0.00000  0.00000  0.00000  351 ARG   K NH1 
17402 N NH2 . ARG   K  351 ? 0.41811 0.41811 0.41811 0.00000  0.00000  0.00000  351 ARG   K NH2 
17403 N N   . GLN   K  352 ? 0.58988 0.58988 0.58988 0.00000  0.00000  0.00000  352 GLN   K N   
17404 C CA  . GLN   K  352 ? 0.50578 0.50578 0.50578 0.00000  0.00000  0.00000  352 GLN   K CA  
17405 C C   . GLN   K  352 ? 0.65999 0.65999 0.65999 0.00000  0.00000  0.00000  352 GLN   K C   
17406 O O   . GLN   K  352 ? 0.64579 0.64579 0.64579 0.00000  0.00000  0.00000  352 GLN   K O   
17407 C CB  . GLN   K  352 ? 0.63452 0.63452 0.63452 0.00000  0.00000  0.00000  352 GLN   K CB  
17408 C CG  . GLN   K  352 ? 0.57187 0.57187 0.57187 0.00000  0.00000  0.00000  352 GLN   K CG  
17409 C CD  . GLN   K  352 ? 0.67758 0.67758 0.67758 0.00000  0.00000  0.00000  352 GLN   K CD  
17410 O OE1 . GLN   K  352 ? 0.70365 0.70365 0.70365 0.00000  -0.00000 0.00000  352 GLN   K OE1 
17411 N NE2 . GLN   K  352 ? 0.54035 0.54035 0.54035 0.00000  0.00000  0.00000  352 GLN   K NE2 
17412 N N   . ILE   K  353 ? 0.63769 0.63769 0.63769 -0.00000 0.00000  0.00000  353 ILE   K N   
17413 C CA  . ILE   K  353 ? 0.67345 0.67345 0.67345 0.00000  0.00000  0.00000  353 ILE   K CA  
17414 C C   . ILE   K  353 ? 0.58500 0.58500 0.58500 0.00000  0.00000  0.00000  353 ILE   K C   
17415 O O   . ILE   K  353 ? 0.76346 0.76346 0.76346 0.00000  0.00000  0.00000  353 ILE   K O   
17416 C CB  . ILE   K  353 ? 0.64687 0.64687 0.64687 0.00000  0.00000  0.00000  353 ILE   K CB  
17417 C CG1 . ILE   K  353 ? 0.73859 0.73859 0.73859 -0.00000 0.00000  0.00000  353 ILE   K CG1 
17418 C CG2 . ILE   K  353 ? 0.53116 0.53116 0.53116 0.00000  0.00000  0.00000  353 ILE   K CG2 
17419 C CD1 . ILE   K  353 ? 0.48746 0.48746 0.48746 -0.00000 0.00000  0.00000  353 ILE   K CD1 
17420 N N   . MET   K  354 ? 0.73899 0.73899 0.73899 0.00000  0.00000  0.00000  354 MET   K N   
17421 C CA  . MET   K  354 ? 0.80621 0.80621 0.80621 0.00000  0.00000  0.00000  354 MET   K CA  
17422 C C   . MET   K  354 ? 0.87073 0.87073 0.87073 -0.00000 0.00000  0.00000  354 MET   K C   
17423 O O   . MET   K  354 ? 0.88935 0.88935 0.88935 0.00000  0.00000  0.00000  354 MET   K O   
17424 C CB  . MET   K  354 ? 0.66709 0.66709 0.66709 0.00000  -0.00000 0.00000  354 MET   K CB  
17425 C CG  . MET   K  354 ? 0.94373 0.94373 0.94373 0.00000  0.00000  0.00000  354 MET   K CG  
17426 S SD  . MET   K  354 ? 0.90876 0.90876 0.90876 -0.00000 0.00000  0.00000  354 MET   K SD  
17427 C CE  . MET   K  354 ? 0.88605 0.88605 0.88605 -0.00000 0.00000  0.00000  354 MET   K CE  
17428 N N   . PHE   K  355 ? 0.92092 0.92092 0.92092 0.00000  0.00000  0.00000  355 PHE   K N   
17429 C CA  . PHE   K  355 ? 0.94158 0.94158 0.94158 0.00000  -0.00000 0.00000  355 PHE   K CA  
17430 C C   . PHE   K  355 ? 0.92562 0.92562 0.92562 0.00000  0.00000  0.00000  355 PHE   K C   
17431 O O   . PHE   K  355 ? 0.98402 0.98402 0.98402 -0.00000 0.00000  0.00000  355 PHE   K O   
17432 C CB  . PHE   K  355 ? 0.99044 0.99044 0.99044 0.00000  0.00000  0.00000  355 PHE   K CB  
17433 C CG  . PHE   K  355 ? 1.01399 1.01399 1.01399 -0.00000 0.00000  0.00000  355 PHE   K CG  
17434 C CD1 . PHE   K  355 ? 0.84990 0.84990 0.84990 -0.00000 0.00000  0.00000  355 PHE   K CD1 
17435 C CD2 . PHE   K  355 ? 0.96001 0.96001 0.96001 -0.00000 0.00000  0.00000  355 PHE   K CD2 
17436 C CE1 . PHE   K  355 ? 1.01300 1.01300 1.01300 -0.00000 0.00000  0.00000  355 PHE   K CE1 
17437 C CE2 . PHE   K  355 ? 0.79745 0.79745 0.79745 0.00000  0.00000  0.00000  355 PHE   K CE2 
17438 C CZ  . PHE   K  355 ? 0.81719 0.81719 0.81719 0.00000  0.00000  0.00000  355 PHE   K CZ  
17439 N N   . ILE   K  356 ? 0.89515 0.89515 0.89515 0.00000  0.00000  0.00000  356 ILE   K N   
17440 C CA  . ILE   K  356 ? 0.93770 0.93770 0.93770 0.00000  0.00000  0.00000  356 ILE   K CA  
17441 C C   . ILE   K  356 ? 1.10159 1.10159 1.10159 0.00000  0.00000  0.00000  356 ILE   K C   
17442 O O   . ILE   K  356 ? 0.93365 0.93365 0.93365 0.00000  0.00000  0.00000  356 ILE   K O   
17443 C CB  . ILE   K  356 ? 0.86273 0.86273 0.86273 0.00000  0.00000  0.00000  356 ILE   K CB  
17444 C CG1 . ILE   K  356 ? 0.85387 0.85387 0.85387 0.00000  0.00000  0.00000  356 ILE   K CG1 
17445 C CG2 . ILE   K  356 ? 0.90122 0.90122 0.90122 0.00000  0.00000  0.00000  356 ILE   K CG2 
17446 C CD1 . ILE   K  356 ? 0.77921 0.77921 0.77921 0.00000  0.00000  -0.00000 356 ILE   K CD1 
17447 N N   . GLU   K  357 ? 0.94494 0.94494 0.94494 -0.00000 0.00000  0.00000  357 GLU   K N   
17448 C CA  . GLU   K  357 ? 1.13483 1.13483 1.13483 0.00000  -0.00000 0.00000  357 GLU   K CA  
17449 C C   . GLU   K  357 ? 1.11210 1.11210 1.11210 0.00000  0.00000  0.00000  357 GLU   K C   
17450 O O   . GLU   K  357 ? 1.09549 1.09549 1.09549 -0.00000 0.00000  0.00000  357 GLU   K O   
17451 C CB  . GLU   K  357 ? 1.01470 1.01470 1.01470 -0.00000 0.00000  0.00000  357 GLU   K CB  
17452 C CG  . GLU   K  357 ? 0.99925 0.99925 0.99925 0.00000  0.00000  0.00000  357 GLU   K CG  
17453 C CD  . GLU   K  357 ? 1.67430 1.67430 1.67430 0.00000  0.00000  0.00000  357 GLU   K CD  
17454 O OE1 . GLU   K  357 ? 1.45303 1.45303 1.45303 0.00000  0.00000  0.00000  357 GLU   K OE1 
17455 O OE2 . GLU   K  357 ? 1.28939 1.28939 1.28939 -0.00000 0.00000  0.00000  357 GLU   K OE2 
17456 N N   . ALA   K  358 ? 1.02444 1.02444 1.02444 0.00000  0.00000  0.00000  358 ALA   K N   
17457 C CA  . ALA   K  358 ? 1.26332 1.26332 1.26332 0.00000  0.00000  0.00000  358 ALA   K CA  
17458 C C   . ALA   K  358 ? 1.19275 1.19275 1.19275 -0.00000 0.00000  0.00000  358 ALA   K C   
17459 O O   . ALA   K  358 ? 1.52197 1.52197 1.52197 0.00000  0.00000  0.00000  358 ALA   K O   
17460 C CB  . ALA   K  358 ? 1.11945 1.11945 1.11945 0.00000  -0.00000 0.00000  358 ALA   K CB  
17461 N N   . ASP   K  359 ? 1.29945 1.29945 1.29945 0.00000  0.00000  0.00000  359 ASP   K N   
17462 C CA  . ASP   K  359 ? 1.24007 1.24007 1.24007 -0.00000 0.00000  0.00000  359 ASP   K CA  
17463 C C   . ASP   K  359 ? 1.01404 1.01404 1.01404 -0.00000 0.00000  0.00000  359 ASP   K C   
17464 O O   . ASP   K  359 ? 1.09970 1.09970 1.09970 0.00000  0.00000  0.00000  359 ASP   K O   
17465 C CB  . ASP   K  359 ? 0.97491 0.97491 0.97491 0.00000  0.00000  -0.00000 359 ASP   K CB  
17466 C CG  . ASP   K  359 ? 1.44718 1.44718 1.44718 0.00000  0.00000  0.00000  359 ASP   K CG  
17467 O OD1 . ASP   K  359 ? 1.19418 1.19418 1.19418 -0.00000 0.00000  0.00000  359 ASP   K OD1 
17468 O OD2 . ASP   K  359 ? 1.11453 1.11453 1.11453 -0.00000 0.00000  0.00000  359 ASP   K OD2 
17469 N N   . ASN   K  360 ? 1.08178 1.08178 1.08178 -0.00000 0.00000  0.00000  360 ASN   K N   
17470 C CA  . ASN   K  360 ? 0.97099 0.97099 0.97099 0.00000  0.00000  0.00000  360 ASN   K CA  
17471 C C   . ASN   K  360 ? 1.10986 1.10986 1.10986 0.00000  0.00000  0.00000  360 ASN   K C   
17472 O O   . ASN   K  360 ? 1.24503 1.24503 1.24503 -0.00000 0.00000  0.00000  360 ASN   K O   
17473 C CB  . ASN   K  360 ? 0.98720 0.98720 0.98720 0.00000  0.00000  0.00000  360 ASN   K CB  
17474 C CG  . ASN   K  360 ? 1.22513 1.22513 1.22513 -0.00000 0.00000  0.00000  360 ASN   K CG  
17475 O OD1 . ASN   K  360 ? 1.26445 1.26445 1.26445 0.00000  0.00000  0.00000  360 ASN   K OD1 
17476 N ND2 . ASN   K  360 ? 1.30065 1.30065 1.30065 0.00000  0.00000  0.00000  360 ASN   K ND2 
17477 N N   . LYS   K  361 ? 1.01897 1.01897 1.01897 -0.00000 0.00000  0.00000  361 LYS   K N   
17478 C CA  . LYS   K  361 ? 1.11737 1.11737 1.11737 -0.00000 0.00000  0.00000  361 LYS   K CA  
17479 C C   . LYS   K  361 ? 0.76676 0.76676 0.76676 0.00000  0.00000  0.00000  361 LYS   K C   
17480 O O   . LYS   K  361 ? 1.40487 1.40487 1.40487 0.00000  0.00000  0.00000  361 LYS   K O   
17481 C CB  . LYS   K  361 ? 0.81940 0.81940 0.81940 0.00000  0.00000  0.00000  361 LYS   K CB  
17482 N N   . GLU   K  362 ? 1.02643 1.02643 1.02643 0.00000  0.00000  0.00000  362 GLU   K N   
17483 C CA  . GLU   K  362 ? 0.96897 0.96897 0.96897 0.00000  0.00000  0.00000  362 GLU   K CA  
17484 C C   . GLU   K  362 ? 1.22585 1.22585 1.22585 0.00000  0.00000  0.00000  362 GLU   K C   
17485 O O   . GLU   K  362 ? 1.12785 1.12785 1.12785 -0.00000 0.00000  0.00000  362 GLU   K O   
17486 C CB  . GLU   K  362 ? 1.08117 1.08117 1.08117 0.00000  0.00000  0.00000  362 GLU   K CB  
17487 N N   . ILE   K  363 ? 0.97009 0.97009 0.97009 -0.00000 0.00000  0.00000  363 ILE   K N   
17488 C CA  . ILE   K  363 ? 1.19765 1.19765 1.19765 -0.00000 0.00000  0.00000  363 ILE   K CA  
17489 C C   . ILE   K  363 ? 1.05190 1.05190 1.05190 0.00000  0.00000  -0.00000 363 ILE   K C   
17490 O O   . ILE   K  363 ? 1.15769 1.15769 1.15769 0.00000  0.00000  0.00000  363 ILE   K O   
17491 C CB  . ILE   K  363 ? 1.07400 1.07400 1.07400 0.00000  0.00000  0.00000  363 ILE   K CB  
17492 C CG1 . ILE   K  363 ? 0.99683 0.99683 0.99683 0.00000  0.00000  0.00000  363 ILE   K CG1 
17493 C CG2 . ILE   K  363 ? 0.81795 0.81795 0.81795 0.00000  0.00000  0.00000  363 ILE   K CG2 
17494 C CD1 . ILE   K  363 ? 1.03991 1.03991 1.03991 0.00000  0.00000  0.00000  363 ILE   K CD1 
17495 N N   . GLY   K  364 ? 0.99730 0.99730 0.99730 0.00000  0.00000  0.00000  364 GLY   K N   
17496 C CA  . GLY   K  364 ? 0.84400 0.84400 0.84400 0.00000  0.00000  0.00000  364 GLY   K CA  
17497 C C   . GLY   K  364 ? 1.41701 1.41701 1.41701 0.00000  0.00000  0.00000  364 GLY   K C   
17498 O O   . GLY   K  364 ? 0.96855 0.96855 0.96855 0.00000  0.00000  0.00000  364 GLY   K O   
17499 N N   . LEU   K  365 ? 1.05459 1.05459 1.05459 -0.00000 0.00000  0.00000  365 LEU   K N   
17500 C CA  . LEU   K  365 ? 0.76187 0.76187 0.76187 0.00000  0.00000  0.00000  365 LEU   K CA  
17501 C C   . LEU   K  365 ? 1.07414 1.07414 1.07414 0.00000  0.00000  0.00000  365 LEU   K C   
17502 O O   . LEU   K  365 ? 0.91330 0.91330 0.91330 0.00000  0.00000  0.00000  365 LEU   K O   
17503 C CB  . LEU   K  365 ? 0.94048 0.94048 0.94048 0.00000  0.00000  0.00000  365 LEU   K CB  
17504 C CG  . LEU   K  365 ? 0.98555 0.98555 0.98555 0.00000  0.00000  0.00000  365 LEU   K CG  
17505 C CD1 . LEU   K  365 ? 0.82388 0.82388 0.82388 0.00000  0.00000  0.00000  365 LEU   K CD1 
17506 C CD2 . LEU   K  365 ? 0.81168 0.81168 0.81168 0.00000  0.00000  0.00000  365 LEU   K CD2 
17507 N N   . ILE   K  366 ? 0.72315 0.72315 0.72315 0.00000  0.00000  0.00000  366 ILE   K N   
17508 C CA  . ILE   K  366 ? 0.90462 0.90462 0.90462 0.00000  0.00000  0.00000  366 ILE   K CA  
17509 C C   . ILE   K  366 ? 0.93390 0.93390 0.93390 0.00000  0.00000  0.00000  366 ILE   K C   
17510 O O   . ILE   K  366 ? 0.87722 0.87722 0.87722 -0.00000 0.00000  0.00000  366 ILE   K O   
17511 C CB  . ILE   K  366 ? 0.82055 0.82055 0.82055 0.00000  0.00000  0.00000  366 ILE   K CB  
17512 C CG1 . ILE   K  366 ? 0.86518 0.86518 0.86518 0.00000  0.00000  0.00000  366 ILE   K CG1 
17513 C CG2 . ILE   K  366 ? 0.71851 0.71851 0.71851 0.00000  -0.00000 0.00000  366 ILE   K CG2 
17514 C CD1 . ILE   K  366 ? 0.87494 0.87494 0.87494 0.00000  0.00000  0.00000  366 ILE   K CD1 
17515 N N   . PHE   K  367 ? 0.72461 0.72461 0.72461 -0.00000 0.00000  0.00000  367 PHE   K N   
17516 C CA  . PHE   K  367 ? 0.68621 0.68621 0.68621 0.00000  0.00000  0.00000  367 PHE   K CA  
17517 C C   . PHE   K  367 ? 0.80368 0.80368 0.80368 0.00000  0.00000  0.00000  367 PHE   K C   
17518 O O   . PHE   K  367 ? 0.74677 0.74677 0.74677 0.00000  0.00000  0.00000  367 PHE   K O   
17519 C CB  . PHE   K  367 ? 0.67314 0.67314 0.67314 0.00000  0.00000  0.00000  367 PHE   K CB  
17520 C CG  . PHE   K  367 ? 0.57188 0.57188 0.57188 0.00000  0.00000  0.00000  367 PHE   K CG  
17521 C CD1 . PHE   K  367 ? 0.77824 0.77824 0.77824 0.00000  0.00000  0.00000  367 PHE   K CD1 
17522 C CD2 . PHE   K  367 ? 0.71679 0.71679 0.71679 0.00000  0.00000  0.00000  367 PHE   K CD2 
17523 C CE1 . PHE   K  367 ? 0.57757 0.57757 0.57757 -0.00000 0.00000  0.00000  367 PHE   K CE1 
17524 C CE2 . PHE   K  367 ? 0.69224 0.69224 0.69224 0.00000  0.00000  0.00000  367 PHE   K CE2 
17525 C CZ  . PHE   K  367 ? 0.65072 0.65072 0.65072 0.00000  0.00000  0.00000  367 PHE   K CZ  
17526 N N   . LEU   K  368 ? 0.76583 0.76583 0.76583 0.00000  0.00000  0.00000  368 LEU   K N   
17527 C CA  . LEU   K  368 ? 0.65128 0.65128 0.65128 -0.00000 0.00000  0.00000  368 LEU   K CA  
17528 C C   . LEU   K  368 ? 0.66077 0.66077 0.66077 0.00000  0.00000  0.00000  368 LEU   K C   
17529 O O   . LEU   K  368 ? 0.76857 0.76857 0.76857 0.00000  0.00000  0.00000  368 LEU   K O   
17530 C CB  . LEU   K  368 ? 0.62171 0.62171 0.62171 0.00000  -0.00000 0.00000  368 LEU   K CB  
17531 C CG  . LEU   K  368 ? 0.75591 0.75591 0.75591 0.00000  0.00000  0.00000  368 LEU   K CG  
17532 C CD1 . LEU   K  368 ? 0.70248 0.70248 0.70248 -0.00000 0.00000  0.00000  368 LEU   K CD1 
17533 C CD2 . LEU   K  368 ? 0.72342 0.72342 0.72342 0.00000  0.00000  0.00000  368 LEU   K CD2 
17534 N N   . VAL   K  369 ? 0.45501 0.45501 0.45501 0.00000  0.00000  0.00000  369 VAL   K N   
17535 C CA  . VAL   K  369 ? 0.48464 0.48464 0.48464 0.00000  0.00000  0.00000  369 VAL   K CA  
17536 C C   . VAL   K  369 ? 0.45278 0.45278 0.45278 0.00000  0.00000  0.00000  369 VAL   K C   
17537 O O   . VAL   K  369 ? 0.57243 0.57243 0.57243 0.00000  0.00000  0.00000  369 VAL   K O   
17538 C CB  . VAL   K  369 ? 0.56357 0.56357 0.56357 0.00000  0.00000  0.00000  369 VAL   K CB  
17539 C CG1 . VAL   K  369 ? 0.43397 0.43397 0.43397 -0.00000 0.00000  0.00000  369 VAL   K CG1 
17540 C CG2 . VAL   K  369 ? 0.52761 0.52761 0.52761 -0.00000 0.00000  0.00000  369 VAL   K CG2 
17541 N N   . PHE   K  370 ? 0.69285 0.69285 0.69285 0.00000  0.00000  0.00000  370 PHE   K N   
17542 C CA  . PHE   K  370 ? 0.46038 0.46038 0.46038 0.00000  0.00000  0.00000  370 PHE   K CA  
17543 C C   . PHE   K  370 ? 0.63568 0.63568 0.63568 0.00000  0.00000  0.00000  370 PHE   K C   
17544 O O   . PHE   K  370 ? 0.61317 0.61317 0.61317 0.00000  0.00000  0.00000  370 PHE   K O   
17545 C CB  . PHE   K  370 ? 0.55517 0.55517 0.55517 0.00000  0.00000  0.00000  370 PHE   K CB  
17546 C CG  . PHE   K  370 ? 0.68191 0.68191 0.68191 0.00000  0.00000  0.00000  370 PHE   K CG  
17547 C CD1 . PHE   K  370 ? 0.56191 0.56191 0.56191 0.00000  0.00000  0.00000  370 PHE   K CD1 
17548 C CD2 . PHE   K  370 ? 0.74255 0.74255 0.74255 -0.00000 0.00000  0.00000  370 PHE   K CD2 
17549 C CE1 . PHE   K  370 ? 0.69058 0.69058 0.69058 0.00000  0.00000  0.00000  370 PHE   K CE1 
17550 C CE2 . PHE   K  370 ? 0.54474 0.54474 0.54474 0.00000  0.00000  0.00000  370 PHE   K CE2 
17551 C CZ  . PHE   K  370 ? 0.68416 0.68416 0.68416 0.00000  0.00000  0.00000  370 PHE   K CZ  
17552 N N   . ILE   K  371 ? 0.49857 0.49857 0.49857 -0.00000 0.00000  0.00000  371 ILE   K N   
17553 C CA  . ILE   K  371 ? 0.44511 0.44511 0.44511 0.00000  0.00000  0.00000  371 ILE   K CA  
17554 C C   . ILE   K  371 ? 0.45676 0.45676 0.45676 -0.00000 0.00000  0.00000  371 ILE   K C   
17555 O O   . ILE   K  371 ? 0.58224 0.58224 0.58224 0.00000  0.00000  -0.00000 371 ILE   K O   
17556 C CB  . ILE   K  371 ? 0.56056 0.56056 0.56056 0.00000  0.00000  0.00000  371 ILE   K CB  
17557 C CG1 . ILE   K  371 ? 0.42869 0.42869 0.42869 0.00000  0.00000  0.00000  371 ILE   K CG1 
17558 C CG2 . ILE   K  371 ? 0.37657 0.37657 0.37657 0.00000  0.00000  0.00000  371 ILE   K CG2 
17559 C CD1 . ILE   K  371 ? 0.40167 0.40167 0.40167 0.00000  -0.00000 0.00000  371 ILE   K CD1 
17560 N N   . GLY   K  372 ? 0.42819 0.42819 0.42819 0.00000  0.00000  -0.00000 372 GLY   K N   
17561 C CA  . GLY   K  372 ? 0.31797 0.31797 0.31797 0.00000  -0.00000 0.00000  372 GLY   K CA  
17562 C C   . GLY   K  372 ? 0.42345 0.42345 0.42345 0.00000  0.00000  0.00000  372 GLY   K C   
17563 O O   . GLY   K  372 ? 0.42564 0.42564 0.42564 -0.00000 0.00000  0.00000  372 GLY   K O   
17564 N N   . MET   K  373 ? 0.41229 0.41229 0.41229 -0.00000 0.00000  0.00000  373 MET   K N   
17565 C CA  . MET   K  373 ? 0.57739 0.57739 0.57739 0.00000  0.00000  0.00000  373 MET   K CA  
17566 C C   . MET   K  373 ? 0.54891 0.54891 0.54891 0.00000  0.00000  0.00000  373 MET   K C   
17567 O O   . MET   K  373 ? 0.48929 0.48929 0.48929 0.00000  0.00000  0.00000  373 MET   K O   
17568 C CB  . MET   K  373 ? 0.32413 0.32413 0.32413 0.00000  0.00000  0.00000  373 MET   K CB  
17569 C CG  . MET   K  373 ? 0.60053 0.60053 0.60053 0.00000  -0.00000 0.00000  373 MET   K CG  
17570 S SD  . MET   K  373 ? 0.51834 0.51834 0.51834 0.00000  0.00000  0.00000  373 MET   K SD  
17571 C CE  . MET   K  373 ? 0.21161 0.21161 0.21161 0.00000  0.00000  0.00000  373 MET   K CE  
17572 N N   . THR   K  374 ? 0.41760 0.41760 0.41760 -0.00000 0.00000  0.00000  374 THR   K N   
17573 C CA  . THR   K  374 ? 0.43497 0.43497 0.43497 -0.00000 0.00000  0.00000  374 THR   K CA  
17574 C C   . THR   K  374 ? 0.39582 0.39582 0.39582 -0.00000 0.00000  0.00000  374 THR   K C   
17575 O O   . THR   K  374 ? 0.53034 0.53034 0.53034 -0.00000 0.00000  0.00000  374 THR   K O   
17576 C CB  . THR   K  374 ? 0.54867 0.54867 0.54867 0.00000  0.00000  0.00000  374 THR   K CB  
17577 O OG1 . THR   K  374 ? 0.48475 0.48475 0.48475 0.00000  0.00000  0.00000  374 THR   K OG1 
17578 C CG2 . THR   K  374 ? 0.35329 0.35329 0.35329 -0.00000 0.00000  0.00000  374 THR   K CG2 
17579 N N   . GLU   K  375 ? 0.53081 0.53081 0.53081 0.00000  0.00000  0.00000  375 GLU   K N   
17580 C CA  . GLU   K  375 ? 0.37290 0.37290 0.37290 -0.00000 0.00000  0.00000  375 GLU   K CA  
17581 C C   . GLU   K  375 ? 0.56094 0.56094 0.56094 0.00000  0.00000  0.00000  375 GLU   K C   
17582 O O   . GLU   K  375 ? 0.38481 0.38481 0.38481 0.00000  0.00000  0.00000  375 GLU   K O   
17583 C CB  . GLU   K  375 ? 0.53574 0.53574 0.53574 0.00000  0.00000  0.00000  375 GLU   K CB  
17584 C CG  . GLU   K  375 ? 0.39207 0.39207 0.39207 -0.00000 0.00000  0.00000  375 GLU   K CG  
17585 C CD  . GLU   K  375 ? 0.52330 0.52330 0.52330 -0.00000 0.00000  0.00000  375 GLU   K CD  
17586 O OE1 . GLU   K  375 ? 0.59085 0.59085 0.59085 0.00000  0.00000  0.00000  375 GLU   K OE1 
17587 O OE2 . GLU   K  375 ? 0.57873 0.57873 0.57873 0.00000  0.00000  0.00000  375 GLU   K OE2 
17588 N N   . ILE   K  376 ? 0.38097 0.38097 0.38097 -0.00000 0.00000  0.00000  376 ILE   K N   
17589 C CA  . ILE   K  376 ? 0.38382 0.38382 0.38382 -0.00000 0.00000  0.00000  376 ILE   K CA  
17590 C C   . ILE   K  376 ? 0.43285 0.43285 0.43285 0.00000  0.00000  0.00000  376 ILE   K C   
17591 O O   . ILE   K  376 ? 0.52858 0.52858 0.52858 0.00000  -0.00000 0.00000  376 ILE   K O   
17592 C CB  . ILE   K  376 ? 0.52213 0.52213 0.52213 0.00000  0.00000  0.00000  376 ILE   K CB  
17593 C CG1 . ILE   K  376 ? 0.38829 0.38829 0.38829 -0.00000 -0.00000 0.00000  376 ILE   K CG1 
17594 C CG2 . ILE   K  376 ? 0.24442 0.24442 0.24442 0.00000  0.00000  0.00000  376 ILE   K CG2 
17595 C CD1 . ILE   K  376 ? 0.65210 0.65210 0.65210 0.00000  0.00000  0.00000  376 ILE   K CD1 
17596 N N   . SER   K  377 ? 0.45909 0.45909 0.45909 0.00000  0.00000  0.00000  377 SER   K N   
17597 C CA  . SER   K  377 ? 0.63057 0.63057 0.63057 0.00000  0.00000  0.00000  377 SER   K CA  
17598 C C   . SER   K  377 ? 0.42775 0.42775 0.42775 0.00000  0.00000  0.00000  377 SER   K C   
17599 O O   . SER   K  377 ? 0.73470 0.73470 0.73470 0.00000  0.00000  0.00000  377 SER   K O   
17600 C CB  . SER   K  377 ? 0.34990 0.34990 0.34990 0.00000  0.00000  0.00000  377 SER   K CB  
17601 O OG  . SER   K  377 ? 0.42688 0.42688 0.42688 0.00000  0.00000  0.00000  377 SER   K OG  
17602 N N   . THR   K  378 ? 0.72206 0.72206 0.72206 -0.00000 0.00000  0.00000  378 THR   K N   
17603 C CA  . THR   K  378 ? 0.54634 0.54634 0.54634 0.00000  0.00000  0.00000  378 THR   K CA  
17604 C C   . THR   K  378 ? 0.74088 0.74088 0.74088 0.00000  0.00000  0.00000  378 THR   K C   
17605 O O   . THR   K  378 ? 0.63619 0.63619 0.63619 0.00000  0.00000  0.00000  378 THR   K O   
17606 C CB  . THR   K  378 ? 0.70494 0.70494 0.70494 0.00000  0.00000  0.00000  378 THR   K CB  
17607 O OG1 . THR   K  378 ? 0.63901 0.63901 0.63901 0.00000  0.00000  0.00000  378 THR   K OG1 
17608 C CG2 . THR   K  378 ? 0.39100 0.39100 0.39100 0.00000  0.00000  0.00000  378 THR   K CG2 
17609 N N   . CYS   K  379 ? 0.54810 0.54810 0.54810 0.00000  0.00000  0.00000  379 CYS   K N   
17610 C CA  . CYS   K  379 ? 0.52634 0.52634 0.52634 -0.00000 0.00000  0.00000  379 CYS   K CA  
17611 C C   . CYS   K  379 ? 0.62855 0.62855 0.62855 -0.00000 0.00000  0.00000  379 CYS   K C   
17612 O O   . CYS   K  379 ? 0.69647 0.69647 0.69647 0.00000  0.00000  0.00000  379 CYS   K O   
17613 C CB  . CYS   K  379 ? 0.53370 0.53370 0.53370 0.00000  0.00000  0.00000  379 CYS   K CB  
17614 S SG  . CYS   K  379 ? 0.67967 0.67967 0.67967 -0.00000 0.00000  0.00000  379 CYS   K SG  
17615 N N   . GLU   K  380 ? 0.70976 0.70976 0.70976 0.00000  0.00000  0.00000  380 GLU   K N   
17616 C CA  . GLU   K  380 ? 0.52616 0.52616 0.52616 0.00000  0.00000  0.00000  380 GLU   K CA  
17617 C C   . GLU   K  380 ? 0.73251 0.73251 0.73251 0.00000  0.00000  0.00000  380 GLU   K C   
17618 O O   . GLU   K  380 ? 0.71807 0.71807 0.71807 0.00000  0.00000  0.00000  380 GLU   K O   
17619 C CB  . GLU   K  380 ? 0.67151 0.67151 0.67151 0.00000  0.00000  0.00000  380 GLU   K CB  
17620 C CG  . GLU   K  380 ? 0.83326 0.83326 0.83326 0.00000  0.00000  0.00000  380 GLU   K CG  
17621 C CD  . GLU   K  380 ? 0.77974 0.77974 0.77974 0.00000  0.00000  0.00000  380 GLU   K CD  
17622 O OE1 . GLU   K  380 ? 0.84339 0.84339 0.84339 -0.00000 0.00000  0.00000  380 GLU   K OE1 
17623 O OE2 . GLU   K  380 ? 0.93319 0.93319 0.93319 0.00000  0.00000  0.00000  380 GLU   K OE2 
17624 N N   . ALA   K  381 ? 0.69743 0.69743 0.69743 0.00000  0.00000  0.00000  381 ALA   K N   
17625 C CA  . ALA   K  381 ? 0.93171 0.93171 0.93171 0.00000  0.00000  0.00000  381 ALA   K CA  
17626 C C   . ALA   K  381 ? 0.80999 0.80999 0.80999 0.00000  0.00000  0.00000  381 ALA   K C   
17627 O O   . ALA   K  381 ? 0.81779 0.81779 0.81779 0.00000  0.00000  0.00000  381 ALA   K O   
17628 C CB  . ALA   K  381 ? 0.68451 0.68451 0.68451 -0.00000 0.00000  0.00000  381 ALA   K CB  
17629 N N   . THR   K  382 ? 0.72938 0.72938 0.72938 0.00000  0.00000  0.00000  382 THR   K N   
17630 C CA  . THR   K  382 ? 0.72408 0.72408 0.72408 0.00000  0.00000  0.00000  382 THR   K CA  
17631 C C   . THR   K  382 ? 0.66245 0.66245 0.66245 0.00000  0.00000  0.00000  382 THR   K C   
17632 O O   . THR   K  382 ? 1.01127 1.01127 1.01127 0.00000  0.00000  0.00000  382 THR   K O   
17633 C CB  . THR   K  382 ? 0.59379 0.59379 0.59379 -0.00000 0.00000  0.00000  382 THR   K CB  
17634 O OG1 . THR   K  382 ? 0.70641 0.70641 0.70641 -0.00000 0.00000  0.00000  382 THR   K OG1 
17635 C CG2 . THR   K  382 ? 0.73042 0.73042 0.73042 0.00000  0.00000  0.00000  382 THR   K CG2 
17636 N N   . VAL   K  383 ? 0.76890 0.76890 0.76890 -0.00000 0.00000  0.00000  383 VAL   K N   
17637 C CA  . VAL   K  383 ? 0.63386 0.63386 0.63386 0.00000  0.00000  0.00000  383 VAL   K CA  
17638 C C   . VAL   K  383 ? 0.81120 0.81120 0.81120 0.00000  0.00000  0.00000  383 VAL   K C   
17639 O O   . VAL   K  383 ? 0.75740 0.75740 0.75740 0.00000  0.00000  0.00000  383 VAL   K O   
17640 C CB  . VAL   K  383 ? 0.89619 0.89619 0.89619 -0.00000 0.00000  0.00000  383 VAL   K CB  
17641 C CG1 . VAL   K  383 ? 0.64356 0.64356 0.64356 0.00000  0.00000  0.00000  383 VAL   K CG1 
17642 C CG2 . VAL   K  383 ? 0.70320 0.70320 0.70320 0.00000  0.00000  0.00000  383 VAL   K CG2 
17643 N N   . SER   K  384 ? 0.91236 0.91236 0.91236 -0.00000 0.00000  0.00000  384 SER   K N   
17644 C CA  . SER   K  384 ? 0.66566 0.66566 0.66566 0.00000  0.00000  0.00000  384 SER   K CA  
17645 C C   . SER   K  384 ? 0.97465 0.97465 0.97465 -0.00000 0.00000  0.00000  384 SER   K C   
17646 O O   . SER   K  384 ? 0.83237 0.83237 0.83237 -0.00000 0.00000  0.00000  384 SER   K O   
17647 C CB  . SER   K  384 ? 0.69601 0.69601 0.69601 0.00000  0.00000  0.00000  384 SER   K CB  
17648 O OG  . SER   K  384 ? 1.04058 1.04058 1.04058 -0.00000 0.00000  0.00000  384 SER   K OG  
17649 N N   . GLU   K  385 ? 0.98613 0.98613 0.98613 0.00000  0.00000  0.00000  385 GLU   K N   
17650 C CA  . GLU   K  385 ? 1.09668 1.09668 1.09668 0.00000  0.00000  0.00000  385 GLU   K CA  
17651 C C   . GLU   K  385 ? 1.09183 1.09183 1.09183 0.00000  0.00000  0.00000  385 GLU   K C   
17652 O O   . GLU   K  385 ? 1.06594 1.06594 1.06594 0.00000  0.00000  0.00000  385 GLU   K O   
17653 C CB  . GLU   K  385 ? 0.81728 0.81728 0.81728 0.00000  0.00000  0.00000  385 GLU   K CB  
17654 C CG  . GLU   K  385 ? 0.99206 0.99206 0.99206 0.00000  0.00000  -0.00000 385 GLU   K CG  
17655 C CD  . GLU   K  385 ? 1.20622 1.20622 1.20622 0.00000  0.00000  0.00000  385 GLU   K CD  
17656 O OE1 . GLU   K  385 ? 1.18582 1.18582 1.18582 0.00000  0.00000  -0.00000 385 GLU   K OE1 
17657 O OE2 . GLU   K  385 ? 1.02322 1.02322 1.02322 0.00000  0.00000  0.00000  385 GLU   K OE2 
17658 N N   . GLY   K  386 ? 1.09460 1.09460 1.09460 0.00000  0.00000  0.00000  386 GLY   K N   
17659 C CA  . GLY   K  386 ? 0.91927 0.91927 0.91927 0.00000  0.00000  0.00000  386 GLY   K CA  
17660 C C   . GLY   K  386 ? 1.15623 1.15623 1.15623 0.00000  -0.00000 0.00000  386 GLY   K C   
17661 O O   . GLY   K  386 ? 1.08764 1.08764 1.08764 0.00000  0.00000  0.00000  386 GLY   K O   
17662 N N   . GLN   K  387 ? 0.92528 0.92528 0.92528 0.00000  0.00000  0.00000  387 GLN   K N   
17663 C CA  . GLN   K  387 ? 0.88337 0.88337 0.88337 0.00000  0.00000  0.00000  387 GLN   K CA  
17664 C C   . GLN   K  387 ? 1.12698 1.12698 1.12698 0.00000  0.00000  0.00000  387 GLN   K C   
17665 O O   . GLN   K  387 ? 1.04006 1.04006 1.04006 0.00000  0.00000  0.00000  387 GLN   K O   
17666 C CB  . GLN   K  387 ? 0.86887 0.86887 0.86887 0.00000  0.00000  0.00000  387 GLN   K CB  
17667 C CG  . GLN   K  387 ? 0.87601 0.87601 0.87601 0.00000  0.00000  0.00000  387 GLN   K CG  
17668 C CD  . GLN   K  387 ? 0.97734 0.97734 0.97734 0.00000  0.00000  0.00000  387 GLN   K CD  
17669 O OE1 . GLN   K  387 ? 1.04020 1.04020 1.04020 0.00000  0.00000  0.00000  387 GLN   K OE1 
17670 N NE2 . GLN   K  387 ? 0.89350 0.89350 0.89350 -0.00000 0.00000  0.00000  387 GLN   K NE2 
17671 N N   . HIS   K  388 ? 0.82126 0.82126 0.82126 0.00000  0.00000  0.00000  388 HIS   K N   
17672 C CA  . HIS   K  388 ? 0.96430 0.96430 0.96430 -0.00000 0.00000  0.00000  388 HIS   K CA  
17673 C C   . HIS   K  388 ? 1.13717 1.13717 1.13717 -0.00000 0.00000  0.00000  388 HIS   K C   
17674 O O   . HIS   K  388 ? 0.80893 0.80893 0.80893 0.00000  0.00000  0.00000  388 HIS   K O   
17675 C CB  . HIS   K  388 ? 0.68588 0.68588 0.68588 -0.00000 0.00000  0.00000  388 HIS   K CB  
17676 C CG  . HIS   K  388 ? 0.90540 0.90540 0.90540 0.00000  0.00000  0.00000  388 HIS   K CG  
17677 N ND1 . HIS   K  388 ? 0.91754 0.91754 0.91754 0.00000  0.00000  0.00000  388 HIS   K ND1 
17678 C CD2 . HIS   K  388 ? 0.76521 0.76521 0.76521 -0.00000 0.00000  0.00000  388 HIS   K CD2 
17679 C CE1 . HIS   K  388 ? 0.87088 0.87088 0.87088 -0.00000 0.00000  0.00000  388 HIS   K CE1 
17680 N NE2 . HIS   K  388 ? 0.81947 0.81947 0.81947 0.00000  0.00000  0.00000  388 HIS   K NE2 
17681 N N   . VAL   K  389 ? 0.88651 0.88651 0.88651 0.00000  -0.00000 0.00000  389 VAL   K N   
17682 C CA  . VAL   K  389 ? 1.04360 1.04360 1.04360 0.00000  0.00000  0.00000  389 VAL   K CA  
17683 C C   . VAL   K  389 ? 1.03022 1.03022 1.03022 0.00000  0.00000  0.00000  389 VAL   K C   
17684 O O   . VAL   K  389 ? 1.20922 1.20922 1.20922 0.00000  0.00000  0.00000  389 VAL   K O   
17685 C CB  . VAL   K  389 ? 1.10929 1.10929 1.10929 -0.00000 0.00000  0.00000  389 VAL   K CB  
17686 C CG1 . VAL   K  389 ? 0.91676 0.91676 0.91676 -0.00000 0.00000  0.00000  389 VAL   K CG1 
17687 C CG2 . VAL   K  389 ? 0.84441 0.84441 0.84441 -0.00000 -0.00000 0.00000  389 VAL   K CG2 
17688 N N   . ASN   K  390 ? 0.96229 0.96229 0.96229 0.00000  0.00000  0.00000  390 ASN   K N   
17689 C CA  . ASN   K  390 ? 1.00616 1.00616 1.00616 0.00000  0.00000  0.00000  390 ASN   K CA  
17690 C C   . ASN   K  390 ? 1.32738 1.32738 1.32738 0.00000  0.00000  0.00000  390 ASN   K C   
17691 O O   . ASN   K  390 ? 1.04208 1.04208 1.04208 -0.00000 0.00000  0.00000  390 ASN   K O   
17692 C CB  . ASN   K  390 ? 1.16701 1.16701 1.16701 0.00000  0.00000  0.00000  390 ASN   K CB  
17693 C CG  . ASN   K  390 ? 1.08529 1.08529 1.08529 0.00000  0.00000  0.00000  390 ASN   K CG  
17694 O OD1 . ASN   K  390 ? 1.21808 1.21808 1.21808 0.00000  0.00000  0.00000  390 ASN   K OD1 
17695 N ND2 . ASN   K  390 ? 1.21115 1.21115 1.21115 -0.00000 0.00000  0.00000  390 ASN   K ND2 
17696 N N   . ARG   K  391 ? 1.03117 1.03117 1.03117 -0.00000 0.00000  0.00000  391 ARG   K N   
17697 C CA  . ARG   K  391 ? 1.16535 1.16535 1.16535 -0.00000 0.00000  0.00000  391 ARG   K CA  
17698 C C   . ARG   K  391 ? 1.01346 1.01346 1.01346 0.00000  0.00000  0.00000  391 ARG   K C   
17699 O O   . ARG   K  391 ? 1.14872 1.14872 1.14872 0.00000  0.00000  0.00000  391 ARG   K O   
17700 C CB  . ARG   K  391 ? 0.90416 0.90416 0.90416 0.00000  0.00000  -0.00000 391 ARG   K CB  
17701 C CG  . ARG   K  391 ? 1.02663 1.02663 1.02663 -0.00000 -0.00000 0.00000  391 ARG   K CG  
17702 C CD  . ARG   K  391 ? 1.14806 1.14806 1.14806 -0.00000 0.00000  0.00000  391 ARG   K CD  
17703 N NE  . ARG   K  391 ? 1.05130 1.05130 1.05130 0.00000  -0.00000 0.00000  391 ARG   K NE  
17704 C CZ  . ARG   K  391 ? 1.57779 1.57779 1.57779 0.00000  0.00000  -0.00000 391 ARG   K CZ  
17705 N NH1 . ARG   K  391 ? 1.06353 1.06353 1.06353 0.00000  0.00000  0.00000  391 ARG   K NH1 
17706 N NH2 . ARG   K  391 ? 1.07553 1.07553 1.07553 -0.00000 0.00000  0.00000  391 ARG   K NH2 
17707 N N   . GLY   K  392 ? 1.01310 1.01310 1.01310 -0.00000 0.00000  0.00000  392 GLY   K N   
17708 C CA  . GLY   K  392 ? 0.96786 0.96786 0.96786 0.00000  0.00000  0.00000  392 GLY   K CA  
17709 C C   . GLY   K  392 ? 1.07907 1.07907 1.07907 0.00000  0.00000  0.00000  392 GLY   K C   
17710 O O   . GLY   K  392 ? 1.06103 1.06103 1.06103 -0.00000 0.00000  0.00000  392 GLY   K O   
17711 N N   . ASP   K  393 ? 0.93580 0.93580 0.93580 0.00000  0.00000  0.00000  393 ASP   K N   
17712 C CA  . ASP   K  393 ? 1.09653 1.09653 1.09653 0.00000  0.00000  0.00000  393 ASP   K CA  
17713 C C   . ASP   K  393 ? 1.02757 1.02757 1.02757 0.00000  0.00000  0.00000  393 ASP   K C   
17714 O O   . ASP   K  393 ? 1.26890 1.26890 1.26890 -0.00000 0.00000  0.00000  393 ASP   K O   
17715 C CB  . ASP   K  393 ? 0.97798 0.97798 0.97798 0.00000  0.00000  0.00000  393 ASP   K CB  
17716 C CG  . ASP   K  393 ? 1.34384 1.34384 1.34384 0.00000  0.00000  0.00000  393 ASP   K CG  
17717 O OD1 . ASP   K  393 ? 1.30081 1.30081 1.30081 0.00000  0.00000  0.00000  393 ASP   K OD1 
17718 O OD2 . ASP   K  393 ? 1.15010 1.15010 1.15010 0.00000  -0.00000 0.00000  393 ASP   K OD2 
17719 N N   . ASP   K  394 ? 1.20388 1.20388 1.20388 0.00000  0.00000  0.00000  394 ASP   K N   
17720 C CA  . ASP   K  394 ? 0.89633 0.89633 0.89633 0.00000  0.00000  0.00000  394 ASP   K CA  
17721 C C   . ASP   K  394 ? 1.23427 1.23427 1.23427 0.00000  0.00000  0.00000  394 ASP   K C   
17722 O O   . ASP   K  394 ? 1.01674 1.01674 1.01674 -0.00000 0.00000  0.00000  394 ASP   K O   
17723 C CB  . ASP   K  394 ? 1.14328 1.14328 1.14328 0.00000  0.00000  0.00000  394 ASP   K CB  
17724 C CG  . ASP   K  394 ? 1.01032 1.01032 1.01032 -0.00000 0.00000  0.00000  394 ASP   K CG  
17725 O OD1 . ASP   K  394 ? 1.57213 1.57213 1.57213 -0.00000 0.00000  0.00000  394 ASP   K OD1 
17726 O OD2 . ASP   K  394 ? 1.51197 1.51197 1.51197 -0.00000 0.00000  0.00000  394 ASP   K OD2 
17727 N N   . LEU   K  395 ? 0.81381 0.81381 0.81381 0.00000  0.00000  0.00000  395 LEU   K N   
17728 C CA  . LEU   K  395 ? 1.05370 1.05370 1.05370 -0.00000 0.00000  0.00000  395 LEU   K CA  
17729 C C   . LEU   K  395 ? 0.96423 0.96423 0.96423 0.00000  0.00000  0.00000  395 LEU   K C   
17730 O O   . LEU   K  395 ? 0.93212 0.93212 0.93212 0.00000  0.00000  0.00000  395 LEU   K O   
17731 C CB  . LEU   K  395 ? 0.76835 0.76835 0.76835 0.00000  0.00000  0.00000  395 LEU   K CB  
17732 C CG  . LEU   K  395 ? 0.95168 0.95168 0.95168 -0.00000 -0.00000 0.00000  395 LEU   K CG  
17733 C CD1 . LEU   K  395 ? 0.76166 0.76166 0.76166 -0.00000 0.00000  0.00000  395 LEU   K CD1 
17734 C CD2 . LEU   K  395 ? 0.88870 0.88870 0.88870 0.00000  0.00000  0.00000  395 LEU   K CD2 
17735 N N   . GLY   K  396 ? 0.66000 0.66000 0.66000 0.00000  0.00000  0.00000  396 GLY   K N   
17736 C CA  . GLY   K  396 ? 0.76637 0.76637 0.76637 0.00000  0.00000  0.00000  396 GLY   K CA  
17737 C C   . GLY   K  396 ? 0.71783 0.71783 0.71783 0.00000  0.00000  0.00000  396 GLY   K C   
17738 O O   . GLY   K  396 ? 0.76154 0.76154 0.76154 0.00000  0.00000  0.00000  396 GLY   K O   
17739 N N   . MET   K  397 ? 0.74836 0.74836 0.74836 0.00000  0.00000  0.00000  397 MET   K N   
17740 C CA  . MET   K  397 ? 0.73414 0.73414 0.73414 0.00000  0.00000  0.00000  397 MET   K CA  
17741 C C   . MET   K  397 ? 0.93058 0.93058 0.93058 0.00000  0.00000  0.00000  397 MET   K C   
17742 O O   . MET   K  397 ? 0.79416 0.79416 0.79416 -0.00000 0.00000  0.00000  397 MET   K O   
17743 C CB  . MET   K  397 ? 0.70658 0.70658 0.70658 0.00000  0.00000  0.00000  397 MET   K CB  
17744 C CG  . MET   K  397 ? 0.76333 0.76333 0.76333 0.00000  0.00000  0.00000  397 MET   K CG  
17745 S SD  . MET   K  397 ? 0.89506 0.89506 0.89506 -0.00000 0.00000  0.00000  397 MET   K SD  
17746 C CE  . MET   K  397 ? 0.61954 0.61954 0.61954 0.00000  -0.00000 0.00000  397 MET   K CE  
17747 N N   . PHE   K  398 ? 0.61065 0.61065 0.61065 -0.00000 0.00000  0.00000  398 PHE   K N   
17748 C CA  . PHE   K  398 ? 0.52557 0.52557 0.52557 -0.00000 0.00000  0.00000  398 PHE   K CA  
17749 C C   . PHE   K  398 ? 0.64942 0.64942 0.64942 0.00000  -0.00000 0.00000  398 PHE   K C   
17750 O O   . PHE   K  398 ? 0.77241 0.77241 0.77241 0.00000  0.00000  0.00000  398 PHE   K O   
17751 C CB  . PHE   K  398 ? 0.52660 0.52660 0.52660 0.00000  0.00000  0.00000  398 PHE   K CB  
17752 C CG  . PHE   K  398 ? 0.69943 0.69943 0.69943 0.00000  0.00000  0.00000  398 PHE   K CG  
17753 C CD1 . PHE   K  398 ? 0.53058 0.53058 0.53058 0.00000  0.00000  0.00000  398 PHE   K CD1 
17754 C CD2 . PHE   K  398 ? 0.61617 0.61617 0.61617 -0.00000 0.00000  0.00000  398 PHE   K CD2 
17755 C CE1 . PHE   K  398 ? 0.68307 0.68307 0.68307 -0.00000 0.00000  0.00000  398 PHE   K CE1 
17756 C CE2 . PHE   K  398 ? 0.56608 0.56608 0.56608 0.00000  0.00000  0.00000  398 PHE   K CE2 
17757 C CZ  . PHE   K  398 ? 0.65899 0.65899 0.65899 0.00000  0.00000  0.00000  398 PHE   K CZ  
17758 N N   . HIS   K  399 ? 0.70020 0.70020 0.70020 0.00000  0.00000  0.00000  399 HIS   K N   
17759 C CA  . HIS   K  399 ? 0.80651 0.80651 0.80651 0.00000  0.00000  0.00000  399 HIS   K CA  
17760 C C   . HIS   K  399 ? 0.53369 0.53369 0.53369 0.00000  0.00000  0.00000  399 HIS   K C   
17761 O O   . HIS   K  399 ? 0.89337 0.89337 0.89337 0.00000  0.00000  0.00000  399 HIS   K O   
17762 C CB  . HIS   K  399 ? 0.50204 0.50204 0.50204 0.00000  0.00000  0.00000  399 HIS   K CB  
17763 C CG  . HIS   K  399 ? 0.54958 0.54958 0.54958 -0.00000 0.00000  0.00000  399 HIS   K CG  
17764 N ND1 . HIS   K  399 ? 0.65147 0.65147 0.65147 0.00000  0.00000  0.00000  399 HIS   K ND1 
17765 C CD2 . HIS   K  399 ? 0.74498 0.74498 0.74498 -0.00000 0.00000  0.00000  399 HIS   K CD2 
17766 C CE1 . HIS   K  399 ? 0.87505 0.87505 0.87505 0.00000  0.00000  0.00000  399 HIS   K CE1 
17767 N NE2 . HIS   K  399 ? 0.51043 0.51043 0.51043 0.00000  0.00000  -0.00000 399 HIS   K NE2 
17768 N N   . PHE   K  400 ? 0.71491 0.71491 0.71491 -0.00000 0.00000  0.00000  400 PHE   K N   
17769 C CA  . PHE   K  400 ? 0.48022 0.48022 0.48022 -0.00000 0.00000  0.00000  400 PHE   K CA  
17770 C C   . PHE   K  400 ? 0.58953 0.58953 0.58953 0.00000  0.00000  0.00000  400 PHE   K C   
17771 O O   . PHE   K  400 ? 0.72238 0.72238 0.72238 0.00000  0.00000  0.00000  400 PHE   K O   
17772 C CB  . PHE   K  400 ? 0.70411 0.70411 0.70411 -0.00000 -0.00000 0.00000  400 PHE   K CB  
17773 C CG  . PHE   K  400 ? 0.44988 0.44988 0.44988 -0.00000 0.00000  0.00000  400 PHE   K CG  
17774 C CD1 . PHE   K  400 ? 0.69108 0.69108 0.69108 -0.00000 0.00000  0.00000  400 PHE   K CD1 
17775 C CD2 . PHE   K  400 ? 0.70366 0.70366 0.70366 0.00000  0.00000  0.00000  400 PHE   K CD2 
17776 C CE1 . PHE   K  400 ? 0.49690 0.49690 0.49690 0.00000  0.00000  0.00000  400 PHE   K CE1 
17777 C CE2 . PHE   K  400 ? 0.65104 0.65104 0.65104 -0.00000 0.00000  0.00000  400 PHE   K CE2 
17778 C CZ  . PHE   K  400 ? 0.68796 0.68796 0.68796 0.00000  0.00000  0.00000  400 PHE   K CZ  
17779 N N   . GLY   K  401 ? 0.47501 0.47501 0.47501 -0.00000 0.00000  -0.00000 401 GLY   K N   
17780 C CA  . GLY   K  401 ? 0.42344 0.42344 0.42344 0.00000  0.00000  0.00000  401 GLY   K CA  
17781 C C   . GLY   K  401 ? 0.55591 0.55591 0.55591 -0.00000 0.00000  0.00000  401 GLY   K C   
17782 O O   . GLY   K  401 ? 0.63434 0.63434 0.63434 0.00000  0.00000  0.00000  401 GLY   K O   
17783 N N   . GLY   K  402 ? 0.46990 0.46990 0.46990 0.00000  0.00000  0.00000  402 GLY   K N   
17784 C CA  . GLY   K  402 ? 0.37625 0.37625 0.37625 0.00000  0.00000  0.00000  402 GLY   K CA  
17785 C C   . GLY   K  402 ? 0.74655 0.74655 0.74655 0.00000  0.00000  0.00000  402 GLY   K C   
17786 O O   . GLY   K  402 ? 0.51374 0.51374 0.51374 0.00000  0.00000  0.00000  402 GLY   K O   
17787 O OXT . GLY   K  402 ? 0.63005 0.63005 0.63005 -0.00000 0.00000  0.00000  402 GLY   K OXT 
17788 N N   . SER   L  1   ? 0.42611 0.42611 0.42611 0.00000  0.00000  0.00000  404 SER   L N   
17789 C CA  . SER   L  1   ? 0.36430 0.36430 0.36430 0.00000  0.00000  0.00000  404 SER   L CA  
17790 C C   . SER   L  1   ? 0.50901 0.50901 0.50901 0.00000  0.00000  0.00000  404 SER   L C   
17791 O O   . SER   L  1   ? 0.55353 0.55353 0.55353 0.00000  0.00000  0.00000  404 SER   L O   
17792 C CB  . SER   L  1   ? 0.44378 0.44378 0.44378 0.00000  0.00000  0.00000  404 SER   L CB  
17793 O OG  . SER   L  1   ? 0.47846 0.47846 0.47846 0.00000  0.00000  0.00000  404 SER   L OG  
17794 N N   . PHE   L  2   ? 0.51185 0.51185 0.51185 -0.00000 0.00000  0.00000  405 PHE   L N   
17795 C CA  . PHE   L  2   ? 0.59132 0.59132 0.59132 0.00000  0.00000  0.00000  405 PHE   L CA  
17796 C C   . PHE   L  2   ? 0.56182 0.56182 0.56182 0.00000  0.00000  0.00000  405 PHE   L C   
17797 O O   . PHE   L  2   ? 0.67958 0.67958 0.67958 0.00000  0.00000  0.00000  405 PHE   L O   
17798 C CB  . PHE   L  2   ? 0.59994 0.59994 0.59994 -0.00000 -0.00000 0.00000  405 PHE   L CB  
17799 C CG  . PHE   L  2   ? 0.63126 0.63126 0.63126 -0.00000 -0.00000 -0.00000 405 PHE   L CG  
17800 C CD1 . PHE   L  2   ? 0.71096 0.71096 0.71096 -0.00000 0.00000  0.00000  405 PHE   L CD1 
17801 C CD2 . PHE   L  2   ? 0.67476 0.67476 0.67476 0.00000  0.00000  0.00000  405 PHE   L CD2 
17802 C CE1 . PHE   L  2   ? 0.63153 0.63153 0.63153 0.00000  0.00000  0.00000  405 PHE   L CE1 
17803 C CE2 . PHE   L  2   ? 0.58261 0.58261 0.58261 -0.00000 0.00000  0.00000  405 PHE   L CE2 
17804 C CZ  . PHE   L  2   ? 0.66098 0.66098 0.66098 0.00000  0.00000  0.00000  405 PHE   L CZ  
17805 N N   . ALA   L  3   ? 0.47324 0.47324 0.47324 -0.00000 0.00000  0.00000  406 ALA   L N   
17806 C CA  . ALA   L  3   ? 0.52710 0.52710 0.52710 0.00000  0.00000  0.00000  406 ALA   L CA  
17807 C C   . ALA   L  3   ? 0.56687 0.56687 0.56687 0.00000  0.00000  0.00000  406 ALA   L C   
17808 O O   . ALA   L  3   ? 0.55304 0.55304 0.55304 0.00000  0.00000  0.00000  406 ALA   L O   
17809 C CB  . ALA   L  3   ? 0.32192 0.32192 0.32192 0.00000  -0.00000 0.00000  406 ALA   L CB  
17810 N N   . LEU   L  4   ? 0.74822 0.74822 0.74822 0.00000  0.00000  0.00000  407 LEU   L N   
17811 C CA  . LEU   L  4   ? 0.73907 0.73907 0.73907 0.00000  0.00000  0.00000  407 LEU   L CA  
17812 C C   . LEU   L  4   ? 0.55186 0.55186 0.55186 0.00000  -0.00000 0.00000  407 LEU   L C   
17813 O O   . LEU   L  4   ? 0.79956 0.79956 0.79956 0.00000  0.00000  0.00000  407 LEU   L O   
17814 C CB  . LEU   L  4   ? 0.59910 0.59910 0.59910 0.00000  0.00000  0.00000  407 LEU   L CB  
17815 C CG  . LEU   L  4   ? 0.74765 0.74765 0.74765 0.00000  0.00000  0.00000  407 LEU   L CG  
17816 C CD1 . LEU   L  4   ? 0.57533 0.57533 0.57533 -0.00000 0.00000  0.00000  407 LEU   L CD1 
17817 C CD2 . LEU   L  4   ? 0.65066 0.65066 0.65066 0.00000  0.00000  0.00000  407 LEU   L CD2 
17818 N N   . GLY   L  5   ? 0.85537 0.85537 0.85537 -0.00000 0.00000  0.00000  408 GLY   L N   
17819 C CA  . GLY   L  5   ? 0.56043 0.56043 0.56043 0.00000  0.00000  0.00000  408 GLY   L CA  
17820 C C   . GLY   L  5   ? 0.75705 0.75705 0.75705 0.00000  0.00000  0.00000  408 GLY   L C   
17821 O O   . GLY   L  5   ? 0.83715 0.83715 0.83715 0.00000  0.00000  0.00000  408 GLY   L O   
17822 N N   . LEU   L  6   ? 0.67224 0.67224 0.67224 -0.00000 0.00000  0.00000  409 LEU   L N   
17823 C CA  . LEU   L  6   ? 0.91738 0.91738 0.91738 0.00000  0.00000  0.00000  409 LEU   L CA  
17824 C C   . LEU   L  6   ? 0.83374 0.83374 0.83374 0.00000  0.00000  0.00000  409 LEU   L C   
17825 O O   . LEU   L  6   ? 0.89790 0.89790 0.89790 0.00000  0.00000  0.00000  409 LEU   L O   
17826 C CB  . LEU   L  6   ? 0.80696 0.80696 0.80696 -0.00000 0.00000  0.00000  409 LEU   L CB  
17827 C CG  . LEU   L  6   ? 0.89404 0.89404 0.89404 0.00000  0.00000  0.00000  409 LEU   L CG  
17828 C CD1 . LEU   L  6   ? 0.71777 0.71777 0.71777 0.00000  -0.00000 -0.00000 409 LEU   L CD1 
17829 C CD2 . LEU   L  6   ? 0.66143 0.66143 0.66143 -0.00000 0.00000  0.00000  409 LEU   L CD2 
17830 N N   . ARG   L  7   ? 0.84226 0.84226 0.84226 0.00000  0.00000  0.00000  410 ARG   L N   
17831 C CA  . ARG   L  7   ? 0.82614 0.82614 0.82614 -0.00000 0.00000  0.00000  410 ARG   L CA  
17832 C C   . ARG   L  7   ? 0.90085 0.90085 0.90085 0.00000  0.00000  0.00000  410 ARG   L C   
17833 O O   . ARG   L  7   ? 1.04349 1.04349 1.04349 0.00000  -0.00000 0.00000  410 ARG   L O   
17834 C CB  . ARG   L  7   ? 0.65959 0.65959 0.65959 0.00000  0.00000  0.00000  410 ARG   L CB  
17835 C CG  . ARG   L  7   ? 0.68502 0.68502 0.68502 0.00000  0.00000  0.00000  410 ARG   L CG  
17836 C CD  . ARG   L  7   ? 0.82745 0.82745 0.82745 0.00000  0.00000  0.00000  410 ARG   L CD  
17837 N NE  . ARG   L  7   ? 1.06927 1.06927 1.06927 0.00000  0.00000  0.00000  410 ARG   L NE  
17838 C CZ  . ARG   L  7   ? 0.95351 0.95351 0.95351 0.00000  0.00000  0.00000  410 ARG   L CZ  
17839 N NH1 . ARG   L  7   ? 0.99612 0.99612 0.99612 0.00000  0.00000  0.00000  410 ARG   L NH1 
17840 N NH2 . ARG   L  7   ? 1.07038 1.07038 1.07038 0.00000  -0.00000 0.00000  410 ARG   L NH2 
17841 N N   . LYS   L  8   ? 0.92377 0.92377 0.92377 0.00000  0.00000  0.00000  411 LYS   L N   
17842 C CA  . LYS   L  8   ? 1.15251 1.15251 1.15251 0.00000  0.00000  0.00000  411 LYS   L CA  
17843 C C   . LYS   L  8   ? 1.05404 1.05404 1.05404 -0.00000 0.00000  0.00000  411 LYS   L C   
17844 O O   . LYS   L  8   ? 1.01493 1.01493 1.01493 0.00000  0.00000  0.00000  411 LYS   L O   
17845 C CB  . LYS   L  8   ? 0.79941 0.79941 0.79941 0.00000  0.00000  0.00000  411 LYS   L CB  
17846 N N   . ASP   L  9   ? 0.89525 0.89525 0.89525 -0.00000 -0.00000 -0.00000 412 ASP   L N   
17847 C CA  . ASP   L  9   ? 1.54660 1.54660 1.54660 0.00000  0.00000  0.00000  412 ASP   L CA  
17848 C C   . ASP   L  9   ? 0.98068 0.98068 0.98068 0.00000  0.00000  0.00000  412 ASP   L C   
17849 O O   . ASP   L  9   ? 1.36795 1.36795 1.36795 0.00000  -0.00000 -0.00000 412 ASP   L O   
17850 C CB  . ASP   L  9   ? 1.21168 1.21168 1.21168 -0.00000 -0.00000 0.00000  412 ASP   L CB  
17851 C CG  . ASP   L  9   ? 1.33115 1.33115 1.33115 0.00000  0.00000  0.00000  412 ASP   L CG  
17852 O OD1 . ASP   L  9   ? 1.36395 1.36395 1.36395 0.00000  0.00000  0.00000  412 ASP   L OD1 
17853 O OD2 . ASP   L  9   ? 1.65096 1.65096 1.65096 0.00000  0.00000  0.00000  412 ASP   L OD2 
17854 N N   . CYS   L  10  ? 1.30059 1.30059 1.30059 0.00000  0.00000  0.00000  413 CYS   L N   
17855 C CA  . CYS   L  10  ? 1.00831 1.00831 1.00831 0.00000  0.00000  0.00000  413 CYS   L CA  
17856 C C   . CYS   L  10  ? 1.14190 1.14190 1.14190 0.00000  0.00000  0.00000  413 CYS   L C   
17857 O O   . CYS   L  10  ? 1.11662 1.11662 1.11662 0.00000  0.00000  0.00000  413 CYS   L O   
17858 C CB  . CYS   L  10  ? 0.90050 0.90050 0.90050 0.00000  0.00000  0.00000  413 CYS   L CB  
17859 S SG  . CYS   L  10  ? 1.05091 1.05091 1.05091 -0.00000 0.00000  0.00000  413 CYS   L SG  
17860 N N   . ARG   L  11  ? 1.04380 1.04380 1.04380 0.00000  0.00000  0.00000  414 ARG   L N   
17861 C CA  . ARG   L  11  ? 1.32706 1.32706 1.32706 0.00000  0.00000  0.00000  414 ARG   L CA  
17862 C C   . ARG   L  11  ? 1.47056 1.47056 1.47056 0.00000  0.00000  0.00000  414 ARG   L C   
17863 O O   . ARG   L  11  ? 1.12282 1.12282 1.12282 0.00000  0.00000  0.00000  414 ARG   L O   
17864 C CB  . ARG   L  11  ? 0.96800 0.96800 0.96800 0.00000  0.00000  0.00000  414 ARG   L CB  
17865 N N   . ALA   L  12  ? 1.18139 1.18139 1.18139 0.00000  0.00000  0.00000  415 ALA   L N   
17866 C CA  . ALA   L  12  ? 1.04081 1.04081 1.04081 0.00000  0.00000  0.00000  415 ALA   L CA  
17867 C C   . ALA   L  12  ? 0.96329 0.96329 0.96329 -0.00000 0.00000  0.00000  415 ALA   L C   
17868 O O   . ALA   L  12  ? 1.31348 1.31348 1.31348 0.00000  0.00000  0.00000  415 ALA   L O   
17869 C CB  . ALA   L  12  ? 0.78343 0.78343 0.78343 -0.00000 0.00000  0.00000  415 ALA   L CB  
17870 N N   . GLU   L  13  ? 0.67359 0.67359 0.67359 0.00000  0.00000  0.00000  416 GLU   L N   
17871 C CA  . GLU   L  13  ? 0.84689 0.84689 0.84689 0.00000  0.00000  0.00000  416 GLU   L CA  
17872 C C   . GLU   L  13  ? 0.87602 0.87602 0.87602 0.00000  0.00000  0.00000  416 GLU   L C   
17873 O O   . GLU   L  13  ? 0.94148 0.94148 0.94148 0.00000  0.00000  0.00000  416 GLU   L O   
17874 C CB  . GLU   L  13  ? 0.71110 0.71110 0.71110 0.00000  0.00000  0.00000  416 GLU   L CB  
17875 N N   . ILE   L  14  ? 0.84043 0.84043 0.84043 0.00000  0.00000  0.00000  417 ILE   L N   
17876 C CA  . ILE   L  14  ? 0.93828 0.93828 0.93828 0.00000  0.00000  0.00000  417 ILE   L CA  
17877 C C   . ILE   L  14  ? 0.81342 0.81342 0.81342 0.00000  0.00000  0.00000  417 ILE   L C   
17878 O O   . ILE   L  14  ? 0.91903 0.91903 0.91903 0.00000  0.00000  0.00000  417 ILE   L O   
17879 C CB  . ILE   L  14  ? 0.68956 0.68956 0.68956 0.00000  0.00000  0.00000  417 ILE   L CB  
17880 C CG1 . ILE   L  14  ? 0.73225 0.73225 0.73225 0.00000  0.00000  0.00000  417 ILE   L CG1 
17881 C CG2 . ILE   L  14  ? 0.77844 0.77844 0.77844 0.00000  0.00000  0.00000  417 ILE   L CG2 
17882 C CD1 . ILE   L  14  ? 0.85975 0.85975 0.85975 0.00000  0.00000  0.00000  417 ILE   L CD1 
17883 N N   . VAL   L  15  ? 0.93269 0.93269 0.93269 0.00000  0.00000  0.00000  418 VAL   L N   
17884 C CA  . VAL   L  15  ? 0.70091 0.70091 0.70091 0.00000  0.00000  0.00000  418 VAL   L CA  
17885 C C   . VAL   L  15  ? 0.74898 0.74898 0.74898 0.00000  0.00000  0.00000  418 VAL   L C   
17886 O O   . VAL   L  15  ? 1.00360 1.00360 1.00360 -0.00000 0.00000  0.00000  418 VAL   L O   
17887 C CB  . VAL   L  15  ? 0.99682 0.99682 0.99682 0.00000  0.00000  0.00000  418 VAL   L CB  
17888 C CG1 . VAL   L  15  ? 0.59550 0.59550 0.59550 -0.00000 0.00000  0.00000  418 VAL   L CG1 
17889 C CG2 . VAL   L  15  ? 0.57356 0.57356 0.57356 0.00000  0.00000  0.00000  418 VAL   L CG2 
17890 N N   . GLU   L  16  ? 0.83894 0.83894 0.83894 0.00000  0.00000  0.00000  419 GLU   L N   
17891 C CA  . GLU   L  16  ? 0.70559 0.70559 0.70559 -0.00000 0.00000  0.00000  419 GLU   L CA  
17892 C C   . GLU   L  16  ? 0.83783 0.83783 0.83783 0.00000  0.00000  0.00000  419 GLU   L C   
17893 O O   . GLU   L  16  ? 0.83935 0.83935 0.83935 0.00000  0.00000  0.00000  419 GLU   L O   
17894 C CB  . GLU   L  16  ? 0.71437 0.71437 0.71437 0.00000  0.00000  0.00000  419 GLU   L CB  
17895 C CG  . GLU   L  16  ? 2.03964 2.03964 2.03964 -0.00000 0.00000  0.00000  419 GLU   L CG  
17896 C CD  . GLU   L  16  ? 2.20495 2.20495 2.20495 0.00000  0.00000  0.00000  419 GLU   L CD  
17897 O OE1 . GLU   L  16  ? 2.16437 2.16437 2.16437 -0.00000 0.00000  0.00000  419 GLU   L OE1 
17898 O OE2 . GLU   L  16  ? 2.34289 2.34289 2.34289 0.00000  0.00000  0.00000  419 GLU   L OE2 
17899 N N   . LYS   L  17  ? 0.78332 0.78332 0.78332 0.00000  0.00000  0.00000  420 LYS   L N   
17900 C CA  . LYS   L  17  ? 0.81190 0.81190 0.81190 0.00000  0.00000  0.00000  420 LYS   L CA  
17901 C C   . LYS   L  17  ? 0.89446 0.89446 0.89446 -0.00000 0.00000  0.00000  420 LYS   L C   
17902 O O   . LYS   L  17  ? 0.87421 0.87421 0.87421 0.00000  0.00000  0.00000  420 LYS   L O   
17903 C CB  . LYS   L  17  ? 0.58993 0.58993 0.58993 -0.00000 0.00000  0.00000  420 LYS   L CB  
17904 C CG  . LYS   L  17  ? 0.65326 0.65326 0.65326 0.00000  0.00000  0.00000  420 LYS   L CG  
17905 C CD  . LYS   L  17  ? 0.92096 0.92096 0.92096 0.00000  0.00000  0.00000  420 LYS   L CD  
17906 C CE  . LYS   L  17  ? 1.04503 1.04503 1.04503 0.00000  0.00000  0.00000  420 LYS   L CE  
17907 N NZ  . LYS   L  17  ? 1.33500 1.33500 1.33500 -0.00000 0.00000  0.00000  420 LYS   L NZ  
17908 N N   . PHE   L  18  ? 0.90314 0.90314 0.90314 0.00000  0.00000  0.00000  421 PHE   L N   
17909 C CA  . PHE   L  18  ? 1.20302 1.20302 1.20302 -0.00000 0.00000  0.00000  421 PHE   L CA  
17910 C C   . PHE   L  18  ? 1.04100 1.04100 1.04100 -0.00000 0.00000  0.00000  421 PHE   L C   
17911 O O   . PHE   L  18  ? 0.97405 0.97405 0.97405 -0.00000 0.00000  0.00000  421 PHE   L O   
17912 C CB  . PHE   L  18  ? 0.76162 0.76162 0.76162 -0.00000 0.00000  0.00000  421 PHE   L CB  
17913 C CG  . PHE   L  18  ? 0.90385 0.90385 0.90385 -0.00000 0.00000  0.00000  421 PHE   L CG  
17914 C CD1 . PHE   L  18  ? 0.89675 0.89675 0.89675 0.00000  0.00000  0.00000  421 PHE   L CD1 
17915 C CD2 . PHE   L  18  ? 1.11695 1.11695 1.11695 -0.00000 0.00000  0.00000  421 PHE   L CD2 
17916 C CE1 . PHE   L  18  ? 0.79941 0.79941 0.79941 0.00000  0.00000  0.00000  421 PHE   L CE1 
17917 C CE2 . PHE   L  18  ? 0.99518 0.99518 0.99518 -0.00000 0.00000  0.00000  421 PHE   L CE2 
17918 C CZ  . PHE   L  18  ? 1.06702 1.06702 1.06702 0.00000  0.00000  0.00000  421 PHE   L CZ  
17919 N N   . THR   L  19  ? 0.78793 0.78793 0.78793 0.00000  -0.00000 0.00000  422 THR   L N   
17920 C CA  . THR   L  19  ? 0.66409 0.66409 0.66409 0.00000  0.00000  0.00000  422 THR   L CA  
17921 C C   . THR   L  19  ? 0.76602 0.76602 0.76602 0.00000  0.00000  0.00000  422 THR   L C   
17922 O O   . THR   L  19  ? 0.74240 0.74240 0.74240 -0.00000 0.00000  0.00000  422 THR   L O   
17923 C CB  . THR   L  19  ? 0.81132 0.81132 0.81132 0.00000  -0.00000 0.00000  422 THR   L CB  
17924 O OG1 . THR   L  19  ? 0.76324 0.76324 0.76324 -0.00000 0.00000  0.00000  422 THR   L OG1 
17925 C CG2 . THR   L  19  ? 0.83565 0.83565 0.83565 0.00000  0.00000  0.00000  422 THR   L CG2 
17926 N N   . GLU   L  20  ? 0.87028 0.87028 0.87028 0.00000  0.00000  0.00000  423 GLU   L N   
17927 C CA  . GLU   L  20  ? 0.84862 0.84862 0.84862 0.00000  0.00000  0.00000  423 GLU   L CA  
17928 C C   . GLU   L  20  ? 0.72766 0.72766 0.72766 0.00000  0.00000  0.00000  423 GLU   L C   
17929 O O   . GLU   L  20  ? 0.92743 0.92743 0.92743 -0.00000 -0.00000 0.00000  423 GLU   L O   
17930 C CB  . GLU   L  20  ? 0.67478 0.67478 0.67478 0.00000  0.00000  0.00000  423 GLU   L CB  
17931 N N   . PRO   L  21  ? 0.74156 0.74156 0.74156 0.00000  0.00000  0.00000  424 PRO   L N   
17932 C CA  . PRO   L  21  ? 0.91178 0.91178 0.91178 -0.00000 0.00000  0.00000  424 PRO   L CA  
17933 C C   . PRO   L  21  ? 0.72959 0.72959 0.72959 0.00000  0.00000  0.00000  424 PRO   L C   
17934 O O   . PRO   L  21  ? 0.83974 0.83974 0.83974 0.00000  0.00000  -0.00000 424 PRO   L O   
17935 C CB  . PRO   L  21  ? 0.51290 0.51290 0.51290 0.00000  0.00000  0.00000  424 PRO   L CB  
17936 C CG  . PRO   L  21  ? 0.70438 0.70438 0.70438 -0.00000 0.00000  0.00000  424 PRO   L CG  
17937 C CD  . PRO   L  21  ? 0.68781 0.68781 0.68781 0.00000  0.00000  0.00000  424 PRO   L CD  
17938 N N   . GLY   L  22  ? 0.80397 0.80397 0.80397 -0.00000 0.00000  0.00000  425 GLY   L N   
17939 C CA  . GLY   L  22  ? 0.58458 0.58458 0.58458 -0.00000 0.00000  0.00000  425 GLY   L CA  
17940 C C   . GLY   L  22  ? 0.69400 0.69400 0.69400 0.00000  0.00000  0.00000  425 GLY   L C   
17941 O O   . GLY   L  22  ? 0.76845 0.76845 0.76845 0.00000  0.00000  0.00000  425 GLY   L O   
17942 N N   . THR   L  23  ? 0.78288 0.78288 0.78288 0.00000  0.00000  0.00000  426 THR   L N   
17943 C CA  . THR   L  23  ? 0.75335 0.75335 0.75335 -0.00000 0.00000  0.00000  426 THR   L CA  
17944 C C   . THR   L  23  ? 0.75301 0.75301 0.75301 -0.00000 0.00000  0.00000  426 THR   L C   
17945 O O   . THR   L  23  ? 1.12373 1.12373 1.12373 -0.00000 -0.00000 0.00000  426 THR   L O   
17946 C CB  . THR   L  23  ? 0.86318 0.86318 0.86318 -0.00000 0.00000  0.00000  426 THR   L CB  
17947 O OG1 . THR   L  23  ? 0.96829 0.96829 0.96829 -0.00000 0.00000  0.00000  426 THR   L OG1 
17948 C CG2 . THR   L  23  ? 0.74210 0.74210 0.74210 0.00000  0.00000  0.00000  426 THR   L CG2 
17949 N N   . VAL   L  24  ? 1.04485 1.04485 1.04485 0.00000  0.00000  0.00000  427 VAL   L N   
17950 C CA  . VAL   L  24  ? 0.80629 0.80629 0.80629 0.00000  0.00000  0.00000  427 VAL   L CA  
17951 C C   . VAL   L  24  ? 0.73607 0.73607 0.73607 -0.00000 0.00000  0.00000  427 VAL   L C   
17952 O O   . VAL   L  24  ? 1.05086 1.05086 1.05086 0.00000  0.00000  0.00000  427 VAL   L O   
17953 C CB  . VAL   L  24  ? 0.71597 0.71597 0.71597 0.00000  0.00000  0.00000  427 VAL   L CB  
17954 C CG1 . VAL   L  24  ? 0.62401 0.62401 0.62401 0.00000  0.00000  0.00000  427 VAL   L CG1 
17955 C CG2 . VAL   L  24  ? 0.71529 0.71529 0.71529 0.00000  0.00000  0.00000  427 VAL   L CG2 
17956 N N   . ILE   L  25  ? 1.13052 1.13052 1.13052 0.00000  0.00000  0.00000  428 ILE   L N   
17957 C CA  . ILE   L  25  ? 0.73659 0.73659 0.73659 0.00000  -0.00000 0.00000  428 ILE   L CA  
17958 C C   . ILE   L  25  ? 1.00778 1.00778 1.00778 -0.00000 0.00000  0.00000  428 ILE   L C   
17959 O O   . ILE   L  25  ? 0.89760 0.89760 0.89760 -0.00000 0.00000  0.00000  428 ILE   L O   
17960 C CB  . ILE   L  25  ? 0.96971 0.96971 0.96971 -0.00000 0.00000  0.00000  428 ILE   L CB  
17961 C CG1 . ILE   L  25  ? 0.85406 0.85406 0.85406 0.00000  0.00000  0.00000  428 ILE   L CG1 
17962 C CG2 . ILE   L  25  ? 0.70162 0.70162 0.70162 0.00000  0.00000  0.00000  428 ILE   L CG2 
17963 C CD1 . ILE   L  25  ? 0.78603 0.78603 0.78603 0.00000  0.00000  0.00000  428 ILE   L CD1 
17964 N N   . ARG   L  26  ? 0.88001 0.88001 0.88001 -0.00000 0.00000  0.00000  429 ARG   L N   
17965 C CA  . ARG   L  26  ? 0.86496 0.86496 0.86496 0.00000  0.00000  0.00000  429 ARG   L CA  
17966 C C   . ARG   L  26  ? 0.87168 0.87168 0.87168 0.00000  0.00000  0.00000  429 ARG   L C   
17967 O O   . ARG   L  26  ? 0.85952 0.85952 0.85952 -0.00000 0.00000  0.00000  429 ARG   L O   
17968 C CB  . ARG   L  26  ? 0.96647 0.96647 0.96647 -0.00000 0.00000  0.00000  429 ARG   L CB  
17969 C CG  . ARG   L  26  ? 0.88767 0.88767 0.88767 -0.00000 0.00000  0.00000  429 ARG   L CG  
17970 C CD  . ARG   L  26  ? 1.06020 1.06020 1.06020 -0.00000 0.00000  0.00000  429 ARG   L CD  
17971 N NE  . ARG   L  26  ? 0.88014 0.88014 0.88014 -0.00000 0.00000  0.00000  429 ARG   L NE  
17972 C CZ  . ARG   L  26  ? 2.55832 2.55832 2.55832 0.00000  0.00000  0.00000  429 ARG   L CZ  
17973 N NH1 . ARG   L  26  ? 0.82489 0.82489 0.82489 0.00000  0.00000  0.00000  429 ARG   L NH1 
17974 N NH2 . ARG   L  26  ? 0.91135 0.91135 0.91135 0.00000  -0.00000 0.00000  429 ARG   L NH2 
17975 N N   . ILE   L  27  ? 0.77027 0.77027 0.77027 -0.00000 -0.00000 0.00000  430 ILE   L N   
17976 C CA  . ILE   L  27  ? 0.99056 0.99056 0.99056 -0.00000 0.00000  0.00000  430 ILE   L CA  
17977 C C   . ILE   L  27  ? 0.83391 0.83391 0.83391 0.00000  0.00000  0.00000  430 ILE   L C   
17978 O O   . ILE   L  27  ? 1.17336 1.17336 1.17336 0.00000  -0.00000 0.00000  430 ILE   L O   
17979 C CB  . ILE   L  27  ? 0.90829 0.90829 0.90829 0.00000  0.00000  0.00000  430 ILE   L CB  
17980 C CG1 . ILE   L  27  ? 0.83843 0.83843 0.83843 0.00000  0.00000  0.00000  430 ILE   L CG1 
17981 C CG2 . ILE   L  27  ? 0.88441 0.88441 0.88441 -0.00000 0.00000  0.00000  430 ILE   L CG2 
17982 C CD1 . ILE   L  27  ? 0.80276 0.80276 0.80276 -0.00000 0.00000  0.00000  430 ILE   L CD1 
17983 N N   . ASN   L  28  ? 1.31044 1.31044 1.31044 -0.00000 0.00000  0.00000  431 ASN   L N   
17984 C CA  . ASN   L  28  ? 1.05019 1.05019 1.05019 0.00000  0.00000  0.00000  431 ASN   L CA  
17985 C C   . ASN   L  28  ? 1.19670 1.19670 1.19670 0.00000  0.00000  0.00000  431 ASN   L C   
17986 O O   . ASN   L  28  ? 1.07696 1.07696 1.07696 -0.00000 0.00000  0.00000  431 ASN   L O   
17987 C CB  . ASN   L  28  ? 0.99535 0.99535 0.99535 0.00000  0.00000  0.00000  431 ASN   L CB  
17988 C CG  . ASN   L  28  ? 1.14618 1.14618 1.14618 0.00000  0.00000  0.00000  431 ASN   L CG  
17989 O OD1 . ASN   L  28  ? 1.20888 1.20888 1.20888 0.00000  0.00000  0.00000  431 ASN   L OD1 
17990 N ND2 . ASN   L  28  ? 1.04673 1.04673 1.04673 -0.00000 0.00000  0.00000  431 ASN   L ND2 
17991 N N   . GLU   L  29  ? 0.86722 0.86722 0.86722 0.00000  0.00000  0.00000  432 GLU   L N   
17992 C CA  . GLU   L  29  ? 0.97672 0.97672 0.97672 0.00000  0.00000  0.00000  432 GLU   L CA  
17993 C C   . GLU   L  29  ? 0.92324 0.92324 0.92324 -0.00000 0.00000  0.00000  432 GLU   L C   
17994 O O   . GLU   L  29  ? 1.11907 1.11907 1.11907 -0.00000 0.00000  0.00000  432 GLU   L O   
17995 C CB  . GLU   L  29  ? 0.77631 0.77631 0.77631 0.00000  0.00000  0.00000  432 GLU   L CB  
17996 C CG  . GLU   L  29  ? 0.94452 0.94452 0.94452 -0.00000 0.00000  0.00000  432 GLU   L CG  
17997 C CD  . GLU   L  29  ? 1.25328 1.25328 1.25328 0.00000  0.00000  0.00000  432 GLU   L CD  
17998 O OE1 . GLU   L  29  ? 1.06348 1.06348 1.06348 0.00000  0.00000  0.00000  432 GLU   L OE1 
17999 O OE2 . GLU   L  29  ? 1.14267 1.14267 1.14267 -0.00000 0.00000  0.00000  432 GLU   L OE2 
18000 N N   . VAL   L  30  ? 1.15364 1.15364 1.15364 -0.00000 0.00000  0.00000  433 VAL   L N   
18001 C CA  . VAL   L  30  ? 0.84102 0.84102 0.84102 0.00000  0.00000  0.00000  433 VAL   L CA  
18002 C C   . VAL   L  30  ? 1.09562 1.09562 1.09562 0.00000  0.00000  0.00000  433 VAL   L C   
18003 O O   . VAL   L  30  ? 0.97956 0.97956 0.97956 0.00000  0.00000  0.00000  433 VAL   L O   
18004 C CB  . VAL   L  30  ? 1.10638 1.10638 1.10638 -0.00000 0.00000  0.00000  433 VAL   L CB  
18005 C CG1 . VAL   L  30  ? 0.97755 0.97755 0.97755 -0.00000 0.00000  0.00000  433 VAL   L CG1 
18006 C CG2 . VAL   L  30  ? 0.91138 0.91138 0.91138 -0.00000 0.00000  0.00000  433 VAL   L CG2 
18007 N N   . VAL   L  31  ? 0.86387 0.86387 0.86387 0.00000  0.00000  0.00000  434 VAL   L N   
18008 C CA  . VAL   L  31  ? 1.00422 1.00422 1.00422 0.00000  0.00000  0.00000  434 VAL   L CA  
18009 C C   . VAL   L  31  ? 0.84713 0.84713 0.84713 0.00000  0.00000  0.00000  434 VAL   L C   
18010 O O   . VAL   L  31  ? 0.83676 0.83676 0.83676 0.00000  0.00000  0.00000  434 VAL   L O   
18011 C CB  . VAL   L  31  ? 0.88162 0.88162 0.88162 0.00000  0.00000  -0.00000 434 VAL   L CB  
18012 C CG1 . VAL   L  31  ? 0.67599 0.67599 0.67599 0.00000  0.00000  -0.00000 434 VAL   L CG1 
18013 C CG2 . VAL   L  31  ? 0.70865 0.70865 0.70865 -0.00000 0.00000  0.00000  434 VAL   L CG2 
18014 N N   . ALA   L  32  ? 0.96482 0.96482 0.96482 0.00000  0.00000  0.00000  435 ALA   L N   
18015 C CA  . ALA   L  32  ? 1.00633 1.00633 1.00633 0.00000  0.00000  0.00000  435 ALA   L CA  
18016 C C   . ALA   L  32  ? 1.13226 1.13226 1.13226 0.00000  0.00000  0.00000  435 ALA   L C   
18017 O O   . ALA   L  32  ? 1.03182 1.03182 1.03182 0.00000  0.00000  0.00000  435 ALA   L O   
18018 C CB  . ALA   L  32  ? 0.92651 0.92651 0.92651 0.00000  0.00000  0.00000  435 ALA   L CB  
18019 N N   . ALA   L  33  ? 1.08370 1.08370 1.08370 0.00000  0.00000  0.00000  436 ALA   L N   
18020 C CA  . ALA   L  33  ? 1.19767 1.19767 1.19767 0.00000  0.00000  0.00000  436 ALA   L CA  
18021 C C   . ALA   L  33  ? 1.44619 1.44619 1.44619 0.00000  0.00000  0.00000  436 ALA   L C   
18022 O O   . ALA   L  33  ? 1.15991 1.15991 1.15991 -0.00000 0.00000  0.00000  436 ALA   L O   
18023 C CB  . ALA   L  33  ? 0.99633 0.99633 0.99633 0.00000  0.00000  0.00000  436 ALA   L CB  
18024 N N   . LEU   L  34  ? 0.95816 0.95816 0.95816 0.00000  0.00000  0.00000  437 LEU   L N   
18025 C CA  . LEU   L  34  ? 1.33462 1.33462 1.33462 -0.00000 0.00000  0.00000  437 LEU   L CA  
18026 C C   . LEU   L  34  ? 0.92769 0.92769 0.92769 0.00000  0.00000  0.00000  437 LEU   L C   
18027 O O   . LEU   L  34  ? 1.01303 1.01303 1.01303 0.00000  0.00000  0.00000  437 LEU   L O   
18028 C CB  . LEU   L  34  ? 0.91277 0.91277 0.91277 -0.00000 0.00000  0.00000  437 LEU   L CB  
18029 C CG  . LEU   L  34  ? 1.23095 1.23095 1.23095 -0.00000 0.00000  0.00000  437 LEU   L CG  
18030 C CD1 . LEU   L  34  ? 0.99228 0.99228 0.99228 0.00000  0.00000  0.00000  437 LEU   L CD1 
18031 C CD2 . LEU   L  34  ? 1.26584 1.26584 1.26584 -0.00000 0.00000  0.00000  437 LEU   L CD2 
18032 C C   . A1LWG M  .   ? 0.21757 0.21757 0.21757 -0.00000 0.00000  0.00000  501 A1LWG J C   
18033 C CA  . A1LWG M  .   ? 0.28891 0.28891 0.28891 0.00000  0.00000  0.00000  501 A1LWG J CA  
18034 C CB  . A1LWG M  .   ? 0.22199 0.22199 0.22199 0.00000  0.00000  0.00000  501 A1LWG J CB  
18035 C C06 . A1LWG M  .   ? 0.32531 0.32531 0.32531 0.00000  0.00000  0.00000  501 A1LWG J C06 
18036 C C07 . A1LWG M  .   ? 0.70985 0.70985 0.70985 0.00000  0.00000  0.00000  501 A1LWG J C07 
18037 C C08 . A1LWG M  .   ? 1.07265 1.07265 1.07265 -0.00000 0.00000  0.00000  501 A1LWG J C08 
18038 C C09 . A1LWG M  .   ? 1.16888 1.16888 1.16888 -0.00000 0.00000  0.00000  501 A1LWG J C09 
18039 C C11 . A1LWG M  .   ? 1.03110 1.03110 1.03110 -0.00000 0.00000  0.00000  501 A1LWG J C11 
18040 C C12 . A1LWG M  .   ? 1.12734 1.12734 1.12734 0.00000  0.00000  0.00000  501 A1LWG J C12 
18041 C C13 . A1LWG M  .   ? 1.22828 1.22828 1.22828 0.00000  0.00000  0.00000  501 A1LWG J C13 
18042 C C14 . A1LWG M  .   ? 0.57305 0.57305 0.57305 0.00000  -0.00000 0.00000  501 A1LWG J C14 
18043 C C15 . A1LWG M  .   ? 0.45323 0.45323 0.45323 -0.00000 -0.00000 -0.00000 501 A1LWG J C15 
18044 C C16 . A1LWG M  .   ? 0.68786 0.68786 0.68786 0.00000  0.00000  0.00000  501 A1LWG J C16 
18045 N N   . A1LWG M  .   ? 0.89132 0.89132 0.89132 -0.00000 0.00000  0.00000  501 A1LWG J N   
18046 N N10 . A1LWG M  .   ? 1.15644 1.15644 1.15644 -0.00000 0.00000  0.00000  501 A1LWG J N10 
18047 O O   . A1LWG M  .   ? 0.36097 0.36097 0.36097 -0.00000 0.00000  0.00000  501 A1LWG J O   
18048 C C   . A1LWG N  .   ? 0.70117 0.70117 0.70117 -0.00000 0.00000  0.00000  501 A1LWG H C   
18049 C CA  . A1LWG N  .   ? 0.37649 0.37649 0.37649 0.00000  0.00000  0.00000  501 A1LWG H CA  
18050 C CB  . A1LWG N  .   ? 0.21455 0.21455 0.21455 -0.00000 0.00000  0.00000  501 A1LWG H CB  
18051 C C06 . A1LWG N  .   ? 1.13387 1.13387 1.13387 0.00000  0.00000  -0.00000 501 A1LWG H C06 
18052 C C07 . A1LWG N  .   ? 0.22122 0.22122 0.22122 0.00000  0.00000  0.00000  501 A1LWG H C07 
18053 C C08 . A1LWG N  .   ? 0.74411 0.74411 0.74411 0.00000  0.00000  0.00000  501 A1LWG H C08 
18054 C C09 . A1LWG N  .   ? 0.82635 0.82635 0.82635 0.00000  0.00000  0.00000  501 A1LWG H C09 
18055 C C11 . A1LWG N  .   ? 1.12000 1.12000 1.12000 -0.00000 0.00000  0.00000  501 A1LWG H C11 
18056 C C12 . A1LWG N  .   ? 1.14929 1.14929 1.14929 0.00000  0.00000  0.00000  501 A1LWG H C12 
18057 C C13 . A1LWG N  .   ? 0.49542 0.49542 0.49542 -0.00000 0.00000  0.00000  501 A1LWG H C13 
18058 C C14 . A1LWG N  .   ? 0.64174 0.64174 0.64174 -0.00000 0.00000  0.00000  501 A1LWG H C14 
18059 C C15 . A1LWG N  .   ? 0.32908 0.32908 0.32908 0.00000  -0.00000 0.00000  501 A1LWG H C15 
18060 C C16 . A1LWG N  .   ? 0.45551 0.45551 0.45551 0.00000  0.00000  0.00000  501 A1LWG H C16 
18061 N N   . A1LWG N  .   ? 1.13687 1.13687 1.13687 0.00000  0.00000  0.00000  501 A1LWG H N   
18062 N N10 . A1LWG N  .   ? 0.42586 0.42586 0.42586 0.00000  0.00000  0.00000  501 A1LWG H N10 
18063 O O   . A1LWG N  .   ? 0.24955 0.24955 0.24955 -0.00000 0.00000  0.00000  501 A1LWG H O   
18064 C C   . A1LWG O  .   ? 0.30219 0.30219 0.30219 0.00000  0.00000  0.00000  501 A1LWG B C   
18065 C CA  . A1LWG O  .   ? 0.20535 0.20535 0.20535 -0.00000 0.00000  0.00000  501 A1LWG B CA  
18066 C CB  . A1LWG O  .   ? 0.22637 0.22637 0.22637 -0.00000 0.00000  0.00000  501 A1LWG B CB  
18067 C C06 . A1LWG O  .   ? 1.55137 1.55137 1.55137 0.00000  0.00000  0.00000  501 A1LWG B C06 
18068 C C07 . A1LWG O  .   ? 1.25067 1.25067 1.25067 0.00000  0.00000  0.00000  501 A1LWG B C07 
18069 C C08 . A1LWG O  .   ? 1.19670 1.19670 1.19670 0.00000  0.00000  0.00000  501 A1LWG B C08 
18070 C C09 . A1LWG O  .   ? 1.57320 1.57320 1.57320 -0.00000 0.00000  0.00000  501 A1LWG B C09 
18071 C C11 . A1LWG O  .   ? 1.39503 1.39503 1.39503 0.00000  0.00000  0.00000  501 A1LWG B C11 
18072 C C12 . A1LWG O  .   ? 1.03405 1.03405 1.03405 0.00000  0.00000  0.00000  501 A1LWG B C12 
18073 C C13 . A1LWG O  .   ? 0.61705 0.61705 0.61705 -0.00000 0.00000  0.00000  501 A1LWG B C13 
18074 C C14 . A1LWG O  .   ? 0.27201 0.27201 0.27201 0.00000  0.00000  0.00000  501 A1LWG B C14 
18075 C C15 . A1LWG O  .   ? 0.76633 0.76633 0.76633 0.00000  0.00000  0.00000  501 A1LWG B C15 
18076 C C16 . A1LWG O  .   ? 0.24983 0.24983 0.24983 0.00000  0.00000  0.00000  501 A1LWG B C16 
18077 N N   . A1LWG O  .   ? 1.35761 1.35761 1.35761 -0.00000 0.00000  0.00000  501 A1LWG B N   
18078 N N10 . A1LWG O  .   ? 1.08899 1.08899 1.08899 0.00000  0.00000  -0.00000 501 A1LWG B N10 
18079 O O   . A1LWG O  .   ? 0.21655 0.21655 0.21655 0.00000  0.00000  0.00000  501 A1LWG B O   
18080 C C   . A1LWG P  .   ? 0.86962 0.86962 0.86962 -0.00000 0.00000  0.00000  501 A1LWG D C   
18081 C CA  . A1LWG P  .   ? 0.52388 0.52388 0.52388 0.00000  0.00000  0.00000  501 A1LWG D CA  
18082 C CB  . A1LWG P  .   ? 0.23913 0.23913 0.23913 -0.00000 0.00000  0.00000  501 A1LWG D CB  
18083 C C06 . A1LWG P  .   ? 0.39237 0.39237 0.39237 0.00000  0.00000  0.00000  501 A1LWG D C06 
18084 C C07 . A1LWG P  .   ? 1.22997 1.22997 1.22997 0.00000  0.00000  0.00000  501 A1LWG D C07 
18085 C C08 . A1LWG P  .   ? 1.11807 1.11807 1.11807 0.00000  0.00000  0.00000  501 A1LWG D C08 
18086 C C09 . A1LWG P  .   ? 1.29967 1.29967 1.29967 0.00000  0.00000  0.00000  501 A1LWG D C09 
18087 C C11 . A1LWG P  .   ? 1.62658 1.62658 1.62658 0.00000  0.00000  0.00000  501 A1LWG D C11 
18088 C C12 . A1LWG P  .   ? 1.56977 1.56977 1.56977 0.00000  0.00000  0.00000  501 A1LWG D C12 
18089 C C13 . A1LWG P  .   ? 0.75750 0.75750 0.75750 -0.00000 0.00000  0.00000  501 A1LWG D C13 
18090 C C14 . A1LWG P  .   ? 0.42929 0.42929 0.42929 -0.00000 0.00000  0.00000  501 A1LWG D C14 
18091 C C15 . A1LWG P  .   ? 0.52049 0.52049 0.52049 0.00000  0.00000  0.00000  501 A1LWG D C15 
18092 C C16 . A1LWG P  .   ? 0.61735 0.61735 0.61735 -0.00000 0.00000  0.00000  501 A1LWG D C16 
18093 N N   . A1LWG P  .   ? 1.47854 1.47854 1.47854 0.00000  0.00000  0.00000  501 A1LWG D N   
18094 N N10 . A1LWG P  .   ? 0.28537 0.28537 0.28537 -0.00000 0.00000  0.00000  501 A1LWG D N10 
18095 O O   . A1LWG P  .   ? 0.21651 0.21651 0.21651 0.00000  0.00000  0.00000  501 A1LWG D O   
18096 C C   . A1LWG Q  .   ? 0.36578 0.36578 0.36578 0.00000  -0.00000 0.00000  501 A1LWG F C   
18097 C CA  . A1LWG Q  .   ? 0.49268 0.49268 0.49268 0.00000  -0.00000 0.00000  501 A1LWG F CA  
18098 C CB  . A1LWG Q  .   ? 0.31651 0.31651 0.31651 0.00000  0.00000  0.00000  501 A1LWG F CB  
18099 C C06 . A1LWG Q  .   ? 0.92495 0.92495 0.92495 0.00000  0.00000  0.00000  501 A1LWG F C06 
18100 C C07 . A1LWG Q  .   ? 0.41647 0.41647 0.41647 0.00000  0.00000  0.00000  501 A1LWG F C07 
18101 C C08 . A1LWG Q  .   ? 1.60738 1.60738 1.60738 0.00000  0.00000  0.00000  501 A1LWG F C08 
18102 C C09 . A1LWG Q  .   ? 1.49513 1.49513 1.49513 0.00000  0.00000  0.00000  501 A1LWG F C09 
18103 C C11 . A1LWG Q  .   ? 1.54879 1.54879 1.54879 0.00000  0.00000  0.00000  501 A1LWG F C11 
18104 C C12 . A1LWG Q  .   ? 1.85427 1.85427 1.85427 0.00000  0.00000  0.00000  501 A1LWG F C12 
18105 C C13 . A1LWG Q  .   ? 0.32651 0.32651 0.32651 0.00000  0.00000  0.00000  501 A1LWG F C13 
18106 C C14 . A1LWG Q  .   ? 1.12386 1.12386 1.12386 0.00000  0.00000  0.00000  501 A1LWG F C14 
18107 C C15 . A1LWG Q  .   ? 0.39202 0.39202 0.39202 -0.00000 -0.00000 0.00000  501 A1LWG F C15 
18108 C C16 . A1LWG Q  .   ? 0.52892 0.52892 0.52892 0.00000  0.00000  0.00000  501 A1LWG F C16 
18109 N N   . A1LWG Q  .   ? 1.33218 1.33218 1.33218 0.00000  0.00000  0.00000  501 A1LWG F N   
18110 N N10 . A1LWG Q  .   ? 0.31332 0.31332 0.31332 0.00000  0.00000  0.00000  501 A1LWG F N10 
18111 O O   . A1LWG Q  .   ? 0.46193 0.46193 0.46193 0.00000  0.00000  0.00000  501 A1LWG F O   
18112 C C   . A1LWG R  .   ? 0.58784 0.58784 0.58784 0.00000  0.00000  0.00000  501 A1LWG L C   
18113 C CA  . A1LWG R  .   ? 0.29634 0.29634 0.29634 0.00000  0.00000  0.00000  501 A1LWG L CA  
18114 C CB  . A1LWG R  .   ? 0.57498 0.57498 0.57498 0.00000  0.00000  0.00000  501 A1LWG L CB  
18115 C C06 . A1LWG R  .   ? 1.61953 1.61953 1.61953 0.00000  0.00000  0.00000  501 A1LWG L C06 
18116 C C07 . A1LWG R  .   ? 0.75971 0.75971 0.75971 -0.00000 0.00000  0.00000  501 A1LWG L C07 
18117 C C08 . A1LWG R  .   ? 1.21102 1.21102 1.21102 0.00000  0.00000  0.00000  501 A1LWG L C08 
18118 C C09 . A1LWG R  .   ? 0.91747 0.91747 0.91747 0.00000  0.00000  0.00000  501 A1LWG L C09 
18119 C C11 . A1LWG R  .   ? 0.88946 0.88946 0.88946 0.00000  0.00000  0.00000  501 A1LWG L C11 
18120 C C12 . A1LWG R  .   ? 1.50304 1.50304 1.50304 0.00000  0.00000  0.00000  501 A1LWG L C12 
18121 C C13 . A1LWG R  .   ? 1.10454 1.10454 1.10454 -0.00000 0.00000  0.00000  501 A1LWG L C13 
18122 C C14 . A1LWG R  .   ? 0.77162 0.77162 0.77162 0.00000  0.00000  0.00000  501 A1LWG L C14 
18123 C C15 . A1LWG R  .   ? 0.75064 0.75064 0.75064 0.00000  0.00000  0.00000  501 A1LWG L C15 
18124 C C16 . A1LWG R  .   ? 0.49124 0.49124 0.49124 -0.00000 0.00000  0.00000  501 A1LWG L C16 
18125 N N   . A1LWG R  .   ? 1.65177 1.65177 1.65177 0.00000  0.00000  0.00000  501 A1LWG L N   
18126 N N10 . A1LWG R  .   ? 0.48715 0.48715 0.48715 -0.00000 0.00000  -0.00000 501 A1LWG L N10 
18127 O O   . A1LWG R  .   ? 0.41608 0.41608 0.41608 -0.00000 0.00000  0.00000  501 A1LWG L O   
18128 O O   . HOH   S  .   ? 0.42717 0.42717 0.42717 0.00000  0.00000  0.00000  501 HOH   I O   
18129 O O   . HOH   S  .   ? 0.40228 0.40228 0.40228 0.00000  0.00000  0.00000  502 HOH   I O   
18130 O O   . HOH   S  .   ? 0.57997 0.57997 0.57997 0.00000  0.00000  0.00000  503 HOH   I O   
18131 O O   . HOH   S  .   ? 0.55772 0.55772 0.55772 0.00000  0.00000  0.00000  504 HOH   I O   
18132 O O   . HOH   S  .   ? 0.45796 0.45796 0.45796 -0.00000 0.00000  0.00000  505 HOH   I O   
18133 O O   . HOH   S  .   ? 0.43120 0.43120 0.43120 0.00000  0.00000  0.00000  506 HOH   I O   
18134 O O   . HOH   S  .   ? 0.55975 0.55975 0.55975 0.00000  0.00000  0.00000  507 HOH   I O   
18135 O O   . HOH   S  .   ? 0.45950 0.45950 0.45950 0.00000  0.00000  0.00000  508 HOH   I O   
18136 O O   . HOH   S  .   ? 0.34877 0.34877 0.34877 0.00000  0.00000  -0.00000 509 HOH   I O   
18137 O O   . HOH   S  .   ? 0.46342 0.46342 0.46342 0.00000  0.00000  0.00000  510 HOH   I O   
18138 O O   . HOH   S  .   ? 0.43111 0.43111 0.43111 -0.00000 0.00000  -0.00000 511 HOH   I O   
18139 O O   . HOH   S  .   ? 0.55183 0.55183 0.55183 0.00000  0.00000  0.00000  512 HOH   I O   
18140 O O   . HOH   S  .   ? 0.40771 0.40771 0.40771 0.00000  0.00000  0.00000  513 HOH   I O   
18141 O O   . HOH   S  .   ? 0.47030 0.47030 0.47030 -0.00000 0.00000  0.00000  514 HOH   I O   
18142 O O   . HOH   S  .   ? 0.50633 0.50633 0.50633 0.00000  0.00000  0.00000  515 HOH   I O   
18143 O O   . HOH   S  .   ? 0.83063 0.83063 0.83063 -0.00000 0.00000  0.00000  516 HOH   I O   
18144 O O   . HOH   S  .   ? 0.41108 0.41108 0.41108 0.00000  0.00000  0.00000  517 HOH   I O   
18145 O O   . HOH   S  .   ? 0.34569 0.34569 0.34569 -0.00000 0.00000  0.00000  518 HOH   I O   
18146 O O   . HOH   S  .   ? 0.30295 0.30295 0.30295 0.00000  0.00000  0.00000  519 HOH   I O   
18147 O O   . HOH   S  .   ? 0.48345 0.48345 0.48345 0.00000  0.00000  0.00000  520 HOH   I O   
18148 O O   . HOH   S  .   ? 0.36366 0.36366 0.36366 0.00000  -0.00000 0.00000  521 HOH   I O   
18149 O O   . HOH   S  .   ? 0.31646 0.31646 0.31646 -0.00000 0.00000  0.00000  522 HOH   I O   
18150 O O   . HOH   S  .   ? 0.39126 0.39126 0.39126 0.00000  0.00000  0.00000  523 HOH   I O   
18151 O O   . HOH   S  .   ? 0.60734 0.60734 0.60734 0.00000  0.00000  0.00000  524 HOH   I O   
18152 O O   . HOH   S  .   ? 0.45585 0.45585 0.45585 -0.00000 0.00000  0.00000  525 HOH   I O   
18153 O O   . HOH   S  .   ? 0.37256 0.37256 0.37256 0.00000  0.00000  0.00000  526 HOH   I O   
18154 O O   . HOH   S  .   ? 0.33608 0.33608 0.33608 0.00000  0.00000  0.00000  527 HOH   I O   
18155 O O   . HOH   S  .   ? 0.46311 0.46311 0.46311 0.00000  0.00000  0.00000  528 HOH   I O   
18156 O O   . HOH   S  .   ? 0.31381 0.31381 0.31381 0.00000  0.00000  0.00000  529 HOH   I O   
18157 O O   . HOH   S  .   ? 0.27843 0.27843 0.27843 0.00000  0.00000  0.00000  530 HOH   I O   
18158 O O   . HOH   S  .   ? 0.42900 0.42900 0.42900 0.00000  0.00000  0.00000  531 HOH   I O   
18159 O O   . HOH   S  .   ? 0.27904 0.27904 0.27904 0.00000  0.00000  0.00000  532 HOH   I O   
18160 O O   . HOH   S  .   ? 0.29928 0.29928 0.29928 0.00000  0.00000  0.00000  533 HOH   I O   
18161 O O   . HOH   S  .   ? 0.46423 0.46423 0.46423 0.00000  0.00000  0.00000  534 HOH   I O   
18162 O O   . HOH   S  .   ? 0.30759 0.30759 0.30759 0.00000  -0.00000 0.00000  535 HOH   I O   
18163 O O   . HOH   S  .   ? 0.39719 0.39719 0.39719 0.00000  0.00000  0.00000  536 HOH   I O   
18164 O O   . HOH   S  .   ? 0.59146 0.59146 0.59146 0.00000  0.00000  0.00000  537 HOH   I O   
18165 O O   . HOH   S  .   ? 0.59883 0.59883 0.59883 -0.00000 0.00000  0.00000  538 HOH   I O   
18166 O O   . HOH   S  .   ? 0.39316 0.39316 0.39316 -0.00000 0.00000  0.00000  539 HOH   I O   
18167 O O   . HOH   S  .   ? 0.46848 0.46848 0.46848 0.00000  0.00000  0.00000  540 HOH   I O   
18168 O O   . HOH   S  .   ? 0.33988 0.33988 0.33988 0.00000  0.00000  0.00000  541 HOH   I O   
18169 O O   . HOH   S  .   ? 0.27348 0.27348 0.27348 0.00000  0.00000  0.00000  542 HOH   I O   
18170 O O   . HOH   S  .   ? 0.38607 0.38607 0.38607 0.00000  0.00000  0.00000  543 HOH   I O   
18171 O O   . HOH   S  .   ? 0.59316 0.59316 0.59316 0.00000  0.00000  0.00000  544 HOH   I O   
18172 O O   . HOH   S  .   ? 0.47793 0.47793 0.47793 0.00000  0.00000  0.00000  545 HOH   I O   
18173 O O   . HOH   S  .   ? 0.55656 0.55656 0.55656 0.00000  0.00000  0.00000  546 HOH   I O   
18174 O O   . HOH   S  .   ? 0.38164 0.38164 0.38164 0.00000  0.00000  0.00000  547 HOH   I O   
18175 O O   . HOH   S  .   ? 0.52932 0.52932 0.52932 -0.00000 0.00000  0.00000  548 HOH   I O   
18176 O O   . HOH   S  .   ? 0.48295 0.48295 0.48295 0.00000  0.00000  0.00000  549 HOH   I O   
18177 O O   . HOH   S  .   ? 0.43551 0.43551 0.43551 0.00000  0.00000  0.00000  550 HOH   I O   
18178 O O   . HOH   S  .   ? 0.26011 0.26011 0.26011 -0.00000 0.00000  0.00000  551 HOH   I O   
18179 O O   . HOH   S  .   ? 0.43908 0.43908 0.43908 0.00000  0.00000  0.00000  552 HOH   I O   
18180 O O   . HOH   S  .   ? 0.44931 0.44931 0.44931 -0.00000 0.00000  0.00000  553 HOH   I O   
18181 O O   . HOH   S  .   ? 0.31480 0.31480 0.31480 -0.00000 0.00000  0.00000  554 HOH   I O   
18182 O O   . HOH   S  .   ? 0.30732 0.30732 0.30732 -0.00000 0.00000  0.00000  555 HOH   I O   
18183 O O   . HOH   S  .   ? 0.33254 0.33254 0.33254 0.00000  0.00000  0.00000  556 HOH   I O   
18184 O O   . HOH   S  .   ? 1.15314 1.15314 1.15314 -0.00000 0.00000  0.00000  557 HOH   I O   
18185 O O   . HOH   S  .   ? 0.53778 0.53778 0.53778 -0.00000 0.00000  0.00000  558 HOH   I O   
18186 O O   . HOH   S  .   ? 0.52818 0.52818 0.52818 -0.00000 -0.00000 0.00000  559 HOH   I O   
18187 O O   . HOH   S  .   ? 0.35163 0.35163 0.35163 0.00000  0.00000  0.00000  560 HOH   I O   
18188 O O   . HOH   S  .   ? 0.38800 0.38800 0.38800 0.00000  0.00000  0.00000  561 HOH   I O   
18189 O O   . HOH   S  .   ? 0.47665 0.47665 0.47665 -0.00000 0.00000  0.00000  562 HOH   I O   
18190 O O   . HOH   S  .   ? 0.37482 0.37482 0.37482 0.00000  0.00000  -0.00000 563 HOH   I O   
18191 O O   . HOH   S  .   ? 0.30429 0.30429 0.30429 -0.00000 0.00000  0.00000  564 HOH   I O   
18192 O O   . HOH   T  .   ? 0.58359 0.58359 0.58359 0.00000  0.00000  0.00000  601 HOH   J O   
18193 O O   . HOH   T  .   ? 0.45436 0.45436 0.45436 0.00000  0.00000  0.00000  602 HOH   J O   
18194 O O   . HOH   U  .   ? 0.39817 0.39817 0.39817 0.00000  0.00000  0.00000  501 HOH   G O   
18195 O O   . HOH   U  .   ? 0.51813 0.51813 0.51813 -0.00000 0.00000  0.00000  502 HOH   G O   
18196 O O   . HOH   U  .   ? 0.38412 0.38412 0.38412 -0.00000 0.00000  0.00000  503 HOH   G O   
18197 O O   . HOH   U  .   ? 0.43651 0.43651 0.43651 0.00000  -0.00000 0.00000  504 HOH   G O   
18198 O O   . HOH   U  .   ? 0.40394 0.40394 0.40394 0.00000  0.00000  0.00000  505 HOH   G O   
18199 O O   . HOH   U  .   ? 0.37112 0.37112 0.37112 0.00000  0.00000  -0.00000 506 HOH   G O   
18200 O O   . HOH   U  .   ? 0.20929 0.20929 0.20929 -0.00000 0.00000  0.00000  507 HOH   G O   
18201 O O   . HOH   U  .   ? 0.44725 0.44725 0.44725 0.00000  0.00000  0.00000  508 HOH   G O   
18202 O O   . HOH   U  .   ? 0.25387 0.25387 0.25387 -0.00000 0.00000  0.00000  509 HOH   G O   
18203 O O   . HOH   U  .   ? 0.44849 0.44849 0.44849 0.00000  0.00000  0.00000  510 HOH   G O   
18204 O O   . HOH   U  .   ? 0.31373 0.31373 0.31373 0.00000  0.00000  0.00000  511 HOH   G O   
18205 O O   . HOH   U  .   ? 0.24772 0.24772 0.24772 -0.00000 0.00000  0.00000  512 HOH   G O   
18206 O O   . HOH   U  .   ? 0.56444 0.56444 0.56444 -0.00000 0.00000  0.00000  513 HOH   G O   
18207 O O   . HOH   U  .   ? 0.39318 0.39318 0.39318 -0.00000 0.00000  0.00000  514 HOH   G O   
18208 O O   . HOH   U  .   ? 0.32678 0.32678 0.32678 -0.00000 0.00000  0.00000  515 HOH   G O   
18209 O O   . HOH   U  .   ? 0.27859 0.27859 0.27859 0.00000  0.00000  0.00000  516 HOH   G O   
18210 O O   . HOH   U  .   ? 0.38095 0.38095 0.38095 -0.00000 0.00000  0.00000  517 HOH   G O   
18211 O O   . HOH   U  .   ? 0.31807 0.31807 0.31807 0.00000  -0.00000 0.00000  518 HOH   G O   
18212 O O   . HOH   U  .   ? 0.21373 0.21373 0.21373 0.00000  0.00000  0.00000  519 HOH   G O   
18213 O O   . HOH   U  .   ? 0.28625 0.28625 0.28625 0.00000  0.00000  0.00000  520 HOH   G O   
18214 O O   . HOH   U  .   ? 0.29408 0.29408 0.29408 -0.00000 0.00000  0.00000  521 HOH   G O   
18215 O O   . HOH   U  .   ? 0.43716 0.43716 0.43716 0.00000  0.00000  0.00000  522 HOH   G O   
18216 O O   . HOH   U  .   ? 0.29364 0.29364 0.29364 0.00000  0.00000  0.00000  523 HOH   G O   
18217 O O   . HOH   U  .   ? 0.18665 0.18665 0.18665 -0.00000 0.00000  0.00000  524 HOH   G O   
18218 O O   . HOH   U  .   ? 0.42880 0.42880 0.42880 0.00000  0.00000  -0.00000 525 HOH   G O   
18219 O O   . HOH   U  .   ? 0.37998 0.37998 0.37998 0.00000  0.00000  0.00000  526 HOH   G O   
18220 O O   . HOH   U  .   ? 0.35769 0.35769 0.35769 -0.00000 0.00000  0.00000  527 HOH   G O   
18221 O O   . HOH   U  .   ? 0.39628 0.39628 0.39628 -0.00000 -0.00000 0.00000  528 HOH   G O   
18222 O O   . HOH   U  .   ? 0.45864 0.45864 0.45864 -0.00000 0.00000  0.00000  529 HOH   G O   
18223 O O   . HOH   U  .   ? 0.36213 0.36213 0.36213 -0.00000 0.00000  0.00000  530 HOH   G O   
18224 O O   . HOH   U  .   ? 0.40079 0.40079 0.40079 0.00000  0.00000  0.00000  531 HOH   G O   
18225 O O   . HOH   U  .   ? 0.48617 0.48617 0.48617 -0.00000 0.00000  0.00000  532 HOH   G O   
18226 O O   . HOH   U  .   ? 0.38653 0.38653 0.38653 -0.00000 0.00000  0.00000  533 HOH   G O   
18227 O O   . HOH   U  .   ? 0.28007 0.28007 0.28007 -0.00000 0.00000  0.00000  534 HOH   G O   
18228 O O   . HOH   U  .   ? 0.29081 0.29081 0.29081 -0.00000 0.00000  0.00000  535 HOH   G O   
18229 O O   . HOH   U  .   ? 0.41213 0.41213 0.41213 0.00000  0.00000  0.00000  536 HOH   G O   
18230 O O   . HOH   U  .   ? 0.35479 0.35479 0.35479 0.00000  0.00000  0.00000  537 HOH   G O   
18231 O O   . HOH   U  .   ? 0.42091 0.42091 0.42091 0.00000  0.00000  0.00000  538 HOH   G O   
18232 O O   . HOH   U  .   ? 0.22532 0.22532 0.22532 -0.00000 0.00000  0.00000  539 HOH   G O   
18233 O O   . HOH   U  .   ? 0.35565 0.35565 0.35565 -0.00000 0.00000  0.00000  540 HOH   G O   
18234 O O   . HOH   U  .   ? 0.33664 0.33664 0.33664 0.00000  0.00000  0.00000  541 HOH   G O   
18235 O O   . HOH   U  .   ? 0.32544 0.32544 0.32544 0.00000  0.00000  0.00000  542 HOH   G O   
18236 O O   . HOH   U  .   ? 0.33265 0.33265 0.33265 0.00000  0.00000  0.00000  543 HOH   G O   
18237 O O   . HOH   U  .   ? 0.24809 0.24809 0.24809 0.00000  0.00000  0.00000  544 HOH   G O   
18238 O O   . HOH   U  .   ? 0.40392 0.40392 0.40392 0.00000  0.00000  0.00000  545 HOH   G O   
18239 O O   . HOH   U  .   ? 0.43852 0.43852 0.43852 0.00000  0.00000  0.00000  546 HOH   G O   
18240 O O   . HOH   U  .   ? 0.46905 0.46905 0.46905 0.00000  0.00000  0.00000  547 HOH   G O   
18241 O O   . HOH   U  .   ? 0.43264 0.43264 0.43264 0.00000  0.00000  -0.00000 548 HOH   G O   
18242 O O   . HOH   U  .   ? 0.23102 0.23102 0.23102 0.00000  0.00000  0.00000  549 HOH   G O   
18243 O O   . HOH   U  .   ? 0.37503 0.37503 0.37503 0.00000  0.00000  0.00000  550 HOH   G O   
18244 O O   . HOH   U  .   ? 0.41548 0.41548 0.41548 0.00000  0.00000  0.00000  551 HOH   G O   
18245 O O   . HOH   U  .   ? 0.38252 0.38252 0.38252 -0.00000 0.00000  0.00000  552 HOH   G O   
18246 O O   . HOH   U  .   ? 0.25656 0.25656 0.25656 0.00000  0.00000  0.00000  553 HOH   G O   
18247 O O   . HOH   U  .   ? 0.28595 0.28595 0.28595 0.00000  0.00000  0.00000  554 HOH   G O   
18248 O O   . HOH   U  .   ? 0.32924 0.32924 0.32924 -0.00000 0.00000  0.00000  555 HOH   G O   
18249 O O   . HOH   U  .   ? 0.39010 0.39010 0.39010 0.00000  0.00000  0.00000  556 HOH   G O   
18250 O O   . HOH   U  .   ? 0.28882 0.28882 0.28882 0.00000  0.00000  0.00000  557 HOH   G O   
18251 O O   . HOH   U  .   ? 0.53254 0.53254 0.53254 0.00000  0.00000  0.00000  558 HOH   G O   
18252 O O   . HOH   U  .   ? 0.24890 0.24890 0.24890 0.00000  0.00000  0.00000  559 HOH   G O   
18253 O O   . HOH   U  .   ? 0.38444 0.38444 0.38444 0.00000  0.00000  0.00000  560 HOH   G O   
18254 O O   . HOH   U  .   ? 0.27789 0.27789 0.27789 0.00000  0.00000  0.00000  561 HOH   G O   
18255 O O   . HOH   U  .   ? 0.29105 0.29105 0.29105 0.00000  0.00000  0.00000  562 HOH   G O   
18256 O O   . HOH   U  .   ? 0.51302 0.51302 0.51302 0.00000  0.00000  0.00000  563 HOH   G O   
18257 O O   . HOH   U  .   ? 0.28751 0.28751 0.28751 0.00000  0.00000  0.00000  564 HOH   G O   
18258 O O   . HOH   U  .   ? 0.39108 0.39108 0.39108 -0.00000 0.00000  0.00000  565 HOH   G O   
18259 O O   . HOH   U  .   ? 0.28876 0.28876 0.28876 -0.00000 0.00000  0.00000  566 HOH   G O   
18260 O O   . HOH   U  .   ? 0.31295 0.31295 0.31295 0.00000  0.00000  -0.00000 567 HOH   G O   
18261 O O   . HOH   U  .   ? 0.27220 0.27220 0.27220 -0.00000 -0.00000 -0.00000 568 HOH   G O   
18262 O O   . HOH   U  .   ? 0.44016 0.44016 0.44016 -0.00000 0.00000  0.00000  569 HOH   G O   
18263 O O   . HOH   U  .   ? 0.33364 0.33364 0.33364 0.00000  0.00000  0.00000  570 HOH   G O   
18264 O O   . HOH   U  .   ? 0.46661 0.46661 0.46661 -0.00000 0.00000  0.00000  571 HOH   G O   
18265 O O   . HOH   U  .   ? 0.29383 0.29383 0.29383 0.00000  0.00000  0.00000  572 HOH   G O   
18266 O O   . HOH   U  .   ? 0.48720 0.48720 0.48720 0.00000  0.00000  0.00000  573 HOH   G O   
18267 O O   . HOH   U  .   ? 0.37516 0.37516 0.37516 -0.00000 0.00000  0.00000  574 HOH   G O   
18268 O O   . HOH   U  .   ? 0.38649 0.38649 0.38649 0.00000  0.00000  0.00000  575 HOH   G O   
18269 O O   . HOH   U  .   ? 0.38289 0.38289 0.38289 0.00000  0.00000  0.00000  576 HOH   G O   
18270 O O   . HOH   U  .   ? 0.35381 0.35381 0.35381 0.00000  0.00000  0.00000  577 HOH   G O   
18271 O O   . HOH   U  .   ? 0.43701 0.43701 0.43701 -0.00000 0.00000  0.00000  578 HOH   G O   
18272 O O   . HOH   U  .   ? 0.45311 0.45311 0.45311 -0.00000 0.00000  0.00000  579 HOH   G O   
18273 O O   . HOH   U  .   ? 0.26971 0.26971 0.26971 0.00000  0.00000  0.00000  580 HOH   G O   
18274 O O   . HOH   U  .   ? 0.52759 0.52759 0.52759 -0.00000 0.00000  0.00000  581 HOH   G O   
18275 O O   . HOH   U  .   ? 0.26182 0.26182 0.26182 0.00000  0.00000  0.00000  582 HOH   G O   
18276 O O   . HOH   U  .   ? 0.42214 0.42214 0.42214 0.00000  0.00000  0.00000  583 HOH   G O   
18277 O O   . HOH   U  .   ? 0.52582 0.52582 0.52582 0.00000  0.00000  0.00000  584 HOH   G O   
18278 O O   . HOH   U  .   ? 0.45833 0.45833 0.45833 -0.00000 0.00000  0.00000  585 HOH   G O   
18279 O O   . HOH   U  .   ? 0.22481 0.22481 0.22481 0.00000  0.00000  0.00000  586 HOH   G O   
18280 O O   . HOH   U  .   ? 0.23517 0.23517 0.23517 0.00000  0.00000  0.00000  587 HOH   G O   
18281 O O   . HOH   U  .   ? 0.48506 0.48506 0.48506 0.00000  0.00000  0.00000  588 HOH   G O   
18282 O O   . HOH   U  .   ? 0.38912 0.38912 0.38912 0.00000  0.00000  0.00000  589 HOH   G O   
18283 O O   . HOH   U  .   ? 0.40114 0.40114 0.40114 0.00000  0.00000  0.00000  590 HOH   G O   
18284 O O   . HOH   U  .   ? 0.46736 0.46736 0.46736 0.00000  0.00000  0.00000  591 HOH   G O   
18285 O O   . HOH   U  .   ? 0.46347 0.46347 0.46347 0.00000  0.00000  0.00000  592 HOH   G O   
18286 O O   . HOH   U  .   ? 0.44168 0.44168 0.44168 -0.00000 0.00000  0.00000  593 HOH   G O   
18287 O O   . HOH   U  .   ? 0.41250 0.41250 0.41250 0.00000  0.00000  0.00000  594 HOH   G O   
18288 O O   . HOH   U  .   ? 0.31192 0.31192 0.31192 0.00000  0.00000  0.00000  595 HOH   G O   
18289 O O   . HOH   U  .   ? 0.53784 0.53784 0.53784 0.00000  -0.00000 -0.00000 596 HOH   G O   
18290 O O   . HOH   U  .   ? 0.33988 0.33988 0.33988 0.00000  0.00000  0.00000  597 HOH   G O   
18291 O O   . HOH   U  .   ? 0.36748 0.36748 0.36748 -0.00000 0.00000  0.00000  598 HOH   G O   
18292 O O   . HOH   U  .   ? 0.55997 0.55997 0.55997 0.00000  0.00000  0.00000  599 HOH   G O   
18293 O O   . HOH   V  .   ? 0.46083 0.46083 0.46083 -0.00000 0.00000  0.00000  601 HOH   H O   
18294 O O   . HOH   V  .   ? 0.40124 0.40124 0.40124 0.00000  0.00000  0.00000  602 HOH   H O   
18295 O O   . HOH   V  .   ? 0.30896 0.30896 0.30896 0.00000  0.00000  0.00000  603 HOH   H O   
18296 O O   . HOH   V  .   ? 0.45188 0.45188 0.45188 0.00000  -0.00000 0.00000  604 HOH   H O   
18297 O O   . HOH   V  .   ? 0.46678 0.46678 0.46678 0.00000  0.00000  0.00000  605 HOH   H O   
18298 O O   . HOH   V  .   ? 0.33164 0.33164 0.33164 0.00000  0.00000  0.00000  606 HOH   H O   
18299 O O   . HOH   V  .   ? 0.24914 0.24914 0.24914 0.00000  0.00000  0.00000  607 HOH   H O   
18300 O O   . HOH   V  .   ? 0.42647 0.42647 0.42647 0.00000  -0.00000 0.00000  608 HOH   H O   
18301 O O   . HOH   W  .   ? 0.52958 0.52958 0.52958 0.00000  0.00000  0.00000  501 HOH   A O   
18302 O O   . HOH   W  .   ? 0.31284 0.31284 0.31284 0.00000  0.00000  0.00000  502 HOH   A O   
18303 O O   . HOH   W  .   ? 0.24307 0.24307 0.24307 0.00000  0.00000  0.00000  503 HOH   A O   
18304 O O   . HOH   W  .   ? 0.54662 0.54662 0.54662 0.00000  0.00000  0.00000  504 HOH   A O   
18305 O O   . HOH   W  .   ? 0.42450 0.42450 0.42450 0.00000  0.00000  0.00000  505 HOH   A O   
18306 O O   . HOH   W  .   ? 0.41001 0.41001 0.41001 0.00000  0.00000  0.00000  506 HOH   A O   
18307 O O   . HOH   W  .   ? 0.58227 0.58227 0.58227 0.00000  0.00000  0.00000  507 HOH   A O   
18308 O O   . HOH   W  .   ? 0.35891 0.35891 0.35891 0.00000  0.00000  0.00000  508 HOH   A O   
18309 O O   . HOH   W  .   ? 0.41341 0.41341 0.41341 0.00000  0.00000  0.00000  509 HOH   A O   
18310 O O   . HOH   W  .   ? 0.31003 0.31003 0.31003 0.00000  0.00000  -0.00000 510 HOH   A O   
18311 O O   . HOH   W  .   ? 0.44921 0.44921 0.44921 -0.00000 0.00000  0.00000  511 HOH   A O   
18312 O O   . HOH   W  .   ? 0.23522 0.23522 0.23522 0.00000  0.00000  0.00000  512 HOH   A O   
18313 O O   . HOH   W  .   ? 0.41801 0.41801 0.41801 0.00000  0.00000  0.00000  513 HOH   A O   
18314 O O   . HOH   W  .   ? 0.53944 0.53944 0.53944 -0.00000 0.00000  0.00000  514 HOH   A O   
18315 O O   . HOH   W  .   ? 0.41007 0.41007 0.41007 0.00000  0.00000  0.00000  515 HOH   A O   
18316 O O   . HOH   W  .   ? 0.48727 0.48727 0.48727 0.00000  0.00000  0.00000  516 HOH   A O   
18317 O O   . HOH   W  .   ? 0.31094 0.31094 0.31094 -0.00000 0.00000  -0.00000 517 HOH   A O   
18318 O O   . HOH   W  .   ? 0.33482 0.33482 0.33482 0.00000  0.00000  0.00000  518 HOH   A O   
18319 O O   . HOH   W  .   ? 0.58027 0.58027 0.58027 0.00000  0.00000  0.00000  519 HOH   A O   
18320 O O   . HOH   W  .   ? 0.25340 0.25340 0.25340 0.00000  0.00000  0.00000  520 HOH   A O   
18321 O O   . HOH   W  .   ? 0.29552 0.29552 0.29552 0.00000  0.00000  0.00000  521 HOH   A O   
18322 O O   . HOH   W  .   ? 0.40467 0.40467 0.40467 0.00000  0.00000  0.00000  522 HOH   A O   
18323 O O   . HOH   W  .   ? 0.19648 0.19648 0.19648 0.00000  0.00000  0.00000  523 HOH   A O   
18324 O O   . HOH   W  .   ? 0.45917 0.45917 0.45917 0.00000  0.00000  0.00000  524 HOH   A O   
18325 O O   . HOH   W  .   ? 0.52651 0.52651 0.52651 0.00000  0.00000  0.00000  525 HOH   A O   
18326 O O   . HOH   W  .   ? 0.45043 0.45043 0.45043 0.00000  0.00000  0.00000  526 HOH   A O   
18327 O O   . HOH   W  .   ? 0.33356 0.33356 0.33356 0.00000  -0.00000 0.00000  527 HOH   A O   
18328 O O   . HOH   W  .   ? 0.28883 0.28883 0.28883 0.00000  0.00000  0.00000  528 HOH   A O   
18329 O O   . HOH   W  .   ? 0.51500 0.51500 0.51500 0.00000  0.00000  0.00000  529 HOH   A O   
18330 O O   . HOH   W  .   ? 0.41917 0.41917 0.41917 -0.00000 0.00000  0.00000  530 HOH   A O   
18331 O O   . HOH   W  .   ? 0.43291 0.43291 0.43291 -0.00000 0.00000  0.00000  531 HOH   A O   
18332 O O   . HOH   W  .   ? 0.38224 0.38224 0.38224 0.00000  0.00000  0.00000  532 HOH   A O   
18333 O O   . HOH   W  .   ? 0.37499 0.37499 0.37499 0.00000  0.00000  0.00000  533 HOH   A O   
18334 O O   . HOH   W  .   ? 0.37004 0.37004 0.37004 -0.00000 0.00000  0.00000  534 HOH   A O   
18335 O O   . HOH   W  .   ? 0.39589 0.39589 0.39589 -0.00000 0.00000  0.00000  535 HOH   A O   
18336 O O   . HOH   W  .   ? 0.38396 0.38396 0.38396 0.00000  0.00000  0.00000  536 HOH   A O   
18337 O O   . HOH   W  .   ? 0.53564 0.53564 0.53564 0.00000  0.00000  0.00000  537 HOH   A O   
18338 O O   . HOH   W  .   ? 0.39301 0.39301 0.39301 0.00000  0.00000  0.00000  538 HOH   A O   
18339 O O   . HOH   W  .   ? 0.44204 0.44204 0.44204 0.00000  0.00000  0.00000  539 HOH   A O   
18340 O O   . HOH   W  .   ? 0.40612 0.40612 0.40612 0.00000  0.00000  0.00000  540 HOH   A O   
18341 O O   . HOH   W  .   ? 0.37789 0.37789 0.37789 0.00000  0.00000  0.00000  541 HOH   A O   
18342 O O   . HOH   W  .   ? 0.33065 0.33065 0.33065 -0.00000 0.00000  0.00000  542 HOH   A O   
18343 O O   . HOH   W  .   ? 0.48125 0.48125 0.48125 -0.00000 0.00000  0.00000  543 HOH   A O   
18344 O O   . HOH   W  .   ? 0.27735 0.27735 0.27735 0.00000  0.00000  0.00000  544 HOH   A O   
18345 O O   . HOH   W  .   ? 0.45712 0.45712 0.45712 -0.00000 0.00000  0.00000  545 HOH   A O   
18346 O O   . HOH   W  .   ? 0.44234 0.44234 0.44234 0.00000  0.00000  0.00000  546 HOH   A O   
18347 O O   . HOH   W  .   ? 0.28716 0.28716 0.28716 0.00000  0.00000  0.00000  547 HOH   A O   
18348 O O   . HOH   W  .   ? 0.28616 0.28616 0.28616 -0.00000 0.00000  0.00000  548 HOH   A O   
18349 O O   . HOH   W  .   ? 0.28597 0.28597 0.28597 -0.00000 0.00000  0.00000  549 HOH   A O   
18350 O O   . HOH   W  .   ? 0.42600 0.42600 0.42600 0.00000  0.00000  0.00000  550 HOH   A O   
18351 O O   . HOH   W  .   ? 0.48817 0.48817 0.48817 -0.00000 0.00000  0.00000  551 HOH   A O   
18352 O O   . HOH   W  .   ? 0.31709 0.31709 0.31709 0.00000  0.00000  0.00000  552 HOH   A O   
18353 O O   . HOH   W  .   ? 0.42193 0.42193 0.42193 -0.00000 0.00000  0.00000  553 HOH   A O   
18354 O O   . HOH   W  .   ? 0.34579 0.34579 0.34579 0.00000  0.00000  0.00000  554 HOH   A O   
18355 O O   . HOH   W  .   ? 0.34003 0.34003 0.34003 0.00000  0.00000  0.00000  555 HOH   A O   
18356 O O   . HOH   W  .   ? 0.45192 0.45192 0.45192 -0.00000 0.00000  0.00000  556 HOH   A O   
18357 O O   . HOH   W  .   ? 0.43384 0.43384 0.43384 0.00000  0.00000  0.00000  557 HOH   A O   
18358 O O   . HOH   W  .   ? 0.29352 0.29352 0.29352 0.00000  0.00000  0.00000  558 HOH   A O   
18359 O O   . HOH   W  .   ? 0.42693 0.42693 0.42693 0.00000  0.00000  0.00000  559 HOH   A O   
18360 O O   . HOH   W  .   ? 0.41343 0.41343 0.41343 0.00000  0.00000  0.00000  560 HOH   A O   
18361 O O   . HOH   W  .   ? 0.36920 0.36920 0.36920 0.00000  0.00000  0.00000  561 HOH   A O   
18362 O O   . HOH   W  .   ? 0.24207 0.24207 0.24207 0.00000  0.00000  0.00000  562 HOH   A O   
18363 O O   . HOH   W  .   ? 0.39955 0.39955 0.39955 0.00000  0.00000  0.00000  563 HOH   A O   
18364 O O   . HOH   W  .   ? 0.37259 0.37259 0.37259 -0.00000 0.00000  0.00000  564 HOH   A O   
18365 O O   . HOH   W  .   ? 0.41676 0.41676 0.41676 -0.00000 0.00000  0.00000  565 HOH   A O   
18366 O O   . HOH   W  .   ? 0.31885 0.31885 0.31885 0.00000  0.00000  0.00000  566 HOH   A O   
18367 O O   . HOH   W  .   ? 0.40087 0.40087 0.40087 0.00000  0.00000  0.00000  567 HOH   A O   
18368 O O   . HOH   W  .   ? 0.46820 0.46820 0.46820 0.00000  0.00000  0.00000  568 HOH   A O   
18369 O O   . HOH   W  .   ? 0.42349 0.42349 0.42349 -0.00000 0.00000  0.00000  569 HOH   A O   
18370 O O   . HOH   W  .   ? 0.33983 0.33983 0.33983 0.00000  0.00000  0.00000  570 HOH   A O   
18371 O O   . HOH   W  .   ? 0.45570 0.45570 0.45570 0.00000  0.00000  0.00000  571 HOH   A O   
18372 O O   . HOH   W  .   ? 0.20132 0.20132 0.20132 0.00000  0.00000  0.00000  572 HOH   A O   
18373 O O   . HOH   W  .   ? 0.39156 0.39156 0.39156 0.00000  0.00000  0.00000  573 HOH   A O   
18374 O O   . HOH   W  .   ? 0.28712 0.28712 0.28712 0.00000  0.00000  0.00000  574 HOH   A O   
18375 O O   . HOH   W  .   ? 0.62190 0.62190 0.62190 0.00000  0.00000  0.00000  575 HOH   A O   
18376 O O   . HOH   W  .   ? 0.36797 0.36797 0.36797 0.00000  -0.00000 0.00000  576 HOH   A O   
18377 O O   . HOH   W  .   ? 0.38726 0.38726 0.38726 0.00000  0.00000  0.00000  577 HOH   A O   
18378 O O   . HOH   W  .   ? 0.44982 0.44982 0.44982 0.00000  0.00000  0.00000  578 HOH   A O   
18379 O O   . HOH   W  .   ? 0.46085 0.46085 0.46085 0.00000  0.00000  0.00000  579 HOH   A O   
18380 O O   . HOH   W  .   ? 0.38103 0.38103 0.38103 0.00000  0.00000  0.00000  580 HOH   A O   
18381 O O   . HOH   W  .   ? 0.44074 0.44074 0.44074 -0.00000 0.00000  0.00000  581 HOH   A O   
18382 O O   . HOH   W  .   ? 0.60857 0.60857 0.60857 -0.00000 0.00000  0.00000  582 HOH   A O   
18383 O O   . HOH   W  .   ? 0.46753 0.46753 0.46753 0.00000  0.00000  0.00000  583 HOH   A O   
18384 O O   . HOH   W  .   ? 0.41781 0.41781 0.41781 -0.00000 0.00000  0.00000  584 HOH   A O   
18385 O O   . HOH   W  .   ? 0.46381 0.46381 0.46381 0.00000  0.00000  0.00000  585 HOH   A O   
18386 O O   . HOH   W  .   ? 0.37807 0.37807 0.37807 0.00000  0.00000  0.00000  586 HOH   A O   
18387 O O   . HOH   W  .   ? 0.57075 0.57075 0.57075 -0.00000 -0.00000 0.00000  587 HOH   A O   
18388 O O   . HOH   W  .   ? 0.32142 0.32142 0.32142 0.00000  -0.00000 0.00000  588 HOH   A O   
18389 O O   . HOH   W  .   ? 0.51482 0.51482 0.51482 -0.00000 0.00000  0.00000  589 HOH   A O   
18390 O O   . HOH   W  .   ? 0.45973 0.45973 0.45973 -0.00000 0.00000  0.00000  590 HOH   A O   
18391 O O   . HOH   X  .   ? 0.51026 0.51026 0.51026 -0.00000 0.00000  0.00000  601 HOH   B O   
18392 O O   . HOH   X  .   ? 0.50679 0.50679 0.50679 0.00000  0.00000  0.00000  602 HOH   B O   
18393 O O   . HOH   X  .   ? 0.55370 0.55370 0.55370 0.00000  0.00000  0.00000  603 HOH   B O   
18394 O O   . HOH   X  .   ? 0.47281 0.47281 0.47281 0.00000  0.00000  0.00000  604 HOH   B O   
18395 O O   . HOH   X  .   ? 0.48199 0.48199 0.48199 -0.00000 0.00000  0.00000  605 HOH   B O   
18396 O O   . HOH   X  .   ? 0.41996 0.41996 0.41996 0.00000  0.00000  0.00000  606 HOH   B O   
18397 O O   . HOH   X  .   ? 0.29880 0.29880 0.29880 -0.00000 0.00000  0.00000  607 HOH   B O   
18398 O O   . HOH   X  .   ? 0.32626 0.32626 0.32626 0.00000  0.00000  0.00000  608 HOH   B O   
18399 O O   . HOH   X  .   ? 0.49650 0.49650 0.49650 0.00000  0.00000  0.00000  609 HOH   B O   
18400 O O   . HOH   Y  .   ? 0.33140 0.33140 0.33140 0.00000  0.00000  0.00000  501 HOH   C O   
18401 O O   . HOH   Y  .   ? 0.40364 0.40364 0.40364 0.00000  0.00000  0.00000  502 HOH   C O   
18402 O O   . HOH   Y  .   ? 0.45056 0.45056 0.45056 -0.00000 0.00000  0.00000  503 HOH   C O   
18403 O O   . HOH   Y  .   ? 0.31012 0.31012 0.31012 -0.00000 0.00000  0.00000  504 HOH   C O   
18404 O O   . HOH   Y  .   ? 0.44118 0.44118 0.44118 -0.00000 0.00000  0.00000  505 HOH   C O   
18405 O O   . HOH   Y  .   ? 0.45619 0.45619 0.45619 -0.00000 0.00000  0.00000  506 HOH   C O   
18406 O O   . HOH   Y  .   ? 0.64734 0.64734 0.64734 0.00000  0.00000  0.00000  507 HOH   C O   
18407 O O   . HOH   Y  .   ? 0.53008 0.53008 0.53008 0.00000  0.00000  0.00000  508 HOH   C O   
18408 O O   . HOH   Y  .   ? 0.41417 0.41417 0.41417 -0.00000 0.00000  0.00000  509 HOH   C O   
18409 O O   . HOH   Y  .   ? 0.56105 0.56105 0.56105 -0.00000 0.00000  -0.00000 510 HOH   C O   
18410 O O   . HOH   Y  .   ? 0.28814 0.28814 0.28814 0.00000  0.00000  0.00000  511 HOH   C O   
18411 O O   . HOH   Y  .   ? 0.39191 0.39191 0.39191 0.00000  0.00000  0.00000  512 HOH   C O   
18412 O O   . HOH   Y  .   ? 0.36070 0.36070 0.36070 0.00000  0.00000  0.00000  513 HOH   C O   
18413 O O   . HOH   Y  .   ? 0.45743 0.45743 0.45743 0.00000  0.00000  0.00000  514 HOH   C O   
18414 O O   . HOH   Y  .   ? 0.34101 0.34101 0.34101 0.00000  0.00000  0.00000  515 HOH   C O   
18415 O O   . HOH   Y  .   ? 0.49352 0.49352 0.49352 0.00000  0.00000  -0.00000 516 HOH   C O   
18416 O O   . HOH   Y  .   ? 0.46843 0.46843 0.46843 0.00000  0.00000  0.00000  517 HOH   C O   
18417 O O   . HOH   Y  .   ? 0.53237 0.53237 0.53237 0.00000  0.00000  0.00000  518 HOH   C O   
18418 O O   . HOH   Y  .   ? 0.36357 0.36357 0.36357 -0.00000 0.00000  0.00000  519 HOH   C O   
18419 O O   . HOH   Y  .   ? 0.33999 0.33999 0.33999 0.00000  0.00000  0.00000  520 HOH   C O   
18420 O O   . HOH   Y  .   ? 0.28173 0.28173 0.28173 0.00000  0.00000  -0.00000 521 HOH   C O   
18421 O O   . HOH   Y  .   ? 0.46293 0.46293 0.46293 0.00000  0.00000  0.00000  522 HOH   C O   
18422 O O   . HOH   Y  .   ? 0.36313 0.36313 0.36313 -0.00000 0.00000  0.00000  523 HOH   C O   
18423 O O   . HOH   Y  .   ? 0.35642 0.35642 0.35642 -0.00000 0.00000  0.00000  524 HOH   C O   
18424 O O   . HOH   Y  .   ? 0.31787 0.31787 0.31787 0.00000  0.00000  0.00000  525 HOH   C O   
18425 O O   . HOH   Y  .   ? 0.36062 0.36062 0.36062 0.00000  0.00000  0.00000  526 HOH   C O   
18426 O O   . HOH   Y  .   ? 0.26136 0.26136 0.26136 0.00000  0.00000  0.00000  527 HOH   C O   
18427 O O   . HOH   Y  .   ? 0.44959 0.44959 0.44959 0.00000  0.00000  0.00000  528 HOH   C O   
18428 O O   . HOH   Y  .   ? 0.34979 0.34979 0.34979 0.00000  0.00000  0.00000  529 HOH   C O   
18429 O O   . HOH   Y  .   ? 0.41438 0.41438 0.41438 0.00000  0.00000  0.00000  530 HOH   C O   
18430 O O   . HOH   Y  .   ? 0.61042 0.61042 0.61042 0.00000  0.00000  0.00000  531 HOH   C O   
18431 O O   . HOH   Y  .   ? 0.43191 0.43191 0.43191 0.00000  0.00000  0.00000  532 HOH   C O   
18432 O O   . HOH   Y  .   ? 0.20670 0.20670 0.20670 -0.00000 0.00000  -0.00000 533 HOH   C O   
18433 O O   . HOH   Y  .   ? 0.45231 0.45231 0.45231 0.00000  0.00000  0.00000  534 HOH   C O   
18434 O O   . HOH   Y  .   ? 0.31489 0.31489 0.31489 -0.00000 0.00000  0.00000  535 HOH   C O   
18435 O O   . HOH   Y  .   ? 0.44167 0.44167 0.44167 0.00000  0.00000  0.00000  536 HOH   C O   
18436 O O   . HOH   Y  .   ? 0.34109 0.34109 0.34109 0.00000  0.00000  0.00000  537 HOH   C O   
18437 O O   . HOH   Y  .   ? 0.38111 0.38111 0.38111 0.00000  0.00000  0.00000  538 HOH   C O   
18438 O O   . HOH   Y  .   ? 0.31991 0.31991 0.31991 0.00000  0.00000  0.00000  539 HOH   C O   
18439 O O   . HOH   Y  .   ? 0.57499 0.57499 0.57499 0.00000  0.00000  0.00000  540 HOH   C O   
18440 O O   . HOH   Y  .   ? 0.21154 0.21154 0.21154 0.00000  0.00000  0.00000  541 HOH   C O   
18441 O O   . HOH   Y  .   ? 0.48715 0.48715 0.48715 0.00000  0.00000  0.00000  542 HOH   C O   
18442 O O   . HOH   Y  .   ? 0.41317 0.41317 0.41317 0.00000  0.00000  0.00000  543 HOH   C O   
18443 O O   . HOH   Y  .   ? 0.47845 0.47845 0.47845 0.00000  0.00000  -0.00000 544 HOH   C O   
18444 O O   . HOH   Y  .   ? 0.27766 0.27766 0.27766 -0.00000 0.00000  0.00000  545 HOH   C O   
18445 O O   . HOH   Y  .   ? 0.38990 0.38990 0.38990 0.00000  -0.00000 0.00000  546 HOH   C O   
18446 O O   . HOH   Y  .   ? 0.44536 0.44536 0.44536 -0.00000 0.00000  0.00000  547 HOH   C O   
18447 O O   . HOH   Y  .   ? 0.40759 0.40759 0.40759 -0.00000 0.00000  0.00000  548 HOH   C O   
18448 O O   . HOH   Y  .   ? 0.33363 0.33363 0.33363 -0.00000 0.00000  0.00000  549 HOH   C O   
18449 O O   . HOH   Y  .   ? 0.37936 0.37936 0.37936 -0.00000 0.00000  -0.00000 550 HOH   C O   
18450 O O   . HOH   Y  .   ? 0.48245 0.48245 0.48245 -0.00000 0.00000  0.00000  551 HOH   C O   
18451 O O   . HOH   Y  .   ? 0.62140 0.62140 0.62140 0.00000  0.00000  0.00000  552 HOH   C O   
18452 O O   . HOH   Y  .   ? 0.44622 0.44622 0.44622 0.00000  0.00000  0.00000  553 HOH   C O   
18453 O O   . HOH   Y  .   ? 0.31536 0.31536 0.31536 0.00000  0.00000  0.00000  554 HOH   C O   
18454 O O   . HOH   Y  .   ? 0.44469 0.44469 0.44469 0.00000  -0.00000 0.00000  555 HOH   C O   
18455 O O   . HOH   Y  .   ? 0.44732 0.44732 0.44732 0.00000  0.00000  0.00000  556 HOH   C O   
18456 O O   . HOH   Y  .   ? 0.69930 0.69930 0.69930 0.00000  0.00000  0.00000  557 HOH   C O   
18457 O O   . HOH   Y  .   ? 0.42267 0.42267 0.42267 0.00000  0.00000  0.00000  558 HOH   C O   
18458 O O   . HOH   Y  .   ? 0.39358 0.39358 0.39358 0.00000  0.00000  0.00000  559 HOH   C O   
18459 O O   . HOH   Y  .   ? 0.36681 0.36681 0.36681 0.00000  0.00000  0.00000  560 HOH   C O   
18460 O O   . HOH   Y  .   ? 0.34114 0.34114 0.34114 0.00000  0.00000  0.00000  561 HOH   C O   
18461 O O   . HOH   Y  .   ? 0.61372 0.61372 0.61372 -0.00000 0.00000  0.00000  562 HOH   C O   
18462 O O   . HOH   Y  .   ? 0.30365 0.30365 0.30365 0.00000  0.00000  0.00000  563 HOH   C O   
18463 O O   . HOH   Y  .   ? 0.45182 0.45182 0.45182 0.00000  0.00000  0.00000  564 HOH   C O   
18464 O O   . HOH   Y  .   ? 0.40465 0.40465 0.40465 0.00000  0.00000  0.00000  565 HOH   C O   
18465 O O   . HOH   Y  .   ? 0.08528 0.08528 0.08528 0.00000  0.00000  0.00000  566 HOH   C O   
18466 O O   . HOH   Y  .   ? 0.37083 0.37083 0.37083 -0.00000 0.00000  0.00000  567 HOH   C O   
18467 O O   . HOH   Y  .   ? 0.42467 0.42467 0.42467 0.00000  0.00000  0.00000  568 HOH   C O   
18468 O O   . HOH   Y  .   ? 0.64762 0.64762 0.64762 -0.00000 0.00000  0.00000  569 HOH   C O   
18469 O O   . HOH   Y  .   ? 0.37907 0.37907 0.37907 -0.00000 0.00000  -0.00000 570 HOH   C O   
18470 O O   . HOH   Y  .   ? 0.35049 0.35049 0.35049 -0.00000 0.00000  0.00000  571 HOH   C O   
18471 O O   . HOH   Y  .   ? 0.45450 0.45450 0.45450 0.00000  0.00000  0.00000  572 HOH   C O   
18472 O O   . HOH   Y  .   ? 0.42105 0.42105 0.42105 0.00000  0.00000  0.00000  573 HOH   C O   
18473 O O   . HOH   Y  .   ? 0.54386 0.54386 0.54386 0.00000  0.00000  0.00000  574 HOH   C O   
18474 O O   . HOH   Z  .   ? 0.39291 0.39291 0.39291 0.00000  0.00000  -0.00000 601 HOH   D O   
18475 O O   . HOH   Z  .   ? 0.49747 0.49747 0.49747 0.00000  0.00000  0.00000  602 HOH   D O   
18476 O O   . HOH   Z  .   ? 0.42999 0.42999 0.42999 0.00000  0.00000  -0.00000 603 HOH   D O   
18477 O O   . HOH   Z  .   ? 0.26346 0.26346 0.26346 0.00000  0.00000  0.00000  604 HOH   D O   
18478 O O   . HOH   Z  .   ? 0.51206 0.51206 0.51206 0.00000  0.00000  0.00000  605 HOH   D O   
18479 O O   . HOH   Z  .   ? 0.50530 0.50530 0.50530 0.00000  0.00000  0.00000  606 HOH   D O   
18480 O O   . HOH   Z  .   ? 0.34147 0.34147 0.34147 -0.00000 0.00000  0.00000  607 HOH   D O   
18481 O O   . HOH   Z  .   ? 0.43228 0.43228 0.43228 -0.00000 0.00000  0.00000  608 HOH   D O   
18482 O O   . HOH   Z  .   ? 0.54708 0.54708 0.54708 0.00000  0.00000  0.00000  609 HOH   D O   
18483 O O   . HOH   AA .   ? 0.64393 0.64393 0.64393 -0.00000 0.00000  0.00000  501 HOH   E O   
18484 O O   . HOH   AA .   ? 0.69535 0.69535 0.69535 -0.00000 0.00000  0.00000  502 HOH   E O   
18485 O O   . HOH   AA .   ? 0.86766 0.86766 0.86766 0.00000  0.00000  -0.00000 503 HOH   E O   
18486 O O   . HOH   AA .   ? 0.60231 0.60231 0.60231 0.00000  0.00000  0.00000  504 HOH   E O   
18487 O O   . HOH   AA .   ? 0.53246 0.53246 0.53246 -0.00000 0.00000  0.00000  505 HOH   E O   
18488 O O   . HOH   AA .   ? 0.39031 0.39031 0.39031 0.00000  0.00000  0.00000  506 HOH   E O   
18489 O O   . HOH   AA .   ? 0.58829 0.58829 0.58829 0.00000  0.00000  0.00000  507 HOH   E O   
18490 O O   . HOH   AA .   ? 0.40440 0.40440 0.40440 -0.00000 0.00000  0.00000  508 HOH   E O   
18491 O O   . HOH   AA .   ? 0.69239 0.69239 0.69239 0.00000  0.00000  0.00000  509 HOH   E O   
18492 O O   . HOH   AA .   ? 0.40799 0.40799 0.40799 -0.00000 0.00000  0.00000  510 HOH   E O   
18493 O O   . HOH   AA .   ? 0.36190 0.36190 0.36190 -0.00000 0.00000  0.00000  511 HOH   E O   
18494 O O   . HOH   AA .   ? 0.48478 0.48478 0.48478 0.00000  0.00000  0.00000  512 HOH   E O   
18495 O O   . HOH   AA .   ? 0.46551 0.46551 0.46551 0.00000  0.00000  0.00000  513 HOH   E O   
18496 O O   . HOH   AA .   ? 0.36724 0.36724 0.36724 0.00000  0.00000  0.00000  514 HOH   E O   
18497 O O   . HOH   AA .   ? 0.20481 0.20481 0.20481 -0.00000 0.00000  0.00000  515 HOH   E O   
18498 O O   . HOH   AA .   ? 0.55670 0.55670 0.55670 0.00000  0.00000  0.00000  516 HOH   E O   
18499 O O   . HOH   AA .   ? 0.51327 0.51327 0.51327 0.00000  0.00000  0.00000  517 HOH   E O   
18500 O O   . HOH   AA .   ? 0.25035 0.25035 0.25035 -0.00000 -0.00000 -0.00000 518 HOH   E O   
18501 O O   . HOH   AA .   ? 0.41577 0.41577 0.41577 0.00000  0.00000  0.00000  519 HOH   E O   
18502 O O   . HOH   AA .   ? 0.49633 0.49633 0.49633 -0.00000 0.00000  0.00000  520 HOH   E O   
18503 O O   . HOH   AA .   ? 0.37914 0.37914 0.37914 -0.00000 0.00000  0.00000  521 HOH   E O   
18504 O O   . HOH   AA .   ? 0.34258 0.34258 0.34258 0.00000  0.00000  0.00000  522 HOH   E O   
18505 O O   . HOH   AA .   ? 0.51720 0.51720 0.51720 -0.00000 0.00000  0.00000  523 HOH   E O   
18506 O O   . HOH   AA .   ? 0.53301 0.53301 0.53301 0.00000  0.00000  0.00000  524 HOH   E O   
18507 O O   . HOH   AA .   ? 0.29382 0.29382 0.29382 -0.00000 0.00000  0.00000  525 HOH   E O   
18508 O O   . HOH   AA .   ? 0.43766 0.43766 0.43766 0.00000  0.00000  0.00000  526 HOH   E O   
18509 O O   . HOH   AA .   ? 0.51537 0.51537 0.51537 -0.00000 0.00000  0.00000  527 HOH   E O   
18510 O O   . HOH   AA .   ? 0.20227 0.20227 0.20227 -0.00000 0.00000  0.00000  528 HOH   E O   
18511 O O   . HOH   AA .   ? 0.45473 0.45473 0.45473 0.00000  0.00000  0.00000  529 HOH   E O   
18512 O O   . HOH   AA .   ? 0.40280 0.40280 0.40280 -0.00000 0.00000  0.00000  530 HOH   E O   
18513 O O   . HOH   AA .   ? 0.35568 0.35568 0.35568 0.00000  0.00000  0.00000  531 HOH   E O   
18514 O O   . HOH   AA .   ? 0.35738 0.35738 0.35738 0.00000  0.00000  0.00000  532 HOH   E O   
18515 O O   . HOH   AA .   ? 0.40689 0.40689 0.40689 0.00000  0.00000  0.00000  533 HOH   E O   
18516 O O   . HOH   AA .   ? 0.20205 0.20205 0.20205 0.00000  0.00000  0.00000  534 HOH   E O   
18517 O O   . HOH   AA .   ? 0.48018 0.48018 0.48018 0.00000  0.00000  0.00000  535 HOH   E O   
18518 O O   . HOH   AA .   ? 0.43245 0.43245 0.43245 -0.00000 0.00000  0.00000  536 HOH   E O   
18519 O O   . HOH   AA .   ? 0.42520 0.42520 0.42520 0.00000  0.00000  0.00000  537 HOH   E O   
18520 O O   . HOH   AA .   ? 0.45300 0.45300 0.45300 0.00000  0.00000  0.00000  538 HOH   E O   
18521 O O   . HOH   AA .   ? 0.27830 0.27830 0.27830 -0.00000 0.00000  0.00000  539 HOH   E O   
18522 O O   . HOH   AA .   ? 0.44619 0.44619 0.44619 -0.00000 0.00000  0.00000  540 HOH   E O   
18523 O O   . HOH   AA .   ? 0.40303 0.40303 0.40303 0.00000  0.00000  0.00000  541 HOH   E O   
18524 O O   . HOH   AA .   ? 0.42616 0.42616 0.42616 0.00000  0.00000  0.00000  542 HOH   E O   
18525 O O   . HOH   AA .   ? 0.27753 0.27753 0.27753 0.00000  0.00000  0.00000  543 HOH   E O   
18526 O O   . HOH   AA .   ? 0.33163 0.33163 0.33163 0.00000  0.00000  0.00000  544 HOH   E O   
18527 O O   . HOH   AA .   ? 0.37115 0.37115 0.37115 0.00000  0.00000  0.00000  545 HOH   E O   
18528 O O   . HOH   AA .   ? 0.57287 0.57287 0.57287 0.00000  0.00000  0.00000  546 HOH   E O   
18529 O O   . HOH   AA .   ? 0.36874 0.36874 0.36874 0.00000  0.00000  0.00000  547 HOH   E O   
18530 O O   . HOH   AA .   ? 0.37621 0.37621 0.37621 0.00000  0.00000  0.00000  548 HOH   E O   
18531 O O   . HOH   AA .   ? 0.38157 0.38157 0.38157 0.00000  0.00000  0.00000  549 HOH   E O   
18532 O O   . HOH   AA .   ? 0.38702 0.38702 0.38702 0.00000  0.00000  0.00000  550 HOH   E O   
18533 O O   . HOH   AA .   ? 0.43940 0.43940 0.43940 -0.00000 0.00000  0.00000  551 HOH   E O   
18534 O O   . HOH   AA .   ? 0.55800 0.55800 0.55800 -0.00000 0.00000  0.00000  552 HOH   E O   
18535 O O   . HOH   AA .   ? 0.40834 0.40834 0.40834 0.00000  0.00000  0.00000  553 HOH   E O   
18536 O O   . HOH   AA .   ? 0.45501 0.45501 0.45501 0.00000  0.00000  0.00000  554 HOH   E O   
18537 O O   . HOH   AA .   ? 0.45817 0.45817 0.45817 0.00000  0.00000  0.00000  555 HOH   E O   
18538 O O   . HOH   AA .   ? 0.43766 0.43766 0.43766 0.00000  0.00000  0.00000  556 HOH   E O   
18539 O O   . HOH   AA .   ? 0.42279 0.42279 0.42279 -0.00000 0.00000  0.00000  557 HOH   E O   
18540 O O   . HOH   AA .   ? 0.38162 0.38162 0.38162 0.00000  0.00000  0.00000  558 HOH   E O   
18541 O O   . HOH   AA .   ? 0.52132 0.52132 0.52132 -0.00000 0.00000  -0.00000 559 HOH   E O   
18542 O O   . HOH   AA .   ? 0.63082 0.63082 0.63082 -0.00000 0.00000  0.00000  560 HOH   E O   
18543 O O   . HOH   AA .   ? 0.47735 0.47735 0.47735 0.00000  0.00000  0.00000  561 HOH   E O   
18544 O O   . HOH   AA .   ? 0.49185 0.49185 0.49185 -0.00000 0.00000  0.00000  562 HOH   E O   
18545 O O   . HOH   AA .   ? 0.45920 0.45920 0.45920 0.00000  0.00000  0.00000  563 HOH   E O   
18546 O O   . HOH   AA .   ? 0.44929 0.44929 0.44929 0.00000  0.00000  0.00000  564 HOH   E O   
18547 O O   . HOH   AA .   ? 0.45397 0.45397 0.45397 0.00000  0.00000  0.00000  565 HOH   E O   
18548 O O   . HOH   AA .   ? 0.23569 0.23569 0.23569 -0.00000 0.00000  0.00000  566 HOH   E O   
18549 O O   . HOH   AA .   ? 0.40396 0.40396 0.40396 0.00000  0.00000  0.00000  567 HOH   E O   
18550 O O   . HOH   AA .   ? 0.48311 0.48311 0.48311 0.00000  0.00000  0.00000  568 HOH   E O   
18551 O O   . HOH   AA .   ? 0.52899 0.52899 0.52899 -0.00000 -0.00000 0.00000  569 HOH   E O   
18552 O O   . HOH   AA .   ? 0.56165 0.56165 0.56165 -0.00000 0.00000  0.00000  570 HOH   E O   
18553 O O   . HOH   AA .   ? 0.62196 0.62196 0.62196 0.00000  0.00000  0.00000  571 HOH   E O   
18554 O O   . HOH   AA .   ? 0.36486 0.36486 0.36486 0.00000  0.00000  0.00000  572 HOH   E O   
18555 O O   . HOH   AA .   ? 0.41201 0.41201 0.41201 -0.00000 0.00000  0.00000  573 HOH   E O   
18556 O O   . HOH   BA .   ? 0.48618 0.48618 0.48618 0.00000  0.00000  -0.00000 601 HOH   F O   
18557 O O   . HOH   BA .   ? 0.43792 0.43792 0.43792 0.00000  0.00000  0.00000  602 HOH   F O   
18558 O O   . HOH   BA .   ? 0.60104 0.60104 0.60104 0.00000  0.00000  0.00000  603 HOH   F O   
18559 O O   . HOH   BA .   ? 0.38692 0.38692 0.38692 0.00000  0.00000  0.00000  604 HOH   F O   
18560 O O   . HOH   CA .   ? 0.72375 0.72375 0.72375 -0.00000 0.00000  0.00000  501 HOH   K O   
18561 O O   . HOH   CA .   ? 1.00055 1.00055 1.00055 0.00000  0.00000  0.00000  502 HOH   K O   
18562 O O   . HOH   CA .   ? 0.38927 0.38927 0.38927 0.00000  -0.00000 0.00000  503 HOH   K O   
18563 O O   . HOH   CA .   ? 0.45852 0.45852 0.45852 -0.00000 0.00000  0.00000  504 HOH   K O   
18564 O O   . HOH   CA .   ? 0.58459 0.58459 0.58459 -0.00000 0.00000  0.00000  505 HOH   K O   
18565 O O   . HOH   CA .   ? 0.45477 0.45477 0.45477 -0.00000 0.00000  0.00000  506 HOH   K O   
18566 O O   . HOH   CA .   ? 0.51536 0.51536 0.51536 0.00000  0.00000  0.00000  507 HOH   K O   
18567 O O   . HOH   CA .   ? 0.29986 0.29986 0.29986 0.00000  0.00000  0.00000  508 HOH   K O   
18568 O O   . HOH   CA .   ? 0.39433 0.39433 0.39433 -0.00000 0.00000  0.00000  509 HOH   K O   
18569 O O   . HOH   CA .   ? 0.71241 0.71241 0.71241 0.00000  0.00000  0.00000  510 HOH   K O   
18570 O O   . HOH   CA .   ? 0.38764 0.38764 0.38764 -0.00000 0.00000  -0.00000 511 HOH   K O   
18571 O O   . HOH   CA .   ? 0.39391 0.39391 0.39391 0.00000  0.00000  0.00000  512 HOH   K O   
18572 O O   . HOH   CA .   ? 0.39221 0.39221 0.39221 0.00000  0.00000  0.00000  513 HOH   K O   
18573 O O   . HOH   CA .   ? 0.38531 0.38531 0.38531 -0.00000 0.00000  0.00000  514 HOH   K O   
18574 O O   . HOH   CA .   ? 0.42659 0.42659 0.42659 0.00000  -0.00000 0.00000  515 HOH   K O   
18575 O O   . HOH   CA .   ? 0.62189 0.62189 0.62189 0.00000  0.00000  0.00000  516 HOH   K O   
18576 O O   . HOH   CA .   ? 0.39328 0.39328 0.39328 0.00000  0.00000  0.00000  517 HOH   K O   
18577 O O   . HOH   CA .   ? 0.30829 0.30829 0.30829 0.00000  0.00000  0.00000  518 HOH   K O   
18578 O O   . HOH   CA .   ? 0.81711 0.81711 0.81711 -0.00000 0.00000  0.00000  519 HOH   K O   
18579 O O   . HOH   CA .   ? 0.20023 0.20023 0.20023 -0.00000 0.00000  0.00000  520 HOH   K O   
18580 O O   . HOH   CA .   ? 1.12510 1.12510 1.12510 0.00000  0.00000  0.00000  521 HOH   K O   
18581 O O   . HOH   CA .   ? 0.60508 0.60508 0.60508 -0.00000 0.00000  0.00000  522 HOH   K O   
18582 O O   . HOH   CA .   ? 0.65731 0.65731 0.65731 0.00000  0.00000  0.00000  523 HOH   K O   
18583 O O   . HOH   CA .   ? 0.43458 0.43458 0.43458 0.00000  0.00000  0.00000  524 HOH   K O   
18584 O O   . HOH   CA .   ? 0.56975 0.56975 0.56975 0.00000  0.00000  0.00000  525 HOH   K O   
18585 O O   . HOH   CA .   ? 0.51524 0.51524 0.51524 0.00000  -0.00000 0.00000  526 HOH   K O   
18586 O O   . HOH   CA .   ? 0.60469 0.60469 0.60469 -0.00000 0.00000  0.00000  527 HOH   K O   
18587 O O   . HOH   CA .   ? 0.41559 0.41559 0.41559 0.00000  0.00000  0.00000  528 HOH   K O   
18588 O O   . HOH   CA .   ? 0.43156 0.43156 0.43156 0.00000  0.00000  0.00000  529 HOH   K O   
18589 O O   . HOH   CA .   ? 0.52050 0.52050 0.52050 0.00000  0.00000  0.00000  530 HOH   K O   
18590 O O   . HOH   CA .   ? 0.45344 0.45344 0.45344 0.00000  0.00000  0.00000  531 HOH   K O   
18591 O O   . HOH   CA .   ? 0.60031 0.60031 0.60031 0.00000  0.00000  0.00000  532 HOH   K O   
18592 O O   . HOH   CA .   ? 0.55267 0.55267 0.55267 0.00000  0.00000  0.00000  533 HOH   K O   
18593 O O   . HOH   CA .   ? 0.43375 0.43375 0.43375 0.00000  0.00000  0.00000  534 HOH   K O   
18594 O O   . HOH   DA .   ? 0.67688 0.67688 0.67688 -0.00000 0.00000  0.00000  601 HOH   L O   
# 
