data_9FT9
# 
_entry.id   9FT9 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.402 
_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   9FT9         pdb_00009ft9 10.2210/pdb9ft9/pdb 
WWPDB D_1292139680 ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
_pdbx_audit_revision_history.part_number 
1 'Structure model' 1 0 2025-02-05 ? 
2 'Structure model' 1 1 2025-02-12 ? 
3 'Structure model' 1 2 2025-03-12 ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
loop_
_pdbx_audit_revision_group.ordinal 
_pdbx_audit_revision_group.revision_ordinal 
_pdbx_audit_revision_group.data_content_type 
_pdbx_audit_revision_group.group 
1 2 'Structure model' 'Database references' 
2 3 'Structure model' 'Database references' 
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 2 'Structure model' citation        
2 2 'Structure model' citation_author 
3 3 'Structure model' citation        
4 3 'Structure model' citation_author 
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1  2 'Structure model' '_citation.title'                   
2  2 'Structure model' '_citation_author.identifier_ORCID' 
3  2 'Structure model' '_citation_author.name'             
4  3 'Structure model' '_citation.journal_volume'          
5  3 'Structure model' '_citation.page_first'              
6  3 'Structure model' '_citation.page_last'               
7  3 'Structure model' '_citation.pdbx_database_id_DOI'    
8  3 'Structure model' '_citation.pdbx_database_id_PubMed' 
9  3 'Structure model' '_citation.title'                   
10 3 'Structure model' '_citation.year'                    
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9FT9 
_pdbx_database_status.recvd_initial_deposition_date   2024-06-24 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_database_related.db_name        PDB 
_pdbx_database_related.details        'Same chain A' 
_pdbx_database_related.db_id          4UX9 
_pdbx_database_related.content_type   unspecified 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              andres.palencia@univ-grenoble-alpes.fr 
_pdbx_contact_author.name_first         Andres 
_pdbx_contact_author.name_last          Palencia 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-1805-319X 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Orand, T.'     1 ?                   
'Delaforge, E.' 2 0000-0001-8014-5100 
'Palencia, A.'  3 0000-0002-1805-319X 
'Jensen, M.R.'  4 0000-0003-0419-2196 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            Proc.Natl.Acad.Sci.USA 
_citation.journal_id_ASTM           PNASA6 
_citation.journal_id_CSD            0040 
_citation.journal_id_ISSN           1091-6490 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            122 
_citation.language                  ? 
_citation.page_first                e2419915122 
_citation.page_last                 e2419915122 
_citation.title                     'Bipartite binding of the intrinsically disordered scaffold protein JIP1 to the kinase JNK1.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1073/pnas.2419915122 
_citation.pdbx_database_id_PubMed   39999166 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Orand, T.'      1  ?                   
primary 'Delaforge, E.'  2  0000-0001-8014-5100 
primary 'Lee, A.'        3  ?                   
primary 'Kragelj, J.'    4  0000-0001-6472-8429 
primary 'Tengo, M.'      5  ?                   
primary 'Tengo, L.'      6  ?                   
primary 'Blackledge, M.' 7  ?                   
primary 'Boeri Erba, E.' 8  0000-0002-5910-4707 
primary 'Davis, R.J.'    9  0000-0002-0130-1652 
primary 'Palencia, A.'   10 ?                   
primary 'Jensen, M.R.'   11 0000-0003-0419-2196 
# 
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 'Isoform 1 of Mitogen-activated protein kinase 8'   41634.195 1   2.7.11.24 ? ? 
'GAMA is from the expression vector' 
2 polymer     man 'C-Jun-amino-terminal kinase-interacting protein 1' 4497.104  1   ?         ? ? 
;GHM belong to the expression vector tag. This is a peptide of the intrinsically disorder scaffold protein JIP1. There is a deletion of the flexible linker comprising residues 176TLNNNSLGK184
;
3 non-polymer syn 'PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER'       506.196   1   ?         ? ? ? 
4 water       nat water                                               18.015    123 ?         ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        
'MAP kinase 8,MAPK 8,JNK-46,Stress-activated protein kinase 1c,SAPK1c,Stress-activated protein kinase JNK1,c-Jun N-terminal kinase 1' 
# 
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 
;KRDNNFYSVEIGDSTFTVLKRYQNLKPIGSGAQGIVCAAYDAILERNVAIKKLSRPFQNQTHAKRAYRELVLMKCVNHKN
IIGLLNVFTPQKSLEEFQDVYIVMELMDANLCQVIQMELDHERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCT
LKILDFGLARTAGTSFMMTPYVVTRYYRAPEVILGMGYKENVDLWSVGCIMGEMVCHKILFPGRDYIDQWNKVIEQLGTP
CPEFMKKLQPTVRTYVENRPKYAGYSFEKLFPDVLFPADSEHNKLKASQARDLLSKMLVIDASKRISVDEALQHPYINVW
YDPSEAEAPPPKIPDKQLDEREHTIEEWKELIYKEVMDLE
;
;KRDNNFYSVEIGDSTFTVLKRYQNLKPIGSGAQGIVCAAYDAILERNVAIKKLSRPFQNQTHAKRAYRELVLMKCVNHKN
IIGLLNVFTPQKSLEEFQDVYIVMELMDANLCQVIQMELDHERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCT
LKILDFGLARTAGTSFMMTPYVVTRYYRAPEVILGMGYKENVDLWSVGCIMGEMVCHKILFPGRDYIDQWNKVIEQLGTP
CPEFMKKLQPTVRTYVENRPKYAGYSFEKLFPDVLFPADSEHNKLKASQARDLLSKMLVIDASKRISVDEALQHPYINVW
YDPSEAEAPPPKIPDKQLDEREHTIEEWKELIYKEVMDLE
;
A ? 
2 'polypeptide(L)' no no RPKRPTTLNLFPQVPRSQDKHSWQDRVSRSICLSDELP RPKRPTTLNLFPQVPRSQDKHSWQDRVSRSICLSDELP B ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
3 'PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER' ANP 
4 water                                         HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   LYS n 
1 2   ARG n 
1 3   ASP n 
1 4   ASN n 
1 5   ASN n 
1 6   PHE n 
1 7   TYR n 
1 8   SER n 
1 9   VAL n 
1 10  GLU n 
1 11  ILE n 
1 12  GLY n 
1 13  ASP n 
1 14  SER n 
1 15  THR n 
1 16  PHE n 
1 17  THR n 
1 18  VAL n 
1 19  LEU n 
1 20  LYS n 
1 21  ARG n 
1 22  TYR n 
1 23  GLN n 
1 24  ASN n 
1 25  LEU n 
1 26  LYS n 
1 27  PRO n 
1 28  ILE n 
1 29  GLY n 
1 30  SER n 
1 31  GLY n 
1 32  ALA n 
1 33  GLN n 
1 34  GLY n 
1 35  ILE n 
1 36  VAL n 
1 37  CYS n 
1 38  ALA n 
1 39  ALA n 
1 40  TYR n 
1 41  ASP n 
1 42  ALA n 
1 43  ILE n 
1 44  LEU n 
1 45  GLU n 
1 46  ARG n 
1 47  ASN n 
1 48  VAL n 
1 49  ALA n 
1 50  ILE n 
1 51  LYS n 
1 52  LYS n 
1 53  LEU n 
1 54  SER n 
1 55  ARG n 
1 56  PRO n 
1 57  PHE n 
1 58  GLN n 
1 59  ASN n 
1 60  GLN n 
1 61  THR n 
1 62  HIS n 
1 63  ALA n 
1 64  LYS n 
1 65  ARG n 
1 66  ALA n 
1 67  TYR n 
1 68  ARG n 
1 69  GLU n 
1 70  LEU n 
1 71  VAL n 
1 72  LEU n 
1 73  MET n 
1 74  LYS n 
1 75  CYS n 
1 76  VAL n 
1 77  ASN n 
1 78  HIS n 
1 79  LYS n 
1 80  ASN n 
1 81  ILE n 
1 82  ILE n 
1 83  GLY n 
1 84  LEU n 
1 85  LEU n 
1 86  ASN n 
1 87  VAL n 
1 88  PHE n 
1 89  THR n 
1 90  PRO n 
1 91  GLN n 
1 92  LYS n 
1 93  SER n 
1 94  LEU n 
1 95  GLU n 
1 96  GLU n 
1 97  PHE n 
1 98  GLN n 
1 99  ASP n 
1 100 VAL n 
1 101 TYR n 
1 102 ILE n 
1 103 VAL n 
1 104 MET n 
1 105 GLU n 
1 106 LEU n 
1 107 MET n 
1 108 ASP n 
1 109 ALA n 
1 110 ASN n 
1 111 LEU n 
1 112 CYS n 
1 113 GLN n 
1 114 VAL n 
1 115 ILE n 
1 116 GLN n 
1 117 MET n 
1 118 GLU n 
1 119 LEU n 
1 120 ASP n 
1 121 HIS n 
1 122 GLU n 
1 123 ARG n 
1 124 MET n 
1 125 SER n 
1 126 TYR n 
1 127 LEU n 
1 128 LEU n 
1 129 TYR n 
1 130 GLN n 
1 131 MET n 
1 132 LEU n 
1 133 CYS n 
1 134 GLY n 
1 135 ILE n 
1 136 LYS n 
1 137 HIS n 
1 138 LEU n 
1 139 HIS n 
1 140 SER n 
1 141 ALA n 
1 142 GLY n 
1 143 ILE n 
1 144 ILE n 
1 145 HIS n 
1 146 ARG n 
1 147 ASP n 
1 148 LEU n 
1 149 LYS n 
1 150 PRO n 
1 151 SER n 
1 152 ASN n 
1 153 ILE n 
1 154 VAL n 
1 155 VAL n 
1 156 LYS n 
1 157 SER n 
1 158 ASP n 
1 159 CYS n 
1 160 THR n 
1 161 LEU n 
1 162 LYS n 
1 163 ILE n 
1 164 LEU n 
1 165 ASP n 
1 166 PHE n 
1 167 GLY n 
1 168 LEU n 
1 169 ALA n 
1 170 ARG n 
1 171 THR n 
1 172 ALA n 
1 173 GLY n 
1 174 THR n 
1 175 SER n 
1 176 PHE n 
1 177 MET n 
1 178 MET n 
1 179 THR n 
1 180 PRO n 
1 181 TYR n 
1 182 VAL n 
1 183 VAL n 
1 184 THR n 
1 185 ARG n 
1 186 TYR n 
1 187 TYR n 
1 188 ARG n 
1 189 ALA n 
1 190 PRO n 
1 191 GLU n 
1 192 VAL n 
1 193 ILE n 
1 194 LEU n 
1 195 GLY n 
1 196 MET n 
1 197 GLY n 
1 198 TYR n 
1 199 LYS n 
1 200 GLU n 
1 201 ASN n 
1 202 VAL n 
1 203 ASP n 
1 204 LEU n 
1 205 TRP n 
1 206 SER n 
1 207 VAL n 
1 208 GLY n 
1 209 CYS n 
1 210 ILE n 
1 211 MET n 
1 212 GLY n 
1 213 GLU n 
1 214 MET n 
1 215 VAL n 
1 216 CYS n 
1 217 HIS n 
1 218 LYS n 
1 219 ILE n 
1 220 LEU n 
1 221 PHE n 
1 222 PRO n 
1 223 GLY n 
1 224 ARG n 
1 225 ASP n 
1 226 TYR n 
1 227 ILE n 
1 228 ASP n 
1 229 GLN n 
1 230 TRP n 
1 231 ASN n 
1 232 LYS n 
1 233 VAL n 
1 234 ILE n 
1 235 GLU n 
1 236 GLN n 
1 237 LEU n 
1 238 GLY n 
1 239 THR n 
1 240 PRO n 
1 241 CYS n 
1 242 PRO n 
1 243 GLU n 
1 244 PHE n 
1 245 MET n 
1 246 LYS n 
1 247 LYS n 
1 248 LEU n 
1 249 GLN n 
1 250 PRO n 
1 251 THR n 
1 252 VAL n 
1 253 ARG n 
1 254 THR n 
1 255 TYR n 
1 256 VAL n 
1 257 GLU n 
1 258 ASN n 
1 259 ARG n 
1 260 PRO n 
1 261 LYS n 
1 262 TYR n 
1 263 ALA n 
1 264 GLY n 
1 265 TYR n 
1 266 SER n 
1 267 PHE n 
1 268 GLU n 
1 269 LYS n 
1 270 LEU n 
1 271 PHE n 
1 272 PRO n 
1 273 ASP n 
1 274 VAL n 
1 275 LEU n 
1 276 PHE n 
1 277 PRO n 
1 278 ALA n 
1 279 ASP n 
1 280 SER n 
1 281 GLU n 
1 282 HIS n 
1 283 ASN n 
1 284 LYS n 
1 285 LEU n 
1 286 LYS n 
1 287 ALA n 
1 288 SER n 
1 289 GLN n 
1 290 ALA n 
1 291 ARG n 
1 292 ASP n 
1 293 LEU n 
1 294 LEU n 
1 295 SER n 
1 296 LYS n 
1 297 MET n 
1 298 LEU n 
1 299 VAL n 
1 300 ILE n 
1 301 ASP n 
1 302 ALA n 
1 303 SER n 
1 304 LYS n 
1 305 ARG n 
1 306 ILE n 
1 307 SER n 
1 308 VAL n 
1 309 ASP n 
1 310 GLU n 
1 311 ALA n 
1 312 LEU n 
1 313 GLN n 
1 314 HIS n 
1 315 PRO n 
1 316 TYR n 
1 317 ILE n 
1 318 ASN n 
1 319 VAL n 
1 320 TRP n 
1 321 TYR n 
1 322 ASP n 
1 323 PRO n 
1 324 SER n 
1 325 GLU n 
1 326 ALA n 
1 327 GLU n 
1 328 ALA n 
1 329 PRO n 
1 330 PRO n 
1 331 PRO n 
1 332 LYS n 
1 333 ILE n 
1 334 PRO n 
1 335 ASP n 
1 336 LYS n 
1 337 GLN n 
1 338 LEU n 
1 339 ASP n 
1 340 GLU n 
1 341 ARG n 
1 342 GLU n 
1 343 HIS n 
1 344 THR n 
1 345 ILE n 
1 346 GLU n 
1 347 GLU n 
1 348 TRP n 
1 349 LYS n 
1 350 GLU n 
1 351 LEU n 
1 352 ILE n 
1 353 TYR n 
1 354 LYS n 
1 355 GLU n 
1 356 VAL n 
1 357 MET n 
1 358 ASP n 
1 359 LEU n 
1 360 GLU n 
2 1   ARG n 
2 2   PRO n 
2 3   LYS n 
2 4   ARG n 
2 5   PRO n 
2 6   THR n 
2 7   THR n 
2 8   LEU n 
2 9   ASN n 
2 10  LEU n 
2 11  PHE n 
2 12  PRO n 
2 13  GLN n 
2 14  VAL n 
2 15  PRO n 
2 16  ARG n 
2 17  SER n 
2 18  GLN n 
2 19  ASP n 
2 20  LYS n 
2 21  HIS n 
2 22  SER n 
2 23  TRP n 
2 24  GLN n 
2 25  ASP n 
2 26  ARG n 
2 27  VAL n 
2 28  SER n 
2 29  ARG n 
2 30  SER n 
2 31  ILE n 
2 32  CYS n 
2 33  LEU n 
2 34  SER n 
2 35  ASP n 
2 36  GLU n 
2 37  LEU n 
2 38  PRO 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' 1 360 human ? 'MAPK8, JNK1, PRKM8, SAPK1, SAPK1C' ? ? ? ? ? ? 'Homo sapiens' 9606 ? ? ? ? ? ? ? ? 
'Escherichia coli BL21(DE3)' 469008 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
2 1 sample 'Biological sequence' 1 38  human ? 'MAPK8IP1, IB1, JIP1, PRKM8IP'      ? ? ? ? ? ? 'Homo sapiens' 9606 ? ? ? ? ? ? ? ? 
'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 
ALA 'L-peptide linking' y ALANINE                                       ? 'C3 H7 N O2'        89.093  
ANP non-polymer         . 'PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER' ? 'C10 H17 N6 O12 P3' 506.196 
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   LYS 1   5   ?   ?   ?   A . n 
A 1 2   ARG 2   6   ?   ?   ?   A . n 
A 1 3   ASP 3   7   7   ASP ASP A . n 
A 1 4   ASN 4   8   8   ASN ASN A . n 
A 1 5   ASN 5   9   9   ASN ASN A . n 
A 1 6   PHE 6   10  10  PHE PHE A . n 
A 1 7   TYR 7   11  11  TYR TYR A . n 
A 1 8   SER 8   12  12  SER SER A . n 
A 1 9   VAL 9   13  13  VAL VAL A . n 
A 1 10  GLU 10  14  14  GLU GLU A . n 
A 1 11  ILE 11  15  15  ILE ILE A . n 
A 1 12  GLY 12  16  16  GLY GLY A . n 
A 1 13  ASP 13  17  17  ASP ASP A . n 
A 1 14  SER 14  18  18  SER SER A . n 
A 1 15  THR 15  19  19  THR THR A . n 
A 1 16  PHE 16  20  20  PHE PHE A . n 
A 1 17  THR 17  21  21  THR THR A . n 
A 1 18  VAL 18  22  22  VAL VAL A . n 
A 1 19  LEU 19  23  23  LEU LEU A . n 
A 1 20  LYS 20  24  24  LYS LYS A . n 
A 1 21  ARG 21  25  25  ARG ARG A . n 
A 1 22  TYR 22  26  26  TYR TYR A . n 
A 1 23  GLN 23  27  27  GLN GLN A . n 
A 1 24  ASN 24  28  28  ASN ASN A . n 
A 1 25  LEU 25  29  29  LEU LEU A . n 
A 1 26  LYS 26  30  30  LYS LYS A . n 
A 1 27  PRO 27  31  31  PRO PRO A . n 
A 1 28  ILE 28  32  32  ILE ILE A . n 
A 1 29  GLY 29  33  33  GLY GLY A . n 
A 1 30  SER 30  34  34  SER SER A . n 
A 1 31  GLY 31  35  35  GLY GLY A . n 
A 1 32  ALA 32  36  36  ALA ALA A . n 
A 1 33  GLN 33  37  37  GLN GLN A . n 
A 1 34  GLY 34  38  38  GLY GLY A . n 
A 1 35  ILE 35  39  39  ILE ILE A . n 
A 1 36  VAL 36  40  40  VAL VAL A . n 
A 1 37  CYS 37  41  41  CYS CYS A . n 
A 1 38  ALA 38  42  42  ALA ALA A . n 
A 1 39  ALA 39  43  43  ALA ALA A . n 
A 1 40  TYR 40  44  44  TYR TYR A . n 
A 1 41  ASP 41  45  45  ASP ASP A . n 
A 1 42  ALA 42  46  46  ALA ALA A . n 
A 1 43  ILE 43  47  47  ILE ILE A . n 
A 1 44  LEU 44  48  48  LEU LEU A . n 
A 1 45  GLU 45  49  49  GLU GLU A . n 
A 1 46  ARG 46  50  50  ARG ARG A . n 
A 1 47  ASN 47  51  51  ASN ASN A . n 
A 1 48  VAL 48  52  52  VAL VAL A . n 
A 1 49  ALA 49  53  53  ALA ALA A . n 
A 1 50  ILE 50  54  54  ILE ILE A . n 
A 1 51  LYS 51  55  55  LYS LYS A . n 
A 1 52  LYS 52  56  56  LYS LYS A . n 
A 1 53  LEU 53  57  57  LEU LEU A . n 
A 1 54  SER 54  58  58  SER SER A . n 
A 1 55  ARG 55  59  59  ARG ARG A . n 
A 1 56  PRO 56  60  60  PRO PRO A . n 
A 1 57  PHE 57  61  61  PHE PHE A . n 
A 1 58  GLN 58  62  62  GLN GLN A . n 
A 1 59  ASN 59  63  63  ASN ASN A . n 
A 1 60  GLN 60  64  64  GLN GLN A . n 
A 1 61  THR 61  65  65  THR THR A . n 
A 1 62  HIS 62  66  66  HIS HIS A . n 
A 1 63  ALA 63  67  67  ALA ALA A . n 
A 1 64  LYS 64  68  68  LYS LYS A . n 
A 1 65  ARG 65  69  69  ARG ARG A . n 
A 1 66  ALA 66  70  70  ALA ALA A . n 
A 1 67  TYR 67  71  71  TYR TYR A . n 
A 1 68  ARG 68  72  72  ARG ARG A . n 
A 1 69  GLU 69  73  73  GLU GLU A . n 
A 1 70  LEU 70  74  74  LEU LEU A . n 
A 1 71  VAL 71  75  75  VAL VAL A . n 
A 1 72  LEU 72  76  76  LEU LEU A . n 
A 1 73  MET 73  77  77  MET MET A . n 
A 1 74  LYS 74  78  78  LYS LYS A . n 
A 1 75  CYS 75  79  79  CYS CYS A . n 
A 1 76  VAL 76  80  80  VAL VAL A . n 
A 1 77  ASN 77  81  81  ASN ASN A . n 
A 1 78  HIS 78  82  82  HIS HIS A . n 
A 1 79  LYS 79  83  83  LYS LYS A . n 
A 1 80  ASN 80  84  84  ASN ASN A . n 
A 1 81  ILE 81  85  85  ILE ILE A . n 
A 1 82  ILE 82  86  86  ILE ILE A . n 
A 1 83  GLY 83  87  87  GLY GLY A . n 
A 1 84  LEU 84  88  88  LEU LEU A . n 
A 1 85  LEU 85  89  89  LEU LEU A . n 
A 1 86  ASN 86  90  90  ASN ASN A . n 
A 1 87  VAL 87  91  91  VAL VAL A . n 
A 1 88  PHE 88  92  92  PHE PHE A . n 
A 1 89  THR 89  93  93  THR THR A . n 
A 1 90  PRO 90  94  94  PRO PRO A . n 
A 1 91  GLN 91  95  95  GLN GLN A . n 
A 1 92  LYS 92  96  96  LYS LYS A . n 
A 1 93  SER 93  97  97  SER SER A . n 
A 1 94  LEU 94  98  98  LEU LEU A . n 
A 1 95  GLU 95  99  99  GLU GLU A . n 
A 1 96  GLU 96  100 100 GLU GLU A . n 
A 1 97  PHE 97  101 101 PHE PHE A . n 
A 1 98  GLN 98  102 102 GLN GLN A . n 
A 1 99  ASP 99  103 103 ASP ASP A . n 
A 1 100 VAL 100 104 104 VAL VAL A . n 
A 1 101 TYR 101 105 105 TYR TYR A . n 
A 1 102 ILE 102 106 106 ILE ILE A . n 
A 1 103 VAL 103 107 107 VAL VAL A . n 
A 1 104 MET 104 108 108 MET MET A . n 
A 1 105 GLU 105 109 109 GLU GLU A . n 
A 1 106 LEU 106 110 110 LEU LEU A . n 
A 1 107 MET 107 111 111 MET MET A . n 
A 1 108 ASP 108 112 112 ASP ASP A . n 
A 1 109 ALA 109 113 113 ALA ALA A . n 
A 1 110 ASN 110 114 114 ASN ASN A . n 
A 1 111 LEU 111 115 115 LEU LEU A . n 
A 1 112 CYS 112 116 116 CYS CYS A . n 
A 1 113 GLN 113 117 117 GLN GLN A . n 
A 1 114 VAL 114 118 118 VAL VAL A . n 
A 1 115 ILE 115 119 119 ILE ILE A . n 
A 1 116 GLN 116 120 120 GLN GLN A . n 
A 1 117 MET 117 121 121 MET MET A . n 
A 1 118 GLU 118 122 122 GLU GLU A . n 
A 1 119 LEU 119 123 123 LEU LEU A . n 
A 1 120 ASP 120 124 124 ASP ASP A . n 
A 1 121 HIS 121 125 125 HIS HIS A . n 
A 1 122 GLU 122 126 126 GLU GLU A . n 
A 1 123 ARG 123 127 127 ARG ARG A . n 
A 1 124 MET 124 128 128 MET MET A . n 
A 1 125 SER 125 129 129 SER SER A . n 
A 1 126 TYR 126 130 130 TYR TYR A . n 
A 1 127 LEU 127 131 131 LEU LEU A . n 
A 1 128 LEU 128 132 132 LEU LEU A . n 
A 1 129 TYR 129 133 133 TYR TYR A . n 
A 1 130 GLN 130 134 134 GLN GLN A . n 
A 1 131 MET 131 135 135 MET MET A . n 
A 1 132 LEU 132 136 136 LEU LEU A . n 
A 1 133 CYS 133 137 137 CYS CYS A . n 
A 1 134 GLY 134 138 138 GLY GLY A . n 
A 1 135 ILE 135 139 139 ILE ILE A . n 
A 1 136 LYS 136 140 140 LYS LYS A . n 
A 1 137 HIS 137 141 141 HIS HIS A . n 
A 1 138 LEU 138 142 142 LEU LEU A . n 
A 1 139 HIS 139 143 143 HIS HIS A . n 
A 1 140 SER 140 144 144 SER SER A . n 
A 1 141 ALA 141 145 145 ALA ALA A . n 
A 1 142 GLY 142 146 146 GLY GLY A . n 
A 1 143 ILE 143 147 147 ILE ILE A . n 
A 1 144 ILE 144 148 148 ILE ILE A . n 
A 1 145 HIS 145 149 149 HIS HIS A . n 
A 1 146 ARG 146 150 150 ARG ARG A . n 
A 1 147 ASP 147 151 151 ASP ASP A . n 
A 1 148 LEU 148 152 152 LEU LEU A . n 
A 1 149 LYS 149 153 153 LYS LYS A . n 
A 1 150 PRO 150 154 154 PRO PRO A . n 
A 1 151 SER 151 155 155 SER SER A . n 
A 1 152 ASN 152 156 156 ASN ASN A . n 
A 1 153 ILE 153 157 157 ILE ILE A . n 
A 1 154 VAL 154 158 158 VAL VAL A . n 
A 1 155 VAL 155 159 159 VAL VAL A . n 
A 1 156 LYS 156 160 160 LYS LYS A . n 
A 1 157 SER 157 161 161 SER SER A . n 
A 1 158 ASP 158 162 162 ASP ASP A . n 
A 1 159 CYS 159 163 163 CYS CYS A . n 
A 1 160 THR 160 164 164 THR THR A . n 
A 1 161 LEU 161 165 165 LEU LEU A . n 
A 1 162 LYS 162 166 166 LYS LYS A . n 
A 1 163 ILE 163 167 167 ILE ILE A . n 
A 1 164 LEU 164 168 168 LEU LEU A . n 
A 1 165 ASP 165 169 169 ASP ASP A . n 
A 1 166 PHE 166 170 170 PHE PHE A . n 
A 1 167 GLY 167 171 171 GLY GLY A . n 
A 1 168 LEU 168 172 172 LEU LEU A . n 
A 1 169 ALA 169 173 173 ALA ALA A . n 
A 1 170 ARG 170 174 174 ARG ARG A . n 
A 1 171 THR 171 175 175 THR THR A . n 
A 1 172 ALA 172 176 176 ALA ALA A . n 
A 1 173 GLY 173 177 177 GLY GLY A . n 
A 1 174 THR 174 178 178 THR THR A . n 
A 1 175 SER 175 179 179 SER SER A . n 
A 1 176 PHE 176 180 180 PHE PHE A . n 
A 1 177 MET 177 181 181 MET MET A . n 
A 1 178 MET 178 182 182 MET MET A . n 
A 1 179 THR 179 183 183 THR THR A . n 
A 1 180 PRO 180 184 184 PRO PRO A . n 
A 1 181 TYR 181 185 185 TYR TYR A . n 
A 1 182 VAL 182 186 186 VAL VAL A . n 
A 1 183 VAL 183 187 187 VAL VAL A . n 
A 1 184 THR 184 188 188 THR THR A . n 
A 1 185 ARG 185 189 189 ARG ARG A . n 
A 1 186 TYR 186 190 190 TYR TYR A . n 
A 1 187 TYR 187 191 191 TYR TYR A . n 
A 1 188 ARG 188 192 192 ARG ARG A . n 
A 1 189 ALA 189 193 193 ALA ALA A . n 
A 1 190 PRO 190 194 194 PRO PRO A . n 
A 1 191 GLU 191 195 195 GLU GLU A . n 
A 1 192 VAL 192 196 196 VAL VAL A . n 
A 1 193 ILE 193 197 197 ILE ILE A . n 
A 1 194 LEU 194 198 198 LEU LEU A . n 
A 1 195 GLY 195 199 199 GLY GLY A . n 
A 1 196 MET 196 200 200 MET MET A . n 
A 1 197 GLY 197 201 201 GLY GLY A . n 
A 1 198 TYR 198 202 202 TYR TYR A . n 
A 1 199 LYS 199 203 203 LYS LYS A . n 
A 1 200 GLU 200 204 204 GLU GLU A . n 
A 1 201 ASN 201 205 205 ASN ASN A . n 
A 1 202 VAL 202 206 206 VAL VAL A . n 
A 1 203 ASP 203 207 207 ASP ASP A . n 
A 1 204 LEU 204 208 208 LEU LEU A . n 
A 1 205 TRP 205 209 209 TRP TRP A . n 
A 1 206 SER 206 210 210 SER SER A . n 
A 1 207 VAL 207 211 211 VAL VAL A . n 
A 1 208 GLY 208 212 212 GLY GLY A . n 
A 1 209 CYS 209 213 213 CYS CYS A . n 
A 1 210 ILE 210 214 214 ILE ILE A . n 
A 1 211 MET 211 215 215 MET MET A . n 
A 1 212 GLY 212 216 216 GLY GLY A . n 
A 1 213 GLU 213 217 217 GLU GLU A . n 
A 1 214 MET 214 218 218 MET MET A . n 
A 1 215 VAL 215 219 219 VAL VAL A . n 
A 1 216 CYS 216 220 220 CYS CYS A . n 
A 1 217 HIS 217 221 221 HIS HIS A . n 
A 1 218 LYS 218 222 222 LYS LYS A . n 
A 1 219 ILE 219 223 223 ILE ILE A . n 
A 1 220 LEU 220 224 224 LEU LEU A . n 
A 1 221 PHE 221 225 225 PHE PHE A . n 
A 1 222 PRO 222 226 226 PRO PRO A . n 
A 1 223 GLY 223 227 227 GLY GLY A . n 
A 1 224 ARG 224 228 228 ARG ARG A . n 
A 1 225 ASP 225 229 229 ASP ASP A . n 
A 1 226 TYR 226 230 230 TYR TYR A . n 
A 1 227 ILE 227 231 231 ILE ILE A . n 
A 1 228 ASP 228 232 232 ASP ASP A . n 
A 1 229 GLN 229 233 233 GLN GLN A . n 
A 1 230 TRP 230 234 234 TRP TRP A . n 
A 1 231 ASN 231 235 235 ASN ASN A . n 
A 1 232 LYS 232 236 236 LYS LYS A . n 
A 1 233 VAL 233 237 237 VAL VAL A . n 
A 1 234 ILE 234 238 238 ILE ILE A . n 
A 1 235 GLU 235 239 239 GLU GLU A . n 
A 1 236 GLN 236 240 240 GLN GLN A . n 
A 1 237 LEU 237 241 241 LEU LEU A . n 
A 1 238 GLY 238 242 242 GLY GLY A . n 
A 1 239 THR 239 243 243 THR THR A . n 
A 1 240 PRO 240 244 244 PRO PRO A . n 
A 1 241 CYS 241 245 245 CYS CYS A . n 
A 1 242 PRO 242 246 246 PRO PRO A . n 
A 1 243 GLU 243 247 247 GLU GLU A . n 
A 1 244 PHE 244 248 248 PHE PHE A . n 
A 1 245 MET 245 249 249 MET MET A . n 
A 1 246 LYS 246 250 250 LYS LYS A . n 
A 1 247 LYS 247 251 251 LYS LYS A . n 
A 1 248 LEU 248 252 252 LEU LEU A . n 
A 1 249 GLN 249 253 253 GLN GLN A . n 
A 1 250 PRO 250 254 254 PRO PRO A . n 
A 1 251 THR 251 255 255 THR THR A . n 
A 1 252 VAL 252 256 256 VAL VAL A . n 
A 1 253 ARG 253 257 257 ARG ARG A . n 
A 1 254 THR 254 258 258 THR THR A . n 
A 1 255 TYR 255 259 259 TYR TYR A . n 
A 1 256 VAL 256 260 260 VAL VAL A . n 
A 1 257 GLU 257 261 261 GLU GLU A . n 
A 1 258 ASN 258 262 262 ASN ASN A . n 
A 1 259 ARG 259 263 263 ARG ARG A . n 
A 1 260 PRO 260 264 264 PRO PRO A . n 
A 1 261 LYS 261 265 265 LYS LYS A . n 
A 1 262 TYR 262 266 266 TYR TYR A . n 
A 1 263 ALA 263 267 267 ALA ALA A . n 
A 1 264 GLY 264 268 268 GLY GLY A . n 
A 1 265 TYR 265 269 269 TYR TYR A . n 
A 1 266 SER 266 270 270 SER SER A . n 
A 1 267 PHE 267 271 271 PHE PHE A . n 
A 1 268 GLU 268 272 272 GLU GLU A . n 
A 1 269 LYS 269 273 273 LYS LYS A . n 
A 1 270 LEU 270 274 274 LEU LEU A . n 
A 1 271 PHE 271 275 275 PHE PHE A . n 
A 1 272 PRO 272 276 276 PRO PRO A . n 
A 1 273 ASP 273 277 277 ASP ASP A . n 
A 1 274 VAL 274 278 278 VAL VAL A . n 
A 1 275 LEU 275 279 279 LEU LEU A . n 
A 1 276 PHE 276 280 280 PHE PHE A . n 
A 1 277 PRO 277 281 281 PRO PRO A . n 
A 1 278 ALA 278 282 282 ALA ALA A . n 
A 1 279 ASP 279 283 283 ASP ASP A . n 
A 1 280 SER 280 284 284 SER SER A . n 
A 1 281 GLU 281 285 285 GLU GLU A . n 
A 1 282 HIS 282 286 286 HIS HIS A . n 
A 1 283 ASN 283 287 287 ASN ASN A . n 
A 1 284 LYS 284 288 288 LYS LYS A . n 
A 1 285 LEU 285 289 289 LEU LEU A . n 
A 1 286 LYS 286 290 290 LYS LYS A . n 
A 1 287 ALA 287 291 291 ALA ALA A . n 
A 1 288 SER 288 292 292 SER SER A . n 
A 1 289 GLN 289 293 293 GLN GLN A . n 
A 1 290 ALA 290 294 294 ALA ALA A . n 
A 1 291 ARG 291 295 295 ARG ARG A . n 
A 1 292 ASP 292 296 296 ASP ASP A . n 
A 1 293 LEU 293 297 297 LEU LEU A . n 
A 1 294 LEU 294 298 298 LEU LEU A . n 
A 1 295 SER 295 299 299 SER SER A . n 
A 1 296 LYS 296 300 300 LYS LYS A . n 
A 1 297 MET 297 301 301 MET MET A . n 
A 1 298 LEU 298 302 302 LEU LEU A . n 
A 1 299 VAL 299 303 303 VAL VAL A . n 
A 1 300 ILE 300 304 304 ILE ILE A . n 
A 1 301 ASP 301 305 305 ASP ASP A . n 
A 1 302 ALA 302 306 306 ALA ALA A . n 
A 1 303 SER 303 307 307 SER SER A . n 
A 1 304 LYS 304 308 308 LYS LYS A . n 
A 1 305 ARG 305 309 309 ARG ARG A . n 
A 1 306 ILE 306 310 310 ILE ILE A . n 
A 1 307 SER 307 311 311 SER SER A . n 
A 1 308 VAL 308 312 312 VAL VAL A . n 
A 1 309 ASP 309 313 313 ASP ASP A . n 
A 1 310 GLU 310 314 314 GLU GLU A . n 
A 1 311 ALA 311 315 315 ALA ALA A . n 
A 1 312 LEU 312 316 316 LEU LEU A . n 
A 1 313 GLN 313 317 317 GLN GLN A . n 
A 1 314 HIS 314 318 318 HIS HIS A . n 
A 1 315 PRO 315 319 319 PRO PRO A . n 
A 1 316 TYR 316 320 320 TYR TYR A . n 
A 1 317 ILE 317 321 321 ILE ILE A . n 
A 1 318 ASN 318 322 322 ASN ASN A . n 
A 1 319 VAL 319 323 323 VAL VAL A . n 
A 1 320 TRP 320 324 324 TRP TRP A . n 
A 1 321 TYR 321 325 325 TYR TYR A . n 
A 1 322 ASP 322 326 326 ASP ASP A . n 
A 1 323 PRO 323 327 327 PRO PRO A . n 
A 1 324 SER 324 328 328 SER SER A . n 
A 1 325 GLU 325 329 329 GLU GLU A . n 
A 1 326 ALA 326 330 330 ALA ALA A . n 
A 1 327 GLU 327 331 331 GLU GLU A . n 
A 1 328 ALA 328 332 332 ALA ALA A . n 
A 1 329 PRO 329 333 333 PRO PRO A . n 
A 1 330 PRO 330 334 334 PRO PRO A . n 
A 1 331 PRO 331 335 335 PRO PRO A . n 
A 1 332 LYS 332 336 336 LYS LYS A . n 
A 1 333 ILE 333 337 337 ILE ILE A . n 
A 1 334 PRO 334 338 338 PRO PRO A . n 
A 1 335 ASP 335 339 339 ASP ASP A . n 
A 1 336 LYS 336 340 340 LYS LYS A . n 
A 1 337 GLN 337 341 341 GLN GLN A . n 
A 1 338 LEU 338 342 342 LEU LEU A . n 
A 1 339 ASP 339 343 343 ASP ASP A . n 
A 1 340 GLU 340 344 344 GLU GLU A . n 
A 1 341 ARG 341 345 345 ARG ARG A . n 
A 1 342 GLU 342 346 346 GLU GLU A . n 
A 1 343 HIS 343 347 347 HIS HIS A . n 
A 1 344 THR 344 348 348 THR THR A . n 
A 1 345 ILE 345 349 349 ILE ILE A . n 
A 1 346 GLU 346 350 350 GLU GLU A . n 
A 1 347 GLU 347 351 351 GLU GLU A . n 
A 1 348 TRP 348 352 352 TRP TRP A . n 
A 1 349 LYS 349 353 353 LYS LYS A . n 
A 1 350 GLU 350 354 354 GLU GLU A . n 
A 1 351 LEU 351 355 355 LEU LEU A . n 
A 1 352 ILE 352 356 356 ILE ILE A . n 
A 1 353 TYR 353 357 357 TYR TYR A . n 
A 1 354 LYS 354 358 358 LYS LYS A . n 
A 1 355 GLU 355 359 359 GLU GLU A . n 
A 1 356 VAL 356 360 360 VAL VAL A . n 
A 1 357 MET 357 361 361 MET MET A . n 
A 1 358 ASP 358 362 362 ASP ASP A . n 
A 1 359 LEU 359 363 363 LEU LEU A . n 
A 1 360 GLU 360 364 ?   ?   ?   A . n 
B 2 1   ARG 1   157 157 ARG ARG B . n 
B 2 2   PRO 2   158 158 PRO PRO B . n 
B 2 3   LYS 3   159 159 LYS LYS B . n 
B 2 4   ARG 4   160 160 ARG ARG B . n 
B 2 5   PRO 5   161 161 PRO PRO B . n 
B 2 6   THR 6   162 162 THR THR B . n 
B 2 7   THR 7   163 163 THR THR B . n 
B 2 8   LEU 8   164 164 LEU LEU B . n 
B 2 9   ASN 9   165 165 ASN ASN B . n 
B 2 10  LEU 10  166 166 LEU LEU B . n 
B 2 11  PHE 11  167 167 PHE PHE B . n 
B 2 12  PRO 12  168 168 PRO PRO B . n 
B 2 13  GLN 13  169 169 GLN GLN B . n 
B 2 14  VAL 14  170 170 VAL VAL B . n 
B 2 15  PRO 15  195 ?   ?   ?   B . n 
B 2 16  ARG 16  196 ?   ?   ?   B . n 
B 2 17  SER 17  197 ?   ?   ?   B . n 
B 2 18  GLN 18  198 ?   ?   ?   B . n 
B 2 19  ASP 19  199 ?   ?   ?   B . n 
B 2 20  LYS 20  200 ?   ?   ?   B . n 
B 2 21  HIS 21  201 ?   ?   ?   B . n 
B 2 22  SER 22  202 ?   ?   ?   B . n 
B 2 23  TRP 23  203 ?   ?   ?   B . n 
B 2 24  GLN 24  204 ?   ?   ?   B . n 
B 2 25  ASP 25  205 ?   ?   ?   B . n 
B 2 26  ARG 26  206 ?   ?   ?   B . n 
B 2 27  VAL 27  207 ?   ?   ?   B . n 
B 2 28  SER 28  208 ?   ?   ?   B . n 
B 2 29  ARG 29  209 ?   ?   ?   B . n 
B 2 30  SER 30  210 210 SER SER B . n 
B 2 31  ILE 31  211 211 ILE ILE B . n 
B 2 32  CYS 32  212 212 CYS CYS B . n 
B 2 33  LEU 33  213 213 LEU LEU B . n 
B 2 34  SER 34  214 214 SER SER B . n 
B 2 35  ASP 35  215 215 ASP ASP B . n 
B 2 36  GLU 36  216 216 GLU GLU B . n 
B 2 37  LEU 37  217 217 LEU LEU B . n 
B 2 38  PRO 38  218 218 PRO PRO B . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        ANP 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   ANP 
_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 
C 3 ANP 1   401 401 ANP ANP A . 
D 4 HOH 1   501 112 HOH HOH A . 
D 4 HOH 2   502 115 HOH HOH A . 
D 4 HOH 3   503 1   HOH HOH A . 
D 4 HOH 4   504 95  HOH HOH A . 
D 4 HOH 5   505 11  HOH HOH A . 
D 4 HOH 6   506 5   HOH HOH A . 
D 4 HOH 7   507 30  HOH HOH A . 
D 4 HOH 8   508 27  HOH HOH A . 
D 4 HOH 9   509 48  HOH HOH A . 
D 4 HOH 10  510 108 HOH HOH A . 
D 4 HOH 11  511 12  HOH HOH A . 
D 4 HOH 12  512 100 HOH HOH A . 
D 4 HOH 13  513 123 HOH HOH A . 
D 4 HOH 14  514 45  HOH HOH A . 
D 4 HOH 15  515 77  HOH HOH A . 
D 4 HOH 16  516 40  HOH HOH A . 
D 4 HOH 17  517 16  HOH HOH A . 
D 4 HOH 18  518 4   HOH HOH A . 
D 4 HOH 19  519 14  HOH HOH A . 
D 4 HOH 20  520 29  HOH HOH A . 
D 4 HOH 21  521 75  HOH HOH A . 
D 4 HOH 22  522 43  HOH HOH A . 
D 4 HOH 23  523 121 HOH HOH A . 
D 4 HOH 24  524 28  HOH HOH A . 
D 4 HOH 25  525 3   HOH HOH A . 
D 4 HOH 26  526 44  HOH HOH A . 
D 4 HOH 27  527 25  HOH HOH A . 
D 4 HOH 28  528 38  HOH HOH A . 
D 4 HOH 29  529 34  HOH HOH A . 
D 4 HOH 30  530 72  HOH HOH A . 
D 4 HOH 31  531 92  HOH HOH A . 
D 4 HOH 32  532 42  HOH HOH A . 
D 4 HOH 33  533 7   HOH HOH A . 
D 4 HOH 34  534 15  HOH HOH A . 
D 4 HOH 35  535 111 HOH HOH A . 
D 4 HOH 36  536 81  HOH HOH A . 
D 4 HOH 37  537 114 HOH HOH A . 
D 4 HOH 38  538 18  HOH HOH A . 
D 4 HOH 39  539 23  HOH HOH A . 
D 4 HOH 40  540 122 HOH HOH A . 
D 4 HOH 41  541 22  HOH HOH A . 
D 4 HOH 42  542 6   HOH HOH A . 
D 4 HOH 43  543 39  HOH HOH A . 
D 4 HOH 44  544 120 HOH HOH A . 
D 4 HOH 45  545 99  HOH HOH A . 
D 4 HOH 46  546 105 HOH HOH A . 
D 4 HOH 47  547 9   HOH HOH A . 
D 4 HOH 48  548 13  HOH HOH A . 
D 4 HOH 49  549 68  HOH HOH A . 
D 4 HOH 50  550 41  HOH HOH A . 
D 4 HOH 51  551 94  HOH HOH A . 
D 4 HOH 52  552 17  HOH HOH A . 
D 4 HOH 53  553 90  HOH HOH A . 
D 4 HOH 54  554 20  HOH HOH A . 
D 4 HOH 55  555 74  HOH HOH A . 
D 4 HOH 56  556 10  HOH HOH A . 
D 4 HOH 57  557 49  HOH HOH A . 
D 4 HOH 58  558 76  HOH HOH A . 
D 4 HOH 59  559 26  HOH HOH A . 
D 4 HOH 60  560 66  HOH HOH A . 
D 4 HOH 61  561 36  HOH HOH A . 
D 4 HOH 62  562 109 HOH HOH A . 
D 4 HOH 63  563 86  HOH HOH A . 
D 4 HOH 64  564 32  HOH HOH A . 
D 4 HOH 65  565 19  HOH HOH A . 
D 4 HOH 66  566 2   HOH HOH A . 
D 4 HOH 67  567 52  HOH HOH A . 
D 4 HOH 68  568 31  HOH HOH A . 
D 4 HOH 69  569 73  HOH HOH A . 
D 4 HOH 70  570 78  HOH HOH A . 
D 4 HOH 71  571 64  HOH HOH A . 
D 4 HOH 72  572 46  HOH HOH A . 
D 4 HOH 73  573 55  HOH HOH A . 
D 4 HOH 74  574 21  HOH HOH A . 
D 4 HOH 75  575 67  HOH HOH A . 
D 4 HOH 76  576 65  HOH HOH A . 
D 4 HOH 77  577 71  HOH HOH A . 
D 4 HOH 78  578 53  HOH HOH A . 
D 4 HOH 79  579 101 HOH HOH A . 
D 4 HOH 80  580 69  HOH HOH A . 
D 4 HOH 81  581 113 HOH HOH A . 
D 4 HOH 82  582 37  HOH HOH A . 
D 4 HOH 83  583 50  HOH HOH A . 
D 4 HOH 84  584 47  HOH HOH A . 
D 4 HOH 85  585 83  HOH HOH A . 
D 4 HOH 86  586 85  HOH HOH A . 
D 4 HOH 87  587 59  HOH HOH A . 
D 4 HOH 88  588 103 HOH HOH A . 
D 4 HOH 89  589 35  HOH HOH A . 
D 4 HOH 90  590 91  HOH HOH A . 
D 4 HOH 91  591 104 HOH HOH A . 
D 4 HOH 92  592 61  HOH HOH A . 
D 4 HOH 93  593 57  HOH HOH A . 
D 4 HOH 94  594 56  HOH HOH A . 
D 4 HOH 95  595 107 HOH HOH A . 
D 4 HOH 96  596 96  HOH HOH A . 
D 4 HOH 97  597 89  HOH HOH A . 
D 4 HOH 98  598 93  HOH HOH A . 
D 4 HOH 99  599 54  HOH HOH A . 
D 4 HOH 100 600 98  HOH HOH A . 
D 4 HOH 101 601 63  HOH HOH A . 
D 4 HOH 102 602 118 HOH HOH A . 
D 4 HOH 103 603 117 HOH HOH A . 
D 4 HOH 104 604 24  HOH HOH A . 
D 4 HOH 105 605 80  HOH HOH A . 
D 4 HOH 106 606 51  HOH HOH A . 
D 4 HOH 107 607 87  HOH HOH A . 
D 4 HOH 108 608 70  HOH HOH A . 
D 4 HOH 109 609 60  HOH HOH A . 
D 4 HOH 110 610 84  HOH HOH A . 
D 4 HOH 111 611 33  HOH HOH A . 
D 4 HOH 112 612 62  HOH HOH A . 
D 4 HOH 113 613 97  HOH HOH A . 
D 4 HOH 114 614 82  HOH HOH A . 
D 4 HOH 115 615 116 HOH HOH A . 
D 4 HOH 116 616 119 HOH HOH A . 
E 4 HOH 1   301 8   HOH HOH B . 
E 4 HOH 2   302 88  HOH HOH B . 
E 4 HOH 3   303 106 HOH HOH B . 
E 4 HOH 4   304 58  HOH HOH B . 
E 4 HOH 5   305 79  HOH HOH B . 
E 4 HOH 6   306 110 HOH HOH B . 
E 4 HOH 7   307 102 HOH HOH B . 
# 
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 A ASP 7   ? CG  ? A ASP 3   CG  
2 1 Y 1 A ASP 7   ? OD1 ? A ASP 3   OD1 
3 1 Y 1 A ASP 7   ? OD2 ? A ASP 3   OD2 
4 1 Y 1 A LEU 363 ? CG  ? A LEU 359 CG  
5 1 Y 1 A LEU 363 ? CD1 ? A LEU 359 CD1 
6 1 Y 1 A LEU 363 ? CD2 ? A LEU 359 CD2 
# 
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 ? ? ? 1.19_4080 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? 2023      2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? XSCALE ? ? ? 2023      3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER ? ? ? 2.8.3     4 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.000 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  120.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9FT9 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     137.700 
_cell.length_a_esd                 ? 
_cell.length_b                     137.700 
_cell.length_b_esd                 ? 
_cell.length_c                     63.950 
_cell.length_c_esd                 ? 
_cell.volume                       1050120.317 
_cell.volume_esd                   ? 
_cell.Z_PDB                        6 
_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                         9FT9 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                152 
_symmetry.space_group_name_Hall            
;P 31 2"
;
_symmetry.space_group_name_H-M             'P 31 2 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                   9FT9 
_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             3.8 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          68 
_exptl_crystal.description                  rods 
_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              5.5 
_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    
;20% w/v PEG 3350, 
0.1 M Bis Tris propane pH 6.5, 
0.2 M sodium acetate trihydrate
;
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            277 
# 
_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         2024-05-24 
_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                    'Silicon crystal' 
_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   0.96546 
_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                        'ESRF BEAMLINE MASSIF-1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.96546 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   MASSIF-1 
_diffrn_source.pdbx_synchrotron_site       ESRF 
# 
_reflns.B_iso_Wilson_estimate                          75.21 
_reflns.entry_id                                       9FT9 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.35 
_reflns.d_resolution_low                               46.86 
_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                                     29338 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           99.9 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                15.03 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          13.2 
_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                                0.14 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.99 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    2.35 
_reflns_shell.d_res_low                                     2.43 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             2790 
_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                               12.8 
_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                               1.7 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.20 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          99.9 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               87.96 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  
;TLS refinement in phenix.refine
B-factors are total (local + TLS + crystal)
;
_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                                 9FT9 
_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                            2.35 
_refine.ls_d_res_low                             46.86 
_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                     29318 
_refine.ls_number_reflns_R_free                  1484 
_refine.ls_number_reflns_R_work                  27834 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.89 
_refine.ls_percent_reflns_R_free                 5.06 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2336 
_refine.ls_R_factor_R_free                       0.2701 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2313 
_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                          1.33 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       '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             1.1100 
_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                 41.4863 
_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                            0.5322 
_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                       2.35 
_refine_hist.d_res_low                        46.86 
_refine_hist.number_atoms_solvent             123 
_refine_hist.number_atoms_total               3221 
_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        3067 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         31 
_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' ? 0.0092 ? 3169 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.1153 ? 4296 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0572 ? 476  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0101 ? 544  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 9.1905 ? 424  ? f_dihedral_angle_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' 2.35 2.43  . . 117 2489 99.20  . . . . 0.4390 . . . . . . . . . . . 0.4531 
'X-RAY DIFFRACTION' 2.43 2.51  . . 113 2546 100.00 . . . . 0.4404 . . . . . . . . . . . 0.5444 
'X-RAY DIFFRACTION' 2.51 2.61  . . 131 2502 99.96  . . . . 0.3810 . . . . . . . . . . . 0.4428 
'X-RAY DIFFRACTION' 2.61 2.73  . . 129 2508 100.00 . . . . 0.3298 . . . . . . . . . . . 0.3609 
'X-RAY DIFFRACTION' 2.73 2.88  . . 154 2509 100.00 . . . . 0.3055 . . . . . . . . . . . 0.3341 
'X-RAY DIFFRACTION' 2.88 3.06  . . 117 2542 100.00 . . . . 0.3026 . . . . . . . . . . . 0.3309 
'X-RAY DIFFRACTION' 3.06 3.29  . . 154 2489 99.96  . . . . 0.2852 . . . . . . . . . . . 0.3365 
'X-RAY DIFFRACTION' 3.29 3.62  . . 126 2550 100.00 . . . . 0.2435 . . . . . . . . . . . 0.3415 
'X-RAY DIFFRACTION' 3.62 4.15  . . 97  2559 99.74  . . . . 0.2087 . . . . . . . . . . . 0.3057 
'X-RAY DIFFRACTION' 4.15 5.22  . . 179 2524 100.00 . . . . 0.1904 . . . . . . . . . . . 0.2277 
'X-RAY DIFFRACTION' 5.22 46.86 . . 167 2616 99.96  . . . . 0.1932 . . . . . . . . . . . 0.2131 
# 
_struct.entry_id                     9FT9 
_struct.title                        'Structure of the bipartite JNK1-JIP1 complex' 
_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        9FT9 
_struct_keywords.text            
;c-Jun N-terminal kinase 1 (JNK-1) Serine/threonine-protein kinase cell proliferation, differentiation, migration, transformation programmed cell death, SIGNALING PROTEIN
;
_struct_keywords.pdbx_keywords   'SIGNALING PROTEIN' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 4 ? 
E 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 MK08_HUMAN P45983 P45983-2 1 
;KRDNNFYSVEIGDSTFTVLKRYQNLKPIGSGAQGIVCAAYDAILERNVAIKKLSRPFQNQTHAKRAYRELVLMKCVNHKN
IIGLLNVFTPQKSLEEFQDVYIVMELMDANLCQVIQMELDHERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCT
LKILDFGLARTAGTSFMMTPYVVTRYYRAPEVILGMGYKENVDLWSVGCIMGEMVCHKILFPGRDYIDQWNKVIEQLGTP
CPEFMKKLQPTVRTYVENRPKYAGYSFEKLFPDVLFPADSEHNKLKASQARDLLSKMLVIDASKRISVDEALQHPYINVW
YDPSEAEAPPPKIPDKQLDEREHTIEEWKELIYKEVMDLE
;
5 
2 PDB 9FT9       9FT9   ?        2 ? 1 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 9FT9 A 1 ? 360 ? P45983 5   ? 364 ? 5   364 
2 2 9FT9 B 1 ? 38  ? 9FT9   157 ? 218 ? 157 218 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 3260  ? 
1 MORE         -17   ? 
1 'SSA (A^2)'  17230 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E 
# 
loop_
_pdbx_struct_assembly_auth_evidence.id 
_pdbx_struct_assembly_auth_evidence.assembly_id 
_pdbx_struct_assembly_auth_evidence.experimental_support 
_pdbx_struct_assembly_auth_evidence.details 
1 1 'NMR Distance Restraints'          ? 
2 1 'isothermal titration calorimetry' ? 
3 1 'gel filtration'                   ? 
# 
_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 PRO A 56  ? GLN A 58  ? PRO A 60  GLN A 62  5 ? 3  
HELX_P HELX_P2  AA2 ASN A 59  ? VAL A 76  ? ASN A 63  VAL A 80  1 ? 18 
HELX_P HELX_P3  AA3 LEU A 111 ? MET A 117 ? LEU A 115 MET A 121 1 ? 7  
HELX_P HELX_P4  AA4 ASP A 120 ? SER A 140 ? ASP A 124 SER A 144 1 ? 21 
HELX_P HELX_P5  AA5 LYS A 149 ? SER A 151 ? LYS A 153 SER A 155 5 ? 3  
HELX_P HELX_P6  AA6 ALA A 189 ? GLY A 195 ? ALA A 193 GLY A 199 1 ? 7  
HELX_P HELX_P7  AA7 ASN A 201 ? HIS A 217 ? ASN A 205 HIS A 221 1 ? 17 
HELX_P HELX_P8  AA8 ASP A 225 ? GLY A 238 ? ASP A 229 GLY A 242 1 ? 14 
HELX_P HELX_P9  AA9 CYS A 241 ? LYS A 247 ? CYS A 245 LYS A 251 1 ? 7  
HELX_P HELX_P10 AB1 GLN A 249 ? ASN A 258 ? GLN A 253 ASN A 262 1 ? 10 
HELX_P HELX_P11 AB2 SER A 266 ? PHE A 271 ? SER A 270 PHE A 275 1 ? 6  
HELX_P HELX_P12 AB3 PRO A 272 ? PHE A 276 ? PRO A 276 PHE A 280 5 ? 5  
HELX_P HELX_P13 AB4 LYS A 286 ? LEU A 298 ? LYS A 290 LEU A 302 1 ? 13 
HELX_P HELX_P14 AB5 ASP A 301 ? ARG A 305 ? ASP A 305 ARG A 309 5 ? 5  
HELX_P HELX_P15 AB6 SER A 307 ? GLN A 313 ? SER A 311 GLN A 317 1 ? 7  
HELX_P HELX_P16 AB7 HIS A 314 ? VAL A 319 ? HIS A 318 VAL A 323 1 ? 6  
HELX_P HELX_P17 AB8 ASP A 322 ? GLU A 327 ? ASP A 326 GLU A 331 1 ? 6  
HELX_P HELX_P18 AB9 THR A 344 ? LEU A 359 ? THR A 348 LEU A 363 1 ? 16 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 2 ? 
AA2 ? 5 ? 
AA3 ? 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 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 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 PHE A 6   ? ILE A 11  ? PHE A 10  ILE A 15  
AA1 2 SER A 14  ? LEU A 19  ? SER A 18  LEU A 23  
AA2 1 TYR A 22  ? GLY A 31  ? TYR A 26  GLY A 35  
AA2 2 GLY A 34  ? ASP A 41  ? GLY A 38  ASP A 45  
AA2 3 ARG A 46  ? SER A 54  ? ARG A 50  SER A 58  
AA2 4 ASP A 99  ? GLU A 105 ? ASP A 103 GLU A 109 
AA2 5 LEU A 84  ? PHE A 88  ? LEU A 88  PHE A 92  
AA3 1 ALA A 109 ? ASN A 110 ? ALA A 113 ASN A 114 
AA3 2 ILE A 153 ? VAL A 155 ? ILE A 157 VAL A 159 
AA3 3 LEU A 161 ? ILE A 163 ? LEU A 165 ILE A 167 
# 
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 VAL A 9   ? N VAL A 13  O PHE A 16  ? O PHE A 20  
AA2 1 2 N GLN A 23  ? N GLN A 27  O TYR A 40  ? O TYR A 44  
AA2 2 3 N ALA A 39  ? N ALA A 43  O VAL A 48  ? O VAL A 52  
AA2 3 4 N ALA A 49  ? N ALA A 53  O MET A 104 ? O MET A 108 
AA2 4 5 O VAL A 103 ? O VAL A 107 N ASN A 86  ? N ASN A 90  
AA3 1 2 N ALA A 109 ? N ALA A 113 O VAL A 155 ? O VAL A 159 
AA3 2 3 N VAL A 154 ? N VAL A 158 O LYS A 162 ? O LYS A 166 
# 
_pdbx_entry_details.entry_id                   9FT9 
_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   N 
# 
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 O  B PHE 167 ? ? O   B HOH 301 ? ? 1.98 
2 1 O  A PHE 248 ? ? O   A HOH 501 ? ? 2.09 
3 1 OG A SER 270 ? ? OE1 A GLU 272 ? ? 2.11 
4 1 N  B CYS 212 ? ? OE2 B GLU 216 ? ? 2.19 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ARG A 59  ? ? 34.82   53.89   
2 1 GLN A 102 ? ? -125.70 -51.28  
3 1 ASP A 169 ? ? 58.94   78.24   
4 1 LYS A 203 ? ? -103.90 -169.41 
# 
_pdbx_validate_planes.id              1 
_pdbx_validate_planes.PDB_model_num   1 
_pdbx_validate_planes.auth_comp_id    ARG 
_pdbx_validate_planes.auth_asym_id    A 
_pdbx_validate_planes.auth_seq_id     192 
_pdbx_validate_planes.PDB_ins_code    ? 
_pdbx_validate_planes.label_alt_id    ? 
_pdbx_validate_planes.rmsd            0.099 
_pdbx_validate_planes.type            'SIDE CHAIN' 
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1 x,y,z          
2 -y,x-y,z+1/3   
3 -x+y,-x,z+2/3  
4 x-y,-y,-z+2/3  
5 -x,-x+y,-z+1/3 
6 y,x,-z         
# 
loop_
_pdbx_refine_tls.id 
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[1][1]_esd 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][2]_esd 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[1][3]_esd 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[2][2]_esd 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.T[2][3]_esd 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[3][3]_esd 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[1][1]_esd 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][2]_esd 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[1][3]_esd 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[2][2]_esd 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.L[2][3]_esd 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[3][3]_esd 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][1]_esd 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][2]_esd 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[1][3]_esd 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][1]_esd 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][2]_esd 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[2][3]_esd 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][1]_esd 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][2]_esd 
_pdbx_refine_tls.S[3][3] 
_pdbx_refine_tls.S[3][3]_esd 
1 'X-RAY DIFFRACTION' ? refined -49.1300664934 65.8581690221 -1.92393255282 0.672249026466 ? -0.131288647611 ? -0.0472041956906 ? 
0.701461977716 ? 0.079368530193    ? 0.635946223762 ? 2.46099180774    ? 0.676692234982   ? 1.32625496844    ? 2.04060354147   ? 
0.447652246952  ? 1.90972487592   ? -0.240194247664 ? 0.215038617157   ? 0.251932882698  ? -0.37461852674    ? 0.154286083719  ? 
0.0459752756868   ? -0.287127244618 ? 0.485545803645  ? 2.75621418681e-05 ? 
2 'X-RAY DIFFRACTION' ? refined -47.1333825615 38.9723775655 10.2567997155  0.528665724149 ? 0.0412941378676 ? -0.0596290515763 ? 
0.716093217476 ? 0.0400507711349   ? 0.730725815672 ? 1.85761382749    ? 0.529794329102   ? 0.409955526197   ? 3.15869937278   ? 
1.36453108578   ? 2.82906936188   ? 0.0897347595386 ? -0.0556678982186 ? -0.444537910764 ? 0.213997040644    ? 0.138420016495  ? 
-0.443631926395   ? 0.34695580754   ? 0.568160599924  ? 8.90243137655e-05 ? 
3 'X-RAY DIFFRACTION' ? refined -60.3036097542 51.9702697413 2.32255584165  0.653288169301 ? 0.0102274406245 ? -0.108227239386  ? 
0.6600489729   ? -0.00805499834515 ? 0.753202446564 ? 1.11890199144    ? 0.700475542941   ? 0.308030260164   ? 1.80743556355   ? 
0.0719574452266 ? 0.124454139581  ? -0.160737608563 ? 0.124070646315   ? -0.231706286394 ? -0.28583630955    ? 0.0270863676413 ? 
0.511230558585    ? 0.282322427021  ? -0.108514209267 ? 0.000457455236323 ? 
4 'X-RAY DIFFRACTION' ? refined -44.3508526786 56.0179664578 25.9540955654  0.913340825534 ? -0.146576562982 ? -0.190856462925  ? 
0.969567654549 ? 0.149679082771    ? 0.595501170605 ? 0.23567837823    ? -0.172946515197  ? 0.0203957338514  ? 0.396202832334  ? 
0.19019973763   ? 0.158053389691  ? -0.444116854248 ? -0.160433614249  ? -0.222155906405 ? 0.706129671943    ? -0.558778702604 ? 
-0.530390672856   ? 0.0248417124657 ? 0.518449180305  ? -0.0304903034219  ? 
5 'X-RAY DIFFRACTION' ? refined -42.1587489337 34.2644349341 -9.24224762076 1.49465096162  ? -0.206319302248 ? 0.263824628569   ? 
1.22410455909  ? -0.117860943786   ? 1.33554520626  ? 0.00952241853369 ? 0.00770969239486 ? 0.00811903259159 ? 0.0565314628203 ? 
0.0264709015153 ? 0.0145881263843 ? 0.434153029186  ? 0.248181863693   ? -0.361484139888 ? -0.00201445643717 ? 0.122419166431  ? 
-0.00758104704852 ? -0.278211641589 ? 0.0991457397255 ? 0.000946715655638 ? 
# 
loop_
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_PDB_ins_code 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_PDB_ins_code 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
1 'X-RAY DIFFRACTION' 1 A 1   A 7   ? A 108 A 114 ? ? 
;chain 'A' and (resid    7  through  114 )
;
2 'X-RAY DIFFRACTION' 2 A 109 A 115 ? A 305 A 311 ? ? 
;chain 'A' and (resid  115  through  311 )
;
3 'X-RAY DIFFRACTION' 3 A 306 A 312 ? A 357 A 363 ? ? 
;chain 'A' and (resid  312  through  363 )
;
4 'X-RAY DIFFRACTION' 4 C 1   B 157 ? C 14  B 170 ? ? 
;chain 'B' and (resid  157  through  170 )
;
5 'X-RAY DIFFRACTION' 5 C 15  B 210 ? C 23  B 218 ? ? 
;chain 'B' and (resid  210  through  218 )
;
# 
loop_
_pdbx_distant_solvent_atoms.id 
_pdbx_distant_solvent_atoms.PDB_model_num 
_pdbx_distant_solvent_atoms.auth_atom_id 
_pdbx_distant_solvent_atoms.label_alt_id 
_pdbx_distant_solvent_atoms.auth_asym_id 
_pdbx_distant_solvent_atoms.auth_comp_id 
_pdbx_distant_solvent_atoms.auth_seq_id 
_pdbx_distant_solvent_atoms.PDB_ins_code 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance 
1 1 O ? A HOH 615 ? 6.05 . 
2 1 O ? A HOH 616 ? 6.18 . 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A LYS 5   ? A LYS 1   
2  1 Y 1 A ARG 6   ? A ARG 2   
3  1 Y 1 A GLU 364 ? A GLU 360 
4  1 Y 1 B PRO 195 ? B PRO 15  
5  1 Y 1 B ARG 196 ? B ARG 16  
6  1 Y 1 B SER 197 ? B SER 17  
7  1 Y 1 B GLN 198 ? B GLN 18  
8  1 Y 1 B ASP 199 ? B ASP 19  
9  1 Y 1 B LYS 200 ? B LYS 20  
10 1 Y 1 B HIS 201 ? B HIS 21  
11 1 Y 1 B SER 202 ? B SER 22  
12 1 Y 1 B TRP 203 ? B TRP 23  
13 1 Y 1 B GLN 204 ? B GLN 24  
14 1 Y 1 B ASP 205 ? B ASP 25  
15 1 Y 1 B ARG 206 ? B ARG 26  
16 1 Y 1 B VAL 207 ? B VAL 27  
17 1 Y 1 B SER 208 ? B SER 28  
18 1 Y 1 B ARG 209 ? B ARG 29  
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N      N N N 1   
ALA CA     C N S 2   
ALA C      C N N 3   
ALA O      O N N 4   
ALA CB     C N N 5   
ALA OXT    O N N 6   
ALA H      H N N 7   
ALA H2     H N N 8   
ALA HA     H N N 9   
ALA HB1    H N N 10  
ALA HB2    H N N 11  
ALA HB3    H N N 12  
ALA HXT    H N N 13  
ANP PG     P N N 14  
ANP O1G    O N N 15  
ANP O2G    O N N 16  
ANP O3G    O N N 17  
ANP PB     P N N 18  
ANP O1B    O N N 19  
ANP O2B    O N N 20  
ANP N3B    N N N 21  
ANP PA     P N N 22  
ANP O1A    O N N 23  
ANP O2A    O N N 24  
ANP O3A    O N N 25  
ANP "O5'"  O N N 26  
ANP "C5'"  C N N 27  
ANP "C4'"  C N R 28  
ANP "O4'"  O N N 29  
ANP "C3'"  C N S 30  
ANP "O3'"  O N N 31  
ANP "C2'"  C N R 32  
ANP "O2'"  O N N 33  
ANP "C1'"  C N R 34  
ANP N9     N Y N 35  
ANP C8     C Y N 36  
ANP N7     N Y N 37  
ANP C5     C Y N 38  
ANP C6     C Y N 39  
ANP N6     N N N 40  
ANP N1     N Y N 41  
ANP C2     C Y N 42  
ANP N3     N Y N 43  
ANP C4     C Y N 44  
ANP HOG2   H N N 45  
ANP HOG3   H N N 46  
ANP HOB2   H N N 47  
ANP HNB1   H N N 48  
ANP HOA2   H N N 49  
ANP "H5'1" H N N 50  
ANP "H5'2" H N N 51  
ANP "H4'"  H N N 52  
ANP "H3'"  H N N 53  
ANP "HO3'" H N N 54  
ANP "H2'"  H N N 55  
ANP "HO2'" H N N 56  
ANP "H1'"  H N N 57  
ANP H8     H N N 58  
ANP HN61   H N N 59  
ANP HN62   H N N 60  
ANP H2     H N N 61  
ARG N      N N N 62  
ARG CA     C N S 63  
ARG C      C N N 64  
ARG O      O N N 65  
ARG CB     C N N 66  
ARG CG     C N N 67  
ARG CD     C N N 68  
ARG NE     N N N 69  
ARG CZ     C N N 70  
ARG NH1    N N N 71  
ARG NH2    N N N 72  
ARG OXT    O N N 73  
ARG H      H N N 74  
ARG H2     H N N 75  
ARG HA     H N N 76  
ARG HB2    H N N 77  
ARG HB3    H N N 78  
ARG HG2    H N N 79  
ARG HG3    H N N 80  
ARG HD2    H N N 81  
ARG HD3    H N N 82  
ARG HE     H N N 83  
ARG HH11   H N N 84  
ARG HH12   H N N 85  
ARG HH21   H N N 86  
ARG HH22   H N N 87  
ARG HXT    H N N 88  
ASN N      N N N 89  
ASN CA     C N S 90  
ASN C      C N N 91  
ASN O      O N N 92  
ASN CB     C N N 93  
ASN CG     C N N 94  
ASN OD1    O N N 95  
ASN ND2    N N N 96  
ASN OXT    O N N 97  
ASN H      H N N 98  
ASN H2     H N N 99  
ASN HA     H N N 100 
ASN HB2    H N N 101 
ASN HB3    H N N 102 
ASN HD21   H N N 103 
ASN HD22   H N N 104 
ASN HXT    H N N 105 
ASP N      N N N 106 
ASP CA     C N S 107 
ASP C      C N N 108 
ASP O      O N N 109 
ASP CB     C N N 110 
ASP CG     C N N 111 
ASP OD1    O N N 112 
ASP OD2    O N N 113 
ASP OXT    O N N 114 
ASP H      H N N 115 
ASP H2     H N N 116 
ASP HA     H N N 117 
ASP HB2    H N N 118 
ASP HB3    H N N 119 
ASP HD2    H N N 120 
ASP HXT    H N N 121 
CYS N      N N N 122 
CYS CA     C N R 123 
CYS C      C N N 124 
CYS O      O N N 125 
CYS CB     C N N 126 
CYS SG     S N N 127 
CYS OXT    O N N 128 
CYS H      H N N 129 
CYS H2     H N N 130 
CYS HA     H N N 131 
CYS HB2    H N N 132 
CYS HB3    H N N 133 
CYS HG     H N N 134 
CYS HXT    H N N 135 
GLN N      N N N 136 
GLN CA     C N S 137 
GLN C      C N N 138 
GLN O      O N N 139 
GLN CB     C N N 140 
GLN CG     C N N 141 
GLN CD     C N N 142 
GLN OE1    O N N 143 
GLN NE2    N N N 144 
GLN OXT    O N N 145 
GLN H      H N N 146 
GLN H2     H N N 147 
GLN HA     H N N 148 
GLN HB2    H N N 149 
GLN HB3    H N N 150 
GLN HG2    H N N 151 
GLN HG3    H N N 152 
GLN HE21   H N N 153 
GLN HE22   H N N 154 
GLN HXT    H N N 155 
GLU N      N N N 156 
GLU CA     C N S 157 
GLU C      C N N 158 
GLU O      O N N 159 
GLU CB     C N N 160 
GLU CG     C N N 161 
GLU CD     C N N 162 
GLU OE1    O N N 163 
GLU OE2    O N N 164 
GLU OXT    O N N 165 
GLU H      H N N 166 
GLU H2     H N N 167 
GLU HA     H N N 168 
GLU HB2    H N N 169 
GLU HB3    H N N 170 
GLU HG2    H N N 171 
GLU HG3    H N N 172 
GLU HE2    H N N 173 
GLU HXT    H N N 174 
GLY N      N N N 175 
GLY CA     C N N 176 
GLY C      C N N 177 
GLY O      O N N 178 
GLY OXT    O N N 179 
GLY H      H N N 180 
GLY H2     H N N 181 
GLY HA2    H N N 182 
GLY HA3    H N N 183 
GLY HXT    H N N 184 
HIS N      N N N 185 
HIS CA     C N S 186 
HIS C      C N N 187 
HIS O      O N N 188 
HIS CB     C N N 189 
HIS CG     C Y N 190 
HIS ND1    N Y N 191 
HIS CD2    C Y N 192 
HIS CE1    C Y N 193 
HIS NE2    N Y N 194 
HIS OXT    O N N 195 
HIS H      H N N 196 
HIS H2     H N N 197 
HIS HA     H N N 198 
HIS HB2    H N N 199 
HIS HB3    H N N 200 
HIS HD1    H N N 201 
HIS HD2    H N N 202 
HIS HE1    H N N 203 
HIS HE2    H N N 204 
HIS HXT    H N N 205 
HOH O      O N N 206 
HOH H1     H N N 207 
HOH H2     H N N 208 
ILE N      N N N 209 
ILE CA     C N S 210 
ILE C      C N N 211 
ILE O      O N N 212 
ILE CB     C N S 213 
ILE CG1    C N N 214 
ILE CG2    C N N 215 
ILE CD1    C N N 216 
ILE OXT    O N N 217 
ILE H      H N N 218 
ILE H2     H N N 219 
ILE HA     H N N 220 
ILE HB     H N N 221 
ILE HG12   H N N 222 
ILE HG13   H N N 223 
ILE HG21   H N N 224 
ILE HG22   H N N 225 
ILE HG23   H N N 226 
ILE HD11   H N N 227 
ILE HD12   H N N 228 
ILE HD13   H N N 229 
ILE HXT    H N N 230 
LEU N      N N N 231 
LEU CA     C N S 232 
LEU C      C N N 233 
LEU O      O N N 234 
LEU CB     C N N 235 
LEU CG     C N N 236 
LEU CD1    C N N 237 
LEU CD2    C N N 238 
LEU OXT    O N N 239 
LEU H      H N N 240 
LEU H2     H N N 241 
LEU HA     H N N 242 
LEU HB2    H N N 243 
LEU HB3    H N N 244 
LEU HG     H N N 245 
LEU HD11   H N N 246 
LEU HD12   H N N 247 
LEU HD13   H N N 248 
LEU HD21   H N N 249 
LEU HD22   H N N 250 
LEU HD23   H N N 251 
LEU HXT    H N N 252 
LYS N      N N N 253 
LYS CA     C N S 254 
LYS C      C N N 255 
LYS O      O N N 256 
LYS CB     C N N 257 
LYS CG     C N N 258 
LYS CD     C N N 259 
LYS CE     C N N 260 
LYS NZ     N N N 261 
LYS OXT    O N N 262 
LYS H      H N N 263 
LYS H2     H N N 264 
LYS HA     H N N 265 
LYS HB2    H N N 266 
LYS HB3    H N N 267 
LYS HG2    H N N 268 
LYS HG3    H N N 269 
LYS HD2    H N N 270 
LYS HD3    H N N 271 
LYS HE2    H N N 272 
LYS HE3    H N N 273 
LYS HZ1    H N N 274 
LYS HZ2    H N N 275 
LYS HZ3    H N N 276 
LYS HXT    H N N 277 
MET N      N N N 278 
MET CA     C N S 279 
MET C      C N N 280 
MET O      O N N 281 
MET CB     C N N 282 
MET CG     C N N 283 
MET SD     S N N 284 
MET CE     C N N 285 
MET OXT    O N N 286 
MET H      H N N 287 
MET H2     H N N 288 
MET HA     H N N 289 
MET HB2    H N N 290 
MET HB3    H N N 291 
MET HG2    H N N 292 
MET HG3    H N N 293 
MET HE1    H N N 294 
MET HE2    H N N 295 
MET HE3    H N N 296 
MET HXT    H N N 297 
PHE N      N N N 298 
PHE CA     C N S 299 
PHE C      C N N 300 
PHE O      O N N 301 
PHE CB     C N N 302 
PHE CG     C Y N 303 
PHE CD1    C Y N 304 
PHE CD2    C Y N 305 
PHE CE1    C Y N 306 
PHE CE2    C Y N 307 
PHE CZ     C Y N 308 
PHE OXT    O N N 309 
PHE H      H N N 310 
PHE H2     H N N 311 
PHE HA     H N N 312 
PHE HB2    H N N 313 
PHE HB3    H N N 314 
PHE HD1    H N N 315 
PHE HD2    H N N 316 
PHE HE1    H N N 317 
PHE HE2    H N N 318 
PHE HZ     H N N 319 
PHE HXT    H N N 320 
PRO N      N N N 321 
PRO CA     C N S 322 
PRO C      C N N 323 
PRO O      O N N 324 
PRO CB     C N N 325 
PRO CG     C N N 326 
PRO CD     C N N 327 
PRO OXT    O N N 328 
PRO H      H N N 329 
PRO HA     H N N 330 
PRO HB2    H N N 331 
PRO HB3    H N N 332 
PRO HG2    H N N 333 
PRO HG3    H N N 334 
PRO HD2    H N N 335 
PRO HD3    H N N 336 
PRO HXT    H N N 337 
SER N      N N N 338 
SER CA     C N S 339 
SER C      C N N 340 
SER O      O N N 341 
SER CB     C N N 342 
SER OG     O N N 343 
SER OXT    O N N 344 
SER H      H N N 345 
SER H2     H N N 346 
SER HA     H N N 347 
SER HB2    H N N 348 
SER HB3    H N N 349 
SER HG     H N N 350 
SER HXT    H N N 351 
THR N      N N N 352 
THR CA     C N S 353 
THR C      C N N 354 
THR O      O N N 355 
THR CB     C N R 356 
THR OG1    O N N 357 
THR CG2    C N N 358 
THR OXT    O N N 359 
THR H      H N N 360 
THR H2     H N N 361 
THR HA     H N N 362 
THR HB     H N N 363 
THR HG1    H N N 364 
THR HG21   H N N 365 
THR HG22   H N N 366 
THR HG23   H N N 367 
THR HXT    H N N 368 
TRP N      N N N 369 
TRP CA     C N S 370 
TRP C      C N N 371 
TRP O      O N N 372 
TRP CB     C N N 373 
TRP CG     C Y N 374 
TRP CD1    C Y N 375 
TRP CD2    C Y N 376 
TRP NE1    N Y N 377 
TRP CE2    C Y N 378 
TRP CE3    C Y N 379 
TRP CZ2    C Y N 380 
TRP CZ3    C Y N 381 
TRP CH2    C Y N 382 
TRP OXT    O N N 383 
TRP H      H N N 384 
TRP H2     H N N 385 
TRP HA     H N N 386 
TRP HB2    H N N 387 
TRP HB3    H N N 388 
TRP HD1    H N N 389 
TRP HE1    H N N 390 
TRP HE3    H N N 391 
TRP HZ2    H N N 392 
TRP HZ3    H N N 393 
TRP HH2    H N N 394 
TRP HXT    H N N 395 
TYR N      N N N 396 
TYR CA     C N S 397 
TYR C      C N N 398 
TYR O      O N N 399 
TYR CB     C N N 400 
TYR CG     C Y N 401 
TYR CD1    C Y N 402 
TYR CD2    C Y N 403 
TYR CE1    C Y N 404 
TYR CE2    C Y N 405 
TYR CZ     C Y N 406 
TYR OH     O N N 407 
TYR OXT    O N N 408 
TYR H      H N N 409 
TYR H2     H N N 410 
TYR HA     H N N 411 
TYR HB2    H N N 412 
TYR HB3    H N N 413 
TYR HD1    H N N 414 
TYR HD2    H N N 415 
TYR HE1    H N N 416 
TYR HE2    H N N 417 
TYR HH     H N N 418 
TYR HXT    H N N 419 
VAL N      N N N 420 
VAL CA     C N S 421 
VAL C      C N N 422 
VAL O      O N N 423 
VAL CB     C N N 424 
VAL CG1    C N N 425 
VAL CG2    C N N 426 
VAL OXT    O N N 427 
VAL H      H N N 428 
VAL H2     H N N 429 
VAL HA     H N N 430 
VAL HB     H N N 431 
VAL HG11   H N N 432 
VAL HG12   H N N 433 
VAL HG13   H N N 434 
VAL HG21   H N N 435 
VAL HG22   H N N 436 
VAL HG23   H N N 437 
VAL HXT    H N N 438 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N     CA     sing N N 1   
ALA N     H      sing N N 2   
ALA N     H2     sing N N 3   
ALA CA    C      sing N N 4   
ALA CA    CB     sing N N 5   
ALA CA    HA     sing N N 6   
ALA C     O      doub N N 7   
ALA C     OXT    sing N N 8   
ALA CB    HB1    sing N N 9   
ALA CB    HB2    sing N N 10  
ALA CB    HB3    sing N N 11  
ALA OXT   HXT    sing N N 12  
ANP PG    O1G    doub N N 13  
ANP PG    O2G    sing N N 14  
ANP PG    O3G    sing N N 15  
ANP PG    N3B    sing N N 16  
ANP O2G   HOG2   sing N N 17  
ANP O3G   HOG3   sing N N 18  
ANP PB    O1B    doub N N 19  
ANP PB    O2B    sing N N 20  
ANP PB    N3B    sing N N 21  
ANP PB    O3A    sing N N 22  
ANP O2B   HOB2   sing N N 23  
ANP N3B   HNB1   sing N N 24  
ANP PA    O1A    doub N N 25  
ANP PA    O2A    sing N N 26  
ANP PA    O3A    sing N N 27  
ANP PA    "O5'"  sing N N 28  
ANP O2A   HOA2   sing N N 29  
ANP "O5'" "C5'"  sing N N 30  
ANP "C5'" "C4'"  sing N N 31  
ANP "C5'" "H5'1" sing N N 32  
ANP "C5'" "H5'2" sing N N 33  
ANP "C4'" "O4'"  sing N N 34  
ANP "C4'" "C3'"  sing N N 35  
ANP "C4'" "H4'"  sing N N 36  
ANP "O4'" "C1'"  sing N N 37  
ANP "C3'" "O3'"  sing N N 38  
ANP "C3'" "C2'"  sing N N 39  
ANP "C3'" "H3'"  sing N N 40  
ANP "O3'" "HO3'" sing N N 41  
ANP "C2'" "O2'"  sing N N 42  
ANP "C2'" "C1'"  sing N N 43  
ANP "C2'" "H2'"  sing N N 44  
ANP "O2'" "HO2'" sing N N 45  
ANP "C1'" N9     sing N N 46  
ANP "C1'" "H1'"  sing N N 47  
ANP N9    C8     sing Y N 48  
ANP N9    C4     sing Y N 49  
ANP C8    N7     doub Y N 50  
ANP C8    H8     sing N N 51  
ANP N7    C5     sing Y N 52  
ANP C5    C6     sing Y N 53  
ANP C5    C4     doub Y N 54  
ANP C6    N6     sing N N 55  
ANP C6    N1     doub Y N 56  
ANP N6    HN61   sing N N 57  
ANP N6    HN62   sing N N 58  
ANP N1    C2     sing Y N 59  
ANP C2    N3     doub Y N 60  
ANP C2    H2     sing N N 61  
ANP N3    C4     sing Y N 62  
ARG N     CA     sing N N 63  
ARG N     H      sing N N 64  
ARG N     H2     sing N N 65  
ARG CA    C      sing N N 66  
ARG CA    CB     sing N N 67  
ARG CA    HA     sing N N 68  
ARG C     O      doub N N 69  
ARG C     OXT    sing N N 70  
ARG CB    CG     sing N N 71  
ARG CB    HB2    sing N N 72  
ARG CB    HB3    sing N N 73  
ARG CG    CD     sing N N 74  
ARG CG    HG2    sing N N 75  
ARG CG    HG3    sing N N 76  
ARG CD    NE     sing N N 77  
ARG CD    HD2    sing N N 78  
ARG CD    HD3    sing N N 79  
ARG NE    CZ     sing N N 80  
ARG NE    HE     sing N N 81  
ARG CZ    NH1    sing N N 82  
ARG CZ    NH2    doub N N 83  
ARG NH1   HH11   sing N N 84  
ARG NH1   HH12   sing N N 85  
ARG NH2   HH21   sing N N 86  
ARG NH2   HH22   sing N N 87  
ARG OXT   HXT    sing N N 88  
ASN N     CA     sing N N 89  
ASN N     H      sing N N 90  
ASN N     H2     sing N N 91  
ASN CA    C      sing N N 92  
ASN CA    CB     sing N N 93  
ASN CA    HA     sing N N 94  
ASN C     O      doub N N 95  
ASN C     OXT    sing N N 96  
ASN CB    CG     sing N N 97  
ASN CB    HB2    sing N N 98  
ASN CB    HB3    sing N N 99  
ASN CG    OD1    doub N N 100 
ASN CG    ND2    sing N N 101 
ASN ND2   HD21   sing N N 102 
ASN ND2   HD22   sing N N 103 
ASN OXT   HXT    sing N N 104 
ASP N     CA     sing N N 105 
ASP N     H      sing N N 106 
ASP N     H2     sing N N 107 
ASP CA    C      sing N N 108 
ASP CA    CB     sing N N 109 
ASP CA    HA     sing N N 110 
ASP C     O      doub N N 111 
ASP C     OXT    sing N N 112 
ASP CB    CG     sing N N 113 
ASP CB    HB2    sing N N 114 
ASP CB    HB3    sing N N 115 
ASP CG    OD1    doub N N 116 
ASP CG    OD2    sing N N 117 
ASP OD2   HD2    sing N N 118 
ASP OXT   HXT    sing N N 119 
CYS N     CA     sing N N 120 
CYS N     H      sing N N 121 
CYS N     H2     sing N N 122 
CYS CA    C      sing N N 123 
CYS CA    CB     sing N N 124 
CYS CA    HA     sing N N 125 
CYS C     O      doub N N 126 
CYS C     OXT    sing N N 127 
CYS CB    SG     sing N N 128 
CYS CB    HB2    sing N N 129 
CYS CB    HB3    sing N N 130 
CYS SG    HG     sing N N 131 
CYS OXT   HXT    sing N N 132 
GLN N     CA     sing N N 133 
GLN N     H      sing N N 134 
GLN N     H2     sing N N 135 
GLN CA    C      sing N N 136 
GLN CA    CB     sing N N 137 
GLN CA    HA     sing N N 138 
GLN C     O      doub N N 139 
GLN C     OXT    sing N N 140 
GLN CB    CG     sing N N 141 
GLN CB    HB2    sing N N 142 
GLN CB    HB3    sing N N 143 
GLN CG    CD     sing N N 144 
GLN CG    HG2    sing N N 145 
GLN CG    HG3    sing N N 146 
GLN CD    OE1    doub N N 147 
GLN CD    NE2    sing N N 148 
GLN NE2   HE21   sing N N 149 
GLN NE2   HE22   sing N N 150 
GLN OXT   HXT    sing N N 151 
GLU N     CA     sing N N 152 
GLU N     H      sing N N 153 
GLU N     H2     sing N N 154 
GLU CA    C      sing N N 155 
GLU CA    CB     sing N N 156 
GLU CA    HA     sing N N 157 
GLU C     O      doub N N 158 
GLU C     OXT    sing N N 159 
GLU CB    CG     sing N N 160 
GLU CB    HB2    sing N N 161 
GLU CB    HB3    sing N N 162 
GLU CG    CD     sing N N 163 
GLU CG    HG2    sing N N 164 
GLU CG    HG3    sing N N 165 
GLU CD    OE1    doub N N 166 
GLU CD    OE2    sing N N 167 
GLU OE2   HE2    sing N N 168 
GLU OXT   HXT    sing N N 169 
GLY N     CA     sing N N 170 
GLY N     H      sing N N 171 
GLY N     H2     sing N N 172 
GLY CA    C      sing N N 173 
GLY CA    HA2    sing N N 174 
GLY CA    HA3    sing N N 175 
GLY C     O      doub N N 176 
GLY C     OXT    sing N N 177 
GLY OXT   HXT    sing N N 178 
HIS N     CA     sing N N 179 
HIS N     H      sing N N 180 
HIS N     H2     sing N N 181 
HIS CA    C      sing N N 182 
HIS CA    CB     sing N N 183 
HIS CA    HA     sing N N 184 
HIS C     O      doub N N 185 
HIS C     OXT    sing N N 186 
HIS CB    CG     sing N N 187 
HIS CB    HB2    sing N N 188 
HIS CB    HB3    sing N N 189 
HIS CG    ND1    sing Y N 190 
HIS CG    CD2    doub Y N 191 
HIS ND1   CE1    doub Y N 192 
HIS ND1   HD1    sing N N 193 
HIS CD2   NE2    sing Y N 194 
HIS CD2   HD2    sing N N 195 
HIS CE1   NE2    sing Y N 196 
HIS CE1   HE1    sing N N 197 
HIS NE2   HE2    sing N N 198 
HIS OXT   HXT    sing N N 199 
HOH O     H1     sing N N 200 
HOH O     H2     sing N N 201 
ILE N     CA     sing N N 202 
ILE N     H      sing N N 203 
ILE N     H2     sing N N 204 
ILE CA    C      sing N N 205 
ILE CA    CB     sing N N 206 
ILE CA    HA     sing N N 207 
ILE C     O      doub N N 208 
ILE C     OXT    sing N N 209 
ILE CB    CG1    sing N N 210 
ILE CB    CG2    sing N N 211 
ILE CB    HB     sing N N 212 
ILE CG1   CD1    sing N N 213 
ILE CG1   HG12   sing N N 214 
ILE CG1   HG13   sing N N 215 
ILE CG2   HG21   sing N N 216 
ILE CG2   HG22   sing N N 217 
ILE CG2   HG23   sing N N 218 
ILE CD1   HD11   sing N N 219 
ILE CD1   HD12   sing N N 220 
ILE CD1   HD13   sing N N 221 
ILE OXT   HXT    sing N N 222 
LEU N     CA     sing N N 223 
LEU N     H      sing N N 224 
LEU N     H2     sing N N 225 
LEU CA    C      sing N N 226 
LEU CA    CB     sing N N 227 
LEU CA    HA     sing N N 228 
LEU C     O      doub N N 229 
LEU C     OXT    sing N N 230 
LEU CB    CG     sing N N 231 
LEU CB    HB2    sing N N 232 
LEU CB    HB3    sing N N 233 
LEU CG    CD1    sing N N 234 
LEU CG    CD2    sing N N 235 
LEU CG    HG     sing N N 236 
LEU CD1   HD11   sing N N 237 
LEU CD1   HD12   sing N N 238 
LEU CD1   HD13   sing N N 239 
LEU CD2   HD21   sing N N 240 
LEU CD2   HD22   sing N N 241 
LEU CD2   HD23   sing N N 242 
LEU OXT   HXT    sing N N 243 
LYS N     CA     sing N N 244 
LYS N     H      sing N N 245 
LYS N     H2     sing N N 246 
LYS CA    C      sing N N 247 
LYS CA    CB     sing N N 248 
LYS CA    HA     sing N N 249 
LYS C     O      doub N N 250 
LYS C     OXT    sing N N 251 
LYS CB    CG     sing N N 252 
LYS CB    HB2    sing N N 253 
LYS CB    HB3    sing N N 254 
LYS CG    CD     sing N N 255 
LYS CG    HG2    sing N N 256 
LYS CG    HG3    sing N N 257 
LYS CD    CE     sing N N 258 
LYS CD    HD2    sing N N 259 
LYS CD    HD3    sing N N 260 
LYS CE    NZ     sing N N 261 
LYS CE    HE2    sing N N 262 
LYS CE    HE3    sing N N 263 
LYS NZ    HZ1    sing N N 264 
LYS NZ    HZ2    sing N N 265 
LYS NZ    HZ3    sing N N 266 
LYS OXT   HXT    sing N N 267 
MET N     CA     sing N N 268 
MET N     H      sing N N 269 
MET N     H2     sing N N 270 
MET CA    C      sing N N 271 
MET CA    CB     sing N N 272 
MET CA    HA     sing N N 273 
MET C     O      doub N N 274 
MET C     OXT    sing N N 275 
MET CB    CG     sing N N 276 
MET CB    HB2    sing N N 277 
MET CB    HB3    sing N N 278 
MET CG    SD     sing N N 279 
MET CG    HG2    sing N N 280 
MET CG    HG3    sing N N 281 
MET SD    CE     sing N N 282 
MET CE    HE1    sing N N 283 
MET CE    HE2    sing N N 284 
MET CE    HE3    sing N N 285 
MET OXT   HXT    sing N N 286 
PHE N     CA     sing N N 287 
PHE N     H      sing N N 288 
PHE N     H2     sing N N 289 
PHE CA    C      sing N N 290 
PHE CA    CB     sing N N 291 
PHE CA    HA     sing N N 292 
PHE C     O      doub N N 293 
PHE C     OXT    sing N N 294 
PHE CB    CG     sing N N 295 
PHE CB    HB2    sing N N 296 
PHE CB    HB3    sing N N 297 
PHE CG    CD1    doub Y N 298 
PHE CG    CD2    sing Y N 299 
PHE CD1   CE1    sing Y N 300 
PHE CD1   HD1    sing N N 301 
PHE CD2   CE2    doub Y N 302 
PHE CD2   HD2    sing N N 303 
PHE CE1   CZ     doub Y N 304 
PHE CE1   HE1    sing N N 305 
PHE CE2   CZ     sing Y N 306 
PHE CE2   HE2    sing N N 307 
PHE CZ    HZ     sing N N 308 
PHE OXT   HXT    sing N N 309 
PRO N     CA     sing N N 310 
PRO N     CD     sing N N 311 
PRO N     H      sing N N 312 
PRO CA    C      sing N N 313 
PRO CA    CB     sing N N 314 
PRO CA    HA     sing N N 315 
PRO C     O      doub N N 316 
PRO C     OXT    sing N N 317 
PRO CB    CG     sing N N 318 
PRO CB    HB2    sing N N 319 
PRO CB    HB3    sing N N 320 
PRO CG    CD     sing N N 321 
PRO CG    HG2    sing N N 322 
PRO CG    HG3    sing N N 323 
PRO CD    HD2    sing N N 324 
PRO CD    HD3    sing N N 325 
PRO OXT   HXT    sing N N 326 
SER N     CA     sing N N 327 
SER N     H      sing N N 328 
SER N     H2     sing N N 329 
SER CA    C      sing N N 330 
SER CA    CB     sing N N 331 
SER CA    HA     sing N N 332 
SER C     O      doub N N 333 
SER C     OXT    sing N N 334 
SER CB    OG     sing N N 335 
SER CB    HB2    sing N N 336 
SER CB    HB3    sing N N 337 
SER OG    HG     sing N N 338 
SER OXT   HXT    sing N N 339 
THR N     CA     sing N N 340 
THR N     H      sing N N 341 
THR N     H2     sing N N 342 
THR CA    C      sing N N 343 
THR CA    CB     sing N N 344 
THR CA    HA     sing N N 345 
THR C     O      doub N N 346 
THR C     OXT    sing N N 347 
THR CB    OG1    sing N N 348 
THR CB    CG2    sing N N 349 
THR CB    HB     sing N N 350 
THR OG1   HG1    sing N N 351 
THR CG2   HG21   sing N N 352 
THR CG2   HG22   sing N N 353 
THR CG2   HG23   sing N N 354 
THR OXT   HXT    sing N N 355 
TRP N     CA     sing N N 356 
TRP N     H      sing N N 357 
TRP N     H2     sing N N 358 
TRP CA    C      sing N N 359 
TRP CA    CB     sing N N 360 
TRP CA    HA     sing N N 361 
TRP C     O      doub N N 362 
TRP C     OXT    sing N N 363 
TRP CB    CG     sing N N 364 
TRP CB    HB2    sing N N 365 
TRP CB    HB3    sing N N 366 
TRP CG    CD1    doub Y N 367 
TRP CG    CD2    sing Y N 368 
TRP CD1   NE1    sing Y N 369 
TRP CD1   HD1    sing N N 370 
TRP CD2   CE2    doub Y N 371 
TRP CD2   CE3    sing Y N 372 
TRP NE1   CE2    sing Y N 373 
TRP NE1   HE1    sing N N 374 
TRP CE2   CZ2    sing Y N 375 
TRP CE3   CZ3    doub Y N 376 
TRP CE3   HE3    sing N N 377 
TRP CZ2   CH2    doub Y N 378 
TRP CZ2   HZ2    sing N N 379 
TRP CZ3   CH2    sing Y N 380 
TRP CZ3   HZ3    sing N N 381 
TRP CH2   HH2    sing N N 382 
TRP OXT   HXT    sing N N 383 
TYR N     CA     sing N N 384 
TYR N     H      sing N N 385 
TYR N     H2     sing N N 386 
TYR CA    C      sing N N 387 
TYR CA    CB     sing N N 388 
TYR CA    HA     sing N N 389 
TYR C     O      doub N N 390 
TYR C     OXT    sing N N 391 
TYR CB    CG     sing N N 392 
TYR CB    HB2    sing N N 393 
TYR CB    HB3    sing N N 394 
TYR CG    CD1    doub Y N 395 
TYR CG    CD2    sing Y N 396 
TYR CD1   CE1    sing Y N 397 
TYR CD1   HD1    sing N N 398 
TYR CD2   CE2    doub Y N 399 
TYR CD2   HD2    sing N N 400 
TYR CE1   CZ     doub Y N 401 
TYR CE1   HE1    sing N N 402 
TYR CE2   CZ     sing Y N 403 
TYR CE2   HE2    sing N N 404 
TYR CZ    OH     sing N N 405 
TYR OH    HH     sing N N 406 
TYR OXT   HXT    sing N N 407 
VAL N     CA     sing N N 408 
VAL N     H      sing N N 409 
VAL N     H2     sing N N 410 
VAL CA    C      sing N N 411 
VAL CA    CB     sing N N 412 
VAL CA    HA     sing N N 413 
VAL C     O      doub N N 414 
VAL C     OXT    sing N N 415 
VAL CB    CG1    sing N N 416 
VAL CB    CG2    sing N N 417 
VAL CB    HB     sing N N 418 
VAL CG1   HG11   sing N N 419 
VAL CG1   HG12   sing N N 420 
VAL CG1   HG13   sing N N 421 
VAL CG2   HG21   sing N N 422 
VAL CG2   HG22   sing N N 423 
VAL CG2   HG23   sing N N 424 
VAL OXT   HXT    sing N N 425 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'Agence Nationale de la Recherche (ANR)' France ScaffoldDisorder                1 
'La ligue contre le cancer'              France 'Thibault Orand thesis funding' 2 
# 
loop_
_pdbx_initial_refinement_model.id 
_pdbx_initial_refinement_model.entity_id_list 
_pdbx_initial_refinement_model.type 
_pdbx_initial_refinement_model.source_name 
_pdbx_initial_refinement_model.accession_code 
_pdbx_initial_refinement_model.details 
1 ? 'experimental model' PDB 4UX9 ? 
2 ? 'experimental model' PDB 1UKH ? 
# 
_space_group.name_H-M_alt     'P 31 2 1' 
_space_group.name_Hall        
;P 31 2"
;
_space_group.IT_number        152 
_space_group.crystal_system   trigonal 
_space_group.id               1 
# 
_atom_sites.entry_id                    9FT9 
_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]   0.007262 
_atom_sites.fract_transf_matrix[1][2]   0.004193 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.008386 
_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]   0.015637 
_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 ? ? 4.49882 3.47563 ? ? 15.80542 1.70748  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
P ? ? 9.51135 5.44231 ? ? 1.42069  35.72801 ? ? 0.0 
;2-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     . ASP A 1 3   ? -51.06141 86.79520 -9.46202  1.000 141.57296 ? 7   ASP A N     1 
ATOM   2    C CA    . ASP A 1 3   ? -51.91879 85.94446 -10.27903 1.000 145.44409 ? 7   ASP A CA    1 
ATOM   3    C C     . ASP A 1 3   ? -51.60867 84.47607 -10.01822 1.000 150.37841 ? 7   ASP A C     1 
ATOM   4    O O     . ASP A 1 3   ? -52.51628 83.63826 -9.94984  1.000 146.50882 ? 7   ASP A O     1 
ATOM   5    C CB    . ASP A 1 3   ? -51.74585 86.26838 -11.76512 1.000 145.34006 ? 7   ASP A CB    1 
ATOM   6    N N     . ASN A 1 4   ? -50.32125 84.17001 -9.85818  1.000 160.02623 ? 8   ASN A N     1 
ATOM   7    C CA    . ASN A 1 4   ? -49.86533 82.79312 -9.69578  1.000 156.24762 ? 8   ASN A CA    1 
ATOM   8    C C     . ASN A 1 4   ? -49.83015 82.41655 -8.21843  1.000 144.62555 ? 8   ASN A C     1 
ATOM   9    O O     . ASN A 1 4   ? -49.07159 82.99924 -7.43343  1.000 138.75971 ? 8   ASN A O     1 
ATOM   10   C CB    . ASN A 1 4   ? -48.49222 82.59400 -10.33592 1.000 154.61532 ? 8   ASN A CB    1 
ATOM   11   C CG    . ASN A 1 4   ? -48.35480 81.23180 -11.00037 1.000 158.36782 ? 8   ASN A CG    1 
ATOM   12   O OD1   . ASN A 1 4   ? -49.21534 80.81695 -11.78540 1.000 159.20660 ? 8   ASN A OD1   1 
ATOM   13   N ND2   . ASN A 1 4   ? -47.26473 80.53049 -10.69163 1.000 150.03878 ? 8   ASN A ND2   1 
ATOM   14   N N     . ASN A 1 5   ? -50.62813 81.41958 -7.85677  1.000 123.88073 ? 9   ASN A N     1 
ATOM   15   C CA    . ASN A 1 5   ? -50.79197 80.98307 -6.47862  1.000 117.57166 ? 9   ASN A CA    1 
ATOM   16   C C     . ASN A 1 5   ? -49.79668 79.90820 -6.07463  1.000 103.08494 ? 9   ASN A C     1 
ATOM   17   O O     . ASN A 1 5   ? -49.85525 79.41702 -4.93795  1.000 90.88548  ? 9   ASN A O     1 
ATOM   18   C CB    . ASN A 1 5   ? -52.21299 80.46631 -6.28269  1.000 108.28083 ? 9   ASN A CB    1 
ATOM   19   C CG    . ASN A 1 5   ? -53.21369 81.26314 -7.07711  1.000 120.57495 ? 9   ASN A CG    1 
ATOM   20   O OD1   . ASN A 1 5   ? -53.15509 81.29968 -8.31281  1.000 123.73915 ? 9   ASN A OD1   1 
ATOM   21   N ND2   . ASN A 1 5   ? -54.12630 81.93249 -6.37831  1.000 117.59686 ? 9   ASN A ND2   1 
ATOM   22   N N     . PHE A 1 6   ? -48.90064 79.52169 -6.97205  1.000 100.57063 ? 10  PHE A N     1 
ATOM   23   C CA    . PHE A 1 6   ? -47.94922 78.46326 -6.68983  1.000 98.74158  ? 10  PHE A CA    1 
ATOM   24   C C     . PHE A 1 6   ? -46.53251 78.99283 -6.77337  1.000 101.01327 ? 10  PHE A C     1 
ATOM   25   O O     . PHE A 1 6   ? -46.16996 79.71696 -7.70926  1.000 108.47170 ? 10  PHE A O     1 
ATOM   26   C CB    . PHE A 1 6   ? -48.08988 77.29452 -7.65803  1.000 96.13874  ? 10  PHE A CB    1 
ATOM   27   C CG    . PHE A 1 6   ? -49.41907 76.62290 -7.59680  1.000 92.97193  ? 10  PHE A CG    1 
ATOM   28   C CD1   . PHE A 1 6   ? -49.64163 75.59732 -6.69816  1.000 92.96802  ? 10  PHE A CD1   1 
ATOM   29   C CD2   . PHE A 1 6   ? -50.45492 77.03697 -8.41803  1.000 88.25226  ? 10  PHE A CD2   1 
ATOM   30   C CE1   . PHE A 1 6   ? -50.87359 74.98063 -6.63198  1.000 84.85296  ? 10  PHE A CE1   1 
ATOM   31   C CE2   . PHE A 1 6   ? -51.67003 76.43946 -8.35418  1.000 92.70629  ? 10  PHE A CE2   1 
ATOM   32   C CZ    . PHE A 1 6   ? -51.88791 75.40274 -7.45685  1.000 89.89025  ? 10  PHE A CZ    1 
ATOM   33   N N     . TYR A 1 7   ? -45.73733 78.59835 -5.79660  1.000 96.74027  ? 11  TYR A N     1 
ATOM   34   C CA    . TYR A 1 7   ? -44.29908 78.75387 -5.85254  1.000 96.57211  ? 11  TYR A CA    1 
ATOM   35   C C     . TYR A 1 7   ? -43.67640 77.36073 -5.85141  1.000 93.71939  ? 11  TYR A C     1 
ATOM   36   O O     . TYR A 1 7   ? -44.29959 76.37792 -5.43135  1.000 92.74368  ? 11  TYR A O     1 
ATOM   37   C CB    . TYR A 1 7   ? -43.80759 79.62736 -4.69130  1.000 90.87070  ? 11  TYR A CB    1 
ATOM   38   C CG    . TYR A 1 7   ? -43.73155 78.91030 -3.36936  1.000 90.72881  ? 11  TYR A CG    1 
ATOM   39   C CD1   . TYR A 1 7   ? -44.88060 78.52367 -2.69975  1.000 88.64907  ? 11  TYR A CD1   1 
ATOM   40   C CD2   . TYR A 1 7   ? -42.51425 78.64913 -2.77451  1.000 88.65184  ? 11  TYR A CD2   1 
ATOM   41   C CE1   . TYR A 1 7   ? -44.81271 77.87636 -1.47603  1.000 87.64956  ? 11  TYR A CE1   1 
ATOM   42   C CE2   . TYR A 1 7   ? -42.44057 78.01493 -1.55729  1.000 93.14304  ? 11  TYR A CE2   1 
ATOM   43   C CZ    . TYR A 1 7   ? -43.58098 77.62141 -0.91374  1.000 84.76544  ? 11  TYR A CZ    1 
ATOM   44   O OH    . TYR A 1 7   ? -43.47866 76.97901 0.30300   1.000 89.10205  ? 11  TYR A OH    1 
ATOM   45   N N     . SER A 1 8   ? -42.45907 77.27998 -6.37871  1.000 90.73845  ? 12  SER A N     1 
ATOM   46   C CA    . SER A 1 8   ? -41.79060 76.01840 -6.67638  1.000 88.61020  ? 12  SER A CA    1 
ATOM   47   C C     . SER A 1 8   ? -40.52341 75.91810 -5.83162  1.000 97.01584  ? 12  SER A C     1 
ATOM   48   O O     . SER A 1 8   ? -39.56095 76.65837 -6.05995  1.000 106.36634 ? 12  SER A O     1 
ATOM   49   C CB    . SER A 1 8   ? -41.45499 75.93436 -8.16491  1.000 92.19065  ? 12  SER A CB    1 
ATOM   50   O OG    . SER A 1 8   ? -42.50846 76.47065 -8.94954  1.000 104.13950 ? 12  SER A OG    1 
ATOM   51   N N     . VAL A 1 9   ? -40.51412 75.00084 -4.87965  1.000 91.65799  ? 13  VAL A N     1 
ATOM   52   C CA    . VAL A 1 9   ? -39.34008 74.72088 -4.06365  1.000 85.56269  ? 13  VAL A CA    1 
ATOM   53   C C     . VAL A 1 9   ? -38.56246 73.58214 -4.70385  1.000 90.07719  ? 13  VAL A C     1 
ATOM   54   O O     . VAL A 1 9   ? -39.13719 72.71007 -5.36083  1.000 99.04387  ? 13  VAL A O     1 
ATOM   55   C CB    . VAL A 1 9   ? -39.75674 74.36090 -2.62159  1.000 91.25592  ? 13  VAL A CB    1 
ATOM   56   C CG1   . VAL A 1 9   ? -38.59950 73.81026 -1.85071  1.000 91.74141  ? 13  VAL A CG1   1 
ATOM   57   C CG2   . VAL A 1 9   ? -40.27535 75.56280 -1.90525  1.000 100.50814 ? 13  VAL A CG2   1 
ATOM   58   N N     . GLU A 1 10  ? -37.24535 73.58219 -4.51543  1.000 92.43425  ? 14  GLU A N     1 
ATOM   59   C CA    . GLU A 1 10  ? -36.39254 72.47421 -4.91840  1.000 87.86769  ? 14  GLU A CA    1 
ATOM   60   C C     . GLU A 1 10  ? -36.04597 71.64302 -3.69174  1.000 82.38898  ? 14  GLU A C     1 
ATOM   61   O O     . GLU A 1 10  ? -35.67972 72.20007 -2.65577  1.000 88.05670  ? 14  GLU A O     1 
ATOM   62   C CB    . GLU A 1 10  ? -35.12338 72.99172 -5.58769  1.000 88.94263  ? 14  GLU A CB    1 
ATOM   63   C CG    . GLU A 1 10  ? -35.39468 73.59570 -6.94571  1.000 94.15393  ? 14  GLU A CG    1 
ATOM   64   C CD    . GLU A 1 10  ? -35.64267 72.52916 -7.99917  1.000 105.69106 ? 14  GLU A CD    1 
ATOM   65   O OE1   . GLU A 1 10  ? -35.15350 71.38464 -7.82104  1.000 108.94516 ? 14  GLU A OE1   1 
ATOM   66   O OE2   . GLU A 1 10  ? -36.32365 72.83777 -9.00406  1.000 109.42307 ? 14  GLU A OE2   1 
ATOM   67   N N     . ILE A 1 11  ? -36.22826 70.32085 -3.78364  1.000 95.94159  ? 15  ILE A N     1 
ATOM   68   C CA    . ILE A 1 11  ? -35.87447 69.38523 -2.70597  1.000 88.23222  ? 15  ILE A CA    1 
ATOM   69   C C     . ILE A 1 11  ? -35.01933 68.28864 -3.33747  1.000 89.38326  ? 15  ILE A C     1 
ATOM   70   O O     . ILE A 1 11  ? -35.53064 67.23710 -3.73220  1.000 97.61328  ? 15  ILE A O     1 
ATOM   71   C CB    . ILE A 1 11  ? -37.10541 68.78976 -2.00647  1.000 85.07463  ? 15  ILE A CB    1 
ATOM   72   C CG1   . ILE A 1 11  ? -38.16167 69.85726 -1.76621  1.000 85.07800  ? 15  ILE A CG1   1 
ATOM   73   C CG2   . ILE A 1 11  ? -36.72872 68.16958 -0.65408  1.000 79.92753  ? 15  ILE A CG2   1 
ATOM   74   C CD1   . ILE A 1 11  ? -37.80334 70.76407 -0.61337  1.000 78.08825  ? 15  ILE A CD1   1 
ATOM   75   N N     . GLY A 1 12  ? -33.70849 68.49834 -3.38190  1.000 91.97326  ? 16  GLY A N     1 
ATOM   76   C CA    . GLY A 1 12  ? -32.86731 67.54890 -4.09301  1.000 90.72308  ? 16  GLY A CA    1 
ATOM   77   C C     . GLY A 1 12  ? -33.29021 67.46491 -5.54831  1.000 100.90150 ? 16  GLY A C     1 
ATOM   78   O O     . GLY A 1 12  ? -33.41456 68.48514 -6.23805  1.000 95.14136  ? 16  GLY A O     1 
ATOM   79   N N     . ASP A 1 13  ? -33.53218 66.23187 -6.01720  1.000 110.21594 ? 17  ASP A N     1 
ATOM   80   C CA    . ASP A 1 13  ? -33.92771 66.00444 -7.40964  1.000 121.60055 ? 17  ASP A CA    1 
ATOM   81   C C     . ASP A 1 13  ? -35.24985 66.67740 -7.73701  1.000 116.29560 ? 17  ASP A C     1 
ATOM   82   O O     . ASP A 1 13  ? -35.35551 67.44266 -8.70438  1.000 120.08101 ? 17  ASP A O     1 
ATOM   83   C CB    . ASP A 1 13  ? -34.05695 64.50377 -7.68889  1.000 131.78865 ? 17  ASP A CB    1 
ATOM   84   C CG    . ASP A 1 13  ? -32.72817 63.78174 -7.67858  1.000 139.71927 ? 17  ASP A CG    1 
ATOM   85   O OD1   . ASP A 1 13  ? -32.49417 62.95103 -8.59112  1.000 136.07256 ? 17  ASP A OD1   1 
ATOM   86   O OD2   . ASP A 1 13  ? -31.91285 64.06173 -6.77801  1.000 145.52243 ? 17  ASP A OD2   1 
ATOM   87   N N     . SER A 1 14  ? -36.27297 66.39047 -6.94464  1.000 109.93835 ? 18  SER A N     1 
ATOM   88   C CA    . SER A 1 14  ? -37.63429 66.71411 -7.32406  1.000 109.74598 ? 18  SER A CA    1 
ATOM   89   C C     . SER A 1 14  ? -37.96422 68.16295 -6.98600  1.000 103.04427 ? 18  SER A C     1 
ATOM   90   O O     . SER A 1 14  ? -37.41858 68.75299 -6.04496  1.000 95.94262  ? 18  SER A O     1 
ATOM   91   C CB    . SER A 1 14  ? -38.60505 65.75451 -6.63361  1.000 109.80178 ? 18  SER A CB    1 
ATOM   92   O OG    . SER A 1 14  ? -38.67120 66.02110 -5.24858  1.000 118.02329 ? 18  SER A OG    1 
ATOM   93   N N     . THR A 1 15  ? -38.85534 68.73820 -7.78711  1.000 101.30569 ? 19  THR A N     1 
ATOM   94   C CA    . THR A 1 15  ? -39.33952 70.09692 -7.59459  1.000 91.88444  ? 19  THR A CA    1 
ATOM   95   C C     . THR A 1 15  ? -40.77446 70.03776 -7.09304  1.000 89.29396  ? 19  THR A C     1 
ATOM   96   O O     . THR A 1 15  ? -41.64255 69.46831 -7.76393  1.000 91.16635  ? 19  THR A O     1 
ATOM   97   C CB    . THR A 1 15  ? -39.27437 70.89133 -8.89693  1.000 93.35317  ? 19  THR A CB    1 
ATOM   98   O OG1   . THR A 1 15  ? -38.07356 70.56222 -9.61491  1.000 96.23419  ? 19  THR A OG1   1 
ATOM   99   C CG2   . THR A 1 15  ? -39.33599 72.38251 -8.60376  1.000 93.78970  ? 19  THR A CG2   1 
ATOM   100  N N     . PHE A 1 16  ? -41.02362 70.61679 -5.92183  1.000 85.55620  ? 20  PHE A N     1 
ATOM   101  C CA    . PHE A 1 16  ? -42.38182 70.74982 -5.40615  1.000 84.12073  ? 20  PHE A CA    1 
ATOM   102  C C     . PHE A 1 16  ? -42.95269 72.08988 -5.84456  1.000 87.74964  ? 20  PHE A C     1 
ATOM   103  O O     . PHE A 1 16  ? -42.37612 73.14735 -5.55064  1.000 93.67989  ? 20  PHE A O     1 
ATOM   104  C CB    . PHE A 1 16  ? -42.41519 70.65233 -3.88381  1.000 85.64626  ? 20  PHE A CB    1 
ATOM   105  C CG    . PHE A 1 16  ? -42.35068 69.25420 -3.36698  1.000 81.72382  ? 20  PHE A CG    1 
ATOM   106  C CD1   . PHE A 1 16  ? -41.29039 68.42624 -3.69549  1.000 83.15710  ? 20  PHE A CD1   1 
ATOM   107  C CD2   . PHE A 1 16  ? -43.35033 68.76551 -2.55227  1.000 73.81348  ? 20  PHE A CD2   1 
ATOM   108  C CE1   . PHE A 1 16  ? -41.22827 67.13294 -3.21421  1.000 85.40638  ? 20  PHE A CE1   1 
ATOM   109  C CE2   . PHE A 1 16  ? -43.29782 67.47206 -2.07277  1.000 79.01112  ? 20  PHE A CE2   1 
ATOM   110  C CZ    . PHE A 1 16  ? -42.23510 66.65203 -2.40469  1.000 80.65268  ? 20  PHE A CZ    1 
ATOM   111  N N     . THR A 1 17  ? -44.05975 72.05163 -6.56100  1.000 81.33245  ? 21  THR A N     1 
ATOM   112  C CA    . THR A 1 17  ? -44.80271 73.26376 -6.86386  1.000 88.73414  ? 21  THR A CA    1 
ATOM   113  C C     . THR A 1 17  ? -46.06616 73.19694 -6.03387  1.000 82.13590  ? 21  THR A C     1 
ATOM   114  O O     . THR A 1 17  ? -46.91674 72.33620 -6.26514  1.000 84.07704  ? 21  THR A O     1 
ATOM   115  C CB    . THR A 1 17  ? -45.11409 73.38540 -8.34925  1.000 89.82756  ? 21  THR A CB    1 
ATOM   116  O OG1   . THR A 1 17  ? -43.88853 73.33870 -9.08800  1.000 91.66859  ? 21  THR A OG1   1 
ATOM   117  C CG2   . THR A 1 17  ? -45.80574 74.71001 -8.61664  1.000 89.26351  ? 21  THR A CG2   1 
ATOM   118  N N     . VAL A 1 18  ? -46.16993 74.08372 -5.05005  1.000 82.25475  ? 22  VAL A N     1 
ATOM   119  C CA    . VAL A 1 18  ? -47.20813 73.99160 -4.03754  1.000 81.10039  ? 22  VAL A CA    1 
ATOM   120  C C     . VAL A 1 18  ? -47.83123 75.35920 -3.82241  1.000 85.31458  ? 22  VAL A C     1 
ATOM   121  O O     . VAL A 1 18  ? -47.24373 76.39606 -4.14966  1.000 90.81694  ? 22  VAL A O     1 
ATOM   122  C CB    . VAL A 1 18  ? -46.64190 73.44513 -2.71517  1.000 78.19237  ? 22  VAL A CB    1 
ATOM   123  C CG1   . VAL A 1 18  ? -46.00067 72.09444 -2.95418  1.000 76.16203  ? 22  VAL A CG1   1 
ATOM   124  C CG2   . VAL A 1 18  ? -45.61325 74.41182 -2.13220  1.000 78.40212  ? 22  VAL A CG2   1 
ATOM   125  N N     . LEU A 1 19  ? -49.03521 75.34532 -3.24921  1.000 80.01432  ? 23  LEU A N     1 
ATOM   126  C CA    . LEU A 1 19  ? -49.72523 76.58967 -2.93451  1.000 81.33968  ? 23  LEU A CA    1 
ATOM   127  C C     . LEU A 1 19  ? -48.90489 77.41356 -1.95665  1.000 80.40952  ? 23  LEU A C     1 
ATOM   128  O O     . LEU A 1 19  ? -48.12297 76.88151 -1.16062  1.000 79.20264  ? 23  LEU A O     1 
ATOM   129  C CB    . LEU A 1 19  ? -51.11379 76.32601 -2.33800  1.000 73.80920  ? 23  LEU A CB    1 
ATOM   130  C CG    . LEU A 1 19  ? -52.19811 75.69658 -3.20987  1.000 77.87659  ? 23  LEU A CG    1 
ATOM   131  C CD1   . LEU A 1 19  ? -53.40586 75.32819 -2.37539  1.000 73.62037  ? 23  LEU A CD1   1 
ATOM   132  C CD2   . LEU A 1 19  ? -52.59145 76.68457 -4.26912  1.000 83.50729  ? 23  LEU A CD2   1 
ATOM   133  N N     . LYS A 1 20  ? -49.10044 78.73424 -2.02680  1.000 82.61617  ? 24  LYS A N     1 
ATOM   134  C CA    . LYS A 1 20  ? -48.34178 79.64305 -1.17751  1.000 81.14207  ? 24  LYS A CA    1 
ATOM   135  C C     . LYS A 1 20  ? -48.57448 79.36379 0.31317   1.000 78.93830  ? 24  LYS A C     1 
ATOM   136  O O     . LYS A 1 20  ? -47.68986 79.63481 1.13546   1.000 83.78460  ? 24  LYS A O     1 
ATOM   137  C CB    . LYS A 1 20  ? -48.70456 81.09129 -1.53148  1.000 86.41361  ? 24  LYS A CB    1 
ATOM   138  C CG    . LYS A 1 20  ? -48.26763 81.59823 -2.93423  1.000 87.72578  ? 24  LYS A CG    1 
ATOM   139  C CD    . LYS A 1 20  ? -46.80993 82.06165 -2.98423  1.000 94.69098  ? 24  LYS A CD    1 
ATOM   140  C CE    . LYS A 1 20  ? -46.62553 83.22662 -3.97016  1.000 96.11450  ? 24  LYS A CE    1 
ATOM   141  N NZ    . LYS A 1 20  ? -47.36674 83.02526 -5.25347  1.000 98.68296  ? 24  LYS A NZ    1 
ATOM   142  N N     . ARG A 1 21  ? -49.73709 78.80082 0.68010   1.000 78.26740  ? 25  ARG A N     1 
ATOM   143  C CA    . ARG A 1 21  ? -50.07704 78.61033 2.09086   1.000 75.09355  ? 25  ARG A CA    1 
ATOM   144  C C     . ARG A 1 21  ? -49.11221 77.66549 2.79952   1.000 81.30186  ? 25  ARG A C     1 
ATOM   145  O O     . ARG A 1 21  ? -49.01420 77.70543 4.03605   1.000 80.76605  ? 25  ARG A O     1 
ATOM   146  C CB    . ARG A 1 21  ? -51.50509 78.06961 2.22909   1.000 70.76162  ? 25  ARG A CB    1 
ATOM   147  C CG    . ARG A 1 21  ? -51.69286 76.65760 1.67781   1.000 74.36525  ? 25  ARG A CG    1 
ATOM   148  C CD    . ARG A 1 21  ? -53.16008 76.18186 1.67785   1.000 71.49620  ? 25  ARG A CD    1 
ATOM   149  N NE    . ARG A 1 21  ? -53.67615 75.86577 3.00880   1.000 75.18050  ? 25  ARG A NE    1 
ATOM   150  C CZ    . ARG A 1 21  ? -54.94083 75.54317 3.27050   1.000 83.29538  ? 25  ARG A CZ    1 
ATOM   151  N NH1   . ARG A 1 21  ? -55.85722 75.47902 2.30729   1.000 77.32821  ? 25  ARG A NH1   1 
ATOM   152  N NH2   . ARG A 1 21  ? -55.29475 75.27080 4.52877   1.000 83.60067  ? 25  ARG A NH2   1 
ATOM   153  N N     . TYR A 1 22  ? -48.39900 76.82206 2.04490   1.000 75.88132  ? 26  TYR A N     1 
ATOM   154  C CA    . TYR A 1 22  ? -47.50379 75.81327 2.59960   1.000 77.80758  ? 26  TYR A CA    1 
ATOM   155  C C     . TYR A 1 22  ? -46.07522 76.33475 2.50565   1.000 82.61879  ? 26  TYR A C     1 
ATOM   156  O O     . TYR A 1 22  ? -45.51446 76.44383 1.40962   1.000 82.58774  ? 26  TYR A O     1 
ATOM   157  C CB    . TYR A 1 22  ? -47.67961 74.48727 1.85728   1.000 79.78378  ? 26  TYR A CB    1 
ATOM   158  C CG    . TYR A 1 22  ? -49.09827 73.93238 1.92951   1.000 68.70877  ? 26  TYR A CG    1 
ATOM   159  C CD1   . TYR A 1 22  ? -49.66052 73.56284 3.15230   1.000 74.80251  ? 26  TYR A CD1   1 
ATOM   160  C CD2   . TYR A 1 22  ? -49.87601 73.78174 0.78624   1.000 63.97578  ? 26  TYR A CD2   1 
ATOM   161  C CE1   . TYR A 1 22  ? -50.96451 73.04629 3.23756   1.000 69.10088  ? 26  TYR A CE1   1 
ATOM   162  C CE2   . TYR A 1 22  ? -51.19449 73.26487 0.86122   1.000 72.05198  ? 26  TYR A CE2   1 
ATOM   163  C CZ    . TYR A 1 22  ? -51.72632 72.90448 2.09089   1.000 70.97857  ? 26  TYR A CZ    1 
ATOM   164  O OH    . TYR A 1 22  ? -53.01918 72.40604 2.18418   1.000 70.33559  ? 26  TYR A OH    1 
ATOM   165  N N     . GLN A 1 23  ? -45.49238 76.64561 3.65947   1.000 82.84757  ? 27  GLN A N     1 
ATOM   166  C CA    . GLN A 1 23  ? -44.22561 77.34928 3.75987   1.000 80.48515  ? 27  GLN A CA    1 
ATOM   167  C C     . GLN A 1 23  ? -43.17820 76.45232 4.38914   1.000 79.15903  ? 27  GLN A C     1 
ATOM   168  O O     . GLN A 1 23  ? -43.50034 75.56223 5.17724   1.000 82.88273  ? 27  GLN A O     1 
ATOM   169  C CB    . GLN A 1 23  ? -44.36161 78.61739 4.60912   1.000 79.83205  ? 27  GLN A CB    1 
ATOM   170  C CG    . GLN A 1 23  ? -45.55258 79.47301 4.24636   1.000 86.40781  ? 27  GLN A CG    1 
ATOM   171  C CD    . GLN A 1 23  ? -45.40714 80.13312 2.88400   1.000 94.95520  ? 27  GLN A CD    1 
ATOM   172  O OE1   . GLN A 1 23  ? -44.47500 79.84704 2.11589   1.000 96.39158  ? 27  GLN A OE1   1 
ATOM   173  N NE2   . GLN A 1 23  ? -46.35054 81.01119 2.56497   1.000 97.80981  ? 27  GLN A NE2   1 
ATOM   174  N N     . ASN A 1 24  ? -41.92120 76.69618 4.03073   1.000 76.09573  ? 28  ASN A N     1 
ATOM   175  C CA    . ASN A 1 24  ? -40.77806 76.10142 4.72876   1.000 81.37169  ? 28  ASN A CA    1 
ATOM   176  C C     . ASN A 1 24  ? -40.76419 74.56890 4.60159   1.000 79.97970  ? 28  ASN A C     1 
ATOM   177  O O     . ASN A 1 24  ? -40.57796 73.83851 5.58298   1.000 76.21119  ? 28  ASN A O     1 
ATOM   178  C CB    . ASN A 1 24  ? -40.75751 76.53925 6.20163   1.000 74.70731  ? 28  ASN A CB    1 
ATOM   179  C CG    . ASN A 1 24  ? -41.03901 78.04808 6.38597   1.000 91.60665  ? 28  ASN A CG    1 
ATOM   180  O OD1   . ASN A 1 24  ? -42.12647 78.43355 6.83802   1.000 92.20087  ? 28  ASN A OD1   1 
ATOM   181  N ND2   . ASN A 1 24  ? -40.04797 78.89598 6.07585   1.000 82.97040  ? 28  ASN A ND2   1 
ATOM   182  N N     . LEU A 1 25  ? -40.94850 74.07902 3.37253   1.000 77.52131  ? 29  LEU A N     1 
ATOM   183  C CA    . LEU A 1 25  ? -40.89202 72.63877 3.12917   1.000 79.14340  ? 29  LEU A CA    1 
ATOM   184  C C     . LEU A 1 25  ? -39.52155 72.07422 3.48956   1.000 72.11995  ? 29  LEU A C     1 
ATOM   185  O O     . LEU A 1 25  ? -38.48548 72.70765 3.24601   1.000 78.11844  ? 29  LEU A O     1 
ATOM   186  C CB    . LEU A 1 25  ? -41.19987 72.31674 1.66373   1.000 76.94809  ? 29  LEU A CB    1 
ATOM   187  C CG    . LEU A 1 25  ? -42.67074 72.16864 1.26357   1.000 72.70514  ? 29  LEU A CG    1 
ATOM   188  C CD1   . LEU A 1 25  ? -43.45415 73.49134 1.42994   1.000 73.07000  ? 29  LEU A CD1   1 
ATOM   189  C CD2   . LEU A 1 25  ? -42.75504 71.67124 -0.17562  1.000 72.21496  ? 29  LEU A CD2   1 
ATOM   190  N N     . LYS A 1 26  ? -39.52453 70.87575 4.09384   1.000 65.65358  ? 30  LYS A N     1 
ATOM   191  C CA    . LYS A 1 26  ? -38.30683 70.12646 4.40579   1.000 67.59916  ? 30  LYS A CA    1 
ATOM   192  C C     . LYS A 1 26  ? -38.59889 68.63666 4.30223   1.000 71.80883  ? 30  LYS A C     1 
ATOM   193  O O     . LYS A 1 26  ? -39.72824 68.21975 4.58819   1.000 77.06111  ? 30  LYS A O     1 
ATOM   194  C CB    . LYS A 1 26  ? -37.77203 70.47053 5.80469   1.000 71.72001  ? 30  LYS A CB    1 
ATOM   195  C CG    . LYS A 1 26  ? -38.71293 70.12072 6.95919   1.000 77.42373  ? 30  LYS A CG    1 
ATOM   196  C CD    . LYS A 1 26  ? -38.34915 70.91259 8.24936   1.000 81.65449  ? 30  LYS A CD    1 
ATOM   197  C CE    . LYS A 1 26  ? -39.17850 70.42600 9.46282   1.000 68.23884  ? 30  LYS A CE    1 
ATOM   198  N NZ    . LYS A 1 26  ? -39.38957 71.47533 10.51329  1.000 72.88663  ? 30  LYS A NZ    1 
ATOM   199  N N     . PRO A 1 27  ? -37.62684 67.81514 3.89701   1.000 72.79044  ? 31  PRO A N     1 
ATOM   200  C CA    . PRO A 1 27  ? -37.91254 66.39291 3.65330   1.000 67.16126  ? 31  PRO A CA    1 
ATOM   201  C C     . PRO A 1 27  ? -37.89023 65.56225 4.92732   1.000 73.26312  ? 31  PRO A C     1 
ATOM   202  O O     . PRO A 1 27  ? -37.01861 65.74196 5.78432   1.000 68.74736  ? 31  PRO A O     1 
ATOM   203  C CB    . PRO A 1 27  ? -36.78715 65.96122 2.69935   1.000 67.99811  ? 31  PRO A CB    1 
ATOM   204  C CG    . PRO A 1 27  ? -35.69691 66.96833 2.86136   1.000 71.09413  ? 31  PRO A CG    1 
ATOM   205  C CD    . PRO A 1 27  ? -36.20488 68.13606 3.67216   1.000 77.88769  ? 31  PRO A CD    1 
ATOM   206  N N     . ILE A 1 28  ? -38.83389 64.59950 5.01715   1.000 70.64623  ? 32  ILE A N     1 
ATOM   207  C CA    . ILE A 1 28  ? -38.99651 63.76743 6.21763   1.000 71.98591  ? 32  ILE A CA    1 
ATOM   208  C C     . ILE A 1 28  ? -39.01289 62.25975 5.94363   1.000 70.01706  ? 32  ILE A C     1 
ATOM   209  O O     . ILE A 1 28  ? -38.92010 61.46200 6.88646   1.000 73.90344  ? 32  ILE A O     1 
ATOM   210  C CB    . ILE A 1 28  ? -40.26667 64.16958 6.99758   1.000 68.07552  ? 32  ILE A CB    1 
ATOM   211  C CG1   . ILE A 1 28  ? -41.51448 64.00871 6.13567   1.000 68.73563  ? 32  ILE A CG1   1 
ATOM   212  C CG2   . ILE A 1 28  ? -40.19779 65.61867 7.45587   1.000 70.51679  ? 32  ILE A CG2   1 
ATOM   213  C CD1   . ILE A 1 28  ? -42.79826 64.07492 6.93591   1.000 66.01428  ? 32  ILE A CD1   1 
ATOM   214  N N     . GLY A 1 29  ? -39.13474 61.85122 4.68052   1.000 71.44398  ? 33  GLY A N     1 
ATOM   215  C CA    . GLY A 1 29  ? -39.20461 60.43276 4.35336   1.000 72.13161  ? 33  GLY A CA    1 
ATOM   216  C C     . GLY A 1 29  ? -39.39377 60.22573 2.86163   1.000 74.32702  ? 33  GLY A C     1 
ATOM   217  O O     . GLY A 1 29  ? -39.54191 61.18100 2.09073   1.000 72.65706  ? 33  GLY A O     1 
ATOM   218  N N     . SER A 1 30  ? -39.41270 58.95087 2.45931   1.000 75.31886  ? 34  SER A N     1 
ATOM   219  C CA    . SER A 1 30  ? -39.45751 58.62745 1.03651   1.000 77.41705  ? 34  SER A CA    1 
ATOM   220  C C     . SER A 1 30  ? -39.90256 57.18380 0.81934   1.000 78.83542  ? 34  SER A C     1 
ATOM   221  O O     . SER A 1 30  ? -39.99647 56.38248 1.75253   1.000 76.54961  ? 34  SER A O     1 
ATOM   222  C CB    . SER A 1 30  ? -38.09891 58.84449 0.38230   1.000 77.72326  ? 34  SER A CB    1 
ATOM   223  O OG    . SER A 1 30  ? -37.22682 57.75348 0.68929   1.000 90.43360  ? 34  SER A OG    1 
ATOM   224  N N     . GLY A 1 31  ? -40.15982 56.86831 -0.44277  1.000 80.88158  ? 35  GLY A N     1 
ATOM   225  C CA    . GLY A 1 31  ? -40.55867 55.53650 -0.82653  1.000 81.63911  ? 35  GLY A CA    1 
ATOM   226  C C     . GLY A 1 31  ? -40.63603 55.43571 -2.33226  1.000 91.29289  ? 35  GLY A C     1 
ATOM   227  O O     . GLY A 1 31  ? -40.19215 56.32842 -3.05932  1.000 82.84070  ? 35  GLY A O     1 
ATOM   228  N N     . ALA A 1 32  ? -41.24768 54.33911 -2.78861  1.000 88.38175  ? 36  ALA A N     1 
ATOM   229  C CA    . ALA A 1 32  ? -41.37243 54.08570 -4.22071  1.000 94.57895  ? 36  ALA A CA    1 
ATOM   230  C C     . ALA A 1 32  ? -41.97531 55.27618 -4.95912  1.000 96.33111  ? 36  ALA A C     1 
ATOM   231  O O     . ALA A 1 32  ? -41.56406 55.59202 -6.08350  1.000 101.88691 ? 36  ALA A O     1 
ATOM   232  C CB    . ALA A 1 32  ? -42.22573 52.83740 -4.45792  1.000 86.36008  ? 36  ALA A CB    1 
ATOM   233  N N     . GLN A 1 33  ? -42.94119 55.95427 -4.33955  1.000 88.15315  ? 37  GLN A N     1 
ATOM   234  C CA    . GLN A 1 33  ? -43.67730 57.02845 -4.99113  1.000 95.33386  ? 37  GLN A CA    1 
ATOM   235  C C     . GLN A 1 33  ? -42.98030 58.39990 -4.88224  1.000 93.18484  ? 37  GLN A C     1 
ATOM   236  O O     . GLN A 1 33  ? -43.54346 59.41041 -5.32366  1.000 93.39350  ? 37  GLN A O     1 
ATOM   237  C CB    . GLN A 1 33  ? -45.10832 57.09216 -4.42469  1.000 92.42663  ? 37  GLN A CB    1 
ATOM   238  C CG    . GLN A 1 33  ? -45.99494 55.87960 -4.78113  1.000 93.65770  ? 37  GLN A CG    1 
ATOM   239  C CD    . GLN A 1 33  ? -47.48694 56.06920 -4.43222  1.000 99.58131  ? 37  GLN A CD    1 
ATOM   240  O OE1   . GLN A 1 33  ? -48.35424 56.04645 -5.31739  1.000 91.78441  ? 37  GLN A OE1   1 
ATOM   241  N NE2   . GLN A 1 33  ? -47.78452 56.23817 -3.14326  1.000 93.97171  ? 37  GLN A NE2   1 
ATOM   242  N N     . GLY A 1 34  ? -41.76673 58.46462 -4.33151  1.000 94.88060  ? 38  GLY A N     1 
ATOM   243  C CA    . GLY A 1 34  ? -41.01092 59.70024 -4.27061  1.000 98.21317  ? 38  GLY A CA    1 
ATOM   244  C C     . GLY A 1 34  ? -40.74545 60.12157 -2.82960  1.000 98.55364  ? 38  GLY A C     1 
ATOM   245  O O     . GLY A 1 34  ? -40.50919 59.28822 -1.95383  1.000 107.60701 ? 38  GLY A O     1 
ATOM   246  N N     . ILE A 1 35  ? -40.80631 61.42847 -2.59793  1.000 86.81055  ? 39  ILE A N     1 
ATOM   247  C CA    . ILE A 1 35  ? -40.27730 62.04442 -1.38903  1.000 84.88362  ? 39  ILE A CA    1 
ATOM   248  C C     . ILE A 1 35  ? -41.39624 62.79509 -0.67698  1.000 77.69522  ? 39  ILE A C     1 
ATOM   249  O O     . ILE A 1 35  ? -42.25077 63.41261 -1.32167  1.000 80.53150  ? 39  ILE A O     1 
ATOM   250  C CB    . ILE A 1 35  ? -39.09372 62.96708 -1.74845  1.000 84.11474  ? 39  ILE A CB    1 
ATOM   251  C CG1   . ILE A 1 35  ? -38.77348 63.93820 -0.62720  1.000 81.40400  ? 39  ILE A CG1   1 
ATOM   252  C CG2   . ILE A 1 35  ? -39.37317 63.71743 -3.03993  1.000 89.46601  ? 39  ILE A CG2   1 
ATOM   253  C CD1   . ILE A 1 35  ? -37.45869 64.63669 -0.85508  1.000 86.89813  ? 39  ILE A CD1   1 
ATOM   254  N N     . VAL A 1 36  ? -41.41454 62.70564 0.65154   1.000 68.81060  ? 40  VAL A N     1 
ATOM   255  C CA    . VAL A 1 36  ? -42.43575 63.34217 1.47325   1.000 69.63939  ? 40  VAL A CA    1 
ATOM   256  C C     . VAL A 1 36  ? -41.81277 64.51920 2.20609   1.000 68.18619  ? 40  VAL A C     1 
ATOM   257  O O     . VAL A 1 36  ? -40.68971 64.42313 2.70647   1.000 73.23503  ? 40  VAL A O     1 
ATOM   258  C CB    . VAL A 1 36  ? -43.06033 62.34372 2.46617   1.000 75.33731  ? 40  VAL A CB    1 
ATOM   259  C CG1   . VAL A 1 36  ? -44.10117 63.03441 3.35767   1.000 66.32238  ? 40  VAL A CG1   1 
ATOM   260  C CG2   . VAL A 1 36  ? -43.69654 61.18589 1.70584   1.000 70.92653  ? 40  VAL A CG2   1 
ATOM   261  N N     . CYS A 1 37  ? -42.53241 65.63589 2.25892   1.000 66.51761  ? 41  CYS A N     1 
ATOM   262  C CA    . CYS A 1 37  ? -42.05324 66.84393 2.91904   1.000 68.85359  ? 41  CYS A CA    1 
ATOM   263  C C     . CYS A 1 37  ? -42.96051 67.24698 4.07355   1.000 69.18956  ? 41  CYS A C     1 
ATOM   264  O O     . CYS A 1 37  ? -44.17956 67.08781 3.99960   1.000 73.40092  ? 41  CYS A O     1 
ATOM   265  C CB    . CYS A 1 37  ? -41.96284 68.00327 1.93878   1.000 70.40296  ? 41  CYS A CB    1 
ATOM   266  S SG    . CYS A 1 37  ? -40.57368 67.87890 0.80949   1.000 82.82871  ? 41  CYS A SG    1 
ATOM   267  N N     . ALA A 1 38  ? -42.36486 67.74226 5.15494   1.000 70.00289  ? 42  ALA A N     1 
ATOM   268  C CA    . ALA A 1 38  ? -43.13937 68.47080 6.14548   1.000 63.15931  ? 42  ALA A CA    1 
ATOM   269  C C     . ALA A 1 38  ? -43.25580 69.92217 5.70924   1.000 69.73715  ? 42  ALA A C     1 
ATOM   270  O O     . ALA A 1 38  ? -42.39144 70.44410 4.99865   1.000 75.97092  ? 42  ALA A O     1 
ATOM   271  C CB    . ALA A 1 38  ? -42.48232 68.39220 7.52337   1.000 61.61489  ? 42  ALA A CB    1 
ATOM   272  N N     . ALA A 1 39  ? -44.33756 70.57702 6.12078   1.000 69.24500  ? 43  ALA A N     1 
ATOM   273  C CA    . ALA A 1 39  ? -44.48329 71.99321 5.80708   1.000 71.64214  ? 43  ALA A CA    1 
ATOM   274  C C     . ALA A 1 39  ? -45.35699 72.66279 6.84996   1.000 78.04063  ? 43  ALA A C     1 
ATOM   275  O O     . ALA A 1 39  ? -46.12820 72.00924 7.56395   1.000 74.49851  ? 43  ALA A O     1 
ATOM   276  C CB    . ALA A 1 39  ? -45.08903 72.22991 4.41612   1.000 67.74535  ? 43  ALA A CB    1 
ATOM   277  N N     . TYR A 1 40  ? -45.23762 73.98781 6.90969   1.000 73.97980  ? 44  TYR A N     1 
ATOM   278  C CA    . TYR A 1 40  ? -46.09691 74.81000 7.74362   1.000 78.01369  ? 44  TYR A CA    1 
ATOM   279  C C     . TYR A 1 40  ? -47.22903 75.37785 6.88780   1.000 80.96908  ? 44  TYR A C     1 
ATOM   280  O O     . TYR A 1 40  ? -46.97489 76.06976 5.89008   1.000 80.86681  ? 44  TYR A O     1 
ATOM   281  C CB    . TYR A 1 40  ? -45.29040 75.92172 8.40300   1.000 82.71896  ? 44  TYR A CB    1 
ATOM   282  C CG    . TYR A 1 40  ? -46.11847 76.78795 9.30085   1.000 81.80935  ? 44  TYR A CG    1 
ATOM   283  C CD1   . TYR A 1 40  ? -46.39355 76.39379 10.60337  1.000 80.63432  ? 44  TYR A CD1   1 
ATOM   284  C CD2   . TYR A 1 40  ? -46.62232 77.99936 8.85216   1.000 82.10808  ? 44  TYR A CD2   1 
ATOM   285  C CE1   . TYR A 1 40  ? -47.15040 77.17604 11.43765  1.000 84.46507  ? 44  TYR A CE1   1 
ATOM   286  C CE2   . TYR A 1 40  ? -47.37985 78.79646 9.68083   1.000 89.13088  ? 44  TYR A CE2   1 
ATOM   287  C CZ    . TYR A 1 40  ? -47.64818 78.37956 10.97612  1.000 88.74065  ? 44  TYR A CZ    1 
ATOM   288  O OH    . TYR A 1 40  ? -48.41003 79.17054 11.81418  1.000 89.91519  ? 44  TYR A OH    1 
ATOM   289  N N     . ASP A 1 41  ? -48.47480 75.06425 7.26638   1.000 80.70273  ? 45  ASP A N     1 
ATOM   290  C CA    . ASP A 1 41  ? -49.66853 75.58303 6.59093   1.000 78.42450  ? 45  ASP A CA    1 
ATOM   291  C C     . ASP A 1 41  ? -50.11271 76.87010 7.28334   1.000 86.12077  ? 45  ASP A C     1 
ATOM   292  O O     . ASP A 1 41  ? -50.75004 76.82556 8.34530   1.000 81.91230  ? 45  ASP A O     1 
ATOM   293  C CB    . ASP A 1 41  ? -50.79512 74.55402 6.60717   1.000 73.82987  ? 45  ASP A CB    1 
ATOM   294  C CG    . ASP A 1 41  ? -52.06106 75.04373 5.88815   1.000 83.03512  ? 45  ASP A CG    1 
ATOM   295  O OD1   . ASP A 1 41  ? -52.06160 76.17964 5.36532   1.000 80.82292  ? 45  ASP A OD1   1 
ATOM   296  O OD2   . ASP A 1 41  ? -53.07751 74.29844 5.86348   1.000 82.52840  ? 45  ASP A OD2   1 
ATOM   297  N N     . ALA A 1 42  ? -49.82663 78.01474 6.64922   1.000 82.44020  ? 46  ALA A N     1 
ATOM   298  C CA    . ALA A 1 42  ? -50.07097 79.31350 7.27158   1.000 86.83023  ? 46  ALA A CA    1 
ATOM   299  C C     . ALA A 1 42  ? -51.54984 79.57823 7.53891   1.000 87.09409  ? 46  ALA A C     1 
ATOM   300  O O     . ALA A 1 42  ? -51.87064 80.39692 8.40742   1.000 90.99922  ? 46  ALA A O     1 
ATOM   301  C CB    . ALA A 1 42  ? -49.48636 80.42434 6.39528   1.000 85.67067  ? 46  ALA A CB    1 
ATOM   302  N N     . ILE A 1 43  ? -52.45176 78.88247 6.84357   1.000 87.40157  ? 47  ILE A N     1 
ATOM   303  C CA    . ILE A 1 43  ? -53.88544 79.08982 7.02916   1.000 79.93201  ? 47  ILE A CA    1 
ATOM   304  C C     . ILE A 1 43  ? -54.40702 78.29197 8.22231   1.000 84.22525  ? 47  ILE A C     1 
ATOM   305  O O     . ILE A 1 43  ? -55.17448 78.81222 9.04159   1.000 85.55755  ? 47  ILE A O     1 
ATOM   306  C CB    . ILE A 1 43  ? -54.63117 78.74236 5.72898   1.000 79.48702  ? 47  ILE A CB    1 
ATOM   307  C CG1   . ILE A 1 43  ? -54.29906 79.77943 4.64858   1.000 75.02092  ? 47  ILE A CG1   1 
ATOM   308  C CG2   . ILE A 1 43  ? -56.12899 78.66249 5.96104   1.000 78.96778  ? 47  ILE A CG2   1 
ATOM   309  C CD1   . ILE A 1 43  ? -54.58950 79.28902 3.25893   1.000 80.38432  ? 47  ILE A CD1   1 
ATOM   310  N N     . LEU A 1 44  ? -54.01484 77.01264 8.33567   1.000 86.68604  ? 48  LEU A N     1 
ATOM   311  C CA    . LEU A 1 44  ? -54.39934 76.18137 9.48005   1.000 81.62299  ? 48  LEU A CA    1 
ATOM   312  C C     . LEU A 1 44  ? -53.48521 76.38312 10.68844  1.000 89.50103  ? 48  LEU A C     1 
ATOM   313  O O     . LEU A 1 44  ? -53.83416 75.93141 11.79397  1.000 85.47881  ? 48  LEU A O     1 
ATOM   314  C CB    . LEU A 1 44  ? -54.39690 74.70294 9.07015   1.000 76.37595  ? 48  LEU A CB    1 
ATOM   315  C CG    . LEU A 1 44  ? -55.47232 74.24381 8.07342   1.000 84.30203  ? 48  LEU A CG    1 
ATOM   316  C CD1   . LEU A 1 44  ? -55.22943 72.80136 7.63118   1.000 85.04209  ? 48  LEU A CD1   1 
ATOM   317  C CD2   . LEU A 1 44  ? -56.87893 74.37517 8.65776   1.000 73.99552  ? 48  LEU A CD2   1 
ATOM   318  N N     . GLU A 1 45  ? -52.32716 77.03718 10.48459  1.000 84.97878  ? 49  GLU A N     1 
ATOM   319  C CA    . GLU A 1 45  ? -51.35081 77.34687 11.53206  1.000 83.72340  ? 49  GLU A CA    1 
ATOM   320  C C     . GLU A 1 45  ? -50.90524 76.08640 12.27183  1.000 83.11187  ? 49  GLU A C     1 
ATOM   321  O O     . GLU A 1 45  ? -50.97023 75.99423 13.50268  1.000 83.25912  ? 49  GLU A O     1 
ATOM   322  C CB    . GLU A 1 45  ? -51.89909 78.40314 12.49320  1.000 87.50573  ? 49  GLU A CB    1 
ATOM   323  C CG    . GLU A 1 45  ? -51.47217 79.81538 12.10197  1.000 98.11728  ? 49  GLU A CG    1 
ATOM   324  C CD    . GLU A 1 45  ? -52.43077 80.89385 12.57663  1.000 110.22046 ? 49  GLU A CD    1 
ATOM   325  O OE1   . GLU A 1 45  ? -53.43732 81.11303 11.86562  1.000 110.51011 ? 49  GLU A OE1   1 
ATOM   326  O OE2   . GLU A 1 45  ? -52.16099 81.54347 13.62138  1.000 109.56448 ? 49  GLU A OE2   1 
ATOM   327  N N     . ARG A 1 46  ? -50.44308 75.10866 11.49598  1.000 85.57909  ? 50  ARG A N     1 
ATOM   328  C CA    . ARG A 1 46  ? -49.89046 73.87313 12.03125  1.000 82.77419  ? 50  ARG A CA    1 
ATOM   329  C C     . ARG A 1 46  ? -49.07086 73.22111 10.93158  1.000 77.55919  ? 50  ARG A C     1 
ATOM   330  O O     . ARG A 1 46  ? -49.16921 73.59014 9.75395   1.000 70.43495  ? 50  ARG A O     1 
ATOM   331  C CB    . ARG A 1 46  ? -50.98791 72.93276 12.51447  1.000 80.86669  ? 50  ARG A CB    1 
ATOM   332  C CG    . ARG A 1 46  ? -52.03546 72.71543 11.45860  1.000 80.33287  ? 50  ARG A CG    1 
ATOM   333  C CD    . ARG A 1 46  ? -53.13514 71.79545 11.95014  1.000 86.69629  ? 50  ARG A CD    1 
ATOM   334  N NE    . ARG A 1 46  ? -52.89956 70.40772 11.57493  1.000 87.60988  ? 50  ARG A NE    1 
ATOM   335  C CZ    . ARG A 1 46  ? -53.84614 69.48051 11.55462  1.000 83.18240  ? 50  ARG A CZ    1 
ATOM   336  N NH1   . ARG A 1 46  ? -55.10076 69.77972 11.85337  1.000 87.30277  ? 50  ARG A NH1   1 
ATOM   337  N NH2   . ARG A 1 46  ? -53.52555 68.22378 11.23030  1.000 72.80838  ? 50  ARG A NH2   1 
ATOM   338  N N     . ASN A 1 47  ? -48.26038 72.24192 11.33613  1.000 81.81984  ? 51  ASN A N     1 
ATOM   339  C CA    . ASN A 1 47  ? -47.45545 71.47207 10.39902  1.000 74.35446  ? 51  ASN A CA    1 
ATOM   340  C C     . ASN A 1 47  ? -48.30467 70.43113 9.68461   1.000 71.04775  ? 51  ASN A C     1 
ATOM   341  O O     . ASN A 1 47  ? -49.26218 69.87690 10.23919  1.000 71.50638  ? 51  ASN A O     1 
ATOM   342  C CB    . ASN A 1 47  ? -46.30845 70.74900 11.10364  1.000 74.12537  ? 51  ASN A CB    1 
ATOM   343  C CG    . ASN A 1 47  ? -45.27493 71.69085 11.66933  1.000 82.01546  ? 51  ASN A CG    1 
ATOM   344  O OD1   . ASN A 1 47  ? -44.82811 72.64998 11.00619  1.000 80.63721  ? 51  ASN A OD1   1 
ATOM   345  N ND2   . ASN A 1 47  ? -44.84777 71.39573 12.90083  1.000 74.79782  ? 51  ASN A ND2   1 
ATOM   346  N N     . VAL A 1 48  ? -47.92696 70.14981 8.44342   1.000 66.06283  ? 52  VAL A N     1 
ATOM   347  C CA    . VAL A 1 48  ? -48.57975 69.12982 7.64428   1.000 70.23270  ? 52  VAL A CA    1 
ATOM   348  C C     . VAL A 1 48  ? -47.51528 68.30136 6.93535   1.000 68.47955  ? 52  VAL A C     1 
ATOM   349  O O     . VAL A 1 48  ? -46.32475 68.62331 6.94483   1.000 68.40018  ? 52  VAL A O     1 
ATOM   350  C CB    . VAL A 1 48  ? -49.54380 69.74153 6.61732   1.000 69.19014  ? 52  VAL A CB    1 
ATOM   351  C CG1   . VAL A 1 48  ? -50.60184 70.64495 7.31355   1.000 63.95914  ? 52  VAL A CG1   1 
ATOM   352  C CG2   . VAL A 1 48  ? -48.72893 70.51773 5.59573   1.000 69.89605  ? 52  VAL A CG2   1 
ATOM   353  N N     . ALA A 1 49  ? -47.96832 67.23616 6.29353   1.000 64.25128  ? 53  ALA A N     1 
ATOM   354  C CA    . ALA A 1 49  ? -47.13157 66.42730 5.42711   1.000 66.63879  ? 53  ALA A CA    1 
ATOM   355  C C     . ALA A 1 49  ? -47.63031 66.55749 3.99703   1.000 67.38407  ? 53  ALA A C     1 
ATOM   356  O O     . ALA A 1 49  ? -48.82694 66.73586 3.75787   1.000 67.52278  ? 53  ALA A O     1 
ATOM   357  C CB    . ALA A 1 49  ? -47.13248 64.96251 5.85832   1.000 63.62828  ? 53  ALA A CB    1 
ATOM   358  N N     . ILE A 1 50  ? -46.69355 66.50854 3.04908   1.000 67.00436  ? 54  ILE A N     1 
ATOM   359  C CA    . ILE A 1 50  ? -46.98354 66.75664 1.63951   1.000 66.97320  ? 54  ILE A CA    1 
ATOM   360  C C     . ILE A 1 50  ? -46.29723 65.67766 0.81360   1.000 69.15200  ? 54  ILE A C     1 
ATOM   361  O O     . ILE A 1 50  ? -45.06768 65.56092 0.83354   1.000 75.29662  ? 54  ILE A O     1 
ATOM   362  C CB    . ILE A 1 50  ? -46.52403 68.15510 1.17847   1.000 68.35686  ? 54  ILE A CB    1 
ATOM   363  C CG1   . ILE A 1 50  ? -47.23510 69.26518 1.96292   1.000 62.62525  ? 54  ILE A CG1   1 
ATOM   364  C CG2   . ILE A 1 50  ? -46.77658 68.33454 -0.32018  1.000 69.05624  ? 54  ILE A CG2   1 
ATOM   365  C CD1   . ILE A 1 50  ? -47.15152 70.63545 1.25934   1.000 66.43965  ? 54  ILE A CD1   1 
ATOM   366  N N     . LYS A 1 51  ? -47.08148 64.90668 0.07969   1.000 70.36834  ? 55  LYS A N     1 
ATOM   367  C CA    . LYS A 1 51  ? -46.59008 63.82769 -0.75287  1.000 70.51790  ? 55  LYS A CA    1 
ATOM   368  C C     . LYS A 1 51  ? -46.80652 64.25827 -2.18975  1.000 71.18286  ? 55  LYS A C     1 
ATOM   369  O O     . LYS A 1 51  ? -47.81283 64.90149 -2.49038  1.000 71.63741  ? 55  LYS A O     1 
ATOM   370  C CB    . LYS A 1 51  ? -47.35468 62.53723 -0.42670  1.000 72.49116  ? 55  LYS A CB    1 
ATOM   371  C CG    . LYS A 1 51  ? -46.94754 61.26247 -1.13780  1.000 74.70532  ? 55  LYS A CG    1 
ATOM   372  C CD    . LYS A 1 51  ? -48.11871 60.28096 -1.14648  1.000 78.41695  ? 55  LYS A CD    1 
ATOM   373  C CE    . LYS A 1 51  ? -47.65666 58.83897 -1.12751  1.000 78.05621  ? 55  LYS A CE    1 
ATOM   374  N NZ    . LYS A 1 51  ? -47.49920 58.36803 0.27711   1.000 78.98160  ? 55  LYS A NZ    1 
ATOM   375  N N     . LYS A 1 52  ? -45.85893 63.94275 -3.07099  1.000 71.53297  ? 56  LYS A N     1 
ATOM   376  C CA    . LYS A 1 52  ? -45.99238 64.28353 -4.48260  1.000 78.55763  ? 56  LYS A CA    1 
ATOM   377  C C     . LYS A 1 52  ? -46.00696 63.02301 -5.32852  1.000 83.31837  ? 56  LYS A C     1 
ATOM   378  O O     . LYS A 1 52  ? -45.07743 62.21013 -5.25434  1.000 91.29761  ? 56  LYS A O     1 
ATOM   379  C CB    . LYS A 1 52  ? -44.85760 65.18802 -4.96750  1.000 79.60265  ? 56  LYS A CB    1 
ATOM   380  C CG    . LYS A 1 52  ? -45.07154 65.64121 -6.40118  1.000 77.29306  ? 56  LYS A CG    1 
ATOM   381  C CD    . LYS A 1 52  ? -43.99798 66.59759 -6.90643  1.000 81.96681  ? 56  LYS A CD    1 
ATOM   382  C CE    . LYS A 1 52  ? -42.85597 65.86241 -7.56807  1.000 85.78785  ? 56  LYS A CE    1 
ATOM   383  N NZ    . LYS A 1 52  ? -42.36645 66.69527 -8.69193  1.000 88.40488  ? 56  LYS A NZ    1 
ATOM   384  N N     . LEU A 1 53  ? -47.04124 62.88096 -6.15374  1.000 82.32791  ? 57  LEU A N     1 
ATOM   385  C CA    . LEU A 1 53  ? -47.09165 61.84513 -7.18360  1.000 85.15565  ? 57  LEU A CA    1 
ATOM   386  C C     . LEU A 1 53  ? -46.80277 62.51360 -8.52338  1.000 83.44018  ? 57  LEU A C     1 
ATOM   387  O O     . LEU A 1 53  ? -47.62000 63.29530 -9.02245  1.000 81.03786  ? 57  LEU A O     1 
ATOM   388  C CB    . LEU A 1 53  ? -48.45005 61.15102 -7.20954  1.000 72.32518  ? 57  LEU A CB    1 
ATOM   389  C CG    . LEU A 1 53  ? -49.08623 60.79575 -5.86969  1.000 72.47425  ? 57  LEU A CG    1 
ATOM   390  C CD1   . LEU A 1 53  ? -50.47685 60.20365 -6.07980  1.000 71.35218  ? 57  LEU A CD1   1 
ATOM   391  C CD2   . LEU A 1 53  ? -48.20938 59.81934 -5.13226  1.000 80.49861  ? 57  LEU A CD2   1 
ATOM   392  N N     . SER A 1 54  ? -45.64871 62.21642 -9.10455  1.000 82.61462  ? 58  SER A N     1 
ATOM   393  C CA    . SER A 1 54  ? -45.27825 62.80179 -10.38254 1.000 87.72569  ? 58  SER A CA    1 
ATOM   394  C C     . SER A 1 54  ? -45.65586 61.83950 -11.50274 1.000 90.62673  ? 58  SER A C     1 
ATOM   395  O O     . SER A 1 54  ? -45.39281 60.63372 -11.40749 1.000 93.26787  ? 58  SER A O     1 
ATOM   396  C CB    . SER A 1 54  ? -43.78886 63.16817 -10.41602 1.000 86.39683  ? 58  SER A CB    1 
ATOM   397  O OG    . SER A 1 54  ? -42.96673 62.09656 -10.00850 1.000 93.90575  ? 58  SER A OG    1 
ATOM   398  N N     . ARG A 1 55  ? -46.30884 62.38995 -12.55031 1.000 90.74747  ? 59  ARG A N     1 
ATOM   399  C CA    . ARG A 1 55  ? -46.86349 61.72956 -13.73436 1.000 92.57841  ? 59  ARG A CA    1 
ATOM   400  C C     . ARG A 1 55  ? -47.40931 60.35200 -13.39302 1.000 93.29275  ? 59  ARG A C     1 
ATOM   401  O O     . ARG A 1 55  ? -47.01279 59.35791 -14.01461 1.000 93.14135  ? 59  ARG A O     1 
ATOM   402  C CB    . ARG A 1 55  ? -45.81146 61.61335 -14.83673 1.000 100.11203 ? 59  ARG A CB    1 
ATOM   403  C CG    . ARG A 1 55  ? -45.54961 62.90201 -15.58932 1.000 103.81250 ? 59  ARG A CG    1 
ATOM   404  C CD    . ARG A 1 55  ? -44.20847 62.82850 -16.29493 1.000 125.88296 ? 59  ARG A CD    1 
ATOM   405  N NE    . ARG A 1 55  ? -43.37083 61.76420 -15.74606 1.000 131.29675 ? 59  ARG A NE    1 
ATOM   406  C CZ    . ARG A 1 55  ? -42.26748 61.95523 -15.02984 1.000 134.80759 ? 59  ARG A CZ    1 
ATOM   407  N NH1   . ARG A 1 55  ? -41.80853 63.17313 -14.77108 1.000 132.93633 ? 59  ARG A NH1   1 
ATOM   408  N NH2   . ARG A 1 55  ? -41.60745 60.89666 -14.56006 1.000 131.22330 ? 59  ARG A NH2   1 
ATOM   409  N N     . PRO A 1 56  ? -48.30053 60.24610 -12.40678 1.000 91.87843  ? 60  PRO A N     1 
ATOM   410  C CA    . PRO A 1 56  ? -48.73013 58.91026 -11.96579 1.000 89.23628  ? 60  PRO A CA    1 
ATOM   411  C C     . PRO A 1 56  ? -49.44967 58.11721 -13.04920 1.000 93.52608  ? 60  PRO A C     1 
ATOM   412  O O     . PRO A 1 56  ? -49.40364 56.87898 -13.01981 1.000 92.53654  ? 60  PRO A O     1 
ATOM   413  C CB    . PRO A 1 56  ? -49.63635 59.21909 -10.76967 1.000 83.11414  ? 60  PRO A CB    1 
ATOM   414  C CG    . PRO A 1 56  ? -50.15952 60.58668 -11.04697 1.000 83.88560  ? 60  PRO A CG    1 
ATOM   415  C CD    . PRO A 1 56  ? -49.06814 61.32386 -11.75501 1.000 84.54289  ? 60  PRO A CD    1 
ATOM   416  N N     . PHE A 1 57  ? -50.09204 58.78926 -14.01674 1.000 90.83780  ? 61  PHE A N     1 
ATOM   417  C CA    . PHE A 1 57  ? -50.73784 58.13767 -15.15712 1.000 88.05962  ? 61  PHE A CA    1 
ATOM   418  C C     . PHE A 1 57  ? -49.73943 57.62042 -16.19940 1.000 92.60040  ? 61  PHE A C     1 
ATOM   419  O O     . PHE A 1 57  ? -50.17364 57.16272 -17.26359 1.000 94.45818  ? 61  PHE A O     1 
ATOM   420  C CB    . PHE A 1 57  ? -51.71242 59.11236 -15.83213 1.000 85.74256  ? 61  PHE A CB    1 
ATOM   421  C CG    . PHE A 1 57  ? -51.06399 60.40641 -16.23731 1.000 92.44365  ? 61  PHE A CG    1 
ATOM   422  C CD1   . PHE A 1 57  ? -50.34799 60.50197 -17.42068 1.000 92.55672  ? 61  PHE A CD1   1 
ATOM   423  C CD2   . PHE A 1 57  ? -51.11730 61.50919 -15.40593 1.000 88.51035  ? 61  PHE A CD2   1 
ATOM   424  C CE1   . PHE A 1 57  ? -49.71993 61.68341 -17.78010 1.000 92.46399  ? 61  PHE A CE1   1 
ATOM   425  C CE2   . PHE A 1 57  ? -50.48843 62.69270 -15.76336 1.000 94.46110  ? 61  PHE A CE2   1 
ATOM   426  C CZ    . PHE A 1 57  ? -49.78983 62.77747 -16.95205 1.000 91.21874  ? 61  PHE A CZ    1 
ATOM   427  N N     . GLN A 1 58  ? -48.42658 57.68909 -15.93232 1.000 92.50172  ? 62  GLN A N     1 
ATOM   428  C CA    . GLN A 1 58  ? -47.43352 57.37360 -16.96358 1.000 97.15732  ? 62  GLN A CA    1 
ATOM   429  C C     . GLN A 1 58  ? -47.45981 55.89984 -17.36598 1.000 101.83912 ? 62  GLN A C     1 
ATOM   430  O O     . GLN A 1 58  ? -47.16415 55.57771 -18.52196 1.000 110.17990 ? 62  GLN A O     1 
ATOM   431  C CB    . GLN A 1 58  ? -46.02479 57.75954 -16.49610 1.000 101.57642 ? 62  GLN A CB    1 
ATOM   432  C CG    . GLN A 1 58  ? -45.44009 56.80551 -15.46055 1.000 107.71970 ? 62  GLN A CG    1 
ATOM   433  C CD    . GLN A 1 58  ? -44.18895 57.32955 -14.78438 1.000 113.93594 ? 62  GLN A CD    1 
ATOM   434  O OE1   . GLN A 1 58  ? -43.09376 56.79486 -14.98387 1.000 120.01552 ? 62  GLN A OE1   1 
ATOM   435  N NE2   . GLN A 1 58  ? -44.34594 58.36400 -13.95892 1.000 109.92467 ? 62  GLN A NE2   1 
ATOM   436  N N     . ASN A 1 59  ? -47.78907 54.99219 -16.44506 1.000 98.31142  ? 63  ASN A N     1 
ATOM   437  C CA    . ASN A 1 59  ? -47.89732 53.58001 -16.79108 1.000 97.31850  ? 63  ASN A CA    1 
ATOM   438  C C     . ASN A 1 59  ? -48.88140 52.90310 -15.84884 1.000 93.27152  ? 63  ASN A C     1 
ATOM   439  O O     . ASN A 1 59  ? -49.34635 53.49473 -14.87194 1.000 91.68859  ? 63  ASN A O     1 
ATOM   440  C CB    . ASN A 1 59  ? -46.52944 52.87948 -16.76247 1.000 92.95486  ? 63  ASN A CB    1 
ATOM   441  C CG    . ASN A 1 59  ? -45.97265 52.70909 -15.35456 1.000 94.40248  ? 63  ASN A CG    1 
ATOM   442  O OD1   . ASN A 1 59  ? -46.59404 52.09123 -14.49528 1.000 93.15489  ? 63  ASN A OD1   1 
ATOM   443  N ND2   . ASN A 1 59  ? -44.77255 53.23470 -15.12619 1.000 103.63056 ? 63  ASN A ND2   1 
ATOM   444  N N     . GLN A 1 60  ? -49.14782 51.62467 -16.12581 1.000 94.06814  ? 64  GLN A N     1 
ATOM   445  C CA    . GLN A 1 60  ? -50.24809 50.92484 -15.46959 1.000 92.34467  ? 64  GLN A CA    1 
ATOM   446  C C     . GLN A 1 60  ? -50.07760 50.86995 -13.95696 1.000 90.84523  ? 64  GLN A C     1 
ATOM   447  O O     . GLN A 1 60  ? -50.97388 51.27793 -13.20759 1.000 90.78785  ? 64  GLN A O     1 
ATOM   448  C CB    . GLN A 1 60  ? -50.37123 49.51188 -16.02604 1.000 96.21991  ? 64  GLN A CB    1 
ATOM   449  C CG    . GLN A 1 60  ? -51.79825 49.11489 -16.24793 1.000 107.79125 ? 64  GLN A CG    1 
ATOM   450  C CD    . GLN A 1 60  ? -52.39122 49.83732 -17.44882 1.000 122.88545 ? 64  GLN A CD    1 
ATOM   451  O OE1   . GLN A 1 60  ? -51.66274 50.34014 -18.31745 1.000 116.44234 ? 64  GLN A OE1   1 
ATOM   452  N NE2   . GLN A 1 60  ? -53.71855 49.89350 -17.50580 1.000 124.66149 ? 64  GLN A NE2   1 
ATOM   453  N N     . THR A 1 61  ? -48.93179 50.36076 -13.48530 1.000 85.90137  ? 65  THR A N     1 
ATOM   454  C CA    . THR A 1 61  ? -48.80550 50.05947 -12.05950 1.000 87.14342  ? 65  THR A CA    1 
ATOM   455  C C     . THR A 1 61  ? -48.75161 51.33582 -11.21670 1.000 89.76992  ? 65  THR A C     1 
ATOM   456  O O     . THR A 1 61  ? -49.26642 51.36115 -10.08786 1.000 86.60970  ? 65  THR A O     1 
ATOM   457  C CB    . THR A 1 61  ? -47.58346 49.17363 -11.80037 1.000 82.22353  ? 65  THR A CB    1 
ATOM   458  O OG1   . THR A 1 61  ? -46.39710 49.87347 -12.17346 1.000 96.34335  ? 65  THR A OG1   1 
ATOM   459  C CG2   . THR A 1 61  ? -47.66435 47.87873 -12.61351 1.000 82.27631  ? 65  THR A CG2   1 
ATOM   460  N N     . HIS A 1 62  ? -48.14191 52.40731 -11.74423 1.000 87.60350  ? 66  HIS A N     1 
ATOM   461  C CA    . HIS A 1 62  ? -48.16711 53.69197 -11.04536 1.000 81.19946  ? 66  HIS A CA    1 
ATOM   462  C C     . HIS A 1 62  ? -49.56989 54.26916 -11.00420 1.000 79.08092  ? 66  HIS A C     1 
ATOM   463  O O     . HIS A 1 62  ? -49.96716 54.86248 -9.99408  1.000 77.72281  ? 66  HIS A O     1 
ATOM   464  C CB    . HIS A 1 62  ? -47.22125 54.68712 -11.71118 1.000 90.41121  ? 66  HIS A CB    1 
ATOM   465  C CG    . HIS A 1 62  ? -45.79116 54.24447 -11.73912 1.000 98.48984  ? 66  HIS A CG    1 
ATOM   466  N ND1   . HIS A 1 62  ? -44.76590 55.00104 -11.21042 1.000 95.73725  ? 66  HIS A ND1   1 
ATOM   467  C CD2   . HIS A 1 62  ? -45.21941 53.10798 -12.20571 1.000 98.82498  ? 66  HIS A CD2   1 
ATOM   468  C CE1   . HIS A 1 62  ? -43.62133 54.35947 -11.37639 1.000 103.68268 ? 66  HIS A CE1   1 
ATOM   469  N NE2   . HIS A 1 62  ? -43.86946 53.20695 -11.97578 1.000 110.22022 ? 66  HIS A NE2   1 
ATOM   470  N N     . ALA A 1 63  ? -50.32832 54.11932 -12.10166 1.000 83.97323  ? 67  ALA A N     1 
ATOM   471  C CA    . ALA A 1 63  ? -51.66729 54.70640 -12.18865 1.000 82.64517  ? 67  ALA A CA    1 
ATOM   472  C C     . ALA A 1 63  ? -52.63553 54.03482 -11.22842 1.000 79.91896  ? 67  ALA A C     1 
ATOM   473  O O     . ALA A 1 63  ? -53.35243 54.70968 -10.48075 1.000 78.84954  ? 67  ALA A O     1 
ATOM   474  C CB    . ALA A 1 63  ? -52.19903 54.60451 -13.61178 1.000 80.39563  ? 67  ALA A CB    1 
ATOM   475  N N     . LYS A 1 64  ? -52.68071 52.70220 -11.24625 1.000 82.83206  ? 68  LYS A N     1 
ATOM   476  C CA    . LYS A 1 64  ? -53.54391 51.97747 -10.31943 1.000 81.82013  ? 68  LYS A CA    1 
ATOM   477  C C     . LYS A 1 64  ? -53.20502 52.34989 -8.88404  1.000 74.96263  ? 68  LYS A C     1 
ATOM   478  O O     . LYS A 1 64  ? -54.10077 52.58403 -8.06176  1.000 72.31780  ? 68  LYS A O     1 
ATOM   479  C CB    . LYS A 1 64  ? -53.39156 50.46974 -10.55954 1.000 87.01397  ? 68  LYS A CB    1 
ATOM   480  C CG    . LYS A 1 64  ? -54.09095 49.52985 -9.58653  1.000 88.56504  ? 68  LYS A CG    1 
ATOM   481  C CD    . LYS A 1 64  ? -53.22949 48.27827 -9.36108  1.000 95.73731  ? 68  LYS A CD    1 
ATOM   482  C CE    . LYS A 1 64  ? -52.34707 47.94007 -10.57361 1.000 98.05260  ? 68  LYS A CE    1 
ATOM   483  N NZ    . LYS A 1 64  ? -51.57719 46.65810 -10.40150 1.000 97.34210  ? 68  LYS A NZ    1 
ATOM   484  N N     . ARG A 1 65  ? -51.90967 52.45186 -8.58259  1.000 71.48513  ? 69  ARG A N     1 
ATOM   485  C CA    . ARG A 1 65  ? -51.47311 52.75430 -7.22522  1.000 73.29299  ? 69  ARG A CA    1 
ATOM   486  C C     . ARG A 1 65  ? -51.91174 54.15975 -6.79925  1.000 74.13951  ? 69  ARG A C     1 
ATOM   487  O O     . ARG A 1 65  ? -52.33842 54.35793 -5.65545  1.000 74.65813  ? 69  ARG A O     1 
ATOM   488  C CB    . ARG A 1 65  ? -49.95023 52.56596 -7.14155  1.000 70.97922  ? 69  ARG A CB    1 
ATOM   489  C CG    . ARG A 1 65  ? -49.33701 52.77555 -5.77614  1.000 78.14529  ? 69  ARG A CG    1 
ATOM   490  C CD    . ARG A 1 65  ? -47.84746 53.06829 -5.90787  1.000 85.03148  ? 69  ARG A CD    1 
ATOM   491  N NE    . ARG A 1 65  ? -47.00629 51.90895 -5.62835  1.000 97.24221  ? 69  ARG A NE    1 
ATOM   492  C CZ    . ARG A 1 65  ? -46.76206 51.43202 -4.41193  1.000 99.33746  ? 69  ARG A CZ    1 
ATOM   493  N NH1   . ARG A 1 65  ? -47.25111 52.02261 -3.32592  1.000 86.72734  ? 69  ARG A NH1   1 
ATOM   494  N NH2   . ARG A 1 65  ? -45.99816 50.34299 -4.28078  1.000 87.27122  ? 69  ARG A NH2   1 
ATOM   495  N N     . ALA A 1 66  ? -51.84178 55.14058 -7.71219  1.000 70.64057  ? 70  ALA A N     1 
ATOM   496  C CA    . ALA A 1 66  ? -52.24757 56.50896 -7.38897  1.000 67.27345  ? 70  ALA A CA    1 
ATOM   497  C C     . ALA A 1 66  ? -53.75707 56.62892 -7.21607  1.000 70.92739  ? 70  ALA A C     1 
ATOM   498  O O     . ALA A 1 66  ? -54.23320 57.22758 -6.24256  1.000 72.34044  ? 70  ALA A O     1 
ATOM   499  C CB    . ALA A 1 66  ? -51.78535 57.46761 -8.48849  1.000 71.62795  ? 70  ALA A CB    1 
ATOM   500  N N     . TYR A 1 67  ? -54.52502 56.08982 -8.17067  1.000 69.52924  ? 71  TYR A N     1 
ATOM   501  C CA    . TYR A 1 67  ? -55.98101 56.09649 -8.06587  1.000 73.76975  ? 71  TYR A CA    1 
ATOM   502  C C     . TYR A 1 67  ? -56.43389 55.52220 -6.72931  1.000 71.03753  ? 71  TYR A C     1 
ATOM   503  O O     . TYR A 1 67  ? -57.19755 56.15486 -5.98965  1.000 66.92591  ? 71  TYR A O     1 
ATOM   504  C CB    . TYR A 1 67  ? -56.58247 55.28261 -9.21172  1.000 72.98574  ? 71  TYR A CB    1 
ATOM   505  C CG    . TYR A 1 67  ? -58.06008 55.48719 -9.40061  1.000 76.01452  ? 71  TYR A CG    1 
ATOM   506  C CD1   . TYR A 1 67  ? -58.94171 54.41218 -9.36700  1.000 81.71522  ? 71  TYR A CD1   1 
ATOM   507  C CD2   . TYR A 1 67  ? -58.57922 56.74855 -9.63399  1.000 77.92547  ? 71  TYR A CD2   1 
ATOM   508  C CE1   . TYR A 1 67  ? -60.31249 54.59712 -9.55350  1.000 84.18376  ? 71  TYR A CE1   1 
ATOM   509  C CE2   . TYR A 1 67  ? -59.94272 56.94672 -9.82500  1.000 78.66923  ? 71  TYR A CE2   1 
ATOM   510  C CZ    . TYR A 1 67  ? -60.80338 55.86982 -9.77873  1.000 85.01767  ? 71  TYR A CZ    1 
ATOM   511  O OH    . TYR A 1 67  ? -62.15770 56.06162 -9.95971  1.000 94.50328  ? 71  TYR A OH    1 
ATOM   512  N N     . ARG A 1 68  ? -55.93946 54.33032 -6.38780  1.000 70.21241  ? 72  ARG A N     1 
ATOM   513  C CA    . ARG A 1 68  ? -56.29641 53.72002 -5.11290  1.000 71.85649  ? 72  ARG A CA    1 
ATOM   514  C C     . ARG A 1 68  ? -55.99153 54.66069 -3.95351  1.000 71.79780  ? 72  ARG A C     1 
ATOM   515  O O     . ARG A 1 68  ? -56.84072 54.86570 -3.07262  1.000 68.76230  ? 72  ARG A O     1 
ATOM   516  C CB    . ARG A 1 68  ? -55.55265 52.39578 -4.94533  1.000 71.19549  ? 72  ARG A CB    1 
ATOM   517  C CG    . ARG A 1 68  ? -56.33271 51.19256 -5.44377  1.000 77.10559  ? 72  ARG A CG    1 
ATOM   518  C CD    . ARG A 1 68  ? -55.41197 50.04025 -5.79945  1.000 78.68900  ? 72  ARG A CD    1 
ATOM   519  N NE    . ARG A 1 68  ? -56.16083 48.80255 -5.92378  1.000 78.50761  ? 72  ARG A NE    1 
ATOM   520  C CZ    . ARG A 1 68  ? -55.63070 47.63217 -6.23710  1.000 84.80373  ? 72  ARG A CZ    1 
ATOM   521  N NH1   . ARG A 1 68  ? -54.33823 47.50790 -6.50515  1.000 83.21681  ? 72  ARG A NH1   1 
ATOM   522  N NH2   . ARG A 1 68  ? -56.41814 46.55865 -6.27761  1.000 92.15912  ? 72  ARG A NH2   1 
ATOM   523  N N     . GLU A 1 69  ? -54.80199 55.27653 -3.95935  1.000 62.83125  ? 73  GLU A N     1 
ATOM   524  C CA    . GLU A 1 69  ? -54.45021 56.19594 -2.88233  1.000 70.57947  ? 73  GLU A CA    1 
ATOM   525  C C     . GLU A 1 69  ? -55.47481 57.32928 -2.76297  1.000 71.64553  ? 73  GLU A C     1 
ATOM   526  O O     . GLU A 1 69  ? -56.05457 57.54835 -1.68909  1.000 69.58674  ? 73  GLU A O     1 
ATOM   527  C CB    . GLU A 1 69  ? -53.04106 56.75495 -3.10906  1.000 74.84385  ? 73  GLU A CB    1 
ATOM   528  C CG    . GLU A 1 69  ? -52.57560 57.71129 -2.00132  1.000 76.78198  ? 73  GLU A CG    1 
ATOM   529  C CD    . GLU A 1 69  ? -51.57717 57.08251 -1.03228  1.000 90.51479  ? 73  GLU A CD    1 
ATOM   530  O OE1   . GLU A 1 69  ? -50.46937 56.67946 -1.48124  1.000 94.29517  ? 73  GLU A OE1   1 
ATOM   531  O OE2   . GLU A 1 69  ? -51.92053 56.96186 0.17320   1.000 84.25165  ? 73  GLU A OE2   1 
ATOM   532  N N     . LEU A 1 70  ? -55.74524 58.03330 -3.86657  1.000 69.78511  ? 74  LEU A N     1 
ATOM   533  C CA    . LEU A 1 70  ? -56.66746 59.16425 -3.80583  1.000 70.94451  ? 74  LEU A CA    1 
ATOM   534  C C     . LEU A 1 70  ? -58.03904 58.72556 -3.32047  1.000 73.08567  ? 74  LEU A C     1 
ATOM   535  O O     . LEU A 1 70  ? -58.60997 59.34020 -2.41163  1.000 75.21672  ? 74  LEU A O     1 
ATOM   536  C CB    . LEU A 1 70  ? -56.78255 59.82788 -5.17185  1.000 65.35610  ? 74  LEU A CB    1 
ATOM   537  C CG    . LEU A 1 70  ? -55.51199 60.51946 -5.64604  1.000 64.54525  ? 74  LEU A CG    1 
ATOM   538  C CD1   . LEU A 1 70  ? -55.60429 60.85449 -7.13199  1.000 58.77808  ? 74  LEU A CD1   1 
ATOM   539  C CD2   . LEU A 1 70  ? -55.38325 61.76038 -4.84631  1.000 69.47623  ? 74  LEU A CD2   1 
ATOM   540  N N     . VAL A 1 71  ? -58.57964 57.64876 -3.89961  1.000 71.52636  ? 75  VAL A N     1 
ATOM   541  C CA    . VAL A 1 71  ? -59.95884 57.27990 -3.59098  1.000 67.01418  ? 75  VAL A CA    1 
ATOM   542  C C     . VAL A 1 71  ? -60.08564 56.93108 -2.12307  1.000 67.43407  ? 75  VAL A C     1 
ATOM   543  O O     . VAL A 1 71  ? -61.03608 57.34973 -1.45140  1.000 71.73470  ? 75  VAL A O     1 
ATOM   544  C CB    . VAL A 1 71  ? -60.44405 56.11623 -4.47230  1.000 72.34101  ? 75  VAL A CB    1 
ATOM   545  C CG1   . VAL A 1 71  ? -61.75701 55.58152 -3.93568  1.000 74.53066  ? 75  VAL A CG1   1 
ATOM   546  C CG2   . VAL A 1 71  ? -60.60383 56.56322 -5.90692  1.000 74.20995  ? 75  VAL A CG2   1 
ATOM   547  N N     . LEU A 1 72  ? -59.12689 56.15851 -1.60003  1.000 67.37161  ? 76  LEU A N     1 
ATOM   548  C CA    . LEU A 1 72  ? -59.24157 55.66967 -0.22603  1.000 66.64179  ? 76  LEU A CA    1 
ATOM   549  C C     . LEU A 1 72  ? -58.87056 56.72392 0.80903   1.000 74.41054  ? 76  LEU A C     1 
ATOM   550  O O     . LEU A 1 72  ? -59.43523 56.71661 1.90751   1.000 74.50717  ? 76  LEU A O     1 
ATOM   551  C CB    . LEU A 1 72  ? -58.37760 54.42360 -0.03451  1.000 66.31296  ? 76  LEU A CB    1 
ATOM   552  C CG    . LEU A 1 72  ? -58.93625 53.27682 -0.90465  1.000 70.22219  ? 76  LEU A CG    1 
ATOM   553  C CD1   . LEU A 1 72  ? -57.87499 52.24192 -1.08527  1.000 66.04198  ? 76  LEU A CD1   1 
ATOM   554  C CD2   . LEU A 1 72  ? -60.25557 52.64846 -0.41557  1.000 66.84015  ? 76  LEU A CD2   1 
ATOM   555  N N     . MET A 1 73  ? -57.92811 57.62746 0.50433   1.000 70.88146  ? 77  MET A N     1 
ATOM   556  C CA    . MET A 1 73  ? -57.69151 58.73224 1.42757   1.000 71.44795  ? 77  MET A CA    1 
ATOM   557  C C     . MET A 1 73  ? -58.95658 59.55956 1.63888   1.000 69.83005  ? 77  MET A C     1 
ATOM   558  O O     . MET A 1 73  ? -59.17949 60.09642 2.73635   1.000 65.77204  ? 77  MET A O     1 
ATOM   559  C CB    . MET A 1 73  ? -56.55963 59.62049 0.92177   1.000 73.07424  ? 77  MET A CB    1 
ATOM   560  C CG    . MET A 1 73  ? -55.20104 58.95823 0.97935   1.000 76.00618  ? 77  MET A CG    1 
ATOM   561  S SD    . MET A 1 73  ? -54.59450 58.78735 2.65769   1.000 92.79263  ? 77  MET A SD    1 
ATOM   562  C CE    . MET A 1 73  ? -54.85000 60.43189 3.33322   1.000 75.48494  ? 77  MET A CE    1 
ATOM   563  N N     . LYS A 1 74  ? -59.81349 59.65198 0.62155   1.000 72.18597  ? 78  LYS A N     1 
ATOM   564  C CA    . LYS A 1 74  ? -61.04492 60.41452 0.80148   1.000 73.81389  ? 78  LYS A CA    1 
ATOM   565  C C     . LYS A 1 74  ? -62.09309 59.66802 1.61993   1.000 72.66808  ? 78  LYS A C     1 
ATOM   566  O O     . LYS A 1 74  ? -62.93532 60.31755 2.24551   1.000 83.35268  ? 78  LYS A O     1 
ATOM   567  C CB    . LYS A 1 74  ? -61.62493 60.78723 -0.54589  1.000 70.92522  ? 78  LYS A CB    1 
ATOM   568  C CG    . LYS A 1 74  ? -60.75459 61.71362 -1.34387  1.000 77.83491  ? 78  LYS A CG    1 
ATOM   569  C CD    . LYS A 1 74  ? -61.60489 62.33854 -2.43220  1.000 90.68531  ? 78  LYS A CD    1 
ATOM   570  C CE    . LYS A 1 74  ? -60.79739 62.72227 -3.64601  1.000 93.46283  ? 78  LYS A CE    1 
ATOM   571  N NZ    . LYS A 1 74  ? -61.69626 62.88027 -4.83408  1.000 101.95212 ? 78  LYS A NZ    1 
ATOM   572  N N     . CYS A 1 75  ? -62.06240 58.32707 1.63592   1.000 68.23108  ? 79  CYS A N     1 
ATOM   573  C CA    . CYS A 1 75  ? -63.07392 57.54925 2.36002   1.000 75.48247  ? 79  CYS A CA    1 
ATOM   574  C C     . CYS A 1 75  ? -62.75845 57.41177 3.82999   1.000 74.19171  ? 79  CYS A C     1 
ATOM   575  O O     . CYS A 1 75  ? -63.67576 57.39604 4.65813   1.000 76.26749  ? 79  CYS A O     1 
ATOM   576  C CB    . CYS A 1 75  ? -63.20979 56.13400 1.80002   1.000 64.67710  ? 79  CYS A CB    1 
ATOM   577  S SG    . CYS A 1 75  ? -63.43250 56.07080 0.04662   1.000 92.85772  ? 79  CYS A SG    1 
ATOM   578  N N     . VAL A 1 76  ? -61.48025 57.26548 4.16231   1.000 66.67421  ? 80  VAL A N     1 
ATOM   579  C CA    . VAL A 1 76  ? -61.12866 56.81428 5.49102   1.000 68.02095  ? 80  VAL A CA    1 
ATOM   580  C C     . VAL A 1 76  ? -61.42731 57.90516 6.49755   1.000 71.25895  ? 80  VAL A C     1 
ATOM   581  O O     . VAL A 1 76  ? -61.39490 59.10178 6.19237   1.000 74.67415  ? 80  VAL A O     1 
ATOM   582  C CB    . VAL A 1 76  ? -59.65361 56.42058 5.53354   1.000 73.55141  ? 80  VAL A CB    1 
ATOM   583  C CG1   . VAL A 1 76  ? -59.48955 55.13992 4.72252   1.000 64.11824  ? 80  VAL A CG1   1 
ATOM   584  C CG2   . VAL A 1 76  ? -58.81165 57.60464 5.02336   1.000 64.94192  ? 80  VAL A CG2   1 
ATOM   585  N N     . ASN A 1 77  ? -61.78133 57.48208 7.70167   1.000 62.35603  ? 81  ASN A N     1 
ATOM   586  C CA    . ASN A 1 77  ? -62.11913 58.45129 8.72468   1.000 69.22838  ? 81  ASN A CA    1 
ATOM   587  C C     . ASN A 1 77  ? -61.95056 57.72802 10.05920  1.000 64.51643  ? 81  ASN A C     1 
ATOM   588  O O     . ASN A 1 77  ? -62.90390 57.13385 10.56332  1.000 73.24144  ? 81  ASN A O     1 
ATOM   589  C CB    . ASN A 1 77  ? -63.53179 58.94505 8.53397   1.000 78.99343  ? 81  ASN A CB    1 
ATOM   590  C CG    . ASN A 1 77  ? -63.76528 60.24586 9.19689   1.000 84.14633  ? 81  ASN A CG    1 
ATOM   591  O OD1   . ASN A 1 77  ? -63.09860 60.58001 10.18534  1.000 83.97390  ? 81  ASN A OD1   1 
ATOM   592  N ND2   . ASN A 1 77  ? -64.69214 61.01950 8.65340   1.000 91.54434  ? 81  ASN A ND2   1 
ATOM   593  N N     . HIS A 1 78  ? -60.76277 57.83831 10.64311  1.000 60.35539  ? 82  HIS A N     1 
ATOM   594  C CA    . HIS A 1 78  ? -60.53698 57.15332 11.90382  1.000 60.95563  ? 82  HIS A CA    1 
ATOM   595  C C     . HIS A 1 78  ? -59.24132 57.67834 12.51111  1.000 59.61227  ? 82  HIS A C     1 
ATOM   596  O O     . HIS A 1 78  ? -58.28975 57.98380 11.78139  1.000 57.92719  ? 82  HIS A O     1 
ATOM   597  C CB    . HIS A 1 78  ? -60.49268 55.63180 11.68343  1.000 55.39630  ? 82  HIS A CB    1 
ATOM   598  C CG    . HIS A 1 78  ? -60.50435 54.83670 12.95115  1.000 57.95159  ? 82  HIS A CG    1 
ATOM   599  N ND1   . HIS A 1 78  ? -59.35414 54.56054 13.66752  1.000 59.19505  ? 82  HIS A ND1   1 
ATOM   600  C CD2   . HIS A 1 78  ? -61.52405 54.28055 13.64578  1.000 60.93857  ? 82  HIS A CD2   1 
ATOM   601  C CE1   . HIS A 1 78  ? -59.66474 53.86111 14.74437  1.000 64.28183  ? 82  HIS A CE1   1 
ATOM   602  N NE2   . HIS A 1 78  ? -60.97482 53.68046 14.75829  1.000 60.94723  ? 82  HIS A NE2   1 
ATOM   603  N N     . LYS A 1 79  ? -59.21916 57.79349 13.84779  1.000 57.09362  ? 83  LYS A N     1 
ATOM   604  C CA    . LYS A 1 79  ? -58.07408 58.38299 14.53746  1.000 62.57067  ? 83  LYS A CA    1 
ATOM   605  C C     . LYS A 1 79  ? -56.78369 57.60898 14.28714  1.000 63.63311  ? 83  LYS A C     1 
ATOM   606  O O     . LYS A 1 79  ? -55.70688 58.15658 14.50013  1.000 69.99623  ? 83  LYS A O     1 
ATOM   607  C CB    . LYS A 1 79  ? -58.32929 58.43794 16.05237  1.000 63.74327  ? 83  LYS A CB    1 
ATOM   608  C CG    . LYS A 1 79  ? -58.12112 57.07200 16.70354  1.000 70.49010  ? 83  LYS A CG    1 
ATOM   609  C CD    . LYS A 1 79  ? -58.68623 56.90205 18.10938  1.000 70.17748  ? 83  LYS A CD    1 
ATOM   610  C CE    . LYS A 1 79  ? -58.04219 57.79130 19.13990  1.000 77.02829  ? 83  LYS A CE    1 
ATOM   611  N NZ    . LYS A 1 79  ? -58.85246 57.79173 20.39960  1.000 81.44016  ? 83  LYS A NZ    1 
ATOM   612  N N     . ASN A 1 80  ? -56.85992 56.33777 13.88506  1.000 63.22348  ? 84  ASN A N     1 
ATOM   613  C CA    . ASN A 1 80  ? -55.66739 55.53792 13.63099  1.000 57.49227  ? 84  ASN A CA    1 
ATOM   614  C C     . ASN A 1 80  ? -55.45150 55.28337 12.14632  1.000 58.39853  ? 84  ASN A C     1 
ATOM   615  O O     . ASN A 1 80  ? -54.71072 54.36742 11.77493  1.000 61.90956  ? 84  ASN A O     1 
ATOM   616  C CB    . ASN A 1 80  ? -55.71062 54.21814 14.40243  1.000 54.18247  ? 84  ASN A CB    1 
ATOM   617  C CG    . ASN A 1 80  ? -55.66201 54.42621 15.90268  1.000 60.88664  ? 84  ASN A CG    1 
ATOM   618  O OD1   . ASN A 1 80  ? -56.54571 53.98089 16.63749  1.000 66.90528  ? 84  ASN A OD1   1 
ATOM   619  N ND2   . ASN A 1 80  ? -54.62839 55.13773 16.36690  1.000 69.80494  ? 84  ASN A ND2   1 
ATOM   620  N N     . ILE A 1 81  ? -56.06273 56.09525 11.29686  1.000 62.15121  ? 85  ILE A N     1 
ATOM   621  C CA    . ILE A 1 81  ? -55.74369 56.17106 9.87756   1.000 62.74968  ? 85  ILE A CA    1 
ATOM   622  C C     . ILE A 1 81  ? -55.31243 57.60133 9.59166   1.000 64.03741  ? 85  ILE A C     1 
ATOM   623  O O     . ILE A 1 81  ? -55.97248 58.55374 10.03024  1.000 73.45691  ? 85  ILE A O     1 
ATOM   624  C CB    . ILE A 1 81  ? -56.94557 55.77610 8.98838   1.000 59.05581  ? 85  ILE A CB    1 
ATOM   625  C CG1   . ILE A 1 81  ? -57.44601 54.37164 9.34955   1.000 56.50021  ? 85  ILE A CG1   1 
ATOM   626  C CG2   . ILE A 1 81  ? -56.58550 55.90846 7.51039   1.000 58.52442  ? 85  ILE A CG2   1 
ATOM   627  C CD1   . ILE A 1 81  ? -56.48064 53.23884 9.02657   1.000 56.80431  ? 85  ILE A CD1   1 
ATOM   628  N N     . ILE A 1 82  ? -54.21359 57.75207 8.85458   1.000 64.98165  ? 86  ILE A N     1 
ATOM   629  C CA    . ILE A 1 82  ? -53.71557 59.08468 8.54519   1.000 65.84760  ? 86  ILE A CA    1 
ATOM   630  C C     . ILE A 1 82  ? -54.82402 59.91368 7.91538   1.000 68.18496  ? 86  ILE A C     1 
ATOM   631  O O     . ILE A 1 82  ? -55.59777 59.43151 7.07181   1.000 67.83322  ? 86  ILE A O     1 
ATOM   632  C CB    . ILE A 1 82  ? -52.49895 58.98787 7.61544   1.000 57.98400  ? 86  ILE A CB    1 
ATOM   633  C CG1   . ILE A 1 82  ? -51.66214 60.24962 7.72092   1.000 56.31013  ? 86  ILE A CG1   1 
ATOM   634  C CG2   . ILE A 1 82  ? -52.93750 58.70818 6.18654   1.000 65.41166  ? 86  ILE A CG2   1 
ATOM   635  C CD1   . ILE A 1 82  ? -51.06638 60.44256 9.11231   1.000 67.32632  ? 86  ILE A CD1   1 
ATOM   636  N N     . GLY A 1 83  ? -54.93492 61.16400 8.36111   1.000 66.55279  ? 87  GLY A N     1 
ATOM   637  C CA    . GLY A 1 83  ? -56.05446 62.01007 7.98195   1.000 71.84740  ? 87  GLY A CA    1 
ATOM   638  C C     . GLY A 1 83  ? -55.71491 62.84764 6.76771   1.000 69.22368  ? 87  GLY A C     1 
ATOM   639  O O     . GLY A 1 83  ? -54.63734 63.44217 6.69732   1.000 68.66017  ? 87  GLY A O     1 
ATOM   640  N N     . LEU A 1 84  ? -56.62966 62.87611 5.80298   1.000 63.80592  ? 88  LEU A N     1 
ATOM   641  C CA    . LEU A 1 84  ? -56.44589 63.68963 4.61288   1.000 65.28544  ? 88  LEU A CA    1 
ATOM   642  C C     . LEU A 1 84  ? -56.81597 65.14189 4.91752   1.000 72.24675  ? 88  LEU A C     1 
ATOM   643  O O     . LEU A 1 84  ? -57.74142 65.40552 5.69642   1.000 74.43039  ? 88  LEU A O     1 
ATOM   644  C CB    . LEU A 1 84  ? -57.30051 63.14706 3.46285   1.000 60.95103  ? 88  LEU A CB    1 
ATOM   645  C CG    . LEU A 1 84  ? -57.10645 63.88286 2.13667   1.000 70.38032  ? 88  LEU A CG    1 
ATOM   646  C CD1   . LEU A 1 84  ? -55.72576 63.58200 1.58968   1.000 69.38042  ? 88  LEU A CD1   1 
ATOM   647  C CD2   . LEU A 1 84  ? -58.16814 63.47648 1.13915   1.000 69.22233  ? 88  LEU A CD2   1 
ATOM   648  N N     . LEU A 1 85  ? -56.06510 66.08441 4.32354   1.000 63.68327  ? 89  LEU A N     1 
ATOM   649  C CA    . LEU A 1 85  ? -56.24929 67.51651 4.54028   1.000 69.23577  ? 89  LEU A CA    1 
ATOM   650  C C     . LEU A 1 85  ? -56.47399 68.30117 3.25809   1.000 66.50240  ? 89  LEU A C     1 
ATOM   651  O O     . LEU A 1 85  ? -57.25844 69.25240 3.25806   1.000 76.67858  ? 89  LEU A O     1 
ATOM   652  C CB    . LEU A 1 85  ? -55.03684 68.11917 5.24985   1.000 71.11832  ? 89  LEU A CB    1 
ATOM   653  C CG    . LEU A 1 85  ? -54.93335 67.93035 6.76134   1.000 71.69255  ? 89  LEU A CG    1 
ATOM   654  C CD1   . LEU A 1 85  ? -53.73423 68.72735 7.29587   1.000 69.15410  ? 89  LEU A CD1   1 
ATOM   655  C CD2   . LEU A 1 85  ? -56.20480 68.31005 7.44025   1.000 60.45277  ? 89  LEU A CD2   1 
ATOM   656  N N     . ASN A 1 86  ? -55.79339 67.95292 2.16740   1.000 64.05961  ? 90  ASN A N     1 
ATOM   657  C CA    . ASN A 1 86  ? -55.94868 68.70495 0.92734   1.000 69.39952  ? 90  ASN A CA    1 
ATOM   658  C C     . ASN A 1 86  ? -55.38501 67.89642 -0.22580  1.000 62.57512  ? 90  ASN A C     1 
ATOM   659  O O     . ASN A 1 86  ? -54.41910 67.15273 -0.06107  1.000 73.62274  ? 90  ASN A O     1 
ATOM   660  C CB    . ASN A 1 86  ? -55.24349 70.07655 0.96298   1.000 66.76825  ? 90  ASN A CB    1 
ATOM   661  C CG    . ASN A 1 86  ? -55.75484 71.00955 -0.12726  1.000 73.58986  ? 90  ASN A CG    1 
ATOM   662  O OD1   . ASN A 1 86  ? -56.72176 70.67612 -0.82038  1.000 72.70823  ? 90  ASN A OD1   1 
ATOM   663  N ND2   . ASN A 1 86  ? -55.11612 72.18325 -0.28376  1.000 71.10068  ? 90  ASN A ND2   1 
ATOM   664  N N     . VAL A 1 87  ? -55.98248 68.07550 -1.39873  1.000 60.89221  ? 91  VAL A N     1 
ATOM   665  C CA    . VAL A 1 87  ? -55.50418 67.48336 -2.64001  1.000 65.00957  ? 91  VAL A CA    1 
ATOM   666  C C     . VAL A 1 87  ? -55.49764 68.58203 -3.68833  1.000 70.89598  ? 91  VAL A C     1 
ATOM   667  O O     . VAL A 1 87  ? -56.49690 69.28879 -3.85761  1.000 80.12851  ? 91  VAL A O     1 
ATOM   668  C CB    . VAL A 1 87  ? -56.38529 66.30758 -3.11187  1.000 69.35361  ? 91  VAL A CB    1 
ATOM   669  C CG1   . VAL A 1 87  ? -55.74177 65.58174 -4.30701  1.000 70.28808  ? 91  VAL A CG1   1 
ATOM   670  C CG2   . VAL A 1 87  ? -56.64347 65.33358 -1.97896  1.000 68.76262  ? 91  VAL A CG2   1 
ATOM   671  N N     . PHE A 1 88  ? -54.38553 68.72021 -4.39996  1.000 67.26897  ? 92  PHE A N     1 
ATOM   672  C CA    . PHE A 1 88  ? -54.31903 69.74235 -5.42764  1.000 69.50718  ? 92  PHE A CA    1 
ATOM   673  C C     . PHE A 1 88  ? -53.28551 69.34172 -6.47056  1.000 78.56503  ? 92  PHE A C     1 
ATOM   674  O O     . PHE A 1 88  ? -52.45212 68.45588 -6.24551  1.000 75.66406  ? 92  PHE A O     1 
ATOM   675  C CB    . PHE A 1 88  ? -54.01311 71.11792 -4.81638  1.000 67.82750  ? 92  PHE A CB    1 
ATOM   676  C CG    . PHE A 1 88  ? -52.62376 71.24916 -4.20438  1.000 70.02137  ? 92  PHE A CG    1 
ATOM   677  C CD1   . PHE A 1 88  ? -51.52114 71.61350 -4.98674  1.000 75.19537  ? 92  PHE A CD1   1 
ATOM   678  C CD2   . PHE A 1 88  ? -52.42797 71.05452 -2.83761  1.000 68.18995  ? 92  PHE A CD2   1 
ATOM   679  C CE1   . PHE A 1 88  ? -50.23447 71.75989 -4.42113  1.000 71.55947  ? 92  PHE A CE1   1 
ATOM   680  C CE2   . PHE A 1 88  ? -51.13954 71.20051 -2.26079  1.000 67.84243  ? 92  PHE A CE2   1 
ATOM   681  C CZ    . PHE A 1 88  ? -50.05106 71.55374 -3.06020  1.000 69.74239  ? 92  PHE A CZ    1 
ATOM   682  N N     . THR A 1 89  ? -53.37069 70.00410 -7.62588  1.000 79.33618  ? 93  THR A N     1 
ATOM   683  C CA    . THR A 1 89  ? -52.38938 69.91839 -8.68879  1.000 76.18561  ? 93  THR A CA    1 
ATOM   684  C C     . THR A 1 89  ? -52.09308 71.31914 -9.20137  1.000 85.85027  ? 93  THR A C     1 
ATOM   685  O O     . THR A 1 89  ? -53.01588 72.13581 -9.33341  1.000 87.22700  ? 93  THR A O     1 
ATOM   686  C CB    . THR A 1 89  ? -52.89478 69.04570 -9.84452  1.000 85.34455  ? 93  THR A CB    1 
ATOM   687  O OG1   . THR A 1 89  ? -52.01743 69.19333 -10.97250 1.000 86.47620  ? 93  THR A OG1   1 
ATOM   688  C CG2   . THR A 1 89  ? -54.33502 69.42401 -10.23043 1.000 83.48040  ? 93  THR A CG2   1 
ATOM   689  N N     . PRO A 1 90  ? -50.82406 71.63122 -9.50220  1.000 92.82752  ? 94  PRO A N     1 
ATOM   690  C CA    . PRO A 1 90  ? -50.50426 72.98937 -9.98631  1.000 87.61015  ? 94  PRO A CA    1 
ATOM   691  C C     . PRO A 1 90  ? -50.96386 73.26439 -11.41826 1.000 94.39357  ? 94  PRO A C     1 
ATOM   692  O O     . PRO A 1 90  ? -51.24364 74.42415 -11.75075 1.000 104.72408 ? 94  PRO A O     1 
ATOM   693  C CB    . PRO A 1 90  ? -48.97795 73.05886 -9.83872  1.000 83.37332  ? 94  PRO A CB    1 
ATOM   694  C CG    . PRO A 1 90  ? -48.52153 71.62667 -9.90066  1.000 86.32426  ? 94  PRO A CG    1 
ATOM   695  C CD    . PRO A 1 90  ? -49.61421 70.82614 -9.24700  1.000 82.54243  ? 94  PRO A CD    1 
ATOM   696  N N     . GLN A 1 91  ? -51.07408 72.24395 -12.26871 1.000 96.05610  ? 95  GLN A N     1 
ATOM   697  C CA    . GLN A 1 91  ? -51.52110 72.43505 -13.64738 1.000 99.61249  ? 95  GLN A CA    1 
ATOM   698  C C     . GLN A 1 91  ? -53.01119 72.78062 -13.70795 1.000 102.95889 ? 95  GLN A C     1 
ATOM   699  O O     . GLN A 1 91  ? -53.81490 72.31329 -12.89677 1.000 99.99092  ? 95  GLN A O     1 
ATOM   700  C CB    . GLN A 1 91  ? -51.22376 71.17453 -14.46684 1.000 93.41848  ? 95  GLN A CB    1 
ATOM   701  C CG    . GLN A 1 91  ? -49.72679 70.85515 -14.54354 1.000 93.48269  ? 95  GLN A CG    1 
ATOM   702  C CD    . GLN A 1 91  ? -49.20102 70.06017 -13.35020 1.000 96.14172  ? 95  GLN A CD    1 
ATOM   703  O OE1   . GLN A 1 91  ? -49.94981 69.34965 -12.67018 1.000 95.79551  ? 95  GLN A OE1   1 
ATOM   704  N NE2   . GLN A 1 91  ? -47.90144 70.17493 -13.09612 1.000 93.66727  ? 95  GLN A NE2   1 
ATOM   705  N N     . LYS A 1 92  ? -53.38281 73.60563 -14.69251 1.000 108.39323 ? 96  LYS A N     1 
ATOM   706  C CA    . LYS A 1 92  ? -54.71437 74.20230 -14.71529 1.000 110.01701 ? 96  LYS A CA    1 
ATOM   707  C C     . LYS A 1 92  ? -55.71227 73.47177 -15.61651 1.000 111.18830 ? 96  LYS A C     1 
ATOM   708  O O     . LYS A 1 92  ? -56.91443 73.76169 -15.54325 1.000 102.52956 ? 96  LYS A O     1 
ATOM   709  C CB    . LYS A 1 92  ? -54.61801 75.67348 -15.14501 1.000 111.26567 ? 96  LYS A CB    1 
ATOM   710  C CG    . LYS A 1 92  ? -54.76275 76.68551 -13.99951 1.000 126.07560 ? 96  LYS A CG    1 
ATOM   711  C CD    . LYS A 1 92  ? -56.20483 76.74439 -13.47229 1.000 132.09466 ? 96  LYS A CD    1 
ATOM   712  C CE    . LYS A 1 92  ? -56.51236 78.08097 -12.77947 1.000 128.89981 ? 96  LYS A CE    1 
ATOM   713  N NZ    . LYS A 1 92  ? -57.27991 77.95336 -11.49928 1.000 125.88056 ? 96  LYS A NZ    1 
ATOM   714  N N     . SER A 1 93  ? -55.26359 72.52937 -16.44791 1.000 111.25139 ? 97  SER A N     1 
ATOM   715  C CA    . SER A 1 93  ? -56.15195 71.84185 -17.37938 1.000 109.38004 ? 97  SER A CA    1 
ATOM   716  C C     . SER A 1 93  ? -55.79471 70.36158 -17.44003 1.000 103.62127 ? 97  SER A C     1 
ATOM   717  O O     . SER A 1 93  ? -54.80717 69.91045 -16.85334 1.000 102.66662 ? 97  SER A O     1 
ATOM   718  C CB    . SER A 1 93  ? -56.08402 72.46358 -18.78350 1.000 111.74735 ? 97  SER A CB    1 
ATOM   719  O OG    . SER A 1 93  ? -54.87678 72.11549 -19.44284 1.000 117.01382 ? 97  SER A OG    1 
ATOM   720  N N     . LEU A 1 94  ? -56.61419 69.60037 -18.16838 1.000 102.40006 ? 98  LEU A N     1 
ATOM   721  C CA    . LEU A 1 94  ? -56.34187 68.17373 -18.32368 1.000 102.29275 ? 98  LEU A CA    1 
ATOM   722  C C     . LEU A 1 94  ? -55.11828 67.93552 -19.20174 1.000 108.36605 ? 98  LEU A C     1 
ATOM   723  O O     . LEU A 1 94  ? -54.31929 67.02928 -18.92588 1.000 106.06278 ? 98  LEU A O     1 
ATOM   724  C CB    . LEU A 1 94  ? -57.56243 67.45733 -18.90295 1.000 93.18473  ? 98  LEU A CB    1 
ATOM   725  C CG    . LEU A 1 94  ? -57.75904 65.94050 -18.71007 1.000 101.69880 ? 98  LEU A CG    1 
ATOM   726  C CD1   . LEU A 1 94  ? -58.98689 65.47422 -19.49372 1.000 101.70264 ? 98  LEU A CD1   1 
ATOM   727  C CD2   . LEU A 1 94  ? -56.55676 65.06094 -19.08483 1.000 100.22992 ? 98  LEU A CD2   1 
ATOM   728  N N     . GLU A 1 95  ? -54.95873 68.71746 -20.27527 1.000 107.84815 ? 99  GLU A N     1 
ATOM   729  C CA    . GLU A 1 95  ? -53.81089 68.50058 -21.15397 1.000 112.23938 ? 99  GLU A CA    1 
ATOM   730  C C     . GLU A 1 95  ? -52.50355 68.73334 -20.40436 1.000 113.96795 ? 99  GLU A C     1 
ATOM   731  O O     . GLU A 1 95  ? -51.55249 67.94910 -20.52849 1.000 115.39081 ? 99  GLU A O     1 
ATOM   732  C CB    . GLU A 1 95  ? -53.90005 69.40453 -22.38857 1.000 119.47384 ? 99  GLU A CB    1 
ATOM   733  C CG    . GLU A 1 95  ? -52.91832 69.05689 -23.53226 1.000 127.50402 ? 99  GLU A CG    1 
ATOM   734  C CD    . GLU A 1 95  ? -53.54692 68.23552 -24.66336 1.000 130.06037 ? 99  GLU A CD    1 
ATOM   735  O OE1   . GLU A 1 95  ? -53.72492 67.00535 -24.49574 1.000 129.87151 ? 99  GLU A OE1   1 
ATOM   736  O OE2   . GLU A 1 95  ? -53.86074 68.82786 -25.72642 1.000 129.28028 ? 99  GLU A OE2   1 
ATOM   737  N N     . GLU A 1 96  ? -52.45652 69.78120 -19.58409 1.000 113.33647 ? 100 GLU A N     1 
ATOM   738  C CA    . GLU A 1 96  ? -51.23381 70.16998 -18.90088 1.000 112.92697 ? 100 GLU A CA    1 
ATOM   739  C C     . GLU A 1 96  ? -50.95165 69.33599 -17.65725 1.000 102.53782 ? 100 GLU A C     1 
ATOM   740  O O     . GLU A 1 96  ? -49.86430 69.46736 -17.08517 1.000 100.73590 ? 100 GLU A O     1 
ATOM   741  C CB    . GLU A 1 96  ? -51.30868 71.65141 -18.52293 1.000 116.00744 ? 100 GLU A CB    1 
ATOM   742  C CG    . GLU A 1 96  ? -51.46417 72.60130 -19.70576 1.000 120.10611 ? 100 GLU A CG    1 
ATOM   743  C CD    . GLU A 1 96  ? -50.47123 73.75088 -19.65504 1.000 140.84571 ? 100 GLU A CD    1 
ATOM   744  O OE1   . GLU A 1 96  ? -49.37167 73.62652 -20.24069 1.000 148.30249 ? 100 GLU A OE1   1 
ATOM   745  O OE2   . GLU A 1 96  ? -50.78143 74.77623 -19.00908 1.000 145.64546 ? 100 GLU A OE2   1 
ATOM   746  N N     . PHE A 1 97  ? -51.88441 68.48111 -17.24726 1.000 96.29255  ? 101 PHE A N     1 
ATOM   747  C CA    . PHE A 1 97  ? -51.80020 67.79325 -15.95867 1.000 99.62672  ? 101 PHE A CA    1 
ATOM   748  C C     . PHE A 1 97  ? -50.53312 66.93931 -15.83991 1.000 98.40542  ? 101 PHE A C     1 
ATOM   749  O O     . PHE A 1 97  ? -50.23451 66.12202 -16.71646 1.000 103.96755 ? 101 PHE A O     1 
ATOM   750  C CB    . PHE A 1 97  ? -53.06316 66.93598 -15.78285 1.000 97.95239  ? 101 PHE A CB    1 
ATOM   751  C CG    . PHE A 1 97  ? -53.07583 66.08808 -14.54448 1.000 93.72384  ? 101 PHE A CG    1 
ATOM   752  C CD1   . PHE A 1 97  ? -52.90715 66.65779 -13.28169 1.000 88.02872  ? 101 PHE A CD1   1 
ATOM   753  C CD2   . PHE A 1 97  ? -53.27870 64.71198 -14.64778 1.000 90.98328  ? 101 PHE A CD2   1 
ATOM   754  C CE1   . PHE A 1 97  ? -52.92279 65.86541 -12.14514 1.000 81.36195  ? 101 PHE A CE1   1 
ATOM   755  C CE2   . PHE A 1 97  ? -53.29552 63.90722 -13.52331 1.000 82.02986  ? 101 PHE A CE2   1 
ATOM   756  C CZ    . PHE A 1 97  ? -53.11967 64.47818 -12.27238 1.000 84.05756  ? 101 PHE A CZ    1 
ATOM   757  N N     . GLN A 1 98  ? -49.75923 67.15979 -14.76960 1.000 95.07616  ? 102 GLN A N     1 
ATOM   758  C CA    . GLN A 1 98  ? -48.57739 66.33610 -14.51205 1.000 92.66422  ? 102 GLN A CA    1 
ATOM   759  C C     . GLN A 1 98  ? -48.53844 65.69240 -13.13006 1.000 90.22988  ? 102 GLN A C     1 
ATOM   760  O O     . GLN A 1 98  ? -48.32918 64.48115 -13.01468 1.000 92.56268  ? 102 GLN A O     1 
ATOM   761  C CB    . GLN A 1 98  ? -47.30527 67.16190 -14.69084 1.000 95.56204  ? 102 GLN A CB    1 
ATOM   762  C CG    . GLN A 1 98  ? -47.06306 67.62793 -16.11367 1.000 106.85270 ? 102 GLN A CG    1 
ATOM   763  C CD    . GLN A 1 98  ? -46.77229 66.48369 -17.07083 1.000 113.10201 ? 102 GLN A CD    1 
ATOM   764  O OE1   . GLN A 1 98  ? -45.63513 66.01065 -17.16724 1.000 116.93637 ? 102 GLN A OE1   1 
ATOM   765  N NE2   . GLN A 1 98  ? -47.80032 66.03855 -17.79259 1.000 110.57254 ? 102 GLN A NE2   1 
ATOM   766  N N     . ASP A 1 99  ? -48.72977 66.48935 -12.07440 1.000 88.77920  ? 103 ASP A N     1 
ATOM   767  C CA    . ASP A 1 99  ? -48.40546 66.07682 -10.71222 1.000 84.38176  ? 103 ASP A CA    1 
ATOM   768  C C     . ASP A 1 99  ? -49.61826 66.23972 -9.81051  1.000 77.38624  ? 103 ASP A C     1 
ATOM   769  O O     . ASP A 1 99  ? -50.40748 67.17304 -9.96734  1.000 81.39222  ? 103 ASP A O     1 
ATOM   770  C CB    . ASP A 1 99  ? -47.24401 66.91050 -10.09243 1.000 76.02772  ? 103 ASP A CB    1 
ATOM   771  C CG    . ASP A 1 99  ? -46.07673 67.10366 -11.04425 1.000 92.86117  ? 103 ASP A CG    1 
ATOM   772  O OD1   . ASP A 1 99  ? -45.73639 66.12983 -11.75848 1.000 95.23533  ? 103 ASP A OD1   1 
ATOM   773  O OD2   . ASP A 1 99  ? -45.49709 68.22956 -11.06762 1.000 89.50528  ? 103 ASP A OD2   1 
ATOM   774  N N     . VAL A 1 100 ? -49.72175 65.35263 -8.83035  1.000 74.19658  ? 104 VAL A N     1 
ATOM   775  C CA    . VAL A 1 100 ? -50.73954 65.40339 -7.78979  1.000 73.71126  ? 104 VAL A CA    1 
ATOM   776  C C     . VAL A 1 100 ? -50.01735 65.60366 -6.47187  1.000 73.91908  ? 104 VAL A C     1 
ATOM   777  O O     . VAL A 1 100 ? -48.93218 65.04991 -6.26566  1.000 79.11875  ? 104 VAL A O     1 
ATOM   778  C CB    . VAL A 1 100 ? -51.59628 64.11513 -7.76135  1.000 75.04011  ? 104 VAL A CB    1 
ATOM   779  C CG1   . VAL A 1 100 ? -52.69211 64.19194 -6.71244  1.000 73.26489  ? 104 VAL A CG1   1 
ATOM   780  C CG2   . VAL A 1 100 ? -52.20316 63.86494 -9.10718  1.000 72.17505  ? 104 VAL A CG2   1 
ATOM   781  N N     . TYR A 1 101 ? -50.59600 66.41641 -5.59683  1.000 75.64804  ? 105 TYR A N     1 
ATOM   782  C CA    . TYR A 1 101 ? -50.02453 66.66936 -4.28023  1.000 73.58270  ? 105 TYR A CA    1 
ATOM   783  C C     . TYR A 1 101 ? -51.08050 66.32030 -3.24194  1.000 74.51403  ? 105 TYR A C     1 
ATOM   784  O O     . TYR A 1 101 ? -52.21324 66.81175 -3.31872  1.000 70.62834  ? 105 TYR A O     1 
ATOM   785  C CB    . TYR A 1 101 ? -49.55419 68.12761 -4.14408  1.000 70.90567  ? 105 TYR A CB    1 
ATOM   786  C CG    . TYR A 1 101 ? -48.36222 68.52852 -5.03837  1.000 78.13478  ? 105 TYR A CG    1 
ATOM   787  C CD1   . TYR A 1 101 ? -48.55176 68.83273 -6.38552  1.000 72.74203  ? 105 TYR A CD1   1 
ATOM   788  C CD2   . TYR A 1 101 ? -47.05348 68.62697 -4.52808  1.000 79.10817  ? 105 TYR A CD2   1 
ATOM   789  C CE1   . TYR A 1 101 ? -47.48144 69.20498 -7.20805  1.000 74.97698  ? 105 TYR A CE1   1 
ATOM   790  C CE2   . TYR A 1 101 ? -45.96542 69.00324 -5.35911  1.000 67.16963  ? 105 TYR A CE2   1 
ATOM   791  C CZ    . TYR A 1 101 ? -46.19979 69.28620 -6.69813  1.000 78.46967  ? 105 TYR A CZ    1 
ATOM   792  O OH    . TYR A 1 101 ? -45.17455 69.66620 -7.55033  1.000 83.18744  ? 105 TYR A OH    1 
ATOM   793  N N     . ILE A 1 102 ? -50.71372 65.44595 -2.30174  1.000 73.77412  ? 106 ILE A N     1 
ATOM   794  C CA    . ILE A 1 102 ? -51.56554 65.00315 -1.19840  1.000 66.07759  ? 106 ILE A CA    1 
ATOM   795  C C     . ILE A 1 102 ? -51.05505 65.63979 0.08846   1.000 67.34561  ? 106 ILE A C     1 
ATOM   796  O O     . ILE A 1 102 ? -49.87529 65.48497 0.42789   1.000 63.21546  ? 106 ILE A O     1 
ATOM   797  C CB    . ILE A 1 102 ? -51.54089 63.47272 -1.05412  1.000 68.30467  ? 106 ILE A CB    1 
ATOM   798  C CG1   . ILE A 1 102 ? -51.62893 62.79239 -2.40579  1.000 66.68616  ? 106 ILE A CG1   1 
ATOM   799  C CG2   . ILE A 1 102 ? -52.66457 63.02585 -0.17996  1.000 72.08981  ? 106 ILE A CG2   1 
ATOM   800  C CD1   . ILE A 1 102 ? -52.86899 63.13046 -3.07499  1.000 72.37839  ? 106 ILE A CD1   1 
ATOM   801  N N     . VAL A 1 103 ? -51.93727 66.31801 0.82193   1.000 66.29206  ? 107 VAL A N     1 
ATOM   802  C CA    . VAL A 1 103 ? -51.58525 66.98330 2.07651   1.000 63.62944  ? 107 VAL A CA    1 
ATOM   803  C C     . VAL A 1 103 ? -52.27984 66.26008 3.22982   1.000 63.89621  ? 107 VAL A C     1 
ATOM   804  O O     . VAL A 1 103 ? -53.50819 66.09952 3.21722   1.000 70.91035  ? 107 VAL A O     1 
ATOM   805  C CB    . VAL A 1 103 ? -51.96580 68.47733 2.05684   1.000 68.79070  ? 107 VAL A CB    1 
ATOM   806  C CG1   . VAL A 1 103 ? -51.49288 69.14388 3.34017   1.000 60.62151  ? 107 VAL A CG1   1 
ATOM   807  C CG2   . VAL A 1 103 ? -51.37964 69.21180 0.82027   1.000 66.44641  ? 107 VAL A CG2   1 
ATOM   808  N N     . MET A 1 104 ? -51.50106 65.85638 4.24018   1.000 63.91901  ? 108 MET A N     1 
ATOM   809  C CA    . MET A 1 104 ? -51.95185 65.01368 5.34808   1.000 66.49699  ? 108 MET A CA    1 
ATOM   810  C C     . MET A 1 104 ? -51.49177 65.60432 6.66804   1.000 62.16354  ? 108 MET A C     1 
ATOM   811  O O     . MET A 1 104 ? -50.53100 66.36933 6.71040   1.000 73.49806  ? 108 MET A O     1 
ATOM   812  C CB    . MET A 1 104 ? -51.36789 63.59350 5.28755   1.000 65.69796  ? 108 MET A CB    1 
ATOM   813  C CG    . MET A 1 104 ? -51.49603 62.87782 3.96428   1.000 68.52292  ? 108 MET A CG    1 
ATOM   814  S SD    . MET A 1 104 ? -50.33060 61.47550 3.85035   1.000 73.17778  ? 108 MET A SD    1 
ATOM   815  C CE    . MET A 1 104 ? -48.86579 62.30227 3.17519   1.000 69.03773  ? 108 MET A CE    1 
ATOM   816  N N     . GLU A 1 105 ? -52.13487 65.18706 7.76358   1.000 64.24284  ? 109 GLU A N     1 
ATOM   817  C CA    . GLU A 1 105 ? -51.61475 65.55109 9.07715   1.000 69.54298  ? 109 GLU A CA    1 
ATOM   818  C C     . GLU A 1 105 ? -50.20466 64.97548 9.25004   1.000 68.57081  ? 109 GLU A C     1 
ATOM   819  O O     . GLU A 1 105 ? -49.86332 63.93462 8.67661   1.000 65.21941  ? 109 GLU A O     1 
ATOM   820  C CB    . GLU A 1 105 ? -52.55961 65.06240 10.19695  1.000 62.72892  ? 109 GLU A CB    1 
ATOM   821  C CG    . GLU A 1 105 ? -52.71182 63.54569 10.35118  1.000 79.61846  ? 109 GLU A CG    1 
ATOM   822  C CD    . GLU A 1 105 ? -53.88041 63.11619 11.27740  1.000 90.65374  ? 109 GLU A CD    1 
ATOM   823  O OE1   . GLU A 1 105 ? -53.92507 63.55603 12.45125  1.000 98.06650  ? 109 GLU A OE1   1 
ATOM   824  O OE2   . GLU A 1 105 ? -54.74119 62.31640 10.83689  1.000 84.16310  ? 109 GLU A OE2   1 
ATOM   825  N N     . LEU A 1 106 ? -49.36237 65.68608 10.00349  1.000 72.84603  ? 110 LEU A N     1 
ATOM   826  C CA    . LEU A 1 106 ? -47.94363 65.34888 10.13272  1.000 70.26397  ? 110 LEU A CA    1 
ATOM   827  C C     . LEU A 1 106 ? -47.69868 64.48833 11.36932  1.000 65.99321  ? 110 LEU A C     1 
ATOM   828  O O     . LEU A 1 106 ? -48.08139 64.86471 12.48357  1.000 77.20626  ? 110 LEU A O     1 
ATOM   829  C CB    . LEU A 1 106 ? -47.08507 66.61655 10.21397  1.000 66.76474  ? 110 LEU A CB    1 
ATOM   830  C CG    . LEU A 1 106 ? -45.57757 66.35954 10.40340  1.000 66.19049  ? 110 LEU A CG    1 
ATOM   831  C CD1   . LEU A 1 106 ? -45.07636 65.51243 9.26105   1.000 56.50802  ? 110 LEU A CD1   1 
ATOM   832  C CD2   . LEU A 1 106 ? -44.74079 67.65464 10.46413  1.000 67.39708  ? 110 LEU A CD2   1 
ATOM   833  N N     . MET A 1 107 ? -47.03617 63.35183 11.18507  1.000 62.91519  ? 111 MET A N     1 
ATOM   834  C CA    . MET A 1 107 ? -46.65208 62.49994 12.30634  1.000 66.79804  ? 111 MET A CA    1 
ATOM   835  C C     . MET A 1 107 ? -45.14400 62.57850 12.51526  1.000 73.94193  ? 111 MET A C     1 
ATOM   836  O O     . MET A 1 107 ? -44.39822 63.01533 11.63047  1.000 73.54916  ? 111 MET A O     1 
ATOM   837  C CB    . MET A 1 107 ? -47.09968 61.04707 12.08024  1.000 61.26321  ? 111 MET A CB    1 
ATOM   838  C CG    . MET A 1 107 ? -48.60374 60.88971 11.93614  1.000 64.88723  ? 111 MET A CG    1 
ATOM   839  S SD    . MET A 1 107 ? -49.51623 61.35383 13.44436  1.000 74.44524  ? 111 MET A SD    1 
ATOM   840  C CE    . MET A 1 107 ? -49.06216 60.06655 14.63628  1.000 59.24368  ? 111 MET A CE    1 
ATOM   841  N N     . ASP A 1 108 ? -44.69011 62.16553 13.70429  1.000 67.59929  ? 112 ASP A N     1 
ATOM   842  C CA    . ASP A 1 108 ? -43.30129 62.45449 14.04841  1.000 62.32084  ? 112 ASP A CA    1 
ATOM   843  C C     . ASP A 1 108 ? -42.31588 61.46995 13.42452  1.000 70.89839  ? 112 ASP A C     1 
ATOM   844  O O     . ASP A 1 108 ? -41.18334 61.84909 13.12141  1.000 79.62266  ? 112 ASP A O     1 
ATOM   845  C CB    . ASP A 1 108 ? -43.09573 62.46523 15.56182  1.000 66.92302  ? 112 ASP A CB    1 
ATOM   846  C CG    . ASP A 1 108 ? -43.78658 63.62841 16.24651  1.000 75.72445  ? 112 ASP A CG    1 
ATOM   847  O OD1   . ASP A 1 108 ? -43.88988 63.57779 17.50050  1.000 73.60956  ? 112 ASP A OD1   1 
ATOM   848  O OD2   . ASP A 1 108 ? -44.26346 64.55992 15.53235  1.000 80.30915  ? 112 ASP A OD2   1 
ATOM   849  N N     . ALA A 1 109 ? -42.68261 60.20107 13.27657  1.000 73.52302  ? 113 ALA A N     1 
ATOM   850  C CA    . ALA A 1 109 ? -41.73298 59.22063 12.75504  1.000 68.99120  ? 113 ALA A CA    1 
ATOM   851  C C     . ALA A 1 109 ? -42.49386 58.00689 12.26028  1.000 66.33462  ? 113 ALA A C     1 
ATOM   852  O O     . ALA A 1 109 ? -43.60852 57.73040 12.71675  1.000 61.09047  ? 113 ALA A O     1 
ATOM   853  C CB    . ALA A 1 109 ? -40.72989 58.77967 13.81625  1.000 67.05717  ? 113 ALA A CB    1 
ATOM   854  N N     . ASN A 1 110 ? -41.86303 57.25161 11.36647  1.000 64.89557  ? 114 ASN A N     1 
ATOM   855  C CA    . ASN A 1 110 ? -42.43495 55.95406 11.05996  1.000 63.88042  ? 114 ASN A CA    1 
ATOM   856  C C     . ASN A 1 110 ? -41.91928 54.90458 12.05497  1.000 65.66564  ? 114 ASN A C     1 
ATOM   857  O O     . ASN A 1 110 ? -40.99879 55.15097 12.83331  1.000 73.81766  ? 114 ASN A O     1 
ATOM   858  C CB    . ASN A 1 110 ? -42.19324 55.59323 9.58596   1.000 66.77141  ? 114 ASN A CB    1 
ATOM   859  C CG    . ASN A 1 110 ? -40.79008 55.10390 9.29525   1.000 65.94544  ? 114 ASN A CG    1 
ATOM   860  O OD1   . ASN A 1 110 ? -40.18070 54.37093 10.07349  1.000 63.63074  ? 114 ASN A OD1   1 
ATOM   861  N ND2   . ASN A 1 110 ? -40.28345 55.48712 8.12428   1.000 65.71954  ? 114 ASN A ND2   1 
ATOM   862  N N     . LEU A 1 111 ? -42.54638 53.71885 12.03436  1.000 64.48187  ? 115 LEU A N     1 
ATOM   863  C CA    . LEU A 1 111 ? -42.33620 52.69855 13.05862  1.000 67.73709  ? 115 LEU A CA    1 
ATOM   864  C C     . LEU A 1 111 ? -40.92732 52.08929 13.05512  1.000 74.47108  ? 115 LEU A C     1 
ATOM   865  O O     . LEU A 1 111 ? -40.57086 51.41255 14.02811  1.000 74.62580  ? 115 LEU A O     1 
ATOM   866  C CB    . LEU A 1 111 ? -43.37584 51.59665 12.87309  1.000 65.72895  ? 115 LEU A CB    1 
ATOM   867  C CG    . LEU A 1 111 ? -43.68390 50.72211 14.08414  1.000 72.21809  ? 115 LEU A CG    1 
ATOM   868  C CD1   . LEU A 1 111 ? -44.14687 51.61338 15.21240  1.000 68.72836  ? 115 LEU A CD1   1 
ATOM   869  C CD2   . LEU A 1 111 ? -44.77341 49.72248 13.73204  1.000 68.19845  ? 115 LEU A CD2   1 
ATOM   870  N N     . CYS A 1 112 ? -40.12088 52.30307 12.00539  1.000 66.14605  ? 116 CYS A N     1 
ATOM   871  C CA    . CYS A 1 112 ? -38.77213 51.74479 11.99233  1.000 81.41987  ? 116 CYS A CA    1 
ATOM   872  C C     . CYS A 1 112 ? -37.93352 52.28531 13.14064  1.000 84.79862  ? 116 CYS A C     1 
ATOM   873  O O     . CYS A 1 112 ? -37.00637 51.61783 13.60141  1.000 93.45739  ? 116 CYS A O     1 
ATOM   874  C CB    . CYS A 1 112 ? -38.06800 52.05563 10.66885  1.000 80.04731  ? 116 CYS A CB    1 
ATOM   875  S SG    . CYS A 1 112 ? -38.81686 51.31457 9.19406   1.000 82.22762  ? 116 CYS A SG    1 
ATOM   876  N N     . GLN A 1 113 ? -38.22103 53.49639 13.59559  1.000 82.80676  ? 117 GLN A N     1 
ATOM   877  C CA    . GLN A 1 113 ? -37.42555 54.06492 14.67218  1.000 97.01594  ? 117 GLN A CA    1 
ATOM   878  C C     . GLN A 1 113 ? -37.70632 53.36246 15.99093  1.000 88.73406  ? 117 GLN A C     1 
ATOM   879  O O     . GLN A 1 113 ? -36.78191 53.05942 16.75402  1.000 93.61841  ? 117 GLN A O     1 
ATOM   880  C CB    . GLN A 1 113 ? -37.70810 55.56426 14.78847  1.000 98.94757  ? 117 GLN A CB    1 
ATOM   881  C CG    . GLN A 1 113 ? -37.17240 56.40233 13.62503  1.000 105.39731 ? 117 GLN A CG    1 
ATOM   882  C CD    . GLN A 1 113 ? -37.42808 57.89287 13.82998  1.000 111.49126 ? 117 GLN A CD    1 
ATOM   883  O OE1   . GLN A 1 113 ? -37.29266 58.39735 14.94912  1.000 102.61071 ? 117 GLN A OE1   1 
ATOM   884  N NE2   . GLN A 1 113 ? -37.75202 58.61244 12.74522  1.000 103.77007 ? 117 GLN A NE2   1 
ATOM   885  N N     . VAL A 1 114 ? -38.98304 53.11026 16.27005  1.000 84.56170  ? 118 VAL A N     1 
ATOM   886  C CA    . VAL A 1 114 ? -39.41883 52.50318 17.52480  1.000 88.18392  ? 118 VAL A CA    1 
ATOM   887  C C     . VAL A 1 114 ? -38.91121 51.07330 17.65033  1.000 91.25516  ? 118 VAL A C     1 
ATOM   888  O O     . VAL A 1 114 ? -38.67957 50.56815 18.75511  1.000 92.33522  ? 118 VAL A O     1 
ATOM   889  C CB    . VAL A 1 114 ? -40.95756 52.56508 17.57764  1.000 86.62711  ? 118 VAL A CB    1 
ATOM   890  C CG1   . VAL A 1 114 ? -41.50904 51.65812 18.64966  1.000 86.61388  ? 118 VAL A CG1   1 
ATOM   891  C CG2   . VAL A 1 114 ? -41.41794 54.00329 17.77596  1.000 88.34643  ? 118 VAL A CG2   1 
ATOM   892  N N     . ILE A 1 115 ? -38.72795 50.40030 16.52203  1.000 87.21567  ? 119 ILE A N     1 
ATOM   893  C CA    . ILE A 1 115 ? -38.47791 48.97178 16.54595  1.000 91.75194  ? 119 ILE A CA    1 
ATOM   894  C C     . ILE A 1 115 ? -37.13754 48.62847 17.18674  1.000 100.01496 ? 119 ILE A C     1 
ATOM   895  O O     . ILE A 1 115 ? -36.99989 47.56168 17.80366  1.000 97.99479  ? 119 ILE A O     1 
ATOM   896  C CB    . ILE A 1 115 ? -38.59401 48.44949 15.11163  1.000 86.53156  ? 119 ILE A CB    1 
ATOM   897  C CG1   . ILE A 1 115 ? -40.05235 48.12147 14.82389  1.000 73.68783  ? 119 ILE A CG1   1 
ATOM   898  C CG2   . ILE A 1 115 ? -37.66782 47.27282 14.87367  1.000 84.21747  ? 119 ILE A CG2   1 
ATOM   899  C CD1   . ILE A 1 115 ? -40.31866 48.12226 13.37574  1.000 81.39816  ? 119 ILE A CD1   1 
ATOM   900  N N     . GLN A 1 116 ? -36.13156 49.50784 17.06573  1.000 102.67100 ? 120 GLN A N     1 
ATOM   901  C CA    . GLN A 1 116 ? -34.82041 49.20115 17.63604  1.000 112.14929 ? 120 GLN A CA    1 
ATOM   902  C C     . GLN A 1 116 ? -34.79050 49.35129 19.15834  1.000 113.92645 ? 120 GLN A C     1 
ATOM   903  O O     . GLN A 1 116 ? -33.94307 48.73264 19.81706  1.000 118.70171 ? 120 GLN A O     1 
ATOM   904  C CB    . GLN A 1 116 ? -33.73465 50.07603 16.99507  1.000 122.06529 ? 120 GLN A CB    1 
ATOM   905  C CG    . GLN A 1 116 ? -34.21393 51.43307 16.48711  1.000 120.37632 ? 120 GLN A CG    1 
ATOM   906  C CD    . GLN A 1 116 ? -33.06303 52.39364 16.15194  1.000 125.54288 ? 120 GLN A CD    1 
ATOM   907  O OE1   . GLN A 1 116 ? -32.35996 52.88013 17.04478  1.000 128.53644 ? 120 GLN A OE1   1 
ATOM   908  N NE2   . GLN A 1 116 ? -32.88279 52.68043 14.86311  1.000 120.43913 ? 120 GLN A NE2   1 
ATOM   909  N N     . MET A 1 117 ? -35.67652 50.16587 19.73386  1.000 111.01347 ? 121 MET A N     1 
ATOM   910  C CA    . MET A 1 117 ? -35.67427 50.40934 21.17132  1.000 114.57420 ? 121 MET A CA    1 
ATOM   911  C C     . MET A 1 117 ? -36.54711 49.39128 21.89753  1.000 110.61646 ? 121 MET A C     1 
ATOM   912  O O     . MET A 1 117 ? -37.40607 48.74031 21.30325  1.000 107.90580 ? 121 MET A O     1 
ATOM   913  C CB    . MET A 1 117 ? -36.16387 51.82087 21.48666  1.000 113.41997 ? 121 MET A CB    1 
ATOM   914  C CG    . MET A 1 117 ? -37.49046 52.15639 20.85501  1.000 110.61066 ? 121 MET A CG    1 
ATOM   915  S SD    . MET A 1 117 ? -38.09036 53.77552 21.33718  1.000 124.95700 ? 121 MET A SD    1 
ATOM   916  C CE    . MET A 1 117 ? -36.53688 54.68033 21.27428  1.000 125.32759 ? 121 MET A CE    1 
ATOM   917  N N     . GLU A 1 118 ? -36.32508 49.27128 23.20811  1.000 114.19610 ? 122 GLU A N     1 
ATOM   918  C CA    . GLU A 1 118 ? -37.05448 48.30878 24.02767  1.000 113.41656 ? 122 GLU A CA    1 
ATOM   919  C C     . GLU A 1 118 ? -38.32240 48.95793 24.56615  1.000 107.79304 ? 122 GLU A C     1 
ATOM   920  O O     . GLU A 1 118 ? -38.26357 49.98953 25.24551  1.000 107.16336 ? 122 GLU A O     1 
ATOM   921  C CB    . GLU A 1 118 ? -36.20529 47.78530 25.18713  1.000 122.24176 ? 122 GLU A CB    1 
ATOM   922  C CG    . GLU A 1 118 ? -36.98257 46.80788 26.09313  1.000 132.92212 ? 122 GLU A CG    1 
ATOM   923  C CD    . GLU A 1 118 ? -36.77367 47.04849 27.58275  1.000 141.29411 ? 122 GLU A CD    1 
ATOM   924  O OE1   . GLU A 1 118 ? -37.47158 47.92442 28.14649  1.000 140.04371 ? 122 GLU A OE1   1 
ATOM   925  O OE2   . GLU A 1 118 ? -35.92748 46.34860 28.19023  1.000 144.45146 ? 122 GLU A OE2   1 
ATOM   926  N N     . LEU A 1 119 ? -39.46149 48.35122 24.26774  1.000 104.30216 ? 123 LEU A N     1 
ATOM   927  C CA    . LEU A 1 119 ? -40.74599 48.86202 24.70914  1.000 95.60707  ? 123 LEU A CA    1 
ATOM   928  C C     . LEU A 1 119 ? -41.22594 48.03140 25.88482  1.000 94.27787  ? 123 LEU A C     1 
ATOM   929  O O     . LEU A 1 119 ? -41.08297 46.80363 25.89062  1.000 98.31516  ? 123 LEU A O     1 
ATOM   930  C CB    . LEU A 1 119 ? -41.77137 48.81042 23.57535  1.000 94.17971  ? 123 LEU A CB    1 
ATOM   931  C CG    . LEU A 1 119 ? -41.75053 49.95781 22.55581  1.000 97.50216  ? 123 LEU A CG    1 
ATOM   932  C CD1   . LEU A 1 119 ? -42.14869 51.28150 23.18940  1.000 89.10709  ? 123 LEU A CD1   1 
ATOM   933  C CD2   . LEU A 1 119 ? -40.39241 50.09318 21.85810  1.000 102.53075 ? 123 LEU A CD2   1 
ATOM   934  N N     . ASP A 1 120 ? -41.77553 48.70276 26.88958  1.000 84.99320  ? 124 ASP A N     1 
ATOM   935  C CA    . ASP A 1 120 ? -42.41383 47.97380 27.97393  1.000 86.75856  ? 124 ASP A CA    1 
ATOM   936  C C     . ASP A 1 120 ? -43.76368 47.43314 27.49825  1.000 86.10653  ? 124 ASP A C     1 
ATOM   937  O O     . ASP A 1 120 ? -44.19701 47.67176 26.36566  1.000 83.99941  ? 124 ASP A O     1 
ATOM   938  C CB    . ASP A 1 120 ? -42.56874 48.86954 29.19319  1.000 84.92517  ? 124 ASP A CB    1 
ATOM   939  C CG    . ASP A 1 120 ? -43.38858 50.09305 28.89212  1.000 93.57644  ? 124 ASP A CG    1 
ATOM   940  O OD1   . ASP A 1 120 ? -42.97527 50.87121 28.00137  1.000 95.02282  ? 124 ASP A OD1   1 
ATOM   941  O OD2   . ASP A 1 120 ? -44.45721 50.26089 29.52137  1.000 101.06785 ? 124 ASP A OD2   1 
ATOM   942  N N     . HIS A 1 121 ? -44.44439 46.69303 28.37657  1.000 87.02878  ? 125 HIS A N     1 
ATOM   943  C CA    . HIS A 1 121 ? -45.65535 45.99541 27.94874  1.000 84.02455  ? 125 HIS A CA    1 
ATOM   944  C C     . HIS A 1 121 ? -46.78748 46.97351 27.66431  1.000 81.38813  ? 125 HIS A C     1 
ATOM   945  O O     . HIS A 1 121 ? -47.48437 46.83353 26.65024  1.000 78.53282  ? 125 HIS A O     1 
ATOM   946  C CB    . HIS A 1 121 ? -46.07199 44.96361 28.99777  1.000 86.52813  ? 125 HIS A CB    1 
ATOM   947  C CG    . HIS A 1 121 ? -45.35017 43.65495 28.87794  1.000 86.26629  ? 125 HIS A CG    1 
ATOM   948  N ND1   . HIS A 1 121 ? -45.14020 43.02677 27.66774  1.000 80.01409  ? 125 HIS A ND1   1 
ATOM   949  C CD2   . HIS A 1 121 ? -44.74659 42.88177 29.81305  1.000 96.31518  ? 125 HIS A CD2   1 
ATOM   950  C CE1   . HIS A 1 121 ? -44.46114 41.91032 27.86667  1.000 84.86655  ? 125 HIS A CE1   1 
ATOM   951  N NE2   . HIS A 1 121 ? -44.20738 41.80107 29.15844  1.000 92.02113  ? 125 HIS A NE2   1 
ATOM   952  N N     . GLU A 1 122 ? -46.97309 47.98249 28.52664  1.000 79.72898  ? 126 GLU A N     1 
ATOM   953  C CA    . GLU A 1 122 ? -48.02594 48.96216 28.28085  1.000 75.75611  ? 126 GLU A CA    1 
ATOM   954  C C     . GLU A 1 122 ? -47.89948 49.53698 26.87961  1.000 74.62621  ? 126 GLU A C     1 
ATOM   955  O O     . GLU A 1 122 ? -48.85279 49.49776 26.09614  1.000 76.52906  ? 126 GLU A O     1 
ATOM   956  C CB    . GLU A 1 122 ? -47.98950 50.08318 29.32220  1.000 75.02271  ? 126 GLU A CB    1 
ATOM   957  C CG    . GLU A 1 122 ? -48.89818 49.87300 30.53984  1.000 86.76392  ? 126 GLU A CG    1 
ATOM   958  C CD    . GLU A 1 122 ? -48.39709 48.77771 31.48188  1.000 101.71507 ? 126 GLU A CD    1 
ATOM   959  O OE1   . GLU A 1 122 ? -47.32925 48.17980 31.19435  1.000 104.51908 ? 126 GLU A OE1   1 
ATOM   960  O OE2   . GLU A 1 122 ? -49.05931 48.52706 32.52131  1.000 106.43368 ? 126 GLU A OE2   1 
ATOM   961  N N     . ARG A 1 123 ? -46.70330 50.00405 26.51508  1.000 73.91921  ? 127 ARG A N     1 
ATOM   962  C CA    . ARG A 1 123 ? -46.55796 50.68839 25.23250  1.000 76.44608  ? 127 ARG A CA    1 
ATOM   963  C C     . ARG A 1 123 ? -46.67483 49.72469 24.06029  1.000 71.91489  ? 127 ARG A C     1 
ATOM   964  O O     . ARG A 1 123 ? -47.25047 50.06756 23.02212  1.000 70.66191  ? 127 ARG A O     1 
ATOM   965  C CB    . ARG A 1 123 ? -45.23082 51.43298 25.17043  1.000 71.16638  ? 127 ARG A CB    1 
ATOM   966  C CG    . ARG A 1 123 ? -45.27873 52.71581 25.94917  1.000 79.43796  ? 127 ARG A CG    1 
ATOM   967  C CD    . ARG A 1 123 ? -43.90440 53.23129 26.29526  1.000 78.87864  ? 127 ARG A CD    1 
ATOM   968  N NE    . ARG A 1 123 ? -44.01719 54.62975 26.66919  1.000 76.36732  ? 127 ARG A NE    1 
ATOM   969  C CZ    . ARG A 1 123 ? -44.01480 55.06340 27.92081  1.000 86.09087  ? 127 ARG A CZ    1 
ATOM   970  N NH1   . ARG A 1 123 ? -43.81592 54.23646 28.93461  1.000 90.87411  ? 127 ARG A NH1   1 
ATOM   971  N NH2   . ARG A 1 123 ? -44.20768 56.36002 28.16158  1.000 82.09038  ? 127 ARG A NH2   1 
ATOM   972  N N     . MET A 1 124 ? -46.11784 48.52815 24.19589  1.000 74.14549  ? 128 MET A N     1 
ATOM   973  C CA    . MET A 1 124 ? -46.19213 47.55281 23.11898  1.000 69.26829  ? 128 MET A CA    1 
ATOM   974  C C     . MET A 1 124 ? -47.64581 47.17846 22.83396  1.000 74.17850  ? 128 MET A C     1 
ATOM   975  O O     . MET A 1 124 ? -48.09096 47.21680 21.67976  1.000 70.16964  ? 128 MET A O     1 
ATOM   976  C CB    . MET A 1 124 ? -45.34942 46.33505 23.50846  1.000 68.86504  ? 128 MET A CB    1 
ATOM   977  C CG    . MET A 1 124 ? -45.17094 45.29756 22.45065  1.000 72.60231  ? 128 MET A CG    1 
ATOM   978  S SD    . MET A 1 124 ? -43.42751 44.86146 22.39734  1.000 103.18722 ? 128 MET A SD    1 
ATOM   979  C CE    . MET A 1 124 ? -43.14894 44.19540 24.05514  1.000 88.29636  ? 128 MET A CE    1 
ATOM   980  N N     . SER A 1 125 ? -48.42552 46.87545 23.88518  1.000 67.76244  ? 129 SER A N     1 
ATOM   981  C CA    . SER A 1 125 ? -49.80564 46.45049 23.65637  1.000 73.13246  ? 129 SER A CA    1 
ATOM   982  C C     . SER A 1 125 ? -50.67381 47.61033 23.17755  1.000 71.38321  ? 129 SER A C     1 
ATOM   983  O O     . SER A 1 125 ? -51.59252 47.40930 22.36891  1.000 63.13058  ? 129 SER A O     1 
ATOM   984  C CB    . SER A 1 125 ? -50.41972 45.83817 24.91822  1.000 69.98936  ? 129 SER A CB    1 
ATOM   985  O OG    . SER A 1 125 ? -50.43801 46.77763 25.97257  1.000 79.59833  ? 129 SER A OG    1 
ATOM   986  N N     . TYR A 1 126 ? -50.42697 48.82501 23.68780  1.000 69.21720  ? 130 TYR A N     1 
ATOM   987  C CA    . TYR A 1 126 ? -51.22663 49.97608 23.26459  1.000 69.70894  ? 130 TYR A CA    1 
ATOM   988  C C     . TYR A 1 126 ? -51.01239 50.27119 21.78331  1.000 70.36364  ? 130 TYR A C     1 
ATOM   989  O O     . TYR A 1 126 ? -51.97659 50.53032 21.03948  1.000 67.43741  ? 130 TYR A O     1 
ATOM   990  C CB    . TYR A 1 126 ? -50.89825 51.20425 24.12120  1.000 65.36132  ? 130 TYR A CB    1 
ATOM   991  C CG    . TYR A 1 126 ? -51.80839 52.39942 23.89326  1.000 74.13230  ? 130 TYR A CG    1 
ATOM   992  C CD1   . TYR A 1 126 ? -53.19178 52.24745 23.80289  1.000 71.36077  ? 130 TYR A CD1   1 
ATOM   993  C CD2   . TYR A 1 126 ? -51.28416 53.68213 23.75826  1.000 68.87819  ? 130 TYR A CD2   1 
ATOM   994  C CE1   . TYR A 1 126 ? -54.02185 53.34432 23.59729  1.000 69.26900  ? 130 TYR A CE1   1 
ATOM   995  C CE2   . TYR A 1 126 ? -52.09602 54.77793 23.54620  1.000 70.96006  ? 130 TYR A CE2   1 
ATOM   996  C CZ    . TYR A 1 126 ? -53.45989 54.60845 23.45213  1.000 72.41773  ? 130 TYR A CZ    1 
ATOM   997  O OH    . TYR A 1 126 ? -54.25954 55.70820 23.24432  1.000 79.46844  ? 130 TYR A OH    1 
ATOM   998  N N     . LEU A 1 127 ? -49.75911 50.20207 21.32689  1.000 64.99119  ? 131 LEU A N     1 
ATOM   999  C CA    . LEU A 1 127 ? -49.47003 50.48777 19.92458  1.000 66.34685  ? 131 LEU A CA    1 
ATOM   1000 C C     . LEU A 1 127 ? -50.11824 49.46138 19.00253  1.000 60.72511  ? 131 LEU A C     1 
ATOM   1001 O O     . LEU A 1 127 ? -50.65150 49.82056 17.94967  1.000 65.28721  ? 131 LEU A O     1 
ATOM   1002 C CB    . LEU A 1 127 ? -47.95717 50.53769 19.69730  1.000 61.44860  ? 131 LEU A CB    1 
ATOM   1003 C CG    . LEU A 1 127 ? -47.19226 51.68362 20.36990  1.000 65.15549  ? 131 LEU A CG    1 
ATOM   1004 C CD1   . LEU A 1 127 ? -45.67889 51.53969 20.12123  1.000 62.63769  ? 131 LEU A CD1   1 
ATOM   1005 C CD2   . LEU A 1 127 ? -47.69478 53.01918 19.87419  1.000 63.19886  ? 131 LEU A CD2   1 
ATOM   1006 N N     . LEU A 1 128 ? -50.06869 48.17929 19.36813  1.000 65.93555  ? 132 LEU A N     1 
ATOM   1007 C CA    . LEU A 1 128 ? -50.72261 47.14990 18.55994  1.000 69.08059  ? 132 LEU A CA    1 
ATOM   1008 C C     . LEU A 1 128 ? -52.23300 47.37053 18.54226  1.000 65.84763  ? 132 LEU A C     1 
ATOM   1009 O O     . LEU A 1 128 ? -52.87370 47.35556 17.47610  1.000 58.79060  ? 132 LEU A O     1 
ATOM   1010 C CB    . LEU A 1 128 ? -50.36442 45.76239 19.10712  1.000 56.80065  ? 132 LEU A CB    1 
ATOM   1011 C CG    . LEU A 1 128 ? -48.84392 45.45555 19.09784  1.000 70.87791  ? 132 LEU A CG    1 
ATOM   1012 C CD1   . LEU A 1 128 ? -48.48147 44.31821 20.05621  1.000 63.77844  ? 132 LEU A CD1   1 
ATOM   1013 C CD2   . LEU A 1 128 ? -48.29640 45.14266 17.69898  1.000 64.06663  ? 132 LEU A CD2   1 
ATOM   1014 N N     . TYR A 1 129 ? -52.81614 47.63227 19.71796  1.000 63.39495  ? 133 TYR A N     1 
ATOM   1015 C CA    . TYR A 1 129 ? -54.24302 47.93782 19.77463  1.000 63.14487  ? 133 TYR A CA    1 
ATOM   1016 C C     . TYR A 1 129 ? -54.61312 49.04111 18.78265  1.000 63.62920  ? 133 TYR A C     1 
ATOM   1017 O O     . TYR A 1 129 ? -55.53620 48.87877 17.97534  1.000 62.77052  ? 133 TYR A O     1 
ATOM   1018 C CB    . TYR A 1 129 ? -54.62809 48.34430 21.18973  1.000 59.55885  ? 133 TYR A CB    1 
ATOM   1019 C CG    . TYR A 1 129 ? -56.01476 48.89313 21.32358  1.000 67.39655  ? 133 TYR A CG    1 
ATOM   1020 C CD1   . TYR A 1 129 ? -57.11928 48.04426 21.29202  1.000 64.87626  ? 133 TYR A CD1   1 
ATOM   1021 C CD2   . TYR A 1 129 ? -56.23288 50.26565 21.47610  1.000 69.36451  ? 133 TYR A CD2   1 
ATOM   1022 C CE1   . TYR A 1 129 ? -58.40698 48.54411 21.42250  1.000 67.55659  ? 133 TYR A CE1   1 
ATOM   1023 C CE2   . TYR A 1 129 ? -57.52791 50.78053 21.60010  1.000 69.89147  ? 133 TYR A CE2   1 
ATOM   1024 C CZ    . TYR A 1 129 ? -58.60885 49.91222 21.57636  1.000 68.93273  ? 133 TYR A CZ    1 
ATOM   1025 O OH    . TYR A 1 129 ? -59.89948 50.39492 21.70141  1.000 67.33182  ? 133 TYR A OH    1 
ATOM   1026 N N     . GLN A 1 130 ? -53.87827 50.15681 18.79726  1.000 62.13241  ? 134 GLN A N     1 
ATOM   1027 C CA    . GLN A 1 130 ? -54.18238 51.22127 17.84706  1.000 63.71141  ? 134 GLN A CA    1 
ATOM   1028 C C     . GLN A 1 130 ? -54.05136 50.71934 16.42388  1.000 62.33691  ? 134 GLN A C     1 
ATOM   1029 O O     . GLN A 1 130 ? -54.92429 50.97874 15.58840  1.000 61.93587  ? 134 GLN A O     1 
ATOM   1030 C CB    . GLN A 1 130 ? -53.25658 52.41558 18.06270  1.000 62.47477  ? 134 GLN A CB    1 
ATOM   1031 C CG    . GLN A 1 130 ? -53.44510 53.09974 19.39968  1.000 59.62812  ? 134 GLN A CG    1 
ATOM   1032 C CD    . GLN A 1 130 ? -52.56019 54.32527 19.53565  1.000 70.78439  ? 134 GLN A CD    1 
ATOM   1033 O OE1   . GLN A 1 130 ? -52.74160 55.31761 18.83297  1.000 75.45734  ? 134 GLN A OE1   1 
ATOM   1034 N NE2   . GLN A 1 130 ? -51.57536 54.24961 20.42619  1.000 64.30495  ? 134 GLN A NE2   1 
ATOM   1035 N N     . MET A 1 131 ? -52.98345 49.95998 16.14752  1.000 56.82526  ? 135 MET A N     1 
ATOM   1036 C CA    . MET A 1 131 ? -52.76424 49.39123 14.82109  1.000 59.74970  ? 135 MET A CA    1 
ATOM   1037 C C     . MET A 1 131 ? -53.91393 48.48052 14.41779  1.000 63.71785  ? 135 MET A C     1 
ATOM   1038 O O     . MET A 1 131 ? -54.38598 48.53345 13.27245  1.000 60.70306  ? 135 MET A O     1 
ATOM   1039 C CB    . MET A 1 131 ? -51.45325 48.60582 14.81947  1.000 64.46430  ? 135 MET A CB    1 
ATOM   1040 C CG    . MET A 1 131 ? -50.86930 48.27075 13.45802  1.000 65.00961  ? 135 MET A CG    1 
ATOM   1041 S SD    . MET A 1 131 ? -49.31995 47.29865 13.62758  1.000 82.80552  ? 135 MET A SD    1 
ATOM   1042 C CE    . MET A 1 131 ? -48.47371 48.10590 14.99696  1.000 54.62595  ? 135 MET A CE    1 
ATOM   1043 N N     . LEU A 1 132 ? -54.38129 47.63332 15.34698  1.000 59.53540  ? 136 LEU A N     1 
ATOM   1044 C CA    . LEU A 1 132 ? -55.48927 46.73491 15.02633  1.000 60.99190  ? 136 LEU A CA    1 
ATOM   1045 C C     . LEU A 1 132 ? -56.77471 47.51831 14.79796  1.000 60.39605  ? 136 LEU A C     1 
ATOM   1046 O O     . LEU A 1 132 ? -57.57938 47.16100 13.93030  1.000 61.34572  ? 136 LEU A O     1 
ATOM   1047 C CB    . LEU A 1 132 ? -55.67129 45.69944 16.13636  1.000 61.76621  ? 136 LEU A CB    1 
ATOM   1048 C CG    . LEU A 1 132 ? -54.61877 44.57829 16.23928  1.000 65.43107  ? 136 LEU A CG    1 
ATOM   1049 C CD1   . LEU A 1 132 ? -54.71187 43.84380 17.58546  1.000 63.89058  ? 136 LEU A CD1   1 
ATOM   1050 C CD2   . LEU A 1 132 ? -54.72352 43.55819 15.08004  1.000 59.93820  ? 136 LEU A CD2   1 
ATOM   1051 N N     . CYS A 1 133 ? -56.98500 48.59904 15.55958  1.000 65.85108  ? 137 CYS A N     1 
ATOM   1052 C CA    . CYS A 1 133 ? -58.16623 49.44036 15.34576  1.000 60.86056  ? 137 CYS A CA    1 
ATOM   1053 C C     . CYS A 1 133 ? -58.14721 50.08669 13.96168  1.000 58.83928  ? 137 CYS A C     1 
ATOM   1054 O O     . CYS A 1 133 ? -59.20166 50.27574 13.33743  1.000 59.98081  ? 137 CYS A O     1 
ATOM   1055 C CB    . CYS A 1 133 ? -58.24740 50.52911 16.41251  1.000 55.15277  ? 137 CYS A CB    1 
ATOM   1056 S SG    . CYS A 1 133 ? -58.70502 49.98371 18.05138  1.000 84.75564  ? 137 CYS A SG    1 
ATOM   1057 N N     . GLY A 1 134 ? -56.96773 50.49624 13.49321  1.000 59.49924  ? 138 GLY A N     1 
ATOM   1058 C CA    . GLY A 1 134 ? -56.88439 51.04190 12.15056  1.000 58.26836  ? 138 GLY A CA    1 
ATOM   1059 C C     . GLY A 1 134 ? -57.28898 50.01080 11.12178  1.000 58.17723  ? 138 GLY A C     1 
ATOM   1060 O O     . GLY A 1 134 ? -58.05926 50.30445 10.20117  1.000 61.32162  ? 138 GLY A O     1 
ATOM   1061 N N     . ILE A 1 135 ? -56.83055 48.77258 11.30934  1.000 54.63515  ? 139 ILE A N     1 
ATOM   1062 C CA    . ILE A 1 135 ? -57.11159 47.69686 10.36022  1.000 53.11613  ? 139 ILE A CA    1 
ATOM   1063 C C     . ILE A 1 135 ? -58.59318 47.33194 10.38313  1.000 56.68599  ? 139 ILE A C     1 
ATOM   1064 O O     . ILE A 1 135 ? -59.24127 47.22816 9.32749   1.000 56.81720  ? 139 ILE A O     1 
ATOM   1065 C CB    . ILE A 1 135 ? -56.21794 46.48931 10.68210  1.000 62.17832  ? 139 ILE A CB    1 
ATOM   1066 C CG1   . ILE A 1 135 ? -54.81000 46.77057 10.17238  1.000 64.87099  ? 139 ILE A CG1   1 
ATOM   1067 C CG2   . ILE A 1 135 ? -56.75209 45.25499 10.03786  1.000 64.55526  ? 139 ILE A CG2   1 
ATOM   1068 C CD1   . ILE A 1 135 ? -53.78644 45.89600 10.78917  1.000 70.78034  ? 139 ILE A CD1   1 
ATOM   1069 N N     . LYS A 1 136 ? -59.16904 47.17065 11.58288  1.000 55.46329  ? 140 LYS A N     1 
ATOM   1070 C CA    . LYS A 1 136 ? -60.58765 46.84777 11.64605  1.000 57.89902  ? 140 LYS A CA    1 
ATOM   1071 C C     . LYS A 1 136 ? -61.39959 47.88322 10.89401  1.000 59.68038  ? 140 LYS A C     1 
ATOM   1072 O O     . LYS A 1 136 ? -62.35726 47.54063 10.18677  1.000 57.02726  ? 140 LYS A O     1 
ATOM   1073 C CB    . LYS A 1 136 ? -61.07062 46.75083 13.08631  1.000 54.58888  ? 140 LYS A CB    1 
ATOM   1074 C CG    . LYS A 1 136 ? -62.50399 46.30880 13.12119  1.000 57.87365  ? 140 LYS A CG    1 
ATOM   1075 C CD    . LYS A 1 136 ? -62.98966 45.89245 14.48370  1.000 69.63750  ? 140 LYS A CD    1 
ATOM   1076 C CE    . LYS A 1 136 ? -64.46931 45.48146 14.40364  1.000 69.77196  ? 140 LYS A CE    1 
ATOM   1077 N NZ    . LYS A 1 136 ? -65.34197 46.64174 13.94229  1.000 72.81254  ? 140 LYS A NZ    1 
ATOM   1078 N N     . HIS A 1 137 ? -61.01445 49.15523 11.00231  1.000 53.42935  ? 141 HIS A N     1 
ATOM   1079 C CA    . HIS A 1 137 ? -61.75247 50.19502 10.28214  1.000 58.82448  ? 141 HIS A CA    1 
ATOM   1080 C C     . HIS A 1 137 ? -61.69566 49.94406 8.77636   1.000 57.98293  ? 141 HIS A C     1 
ATOM   1081 O O     . HIS A 1 137 ? -62.72394 49.96223 8.09528   1.000 63.02677  ? 141 HIS A O     1 
ATOM   1082 C CB    . HIS A 1 137 ? -61.19280 51.57371 10.63757  1.000 58.96721  ? 141 HIS A CB    1 
ATOM   1083 C CG    . HIS A 1 137 ? -61.83355 52.71089 9.90472   1.000 59.66325  ? 141 HIS A CG    1 
ATOM   1084 N ND1   . HIS A 1 137 ? -63.01525 53.28283 10.31259  1.000 61.89760  ? 141 HIS A ND1   1 
ATOM   1085 C CD2   . HIS A 1 137 ? -61.42954 53.42135 8.82273   1.000 53.09183  ? 141 HIS A CD2   1 
ATOM   1086 C CE1   . HIS A 1 137 ? -63.32890 54.28170 9.50349   1.000 62.99294  ? 141 HIS A CE1   1 
ATOM   1087 N NE2   . HIS A 1 137 ? -62.38182 54.38721 8.59015   1.000 62.83295  ? 141 HIS A NE2   1 
ATOM   1088 N N     . LEU A 1 138 ? -60.50387 49.62685 8.24622   1.000 56.12835  ? 142 LEU A N     1 
ATOM   1089 C CA    . LEU A 1 138 ? -60.41422 49.29077 6.82528   1.000 53.21769  ? 142 LEU A CA    1 
ATOM   1090 C C     . LEU A 1 138 ? -61.21184 48.04091 6.49847   1.000 65.59712  ? 142 LEU A C     1 
ATOM   1091 O O     . LEU A 1 138 ? -61.86492 47.95736 5.44612   1.000 58.69943  ? 142 LEU A O     1 
ATOM   1092 C CB    . LEU A 1 138 ? -58.96346 49.06371 6.43297   1.000 57.14317  ? 142 LEU A CB    1 
ATOM   1093 C CG    . LEU A 1 138 ? -58.05618 50.26225 6.52582   1.000 56.66446  ? 142 LEU A CG    1 
ATOM   1094 C CD1   . LEU A 1 138 ? -56.68122 49.78556 6.10371   1.000 53.45590  ? 142 LEU A CD1   1 
ATOM   1095 C CD2   . LEU A 1 138 ? -58.59888 51.33990 5.61608   1.000 51.74310  ? 142 LEU A CD2   1 
ATOM   1096 N N     . HIS A 1 139 ? -61.11088 47.03305 7.36404   1.000 56.16044  ? 143 HIS A N     1 
ATOM   1097 C CA    . HIS A 1 139 ? -61.81382 45.80003 7.11114   1.000 62.00638  ? 143 HIS A CA    1 
ATOM   1098 C C     . HIS A 1 139 ? -63.31597 45.97783 7.22577   1.000 67.18402  ? 143 HIS A C     1 
ATOM   1099 O O     . HIS A 1 139 ? -64.06325 45.24861 6.56294   1.000 54.11565  ? 143 HIS A O     1 
ATOM   1100 C CB    . HIS A 1 139 ? -61.31199 44.72798 8.05958   1.000 58.85337  ? 143 HIS A CB    1 
ATOM   1101 C CG    . HIS A 1 139 ? -59.93073 44.26593 7.73122   1.000 63.33881  ? 143 HIS A CG    1 
ATOM   1102 N ND1   . HIS A 1 139 ? -59.24530 43.34309 8.49237   1.000 65.73836  ? 143 HIS A ND1   1 
ATOM   1103 C CD2   . HIS A 1 139 ? -59.09766 44.61454 6.72372   1.000 63.65453  ? 143 HIS A CD2   1 
ATOM   1104 C CE1   . HIS A 1 139 ? -58.05673 43.12526 7.95797   1.000 62.58491  ? 143 HIS A CE1   1 
ATOM   1105 N NE2   . HIS A 1 139 ? -57.93918 43.88568 6.88537   1.000 65.83075  ? 143 HIS A NE2   1 
ATOM   1106 N N     . SER A 1 140 ? -63.78012 46.93652 8.03511   1.000 65.38448  ? 144 SER A N     1 
ATOM   1107 C CA    . SER A 1 140 ? -65.22688 47.09945 8.20671   1.000 63.91699  ? 144 SER A CA    1 
ATOM   1108 C C     . SER A 1 140 ? -65.92424 47.58785 6.93623   1.000 54.14343  ? 144 SER A C     1 
ATOM   1109 O O     . SER A 1 140 ? -67.15167 47.57510 6.88679   1.000 67.02067  ? 144 SER A O     1 
ATOM   1110 C CB    . SER A 1 140 ? -65.51519 48.04900 9.37129   1.000 65.35439  ? 144 SER A CB    1 
ATOM   1111 O OG    . SER A 1 140 ? -64.96933 49.34792 9.12271   1.000 62.58852  ? 144 SER A OG    1 
ATOM   1112 N N     . ALA A 1 141 ? -65.18010 48.02439 5.91104   1.000 65.22722  ? 145 ALA A N     1 
ATOM   1113 C CA    . ALA A 1 141 ? -65.75060 48.28295 4.58795   1.000 60.18100  ? 145 ALA A CA    1 
ATOM   1114 C C     . ALA A 1 141 ? -65.17657 47.36619 3.50745   1.000 63.93781  ? 145 ALA A C     1 
ATOM   1115 O O     . ALA A 1 141 ? -65.31463 47.66372 2.31191   1.000 68.53260  ? 145 ALA A O     1 
ATOM   1116 C CB    . ALA A 1 141 ? -65.53983 49.73910 4.17807   1.000 64.35588  ? 145 ALA A CB    1 
ATOM   1117 N N     . GLY A 1 142 ? -64.51782 46.26911 3.88918   1.000 60.94483  ? 146 GLY A N     1 
ATOM   1118 C CA    . GLY A 1 142 ? -63.99315 45.32762 2.91257   1.000 63.34021  ? 146 GLY A CA    1 
ATOM   1119 C C     . GLY A 1 142 ? -62.63446 45.68205 2.34446   1.000 71.29504  ? 146 GLY A C     1 
ATOM   1120 O O     . GLY A 1 142 ? -62.11199 44.92757 1.51162   1.000 72.77243  ? 146 GLY A O     1 
ATOM   1121 N N     . ILE A 1 143 ? -62.05238 46.79939 2.76830   1.000 61.77516  ? 147 ILE A N     1 
ATOM   1122 C CA    . ILE A 1 143 ? -60.74624 47.21218 2.29896   1.000 62.23060  ? 147 ILE A CA    1 
ATOM   1123 C C     . ILE A 1 143 ? -59.68425 46.33389 2.93865   1.000 62.49072  ? 147 ILE A C     1 
ATOM   1124 O O     . ILE A 1 143 ? -59.59772 46.23952 4.16970   1.000 58.22489  ? 147 ILE A O     1 
ATOM   1125 C CB    . ILE A 1 143 ? -60.50349 48.68450 2.62896   1.000 65.17137  ? 147 ILE A CB    1 
ATOM   1126 C CG1   . ILE A 1 143 ? -61.55682 49.56739 1.93656   1.000 71.66464  ? 147 ILE A CG1   1 
ATOM   1127 C CG2   . ILE A 1 143 ? -59.13025 49.03700 2.21830   1.000 49.88111  ? 147 ILE A CG2   1 
ATOM   1128 C CD1   . ILE A 1 143 ? -61.71773 50.94036 2.56304   1.000 58.14845  ? 147 ILE A CD1   1 
ATOM   1129 N N     . ILE A 1 144 ? -58.86145 45.70244 2.10589   1.000 60.59535  ? 148 ILE A N     1 
ATOM   1130 C CA    . ILE A 1 144 ? -57.69434 44.95234 2.56256   1.000 62.89916  ? 148 ILE A CA    1 
ATOM   1131 C C     . ILE A 1 144 ? -56.44961 45.74781 2.18917   1.000 63.94313  ? 148 ILE A C     1 
ATOM   1132 O O     . ILE A 1 144 ? -56.21926 46.02964 1.00560   1.000 67.41738  ? 148 ILE A O     1 
ATOM   1133 C CB    . ILE A 1 144 ? -57.65333 43.53796 1.94941   1.000 62.37436  ? 148 ILE A CB    1 
ATOM   1134 C CG1   . ILE A 1 144 ? -58.93837 42.75971 2.19035   1.000 56.37745  ? 148 ILE A CG1   1 
ATOM   1135 C CG2   . ILE A 1 144 ? -56.53652 42.74301 2.54550   1.000 61.10644  ? 148 ILE A CG2   1 
ATOM   1136 C CD1   . ILE A 1 144 ? -58.94794 41.42011 1.43174   1.000 53.74873  ? 148 ILE A CD1   1 
ATOM   1137 N N     . HIS A 1 145 ? -55.63143 46.08497 3.18978   1.000 64.56615  ? 149 HIS A N     1 
ATOM   1138 C CA    . HIS A 1 145 ? -54.47553 46.96314 2.96154   1.000 60.54928  ? 149 HIS A CA    1 
ATOM   1139 C C     . HIS A 1 145 ? -53.40725 46.31374 2.08029   1.000 63.06222  ? 149 HIS A C     1 
ATOM   1140 O O     . HIS A 1 145 ? -52.86561 46.96186 1.17480   1.000 58.97736  ? 149 HIS A O     1 
ATOM   1141 C CB    . HIS A 1 145 ? -53.86819 47.35797 4.30058   1.000 61.51017  ? 149 HIS A CB    1 
ATOM   1142 C CG    . HIS A 1 145 ? -52.84222 48.43249 4.20106   1.000 64.02467  ? 149 HIS A CG    1 
ATOM   1143 N ND1   . HIS A 1 145 ? -51.64913 48.26034 3.53089   1.000 64.42925  ? 149 HIS A ND1   1 
ATOM   1144 C CD2   . HIS A 1 145 ? -52.80990 49.68292 4.71790   1.000 63.09681  ? 149 HIS A CD2   1 
ATOM   1145 C CE1   . HIS A 1 145 ? -50.93464 49.36779 3.62446   1.000 64.76503  ? 149 HIS A CE1   1 
ATOM   1146 N NE2   . HIS A 1 145 ? -51.61629 50.24769 4.33962   1.000 67.46673  ? 149 HIS A NE2   1 
ATOM   1147 N N     . ARG A 1 146 ? -53.04409 45.05779 2.37463   1.000 61.35162  ? 150 ARG A N     1 
ATOM   1148 C CA    . ARG A 1 146 ? -52.04379 44.23238 1.68263   1.000 59.82224  ? 150 ARG A CA    1 
ATOM   1149 C C     . ARG A 1 146 ? -50.61525 44.74309 1.77602   1.000 67.59927  ? 150 ARG A C     1 
ATOM   1150 O O     . ARG A 1 146 ? -49.71975 44.11291 1.18451   1.000 75.95039  ? 150 ARG A O     1 
ATOM   1151 C CB    . ARG A 1 146 ? -52.32802 44.04528 0.18962   1.000 57.26569  ? 150 ARG A CB    1 
ATOM   1152 C CG    . ARG A 1 146 ? -53.72190 43.53325 -0.11008  1.000 65.30893  ? 150 ARG A CG    1 
ATOM   1153 C CD    . ARG A 1 146 ? -54.22604 44.17701 -1.37003  1.000 62.76632  ? 150 ARG A CD    1 
ATOM   1154 N NE    . ARG A 1 146 ? -54.18325 43.28196 -2.51120  1.000 59.35246  ? 150 ARG A NE    1 
ATOM   1155 C CZ    . ARG A 1 146 ? -54.14990 43.69857 -3.76624  1.000 66.29296  ? 150 ARG A CZ    1 
ATOM   1156 N NH1   . ARG A 1 146 ? -54.08398 44.98235 -4.06386  1.000 61.22209  ? 150 ARG A NH1   1 
ATOM   1157 N NH2   . ARG A 1 146 ? -54.18564 42.80195 -4.74569  1.000 76.04235  ? 150 ARG A NH2   1 
ATOM   1158 N N     . ASP A 1 147 ? -50.35243 45.85602 2.45799   1.000 65.42387  ? 151 ASP A N     1 
ATOM   1159 C CA    . ASP A 1 147 ? -48.99357 46.39937 2.45410   1.000 63.24834  ? 151 ASP A CA    1 
ATOM   1160 C C     . ASP A 1 147 ? -48.60063 46.92127 3.82779   1.000 61.40772  ? 151 ASP A C     1 
ATOM   1161 O O     . ASP A 1 147 ? -47.87163 47.91151 3.93180   1.000 60.77052  ? 151 ASP A O     1 
ATOM   1162 C CB    . ASP A 1 147 ? -48.83267 47.51039 1.41770   1.000 67.53902  ? 151 ASP A CB    1 
ATOM   1163 C CG    . ASP A 1 147 ? -47.38801 47.61705 0.89716   1.000 79.92977  ? 151 ASP A CG    1 
ATOM   1164 O OD1   . ASP A 1 147 ? -46.68911 46.57630 0.93936   1.000 80.31536  ? 151 ASP A OD1   1 
ATOM   1165 O OD2   . ASP A 1 147 ? -46.95322 48.71671 0.45040   1.000 81.43891  ? 151 ASP A OD2   1 
ATOM   1166 N N     . LEU A 1 148 ? -49.08877 46.29388 4.90238   1.000 48.95307  ? 152 LEU A N     1 
ATOM   1167 C CA    . LEU A 1 148 ? -48.62679 46.67721 6.22732   1.000 54.74900  ? 152 LEU A CA    1 
ATOM   1168 C C     . LEU A 1 148 ? -47.17421 46.24808 6.42418   1.000 68.61760  ? 152 LEU A C     1 
ATOM   1169 O O     . LEU A 1 148 ? -46.78232 45.12901 6.07593   1.000 63.57021  ? 152 LEU A O     1 
ATOM   1170 C CB    . LEU A 1 148 ? -49.48477 46.04776 7.30171   1.000 54.78882  ? 152 LEU A CB    1 
ATOM   1171 C CG    . LEU A 1 148 ? -50.84946 46.67590 7.37039   1.000 65.44241  ? 152 LEU A CG    1 
ATOM   1172 C CD1   . LEU A 1 148 ? -51.74996 45.66181 8.06939   1.000 69.66340  ? 152 LEU A CD1   1 
ATOM   1173 C CD2   . LEU A 1 148 ? -50.83054 48.05129 8.08881   1.000 66.10823  ? 152 LEU A CD2   1 
ATOM   1174 N N     . LYS A 1 149 ? -46.39644 47.15142 7.00360   1.000 65.77313  ? 153 LYS A N     1 
ATOM   1175 C CA    . LYS A 1 149 ? -44.96806 47.03986 7.25620   1.000 66.74827  ? 153 LYS A CA    1 
ATOM   1176 C C     . LYS A 1 149 ? -44.56041 48.29679 8.03281   1.000 67.53042  ? 153 LYS A C     1 
ATOM   1177 O O     . LYS A 1 149 ? -45.27568 49.30041 7.97949   1.000 64.72957  ? 153 LYS A O     1 
ATOM   1178 C CB    . LYS A 1 149 ? -44.17246 46.91536 5.94471   1.000 60.76330  ? 153 LYS A CB    1 
ATOM   1179 C CG    . LYS A 1 149 ? -44.22469 48.14540 5.08871   1.000 59.82965  ? 153 LYS A CG    1 
ATOM   1180 C CD    . LYS A 1 149 ? -43.55486 47.93750 3.74566   1.000 61.98427  ? 153 LYS A CD    1 
ATOM   1181 C CE    . LYS A 1 149 ? -44.29244 46.88491 2.96158   1.000 73.12191  ? 153 LYS A CE    1 
ATOM   1182 N NZ    . LYS A 1 149 ? -44.09264 47.13914 1.51050   1.000 77.47558  ? 153 LYS A NZ    1 
ATOM   1183 N N     . PRO A 1 150 ? -43.45521 48.25361 8.79208   1.000 65.47536  ? 154 PRO A N     1 
ATOM   1184 C CA    . PRO A 1 150 ? -43.12520 49.39439 9.66950   1.000 67.66790  ? 154 PRO A CA    1 
ATOM   1185 C C     . PRO A 1 150 ? -42.93093 50.72438 8.94464   1.000 65.14255  ? 154 PRO A C     1 
ATOM   1186 O O     . PRO A 1 150 ? -43.17879 51.78202 9.55000   1.000 63.51463  ? 154 PRO A O     1 
ATOM   1187 C CB    . PRO A 1 150 ? -41.82631 48.93680 10.35612  1.000 72.23758  ? 154 PRO A CB    1 
ATOM   1188 C CG    . PRO A 1 150 ? -41.89058 47.46163 10.31102  1.000 65.77467  ? 154 PRO A CG    1 
ATOM   1189 C CD    . PRO A 1 150 ? -42.49057 47.15812 8.96582   1.000 67.11368  ? 154 PRO A CD    1 
ATOM   1190 N N     . SER A 1 151 ? -42.46838 50.72188 7.68829   1.000 58.27813  ? 155 SER A N     1 
ATOM   1191 C CA    . SER A 1 151 ? -42.34394 51.99833 6.99149   1.000 64.10269  ? 155 SER A CA    1 
ATOM   1192 C C     . SER A 1 151 ? -43.70042 52.58635 6.62214   1.000 67.41780  ? 155 SER A C     1 
ATOM   1193 O O     . SER A 1 151 ? -43.75173 53.72066 6.14510   1.000 68.34715  ? 155 SER A O     1 
ATOM   1194 C CB    . SER A 1 151 ? -41.47712 51.83808 5.73931   1.000 66.64205  ? 155 SER A CB    1 
ATOM   1195 O OG    . SER A 1 151 ? -42.16808 51.12037 4.72809   1.000 72.11054  ? 155 SER A OG    1 
ATOM   1196 N N     . ASN A 1 152 ? -44.79279 51.85179 6.83314   1.000 62.35306  ? 156 ASN A N     1 
ATOM   1197 C CA    . ASN A 1 152 ? -46.13931 52.31919 6.52296   1.000 62.38833  ? 156 ASN A CA    1 
ATOM   1198 C C     . ASN A 1 152 ? -46.96100 52.61118 7.76691   1.000 63.51773  ? 156 ASN A C     1 
ATOM   1199 O O     . ASN A 1 152 ? -48.17353 52.78803 7.66602   1.000 58.29633  ? 156 ASN A O     1 
ATOM   1200 C CB    . ASN A 1 152 ? -46.87366 51.30268 5.65182   1.000 62.54140  ? 156 ASN A CB    1 
ATOM   1201 C CG    . ASN A 1 152 ? -46.45208 51.37730 4.21623   1.000 65.97693  ? 156 ASN A CG    1 
ATOM   1202 O OD1   . ASN A 1 152 ? -45.77751 52.32260 3.82928   1.000 71.39092  ? 156 ASN A OD1   1 
ATOM   1203 N ND2   . ASN A 1 152 ? -46.84320 50.38618 3.40857   1.000 69.99805  ? 156 ASN A ND2   1 
ATOM   1204 N N     . ILE A 1 153 ? -46.33886 52.63438 8.94157   1.000 62.82509  ? 157 ILE A N     1 
ATOM   1205 C CA    . ILE A 1 153 ? -47.01380 53.00691 10.17986  1.000 58.77958  ? 157 ILE A CA    1 
ATOM   1206 C C     . ILE A 1 153 ? -46.25213 54.17876 10.76841  1.000 65.98028  ? 157 ILE A C     1 
ATOM   1207 O O     . ILE A 1 153 ? -45.01644 54.15507 10.80565  1.000 65.51824  ? 157 ILE A O     1 
ATOM   1208 C CB    . ILE A 1 153 ? -47.06657 51.83094 11.17447  1.000 60.86185  ? 157 ILE A CB    1 
ATOM   1209 C CG1   . ILE A 1 153 ? -48.11296 50.82089 10.74806  1.000 66.95437  ? 157 ILE A CG1   1 
ATOM   1210 C CG2   . ILE A 1 153 ? -47.40260 52.30997 12.56257  1.000 60.48998  ? 157 ILE A CG2   1 
ATOM   1211 C CD1   . ILE A 1 153 ? -47.57765 49.73145 9.91805   1.000 67.34961  ? 157 ILE A CD1   1 
ATOM   1212 N N     . VAL A 1 154 ? -46.96658 55.21288 11.20696  1.000 60.29807  ? 158 VAL A N     1 
ATOM   1213 C CA    . VAL A 1 154 ? -46.26849 56.35558 11.77643  1.000 63.08914  ? 158 VAL A CA    1 
ATOM   1214 C C     . VAL A 1 154 ? -46.77442 56.58655 13.19290  1.000 62.53500  ? 158 VAL A C     1 
ATOM   1215 O O     . VAL A 1 154 ? -47.87755 56.17538 13.56158  1.000 59.90826  ? 158 VAL A O     1 
ATOM   1216 C CB    . VAL A 1 154 ? -46.42068 57.62540 10.92055  1.000 64.04500  ? 158 VAL A CB    1 
ATOM   1217 C CG1   . VAL A 1 154 ? -45.44194 57.56750 9.76200   1.000 59.86536  ? 158 VAL A CG1   1 
ATOM   1218 C CG2   . VAL A 1 154 ? -47.88886 57.78304 10.45341  1.000 54.86388  ? 158 VAL A CG2   1 
ATOM   1219 N N     . VAL A 1 155 ? -45.94223 57.26007 13.99547  1.000 58.55224  ? 159 VAL A N     1 
ATOM   1220 C CA    . VAL A 1 155 ? -46.22056 57.46350 15.40664  1.000 59.49296  ? 159 VAL A CA    1 
ATOM   1221 C C     . VAL A 1 155 ? -45.86505 58.89439 15.79551  1.000 67.14316  ? 159 VAL A C     1 
ATOM   1222 O O     . VAL A 1 155 ? -45.10711 59.58215 15.10799  1.000 65.04752  ? 159 VAL A O     1 
ATOM   1223 C CB    . VAL A 1 155 ? -45.43315 56.45368 16.26230  1.000 70.65330  ? 159 VAL A CB    1 
ATOM   1224 C CG1   . VAL A 1 155 ? -45.90562 55.02577 15.96723  1.000 57.50478  ? 159 VAL A CG1   1 
ATOM   1225 C CG2   . VAL A 1 155 ? -43.93322 56.58111 16.00213  1.000 63.95003  ? 159 VAL A CG2   1 
ATOM   1226 N N     . LYS A 1 156 ? -46.43671 59.34176 16.90786  1.000 66.73479  ? 160 LYS A N     1 
ATOM   1227 C CA    . LYS A 1 156 ? -46.12016 60.62211 17.50995  1.000 68.89556  ? 160 LYS A CA    1 
ATOM   1228 C C     . LYS A 1 156 ? -45.57130 60.38175 18.90002  1.000 72.44576  ? 160 LYS A C     1 
ATOM   1229 O O     . LYS A 1 156 ? -45.86234 59.36367 19.53088  1.000 73.78589  ? 160 LYS A O     1 
ATOM   1230 C CB    . LYS A 1 156 ? -47.33825 61.53916 17.59940  1.000 68.02843  ? 160 LYS A CB    1 
ATOM   1231 C CG    . LYS A 1 156 ? -47.43833 62.46335 16.43526  1.000 75.13624  ? 160 LYS A CG    1 
ATOM   1232 C CD    . LYS A 1 156 ? -48.66264 63.33175 16.51811  1.000 82.80726  ? 160 LYS A CD    1 
ATOM   1233 C CE    . LYS A 1 156 ? -48.47565 64.44314 17.52708  1.000 82.68740  ? 160 LYS A CE    1 
ATOM   1234 N NZ    . LYS A 1 156 ? -49.39145 65.55596 17.14283  1.000 94.29845  ? 160 LYS A NZ    1 
ATOM   1235 N N     . SER A 1 157 ? -44.78856 61.34608 19.37748  1.000 68.92328  ? 161 SER A N     1 
ATOM   1236 C CA    . SER A 1 157 ? -44.17429 61.20652 20.68720  1.000 72.88327  ? 161 SER A CA    1 
ATOM   1237 C C     . SER A 1 157 ? -45.18118 61.28350 21.82802  1.000 72.22874  ? 161 SER A C     1 
ATOM   1238 O O     . SER A 1 157 ? -44.78689 61.13631 22.99002  1.000 75.15296  ? 161 SER A O     1 
ATOM   1239 C CB    . SER A 1 157 ? -43.07201 62.26010 20.83751  1.000 75.42926  ? 161 SER A CB    1 
ATOM   1240 O OG    . SER A 1 157 ? -43.44904 63.46861 20.19884  1.000 79.33150  ? 161 SER A OG    1 
ATOM   1241 N N     . ASP A 1 158 ? -46.46333 61.51212 21.54415  1.000 72.39844  ? 162 ASP A N     1 
ATOM   1242 C CA    . ASP A 1 158 ? -47.51245 61.34393 22.54688  1.000 71.24427  ? 162 ASP A CA    1 
ATOM   1243 C C     . ASP A 1 158 ? -48.04878 59.92423 22.56314  1.000 75.73137  ? 162 ASP A C     1 
ATOM   1244 O O     . ASP A 1 158 ? -49.07616 59.66390 23.20293  1.000 81.38256  ? 162 ASP A O     1 
ATOM   1245 C CB    . ASP A 1 158 ? -48.65643 62.35226 22.32027  1.000 74.95724  ? 162 ASP A CB    1 
ATOM   1246 C CG    . ASP A 1 158 ? -49.41812 62.14065 20.99092  1.000 81.94632  ? 162 ASP A CG    1 
ATOM   1247 O OD1   . ASP A 1 158 ? -49.05640 61.25648 20.16976  1.000 79.31687  ? 162 ASP A OD1   1 
ATOM   1248 O OD2   . ASP A 1 158 ? -50.39939 62.89046 20.76341  1.000 87.53827  ? 162 ASP A OD2   1 
ATOM   1249 N N     . CYS A 1 159 ? -47.39432 59.02132 21.83223  1.000 69.77525  ? 163 CYS A N     1 
ATOM   1250 C CA    . CYS A 1 159 ? -47.71752 57.60190 21.75527  1.000 73.96371  ? 163 CYS A CA    1 
ATOM   1251 C C     . CYS A 1 159 ? -48.96786 57.29636 20.92539  1.000 76.01581  ? 163 CYS A C     1 
ATOM   1252 O O     . CYS A 1 159 ? -49.60879 56.26400 21.15157  1.000 68.18956  ? 163 CYS A O     1 
ATOM   1253 C CB    . CYS A 1 159 ? -47.87396 57.00296 23.15628  1.000 75.28061  ? 163 CYS A CB    1 
ATOM   1254 S SG    . CYS A 1 159 ? -47.36985 55.29884 23.24437  1.000 78.79865  ? 163 CYS A SG    1 
ATOM   1255 N N     . THR A 1 160 ? -49.35677 58.14879 19.97747  1.000 74.13350  ? 164 THR A N     1 
ATOM   1256 C CA    . THR A 1 160 ? -50.39842 57.78060 19.03077  1.000 66.73069  ? 164 THR A CA    1 
ATOM   1257 C C     . THR A 1 160 ? -49.77153 57.19735 17.76759  1.000 73.04875  ? 164 THR A C     1 
ATOM   1258 O O     . THR A 1 160 ? -48.59185 57.43984 17.46031  1.000 61.67011  ? 164 THR A O     1 
ATOM   1259 C CB    . THR A 1 160 ? -51.27439 58.97874 18.66621  1.000 70.28786  ? 164 THR A CB    1 
ATOM   1260 O OG1   . THR A 1 160 ? -50.47013 60.04010 18.12741  1.000 68.84640  ? 164 THR A OG1   1 
ATOM   1261 C CG2   . THR A 1 160 ? -52.03499 59.45729 19.88442  1.000 68.26546  ? 164 THR A CG2   1 
ATOM   1262 N N     . LEU A 1 161 ? -50.58392 56.41571 17.03195  1.000 62.70262  ? 165 LEU A N     1 
ATOM   1263 C CA    . LEU A 1 161 ? -50.12500 55.65092 15.87186  1.000 57.73294  ? 165 LEU A CA    1 
ATOM   1264 C C     . LEU A 1 161 ? -51.18096 55.71303 14.77114  1.000 59.29895  ? 165 LEU A C     1 
ATOM   1265 O O     . LEU A 1 161 ? -52.38593 55.71723 15.06207  1.000 62.33844  ? 165 LEU A O     1 
ATOM   1266 C CB    . LEU A 1 161 ? -49.80574 54.20019 16.29630  1.000 58.07134  ? 165 LEU A CB    1 
ATOM   1267 C CG    . LEU A 1 161 ? -49.56010 53.01293 15.35737  1.000 62.70586  ? 165 LEU A CG    1 
ATOM   1268 C CD1   . LEU A 1 161 ? -48.86059 51.87709 16.09742  1.000 64.91525  ? 165 LEU A CD1   1 
ATOM   1269 C CD2   . LEU A 1 161 ? -50.86752 52.51061 14.79133  1.000 56.80283  ? 165 LEU A CD2   1 
ATOM   1270 N N     . LYS A 1 162 ? -50.73678 55.80123 13.50467  1.000 57.15176  ? 166 LYS A N     1 
ATOM   1271 C CA    . LYS A 1 162 ? -51.65629 55.87196 12.36793  1.000 59.79785  ? 166 LYS A CA    1 
ATOM   1272 C C     . LYS A 1 162 ? -51.10362 55.05159 11.20584  1.000 63.35828  ? 166 LYS A C     1 
ATOM   1273 O O     . LYS A 1 162 ? -49.89004 54.97647 11.02679  1.000 57.18112  ? 166 LYS A O     1 
ATOM   1274 C CB    . LYS A 1 162 ? -51.88212 57.31635 11.91296  1.000 61.64135  ? 166 LYS A CB    1 
ATOM   1275 C CG    . LYS A 1 162 ? -52.49667 58.24968 12.97559  1.000 64.89195  ? 166 LYS A CG    1 
ATOM   1276 C CD    . LYS A 1 162 ? -52.64157 59.67336 12.47048  1.000 66.86962  ? 166 LYS A CD    1 
ATOM   1277 C CE    . LYS A 1 162 ? -52.99274 60.60080 13.60959  1.000 74.45620  ? 166 LYS A CE    1 
ATOM   1278 N NZ    . LYS A 1 162 ? -54.30193 60.19653 14.18897  1.000 64.44626  ? 166 LYS A NZ    1 
ATOM   1279 N N     . ILE A 1 163 ? -51.99832 54.41648 10.41716  1.000 61.91804  ? 167 ILE A N     1 
ATOM   1280 C CA    . ILE A 1 163 ? -51.59613 53.66728 9.23029   1.000 59.98441  ? 167 ILE A CA    1 
ATOM   1281 C C     . ILE A 1 163 ? -51.67587 54.57588 8.01459   1.000 62.62006  ? 167 ILE A C     1 
ATOM   1282 O O     . ILE A 1 163 ? -52.55022 55.45722 7.93800   1.000 57.65308  ? 167 ILE A O     1 
ATOM   1283 C CB    . ILE A 1 163 ? -52.48421 52.42327 9.04430   1.000 59.06609  ? 167 ILE A CB    1 
ATOM   1284 C CG1   . ILE A 1 163 ? -52.35261 51.49622 10.23726  1.000 57.73779  ? 167 ILE A CG1   1 
ATOM   1285 C CG2   . ILE A 1 163 ? -52.14521 51.68894 7.75517   1.000 52.27222  ? 167 ILE A CG2   1 
ATOM   1286 C CD1   . ILE A 1 163 ? -53.39653 50.46609 10.22854  1.000 58.38543  ? 167 ILE A CD1   1 
ATOM   1287 N N     . LEU A 1 164 ? -50.76643 54.38557 7.05196   1.000 54.71620  ? 168 LEU A N     1 
ATOM   1288 C CA    . LEU A 1 164 ? -50.86905 55.14446 5.80298   1.000 64.80752  ? 168 LEU A CA    1 
ATOM   1289 C C     . LEU A 1 164 ? -50.56600 54.23616 4.60454   1.000 64.07951  ? 168 LEU A C     1 
ATOM   1290 O O     . LEU A 1 164 ? -50.50349 53.00746 4.71876   1.000 64.24382  ? 168 LEU A O     1 
ATOM   1291 C CB    . LEU A 1 164 ? -49.96441 56.38788 5.85581   1.000 67.96430  ? 168 LEU A CB    1 
ATOM   1292 C CG    . LEU A 1 164 ? -48.58820 56.28996 6.52508   1.000 71.51877  ? 168 LEU A CG    1 
ATOM   1293 C CD1   . LEU A 1 164 ? -47.56258 55.60797 5.64134   1.000 66.60098  ? 168 LEU A CD1   1 
ATOM   1294 C CD2   . LEU A 1 164 ? -48.12610 57.68632 6.91043   1.000 67.29683  ? 168 LEU A CD2   1 
ATOM   1295 N N     . ASP A 1 165 ? -50.42697 54.86849 3.43639   1.000 71.06972  ? 169 ASP A N     1 
ATOM   1296 C CA    . ASP A 1 165 ? -50.10382 54.23344 2.16128   1.000 75.45580  ? 169 ASP A CA    1 
ATOM   1297 C C     . ASP A 1 165 ? -51.08989 53.17046 1.70154   1.000 71.64726  ? 169 ASP A C     1 
ATOM   1298 O O     . ASP A 1 165 ? -50.83343 51.97624 1.90966   1.000 69.52880  ? 169 ASP A O     1 
ATOM   1299 C CB    . ASP A 1 165 ? -48.70152 53.61917 2.14355   1.000 62.99665  ? 169 ASP A CB    1 
ATOM   1300 C CG    . ASP A 1 165 ? -48.22387 53.38291 0.70554   1.000 78.42541  ? 169 ASP A CG    1 
ATOM   1301 O OD1   . ASP A 1 165 ? -48.85824 53.94520 -0.22930  1.000 87.70281  ? 169 ASP A OD1   1 
ATOM   1302 O OD2   . ASP A 1 165 ? -47.25236 52.63837 0.48266   1.000 76.35950  ? 169 ASP A OD2   1 
ATOM   1303 N N     . PHE A 1 166 ? -52.23690 53.58306 1.15395   1.000 67.80855  ? 170 PHE A N     1 
ATOM   1304 C CA    . PHE A 1 166 ? -53.22094 52.64595 0.61706   1.000 68.51305  ? 170 PHE A CA    1 
ATOM   1305 C C     . PHE A 1 166 ? -53.05174 52.36769 -0.87480  1.000 61.70673  ? 170 PHE A C     1 
ATOM   1306 O O     . PHE A 1 166 ? -54.00002 51.90849 -1.50949  1.000 71.12082  ? 170 PHE A O     1 
ATOM   1307 C CB    . PHE A 1 166 ? -54.63691 53.15541 0.91761   1.000 62.33073  ? 170 PHE A CB    1 
ATOM   1308 C CG    . PHE A 1 166 ? -54.76687 53.63385 2.30197   1.000 64.55874  ? 170 PHE A CG    1 
ATOM   1309 C CD1   . PHE A 1 166 ? -54.86760 52.73075 3.34309   1.000 66.41586  ? 170 PHE A CD1   1 
ATOM   1310 C CD2   . PHE A 1 166 ? -54.64062 54.97387 2.59747   1.000 66.31176  ? 170 PHE A CD2   1 
ATOM   1311 C CE1   . PHE A 1 166 ? -54.91885 53.16436 4.66387   1.000 67.09815  ? 170 PHE A CE1   1 
ATOM   1312 C CE2   . PHE A 1 166 ? -54.68861 55.41703 3.91441   1.000 66.46676  ? 170 PHE A CE2   1 
ATOM   1313 C CZ    . PHE A 1 166 ? -54.82486 54.50920 4.94930   1.000 62.60293  ? 170 PHE A CZ    1 
ATOM   1314 N N     . GLY A 1 167 ? -51.86302 52.57091 -1.44078  1.000 68.41993  ? 171 GLY A N     1 
ATOM   1315 C CA    . GLY A 1 167 ? -51.68048 52.33072 -2.86879  1.000 58.58950  ? 171 GLY A CA    1 
ATOM   1316 C C     . GLY A 1 167 ? -51.87295 50.88372 -3.28087  1.000 65.20350  ? 171 GLY A C     1 
ATOM   1317 O O     . GLY A 1 167 ? -52.22558 50.60223 -4.43195  1.000 77.70523  ? 171 GLY A O     1 
ATOM   1318 N N     . LEU A 1 168 ? -51.65126 49.94368 -2.36800  1.000 63.92699  ? 172 LEU A N     1 
ATOM   1319 C CA    . LEU A 1 168 ? -51.93396 48.54605 -2.66624  1.000 62.44027  ? 172 LEU A CA    1 
ATOM   1320 C C     . LEU A 1 168 ? -53.30401 48.08623 -2.16738  1.000 67.91371  ? 172 LEU A C     1 
ATOM   1321 O O     . LEU A 1 168 ? -53.64350 46.91221 -2.32828  1.000 66.93347  ? 172 LEU A O     1 
ATOM   1322 C CB    . LEU A 1 168 ? -50.86830 47.64588 -2.06916  1.000 65.63783  ? 172 LEU A CB    1 
ATOM   1323 C CG    . LEU A 1 168 ? -49.46172 47.70969 -2.65639  1.000 74.46094  ? 172 LEU A CG    1 
ATOM   1324 C CD1   . LEU A 1 168 ? -48.97013 46.26966 -2.84340  1.000 71.15050  ? 172 LEU A CD1   1 
ATOM   1325 C CD2   . LEU A 1 168 ? -49.43776 48.48779 -3.94856  1.000 66.80030  ? 172 LEU A CD2   1 
ATOM   1326 N N     . ALA A 1 169 ? -54.09867 48.96044 -1.56167  1.000 58.77242  ? 173 ALA A N     1 
ATOM   1327 C CA    . ALA A 1 169 ? -55.30160 48.45967 -0.91939  1.000 66.56185  ? 173 ALA A CA    1 
ATOM   1328 C C     . ALA A 1 169 ? -56.30427 47.96741 -1.95794  1.000 71.28689  ? 173 ALA A C     1 
ATOM   1329 O O     . ALA A 1 169 ? -56.36701 48.46243 -3.08567  1.000 71.08153  ? 173 ALA A O     1 
ATOM   1330 C CB    . ALA A 1 169 ? -55.93239 49.52778 -0.03311  1.000 63.73970  ? 173 ALA A CB    1 
ATOM   1331 N N     . ARG A 1 170 ? -57.06503 46.95490 -1.56623  1.000 67.07630  ? 174 ARG A N     1 
ATOM   1332 C CA    . ARG A 1 170 ? -58.01354 46.26954 -2.42739  1.000 69.84568  ? 174 ARG A CA    1 
ATOM   1333 C C     . ARG A 1 170 ? -59.39760 46.36672 -1.80344  1.000 63.80254  ? 174 ARG A C     1 
ATOM   1334 O O     . ARG A 1 170 ? -59.53290 46.28821 -0.57709  1.000 65.82572  ? 174 ARG A O     1 
ATOM   1335 C CB    . ARG A 1 170 ? -57.57044 44.81252 -2.60697  1.000 64.53035  ? 174 ARG A CB    1 
ATOM   1336 C CG    . ARG A 1 170 ? -58.67950 43.81903 -2.68623  1.000 70.76165  ? 174 ARG A CG    1 
ATOM   1337 C CD    . ARG A 1 170 ? -58.18400 42.38938 -2.74193  1.000 75.13396  ? 174 ARG A CD    1 
ATOM   1338 N NE    . ARG A 1 170 ? -59.29866 41.44858 -2.85694  1.000 71.79492  ? 174 ARG A NE    1 
ATOM   1339 C CZ    . ARG A 1 170 ? -60.16068 41.44063 -3.86770  1.000 87.47660  ? 174 ARG A CZ    1 
ATOM   1340 N NH1   . ARG A 1 170 ? -60.06526 42.30903 -4.86545  1.000 93.63161  ? 174 ARG A NH1   1 
ATOM   1341 N NH2   . ARG A 1 170 ? -61.15610 40.55290 -3.87153  1.000 91.89303  ? 174 ARG A NH2   1 
ATOM   1342 N N     . THR A 1 171 ? -60.41701 46.59408 -2.62931  1.000 68.95878  ? 175 THR A N     1 
ATOM   1343 C CA    . THR A 1 171 ? -61.78383 46.56584 -2.12951  1.000 70.36023  ? 175 THR A CA    1 
ATOM   1344 C C     . THR A 1 171 ? -62.31393 45.12655 -2.10412  1.000 76.44390  ? 175 THR A C     1 
ATOM   1345 O O     . THR A 1 171 ? -61.68090 44.18728 -2.59214  1.000 59.16921  ? 175 THR A O     1 
ATOM   1346 C CB    . THR A 1 171 ? -62.70276 47.43215 -2.97714  1.000 69.54166  ? 175 THR A CB    1 
ATOM   1347 O OG1   . THR A 1 171 ? -62.60100 47.05820 -4.35536  1.000 78.71869  ? 175 THR A OG1   1 
ATOM   1348 C CG2   . THR A 1 171 ? -62.33297 48.88337 -2.82080  1.000 75.65540  ? 175 THR A CG2   1 
ATOM   1349 N N     . ALA A 1 172 ? -63.49887 44.95275 -1.53145  1.000 71.51513  ? 176 ALA A N     1 
ATOM   1350 C CA    . ALA A 1 172 ? -64.02689 43.60326 -1.39988  1.000 70.84100  ? 176 ALA A CA    1 
ATOM   1351 C C     . ALA A 1 172 ? -64.43676 43.02792 -2.76262  1.000 72.21052  ? 176 ALA A C     1 
ATOM   1352 O O     . ALA A 1 172 ? -64.73582 43.75211 -3.72333  1.000 80.17557  ? 176 ALA A O     1 
ATOM   1353 C CB    . ALA A 1 172 ? -65.21145 43.58564 -0.42894  1.000 72.76546  ? 176 ALA A CB    1 
ATOM   1354 N N     . GLY A 1 173 ? -64.42979 41.70530 -2.82922  1.000 69.04500  ? 177 GLY A N     1 
ATOM   1355 C CA    . GLY A 1 173 ? -64.79128 40.94472 -4.01062  1.000 75.58547  ? 177 GLY A CA    1 
ATOM   1356 C C     . GLY A 1 173 ? -64.41400 39.48804 -3.84692  1.000 73.56801  ? 177 GLY A C     1 
ATOM   1357 O O     . GLY A 1 173 ? -63.54405 39.12157 -3.05609  1.000 74.72160  ? 177 GLY A O     1 
ATOM   1358 N N     . THR A 1 174 ? -65.09670 38.63341 -4.60805  1.000 74.96044  ? 178 THR A N     1 
ATOM   1359 C CA    . THR A 1 174 ? -64.86839 37.19418 -4.55223  1.000 73.91910  ? 178 THR A CA    1 
ATOM   1360 C C     . THR A 1 174 ? -63.97804 36.71784 -5.68630  1.000 67.93876  ? 178 THR A C     1 
ATOM   1361 O O     . THR A 1 174 ? -63.92734 35.51876 -5.95662  1.000 71.78235  ? 178 THR A O     1 
ATOM   1362 C CB    . THR A 1 174 ? -66.20285 36.43020 -4.57420  1.000 73.86369  ? 178 THR A CB    1 
ATOM   1363 O OG1   . THR A 1 174 ? -66.88475 36.65902 -5.82108  1.000 74.55082  ? 178 THR A OG1   1 
ATOM   1364 C CG2   . THR A 1 174 ? -67.09151 36.88184 -3.41431  1.000 74.75702  ? 178 THR A CG2   1 
ATOM   1365 N N     . SER A 1 175 ? -63.33289 37.63469 -6.39097  1.000 71.27674  ? 179 SER A N     1 
ATOM   1366 C CA    . SER A 1 175 ? -62.41895 37.29838 -7.46354  1.000 65.58725  ? 179 SER A CA    1 
ATOM   1367 C C     . SER A 1 175 ? -60.98672 37.41836 -6.96680  1.000 74.62311  ? 179 SER A C     1 
ATOM   1368 O O     . SER A 1 175 ? -60.66123 38.26340 -6.12227  1.000 70.84977  ? 179 SER A O     1 
ATOM   1369 C CB    . SER A 1 175 ? -62.61824 38.21274 -8.67496  1.000 75.10703  ? 179 SER A CB    1 
ATOM   1370 O OG    . SER A 1 175 ? -63.59666 37.68639 -9.54797  1.000 85.15560  ? 179 SER A OG    1 
ATOM   1371 N N     . PHE A 1 176 ? -60.13968 36.54330 -7.49709  1.000 62.60645  ? 180 PHE A N     1 
ATOM   1372 C CA    . PHE A 1 176 ? -58.73595 36.56553 -7.16800  1.000 68.17671  ? 180 PHE A CA    1 
ATOM   1373 C C     . PHE A 1 176 ? -58.09942 37.82514 -7.72793  1.000 71.17545  ? 180 PHE A C     1 
ATOM   1374 O O     . PHE A 1 176 ? -58.33860 38.19418 -8.88306  1.000 69.43646  ? 180 PHE A O     1 
ATOM   1375 C CB    . PHE A 1 176 ? -58.03293 35.34461 -7.74216  1.000 63.87014  ? 180 PHE A CB    1 
ATOM   1376 C CG    . PHE A 1 176 ? -56.56526 35.37283 -7.52519  1.000 66.70052  ? 180 PHE A CG    1 
ATOM   1377 C CD1   . PHE A 1 176 ? -56.04195 35.16082 -6.25003  1.000 69.25669  ? 180 PHE A CD1   1 
ATOM   1378 C CD2   . PHE A 1 176 ? -55.69209 35.67451 -8.56462  1.000 68.40446  ? 180 PHE A CD2   1 
ATOM   1379 C CE1   . PHE A 1 176 ? -54.66549 35.19343 -6.03346  1.000 68.63918  ? 180 PHE A CE1   1 
ATOM   1380 C CE2   . PHE A 1 176 ? -54.31285 35.70650 -8.34555  1.000 66.14349  ? 180 PHE A CE2   1 
ATOM   1381 C CZ    . PHE A 1 176 ? -53.81109 35.46458 -7.08746  1.000 62.90953  ? 180 PHE A CZ    1 
ATOM   1382 N N     . MET A 1 177 ? -57.27644 38.46987 -6.90853  1.000 68.41621  ? 181 MET A N     1 
ATOM   1383 C CA    . MET A 1 177 ? -56.49044 39.61983 -7.32821  1.000 72.20228  ? 181 MET A CA    1 
ATOM   1384 C C     . MET A 1 177 ? -55.04383 39.38551 -6.98139  1.000 71.71553  ? 181 MET A C     1 
ATOM   1385 O O     . MET A 1 177 ? -54.71301 39.25479 -5.79826  1.000 69.72429  ? 181 MET A O     1 
ATOM   1386 C CB    . MET A 1 177 ? -56.93090 40.88092 -6.63242  1.000 76.23666  ? 181 MET A CB    1 
ATOM   1387 C CG    . MET A 1 177 ? -58.26685 41.16065 -7.04900  1.000 80.72009  ? 181 MET A CG    1 
ATOM   1388 S SD    . MET A 1 177 ? -58.77321 42.85069 -6.93679  1.000 104.39889 ? 181 MET A SD    1 
ATOM   1389 C CE    . MET A 1 177 ? -60.05518 42.61762 -8.13687  1.000 113.08772 ? 181 MET A CE    1 
ATOM   1390 N N     . MET A 1 178 ? -54.18916 39.37260 -7.99607  1.000 69.22116  ? 182 MET A N     1 
ATOM   1391 C CA    . MET A 1 178 ? -52.76284 39.25247 -7.75755  1.000 68.47053  ? 182 MET A CA    1 
ATOM   1392 C C     . MET A 1 178 ? -52.25637 40.48005 -7.00816  1.000 68.73580  ? 182 MET A C     1 
ATOM   1393 O O     . MET A 1 178 ? -52.57095 41.60907 -7.37308  1.000 77.92442  ? 182 MET A O     1 
ATOM   1394 C CB    . MET A 1 178 ? -52.04911 39.08497 -9.10176  1.000 70.26543  ? 182 MET A CB    1 
ATOM   1395 C CG    . MET A 1 178 ? -50.54454 38.73274 -9.03262  1.000 87.19055  ? 182 MET A CG    1 
ATOM   1396 S SD    . MET A 1 178 ? -50.21086 37.29432 -7.98209  1.000 118.13795 ? 182 MET A SD    1 
ATOM   1397 C CE    . MET A 1 178 ? -50.14871 35.95938 -9.19478  1.000 88.13240  ? 182 MET A CE    1 
ATOM   1398 N N     . THR A 1 179 ? -51.48703 40.26543 -5.95165  1.000 68.06667  ? 183 THR A N     1 
ATOM   1399 C CA    . THR A 1 179 ? -50.89568 41.38815 -5.22603  1.000 73.55459  ? 183 THR A CA    1 
ATOM   1400 C C     . THR A 1 179 ? -49.79828 42.06400 -6.05093  1.000 72.34291  ? 183 THR A C     1 
ATOM   1401 O O     . THR A 1 179 ? -48.90528 41.37563 -6.56206  1.000 78.97791  ? 183 THR A O     1 
ATOM   1402 C CB    . THR A 1 179 ? -50.32906 40.90513 -3.89840  1.000 77.00919  ? 183 THR A CB    1 
ATOM   1403 O OG1   . THR A 1 179 ? -51.34334 40.18216 -3.19116  1.000 74.25450  ? 183 THR A OG1   1 
ATOM   1404 C CG2   . THR A 1 179 ? -49.84773 42.08223 -3.05836  1.000 74.55806  ? 183 THR A CG2   1 
ATOM   1405 N N     . PRO A 1 180 ? -49.82184 43.39861 -6.19950  1.000 74.37036  ? 184 PRO A N     1 
ATOM   1406 C CA    . PRO A 1 180 ? -48.78166 44.06671 -6.99431  1.000 77.96445  ? 184 PRO A CA    1 
ATOM   1407 C C     . PRO A 1 180 ? -47.39753 43.85459 -6.40109  1.000 76.01270  ? 184 PRO A C     1 
ATOM   1408 O O     . PRO A 1 180 ? -47.23132 43.68174 -5.18816  1.000 69.70482  ? 184 PRO A O     1 
ATOM   1409 C CB    . PRO A 1 180 ? -49.17737 45.55186 -6.95093  1.000 68.71989  ? 184 PRO A CB    1 
ATOM   1410 C CG    . PRO A 1 180 ? -50.58892 45.57602 -6.56089  1.000 74.87359  ? 184 PRO A CG    1 
ATOM   1411 C CD    . PRO A 1 180 ? -50.83709 44.34897 -5.71840  1.000 70.59345  ? 184 PRO A CD    1 
ATOM   1412 N N     . TYR A 1 181 ? -46.40062 43.86030 -7.28902  1.000 80.04686  ? 185 TYR A N     1 
ATOM   1413 C CA    . TYR A 1 181 ? -45.00661 43.84067 -6.87010  1.000 87.87940  ? 185 TYR A CA    1 
ATOM   1414 C C     . TYR A 1 181 ? -44.72673 44.97860 -5.89511  1.000 82.25062  ? 185 TYR A C     1 
ATOM   1415 O O     . TYR A 1 181 ? -45.28879 46.06951 -6.00917  1.000 87.18796  ? 185 TYR A O     1 
ATOM   1416 C CB    . TYR A 1 181 ? -44.08844 43.96746 -8.09129  1.000 97.96766  ? 185 TYR A CB    1 
ATOM   1417 C CG    . TYR A 1 181 ? -42.66617 44.26487 -7.71093  1.000 99.52637  ? 185 TYR A CG    1 
ATOM   1418 C CD1   . TYR A 1 181 ? -41.75614 43.23624 -7.56472  1.000 110.23793 ? 185 TYR A CD1   1 
ATOM   1419 C CD2   . TYR A 1 181 ? -42.23156 45.56746 -7.48540  1.000 96.38908  ? 185 TYR A CD2   1 
ATOM   1420 C CE1   . TYR A 1 181 ? -40.45303 43.48197 -7.19849  1.000 114.20086 ? 185 TYR A CE1   1 
ATOM   1421 C CE2   . TYR A 1 181 ? -40.92521 45.82449 -7.10857  1.000 101.75524 ? 185 TYR A CE2   1 
ATOM   1422 C CZ    . TYR A 1 181 ? -40.03994 44.77822 -6.97014  1.000 106.32626 ? 185 TYR A CZ    1 
ATOM   1423 O OH    . TYR A 1 181 ? -38.73448 45.01679 -6.60533  1.000 115.40491 ? 185 TYR A OH    1 
ATOM   1424 N N     . VAL A 1 182 ? -43.83806 44.72605 -4.93178  1.000 88.06153  ? 186 VAL A N     1 
ATOM   1425 C CA    . VAL A 1 182 ? -43.37357 45.75465 -4.00318  1.000 91.82486  ? 186 VAL A CA    1 
ATOM   1426 C C     . VAL A 1 182 ? -41.94572 45.40457 -3.58835  1.000 96.60329  ? 186 VAL A C     1 
ATOM   1427 O O     . VAL A 1 182 ? -41.52360 44.24658 -3.66935  1.000 91.56428  ? 186 VAL A O     1 
ATOM   1428 C CB    . VAL A 1 182 ? -44.30663 45.88585 -2.77223  1.000 84.27668  ? 186 VAL A CB    1 
ATOM   1429 C CG1   . VAL A 1 182 ? -44.08222 44.73202 -1.80771  1.000 83.90789  ? 186 VAL A CG1   1 
ATOM   1430 C CG2   . VAL A 1 182 ? -44.09540 47.21497 -2.08282  1.000 92.18473  ? 186 VAL A CG2   1 
ATOM   1431 N N     . VAL A 1 183 ? -41.18591 46.42523 -3.15521  1.000 99.62341  ? 187 VAL A N     1 
ATOM   1432 C CA    . VAL A 1 183 ? -39.76176 46.22417 -2.84837  1.000 96.93688  ? 187 VAL A CA    1 
ATOM   1433 C C     . VAL A 1 183 ? -39.58718 45.48721 -1.51985  1.000 93.81926  ? 187 VAL A C     1 
ATOM   1434 O O     . VAL A 1 183 ? -38.87181 44.47921 -1.44043  1.000 90.87851  ? 187 VAL A O     1 
ATOM   1435 C CB    . VAL A 1 183 ? -38.99765 47.56382 -2.84487  1.000 97.27316  ? 187 VAL A CB    1 
ATOM   1436 C CG1   . VAL A 1 183 ? -37.67238 47.40382 -2.12628  1.000 89.52809  ? 187 VAL A CG1   1 
ATOM   1437 C CG2   . VAL A 1 183 ? -38.74379 48.06149 -4.26601  1.000 84.56654  ? 187 VAL A CG2   1 
ATOM   1438 N N     . THR A 1 184 ? -40.22388 45.98193 -0.45570  1.000 91.44799  ? 188 THR A N     1 
ATOM   1439 C CA    . THR A 1 184 ? -40.13159 45.35837 0.86619   1.000 89.72769  ? 188 THR A CA    1 
ATOM   1440 C C     . THR A 1 184 ? -41.22582 44.29574 0.99419   1.000 91.99057  ? 188 THR A C     1 
ATOM   1441 O O     . THR A 1 184 ? -42.38287 44.60441 1.29168   1.000 91.37124  ? 188 THR A O     1 
ATOM   1442 C CB    . THR A 1 184 ? -40.24053 46.41546 1.96283   1.000 85.44535  ? 188 THR A CB    1 
ATOM   1443 O OG1   . THR A 1 184 ? -39.34101 47.49479 1.67597   1.000 95.22893  ? 188 THR A OG1   1 
ATOM   1444 C CG2   . THR A 1 184 ? -39.88430 45.82121 3.32539   1.000 77.74871  ? 188 THR A CG2   1 
ATOM   1445 N N     . ARG A 1 185 ? -40.85175 43.03166 0.80473   1.000 92.90861  ? 189 ARG A N     1 
ATOM   1446 C CA    . ARG A 1 185 ? -41.79687 41.92174 0.78976   1.000 86.51918  ? 189 ARG A CA    1 
ATOM   1447 C C     . ARG A 1 185 ? -41.80339 41.10007 2.07617   1.000 83.27815  ? 189 ARG A C     1 
ATOM   1448 O O     . ARG A 1 185 ? -42.57873 40.14765 2.17962   1.000 79.70957  ? 189 ARG A O     1 
ATOM   1449 C CB    . ARG A 1 185 ? -41.48236 41.01406 -0.40305  1.000 87.16546  ? 189 ARG A CB    1 
ATOM   1450 C CG    . ARG A 1 185 ? -40.10582 40.38299 -0.30448  1.000 101.09179 ? 189 ARG A CG    1 
ATOM   1451 C CD    . ARG A 1 185 ? -39.87701 39.31943 -1.38236  1.000 104.56038 ? 189 ARG A CD    1 
ATOM   1452 N NE    . ARG A 1 185 ? -39.87813 39.85476 -2.74176  1.000 107.64715 ? 189 ARG A NE    1 
ATOM   1453 C CZ    . ARG A 1 185 ? -39.09991 40.83450 -3.19269  1.000 112.78112 ? 189 ARG A CZ    1 
ATOM   1454 N NH1   . ARG A 1 185 ? -38.19616 41.42517 -2.41893  1.000 100.57156 ? 189 ARG A NH1   1 
ATOM   1455 N NH2   . ARG A 1 185 ? -39.22134 41.22287 -4.46119  1.000 114.23989 ? 189 ARG A NH2   1 
ATOM   1456 N N     . TYR A 1 186 ? -41.00857 41.47181 3.08100   1.000 85.10286  ? 190 TYR A N     1 
ATOM   1457 C CA    . TYR A 1 186 ? -40.80237 40.61853 4.25152   1.000 83.76547  ? 190 TYR A CA    1 
ATOM   1458 C C     . TYR A 1 186 ? -42.06134 40.40378 5.07705   1.000 73.66053  ? 190 TYR A C     1 
ATOM   1459 O O     . TYR A 1 186 ? -42.03927 39.56801 5.98245   1.000 69.81953  ? 190 TYR A O     1 
ATOM   1460 C CB    . TYR A 1 186 ? -39.72490 41.19919 5.18112   1.000 82.82773  ? 190 TYR A CB    1 
ATOM   1461 C CG    . TYR A 1 186 ? -38.52425 41.79535 4.48968   1.000 81.46658  ? 190 TYR A CG    1 
ATOM   1462 C CD1   . TYR A 1 186 ? -37.86936 41.11147 3.47635   1.000 87.26802  ? 190 TYR A CD1   1 
ATOM   1463 C CD2   . TYR A 1 186 ? -38.03650 43.04874 4.85881   1.000 86.56968  ? 190 TYR A CD2   1 
ATOM   1464 C CE1   . TYR A 1 186 ? -36.75704 41.66211 2.83953   1.000 91.15428  ? 190 TYR A CE1   1 
ATOM   1465 C CE2   . TYR A 1 186 ? -36.92313 43.60430 4.22681   1.000 83.93649  ? 190 TYR A CE2   1 
ATOM   1466 C CZ    . TYR A 1 186 ? -36.29122 42.90372 3.21847   1.000 83.78127  ? 190 TYR A CZ    1 
ATOM   1467 O OH    . TYR A 1 186 ? -35.19131 43.43790 2.58093   1.000 89.69032  ? 190 TYR A OH    1 
ATOM   1468 N N     . TYR A 1 187 ? -43.12790 41.15622 4.82314   1.000 77.68259  ? 191 TYR A N     1 
ATOM   1469 C CA    . TYR A 1 187 ? -44.32317 41.14854 5.65730   1.000 74.37579  ? 191 TYR A CA    1 
ATOM   1470 C C     . TYR A 1 187 ? -45.51738 40.49650 4.97384   1.000 69.71888  ? 191 TYR A C     1 
ATOM   1471 O O     . TYR A 1 187 ? -46.59989 40.45366 5.56691   1.000 70.40822  ? 191 TYR A O     1 
ATOM   1472 C CB    . TYR A 1 187 ? -44.64942 42.59018 6.08761   1.000 70.56986  ? 191 TYR A CB    1 
ATOM   1473 C CG    . TYR A 1 187 ? -43.49966 43.16929 6.86515   1.000 74.45078  ? 191 TYR A CG    1 
ATOM   1474 C CD1   . TYR A 1 187 ? -42.36958 43.65521 6.20926   1.000 78.25038  ? 191 TYR A CD1   1 
ATOM   1475 C CD2   . TYR A 1 187 ? -43.49920 43.15493 8.25223   1.000 74.52965  ? 191 TYR A CD2   1 
ATOM   1476 C CE1   . TYR A 1 187 ? -41.28656 44.14284 6.90828   1.000 73.87862  ? 191 TYR A CE1   1 
ATOM   1477 C CE2   . TYR A 1 187 ? -42.41080 43.64445 8.96829   1.000 71.78701  ? 191 TYR A CE2   1 
ATOM   1478 C CZ    . TYR A 1 187 ? -41.30761 44.13093 8.29027   1.000 73.68917  ? 191 TYR A CZ    1 
ATOM   1479 O OH    . TYR A 1 187 ? -40.22296 44.63505 8.98443   1.000 78.05057  ? 191 TYR A OH    1 
ATOM   1480 N N     . ARG A 1 188 ? -45.33803 39.99759 3.74414   1.000 76.43908  ? 192 ARG A N     1 
ATOM   1481 C CA    . ARG A 1 188 ? -46.37560 39.28451 3.00206   1.000 67.56656  ? 192 ARG A CA    1 
ATOM   1482 C C     . ARG A 1 188 ? -46.68866 37.94170 3.65730   1.000 69.85515  ? 192 ARG A C     1 
ATOM   1483 O O     . ARG A 1 188 ? -45.78657 37.20312 4.05279   1.000 74.25436  ? 192 ARG A O     1 
ATOM   1484 C CB    . ARG A 1 188 ? -45.92403 39.01534 1.56142   1.000 70.03466  ? 192 ARG A CB    1 
ATOM   1485 C CG    . ARG A 1 188 ? -45.43681 40.22649 0.73550   1.000 77.67260  ? 192 ARG A CG    1 
ATOM   1486 C CD    . ARG A 1 188 ? -46.56282 41.17373 0.48031   1.000 72.35991  ? 192 ARG A CD    1 
ATOM   1487 N NE    . ARG A 1 188 ? -46.35572 42.16586 -0.56981  1.000 78.67007  ? 192 ARG A NE    1 
ATOM   1488 C CZ    . ARG A 1 188 ? -46.26244 41.90900 -1.86852  1.000 73.77639  ? 192 ARG A CZ    1 
ATOM   1489 N NH1   . ARG A 1 188 ? -45.97383 40.69728 -2.31667  1.000 65.39229  ? 192 ARG A NH1   1 
ATOM   1490 N NH2   . ARG A 1 188 ? -46.49214 42.89249 -2.73945  1.000 76.85869  ? 192 ARG A NH2   1 
ATOM   1491 N N     . ALA A 1 189 ? -47.96986 37.60679 3.72208   1.000 67.96564  ? 193 ALA A N     1 
ATOM   1492 C CA    . ALA A 1 189 ? -48.43146 36.32181 4.22833   1.000 69.11188  ? 193 ALA A CA    1 
ATOM   1493 C C     . ALA A 1 189 ? -48.12368 35.19419 3.25047   1.000 67.53199  ? 193 ALA A C     1 
ATOM   1494 O O     . ALA A 1 189 ? -47.97986 35.42664 2.04116   1.000 68.76106  ? 193 ALA A O     1 
ATOM   1495 C CB    . ALA A 1 189 ? -49.93594 36.36586 4.47515   1.000 67.50962  ? 193 ALA A CB    1 
ATOM   1496 N N     . PRO A 1 190 ? -48.04393 33.94735 3.75309   1.000 63.53042  ? 194 PRO A N     1 
ATOM   1497 C CA    . PRO A 1 190 ? -47.77759 32.80784 2.85622   1.000 66.43830  ? 194 PRO A CA    1 
ATOM   1498 C C     . PRO A 1 190 ? -48.72963 32.71895 1.67816   1.000 68.24965  ? 194 PRO A C     1 
ATOM   1499 O O     . PRO A 1 190 ? -48.30156 32.39159 0.56186   1.000 66.43644  ? 194 PRO A O     1 
ATOM   1500 C CB    . PRO A 1 190 ? -47.93263 31.60311 3.78965   1.000 70.28876  ? 194 PRO A CB    1 
ATOM   1501 C CG    . PRO A 1 190 ? -47.48228 32.12655 5.13219   1.000 69.15806  ? 194 PRO A CG    1 
ATOM   1502 C CD    . PRO A 1 190 ? -48.03392 33.53550 5.17213   1.000 66.16489  ? 194 PRO A CD    1 
ATOM   1503 N N     . GLU A 1 191 ? -50.01167 33.02351 1.88491   1.000 63.26557  ? 195 GLU A N     1 
ATOM   1504 C CA    . GLU A 1 191 ? -50.95305 32.90580 0.78157   1.000 69.45090  ? 195 GLU A CA    1 
ATOM   1505 C C     . GLU A 1 191 ? -50.58500 33.85799 -0.34857  1.000 70.36601  ? 195 GLU A C     1 
ATOM   1506 O O     . GLU A 1 191 ? -50.74105 33.51580 -1.53217  1.000 72.15284  ? 195 GLU A O     1 
ATOM   1507 C CB    . GLU A 1 191 ? -52.38009 33.14846 1.27867   1.000 71.75135  ? 195 GLU A CB    1 
ATOM   1508 C CG    . GLU A 1 191 ? -52.52623 34.34179 2.22989   1.000 70.00101  ? 195 GLU A CG    1 
ATOM   1509 C CD    . GLU A 1 191 ? -52.33729 33.97074 3.71003   1.000 69.34225  ? 195 GLU A CD    1 
ATOM   1510 O OE1   . GLU A 1 191 ? -51.45591 33.13263 4.02060   1.000 66.92051  ? 195 GLU A OE1   1 
ATOM   1511 O OE2   . GLU A 1 191 ? -53.05606 34.53991 4.56620   1.000 63.63922  ? 195 GLU A OE2   1 
ATOM   1512 N N     . VAL A 1 192 ? -50.05416 35.03286 -0.00346  1.000 70.71130  ? 196 VAL A N     1 
ATOM   1513 C CA    . VAL A 1 192 ? -49.60386 35.98591 -1.01343  1.000 72.11903  ? 196 VAL A CA    1 
ATOM   1514 C C     . VAL A 1 192 ? -48.33592 35.48646 -1.68882  1.000 72.77467  ? 196 VAL A C     1 
ATOM   1515 O O     . VAL A 1 192 ? -48.20888 35.54813 -2.92150  1.000 69.74296  ? 196 VAL A O     1 
ATOM   1516 C CB    . VAL A 1 192 ? -49.39767 37.36599 -0.37180  1.000 71.01852  ? 196 VAL A CB    1 
ATOM   1517 C CG1   . VAL A 1 192 ? -49.23400 38.42995 -1.43048  1.000 74.57525  ? 196 VAL A CG1   1 
ATOM   1518 C CG2   . VAL A 1 192 ? -50.56938 37.68261 0.52755   1.000 68.09422  ? 196 VAL A CG2   1 
ATOM   1519 N N     . ILE A 1 193 ? -47.38055 34.98589 -0.89665  1.000 67.96825  ? 197 ILE A N     1 
ATOM   1520 C CA    . ILE A 1 193 ? -46.12607 34.47167 -1.45657  1.000 76.82695  ? 197 ILE A CA    1 
ATOM   1521 C C     . ILE A 1 193 ? -46.41059 33.34491 -2.44032  1.000 76.81118  ? 197 ILE A C     1 
ATOM   1522 O O     . ILE A 1 193 ? -45.86194 33.29539 -3.54726  1.000 81.33003  ? 197 ILE A O     1 
ATOM   1523 C CB    . ILE A 1 193 ? -45.19979 33.97652 -0.33008  1.000 77.67060  ? 197 ILE A CB    1 
ATOM   1524 C CG1   . ILE A 1 193 ? -44.71820 35.11305 0.57152   1.000 76.66491  ? 197 ILE A CG1   1 
ATOM   1525 C CG2   . ILE A 1 193 ? -44.05498 33.14914 -0.87747  1.000 77.45667  ? 197 ILE A CG2   1 
ATOM   1526 C CD1   . ILE A 1 193 ? -44.10403 34.57309 1.86262   1.000 72.42424  ? 197 ILE A CD1   1 
ATOM   1527 N N     . LEU A 1 194 ? -47.27491 32.42685 -2.04571  1.000 71.11984  ? 198 LEU A N     1 
ATOM   1528 C CA    . LEU A 1 194 ? -47.52856 31.21796 -2.80287  1.000 72.88826  ? 198 LEU A CA    1 
ATOM   1529 C C     . LEU A 1 194 ? -48.56315 31.41885 -3.90752  1.000 72.65763  ? 198 LEU A C     1 
ATOM   1530 O O     . LEU A 1 194 ? -48.78953 30.50038 -4.70314  1.000 72.19249  ? 198 LEU A O     1 
ATOM   1531 C CB    . LEU A 1 194 ? -47.95684 30.11674 -1.83693  1.000 72.88537  ? 198 LEU A CB    1 
ATOM   1532 C CG    . LEU A 1 194 ? -46.88641 29.83253 -0.76681  1.000 77.74004  ? 198 LEU A CG    1 
ATOM   1533 C CD1   . LEU A 1 194 ? -47.32547 28.76744 0.24164   1.000 76.50166  ? 198 LEU A CD1   1 
ATOM   1534 C CD2   . LEU A 1 194 ? -45.50783 29.45948 -1.37410  1.000 69.69005  ? 198 LEU A CD2   1 
ATOM   1535 N N     . GLY A 1 195 ? -49.16830 32.60120 -3.99795  1.000 67.20492  ? 199 GLY A N     1 
ATOM   1536 C CA    . GLY A 1 195 ? -50.08899 32.87040 -5.08072  1.000 70.86201  ? 199 GLY A CA    1 
ATOM   1537 C C     . GLY A 1 195 ? -51.45442 32.25459 -4.90101  1.000 70.00142  ? 199 GLY A C     1 
ATOM   1538 O O     . GLY A 1 195 ? -52.09239 31.88150 -5.89231  1.000 73.87457  ? 199 GLY A O     1 
ATOM   1539 N N     . MET A 1 196 ? -51.91808 32.12263 -3.66050  1.000 61.84888  ? 200 MET A N     1 
ATOM   1540 C CA    . MET A 1 196 ? -53.25163 31.61669 -3.36849  1.000 71.73055  ? 200 MET A CA    1 
ATOM   1541 C C     . MET A 1 196 ? -54.23285 32.75904 -3.13322  1.000 69.59231  ? 200 MET A C     1 
ATOM   1542 O O     . MET A 1 196 ? -53.84581 33.88219 -2.80569  1.000 71.38304  ? 200 MET A O     1 
ATOM   1543 C CB    . MET A 1 196 ? -53.23804 30.70485 -2.13437  1.000 72.80737  ? 200 MET A CB    1 
ATOM   1544 C CG    . MET A 1 196 ? -52.38536 29.45602 -2.25012  1.000 68.48783  ? 200 MET A CG    1 
ATOM   1545 S SD    . MET A 1 196 ? -51.65434 29.17070 -0.62886  1.000 79.54821  ? 200 MET A SD    1 
ATOM   1546 C CE    . MET A 1 196 ? -52.98420 28.31537 0.19823   1.000 72.60035  ? 200 MET A CE    1 
ATOM   1547 N N     . GLY A 1 197 ? -55.52145 32.44624 -3.26685  1.000 69.93674  ? 201 GLY A N     1 
ATOM   1548 C CA    . GLY A 1 197 ? -56.53787 33.36930 -2.80940  1.000 62.47683  ? 201 GLY A CA    1 
ATOM   1549 C C     . GLY A 1 197 ? -56.41713 33.62645 -1.32147  1.000 62.48195  ? 201 GLY A C     1 
ATOM   1550 O O     . GLY A 1 197 ? -55.83195 32.83729 -0.56684  1.000 64.69784  ? 201 GLY A O     1 
ATOM   1551 N N     . TYR A 1 198 ? -56.97119 34.75485 -0.88596  1.000 67.37653  ? 202 TYR A N     1 
ATOM   1552 C CA    . TYR A 1 198 ? -56.70896 35.19987 0.47828   1.000 73.85887  ? 202 TYR A CA    1 
ATOM   1553 C C     . TYR A 1 198 ? -57.83245 36.12074 0.93003   1.000 67.62373  ? 202 TYR A C     1 
ATOM   1554 O O     . TYR A 1 198 ? -58.46416 36.78209 0.10742   1.000 67.47978  ? 202 TYR A O     1 
ATOM   1555 C CB    . TYR A 1 198 ? -55.35591 35.92361 0.55486   1.000 63.23878  ? 202 TYR A CB    1 
ATOM   1556 C CG    . TYR A 1 198 ? -55.27505 37.04512 -0.45832  1.000 70.53232  ? 202 TYR A CG    1 
ATOM   1557 C CD1   . TYR A 1 198 ? -55.76022 38.31391 -0.14840  1.000 65.67597  ? 202 TYR A CD1   1 
ATOM   1558 C CD2   . TYR A 1 198 ? -54.74506 36.82987 -1.74022  1.000 68.85656  ? 202 TYR A CD2   1 
ATOM   1559 C CE1   . TYR A 1 198 ? -55.72998 39.35468 -1.08292  1.000 60.79122  ? 202 TYR A CE1   1 
ATOM   1560 C CE2   . TYR A 1 198 ? -54.69999 37.87710 -2.68277  1.000 75.58864  ? 202 TYR A CE2   1 
ATOM   1561 C CZ    . TYR A 1 198 ? -55.19861 39.13556 -2.33611  1.000 68.55137  ? 202 TYR A CZ    1 
ATOM   1562 O OH    . TYR A 1 198 ? -55.18117 40.17284 -3.23702  1.000 69.88017  ? 202 TYR A OH    1 
ATOM   1563 N N     . LYS A 1 199 ? -58.05027 36.16889 2.24405   1.000 63.08207  ? 203 LYS A N     1 
ATOM   1564 C CA    . LYS A 1 199 ? -59.02493 37.02722 2.89936   1.000 71.54656  ? 203 LYS A CA    1 
ATOM   1565 C C     . LYS A 1 199 ? -58.30868 38.20549 3.56192   1.000 71.73099  ? 203 LYS A C     1 
ATOM   1566 O O     . LYS A 1 199 ? -57.12064 38.44933 3.32381   1.000 67.25485  ? 203 LYS A O     1 
ATOM   1567 C CB    . LYS A 1 199 ? -59.86924 36.21393 3.90343   1.000 83.52459  ? 203 LYS A CB    1 
ATOM   1568 C CG    . LYS A 1 199 ? -59.08720 35.43305 4.98168   1.000 82.80189  ? 203 LYS A CG    1 
ATOM   1569 C CD    . LYS A 1 199 ? -60.01997 34.62982 5.91392   1.000 80.34782  ? 203 LYS A CD    1 
ATOM   1570 C CE    . LYS A 1 199 ? -60.92530 35.55099 6.76131   1.000 95.21357  ? 203 LYS A CE    1 
ATOM   1571 N NZ    . LYS A 1 199 ? -60.22593 36.49561 7.72908   1.000 78.76579  ? 203 LYS A NZ    1 
ATOM   1572 N N     . GLU A 1 200 ? -59.04088 38.96148 4.38592   1.000 68.71397  ? 204 GLU A N     1 
ATOM   1573 C CA    . GLU A 1 200 ? -58.44077 40.12006 5.03710   1.000 68.47979  ? 204 GLU A CA    1 
ATOM   1574 C C     . GLU A 1 200 ? -57.39264 39.77232 6.08716   1.000 67.27525  ? 204 GLU A C     1 
ATOM   1575 O O     . GLU A 1 200 ? -56.59597 40.64530 6.43851   1.000 59.33865  ? 204 GLU A O     1 
ATOM   1576 C CB    . GLU A 1 200 ? -59.48294 41.01754 5.71393   1.000 67.22912  ? 204 GLU A CB    1 
ATOM   1577 C CG    . GLU A 1 200 ? -60.63317 40.34994 6.37613   1.000 80.98456  ? 204 GLU A CG    1 
ATOM   1578 C CD    . GLU A 1 200 ? -61.78350 40.20549 5.41534   1.000 92.35277  ? 204 GLU A CD    1 
ATOM   1579 O OE1   . GLU A 1 200 ? -61.79794 39.19786 4.66147   1.000 90.70475  ? 204 GLU A OE1   1 
ATOM   1580 O OE2   . GLU A 1 200 ? -62.60624 41.15894 5.35741   1.000 96.85032  ? 204 GLU A OE2   1 
ATOM   1581 N N     . ASN A 1 201 ? -57.35541 38.56434 6.62478   1.000 64.20782  ? 205 ASN A N     1 
ATOM   1582 C CA    . ASN A 1 201 ? -56.34441 38.35662 7.64658   1.000 66.79378  ? 205 ASN A CA    1 
ATOM   1583 C C     . ASN A 1 201 ? -54.96618 38.03700 7.05023   1.000 63.51558  ? 205 ASN A C     1 
ATOM   1584 O O     . ASN A 1 201 ? -54.09185 37.54984 7.77071   1.000 61.93387  ? 205 ASN A O     1 
ATOM   1585 C CB    . ASN A 1 201 ? -56.78836 37.30161 8.66572   1.000 65.71062  ? 205 ASN A CB    1 
ATOM   1586 C CG    . ASN A 1 201 ? -56.87680 35.92536 8.09077   1.000 78.20406  ? 205 ASN A CG    1 
ATOM   1587 O OD1   . ASN A 1 201 ? -56.77588 35.73724 6.87553   1.000 80.58655  ? 205 ASN A OD1   1 
ATOM   1588 N ND2   . ASN A 1 201 ? -57.09551 34.93321 8.96361   1.000 81.72009  ? 205 ASN A ND2   1 
ATOM   1589 N N     . VAL A 1 202 ? -54.74583 38.32098 5.76113   1.000 57.39665  ? 206 VAL A N     1 
ATOM   1590 C CA    . VAL A 1 202 ? -53.36447 38.52792 5.34410   1.000 59.53455  ? 206 VAL A CA    1 
ATOM   1591 C C     . VAL A 1 202 ? -52.78094 39.69637 6.12986   1.000 68.64166  ? 206 VAL A C     1 
ATOM   1592 O O     . VAL A 1 202 ? -51.58647 39.69803 6.46694   1.000 68.11754  ? 206 VAL A O     1 
ATOM   1593 C CB    . VAL A 1 202 ? -53.24059 38.77371 3.82208   1.000 61.34218  ? 206 VAL A CB    1 
ATOM   1594 C CG1   . VAL A 1 202 ? -53.87594 37.65607 3.05543   1.000 60.65161  ? 206 VAL A CG1   1 
ATOM   1595 C CG2   . VAL A 1 202 ? -53.84738 40.17497 3.41543   1.000 58.33447  ? 206 VAL A CG2   1 
ATOM   1596 N N     . ASP A 1 203 ? -53.61287 40.70418 6.44115   1.000 56.56345  ? 207 ASP A N     1 
ATOM   1597 C CA    . ASP A 1 203 ? -53.12977 41.86003 7.18788   1.000 60.16750  ? 207 ASP A CA    1 
ATOM   1598 C C     . ASP A 1 203 ? -52.73131 41.46202 8.59711   1.000 62.65805  ? 207 ASP A C     1 
ATOM   1599 O O     . ASP A 1 203 ? -51.79567 42.04661 9.17146   1.000 59.81587  ? 207 ASP A O     1 
ATOM   1600 C CB    . ASP A 1 203 ? -54.19334 42.96333 7.24727   1.000 51.74657  ? 207 ASP A CB    1 
ATOM   1601 C CG    . ASP A 1 203 ? -54.39806 43.65076 5.91202   1.000 61.79062  ? 207 ASP A CG    1 
ATOM   1602 O OD1   . ASP A 1 203 ? -53.44585 43.58685 5.10048   1.000 60.05137  ? 207 ASP A OD1   1 
ATOM   1603 O OD2   . ASP A 1 203 ? -55.48694 44.26756 5.67859   1.000 63.43750  ? 207 ASP A OD2   1 
ATOM   1604 N N     . LEU A 1 204 ? -53.42859 40.47783 9.16966   1.000 56.95874  ? 208 LEU A N     1 
ATOM   1605 C CA    . LEU A 1 204 ? -53.05415 40.02394 10.50224  1.000 64.34011  ? 208 LEU A CA    1 
ATOM   1606 C C     . LEU A 1 204 ? -51.68566 39.35348 10.50163  1.000 60.57669  ? 208 LEU A C     1 
ATOM   1607 O O     . LEU A 1 204 ? -50.88471 39.57664 11.41810  1.000 56.64154  ? 208 LEU A O     1 
ATOM   1608 C CB    . LEU A 1 204 ? -54.11596 39.09446 11.07510  1.000 65.12379  ? 208 LEU A CB    1 
ATOM   1609 C CG    . LEU A 1 204 ? -54.88802 39.81177 12.18129  1.000 64.83389  ? 208 LEU A CG    1 
ATOM   1610 C CD1   . LEU A 1 204 ? -55.45077 38.79570 13.06558  1.000 77.52719  ? 208 LEU A CD1   1 
ATOM   1611 C CD2   . LEU A 1 204 ? -54.01247 40.69641 13.03681  1.000 68.85965  ? 208 LEU A CD2   1 
ATOM   1612 N N     . TRP A 1 205 ? -51.37390 38.56090 9.47094   1.000 61.89553  ? 209 TRP A N     1 
ATOM   1613 C CA    . TRP A 1 205 ? -50.01957 38.01876 9.38067   1.000 63.29929  ? 209 TRP A CA    1 
ATOM   1614 C C     . TRP A 1 205 ? -48.98398 39.13812 9.42026   1.000 65.57276  ? 209 TRP A C     1 
ATOM   1615 O O     . TRP A 1 205 ? -47.92255 38.98141 10.03784  1.000 63.47956  ? 209 TRP A O     1 
ATOM   1616 C CB    . TRP A 1 205 ? -49.84984 37.18248 8.11502   1.000 58.79413  ? 209 TRP A CB    1 
ATOM   1617 C CG    . TRP A 1 205 ? -48.42513 36.76274 7.86575   1.000 68.87292  ? 209 TRP A CG    1 
ATOM   1618 C CD1   . TRP A 1 205 ? -47.46027 37.47984 7.20981   1.000 69.96473  ? 209 TRP A CD1   1 
ATOM   1619 C CD2   . TRP A 1 205 ? -47.80299 35.52001 8.25431   1.000 71.59491  ? 209 TRP A CD2   1 
ATOM   1620 N NE1   . TRP A 1 205 ? -46.27869 36.76868 7.17266   1.000 69.72349  ? 209 TRP A NE1   1 
ATOM   1621 C CE2   . TRP A 1 205 ? -46.46067 35.56515 7.80416   1.000 72.51502  ? 209 TRP A CE2   1 
ATOM   1622 C CE3   . TRP A 1 205 ? -48.25059 34.37806 8.93404   1.000 66.21235  ? 209 TRP A CE3   1 
ATOM   1623 C CZ2   . TRP A 1 205 ? -45.55595 34.51125 8.01877   1.000 68.85032  ? 209 TRP A CZ2   1 
ATOM   1624 C CZ3   . TRP A 1 205 ? -47.36648 33.34588 9.14620   1.000 73.02993  ? 209 TRP A CZ3   1 
ATOM   1625 C CH2   . TRP A 1 205 ? -46.02345 33.41695 8.68828   1.000 71.32642  ? 209 TRP A CH2   1 
ATOM   1626 N N     . SER A 1 206 ? -49.27298 40.27781 8.76687   1.000 61.67730  ? 210 SER A N     1 
ATOM   1627 C CA    . SER A 1 206 ? -48.32639 41.39247 8.75281   1.000 58.77970  ? 210 SER A CA    1 
ATOM   1628 C C     . SER A 1 206 ? -48.19053 42.00579 10.13740  1.000 63.09843  ? 210 SER A C     1 
ATOM   1629 O O     . SER A 1 206 ? -47.07774 42.31694 10.58108  1.000 63.32251  ? 210 SER A O     1 
ATOM   1630 C CB    . SER A 1 206 ? -48.76155 42.44580 7.73939   1.000 63.44167  ? 210 SER A CB    1 
ATOM   1631 O OG    . SER A 1 206 ? -48.69465 41.90553 6.42729   1.000 66.40616  ? 210 SER A OG    1 
ATOM   1632 N N     . VAL A 1 207 ? -49.30779 42.15704 10.85286  1.000 63.34472  ? 211 VAL A N     1 
ATOM   1633 C CA    . VAL A 1 207 ? -49.20253 42.57967 12.24397  1.000 62.97829  ? 211 VAL A CA    1 
ATOM   1634 C C     . VAL A 1 207 ? -48.34329 41.59392 13.02371  1.000 61.74423  ? 211 VAL A C     1 
ATOM   1635 O O     . VAL A 1 207 ? -47.53790 41.99976 13.87221  1.000 67.31707  ? 211 VAL A O     1 
ATOM   1636 C CB    . VAL A 1 207 ? -50.59583 42.73894 12.87790  1.000 59.38957  ? 211 VAL A CB    1 
ATOM   1637 C CG1   . VAL A 1 207 ? -50.45619 43.00205 14.35260  1.000 55.14652  ? 211 VAL A CG1   1 
ATOM   1638 C CG2   . VAL A 1 207 ? -51.37193 43.86246 12.20957  1.000 56.27738  ? 211 VAL A CG2   1 
ATOM   1639 N N     . GLY A 1 208 ? -48.46015 40.29739 12.72695  1.000 62.86671  ? 212 GLY A N     1 
ATOM   1640 C CA    . GLY A 1 208 ? -47.60572 39.32203 13.39730  1.000 59.62212  ? 212 GLY A CA    1 
ATOM   1641 C C     . GLY A 1 208 ? -46.12814 39.61921 13.20357  1.000 66.49320  ? 212 GLY A C     1 
ATOM   1642 O O     . GLY A 1 208 ? -45.36692 39.68579 14.17484  1.000 66.41576  ? 212 GLY A O     1 
ATOM   1643 N N     . CYS A 1 209 ? -45.71068 39.86967 11.95370  1.000 63.42713  ? 213 CYS A N     1 
ATOM   1644 C CA    . CYS A 1 209 ? -44.30476 40.18075 11.70307  1.000 71.10749  ? 213 CYS A CA    1 
ATOM   1645 C C     . CYS A 1 209 ? -43.88104 41.43328 12.45882  1.000 71.01601  ? 213 CYS A C     1 
ATOM   1646 O O     . CYS A 1 209 ? -42.82018 41.46326 13.09383  1.000 70.66073  ? 213 CYS A O     1 
ATOM   1647 C CB    . CYS A 1 209 ? -44.06380 40.34533 10.20330  1.000 67.64462  ? 213 CYS A CB    1 
ATOM   1648 S SG    . CYS A 1 209 ? -44.47576 38.81985 9.31633   1.000 76.13989  ? 213 CYS A SG    1 
ATOM   1649 N N     . ILE A 1 210 ? -44.71676 42.47253 12.42410  1.000 75.56453  ? 214 ILE A N     1 
ATOM   1650 C CA    . ILE A 1 210 ? -44.37908 43.72391 13.09830  1.000 72.79057  ? 214 ILE A CA    1 
ATOM   1651 C C     . ILE A 1 210 ? -44.22920 43.50699 14.59967  1.000 71.53310  ? 214 ILE A C     1 
ATOM   1652 O O     . ILE A 1 210 ? -43.25900 43.97241 15.20756  1.000 66.95474  ? 214 ILE A O     1 
ATOM   1653 C CB    . ILE A 1 210 ? -45.43243 44.79128 12.76087  1.000 73.17694  ? 214 ILE A CB    1 
ATOM   1654 C CG1   . ILE A 1 210 ? -45.42670 45.04954 11.25562  1.000 68.02218  ? 214 ILE A CG1   1 
ATOM   1655 C CG2   . ILE A 1 210 ? -45.17037 46.04327 13.51644  1.000 68.26961  ? 214 ILE A CG2   1 
ATOM   1656 C CD1   . ILE A 1 210 ? -46.70014 45.68154 10.75918  1.000 63.21631  ? 214 ILE A CD1   1 
ATOM   1657 N N     . MET A 1 211 ? -45.15513 42.76736 15.21675  1.000 68.51091  ? 215 MET A N     1 
ATOM   1658 C CA    . MET A 1 211 ? -45.02320 42.50246 16.64682  1.000 69.66243  ? 215 MET A CA    1 
ATOM   1659 C C     . MET A 1 211 ? -43.77645 41.68796 16.96903  1.000 74.82080  ? 215 MET A C     1 
ATOM   1660 O O     . MET A 1 211 ? -43.05055 42.00458 17.91800  1.000 79.58119  ? 215 MET A O     1 
ATOM   1661 C CB    . MET A 1 211 ? -46.26007 41.80014 17.17612  1.000 72.25121  ? 215 MET A CB    1 
ATOM   1662 C CG    . MET A 1 211 ? -46.26235 41.69422 18.67998  1.000 73.26354  ? 215 MET A CG    1 
ATOM   1663 S SD    . MET A 1 211 ? -47.72759 40.84291 19.27640  1.000 77.37336  ? 215 MET A SD    1 
ATOM   1664 C CE    . MET A 1 211 ? -47.30634 40.72784 21.02544  1.000 72.16481  ? 215 MET A CE    1 
ATOM   1665 N N     . GLY A 1 212 ? -43.49419 40.64853 16.19075  1.000 73.19109  ? 216 GLY A N     1 
ATOM   1666 C CA    . GLY A 1 212 ? -42.25317 39.91897 16.40596  1.000 75.14533  ? 216 GLY A CA    1 
ATOM   1667 C C     . GLY A 1 212 ? -41.03797 40.82110 16.32188  1.000 78.30579  ? 216 GLY A C     1 
ATOM   1668 O O     . GLY A 1 212 ? -40.12652 40.72746 17.14692  1.000 81.92394  ? 216 GLY A O     1 
ATOM   1669 N N     . GLU A 1 213 ? -41.02881 41.73996 15.34760  1.000 79.53512  ? 217 GLU A N     1 
ATOM   1670 C CA    . GLU A 1 213 ? -39.90626 42.67286 15.19868  1.000 78.28639  ? 217 GLU A CA    1 
ATOM   1671 C C     . GLU A 1 213 ? -39.77240 43.60713 16.40189  1.000 81.65796  ? 217 GLU A C     1 
ATOM   1672 O O     . GLU A 1 213 ? -38.66453 43.81575 16.89964  1.000 85.16695  ? 217 GLU A O     1 
ATOM   1673 C CB    . GLU A 1 213 ? -40.06105 43.48739 13.90918  1.000 76.18950  ? 217 GLU A CB    1 
ATOM   1674 C CG    . GLU A 1 213 ? -38.80182 44.24143 13.48089  1.000 79.10771  ? 217 GLU A CG    1 
ATOM   1675 C CD    . GLU A 1 213 ? -38.85453 44.69271 12.00787  1.000 89.53849  ? 217 GLU A CD    1 
ATOM   1676 O OE1   . GLU A 1 213 ? -39.30436 43.86436 11.16928  1.000 89.41982  ? 217 GLU A OE1   1 
ATOM   1677 O OE2   . GLU A 1 213 ? -38.40655 45.83593 11.67932  1.000 82.85678  ? 217 GLU A OE2   1 
ATOM   1678 N N     . MET A 1 214 ? -40.88660 44.17033 16.89790  1.000 86.76627  ? 218 MET A N     1 
ATOM   1679 C CA    . MET A 1 214 ? -40.81147 45.03045 18.08376  1.000 84.52877  ? 218 MET A CA    1 
ATOM   1680 C C     . MET A 1 214 ? -40.23632 44.29822 19.28524  1.000 81.35332  ? 218 MET A C     1 
ATOM   1681 O O     . MET A 1 214 ? -39.80195 44.95088 20.24327  1.000 100.68183 ? 218 MET A O     1 
ATOM   1682 C CB    . MET A 1 214 ? -42.18900 45.57494 18.49281  1.000 74.54327  ? 218 MET A CB    1 
ATOM   1683 C CG    . MET A 1 214 ? -43.10678 45.94599 17.36392  1.000 87.76425  ? 218 MET A CG    1 
ATOM   1684 S SD    . MET A 1 214 ? -44.40511 47.15497 17.74751  1.000 101.19340 ? 218 MET A SD    1 
ATOM   1685 C CE    . MET A 1 214 ? -45.07787 46.54559 19.27520  1.000 86.67959  ? 218 MET A CE    1 
ATOM   1686 N N     . VAL A 1 215 ? -40.27472 42.96933 19.28067  1.000 83.41478  ? 219 VAL A N     1 
ATOM   1687 C CA    . VAL A 1 215 ? -39.76077 42.15596 20.38602  1.000 85.43243  ? 219 VAL A CA    1 
ATOM   1688 C C     . VAL A 1 215 ? -38.33327 41.68097 20.11593  1.000 86.29795  ? 219 VAL A C     1 
ATOM   1689 O O     . VAL A 1 215 ? -37.47161 41.72521 20.99638  1.000 86.68211  ? 219 VAL A O     1 
ATOM   1690 C CB    . VAL A 1 215 ? -40.70697 40.96148 20.63711  1.000 86.42237  ? 219 VAL A CB    1 
ATOM   1691 C CG1   . VAL A 1 215 ? -40.03112 39.93722 21.54977  1.000 85.27940  ? 219 VAL A CG1   1 
ATOM   1692 C CG2   . VAL A 1 215 ? -42.06435 41.43397 21.18371  1.000 83.55864  ? 219 VAL A CG2   1 
ATOM   1693 N N     . CYS A 1 216 ? -38.08232 41.20375 18.89126  1.000 88.31104  ? 220 CYS A N     1 
ATOM   1694 C CA    . CYS A 1 216 ? -36.75032 40.77231 18.47745  1.000 84.86661  ? 220 CYS A CA    1 
ATOM   1695 C C     . CYS A 1 216 ? -35.82803 41.94848 18.22288  1.000 85.47748  ? 220 CYS A C     1 
ATOM   1696 O O     . CYS A 1 216 ? -34.61305 41.82071 18.39520  1.000 80.87858  ? 220 CYS A O     1 
ATOM   1697 C CB    . CYS A 1 216 ? -36.83874 39.94296 17.19431  1.000 83.19869  ? 220 CYS A CB    1 
ATOM   1698 S SG    . CYS A 1 216 ? -37.11148 38.20549 17.45596  1.000 115.07114 ? 220 CYS A SG    1 
ATOM   1699 N N     . HIS A 1 217 ? -36.38162 43.08896 17.79631  1.000 86.31896  ? 221 HIS A N     1 
ATOM   1700 C CA    . HIS A 1 217 ? -35.59172 44.17712 17.20254  1.000 91.99905  ? 221 HIS A CA    1 
ATOM   1701 C C     . HIS A 1 217 ? -34.85171 43.67332 15.96392  1.000 89.23399  ? 221 HIS A C     1 
ATOM   1702 O O     . HIS A 1 217 ? -33.70139 44.03491 15.70797  1.000 91.67039  ? 221 HIS A O     1 
ATOM   1703 C CB    . HIS A 1 217 ? -34.62234 44.80215 18.21534  1.000 88.61177  ? 221 HIS A CB    1 
ATOM   1704 C CG    . HIS A 1 217 ? -35.19025 44.90799 19.59795  1.000 91.43650  ? 221 HIS A CG    1 
ATOM   1705 N ND1   . HIS A 1 217 ? -36.23830 45.75284 19.91073  1.000 94.14821  ? 221 HIS A ND1   1 
ATOM   1706 C CD2   . HIS A 1 217 ? -34.86487 44.26727 20.74750  1.000 88.51008  ? 221 HIS A CD2   1 
ATOM   1707 C CE1   . HIS A 1 217 ? -36.53119 45.62819 21.19391  1.000 96.53327  ? 221 HIS A CE1   1 
ATOM   1708 N NE2   . HIS A 1 217 ? -35.71301 44.73349 21.72415  1.000 98.14851  ? 221 HIS A NE2   1 
ATOM   1709 N N     . LYS A 1 218 ? -35.52310 42.81596 15.19836  1.000 82.99082  ? 222 LYS A N     1 
ATOM   1710 C CA    . LYS A 1 218 ? -34.94219 42.18827 14.02364  1.000 86.07981  ? 222 LYS A CA    1 
ATOM   1711 C C     . LYS A 1 218 ? -36.07946 41.63666 13.16633  1.000 87.42831  ? 222 LYS A C     1 
ATOM   1712 O O     . LYS A 1 218 ? -37.09394 41.16849 13.69558  1.000 83.42531  ? 222 LYS A O     1 
ATOM   1713 C CB    . LYS A 1 218 ? -33.95016 41.08509 14.43512  1.000 86.52403  ? 222 LYS A CB    1 
ATOM   1714 C CG    . LYS A 1 218 ? -32.84420 40.82087 13.41989  1.000 97.53483  ? 222 LYS A CG    1 
ATOM   1715 C CD    . LYS A 1 218 ? -31.94700 42.05893 13.18155  1.000 105.12911 ? 222 LYS A CD    1 
ATOM   1716 C CE    . LYS A 1 218 ? -30.65652 41.70338 12.41570  1.000 107.49918 ? 222 LYS A CE    1 
ATOM   1717 N NZ    . LYS A 1 218 ? -30.05441 42.87816 11.70634  1.000 103.22732 ? 222 LYS A NZ    1 
ATOM   1718 N N     . ILE A 1 219 ? -35.91092 41.72853 11.84423  1.000 84.61171  ? 223 ILE A N     1 
ATOM   1719 C CA    . ILE A 1 219 ? -36.91166 41.24329 10.89707  1.000 81.11620  ? 223 ILE A CA    1 
ATOM   1720 C C     . ILE A 1 219 ? -37.03332 39.72822 11.00594  1.000 84.64598  ? 223 ILE A C     1 
ATOM   1721 O O     . ILE A 1 219 ? -36.02451 39.01192 10.99107  1.000 86.12010  ? 223 ILE A O     1 
ATOM   1722 C CB    . ILE A 1 219 ? -36.52670 41.66287 9.47169   1.000 82.40839  ? 223 ILE A CB    1 
ATOM   1723 C CG1   . ILE A 1 219 ? -36.34518 43.17816 9.39484   1.000 84.91169  ? 223 ILE A CG1   1 
ATOM   1724 C CG2   . ILE A 1 219 ? -37.57937 41.21504 8.48441   1.000 82.09564  ? 223 ILE A CG2   1 
ATOM   1725 C CD1   . ILE A 1 219 ? -35.69835 43.66206 8.07917   1.000 66.78256  ? 223 ILE A CD1   1 
ATOM   1726 N N     . LEU A 1 220 ? -38.27373 39.23324 11.10602  1.000 79.44049  ? 224 LEU A N     1 
ATOM   1727 C CA    . LEU A 1 220 ? -38.50189 37.80247 11.32333  1.000 79.72339  ? 224 LEU A CA    1 
ATOM   1728 C C     . LEU A 1 220 ? -38.12164 36.96937 10.10726  1.000 81.67982  ? 224 LEU A C     1 
ATOM   1729 O O     . LEU A 1 220 ? -37.49157 35.91216 10.23660  1.000 86.44817  ? 224 LEU A O     1 
ATOM   1730 C CB    . LEU A 1 220 ? -39.96647 37.53141 11.67182  1.000 76.27911  ? 224 LEU A CB    1 
ATOM   1731 C CG    . LEU A 1 220 ? -40.45601 38.04967 13.01249  1.000 78.36356  ? 224 LEU A CG    1 
ATOM   1732 C CD1   . LEU A 1 220 ? -41.67257 37.25498 13.39606  1.000 80.37497  ? 224 LEU A CD1   1 
ATOM   1733 C CD2   . LEU A 1 220 ? -39.36905 37.94225 14.07098  1.000 72.46867  ? 224 LEU A CD2   1 
ATOM   1734 N N     . PHE A 1 221 ? -38.53263 37.39992 8.92082   1.000 84.08782  ? 225 PHE A N     1 
ATOM   1735 C CA    . PHE A 1 221 ? -38.44273 36.57267 7.72033   1.000 85.51243  ? 225 PHE A CA    1 
ATOM   1736 C C     . PHE A 1 221 ? -37.77127 37.34684 6.59270   1.000 86.14150  ? 225 PHE A C     1 
ATOM   1737 O O     . PHE A 1 221 ? -38.38835 37.63229 5.56070   1.000 88.19206  ? 225 PHE A O     1 
ATOM   1738 C CB    . PHE A 1 221 ? -39.82972 36.08485 7.30061   1.000 79.20159  ? 225 PHE A CB    1 
ATOM   1739 C CG    . PHE A 1 221 ? -40.63399 35.46804 8.41934   1.000 74.09092  ? 225 PHE A CG    1 
ATOM   1740 C CD1   . PHE A 1 221 ? -40.18857 34.33380 9.06473   1.000 78.36225  ? 225 PHE A CD1   1 
ATOM   1741 C CD2   . PHE A 1 221 ? -41.85325 36.01192 8.79516   1.000 74.00297  ? 225 PHE A CD2   1 
ATOM   1742 C CE1   . PHE A 1 221 ? -40.93870 33.75337 10.07465  1.000 73.81402  ? 225 PHE A CE1   1 
ATOM   1743 C CE2   . PHE A 1 221 ? -42.62025 35.43762 9.81100   1.000 70.03485  ? 225 PHE A CE2   1 
ATOM   1744 C CZ    . PHE A 1 221 ? -42.15791 34.30100 10.45252  1.000 75.39990  ? 225 PHE A CZ    1 
ATOM   1745 N N     . PRO A 1 222 ? -36.48919 37.66984 6.74056   1.000 81.97971  ? 226 PRO A N     1 
ATOM   1746 C CA    . PRO A 1 222 ? -35.80381 38.46753 5.71349   1.000 86.96368  ? 226 PRO A CA    1 
ATOM   1747 C C     . PRO A 1 222 ? -35.48185 37.62670 4.48310   1.000 100.48075 ? 226 PRO A C     1 
ATOM   1748 O O     . PRO A 1 222 ? -34.81192 36.59178 4.57749   1.000 105.04468 ? 226 PRO A O     1 
ATOM   1749 C CB    . PRO A 1 222 ? -34.52327 38.92350 6.42030   1.000 90.09332  ? 226 PRO A CB    1 
ATOM   1750 C CG    . PRO A 1 222 ? -34.23303 37.81755 7.37586   1.000 91.78967  ? 226 PRO A CG    1 
ATOM   1751 C CD    . PRO A 1 222 ? -35.58665 37.28383 7.83346   1.000 87.98514  ? 226 PRO A CD    1 
ATOM   1752 N N     . GLY A 1 223 ? -35.93609 38.09183 3.31926   1.000 97.27921  ? 227 GLY A N     1 
ATOM   1753 C CA    . GLY A 1 223 ? -35.65587 37.37190 2.09712   1.000 101.06610 ? 227 GLY A CA    1 
ATOM   1754 C C     . GLY A 1 223 ? -35.26310 38.22489 0.90949   1.000 104.23919 ? 227 GLY A C     1 
ATOM   1755 O O     . GLY A 1 223 ? -36.00103 39.13134 0.50623   1.000 100.36756 ? 227 GLY A O     1 
ATOM   1756 N N     . ARG A 1 224 ? -34.09990 37.91808 0.32640   1.000 104.22942 ? 228 ARG A N     1 
ATOM   1757 C CA    . ARG A 1 224 ? -33.75404 38.49070 -0.97022  1.000 110.47124 ? 228 ARG A CA    1 
ATOM   1758 C C     . ARG A 1 224 ? -34.80619 38.13978 -2.01428  1.000 110.66651 ? 228 ARG A C     1 
ATOM   1759 O O     . ARG A 1 224 ? -35.13446 38.95909 -2.88206  1.000 111.13590 ? 228 ARG A O     1 
ATOM   1760 C CB    . ARG A 1 224 ? -32.38445 37.98208 -1.42555  1.000 111.61500 ? 228 ARG A CB    1 
ATOM   1761 C CG    . ARG A 1 224 ? -31.28537 38.00026 -0.35694  1.000 122.54688 ? 228 ARG A CG    1 
ATOM   1762 C CD    . ARG A 1 224 ? -29.94967 38.42648 -0.98176  1.000 133.87254 ? 228 ARG A CD    1 
ATOM   1763 N NE    . ARG A 1 224 ? -28.77893 37.84423 -0.33319  1.000 141.81006 ? 228 ARG A NE    1 
ATOM   1764 C CZ    . ARG A 1 224 ? -27.73095 37.34748 -0.98366  1.000 148.71476 ? 228 ARG A CZ    1 
ATOM   1765 N NH1   . ARG A 1 224 ? -27.69443 37.29955 -2.30790  1.000 144.90788 ? 228 ARG A NH1   1 
ATOM   1766 N NH2   . ARG A 1 224 ? -26.69368 36.88321 -0.28932  1.000 147.31202 ? 228 ARG A NH2   1 
ATOM   1767 N N     . ASP A 1 225 ? -35.36570 36.94049 -1.91428  1.000 108.62008 ? 229 ASP A N     1 
ATOM   1768 C CA    . ASP A 1 225 ? -36.17423 36.32947 -2.94627  1.000 99.75992  ? 229 ASP A CA    1 
ATOM   1769 C C     . ASP A 1 225 ? -37.42359 35.78575 -2.26643  1.000 99.06196  ? 229 ASP A C     1 
ATOM   1770 O O     . ASP A 1 225 ? -37.53193 35.76891 -1.03562  1.000 96.39697  ? 229 ASP A O     1 
ATOM   1771 C CB    . ASP A 1 225 ? -35.35009 35.23126 -3.67775  1.000 100.97731 ? 229 ASP A CB    1 
ATOM   1772 C CG    . ASP A 1 225 ? -36.15932 34.42222 -4.71280  1.000 123.05848 ? 229 ASP A CG    1 
ATOM   1773 O OD1   . ASP A 1 225 ? -35.58529 34.19493 -5.80656  1.000 131.59651 ? 229 ASP A OD1   1 
ATOM   1774 O OD2   . ASP A 1 225 ? -37.29478 33.96557 -4.42977  1.000 119.70270 ? 229 ASP A OD2   1 
ATOM   1775 N N     . TYR A 1 226 ? -38.39855 35.38465 -3.07935  1.000 99.22487  ? 230 TYR A N     1 
ATOM   1776 C CA    . TYR A 1 226 ? -39.54993 34.70265 -2.52190  1.000 97.78089  ? 230 TYR A CA    1 
ATOM   1777 C C     . TYR A 1 226 ? -39.18674 33.30231 -2.04953  1.000 99.52921  ? 230 TYR A C     1 
ATOM   1778 O O     . TYR A 1 226 ? -39.63281 32.87907 -0.97243  1.000 96.75437  ? 230 TYR A O     1 
ATOM   1779 C CB    . TYR A 1 226 ? -40.68124 34.68311 -3.54215  1.000 98.91128  ? 230 TYR A CB    1 
ATOM   1780 C CG    . TYR A 1 226 ? -41.51488 35.93365 -3.43107  1.000 103.17294 ? 230 TYR A CG    1 
ATOM   1781 C CD1   . TYR A 1 226 ? -41.66312 36.80166 -4.50518  1.000 108.44013 ? 230 TYR A CD1   1 
ATOM   1782 C CD2   . TYR A 1 226 ? -42.12736 36.26806 -2.22602  1.000 95.11601  ? 230 TYR A CD2   1 
ATOM   1783 C CE1   . TYR A 1 226 ? -42.42314 37.96026 -4.39006  1.000 110.22845 ? 230 TYR A CE1   1 
ATOM   1784 C CE2   . TYR A 1 226 ? -42.88818 37.42528 -2.09818  1.000 93.72111  ? 230 TYR A CE2   1 
ATOM   1785 C CZ    . TYR A 1 226 ? -43.03633 38.26662 -3.18422  1.000 104.39577 ? 230 TYR A CZ    1 
ATOM   1786 O OH    . TYR A 1 226 ? -43.79299 39.41656 -3.06584  1.000 98.61753  ? 230 TYR A OH    1 
ATOM   1787 N N     . ILE A 1 227 ? -38.36530 32.56879 -2.82063  1.000 101.92184 ? 231 ILE A N     1 
ATOM   1788 C CA    . ILE A 1 227 ? -38.00128 31.21912 -2.37984  1.000 100.42035 ? 231 ILE A CA    1 
ATOM   1789 C C     . ILE A 1 227 ? -37.13895 31.30813 -1.13267  1.000 97.82456  ? 231 ILE A C     1 
ATOM   1790 O O     . ILE A 1 227 ? -37.23860 30.46464 -0.23216  1.000 97.73737  ? 231 ILE A O     1 
ATOM   1791 C CB    . ILE A 1 227 ? -37.32700 30.36973 -3.49465  1.000 110.32539 ? 231 ILE A CB    1 
ATOM   1792 C CG1   . ILE A 1 227 ? -36.26190 31.08270 -4.33750  1.000 108.29336 ? 231 ILE A CG1   1 
ATOM   1793 C CG2   . ILE A 1 227 ? -38.38330 29.68462 -4.40307  1.000 119.66949 ? 231 ILE A CG2   1 
ATOM   1794 C CD1   . ILE A 1 227 ? -34.93288 31.27993 -3.62213  1.000 113.60109 ? 231 ILE A CD1   1 
ATOM   1795 N N     . ASP A 1 228 ? -36.28399 32.33591 -1.05795  1.000 98.53345  ? 232 ASP A N     1 
ATOM   1796 C CA    . ASP A 1 228 ? -35.57055 32.62497 0.18176   1.000 94.07227  ? 232 ASP A CA    1 
ATOM   1797 C C     . ASP A 1 228 ? -36.54721 32.86253 1.32891   1.000 93.09153  ? 232 ASP A C     1 
ATOM   1798 O O     . ASP A 1 228 ? -36.38345 32.31757 2.42784   1.000 90.25922  ? 232 ASP A O     1 
ATOM   1799 C CB    . ASP A 1 228 ? -34.66483 33.84197 -0.01561  1.000 96.92843  ? 232 ASP A CB    1 
ATOM   1800 C CG    . ASP A 1 228 ? -33.34325 33.70899 0.72002   1.000 106.89631 ? 232 ASP A CG    1 
ATOM   1801 O OD1   . ASP A 1 228 ? -32.58353 32.75352 0.41128   1.000 105.59465 ? 232 ASP A OD1   1 
ATOM   1802 O OD2   . ASP A 1 228 ? -33.06389 34.56204 1.59152   1.000 110.85241 ? 232 ASP A OD2   1 
ATOM   1803 N N     . GLN A 1 229 ? -37.58280 33.66742 1.08325   1.000 86.50964  ? 233 GLN A N     1 
ATOM   1804 C CA    . GLN A 1 229 ? -38.46424 34.07041 2.16853   1.000 89.33309  ? 233 GLN A CA    1 
ATOM   1805 C C     . GLN A 1 229 ? -39.25747 32.89160 2.70795   1.000 88.76160  ? 233 GLN A C     1 
ATOM   1806 O O     . GLN A 1 229 ? -39.33691 32.69706 3.92689   1.000 86.76358  ? 233 GLN A O     1 
ATOM   1807 C CB    . GLN A 1 229 ? -39.39843 35.16678 1.68958   1.000 87.13495  ? 233 GLN A CB    1 
ATOM   1808 C CG    . GLN A 1 229 ? -40.18046 35.76536 2.80503   1.000 88.59727  ? 233 GLN A CG    1 
ATOM   1809 C CD    . GLN A 1 229 ? -40.68029 37.10735 2.42909   1.000 90.58688  ? 233 GLN A CD    1 
ATOM   1810 O OE1   . GLN A 1 229 ? -40.20321 37.69463 1.45744   1.000 95.38702  ? 233 GLN A OE1   1 
ATOM   1811 N NE2   . GLN A 1 229 ? -41.64439 37.61797 3.18151   1.000 90.80820  ? 233 GLN A NE2   1 
ATOM   1812 N N     . TRP A 1 230 ? -39.82607 32.08007 1.81416   1.000 87.75578  ? 234 TRP A N     1 
ATOM   1813 C CA    . TRP A 1 230 ? -40.52663 30.88204 2.25281   1.000 80.78645  ? 234 TRP A CA    1 
ATOM   1814 C C     . TRP A 1 230 ? -39.62986 30.00624 3.11507   1.000 84.94094  ? 234 TRP A C     1 
ATOM   1815 O O     . TRP A 1 230 ? -40.07603 29.46719 4.13423   1.000 85.53883  ? 234 TRP A O     1 
ATOM   1816 C CB    . TRP A 1 230 ? -41.03773 30.10456 1.04403   1.000 77.10471  ? 234 TRP A CB    1 
ATOM   1817 C CG    . TRP A 1 230 ? -41.71045 28.83147 1.41077   1.000 81.25223  ? 234 TRP A CG    1 
ATOM   1818 C CD1   . TRP A 1 230 ? -41.25594 27.56359 1.16668   1.000 84.43874  ? 234 TRP A CD1   1 
ATOM   1819 C CD2   . TRP A 1 230 ? -42.95607 28.68302 2.10053   1.000 77.73793  ? 234 TRP A CD2   1 
ATOM   1820 N NE1   . TRP A 1 230 ? -42.14803 26.63613 1.65643   1.000 82.68605  ? 234 TRP A NE1   1 
ATOM   1821 C CE2   . TRP A 1 230 ? -43.19864 27.29480 2.23573   1.000 78.39875  ? 234 TRP A CE2   1 
ATOM   1822 C CE3   . TRP A 1 230 ? -43.89146 29.58287 2.61335   1.000 79.46794  ? 234 TRP A CE3   1 
ATOM   1823 C CZ2   . TRP A 1 230 ? -44.33812 26.79112 2.86276   1.000 80.06941  ? 234 TRP A CZ2   1 
ATOM   1824 C CZ3   . TRP A 1 230 ? -45.02955 29.08141 3.24323   1.000 71.16420  ? 234 TRP A CZ3   1 
ATOM   1825 C CH2   . TRP A 1 230 ? -45.23773 27.70200 3.36331   1.000 79.13236  ? 234 TRP A CH2   1 
ATOM   1826 N N     . ASN A 1 231 ? -38.35166 29.87646 2.74591   1.000 87.45466  ? 235 ASN A N     1 
ATOM   1827 C CA    . ASN A 1 231 ? -37.45678 29.01969 3.52205   1.000 88.72793  ? 235 ASN A CA    1 
ATOM   1828 C C     . ASN A 1 231 ? -37.28422 29.53874 4.94698   1.000 88.25669  ? 235 ASN A C     1 
ATOM   1829 O O     . ASN A 1 231 ? -37.26824 28.75165 5.90310   1.000 87.67319  ? 235 ASN A O     1 
ATOM   1830 C CB    . ASN A 1 231 ? -36.10569 28.89345 2.82458   1.000 95.00354  ? 235 ASN A CB    1 
ATOM   1831 C CG    . ASN A 1 231 ? -36.08685 27.77437 1.78426   1.000 103.32390 ? 235 ASN A CG    1 
ATOM   1832 O OD1   . ASN A 1 231 ? -36.97013 26.90140 1.75721   1.000 102.27720 ? 235 ASN A OD1   1 
ATOM   1833 N ND2   . ASN A 1 231 ? -35.06014 27.77821 0.94297   1.000 102.22943 ? 235 ASN A ND2   1 
ATOM   1834 N N     . LYS A 1 232 ? -37.16731 30.86073 5.11213   1.000 86.84537  ? 236 LYS A N     1 
ATOM   1835 C CA    . LYS A 1 232 ? -37.11236 31.41788 6.45767   1.000 86.80600  ? 236 LYS A CA    1 
ATOM   1836 C C     . LYS A 1 232 ? -38.37937 31.09232 7.24456   1.000 86.58656  ? 236 LYS A C     1 
ATOM   1837 O O     . LYS A 1 232 ? -38.31523 30.80338 8.44530   1.000 90.01628  ? 236 LYS A O     1 
ATOM   1838 C CB    . LYS A 1 232 ? -36.87913 32.92776 6.40087   1.000 92.04417  ? 236 LYS A CB    1 
ATOM   1839 C CG    . LYS A 1 232 ? -35.40119 33.37136 6.51278   1.000 95.35055  ? 236 LYS A CG    1 
ATOM   1840 C CD    . LYS A 1 232 ? -34.64053 33.26437 5.17626   1.000 99.01566  ? 236 LYS A CD    1 
ATOM   1841 C CE    . LYS A 1 232 ? -33.12322 33.50397 5.33014   1.000 100.09175 ? 236 LYS A CE    1 
ATOM   1842 N NZ    . LYS A 1 232 ? -32.36517 32.35315 5.94055   1.000 100.70979 ? 236 LYS A NZ    1 
ATOM   1843 N N     . VAL A 1 233 ? -39.54178 31.12082 6.58989   1.000 84.41069  ? 237 VAL A N     1 
ATOM   1844 C CA    . VAL A 1 233 ? -40.78698 30.84458 7.30645   1.000 83.85055  ? 237 VAL A CA    1 
ATOM   1845 C C     . VAL A 1 233 ? -40.82426 29.39980 7.79998   1.000 86.00366  ? 237 VAL A C     1 
ATOM   1846 O O     . VAL A 1 233 ? -41.10052 29.13819 8.97675   1.000 86.23340  ? 237 VAL A O     1 
ATOM   1847 C CB    . VAL A 1 233 ? -42.01102 31.18092 6.43558   1.000 82.22305  ? 237 VAL A CB    1 
ATOM   1848 C CG1   . VAL A 1 233 ? -43.26840 31.08082 7.25907   1.000 72.89957  ? 237 VAL A CG1   1 
ATOM   1849 C CG2   . VAL A 1 233 ? -41.89157 32.59762 5.88490   1.000 80.66871  ? 237 VAL A CG2   1 
ATOM   1850 N N     . ILE A 1 234 ? -40.53479 28.44007 6.92058   1.000 87.64446  ? 238 ILE A N     1 
ATOM   1851 C CA    . ILE A 1 234 ? -40.64270 27.04575 7.33318   1.000 89.09869  ? 238 ILE A CA    1 
ATOM   1852 C C     . ILE A 1 234 ? -39.54840 26.68827 8.32143   1.000 90.94724  ? 238 ILE A C     1 
ATOM   1853 O O     . ILE A 1 234 ? -39.75526 25.84896 9.20550   1.000 93.84431  ? 238 ILE A O     1 
ATOM   1854 C CB    . ILE A 1 234 ? -40.63959 26.10893 6.11474   1.000 89.87592  ? 238 ILE A CB    1 
ATOM   1855 C CG1   . ILE A 1 234 ? -39.39928 26.35276 5.23995   1.000 88.17571  ? 238 ILE A CG1   1 
ATOM   1856 C CG2   . ILE A 1 234 ? -41.96026 26.27115 5.33707   1.000 84.00253  ? 238 ILE A CG2   1 
ATOM   1857 C CD1   . ILE A 1 234 ? -39.27069 25.37665 4.06795   1.000 88.94293  ? 238 ILE A CD1   1 
ATOM   1858 N N     . GLU A 1 235 ? -38.37246 27.30425 8.20212   1.000 91.51000  ? 239 GLU A N     1 
ATOM   1859 C CA    . GLU A 1 235 ? -37.31451 27.03857 9.17250   1.000 101.12748 ? 239 GLU A CA    1 
ATOM   1860 C C     . GLU A 1 235 ? -37.77531 27.37114 10.58914  1.000 101.02270 ? 239 GLU A C     1 
ATOM   1861 O O     . GLU A 1 235 ? -37.53304 26.60802 11.53568  1.000 100.54103 ? 239 GLU A O     1 
ATOM   1862 C CB    . GLU A 1 235 ? -36.06324 27.84188 8.82226   1.000 104.65236 ? 239 GLU A CB    1 
ATOM   1863 C CG    . GLU A 1 235 ? -34.83177 27.40123 9.60072   1.000 133.58563 ? 239 GLU A CG    1 
ATOM   1864 C CD    . GLU A 1 235 ? -33.62281 28.30799 9.39004   1.000 147.52527 ? 239 GLU A CD    1 
ATOM   1865 O OE1   . GLU A 1 235 ? -33.74204 29.30913 8.63768   1.000 139.27362 ? 239 GLU A OE1   1 
ATOM   1866 O OE2   . GLU A 1 235 ? -32.55140 28.00344 9.97871   1.000 140.10116 ? 239 GLU A OE2   1 
ATOM   1867 N N     . GLN A 1 236 ? -38.45864 28.50470 10.74594  1.000 92.35853  ? 240 GLN A N     1 
ATOM   1868 C CA    . GLN A 1 236 ? -38.78535 29.03043 12.06109  1.000 90.88376  ? 240 GLN A CA    1 
ATOM   1869 C C     . GLN A 1 236 ? -40.11184 28.50148 12.59022  1.000 90.15623  ? 240 GLN A C     1 
ATOM   1870 O O     . GLN A 1 236 ? -40.22899 28.23666 13.79486  1.000 92.91822  ? 240 GLN A O     1 
ATOM   1871 C CB    . GLN A 1 236 ? -38.79489 30.56295 12.01740  1.000 92.18275  ? 240 GLN A CB    1 
ATOM   1872 C CG    . GLN A 1 236 ? -37.46561 31.17515 11.54266  1.000 105.74745 ? 240 GLN A CG    1 
ATOM   1873 C CD    . GLN A 1 236 ? -36.89132 32.20245 12.51668  1.000 114.14784 ? 240 GLN A CD    1 
ATOM   1874 O OE1   . GLN A 1 236 ? -35.88316 31.94595 13.19872  1.000 118.29181 ? 240 GLN A OE1   1 
ATOM   1875 N NE2   . GLN A 1 236 ? -37.52758 33.37720 12.58090  1.000 104.13387 ? 240 GLN A NE2   1 
ATOM   1876 N N     . LEU A 1 237 ? -41.11004 28.33706 11.71111  1.000 89.58847  ? 241 LEU A N     1 
ATOM   1877 C CA    . LEU A 1 237 ? -42.44270 27.87250 12.08971  1.000 79.48994  ? 241 LEU A CA    1 
ATOM   1878 C C     . LEU A 1 237 ? -42.68684 26.40700 11.76235  1.000 86.11144  ? 241 LEU A C     1 
ATOM   1879 O O     . LEU A 1 237 ? -43.47816 25.75703 12.44904  1.000 94.36997  ? 241 LEU A O     1 
ATOM   1880 C CB    . LEU A 1 237 ? -43.52315 28.72939 11.40384  1.000 81.73720  ? 241 LEU A CB    1 
ATOM   1881 C CG    . LEU A 1 237 ? -43.40327 30.25094 11.61502  1.000 78.27648  ? 241 LEU A CG    1 
ATOM   1882 C CD1   . LEU A 1 237 ? -44.56506 31.03657 11.01353  1.000 69.20039  ? 241 LEU A CD1   1 
ATOM   1883 C CD2   . LEU A 1 237 ? -43.26022 30.56263 13.09339  1.000 74.33445  ? 241 LEU A CD2   1 
ATOM   1884 N N     . GLY A 1 238 ? -42.03141 25.86742 10.75030  1.000 88.25851  ? 242 GLY A N     1 
ATOM   1885 C CA    . GLY A 1 238 ? -42.16863 24.45407 10.46049  1.000 85.67210  ? 242 GLY A CA    1 
ATOM   1886 C C     . GLY A 1 238 ? -42.94934 24.21392 9.17686   1.000 89.06457  ? 242 GLY A C     1 
ATOM   1887 O O     . GLY A 1 238 ? -43.79537 25.02029 8.77065   1.000 92.98176  ? 242 GLY A O     1 
ATOM   1888 N N     . THR A 1 239 ? -42.66071 23.08269 8.53360   1.000 89.27750  ? 243 THR A N     1 
ATOM   1889 C CA    . THR A 1 239 ? -43.39147 22.66552 7.34466   1.000 89.12256  ? 243 THR A CA    1 
ATOM   1890 C C     . THR A 1 239 ? -44.87612 22.56080 7.68468   1.000 90.39571  ? 243 THR A C     1 
ATOM   1891 O O     . THR A 1 239 ? -45.22759 21.99480 8.73129   1.000 91.11473  ? 243 THR A O     1 
ATOM   1892 C CB    . THR A 1 239 ? -42.85632 21.31372 6.83481   1.000 90.34965  ? 243 THR A CB    1 
ATOM   1893 O OG1   . THR A 1 239 ? -41.53581 21.47360 6.29757   1.000 96.67480  ? 243 THR A OG1   1 
ATOM   1894 C CG2   . THR A 1 239 ? -43.75292 20.71955 5.75087   1.000 87.39253  ? 243 THR A CG2   1 
ATOM   1895 N N     . PRO A 1 240 ? -45.76662 23.11393 6.86556   1.000 94.13359  ? 244 PRO A N     1 
ATOM   1896 C CA    . PRO A 1 240 ? -47.18872 23.13641 7.21764   1.000 87.24887  ? 244 PRO A CA    1 
ATOM   1897 C C     . PRO A 1 240 ? -47.85570 21.79059 6.94717   1.000 93.59126  ? 244 PRO A C     1 
ATOM   1898 O O     . PRO A 1 240 ? -47.30310 20.91108 6.28543   1.000 96.39240  ? 244 PRO A O     1 
ATOM   1899 C CB    . PRO A 1 240 ? -47.74516 24.24621 6.32288   1.000 81.90196  ? 244 PRO A CB    1 
ATOM   1900 C CG    . PRO A 1 240 ? -46.86510 24.24357 5.13105   1.000 77.50029  ? 244 PRO A CG    1 
ATOM   1901 C CD    . PRO A 1 240 ? -45.49868 23.81851 5.59740   1.000 94.06836  ? 244 PRO A CD    1 
ATOM   1902 N N     . CYS A 1 241 ? -49.06838 21.64347 7.49178   1.000 97.36196  ? 245 CYS A N     1 
ATOM   1903 C CA    . CYS A 1 241 ? -49.77010 20.36346 7.47667   1.000 95.39834  ? 245 CYS A CA    1 
ATOM   1904 C C     . CYS A 1 241 ? -50.13971 19.95809 6.04985   1.000 99.85768  ? 245 CYS A C     1 
ATOM   1905 O O     . CYS A 1 241 ? -50.32114 20.81665 5.17937   1.000 99.81878  ? 245 CYS A O     1 
ATOM   1906 C CB    . CYS A 1 241 ? -51.03133 20.44160 8.33598   1.000 96.09461  ? 245 CYS A CB    1 
ATOM   1907 S SG    . CYS A 1 241 ? -50.77179 21.20625 9.96167   1.000 120.51017 ? 245 CYS A SG    1 
ATOM   1908 N N     . PRO A 1 242 ? -50.26124 18.65140 5.78263   1.000 104.23497 ? 246 PRO A N     1 
ATOM   1909 C CA    . PRO A 1 242 ? -50.58678 18.20950 4.40754   1.000 105.61118 ? 246 PRO A CA    1 
ATOM   1910 C C     . PRO A 1 242 ? -51.92625 18.71733 3.88770   1.000 104.33672 ? 246 PRO A C     1 
ATOM   1911 O O     . PRO A 1 242 ? -52.09775 18.81431 2.66570   1.000 102.31016 ? 246 PRO A O     1 
ATOM   1912 C CB    . PRO A 1 242 ? -50.55976 16.67206 4.49343   1.000 101.60073 ? 246 PRO A CB    1 
ATOM   1913 C CG    . PRO A 1 242 ? -50.45568 16.31921 5.94370   1.000 102.75222 ? 246 PRO A CG    1 
ATOM   1914 C CD    . PRO A 1 242 ? -50.02160 17.52856 6.71342   1.000 102.84191 ? 246 PRO A CD    1 
ATOM   1915 N N     . GLU A 1 243 ? -52.88210 19.05206 4.75725   1.000 113.51750 ? 247 GLU A N     1 
ATOM   1916 C CA    . GLU A 1 243 ? -54.10985 19.65800 4.25594   1.000 108.69363 ? 247 GLU A CA    1 
ATOM   1917 C C     . GLU A 1 243 ? -53.84062 21.03197 3.66066   1.000 106.14836 ? 247 GLU A C     1 
ATOM   1918 O O     . GLU A 1 243 ? -54.42720 21.39913 2.63486   1.000 112.65880 ? 247 GLU A O     1 
ATOM   1919 C CB    . GLU A 1 243 ? -55.15843 19.74674 5.35929   1.000 122.25937 ? 247 GLU A CB    1 
ATOM   1920 C CG    . GLU A 1 243 ? -56.56789 19.55236 4.81712   1.000 132.58529 ? 247 GLU A CG    1 
ATOM   1921 C CD    . GLU A 1 243 ? -56.89509 18.09621 4.51315   1.000 137.40760 ? 247 GLU A CD    1 
ATOM   1922 O OE1   . GLU A 1 243 ? -56.25125 17.50110 3.61205   1.000 132.20014 ? 247 GLU A OE1   1 
ATOM   1923 O OE2   . GLU A 1 243 ? -57.81428 17.55240 5.16902   1.000 136.92729 ? 247 GLU A OE2   1 
ATOM   1924 N N     . PHE A 1 244 ? -52.95210 21.80246 4.28398   1.000 95.18343  ? 248 PHE A N     1 
ATOM   1925 C CA    . PHE A 1 244 ? -52.56006 23.06498 3.68413   1.000 87.69430  ? 248 PHE A CA    1 
ATOM   1926 C C     . PHE A 1 244 ? -51.87834 22.86566 2.33489   1.000 88.78552  ? 248 PHE A C     1 
ATOM   1927 O O     . PHE A 1 244 ? -51.91162 23.76616 1.49215   1.000 85.70275  ? 248 PHE A O     1 
ATOM   1928 C CB    . PHE A 1 244 ? -51.64971 23.83076 4.63332   1.000 84.88287  ? 248 PHE A CB    1 
ATOM   1929 C CG    . PHE A 1 244 ? -51.11818 25.10019 4.04942   1.000 85.00295  ? 248 PHE A CG    1 
ATOM   1930 C CD1   . PHE A 1 244 ? -51.84356 26.28478 4.15946   1.000 79.92700  ? 248 PHE A CD1   1 
ATOM   1931 C CD2   . PHE A 1 244 ? -49.89370 25.11954 3.38646   1.000 75.05387  ? 248 PHE A CD2   1 
ATOM   1932 C CE1   . PHE A 1 244 ? -51.35415 27.47354 3.62657   1.000 74.97027  ? 248 PHE A CE1   1 
ATOM   1933 C CE2   . PHE A 1 244 ? -49.40276 26.30102 2.84006   1.000 74.78522  ? 248 PHE A CE2   1 
ATOM   1934 C CZ    . PHE A 1 244 ? -50.13438 27.48660 2.96775   1.000 75.14091  ? 248 PHE A CZ    1 
ATOM   1935 N N     . MET A 1 245 ? -51.24262 21.70900 2.11298   1.000 93.11988  ? 249 MET A N     1 
ATOM   1936 C CA    . MET A 1 245 ? -50.55473 21.45931 0.84252   1.000 90.54205  ? 249 MET A CA    1 
ATOM   1937 C C     . MET A 1 245 ? -51.52663 21.23016 -0.31689  1.000 90.72572  ? 249 MET A C     1 
ATOM   1938 O O     . MET A 1 245 ? -51.18383 21.52156 -1.47251  1.000 83.76643  ? 249 MET A O     1 
ATOM   1939 C CB    . MET A 1 245 ? -49.63920 20.23989 0.95382   1.000 104.12143 ? 249 MET A CB    1 
ATOM   1940 C CG    . MET A 1 245 ? -48.58593 20.27549 2.04591   1.000 102.10956 ? 249 MET A CG    1 
ATOM   1941 S SD    . MET A 1 245 ? -47.20600 21.36333 1.67606   1.000 104.54600 ? 249 MET A SD    1 
ATOM   1942 C CE    . MET A 1 245 ? -46.01296 20.79122 2.89986   1.000 96.49394  ? 249 MET A CE    1 
ATOM   1943 N N     . LYS A 1 246 ? -52.72302 20.69367 -0.03556  1.000 90.73092  ? 250 LYS A N     1 
ATOM   1944 C CA    . LYS A 1 246 ? -53.70814 20.43062 -1.08841  1.000 94.97362  ? 250 LYS A CA    1 
ATOM   1945 C C     . LYS A 1 246 ? -54.11331 21.70593 -1.82304  1.000 92.02590  ? 250 LYS A C     1 
ATOM   1946 O O     . LYS A 1 246 ? -54.33253 21.68769 -3.04185  1.000 85.50937  ? 250 LYS A O     1 
ATOM   1947 C CB    . LYS A 1 246 ? -54.95452 19.77304 -0.49211  1.000 94.12568  ? 250 LYS A CB    1 
ATOM   1948 C CG    . LYS A 1 246 ? -54.67003 18.71200 0.54444   1.000 102.05477 ? 250 LYS A CG    1 
ATOM   1949 C CD    . LYS A 1 246 ? -53.86304 17.57376 -0.05168  1.000 104.19241 ? 250 LYS A CD    1 
ATOM   1950 C CE    . LYS A 1 246 ? -54.70700 16.32528 -0.21372  1.000 105.07078 ? 250 LYS A CE    1 
ATOM   1951 N NZ    . LYS A 1 246 ? -54.06156 15.36311 -1.14887  1.000 108.51969 ? 250 LYS A NZ    1 
ATOM   1952 N N     . LYS A 1 247 ? -54.23788 22.81841 -1.09244  1.000 86.87184  ? 251 LYS A N     1 
ATOM   1953 C CA    . LYS A 1 247 ? -54.74361 24.06229 -1.66385  1.000 82.52139  ? 251 LYS A CA    1 
ATOM   1954 C C     . LYS A 1 247 ? -53.81749 24.64373 -2.72574  1.000 78.21736  ? 251 LYS A C     1 
ATOM   1955 O O     . LYS A 1 247 ? -54.23830 25.52384 -3.48146  1.000 87.26837  ? 251 LYS A O     1 
ATOM   1956 C CB    . LYS A 1 247 ? -54.94013 25.10329 -0.56193  1.000 80.83746  ? 251 LYS A CB    1 
ATOM   1957 C CG    . LYS A 1 247 ? -55.67789 24.62466 0.69055   1.000 79.21650  ? 251 LYS A CG    1 
ATOM   1958 C CD    . LYS A 1 247 ? -55.49012 25.69261 1.77380   1.000 77.97346  ? 251 LYS A CD    1 
ATOM   1959 C CE    . LYS A 1 247 ? -56.04559 25.27433 3.12420   1.000 89.62216  ? 251 LYS A CE    1 
ATOM   1960 N NZ    . LYS A 1 247 ? -56.23258 26.51822 3.93702   1.000 77.60714  ? 251 LYS A NZ    1 
ATOM   1961 N N     . LEU A 1 248 ? -52.57105 24.19545 -2.78360  1.000 79.58340  ? 252 LEU A N     1 
ATOM   1962 C CA    . LEU A 1 248 ? -51.60648 24.72890 -3.73293  1.000 80.36463  ? 252 LEU A CA    1 
ATOM   1963 C C     . LEU A 1 248 ? -51.84045 24.21707 -5.15239  1.000 85.64358  ? 252 LEU A C     1 
ATOM   1964 O O     . LEU A 1 248 ? -52.31304 23.09976 -5.37333  1.000 87.08326  ? 252 LEU A O     1 
ATOM   1965 C CB    . LEU A 1 248 ? -50.19580 24.37905 -3.26910  1.000 86.04943  ? 252 LEU A CB    1 
ATOM   1966 C CG    . LEU A 1 248 ? -49.28713 25.47683 -2.71430  1.000 90.17026  ? 252 LEU A CG    1 
ATOM   1967 C CD1   . LEU A 1 248 ? -49.80894 26.14871 -1.45544  1.000 72.99298  ? 252 LEU A CD1   1 
ATOM   1968 C CD2   . LEU A 1 248 ? -47.94178 24.80483 -2.42577  1.000 91.98846  ? 252 LEU A CD2   1 
ATOM   1969 N N     . GLN A 1 249 ? -51.50189 25.06775 -6.12005  1.000 87.93235  ? 253 GLN A N     1 
ATOM   1970 C CA    . GLN A 1 249 ? -51.46086 24.65744 -7.51416  1.000 90.05385  ? 253 GLN A CA    1 
ATOM   1971 C C     . GLN A 1 249 ? -50.34912 23.61827 -7.69626  1.000 90.86582  ? 253 GLN A C     1 
ATOM   1972 O O     . GLN A 1 249 ? -49.34515 23.65543 -6.98022  1.000 92.88849  ? 253 GLN A O     1 
ATOM   1973 C CB    . GLN A 1 249 ? -51.24441 25.89718 -8.40687  1.000 89.07718  ? 253 GLN A CB    1 
ATOM   1974 C CG    . GLN A 1 249 ? -50.97660 25.70188 -9.92987  1.000 104.73574 ? 253 GLN A CG    1 
ATOM   1975 C CD    . GLN A 1 249 ? -49.56120 25.20697 -10.33201 1.000 97.46873  ? 253 GLN A CD    1 
ATOM   1976 O OE1   . GLN A 1 249 ? -48.64717 25.13343 -9.50873  1.000 104.45590 ? 253 GLN A OE1   1 
ATOM   1977 N NE2   . GLN A 1 249 ? -49.39616 24.87285 -11.61755 1.000 75.40737  ? 253 GLN A NE2   1 
ATOM   1978 N N     . PRO A 1 250 ? -50.51802 22.66099 -8.64308  1.000 89.33098  ? 254 PRO A N     1 
ATOM   1979 C CA    . PRO A 1 250 ? -49.51205 21.59369 -8.85095  1.000 93.14483  ? 254 PRO A CA    1 
ATOM   1980 C C     . PRO A 1 250 ? -48.02769 21.97615 -8.79344  1.000 101.14894 ? 254 PRO A C     1 
ATOM   1981 O O     . PRO A 1 250 ? -47.28728 21.38698 -7.99085  1.000 99.97394  ? 254 PRO A O     1 
ATOM   1982 C CB    . PRO A 1 250 ? -49.86743 21.07302 -10.24916 1.000 81.61863  ? 254 PRO A CB    1 
ATOM   1983 C CG    . PRO A 1 250 ? -51.38504 21.32194 -10.37014 1.000 94.69651  ? 254 PRO A CG    1 
ATOM   1984 C CD    . PRO A 1 250 ? -51.79331 22.32644 -9.30313  1.000 84.73628  ? 254 PRO A CD    1 
ATOM   1985 N N     . THR A 1 251 ? -47.55757 22.91487 -9.63702  1.000 100.56818 ? 255 THR A N     1 
ATOM   1986 C CA    . THR A 1 251 ? -46.11441 23.19311 -9.68008  1.000 98.79279  ? 255 THR A CA    1 
ATOM   1987 C C     . THR A 1 251 ? -45.63249 23.84794 -8.38974  1.000 98.13322  ? 255 THR A C     1 
ATOM   1988 O O     . THR A 1 251 ? -44.59598 23.45636 -7.83847  1.000 98.02943  ? 255 THR A O     1 
ATOM   1989 C CB    . THR A 1 251 ? -45.73383 24.05982 -10.89286 1.000 90.87327  ? 255 THR A CB    1 
ATOM   1990 O OG1   . THR A 1 251 ? -45.91377 25.44851 -10.58828 1.000 106.27923 ? 255 THR A OG1   1 
ATOM   1991 C CG2   . THR A 1 251 ? -46.53171 23.68014 -12.13877 1.000 90.71253  ? 255 THR A CG2   1 
ATOM   1992 N N     . VAL A 1 252 ? -46.37346 24.83845 -7.88793  1.000 98.68922  ? 256 VAL A N     1 
ATOM   1993 C CA    . VAL A 1 252 ? -46.06184 25.39132 -6.57435  1.000 98.24692  ? 256 VAL A CA    1 
ATOM   1994 C C     . VAL A 1 252 ? -46.12543 24.28485 -5.52676  1.000 97.34493  ? 256 VAL A C     1 
ATOM   1995 O O     . VAL A 1 252 ? -45.27871 24.21081 -4.62629  1.000 95.34405  ? 256 VAL A O     1 
ATOM   1996 C CB    . VAL A 1 252 ? -47.01105 26.56491 -6.24870  1.000 95.98469  ? 256 VAL A CB    1 
ATOM   1997 C CG1   . VAL A 1 252 ? -46.74656 27.11031 -4.85061  1.000 83.70482  ? 256 VAL A CG1   1 
ATOM   1998 C CG2   . VAL A 1 252 ? -46.89132 27.68171 -7.31014  1.000 96.18852  ? 256 VAL A CG2   1 
ATOM   1999 N N     . ARG A 1 253 ? -47.10019 23.37611 -5.66787  1.000 101.38528 ? 257 ARG A N     1 
ATOM   2000 C CA    . ARG A 1 253 ? -47.25743 22.26973 -4.72659  1.000 100.69876 ? 257 ARG A CA    1 
ATOM   2001 C C     . ARG A 1 253 ? -46.03712 21.35218 -4.73189  1.000 104.90930 ? 257 ARG A C     1 
ATOM   2002 O O     . ARG A 1 253 ? -45.50598 21.00867 -3.66786  1.000 103.25086 ? 257 ARG A O     1 
ATOM   2003 C CB    . ARG A 1 253 ? -48.53690 21.48900 -5.04333  1.000 92.82855  ? 257 ARG A CB    1 
ATOM   2004 C CG    . ARG A 1 253 ? -49.09897 20.70820 -3.88105  1.000 95.25350  ? 257 ARG A CG    1 
ATOM   2005 C CD    . ARG A 1 253 ? -50.19774 19.76445 -4.33808  1.000 90.18221  ? 257 ARG A CD    1 
ATOM   2006 N NE    . ARG A 1 253 ? -50.70484 18.96193 -3.22880  1.000 98.28759  ? 257 ARG A NE    1 
ATOM   2007 C CZ    . ARG A 1 253 ? -50.40803 17.67949 -3.03299  1.000 107.71850 ? 257 ARG A CZ    1 
ATOM   2008 N NH1   . ARG A 1 253 ? -49.60610 17.01869 -3.85547  1.000 112.24433 ? 257 ARG A NH1   1 
ATOM   2009 N NH2   . ARG A 1 253 ? -50.92140 17.04143 -1.98131  1.000 103.91592 ? 257 ARG A NH2   1 
ATOM   2010 N N     . THR A 1 254 ? -45.55457 20.96450 -5.91864  1.000 110.54824 ? 258 THR A N     1 
ATOM   2011 C CA    . THR A 1 254 ? -44.41473 20.04760 -5.95892  1.000 125.60988 ? 258 THR A CA    1 
ATOM   2012 C C     . THR A 1 254 ? -43.18679 20.66665 -5.29830  1.000 122.63629 ? 258 THR A C     1 
ATOM   2013 O O     . THR A 1 254 ? -42.44554 19.97889 -4.58418  1.000 128.77713 ? 258 THR A O     1 
ATOM   2014 C CB    . THR A 1 254 ? -44.08740 19.60664 -7.39878  1.000 125.13719 ? 258 THR A CB    1 
ATOM   2015 O OG1   . THR A 1 254 ? -43.61470 20.71705 -8.17443  1.000 133.16085 ? 258 THR A OG1   1 
ATOM   2016 C CG2   . THR A 1 254 ? -45.29371 18.94883 -8.08387  1.000 123.50658 ? 258 THR A CG2   1 
ATOM   2017 N N     . TYR A 1 255 ? -42.96021 21.96730 -5.50933  1.000 114.56931 ? 259 TYR A N     1 
ATOM   2018 C CA    . TYR A 1 255 ? -41.75928 22.59329 -4.95850  1.000 118.29944 ? 259 TYR A CA    1 
ATOM   2019 C C     . TYR A 1 255 ? -41.83323 22.73255 -3.44202  1.000 113.68692 ? 259 TYR A C     1 
ATOM   2020 O O     . TYR A 1 255 ? -40.81009 22.61602 -2.75338  1.000 112.00382 ? 259 TYR A O     1 
ATOM   2021 C CB    . TYR A 1 255 ? -41.52830 23.96300 -5.59204  1.000 115.96306 ? 259 TYR A CB    1 
ATOM   2022 C CG    . TYR A 1 255 ? -40.44170 24.73276 -4.88361  1.000 115.19866 ? 259 TYR A CG    1 
ATOM   2023 C CD1   . TYR A 1 255 ? -39.11314 24.31596 -4.95900  1.000 117.52569 ? 259 TYR A CD1   1 
ATOM   2024 C CD2   . TYR A 1 255 ? -40.73927 25.85986 -4.12699  1.000 110.36814 ? 259 TYR A CD2   1 
ATOM   2025 C CE1   . TYR A 1 255 ? -38.11154 25.00536 -4.31214  1.000 114.53668 ? 259 TYR A CE1   1 
ATOM   2026 C CE2   . TYR A 1 255 ? -39.74259 26.56017 -3.47549  1.000 115.22095 ? 259 TYR A CE2   1 
ATOM   2027 C CZ    . TYR A 1 255 ? -38.42572 26.12946 -3.57503  1.000 114.00827 ? 259 TYR A CZ    1 
ATOM   2028 O OH    . TYR A 1 255 ? -37.42550 26.81852 -2.92958  1.000 103.86936 ? 259 TYR A OH    1 
ATOM   2029 N N     . VAL A 1 256 ? -43.02577 23.00082 -2.91280  1.000 111.99779 ? 260 VAL A N     1 
ATOM   2030 C CA    . VAL A 1 256 ? -43.19627 23.16120 -1.47448  1.000 105.94649 ? 260 VAL A CA    1 
ATOM   2031 C C     . VAL A 1 256 ? -43.11154 21.81420 -0.75089  1.000 105.86268 ? 260 VAL A C     1 
ATOM   2032 O O     . VAL A 1 256 ? -42.59209 21.73846 0.37024   1.000 105.03053 ? 260 VAL A O     1 
ATOM   2033 C CB    . VAL A 1 256 ? -44.52805 23.88444 -1.20977  1.000 94.02687  ? 260 VAL A CB    1 
ATOM   2034 C CG1   . VAL A 1 256 ? -45.00491 23.64778 0.20983   1.000 84.30913  ? 260 VAL A CG1   1 
ATOM   2035 C CG2   . VAL A 1 256 ? -44.39818 25.38652 -1.52598  1.000 93.87602  ? 260 VAL A CG2   1 
ATOM   2036 N N     . GLU A 1 257 ? -43.61079 20.74023 -1.36917  1.000 105.42314 ? 261 GLU A N     1 
ATOM   2037 C CA    . GLU A 1 257 ? -43.52317 19.41259 -0.77261  1.000 108.09697 ? 261 GLU A CA    1 
ATOM   2038 C C     . GLU A 1 257 ? -42.13115 18.79865 -0.89201  1.000 108.30265 ? 261 GLU A C     1 
ATOM   2039 O O     . GLU A 1 257 ? -41.81799 17.87061 -0.13910  1.000 107.59286 ? 261 GLU A O     1 
ATOM   2040 C CB    . GLU A 1 257 ? -44.55305 18.48563 -1.41941  1.000 103.89329 ? 261 GLU A CB    1 
ATOM   2041 C CG    . GLU A 1 257 ? -45.95441 18.66991 -0.87670  1.000 104.70486 ? 261 GLU A CG    1 
ATOM   2042 C CD    . GLU A 1 257 ? -46.99052 17.89174 -1.66720  1.000 109.41689 ? 261 GLU A CD    1 
ATOM   2043 O OE1   . GLU A 1 257 ? -46.64289 17.33560 -2.73871  1.000 112.03098 ? 261 GLU A OE1   1 
ATOM   2044 O OE2   . GLU A 1 257 ? -48.15546 17.84362 -1.21496  1.000 107.35552 ? 261 GLU A OE2   1 
ATOM   2045 N N     . ASN A 1 258 ? -41.30483 19.28575 -1.82401  1.000 109.21576 ? 262 ASN A N     1 
ATOM   2046 C CA    . ASN A 1 258 ? -39.93994 18.81233 -2.03094  1.000 111.06504 ? 262 ASN A CA    1 
ATOM   2047 C C     . ASN A 1 258 ? -38.92298 19.54175 -1.16973  1.000 114.25503 ? 262 ASN A C     1 
ATOM   2048 O O     . ASN A 1 258 ? -37.73866 19.18485 -1.19652  1.000 115.57348 ? 262 ASN A O     1 
ATOM   2049 C CB    . ASN A 1 258 ? -39.53622 18.96225 -3.50202  1.000 112.96994 ? 262 ASN A CB    1 
ATOM   2050 C CG    . ASN A 1 258 ? -40.01170 17.80696 -4.35506  1.000 125.74298 ? 262 ASN A CG    1 
ATOM   2051 O OD1   . ASN A 1 258 ? -40.76562 16.94663 -3.89048  1.000 125.32524 ? 262 ASN A OD1   1 
ATOM   2052 N ND2   . ASN A 1 258 ? -39.56638 17.77347 -5.61183  1.000 129.71811 ? 262 ASN A ND2   1 
ATOM   2053 N N     . ARG A 1 259 ? -39.34606 20.56630 -0.43753  1.000 108.49656 ? 263 ARG A N     1 
ATOM   2054 C CA    . ARG A 1 259 ? -38.44620 21.23543 0.47546   1.000 108.48353 ? 263 ARG A CA    1 
ATOM   2055 C C     . ARG A 1 259 ? -38.08499 20.29225 1.61893   1.000 113.77174 ? 263 ARG A C     1 
ATOM   2056 O O     . ARG A 1 259 ? -38.84385 19.37167 1.93895   1.000 117.46686 ? 263 ARG A O     1 
ATOM   2057 C CB    . ARG A 1 259 ? -39.08840 22.50410 1.03701   1.000 109.95465 ? 263 ARG A CB    1 
ATOM   2058 C CG    . ARG A 1 259 ? -39.47951 23.53981 -0.01505  1.000 109.11325 ? 263 ARG A CG    1 
ATOM   2059 C CD    . ARG A 1 259 ? -38.36480 23.76129 -1.03865  1.000 112.98447 ? 263 ARG A CD    1 
ATOM   2060 N NE    . ARG A 1 259 ? -37.15049 24.28308 -0.42596  1.000 110.68179 ? 263 ARG A NE    1 
ATOM   2061 C CZ    . ARG A 1 259 ? -35.94072 23.76388 -0.59503  1.000 111.19164 ? 263 ARG A CZ    1 
ATOM   2062 N NH1   . ARG A 1 259 ? -35.74486 22.69599 -1.35326  1.000 113.58340 ? 263 ARG A NH1   1 
ATOM   2063 N NH2   . ARG A 1 259 ? -34.90247 24.32384 0.02159   1.000 100.59764 ? 263 ARG A NH2   1 
ATOM   2064 N N     . PRO A 1 260 ? -36.91785 20.47761 2.22817   1.000 114.25031 ? 264 PRO A N     1 
ATOM   2065 C CA    . PRO A 1 260 ? -36.60611 19.72648 3.44764   1.000 118.72734 ? 264 PRO A CA    1 
ATOM   2066 C C     . PRO A 1 260 ? -37.65848 20.00740 4.51027   1.000 111.98329 ? 264 PRO A C     1 
ATOM   2067 O O     . PRO A 1 260 ? -38.01314 21.16010 4.76209   1.000 112.09928 ? 264 PRO A O     1 
ATOM   2068 C CB    . PRO A 1 260 ? -35.22754 20.26487 3.85329   1.000 121.14758 ? 264 PRO A CB    1 
ATOM   2069 C CG    . PRO A 1 260 ? -34.65373 20.82845 2.60293   1.000 117.39894 ? 264 PRO A CG    1 
ATOM   2070 C CD    . PRO A 1 260 ? -35.81693 21.36732 1.82874   1.000 112.45676 ? 264 PRO A CD    1 
ATOM   2071 N N     . LYS A 1 261 ? -38.16450 18.94192 5.12804   1.000 113.87630 ? 265 LYS A N     1 
ATOM   2072 C CA    . LYS A 1 261 ? -39.20994 19.06613 6.14316   1.000 110.49710 ? 265 LYS A CA    1 
ATOM   2073 C C     . LYS A 1 261 ? -38.60385 19.58732 7.44049   1.000 111.64792 ? 265 LYS A C     1 
ATOM   2074 O O     . LYS A 1 261 ? -38.03961 18.81904 8.22344   1.000 114.41162 ? 265 LYS A O     1 
ATOM   2075 C CB    . LYS A 1 261 ? -39.89385 17.72268 6.37538   1.000 111.41799 ? 265 LYS A CB    1 
ATOM   2076 C CG    . LYS A 1 261 ? -40.94026 17.35695 5.33118   1.000 116.94580 ? 265 LYS A CG    1 
ATOM   2077 C CD    . LYS A 1 261 ? -40.29986 16.84993 4.04834   1.000 120.54660 ? 265 LYS A CD    1 
ATOM   2078 C CE    . LYS A 1 261 ? -41.34606 16.30854 3.09293   1.000 119.91840 ? 265 LYS A CE    1 
ATOM   2079 N NZ    . LYS A 1 261 ? -40.74330 15.94397 1.78245   1.000 119.73405 ? 265 LYS A NZ    1 
ATOM   2080 N N     . TYR A 1 262 ? -38.72463 20.89386 7.68198   1.000 108.43126 ? 266 TYR A N     1 
ATOM   2081 C CA    . TYR A 1 262 ? -38.33251 21.46245 8.96452   1.000 104.75524 ? 266 TYR A CA    1 
ATOM   2082 C C     . TYR A 1 262 ? -39.44324 21.27189 9.99400   1.000 102.64339 ? 266 TYR A C     1 
ATOM   2083 O O     . TYR A 1 262 ? -40.62267 21.12706 9.65946   1.000 102.86542 ? 266 TYR A O     1 
ATOM   2084 C CB    . TYR A 1 262 ? -38.00998 22.95197 8.84715   1.000 100.89496 ? 266 TYR A CB    1 
ATOM   2085 C CG    . TYR A 1 262 ? -36.94855 23.27399 7.83433   1.000 104.20597 ? 266 TYR A CG    1 
ATOM   2086 C CD1   . TYR A 1 262 ? -35.60543 23.03594 8.10410   1.000 104.88908 ? 266 TYR A CD1   1 
ATOM   2087 C CD2   . TYR A 1 262 ? -37.28487 23.83592 6.61208   1.000 102.16817 ? 266 TYR A CD2   1 
ATOM   2088 C CE1   . TYR A 1 262 ? -34.63247 23.33275 7.17274   1.000 108.25647 ? 266 TYR A CE1   1 
ATOM   2089 C CE2   . TYR A 1 262 ? -36.32232 24.13861 5.67909   1.000 108.22295 ? 266 TYR A CE2   1 
ATOM   2090 C CZ    . TYR A 1 262 ? -35.00095 23.88492 5.96021   1.000 107.20754 ? 266 TYR A CZ    1 
ATOM   2091 O OH    . TYR A 1 262 ? -34.05470 24.18874 5.01440   1.000 116.14119 ? 266 TYR A OH    1 
ATOM   2092 N N     . ALA A 1 263 ? -39.04831 21.28939 11.26662  1.000 104.35324 ? 267 ALA A N     1 
ATOM   2093 C CA    . ALA A 1 263 ? -39.97217 21.04662 12.36626  1.000 99.28208  ? 267 ALA A CA    1 
ATOM   2094 C C     . ALA A 1 263 ? -40.53507 22.32439 12.97620  1.000 100.42630 ? 267 ALA A C     1 
ATOM   2095 O O     . ALA A 1 263 ? -41.64249 22.30377 13.53043  1.000 100.69367 ? 267 ALA A O     1 
ATOM   2096 C CB    . ALA A 1 263 ? -39.27538 20.22932 13.46059  1.000 96.67982  ? 267 ALA A CB    1 
ATOM   2097 N N     . GLY A 1 264 ? -39.80331 23.43200 12.89007  1.000 101.99223 ? 268 GLY A N     1 
ATOM   2098 C CA    . GLY A 1 264 ? -40.23785 24.65848 13.51731  1.000 97.28276  ? 268 GLY A CA    1 
ATOM   2099 C C     . GLY A 1 264 ? -39.83829 24.65413 14.97324  1.000 101.39291 ? 268 GLY A C     1 
ATOM   2100 O O     . GLY A 1 264 ? -39.65483 23.59370 15.57834  1.000 100.90089 ? 268 GLY A O     1 
ATOM   2101 N N     . TYR A 1 265 ? -39.67567 25.82795 15.55038  1.000 101.30631 ? 269 TYR A N     1 
ATOM   2102 C CA    . TYR A 1 265 ? -39.37481 25.89817 16.96736  1.000 104.92758 ? 269 TYR A CA    1 
ATOM   2103 C C     . TYR A 1 265 ? -40.60600 26.31912 17.75442  1.000 102.06412 ? 269 TYR A C     1 
ATOM   2104 O O     . TYR A 1 265 ? -41.58077 26.84579 17.21127  1.000 98.59936  ? 269 TYR A O     1 
ATOM   2105 C CB    . TYR A 1 265 ? -38.23080 26.87215 17.22787  1.000 106.53772 ? 269 TYR A CB    1 
ATOM   2106 C CG    . TYR A 1 265 ? -37.00488 26.58402 16.40117  1.000 112.33726 ? 269 TYR A CG    1 
ATOM   2107 C CD1   . TYR A 1 265 ? -36.75837 27.28751 15.22711  1.000 113.20562 ? 269 TYR A CD1   1 
ATOM   2108 C CD2   . TYR A 1 265 ? -36.08423 25.62712 16.80287  1.000 114.44670 ? 269 TYR A CD2   1 
ATOM   2109 C CE1   . TYR A 1 265 ? -35.63515 27.03315 14.46825  1.000 114.28049 ? 269 TYR A CE1   1 
ATOM   2110 C CE2   . TYR A 1 265 ? -34.96081 25.36526 16.05419  1.000 123.09110 ? 269 TYR A CE2   1 
ATOM   2111 C CZ    . TYR A 1 265 ? -34.73662 26.06879 14.88729  1.000 126.18328 ? 269 TYR A CZ    1 
ATOM   2112 O OH    . TYR A 1 265 ? -33.60491 25.79694 14.14187  1.000 122.58330 ? 269 TYR A OH    1 
ATOM   2113 N N     . SER A 1 266 ? -40.54566 26.07094 19.05524  1.000 98.67298  ? 270 SER A N     1 
ATOM   2114 C CA    . SER A 1 266 ? -41.55877 26.57719 19.95407  1.000 103.72042 ? 270 SER A CA    1 
ATOM   2115 C C     . SER A 1 266 ? -41.61239 28.10437 19.87880  1.000 103.57843 ? 270 SER A C     1 
ATOM   2116 O O     . SER A 1 266 ? -40.70828 28.76492 19.35302  1.000 99.04137  ? 270 SER A O     1 
ATOM   2117 C CB    . SER A 1 266 ? -41.25347 26.13109 21.38043  1.000 106.51134 ? 270 SER A CB    1 
ATOM   2118 O OG    . SER A 1 266 ? -42.25850 26.58086 22.25852  1.000 119.68332 ? 270 SER A OG    1 
ATOM   2119 N N     . PHE A 1 267 ? -42.69595 28.67408 20.41122  1.000 100.18518 ? 271 PHE A N     1 
ATOM   2120 C CA    . PHE A 1 267 ? -42.76392 30.12840 20.49975  1.000 96.39247  ? 271 PHE A CA    1 
ATOM   2121 C C     . PHE A 1 267 ? -42.05035 30.67298 21.72552  1.000 103.25155 ? 271 PHE A C     1 
ATOM   2122 O O     . PHE A 1 267 ? -41.75643 31.87655 21.77471  1.000 97.48551  ? 271 PHE A O     1 
ATOM   2123 C CB    . PHE A 1 267 ? -44.21351 30.58955 20.48300  1.000 97.49849  ? 271 PHE A CB    1 
ATOM   2124 C CG    . PHE A 1 267 ? -44.72961 30.81646 19.11232  1.000 85.79938  ? 271 PHE A CG    1 
ATOM   2125 C CD1   . PHE A 1 267 ? -44.53151 32.03256 18.47970  1.000 78.34570  ? 271 PHE A CD1   1 
ATOM   2126 C CD2   . PHE A 1 267 ? -45.34811 29.78482 18.42555  1.000 79.95323  ? 271 PHE A CD2   1 
ATOM   2127 C CE1   . PHE A 1 267 ? -44.98060 32.22494 17.20237  1.000 79.64068  ? 271 PHE A CE1   1 
ATOM   2128 C CE2   . PHE A 1 267 ? -45.80869 29.97123 17.15028  1.000 81.25404  ? 271 PHE A CE2   1 
ATOM   2129 C CZ    . PHE A 1 267 ? -45.62434 31.19001 16.52940  1.000 80.23074  ? 271 PHE A CZ    1 
ATOM   2130 N N     . GLU A 1 268 ? -41.78723 29.81086 22.70987  1.000 108.31581 ? 272 GLU A N     1 
ATOM   2131 C CA    . GLU A 1 268 ? -40.85418 30.13409 23.77984  1.000 106.58072 ? 272 GLU A CA    1 
ATOM   2132 C C     . GLU A 1 268 ? -39.43846 30.18652 23.23745  1.000 104.31151 ? 272 GLU A C     1 
ATOM   2133 O O     . GLU A 1 268 ? -38.68249 31.11871 23.53129  1.000 103.92593 ? 272 GLU A O     1 
ATOM   2134 C CB    . GLU A 1 268 ? -40.95377 29.08799 24.89825  1.000 109.65392 ? 272 GLU A CB    1 
ATOM   2135 C CG    . GLU A 1 268 ? -42.36165 28.80622 25.48879  1.000 118.30011 ? 272 GLU A CG    1 
ATOM   2136 C CD    . GLU A 1 268 ? -43.39660 28.24547 24.49049  1.000 127.99243 ? 272 GLU A CD    1 
ATOM   2137 O OE1   . GLU A 1 268 ? -43.13201 28.21215 23.26472  1.000 123.13487 ? 272 GLU A OE1   1 
ATOM   2138 O OE2   . GLU A 1 268 ? -44.49140 27.83260 24.93684  1.000 134.05321 ? 272 GLU A OE2   1 
ATOM   2139 N N     . LYS A 1 269 ? -39.07239 29.19457 22.42479  1.000 110.01598 ? 273 LYS A N     1 
ATOM   2140 C CA    . LYS A 1 269 ? -37.76475 29.18333 21.78543  1.000 109.45902 ? 273 LYS A CA    1 
ATOM   2141 C C     . LYS A 1 269 ? -37.61576 30.32284 20.77824  1.000 108.91601 ? 273 LYS A C     1 
ATOM   2142 O O     . LYS A 1 269 ? -36.48777 30.73412 20.48371  1.000 115.91232 ? 273 LYS A O     1 
ATOM   2143 C CB    . LYS A 1 269 ? -37.54829 27.82340 21.11225  1.000 110.89018 ? 273 LYS A CB    1 
ATOM   2144 C CG    . LYS A 1 269 ? -36.11338 27.28946 21.15185  1.000 124.84083 ? 273 LYS A CG    1 
ATOM   2145 C CD    . LYS A 1 269 ? -35.20392 27.95020 20.10685  1.000 129.96791 ? 273 LYS A CD    1 
ATOM   2146 C CE    . LYS A 1 269 ? -33.79639 27.34684 20.11974  1.000 126.12160 ? 273 LYS A CE    1 
ATOM   2147 N NZ    . LYS A 1 269 ? -32.89598 28.01064 19.13309  1.000 126.01602 ? 273 LYS A NZ    1 
ATOM   2148 N N     . LEU A 1 270 ? -38.72159 30.85482 20.25520  1.000 100.49463 ? 274 LEU A N     1 
ATOM   2149 C CA    . LEU A 1 270 ? -38.64306 31.92295 19.27039  1.000 98.74690  ? 274 LEU A CA    1 
ATOM   2150 C C     . LEU A 1 270 ? -38.72213 33.31448 19.89342  1.000 97.07133  ? 274 LEU A C     1 
ATOM   2151 O O     . LEU A 1 270 ? -38.29956 34.28691 19.25111  1.000 93.40511  ? 274 LEU A O     1 
ATOM   2152 C CB    . LEU A 1 270 ? -39.76551 31.76979 18.23211  1.000 94.47425  ? 274 LEU A CB    1 
ATOM   2153 C CG    . LEU A 1 270 ? -39.53938 30.73447 17.12841  1.000 94.66404  ? 274 LEU A CG    1 
ATOM   2154 C CD1   . LEU A 1 270 ? -40.81362 30.53072 16.34818  1.000 85.66417  ? 274 LEU A CD1   1 
ATOM   2155 C CD2   . LEU A 1 270 ? -38.39469 31.14694 16.20816  1.000 101.86332 ? 274 LEU A CD2   1 
ATOM   2156 N N     . PHE A 1 271 ? -39.26569 33.42602 21.11384  1.000 99.12879  ? 275 PHE A N     1 
ATOM   2157 C CA    . PHE A 1 271 ? -39.42576 34.71242 21.80030  1.000 94.03076  ? 275 PHE A CA    1 
ATOM   2158 C C     . PHE A 1 271 ? -39.29235 34.51357 23.30647  1.000 100.52523 ? 275 PHE A C     1 
ATOM   2159 O O     . PHE A 1 271 ? -40.26649 34.68311 24.05710  1.000 99.55615  ? 275 PHE A O     1 
ATOM   2160 C CB    . PHE A 1 271 ? -40.78624 35.33634 21.49063  1.000 86.71159  ? 275 PHE A CB    1 
ATOM   2161 C CG    . PHE A 1 271 ? -41.05945 35.53059 20.04360  1.000 85.54007  ? 275 PHE A CG    1 
ATOM   2162 C CD1   . PHE A 1 271 ? -40.45861 36.57319 19.34560  1.000 83.74772  ? 275 PHE A CD1   1 
ATOM   2163 C CD2   . PHE A 1 271 ? -41.97190 34.71647 19.38704  1.000 82.19935  ? 275 PHE A CD2   1 
ATOM   2164 C CE1   . PHE A 1 271 ? -40.71828 36.77352 18.01028  1.000 80.92654  ? 275 PHE A CE1   1 
ATOM   2165 C CE2   . PHE A 1 271 ? -42.24361 34.91730 18.04864  1.000 80.73021  ? 275 PHE A CE2   1 
ATOM   2166 C CZ    . PHE A 1 271 ? -41.61334 35.95439 17.36174  1.000 81.10928  ? 275 PHE A CZ    1 
ATOM   2167 N N     . PRO A 1 272 ? -38.08609 34.20686 23.79436  1.000 102.18183 ? 276 PRO A N     1 
ATOM   2168 C CA    . PRO A 1 272 ? -37.91395 33.92498 25.22708  1.000 104.06917 ? 276 PRO A CA    1 
ATOM   2169 C C     . PRO A 1 272 ? -38.07332 35.16932 26.08794  1.000 105.23483 ? 276 PRO A C     1 
ATOM   2170 O O     . PRO A 1 272 ? -38.00218 36.30497 25.61319  1.000 105.03397 ? 276 PRO A O     1 
ATOM   2171 C CB    . PRO A 1 272 ? -36.48135 33.37339 25.33083  1.000 106.48468 ? 276 PRO A CB    1 
ATOM   2172 C CG    . PRO A 1 272 ? -35.90379 33.40151 23.93910  1.000 100.36355 ? 276 PRO A CG    1 
ATOM   2173 C CD    . PRO A 1 272 ? -36.79812 34.23651 23.07763  1.000 101.87984 ? 276 PRO A CD    1 
ATOM   2174 N N     . ASP A 1 273 ? -38.26107 34.92081 27.39059  1.000 105.62950 ? 277 ASP A N     1 
ATOM   2175 C CA    . ASP A 1 273 ? -38.52976 35.99544 28.34283  1.000 112.68053 ? 277 ASP A CA    1 
ATOM   2176 C C     . ASP A 1 273 ? -37.47498 37.09490 28.29437  1.000 113.35333 ? 277 ASP A C     1 
ATOM   2177 O O     . ASP A 1 273 ? -37.76504 38.24698 28.64204  1.000 116.67593 ? 277 ASP A O     1 
ATOM   2178 C CB    . ASP A 1 273 ? -38.60545 35.42933 29.76351  1.000 120.28509 ? 277 ASP A CB    1 
ATOM   2179 C CG    . ASP A 1 273 ? -39.53343 34.24348 29.86975  1.000 122.13192 ? 277 ASP A CG    1 
ATOM   2180 O OD1   . ASP A 1 273 ? -40.52305 34.33858 30.62881  1.000 126.09751 ? 277 ASP A OD1   1 
ATOM   2181 O OD2   . ASP A 1 273 ? -39.26152 33.21540 29.20995  1.000 122.12206 ? 277 ASP A OD2   1 
ATOM   2182 N N     . VAL A 1 274 ? -36.25206 36.76115 27.86861  1.000 111.37774 ? 278 VAL A N     1 
ATOM   2183 C CA    . VAL A 1 274 ? -35.15413 37.72618 27.89327  1.000 112.90933 ? 278 VAL A CA    1 
ATOM   2184 C C     . VAL A 1 274 ? -35.44731 38.91648 26.99426  1.000 107.68364 ? 278 VAL A C     1 
ATOM   2185 O O     . VAL A 1 274 ? -35.10186 40.05875 27.32754  1.000 109.76156 ? 278 VAL A O     1 
ATOM   2186 C CB    . VAL A 1 274 ? -33.83864 37.04318 27.49370  1.000 111.22246 ? 278 VAL A CB    1 
ATOM   2187 C CG1   . VAL A 1 274 ? -32.66369 37.99997 27.71192  1.000 105.50339 ? 278 VAL A CG1   1 
ATOM   2188 C CG2   . VAL A 1 274 ? -33.68149 35.74653 28.26600  1.000 110.77401 ? 278 VAL A CG2   1 
ATOM   2189 N N     . LEU A 1 275 ? -36.05901 38.67295 25.82834  1.000 106.36231 ? 279 LEU A N     1 
ATOM   2190 C CA    . LEU A 1 275 ? -36.34764 39.78000 24.92244  1.000 104.35359 ? 279 LEU A CA    1 
ATOM   2191 C C     . LEU A 1 275 ? -37.48715 40.65387 25.42441  1.000 104.99411 ? 279 LEU A C     1 
ATOM   2192 O O     . LEU A 1 275 ? -37.61678 41.80505 24.97838  1.000 103.70060 ? 279 LEU A O     1 
ATOM   2193 C CB    . LEU A 1 275 ? -36.69645 39.27429 23.52642  1.000 101.57251 ? 279 LEU A CB    1 
ATOM   2194 C CG    . LEU A 1 275 ? -35.71457 38.33942 22.82140  1.000 107.36097 ? 279 LEU A CG    1 
ATOM   2195 C CD1   . LEU A 1 275 ? -36.49140 37.49641 21.80113  1.000 104.47850 ? 279 LEU A CD1   1 
ATOM   2196 C CD2   . LEU A 1 275 ? -34.57485 39.11609 22.16677  1.000 88.91793  ? 279 LEU A CD2   1 
ATOM   2197 N N     . PHE A 1 276 ? -38.36062 40.10128 26.35320  1.000 104.41547 ? 280 PHE A N     1 
ATOM   2198 C CA    . PHE A 1 276 ? -39.48483 40.83152 26.91377  1.000 103.30836 ? 280 PHE A CA    1 
ATOM   2199 C C     . PHE A 1 276 ? -39.05703 41.62008 28.14267  1.000 103.53806 ? 280 PHE A C     1 
ATOM   2200 O O     . PHE A 1 276 ? -38.18175 41.18428 28.89742  1.000 113.11276 ? 280 PHE A O     1 
ATOM   2201 C CB    . PHE A 1 276 ? -40.61991 39.87783 27.27970  1.000 101.15765 ? 280 PHE A CB    1 
ATOM   2202 C CG    . PHE A 1 276 ? -41.42521 39.43470 26.09599  1.000 91.65010  ? 280 PHE A CG    1 
ATOM   2203 C CD1   . PHE A 1 276 ? -42.38355 40.27380 25.54110  1.000 91.34370  ? 280 PHE A CD1   1 
ATOM   2204 C CD2   . PHE A 1 276 ? -41.21502 38.18441 25.52364  1.000 95.86711  ? 280 PHE A CD2   1 
ATOM   2205 C CE1   . PHE A 1 276 ? -43.12510 39.87799 24.43246  1.000 85.03898  ? 280 PHE A CE1   1 
ATOM   2206 C CE2   . PHE A 1 276 ? -41.95647 37.77569 24.41351  1.000 97.38655  ? 280 PHE A CE2   1 
ATOM   2207 C CZ    . PHE A 1 276 ? -42.91180 38.62842 23.86635  1.000 83.75444  ? 280 PHE A CZ    1 
ATOM   2208 N N     . PRO A 1 277 ? -39.67518 42.77103 28.37042  1.000 106.48826 ? 281 PRO A N     1 
ATOM   2209 C CA    . PRO A 1 277 ? -39.32019 43.57212 29.53478  1.000 108.62372 ? 281 PRO A CA    1 
ATOM   2210 C C     . PRO A 1 277 ? -39.76228 42.87642 30.80387  1.000 122.81280 ? 281 PRO A C     1 
ATOM   2211 O O     . PRO A 1 277 ? -40.43807 41.83899 30.77834  1.000 123.89116 ? 281 PRO A O     1 
ATOM   2212 C CB    . PRO A 1 277 ? -40.10718 44.86057 29.31768  1.000 108.70816 ? 281 PRO A CB    1 
ATOM   2213 C CG    . PRO A 1 277 ? -41.33861 44.37173 28.65380  1.000 103.68435 ? 281 PRO A CG    1 
ATOM   2214 C CD    . PRO A 1 277 ? -40.86830 43.30820 27.69719  1.000 102.00032 ? 281 PRO A CD    1 
ATOM   2215 N N     . ALA A 1 278 ? -39.36718 43.47916 31.92305  1.000 133.95008 ? 282 ALA A N     1 
ATOM   2216 C CA    . ALA A 1 278 ? -39.81977 43.04587 33.23468  1.000 145.76700 ? 282 ALA A CA    1 
ATOM   2217 C C     . ALA A 1 278 ? -41.31593 42.75835 33.20746  1.000 158.01078 ? 282 ALA A C     1 
ATOM   2218 O O     . ALA A 1 278 ? -42.10821 43.51873 32.63822  1.000 143.16858 ? 282 ALA A O     1 
ATOM   2219 C CB    . ALA A 1 278 ? -39.49225 44.11030 34.28361  1.000 140.82894 ? 282 ALA A CB    1 
ATOM   2220 N N     . ASP A 1 279 ? -41.68432 41.62104 33.77717  1.000 158.83362 ? 283 ASP A N     1 
ATOM   2221 C CA    . ASP A 1 279 ? -43.05858 41.16165 33.70700  1.000 150.01196 ? 283 ASP A CA    1 
ATOM   2222 C C     . ASP A 1 279 ? -43.94170 41.98811 34.63578  1.000 155.13839 ? 283 ASP A C     1 
ATOM   2223 O O     . ASP A 1 279 ? -43.67443 42.07733 35.83901  1.000 161.81117 ? 283 ASP A O     1 
ATOM   2224 C CB    . ASP A 1 279 ? -43.10415 39.68166 34.07067  1.000 148.17612 ? 283 ASP A CB    1 
ATOM   2225 C CG    . ASP A 1 279 ? -44.39168 39.04471 33.68594  1.000 142.89632 ? 283 ASP A CG    1 
ATOM   2226 O OD1   . ASP A 1 279 ? -45.40200 39.39520 34.31524  1.000 147.03562 ? 283 ASP A OD1   1 
ATOM   2227 O OD2   . ASP A 1 279 ? -44.40514 38.23025 32.74100  1.000 138.95414 ? 283 ASP A OD2   1 
ATOM   2228 N N     . SER A 1 280 ? -45.00146 42.58023 34.07688  1.000 153.78726 ? 284 SER A N     1 
ATOM   2229 C CA    . SER A 1 280 ? -45.89450 43.43631 34.85016  1.000 158.73141 ? 284 SER A CA    1 
ATOM   2230 C C     . SER A 1 280 ? -46.56599 42.65697 35.97506  1.000 166.86458 ? 284 SER A C     1 
ATOM   2231 O O     . SER A 1 280 ? -46.62022 41.42366 35.97466  1.000 164.25193 ? 284 SER A O     1 
ATOM   2232 C CB    . SER A 1 280 ? -46.98511 44.05478 33.96284  1.000 148.69883 ? 284 SER A CB    1 
ATOM   2233 O OG    . SER A 1 280 ? -46.46075 44.99358 33.04456  1.000 137.92970 ? 284 SER A OG    1 
ATOM   2234 N N     . GLU A 1 281 ? -47.06402 43.40239 36.96223  1.000 180.53997 ? 285 GLU A N     1 
ATOM   2235 C CA    . GLU A 1 281 ? -47.95967 42.81511 37.94810  1.000 183.71509 ? 285 GLU A CA    1 
ATOM   2236 C C     . GLU A 1 281 ? -49.38421 42.71246 37.42560  1.000 182.18040 ? 285 GLU A C     1 
ATOM   2237 O O     . GLU A 1 281 ? -50.19765 41.99194 38.01559  1.000 183.97559 ? 285 GLU A O     1 
ATOM   2238 C CB    . GLU A 1 281 ? -47.93553 43.62785 39.24620  1.000 185.55676 ? 285 GLU A CB    1 
ATOM   2239 C CG    . GLU A 1 281 ? -46.53823 43.85726 39.78083  1.000 180.35520 ? 285 GLU A CG    1 
ATOM   2240 C CD    . GLU A 1 281 ? -45.77536 42.55918 39.96341  1.000 183.31429 ? 285 GLU A CD    1 
ATOM   2241 O OE1   . GLU A 1 281 ? -46.19084 41.74033 40.80906  1.000 185.54031 ? 285 GLU A OE1   1 
ATOM   2242 O OE2   . GLU A 1 281 ? -44.76979 42.34710 39.25052  1.000 180.35186 ? 285 GLU A OE2   1 
ATOM   2243 N N     . HIS A 1 282 ? -49.69279 43.41942 36.33844  1.000 175.51624 ? 286 HIS A N     1 
ATOM   2244 C CA    . HIS A 1 282 ? -50.98344 43.28860 35.67636  1.000 170.78331 ? 286 HIS A CA    1 
ATOM   2245 C C     . HIS A 1 282 ? -51.17291 41.88536 35.10172  1.000 168.73816 ? 286 HIS A C     1 
ATOM   2246 O O     . HIS A 1 282 ? -50.36086 41.42125 34.29654  1.000 160.62597 ? 286 HIS A O     1 
ATOM   2247 C CB    . HIS A 1 282 ? -51.08738 44.32775 34.56478  1.000 161.48851 ? 286 HIS A CB    1 
ATOM   2248 C CG    . HIS A 1 282 ? -52.48622 44.56527 34.09694  1.000 164.29092 ? 286 HIS A CG    1 
ATOM   2249 N ND1   . HIS A 1 282 ? -52.91482 44.20939 32.83612  1.000 167.04378 ? 286 HIS A ND1   1 
ATOM   2250 C CD2   . HIS A 1 282 ? -53.55708 45.11169 34.72082  1.000 162.09369 ? 286 HIS A CD2   1 
ATOM   2251 C CE1   . HIS A 1 282 ? -54.18959 44.52699 32.70359  1.000 163.80913 ? 286 HIS A CE1   1 
ATOM   2252 N NE2   . HIS A 1 282 ? -54.60273 45.07818 33.83095  1.000 159.56281 ? 286 HIS A NE2   1 
ATOM   2253 N N     . ASN A 1 283 ? -52.29218 41.23845 35.46462  1.000 171.84997 ? 287 ASN A N     1 
ATOM   2254 C CA    . ASN A 1 283 ? -52.54227 39.82504 35.17006  1.000 163.09790 ? 287 ASN A CA    1 
ATOM   2255 C C     . ASN A 1 283 ? -52.74413 39.53095 33.68575  1.000 153.00923 ? 287 ASN A C     1 
ATOM   2256 O O     . ASN A 1 283 ? -52.91449 38.35788 33.32994  1.000 151.49926 ? 287 ASN A O     1 
ATOM   2257 C CB    . ASN A 1 283 ? -53.77052 39.32226 35.94091  1.000 163.97710 ? 287 ASN A CB    1 
ATOM   2258 C CG    . ASN A 1 283 ? -53.74148 39.69919 37.41352  1.000 169.34399 ? 287 ASN A CG    1 
ATOM   2259 O OD1   . ASN A 1 283 ? -52.81157 39.35041 38.14407  1.000 170.16232 ? 287 ASN A OD1   1 
ATOM   2260 N ND2   . ASN A 1 283 ? -54.77346 40.40718 37.85857  1.000 172.69212 ? 287 ASN A ND2   1 
ATOM   2261 N N     . LYS A 1 284 ? -52.73990 40.54513 32.82051  1.000 144.17431 ? 288 LYS A N     1 
ATOM   2262 C CA    . LYS A 1 284 ? -52.91676 40.34787 31.38661  1.000 136.85716 ? 288 LYS A CA    1 
ATOM   2263 C C     . LYS A 1 284 ? -51.69744 40.74121 30.55941  1.000 122.93671 ? 288 LYS A C     1 
ATOM   2264 O O     . LYS A 1 284 ? -51.47091 40.14859 29.50130  1.000 111.22401 ? 288 LYS A O     1 
ATOM   2265 C CB    . LYS A 1 284 ? -54.14909 41.13294 30.89655  1.000 136.90812 ? 288 LYS A CB    1 
ATOM   2266 C CG    . LYS A 1 284 ? -55.45177 40.79244 31.65842  1.000 137.52723 ? 288 LYS A CG    1 
ATOM   2267 C CD    . LYS A 1 284 ? -56.65690 41.68101 31.27351  1.000 126.81360 ? 288 LYS A CD    1 
ATOM   2268 C CE    . LYS A 1 284 ? -57.20891 41.38249 29.87062  1.000 122.47239 ? 288 LYS A CE    1 
ATOM   2269 N NZ    . LYS A 1 284 ? -58.42267 42.19531 29.51722  1.000 122.70913 ? 288 LYS A NZ    1 
ATOM   2270 N N     . LEU A 1 285 ? -50.90073 41.71079 31.01867  1.000 124.45141 ? 289 LEU A N     1 
ATOM   2271 C CA    . LEU A 1 285 ? -49.72986 42.18561 30.27141  1.000 106.30400 ? 289 LEU A CA    1 
ATOM   2272 C C     . LEU A 1 285 ? -48.46667 41.40250 30.66659  1.000 108.47768 ? 289 LEU A C     1 
ATOM   2273 O O     . LEU A 1 285 ? -47.47216 41.94561 31.16288  1.000 109.05732 ? 289 LEU A O     1 
ATOM   2274 C CB    . LEU A 1 285 ? -49.55823 43.68571 30.47922  1.000 109.50591 ? 289 LEU A CB    1 
ATOM   2275 C CG    . LEU A 1 285 ? -50.78416 44.56056 30.16531  1.000 111.82457 ? 289 LEU A CG    1 
ATOM   2276 C CD1   . LEU A 1 285 ? -50.68778 45.95697 30.80800  1.000 105.93592 ? 289 LEU A CD1   1 
ATOM   2277 C CD2   . LEU A 1 285 ? -51.00542 44.68765 28.66437  1.000 90.35504  ? 289 LEU A CD2   1 
ATOM   2278 N N     . LYS A 1 286 ? -48.52791 40.09185 30.41117  1.000 109.97518 ? 290 LYS A N     1 
ATOM   2279 C CA    . LYS A 1 286 ? -47.47388 39.10704 30.63614  1.000 101.52027 ? 290 LYS A CA    1 
ATOM   2280 C C     . LYS A 1 286 ? -46.62647 38.92492 29.37489  1.000 92.70610  ? 290 LYS A C     1 
ATOM   2281 O O     . LYS A 1 286 ? -47.09214 39.12952 28.24989  1.000 85.21611  ? 290 LYS A O     1 
ATOM   2282 C CB    . LYS A 1 286 ? -48.07413 37.73322 30.99820  1.000 104.71891 ? 290 LYS A CB    1 
ATOM   2283 C CG    . LYS A 1 286 ? -48.75632 37.53677 32.35576  1.000 110.95928 ? 290 LYS A CG    1 
ATOM   2284 C CD    . LYS A 1 286 ? -47.95147 38.11994 33.47002  1.000 122.62910 ? 290 LYS A CD    1 
ATOM   2285 C CE    . LYS A 1 286 ? -48.82829 38.84917 34.46830  1.000 138.75449 ? 290 LYS A CE    1 
ATOM   2286 N NZ    . LYS A 1 286 ? -48.07417 39.90434 35.21851  1.000 152.07804 ? 290 LYS A NZ    1 
ATOM   2287 N N     . ALA A 1 287 ? -45.38963 38.45207 29.56160  1.000 96.60229  ? 291 ALA A N     1 
ATOM   2288 C CA    . ALA A 1 287 ? -44.64575 37.93876 28.41058  1.000 90.58517  ? 291 ALA A CA    1 
ATOM   2289 C C     . ALA A 1 287 ? -45.36515 36.73646 27.78948  1.000 91.93651  ? 291 ALA A C     1 
ATOM   2290 O O     . ALA A 1 287 ? -45.43592 36.60563 26.55517  1.000 86.00028  ? 291 ALA A O     1 
ATOM   2291 C CB    . ALA A 1 287 ? -43.21479 37.57784 28.82160  1.000 90.66046  ? 291 ALA A CB    1 
ATOM   2292 N N     . SER A 1 288 ? -45.93847 35.86660 28.63790  1.000 94.05253  ? 292 SER A N     1 
ATOM   2293 C CA    . SER A 1 288 ? -46.64710 34.66806 28.18496  1.000 85.83210  ? 292 SER A CA    1 
ATOM   2294 C C     . SER A 1 288 ? -47.89605 34.98001 27.37749  1.000 88.92718  ? 292 SER A C     1 
ATOM   2295 O O     . SER A 1 288 ? -48.35614 34.11801 26.61984  1.000 87.82516  ? 292 SER A O     1 
ATOM   2296 C CB    . SER A 1 288 ? -47.07091 33.81040 29.37480  1.000 81.54120  ? 292 SER A CB    1 
ATOM   2297 O OG    . SER A 1 288 ? -48.16773 34.39612 30.05077  1.000 88.44578  ? 292 SER A OG    1 
ATOM   2298 N N     . GLN A 1 289 ? -48.48018 36.16976 27.55597  1.000 90.75199  ? 293 GLN A N     1 
ATOM   2299 C CA    . GLN A 1 289 ? -49.64532 36.56581 26.77447  1.000 85.47367  ? 293 GLN A CA    1 
ATOM   2300 C C     . GLN A 1 289 ? -49.23906 37.15608 25.43678  1.000 80.07437  ? 293 GLN A C     1 
ATOM   2301 O O     . GLN A 1 289 ? -49.86666 36.86520 24.41169  1.000 74.89175  ? 293 GLN A O     1 
ATOM   2302 C CB    . GLN A 1 289 ? -50.48583 37.57470 27.55510  1.000 86.69941  ? 293 GLN A CB    1 
ATOM   2303 C CG    . GLN A 1 289 ? -51.09817 37.01763 28.81073  1.000 92.93760  ? 293 GLN A CG    1 
ATOM   2304 C CD    . GLN A 1 289 ? -52.47657 36.45109 28.56039  1.000 102.67497 ? 293 GLN A CD    1 
ATOM   2305 O OE1   . GLN A 1 289 ? -52.69011 35.64833 27.63691  1.000 94.65892  ? 293 GLN A OE1   1 
ATOM   2306 N NE2   . GLN A 1 289 ? -53.42927 36.86425 29.38604  1.000 110.47956 ? 293 GLN A NE2   1 
ATOM   2307 N N     . ALA A 1 290 ? -48.20299 37.99624 25.41763  1.000 78.82268  ? 294 ALA A N     1 
ATOM   2308 C CA    . ALA A 1 290 ? -47.77212 38.52754 24.13279  1.000 76.69311  ? 294 ALA A CA    1 
ATOM   2309 C C     . ALA A 1 290 ? -47.35680 37.38646 23.22391  1.000 82.80301  ? 294 ALA A C     1 
ATOM   2310 O O     . ALA A 1 290 ? -47.69462 37.37582 22.03180  1.000 78.12095  ? 294 ALA A O     1 
ATOM   2311 C CB    . ALA A 1 290 ? -46.63303 39.52383 24.32454  1.000 76.06774  ? 294 ALA A CB    1 
ATOM   2312 N N     . ARG A 1 291 ? -46.67266 36.38640 23.80177  1.000 81.90463  ? 295 ARG A N     1 
ATOM   2313 C CA    . ARG A 1 291 ? -46.23556 35.20601 23.06268  1.000 77.32269  ? 295 ARG A CA    1 
ATOM   2314 C C     . ARG A 1 291 ? -47.42270 34.42355 22.52102  1.000 81.22038  ? 295 ARG A C     1 
ATOM   2315 O O     . ARG A 1 291 ? -47.42961 33.99744 21.35818  1.000 78.37977  ? 295 ARG A O     1 
ATOM   2316 C CB    . ARG A 1 291 ? -45.40437 34.31444 23.98360  1.000 81.49381  ? 295 ARG A CB    1 
ATOM   2317 C CG    . ARG A 1 291 ? -44.28749 33.57259 23.29775  1.000 91.97089  ? 295 ARG A CG    1 
ATOM   2318 C CD    . ARG A 1 291 ? -43.63128 32.60899 24.27831  1.000 98.78594  ? 295 ARG A CD    1 
ATOM   2319 N NE    . ARG A 1 291 ? -42.67726 33.29617 25.13889  1.000 94.83509  ? 295 ARG A NE    1 
ATOM   2320 C CZ    . ARG A 1 291 ? -42.76990 33.33336 26.46070  1.000 95.03629  ? 295 ARG A CZ    1 
ATOM   2321 N NH1   . ARG A 1 291 ? -43.71383 32.66206 27.10537  1.000 90.83358  ? 295 ARG A NH1   1 
ATOM   2322 N NH2   . ARG A 1 291 ? -41.89579 34.06093 27.15379  1.000 98.02199  ? 295 ARG A NH2   1 
ATOM   2323 N N     . ASP A 1 292 ? -48.43071 34.20767 23.37030  1.000 78.10926  ? 296 ASP A N     1 
ATOM   2324 C CA    . ASP A 1 292 ? -49.65361 33.53452 22.94507  1.000 79.12294  ? 296 ASP A CA    1 
ATOM   2325 C C     . ASP A 1 292 ? -50.27723 34.23036 21.72866  1.000 83.15429  ? 296 ASP A C     1 
ATOM   2326 O O     . ASP A 1 292 ? -50.66093 33.57371 20.75079  1.000 86.23573  ? 296 ASP A O     1 
ATOM   2327 C CB    . ASP A 1 292 ? -50.64081 33.49828 24.11906  1.000 82.12649  ? 296 ASP A CB    1 
ATOM   2328 C CG    . ASP A 1 292 ? -51.95279 32.81318 23.76761  1.000 91.65175  ? 296 ASP A CG    1 
ATOM   2329 O OD1   . ASP A 1 292 ? -53.01704 33.47738 23.87178  1.000 94.48502  ? 296 ASP A OD1   1 
ATOM   2330 O OD2   . ASP A 1 292 ? -51.92264 31.59757 23.44061  1.000 99.96211  ? 296 ASP A OD2   1 
ATOM   2331 N N     . LEU A 1 293 ? -50.36062 35.56578 21.76340  1.000 77.34527  ? 297 LEU A N     1 
ATOM   2332 C CA    . LEU A 1 293 ? -50.89788 36.31952 20.63323  1.000 76.03255  ? 297 LEU A CA    1 
ATOM   2333 C C     . LEU A 1 293 ? -50.02021 36.16895 19.39447  1.000 74.79242  ? 297 LEU A C     1 
ATOM   2334 O O     . LEU A 1 293 ? -50.52223 36.16140 18.26040  1.000 73.84115  ? 297 LEU A O     1 
ATOM   2335 C CB    . LEU A 1 293 ? -51.04081 37.78816 21.02430  1.000 61.93072  ? 297 LEU A CB    1 
ATOM   2336 C CG    . LEU A 1 293 ? -51.60880 38.73945 19.99636  1.000 73.06437  ? 297 LEU A CG    1 
ATOM   2337 C CD1   . LEU A 1 293 ? -53.00674 38.29056 19.64529  1.000 66.06158  ? 297 LEU A CD1   1 
ATOM   2338 C CD2   . LEU A 1 293 ? -51.58901 40.18368 20.52623  1.000 71.77084  ? 297 LEU A CD2   1 
ATOM   2339 N N     . LEU A 1 294 ? -48.70403 36.09149 19.57818  1.000 76.42486  ? 298 LEU A N     1 
ATOM   2340 C CA    . LEU A 1 294 ? -47.84060 35.87719 18.42563  1.000 75.78363  ? 298 LEU A CA    1 
ATOM   2341 C C     . LEU A 1 294 ? -48.11364 34.51899 17.78992  1.000 73.65965  ? 298 LEU A C     1 
ATOM   2342 O O     . LEU A 1 294 ? -48.24879 34.40807 16.56265  1.000 68.43252  ? 298 LEU A O     1 
ATOM   2343 C CB    . LEU A 1 294 ? -46.38374 35.99258 18.84581  1.000 69.63140  ? 298 LEU A CB    1 
ATOM   2344 C CG    . LEU A 1 294 ? -45.86218 37.41235 18.85549  1.000 72.59308  ? 298 LEU A CG    1 
ATOM   2345 C CD1   . LEU A 1 294 ? -44.62875 37.46208 19.75666  1.000 72.36144  ? 298 LEU A CD1   1 
ATOM   2346 C CD2   . LEU A 1 294 ? -45.54399 37.85595 17.42724  1.000 70.86545  ? 298 LEU A CD2   1 
ATOM   2347 N N     . SER A 1 295 ? -48.23810 33.48016 18.61747  1.000 72.44646  ? 299 SER A N     1 
ATOM   2348 C CA    . SER A 1 295 ? -48.43321 32.12635 18.10988  1.000 75.57144  ? 299 SER A CA    1 
ATOM   2349 C C     . SER A 1 295 ? -49.76741 31.94242 17.40307  1.000 77.99923  ? 299 SER A C     1 
ATOM   2350 O O     . SER A 1 295 ? -49.96309 30.90033 16.76466  1.000 84.72691  ? 299 SER A O     1 
ATOM   2351 C CB    . SER A 1 295 ? -48.36599 31.11108 19.23605  1.000 76.92353  ? 299 SER A CB    1 
ATOM   2352 O OG    . SER A 1 295 ? -49.51010 31.21957 20.05439  1.000 78.92123  ? 299 SER A OG    1 
ATOM   2353 N N     . LYS A 1 296 ? -50.69777 32.89467 17.54779  1.000 70.63705  ? 300 LYS A N     1 
ATOM   2354 C CA    . LYS A 1 296 ? -51.97217 32.87818 16.83788  1.000 74.57183  ? 300 LYS A CA    1 
ATOM   2355 C C     . LYS A 1 296 ? -52.00635 33.82045 15.64129  1.000 75.21354  ? 300 LYS A C     1 
ATOM   2356 O O     . LYS A 1 296 ? -52.94758 33.75363 14.84369  1.000 71.58538  ? 300 LYS A O     1 
ATOM   2357 C CB    . LYS A 1 296 ? -53.12020 33.22883 17.79283  1.000 67.22825  ? 300 LYS A CB    1 
ATOM   2358 C CG    . LYS A 1 296 ? -53.37341 32.14236 18.83282  1.000 70.34119  ? 300 LYS A CG    1 
ATOM   2359 C CD    . LYS A 1 296 ? -54.36670 32.57713 19.89629  1.000 75.86509  ? 300 LYS A CD    1 
ATOM   2360 C CE    . LYS A 1 296 ? -54.38285 31.58482 21.06640  1.000 87.82435  ? 300 LYS A CE    1 
ATOM   2361 N NZ    . LYS A 1 296 ? -55.27328 32.01975 22.19443  1.000 90.07797  ? 300 LYS A NZ    1 
ATOM   2362 N N     . MET A 1 297 ? -51.03463 34.71730 15.51508  1.000 70.44020  ? 301 MET A N     1 
ATOM   2363 C CA    . MET A 1 297 ? -50.95416 35.54808 14.32425  1.000 67.89503  ? 301 MET A CA    1 
ATOM   2364 C C     . MET A 1 297 ? -49.99215 34.97994 13.30758  1.000 71.68958  ? 301 MET A C     1 
ATOM   2365 O O     . MET A 1 297 ? -50.27941 34.98867 12.10370  1.000 69.46581  ? 301 MET A O     1 
ATOM   2366 C CB    . MET A 1 297 ? -50.54550 36.97159 14.70190  1.000 61.40208  ? 301 MET A CB    1 
ATOM   2367 C CG    . MET A 1 297 ? -51.67553 37.80951 15.23476  1.000 68.06289  ? 301 MET A CG    1 
ATOM   2368 S SD    . MET A 1 297 ? -51.17462 39.47925 15.77482  1.000 78.46252  ? 301 MET A SD    1 
ATOM   2369 C CE    . MET A 1 297 ? -49.47060 39.20736 16.25064  1.000 68.85484  ? 301 MET A CE    1 
ATOM   2370 N N     . LEU A 1 298 ? -48.85697 34.48513 13.79372  1.000 75.25819  ? 302 LEU A N     1 
ATOM   2371 C CA    . LEU A 1 298 ? -47.82387 33.89883 12.95345  1.000 74.28043  ? 302 LEU A CA    1 
ATOM   2372 C C     . LEU A 1 298 ? -48.16121 32.43563 12.68644  1.000 71.01027  ? 302 LEU A C     1 
ATOM   2373 O O     . LEU A 1 298 ? -47.45234 31.51151 13.07918  1.000 79.31748  ? 302 LEU A O     1 
ATOM   2374 C CB    . LEU A 1 298 ? -46.46701 34.05236 13.62041  1.000 73.45816  ? 302 LEU A CB    1 
ATOM   2375 C CG    . LEU A 1 298 ? -46.03233 35.50764 13.79155  1.000 73.86667  ? 302 LEU A CG    1 
ATOM   2376 C CD1   . LEU A 1 298 ? -44.76689 35.61209 14.63038  1.000 76.44154  ? 302 LEU A CD1   1 
ATOM   2377 C CD2   . LEU A 1 298 ? -45.84194 36.15124 12.42317  1.000 72.37102  ? 302 LEU A CD2   1 
ATOM   2378 N N     . VAL A 1 299 ? -49.28371 32.24565 12.00432  1.000 71.34417  ? 303 VAL A N     1 
ATOM   2379 C CA    . VAL A 1 299 ? -49.78886 30.92740 11.65089  1.000 68.36291  ? 303 VAL A CA    1 
ATOM   2380 C C     . VAL A 1 299 ? -49.82796 30.83533 10.13301  1.000 71.68538  ? 303 VAL A C     1 
ATOM   2381 O O     . VAL A 1 299 ? -50.42802 31.68703 9.47008   1.000 76.25236  ? 303 VAL A O     1 
ATOM   2382 C CB    . VAL A 1 299 ? -51.17573 30.69428 12.26677  1.000 74.72754  ? 303 VAL A CB    1 
ATOM   2383 C CG1   . VAL A 1 299 ? -51.82945 29.48213 11.66471  1.000 74.05293  ? 303 VAL A CG1   1 
ATOM   2384 C CG2   . VAL A 1 299 ? -51.04527 30.54671 13.75589  1.000 76.78648  ? 303 VAL A CG2   1 
ATOM   2385 N N     . ILE A 1 300 ? -49.17735 29.81239 9.58189   1.000 70.56439  ? 304 ILE A N     1 
ATOM   2386 C CA    . ILE A 1 300 ? -49.01083 29.74711 8.13156   1.000 71.33278  ? 304 ILE A CA    1 
ATOM   2387 C C     . ILE A 1 300 ? -50.35576 29.59475 7.42019   1.000 71.82288  ? 304 ILE A C     1 
ATOM   2388 O O     . ILE A 1 300 ? -50.58849 30.21937 6.37886   1.000 73.64536  ? 304 ILE A O     1 
ATOM   2389 C CB    . ILE A 1 300 ? -48.04747 28.61572 7.74348   1.000 73.50907  ? 304 ILE A CB    1 
ATOM   2390 C CG1   . ILE A 1 300 ? -46.60453 28.96362 8.10508   1.000 71.01538  ? 304 ILE A CG1   1 
ATOM   2391 C CG2   . ILE A 1 300 ? -48.14706 28.32995 6.24919   1.000 72.70957  ? 304 ILE A CG2   1 
ATOM   2392 C CD1   . ILE A 1 300 ? -45.63381 28.03976 7.42311   1.000 67.86688  ? 304 ILE A CD1   1 
ATOM   2393 N N     . ASP A 1 301 ? -51.24515 28.75124 7.94255   1.000 72.65867  ? 305 ASP A N     1 
ATOM   2394 C CA    . ASP A 1 301 ? -52.51101 28.42636 7.27884   1.000 79.34863  ? 305 ASP A CA    1 
ATOM   2395 C C     . ASP A 1 301 ? -53.58418 29.42376 7.71808   1.000 71.37978  ? 305 ASP A C     1 
ATOM   2396 O O     . ASP A 1 301 ? -54.08705 29.33958 8.84202   1.000 73.30481  ? 305 ASP A O     1 
ATOM   2397 C CB    . ASP A 1 301 ? -52.91288 26.97715 7.59102   1.000 80.57939  ? 305 ASP A CB    1 
ATOM   2398 C CG    . ASP A 1 301 ? -54.29329 26.57447 6.99715   1.000 86.63150  ? 305 ASP A CG    1 
ATOM   2399 O OD1   . ASP A 1 301 ? -54.85050 25.52475 7.42107   1.000 88.97319  ? 305 ASP A OD1   1 
ATOM   2400 O OD2   . ASP A 1 301 ? -54.82831 27.30556 6.11886   1.000 86.14877  ? 305 ASP A OD2   1 
ATOM   2401 N N     . ALA A 1 302 ? -53.97377 30.33466 6.80757   1.000 73.54754  ? 306 ALA A N     1 
ATOM   2402 C CA    . ALA A 1 302 ? -54.87692 31.43867 7.15641   1.000 70.96026  ? 306 ALA A CA    1 
ATOM   2403 C C     . ALA A 1 302 ? -56.20715 30.96202 7.73168   1.000 78.31442  ? 306 ALA A C     1 
ATOM   2404 O O     . ALA A 1 302 ? -56.82374 31.67710 8.53841   1.000 76.39250  ? 306 ALA A O     1 
ATOM   2405 C CB    . ALA A 1 302 ? -55.15212 32.32388 5.93127   1.000 62.37280  ? 306 ALA A CB    1 
ATOM   2406 N N     . SER A 1 303 ? -56.69157 29.78874 7.31795   1.000 69.27365  ? 307 SER A N     1 
ATOM   2407 C CA    . SER A 1 303 ? -57.94390 29.33583 7.90158   1.000 71.00043  ? 307 SER A CA    1 
ATOM   2408 C C     . SER A 1 303 ? -57.79620 28.98198 9.36846   1.000 76.82337  ? 307 SER A C     1 
ATOM   2409 O O     . SER A 1 303 ? -58.80823 28.83634 10.05543  1.000 78.47612  ? 307 SER A O     1 
ATOM   2410 C CB    . SER A 1 303 ? -58.45888 28.13213 7.14744   1.000 69.46257  ? 307 SER A CB    1 
ATOM   2411 O OG    . SER A 1 303 ? -57.40502 27.19771 7.02565   1.000 83.81261  ? 307 SER A OG    1 
ATOM   2412 N N     . LYS A 1 304 ? -56.56744 28.84087 9.85575   1.000 76.84735  ? 308 LYS A N     1 
ATOM   2413 C CA    . LYS A 1 304 ? -56.29079 28.60386 11.26467  1.000 77.56769  ? 308 LYS A CA    1 
ATOM   2414 C C     . LYS A 1 304 ? -55.87192 29.87180 11.97375  1.000 76.70472  ? 308 LYS A C     1 
ATOM   2415 O O     . LYS A 1 304 ? -55.65957 29.84796 13.18824  1.000 80.43513  ? 308 LYS A O     1 
ATOM   2416 C CB    . LYS A 1 304 ? -55.18671 27.55538 11.42148  1.000 78.62364  ? 308 LYS A CB    1 
ATOM   2417 C CG    . LYS A 1 304 ? -55.69936 26.13202 11.64668  1.000 93.00716  ? 308 LYS A CG    1 
ATOM   2418 C CD    . LYS A 1 304 ? -54.72549 25.10346 11.08639  1.000 95.63402  ? 308 LYS A CD    1 
ATOM   2419 C CE    . LYS A 1 304 ? -55.04979 23.68095 11.51988  1.000 91.04295  ? 308 LYS A CE    1 
ATOM   2420 N NZ    . LYS A 1 304 ? -53.98136 22.77748 10.99346  1.000 89.62439  ? 308 LYS A NZ    1 
ATOM   2421 N N     . ARG A 1 305 ? -55.71906 30.96456 11.23474  1.000 79.35048  ? 309 ARG A N     1 
ATOM   2422 C CA    . ARG A 1 305 ? -55.14905 32.18917 11.76597  1.000 75.41812  ? 309 ARG A CA    1 
ATOM   2423 C C     . ARG A 1 305 ? -56.25297 33.04824 12.37996  1.000 74.22156  ? 309 ARG A C     1 
ATOM   2424 O O     . ARG A 1 305 ? -57.38539 33.10156 11.88073  1.000 74.95680  ? 309 ARG A O     1 
ATOM   2425 C CB    . ARG A 1 305 ? -54.39676 32.94452 10.66183  1.000 70.91100  ? 309 ARG A CB    1 
ATOM   2426 C CG    . ARG A 1 305 ? -53.55678 34.12862 11.14284  1.000 68.49068  ? 309 ARG A CG    1 
ATOM   2427 C CD    . ARG A 1 305 ? -52.84560 34.86653 9.97374   1.000 61.22744  ? 309 ARG A CD    1 
ATOM   2428 N NE    . ARG A 1 305 ? -52.23025 33.93642 9.02745   1.000 65.98868  ? 309 ARG A NE    1 
ATOM   2429 C CZ    . ARG A 1 305 ? -52.15641 34.13868 7.71706   1.000 67.57095  ? 309 ARG A CZ    1 
ATOM   2430 N NH1   . ARG A 1 305 ? -52.65980 35.22592 7.15911   1.000 60.61202  ? 309 ARG A NH1   1 
ATOM   2431 N NH2   . ARG A 1 305 ? -51.56690 33.22468 6.94906   1.000 59.79681  ? 309 ARG A NH2   1 
ATOM   2432 N N     . ILE A 1 306 ? -55.91598 33.67695 13.50518  1.000 71.71159  ? 310 ILE A N     1 
ATOM   2433 C CA    . ILE A 1 306 ? -56.83030 34.57343 14.19785  1.000 69.06723  ? 310 ILE A CA    1 
ATOM   2434 C C     . ILE A 1 306 ? -57.21883 35.75023 13.30217  1.000 72.48404  ? 310 ILE A C     1 
ATOM   2435 O O     . ILE A 1 306 ? -56.46848 36.15367 12.40127  1.000 65.26089  ? 310 ILE A O     1 
ATOM   2436 C CB    . ILE A 1 306 ? -56.15151 35.04444 15.49865  1.000 69.48221  ? 310 ILE A CB    1 
ATOM   2437 C CG1   . ILE A 1 306 ? -57.15350 35.35938 16.60188  1.000 75.60091  ? 310 ILE A CG1   1 
ATOM   2438 C CG2   . ILE A 1 306 ? -55.14952 36.17875 15.25260  1.000 65.72286  ? 310 ILE A CG2   1 
ATOM   2439 C CD1   . ILE A 1 306 ? -56.50220 36.02173 17.81753  1.000 70.53467  ? 310 ILE A CD1   1 
ATOM   2440 N N     . SER A 1 307 ? -58.41585 36.29134 13.53731  1.000 72.33769  ? 311 SER A N     1 
ATOM   2441 C CA    . SER A 1 307 ? -58.90464 37.45116 12.80252  1.000 73.27587  ? 311 SER A CA    1 
ATOM   2442 C C     . SER A 1 307 ? -58.60239 38.74332 13.55976  1.000 63.81362  ? 311 SER A C     1 
ATOM   2443 O O     . SER A 1 307 ? -58.18795 38.73569 14.71711  1.000 56.90670  ? 311 SER A O     1 
ATOM   2444 C CB    . SER A 1 307 ? -60.40811 37.33755 12.54547  1.000 64.48966  ? 311 SER A CB    1 
ATOM   2445 O OG    . SER A 1 307 ? -61.16892 37.70259 13.68993  1.000 66.05476  ? 311 SER A OG    1 
ATOM   2446 N N     . VAL A 1 308 ? -58.79576 39.87391 12.87768  1.000 62.25616  ? 312 VAL A N     1 
ATOM   2447 C CA    . VAL A 1 308 ? -58.58141 41.16233 13.53471  1.000 62.31241  ? 312 VAL A CA    1 
ATOM   2448 C C     . VAL A 1 308 ? -59.47916 41.31781 14.74564  1.000 60.10231  ? 312 VAL A C     1 
ATOM   2449 O O     . VAL A 1 308 ? -59.05805 41.86499 15.77635  1.000 58.88967  ? 312 VAL A O     1 
ATOM   2450 C CB    . VAL A 1 308 ? -58.81701 42.31378 12.56254  1.000 70.04166  ? 312 VAL A CB    1 
ATOM   2451 C CG1   . VAL A 1 308 ? -58.54864 43.63576 13.29049  1.000 60.53468  ? 312 VAL A CG1   1 
ATOM   2452 C CG2   . VAL A 1 308 ? -57.93049 42.11410 11.36282  1.000 68.31186  ? 312 VAL A CG2   1 
ATOM   2453 N N     . ASP A 1 309 ? -60.74137 40.88055 14.62759  1.000 66.36547  ? 313 ASP A N     1 
ATOM   2454 C CA    . ASP A 1 309 ? -61.70316 41.03143 15.71810  1.000 69.70517  ? 313 ASP A CA    1 
ATOM   2455 C C     . ASP A 1 309 ? -61.32905 40.16728 16.90385  1.000 63.86917  ? 313 ASP A C     1 
ATOM   2456 O O     . ASP A 1 309 ? -61.36445 40.63117 18.04896  1.000 67.03451  ? 313 ASP A O     1 
ATOM   2457 C CB    . ASP A 1 309 ? -63.11499 40.68291 15.24979  1.000 73.42679  ? 313 ASP A CB    1 
ATOM   2458 C CG    . ASP A 1 309 ? -63.43180 41.27847 13.88910  1.000 91.16405  ? 313 ASP A CG    1 
ATOM   2459 O OD1   . ASP A 1 309 ? -63.00808 40.67818 12.86388  1.000 100.27911 ? 313 ASP A OD1   1 
ATOM   2460 O OD2   . ASP A 1 309 ? -64.07006 42.35890 13.85155  1.000 84.03720  ? 313 ASP A OD2   1 
ATOM   2461 N N     . GLU A 1 310 ? -60.99510 38.89506 16.66491  1.000 65.60395  ? 314 GLU A N     1 
ATOM   2462 C CA    . GLU A 1 310 ? -60.56279 38.06897 17.78782  1.000 72.15827  ? 314 GLU A CA    1 
ATOM   2463 C C     . GLU A 1 310 ? -59.29230 38.64172 18.38938  1.000 66.46830  ? 314 GLU A C     1 
ATOM   2464 O O     . GLU A 1 310 ? -59.08790 38.59201 19.60629  1.000 67.78544  ? 314 GLU A O     1 
ATOM   2465 C CB    . GLU A 1 310 ? -60.32792 36.62323 17.35943  1.000 73.96987  ? 314 GLU A CB    1 
ATOM   2466 C CG    . GLU A 1 310 ? -61.18794 36.10850 16.22438  1.000 81.01833  ? 314 GLU A CG    1 
ATOM   2467 C CD    . GLU A 1 310 ? -60.85247 34.67405 15.85538  1.000 87.27352  ? 314 GLU A CD    1 
ATOM   2468 O OE1   . GLU A 1 310 ? -60.64114 34.41180 14.64773  1.000 85.93024  ? 314 GLU A OE1   1 
ATOM   2469 O OE2   . GLU A 1 310 ? -60.78831 33.81130 16.76306  1.000 102.84337 ? 314 GLU A OE2   1 
ATOM   2470 N N     . ALA A 1 311 ? -58.44356 39.22960 17.55499  1.000 61.07599  ? 315 ALA A N     1 
ATOM   2471 C CA    . ALA A 1 311 ? -57.21193 39.79151 18.08054  1.000 63.23307  ? 315 ALA A CA    1 
ATOM   2472 C C     . ALA A 1 311 ? -57.51309 40.90289 19.08178  1.000 73.46406  ? 315 ALA A C     1 
ATOM   2473 O O     . ALA A 1 311 ? -56.88405 40.96966 20.15042  1.000 66.90392  ? 315 ALA A O     1 
ATOM   2474 C CB    . ALA A 1 311 ? -56.33928 40.28505 16.92999  1.000 65.30567  ? 315 ALA A CB    1 
ATOM   2475 N N     . LEU A 1 312 ? -58.50336 41.76293 18.77575  1.000 63.29782  ? 316 LEU A N     1 
ATOM   2476 C CA    . LEU A 1 312 ? -58.86558 42.83429 19.69962  1.000 61.57074  ? 316 LEU A CA    1 
ATOM   2477 C C     . LEU A 1 312 ? -59.47896 42.29959 20.99564  1.000 64.65063  ? 316 LEU A C     1 
ATOM   2478 O O     . LEU A 1 312 ? -59.51993 43.01605 22.00694  1.000 65.51987  ? 316 LEU A O     1 
ATOM   2479 C CB    . LEU A 1 312 ? -59.82931 43.81101 19.02056  1.000 63.94871  ? 316 LEU A CB    1 
ATOM   2480 C CG    . LEU A 1 312 ? -59.23606 44.84430 18.06209  1.000 68.15022  ? 316 LEU A CG    1 
ATOM   2481 C CD1   . LEU A 1 312 ? -60.32037 45.47365 17.16954  1.000 65.65254  ? 316 LEU A CD1   1 
ATOM   2482 C CD2   . LEU A 1 312 ? -58.50748 45.92862 18.83495  1.000 65.43337  ? 316 LEU A CD2   1 
ATOM   2483 N N     . GLN A 1 313 ? -59.96514 41.06725 20.99830  1.000 66.72326  ? 317 GLN A N     1 
ATOM   2484 C CA    . GLN A 1 313 ? -60.50427 40.49708 22.22398  1.000 67.90631  ? 317 GLN A CA    1 
ATOM   2485 C C     . GLN A 1 313 ? -59.44989 39.75130 23.03934  1.000 71.10968  ? 317 GLN A C     1 
ATOM   2486 O O     . GLN A 1 313 ? -59.76344 39.25382 24.13283  1.000 73.79881  ? 317 GLN A O     1 
ATOM   2487 C CB    . GLN A 1 313 ? -61.66383 39.55341 21.89023  1.000 66.66230  ? 317 GLN A CB    1 
ATOM   2488 C CG    . GLN A 1 313 ? -62.95299 40.21091 21.38275  1.000 67.63422  ? 317 GLN A CG    1 
ATOM   2489 C CD    . GLN A 1 313 ? -63.58127 41.15948 22.38981  1.000 72.84176  ? 317 GLN A CD    1 
ATOM   2490 O OE1   . GLN A 1 313 ? -63.55760 40.91373 23.60567  1.000 78.79450  ? 317 GLN A OE1   1 
ATOM   2491 N NE2   . GLN A 1 313 ? -64.18482 42.23327 21.88673  1.000 70.51858  ? 317 GLN A NE2   1 
ATOM   2492 N N     . HIS A 1 314 ? -58.22082 39.65794 22.52839  1.000 67.52688  ? 318 HIS A N     1 
ATOM   2493 C CA    . HIS A 1 314 ? -57.17321 38.91904 23.21039  1.000 70.45025  ? 318 HIS A CA    1 
ATOM   2494 C C     . HIS A 1 314 ? -56.70004 39.67686 24.44988  1.000 74.91039  ? 318 HIS A C     1 
ATOM   2495 O O     . HIS A 1 314 ? -56.49341 40.89511 24.39029  1.000 76.94338  ? 318 HIS A O     1 
ATOM   2496 C CB    . HIS A 1 314 ? -55.99851 38.68596 22.26576  1.000 77.32925  ? 318 HIS A CB    1 
ATOM   2497 C CG    . HIS A 1 314 ? -54.99241 37.71809 22.79261  1.000 73.63414  ? 318 HIS A CG    1 
ATOM   2498 N ND1   . HIS A 1 314 ? -54.04593 38.07085 23.72936  1.000 73.94815  ? 318 HIS A ND1   1 
ATOM   2499 C CD2   . HIS A 1 314 ? -54.80705 36.40171 22.53914  1.000 65.88690  ? 318 HIS A CD2   1 
ATOM   2500 C CE1   . HIS A 1 314 ? -53.30790 37.01344 24.01895  1.000 79.67241  ? 318 HIS A CE1   1 
ATOM   2501 N NE2   . HIS A 1 314 ? -53.74669 35.98874 23.30859  1.000 77.88784  ? 318 HIS A NE2   1 
ATOM   2502 N N     . PRO A 1 315 ? -56.47033 38.97699 25.56611  1.000 76.30300  ? 319 PRO A N     1 
ATOM   2503 C CA    . PRO A 1 315 ? -56.21231 39.67736 26.83654  1.000 76.65777  ? 319 PRO A CA    1 
ATOM   2504 C C     . PRO A 1 315 ? -54.98637 40.58358 26.82467  1.000 82.67818  ? 319 PRO A C     1 
ATOM   2505 O O     . PRO A 1 315 ? -54.96784 41.58683 27.55193  1.000 85.56366  ? 319 PRO A O     1 
ATOM   2506 C CB    . PRO A 1 315 ? -56.07833 38.52413 27.84545  1.000 78.55531  ? 319 PRO A CB    1 
ATOM   2507 C CG    . PRO A 1 315 ? -55.88046 37.29737 27.02133  1.000 77.07295  ? 319 PRO A CG    1 
ATOM   2508 C CD    . PRO A 1 315 ? -56.61084 37.52457 25.74566  1.000 70.71495  ? 319 PRO A CD    1 
ATOM   2509 N N     . TYR A 1 316 ? -53.96219 40.27810 26.02317  1.000 77.54261  ? 320 TYR A N     1 
ATOM   2510 C CA    . TYR A 1 316 ? -52.81608 41.17857 25.94889  1.000 77.90466  ? 320 TYR A CA    1 
ATOM   2511 C C     . TYR A 1 316 ? -53.21136 42.53614 25.38556  1.000 75.21747  ? 320 TYR A C     1 
ATOM   2512 O O     . TYR A 1 316 ? -52.60326 43.55259 25.72586  1.000 76.70427  ? 320 TYR A O     1 
ATOM   2513 C CB    . TYR A 1 316 ? -51.71168 40.56253 25.09029  1.000 73.66511  ? 320 TYR A CB    1 
ATOM   2514 C CG    . TYR A 1 316 ? -50.40287 41.33802 25.09228  1.000 79.32074  ? 320 TYR A CG    1 
ATOM   2515 C CD1   . TYR A 1 316 ? -49.54651 41.30837 26.18789  1.000 78.84008  ? 320 TYR A CD1   1 
ATOM   2516 C CD2   . TYR A 1 316 ? -50.02781 42.10566 23.99464  1.000 79.73253  ? 320 TYR A CD2   1 
ATOM   2517 C CE1   . TYR A 1 316 ? -48.33628 42.00895 26.17663  1.000 75.81214  ? 320 TYR A CE1   1 
ATOM   2518 C CE2   . TYR A 1 316 ? -48.83017 42.80150 23.97465  1.000 78.20992  ? 320 TYR A CE2   1 
ATOM   2519 C CZ    . TYR A 1 316 ? -47.99015 42.75226 25.06285  1.000 79.19611  ? 320 TYR A CZ    1 
ATOM   2520 O OH    . TYR A 1 316 ? -46.81263 43.47143 25.01731  1.000 77.10056  ? 320 TYR A OH    1 
ATOM   2521 N N     . ILE A 1 317 ? -54.22416 42.56734 24.52691  1.000 75.09565  ? 321 ILE A N     1 
ATOM   2522 C CA    . ILE A 1 317 ? -54.67799 43.77011 23.84193  1.000 67.25408  ? 321 ILE A CA    1 
ATOM   2523 C C     . ILE A 1 317 ? -55.91937 44.33953 24.51811  1.000 73.59024  ? 321 ILE A C     1 
ATOM   2524 O O     . ILE A 1 317 ? -56.14077 45.56080 24.51822  1.000 67.38322  ? 321 ILE A O     1 
ATOM   2525 C CB    . ILE A 1 317 ? -54.95083 43.44700 22.36099  1.000 71.71588  ? 321 ILE A CB    1 
ATOM   2526 C CG1   . ILE A 1 317 ? -53.69898 42.82131 21.74488  1.000 72.10407  ? 321 ILE A CG1   1 
ATOM   2527 C CG2   . ILE A 1 317 ? -55.38822 44.68041 21.58417  1.000 70.70661  ? 321 ILE A CG2   1 
ATOM   2528 C CD1   . ILE A 1 317 ? -52.65741 43.89017 21.37675  1.000 63.56157  ? 321 ILE A CD1   1 
ATOM   2529 N N     . ASN A 1 318 ? -56.72685 43.46081 25.12029  1.000 70.06445  ? 322 ASN A N     1 
ATOM   2530 C CA    . ASN A 1 318 ? -58.09386 43.81936 25.48236  1.000 75.65085  ? 322 ASN A CA    1 
ATOM   2531 C C     . ASN A 1 318 ? -58.18865 44.86751 26.58353  1.000 77.46985  ? 322 ASN A C     1 
ATOM   2532 O O     . ASN A 1 318 ? -59.26451 45.45724 26.74567  1.000 73.51062  ? 322 ASN A O     1 
ATOM   2533 C CB    . ASN A 1 318 ? -58.87971 42.58866 25.91535  1.000 77.71186  ? 322 ASN A CB    1 
ATOM   2534 C CG    . ASN A 1 318 ? -60.33023 42.91714 26.18971  1.000 84.29996  ? 322 ASN A CG    1 
ATOM   2535 O OD1   . ASN A 1 318 ? -60.75757 42.97424 27.34807  1.000 88.60188  ? 322 ASN A OD1   1 
ATOM   2536 N ND2   . ASN A 1 318 ? -61.08412 43.20884 25.12306  1.000 75.53757  ? 322 ASN A ND2   1 
ATOM   2537 N N     . VAL A 1 319 ? -57.10037 45.12715 27.31897  1.000 80.21427  ? 323 VAL A N     1 
ATOM   2538 C CA    . VAL A 1 319 ? -57.12941 46.06894 28.43951  1.000 81.55863  ? 323 VAL A CA    1 
ATOM   2539 C C     . VAL A 1 319 ? -57.45737 47.49862 27.99858  1.000 79.68035  ? 323 VAL A C     1 
ATOM   2540 O O     . VAL A 1 319 ? -57.93465 48.30773 28.80974  1.000 80.77755  ? 323 VAL A O     1 
ATOM   2541 C CB    . VAL A 1 319 ? -55.77592 46.03197 29.16608  1.000 86.62666  ? 323 VAL A CB    1 
ATOM   2542 C CG1   . VAL A 1 319 ? -55.56290 44.66700 29.75096  1.000 87.61230  ? 323 VAL A CG1   1 
ATOM   2543 C CG2   . VAL A 1 319 ? -54.64059 46.39379 28.20797  1.000 75.13869  ? 323 VAL A CG2   1 
ATOM   2544 N N     . TRP A 1 320 ? -57.19454 47.83982 26.73633  1.000 64.92085  ? 324 TRP A N     1 
ATOM   2545 C CA    . TRP A 1 320 ? -57.42209 49.19027 26.23403  1.000 72.88910  ? 324 TRP A CA    1 
ATOM   2546 C C     . TRP A 1 320 ? -58.73390 49.32861 25.46893  1.000 73.42431  ? 324 TRP A C     1 
ATOM   2547 O O     . TRP A 1 320 ? -58.94113 50.35873 24.82403  1.000 72.10956  ? 324 TRP A O     1 
ATOM   2548 C CB    . TRP A 1 320 ? -56.27271 49.63570 25.32121  1.000 61.58493  ? 324 TRP A CB    1 
ATOM   2549 C CG    . TRP A 1 320 ? -54.88228 49.28467 25.79768  1.000 69.22058  ? 324 TRP A CG    1 
ATOM   2550 C CD1   . TRP A 1 320 ? -53.99301 48.43618 25.19053  1.000 73.27636  ? 324 TRP A CD1   1 
ATOM   2551 C CD2   . TRP A 1 320 ? -54.21037 49.79574 26.96122  1.000 69.72495  ? 324 TRP A CD2   1 
ATOM   2552 N NE1   . TRP A 1 320 ? -52.81831 48.37718 25.91358  1.000 68.31005  ? 324 TRP A NE1   1 
ATOM   2553 C CE2   . TRP A 1 320 ? -52.92758 49.20271 27.00181  1.000 68.05386  ? 324 TRP A CE2   1 
ATOM   2554 C CE3   . TRP A 1 320 ? -54.57171 50.69155 27.97599  1.000 74.65600  ? 324 TRP A CE3   1 
ATOM   2555 C CZ2   . TRP A 1 320 ? -52.01229 49.47677 28.01257  1.000 68.72306  ? 324 TRP A CZ2   1 
ATOM   2556 C CZ3   . TRP A 1 320 ? -53.65372 50.96786 28.98175  1.000 79.95383  ? 324 TRP A CZ3   1 
ATOM   2557 C CH2   . TRP A 1 320 ? -52.38794 50.36452 28.98683  1.000 77.59235  ? 324 TRP A CH2   1 
ATOM   2558 N N     . TYR A 1 321 ? -59.61363 48.32183 25.50953  1.000 68.71308  ? 325 TYR A N     1 
ATOM   2559 C CA    . TYR A 1 321 ? -60.71731 48.25856 24.55396  1.000 62.85365  ? 325 TYR A CA    1 
ATOM   2560 C C     . TYR A 1 321 ? -61.76097 49.33275 24.82364  1.000 67.66954  ? 325 TYR A C     1 
ATOM   2561 O O     . TYR A 1 321 ? -62.25243 49.46975 25.94720  1.000 65.75940  ? 325 TYR A O     1 
ATOM   2562 C CB    . TYR A 1 321 ? -61.38118 46.89121 24.59181  1.000 68.99908  ? 325 TYR A CB    1 
ATOM   2563 C CG    . TYR A 1 321 ? -62.31906 46.61670 23.43538  1.000 69.05506  ? 325 TYR A CG    1 
ATOM   2564 C CD1   . TYR A 1 321 ? -63.67635 47.00638 23.48022  1.000 66.71484  ? 325 TYR A CD1   1 
ATOM   2565 C CD2   . TYR A 1 321 ? -61.85802 45.96141 22.29636  1.000 63.34566  ? 325 TYR A CD2   1 
ATOM   2566 C CE1   . TYR A 1 321 ? -64.55610 46.72820 22.41317  1.000 62.03693  ? 325 TYR A CE1   1 
ATOM   2567 C CE2   . TYR A 1 321 ? -62.72345 45.67793 21.22813  1.000 74.70670  ? 325 TYR A CE2   1 
ATOM   2568 C CZ    . TYR A 1 321 ? -64.06562 46.05608 21.28787  1.000 72.81783  ? 325 TYR A CZ    1 
ATOM   2569 O OH    . TYR A 1 321 ? -64.89065 45.75950 20.21193  1.000 68.89701  ? 325 TYR A OH    1 
ATOM   2570 N N     . ASP A 1 322 ? -62.12637 50.06654 23.76901  1.000 67.33148  ? 326 ASP A N     1 
ATOM   2571 C CA    . ASP A 1 322 ? -63.14308 51.10578 23.77294  1.000 64.28066  ? 326 ASP A CA    1 
ATOM   2572 C C     . ASP A 1 322 ? -63.96550 51.00205 22.48783  1.000 69.41892  ? 326 ASP A C     1 
ATOM   2573 O O     . ASP A 1 322 ? -63.40773 51.12316 21.38046  1.000 60.26533  ? 326 ASP A O     1 
ATOM   2574 C CB    . ASP A 1 322 ? -62.48894 52.48954 23.88777  1.000 69.19600  ? 326 ASP A CB    1 
ATOM   2575 C CG    . ASP A 1 322 ? -63.50816 53.62173 24.10884  1.000 70.55718  ? 326 ASP A CG    1 
ATOM   2576 O OD1   . ASP A 1 322 ? -64.57940 53.61598 23.45329  1.000 69.19897  ? 326 ASP A OD1   1 
ATOM   2577 O OD2   . ASP A 1 322 ? -63.22123 54.53807 24.91544  1.000 81.48720  ? 326 ASP A OD2   1 
ATOM   2578 N N     . PRO A 1 323 ? -65.28706 50.79569 22.57786  1.000 66.57132  ? 327 PRO A N     1 
ATOM   2579 C CA    . PRO A 1 323 ? -66.07484 50.68539 21.34176  1.000 62.76916  ? 327 PRO A CA    1 
ATOM   2580 C C     . PRO A 1 323 ? -65.96454 51.90776 20.45023  1.000 65.62007  ? 327 PRO A C     1 
ATOM   2581 O O     . PRO A 1 323 ? -66.09574 51.77299 19.22642  1.000 68.50778  ? 327 PRO A O     1 
ATOM   2582 C CB    . PRO A 1 323 ? -67.50505 50.46411 21.84741  1.000 63.69333  ? 327 PRO A CB    1 
ATOM   2583 C CG    . PRO A 1 323 ? -67.50035 50.90554 23.27236  1.000 69.68685  ? 327 PRO A CG    1 
ATOM   2584 C CD    . PRO A 1 323 ? -66.12029 50.59179 23.77353  1.000 62.17268  ? 327 PRO A CD    1 
ATOM   2585 N N     . SER A 1 324 ? -65.70379 53.09354 20.99670  1.000 60.23807  ? 328 SER A N     1 
ATOM   2586 C CA    . SER A 1 324 ? -65.63238 54.25061 20.11407  1.000 63.54308  ? 328 SER A CA    1 
ATOM   2587 C C     . SER A 1 324 ? -64.45369 54.12650 19.16870  1.000 65.66148  ? 328 SER A C     1 
ATOM   2588 O O     . SER A 1 324 ? -64.44395 54.76425 18.11115  1.000 69.87167  ? 328 SER A O     1 
ATOM   2589 C CB    . SER A 1 324 ? -65.53174 55.54397 20.90915  1.000 68.50515  ? 328 SER A CB    1 
ATOM   2590 O OG    . SER A 1 324 ? -64.36683 55.55944 21.72187  1.000 73.64973  ? 328 SER A OG    1 
ATOM   2591 N N     . GLU A 1 325 ? -63.44866 53.31707 19.53411  1.000 63.74621  ? 329 GLU A N     1 
ATOM   2592 C CA    . GLU A 1 325 ? -62.28865 53.05237 18.68505  1.000 62.53379  ? 329 GLU A CA    1 
ATOM   2593 C C     . GLU A 1 325 ? -62.38130 51.73277 17.91837  1.000 63.28662  ? 329 GLU A C     1 
ATOM   2594 O O     . GLU A 1 325 ? -62.07638 51.69046 16.72491  1.000 68.28666  ? 329 GLU A O     1 
ATOM   2595 C CB    . GLU A 1 325 ? -60.99188 53.08609 19.51788  1.000 67.77834  ? 329 GLU A CB    1 
ATOM   2596 C CG    . GLU A 1 325 ? -60.83829 54.36689 20.36354  1.000 67.27183  ? 329 GLU A CG    1 
ATOM   2597 C CD    . GLU A 1 325 ? -59.80114 54.26037 21.49427  1.000 74.03868  ? 329 GLU A CD    1 
ATOM   2598 O OE1   . GLU A 1 325 ? -59.72675 53.20996 22.18579  1.000 74.15142  ? 329 GLU A OE1   1 
ATOM   2599 O OE2   . GLU A 1 325 ? -59.08019 55.26481 21.71502  1.000 74.41758  ? 329 GLU A OE2   1 
ATOM   2600 N N     . ALA A 1 326 ? -62.78243 50.64336 18.56194  1.000 65.62310  ? 330 ALA A N     1 
ATOM   2601 C CA    . ALA A 1 326 ? -62.79059 49.35905 17.87423  1.000 65.28613  ? 330 ALA A CA    1 
ATOM   2602 C C     . ALA A 1 326 ? -64.11797 49.02987 17.18874  1.000 67.01492  ? 330 ALA A C     1 
ATOM   2603 O O     . ALA A 1 326 ? -64.20565 47.98584 16.52095  1.000 59.09974  ? 330 ALA A O     1 
ATOM   2604 C CB    . ALA A 1 326 ? -62.44739 48.23720 18.86490  1.000 64.11212  ? 330 ALA A CB    1 
ATOM   2605 N N     . GLU A 1 327 ? -65.16269 49.84194 17.38118  1.000 58.50320  ? 331 GLU A N     1 
ATOM   2606 C CA    . GLU A 1 327 ? -66.46984 49.58627 16.77990  1.000 62.17857  ? 331 GLU A CA    1 
ATOM   2607 C C     . GLU A 1 327 ? -66.99151 50.85865 16.14606  1.000 69.77657  ? 331 GLU A C     1 
ATOM   2608 O O     . GLU A 1 327 ? -68.18065 51.18782 16.23003  1.000 73.01871  ? 331 GLU A O     1 
ATOM   2609 C CB    . GLU A 1 327 ? -67.45334 49.02674 17.80780  1.000 62.50927  ? 331 GLU A CB    1 
ATOM   2610 C CG    . GLU A 1 327 ? -67.09458 47.61897 18.32206  1.000 69.62651  ? 331 GLU A CG    1 
ATOM   2611 C CD    . GLU A 1 327 ? -67.90708 47.14582 19.54889  1.000 71.59682  ? 331 GLU A CD    1 
ATOM   2612 O OE1   . GLU A 1 327 ? -69.16666 47.20918 19.54943  1.000 77.09643  ? 331 GLU A OE1   1 
ATOM   2613 O OE2   . GLU A 1 327 ? -67.25869 46.67642 20.51303  1.000 69.58874  ? 331 GLU A OE2   1 
ATOM   2614 N N     . ALA A 1 328 ? -66.08869 51.58417 15.49686  1.000 66.70765  ? 332 ALA A N     1 
ATOM   2615 C CA    . ALA A 1 328 ? -66.34113 52.92095 14.99523  1.000 66.57623  ? 332 ALA A CA    1 
ATOM   2616 C C     . ALA A 1 328 ? -67.04687 52.84586 13.64998  1.000 65.42715  ? 332 ALA A C     1 
ATOM   2617 O O     . ALA A 1 328 ? -67.10759 51.77932 13.02900  1.000 65.85109  ? 332 ALA A O     1 
ATOM   2618 C CB    . ALA A 1 328 ? -65.01673 53.67068 14.89893  1.000 70.47741  ? 332 ALA A CB    1 
ATOM   2619 N N     . PRO A 1 329 ? -67.61688 53.95524 13.18163  1.000 58.57494  ? 333 PRO A N     1 
ATOM   2620 C CA    . PRO A 1 329 ? -68.32782 53.93616 11.88929  1.000 67.92208  ? 333 PRO A CA    1 
ATOM   2621 C C     . PRO A 1 329 ? -67.36528 53.64041 10.75832  1.000 67.01177  ? 333 PRO A C     1 
ATOM   2622 O O     . PRO A 1 329 ? -66.19682 54.06341 10.80012  1.000 63.31370  ? 333 PRO A O     1 
ATOM   2623 C CB    . PRO A 1 329 ? -68.91106 55.35134 11.76785  1.000 64.11759  ? 333 PRO A CB    1 
ATOM   2624 C CG    . PRO A 1 329 ? -68.94097 55.86154 13.17429  1.000 72.24464  ? 333 PRO A CG    1 
ATOM   2625 C CD    . PRO A 1 329 ? -67.73863 55.26180 13.84620  1.000 72.56448  ? 333 PRO A CD    1 
ATOM   2626 N N     . PRO A 1 330 ? -67.81380 52.90413 9.74544   1.000 69.38283  ? 334 PRO A N     1 
ATOM   2627 C CA    . PRO A 1 330 ? -66.90282 52.45338 8.69158   1.000 68.10884  ? 334 PRO A CA    1 
ATOM   2628 C C     . PRO A 1 330 ? -66.57806 53.59945 7.74796   1.000 67.98642  ? 334 PRO A C     1 
ATOM   2629 O O     . PRO A 1 330 ? -67.16579 54.68648 7.86401   1.000 71.53386  ? 334 PRO A O     1 
ATOM   2630 C CB    . PRO A 1 330 ? -67.70233 51.33162 8.00297   1.000 60.78839  ? 334 PRO A CB    1 
ATOM   2631 C CG    . PRO A 1 330 ? -69.13776 51.68805 8.23468   1.000 59.58739  ? 334 PRO A CG    1 
ATOM   2632 C CD    . PRO A 1 330 ? -69.17823 52.35971 9.58458   1.000 64.83112  ? 334 PRO A CD    1 
ATOM   2633 N N     . PRO A 1 331 ? -65.59881 53.43677 6.85778   1.000 69.12950  ? 335 PRO A N     1 
ATOM   2634 C CA    . PRO A 1 331 ? -65.44197 54.39189 5.75194   1.000 69.85183  ? 335 PRO A CA    1 
ATOM   2635 C C     . PRO A 1 331 ? -66.54904 54.18772 4.74213   1.000 72.32322  ? 335 PRO A C     1 
ATOM   2636 O O     . PRO A 1 331 ? -67.12926 53.11066 4.65208   1.000 69.86024  ? 335 PRO A O     1 
ATOM   2637 C CB    . PRO A 1 331 ? -64.09010 54.02864 5.14384   1.000 65.29597  ? 335 PRO A CB    1 
ATOM   2638 C CG    . PRO A 1 331 ? -63.92847 52.57410 5.45239   1.000 67.88991  ? 335 PRO A CG    1 
ATOM   2639 C CD    . PRO A 1 331 ? -64.60243 52.35305 6.80093   1.000 66.21883  ? 335 PRO A CD    1 
ATOM   2640 N N     . LYS A 1 332 ? -66.85203 55.22589 3.96884   1.000 79.07891  ? 336 LYS A N     1 
ATOM   2641 C CA    . LYS A 1 332 ? -67.93586 55.10919 2.99261   1.000 92.74530  ? 336 LYS A CA    1 
ATOM   2642 C C     . LYS A 1 332 ? -67.31462 54.87355 1.61602   1.000 94.06629  ? 336 LYS A C     1 
ATOM   2643 O O     . LYS A 1 332 ? -66.79042 55.79548 0.98819   1.000 101.24193 ? 336 LYS A O     1 
ATOM   2644 C CB    . LYS A 1 332 ? -68.87913 56.31548 3.06304   1.000 93.77275  ? 336 LYS A CB    1 
ATOM   2645 C CG    . LYS A 1 332 ? -68.44341 57.62792 2.41463   1.000 106.91672 ? 336 LYS A CG    1 
ATOM   2646 C CD    . LYS A 1 332 ? -67.36235 58.36217 3.19594   1.000 97.60833  ? 336 LYS A CD    1 
ATOM   2647 C CE    . LYS A 1 332 ? -67.18405 59.79056 2.66913   1.000 84.79149  ? 336 LYS A CE    1 
ATOM   2648 N NZ    . LYS A 1 332 ? -66.47820 60.67370 3.64290   1.000 97.70980  ? 336 LYS A NZ    1 
ATOM   2649 N N     . ILE A 1 333 ? -67.34581 53.61972 1.16298   1.000 92.71872  ? 337 ILE A N     1 
ATOM   2650 C CA    . ILE A 1 333 ? -66.70580 53.24305 -0.09664  1.000 98.65932  ? 337 ILE A CA    1 
ATOM   2651 C C     . ILE A 1 333 ? -67.65553 53.52987 -1.24972  1.000 110.02582 ? 337 ILE A C     1 
ATOM   2652 O O     . ILE A 1 333 ? -68.73156 52.91486 -1.35483  1.000 114.17267 ? 337 ILE A O     1 
ATOM   2653 C CB    . ILE A 1 333 ? -66.25583 51.77644 -0.10116  1.000 105.20047 ? 337 ILE A CB    1 
ATOM   2654 C CG1   . ILE A 1 333 ? -64.84226 51.67250 0.44791   1.000 95.41004  ? 337 ILE A CG1   1 
ATOM   2655 C CG2   . ILE A 1 333 ? -66.24463 51.21992 -1.51614  1.000 112.16323 ? 337 ILE A CG2   1 
ATOM   2656 C CD1   . ILE A 1 333 ? -63.80858 52.15179 -0.53474  1.000 100.90772 ? 337 ILE A CD1   1 
ATOM   2657 N N     . PRO A 1 334 ? -67.28877 54.46477 -2.13669  1.000 124.40147 ? 338 PRO A N     1 
ATOM   2658 C CA    . PRO A 1 334 ? -68.21644 54.88929 -3.19499  1.000 124.92447 ? 338 PRO A CA    1 
ATOM   2659 C C     . PRO A 1 334 ? -68.37133 53.84962 -4.29405  1.000 132.22697 ? 338 PRO A C     1 
ATOM   2660 O O     . PRO A 1 334 ? -67.84158 52.73614 -4.20166  1.000 127.76708 ? 338 PRO A O     1 
ATOM   2661 C CB    . PRO A 1 334 ? -67.59310 56.19402 -3.72852  1.000 122.15873 ? 338 PRO A CB    1 
ATOM   2662 C CG    . PRO A 1 334 ? -66.40646 56.51853 -2.83269  1.000 109.12666 ? 338 PRO A CG    1 
ATOM   2663 C CD    . PRO A 1 334 ? -66.03965 55.25163 -2.11820  1.000 117.05880 ? 338 PRO A CD    1 
ATOM   2664 N N     . ASP A 1 335 ? -69.12011 54.20078 -5.33888  1.000 139.23116 ? 339 ASP A N     1 
ATOM   2665 C CA    . ASP A 1 335 ? -69.33897 53.29291 -6.46326  1.000 149.27156 ? 339 ASP A CA    1 
ATOM   2666 C C     . ASP A 1 335 ? -68.12048 53.37377 -7.38713  1.000 151.05903 ? 339 ASP A C     1 
ATOM   2667 O O     . ASP A 1 335 ? -68.16307 53.88915 -8.50751  1.000 148.84103 ? 339 ASP A O     1 
ATOM   2668 C CB    . ASP A 1 335 ? -70.64110 53.63684 -7.17640  1.000 158.17228 ? 339 ASP A CB    1 
ATOM   2669 C CG    . ASP A 1 335 ? -71.39072 52.40432 -7.65933  1.000 162.23538 ? 339 ASP A CG    1 
ATOM   2670 O OD1   . ASP A 1 335 ? -71.67850 51.52162 -6.82045  1.000 163.54743 ? 339 ASP A OD1   1 
ATOM   2671 O OD2   . ASP A 1 335 ? -71.70984 52.33257 -8.86634  1.000 163.32129 ? 339 ASP A OD2   1 
ATOM   2672 N N     . LYS A 1 336 ? -66.99534 52.88863 -6.85868  1.000 135.95376 ? 340 LYS A N     1 
ATOM   2673 C CA    . LYS A 1 336 ? -65.74234 52.78506 -7.59301  1.000 126.22369 ? 340 LYS A CA    1 
ATOM   2674 C C     . LYS A 1 336 ? -65.08321 51.46190 -7.22773  1.000 127.29684 ? 340 LYS A C     1 
ATOM   2675 O O     . LYS A 1 336 ? -65.00426 51.11012 -6.04677  1.000 124.84787 ? 340 LYS A O     1 
ATOM   2676 C CB    . LYS A 1 336 ? -64.80559 53.96200 -7.28117  1.000 119.79568 ? 340 LYS A CB    1 
ATOM   2677 C CG    . LYS A 1 336 ? -65.50595 55.29634 -7.06406  1.000 117.73911 ? 340 LYS A CG    1 
ATOM   2678 C CD    . LYS A 1 336 ? -64.62118 56.43455 -7.54823  1.000 109.94616 ? 340 LYS A CD    1 
ATOM   2679 C CE    . LYS A 1 336 ? -64.89123 57.75601 -6.81259  1.000 108.29138 ? 340 LYS A CE    1 
ATOM   2680 N NZ    . LYS A 1 336 ? -65.06258 57.66125 -5.33170  1.000 109.25506 ? 340 LYS A NZ    1 
ATOM   2681 N N     . GLN A 1 337 ? -64.62122 50.72274 -8.22870  1.000 127.15679 ? 341 GLN A N     1 
ATOM   2682 C CA    . GLN A 1 337 ? -64.01616 49.41785 -8.00156  1.000 125.26479 ? 341 GLN A CA    1 
ATOM   2683 C C     . GLN A 1 337 ? -62.50160 49.55274 -8.09371  1.000 119.39307 ? 341 GLN A C     1 
ATOM   2684 O O     . GLN A 1 337 ? -61.96856 49.93218 -9.14475  1.000 123.72752 ? 341 GLN A O     1 
ATOM   2685 C CB    . GLN A 1 337 ? -64.53671 48.39003 -9.01061  1.000 138.18273 ? 341 GLN A CB    1 
ATOM   2686 C CG    . GLN A 1 337 ? -65.98423 47.93284 -8.78876  1.000 130.65577 ? 341 GLN A CG    1 
ATOM   2687 C CD    . GLN A 1 337 ? -66.13895 47.00295 -7.59507  1.000 121.64081 ? 341 GLN A CD    1 
ATOM   2688 O OE1   . GLN A 1 337 ? -65.15343 46.52967 -7.02007  1.000 120.55055 ? 341 GLN A OE1   1 
ATOM   2689 N NE2   . GLN A 1 337 ? -67.38388 46.73764 -7.21641  1.000 120.84962 ? 341 GLN A NE2   1 
ATOM   2690 N N     . LEU A 1 338 ? -61.81357 49.25363 -6.99276  1.000 108.43935 ? 342 LEU A N     1 
ATOM   2691 C CA    . LEU A 1 338 ? -60.35017 49.20396 -6.98874  1.000 106.43715 ? 342 LEU A CA    1 
ATOM   2692 C C     . LEU A 1 338 ? -59.93523 47.76543 -7.28491  1.000 109.57461 ? 342 LEU A C     1 
ATOM   2693 O O     . LEU A 1 338 ? -59.47420 47.00635 -6.42920  1.000 97.60849  ? 342 LEU A O     1 
ATOM   2694 C CB    . LEU A 1 338 ? -59.80579 49.70526 -5.65734  1.000 89.62537  ? 342 LEU A CB    1 
ATOM   2695 C CG    . LEU A 1 338 ? -60.48201 50.99504 -5.19944  1.000 89.65209  ? 342 LEU A CG    1 
ATOM   2696 C CD1   . LEU A 1 338 ? -59.76719 51.49243 -3.98234  1.000 78.66176  ? 342 LEU A CD1   1 
ATOM   2697 C CD2   . LEU A 1 338 ? -60.49726 52.08168 -6.28479  1.000 89.17982  ? 342 LEU A CD2   1 
ATOM   2698 N N     . ASP A 1 339 ? -60.15443 47.37659 -8.52470  1.000 121.12620 ? 343 ASP A N     1 
ATOM   2699 C CA    . ASP A 1 339 ? -60.17614 45.95526 -8.82508  1.000 125.59967 ? 343 ASP A CA    1 
ATOM   2700 C C     . ASP A 1 339 ? -59.16113 45.58403 -9.89052  1.000 133.09705 ? 343 ASP A C     1 
ATOM   2701 O O     . ASP A 1 339 ? -59.40708 44.68533 -10.69557 1.000 149.93473 ? 343 ASP A O     1 
ATOM   2702 C CB    . ASP A 1 339 ? -61.57866 45.51377 -9.24260  1.000 133.19736 ? 343 ASP A CB    1 
ATOM   2703 C CG    . ASP A 1 339 ? -62.10015 46.23589 -10.49886 1.000 141.04801 ? 343 ASP A CG    1 
ATOM   2704 O OD1   . ASP A 1 339 ? -61.40108 47.10689 -11.07458 1.000 139.06365 ? 343 ASP A OD1   1 
ATOM   2705 O OD2   . ASP A 1 339 ? -63.23259 45.91291 -10.91686 1.000 142.48481 ? 343 ASP A OD2   1 
ATOM   2706 N N     . GLU A 1 340 ? -58.03317 46.29394 -9.92730  1.000 117.85300 ? 344 GLU A N     1 
ATOM   2707 C CA    . GLU A 1 340 ? -56.90199 45.92864 -10.77350 1.000 118.91625 ? 344 GLU A CA    1 
ATOM   2708 C C     . GLU A 1 340 ? -57.28466 45.75344 -12.23355 1.000 119.83614 ? 344 GLU A C     1 
ATOM   2709 O O     . GLU A 1 340 ? -56.59695 45.03866 -12.97191 1.000 113.51781 ? 344 GLU A O     1 
ATOM   2710 C CB    . GLU A 1 340 ? -56.22983 44.65673 -10.26563 1.000 106.53087 ? 344 GLU A CB    1 
ATOM   2711 C CG    . GLU A 1 340 ? -56.13278 44.67256 -8.77216  1.000 107.97429 ? 344 GLU A CG    1 
ATOM   2712 C CD    . GLU A 1 340 ? -54.87659 44.03276 -8.28403  1.000 94.79933  ? 344 GLU A CD    1 
ATOM   2713 O OE1   . GLU A 1 340 ? -54.77858 43.78356 -7.06131  1.000 84.47155  ? 344 GLU A OE1   1 
ATOM   2714 O OE2   . GLU A 1 340 ? -53.99156 43.79450 -9.13255  1.000 101.24553 ? 344 GLU A OE2   1 
ATOM   2715 N N     . ARG A 1 341 ? -58.38788 46.36642 -12.65319 1.000 127.00476 ? 345 ARG A N     1 
ATOM   2716 C CA    . ARG A 1 341 ? -58.68378 46.43881 -14.07013 1.000 131.54369 ? 345 ARG A CA    1 
ATOM   2717 C C     . ARG A 1 341 ? -57.62975 47.29675 -14.75721 1.000 131.60351 ? 345 ARG A C     1 
ATOM   2718 O O     . ARG A 1 341 ? -56.84514 48.00305 -14.11413 1.000 125.11470 ? 345 ARG A O     1 
ATOM   2719 C CB    . ARG A 1 341 ? -60.08102 47.01458 -14.31225 1.000 131.77203 ? 345 ARG A CB    1 
ATOM   2720 C CG    . ARG A 1 341 ? -61.21761 46.08936 -13.93124 1.000 138.94075 ? 345 ARG A CG    1 
ATOM   2721 C CD    . ARG A 1 341 ? -62.55786 46.70097 -14.28521 1.000 142.54226 ? 345 ARG A CD    1 
ATOM   2722 N NE    . ARG A 1 341 ? -63.05344 47.54319 -13.20597 1.000 140.93876 ? 345 ARG A NE    1 
ATOM   2723 C CZ    . ARG A 1 341 ? -63.99427 48.46553 -13.35223 1.000 143.87853 ? 345 ARG A CZ    1 
ATOM   2724 N NH1   . ARG A 1 341 ? -64.58934 48.66489 -14.51793 1.000 135.38926 ? 345 ARG A NH1   1 
ATOM   2725 N NH2   . ARG A 1 341 ? -64.34013 49.21328 -12.30514 1.000 143.62030 ? 345 ARG A NH2   1 
ATOM   2726 N N     . GLU A 1 342 ? -57.61320 47.23082 -16.08213 1.000 133.14130 ? 346 GLU A N     1 
ATOM   2727 C CA    . GLU A 1 342 ? -56.69081 48.01868 -16.88383 1.000 130.26707 ? 346 GLU A CA    1 
ATOM   2728 C C     . GLU A 1 342 ? -57.46488 49.01778 -17.73051 1.000 129.60420 ? 346 GLU A C     1 
ATOM   2729 O O     . GLU A 1 342 ? -58.49117 48.67535 -18.32937 1.000 138.68586 ? 346 GLU A O     1 
ATOM   2730 C CB    . GLU A 1 342 ? -55.82447 47.12177 -17.76927 1.000 131.82752 ? 346 GLU A CB    1 
ATOM   2731 C CG    . GLU A 1 342 ? -54.74146 46.37946 -17.00089 1.000 143.35421 ? 346 GLU A CG    1 
ATOM   2732 C CD    . GLU A 1 342 ? -53.51282 46.07918 -17.84967 1.000 152.96111 ? 346 GLU A CD    1 
ATOM   2733 O OE1   . GLU A 1 342 ? -53.13989 46.94259 -18.67386 1.000 151.46186 ? 346 GLU A OE1   1 
ATOM   2734 O OE2   . GLU A 1 342 ? -52.92071 44.98315 -17.69298 1.000 157.39645 ? 346 GLU A OE2   1 
ATOM   2735 N N     . HIS A 1 343 ? -56.99353 50.25860 -17.72456 1.000 126.41223 ? 347 HIS A N     1 
ATOM   2736 C CA    . HIS A 1 343 ? -57.33288 51.28639 -18.69475 1.000 121.38338 ? 347 HIS A CA    1 
ATOM   2737 C C     . HIS A 1 343 ? -56.02196 51.79545 -19.28965 1.000 116.49266 ? 347 HIS A C     1 
ATOM   2738 O O     . HIS A 1 343 ? -54.93772 51.52974 -18.75833 1.000 114.27098 ? 347 HIS A O     1 
ATOM   2739 C CB    . HIS A 1 343 ? -58.12533 52.44784 -18.06355 1.000 115.42546 ? 347 HIS A CB    1 
ATOM   2740 C CG    . HIS A 1 343 ? -59.11712 52.03955 -17.00982 1.000 117.71839 ? 347 HIS A CG    1 
ATOM   2741 N ND1   . HIS A 1 343 ? -58.75272 51.42881 -15.82572 1.000 121.25785 ? 347 HIS A ND1   1 
ATOM   2742 C CD2   . HIS A 1 343 ? -60.46149 52.19955 -16.94815 1.000 117.98089 ? 347 HIS A CD2   1 
ATOM   2743 C CE1   . HIS A 1 343 ? -59.83058 51.21305 -15.09086 1.000 120.71239 ? 347 HIS A CE1   1 
ATOM   2744 N NE2   . HIS A 1 343 ? -60.87982 51.67577 -15.74745 1.000 119.64736 ? 347 HIS A NE2   1 
ATOM   2745 N N     . THR A 1 344 ? -56.10594 52.53825 -20.39573 1.000 111.07477 ? 348 THR A N     1 
ATOM   2746 C CA    . THR A 1 344 ? -54.87948 52.98986 -21.03862 1.000 108.31568 ? 348 THR A CA    1 
ATOM   2747 C C     . THR A 1 344 ? -54.35294 54.26826 -20.38020 1.000 103.63746 ? 348 THR A C     1 
ATOM   2748 O O     . THR A 1 344 ? -54.95512 54.82402 -19.45238 1.000 102.18845 ? 348 THR A O     1 
ATOM   2749 C CB    . THR A 1 344 ? -55.08123 53.18746 -22.54304 1.000 111.91728 ? 348 THR A CB    1 
ATOM   2750 O OG1   . THR A 1 344 ? -53.82039 53.55038 -23.13447 1.000 117.50990 ? 348 THR A OG1   1 
ATOM   2751 C CG2   . THR A 1 344 ? -56.11781 54.27423 -22.83539 1.000 100.64513 ? 348 THR A CG2   1 
ATOM   2752 N N     . ILE A 1 345 ? -53.19257 54.72659 -20.86670 1.000 101.04701 ? 349 ILE A N     1 
ATOM   2753 C CA    . ILE A 1 345 ? -52.56459 55.93117 -20.32148 1.000 105.64900 ? 349 ILE A CA    1 
ATOM   2754 C C     . ILE A 1 345 ? -53.53251 57.10793 -20.39922 1.000 104.55324 ? 349 ILE A C     1 
ATOM   2755 O O     . ILE A 1 345 ? -53.73594 57.83931 -19.42186 1.000 97.61095  ? 349 ILE A O     1 
ATOM   2756 C CB    . ILE A 1 345 ? -51.24908 56.23417 -21.06880 1.000 100.93451 ? 349 ILE A CB    1 
ATOM   2757 C CG1   . ILE A 1 345 ? -50.30803 55.01101 -21.10023 1.000 96.32702  ? 349 ILE A CG1   1 
ATOM   2758 C CG2   . ILE A 1 345 ? -50.56058 57.46298 -20.47555 1.000 97.85094  ? 349 ILE A CG2   1 
ATOM   2759 C CD1   . ILE A 1 345 ? -49.95713 54.39451 -19.74135 1.000 93.17619  ? 349 ILE A CD1   1 
ATOM   2760 N N     . GLU A 1 346 ? -54.16267 57.28319 -21.56356 1.000 114.24746 ? 350 GLU A N     1 
ATOM   2761 C CA    . GLU A 1 346 ? -55.09264 58.38686 -21.76736 1.000 110.32512 ? 350 GLU A CA    1 
ATOM   2762 C C     . GLU A 1 346 ? -56.23690 58.34807 -20.76144 1.000 109.55434 ? 350 GLU A C     1 
ATOM   2763 O O     . GLU A 1 346 ? -56.67164 59.39271 -20.25995 1.000 114.91701 ? 350 GLU A O     1 
ATOM   2764 C CB    . GLU A 1 346 ? -55.62817 58.32386 -23.19296 1.000 114.34051 ? 350 GLU A CB    1 
ATOM   2765 C CG    . GLU A 1 346 ? -56.59584 59.41597 -23.56923 1.000 122.55327 ? 350 GLU A CG    1 
ATOM   2766 C CD    . GLU A 1 346 ? -57.08104 59.24047 -24.99603 1.000 136.90531 ? 350 GLU A CD    1 
ATOM   2767 O OE1   . GLU A 1 346 ? -57.05505 58.08954 -25.49164 1.000 137.04620 ? 350 GLU A OE1   1 
ATOM   2768 O OE2   . GLU A 1 346 ? -57.47258 60.24370 -25.62695 1.000 138.26982 ? 350 GLU A OE2   1 
ATOM   2769 N N     . GLU A 1 347 ? -56.72414 57.15038 -20.44012 1.000 103.91915 ? 351 GLU A N     1 
ATOM   2770 C CA    . GLU A 1 347 ? -57.91208 57.01804 -19.60431 1.000 101.64035 ? 351 GLU A CA    1 
ATOM   2771 C C     . GLU A 1 347 ? -57.59842 57.19914 -18.12434 1.000 100.37466 ? 351 GLU A C     1 
ATOM   2772 O O     . GLU A 1 347 ? -58.35141 57.87310 -17.40860 1.000 100.77518 ? 351 GLU A O     1 
ATOM   2773 C CB    . GLU A 1 347 ? -58.54566 55.65521 -19.84686 1.000 110.32339 ? 351 GLU A CB    1 
ATOM   2774 C CG    . GLU A 1 347 ? -58.93799 55.43399 -21.28447 1.000 114.11191 ? 351 GLU A CG    1 
ATOM   2775 C CD    . GLU A 1 347 ? -59.46107 54.03728 -21.53311 1.000 115.96716 ? 351 GLU A CD    1 
ATOM   2776 O OE1   . GLU A 1 347 ? -58.71735 53.06049 -21.27897 1.000 114.36233 ? 351 GLU A OE1   1 
ATOM   2777 O OE2   . GLU A 1 347 ? -60.62129 53.92112 -21.98115 1.000 120.18540 ? 351 GLU A OE2   1 
ATOM   2778 N N     . TRP A 1 348 ? -56.50663 56.58302 -17.65056 1.000 100.94809 ? 352 TRP A N     1 
ATOM   2779 C CA    . TRP A 1 348 ? -56.03386 56.80006 -16.28238 1.000 93.89281  ? 352 TRP A CA    1 
ATOM   2780 C C     . TRP A 1 348 ? -55.85160 58.27771 -15.99088 1.000 91.69839  ? 352 TRP A C     1 
ATOM   2781 O O     . TRP A 1 348 ? -56.12805 58.73957 -14.87666 1.000 87.32105  ? 352 TRP A O     1 
ATOM   2782 C CB    . TRP A 1 348 ? -54.70139 56.09086 -16.06930 1.000 88.18281  ? 352 TRP A CB    1 
ATOM   2783 C CG    . TRP A 1 348 ? -54.81690 54.67009 -15.68418 1.000 93.67228  ? 352 TRP A CG    1 
ATOM   2784 C CD1   . TRP A 1 348 ? -54.31692 53.59083 -16.36520 1.000 96.88465  ? 352 TRP A CD1   1 
ATOM   2785 C CD2   . TRP A 1 348 ? -55.44388 54.14832 -14.50632 1.000 94.99613  ? 352 TRP A CD2   1 
ATOM   2786 N NE1   . TRP A 1 348 ? -54.61101 52.42426 -15.68765 1.000 102.28464 ? 352 TRP A NE1   1 
ATOM   2787 C CE2   . TRP A 1 348 ? -55.29963 52.74004 -14.54366 1.000 99.14969  ? 352 TRP A CE2   1 
ATOM   2788 C CE3   . TRP A 1 348 ? -56.12051 54.72974 -13.42872 1.000 87.54200  ? 352 TRP A CE3   1 
ATOM   2789 C CZ2   . TRP A 1 348 ? -55.80997 51.91308 -13.54651 1.000 91.27202  ? 352 TRP A CZ2   1 
ATOM   2790 C CZ3   . TRP A 1 348 ? -56.62465 53.90430 -12.43970 1.000 84.45529  ? 352 TRP A CZ3   1 
ATOM   2791 C CH2   . TRP A 1 348 ? -56.46819 52.51310 -12.50661 1.000 87.00318  ? 352 TRP A CH2   1 
ATOM   2792 N N     . LYS A 1 349 ? -55.36426 59.03109 -16.98212 1.000 91.45591  ? 353 LYS A N     1 
ATOM   2793 C CA    . LYS A 1 349 ? -55.14057 60.45426 -16.78253 1.000 94.27827  ? 353 LYS A CA    1 
ATOM   2794 C C     . LYS A 1 349 ? -56.43591 61.14745 -16.40445 1.000 91.66140  ? 353 LYS A C     1 
ATOM   2795 O O     . LYS A 1 349 ? -56.47219 61.93406 -15.45040 1.000 92.13946  ? 353 LYS A O     1 
ATOM   2796 C CB    . LYS A 1 349 ? -54.54179 61.07743 -18.04419 1.000 98.19948  ? 353 LYS A CB    1 
ATOM   2797 C CG    . LYS A 1 349 ? -53.97051 62.47626 -17.83101 1.000 95.59829  ? 353 LYS A CG    1 
ATOM   2798 C CD    . LYS A 1 349 ? -53.05146 62.88032 -18.98644 1.000 102.38327 ? 353 LYS A CD    1 
ATOM   2799 C CE    . LYS A 1 349 ? -52.45675 64.28417 -18.78308 1.000 105.21438 ? 353 LYS A CE    1 
ATOM   2800 N NZ    . LYS A 1 349 ? -51.47115 64.70353 -19.83886 1.000 105.68041 ? 353 LYS A NZ    1 
ATOM   2801 N N     . GLU A 1 350 ? -57.51982 60.84207 -17.12118 1.000 96.23112  ? 354 GLU A N     1 
ATOM   2802 C CA    . GLU A 1 350 ? -58.80661 61.43903 -16.78488 1.000 98.28181  ? 354 GLU A CA    1 
ATOM   2803 C C     . GLU A 1 350 ? -59.28285 60.97822 -15.41147 1.000 95.43035  ? 354 GLU A C     1 
ATOM   2804 O O     . GLU A 1 350 ? -59.70548 61.80351 -14.59166 1.000 95.41129  ? 354 GLU A O     1 
ATOM   2805 C CB    . GLU A 1 350 ? -59.84162 61.10789 -17.86166 1.000 108.49865 ? 354 GLU A CB    1 
ATOM   2806 C CG    . GLU A 1 350 ? -61.27780 61.51255 -17.50965 1.000 117.73056 ? 354 GLU A CG    1 
ATOM   2807 C CD    . GLU A 1 350 ? -61.96835 62.31878 -18.61444 1.000 129.80790 ? 354 GLU A CD    1 
ATOM   2808 O OE1   . GLU A 1 350 ? -61.42818 62.38649 -19.74193 1.000 134.35715 ? 354 GLU A OE1   1 
ATOM   2809 O OE2   . GLU A 1 350 ? -63.05962 62.87900 -18.35812 1.000 133.24265 ? 354 GLU A OE2   1 
ATOM   2810 N N     . LEU A 1 351 ? -59.19202 59.66935 -15.13037 1.000 97.23372  ? 355 LEU A N     1 
ATOM   2811 C CA    . LEU A 1 351 ? -59.66624 59.14841 -13.84994 1.000 87.58044  ? 355 LEU A CA    1 
ATOM   2812 C C     . LEU A 1 351 ? -58.98050 59.84680 -12.68757 1.000 85.73952  ? 355 LEU A C     1 
ATOM   2813 O O     . LEU A 1 351 ? -59.62707 60.23190 -11.70805 1.000 83.56612  ? 355 LEU A O     1 
ATOM   2814 C CB    . LEU A 1 351 ? -59.42139 57.64262 -13.76882 1.000 84.84847  ? 355 LEU A CB    1 
ATOM   2815 C CG    . LEU A 1 351 ? -60.33824 56.77196 -14.62151 1.000 97.80343  ? 355 LEU A CG    1 
ATOM   2816 C CD1   . LEU A 1 351 ? -60.09444 55.27019 -14.36410 1.000 92.66888  ? 355 LEU A CD1   1 
ATOM   2817 C CD2   . LEU A 1 351 ? -61.80218 57.16176 -14.39522 1.000 96.82991  ? 355 LEU A CD2   1 
ATOM   2818 N N     . ILE A 1 352 ? -57.66728 60.02238 -12.78602 1.000 87.04551  ? 356 ILE A N     1 
ATOM   2819 C CA    . ILE A 1 352 ? -56.90395 60.63430 -11.70853 1.000 83.40871  ? 356 ILE A CA    1 
ATOM   2820 C C     . ILE A 1 352 ? -57.18921 62.13258 -11.61502 1.000 85.19930  ? 356 ILE A C     1 
ATOM   2821 O O     . ILE A 1 352 ? -57.22015 62.70603 -10.51565 1.000 78.36094  ? 356 ILE A O     1 
ATOM   2822 C CB    . ILE A 1 352 ? -55.41497 60.33391 -11.92573 1.000 78.98003  ? 356 ILE A CB    1 
ATOM   2823 C CG1   . ILE A 1 352 ? -55.20653 58.84142 -11.74465 1.000 78.55119  ? 356 ILE A CG1   1 
ATOM   2824 C CG2   . ILE A 1 352 ? -54.55389 61.12981 -10.95658 1.000 70.68963  ? 356 ILE A CG2   1 
ATOM   2825 C CD1   . ILE A 1 352 ? -53.91404 58.34420 -12.27756 1.000 85.64381  ? 356 ILE A CD1   1 
ATOM   2826 N N     . TYR A 1 353 ? -57.38428 62.79274 -12.76260 1.000 82.13843  ? 357 TYR A N     1 
ATOM   2827 C CA    . TYR A 1 353 ? -57.65616 64.22799 -12.75417 1.000 84.64769  ? 357 TYR A CA    1 
ATOM   2828 C C     . TYR A 1 353 ? -59.00741 64.52148 -12.11847 1.000 94.40507  ? 357 TYR A C     1 
ATOM   2829 O O     . TYR A 1 353 ? -59.12862 65.43846 -11.29350 1.000 95.49177  ? 357 TYR A O     1 
ATOM   2830 C CB    . TYR A 1 353 ? -57.59368 64.78253 -14.18067 1.000 84.23374  ? 357 TYR A CB    1 
ATOM   2831 C CG    . TYR A 1 353 ? -57.62042 66.30556 -14.30177 1.000 93.60395  ? 357 TYR A CG    1 
ATOM   2832 C CD1   . TYR A 1 353 ? -56.77004 67.10978 -13.54662 1.000 92.27748  ? 357 TYR A CD1   1 
ATOM   2833 C CD2   . TYR A 1 353 ? -58.46992 66.93121 -15.20562 1.000 89.38973  ? 357 TYR A CD2   1 
ATOM   2834 C CE1   . TYR A 1 353 ? -56.79202 68.48975 -13.67735 1.000 90.84906  ? 357 TYR A CE1   1 
ATOM   2835 C CE2   . TYR A 1 353 ? -58.48911 68.30340 -15.34230 1.000 92.78719  ? 357 TYR A CE2   1 
ATOM   2836 C CZ    . TYR A 1 353 ? -57.65140 69.07894 -14.57831 1.000 94.52554  ? 357 TYR A CZ    1 
ATOM   2837 O OH    . TYR A 1 353 ? -57.68552 70.45040 -14.72194 1.000 106.27766 ? 357 TYR A OH    1 
ATOM   2838 N N     . LYS A 1 354 ? -60.03262 63.73484 -12.47574 1.000 91.92646  ? 358 LYS A N     1 
ATOM   2839 C CA    . LYS A 1 354 ? -61.36269 63.93557 -11.90687 1.000 89.28460  ? 358 LYS A CA    1 
ATOM   2840 C C     . LYS A 1 354 ? -61.33774 63.77552 -10.38869 1.000 95.60975  ? 358 LYS A C     1 
ATOM   2841 O O     . LYS A 1 354 ? -61.95323 64.56832 -9.66290  1.000 99.75537  ? 358 LYS A O     1 
ATOM   2842 C CB    . LYS A 1 354 ? -62.36019 62.96125 -12.54252 1.000 88.06495  ? 358 LYS A CB    1 
ATOM   2843 C CG    . LYS A 1 354 ? -63.35674 63.62812 -13.49778 1.000 103.91868 ? 358 LYS A CG    1 
ATOM   2844 C CD    . LYS A 1 354 ? -64.23455 62.60655 -14.22942 1.000 104.86159 ? 358 LYS A CD    1 
ATOM   2845 C CE    . LYS A 1 354 ? -64.70757 63.12662 -15.57495 1.000 103.69403 ? 358 LYS A CE    1 
ATOM   2846 N NZ    . LYS A 1 354 ? -64.72663 62.05816 -16.61876 1.000 116.04715 ? 358 LYS A NZ    1 
ATOM   2847 N N     . GLU A 1 355 ? -60.60385 62.77349 -9.88617  1.000 92.48510  ? 359 GLU A N     1 
ATOM   2848 C CA    . GLU A 1 355 ? -60.53420 62.56929 -8.44115  1.000 92.11628  ? 359 GLU A CA    1 
ATOM   2849 C C     . GLU A 1 355 ? -59.90595 63.76814 -7.74714  1.000 87.75603  ? 359 GLU A C     1 
ATOM   2850 O O     . GLU A 1 355 ? -60.33276 64.15388 -6.65365  1.000 91.45085  ? 359 GLU A O     1 
ATOM   2851 C CB    . GLU A 1 355 ? -59.75853 61.29235 -8.10719  1.000 85.90885  ? 359 GLU A CB    1 
ATOM   2852 C CG    . GLU A 1 355 ? -60.63030 60.03841 -7.99664  1.000 81.18294  ? 359 GLU A CG    1 
ATOM   2853 C CD    . GLU A 1 355 ? -61.75242 60.16468 -6.95984  1.000 94.13783  ? 359 GLU A CD    1 
ATOM   2854 O OE1   . GLU A 1 355 ? -61.48888 60.56120 -5.79957  1.000 93.39003  ? 359 GLU A OE1   1 
ATOM   2855 O OE2   . GLU A 1 355 ? -62.91148 59.86582 -7.31057  1.000 103.19616 ? 359 GLU A OE2   1 
ATOM   2856 N N     . VAL A 1 356 ? -58.89495 64.37560 -8.36474  1.000 86.32330  ? 360 VAL A N     1 
ATOM   2857 C CA    . VAL A 1 356 ? -58.27858 65.54344 -7.74715  1.000 84.07767  ? 360 VAL A CA    1 
ATOM   2858 C C     . VAL A 1 356 ? -59.24450 66.72267 -7.72945  1.000 85.69213  ? 360 VAL A C     1 
ATOM   2859 O O     . VAL A 1 356 ? -59.28963 67.48454 -6.75684  1.000 90.07717  ? 360 VAL A O     1 
ATOM   2860 C CB    . VAL A 1 356 ? -56.96704 65.89526 -8.46315  1.000 83.42532  ? 360 VAL A CB    1 
ATOM   2861 C CG1   . VAL A 1 356 ? -56.27450 67.02025 -7.73632  1.000 87.23948  ? 360 VAL A CG1   1 
ATOM   2862 C CG2   . VAL A 1 356 ? -56.07186 64.68273 -8.50749  1.000 81.03935  ? 360 VAL A CG2   1 
ATOM   2863 N N     . MET A 1 357 ? -60.03555 66.89280 -8.79217  1.000 86.59785  ? 361 MET A N     1 
ATOM   2864 C CA    . MET A 1 357 ? -60.86649 68.08271 -8.92198  1.000 93.15994  ? 361 MET A CA    1 
ATOM   2865 C C     . MET A 1 357 ? -62.24437 67.96230 -8.27805  1.000 103.10851 ? 361 MET A C     1 
ATOM   2866 O O     . MET A 1 357 ? -62.86682 68.99226 -7.99887  1.000 107.18175 ? 361 MET A O     1 
ATOM   2867 C CB    . MET A 1 357 ? -61.06213 68.45212 -10.39989 1.000 94.99317  ? 361 MET A CB    1 
ATOM   2868 C CG    . MET A 1 357 ? -59.79258 68.53746 -11.23769 1.000 95.86555  ? 361 MET A CG    1 
ATOM   2869 S SD    . MET A 1 357 ? -58.57738 69.76120 -10.68466 1.000 113.16473 ? 361 MET A SD    1 
ATOM   2870 C CE    . MET A 1 357 ? -59.60438 71.14447 -10.19914 1.000 102.52165 ? 361 MET A CE    1 
ATOM   2871 N N     . ASP A 1 358 ? -62.76416 66.75283 -8.07325  1.000 105.26542 ? 362 ASP A N     1 
ATOM   2872 C CA    . ASP A 1 358 ? -64.13867 66.61012 -7.59343  1.000 113.24018 ? 362 ASP A CA    1 
ATOM   2873 C C     . ASP A 1 358 ? -64.22615 66.69518 -6.06926  1.000 122.73872 ? 362 ASP A C     1 
ATOM   2874 O O     . ASP A 1 358 ? -64.84578 67.61713 -5.52877  1.000 130.29655 ? 362 ASP A O     1 
ATOM   2875 C CB    . ASP A 1 358 ? -64.73628 65.29504 -8.10790  1.000 134.84617 ? 362 ASP A CB    1 
ATOM   2876 C CG    . ASP A 1 358 ? -66.17670 65.07476 -7.64787  1.000 145.66107 ? 362 ASP A CG    1 
ATOM   2877 O OD1   . ASP A 1 358 ? -66.93233 66.07127 -7.56380  1.000 145.59694 ? 362 ASP A OD1   1 
ATOM   2878 O OD2   . ASP A 1 358 ? -66.55564 63.90576 -7.38068  1.000 145.83591 ? 362 ASP A OD2   1 
ATOM   2879 N N     . LEU A 1 359 ? -63.59801 65.75551 -5.36544  1.000 126.74876 ? 363 LEU A N     1 
ATOM   2880 C CA    . LEU A 1 359 ? -63.67264 65.71698 -3.90232  1.000 135.54375 ? 363 LEU A CA    1 
ATOM   2881 C C     . LEU A 1 359 ? -62.29157 65.87475 -3.27073  1.000 130.30156 ? 363 LEU A C     1 
ATOM   2882 O O     . LEU A 1 359 ? -61.71109 66.96406 -3.27793  1.000 127.42887 ? 363 LEU A O     1 
ATOM   2883 C CB    . LEU A 1 359 ? -64.32173 64.41144 -3.42328  1.000 125.15068 ? 363 LEU A CB    1 
ATOM   2884 N N     . ARG B 2 1   ? -58.31330 49.03721 35.59500  1.000 110.06966 ? 157 ARG B N     1 
ATOM   2885 C CA    . ARG B 2 1   ? -57.89316 49.35476 34.22667  1.000 115.23059 ? 157 ARG B CA    1 
ATOM   2886 C C     . ARG B 2 1   ? -56.69991 50.31019 34.25938  1.000 108.70550 ? 157 ARG B C     1 
ATOM   2887 O O     . ARG B 2 1   ? -56.78013 51.37029 34.87428  1.000 110.77329 ? 157 ARG B O     1 
ATOM   2888 C CB    . ARG B 2 1   ? -59.05420 49.96768 33.41862  1.000 110.55501 ? 157 ARG B CB    1 
ATOM   2889 C CG    . ARG B 2 1   ? -59.18751 49.45685 31.96318  1.000 114.71568 ? 157 ARG B CG    1 
ATOM   2890 C CD    . ARG B 2 1   ? -59.61310 47.97385 31.90400  1.000 117.60874 ? 157 ARG B CD    1 
ATOM   2891 N NE    . ARG B 2 1   ? -60.02712 47.50219 30.57913  1.000 119.61730 ? 157 ARG B NE    1 
ATOM   2892 C CZ    . ARG B 2 1   ? -60.44989 46.26507 30.31781  1.000 117.16810 ? 157 ARG B CZ    1 
ATOM   2893 N NH1   . ARG B 2 1   ? -60.50594 45.33697 31.26274  1.000 119.12654 ? 157 ARG B NH1   1 
ATOM   2894 N NH2   . ARG B 2 1   ? -60.82872 45.94826 29.07652  1.000 98.03986  ? 157 ARG B NH2   1 
ATOM   2895 N N     . PRO B 2 2   ? -55.60154 49.93240 33.60481  1.000 107.63714 ? 158 PRO B N     1 
ATOM   2896 C CA    . PRO B 2 2   ? -54.39442 50.76330 33.63875  1.000 104.84167 ? 158 PRO B CA    1 
ATOM   2897 C C     . PRO B 2 2   ? -54.49626 51.97782 32.72480  1.000 99.40687  ? 158 PRO B C     1 
ATOM   2898 O O     . PRO B 2 2   ? -55.11113 51.94087 31.65523  1.000 98.79032  ? 158 PRO B O     1 
ATOM   2899 C CB    . PRO B 2 2   ? -53.30463 49.80339 33.14966  1.000 104.30443 ? 158 PRO B CB    1 
ATOM   2900 C CG    . PRO B 2 2   ? -54.02998 48.95085 32.15807  1.000 101.38828 ? 158 PRO B CG    1 
ATOM   2901 C CD    . PRO B 2 2   ? -55.41580 48.74439 32.75083  1.000 106.67619 ? 158 PRO B CD    1 
ATOM   2902 N N     . LYS B 2 3   ? -53.86647 53.06717 33.16370  1.000 99.24108  ? 159 LYS B N     1 
ATOM   2903 C CA    . LYS B 2 3   ? -53.88400 54.30890 32.39997  1.000 96.06362  ? 159 LYS B CA    1 
ATOM   2904 C C     . LYS B 2 3   ? -53.11384 54.14438 31.09428  1.000 89.56128  ? 159 LYS B C     1 
ATOM   2905 O O     . LYS B 2 3   ? -52.02874 53.55735 31.05584  1.000 89.72151  ? 159 LYS B O     1 
ATOM   2906 C CB    . LYS B 2 3   ? -53.28363 55.44144 33.22742  1.000 106.45577 ? 159 LYS B CB    1 
ATOM   2907 C CG    . LYS B 2 3   ? -53.48110 56.84099 32.64791  1.000 118.98386 ? 159 LYS B CG    1 
ATOM   2908 C CD    . LYS B 2 3   ? -54.92230 57.33064 32.75340  1.000 124.98794 ? 159 LYS B CD    1 
ATOM   2909 C CE    . LYS B 2 3   ? -54.99882 58.83314 32.48405  1.000 128.20746 ? 159 LYS B CE    1 
ATOM   2910 N NZ    . LYS B 2 3   ? -56.32466 59.41602 32.83251  1.000 122.97099 ? 159 LYS B NZ    1 
ATOM   2911 N N     . ARG B 2 4   ? -53.68047 54.65919 30.01957  1.000 86.24170  ? 160 ARG B N     1 
ATOM   2912 C CA    . ARG B 2 4   ? -53.00484 54.57419 28.73868  1.000 81.65526  ? 160 ARG B CA    1 
ATOM   2913 C C     . ARG B 2 4   ? -51.72707 55.40519 28.75305  1.000 79.80536  ? 160 ARG B C     1 
ATOM   2914 O O     . ARG B 2 4   ? -51.69612 56.48341 29.35238  1.000 83.74528  ? 160 ARG B O     1 
ATOM   2915 C CB    . ARG B 2 4   ? -53.90438 55.07772 27.63260  1.000 79.64308  ? 160 ARG B CB    1 
ATOM   2916 C CG    . ARG B 2 4   ? -55.06340 54.20047 27.35459  1.000 78.30256  ? 160 ARG B CG    1 
ATOM   2917 C CD    . ARG B 2 4   ? -55.96611 54.93010 26.44154  1.000 65.53108  ? 160 ARG B CD    1 
ATOM   2918 N NE    . ARG B 2 4   ? -57.08795 54.09492 26.08579  1.000 69.44685  ? 160 ARG B NE    1 
ATOM   2919 C CZ    . ARG B 2 4   ? -57.64356 54.11670 24.89057  1.000 72.96078  ? 160 ARG B CZ    1 
ATOM   2920 N NH1   . ARG B 2 4   ? -57.22565 54.95660 23.96022  1.000 72.17013  ? 160 ARG B NH1   1 
ATOM   2921 N NH2   . ARG B 2 4   ? -58.62733 53.26076 24.61556  1.000 70.49091  ? 160 ARG B NH2   1 
ATOM   2922 N N     . PRO B 2 5   ? -50.66751 54.93754 28.09969  1.000 77.10309  ? 161 PRO B N     1 
ATOM   2923 C CA    . PRO B 2 5   ? -49.44918 55.75074 27.99620  1.000 71.68819  ? 161 PRO B CA    1 
ATOM   2924 C C     . PRO B 2 5   ? -49.70501 57.02274 27.20045  1.000 80.09398  ? 161 PRO B C     1 
ATOM   2925 O O     . PRO B 2 5   ? -50.44083 57.01832 26.21133  1.000 85.54929  ? 161 PRO B O     1 
ATOM   2926 C CB    . PRO B 2 5   ? -48.45403 54.83462 27.27513  1.000 73.40064  ? 161 PRO B CB    1 
ATOM   2927 C CG    . PRO B 2 5   ? -49.23520 53.68017 26.75752  1.000 76.84952  ? 161 PRO B CG    1 
ATOM   2928 C CD    . PRO B 2 5   ? -50.60943 53.68567 27.32732  1.000 78.25047  ? 161 PRO B CD    1 
ATOM   2929 N N     . THR B 2 6   ? -49.07112 58.11901 27.63445  1.000 77.07316  ? 162 THR B N     1 
ATOM   2930 C CA    . THR B 2 6   ? -49.15763 59.39765 26.94319  1.000 83.11644  ? 162 THR B CA    1 
ATOM   2931 C C     . THR B 2 6   ? -47.84382 59.84202 26.30872  1.000 83.66171  ? 162 THR B C     1 
ATOM   2932 O O     . THR B 2 6   ? -47.83896 60.81369 25.53577  1.000 81.12283  ? 162 THR B O     1 
ATOM   2933 C CB    . THR B 2 6   ? -49.62023 60.49991 27.90774  1.000 81.85785  ? 162 THR B CB    1 
ATOM   2934 O OG1   . THR B 2 6   ? -48.83913 60.44472 29.10730  1.000 82.82305  ? 162 THR B OG1   1 
ATOM   2935 C CG2   . THR B 2 6   ? -51.10519 60.31071 28.24042  1.000 85.86799  ? 162 THR B CG2   1 
ATOM   2936 N N     . THR B 2 7   ? -46.73135 59.19281 26.62323  1.000 78.01505  ? 163 THR B N     1 
ATOM   2937 C CA    . THR B 2 7   ? -45.45264 59.60793 26.07117  1.000 87.30002  ? 163 THR B CA    1 
ATOM   2938 C C     . THR B 2 7   ? -44.76021 58.40800 25.44245  1.000 79.34032  ? 163 THR B C     1 
ATOM   2939 O O     . THR B 2 7   ? -44.84088 57.29902 25.97383  1.000 76.64063  ? 163 THR B O     1 
ATOM   2940 C CB    . THR B 2 7   ? -44.57147 60.27698 27.15731  1.000 80.89464  ? 163 THR B CB    1 
ATOM   2941 O OG1   . THR B 2 7   ? -43.93064 59.28259 27.96144  1.000 92.68214  ? 163 THR B OG1   1 
ATOM   2942 C CG2   . THR B 2 7   ? -45.41121 61.17949 28.05501  1.000 82.35676  ? 163 THR B CG2   1 
ATOM   2943 N N     . LEU B 2 8   ? -44.11261 58.63134 24.29299  1.000 77.22433  ? 164 LEU B N     1 
ATOM   2944 C CA    . LEU B 2 8   ? -43.33631 57.60112 23.60426  1.000 79.62930  ? 164 LEU B CA    1 
ATOM   2945 C C     . LEU B 2 8   ? -42.07887 58.23333 23.01693  1.000 82.87963  ? 164 LEU B C     1 
ATOM   2946 O O     . LEU B 2 8   ? -42.17137 59.12779 22.16883  1.000 81.23409  ? 164 LEU B O     1 
ATOM   2947 C CB    . LEU B 2 8   ? -44.15658 56.93525 22.50120  1.000 73.07819  ? 164 LEU B CB    1 
ATOM   2948 C CG    . LEU B 2 8   ? -43.39213 56.11651 21.45336  1.000 73.53326  ? 164 LEU B CG    1 
ATOM   2949 C CD1   . LEU B 2 8   ? -43.18465 54.71304 21.99985  1.000 63.97571  ? 164 LEU B CD1   1 
ATOM   2950 C CD2   . LEU B 2 8   ? -44.12416 56.05012 20.14506  1.000 65.32297  ? 164 LEU B CD2   1 
ATOM   2951 N N     . ASN B 2 9   ? -40.91188 57.74656 23.43339  1.000 81.36368  ? 165 ASN B N     1 
ATOM   2952 C CA    . ASN B 2 9   ? -39.64131 58.33876 23.01521  1.000 87.53645  ? 165 ASN B CA    1 
ATOM   2953 C C     . ASN B 2 9   ? -39.17398 57.76720 21.69270  1.000 89.54223  ? 165 ASN B C     1 
ATOM   2954 O O     . ASN B 2 9   ? -39.04879 56.54909 21.53689  1.000 96.24565  ? 165 ASN B O     1 
ATOM   2955 C CB    . ASN B 2 9   ? -38.56513 58.10555 24.06258  1.000 88.34841  ? 165 ASN B CB    1 
ATOM   2956 C CG    . ASN B 2 9   ? -38.89766 58.77238 25.35174  1.000 97.17521  ? 165 ASN B CG    1 
ATOM   2957 O OD1   . ASN B 2 9   ? -39.32186 59.93602 25.36200  1.000 100.49298 ? 165 ASN B OD1   1 
ATOM   2958 N ND2   . ASN B 2 9   ? -38.73534 58.05239 26.45466  1.000 104.82239 ? 165 ASN B ND2   1 
ATOM   2959 N N     . LEU B 2 10  ? -38.89063 58.65027 20.75262  1.000 80.35878  ? 166 LEU B N     1 
ATOM   2960 C CA    . LEU B 2 10  ? -38.59049 58.23132 19.40044  1.000 79.02412  ? 166 LEU B CA    1 
ATOM   2961 C C     . LEU B 2 10  ? -37.09448 58.16301 19.11281  1.000 83.79286  ? 166 LEU B C     1 
ATOM   2962 O O     . LEU B 2 10  ? -36.70630 57.73943 18.01965  1.000 86.38516  ? 166 LEU B O     1 
ATOM   2963 C CB    . LEU B 2 10  ? -39.29341 59.16841 18.42168  1.000 68.60241  ? 166 LEU B CB    1 
ATOM   2964 C CG    . LEU B 2 10  ? -40.81958 59.21025 18.57298  1.000 78.12217  ? 166 LEU B CG    1 
ATOM   2965 C CD1   . LEU B 2 10  ? -41.41920 60.01957 17.46588  1.000 71.05084  ? 166 LEU B CD1   1 
ATOM   2966 C CD2   . LEU B 2 10  ? -41.45726 57.80255 18.60270  1.000 79.86575  ? 166 LEU B CD2   1 
ATOM   2967 N N     . PHE B 2 11  ? -36.24838 58.56091 20.05381  1.000 80.36183  ? 167 PHE B N     1 
ATOM   2968 C CA    . PHE B 2 11  ? -34.82078 58.52915 19.78850  1.000 93.25836  ? 167 PHE B CA    1 
ATOM   2969 C C     . PHE B 2 11  ? -34.12440 57.86140 20.96479  1.000 110.14458 ? 167 PHE B C     1 
ATOM   2970 O O     . PHE B 2 11  ? -34.52184 58.05932 22.12153  1.000 114.24085 ? 167 PHE B O     1 
ATOM   2971 C CB    . PHE B 2 11  ? -34.26948 59.94964 19.54337  1.000 80.92054  ? 167 PHE B CB    1 
ATOM   2972 C CG    . PHE B 2 11  ? -34.73989 60.55844 18.24123  1.000 76.88156  ? 167 PHE B CG    1 
ATOM   2973 C CD1   . PHE B 2 11  ? -34.02208 60.37651 17.06471  1.000 73.45901  ? 167 PHE B CD1   1 
ATOM   2974 C CD2   . PHE B 2 11  ? -35.93560 61.26115 18.18000  1.000 77.43240  ? 167 PHE B CD2   1 
ATOM   2975 C CE1   . PHE B 2 11  ? -34.47611 60.92313 15.85188  1.000 84.81515  ? 167 PHE B CE1   1 
ATOM   2976 C CE2   . PHE B 2 11  ? -36.40582 61.79227 16.97058  1.000 78.83764  ? 167 PHE B CE2   1 
ATOM   2977 C CZ    . PHE B 2 11  ? -35.67728 61.61943 15.80123  1.000 74.65149  ? 167 PHE B CZ    1 
ATOM   2978 N N     . PRO B 2 12  ? -33.11117 57.04263 20.70458  1.000 127.78527 ? 168 PRO B N     1 
ATOM   2979 C CA    . PRO B 2 12  ? -32.54073 56.22400 21.77553  1.000 134.49880 ? 168 PRO B CA    1 
ATOM   2980 C C     . PRO B 2 12  ? -31.71982 57.05744 22.74467  1.000 139.17012 ? 168 PRO B C     1 
ATOM   2981 O O     . PRO B 2 12  ? -31.30211 58.18136 22.45464  1.000 135.35291 ? 168 PRO B O     1 
ATOM   2982 C CB    . PRO B 2 12  ? -31.65820 55.21003 21.03499  1.000 138.46549 ? 168 PRO B CB    1 
ATOM   2983 C CG    . PRO B 2 12  ? -31.63782 55.63073 19.58486  1.000 129.03437 ? 168 PRO B CG    1 
ATOM   2984 C CD    . PRO B 2 12  ? -32.36421 56.92699 19.44001  1.000 115.44042 ? 168 PRO B CD    1 
ATOM   2985 N N     . GLN B 2 13  ? -31.52624 56.48997 23.93312  1.000 149.62915 ? 169 GLN B N     1 
ATOM   2986 C CA    . GLN B 2 13  ? -30.51652 56.95267 24.87631  1.000 159.95162 ? 169 GLN B CA    1 
ATOM   2987 C C     . GLN B 2 13  ? -29.51468 55.85689 25.21022  1.000 166.55744 ? 169 GLN B C     1 
ATOM   2988 O O     . GLN B 2 13  ? -28.30188 56.10171 25.16614  1.000 167.38742 ? 169 GLN B O     1 
ATOM   2989 C CB    . GLN B 2 13  ? -31.18424 57.48834 26.15470  1.000 158.31607 ? 169 GLN B CB    1 
ATOM   2990 C CG    . GLN B 2 13  ? -30.29049 58.38421 27.01538  1.000 161.40483 ? 169 GLN B CG    1 
ATOM   2991 C CD    . GLN B 2 13  ? -30.05144 59.75956 26.40424  1.000 154.46329 ? 169 GLN B CD    1 
ATOM   2992 O OE1   . GLN B 2 13  ? -29.44831 59.88359 25.33662  1.000 144.32177 ? 169 GLN B OE1   1 
ATOM   2993 N NE2   . GLN B 2 13  ? -30.52277 60.80126 27.08583  1.000 150.73720 ? 169 GLN B NE2   1 
ATOM   2994 N N     . VAL B 2 14  ? -29.99342 54.64640 25.52242  1.000 164.45191 ? 170 VAL B N     1 
ATOM   2995 C CA    . VAL B 2 14  ? -29.16104 53.48144 25.87059  1.000 161.94452 ? 170 VAL B CA    1 
ATOM   2996 C C     . VAL B 2 14  ? -28.25785 53.76151 27.07625  1.000 159.85175 ? 170 VAL B C     1 
ATOM   2997 O O     . VAL B 2 14  ? -28.44915 53.19662 28.15840  1.000 149.93467 ? 170 VAL B O     1 
ATOM   2998 C CB    . VAL B 2 14  ? -28.31833 53.00501 24.65172  1.000 160.76534 ? 170 VAL B CB    1 
ATOM   2999 C CG1   . VAL B 2 14  ? -27.35705 51.88467 25.05851  1.000 153.17462 ? 170 VAL B CG1   1 
ATOM   3000 C CG2   . VAL B 2 14  ? -29.23032 52.55421 23.50826  1.000 151.48615 ? 170 VAL B CG2   1 
ATOM   3001 N N     . SER B 2 30  ? -40.53053 42.74756 -10.55551 1.000 136.98530 ? 210 SER B N     1 
ATOM   3002 C CA    . SER B 2 30  ? -40.10832 41.65533 -11.43249 1.000 149.16469 ? 210 SER B CA    1 
ATOM   3003 C C     . SER B 2 30  ? -40.72668 40.32350 -11.00690 1.000 150.02808 ? 210 SER B C     1 
ATOM   3004 O O     . SER B 2 30  ? -41.08465 39.50073 -11.85529 1.000 153.89450 ? 210 SER B O     1 
ATOM   3005 C CB    . SER B 2 30  ? -38.57852 41.52406 -11.45432 1.000 149.73119 ? 210 SER B CB    1 
ATOM   3006 O OG    . SER B 2 30  ? -38.06417 41.14182 -10.18613 1.000 142.22569 ? 210 SER B OG    1 
ATOM   3007 N N     . ILE B 2 31  ? -40.83200 40.11328 -9.69274  1.000 148.12484 ? 211 ILE B N     1 
ATOM   3008 C CA    . ILE B 2 31  ? -41.32703 38.86426 -9.11183  1.000 146.17774 ? 211 ILE B CA    1 
ATOM   3009 C C     . ILE B 2 31  ? -42.41732 39.19989 -8.08584  1.000 141.76237 ? 211 ILE B C     1 
ATOM   3010 O O     . ILE B 2 31  ? -42.17213 39.97053 -7.14571  1.000 128.83726 ? 211 ILE B O     1 
ATOM   3011 C CB    . ILE B 2 31  ? -40.18256 38.04780 -8.47083  1.000 143.14956 ? 211 ILE B CB    1 
ATOM   3012 C CG1   . ILE B 2 31  ? -39.01827 37.85561 -9.45174  1.000 152.48801 ? 211 ILE B CG1   1 
ATOM   3013 C CG2   . ILE B 2 31  ? -40.65794 36.67500 -8.03496  1.000 143.42218 ? 211 ILE B CG2   1 
ATOM   3014 C CD1   . ILE B 2 31  ? -39.32335 36.91985 -10.62529 1.000 150.56260 ? 211 ILE B CD1   1 
ATOM   3015 N N     . CYS B 2 32  ? -43.62323 38.63154 -8.27945  1.000 151.57376 ? 212 CYS B N     1 
ATOM   3016 C CA    . CYS B 2 32  ? -44.78073 38.78468 -7.38534  1.000 138.84771 ? 212 CYS B CA    1 
ATOM   3017 C C     . CYS B 2 32  ? -45.04496 37.57621 -6.49421  1.000 132.56168 ? 212 CYS B C     1 
ATOM   3018 O O     . CYS B 2 32  ? -45.53072 37.75499 -5.37324  1.000 124.19919 ? 212 CYS B O     1 
ATOM   3019 C CB    . CYS B 2 32  ? -46.06986 39.05214 -8.17851  1.000 129.70815 ? 212 CYS B CB    1 
ATOM   3020 S SG    . CYS B 2 32  ? -46.07246 40.49986 -9.24446  1.000 137.53055 ? 212 CYS B SG    1 
ATOM   3021 N N     . LEU B 2 33  ? -44.78276 36.35448 -6.97428  1.000 123.37616 ? 213 LEU B N     1 
ATOM   3022 C CA    . LEU B 2 33  ? -45.01620 35.13441 -6.20672  1.000 115.74468 ? 213 LEU B CA    1 
ATOM   3023 C C     . LEU B 2 33  ? -43.86387 34.16444 -6.45023  1.000 119.53547 ? 213 LEU B C     1 
ATOM   3024 O O     . LEU B 2 33  ? -43.06638 34.33745 -7.37751  1.000 126.10135 ? 213 LEU B O     1 
ATOM   3025 C CB    . LEU B 2 33  ? -46.36635 34.47921 -6.56312  1.000 108.92386 ? 213 LEU B CB    1 
ATOM   3026 C CG    . LEU B 2 33  ? -46.53708 33.63427 -7.83352  1.000 115.03308 ? 213 LEU B CG    1 
ATOM   3027 C CD1   . LEU B 2 33  ? -47.58622 32.54009 -7.59300  1.000 107.42885 ? 213 LEU B CD1   1 
ATOM   3028 C CD2   . LEU B 2 33  ? -46.89484 34.48051 -9.05153  1.000 114.41976 ? 213 LEU B CD2   1 
ATOM   3029 N N     . SER B 2 34  ? -43.78179 33.11070 -5.59701  1.000 113.16119 ? 214 SER B N     1 
ATOM   3030 C CA    . SER B 2 34  ? -42.70493 32.10219 -5.64684  1.000 111.24545 ? 214 SER B CA    1 
ATOM   3031 C C     . SER B 2 34  ? -42.82471 31.18612 -6.82203  1.000 125.89118 ? 214 SER B C     1 
ATOM   3032 O O     . SER B 2 34  ? -42.07390 30.20540 -6.82757  1.000 132.93517 ? 214 SER B O     1 
ATOM   3033 C CB    . SER B 2 34  ? -42.67735 31.26791 -4.35922  1.000 106.31042 ? 214 SER B CB    1 
ATOM   3034 O OG    . SER B 2 34  ? -41.56462 30.37696 -4.30970  1.000 105.95093 ? 214 SER B OG    1 
ATOM   3035 N N     . ASP B 2 35  ? -43.72887 31.47709 -7.76256  1.000 134.35529 ? 215 ASP B N     1 
ATOM   3036 C CA    . ASP B 2 35  ? -43.95883 30.66074 -8.94853  1.000 139.56451 ? 215 ASP B CA    1 
ATOM   3037 C C     . ASP B 2 35  ? -43.28402 31.21716 -10.20268 1.000 148.12273 ? 215 ASP B C     1 
ATOM   3038 O O     . ASP B 2 35  ? -43.14538 30.48408 -11.18998 1.000 154.92217 ? 215 ASP B O     1 
ATOM   3039 C CB    . ASP B 2 35  ? -45.47843 30.49723 -9.16417  1.000 137.18632 ? 215 ASP B CB    1 
ATOM   3040 C CG    . ASP B 2 35  ? -45.85466 30.03901 -10.56549 1.000 151.82255 ? 215 ASP B CG    1 
ATOM   3041 O OD1   . ASP B 2 35  ? -45.84897 30.88296 -11.49571 1.000 152.00941 ? 215 ASP B OD1   1 
ATOM   3042 O OD2   . ASP B 2 35  ? -46.17515 28.83606 -10.73108 1.000 149.00345 ? 215 ASP B OD2   1 
ATOM   3043 N N     . GLU B 2 36  ? -42.82652 32.47110 -10.18433 1.000 146.63740 ? 216 GLU B N     1 
ATOM   3044 C CA    . GLU B 2 36  ? -42.12615 33.03919 -11.33388 1.000 153.33444 ? 216 GLU B CA    1 
ATOM   3045 C C     . GLU B 2 36  ? -40.62780 32.75049 -11.35541 1.000 157.86498 ? 216 GLU B C     1 
ATOM   3046 O O     . GLU B 2 36  ? -39.97346 33.06702 -12.35792 1.000 158.89145 ? 216 GLU B O     1 
ATOM   3047 C CB    . GLU B 2 36  ? -42.34285 34.54454 -11.37196 1.000 150.75243 ? 216 GLU B CB    1 
ATOM   3048 C CG    . GLU B 2 36  ? -43.64755 34.94136 -10.76829 1.000 144.39377 ? 216 GLU B CG    1 
ATOM   3049 C CD    . GLU B 2 36  ? -43.82026 36.42491 -10.76118 1.000 149.87107 ? 216 GLU B CD    1 
ATOM   3050 O OE1   . GLU B 2 36  ? -43.76721 37.04559 -11.84409 1.000 153.04688 ? 216 GLU B OE1   1 
ATOM   3051 O OE2   . GLU B 2 36  ? -43.99977 36.97467 -9.66091  1.000 155.33888 ? 216 GLU B OE2   1 
ATOM   3052 N N     . LEU B 2 37  ? -40.06171 32.22718 -10.26368 1.000 158.71812 ? 217 LEU B N     1 
ATOM   3053 C CA    . LEU B 2 37  ? -38.66805 31.78581 -10.18059 1.000 166.46371 ? 217 LEU B CA    1 
ATOM   3054 C C     . LEU B 2 37  ? -38.39465 30.35625 -10.68031 1.000 168.64826 ? 217 LEU B C     1 
ATOM   3055 O O     . LEU B 2 37  ? -37.40854 30.15891 -11.40560 1.000 172.61024 ? 217 LEU B O     1 
ATOM   3056 C CB    . LEU B 2 37  ? -38.18429 31.98131 -8.74251  1.000 162.96729 ? 217 LEU B CB    1 
ATOM   3057 C CG    . LEU B 2 37  ? -38.46904 33.44398 -8.37876  1.000 161.02040 ? 217 LEU B CG    1 
ATOM   3058 C CD1   . LEU B 2 37  ? -38.80904 33.59186 -6.92278  1.000 158.26180 ? 217 LEU B CD1   1 
ATOM   3059 C CD2   . LEU B 2 37  ? -37.31160 34.36530 -8.77571  1.000 168.34443 ? 217 LEU B CD2   1 
ATOM   3060 N N     . PRO B 2 38  ? -39.20697 29.32230 -10.31993 1.000 157.14599 ? 218 PRO B N     1 
ATOM   3061 C CA    . PRO B 2 38  ? -38.93969 27.94229 -10.78394 1.000 151.68328 ? 218 PRO B CA    1 
ATOM   3062 C C     . PRO B 2 38  ? -38.80012 27.71784 -12.30543 1.000 148.68149 ? 218 PRO B C     1 
ATOM   3063 O O     . PRO B 2 38  ? -37.97685 26.91680 -12.76794 1.000 140.32604 ? 218 PRO B O     1 
ATOM   3064 C CB    . PRO B 2 38  ? -40.16095 27.17551 -10.26946 1.000 142.02722 ? 218 PRO B CB    1 
ATOM   3065 C CG    . PRO B 2 38  ? -40.51623 27.85682 -9.01015  1.000 137.48715 ? 218 PRO B CG    1 
ATOM   3066 C CD    . PRO B 2 38  ? -40.25115 29.32559 -9.27165  1.000 150.06621 ? 218 PRO B CD    1 
ATOM   3067 O OXT   . PRO B 2 38  ? -39.51337 28.30479 -13.11891 1.000 151.47608 ? 218 PRO B OXT   1 
HETATM 3068 P PG    . ANP C 3 .   ? -44.57594 54.95593 -0.86659  1.000 83.43007  ? 401 ANP A PG    1 
HETATM 3069 O O1G   . ANP C 3 .   ? -44.33184 53.90046 -1.89699  1.000 118.48561 ? 401 ANP A O1G   1 
HETATM 3070 O O2G   . ANP C 3 .   ? -44.13020 56.36368 -1.37779  1.000 76.29007  ? 401 ANP A O2G   1 
HETATM 3071 O O3G   . ANP C 3 .   ? -46.11788 55.06974 -0.60711  1.000 97.56007  ? 401 ANP A O3G   1 
HETATM 3072 P PB    . ANP C 3 .   ? -44.48679 53.80662 1.76028   1.000 88.48007  ? 401 ANP A PB    1 
HETATM 3073 O O1B   . ANP C 3 .   ? -44.95680 52.47309 1.28423   1.000 84.52007  ? 401 ANP A O1B   1 
HETATM 3074 O O2B   . ANP C 3 .   ? -43.48421 53.37793 2.89123   1.000 88.68007  ? 401 ANP A O2B   1 
HETATM 3075 N N3B   . ANP C 3 .   ? -43.68840 54.62136 0.52910   1.000 91.63019  ? 401 ANP A N3B   1 
HETATM 3076 P PA    . ANP C 3 .   ? -45.60865 56.43895 2.09516   1.000 68.47331  ? 401 ANP A PA    1 
HETATM 3077 O O1A   . ANP C 3 .   ? -45.16747 56.87647 0.77912   1.000 71.79482  ? 401 ANP A O1A   1 
HETATM 3078 O O2A   . ANP C 3 .   ? -46.99337 57.03358 2.38438   1.000 70.66007  ? 401 ANP A O2A   1 
HETATM 3079 O O3A   . ANP C 3 .   ? -45.57042 54.80572 2.33955   1.000 75.82007  ? 401 ANP A O3A   1 
HETATM 3080 O "O5'" . ANP C 3 .   ? -44.55208 57.10876 3.08812   1.000 83.45162  ? 401 ANP A "O5'" 1 
HETATM 3081 C "C5'" . ANP C 3 .   ? -43.11965 57.21223 2.87408   1.000 69.76007  ? 401 ANP A "C5'" 1 
HETATM 3082 C "C4'" . ANP C 3 .   ? -42.49760 57.64643 4.18507   1.000 74.09637  ? 401 ANP A "C4'" 1 
HETATM 3083 O "O4'" . ANP C 3 .   ? -42.71957 59.06124 4.37074   1.000 67.06014  ? 401 ANP A "O4'" 1 
HETATM 3084 C "C3'" . ANP C 3 .   ? -43.06636 56.96947 5.43145   1.000 68.01007  ? 401 ANP A "C3'" 1 
HETATM 3085 O "O3'" . ANP C 3 .   ? -42.30031 55.83680 5.81708   1.000 72.12007  ? 401 ANP A "O3'" 1 
HETATM 3086 C "C2'" . ANP C 3 .   ? -42.92160 58.04594 6.50730   1.000 68.06007  ? 401 ANP A "C2'" 1 
HETATM 3087 O "O2'" . ANP C 3 .   ? -41.62784 58.02317 7.09369   1.000 77.00007  ? 401 ANP A "O2'" 1 
HETATM 3088 C "C1'" . ANP C 3 .   ? -43.08625 59.33874 5.71148   1.000 71.62909  ? 401 ANP A "C1'" 1 
HETATM 3089 N N9    . ANP C 3 .   ? -44.43843 59.87930 5.73613   1.000 65.74885  ? 401 ANP A N9    1 
HETATM 3090 C C8    . ANP C 3 .   ? -45.38800 59.81110 4.74921   1.000 68.95989  ? 401 ANP A C8    1 
HETATM 3091 N N7    . ANP C 3 .   ? -46.52877 60.39247 5.04993   1.000 70.05335  ? 401 ANP A N7    1 
HETATM 3092 C C5    . ANP C 3 .   ? -46.30260 60.88471 6.33363   1.000 55.80706  ? 401 ANP A C5    1 
HETATM 3093 C C6    . ANP C 3 .   ? -47.12581 61.60542 7.22115   1.000 57.46007  ? 401 ANP A C6    1 
HETATM 3094 N N6    . ANP C 3 .   ? -48.37976 61.96683 6.94784   1.000 64.40007  ? 401 ANP A N6    1 
HETATM 3095 N N1    . ANP C 3 .   ? -46.60142 61.93508 8.42628   1.000 62.23007  ? 401 ANP A N1    1 
HETATM 3096 C C2    . ANP C 3 .   ? -45.35126 61.56378 8.70922   1.000 61.29007  ? 401 ANP A C2    1 
HETATM 3097 N N3    . ANP C 3 .   ? -44.48988 60.88137 7.95250   1.000 57.63269  ? 401 ANP A N3    1 
HETATM 3098 C C4    . ANP C 3 .   ? -45.03313 60.57188 6.76634   1.000 63.92445  ? 401 ANP A C4    1 
HETATM 3099 O O     . HOH D 4 .   ? -51.82767 23.97857 -0.58064  1.000 95.07007  ? 501 HOH A O     1 
HETATM 3100 O O     . HOH D 4 .   ? -52.23277 40.70216 -1.16797  1.000 88.47007  ? 502 HOH A O     1 
HETATM 3101 O O     . HOH D 4 .   ? -47.45839 44.20757 -0.41553  1.000 76.19007  ? 503 HOH A O     1 
HETATM 3102 O O     . HOH D 4 .   ? -45.20552 36.32564 31.47216  1.000 95.19138  ? 504 HOH A O     1 
HETATM 3103 O O     . HOH D 4 .   ? -66.41813 55.92111 17.29834  1.000 67.65007  ? 505 HOH A O     1 
HETATM 3104 O O     . HOH D 4 .   ? -48.34521 58.98319 3.09224   1.000 60.09007  ? 506 HOH A O     1 
HETATM 3105 O O     . HOH D 4 .   ? -65.03474 68.64476 -3.26304  1.000 110.44174 ? 507 HOH A O     1 
HETATM 3106 O O     . HOH D 4 .   ? -54.99378 19.57647 -4.23075  1.000 83.38007  ? 508 HOH A O     1 
HETATM 3107 O O     . HOH D 4 .   ? -69.65510 55.05179 8.15525   1.000 76.13007  ? 509 HOH A O     1 
HETATM 3108 O O     . HOH D 4 .   ? -42.08604 41.77412 -3.47558  1.000 119.01007 ? 510 HOH A O     1 
HETATM 3109 O O     . HOH D 4 .   ? -57.76544 37.93058 -4.46481  1.000 80.40007  ? 511 HOH A O     1 
HETATM 3110 O O     . HOH D 4 .   ? -64.40099 61.93535 4.42599   1.000 93.58007  ? 512 HOH A O     1 
HETATM 3111 O O     . HOH D 4 .   ? -40.30038 22.00617 4.00512   1.000 98.18330  ? 513 HOH A O     1 
HETATM 3112 O O     . HOH D 4 .   ? -55.88365 60.21973 12.16078  1.000 71.32241  ? 514 HOH A O     1 
HETATM 3113 O O     . HOH D 4 .   ? -43.74741 40.28913 37.74860  1.000 141.71215 ? 515 HOH A O     1 
HETATM 3114 O O     . HOH D 4 .   ? -63.90665 44.87862 17.92555  1.000 75.62007  ? 516 HOH A O     1 
HETATM 3115 O O     . HOH D 4 .   ? -64.76617 55.87440 12.08290  1.000 72.00007  ? 517 HOH A O     1 
HETATM 3116 O O     . HOH D 4 .   ? -55.84907 32.56607 2.07071   1.000 75.88007  ? 518 HOH A O     1 
HETATM 3117 O O     . HOH D 4 .   ? -48.15176 27.80423 10.98382  1.000 67.25623  ? 519 HOH A O     1 
HETATM 3118 O O     . HOH D 4 .   ? -63.74571 36.16377 -11.72387 1.000 78.43007  ? 520 HOH A O     1 
HETATM 3119 O O     . HOH D 4 .   ? -44.89813 78.47040 -9.70133  1.000 95.31200  ? 521 HOH A O     1 
HETATM 3120 O O     . HOH D 4 .   ? -64.49186 43.17763 24.68303  1.000 80.25462  ? 522 HOH A O     1 
HETATM 3121 O O     . HOH D 4 .   ? -36.61025 41.17028 31.06368  1.000 106.00418 ? 523 HOH A O     1 
HETATM 3122 O O     . HOH D 4 .   ? -64.36527 47.22887 -0.41364  1.000 70.89007  ? 524 HOH A O     1 
HETATM 3123 O O     . HOH D 4 .   ? -51.88888 49.77528 0.30045   1.000 68.61007  ? 525 HOH A O     1 
HETATM 3124 O O     . HOH D 4 .   ? -56.05637 35.21209 3.83535   1.000 71.60007  ? 526 HOH A O     1 
HETATM 3125 O O     . HOH D 4 .   ? -33.56295 29.90851 5.79393   1.000 98.00192  ? 527 HOH A O     1 
HETATM 3126 O O     . HOH D 4 .   ? -54.27033 58.36016 16.81253  1.000 81.02007  ? 528 HOH A O     1 
HETATM 3127 O O     . HOH D 4 .   ? -59.28237 60.81198 6.49558   1.000 93.88007  ? 529 HOH A O     1 
HETATM 3128 O O     . HOH D 4 .   ? -40.70983 75.80968 1.23666   1.000 90.36007  ? 530 HOH A O     1 
HETATM 3129 O O     . HOH D 4 .   ? -40.02761 41.19531 35.95157  1.000 120.90951 ? 531 HOH A O     1 
HETATM 3130 O O     . HOH D 4 .   ? -51.63386 80.05207 -10.66227 1.000 115.09805 ? 532 HOH A O     1 
HETATM 3131 O O     . HOH D 4 .   ? -44.10896 42.88928 2.89115   1.000 80.15007  ? 533 HOH A O     1 
HETATM 3132 O O     . HOH D 4 .   ? -46.75668 43.79331 3.64382   1.000 81.80007  ? 534 HOH A O     1 
HETATM 3133 O O     . HOH D 4 .   ? -64.97359 52.75762 -3.81043  1.000 115.07922 ? 535 HOH A O     1 
HETATM 3134 O O     . HOH D 4 .   ? -45.45819 57.69154 -11.26535 1.000 94.15322  ? 536 HOH A O     1 
HETATM 3135 O O     . HOH D 4 .   ? -51.42150 42.91873 -9.72745  1.000 79.75807  ? 537 HOH A O     1 
HETATM 3136 O O     . HOH D 4 .   ? -66.90804 57.37409 8.55701   1.000 69.04007  ? 538 HOH A O     1 
HETATM 3137 O O     . HOH D 4 .   ? -63.27927 44.12315 26.82501  1.000 88.48007  ? 539 HOH A O     1 
HETATM 3138 O O     . HOH D 4 .   ? -43.06679 20.87170 -10.94352 1.000 91.63624  ? 540 HOH A O     1 
HETATM 3139 O O     . HOH D 4 .   ? -61.92424 50.02123 14.19659  1.000 69.35007  ? 541 HOH A O     1 
HETATM 3140 O O     . HOH D 4 .   ? -50.59757 43.74001 4.79852   1.000 64.66007  ? 542 HOH A O     1 
HETATM 3141 O O     . HOH D 4 .   ? -69.49434 37.74434 -5.32544  1.000 82.70007  ? 543 HOH A O     1 
HETATM 3142 O O     . HOH D 4 .   ? -62.58238 51.45138 -11.92922 1.000 107.47853 ? 544 HOH A O     1 
HETATM 3143 O O     . HOH D 4 .   ? -66.11599 58.14750 5.97668   1.000 93.34007  ? 545 HOH A O     1 
HETATM 3144 O O     . HOH D 4 .   ? -58.73219 35.78419 -2.91754  1.000 72.54007  ? 546 HOH A O     1 
HETATM 3145 O O     . HOH D 4 .   ? -63.58626 42.42209 19.07623  1.000 74.41007  ? 547 HOH A O     1 
HETATM 3146 O O     . HOH D 4 .   ? -58.56162 59.15575 8.89528   1.000 75.99007  ? 548 HOH A O     1 
HETATM 3147 O O     . HOH D 4 .   ? -63.39741 58.36985 -2.79317  1.000 80.77007  ? 549 HOH A O     1 
HETATM 3148 O O     . HOH D 4 .   ? -38.82941 57.92982 10.13258  1.000 73.31007  ? 550 HOH A O     1 
HETATM 3149 O O     . HOH D 4 .   ? -70.088   45.068   21.301    1.000 83.23007  ? 551 HOH A O     1 
HETATM 3150 O O     . HOH D 4 .   ? -64.56466 51.24060 11.70643  1.000 75.33007  ? 552 HOH A O     1 
HETATM 3151 O O     . HOH D 4 .   ? -59.16773 70.94757 0.75734   1.000 103.39007 ? 553 HOH A O     1 
HETATM 3152 O O     . HOH D 4 .   ? -40.91991 39.72679 8.71961   1.000 71.29174  ? 554 HOH A O     1 
HETATM 3153 O O     . HOH D 4 .   ? -42.71581 15.00083 -0.21945  1.000 108.41911 ? 555 HOH A O     1 
HETATM 3154 O O     . HOH D 4 .   ? -51.10227 57.71960 2.97380   1.000 70.02007  ? 556 HOH A O     1 
HETATM 3155 O O     . HOH D 4 .   ? -39.57433 44.70116 24.41044  1.000 99.97762  ? 557 HOH A O     1 
HETATM 3156 O O     . HOH D 4 .   ? -60.09288 50.50683 -11.39673 1.000 106.08086 ? 558 HOH A O     1 
HETATM 3157 O O     . HOH D 4 .   ? -42.61544 62.30982 -6.95903  1.000 87.86007  ? 559 HOH A O     1 
HETATM 3158 O O     . HOH D 4 .   ? -41.89810 52.39525 -0.59016  1.000 84.98614  ? 560 HOH A O     1 
HETATM 3159 O O     . HOH D 4 .   ? -49.77363 29.51367 23.73152  1.000 85.44675  ? 561 HOH A O     1 
HETATM 3160 O O     . HOH D 4 .   ? -40.59308 41.16177 10.87963  1.000 77.56716  ? 562 HOH A O     1 
HETATM 3161 O O     . HOH D 4 .   ? -48.48404 87.63431 -8.05680  1.000 107.79999 ? 563 HOH A O     1 
HETATM 3162 O O     . HOH D 4 .   ? -50.12570 24.30396 8.65353   1.000 75.90007  ? 564 HOH A O     1 
HETATM 3163 O O     . HOH D 4 .   ? -54.33301 27.63486 -5.74836  1.000 72.20361  ? 565 HOH A O     1 
HETATM 3164 O O     . HOH D 4 .   ? -40.77234 48.50223 6.34477   1.000 55.82007  ? 566 HOH A O     1 
HETATM 3165 O O     . HOH D 4 .   ? -34.41277 30.72591 15.64334  1.000 97.20781  ? 567 HOH A O     1 
HETATM 3166 O O     . HOH D 4 .   ? -49.28556 37.75747 -4.82718  1.000 130.24007 ? 568 HOH A O     1 
HETATM 3167 O O     . HOH D 4 .   ? -37.04981 18.39671 11.15797  1.000 101.08790 ? 569 HOH A O     1 
HETATM 3168 O O     . HOH D 4 .   ? -47.56554 33.46985 32.99994  1.000 88.58007  ? 570 HOH A O     1 
HETATM 3169 O O     . HOH D 4 .   ? -61.81169 57.49024 15.61182  1.000 60.60007  ? 571 HOH A O     1 
HETATM 3170 O O     . HOH D 4 .   ? -57.14214 74.29233 -1.51027  1.000 86.16007  ? 572 HOH A O     1 
HETATM 3171 O O     . HOH D 4 .   ? -54.69233 22.62835 -7.42146  1.000 94.03007  ? 573 HOH A O     1 
HETATM 3172 O O     . HOH D 4 .   ? -50.50988 26.60705 10.21980  1.000 73.01299  ? 574 HOH A O     1 
HETATM 3173 O O     . HOH D 4 .   ? -70.18845 47.11883 22.61525  1.000 84.75007  ? 575 HOH A O     1 
HETATM 3174 O O     . HOH D 4 .   ? -65.01278 68.05437 -10.28681 1.000 100.77669 ? 576 HOH A O     1 
HETATM 3175 O O     . HOH D 4 .   ? -48.85729 70.60587 14.11419  1.000 82.99007  ? 577 HOH A O     1 
HETATM 3176 O O     . HOH D 4 .   ? -36.27503 68.27575 7.75218   1.000 73.93007  ? 578 HOH A O     1 
HETATM 3177 O O     . HOH D 4 .   ? -59.09924 38.90286 9.67498   1.000 77.63007  ? 579 HOH A O     1 
HETATM 3178 O O     . HOH D 4 .   ? -37.64891 48.49103 9.87805   1.000 91.54602  ? 580 HOH A O     1 
HETATM 3179 O O     . HOH D 4 .   ? -52.64786 23.06555 7.44353   1.000 100.94007 ? 581 HOH A O     1 
HETATM 3180 O O     . HOH D 4 .   ? -45.70227 23.30806 12.68615  1.000 91.71116  ? 582 HOH A O     1 
HETATM 3181 O O     . HOH D 4 .   ? -59.74735 30.88371 12.63713  1.000 81.85007  ? 583 HOH A O     1 
HETATM 3182 O O     . HOH D 4 .   ? -51.43711 64.20541 14.87071  1.000 98.50007  ? 584 HOH A O     1 
HETATM 3183 O O     . HOH D 4 .   ? -40.02123 64.31242 -8.99858  1.000 110.02007 ? 585 HOH A O     1 
HETATM 3184 O O     . HOH D 4 .   ? -64.51373 65.94268 -11.72318 1.000 97.90007  ? 586 HOH A O     1 
HETATM 3185 O O     . HOH D 4 .   ? -32.13731 45.29075 21.51209  1.000 94.52888  ? 587 HOH A O     1 
HETATM 3186 O O     . HOH D 4 .   ? -55.84121 75.46737 -20.45761 1.000 107.44995 ? 588 HOH A O     1 
HETATM 3187 O O     . HOH D 4 .   ? -54.71175 80.38705 -12.54230 1.000 101.96658 ? 589 HOH A O     1 
HETATM 3188 O O     . HOH D 4 .   ? -62.68873 63.70340 7.10149   1.000 93.91477  ? 590 HOH A O     1 
HETATM 3189 O O     . HOH D 4 .   ? -60.26110 62.30377 8.39679   1.000 99.56007  ? 591 HOH A O     1 
HETATM 3190 O O     . HOH D 4 .   ? -33.63603 43.49513 29.35130  1.000 99.74741  ? 592 HOH A O     1 
HETATM 3191 O O     . HOH D 4 .   ? -67.80319 44.21299 4.29413   1.000 99.91007  ? 593 HOH A O     1 
HETATM 3192 O O     . HOH D 4 .   ? -68.32955 49.18981 -0.00073  1.000 98.98432  ? 594 HOH A O     1 
HETATM 3193 O O     . HOH D 4 .   ? -32.37916 31.39630 -5.89572  1.000 97.32952  ? 595 HOH A O     1 
HETATM 3194 O O     . HOH D 4 .   ? -54.25154 62.43763 -22.15710 1.000 99.07436  ? 596 HOH A O     1 
HETATM 3195 O O     . HOH D 4 .   ? -53.40519 84.14123 6.96295   1.000 96.01924  ? 597 HOH A O     1 
HETATM 3196 O O     . HOH D 4 .   ? -43.10764 47.62503 -10.41633 1.000 89.92195  ? 598 HOH A O     1 
HETATM 3197 O O     . HOH D 4 .   ? -70.21105 36.94453 -2.97187  1.000 81.85452  ? 599 HOH A O     1 
HETATM 3198 O O     . HOH D 4 .   ? -67.36596 59.36939 11.73701  1.000 85.73960  ? 600 HOH A O     1 
HETATM 3199 O O     . HOH D 4 .   ? -62.45550 64.06298 4.63234   1.000 98.81946  ? 601 HOH A O     1 
HETATM 3200 O O     . HOH D 4 .   ? -41.70374 26.30922 28.11599  1.000 104.14445 ? 602 HOH A O     1 
HETATM 3201 O O     . HOH D 4 .   ? -58.46463 75.29804 -19.54449 1.000 103.46571 ? 603 HOH A O     1 
HETATM 3202 O O     . HOH D 4 .   ? -36.47063 47.42757 5.33832   1.000 85.19007  ? 604 HOH A O     1 
HETATM 3203 O O     . HOH D 4 .   ? -54.68515 87.62993 -12.37458 1.000 117.55917 ? 605 HOH A O     1 
HETATM 3204 O O     . HOH D 4 .   ? -30.15540 56.02609 12.69577  1.000 95.58007  ? 606 HOH A O     1 
HETATM 3205 O O     . HOH D 4 .   ? -43.61893 82.19485 -2.08106  1.000 102.72007 ? 607 HOH A O     1 
HETATM 3206 O O     . HOH D 4 .   ? -56.92830 78.20290 -4.65254  1.000 94.19764  ? 608 HOH A O     1 
HETATM 3207 O O     . HOH D 4 .   ? -34.68243 36.49891 15.38789  1.000 99.02490  ? 609 HOH A O     1 
HETATM 3208 O O     . HOH D 4 .   ? -56.08541 82.36363 16.97906  1.000 96.05931  ? 610 HOH A O     1 
HETATM 3209 O O     . HOH D 4 .   ? -47.75453 23.93344 14.94118  1.000 90.61545  ? 611 HOH A O     1 
HETATM 3210 O O     . HOH D 4 .   ? -68.54700 61.84141 -1.11920  1.000 93.15747  ? 612 HOH A O     1 
HETATM 3211 O O     . HOH D 4 .   ? -36.05419 45.35685 35.82438  1.000 83.72974  ? 613 HOH A O     1 
HETATM 3212 O O     . HOH D 4 .   ? -58.64688 77.45127 -2.26132  1.000 93.43404  ? 614 HOH A O     1 
HETATM 3213 O O     . HOH D 4 .   ? -55.04979 79.32995 -17.00809 1.000 101.33827 ? 615 HOH A O     1 
HETATM 3214 O O     . HOH D 4 .   ? -42.84839 86.26241 -7.95045  1.000 86.94460  ? 616 HOH A O     1 
HETATM 3215 O O     . HOH E 4 .   ? -35.79958 57.03763 23.24538  1.000 104.87007 ? 301 HOH B O     1 
HETATM 3216 O O     . HOH E 4 .   ? -58.18793 48.51226 37.96175  1.000 113.41007 ? 302 HOH B O     1 
HETATM 3217 O O     . HOH E 4 .   ? -58.18136 52.21108 28.09212  1.000 78.49007  ? 303 HOH B O     1 
HETATM 3218 O O     . HOH E 4 .   ? -55.70149 47.97611 36.89657  1.000 96.48942  ? 304 HOH B O     1 
HETATM 3219 O O     . HOH E 4 .   ? -46.52946 37.60750 -14.32565 1.000 104.45398 ? 305 HOH B O     1 
HETATM 3220 O O     . HOH E 4 .   ? -58.893   57.814   26.218    1.000 95.46645  ? 306 HOH B O     1 
HETATM 3221 O O     . HOH E 4 .   ? -25.86109 50.85209 32.49571  1.000 89.10423  ? 307 HOH B 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   . ASP A 3   ? 2.02604 1.47031 1.88278 -0.40090 -0.40924 0.29787  7   ASP A N   
2    C CA  . ASP A 3   ? 2.07907 1.52732 1.91982 -0.39148 -0.40618 0.30174  7   ASP A CA  
3    C C   . ASP A 3   ? 2.12233 1.63085 1.96051 -0.37718 -0.36573 0.28542  7   ASP A C   
4    O O   . ASP A 3   ? 2.06640 1.58545 1.91482 -0.35245 -0.35922 0.27212  7   ASP A O   
5    C CB  . ASP A 3   ? 2.10098 1.52494 1.89634 -0.42544 -0.42135 0.33575  7   ASP A CB  
6    N N   . ASN A 4   ? 2.23521 1.78306 2.06200 -0.39282 -0.33985 0.28627  8   ASN A N   
7    C CA  . ASN A 4   ? 2.16988 1.77431 1.99251 -0.38223 -0.30288 0.27272  8   ASN A CA  
8    C C   . ASN A 4   ? 2.00156 1.63176 1.86180 -0.35437 -0.28765 0.24432  8   ASN A C   
9    O O   . ASN A 4   ? 1.92075 1.55593 1.79555 -0.35981 -0.28663 0.23899  8   ASN A O   
10   C CB  . ASN A 4   ? 2.14811 1.78584 1.94073 -0.41263 -0.28242 0.28710  8   ASN A CB  
11   C CG  . ASN A 4   ? 2.18925 1.86800 1.96001 -0.40919 -0.25517 0.28394  8   ASN A CG  
12   O OD1 . ASN A 4   ? 2.21030 1.87459 1.96423 -0.40431 -0.26232 0.28922  8   ASN A OD1 
13   N ND2 . ASN A 4   ? 2.06630 1.79600 1.83849 -0.41131 -0.22514 0.27441  8   ASN A ND2 
14   N N   . ASN A 5   ? 1.72850 1.37589 1.60251 -0.32628 -0.27589 0.22697  9   ASN A N   
15   C CA  . ASN A 5   ? 1.62993 1.30029 1.53696 -0.29895 -0.26256 0.20082  9   ASN A CA  
16   C C   . ASN A 5   ? 1.42980 1.15326 1.33370 -0.29688 -0.22963 0.19159  9   ASN A C   
17   O O   . ASN A 5   ? 1.26005 1.00589 1.18730 -0.27567 -0.21693 0.17142  9   ASN A O   
18   C CB  . ASN A 5   ? 1.50916 1.17103 1.43399 -0.27125 -0.26783 0.18805  9   ASN A CB  
19   C CG  . ASN A 5   ? 1.68202 1.29532 1.60396 -0.27493 -0.29961 0.20088  9   ASN A CG  
20   O OD1 . ASN A 5   ? 1.73718 1.33608 1.62827 -0.29457 -0.30766 0.22216  9   ASN A OD1 
21   N ND2 . ASN A 5   ? 1.64214 1.22999 1.59601 -0.25640 -0.31887 0.18766  9   ASN A ND2 
22   N N   . PHE A 6   ? 1.40014 1.14499 1.27610 -0.31808 -0.21602 0.20530  10  PHE A N   
23   C CA  . PHE A 6   ? 1.36034 1.15614 1.23525 -0.31522 -0.18610 0.19592  10  PHE A CA  
24   C C   . PHE A 6   ? 1.38566 1.19963 1.25275 -0.34115 -0.17921 0.20491  10  PHE A C   
25   O O   . PHE A 6   ? 1.49306 1.29093 1.33744 -0.36889 -0.18925 0.22524  10  PHE A O   
26   C CB  . PHE A 6   ? 1.32815 1.14412 1.18056 -0.31390 -0.17112 0.19885  10  PHE A CB  
27   C CG  . PHE A 6   ? 1.28934 1.09294 1.15023 -0.28939 -0.17576 0.18991  10  PHE A CG  
28   C CD1 . PHE A 6   ? 1.27379 1.10336 1.15521 -0.26438 -0.15991 0.17084  10  PHE A CD1 
29   C CD2 . PHE A 6   ? 1.24611 1.01163 1.09545 -0.29233 -0.19752 0.20143  10  PHE A CD2 
30   C CE1 . PHE A 6   ? 1.17117 0.99103 1.06183 -0.24382 -0.16405 0.16344  10  PHE A CE1 
31   C CE2 . PHE A 6   ? 1.30188 1.05833 1.16220 -0.27065 -0.20227 0.19302  10  PHE A CE2 
32   C CZ  . PHE A 6   ? 1.24977 1.03438 1.13127 -0.24670 -0.18476 0.17387  10  PHE A CZ  
33   N N   . TYR A 7   ? 1.31370 1.16251 1.19948 -0.33288 -0.16232 0.19034  11  TYR A N   
34   C CA  . TYR A 7   ? 1.30231 1.18260 1.18438 -0.35431 -0.14950 0.19533  11  TYR A CA  
35   C C   . TYR A 7   ? 1.24891 1.18069 1.13130 -0.34398 -0.12106 0.18404  11  TYR A C   
36   O O   . TYR A 7   ? 1.23058 1.17109 1.12217 -0.31811 -0.11316 0.17002  11  TYR A O   
37   C CB  . TYR A 7   ? 1.22395 1.09863 1.13009 -0.35531 -0.15829 0.18814  11  TYR A CB  
38   C CG  . TYR A 7   ? 1.20494 1.10607 1.13627 -0.32901 -0.14561 0.16529  11  TYR A CG  
39   C CD1 . TYR A 7   ? 1.17898 1.06620 1.12308 -0.30111 -0.14957 0.15121  11  TYR A CD1 
40   C CD2 . TYR A 7   ? 1.16179 1.10216 1.10441 -0.33323 -0.13073 0.15843  11  TYR A CD2 
41   C CE1 . TYR A 7   ? 1.15182 1.06300 1.11547 -0.27947 -0.13839 0.13214  11  TYR A CE1 
42   C CE2 . TYR A 7   ? 1.20462 1.16672 1.16768 -0.31051 -0.12159 0.13932  11  TYR A CE2 
43   C CZ  . TYR A 7   ? 1.10061 1.04786 1.07223 -0.28445 -0.12510 0.12687  11  TYR A CZ  
44   O OH  . TYR A 7   ? 1.14240 1.11220 1.13087 -0.26438 -0.11587 0.10963  11  TYR A OH  
45   N N   . SER A 8   ? 1.20311 1.16877 1.07576 -0.36521 -0.10650 0.19060  12  SER A N   
46   C CA  . SER A 8   ? 1.16071 1.17520 1.03087 -0.35919 -0.08067 0.18143  12  SER A CA  
47   C C   . SER A 8   ? 1.24583 1.30095 1.13939 -0.36056 -0.06760 0.17145  12  SER A C   
48   O O   . SER A 8   ? 1.36062 1.42813 1.25269 -0.38634 -0.06706 0.18126  12  SER A O   
49   C CB  . SER A 8   ? 1.21324 1.23853 1.05105 -0.38306 -0.07304 0.19595  12  SER A CB  
50   O OG  . SER A 8   ? 1.38766 1.36716 1.20200 -0.39030 -0.09232 0.21090  12  SER A OG  
51   N N   . VAL A 9   ? 1.16389 1.23992 1.07878 -0.33431 -0.05805 0.15311  13  VAL A N   
52   C CA  . VAL A 9   ? 1.06537 1.18216 1.00346 -0.33212 -0.04614 0.14224  13  VAL A CA  
53   C C   . VAL A 9   ? 1.10732 1.27187 1.04334 -0.33060 -0.02344 0.13576  13  VAL A C   
54   O O   . VAL A 9   ? 1.22552 1.38990 1.14779 -0.31956 -0.01676 0.13289  13  VAL A O   
55   C CB  . VAL A 9   ? 1.13150 1.24325 1.09256 -0.30487 -0.05037 0.12648  13  VAL A CB  
56   C CG1 . VAL A 9   ? 1.11564 1.27130 1.09881 -0.29932 -0.03804 0.11476  13  VAL A CG1 
57   C CG2 . VAL A 9   ? 1.25967 1.33253 1.22665 -0.30767 -0.07092 0.12906  13  VAL A CG2 
58   N N   . GLU A 10  ? 1.11798 1.32453 1.06957 -0.34122 -0.01211 0.13205  14  GLU A N   
59   C CA  . GLU A 10  ? 1.04084 1.29843 0.99930 -0.33588 0.00945  0.12108  14  GLU A CA  
60   C C   . GLU A 10  ? 0.95409 1.23366 0.94266 -0.31001 0.01307  0.10337  14  GLU A C   
61   O O   . GLU A 10  ? 1.02014 1.29828 1.02733 -0.31043 0.00460  0.10158  14  GLU A O   
62   C CB  . GLU A 10  ? 1.04192 1.33720 1.00029 -0.36561 0.02041  0.12816  14  GLU A CB  
63   C CG  . GLU A 10  ? 1.12464 1.40442 1.04836 -0.39239 0.01971  0.14622  14  GLU A CG  
64   C CD  . GLU A 10  ? 1.27166 1.56858 1.17553 -0.38473 0.03501  0.14006  14  GLU A CD  
65   O OE1 . GLU A 10  ? 1.29399 1.62988 1.21556 -0.36527 0.05070  0.12137  14  GLU A OE1 
66   O OE2 . GLU A 10  ? 1.33894 1.60908 1.20956 -0.39802 0.02981  0.15351  14  GLU A OE2 
67   N N   . ILE A 11  ? 1.11929 1.41490 1.11115 -0.28740 0.02327  0.09074  15  ILE A N   
68   C CA  . ILE A 11  ? 1.00560 1.32245 1.02437 -0.26284 0.02599  0.07508  15  ILE A CA  
69   C C   . ILE A 11  ? 1.00139 1.36536 1.02941 -0.25680 0.04407  0.06303  15  ILE A C   
70   O O   . ILE A 11  ? 1.10853 1.47043 1.12990 -0.23952 0.04898  0.05542  15  ILE A O   
71   C CB  . ILE A 11  ? 0.97766 1.26069 0.99410 -0.23770 0.01657  0.07089  15  ILE A CB  
72   C CG1 . ILE A 11  ? 0.99814 1.23351 1.00093 -0.24409 0.00045  0.08179  15  ILE A CG1 
73   C CG2 . ILE A 11  ? 0.89897 1.19691 0.94100 -0.21795 0.01431  0.05931  15  ILE A CG2 
74   C CD1 . ILE A 11  ? 0.90629 1.13622 0.92449 -0.24866 -0.01006 0.08170  15  ILE A CD1 
75   N N   . GLY A 12  ? 1.01346 1.42115 1.05995 -0.26973 0.05335  0.05955  16  GLY A N   
76   C CA  . GLY A 12  ? 0.97806 1.43417 1.03483 -0.26531 0.07153  0.04636  16  GLY A CA  
77   C C   . GLY A 12  ? 1.11881 1.57113 1.14386 -0.27693 0.08122  0.05103  16  GLY A C   
78   O O   . GLY A 12  ? 1.05805 1.49700 1.05989 -0.30369 0.07978  0.06696  16  GLY A O   
79   N N   . ASP A 13  ? 1.23440 1.69620 1.25710 -0.25697 0.08948  0.03732  17  ASP A N   
80   C CA  . ASP A 13  ? 1.38959 1.84989 1.38079 -0.26567 0.09893  0.03869  17  ASP A CA  
81   C C   . ASP A 13  ? 1.35255 1.75633 1.30983 -0.27432 0.08467  0.05670  17  ASP A C   
82   O O   . ASP A 13  ? 1.41244 1.80881 1.34128 -0.29968 0.08620  0.07044  17  ASP A O   
83   C CB  . ASP A 13  ? 1.51211 1.98595 1.50931 -0.23871 0.10653  0.01865  17  ASP A CB  
84   C CG  . ASP A 13  ? 1.58188 2.11560 1.61122 -0.23057 0.12199  -0.00155 17  ASP A CG  
85   O OD1 . ASP A 13  ? 1.52862 2.08847 1.55305 -0.22425 0.13569  -0.01675 17  ASP A OD1 
86   O OD2 . ASP A 13  ? 1.63787 2.19335 1.69796 -0.23050 0.11992  -0.00326 17  ASP A OD2 
87   N N   . SER A 14  ? 1.28411 1.64859 1.24445 -0.25386 0.07019  0.05702  18  SER A N   
88   C CA  . SER A 14  ? 1.30765 1.62213 1.24006 -0.25540 0.05744  0.06923  18  SER A CA  
89   C C   . SER A 14  ? 1.23581 1.51818 1.16123 -0.27430 0.04271  0.08744  18  SER A C   
90   O O   . SER A 14  ? 1.13683 1.42540 1.08316 -0.27751 0.03837  0.08836  18  SER A O   
91   C CB  . SER A 14  ? 1.31370 1.60357 1.25470 -0.22608 0.04918  0.06100  18  SER A CB  
92   O OG  . SER A 14  ? 1.41384 1.69315 1.37736 -0.21620 0.03931  0.06113  18  SER A OG  
93   N N   . THR A 15  ? 1.23547 1.48237 1.13131 -0.28689 0.03353  0.10150  19  THR A N   
94   C CA  . THR A 15  ? 1.13160 1.34041 1.01917 -0.30337 0.01609  0.11880  19  THR A CA  
95   C C   . THR A 15  ? 1.11425 1.27727 1.00124 -0.28461 -0.00041 0.11969  19  THR A C   
96   O O   . THR A 15  ? 1.14923 1.29562 1.01906 -0.27685 -0.00223 0.11973  19  THR A O   
97   C CB  . THR A 15  ? 1.16372 1.36465 1.01863 -0.33377 0.01501  0.13610  19  THR A CB  
98   O OG1 . THR A 15  ? 1.18465 1.43593 1.03588 -0.34817 0.03570  0.13158  19  THR A OG1 
99   C CG2 . THR A 15  ? 1.17994 1.35028 1.03336 -0.35455 -0.00246 0.15346  19  THR A CG2 
100  N N   . PHE A 16  ? 1.06661 1.21135 0.97279 -0.27761 -0.01216 0.11934  20  PHE A N   
101  C CA  . PHE A 16  ? 1.06157 1.16520 0.96943 -0.26232 -0.02779 0.12004  20  PHE A CA  
102  C C   . PHE A 16  ? 1.12566 1.18976 1.01867 -0.28078 -0.04585 0.13630  20  PHE A C   
103  O O   . PHE A 16  ? 1.20034 1.26066 1.09841 -0.29725 -0.05242 0.14305  20  PHE A O   
104  C CB  . PHE A 16  ? 1.07121 1.17668 1.00628 -0.24417 -0.03081 0.10915  20  PHE A CB  
105  C CG  . PHE A 16  ? 1.00936 1.13826 0.95752 -0.22111 -0.01981 0.09506  20  PHE A CG  
106  C CD1 . PHE A 16  ? 1.01273 1.18151 0.96535 -0.22063 -0.00421 0.08774  20  PHE A CD1 
107  C CD2 . PHE A 16  ? 0.91196 1.02350 0.86911 -0.20031 -0.02571 0.08900  20  PHE A CD2 
108  C CE1 . PHE A 16  ? 1.03082 1.21738 0.99685 -0.19883 0.00289  0.07508  20  PHE A CE1 
109  C CE2 . PHE A 16  ? 0.96802 1.09799 0.93605 -0.18091 -0.01765 0.07829  20  PHE A CE2 
110  C CZ  . PHE A 16  ? 0.97553 1.14086 0.94805 -0.17972 -0.00455 0.07156  20  PHE A CZ  
111  N N   . THR A 17  ? 1.06029 1.09409 0.93588 -0.27862 -0.05554 0.14282  21  THR A N   
112  C CA  . THR A 17  ? 1.17191 1.16213 1.03746 -0.29111 -0.07706 0.15713  21  THR A CA  
113  C C   . THR A 17  ? 1.09165 1.05459 0.97455 -0.26760 -0.08932 0.14915  21  THR A C   
114  O O   . THR A 17  ? 1.11859 1.07715 0.99880 -0.25206 -0.08791 0.14435  21  THR A O   
115  C CB  . THR A 17  ? 1.20181 1.17722 1.03401 -0.30859 -0.08164 0.17203  21  THR A CB  
116  O OG1 . THR A 17  ? 1.21930 1.22819 1.03550 -0.33043 -0.06622 0.17722  21  THR A OG1 
117  C CG2 . THR A 17  ? 1.21326 1.14122 1.03713 -0.32236 -0.10724 0.18826  21  THR A CG2 
118  N N   . VAL A 18  ? 1.09223 1.03921 0.99387 -0.26518 -0.10074 0.14646  22  VAL A N   
119  C CA  . VAL A 18  ? 1.07588 1.00721 0.99836 -0.24191 -0.10824 0.13476  22  VAL A CA  
120  C C   . VAL A 18  ? 1.14035 1.03178 1.06943 -0.24693 -0.13128 0.13959  22  VAL A C   
121  O O   . VAL A 18  ? 1.21685 1.09512 1.13866 -0.26800 -0.14101 0.15072  22  VAL A O   
122  C CB  . VAL A 18  ? 1.02204 0.98313 0.96578 -0.22730 -0.09545 0.11923  22  VAL A CB  
123  C CG1 . VAL A 18  ? 0.98535 0.98342 0.92505 -0.22152 -0.07544 0.11427  22  VAL A CG1 
124  C CG2 . VAL A 18  ? 1.02012 0.98680 0.97200 -0.24116 -0.09843 0.11984  22  VAL A CG2 
125  N N   . LEU A 19  ? 1.07417 0.94706 1.01895 -0.22727 -0.14040 0.13045  23  LEU A N   
126  C CA  . LEU A 19  ? 1.09928 0.93512 1.05614 -0.22700 -0.16299 0.13042  23  LEU A CA  
127  C C   . LEU A 19  ? 1.08197 0.92126 1.05196 -0.23223 -0.16519 0.12394  23  LEU A C   
128  O O   . LEU A 19  ? 1.05358 0.92528 1.03049 -0.22757 -0.14907 0.11438  23  LEU A O   
129  C CB  . LEU A 19  ? 1.00087 0.82596 0.97759 -0.20250 -0.16859 0.11734  23  LEU A CB  
130  C CG  . LEU A 19  ? 1.05833 0.87251 1.02812 -0.19550 -0.17257 0.12243  23  LEU A CG  
131  C CD1 . LEU A 19  ? 0.99577 0.81085 0.99062 -0.17117 -0.17326 0.10675  23  LEU A CD1 
132  C CD2 . LEU A 19  ? 1.14680 0.92178 1.10432 -0.21032 -0.19608 0.13838  23  LEU A CD2 
133  N N   . LYS A 20  ? 1.12065 0.92394 1.09445 -0.24202 -0.18758 0.12926  24  LYS A N   
134  C CA  . LYS A 20  ? 1.09890 0.89969 1.08444 -0.24912 -0.19344 0.12360  24  LYS A CA  
135  C C   . LYS A 20  ? 1.05777 0.87544 1.06609 -0.22614 -0.18586 0.10015  24  LYS A C   
136  O O   . LYS A 20  ? 1.11193 0.94445 1.12706 -0.23003 -0.18177 0.09295  24  LYS A O   
137  C CB  . LYS A 20  ? 1.18113 0.93369 1.16850 -0.26117 -0.22254 0.13245  24  LYS A CB  
138  C CG  . LYS A 20  ? 1.21289 0.94614 1.17415 -0.29060 -0.23294 0.15898  24  LYS A CG  
139  C CD  . LYS A 20  ? 1.29900 1.04707 1.25176 -0.31691 -0.22807 0.16890  24  LYS A CD  
140  C CE  . LYS A 20  ? 1.33556 1.04489 1.27147 -0.34634 -0.25140 0.19287  24  LYS A CE  
141  N NZ  . LYS A 20  ? 1.38246 1.07189 1.29516 -0.35232 -0.25912 0.20978  24  LYS A NZ  
142  N N   . ARG A 21  ? 1.04553 0.86335 1.06493 -0.20343 -0.18356 0.08840  25  ARG A N   
143  C CA  . ARG A 21  ? 0.99388 0.82662 1.03272 -0.18310 -0.17718 0.06654  25  ARG A CA  
144  C C   . ARG A 21  ? 1.05971 0.93409 1.09530 -0.18110 -0.15535 0.06119  25  ARG A C   
145  O O   . ARG A 21  ? 1.04481 0.93205 1.09189 -0.17073 -0.15149 0.04525  25  ARG A O   
146  C CB  . ARG A 21  ? 0.93598 0.76623 0.98641 -0.16182 -0.17652 0.05724  25  ARG A CB  
147  C CG  . ARG A 21  ? 0.97766 0.83096 1.01692 -0.15728 -0.15967 0.06398  25  ARG A CG  
148  C CD  . ARG A 21  ? 0.93875 0.78723 0.99055 -0.13921 -0.16147 0.05720  25  ARG A CD  
149  N NE  . ARG A 21  ? 0.97292 0.84072 1.04288 -0.12102 -0.15248 0.03784  25  ARG A NE  
150  C CZ  . ARG A 21  ? 1.06989 0.93912 1.15583 -0.10509 -0.15259 0.02854  25  ARG A CZ  
151  N NH1 . ARG A 21  ? 0.99952 0.85074 1.08786 -0.10345 -0.16269 0.03620  25  ARG A NH1 
152  N NH2 . ARG A 21  ? 1.06200 0.95294 1.16151 -0.09145 -0.14237 0.01132  25  ARG A NH2 
153  N N   . TYR A 22  ? 0.98905 0.88480 1.00929 -0.19047 -0.14195 0.07334  26  TYR A N   
154  C CA  . TYR A 22  ? 1.00070 0.93574 1.01989 -0.18710 -0.12272 0.06884  26  TYR A CA  
155  C C   . TYR A 22  ? 1.05911 1.00558 1.07445 -0.20695 -0.12213 0.07522  26  TYR A C   
156  O O   . TYR A 22  ? 1.06297 1.00966 1.06533 -0.22482 -0.12141 0.08984  26  TYR A O   
157  C CB  . TYR A 22  ? 1.02332 0.97590 1.03220 -0.18195 -0.10886 0.07484  26  TYR A CB  
158  C CG  . TYR A 22  ? 0.88458 0.82724 0.89880 -0.16396 -0.10982 0.06949  26  TYR A CG  
159  C CD1 . TYR A 22  ? 0.95372 0.90677 0.98166 -0.14647 -0.10525 0.05503  26  TYR A CD1 
160  C CD2 . TYR A 22  ? 0.83370 0.75818 0.83891 -0.16571 -0.11549 0.07910  26  TYR A CD2 
161  C CE1 . TYR A 22  ? 0.88085 0.82876 0.91592 -0.13160 -0.10511 0.05029  26  TYR A CE1 
162  C CE2 . TYR A 22  ? 0.93567 0.85300 0.94897 -0.14969 -0.11704 0.07398  26  TYR A CE2 
163  C CZ  . TYR A 22  ? 0.91240 0.84259 0.94187 -0.13302 -0.11131 0.05959  26  TYR A CZ  
164  O OH  . TYR A 22  ? 0.90202 0.82884 0.94158 -0.11898 -0.11192 0.05471  26  TYR A OH  
165  N N   . GLN A 23  ? 1.05457 1.01243 1.08083 -0.20464 -0.12221 0.06405  27  GLN A N   
166  C CA  . GLN A 23  ? 1.02166 0.98709 1.04932 -0.22337 -0.12550 0.06792  27  GLN A CA  
167  C C   . GLN A 23  ? 0.98943 0.99680 1.02145 -0.22018 -0.10984 0.06252  27  GLN A C   
168  O O   . GLN A 23  ? 1.02986 1.05340 1.06591 -0.20173 -0.10117 0.05218  27  GLN A O   
169  C CB  . GLN A 23  ? 1.01826 0.95835 1.05665 -0.22460 -0.14306 0.05825  27  GLN A CB  
170  C CG  . GLN A 23  ? 1.11520 1.01253 1.15537 -0.22134 -0.16100 0.05857  27  GLN A CG  
171  C CD  . GLN A 23  ? 1.23559 1.10835 1.26392 -0.24333 -0.17231 0.07918  27  GLN A CD  
172  O OE1 . GLN A 23  ? 1.25145 1.14293 1.26807 -0.26120 -0.16336 0.09342  27  GLN A OE1 
173  N NE2 . GLN A 23  ? 1.28452 1.11594 1.31586 -0.24220 -0.19243 0.08073  27  GLN A NE2 
174  N N   . ASN A 24  ? 0.94465 0.96994 0.97670 -0.23910 -0.10716 0.07020  28  ASN A N   
175  C CA  . ASN A 24  ? 0.99540 1.05946 1.03689 -0.23793 -0.09677 0.06401  28  ASN A CA  
176  C C   . ASN A 24  ? 0.96842 1.06189 1.00856 -0.22286 -0.07978 0.06192  28  ASN A C   
177  O O   . ASN A 24  ? 0.91161 1.02479 0.95928 -0.20845 -0.07467 0.05203  28  ASN A O   
178  C CB  . ASN A 24  ? 0.90859 0.96948 0.96047 -0.22911 -0.10503 0.04927  28  ASN A CB  
179  C CG  . ASN A 24  ? 1.13410 1.15834 1.18819 -0.23944 -0.12451 0.04776  28  ASN A CG  
180  O OD1 . ASN A 24  ? 1.15035 1.14787 1.20500 -0.22681 -0.13327 0.03862  28  ASN A OD1 
181  N ND2 . ASN A 24  ? 1.02368 1.04775 1.08106 -0.26224 -0.13180 0.05566  28  ASN A ND2 
182  N N   . LEU A 25  ? 0.94033 1.03540 0.96973 -0.22690 -0.07234 0.07151  29  LEU A N   
183  C CA  . LEU A 25  ? 0.95259 1.07333 0.98117 -0.21348 -0.05765 0.06897  29  LEU A CA  
184  C C   . LEU A 25  ? 0.84551 1.00756 0.88716 -0.21494 -0.04828 0.06446  29  LEU A C   
185  O O   . LEU A 25  ? 0.91468 1.09169 0.96178 -0.23320 -0.04836 0.06844  29  LEU A O   
186  C CB  . LEU A 25  ? 0.93142 1.04759 0.94467 -0.22027 -0.05201 0.07898  29  LEU A CB  
187  C CG  . LEU A 25  ? 0.89192 0.97638 0.89417 -0.21006 -0.05751 0.08127  29  LEU A CG  
188  C CD1 . LEU A 25  ? 0.90995 0.95543 0.91095 -0.21591 -0.07503 0.08434  29  LEU A CD1 
189  C CD2 . LEU A 25  ? 0.89041 0.97729 0.87613 -0.21702 -0.05064 0.09000  29  LEU A CD2 
190  N N   . LYS A 26  ? 0.75528 0.93573 0.80353 -0.19594 -0.04144 0.05645  30  LYS A N   
191  C CA  . LYS A 26  ? 0.76183 0.98165 0.82498 -0.19299 -0.03373 0.05120  30  LYS A CA  
192  C C   . LYS A 26  ? 0.81118 1.04245 0.87478 -0.17383 -0.02549 0.04710  30  LYS A C   
193  O O   . LYS A 26  ? 0.88768 1.09718 0.94311 -0.16068 -0.02806 0.04639  30  LYS A O   
194  C CB  . LYS A 26  ? 0.80725 1.03491 0.88288 -0.19050 -0.04166 0.04409  30  LYS A CB  
195  C CG  . LYS A 26  ? 0.88654 1.09729 0.95792 -0.17264 -0.04723 0.03771  30  LYS A CG  
196  C CD  . LYS A 26  ? 0.93872 1.14808 1.01570 -0.17541 -0.05779 0.03097  30  LYS A CD  
197  C CE  . LYS A 26  ? 0.77387 0.97410 0.84480 -0.15818 -0.06095 0.02379  30  LYS A CE  
198  N NZ  . LYS A 26  ? 0.83861 1.02371 0.90703 -0.16104 -0.07170 0.01590  30  LYS A NZ  
199  N N   . PRO A 27  ? 0.80867 1.07375 0.88328 -0.17179 -0.01621 0.04370  31  PRO A N   
200  C CA  . PRO A 27  ? 0.73475 1.00708 0.80999 -0.15380 -0.01000 0.03939  31  PRO A CA  
201  C C   . PRO A 27  ? 0.80678 1.08430 0.89258 -0.13600 -0.01531 0.03354  31  PRO A C   
202  O O   . PRO A 27  ? 0.73882 1.03466 0.83860 -0.13699 -0.01958 0.02993  31  PRO A O   
203  C CB  . PRO A 27  ? 0.72996 1.03847 0.81520 -0.15936 0.00142  0.03584  31  PRO A CB  
204  C CG  . PRO A 27  ? 0.75845 1.08756 0.85524 -0.17755 0.00082  0.03715  31  PRO A CG  
205  C CD  . PRO A 27  ? 0.85654 1.15637 0.94646 -0.18541 -0.01158 0.04235  31  PRO A CD  
206  N N   . ILE A 28  ? 0.78126 1.04305 0.85992 -0.12061 -0.01578 0.03343  32  ILE A N   
207  C CA  . ILE A 28  ? 0.79652 1.05817 0.88044 -0.10526 -0.02196 0.03083  32  ILE A CA  
208  C C   . ILE A 28  ? 0.76749 1.03597 0.85687 -0.08949 -0.01977 0.02816  32  ILE A C   
209  O O   . ILE A 28  ? 0.81362 1.08511 0.90927 -0.07781 -0.02619 0.02717  32  ILE A O   
210  C CB  . ILE A 28  ? 0.76139 0.99368 0.83150 -0.10298 -0.02793 0.03406  32  ILE A CB  
211  C CG1 . ILE A 28  ? 0.78213 0.99026 0.83926 -0.10114 -0.02495 0.03813  32  ILE A CG1 
212  C CG2 . ILE A 28  ? 0.79574 1.02033 0.86324 -0.11582 -0.03277 0.03378  32  ILE A CG2 
213  C CD1 . ILE A 28  ? 0.75800 0.94365 0.80659 -0.09525 -0.02950 0.03954  32  ILE A CD1 
214  N N   . GLY A 29  ? 0.78641 1.05579 0.87234 -0.08933 -0.01218 0.02700  33  GLY A N   
215  C CA  . GLY A 29  ? 0.79239 1.06477 0.88351 -0.07389 -0.01138 0.02274  33  GLY A CA  
216  C C   . GLY A 29  ? 0.82309 1.09506 0.90594 -0.07676 -0.00246 0.02030  33  GLY A C   
217  O O   . GLY A 29  ? 0.80745 1.07501 0.87817 -0.09163 0.00258  0.02408  33  GLY A O   
218  N N   . SER A 30  ? 0.83306 1.10758 0.92114 -0.06261 -0.00198 0.01406  34  SER A N   
219  C CA  . SER A 30  ? 0.86099 1.13926 0.94124 -0.06397 0.00670  0.00861  34  SER A CA  
220  C C   . SER A 30  ? 0.88165 1.14926 0.96447 -0.04628 0.00275  0.00285  34  SER A C   
221  O O   . SER A 30  ? 0.85140 1.11226 0.94487 -0.03338 -0.00673 0.00344  34  SER A O   
222  C CB  . SER A 30  ? 0.84769 1.16490 0.94054 -0.07041 0.01712  -0.00074 34  SER A CB  
223  O OG  . SER A 30  ? 0.99252 1.33344 1.11010 -0.05387 0.01545  -0.01275 34  SER A OG  
224  N N   . GLY A 31  ? 0.91209 1.17740 0.98364 -0.04697 0.00915  -0.00242 35  GLY A N   
225  C CA  . GLY A 31  ? 0.92482 1.17910 0.99799 -0.03129 0.00518  -0.00976 35  GLY A CA  
226  C C   . GLY A 31  ? 1.05080 1.30893 1.10898 -0.03563 0.01440  -0.01760 35  GLY A C   
227  O O   . GLY A 31  ? 0.94145 1.21629 0.98983 -0.05087 0.02480  -0.01758 35  GLY A O   
228  N N   . ALA A 32  ? 1.02097 1.26169 1.07545 -0.02337 0.00950  -0.02350 36  ALA A N   
229  C CA  . ALA A 32  ? 1.10425 1.34697 1.14235 -0.02568 0.01688  -0.03302 36  ALA A CA  
230  C C   . ALA A 32  ? 1.13933 1.37108 1.14973 -0.04621 0.02192  -0.02166 36  ALA A C   
231  O O   . ALA A 32  ? 1.20894 1.45739 1.20491 -0.05626 0.03255  -0.02759 36  ALA A O   
232  C CB  . ALA A 32  ? 1.00999 1.22567 1.04564 -0.01107 0.00694  -0.03776 36  ALA A CB  
233  N N   . GLN A 33  ? 1.04738 1.25187 1.05017 -0.05292 0.01393  -0.00557 37  GLN A N   
234  C CA  . GLN A 33  ? 1.15217 1.33926 1.13082 -0.07018 0.01416  0.00595  37  GLN A CA  
235  C C   . GLN A 33  ? 1.12025 1.32345 1.09690 -0.08796 0.02021  0.01307  37  GLN A C   
236  O O   . GLN A 33  ? 1.13465 1.32101 1.09287 -0.10321 0.01791  0.02429  37  GLN A O   
237  C CB  . GLN A 33  ? 1.12866 1.27958 1.10355 -0.06767 0.00190  0.01771  37  GLN A CB  
238  C CG  . GLN A 33  ? 1.15209 1.28239 1.12408 -0.05530 -0.00525 0.01354  37  GLN A CG  
239  C CD  . GLN A 33  ? 1.23943 1.33729 1.20691 -0.05642 -0.01604 0.02557  37  GLN A CD  
240  O OE1 . GLN A 33  ? 1.15228 1.23110 1.10401 -0.06025 -0.02044 0.02788  37  GLN A OE1 
241  N NE2 . GLN A 33  ? 1.16508 1.25865 1.14677 -0.05316 -0.02035 0.03241  37  GLN A NE2 
242  N N   . GLY A 34  ? 1.12487 1.35923 1.12093 -0.08686 0.02627  0.00703  38  GLY A N   
243  C CA  . GLY A 34  ? 1.16128 1.41308 1.15730 -0.10476 0.03173  0.01294  38  GLY A CA  
244  C C   . GLY A 34  ? 1.15867 1.41185 1.17407 -0.10205 0.02548  0.01734  38  GLY A C   
245  O O   . GLY A 34  ? 1.26493 1.52432 1.29932 -0.08603 0.02157  0.01134  38  GLY A O   
246  N N   . ILE A 35  ? 1.01470 1.25993 1.02377 -0.11831 0.02304  0.02803  39  ILE A N   
247  C CA  . ILE A 35  ? 0.98214 1.23539 1.00766 -0.12025 0.01897  0.03032  39  ILE A CA  
248  C C   . ILE A 35  ? 0.90519 1.12383 0.92305 -0.12227 0.00799  0.04028  39  ILE A C   
249  O O   . ILE A 35  ? 0.95518 1.14920 0.95545 -0.13121 0.00459  0.04804  39  ILE A O   
250  C CB  . ILE A 35  ? 0.96176 1.24320 0.99102 -0.13897 0.02648  0.03105  39  ILE A CB  
251  C CG1 . ILE A 35  ? 0.92423 1.20437 0.96438 -0.14594 0.01942  0.03608  39  ILE A CG1 
252  C CG2 . ILE A 35  ? 1.04088 1.31303 1.04539 -0.15835 0.03044  0.03914  39  ILE A CG2 
253  C CD1 . ILE A 35  ? 0.97941 1.29273 1.02959 -0.16284 0.02635  0.03537  39  ILE A CD1 
254  N N   . VAL A 36  ? 0.78864 1.00599 0.81987 -0.11329 0.00189  0.03924  40  VAL A N   
255  C CA  . VAL A 36  ? 0.80973 0.99970 0.83655 -0.11306 -0.00714 0.04518  40  VAL A CA  
256  C C   . VAL A 36  ? 0.78721 0.98323 0.82033 -0.12411 -0.01041 0.04657  40  VAL A C   
257  O O   . VAL A 36  ? 0.83787 1.05991 0.88482 -0.12427 -0.00828 0.04198  40  VAL A O   
258  C CB  . VAL A 36  ? 0.88216 1.06490 0.91542 -0.09586 -0.01164 0.04305  40  VAL A CB  
259  C CG1 . VAL A 36  ? 0.77666 0.93695 0.80633 -0.09609 -0.01876 0.04702  40  VAL A CG1 
260  C CG2 . VAL A 36  ? 0.83103 1.00498 0.85888 -0.08604 -0.01021 0.04188  40  VAL A CG2 
261  N N   . CYS A 37  ? 0.77707 0.94861 0.80169 -0.13303 -0.01701 0.05213  41  CYS A N   
262  C CA  . CYS A 37  ? 0.80503 0.97646 0.83463 -0.14405 -0.02242 0.05280  41  CYS A CA  
263  C C   . CYS A 37  ? 0.81558 0.96685 0.84646 -0.13667 -0.03085 0.05050  41  CYS A C   
264  O O   . CYS A 37  ? 0.87803 1.00798 0.90289 -0.12957 -0.03359 0.05173  41  CYS A O   
265  C CB  . CYS A 37  ? 0.83195 0.99167 0.85137 -0.16369 -0.02472 0.06058  41  CYS A CB  
266  S SG  . CYS A 37  ? 0.97832 1.17131 0.99748 -0.17865 -0.01326 0.06240  41  CYS A SG  
267  N N   . ALA A 38  ? 0.82003 0.98037 0.85940 -0.13825 -0.03473 0.04602  42  ALA A N   
268  C CA  . ALA A 38  ? 0.73988 0.88133 0.77855 -0.13531 -0.04276 0.04213  42  ALA A CA  
269  C C   . ALA A 38  ? 0.83109 0.95181 0.86680 -0.14986 -0.05070 0.04497  42  ALA A C   
270  O O   . ALA A 38  ? 0.90786 1.03517 0.94352 -0.16493 -0.05043 0.05021  42  ALA A O   
271  C CB  . ALA A 38  ? 0.71223 0.87052 0.75833 -0.13099 -0.04498 0.03518  42  ALA A CB  
272  N N   . ALA A 39  ? 0.83364 0.92949 0.86786 -0.14581 -0.05832 0.04148  43  ALA A N   
273  C CA  . ALA A 39  ? 0.87224 0.94402 0.90581 -0.15818 -0.06941 0.04328  43  ALA A CA  
274  C C   . ALA A 39  ? 0.95738 1.01195 0.99586 -0.14962 -0.07770 0.03232  43  ALA A C   
275  O O   . ALA A 39  ? 0.91065 0.96961 0.95035 -0.13497 -0.07341 0.02550  43  ALA A O   
276  C CB  . ALA A 39  ? 0.83295 0.88345 0.85762 -0.16534 -0.07245 0.05375  43  ALA A CB  
277  N N   . TYR A 40  ? 0.91143 0.94650 0.95296 -0.15966 -0.08989 0.03036  44  TYR A N   
278  C CA  . TYR A 40  ? 0.96702 0.98238 1.01476 -0.15189 -0.09963 0.01772  44  TYR A CA  
279  C C   . TYR A 40  ? 1.01463 0.99840 1.06342 -0.15118 -0.10915 0.02147  44  TYR A C   
280  O O   . TYR A 40  ? 1.02088 0.98581 1.06588 -0.16568 -0.11811 0.03267  44  TYR A O   
281  C CB  . TYR A 40  ? 1.02662 1.03720 1.07913 -0.16178 -0.10996 0.01101  44  TYR A CB  
282  C CG  . TYR A 40  ? 1.01920 1.01050 1.07869 -0.15267 -0.12021 -0.00550 44  TYR A CG  
283  C CD1 . TYR A 40  ? 0.99858 1.00654 1.05861 -0.13916 -0.11424 -0.02069 44  TYR A CD1 
284  C CD2 . TYR A 40  ? 1.03259 0.98927 1.09787 -0.15766 -0.13649 -0.00651 44  TYR A CD2 
285  C CE1 . TYR A 40  ? 1.04957 1.04383 1.11589 -0.13026 -0.12192 -0.03867 44  TYR A CE1 
286  C CE2 . TYR A 40  ? 1.12396 1.06399 1.19862 -0.14731 -0.14630 -0.02483 44  TYR A CE2 
287  C CZ  . TYR A 40  ? 1.11193 1.07260 1.18721 -0.13324 -0.13783 -0.04208 44  TYR A CZ  
288  O OH  . TYR A 40  ? 1.12802 1.07580 1.21255 -0.12237 -0.14598 -0.06320 44  TYR A OH  
289  N N   . ASP A 41  ? 1.01101 0.99022 1.06511 -0.13523 -0.10766 0.01292  45  ASP A N   
290  C CA  . ASP A 41  ? 0.98977 0.94054 1.04946 -0.13145 -0.11824 0.01389  45  ASP A CA  
291  C C   . ASP A 41  ? 1.09012 1.01943 1.16264 -0.12774 -0.13286 -0.00099 45  ASP A C   
292  O O   . ASP A 41  ? 1.03087 0.96912 1.11230 -0.11358 -0.12944 -0.01809 45  ASP A O   
293  C CB  . ASP A 41  ? 0.92752 0.88753 0.99015 -0.11645 -0.10914 0.01171  45  ASP A CB  
294  C CG  . ASP A 41  ? 1.05022 0.98301 1.12173 -0.11171 -0.12111 0.01243  45  ASP A CG  
295  O OD1 . ASP A 41  ? 1.03079 0.93509 1.10503 -0.11975 -0.13764 0.01535  45  ASP A OD1 
296  O OD2 . ASP A 41  ? 1.03978 0.97903 1.11689 -0.10017 -0.11547 0.01032  45  ASP A OD2 
297  N N   . ALA A 42  ? 1.05291 0.95320 1.12624 -0.14073 -0.14973 0.00528  46  ALA A N   
298  C CA  . ALA A 42  ? 1.11216 0.98855 1.19844 -0.13855 -0.16655 -0.00922 46  ALA A CA  
299  C C   . ALA A 42  ? 1.11445 0.97713 1.21760 -0.12010 -0.17310 -0.02412 46  ALA A C   
300  O O   . ALA A 42  ? 1.16250 1.01601 1.27904 -0.11163 -0.18185 -0.04378 46  ALA A O   
301  C CB  . ALA A 42  ? 1.10919 0.95367 1.19223 -0.15836 -0.18537 0.00431  46  ALA A CB  
302  N N   . ILE A 43  ? 1.11772 0.98119 1.22194 -0.11317 -0.16881 -0.01693 47  ILE A N   
303  C CA  . ILE A 43  ? 1.01962 0.87378 1.14365 -0.09581 -0.17485 -0.03075 47  ILE A CA  
304  C C   . ILE A 43  ? 1.06036 0.94915 1.19067 -0.07974 -0.15645 -0.04820 47  ILE A C   
305  O O   . ILE A 43  ? 1.07114 0.96048 1.21918 -0.06617 -0.15965 -0.06978 47  ILE A O   
306  C CB  . ILE A 43  ? 1.01936 0.85827 1.14252 -0.09696 -0.18060 -0.01472 47  ILE A CB  
307  C CG1 . ILE A 43  ? 0.97776 0.77718 1.09551 -0.11282 -0.20309 0.00058  47  ILE A CG1 
308  C CG2 . ILE A 43  ? 1.00497 0.84436 1.15109 -0.07786 -0.18286 -0.02884 47  ILE A CG2 
309  C CD1 . ILE A 43  ? 1.05351 0.84214 1.15858 -0.12068 -0.20612 0.02180  47  ILE A CD1 
310  N N   . LEU A 44  ? 1.08642 1.00488 1.20238 -0.08130 -0.13735 -0.03944 48  LEU A N   
311  C CA  . LEU A 44  ? 1.01081 0.96224 1.12825 -0.06965 -0.12011 -0.05215 48  LEU A CA  
312  C C   . LEU A 44  ? 1.10787 1.07559 1.21717 -0.07181 -0.11496 -0.06333 48  LEU A C   
313  O O   . LEU A 44  ? 1.04860 1.04131 1.15790 -0.06283 -0.10315 -0.07658 48  LEU A O   
314  C CB  . LEU A 44  ? 0.94132 0.91327 1.04734 -0.07058 -0.10508 -0.03693 48  LEU A CB  
315  C CG  . LEU A 44  ? 1.04219 1.00494 1.15597 -0.06618 -0.10734 -0.02844 48  LEU A CG  
316  C CD1 . LEU A 44  ? 1.05045 1.03039 1.15037 -0.06910 -0.09428 -0.01324 48  LEU A CD1 
317  C CD2 . LEU A 44  ? 0.90213 0.87150 1.03787 -0.05124 -0.10661 -0.04526 48  LEU A CD2 
318  N N   . GLU A 45  ? 1.05743 1.01239 1.15899 -0.08489 -0.12389 -0.05742 49  GLU A N   
319  C CA  . GLU A 45  ? 1.03989 1.00685 1.13436 -0.08898 -0.12268 -0.06706 49  GLU A CA  
320  C C   . GLU A 45  ? 1.02483 1.02726 1.10579 -0.08709 -0.10478 -0.06435 49  GLU A C   
321  O O   . GLU A 45  ? 1.02172 1.04234 1.09941 -0.08066 -0.09872 -0.07929 49  GLU A O   
322  C CB  . GLU A 45  ? 1.08665 1.04462 1.19355 -0.07947 -0.13136 -0.09253 49  GLU A CB  
323  C CG  . GLU A 45  ? 1.23028 1.15303 1.34470 -0.08819 -0.15309 -0.09461 49  GLU A CG  
324  C CD  . GLU A 45  ? 1.38352 1.28675 1.51761 -0.07525 -0.16613 -0.11887 49  GLU A CD  
325  O OE1 . GLU A 45  ? 1.38819 1.27345 1.53725 -0.06813 -0.17382 -0.11789 49  GLU A OE1 
326  O OE2 . GLU A 45  ? 1.37417 1.27913 1.50965 -0.07207 -0.17015 -0.13946 49  GLU A OE2 
327  N N   . ARG A 46  ? 1.05598 1.06736 1.12827 -0.09301 -0.09736 -0.04519 50  ARG A N   
328  C CA  . ARG A 46  ? 1.01455 1.05527 1.07522 -0.09218 -0.08373 -0.03958 50  ARG A CA  
329  C C   . ARG A 46  ? 0.94979 0.99265 1.00446 -0.10145 -0.08121 -0.02022 50  ARG A C   
330  O O   . ARG A 46  ? 0.86514 0.88893 0.92213 -0.10773 -0.08739 -0.01082 50  ARG A O   
331  C CB  . ARG A 46  ? 0.98505 1.04142 1.04609 -0.08024 -0.07231 -0.04323 50  ARG A CB  
332  C CG  . ARG A 46  ? 0.97986 1.02258 1.04985 -0.07626 -0.07312 -0.03628 50  ARG A CG  
333  C CD  . ARG A 46  ? 1.05378 1.11373 1.12655 -0.06615 -0.06201 -0.03957 50  ARG A CD  
334  N NE  . ARG A 46  ? 1.06430 1.13664 1.12784 -0.06773 -0.05332 -0.02381 50  ARG A NE  
335  C CZ  . ARG A 46  ? 1.00424 1.08554 1.07077 -0.06201 -0.04589 -0.02031 50  ARG A CZ  
336  N NH1 . ARG A 46  ? 1.05153 1.13429 1.13129 -0.05464 -0.04464 -0.03115 50  ARG A NH1 
337  N NH2 . ARG A 46  ? 0.87291 0.96254 0.93094 -0.06367 -0.04018 -0.00643 50  ARG A NH2 
338  N N   . ASN A 47  ? 0.99842 1.06527 1.04509 -0.10215 -0.07264 -0.01496 51  ASN A N   
339  C CA  . ASN A 47  ? 0.90244 0.97735 0.94533 -0.10842 -0.06834 0.00006  51  ASN A CA  
340  C C   . ASN A 47  ? 0.86120 0.93545 0.90284 -0.10147 -0.06147 0.00811  51  ASN A C   
341  O O   . ASN A 47  ? 0.86531 0.94395 0.90765 -0.09160 -0.05670 0.00394  51  ASN A O   
342  C CB  . ASN A 47  ? 0.89235 0.99306 0.93102 -0.10944 -0.06364 0.00138  51  ASN A CB  
343  C CG  . ASN A 47  ? 0.99069 1.09430 1.03123 -0.11844 -0.07120 -0.00469 51  ASN A CG  
344  O OD1 . ASN A 47  ? 0.97622 1.06665 1.02098 -0.12978 -0.07848 -0.00222 51  ASN A OD1 
345  N ND2 . ASN A 47  ? 0.89487 1.01581 0.93130 -0.11488 -0.07052 -0.01152 51  ASN A ND2 
346  N N   . VAL A 48  ? 0.80018 0.87047 0.83943 -0.10779 -0.06076 0.01956  52  VAL A N   
347  C CA  . VAL A 48  ? 0.85424 0.92325 0.89103 -0.10245 -0.05545 0.02722  52  VAL A CA  
348  C C   . VAL A 48  ? 0.82865 0.91254 0.86072 -0.10687 -0.04975 0.03562  52  VAL A C   
349  O O   . VAL A 48  ? 0.82370 0.91894 0.85625 -0.11514 -0.04993 0.03621  52  VAL A O   
350  C CB  . VAL A 48  ? 0.84907 0.89249 0.88735 -0.10450 -0.06244 0.03061  52  VAL A CB  
351  C CG1 . VAL A 48  ? 0.78414 0.81379 0.83223 -0.09836 -0.06931 0.01938  52  VAL A CG1 
352  C CG2 . VAL A 48  ? 0.86322 0.89624 0.89627 -0.11919 -0.06824 0.03840  52  VAL A CG2 
353  N N   . ALA A 49  ? 0.77583 0.86040 0.80503 -0.10119 -0.04501 0.04096  53  ALA A N   
354  C CA  . ALA A 49  ? 0.80326 0.89991 0.82880 -0.10362 -0.03972 0.04660  53  ALA A CA  
355  C C   . ALA A 49  ? 0.82066 0.90073 0.83890 -0.10892 -0.04135 0.05301  53  ALA A C   
356  O O   . ALA A 49  ? 0.82895 0.88986 0.84675 -0.10569 -0.04598 0.05403  53  ALA A O   
357  C CB  . ALA A 49  ? 0.75996 0.87050 0.78712 -0.09227 -0.03447 0.04657  53  ALA A CB  
358  N N   . ILE A 50  ? 0.81469 0.90385 0.82732 -0.11783 -0.03780 0.05694  54  ILE A N   
359  C CA  . ILE A 50  ? 0.82293 0.89789 0.82386 -0.12653 -0.03958 0.06384  54  ILE A CA  
360  C C   . ILE A 50  ? 0.84613 0.93962 0.84171 -0.12550 -0.03046 0.06394  54  ILE A C   
361  O O   . ILE A 50  ? 0.91462 1.03227 0.91404 -0.12981 -0.02407 0.06147  54  ILE A O   
362  C CB  . ILE A 50  ? 0.84541 0.91057 0.84127 -0.14394 -0.04562 0.06905  54  ILE A CB  
363  C CG1 . ILE A 50  ? 0.77756 0.82132 0.78059 -0.14341 -0.05674 0.06651  54  ILE A CG1 
364  C CG2 . ILE A 50  ? 0.86440 0.91563 0.84380 -0.15483 -0.04783 0.07820  54  ILE A CG2 
365  C CD1 . ILE A 50  ? 0.83532 0.85727 0.83181 -0.16036 -0.06762 0.07412  54  ILE A CD1 
366  N N   . LYS A 51  ? 0.86737 0.95060 0.85570 -0.11960 -0.03036 0.06546  55  LYS A N   
367  C CA  . LYS A 51  ? 0.86633 0.96394 0.84909 -0.11659 -0.02281 0.06300  55  LYS A CA  
368  C C   . LYS A 51  ? 0.88512 0.97054 0.84897 -0.12897 -0.02419 0.06908  55  LYS A C   
369  O O   . LYS A 51  ? 0.90187 0.96111 0.85892 -0.13290 -0.03357 0.07539  55  LYS A O   
370  C CB  . LYS A 51  ? 0.89107 0.98420 0.87907 -0.10041 -0.02343 0.05967  55  LYS A CB  
371  C CG  . LYS A 51  ? 0.91608 1.02091 0.90147 -0.09339 -0.01786 0.05442  55  LYS A CG  
372  C CD  . LYS A 51  ? 0.96881 1.05615 0.95453 -0.08223 -0.02294 0.05481  55  LYS A CD  
373  C CE  . LYS A 51  ? 0.95809 1.05727 0.95042 -0.06992 -0.02018 0.04772  55  LYS A CE  
374  N NZ  . LYS A 51  ? 0.96232 1.06864 0.96998 -0.06090 -0.02210 0.04743  55  LYS A NZ  
375  N N   . LYS A 52  ? 0.88571 0.99107 0.84115 -0.13560 -0.01539 0.06691  56  LYS A N   
376  C CA  . LYS A 52  ? 0.98515 1.08178 0.91789 -0.14923 -0.01563 0.07295  56  LYS A CA  
377  C C   . LYS A 52  ? 1.04543 1.15073 0.96956 -0.14114 -0.00924 0.06564  56  LYS A C   
378  O O   . LYS A 52  ? 1.13415 1.26751 1.06723 -0.13423 0.00089  0.05538  56  LYS A O   
379  C CB  . LYS A 52  ? 0.99509 1.10909 0.92036 -0.16917 -0.00997 0.07728  56  LYS A CB  
380  C CG  . LYS A 52  ? 0.97905 1.08136 0.87637 -0.18632 -0.01167 0.08632  56  LYS A CG  
381  C CD  . LYS A 52  ? 1.03588 1.15475 0.92374 -0.20988 -0.00642 0.09336  56  LYS A CD  
382  C CE  . LYS A 52  ? 1.07181 1.23146 0.95628 -0.21305 0.01128  0.08408  56  LYS A CE  
383  N NZ  . LYS A 52  ? 1.11140 1.27667 0.97091 -0.24014 0.01460  0.09506  56  LYS A NZ  
384  N N   . LEU A 53  ? 1.04639 1.12753 0.95416 -0.14184 -0.01634 0.06993  57  LEU A N   
385  C CA  . LEU A 53  ? 1.08534 1.17104 0.97914 -0.13759 -0.01186 0.06310  57  LEU A CA  
386  C C   . LEU A 53  ? 1.07303 1.15910 0.93821 -0.15767 -0.00973 0.06946  57  LEU A C   
387  O O   . LEU A 53  ? 1.05706 1.11559 0.90641 -0.16826 -0.02121 0.08144  57  LEU A O   
388  C CB  . LEU A 53  ? 0.93163 0.99075 0.82565 -0.12553 -0.02223 0.06338  57  LEU A CB  
389  C CG  . LEU A 53  ? 0.92796 0.97935 0.84638 -0.11081 -0.02743 0.06257  57  LEU A CG  
390  C CD1 . LEU A 53  ? 0.92237 0.94883 0.83986 -0.10297 -0.03768 0.06439  57  LEU A CD1 
391  C CD2 . LEU A 53  ? 1.01578 1.09151 0.95129 -0.09828 -0.01905 0.05222  57  LEU A CD2 
392  N N   . SER A 54  ? 1.05408 1.17207 0.91283 -0.16341 0.00437  0.06159  58  SER A N   
393  C CA  . SER A 54  ? 1.12685 1.25060 0.95573 -0.18483 0.00879  0.06762  58  SER A CA  
394  C C   . SER A 54  ? 1.17146 1.29324 0.97870 -0.18037 0.01089  0.05925  58  SER A C   
395  O O   . SER A 54  ? 1.19557 1.33358 1.01460 -0.16303 0.01791  0.04276  58  SER A O   
396  C CB  . SER A 54  ? 1.09504 1.25894 0.92870 -0.19719 0.02424  0.06407  58  SER A CB  
397  O OG  . SER A 54  ? 1.17165 1.36878 1.02757 -0.18045 0.03638  0.04583  58  SER A OG  
398  N N   . ARG A 55  ? 1.19123 1.29020 0.96656 -0.19598 0.00249  0.07086  59  ARG A N   
399  C CA  . ARG A 55  ? 1.22709 1.31617 0.97429 -0.19623 0.00017  0.06655  59  ARG A CA  
400  C C   . ARG A 55  ? 1.23230 1.31608 0.99632 -0.17100 -0.00207 0.05144  59  ARG A C   
401  O O   . ARG A 55  ? 1.22696 1.32872 0.98326 -0.16392 0.00710  0.03524  59  ARG A O   
402  C CB  . ARG A 55  ? 1.31972 1.44265 1.04143 -0.21073 0.01703  0.05914  59  ARG A CB  
403  C CG  . ARG A 55  ? 1.37751 1.49776 1.06913 -0.24095 0.01583  0.07769  59  ARG A CG  
404  C CD  . ARG A 55  ? 1.64599 1.81315 1.32383 -0.25517 0.03789  0.06877  59  ARG A CD  
405  N NE  . ARG A 55  ? 1.69183 1.89646 1.40039 -0.23428 0.05382  0.04503  59  ARG A NE  
406  C CZ  . ARG A 55  ? 1.71571 1.95450 1.45186 -0.23426 0.06601  0.04003  59  ARG A CZ  
407  N NH1 . ARG A 55  ? 1.69070 1.93288 1.42739 -0.25515 0.06563  0.05654  59  ARG A NH1 
408  N NH2 . ARG A 55  ? 1.65062 1.91962 1.41564 -0.21278 0.07706  0.01794  59  ARG A NH2 
409  N N   . PRO A 56  ? 1.21435 1.27470 1.00191 -0.15742 -0.01408 0.05554  60  PRO A N   
410  C CA  . PRO A 56  ? 1.17590 1.23279 0.98188 -0.13508 -0.01611 0.04269  60  PRO A CA  
411  C C   . PRO A 56  ? 1.24287 1.28394 1.02676 -0.13236 -0.02249 0.03677  60  PRO A C   
412  O O   . PRO A 56  ? 1.22543 1.27182 1.01872 -0.11636 -0.02038 0.02170  60  PRO A O   
413  C CB  . PRO A 56  ? 1.09753 1.13235 0.92808 -0.12714 -0.02785 0.05217  60  PRO A CB  
414  C CG  . PRO A 56  ? 1.11862 1.13304 0.93561 -0.14387 -0.03766 0.06886  60  PRO A CG  
415  C CD  . PRO A 56  ? 1.12732 1.16134 0.92358 -0.16269 -0.02766 0.07185  60  PRO A CD  
416  N N   . PHE A 57  ? 1.22552 1.24602 0.97988 -0.14780 -0.03183 0.04809  61  PHE A N   
417  C CA  . PHE A 57  ? 1.20403 1.20958 0.93225 -0.14806 -0.03895 0.04296  61  PHE A CA  
418  C C   . PHE A 57  ? 1.26050 1.29431 0.96358 -0.15294 -0.02366 0.02756  61  PHE A C   
419  O O   . PHE A 57  ? 1.29677 1.32023 0.97198 -0.15570 -0.02861 0.02225  61  PHE A O   
420  C CB  . PHE A 57  ? 1.19310 1.16743 0.89730 -0.16414 -0.05585 0.06148  61  PHE A CB  
421  C CG  . PHE A 57  ? 1.28261 1.26399 0.96584 -0.18701 -0.05200 0.07511  61  PHE A CG  
422  C CD1 . PHE A 57  ? 1.29083 1.28908 0.93683 -0.20368 -0.04244 0.07296  61  PHE A CD1 
423  C CD2 . PHE A 57  ? 1.22968 1.20262 0.93069 -0.19245 -0.05729 0.08922  61  PHE A CD2 
424  C CE1 . PHE A 57  ? 1.29380 1.29929 0.92012 -0.22736 -0.03890 0.08738  61  PHE A CE1 
425  C CE2 . PHE A 57  ? 1.30966 1.28702 0.99241 -0.21466 -0.05529 0.10248  61  PHE A CE2 
426  C CZ  . PHE A 57  ? 1.27571 1.26918 0.92100 -0.23302 -0.04622 0.10277  61  PHE A CZ  
427  N N   . GLN A 58  ? 1.24379 1.31454 0.95632 -0.15425 -0.00538 0.01926  62  GLN A N   
428  C CA  . GLN A 58  ? 1.29980 1.40320 0.98854 -0.16162 0.01123  0.00450  62  GLN A CA  
429  C C   . GLN A 58  ? 1.35686 1.46542 1.04714 -0.14246 0.01340  -0.01980 62  GLN A C   
430  O O   . GLN A 58  ? 1.46813 1.59019 1.12802 -0.14884 0.02085  -0.03192 62  GLN A O   
431  C CB  . GLN A 58  ? 1.33618 1.48141 1.04185 -0.16618 0.03003  0.00007  62  GLN A CB  
432  C CG  . GLN A 58  ? 1.39363 1.55820 1.14103 -0.14191 0.03623  -0.01700 62  GLN A CG  
433  C CD  . GLN A 58  ? 1.45266 1.65379 1.22260 -0.14625 0.05030  -0.01767 62  GLN A CD  
434  O OE1 . GLN A 58  ? 1.51319 1.75404 1.29281 -0.14091 0.06612  -0.03648 62  GLN A OE1 
435  N NE2 . GLN A 58  ? 1.40237 1.59105 1.18322 -0.15503 0.04388  0.00136  62  GLN A NE2 
436  N N   . ASN A 59  ? 1.30446 1.40255 1.02838 -0.11980 0.00670  -0.02760 63  ASN A N   
437  C CA  . ASN A 59  ? 1.29132 1.38775 1.01860 -0.10129 0.00486  -0.04976 63  ASN A CA  
438  C C   . ASN A 59  ? 1.24121 1.30614 0.99655 -0.08431 -0.01192 -0.04558 63  ASN A C   
439  O O   . ASN A 59  ? 1.21949 1.27080 0.99345 -0.08564 -0.01877 -0.02820 63  ASN A O   
440  C CB  . ASN A 59  ? 1.21660 1.35516 0.96010 -0.08971 0.02279  -0.07409 63  ASN A CB  
441  C CG  . ASN A 59  ? 1.21629 1.36674 1.00383 -0.07562 0.02475  -0.07396 63  ASN A CG  
442  O OD1 . ASN A 59  ? 1.20043 1.32727 1.01176 -0.06058 0.01181  -0.07135 63  ASN A OD1 
443  N ND2 . ASN A 59  ? 1.31697 1.50562 1.11489 -0.08149 0.04077  -0.07677 63  ASN A ND2 
444  N N   . GLN A 60  ? 1.25321 1.30857 1.01238 -0.06838 -0.01801 -0.06297 64  GLN A N   
445  C CA  . GLN A 60  ? 1.23587 1.25778 1.01503 -0.05614 -0.03592 -0.05773 64  GLN A CA  
446  C C   . GLN A 60  ? 1.20304 1.22774 1.02093 -0.04606 -0.03648 -0.05008 64  GLN A C   
447  O O   . GLN A 60  ? 1.20538 1.20929 1.03485 -0.04876 -0.04657 -0.03218 64  GLN A O   
448  C CB  . GLN A 60  ? 1.28825 1.30135 1.06632 -0.04092 -0.04214 -0.07971 64  GLN A CB  
449  C CG  . GLN A 60  ? 1.44984 1.42371 1.22203 -0.04083 -0.06233 -0.07214 64  GLN A CG  
450  C CD  . GLN A 60  ? 1.65820 1.62090 1.38999 -0.05876 -0.06657 -0.06497 64  GLN A CD  
451  O OE1 . GLN A 60  ? 1.57896 1.56335 1.28196 -0.06978 -0.05389 -0.07092 64  GLN A OE1 
452  N NE2 . GLN A 60  ? 1.69242 1.62222 1.42194 -0.06270 -0.08499 -0.05158 64  GLN A NE2 
453  N N   . THR A 61  ? 1.12453 1.17617 0.96316 -0.03424 -0.02607 -0.06423 65  THR A N   
454  C CA  . THR A 61  ? 1.12872 1.17966 1.00267 -0.02276 -0.02978 -0.05855 65  THR A CA  
455  C C   . THR A 61  ? 1.15767 1.21519 1.03798 -0.03466 -0.02548 -0.03886 65  THR A C   
456  O O   . THR A 61  ? 1.11536 1.15975 1.01567 -0.03088 -0.03307 -0.02668 65  THR A O   
457  C CB  . THR A 61  ? 1.05051 1.12737 0.94625 -0.00625 -0.02258 -0.07910 65  THR A CB  
458  O OG1 . THR A 61  ? 1.21854 1.33366 1.10840 -0.01396 -0.00458 -0.08608 65  THR A OG1 
459  C CG2 . THR A 61  ? 1.05566 1.12328 0.94718 0.00742  -0.02870 -0.10111 65  THR A CG2 
460  N N   . HIS A 62  ? 1.12939 1.20699 0.99215 -0.04997 -0.01371 -0.03564 66  HIS A N   
461  C CA  . HIS A 62  ? 1.04649 1.12560 0.91312 -0.06251 -0.01204 -0.01720 66  HIS A CA  
462  C C   . HIS A 62  ? 1.03382 1.07916 0.89174 -0.07030 -0.02576 0.00029  66  HIS A C   
463  O O   . HIS A 62  ? 1.01400 1.05143 0.88768 -0.07148 -0.03007 0.01308  66  HIS A O   
464  C CB  . HIS A 62  ? 1.16028 1.26599 1.00894 -0.07929 0.00183  -0.01673 66  HIS A CB  
465  C CG  . HIS A 62  ? 1.24523 1.39068 1.10625 -0.07290 0.01694  -0.03444 66  HIS A CG  
466  N ND1 . HIS A 62  ? 1.19662 1.37068 1.07028 -0.08009 0.02756  -0.03143 66  HIS A ND1 
467  C CD2 . HIS A 62  ? 1.24225 1.40436 1.10829 -0.05893 0.02222  -0.05674 66  HIS A CD2 
468  C CE1 . HIS A 62  ? 1.28125 1.49031 1.16791 -0.07129 0.03939  -0.05074 66  HIS A CE1 
469  N NE2 . HIS A 62  ? 1.36753 1.57005 1.25028 -0.05759 0.03648  -0.06709 66  HIS A NE2 
470  N N   . ALA A 63  ? 1.11023 1.13676 0.94361 -0.07548 -0.03310 -0.00007 67  ALA A N   
471  C CA  . ALA A 63  ? 1.10603 1.10190 0.93221 -0.08312 -0.04754 0.01579  67  ALA A CA  
472  C C   . ALA A 63  ? 1.06904 1.04608 0.92144 -0.07065 -0.05872 0.01941  67  ALA A C   
473  O O   . ALA A 63  ? 1.05487 1.02086 0.92019 -0.07358 -0.06481 0.03271  67  ALA A O   
474  C CB  . ALA A 63  ? 1.09338 1.07445 0.88683 -0.09123 -0.05424 0.01365  67  ALA A CB  
475  N N   . LYS A 64  ? 1.10436 1.07780 0.96508 -0.05722 -0.06187 0.00725  68  LYS A N   
476  C CA  . LYS A 64  ? 1.08890 1.04577 0.97412 -0.04738 -0.07230 0.01183  68  LYS A CA  
477  C C   . LYS A 64  ? 0.98981 0.95901 0.89942 -0.04447 -0.06701 0.01948  68  LYS A C   
478  O O   . LYS A 64  ? 0.95513 0.91321 0.87940 -0.04522 -0.07344 0.03097  68  LYS A O   
479  C CB  . LYS A 64  ? 1.15458 1.10656 1.04500 -0.03380 -0.07662 -0.00335 68  LYS A CB  
480  C CG  . LYS A 64  ? 1.17100 1.10725 1.08682 -0.02431 -0.08736 0.00111  68  LYS A CG  
481  C CD  . LYS A 64  ? 1.25549 1.19808 1.18401 -0.00932 -0.08695 -0.01392 68  LYS A CD  
482  C CE  . LYS A 64  ? 1.28691 1.24162 1.19702 -0.00542 -0.08039 -0.03458 68  LYS A CE  
483  N NZ  . LYS A 64  ? 1.27114 1.22995 1.19747 0.01176  -0.08260 -0.05208 68  LYS A NZ  
484  N N   . ARG A 65  ? 0.93592 0.93031 0.84988 -0.04182 -0.05505 0.01254  69  ARG A N   
485  C CA  . ARG A 65  ? 0.94746 0.95458 0.88276 -0.03889 -0.05078 0.01843  69  ARG A CA  
486  C C   . ARG A 65  ? 0.95945 0.96413 0.89338 -0.05072 -0.05025 0.03235  69  ARG A C   
487  O O   . ARG A 65  ? 0.96129 0.96347 0.91191 -0.04881 -0.05272 0.04024  69  ARG A O   
488  C CB  . ARG A 65  ? 0.90672 0.94274 0.84742 -0.03381 -0.03936 0.00661  69  ARG A CB  
489  C CG  . ARG A 65  ? 0.98548 1.03631 0.94738 -0.03007 -0.03607 0.01092  69  ARG A CG  
490  C CD  . ARG A 65  ? 1.06116 1.14396 1.02570 -0.03060 -0.02386 0.00125  69  ARG A CD  
491  N NE  . ARG A 65  ? 1.20550 1.30152 1.18774 -0.01502 -0.02401 -0.01217 69  ARG A NE  
492  C CZ  . ARG A 65  ? 1.22441 1.32202 1.22795 -0.00574 -0.02929 -0.00935 69  ARG A CZ  
493  N NH1 . ARG A 65  ? 1.06550 1.15578 1.07397 -0.01091 -0.03254 0.00530  69  ARG A NH1 
494  N NH2 . ARG A 65  ? 1.06298 1.16997 1.08296 0.00916  -0.03206 -0.02214 69  ARG A NH2 
495  N N   . ALA A 66  ? 0.92204 0.92645 0.83553 -0.06334 -0.04799 0.03530  70  ALA A N   
496  C CA  . ALA A 66  ? 0.88162 0.88005 0.79441 -0.07421 -0.05016 0.04769  70  ALA A CA  
497  C C   . ALA A 66  ? 0.93397 0.90781 0.85314 -0.07387 -0.06292 0.05629  70  ALA A C   
498  O O   . ALA A 66  ? 0.94725 0.91898 0.88238 -0.07371 -0.06502 0.06290  70  ALA A O   
499  C CB  . ALA A 66  ? 0.94417 0.94551 0.83185 -0.08929 -0.04696 0.05025  70  ALA A CB  
500  N N   . TYR A 67  ? 0.92588 0.88259 0.83332 -0.07393 -0.07163 0.05514  71  TYR A N   
501  C CA  . TYR A 67  ? 0.98342 0.91920 0.90030 -0.07324 -0.08454 0.06226  71  TYR A CA  
502  C C   . TYR A 67  ? 0.93846 0.87774 0.88291 -0.06401 -0.08443 0.06365  71  TYR A C   
503  O O   . TYR A 67  ? 0.88215 0.81870 0.84203 -0.06516 -0.08761 0.07039  71  TYR A O   
504  C CB  . TYR A 67  ? 0.98382 0.90331 0.88599 -0.07275 -0.09390 0.05830  71  TYR A CB  
505  C CG  . TYR A 67  ? 1.02701 0.92534 0.93586 -0.07510 -0.10891 0.06615  71  TYR A CG  
506  C CD1 . TYR A 67  ? 1.09900 0.98629 1.01952 -0.06874 -0.11763 0.06428  71  TYR A CD1 
507  C CD2 . TYR A 67  ? 1.05548 0.94447 0.96087 -0.08384 -0.11592 0.07532  71  TYR A CD2 
508  C CE1 . TYR A 67  ? 1.13252 1.00349 1.06259 -0.07126 -0.13173 0.07100  71  TYR A CE1 
509  C CE2 . TYR A 67  ? 1.06749 0.93873 0.98285 -0.08481 -0.13106 0.08138  71  TYR A CE2 
510  C CZ  . TYR A 67  ? 1.14590 1.01006 1.07432 -0.07857 -0.13821 0.07896  71  TYR A CZ  
511  O OH  . TYR A 67  ? 1.26631 1.11619 1.20819 -0.07979 -0.15329 0.08446  71  TYR A OH  
512  N N   . ARG A 68  ? 0.92358 0.86975 0.87442 -0.05504 -0.08097 0.05694  72  ARG A N   
513  C CA  . ARG A 68  ? 0.93586 0.88506 0.90930 -0.04841 -0.08142 0.06022  72  ARG A CA  
514  C C   . ARG A 68  ? 0.92667 0.89044 0.91088 -0.05045 -0.07411 0.06491  72  ARG A C   
515  O O   . ARG A 68  ? 0.88337 0.84642 0.88286 -0.05067 -0.07614 0.07086  72  ARG A O   
516  C CB  . ARG A 68  ? 0.92487 0.87848 0.90175 -0.03892 -0.08011 0.05261  72  ARG A CB  
517  C CG  . ARG A 68  ? 1.00549 0.94025 0.98393 -0.03484 -0.09126 0.05053  72  ARG A CG  
518  C CD  . ARG A 68  ? 1.02609 0.96215 1.00158 -0.02526 -0.09139 0.03836  72  ARG A CD  
519  N NE  . ARG A 68  ? 1.02811 0.94428 1.01054 -0.02072 -0.10390 0.03769  72  ARG A NE  
520  C CZ  . ARG A 68  ? 1.10959 1.01978 1.09279 -0.01113 -0.10871 0.02664  72  ARG A CZ  
521  N NH1 . ARG A 68  ? 1.08590 1.01147 1.06448 -0.00393 -0.10100 0.01367  72  ARG A NH1 
522  N NH2 . ARG A 68  ? 1.20732 1.09611 1.19820 -0.00865 -0.12221 0.02791  72  ARG A NH2 
523  N N   . GLU A 69  ? 0.81077 0.78922 0.78731 -0.05270 -0.06548 0.06147  73  GLU A N   
524  C CA  . GLU A 69  ? 0.90162 0.89285 0.88723 -0.05500 -0.05973 0.06468  73  GLU A CA  
525  C C   . GLU A 69  ? 0.91702 0.89834 0.90684 -0.06100 -0.06466 0.07072  73  GLU A C   
526  O O   . GLU A 69  ? 0.88461 0.86956 0.88981 -0.05905 -0.06444 0.07325  73  GLU A O   
527  C CB  . GLU A 69  ? 0.95321 0.96084 0.92968 -0.05872 -0.05120 0.06025  73  GLU A CB  
528  C CG  . GLU A 69  ? 0.97058 0.99087 0.95592 -0.06155 -0.04645 0.06255  73  GLU A CG  
529  C CD  . GLU A 69  ? 1.13495 1.17402 1.13018 -0.05463 -0.04098 0.05871  73  GLU A CD  
530  O OE1 . GLU A 69  ? 1.17950 1.23191 1.17138 -0.05266 -0.03619 0.05222  73  GLU A OE1 
531  O OE2 . GLU A 69  ? 1.05104 1.09250 1.05764 -0.05116 -0.04193 0.06184  73  GLU A OE2 
532  N N   . LEU A 70  ? 0.90209 0.87087 0.87856 -0.06820 -0.07001 0.07264  74  LEU A N   
533  C CA  . LEU A 70  ? 0.91847 0.87595 0.90115 -0.07280 -0.07734 0.07763  74  LEU A CA  
534  C C   . LEU A 70  ? 0.94127 0.89269 0.94296 -0.06746 -0.08355 0.07932  74  LEU A C   
535  O O   . LEU A 70  ? 0.96108 0.91696 0.97986 -0.06598 -0.08344 0.07964  74  LEU A O   
536  C CB  . LEU A 70  ? 0.85956 0.80094 0.82274 -0.08192 -0.08533 0.08125  74  LEU A CB  
537  C CG  . LEU A 70  ? 0.85293 0.80187 0.79762 -0.09110 -0.07907 0.08152  74  LEU A CG  
538  C CD1 . LEU A 70  ? 0.79341 0.72719 0.71269 -0.10161 -0.08652 0.08600  74  LEU A CD1 
539  C CD2 . LEU A 70  ? 0.91137 0.86197 0.86644 -0.09468 -0.07929 0.08411  74  LEU A CD2 
540  N N   . VAL A 71  ? 0.92494 0.86785 0.92489 -0.06480 -0.08876 0.07938  75  VAL A N   
541  C CA  . VAL A 71  ? 0.86328 0.80073 0.88222 -0.06218 -0.09586 0.08197  75  VAL A CA  
542  C C   . VAL A 71  ? 0.85678 0.81086 0.89455 -0.05799 -0.08804 0.08208  75  VAL A C   
543  O O   . VAL A 71  ? 0.90324 0.86240 0.95995 -0.05763 -0.08901 0.08302  75  VAL A O   
544  C CB  . VAL A 71  ? 0.93696 0.86142 0.95025 -0.06108 -0.10389 0.08192  75  VAL A CB  
545  C CG1 . VAL A 71  ? 0.95705 0.88099 0.99379 -0.05928 -0.10939 0.08513  75  VAL A CG1 
546  C CG2 . VAL A 71  ? 0.97278 0.88003 0.96683 -0.06657 -0.11365 0.08249  75  VAL A CG2 
547  N N   . LEU A 72  ? 0.85431 0.81829 0.88722 -0.05490 -0.08052 0.08071  76  LEU A N   
548  C CA  . LEU A 72  ? 0.83580 0.81383 0.88245 -0.05244 -0.07475 0.08284  76  LEU A CA  
549  C C   . LEU A 72  ? 0.92764 0.92085 0.97878 -0.05327 -0.06688 0.08093  76  LEU A C   
550  O O   . LEU A 72  ? 0.92064 0.92555 0.98474 -0.05316 -0.06307 0.08221  76  LEU A O   
551  C CB  . LEU A 72  ? 0.83297 0.81295 0.87367 -0.04840 -0.07307 0.08283  76  LEU A CB  
552  C CG  . LEU A 72  ? 0.88840 0.85176 0.92797 -0.04704 -0.08245 0.08365  76  LEU A CG  
553  C CD1 . LEU A 72  ? 0.83872 0.80040 0.87018 -0.04133 -0.08267 0.07974  76  LEU A CD1 
554  C CD2 . LEU A 72  ? 0.84098 0.80134 0.89729 -0.04951 -0.08768 0.09041  76  LEU A CD2 
555  N N   . MET A 73  ? 0.88622 0.88053 0.92643 -0.05506 -0.06427 0.07758  77  MET A N   
556  C CA  . MET A 73  ? 0.88794 0.89335 0.93340 -0.05629 -0.05922 0.07475  77  MET A CA  
557  C C   . MET A 73  ? 0.86325 0.86578 0.92420 -0.05660 -0.06320 0.07323  77  MET A C   
558  O O   . MET A 73  ? 0.80407 0.81940 0.87557 -0.05541 -0.05832 0.06934  77  MET A O   
559  C CB  . MET A 73  ? 0.91324 0.91765 0.94560 -0.06029 -0.05791 0.07246  77  MET A CB  
560  C CG  . MET A 73  ? 0.94994 0.96519 0.97276 -0.05901 -0.05199 0.07123  77  MET A CG  
561  S SD  . MET A 73  ? 1.15338 1.18873 1.18359 -0.05575 -0.04506 0.06987  77  MET A SD  
562  C CE  . MET A 73  ? 0.93146 0.96935 0.96727 -0.05982 -0.04435 0.06598  77  MET A CE  
563  N N   . LYS A 74  ? 0.89741 0.88442 0.96091 -0.05763 -0.07256 0.07509  78  LYS A N   
564  C CA  . LYS A 74  ? 0.91204 0.89754 0.99501 -0.05637 -0.07794 0.07245  78  LYS A CA  
565  C C   . LYS A 74  ? 0.88636 0.88586 0.98883 -0.05387 -0.07439 0.07250  78  LYS A C   
566  O O   . LYS A 74  ? 1.01181 1.02124 1.13397 -0.05171 -0.07354 0.06708  78  LYS A O   
567  C CB  . LYS A 74  ? 0.88354 0.84760 0.96370 -0.05863 -0.09142 0.07519  78  LYS A CB  
568  C CG  . LYS A 74  ? 0.98192 0.93234 1.04311 -0.06391 -0.09583 0.07659  78  LYS A CG  
569  C CD  . LYS A 74  ? 1.15142 1.08036 1.21385 -0.06645 -0.11173 0.07976  78  LYS A CD  
570  C CE  . LYS A 74  ? 1.20140 1.11379 1.23597 -0.07508 -0.11738 0.08541  78  LYS A CE  
571  N NZ  . LYS A 74  ? 1.31749 1.20796 1.34827 -0.07814 -0.13418 0.09061  78  LYS A NZ  
572  N N   . CYS A 75  ? 0.83098 0.83212 0.92937 -0.05453 -0.07258 0.07803  79  CYS A N   
573  C CA  . CYS A 75  ? 0.91275 0.92662 1.02862 -0.05521 -0.06994 0.08065  79  CYS A CA  
574  C C   . CYS A 75  ? 0.88860 0.92442 1.00593 -0.05591 -0.05802 0.08008  79  CYS A C   
575  O O   . CYS A 75  ? 0.90344 0.95674 1.03763 -0.05746 -0.05298 0.07892  79  CYS A O   
576  C CB  . CYS A 75  ? 0.78099 0.78435 0.89209 -0.05697 -0.07533 0.08792  79  CYS A CB  
577  S SG  . CYS A 75  ? 1.14957 1.12673 1.25187 -0.05697 -0.08950 0.08835  79  CYS A SG  
578  N N   . VAL A 76  ? 0.79886 0.83577 0.89869 -0.05542 -0.05358 0.08088  80  VAL A N   
579  C CA  . VAL A 76  ? 0.81094 0.86555 0.90799 -0.05715 -0.04500 0.08328  80  VAL A CA  
580  C C   . VAL A 76  ? 0.84305 0.91613 0.94833 -0.05698 -0.03723 0.07492  80  VAL A C   
581  O O   . VAL A 76  ? 0.88641 0.95554 0.99533 -0.05420 -0.03900 0.06652  80  VAL A O   
582  C CB  . VAL A 76  ? 0.88830 0.93923 0.96709 -0.05560 -0.04448 0.08532  80  VAL A CB  
583  C CG1 . VAL A 76  ? 0.77564 0.81118 0.84938 -0.05465 -0.05176 0.09172  80  VAL A CG1 
584  C CG2 . VAL A 76  ? 0.78327 0.82961 0.85462 -0.05377 -0.04459 0.07802  80  VAL A CG2 
585  N N   . ASN A 77  ? 0.72272 0.81564 0.83088 -0.06056 -0.02934 0.07703  81  ASN A N   
586  C CA  . ASN A 77  ? 0.80048 0.91410 0.91579 -0.06018 -0.02076 0.06673  81  ASN A CA  
587  C C   . ASN A 77  ? 0.73754 0.87082 0.84297 -0.06618 -0.01222 0.07253  81  ASN A C   
588  O O   . ASN A 77  ? 0.84014 0.98822 0.95448 -0.07187 -0.00749 0.07705  81  ASN A O   
589  C CB  . ASN A 77  ? 0.91321 1.03471 1.05347 -0.05874 -0.02064 0.05972  81  ASN A CB  
590  C CG  . ASN A 77  ? 0.97035 1.10631 1.12052 -0.05450 -0.01525 0.04409  81  ASN A CG  
591  O OD1 . ASN A 77  ? 0.96818 1.11632 1.10612 -0.05519 -0.00801 0.03921  81  ASN A OD1 
592  N ND2 . ASN A 77  ? 1.05730 1.19081 1.23016 -0.04946 -0.02035 0.03511  81  ASN A ND2 
593  N N   . HIS A 78  ? 0.69043 0.82503 0.77778 -0.06598 -0.01070 0.07255  82  HIS A N   
594  C CA  . HIS A 78  ? 0.69689 0.84776 0.77139 -0.07247 -0.00498 0.07960  82  HIS A CA  
595  C C   . HIS A 78  ? 0.68470 0.83790 0.74240 -0.07059 -0.00454 0.07517  82  HIS A C   
596  O O   . HIS A 78  ? 0.66967 0.80770 0.72360 -0.06569 -0.01071 0.07321  82  HIS A O   
597  C CB  . HIS A 78  ? 0.63187 0.77176 0.70117 -0.07706 -0.01135 0.09650  82  HIS A CB  
598  C CG  . HIS A 78  ? 0.66344 0.81813 0.72033 -0.08632 -0.00751 0.10720  82  HIS A CG  
599  N ND1 . HIS A 78  ? 0.68572 0.84018 0.72323 -0.08717 -0.01028 0.11221  82  HIS A ND1 
600  C CD2 . HIS A 78  ? 0.69463 0.86573 0.75503 -0.09645 -0.00164 0.11463  82  HIS A CD2 
601  C CE1 . HIS A 78  ? 0.74926 0.91677 0.77638 -0.09759 -0.00741 0.12326  82  HIS A CE1 
602  N NE2 . HIS A 78  ? 0.69899 0.87767 0.73906 -0.10417 -0.00124 0.12515  82  HIS A NE2 
603  N N   . LYS A 79  ? 0.64930 0.82332 0.69668 -0.07549 0.00290  0.07334  83  LYS A N   
604  C CA  . LYS A 79  ? 0.72233 0.90070 0.75437 -0.07432 0.00277  0.06761  83  LYS A CA  
605  C C   . LYS A 79  ? 0.74443 0.90883 0.76451 -0.07326 -0.00661 0.07846  83  LYS A C   
606  O O   . LYS A 79  ? 0.82762 0.99202 0.83990 -0.07089 -0.00918 0.07322  83  LYS A O   
607  C CB  . LYS A 79  ? 0.73307 0.93670 0.75218 -0.08130 0.01167  0.06540  83  LYS A CB  
608  C CG  . LYS A 79  ? 0.82319 1.02908 0.82602 -0.08996 0.00892  0.08428  83  LYS A CG  
609  C CD  . LYS A 79  ? 0.81522 1.04743 0.80377 -0.10068 0.01865  0.08624  83  LYS A CD  
610  C CE  . LYS A 79  ? 0.90266 1.14952 0.87454 -0.10077 0.02252  0.07401  83  LYS A CE  
611  N NZ  . LYS A 79  ? 0.95264 1.22948 0.91224 -0.11120 0.03525  0.07159  83  LYS A NZ  
612  N N   . ASN A 80  ? 0.74288 0.89629 0.76303 -0.07482 -0.01252 0.09257  84  ASN A N   
613  C CA  . ASN A 80  ? 0.67698 0.81775 0.68971 -0.07182 -0.02244 0.10085  84  ASN A CA  
614  C C   . ASN A 80  ? 0.69145 0.81272 0.71470 -0.06506 -0.02850 0.10012  84  ASN A C   
615  O O   . ASN A 80  ? 0.74019 0.85047 0.76161 -0.06163 -0.03683 0.10657  84  ASN A O   
616  C CB  . ASN A 80  ? 0.63843 0.77920 0.64106 -0.07819 -0.02756 0.11711  84  ASN A CB  
617  C CG  . ASN A 80  ? 0.72238 0.88276 0.70828 -0.08610 -0.02279 0.11900  84  ASN A CG  
618  O OD1 . ASN A 80  ? 0.79694 0.96804 0.77712 -0.09577 -0.01806 0.12701  84  ASN A OD1 
619  N ND2 . ASN A 80  ? 0.83611 1.00282 0.81334 -0.08314 -0.02376 0.11123  84  ASN A ND2 
620  N N   . ILE A 81  ? 0.73689 0.85385 0.77072 -0.06283 -0.02527 0.09153  85  ILE A N   
621  C CA  . ILE A 81  ? 0.74812 0.84865 0.78744 -0.05761 -0.03007 0.08855  85  ILE A CA  
622  C C   . ILE A 81  ? 0.76350 0.86598 0.80365 -0.05620 -0.02732 0.07714  85  ILE A C   
623  O O   . ILE A 81  ? 0.87881 0.98862 0.92360 -0.05776 -0.02267 0.06996  85  ILE A O   
624  C CB  . ILE A 81  ? 0.70162 0.79076 0.75147 -0.05801 -0.03215 0.09128  85  ILE A CB  
625  C CG1 . ILE A 81  ? 0.67012 0.75649 0.72014 -0.06152 -0.03585 0.10352  85  ILE A CG1 
626  C CG2 . ILE A 81  ? 0.70008 0.77258 0.75100 -0.05367 -0.03726 0.08770  85  ILE A CG2 
627  C CD1 . ILE A 81  ? 0.68022 0.75382 0.72427 -0.05760 -0.04479 0.10974  85  ILE A CD1 
628  N N   . ILE A 82  ? 0.77857 0.87504 0.81540 -0.05360 -0.03053 0.07495  86  ILE A N   
629  C CA  . ILE A 82  ? 0.78947 0.88619 0.82625 -0.05468 -0.02931 0.06633  86  ILE A CA  
630  C C   . ILE A 82  ? 0.81960 0.90671 0.86441 -0.05555 -0.02960 0.06214  86  ILE A C   
631  O O   . ILE A 82  ? 0.81733 0.89336 0.86667 -0.05463 -0.03247 0.06585  86  ILE A O   
632  C CB  . ILE A 82  ? 0.69228 0.78528 0.72557 -0.05359 -0.03192 0.06597  86  ILE A CB  
633  C CG1 . ILE A 82  ? 0.66979 0.76835 0.70140 -0.05729 -0.03084 0.05931  86  ILE A CG1 
634  C CG2 . ILE A 82  ? 0.79108 0.86886 0.82540 -0.05281 -0.03460 0.06754  86  ILE A CG2 
635  C CD1 . ILE A 82  ? 0.80519 0.91902 0.83388 -0.05797 -0.02964 0.05695  86  ILE A CD1 
636  N N   . GLY A 83  ? 0.79679 0.88736 0.84455 -0.05691 -0.02821 0.05375  87  GLY A N   
637  C CA  . GLY A 83  ? 0.86281 0.94528 0.92179 -0.05626 -0.03020 0.04830  87  GLY A CA  
638  C C   . GLY A 83  ? 0.83581 0.90074 0.89364 -0.05842 -0.03692 0.04762  87  GLY A C   
639  O O   . GLY A 83  ? 0.83117 0.89573 0.88188 -0.06181 -0.03787 0.04603  87  GLY A O   
640  N N   . LEU A 84  ? 0.76976 0.82053 0.83404 -0.05776 -0.04234 0.04985  88  LEU A N   
641  C CA  . LEU A 84  ? 0.79595 0.82797 0.85663 -0.06153 -0.05038 0.05110  88  LEU A CA  
642  C C   . LEU A 84  ? 0.88304 0.90849 0.95352 -0.06160 -0.05567 0.04277  88  LEU A C   
643  O O   . LEU A 84  ? 0.90334 0.93613 0.98855 -0.05641 -0.05429 0.03496  88  LEU A O   
644  C CB  . LEU A 84  ? 0.74531 0.76308 0.80747 -0.06105 -0.05647 0.05698  88  LEU A CB  
645  C CG  . LEU A 84  ? 0.87452 0.87180 0.92781 -0.06684 -0.06580 0.06065  88  LEU A CG  
646  C CD1 . LEU A 84  ? 0.86701 0.86723 0.90190 -0.07242 -0.06184 0.06460  88  LEU A CD1 
647  C CD2 . LEU A 84  ? 0.86372 0.84648 0.91993 -0.06590 -0.07394 0.06507  88  LEU A CD2 
648  N N   . LEU A 85  ? 0.78140 0.79395 0.84432 -0.06791 -0.06183 0.04384  89  LEU A N   
649  C CA  . LEU A 85  ? 0.85265 0.85394 0.92405 -0.06885 -0.06991 0.03646  89  LEU A CA  
650  C C   . LEU A 85  ? 0.82773 0.80240 0.89666 -0.07468 -0.08356 0.04258  89  LEU A C   
651  O O   . LEU A 85  ? 0.95677 0.91707 1.03959 -0.07176 -0.09412 0.03700  89  LEU A O   
652  C CB  . LEU A 85  ? 0.87617 0.88514 0.94086 -0.07352 -0.06714 0.03231  89  LEU A CB  
653  C CG  . LEU A 85  ? 0.87482 0.90568 0.94349 -0.06812 -0.05831 0.02255  89  LEU A CG  
654  C CD1 . LEU A 85  ? 0.84377 0.87749 0.90628 -0.07399 -0.05953 0.01828  89  LEU A CD1 
655  C CD2 . LEU A 85  ? 0.72596 0.75949 0.81148 -0.05988 -0.05878 0.01114  89  LEU A CD2 
656  N N   . ASN A 86  ? 0.80492 0.77278 0.85627 -0.08307 -0.08437 0.05345  90  ASN A N   
657  C CA  . ASN A 86  ? 0.88357 0.82587 0.92743 -0.09137 -0.09786 0.06138  90  ASN A CA  
658  C C   . ASN A 86  ? 0.80408 0.74655 0.82694 -0.09875 -0.09444 0.07175  90  ASN A C   
659  O O   . ASN A 86  ? 0.94068 0.90202 0.95463 -0.10003 -0.08265 0.07193  90  ASN A O   
660  C CB  . ASN A 86  ? 0.85546 0.78490 0.89653 -0.10073 -0.10609 0.06152  90  ASN A CB  
661  C CG  . ASN A 86  ? 0.95343 0.85139 0.99125 -0.10807 -0.12446 0.06954  90  ASN A CG  
662  O OD1 . ASN A 86  ? 0.94530 0.83210 0.98519 -0.10444 -0.13144 0.07331  90  ASN A OD1 
663  N ND2 . ASN A 86  ? 0.92886 0.81104 0.96160 -0.11928 -0.13411 0.07306  90  ASN A ND2 
664  N N   . VAL A 87  ? 0.79229 0.71378 0.80755 -0.10336 -0.10579 0.07940  91  VAL A N   
665  C CA  . VAL A 87  ? 0.85304 0.77210 0.84494 -0.11198 -0.10426 0.08831  91  VAL A CA  
666  C C   . VAL A 87  ? 0.94081 0.83425 0.91866 -0.12557 -0.11909 0.09833  91  VAL A C   
667  O O   . VAL A 87  ? 1.06181 0.93289 1.04982 -0.12356 -0.13487 0.09984  91  VAL A O   
668  C CB  . VAL A 87  ? 0.90803 0.82673 0.90036 -0.10435 -0.10415 0.08862  91  VAL A CB  
669  C CG1 . VAL A 87  ? 0.92795 0.84816 0.89452 -0.11204 -0.10021 0.09423  91  VAL A CG1 
670  C CG2 . VAL A 87  ? 0.88810 0.82727 0.89730 -0.09180 -0.09321 0.08057  91  VAL A CG2 
671  N N   . PHE A 88  ? 0.90112 0.79843 0.85636 -0.13986 -0.11475 0.10542  92  PHE A N   
672  C CA  . PHE A 88  ? 0.94347 0.81635 0.88114 -0.15615 -0.12900 0.11768  92  PHE A CA  
673  C C   . PHE A 88  ? 1.06411 0.94870 0.97231 -0.17095 -0.11973 0.12496  92  PHE A C   
674  O O   . PHE A 88  ? 1.01855 0.93158 0.92476 -0.16782 -0.10232 0.11847  92  PHE A O   
675  C CB  . PHE A 88  ? 0.92276 0.78367 0.87071 -0.16231 -0.13798 0.11834  92  PHE A CB  
676  C CG  . PHE A 88  ? 0.94322 0.82755 0.88972 -0.16916 -0.12436 0.11538  92  PHE A CG  
677  C CD1 . PHE A 88  ? 1.01468 0.90316 0.93924 -0.18922 -0.12150 0.12567  92  PHE A CD1 
678  C CD2 . PHE A 88  ? 0.90685 0.81000 0.87406 -0.15680 -0.11517 0.10260  92  PHE A CD2 
679  C CE1 . PHE A 88  ? 0.95985 0.87228 0.88681 -0.19603 -0.10973 0.12263  92  PHE A CE1 
680  C CE2 . PHE A 88  ? 0.89538 0.81983 0.86250 -0.16322 -0.10481 0.09990  92  PHE A CE2 
681  C CZ  . PHE A 88  ? 0.92388 0.85325 0.87277 -0.18245 -0.10236 0.10967  92  PHE A CZ  
682  N N   . THR A 89  ? 1.08875 0.95141 0.97425 -0.18716 -0.13235 0.13821  93  THR A N   
683  C CA  . THR A 89  ? 1.05587 0.92860 0.91023 -0.20576 -0.12488 0.14658  93  THR A CA  
684  C C   . THR A 89  ? 1.19065 1.04066 1.03061 -0.22744 -0.13935 0.16190  93  THR A C   
685  O O   . THR A 89  ? 1.21785 1.03395 1.06243 -0.22802 -0.16102 0.16904  93  THR A O   
686  C CB  . THR A 89  ? 1.18072 1.04944 1.01255 -0.20605 -0.12580 0.14894  93  THR A CB  
687  O OG1 . THR A 89  ? 1.20398 1.07994 1.00178 -0.22729 -0.12059 0.15810  93  THR A OG1 
688  C CG2 . THR A 89  ? 1.16800 1.00117 1.00271 -0.20211 -0.14884 0.15541  93  THR A CG2 
689  N N   . PRO A 90  ? 1.27842 1.14618 1.10243 -0.24597 -0.12901 0.16748  94  PRO A N   
690  C CA  . PRO A 90  ? 1.22489 1.06963 1.03427 -0.26976 -0.14387 0.18439  94  PRO A CA  
691  C C   . PRO A 90  ? 1.33070 1.15006 1.10577 -0.28694 -0.15829 0.20146  94  PRO A C   
692  O O   . PRO A 90  ? 1.47535 1.26069 1.24300 -0.30149 -0.18004 0.21671  94  PRO A O   
693  C CB  . PRO A 90  ? 1.16136 1.04019 0.96625 -0.28430 -0.12534 0.18393  94  PRO A CB  
694  C CG  . PRO A 90  ? 1.18623 1.10388 0.98982 -0.27255 -0.10189 0.17023  94  PRO A CG  
695  C CD  . PRO A 90  ? 1.13377 1.04406 0.95841 -0.24525 -0.10452 0.15779  94  PRO A CD  
696  N N   . GLN A 91  ? 1.35456 1.18711 1.10803 -0.28567 -0.14885 0.19928  95  GLN A N   
697  C CA  . GLN A 91  ? 1.41943 1.22898 1.13642 -0.30227 -0.16261 0.21490  95  GLN A CA  
698  C C   . GLN A 91  ? 1.47228 1.24016 1.19953 -0.29135 -0.18970 0.21947  95  GLN A C   
699  O O   . GLN A 91  ? 1.42446 1.19154 1.18320 -0.26689 -0.19089 0.20592  95  GLN A O   
700  C CB  . GLN A 91  ? 1.33982 1.17725 1.03241 -0.30152 -0.14422 0.20728  95  GLN A CB  
701  C CG  . GLN A 91  ? 1.32915 1.21067 1.01210 -0.31307 -0.11785 0.20190  95  GLN A CG  
702  C CD  . GLN A 91  ? 1.33998 1.25492 1.05805 -0.29124 -0.09833 0.18151  95  GLN A CD  
703  O OE1 . GLN A 91  ? 1.32892 1.24012 1.07075 -0.26685 -0.09958 0.16940  95  GLN A OE1 
704  N NE2 . GLN A 91  ? 1.29632 1.24482 1.01779 -0.30112 -0.08092 0.17849  95  GLN A NE2 
705  N N   . LYS A 92  ? 1.56128 1.29527 1.26190 -0.31054 -0.21224 0.23924  96  LYS A N   
706  C CA  . LYS A 92  ? 1.59136 1.28281 1.30597 -0.30208 -0.24236 0.24525  96  LYS A CA  
707  C C   . LYS A 92  ? 1.61571 1.29502 1.31392 -0.29642 -0.25233 0.24658  96  LYS A C   
708  O O   . LYS A 92  ? 1.50952 1.15937 1.22677 -0.28450 -0.27573 0.24764  96  LYS A O   
709  C CB  . LYS A 92  ? 1.62432 1.27834 1.32494 -0.32522 -0.26768 0.26726  96  LYS A CB  
710  C CG  . LYS A 92  ? 1.80475 1.44103 1.54453 -0.31608 -0.28026 0.26290  96  LYS A CG  
711  C CD  . LYS A 92  ? 1.87664 1.48946 1.65289 -0.28993 -0.29977 0.25259  96  LYS A CD  
712  C CE  . LYS A 92  ? 1.83741 1.41748 1.64271 -0.28709 -0.32358 0.25389  96  LYS A CE  
713  N NZ  . LYS A 92  ? 1.78037 1.36753 1.63499 -0.25658 -0.32194 0.23062  96  LYS A NZ  
714  N N   . SER A 93  ? 1.61978 1.32188 1.28538 -0.30376 -0.23584 0.24493  97  SER A N   
715  C CA  . SER A 93  ? 1.60683 1.29650 1.25262 -0.30058 -0.24629 0.24617  97  SER A CA  
716  C C   . SER A 93  ? 1.52318 1.25013 1.16382 -0.28918 -0.21983 0.22797  97  SER A C   
717  O O   . SER A 93  ? 1.49635 1.25833 1.14618 -0.28541 -0.19429 0.21613  97  SER A O   
718  C CB  . SER A 93  ? 1.66169 1.32697 1.25723 -0.32937 -0.26352 0.26909  97  SER A CB  
719  O OG  . SER A 93  ? 1.73086 1.42687 1.28826 -0.34904 -0.24035 0.27064  97  SER A OG  
720  N N   . LEU A 94  ? 1.51538 1.23317 1.14218 -0.28342 -0.22805 0.22545  98  LEU A N   
721  C CA  . LEU A 94  ? 1.50601 1.25409 1.12656 -0.27262 -0.20649 0.20779  98  LEU A CA  
722  C C   . LEU A 94  ? 1.58865 1.36250 1.16626 -0.29253 -0.18720 0.20860  98  LEU A C   
723  O O   . LEU A 94  ? 1.54577 1.35575 1.12838 -0.28433 -0.16177 0.19170  98  LEU A O   
724  C CB  . LEU A 94  ? 1.39813 1.12752 1.01495 -0.26251 -0.22253 0.20482  98  LEU A CB  
725  C CG  . LEU A 94  ? 1.49483 1.24544 1.12382 -0.24279 -0.20798 0.18424  98  LEU A CG  
726  C CD1 . LEU A 94  ? 1.50640 1.23240 1.12544 -0.23910 -0.22937 0.18587  98  LEU A CD1 
727  C CD2 . LEU A 94  ? 1.47252 1.25844 1.07733 -0.24671 -0.18085 0.17158  98  LEU A CD2 
728  N N   . GLU A 95  ? 1.60184 1.35878 1.13712 -0.31900 -0.19919 0.22777  99  GLU A N   
729  C CA  . GLU A 95  ? 1.66206 1.44779 1.15473 -0.33991 -0.17921 0.22809  99  GLU A CA  
730  C C   . GLU A 95  ? 1.66657 1.48753 1.17616 -0.34371 -0.15482 0.22266  99  GLU A C   
731  O O   . GLU A 95  ? 1.67338 1.53512 1.17582 -0.34293 -0.12836 0.20752  99  GLU A O   
732  C CB  . GLU A 95  ? 1.77909 1.53880 1.22158 -0.37083 -0.19802 0.25295  99  GLU A CB  
733  C CG  . GLU A 95  ? 1.88832 1.67810 1.27815 -0.39414 -0.17843 0.25274  99  GLU A CG  
734  C CD  . GLU A 95  ? 1.93590 1.71814 1.28765 -0.39448 -0.18515 0.24788  99  GLU A CD  
735  O OE1 . GLU A 95  ? 1.92276 1.72276 1.28901 -0.37166 -0.17295 0.22419  99  GLU A OE1 
736  O OE2 . GLU A 95  ? 1.94969 1.70656 1.25581 -0.41844 -0.20418 0.26829  99  GLU A OE2 
737  N N   . GLU A 96  ? 1.65490 1.46110 1.19026 -0.34613 -0.16425 0.23298  100 GLU A N   
738  C CA  . GLU A 96  ? 1.63494 1.47056 1.18521 -0.35301 -0.14516 0.23068  100 GLU A CA  
739  C C   . GLU A 96  ? 1.47903 1.34339 1.07355 -0.32549 -0.12638 0.20769  100 GLU A C   
740  O O   . GLU A 96  ? 1.44171 1.33610 1.04970 -0.32901 -0.10854 0.20263  100 GLU A O   
741  C CB  . GLU A 96  ? 1.68120 1.48604 1.24051 -0.36712 -0.16532 0.25050  100 GLU A CB  
742  C CG  . GLU A 96  ? 1.75820 1.53219 1.27310 -0.39797 -0.18614 0.27699  100 GLU A CG  
743  C CD  . GLU A 96  ? 2.02285 1.79915 1.52949 -0.42548 -0.18536 0.29385  100 GLU A CD  
744  O OE1 . GLU A 96  ? 2.11516 1.92590 1.59377 -0.44697 -0.16441 0.29617  100 GLU A OE1 
745  O OE2 . GLU A 96  ? 2.08625 1.83127 1.61634 -0.42553 -0.20555 0.30365  100 GLU A OE2 
746  N N   . PHE A 97  ? 1.39531 1.25161 1.01176 -0.29989 -0.13072 0.19475  101 PHE A N   
747  C CA  . PHE A 97  ? 1.41668 1.29257 1.07610 -0.27439 -0.11805 0.17655  101 PHE A CA  
748  C C   . PHE A 97  ? 1.38543 1.30789 1.04564 -0.27168 -0.08961 0.16071  101 PHE A C   
749  O O   . PHE A 97  ? 1.45830 1.39818 1.09382 -0.27412 -0.07882 0.15273  101 PHE A O   
750  C CB  . PHE A 97  ? 1.39561 1.25497 1.07116 -0.25186 -0.12818 0.16766  101 PHE A CB  
751  C CG  . PHE A 97  ? 1.32266 1.20079 1.03763 -0.22704 -0.11614 0.15038  101 PHE A CG  
752  C CD1 . PHE A 97  ? 1.23855 1.11977 0.98636 -0.21999 -0.11477 0.14930  101 PHE A CD1 
753  C CD2 . PHE A 97  ? 1.28282 1.17363 1.00050 -0.21144 -0.10770 0.13549  101 PHE A CD2 
754  C CE1 . PHE A 97  ? 1.13765 1.03598 0.91776 -0.19898 -0.10436 0.13494  101 PHE A CE1 
755  C CE2 . PHE A 97  ? 1.15309 1.05888 0.90480 -0.19047 -0.09844 0.12193  101 PHE A CE2 
756  C CZ  . PHE A 97  ? 1.16729 1.07747 0.94904 -0.18473 -0.09648 0.12231  101 PHE A CZ  
757  N N   . GLN A 98  ? 1.32679 1.27002 1.01565 -0.26680 -0.07830 0.15530  102 GLN A N   
758  C CA  . GLN A 98  ? 1.27841 1.26640 0.97600 -0.26097 -0.05338 0.13899  102 GLN A CA  
759  C C   . GLN A 98  ? 1.22953 1.23014 0.96865 -0.23598 -0.04690 0.12447  102 GLN A C   
760  O O   . GLN A 98  ? 1.24928 1.27045 0.99723 -0.21975 -0.03528 0.10820  102 GLN A O   
761  C CB  . GLN A 98  ? 1.31037 1.32244 0.99811 -0.28427 -0.04225 0.14640  102 GLN A CB  
762  C CG  . GLN A 98  ? 1.46894 1.47971 1.11126 -0.31212 -0.04286 0.15961  102 GLN A CG  
763  C CD  . GLN A 98  ? 1.54713 1.58432 1.16592 -0.30954 -0.02721 0.14508  102 GLN A CD  
764  O OE1 . GLN A 98  ? 1.58030 1.66157 1.20118 -0.31146 -0.00475 0.13211  102 GLN A OE1 
765  N NE2 . GLN A 98  ? 1.53088 1.54196 1.12841 -0.30482 -0.03972 0.14589  102 GLN A NE2 
766  N N   . ASP A 99  ? 1.20722 1.19494 0.97104 -0.23306 -0.05525 0.12994  103 ASP A N   
767  C CA  . ASP A 99  ? 1.13397 1.13911 0.93305 -0.21494 -0.04720 0.11809  103 ASP A CA  
768  C C   . ASP A 99  ? 1.04714 1.02441 0.86878 -0.19978 -0.06199 0.11900  103 ASP A C   
769  O O   . ASP A 99  ? 1.10935 1.05598 0.92720 -0.20664 -0.07899 0.13034  103 ASP A O   
770  C CB  . ASP A 99  ? 1.01773 1.04293 0.82805 -0.22638 -0.03979 0.12057  103 ASP A CB  
771  C CG  . ASP A 99  ? 1.22945 1.28171 1.01714 -0.24768 -0.02679 0.12354  103 ASP A CG  
772  O OD1 . ASP A 99  ? 1.25625 1.33076 1.03150 -0.24441 -0.01416 0.11351  103 ASP A OD1 
773  O OD2 . ASP A 99  ? 1.18852 1.24065 0.97162 -0.26808 -0.02920 0.13523  103 ASP A OD2 
774  N N   . VAL A 100 ? 0.99438 0.98397 0.84078 -0.17963 -0.05562 0.10684  104 VAL A N   
775  C CA  . VAL A 100 ? 0.98572 0.95843 0.85654 -0.16491 -0.06515 0.10526  104 VAL A CA  
776  C C   . VAL A 100 ? 0.97441 0.96593 0.86824 -0.15937 -0.05747 0.09942  104 VAL A C   
777  O O   . VAL A 100 ? 1.02964 1.04983 0.92668 -0.15782 -0.04382 0.09231  104 VAL A O   
778  C CB  . VAL A 100 ? 1.00132 0.97097 0.87890 -0.14780 -0.06559 0.09768  104 VAL A CB  
779  C CG1 . VAL A 100 ? 0.97503 0.93100 0.87770 -0.13492 -0.07412 0.09662  104 VAL A CG1 
780  C CG2 . VAL A 100 ? 0.97879 0.93175 0.83178 -0.15386 -0.07326 0.10214  104 VAL A CG2 
781  N N   . TYR A 101 ? 0.99599 0.97219 0.90610 -0.15636 -0.06692 0.10139  105 TYR A N   
782  C CA  . TYR A 101 ? 0.95806 0.94943 0.88832 -0.15111 -0.06163 0.09531  105 TYR A CA  
783  C C   . TYR A 101 ? 0.96546 0.94971 0.91602 -0.13423 -0.06558 0.08933  105 TYR A C   
784  O O   . TYR A 101 ? 0.92253 0.88357 0.87746 -0.13216 -0.07763 0.09216  105 TYR A O   
785  C CB  . TYR A 101 ? 0.92736 0.90988 0.85685 -0.16604 -0.06851 0.10171  105 TYR A CB  
786  C CG  . TYR A 101 ? 1.02089 1.01611 0.93177 -0.18609 -0.06271 0.10866  105 TYR A CG  
787  C CD1 . TYR A 101 ? 0.96590 0.94631 0.85166 -0.20093 -0.06840 0.11953  105 TYR A CD1 
788  C CD2 . TYR A 101 ? 1.02132 1.04479 0.93964 -0.19148 -0.05191 0.10476  105 TYR A CD2 
789  C CE1 . TYR A 101 ? 0.99560 0.99063 0.86256 -0.22159 -0.06172 0.12652  105 TYR A CE1 
790  C CE2 . TYR A 101 ? 0.86973 0.90934 0.77307 -0.21152 -0.04528 0.11101  105 TYR A CE2 
791  C CZ  . TYR A 101 ? 1.02625 1.05210 0.90314 -0.22696 -0.04944 0.12200  105 TYR A CZ  
792  O OH  . TYR A 101 ? 1.08587 1.12948 0.94540 -0.24910 -0.04192 0.12911  105 TYR A OH  
793  N N   . ILE A 102 ? 0.94489 0.95023 0.90797 -0.12273 -0.05584 0.08130  106 ILE A N   
794  C CA  . ILE A 102 ? 0.84172 0.84661 0.82232 -0.10865 -0.05672 0.07601  106 ILE A CA  
795  C C   . ILE A 102 ? 0.85010 0.86575 0.84298 -0.10772 -0.05458 0.07119  106 ILE A C   
796  O O   . ILE A 102 ? 0.79122 0.82677 0.78390 -0.11009 -0.04718 0.06885  106 ILE A O   
797  C CB  . ILE A 102 ? 0.86461 0.88301 0.84764 -0.09763 -0.04933 0.07212  106 ILE A CB  
798  C CG1 . ILE A 102 ? 0.85117 0.86370 0.81890 -0.09985 -0.04968 0.07435  106 ILE A CG1 
799  C CG2 . ILE A 102 ? 0.90922 0.92325 0.90662 -0.08685 -0.05186 0.07006  106 ILE A CG2 
800  C CD1 . ILE A 102 ? 0.93272 0.92084 0.89648 -0.10171 -0.06069 0.07940  106 ILE A CD1 
801  N N   . VAL A 103 ? 0.83660 0.84092 0.84127 -0.10356 -0.06118 0.06824  107 VAL A N   
802  C CA  . VAL A 103 ? 0.79670 0.80929 0.81164 -0.10219 -0.06031 0.06159  107 VAL A CA  
803  C C   . VAL A 103 ? 0.79269 0.81596 0.81911 -0.08954 -0.05567 0.05521  107 VAL A C   
804  O O   . VAL A 103 ? 0.88203 0.89629 0.91595 -0.08340 -0.05900 0.05428  107 VAL A O   
805  C CB  . VAL A 103 ? 0.86756 0.85932 0.88685 -0.10814 -0.07208 0.06084  107 VAL A CB  
806  C CG1 . VAL A 103 ? 0.75808 0.75892 0.78634 -0.10695 -0.07125 0.05195  107 VAL A CG1 
807  C CG2 . VAL A 103 ? 0.84733 0.82495 0.85238 -0.12383 -0.07864 0.07066  107 VAL A CG2 
808  N N   . MET A 104 ? 0.78578 0.82910 0.81376 -0.08678 -0.04867 0.05132  108 MET A N   
809  C CA  . MET A 104 ? 0.81214 0.86840 0.84604 -0.07749 -0.04349 0.04784  108 MET A CA  
810  C C   . MET A 104 ? 0.75233 0.82038 0.78923 -0.07736 -0.04209 0.04039  108 MET A C   
811  O O   . MET A 104 ? 0.89600 0.96595 0.93064 -0.08397 -0.04412 0.03863  108 MET A O   
812  C CB  . MET A 104 ? 0.79914 0.86847 0.82862 -0.07370 -0.03788 0.05211  108 MET A CB  
813  C CG  . MET A 104 ? 0.83963 0.90041 0.86351 -0.07387 -0.03857 0.05749  108 MET A CG  
814  S SD  . MET A 104 ? 0.89400 0.97159 0.91484 -0.06948 -0.03343 0.05843  108 MET A SD  
815  C CE  . MET A 104 ? 0.83988 0.92759 0.85565 -0.07933 -0.03096 0.05677  108 MET A CE  
816  N N   . GLU A 105 ? 0.77414 0.85187 0.81492 -0.07096 -0.03841 0.03630  109 GLU A N   
817  C CA  . GLU A 105 ? 0.83712 0.92877 0.87642 -0.07098 -0.03651 0.02917  109 GLU A CA  
818  C C   . GLU A 105 ? 0.82243 0.92774 0.85521 -0.07340 -0.03499 0.03335  109 GLU A C   
819  O O   . GLU A 105 ? 0.77961 0.88800 0.81043 -0.07161 -0.03322 0.04059  109 GLU A O   
820  C CB  . GLU A 105 ? 0.74652 0.84935 0.78754 -0.06534 -0.03140 0.02534  109 GLU A CB  
821  C CG  . GLU A 105 ? 0.95893 1.07042 0.99579 -0.06257 -0.02716 0.03480  109 GLU A CG  
822  C CD  . GLU A 105 ? 1.09460 1.21619 1.13364 -0.06003 -0.02181 0.03309  109 GLU A CD  
823  O OE1 . GLU A 105 ? 1.18540 1.31992 1.22076 -0.06056 -0.01853 0.02517  109 GLU A OE1 
824  O OE2 . GLU A 105 ? 1.01195 1.13005 1.05581 -0.05845 -0.02066 0.03952  109 GLU A OE2 
825  N N   . LEU A 106 ? 0.87439 0.98775 0.90568 -0.07710 -0.03688 0.02753  110 LEU A N   
826  C CA  . LEU A 106 ? 0.83762 0.96526 0.86683 -0.08005 -0.03722 0.03014  110 LEU A CA  
827  C C   . LEU A 106 ? 0.77977 0.92341 0.80427 -0.07538 -0.03599 0.03057  110 LEU A C   
828  O O   . LEU A 106 ? 0.92192 1.06966 0.94190 -0.07483 -0.03602 0.02431  110 LEU A O   
829  C CB  . LEU A 106 ? 0.79275 0.92006 0.82395 -0.08856 -0.04196 0.02468  110 LEU A CB  
830  C CG  . LEU A 106 ? 0.77865 0.92467 0.81161 -0.09236 -0.04275 0.02620  110 LEU A CG  
831  C CD1 . LEU A 106 ? 0.65322 0.80473 0.68909 -0.09202 -0.03898 0.03349  110 LEU A CD1 
832  C CD2 . LEU A 106 ? 0.79289 0.93862 0.82927 -0.10303 -0.04823 0.02148  110 LEU A CD2 
833  N N   . MET A 107 ? 0.73763 0.89023 0.76263 -0.07219 -0.03582 0.03739  111 MET A N   
834  C CA  . MET A 107 ? 0.78410 0.94966 0.80426 -0.06867 -0.03793 0.04013  111 MET A CA  
835  C C   . MET A 107 ? 0.86814 1.04848 0.89284 -0.07071 -0.04256 0.03873  111 MET A C   
836  O O   . MET A 107 ? 0.85955 1.04248 0.89250 -0.07446 -0.04212 0.03707  111 MET A O   
837  C CB  . MET A 107 ? 0.71517 0.87772 0.73484 -0.06236 -0.03756 0.04917  111 MET A CB  
838  C CG  . MET A 107 ? 0.76572 0.91658 0.78312 -0.06130 -0.03342 0.05118  111 MET A CG  
839  S SD  . MET A 107 ? 0.88760 1.04547 0.89551 -0.06384 -0.03030 0.04670  111 MET A SD  
840  C CE  . MET A 107 ? 0.69512 0.86432 0.69155 -0.06343 -0.03458 0.05671  111 MET A CE  
841  N N   . ASP A 108 ? 0.78590 0.97744 0.80512 -0.06931 -0.04739 0.03975  112 ASP A N   
842  C CA  . ASP A 108 ? 0.71198 0.91872 0.73721 -0.07200 -0.05337 0.03670  112 ASP A CA  
843  C C   . ASP A 108 ? 0.81268 1.02997 0.85116 -0.06669 -0.05611 0.04092  112 ASP A C   
844  O O   . ASP A 108 ? 0.91452 1.14572 0.96506 -0.06974 -0.05795 0.03706  112 ASP A O   
845  C CB  . ASP A 108 ? 0.77135 0.98645 0.78496 -0.07308 -0.05967 0.03554  112 ASP A CB  
846  C CG  . ASP A 108 ? 0.88822 1.09806 0.89090 -0.07832 -0.05733 0.02641  112 ASP A CG  
847  O OD1 . ASP A 108 ? 0.86415 1.08018 0.85250 -0.07933 -0.06051 0.02476  112 ASP A OD1 
848  O OD2 . ASP A 108 ? 0.94822 1.14717 0.95599 -0.08120 -0.05301 0.02065  112 ASP A OD2 
849  N N   . ALA A 109 ? 0.84764 1.06001 0.88589 -0.05879 -0.05720 0.04787  113 ALA A N   
850  C CA  . ALA A 109 ? 0.78197 1.00434 0.83504 -0.05145 -0.06136 0.04921  113 ALA A CA  
851  C C   . ALA A 109 ? 0.75333 0.96181 0.80527 -0.04367 -0.06122 0.05545  113 ALA A C   
852  O O   . ALA A 109 ? 0.69575 0.89054 0.73487 -0.04441 -0.06068 0.06148  113 ALA A O   
853  C CB  . ALA A 109 ? 0.75137 0.98799 0.80851 -0.04849 -0.07287 0.05070  113 ALA A CB  
854  N N   . ASN A 110 ? 0.72853 0.94222 0.79499 -0.03633 -0.06211 0.05314  114 ASN A N   
855  C CA  . ASN A 110 ? 0.72029 0.91986 0.78701 -0.02779 -0.06585 0.05854  114 ASN A CA  
856  C C   . ASN A 110 ? 0.74116 0.94250 0.81134 -0.02080 -0.07996 0.06475  114 ASN A C   
857  O O   . ASN A 110 ? 0.83801 1.05416 0.91256 -0.02141 -0.08661 0.06359  114 ASN A O   
858  C CB  . ASN A 110 ? 0.75274 0.95345 0.83082 -0.02255 -0.06045 0.05165  114 ASN A CB  
859  C CG  . ASN A 110 ? 0.72842 0.95006 0.82714 -0.01446 -0.06445 0.04374  114 ASN A CG  
860  O OD1 . ASN A 110 ? 0.69443 0.92121 0.80203 -0.00709 -0.07616 0.04582  114 ASN A OD1 
861  N ND2 . ASN A 110 ? 0.71845 0.95316 0.82544 -0.01597 -0.05497 0.03441  114 ASN A ND2 
862  N N   . LEU A 111 ? 0.66374 0.96014 0.82614 -0.12779 -0.01136 -0.00365 115 LEU A N   
863  C CA  . LEU A 111 ? 0.69306 1.00935 0.87128 -0.11101 -0.02597 -0.00317 115 LEU A CA  
864  C C   . LEU A 111 ? 0.75075 1.11264 0.96618 -0.10843 -0.03014 -0.01450 115 LEU A C   
865  O O   . LEU A 111 ? 0.74312 1.12145 0.97087 -0.09563 -0.04595 -0.01502 115 LEU A O   
866  C CB  . LEU A 111 ? 0.67674 0.97423 0.84643 -0.09269 -0.02819 0.00700  115 LEU A CB  
867  C CG  . LEU A 111 ? 0.75991 1.05646 0.92758 -0.07727 -0.04280 0.01306  115 LEU A CG  
868  C CD1 . LEU A 111 ? 0.72819 1.00919 0.87398 -0.08428 -0.04741 0.01506  115 LEU A CD1 
869  C CD2 . LEU A 111 ? 0.71938 0.99403 0.87782 -0.06380 -0.04146 0.02251  115 LEU A CD2 
870  N N   . CYS A 112 ? 0.63248 1.01511 0.86566 -0.11999 -0.01677 -0.02418 116 CYS A N   
871  C CA  . CYS A 112 ? 0.79561 1.22723 1.07074 -0.11697 -0.01980 -0.03831 116 CYS A CA  
872  C C   . CYS A 112 ? 0.82453 1.28190 1.11553 -0.12363 -0.03301 -0.04670 116 CYS A C   
873  O O   . CYS A 112 ? 0.90998 1.40576 1.23522 -0.11274 -0.04569 -0.05618 116 CYS A O   
874  C CB  . CYS A 112 ? 0.76733 1.21751 1.05659 -0.13321 0.00111  -0.04926 116 CYS A CB  
875  S SG  . CYS A 112 ? 0.80809 1.23499 1.08119 -0.12559 0.01604  -0.04333 116 CYS A SG  
876  N N   . GLN A 113 ? 0.81402 1.25077 1.08149 -0.14085 -0.03153 -0.04467 117 GLN A N   
877  C CA  . GLN A 113 ? 0.98177 1.44200 1.26240 -0.14910 -0.04437 -0.05413 117 GLN A CA  
878  C C   . GLN A 113 ? 0.88024 1.33741 1.15384 -0.12888 -0.06757 -0.04772 117 GLN A C   
879  O O   . GLN A 113 ? 0.92238 1.41369 1.22100 -0.12329 -0.08455 -0.05672 117 GLN A O   
880  C CB  . GLN A 113 ? 1.02412 1.45739 1.27805 -0.17325 -0.03620 -0.05426 117 GLN A CB  
881  C CG  . GLN A 113 ? 1.10278 1.53986 1.36198 -0.19854 -0.01479 -0.06185 117 GLN A CG  
882  C CD  . GLN A 113 ? 1.20038 1.60484 1.43094 -0.22197 -0.00940 -0.06158 117 GLN A CD  
883  O OE1 . GLN A 113 ? 1.08846 1.49417 1.31610 -0.22546 -0.02233 -0.06588 117 GLN A OE1 
884  N NE2 . GLN A 113 ? 1.12061 1.49398 1.32820 -0.23852 0.00887  -0.05721 117 GLN A NE2 
885  N N   . VAL A 114 ? 0.85272 1.26887 1.09137 -0.11859 -0.06869 -0.03259 118 VAL A N   
886  C CA  . VAL A 114 ? 0.90822 1.31268 1.12969 -0.10288 -0.08720 -0.02436 118 VAL A CA  
887  C C   . VAL A 114 ? 0.93239 1.35818 1.17671 -0.08075 -0.10143 -0.02344 118 VAL A C   
888  O O   . VAL A 114 ? 0.94631 1.37594 1.18607 -0.06925 -0.12194 -0.02100 118 VAL A O   
889  C CB  . VAL A 114 ? 0.91691 1.27482 1.09971 -0.09965 -0.07959 -0.01025 118 VAL A CB  
890  C CG1 . VAL A 114 ? 0.92785 1.27146 1.09162 -0.08325 -0.09391 -0.00001 118 VAL A CG1 
891  C CG2 . VAL A 114 ? 0.95388 1.28940 1.11348 -0.11794 -0.07142 -0.01265 118 VAL A CG2 
892  N N   . ILE A 115 ? 0.87005 1.30711 1.13663 -0.07409 -0.09163 -0.02561 119 ILE A N   
893  C CA  . ILE A 115 ? 0.91849 1.36533 1.20233 -0.05060 -0.10391 -0.02338 119 ILE A CA  
894  C C   . ILE A 115 ? 0.99725 1.48661 1.31626 -0.04182 -0.12442 -0.03568 119 ILE A C   
895  O O   . ILE A 115 ? 0.97140 1.45924 1.29272 -0.02042 -0.14441 -0.03073 119 ILE A O   
896  C CB  . ILE A 115 ? 0.84676 1.29549 1.14555 -0.04742 -0.08657 -0.02567 119 ILE A CB  
897  C CG1 . ILE A 115 ? 0.71108 1.11397 0.97475 -0.04321 -0.07858 -0.00988 119 ILE A CG1 
898  C CG2 . ILE A 115 ? 0.79390 1.27440 1.13159 -0.02797 -0.09649 -0.03482 119 ILE A CG2 
899  C CD1 . ILE A 115 ? 0.80896 1.20756 1.07624 -0.04843 -0.05885 -0.01248 119 ILE A CD1 
900  N N   . GLN A 116 ? 1.00911 1.53590 1.35602 -0.05805 -0.12117 -0.05209 120 GLN A N   
901  C CA  . GLN A 116 ? 1.10003 1.67371 1.48742 -0.04944 -0.14196 -0.06675 120 GLN A CA  
902  C C   . GLN A 116 ? 1.13276 1.69789 1.49803 -0.04530 -0.16808 -0.06181 120 GLN A C   
903  O O   . GLN A 116 ? 1.17636 1.76845 1.56531 -0.02912 -0.19343 -0.06834 120 GLN A O   
904  C CB  . GLN A 116 ? 1.19643 1.81694 1.62456 -0.07062 -0.12859 -0.08799 120 GLN A CB  
905  C CG  . GLN A 116 ? 1.19050 1.78972 1.59353 -0.10059 -0.10438 -0.08659 120 GLN A CG  
906  C CD  . GLN A 116 ? 1.22940 1.87250 1.66816 -0.12557 -0.09440 -0.10736 120 GLN A CD  
907  O OE1 . GLN A 116 ? 1.25418 1.92209 1.70753 -0.13242 -0.11021 -0.11761 120 GLN A OE1 
908  N NE2 . GLN A 116 ? 1.15810 1.80948 1.60856 -0.14103 -0.06770 -0.11386 120 GLN A NE2 
909  N N   . MET A 117 ? 1.12314 1.65158 1.44329 -0.05891 -0.16339 -0.05165 121 MET A N   
910  C CA  . MET A 117 ? 1.18038 1.69902 1.47389 -0.05805 -0.18554 -0.04836 121 MET A CA  
911  C C   . MET A 117 ? 1.15674 1.63534 1.41084 -0.03858 -0.19820 -0.02904 121 MET A C   
912  O O   . MET A 117 ? 1.13573 1.58714 1.37706 -0.03071 -0.18569 -0.01715 121 MET A O   
913  C CB  . MET A 117 ? 1.18199 1.68114 1.44631 -0.08274 -0.17354 -0.04967 121 MET A CB  
914  C CG  . MET A 117 ? 1.17136 1.62759 1.40375 -0.08980 -0.14920 -0.03757 121 MET A CG  
915  S SD  . MET A 117 ? 1.37364 1.80276 1.57140 -0.11437 -0.13873 -0.04014 121 MET A SD  
916  C CE  . MET A 117 ? 1.34850 1.82616 1.58722 -0.13384 -0.14339 -0.06250 121 MET A CE  
917  N N   . GLU A 118 ? 1.21103 1.68468 1.44322 -0.03253 -0.22328 -0.02616 122 GLU A N   
918  C CA  . GLU A 118 ? 1.22870 1.66246 1.41816 -0.01651 -0.23667 -0.00749 122 GLU A CA  
919  C C   . GLU A 118 ? 1.18945 1.58059 1.32561 -0.03083 -0.22206 0.00321  122 GLU A C   
920  O O   . GLU A 118 ? 1.18676 1.57892 1.30604 -0.04610 -0.22350 -0.00359 122 GLU A O   
921  C CB  . GLU A 118 ? 1.33817 1.78282 1.52365 -0.00196 -0.27258 -0.00833 122 GLU A CB  
922  C CG  . GLU A 118 ? 1.50780 1.90342 1.63922 0.01182  -0.28594 0.01319  122 GLU A CG  
923  C CD  . GLU A 118 ? 1.63160 2.01534 1.72160 0.01020  -0.31116 0.01598  122 GLU A CD  
924  O OE1 . GLU A 118 ? 1.63566 1.99876 1.68660 -0.00811 -0.29909 0.01761  122 GLU A OE1 
925  O OE2 . GLU A 118 ? 1.66663 2.06016 1.76170 0.02816  -0.34387 0.01603  122 GLU A OE2 
926  N N   . LEU A 119 ? 1.16526 1.52050 1.27725 -0.02595 -0.20803 0.01807  123 LEU A N   
927  C CA  . LEU A 119 ? 1.08256 1.40042 1.14966 -0.03774 -0.19223 0.02666  123 LEU A CA  
928  C C   . LEU A 119 ? 1.09212 1.37724 1.11277 -0.02897 -0.20642 0.04167  123 LEU A C   
929  O O   . LEU A 119 ? 1.14633 1.42218 1.16702 -0.01211 -0.21905 0.05172  123 LEU A O   
930  C CB  . LEU A 119 ? 1.06820 1.36966 1.14054 -0.04052 -0.16592 0.03154  123 LEU A CB  
931  C CG  . LEU A 119 ? 1.09753 1.41359 1.19351 -0.05557 -0.14640 0.01993  123 LEU A CG  
932  C CD1 . LEU A 119 ? 1.00320 1.30787 1.07459 -0.07279 -0.13984 0.01420  123 LEU A CD1 
933  C CD2 . LEU A 119 ? 1.13149 1.49013 1.27408 -0.05601 -0.15164 0.00622  123 LEU A CD2 
934  N N   . ASP A 120 ? 0.99506 1.26046 0.97383 -0.04094 -0.20422 0.04274  124 ASP A N   
935  C CA  . ASP A 120 ? 1.04707 1.27585 0.97350 -0.03693 -0.21167 0.05787  124 ASP A CA  
936  C C   . ASP A 120 ? 1.05359 1.25206 0.96600 -0.03773 -0.18822 0.06971  124 ASP A C   
937  O O   . ASP A 120 ? 1.01451 1.22055 0.95654 -0.04023 -0.16879 0.06574  124 ASP A O   
938  C CB  . ASP A 120 ? 1.04105 1.25985 0.92588 -0.05059 -0.21477 0.05303  124 ASP A CB  
939  C CG  . ASP A 120 ? 1.15160 1.36771 1.03616 -0.06752 -0.18804 0.04324  124 ASP A CG  
940  O OD1 . ASP A 120 ? 1.14820 1.38933 1.07290 -0.07286 -0.18057 0.03098  124 ASP A OD1 
941  O OD2 . ASP A 120 ? 1.26931 1.45723 1.11358 -0.07541 -0.17402 0.04749  124 ASP A OD2 
942  N N   . HIS A 121 ? 1.09289 1.25587 0.95794 -0.03674 -0.19025 0.08422  125 HIS A N   
943  C CA  . HIS A 121 ? 1.06710 1.20320 0.92225 -0.03744 -0.17012 0.09534  125 HIS A CA  
944  C C   . HIS A 121 ? 1.03455 1.16865 0.88918 -0.05255 -0.14147 0.08758  125 HIS A C   
945  O O   . HIS A 121 ? 0.99042 1.12440 0.86908 -0.05215 -0.12416 0.08760  125 HIS A O   
946  C CB  . HIS A 121 ? 1.12970 1.22637 0.93160 -0.03564 -0.17832 0.11284  125 HIS A CB  
947  C CG  . HIS A 121 ? 1.12772 1.21493 0.93508 -0.01698 -0.20164 0.12431  125 HIS A CG  
948  N ND1 . HIS A 121 ? 1.02960 1.12856 0.88201 -0.00469 -0.20008 0.12346  125 HIS A ND1 
949  C CD2 . HIS A 121 ? 1.27344 1.33953 1.04657 -0.00722 -0.22888 0.13578  125 HIS A CD2 
950  C CE1 . HIS A 121 ? 1.09683 1.18258 0.94513 0.01251  -0.22440 0.13306  125 HIS A CE1 
951  N NE2 . HIS A 121 ? 1.21040 1.27517 1.01082 0.01190  -0.24336 0.14138  125 HIS A NE2 
952  N N   . GLU A 122 ? 1.02270 1.15534 0.85129 -0.06490 -0.13749 0.07951  126 GLU A N   
953  C CA  . GLU A 122 ? 0.97229 1.10302 0.80308 -0.07680 -0.11206 0.06997  126 GLU A CA  
954  C C   . GLU A 122 ? 0.93429 1.08658 0.81459 -0.07496 -0.10357 0.06098  126 GLU A C   
955  O O   . GLU A 122 ? 0.95570 1.10200 0.85006 -0.07543 -0.08570 0.06150  126 GLU A O   
956  C CB  . GLU A 122 ? 0.97279 1.10280 0.77493 -0.08866 -0.11189 0.05866  126 GLU A CB  
957  C CG  . GLU A 122 ? 1.14874 1.25106 0.89683 -0.09733 -0.10232 0.06354  126 GLU A CG  
958  C CD  . GLU A 122 ? 1.35802 1.44151 1.06518 -0.09274 -0.12261 0.07898  126 GLU A CD  
959  O OE1 . GLU A 122 ? 1.38405 1.47790 1.10930 -0.08023 -0.14621 0.08481  126 GLU A OE1 
960  O OE2 . GLU A 122 ? 1.44358 1.50109 1.09933 -0.10160 -0.11527 0.08470  126 GLU A OE2 
961  N N   . ARG A 123 ? 0.90797 1.08555 0.81507 -0.07312 -0.11692 0.05288  127 ARG A N   
962  C CA  . ARG A 123 ? 0.92101 1.11579 0.86780 -0.07519 -0.10704 0.04399  127 ARG A CA  
963  C C   . ARG A 123 ? 0.85376 1.05105 0.82763 -0.06466 -0.10309 0.05133  127 ARG A C   
964  O O   . ARG A 123 ? 0.83213 1.02852 0.82418 -0.06670 -0.08809 0.04851  127 ARG A O   
965  C CB  . ARG A 123 ? 0.83792 1.06013 0.80595 -0.07940 -0.11992 0.03236  127 ARG A CB  
966  C CG  . ARG A 123 ? 0.95049 1.16903 0.89877 -0.09310 -0.11800 0.02100  127 ARG A CG  
967  C CD  . ARG A 123 ? 0.93040 1.17492 0.89170 -0.09803 -0.13594 0.01034  127 ARG A CD  
968  N NE  . ARG A 123 ? 0.90413 1.14347 0.85401 -0.11332 -0.12955 -0.00286 127 ARG A NE  
969  C CZ  . ARG A 123 ? 1.04140 1.27205 0.95761 -0.11958 -0.13738 -0.00821 127 ARG A CZ  
970  N NH1 . ARG A 123 ? 1.11248 1.33930 1.00103 -0.11269 -0.15361 -0.00067 127 ARG A NH1 
971  N NH2 . ARG A 123 ? 0.99646 1.21904 0.90355 -0.13312 -0.12949 -0.02156 127 ARG A NH2 
972  N N   . MET A 124 ? 0.88094 1.07958 0.85667 -0.05267 -0.11783 0.06011  128 MET A N   
973  C CA  . MET A 124 ? 0.81071 1.01011 0.81106 -0.04201 -0.11480 0.06563  128 MET A CA  
974  C C   . MET A 124 ? 0.88563 1.05968 0.87313 -0.04419 -0.09687 0.07286  128 MET A C   
975  O O   . MET A 124 ? 0.82653 1.00320 0.83640 -0.04359 -0.08480 0.07037  128 MET A O   
976  C CB  . MET A 124 ? 0.80521 1.00559 0.80576 -0.02730 -0.13636 0.07322  128 MET A CB  
977  C CG  . MET A 124 ? 0.84207 1.04568 0.87080 -0.01430 -0.13669 0.07612  128 MET A CG  
978  S SD  . MET A 124 ? 1.20718 1.44406 1.26940 0.00069  -0.16181 0.06863  128 MET A SD  
979  C CE  . MET A 124 ? 1.04014 1.25448 1.06024 0.00855  -0.18840 0.08063  128 MET A CE  
980  N N   . SER A 125 ? 0.82465 0.97478 0.77523 -0.04836 -0.09420 0.08062  129 SER A N   
981  C CA  . SER A 125 ? 0.90210 1.03208 0.84452 -0.05178 -0.07657 0.08590  129 SER A CA  
982  C C   . SER A 125 ? 0.87466 1.00962 0.82796 -0.06049 -0.05853 0.07499  129 SER A C   
983  O O   . SER A 125 ? 0.76685 0.89717 0.73465 -0.06002 -0.04601 0.07485  129 SER A O   
984  C CB  . SER A 125 ? 0.88562 0.98920 0.78446 -0.05693 -0.07544 0.09612  129 SER A CB  
985  O OG  . SER A 125 ? 1.01627 1.11980 0.88831 -0.06666 -0.07423 0.08999  129 SER A OG  
986  N N   . TYR A 126 ? 0.84723 0.98969 0.79302 -0.06795 -0.05835 0.06518  130 TYR A N   
987  C CA  . TYR A 126 ? 0.85021 0.99316 0.80525 -0.07430 -0.04352 0.05430  130 TYR A CA  
988  C C   . TYR A 126 ? 0.84382 0.99718 0.83250 -0.07044 -0.04182 0.05068  130 TYR A C   
989  O O   . TYR A 126 ? 0.80497 0.95239 0.80495 -0.07015 -0.03049 0.04778  130 TYR A O   
990  C CB  . TYR A 126 ? 0.79975 0.94514 0.73854 -0.08287 -0.04529 0.04379  130 TYR A CB  
991  C CG  . TYR A 126 ? 0.91118 1.05104 0.85447 -0.08812 -0.03097 0.03190  130 TYR A CG  
992  C CD1 . TYR A 126 ? 0.87909 1.00930 0.82299 -0.08748 -0.01568 0.03071  130 TYR A CD1 
993  C CD2 . TYR A 126 ? 0.84147 0.98534 0.79025 -0.09353 -0.03348 0.02086  130 TYR A CD2 
994  C CE1 . TYR A 126 ? 0.85155 0.97739 0.80297 -0.08926 -0.00504 0.01825  130 TYR A CE1 
995  C CE2 . TYR A 126 ? 0.87009 1.00410 0.82197 -0.09629 -0.02274 0.01002  130 TYR A CE2 
996  C CZ  . TYR A 126 ? 0.89055 1.01611 0.84489 -0.09264 -0.00944 0.00850  130 TYR A CZ  
997  O OH  . TYR A 126 ? 0.98085 1.09720 0.94140 -0.09255 -0.00114 -0.00378 130 TYR A OH  
998  N N   . LEU A 127 ? 0.76506 0.93453 0.76978 -0.06748 -0.05320 0.05025  131 LEU A N   
999  C CA  . LEU A 127 ? 0.77014 0.94884 0.80189 -0.06621 -0.04991 0.04655  131 LEU A CA  
1000 C C   . LEU A 127 ? 0.69715 0.86941 0.74072 -0.05812 -0.04483 0.05308  131 LEU A C   
1001 O O   . LEU A 127 ? 0.75239 0.92084 0.80739 -0.05854 -0.03692 0.05020  131 LEU A O   
1002 C CB  . LEU A 127 ? 0.69485 0.89653 0.74339 -0.06613 -0.06104 0.04282  131 LEU A CB  
1003 C CG  . LEU A 127 ? 0.74029 0.95184 0.78348 -0.07657 -0.06636 0.03361  131 LEU A CG  
1004 C CD1 . LEU A 127 ? 0.69082 0.93140 0.75773 -0.07615 -0.07764 0.02864  131 LEU A CD1 
1005 C CD2 . LEU A 127 ? 0.71978 0.92027 0.76122 -0.08673 -0.05498 0.02618  131 LEU A CD2 
1006 N N   . LEU A 128 ? 0.76601 0.93426 0.80498 -0.05079 -0.05068 0.06184  132 LEU A N   
1007 C CA  . LEU A 128 ? 0.80551 0.96494 0.85430 -0.04422 -0.04606 0.06724  132 LEU A CA  
1008 C C   . LEU A 128 ? 0.77151 0.91654 0.81387 -0.04887 -0.03286 0.06645  132 LEU A C   
1009 O O   . LEU A 128 ? 0.67781 0.82086 0.73510 -0.04707 -0.02671 0.06400  132 LEU A O   
1010 C CB  . LEU A 128 ? 0.65511 0.80709 0.69596 -0.03620 -0.05608 0.07709  132 LEU A CB  
1011 C CG  . LEU A 128 ? 0.82310 0.99300 0.87694 -0.02803 -0.07178 0.07581  132 LEU A CG  
1012 C CD1 . LEU A 128 ? 0.74325 0.90025 0.77979 -0.01979 -0.08621 0.08608  132 LEU A CD1 
1013 C CD2 . LEU A 128 ? 0.72162 0.90632 0.80630 -0.02123 -0.07067 0.07040  132 LEU A CD2 
1014 N N   . TYR A 129 ? 0.75050 0.88708 0.77114 -0.05510 -0.02848 0.06679  133 TYR A N   
1015 C CA  . TYR A 129 ? 0.75035 0.87898 0.76988 -0.05973 -0.01468 0.06250  133 TYR A CA  
1016 C C   . TYR A 129 ? 0.74886 0.88209 0.78667 -0.05922 -0.01059 0.05274  133 TYR A C   
1017 O O   . TYR A 129 ? 0.73398 0.86450 0.78652 -0.05655 -0.00516 0.05059  133 TYR A O   
1018 C CB  . TYR A 129 ? 0.71560 0.83846 0.70891 -0.06776 -0.00908 0.06040  133 TYR A CB  
1019 C CG  . TYR A 129 ? 0.81445 0.93516 0.81115 -0.07244 0.00627  0.05132  133 TYR A CG  
1020 C CD1 . TYR A 129 ? 0.78276 0.89851 0.78373 -0.07464 0.01681  0.05355  133 TYR A CD1 
1021 C CD2 . TYR A 129 ? 0.83774 0.96186 0.83593 -0.07463 0.01018  0.03892  133 TYR A CD2 
1022 C CE1 . TYR A 129 ? 0.81232 0.93183 0.82269 -0.07850 0.03120  0.04241  133 TYR A CE1 
1023 C CE2 . TYR A 129 ? 0.84174 0.96609 0.84774 -0.07638 0.02352  0.02803  133 TYR A CE2 
1024 C CZ  . TYR A 129 ? 0.82680 0.95153 0.84080 -0.07808 0.03413  0.02922  133 TYR A CZ  
1025 O OH  . TYR A 129 ? 0.79994 0.93053 0.82783 -0.07943 0.04758  0.01592  133 TYR A OH  
1026 N N   . GLN A 130 ? 0.72883 0.86704 0.76488 -0.06198 -0.01465 0.04692  134 GLN A N   
1027 C CA  . GLN A 130 ? 0.74592 0.88129 0.79354 -0.06192 -0.01225 0.03946  134 GLN A CA  
1028 C C   . GLN A 130 ? 0.72268 0.85923 0.78661 -0.05664 -0.01464 0.04283  134 GLN A C   
1029 O O   . GLN A 130 ? 0.71718 0.84644 0.78967 -0.05366 -0.01178 0.03976  134 GLN A O   
1030 C CB  . GLN A 130 ? 0.73186 0.86912 0.77278 -0.06812 -0.01647 0.03377  134 GLN A CB  
1031 C CG  . GLN A 130 ? 0.70296 0.83677 0.72586 -0.07375 -0.01408 0.02755  134 GLN A CG  
1032 C CD  . GLN A 130 ? 0.84614 0.97973 0.86362 -0.08116 -0.01865 0.02046  134 GLN A CD  
1033 O OE1 . GLN A 130 ? 0.90733 1.03035 0.92936 -0.08282 -0.01696 0.01499  134 GLN A OE1 
1034 N NE2 . GLN A 130 ? 0.76436 0.90783 0.77110 -0.08604 -0.02583 0.02065  134 GLN A NE2 
1035 N N   . MET A 131 ? 0.64822 0.79425 0.71663 -0.05453 -0.02062 0.04807  135 MET A N   
1036 C CA  . MET A 131 ? 0.67998 0.82816 0.76207 -0.04979 -0.02167 0.04980  135 MET A CA  
1037 C C   . MET A 131 ? 0.73099 0.87089 0.81911 -0.04454 -0.01832 0.05238  135 MET A C   
1038 O O   . MET A 131 ? 0.69184 0.82694 0.78766 -0.04207 -0.01738 0.05019  135 MET A O   
1039 C CB  . MET A 131 ? 0.73271 0.89523 0.82141 -0.04672 -0.02820 0.05272  135 MET A CB  
1040 C CG  . MET A 131 ? 0.73269 0.90213 0.83525 -0.04379 -0.02780 0.05084  135 MET A CG  
1041 S SD  . MET A 131 ? 0.94597 1.13728 1.06298 -0.03735 -0.03597 0.05077  135 MET A SD  
1042 C CE  . MET A 131 ? 0.58726 0.79086 0.69741 -0.04368 -0.04306 0.04873  135 MET A CE  
1043 N N   . LEU A 132 ? 0.68093 0.81759 0.76355 -0.04407 -0.01676 0.05693  136 LEU A N   
1044 C CA  . LEU A 132 ? 0.69944 0.82876 0.78921 -0.04194 -0.01245 0.05847  136 LEU A CA  
1045 C C   . LEU A 132 ? 0.69047 0.81728 0.78703 -0.04365 -0.00634 0.05071  136 LEU A C   
1046 O O   . LEU A 132 ? 0.69883 0.82345 0.80858 -0.04070 -0.00578 0.04818  136 LEU A O   
1047 C CB  . LEU A 132 ? 0.71543 0.83805 0.79335 -0.04413 -0.01078 0.06580  136 LEU A CB  
1048 C CG  . LEU A 132 ? 0.76408 0.88397 0.83804 -0.03858 -0.01976 0.07418  136 LEU A CG  
1049 C CD1 . LEU A 132 ? 0.75637 0.86330 0.80789 -0.04216 -0.02015 0.08302  136 LEU A CD1 
1050 C CD2 . LEU A 132 ? 0.69082 0.80643 0.78013 -0.03226 -0.02148 0.07486  136 LEU A CD2 
1051 N N   . CYS A 133 ? 0.76185 0.88929 0.85090 -0.04746 -0.00297 0.04537  137 CYS A N   
1052 C CA  . CYS A 133 ? 0.69592 0.82170 0.79480 -0.04633 0.00118  0.03573  137 CYS A CA  
1053 C C   . CYS A 133 ? 0.66959 0.78978 0.77626 -0.04101 -0.00591 0.03287  137 CYS A C   
1054 O O   . CYS A 133 ? 0.68044 0.79827 0.80028 -0.03633 -0.00696 0.02690  137 CYS A O   
1055 C CB  . CYS A 133 ? 0.62732 0.75284 0.71539 -0.05036 0.00558  0.02901  137 CYS A CB  
1056 S SG  . CYS A 133 ? 1.00577 1.13468 1.07988 -0.05812 0.01686  0.02917  137 CYS A SG  
1057 N N   . GLY A 134 ? 0.68177 0.79955 0.77938 -0.04238 -0.01107 0.03629  138 GLY A N   
1058 C CA  . GLY A 134 ? 0.66929 0.77763 0.76701 -0.03981 -0.01656 0.03527  138 GLY A CA  
1059 C C   . GLY A 134 ? 0.66484 0.77347 0.77215 -0.03490 -0.01897 0.03732  138 GLY A C   
1060 O O   . GLY A 134 ? 0.70638 0.80620 0.81736 -0.03041 -0.02370 0.03389  138 GLY A O   
1061 N N   . ILE A 135 ? 0.61602 0.73296 0.72691 -0.03495 -0.01720 0.04230  139 ILE A N   
1062 C CA  . ILE A 135 ? 0.59439 0.71023 0.71355 -0.03085 -0.01931 0.04328  139 ILE A CA  
1063 C C   . ILE A 135 ? 0.63543 0.75031 0.76807 -0.02880 -0.01841 0.03885  139 ILE A C   
1064 O O   . ILE A 135 ? 0.63633 0.74682 0.77565 -0.02496 -0.02353 0.03502  139 ILE A O   
1065 C CB  . ILE A 135 ? 0.70692 0.82884 0.82673 -0.03028 -0.01849 0.04891  139 ILE A CB  
1066 C CG1 . ILE A 135 ? 0.74077 0.86853 0.85550 -0.03082 -0.02024 0.04944  139 ILE A CG1 
1067 C CG2 . ILE A 135 ? 0.73527 0.85326 0.86427 -0.02666 -0.01945 0.04890  139 ILE A CG2 
1068 C CD1 . ILE A 135 ? 0.81158 0.94864 0.92911 -0.02856 -0.02162 0.05321  139 ILE A CD1 
1069 N N   . LYS A 136 ? 0.61696 0.73689 0.75350 -0.03228 -0.01175 0.03812  140 LYS A N   
1070 C CA  . LYS A 136 ? 0.64076 0.76461 0.79453 -0.03249 -0.00848 0.03158  140 LYS A CA  
1071 C C   . LYS A 136 ? 0.66039 0.78308 0.82411 -0.02650 -0.01493 0.02246  140 LYS A C   
1072 O O   . LYS A 136 ? 0.62030 0.74565 0.80082 -0.02314 -0.01920 0.01647  140 LYS A O   
1073 C CB  . LYS A 136 ? 0.59704 0.72686 0.75023 -0.03934 0.00255  0.03052  140 LYS A CB  
1074 C CG  . LYS A 136 ? 0.62863 0.76667 0.80364 -0.04192 0.00847  0.02221  140 LYS A CG  
1075 C CD  . LYS A 136 ? 0.77716 0.91994 0.94881 -0.05228 0.02288  0.02199  140 LYS A CD  
1076 C CE  . LYS A 136 ? 0.76534 0.92093 0.96475 -0.05675 0.03046  0.01093  140 LYS A CE  
1077 N NZ  . LYS A 136 ? 0.79142 0.96015 1.01497 -0.04810 0.02613  -0.00439 140 LYS A NZ  
1078 N N   . HIS A 137 ? 0.58680 0.70351 0.73976 -0.02474 -0.01758 0.02104  141 HIS A N   
1079 C CA  . HIS A 137 ? 0.65567 0.76491 0.81448 -0.01723 -0.02648 0.01333  141 HIS A CA  
1080 C C   . HIS A 137 ? 0.64984 0.74878 0.80446 -0.01268 -0.03771 0.01565  141 HIS A C   
1081 O O   . HIS A 137 ? 0.70918 0.80783 0.87772 -0.00599 -0.04625 0.00880  141 HIS A O   
1082 C CB  . HIS A 137 ? 0.66660 0.76447 0.80941 -0.01745 -0.02770 0.01285  141 HIS A CB  
1083 C CG  . HIS A 137 ? 0.68038 0.76280 0.82375 -0.00869 -0.03905 0.00655  141 HIS A CG  
1084 N ND1 . HIS A 137 ? 0.70051 0.78774 0.86358 -0.00114 -0.04041 -0.00563 141 HIS A ND1 
1085 C CD2 . HIS A 137 ? 0.61096 0.67083 0.73547 -0.00616 -0.04997 0.01064  141 HIS A CD2 
1086 C CE1 . HIS A 137 ? 0.72293 0.78993 0.88059 0.00798  -0.05430 -0.00854 141 HIS A CE1 
1087 N NE2 . HIS A 137 ? 0.73618 0.78389 0.86730 0.00415  -0.06022 0.00234  141 HIS A NE2 
1088 N N   . LEU A 138 ? 0.63456 0.72707 0.77099 -0.01642 -0.03772 0.02401  142 LEU A N   
1089 C CA  . LEU A 138 ? 0.60358 0.68631 0.73214 -0.01365 -0.04603 0.02533  142 LEU A CA  
1090 C C   . LEU A 138 ? 0.75130 0.84291 0.89819 -0.01160 -0.04738 0.02165  142 LEU A C   
1091 O O   . LEU A 138 ? 0.66543 0.75074 0.81414 -0.00671 -0.05777 0.01741  142 LEU A O   
1092 C CB  . LEU A 138 ? 0.66046 0.74029 0.77042 -0.01916 -0.04194 0.03232  142 LEU A CB  
1093 C CG  . LEU A 138 ? 0.66393 0.73434 0.75472 -0.02427 -0.04049 0.03544  142 LEU A CG  
1094 C CD1 . LEU A 138 ? 0.62482 0.70053 0.70573 -0.03022 -0.03473 0.03944  142 LEU A CD1 
1095 C CD2 . LEU A 138 ? 0.61433 0.66174 0.68994 -0.02104 -0.05076 0.03410  142 LEU A CD2 
1096 N N   . HIS A 139 ? 0.62433 0.72773 0.78178 -0.01610 -0.03792 0.02364  143 HIS A N   
1097 C CA  . HIS A 139 ? 0.69128 0.79988 0.86480 -0.01669 -0.03794 0.02044  143 HIS A CA  
1098 C C   . HIS A 139 ? 0.74566 0.86358 0.94345 -0.01479 -0.04072 0.01019  143 HIS A C   
1099 O O   . HIS A 139 ? 0.57439 0.69524 0.78652 -0.01413 -0.04597 0.00442  143 HIS A O   
1100 C CB  . HIS A 139 ? 0.64982 0.76240 0.82394 -0.02259 -0.02780 0.02656  143 HIS A CB  
1101 C CG  . HIS A 139 ? 0.71367 0.82063 0.87229 -0.02172 -0.02782 0.03344  143 HIS A CG  
1102 N ND1 . HIS A 139 ? 0.74497 0.85185 0.90094 -0.02385 -0.02268 0.03983  143 HIS A ND1 
1103 C CD2 . HIS A 139 ? 0.72375 0.82560 0.86923 -0.01887 -0.03221 0.03388  143 HIS A CD2 
1104 C CE1 . HIS A 139 ? 0.70841 0.81386 0.85567 -0.02050 -0.02470 0.04226  143 HIS A CE1 
1105 N NE2 . HIS A 139 ? 0.75225 0.85596 0.89306 -0.01873 -0.02872 0.03834  143 HIS A NE2 
1106 N N   . SER A 140 ? 0.71837 0.84263 0.92331 -0.01375 -0.03753 0.00582  144 SER A N   
1107 C CA  . SER A 140 ? 0.68509 0.82386 0.91961 -0.01122 -0.03884 -0.00702 144 SER A CA  
1108 C C   . SER A 140 ? 0.56033 0.69437 0.80250 -0.00065 -0.05715 -0.01459 144 SER A C   
1109 O O   . SER A 140 ? 0.70832 0.85766 0.98049 0.00290  -0.06145 -0.02716 144 SER A O   
1110 C CB  . SER A 140 ? 0.69870 0.84552 0.93895 -0.01136 -0.03036 -0.01214 144 SER A CB  
1111 O OG  . SER A 140 ? 0.67483 0.80648 0.89677 -0.00435 -0.03839 -0.01013 144 SER A OG  
1112 N N   . ALA A 141 ? 0.71656 0.83001 0.93177 0.00398  -0.06830 -0.00786 145 ALA A N   
1113 C CA  . ALA A 141 ? 0.65664 0.75994 0.87002 0.01288  -0.08749 -0.01268 145 ALA A CA  
1114 C C   . ALA A 141 ? 0.71390 0.80672 0.90873 0.00977  -0.09148 -0.00755 145 ALA A C   
1115 O O   . ALA A 141 ? 0.78260 0.85989 0.96143 0.01567  -0.10723 -0.00846 145 ALA A O   
1116 C CB  . ALA A 141 ? 0.72411 0.80556 0.91556 0.02106  -0.09915 -0.01029 145 ALA A CB  
1117 N N   . GLY A 142 ? 0.67443 0.77286 0.86833 0.00124  -0.07830 -0.00252 146 GLY A N   
1118 C CA  . GLY A 142 ? 0.71245 0.80212 0.89208 -0.00079 -0.08079 -0.00038 146 GLY A CA  
1119 C C   . GLY A 142 ? 0.82995 0.90364 0.97529 -0.00195 -0.07868 0.00829  146 GLY A C   
1120 O O   . GLY A 142 ? 0.85510 0.92238 0.98754 -0.00342 -0.07888 0.00846  146 GLY A O   
1121 N N   . ILE A 143 ? 0.71598 0.78387 0.84733 -0.00233 -0.07564 0.01389  147 ILE A N   
1122 C CA  . ILE A 143 ? 0.73571 0.79145 0.83732 -0.00633 -0.07137 0.02095  147 ILE A CA  
1123 C C   . ILE A 143 ? 0.73327 0.80149 0.83960 -0.01149 -0.05749 0.02471  147 ILE A C   
1124 O O   . ILE A 143 ? 0.67067 0.75052 0.79110 -0.01333 -0.05001 0.02690  147 ILE A O   
1125 C CB  . ILE A 143 ? 0.78139 0.82608 0.86874 -0.00680 -0.07259 0.02483  147 ILE A CB  
1126 C CG1 . ILE A 143 ? 0.87142 0.89894 0.95257 0.00122  -0.08979 0.02118  147 ILE A CG1 
1127 C CG2 . ILE A 143 ? 0.59985 0.63546 0.65995 -0.01438 -0.06543 0.03110  147 ILE A CG2 
1128 C CD1 . ILE A 143 ? 0.70462 0.72211 0.78265 0.00377  -0.09245 0.02204  147 ILE A CD1 
1129 N N   . ILE A 144 ? 0.71466 0.77974 0.80795 -0.01320 -0.05467 0.02475  148 ILE A N   
1130 C CA  . ILE A 144 ? 0.73871 0.81493 0.83624 -0.01559 -0.04376 0.02702  148 ILE A CA  
1131 C C   . ILE A 144 ? 0.75927 0.83380 0.83648 -0.02085 -0.03789 0.02958  148 ILE A C   
1132 O O   . ILE A 144 ? 0.81450 0.87736 0.86969 -0.02334 -0.03919 0.02774  148 ILE A O   
1133 C CB  . ILE A 144 ? 0.72990 0.80660 0.83344 -0.01290 -0.04346 0.02203  148 ILE A CB  
1134 C CG1 . ILE A 144 ? 0.64756 0.72408 0.77044 -0.01081 -0.04900 0.01846  148 ILE A CG1 
1135 C CG2 . ILE A 144 ? 0.70744 0.79476 0.81957 -0.01212 -0.03486 0.02369  148 ILE A CG2 
1136 C CD1 . ILE A 144 ? 0.61492 0.68671 0.74058 -0.00903 -0.05017 0.01221  148 ILE A CD1 
1137 N N   . HIS A 145 ? 0.76129 0.84743 0.84450 -0.02399 -0.03105 0.03325  149 HIS A N   
1138 C CA  . HIS A 145 ? 0.71510 0.80251 0.78298 -0.03165 -0.02469 0.03456  149 HIS A CA  
1139 C C   . HIS A 145 ? 0.74572 0.84109 0.80926 -0.03371 -0.01708 0.02975  149 HIS A C   
1140 O O   . HIS A 145 ? 0.70371 0.79170 0.74546 -0.04163 -0.01238 0.02858  149 HIS A O   
1141 C CB  . HIS A 145 ? 0.71893 0.82015 0.79803 -0.03432 -0.02075 0.03761  149 HIS A CB  
1142 C CG  . HIS A 145 ? 0.75472 0.85714 0.82079 -0.04439 -0.01507 0.03811  149 HIS A CG  
1143 N ND1 . HIS A 145 ? 0.75727 0.87058 0.82017 -0.05020 -0.00667 0.03427  149 HIS A ND1 
1144 C CD2 . HIS A 145 ? 0.74858 0.84334 0.80547 -0.05089 -0.01554 0.04065  149 HIS A CD2 
1145 C CE1 . HIS A 145 ? 0.76518 0.87805 0.81755 -0.06162 -0.00171 0.03495  149 HIS A CE1 
1146 N NE2 . HIS A 145 ? 0.80552 0.90509 0.85283 -0.06209 -0.00769 0.03924  149 HIS A NE2 
1147 N N   . ARG A 146 ? 0.71276 0.82228 0.79605 -0.02719 -0.01490 0.02645  150 ARG A N   
1148 C CA  . ARG A 146 ? 0.68826 0.80918 0.77553 -0.02562 -0.00770 0.01890  150 ARG A CA  
1149 C C   . ARG A 146 ? 0.77930 0.91962 0.86954 -0.03235 0.00224  0.01583  150 ARG A C   
1150 O O   . ARG A 146 ? 0.87810 1.03237 0.97531 -0.03095 0.00987  0.00695  150 ARG A O   
1151 C CB  . ARG A 146 ? 0.66751 0.77439 0.73393 -0.02731 -0.00686 0.01308  150 ARG A CB  
1152 C CG  . ARG A 146 ? 0.77570 0.86551 0.84023 -0.02160 -0.01789 0.01332  150 ARG A CG  
1153 C CD  . ARG A 146 ? 0.76066 0.83024 0.79393 -0.02643 -0.02208 0.01219  150 ARG A CD  
1154 N NE  . ARG A 146 ? 0.72255 0.78691 0.74566 -0.02456 -0.02096 0.00312  150 ARG A NE  
1155 C CZ  . ARG A 146 ? 0.82701 0.87559 0.81622 -0.03051 -0.02056 0.00033  150 ARG A CZ  
1156 N NH1 . ARG A 146 ? 0.77683 0.81116 0.73816 -0.03903 -0.02098 0.00704  150 ARG A NH1 
1157 N NH2 . ARG A 146 ? 0.95527 0.99895 0.93504 -0.02838 -0.02001 -0.00941 150 ARG A NH2 
1158 N N   . ASP A 147 ? 0.75190 0.89504 0.83887 -0.04007 0.00302  0.02080  151 ASP A N   
1159 C CA  . ASP A 147 ? 0.71636 0.87948 0.80731 -0.04937 0.01299  0.01617  151 ASP A CA  
1160 C C   . ASP A 147 ? 0.68391 0.86022 0.78908 -0.05096 0.00967  0.01992  151 ASP A C   
1161 O O   . ASP A 147 ? 0.67483 0.85841 0.77576 -0.06308 0.01536  0.01871  151 ASP A O   
1162 C CB  . ASP A 147 ? 0.78577 0.93397 0.84644 -0.06446 0.02076  0.01616  151 ASP A CB  
1163 C CG  . ASP A 147 ? 0.93313 1.10501 0.99882 -0.07528 0.03616  0.00653  151 ASP A CG  
1164 O OD1 . ASP A 147 ? 0.92051 1.11840 1.01271 -0.06683 0.03978  -0.00271 151 ASP A OD1 
1165 O OD2 . ASP A 147 ? 0.96190 1.12620 1.00621 -0.09228 0.04484  0.00734  151 ASP A OD2 
1166 N N   . LEU A 148 ? 0.52115 0.69859 0.64025 -0.04053 0.00071  0.02440  152 LEU A N   
1167 C CA  . LEU A 148 ? 0.58672 0.77713 0.71637 -0.04166 -0.00310 0.02703  152 LEU A CA  
1168 C C   . LEU A 148 ? 0.74450 0.96576 0.89689 -0.03989 -0.00082 0.01927  152 LEU A C   
1169 O O   . LEU A 148 ? 0.67203 0.90357 0.83977 -0.02969 -0.00099 0.01393  152 LEU A O   
1170 C CB  . LEU A 148 ? 0.58872 0.77058 0.72243 -0.03241 -0.01194 0.03387  152 LEU A CB  
1171 C CG  . LEU A 148 ? 0.73631 0.89559 0.85461 -0.03504 -0.01388 0.03895  152 LEU A CG  
1172 C CD1 . LEU A 148 ? 0.79004 0.94223 0.91462 -0.02664 -0.01884 0.04331  152 LEU A CD1 
1173 C CD2 . LEU A 148 ? 0.74882 0.90538 0.85761 -0.04392 -0.01380 0.04062  152 LEU A CD2 
1174 N N   . LYS A 149 ? 0.70217 0.93835 0.85856 -0.04933 0.00035  0.01735  153 LYS A N   
1175 C CA  . LYS A 149 ? 0.69475 0.96529 0.87610 -0.05037 0.00176  0.00796  153 LYS A CA  
1176 C C   . LYS A 149 ? 0.70384 0.98052 0.88149 -0.06392 0.00099  0.00833  153 LYS A C   
1177 O O   . LYS A 149 ? 0.68444 0.93687 0.83812 -0.07387 0.00330  0.01405  153 LYS A O   
1178 C CB  . LYS A 149 ? 0.61105 0.89776 0.79992 -0.05606 0.01542  -0.00345 153 LYS A CB  
1179 C CG  . LYS A 149 ? 0.61199 0.88530 0.77597 -0.07592 0.02781  -0.00335 153 LYS A CG  
1180 C CD  . LYS A 149 ? 0.63515 0.92038 0.79959 -0.08293 0.04346  -0.01412 153 LYS A CD  
1181 C CE  . LYS A 149 ? 0.78430 1.05332 0.94068 -0.06995 0.04230  -0.01364 153 LYS A CE  
1182 N NZ  . LYS A 149 ? 0.84883 1.11124 0.98365 -0.08243 0.05810  -0.01981 153 LYS A NZ  
1183 N N   . PRO A 150 ? 0.65959 0.96709 0.86108 -0.06342 -0.00411 0.00160  154 PRO A N   
1184 C CA  . PRO A 150 ? 0.68722 0.99921 0.88465 -0.07608 -0.00715 0.00135  154 PRO A CA  
1185 C C   . PRO A 150 ? 0.66269 0.96712 0.84531 -0.09797 0.00614  -0.00177 154 PRO A C   
1186 O O   . PRO A 150 ? 0.65208 0.94203 0.81916 -0.10841 0.00394  0.00132  154 PRO A O   
1187 C CB  . PRO A 150 ? 0.72049 1.07269 0.95151 -0.07053 -0.01570 -0.00839 154 PRO A CB  
1188 C CG  . PRO A 150 ? 0.63275 0.98857 0.87782 -0.04927 -0.02323 -0.00740 154 PRO A CG  
1189 C CD  . PRO A 150 ? 0.65913 0.99779 0.89310 -0.04969 -0.01007 -0.00682 154 PRO A CD  
1190 N N   . SER A 151 ? 0.57279 0.88430 0.75721 -0.10620 0.02023  -0.00820 155 SER A N   
1191 C CA  . SER A 151 ? 0.65906 0.95514 0.82141 -0.12894 0.03296  -0.00878 155 SER A CA  
1192 C C   . SER A 151 ? 0.73012 0.97777 0.85368 -0.12978 0.03153  0.00358  155 SER A C   
1193 O O   . SER A 151 ? 0.75784 0.98244 0.85660 -0.14703 0.03856  0.00573  155 SER A O   
1194 C CB  . SER A 151 ? 0.68229 0.99758 0.85222 -0.13976 0.05039  -0.01913 155 SER A CB  
1195 O OG  . SER A 151 ? 0.76303 1.05959 0.91724 -0.13051 0.05425  -0.01556 155 SER A OG  
1196 N N   . ASN A 152 ? 0.67313 0.90435 0.79166 -0.11187 0.02201  0.01115  156 ASN A N   
1197 C CA  . ASN A 152 ? 0.69692 0.88765 0.78591 -0.10966 0.01842  0.02060  156 ASN A CA  
1198 C C   . ASN A 152 ? 0.71585 0.89478 0.80275 -0.10247 0.00736  0.02581  156 ASN A C   
1199 O O   . ASN A 152 ? 0.66399 0.81578 0.73522 -0.09625 0.00279  0.03163  156 ASN A O   
1200 C CB  . ASN A 152 ? 0.70343 0.88452 0.78834 -0.09709 0.01780  0.02299  156 ASN A CB  
1201 C CG  . ASN A 152 ? 0.75331 0.92994 0.82357 -0.10696 0.02959  0.01937  156 ASN A CG  
1202 O OD1 . ASN A 152 ? 0.82695 1.00093 0.88464 -0.12495 0.03895  0.01718  156 ASN A OD1 
1203 N ND2 . ASN A 152 ? 0.80547 0.97947 0.87466 -0.09696 0.03004  0.01826  156 ASN A ND2 
1204 N N   . ILE A 153 ? 0.69463 0.89488 0.79755 -0.10280 0.00270  0.02258  157 ILE A N   
1205 C CA  . ILE A 153 ? 0.64894 0.83851 0.74590 -0.09880 -0.00568 0.02587  157 ILE A CA  
1206 C C   . ILE A 153 ? 0.73959 0.93348 0.83389 -0.11416 -0.00500 0.02063  157 ILE A C   
1207 O O   . ILE A 153 ? 0.71867 0.94066 0.83006 -0.12220 -0.00275 0.01364  157 ILE A O   
1208 C CB  . ILE A 153 ? 0.66462 0.87100 0.77685 -0.08441 -0.01409 0.02769  157 ILE A CB  
1209 C CG1 . ILE A 153 ? 0.74663 0.94012 0.85722 -0.07122 -0.01499 0.03340  157 ILE A CG1 
1210 C CG2 . ILE A 153 ? 0.66427 0.86552 0.76855 -0.08482 -0.02062 0.02872  157 ILE A CG2 
1211 C CD1 . ILE A 153 ? 0.74183 0.94992 0.86723 -0.06467 -0.01283 0.03122  157 ILE A CD1 
1212 N N   . VAL A 154 ? 0.68281 0.85014 0.75810 -0.11842 -0.00698 0.02220  158 VAL A N   
1213 C CA  . VAL A 154 ? 0.71945 0.88712 0.79053 -0.13404 -0.00667 0.01625  158 VAL A CA  
1214 C C   . VAL A 154 ? 0.71523 0.87893 0.78189 -0.12865 -0.01476 0.01506  158 VAL A C   
1215 O O   . VAL A 154 ? 0.68780 0.83954 0.74890 -0.11565 -0.01773 0.01934  158 VAL A O   
1216 C CB  . VAL A 154 ? 0.75044 0.88483 0.79815 -0.14858 -0.00032 0.01704  158 VAL A CB  
1217 C CG1 . VAL A 154 ? 0.69258 0.83844 0.74359 -0.16192 0.01027  0.01513  158 VAL A CG1 
1218 C CG2 . VAL A 154 ? 0.65282 0.75065 0.68110 -0.13700 -0.00332 0.02400  158 VAL A CG2 
1219 N N   . VAL A 155 ? 0.66020 0.83527 0.72924 -0.14030 -0.01752 0.00783  159 VAL A N   
1220 C CA  . VAL A 155 ? 0.67445 0.84900 0.73701 -0.13715 -0.02516 0.00484  159 VAL A CA  
1221 C C   . VAL A 155 ? 0.78003 0.94045 0.83065 -0.15390 -0.02473 -0.00326 159 VAL A C   
1222 O O   . VAL A 155 ? 0.75335 0.91257 0.80559 -0.16990 -0.01942 -0.00678 159 VAL A O   
1223 C CB  . VAL A 155 ? 0.79865 1.00789 0.87796 -0.13074 -0.03418 0.00353  159 VAL A CB  
1224 C CG1 . VAL A 155 ? 0.62738 0.84276 0.71477 -0.11349 -0.03530 0.01200  159 VAL A CG1 
1225 C CG2 . VAL A 155 ? 0.69613 0.93658 0.79710 -0.14267 -0.03503 -0.00446 159 VAL A CG2 
1226 N N   . LYS A 156 ? 0.78357 0.93154 0.82052 -0.15135 -0.02923 -0.00694 160 LYS A N   
1227 C CA  . LYS A 156 ? 0.81944 0.95389 0.84439 -0.16582 -0.03060 -0.01655 160 LYS A CA  
1228 C C   . LYS A 156 ? 0.85604 1.01391 0.88266 -0.16636 -0.04007 -0.02305 160 LYS A C   
1229 O O   . LYS A 156 ? 0.86811 1.03969 0.89572 -0.15303 -0.04502 -0.01848 160 LYS A O   
1230 C CB  . LYS A 156 ? 0.82896 0.92297 0.83284 -0.16214 -0.02784 -0.01820 160 LYS A CB  
1231 C CG  . LYS A 156 ? 0.93279 0.99505 0.92699 -0.17089 -0.02265 -0.01625 160 LYS A CG  
1232 C CD  . LYS A 156 ? 1.04937 1.07118 1.02575 -0.16336 -0.02300 -0.01873 160 LYS A CD  
1233 C CE  . LYS A 156 ? 1.05689 1.06389 1.02097 -0.17323 -0.02554 -0.03108 160 LYS A CE  
1234 N NZ  . LYS A 156 ? 1.22564 1.18483 1.17245 -0.16966 -0.02572 -0.03361 160 LYS A NZ  
1235 N N   . SER A 157 ? 0.81192 0.97108 0.83577 -0.18288 -0.04322 -0.03368 161 SER A N   
1236 C CA  . SER A 157 ? 0.85492 1.03615 0.87816 -0.18487 -0.05474 -0.04123 161 SER A CA  
1237 C C   . SER A 157 ? 0.86127 1.02388 0.85921 -0.17581 -0.05686 -0.04293 161 SER A C   
1238 O O   . SER A 157 ? 0.89654 1.07285 0.88608 -0.17678 -0.06695 -0.04837 161 SER A O   
1239 C CB  . SER A 157 ? 0.88309 1.07122 0.91166 -0.20699 -0.05751 -0.05401 161 SER A CB  
1240 O OG  . SER A 157 ? 0.94939 1.10033 0.96451 -0.21895 -0.04782 -0.05646 161 SER A OG  
1241 N N   . ASP A 158 ? 0.87745 1.01044 0.86292 -0.16723 -0.04786 -0.03960 162 ASP A N   
1242 C CA  . ASP A 158 ? 0.87305 0.99466 0.83924 -0.15707 -0.04642 -0.04136 162 ASP A CA  
1243 C C   . ASP A 158 ? 0.92419 1.05875 0.89450 -0.14195 -0.04559 -0.02943 162 ASP A C   
1244 O O   . ASP A 158 ? 1.00376 1.12853 0.95988 -0.13406 -0.04055 -0.02941 162 ASP A O   
1245 C CB  . ASP A 158 ? 0.93563 1.02164 0.89076 -0.15473 -0.03750 -0.04730 162 ASP A CB  
1246 C CG  . ASP A 158 ? 1.02479 1.09729 0.99151 -0.14528 -0.03097 -0.03802 162 ASP A CG  
1247 O OD1 . ASP A 158 ? 0.98091 1.07000 0.96277 -0.14217 -0.03140 -0.02735 162 ASP A OD1 
1248 O OD2 . ASP A 158 ? 1.10716 1.15133 1.06757 -0.14011 -0.02642 -0.04270 162 ASP A OD2 
1249 N N   . CYS A 159 ? 0.83525 0.99057 0.82532 -0.13865 -0.04906 -0.02044 163 CYS A N   
1250 C CA  . CYS A 159 ? 0.88271 1.04919 0.87838 -0.12521 -0.04995 -0.00890 163 CYS A CA  
1251 C C   . CYS A 159 ? 0.91305 1.06289 0.91232 -0.11558 -0.03924 -0.00262 163 CYS A C   
1252 O O   . CYS A 159 ? 0.81412 0.96557 0.81120 -0.10586 -0.03758 0.00477  163 CYS A O   
1253 C CB  . CYS A 159 ? 0.90524 1.07515 0.87993 -0.12130 -0.05613 -0.00769 163 CYS A CB  
1254 S SG  . CYS A 159 ? 0.94087 1.13008 0.92303 -0.10969 -0.06644 0.00548  163 CYS A SG  
1255 N N   . THR A 160 ? 0.89373 1.02584 0.89716 -0.11828 -0.03296 -0.00528 164 THR A N   
1256 C CA  . THR A 160 ? 0.80164 0.92177 0.81205 -0.10833 -0.02652 0.00064  164 THR A CA  
1257 C C   . THR A 160 ? 0.87287 1.00333 0.89933 -0.10783 -0.02712 0.00794  164 THR A C   
1258 O O   . THR A 160 ? 0.72234 0.86526 0.75558 -0.11746 -0.02970 0.00611  164 THR A O   
1259 C CB  . THR A 160 ? 0.85851 0.95001 0.86210 -0.10851 -0.02204 -0.00594 164 THR A CB  
1260 O OG1 . THR A 160 ? 0.84529 0.92514 0.84542 -0.12076 -0.02384 -0.00948 164 THR A OG1 
1261 C CG2 . THR A 160 ? 0.84001 0.92318 0.83058 -0.10676 -0.01912 -0.01554 164 THR A CG2 
1262 N N   . LEU A 161 ? 0.74072 0.86746 0.77424 -0.09731 -0.02387 0.01463  165 LEU A N   
1263 C CA  . LEU A 161 ? 0.67003 0.80663 0.71693 -0.09482 -0.02360 0.02090  165 LEU A CA  
1264 C C   . LEU A 161 ? 0.69656 0.81342 0.74311 -0.08844 -0.01997 0.02372  165 LEU A C   
1265 O O   . LEU A 161 ? 0.73949 0.84517 0.78391 -0.08085 -0.01862 0.02261  165 LEU A O   
1266 C CB  . LEU A 161 ? 0.66406 0.82188 0.72050 -0.08680 -0.02742 0.02652  165 LEU A CB  
1267 C CG  . LEU A 161 ? 0.71417 0.88282 0.78555 -0.07933 -0.02747 0.03228  165 LEU A CG  
1268 C CD1 . LEU A 161 ? 0.73341 0.92131 0.81176 -0.07325 -0.03499 0.03558  165 LEU A CD1 
1269 C CD2 . LEU A 161 ? 0.64460 0.79805 0.71559 -0.07084 -0.02338 0.03639  165 LEU A CD2 
1270 N N   . LYS A 162 ? 0.67005 0.78318 0.71827 -0.09213 -0.01844 0.02617  166 LYS A N   
1271 C CA  . LYS A 162 ? 0.71188 0.80439 0.75577 -0.08624 -0.01781 0.02917  166 LYS A CA  
1272 C C   . LYS A 162 ? 0.75177 0.85399 0.80157 -0.08618 -0.01567 0.03343  166 LYS A C   
1273 O O   . LYS A 162 ? 0.66647 0.78515 0.72100 -0.09486 -0.01279 0.03213  166 LYS A O   
1274 C CB  . LYS A 162 ? 0.75125 0.81308 0.77777 -0.09281 -0.01870 0.02675  166 LYS A CB  
1275 C CG  . LYS A 162 ? 0.79890 0.84722 0.81947 -0.09164 -0.02059 0.01985  166 LYS A CG  
1276 C CD  . LYS A 162 ? 0.84192 0.85463 0.84420 -0.09733 -0.02313 0.01760  166 LYS A CD  
1277 C CE  . LYS A 162 ? 0.94320 0.94502 0.94078 -0.09752 -0.02419 0.00824  166 LYS A CE  
1278 N NZ  . LYS A 162 ? 0.81086 0.81781 0.82000 -0.08191 -0.02445 0.00367  166 LYS A NZ  
1279 N N   . ILE A 163 ? 0.73567 0.82986 0.78707 -0.07645 -0.01688 0.03667  167 ILE A N   
1280 C CA  . ILE A 163 ? 0.70872 0.80825 0.76216 -0.07596 -0.01455 0.03917  167 ILE A CA  
1281 C C   . ILE A 163 ? 0.75805 0.83110 0.79013 -0.08271 -0.01404 0.04057  167 ILE A C   
1282 O O   . ILE A 163 ? 0.70834 0.75485 0.72737 -0.08041 -0.01929 0.04101  167 ILE A O   
1283 C CB  . ILE A 163 ? 0.69188 0.79578 0.75658 -0.06307 -0.01701 0.04120  167 ILE A CB  
1284 C CG1 . ILE A 163 ? 0.66353 0.78731 0.74294 -0.05818 -0.01739 0.04179  167 ILE A CG1 
1285 C CG2 . ILE A 163 ? 0.60526 0.71135 0.66950 -0.06213 -0.01487 0.04198  167 ILE A CG2 
1286 C CD1 . ILE A 163 ? 0.66947 0.79169 0.75722 -0.04856 -0.01889 0.04365  167 ILE A CD1 
1287 N N   . LEU A 164 ? 0.65795 0.73631 0.68471 -0.09100 -0.00785 0.04081  168 LEU A N   
1288 C CA  . LEU A 164 ? 0.80496 0.85352 0.80392 -0.09870 -0.00687 0.04378  168 LEU A CA  
1289 C C   . LEU A 164 ? 0.79439 0.84998 0.79036 -0.09837 -0.00182 0.04384  168 LEU A C   
1290 O O   . LEU A 164 ? 0.78133 0.86110 0.79854 -0.08913 -0.00105 0.04138  168 LEU A O   
1291 C CB  . LEU A 164 ? 0.85383 0.89138 0.83712 -0.11731 -0.00108 0.04299  168 LEU A CB  
1292 C CG  . LEU A 164 ? 0.88099 0.95270 0.88370 -0.12876 0.00720  0.03700  168 LEU A CG  
1293 C CD1 . LEU A 164 ? 0.80875 0.90355 0.81824 -0.13624 0.01818  0.03362  168 LEU A CD1 
1294 C CD2 . LEU A 164 ? 0.83799 0.89258 0.82640 -0.14537 0.00906  0.03550  168 LEU A CD2 
1295 N N   . ASP A 165 ? 0.90169 0.93142 0.86722 -0.10867 0.00125  0.04669  169 ASP A N   
1296 C CA  . ASP A 165 ? 0.96123 0.99153 0.91422 -0.11185 0.00782  0.04588  169 ASP A CA  
1297 C C   . ASP A 165 ? 0.91143 0.94095 0.86990 -0.09523 -0.00053 0.04587  169 ASP A C   
1298 O O   . ASP A 165 ? 0.86647 0.92464 0.85067 -0.08765 0.00262  0.04103  169 ASP A O   
1299 C CB  . ASP A 165 ? 0.78439 0.85214 0.75706 -0.12072 0.02255  0.03831  169 ASP A CB  
1300 C CG  . ASP A 165 ? 0.98927 1.05127 0.93927 -0.13036 0.03365  0.03603  169 ASP A CG  
1301 O OD1 . ASP A 165 ? 1.13261 1.15587 1.04383 -0.13411 0.02961  0.04248  169 ASP A OD1 
1302 O OD2 . ASP A 165 ? 0.94595 1.04042 0.91494 -0.13346 0.04564  0.02726  169 ASP A OD2 
1303 N N   . PHE A 166 ? 0.88085 0.87779 0.81777 -0.08864 -0.01284 0.05050  170 PHE A N   
1304 C CA  . PHE A 166 ? 0.88881 0.88413 0.83024 -0.07468 -0.02207 0.04918  170 PHE A CA  
1305 C C   . PHE A 166 ? 0.81793 0.79777 0.72887 -0.07975 -0.01983 0.04908  170 PHE A C   
1306 O O   . PHE A 166 ? 0.94339 0.91117 0.84771 -0.06978 -0.03123 0.04860  170 PHE A O   
1307 C CB  . PHE A 166 ? 0.81701 0.79199 0.75928 -0.06250 -0.03876 0.05139  170 PHE A CB  
1308 C CG  . PHE A 166 ? 0.83451 0.81984 0.79858 -0.06016 -0.03879 0.05052  170 PHE A CG  
1309 C CD1 . PHE A 166 ? 0.83656 0.85248 0.83445 -0.05351 -0.03555 0.04683  170 PHE A CD1 
1310 C CD2 . PHE A 166 ? 0.86969 0.83276 0.81710 -0.06670 -0.04052 0.05331  170 PHE A CD2 
1311 C CE1 . PHE A 166 ? 0.83699 0.86221 0.85022 -0.05298 -0.03429 0.04563  170 PHE A CE1 
1312 C CE2 . PHE A 166 ? 0.86203 0.83536 0.82804 -0.06544 -0.03942 0.05071  170 PHE A CE2 
1313 C CZ  . PHE A 166 ? 0.79171 0.79713 0.78979 -0.05875 -0.03601 0.04672  170 PHE A CZ  
1314 N N   . GLY A 167 ? 0.90784 0.89043 0.80138 -0.09566 -0.00468 0.04795  171 GLY A N   
1315 C CA  . GLY A 167 ? 0.80004 0.76670 0.65939 -0.10240 -0.00016 0.04700  171 GLY A CA  
1316 C C   . GLY A 167 ? 0.87129 0.85818 0.74797 -0.09142 0.00004  0.03898  171 GLY A C   
1317 O O   . GLY A 167 ? 1.04555 1.01360 0.89329 -0.09137 -0.00340 0.03793  171 GLY A O   
1318 N N   . LEU A 168 ? 0.82887 0.85064 0.74942 -0.08218 0.00300  0.03325  172 LEU A N   
1319 C CA  . LEU A 168 ? 0.79951 0.83544 0.73750 -0.07070 0.00127  0.02590  172 LEU A CA  
1320 C C   . LEU A 168 ? 0.86458 0.89544 0.82040 -0.05572 -0.01561 0.02788  172 LEU A C   
1321 O O   . LEU A 168 ? 0.84390 0.88382 0.81545 -0.04699 -0.01813 0.02204  172 LEU A O   
1322 C CB  . LEU A 168 ? 0.81584 0.88896 0.78914 -0.06862 0.01347  0.01797  172 LEU A CB  
1323 C CG  . LEU A 168 ? 0.92387 1.01379 0.89152 -0.08139 0.03240  0.01017  172 LEU A CG  
1324 C CD1 . LEU A 168 ? 0.86475 0.98005 0.85859 -0.07140 0.03835  -0.00203 172 LEU A CD1 
1325 C CD2 . LEU A 168 ? 0.85256 0.91406 0.77149 -0.09603 0.03803  0.01216  172 LEU A CD2 
1326 N N   . ALA A 169 ? 0.75339 0.77075 0.70894 -0.05308 -0.02632 0.03444  173 ALA A N   
1327 C CA  . ALA A 169 ? 0.84216 0.86374 0.82314 -0.04041 -0.03835 0.03370  173 ALA A CA  
1328 C C   . ALA A 169 ? 0.91098 0.91727 0.88033 -0.03396 -0.05080 0.03021  173 ALA A C   
1329 O O   . ALA A 169 ? 0.92833 0.91058 0.86186 -0.03788 -0.05583 0.03154  173 ALA A O   
1330 C CB  . ALA A 169 ? 0.80744 0.82090 0.79348 -0.03838 -0.04569 0.03855  173 ALA A CB  
1331 N N   . ARG A 170 ? 0.84371 0.86309 0.84179 -0.02527 -0.05583 0.02556  174 ARG A N   
1332 C CA  . ARG A 170 ? 0.88242 0.89349 0.87791 -0.01947 -0.06767 0.01969  174 ARG A CA  
1333 C C   . ARG A 170 ? 0.79642 0.81060 0.81719 -0.01152 -0.08065 0.01825  174 ARG A C   
1334 O O   . ARG A 170 ? 0.80736 0.83776 0.85596 -0.01037 -0.07528 0.01951  174 ARG A O   
1335 C CB  . ARG A 170 ? 0.80578 0.83095 0.81513 -0.01850 -0.05955 0.01263  174 ARG A CB  
1336 C CG  . ARG A 170 ? 0.87723 0.90468 0.90671 -0.01221 -0.06951 0.00601  174 ARG A CG  
1337 C CD  . ARG A 170 ? 0.92491 0.96181 0.96803 -0.01112 -0.06129 -0.00058 174 ARG A CD  
1338 N NE  . ARG A 170 ? 0.87699 0.91287 0.93803 -0.00761 -0.07094 -0.00742 174 ARG A NE  
1339 C CZ  . ARG A 170 ? 1.08378 1.10780 1.13214 -0.00643 -0.08471 -0.01372 174 ARG A CZ  
1340 N NH1 . ARG A 170 ? 1.17886 1.18690 1.19182 -0.00769 -0.09136 -0.01257 174 ARG A NH1 
1341 N NH2 . ARG A 170 ? 1.13159 1.15828 1.20164 -0.00485 -0.09285 -0.02128 174 ARG A NH2 
1342 N N   . THR A 171 ? 0.87011 0.86940 0.88061 -0.00634 -0.09784 0.01487  175 THR A N   
1343 C CA  . THR A 171 ? 0.87457 0.88282 0.91597 0.00155  -0.11010 0.00970  175 THR A CA  
1344 C C   . THR A 171 ? 0.93708 0.96158 1.00586 0.00219  -0.10947 0.00117  175 THR A C   
1345 O O   . THR A 171 ? 0.72115 0.74535 0.78166 -0.00137 -0.10247 -0.00099 175 THR A O   
1346 C CB  . THR A 171 ? 0.87692 0.86444 0.90090 0.00879  -0.13208 0.00816  175 THR A CB  
1347 O OG1 . THR A 171 ? 1.00979 0.97968 1.00149 0.00755  -0.14055 0.00605  175 THR A OG1 
1348 C CG2 . THR A 171 ? 0.96895 0.93651 0.96910 0.00852  -0.13367 0.01678  175 THR A CG2 
1349 N N   . ALA A 172 ? 0.85866 0.89722 0.96137 0.00618  -0.11620 -0.00504 176 ALA A N   
1350 C CA  . ALA A 172 ? 0.83652 0.88896 0.96616 0.00377  -0.11397 -0.01287 176 ALA A CA  
1351 C C   . ALA A 172 ? 0.86180 0.90364 0.97823 0.00540  -0.12820 -0.02118 176 ALA A C   
1352 O O   . ALA A 172 ? 0.97581 1.00215 1.06835 0.01033  -0.14451 -0.02221 176 ALA A O   
1353 C CB  . ALA A 172 ? 0.84055 0.91320 1.01100 0.00458  -0.11493 -0.01886 176 ALA A CB  
1354 N N   . GLY A 173 ? 0.81576 0.86282 0.94482 0.00105  -0.12268 -0.02696 177 GLY A N   
1355 C CA  . GLY A 173 ? 0.90475 0.94308 1.02407 0.00105  -0.13418 -0.03696 177 GLY A CA  
1356 C C   . GLY A 173 ? 0.87475 0.91501 1.00549 -0.00447 -0.12244 -0.04110 177 GLY A C   
1357 O O   . GLY A 173 ? 0.88718 0.93013 1.02177 -0.00680 -0.10598 -0.03425 177 GLY A O   
1358 N N   . THR A 174 ? 0.89163 0.92875 1.02777 -0.00604 -0.13292 -0.05315 178 THR A N   
1359 C CA  . THR A 174 ? 0.87612 0.90984 1.02262 -0.01116 -0.12434 -0.05897 178 THR A CA  
1360 C C   . THR A 174 ? 0.81748 0.83386 0.93003 -0.00953 -0.12323 -0.06388 178 THR A C   
1361 O O   . THR A 174 ? 0.86684 0.87611 0.98445 -0.01217 -0.12087 -0.07267 178 THR A O   
1362 C CB  . THR A 174 ? 0.86216 0.90392 1.04040 -0.01659 -0.13438 -0.07133 178 THR A CB  
1363 O OG1 . THR A 174 ? 0.87663 0.91392 1.04204 -0.01348 -0.15543 -0.08232 178 THR A OG1 
1364 C CG2 . THR A 174 ? 0.85429 0.91718 1.06896 -0.01959 -0.13196 -0.06879 178 THR A CG2 
1365 N N   . SER A 175 ? 0.87446 0.88234 0.95139 -0.00621 -0.12476 -0.05962 179 SER A N   
1366 C CA  . SER A 175 ? 0.81897 0.81240 0.86064 -0.00616 -0.12017 -0.06501 179 SER A CA  
1367 C C   . SER A 175 ? 0.93420 0.93164 0.96949 -0.00573 -0.09977 -0.05716 179 SER A C   
1368 O O   . SER A 175 ? 0.88131 0.88765 0.92301 -0.00552 -0.09362 -0.04547 179 SER A O   
1369 C CB  . SER A 175 ? 0.95834 0.93693 0.95846 -0.00536 -0.13436 -0.06605 179 SER A CB  
1370 O OG  . SER A 175 ? 1.08920 1.06044 1.08588 -0.00531 -0.15295 -0.07884 179 SER A OG  
1371 N N   . PHE A 176 ? 0.78723 0.77936 0.81217 -0.00519 -0.08989 -0.06563 180 PHE A N   
1372 C CA  . PHE A 176 ? 0.85620 0.85573 0.87847 -0.00370 -0.07161 -0.06214 180 PHE A CA  
1373 C C   . PHE A 176 ? 0.90634 0.90398 0.89402 -0.00750 -0.06715 -0.05647 180 PHE A C   
1374 O O   . PHE A 176 ? 0.90118 0.88404 0.85305 -0.01074 -0.07430 -0.06092 180 PHE A O   
1375 C CB  . PHE A 176 ? 0.80392 0.79864 0.82422 -0.00069 -0.06312 -0.07607 180 PHE A CB  
1376 C CG  . PHE A 176 ? 0.83563 0.84219 0.85650 0.00218  -0.04524 -0.07596 180 PHE A CG  
1377 C CD1 . PHE A 176 ? 0.85351 0.87279 0.90514 0.00686  -0.03873 -0.06794 180 PHE A CD1 
1378 C CD2 . PHE A 176 ? 0.86744 0.87393 0.85769 -0.00061 -0.03483 -0.08407 180 PHE A CD2 
1379 C CE1 . PHE A 176 ? 0.83891 0.87316 0.89590 0.01065  -0.02441 -0.06954 180 PHE A CE1 
1380 C CE2 . PHE A 176 ? 0.83075 0.85428 0.82813 0.00144  -0.01719 -0.08649 180 PHE A CE2 
1381 C CZ  . PHE A 176 ? 0.77289 0.81150 0.80588 0.00791  -0.01328 -0.07973 180 PHE A CZ  
1382 N N   . MET A 177 ? 0.86442 0.87481 0.86027 -0.00823 -0.05567 -0.04666 181 MET A N   
1383 C CA  . MET A 177 ? 0.92304 0.93189 0.88842 -0.01444 -0.04766 -0.04130 181 MET A CA  
1384 C C   . MET A 177 ? 0.90724 0.93409 0.88354 -0.01470 -0.02805 -0.04387 181 MET A C   
1385 O O   . MET A 177 ? 0.86634 0.90871 0.87415 -0.01079 -0.02416 -0.03824 181 MET A O   
1386 C CB  . MET A 177 ? 0.97420 0.98218 0.94026 -0.01648 -0.05432 -0.02745 181 MET A CB  
1387 C CG  . MET A 177 ? 1.03877 1.03193 0.99630 -0.01451 -0.07413 -0.02716 181 MET A CG  
1388 S SD  . MET A 177 ? 1.34975 1.32954 1.28739 -0.01621 -0.08548 -0.01457 181 MET A SD  
1389 C CE  . MET A 177 ? 1.47300 1.43321 1.39060 -0.01232 -0.10948 -0.02252 181 MET A CE  
1390 N N   . MET A 178 ? 0.88483 0.91053 0.83473 -0.01963 -0.01602 -0.05294 182 MET A N   
1391 C CA  . MET A 178 ? 0.86357 0.91140 0.82660 -0.02037 0.00338  -0.05812 182 MET A CA  
1392 C C   . MET A 178 ? 0.86272 0.92102 0.82791 -0.02728 0.00875  -0.04546 182 MET A C   
1393 O O   . MET A 178 ? 0.99474 1.03741 0.92862 -0.03652 0.00525  -0.03681 182 MET A O   
1394 C CB  . MET A 178 ? 0.89786 0.94286 0.82905 -0.02676 0.01710  -0.07233 182 MET A CB  
1395 C CG  . MET A 178 ? 1.09619 1.16959 1.04707 -0.02620 0.03890  -0.08428 182 MET A CG  
1396 S SD  . MET A 178 ? 1.46273 1.55491 1.47106 -0.00718 0.03650  -0.09169 182 MET A SD  
1397 C CE  . MET A 178 ? 1.08905 1.17181 1.08777 -0.00081 0.04119  -0.11499 182 MET A CE  
1398 N N   . THR A 179 ? 0.83450 0.91655 0.83517 -0.02250 0.01548  -0.04444 183 THR A N   
1399 C CA  . THR A 179 ? 0.89876 0.99292 0.90306 -0.02991 0.02112  -0.03480 183 THR A CA  
1400 C C   . THR A 179 ? 0.88863 0.99049 0.86957 -0.04341 0.03918  -0.04087 183 THR A C   
1401 O O   . THR A 179 ? 0.96430 1.08322 0.95328 -0.04220 0.05286  -0.05559 183 THR A O   
1402 C CB  . THR A 179 ? 0.92043 1.03824 0.96733 -0.02088 0.02166  -0.03344 183 THR A CB  
1403 O OG1 . THR A 179 ? 0.88327 0.99085 0.94720 -0.01092 0.00753  -0.02819 183 THR A OG1 
1404 C CG2 . THR A 179 ? 0.88430 1.01344 0.93513 -0.02878 0.02469  -0.02376 183 THR A CG2 
1405 N N   . PRO A 180 ? 0.92817 1.01725 0.88032 -0.05702 0.04067  -0.03086 184 PRO A N   
1406 C CA  . PRO A 180 ? 0.98079 1.07443 0.90707 -0.07381 0.06009  -0.03606 184 PRO A CA  
1407 C C   . PRO A 180 ? 0.92977 1.06399 0.89437 -0.07487 0.07655  -0.04571 184 PRO A C   
1408 O O   . PRO A 180 ? 0.83053 0.98392 0.83401 -0.06568 0.07030  -0.04239 184 PRO A O   
1409 C CB  . PRO A 180 ? 0.88343 0.95114 0.77648 -0.08667 0.05464  -0.02045 184 PRO A CB  
1410 C CG  . PRO A 180 ? 0.96870 1.01429 0.86186 -0.07510 0.03136  -0.01033 184 PRO A CG  
1411 C CD  . PRO A 180 ? 0.89181 0.95877 0.83165 -0.05818 0.02505  -0.01546 184 PRO A CD  
1412 N N   . TYR A 181 ? 0.98030 1.12821 0.93290 -0.08647 0.09764  -0.05884 185 TYR A N   
1413 C CA  . TYR A 181 ? 1.05334 1.24356 1.04212 -0.09047 0.11498  -0.07045 185 TYR A CA  
1414 C C   . TYR A 181 ? 0.97678 1.17351 0.97486 -0.10025 0.11302  -0.05848 185 TYR A C   
1415 O O   . TYR A 181 ? 1.06172 1.22776 1.02327 -0.11260 0.10819  -0.04415 185 TYR A O   
1416 C CB  . TYR A 181 ? 1.18534 1.38588 1.15111 -0.10750 0.14095  -0.08575 185 TYR A CB  
1417 C CG  . TYR A 181 ? 1.17833 1.42386 1.17936 -0.11712 0.16039  -0.09756 185 TYR A CG  
1418 C CD1 . TYR A 181 ? 1.28333 1.57167 1.33353 -0.10391 0.16914  -0.11839 185 TYR A CD1 
1419 C CD2 . TYR A 181 ? 1.14306 1.38854 1.13075 -0.13892 0.16883  -0.08915 185 TYR A CD2 
1420 C CE1 . TYR A 181 ? 1.30504 1.63990 1.39417 -0.11124 0.18507  -0.13156 185 TYR A CE1 
1421 C CE2 . TYR A 181 ? 1.18351 1.47426 1.20847 -0.14881 0.18600  -0.10183 185 TYR A CE2 
1422 C CZ  . TYR A 181 ? 1.20832 1.54602 1.28558 -0.13463 0.19382  -0.12353 185 TYR A CZ  
1423 O OH  . TYR A 181 ? 1.29245 1.68010 1.41231 -0.14334 0.20946  -0.13855 185 TYR A OH  
1424 N N   . VAL A 182 ? 1.02114 1.25680 1.06800 -0.09400 0.11539  -0.06524 186 VAL A N   
1425 C CA  . VAL A 182 ? 1.06055 1.30843 1.11995 -0.10447 0.11520  -0.05785 186 VAL A CA  
1426 C C   . VAL A 182 ? 1.08732 1.38753 1.19564 -0.10351 0.12732  -0.07503 186 VAL A C   
1427 O O   . VAL A 182 ? 1.00498 1.32924 1.14481 -0.08731 0.12865  -0.08944 186 VAL A O   
1428 C CB  . VAL A 182 ? 0.96718 1.19914 1.03581 -0.09201 0.09211  -0.04169 186 VAL A CB  
1429 C CG1 . VAL A 182 ? 0.93837 1.19592 1.05383 -0.07021 0.08171  -0.04697 186 VAL A CG1 
1430 C CG2 . VAL A 182 ? 1.07007 1.29963 1.13290 -0.10697 0.09188  -0.03234 186 VAL A CG2 
1431 N N   . VAL A 183 ? 1.11708 1.43500 1.23316 -0.12086 0.13546  -0.07478 187 VAL A N   
1432 C CA  . VAL A 183 ? 1.04870 1.42114 1.21332 -0.12292 0.14781  -0.09356 187 VAL A CA  
1433 C C   . VAL A 183 ? 0.98462 1.38164 1.19845 -0.09889 0.12778  -0.09439 187 VAL A C   
1434 O O   . VAL A 183 ? 0.92196 1.35362 1.17739 -0.08273 0.12835  -0.11075 187 VAL A O   
1435 C CB  . VAL A 183 ? 1.05169 1.43537 1.20888 -0.15207 0.16333  -0.09429 187 VAL A CB  
1436 C CG1 . VAL A 183 ? 0.91371 1.35689 1.13106 -0.15077 0.16785  -0.11182 187 VAL A CG1 
1437 C CG2 . VAL A 183 ? 0.90897 1.27970 1.02447 -0.17725 0.18922  -0.09984 187 VAL A CG2 
1438 N N   . THR A 184 ? 0.96285 1.34079 1.17097 -0.09588 0.10950  -0.07733 188 THR A N   
1439 C CA  . THR A 184 ? 0.92338 1.31763 1.16823 -0.07519 0.08944  -0.07528 188 THR A CA  
1440 C C   . THR A 184 ? 0.96485 1.32943 1.20095 -0.05344 0.07379  -0.06629 188 THR A C   
1441 O O   . THR A 184 ? 0.97853 1.30685 1.18632 -0.05344 0.06328  -0.04971 188 THR A O   
1442 C CB  . THR A 184 ? 0.87229 1.26130 1.11295 -0.08461 0.07959  -0.06327 188 THR A CB  
1443 O OG1 . THR A 184 ? 0.98918 1.39825 1.23084 -0.10936 0.09606  -0.07102 188 THR A OG1 
1444 C CG2 . THR A 184 ? 0.75500 1.16636 1.03273 -0.06597 0.06043  -0.06365 188 THR A CG2 
1445 N N   . ARG A 185 ? 0.96208 1.34282 1.22520 -0.03482 0.07210  -0.07851 189 ARG A N   
1446 C CA  . ARG A 185 ? 0.89314 1.24538 1.14881 -0.01620 0.05967  -0.07263 189 ARG A CA  
1447 C C   . ARG A 185 ? 0.84256 1.19715 1.12449 0.00465  0.03890  -0.06717 189 ARG A C   
1448 O O   . ARG A 185 ? 0.80792 1.13668 1.08400 0.01874  0.02834  -0.06142 189 ARG A O   
1449 C CB  . ARG A 185 ? 0.89744 1.25643 1.15802 -0.00983 0.07185  -0.09003 189 ARG A CB  
1450 C CG  . ARG A 185 ? 1.04233 1.44737 1.35132 0.00163  0.07661  -0.11106 189 ARG A CG  
1451 C CD  . ARG A 185 ? 1.08244 1.49163 1.39874 0.01226  0.08696  -0.12993 189 ARG A CD  
1452 N NE  . ARG A 185 ? 1.13325 1.53884 1.41800 -0.00798 0.11027  -0.13789 189 ARG A NE  
1453 C CZ  . ARG A 185 ? 1.19082 1.62156 1.47278 -0.03007 0.13054  -0.14573 189 ARG A CZ  
1454 N NH1 . ARG A 185 ? 1.01335 1.48021 1.32770 -0.03547 0.13109  -0.14901 189 ARG A NH1 
1455 N NH2 . ARG A 185 ? 1.22616 1.64438 1.47005 -0.04846 0.15074  -0.15080 189 ARG A NH2 
1456 N N   . TYR A 186 ? 0.84841 1.22985 1.15526 0.00549  0.03190  -0.06786 190 TYR A N   
1457 C CA  . TYR A 186 ? 0.82219 1.20749 1.15302 0.02637  0.01134  -0.06455 190 TYR A CA  
1458 C C   . TYR A 186 ? 0.71679 1.06094 1.02103 0.03098  -0.00368 -0.04381 190 TYR A C   
1459 O O   . TYR A 186 ? 0.66679 1.00422 0.98182 0.04767  -0.02050 -0.03876 190 TYR A O   
1460 C CB  . TYR A 186 ? 0.78865 1.21083 1.14760 0.02435  0.00495  -0.06932 190 TYR A CB  
1461 C CG  . TYR A 186 ? 0.74801 1.21493 1.13242 0.01155  0.02278  -0.08909 190 TYR A CG  
1462 C CD1 . TYR A 186 ? 0.80614 1.29610 1.21355 0.01800  0.03590  -0.10903 190 TYR A CD1 
1463 C CD2 . TYR A 186 ? 0.80567 1.29213 1.19145 -0.00845 0.02784  -0.08923 190 TYR A CD2 
1464 C CE1 . TYR A 186 ? 0.83245 1.36662 1.26437 0.00374  0.05550  -0.12890 190 TYR A CE1 
1465 C CE2 . TYR A 186 ? 0.75028 1.27872 1.16021 -0.02364 0.04634  -0.10812 190 TYR A CE2 
1466 C CZ  . TYR A 186 ? 0.73223 1.28560 1.16548 -0.01792 0.06093  -0.12794 190 TYR A CZ  
1467 O OH  . TYR A 186 ? 0.78408 1.38162 1.24212 -0.03504 0.08232  -0.14826 190 TYR A OH  
1468 N N   . TYR A 187 ? 0.78816 1.10509 1.05833 0.01645  0.00167  -0.03223 191 TYR A N   
1469 C CA  . TYR A 187 ? 0.76456 1.04875 1.01263 0.01752  -0.00967 -0.01467 191 TYR A CA  
1470 C C   . TYR A 187 ? 0.72280 0.97456 0.95164 0.02030  -0.00865 -0.01036 191 TYR A C   
1471 O O   . TYR A 187 ? 0.74537 0.97172 0.95811 0.01971  -0.01575 0.00232  191 TYR A O   
1472 C CB  . TYR A 187 ? 0.72378 1.00453 0.95303 0.00018  -0.00692 -0.00628 191 TYR A CB  
1473 C CG  . TYR A 187 ? 0.75593 1.06789 1.00497 -0.00310 -0.00995 -0.01111 191 TYR A CG  
1474 C CD1 . TYR A 187 ? 0.78740 1.13162 1.05414 -0.01198 0.00193  -0.02541 191 TYR A CD1 
1475 C CD2 . TYR A 187 ? 0.75671 1.06751 1.00756 0.00230  -0.02469 -0.00284 191 TYR A CD2 
1476 C CE1 . TYR A 187 ? 0.71334 1.09033 1.00339 -0.01558 -0.00158 -0.03216 191 TYR A CE1 
1477 C CE2 . TYR A 187 ? 0.70545 1.04651 0.97563 -0.00010 -0.03004 -0.00879 191 TYR A CE2 
1478 C CZ  . TYR A 187 ? 0.71067 1.08619 1.00299 -0.00880 -0.01899 -0.02395 191 TYR A CZ  
1479 O OH  . TYR A 187 ? 0.74694 1.15612 1.06251 -0.01263 -0.02461 -0.03184 191 TYR A OH  
1480 N N   . ARG A 188 ? 0.80654 1.06041 1.03739 0.02234  0.00059  -0.02218 192 ARG A N   
1481 C CA  . ARG A 188 ? 0.70900 0.93437 0.92385 0.02536  0.00046  -0.02120 192 ARG A CA  
1482 C C   . ARG A 188 ? 0.74001 0.94863 0.96554 0.04160  -0.01231 -0.01746 192 ARG A C   
1483 O O   . ARG A 188 ? 0.78351 1.00534 1.03248 0.05546  -0.01801 -0.02359 192 ARG A O   
1484 C CB  . ARG A 188 ? 0.73783 0.97142 0.95175 0.02414  0.01350  -0.03728 192 ARG A CB  
1485 C CG  . ARG A 188 ? 0.83446 1.08265 1.03410 0.00637  0.02902  -0.04268 192 ARG A CG  
1486 C CD  . ARG A 188 ? 0.78771 1.00888 0.95276 -0.00690 0.02796  -0.03029 192 ARG A CD  
1487 N NE  . ARG A 188 ? 0.87659 1.09659 1.01592 -0.02374 0.04129  -0.03376 192 ARG A NE  
1488 C CZ  . ARG A 188 ? 0.82183 1.03710 0.94424 -0.02762 0.05170  -0.04400 192 ARG A CZ  
1489 N NH1 . ARG A 188 ? 0.70819 0.93054 0.84588 -0.01548 0.05395  -0.05699 192 ARG A NH1 
1490 N NH2 . ARG A 188 ? 0.87835 1.07770 0.96423 -0.04399 0.05928  -0.04107 192 ARG A NH2 
1491 N N   . ALA A 189 ? 0.73173 0.91027 0.94038 0.03973  -0.01706 -0.00829 193 ALA A N   
1492 C CA  . ALA A 189 ? 0.75265 0.90787 0.96542 0.05101  -0.02721 -0.00389 193 ALA A CA  
1493 C C   . ALA A 189 ? 0.73119 0.88131 0.95341 0.06185  -0.02528 -0.01810 193 ALA A C   
1494 O O   . ALA A 189 ? 0.74544 0.90405 0.96311 0.05740  -0.01484 -0.03012 193 ALA A O   
1495 C CB  . ALA A 189 ? 0.74747 0.87584 0.94175 0.04218  -0.02983 0.00739  193 ALA A CB  
1496 N N   . PRO A 190 ? 0.68319 0.81552 0.91516 0.07586  -0.03543 -0.01701 194 PRO A N   
1497 C CA  . PRO A 190 ? 0.71979 0.84332 0.96125 0.08765  -0.03444 -0.03198 194 PRO A CA  
1498 C C   . PRO A 190 ? 0.75369 0.86164 0.97785 0.07826  -0.02719 -0.03818 194 PRO A C   
1499 O O   . PRO A 190 ? 0.72730 0.84226 0.95472 0.08212  -0.01952 -0.05518 194 PRO A O   
1500 C CB  . PRO A 190 ? 0.77732 0.87089 1.02244 0.10031  -0.04907 -0.02352 194 PRO A CB  
1501 C CG  . PRO A 190 ? 0.75870 0.86265 1.00633 0.10154  -0.05755 -0.01014 194 PRO A CG  
1502 C CD  . PRO A 190 ? 0.72072 0.83936 0.95389 0.08240  -0.04866 -0.00299 194 PRO A CD  
1503 N N   . GLU A 191 ? 0.70292 0.79174 0.90915 0.06591  -0.02951 -0.02631 195 GLU A N   
1504 C CA  . GLU A 191 ? 0.79094 0.86552 0.98236 0.05803  -0.02617 -0.03299 195 GLU A CA  
1505 C C   . GLU A 191 ? 0.79957 0.89431 0.97971 0.05072  -0.01539 -0.04271 195 GLU A C   
1506 O O   . GLU A 191 ? 0.82775 0.91603 0.99770 0.04986  -0.01123 -0.05552 195 GLU A O   
1507 C CB  . GLU A 191 ? 0.82977 0.88648 1.00998 0.04641  -0.03125 -0.01999 195 GLU A CB  
1508 C CG  . GLU A 191 ? 0.80436 0.87425 0.98112 0.03845  -0.03098 -0.00624 195 GLU A CG  
1509 C CD  . GLU A 191 ? 0.79590 0.85923 0.97955 0.04272  -0.03705 0.00637  195 GLU A CD  
1510 O OE1 . GLU A 191 ? 0.76273 0.82302 0.95693 0.05545  -0.04143 0.00412  195 GLU A OE1 
1511 O OE2 . GLU A 191 ? 0.72668 0.78742 0.90390 0.03386  -0.03794 0.01796  195 GLU A OE2 
1512 N N   . VAL A 192 ? 0.79691 0.91378 0.97602 0.04455  -0.01060 -0.03719 196 VAL A N   
1513 C CA  . VAL A 192 ? 0.81420 0.94701 0.97898 0.03529  0.00089  -0.04485 196 VAL A CA  
1514 C C   . VAL A 192 ? 0.81139 0.96402 0.98969 0.04296  0.01114  -0.06287 196 VAL A C   
1515 O O   . VAL A 192 ? 0.77801 0.93151 0.94039 0.03786  0.02114  -0.07526 196 VAL A O   
1516 C CB  . VAL A 192 ? 0.79687 0.94428 0.95723 0.02525  0.00300  -0.03382 196 VAL A CB  
1517 C CG1 . VAL A 192 ? 0.84829 1.00063 0.98460 0.01199  0.01354  -0.03798 196 VAL A CG1 
1518 C CG2 . VAL A 192 ? 0.76727 0.89801 0.92198 0.02138  -0.00713 -0.01826 196 VAL A CG2 
1519 N N   . ILE A 193 ? 0.73528 0.90449 0.94271 0.05562  0.00848  -0.06565 197 ILE A N   
1520 C CA  . ILE A 193 ? 0.83230 1.02574 1.06104 0.06551  0.01778  -0.08562 197 ILE A CA  
1521 C C   . ILE A 193 ? 0.83992 1.01465 1.06391 0.07328  0.01948  -0.10026 197 ILE A C   
1522 O O   . ILE A 193 ? 0.89400 1.08181 1.11435 0.07152  0.03352  -0.11842 197 ILE A O   
1523 C CB  . ILE A 193 ? 0.82581 1.03596 1.08936 0.08188  0.00850  -0.08560 197 ILE A CB  
1524 C CG1 . ILE A 193 ? 0.80296 1.03701 1.07295 0.07380  0.00773  -0.07531 197 ILE A CG1 
1525 C CG2 . ILE A 193 ? 0.80634 1.03810 1.09856 0.09751  0.01453  -0.10877 197 ILE A CG2 
1526 C CD1 . ILE A 193 ? 0.73795 0.97892 1.03492 0.09029  -0.00789 -0.07066 197 ILE A CD1 
1527 N N   . LEU A 194 ? 0.77895 0.92191 1.00137 0.08045  0.00620  -0.09331 198 LEU A N   
1528 C CA  . LEU A 194 ? 0.80887 0.93034 1.03022 0.08932  0.00508  -0.10737 198 LEU A CA  
1529 C C   . LEU A 194 ? 0.82296 0.92579 1.01191 0.07560  0.00862  -0.11013 198 LEU A C   
1530 O O   . LEU A 194 ? 0.82448 0.91012 1.00839 0.08048  0.00887  -0.12430 198 LEU A O   
1531 C CB  . LEU A 194 ? 0.81461 0.90688 1.04782 0.10147  -0.01111 -0.09827 198 LEU A CB  
1532 C CG  . LEU A 194 ? 0.86154 0.96843 1.12380 0.11784  -0.01840 -0.09594 198 LEU A CG  
1533 C CD1 . LEU A 194 ? 0.85688 0.92727 1.12257 0.12850  -0.03553 -0.08380 198 LEU A CD1 
1534 C CD2 . LEU A 194 ? 0.74090 0.87701 1.02999 0.13304  -0.01010 -0.12004 198 LEU A CD2 
1535 N N   . GLY A 195 ? 0.76066 0.86566 0.92716 0.05947  0.01006  -0.09815 199 GLY A N   
1536 C CA  . GLY A 195 ? 0.82313 0.91150 0.95780 0.04790  0.01064  -0.10113 199 GLY A CA  
1537 C C   . GLY A 195 ? 0.82370 0.88227 0.95377 0.04671  -0.00356 -0.09457 199 GLY A C   
1538 O O   . GLY A 195 ? 0.88433 0.92648 0.99608 0.04305  -0.00565 -0.10433 199 GLY A O   
1539 N N   . MET A 196 ? 0.71754 0.76918 0.86325 0.04850  -0.01293 -0.07928 200 MET A N   
1540 C CA  . MET A 196 ? 0.85142 0.87828 0.99574 0.04403  -0.02418 -0.07257 200 MET A CA  
1541 C C   . MET A 196 ? 0.82716 0.85707 0.95995 0.03149  -0.02844 -0.05956 200 MET A C   
1542 O O   . MET A 196 ? 0.84545 0.89255 0.97423 0.02779  -0.02433 -0.05134 200 MET A O   
1543 C CB  . MET A 196 ? 0.86266 0.87600 1.02768 0.05174  -0.03056 -0.06395 200 MET A CB  
1544 C CG  . MET A 196 ? 0.80673 0.81014 0.98535 0.06708  -0.03050 -0.07611 200 MET A CG  
1545 S SD  . MET A 196 ? 0.94021 0.94369 1.13857 0.07833  -0.03655 -0.06136 200 MET A SD  
1546 C CE  . MET A 196 ? 0.86692 0.83078 1.06078 0.07078  -0.04661 -0.04780 200 MET A CE  
1547 N N   . GLY A 197 ? 0.83793 0.85119 0.96816 0.02521  -0.03727 -0.05891 201 GLY A N   
1548 C CA  . GLY A 197 ? 0.74280 0.75973 0.87130 0.01606  -0.04286 -0.04749 201 GLY A CA  
1549 C C   . GLY A 197 ? 0.73548 0.75916 0.87939 0.01625  -0.04134 -0.03249 201 GLY A C   
1550 O O   . GLY A 197 ? 0.76125 0.77970 0.91727 0.02279  -0.03977 -0.02948 201 GLY A O   
1551 N N   . TYR A 198 ? 0.79508 0.82846 0.93646 0.00971  -0.04288 -0.02331 202 TYR A N   
1552 C CA  . TYR A 198 ? 0.87120 0.91321 1.02189 0.00937  -0.03999 -0.01025 202 TYR A CA  
1553 C C   . TYR A 198 ? 0.79024 0.83684 0.94230 0.00133  -0.04333 -0.00381 202 TYR A C   
1554 O O   . TYR A 198 ? 0.79096 0.83867 0.93430 -0.00166 -0.04822 -0.00836 202 TYR A O   
1555 C CB  . TYR A 198 ? 0.73277 0.79143 0.87859 0.01355  -0.03344 -0.00849 202 TYR A CB  
1556 C CG  . TYR A 198 ? 0.82912 0.89476 0.95602 0.00879  -0.03150 -0.01232 202 TYR A CG  
1557 C CD1 . TYR A 198 ? 0.76860 0.83859 0.88820 0.00254  -0.03345 -0.00446 202 TYR A CD1 
1558 C CD2 . TYR A 198 ? 0.81294 0.87725 0.92605 0.01014  -0.02771 -0.02410 202 TYR A CD2 
1559 C CE1 . TYR A 198 ? 0.71459 0.78347 0.81172 -0.00213 -0.03348 -0.00624 202 TYR A CE1 
1560 C CE2 . TYR A 198 ? 0.90637 0.97126 0.99439 0.00364  -0.02588 -0.02585 202 TYR A CE2 
1561 C CZ  . TYR A 198 ? 0.82003 0.88519 0.89942 -0.00236 -0.02970 -0.01586 202 TYR A CZ  
1562 O OH  . TYR A 198 ? 0.84863 0.90738 0.89912 -0.00875 -0.02973 -0.01576 202 TYR A OH  
1563 N N   . LYS A 199 ? 0.72883 0.77739 0.89061 -0.00139 -0.04117 0.00614  203 LYS A N   
1564 C CA  . LYS A 199 ? 0.83192 0.88781 0.99871 -0.00819 -0.04177 0.01107  203 LYS A CA  
1565 C C   . LYS A 199 ? 0.83234 0.90078 0.99233 -0.00734 -0.03798 0.01868  203 LYS A C   
1566 O O   . LYS A 199 ? 0.77657 0.85030 0.92851 -0.00291 -0.03545 0.01898  203 LYS A O   
1567 C CB  . LYS A 199 ? 0.98184 1.02998 1.16174 -0.01484 -0.03955 0.01503  203 LYS A CB  
1568 C CG  . LYS A 199 ? 0.97703 1.01476 1.15431 -0.01289 -0.03541 0.02454  203 LYS A CG  
1569 C CD  . LYS A 199 ? 0.94836 0.97271 1.13177 -0.02302 -0.03187 0.02934  203 LYS A CD  
1570 C CE  . LYS A 199 ? 1.13008 1.16876 1.31884 -0.03237 -0.02634 0.03233  203 LYS A CE  
1571 N NZ  . LYS A 199 ? 0.92194 0.97052 1.10028 -0.03001 -0.02302 0.04121  203 LYS A NZ  
1572 N N   . GLU A 200 ? 0.79043 0.86514 0.95526 -0.01230 -0.03696 0.02302  204 GLU A N   
1573 C CA  . GLU A 200 ? 0.78660 0.87105 0.94427 -0.01242 -0.03393 0.02893  204 GLU A CA  
1574 C C   . GLU A 200 ? 0.77127 0.85777 0.92711 -0.01068 -0.02978 0.03658  204 GLU A C   
1575 O O   . GLU A 200 ? 0.66980 0.76556 0.81924 -0.01033 -0.02817 0.03959  204 GLU A O   
1576 C CB  . GLU A 200 ? 0.76675 0.85704 0.93061 -0.01703 -0.03348 0.02959  204 GLU A CB  
1577 C CG  . GLU A 200 ? 0.93604 1.02579 1.11521 -0.02271 -0.03075 0.02838  204 GLU A CG  
1578 C CD  . GLU A 200 ? 1.07573 1.16599 1.26727 -0.02324 -0.03749 0.01838  204 GLU A CD  
1579 O OE1 . GLU A 200 ? 1.05733 1.13891 1.25013 -0.02275 -0.04082 0.01440  204 GLU A OE1 
1580 O OE2 . GLU A 200 ? 1.12715 1.22611 1.32661 -0.02279 -0.04110 0.01347  204 GLU A OE2 
1581 N N   . ASN A 201 ? 0.73439 0.81086 0.89436 -0.00975 -0.02936 0.03991  205 ASN A N   
1582 C CA  . ASN A 201 ? 0.76841 0.84555 0.92390 -0.00639 -0.02900 0.04774  205 ASN A CA  
1583 C C   . ASN A 201 ? 0.72455 0.80729 0.88146 0.00325  -0.03148 0.04396  205 ASN A C   
1584 O O   . ASN A 201 ? 0.70454 0.78662 0.86204 0.00926  -0.03450 0.04856  205 ASN A O   
1585 C CB  . ASN A 201 ? 0.76111 0.82092 0.91467 -0.00955 -0.02851 0.05534  205 ASN A CB  
1586 C CG  . ASN A 201 ? 0.92408 0.96551 1.08181 -0.00608 -0.03143 0.05246  205 ASN A CG  
1587 O OD1 . ASN A 201 ? 0.95176 0.99499 1.11517 -0.00170 -0.03333 0.04297  205 ASN A OD1 
1588 N ND2 . ASN A 201 ? 0.97779 0.99780 1.12941 -0.00902 -0.03168 0.06058  205 ASN A ND2 
1589 N N   . VAL A 202 ? 0.64498 0.73385 0.80198 0.00489  -0.03045 0.03491  206 VAL A N   
1590 C CA  . VAL A 202 ? 0.66658 0.77010 0.82536 0.01051  -0.02876 0.03014  206 VAL A CA  
1591 C C   . VAL A 202 ? 0.77771 0.89669 0.93366 0.00650  -0.02724 0.03514  206 VAL A C   
1592 O O   . VAL A 202 ? 0.76402 0.89731 0.92682 0.01105  -0.02772 0.03407  206 VAL A O   
1593 C CB  . VAL A 202 ? 0.69046 0.79687 0.84340 0.00958  -0.02520 0.01966  206 VAL A CB  
1594 C CG1 . VAL A 202 ? 0.68659 0.77704 0.84086 0.01275  -0.02771 0.01328  206 VAL A CG1 
1595 C CG2 . VAL A 202 ? 0.65676 0.76415 0.79554 0.00037  -0.02397 0.02108  206 VAL A CG2 
1596 N N   . ASP A 203 ? 0.62802 0.74516 0.77597 -0.00159 -0.02617 0.03910  207 ASP A N   
1597 C CA  . ASP A 203 ? 0.67132 0.79987 0.81490 -0.00631 -0.02482 0.04268  207 ASP A CA  
1598 C C   . ASP A 203 ? 0.70138 0.83193 0.84740 -0.00379 -0.02823 0.04964  207 ASP A C   
1599 O O   . ASP A 203 ? 0.66071 0.80498 0.80704 -0.00450 -0.02930 0.05035  207 ASP A O   
1600 C CB  . ASP A 203 ? 0.56938 0.69211 0.70464 -0.01344 -0.02390 0.04398  207 ASP A CB  
1601 C CG  . ASP A 203 ? 0.70103 0.81941 0.82732 -0.01596 -0.02341 0.03869  207 ASP A CG  
1602 O OD1 . ASP A 203 ? 0.67811 0.80227 0.80130 -0.01570 -0.02045 0.03446  207 ASP A OD1 
1603 O OD2 . ASP A 203 ? 0.72651 0.83566 0.84817 -0.01808 -0.02620 0.03819  207 ASP A OD2 
1604 N N   . LEU A 204 ? 0.63437 0.74985 0.77996 -0.00206 -0.03042 0.05480  208 LEU A N   
1605 C CA  . LEU A 204 ? 0.73097 0.84216 0.87150 0.00001  -0.03487 0.06308  208 LEU A CA  
1606 C C   . LEU A 204 ? 0.67808 0.79656 0.82700 0.01119  -0.04206 0.06164  208 LEU A C   
1607 O O   . LEU A 204 ? 0.62619 0.75306 0.77287 0.01359  -0.04794 0.06524  208 LEU A O   
1608 C CB  . LEU A 204 ? 0.75041 0.83956 0.88444 -0.00324 -0.03405 0.06960  208 LEU A CB  
1609 C CG  . LEU A 204 ? 0.75105 0.83903 0.87332 -0.01334 -0.02908 0.07465  208 LEU A CG  
1610 C CD1 . LEU A 204 ? 0.92268 0.98937 1.03363 -0.01725 -0.02829 0.08317  208 LEU A CD1 
1611 C CD2 . LEU A 204 ? 0.80067 0.90110 0.91459 -0.01347 -0.03202 0.07701  208 LEU A CD2 
1612 N N   . TRP A 205 ? 0.69150 0.80873 0.85152 0.01885  -0.04244 0.05458  209 TRP A N   
1613 C CA  . TRP A 205 ? 0.70049 0.83013 0.87447 0.03119  -0.04862 0.04946  209 TRP A CA  
1614 C C   . TRP A 205 ? 0.71676 0.87626 0.89844 0.02851  -0.04696 0.04411  209 TRP A C   
1615 O O   . TRP A 205 ? 0.68212 0.85569 0.87412 0.03631  -0.05511 0.04316  209 TRP A O   
1616 C CB  . TRP A 205 ? 0.64041 0.76764 0.82586 0.03874  -0.04619 0.03886  209 TRP A CB  
1617 C CG  . TRP A 205 ? 0.75481 0.90166 0.96039 0.05191  -0.05009 0.02908  209 TRP A CG  
1618 C CD1 . TRP A 205 ? 0.75388 0.93161 0.97285 0.05059  -0.04340 0.01756  209 TRP A CD1 
1619 C CD2 . TRP A 205 ? 0.78883 0.92617 1.00528 0.06855  -0.06148 0.02856  209 TRP A CD2 
1620 N NE1 . TRP A 205 ? 0.73775 0.93147 0.97996 0.06554  -0.04892 0.00798  209 TRP A NE1 
1621 C CE2 . TRP A 205 ? 0.78184 0.95026 1.02314 0.07843  -0.06152 0.01456  209 TRP A CE2 
1622 C CE3 . TRP A 205 ? 0.73500 0.83881 0.94196 0.07563  -0.07165 0.03832  209 TRP A CE3 
1623 C CZ2 . TRP A 205 ? 0.72870 0.89794 0.98936 0.09822  -0.07335 0.00880  209 TRP A CZ2 
1624 C CZ3 . TRP A 205 ? 0.81881 0.91701 1.03899 0.09429  -0.08403 0.03504  209 TRP A CZ3 
1625 C CH2 . TRP A 205 ? 0.77643 0.90842 1.02523 0.10705  -0.08579 0.01968  209 TRP A CH2 
1626 N N   . SER A 206 ? 0.66619 0.83441 0.84285 0.01726  -0.03761 0.04028  210 SER A N   
1627 C CA  . SER A 206 ? 0.61941 0.81260 0.80135 0.01121  -0.03435 0.03506  210 SER A CA  
1628 C C   . SER A 206 ? 0.67519 0.87175 0.85051 0.00748  -0.04059 0.04230  210 SER A C   
1629 O O   . SER A 206 ? 0.66699 0.88545 0.85353 0.00871  -0.04495 0.03837  210 SER A O   
1630 C CB  . SER A 206 ? 0.68235 0.87454 0.85360 -0.00069 -0.02400 0.03136  210 SER A CB  
1631 O OG  . SER A 206 ? 0.71920 0.91040 0.89353 0.00216  -0.01842 0.02321  210 SER A OG  
1632 N N   . VAL A 207 ? 0.69068 0.86735 0.84878 0.00266  -0.04105 0.05138  211 VAL A N   
1633 C CA  . VAL A 207 ? 0.68939 0.86638 0.83711 -0.00034 -0.04689 0.05777  211 VAL A CA  
1634 C C   . VAL A 207 ? 0.67138 0.85044 0.82417 0.01133  -0.05977 0.06106  211 VAL A C   
1635 O O   . VAL A 207 ? 0.73743 0.93004 0.89027 0.01160  -0.06780 0.06110  211 VAL A O   
1636 C CB  . VAL A 207 ? 0.65720 0.81295 0.78638 -0.00721 -0.04296 0.06522  211 VAL A CB  
1637 C CG1 . VAL A 207 ? 0.60921 0.76290 0.72321 -0.01007 -0.04841 0.07138  211 VAL A CG1 
1638 C CG2 . VAL A 207 ? 0.61892 0.77409 0.74527 -0.01621 -0.03388 0.06077  211 VAL A CG2 
1639 N N   . GLY A 208 ? 0.68896 0.85359 0.84610 0.02180  -0.06372 0.06308  212 GLY A N   
1640 C CA  . GLY A 208 ? 0.64707 0.80947 0.80882 0.03571  -0.07872 0.06612  212 GLY A CA  
1641 C C   . GLY A 208 ? 0.71411 0.91094 0.90139 0.04298  -0.08494 0.05491  212 GLY A C   
1642 O O   . GLY A 208 ? 0.70986 0.91607 0.89757 0.04791  -0.09835 0.05685  212 GLY A O   
1643 N N   . CYS A 209 ? 0.66136 0.87907 0.86951 0.04208  -0.07475 0.04209  213 CYS A N   
1644 C CA  . CYS A 209 ? 0.73660 0.99201 0.97315 0.04630  -0.07710 0.02877  213 CYS A CA  
1645 C C   . CYS A 209 ? 0.73027 1.00452 0.96350 0.03443  -0.07862 0.02863  213 CYS A C   
1646 O O   . CYS A 209 ? 0.71237 1.01014 0.96227 0.04053  -0.09083 0.02363  213 CYS A O   
1647 C CB  . CYS A 209 ? 0.68203 0.95373 0.93443 0.04251  -0.06140 0.01529  213 CYS A CB  
1648 S SG  . CYS A 209 ? 0.79536 1.04530 1.05231 0.05729  -0.06086 0.01243  213 CYS A SG  
1649 N N   . ILE A 210 ? 0.79844 1.06181 1.01086 0.01814  -0.06785 0.03319  214 ILE A N   
1650 C CA  . ILE A 210 ? 0.76050 1.03755 0.96766 0.00563  -0.06829 0.03196  214 ILE A CA  
1651 C C   . ILE A 210 ? 0.75052 1.02175 0.94567 0.01091  -0.08499 0.03979  214 ILE A C   
1652 O O   . ILE A 210 ? 0.68107 0.97600 0.88690 0.00979  -0.09422 0.03408  214 ILE A O   
1653 C CB  . ILE A 210 ? 0.77840 1.03807 0.96392 -0.00993 -0.05495 0.03542  214 ILE A CB  
1654 C CG1 . ILE A 210 ? 0.70911 0.97337 0.90205 -0.01542 -0.04098 0.02790  214 ILE A CG1 
1655 C CG2 . ILE A 210 ? 0.71633 0.98389 0.89372 -0.02230 -0.05588 0.03403  214 ILE A CG2 
1656 C CD1 . ILE A 210 ? 0.66426 0.90277 0.83490 -0.02422 -0.03199 0.03307  214 ILE A CD1 
1657 N N   . MET A 211 ? 0.73057 0.97019 0.90234 0.01584  -0.08945 0.05243  215 MET A N   
1658 C CA  . MET A 211 ? 0.75507 0.98408 0.90770 0.01991  -0.10520 0.06119  215 MET A CA  
1659 C C   . MET A 211 ? 0.80862 1.05344 0.98079 0.03691  -0.12494 0.05779  215 MET A C   
1660 O O   . MET A 211 ? 0.86546 1.12292 1.03535 0.03822  -0.13972 0.05694  215 MET A O   
1661 C CB  . MET A 211 ? 0.81096 1.00126 0.93299 0.01952  -0.10341 0.07530  215 MET A CB  
1662 C CG  . MET A 211 ? 0.83909 1.01358 0.93101 0.01915  -0.11630 0.08538  215 MET A CG  
1663 S SD  . MET A 211 ? 0.91882 1.04768 0.97334 0.01452  -0.10989 0.10132  215 MET A SD  
1664 C CE  . MET A 211 ? 0.87076 0.98410 0.88708 0.01512  -0.12829 0.11195  215 MET A CE  
1665 N N   . GLY A 212 ? 0.78107 1.02608 0.97378 0.05103  -0.12686 0.05429  216 GLY A N   
1666 C CA  . GLY A 212 ? 0.79109 1.05490 1.00919 0.06980  -0.14634 0.04784  216 GLY A CA  
1667 C C   . GLY A 212 ? 0.80454 1.11631 1.05442 0.06615  -0.14860 0.03190  216 GLY A C   
1668 O O   . GLY A 212 ? 0.84149 1.16990 1.10135 0.07549  -0.16919 0.02905  216 GLY A O   
1669 N N   . GLU A 213 ? 0.80828 1.14136 1.07233 0.05108  -0.12805 0.02147  217 GLU A N   
1670 C CA  . GLU A 213 ? 0.76757 1.14565 1.06130 0.04270  -0.12636 0.00560  217 GLU A CA  
1671 C C   . GLU A 213 ? 0.81499 1.19617 1.09146 0.03199  -0.13642 0.00905  217 GLU A C   
1672 O O   . GLU A 213 ? 0.84054 1.25467 1.14074 0.03513  -0.15064 -0.00111 217 GLU A O   
1673 C CB  . GLU A 213 ? 0.73453 1.12422 1.03611 0.02558  -0.10074 -0.00321 217 GLU A CB  
1674 C CG  . GLU A 213 ? 0.74344 1.18128 1.08101 0.01601  -0.09480 -0.02201 217 GLU A CG  
1675 C CD  . GLU A 213 ? 0.87081 1.31638 1.21486 0.00216  -0.06910 -0.03079 217 GLU A CD  
1676 O OE1 . GLU A 213 ? 0.87486 1.30556 1.21712 0.01135  -0.06202 -0.02978 217 GLU A OE1 
1677 O OE2 . GLU A 213 ? 0.77793 1.24295 1.12730 -0.01828 -0.05651 -0.03911 217 GLU A OE2 
1678 N N   . MET A 214 ? 0.90371 1.25248 1.14053 0.01967  -0.12977 0.02156  218 MET A N   
1679 C CA  . MET A 214 ? 0.88221 1.23072 1.09877 0.00975  -0.13885 0.02377  218 MET A CA  
1680 C C   . MET A 214 ? 0.84441 1.19189 1.05476 0.02500  -0.16618 0.02845  218 MET A C   
1681 O O   . MET A 214 ? 1.08892 1.44631 1.29022 0.01891  -0.17822 0.02598  218 MET A O   
1682 C CB  . MET A 214 ? 0.78203 1.09361 0.95667 -0.00260 -0.12751 0.03562  218 MET A CB  
1683 C CG  . MET A 214 ? 0.95459 1.25315 1.12691 -0.01170 -0.10494 0.03600  218 MET A CG  
1684 S SD  . MET A 214 ? 1.14525 1.41681 1.28284 -0.02911 -0.09127 0.04107  218 MET A SD  
1685 C CE  . MET A 214 ? 0.98264 1.22684 1.08396 -0.02400 -0.10262 0.05404  218 MET A CE  
1686 N N   . VAL A 215 ? 0.87593 1.20695 1.08650 0.04432  -0.17727 0.03575  219 VAL A N   
1687 C CA  . VAL A 215 ? 0.90823 1.23005 1.10776 0.06126  -0.20609 0.04252  219 VAL A CA  
1688 C C   . VAL A 215 ? 0.88915 1.25184 1.13794 0.07927  -0.22399 0.02729  219 VAL A C   
1689 O O   . VAL A 215 ? 0.88632 1.26622 1.14099 0.08692  -0.24856 0.02342  219 VAL A O   
1690 C CB  . VAL A 215 ? 0.94896 1.22054 1.11415 0.07121  -0.20900 0.06105  219 VAL A CB  
1691 C CG1 . VAL A 215 ? 0.94158 1.20028 1.09837 0.09254  -0.24093 0.06796  219 VAL A CG1 
1692 C CG2 . VAL A 215 ? 0.94080 1.17631 1.05773 0.05322  -0.19403 0.07460  219 VAL A CG2 
1693 N N   . CYS A 216 ? 0.89690 1.27639 1.18213 0.08677  -0.21222 0.01715  220 CYS A N   
1694 C CA  . CYS A 216 ? 0.82040 1.24443 1.15972 0.10362  -0.22445 -0.00142 220 CYS A CA  
1695 C C   . CYS A 216 ? 0.79796 1.27620 1.17360 0.08817  -0.21697 -0.02117 220 CYS A C   
1696 O O   . CYS A 216 ? 0.71139 1.23232 1.12931 0.09961  -0.23410 -0.03706 220 CYS A O   
1697 C CB  . CYS A 216 ? 0.79095 1.21516 1.15506 0.11405  -0.21001 -0.00802 220 CYS A CB  
1698 S SG  . CYS A 216 ? 1.21386 1.59387 1.56444 0.14326  -0.23064 0.00459  220 CYS A SG  
1699 N N   . HIS A 217 ? 0.81386 1.29075 1.17511 0.06224  -0.19203 -0.02125 221 HIS A N   
1700 C CA  . HIS A 217 ? 0.85888 1.38221 1.25446 0.04376  -0.17735 -0.04035 221 HIS A CA  
1701 C C   . HIS A 217 ? 0.79557 1.35480 1.24011 0.05137  -0.16548 -0.05817 221 HIS A C   
1702 O O   . HIS A 217 ? 0.79376 1.40503 1.28427 0.04755  -0.16485 -0.07881 221 HIS A O   
1703 C CB  . HIS A 217 ? 0.79978 1.35615 1.21091 0.04011  -0.19788 -0.05005 221 HIS A CB  
1704 C CG  . HIS A 217 ? 0.86344 1.38420 1.22653 0.04082  -0.21696 -0.03346 221 HIS A CG  
1705 N ND1 . HIS A 217 ? 0.92466 1.41081 1.24173 0.02143  -0.20313 -0.02152 221 HIS A ND1 
1706 C CD2 . HIS A 217 ? 0.83288 1.34573 1.18437 0.05869  -0.24868 -0.02731 221 HIS A CD2 
1707 C CE1 . HIS A 217 ? 0.97586 1.43655 1.25542 0.02596  -0.22301 -0.00978 221 HIS A CE1 
1708 N NE2 . HIS A 217 ? 0.98618 1.46039 1.28263 0.04783  -0.25125 -0.01189 221 HIS A NE2 
1709 N N   . LYS A 218 ? 0.72869 1.26083 1.16375 0.06151  -0.15536 -0.05157 222 LYS A N   
1710 C CA  . LYS A 218 ? 0.74523 1.30472 1.22070 0.07095  -0.14371 -0.06817 222 LYS A CA  
1711 C C   . LYS A 218 ? 0.78603 1.30312 1.23273 0.07187  -0.12700 -0.05699 222 LYS A C   
1712 O O   . LYS A 218 ? 0.76410 1.23389 1.17179 0.07762  -0.13500 -0.03748 222 LYS A O   
1713 C CB  . LYS A 218 ? 0.72943 1.31340 1.24469 0.10090  -0.17005 -0.07880 222 LYS A CB  
1714 C CG  . LYS A 218 ? 0.83065 1.46900 1.40623 0.10732  -0.15923 -0.10621 222 LYS A CG  
1715 C CD  . LYS A 218 ? 0.89764 1.59103 1.50575 0.08295  -0.14486 -0.12537 222 LYS A CD  
1716 C CE  . LYS A 218 ? 0.88358 1.64063 1.56027 0.09181  -0.13824 -0.15609 222 LYS A CE  
1717 N NZ  . LYS A 218 ? 0.80703 1.60839 1.50674 0.06039  -0.11006 -0.17389 222 LYS A NZ  
1718 N N   . ILE A 219 ? 0.73844 1.27322 1.20320 0.06416  -0.10307 -0.07020 223 ILE A N   
1719 C CA  . ILE A 219 ? 0.71425 1.21338 1.15442 0.06405  -0.08722 -0.06288 223 ILE A CA  
1720 C C   . ILE A 219 ? 0.76396 1.24249 1.20971 0.09214  -0.10305 -0.06004 223 ILE A C   
1721 O O   . ILE A 219 ? 0.75910 1.26739 1.24568 0.11172  -0.11425 -0.07531 223 ILE A O   
1722 C CB  . ILE A 219 ? 0.71603 1.24153 1.17359 0.04976  -0.05961 -0.07986 223 ILE A CB  
1723 C CG1 . ILE A 219 ? 0.74516 1.28632 1.19478 0.02064  -0.04490 -0.08191 223 ILE A CG1 
1724 C CG2 . ILE A 219 ? 0.73423 1.22210 1.16293 0.04890  -0.04522 -0.07275 223 ILE A CG2 
1725 C CD1 . ILE A 219 ? 0.49881 1.07144 0.96719 0.00358  -0.01760 -0.10046 223 ILE A CD1 
1726 N N   . LEU A 220 ? 0.72830 1.15551 1.13457 0.09413  -0.10410 -0.04155 224 LEU A N   
1727 C CA  . LEU A 220 ? 0.74240 1.14018 1.14655 0.11826  -0.12004 -0.03580 224 LEU A CA  
1728 C C   . LEU A 220 ? 0.75369 1.16352 1.18625 0.13063  -0.10990 -0.05322 224 LEU A C   
1729 O O   . LEU A 220 ? 0.80420 1.21804 1.26240 0.15536  -0.12570 -0.06121 224 LEU A O   
1730 C CB  . LEU A 220 ? 0.73354 1.07528 1.08944 0.11272  -0.11999 -0.01327 224 LEU A CB  
1731 C CG  . LEU A 220 ? 0.77760 1.09902 1.10084 0.10464  -0.13181 0.00471  224 LEU A CG  
1732 C CD1 . LEU A 220 ? 0.83330 1.10137 1.11921 0.10700  -0.13549 0.02339  224 LEU A CD1 
1733 C CD2 . LEU A 220 ? 0.69023 1.03270 1.03055 0.11813  -0.15646 0.00191  224 LEU A CD2 
1734 N N   . PHE A 221 ? 0.78589 1.19776 1.21131 0.11469  -0.08467 -0.05929 225 PHE A N   
1735 C CA  . PHE A 221 ? 0.79862 1.21151 1.23895 0.12409  -0.07296 -0.07390 225 PHE A CA  
1736 C C   . PHE A 221 ? 0.78581 1.24093 1.24625 0.10843  -0.04793 -0.09394 225 PHE A C   
1737 O O   . PHE A 221 ? 0.82374 1.26544 1.26172 0.09380  -0.02793 -0.09447 225 PHE A O   
1738 C CB  . PHE A 221 ? 0.74880 1.11026 1.15024 0.12050  -0.06769 -0.05993 225 PHE A CB  
1739 C CG  . PHE A 221 ? 0.70781 1.02467 1.08264 0.12876  -0.08759 -0.03836 225 PHE A CG  
1740 C CD1 . PHE A 221 ? 0.76158 1.06627 1.14956 0.15311  -0.10929 -0.03766 225 PHE A CD1 
1741 C CD2 . PHE A 221 ? 0.73020 1.01572 1.06585 0.11184  -0.08393 -0.01943 225 PHE A CD2 
1742 C CE1 . PHE A 221 ? 0.72956 0.98830 1.08674 0.15791  -0.12591 -0.01663 225 PHE A CE1 
1743 C CE2 . PHE A 221 ? 0.70214 0.94724 1.01162 0.11637  -0.09865 -0.00052 225 PHE A CE2 
1744 C CZ  . PHE A 221 ? 0.77242 1.00238 1.09005 0.13823  -0.11912 0.00176  225 PHE A CZ  
1745 N N   . PRO A 222 ? 0.70191 1.20853 1.20441 0.11065  -0.04861 -0.11152 226 PRO A N   
1746 C CA  . PRO A 222 ? 0.74521 1.29331 1.26570 0.09154  -0.02208 -0.13087 226 PRO A CA  
1747 C C   . PRO A 222 ? 0.90616 1.46576 1.44590 0.10143  -0.00667 -0.15162 226 PRO A C   
1748 O O   . PRO A 222 ? 0.94584 1.52207 1.52331 0.12736  -0.01827 -0.16624 226 PRO A O   
1749 C CB  . PRO A 222 ? 0.75207 1.35364 1.31743 0.09295  -0.03097 -0.14443 226 PRO A CB  
1750 C CG  . PRO A 222 ? 0.76825 1.36449 1.35485 0.12488  -0.06197 -0.14263 226 PRO A CG  
1751 C CD  . PRO A 222 ? 0.75898 1.28886 1.29519 0.13064  -0.07424 -0.11567 226 PRO A CD  
1752 N N   . GLY A 223 ? 0.87785 1.42782 1.39050 0.08114  0.01892  -0.15390 227 GLY A N   
1753 C CA  . GLY A 223 ? 0.91840 1.47834 1.44331 0.08752  0.03607  -0.17469 227 GLY A CA  
1754 C C   . GLY A 223 ? 0.95235 1.53764 1.47062 0.06094  0.06839  -0.18923 227 GLY A C   
1755 O O   . GLY A 223 ? 0.92731 1.48625 1.39995 0.03666  0.08010  -0.17491 227 GLY A O   
1756 N N   . ARG A 224 ? 0.92060 1.55601 1.48364 0.06567  0.08311  -0.21850 228 ARG A N   
1757 C CA  . ARG A 224 ? 0.99669 1.65180 1.54891 0.04100  0.11735  -0.23470 228 ARG A CA  
1758 C C   . ARG A 224 ? 1.03261 1.63921 1.53300 0.03671  0.12757  -0.22785 228 ARG A C   
1759 O O   . ARG A 224 ? 1.05698 1.65001 1.51567 0.00969  0.14887  -0.22405 228 ARG A O   
1760 C CB  . ARG A 224 ? 0.97002 1.68770 1.58314 0.05089  0.13171  -0.27059 228 ARG A CB  
1761 C CG  . ARG A 224 ? 1.06981 1.84000 1.74642 0.06435  0.11496  -0.28205 228 ARG A CG  
1762 C CD  . ARG A 224 ? 1.17358 2.01479 1.89818 0.04941  0.14305  -0.31510 228 ARG A CD  
1763 N NE  . ARG A 224 ? 1.22895 2.12851 2.03067 0.07507  0.12774  -0.33919 228 ARG A NE  
1764 C CZ  . ARG A 224 ? 1.27895 2.23534 2.13620 0.08376  0.14528  -0.37566 228 ARG A CZ  
1765 N NH1 . ARG A 224 ? 1.23437 2.19564 2.07583 0.06857  0.18031  -0.39262 228 ARG A NH1 
1766 N NH2 . ARG A 224 ? 1.21893 2.22906 2.14919 0.10883  0.12677  -0.39676 228 ARG A NH2 
1767 N N   . ASP A 225 ? 1.01677 1.59364 1.51666 0.06261  0.11073  -0.22535 229 ASP A N   
1768 C CA  . ASP A 225 ? 0.92921 1.46849 1.39273 0.06369  0.11895  -0.22657 229 ASP A CA  
1769 C C   . ASP A 225 ? 0.94753 1.43204 1.38433 0.07685  0.09270  -0.20140 229 ASP A C   
1770 O O   . ASP A 225 ? 0.91166 1.39034 1.36064 0.08698  0.07027  -0.18601 229 ASP A O   
1771 C CB  . ASP A 225 ? 0.92244 1.49025 1.42399 0.08282  0.12983  -0.25903 229 ASP A CB  
1772 C CG  . ASP A 225 ? 1.22733 1.75481 1.69352 0.08724  0.13576  -0.26323 229 ASP A CG  
1773 O OD1 . ASP A 225 ? 1.32584 1.87634 1.79789 0.08333  0.16020  -0.28951 229 ASP A OD1 
1774 O OD2 . ASP A 225 ? 1.21171 1.68834 1.64810 0.09480  0.11685  -0.24329 229 ASP A OD2 
1775 N N   . TYR A 226 ? 0.97620 1.42016 1.37373 0.07429  0.09627  -0.19732 230 TYR A N   
1776 C CA  . TYR A 226 ? 0.98056 1.37599 1.35868 0.08678  0.07361  -0.17793 230 TYR A CA  
1777 C C   . TYR A 226 ? 0.99124 1.38474 1.40568 0.11764  0.05713  -0.18791 230 TYR A C   
1778 O O   . TYR A 226 ? 0.96368 1.33256 1.37998 0.13017  0.03395  -0.17054 230 TYR A O   
1779 C CB  . TYR A 226 ? 1.02443 1.38013 1.35362 0.07468  0.08074  -0.17274 230 TYR A CB  
1780 C CG  . TYR A 226 ? 1.09817 1.43465 1.38729 0.05152  0.08097  -0.15034 230 TYR A CG  
1781 C CD1 . TYR A 226 ? 1.17807 1.51145 1.43070 0.02890  0.09954  -0.15246 230 TYR A CD1 
1782 C CD2 . TYR A 226 ? 1.00244 1.32260 1.28893 0.05258  0.06236  -0.12749 230 TYR A CD2 
1783 C CE1 . TYR A 226 ? 1.21984 1.53214 1.43619 0.01007  0.09724  -0.13208 230 TYR A CE1 
1784 C CE2 . TYR A 226 ? 1.00157 1.30470 1.25470 0.03346  0.06212  -0.10906 230 TYR A CE2 
1785 C CZ  . TYR A 226 ? 1.14959 1.44808 1.36889 0.01331  0.07848  -0.11135 230 TYR A CZ  
1786 O OH  . TYR A 226 ? 1.09425 1.37223 1.28054 -0.00336 0.07597  -0.09340 230 TYR A OH  
1787 N N   . ILE A 227 ? 1.00426 1.42169 1.44662 0.13036  0.06874  -0.21615 231 ILE A N   
1788 C CA  . ILE A 227 ? 0.97553 1.38706 1.45292 0.16225  0.05100  -0.22646 231 ILE A CA  
1789 C C   . ILE A 227 ? 0.91895 1.35976 1.43817 0.17680  0.03315  -0.22366 231 ILE A C   
1790 O O   . ILE A 227 ? 0.92186 1.33896 1.45276 0.19946  0.00766  -0.21482 231 ILE A O   
1791 C CB  . ILE A 227 ? 1.08726 1.51716 1.58745 0.17520  0.06703  -0.26024 231 ILE A CB  
1792 C CG1 . ILE A 227 ? 1.03577 1.52305 1.55584 0.16094  0.09681  -0.28567 231 ILE A CG1 
1793 C CG2 . ILE A 227 ? 1.23541 1.61660 1.69489 0.17296  0.07051  -0.26037 231 ILE A CG2 
1794 C CD1 . ILE A 227 ? 1.06370 1.60863 1.64399 0.17240  0.09334  -0.29955 231 ILE A CD1 
1795 N N   . ASP A 228 ? 0.90444 1.39503 1.44435 0.16293  0.04544  -0.23092 232 ASP A N   
1796 C CA  . ASP A 228 ? 0.82744 1.34553 1.40135 0.17213  0.02685  -0.22566 232 ASP A CA  
1797 C C   . ASP A 228 ? 0.84092 1.31541 1.38073 0.16880  0.00426  -0.19179 232 ASP A C   
1798 O O   . ASP A 228 ? 0.80316 1.26792 1.35836 0.18901  -0.02196 -0.18303 232 ASP A O   
1799 C CB  . ASP A 228 ? 0.83805 1.41267 1.43212 0.15038  0.04674  -0.23754 232 ASP A CB  
1800 C CG  . ASP A 228 ? 0.92532 1.55374 1.58252 0.16837  0.03452  -0.25479 232 ASP A CG  
1801 O OD1 . ASP A 228 ? 0.88616 1.53861 1.58735 0.19314  0.03303  -0.28044 232 ASP A OD1 
1802 O OD2 . ASP A 228 ? 0.96690 1.61413 1.63085 0.15832  0.02570  -0.24424 232 ASP A OD2 
1803 N N   . GLN A 229 ? 0.78284 1.22947 1.27467 0.14368  0.01388  -0.17299 233 GLN A N   
1804 C CA  . GLN A 229 ? 0.83953 1.25283 1.30189 0.13740  -0.00338 -0.14370 233 GLN A CA  
1805 C C   . GLN A 229 ? 0.85339 1.21711 1.30204 0.15597  -0.02424 -0.13033 233 GLN A C   
1806 O O   . GLN A 229 ? 0.83304 1.18199 1.28159 0.16550  -0.04591 -0.11466 233 GLN A O   
1807 C CB  . GLN A 229 ? 0.83231 1.22805 1.25038 0.10864  0.01168  -0.12990 233 GLN A CB  
1808 C CG  . GLN A 229 ? 0.86720 1.23846 1.26063 0.10057  -0.00254 -0.10390 233 GLN A CG  
1809 C CD  . GLN A 229 ? 0.90318 1.27262 1.26610 0.07352  0.01205  -0.09538 233 GLN A CD  
1810 O OE1 . GLN A 229 ? 0.95649 1.34839 1.31939 0.05965  0.03214  -0.10859 233 GLN A OE1 
1811 N NE2 . GLN A 229 ? 0.92464 1.26584 1.25981 0.06533  0.00273  -0.07379 233 GLN A NE2 
1812 N N   . TRP A 230 ? 0.85435 1.19050 1.28948 0.16024  -0.01791 -0.13688 234 TRP A N   
1813 C CA  . TRP A 230 ? 0.78605 1.07362 1.20984 0.17656  -0.03628 -0.12645 234 TRP A CA  
1814 C C   . TRP A 230 ? 0.82540 1.11817 1.28380 0.20504  -0.05821 -0.13134 234 TRP A C   
1815 O O   . TRP A 230 ? 0.85000 1.10548 1.29461 0.21415  -0.07952 -0.11235 234 TRP A O   
1816 C CB  . TRP A 230 ? 0.75119 1.01559 1.16285 0.17806  -0.02533 -0.13930 234 TRP A CB  
1817 C CG  . TRP A 230 ? 0.82412 1.03743 1.22567 0.19320  -0.04272 -0.13102 234 TRP A CG  
1818 C CD1 . TRP A 230 ? 0.86164 1.06210 1.28455 0.21749  -0.05048 -0.14703 234 TRP A CD1 
1819 C CD2 . TRP A 230 ? 0.80648 0.97292 1.17429 0.18431  -0.05393 -0.10557 234 TRP A CD2 
1820 N NE1 . TRP A 230 ? 0.86537 1.00966 1.26666 0.22300  -0.06629 -0.13155 234 TRP A NE1 
1821 C CE2 . TRP A 230 ? 0.82878 0.95322 1.19680 0.20190  -0.06765 -0.10628 234 TRP A CE2 
1822 C CE3 . TRP A 230 ? 0.84158 0.99761 1.18022 0.16301  -0.05289 -0.08365 234 TRP A CE3 
1823 C CZ2 . TRP A 230 ? 0.87663 0.95006 1.21557 0.19591  -0.07866 -0.08517 234 TRP A CZ2 
1824 C CZ3 . TRP A 230 ? 0.76045 0.86994 1.07353 0.15868  -0.06353 -0.06429 234 TRP A CZ3 
1825 C CH2 . TRP A 230 ? 0.87482 0.94410 1.18775 0.17369  -0.07550 -0.06485 234 TRP A CH2 
1826 N N   . ASN A 231 ? 0.82690 1.16591 1.33006 0.21914  -0.05378 -0.15690 235 ASN A N   
1827 C CA  . ASN A 231 ? 0.82860 1.17398 1.36867 0.24982  -0.07772 -0.16384 235 ASN A CA  
1828 C C   . ASN A 231 ? 0.82239 1.17068 1.36028 0.25001  -0.09897 -0.14370 235 ASN A C   
1829 O O   . ASN A 231 ? 0.82586 1.14327 1.36205 0.27022  -0.12592 -0.13207 235 ASN A O   
1830 C CB  . ASN A 231 ? 0.87061 1.27386 1.46524 0.26386  -0.06713 -0.19842 235 ASN A CB  
1831 C CG  . ASN A 231 ? 0.97755 1.36615 1.58214 0.27999  -0.05913 -0.22044 235 ASN A CG  
1832 O OD1 . ASN A 231 ? 0.99297 1.32443 1.56867 0.28629  -0.06826 -0.20944 235 ASN A OD1 
1833 N ND2 . ASN A 231 ? 0.93225 1.37303 1.57898 0.28624  -0.04152 -0.25319 235 ASN A ND2 
1834 N N   . LYS A 232 ? 0.79490 1.17607 1.32876 0.22701  -0.08777 -0.13901 236 LYS A N   
1835 C CA  . LYS A 232 ? 0.79735 1.17803 1.32285 0.22433  -0.10689 -0.11978 236 LYS A CA  
1836 C C   . LYS A 232 ? 0.83227 1.14977 1.30786 0.21987  -0.11995 -0.08983 236 LYS A C   
1837 O O   . LYS A 232 ? 0.88496 1.18285 1.35240 0.23092  -0.14438 -0.07475 236 LYS A O   
1838 C CB  . LYS A 232 ? 0.85006 1.27145 1.37575 0.19754  -0.09013 -0.12062 236 LYS A CB  
1839 C CG  . LYS A 232 ? 0.85213 1.33953 1.43123 0.20343  -0.09112 -0.14299 236 LYS A CG  
1840 C CD  . LYS A 232 ? 0.87204 1.40233 1.48777 0.20376  -0.06658 -0.17418 236 LYS A CD  
1841 C CE  . LYS A 232 ? 0.84170 1.44139 1.51994 0.21295  -0.06897 -0.20004 236 LYS A CE  
1842 N NZ  . LYS A 232 ? 0.83340 1.43990 1.55321 0.25100  -0.09825 -0.21081 236 LYS A NZ  
1843 N N   . VAL A 233 ? 0.82692 1.11218 1.26812 0.20323  -0.10420 -0.08152 237 VAL A N   
1844 C CA  . VAL A 233 ? 0.85279 1.08289 1.25026 0.19608  -0.11339 -0.05532 237 VAL A CA  
1845 C C   . VAL A 233 ? 0.89535 1.08191 1.29049 0.21990  -0.13512 -0.04997 237 VAL A C   
1846 O O   . VAL A 233 ? 0.91623 1.07104 1.28921 0.22348  -0.15409 -0.02983 237 VAL A O   
1847 C CB  . VAL A 233 ? 0.84895 1.05887 1.21628 0.17395  -0.09293 -0.05070 237 VAL A CB  
1848 C CG1 . VAL A 233 ? 0.75953 0.92280 1.08752 0.16338  -0.10013 -0.02554 237 VAL A CG1 
1849 C CG2 . VAL A 233 ? 0.81638 1.06470 1.18396 0.15220  -0.07314 -0.05628 237 VAL A CG2 
1850 N N   . ILE A 234 ? 0.91122 1.09262 1.32626 0.23619  -0.13277 -0.06803 238 ILE A N   
1851 C CA  . ILE A 234 ? 0.94806 1.07999 1.35729 0.25818  -0.15346 -0.06254 238 ILE A CA  
1852 C C   . ILE A 234 ? 0.96052 1.10178 1.39328 0.28395  -0.18074 -0.06293 238 ILE A C   
1853 O O   . ILE A 234 ? 1.02054 1.11263 1.43248 0.29698  -0.20392 -0.04634 238 ILE A O   
1854 C CB  . ILE A 234 ? 0.95662 1.07790 1.38036 0.26935  -0.14409 -0.08359 238 ILE A CB  
1855 C CG1 . ILE A 234 ? 0.89843 1.08079 1.37106 0.28083  -0.13259 -0.11523 238 ILE A CG1 
1856 C CG2 . ILE A 234 ? 0.90184 0.99798 1.29190 0.24433  -0.12421 -0.07767 238 ILE A CG2 
1857 C CD1 . ILE A 234 ? 0.90562 1.07944 1.39437 0.29469  -0.12362 -0.13957 238 ILE A CD1 
1858 N N   . GLU A 235 ? 0.93297 1.13577 1.40822 0.29123  -0.17948 -0.08175 239 GLU A N   
1859 C CA  . GLU A 235 ? 1.04151 1.25844 1.54244 0.31615  -0.20828 -0.08333 239 GLU A CA  
1860 C C   . GLU A 235 ? 1.06403 1.25017 1.52420 0.30764  -0.22707 -0.05325 239 GLU A C   
1861 O O   . GLU A 235 ? 1.07265 1.22448 1.52297 0.32828  -0.25678 -0.04164 239 GLU A O   
1862 C CB  . GLU A 235 ? 1.04217 1.33754 1.59660 0.31873  -0.20045 -0.10901 239 GLU A CB  
1863 C CG  . GLU A 235 ? 1.38762 1.70570 1.98233 0.35017  -0.23159 -0.11878 239 GLU A CG  
1864 C CD  . GLU A 235 ? 1.51838 1.91900 2.16791 0.34846  -0.22388 -0.14374 239 GLU A CD  
1865 O OE1 . GLU A 235 ? 1.40126 1.83764 2.05287 0.32087  -0.19278 -0.15185 239 GLU A OE1 
1866 O OE2 . GLU A 235 ? 1.40147 1.82987 2.09187 0.37465  -0.24991 -0.15548 239 GLU A OE2 
1867 N N   . GLN A 236 ? 0.96033 1.15534 1.39353 0.27738  -0.21023 -0.04052 240 GLN A N   
1868 C CA  . GLN A 236 ? 0.95912 1.13665 1.35740 0.26699  -0.22417 -0.01645 240 GLN A CA  
1869 C C   . GLN A 236 ? 0.99164 1.10005 1.33384 0.25587  -0.22598 0.01020  240 GLN A C   
1870 O O   . GLN A 236 ? 1.04846 1.12236 1.35965 0.25984  -0.24721 0.03012  240 GLN A O   
1871 C CB  . GLN A 236 ? 0.95984 1.18284 1.35984 0.24086  -0.20556 -0.01838 240 GLN A CB  
1872 C CG  . GLN A 236 ? 1.08972 1.38341 1.54479 0.24686  -0.20146 -0.04483 240 GLN A CG  
1873 C CD  . GLN A 236 ? 1.18389 1.51035 1.64286 0.23901  -0.21223 -0.04123 240 GLN A CD  
1874 O OE1 . GLN A 236 ? 1.22077 1.56760 1.70618 0.25950  -0.23762 -0.04772 240 GLN A OE1 
1875 N NE2 . GLN A 236 ? 1.06397 1.39531 1.49734 0.21002  -0.19437 -0.03204 240 GLN A NE2 
1876 N N   . LEU A 237 ? 0.99603 1.08398 1.32395 0.24104  -0.20407 0.01022  241 LEU A N   
1877 C CA  . LEU A 237 ? 0.90393 0.93221 1.18411 0.22669  -0.20151 0.03230  241 LEU A CA  
1878 C C   . LEU A 237 ? 1.00638 0.98417 1.28128 0.24231  -0.21004 0.03208  241 LEU A C   
1879 O O   . LEU A 237 ? 1.14317 1.06394 1.37853 0.23690  -0.21785 0.05261  241 LEU A O   
1880 C CB  . LEU A 237 ? 0.93361 0.97174 1.20029 0.19761  -0.17318 0.03309  241 LEU A CB  
1881 C CG  . LEU A 237 ? 0.87405 0.95692 1.14319 0.17988  -0.16227 0.03287  241 LEU A CG  
1882 C CD1 . LEU A 237 ? 0.76452 0.84830 1.01648 0.15371  -0.13829 0.03563  241 LEU A CD1 
1883 C CD2 . LEU A 237 ? 0.83517 0.90810 1.08111 0.17891  -0.17951 0.05042  241 LEU A CD2 
1884 N N   . GLY A 238 ? 1.01524 1.01073 1.32745 0.26038  -0.20792 0.00887  242 GLY A N   
1885 C CA  . GLY A 238 ? 1.00012 0.94592 1.30911 0.27766  -0.21803 0.00656  242 GLY A CA  
1886 C C   . GLY A 238 ? 1.04516 0.98409 1.35480 0.26520  -0.19473 -0.00549 242 GLY A C   
1887 O O   . GLY A 238 ? 1.09498 1.04729 1.39061 0.23890  -0.17355 -0.00226 242 GLY A O   
1888 N N   . THR A 239 ? 1.05002 0.96640 1.37572 0.28546  -0.20039 -0.02042 243 THR A N   
1889 C CA  . THR A 239 ? 1.05372 0.95571 1.37682 0.27580  -0.18195 -0.03271 243 THR A CA  
1890 C C   . THR A 239 ? 1.10092 0.95477 1.37893 0.24923  -0.17583 -0.00997 243 THR A C   
1891 O O   . THR A 239 ? 1.13637 0.94047 1.38510 0.24943  -0.19160 0.01184  243 THR A O   
1892 C CB  . THR A 239 ? 1.07220 0.94579 1.41488 0.30406  -0.19358 -0.05030 243 THR A CB  
1893 O OG1 . THR A 239 ? 1.11773 1.04616 1.50931 0.32667  -0.19342 -0.07752 243 THR A OG1 
1894 C CG2 . THR A 239 ? 1.04798 0.89316 1.37938 0.29277  -0.17796 -0.06026 243 THR A CG2 
1895 N N   . PRO A 240 ? 1.14622 1.01362 1.41681 0.22556  -0.15374 -0.01426 244 PRO A N   
1896 C CA  . PRO A 240 ? 1.08302 0.91455 1.31750 0.19924  -0.14710 0.00511  244 PRO A CA  
1897 C C   . PRO A 240 ? 1.18812 0.95980 1.40812 0.20012  -0.15146 0.00523  244 PRO A C   
1898 O O   . PRO A 240 ? 1.22184 0.98122 1.45942 0.22004  -0.15699 -0.01224 244 PRO A O   
1899 C CB  . PRO A 240 ? 0.99989 0.87344 1.23857 0.17825  -0.12489 -0.00367 244 PRO A CB  
1900 C CG  . PRO A 240 ? 0.92229 0.83078 1.19159 0.19264  -0.11789 -0.03059 244 PRO A CG  
1901 C CD  . PRO A 240 ? 1.12049 1.03896 1.41471 0.22100  -0.13398 -0.03722 244 PRO A CD  
1902 N N   . CYS A 241 ? 1.25892 0.99329 1.44709 0.17714  -0.14812 0.02420  245 CYS A N   
1903 C CA  . CYS A 241 ? 1.26152 0.93233 1.43085 0.17347  -0.15306 0.02858  245 CYS A CA  
1904 C C   . CYS A 241 ? 1.31213 0.98545 1.49656 0.17119  -0.14197 0.00528  245 CYS A C   
1905 O O   . CYS A 241 ? 1.29179 1.01123 1.48964 0.16192  -0.12695 -0.00786 245 CYS A O   
1906 C CB  . CYS A 241 ? 1.29218 0.93191 1.42707 0.14453  -0.14733 0.05186  245 CYS A CB  
1907 S SG  . CYS A 241 ? 1.60749 1.25268 1.71867 0.14057  -0.15506 0.07808  245 CYS A SG  
1908 N N   . PRO A 242 ? 1.38681 1.00754 1.56610 0.17922  -0.14999 -0.00023 246 PRO A N   
1909 C CA  . PRO A 242 ? 1.40001 1.02093 1.59181 0.17755  -0.14051 -0.02453 246 PRO A CA  
1910 C C   . PRO A 242 ? 1.38343 1.01547 1.56542 0.14630  -0.12423 -0.02452 246 PRO A C   
1911 O O   . PRO A 242 ? 1.34701 0.99982 1.54049 0.14391  -0.11487 -0.04575 246 PRO A O   
1912 C CB  . PRO A 242 ? 1.37548 0.92703 1.55785 0.18983  -0.15454 -0.02596 246 PRO A CB  
1913 C CG  . PRO A 242 ? 1.41259 0.92115 1.57038 0.19244  -0.17033 0.00169  246 PRO A CG  
1914 C CD  . PRO A 242 ? 1.39702 0.95359 1.55691 0.19178  -0.16965 0.01479  246 PRO A CD  
1915 N N   . GLU A 243 ? 1.51051 1.13077 1.67187 0.12260  -0.12079 -0.00281 247 GLU A N   
1916 C CA  . GLU A 243 ? 1.44339 1.08379 1.60268 0.09542  -0.10642 -0.00534 247 GLU A CA  
1917 C C   . GLU A 243 ? 1.38460 1.08966 1.55889 0.09542  -0.09669 -0.01428 247 GLU A C   
1918 O O   . GLU A 243 ? 1.45817 1.18439 1.63796 0.08491  -0.08803 -0.02827 247 GLU A O   
1919 C CB  . GLU A 243 ? 1.62968 1.24809 1.76752 0.07045  -0.10305 0.01764  247 GLU A CB  
1920 C CG  . GLU A 243 ? 1.76350 1.37365 1.90049 0.04397  -0.09329 0.01146  247 GLU A CG  
1921 C CD  . GLU A 243 ? 1.84640 1.39828 1.97619 0.04165  -0.09884 0.00526  247 GLU A CD  
1922 O OE1 . GLU A 243 ? 1.77975 1.32336 1.91989 0.06051  -0.10472 -0.01337 247 GLU A OE1 
1923 O OE2 . GLU A 243 ? 1.85839 1.37237 1.97186 0.01956  -0.09609 0.01798  247 GLU A OE2 
1924 N N   . PHE A 244 ? 1.23427 0.96892 1.41335 0.10664  -0.09909 -0.00640 248 PHE A N   
1925 C CA  . PHE A 244 ? 1.11602 0.90769 1.30827 0.10711  -0.08989 -0.01564 248 PHE A CA  
1926 C C   . PHE A 244 ? 1.11841 0.92809 1.32694 0.12112  -0.08614 -0.04136 248 PHE A C   
1927 O O   . PHE A 244 ? 1.06559 0.91283 1.27790 0.11474  -0.07575 -0.05168 248 PHE A O   
1928 C CB  . PHE A 244 ? 1.07064 0.88811 1.26641 0.11647  -0.09413 -0.00400 248 PHE A CB  
1929 C CG  . PHE A 244 ? 1.04936 0.92204 1.25833 0.11663  -0.08461 -0.01357 248 PHE A CG  
1930 C CD1 . PHE A 244 ? 0.97972 0.87657 1.18057 0.09750  -0.07563 -0.00569 248 PHE A CD1 
1931 C CD2 . PHE A 244 ? 0.90741 0.80716 1.13714 0.13531  -0.08394 -0.03132 248 PHE A CD2 
1932 C CE1 . PHE A 244 ? 0.89941 0.84088 1.10823 0.09636  -0.06729 -0.01318 248 PHE A CE1 
1933 C CE2 . PHE A 244 ? 0.88484 0.83298 1.12368 0.13198  -0.07316 -0.03968 248 PHE A CE2 
1934 C CZ  . PHE A 244 ? 0.88754 0.85378 1.11368 0.11209  -0.06539 -0.02943 248 PHE A CZ  
1935 N N   . MET A 245 ? 1.18001 0.96182 1.39629 0.14031  -0.09425 -0.05238 249 MET A N   
1936 C CA  . MET A 245 ? 1.13634 0.93550 1.36834 0.15428  -0.08890 -0.07957 249 MET A CA  
1937 C C   . MET A 245 ? 1.14527 0.93453 1.36736 0.13916  -0.08112 -0.09359 249 MET A C   
1938 O O   . MET A 245 ? 1.04656 0.86260 1.27359 0.14204  -0.07183 -0.11423 249 MET A O   
1939 C CB  . MET A 245 ? 1.31363 1.08367 1.55884 0.18100  -0.10079 -0.08949 249 MET A CB  
1940 C CG  . MET A 245 ? 1.28217 1.05821 1.53932 0.20077  -0.11343 -0.07863 249 MET A CG  
1941 S SD  . MET A 245 ? 1.27848 1.12769 1.56610 0.21432  -0.10502 -0.09419 249 MET A SD  
1942 C CE  . MET A 245 ? 1.17427 1.01241 1.47965 0.24421  -0.12795 -0.08662 249 MET A CE  
1943 N N   . LYS A 246 ? 1.16297 0.91409 1.37030 0.12222  -0.08472 -0.08368 250 LYS A N   
1944 C CA  . LYS A 246 ? 1.22250 0.96388 1.42219 0.10715  -0.08019 -0.09763 250 LYS A CA  
1945 C C   . LYS A 246 ? 1.17153 0.95774 1.36729 0.09366  -0.07043 -0.10186 250 LYS A C   
1946 O O   . LYS A 246 ? 1.08829 0.88138 1.27930 0.09052  -0.06628 -0.12090 250 LYS A O   
1947 C CB  . LYS A 246 ? 1.22966 0.92868 1.41800 0.08785  -0.08491 -0.08454 250 LYS A CB  
1948 C CG  . LYS A 246 ? 1.34820 0.99758 1.53183 0.09650  -0.09515 -0.07148 250 LYS A CG  
1949 C CD  . LYS A 246 ? 1.38275 1.00288 1.57321 0.11911  -0.10188 -0.09055 250 LYS A CD  
1950 C CE  . LYS A 246 ? 1.41676 0.97887 1.59658 0.10818  -0.10671 -0.09453 250 LYS A CE  
1951 N NZ  . LYS A 246 ? 1.46501 1.00571 1.65253 0.12828  -0.11062 -0.12032 250 LYS A NZ  
1952 N N   . LYS A 247 ? 1.09756 0.91100 1.29218 0.08554  -0.06772 -0.08423 251 LYS A N   
1953 C CA  . LYS A 247 ? 1.03271 0.88162 1.22110 0.07212  -0.06083 -0.08510 251 LYS A CA  
1954 C C   . LYS A 247 ? 0.96765 0.84847 1.15578 0.08144  -0.05295 -0.10186 251 LYS A C   
1955 O O   . LYS A 247 ? 1.07917 0.98079 1.25584 0.07080  -0.04831 -0.10586 251 LYS A O   
1956 C CB  . LYS A 247 ? 1.00497 0.87340 1.19308 0.06400  -0.05972 -0.06355 251 LYS A CB  
1957 C CG  . LYS A 247 ? 0.99466 0.83466 1.18054 0.05440  -0.06450 -0.04508 251 LYS A CG  
1958 C CD  . LYS A 247 ? 0.97147 0.83484 1.15632 0.05145  -0.06234 -0.02687 251 LYS A CD  
1959 C CE  . LYS A 247 ? 1.13045 0.96658 1.30820 0.04231  -0.06520 -0.00776 251 LYS A CE  
1960 N NZ  . LYS A 247 ? 0.96992 0.83391 1.14489 0.03395  -0.06070 0.00581  251 LYS A NZ  
1961 N N   . LEU A 248 ? 0.97955 0.86463 1.17962 0.10067  -0.05134 -0.11183 252 LEU A N   
1962 C CA  . LEU A 248 ? 0.97777 0.89616 1.17957 0.10797  -0.04053 -0.12905 252 LEU A CA  
1963 C C   . LEU A 248 ? 1.05191 0.96070 1.24146 0.10638  -0.03602 -0.15254 252 LEU A C   
1964 O O   . LEU A 248 ? 1.08205 0.95610 1.27062 0.10840  -0.04248 -0.16086 252 LEU A O   
1965 C CB  . LEU A 248 ? 1.03799 0.96849 1.26301 0.12980  -0.04045 -0.13445 252 LEU A CB  
1966 C CG  . LEU A 248 ? 1.07260 1.04446 1.30899 0.13233  -0.03532 -0.12654 252 LEU A CG  
1967 C CD1 . LEU A 248 ? 0.85689 0.82780 1.08871 0.12238  -0.04229 -0.09987 252 LEU A CD1 
1968 C CD2 . LEU A 248 ? 1.08330 1.06386 1.34798 0.15698  -0.03819 -0.13827 252 LEU A CD2 
1969 N N   . GLN A 249 ? 1.07542 1.01329 1.25231 0.10135  -0.02464 -0.16321 253 GLN A N   
1970 C CA  . GLN A 249 ? 1.10899 1.04210 1.27055 0.10132  -0.01807 -0.18782 253 GLN A CA  
1971 C C   . GLN A 249 ? 1.11363 1.04329 1.29558 0.12268  -0.01378 -0.20855 253 GLN A C   
1972 O O   . GLN A 249 ? 1.12503 1.07259 1.33172 0.13681  -0.01218 -0.20570 253 GLN A O   
1973 C CB  . GLN A 249 ? 1.09419 1.05777 1.23257 0.09003  -0.00576 -0.19177 253 GLN A CB  
1974 C CG  . GLN A 249 ? 1.29996 1.26479 1.41474 0.08845  0.00519  -0.21793 253 GLN A CG  
1975 C CD  . GLN A 249 ? 1.19614 1.17939 1.32783 0.10456  0.02035  -0.24137 253 GLN A CD  
1976 O OE1 . GLN A 249 ? 1.26805 1.26910 1.43171 0.11806  0.02243  -0.23846 253 GLN A OE1 
1977 N NE2 . GLN A 249 ? 0.92491 0.90508 1.03515 0.10319  0.03055  -0.26617 253 GLN A NE2 
1978 N N   . PRO A 250 ? 1.10474 1.01126 1.27817 0.12635  -0.01322 -0.23107 254 PRO A N   
1979 C CA  . PRO A 250 ? 1.14815 1.04814 1.34279 0.14880  -0.00989 -0.25385 254 PRO A CA  
1980 C C   . PRO A 250 ? 1.22749 1.16945 1.44626 0.16408  0.00302  -0.26442 254 PRO A C   
1981 O O   . PRO A 250 ? 1.20293 1.14279 1.45283 0.18441  -0.00374 -0.26426 254 PRO A O   
1982 C CB  . PRO A 250 ? 1.01519 0.89976 1.18618 0.14391  -0.00433 -0.27981 254 PRO A CB  
1983 C CG  . PRO A 250 ? 1.19693 1.05950 1.34161 0.12163  -0.01531 -0.26564 254 PRO A CG  
1984 C CD  . PRO A 250 ? 1.06426 0.94197 1.21337 0.11148  -0.02065 -0.23459 254 PRO A CD  
1985 N N   . THR A 251 ? 1.21229 1.19133 1.41751 0.15471  0.02097  -0.27461 255 THR A N   
1986 C CA  . THR A 251 ? 1.16649 1.18860 1.39859 0.16755  0.03593  -0.28955 255 THR A CA  
1987 C C   . THR A 251 ? 1.14176 1.18728 1.39957 0.17155  0.02967  -0.26740 255 THR A C   
1988 O O   . THR A 251 ? 1.12209 1.18511 1.41747 0.19221  0.02798  -0.27538 255 THR A O   
1989 C CB  . THR A 251 ? 1.06394 1.11776 1.27107 0.15256  0.05910  -0.30518 255 THR A CB  
1990 O OG1 . THR A 251 ? 1.25711 1.33229 1.44873 0.13380  0.06244  -0.28264 255 THR A OG1 
1991 C CG2 . THR A 251 ? 1.08456 1.11056 1.25154 0.14170  0.06189  -0.31997 255 THR A CG2 
1992 N N   . VAL A 252 ? 1.15494 1.20104 1.39377 0.15305  0.02485  -0.24078 256 VAL A N   
1993 C CA  . VAL A 252 ? 1.13737 1.19888 1.39668 0.15603  0.01650  -0.21875 256 VAL A CA  
1994 C C   . VAL A 252 ? 1.12948 1.15917 1.41001 0.17452  -0.00305 -0.21060 256 VAL A C   
1995 O O   . VAL A 252 ? 1.08954 1.13415 1.39895 0.19007  -0.00980 -0.20657 256 VAL A O   
1996 C CB  . VAL A 252 ? 1.11782 1.17876 1.35040 0.13312  0.01401  -0.19314 256 VAL A CB  
1997 C CG1 . VAL A 252 ? 0.95199 1.02577 1.20265 0.13550  0.00515  -0.17110 256 VAL A CG1 
1998 C CG2 . VAL A 252 ? 1.12055 1.20696 1.32721 0.11535  0.03189  -0.20011 256 VAL A CG2 
1999 N N   . ARG A 253 ? 1.20106 1.18475 1.46637 0.17294  -0.01298 -0.20925 257 ARG A N   
2000 C CA  . ARG A 253 ? 1.20154 1.14523 1.47932 0.18745  -0.03120 -0.20024 257 ARG A CA  
2001 C C   . ARG A 253 ? 1.24315 1.18985 1.55307 0.21646  -0.03380 -0.22115 257 ARG A C   
2002 O O   . ARG A 253 ? 1.21756 1.15761 1.54790 0.23317  -0.04783 -0.21090 257 ARG A O   
2003 C CB  . ARG A 253 ? 1.12577 1.02069 1.38060 0.17657  -0.03839 -0.19835 257 ARG A CB  
2004 C CG  . ARG A 253 ? 1.17142 1.02116 1.42662 0.17909  -0.05596 -0.17807 257 ARG A CG  
2005 C CD  . ARG A 253 ? 1.12874 0.93103 1.36675 0.16930  -0.06115 -0.18289 257 ARG A CD  
2006 N NE  . ARG A 253 ? 1.24795 1.00287 1.48366 0.16942  -0.07599 -0.16359 257 ARG A NE  
2007 C CZ  . ARG A 253 ? 1.37992 1.09087 1.62202 0.18615  -0.08648 -0.17027 257 ARG A CZ  
2008 N NH1 . ARG A 253 ? 1.43294 1.14327 1.68857 0.20630  -0.08413 -0.19774 257 ARG A NH1 
2009 N NH2 . ARG A 253 ? 1.35025 1.01464 1.58344 0.18245  -0.09922 -0.14934 257 ARG A NH2 
2010 N N   . THR A 254 ? 1.30936 1.26692 1.62405 0.22372  -0.02093 -0.25159 258 THR A N   
2011 C CA  . THR A 254 ? 1.48720 1.44860 1.83680 0.25354  -0.02339 -0.27503 258 THR A CA  
2012 C C   . THR A 254 ? 1.42136 1.43212 1.80613 0.26675  -0.02235 -0.27463 258 THR A C   
2013 O O   . THR A 254 ? 1.49078 1.49564 1.90653 0.29288  -0.03723 -0.27762 258 THR A O   
2014 C CB  . THR A 254 ? 1.47882 1.44862 1.82719 0.25765  -0.00617 -0.31098 258 THR A CB  
2015 O OG1 . THR A 254 ? 1.56450 1.58723 1.90778 0.24356  0.01704  -0.32175 258 THR A OG1 
2016 C CG2 . THR A 254 ? 1.48608 1.40664 1.79997 0.24470  -0.00923 -0.31383 258 THR A CG2 
2017 N N   . TYR A 255 ? 1.30499 1.36296 1.68516 0.24897  -0.00652 -0.27088 259 TYR A N   
2018 C CA  . TYR A 255 ? 1.32320 1.43247 1.73917 0.25896  -0.00396 -0.27368 259 TYR A CA  
2019 C C   . TYR A 255 ? 1.26649 1.36369 1.68941 0.26428  -0.02641 -0.24439 259 TYR A C   
2020 O O   . TYR A 255 ? 1.22504 1.34595 1.68464 0.28492  -0.03616 -0.24868 259 TYR A O   
2021 C CB  . TYR A 255 ? 1.28106 1.43879 1.68622 0.23535  0.01964  -0.27670 259 TYR A CB  
2022 C CG  . TYR A 255 ? 1.24278 1.45167 1.68257 0.24009  0.02095  -0.27526 259 TYR A CG  
2023 C CD1 . TYR A 255 ? 1.24307 1.49057 1.73180 0.26333  0.02464  -0.30238 259 TYR A CD1 
2024 C CD2 . TYR A 255 ? 1.18243 1.40219 1.60886 0.22201  0.01772  -0.24875 259 TYR A CD2 
2025 C CE1 . TYR A 255 ? 1.17663 1.47424 1.70100 0.26716  0.02456  -0.30306 259 TYR A CE1 
2026 C CE2 . TYR A 255 ? 1.21783 1.48402 1.67603 0.22519  0.01802  -0.24871 259 TYR A CE2 
2027 C CZ  . TYR A 255 ? 1.17261 1.47877 1.68042 0.24724  0.02117  -0.27594 259 TYR A CZ  
2028 O OH  . TYR A 255 ? 1.01582 1.37166 1.55908 0.24982  0.02033  -0.27781 259 TYR A OH  
2029 N N   . VAL A 256 ? 1.26816 1.33074 1.65651 0.24568  -0.03474 -0.21585 260 VAL A N   
2030 C CA  . VAL A 256 ? 1.19673 1.24470 1.58406 0.24736  -0.05394 -0.18743 260 VAL A CA  
2031 C C   . VAL A 256 ? 1.20855 1.20905 1.60470 0.27154  -0.07699 -0.18378 260 VAL A C   
2032 O O   . VAL A 256 ? 1.19386 1.19321 1.60361 0.28558  -0.09458 -0.17097 260 VAL A O   
2033 C CB  . VAL A 256 ? 1.06513 1.09371 1.41375 0.21879  -0.05239 -0.16137 260 VAL A CB  
2034 C CG1 . VAL A 256 ? 0.95680 0.95122 1.29534 0.21977  -0.07227 -0.13316 260 VAL A CG1 
2035 C CG2 . VAL A 256 ? 1.04945 1.12519 1.39222 0.19878  -0.03564 -0.15920 260 VAL A CG2 
2036 N N   . GLU A 257 ? 1.22058 1.17841 1.60660 0.27652  -0.07852 -0.19471 261 GLU A N   
2037 C CA  . GLU A 257 ? 1.27003 1.17573 1.66143 0.29936  -0.10024 -0.19235 261 GLU A CA  
2038 C C   . GLU A 257 ? 1.25116 1.17757 1.68628 0.33397  -0.10673 -0.21813 261 GLU A C   
2039 O O   . GLU A 257 ? 1.25182 1.14050 1.69572 0.35755  -0.12972 -0.21292 261 GLU A O   
2040 C CB  . GLU A 257 ? 1.24337 1.09477 1.60933 0.29105  -0.09932 -0.19673 261 GLU A CB  
2041 C CG  . GLU A 257 ? 1.27848 1.09298 1.60685 0.26369  -0.10278 -0.16774 261 GLU A CG  
2042 C CD  . GLU A 257 ? 1.35987 1.13081 1.66666 0.25140  -0.09934 -0.17579 261 GLU A CD  
2043 O OE1 . GLU A 257 ? 1.38925 1.16136 1.70606 0.26213  -0.09225 -0.20446 261 GLU A OE1 
2044 O OE2 . GLU A 257 ? 1.35369 1.09095 1.63438 0.23017  -0.10315 -0.15489 261 GLU A OE2 
2045 N N   . ASN A 258 ? 1.23455 1.21866 1.69649 0.33731  -0.08704 -0.24624 262 ASN A N   
2046 C CA  . ASN A 258 ? 1.23091 1.24726 1.74180 0.36913  -0.08921 -0.27578 262 ASN A CA  
2047 C C   . ASN A 258 ? 1.24326 1.31033 1.78758 0.37913  -0.09698 -0.27097 262 ASN A C   
2048 O O   . ASN A 258 ? 1.23340 1.33272 1.82514 0.40728  -0.10188 -0.29520 262 ASN A O   
2049 C CB  . ASN A 258 ? 1.23748 1.29390 1.76096 0.36542  -0.06068 -0.31150 262 ASN A CB  
2050 C CG  . ASN A 258 ? 1.41944 1.42865 1.92958 0.37270  -0.05908 -0.33002 262 ASN A CG  
2051 O OD1 . ASN A 258 ? 1.44300 1.38723 1.93156 0.37628  -0.07799 -0.31429 262 ASN A OD1 
2052 N ND2 . ASN A 258 ? 1.45570 1.49607 1.97693 0.37355  -0.03561 -0.36445 262 ASN A ND2 
2053 N N   . ARG A 259 ? 1.17391 1.25138 1.69709 0.35691  -0.09802 -0.24279 263 ARG A N   
2054 C CA  . ARG A 259 ? 1.14999 1.27041 1.70148 0.36517  -0.10832 -0.23668 263 ARG A CA  
2055 C C   . ARG A 259 ? 1.22591 1.30823 1.78867 0.39527  -0.14277 -0.22577 263 ARG A C   
2056 O O   . ARG A 259 ? 1.30539 1.31927 1.83855 0.39935  -0.15779 -0.21071 263 ARG A O   
2057 C CB  . ARG A 259 ? 1.17512 1.30672 1.69594 0.33407  -0.10272 -0.20829 263 ARG A CB  
2058 C CG  . ARG A 259 ? 1.15924 1.32317 1.66340 0.30383  -0.07192 -0.21511 263 ARG A CG  
2059 C CD  . ARG A 259 ? 1.17561 1.39901 1.71828 0.31027  -0.05062 -0.25073 263 ARG A CD  
2060 N NE  . ARG A 259 ? 1.11352 1.39186 1.70002 0.32156  -0.05566 -0.25817 263 ARG A NE  
2061 C CZ  . ARG A 259 ? 1.09030 1.40499 1.72948 0.34848  -0.05792 -0.28730 263 ARG A CZ  
2062 N NH1 . ARG A 259 ? 1.12031 1.42081 1.77453 0.36842  -0.05499 -0.31240 263 ARG A NH1 
2063 N NH2 . ARG A 259 ? 0.92493 1.29247 1.60486 0.35610  -0.06395 -0.29298 263 ARG A NH2 
2064 N N   . PRO A 260 ? 1.20408 1.32802 1.80889 0.41660  -0.15660 -0.23386 264 PRO A N   
2065 C CA  . PRO A 260 ? 1.27244 1.35796 1.88069 0.44379  -0.19336 -0.21852 264 PRO A CA  
2066 C C   . PRO A 260 ? 1.22195 1.25788 1.77503 0.42235  -0.20537 -0.17694 264 PRO A C   
2067 O O   . PRO A 260 ? 1.22008 1.28320 1.75598 0.39500  -0.19311 -0.16196 264 PRO A O   
2068 C CB  . PRO A 260 ? 1.26164 1.41695 1.92447 0.46205  -0.20190 -0.23445 264 PRO A CB  
2069 C CG  . PRO A 260 ? 1.17921 1.40330 1.87811 0.45360  -0.16855 -0.26856 264 PRO A CG  
2070 C CD  . PRO A 260 ? 1.13810 1.34561 1.78914 0.41635  -0.14011 -0.25810 264 PRO A CD  
2071 N N   . LYS A 261 ? 1.28049 1.24157 1.80472 0.43416  -0.22849 -0.15909 265 LYS A N   
2072 C CA  . LYS A 261 ? 1.27363 1.18198 1.74278 0.41305  -0.23828 -0.12061 265 LYS A CA  
2073 C C   . LYS A 261 ? 1.28217 1.20664 1.75330 0.42082  -0.26096 -0.10320 265 LYS A C   
2074 O O   . LYS A 261 ? 1.32618 1.21942 1.80152 0.44918  -0.29216 -0.09776 265 LYS A O   
2075 C CB  . LYS A 261 ? 1.32552 1.14626 1.76159 0.42132  -0.25450 -0.10794 265 LYS A CB  
2076 C CG  . LYS A 261 ? 1.41180 1.20441 1.82720 0.40102  -0.23200 -0.11462 265 LYS A CG  
2077 C CD  . LYS A 261 ? 1.43576 1.25309 1.89137 0.42035  -0.22079 -0.15320 265 LYS A CD  
2078 C CE  . LYS A 261 ? 1.44910 1.22761 1.87965 0.40279  -0.20409 -0.15940 265 LYS A CE  
2079 N NZ  . LYS A 261 ? 1.42534 1.23291 1.89109 0.41823  -0.18944 -0.19872 265 LYS A NZ  
2080 N N   . TYR A 262 ? 1.22796 1.19819 1.69375 0.39605  -0.24706 -0.09437 266 TYR A N   
2081 C CA  . TYR A 262 ? 1.18042 1.16099 1.63881 0.39776  -0.26739 -0.07535 266 TYR A CA  
2082 C C   . TYR A 262 ? 1.19744 1.10977 1.59277 0.38020  -0.27753 -0.03853 266 TYR A C   
2083 O O   . TYR A 262 ? 1.22407 1.09958 1.58477 0.35696  -0.26093 -0.02769 266 TYR A O   
2084 C CB  . TYR A 262 ? 1.10101 1.15490 1.57763 0.37732  -0.24846 -0.08140 266 TYR A CB  
2085 C CG  . TYR A 262 ? 1.09947 1.22462 1.63527 0.38791  -0.23337 -0.11724 266 TYR A CG  
2086 C CD1 . TYR A 262 ? 1.07827 1.24175 1.66528 0.41885  -0.25310 -0.13652 266 TYR A CD1 
2087 C CD2 . TYR A 262 ? 1.06219 1.21747 1.60227 0.36623  -0.19931 -0.13247 266 TYR A CD2 
2088 C CE1 . TYR A 262 ? 1.07881 1.31164 1.72280 0.42641  -0.23614 -0.17155 266 TYR A CE1 
2089 C CE2 . TYR A 262 ? 1.10110 1.32019 1.69069 0.37270  -0.18242 -0.16524 266 TYR A CE2 
2090 C CZ  . TYR A 262 ? 1.05705 1.31639 1.69996 0.40192  -0.19928 -0.18539 266 TYR A CZ  
2091 O OH  . TYR A 262 ? 1.13065 1.45712 1.82507 0.40601  -0.17909 -0.22010 266 TYR A OH  
2092 N N   . ALA A 263 ? 1.22890 1.12651 1.60954 0.39067  -0.30497 -0.02026 267 ALA A N   
2093 C CA  . ALA A 263 ? 1.20768 1.03868 1.52591 0.37567  -0.31629 0.01450  267 ALA A CA  
2094 C C   . ALA A 263 ? 1.22309 1.07835 1.51430 0.34392  -0.30254 0.03181  267 ALA A C   
2095 O O   . ALA A 263 ? 1.25901 1.06781 1.49908 0.32042  -0.29681 0.05633  267 ALA A O   
2096 C CB  . ALA A 263 ? 1.19259 0.98135 1.49945 0.40570  -0.35678 0.02683  267 ALA A CB  
2097 N N   . GLY A 264 ? 1.20782 1.13445 1.53297 0.34198  -0.29630 0.01840  268 GLY A N   
2098 C CA  . GLY A 264 ? 1.14884 1.09743 1.45003 0.31462  -0.28582 0.03309  268 GLY A CA  
2099 C C   . GLY A 264 ? 1.21631 1.14458 1.49159 0.32376  -0.31586 0.05248  268 GLY A C   
2100 O O   . GLY A 264 ? 1.23411 1.10938 1.49028 0.34447  -0.34293 0.06356  268 GLY A O   
2101 N N   . TYR A 265 ? 1.20336 1.17047 1.47536 0.30897  -0.31294 0.05656  269 TYR A N   
2102 C CA  . TYR A 265 ? 1.26656 1.21321 1.50699 0.31446  -0.34087 0.07554  269 TYR A CA  
2103 C C   . TYR A 265 ? 1.26428 1.17185 1.44184 0.28326  -0.32899 0.10231  269 TYR A C   
2104 O O   . TYR A 265 ? 1.22151 1.13467 1.39015 0.25682  -0.29861 0.10299  269 TYR A O   
2105 C CB  . TYR A 265 ? 1.25064 1.26679 1.53052 0.32137  -0.35038 0.06029  269 TYR A CB  
2106 C CG  . TYR A 265 ? 1.28408 1.35075 1.63347 0.34910  -0.35725 0.02976  269 TYR A CG  
2107 C CD1 . TYR A 265 ? 1.25910 1.38745 1.65474 0.33888  -0.32813 0.00489  269 TYR A CD1 
2108 C CD2 . TYR A 265 ? 1.30914 1.36195 1.67736 0.38541  -0.39285 0.02506  269 TYR A CD2 
2109 C CE1 . TYR A 265 ? 1.23486 1.41262 1.69466 0.36219  -0.33100 -0.02507 269 TYR A CE1 
2110 C CE2 . TYR A 265 ? 1.37879 1.48240 1.81571 0.41166  -0.39808 -0.00587 269 TYR A CE2 
2111 C CZ  . TYR A 265 ? 1.38107 1.54893 1.86439 0.39904  -0.36553 -0.03158 269 TYR A CZ  
2112 O OH  . TYR A 265 ? 1.29462 1.51577 1.84722 0.42379  -0.36794 -0.06445 269 TYR A OH  
2113 N N   . SER A 266 ? 1.24937 1.11701 1.38275 0.28726  -0.35414 0.12364  270 SER A N   
2114 C CA  . SER A 266 ? 1.34282 1.18077 1.41732 0.25804  -0.34363 0.14686  270 SER A CA  
2115 C C   . SER A 266 ? 1.31512 1.21483 1.40555 0.23646  -0.32273 0.13752  270 SER A C   
2116 O O   . SER A 266 ? 1.21977 1.18194 1.36141 0.24501  -0.32218 0.11606  270 SER A O   
2117 C CB  . SER A 266 ? 1.41051 1.20112 1.43531 0.26814  -0.37693 0.16880  270 SER A CB  
2118 O OG  . SER A 266 ? 1.60736 1.36789 1.57217 0.23845  -0.36409 0.19019  270 SER A OG  
2119 N N   . PHE A 267 ? 1.29310 1.17421 1.33927 0.20733  -0.30444 0.15301  271 PHE A N   
2120 C CA  . PHE A 267 ? 1.22545 1.15680 1.28023 0.18782  -0.28784 0.14588  271 PHE A CA  
2121 C C   . PHE A 267 ? 1.31529 1.25672 1.35107 0.19159  -0.31105 0.15184  271 PHE A C   
2122 O O   . PHE A 267 ? 1.22030 1.21031 1.27340 0.18101  -0.30319 0.14137  271 PHE A O   
2123 C CB  . PHE A 267 ? 1.25591 1.16982 1.27877 0.15671  -0.25774 0.15558  271 PHE A CB  
2124 C CG  . PHE A 267 ? 1.08792 1.02652 1.14554 0.14832  -0.23102 0.14076  271 PHE A CG  
2125 C CD1 . PHE A 267 ? 0.96411 0.95840 1.05427 0.13927  -0.21483 0.12462  271 PHE A CD1 
2126 C CD2 . PHE A 267 ? 1.02572 0.92966 1.08248 0.15021  -0.22402 0.14238  271 PHE A CD2 
2127 C CE1 . PHE A 267 ? 0.96541 0.97837 1.08220 0.13224  -0.19256 0.11191  271 PHE A CE1 
2128 C CE2 . PHE A 267 ? 1.02524 0.95082 1.11123 0.14308  -0.20177 0.12817  271 PHE A CE2 
2129 C CZ  . PHE A 267 ? 0.98468 0.96434 1.09938 0.13454  -0.18644 0.11336  271 PHE A CZ  
2130 N N   . GLU A 268 ? 1.40834 1.30138 1.40579 0.20571  -0.34016 0.16867  272 GLU A N   
2131 C CA  . GLU A 268 ? 1.38666 1.29046 1.37246 0.21714  -0.37064 0.17140  272 GLU A CA  
2132 C C   . GLU A 268 ? 1.31677 1.27663 1.36997 0.24439  -0.38988 0.14767  272 GLU A C   
2133 O O   . GLU A 268 ? 1.28737 1.29778 1.36356 0.24400  -0.39760 0.13573  272 GLU A O   
2134 C CB  . GLU A 268 ? 1.47104 1.30124 1.39407 0.22675  -0.39892 0.19671  272 GLU A CB  
2135 C CG  . GLU A 268 ? 1.62553 1.39200 1.47734 0.19918  -0.37979 0.22141  272 GLU A CG  
2136 C CD  . GLU A 268 ? 1.75240 1.49772 1.61300 0.18728  -0.35016 0.22117  272 GLU A CD  
2137 O OE1 . GLU A 268 ? 1.65900 1.44118 1.57838 0.19723  -0.34002 0.20140  272 GLU A OE1 
2138 O OE2 . GLU A 268 ? 1.86472 1.55652 1.67217 0.16652  -0.33641 0.24009  272 GLU A OE2 
2139 N N   . LYS A 269 ? 1.37978 1.33293 1.46739 0.26735  -0.39648 0.13869  273 LYS A N   
2140 C CA  . LYS A 269 ? 1.33001 1.34056 1.48837 0.29328  -0.41042 0.11242  273 LYS A CA  
2141 C C   . LYS A 269 ? 1.28208 1.36441 1.49182 0.27698  -0.37923 0.08892  273 LYS A C   
2142 O O   . LYS A 269 ? 1.33207 1.47482 1.59724 0.28957  -0.38756 0.06648  273 LYS A O   
2143 C CB  . LYS A 269 ? 1.35086 1.33211 1.53035 0.32033  -0.42093 0.10753  273 LYS A CB  
2144 C CG  . LYS A 269 ? 1.50194 1.51040 1.73105 0.35894  -0.45659 0.09027  273 LYS A CG  
2145 C CD  . LYS A 269 ? 1.51055 1.60652 1.82112 0.36414  -0.44202 0.05568  273 LYS A CD  
2146 C CE  . LYS A 269 ? 1.43284 1.55956 1.79964 0.40400  -0.47671 0.03535  273 LYS A CE  
2147 N NZ  . LYS A 269 ? 1.37529 1.59073 1.82202 0.40591  -0.45953 0.00019  273 LYS A NZ  
2148 N N   . LEU A 270 ? 1.18310 1.25988 1.37535 0.24876  -0.34414 0.09326  274 LEU A N   
2149 C CA  . LEU A 270 ? 1.12765 1.26343 1.36085 0.23261  -0.31522 0.07338  274 LEU A CA  
2150 C C   . LEU A 270 ? 1.10197 1.26544 1.32086 0.20943  -0.30762 0.07508  274 LEU A C   
2151 O O   . LEU A 270 ? 1.02490 1.24246 1.28161 0.19927  -0.29146 0.05693  274 LEU A O   
2152 C CB  . LEU A 270 ? 1.08225 1.19893 1.30842 0.21683  -0.28321 0.07458  274 LEU A CB  
2153 C CG  . LEU A 270 ? 1.07487 1.18757 1.33436 0.23572  -0.28073 0.06145  274 LEU A CG  
2154 C CD1 . LEU A 270 ? 0.97759 1.06039 1.21688 0.21802  -0.25365 0.06713  274 LEU A CD1 
2155 C CD2 . LEU A 270 ? 1.12192 1.30229 1.44614 0.24589  -0.27539 0.03238  274 LEU A CD2 
2156 N N   . PHE A 271 ? 1.15956 1.28457 1.32231 0.19973  -0.31774 0.09602  275 PHE A N   
2157 C CA  . PHE A 271 ? 1.09507 1.23961 1.23806 0.17765  -0.31089 0.09783  275 PHE A CA  
2158 C C   . PHE A 271 ? 1.20491 1.31615 1.29843 0.18199  -0.33955 0.11498  275 PHE A C   
2159 O O   . PHE A 271 ? 1.22465 1.29647 1.26155 0.16378  -0.33120 0.13287  275 PHE A O   
2160 C CB  . PHE A 271 ? 1.01673 1.14546 1.13246 0.14939  -0.27693 0.10513  275 PHE A CB  
2161 C CG  . PHE A 271 ? 0.98131 1.13420 1.13462 0.14358  -0.24999 0.09117  275 PHE A CG  
2162 C CD1 . PHE A 271 ? 0.92656 1.13449 1.12098 0.13619  -0.23751 0.07180  275 PHE A CD1 
2163 C CD2 . PHE A 271 ? 0.95401 1.07204 1.09715 0.14272  -0.23622 0.09778  275 PHE A CD2 
2164 C CE1 . PHE A 271 ? 0.87570 1.10175 1.09738 0.12953  -0.21290 0.06011  275 PHE A CE1 
2165 C CE2 . PHE A 271 ? 0.91844 1.05726 1.09168 0.13692  -0.21278 0.08477  275 PHE A CE2 
2166 C CZ  . PHE A 271 ? 0.89319 1.08506 1.10354 0.13052  -0.20126 0.06651  275 PHE A CZ  
2167 N N   . PRO A 272 ? 1.21358 1.34202 1.32684 0.20527  -0.37370 0.10869  276 PRO A N   
2168 C CA  . PRO A 272 ? 1.26718 1.35878 1.32819 0.21176  -0.40550 0.12601  276 PRO A CA  
2169 C C   . PRO A 272 ? 1.28671 1.39334 1.31839 0.18867  -0.40100 0.12740  276 PRO A C   
2170 O O   . PRO A 272 ? 1.25780 1.41234 1.32067 0.17219  -0.37998 0.11148  276 PRO A O   
2171 C CB  . PRO A 272 ? 1.27470 1.39270 1.37853 0.24506  -0.44402 0.11335  276 PRO A CB  
2172 C CG  . PRO A 272 ? 1.15291 1.32596 1.33449 0.25421  -0.42844 0.08747  276 PRO A CG  
2173 C CD  . PRO A 272 ? 1.16567 1.35386 1.35144 0.22488  -0.38422 0.08323  276 PRO A CD  
2174 N N   . ASP A 273 ? 1.32819 1.38948 1.29577 0.18788  -0.42237 0.14676  277 ASP A N   
2175 C CA  . ASP A 273 ? 1.42957 1.49451 1.35727 0.16552  -0.41848 0.14983  277 ASP A CA  
2176 C C   . ASP A 273 ? 1.39899 1.53228 1.37564 0.16503  -0.42685 0.12627  277 ASP A C   
2177 O O   . ASP A 273 ? 1.44026 1.59020 1.40269 0.14207  -0.41177 0.12148  277 ASP A O   
2178 C CB  . ASP A 273 ? 1.56983 1.57771 1.42274 0.16979  -0.44752 0.17223  277 ASP A CB  
2179 C CG  . ASP A 273 ? 1.63386 1.57006 1.43654 0.17014  -0.44223 0.19623  277 ASP A CG  
2180 O OD1 . ASP A 273 ? 1.72098 1.61336 1.45679 0.14819  -0.42799 0.21348  277 ASP A OD1 
2181 O OD2 . ASP A 273 ? 1.62881 1.55238 1.45889 0.19163  -0.45186 0.19674  277 ASP A OD2 
2182 N N   . VAL A 274 ? 1.34071 1.51447 1.37667 0.18955  -0.45020 0.10997  278 VAL A N   
2183 C CA  . VAL A 274 ? 1.32155 1.56200 1.40649 0.18892  -0.46107 0.08647  278 VAL A CA  
2184 C C   . VAL A 274 ? 1.22966 1.51270 1.34913 0.16337  -0.42181 0.07045  278 VAL A C   
2185 O O   . VAL A 274 ? 1.24211 1.55932 1.36901 0.14728  -0.42006 0.05858  278 VAL A O   
2186 C CB  . VAL A 274 ? 1.26584 1.54479 1.41532 0.22083  -0.49044 0.06973  278 VAL A CB  
2187 C CG1 . VAL A 274 ? 1.15444 1.50226 1.35194 0.21921  -0.50595 0.04543  278 VAL A CG1 
2188 C CG2 . VAL A 274 ? 1.29072 1.51596 1.40223 0.24854  -0.52902 0.08818  278 VAL A CG2 
2189 N N   . LEU A 275 ? 1.20707 1.48701 1.34720 0.15938  -0.39129 0.06938  279 LEU A N   
2190 C CA  . LEU A 275 ? 1.16050 1.47535 1.32911 0.13607  -0.35574 0.05560  279 LEU A CA  
2191 C C   . LEU A 275 ? 1.19569 1.48220 1.31141 0.10882  -0.33404 0.06691  279 LEU A C   
2192 O O   . LEU A 275 ? 1.16470 1.47873 1.29672 0.08858  -0.31131 0.05537  279 LEU A O   
2193 C CB  . LEU A 275 ? 1.11353 1.43102 1.31474 0.13971  -0.33099 0.05114  279 LEU A CB  
2194 C CG  . LEU A 275 ? 1.15970 1.50349 1.41604 0.16679  -0.34546 0.03765  279 LEU A CG  
2195 C CD1 . LEU A 275 ? 1.13273 1.44759 1.38938 0.17115  -0.32471 0.04340  279 LEU A CD1 
2196 C CD2 . LEU A 275 ? 0.87971 1.29587 1.20290 0.16397  -0.34085 0.00981  279 LEU A CD2 
2197 N N   . PHE A 276 ? 1.22957 1.45807 1.27968 0.10752  -0.33974 0.08947  280 PHE A N   
2198 C CA  . PHE A 276 ? 1.24169 1.44266 1.24089 0.08312  -0.31896 0.09904  280 PHE A CA  
2199 C C   . PHE A 276 ? 1.25221 1.45970 1.22206 0.07504  -0.33693 0.09665  280 PHE A C   
2200 O O   . PHE A 276 ? 1.37540 1.58386 1.33851 0.09077  -0.37140 0.09802  280 PHE A O   
2201 C CB  . PHE A 276 ? 1.25286 1.39247 1.19820 0.08239  -0.31259 0.12185  280 PHE A CB  
2202 C CG  . PHE A 276 ? 1.12864 1.25931 1.09433 0.08047  -0.28577 0.12321  280 PHE A CG  
2203 C CD1 . PHE A 276 ? 1.12198 1.25870 1.08996 0.05977  -0.25278 0.11884  280 PHE A CD1 
2204 C CD2 . PHE A 276 ? 1.18127 1.29686 1.16438 0.10038  -0.29521 0.12765  280 PHE A CD2 
2205 C CE1 . PHE A 276 ? 1.03835 1.16787 1.02487 0.05829  -0.23053 0.11919  280 PHE A CE1 
2206 C CE2 . PHE A 276 ? 1.19728 1.30469 1.19828 0.09788  -0.27122 0.12743  280 PHE A CE2 
2207 C CZ  . PHE A 276 ? 1.02150 1.13687 1.02391 0.07649  -0.23934 0.12330  280 PHE A CZ  
2208 N N   . PRO A 277 ? 1.29500 1.50516 1.24591 0.05156  -0.31557 0.09246  281 PRO A N   
2209 C CA  . PRO A 277 ? 1.33070 1.54542 1.25108 0.04211  -0.33088 0.08841  281 PRO A CA  
2210 C C   . PRO A 277 ? 1.55180 1.71436 1.40017 0.04471  -0.34732 0.10858  281 PRO A C   
2211 O O   . PRO A 277 ? 1.58856 1.70930 1.40944 0.05080  -0.34338 0.12630  281 PRO A O   
2212 C CB  . PRO A 277 ? 1.33104 1.55230 1.24707 0.01704  -0.29867 0.08001  281 PRO A CB  
2213 C CG  . PRO A 277 ? 1.28045 1.47215 1.18694 0.01361  -0.27094 0.09141  281 PRO A CG  
2214 C CD  . PRO A 277 ? 1.24248 1.44293 1.19014 0.03342  -0.27800 0.09299  281 PRO A CD  
2215 N N   . ALA A 278 ? 1.70343 1.86729 1.51878 0.03826  -0.36552 0.10529  282 ALA A N   
2216 C CA  . ALA A 278 ? 1.89625 2.00945 1.63278 0.03537  -0.37854 0.12322  282 ALA A CA  
2217 C C   . ALA A 278 ? 2.08017 2.14892 1.77461 0.02084  -0.34513 0.13828  282 ALA A C   
2218 O O   . ALA A 278 ? 1.88292 1.96329 1.59354 0.00459  -0.31135 0.13006  282 ALA A O   
2219 C CB  . ALA A 278 ? 1.84022 1.96416 1.54648 0.02176  -0.38940 0.11300  282 ALA A CB  
2220 N N   . ASP A 279 ? 2.12475 2.14240 1.76781 0.02735  -0.35554 0.15999  283 ASP A N   
2221 C CA  . ASP A 279 ? 2.03860 2.01480 1.64637 0.01388  -0.32482 0.17438  283 ASP A CA  
2222 C C   . ASP A 279 ? 2.12753 2.08712 1.67990 -0.01126 -0.30372 0.17377  283 ASP A C   
2223 O O   . ASP A 279 ? 2.23794 2.17674 1.73341 -0.01499 -0.32246 0.17909  283 ASP A O   
2224 C CB  . ASP A 279 ? 2.04658 1.96977 1.61366 0.02690  -0.34360 0.19788  283 ASP A CB  
2225 C CG  . ASP A 279 ? 1.99742 1.88490 1.54709 0.01524  -0.31233 0.21053  283 ASP A CG  
2226 O OD1 . ASP A 279 ? 2.07328 1.93828 1.57512 -0.00743 -0.28819 0.21504  283 ASP A OD1 
2227 O OD2 . ASP A 279 ? 1.93624 1.82091 1.52248 0.02785  -0.31065 0.21376  283 ASP A OD2 
2228 N N   . SER A 280 ? 2.10216 2.07050 1.67055 -0.02769 -0.26543 0.16635  284 SER A N   
2229 C CA  . SER A 280 ? 2.18247 2.14070 1.70789 -0.05057 -0.24170 0.16145  284 SER A CA  
2230 C C   . SER A 280 ? 2.33107 2.23380 1.77522 -0.06060 -0.24001 0.18124  284 SER A C   
2231 O O   . SER A 280 ? 2.31668 2.18385 1.74030 -0.05252 -0.24983 0.20043  284 SER A O   
2232 C CB  . SER A 280 ? 2.03771 2.01293 1.59924 -0.06290 -0.20239 0.15057  284 SER A CB  
2233 O OG  . SER A 280 ? 1.86494 1.88626 1.48950 -0.05877 -0.20063 0.13185  284 SER A OG  
2234 N N   . GLU A 281 ? 2.52391 2.41709 1.91870 -0.07934 -0.22710 0.17589  285 GLU A N   
2235 C CA  . GLU A 281 ? 2.60680 2.44946 1.92408 -0.09552 -0.21361 0.19186  285 GLU A CA  
2236 C C   . GLU A 281 ? 2.58513 2.42256 1.91433 -0.11094 -0.17084 0.19109  285 GLU A C   
2237 O O   . GLU A 281 ? 2.64004 2.43561 1.91459 -0.12489 -0.15598 0.20588  285 GLU A O   
2238 C CB  . GLU A 281 ? 2.65320 2.48769 1.90942 -0.11031 -0.21537 0.18472  285 GLU A CB  
2239 C CG  . GLU A 281 ? 2.58669 2.43168 1.83430 -0.09632 -0.25875 0.18201  285 GLU A CG  
2240 C CD  . GLU A 281 ? 2.64247 2.45534 1.86729 -0.07735 -0.29602 0.20442  285 GLU A CD  
2241 O OE1 . GLU A 281 ? 2.71423 2.47233 1.86313 -0.08485 -0.29829 0.22513  285 GLU A OE1 
2242 O OE2 . GLU A 281 ? 2.57635 2.41734 1.85886 -0.05506 -0.32248 0.20097  285 GLU A OE2 
2243 N N   . HIS A 282 ? 2.46396 2.34243 1.86242 -0.10938 -0.15159 0.17391  286 HIS A N   
2244 C CA  . HIS A 282 ? 2.39613 2.27527 1.81758 -0.12016 -0.11548 0.17160  286 HIS A CA  
2245 C C   . HIS A 282 ? 2.37715 2.22977 1.80436 -0.11310 -0.11845 0.19043  286 HIS A C   
2246 O O   . HIS A 282 ? 2.25730 2.12060 1.72515 -0.09346 -0.14000 0.19369  286 HIS A O   
2247 C CB  . HIS A 282 ? 2.23847 2.16480 1.73256 -0.11590 -0.10226 0.15043  286 HIS A CB  
2248 C CG  . HIS A 282 ? 2.26529 2.19773 1.77928 -0.12864 -0.06524 0.14214  286 HIS A CG  
2249 N ND1 . HIS A 282 ? 2.27796 2.22338 1.84556 -0.12214 -0.05513 0.14148  286 HIS A ND1 
2250 C CD2 . HIS A 282 ? 2.24682 2.17598 1.73602 -0.14686 -0.03665 0.13257  286 HIS A CD2 
2251 C CE1 . HIS A 282 ? 2.23233 2.18287 1.80880 -0.13525 -0.02388 0.13225  286 HIS A CE1 
2252 N NE2 . HIS A 282 ? 2.19619 2.13848 1.72799 -0.15005 -0.01134 0.12606  286 HIS A NE2 
2253 N N   . ASN A 283 ? 2.43985 2.25973 1.82994 -0.13039 -0.09412 0.20060  287 ASN A N   
2254 C CA  . ASN A 283 ? 2.34503 2.12774 1.72421 -0.12830 -0.09652 0.22062  287 ASN A CA  
2255 C C   . ASN A 283 ? 2.18501 1.99146 1.63719 -0.11720 -0.08973 0.21509  287 ASN A C   
2256 O O   . ASN A 283 ? 2.17677 1.95359 1.62592 -0.11421 -0.09261 0.22970  287 ASN A O   
2257 C CB  . ASN A 283 ? 2.38793 2.13246 1.70999 -0.15474 -0.06727 0.23025  287 ASN A CB  
2258 C CG  . ASN A 283 ? 2.48950 2.21070 1.73410 -0.16986 -0.06739 0.23344  287 ASN A CG  
2259 O OD1 . ASN A 283 ? 2.52524 2.21825 1.72190 -0.16130 -0.09910 0.24719  287 ASN A OD1 
2260 N ND2 . ASN A 283 ? 2.53232 2.26523 1.76396 -0.19196 -0.03236 0.21962  287 ASN A ND2 
2261 N N   . LYS A 284 ? 2.03660 1.89145 1.54992 -0.11180 -0.08120 0.19479  288 LYS A N   
2262 C CA  . LYS A 284 ? 1.91456 1.79209 1.49330 -0.10178 -0.07527 0.18859  288 LYS A CA  
2263 C C   . LYS A 284 ? 1.71045 1.62146 1.33912 -0.08023 -0.09876 0.18011  288 LYS A C   
2264 O O   . LYS A 284 ? 1.54662 1.46382 1.21556 -0.06753 -0.10423 0.18123  288 LYS A O   
2265 C CB  . LYS A 284 ? 1.89626 1.79944 1.50619 -0.11538 -0.04161 0.17202  288 LYS A CB  
2266 C CG  . LYS A 284 ? 1.92592 1.80423 1.49525 -0.13895 -0.01330 0.17613  288 LYS A CG  
2267 C CD  . LYS A 284 ? 1.76831 1.67761 1.37242 -0.15052 0.01837  0.15598  288 LYS A CD  
2268 C CE  . LYS A 284 ? 1.68736 1.61442 1.35161 -0.14435 0.02647  0.15048  288 LYS A CE  
2269 N NZ  . LYS A 284 ? 1.66938 1.62527 1.36773 -0.15380 0.05410  0.13085  288 LYS A NZ  
2270 N N   . LEU A 285 ? 1.72305 1.65591 1.34963 -0.07712 -0.11191 0.17059  289 LEU A N   
2271 C CA  . LEU A 285 ? 1.46490 1.43372 1.14045 -0.06031 -0.13145 0.16020  289 LEU A CA  
2272 C C   . LEU A 285 ? 1.50085 1.45785 1.16296 -0.04309 -0.16709 0.17097  289 LEU A C   
2273 O O   . LEU A 285 ? 1.50344 1.47732 1.16292 -0.03733 -0.18842 0.16504  289 LEU A O   
2274 C CB  . LEU A 285 ? 1.49161 1.49159 1.17753 -0.06757 -0.12596 0.14216  289 LEU A CB  
2275 C CG  . LEU A 285 ? 1.51299 1.52379 1.21205 -0.08201 -0.09363 0.12967  289 LEU A CG  
2276 C CD1 . LEU A 285 ? 1.43657 1.46355 1.12496 -0.09123 -0.08969 0.11409  289 LEU A CD1 
2277 C CD2 . LEU A 285 ? 1.21359 1.24744 0.97205 -0.07529 -0.08370 0.12206  289 LEU A CD2 
2278 N N   . LYS A 286 ? 1.53174 1.45906 1.18776 -0.03420 -0.17438 0.18595  290 LYS A N   
2279 C CA  . LYS A 286 ? 1.43375 1.34292 1.08063 -0.01431 -0.20831 0.19749  290 LYS A CA  
2280 C C   . LYS A 286 ? 1.28797 1.23140 1.00305 0.00603  -0.21930 0.18715  290 LYS A C   
2281 O O   . LYS A 286 ? 1.17157 1.13610 0.93015 0.00368  -0.19849 0.17776  290 LYS A O   
2282 C CB  . LYS A 286 ? 1.50859 1.36017 1.11008 -0.01624 -0.20867 0.21937  290 LYS A CB  
2283 C CG  . LYS A 286 ? 1.62969 1.43493 1.15133 -0.03521 -0.20254 0.23465  290 LYS A CG  
2284 C CD  . LYS A 286 ? 1.78931 1.59657 1.27347 -0.03341 -0.22576 0.23416  290 LYS A CD  
2285 C CE  . LYS A 286 ? 2.01469 1.81110 1.44624 -0.05939 -0.20236 0.23276  290 LYS A CE  
2286 N NZ  . LYS A 286 ? 2.17979 2.00016 1.59833 -0.05909 -0.21834 0.22140  290 LYS A NZ  
2287 N N   . ALA A 287 ? 1.33356 1.28050 1.05639 0.02679  -0.25292 0.18892  291 ALA A N   
2288 C CA  . ALA A 287 ? 1.22958 1.20041 1.01184 0.04749  -0.26290 0.18100  291 ALA A CA  
2289 C C   . ALA A 287 ? 1.25930 1.19404 1.03983 0.05086  -0.25282 0.19233  291 ALA A C   
2290 O O   . ALA A 287 ? 1.16082 1.11657 0.99023 0.05617  -0.24051 0.18254  291 ALA A O   
2291 C CB  . ALA A 287 ? 1.22404 1.20496 1.01568 0.07072  -0.30244 0.17970  291 ALA A CB  
2292 N N   . SER A 288 ? 1.32486 1.20285 1.04586 0.04562  -0.25674 0.21283  292 SER A N   
2293 C CA  . SER A 288 ? 1.23751 1.07388 0.94984 0.04607  -0.24817 0.22493  292 SER A CA  
2294 C C   . SER A 288 ? 1.26684 1.11320 0.99880 0.02692  -0.21069 0.21835  292 SER A C   
2295 O O   . SER A 288 ? 1.25429 1.08206 1.00061 0.02937  -0.20273 0.22138  292 SER A O   
2296 C CB  . SER A 288 ? 1.23052 1.00085 0.86682 0.03857  -0.25707 0.24899  292 SER A CB  
2297 O OG  . SER A 288 ? 1.33542 1.09491 0.93020 0.01010  -0.22998 0.25279  292 SER A OG  
2298 N N   . GLN A 289 ? 1.28127 1.15414 1.01275 0.00834  -0.18891 0.20900  293 GLN A N   
2299 C CA  . GLN A 289 ? 1.20200 1.08880 0.95681 -0.00747 -0.15620 0.20054  293 GLN A CA  
2300 C C   . GLN A 289 ? 1.09610 1.03059 0.91577 0.00224  -0.15189 0.18214  293 GLN A C   
2301 O O   . GLN A 289 ? 1.02013 0.95767 0.86774 0.00056  -0.13646 0.17766  293 GLN A O   
2302 C CB  . GLN A 289 ? 1.22520 1.11740 0.95159 -0.02990 -0.13520 0.19730  293 GLN A CB  
2303 C CG  . GLN A 289 ? 1.34258 1.18720 1.00142 -0.04491 -0.13165 0.21435  293 GLN A CG  
2304 C CD  . GLN A 289 ? 1.47577 1.29794 1.12747 -0.06260 -0.10392 0.21884  293 GLN A CD  
2305 O OE1 . GLN A 289 ? 1.36764 1.18201 1.04695 -0.05665 -0.10199 0.22026  293 GLN A OE1 
2306 N NE2 . GLN A 289 ? 1.58959 1.40276 1.20537 -0.08526 -0.08159 0.21936  293 GLN A NE2 
2307 N N   . ALA A 290 ? 1.06030 1.03172 0.90289 0.01080  -0.16491 0.17088  294 ALA A N   
2308 C CA  . ALA A 290 ? 1.00016 1.01379 0.90004 0.01785  -0.15953 0.15416  294 ALA A CA  
2309 C C   . ALA A 290 ? 1.07057 1.07755 0.99801 0.03547  -0.16869 0.15482  294 ALA A C   
2310 O O   . ALA A 290 ? 0.99538 1.01641 0.95645 0.03549  -0.15418 0.14610  294 ALA A O   
2311 C CB  . ALA A 290 ? 0.97293 1.02542 0.89187 0.02253  -0.17281 0.14214  294 ALA A CB  
2312 N N   . ARG A 291 ? 1.07360 1.05502 0.98339 0.05087  -0.19356 0.16530  295 ARG A N   
2313 C CA  . ARG A 291 ? 1.01188 0.98123 0.94480 0.07017  -0.20506 0.16571  295 ARG A CA  
2314 C C   . ARG A 291 ? 1.07539 1.01134 0.99928 0.06122  -0.18637 0.17260  295 ARG A C   
2315 O O   . ARG A 291 ? 1.02468 0.96944 0.98396 0.06884  -0.18031 0.16378  295 ARG A O   
2316 C CB  . ARG A 291 ? 1.08336 1.02292 0.99012 0.08803  -0.23743 0.17778  295 ARG A CB  
2317 C CG  . ARG A 291 ? 1.19746 1.15050 1.14652 0.11558  -0.25829 0.16882  295 ARG A CG  
2318 C CD  . ARG A 291 ? 1.30763 1.22127 1.22452 0.13426  -0.29255 0.18315  295 ARG A CD  
2319 N NE  . ARG A 291 ? 1.25002 1.18961 1.16366 0.14028  -0.31497 0.17961  295 ARG A NE  
2320 C CZ  . ARG A 291 ? 1.28249 1.18992 1.13854 0.13421  -0.32965 0.19546  295 ARG A CZ  
2321 N NH1 . ARG A 291 ? 1.26984 1.11602 1.06540 0.12235  -0.32440 0.21693  295 ARG A NH1 
2322 N NH2 . ARG A 291 ? 1.30994 1.24698 1.16747 0.13859  -0.34952 0.18904  295 ARG A NH2 
2323 N N   . ASP A 292 ? 1.06483 0.96239 0.94058 0.04388  -0.17673 0.18741  296 ASP A N   
2324 C CA  . ASP A 292 ? 1.09020 0.95847 0.95764 0.03104  -0.15699 0.19286  296 ASP A CA  
2325 C C   . ASP A 292 ? 1.11482 1.01983 1.02484 0.02316  -0.13371 0.17649  296 ASP A C   
2326 O O   . ASP A 292 ? 1.14893 1.04713 1.08051 0.02574  -0.12691 0.17257  296 ASP A O   
2327 C CB  . ASP A 292 ? 1.15872 0.99136 0.97035 0.00887  -0.14546 0.20774  296 ASP A CB  
2328 C CG  . ASP A 292 ? 1.29117 1.09581 1.09537 -0.00783 -0.12359 0.21233  296 ASP A CG  
2329 O OD1 . ASP A 292 ? 1.32385 1.14095 1.12520 -0.02869 -0.09889 0.20772  296 ASP A OD1 
2330 O OD2 . ASP A 292 ? 1.40928 1.17850 1.21032 -0.00025 -0.13179 0.21985  296 ASP A OD2 
2331 N N   . LEU A 293 ? 1.02541 0.96717 0.94620 0.01414  -0.12304 0.16652  297 LEU A N   
2332 C CA  . LEU A 293 ? 0.98604 0.95968 0.94317 0.00796  -0.10422 0.15185  297 LEU A CA  
2333 C C   . LEU A 293 ? 0.94778 0.94611 0.94788 0.02476  -0.11152 0.13993  297 LEU A C   
2334 O O   . LEU A 293 ? 0.92442 0.93213 0.94908 0.02282  -0.09910 0.13133  297 LEU A O   
2335 C CB  . LEU A 293 ? 0.79844 0.80043 0.75422 -0.00325 -0.09480 0.14440  297 LEU A CB  
2336 C CG  . LEU A 293 ? 0.91964 0.95028 0.90620 -0.00983 -0.07762 0.13053  297 LEU A CG  
2337 C CD1 . LEU A 293 ? 0.83716 0.85080 0.82208 -0.02093 -0.06054 0.13202  297 LEU A CD1 
2338 C CD2 . LEU A 293 ? 0.89756 0.95035 0.87906 -0.01881 -0.07217 0.12371  297 LEU A CD2 
2339 N N   . LEU A 294 ? 0.96054 0.97228 0.97099 0.04091  -0.13132 0.13759  298 LEU A N   
2340 C CA  . LEU A 294 ? 0.93006 0.96698 0.98240 0.05643  -0.13622 0.12440  298 LEU A CA  
2341 C C   . LEU A 294 ? 0.91139 0.91901 0.96833 0.06574  -0.13797 0.12703  298 LEU A C   
2342 O O   . LEU A 294 ? 0.83178 0.85214 0.91621 0.06784  -0.12797 0.11582  298 LEU A O   
2343 C CB  . LEU A 294 ? 0.84006 0.89951 0.90610 0.07218  -0.15783 0.11980  298 LEU A CB  
2344 C CG  . LEU A 294 ? 0.85796 0.96029 0.93996 0.06441  -0.15342 0.10858  298 LEU A CG  
2345 C CD1 . LEU A 294 ? 0.85015 0.96626 0.93300 0.07630  -0.17799 0.10808  298 LEU A CD1 
2346 C CD2 . LEU A 294 ? 0.81071 0.94773 0.93413 0.06505  -0.14043 0.09170  298 LEU A CD2 
2347 N N   . SER A 295 ? 0.92076 0.88504 0.94683 0.07009  -0.15048 0.14207  299 SER A N   
2348 C CA  . SER A 295 ? 0.97137 0.90119 0.99881 0.07940  -0.15457 0.14513  299 SER A CA  
2349 C C   . SER A 295 ? 1.00666 0.92330 1.03366 0.06283  -0.13260 0.14400  299 SER A C   
2350 O O   . SER A 295 ? 1.09767 0.99014 1.13142 0.06900  -0.13364 0.14277  299 SER A O   
2351 C CB  . SER A 295 ? 1.01932 0.89764 1.00578 0.08464  -0.17260 0.16398  299 SER A CB  
2352 O OG  . SER A 295 ? 1.06801 0.91795 1.01268 0.06157  -0.15933 0.17798  299 SER A OG  
2353 N N   . LYS A 296 ? 0.91131 0.84185 0.93073 0.04259  -0.11424 0.14363  300 LYS A N   
2354 C CA  . LYS A 296 ? 0.96025 0.88715 0.98598 0.02737  -0.09454 0.13950  300 LYS A CA  
2355 C C   . LYS A 296 ? 0.94323 0.91145 1.00309 0.02676  -0.08381 0.12274  300 LYS A C   
2356 O O   . LYS A 296 ? 0.89407 0.86171 0.96413 0.01812  -0.07137 0.11689  300 LYS A O   
2357 C CB  . LYS A 296 ? 0.88201 0.79473 0.87763 0.00544  -0.08089 0.14901  300 LYS A CB  
2358 C CG  . LYS A 296 ? 0.95171 0.81415 0.90679 0.00037  -0.08669 0.16679  300 LYS A CG  
2359 C CD  . LYS A 296 ? 1.03587 0.88830 0.95835 -0.02244 -0.07147 0.17499  300 LYS A CD  
2360 C CE  . LYS A 296 ? 1.22161 1.02118 1.09414 -0.02772 -0.07928 0.19486  300 LYS A CE  
2361 N NZ  . LYS A 296 ? 1.26564 1.05569 1.10122 -0.05143 -0.06264 0.20231  300 LYS A NZ  
2362 N N   . MET A 297 ? 0.86609 0.86863 0.94168 0.03424  -0.08861 0.11504  301 MET A N   
2363 C CA  . MET A 297 ? 0.81358 0.84950 0.91661 0.03343  -0.07917 0.10032  301 MET A CA  
2364 C C   . MET A 297 ? 0.84924 0.89642 0.97822 0.04968  -0.08554 0.08940  301 MET A C   
2365 O O   . MET A 297 ? 0.81316 0.86857 0.95766 0.04863  -0.07665 0.07906  301 MET A O   
2366 C CB  . MET A 297 ? 0.72088 0.78699 0.82513 0.02776  -0.07691 0.09691  301 MET A CB  
2367 C CG  . MET A 297 ? 0.81170 0.87508 0.89929 0.01088  -0.06481 0.10057  301 MET A CG  
2368 S SD  . MET A 297 ? 0.93425 1.02685 1.02011 0.00442  -0.06342 0.09600  301 MET A SD  
2369 C CE  . MET A 297 ? 0.80599 0.91188 0.89830 0.01893  -0.08253 0.09588  301 MET A CE  
2370 N N   . LEU A 298 ? 0.89271 0.94064 1.02612 0.06516  -0.10147 0.09061  302 LEU A N   
2371 C CA  . LEU A 298 ? 0.86622 0.92804 1.02806 0.08304  -0.10825 0.07800  302 LEU A CA  
2372 C C   . LEU A 298 ? 0.83896 0.86257 0.99654 0.09219  -0.11357 0.08081  302 LEU A C   
2373 O O   . LEU A 298 ? 0.94925 0.95607 1.10839 0.10940  -0.13018 0.08326  302 LEU A O   
2374 C CB  . LEU A 298 ? 0.84473 0.92792 1.01842 0.09684  -0.12467 0.07580  302 LEU A CB  
2375 C CG  . LEU A 298 ? 0.83436 0.95672 1.01551 0.08668  -0.11914 0.07038  302 LEU A CG  
2376 C CD1 . LEU A 298 ? 0.85692 0.99912 1.04839 0.09890  -0.13802 0.06877  302 LEU A CD1 
2377 C CD2 . LEU A 298 ? 0.79654 0.95038 1.00285 0.08171  -0.10307 0.05410  302 LEU A CD2 
2378 N N   . VAL A 299 ? 0.84995 0.85855 1.00225 0.08047  -0.10037 0.07983  303 VAL A N   
2379 C CA  . VAL A 299 ? 0.82642 0.79717 0.97389 0.08451  -0.10259 0.08116  303 VAL A CA  
2380 C C   . VAL A 299 ? 0.85585 0.84191 1.02596 0.08693  -0.09307 0.06344  303 VAL A C   
2381 O O   . VAL A 299 ? 0.90622 0.91191 1.07911 0.07393  -0.07987 0.05776  303 VAL A O   
2382 C CB  . VAL A 299 ? 0.92741 0.86492 1.04698 0.06567  -0.09554 0.09504  303 VAL A CB  
2383 C CG1 . VAL A 299 ? 0.93088 0.83360 1.04919 0.06502  -0.09416 0.09313  303 VAL A CG1 
2384 C CG2 . VAL A 299 ? 0.97073 0.88525 1.06156 0.06438  -0.10561 0.11264  303 VAL A CG2 
2385 N N   . ILE A 300 ? 0.84035 0.81594 1.02484 0.10431  -0.10062 0.05412  304 ILE A N   
2386 C CA  . ILE A 300 ? 0.83735 0.83077 1.04220 0.10805  -0.09145 0.03478  304 ILE A CA  
2387 C C   . ILE A 300 ? 0.85321 0.82864 1.04709 0.09214  -0.08058 0.03365  304 ILE A C   
2388 O O   . ILE A 300 ? 0.86685 0.86435 1.06699 0.08519  -0.06967 0.02234  304 ILE A O   
2389 C CB  . ILE A 300 ? 0.86163 0.84623 1.08515 0.13135  -0.10169 0.02294  304 ILE A CB  
2390 C CG1 . ILE A 300 ? 0.81107 0.82993 1.05727 0.14795  -0.11061 0.01655  304 ILE A CG1 
2391 C CG2 . ILE A 300 ? 0.84472 0.83665 1.08126 0.13241  -0.09054 0.00322  304 ILE A CG2 
2392 C CD1 . ILE A 300 ? 0.76061 0.78360 1.03442 0.17131  -0.11660 -0.00210 304 ILE A CD1 
2393 N N   . ASP A 301 ? 0.88311 0.81769 1.05990 0.08561  -0.08398 0.04470  305 ASP A N   
2394 C CA  . ASP A 301 ? 0.97552 0.89270 1.14666 0.07105  -0.07565 0.04147  305 ASP A CA  
2395 C C   . ASP A 301 ? 0.87422 0.80289 1.03500 0.05047  -0.06649 0.05022  305 ASP A C   
2396 O O   . ASP A 301 ? 0.91006 0.82052 1.05467 0.04125  -0.06716 0.06506  305 ASP A O   
2397 C CB  . ASP A 301 ? 1.01147 0.87844 1.17173 0.07249  -0.08277 0.04716  305 ASP A CB  
2398 C CG  . ASP A 301 ? 1.09557 0.94413 1.25190 0.05464  -0.07467 0.04329  305 ASP A CG  
2399 O OD1 . ASP A 301 ? 1.14369 0.94940 1.28749 0.04863  -0.07781 0.05065  305 ASP A OD1 
2400 O OD2 . ASP A 301 ? 1.07761 0.95312 1.24253 0.04601  -0.06611 0.03293  305 ASP A OD2 
2401 N N   . ALA A 302 ? 0.88985 0.84625 1.05836 0.04328  -0.05795 0.04032  306 ALA A N   
2402 C CA  . ALA A 302 ? 0.85361 0.82573 1.01682 0.02755  -0.05067 0.04588  306 ALA A CA  
2403 C C   . ALA A 302 ? 0.95727 0.90591 1.11242 0.01202  -0.04721 0.05340  306 ALA A C   
2404 O O   . ALA A 302 ? 0.93233 0.88886 1.08138 0.00058  -0.04187 0.06119  306 ALA A O   
2405 C CB  . ALA A 302 ? 0.73421 0.73114 0.90454 0.02403  -0.04517 0.03351  306 ALA A CB  
2406 N N   . SER A 303 ? 0.85171 0.77264 1.00773 0.00999  -0.04885 0.04957  307 SER A N   
2407 C CA  . SER A 303 ? 0.88247 0.78280 1.03242 -0.00787 -0.04361 0.05600  307 SER A CA  
2408 C C   . SER A 303 ? 0.97090 0.84744 1.10060 -0.01185 -0.04422 0.07364  307 SER A C   
2409 O O   . SER A 303 ? 0.99866 0.86291 1.12016 -0.02982 -0.03628 0.08038  307 SER A O   
2410 C CB  . SER A 303 ? 0.87044 0.74382 1.02500 -0.01095 -0.04549 0.04754  307 SER A CB  
2411 O OG  . SER A 303 ? 1.06154 0.91115 1.21181 0.00574  -0.05441 0.04722  307 SER A OG  
2412 N N   . LYS A 304 ? 0.97610 0.84655 1.09720 0.00398  -0.05357 0.08039  308 LYS A N   
2413 C CA  . LYS A 304 ? 1.00104 0.84854 1.09764 0.00238  -0.05752 0.09796  308 LYS A CA  
2414 C C   . LYS A 304 ? 0.98120 0.85964 1.07359 0.00288  -0.05615 0.10273  308 LYS A C   
2415 O O   . LYS A 304 ? 1.04138 0.90450 1.11028 0.00047  -0.05943 0.11681  308 LYS A O   
2416 C CB  . LYS A 304 ? 1.02690 0.84421 1.11623 0.02172  -0.07309 0.10224  308 LYS A CB  
2417 C CG  . LYS A 304 ? 1.23287 0.99574 1.30525 0.01566  -0.07593 0.10953  308 LYS A CG  
2418 C CD  . LYS A 304 ? 1.27128 1.01123 1.35114 0.03865  -0.09069 0.10322  308 LYS A CD  
2419 C CE  . LYS A 304 ? 1.24203 0.91859 1.29860 0.03492  -0.09706 0.11374  308 LYS A CE  
2420 N NZ  . LYS A 304 ? 1.22715 0.88407 1.29410 0.06180  -0.11334 0.10561  308 LYS A NZ  
2421 N N   . ARG A 305 ? 0.99511 0.91334 1.10651 0.00567  -0.05218 0.09137  309 ARG A N   
2422 C CA  . ARG A 305 ? 0.93618 0.88347 1.04590 0.00777  -0.05217 0.09356  309 ARG A CA  
2423 C C   . ARG A 305 ? 0.92014 0.87724 1.02270 -0.01029 -0.04020 0.09680  309 ARG A C   
2424 O O   . ARG A 305 ? 0.92524 0.88533 1.03745 -0.02160 -0.03129 0.09048  309 ARG A O   
2425 C CB  . ARG A 305 ? 0.86086 0.84179 0.99164 0.01814  -0.05298 0.07997  309 ARG A CB  
2426 C CG  . ARG A 305 ? 0.82071 0.83006 0.95157 0.02134  -0.05459 0.08097  309 ARG A CG  
2427 C CD  . ARG A 305 ? 0.71228 0.75238 0.86171 0.02777  -0.05261 0.06736  309 ARG A CD  
2428 N NE  . ARG A 305 ? 0.76975 0.80541 0.93211 0.04034  -0.05654 0.05793  309 ARG A NE  
2429 C CZ  . ARG A 305 ? 0.78159 0.83097 0.95483 0.04152  -0.05114 0.04484  309 ARG A CZ  
2430 N NH1 . ARG A 305 ? 0.68876 0.75412 0.86010 0.03152  -0.04354 0.04110  309 ARG A NH1 
2431 N NH2 . ARG A 305 ? 0.68123 0.72567 0.86511 0.05338  -0.05392 0.03496  309 ARG A NH2 
2432 N N   . ILE A 306 ? 0.89211 0.85422 0.97839 -0.01241 -0.04085 0.10547  310 ILE A N   
2433 C CA  . ILE A 306 ? 0.85726 0.83065 0.93633 -0.02777 -0.02905 0.10683  310 ILE A CA  
2434 C C   . ILE A 306 ? 0.88221 0.88831 0.98354 -0.02873 -0.02324 0.09371  310 ILE A C   
2435 O O   . ILE A 306 ? 0.78076 0.80346 0.89540 -0.01796 -0.02877 0.08641  310 ILE A O   
2436 C CB  . ILE A 306 ? 0.87068 0.84331 0.92601 -0.02709 -0.03337 0.11688  310 ILE A CB  
2437 C CG1 . ILE A 306 ? 0.95714 0.92315 0.99220 -0.04515 -0.02049 0.12240  310 ILE A CG1 
2438 C CG2 . ILE A 306 ? 0.80874 0.81290 0.87553 -0.01702 -0.03926 0.11033  310 ILE A CG2 
2439 C CD1 . ILE A 306 ? 0.90044 0.86916 0.91039 -0.04503 -0.02459 0.12968  310 ILE A CD1 
2440 N N   . SER A 307 ? 0.87646 0.89070 0.98135 -0.04194 -0.01190 0.09016  311 SER A N   
2441 C CA  . SER A 307 ? 0.87340 0.91400 0.99675 -0.04216 -0.00845 0.07859  311 SER A CA  
2442 C C   . SER A 307 ? 0.75091 0.80767 0.86605 -0.04294 -0.00623 0.07925  311 SER A C   
2443 O O   . SER A 307 ? 0.67255 0.72204 0.76761 -0.04560 -0.00584 0.08778  311 SER A O   
2444 C CB  . SER A 307 ? 0.75602 0.79969 0.89460 -0.05358 0.00048  0.07100  311 SER A CB  
2445 O OG  . SER A 307 ? 0.77707 0.82390 0.90881 -0.06602 0.01203  0.07275  311 SER A OG  
2446 N N   . VAL A 308 ? 0.77268 0.67671 0.91605 -0.00536 0.00549  0.05639  312 VAL A N   
2447 C CA  . VAL A 308 ? 0.77259 0.69001 0.90498 -0.00207 0.00808  0.06070  312 VAL A CA  
2448 C C   . VAL A 308 ? 0.74037 0.66481 0.87843 -0.00995 0.01675  0.06710  312 VAL A C   
2449 O O   . VAL A 308 ? 0.72813 0.65567 0.85374 -0.00920 0.02186  0.07549  312 VAL A O   
2450 C CB  . VAL A 308 ? 0.86603 0.79718 0.99805 0.00206  0.00163  0.05077  312 VAL A CB  
2451 C CG1 . VAL A 308 ? 0.74448 0.68903 0.86653 0.00578  0.00427  0.05534  312 VAL A CG1 
2452 C CG2 . VAL A 308 ? 0.84948 0.77262 0.97344 0.00845  -0.00554 0.04420  312 VAL A CG2 
2453 N N   . ASP A 309 ? 0.81250 0.73973 0.96935 -0.01801 0.01878  0.06269  313 ASP A N   
2454 C CA  . ASP A 309 ? 0.84960 0.78449 1.01439 -0.02650 0.02868  0.06716  313 ASP A CA  
2455 C C   . ASP A 309 ? 0.78293 0.70502 0.93879 -0.03168 0.03611  0.08003  313 ASP A C   
2456 O O   . ASP A 309 ? 0.82480 0.75124 0.97097 -0.03525 0.04440  0.08734  313 ASP A O   
2457 C CB  . ASP A 309 ? 0.88658 0.82660 1.07670 -0.03397 0.02870  0.05933  313 ASP A CB  
2458 C CG  . ASP A 309 ? 1.10567 1.05357 1.30458 -0.02973 0.01785  0.04710  313 ASP A CG  
2459 O OD1 . ASP A 309 ? 1.22534 1.16285 1.42196 -0.02659 0.00936  0.04229  313 ASP A OD1 
2460 O OD2 . ASP A 309 ? 1.00723 0.97109 1.21471 -0.02982 0.01763  0.04234  313 ASP A OD2 
2461 N N   . GLU A 310 ? 0.80938 0.71492 0.96835 -0.03298 0.03308  0.08298  314 GLU A N   
2462 C CA  . GLU A 310 ? 0.89985 0.79177 1.05007 -0.03811 0.03818  0.09666  314 GLU A CA  
2463 C C   . GLU A 310 ? 0.83641 0.72544 0.96365 -0.03167 0.03705  0.10511  314 GLU A C   
2464 O O   . GLU A 310 ? 0.85890 0.74335 0.97329 -0.03682 0.04274  0.11687  314 GLU A O   
2465 C CB  . GLU A 310 ? 0.92552 0.79963 1.08537 -0.03959 0.03354  0.09809  314 GLU A CB  
2466 C CG  . GLU A 310 ? 1.00749 0.88238 1.18846 -0.04133 0.02932  0.08600  314 GLU A CG  
2467 C CD  . GLU A 310 ? 1.08999 0.94619 1.27981 -0.04244 0.02493  0.08728  314 GLU A CD  
2468 O OE1 . GLU A 310 ? 1.07231 0.92465 1.26800 -0.03732 0.01759  0.07657  314 GLU A OE1 
2469 O OE2 . GLU A 310 ? 1.29076 1.13554 1.48128 -0.04880 0.02866  0.09882  314 GLU A OE2 
2470 N N   . ALA A 311 ? 0.76928 0.66093 0.89040 -0.02100 0.02967  0.09931  315 ALA A N   
2471 C CA  . ALA A 311 ? 0.80396 0.69307 0.90554 -0.01444 0.02786  0.10711  315 ALA A CA  
2472 C C   . ALA A 311 ? 0.93338 0.83497 1.02295 -0.01718 0.03460  0.11107  315 ALA A C   
2473 O O   . ALA A 311 ? 0.85798 0.75320 0.93087 -0.01877 0.03683  0.12265  315 ALA A O   
2474 C CB  . ALA A 311 ? 0.83028 0.72167 0.92937 -0.00300 0.01979  0.09893  315 ALA A CB  
2475 N N   . LEU A 312 ? 0.79587 0.71460 0.89456 -0.01847 0.03768  0.10149  316 LEU A N   
2476 C CA  . LEU A 312 ? 0.77259 0.70392 0.86290 -0.02131 0.04518  0.10327  316 LEU A CA  
2477 C C   . LEU A 312 ? 0.81449 0.74081 0.90113 -0.03352 0.05623  0.11212  316 LEU A C   
2478 O O   . LEU A 312 ? 0.82820 0.75999 0.90127 -0.03695 0.06355  0.11631  316 LEU A O   
2479 C CB  . LEU A 312 ? 0.79109 0.74148 0.89719 -0.02011 0.04529  0.09044  316 LEU A CB  
2480 C CG  . LEU A 312 ? 0.84223 0.80168 0.94549 -0.00914 0.03604  0.08323  316 LEU A CG  
2481 C CD1 . LEU A 312 ? 0.79862 0.77324 0.92264 -0.00958 0.03314  0.07072  316 LEU A CD1 
2482 C CD2 . LEU A 312 ? 0.81200 0.77727 0.89691 -0.00471 0.03783  0.08822  316 LEU A CD2 
2483 N N   . GLN A 313 ? 0.84061 0.75633 0.93825 -0.04078 0.05796  0.11489  317 GLN A N   
2484 C CA  . GLN A 313 ? 0.85933 0.76884 0.95196 -0.05336 0.06847  0.12440  317 GLN A CA  
2485 C C   . GLN A 313 ? 0.91311 0.80314 0.98559 -0.05534 0.06567  0.13991  317 GLN A C   
2486 O O   . GLN A 313 ? 0.95276 0.83505 1.01620 -0.06670 0.07342  0.15001  317 GLN A O   
2487 C CB  . GLN A 313 ? 0.83601 0.74431 0.95255 -0.06157 0.07209  0.12034  317 GLN A CB  
2488 C CG  . GLN A 313 ? 0.83452 0.76154 0.97373 -0.06345 0.07673  0.10702  317 GLN A CG  
2489 C CD  . GLN A 313 ? 0.89762 0.83792 1.03212 -0.06968 0.08975  0.10659  317 GLN A CD  
2490 O OE1 . GLN A 313 ? 0.98050 0.91424 1.09909 -0.07859 0.09949  0.11659  317 GLN A OE1 
2491 N NE2 . GLN A 313 ? 0.85728 0.81585 1.00625 -0.06585 0.09010  0.09470  317 GLN A NE2 
2492 N N   . HIS A 314 ? 0.87265 0.75426 0.93881 -0.04516 0.05467  0.14214  318 HIS A N   
2493 C CA  . HIS A 314 ? 0.92090 0.78332 0.97257 -0.04629 0.04977  0.15680  318 HIS A CA  
2494 C C   . HIS A 314 ? 0.98639 0.84848 1.01139 -0.04933 0.05325  0.16680  318 HIS A C   
2495 O O   . HIS A 314 ? 1.01053 0.88559 1.02738 -0.04303 0.05371  0.16126  318 HIS A O   
2496 C CB  . HIS A 314 ? 1.00902 0.86404 1.06510 -0.03402 0.03784  0.15468  318 HIS A CB  
2497 C CG  . HIS A 314 ? 0.97121 0.80528 1.02128 -0.03502 0.03132  0.16866  318 HIS A CG  
2498 N ND1 . HIS A 314 ? 0.98458 0.81140 1.01371 -0.03455 0.02814  0.18103  318 HIS A ND1 
2499 C CD2 . HIS A 314 ? 0.87379 0.69204 0.93757 -0.03696 0.02661  0.17251  318 HIS A CD2 
2500 C CE1 . HIS A 314 ? 1.06293 0.87024 1.09402 -0.03610 0.02102  0.19241  318 HIS A CE1 
2501 N NE2 . HIS A 314 ? 1.03492 0.83690 1.08756 -0.03739 0.02026  0.18730  318 HIS A NE2 
2502 N N   . PRO A 315 ? 1.01420 0.86052 1.02445 -0.05907 0.05462  0.18189  319 PRO A N   
2503 C CA  . PRO A 315 ? 1.02837 0.87375 1.01053 -0.06493 0.05927  0.19110  319 PRO A CA  
2504 C C   . PRO A 315 ? 1.10926 0.95558 1.07655 -0.05395 0.05067  0.19286  319 PRO A C   
2505 O O   . PRO A 315 ? 1.14983 1.00325 1.09795 -0.05579 0.05551  0.19360  319 PRO A O   
2506 C CB  . PRO A 315 ? 1.06330 0.88758 1.03386 -0.07743 0.05886  0.20816  319 PRO A CB  
2507 C CG  . PRO A 315 ? 1.04063 0.85374 1.03405 -0.07412 0.05051  0.20859  319 PRO A CG  
2508 C CD  . PRO A 315 ? 0.94631 0.77545 0.96509 -0.06705 0.05284  0.19073  319 PRO A CD  
2509 N N   . TYR A 316 ? 1.04347 0.88299 1.01981 -0.04273 0.03863  0.19295  320 TYR A N   
2510 C CA  . TYR A 316 ? 1.05108 0.89279 1.01616 -0.03196 0.03088  0.19389  320 TYR A CA  
2511 C C   . TYR A 316 ? 1.00881 0.87270 0.97642 -0.02488 0.03511  0.17965  320 TYR A C   
2512 O O   . TYR A 316 ? 1.03089 0.89991 0.98361 -0.02000 0.03293  0.18090  320 TYR A O   
2513 C CB  . TYR A 316 ? 0.99628 0.82768 0.97498 -0.02138 0.01892  0.19475  320 TYR A CB  
2514 C CG  . TYR A 316 ? 1.07143 0.90225 1.04014 -0.01089 0.01027  0.19801  320 TYR A CG  
2515 C CD1 . TYR A 316 ? 1.07633 0.89332 1.02591 -0.01416 0.00434  0.21358  320 TYR A CD1 
2516 C CD2 . TYR A 316 ? 1.06919 0.91283 1.04745 0.00167  0.00751  0.18590  320 TYR A CD2 
2517 C CE1 . TYR A 316 ? 1.04046 0.85675 0.98330 -0.00441 -0.00430 0.21668  320 TYR A CE1 
2518 C CE2 . TYR A 316 ? 1.05241 0.89577 1.02343 0.01115  -0.00002 0.18891  320 TYR A CE2 
2519 C CZ  . TYR A 316 ? 1.07485 0.90486 1.02938 0.00842  -0.00589 0.20407  320 TYR A CZ  
2520 O OH  . TYR A 316 ? 1.04987 0.88015 0.99945 0.01806  -0.01378 0.20673  320 TYR A OH  
2521 N N   . ILE A 317 ? 0.99647 0.87307 0.98375 -0.02450 0.04011  0.16648  321 ILE A N   
2522 C CA  . ILE A 317 ? 0.88787 0.78509 0.88239 -0.01801 0.04235  0.15263  321 ILE A CA  
2523 C C   . ILE A 317 ? 0.96427 0.87406 0.95776 -0.02747 0.05498  0.14827  321 ILE A C   
2524 O O   . ILE A 317 ? 0.88108 0.80644 0.87274 -0.02407 0.05785  0.14089  321 ILE A O   
2525 C CB  . ILE A 317 ? 0.93493 0.83707 0.95288 -0.01147 0.03775  0.14067  321 ILE A CB  
2526 C CG1 . ILE A 317 ? 0.94384 0.83259 0.96319 -0.00295 0.02731  0.14427  321 ILE A CG1 
2527 C CG2 . ILE A 317 ? 0.91284 0.83507 0.93861 -0.00512 0.03775  0.12736  321 ILE A CG2 
2528 C CD1 . ILE A 317 ? 0.83626 0.73153 0.84726 0.00868  0.02090  0.14221  321 ILE A CD1 
2529 N N   . ASN A 318 ? 0.92110 0.82411 0.91692 -0.03969 0.06300  0.15275  322 ASN A N   
2530 C CA  . ASN A 318 ? 0.98473 0.90086 0.98880 -0.04876 0.07624  0.14553  322 ASN A CA  
2531 C C   . ASN A 318 ? 1.01197 0.93534 0.99619 -0.05334 0.08521  0.14678  322 ASN A C   
2532 O O   . ASN A 318 ? 0.95348 0.89162 0.94797 -0.05831 0.09630  0.13751  322 ASN A O   
2533 C CB  . ASN A 318 ? 1.01198 0.91810 1.02262 -0.06148 0.08331  0.15100  322 ASN A CB  
2534 C CG  . ASN A 318 ? 1.08613 1.00661 1.11028 -0.07066 0.09767  0.14234  322 ASN A CG  
2535 O OD1 . ASN A 318 ? 1.14582 1.06481 1.15584 -0.08217 0.10974  0.14751  322 ASN A OD1 
2536 N ND2 . ASN A 318 ? 0.96125 0.89603 1.01280 -0.06579 0.09646  0.12865  322 ASN A ND2 
2537 N N   . VAL A 319 ? 1.05889 0.97226 1.01663 -0.05179 0.08049  0.15728  323 VAL A N   
2538 C CA  . VAL A 319 ? 1.08197 0.99971 1.01718 -0.05717 0.08875  0.15893  323 VAL A CA  
2539 C C   . VAL A 319 ? 1.04757 0.98700 0.99292 -0.04941 0.09116  0.14475  323 VAL A C   
2540 O O   . VAL A 319 ? 1.06187 1.00966 0.99765 -0.05530 0.10205  0.14105  323 VAL A O   
2541 C CB  . VAL A 319 ? 1.16135 1.06253 1.06753 -0.05574 0.07956  0.17336  323 VAL A CB  
2542 C CG1 . VAL A 319 ? 1.18430 1.06387 1.08070 -0.06549 0.07758  0.18815  323 VAL A CG1 
2543 C CG2 . VAL A 319 ? 1.01339 0.91557 0.92597 -0.03968 0.06452  0.17190  323 VAL A CG2 
2544 N N   . TRP A 320 ? 0.85147 0.79965 0.81558 -0.03673 0.08115  0.13666  324 TRP A N   
2545 C CA  . TRP A 320 ? 0.94232 0.91004 0.91710 -0.02888 0.08077  0.12441  324 TRP A CA  
2546 C C   . TRP A 320 ? 0.93353 0.91697 0.93929 -0.03027 0.08591  0.11090  324 TRP A C   
2547 O O   . TRP A 320 ? 0.90699 0.90620 0.92664 -0.02303 0.08271  0.10064  324 TRP A O   
2548 C CB  . TRP A 320 ? 0.79917 0.76724 0.77354 -0.01445 0.06587  0.12424  324 TRP A CB  
2549 C CG  . TRP A 320 ? 0.90936 0.86029 0.86042 -0.01135 0.05756  0.13778  324 TRP A CG  
2550 C CD1 . TRP A 320 ? 0.96443 0.90232 0.91742 -0.00556 0.04710  0.14388  324 TRP A CD1 
2551 C CD2 . TRP A 320 ? 0.92679 0.87154 0.85090 -0.01387 0.05836  0.14645  324 TRP A CD2 
2552 N NE1 . TRP A 320 ? 0.91324 0.83751 0.84472 -0.00417 0.04096  0.15631  324 TRP A NE1 
2553 C CE2 . TRP A 320 ? 0.91522 0.84300 0.82751 -0.00937 0.04703  0.15849  324 TRP A CE2 
2554 C CE3 . TRP A 320 ? 0.99196 0.94339 0.90123 -0.01986 0.06756  0.14473  324 TRP A CE3 
2555 C CZ2 . TRP A 320 ? 0.93597 0.85298 0.82222 -0.01081 0.04319  0.16969  324 TRP A CZ2 
2556 C CZ3 . TRP A 320 ? 1.07234 1.01271 0.95283 -0.02153 0.06442  0.15529  324 TRP A CZ3 
2557 C CH2 . TRP A 320 ? 1.05191 0.97510 0.92115 -0.01702 0.05156  0.16809  324 TRP A CH2 
2558 N N   . TYR A 321 ? 0.87116 0.85032 0.88931 -0.03948 0.09269  0.11110  325 TYR A N   
2559 C CA  . TYR A 321 ? 0.78217 0.77338 0.83260 -0.03942 0.09334  0.09935  325 TYR A CA  
2560 C C   . TYR A 321 ? 0.83152 0.84204 0.89757 -0.04265 0.10365  0.08806  325 TYR A C   
2561 O O   . TYR A 321 ? 0.80958 0.82138 0.86760 -0.05249 0.11796  0.08913  325 TYR A O   
2562 C CB  . TYR A 321 ? 0.86001 0.84115 0.92049 -0.04886 0.09797  0.10292  325 TYR A CB  
2563 C CG  . TYR A 321 ? 0.84710 0.83656 0.94012 -0.04769 0.09446  0.09235  325 TYR A CG  
2564 C CD1 . TYR A 321 ? 0.80414 0.80863 0.92209 -0.05401 0.10417  0.08238  325 TYR A CD1 
2565 C CD2 . TYR A 321 ? 0.77511 0.75694 0.87480 -0.04076 0.08141  0.09192  325 TYR A CD2 
2566 C CE1 . TYR A 321 ? 0.73238 0.74344 0.88130 -0.05352 0.09923  0.07329  325 TYR A CE1 
2567 C CE2 . TYR A 321 ? 0.90780 0.89559 1.03513 -0.04065 0.07714  0.08236  325 TYR A CE2 
2568 C CZ  . TYR A 321 ? 0.87097 0.87303 1.02274 -0.04702 0.08517  0.07362  325 TYR A CZ  
2569 O OH  . TYR A 321 ? 0.81059 0.81727 0.98992 -0.04708 0.07890  0.06488  325 TYR A OH  
2570 N N   . ASP A 322 ? 0.81458 0.83965 0.90406 -0.03502 0.09637  0.07699  326 ASP A N   
2571 C CA  . ASP A 322 ? 0.76177 0.80628 0.87432 -0.03643 0.10300  0.06492  326 ASP A CA  
2572 C C   . ASP A 322 ? 0.81277 0.86591 0.95893 -0.03390 0.09489  0.05552  326 ASP A C   
2573 O O   . ASP A 322 ? 0.69660 0.74893 0.84428 -0.02461 0.07980  0.05432  326 ASP A O   
2574 C CB  . ASP A 322 ? 0.82420 0.87809 0.92684 -0.02804 0.09891  0.06213  326 ASP A CB  
2575 C CG  . ASP A 322 ? 0.82695 0.90056 0.95334 -0.03025 0.10744  0.04978  326 ASP A CG  
2576 O OD1 . ASP A 322 ? 0.79527 0.87918 0.95480 -0.03218 0.10729  0.04082  326 ASP A OD1 
2577 O OD2 . ASP A 322 ? 0.96806 1.04668 1.08139 -0.02986 0.11350  0.04872  326 ASP A OD2 
2578 N N   . PRO A 323 ? 0.76490 0.82608 0.93843 -0.04236 0.10418  0.04862  327 PRO A N   
2579 C CA  . PRO A 323 ? 0.70363 0.77184 0.90947 -0.04046 0.09451  0.04022  327 PRO A CA  
2580 C C   . PRO A 323 ? 0.73120 0.81265 0.94941 -0.03085 0.08187  0.03241  327 PRO A C   
2581 O O   . PRO A 323 ? 0.76303 0.84481 0.99515 -0.02675 0.06793  0.02872  327 PRO A O   
2582 C CB  . PRO A 323 ? 0.70319 0.77966 0.93720 -0.05170 0.10896  0.03415  327 PRO A CB  
2583 C CG  . PRO A 323 ? 0.78344 0.86245 1.00190 -0.05791 0.12658  0.03599  327 PRO A CG  
2584 C CD  . PRO A 323 ? 0.70756 0.77071 0.88401 -0.05472 0.12362  0.04836  327 PRO A CD  
2585 N N   . SER A 324 ? 0.66158 0.75307 0.87412 -0.02746 0.08543  0.02998  328 SER A N   
2586 C CA  . SER A 324 ? 0.69465 0.79859 0.92110 -0.01874 0.07232  0.02310  328 SER A CA  
2587 C C   . SER A 324 ? 0.73147 0.82599 0.93739 -0.00925 0.05591  0.02851  328 SER A C   
2588 O O   . SER A 324 ? 0.77857 0.87997 0.99626 -0.00317 0.04206  0.02370  328 SER A O   
2589 C CB  . SER A 324 ? 0.75411 0.87009 0.97869 -0.01674 0.07924  0.01940  328 SER A CB  
2590 O OG  . SER A 324 ? 0.83495 0.94106 1.02234 -0.01435 0.08288  0.02833  328 SER A OG  
2591 N N   . GLU A 325 ? 0.72257 0.80106 0.89844 -0.00836 0.05722  0.03855  329 GLU A N   
2592 C CA  . GLU A 325 ? 0.71684 0.78500 0.87416 0.00004  0.04381  0.04351  329 GLU A CA  
2593 C C   . GLU A 325 ? 0.72963 0.78505 0.88992 -0.00231 0.03884  0.04494  329 GLU A C   
2594 O O   . GLU A 325 ? 0.79313 0.84640 0.95505 0.00296  0.02607  0.04219  329 GLU A O   
2595 C CB  . GLU A 325 ? 0.79735 0.85583 0.92210 0.00380  0.04651  0.05347  329 GLU A CB  
2596 C CG  . GLU A 325 ? 0.78923 0.85874 0.90806 0.00572  0.05173  0.05218  329 GLU A CG  
2597 C CD  . GLU A 325 ? 0.88918 0.94770 0.97625 0.00575  0.05717  0.06256  329 GLU A CD  
2598 O OE1 . GLU A 325 ? 0.89938 0.94447 0.97357 -0.00112 0.06433  0.07014  329 GLU A OE1 
2599 O OE2 . GLU A 325 ? 0.89626 0.95948 0.97179 0.01218  0.05362  0.06341  329 GLU A OE2 
2600 N N   . ALA A 326 ? 0.76231 0.80855 0.92252 -0.01057 0.04859  0.04906  330 ALA A N   
2601 C CA  . ALA A 326 ? 0.76166 0.79465 0.92427 -0.01250 0.04368  0.05062  330 ALA A CA  
2602 C C   . ALA A 326 ? 0.77138 0.81015 0.96474 -0.01833 0.04183  0.04214  330 ALA A C   
2603 O O   . ALA A 326 ? 0.67340 0.70146 0.87066 -0.02013 0.03675  0.04206  330 ALA A O   
2604 C CB  . ALA A 326 ? 0.75723 0.77493 0.90382 -0.01844 0.05308  0.06090  330 ALA A CB  
2605 N N   . GLU A 327 ? 0.65044 0.70515 0.86726 -0.02177 0.04608  0.03496  331 GLU A N   
2606 C CA  . GLU A 327 ? 0.68395 0.74482 0.93373 -0.02762 0.04377  0.02705  331 GLU A CA  
2607 C C   . GLU A 327 ? 0.76753 0.84497 1.03870 -0.02404 0.03513  0.01823  331 GLU A C   
2608 O O   . GLU A 327 ? 0.79417 0.88343 1.09678 -0.02940 0.03866  0.01139  331 GLU A O   
2609 C CB  . GLU A 327 ? 0.68271 0.74508 0.94728 -0.03848 0.06028  0.02766  331 GLU A CB  
2610 C CG  . GLU A 327 ? 0.78443 0.82906 1.03200 -0.04368 0.06685  0.03690  331 GLU A CG  
2611 C CD  . GLU A 327 ? 0.80663 0.85193 1.06179 -0.05528 0.08533  0.03957  331 GLU A CD  
2612 O OE1 . GLU A 327 ? 0.86234 0.91796 1.14901 -0.06196 0.09109  0.03243  331 GLU A OE1 
2613 O OE2 . GLU A 327 ? 0.79344 0.82799 1.02262 -0.05825 0.09387  0.04933  331 GLU A OE2 
2614 N N   . ALA A 328 ? 0.73358 0.81178 0.98923 -0.01509 0.02336  0.01857  332 ALA A N   
2615 C CA  . ALA A 328 ? 0.72194 0.81504 0.99261 -0.01078 0.01433  0.01225  332 ALA A CA  
2616 C C   . ALA A 328 ? 0.69970 0.79414 0.99209 -0.01211 -0.00133 0.00588  332 ALA A C   
2617 O O   . ALA A 328 ? 0.71003 0.79243 0.99959 -0.01486 -0.00596 0.00643  332 ALA A O   
2618 C CB  . ALA A 328 ? 0.78098 0.87298 1.02386 -0.00129 0.00849  0.01655  332 ALA A CB  
2619 N N   . PRO A 329 ? 0.60070 0.70904 0.91584 -0.01078 -0.01038 -0.00027 333 PRO A N   
2620 C CA  . PRO A 329 ? 0.71201 0.82089 1.04783 -0.01308 -0.02743 -0.00572 333 PRO A CA  
2621 C C   . PRO A 329 ? 0.71402 0.81028 1.02184 -0.00847 -0.04148 -0.00317 333 PRO A C   
2622 O O   . PRO A 329 ? 0.67718 0.77099 0.95746 -0.00135 -0.04213 0.00117  333 PRO A O   
2623 C CB  . PRO A 329 ? 0.64905 0.77539 1.01174 -0.01154 -0.03440 -0.01113 333 PRO A CB  
2624 C CG  . PRO A 329 ? 0.74755 0.88365 1.11377 -0.01133 -0.01603 -0.01099 333 PRO A CG  
2625 C CD  . PRO A 329 ? 0.76900 0.89301 1.09510 -0.00812 -0.00570 -0.00287 333 PRO A CD  
2626 N N   . PRO A 330 ? 0.74489 0.83253 1.05882 -0.01274 -0.05232 -0.00613 334 PRO A N   
2627 C CA  . PRO A 330 ? 0.74297 0.81660 1.02826 -0.00966 -0.06310 -0.00480 334 PRO A CA  
2628 C C   . PRO A 330 ? 0.74135 0.82056 1.02127 -0.00563 -0.07934 -0.00635 334 PRO A C   
2629 O O   . PRO A 330 ? 0.77399 0.86766 1.07632 -0.00554 -0.08393 -0.00855 334 PRO A O   
2630 C CB  . PRO A 330 ? 0.64943 0.71301 0.94724 -0.01714 -0.06874 -0.00871 334 PRO A CB  
2631 C CG  . PRO A 330 ? 0.61640 0.69258 0.95507 -0.02331 -0.06965 -0.01324 334 PRO A CG  
2632 C CD  . PRO A 330 ? 0.67551 0.76487 1.02291 -0.02123 -0.05371 -0.01112 334 PRO A CD  
2633 N N   . PRO A 331 ? 0.76921 0.83756 1.01983 -0.00222 -0.08744 -0.00512 335 PRO A N   
2634 C CA  . PRO A 331 ? 0.77900 0.85044 1.02462 -0.00091 -0.10505 -0.00684 335 PRO A CA  
2635 C C   . PRO A 331 ? 0.80452 0.87359 1.06984 -0.00897 -0.12049 -0.01229 335 PRO A C   
2636 O O   . PRO A 331 ? 0.77340 0.83409 1.04688 -0.01457 -0.11832 -0.01491 335 PRO A O   
2637 C CB  . PRO A 331 ? 0.73834 0.79663 0.94598 0.00362  -0.10597 -0.00454 335 PRO A CB  
2638 C CG  . PRO A 331 ? 0.77830 0.82305 0.97816 0.00169  -0.09492 -0.00439 335 PRO A CG  
2639 C CD  . PRO A 331 ? 0.74726 0.79954 0.96921 -0.00003 -0.08077 -0.00236 335 PRO A CD  
2640 N N   . LYS A 332 ? 0.88506 0.96091 1.15867 -0.00998 -0.13732 -0.01359 336 LYS A N   
2641 C CA  . LYS A 332 ? 1.05242 1.12560 1.34589 -0.01834 -0.15464 -0.01808 336 LYS A CA  
2642 C C   . LYS A 332 ? 1.08489 1.14325 1.34594 -0.02056 -0.16883 -0.01890 336 LYS A C   
2643 O O   . LYS A 332 ? 1.18011 1.24042 1.42621 -0.01859 -0.17992 -0.01690 336 LYS A O   
2644 C CB  . LYS A 332 ? 1.04781 1.13735 1.37778 -0.01991 -0.16513 -0.01916 336 LYS A CB  
2645 C CG  . LYS A 332 ? 1.21503 1.31036 1.53696 -0.01709 -0.18057 -0.01668 336 LYS A CG  
2646 C CD  . LYS A 332 ? 1.10030 1.20330 1.40507 -0.00765 -0.16873 -0.01235 336 LYS A CD  
2647 C CE  . LYS A 332 ? 0.93408 1.04595 1.24166 -0.00551 -0.18467 -0.01004 336 LYS A CE  
2648 N NZ  . LYS A 332 ? 1.09461 1.21823 1.39968 0.00318  -0.17331 -0.00689 336 LYS A NZ  
2649 N N   . ILE A 333 ? 1.07689 1.11991 1.32608 -0.02500 -0.16759 -0.02205 337 ILE A N   
2650 C CA  . ILE A 333 ? 1.16868 1.19580 1.38413 -0.02773 -0.17781 -0.02430 337 ILE A CA  
2651 C C   . ILE A 333 ? 1.31007 1.33399 1.53642 -0.03699 -0.20092 -0.02756 337 ILE A C   
2652 O O   . ILE A 333 ? 1.35550 1.37658 1.60597 -0.04380 -0.20600 -0.03106 337 ILE A O   
2653 C CB  . ILE A 333 ? 1.26286 1.27400 1.46028 -0.02835 -0.16637 -0.02710 337 ILE A CB  
2654 C CG1 . ILE A 333 ? 1.14856 1.15746 1.31912 -0.01941 -0.15061 -0.02342 337 ILE A CG1 
2655 C CG2 . ILE A 333 ? 1.36380 1.35807 1.53982 -0.03559 -0.18016 -0.03272 337 ILE A CG2 
2656 C CD1 . ILE A 333 ? 1.23156 1.23411 1.36836 -0.01761 -0.15778 -0.02375 337 ILE A CD1 
2657 N N   . PRO A 334 ? 1.49791 1.52164 1.70714 -0.03803 -0.21617 -0.02595 338 PRO A N   
2658 C CA  . PRO A 334 ? 1.50159 1.52270 1.72226 -0.04750 -0.24071 -0.02750 338 PRO A CA  
2659 C C   . PRO A 334 ? 1.60768 1.60875 1.80760 -0.05642 -0.24988 -0.03297 338 PRO A C   
2660 O O   . PRO A 334 ? 1.56128 1.55105 1.74224 -0.05511 -0.23631 -0.03639 338 PRO A O   
2661 C CB  . PRO A 334 ? 1.47059 1.49668 1.67420 -0.04561 -0.25237 -0.02287 338 PRO A CB  
2662 C CG  . PRO A 334 ? 1.30808 1.34179 1.49645 -0.03426 -0.23292 -0.01912 338 PRO A CG  
2663 C CD  . PRO A 334 ? 1.41300 1.44003 1.59467 -0.03068 -0.21188 -0.02166 338 PRO A CD  
2664 N N   . ASP A 335 ? 1.69663 1.69252 1.90100 -0.06601 -0.27377 -0.03392 339 ASP A N   
2665 C CA  . ASP A 335 ? 1.83747 1.81331 2.02086 -0.07596 -0.28510 -0.03954 339 ASP A CA  
2666 C C   . ASP A 335 ? 1.88171 1.84471 2.01313 -0.07678 -0.28619 -0.04035 339 ASP A C   
2667 O O   . ASP A 335 ? 1.86290 1.81791 1.97447 -0.08491 -0.30590 -0.03984 339 ASP A O   
2668 C CB  . ASP A 335 ? 1.94200 1.91661 2.15122 -0.08663 -0.31120 -0.03970 339 ASP A CB  
2669 C CG  . ASP A 335 ? 1.99702 1.95649 2.21070 -0.09536 -0.31681 -0.04616 339 ASP A CG  
2670 O OD1 . ASP A 335 ? 2.00602 1.96785 2.24018 -0.09201 -0.30054 -0.04872 339 ASP A OD1 
2671 O OD2 . ASP A 335 ? 2.02126 1.96616 2.21805 -0.10611 -0.33806 -0.04836 339 ASP A OD2 
2672 N N   . LYS A 336 ? 1.69804 1.65944 1.80814 -0.06830 -0.26409 -0.04122 340 LYS A N   
2673 C CA  . LYS A 336 ? 1.59438 1.54379 1.65775 -0.06792 -0.25959 -0.04331 340 LYS A CA  
2674 C C   . LYS A 336 ? 1.61559 1.55489 1.66622 -0.06369 -0.23874 -0.04885 340 LYS A C   
2675 O O   . LYS A 336 ? 1.57486 1.52274 1.64605 -0.05556 -0.22204 -0.04667 340 LYS A O   
2676 C CB  . LYS A 336 ? 1.51255 1.47408 1.56506 -0.05985 -0.25507 -0.03649 340 LYS A CB  
2677 C CG  . LYS A 336 ? 1.47166 1.44950 1.55239 -0.05988 -0.26999 -0.02964 340 LYS A CG  
2678 C CD  . LYS A 336 ? 1.38039 1.36135 1.43571 -0.05821 -0.27594 -0.02444 340 LYS A CD  
2679 C CE  . LYS A 336 ? 1.34250 1.34392 1.42815 -0.05221 -0.28043 -0.01700 340 LYS A CE  
2680 N NZ  . LYS A 336 ? 1.33892 1.35516 1.45711 -0.04230 -0.26249 -0.01596 340 LYS A NZ  
2681 N N   . GLN A 337 ? 1.63120 1.55177 1.64841 -0.06972 -0.23980 -0.05613 341 GLN A N   
2682 C CA  . GLN A 337 ? 1.61453 1.52379 1.62117 -0.06653 -0.22164 -0.06245 341 GLN A CA  
2683 C C   . GLN A 337 ? 1.55182 1.45828 1.52629 -0.05982 -0.20738 -0.06281 341 GLN A C   
2684 O O   . GLN A 337 ? 1.62049 1.51853 1.56206 -0.06500 -0.21422 -0.06557 341 GLN A O   
2685 C CB  . GLN A 337 ? 1.78879 1.67834 1.78319 -0.07769 -0.23070 -0.07208 341 GLN A CB  
2686 C CG  . GLN A 337 ? 1.68118 1.57176 1.71138 -0.08346 -0.24117 -0.07268 341 GLN A CG  
2687 C CD  . GLN A 337 ? 1.55623 1.45116 1.61440 -0.07664 -0.22334 -0.07224 341 GLN A CD  
2688 O OE1 . GLN A 337 ? 1.54599 1.43994 1.59445 -0.06846 -0.20413 -0.07233 341 GLN A OE1 
2689 N NE2 . GLN A 337 ? 1.53276 1.43220 1.62678 -0.08050 -0.23007 -0.07135 341 GLN A NE2 
2690 N N   . LEU A 338 ? 1.40761 1.32079 1.39180 -0.04888 -0.18787 -0.05971 342 LEU A N   
2691 C CA  . LEU A 338 ? 1.39195 1.30162 1.35056 -0.04184 -0.17279 -0.06046 342 LEU A CA  
2692 C C   . LEU A 338 ? 1.44138 1.33347 1.38848 -0.04334 -0.16163 -0.07000 342 LEU A C   
2693 O O   . LEU A 338 ? 1.28625 1.17782 1.24460 -0.03605 -0.14581 -0.06941 342 LEU A O   
2694 C CB  . LEU A 338 ? 1.16818 1.09367 1.14350 -0.02970 -0.15977 -0.05142 342 LEU A CB  
2695 C CG  . LEU A 338 ? 1.15571 1.09923 1.15143 -0.02852 -0.17048 -0.04312 342 LEU A CG  
2696 C CD1 . LEU A 338 ? 1.00892 0.96577 1.01409 -0.01697 -0.15687 -0.03537 342 LEU A CD1 
2697 C CD2 . LEU A 338 ? 1.15581 1.09991 1.13270 -0.03459 -0.18769 -0.04230 342 LEU A CD2 
2698 N N   . ASP A 339 ? 1.60018 1.47687 1.52519 -0.05374 -0.17114 -0.07899 343 ASP A N   
2699 C CA  . ASP A 339 ? 1.66360 1.52342 1.58520 -0.05731 -0.16447 -0.08915 343 ASP A CA  
2700 C C   . ASP A 339 ? 1.77647 1.62026 1.66034 -0.06081 -0.15835 -0.09942 343 ASP A C   
2701 O O   . ASP A 339 ? 1.99955 1.82643 1.87086 -0.06910 -0.16094 -0.11025 343 ASP A O   
2702 C CB  . ASP A 339 ? 1.75726 1.61086 1.69277 -0.06772 -0.18052 -0.09274 343 ASP A CB  
2703 C CG  . ASP A 339 ? 1.86575 1.71371 1.77972 -0.07958 -0.20198 -0.09491 343 ASP A CG  
2704 O OD1 . ASP A 339 ? 1.84934 1.69828 1.73616 -0.08037 -0.20455 -0.09340 343 ASP A OD1 
2705 O OD2 . ASP A 339 ? 1.88243 1.72425 1.80709 -0.08878 -0.21714 -0.09774 343 ASP A OD2 
2706 N N   . GLU A 340 ? 1.58780 1.43661 1.45347 -0.05511 -0.15019 -0.09662 344 GLU A N   
2707 C CA  . GLU A 340 ? 1.61662 1.45192 1.44973 -0.05675 -0.13953 -0.10643 344 GLU A CA  
2708 C C   . GLU A 340 ? 1.64428 1.46280 1.44615 -0.07136 -0.15164 -0.11695 344 GLU A C   
2709 O O   . GLU A 340 ? 1.57744 1.38041 1.35530 -0.07501 -0.14183 -0.12896 344 GLU A O   
2710 C CB  . GLU A 340 ? 1.45898 1.28618 1.30252 -0.04998 -0.12044 -0.11270 344 GLU A CB  
2711 C CG  . GLU A 340 ? 1.46157 1.30302 1.33794 -0.03794 -0.11183 -0.10168 344 GLU A CG  
2712 C CD  . GLU A 340 ? 1.29519 1.13291 1.17384 -0.02857 -0.09221 -0.10371 344 GLU A CD  
2713 O OE1 . GLU A 340 ? 1.15320 0.99861 1.05772 -0.01982 -0.08467 -0.09562 344 GLU A OE1 
2714 O OE2 . GLU A 340 ? 1.38851 1.21524 1.24312 -0.03055 -0.08455 -0.11341 344 GLU A OE2 
2715 N N   . ARG A 341 ? 1.73406 1.55475 1.53678 -0.08024 -0.17298 -0.11300 345 ARG A N   
2716 C CA  . ARG A 341 ? 1.80825 1.61333 1.57648 -0.09508 -0.18709 -0.12078 345 ARG A CA  
2717 C C   . ARG A 341 ? 1.82119 1.62565 1.55349 -0.09672 -0.18342 -0.12055 345 ARG A C   
2718 O O   . ARG A 341 ? 1.73227 1.55074 1.47078 -0.08638 -0.17381 -0.11259 345 ARG A O   
2719 C CB  . ARG A 341 ? 1.80595 1.61444 1.58636 -0.10394 -0.21278 -0.11464 345 ARG A CB  
2720 C CG  . ARG A 341 ? 1.88763 1.69283 1.69867 -0.10598 -0.21851 -0.11714 345 ARG A CG  
2721 C CD  . ARG A 341 ? 1.92834 1.73603 1.75158 -0.11557 -0.24487 -0.11166 345 ARG A CD  
2722 N NE  . ARG A 341 ? 1.88794 1.71777 1.74932 -0.10714 -0.24817 -0.09890 345 ARG A NE  
2723 C CZ  . ARG A 341 ? 1.91765 1.75541 1.79367 -0.11247 -0.26949 -0.09136 345 ARG A CZ  
2724 N NH1 . ARG A 341 ? 1.82098 1.64601 1.67718 -0.12660 -0.29146 -0.09393 345 ARG A NH1 
2725 N NH2 . ARG A 341 ? 1.89563 1.75405 1.80724 -0.10384 -0.26909 -0.08115 345 ARG A NH2 
2726 N N   . GLU A 342 ? 1.85929 1.64672 1.55275 -0.11052 -0.19118 -0.12939 346 GLU A N   
2727 C CA  . GLU A 342 ? 1.83664 1.62121 1.49171 -0.11499 -0.18865 -0.12986 346 GLU A CA  
2728 C C   . GLU A 342 ? 1.83532 1.61791 1.47113 -0.12829 -0.21485 -0.12355 346 GLU A C   
2729 O O   . GLU A 342 ? 1.95562 1.72669 1.58712 -0.14000 -0.23255 -0.12715 346 GLU A O   
2730 C CB  . GLU A 342 ? 1.87451 1.63943 1.49491 -0.12089 -0.17259 -0.14636 346 GLU A CB  
2731 C CG  . GLU A 342 ? 2.01395 1.78201 1.65085 -0.10701 -0.14556 -0.15131 346 GLU A CG  
2732 C CD  . GLU A 342 ? 2.15185 1.90693 1.75305 -0.11076 -0.12743 -0.16426 346 GLU A CD  
2733 O OE1 . GLU A 342 ? 2.14503 1.89792 1.71191 -0.11892 -0.13182 -0.16311 346 GLU A OE1 
2734 O OE2 . GLU A 342 ? 2.20830 1.95527 1.81678 -0.10589 -0.10860 -0.17563 346 GLU A OE2 
2735 N N   . HIS A 343 ? 1.79386 1.58799 1.42124 -0.12619 -0.21834 -0.11330 347 HIS A N   
2736 C CA  . HIS A 343 ? 1.74087 1.53098 1.34016 -0.13952 -0.24007 -0.10761 347 HIS A CA  
2737 C C   . HIS A 343 ? 1.69272 1.47976 1.25370 -0.14117 -0.22707 -0.10938 347 HIS A C   
2738 O O   . HIS A 343 ? 1.66117 1.45374 1.22687 -0.12962 -0.20310 -0.11244 347 HIS A O   
2739 C CB  . HIS A 343 ? 1.64838 1.45740 1.27986 -0.13557 -0.25934 -0.09158 347 HIS A CB  
2740 C CG  . HIS A 343 ? 1.65739 1.47709 1.33828 -0.12755 -0.26282 -0.08834 347 HIS A CG  
2741 N ND1 . HIS A 343 ? 1.68880 1.51858 1.39987 -0.11259 -0.24209 -0.08922 347 HIS A ND1 
2742 C CD2 . HIS A 343 ? 1.65145 1.47359 1.35770 -0.13287 -0.28476 -0.08363 347 HIS A CD2 
2743 C CE1 . HIS A 343 ? 1.66612 1.50381 1.41659 -0.10959 -0.25006 -0.08553 347 HIS A CE1 
2744 N NE2 . HIS A 343 ? 1.65409 1.48790 1.40407 -0.12136 -0.27542 -0.08242 347 HIS A NE2 
2745 N N   . THR A 344 ? 1.63968 1.41759 1.16307 -0.15601 -0.24314 -0.10700 348 THR A N   
2746 C CA  . THR A 344 ? 1.61911 1.39281 1.10358 -0.15937 -0.23014 -0.10928 348 THR A CA  
2747 C C   . THR A 344 ? 1.54750 1.34228 1.04797 -0.14887 -0.22986 -0.09436 348 THR A C   
2748 O O   . THR A 344 ? 1.51013 1.32226 1.05031 -0.13953 -0.24006 -0.08285 348 THR A O   
2749 C CB  . THR A 344 ? 1.68922 1.44213 1.12100 -0.18111 -0.24526 -0.11366 348 THR A CB  
2750 O OG1 . THR A 344 ? 1.77402 1.52283 1.16799 -0.18435 -0.22887 -0.11699 348 THR A OG1 
2751 C CG2 . THR A 344 ? 1.54439 1.30088 0.97879 -0.19042 -0.27833 -0.09921 348 THR A CG2 
2752 N N   . ILE A 345 ? 1.52562 1.31866 0.99505 -0.15063 -0.21696 -0.09531 349 ILE A N   
2753 C CA  . ILE A 345 ? 1.57373 1.38544 1.05501 -0.14120 -0.21547 -0.08192 349 ILE A CA  
2754 C C   . ILE A 345 ? 1.55414 1.37379 1.04462 -0.14697 -0.24550 -0.06700 349 ILE A C   
2755 O O   . ILE A 345 ? 1.44718 1.28648 0.97512 -0.13503 -0.25063 -0.05537 349 ILE A O   
2756 C CB  . ILE A 345 ? 1.52953 1.33496 0.97056 -0.14598 -0.19921 -0.08595 349 ILE A CB  
2757 C CG1 . ILE A 345 ? 1.47711 1.27290 0.90998 -0.14158 -0.16947 -0.10262 349 ILE A CG1 
2758 C CG2 . ILE A 345 ? 1.47927 1.30416 0.93446 -0.13565 -0.19735 -0.07201 349 ILE A CG2 
2759 C CD1 . ILE A 345 ? 1.41737 1.22647 0.89643 -0.12138 -0.15166 -0.10326 349 ILE A CD1 
2760 N N   . GLU A 346 ? 1.69339 1.49702 1.15047 -0.16585 -0.26627 -0.06754 350 GLU A N   
2761 C CA  . GLU A 346 ? 1.63944 1.44820 1.10421 -0.17326 -0.29714 -0.05345 350 GLU A CA  
2762 C C   . GLU A 346 ? 1.60714 1.42948 1.12595 -0.16389 -0.30966 -0.04781 350 GLU A C   
2763 O O   . GLU A 346 ? 1.66033 1.49845 1.20754 -0.15921 -0.32493 -0.03468 350 GLU A O   
2764 C CB  . GLU A 346 ? 1.71322 1.49883 1.13237 -0.19621 -0.31726 -0.05668 350 GLU A CB  
2765 C CG  . GLU A 346 ? 1.81520 1.60247 1.23880 -0.20656 -0.35189 -0.04223 350 GLU A CG  
2766 C CD  . GLU A 346 ? 2.02179 1.78340 1.39659 -0.23038 -0.37161 -0.04592 350 GLU A CD  
2767 O OE1 . GLU A 346 ? 2.03757 1.78149 1.38807 -0.23713 -0.36129 -0.06088 350 GLU A OE1 
2768 O OE2 . GLU A 346 ? 2.04508 1.80340 1.40514 -0.24278 -0.39768 -0.03395 350 GLU A OE2 
2769 N N   . GLU A 347 ? 1.53231 1.34894 1.06721 -0.16106 -0.30250 -0.05797 351 GLU A N   
2770 C CA  . GLU A 347 ? 1.48377 1.31080 1.06730 -0.15489 -0.31475 -0.05381 351 GLU A CA  
2771 C C   . GLU A 347 ? 1.44522 1.29506 1.07350 -0.13456 -0.29865 -0.04858 351 GLU A C   
2772 O O   . GLU A 347 ? 1.43222 1.29764 1.09914 -0.12894 -0.31153 -0.03896 351 GLU A O   
2773 C CB  . GLU A 347 ? 1.59919 1.41068 1.18192 -0.16044 -0.31331 -0.06639 351 GLU A CB  
2774 C CG  . GLU A 347 ? 1.66992 1.45754 1.20827 -0.18134 -0.33057 -0.07209 351 GLU A CG  
2775 C CD  . GLU A 347 ? 1.69964 1.47099 1.23560 -0.18647 -0.32732 -0.08582 351 GLU A CD  
2776 O OE1 . GLU A 347 ? 1.68222 1.44956 1.21346 -0.17942 -0.30146 -0.09730 351 GLU A OE1 
2777 O OE2 . GLU A 347 ? 1.75446 1.51686 1.29518 -0.19761 -0.35143 -0.08496 351 GLU A OE2 
2778 N N   . TRP A 348 ? 1.45333 1.30465 1.07759 -0.12389 -0.27072 -0.05523 352 TRP A N   
2779 C CA  . TRP A 348 ? 1.34526 1.21657 1.00567 -0.10539 -0.25492 -0.04968 352 TRP A CA  
2780 C C   . TRP A 348 ? 1.30873 1.19651 0.97888 -0.10118 -0.26471 -0.03600 352 TRP A C   
2781 O O   . TRP A 348 ? 1.23427 1.14006 0.94347 -0.08945 -0.26462 -0.02856 352 TRP A O   
2782 C CB  . TRP A 348 ? 1.27864 1.14655 0.92536 -0.09708 -0.22608 -0.05777 352 TRP A CB  
2783 C CG  . TRP A 348 ? 1.34668 1.20685 1.00559 -0.09313 -0.21173 -0.06861 352 TRP A CG  
2784 C CD1 . TRP A 348 ? 1.40223 1.24444 1.03450 -0.09865 -0.19833 -0.08241 352 TRP A CD1 
2785 C CD2 . TRP A 348 ? 1.34602 1.21587 1.04753 -0.08293 -0.20834 -0.06684 352 TRP A CD2 
2786 N NE1 . TRP A 348 ? 1.46301 1.30305 1.12029 -0.09223 -0.18812 -0.08888 352 TRP A NE1 
2787 C CE2 . TRP A 348 ? 1.40391 1.26059 1.10273 -0.08286 -0.19398 -0.07906 352 TRP A CE2 
2788 C CE3 . TRP A 348 ? 1.23225 1.12021 0.97374 -0.07447 -0.21554 -0.05654 352 TRP A CE3 
2789 C CZ2 . TRP A 348 ? 1.29103 1.15196 1.02493 -0.07496 -0.18766 -0.07999 352 TRP A CZ2 
2790 C CZ3 . TRP A 348 ? 1.18069 1.07283 0.95540 -0.06701 -0.20791 -0.05821 352 TRP A CZ3 
2791 C CH2 . TRP A 348 ? 1.21893 1.09752 0.98927 -0.06746 -0.19458 -0.06924 352 TRP A CH2 
2792 N N   . LYS A 349 ? 1.31979 1.20121 0.95391 -0.11107 -0.27261 -0.03280 353 LYS A N   
2793 C CA  . LYS A 349 ? 1.34807 1.24414 0.98994 -0.10781 -0.28260 -0.01962 353 LYS A CA  
2794 C C   . LYS A 349 ? 1.29927 1.20595 0.97750 -0.10861 -0.30710 -0.01060 353 LYS A C   
2795 O O   . LYS A 349 ? 1.28775 1.21339 0.99975 -0.09724 -0.30766 -0.00214 353 LYS A O   
2796 C CB  . LYS A 349 ? 1.41733 1.30201 1.01180 -0.12137 -0.28960 -0.01761 353 LYS A CB  
2797 C CG  . LYS A 349 ? 1.37813 1.27745 0.97672 -0.11659 -0.29424 -0.00473 353 LYS A CG  
2798 C CD  . LYS A 349 ? 1.48478 1.37232 1.03300 -0.12832 -0.29219 -0.00458 353 LYS A CD  
2799 C CE  . LYS A 349 ? 1.51420 1.41626 1.06721 -0.12370 -0.29705 0.00881  353 LYS A CE  
2800 N NZ  . LYS A 349 ? 1.53953 1.43134 1.04450 -0.13461 -0.29252 0.00958  353 LYS A NZ  
2801 N N   . GLU A 350 ? 1.36270 1.25717 1.03647 -0.12197 -0.32726 -0.01290 354 GLU A N   
2802 C CA  . GLU A 350 ? 1.37251 1.27656 1.08519 -0.12314 -0.35086 -0.00519 354 GLU A CA  
2803 C C   . GLU A 350 ? 1.31508 1.23401 1.07683 -0.10866 -0.33918 -0.00694 354 GLU A C   
2804 O O   . GLU A 350 ? 1.29611 1.23295 1.09613 -0.10075 -0.34555 0.00102  354 GLU A O   
2805 C CB  . GLU A 350 ? 1.51289 1.39903 1.21053 -0.14096 -0.37493 -0.00777 354 GLU A CB  
2806 C CG  . GLU A 350 ? 1.61168 1.50635 1.35519 -0.14242 -0.39884 -0.00167 354 GLU A CG  
2807 C CD  . GLU A 350 ? 1.77258 1.65747 1.50206 -0.15946 -0.43237 0.00620  354 GLU A CD  
2808 O OE1 . GLU A 350 ? 1.85270 1.72088 1.53138 -0.17237 -0.43737 0.00568  354 GLU A OE1 
2809 O OE2 . GLU A 350 ? 1.79983 1.69324 1.56955 -0.16053 -0.45390 0.01287  354 GLU A OE2 
2810 N N   . LEU A 351 ? 1.34066 1.25219 1.10159 -0.10528 -0.32133 -0.01746 355 LEU A N   
2811 C CA  . LEU A 351 ? 1.19973 1.12355 1.00438 -0.09315 -0.31006 -0.01894 355 LEU A CA  
2812 C C   . LEU A 351 ? 1.16252 1.10614 0.98905 -0.07754 -0.29591 -0.01224 355 LEU A C   
2813 O O   . LEU A 351 ? 1.11613 1.07536 0.98365 -0.07009 -0.29828 -0.00765 355 LEU A O   
2814 C CB  . LEU A 351 ? 1.17237 1.08399 0.96749 -0.09175 -0.29112 -0.03067 355 LEU A CB  
2815 C CG  . LEU A 351 ? 1.34565 1.23942 1.13102 -0.10527 -0.30411 -0.03840 355 LEU A CG  
2816 C CD1 . LEU A 351 ? 1.28482 1.16852 1.06765 -0.10188 -0.28386 -0.04991 355 LEU A CD1 
2817 C CD2 . LEU A 351 ? 1.31796 1.21910 1.14203 -0.10906 -0.32656 -0.03306 355 LEU A CD2 
2818 N N   . ILE A 352 ? 1.18823 1.13112 0.98798 -0.07286 -0.28090 -0.01201 356 ILE A N   
2819 C CA  . ILE A 352 ? 1.13061 1.09057 0.94798 -0.05818 -0.26705 -0.00595 356 ILE A CA  
2820 C C   . ILE A 352 ? 1.14331 1.11737 0.97650 -0.05776 -0.28458 0.00515  356 ILE A C   
2821 O O   . ILE A 352 ? 1.04039 1.03158 0.90539 -0.04656 -0.28026 0.01044  356 ILE A O   
2822 C CB  . ILE A 352 ? 1.08732 1.04105 0.87251 -0.05413 -0.24669 -0.00941 356 ILE A CB  
2823 C CG1 . ILE A 352 ? 1.08691 1.02956 0.86812 -0.05195 -0.22843 -0.02022 356 ILE A CG1 
2824 C CG2 . ILE A 352 ? 0.97194 0.94229 0.77166 -0.04033 -0.23572 -0.00185 356 ILE A CG2 
2825 C CD1 . ILE A 352 ? 1.19166 1.12332 0.93910 -0.05188 -0.21079 -0.02667 356 ILE A CD1 
2826 N N   . TYR A 353 ? 1.11459 1.08103 0.92526 -0.07038 -0.30476 0.00883  357 TYR A N   
2827 C CA  . TYR A 353 ? 1.13712 1.11581 0.96330 -0.07088 -0.32337 0.01980  357 TYR A CA  
2828 C C   . TYR A 353 ? 1.24108 1.23100 1.11489 -0.06949 -0.33790 0.02241  357 TYR A C   
2829 O O   . TYR A 353 ? 1.23837 1.24578 1.14410 -0.06083 -0.34005 0.02878  357 TYR A O   
2830 C CB  . TYR A 353 ? 1.14854 1.11416 0.93780 -0.08651 -0.34293 0.02361  357 TYR A CB  
2831 C CG  . TYR A 353 ? 1.26047 1.23691 1.05915 -0.08767 -0.36156 0.03591  357 TYR A CG  
2832 C CD1 . TYR A 353 ? 1.23488 1.22680 1.04444 -0.07524 -0.35071 0.04179  357 TYR A CD1 
2833 C CD2 . TYR A 353 ? 1.21012 1.18013 1.00615 -0.10177 -0.39101 0.04189  357 TYR A CD2 
2834 C CE1 . TYR A 353 ? 1.21053 1.21183 1.02949 -0.07649 -0.36815 0.05281  357 TYR A CE1 
2835 C CE2 . TYR A 353 ? 1.24693 1.22596 1.05259 -0.10329 -0.40901 0.05346  357 TYR A CE2 
2836 C CZ  . TYR A 353 ? 1.25975 1.25463 1.07717 -0.09049 -0.39719 0.05867  357 TYR A CZ  
2837 O OH  . TYR A 353 ? 1.40193 1.40560 1.23054 -0.09210 -0.41583 0.07013  357 TYR A OH  
2838 N N   . LYS A 354 ? 1.21070 1.19076 1.09132 -0.07794 -0.34722 0.01686  358 LYS A N   
2839 C CA  . LYS A 354 ? 1.15793 1.14812 1.08636 -0.07734 -0.36029 0.01837  358 LYS A CA  
2840 C C   . LYS A 354 ? 1.22026 1.22733 1.18514 -0.06199 -0.34006 0.01696  358 LYS A C   
2841 O O   . LYS A 354 ? 1.25413 1.27724 1.25889 -0.05693 -0.34658 0.02136  358 LYS A O   
2842 C CB  . LYS A 354 ? 1.14778 1.12304 1.07524 -0.08877 -0.37112 0.01180  358 LYS A CB  
2843 C CG  . LYS A 354 ? 1.34875 1.31819 1.28150 -0.10290 -0.40400 0.01716  358 LYS A CG  
2844 C CD  . LYS A 354 ? 1.36886 1.32077 1.29463 -0.11522 -0.41510 0.01036  358 LYS A CD  
2845 C CE  . LYS A 354 ? 1.36614 1.30375 1.27001 -0.13251 -0.44597 0.01537  358 LYS A CE  
2846 N NZ  . LYS A 354 ? 1.54445 1.45796 1.40686 -0.14551 -0.44856 0.00735  358 LYS A NZ  
2847 N N   . GLU A 355 ? 1.18642 1.18969 1.13791 -0.05479 -0.31535 0.01084  359 GLU A N   
2848 C CA  . GLU A 355 ? 1.16701 1.18430 1.14869 -0.04140 -0.29618 0.01012  359 GLU A CA  
2849 C C   . GLU A 355 ? 1.10275 1.13642 1.09516 -0.03153 -0.29281 0.01758  359 GLU A C   
2850 O O   . GLU A 355 ? 1.13249 1.18137 1.16085 -0.02370 -0.28848 0.01927  359 GLU A O   
2851 C CB  . GLU A 355 ? 1.09767 1.10605 1.06043 -0.03627 -0.27212 0.00336  359 GLU A CB  
2852 C CG  . GLU A 355 ? 1.03625 1.03641 1.01192 -0.04029 -0.26917 -0.00408 359 GLU A CG  
2853 C CD  . GLU A 355 ? 1.17973 1.19392 1.20315 -0.03660 -0.27058 -0.00291 359 GLU A CD  
2854 O OE1 . GLU A 355 ? 1.15883 1.18743 1.20213 -0.02599 -0.25809 0.00035  359 GLU A OE1 
2855 O OE2 . GLU A 355 ? 1.28976 1.30019 1.33103 -0.04485 -0.28412 -0.00556 359 GLU A OE2 
2856 N N   . VAL A 356 ? 1.09588 1.12651 1.05750 -0.03218 -0.29436 0.02178  360 VAL A N   
2857 C CA  . VAL A 356 ? 1.05901 1.10474 1.03082 -0.02305 -0.29233 0.02910  360 VAL A CA  
2858 C C   . VAL A 356 ? 1.06464 1.12211 1.06917 -0.02587 -0.31429 0.03492  360 VAL A C   
2859 O O   . VAL A 356 ? 1.10499 1.17871 1.13883 -0.01676 -0.31112 0.03821  360 VAL A O   
2860 C CB  . VAL A 356 ? 1.06624 1.10553 0.99801 -0.02378 -0.28878 0.03231  360 VAL A CB  
2861 C CG1 . VAL A 356 ? 1.10545 1.16024 1.04902 -0.01337 -0.28512 0.03963  360 VAL A CG1 
2862 C CG2 . VAL A 356 ? 1.04924 1.07661 0.95328 -0.02134 -0.26719 0.02535  360 VAL A CG2 
2863 N N   . MET A 357 ? 1.08008 1.12906 1.08118 -0.03876 -0.33729 0.03608  361 MET A N   
2864 C CA  . MET A 357 ? 1.14986 1.20857 1.18123 -0.04239 -0.36086 0.04256  361 MET A CA  
2865 C C   . MET A 357 ? 1.25656 1.32400 1.33709 -0.04206 -0.36684 0.03927  361 MET A C   
2866 O O   . MET A 357 ? 1.29194 1.37213 1.40834 -0.04098 -0.38077 0.04359  361 MET A O   
2867 C CB  . MET A 357 ? 1.18635 1.23134 1.19162 -0.05753 -0.38603 0.04712  361 MET A CB  
2868 C CG  . MET A 357 ? 1.21836 1.25237 1.17172 -0.06112 -0.38148 0.04981  361 MET A CG  
2869 S SD  . MET A 357 ? 1.43302 1.48182 1.38490 -0.04968 -0.37313 0.05798  361 MET A SD  
2870 C CE  . MET A 357 ? 1.27441 1.34109 1.27986 -0.04774 -0.39560 0.06534  361 MET A CE  
2871 N N   . ASP A 358 ? 1.28459 1.34539 1.36962 -0.04352 -0.35739 0.03163  362 ASP A N   
2872 C CA  . ASP A 358 ? 1.36766 1.43553 1.49942 -0.04509 -0.36431 0.02842  362 ASP A CA  
2873 C C   . ASP A 358 ? 1.47045 1.55580 1.63726 -0.03243 -0.34443 0.02598  362 ASP A C   
2874 O O   . ASP A 358 ? 1.54785 1.64817 1.75465 -0.02946 -0.35171 0.02799  362 ASP A O   
2875 C CB  . ASP A 358 ? 1.64961 1.70201 1.77192 -0.05357 -0.36494 0.02164  362 ASP A CB  
2876 C CG  . ASP A 358 ? 1.76786 1.82694 1.93965 -0.05585 -0.37174 0.01813  362 ASP A CG  
2877 O OD1 . ASP A 358 ? 1.75098 1.82120 1.95984 -0.05709 -0.38849 0.02194  362 ASP A OD1 
2878 O OD2 . ASP A 358 ? 1.77086 1.82401 1.94623 -0.05658 -0.36044 0.01148  362 ASP A OD2 
2879 N N   . LEU A 359 ? 1.52690 1.60999 1.67899 -0.02538 -0.31947 0.02161  363 LEU A N   
2880 C CA  . LEU A 359 ? 1.62412 1.72142 1.80451 -0.01483 -0.29976 0.01932  363 LEU A CA  
2881 C C   . LEU A 359 ? 1.56477 1.66527 1.72083 -0.00425 -0.28096 0.02194  363 LEU A C   
2882 O O   . LEU A 359 ? 1.52693 1.63497 1.67982 -0.00027 -0.28607 0.02743  363 LEU A O   
2883 C CB  . LEU A 359 ? 1.49020 1.58269 1.68227 -0.01620 -0.28705 0.01242  363 LEU A CB  
2884 N N   . ARG B 1   ? 1.77396 1.38418 1.02400 -0.11677 0.09341  -0.17272 157 ARG B N   
2885 C CA  . ARG B 1   ? 1.81354 1.45968 1.10501 -0.11628 0.08912  -0.16891 157 ARG B CA  
2886 C C   . ARG B 1   ? 1.72054 1.38832 1.02145 -0.12290 0.04736  -0.13832 157 ARG B C   
2887 O O   . ARG B 1   ? 1.75914 1.41557 1.03416 -0.13303 0.01591  -0.14127 157 ARG B O   
2888 C CB  . ARG B 1   ? 1.75461 1.39937 1.04661 -0.12113 0.09461  -0.20815 157 ARG B CB  
2889 C CG  . ARG B 1   ? 1.78478 1.45565 1.11824 -0.11386 0.12028  -0.21766 157 ARG B CG  
2890 C CD  . ARG B 1   ? 1.81996 1.48372 1.16492 -0.10123 0.16450  -0.22397 157 ARG B CD  
2891 N NE  . ARG B 1   ? 1.81530 1.51137 1.21824 -0.09017 0.18365  -0.23210 157 ARG B NE  
2892 C CZ  . ARG B 1   ? 1.77026 1.47470 1.20689 -0.07656 0.21303  -0.23221 157 ARG B CZ  
2893 N NH1 . ARG B 1   ? 1.80758 1.49108 1.22760 -0.07218 0.23040  -0.22594 157 ARG B NH1 
2894 N NH2 . ARG B 1   ? 1.50067 1.23539 0.98901 -0.06718 0.22213  -0.23694 157 ARG B NH2 
2895 N N   . PRO B 2   ? 1.68429 1.38303 1.02240 -0.11719 0.04725  -0.10930 158 PRO B N   
2896 C CA  . PRO B 2   ? 1.63783 1.35828 0.98740 -0.12291 0.00882  -0.07811 158 PRO B CA  
2897 C C   . PRO B 2   ? 1.55785 1.29761 0.92154 -0.13168 -0.01446 -0.08941 158 PRO B C   
2898 O O   . PRO B 2   ? 1.54003 1.29065 0.92290 -0.12986 0.00302  -0.11162 158 PRO B O   
2899 C CB  . PRO B 2   ? 1.60981 1.35663 0.99666 -0.11259 0.02295  -0.04676 158 PRO B CB  
2900 C CG  . PRO B 2   ? 1.56365 1.31630 0.97234 -0.10426 0.06269  -0.06899 158 PRO B CG  
2901 C CD  . PRO B 2   ? 1.65454 1.37105 1.02762 -0.10527 0.08230  -0.10427 158 PRO B CD  
2902 N N   . LYS B 3   ? 1.55761 1.30153 0.91157 -0.14115 -0.05483 -0.07340 159 LYS B N   
2903 C CA  . LYS B 3   ? 1.50795 1.26907 0.87296 -0.15037 -0.08095 -0.08152 159 LYS B CA  
2904 C C   . LYS B 3   ? 1.39674 1.19653 0.80965 -0.14578 -0.07625 -0.06527 159 LYS B C   
2905 O O   . LYS B 3   ? 1.38496 1.20323 0.82082 -0.13974 -0.07487 -0.03325 159 LYS B O   
2906 C CB  . LYS B 3   ? 1.64766 1.40474 0.99244 -0.16104 -0.12518 -0.06485 159 LYS B CB  
2907 C CG  . LYS B 3   ? 1.80216 1.56955 1.14914 -0.17216 -0.15444 -0.07758 159 LYS B CG  
2908 C CD  . LYS B 3   ? 1.89672 1.63821 1.21404 -0.17765 -0.14927 -0.11919 159 LYS B CD  
2909 C CE  . LYS B 3   ? 1.92904 1.68389 1.25836 -0.18481 -0.18122 -0.12500 159 LYS B CE  
2910 N NZ  . LYS B 3   ? 1.85457 1.60931 1.20846 -0.17329 -0.16851 -0.15201 159 LYS B NZ  
2911 N N   . ARG B 4   ? 1.34569 1.15758 0.77352 -0.14843 -0.07360 -0.08761 160 ARG B N   
2912 C CA  . ARG B 4   ? 1.26067 1.10895 0.73292 -0.14445 -0.06969 -0.07406 160 ARG B CA  
2913 C C   . ARG B 4   ? 1.22478 1.09595 0.71151 -0.15084 -0.10754 -0.04071 160 ARG B C   
2914 O O   . ARG B 4   ? 1.28544 1.14692 0.74958 -0.16144 -0.14081 -0.04060 160 ARG B O   
2915 C CB  . ARG B 4   ? 1.22982 1.08459 0.71166 -0.14679 -0.06237 -0.10585 160 ARG B CB  
2916 C CG  . ARG B 4   ? 1.21953 1.05880 0.69681 -0.13930 -0.02284 -0.13734 160 ARG B CG  
2917 C CD  . ARG B 4   ? 1.05584 0.89807 0.53598 -0.14367 -0.02331 -0.16938 160 ARG B CD  
2918 N NE  . ARG B 4   ? 1.11031 0.93948 0.58887 -0.13624 0.01508  -0.20073 160 ARG B NE  
2919 C CZ  . ARG B 4   ? 1.14334 0.98595 0.64288 -0.13333 0.03046  -0.22240 160 ARG B CZ  
2920 N NH1 . ARG B 4   ? 1.11757 0.98551 0.63906 -0.13751 0.01065  -0.21702 160 ARG B NH1 
2921 N NH2 . ARG B 4   ? 1.11435 0.94640 0.61759 -0.12430 0.06604  -0.24769 160 ARG B NH2 
2922 N N   . PRO B 5   ? 1.16780 1.06945 0.69231 -0.14472 -0.10344 -0.01253 161 PRO B N   
2923 C CA  . PRO B 5   ? 1.08530 1.01124 0.62729 -0.15091 -0.13881 0.01847  161 PRO B CA  
2924 C C   . PRO B 5   ? 1.18566 1.12361 0.73393 -0.16052 -0.16136 0.00433  161 PRO B C   
2925 O O   . PRO B 5   ? 1.24889 1.19265 0.80895 -0.15858 -0.14363 -0.02024 161 PRO B O   
2926 C CB  . PRO B 5   ? 1.08287 1.03919 0.66683 -0.14076 -0.12162 0.04573  161 PRO B CB  
2927 C CG  . PRO B 5   ? 1.12560 1.07679 0.71755 -0.12990 -0.07786 0.02524  161 PRO B CG  
2928 C CD  . PRO B 5   ? 1.16760 1.08365 0.72190 -0.13206 -0.06552 -0.01055 161 PRO B CD  
2929 N N   . THR B 6   ? 1.14863 1.09048 0.68932 -0.17081 -0.20113 0.02047  162 THR B N   
2930 C CA  . THR B 6   ? 1.21888 1.17317 0.76600 -0.18064 -0.22674 0.01161  162 THR B CA  
2931 C C   . THR B 6   ? 1.20206 1.19168 0.78502 -0.18282 -0.24845 0.04432  162 THR B C   
2932 O O   . THR B 6   ? 1.16100 1.16545 0.75586 -0.18976 -0.26629 0.03881  162 THR B O   
2933 C CB  . THR B 6   ? 1.22463 1.15349 0.73210 -0.19253 -0.25790 -0.00076 162 THR B CB  
2934 O OG1 . THR B 6   ? 1.24491 1.16502 0.73698 -0.19414 -0.27683 0.02563  162 THR B OG1 
2935 C CG2 . THR B 6   ? 1.29715 1.19370 0.77174 -0.19209 -0.23764 -0.04029 162 THR B CG2 
2936 N N   . THR B 7   ? 1.12033 1.12351 0.72037 -0.17737 -0.24831 0.07806  163 THR B N   
2937 C CA  . THR B 7   ? 1.21537 1.25203 0.84960 -0.17959 -0.26934 0.10993  163 THR B CA  
2938 C C   . THR B 7   ? 1.09458 1.15480 0.76519 -0.16729 -0.24149 0.12991  163 THR B C   
2939 O O   . THR B 7   ? 1.06673 1.11476 0.73051 -0.15839 -0.21740 0.13279  163 THR B O   
2940 C CB  . THR B 7   ? 1.14038 1.17304 0.76021 -0.18748 -0.30724 0.13604  163 THR B CB  
2941 O OG1 . THR B 7   ? 1.29145 1.31993 0.91012 -0.17972 -0.29750 0.15926  163 THR B OG1 
2942 C CG2 . THR B 7   ? 1.18391 1.18525 0.76002 -0.19751 -0.32838 0.11371  163 THR B CG2 
2943 N N   . LEU B 8   ? 1.04392 1.13741 0.75284 -0.16673 -0.24415 0.14275  164 LEU B N   
2944 C CA  . LEU B 8   ? 1.05279 1.17276 0.80000 -0.15571 -0.22103 0.16413  164 LEU B CA  
2945 C C   . LEU B 8   ? 1.07136 1.22549 0.85220 -0.15997 -0.24621 0.19456  164 LEU B C   
2946 O O   . LEU B 8   ? 1.04181 1.21008 0.83463 -0.16632 -0.25927 0.18675  164 LEU B O   
2947 C CB  . LEU B 8   ? 0.96284 1.08817 0.72563 -0.14732 -0.18420 0.13928  164 LEU B CB  
2948 C CG  . LEU B 8   ? 0.94256 1.10101 0.75036 -0.13724 -0.16295 0.15829  164 LEU B CG  
2949 C CD1 . LEU B 8   ? 0.82348 0.97487 0.63244 -0.12569 -0.13548 0.16957  164 LEU B CD1 
2950 C CD2 . LEU B 8   ? 0.82913 0.99849 0.65436 -0.13344 -0.14052 0.13332  164 LEU B CD2 
2951 N N   . ASN B 9   ? 1.04228 1.20998 0.83919 -0.15616 -0.25196 0.22892  165 ASN B N   
2952 C CA  . ASN B 9   ? 1.09961 1.29883 0.92754 -0.16057 -0.27768 0.26015  165 ASN B CA  
2953 C C   . ASN B 9   ? 1.09924 1.33151 0.97144 -0.15244 -0.25583 0.26956  165 ASN B C   
2954 O O   . ASN B 9   ? 1.17770 1.41489 1.06431 -0.14072 -0.22561 0.27537  165 ASN B O   
2955 C CB  . ASN B 9   ? 1.11037 1.31005 0.93642 -0.16022 -0.29517 0.29319  165 ASN B CB  
2956 C CG  . ASN B 9   ? 1.24614 1.41582 1.03026 -0.16884 -0.32074 0.28693  165 ASN B CG  
2957 O OD1 . ASN B 9   ? 1.29603 1.45817 1.06408 -0.17978 -0.34478 0.27246  165 ASN B OD1 
2958 N ND2 . ASN B 9   ? 1.35544 1.50691 1.12041 -0.16392 -0.31583 0.29700  165 ASN B ND2 
2959 N N   . LEU B 10  ? 0.96819 1.22314 0.86194 -0.15862 -0.27154 0.27181  166 LEU B N   
2960 C CA  . LEU B 10  ? 0.92786 1.21314 0.86156 -0.15162 -0.25105 0.27626  166 LEU B CA  
2961 C C   . LEU B 10  ? 0.96466 1.28332 0.93577 -0.15040 -0.26349 0.31564  166 LEU B C   
2962 O O   . LEU B 10  ? 0.97651 1.32248 0.98325 -0.14388 -0.24631 0.32333  166 LEU B O   
2963 C CB  . LEU B 10  ? 0.79392 1.08358 0.72908 -0.15795 -0.25631 0.25183  166 LEU B CB  
2964 C CG  . LEU B 10  ? 0.93621 1.19475 0.83733 -0.15849 -0.24169 0.21078  166 LEU B CG  
2965 C CD1 . LEU B 10  ? 0.84152 1.10845 0.74964 -0.16295 -0.24410 0.18879  166 LEU B CD1 
2966 C CD2 . LEU B 10  ? 0.96326 1.20978 0.86149 -0.14547 -0.20000 0.19666  166 LEU B CD2 
2967 N N   . PHE B 11  ? 0.92384 1.24130 0.88824 -0.15629 -0.29260 0.34045  167 PHE B N   
2968 C CA  . PHE B 11  ? 1.06447 1.41393 1.06500 -0.15548 -0.30540 0.37759  167 PHE B CA  
2969 C C   . PHE B 11  ? 1.28381 1.62497 1.27621 -0.15145 -0.30955 0.40131  167 PHE B C   
2970 O O   . PHE B 11  ? 1.35757 1.66975 1.31331 -0.15554 -0.32197 0.39408  167 PHE B O   
2971 C CB  . PHE B 11  ? 0.90098 1.26367 0.90996 -0.16824 -0.34202 0.38662  167 PHE B CB  
2972 C CG  . PHE B 11  ? 0.83999 1.21707 0.86409 -0.17123 -0.33798 0.36916  167 PHE B CG  
2973 C CD1 . PHE B 11  ? 0.77120 1.18213 0.83777 -0.16688 -0.32808 0.38427  167 PHE B CD1 
2974 C CD2 . PHE B 11  ? 0.86355 1.21963 0.85890 -0.17771 -0.34228 0.33652  167 PHE B CD2 
2975 C CE1 . PHE B 11  ? 0.90662 1.32987 0.98610 -0.16905 -0.32343 0.36757  167 PHE B CE1 
2976 C CE2 . PHE B 11  ? 0.87302 1.24098 0.88147 -0.17966 -0.33710 0.31895  167 PHE B CE2 
2977 C CZ  . PHE B 11  ? 0.79476 1.19659 0.84507 -0.17526 -0.32788 0.33487  167 PHE B CZ  
2978 N N   . PRO B 12  ? 1.48827 1.85359 1.51340 -0.14302 -0.29860 0.42906  168 PRO B N   
2979 C CA  . PRO B 12  ? 1.57899 1.93509 1.59626 -0.13702 -0.29679 0.44940  168 PRO B CA  
2980 C C   . PRO B 12  ? 1.64277 1.99431 1.65075 -0.14609 -0.33402 0.46793  168 PRO B C   
2981 O O   . PRO B 12  ? 1.58948 1.94305 1.61027 -0.15425 -0.34821 0.45870  168 PRO B O   
2982 C CB  . PRO B 12  ? 1.60482 1.99153 1.66471 -0.12574 -0.27462 0.47243  168 PRO B CB  
2983 C CG  . PRO B 12  ? 1.46559 1.87996 1.55716 -0.12712 -0.26944 0.46727  168 PRO B CG  
2984 C CD  . PRO B 12  ? 1.30400 1.70712 1.37509 -0.13942 -0.29088 0.44487  168 PRO B CD  
2985 N N   . GLN B 13  ? 1.78844 2.12104 1.77574 -0.14232 -0.33516 0.47770  169 GLN B N   
2986 C CA  . GLN B 13  ? 1.92173 2.24446 1.91124 -0.14533 -0.35184 0.48471  169 GLN B CA  
2987 C C   . GLN B 13  ? 1.99471 2.32990 2.00382 -0.13533 -0.34143 0.51255  169 GLN B C   
2988 O O   . GLN B 13  ? 1.99058 2.34079 2.02859 -0.13630 -0.34845 0.52533  169 GLN B O   
2989 C CB  . GLN B 13  ? 1.92892 2.21373 1.87264 -0.15093 -0.36677 0.46675  169 GLN B CB  
2990 C CG  . GLN B 13  ? 1.97120 2.24542 1.91603 -0.15625 -0.38705 0.46700  169 GLN B CG  
2991 C CD  . GLN B 13  ? 1.87606 2.15600 1.83684 -0.16551 -0.39929 0.45356  169 GLN B CD  
2992 O OE1 . GLN B 13  ? 1.72702 2.03337 1.72318 -0.16596 -0.39443 0.46177  169 GLN B OE1 
2993 N NE2 . GLN B 13  ? 1.84628 2.10048 1.78057 -0.17240 -0.41373 0.43306  169 GLN B NE2 
2994 N N   . VAL B 14  ? 1.97547 2.30396 1.96900 -0.12571 -0.32313 0.52195  170 VAL B N   
2995 C CA  . VAL B 14  ? 1.93562 2.27262 1.94491 -0.11452 -0.30931 0.54721  170 VAL B CA  
2996 C C   . VAL B 14  ? 1.91615 2.23898 1.91851 -0.11667 -0.32750 0.55316  170 VAL B C   
2997 O O   . VAL B 14  ? 1.80797 2.10731 1.78155 -0.11222 -0.32581 0.55652  170 VAL B O   
2998 C CB  . VAL B 14  ? 1.89063 2.26676 1.95097 -0.10824 -0.29444 0.56488  170 VAL B CB  
2999 C CG1 . VAL B 14  ? 1.78578 2.17020 1.86395 -0.09732 -0.28195 0.58925  170 VAL B CG1 
3000 C CG2 . VAL B 14  ? 1.76730 2.15233 1.83616 -0.10304 -0.26618 0.54979  170 VAL B CG2 
3001 N N   . SER B 30  ? 1.96329 1.62678 1.61476 -0.22187 0.41068  -0.10866 210 SER B N   
3002 C CA  . SER B 30  ? 2.10290 1.78596 1.77872 -0.21730 0.39201  -0.12392 210 SER B CA  
3003 C C   . SER B 30  ? 2.10148 1.79185 1.80705 -0.21425 0.36888  -0.11969 210 SER B C   
3004 O O   . SER B 30  ? 2.13975 1.84410 1.86344 -0.20648 0.35474  -0.12436 210 SER B O   
3005 C CB  . SER B 30  ? 2.10665 1.79654 1.78591 -0.22446 0.38995  -0.14281 210 SER B CB  
3006 O OG  . SER B 30  ? 2.01030 1.69502 1.69861 -0.23314 0.38317  -0.14261 210 SER B OG  
3007 N N   . ILE B 31  ? 2.07888 1.75981 1.78938 -0.22048 0.36505  -0.11108 211 ILE B N   
3008 C CA  . ILE B 31  ? 2.04308 1.72954 1.78146 -0.21904 0.34335  -0.10697 211 ILE B CA  
3009 C C   . ILE B 31  ? 1.99498 1.66563 1.72571 -0.21988 0.34895  -0.08614 211 ILE B C   
3010 O O   . ILE B 31  ? 1.84186 1.49782 1.55555 -0.22752 0.36216  -0.07979 211 ILE B O   
3011 C CB  . ILE B 31  ? 1.99636 1.68927 1.75340 -0.22667 0.32922  -0.12004 211 ILE B CB  
3012 C CG1 . ILE B 31  ? 2.10834 1.81556 1.86995 -0.22670 0.32613  -0.14089 211 ILE B CG1 
3013 C CG2 . ILE B 31  ? 1.98698 1.68785 1.77456 -0.22434 0.30539  -0.11760 211 ILE B CG2 
3014 C CD1 . ILE B 31  ? 2.07105 1.79635 1.85330 -0.21724 0.31013  -0.14873 211 ILE B CD1 
3015 N N   . CYS B 32  ? 2.11409 1.78778 1.85724 -0.21198 0.33909  -0.07556 212 CYS B N   
3016 C CA  . CYS B 32  ? 1.95846 1.61904 1.69808 -0.21149 0.34161  -0.05561 212 CYS B CA  
3017 C C   . CYS B 32  ? 1.86881 1.53256 1.63537 -0.21300 0.32068  -0.05211 212 CYS B C   
3018 O O   . CYS B 32  ? 1.76859 1.41930 1.53112 -0.21709 0.32368  -0.03856 212 CYS B O   
3019 C CB  . CYS B 32  ? 1.84486 1.50519 1.57826 -0.20134 0.34621  -0.04426 212 CYS B CB  
3020 S SG  . CYS B 32  ? 1.95644 1.61171 1.65738 -0.19798 0.37121  -0.04467 212 CYS B SG  
3021 N N   . LEU B 33  ? 1.73776 1.41839 1.53158 -0.20956 0.29963  -0.06350 213 LEU B N   
3022 C CA  . LEU B 33  ? 1.63060 1.31562 1.45156 -0.21054 0.27850  -0.06118 213 LEU B CA  
3023 C C   . LEU B 33  ? 1.66619 1.36664 1.50897 -0.21312 0.26175  -0.08051 213 LEU B C   
3024 O O   . LEU B 33  ? 1.74754 1.45708 1.58665 -0.21221 0.26484  -0.09504 213 LEU B O   
3025 C CB  . LEU B 33  ? 1.53781 1.22763 1.37317 -0.20094 0.26722  -0.05034 213 LEU B CB  
3026 C CG  . LEU B 33  ? 1.60272 1.31111 1.45690 -0.19170 0.25271  -0.05998 213 LEU B CG  
3027 C CD1 . LEU B 33  ? 1.49668 1.21000 1.37512 -0.18608 0.23381  -0.05083 213 LEU B CD1 
3028 C CD2 . LEU B 33  ? 1.60093 1.31036 1.43615 -0.18474 0.26738  -0.05978 213 LEU B CD2 
3029 N N   . SER B 34  ? 1.57663 1.28013 1.44285 -0.21637 0.24344  -0.08064 214 SER B N   
3030 C CA  . SER B 34  ? 1.54018 1.25753 1.42911 -0.21956 0.22595  -0.09805 214 SER B CA  
3031 C C   . SER B 34  ? 1.71263 1.44864 1.62202 -0.21098 0.21026  -0.10801 214 SER B C   
3032 O O   . SER B 34  ? 1.79046 1.53856 1.72190 -0.21288 0.19325  -0.12119 214 SER B O   
3033 C CB  . SER B 34  ? 1.47259 1.18679 1.37994 -0.22530 0.21135  -0.09385 214 SER B CB  
3034 O OG  . SER B 34  ? 1.45735 1.18349 1.38482 -0.22938 0.19582  -0.11057 214 SER B OG  
3035 N N   . ASP B 35  ? 1.82130 1.55956 1.72403 -0.20198 0.21542  -0.10199 215 ASP B N   
3036 C CA  . ASP B 35  ? 1.87543 1.63107 1.79632 -0.19298 0.20144  -0.11029 215 ASP B CA  
3037 C C   . ASP B 35  ? 1.98533 1.74873 1.89393 -0.19036 0.21121  -0.12379 215 ASP B C   
3038 O O   . ASP B 35  ? 2.06064 1.84012 1.98558 -0.18438 0.19866  -0.13485 215 ASP B O   
3039 C CB  . ASP B 35  ? 1.84478 1.59864 1.76903 -0.18416 0.19863  -0.09440 215 ASP B CB  
3040 C CG  . ASP B 35  ? 2.02170 1.79079 1.95607 -0.17388 0.19082  -0.10079 215 ASP B CG  
3041 O OD1 . ASP B 35  ? 2.03043 1.79934 1.94589 -0.17027 0.20547  -0.10308 215 ASP B OD1 
3042 O OD2 . ASP B 35  ? 1.97307 1.75415 1.93423 -0.16936 0.17004  -0.10326 215 ASP B OD2 
3043 N N   . GLU B 36  ? 1.97940 1.73205 1.86010 -0.19485 0.23291  -0.12366 216 GLU B N   
3044 C CA  . GLU B 36  ? 2.06617 1.82558 1.93425 -0.19298 0.24292  -0.13676 216 GLU B CA  
3045 C C   . GLU B 36  ? 2.11852 1.88613 1.99350 -0.19965 0.23802  -0.15594 216 GLU B C   
3046 O O   . GLU B 36  ? 2.13126 1.90665 1.99924 -0.19796 0.24371  -0.16867 216 GLU B O   
3047 C CB  . GLU B 36  ? 2.04974 1.79406 1.88410 -0.19433 0.26893  -0.12790 216 GLU B CB  
3048 C CG  . GLU B 36  ? 1.97675 1.70754 1.80201 -0.19194 0.27563  -0.10693 216 GLU B CG  
3049 C CD  . GLU B 36  ? 2.06223 1.77789 1.85430 -0.19370 0.30123  -0.09841 216 GLU B CD  
3050 O OE1 . GLU B 36  ? 2.10603 1.82501 1.88404 -0.18915 0.31206  -0.10317 216 GLU B OE1 
3051 O OE2 . GLU B 36  ? 2.14065 1.84097 1.92056 -0.19977 0.31060  -0.08698 216 GLU B OE2 
3052 N N   . LEU B 37  ? 2.12610 1.89140 2.01307 -0.20741 0.22880  -0.15804 217 LEU B N   
3053 C CA  . LEU B 37  ? 2.21792 1.99166 2.11528 -0.21386 0.22119  -0.17602 217 LEU B CA  
3054 C C   . LEU B 37  ? 2.22853 2.02140 2.15793 -0.20998 0.19652  -0.18865 217 LEU B C   
3055 O O   . LEU B 37  ? 2.27324 2.07774 2.20743 -0.21050 0.19329  -0.20587 217 LEU B O   
3056 C CB  . LEU B 37  ? 2.17922 1.94032 2.07247 -0.22433 0.22430  -0.17184 217 LEU B CB  
3057 C CG  . LEU B 37  ? 2.17159 1.91438 2.03207 -0.22748 0.24957  -0.15980 217 LEU B CG  
3058 C CD1 . LEU B 37  ? 2.14288 1.87043 1.99992 -0.23398 0.25185  -0.14591 217 LEU B CD1 
3059 C CD2 . LEU B 37  ? 2.27154 2.01288 2.11190 -0.23255 0.26564  -0.17211 217 LEU B CD2 
3060 N N   . PRO B 38  ? 2.07390 1.87084 2.02610 -0.20619 0.17850  -0.18118 218 PRO B N   
3061 C CA  . PRO B 38  ? 1.98829 1.80355 1.97143 -0.20255 0.15467  -0.19329 218 PRO B CA  
3062 C C   . PRO B 38  ? 1.94333 1.77441 1.93148 -0.19459 0.15109  -0.20557 218 PRO B C   
3063 O O   . PRO B 38  ? 1.82654 1.67227 1.83293 -0.19468 0.13732  -0.22182 218 PRO B O   
3064 C CB  . PRO B 38  ? 1.86088 1.67483 1.86068 -0.19810 0.14127  -0.17882 218 PRO B CB  
3065 C CG  . PRO B 38  ? 1.81476 1.60993 1.79919 -0.20442 0.15286  -0.16366 218 PRO B CG  
3066 C CD  . PRO B 38  ? 1.98863 1.77281 1.94038 -0.20683 0.17836  -0.16210 218 PRO B CD  
3067 O OXT . PRO B 38  ? 1.98362 1.81350 1.95828 -0.18775 0.16140  -0.19967 218 PRO B OXT 
# 
