data_9ERV
# 
_entry.id   9ERV 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.399 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   9ERV         pdb_00009erv 10.2210/pdb9erv/pdb 
WWPDB D_1292137545 ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
1 'Structure model' 1 0 2024-11-06 
2 'Structure model' 1 1 2024-11-27 
3 'Structure model' 1 2 2024-12-04 
# 
_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' struct_ref      
2 2 'Structure model' struct_ref_seq  
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' '_struct_ref.db_code'                  
2  2 'Structure model' '_struct_ref.db_name'                  
3  2 'Structure model' '_struct_ref.pdbx_align_begin'         
4  2 'Structure model' '_struct_ref.pdbx_db_accession'        
5  2 'Structure model' '_struct_ref.pdbx_seq_one_letter_code' 
6  2 'Structure model' '_struct_ref_seq.pdbx_db_accession'    
7  3 'Structure model' '_citation.journal_volume'             
8  3 'Structure model' '_citation.page_first'                 
9  3 'Structure model' '_citation.page_last'                  
10 3 'Structure model' '_citation_author.identifier_ORCID'    
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9ERV 
_pdbx_database_status.recvd_initial_deposition_date   2024-03-25 
_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_contact_author.id                 2 
_pdbx_contact_author.email              abel.garcia.pino@ulb.be 
_pdbx_contact_author.name_first         Abel 
_pdbx_contact_author.name_last          Garcia-Pino 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-0634-0300 
# 
_audit_author.name               'Garcia-Pino, A.' 
_audit_author.pdbx_ordinal       1 
_audit_author.identifier_ORCID   0000-0002-0634-0300 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   UK 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            Nature 
_citation.journal_id_ASTM           NATUAS 
_citation.journal_id_CSD            0006 
_citation.journal_id_ISSN           1476-4687 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            635 
_citation.language                  ? 
_citation.page_first                728 
_citation.page_last                 735 
_citation.title                     'A bacterial immunity protein directly senses two disparate phage proteins.' 
_citation.year                      2024 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1038/s41586-024-08039-y 
_citation.pdbx_database_id_PubMed   39415022 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Zhang, T.'                 1 ? 
primary 'Cepauskas, A.'             2 ? 
primary 'Nadieina, A.'              3 ? 
primary 'Thureau, A.'               4 ? 
primary 
;Coppieters 't Wallant, K.
;
5 ? 
primary 'Martens, C.'               6 ? 
primary 'Lim, D.C.'                 7 ? 
primary 'Garcia-Pino, A.'           8 ? 
primary 'Laub, M.T.'                9 ? 
# 
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 'RelA/SpoT family protein'  42710.121 1   ? ? ? ? 
2 polymer     man GP54                        8971.309  1   ? ? ? ? 
3 non-polymer syn GLYCEROL                    92.094    1   ? ? ? ? 
4 non-polymer syn "ADENOSINE-5'-TRIPHOSPHATE" 507.181   1   ? ? ? ? 
5 non-polymer syn 'MAGNESIUM ION'             24.305    1   ? ? ? ? 
6 non-polymer syn 'SODIUM ION'                22.990    1   ? ? ? ? 
7 water       nat water                       18.015    354 ? ? ? ? 
# 
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 
;GSEVYQSQKCELKYSKSQIEKAARKIRHGCEGAEREEAIKMIQNFRELHLYPLMLMKNHLDRAAKKVDKENKIIVARRLK
RLSTIIDKLERPSLDGGATNNAIALTRMQDIGGCRAIVRNIEQLKKLKDRLVKSRSKHKILKEYDYLTPKPSGYSGIHLA
YSCFDEENGNNPWSKTKIEVQLRTELQHAWATSLEIIDTLENIKLKTSNEGHPEWRRFFYLSGCLVAHDEGACILDDETI
KNYQTELKTLEEALSVRSKLSTYTFAMKLTSDANLKKSLPKNHNGFFLVRMRNAITKNGKDTGKFLVSVKPFRKKESEQA
LQELNKDDADPEVLIAVLLATNNIKSLKKAYPNYFGSTNQFGRFLSRHIDTV
;
;GSEVYQSQKCELKYSKSQIEKAARKIRHGCEGAEREEAIKMIQNFRELHLYPLMLMKNHLDRAAKKVDKENKIIVARRLK
RLSTIIDKLERPSLDGGATNNAIALTRMQDIGGCRAIVRNIEQLKKLKDRLVKSRSKHKILKEYDYLTPKPSGYSGIHLA
YSCFDEENGNNPWSKTKIEVQLRTELQHAWATSLEIIDTLENIKLKTSNEGHPEWRRFFYLSGCLVAHDEGACILDDETI
KNYQTELKTLEEALSVRSKLSTYTFAMKLTSDANLKKSLPKNHNGFFLVRMRNAITKNGKDTGKFLVSVKPFRKKESEQA
LQELNKDDADPEVLIAVLLATNNIKSLKKAYPNYFGSTNQFGRFLSRHIDTV
;
A ? 
2 'polypeptide(L)' no no MKHHHHHHGSSGMQDQIDAKVIRRNPELTPGIFKKGIEITIDLEEMVCYHSGLTWKVKQLTNTLWSLAGDEHTVMEVI 
MKHHHHHHGSSGMQDQIDAKVIRRNPELTPGIFKKGIEITIDLEEMVCYHSGLTWKVKQLTNTLWSLAGDEHTVMEVI B ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
3 GLYCEROL                    GOL 
4 "ADENOSINE-5'-TRIPHOSPHATE" ATP 
5 'MAGNESIUM ION'             MG  
6 'SODIUM ION'                NA  
7 water                       HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   GLY n 
1 2   SER n 
1 3   GLU n 
1 4   VAL n 
1 5   TYR n 
1 6   GLN n 
1 7   SER n 
1 8   GLN n 
1 9   LYS n 
1 10  CYS n 
1 11  GLU n 
1 12  LEU n 
1 13  LYS n 
1 14  TYR n 
1 15  SER n 
1 16  LYS n 
1 17  SER n 
1 18  GLN n 
1 19  ILE n 
1 20  GLU n 
1 21  LYS n 
1 22  ALA n 
1 23  ALA n 
1 24  ARG n 
1 25  LYS n 
1 26  ILE n 
1 27  ARG n 
1 28  HIS n 
1 29  GLY n 
1 30  CYS n 
1 31  GLU n 
1 32  GLY n 
1 33  ALA n 
1 34  GLU n 
1 35  ARG n 
1 36  GLU n 
1 37  GLU n 
1 38  ALA n 
1 39  ILE n 
1 40  LYS n 
1 41  MET n 
1 42  ILE n 
1 43  GLN n 
1 44  ASN n 
1 45  PHE n 
1 46  ARG n 
1 47  GLU n 
1 48  LEU n 
1 49  HIS n 
1 50  LEU n 
1 51  TYR n 
1 52  PRO n 
1 53  LEU n 
1 54  MET n 
1 55  LEU n 
1 56  MET n 
1 57  LYS n 
1 58  ASN n 
1 59  HIS n 
1 60  LEU n 
1 61  ASP n 
1 62  ARG n 
1 63  ALA n 
1 64  ALA n 
1 65  LYS n 
1 66  LYS n 
1 67  VAL n 
1 68  ASP n 
1 69  LYS n 
1 70  GLU n 
1 71  ASN n 
1 72  LYS n 
1 73  ILE n 
1 74  ILE n 
1 75  VAL n 
1 76  ALA n 
1 77  ARG n 
1 78  ARG n 
1 79  LEU n 
1 80  LYS n 
1 81  ARG n 
1 82  LEU n 
1 83  SER n 
1 84  THR n 
1 85  ILE n 
1 86  ILE n 
1 87  ASP n 
1 88  LYS n 
1 89  LEU n 
1 90  GLU n 
1 91  ARG n 
1 92  PRO n 
1 93  SER n 
1 94  LEU n 
1 95  ASP n 
1 96  GLY n 
1 97  GLY n 
1 98  ALA n 
1 99  THR n 
1 100 ASN n 
1 101 ASN n 
1 102 ALA n 
1 103 ILE n 
1 104 ALA n 
1 105 LEU n 
1 106 THR n 
1 107 ARG n 
1 108 MET n 
1 109 GLN n 
1 110 ASP n 
1 111 ILE n 
1 112 GLY n 
1 113 GLY n 
1 114 CYS n 
1 115 ARG n 
1 116 ALA n 
1 117 ILE n 
1 118 VAL n 
1 119 ARG n 
1 120 ASN n 
1 121 ILE n 
1 122 GLU n 
1 123 GLN n 
1 124 LEU n 
1 125 LYS n 
1 126 LYS n 
1 127 LEU n 
1 128 LYS n 
1 129 ASP n 
1 130 ARG n 
1 131 LEU n 
1 132 VAL n 
1 133 LYS n 
1 134 SER n 
1 135 ARG n 
1 136 SER n 
1 137 LYS n 
1 138 HIS n 
1 139 LYS n 
1 140 ILE n 
1 141 LEU n 
1 142 LYS n 
1 143 GLU n 
1 144 TYR n 
1 145 ASP n 
1 146 TYR n 
1 147 LEU n 
1 148 THR n 
1 149 PRO n 
1 150 LYS n 
1 151 PRO n 
1 152 SER n 
1 153 GLY n 
1 154 TYR n 
1 155 SER n 
1 156 GLY n 
1 157 ILE n 
1 158 HIS n 
1 159 LEU n 
1 160 ALA n 
1 161 TYR n 
1 162 SER n 
1 163 CYS n 
1 164 PHE n 
1 165 ASP n 
1 166 GLU n 
1 167 GLU n 
1 168 ASN n 
1 169 GLY n 
1 170 ASN n 
1 171 ASN n 
1 172 PRO n 
1 173 TRP n 
1 174 SER n 
1 175 LYS n 
1 176 THR n 
1 177 LYS n 
1 178 ILE n 
1 179 GLU n 
1 180 VAL n 
1 181 GLN n 
1 182 LEU n 
1 183 ARG n 
1 184 THR n 
1 185 GLU n 
1 186 LEU n 
1 187 GLN n 
1 188 HIS n 
1 189 ALA n 
1 190 TRP n 
1 191 ALA n 
1 192 THR n 
1 193 SER n 
1 194 LEU n 
1 195 GLU n 
1 196 ILE n 
1 197 ILE n 
1 198 ASP n 
1 199 THR n 
1 200 LEU n 
1 201 GLU n 
1 202 ASN n 
1 203 ILE n 
1 204 LYS n 
1 205 LEU n 
1 206 LYS n 
1 207 THR n 
1 208 SER n 
1 209 ASN n 
1 210 GLU n 
1 211 GLY n 
1 212 HIS n 
1 213 PRO n 
1 214 GLU n 
1 215 TRP n 
1 216 ARG n 
1 217 ARG n 
1 218 PHE n 
1 219 PHE n 
1 220 TYR n 
1 221 LEU n 
1 222 SER n 
1 223 GLY n 
1 224 CYS n 
1 225 LEU n 
1 226 VAL n 
1 227 ALA n 
1 228 HIS n 
1 229 ASP n 
1 230 GLU n 
1 231 GLY n 
1 232 ALA n 
1 233 CYS n 
1 234 ILE n 
1 235 LEU n 
1 236 ASP n 
1 237 ASP n 
1 238 GLU n 
1 239 THR n 
1 240 ILE n 
1 241 LYS n 
1 242 ASN n 
1 243 TYR n 
1 244 GLN n 
1 245 THR n 
1 246 GLU n 
1 247 LEU n 
1 248 LYS n 
1 249 THR n 
1 250 LEU n 
1 251 GLU n 
1 252 GLU n 
1 253 ALA n 
1 254 LEU n 
1 255 SER n 
1 256 VAL n 
1 257 ARG n 
1 258 SER n 
1 259 LYS n 
1 260 LEU n 
1 261 SER n 
1 262 THR n 
1 263 TYR n 
1 264 THR n 
1 265 PHE n 
1 266 ALA n 
1 267 MET n 
1 268 LYS n 
1 269 LEU n 
1 270 THR n 
1 271 SER n 
1 272 ASP n 
1 273 ALA n 
1 274 ASN n 
1 275 LEU n 
1 276 LYS n 
1 277 LYS n 
1 278 SER n 
1 279 LEU n 
1 280 PRO n 
1 281 LYS n 
1 282 ASN n 
1 283 HIS n 
1 284 ASN n 
1 285 GLY n 
1 286 PHE n 
1 287 PHE n 
1 288 LEU n 
1 289 VAL n 
1 290 ARG n 
1 291 MET n 
1 292 ARG n 
1 293 ASN n 
1 294 ALA n 
1 295 ILE n 
1 296 THR n 
1 297 LYS n 
1 298 ASN n 
1 299 GLY n 
1 300 LYS n 
1 301 ASP n 
1 302 THR n 
1 303 GLY n 
1 304 LYS n 
1 305 PHE n 
1 306 LEU n 
1 307 VAL n 
1 308 SER n 
1 309 VAL n 
1 310 LYS n 
1 311 PRO n 
1 312 PHE n 
1 313 ARG n 
1 314 LYS n 
1 315 LYS n 
1 316 GLU n 
1 317 SER n 
1 318 GLU n 
1 319 GLN n 
1 320 ALA n 
1 321 LEU n 
1 322 GLN n 
1 323 GLU n 
1 324 LEU n 
1 325 ASN n 
1 326 LYS n 
1 327 ASP n 
1 328 ASP n 
1 329 ALA n 
1 330 ASP n 
1 331 PRO n 
1 332 GLU n 
1 333 VAL n 
1 334 LEU n 
1 335 ILE n 
1 336 ALA n 
1 337 VAL n 
1 338 LEU n 
1 339 LEU n 
1 340 ALA n 
1 341 THR n 
1 342 ASN n 
1 343 ASN n 
1 344 ILE n 
1 345 LYS n 
1 346 SER n 
1 347 LEU n 
1 348 LYS n 
1 349 LYS n 
1 350 ALA n 
1 351 TYR n 
1 352 PRO n 
1 353 ASN n 
1 354 TYR n 
1 355 PHE n 
1 356 GLY n 
1 357 SER n 
1 358 THR n 
1 359 ASN n 
1 360 GLN n 
1 361 PHE n 
1 362 GLY n 
1 363 ARG n 
1 364 PHE n 
1 365 LEU n 
1 366 SER n 
1 367 ARG n 
1 368 HIS n 
1 369 ILE n 
1 370 ASP n 
1 371 THR n 
1 372 VAL n 
2 1   MET n 
2 2   LYS n 
2 3   HIS n 
2 4   HIS n 
2 5   HIS n 
2 6   HIS n 
2 7   HIS n 
2 8   HIS n 
2 9   GLY n 
2 10  SER n 
2 11  SER n 
2 12  GLY n 
2 13  MET n 
2 14  GLN n 
2 15  ASP n 
2 16  GLN n 
2 17  ILE n 
2 18  ASP n 
2 19  ALA n 
2 20  LYS n 
2 21  VAL n 
2 22  ILE n 
2 23  ARG n 
2 24  ARG n 
2 25  ASN n 
2 26  PRO n 
2 27  GLU n 
2 28  LEU n 
2 29  THR n 
2 30  PRO n 
2 31  GLY n 
2 32  ILE n 
2 33  PHE n 
2 34  LYS n 
2 35  LYS n 
2 36  GLY n 
2 37  ILE n 
2 38  GLU n 
2 39  ILE n 
2 40  THR n 
2 41  ILE n 
2 42  ASP n 
2 43  LEU n 
2 44  GLU n 
2 45  GLU n 
2 46  MET n 
2 47  VAL n 
2 48  CYS n 
2 49  TYR n 
2 50  HIS n 
2 51  SER n 
2 52  GLY n 
2 53  LEU n 
2 54  THR n 
2 55  TRP n 
2 56  LYS n 
2 57  VAL n 
2 58  LYS n 
2 59  GLN n 
2 60  LEU n 
2 61  THR n 
2 62  ASN n 
2 63  THR n 
2 64  LEU n 
2 65  TRP n 
2 66  SER n 
2 67  LEU n 
2 68  ALA n 
2 69  GLY n 
2 70  ASP n 
2 71  GLU n 
2 72  HIS n 
2 73  THR n 
2 74  VAL n 
2 75  MET n 
2 76  GLU n 
2 77  VAL n 
2 78  ILE 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' 1 372 ? ? J46_0058 ? ? ? ? ? ? Salmonella          590   ? ? ? ? ? ? ? ? 
;Escherichia coli 'BL21-Gold(DE3)pLysS AG'
;
866768 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
2 1 sample 'Biological sequence' 1 78  ? ? ?        ? ? ? ? ? ? 'Bacteriophage sp.' 38018 ? ? ? ? ? ? ? ? 
;Escherichia coli 'BL21-Gold(DE3)pLysS AG'
;
866768 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE                     ?                               'C3 H7 N O2'        89.093  
ARG 'L-peptide linking' y ARGININE                    ?                               'C6 H15 N4 O2 1'    175.209 
ASN 'L-peptide linking' y ASPARAGINE                  ?                               'C4 H8 N2 O3'       132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'             ?                               'C4 H7 N O4'        133.103 
ATP non-polymer         . "ADENOSINE-5'-TRIPHOSPHATE" ?                               'C10 H16 N5 O13 P3' 507.181 
CYS 'L-peptide linking' y CYSTEINE                    ?                               'C3 H7 N O2 S'      121.158 
GLN 'L-peptide linking' y GLUTAMINE                   ?                               'C5 H10 N2 O3'      146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'             ?                               'C5 H9 N O4'        147.129 
GLY 'peptide linking'   y GLYCINE                     ?                               'C2 H5 N O2'        75.067  
GOL non-polymer         . GLYCEROL                    'GLYCERIN; PROPANE-1,2,3-TRIOL' 'C3 H8 O3'          92.094  
HIS 'L-peptide linking' y HISTIDINE                   ?                               'C6 H10 N3 O2 1'    156.162 
HOH non-polymer         . WATER                       ?                               'H2 O'              18.015  
ILE 'L-peptide linking' y ISOLEUCINE                  ?                               'C6 H13 N O2'       131.173 
LEU 'L-peptide linking' y LEUCINE                     ?                               'C6 H13 N O2'       131.173 
LYS 'L-peptide linking' y LYSINE                      ?                               'C6 H15 N2 O2 1'    147.195 
MET 'L-peptide linking' y METHIONINE                  ?                               'C5 H11 N O2 S'     149.211 
MG  non-polymer         . 'MAGNESIUM ION'             ?                               'Mg 2'              24.305  
NA  non-polymer         . 'SODIUM ION'                ?                               'Na 1'              22.990  
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   GLY 1   2   ?   ?   ?   A . n 
A 1 2   SER 2   3   ?   ?   ?   A . n 
A 1 3   GLU 3   4   ?   ?   ?   A . n 
A 1 4   VAL 4   5   ?   ?   ?   A . n 
A 1 5   TYR 5   6   ?   ?   ?   A . n 
A 1 6   GLN 6   7   ?   ?   ?   A . n 
A 1 7   SER 7   8   ?   ?   ?   A . n 
A 1 8   GLN 8   9   ?   ?   ?   A . n 
A 1 9   LYS 9   10  ?   ?   ?   A . n 
A 1 10  CYS 10  11  ?   ?   ?   A . n 
A 1 11  GLU 11  12  ?   ?   ?   A . n 
A 1 12  LEU 12  13  13  LEU LEU A . n 
A 1 13  LYS 13  14  14  LYS LYS A . n 
A 1 14  TYR 14  15  15  TYR TYR A . n 
A 1 15  SER 15  16  16  SER SER A . n 
A 1 16  LYS 16  17  17  LYS LYS A . n 
A 1 17  SER 17  18  18  SER SER A . n 
A 1 18  GLN 18  19  19  GLN GLN A . n 
A 1 19  ILE 19  20  20  ILE ILE A . n 
A 1 20  GLU 20  21  21  GLU GLU A . n 
A 1 21  LYS 21  22  22  LYS LYS A . n 
A 1 22  ALA 22  23  23  ALA ALA A . n 
A 1 23  ALA 23  24  24  ALA ALA A . n 
A 1 24  ARG 24  25  25  ARG ARG A . n 
A 1 25  LYS 25  26  26  LYS LYS A . n 
A 1 26  ILE 26  27  27  ILE ILE A . n 
A 1 27  ARG 27  28  28  ARG ARG A . n 
A 1 28  HIS 28  29  29  HIS HIS A . n 
A 1 29  GLY 29  30  30  GLY GLY A . n 
A 1 30  CYS 30  31  31  CYS CYS A . n 
A 1 31  GLU 31  32  32  GLU GLU A . n 
A 1 32  GLY 32  33  33  GLY GLY A . n 
A 1 33  ALA 33  34  34  ALA ALA A . n 
A 1 34  GLU 34  35  35  GLU GLU A . n 
A 1 35  ARG 35  36  36  ARG ARG A . n 
A 1 36  GLU 36  37  37  GLU GLU A . n 
A 1 37  GLU 37  38  38  GLU GLU A . n 
A 1 38  ALA 38  39  39  ALA ALA A . n 
A 1 39  ILE 39  40  40  ILE ILE A . n 
A 1 40  LYS 40  41  41  LYS LYS A . n 
A 1 41  MET 41  42  42  MET MET A . n 
A 1 42  ILE 42  43  43  ILE ILE A . n 
A 1 43  GLN 43  44  44  GLN GLN A . n 
A 1 44  ASN 44  45  45  ASN ASN A . n 
A 1 45  PHE 45  46  46  PHE PHE A . n 
A 1 46  ARG 46  47  47  ARG ARG A . n 
A 1 47  GLU 47  48  48  GLU GLU A . n 
A 1 48  LEU 48  49  49  LEU LEU A . n 
A 1 49  HIS 49  50  50  HIS HIS A . n 
A 1 50  LEU 50  51  51  LEU LEU A . n 
A 1 51  TYR 51  52  52  TYR TYR A . n 
A 1 52  PRO 52  53  53  PRO PRO A . n 
A 1 53  LEU 53  54  54  LEU LEU A . n 
A 1 54  MET 54  55  55  MET MET A . n 
A 1 55  LEU 55  56  56  LEU LEU A . n 
A 1 56  MET 56  57  57  MET MET A . n 
A 1 57  LYS 57  58  58  LYS LYS A . n 
A 1 58  ASN 58  59  59  ASN ASN A . n 
A 1 59  HIS 59  60  60  HIS HIS A . n 
A 1 60  LEU 60  61  61  LEU LEU A . n 
A 1 61  ASP 61  62  62  ASP ASP A . n 
A 1 62  ARG 62  63  63  ARG ARG A . n 
A 1 63  ALA 63  64  64  ALA ALA A . n 
A 1 64  ALA 64  65  65  ALA ALA A . n 
A 1 65  LYS 65  66  66  LYS LYS A . n 
A 1 66  LYS 66  67  67  LYS LYS A . n 
A 1 67  VAL 67  68  68  VAL VAL A . n 
A 1 68  ASP 68  69  69  ASP ASP A . n 
A 1 69  LYS 69  70  70  LYS LYS A . n 
A 1 70  GLU 70  71  71  GLU GLU A . n 
A 1 71  ASN 71  72  72  ASN ASN A . n 
A 1 72  LYS 72  73  73  LYS LYS A . n 
A 1 73  ILE 73  74  74  ILE ILE A . n 
A 1 74  ILE 74  75  75  ILE ILE A . n 
A 1 75  VAL 75  76  76  VAL VAL A . n 
A 1 76  ALA 76  77  77  ALA ALA A . n 
A 1 77  ARG 77  78  78  ARG ARG A . n 
A 1 78  ARG 78  79  79  ARG ARG A . n 
A 1 79  LEU 79  80  80  LEU LEU A . n 
A 1 80  LYS 80  81  81  LYS LYS A . n 
A 1 81  ARG 81  82  82  ARG ARG A . n 
A 1 82  LEU 82  83  83  LEU LEU A . n 
A 1 83  SER 83  84  84  SER SER A . n 
A 1 84  THR 84  85  85  THR THR A . n 
A 1 85  ILE 85  86  86  ILE ILE A . n 
A 1 86  ILE 86  87  87  ILE ILE A . n 
A 1 87  ASP 87  88  88  ASP ASP A . n 
A 1 88  LYS 88  89  89  LYS LYS A . n 
A 1 89  LEU 89  90  90  LEU LEU A . n 
A 1 90  GLU 90  91  91  GLU GLU A . n 
A 1 91  ARG 91  92  92  ARG ARG A . n 
A 1 92  PRO 92  93  ?   ?   ?   A . n 
A 1 93  SER 93  94  ?   ?   ?   A . n 
A 1 94  LEU 94  95  ?   ?   ?   A . n 
A 1 95  ASP 95  96  ?   ?   ?   A . n 
A 1 96  GLY 96  97  ?   ?   ?   A . n 
A 1 97  GLY 97  98  ?   ?   ?   A . n 
A 1 98  ALA 98  99  ?   ?   ?   A . n 
A 1 99  THR 99  100 ?   ?   ?   A . n 
A 1 100 ASN 100 101 ?   ?   ?   A . n 
A 1 101 ASN 101 102 ?   ?   ?   A . n 
A 1 102 ALA 102 103 103 ALA ALA A . n 
A 1 103 ILE 103 104 104 ILE ILE A . n 
A 1 104 ALA 104 105 105 ALA ALA A . n 
A 1 105 LEU 105 106 106 LEU LEU A . n 
A 1 106 THR 106 107 107 THR THR A . n 
A 1 107 ARG 107 108 108 ARG ARG A . n 
A 1 108 MET 108 109 109 MET MET A . n 
A 1 109 GLN 109 110 110 GLN GLN A . n 
A 1 110 ASP 110 111 111 ASP ASP A . n 
A 1 111 ILE 111 112 112 ILE ILE A . n 
A 1 112 GLY 112 113 113 GLY GLY A . n 
A 1 113 GLY 113 114 114 GLY GLY A . n 
A 1 114 CYS 114 115 115 CYS CYS A . n 
A 1 115 ARG 115 116 116 ARG ARG A . n 
A 1 116 ALA 116 117 117 ALA ALA A . n 
A 1 117 ILE 117 118 118 ILE ILE A . n 
A 1 118 VAL 118 119 119 VAL VAL A . n 
A 1 119 ARG 119 120 120 ARG ARG A . n 
A 1 120 ASN 120 121 121 ASN ASN A . n 
A 1 121 ILE 121 122 122 ILE ILE A . n 
A 1 122 GLU 122 123 123 GLU GLU A . n 
A 1 123 GLN 123 124 124 GLN GLN A . n 
A 1 124 LEU 124 125 125 LEU LEU A . n 
A 1 125 LYS 125 126 126 LYS LYS A . n 
A 1 126 LYS 126 127 127 LYS LYS A . n 
A 1 127 LEU 127 128 128 LEU LEU A . n 
A 1 128 LYS 128 129 129 LYS LYS A . n 
A 1 129 ASP 129 130 130 ASP ASP A . n 
A 1 130 ARG 130 131 131 ARG ARG A . n 
A 1 131 LEU 131 132 132 LEU LEU A . n 
A 1 132 VAL 132 133 133 VAL VAL A . n 
A 1 133 LYS 133 134 134 LYS LYS A . n 
A 1 134 SER 134 135 135 SER SER A . n 
A 1 135 ARG 135 136 136 ARG ARG A . n 
A 1 136 SER 136 137 137 SER SER A . n 
A 1 137 LYS 137 138 138 LYS LYS A . n 
A 1 138 HIS 138 139 139 HIS HIS A . n 
A 1 139 LYS 139 140 140 LYS LYS A . n 
A 1 140 ILE 140 141 141 ILE ILE A . n 
A 1 141 LEU 141 142 142 LEU LEU A . n 
A 1 142 LYS 142 143 143 LYS LYS A . n 
A 1 143 GLU 143 144 144 GLU GLU A . n 
A 1 144 TYR 144 145 145 TYR TYR A . n 
A 1 145 ASP 145 146 146 ASP ASP A . n 
A 1 146 TYR 146 147 147 TYR TYR A . n 
A 1 147 LEU 147 148 148 LEU LEU A . n 
A 1 148 THR 148 149 149 THR THR A . n 
A 1 149 PRO 149 150 150 PRO PRO A . n 
A 1 150 LYS 150 151 151 LYS LYS A . n 
A 1 151 PRO 151 152 152 PRO PRO A . n 
A 1 152 SER 152 153 153 SER SER A . n 
A 1 153 GLY 153 154 154 GLY GLY A . n 
A 1 154 TYR 154 155 155 TYR TYR A . n 
A 1 155 SER 155 156 156 SER SER A . n 
A 1 156 GLY 156 157 157 GLY GLY A . n 
A 1 157 ILE 157 158 158 ILE ILE A . n 
A 1 158 HIS 158 159 159 HIS HIS A . n 
A 1 159 LEU 159 160 160 LEU LEU A . n 
A 1 160 ALA 160 161 161 ALA ALA A . n 
A 1 161 TYR 161 162 162 TYR TYR A . n 
A 1 162 SER 162 163 163 SER SER A . n 
A 1 163 CYS 163 164 164 CYS CYS A . n 
A 1 164 PHE 164 165 165 PHE PHE A . n 
A 1 165 ASP 165 166 166 ASP ASP A . n 
A 1 166 GLU 166 167 167 GLU GLU A . n 
A 1 167 GLU 167 168 168 GLU GLU A . n 
A 1 168 ASN 168 169 169 ASN ASN A . n 
A 1 169 GLY 169 170 170 GLY GLY A . n 
A 1 170 ASN 170 171 171 ASN ASN A . n 
A 1 171 ASN 171 172 172 ASN ASN A . n 
A 1 172 PRO 172 173 173 PRO PRO A . n 
A 1 173 TRP 173 174 174 TRP TRP A . n 
A 1 174 SER 174 175 175 SER SER A . n 
A 1 175 LYS 175 176 176 LYS LYS A . n 
A 1 176 THR 176 177 177 THR THR A . n 
A 1 177 LYS 177 178 178 LYS LYS A . n 
A 1 178 ILE 178 179 179 ILE ILE A . n 
A 1 179 GLU 179 180 180 GLU GLU A . n 
A 1 180 VAL 180 181 181 VAL VAL A . n 
A 1 181 GLN 181 182 182 GLN GLN A . n 
A 1 182 LEU 182 183 183 LEU LEU A . n 
A 1 183 ARG 183 184 184 ARG ARG A . n 
A 1 184 THR 184 185 185 THR THR A . n 
A 1 185 GLU 185 186 186 GLU GLU A . n 
A 1 186 LEU 186 187 187 LEU LEU A . n 
A 1 187 GLN 187 188 188 GLN GLN A . n 
A 1 188 HIS 188 189 189 HIS HIS A . n 
A 1 189 ALA 189 190 190 ALA ALA A . n 
A 1 190 TRP 190 191 191 TRP TRP A . n 
A 1 191 ALA 191 192 192 ALA ALA A . n 
A 1 192 THR 192 193 193 THR THR A . n 
A 1 193 SER 193 194 194 SER SER A . n 
A 1 194 LEU 194 195 195 LEU LEU A . n 
A 1 195 GLU 195 196 196 GLU GLU A . n 
A 1 196 ILE 196 197 197 ILE ILE A . n 
A 1 197 ILE 197 198 198 ILE ILE A . n 
A 1 198 ASP 198 199 199 ASP ASP A . n 
A 1 199 THR 199 200 200 THR THR A . n 
A 1 200 LEU 200 201 201 LEU LEU A . n 
A 1 201 GLU 201 202 202 GLU GLU A . n 
A 1 202 ASN 202 203 203 ASN ASN A . n 
A 1 203 ILE 203 204 204 ILE ILE A . n 
A 1 204 LYS 204 205 205 LYS LYS A . n 
A 1 205 LEU 205 206 206 LEU LEU A . n 
A 1 206 LYS 206 207 207 LYS LYS A . n 
A 1 207 THR 207 208 208 THR THR A . n 
A 1 208 SER 208 209 209 SER SER A . n 
A 1 209 ASN 209 210 210 ASN ASN A . n 
A 1 210 GLU 210 211 211 GLU GLU A . n 
A 1 211 GLY 211 212 212 GLY GLY A . n 
A 1 212 HIS 212 213 213 HIS HIS A . n 
A 1 213 PRO 213 214 214 PRO PRO A . n 
A 1 214 GLU 214 215 215 GLU GLU A . n 
A 1 215 TRP 215 216 216 TRP TRP A . n 
A 1 216 ARG 216 217 217 ARG ARG A . n 
A 1 217 ARG 217 218 218 ARG ARG A . n 
A 1 218 PHE 218 219 219 PHE PHE A . n 
A 1 219 PHE 219 220 220 PHE PHE A . n 
A 1 220 TYR 220 221 221 TYR TYR A . n 
A 1 221 LEU 221 222 222 LEU LEU A . n 
A 1 222 SER 222 223 223 SER SER A . n 
A 1 223 GLY 223 224 224 GLY GLY A . n 
A 1 224 CYS 224 225 225 CYS CYS A . n 
A 1 225 LEU 225 226 226 LEU LEU A . n 
A 1 226 VAL 226 227 227 VAL VAL A . n 
A 1 227 ALA 227 228 228 ALA ALA A . n 
A 1 228 HIS 228 229 229 HIS HIS A . n 
A 1 229 ASP 229 230 230 ASP ASP A . n 
A 1 230 GLU 230 231 231 GLU GLU A . n 
A 1 231 GLY 231 232 232 GLY GLY A . n 
A 1 232 ALA 232 233 233 ALA ALA A . n 
A 1 233 CYS 233 234 234 CYS CYS A . n 
A 1 234 ILE 234 235 235 ILE ILE A . n 
A 1 235 LEU 235 236 236 LEU LEU A . n 
A 1 236 ASP 236 237 237 ASP ASP A . n 
A 1 237 ASP 237 238 238 ASP ASP A . n 
A 1 238 GLU 238 239 239 GLU GLU A . n 
A 1 239 THR 239 240 240 THR THR A . n 
A 1 240 ILE 240 241 241 ILE ILE A . n 
A 1 241 LYS 241 242 242 LYS LYS A . n 
A 1 242 ASN 242 243 243 ASN ASN A . n 
A 1 243 TYR 243 244 244 TYR TYR A . n 
A 1 244 GLN 244 245 245 GLN GLN A . n 
A 1 245 THR 245 246 246 THR THR A . n 
A 1 246 GLU 246 247 247 GLU GLU A . n 
A 1 247 LEU 247 248 248 LEU LEU A . n 
A 1 248 LYS 248 249 249 LYS LYS A . n 
A 1 249 THR 249 250 250 THR THR A . n 
A 1 250 LEU 250 251 251 LEU LEU A . n 
A 1 251 GLU 251 252 252 GLU GLU A . n 
A 1 252 GLU 252 253 253 GLU GLU A . n 
A 1 253 ALA 253 254 254 ALA ALA A . n 
A 1 254 LEU 254 255 255 LEU LEU A . n 
A 1 255 SER 255 256 256 SER SER A . n 
A 1 256 VAL 256 257 257 VAL VAL A . n 
A 1 257 ARG 257 258 258 ARG ARG A . n 
A 1 258 SER 258 259 259 SER SER A . n 
A 1 259 LYS 259 260 260 LYS LYS A . n 
A 1 260 LEU 260 261 261 LEU LEU A . n 
A 1 261 SER 261 262 262 SER SER A . n 
A 1 262 THR 262 263 263 THR THR A . n 
A 1 263 TYR 263 264 264 TYR TYR A . n 
A 1 264 THR 264 265 265 THR THR A . n 
A 1 265 PHE 265 266 266 PHE PHE A . n 
A 1 266 ALA 266 267 267 ALA ALA A . n 
A 1 267 MET 267 268 268 MET MET A . n 
A 1 268 LYS 268 269 269 LYS LYS A . n 
A 1 269 LEU 269 270 270 LEU LEU A . n 
A 1 270 THR 270 271 271 THR THR A . n 
A 1 271 SER 271 272 272 SER SER A . n 
A 1 272 ASP 272 273 273 ASP ASP A . n 
A 1 273 ALA 273 274 274 ALA ALA A . n 
A 1 274 ASN 274 275 275 ASN ASN A . n 
A 1 275 LEU 275 276 276 LEU LEU A . n 
A 1 276 LYS 276 277 277 LYS LYS A . n 
A 1 277 LYS 277 278 278 LYS LYS A . n 
A 1 278 SER 278 279 279 SER SER A . n 
A 1 279 LEU 279 280 280 LEU LEU A . n 
A 1 280 PRO 280 281 281 PRO PRO A . n 
A 1 281 LYS 281 282 282 LYS LYS A . n 
A 1 282 ASN 282 283 283 ASN ASN A . n 
A 1 283 HIS 283 284 284 HIS HIS A . n 
A 1 284 ASN 284 285 285 ASN ASN A . n 
A 1 285 GLY 285 286 286 GLY GLY A . n 
A 1 286 PHE 286 287 287 PHE PHE A . n 
A 1 287 PHE 287 288 288 PHE PHE A . n 
A 1 288 LEU 288 289 289 LEU LEU A . n 
A 1 289 VAL 289 290 290 VAL VAL A . n 
A 1 290 ARG 290 291 291 ARG ARG A . n 
A 1 291 MET 291 292 292 MET MET A . n 
A 1 292 ARG 292 293 293 ARG ARG A . n 
A 1 293 ASN 293 294 294 ASN ASN A . n 
A 1 294 ALA 294 295 295 ALA ALA A . n 
A 1 295 ILE 295 296 296 ILE ILE A . n 
A 1 296 THR 296 297 ?   ?   ?   A . n 
A 1 297 LYS 297 298 ?   ?   ?   A . n 
A 1 298 ASN 298 299 ?   ?   ?   A . n 
A 1 299 GLY 299 300 ?   ?   ?   A . n 
A 1 300 LYS 300 301 ?   ?   ?   A . n 
A 1 301 ASP 301 302 ?   ?   ?   A . n 
A 1 302 THR 302 303 ?   ?   ?   A . n 
A 1 303 GLY 303 304 304 GLY GLY A . n 
A 1 304 LYS 304 305 305 LYS LYS A . n 
A 1 305 PHE 305 306 306 PHE PHE A . n 
A 1 306 LEU 306 307 307 LEU LEU A . n 
A 1 307 VAL 307 308 308 VAL VAL A . n 
A 1 308 SER 308 309 309 SER SER A . n 
A 1 309 VAL 309 310 310 VAL VAL A . n 
A 1 310 LYS 310 311 311 LYS LYS A . n 
A 1 311 PRO 311 312 312 PRO PRO A . n 
A 1 312 PHE 312 313 313 PHE PHE A . n 
A 1 313 ARG 313 314 314 ARG ARG A . n 
A 1 314 LYS 314 315 315 LYS LYS A . n 
A 1 315 LYS 315 316 316 LYS LYS A . n 
A 1 316 GLU 316 317 317 GLU GLU A . n 
A 1 317 SER 317 318 318 SER SER A . n 
A 1 318 GLU 318 319 319 GLU GLU A . n 
A 1 319 GLN 319 320 320 GLN GLN A . n 
A 1 320 ALA 320 321 321 ALA ALA A . n 
A 1 321 LEU 321 322 322 LEU LEU A . n 
A 1 322 GLN 322 323 323 GLN GLN A . n 
A 1 323 GLU 323 324 324 GLU GLU A . n 
A 1 324 LEU 324 325 325 LEU LEU A . n 
A 1 325 ASN 325 326 326 ASN ASN A . n 
A 1 326 LYS 326 327 327 LYS LYS A . n 
A 1 327 ASP 327 328 328 ASP ASP A . n 
A 1 328 ASP 328 329 329 ASP ASP A . n 
A 1 329 ALA 329 330 330 ALA ALA A . n 
A 1 330 ASP 330 331 331 ASP ASP A . n 
A 1 331 PRO 331 332 332 PRO PRO A . n 
A 1 332 GLU 332 333 333 GLU GLU A . n 
A 1 333 VAL 333 334 334 VAL VAL A . n 
A 1 334 LEU 334 335 335 LEU LEU A . n 
A 1 335 ILE 335 336 336 ILE ILE A . n 
A 1 336 ALA 336 337 337 ALA ALA A . n 
A 1 337 VAL 337 338 338 VAL VAL A . n 
A 1 338 LEU 338 339 339 LEU LEU A . n 
A 1 339 LEU 339 340 340 LEU LEU A . n 
A 1 340 ALA 340 341 341 ALA ALA A . n 
A 1 341 THR 341 342 342 THR THR A . n 
A 1 342 ASN 342 343 343 ASN ASN A . n 
A 1 343 ASN 343 344 344 ASN ASN A . n 
A 1 344 ILE 344 345 345 ILE ILE A . n 
A 1 345 LYS 345 346 346 LYS LYS A . n 
A 1 346 SER 346 347 347 SER SER A . n 
A 1 347 LEU 347 348 348 LEU LEU A . n 
A 1 348 LYS 348 349 349 LYS LYS A . n 
A 1 349 LYS 349 350 350 LYS LYS A . n 
A 1 350 ALA 350 351 351 ALA ALA A . n 
A 1 351 TYR 351 352 352 TYR TYR A . n 
A 1 352 PRO 352 353 353 PRO PRO A . n 
A 1 353 ASN 353 354 354 ASN ASN A . n 
A 1 354 TYR 354 355 355 TYR TYR A . n 
A 1 355 PHE 355 356 356 PHE PHE A . n 
A 1 356 GLY 356 357 357 GLY GLY A . n 
A 1 357 SER 357 358 358 SER SER A . n 
A 1 358 THR 358 359 359 THR THR A . n 
A 1 359 ASN 359 360 360 ASN ASN A . n 
A 1 360 GLN 360 361 361 GLN GLN A . n 
A 1 361 PHE 361 362 362 PHE PHE A . n 
A 1 362 GLY 362 363 363 GLY GLY A . n 
A 1 363 ARG 363 364 364 ARG ARG A . n 
A 1 364 PHE 364 365 365 PHE PHE A . n 
A 1 365 LEU 365 366 366 LEU LEU A . n 
A 1 366 SER 366 367 367 SER SER A . n 
A 1 367 ARG 367 368 368 ARG ARG A . n 
A 1 368 HIS 368 369 369 HIS HIS A . n 
A 1 369 ILE 369 370 370 ILE ILE A . n 
A 1 370 ASP 370 371 371 ASP ASP A . n 
A 1 371 THR 371 372 372 THR THR A . n 
A 1 372 VAL 372 373 ?   ?   ?   A . n 
B 2 1   MET 1   -11 ?   ?   ?   B . n 
B 2 2   LYS 2   -10 ?   ?   ?   B . n 
B 2 3   HIS 3   -9  ?   ?   ?   B . n 
B 2 4   HIS 4   -8  ?   ?   ?   B . n 
B 2 5   HIS 5   -7  ?   ?   ?   B . n 
B 2 6   HIS 6   -6  ?   ?   ?   B . n 
B 2 7   HIS 7   -5  ?   ?   ?   B . n 
B 2 8   HIS 8   -4  ?   ?   ?   B . n 
B 2 9   GLY 9   -3  ?   ?   ?   B . n 
B 2 10  SER 10  -2  ?   ?   ?   B . n 
B 2 11  SER 11  -1  ?   ?   ?   B . n 
B 2 12  GLY 12  0   ?   ?   ?   B . n 
B 2 13  MET 13  1   ?   ?   ?   B . n 
B 2 14  GLN 14  2   ?   ?   ?   B . n 
B 2 15  ASP 15  3   ?   ?   ?   B . n 
B 2 16  GLN 16  4   ?   ?   ?   B . n 
B 2 17  ILE 17  5   ?   ?   ?   B . n 
B 2 18  ASP 18  6   ?   ?   ?   B . n 
B 2 19  ALA 19  7   ?   ?   ?   B . n 
B 2 20  LYS 20  8   ?   ?   ?   B . n 
B 2 21  VAL 21  9   ?   ?   ?   B . n 
B 2 22  ILE 22  10  ?   ?   ?   B . n 
B 2 23  ARG 23  11  ?   ?   ?   B . n 
B 2 24  ARG 24  12  ?   ?   ?   B . n 
B 2 25  ASN 25  13  ?   ?   ?   B . n 
B 2 26  PRO 26  14  ?   ?   ?   B . n 
B 2 27  GLU 27  15  15  GLU GLU B . n 
B 2 28  LEU 28  16  16  LEU LEU B . n 
B 2 29  THR 29  17  17  THR THR B . n 
B 2 30  PRO 30  18  18  PRO PRO B . n 
B 2 31  GLY 31  19  19  GLY GLY B . n 
B 2 32  ILE 32  20  20  ILE ILE B . n 
B 2 33  PHE 33  21  21  PHE PHE B . n 
B 2 34  LYS 34  22  22  LYS LYS B . n 
B 2 35  LYS 35  23  23  LYS LYS B . n 
B 2 36  GLY 36  24  24  GLY GLY B . n 
B 2 37  ILE 37  25  25  ILE ILE B . n 
B 2 38  GLU 38  26  26  GLU GLU B . n 
B 2 39  ILE 39  27  27  ILE ILE B . n 
B 2 40  THR 40  28  28  THR THR B . n 
B 2 41  ILE 41  29  29  ILE ILE B . n 
B 2 42  ASP 42  30  30  ASP ASP B . n 
B 2 43  LEU 43  31  31  LEU LEU B . n 
B 2 44  GLU 44  32  32  GLU GLU B . n 
B 2 45  GLU 45  33  33  GLU GLU B . n 
B 2 46  MET 46  34  34  MET MET B . n 
B 2 47  VAL 47  35  35  VAL VAL B . n 
B 2 48  CYS 48  36  36  CYS CYS B . n 
B 2 49  TYR 49  37  37  TYR TYR B . n 
B 2 50  HIS 50  38  38  HIS HIS B . n 
B 2 51  SER 51  39  39  SER SER B . n 
B 2 52  GLY 52  40  40  GLY GLY B . n 
B 2 53  LEU 53  41  41  LEU LEU B . n 
B 2 54  THR 54  42  42  THR THR B . n 
B 2 55  TRP 55  43  43  TRP TRP B . n 
B 2 56  LYS 56  44  44  LYS LYS B . n 
B 2 57  VAL 57  45  45  VAL VAL B . n 
B 2 58  LYS 58  46  46  LYS LYS B . n 
B 2 59  GLN 59  47  47  GLN GLN B . n 
B 2 60  LEU 60  48  48  LEU LEU B . n 
B 2 61  THR 61  49  49  THR THR B . n 
B 2 62  ASN 62  50  50  ASN ASN B . n 
B 2 63  THR 63  51  51  THR THR B . n 
B 2 64  LEU 64  52  52  LEU LEU B . n 
B 2 65  TRP 65  53  53  TRP TRP B . n 
B 2 66  SER 66  54  54  SER SER B . n 
B 2 67  LEU 67  55  55  LEU LEU B . n 
B 2 68  ALA 68  56  56  ALA ALA B . n 
B 2 69  GLY 69  57  57  GLY GLY B . n 
B 2 70  ASP 70  58  ?   ?   ?   B . n 
B 2 71  GLU 71  59  ?   ?   ?   B . n 
B 2 72  HIS 72  60  ?   ?   ?   B . n 
B 2 73  THR 73  61  ?   ?   ?   B . n 
B 2 74  VAL 74  62  ?   ?   ?   B . n 
B 2 75  MET 75  63  ?   ?   ?   B . n 
B 2 76  GLU 76  64  ?   ?   ?   B . n 
B 2 77  VAL 77  65  ?   ?   ?   B . n 
B 2 78  ILE 78  66  ?   ?   ?   B . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        ATP 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   ATP 
_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 GOL 1   401 402 GOL GOL A . 
D 4 ATP 1   402 1   ATP ATP A . 
E 5 MG  1   403 1   MG  MG  A . 
F 6 NA  1   404 1   NA  NA  A . 
G 7 HOH 1   501 333 HOH HOH A . 
G 7 HOH 2   502 152 HOH HOH A . 
G 7 HOH 3   503 200 HOH HOH A . 
G 7 HOH 4   504 320 HOH HOH A . 
G 7 HOH 5   505 89  HOH HOH A . 
G 7 HOH 6   506 29  HOH HOH A . 
G 7 HOH 7   507 174 HOH HOH A . 
G 7 HOH 8   508 213 HOH HOH A . 
G 7 HOH 9   509 110 HOH HOH A . 
G 7 HOH 10  510 37  HOH HOH A . 
G 7 HOH 11  511 190 HOH HOH A . 
G 7 HOH 12  512 147 HOH HOH A . 
G 7 HOH 13  513 182 HOH HOH A . 
G 7 HOH 14  514 9   HOH HOH A . 
G 7 HOH 15  515 235 HOH HOH A . 
G 7 HOH 16  516 179 HOH HOH A . 
G 7 HOH 17  517 158 HOH HOH A . 
G 7 HOH 18  518 248 HOH HOH A . 
G 7 HOH 19  519 321 HOH HOH A . 
G 7 HOH 20  520 335 HOH HOH A . 
G 7 HOH 21  521 196 HOH HOH A . 
G 7 HOH 22  522 188 HOH HOH A . 
G 7 HOH 23  523 193 HOH HOH A . 
G 7 HOH 24  524 73  HOH HOH A . 
G 7 HOH 25  525 50  HOH HOH A . 
G 7 HOH 26  526 153 HOH HOH A . 
G 7 HOH 27  527 341 HOH HOH A . 
G 7 HOH 28  528 86  HOH HOH A . 
G 7 HOH 29  529 254 HOH HOH A . 
G 7 HOH 30  530 185 HOH HOH A . 
G 7 HOH 31  531 339 HOH HOH A . 
G 7 HOH 32  532 35  HOH HOH A . 
G 7 HOH 33  533 165 HOH HOH A . 
G 7 HOH 34  534 145 HOH HOH A . 
G 7 HOH 35  535 123 HOH HOH A . 
G 7 HOH 36  536 172 HOH HOH A . 
G 7 HOH 37  537 354 HOH HOH A . 
G 7 HOH 38  538 178 HOH HOH A . 
G 7 HOH 39  539 130 HOH HOH A . 
G 7 HOH 40  540 59  HOH HOH A . 
G 7 HOH 41  541 227 HOH HOH A . 
G 7 HOH 42  542 148 HOH HOH A . 
G 7 HOH 43  543 160 HOH HOH A . 
G 7 HOH 44  544 113 HOH HOH A . 
G 7 HOH 45  545 181 HOH HOH A . 
G 7 HOH 46  546 255 HOH HOH A . 
G 7 HOH 47  547 163 HOH HOH A . 
G 7 HOH 48  548 180 HOH HOH A . 
G 7 HOH 49  549 77  HOH HOH A . 
G 7 HOH 50  550 65  HOH HOH A . 
G 7 HOH 51  551 252 HOH HOH A . 
G 7 HOH 52  552 46  HOH HOH A . 
G 7 HOH 53  553 217 HOH HOH A . 
G 7 HOH 54  554 208 HOH HOH A . 
G 7 HOH 55  555 121 HOH HOH A . 
G 7 HOH 56  556 78  HOH HOH A . 
G 7 HOH 57  557 5   HOH HOH A . 
G 7 HOH 58  558 10  HOH HOH A . 
G 7 HOH 59  559 237 HOH HOH A . 
G 7 HOH 60  560 269 HOH HOH A . 
G 7 HOH 61  561 155 HOH HOH A . 
G 7 HOH 62  562 150 HOH HOH A . 
G 7 HOH 63  563 101 HOH HOH A . 
G 7 HOH 64  564 4   HOH HOH A . 
G 7 HOH 65  565 15  HOH HOH A . 
G 7 HOH 66  566 12  HOH HOH A . 
G 7 HOH 67  567 88  HOH HOH A . 
G 7 HOH 68  568 57  HOH HOH A . 
G 7 HOH 69  569 28  HOH HOH A . 
G 7 HOH 70  570 17  HOH HOH A . 
G 7 HOH 71  571 13  HOH HOH A . 
G 7 HOH 72  572 149 HOH HOH A . 
G 7 HOH 73  573 221 HOH HOH A . 
G 7 HOH 74  574 168 HOH HOH A . 
G 7 HOH 75  575 215 HOH HOH A . 
G 7 HOH 76  576 116 HOH HOH A . 
G 7 HOH 77  577 256 HOH HOH A . 
G 7 HOH 78  578 95  HOH HOH A . 
G 7 HOH 79  579 45  HOH HOH A . 
G 7 HOH 80  580 42  HOH HOH A . 
G 7 HOH 81  581 187 HOH HOH A . 
G 7 HOH 82  582 54  HOH HOH A . 
G 7 HOH 83  583 210 HOH HOH A . 
G 7 HOH 84  584 224 HOH HOH A . 
G 7 HOH 85  585 23  HOH HOH A . 
G 7 HOH 86  586 2   HOH HOH A . 
G 7 HOH 87  587 236 HOH HOH A . 
G 7 HOH 88  588 216 HOH HOH A . 
G 7 HOH 89  589 47  HOH HOH A . 
G 7 HOH 90  590 328 HOH HOH A . 
G 7 HOH 91  591 157 HOH HOH A . 
G 7 HOH 92  592 25  HOH HOH A . 
G 7 HOH 93  593 189 HOH HOH A . 
G 7 HOH 94  594 11  HOH HOH A . 
G 7 HOH 95  595 308 HOH HOH A . 
G 7 HOH 96  596 300 HOH HOH A . 
G 7 HOH 97  597 104 HOH HOH A . 
G 7 HOH 98  598 166 HOH HOH A . 
G 7 HOH 99  599 344 HOH HOH A . 
G 7 HOH 100 600 93  HOH HOH A . 
G 7 HOH 101 601 184 HOH HOH A . 
G 7 HOH 102 602 239 HOH HOH A . 
G 7 HOH 103 603 154 HOH HOH A . 
G 7 HOH 104 604 295 HOH HOH A . 
G 7 HOH 105 605 38  HOH HOH A . 
G 7 HOH 106 606 60  HOH HOH A . 
G 7 HOH 107 607 43  HOH HOH A . 
G 7 HOH 108 608 74  HOH HOH A . 
G 7 HOH 109 609 84  HOH HOH A . 
G 7 HOH 110 610 353 HOH HOH A . 
G 7 HOH 111 611 20  HOH HOH A . 
G 7 HOH 112 612 197 HOH HOH A . 
G 7 HOH 113 613 171 HOH HOH A . 
G 7 HOH 114 614 164 HOH HOH A . 
G 7 HOH 115 615 146 HOH HOH A . 
G 7 HOH 116 616 343 HOH HOH A . 
G 7 HOH 117 617 117 HOH HOH A . 
G 7 HOH 118 618 53  HOH HOH A . 
G 7 HOH 119 619 75  HOH HOH A . 
G 7 HOH 120 620 76  HOH HOH A . 
G 7 HOH 121 621 265 HOH HOH A . 
G 7 HOH 122 622 105 HOH HOH A . 
G 7 HOH 123 623 233 HOH HOH A . 
G 7 HOH 124 624 334 HOH HOH A . 
G 7 HOH 125 625 202 HOH HOH A . 
G 7 HOH 126 626 345 HOH HOH A . 
G 7 HOH 127 627 303 HOH HOH A . 
G 7 HOH 128 628 22  HOH HOH A . 
G 7 HOH 129 629 111 HOH HOH A . 
G 7 HOH 130 630 129 HOH HOH A . 
G 7 HOH 131 631 167 HOH HOH A . 
G 7 HOH 132 632 135 HOH HOH A . 
G 7 HOH 133 633 122 HOH HOH A . 
G 7 HOH 134 634 128 HOH HOH A . 
G 7 HOH 135 635 186 HOH HOH A . 
G 7 HOH 136 636 133 HOH HOH A . 
G 7 HOH 137 637 191 HOH HOH A . 
G 7 HOH 138 638 176 HOH HOH A . 
G 7 HOH 139 639 234 HOH HOH A . 
G 7 HOH 140 640 161 HOH HOH A . 
G 7 HOH 141 641 271 HOH HOH A . 
G 7 HOH 142 642 16  HOH HOH A . 
G 7 HOH 143 643 136 HOH HOH A . 
G 7 HOH 144 644 170 HOH HOH A . 
G 7 HOH 145 645 140 HOH HOH A . 
G 7 HOH 146 646 159 HOH HOH A . 
G 7 HOH 147 647 100 HOH HOH A . 
G 7 HOH 148 648 141 HOH HOH A . 
G 7 HOH 149 649 107 HOH HOH A . 
G 7 HOH 150 650 61  HOH HOH A . 
G 7 HOH 151 651 68  HOH HOH A . 
G 7 HOH 152 652 304 HOH HOH A . 
G 7 HOH 153 653 277 HOH HOH A . 
G 7 HOH 154 654 21  HOH HOH A . 
G 7 HOH 155 655 151 HOH HOH A . 
G 7 HOH 156 656 36  HOH HOH A . 
G 7 HOH 157 657 91  HOH HOH A . 
G 7 HOH 158 658 206 HOH HOH A . 
G 7 HOH 159 659 276 HOH HOH A . 
G 7 HOH 160 660 31  HOH HOH A . 
G 7 HOH 161 661 6   HOH HOH A . 
G 7 HOH 162 662 96  HOH HOH A . 
G 7 HOH 163 663 212 HOH HOH A . 
G 7 HOH 164 664 52  HOH HOH A . 
G 7 HOH 165 665 327 HOH HOH A . 
G 7 HOH 166 666 201 HOH HOH A . 
G 7 HOH 167 667 67  HOH HOH A . 
G 7 HOH 168 668 338 HOH HOH A . 
G 7 HOH 169 669 82  HOH HOH A . 
G 7 HOH 170 670 232 HOH HOH A . 
G 7 HOH 171 671 85  HOH HOH A . 
G 7 HOH 172 672 156 HOH HOH A . 
G 7 HOH 173 673 278 HOH HOH A . 
G 7 HOH 174 674 112 HOH HOH A . 
G 7 HOH 175 675 44  HOH HOH A . 
G 7 HOH 176 676 319 HOH HOH A . 
G 7 HOH 177 677 348 HOH HOH A . 
G 7 HOH 178 678 106 HOH HOH A . 
G 7 HOH 179 679 226 HOH HOH A . 
G 7 HOH 180 680 199 HOH HOH A . 
G 7 HOH 181 681 220 HOH HOH A . 
G 7 HOH 182 682 56  HOH HOH A . 
G 7 HOH 183 683 134 HOH HOH A . 
G 7 HOH 184 684 132 HOH HOH A . 
G 7 HOH 185 685 305 HOH HOH A . 
G 7 HOH 186 686 205 HOH HOH A . 
G 7 HOH 187 687 71  HOH HOH A . 
G 7 HOH 188 688 119 HOH HOH A . 
G 7 HOH 189 689 115 HOH HOH A . 
G 7 HOH 190 690 125 HOH HOH A . 
G 7 HOH 191 691 209 HOH HOH A . 
G 7 HOH 192 692 204 HOH HOH A . 
G 7 HOH 193 693 120 HOH HOH A . 
G 7 HOH 194 694 336 HOH HOH A . 
G 7 HOH 195 695 314 HOH HOH A . 
G 7 HOH 196 696 264 HOH HOH A . 
G 7 HOH 197 697 62  HOH HOH A . 
G 7 HOH 198 698 298 HOH HOH A . 
G 7 HOH 199 699 7   HOH HOH A . 
G 7 HOH 200 700 231 HOH HOH A . 
G 7 HOH 201 701 243 HOH HOH A . 
G 7 HOH 202 702 87  HOH HOH A . 
G 7 HOH 203 703 192 HOH HOH A . 
G 7 HOH 204 704 24  HOH HOH A . 
G 7 HOH 205 705 127 HOH HOH A . 
G 7 HOH 206 706 126 HOH HOH A . 
G 7 HOH 207 707 48  HOH HOH A . 
G 7 HOH 208 708 238 HOH HOH A . 
G 7 HOH 209 709 350 HOH HOH A . 
G 7 HOH 210 710 49  HOH HOH A . 
G 7 HOH 211 711 19  HOH HOH A . 
G 7 HOH 212 712 285 HOH HOH A . 
G 7 HOH 213 713 274 HOH HOH A . 
G 7 HOH 214 714 131 HOH HOH A . 
G 7 HOH 215 715 69  HOH HOH A . 
G 7 HOH 216 716 223 HOH HOH A . 
G 7 HOH 217 717 337 HOH HOH A . 
G 7 HOH 218 718 349 HOH HOH A . 
G 7 HOH 219 719 249 HOH HOH A . 
G 7 HOH 220 720 124 HOH HOH A . 
G 7 HOH 221 721 250 HOH HOH A . 
G 7 HOH 222 722 144 HOH HOH A . 
G 7 HOH 223 723 230 HOH HOH A . 
G 7 HOH 224 724 246 HOH HOH A . 
G 7 HOH 225 725 169 HOH HOH A . 
G 7 HOH 226 726 118 HOH HOH A . 
G 7 HOH 227 727 251 HOH HOH A . 
G 7 HOH 228 728 1   HOH HOH A . 
G 7 HOH 229 729 310 HOH HOH A . 
G 7 HOH 230 730 175 HOH HOH A . 
G 7 HOH 231 731 142 HOH HOH A . 
G 7 HOH 232 732 8   HOH HOH A . 
G 7 HOH 233 733 40  HOH HOH A . 
G 7 HOH 234 734 108 HOH HOH A . 
G 7 HOH 235 735 30  HOH HOH A . 
G 7 HOH 236 736 177 HOH HOH A . 
G 7 HOH 237 737 286 HOH HOH A . 
G 7 HOH 238 738 194 HOH HOH A . 
G 7 HOH 239 739 51  HOH HOH A . 
G 7 HOH 240 740 301 HOH HOH A . 
G 7 HOH 241 741 317 HOH HOH A . 
G 7 HOH 242 742 109 HOH HOH A . 
G 7 HOH 243 743 18  HOH HOH A . 
G 7 HOH 244 744 261 HOH HOH A . 
G 7 HOH 245 745 260 HOH HOH A . 
G 7 HOH 246 746 79  HOH HOH A . 
G 7 HOH 247 747 80  HOH HOH A . 
G 7 HOH 248 748 299 HOH HOH A . 
G 7 HOH 249 749 280 HOH HOH A . 
G 7 HOH 250 750 272 HOH HOH A . 
G 7 HOH 251 751 64  HOH HOH A . 
G 7 HOH 252 752 222 HOH HOH A . 
G 7 HOH 253 753 325 HOH HOH A . 
G 7 HOH 254 754 203 HOH HOH A . 
G 7 HOH 255 755 240 HOH HOH A . 
G 7 HOH 256 756 33  HOH HOH A . 
G 7 HOH 257 757 94  HOH HOH A . 
G 7 HOH 258 758 58  HOH HOH A . 
G 7 HOH 259 759 281 HOH HOH A . 
G 7 HOH 260 760 291 HOH HOH A . 
G 7 HOH 261 761 228 HOH HOH A . 
G 7 HOH 262 762 183 HOH HOH A . 
G 7 HOH 263 763 225 HOH HOH A . 
G 7 HOH 264 764 27  HOH HOH A . 
G 7 HOH 265 765 307 HOH HOH A . 
G 7 HOH 266 766 342 HOH HOH A . 
G 7 HOH 267 767 311 HOH HOH A . 
G 7 HOH 268 768 114 HOH HOH A . 
G 7 HOH 269 769 207 HOH HOH A . 
G 7 HOH 270 770 302 HOH HOH A . 
G 7 HOH 271 771 70  HOH HOH A . 
G 7 HOH 272 772 323 HOH HOH A . 
G 7 HOH 273 773 346 HOH HOH A . 
G 7 HOH 274 774 137 HOH HOH A . 
G 7 HOH 275 775 138 HOH HOH A . 
G 7 HOH 276 776 218 HOH HOH A . 
G 7 HOH 277 777 83  HOH HOH A . 
G 7 HOH 278 778 283 HOH HOH A . 
G 7 HOH 279 779 90  HOH HOH A . 
G 7 HOH 280 780 259 HOH HOH A . 
G 7 HOH 281 781 72  HOH HOH A . 
G 7 HOH 282 782 245 HOH HOH A . 
G 7 HOH 283 783 316 HOH HOH A . 
G 7 HOH 284 784 34  HOH HOH A . 
G 7 HOH 285 785 347 HOH HOH A . 
G 7 HOH 286 786 351 HOH HOH A . 
G 7 HOH 287 787 143 HOH HOH A . 
G 7 HOH 288 788 211 HOH HOH A . 
G 7 HOH 289 789 81  HOH HOH A . 
G 7 HOH 290 790 352 HOH HOH A . 
G 7 HOH 291 791 214 HOH HOH A . 
G 7 HOH 292 792 294 HOH HOH A . 
G 7 HOH 293 793 340 HOH HOH A . 
G 7 HOH 294 794 198 HOH HOH A . 
G 7 HOH 295 795 268 HOH HOH A . 
G 7 HOH 296 796 292 HOH HOH A . 
G 7 HOH 297 797 326 HOH HOH A . 
G 7 HOH 298 798 258 HOH HOH A . 
G 7 HOH 299 799 262 HOH HOH A . 
G 7 HOH 300 800 97  HOH HOH A . 
G 7 HOH 301 801 253 HOH HOH A . 
G 7 HOH 302 802 318 HOH HOH A . 
G 7 HOH 303 803 266 HOH HOH A . 
G 7 HOH 304 804 257 HOH HOH A . 
G 7 HOH 305 805 263 HOH HOH A . 
G 7 HOH 306 806 247 HOH HOH A . 
G 7 HOH 307 807 66  HOH HOH A . 
G 7 HOH 308 808 329 HOH HOH A . 
G 7 HOH 309 809 296 HOH HOH A . 
G 7 HOH 310 810 173 HOH HOH A . 
G 7 HOH 311 811 284 HOH HOH A . 
G 7 HOH 312 812 312 HOH HOH A . 
G 7 HOH 313 813 273 HOH HOH A . 
G 7 HOH 314 814 309 HOH HOH A . 
G 7 HOH 315 815 315 HOH HOH A . 
G 7 HOH 316 816 270 HOH HOH A . 
G 7 HOH 317 817 297 HOH HOH A . 
G 7 HOH 318 818 279 HOH HOH A . 
G 7 HOH 319 819 275 HOH HOH A . 
G 7 HOH 320 820 267 HOH HOH A . 
G 7 HOH 321 821 324 HOH HOH A . 
G 7 HOH 322 822 306 HOH HOH A . 
G 7 HOH 323 823 322 HOH HOH A . 
G 7 HOH 324 824 282 HOH HOH A . 
G 7 HOH 325 825 331 HOH HOH A . 
H 7 HOH 1   101 162 HOH HOH B . 
H 7 HOH 2   102 32  HOH HOH B . 
H 7 HOH 3   103 26  HOH HOH B . 
H 7 HOH 4   104 288 HOH HOH B . 
H 7 HOH 5   105 41  HOH HOH B . 
H 7 HOH 6   106 219 HOH HOH B . 
H 7 HOH 7   107 55  HOH HOH B . 
H 7 HOH 8   108 92  HOH HOH B . 
H 7 HOH 9   109 102 HOH HOH B . 
H 7 HOH 10  110 139 HOH HOH B . 
H 7 HOH 11  111 99  HOH HOH B . 
H 7 HOH 12  112 3   HOH HOH B . 
H 7 HOH 13  113 330 HOH HOH B . 
H 7 HOH 14  114 195 HOH HOH B . 
H 7 HOH 15  115 229 HOH HOH B . 
H 7 HOH 16  116 293 HOH HOH B . 
H 7 HOH 17  117 103 HOH HOH B . 
H 7 HOH 18  118 290 HOH HOH B . 
H 7 HOH 19  119 39  HOH HOH B . 
H 7 HOH 20  120 63  HOH HOH B . 
H 7 HOH 21  121 14  HOH HOH B . 
H 7 HOH 22  122 98  HOH HOH B . 
H 7 HOH 23  123 241 HOH HOH B . 
H 7 HOH 24  124 242 HOH HOH B . 
H 7 HOH 25  125 313 HOH HOH B . 
H 7 HOH 26  126 332 HOH HOH B . 
H 7 HOH 27  127 244 HOH HOH B . 
H 7 HOH 28  128 289 HOH HOH B . 
H 7 HOH 29  129 287 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 LEU 13  ? CG  ? A LEU 12  CG  
2  1 Y 1 A LEU 13  ? CD1 ? A LEU 12  CD1 
3  1 Y 1 A LEU 13  ? CD2 ? A LEU 12  CD2 
4  1 Y 1 A LYS 14  ? CG  ? A LYS 13  CG  
5  1 Y 1 A LYS 14  ? CD  ? A LYS 13  CD  
6  1 Y 1 A LYS 14  ? CE  ? A LYS 13  CE  
7  1 Y 1 A LYS 14  ? NZ  ? A LYS 13  NZ  
8  1 Y 1 A GLU 21  ? CG  ? A GLU 20  CG  
9  1 Y 1 A GLU 21  ? CD  ? A GLU 20  CD  
10 1 Y 1 A GLU 21  ? OE1 ? A GLU 20  OE1 
11 1 Y 1 A GLU 21  ? OE2 ? A GLU 20  OE2 
12 1 Y 1 A LYS 70  ? CD  ? A LYS 69  CD  
13 1 Y 1 A LYS 70  ? CE  ? A LYS 69  CE  
14 1 Y 1 A LYS 70  ? NZ  ? A LYS 69  NZ  
15 1 Y 1 A ARG 92  ? CD  ? A ARG 91  CD  
16 1 Y 1 A ARG 92  ? NE  ? A ARG 91  NE  
17 1 Y 1 A ARG 92  ? CZ  ? A ARG 91  CZ  
18 1 Y 1 A ARG 92  ? NH1 ? A ARG 91  NH1 
19 1 Y 1 A ARG 92  ? NH2 ? A ARG 91  NH2 
20 1 Y 1 A ILE 104 ? CG1 ? A ILE 103 CG1 
21 1 Y 1 A ILE 104 ? CG2 ? A ILE 103 CG2 
22 1 Y 1 A ILE 104 ? CD1 ? A ILE 103 CD1 
23 1 Y 1 A GLU 239 ? CD  ? A GLU 238 CD  
24 1 Y 1 A GLU 239 ? OE1 ? A GLU 238 OE1 
25 1 Y 1 A GLU 239 ? OE2 ? A GLU 238 OE2 
26 1 Y 1 A LYS 282 ? CG  ? A LYS 281 CG  
27 1 Y 1 A LYS 282 ? CD  ? A LYS 281 CD  
28 1 Y 1 A LYS 282 ? CE  ? A LYS 281 CE  
29 1 Y 1 A LYS 282 ? NZ  ? A LYS 281 NZ  
30 1 Y 1 B LEU 16  ? CG  ? B LEU 28  CG  
31 1 Y 1 B LEU 16  ? CD1 ? B LEU 28  CD1 
32 1 Y 1 B LEU 16  ? CD2 ? B LEU 28  CD2 
33 1 Y 1 B LYS 46  ? CE  ? B LYS 58  CE  
34 1 Y 1 B LYS 46  ? NZ  ? B LYS 58  NZ  
# 
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       ? ? ? ? ? ? ? ? ? ? ? BUSTER  ? ? ? '2.10.4 (24-FEB-2021)' 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS     ? ? ? .                      2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? .                      3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER  ? ? ? .                      4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9ERV 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     49.695 
_cell.length_a_esd                 ? 
_cell.length_b                     103.264 
_cell.length_b_esd                 ? 
_cell.length_c                     209.235 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        8 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         9ERV 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                20 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'C 2 2 21' 
_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                   9ERV 
_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             3.01 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          59.16 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              8.0 
_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    '25% PEG 1500' 
_exptl_crystal_grow.pdbx_pH_range   7.5-8.0 
_exptl_crystal_grow.temp            293 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER2 S 9M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2024-03-12 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.9999 
_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                        'DIAMOND BEAMLINE I24' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.9999 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   I24 
_diffrn_source.pdbx_synchrotron_site       Diamond 
# 
_reflns.B_iso_Wilson_estimate                          34.69 
_reflns.entry_id                                       9ERV 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.25 
_reflns.d_resolution_low                               50.13 
_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                                     22597 
_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                           90.5 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                9.4 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          9.1 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                0.09 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.987 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.27 
_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                                    2.25 
_reflns_shell.d_res_low                                     2.36 
_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                             1611 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               ? 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.29 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            -1.86250 
_refine.aniso_B[1][2]                            0.00000 
_refine.aniso_B[1][3]                            0.00000 
_refine.aniso_B[2][2]                            2.22460 
_refine.aniso_B[2][3]                            0.00000 
_refine.aniso_B[3][3]                            -0.36210 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               32.03 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.928 
_refine.correlation_coeff_Fo_to_Fc_free          0.891 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9ERV 
_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                            2.253 
_refine.ls_d_res_low                             50.13 
_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                     22597 
_refine.ls_number_reflns_R_free                  1127 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    86.9 
_refine.ls_percent_reflns_R_free                 4.990 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2011 
_refine.ls_R_factor_R_free                       0.2440 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1988 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    ? 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          0.000 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ? 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             ? 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             ? 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   0.226 
_refine.pdbx_overall_SU_R_free_Blow_DPI          0.235 
_refine.pdbx_overall_SU_R_Blow_DPI               0.345 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            ? 
_refine.overall_SU_R_Cruickshank_DPI             0.297 
_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_analyze.entry_id                        9ERV 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
_refine_analyze.Luzzati_coordinate_error_free   ? 
_refine_analyze.Luzzati_coordinate_error_obs    0.28 
_refine_analyze.Luzzati_d_res_low_free          ? 
_refine_analyze.Luzzati_d_res_low_obs           ? 
_refine_analyze.Luzzati_sigma_a_free            ? 
_refine_analyze.Luzzati_sigma_a_free_details    ? 
_refine_analyze.Luzzati_sigma_a_obs             ? 
_refine_analyze.Luzzati_sigma_a_obs_details     ? 
_refine_analyze.number_disordered_residues      ? 
_refine_analyze.occupancy_sum_hydrogen          ? 
_refine_analyze.occupancy_sum_non_hydrogen      ? 
_refine_analyze.RG_d_res_high                   ? 
_refine_analyze.RG_d_res_low                    ? 
_refine_analyze.RG_free                         ? 
_refine_analyze.RG_work                         ? 
_refine_analyze.RG_free_work_ratio              ? 
_refine_analyze.pdbx_Luzzati_d_res_high_obs     ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       2.253 
_refine_hist.d_res_low                        50.13 
_refine_hist.number_atoms_solvent             353 
_refine_hist.number_atoms_total               3489 
_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        3097 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         39 
_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' ? 0.008 ? 3187 ? t_bond_d                  2.00  HARMONIC     
'X-RAY DIFFRACTION' ? 0.92  ? 4288 ? t_angle_deg               2.00  HARMONIC     
'X-RAY DIFFRACTION' ? ?     ? 1175 ? t_dihedral_angle_d        2.00  SINUSOIDAL   
'X-RAY DIFFRACTION' ? ?     ? ?    ? t_incorr_chiral_ct        ?     ?            
'X-RAY DIFFRACTION' ? ?     ? ?    ? t_pseud_angle             ?     ?            
'X-RAY DIFFRACTION' ? ?     ? ?    ? t_trig_c_planes           ?     ?            
'X-RAY DIFFRACTION' ? ?     ? 537  ? t_gen_planes              5.00  HARMONIC     
'X-RAY DIFFRACTION' ? ?     ? 3182 ? t_it                      10.00 HARMONIC     
'X-RAY DIFFRACTION' ? ?     ? ?    ? t_nbd                     ?     ?            
'X-RAY DIFFRACTION' ? 3.02  ? ?    ? t_omega_torsion           ?     ?            
'X-RAY DIFFRACTION' ? 19.23 ? ?    ? t_other_torsion           ?     ?            
'X-RAY DIFFRACTION' ? ?     ? ?    ? t_improper_torsion        ?     ?            
'X-RAY DIFFRACTION' ? ?     ? 421  ? t_chiral_improper_torsion 5.00  SEMIHARMONIC 
'X-RAY DIFFRACTION' ? ?     ? ?    ? t_sum_occupancies         ?     ?            
'X-RAY DIFFRACTION' ? ?     ? ?    ? t_utility_distance        ?     ?            
'X-RAY DIFFRACTION' ? ?     ? ?    ? t_utility_angle           ?     ?            
'X-RAY DIFFRACTION' ? ?     ? ?    ? t_utility_torsion         ?     ?            
'X-RAY DIFFRACTION' ? ?     ? 2618 ? t_ideal_dist_contact      4.00  SEMIHARMONIC 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       2.253 
_refine_ls_shell.d_res_low                        2.29 
_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             436 
_refine_ls_shell.percent_reflns_obs               40.79 
_refine_ls_shell.percent_reflns_R_free            3.54 
_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                  0.2879 
_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                  0.3598 
# 
_struct.entry_id                     9ERV 
_struct.title                        'Structure of Salmonella CapRel bound to Bas11 Gp54' 
_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        9ERV 
_struct_keywords.text            'tRNA pyrophosphokinase, activated enzyme complex, RNA BINDING PROTEIN' 
_struct_keywords.pdbx_keywords   'RNA BINDING 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 5 ? 
F N N 6 ? 
G N N 7 ? 
H N N 7 ? 
# 
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 PDB 9ERV 9ERV ? 1 ? 1 
2 PDB 9ERV 9ERV ? 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 9ERV A 1 ? 372 ? 9ERV 2   ? 373 ? 2   373 
2 2 9ERV B 1 ? 78  ? 9ERV -11 ? 66  ? -11 66  
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_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)' 4680  ? 
1 MORE         -44   ? 
1 'SSA (A^2)'  19630 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 SER A 15  ? HIS A 28  ? SER A 16  HIS A 29  1 ? 14 
HELX_P HELX_P2  AA2 GLU A 31  ? HIS A 49  ? GLU A 32  HIS A 50  1 ? 19 
HELX_P HELX_P3  AA3 HIS A 49  ? ASP A 68  ? HIS A 50  ASP A 69  1 ? 20 
HELX_P HELX_P4  AA4 ARG A 81  ? GLU A 90  ? ARG A 82  GLU A 91  1 ? 10 
HELX_P HELX_P5  AA5 ALA A 104 ? MET A 108 ? ALA A 105 MET A 109 5 ? 5  
HELX_P HELX_P6  AA6 ASN A 120 ? SER A 134 ? ASN A 121 SER A 135 1 ? 15 
HELX_P HELX_P7  AA7 GLU A 185 ? GLU A 201 ? GLU A 186 GLU A 202 1 ? 17 
HELX_P HELX_P8  AA8 HIS A 212 ? GLU A 230 ? HIS A 213 GLU A 231 1 ? 19 
HELX_P HELX_P9  AA9 ASP A 236 ? SER A 255 ? ASP A 237 SER A 256 1 ? 20 
HELX_P HELX_P10 AB1 SER A 255 ? SER A 271 ? SER A 256 SER A 272 1 ? 17 
HELX_P HELX_P11 AB2 ASP A 272 ? LEU A 279 ? ASP A 273 LEU A 280 1 ? 8  
HELX_P HELX_P12 AB3 ARG A 313 ? LYS A 315 ? ARG A 314 LYS A 316 5 ? 3  
HELX_P HELX_P13 AB4 GLU A 316 ? ASP A 330 ? GLU A 317 ASP A 331 1 ? 15 
HELX_P HELX_P14 AB5 THR A 341 ? TYR A 351 ? THR A 342 TYR A 352 1 ? 11 
HELX_P HELX_P15 AB6 ASN A 353 ? ASP A 370 ? ASN A 354 ASP A 371 1 ? 18 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1 metalc ? ? A ASP 110 OD2 ? ? ? 1_555 E MG  . MG ? ? A ASP 111 A MG  403 1_555 ? ? ? ? ? ? ? 2.194 ? ? 
metalc2 metalc ? ? D ATP .   O1G ? ? ? 1_555 E MG  . MG ? ? A ATP 402 A MG  403 1_555 ? ? ? ? ? ? ? 2.649 ? ? 
metalc3 metalc ? ? D ATP .   O1B ? ? ? 1_555 E MG  . MG ? ? A ATP 402 A MG  403 1_555 ? ? ? ? ? ? ? 2.507 ? ? 
metalc4 metalc ? ? F NA  .   NA  ? ? ? 1_555 G HOH . O  ? ? A NA  404 A HOH 530 1_555 ? ? ? ? ? ? ? 2.813 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1 OD2 ? A ASP 110 ? A ASP 111 ? 1_555 MG ? E MG . ? A MG 403 ? 1_555 O1G ? D ATP . ? A ATP 402 ? 1_555 88.9 ? 
2 OD2 ? A ASP 110 ? A ASP 111 ? 1_555 MG ? E MG . ? A MG 403 ? 1_555 O1B ? D ATP . ? A ATP 402 ? 1_555 92.7 ? 
3 O1G ? D ATP .   ? A ATP 402 ? 1_555 MG ? E MG . ? A MG 403 ? 1_555 O1B ? D ATP . ? A ATP 402 ? 1_555 88.6 ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 5 ? 
AA2 ? 8 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? parallel      
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA2 5 6 ? anti-parallel 
AA2 6 7 ? anti-parallel 
AA2 7 8 ? anti-parallel 
# 
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 ILE A 74  ? LEU A 79  ? ILE A 75  LEU A 80  
AA1 2 GLY A 112 ? VAL A 118 ? GLY A 113 VAL A 119 
AA1 3 THR A 176 ? THR A 184 ? THR A 177 THR A 185 
AA1 4 GLY A 156 ? CYS A 163 ? GLY A 157 CYS A 164 
AA1 5 LYS A 139 ? TYR A 146 ? LYS A 140 TYR A 147 
AA2 1 GLY B 31  ? LYS B 35  ? GLY B 19  LYS B 23  
AA2 2 VAL A 333 ? ALA A 340 ? VAL A 334 ALA A 341 
AA2 3 PHE A 286 ? ASN A 293 ? PHE A 287 ASN A 294 
AA2 4 LYS A 304 ? PHE A 312 ? LYS A 305 PHE A 313 
AA2 5 LEU B 64  ? ALA B 68  ? LEU B 52  ALA B 56  
AA2 6 LEU B 53  ? THR B 61  ? LEU B 41  THR B 49  
AA2 7 VAL B 47  ? HIS B 50  ? VAL B 35  HIS B 38  
AA2 8 ILE B 39  ? ASP B 42  ? ILE B 27  ASP B 30  
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N ILE A 74  ? N ILE A 75  O ILE A 117 ? O ILE A 118 
AA1 2 3 N CYS A 114 ? N CYS A 115 O GLN A 181 ? O GLN A 182 
AA1 3 4 O THR A 176 ? O THR A 177 N CYS A 163 ? N CYS A 164 
AA1 4 5 O HIS A 158 ? O HIS A 159 N TYR A 144 ? N TYR A 145 
AA2 1 2 O ILE B 32  ? O ILE B 20  N LEU A 338 ? N LEU A 339 
AA2 2 3 O LEU A 339 ? O LEU A 340 N PHE A 287 ? N PHE A 288 
AA2 3 4 N ARG A 292 ? N ARG A 293 O LEU A 306 ? O LEU A 307 
AA2 4 5 N VAL A 307 ? N VAL A 308 O TRP B 65  ? O TRP B 53  
AA2 5 6 O ALA B 68  ? O ALA B 56  N LYS B 56  ? N LYS B 44  
AA2 6 7 O TRP B 55  ? O TRP B 43  N CYS B 48  ? N CYS B 36  
AA2 7 8 O TYR B 49  ? O TYR B 37  N THR B 40  ? N THR B 28  
# 
_pdbx_entry_details.entry_id                   9ERV 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ASN A 169 ? ? -126.49 -86.78 
2 1 HIS A 213 ? ? 38.41   55.74  
3 1 ASN A 283 ? ? -103.85 44.07  
4 1 ASN A 285 ? ? -156.16 26.17  
5 1 ASP A 371 ? ? -88.36  37.38  
# 
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 11.4373 72.3951 84.0008 -0.0501 ? 0.0093  ? 0.0004  ? -0.0248 ? -0.0147 ? -0.0401 ? 1.0210 ? 
0.3057  ? 0.0666  ? 0.3412 ? 0.0280 ? 0.3952 ? -0.0029 ? 0.0331  ? 0.0139  ? -0.0210 ? 0.0165 ? 0.0101  ? -0.0149 ? 0.0074 ? 
-0.0136 ? 
2 'X-RAY DIFFRACTION' ? refined 1.3474  59.1532 65.7593 -0.0888 ? -0.0069 ? -0.0116 ? -0.0468 ? -0.0014 ? -0.1949 ? 3.2254 ? 
-0.3677 ? -0.3069 ? 1.9349 ? 1.3361 ? 6.9338 ? 0.0161  ? -0.0420 ? -0.1005 ? 0.0482  ? 0.1333 ? -0.1115 ? 0.5420  ? 0.2764 ? 
-0.1494 ? 
# 
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|* }' 
2 'X-RAY DIFFRACTION' 2 ? ? ? ? ? ? ? ? ? ? ? '{ B|* }' 
# 
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 823 ? 5.84 . 
2 1 O ? A HOH 824 ? 6.12 . 
3 1 O ? A HOH 825 ? 6.98 . 
# 
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 GLY 2   ? A GLY 1   
2  1 Y 1 A SER 3   ? A SER 2   
3  1 Y 1 A GLU 4   ? A GLU 3   
4  1 Y 1 A VAL 5   ? A VAL 4   
5  1 Y 1 A TYR 6   ? A TYR 5   
6  1 Y 1 A GLN 7   ? A GLN 6   
7  1 Y 1 A SER 8   ? A SER 7   
8  1 Y 1 A GLN 9   ? A GLN 8   
9  1 Y 1 A LYS 10  ? A LYS 9   
10 1 Y 1 A CYS 11  ? A CYS 10  
11 1 Y 1 A GLU 12  ? A GLU 11  
12 1 Y 1 A PRO 93  ? A PRO 92  
13 1 Y 1 A SER 94  ? A SER 93  
14 1 Y 1 A LEU 95  ? A LEU 94  
15 1 Y 1 A ASP 96  ? A ASP 95  
16 1 Y 1 A GLY 97  ? A GLY 96  
17 1 Y 1 A GLY 98  ? A GLY 97  
18 1 Y 1 A ALA 99  ? A ALA 98  
19 1 Y 1 A THR 100 ? A THR 99  
20 1 Y 1 A ASN 101 ? A ASN 100 
21 1 Y 1 A ASN 102 ? A ASN 101 
22 1 Y 1 A THR 297 ? A THR 296 
23 1 Y 1 A LYS 298 ? A LYS 297 
24 1 Y 1 A ASN 299 ? A ASN 298 
25 1 Y 1 A GLY 300 ? A GLY 299 
26 1 Y 1 A LYS 301 ? A LYS 300 
27 1 Y 1 A ASP 302 ? A ASP 301 
28 1 Y 1 A THR 303 ? A THR 302 
29 1 Y 1 A VAL 373 ? A VAL 372 
30 1 Y 1 B MET -11 ? B MET 1   
31 1 Y 1 B LYS -10 ? B LYS 2   
32 1 Y 1 B HIS -9  ? B HIS 3   
33 1 Y 1 B HIS -8  ? B HIS 4   
34 1 Y 1 B HIS -7  ? B HIS 5   
35 1 Y 1 B HIS -6  ? B HIS 6   
36 1 Y 1 B HIS -5  ? B HIS 7   
37 1 Y 1 B HIS -4  ? B HIS 8   
38 1 Y 1 B GLY -3  ? B GLY 9   
39 1 Y 1 B SER -2  ? B SER 10  
40 1 Y 1 B SER -1  ? B SER 11  
41 1 Y 1 B GLY 0   ? B GLY 12  
42 1 Y 1 B MET 1   ? B MET 13  
43 1 Y 1 B GLN 2   ? B GLN 14  
44 1 Y 1 B ASP 3   ? B ASP 15  
45 1 Y 1 B GLN 4   ? B GLN 16  
46 1 Y 1 B ILE 5   ? B ILE 17  
47 1 Y 1 B ASP 6   ? B ASP 18  
48 1 Y 1 B ALA 7   ? B ALA 19  
49 1 Y 1 B LYS 8   ? B LYS 20  
50 1 Y 1 B VAL 9   ? B VAL 21  
51 1 Y 1 B ILE 10  ? B ILE 22  
52 1 Y 1 B ARG 11  ? B ARG 23  
53 1 Y 1 B ARG 12  ? B ARG 24  
54 1 Y 1 B ASN 13  ? B ASN 25  
55 1 Y 1 B PRO 14  ? B PRO 26  
56 1 Y 1 B ASP 58  ? B ASP 70  
57 1 Y 1 B GLU 59  ? B GLU 71  
58 1 Y 1 B HIS 60  ? B HIS 72  
59 1 Y 1 B THR 61  ? B THR 73  
60 1 Y 1 B VAL 62  ? B VAL 74  
61 1 Y 1 B MET 63  ? B MET 75  
62 1 Y 1 B GLU 64  ? B GLU 76  
63 1 Y 1 B VAL 65  ? B VAL 77  
64 1 Y 1 B ILE 66  ? B ILE 78  
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N      N  N N 1   
ALA CA     C  N S 2   
ALA C      C  N N 3   
ALA O      O  N N 4   
ALA CB     C  N N 5   
ALA OXT    O  N N 6   
ALA H      H  N N 7   
ALA H2     H  N N 8   
ALA HA     H  N N 9   
ALA HB1    H  N N 10  
ALA HB2    H  N N 11  
ALA HB3    H  N N 12  
ALA HXT    H  N N 13  
ARG N      N  N N 14  
ARG CA     C  N S 15  
ARG C      C  N N 16  
ARG O      O  N N 17  
ARG CB     C  N N 18  
ARG CG     C  N N 19  
ARG CD     C  N N 20  
ARG NE     N  N N 21  
ARG CZ     C  N N 22  
ARG NH1    N  N N 23  
ARG NH2    N  N N 24  
ARG OXT    O  N N 25  
ARG H      H  N N 26  
ARG H2     H  N N 27  
ARG HA     H  N N 28  
ARG HB2    H  N N 29  
ARG HB3    H  N N 30  
ARG HG2    H  N N 31  
ARG HG3    H  N N 32  
ARG HD2    H  N N 33  
ARG HD3    H  N N 34  
ARG HE     H  N N 35  
ARG HH11   H  N N 36  
ARG HH12   H  N N 37  
ARG HH21   H  N N 38  
ARG HH22   H  N N 39  
ARG HXT    H  N N 40  
ASN N      N  N N 41  
ASN CA     C  N S 42  
ASN C      C  N N 43  
ASN O      O  N N 44  
ASN CB     C  N N 45  
ASN CG     C  N N 46  
ASN OD1    O  N N 47  
ASN ND2    N  N N 48  
ASN OXT    O  N N 49  
ASN H      H  N N 50  
ASN H2     H  N N 51  
ASN HA     H  N N 52  
ASN HB2    H  N N 53  
ASN HB3    H  N N 54  
ASN HD21   H  N N 55  
ASN HD22   H  N N 56  
ASN HXT    H  N N 57  
ASP N      N  N N 58  
ASP CA     C  N S 59  
ASP C      C  N N 60  
ASP O      O  N N 61  
ASP CB     C  N N 62  
ASP CG     C  N N 63  
ASP OD1    O  N N 64  
ASP OD2    O  N N 65  
ASP OXT    O  N N 66  
ASP H      H  N N 67  
ASP H2     H  N N 68  
ASP HA     H  N N 69  
ASP HB2    H  N N 70  
ASP HB3    H  N N 71  
ASP HD2    H  N N 72  
ASP HXT    H  N N 73  
ATP PG     P  N N 74  
ATP O1G    O  N N 75  
ATP O2G    O  N N 76  
ATP O3G    O  N N 77  
ATP PB     P  N R 78  
ATP O1B    O  N N 79  
ATP O2B    O  N N 80  
ATP O3B    O  N N 81  
ATP PA     P  N R 82  
ATP O1A    O  N N 83  
ATP O2A    O  N N 84  
ATP O3A    O  N N 85  
ATP "O5'"  O  N N 86  
ATP "C5'"  C  N N 87  
ATP "C4'"  C  N R 88  
ATP "O4'"  O  N N 89  
ATP "C3'"  C  N S 90  
ATP "O3'"  O  N N 91  
ATP "C2'"  C  N R 92  
ATP "O2'"  O  N N 93  
ATP "C1'"  C  N R 94  
ATP N9     N  Y N 95  
ATP C8     C  Y N 96  
ATP N7     N  Y N 97  
ATP C5     C  Y N 98  
ATP C6     C  Y N 99  
ATP N6     N  N N 100 
ATP N1     N  Y N 101 
ATP C2     C  Y N 102 
ATP N3     N  Y N 103 
ATP C4     C  Y N 104 
ATP HOG2   H  N N 105 
ATP HOG3   H  N N 106 
ATP HOB2   H  N N 107 
ATP HOA2   H  N N 108 
ATP "H5'1" H  N N 109 
ATP "H5'2" H  N N 110 
ATP "H4'"  H  N N 111 
ATP "H3'"  H  N N 112 
ATP "HO3'" H  N N 113 
ATP "H2'"  H  N N 114 
ATP "HO2'" H  N N 115 
ATP "H1'"  H  N N 116 
ATP H8     H  N N 117 
ATP HN61   H  N N 118 
ATP HN62   H  N N 119 
ATP H2     H  N N 120 
CYS N      N  N N 121 
CYS CA     C  N R 122 
CYS C      C  N N 123 
CYS O      O  N N 124 
CYS CB     C  N N 125 
CYS SG     S  N N 126 
CYS OXT    O  N N 127 
CYS H      H  N N 128 
CYS H2     H  N N 129 
CYS HA     H  N N 130 
CYS HB2    H  N N 131 
CYS HB3    H  N N 132 
CYS HG     H  N N 133 
CYS HXT    H  N N 134 
GLN N      N  N N 135 
GLN CA     C  N S 136 
GLN C      C  N N 137 
GLN O      O  N N 138 
GLN CB     C  N N 139 
GLN CG     C  N N 140 
GLN CD     C  N N 141 
GLN OE1    O  N N 142 
GLN NE2    N  N N 143 
GLN OXT    O  N N 144 
GLN H      H  N N 145 
GLN H2     H  N N 146 
GLN HA     H  N N 147 
GLN HB2    H  N N 148 
GLN HB3    H  N N 149 
GLN HG2    H  N N 150 
GLN HG3    H  N N 151 
GLN HE21   H  N N 152 
GLN HE22   H  N N 153 
GLN HXT    H  N N 154 
GLU N      N  N N 155 
GLU CA     C  N S 156 
GLU C      C  N N 157 
GLU O      O  N N 158 
GLU CB     C  N N 159 
GLU CG     C  N N 160 
GLU CD     C  N N 161 
GLU OE1    O  N N 162 
GLU OE2    O  N N 163 
GLU OXT    O  N N 164 
GLU H      H  N N 165 
GLU H2     H  N N 166 
GLU HA     H  N N 167 
GLU HB2    H  N N 168 
GLU HB3    H  N N 169 
GLU HG2    H  N N 170 
GLU HG3    H  N N 171 
GLU HE2    H  N N 172 
GLU HXT    H  N N 173 
GLY N      N  N N 174 
GLY CA     C  N N 175 
GLY C      C  N N 176 
GLY O      O  N N 177 
GLY OXT    O  N N 178 
GLY H      H  N N 179 
GLY H2     H  N N 180 
GLY HA2    H  N N 181 
GLY HA3    H  N N 182 
GLY HXT    H  N N 183 
GOL C1     C  N N 184 
GOL O1     O  N N 185 
GOL C2     C  N N 186 
GOL O2     O  N N 187 
GOL C3     C  N N 188 
GOL O3     O  N N 189 
GOL H11    H  N N 190 
GOL H12    H  N N 191 
GOL HO1    H  N N 192 
GOL H2     H  N N 193 
GOL HO2    H  N N 194 
GOL H31    H  N N 195 
GOL H32    H  N N 196 
GOL HO3    H  N N 197 
HIS N      N  N N 198 
HIS CA     C  N S 199 
HIS C      C  N N 200 
HIS O      O  N N 201 
HIS CB     C  N N 202 
HIS CG     C  Y N 203 
HIS ND1    N  Y N 204 
HIS CD2    C  Y N 205 
HIS CE1    C  Y N 206 
HIS NE2    N  Y N 207 
HIS OXT    O  N N 208 
HIS H      H  N N 209 
HIS H2     H  N N 210 
HIS HA     H  N N 211 
HIS HB2    H  N N 212 
HIS HB3    H  N N 213 
HIS HD1    H  N N 214 
HIS HD2    H  N N 215 
HIS HE1    H  N N 216 
HIS HE2    H  N N 217 
HIS HXT    H  N N 218 
HOH O      O  N N 219 
HOH H1     H  N N 220 
HOH H2     H  N N 221 
ILE N      N  N N 222 
ILE CA     C  N S 223 
ILE C      C  N N 224 
ILE O      O  N N 225 
ILE CB     C  N S 226 
ILE CG1    C  N N 227 
ILE CG2    C  N N 228 
ILE CD1    C  N N 229 
ILE OXT    O  N N 230 
ILE H      H  N N 231 
ILE H2     H  N N 232 
ILE HA     H  N N 233 
ILE HB     H  N N 234 
ILE HG12   H  N N 235 
ILE HG13   H  N N 236 
ILE HG21   H  N N 237 
ILE HG22   H  N N 238 
ILE HG23   H  N N 239 
ILE HD11   H  N N 240 
ILE HD12   H  N N 241 
ILE HD13   H  N N 242 
ILE HXT    H  N N 243 
LEU N      N  N N 244 
LEU CA     C  N S 245 
LEU C      C  N N 246 
LEU O      O  N N 247 
LEU CB     C  N N 248 
LEU CG     C  N N 249 
LEU CD1    C  N N 250 
LEU CD2    C  N N 251 
LEU OXT    O  N N 252 
LEU H      H  N N 253 
LEU H2     H  N N 254 
LEU HA     H  N N 255 
LEU HB2    H  N N 256 
LEU HB3    H  N N 257 
LEU HG     H  N N 258 
LEU HD11   H  N N 259 
LEU HD12   H  N N 260 
LEU HD13   H  N N 261 
LEU HD21   H  N N 262 
LEU HD22   H  N N 263 
LEU HD23   H  N N 264 
LEU HXT    H  N N 265 
LYS N      N  N N 266 
LYS CA     C  N S 267 
LYS C      C  N N 268 
LYS O      O  N N 269 
LYS CB     C  N N 270 
LYS CG     C  N N 271 
LYS CD     C  N N 272 
LYS CE     C  N N 273 
LYS NZ     N  N N 274 
LYS OXT    O  N N 275 
LYS H      H  N N 276 
LYS H2     H  N N 277 
LYS HA     H  N N 278 
LYS HB2    H  N N 279 
LYS HB3    H  N N 280 
LYS HG2    H  N N 281 
LYS HG3    H  N N 282 
LYS HD2    H  N N 283 
LYS HD3    H  N N 284 
LYS HE2    H  N N 285 
LYS HE3    H  N N 286 
LYS HZ1    H  N N 287 
LYS HZ2    H  N N 288 
LYS HZ3    H  N N 289 
LYS HXT    H  N N 290 
MET N      N  N N 291 
MET CA     C  N S 292 
MET C      C  N N 293 
MET O      O  N N 294 
MET CB     C  N N 295 
MET CG     C  N N 296 
MET SD     S  N N 297 
MET CE     C  N N 298 
MET OXT    O  N N 299 
MET H      H  N N 300 
MET H2     H  N N 301 
MET HA     H  N N 302 
MET HB2    H  N N 303 
MET HB3    H  N N 304 
MET HG2    H  N N 305 
MET HG3    H  N N 306 
MET HE1    H  N N 307 
MET HE2    H  N N 308 
MET HE3    H  N N 309 
MET HXT    H  N N 310 
MG  MG     MG N N 311 
NA  NA     NA N N 312 
PHE N      N  N N 313 
PHE CA     C  N S 314 
PHE C      C  N N 315 
PHE O      O  N N 316 
PHE CB     C  N N 317 
PHE CG     C  Y N 318 
PHE CD1    C  Y N 319 
PHE CD2    C  Y N 320 
PHE CE1    C  Y N 321 
PHE CE2    C  Y N 322 
PHE CZ     C  Y N 323 
PHE OXT    O  N N 324 
PHE H      H  N N 325 
PHE H2     H  N N 326 
PHE HA     H  N N 327 
PHE HB2    H  N N 328 
PHE HB3    H  N N 329 
PHE HD1    H  N N 330 
PHE HD2    H  N N 331 
PHE HE1    H  N N 332 
PHE HE2    H  N N 333 
PHE HZ     H  N N 334 
PHE HXT    H  N N 335 
PRO N      N  N N 336 
PRO CA     C  N S 337 
PRO C      C  N N 338 
PRO O      O  N N 339 
PRO CB     C  N N 340 
PRO CG     C  N N 341 
PRO CD     C  N N 342 
PRO OXT    O  N N 343 
PRO H      H  N N 344 
PRO HA     H  N N 345 
PRO HB2    H  N N 346 
PRO HB3    H  N N 347 
PRO HG2    H  N N 348 
PRO HG3    H  N N 349 
PRO HD2    H  N N 350 
PRO HD3    H  N N 351 
PRO HXT    H  N N 352 
SER N      N  N N 353 
SER CA     C  N S 354 
SER C      C  N N 355 
SER O      O  N N 356 
SER CB     C  N N 357 
SER OG     O  N N 358 
SER OXT    O  N N 359 
SER H      H  N N 360 
SER H2     H  N N 361 
SER HA     H  N N 362 
SER HB2    H  N N 363 
SER HB3    H  N N 364 
SER HG     H  N N 365 
SER HXT    H  N N 366 
THR N      N  N N 367 
THR CA     C  N S 368 
THR C      C  N N 369 
THR O      O  N N 370 
THR CB     C  N R 371 
THR OG1    O  N N 372 
THR CG2    C  N N 373 
THR OXT    O  N N 374 
THR H      H  N N 375 
THR H2     H  N N 376 
THR HA     H  N N 377 
THR HB     H  N N 378 
THR HG1    H  N N 379 
THR HG21   H  N N 380 
THR HG22   H  N N 381 
THR HG23   H  N N 382 
THR HXT    H  N N 383 
TRP N      N  N N 384 
TRP CA     C  N S 385 
TRP C      C  N N 386 
TRP O      O  N N 387 
TRP CB     C  N N 388 
TRP CG     C  Y N 389 
TRP CD1    C  Y N 390 
TRP CD2    C  Y N 391 
TRP NE1    N  Y N 392 
TRP CE2    C  Y N 393 
TRP CE3    C  Y N 394 
TRP CZ2    C  Y N 395 
TRP CZ3    C  Y N 396 
TRP CH2    C  Y N 397 
TRP OXT    O  N N 398 
TRP H      H  N N 399 
TRP H2     H  N N 400 
TRP HA     H  N N 401 
TRP HB2    H  N N 402 
TRP HB3    H  N N 403 
TRP HD1    H  N N 404 
TRP HE1    H  N N 405 
TRP HE3    H  N N 406 
TRP HZ2    H  N N 407 
TRP HZ3    H  N N 408 
TRP HH2    H  N N 409 
TRP HXT    H  N N 410 
TYR N      N  N N 411 
TYR CA     C  N S 412 
TYR C      C  N N 413 
TYR O      O  N N 414 
TYR CB     C  N N 415 
TYR CG     C  Y N 416 
TYR CD1    C  Y N 417 
TYR CD2    C  Y N 418 
TYR CE1    C  Y N 419 
TYR CE2    C  Y N 420 
TYR CZ     C  Y N 421 
TYR OH     O  N N 422 
TYR OXT    O  N N 423 
TYR H      H  N N 424 
TYR H2     H  N N 425 
TYR HA     H  N N 426 
TYR HB2    H  N N 427 
TYR HB3    H  N N 428 
TYR HD1    H  N N 429 
TYR HD2    H  N N 430 
TYR HE1    H  N N 431 
TYR HE2    H  N N 432 
TYR HH     H  N N 433 
TYR HXT    H  N N 434 
VAL N      N  N N 435 
VAL CA     C  N S 436 
VAL C      C  N N 437 
VAL O      O  N N 438 
VAL CB     C  N N 439 
VAL CG1    C  N N 440 
VAL CG2    C  N N 441 
VAL OXT    O  N N 442 
VAL H      H  N N 443 
VAL H2     H  N N 444 
VAL HA     H  N N 445 
VAL HB     H  N N 446 
VAL HG11   H  N N 447 
VAL HG12   H  N N 448 
VAL HG13   H  N N 449 
VAL HG21   H  N N 450 
VAL HG22   H  N N 451 
VAL HG23   H  N N 452 
VAL HXT    H  N N 453 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N     CA     sing N N 1   
ALA N     H      sing N N 2   
ALA N     H2     sing N N 3   
ALA CA    C      sing N N 4   
ALA CA    CB     sing N N 5   
ALA CA    HA     sing N N 6   
ALA C     O      doub N N 7   
ALA C     OXT    sing N N 8   
ALA CB    HB1    sing N N 9   
ALA CB    HB2    sing N N 10  
ALA CB    HB3    sing N N 11  
ALA OXT   HXT    sing N N 12  
ARG N     CA     sing N N 13  
ARG N     H      sing N N 14  
ARG N     H2     sing N N 15  
ARG CA    C      sing N N 16  
ARG CA    CB     sing N N 17  
ARG CA    HA     sing N N 18  
ARG C     O      doub N N 19  
ARG C     OXT    sing N N 20  
ARG CB    CG     sing N N 21  
ARG CB    HB2    sing N N 22  
ARG CB    HB3    sing N N 23  
ARG CG    CD     sing N N 24  
ARG CG    HG2    sing N N 25  
ARG CG    HG3    sing N N 26  
ARG CD    NE     sing N N 27  
ARG CD    HD2    sing N N 28  
ARG CD    HD3    sing N N 29  
ARG NE    CZ     sing N N 30  
ARG NE    HE     sing N N 31  
ARG CZ    NH1    sing N N 32  
ARG CZ    NH2    doub N N 33  
ARG NH1   HH11   sing N N 34  
ARG NH1   HH12   sing N N 35  
ARG NH2   HH21   sing N N 36  
ARG NH2   HH22   sing N N 37  
ARG OXT   HXT    sing N N 38  
ASN N     CA     sing N N 39  
ASN N     H      sing N N 40  
ASN N     H2     sing N N 41  
ASN CA    C      sing N N 42  
ASN CA    CB     sing N N 43  
ASN CA    HA     sing N N 44  
ASN C     O      doub N N 45  
ASN C     OXT    sing N N 46  
ASN CB    CG     sing N N 47  
ASN CB    HB2    sing N N 48  
ASN CB    HB3    sing N N 49  
ASN CG    OD1    doub N N 50  
ASN CG    ND2    sing N N 51  
ASN ND2   HD21   sing N N 52  
ASN ND2   HD22   sing N N 53  
ASN OXT   HXT    sing N N 54  
ASP N     CA     sing N N 55  
ASP N     H      sing N N 56  
ASP N     H2     sing N N 57  
ASP CA    C      sing N N 58  
ASP CA    CB     sing N N 59  
ASP CA    HA     sing N N 60  
ASP C     O      doub N N 61  
ASP C     OXT    sing N N 62  
ASP CB    CG     sing N N 63  
ASP CB    HB2    sing N N 64  
ASP CB    HB3    sing N N 65  
ASP CG    OD1    doub N N 66  
ASP CG    OD2    sing N N 67  
ASP OD2   HD2    sing N N 68  
ASP OXT   HXT    sing N N 69  
ATP PG    O1G    doub N N 70  
ATP PG    O2G    sing N N 71  
ATP PG    O3G    sing N N 72  
ATP PG    O3B    sing N N 73  
ATP O2G   HOG2   sing N N 74  
ATP O3G   HOG3   sing N N 75  
ATP PB    O1B    doub N N 76  
ATP PB    O2B    sing N N 77  
ATP PB    O3B    sing N N 78  
ATP PB    O3A    sing N N 79  
ATP O2B   HOB2   sing N N 80  
ATP PA    O1A    doub N N 81  
ATP PA    O2A    sing N N 82  
ATP PA    O3A    sing N N 83  
ATP PA    "O5'"  sing N N 84  
ATP O2A   HOA2   sing N N 85  
ATP "O5'" "C5'"  sing N N 86  
ATP "C5'" "C4'"  sing N N 87  
ATP "C5'" "H5'1" sing N N 88  
ATP "C5'" "H5'2" sing N N 89  
ATP "C4'" "O4'"  sing N N 90  
ATP "C4'" "C3'"  sing N N 91  
ATP "C4'" "H4'"  sing N N 92  
ATP "O4'" "C1'"  sing N N 93  
ATP "C3'" "O3'"  sing N N 94  
ATP "C3'" "C2'"  sing N N 95  
ATP "C3'" "H3'"  sing N N 96  
ATP "O3'" "HO3'" sing N N 97  
ATP "C2'" "O2'"  sing N N 98  
ATP "C2'" "C1'"  sing N N 99  
ATP "C2'" "H2'"  sing N N 100 
ATP "O2'" "HO2'" sing N N 101 
ATP "C1'" N9     sing N N 102 
ATP "C1'" "H1'"  sing N N 103 
ATP N9    C8     sing Y N 104 
ATP N9    C4     sing Y N 105 
ATP C8    N7     doub Y N 106 
ATP C8    H8     sing N N 107 
ATP N7    C5     sing Y N 108 
ATP C5    C6     sing Y N 109 
ATP C5    C4     doub Y N 110 
ATP C6    N6     sing N N 111 
ATP C6    N1     doub Y N 112 
ATP N6    HN61   sing N N 113 
ATP N6    HN62   sing N N 114 
ATP N1    C2     sing Y N 115 
ATP C2    N3     doub Y N 116 
ATP C2    H2     sing N N 117 
ATP N3    C4     sing Y N 118 
CYS N     CA     sing N N 119 
CYS N     H      sing N N 120 
CYS N     H2     sing N N 121 
CYS CA    C      sing N N 122 
CYS CA    CB     sing N N 123 
CYS CA    HA     sing N N 124 
CYS C     O      doub N N 125 
CYS C     OXT    sing N N 126 
CYS CB    SG     sing N N 127 
CYS CB    HB2    sing N N 128 
CYS CB    HB3    sing N N 129 
CYS SG    HG     sing N N 130 
CYS OXT   HXT    sing N N 131 
GLN N     CA     sing N N 132 
GLN N     H      sing N N 133 
GLN N     H2     sing N N 134 
GLN CA    C      sing N N 135 
GLN CA    CB     sing N N 136 
GLN CA    HA     sing N N 137 
GLN C     O      doub N N 138 
GLN C     OXT    sing N N 139 
GLN CB    CG     sing N N 140 
GLN CB    HB2    sing N N 141 
GLN CB    HB3    sing N N 142 
GLN CG    CD     sing N N 143 
GLN CG    HG2    sing N N 144 
GLN CG    HG3    sing N N 145 
GLN CD    OE1    doub N N 146 
GLN CD    NE2    sing N N 147 
GLN NE2   HE21   sing N N 148 
GLN NE2   HE22   sing N N 149 
GLN OXT   HXT    sing N N 150 
GLU N     CA     sing N N 151 
GLU N     H      sing N N 152 
GLU N     H2     sing N N 153 
GLU CA    C      sing N N 154 
GLU CA    CB     sing N N 155 
GLU CA    HA     sing N N 156 
GLU C     O      doub N N 157 
GLU C     OXT    sing N N 158 
GLU CB    CG     sing N N 159 
GLU CB    HB2    sing N N 160 
GLU CB    HB3    sing N N 161 
GLU CG    CD     sing N N 162 
GLU CG    HG2    sing N N 163 
GLU CG    HG3    sing N N 164 
GLU CD    OE1    doub N N 165 
GLU CD    OE2    sing N N 166 
GLU OE2   HE2    sing N N 167 
GLU OXT   HXT    sing N N 168 
GLY N     CA     sing N N 169 
GLY N     H      sing N N 170 
GLY N     H2     sing N N 171 
GLY CA    C      sing N N 172 
GLY CA    HA2    sing N N 173 
GLY CA    HA3    sing N N 174 
GLY C     O      doub N N 175 
GLY C     OXT    sing N N 176 
GLY OXT   HXT    sing N N 177 
GOL C1    O1     sing N N 178 
GOL C1    C2     sing N N 179 
GOL C1    H11    sing N N 180 
GOL C1    H12    sing N N 181 
GOL O1    HO1    sing N N 182 
GOL C2    O2     sing N N 183 
GOL C2    C3     sing N N 184 
GOL C2    H2     sing N N 185 
GOL O2    HO2    sing N N 186 
GOL C3    O3     sing N N 187 
GOL C3    H31    sing N N 188 
GOL C3    H32    sing N N 189 
GOL O3    HO3    sing N N 190 
HIS N     CA     sing N N 191 
HIS N     H      sing N N 192 
HIS N     H2     sing N N 193 
HIS CA    C      sing N N 194 
HIS CA    CB     sing N N 195 
HIS CA    HA     sing N N 196 
HIS C     O      doub N N 197 
HIS C     OXT    sing N N 198 
HIS CB    CG     sing N N 199 
HIS CB    HB2    sing N N 200 
HIS CB    HB3    sing N N 201 
HIS CG    ND1    sing Y N 202 
HIS CG    CD2    doub Y N 203 
HIS ND1   CE1    doub Y N 204 
HIS ND1   HD1    sing N N 205 
HIS CD2   NE2    sing Y N 206 
HIS CD2   HD2    sing N N 207 
HIS CE1   NE2    sing Y N 208 
HIS CE1   HE1    sing N N 209 
HIS NE2   HE2    sing N N 210 
HIS OXT   HXT    sing N N 211 
HOH O     H1     sing N N 212 
HOH O     H2     sing N N 213 
ILE N     CA     sing N N 214 
ILE N     H      sing N N 215 
ILE N     H2     sing N N 216 
ILE CA    C      sing N N 217 
ILE CA    CB     sing N N 218 
ILE CA    HA     sing N N 219 
ILE C     O      doub N N 220 
ILE C     OXT    sing N N 221 
ILE CB    CG1    sing N N 222 
ILE CB    CG2    sing N N 223 
ILE CB    HB     sing N N 224 
ILE CG1   CD1    sing N N 225 
ILE CG1   HG12   sing N N 226 
ILE CG1   HG13   sing N N 227 
ILE CG2   HG21   sing N N 228 
ILE CG2   HG22   sing N N 229 
ILE CG2   HG23   sing N N 230 
ILE CD1   HD11   sing N N 231 
ILE CD1   HD12   sing N N 232 
ILE CD1   HD13   sing N N 233 
ILE OXT   HXT    sing N N 234 
LEU N     CA     sing N N 235 
LEU N     H      sing N N 236 
LEU N     H2     sing N N 237 
LEU CA    C      sing N N 238 
LEU CA    CB     sing N N 239 
LEU CA    HA     sing N N 240 
LEU C     O      doub N N 241 
LEU C     OXT    sing N N 242 
LEU CB    CG     sing N N 243 
LEU CB    HB2    sing N N 244 
LEU CB    HB3    sing N N 245 
LEU CG    CD1    sing N N 246 
LEU CG    CD2    sing N N 247 
LEU CG    HG     sing N N 248 
LEU CD1   HD11   sing N N 249 
LEU CD1   HD12   sing N N 250 
LEU CD1   HD13   sing N N 251 
LEU CD2   HD21   sing N N 252 
LEU CD2   HD22   sing N N 253 
LEU CD2   HD23   sing N N 254 
LEU OXT   HXT    sing N N 255 
LYS N     CA     sing N N 256 
LYS N     H      sing N N 257 
LYS N     H2     sing N N 258 
LYS CA    C      sing N N 259 
LYS CA    CB     sing N N 260 
LYS CA    HA     sing N N 261 
LYS C     O      doub N N 262 
LYS C     OXT    sing N N 263 
LYS CB    CG     sing N N 264 
LYS CB    HB2    sing N N 265 
LYS CB    HB3    sing N N 266 
LYS CG    CD     sing N N 267 
LYS CG    HG2    sing N N 268 
LYS CG    HG3    sing N N 269 
LYS CD    CE     sing N N 270 
LYS CD    HD2    sing N N 271 
LYS CD    HD3    sing N N 272 
LYS CE    NZ     sing N N 273 
LYS CE    HE2    sing N N 274 
LYS CE    HE3    sing N N 275 
LYS NZ    HZ1    sing N N 276 
LYS NZ    HZ2    sing N N 277 
LYS NZ    HZ3    sing N N 278 
LYS OXT   HXT    sing N N 279 
MET N     CA     sing N N 280 
MET N     H      sing N N 281 
MET N     H2     sing N N 282 
MET CA    C      sing N N 283 
MET CA    CB     sing N N 284 
MET CA    HA     sing N N 285 
MET C     O      doub N N 286 
MET C     OXT    sing N N 287 
MET CB    CG     sing N N 288 
MET CB    HB2    sing N N 289 
MET CB    HB3    sing N N 290 
MET CG    SD     sing N N 291 
MET CG    HG2    sing N N 292 
MET CG    HG3    sing N N 293 
MET SD    CE     sing N N 294 
MET CE    HE1    sing N N 295 
MET CE    HE2    sing N N 296 
MET CE    HE3    sing N N 297 
MET OXT   HXT    sing N N 298 
PHE N     CA     sing N N 299 
PHE N     H      sing N N 300 
PHE N     H2     sing N N 301 
PHE CA    C      sing N N 302 
PHE CA    CB     sing N N 303 
PHE CA    HA     sing N N 304 
PHE C     O      doub N N 305 
PHE C     OXT    sing N N 306 
PHE CB    CG     sing N N 307 
PHE CB    HB2    sing N N 308 
PHE CB    HB3    sing N N 309 
PHE CG    CD1    doub Y N 310 
PHE CG    CD2    sing Y N 311 
PHE CD1   CE1    sing Y N 312 
PHE CD1   HD1    sing N N 313 
PHE CD2   CE2    doub Y N 314 
PHE CD2   HD2    sing N N 315 
PHE CE1   CZ     doub Y N 316 
PHE CE1   HE1    sing N N 317 
PHE CE2   CZ     sing Y N 318 
PHE CE2   HE2    sing N N 319 
PHE CZ    HZ     sing N N 320 
PHE OXT   HXT    sing N N 321 
PRO N     CA     sing N N 322 
PRO N     CD     sing N N 323 
PRO N     H      sing N N 324 
PRO CA    C      sing N N 325 
PRO CA    CB     sing N N 326 
PRO CA    HA     sing N N 327 
PRO C     O      doub N N 328 
PRO C     OXT    sing N N 329 
PRO CB    CG     sing N N 330 
PRO CB    HB2    sing N N 331 
PRO CB    HB3    sing N N 332 
PRO CG    CD     sing N N 333 
PRO CG    HG2    sing N N 334 
PRO CG    HG3    sing N N 335 
PRO CD    HD2    sing N N 336 
PRO CD    HD3    sing N N 337 
PRO OXT   HXT    sing N N 338 
SER N     CA     sing N N 339 
SER N     H      sing N N 340 
SER N     H2     sing N N 341 
SER CA    C      sing N N 342 
SER CA    CB     sing N N 343 
SER CA    HA     sing N N 344 
SER C     O      doub N N 345 
SER C     OXT    sing N N 346 
SER CB    OG     sing N N 347 
SER CB    HB2    sing N N 348 
SER CB    HB3    sing N N 349 
SER OG    HG     sing N N 350 
SER OXT   HXT    sing N N 351 
THR N     CA     sing N N 352 
THR N     H      sing N N 353 
THR N     H2     sing N N 354 
THR CA    C      sing N N 355 
THR CA    CB     sing N N 356 
THR CA    HA     sing N N 357 
THR C     O      doub N N 358 
THR C     OXT    sing N N 359 
THR CB    OG1    sing N N 360 
THR CB    CG2    sing N N 361 
THR CB    HB     sing N N 362 
THR OG1   HG1    sing N N 363 
THR CG2   HG21   sing N N 364 
THR CG2   HG22   sing N N 365 
THR CG2   HG23   sing N N 366 
THR OXT   HXT    sing N N 367 
TRP N     CA     sing N N 368 
TRP N     H      sing N N 369 
TRP N     H2     sing N N 370 
TRP CA    C      sing N N 371 
TRP CA    CB     sing N N 372 
TRP CA    HA     sing N N 373 
TRP C     O      doub N N 374 
TRP C     OXT    sing N N 375 
TRP CB    CG     sing N N 376 
TRP CB    HB2    sing N N 377 
TRP CB    HB3    sing N N 378 
TRP CG    CD1    doub Y N 379 
TRP CG    CD2    sing Y N 380 
TRP CD1   NE1    sing Y N 381 
TRP CD1   HD1    sing N N 382 
TRP CD2   CE2    doub Y N 383 
TRP CD2   CE3    sing Y N 384 
TRP NE1   CE2    sing Y N 385 
TRP NE1   HE1    sing N N 386 
TRP CE2   CZ2    sing Y N 387 
TRP CE3   CZ3    doub Y N 388 
TRP CE3   HE3    sing N N 389 
TRP CZ2   CH2    doub Y N 390 
TRP CZ2   HZ2    sing N N 391 
TRP CZ3   CH2    sing Y N 392 
TRP CZ3   HZ3    sing N N 393 
TRP CH2   HH2    sing N N 394 
TRP OXT   HXT    sing N N 395 
TYR N     CA     sing N N 396 
TYR N     H      sing N N 397 
TYR N     H2     sing N N 398 
TYR CA    C      sing N N 399 
TYR CA    CB     sing N N 400 
TYR CA    HA     sing N N 401 
TYR C     O      doub N N 402 
TYR C     OXT    sing N N 403 
TYR CB    CG     sing N N 404 
TYR CB    HB2    sing N N 405 
TYR CB    HB3    sing N N 406 
TYR CG    CD1    doub Y N 407 
TYR CG    CD2    sing Y N 408 
TYR CD1   CE1    sing Y N 409 
TYR CD1   HD1    sing N N 410 
TYR CD2   CE2    doub Y N 411 
TYR CD2   HD2    sing N N 412 
TYR CE1   CZ     doub Y N 413 
TYR CE1   HE1    sing N N 414 
TYR CE2   CZ     sing Y N 415 
TYR CE2   HE2    sing N N 416 
TYR CZ    OH     sing N N 417 
TYR OH    HH     sing N N 418 
TYR OXT   HXT    sing N N 419 
VAL N     CA     sing N N 420 
VAL N     H      sing N N 421 
VAL N     H2     sing N N 422 
VAL CA    C      sing N N 423 
VAL CA    CB     sing N N 424 
VAL CA    HA     sing N N 425 
VAL C     O      doub N N 426 
VAL C     OXT    sing N N 427 
VAL CB    CG1    sing N N 428 
VAL CB    CG2    sing N N 429 
VAL CB    HB     sing N N 430 
VAL CG1   HG11   sing N N 431 
VAL CG1   HG12   sing N N 432 
VAL CG1   HG13   sing N N 433 
VAL CG2   HG21   sing N N 434 
VAL CG2   HG22   sing N N 435 
VAL CG2   HG23   sing N N 436 
VAL OXT   HXT    sing N N 437 
# 
_pdbx_audit_support.funding_organization   'European Research Council (ERC)' 
_pdbx_audit_support.country                'European Union' 
_pdbx_audit_support.grant_number           864311 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   7ZTB 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9ERV 
_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]   0.020123 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.009684 
_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]   0.004779 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C  
MG 
N  
NA 
O  
P  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N     . LEU A 1 12  ? 37.187  91.564  82.211  1.00 65.95  ?  13  LEU A N     1 
ATOM   2    C  CA    . LEU A 1 12  ? 37.823  90.304  82.597  1.00 66.18  ?  13  LEU A CA    1 
ATOM   3    C  C     . LEU A 1 12  ? 37.993  90.182  84.115  1.00 65.97  ?  13  LEU A C     1 
ATOM   4    O  O     . LEU A 1 12  ? 37.959  89.071  84.651  1.00 66.00  ?  13  LEU A O     1 
ATOM   5    C  CB    . LEU A 1 12  ? 39.179  90.140  81.892  1.00 66.60  ?  13  LEU A CB    1 
ATOM   6    N  N     . LYS A 1 13  ? 38.179  91.318  84.804  1.00 65.53  ?  14  LYS A N     1 
ATOM   7    C  CA    . LYS A 1 13  ? 38.376  91.327  86.252  1.00 65.50  ?  14  LYS A CA    1 
ATOM   8    C  C     . LYS A 1 13  ? 37.440  92.327  86.959  1.00 64.96  ?  14  LYS A C     1 
ATOM   9    O  O     . LYS A 1 13  ? 37.816  93.482  87.186  1.00 65.69  ?  14  LYS A O     1 
ATOM   10   C  CB    . LYS A 1 13  ? 39.851  91.622  86.587  1.00 67.54  ?  14  LYS A CB    1 
ATOM   11   N  N     . TYR A 1 14  ? 36.219  91.886  87.296  1.00 63.30  ?  15  TYR A N     1 
ATOM   12   C  CA    . TYR A 1 14  ? 35.257  92.751  87.968  1.00 62.10  ?  15  TYR A CA    1 
ATOM   13   C  C     . TYR A 1 14  ? 35.109  92.331  89.419  1.00 61.01  ?  15  TYR A C     1 
ATOM   14   O  O     . TYR A 1 14  ? 34.950  91.146  89.711  1.00 61.01  ?  15  TYR A O     1 
ATOM   15   C  CB    . TYR A 1 14  ? 33.874  92.707  87.290  1.00 61.56  ?  15  TYR A CB    1 
ATOM   16   C  CG    . TYR A 1 14  ? 33.881  92.966  85.802  1.00 61.73  ?  15  TYR A CG    1 
ATOM   17   C  CD1   . TYR A 1 14  ? 34.158  94.227  85.296  1.00 62.67  ?  15  TYR A CD1   1 
ATOM   18   C  CD2   . TYR A 1 14  ? 33.542  91.967  84.904  1.00 62.31  ?  15  TYR A CD2   1 
ATOM   19   C  CE1   . TYR A 1 14  ? 34.153  94.473  83.927  1.00 63.66  ?  15  TYR A CE1   1 
ATOM   20   C  CE2   . TYR A 1 14  ? 33.519  92.202  83.535  1.00 63.32  ?  15  TYR A CE2   1 
ATOM   21   C  CZ    . TYR A 1 14  ? 33.813  93.460  83.048  1.00 64.36  ?  15  TYR A CZ    1 
ATOM   22   O  OH    . TYR A 1 14  ? 33.781  93.683  81.692  1.00 65.58  ?  15  TYR A OH    1 
ATOM   23   N  N     . SER A 1 15  ? 35.126  93.304  90.322  1.00 59.90  ?  16  SER A N     1 
ATOM   24   C  CA    . SER A 1 15  ? 34.953  93.066  91.752  1.00 59.09  ?  16  SER A CA    1 
ATOM   25   C  C     . SER A 1 15  ? 33.472  92.819  92.094  1.00 57.68  ?  16  SER A C     1 
ATOM   26   O  O     . SER A 1 15  ? 32.594  93.188  91.312  1.00 57.71  ?  16  SER A O     1 
ATOM   27   C  CB    . SER A 1 15  ? 35.487  94.259  92.542  1.00 60.85  ?  16  SER A CB    1 
ATOM   28   O  OG    . SER A 1 15  ? 35.004  95.490  92.027  1.00 62.99  ?  16  SER A OG    1 
ATOM   29   N  N     . LYS A 1 16  ? 33.184  92.215  93.265  1.00 56.25  ?  17  LYS A N     1 
ATOM   30   C  CA    . LYS A 1 16  ? 31.797  91.946  93.660  1.00 55.41  ?  17  LYS A CA    1 
ATOM   31   C  C     . LYS A 1 16  ? 30.961  93.208  93.891  1.00 54.72  ?  17  LYS A C     1 
ATOM   32   O  O     . LYS A 1 16  ? 29.731  93.130  93.900  1.00 54.93  ?  17  LYS A O     1 
ATOM   33   C  CB    . LYS A 1 16  ? 31.714  91.012  94.875  1.00 57.07  ?  17  LYS A CB    1 
ATOM   34   C  CG    . LYS A 1 16  ? 30.487  90.101  94.837  1.00 60.24  ?  17  LYS A CG    1 
ATOM   35   C  CD    . LYS A 1 16  ? 30.295  89.322  96.123  1.00 63.97  ?  17  LYS A CD    1 
ATOM   36   C  CE    . LYS A 1 16  ? 29.878  90.210  97.266  1.00 67.55  ?  17  LYS A CE    1 
ATOM   37   N  NZ    . LYS A 1 16  ? 29.346  89.413  98.407  1.00 69.61  ?  17  LYS A NZ    1 
ATOM   38   N  N     . SER A 1 17  ? 31.615  94.365  94.085  1.00 53.83  ?  18  SER A N     1 
ATOM   39   C  CA    . SER A 1 17  ? 30.906  95.629  94.251  1.00 53.27  ?  18  SER A CA    1 
ATOM   40   C  C     . SER A 1 17  ? 30.426  96.113  92.877  1.00 51.27  ?  18  SER A C     1 
ATOM   41   O  O     . SER A 1 17  ? 29.290  96.566  92.757  1.00 51.73  ?  18  SER A O     1 
ATOM   42   C  CB    . SER A 1 17  ? 31.803  96.675  94.908  1.00 55.92  ?  18  SER A CB    1 
ATOM   43   O  OG    . SER A 1 17  ? 32.947  96.968  94.119  1.00 59.35  ?  18  SER A OG    1 
ATOM   44   N  N     . GLN A 1 18  ? 31.279  95.983  91.843  1.00 48.97  ?  19  GLN A N     1 
ATOM   45   C  CA    . GLN A 1 18  ? 30.963  96.348  90.464  1.00 47.49  ?  19  GLN A CA    1 
ATOM   46   C  C     . GLN A 1 18  ? 29.822  95.485  89.911  1.00 45.15  ?  19  GLN A C     1 
ATOM   47   O  O     . GLN A 1 18  ? 29.034  95.965  89.106  1.00 45.08  ?  19  GLN A O     1 
ATOM   48   C  CB    . GLN A 1 18  ? 32.203  96.173  89.560  1.00 49.53  ?  19  GLN A CB    1 
ATOM   49   C  CG    . GLN A 1 18  ? 33.282  97.235  89.742  1.00 53.62  ?  19  GLN A CG    1 
ATOM   50   C  CD    . GLN A 1 18  ? 34.374  97.132  88.699  1.00 58.43  ?  19  GLN A CD    1 
ATOM   51   O  OE1   . GLN A 1 18  ? 34.460  97.939  87.765  1.00 60.55  ?  19  GLN A OE1   1 
ATOM   52   N  NE2   . GLN A 1 18  ? 35.242  96.145  88.836  1.00 58.79  ?  19  GLN A NE2   1 
ATOM   53   N  N     . ILE A 1 19  ? 29.746  94.215  90.327  1.00 43.18  ?  20  ILE A N     1 
ATOM   54   C  CA    . ILE A 1 19  ? 28.724  93.283  89.865  1.00 41.71  ?  20  ILE A CA    1 
ATOM   55   C  C     . ILE A 1 19  ? 27.381  93.587  90.523  1.00 40.42  ?  20  ILE A C     1 
ATOM   56   O  O     . ILE A 1 19  ? 26.365  93.613  89.837  1.00 40.21  ?  20  ILE A O     1 
ATOM   57   C  CB    . ILE A 1 19  ? 29.212  91.816  90.028  1.00 41.92  ?  20  ILE A CB    1 
ATOM   58   C  CG1   . ILE A 1 19  ? 30.258  91.503  88.942  1.00 42.94  ?  20  ILE A CG1   1 
ATOM   59   C  CG2   . ILE A 1 19  ? 28.060  90.812  90.002  1.00 41.90  ?  20  ILE A CG2   1 
ATOM   60   C  CD1   . ILE A 1 19  ? 30.962  90.205  89.075  1.00 44.45  ?  20  ILE A CD1   1 
ATOM   61   N  N     . GLU A 1 20  ? 27.378  93.912  91.819  1.00 39.57  ?  21  GLU A N     1 
ATOM   62   C  CA    . GLU A 1 20  ? 26.153  94.300  92.511  1.00 39.04  ?  21  GLU A CA    1 
ATOM   63   C  C     . GLU A 1 20  ? 25.627  95.629  91.936  1.00 38.23  ?  21  GLU A C     1 
ATOM   64   O  O     . GLU A 1 20  ? 24.415  95.781  91.770  1.00 37.84  ?  21  GLU A O     1 
ATOM   65   C  CB    . GLU A 1 20  ? 26.392  94.411  94.027  1.00 41.70  ?  21  GLU A CB    1 
ATOM   66   N  N     . LYS A 1 21  ? 26.542  96.563  91.584  1.00 37.76  ?  22  LYS A N     1 
ATOM   67   C  CA    . LYS A 1 21  ? 26.179  97.847  90.984  1.00 38.28  ?  22  LYS A CA    1 
ATOM   68   C  C     . LYS A 1 21  ? 25.658  97.677  89.557  1.00 37.59  ?  22  LYS A C     1 
ATOM   69   O  O     . LYS A 1 21  ? 24.738  98.399  89.169  1.00 38.00  ?  22  LYS A O     1 
ATOM   70   C  CB    . LYS A 1 21  ? 27.352  98.837  91.019  1.00 41.46  ?  22  LYS A CB    1 
ATOM   71   C  CG    . LYS A 1 21  ? 26.930  100.276 90.728  1.00 47.43  ?  22  LYS A CG    1 
ATOM   72   C  CD    . LYS A 1 21  ? 28.113  101.246 90.797  1.00 52.78  ?  22  LYS A CD    1 
ATOM   73   C  CE    . LYS A 1 21  ? 28.557  101.726 89.436  1.00 56.72  ?  22  LYS A CE    1 
ATOM   74   N  NZ    . LYS A 1 21  ? 30.042  101.841 89.347  1.00 59.16  1  22  LYS A NZ    1 
ATOM   75   N  N     . ALA A 1 22  ? 26.217  96.702  88.783  1.00 36.11  ?  23  ALA A N     1 
ATOM   76   C  CA    . ALA A 1 22  ? 25.761  96.393  87.417  1.00 34.98  ?  23  ALA A CA    1 
ATOM   77   C  C     . ALA A 1 22  ? 24.348  95.836  87.451  1.00 34.11  ?  23  ALA A C     1 
ATOM   78   O  O     . ALA A 1 22  ? 23.538  96.172  86.598  1.00 34.16  ?  23  ALA A O     1 
ATOM   79   C  CB    . ALA A 1 22  ? 26.692  95.395  86.746  1.00 34.60  ?  23  ALA A CB    1 
ATOM   80   N  N     . ALA A 1 23  ? 24.047  94.991  88.440  1.00 33.65  ?  24  ALA A N     1 
ATOM   81   C  CA    . ALA A 1 23  ? 22.717  94.419  88.616  1.00 33.88  ?  24  ALA A CA    1 
ATOM   82   C  C     . ALA A 1 23  ? 21.675  95.499  89.012  1.00 33.85  ?  24  ALA A C     1 
ATOM   83   O  O     . ALA A 1 23  ? 20.535  95.436  88.560  1.00 33.29  ?  24  ALA A O     1 
ATOM   84   C  CB    . ALA A 1 23  ? 22.757  93.310  89.653  1.00 33.65  ?  24  ALA A CB    1 
ATOM   85   N  N     . ARG A 1 24  ? 22.076  96.500  89.817  1.00 34.36  ?  25  ARG A N     1 
ATOM   86   C  CA    . ARG A 1 24  ? 21.174  97.597  90.189  1.00 35.48  ?  25  ARG A CA    1 
ATOM   87   C  C     . ARG A 1 24  ? 20.799  98.426  88.952  1.00 35.92  ?  25  ARG A C     1 
ATOM   88   O  O     . ARG A 1 24  ? 19.640  98.813  88.814  1.00 36.29  ?  25  ARG A O     1 
ATOM   89   C  CB    . ARG A 1 24  ? 21.781  98.492  91.286  1.00 37.97  ?  25  ARG A CB    1 
ATOM   90   C  CG    . ARG A 1 24  ? 21.804  97.825  92.659  1.00 42.78  ?  25  ARG A CG    1 
ATOM   91   C  CD    . ARG A 1 24  ? 22.285  98.739  93.782  1.00 47.34  ?  25  ARG A CD    1 
ATOM   92   N  NE    . ARG A 1 24  ? 23.322  98.085  94.589  1.00 51.02  ?  25  ARG A NE    1 
ATOM   93   C  CZ    . ARG A 1 24  ? 24.605  98.445  94.599  1.00 53.00  ?  25  ARG A CZ    1 
ATOM   94   N  NH1   . ARG A 1 24  ? 25.013  99.495  93.895  1.00 52.21  1  25  ARG A NH1   1 
ATOM   95   N  NH2   . ARG A 1 24  ? 25.482  97.777  95.339  1.00 52.73  ?  25  ARG A NH2   1 
ATOM   96   N  N     . LYS A 1 25  ? 21.760  98.630  88.020  1.00 35.60  ?  26  LYS A N     1 
ATOM   97   C  CA    . LYS A 1 25  ? 21.533  99.354  86.770  1.00 35.92  ?  26  LYS A CA    1 
ATOM   98   C  C     . LYS A 1 25  ? 20.415  98.728  85.914  1.00 36.71  ?  26  LYS A C     1 
ATOM   99   O  O     . LYS A 1 25  ? 19.545  99.455  85.442  1.00 36.59  ?  26  LYS A O     1 
ATOM   100  C  CB    . LYS A 1 25  ? 22.833  99.460  85.967  1.00 36.60  ?  26  LYS A CB    1 
ATOM   101  C  CG    . LYS A 1 25  ? 23.838  100.408 86.589  1.00 39.05  ?  26  LYS A CG    1 
ATOM   102  C  CD    . LYS A 1 25  ? 25.066  100.521 85.744  1.00 42.89  ?  26  LYS A CD    1 
ATOM   103  C  CE    . LYS A 1 25  ? 26.163  101.269 86.454  1.00 47.52  ?  26  LYS A CE    1 
ATOM   104  N  NZ    . LYS A 1 25  ? 25.729  102.624 86.876  1.00 50.78  1  26  LYS A NZ    1 
ATOM   105  N  N     . ILE A 1 26  ? 20.426  97.382  85.745  1.00 37.08  ?  27  ILE A N     1 
ATOM   106  C  CA    . ILE A 1 26  ? 19.423  96.636  84.978  1.00 38.03  ?  27  ILE A CA    1 
ATOM   107  C  C     . ILE A 1 26  ? 18.040  96.716  85.649  1.00 40.37  ?  27  ILE A C     1 
ATOM   108  O  O     . ILE A 1 26  ? 17.020  96.755  84.955  1.00 40.55  ?  27  ILE A O     1 
ATOM   109  C  CB    . ILE A 1 26  ? 19.876  95.159  84.768  1.00 37.49  ?  27  ILE A CB    1 
ATOM   110  C  CG1   . ILE A 1 26  ? 21.252  95.062  84.055  1.00 37.87  ?  27  ILE A CG1   1 
ATOM   111  C  CG2   . ILE A 1 26  ? 18.809  94.326  84.054  1.00 37.50  ?  27  ILE A CG2   1 
ATOM   112  C  CD1   . ILE A 1 26  ? 21.266  95.437  82.594  1.00 38.51  ?  27  ILE A CD1   1 
ATOM   113  N  N     . ARG A 1 27  ? 18.008  96.753  86.997  1.00 41.90  ?  28  ARG A N     1 
ATOM   114  C  CA    . ARG A 1 27  ? 16.764  96.842  87.754  1.00 44.20  ?  28  ARG A CA    1 
ATOM   115  C  C     . ARG A 1 27  ? 16.054  98.174  87.485  1.00 46.03  ?  28  ARG A C     1 
ATOM   116  O  O     . ARG A 1 27  ? 14.849  98.203  87.231  1.00 45.88  ?  28  ARG A O     1 
ATOM   117  C  CB    . ARG A 1 27  ? 17.027  96.677  89.259  1.00 46.59  ?  28  ARG A CB    1 
ATOM   118  C  CG    . ARG A 1 27  ? 17.327  95.245  89.675  1.00 52.16  ?  28  ARG A CG    1 
ATOM   119  C  CD    . ARG A 1 27  ? 16.803  94.942  91.069  1.00 57.53  ?  28  ARG A CD    1 
ATOM   120  N  NE    . ARG A 1 27  ? 17.877  94.720  92.041  1.00 61.99  ?  28  ARG A NE    1 
ATOM   121  C  CZ    . ARG A 1 27  ? 18.436  95.678  92.777  1.00 64.98  ?  28  ARG A CZ    1 
ATOM   122  N  NH1   . ARG A 1 27  ? 18.041  96.940  92.649  1.00 64.61  1  28  ARG A NH1   1 
ATOM   123  N  NH2   . ARG A 1 27  ? 19.399  95.382  93.641  1.00 65.33  ?  28  ARG A NH2   1 
ATOM   124  N  N     . HIS A 1 28  ? 16.823  99.269  87.486  1.00 47.37  ?  29  HIS A N     1 
ATOM   125  C  CA    . HIS A 1 28  ? 16.281  100.602 87.254  1.00 49.06  ?  29  HIS A CA    1 
ATOM   126  C  C     . HIS A 1 28  ? 16.057  100.954 85.760  1.00 49.51  ?  29  HIS A C     1 
ATOM   127  O  O     . HIS A 1 28  ? 15.533  102.026 85.463  1.00 50.34  ?  29  HIS A O     1 
ATOM   128  C  CB    . HIS A 1 28  ? 17.143  101.646 87.969  1.00 50.81  ?  29  HIS A CB    1 
ATOM   129  C  CG    . HIS A 1 28  ? 17.261  101.355 89.434  1.00 54.33  ?  29  HIS A CG    1 
ATOM   130  N  ND1   . HIS A 1 28  ? 16.136  101.237 90.236  1.00 56.56  ?  29  HIS A ND1   1 
ATOM   131  C  CD2   . HIS A 1 28  ? 18.362  101.111 90.186  1.00 55.81  ?  29  HIS A CD2   1 
ATOM   132  C  CE1   . HIS A 1 28  ? 16.587  100.934 91.445  1.00 57.28  ?  29  HIS A CE1   1 
ATOM   133  N  NE2   . HIS A 1 28  ? 17.921  100.844 91.463  1.00 57.05  ?  29  HIS A NE2   1 
ATOM   134  N  N     . GLY A 1 29  ? 16.391  100.037 84.855  1.00 48.88  ?  30  GLY A N     1 
ATOM   135  C  CA    . GLY A 1 29  ? 16.168  100.198 83.424  1.00 48.82  ?  30  GLY A CA    1 
ATOM   136  C  C     . GLY A 1 29  ? 17.157  101.058 82.663  1.00 48.67  ?  30  GLY A C     1 
ATOM   137  O  O     . GLY A 1 29  ? 16.756  102.052 82.042  1.00 49.90  ?  30  GLY A O     1 
ATOM   138  N  N     . CYS A 1 30  ? 18.448  100.675 82.670  1.00 46.69  ?  31  CYS A N     1 
ATOM   139  C  CA    . CYS A 1 30  ? 19.478  101.394 81.917  1.00 45.74  ?  31  CYS A CA    1 
ATOM   140  C  C     . CYS A 1 30  ? 19.387  101.061 80.414  1.00 44.03  ?  31  CYS A C     1 
ATOM   141  O  O     . CYS A 1 30  ? 18.704  100.116 80.011  1.00 43.99  ?  31  CYS A O     1 
ATOM   142  C  CB    . CYS A 1 30  ? 20.873  101.103 82.469  1.00 46.72  ?  31  CYS A CB    1 
ATOM   143  S  SG    . CYS A 1 30  ? 21.380  99.365  82.325  1.00 50.84  ?  31  CYS A SG    1 
ATOM   144  N  N     . GLU A 1 31  ? 20.061  101.855 79.582  1.00 42.61  ?  32  GLU A N     1 
ATOM   145  C  CA    . GLU A 1 31  ? 20.065  101.675 78.130  1.00 41.00  ?  32  GLU A CA    1 
ATOM   146  C  C     . GLU A 1 31  ? 21.460  101.982 77.561  1.00 38.73  ?  32  GLU A C     1 
ATOM   147  O  O     . GLU A 1 31  ? 22.335  102.440 78.284  1.00 38.52  ?  32  GLU A O     1 
ATOM   148  C  CB    . GLU A 1 31  ? 18.999  102.607 77.480  1.00 43.79  ?  32  GLU A CB    1 
ATOM   149  C  CG    . GLU A 1 31  ? 17.559  102.209 77.769  1.00 49.92  ?  32  GLU A CG    1 
ATOM   150  C  CD    . GLU A 1 31  ? 16.504  102.684 76.785  1.00 58.40  ?  32  GLU A CD    1 
ATOM   151  O  OE1   . GLU A 1 31  ? 16.442  103.907 76.511  1.00 59.98  ?  32  GLU A OE1   1 
ATOM   152  O  OE2   . GLU A 1 31  ? 15.724  101.828 76.304  1.00 60.53  -1 32  GLU A OE2   1 
ATOM   153  N  N     . GLY A 1 32  ? 21.647  101.705 76.278  1.00 37.44  ?  33  GLY A N     1 
ATOM   154  C  CA    . GLY A 1 32  ? 22.840  102.030 75.507  1.00 36.74  ?  33  GLY A CA    1 
ATOM   155  C  C     . GLY A 1 32  ? 24.155  101.419 75.920  1.00 35.65  ?  33  GLY A C     1 
ATOM   156  O  O     . GLY A 1 32  ? 24.253  100.215 76.149  1.00 35.73  ?  33  GLY A O     1 
ATOM   157  N  N     . ALA A 1 33  ? 25.189  102.249 75.955  1.00 34.90  ?  34  ALA A N     1 
ATOM   158  C  CA    . ALA A 1 33  ? 26.518  101.803 76.346  1.00 34.67  ?  34  ALA A CA    1 
ATOM   159  C  C     . ALA A 1 33  ? 26.544  101.374 77.811  1.00 34.72  ?  34  ALA A C     1 
ATOM   160  O  O     . ALA A 1 33  ? 27.304  100.476 78.164  1.00 34.98  ?  34  ALA A O     1 
ATOM   161  C  CB    . ALA A 1 33  ? 27.536  102.904 76.098  1.00 34.56  ?  34  ALA A CB    1 
ATOM   162  N  N     . GLU A 1 34  ? 25.728  102.021 78.658  1.00 34.33  ?  35  GLU A N     1 
ATOM   163  C  CA    . GLU A 1 34  ? 25.602  101.715 80.069  1.00 34.47  ?  35  GLU A CA    1 
ATOM   164  C  C     . GLU A 1 34  ? 25.047  100.291 80.238  1.00 33.72  ?  35  GLU A C     1 
ATOM   165  O  O     . GLU A 1 34  ? 25.601  99.516  81.026  1.00 33.75  ?  35  GLU A O     1 
ATOM   166  C  CB    . GLU A 1 34  ? 24.679  102.741 80.734  1.00 37.56  ?  35  GLU A CB    1 
ATOM   167  C  CG    . GLU A 1 34  ? 24.619  102.626 82.242  1.00 43.56  ?  35  GLU A CG    1 
ATOM   168  C  CD    . GLU A 1 34  ? 23.730  103.659 82.905  1.00 52.07  ?  35  GLU A CD    1 
ATOM   169  O  OE1   . GLU A 1 34  ? 22.849  104.225 82.213  1.00 53.84  ?  35  GLU A OE1   1 
ATOM   170  O  OE2   . GLU A 1 34  ? 23.917  103.904 84.120  1.00 54.52  -1 35  GLU A OE2   1 
ATOM   171  N  N     . ARG A 1 35  ? 24.004  99.933  79.462  1.00 32.60  ?  36  ARG A N     1 
ATOM   172  C  CA    . ARG A 1 35  ? 23.419  98.597  79.492  1.00 32.44  ?  36  ARG A CA    1 
ATOM   173  C  C     . ARG A 1 35  ? 24.404  97.533  79.027  1.00 32.88  ?  36  ARG A C     1 
ATOM   174  O  O     . ARG A 1 35  ? 24.465  96.465  79.620  1.00 32.79  ?  36  ARG A O     1 
ATOM   175  C  CB    . ARG A 1 35  ? 22.100  98.531  78.686  1.00 33.21  ?  36  ARG A CB    1 
ATOM   176  C  CG    . ARG A 1 35  ? 21.512  97.114  78.561  1.00 35.55  ?  36  ARG A CG    1 
ATOM   177  C  CD    . ARG A 1 35  ? 20.099  97.079  78.032  1.00 38.37  ?  36  ARG A CD    1 
ATOM   178  N  NE    . ARG A 1 35  ? 19.151  96.985  79.140  1.00 42.01  ?  36  ARG A NE    1 
ATOM   179  C  CZ    . ARG A 1 35  ? 18.509  95.876  79.490  1.00 43.73  ?  36  ARG A CZ    1 
ATOM   180  N  NH1   . ARG A 1 35  ? 18.661  94.760  78.786  1.00 42.64  1  36  ARG A NH1   1 
ATOM   181  N  NH2   . ARG A 1 35  ? 17.686  95.880  80.527  1.00 44.67  ?  36  ARG A NH2   1 
ATOM   182  N  N     . GLU A 1 36  ? 25.184  97.825  77.986  1.00 33.72  ?  37  GLU A N     1 
ATOM   183  C  CA    . GLU A 1 36  ? 26.148  96.868  77.461  1.00 34.55  ?  37  GLU A CA    1 
ATOM   184  C  C     . GLU A 1 36  ? 27.313  96.608  78.394  1.00 34.01  ?  37  GLU A C     1 
ATOM   185  O  O     . GLU A 1 36  ? 27.886  95.527  78.328  1.00 34.50  ?  37  GLU A O     1 
ATOM   186  C  CB    . GLU A 1 36  ? 26.629  97.248  76.055  1.00 38.32  ?  37  GLU A CB    1 
ATOM   187  C  CG    . GLU A 1 36  ? 25.502  97.289  75.036  1.00 46.14  ?  37  GLU A CG    1 
ATOM   188  C  CD    . GLU A 1 36  ? 24.521  96.126  75.028  1.00 55.92  ?  37  GLU A CD    1 
ATOM   189  O  OE1   . GLU A 1 36  ? 24.967  94.957  75.117  1.00 58.68  ?  37  GLU A OE1   1 
ATOM   190  O  OE2   . GLU A 1 36  ? 23.303  96.388  74.902  1.00 58.22  -1 37  GLU A OE2   1 
ATOM   191  N  N     . GLU A 1 37  ? 27.634  97.543  79.290  1.00 33.24  ?  38  GLU A N     1 
ATOM   192  C  CA    . GLU A 1 37  ? 28.693  97.311  80.268  1.00 32.79  ?  38  GLU A CA    1 
ATOM   193  C  C     . GLU A 1 37  ? 28.134  96.490  81.432  1.00 31.06  ?  38  GLU A C     1 
ATOM   194  O  O     . GLU A 1 37  ? 28.785  95.557  81.879  1.00 30.91  ?  38  GLU A O     1 
ATOM   195  C  CB    . GLU A 1 37  ? 29.323  98.626  80.745  1.00 36.53  ?  38  GLU A CB    1 
ATOM   196  C  CG    . GLU A 1 37  ? 30.598  98.436  81.561  1.00 44.35  ?  38  GLU A CG    1 
ATOM   197  C  CD    . GLU A 1 37  ? 31.656  97.564  80.906  1.00 54.87  ?  38  GLU A CD    1 
ATOM   198  O  OE1   . GLU A 1 37  ? 32.081  96.566  81.537  1.00 56.71  ?  38  GLU A OE1   1 
ATOM   199  O  OE2   . GLU A 1 37  ? 32.034  97.858  79.746  1.00 58.44  -1 38  GLU A OE2   1 
ATOM   200  N  N     . ALA A 1 38  ? 26.914  96.808  81.883  1.00 29.88  ?  39  ALA A N     1 
ATOM   201  C  CA    . ALA A 1 38  ? 26.216  96.102  82.953  1.00 29.40  ?  39  ALA A CA    1 
ATOM   202  C  C     . ALA A 1 38  ? 26.025  94.615  82.610  1.00 29.20  ?  39  ALA A C     1 
ATOM   203  O  O     . ALA A 1 38  ? 26.326  93.761  83.431  1.00 29.19  ?  39  ALA A O     1 
ATOM   204  C  CB    . ALA A 1 38  ? 24.866  96.757  83.218  1.00 29.23  ?  39  ALA A CB    1 
ATOM   205  N  N     . ILE A 1 39  ? 25.593  94.309  81.379  1.00 29.04  ?  40  ILE A N     1 
ATOM   206  C  CA    . ILE A 1 39  ? 25.374  92.951  80.907  1.00 29.04  ?  40  ILE A CA    1 
ATOM   207  C  C     . ILE A 1 39  ? 26.678  92.167  80.764  1.00 29.83  ?  40  ILE A C     1 
ATOM   208  O  O     . ILE A 1 39  ? 26.675  90.963  80.973  1.00 30.25  ?  40  ILE A O     1 
ATOM   209  C  CB    . ILE A 1 39  ? 24.536  92.998  79.608  1.00 29.18  ?  40  ILE A CB    1 
ATOM   210  C  CG1   . ILE A 1 39  ? 23.089  93.432  79.950  1.00 30.11  ?  40  ILE A CG1   1 
ATOM   211  C  CG2   . ILE A 1 39  ? 24.587  91.667  78.839  1.00 29.15  ?  40  ILE A CG2   1 
ATOM   212  C  CD1   . ILE A 1 39  ? 22.086  93.455  78.791  1.00 31.57  ?  40  ILE A CD1   1 
ATOM   213  N  N     . LYS A 1 40  ? 27.789  92.844  80.457  1.00 30.05  ?  41  LYS A N     1 
ATOM   214  C  CA    . LYS A 1 40  ? 29.104  92.237  80.285  1.00 30.63  ?  41  LYS A CA    1 
ATOM   215  C  C     . LYS A 1 40  ? 29.677  91.784  81.640  1.00 30.73  ?  41  LYS A C     1 
ATOM   216  O  O     . LYS A 1 40  ? 30.304  90.726  81.730  1.00 31.50  ?  41  LYS A O     1 
ATOM   217  C  CB    . LYS A 1 40  ? 30.030  93.259  79.617  1.00 33.52  ?  41  LYS A CB    1 
ATOM   218  C  CG    . LYS A 1 40  ? 31.276  92.688  78.962  1.00 39.56  ?  41  LYS A CG    1 
ATOM   219  C  CD    . LYS A 1 40  ? 32.088  93.807  78.288  1.00 45.82  ?  41  LYS A CD    1 
ATOM   220  C  CE    . LYS A 1 40  ? 33.374  93.315  77.654  1.00 51.26  ?  41  LYS A CE    1 
ATOM   221  N  NZ    . LYS A 1 40  ? 33.128  92.423  76.481  1.00 53.78  1  41  LYS A NZ    1 
ATOM   222  N  N     . MET A 1 41  ? 29.463  92.587  82.689  1.00 29.61  ?  42  MET A N     1 
ATOM   223  C  CA    . MET A 1 41  ? 29.881  92.273  84.057  1.00 28.84  ?  42  MET A CA    1 
ATOM   224  C  C     . MET A 1 41  ? 29.024  91.143  84.617  1.00 27.21  ?  42  MET A C     1 
ATOM   225  O  O     . MET A 1 41  ? 29.518  90.336  85.392  1.00 27.09  ?  42  MET A O     1 
ATOM   226  C  CB    . MET A 1 41  ? 29.730  93.504  84.970  1.00 30.01  ?  42  MET A CB    1 
ATOM   227  C  CG    . MET A 1 41  ? 30.578  94.684  84.534  1.00 34.03  ?  42  MET A CG    1 
ATOM   228  S  SD    . MET A 1 41  ? 30.632  96.030  85.754  1.00 41.88  ?  42  MET A SD    1 
ATOM   229  C  CE    . MET A 1 41  ? 31.854  97.116  84.991  1.00 39.31  ?  42  MET A CE    1 
ATOM   230  N  N     . ILE A 1 42  ? 27.723  91.115  84.273  1.00 26.01  ?  43  ILE A N     1 
ATOM   231  C  CA    . ILE A 1 42  ? 26.820  90.074  84.740  1.00 24.94  ?  43  ILE A CA    1 
ATOM   232  C  C     . ILE A 1 42  ? 27.094  88.744  84.040  1.00 24.03  ?  43  ILE A C     1 
ATOM   233  O  O     . ILE A 1 42  ? 26.947  87.696  84.658  1.00 23.72  ?  43  ILE A O     1 
ATOM   234  C  CB    . ILE A 1 42  ? 25.367  90.552  84.639  1.00 25.05  ?  43  ILE A CB    1 
ATOM   235  C  CG1   . ILE A 1 42  ? 25.121  91.674  85.667  1.00 25.99  ?  43  ILE A CG1   1 
ATOM   236  C  CG2   . ILE A 1 42  ? 24.374  89.410  84.819  1.00 25.16  ?  43  ILE A CG2   1 
ATOM   237  C  CD1   . ILE A 1 42  ? 23.892  92.517  85.369  1.00 27.46  ?  43  ILE A CD1   1 
ATOM   238  N  N     . GLN A 1 43  ? 27.538  88.783  82.782  1.00 23.70  ?  44  GLN A N     1 
ATOM   239  C  CA    . GLN A 1 43  ? 27.911  87.589  82.034  1.00 24.21  ?  44  GLN A CA    1 
ATOM   240  C  C     . GLN A 1 43  ? 29.189  86.986  82.646  1.00 23.95  ?  44  GLN A C     1 
ATOM   241  O  O     . GLN A 1 43  ? 29.278  85.760  82.794  1.00 24.48  ?  44  GLN A O     1 
ATOM   242  C  CB    . GLN A 1 43  ? 28.075  87.901  80.526  1.00 26.59  ?  44  GLN A CB    1 
ATOM   243  C  CG    . GLN A 1 43  ? 28.657  86.755  79.682  1.00 31.42  ?  44  GLN A CG    1 
ATOM   244  C  CD    . GLN A 1 43  ? 27.692  85.608  79.426  1.00 37.76  ?  44  GLN A CD    1 
ATOM   245  O  OE1   . GLN A 1 43  ? 27.327  85.307  78.284  1.00 40.99  ?  44  GLN A OE1   1 
ATOM   246  N  NE2   . GLN A 1 43  ? 27.268  84.918  80.464  1.00 37.82  ?  44  GLN A NE2   1 
ATOM   247  N  N     . ASN A 1 44  ? 30.136  87.847  83.066  1.00 22.64  ?  45  ASN A N     1 
ATOM   248  C  CA    . ASN A 1 44  ? 31.354  87.448  83.751  1.00 21.87  ?  45  ASN A CA    1 
ATOM   249  C  C     . ASN A 1 44  ? 31.012  86.704  85.058  1.00 20.78  ?  45  ASN A C     1 
ATOM   250  O  O     . ASN A 1 44  ? 31.624  85.674  85.362  1.00 21.54  ?  45  ASN A O     1 
ATOM   251  C  CB    . ASN A 1 44  ? 32.175  88.698  84.074  1.00 23.71  ?  45  ASN A CB    1 
ATOM   252  C  CG    . ASN A 1 44  ? 33.576  88.424  84.577  1.00 27.18  ?  45  ASN A CG    1 
ATOM   253  O  OD1   . ASN A 1 44  ? 33.856  88.421  85.791  1.00 28.39  ?  45  ASN A OD1   1 
ATOM   254  N  ND2   . ASN A 1 44  ? 34.484  88.197  83.647  1.00 27.81  ?  45  ASN A ND2   1 
ATOM   255  N  N     . PHE A 1 45  ? 30.056  87.237  85.835  1.00 18.85  ?  46  PHE A N     1 
ATOM   256  C  CA    . PHE A 1 45  ? 29.593  86.659  87.090  1.00 17.81  ?  46  PHE A CA    1 
ATOM   257  C  C     . PHE A 1 45  ? 28.922  85.300  86.841  1.00 17.72  ?  46  PHE A C     1 
ATOM   258  O  O     . PHE A 1 45  ? 29.154  84.350  87.584  1.00 17.75  ?  46  PHE A O     1 
ATOM   259  C  CB    . PHE A 1 45  ? 28.611  87.605  87.750  1.00 17.11  ?  46  PHE A CB    1 
ATOM   260  C  CG    . PHE A 1 45  ? 28.143  87.151  89.109  1.00 17.03  ?  46  PHE A CG    1 
ATOM   261  C  CD1   . PHE A 1 45  ? 29.048  86.952  90.140  1.00 16.95  ?  46  PHE A CD1   1 
ATOM   262  C  CD2   . PHE A 1 45  ? 26.794  86.945  89.364  1.00 17.01  ?  46  PHE A CD2   1 
ATOM   263  C  CE1   . PHE A 1 45  ? 28.612  86.567  91.400  1.00 17.14  ?  46  PHE A CE1   1 
ATOM   264  C  CE2   . PHE A 1 45  ? 26.362  86.558  90.625  1.00 17.18  ?  46  PHE A CE2   1 
ATOM   265  C  CZ    . PHE A 1 45  ? 27.274  86.364  91.630  1.00 16.98  ?  46  PHE A CZ    1 
ATOM   266  N  N     . ARG A 1 46  ? 28.135  85.202  85.767  1.00 17.12  ?  47  ARG A N     1 
ATOM   267  C  CA    . ARG A 1 46  ? 27.477  83.976  85.345  1.00 17.17  ?  47  ARG A CA    1 
ATOM   268  C  C     . ARG A 1 46  ? 28.512  82.876  85.029  1.00 18.71  ?  47  ARG A C     1 
ATOM   269  O  O     . ARG A 1 46  ? 28.350  81.730  85.451  1.00 18.78  ?  47  ARG A O     1 
ATOM   270  C  CB    . ARG A 1 46  ? 26.599  84.274  84.126  1.00 16.82  ?  47  ARG A CB    1 
ATOM   271  C  CG    . ARG A 1 46  ? 25.919  83.060  83.578  1.00 18.40  ?  47  ARG A CG    1 
ATOM   272  C  CD    . ARG A 1 46  ? 25.123  83.352  82.330  1.00 19.54  ?  47  ARG A CD    1 
ATOM   273  N  NE    . ARG A 1 46  ? 24.739  82.096  81.696  1.00 20.05  ?  47  ARG A NE    1 
ATOM   274  C  CZ    . ARG A 1 46  ? 25.435  81.484  80.751  1.00 22.18  ?  47  ARG A CZ    1 
ATOM   275  N  NH1   . ARG A 1 46  ? 26.558  82.022  80.290  1.00 21.70  1  47  ARG A NH1   1 
ATOM   276  N  NH2   . ARG A 1 46  ? 25.016  80.328  80.258  1.00 22.56  ?  47  ARG A NH2   1 
ATOM   277  N  N     . GLU A 1 47  ? 29.595  83.239  84.320  1.00 19.63  ?  48  GLU A N     1 
ATOM   278  C  CA    . GLU A 1 47  ? 30.671  82.312  83.969  1.00 20.62  ?  48  GLU A CA    1 
ATOM   279  C  C     . GLU A 1 47  ? 31.456  81.808  85.196  1.00 20.25  ?  48  GLU A C     1 
ATOM   280  O  O     . GLU A 1 47  ? 31.968  80.689  85.173  1.00 21.29  ?  48  GLU A O     1 
ATOM   281  C  CB    . GLU A 1 47  ? 31.617  82.955  82.954  1.00 24.55  ?  48  GLU A CB    1 
ATOM   282  C  CG    . GLU A 1 47  ? 30.944  83.211  81.625  1.00 32.31  ?  48  GLU A CG    1 
ATOM   283  C  CD    . GLU A 1 47  ? 31.749  84.072  80.670  1.00 42.90  ?  48  GLU A CD    1 
ATOM   284  O  OE1   . GLU A 1 47  ? 32.585  84.881  81.141  1.00 43.69  ?  48  GLU A OE1   1 
ATOM   285  O  OE2   . GLU A 1 47  ? 31.527  83.945  79.443  1.00 47.52  -1 48  GLU A OE2   1 
ATOM   286  N  N     . LEU A 1 48  ? 31.523  82.600  86.266  1.00 18.72  ?  49  LEU A N     1 
ATOM   287  C  CA    . LEU A 1 48  ? 32.179  82.182  87.505  1.00 18.34  ?  49  LEU A CA    1 
ATOM   288  C  C     . LEU A 1 48  ? 31.481  80.950  88.146  1.00 18.29  ?  49  LEU A C     1 
ATOM   289  O  O     . LEU A 1 48  ? 32.109  80.214  88.896  1.00 19.20  ?  49  LEU A O     1 
ATOM   290  C  CB    . LEU A 1 48  ? 32.221  83.345  88.506  1.00 18.47  ?  49  LEU A CB    1 
ATOM   291  C  CG    . LEU A 1 48  ? 33.189  83.154  89.672  1.00 20.27  ?  49  LEU A CG    1 
ATOM   292  C  CD1   . LEU A 1 48  ? 34.655  83.109  89.186  1.00 20.39  ?  49  LEU A CD1   1 
ATOM   293  C  CD2   . LEU A 1 48  ? 32.941  84.170  90.784  1.00 20.75  ?  49  LEU A CD2   1 
ATOM   294  N  N     . HIS A 1 49  ? 30.198  80.716  87.834  1.00 16.83  ?  50  HIS A N     1 
ATOM   295  C  CA    . HIS A 1 49  ? 29.456  79.576  88.356  1.00 15.54  ?  50  HIS A CA    1 
ATOM   296  C  C     . HIS A 1 49  ? 29.685  78.264  87.612  1.00 14.81  ?  50  HIS A C     1 
ATOM   297  O  O     . HIS A 1 49  ? 29.247  77.227  88.092  1.00 14.39  ?  50  HIS A O     1 
ATOM   298  C  CB    . HIS A 1 49  ? 27.971  79.918  88.394  1.00 14.88  ?  50  HIS A CB    1 
ATOM   299  C  CG    . HIS A 1 49  ? 27.705  81.007  89.363  1.00 16.12  ?  50  HIS A CG    1 
ATOM   300  N  ND1   . HIS A 1 49  ? 28.161  82.288  89.135  1.00 18.63  ?  50  HIS A ND1   1 
ATOM   301  C  CD2   . HIS A 1 49  ? 27.137  80.952  90.588  1.00 17.64  ?  50  HIS A CD2   1 
ATOM   302  C  CE1   . HIS A 1 49  ? 27.832  82.988  90.208  1.00 19.90  ?  50  HIS A CE1   1 
ATOM   303  N  NE2   . HIS A 1 49  ? 27.185  82.234  91.102  1.00 19.95  ?  50  HIS A NE2   1 
ATOM   304  N  N     . LEU A 1 50  ? 30.370  78.294  86.463  1.00 14.75  ?  51  LEU A N     1 
ATOM   305  C  CA    . LEU A 1 50  ? 30.584  77.091  85.670  1.00 15.33  ?  51  LEU A CA    1 
ATOM   306  C  C     . LEU A 1 50  ? 31.395  76.003  86.369  1.00 15.30  ?  51  LEU A C     1 
ATOM   307  O  O     . LEU A 1 50  ? 30.898  74.882  86.460  1.00 15.53  ?  51  LEU A O     1 
ATOM   308  C  CB    . LEU A 1 50  ? 31.179  77.397  84.297  1.00 16.12  ?  51  LEU A CB    1 
ATOM   309  C  CG    . LEU A 1 50  ? 31.241  76.173  83.373  1.00 18.73  ?  51  LEU A CG    1 
ATOM   310  C  CD1   . LEU A 1 50  ? 29.837  75.551  83.161  1.00 19.13  ?  51  LEU A CD1   1 
ATOM   311  C  CD2   . LEU A 1 50  ? 31.918  76.510  82.077  1.00 19.73  ?  51  LEU A CD2   1 
ATOM   312  N  N     . TYR A 1 51  ? 32.627  76.309  86.841  1.00 14.64  ?  52  TYR A N     1 
ATOM   313  C  CA    . TYR A 1 51  ? 33.438  75.321  87.556  1.00 14.03  ?  52  TYR A CA    1 
ATOM   314  C  C     . TYR A 1 51  ? 32.695  74.758  88.802  1.00 14.31  ?  52  TYR A C     1 
ATOM   315  O  O     . TYR A 1 51  ? 32.554  73.540  88.920  1.00 14.88  ?  52  TYR A O     1 
ATOM   316  C  CB    . TYR A 1 51  ? 34.836  75.885  87.923  1.00 13.01  ?  52  TYR A CB    1 
ATOM   317  C  CG    . TYR A 1 51  ? 35.613  74.915  88.780  1.00 12.57  ?  52  TYR A CG    1 
ATOM   318  C  CD1   . TYR A 1 51  ? 35.802  73.602  88.376  1.00 13.05  ?  52  TYR A CD1   1 
ATOM   319  C  CD2   . TYR A 1 51  ? 36.091  75.285  90.029  1.00 12.54  ?  52  TYR A CD2   1 
ATOM   320  C  CE1   . TYR A 1 51  ? 36.439  72.684  89.189  1.00 13.41  ?  52  TYR A CE1   1 
ATOM   321  C  CE2   . TYR A 1 51  ? 36.769  74.381  90.833  1.00 12.86  ?  52  TYR A CE2   1 
ATOM   322  C  CZ    . TYR A 1 51  ? 36.912  73.071  90.418  1.00 13.93  ?  52  TYR A CZ    1 
ATOM   323  O  OH    . TYR A 1 51  ? 37.579  72.124  91.150  1.00 15.69  ?  52  TYR A OH    1 
ATOM   324  N  N     . PRO A 1 52  ? 32.189  75.612  89.725  1.00 14.00  ?  53  PRO A N     1 
ATOM   325  C  CA    . PRO A 1 52  ? 31.462  75.091  90.886  1.00 13.23  ?  53  PRO A CA    1 
ATOM   326  C  C     . PRO A 1 52  ? 30.209  74.310  90.522  1.00 12.71  ?  53  PRO A C     1 
ATOM   327  O  O     . PRO A 1 52  ? 29.885  73.366  91.229  1.00 13.09  ?  53  PRO A O     1 
ATOM   328  C  CB    . PRO A 1 52  ? 31.120  76.354  91.672  1.00 13.89  ?  53  PRO A CB    1 
ATOM   329  C  CG    . PRO A 1 52  ? 32.091  77.346  91.221  1.00 14.71  ?  53  PRO A CG    1 
ATOM   330  C  CD    . PRO A 1 52  ? 32.255  77.084  89.782  1.00 13.38  ?  53  PRO A CD    1 
ATOM   331  N  N     . LEU A 1 53  ? 29.516  74.663  89.417  1.00 11.88  ?  54  LEU A N     1 
ATOM   332  C  CA    . LEU A 1 53  ? 28.352  73.902  88.972  1.00 11.55  ?  54  LEU A CA    1 
ATOM   333  C  C     . LEU A 1 53  ? 28.757  72.488  88.606  1.00 10.66  ?  54  LEU A C     1 
ATOM   334  O  O     . LEU A 1 53  ? 28.103  71.551  89.005  1.00 10.22  ?  54  LEU A O     1 
ATOM   335  C  CB    . LEU A 1 53  ? 27.693  74.582  87.749  1.00 12.34  ?  54  LEU A CB    1 
ATOM   336  C  CG    . LEU A 1 53  ? 26.585  73.809  87.063  1.00 13.39  ?  54  LEU A CG    1 
ATOM   337  C  CD1   . LEU A 1 53  ? 25.451  73.639  87.969  1.00 14.20  ?  54  LEU A CD1   1 
ATOM   338  C  CD2   . LEU A 1 53  ? 26.169  74.467  85.789  1.00 13.90  ?  54  LEU A CD2   1 
ATOM   339  N  N     . MET A 1 54  ? 29.823  72.338  87.818  1.00 10.99  ?  55  MET A N     1 
ATOM   340  C  CA    . MET A 1 54  ? 30.286  71.025  87.379  1.00 11.66  ?  55  MET A CA    1 
ATOM   341  C  C     . MET A 1 54  ? 30.911  70.209  88.518  1.00 11.40  ?  55  MET A C     1 
ATOM   342  O  O     . MET A 1 54  ? 30.848  68.988  88.520  1.00 11.71  ?  55  MET A O     1 
ATOM   343  C  CB    . MET A 1 54  ? 31.277  71.208  86.227  1.00 13.78  ?  55  MET A CB    1 
ATOM   344  C  CG    . MET A 1 54  ? 30.682  71.935  85.042  1.00 17.81  ?  55  MET A CG    1 
ATOM   345  S  SD    . MET A 1 54  ? 29.203  71.150  84.342  1.00 28.37  ?  55  MET A SD    1 
ATOM   346  C  CE    . MET A 1 54  ? 29.980  70.083  83.080  1.00 29.58  ?  55  MET A CE    1 
ATOM   347  N  N     . LEU A 1 55  ? 31.499  70.895  89.481  1.00 10.86  ?  56  LEU A N     1 
ATOM   348  C  CA    . LEU A 1 55  ? 32.095  70.288  90.639  1.00 11.03  ?  56  LEU A CA    1 
ATOM   349  C  C     . LEU A 1 55  ? 30.999  69.703  91.530  1.00 12.54  ?  56  LEU A C     1 
ATOM   350  O  O     . LEU A 1 55  ? 31.114  68.549  91.962  1.00 13.12  ?  56  LEU A O     1 
ATOM   351  C  CB    . LEU A 1 55  ? 32.934  71.339  91.365  1.00 9.96   ?  56  LEU A CB    1 
ATOM   352  C  CG    . LEU A 1 55  ? 33.562  70.943  92.666  1.00 10.11  ?  56  LEU A CG    1 
ATOM   353  C  CD1   . LEU A 1 55  ? 34.402  69.675  92.508  1.00 10.75  ?  56  LEU A CD1   1 
ATOM   354  C  CD2   . LEU A 1 55  ? 34.396  72.069  93.196  1.00 10.12  ?  56  LEU A CD2   1 
ATOM   355  N  N     . MET A 1 56  ? 29.915  70.476  91.753  1.00 12.26  ?  57  MET A N     1 
ATOM   356  C  CA    . MET A 1 56  ? 28.775  70.049  92.538  1.00 12.53  ?  57  MET A CA    1 
ATOM   357  C  C     . MET A 1 56  ? 28.018  68.933  91.859  1.00 13.23  ?  57  MET A C     1 
ATOM   358  O  O     . MET A 1 56  ? 27.467  68.075  92.536  1.00 13.90  ?  57  MET A O     1 
ATOM   359  C  CB    . MET A 1 56  ? 27.844  71.238  92.854  1.00 13.55  ?  57  MET A CB    1 
ATOM   360  C  CG    . MET A 1 56  ? 28.403  72.175  93.912  1.00 16.97  ?  57  MET A CG    1 
ATOM   361  S  SD    . MET A 1 56  ? 28.945  71.365  95.474  1.00 26.35  ?  57  MET A SD    1 
ATOM   362  C  CE    . MET A 1 56  ? 27.435  70.615  95.939  1.00 22.44  ?  57  MET A CE    1 
ATOM   363  N  N     . LYS A 1 57  ? 28.004  68.923  90.524  1.00 12.71  ?  58  LYS A N     1 
ATOM   364  C  CA    . LYS A 1 57  ? 27.396  67.884  89.761  1.00 13.03  ?  58  LYS A CA    1 
ATOM   365  C  C     . LYS A 1 57  ? 28.127  66.552  89.960  1.00 12.77  ?  58  LYS A C     1 
ATOM   366  O  O     . LYS A 1 57  ? 27.463  65.541  90.141  1.00 13.25  ?  58  LYS A O     1 
ATOM   367  C  CB    . LYS A 1 57  ? 27.323  68.281  88.293  1.00 16.08  ?  58  LYS A CB    1 
ATOM   368  C  CG    . LYS A 1 57  ? 26.097  67.711  87.650  1.00 21.94  ?  58  LYS A CG    1 
ATOM   369  C  CD    . LYS A 1 57  ? 26.412  66.899  86.445  1.00 29.07  ?  58  LYS A CD    1 
ATOM   370  C  CE    . LYS A 1 57  ? 26.930  65.535  86.764  1.00 35.49  ?  58  LYS A CE    1 
ATOM   371  N  NZ    . LYS A 1 57  ? 28.274  65.351  86.165  1.00 39.75  1  58  LYS A NZ    1 
ATOM   372  N  N     . ASN A 1 58  ? 29.466  66.547  89.968  1.00 12.51  ?  59  ASN A N     1 
ATOM   373  C  CA    . ASN A 1 58  ? 30.231  65.326  90.194  1.00 13.29  ?  59  ASN A CA    1 
ATOM   374  C  C     . ASN A 1 58  ? 30.132  64.880  91.651  1.00 13.72  ?  59  ASN A C     1 
ATOM   375  O  O     . ASN A 1 58  ? 30.104  63.691  91.919  1.00 13.96  ?  59  ASN A O     1 
ATOM   376  C  CB    . ASN A 1 58  ? 31.704  65.505  89.787  1.00 15.19  ?  59  ASN A CB    1 
ATOM   377  C  CG    . ASN A 1 58  ? 31.913  65.600  88.303  1.00 18.78  ?  59  ASN A CG    1 
ATOM   378  O  OD1   . ASN A 1 58  ? 31.195  65.010  87.501  1.00 20.92  ?  59  ASN A OD1   1 
ATOM   379  N  ND2   . ASN A 1 58  ? 32.891  66.356  87.899  1.00 19.54  ?  59  ASN A ND2   1 
ATOM   380  N  N     . HIS A 1 59  ? 30.085  65.831  92.588  1.00 14.08  ?  60  HIS A N     1 
ATOM   381  C  CA    . HIS A 1 59  ? 29.882  65.601  94.017  1.00 14.55  ?  60  HIS A CA    1 
ATOM   382  C  C     . HIS A 1 59  ? 28.535  64.887  94.220  1.00 15.17  ?  60  HIS A C     1 
ATOM   383  O  O     . HIS A 1 59  ? 28.431  63.953  94.997  1.00 15.22  ?  60  HIS A O     1 
ATOM   384  C  CB    . HIS A 1 59  ? 29.867  66.954  94.757  1.00 14.60  ?  60  HIS A CB    1 
ATOM   385  C  CG    . HIS A 1 59  ? 29.607  66.843  96.225  1.00 17.17  ?  60  HIS A CG    1 
ATOM   386  N  ND1   . HIS A 1 59  ? 30.638  66.597  97.128  1.00 19.79  ?  60  HIS A ND1   1 
ATOM   387  C  CD2   . HIS A 1 59  ? 28.445  66.956  96.913  1.00 18.07  ?  60  HIS A CD2   1 
ATOM   388  C  CE1   . HIS A 1 59  ? 30.068  66.546  98.322  1.00 20.09  ?  60  HIS A CE1   1 
ATOM   389  N  NE2   . HIS A 1 59  ? 28.748  66.745  98.243  1.00 19.36  ?  60  HIS A NE2   1 
ATOM   390  N  N     . LEU A 1 60  ? 27.506  65.346  93.523  1.00 15.82  ?  61  LEU A N     1 
ATOM   391  C  CA    . LEU A 1 60  ? 26.160  64.806  93.599  1.00 16.45  ?  61  LEU A CA    1 
ATOM   392  C  C     . LEU A 1 60  ? 26.057  63.421  92.948  1.00 17.40  ?  61  LEU A C     1 
ATOM   393  O  O     . LEU A 1 60  ? 25.387  62.563  93.504  1.00 18.22  ?  61  LEU A O     1 
ATOM   394  C  CB    . LEU A 1 60  ? 25.192  65.804  92.970  1.00 16.41  ?  61  LEU A CB    1 
ATOM   395  C  CG    . LEU A 1 60  ? 23.721  65.445  92.996  1.00 17.89  ?  61  LEU A CG    1 
ATOM   396  C  CD1   . LEU A 1 60  ? 23.212  65.263  94.444  1.00 18.02  ?  61  LEU A CD1   1 
ATOM   397  C  CD2   . LEU A 1 60  ? 22.915  66.458  92.200  1.00 17.79  ?  61  LEU A CD2   1 
ATOM   398  N  N     . ASP A 1 61  ? 26.728  63.194  91.809  1.00 17.29  ?  62  ASP A N     1 
ATOM   399  C  CA    . ASP A 1 61  ? 26.779  61.918  91.095  1.00 18.70  ?  62  ASP A CA    1 
ATOM   400  C  C     . ASP A 1 61  ? 27.535  60.847  91.913  1.00 19.50  ?  62  ASP A C     1 
ATOM   401  O  O     . ASP A 1 61  ? 27.189  59.660  91.878  1.00 19.42  ?  62  ASP A O     1 
ATOM   402  C  CB    . ASP A 1 61  ? 27.527  62.124  89.789  1.00 22.88  ?  62  ASP A CB    1 
ATOM   403  C  CG    . ASP A 1 61  ? 26.897  61.453  88.598  1.00 34.35  ?  62  ASP A CG    1 
ATOM   404  O  OD1   . ASP A 1 61  ? 26.277  60.370  88.781  1.00 37.84  ?  62  ASP A OD1   1 
ATOM   405  O  OD2   . ASP A 1 61  ? 27.010  62.010  87.474  1.00 37.80  -1 62  ASP A OD2   1 
ATOM   406  N  N     . ARG A 1 62  ? 28.597  61.271  92.613  1.00 19.42  ?  63  ARG A N     1 
ATOM   407  C  CA    . ARG A 1 62  ? 29.388  60.393  93.442  1.00 20.35  ?  63  ARG A CA    1 
ATOM   408  C  C     . ARG A 1 62  ? 28.562  59.954  94.658  1.00 20.66  ?  63  ARG A C     1 
ATOM   409  O  O     . ARG A 1 62  ? 28.600  58.779  95.025  1.00 21.62  ?  63  ARG A O     1 
ATOM   410  C  CB    . ARG A 1 62  ? 30.670  61.108  93.887  1.00 22.05  ?  63  ARG A CB    1 
ATOM   411  C  CG    . ARG A 1 62  ? 31.649  60.199  94.601  1.00 25.95  ?  63  ARG A CG    1 
ATOM   412  C  CD    . ARG A 1 62  ? 33.019  60.823  94.619  1.00 30.78  ?  63  ARG A CD    1 
ATOM   413  N  NE    . ARG A 1 62  ? 34.077  59.828  94.809  1.00 34.57  ?  63  ARG A NE    1 
ATOM   414  C  CZ    . ARG A 1 62  ? 35.370  60.117  94.932  1.00 35.39  ?  63  ARG A CZ    1 
ATOM   415  N  NH1   . ARG A 1 62  ? 35.783  61.378  94.888  1.00 32.76  1  63  ARG A NH1   1 
ATOM   416  N  NH2   . ARG A 1 62  ? 36.258  59.145  95.103  1.00 35.99  ?  63  ARG A NH2   1 
ATOM   417  N  N     . ALA A 1 63  ? 27.801  60.888  95.266  1.00 19.49  ?  64  ALA A N     1 
ATOM   418  C  CA    . ALA A 1 63  ? 26.937  60.585  96.409  1.00 19.15  ?  64  ALA A CA    1 
ATOM   419  C  C     . ALA A 1 63  ? 25.688  59.770  95.995  1.00 19.82  ?  64  ALA A C     1 
ATOM   420  O  O     . ALA A 1 63  ? 25.239  58.934  96.777  1.00 19.88  ?  64  ALA A O     1 
ATOM   421  C  CB    . ALA A 1 63  ? 26.531  61.860  97.120  1.00 18.25  ?  64  ALA A CB    1 
ATOM   422  N  N     . ALA A 1 64  ? 25.159  59.971  94.760  1.00 20.01  ?  65  ALA A N     1 
ATOM   423  C  CA    . ALA A 1 64  ? 24.003  59.214  94.270  1.00 21.45  ?  65  ALA A CA    1 
ATOM   424  C  C     . ALA A 1 64  ? 24.384  57.769  93.923  1.00 23.63  ?  65  ALA A C     1 
ATOM   425  O  O     . ALA A 1 64  ? 23.557  56.860  94.067  1.00 23.98  ?  65  ALA A O     1 
ATOM   426  C  CB    . ALA A 1 64  ? 23.395  59.890  93.060  1.00 21.30  ?  65  ALA A CB    1 
ATOM   427  N  N     . LYS A 1 65  ? 25.616  57.558  93.449  1.00 24.81  ?  66  LYS A N     1 
ATOM   428  C  CA    . LYS A 1 65  ? 26.102  56.211  93.175  1.00 27.07  ?  66  LYS A CA    1 
ATOM   429  C  C     . LYS A 1 65  ? 26.331  55.426  94.472  1.00 28.79  ?  66  LYS A C     1 
ATOM   430  O  O     . LYS A 1 65  ? 26.231  54.208  94.461  1.00 29.10  ?  66  LYS A O     1 
ATOM   431  C  CB    . LYS A 1 65  ? 27.344  56.227  92.277  1.00 29.32  ?  66  LYS A CB    1 
ATOM   432  C  CG    . LYS A 1 65  ? 26.976  56.577  90.843  1.00 34.53  ?  66  LYS A CG    1 
ATOM   433  C  CD    . LYS A 1 65  ? 28.173  56.763  89.942  1.00 39.89  ?  66  LYS A CD    1 
ATOM   434  C  CE    . LYS A 1 65  ? 27.693  57.098  88.553  1.00 44.45  ?  66  LYS A CE    1 
ATOM   435  N  NZ    . LYS A 1 65  ? 28.818  57.498  87.670  1.00 47.61  1  66  LYS A NZ    1 
ATOM   436  N  N     . LYS A 1 66  ? 26.569  56.116  95.593  1.00 30.14  ?  67  LYS A N     1 
ATOM   437  C  CA    . LYS A 1 66  ? 26.718  55.467  96.879  1.00 32.72  ?  67  LYS A CA    1 
ATOM   438  C  C     . LYS A 1 66  ? 25.357  55.022  97.409  1.00 35.00  ?  67  LYS A C     1 
ATOM   439  O  O     . LYS A 1 66  ? 25.238  53.862  97.792  1.00 35.81  ?  67  LYS A O     1 
ATOM   440  C  CB    . LYS A 1 66  ? 27.436  56.381  97.881  1.00 34.93  ?  67  LYS A CB    1 
ATOM   441  C  CG    . LYS A 1 66  ? 28.619  55.708  98.537  1.00 40.70  ?  67  LYS A CG    1 
ATOM   442  C  CD    . LYS A 1 66  ? 29.835  56.630  98.636  1.00 46.54  ?  67  LYS A CD    1 
ATOM   443  C  CE    . LYS A 1 66  ? 30.400  56.977  97.276  1.00 50.76  ?  67  LYS A CE    1 
ATOM   444  N  NZ    . LYS A 1 66  ? 31.696  57.708  97.372  1.00 52.95  1  67  LYS A NZ    1 
ATOM   445  N  N     . VAL A 1 67  ? 24.322  55.898  97.379  1.00 36.12  ?  68  VAL A N     1 
ATOM   446  C  CA    . VAL A 1 67  ? 22.984  55.546  97.876  1.00 38.25  ?  68  VAL A CA    1 
ATOM   447  C  C     . VAL A 1 67  ? 22.266  54.528  96.973  1.00 40.88  ?  68  VAL A C     1 
ATOM   448  O  O     . VAL A 1 67  ? 21.457  53.748  97.474  1.00 41.57  ?  68  VAL A O     1 
ATOM   449  C  CB    . VAL A 1 67  ? 22.051  56.751  98.221  1.00 38.48  ?  68  VAL A CB    1 
ATOM   450  C  CG1   . VAL A 1 67  ? 22.830  57.907  98.839  1.00 38.83  ?  68  VAL A CG1   1 
ATOM   451  C  CG2   . VAL A 1 67  ? 21.226  57.216  97.024  1.00 38.43  ?  68  VAL A CG2   1 
ATOM   452  N  N     . ASP A 1 68  ? 22.546  54.529  95.667  1.00 42.19  ?  69  ASP A N     1 
ATOM   453  C  CA    . ASP A 1 68  ? 21.918  53.576  94.754  1.00 44.16  ?  69  ASP A CA    1 
ATOM   454  C  C     . ASP A 1 68  ? 22.995  52.802  93.990  1.00 45.93  ?  69  ASP A C     1 
ATOM   455  O  O     . ASP A 1 68  ? 23.607  53.341  93.057  1.00 46.01  ?  69  ASP A O     1 
ATOM   456  C  CB    . ASP A 1 68  ? 20.958  54.281  93.784  1.00 46.45  ?  69  ASP A CB    1 
ATOM   457  C  CG    . ASP A 1 68  ? 20.183  53.323  92.900  1.00 52.23  ?  69  ASP A CG    1 
ATOM   458  O  OD1   . ASP A 1 68  ? 19.893  52.188  93.360  1.00 53.42  ?  69  ASP A OD1   1 
ATOM   459  O  OD2   . ASP A 1 68  ? 19.867  53.703  91.752  1.00 54.27  -1 69  ASP A OD2   1 
ATOM   460  N  N     . LYS A 1 69  ? 23.236  51.537  94.388  1.00 46.78  ?  70  LYS A N     1 
ATOM   461  C  CA    . LYS A 1 69  ? 24.257  50.719  93.735  1.00 47.83  ?  70  LYS A CA    1 
ATOM   462  C  C     . LYS A 1 69  ? 23.845  50.243  92.319  1.00 48.49  ?  70  LYS A C     1 
ATOM   463  O  O     . LYS A 1 69  ? 24.705  49.829  91.541  1.00 48.74  ?  70  LYS A O     1 
ATOM   464  C  CB    . LYS A 1 69  ? 24.684  49.560  94.642  1.00 49.92  ?  70  LYS A CB    1 
ATOM   465  C  CG    . LYS A 1 69  ? 25.262  50.038  95.976  1.00 53.44  ?  70  LYS A CG    1 
ATOM   466  N  N     . GLU A 1 70  ? 22.544  50.352  91.969  1.00 48.42  ?  71  GLU A N     1 
ATOM   467  C  CA    . GLU A 1 70  ? 22.040  50.044  90.624  1.00 48.53  ?  71  GLU A CA    1 
ATOM   468  C  C     . GLU A 1 70  ? 22.416  51.140  89.601  1.00 47.44  ?  71  GLU A C     1 
ATOM   469  O  O     . GLU A 1 70  ? 22.368  50.888  88.399  1.00 47.84  ?  71  GLU A O     1 
ATOM   470  C  CB    . GLU A 1 70  ? 20.518  49.871  90.640  1.00 51.65  ?  71  GLU A CB    1 
ATOM   471  C  CG    . GLU A 1 70  ? 20.063  48.484  91.053  1.00 58.79  ?  71  GLU A CG    1 
ATOM   472  C  CD    . GLU A 1 70  ? 19.660  48.351  92.509  1.00 67.38  ?  71  GLU A CD    1 
ATOM   473  O  OE1   . GLU A 1 70  ? 20.465  48.733  93.390  1.00 68.65  ?  71  GLU A OE1   1 
ATOM   474  O  OE2   . GLU A 1 70  ? 18.539  47.855  92.768  1.00 70.59  -1 71  GLU A OE2   1 
ATOM   475  N  N     . ASN A 1 71  ? 22.774  52.348  90.081  1.00 45.98  ?  72  ASN A N     1 
ATOM   476  C  CA    . ASN A 1 71  ? 23.157  53.506  89.277  1.00 44.79  ?  72  ASN A CA    1 
ATOM   477  C  C     . ASN A 1 71  ? 21.975  54.046  88.458  1.00 41.42  ?  72  ASN A C     1 
ATOM   478  O  O     . ASN A 1 71  ? 22.159  54.499  87.329  1.00 41.12  ?  72  ASN A O     1 
ATOM   479  C  CB    . ASN A 1 71  ? 24.408  53.233  88.426  1.00 47.87  ?  72  ASN A CB    1 
ATOM   480  C  CG    . ASN A 1 71  ? 25.636  52.903  89.261  1.00 53.91  ?  72  ASN A CG    1 
ATOM   481  O  OD1   . ASN A 1 71  ? 25.578  52.796  90.500  1.00 56.27  ?  72  ASN A OD1   1 
ATOM   482  N  ND2   . ASN A 1 71  ? 26.782  52.730  88.604  1.00 54.94  ?  72  ASN A ND2   1 
ATOM   483  N  N     . LYS A 1 72  ? 20.759  54.025  89.060  1.00 38.56  ?  73  LYS A N     1 
ATOM   484  C  CA    . LYS A 1 72  ? 19.524  54.494  88.415  1.00 36.00  ?  73  LYS A CA    1 
ATOM   485  C  C     . LYS A 1 72  ? 19.162  55.966  88.716  1.00 32.14  ?  73  LYS A C     1 
ATOM   486  O  O     . LYS A 1 72  ? 18.185  56.452  88.150  1.00 32.37  ?  73  LYS A O     1 
ATOM   487  C  CB    . LYS A 1 72  ? 18.330  53.590  88.763  1.00 38.35  ?  73  LYS A CB    1 
ATOM   488  C  CG    . LYS A 1 72  ? 18.576  52.103  88.578  1.00 43.42  ?  73  LYS A CG    1 
ATOM   489  C  CD    . LYS A 1 72  ? 18.732  51.720  87.122  1.00 48.75  ?  73  LYS A CD    1 
ATOM   490  C  CE    . LYS A 1 72  ? 18.806  50.221  86.972  1.00 53.62  ?  73  LYS A CE    1 
ATOM   491  N  NZ    . LYS A 1 72  ? 17.640  49.545  87.609  1.00 56.11  1  73  LYS A NZ    1 
ATOM   492  N  N     . ILE A 1 73  ? 19.909  56.658  89.613  1.00 28.51  ?  74  ILE A N     1 
ATOM   493  C  CA    . ILE A 1 73  ? 19.664  58.072  89.904  1.00 25.35  ?  74  ILE A CA    1 
ATOM   494  C  C     . ILE A 1 73  ? 20.099  58.889  88.690  1.00 23.96  ?  74  ILE A C     1 
ATOM   495  O  O     . ILE A 1 73  ? 21.265  58.827  88.286  1.00 24.19  ?  74  ILE A O     1 
ATOM   496  C  CB    . ILE A 1 73  ? 20.446  58.605  91.140  1.00 24.12  ?  74  ILE A CB    1 
ATOM   497  C  CG1   . ILE A 1 73  ? 20.194  57.783  92.427  1.00 24.47  ?  74  ILE A CG1   1 
ATOM   498  C  CG2   . ILE A 1 73  ? 20.202  60.108  91.375  1.00 23.67  ?  74  ILE A CG2   1 
ATOM   499  C  CD1   . ILE A 1 73  ? 18.967  57.682  92.829  1.00 24.91  ?  74  ILE A CD1   1 
ATOM   500  N  N     . ILE A 1 74  ? 19.187  59.677  88.137  1.00 22.37  ?  75  ILE A N     1 
ATOM   501  C  CA    . ILE A 1 74  ? 19.529  60.555  87.021  1.00 21.45  ?  75  ILE A CA    1 
ATOM   502  C  C     . ILE A 1 74  ? 19.959  61.928  87.546  1.00 19.00  ?  75  ILE A C     1 
ATOM   503  O  O     . ILE A 1 74  ? 19.340  62.472  88.451  1.00 17.32  ?  75  ILE A O     1 
ATOM   504  C  CB    . ILE A 1 74  ? 18.394  60.609  85.983  1.00 22.10  ?  75  ILE A CB    1 
ATOM   505  C  CG1   . ILE A 1 74  ? 18.266  59.252  85.304  1.00 23.06  ?  75  ILE A CG1   1 
ATOM   506  C  CG2   . ILE A 1 74  ? 18.645  61.678  84.955  1.00 22.25  ?  75  ILE A CG2   1 
ATOM   507  C  CD1   . ILE A 1 74  ? 17.097  58.695  85.607  1.00 24.94  ?  75  ILE A CD1   1 
ATOM   508  N  N     . VAL A 1 75  ? 21.095  62.420  87.061  1.00 18.60  ?  76  VAL A N     1 
ATOM   509  C  CA    . VAL A 1 75  ? 21.632  63.698  87.504  1.00 18.15  ?  76  VAL A CA    1 
ATOM   510  C  C     . VAL A 1 75  ? 21.693  64.665  86.312  1.00 17.89  ?  76  VAL A C     1 
ATOM   511  O  O     . VAL A 1 75  ? 22.075  64.273  85.219  1.00 18.82  ?  76  VAL A O     1 
ATOM   512  C  CB    . VAL A 1 75  ? 22.965  63.531  88.296  1.00 17.92  ?  76  VAL A CB    1 
ATOM   513  C  CG1   . VAL A 1 75  ? 23.662  64.864  88.518  1.00 18.62  ?  76  VAL A CG1   1 
ATOM   514  C  CG2   . VAL A 1 75  ? 22.720  62.824  89.636  1.00 17.50  ?  76  VAL A CG2   1 
ATOM   515  N  N     . ALA A 1 76  ? 21.199  65.885  86.505  1.00 16.08  ?  77  ALA A N     1 
ATOM   516  C  CA    . ALA A 1 76  ? 21.162  66.918  85.486  1.00 15.10  ?  77  ALA A CA    1 
ATOM   517  C  C     . ALA A 1 76  ? 21.741  68.214  86.050  1.00 14.67  ?  77  ALA A C     1 
ATOM   518  O  O     . ALA A 1 76  ? 21.722  68.424  87.262  1.00 14.83  ?  77  ALA A O     1 
ATOM   519  C  CB    . ALA A 1 76  ? 19.716  67.167  85.061  1.00 14.77  ?  77  ALA A CB    1 
ATOM   520  N  N     . ARG A 1 77  ? 22.192  69.112  85.174  1.00 14.01  ?  78  ARG A N     1 
ATOM   521  C  CA    . ARG A 1 77  ? 22.704  70.396  85.613  1.00 14.19  ?  78  ARG A CA    1 
ATOM   522  C  C     . ARG A 1 77  ? 22.473  71.466  84.568  1.00 13.65  ?  78  ARG A C     1 
ATOM   523  O  O     . ARG A 1 77  ? 22.265  71.145  83.403  1.00 13.72  ?  78  ARG A O     1 
ATOM   524  C  CB    . ARG A 1 77  ? 24.176  70.304  86.088  1.00 16.13  ?  78  ARG A CB    1 
ATOM   525  C  CG    . ARG A 1 77  ? 25.239  70.742  85.103  1.00 20.75  ?  78  ARG A CG    1 
ATOM   526  C  CD    . ARG A 1 77  ? 25.646  69.638  84.168  1.00 26.35  ?  78  ARG A CD    1 
ATOM   527  N  NE    . ARG A 1 77  ? 26.065  70.205  82.888  1.00 33.33  ?  78  ARG A NE    1 
ATOM   528  C  CZ    . ARG A 1 77  ? 26.549  69.499  81.874  1.00 38.37  ?  78  ARG A CZ    1 
ATOM   529  N  NH1   . ARG A 1 77  ? 26.713  68.185  81.988  1.00 38.91  1  78  ARG A NH1   1 
ATOM   530  N  NH2   . ARG A 1 77  ? 26.903  70.103  80.746  1.00 39.47  ?  78  ARG A NH2   1 
ATOM   531  N  N     . ARG A 1 78  ? 22.487  72.738  84.986  1.00 13.31  ?  79  ARG A N     1 
ATOM   532  C  CA    . ARG A 1 78  ? 22.284  73.804  84.036  1.00 13.57  ?  79  ARG A CA    1 
ATOM   533  C  C     . ARG A 1 78  ? 22.777  75.129  84.572  1.00 14.58  ?  79  ARG A C     1 
ATOM   534  O  O     . ARG A 1 78  ? 22.575  75.477  85.734  1.00 15.36  ?  79  ARG A O     1 
ATOM   535  C  CB    . ARG A 1 78  ? 20.812  73.816  83.531  1.00 13.69  ?  79  ARG A CB    1 
ATOM   536  C  CG    . ARG A 1 78  ? 20.026  75.117  83.596  1.00 16.53  ?  79  ARG A CG    1 
ATOM   537  C  CD    . ARG A 1 78  ? 19.502  75.206  84.966  1.00 17.34  ?  79  ARG A CD    1 
ATOM   538  N  NE    . ARG A 1 78  ? 18.860  76.465  85.335  1.00 17.56  ?  79  ARG A NE    1 
ATOM   539  C  CZ    . ARG A 1 78  ? 19.141  77.132  86.450  1.00 16.29  ?  79  ARG A CZ    1 
ATOM   540  N  NH1   . ARG A 1 78  ? 20.209  76.816  87.172  1.00 11.47  1  79  ARG A NH1   1 
ATOM   541  N  NH2   . ARG A 1 78  ? 18.386  78.147  86.825  1.00 18.04  ?  79  ARG A NH2   1 
ATOM   542  N  N     . LEU A 1 79  ? 23.470  75.843  83.715  1.00 15.04  ?  80  LEU A N     1 
ATOM   543  C  CA    . LEU A 1 79  ? 23.911  77.181  84.021  1.00 15.80  ?  80  LEU A CA    1 
ATOM   544  C  C     . LEU A 1 79  ? 22.759  78.048  83.520  1.00 16.29  ?  80  LEU A C     1 
ATOM   545  O  O     . LEU A 1 79  ? 22.265  77.857  82.410  1.00 16.76  ?  80  LEU A O     1 
ATOM   546  C  CB    . LEU A 1 79  ? 25.265  77.517  83.352  1.00 15.60  ?  80  LEU A CB    1 
ATOM   547  C  CG    . LEU A 1 79  ? 25.891  78.858  83.759  1.00 16.88  ?  80  LEU A CG    1 
ATOM   548  C  CD1   . LEU A 1 79  ? 26.142  78.916  85.238  1.00 17.86  ?  80  LEU A CD1   1 
ATOM   549  C  CD2   . LEU A 1 79  ? 27.198  79.093  83.046  1.00 17.34  ?  80  LEU A CD2   1 
ATOM   550  N  N     . LYS A 1 80  ? 22.267  78.932  84.378  1.00 16.11  ?  81  LYS A N     1 
ATOM   551  C  CA    . LYS A 1 80  ? 21.138  79.788  84.093  1.00 17.02  ?  81  LYS A CA    1 
ATOM   552  C  C     . LYS A 1 80  ? 21.510  80.732  82.972  1.00 18.63  ?  81  LYS A C     1 
ATOM   553  O  O     . LYS A 1 80  ? 22.560  81.326  83.052  1.00 19.08  ?  81  LYS A O     1 
ATOM   554  C  CB    . LYS A 1 80  ? 20.757  80.574  85.356  1.00 18.29  ?  81  LYS A CB    1 
ATOM   555  C  CG    . LYS A 1 80  ? 19.313  81.016  85.389  1.00 20.74  ?  81  LYS A CG    1 
ATOM   556  C  CD    . LYS A 1 80  ? 19.031  81.970  86.534  1.00 22.55  ?  81  LYS A CD    1 
ATOM   557  C  CE    . LYS A 1 80  ? 17.546  82.085  86.783  1.00 23.84  ?  81  LYS A CE    1 
ATOM   558  N  NZ    . LYS A 1 80  ? 16.980  80.767  87.177  1.00 24.73  1  81  LYS A NZ    1 
ATOM   559  N  N     . ARG A 1 81  ? 20.694  80.822  81.917  1.00 19.52  ?  82  ARG A N     1 
ATOM   560  C  CA    . ARG A 1 81  ? 20.935  81.672  80.754  1.00 21.69  ?  82  ARG A CA    1 
ATOM   561  C  C     . ARG A 1 81  ? 21.062  83.158  81.091  1.00 21.35  ?  82  ARG A C     1 
ATOM   562  O  O     . ARG A 1 81  ? 20.405  83.636  82.005  1.00 20.52  ?  82  ARG A O     1 
ATOM   563  C  CB    . ARG A 1 81  ? 19.795  81.473  79.734  1.00 25.95  ?  82  ARG A CB    1 
ATOM   564  C  CG    . ARG A 1 81  ? 20.064  80.349  78.721  1.00 33.21  ?  82  ARG A CG    1 
ATOM   565  C  CD    . ARG A 1 81  ? 18.832  79.536  78.318  1.00 40.15  ?  82  ARG A CD    1 
ATOM   566  N  NE    . ARG A 1 81  ? 17.597  80.326  78.229  1.00 46.86  ?  82  ARG A NE    1 
ATOM   567  C  CZ    . ARG A 1 81  ? 17.050  80.745  77.090  1.00 50.90  ?  82  ARG A CZ    1 
ATOM   568  N  NH1   . ARG A 1 81  ? 17.622  80.460  75.924  1.00 51.48  1  82  ARG A NH1   1 
ATOM   569  N  NH2   . ARG A 1 81  ? 15.925  81.448  77.107  1.00 50.55  ?  82  ARG A NH2   1 
ATOM   570  N  N     . LEU A 1 82  ? 21.882  83.894  80.335  1.00 22.39  ?  83  LEU A N     1 
ATOM   571  C  CA    . LEU A 1 82  ? 22.054  85.327  80.561  1.00 23.48  ?  83  LEU A CA    1 
ATOM   572  C  C     . LEU A 1 82  ? 20.727  86.085  80.392  1.00 24.99  ?  83  LEU A C     1 
ATOM   573  O  O     . LEU A 1 82  ? 20.350  86.847  81.278  1.00 25.29  ?  83  LEU A O     1 
ATOM   574  C  CB    . LEU A 1 82  ? 23.135  85.904  79.655  1.00 23.64  ?  83  LEU A CB    1 
ATOM   575  C  CG    . LEU A 1 82  ? 23.480  87.373  79.913  1.00 25.26  ?  83  LEU A CG    1 
ATOM   576  C  CD1   . LEU A 1 82  ? 23.983  87.598  81.351  1.00 25.13  ?  83  LEU A CD1   1 
ATOM   577  C  CD2   . LEU A 1 82  ? 24.502  87.859  78.914  1.00 26.00  ?  83  LEU A CD2   1 
ATOM   578  N  N     . SER A 1 83  ? 19.976  85.800  79.323  1.00 25.57  ?  84  SER A N     1 
ATOM   579  C  CA    . SER A 1 83  ? 18.679  86.430  79.079  1.00 27.23  ?  84  SER A CA    1 
ATOM   580  C  C     . SER A 1 83  ? 17.668  86.223  80.237  1.00 27.71  ?  84  SER A C     1 
ATOM   581  O  O     . SER A 1 83  ? 16.910  87.145  80.566  1.00 28.21  ?  84  SER A O     1 
ATOM   582  C  CB    . SER A 1 83  ? 18.086  85.912  77.773  1.00 29.47  ?  84  SER A CB    1 
ATOM   583  O  OG    . SER A 1 83  ? 17.656  84.570  77.937  1.00 32.60  ?  84  SER A OG    1 
ATOM   584  N  N     . THR A 1 84  ? 17.660  85.014  80.839  1.00 27.02  ?  85  THR A N     1 
ATOM   585  C  CA    . THR A 1 84  ? 16.805  84.676  81.976  1.00 26.84  ?  85  THR A CA    1 
ATOM   586  C  C     . THR A 1 84  ? 17.198  85.530  83.178  1.00 27.38  ?  85  THR A C     1 
ATOM   587  O  O     . THR A 1 84  ? 16.319  86.084  83.833  1.00 27.53  ?  85  THR A O     1 
ATOM   588  C  CB    . THR A 1 84  ? 16.935  83.184  82.328  1.00 27.50  ?  85  THR A CB    1 
ATOM   589  O  OG1   . THR A 1 84  ? 16.786  82.397  81.153  1.00 29.00  ?  85  THR A OG1   1 
ATOM   590  C  CG2   . THR A 1 84  ? 15.947  82.742  83.401  1.00 27.21  ?  85  THR A CG2   1 
ATOM   591  N  N     . ILE A 1 85  ? 18.512  85.646  83.464  1.00 27.54  ?  86  ILE A N     1 
ATOM   592  C  CA    . ILE A 1 85  ? 19.014  86.454  84.576  1.00 28.41  ?  86  ILE A CA    1 
ATOM   593  C  C     . ILE A 1 85  ? 18.628  87.917  84.372  1.00 29.78  ?  86  ILE A C     1 
ATOM   594  O  O     . ILE A 1 85  ? 18.100  88.539  85.290  1.00 29.87  ?  86  ILE A O     1 
ATOM   595  C  CB    . ILE A 1 85  ? 20.556  86.309  84.751  1.00 28.20  ?  86  ILE A CB    1 
ATOM   596  C  CG1   . ILE A 1 85  ? 20.958  84.850  85.043  1.00 28.59  ?  86  ILE A CG1   1 
ATOM   597  C  CG2   . ILE A 1 85  ? 21.084  87.271  85.828  1.00 28.17  ?  86  ILE A CG2   1 
ATOM   598  C  CD1   . ILE A 1 85  ? 22.421  84.579  84.851  1.00 29.33  ?  86  ILE A CD1   1 
ATOM   599  N  N     . ILE A 1 86  ? 18.866  88.453  83.169  1.00 31.02  ?  87  ILE A N     1 
ATOM   600  C  CA    . ILE A 1 86  ? 18.530  89.832  82.831  1.00 33.28  ?  87  ILE A CA    1 
ATOM   601  C  C     . ILE A 1 86  ? 17.021  90.084  83.000  1.00 35.57  ?  87  ILE A C     1 
ATOM   602  O  O     . ILE A 1 86  ? 16.644  91.076  83.616  1.00 35.83  ?  87  ILE A O     1 
ATOM   603  C  CB    . ILE A 1 86  ? 19.055  90.215  81.415  1.00 33.71  ?  87  ILE A CB    1 
ATOM   604  C  CG1   . ILE A 1 86  ? 20.591  90.142  81.349  1.00 33.91  ?  87  ILE A CG1   1 
ATOM   605  C  CG2   . ILE A 1 86  ? 18.554  91.600  80.981  1.00 34.53  ?  87  ILE A CG2   1 
ATOM   606  C  CD1   . ILE A 1 86  ? 21.327  91.014  82.392  1.00 35.11  ?  87  ILE A CD1   1 
ATOM   607  N  N     . ASP A 1 87  ? 16.169  89.147  82.539  1.00 36.96  ?  88  ASP A N     1 
ATOM   608  C  CA    . ASP A 1 87  ? 14.714  89.279  82.668  1.00 38.83  ?  88  ASP A CA    1 
ATOM   609  C  C     . ASP A 1 87  ? 14.264  89.254  84.117  1.00 39.33  ?  88  ASP A C     1 
ATOM   610  O  O     . ASP A 1 87  ? 13.339  89.976  84.485  1.00 39.97  ?  88  ASP A O     1 
ATOM   611  C  CB    . ASP A 1 87  ? 13.986  88.160  81.904  1.00 42.38  ?  88  ASP A CB    1 
ATOM   612  C  CG    . ASP A 1 87  ? 13.853  88.387  80.410  1.00 51.08  ?  88  ASP A CG    1 
ATOM   613  O  OD1   . ASP A 1 87  ? 14.162  89.520  79.947  1.00 52.99  ?  88  ASP A OD1   1 
ATOM   614  O  OD2   . ASP A 1 87  ? 13.453  87.430  79.695  1.00 54.39  ?  88  ASP A OD2   1 
ATOM   615  N  N     . LYS A 1 88  ? 14.894  88.411  84.928  1.00 38.92  ?  89  LYS A N     1 
ATOM   616  C  CA    . LYS A 1 88  ? 14.565  88.280  86.337  1.00 39.48  ?  89  LYS A CA    1 
ATOM   617  C  C     . LYS A 1 88  ? 14.843  89.592  87.071  1.00 40.42  ?  89  LYS A C     1 
ATOM   618  O  O     . LYS A 1 88  ? 14.006  90.041  87.854  1.00 40.93  ?  89  LYS A O     1 
ATOM   619  C  CB    . LYS A 1 88  ? 15.356  87.120  86.958  1.00 40.72  ?  89  LYS A CB    1 
ATOM   620  C  CG    . LYS A 1 88  ? 14.670  86.469  88.144  1.00 44.31  ?  89  LYS A CG    1 
ATOM   621  C  CD    . LYS A 1 88  ? 15.381  85.193  88.573  1.00 48.41  ?  89  LYS A CD    1 
ATOM   622  C  CE    . LYS A 1 88  ? 14.556  84.428  89.573  1.00 51.48  ?  89  LYS A CE    1 
ATOM   623  N  NZ    . LYS A 1 88  ? 13.150  84.291  89.111  1.00 53.38  ?  89  LYS A NZ    1 
ATOM   624  N  N     . LEU A 1 89  ? 15.973  90.235  86.779  1.00 40.61  ?  90  LEU A N     1 
ATOM   625  C  CA    . LEU A 1 89  ? 16.313  91.509  87.402  1.00 41.91  ?  90  LEU A CA    1 
ATOM   626  C  C     . LEU A 1 89  ? 15.398  92.678  86.994  1.00 44.17  ?  90  LEU A C     1 
ATOM   627  O  O     . LEU A 1 89  ? 15.205  93.584  87.800  1.00 44.66  ?  90  LEU A O     1 
ATOM   628  C  CB    . LEU A 1 89  ? 17.781  91.882  87.144  1.00 41.44  ?  90  LEU A CB    1 
ATOM   629  C  CG    . LEU A 1 89  ? 18.815  90.974  87.791  1.00 41.94  ?  90  LEU A CG    1 
ATOM   630  C  CD1   . LEU A 1 89  ? 20.153  91.073  87.074  1.00 42.10  ?  90  LEU A CD1   1 
ATOM   631  C  CD2   . LEU A 1 89  ? 18.958  91.269  89.277  1.00 42.21  ?  90  LEU A CD2   1 
ATOM   632  N  N     . GLU A 1 90  ? 14.839  92.671  85.769  1.00 45.46  ?  91  GLU A N     1 
ATOM   633  C  CA    . GLU A 1 90  ? 14.005  93.789  85.314  1.00 47.52  ?  91  GLU A CA    1 
ATOM   634  C  C     . GLU A 1 90  ? 12.484  93.547  85.377  1.00 49.39  ?  91  GLU A C     1 
ATOM   635  O  O     . GLU A 1 90  ? 11.745  94.095  84.553  1.00 50.17  ?  91  GLU A O     1 
ATOM   636  C  CB    . GLU A 1 90  ? 14.414  94.244  83.904  1.00 49.75  ?  91  GLU A CB    1 
ATOM   637  C  CG    . GLU A 1 90  ? 14.257  93.182  82.826  1.00 54.16  ?  91  GLU A CG    1 
ATOM   638  C  CD    . GLU A 1 90  ? 14.863  93.531  81.479  1.00 60.23  ?  91  GLU A CD    1 
ATOM   639  O  OE1   . GLU A 1 90  ? 15.554  94.572  81.390  1.00 61.18  ?  91  GLU A OE1   1 
ATOM   640  O  OE2   . GLU A 1 90  ? 14.659  92.758  80.513  1.00 62.55  ?  91  GLU A OE2   1 
ATOM   641  N  N     . ARG A 1 91  ? 12.003  92.791  86.379  1.00 50.03  ?  92  ARG A N     1 
ATOM   642  C  CA    . ARG A 1 91  ? 10.561  92.562  86.523  1.00 50.94  ?  92  ARG A CA    1 
ATOM   643  C  C     . ARG A 1 91  ? 9.947   93.262  87.754  1.00 51.72  ?  92  ARG A C     1 
ATOM   644  O  O     . ARG A 1 91  ? 10.664  93.736  88.640  1.00 51.96  ?  92  ARG A O     1 
ATOM   645  C  CB    . ARG A 1 91  ? 10.225  91.068  86.500  1.00 51.91  ?  92  ARG A CB    1 
ATOM   646  C  CG    . ARG A 1 91  ? 10.050  90.539  85.086  1.00 54.61  ?  92  ARG A CG    1 
ATOM   647  N  N     . ALA A 1 102 ? 12.087  91.582  94.767  1.00 51.05  ?  103 ALA A N     1 
ATOM   648  C  CA    . ALA A 1 102 ? 13.315  92.202  94.271  1.00 51.54  ?  103 ALA A CA    1 
ATOM   649  C  C     . ALA A 1 102 ? 14.532  91.352  94.633  1.00 51.19  ?  103 ALA A C     1 
ATOM   650  O  O     . ALA A 1 102 ? 15.179  91.610  95.657  1.00 51.97  ?  103 ALA A O     1 
ATOM   651  C  CB    . ALA A 1 102 ? 13.468  93.605  94.848  1.00 52.21  ?  103 ALA A CB    1 
ATOM   652  N  N     . ILE A 1 103 ? 14.847  90.340  93.799  1.00 49.42  ?  104 ILE A N     1 
ATOM   653  C  CA    . ILE A 1 103 ? 15.980  89.438  94.038  1.00 48.07  ?  104 ILE A CA    1 
ATOM   654  C  C     . ILE A 1 103 ? 17.325  90.134  93.764  1.00 46.03  ?  104 ILE A C     1 
ATOM   655  O  O     . ILE A 1 103 ? 17.464  90.797  92.731  1.00 47.14  ?  104 ILE A O     1 
ATOM   656  C  CB    . ILE A 1 103 ? 15.824  88.167  93.165  1.00 48.50  ?  104 ILE A CB    1 
ATOM   657  N  N     . ALA A 1 104 ? 18.299  90.016  94.686  1.00 42.77  ?  105 ALA A N     1 
ATOM   658  C  CA    . ALA A 1 104 ? 19.618  90.613  94.460  1.00 40.32  ?  105 ALA A CA    1 
ATOM   659  C  C     . ALA A 1 104 ? 20.481  89.590  93.706  1.00 37.54  ?  105 ALA A C     1 
ATOM   660  O  O     . ALA A 1 104 ? 20.450  88.402  94.044  1.00 37.09  ?  105 ALA A O     1 
ATOM   661  C  CB    . ALA A 1 104 ? 20.270  90.985  95.783  1.00 40.31  ?  105 ALA A CB    1 
ATOM   662  N  N     . LEU A 1 105 ? 21.230  90.032  92.679  1.00 35.34  ?  106 LEU A N     1 
ATOM   663  C  CA    . LEU A 1 105 ? 22.058  89.124  91.885  1.00 33.47  ?  106 LEU A CA    1 
ATOM   664  C  C     . LEU A 1 105 ? 23.065  88.300  92.733  1.00 31.53  ?  106 LEU A C     1 
ATOM   665  O  O     . LEU A 1 105 ? 23.163  87.089  92.551  1.00 30.99  ?  106 LEU A O     1 
ATOM   666  C  CB    . LEU A 1 105 ? 22.757  89.871  90.743  1.00 33.40  ?  106 LEU A CB    1 
ATOM   667  C  CG    . LEU A 1 105 ? 23.672  89.032  89.859  1.00 34.29  ?  106 LEU A CG    1 
ATOM   668  C  CD1   . LEU A 1 105 ? 22.883  87.981  89.073  1.00 34.27  ?  106 LEU A CD1   1 
ATOM   669  C  CD2   . LEU A 1 105 ? 24.513  89.910  88.956  1.00 34.76  ?  106 LEU A CD2   1 
ATOM   670  N  N     . THR A 1 106 ? 23.735  88.931  93.697  1.00 30.53  ?  107 THR A N     1 
ATOM   671  C  CA    . THR A 1 106 ? 24.679  88.229  94.568  1.00 30.45  ?  107 THR A CA    1 
ATOM   672  C  C     . THR A 1 106 ? 23.995  87.418  95.711  1.00 30.39  ?  107 THR A C     1 
ATOM   673  O  O     . THR A 1 106 ? 24.674  86.717  96.457  1.00 30.67  ?  107 THR A O     1 
ATOM   674  C  CB    . THR A 1 106 ? 25.747  89.189  95.074  1.00 31.45  ?  107 THR A CB    1 
ATOM   675  O  OG1   . THR A 1 106 ? 25.112  90.270  95.754  1.00 32.30  ?  107 THR A OG1   1 
ATOM   676  C  CG2   . THR A 1 106 ? 26.634  89.693  93.939  1.00 31.19  ?  107 THR A CG2   1 
ATOM   677  N  N     . ARG A 1 107 ? 22.668  87.473  95.805  1.00 29.88  ?  108 ARG A N     1 
ATOM   678  C  CA    . ARG A 1 107 ? 21.872  86.668  96.724  1.00 29.67  ?  108 ARG A CA    1 
ATOM   679  C  C     . ARG A 1 107 ? 21.188  85.476  95.981  1.00 28.34  ?  108 ARG A C     1 
ATOM   680  O  O     . ARG A 1 107 ? 20.631  84.599  96.642  1.00 28.95  ?  108 ARG A O     1 
ATOM   681  C  CB    . ARG A 1 107 ? 20.826  87.541  97.457  1.00 31.88  ?  108 ARG A CB    1 
ATOM   682  C  CG    . ARG A 1 107 ? 21.465  88.544  98.406  1.00 36.78  ?  108 ARG A CG    1 
ATOM   683  C  CD    . ARG A 1 107 ? 20.441  89.300  99.236  1.00 42.65  ?  108 ARG A CD    1 
ATOM   684  N  NE    . ARG A 1 107 ? 21.003  89.742  100.515 1.00 47.35  ?  108 ARG A NE    1 
ATOM   685  C  CZ    . ARG A 1 107 ? 21.312  91.003  100.808 1.00 50.62  ?  108 ARG A CZ    1 
ATOM   686  N  NH1   . ARG A 1 107 ? 21.090  91.972  99.925  1.00 50.48  1  108 ARG A NH1   1 
ATOM   687  N  NH2   . ARG A 1 107 ? 21.836  91.306  101.989 1.00 50.46  ?  108 ARG A NH2   1 
ATOM   688  N  N     . MET A 1 108 ? 21.226  85.445  94.624  1.00 26.63  ?  109 MET A N     1 
ATOM   689  C  CA    . MET A 1 108 ? 20.639  84.372  93.820  1.00 25.67  ?  109 MET A CA    1 
ATOM   690  C  C     . MET A 1 108 ? 21.294  83.023  94.102  1.00 23.99  ?  109 MET A C     1 
ATOM   691  O  O     . MET A 1 108 ? 22.503  82.863  93.977  1.00 23.84  ?  109 MET A O     1 
ATOM   692  C  CB    . MET A 1 108 ? 20.660  84.708  92.322  1.00 26.73  ?  109 MET A CB    1 
ATOM   693  C  CG    . MET A 1 108 ? 19.502  85.608  91.902  1.00 30.83  ?  109 MET A CG    1 
ATOM   694  S  SD    . MET A 1 108 ? 19.508  86.061  90.147  1.00 39.52  ?  109 MET A SD    1 
ATOM   695  C  CE    . MET A 1 108 ? 19.434  84.435  89.389  1.00 37.47  ?  109 MET A CE    1 
ATOM   696  N  N     . GLN A 1 109 ? 20.486  82.071  94.519  1.00 22.73  ?  110 GLN A N     1 
ATOM   697  C  CA    . GLN A 1 109 ? 20.932  80.741  94.912  1.00 22.12  ?  110 GLN A CA    1 
ATOM   698  C  C     . GLN A 1 109 ? 21.129  79.751  93.787  1.00 20.77  ?  110 GLN A C     1 
ATOM   699  O  O     . GLN A 1 109 ? 21.690  78.700  94.025  1.00 20.82  ?  110 GLN A O     1 
ATOM   700  C  CB    . GLN A 1 109 ? 19.908  80.148  95.893  1.00 23.09  ?  110 GLN A CB    1 
ATOM   701  C  CG    . GLN A 1 109 ? 19.839  80.919  97.202  1.00 26.73  ?  110 GLN A CG    1 
ATOM   702  C  CD    . GLN A 1 109 ? 18.702  80.491  98.115  1.00 30.16  ?  110 GLN A CD    1 
ATOM   703  O  OE1   . GLN A 1 109 ? 18.729  80.756  99.319  1.00 31.78  ?  110 GLN A OE1   1 
ATOM   704  N  NE2   . GLN A 1 109 ? 17.685  79.830  97.577  1.00 29.75  ?  110 GLN A NE2   1 
ATOM   705  N  N     . ASP A 1 110 ? 20.628  80.050  92.590  1.00 19.78  ?  111 ASP A N     1 
ATOM   706  C  CA    . ASP A 1 110 ? 20.597  79.102  91.504  1.00 19.17  ?  111 ASP A CA    1 
ATOM   707  C  C     . ASP A 1 110 ? 21.191  79.547  90.157  1.00 18.82  ?  111 ASP A C     1 
ATOM   708  O  O     . ASP A 1 110 ? 20.786  78.965  89.150  1.00 19.59  ?  111 ASP A O     1 
ATOM   709  C  CB    . ASP A 1 110 ? 19.134  78.637  91.290  1.00 21.25  ?  111 ASP A CB    1 
ATOM   710  C  CG    . ASP A 1 110 ? 18.247  79.735  90.706  1.00 27.78  ?  111 ASP A CG    1 
ATOM   711  O  OD1   . ASP A 1 110 ? 18.508  80.932  90.997  1.00 29.37  ?  111 ASP A OD1   1 
ATOM   712  O  OD2   . ASP A 1 110 ? 17.317  79.404  89.932  1.00 30.18  -1 111 ASP A OD2   1 
ATOM   713  N  N     . ILE A 1 111 ? 22.230  80.436  90.081  1.00 18.24  ?  112 ILE A N     1 
ATOM   714  C  CA    . ILE A 1 111 ? 22.885  80.713  88.763  1.00 18.17  ?  112 ILE A CA    1 
ATOM   715  C  C     . ILE A 1 111 ? 23.364  79.363  88.162  1.00 17.05  ?  112 ILE A C     1 
ATOM   716  O  O     . ILE A 1 111 ? 23.078  79.049  87.018  1.00 17.45  ?  112 ILE A O     1 
ATOM   717  C  CB    . ILE A 1 111 ? 24.067  81.715  88.832  1.00 19.27  ?  112 ILE A CB    1 
ATOM   718  C  CG1   . ILE A 1 111 ? 23.690  83.014  89.637  1.00 21.29  ?  112 ILE A CG1   1 
ATOM   719  C  CG2   . ILE A 1 111 ? 24.628  82.008  87.423  1.00 19.19  ?  112 ILE A CG2   1 
ATOM   720  C  CD1   . ILE A 1 111 ? 22.886  83.942  89.026  1.00 22.56  ?  112 ILE A CD1   1 
ATOM   721  N  N     . GLY A 1 112 ? 23.944  78.527  89.014  1.00 15.18  ?  113 GLY A N     1 
ATOM   722  C  CA    . GLY A 1 112 ? 24.250  77.150  88.677  1.00 13.52  ?  113 GLY A CA    1 
ATOM   723  C  C     . GLY A 1 112 ? 23.269  76.297  89.457  1.00 11.71  ?  113 GLY A C     1 
ATOM   724  O  O     . GLY A 1 112 ? 22.963  76.601  90.609  1.00 11.20  ?  113 GLY A O     1 
ATOM   725  N  N     . GLY A 1 113 ? 22.720  75.273  88.823  1.00 10.93  ?  114 GLY A N     1 
ATOM   726  C  CA    . GLY A 1 113 ? 21.764  74.370  89.458  1.00 10.41  ?  114 GLY A CA    1 
ATOM   727  C  C     . GLY A 1 113 ? 21.967  72.928  89.024  1.00 10.90  ?  114 GLY A C     1 
ATOM   728  O  O     . GLY A 1 113 ? 22.171  72.657  87.842  1.00 12.31  ?  114 GLY A O     1 
ATOM   729  N  N     . CYS A 1 114 ? 21.946  72.006  89.982  1.00 9.88   ?  115 CYS A N     1 
ATOM   730  C  CA    . CYS A 1 114 ? 22.066  70.548  89.872  1.00 10.16  ?  115 CYS A CA    1 
ATOM   731  C  C     . CYS A 1 114 ? 20.779  69.912  90.302  1.00 9.27   ?  115 CYS A C     1 
ATOM   732  O  O     . CYS A 1 114 ? 20.127  70.428  91.185  1.00 9.06   ?  115 CYS A O     1 
ATOM   733  C  CB    . CYS A 1 114 ? 23.200  70.040  90.756  1.00 12.44  ?  115 CYS A CB    1 
ATOM   734  S  SG    . CYS A 1 114 ? 24.812  70.393  90.105  1.00 23.42  ?  115 CYS A SG    1 
ATOM   735  N  N     . ARG A 1 115 ? 20.492  68.719  89.799  1.00 9.45   ?  116 ARG A N     1 
ATOM   736  C  CA    . ARG A 1 115 ? 19.267  68.019  90.134  1.00 10.05  ?  116 ARG A CA    1 
ATOM   737  C  C     . ARG A 1 115 ? 19.476  66.518  90.182  1.00 10.42  ?  116 ARG A C     1 
ATOM   738  O  O     . ARG A 1 115 ? 20.055  65.969  89.261  1.00 10.93  ?  116 ARG A O     1 
ATOM   739  C  CB    . ARG A 1 115 ? 18.187  68.382  89.091  1.00 11.45  ?  116 ARG A CB    1 
ATOM   740  C  CG    . ARG A 1 115 ? 16.843  67.700  89.300  1.00 14.93  ?  116 ARG A CG    1 
ATOM   741  C  CD    . ARG A 1 115 ? 15.918  68.058  88.171  1.00 18.22  ?  116 ARG A CD    1 
ATOM   742  N  NE    . ARG A 1 115 ? 15.491  69.445  88.302  1.00 20.49  ?  116 ARG A NE    1 
ATOM   743  C  CZ    . ARG A 1 115 ? 14.950  70.171  87.333  1.00 19.59  ?  116 ARG A CZ    1 
ATOM   744  N  NH1   . ARG A 1 115 ? 14.803  69.663  86.116  1.00 17.73  1  116 ARG A NH1   1 
ATOM   745  N  NH2   . ARG A 1 115 ? 14.551  71.410  87.574  1.00 18.93  ?  116 ARG A NH2   1 
ATOM   746  N  N     . ALA A 1 116 ? 18.994  65.848  91.230  1.00 10.29  ?  117 ALA A N     1 
ATOM   747  C  CA    . ALA A 1 116 ? 19.038  64.389  91.295  1.00 11.12  ?  117 ALA A CA    1 
ATOM   748  C  C     . ALA A 1 116 ? 17.619  63.837  91.301  1.00 12.85  ?  117 ALA A C     1 
ATOM   749  O  O     . ALA A 1 116 ? 16.790  64.263  92.102  1.00 13.96  ?  117 ALA A O     1 
ATOM   750  C  CB    . ALA A 1 116 ? 19.785  63.928  92.535  1.00 11.51  ?  117 ALA A CB    1 
ATOM   751  N  N     . ILE A 1 117 ? 17.321  62.919  90.399  1.00 13.32  ?  118 ILE A N     1 
ATOM   752  C  CA    . ILE A 1 117 ? 16.009  62.272  90.306  1.00 14.45  ?  118 ILE A CA    1 
ATOM   753  C  C     . ILE A 1 117 ? 16.102  60.834  90.836  1.00 15.76  ?  118 ILE A C     1 
ATOM   754  O  O     . ILE A 1 117 ? 16.755  59.974  90.236  1.00 15.88  ?  118 ILE A O     1 
ATOM   755  C  CB    . ILE A 1 117 ? 15.420  62.371  88.868  1.00 14.79  ?  118 ILE A CB    1 
ATOM   756  C  CG1   . ILE A 1 117 ? 15.378  63.844  88.407  1.00 14.71  ?  118 ILE A CG1   1 
ATOM   757  C  CG2   . ILE A 1 117 ? 14.025  61.770  88.798  1.00 15.48  ?  118 ILE A CG2   1 
ATOM   758  C  CD1   . ILE A 1 117 ? 15.507  63.988  87.013  1.00 15.41  ?  118 ILE A CD1   1 
ATOM   759  N  N     . VAL A 1 118 ? 15.506  60.607  92.021  1.00 16.17  ?  119 VAL A N     1 
ATOM   760  C  CA    . VAL A 1 118 ? 15.527  59.338  92.738  1.00 16.72  ?  119 VAL A CA    1 
ATOM   761  C  C     . VAL A 1 118 ? 14.206  58.538  92.537  1.00 18.25  ?  119 VAL A C     1 
ATOM   762  O  O     . VAL A 1 118 ? 13.213  59.064  92.028  1.00 18.04  ?  119 VAL A O     1 
ATOM   763  C  CB    . VAL A 1 118 ? 15.853  59.570  94.233  1.00 16.72  ?  119 VAL A CB    1 
ATOM   764  C  CG1   . VAL A 1 118 ? 17.227  60.231  94.418  1.00 16.96  ?  119 VAL A CG1   1 
ATOM   765  C  CG2   . VAL A 1 118 ? 14.768  60.401  94.889  1.00 16.60  ?  119 VAL A CG2   1 
ATOM   766  N  N     . ARG A 1 119 ? 14.219  57.254  92.899  1.00 19.14  ?  120 ARG A N     1 
ATOM   767  C  CA    . ARG A 1 119 ? 13.090  56.365  92.712  1.00 20.27  ?  120 ARG A CA    1 
ATOM   768  C  C     . ARG A 1 119 ? 11.948  56.690  93.652  1.00 19.48  ?  120 ARG A C     1 
ATOM   769  O  O     . ARG A 1 119 ? 10.814  56.798  93.206  1.00 20.05  ?  120 ARG A O     1 
ATOM   770  C  CB    . ARG A 1 119 ? 13.550  54.907  92.904  1.00 24.00  ?  120 ARG A CB    1 
ATOM   771  C  CG    . ARG A 1 119 ? 12.505  53.829  92.575  1.00 32.09  ?  120 ARG A CG    1 
ATOM   772  C  CD    . ARG A 1 119 ? 12.907  52.428  93.077  1.00 40.38  ?  120 ARG A CD    1 
ATOM   773  N  NE    . ARG A 1 119 ? 14.329  52.127  92.853  1.00 47.39  ?  120 ARG A NE    1 
ATOM   774  C  CZ    . ARG A 1 119 ? 14.906  50.961  93.127  1.00 52.47  ?  120 ARG A CZ    1 
ATOM   775  N  NH1   . ARG A 1 119 ? 14.189  49.955  93.619  1.00 52.68  1  120 ARG A NH1   1 
ATOM   776  N  NH2   . ARG A 1 119 ? 16.203  50.783  92.890  1.00 53.41  ?  120 ARG A NH2   1 
ATOM   777  N  N     . ASN A 1 120 ? 12.235  56.854  94.941  1.00 18.50  ?  121 ASN A N     1 
ATOM   778  C  CA    . ASN A 1 120 ? 11.201  57.082  95.936  1.00 18.62  ?  121 ASN A CA    1 
ATOM   779  C  C     . ASN A 1 120 ? 11.659  58.019  97.089  1.00 18.65  ?  121 ASN A C     1 
ATOM   780  O  O     . ASN A 1 120 ? 12.791  58.491  97.071  1.00 17.93  ?  121 ASN A O     1 
ATOM   781  C  CB    . ASN A 1 120 ? 10.698  55.719  96.455  1.00 20.01  ?  121 ASN A CB    1 
ATOM   782  C  CG    . ASN A 1 120 ? 11.818  54.815  96.899  1.00 23.46  ?  121 ASN A CG    1 
ATOM   783  O  OD1   . ASN A 1 120 ? 12.620  55.167  97.763  1.00 24.84  ?  121 ASN A OD1   1 
ATOM   784  N  ND2   . ASN A 1 120 ? 11.920  53.646  96.285  1.00 24.00  ?  121 ASN A ND2   1 
ATOM   785  N  N     . ILE A 1 121 ? 10.757  58.328  98.045  1.00 19.19  ?  122 ILE A N     1 
ATOM   786  C  CA    . ILE A 1 121 ? 11.016  59.220  99.176  1.00 20.78  ?  122 ILE A CA    1 
ATOM   787  C  C     . ILE A 1 121 ? 12.080  58.664  100.104 1.00 21.96  ?  122 ILE A C     1 
ATOM   788  O  O     . ILE A 1 121 ? 12.856  59.437  100.674 1.00 21.66  ?  122 ILE A O     1 
ATOM   789  C  CB    . ILE A 1 121 ? 9.708   59.617  99.931  1.00 21.59  ?  122 ILE A CB    1 
ATOM   790  C  CG1   . ILE A 1 121 ? 8.863   60.569  99.068  1.00 22.81  ?  122 ILE A CG1   1 
ATOM   791  C  CG2   . ILE A 1 121 ? 9.995   60.285  101.283 1.00 22.35  ?  122 ILE A CG2   1 
ATOM   792  C  CD1   . ILE A 1 121 ? 9.506   61.959  98.772  1.00 24.05  ?  122 ILE A CD1   1 
ATOM   793  N  N     . GLU A 1 122 ? 12.138  57.331  100.251 1.00 23.34  ?  123 GLU A N     1 
ATOM   794  C  CA    . GLU A 1 122 ? 13.150  56.710  101.095 1.00 25.03  ?  123 GLU A CA    1 
ATOM   795  C  C     . GLU A 1 122 ? 14.541  56.947  100.496 1.00 24.93  ?  123 GLU A C     1 
ATOM   796  O  O     . GLU A 1 122 ? 15.472  57.279  101.216 1.00 25.15  ?  123 GLU A O     1 
ATOM   797  C  CB    . GLU A 1 122 ? 12.858  55.212  101.286 1.00 30.06  ?  123 GLU A CB    1 
ATOM   798  C  CG    . GLU A 1 122 ? 12.457  54.852  102.713 1.00 40.97  ?  123 GLU A CG    1 
ATOM   799  C  CD    . GLU A 1 122 ? 10.964  54.779  103.010 1.00 54.49  ?  123 GLU A CD    1 
ATOM   800  O  OE1   . GLU A 1 122 ? 10.192  55.562  102.406 1.00 56.70  ?  123 GLU A OE1   1 
ATOM   801  O  OE2   . GLU A 1 122 ? 10.570  53.942  103.860 1.00 58.57  -1 123 GLU A OE2   1 
ATOM   802  N  N     . GLN A 1 123 ? 14.662  56.824  99.174  1.00 24.46  ?  124 GLN A N     1 
ATOM   803  C  CA    . GLN A 1 123 ? 15.898  57.092  98.468  1.00 24.64  ?  124 GLN A CA    1 
ATOM   804  C  C     . GLN A 1 123 ? 16.257  58.587  98.564  1.00 23.72  ?  124 GLN A C     1 
ATOM   805  O  O     . GLN A 1 123 ? 17.405  58.914  98.830  1.00 23.69  ?  124 GLN A O     1 
ATOM   806  C  CB    . GLN A 1 123 ? 15.765  56.645  97.009  1.00 27.08  ?  124 GLN A CB    1 
ATOM   807  C  CG    . GLN A 1 123 ? 17.105  56.582  96.301  1.00 33.07  ?  124 GLN A CG    1 
ATOM   808  C  CD    . GLN A 1 123 ? 17.068  55.623  95.149  1.00 39.96  ?  124 GLN A CD    1 
ATOM   809  O  OE1   . GLN A 1 123 ? 16.482  55.899  94.096  1.00 40.90  ?  124 GLN A OE1   1 
ATOM   810  N  NE2   . GLN A 1 123 ? 17.708  54.471  95.322  1.00 42.55  ?  124 GLN A NE2   1 
ATOM   811  N  N     . LEU A 1 124 ? 15.265  59.483  98.398  1.00 23.18  ?  125 LEU A N     1 
ATOM   812  C  CA    . LEU A 1 124 ? 15.424  60.931  98.501  1.00 22.83  ?  125 LEU A CA    1 
ATOM   813  C  C     . LEU A 1 124 ? 16.034  61.363  99.834  1.00 22.60  ?  125 LEU A C     1 
ATOM   814  O  O     . LEU A 1 124 ? 16.975  62.146  99.833  1.00 22.29  ?  125 LEU A O     1 
ATOM   815  C  CB    . LEU A 1 124 ? 14.080  61.665  98.256  1.00 22.67  ?  125 LEU A CB    1 
ATOM   816  C  CG    . LEU A 1 124 ? 14.183  63.126  97.754  1.00 24.05  ?  125 LEU A CG    1 
ATOM   817  C  CD1   . LEU A 1 124 ? 12.891  63.591  97.113  1.00 24.32  ?  125 LEU A CD1   1 
ATOM   818  C  CD2   . LEU A 1 124 ? 14.439  64.085  98.888  1.00 25.29  ?  125 LEU A CD2   1 
ATOM   819  N  N     . LYS A 1 125 ? 15.472  60.904  100.959 1.00 22.71  ?  126 LYS A N     1 
ATOM   820  C  CA    . LYS A 1 125 ? 15.947  61.248  102.309 1.00 23.20  ?  126 LYS A CA    1 
ATOM   821  C  C     . LYS A 1 125 ? 17.325  60.657  102.576 1.00 22.41  ?  126 LYS A C     1 
ATOM   822  O  O     . LYS A 1 125 ? 18.139  61.292  103.232 1.00 22.74  ?  126 LYS A O     1 
ATOM   823  C  CB    . LYS A 1 125 ? 14.952  60.767  103.381 1.00 25.95  ?  126 LYS A CB    1 
ATOM   824  C  CG    . LYS A 1 125 ? 13.635  61.549  103.439 1.00 30.64  ?  126 LYS A CG    1 
ATOM   825  C  CD    . LYS A 1 125 ? 12.796  61.081  104.640 1.00 35.76  ?  126 LYS A CD    1 
ATOM   826  C  CE    . LYS A 1 125 ? 11.727  62.052  105.085 1.00 39.03  ?  126 LYS A CE    1 
ATOM   827  N  NZ    . LYS A 1 125 ? 10.557  62.047  104.178 1.00 41.19  1  126 LYS A NZ    1 
ATOM   828  N  N     . LYS A 1 126 ? 17.592  59.466  102.045 1.00 21.75  ?  127 LYS A N     1 
ATOM   829  C  CA    . LYS A 1 126 ? 18.880  58.785  102.143 1.00 22.75  ?  127 LYS A CA    1 
ATOM   830  C  C     . LYS A 1 126 ? 19.971  59.612  101.398 1.00 22.54  ?  127 LYS A C     1 
ATOM   831  O  O     . LYS A 1 126 ? 21.095  59.735  101.896 1.00 23.12  ?  127 LYS A O     1 
ATOM   832  C  CB    . LYS A 1 126 ? 18.731  57.398  101.516 1.00 25.62  ?  127 LYS A CB    1 
ATOM   833  C  CG    . LYS A 1 126 ? 19.909  56.468  101.607 1.00 31.91  ?  127 LYS A CG    1 
ATOM   834  C  CD    . LYS A 1 126 ? 19.485  55.095  101.055 1.00 38.87  ?  127 LYS A CD    1 
ATOM   835  C  CE    . LYS A 1 126 ? 20.606  54.071  101.045 1.00 44.64  ?  127 LYS A CE    1 
ATOM   836  N  NZ    . LYS A 1 126 ? 20.141  52.746  100.532 1.00 47.83  1  127 LYS A NZ    1 
ATOM   837  N  N     . LEU A 1 127 ? 19.630  60.200  100.235 1.00 21.44  ?  128 LEU A N     1 
ATOM   838  C  CA    . LEU A 1 127 ? 20.576  61.042  99.504  1.00 21.69  ?  128 LEU A CA    1 
ATOM   839  C  C     . LEU A 1 127 ? 20.771  62.384  100.223 1.00 21.91  ?  128 LEU A C     1 
ATOM   840  O  O     . LEU A 1 127 ? 21.896  62.857  100.297 1.00 21.97  ?  128 LEU A O     1 
ATOM   841  C  CB    . LEU A 1 127 ? 20.150  61.242  98.027  1.00 21.19  ?  128 LEU A CB    1 
ATOM   842  C  CG    . LEU A 1 127 ? 21.098  62.076  97.134  1.00 21.03  ?  128 LEU A CG    1 
ATOM   843  C  CD1   . LEU A 1 127 ? 22.514  61.540  97.163  1.00 21.34  ?  128 LEU A CD1   1 
ATOM   844  C  CD2   . LEU A 1 127 ? 20.597  62.112  95.704  1.00 20.99  ?  128 LEU A CD2   1 
ATOM   845  N  N     . LYS A 1 128 ? 19.700  62.960  100.807 1.00 22.24  ?  129 LYS A N     1 
ATOM   846  C  CA    . LYS A 1 128 ? 19.812  64.219  101.547 1.00 23.46  ?  129 LYS A CA    1 
ATOM   847  C  C     . LYS A 1 128 ? 20.736  64.075  102.759 1.00 24.83  ?  129 LYS A C     1 
ATOM   848  O  O     . LYS A 1 128 ? 21.544  64.954  103.002 1.00 24.83  ?  129 LYS A O     1 
ATOM   849  C  CB    . LYS A 1 128 ? 18.442  64.780  101.987 1.00 24.95  ?  129 LYS A CB    1 
ATOM   850  C  CG    . LYS A 1 128 ? 18.591  66.082  102.807 1.00 29.52  ?  129 LYS A CG    1 
ATOM   851  C  CD    . LYS A 1 128 ? 17.294  66.777  103.156 1.00 34.26  ?  129 LYS A CD    1 
ATOM   852  C  CE    . LYS A 1 128 ? 16.478  66.050  104.193 1.00 38.03  ?  129 LYS A CE    1 
ATOM   853  N  NZ    . LYS A 1 128 ? 16.878  66.421  105.573 1.00 40.12  1  129 LYS A NZ    1 
ATOM   854  N  N     . ASP A 1 129 ? 20.603  62.983  103.516 1.00 25.88  ?  130 ASP A N     1 
ATOM   855  C  CA    . ASP A 1 129 ? 21.420  62.727  104.702 1.00 27.56  ?  130 ASP A CA    1 
ATOM   856  C  C     . ASP A 1 129 ? 22.899  62.625  104.363 1.00 27.62  ?  130 ASP A C     1 
ATOM   857  O  O     . ASP A 1 129 ? 23.733  63.169  105.083 1.00 29.03  ?  130 ASP A O     1 
ATOM   858  C  CB    . ASP A 1 129 ? 20.942  61.452  105.415 1.00 31.54  ?  130 ASP A CB    1 
ATOM   859  C  CG    . ASP A 1 129 ? 19.680  61.649  106.248 1.00 42.36  ?  130 ASP A CG    1 
ATOM   860  O  OD1   . ASP A 1 129 ? 19.266  62.834  106.448 1.00 44.54  ?  130 ASP A OD1   1 
ATOM   861  O  OD2   . ASP A 1 129 ? 19.094  60.623  106.705 1.00 46.47  -1 130 ASP A OD2   1 
ATOM   862  N  N     . ARG A 1 130 ? 23.221  61.957  103.253 1.00 25.85  ?  131 ARG A N     1 
ATOM   863  C  CA    . ARG A 1 130 ? 24.584  61.801  102.772 1.00 24.61  ?  131 ARG A CA    1 
ATOM   864  C  C     . ARG A 1 130 ? 25.223  63.164  102.373 1.00 23.07  ?  131 ARG A C     1 
ATOM   865  O  O     . ARG A 1 130 ? 26.347  63.455  102.761 1.00 23.89  ?  131 ARG A O     1 
ATOM   866  C  CB    . ARG A 1 130 ? 24.602  60.782  101.615 1.00 26.02  ?  131 ARG A CB    1 
ATOM   867  C  CG    . ARG A 1 130 ? 25.999  60.354  101.241 1.00 31.02  ?  131 ARG A CG    1 
ATOM   868  C  CD    . ARG A 1 130 ? 26.014  59.155  100.326 1.00 35.60  ?  131 ARG A CD    1 
ATOM   869  N  NE    . ARG A 1 130 ? 25.841  57.909  101.070 1.00 40.29  ?  131 ARG A NE    1 
ATOM   870  C  CZ    . ARG A 1 130 ? 26.836  57.222  101.628 1.00 43.38  ?  131 ARG A CZ    1 
ATOM   871  N  NH1   . ARG A 1 130 ? 28.088  57.663  101.546 1.00 42.24  1  131 ARG A NH1   1 
ATOM   872  N  NH2   . ARG A 1 130 ? 26.585  56.092  102.278 1.00 44.58  ?  131 ARG A NH2   1 
ATOM   873  N  N     . LEU A 1 131 ? 24.492  64.006  101.657 1.00 21.51  ?  132 LEU A N     1 
ATOM   874  C  CA    . LEU A 1 131 ? 24.952  65.334  101.276 1.00 20.64  ?  132 LEU A CA    1 
ATOM   875  C  C     . LEU A 1 131 ? 25.132  66.235  102.513 1.00 21.00  ?  132 LEU A C     1 
ATOM   876  O  O     . LEU A 1 131 ? 26.079  67.021  102.559 1.00 20.77  ?  132 LEU A O     1 
ATOM   877  C  CB    . LEU A 1 131 ? 23.966  65.977  100.273 1.00 19.73  ?  132 LEU A CB    1 
ATOM   878  C  CG    . LEU A 1 131 ? 23.849  65.252  98.911  1.00 19.55  ?  132 LEU A CG    1 
ATOM   879  C  CD1   . LEU A 1 131 ? 22.691  65.795  98.099  1.00 19.20  ?  132 LEU A CD1   1 
ATOM   880  C  CD2   . LEU A 1 131 ? 25.165  65.314  98.120  1.00 18.83  ?  132 LEU A CD2   1 
ATOM   881  N  N     . VAL A 1 132 ? 24.230  66.109  103.514 1.00 21.45  ?  133 VAL A N     1 
ATOM   882  C  CA    . VAL A 1 132 ? 24.266  66.896  104.751 1.00 22.58  ?  133 VAL A CA    1 
ATOM   883  C  C     . VAL A 1 132 ? 25.447  66.477  105.641 1.00 23.56  ?  133 VAL A C     1 
ATOM   884  O  O     . VAL A 1 132 ? 26.070  67.324  106.274 1.00 23.15  ?  133 VAL A O     1 
ATOM   885  C  CB    . VAL A 1 132 ? 22.897  66.897  105.509 1.00 23.60  ?  133 VAL A CB    1 
ATOM   886  C  CG1   . VAL A 1 132 ? 23.036  67.461  106.927 1.00 24.41  ?  133 VAL A CG1   1 
ATOM   887  C  CG2   . VAL A 1 132 ? 21.835  67.676  104.734 1.00 23.56  ?  133 VAL A CG2   1 
ATOM   888  N  N     . LYS A 1 133 ? 25.780  65.186  105.652 1.00 24.96  ?  134 LYS A N     1 
ATOM   889  C  CA    . LYS A 1 133 ? 26.909  64.697  106.433 1.00 27.28  ?  134 LYS A CA    1 
ATOM   890  C  C     . LYS A 1 133 ? 28.258  64.849  105.730 1.00 28.35  ?  134 LYS A C     1 
ATOM   891  O  O     . LYS A 1 133 ? 29.270  64.547  106.331 1.00 29.07  ?  134 LYS A O     1 
ATOM   892  C  CB    . LYS A 1 133 ? 26.692  63.237  106.855 1.00 31.43  ?  134 LYS A CB    1 
ATOM   893  C  CG    . LYS A 1 133 ? 25.956  63.100  108.188 1.00 38.93  ?  134 LYS A CG    1 
ATOM   894  C  CD    . LYS A 1 133 ? 26.775  63.673  109.356 1.00 45.20  ?  134 LYS A CD    1 
ATOM   895  C  CE    . LYS A 1 133 ? 26.147  63.459  110.713 1.00 49.68  ?  134 LYS A CE    1 
ATOM   896  N  NZ    . LYS A 1 133 ? 27.035  63.963  111.805 1.00 52.06  1  134 LYS A NZ    1 
ATOM   897  N  N     . SER A 1 134 ? 28.288  65.286  104.469 1.00 28.76  ?  135 SER A N     1 
ATOM   898  C  CA    . SER A 1 134 ? 29.537  65.452  103.726 1.00 29.60  ?  135 SER A CA    1 
ATOM   899  C  C     . SER A 1 134 ? 30.419  66.525  104.329 1.00 30.43  ?  135 SER A C     1 
ATOM   900  O  O     . SER A 1 134 ? 29.954  67.628  104.631 1.00 31.19  ?  135 SER A O     1 
ATOM   901  C  CB    . SER A 1 134 ? 29.255  65.760  102.261 1.00 30.44  ?  135 SER A CB    1 
ATOM   902  O  OG    . SER A 1 134 ? 30.405  66.207  101.563 1.00 32.43  ?  135 SER A OG    1 
ATOM   903  N  N     . ARG A 1 135 ? 31.700  66.201  104.508 1.00 29.95  ?  136 ARG A N     1 
ATOM   904  C  CA    . ARG A 1 135 ? 32.644  67.152  105.064 1.00 29.57  ?  136 ARG A CA    1 
ATOM   905  C  C     . ARG A 1 135 ? 33.480  67.750  103.945 1.00 28.26  ?  136 ARG A C     1 
ATOM   906  O  O     . ARG A 1 135 ? 34.571  67.275  103.665 1.00 29.94  ?  136 ARG A O     1 
ATOM   907  C  CB    . ARG A 1 135 ? 33.496  66.488  106.150 1.00 31.80  ?  136 ARG A CB    1 
ATOM   908  C  CG    . ARG A 1 135 ? 32.790  66.477  107.509 1.00 37.11  ?  136 ARG A CG    1 
ATOM   909  C  CD    . ARG A 1 135 ? 32.851  65.144  108.242 1.00 42.90  ?  136 ARG A CD    1 
ATOM   910  N  NE    . ARG A 1 135 ? 34.208  64.602  108.346 1.00 48.47  ?  136 ARG A NE    1 
ATOM   911  C  CZ    . ARG A 1 135 ? 34.611  63.470  107.768 1.00 51.91  ?  136 ARG A CZ    1 
ATOM   912  N  NH1   . ARG A 1 135 ? 33.761  62.745  107.049 1.00 51.96  1  136 ARG A NH1   1 
ATOM   913  N  NH2   . ARG A 1 135 ? 35.865  63.056  107.908 1.00 51.60  ?  136 ARG A NH2   1 
ATOM   914  N  N     . SER A 1 136 ? 32.937  68.735  103.253 1.00 25.58  ?  137 SER A N     1 
ATOM   915  C  CA    . SER A 1 136 ? 33.652  69.396  102.165 1.00 23.86  ?  137 SER A CA    1 
ATOM   916  C  C     . SER A 1 136 ? 33.691  70.924  102.400 1.00 21.80  ?  137 SER A C     1 
ATOM   917  O  O     . SER A 1 136 ? 33.131  71.404  103.391 1.00 22.25  ?  137 SER A O     1 
ATOM   918  C  CB    . SER A 1 136 ? 33.051  69.017  100.808 1.00 24.08  ?  137 SER A CB    1 
ATOM   919  O  OG    . SER A 1 136 ? 31.878  69.742  100.484 1.00 24.81  ?  137 SER A OG    1 
ATOM   920  N  N     . LYS A 1 137 ? 34.385  71.675  101.542 1.00 19.35  ?  138 LYS A N     1 
ATOM   921  C  CA    . LYS A 1 137 ? 34.425  73.126  101.668 1.00 18.56  ?  138 LYS A CA    1 
ATOM   922  C  C     . LYS A 1 137 ? 33.117  73.802  101.226 1.00 17.80  ?  138 LYS A C     1 
ATOM   923  O  O     . LYS A 1 137 ? 32.996  75.014  101.335 1.00 18.20  ?  138 LYS A O     1 
ATOM   924  C  CB    . LYS A 1 137 ? 35.595  73.691  100.864 1.00 20.44  ?  138 LYS A CB    1 
ATOM   925  C  CG    . LYS A 1 137 ? 36.949  73.237  101.376 1.00 24.72  ?  138 LYS A CG    1 
ATOM   926  C  CD    . LYS A 1 137 ? 38.055  73.701  100.457 1.00 30.14  ?  138 LYS A CD    1 
ATOM   927  C  CE    . LYS A 1 137 ? 39.393  73.072  100.796 1.00 33.53  ?  138 LYS A CE    1 
ATOM   928  N  NZ    . LYS A 1 137 ? 40.317  73.131  99.636  1.00 35.05  1  138 LYS A NZ    1 
ATOM   929  N  N     . HIS A 1 138 ? 32.141  73.031  100.723 1.00 16.87  ?  139 HIS A N     1 
ATOM   930  C  CA    . HIS A 1 138 ? 30.895  73.549  100.189 1.00 16.02  ?  139 HIS A CA    1 
ATOM   931  C  C     . HIS A 1 138 ? 29.811  73.355  101.227 1.00 17.15  ?  139 HIS A C     1 
ATOM   932  O  O     . HIS A 1 138 ? 29.525  72.226  101.634 1.00 18.03  ?  139 HIS A O     1 
ATOM   933  C  CB    . HIS A 1 138 ? 30.602  72.906  98.820  1.00 14.55  ?  139 HIS A CB    1 
ATOM   934  C  CG    . HIS A 1 138 ? 31.846  72.769  97.993  1.00 16.23  ?  139 HIS A CG    1 
ATOM   935  N  ND1   . HIS A 1 138 ? 32.633  73.867  97.688  1.00 17.38  ?  139 HIS A ND1   1 
ATOM   936  C  CD2   . HIS A 1 138 ? 32.500  71.656  97.596  1.00 16.93  ?  139 HIS A CD2   1 
ATOM   937  C  CE1   . HIS A 1 138 ? 33.669  73.392  97.031  1.00 16.76  ?  139 HIS A CE1   1 
ATOM   938  N  NE2   . HIS A 1 138 ? 33.633  72.073  96.957  1.00 17.01  ?  139 HIS A NE2   1 
ATOM   939  N  N     . LYS A 1 139 ? 29.270  74.468  101.726 1.00 16.86  ?  140 LYS A N     1 
ATOM   940  C  CA    . LYS A 1 139 ? 28.312  74.416  102.808 1.00 17.72  ?  140 LYS A CA    1 
ATOM   941  C  C     . LYS A 1 139 ? 26.892  74.633  102.373 1.00 18.15  ?  140 LYS A C     1 
ATOM   942  O  O     . LYS A 1 139 ? 26.639  75.500  101.556 1.00 17.82  ?  140 LYS A O     1 
ATOM   943  C  CB    . LYS A 1 139 ? 28.688  75.434  103.918 1.00 20.38  ?  140 LYS A CB    1 
ATOM   944  C  CG    . LYS A 1 139 ? 30.129  75.339  104.427 1.00 25.09  ?  140 LYS A CG    1 
ATOM   945  C  CD    . LYS A 1 139 ? 30.488  73.943  104.938 1.00 31.61  ?  140 LYS A CD    1 
ATOM   946  C  CE    . LYS A 1 139 ? 31.961  73.784  105.182 1.00 37.17  ?  140 LYS A CE    1 
ATOM   947  N  NZ    . LYS A 1 139 ? 32.425  74.666  106.282 1.00 41.08  1  140 LYS A NZ    1 
ATOM   948  N  N     . ILE A 1 140 ? 25.954  73.857  102.945 1.00 18.07  ?  141 ILE A N     1 
ATOM   949  C  CA    . ILE A 1 140 ? 24.545  74.017  102.714 1.00 17.86  ?  141 ILE A CA    1 
ATOM   950  C  C     . ILE A 1 140 ? 24.113  75.162  103.637 1.00 18.82  ?  141 ILE A C     1 
ATOM   951  O  O     . ILE A 1 140 ? 24.069  74.991  104.852 1.00 19.46  ?  141 ILE A O     1 
ATOM   952  C  CB    . ILE A 1 140 ? 23.787  72.710  103.063 1.00 18.45  ?  141 ILE A CB    1 
ATOM   953  C  CG1   . ILE A 1 140 ? 24.344  71.503  102.267 1.00 18.97  ?  141 ILE A CG1   1 
ATOM   954  C  CG2   . ILE A 1 140 ? 22.275  72.883  102.839 1.00 18.75  ?  141 ILE A CG2   1 
ATOM   955  C  CD1   . ILE A 1 140 ? 23.699  70.142  102.513 1.00 19.31  ?  141 ILE A CD1   1 
ATOM   956  N  N     . LEU A 1 141 ? 23.858  76.338  103.078 1.00 18.78  ?  142 LEU A N     1 
ATOM   957  C  CA    . LEU A 1 141 ? 23.414  77.488  103.857 1.00 19.74  ?  142 LEU A CA    1 
ATOM   958  C  C     . LEU A 1 141 ? 21.953  77.388  104.237 1.00 20.87  ?  142 LEU A C     1 
ATOM   959  O  O     . LEU A 1 141 ? 21.560  77.923  105.279 1.00 22.28  ?  142 LEU A O     1 
ATOM   960  C  CB    . LEU A 1 141 ? 23.674  78.804  103.098 1.00 19.98  ?  142 LEU A CB    1 
ATOM   961  C  CG    . LEU A 1 141 ? 25.130  79.108  102.746 1.00 21.46  ?  142 LEU A CG    1 
ATOM   962  C  CD1   . LEU A 1 141 ? 25.266  80.518  102.249 1.00 21.66  ?  142 LEU A CD1   1 
ATOM   963  C  CD2   . LEU A 1 141 ? 26.058  78.920  103.955 1.00 22.39  ?  142 LEU A CD2   1 
ATOM   964  N  N     . LYS A 1 142 ? 21.134  76.709  103.400 1.00 20.30  ?  143 LYS A N     1 
ATOM   965  C  CA    . LYS A 1 142 ? 19.713  76.532  103.629 1.00 20.09  ?  143 LYS A CA    1 
ATOM   966  C  C     . LYS A 1 142 ? 19.192  75.211  103.060 1.00 19.01  ?  143 LYS A C     1 
ATOM   967  O  O     . LYS A 1 142 ? 19.486  74.847  101.938 1.00 18.15  ?  143 LYS A O     1 
ATOM   968  C  CB    . LYS A 1 142 ? 18.916  77.705  103.018 1.00 22.86  ?  143 LYS A CB    1 
ATOM   969  C  CG    . LYS A 1 142 ? 18.990  78.996  103.819 1.00 28.01  ?  143 LYS A CG    1 
ATOM   970  C  CD    . LYS A 1 142 ? 17.995  80.002  103.341 1.00 34.54  ?  143 LYS A CD    1 
ATOM   971  C  CE    . LYS A 1 142 ? 18.644  81.324  103.024 1.00 39.62  ?  143 LYS A CE    1 
ATOM   972  N  NZ    . LYS A 1 142 ? 17.650  82.356  102.634 1.00 43.06  1  143 LYS A NZ    1 
ATOM   973  N  N     . GLU A 1 143 ? 18.398  74.517  103.838 1.00 19.51  ?  144 GLU A N     1 
ATOM   974  C  CA    . GLU A 1 143 ? 17.735  73.304  103.391 1.00 20.86  ?  144 GLU A CA    1 
ATOM   975  C  C     . GLU A 1 143 ? 16.271  73.711  103.256 1.00 19.53  ?  144 GLU A C     1 
ATOM   976  O  O     . GLU A 1 143 ? 15.695  74.170  104.235 1.00 19.94  ?  144 GLU A O     1 
ATOM   977  C  CB    . GLU A 1 143 ? 17.865  72.155  104.404 1.00 25.86  ?  144 GLU A CB    1 
ATOM   978  C  CG    . GLU A 1 143 ? 19.158  72.181  105.194 1.00 37.12  ?  144 GLU A CG    1 
ATOM   979  C  CD    . GLU A 1 143 ? 19.426  70.938  106.020 1.00 50.30  ?  144 GLU A CD    1 
ATOM   980  O  OE1   . GLU A 1 143 ? 18.456  70.286  106.475 1.00 52.20  ?  144 GLU A OE1   1 
ATOM   981  O  OE2   . GLU A 1 143 ? 20.621  70.619  106.215 1.00 55.34  -1 144 GLU A OE2   1 
ATOM   982  N  N     . TYR A 1 144 ? 15.700  73.618  102.057 1.00 18.03  ?  145 TYR A N     1 
ATOM   983  C  CA    . TYR A 1 144 ? 14.301  73.942  101.848 1.00 18.22  ?  145 TYR A CA    1 
ATOM   984  C  C     . TYR A 1 144 ? 13.518  72.665  101.738 1.00 18.63  ?  145 TYR A C     1 
ATOM   985  O  O     . TYR A 1 144 ? 13.669  71.928  100.770 1.00 17.98  ?  145 TYR A O     1 
ATOM   986  C  CB    . TYR A 1 144 ? 14.102  74.748  100.576 1.00 18.17  ?  145 TYR A CB    1 
ATOM   987  C  CG    . TYR A 1 144 ? 14.653  76.147  100.660 1.00 19.63  ?  145 TYR A CG    1 
ATOM   988  C  CD1   . TYR A 1 144 ? 13.887  77.186  101.169 1.00 21.11  ?  145 TYR A CD1   1 
ATOM   989  C  CD2   . TYR A 1 144 ? 15.940  76.437  100.227 1.00 20.54  ?  145 TYR A CD2   1 
ATOM   990  C  CE1   . TYR A 1 144 ? 14.374  78.484  101.215 1.00 22.08  ?  145 TYR A CE1   1 
ATOM   991  C  CE2   . TYR A 1 144 ? 16.446  77.730  100.291 1.00 21.90  ?  145 TYR A CE2   1 
ATOM   992  C  CZ    . TYR A 1 144 ? 15.655  78.754  100.783 1.00 22.98  ?  145 TYR A CZ    1 
ATOM   993  O  OH    . TYR A 1 144 ? 16.111  80.049  100.830 1.00 24.91  ?  145 TYR A OH    1 
ATOM   994  N  N     . ASP A 1 145 ? 12.674  72.395  102.728 1.00 19.78  ?  146 ASP A N     1 
ATOM   995  C  CA    . ASP A 1 145 ? 11.826  71.221  102.699 1.00 20.39  ?  146 ASP A CA    1 
ATOM   996  C  C     . ASP A 1 145 ? 10.498  71.578  102.056 1.00 19.91  ?  146 ASP A C     1 
ATOM   997  O  O     . ASP A 1 145 ? 9.676   72.282  102.650 1.00 20.57  ?  146 ASP A O     1 
ATOM   998  C  CB    . ASP A 1 145 ? 11.614  70.673  104.104 1.00 24.17  ?  146 ASP A CB    1 
ATOM   999  C  CG    . ASP A 1 145 ? 10.965  69.305  104.151 1.00 32.99  ?  146 ASP A CG    1 
ATOM   1000 O  OD1   . ASP A 1 145 ? 9.901   69.127  103.521 1.00 34.04  ?  146 ASP A OD1   1 
ATOM   1001 O  OD2   . ASP A 1 145 ? 11.512  68.414  104.839 1.00 38.69  -1 146 ASP A OD2   1 
ATOM   1002 N  N     . TYR A 1 146 ? 10.275  71.073  100.849 1.00 18.77  ?  147 TYR A N     1 
ATOM   1003 C  CA    . TYR A 1 146 ? 9.010   71.261  100.171 1.00 18.28  ?  147 TYR A CA    1 
ATOM   1004 C  C     . TYR A 1 146 ? 8.293   69.921  100.047 1.00 18.15  ?  147 TYR A C     1 
ATOM   1005 O  O     . TYR A 1 146 ? 7.532   69.755  99.102  1.00 18.10  ?  147 TYR A O     1 
ATOM   1006 C  CB    . TYR A 1 146 ? 9.210   71.871  98.780  1.00 18.16  ?  147 TYR A CB    1 
ATOM   1007 C  CG    . TYR A 1 146 ? 9.989   73.160  98.735  1.00 18.75  ?  147 TYR A CG    1 
ATOM   1008 C  CD1   . TYR A 1 146 ? 9.553   74.283  99.427  1.00 19.21  ?  147 TYR A CD1   1 
ATOM   1009 C  CD2   . TYR A 1 146 ? 11.090  73.299  97.896  1.00 19.77  ?  147 TYR A CD2   1 
ATOM   1010 C  CE1   . TYR A 1 146 ? 10.228  75.492  99.338  1.00 20.23  ?  147 TYR A CE1   1 
ATOM   1011 C  CE2   . TYR A 1 146 ? 11.761  74.510  97.781  1.00 20.74  ?  147 TYR A CE2   1 
ATOM   1012 C  CZ    . TYR A 1 146 ? 11.326  75.605  98.506  1.00 21.78  ?  147 TYR A CZ    1 
ATOM   1013 O  OH    . TYR A 1 146 ? 11.964  76.815  98.377  1.00 24.43  ?  147 TYR A OH    1 
ATOM   1014 N  N     . LEU A 1 147 ? 8.508   68.956  100.970 1.00 18.39  ?  148 LEU A N     1 
ATOM   1015 C  CA    . LEU A 1 147 ? 7.773   67.675  100.881 1.00 19.15  ?  148 LEU A CA    1 
ATOM   1016 C  C     . LEU A 1 147 ? 6.253   67.877  101.044 1.00 19.77  ?  148 LEU A C     1 
ATOM   1017 O  O     . LEU A 1 147 ? 5.453   67.110  100.491 1.00 20.10  ?  148 LEU A O     1 
ATOM   1018 C  CB    . LEU A 1 147 ? 8.344   66.611  101.811 1.00 19.41  ?  148 LEU A CB    1 
ATOM   1019 C  CG    . LEU A 1 147 ? 9.772   66.209  101.465 1.00 20.28  ?  148 LEU A CG    1 
ATOM   1020 C  CD1   . LEU A 1 147 ? 10.350  65.270  102.518 1.00 20.61  ?  148 LEU A CD1   1 
ATOM   1021 C  CD2   . LEU A 1 147 ? 9.861   65.621  100.044 1.00 20.38  ?  148 LEU A CD2   1 
ATOM   1022 N  N     . THR A 1 148 ? 5.853   68.969  101.717 1.00 19.67  ?  149 THR A N     1 
ATOM   1023 C  CA    . THR A 1 148 ? 4.460   69.392  101.713 1.00 19.61  ?  149 THR A CA    1 
ATOM   1024 C  C     . THR A 1 148 ? 4.422   70.381  100.552 1.00 18.26  ?  149 THR A C     1 
ATOM   1025 O  O     . THR A 1 148 ? 5.210   71.318  100.524 1.00 17.70  ?  149 THR A O     1 
ATOM   1026 C  CB    . THR A 1 148 ? 4.058   70.040  103.012 1.00 20.77  ?  149 THR A CB    1 
ATOM   1027 O  OG1   . THR A 1 148 ? 4.146   69.055  104.037 1.00 21.82  ?  149 THR A OG1   1 
ATOM   1028 C  CG2   . THR A 1 148 ? 2.662   70.619  102.941 1.00 21.27  ?  149 THR A CG2   1 
ATOM   1029 N  N     . PRO A 1 149 ? 3.623   70.101  99.520  1.00 17.92  ?  150 PRO A N     1 
ATOM   1030 C  CA    . PRO A 1 149 ? 3.642   70.963  98.329  1.00 18.09  ?  150 PRO A CA    1 
ATOM   1031 C  C     . PRO A 1 149 ? 3.420   72.463  98.545  1.00 19.36  ?  150 PRO A C     1 
ATOM   1032 O  O     . PRO A 1 149 ? 2.589   72.903  99.330  1.00 19.79  ?  150 PRO A O     1 
ATOM   1033 C  CB    . PRO A 1 149 ? 2.545   70.378  97.422  1.00 17.94  ?  150 PRO A CB    1 
ATOM   1034 C  CG    . PRO A 1 149 ? 2.256   69.044  97.953  1.00 18.26  ?  150 PRO A CG    1 
ATOM   1035 C  CD    . PRO A 1 149 ? 2.685   68.970  99.378  1.00 16.84  ?  150 PRO A CD    1 
ATOM   1036 N  N     . LYS A 1 150 ? 4.151   73.236  97.757  1.00 19.89  ?  151 LYS A N     1 
ATOM   1037 C  CA    . LYS A 1 150 ? 4.082   74.681  97.652  1.00 20.21  ?  151 LYS A CA    1 
ATOM   1038 C  C     . LYS A 1 150 ? 2.714   75.072  97.036  1.00 20.78  ?  151 LYS A C     1 
ATOM   1039 O  O     . LYS A 1 150 ? 2.025   74.226  96.466  1.00 20.38  ?  151 LYS A O     1 
ATOM   1040 C  CB    . LYS A 1 150 ? 5.220   75.137  96.720  1.00 21.38  ?  151 LYS A CB    1 
ATOM   1041 C  CG    . LYS A 1 150 ? 6.597   74.985  97.314  1.00 25.67  ?  151 LYS A CG    1 
ATOM   1042 C  CD    . LYS A 1 150 ? 7.263   76.360  97.432  1.00 30.78  ?  151 LYS A CD    1 
ATOM   1043 C  CE    . LYS A 1 150 ? 7.973   76.750  96.170  1.00 33.76  ?  151 LYS A CE    1 
ATOM   1044 N  NZ    . LYS A 1 150 ? 8.664   75.573  95.575  1.00 36.10  1  151 LYS A NZ    1 
ATOM   1045 N  N     . PRO A 1 151 ? 2.315   76.365  97.093  1.00 20.99  ?  152 PRO A N     1 
ATOM   1046 C  CA    . PRO A 1 151 ? 1.032   76.770  96.490  1.00 19.99  ?  152 PRO A CA    1 
ATOM   1047 C  C     . PRO A 1 151 ? 0.875   76.410  95.007  1.00 18.51  ?  152 PRO A C     1 
ATOM   1048 O  O     . PRO A 1 151 ? -0.260  76.332  94.509  1.00 19.45  ?  152 PRO A O     1 
ATOM   1049 C  CB    . PRO A 1 151 ? 1.022   78.290  96.710  1.00 20.87  ?  152 PRO A CB    1 
ATOM   1050 C  CG    . PRO A 1 151 ? 1.832   78.474  97.975  1.00 21.71  ?  152 PRO A CG    1 
ATOM   1051 C  CD    . PRO A 1 151 ? 2.975   77.509  97.761  1.00 20.35  ?  152 PRO A CD    1 
ATOM   1052 N  N     . SER A 1 152 ? 1.982   76.186  94.300  1.00 15.86  ?  153 SER A N     1 
ATOM   1053 C  CA    . SER A 1 152 ? 1.909   75.781  92.897  1.00 14.32  ?  153 SER A CA    1 
ATOM   1054 C  C     . SER A 1 152 ? 1.560   74.272  92.739  1.00 13.26  ?  153 SER A C     1 
ATOM   1055 O  O     . SER A 1 152 ? 1.101   73.863  91.690  1.00 12.74  ?  153 SER A O     1 
ATOM   1056 C  CB    . SER A 1 152 ? 3.248   76.036  92.209  1.00 14.70  ?  153 SER A CB    1 
ATOM   1057 O  OG    . SER A 1 152 ? 4.274   75.207  92.742  1.00 16.39  ?  153 SER A OG    1 
ATOM   1058 N  N     . GLY A 1 153 ? 1.869   73.475  93.754  1.00 13.19  ?  154 GLY A N     1 
ATOM   1059 C  CA    . GLY A 1 153 ? 1.768   72.020  93.767  1.00 13.43  ?  154 GLY A CA    1 
ATOM   1060 C  C     . GLY A 1 153 ? 3.139   71.354  93.766  1.00 13.30  ?  154 GLY A C     1 
ATOM   1061 O  O     . GLY A 1 153 ? 3.248   70.121  93.815  1.00 12.76  ?  154 GLY A O     1 
ATOM   1062 N  N     . TYR A 1 154 ? 4.204   72.168  93.680  1.00 13.75  ?  155 TYR A N     1 
ATOM   1063 C  CA    . TYR A 1 154 ? 5.583   71.702  93.637  1.00 15.03  ?  155 TYR A CA    1 
ATOM   1064 C  C     . TYR A 1 154 ? 6.032   71.079  94.944  1.00 15.89  ?  155 TYR A C     1 
ATOM   1065 O  O     . TYR A 1 154 ? 5.822   71.660  96.022  1.00 16.72  ?  155 TYR A O     1 
ATOM   1066 C  CB    . TYR A 1 154 ? 6.534   72.852  93.232  1.00 15.10  ?  155 TYR A CB    1 
ATOM   1067 C  CG    . TYR A 1 154 ? 7.972   72.419  93.088  1.00 15.78  ?  155 TYR A CG    1 
ATOM   1068 C  CD1   . TYR A 1 154 ? 8.438   71.872  91.903  1.00 16.98  ?  155 TYR A CD1   1 
ATOM   1069 C  CD2   . TYR A 1 154 ? 8.858   72.509  94.155  1.00 16.80  ?  155 TYR A CD2   1 
ATOM   1070 C  CE1   . TYR A 1 154 ? 9.744   71.414  91.784  1.00 18.06  ?  155 TYR A CE1   1 
ATOM   1071 C  CE2   . TYR A 1 154 ? 10.160  72.045  94.054  1.00 17.81  ?  155 TYR A CE2   1 
ATOM   1072 C  CZ    . TYR A 1 154 ? 10.613  71.532  92.854  1.00 19.23  ?  155 TYR A CZ    1 
ATOM   1073 O  OH    . TYR A 1 154 ? 11.915  71.121  92.737  1.00 21.21  ?  155 TYR A OH    1 
ATOM   1074 N  N     . SER A 1 155 ? 6.632   69.887  94.852  1.00 15.46  ?  156 SER A N     1 
ATOM   1075 C  CA    . SER A 1 155 ? 7.188   69.230  96.020  1.00 16.02  ?  156 SER A CA    1 
ATOM   1076 C  C     . SER A 1 155 ? 8.555   68.592  95.695  1.00 16.80  ?  156 SER A C     1 
ATOM   1077 O  O     . SER A 1 155 ? 8.836   68.209  94.551  1.00 17.11  ?  156 SER A O     1 
ATOM   1078 C  CB    . SER A 1 155 ? 6.196   68.271  96.692  1.00 17.03  ?  156 SER A CB    1 
ATOM   1079 O  OG    . SER A 1 155 ? 5.983   67.040  96.022  1.00 19.81  ?  156 SER A OG    1 
ATOM   1080 N  N     . GLY A 1 156 ? 9.415   68.561  96.705  1.00 16.54  ?  157 GLY A N     1 
ATOM   1081 C  CA    . GLY A 1 156 ? 10.780  68.063  96.627  1.00 16.15  ?  157 GLY A CA    1 
ATOM   1082 C  C     . GLY A 1 156 ? 11.651  68.738  97.668  1.00 15.76  ?  157 GLY A C     1 
ATOM   1083 O  O     . GLY A 1 156 ? 11.142  69.277  98.654  1.00 15.48  ?  157 GLY A O     1 
ATOM   1084 N  N     . ILE A 1 157 ? 12.977  68.685  97.501  1.00 15.54  ?  158 ILE A N     1 
ATOM   1085 C  CA    . ILE A 1 157 ? 13.898  69.290  98.479  1.00 15.21  ?  158 ILE A CA    1 
ATOM   1086 C  C     . ILE A 1 157 ? 14.949  70.105  97.766  1.00 14.05  ?  158 ILE A C     1 
ATOM   1087 O  O     . ILE A 1 157 ? 15.535  69.597  96.832  1.00 13.54  ?  158 ILE A O     1 
ATOM   1088 C  CB    . ILE A 1 157 ? 14.537  68.195  99.373  1.00 16.49  ?  158 ILE A CB    1 
ATOM   1089 C  CG1   . ILE A 1 157 ? 13.518  67.676  100.394 1.00 18.34  ?  158 ILE A CG1   1 
ATOM   1090 C  CG2   . ILE A 1 157 ? 15.811  68.708  100.086 1.00 17.62  ?  158 ILE A CG2   1 
ATOM   1091 C  CD1   . ILE A 1 157 ? 14.014  66.668  101.436 1.00 20.14  ?  158 ILE A CD1   1 
ATOM   1092 N  N     . HIS A 1 158 ? 15.211  71.348  98.198  1.00 13.77  ?  159 HIS A N     1 
ATOM   1093 C  CA    . HIS A 1 158 ? 16.289  72.148  97.616  1.00 13.50  ?  159 HIS A CA    1 
ATOM   1094 C  C     . HIS A 1 158 ? 17.384  72.387  98.642  1.00 13.95  ?  159 HIS A C     1 
ATOM   1095 O  O     . HIS A 1 158 ? 17.100  72.617  99.815  1.00 14.80  ?  159 HIS A O     1 
ATOM   1096 C  CB    . HIS A 1 158 ? 15.774  73.469  97.036  1.00 14.21  ?  159 HIS A CB    1 
ATOM   1097 C  CG    . HIS A 1 158 ? 14.812  73.307  95.883  1.00 16.46  ?  159 HIS A CG    1 
ATOM   1098 N  ND1   . HIS A 1 158 ? 14.336  74.411  95.175  1.00 18.35  ?  159 HIS A ND1   1 
ATOM   1099 C  CD2   . HIS A 1 158 ? 14.262  72.184  95.350  1.00 16.98  ?  159 HIS A CD2   1 
ATOM   1100 C  CE1   . HIS A 1 158 ? 13.536  73.925  94.240  1.00 18.14  ?  159 HIS A CE1   1 
ATOM   1101 N  NE2   . HIS A 1 158 ? 13.431  72.592  94.327  1.00 17.87  ?  159 HIS A NE2   1 
ATOM   1102 N  N     . LEU A 1 159 ? 18.639  72.258  98.229  1.00 13.55  ?  160 LEU A N     1 
ATOM   1103 C  CA    . LEU A 1 159 ? 19.792  72.500  99.082  1.00 13.53  ?  160 LEU A CA    1 
ATOM   1104 C  C     . LEU A 1 159 ? 20.491  73.702  98.499  1.00 14.09  ?  160 LEU A C     1 
ATOM   1105 O  O     . LEU A 1 159 ? 20.834  73.690  97.318  1.00 14.50  ?  160 LEU A O     1 
ATOM   1106 C  CB    . LEU A 1 159 ? 20.742  71.282  99.101  1.00 13.35  ?  160 LEU A CB    1 
ATOM   1107 C  CG    . LEU A 1 159 ? 20.115  69.985  99.622  1.00 14.00  ?  160 LEU A CG    1 
ATOM   1108 C  CD1   . LEU A 1 159 ? 21.070  68.840  99.526  1.00 13.07  ?  160 LEU A CD1   1 
ATOM   1109 C  CD2   . LEU A 1 159 ? 19.587  70.159  101.055 1.00 14.95  ?  160 LEU A CD2   1 
ATOM   1110 N  N     . ALA A 1 160 ? 20.633  74.767  99.279  1.00 13.92  ?  161 ALA A N     1 
ATOM   1111 C  CA    . ALA A 1 160 ? 21.313  75.957  98.797  1.00 14.22  ?  161 ALA A CA    1 
ATOM   1112 C  C     . ALA A 1 160 ? 22.764  75.908  99.257  1.00 14.43  ?  161 ALA A C     1 
ATOM   1113 O  O     . ALA A 1 160 ? 23.042  76.139  100.420 1.00 15.11  ?  161 ALA A O     1 
ATOM   1114 C  CB    . ALA A 1 160 ? 20.626  77.209  99.305  1.00 14.42  ?  161 ALA A CB    1 
ATOM   1115 N  N     . TYR A 1 161 ? 23.682  75.601  98.351  1.00 13.72  ?  162 TYR A N     1 
ATOM   1116 C  CA    . TYR A 1 161 ? 25.106  75.535  98.668  1.00 13.44  ?  162 TYR A CA    1 
ATOM   1117 C  C     . TYR A 1 161 ? 25.811  76.830  98.431  1.00 13.01  ?  162 TYR A C     1 
ATOM   1118 O  O     . TYR A 1 161 ? 25.505  77.535  97.485  1.00 13.05  ?  162 TYR A O     1 
ATOM   1119 C  CB    . TYR A 1 161 ? 25.825  74.493  97.786  1.00 13.02  ?  162 TYR A CB    1 
ATOM   1120 C  CG    . TYR A 1 161 ? 25.646  73.061  98.224  1.00 14.00  ?  162 TYR A CG    1 
ATOM   1121 C  CD1   . TYR A 1 161 ? 24.529  72.334  97.845  1.00 14.51  ?  162 TYR A CD1   1 
ATOM   1122 C  CD2   . TYR A 1 161 ? 26.624  72.410  98.963  1.00 15.04  ?  162 TYR A CD2   1 
ATOM   1123 C  CE1   . TYR A 1 161 ? 24.365  71.013  98.226  1.00 15.16  ?  162 TYR A CE1   1 
ATOM   1124 C  CE2   . TYR A 1 161 ? 26.466  71.089  99.359  1.00 15.94  ?  162 TYR A CE2   1 
ATOM   1125 C  CZ    . TYR A 1 161 ? 25.343  70.385  98.964  1.00 16.41  ?  162 TYR A CZ    1 
ATOM   1126 O  OH    . TYR A 1 161 ? 25.171  69.061  99.307  1.00 17.77  ?  162 TYR A OH    1 
ATOM   1127 N  N     . SER A 1 162 ? 26.850  77.071  99.225  1.00 13.11  ?  163 SER A N     1 
ATOM   1128 C  CA    . SER A 1 162 ? 27.834  78.129  99.082  1.00 13.30  ?  163 SER A CA    1 
ATOM   1129 C  C     . SER A 1 162 ? 29.170  77.368  98.910  1.00 13.39  ?  163 SER A C     1 
ATOM   1130 O  O     . SER A 1 162 ? 29.655  76.760  99.853  1.00 12.95  ?  163 SER A O     1 
ATOM   1131 C  CB    . SER A 1 162 ? 27.876  78.998  100.329 1.00 14.39  ?  163 SER A CB    1 
ATOM   1132 O  OG    . SER A 1 162 ? 28.753  80.096  100.138 1.00 15.77  ?  163 SER A OG    1 
ATOM   1133 N  N     . CYS A 1 163 ? 29.689  77.308  97.688  1.00 14.19  ?  164 CYS A N     1 
ATOM   1134 C  CA    . CYS A 1 163 ? 30.930  76.605  97.355  1.00 16.14  ?  164 CYS A CA    1 
ATOM   1135 C  C     . CYS A 1 163 ? 32.116  77.407  97.846  1.00 17.43  ?  164 CYS A C     1 
ATOM   1136 O  O     . CYS A 1 163 ? 32.082  78.629  97.772  1.00 17.26  ?  164 CYS A O     1 
ATOM   1137 C  CB    . CYS A 1 163 ? 31.020  76.344  95.853  1.00 17.39  ?  164 CYS A CB    1 
ATOM   1138 S  SG    . CYS A 1 163 ? 29.667  75.333  95.184  1.00 21.75  ?  164 CYS A SG    1 
ATOM   1139 N  N     . PHE A 1 164 ? 33.162  76.738  98.400  1.00 18.31  ?  165 PHE A N     1 
ATOM   1140 C  CA    . PHE A 1 164 ? 34.358  77.386  98.975  1.00 19.30  ?  165 PHE A CA    1 
ATOM   1141 C  C     . PHE A 1 164 ? 33.940  78.496  99.940  1.00 20.55  ?  165 PHE A C     1 
ATOM   1142 O  O     . PHE A 1 164 ? 34.356  79.646  99.814  1.00 20.05  ?  165 PHE A O     1 
ATOM   1143 C  CB    . PHE A 1 164 ? 35.320  77.885  97.876  1.00 19.01  ?  165 PHE A CB    1 
ATOM   1144 C  CG    . PHE A 1 164 ? 35.773  76.781  96.942  1.00 18.96  ?  165 PHE A CG    1 
ATOM   1145 C  CD1   . PHE A 1 164 ? 36.540  75.726  97.408  1.00 19.55  ?  165 PHE A CD1   1 
ATOM   1146 C  CD2   . PHE A 1 164 ? 35.392  76.776  95.611  1.00 19.27  ?  165 PHE A CD2   1 
ATOM   1147 C  CE1   . PHE A 1 164 ? 36.940  74.700  96.550  1.00 20.07  ?  165 PHE A CE1   1 
ATOM   1148 C  CE2   . PHE A 1 164 ? 35.787  75.749  94.759  1.00 19.95  ?  165 PHE A CE2   1 
ATOM   1149 C  CZ    . PHE A 1 164 ? 36.586  74.734  95.226  1.00 19.72  ?  165 PHE A CZ    1 
ATOM   1150 N  N     . ASP A 1 165 ? 33.002  78.145  100.821 1.00 22.21  ?  166 ASP A N     1 
ATOM   1151 C  CA    . ASP A 1 165 ? 32.341  79.050  101.751 1.00 24.89  ?  166 ASP A CA    1 
ATOM   1152 C  C     . ASP A 1 165 ? 33.264  79.783  102.749 1.00 28.18  ?  166 ASP A C     1 
ATOM   1153 O  O     . ASP A 1 165 ? 33.269  81.020  102.780 1.00 28.30  ?  166 ASP A O     1 
ATOM   1154 C  CB    . ASP A 1 165 ? 31.238  78.296  102.495 1.00 26.46  ?  166 ASP A CB    1 
ATOM   1155 C  CG    . ASP A 1 165 ? 30.275  79.222  103.195 1.00 32.27  ?  166 ASP A CG    1 
ATOM   1156 O  OD1   . ASP A 1 165 ? 29.790  80.178  102.540 1.00 32.98  ?  166 ASP A OD1   1 
ATOM   1157 O  OD2   . ASP A 1 165 ? 30.005  78.998  104.403 1.00 34.96  -1 166 ASP A OD2   1 
ATOM   1158 N  N     . GLU A 1 166 ? 34.051  79.025  103.543 1.00 30.27  ?  167 GLU A N     1 
ATOM   1159 C  CA    . GLU A 1 166 ? 34.918  79.570  104.578 1.00 32.49  ?  167 GLU A CA    1 
ATOM   1160 C  C     . GLU A 1 166 ? 36.389  79.454  104.255 1.00 33.88  ?  167 GLU A C     1 
ATOM   1161 O  O     . GLU A 1 166 ? 37.167  80.286  104.700 1.00 32.95  ?  167 GLU A O     1 
ATOM   1162 C  CB    . GLU A 1 166 ? 34.623  78.870  105.908 1.00 35.88  ?  167 GLU A CB    1 
ATOM   1163 C  CG    . GLU A 1 166 ? 33.163  78.953  106.312 1.00 42.04  ?  167 GLU A CG    1 
ATOM   1164 C  CD    . GLU A 1 166 ? 32.776  78.091  107.499 1.00 50.63  ?  167 GLU A CD    1 
ATOM   1165 O  OE1   . GLU A 1 166 ? 33.569  77.192  107.869 1.00 52.39  ?  167 GLU A OE1   1 
ATOM   1166 O  OE2   . GLU A 1 166 ? 31.680  78.319  108.062 1.00 53.69  -1 167 GLU A OE2   1 
ATOM   1167 N  N     . GLU A 1 167 ? 36.778  78.396  103.524 1.00 36.07  ?  168 GLU A N     1 
ATOM   1168 C  CA    . GLU A 1 167 ? 38.167  78.140  103.110 1.00 38.59  ?  168 GLU A CA    1 
ATOM   1169 C  C     . GLU A 1 167 ? 38.347  78.690  101.718 1.00 41.31  ?  168 GLU A C     1 
ATOM   1170 O  O     . GLU A 1 167 ? 37.813  78.156  100.750 1.00 41.19  ?  168 GLU A O     1 
ATOM   1171 C  CB    . GLU A 1 167 ? 38.492  76.652  103.175 1.00 40.28  ?  168 GLU A CB    1 
ATOM   1172 C  CG    . GLU A 1 167 ? 38.524  76.166  104.603 1.00 44.46  ?  168 GLU A CG    1 
ATOM   1173 C  CD    . GLU A 1 167 ? 38.839  74.697  104.781 1.00 50.57  ?  168 GLU A CD    1 
ATOM   1174 O  OE1   . GLU A 1 167 ? 39.733  74.192  104.066 1.00 52.55  ?  168 GLU A OE1   1 
ATOM   1175 O  OE2   . GLU A 1 167 ? 38.205  74.055  105.650 1.00 52.18  -1 168 GLU A OE2   1 
ATOM   1176 N  N     . ASN A 1 168 ? 39.053  79.816  101.641 1.00 43.95  ?  169 ASN A N     1 
ATOM   1177 C  CA    . ASN A 1 168 ? 39.194  80.625  100.435 1.00 45.87  ?  169 ASN A CA    1 
ATOM   1178 C  C     . ASN A 1 168 ? 40.672  80.933  100.021 1.00 46.39  ?  169 ASN A C     1 
ATOM   1179 O  O     . ASN A 1 168 ? 41.245  80.182  99.227  1.00 47.02  ?  169 ASN A O     1 
ATOM   1180 C  CB    . ASN A 1 168 ? 38.337  81.924  100.593 1.00 48.15  ?  169 ASN A CB    1 
ATOM   1181 C  CG    . ASN A 1 168 ? 38.631  82.812  101.811 1.00 53.24  ?  169 ASN A CG    1 
ATOM   1182 O  OD1   . ASN A 1 168 ? 38.572  84.053  101.720 1.00 55.97  ?  169 ASN A OD1   1 
ATOM   1183 N  ND2   . ASN A 1 168 ? 38.938  82.226  102.977 1.00 52.81  ?  169 ASN A ND2   1 
ATOM   1184 N  N     . GLY A 1 169 ? 41.265  82.000  100.561 1.00 45.71  ?  170 GLY A N     1 
ATOM   1185 C  CA    . GLY A 1 169 ? 42.597  82.443  100.193 1.00 45.17  ?  170 GLY A CA    1 
ATOM   1186 C  C     . GLY A 1 169 ? 42.519  83.259  98.921  1.00 44.00  ?  170 GLY A C     1 
ATOM   1187 O  O     . GLY A 1 169 ? 41.842  84.291  98.877  1.00 44.20  ?  170 GLY A O     1 
ATOM   1188 N  N     . ASN A 1 170 ? 43.182  82.772  97.870  1.00 42.70  ?  171 ASN A N     1 
ATOM   1189 C  CA    . ASN A 1 170 ? 43.217  83.381  96.537  1.00 41.84  ?  171 ASN A CA    1 
ATOM   1190 C  C     . ASN A 1 170 ? 42.271  82.603  95.587  1.00 38.66  ?  171 ASN A C     1 
ATOM   1191 O  O     . ASN A 1 170 ? 42.578  82.456  94.399  1.00 39.11  ?  171 ASN A O     1 
ATOM   1192 C  CB    . ASN A 1 170 ? 44.656  83.318  95.967  1.00 45.00  ?  171 ASN A CB    1 
ATOM   1193 C  CG    . ASN A 1 170 ? 45.672  84.208  96.652  1.00 51.04  ?  171 ASN A CG    1 
ATOM   1194 O  OD1   . ASN A 1 170 ? 45.331  85.156  97.365  1.00 53.21  ?  171 ASN A OD1   1 
ATOM   1195 N  ND2   . ASN A 1 170 ? 46.951  83.933  96.428  1.00 52.34  ?  171 ASN A ND2   1 
ATOM   1196 N  N     . ASN A 1 171 ? 41.152  82.078  96.114  1.00 35.00  ?  172 ASN A N     1 
ATOM   1197 C  CA    . ASN A 1 171 ? 40.216  81.290  95.327  1.00 31.78  ?  172 ASN A CA    1 
ATOM   1198 C  C     . ASN A 1 171 ? 39.166  82.184  94.692  1.00 29.26  ?  172 ASN A C     1 
ATOM   1199 O  O     . ASN A 1 171 ? 38.365  82.782  95.413  1.00 29.89  ?  172 ASN A O     1 
ATOM   1200 C  CB    . ASN A 1 171 ? 39.546  80.234  96.222  1.00 31.20  ?  172 ASN A CB    1 
ATOM   1201 C  CG    . ASN A 1 171 ? 38.892  79.094  95.472  1.00 31.10  ?  172 ASN A CG    1 
ATOM   1202 O  OD1   . ASN A 1 171 ? 38.445  79.240  94.346  1.00 31.67  ?  172 ASN A OD1   1 
ATOM   1203 N  ND2   . ASN A 1 171 ? 38.831  77.925  96.073  1.00 30.83  ?  172 ASN A ND2   1 
ATOM   1204 N  N     . PRO A 1 172 ? 39.119  82.258  93.343  1.00 26.25  ?  173 PRO A N     1 
ATOM   1205 C  CA    . PRO A 1 172 ? 38.077  83.074  92.685  1.00 24.32  ?  173 PRO A CA    1 
ATOM   1206 C  C     . PRO A 1 172 ? 36.656  82.516  92.836  1.00 21.69  ?  173 PRO A C     1 
ATOM   1207 O  O     . PRO A 1 172 ? 35.688  83.240  92.622  1.00 21.27  ?  173 PRO A O     1 
ATOM   1208 C  CB    . PRO A 1 172 ? 38.496  83.049  91.221  1.00 25.20  ?  173 PRO A CB    1 
ATOM   1209 C  CG    . PRO A 1 172 ? 39.232  81.759  91.078  1.00 25.98  ?  173 PRO A CG    1 
ATOM   1210 C  CD    . PRO A 1 172 ? 39.976  81.576  92.356  1.00 25.01  ?  173 PRO A CD    1 
ATOM   1211 N  N     . TRP A 1 173 ? 36.528  81.243  93.230  1.00 19.71  ?  174 TRP A N     1 
ATOM   1212 C  CA    . TRP A 1 173 ? 35.229  80.611  93.372  1.00 18.56  ?  174 TRP A CA    1 
ATOM   1213 C  C     . TRP A 1 173 ? 34.641  80.671  94.783  1.00 19.29  ?  174 TRP A C     1 
ATOM   1214 O  O     . TRP A 1 173 ? 33.587  80.080  95.020  1.00 19.61  ?  174 TRP A O     1 
ATOM   1215 C  CB    . TRP A 1 173 ? 35.306  79.172  92.857  1.00 17.29  ?  174 TRP A CB    1 
ATOM   1216 C  CG    . TRP A 1 173 ? 35.608  79.122  91.390  1.00 15.87  ?  174 TRP A CG    1 
ATOM   1217 C  CD1   . TRP A 1 173 ? 34.825  79.591  90.381  1.00 15.94  ?  174 TRP A CD1   1 
ATOM   1218 C  CD2   . TRP A 1 173 ? 36.823  78.675  90.782  1.00 15.71  ?  174 TRP A CD2   1 
ATOM   1219 N  NE1   . TRP A 1 173 ? 35.459  79.432  89.178  1.00 16.00  ?  174 TRP A NE1   1 
ATOM   1220 C  CE2   . TRP A 1 173 ? 36.691  78.869  89.393  1.00 15.99  ?  174 TRP A CE2   1 
ATOM   1221 C  CE3   . TRP A 1 173 ? 38.008  78.099  91.275  1.00 16.04  ?  174 TRP A CE3   1 
ATOM   1222 C  CZ2   . TRP A 1 173 ? 37.675  78.466  88.485  1.00 16.37  ?  174 TRP A CZ2   1 
ATOM   1223 C  CZ3   . TRP A 1 173 ? 38.991  77.731  90.376  1.00 16.50  ?  174 TRP A CZ3   1 
ATOM   1224 C  CH2   . TRP A 1 173 ? 38.806  77.887  88.998  1.00 16.52  ?  174 TRP A CH2   1 
ATOM   1225 N  N     . SER A 1 174 ? 35.282  81.406  95.704  1.00 19.54  ?  175 SER A N     1 
ATOM   1226 C  CA    . SER A 1 174 ? 34.813  81.579  97.085  1.00 20.41  ?  175 SER A CA    1 
ATOM   1227 C  C     . SER A 1 174 ? 33.374  82.062  97.144  1.00 20.48  ?  175 SER A C     1 
ATOM   1228 O  O     . SER A 1 174 ? 33.005  82.972  96.397  1.00 20.92  ?  175 SER A O     1 
ATOM   1229 C  CB    . SER A 1 174 ? 35.693  82.572  97.838  1.00 22.01  ?  175 SER A CB    1 
ATOM   1230 O  OG    . SER A 1 174 ? 37.046  82.187  97.675  1.00 25.93  ?  175 SER A OG    1 
ATOM   1231 N  N     . LYS A 1 175 ? 32.579  81.445  98.026  1.00 19.68  ?  176 LYS A N     1 
ATOM   1232 C  CA    . LYS A 1 175 ? 31.172  81.740  98.258  1.00 19.77  ?  176 LYS A CA    1 
ATOM   1233 C  C     . LYS A 1 175 ? 30.302  81.753  96.984  1.00 19.10  ?  176 LYS A C     1 
ATOM   1234 O  O     . LYS A 1 175 ? 29.416  82.595  96.868  1.00 19.52  ?  176 LYS A O     1 
ATOM   1235 C  CB    . LYS A 1 175 ? 31.008  83.034  99.053  1.00 22.10  ?  176 LYS A CB    1 
ATOM   1236 C  CG    . LYS A 1 175 ? 31.579  82.939  100.461 1.00 25.90  ?  176 LYS A CG    1 
ATOM   1237 C  CD    . LYS A 1 175 ? 31.374  84.232  101.228 1.00 28.28  ?  176 LYS A CD    1 
ATOM   1238 C  CE    . LYS A 1 175 ? 31.853  84.085  102.642 1.00 31.17  ?  176 LYS A CE    1 
ATOM   1239 N  NZ    . LYS A 1 175 ? 30.992  83.165  103.423 1.00 31.74  1  176 LYS A NZ    1 
ATOM   1240 N  N     . THR A 1 176 ? 30.553  80.824  96.042  1.00 18.05  ?  177 THR A N     1 
ATOM   1241 C  CA    . THR A 1 176 ? 29.773  80.690  94.809  1.00 17.31  ?  177 THR A CA    1 
ATOM   1242 C  C     . THR A 1 176 ? 28.495  79.900  95.126  1.00 15.31  ?  177 THR A C     1 
ATOM   1243 O  O     . THR A 1 176 ? 28.571  78.790  95.628  1.00 14.56  ?  177 THR A O     1 
ATOM   1244 C  CB    . THR A 1 176 ? 30.602  80.001  93.691  1.00 19.25  ?  177 THR A CB    1 
ATOM   1245 O  OG1   . THR A 1 176 ? 31.534  80.948  93.179  1.00 21.04  ?  177 THR A OG1   1 
ATOM   1246 C  CG2   . THR A 1 176 ? 29.729  79.560  92.524  1.00 19.66  ?  177 THR A CG2   1 
ATOM   1247 N  N     . LYS A 1 177 ? 27.335  80.453  94.814  1.00 14.55  ?  178 LYS A N     1 
ATOM   1248 C  CA    . LYS A 1 177 ? 26.062  79.799  95.123  1.00 13.56  ?  178 LYS A CA    1 
ATOM   1249 C  C     . LYS A 1 177 ? 25.594  78.819  94.043  1.00 11.89  ?  178 LYS A C     1 
ATOM   1250 O  O     . LYS A 1 177 ? 25.474  79.187  92.892  1.00 11.81  ?  178 LYS A O     1 
ATOM   1251 C  CB    . LYS A 1 177 ? 25.008  80.854  95.455  1.00 14.52  ?  178 LYS A CB    1 
ATOM   1252 C  CG    . LYS A 1 177 ? 25.334  81.554  96.764  1.00 18.80  ?  178 LYS A CG    1 
ATOM   1253 C  CD    . LYS A 1 177 ? 24.659  82.929  96.874  1.00 25.47  ?  178 LYS A CD    1 
ATOM   1254 C  CE    . LYS A 1 177 ? 24.256  83.265  98.281  1.00 30.03  ?  178 LYS A CE    1 
ATOM   1255 N  NZ    . LYS A 1 177 ? 22.967  82.604  98.629  1.00 34.16  1  178 LYS A NZ    1 
ATOM   1256 N  N     . ILE A 1 178 ? 25.350  77.559  94.427  1.00 10.67  ?  179 ILE A N     1 
ATOM   1257 C  CA    . ILE A 1 178 ? 24.881  76.497  93.543  1.00 10.17  ?  179 ILE A CA    1 
ATOM   1258 C  C     . ILE A 1 178 ? 23.681  75.838  94.214  1.00 11.00  ?  179 ILE A C     1 
ATOM   1259 O  O     . ILE A 1 178 ? 23.726  75.550  95.411  1.00 11.11  ?  179 ILE A O     1 
ATOM   1260 C  CB    . ILE A 1 178 ? 25.996  75.444  93.215  1.00 9.88   ?  179 ILE A CB    1 
ATOM   1261 C  CG1   . ILE A 1 178 ? 27.224  76.094  92.506  1.00 10.01  ?  179 ILE A CG1   1 
ATOM   1262 C  CG2   . ILE A 1 178 ? 25.437  74.252  92.392  1.00 9.72   ?  179 ILE A CG2   1 
ATOM   1263 C  CD1   . ILE A 1 178 ? 26.950  76.630  91.123  1.00 9.91   ?  179 ILE A CD1   1 
ATOM   1264 N  N     . GLU A 1 179 ? 22.601  75.619  93.462  1.00 11.26  ?  180 GLU A N     1 
ATOM   1265 C  CA    . GLU A 1 179 ? 21.404  75.001  94.015  1.00 12.56  ?  180 GLU A CA    1 
ATOM   1266 C  C     . GLU A 1 179 ? 21.352  73.517  93.705  1.00 13.65  ?  180 GLU A C     1 
ATOM   1267 O  O     . GLU A 1 179 ? 21.658  73.128  92.591  1.00 14.39  ?  180 GLU A O     1 
ATOM   1268 C  CB    . GLU A 1 179 ? 20.137  75.690  93.473  1.00 14.79  ?  180 GLU A CB    1 
ATOM   1269 C  CG    . GLU A 1 179 ? 18.850  75.128  94.077  1.00 20.84  ?  180 GLU A CG    1 
ATOM   1270 C  CD    . GLU A 1 179 ? 17.579  75.636  93.422  1.00 29.50  ?  180 GLU A CD    1 
ATOM   1271 O  OE1   . GLU A 1 179 ? 17.207  75.091  92.358  1.00 31.19  ?  180 GLU A OE1   1 
ATOM   1272 O  OE2   . GLU A 1 179 ? 16.971  76.595  93.952  1.00 32.50  -1 180 GLU A OE2   1 
ATOM   1273 N  N     . VAL A 1 180 ? 20.981  72.682  94.678  1.00 13.46  ?  181 VAL A N     1 
ATOM   1274 C  CA    . VAL A 1 180 ? 20.829  71.256  94.448  1.00 13.61  ?  181 VAL A CA    1 
ATOM   1275 C  C     . VAL A 1 180 ? 19.368  70.838  94.654  1.00 13.02  ?  181 VAL A C     1 
ATOM   1276 O  O     . VAL A 1 180 ? 18.850  70.976  95.754  1.00 14.06  ?  181 VAL A O     1 
ATOM   1277 C  CB    . VAL A 1 180 ? 21.826  70.419  95.293  1.00 14.71  ?  181 VAL A CB    1 
ATOM   1278 C  CG1   . VAL A 1 180 ? 21.453  68.935  95.266  1.00 15.79  ?  181 VAL A CG1   1 
ATOM   1279 C  CG2   . VAL A 1 180 ? 23.250  70.632  94.807  1.00 14.65  ?  181 VAL A CG2   1 
ATOM   1280 N  N     . GLN A 1 181 ? 18.693  70.352  93.611  1.00 11.49  ?  182 GLN A N     1 
ATOM   1281 C  CA    . GLN A 1 181 ? 17.295  69.921  93.720  1.00 10.80  ?  182 GLN A CA    1 
ATOM   1282 C  C     . GLN A 1 181 ? 17.207  68.390  93.831  1.00 11.40  ?  182 GLN A C     1 
ATOM   1283 O  O     . GLN A 1 181 ? 17.849  67.681  93.065  1.00 11.39  ?  182 GLN A O     1 
ATOM   1284 C  CB    . GLN A 1 181 ? 16.490  70.382  92.494  1.00 11.15  ?  182 GLN A CB    1 
ATOM   1285 C  CG    . GLN A 1 181 ? 16.213  71.881  92.439  1.00 11.48  ?  182 GLN A CG    1 
ATOM   1286 C  CD    . GLN A 1 181 ? 15.514  72.322  91.159  1.00 11.15  ?  182 GLN A CD    1 
ATOM   1287 O  OE1   . GLN A 1 181 ? 15.280  71.533  90.244  1.00 12.42  ?  182 GLN A OE1   1 
ATOM   1288 N  NE2   . GLN A 1 181 ? 15.222  73.612  91.027  1.00 7.47   ?  182 GLN A NE2   1 
ATOM   1289 N  N     . LEU A 1 182 ? 16.433  67.882  94.799  1.00 11.97  ?  183 LEU A N     1 
ATOM   1290 C  CA    . LEU A 1 182 ? 16.217  66.446  95.024  1.00 12.75  ?  183 LEU A CA    1 
ATOM   1291 C  C     . LEU A 1 182 ? 14.764  66.157  94.777  1.00 12.89  ?  183 LEU A C     1 
ATOM   1292 O  O     . LEU A 1 182 ? 13.907  66.822  95.348  1.00 13.00  ?  183 LEU A O     1 
ATOM   1293 C  CB    . LEU A 1 182 ? 16.617  66.032  96.443  1.00 13.37  ?  183 LEU A CB    1 
ATOM   1294 C  CG    . LEU A 1 182 ? 18.095  66.278  96.800  1.00 15.47  ?  183 LEU A CG    1 
ATOM   1295 C  CD1   . LEU A 1 182 ? 18.387  65.871  98.228  1.00 15.79  ?  183 LEU A CD1   1 
ATOM   1296 C  CD2   . LEU A 1 182 ? 19.034  65.508  95.847  1.00 16.66  ?  183 LEU A CD2   1 
ATOM   1297 N  N     . ARG A 1 183 ? 14.474  65.215  93.877  1.00 13.23  ?  184 ARG A N     1 
ATOM   1298 C  CA    . ARG A 1 183 ? 13.099  64.898  93.466  1.00 13.44  ?  184 ARG A CA    1 
ATOM   1299 C  C     . ARG A 1 183 ? 12.928  63.417  93.222  1.00 13.00  ?  184 ARG A C     1 
ATOM   1300 O  O     . ARG A 1 183 ? 13.854  62.802  92.726  1.00 12.85  ?  184 ARG A O     1 
ATOM   1301 C  CB    . ARG A 1 183 ? 12.862  65.495  92.083  1.00 14.79  ?  184 ARG A CB    1 
ATOM   1302 C  CG    . ARG A 1 183 ? 12.125  66.751  92.094  1.00 19.65  ?  184 ARG A CG    1 
ATOM   1303 C  CD    . ARG A 1 183 ? 12.983  67.703  91.307  1.00 21.87  ?  184 ARG A CD    1 
ATOM   1304 N  NE    . ARG A 1 183 ? 12.557  67.751  89.916  1.00 20.57  ?  184 ARG A NE    1 
ATOM   1305 C  CZ    . ARG A 1 183 ? 12.215  68.867  89.282  1.00 19.45  ?  184 ARG A CZ    1 
ATOM   1306 N  NH1   . ARG A 1 183 ? 12.237  70.034  89.918  1.00 15.59  1  184 ARG A NH1   1 
ATOM   1307 N  NH2   . ARG A 1 183 ? 11.853  68.825  88.006  1.00 20.47  ?  184 ARG A NH2   1 
ATOM   1308 N  N     . THR A 1 184 ? 11.714  62.893  93.394  1.00 12.42  ?  185 THR A N     1 
ATOM   1309 C  CA    . THR A 1 184 ? 11.419  61.524  92.987  1.00 12.89  ?  185 THR A CA    1 
ATOM   1310 C  C     . THR A 1 184 ? 10.982  61.558  91.485  1.00 13.42  ?  185 THR A C     1 
ATOM   1311 O  O     . THR A 1 184 ? 10.739  62.625  90.908  1.00 12.86  ?  185 THR A O     1 
ATOM   1312 C  CB    . THR A 1 184 ? 10.341  60.870  93.893  1.00 12.67  ?  185 THR A CB    1 
ATOM   1313 O  OG1   . THR A 1 184 ? 9.066   61.448  93.605  1.00 13.33  ?  185 THR A OG1   1 
ATOM   1314 C  CG2   . THR A 1 184 ? 10.660  60.951  95.358  1.00 12.40  ?  185 THR A CG2   1 
ATOM   1315 N  N     . GLU A 1 185 ? 10.885  60.396  90.866  1.00 14.81  ?  186 GLU A N     1 
ATOM   1316 C  CA    . GLU A 1 185 ? 10.460  60.280  89.477  1.00 16.28  ?  186 GLU A CA    1 
ATOM   1317 C  C     . GLU A 1 185 ? 9.072   60.848  89.246  1.00 15.92  ?  186 GLU A C     1 
ATOM   1318 O  O     . GLU A 1 185 ? 8.862   61.499  88.227  1.00 16.52  ?  186 GLU A O     1 
ATOM   1319 C  CB    . GLU A 1 185 ? 10.496  58.827  89.034  1.00 19.99  ?  186 GLU A CB    1 
ATOM   1320 C  CG    . GLU A 1 185 ? 11.901  58.326  88.827  1.00 29.15  ?  186 GLU A CG    1 
ATOM   1321 C  CD    . GLU A 1 185 ? 11.952  56.911  88.286  1.00 41.59  ?  186 GLU A CD    1 
ATOM   1322 O  OE1   . GLU A 1 185 ? 10.972  56.483  87.629  1.00 44.00  ?  186 GLU A OE1   1 
ATOM   1323 O  OE2   . GLU A 1 185 ? 12.985  56.237  88.501  1.00 46.27  -1 186 GLU A OE2   1 
ATOM   1324 N  N     . LEU A 1 186 ? 8.128   60.626  90.183  1.00 14.85  ?  187 LEU A N     1 
ATOM   1325 C  CA    . LEU A 1 186 ? 6.758   61.140  90.064  1.00 13.70  ?  187 LEU A CA    1 
ATOM   1326 C  C     . LEU A 1 186 ? 6.709   62.651  90.323  1.00 12.94  ?  187 LEU A C     1 
ATOM   1327 O  O     . LEU A 1 186 ? 6.013   63.362  89.601  1.00 13.57  ?  187 LEU A O     1 
ATOM   1328 C  CB    . LEU A 1 186 ? 5.806   60.348  90.964  1.00 13.74  ?  187 LEU A CB    1 
ATOM   1329 C  CG    . LEU A 1 186 ? 4.298   60.588  90.796  1.00 14.61  ?  187 LEU A CG    1 
ATOM   1330 C  CD1   . LEU A 1 186 ? 3.796   60.162  89.394  1.00 14.45  ?  187 LEU A CD1   1 
ATOM   1331 C  CD2   . LEU A 1 186 ? 3.518   59.914  91.936  1.00 14.73  ?  187 LEU A CD2   1 
ATOM   1332 N  N     . GLN A 1 187 ? 7.522   63.170  91.254  1.00 12.15  ?  188 GLN A N     1 
ATOM   1333 C  CA    . GLN A 1 187 ? 7.634   64.627  91.448  1.00 11.90  ?  188 GLN A CA    1 
ATOM   1334 C  C     . GLN A 1 187 ? 8.203   65.282  90.186  1.00 12.64  ?  188 GLN A C     1 
ATOM   1335 O  O     . GLN A 1 187 ? 7.757   66.357  89.801  1.00 13.44  ?  188 GLN A O     1 
ATOM   1336 C  CB    . GLN A 1 187 ? 8.530   64.971  92.642  1.00 11.99  ?  188 GLN A CB    1 
ATOM   1337 C  CG    . GLN A 1 187 ? 7.815   64.911  93.972  1.00 12.38  ?  188 GLN A CG    1 
ATOM   1338 C  CD    . GLN A 1 187 ? 8.746   64.784  95.150  1.00 13.45  ?  188 GLN A CD    1 
ATOM   1339 O  OE1   . GLN A 1 187 ? 9.925   64.435  95.020  1.00 13.76  ?  188 GLN A OE1   1 
ATOM   1340 N  NE2   . GLN A 1 187 ? 8.222   65.072  96.343  1.00 13.41  ?  188 GLN A NE2   1 
ATOM   1341 N  N     . HIS A 1 188 ? 9.161   64.614  89.521  1.00 12.65  ?  189 HIS A N     1 
ATOM   1342 C  CA    . HIS A 1 188 ? 9.780   65.067  88.264  1.00 11.68  ?  189 HIS A CA    1 
ATOM   1343 C  C     . HIS A 1 188 ? 8.789   65.001  87.070  1.00 11.70  ?  189 HIS A C     1 
ATOM   1344 O  O     . HIS A 1 188 ? 8.761   65.916  86.259  1.00 12.39  ?  189 HIS A O     1 
ATOM   1345 C  CB    . HIS A 1 188 ? 11.078  64.273  87.986  1.00 10.76  ?  189 HIS A CB    1 
ATOM   1346 C  CG    . HIS A 1 188 ? 11.862  64.802  86.818  1.00 11.42  ?  189 HIS A CG    1 
ATOM   1347 N  ND1   . HIS A 1 188 ? 12.393  66.101  86.817  1.00 12.62  ?  189 HIS A ND1   1 
ATOM   1348 C  CD2   . HIS A 1 188 ? 12.154  64.212  85.636  1.00 12.37  ?  189 HIS A CD2   1 
ATOM   1349 C  CE1   . HIS A 1 188 ? 12.986  66.245  85.644  1.00 13.19  ?  189 HIS A CE1   1 
ATOM   1350 N  NE2   . HIS A 1 188 ? 12.867  65.142  84.894  1.00 13.58  ?  189 HIS A NE2   1 
ATOM   1351 N  N     . ALA A 1 189 ? 7.956   63.954  86.994  1.00 11.41  ?  190 ALA A N     1 
ATOM   1352 C  CA    . ALA A 1 189 ? 6.914   63.755  85.973  1.00 11.71  ?  190 ALA A CA    1 
ATOM   1353 C  C     . ALA A 1 189 ? 5.855   64.879  86.021  1.00 12.25  ?  190 ALA A C     1 
ATOM   1354 O  O     . ALA A 1 189 ? 5.383   65.347  84.986  1.00 12.44  ?  190 ALA A O     1 
ATOM   1355 C  CB    . ALA A 1 189 ? 6.245   62.394  86.188  1.00 11.84  ?  190 ALA A CB    1 
ATOM   1356 N  N     . TRP A 1 190 ? 5.494   65.311  87.232  1.00 12.15  ?  191 TRP A N     1 
ATOM   1357 C  CA    . TRP A 1 190 ? 4.597   66.433  87.495  1.00 11.91  ?  191 TRP A CA    1 
ATOM   1358 C  C     . TRP A 1 190 ? 5.241   67.736  86.959  1.00 13.09  ?  191 TRP A C     1 
ATOM   1359 O  O     . TRP A 1 190 ? 4.595   68.512  86.265  1.00 13.76  ?  191 TRP A O     1 
ATOM   1360 C  CB    . TRP A 1 190 ? 4.368   66.557  89.036  1.00 10.92  ?  191 TRP A CB    1 
ATOM   1361 C  CG    . TRP A 1 190 ? 3.498   67.717  89.436  1.00 9.21   ?  191 TRP A CG    1 
ATOM   1362 C  CD1   . TRP A 1 190 ? 2.140   67.733  89.469  1.00 9.44   ?  191 TRP A CD1   1 
ATOM   1363 C  CD2   . TRP A 1 190 ? 3.924   69.067  89.723  1.00 8.02   ?  191 TRP A CD2   1 
ATOM   1364 N  NE1   . TRP A 1 190 ? 1.689   69.002  89.760  1.00 9.65   ?  191 TRP A NE1   1 
ATOM   1365 C  CE2   . TRP A 1 190 ? 2.764   69.841  89.912  1.00 8.84   ?  191 TRP A CE2   1 
ATOM   1366 C  CE3   . TRP A 1 190 ? 5.170   69.695  89.835  1.00 7.44   ?  191 TRP A CE3   1 
ATOM   1367 C  CZ2   . TRP A 1 190 ? 2.816   71.205  90.238  1.00 8.72   ?  191 TRP A CZ2   1 
ATOM   1368 C  CZ3   . TRP A 1 190 ? 5.215   71.045  90.111  1.00 7.95   ?  191 TRP A CZ3   1 
ATOM   1369 C  CH2   . TRP A 1 190 ? 4.049   71.789  90.302  1.00 7.98   ?  191 TRP A CH2   1 
ATOM   1370 N  N     . ALA A 1 191 ? 6.496   67.998  87.332  1.00 13.65  ?  192 ALA A N     1 
ATOM   1371 C  CA    . ALA A 1 191 ? 7.244   69.203  86.932  1.00 13.84  ?  192 ALA A CA    1 
ATOM   1372 C  C     . ALA A 1 191 ? 7.505   69.300  85.427  1.00 14.63  ?  192 ALA A C     1 
ATOM   1373 O  O     . ALA A 1 191 ? 7.465   70.400  84.868  1.00 14.87  ?  192 ALA A O     1 
ATOM   1374 C  CB    . ALA A 1 191 ? 8.542   69.255  87.680  1.00 13.14  ?  192 ALA A CB    1 
ATOM   1375 N  N     . THR A 1 192 ? 7.756   68.148  84.770  1.00 14.43  ?  193 THR A N     1 
ATOM   1376 C  CA    . THR A 1 192 ? 7.964   68.063  83.329  1.00 14.17  ?  193 THR A CA    1 
ATOM   1377 C  C     . THR A 1 192 ? 6.656   68.364  82.620  1.00 14.12  ?  193 THR A C     1 
ATOM   1378 O  O     . THR A 1 192 ? 6.642   69.160  81.684  1.00 14.66  ?  193 THR A O     1 
ATOM   1379 C  CB    . THR A 1 192 ? 8.473   66.664  82.952  1.00 14.89  ?  193 THR A CB    1 
ATOM   1380 O  OG1   . THR A 1 192 ? 9.699   66.399  83.639  1.00 15.47  ?  193 THR A OG1   1 
ATOM   1381 C  CG2   . THR A 1 192 ? 8.637   66.490  81.473  1.00 15.25  ?  193 THR A CG2   1 
ATOM   1382 N  N     . SER A 1 193 ? 5.547   67.785  83.102  1.00 13.52  ?  194 SER A N     1 
ATOM   1383 C  CA    . SER A 1 193 ? 4.225   68.007  82.531  1.00 13.80  ?  194 SER A CA    1 
ATOM   1384 C  C     . SER A 1 193 ? 3.785   69.446  82.718  1.00 14.41  ?  194 SER A C     1 
ATOM   1385 O  O     . SER A 1 193 ? 3.182   70.020  81.814  1.00 14.82  ?  194 SER A O     1 
ATOM   1386 C  CB    . SER A 1 193 ? 3.208   67.041  83.129  1.00 14.96  ?  194 SER A CB    1 
ATOM   1387 O  OG    . SER A 1 193 ? 3.619   65.706  82.874  1.00 16.91  ?  194 SER A OG    1 
ATOM   1388 N  N     . LEU A 1 194 ? 4.117   70.051  83.859  1.00 14.32  ?  195 LEU A N     1 
ATOM   1389 C  CA    . LEU A 1 194 ? 3.832   71.456  84.094  1.00 14.83  ?  195 LEU A CA    1 
ATOM   1390 C  C     . LEU A 1 194 ? 4.617   72.318  83.105  1.00 16.38  ?  195 LEU A C     1 
ATOM   1391 O  O     . LEU A 1 194 ? 4.036   73.229  82.527  1.00 17.17  ?  195 LEU A O     1 
ATOM   1392 C  CB    . LEU A 1 194 ? 4.125   71.846  85.563  1.00 14.23  ?  195 LEU A CB    1 
ATOM   1393 C  CG    . LEU A 1 194 ? 4.187   73.362  85.874  1.00 15.15  ?  195 LEU A CG    1 
ATOM   1394 C  CD1   . LEU A 1 194 ? 2.806   74.042  85.743  1.00 15.29  ?  195 LEU A CD1   1 
ATOM   1395 C  CD2   . LEU A 1 194 ? 4.820   73.606  87.245  1.00 15.70  ?  195 LEU A CD2   1 
ATOM   1396 N  N     . GLU A 1 195 ? 5.907   72.015  82.870  1.00 17.01  ?  196 GLU A N     1 
ATOM   1397 C  CA    . GLU A 1 195 ? 6.685   72.808  81.919  1.00 18.27  ?  196 GLU A CA    1 
ATOM   1398 C  C     . GLU A 1 195 ? 6.205   72.648  80.474  1.00 18.31  ?  196 GLU A C     1 
ATOM   1399 O  O     . GLU A 1 195 ? 6.113   73.638  79.747  1.00 17.70  ?  196 GLU A O     1 
ATOM   1400 C  CB    . GLU A 1 195 ? 8.184   72.582  82.038  1.00 22.06  ?  196 GLU A CB    1 
ATOM   1401 C  CG    . GLU A 1 195 ? 8.933   73.699  81.343  1.00 30.83  ?  196 GLU A CG    1 
ATOM   1402 C  CD    . GLU A 1 195 ? 10.347  73.902  81.824  1.00 44.58  ?  196 GLU A CD    1 
ATOM   1403 O  OE1   . GLU A 1 195 ? 10.571  73.785  83.053  1.00 48.74  ?  196 GLU A OE1   1 
ATOM   1404 O  OE2   . GLU A 1 195 ? 11.233  74.173  80.977  1.00 48.05  -1 196 GLU A OE2   1 
ATOM   1405 N  N     . ILE A 1 196 ? 5.841   71.422  80.076  1.00 18.76  ?  197 ILE A N     1 
ATOM   1406 C  CA    . ILE A 1 196 ? 5.317   71.186  78.740  1.00 19.71  ?  197 ILE A CA    1 
ATOM   1407 C  C     . ILE A 1 196 ? 4.018   71.974  78.507  1.00 21.14  ?  197 ILE A C     1 
ATOM   1408 O  O     . ILE A 1 196 ? 3.972   72.763  77.569  1.00 21.77  ?  197 ILE A O     1 
ATOM   1409 C  CB    . ILE A 1 196 ? 5.193   69.689  78.448  1.00 19.90  ?  197 ILE A CB    1 
ATOM   1410 C  CG1   . ILE A 1 196 ? 6.592   69.068  78.369  1.00 20.66  ?  197 ILE A CG1   1 
ATOM   1411 C  CG2   . ILE A 1 196 ? 4.441   69.458  77.159  1.00 20.16  ?  197 ILE A CG2   1 
ATOM   1412 C  CD1   . ILE A 1 196 ? 6.581   67.563  78.385  1.00 21.47  ?  197 ILE A CD1   1 
ATOM   1413 N  N     . ILE A 1 197 ? 3.006   71.831  79.395  1.00 21.28  ?  198 ILE A N     1 
ATOM   1414 C  CA    . ILE A 1 197 ? 1.760   72.578  79.287  1.00 21.87  ?  198 ILE A CA    1 
ATOM   1415 C  C     . ILE A 1 197 ? 2.002   74.099  79.321  1.00 22.62  ?  198 ILE A C     1 
ATOM   1416 O  O     . ILE A 1 197 ? 1.430   74.834  78.522  1.00 22.68  ?  198 ILE A O     1 
ATOM   1417 C  CB    . ILE A 1 197 ? 0.783   72.146  80.413  1.00 22.65  ?  198 ILE A CB    1 
ATOM   1418 C  CG1   . ILE A 1 197 ? 0.315   70.692  80.218  1.00 23.94  ?  198 ILE A CG1   1 
ATOM   1419 C  CG2   . ILE A 1 197 ? -0.411  73.118  80.533  1.00 22.72  ?  198 ILE A CG2   1 
ATOM   1420 C  CD1   . ILE A 1 197 ? -0.459  70.458  78.949  1.00 25.59  ?  198 ILE A CD1   1 
ATOM   1421 N  N     . ASP A 1 198 ? 2.802   74.567  80.267  1.00 22.91  ?  199 ASP A N     1 
ATOM   1422 C  CA    . ASP A 1 198 ? 3.070   75.990  80.428  1.00 24.36  ?  199 ASP A CA    1 
ATOM   1423 C  C     . ASP A 1 198 ? 3.732   76.592  79.202  1.00 24.86  ?  199 ASP A C     1 
ATOM   1424 O  O     . ASP A 1 198 ? 3.402   77.712  78.815  1.00 25.76  ?  199 ASP A O     1 
ATOM   1425 C  CB    . ASP A 1 198 ? 3.953   76.223  81.664  1.00 27.39  ?  199 ASP A CB    1 
ATOM   1426 C  CG    . ASP A 1 198 ? 4.052   77.670  82.054  1.00 34.85  ?  199 ASP A CG    1 
ATOM   1427 O  OD1   . ASP A 1 198 ? 3.028   78.240  82.441  1.00 36.61  ?  199 ASP A OD1   1 
ATOM   1428 O  OD2   . ASP A 1 198 ? 5.163   78.243  81.953  1.00 38.76  -1 199 ASP A OD2   1 
ATOM   1429 N  N     . THR A 1 199 ? 4.673   75.870  78.605  1.00 24.36  ?  200 THR A N     1 
ATOM   1430 C  CA    . THR A 1 199 ? 5.357   76.333  77.411  1.00 25.10  ?  200 THR A CA    1 
ATOM   1431 C  C     . THR A 1 199 ? 4.436   76.274  76.180  1.00 26.49  ?  200 THR A C     1 
ATOM   1432 O  O     . THR A 1 199 ? 4.124   77.310  75.614  1.00 26.42  ?  200 THR A O     1 
ATOM   1433 C  CB    . THR A 1 199 ? 6.681   75.579  77.230  1.00 25.71  ?  200 THR A CB    1 
ATOM   1434 O  OG1   . THR A 1 199 ? 7.556   75.899  78.315  1.00 26.48  ?  200 THR A OG1   1 
ATOM   1435 C  CG2   . THR A 1 199 ? 7.349   75.877  75.898  1.00 26.28  ?  200 THR A CG2   1 
ATOM   1436 N  N     . LEU A 1 200 ? 3.954   75.080  75.812  1.00 27.71  ?  201 LEU A N     1 
ATOM   1437 C  CA    . LEU A 1 200 ? 3.148   74.871  74.623  1.00 29.77  ?  201 LEU A CA    1 
ATOM   1438 C  C     . LEU A 1 200 ? 1.758   75.532  74.661  1.00 31.83  ?  201 LEU A C     1 
ATOM   1439 O  O     . LEU A 1 200 ? 1.249   75.892  73.606  1.00 32.49  ?  201 LEU A O     1 
ATOM   1440 C  CB    . LEU A 1 200 ? 3.058   73.372  74.307  1.00 29.82  ?  201 LEU A CB    1 
ATOM   1441 C  CG    . LEU A 1 200 ? 4.408   72.668  74.151  1.00 30.94  ?  201 LEU A CG    1 
ATOM   1442 C  CD1   . LEU A 1 200 ? 4.215   71.198  73.855  1.00 31.25  ?  201 LEU A CD1   1 
ATOM   1443 C  CD2   . LEU A 1 200 ? 5.271   73.325  73.061  1.00 31.57  ?  201 LEU A CD2   1 
ATOM   1444 N  N     . GLU A 1 201 ? 1.153   75.700  75.839  1.00 32.98  ?  202 GLU A N     1 
ATOM   1445 C  CA    . GLU A 1 201 ? -0.136  76.391  75.943  1.00 35.10  ?  202 GLU A CA    1 
ATOM   1446 C  C     . GLU A 1 201 ? 0.020   77.914  76.125  1.00 37.00  ?  202 GLU A C     1 
ATOM   1447 O  O     . GLU A 1 201 ? -0.986  78.615  76.162  1.00 37.30  ?  202 GLU A O     1 
ATOM   1448 C  CB    . GLU A 1 201 ? -1.006  75.817  77.073  1.00 37.70  ?  202 GLU A CB    1 
ATOM   1449 C  CG    . GLU A 1 201 ? -1.492  74.401  76.835  1.00 42.56  ?  202 GLU A CG    1 
ATOM   1450 C  CD    . GLU A 1 201 ? -2.816  74.320  76.112  1.00 50.07  ?  202 GLU A CD    1 
ATOM   1451 O  OE1   . GLU A 1 201 ? -3.864  74.528  76.764  1.00 52.91  ?  202 GLU A OE1   1 
ATOM   1452 O  OE2   . GLU A 1 201 ? -2.809  74.054  74.889  1.00 51.79  -1 202 GLU A OE2   1 
ATOM   1453 N  N     . ASN A 1 202 ? 1.258   78.414  76.281  1.00 38.43  ?  203 ASN A N     1 
ATOM   1454 C  CA    . ASN A 1 202 ? 1.579   79.827  76.464  1.00 40.67  ?  203 ASN A CA    1 
ATOM   1455 C  C     . ASN A 1 202 ? 0.906   80.462  77.682  1.00 42.02  ?  203 ASN A C     1 
ATOM   1456 O  O     . ASN A 1 202 ? 0.705   81.675  77.707  1.00 42.79  ?  203 ASN A O     1 
ATOM   1457 C  CB    . ASN A 1 202 ? 1.299   80.640  75.197  1.00 42.78  ?  203 ASN A CB    1 
ATOM   1458 C  CG    . ASN A 1 202 ? 2.145   81.885  75.075  1.00 47.29  ?  203 ASN A CG    1 
ATOM   1459 O  OD1   . ASN A 1 202 ? 2.887   82.258  75.991  1.00 48.76  ?  203 ASN A OD1   1 
ATOM   1460 N  ND2   . ASN A 1 202 ? 2.049   82.561  73.941  1.00 48.88  ?  203 ASN A ND2   1 
ATOM   1461 N  N     . ILE A 1 203 ? 0.559   79.656  78.686  1.00 42.27  ?  204 ILE A N     1 
ATOM   1462 C  CA    . ILE A 1 203 ? -0.033  80.183  79.901  1.00 43.21  ?  204 ILE A CA    1 
ATOM   1463 C  C     . ILE A 1 203 ? 1.152   80.573  80.767  1.00 44.91  ?  204 ILE A C     1 
ATOM   1464 O  O     . ILE A 1 203 ? 2.005   79.731  81.040  1.00 45.64  ?  204 ILE A O     1 
ATOM   1465 C  CB    . ILE A 1 203 ? -1.011  79.167  80.543  1.00 43.41  ?  204 ILE A CB    1 
ATOM   1466 C  CG1   . ILE A 1 203 ? -0.401  77.761  80.636  1.00 44.01  ?  204 ILE A CG1   1 
ATOM   1467 C  CG2   . ILE A 1 203 ? -2.308  79.129  79.732  1.00 44.05  ?  204 ILE A CG2   1 
ATOM   1468 C  CD1   . ILE A 1 203 ? -1.180  76.805  81.401  1.00 45.25  ?  204 ILE A CD1   1 
ATOM   1469 N  N     . LYS A 1 204 ? 1.301   81.858  81.082  1.00 45.45  ?  205 LYS A N     1 
ATOM   1470 C  CA    . LYS A 1 204 ? 2.459   82.306  81.862  1.00 46.19  ?  205 LYS A CA    1 
ATOM   1471 C  C     . LYS A 1 204 ? 2.230   82.092  83.355  1.00 45.95  ?  205 LYS A C     1 
ATOM   1472 O  O     . LYS A 1 204 ? 1.963   83.051  84.074  1.00 46.18  ?  205 LYS A O     1 
ATOM   1473 C  CB    . LYS A 1 204 ? 2.810   83.763  81.526  1.00 49.06  ?  205 LYS A CB    1 
ATOM   1474 C  CG    . LYS A 1 204 ? 3.441   83.920  80.140  1.00 54.55  ?  205 LYS A CG    1 
ATOM   1475 C  CD    . LYS A 1 204 ? 3.802   85.379  79.848  1.00 60.35  ?  205 LYS A CD    1 
ATOM   1476 C  CE    . LYS A 1 204 ? 5.257   85.556  79.471  1.00 64.83  ?  205 LYS A CE    1 
ATOM   1477 N  NZ    . LYS A 1 204 ? 5.668   86.991  79.495  1.00 67.30  1  205 LYS A NZ    1 
ATOM   1478 N  N     . LEU A 1 205 ? 2.302   80.833  83.819  1.00 45.52  ?  206 LEU A N     1 
ATOM   1479 C  CA    . LEU A 1 205 ? 2.043   80.527  85.221  1.00 46.16  ?  206 LEU A CA    1 
ATOM   1480 C  C     . LEU A 1 205 ? 3.086   81.080  86.172  1.00 47.66  ?  206 LEU A C     1 
ATOM   1481 O  O     . LEU A 1 205 ? 2.727   81.520  87.265  1.00 48.22  ?  206 LEU A O     1 
ATOM   1482 C  CB    . LEU A 1 205 ? 1.840   79.025  85.464  1.00 45.85  ?  206 LEU A CB    1 
ATOM   1483 C  CG    . LEU A 1 205 ? 0.642   78.357  84.802  1.00 46.71  ?  206 LEU A CG    1 
ATOM   1484 C  CD1   . LEU A 1 205 ? 0.510   76.930  85.267  1.00 47.02  ?  206 LEU A CD1   1 
ATOM   1485 C  CD2   . LEU A 1 205 ? -0.650  79.115  85.059  1.00 47.10  ?  206 LEU A CD2   1 
ATOM   1486 N  N     . LYS A 1 206 ? 4.366   81.069  85.775  1.00 48.33  ?  207 LYS A N     1 
ATOM   1487 C  CA    . LYS A 1 206 ? 5.420   81.610  86.630  1.00 49.53  ?  207 LYS A CA    1 
ATOM   1488 C  C     . LYS A 1 206 ? 5.475   83.129  86.513  1.00 50.68  ?  207 LYS A C     1 
ATOM   1489 O  O     . LYS A 1 206 ? 5.607   83.819  87.526  1.00 50.91  ?  207 LYS A O     1 
ATOM   1490 C  CB    . LYS A 1 206 ? 6.786   80.993  86.300  1.00 51.48  ?  207 LYS A CB    1 
ATOM   1491 C  CG    . LYS A 1 206 ? 7.070   79.694  87.048  1.00 55.41  ?  207 LYS A CG    1 
ATOM   1492 C  CD    . LYS A 1 206 ? 8.575   79.457  87.215  1.00 59.92  ?  207 LYS A CD    1 
ATOM   1493 C  CE    . LYS A 1 206 ? 9.289   79.257  85.897  1.00 63.58  ?  207 LYS A CE    1 
ATOM   1494 N  NZ    . LYS A 1 206 ? 10.172  80.404  85.556  1.00 65.76  1  207 LYS A NZ    1 
ATOM   1495 N  N     . THR A 1 207 ? 5.344   83.643  85.275  1.00 50.96  ?  208 THR A N     1 
ATOM   1496 C  CA    . THR A 1 207 ? 5.388   85.069  84.941  1.00 51.66  ?  208 THR A CA    1 
ATOM   1497 C  C     . THR A 1 207 ? 4.446   85.904  85.800  1.00 52.55  ?  208 THR A C     1 
ATOM   1498 O  O     . THR A 1 207 ? 4.819   86.974  86.293  1.00 53.41  ?  208 THR A O     1 
ATOM   1499 C  CB    . THR A 1 207 ? 5.079   85.255  83.455  1.00 52.66  ?  208 THR A CB    1 
ATOM   1500 O  OG1   . THR A 1 207 ? 6.054   84.549  82.690  1.00 53.07  ?  208 THR A OG1   1 
ATOM   1501 C  CG2   . THR A 1 207 ? 5.050   86.718  83.045  1.00 53.51  ?  208 THR A CG2   1 
ATOM   1502 N  N     . SER A 1 208 ? 3.233   85.404  86.008  1.00 52.21  ?  209 SER A N     1 
ATOM   1503 C  CA    . SER A 1 208 ? 2.239   86.109  86.810  1.00 52.25  ?  209 SER A CA    1 
ATOM   1504 C  C     . SER A 1 208 ? 1.590   85.201  87.851  1.00 51.94  ?  209 SER A C     1 
ATOM   1505 O  O     . SER A 1 208 ? 1.624   83.979  87.720  1.00 52.00  ?  209 SER A O     1 
ATOM   1506 C  CB    . SER A 1 208 ? 1.169   86.727  85.907  1.00 53.57  ?  209 SER A CB    1 
ATOM   1507 O  OG    . SER A 1 208 ? 0.840   85.918  84.786  1.00 55.26  ?  209 SER A OG    1 
ATOM   1508 N  N     . ASN A 1 209 ? 1.026   85.788  88.901  1.00 51.54  ?  210 ASN A N     1 
ATOM   1509 C  CA    . ASN A 1 209 ? 0.244   85.019  89.880  1.00 51.50  ?  210 ASN A CA    1 
ATOM   1510 C  C     . ASN A 1 209 ? -1.289  85.148  89.629  1.00 50.03  ?  210 ASN A C     1 
ATOM   1511 O  O     . ASN A 1 209 ? -2.106  84.678  90.431  1.00 50.27  ?  210 ASN A O     1 
ATOM   1512 C  CB    . ASN A 1 209 ? 0.626   85.380  91.313  1.00 54.03  ?  210 ASN A CB    1 
ATOM   1513 C  CG    . ASN A 1 209 ? 1.780   84.552  91.842  1.00 59.04  ?  210 ASN A CG    1 
ATOM   1514 O  OD1   . ASN A 1 209 ? 2.348   83.682  91.145  1.00 60.57  ?  210 ASN A OD1   1 
ATOM   1515 N  ND2   . ASN A 1 209 ? 2.145   84.795  93.099  1.00 60.06  ?  210 ASN A ND2   1 
ATOM   1516 N  N     . GLU A 1 210 ? -1.653  85.751  88.476  1.00 48.19  ?  211 GLU A N     1 
ATOM   1517 C  CA    . GLU A 1 210 ? -3.002  86.012  88.006  1.00 46.95  ?  211 GLU A CA    1 
ATOM   1518 C  C     . GLU A 1 210 ? -3.294  85.261  86.692  1.00 43.62  ?  211 GLU A C     1 
ATOM   1519 O  O     . GLU A 1 210 ? -2.375  84.882  85.956  1.00 44.00  ?  211 GLU A O     1 
ATOM   1520 C  CB    . GLU A 1 210 ? -3.232  87.539  87.849  1.00 50.75  ?  211 GLU A CB    1 
ATOM   1521 C  CG    . GLU A 1 210 ? -2.001  88.357  87.468  1.00 56.96  ?  211 GLU A CG    1 
ATOM   1522 C  CD    . GLU A 1 210 ? -2.173  89.868  87.528  1.00 65.48  ?  211 GLU A CD    1 
ATOM   1523 O  OE1   . GLU A 1 210 ? -3.294  90.353  87.244  1.00 67.41  ?  211 GLU A OE1   1 
ATOM   1524 O  OE2   . GLU A 1 210 ? -1.184  90.568  87.851  1.00 67.28  -1 211 GLU A OE2   1 
ATOM   1525 N  N     . GLY A 1 211 ? -4.573  85.041  86.424  1.00 39.94  ?  212 GLY A N     1 
ATOM   1526 C  CA    . GLY A 1 211 ? -5.005  84.330  85.230  1.00 36.51  ?  212 GLY A CA    1 
ATOM   1527 C  C     . GLY A 1 211 ? -4.981  82.825  85.400  1.00 32.22  ?  212 GLY A C     1 
ATOM   1528 O  O     . GLY A 1 211 ? -4.466  82.317  86.391  1.00 31.57  ?  212 GLY A O     1 
ATOM   1529 N  N     . HIS A 1 212 ? -5.571  82.110  84.436  1.00 29.30  ?  213 HIS A N     1 
ATOM   1530 C  CA    . HIS A 1 212 ? -5.664  80.650  84.367  1.00 26.77  ?  213 HIS A CA    1 
ATOM   1531 C  C     . HIS A 1 212 ? -5.904  79.967  85.722  1.00 23.53  ?  213 HIS A C     1 
ATOM   1532 O  O     . HIS A 1 212 ? -5.106  79.130  86.134  1.00 23.15  ?  213 HIS A O     1 
ATOM   1533 C  CB    . HIS A 1 212 ? -4.426  80.090  83.658  1.00 27.83  ?  213 HIS A CB    1 
ATOM   1534 C  CG    . HIS A 1 212 ? -4.270  80.669  82.287  1.00 31.09  ?  213 HIS A CG    1 
ATOM   1535 N  ND1   . HIS A 1 212 ? -3.318  81.637  82.016  1.00 33.11  ?  213 HIS A ND1   1 
ATOM   1536 C  CD2   . HIS A 1 212 ? -5.030  80.481  81.181  1.00 32.62  ?  213 HIS A CD2   1 
ATOM   1537 C  CE1   . HIS A 1 212 ? -3.487  81.958  80.744  1.00 33.81  ?  213 HIS A CE1   1 
ATOM   1538 N  NE2   . HIS A 1 212 ? -4.504  81.284  80.197  1.00 33.73  ?  213 HIS A NE2   1 
ATOM   1539 N  N     . PRO A 1 213 ? -6.981  80.348  86.458  1.00 21.10  ?  214 PRO A N     1 
ATOM   1540 C  CA    . PRO A 1 213 ? -7.206  79.743  87.773  1.00 19.00  ?  214 PRO A CA    1 
ATOM   1541 C  C     . PRO A 1 213 ? -7.451  78.244  87.723  1.00 16.77  ?  214 PRO A C     1 
ATOM   1542 O  O     . PRO A 1 213 ? -7.093  77.551  88.667  1.00 16.24  ?  214 PRO A O     1 
ATOM   1543 C  CB    . PRO A 1 213 ? -8.429  80.500  88.302  1.00 20.26  ?  214 PRO A CB    1 
ATOM   1544 C  CG    . PRO A 1 213 ? -9.139  80.989  87.076  1.00 20.94  ?  214 PRO A CG    1 
ATOM   1545 C  CD    . PRO A 1 213 ? -8.047  81.321  86.120  1.00 19.92  ?  214 PRO A CD    1 
ATOM   1546 N  N     . GLU A 1 214 ? -8.047  77.750  86.630  1.00 15.65  ?  215 GLU A N     1 
ATOM   1547 C  CA    . GLU A 1 214 ? -8.327  76.337  86.473  1.00 15.68  ?  215 GLU A CA    1 
ATOM   1548 C  C     . GLU A 1 214 ? -7.056  75.525  86.309  1.00 14.70  ?  215 GLU A C     1 
ATOM   1549 O  O     . GLU A 1 214 ? -6.944  74.469  86.934  1.00 14.04  ?  215 GLU A O     1 
ATOM   1550 C  CB    . GLU A 1 214 ? -9.293  76.066  85.303  1.00 18.80  ?  215 GLU A CB    1 
ATOM   1551 C  CG    . GLU A 1 214 ? -10.648 76.731  85.429  1.00 25.93  ?  215 GLU A CG    1 
ATOM   1552 C  CD    . GLU A 1 214 ? -10.754 78.102  84.784  1.00 36.39  ?  215 GLU A CD    1 
ATOM   1553 O  OE1   . GLU A 1 214 ? -9.824  78.491  84.038  1.00 38.33  ?  215 GLU A OE1   1 
ATOM   1554 O  OE2   . GLU A 1 214 ? -11.773 78.790  85.029  1.00 40.08  -1 215 GLU A OE2   1 
ATOM   1555 N  N     . TRP A 1 215 ? -6.103  76.009  85.469  1.00 14.31  ?  216 TRP A N     1 
ATOM   1556 C  CA    . TRP A 1 215 ? -4.820  75.340  85.271  1.00 14.31  ?  216 TRP A CA    1 
ATOM   1557 C  C     . TRP A 1 215 ? -3.999  75.409  86.567  1.00 14.16  ?  216 TRP A C     1 
ATOM   1558 O  O     . TRP A 1 215 ? -3.373  74.413  86.942  1.00 14.31  ?  216 TRP A O     1 
ATOM   1559 C  CB    . TRP A 1 215 ? -4.015  75.967  84.116  1.00 14.27  ?  216 TRP A CB    1 
ATOM   1560 C  CG    . TRP A 1 215 ? -4.292  75.429  82.731  1.00 14.40  ?  216 TRP A CG    1 
ATOM   1561 C  CD1   . TRP A 1 215 ? -4.743  76.140  81.657  1.00 15.10  ?  216 TRP A CD1   1 
ATOM   1562 C  CD2   . TRP A 1 215 ? -4.051  74.091  82.253  1.00 13.96  ?  216 TRP A CD2   1 
ATOM   1563 N  NE1   . TRP A 1 215 ? -4.808  75.331  80.545  1.00 15.29  ?  216 TRP A NE1   1 
ATOM   1564 C  CE2   . TRP A 1 215 ? -4.381  74.071  80.880  1.00 14.60  ?  216 TRP A CE2   1 
ATOM   1565 C  CE3   . TRP A 1 215 ? -3.581  72.911  82.852  1.00 14.01  ?  216 TRP A CE3   1 
ATOM   1566 C  CZ2   . TRP A 1 215 ? -4.231  72.929  80.090  1.00 14.77  ?  216 TRP A CZ2   1 
ATOM   1567 C  CZ3   . TRP A 1 215 ? -3.438  71.781  82.069  1.00 14.65  ?  216 TRP A CZ3   1 
ATOM   1568 C  CH2   . TRP A 1 215 ? -3.786  71.788  80.712  1.00 14.83  ?  216 TRP A CH2   1 
ATOM   1569 N  N     . ARG A 1 216 ? -4.032  76.563  87.272  1.00 13.59  ?  217 ARG A N     1 
ATOM   1570 C  CA    . ARG A 1 216 ? -3.321  76.714  88.542  1.00 13.73  ?  217 ARG A CA    1 
ATOM   1571 C  C     . ARG A 1 216 ? -3.800  75.713  89.571  1.00 13.10  ?  217 ARG A C     1 
ATOM   1572 O  O     . ARG A 1 216 ? -2.986  75.040  90.194  1.00 13.47  ?  217 ARG A O     1 
ATOM   1573 C  CB    . ARG A 1 216 ? -3.478  78.121  89.107  1.00 15.61  ?  217 ARG A CB    1 
ATOM   1574 C  CG    . ARG A 1 216 ? -2.576  79.086  88.441  1.00 19.32  ?  217 ARG A CG    1 
ATOM   1575 C  CD    . ARG A 1 216 ? -2.781  80.483  88.951  1.00 22.97  ?  217 ARG A CD    1 
ATOM   1576 N  NE    . ARG A 1 216 ? -2.319  81.433  87.946  1.00 27.35  ?  217 ARG A NE    1 
ATOM   1577 C  CZ    . ARG A 1 216 ? -1.069  81.866  87.835  1.00 30.99  ?  217 ARG A CZ    1 
ATOM   1578 N  NH1   . ARG A 1 216 ? -0.135  81.449  88.685  1.00 30.89  1  217 ARG A NH1   1 
ATOM   1579 N  NH2   . ARG A 1 216 ? -0.737  82.703  86.863  1.00 31.98  ?  217 ARG A NH2   1 
ATOM   1580 N  N     . ARG A 1 217 ? -5.114  75.578  89.691  1.00 12.18  ?  218 ARG A N     1 
ATOM   1581 C  CA    . ARG A 1 217 ? -5.743  74.662  90.614  1.00 12.05  ?  218 ARG A CA    1 
ATOM   1582 C  C     . ARG A 1 217 ? -5.519  73.206  90.211  1.00 11.93  ?  218 ARG A C     1 
ATOM   1583 O  O     . ARG A 1 217 ? -5.272  72.369  91.071  1.00 12.42  ?  218 ARG A O     1 
ATOM   1584 C  CB    . ARG A 1 217 ? -7.223  75.018  90.787  1.00 13.38  ?  218 ARG A CB    1 
ATOM   1585 C  CG    . ARG A 1 217 ? -7.886  74.202  91.856  1.00 18.07  ?  218 ARG A CG    1 
ATOM   1586 C  CD    . ARG A 1 217 ? -9.035  74.922  92.542  1.00 22.75  ?  218 ARG A CD    1 
ATOM   1587 N  NE    . ARG A 1 217 ? -9.473  74.190  93.729  1.00 26.28  ?  218 ARG A NE    1 
ATOM   1588 C  CZ    . ARG A 1 217 ? -8.896  74.270  94.922  1.00 30.09  ?  218 ARG A CZ    1 
ATOM   1589 N  NH1   . ARG A 1 217 ? -7.866  75.083  95.116  1.00 30.18  1  218 ARG A NH1   1 
ATOM   1590 N  NH2   . ARG A 1 217 ? -9.356  73.550  95.936  1.00 31.69  ?  218 ARG A NH2   1 
ATOM   1591 N  N     . PHE A 1 218 ? -5.539  72.901  88.911  1.00 11.54  ?  219 PHE A N     1 
ATOM   1592 C  CA    . PHE A 1 218 ? -5.241  71.548  88.424  1.00 11.66  ?  219 PHE A CA    1 
ATOM   1593 C  C     . PHE A 1 218 ? -3.852  71.074  88.913  1.00 11.79  ?  219 PHE A C     1 
ATOM   1594 O  O     . PHE A 1 218 ? -3.749  69.993  89.489  1.00 11.33  ?  219 PHE A O     1 
ATOM   1595 C  CB    . PHE A 1 218 ? -5.342  71.458  86.870  1.00 11.20  ?  219 PHE A CB    1 
ATOM   1596 C  CG    . PHE A 1 218 ? -4.813  70.133  86.349  1.00 11.90  ?  219 PHE A CG    1 
ATOM   1597 C  CD1   . PHE A 1 218 ? -5.597  68.990  86.390  1.00 12.27  ?  219 PHE A CD1   1 
ATOM   1598 C  CD2   . PHE A 1 218 ? -3.500  70.010  85.925  1.00 12.15  ?  219 PHE A CD2   1 
ATOM   1599 C  CE1   . PHE A 1 218 ? -5.083  67.763  86.003  1.00 12.11  ?  219 PHE A CE1   1 
ATOM   1600 C  CE2   . PHE A 1 218 ? -2.992  68.778  85.545  1.00 12.18  ?  219 PHE A CE2   1 
ATOM   1601 C  CZ    . PHE A 1 218 ? -3.784  67.666  85.608  1.00 11.90  ?  219 PHE A CZ    1 
ATOM   1602 N  N     . PHE A 1 219 ? -2.799  71.911  88.693  1.00 12.09  ?  220 PHE A N     1 
ATOM   1603 C  CA    . PHE A 1 219 ? -1.412  71.605  89.061  1.00 11.98  ?  220 PHE A CA    1 
ATOM   1604 C  C     . PHE A 1 219 ? -1.195  71.579  90.561  1.00 11.79  ?  220 PHE A C     1 
ATOM   1605 O  O     . PHE A 1 219 ? -0.409  70.762  91.046  1.00 11.92  ?  220 PHE A O     1 
ATOM   1606 C  CB    . PHE A 1 219 ? -0.417  72.540  88.344  1.00 12.10  ?  220 PHE A CB    1 
ATOM   1607 C  CG    . PHE A 1 219 ? -0.142  72.041  86.949  1.00 13.02  ?  220 PHE A CG    1 
ATOM   1608 C  CD1   . PHE A 1 219 ? 0.540   70.851  86.742  1.00 13.60  ?  220 PHE A CD1   1 
ATOM   1609 C  CD2   . PHE A 1 219 ? -0.634  72.716  85.844  1.00 14.05  ?  220 PHE A CD2   1 
ATOM   1610 C  CE1   . PHE A 1 219 ? 0.715   70.344  85.458  1.00 14.15  ?  220 PHE A CE1   1 
ATOM   1611 C  CE2   . PHE A 1 219 ? -0.415  72.230  84.554  1.00 14.43  ?  220 PHE A CE2   1 
ATOM   1612 C  CZ    . PHE A 1 219 ? 0.239   71.041  84.369  1.00 13.86  ?  220 PHE A CZ    1 
ATOM   1613 N  N     . TYR A 1 220 ? -1.925  72.420  91.306  1.00 11.54  ?  221 TYR A N     1 
ATOM   1614 C  CA    . TYR A 1 220 ? -1.843  72.381  92.760  1.00 12.10  ?  221 TYR A CA    1 
ATOM   1615 C  C     . TYR A 1 220 ? -2.418  71.046  93.313  1.00 11.79  ?  221 TYR A C     1 
ATOM   1616 O  O     . TYR A 1 220 ? -1.743  70.377  94.090  1.00 12.32  ?  221 TYR A O     1 
ATOM   1617 C  CB    . TYR A 1 220 ? -2.506  73.612  93.452  1.00 12.11  ?  221 TYR A CB    1 
ATOM   1618 C  CG    . TYR A 1 220 ? -2.448  73.481  94.967  1.00 13.29  ?  221 TYR A CG    1 
ATOM   1619 C  CD1   . TYR A 1 220 ? -1.233  73.429  95.629  1.00 13.92  ?  221 TYR A CD1   1 
ATOM   1620 C  CD2   . TYR A 1 220 ? -3.591  73.206  95.706  1.00 14.93  ?  221 TYR A CD2   1 
ATOM   1621 C  CE1   . TYR A 1 220 ? -1.162  73.260  97.002  1.00 14.87  ?  221 TYR A CE1   1 
ATOM   1622 C  CE2   . TYR A 1 220 ? -3.533  73.010  97.082  1.00 15.92  ?  221 TYR A CE2   1 
ATOM   1623 C  CZ    . TYR A 1 220 ? -2.312  73.045  97.730  1.00 16.48  ?  221 TYR A CZ    1 
ATOM   1624 O  OH    . TYR A 1 220 ? -2.213  72.845  99.097  1.00 18.41  ?  221 TYR A OH    1 
ATOM   1625 N  N     . LEU A 1 221 ? -3.645  70.678  92.928  1.00 10.89  ?  222 LEU A N     1 
ATOM   1626 C  CA    . LEU A 1 221 ? -4.276  69.465  93.430  1.00 11.38  ?  222 LEU A CA    1 
ATOM   1627 C  C     . LEU A 1 221 ? -3.575  68.200  92.985  1.00 11.24  ?  222 LEU A C     1 
ATOM   1628 O  O     . LEU A 1 221 ? -3.386  67.301  93.801  1.00 11.98  ?  222 LEU A O     1 
ATOM   1629 C  CB    . LEU A 1 221 ? -5.780  69.428  93.112  1.00 12.75  ?  222 LEU A CB    1 
ATOM   1630 C  CG    . LEU A 1 221 ? -6.561  70.633  93.642  1.00 15.23  ?  222 LEU A CG    1 
ATOM   1631 C  CD1   . LEU A 1 221 ? -7.984  70.567  93.226  1.00 15.79  ?  222 LEU A CD1   1 
ATOM   1632 C  CD2   . LEU A 1 221 ? -6.415  70.781  95.172  1.00 16.25  ?  222 LEU A CD2   1 
ATOM   1633 N  N     . SER A 1 222 ? -3.144  68.133  91.724  1.00 10.89  ?  223 SER A N     1 
ATOM   1634 C  CA    . SER A 1 222 ? -2.387  66.981  91.238  1.00 10.70  ?  223 SER A CA    1 
ATOM   1635 C  C     . SER A 1 222 ? -1.049  66.888  91.966  1.00 10.40  ?  223 SER A C     1 
ATOM   1636 O  O     . SER A 1 222 ? -0.661  65.789  92.327  1.00 11.04  ?  223 SER A O     1 
ATOM   1637 C  CB    . SER A 1 222 ? -2.230  66.999  89.720  1.00 12.18  ?  223 SER A CB    1 
ATOM   1638 O  OG    . SER A 1 222 ? -1.534  68.137  89.233  1.00 15.39  ?  223 SER A OG    1 
ATOM   1639 N  N     . GLY A 1 223 ? -0.430  68.031  92.284  1.00 9.90   ?  224 GLY A N     1 
ATOM   1640 C  CA    . GLY A 1 223 ? 0.791   68.105  93.088  1.00 10.31  ?  224 GLY A CA    1 
ATOM   1641 C  C     . GLY A 1 223 ? 0.630   67.549  94.494  1.00 10.73  ?  224 GLY A C     1 
ATOM   1642 O  O     . GLY A 1 223 ? 1.424   66.720  94.933  1.00 10.85  ?  224 GLY A O     1 
ATOM   1643 N  N     . CYS A 1 224 ? -0.442  67.946  95.184  1.00 11.37  ?  225 CYS A N     1 
ATOM   1644 C  CA    . CYS A 1 224 ? -0.838  67.429  96.491  1.00 12.31  ?  225 CYS A CA    1 
ATOM   1645 C  C     . CYS A 1 224 ? -1.066  65.916  96.447  1.00 12.23  ?  225 CYS A C     1 
ATOM   1646 O  O     . CYS A 1 224 ? -0.669  65.213  97.367  1.00 12.11  ?  225 CYS A O     1 
ATOM   1647 C  CB    . CYS A 1 224 ? -2.085  68.154  96.995  1.00 13.87  ?  225 CYS A CB    1 
ATOM   1648 S  SG    . CYS A 1 224 ? -1.790  69.870  97.498  1.00 17.54  ?  225 CYS A SG    1 
ATOM   1649 N  N     . LEU A 1 225 ? -1.705  65.416  95.387  1.00 12.45  ?  226 LEU A N     1 
ATOM   1650 C  CA    . LEU A 1 225 ? -1.950  63.983  95.244  1.00 12.88  ?  226 LEU A CA    1 
ATOM   1651 C  C     . LEU A 1 225 ? -0.667  63.203  94.908  1.00 13.53  ?  226 LEU A C     1 
ATOM   1652 O  O     . LEU A 1 225 ? -0.569  62.014  95.245  1.00 14.35  ?  226 LEU A O     1 
ATOM   1653 C  CB    . LEU A 1 225 ? -3.064  63.706  94.227  1.00 12.81  ?  226 LEU A CB    1 
ATOM   1654 C  CG    . LEU A 1 225 ? -4.464  64.137  94.640  1.00 14.35  ?  226 LEU A CG    1 
ATOM   1655 C  CD1   . LEU A 1 225 ? -5.406  64.115  93.461  1.00 14.64  ?  226 LEU A CD1   1 
ATOM   1656 C  CD2   . LEU A 1 225 ? -4.999  63.277  95.774  1.00 14.84  ?  226 LEU A CD2   1 
ATOM   1657 N  N     . VAL A 1 226 ? 0.326   63.870  94.282  1.00 12.70  ?  227 VAL A N     1 
ATOM   1658 C  CA    . VAL A 1 226 ? 1.616   63.265  93.980  1.00 12.94  ?  227 VAL A CA    1 
ATOM   1659 C  C     . VAL A 1 226 ? 2.345   63.082  95.324  1.00 13.17  ?  227 VAL A C     1 
ATOM   1660 O  O     . VAL A 1 226 ? 2.804   61.986  95.609  1.00 13.20  ?  227 VAL A O     1 
ATOM   1661 C  CB    . VAL A 1 226 ? 2.469   64.125  92.975  1.00 13.75  ?  227 VAL A CB    1 
ATOM   1662 C  CG1   . VAL A 1 226 ? 3.963   63.807  93.082  1.00 14.07  ?  227 VAL A CG1   1 
ATOM   1663 C  CG2   . VAL A 1 226 ? 1.993   63.947  91.534  1.00 14.06  ?  227 VAL A CG2   1 
ATOM   1664 N  N     . ALA A 1 227 ? 2.425   64.141  96.155  1.00 13.45  ?  228 ALA A N     1 
ATOM   1665 C  CA    . ALA A 1 227 ? 3.094   64.059  97.463  1.00 14.53  ?  228 ALA A CA    1 
ATOM   1666 C  C     . ALA A 1 227 ? 2.390   63.079  98.430  1.00 16.47  ?  228 ALA A C     1 
ATOM   1667 O  O     . ALA A 1 227 ? 3.041   62.530  99.324  1.00 17.07  ?  228 ALA A O     1 
ATOM   1668 C  CB    . ALA A 1 227 ? 3.222   65.432  98.090  1.00 13.93  ?  228 ALA A CB    1 
ATOM   1669 N  N     . HIS A 1 228 ? 1.083   62.842  98.238  1.00 16.99  ?  229 HIS A N     1 
ATOM   1670 C  CA    . HIS A 1 228 ? 0.372   61.853  99.038  1.00 18.18  ?  229 HIS A CA    1 
ATOM   1671 C  C     . HIS A 1 228 ? 0.834   60.462  98.597  1.00 19.41  ?  229 HIS A C     1 
ATOM   1672 O  O     . HIS A 1 228 ? 1.344   59.712  99.424  1.00 19.64  ?  229 HIS A O     1 
ATOM   1673 C  CB    . HIS A 1 228 ? -1.160  61.990  98.937  1.00 18.19  ?  229 HIS A CB    1 
ATOM   1674 C  CG    . HIS A 1 228 ? -1.888  60.908  99.682  1.00 20.47  ?  229 HIS A CG    1 
ATOM   1675 N  ND1   . HIS A 1 228 ? -2.420  59.798  99.027  1.00 22.77  ?  229 HIS A ND1   1 
ATOM   1676 C  CD2   . HIS A 1 228 ? -2.119  60.779  101.008 1.00 21.22  ?  229 HIS A CD2   1 
ATOM   1677 C  CE1   . HIS A 1 228 ? -2.917  59.028  99.977  1.00 22.91  ?  229 HIS A CE1   1 
ATOM   1678 N  NE2   . HIS A 1 228 ? -2.760  59.578  101.185 1.00 22.50  ?  229 HIS A NE2   1 
ATOM   1679 N  N     . ASP A 1 229 ? 0.725   60.149  97.294  1.00 20.20  ?  230 ASP A N     1 
ATOM   1680 C  CA    . ASP A 1 229 ? 1.123   58.854  96.729  1.00 21.75  ?  230 ASP A CA    1 
ATOM   1681 C  C     . ASP A 1 229 ? 2.563   58.518  97.002  1.00 22.75  ?  230 ASP A C     1 
ATOM   1682 O  O     . ASP A 1 229 ? 2.892   57.353  97.231  1.00 23.59  ?  230 ASP A O     1 
ATOM   1683 C  CB    . ASP A 1 229 ? 0.882   58.820  95.213  1.00 23.96  ?  230 ASP A CB    1 
ATOM   1684 C  CG    . ASP A 1 229 ? -0.563  58.579  94.814  1.00 28.75  ?  230 ASP A CG    1 
ATOM   1685 O  OD1   . ASP A 1 229 ? -1.458  58.684  95.704  1.00 29.99  ?  230 ASP A OD1   1 
ATOM   1686 O  OD2   . ASP A 1 229 ? -0.809  58.286  93.614  1.00 30.08  -1 230 ASP A OD2   1 
ATOM   1687 N  N     . GLU A 1 230 ? 3.437   59.536  96.971  1.00 22.21  ?  231 GLU A N     1 
ATOM   1688 C  CA    . GLU A 1 230 ? 4.852   59.356  97.241  1.00 21.65  ?  231 GLU A CA    1 
ATOM   1689 C  C     . GLU A 1 230 ? 5.192   59.139  98.712  1.00 21.51  ?  231 GLU A C     1 
ATOM   1690 O  O     . GLU A 1 230 ? 6.309   58.733  99.012  1.00 22.14  ?  231 GLU A O     1 
ATOM   1691 C  CB    . GLU A 1 230 ? 5.655   60.550  96.698  1.00 23.54  ?  231 GLU A CB    1 
ATOM   1692 C  CG    . GLU A 1 230 ? 5.859   60.519  95.195  1.00 29.33  ?  231 GLU A CG    1 
ATOM   1693 C  CD    . GLU A 1 230 ? 6.431   59.225  94.641  1.00 39.54  ?  231 GLU A CD    1 
ATOM   1694 O  OE1   . GLU A 1 230 ? 7.653   59.185  94.379  1.00 41.26  ?  231 GLU A OE1   1 
ATOM   1695 O  OE2   . GLU A 1 230 ? 5.662   58.247  94.471  1.00 43.30  -1 231 GLU A OE2   1 
ATOM   1696 N  N     . GLY A 1 231 ? 4.278   59.456  99.614  1.00 20.64  ?  232 GLY A N     1 
ATOM   1697 C  CA    . GLY A 1 231 ? 4.545   59.396  101.040 1.00 21.19  ?  232 GLY A CA    1 
ATOM   1698 C  C     . GLY A 1 231 ? 5.255   60.633  101.572 1.00 22.36  ?  232 GLY A C     1 
ATOM   1699 O  O     . GLY A 1 231 ? 5.644   60.657  102.733 1.00 23.06  ?  232 GLY A O     1 
ATOM   1700 N  N     . ALA A 1 232 ? 5.417   61.683  100.743 1.00 22.61  ?  233 ALA A N     1 
ATOM   1701 C  CA    . ALA A 1 232 ? 6.075   62.932  101.113 1.00 23.42  ?  233 ALA A CA    1 
ATOM   1702 C  C     . ALA A 1 232 ? 5.218   63.776  102.063 1.00 24.57  ?  233 ALA A C     1 
ATOM   1703 O  O     . ALA A 1 232 ? 5.748   64.424  102.965 1.00 24.95  ?  233 ALA A O     1 
ATOM   1704 C  CB    . ALA A 1 232 ? 6.421   63.732  99.859  1.00 23.07  ?  233 ALA A CB    1 
ATOM   1705 N  N     . CYS A 1 233 ? 3.897   63.789  101.839 1.00 25.01  ?  234 CYS A N     1 
ATOM   1706 C  CA    . CYS A 1 233 ? 2.934   64.531  102.650 1.00 25.39  ?  234 CYS A CA    1 
ATOM   1707 C  C     . CYS A 1 233 ? 1.577   63.818  102.575 1.00 26.64  ?  234 CYS A C     1 
ATOM   1708 O  O     . CYS A 1 233 ? 0.826   63.963  101.603 1.00 27.01  ?  234 CYS A O     1 
ATOM   1709 C  CB    . CYS A 1 233 ? 2.833   65.984  102.192 1.00 25.33  ?  234 CYS A CB    1 
ATOM   1710 S  SG    . CYS A 1 233 ? 1.540   66.944  103.026 1.00 28.32  ?  234 CYS A SG    1 
ATOM   1711 N  N     . ILE A 1 234 ? 1.263   63.059  103.611 1.00 26.96  ?  235 ILE A N     1 
ATOM   1712 C  CA    . ILE A 1 234 ? 0.026   62.298  103.671 1.00 28.06  ?  235 ILE A CA    1 
ATOM   1713 C  C     . ILE A 1 234 ? -1.215  63.131  104.011 1.00 28.32  ?  235 ILE A C     1 
ATOM   1714 O  O     . ILE A 1 234 ? -1.300  63.760  105.070 1.00 28.94  ?  235 ILE A O     1 
ATOM   1715 C  CB    . ILE A 1 234 ? 0.199   61.114  104.657 1.00 29.21  ?  235 ILE A CB    1 
ATOM   1716 C  CG1   . ILE A 1 234 ? 1.381   60.212  104.229 1.00 30.53  ?  235 ILE A CG1   1 
ATOM   1717 C  CG2   . ILE A 1 234 ? -1.097  60.325  104.802 1.00 29.57  ?  235 ILE A CG2   1 
ATOM   1718 C  CD1   . ILE A 1 234 ? 1.225   59.622  102.833 1.00 32.12  ?  235 ILE A CD1   1 
ATOM   1719 N  N     . LEU A 1 235 ? -2.188  63.109  103.109 1.00 27.36  ?  236 LEU A N     1 
ATOM   1720 C  CA    . LEU A 1 235 ? -3.469  63.773  103.293 1.00 27.01  ?  236 LEU A CA    1 
ATOM   1721 C  C     . LEU A 1 235 ? -4.448  62.778  103.921 1.00 27.41  ?  236 LEU A C     1 
ATOM   1722 O  O     . LEU A 1 235 ? -4.336  61.570  103.679 1.00 27.29  ?  236 LEU A O     1 
ATOM   1723 C  CB    . LEU A 1 235 ? -4.017  64.192  101.933 1.00 26.54  ?  236 LEU A CB    1 
ATOM   1724 C  CG    . LEU A 1 235 ? -3.138  65.097  101.117 1.00 27.29  ?  236 LEU A CG    1 
ATOM   1725 C  CD1   . LEU A 1 235 ? -3.523  65.052  99.663  1.00 27.78  ?  236 LEU A CD1   1 
ATOM   1726 C  CD2   . LEU A 1 235 ? -3.191  66.498  101.645 1.00 27.79  ?  236 LEU A CD2   1 
ATOM   1727 N  N     . ASP A 1 236 ? -5.409  63.271  104.718 1.00 27.73  ?  237 ASP A N     1 
ATOM   1728 C  CA    . ASP A 1 236 ? -6.429  62.384  105.286 1.00 29.10  ?  237 ASP A CA    1 
ATOM   1729 C  C     . ASP A 1 236 ? -7.430  61.956  104.183 1.00 28.55  ?  237 ASP A C     1 
ATOM   1730 O  O     . ASP A 1 236 ? -7.473  62.563  103.112 1.00 28.18  ?  237 ASP A O     1 
ATOM   1731 C  CB    . ASP A 1 236 ? -7.124  63.045  106.482 1.00 33.31  ?  237 ASP A CB    1 
ATOM   1732 C  CG    . ASP A 1 236 ? -7.673  64.418  106.161 1.00 42.18  ?  237 ASP A CG    1 
ATOM   1733 O  OD1   . ASP A 1 236 ? -6.979  65.425  106.462 1.00 44.86  -1 237 ASP A OD1   1 
ATOM   1734 O  OD2   . ASP A 1 236 ? -8.780  64.493  105.586 1.00 44.80  ?  237 ASP A OD2   1 
ATOM   1735 N  N     . ASP A 1 237 ? -8.216  60.909  104.428 1.00 28.75  ?  238 ASP A N     1 
ATOM   1736 C  CA    . ASP A 1 237 ? -9.137  60.365  103.427 1.00 29.44  ?  238 ASP A CA    1 
ATOM   1737 C  C     . ASP A 1 237 ? -10.206 61.313  102.889 1.00 28.54  ?  238 ASP A C     1 
ATOM   1738 O  O     . ASP A 1 237 ? -10.599 61.155  101.734 1.00 29.10  ?  238 ASP A O     1 
ATOM   1739 C  CB    . ASP A 1 237 ? -9.814  59.107  103.955 1.00 33.56  ?  238 ASP A CB    1 
ATOM   1740 C  CG    . ASP A 1 237 ? -8.847  57.957  104.088 1.00 41.77  ?  238 ASP A CG    1 
ATOM   1741 O  OD1   . ASP A 1 237 ? -8.126  57.666  103.093 1.00 42.94  -1 238 ASP A OD1   1 
ATOM   1742 O  OD2   . ASP A 1 237 ? -8.801  57.345  105.183 1.00 45.17  ?  238 ASP A OD2   1 
ATOM   1743 N  N     . GLU A 1 238 ? -10.712 62.238  103.709 1.00 27.26  ?  239 GLU A N     1 
ATOM   1744 C  CA    . GLU A 1 238 ? -11.730 63.165  103.252 1.00 27.18  ?  239 GLU A CA    1 
ATOM   1745 C  C     . GLU A 1 238 ? -11.128 64.116  102.204 1.00 25.88  ?  239 GLU A C     1 
ATOM   1746 O  O     . GLU A 1 238 ? -11.741 64.333  101.157 1.00 25.72  ?  239 GLU A O     1 
ATOM   1747 C  CB    . GLU A 1 238 ? -12.369 63.930  104.427 1.00 30.54  ?  239 GLU A CB    1 
ATOM   1748 C  CG    . GLU A 1 238 ? -13.860 64.198  104.212 1.00 35.28  ?  239 GLU A CG    1 
ATOM   1749 N  N     . THR A 1 239 ? -9.905  64.606  102.456 1.00 24.55  ?  240 THR A N     1 
ATOM   1750 C  CA    . THR A 1 239 ? -9.172  65.478  101.531 1.00 24.40  ?  240 THR A CA    1 
ATOM   1751 C  C     . THR A 1 239 ? -8.892  64.758  100.203 1.00 23.08  ?  240 THR A C     1 
ATOM   1752 O  O     . THR A 1 239 ? -9.132  65.354  99.159  1.00 23.18  ?  240 THR A O     1 
ATOM   1753 C  CB    . THR A 1 239 ? -7.856  65.972  102.155 1.00 26.20  ?  240 THR A CB    1 
ATOM   1754 O  OG1   . THR A 1 239 ? -8.093  66.390  103.496 1.00 28.32  ?  240 THR A OG1   1 
ATOM   1755 C  CG2   . THR A 1 239 ? -7.233  67.097  101.371 1.00 26.00  ?  240 THR A CG2   1 
ATOM   1756 N  N     . ILE A 1 240 ? -8.438  63.468  100.240 1.00 21.66  ?  241 ILE A N     1 
ATOM   1757 C  CA    . ILE A 1 240 ? -8.167  62.668  99.037  1.00 21.09  ?  241 ILE A CA    1 
ATOM   1758 C  C     . ILE A 1 240 ? -9.414  62.613  98.147  1.00 20.05  ?  241 ILE A C     1 
ATOM   1759 O  O     . ILE A 1 240 ? -9.334  62.844  96.942  1.00 19.86  ?  241 ILE A O     1 
ATOM   1760 C  CB    . ILE A 1 240 ? -7.683  61.210  99.368  1.00 22.00  ?  241 ILE A CB    1 
ATOM   1761 C  CG1   . ILE A 1 240 ? -6.442  61.175  100.287 1.00 23.02  ?  241 ILE A CG1   1 
ATOM   1762 C  CG2   . ILE A 1 240 ? -7.457  60.382  98.101  1.00 21.97  ?  241 ILE A CG2   1 
ATOM   1763 C  CD1   . ILE A 1 240 ? -5.281  61.830  99.730  1.00 24.54  ?  241 ILE A CD1   1 
ATOM   1764 N  N     . LYS A 1 241 ? -10.556 62.344  98.762  1.00 19.68  ?  242 LYS A N     1 
ATOM   1765 C  CA    . LYS A 1 241 ? -11.861 62.193  98.117  1.00 19.50  ?  242 LYS A CA    1 
ATOM   1766 C  C     . LYS A 1 241 ? -12.326 63.476  97.407  1.00 17.66  ?  242 LYS A C     1 
ATOM   1767 O  O     . LYS A 1 241 ? -12.743 63.427  96.267  1.00 17.43  ?  242 LYS A O     1 
ATOM   1768 C  CB    . LYS A 1 241 ? -12.883 61.709  99.165  1.00 22.27  ?  242 LYS A CB    1 
ATOM   1769 C  CG    . LYS A 1 241 ? -14.303 61.493  98.637  1.00 28.56  ?  242 LYS A CG    1 
ATOM   1770 C  CD    . LYS A 1 241 ? -15.269 62.580  99.136  1.00 34.23  ?  242 LYS A CD    1 
ATOM   1771 C  CE    . LYS A 1 241 ? -16.700 62.117  99.185  1.00 38.09  ?  242 LYS A CE    1 
ATOM   1772 N  NZ    . LYS A 1 241 ? -16.844 60.916  100.046 1.00 41.33  1  242 LYS A NZ    1 
ATOM   1773 N  N     . ASN A 1 242 ? -12.223 64.614  98.071  1.00 16.67  ?  243 ASN A N     1 
ATOM   1774 C  CA    . ASN A 1 242 ? -12.599 65.910  97.503  1.00 15.59  ?  243 ASN A CA    1 
ATOM   1775 C  C     . ASN A 1 242 ? -11.593 66.374  96.421  1.00 14.08  ?  243 ASN A C     1 
ATOM   1776 O  O     . ASN A 1 242 ? -11.988 66.962  95.419  1.00 13.11  ?  243 ASN A O     1 
ATOM   1777 C  CB    . ASN A 1 242 ? -12.740 66.945  98.636  1.00 15.81  ?  243 ASN A CB    1 
ATOM   1778 C  CG    . ASN A 1 242 ? -13.895 66.626  99.564  1.00 18.44  ?  243 ASN A CG    1 
ATOM   1779 O  OD1   . ASN A 1 242 ? -15.006 66.274  99.125  1.00 20.26  ?  243 ASN A OD1   1 
ATOM   1780 N  ND2   . ASN A 1 242 ? -13.669 66.735  100.858 1.00 18.29  ?  243 ASN A ND2   1 
ATOM   1781 N  N     . TYR A 1 243 ? -10.314 66.054  96.602  1.00 13.58  ?  244 TYR A N     1 
ATOM   1782 C  CA    . TYR A 1 243 ? -9.271  66.414  95.627  1.00 13.95  ?  244 TYR A CA    1 
ATOM   1783 C  C     . TYR A 1 243 ? -9.449  65.638  94.345  1.00 14.74  ?  244 TYR A C     1 
ATOM   1784 O  O     . TYR A 1 243 ? -9.252  66.192  93.272  1.00 14.83  ?  244 TYR A O     1 
ATOM   1785 C  CB    . TYR A 1 243 ? -7.854  66.190  96.205  1.00 13.38  ?  244 TYR A CB    1 
ATOM   1786 C  CG    . TYR A 1 243 ? -7.330  67.325  97.058  1.00 14.25  ?  244 TYR A CG    1 
ATOM   1787 C  CD1   . TYR A 1 243 ? -8.194  68.244  97.640  1.00 15.15  ?  244 TYR A CD1   1 
ATOM   1788 C  CD2   . TYR A 1 243 ? -5.969  67.462  97.312  1.00 15.44  ?  244 TYR A CD2   1 
ATOM   1789 C  CE1   . TYR A 1 243 ? -7.720  69.284  98.433  1.00 16.72  ?  244 TYR A CE1   1 
ATOM   1790 C  CE2   . TYR A 1 243 ? -5.482  68.497  98.107  1.00 16.62  ?  244 TYR A CE2   1 
ATOM   1791 C  CZ    . TYR A 1 243 ? -6.360  69.414  98.663  1.00 17.72  ?  244 TYR A CZ    1 
ATOM   1792 O  OH    . TYR A 1 243 ? -5.892  70.464  99.424  1.00 18.23  ?  244 TYR A OH    1 
ATOM   1793 N  N     . GLN A 1 244 ? -9.829  64.350  94.455  1.00 15.08  ?  245 GLN A N     1 
ATOM   1794 C  CA    . GLN A 1 244 ? -10.088 63.484  93.320  1.00 14.87  ?  245 GLN A CA    1 
ATOM   1795 C  C     . GLN A 1 244 ? -11.307 63.979  92.552  1.00 13.90  ?  245 GLN A C     1 
ATOM   1796 O  O     . GLN A 1 244 ? -11.272 64.025  91.327  1.00 13.60  ?  245 GLN A O     1 
ATOM   1797 C  CB    . GLN A 1 244 ? -10.297 62.044  93.797  1.00 17.29  ?  245 GLN A CB    1 
ATOM   1798 C  CG    . GLN A 1 244 ? -8.984  61.324  94.105  1.00 19.83  ?  245 GLN A CG    1 
ATOM   1799 C  CD    . GLN A 1 244 ? -9.201  60.015  94.835  1.00 22.50  ?  245 GLN A CD    1 
ATOM   1800 O  OE1   . GLN A 1 244 ? -10.262 59.766  95.435  1.00 23.40  ?  245 GLN A OE1   1 
ATOM   1801 N  NE2   . GLN A 1 244 ? -8.181  59.168  94.818  1.00 21.93  ?  245 GLN A NE2   1 
ATOM   1802 N  N     . THR A 1 245 ? -12.355 64.410  93.255  1.00 13.69  ?  246 THR A N     1 
ATOM   1803 C  CA    . THR A 1 245 ? -13.558 64.969  92.626  1.00 13.79  ?  246 THR A CA    1 
ATOM   1804 C  C     . THR A 1 245 ? -13.235 66.258  91.858  1.00 13.29  ?  246 THR A C     1 
ATOM   1805 O  O     . THR A 1 245 ? -13.702 66.449  90.733  1.00 13.19  ?  246 THR A O     1 
ATOM   1806 C  CB    . THR A 1 245 ? -14.641 65.195  93.687  1.00 15.74  ?  246 THR A CB    1 
ATOM   1807 O  OG1   . THR A 1 245 ? -14.972 63.920  94.239  1.00 17.84  ?  246 THR A OG1   1 
ATOM   1808 C  CG2   . THR A 1 245 ? -15.899 65.844  93.114  1.00 15.25  ?  246 THR A CG2   1 
ATOM   1809 N  N     . GLU A 1 246 ? -12.432 67.137  92.463  1.00 13.41  ?  247 GLU A N     1 
ATOM   1810 C  CA    . GLU A 1 246 ? -11.990 68.370  91.798  1.00 13.97  ?  247 GLU A CA    1 
ATOM   1811 C  C     . GLU A 1 246 ? -11.095 68.035  90.628  1.00 13.91  ?  247 GLU A C     1 
ATOM   1812 O  O     . GLU A 1 246 ? -11.190 68.679  89.606  1.00 13.76  ?  247 GLU A O     1 
ATOM   1813 C  CB    . GLU A 1 246 ? -11.215 69.292  92.750  1.00 15.79  ?  247 GLU A CB    1 
ATOM   1814 C  CG    . GLU A 1 246 ? -12.034 69.873  93.869  1.00 20.37  ?  247 GLU A CG    1 
ATOM   1815 C  CD    . GLU A 1 246 ? -11.546 71.215  94.367  1.00 29.30  ?  247 GLU A CD    1 
ATOM   1816 O  OE1   . GLU A 1 246 ? -11.244 72.085  93.520  1.00 30.35  ?  247 GLU A OE1   1 
ATOM   1817 O  OE2   . GLU A 1 246 ? -11.492 71.411  95.602  1.00 33.32  -1 247 GLU A OE2   1 
ATOM   1818 N  N     . LEU A 1 247 ? -10.213 67.046  90.771  1.00 14.63  ?  248 LEU A N     1 
ATOM   1819 C  CA    . LEU A 1 247 ? -9.277  66.657  89.714  1.00 15.23  ?  248 LEU A CA    1 
ATOM   1820 C  C     . LEU A 1 247 ? -9.986  66.141  88.474  1.00 15.25  ?  248 LEU A C     1 
ATOM   1821 O  O     . LEU A 1 247 ? -9.639  66.521  87.355  1.00 15.73  ?  248 LEU A O     1 
ATOM   1822 C  CB    . LEU A 1 247 ? -8.285  65.626  90.229  1.00 16.10  ?  248 LEU A CB    1 
ATOM   1823 C  CG    . LEU A 1 247 ? -7.105  65.405  89.324  1.00 18.98  ?  248 LEU A CG    1 
ATOM   1824 C  CD1   . LEU A 1 247 ? -6.010  66.449  89.597  1.00 19.13  ?  248 LEU A CD1   1 
ATOM   1825 C  CD2   . LEU A 1 247 ? -6.590  63.984  89.471  1.00 20.92  ?  248 LEU A CD2   1 
ATOM   1826 N  N     . LYS A 1 248 ? -11.005 65.308  88.666  1.00 14.89  ?  249 LYS A N     1 
ATOM   1827 C  CA    . LYS A 1 248 ? -11.827 64.810  87.572  1.00 14.60  ?  249 LYS A CA    1 
ATOM   1828 C  C     . LYS A 1 248 ? -12.532 66.000  86.844  1.00 14.66  ?  249 LYS A C     1 
ATOM   1829 O  O     . LYS A 1 248 ? -12.596 66.044  85.616  1.00 14.49  ?  249 LYS A O     1 
ATOM   1830 C  CB    . LYS A 1 248 ? -12.857 63.813  88.122  1.00 15.50  ?  249 LYS A CB    1 
ATOM   1831 C  CG    . LYS A 1 248 ? -13.902 63.416  87.102  1.00 19.56  ?  249 LYS A CG    1 
ATOM   1832 C  CD    . LYS A 1 248 ? -15.021 62.600  87.686  1.00 23.11  ?  249 LYS A CD    1 
ATOM   1833 C  CE    . LYS A 1 248 ? -15.984 62.149  86.608  1.00 25.86  ?  249 LYS A CE    1 
ATOM   1834 N  NZ    . LYS A 1 248 ? -16.627 60.860  86.973  1.00 28.38  1  249 LYS A NZ    1 
ATOM   1835 N  N     . THR A 1 249 ? -13.030 66.963  87.615  1.00 14.72  ?  250 THR A N     1 
ATOM   1836 C  CA    . THR A 1 249 ? -13.701 68.150  87.090  1.00 15.23  ?  250 THR A CA    1 
ATOM   1837 C  C     . THR A 1 249 ? -12.763 69.057  86.269  1.00 15.15  ?  250 THR A C     1 
ATOM   1838 O  O     . THR A 1 249 ? -13.115 69.429  85.149  1.00 15.20  ?  250 THR A O     1 
ATOM   1839 C  CB    . THR A 1 249 ? -14.325 68.945  88.237  1.00 16.17  ?  250 THR A CB    1 
ATOM   1840 O  OG1   . THR A 1 249 ? -15.145 68.074  89.012  1.00 17.55  ?  250 THR A OG1   1 
ATOM   1841 C  CG2   . THR A 1 249 ? -15.080 70.144  87.737  1.00 15.99  ?  250 THR A CG2   1 
ATOM   1842 N  N     . LEU A 1 250 ? -11.585 69.423  86.843  1.00 14.50  ?  251 LEU A N     1 
ATOM   1843 C  CA    . LEU A 1 250 ? -10.581 70.267  86.210  1.00 14.60  ?  251 LEU A CA    1 
ATOM   1844 C  C     . LEU A 1 250 ? -10.006 69.586  84.981  1.00 16.25  ?  251 LEU A C     1 
ATOM   1845 O  O     . LEU A 1 250 ? -9.853  70.244  83.945  1.00 16.55  ?  251 LEU A O     1 
ATOM   1846 C  CB    . LEU A 1 250 ? -9.447  70.613  87.191  1.00 13.88  ?  251 LEU A CB    1 
ATOM   1847 C  CG    . LEU A 1 250 ? -9.800  71.577  88.306  1.00 15.00  ?  251 LEU A CG    1 
ATOM   1848 C  CD1   . LEU A 1 250 ? -8.841  71.448  89.452  1.00 15.06  ?  251 LEU A CD1   1 
ATOM   1849 C  CD2   . LEU A 1 250 ? -9.942  73.027  87.807  1.00 15.57  ?  251 LEU A CD2   1 
ATOM   1850 N  N     . GLU A 1 251 ? -9.704  68.278  85.072  1.00 17.08  ?  252 GLU A N     1 
ATOM   1851 C  CA    . GLU A 1 251 ? -9.115  67.545  83.947  1.00 18.79  ?  252 GLU A CA    1 
ATOM   1852 C  C     . GLU A 1 251 ? -10.045 67.484  82.744  1.00 20.62  ?  252 GLU A C     1 
ATOM   1853 O  O     . GLU A 1 251 ? -9.568  67.535  81.619  1.00 21.03  ?  252 GLU A O     1 
ATOM   1854 C  CB    . GLU A 1 251 ? -8.664  66.131  84.384  1.00 21.20  ?  252 GLU A CB    1 
ATOM   1855 C  CG    . GLU A 1 251 ? -7.776  65.399  83.387  1.00 26.51  ?  252 GLU A CG    1 
ATOM   1856 C  CD    . GLU A 1 251 ? -8.494  64.691  82.247  1.00 32.16  ?  252 GLU A CD    1 
ATOM   1857 O  OE1   . GLU A 1 251 ? -9.653  64.253  82.450  1.00 32.48  ?  252 GLU A OE1   1 
ATOM   1858 O  OE2   . GLU A 1 251 ? -7.907  64.597  81.143  1.00 33.56  -1 252 GLU A OE2   1 
ATOM   1859 N  N     . GLU A 1 252 ? -11.360 67.353  82.964  1.00 21.56  ?  253 GLU A N     1 
ATOM   1860 C  CA    . GLU A 1 252 ? -12.319 67.313  81.866  1.00 22.91  ?  253 GLU A CA    1 
ATOM   1861 C  C     . GLU A 1 252 ? -12.419 68.691  81.216  1.00 22.79  ?  253 GLU A C     1 
ATOM   1862 O  O     . GLU A 1 252 ? -12.448 68.803  79.993  1.00 23.85  ?  253 GLU A O     1 
ATOM   1863 C  CB    . GLU A 1 252 ? -13.699 66.849  82.359  1.00 27.41  ?  253 GLU A CB    1 
ATOM   1864 C  CG    . GLU A 1 252 ? -14.321 65.745  81.511  1.00 38.78  ?  253 GLU A CG    1 
ATOM   1865 C  CD    . GLU A 1 252 ? -15.356 66.145  80.468  1.00 52.11  ?  253 GLU A CD    1 
ATOM   1866 O  OE1   . GLU A 1 252 ? -15.085 67.077  79.674  1.00 55.38  ?  253 GLU A OE1   1 
ATOM   1867 O  OE2   . GLU A 1 252 ? -16.433 65.504  80.427  1.00 56.27  -1 253 GLU A OE2   1 
ATOM   1868 N  N     . ALA A 1 253 ? -12.443 69.741  82.026  1.00 21.46  ?  254 ALA A N     1 
ATOM   1869 C  CA    . ALA A 1 253 ? -12.516 71.108  81.534  1.00 20.23  ?  254 ALA A CA    1 
ATOM   1870 C  C     . ALA A 1 253 ? -11.275 71.457  80.719  1.00 19.40  ?  254 ALA A C     1 
ATOM   1871 O  O     . ALA A 1 253 ? -11.382 72.096  79.674  1.00 20.01  ?  254 ALA A O     1 
ATOM   1872 C  CB    . ALA A 1 253 ? -12.660 72.067  82.705  1.00 19.56  ?  254 ALA A CB    1 
ATOM   1873 N  N     . LEU A 1 254 ? -10.094 71.009  81.173  1.00 17.84  ?  255 LEU A N     1 
ATOM   1874 C  CA    . LEU A 1 254 ? -8.854  71.364  80.503  1.00 16.36  ?  255 LEU A CA    1 
ATOM   1875 C  C     . LEU A 1 254 ? -8.379  70.393  79.441  1.00 17.77  ?  255 LEU A C     1 
ATOM   1876 O  O     . LEU A 1 254 ? -7.454  70.745  78.704  1.00 19.23  ?  255 LEU A O     1 
ATOM   1877 C  CB    . LEU A 1 254 ? -7.747  71.568  81.537  1.00 13.91  ?  255 LEU A CB    1 
ATOM   1878 C  CG    . LEU A 1 254 ? -8.007  72.597  82.605  1.00 12.08  ?  255 LEU A CG    1 
ATOM   1879 C  CD1   . LEU A 1 254 ? -7.037  72.427  83.741  1.00 11.85  ?  255 LEU A CD1   1 
ATOM   1880 C  CD2   . LEU A 1 254 ? -8.007  74.009  82.041  1.00 11.18  ?  255 LEU A CD2   1 
ATOM   1881 N  N     . SER A 1 255 ? -8.941  69.177  79.399  1.00 17.47  ?  256 SER A N     1 
ATOM   1882 C  CA    . SER A 1 255 ? -8.542  68.059  78.517  1.00 18.27  ?  256 SER A CA    1 
ATOM   1883 C  C     . SER A 1 255 ? -7.062  67.737  78.678  1.00 18.61  ?  256 SER A C     1 
ATOM   1884 O  O     . SER A 1 255 ? -6.344  67.575  77.691  1.00 19.88  ?  256 SER A O     1 
ATOM   1885 C  CB    . SER A 1 255 ? -8.908  68.326  77.057  1.00 19.76  ?  256 SER A CB    1 
ATOM   1886 O  OG    . SER A 1 255 ? -10.308 68.501  76.886  1.00 21.96  ?  256 SER A OG    1 
ATOM   1887 N  N     . VAL A 1 256 ? -6.597  67.677  79.939  1.00 17.51  ?  257 VAL A N     1 
ATOM   1888 C  CA    . VAL A 1 256 ? -5.206  67.453  80.296  1.00 16.36  ?  257 VAL A CA    1 
ATOM   1889 C  C     . VAL A 1 256 ? -4.621  66.160  79.735  1.00 16.02  ?  257 VAL A C     1 
ATOM   1890 O  O     . VAL A 1 256 ? -3.592  66.227  79.075  1.00 15.33  ?  257 VAL A O     1 
ATOM   1891 C  CB    . VAL A 1 256 ? -4.933  67.561  81.819  1.00 16.47  ?  257 VAL A CB    1 
ATOM   1892 C  CG1   . VAL A 1 256 ? -3.423  67.536  82.089  1.00 16.67  ?  257 VAL A CG1   1 
ATOM   1893 C  CG2   . VAL A 1 256 ? -5.547  68.835  82.387  1.00 16.57  ?  257 VAL A CG2   1 
ATOM   1894 N  N     . ARG A 1 257 ? -5.238  65.001  79.987  1.00 16.62  ?  258 ARG A N     1 
ATOM   1895 C  CA    . ARG A 1 257 ? -4.666  63.750  79.476  1.00 17.61  ?  258 ARG A CA    1 
ATOM   1896 C  C     . ARG A 1 257 ? -4.477  63.742  77.929  1.00 18.71  ?  258 ARG A C     1 
ATOM   1897 O  O     . ARG A 1 257 ? -3.432  63.299  77.469  1.00 18.97  ?  258 ARG A O     1 
ATOM   1898 C  CB    . ARG A 1 257 ? -5.437  62.546  79.972  1.00 17.85  ?  258 ARG A CB    1 
ATOM   1899 C  CG    . ARG A 1 257 ? -5.056  62.199  81.414  1.00 18.78  ?  258 ARG A CG    1 
ATOM   1900 C  CD    . ARG A 1 257 ? -6.010  61.184  82.002  1.00 19.87  ?  258 ARG A CD    1 
ATOM   1901 N  NE    . ARG A 1 257 ? -7.412  61.584  81.842  1.00 20.81  ?  258 ARG A NE    1 
ATOM   1902 C  CZ    . ARG A 1 257 ? -8.450  60.820  82.161  1.00 22.10  ?  258 ARG A CZ    1 
ATOM   1903 N  NH1   . ARG A 1 257 ? -8.259  59.606  82.673  1.00 20.85  1  258 ARG A NH1   1 
ATOM   1904 N  NH2   . ARG A 1 257 ? -9.685  61.264  81.983  1.00 21.55  ?  258 ARG A NH2   1 
ATOM   1905 N  N     . SER A 1 258 ? -5.435  64.317  77.159  1.00 18.76  ?  259 SER A N     1 
ATOM   1906 C  CA    . SER A 1 258 ? -5.385  64.438  75.700  1.00 18.61  ?  259 SER A CA    1 
ATOM   1907 C  C     . SER A 1 258 ? -4.337  65.419  75.246  1.00 18.99  ?  259 SER A C     1 
ATOM   1908 O  O     . SER A 1 258 ? -3.531  65.071  74.378  1.00 19.53  ?  259 SER A O     1 
ATOM   1909 C  CB    . SER A 1 258 ? -6.742  64.826  75.132  1.00 18.91  ?  259 SER A CB    1 
ATOM   1910 O  OG    . SER A 1 258 ? -7.455  63.615  75.034  1.00 22.80  ?  259 SER A OG    1 
ATOM   1911 N  N     . LYS A 1 259 ? -4.308  66.640  75.829  1.00 18.53  ?  260 LYS A N     1 
ATOM   1912 C  CA    . LYS A 1 259 ? -3.266  67.607  75.473  1.00 18.55  ?  260 LYS A CA    1 
ATOM   1913 C  C     . LYS A 1 259 ? -1.866  67.042  75.766  1.00 18.86  ?  260 LYS A C     1 
ATOM   1914 O  O     . LYS A 1 259 ? -1.022  67.014  74.883  1.00 19.44  ?  260 LYS A O     1 
ATOM   1915 C  CB    . LYS A 1 259 ? -3.483  68.948  76.191  1.00 19.79  ?  260 LYS A CB    1 
ATOM   1916 C  CG    . LYS A 1 259 ? -4.545  69.806  75.545  1.00 22.80  ?  260 LYS A CG    1 
ATOM   1917 C  CD    . LYS A 1 259 ? -4.732  71.154  76.230  1.00 26.04  ?  260 LYS A CD    1 
ATOM   1918 C  CE    . LYS A 1 259 ? -5.949  71.868  75.670  1.00 30.32  ?  260 LYS A CE    1 
ATOM   1919 N  NZ    . LYS A 1 259 ? -6.603  72.763  76.676  1.00 32.82  1  260 LYS A NZ    1 
ATOM   1920 N  N     . LEU A 1 260 ? -1.660  66.495  76.949  1.00 19.17  ?  261 LEU A N     1 
ATOM   1921 C  CA    . LEU A 1 260 ? -0.380  65.898  77.327  1.00 20.59  ?  261 LEU A CA    1 
ATOM   1922 C  C     . LEU A 1 260 ? 0.056   64.757  76.410  1.00 20.79  ?  261 LEU A C     1 
ATOM   1923 O  O     . LEU A 1 260 ? 1.210   64.704  76.026  1.00 21.43  ?  261 LEU A O     1 
ATOM   1924 C  CB    . LEU A 1 260 ? -0.421  65.434  78.791  1.00 21.57  ?  261 LEU A CB    1 
ATOM   1925 C  CG    . LEU A 1 260 ? 0.898   65.452  79.534  1.00 24.26  ?  261 LEU A CG    1 
ATOM   1926 C  CD1   . LEU A 1 260 ? 1.609   66.836  79.424  1.00 24.30  ?  261 LEU A CD1   1 
ATOM   1927 C  CD2   . LEU A 1 260 ? 0.668   65.090  80.980  1.00 25.98  ?  261 LEU A CD2   1 
ATOM   1928 N  N     . SER A 1 261 ? -0.868  63.878  76.015  1.00 20.30  ?  262 SER A N     1 
ATOM   1929 C  CA    . SER A 1 261 ? -0.560  62.772  75.101  1.00 20.04  ?  262 SER A CA    1 
ATOM   1930 C  C     . SER A 1 261 ? -0.215  63.265  73.690  1.00 20.23  ?  262 SER A C     1 
ATOM   1931 O  O     . SER A 1 261 ? 0.770   62.808  73.111  1.00 20.46  ?  262 SER A O     1 
ATOM   1932 C  CB    . SER A 1 261 ? -1.743  61.804  75.016  1.00 20.27  ?  262 SER A CB    1 
ATOM   1933 O  OG    . SER A 1 261 ? -1.424  60.611  75.707  1.00 22.52  ?  262 SER A OG    1 
ATOM   1934 N  N     . THR A 1 262 ? -1.041  64.170  73.137  1.00 19.93  ?  263 THR A N     1 
ATOM   1935 C  CA    . THR A 1 262 ? -0.877  64.728  71.801  1.00 20.37  ?  263 THR A CA    1 
ATOM   1936 C  C     . THR A 1 262 ? 0.437   65.470  71.664  1.00 19.86  ?  263 THR A C     1 
ATOM   1937 O  O     . THR A 1 262 ? 1.164   65.200  70.718  1.00 20.59  ?  263 THR A O     1 
ATOM   1938 C  CB    . THR A 1 262 ? -2.090  65.586  71.450  1.00 22.09  ?  263 THR A CB    1 
ATOM   1939 O  OG1   . THR A 1 262 ? -3.239  64.766  71.564  1.00 23.23  ?  263 THR A OG1   1 
ATOM   1940 C  CG2   . THR A 1 262 ? -2.015  66.168  70.052  1.00 22.88  ?  263 THR A CG2   1 
ATOM   1941 N  N     . TYR A 1 263 ? 0.767   66.364  72.617  1.00 18.96  ?  264 TYR A N     1 
ATOM   1942 C  CA    . TYR A 1 263 ? 2.051   67.093  72.644  1.00 18.80  ?  264 TYR A CA    1 
ATOM   1943 C  C     . TYR A 1 263 ? 3.247   66.163  72.662  1.00 17.37  ?  264 TYR A C     1 
ATOM   1944 O  O     . TYR A 1 263 ? 4.214   66.422  71.975  1.00 17.29  ?  264 TYR A O     1 
ATOM   1945 C  CB    . TYR A 1 263 ? 2.151   68.040  73.857  1.00 19.32  ?  264 TYR A CB    1 
ATOM   1946 C  CG    . TYR A 1 263 ? 1.231   69.237  73.764  1.00 21.12  ?  264 TYR A CG    1 
ATOM   1947 C  CD1   . TYR A 1 263 ? 0.948   69.827  72.539  1.00 22.42  ?  264 TYR A CD1   1 
ATOM   1948 C  CD2   . TYR A 1 263 ? 0.673   69.800  74.904  1.00 22.81  ?  264 TYR A CD2   1 
ATOM   1949 C  CE1   . TYR A 1 263 ? 0.090   70.915  72.443  1.00 24.25  ?  264 TYR A CE1   1 
ATOM   1950 C  CE2   . TYR A 1 263 ? -0.183  70.894  74.824  1.00 24.55  ?  264 TYR A CE2   1 
ATOM   1951 C  CZ    . TYR A 1 263 ? -0.473  71.448  73.589  1.00 25.91  ?  264 TYR A CZ    1 
ATOM   1952 O  OH    . TYR A 1 263 ? -1.296  72.542  73.504  1.00 28.27  ?  264 TYR A OH    1 
ATOM   1953 N  N     . THR A 1 264 ? 3.191   65.096  73.458  1.00 16.58  ?  265 THR A N     1 
ATOM   1954 C  CA    . THR A 1 264 ? 4.268   64.129  73.557  1.00 16.47  ?  265 THR A CA    1 
ATOM   1955 C  C     . THR A 1 264 ? 4.425   63.346  72.257  1.00 16.69  ?  265 THR A C     1 
ATOM   1956 O  O     . THR A 1 264 ? 5.549   63.123  71.813  1.00 17.14  ?  265 THR A O     1 
ATOM   1957 C  CB    . THR A 1 264 ? 4.022   63.229  74.775  1.00 18.16  ?  265 THR A CB    1 
ATOM   1958 O  OG1   . THR A 1 264 ? 4.011   64.059  75.940  1.00 19.13  ?  265 THR A OG1   1 
ATOM   1959 C  CG2   . THR A 1 264 ? 5.085   62.115  74.920  1.00 18.56  ?  265 THR A CG2   1 
ATOM   1960 N  N     . PHE A 1 265 ? 3.300   62.927  71.655  1.00 16.31  ?  266 PHE A N     1 
ATOM   1961 C  CA    . PHE A 1 265 ? 3.227   62.202  70.386  1.00 17.00  ?  266 PHE A CA    1 
ATOM   1962 C  C     . PHE A 1 265 ? 3.818   63.052  69.249  1.00 18.64  ?  266 PHE A C     1 
ATOM   1963 O  O     . PHE A 1 265 ? 4.622   62.550  68.470  1.00 19.72  ?  266 PHE A O     1 
ATOM   1964 C  CB    . PHE A 1 265 ? 1.750   61.836  70.097  1.00 16.08  ?  266 PHE A CB    1 
ATOM   1965 C  CG    . PHE A 1 265 ? 1.402   61.378  68.705  1.00 15.61  ?  266 PHE A CG    1 
ATOM   1966 C  CD1   . PHE A 1 265 ? 1.625   60.072  68.314  1.00 16.23  ?  266 PHE A CD1   1 
ATOM   1967 C  CD2   . PHE A 1 265 ? 0.753   62.222  67.824  1.00 15.52  ?  266 PHE A CD2   1 
ATOM   1968 C  CE1   . PHE A 1 265 ? 1.287   59.647  67.035  1.00 16.89  ?  266 PHE A CE1   1 
ATOM   1969 C  CE2   . PHE A 1 265 ? 0.419   61.795  66.549  1.00 16.19  ?  266 PHE A CE2   1 
ATOM   1970 C  CZ    . PHE A 1 265 ? 0.682   60.510  66.163  1.00 16.19  ?  266 PHE A CZ    1 
ATOM   1971 N  N     . ALA A 1 266 ? 3.436   64.337  69.166  1.00 18.68  ?  267 ALA A N     1 
ATOM   1972 C  CA    . ALA A 1 266 ? 3.955   65.261  68.162  1.00 18.96  ?  267 ALA A CA    1 
ATOM   1973 C  C     . ALA A 1 266 ? 5.458   65.477  68.340  1.00 19.91  ?  267 ALA A C     1 
ATOM   1974 O  O     . ALA A 1 266 ? 6.178   65.565  67.344  1.00 20.10  ?  267 ALA A O     1 
ATOM   1975 C  CB    . ALA A 1 266 ? 3.222   66.594  68.243  1.00 18.34  ?  267 ALA A CB    1 
ATOM   1976 N  N     . MET A 1 267 ? 5.930   65.574  69.596  1.00 20.11  ?  268 MET A N     1 
ATOM   1977 C  CA    . MET A 1 267 ? 7.349   65.750  69.902  1.00 21.11  ?  268 MET A CA    1 
ATOM   1978 C  C     . MET A 1 267 ? 8.133   64.506  69.509  1.00 21.68  ?  268 MET A C     1 
ATOM   1979 O  O     . MET A 1 267 ? 9.192   64.616  68.913  1.00 22.25  ?  268 MET A O     1 
ATOM   1980 C  CB    . MET A 1 267 ? 7.559   66.047  71.395  1.00 22.52  ?  268 MET A CB    1 
ATOM   1981 C  CG    . MET A 1 267 ? 7.161   67.456  71.808  1.00 25.31  ?  268 MET A CG    1 
ATOM   1982 S  SD    . MET A 1 267 ? 7.186   67.631  73.617  1.00 32.93  ?  268 MET A SD    1 
ATOM   1983 C  CE    . MET A 1 267 ? 8.960   67.589  73.908  1.00 30.13  ?  268 MET A CE    1 
ATOM   1984 N  N     . LYS A 1 268 ? 7.593   63.322  69.779  1.00 21.97  ?  269 LYS A N     1 
ATOM   1985 C  CA    . LYS A 1 268 ? 8.220   62.054  69.418  1.00 22.88  ?  269 LYS A CA    1 
ATOM   1986 C  C     . LYS A 1 268 ? 8.463   61.969  67.898  1.00 24.44  ?  269 LYS A C     1 
ATOM   1987 O  O     . LYS A 1 268 ? 9.592   61.690  67.487  1.00 24.98  ?  269 LYS A O     1 
ATOM   1988 C  CB    . LYS A 1 268 ? 7.354   60.881  69.898  1.00 24.13  ?  269 LYS A CB    1 
ATOM   1989 C  CG    . LYS A 1 268 ? 7.695   60.348  71.285  1.00 27.03  ?  269 LYS A CG    1 
ATOM   1990 C  CD    . LYS A 1 268 ? 8.766   59.261  71.158  1.00 30.72  ?  269 LYS A CD    1 
ATOM   1991 C  CE    . LYS A 1 268 ? 9.009   58.411  72.387  1.00 32.41  ?  269 LYS A CE    1 
ATOM   1992 N  NZ    . LYS A 1 268 ? 7.929   57.431  72.650  1.00 32.39  1  269 LYS A NZ    1 
ATOM   1993 N  N     . LEU A 1 269 ? 7.434   62.283  67.069  1.00 24.56  ?  270 LEU A N     1 
ATOM   1994 C  CA    . LEU A 1 269 ? 7.556   62.244  65.603  1.00 25.44  ?  270 LEU A CA    1 
ATOM   1995 C  C     . LEU A 1 269 ? 8.578   63.216  65.010  1.00 26.96  ?  270 LEU A C     1 
ATOM   1996 O  O     . LEU A 1 269 ? 9.253   62.849  64.055  1.00 27.46  ?  270 LEU A O     1 
ATOM   1997 C  CB    . LEU A 1 269 ? 6.207   62.441  64.905  1.00 25.22  ?  270 LEU A CB    1 
ATOM   1998 C  CG    . LEU A 1 269 ? 5.140   61.424  65.250  1.00 25.97  ?  270 LEU A CG    1 
ATOM   1999 C  CD1   . LEU A 1 269 ? 3.774   61.991  64.981  1.00 26.85  ?  270 LEU A CD1   1 
ATOM   2000 C  CD2   . LEU A 1 269 ? 5.362   60.130  64.509  1.00 26.00  ?  270 LEU A CD2   1 
ATOM   2001 N  N     . THR A 1 270 ? 8.686   64.443  65.543  1.00 27.65  ?  271 THR A N     1 
ATOM   2002 C  CA    . THR A 1 270 ? 9.660   65.430  65.046  1.00 28.95  ?  271 THR A CA    1 
ATOM   2003 C  C     . THR A 1 270 ? 11.121  65.054  65.303  1.00 30.57  ?  271 THR A C     1 
ATOM   2004 O  O     . THR A 1 270 ? 12.015  65.681  64.736  1.00 30.85  ?  271 THR A O     1 
ATOM   2005 C  CB    . THR A 1 270 ? 9.371   66.828  65.576  1.00 29.65  ?  271 THR A CB    1 
ATOM   2006 O  OG1   . THR A 1 270 ? 9.539   66.832  66.992  1.00 30.21  ?  271 THR A OG1   1 
ATOM   2007 C  CG2   . THR A 1 270 ? 8.006   67.342  65.161  1.00 29.53  ?  271 THR A CG2   1 
ATOM   2008 N  N     . SER A 1 271 ? 11.367  64.050  66.155  1.00 31.68  ?  272 SER A N     1 
ATOM   2009 C  CA    . SER A 1 271 ? 12.707  63.521  66.424  1.00 33.03  ?  272 SER A CA    1 
ATOM   2010 C  C     . SER A 1 271 ? 13.109  62.436  65.401  1.00 34.76  ?  272 SER A C     1 
ATOM   2011 O  O     . SER A 1 271 ? 14.202  61.893  65.513  1.00 35.13  ?  272 SER A O     1 
ATOM   2012 C  CB    . SER A 1 271 ? 12.759  62.894  67.811  1.00 34.25  ?  272 SER A CB    1 
ATOM   2013 O  OG    . SER A 1 271 ? 13.044  63.846  68.821  1.00 36.72  ?  272 SER A OG    1 
ATOM   2014 N  N     . ASP A 1 272 ? 12.220  62.064  64.464  1.00 35.61  ?  273 ASP A N     1 
ATOM   2015 C  CA    . ASP A 1 272 ? 12.511  61.046  63.469  1.00 37.22  ?  273 ASP A CA    1 
ATOM   2016 C  C     . ASP A 1 272 ? 13.685  61.496  62.581  1.00 38.69  ?  273 ASP A C     1 
ATOM   2017 O  O     . ASP A 1 272 ? 13.786  62.681  62.253  1.00 38.98  ?  273 ASP A O     1 
ATOM   2018 C  CB    . ASP A 1 272 ? 11.255  60.771  62.628  1.00 39.03  ?  273 ASP A CB    1 
ATOM   2019 C  CG    . ASP A 1 272 ? 11.434  59.646  61.645  1.00 44.73  ?  273 ASP A CG    1 
ATOM   2020 O  OD1   . ASP A 1 272 ? 11.421  58.467  62.084  1.00 45.98  ?  273 ASP A OD1   1 
ATOM   2021 O  OD2   . ASP A 1 272 ? 11.597  59.936  60.435  1.00 47.13  -1 273 ASP A OD2   1 
ATOM   2022 N  N     . ALA A 1 273 ? 14.584  60.569  62.221  1.00 39.34  ?  274 ALA A N     1 
ATOM   2023 C  CA    . ALA A 1 273 ? 15.746  60.910  61.394  1.00 40.68  ?  274 ALA A CA    1 
ATOM   2024 C  C     . ALA A 1 273 ? 15.389  61.328  59.959  1.00 41.53  ?  274 ALA A C     1 
ATOM   2025 O  O     . ALA A 1 273 ? 15.936  62.309  59.465  1.00 41.52  ?  274 ALA A O     1 
ATOM   2026 C  CB    . ALA A 1 273 ? 16.737  59.751  61.376  1.00 41.20  ?  274 ALA A CB    1 
ATOM   2027 N  N     . ASN A 1 274 ? 14.471  60.597  59.300  1.00 42.30  ?  275 ASN A N     1 
ATOM   2028 C  CA    . ASN A 1 274 ? 14.052  60.899  57.931  1.00 43.73  ?  275 ASN A CA    1 
ATOM   2029 C  C     . ASN A 1 274 ? 13.354  62.238  57.842  1.00 44.69  ?  275 ASN A C     1 
ATOM   2030 O  O     . ASN A 1 274 ? 13.571  62.985  56.892  1.00 45.18  ?  275 ASN A O     1 
ATOM   2031 C  CB    . ASN A 1 274 ? 13.148  59.805  57.380  1.00 45.27  ?  275 ASN A CB    1 
ATOM   2032 C  CG    . ASN A 1 274 ? 13.860  58.500  57.141  1.00 49.02  ?  275 ASN A CG    1 
ATOM   2033 O  OD1   . ASN A 1 274 ? 15.091  58.439  57.075  1.00 49.81  ?  275 ASN A OD1   1 
ATOM   2034 N  ND2   . ASN A 1 274 ? 13.096  57.421  57.010  1.00 50.23  ?  275 ASN A ND2   1 
ATOM   2035 N  N     . LEU A 1 275 ? 12.527  62.558  58.839  1.00 44.88  ?  276 LEU A N     1 
ATOM   2036 C  CA    . LEU A 1 275 ? 11.812  63.822  58.889  1.00 45.78  ?  276 LEU A CA    1 
ATOM   2037 C  C     . LEU A 1 275 ? 12.781  64.998  58.903  1.00 47.30  ?  276 LEU A C     1 
ATOM   2038 O  O     . LEU A 1 275 ? 12.565  65.982  58.203  1.00 47.26  ?  276 LEU A O     1 
ATOM   2039 C  CB    . LEU A 1 275 ? 10.940  63.844  60.149  1.00 45.49  ?  276 LEU A CB    1 
ATOM   2040 C  CG    . LEU A 1 275 ? 10.155  65.113  60.394  1.00 46.20  ?  276 LEU A CG    1 
ATOM   2041 C  CD1   . LEU A 1 275 ? 8.770   64.785  60.812  1.00 46.51  ?  276 LEU A CD1   1 
ATOM   2042 C  CD2   . LEU A 1 275 ? 10.835  65.993  61.430  1.00 46.32  ?  276 LEU A CD2   1 
ATOM   2043 N  N     . LYS A 1 276 ? 13.850  64.881  59.698  1.00 48.76  ?  277 LYS A N     1 
ATOM   2044 C  CA    . LYS A 1 276 ? 14.863  65.912  59.864  1.00 50.77  ?  277 LYS A CA    1 
ATOM   2045 C  C     . LYS A 1 276 ? 15.670  66.206  58.586  1.00 53.40  ?  277 LYS A C     1 
ATOM   2046 O  O     . LYS A 1 276 ? 16.103  67.345  58.403  1.00 53.80  ?  277 LYS A O     1 
ATOM   2047 C  CB    . LYS A 1 276 ? 15.779  65.577  61.042  1.00 52.11  ?  277 LYS A CB    1 
ATOM   2048 C  CG    . LYS A 1 276 ? 15.082  65.666  62.390  1.00 55.10  ?  277 LYS A CG    1 
ATOM   2049 C  CD    . LYS A 1 276 ? 15.963  65.079  63.474  1.00 58.73  ?  277 LYS A CD    1 
ATOM   2050 C  CE    . LYS A 1 276 ? 15.416  65.321  64.852  1.00 61.88  ?  277 LYS A CE    1 
ATOM   2051 N  NZ    . LYS A 1 276 ? 16.338  64.811  65.903  1.00 64.02  ?  277 LYS A NZ    1 
ATOM   2052 N  N     . LYS A 1 277 ? 15.815  65.260  57.663  1.00 54.85  ?  278 LYS A N     1 
ATOM   2053 C  CA    . LYS A 1 277 ? 16.510  65.599  56.388  1.00 56.98  ?  278 LYS A CA    1 
ATOM   2054 C  C     . LYS A 1 277 ? 15.533  66.326  55.454  1.00 58.53  ?  278 LYS A C     1 
ATOM   2055 O  O     . LYS A 1 277 ? 15.994  67.180  54.691  1.00 59.20  ?  278 LYS A O     1 
ATOM   2056 C  CB    . LYS A 1 277 ? 17.121  64.340  55.763  1.00 59.48  ?  278 LYS A CB    1 
ATOM   2057 C  CG    . LYS A 1 277 ? 17.337  63.175  56.718  1.00 63.26  ?  278 LYS A CG    1 
ATOM   2058 C  CD    . LYS A 1 277 ? 17.426  61.833  56.025  1.00 67.35  ?  278 LYS A CD    1 
ATOM   2059 C  CE    . LYS A 1 277 ? 16.292  61.588  55.052  1.00 70.93  ?  278 LYS A CE    1 
ATOM   2060 N  NZ    . LYS A 1 277 ? 16.352  60.227  54.469  1.00 73.43  ?  278 LYS A NZ    1 
ATOM   2061 N  N     . SER A 1 278 ? 14.240  66.042  55.554  1.00 59.04  ?  279 SER A N     1 
ATOM   2062 C  CA    . SER A 1 278 ? 13.171  66.709  54.763  1.00 60.37  ?  279 SER A CA    1 
ATOM   2063 C  C     . SER A 1 278 ? 13.110  68.189  55.130  1.00 61.23  ?  279 SER A C     1 
ATOM   2064 O  O     . SER A 1 278 ? 12.556  68.961  54.349  1.00 61.35  ?  279 SER A O     1 
ATOM   2065 C  CB    . SER A 1 278 ? 11.838  66.073  54.979  1.00 62.00  ?  279 SER A CB    1 
ATOM   2066 O  OG    . SER A 1 278 ? 11.969  64.881  55.725  1.00 64.27  ?  279 SER A OG    1 
ATOM   2067 N  N     . LEU A 1 279 ? 13.536  68.537  56.330  1.00 61.63  ?  280 LEU A N     1 
ATOM   2068 C  CA    . LEU A 1 279 ? 13.396  69.919  56.843  1.00 62.63  ?  280 LEU A CA    1 
ATOM   2069 C  C     . LEU A 1 279 ? 14.274  70.877  56.044  1.00 64.08  ?  280 LEU A C     1 
ATOM   2070 O  O     . LEU A 1 279 ? 15.254  70.430  55.430  1.00 64.58  ?  280 LEU A O     1 
ATOM   2071 C  CB    . LEU A 1 279 ? 13.790  69.932  58.320  1.00 62.29  ?  280 LEU A CB    1 
ATOM   2072 C  CG    . LEU A 1 279 ? 12.718  69.396  59.263  1.00 63.10  ?  280 LEU A CG    1 
ATOM   2073 C  CD1   . LEU A 1 279 ? 13.243  69.303  60.683  1.00 63.51  ?  280 LEU A CD1   1 
ATOM   2074 C  CD2   . LEU A 1 279 ? 11.487  70.275  59.206  1.00 63.34  ?  280 LEU A CD2   1 
ATOM   2075 N  N     . PRO A 1 280 ? 13.921  72.185  56.001  1.00 64.42  ?  281 PRO A N     1 
ATOM   2076 C  CA    . PRO A 1 280 ? 14.812  73.170  55.428  1.00 64.98  ?  281 PRO A CA    1 
ATOM   2077 C  C     . PRO A 1 280 ? 15.968  73.191  56.436  1.00 65.50  ?  281 PRO A C     1 
ATOM   2078 O  O     . PRO A 1 280 ? 15.723  72.932  57.594  1.00 66.08  ?  281 PRO A O     1 
ATOM   2079 C  CB    . PRO A 1 280 ? 13.985  74.452  55.514  1.00 65.55  ?  281 PRO A CB    1 
ATOM   2080 C  CG    . PRO A 1 280 ? 12.558  73.996  55.546  1.00 65.70  ?  281 PRO A CG    1 
ATOM   2081 C  CD    . PRO A 1 280 ? 12.636  72.775  56.424  1.00 63.83  ?  281 PRO A CD    1 
ATOM   2082 N  N     . LYS A 1 281 ? 17.179  73.536  56.021  1.00 65.05  ?  282 LYS A N     1 
ATOM   2083 C  CA    . LYS A 1 281 ? 18.357  73.448  56.933  1.00 65.19  ?  282 LYS A CA    1 
ATOM   2084 C  C     . LYS A 1 281 ? 18.194  74.389  58.134  1.00 64.79  ?  282 LYS A C     1 
ATOM   2085 O  O     . LYS A 1 281 ? 18.634  73.998  59.227  1.00 65.13  ?  282 LYS A O     1 
ATOM   2086 C  CB    . LYS A 1 281 ? 19.658  73.735  56.171  1.00 67.40  ?  282 LYS A CB    1 
ATOM   2087 N  N     . ASN A 1 282 ? 17.639  75.583  57.939  1.00 63.68  ?  283 ASN A N     1 
ATOM   2088 C  CA    . ASN A 1 282 ? 17.552  76.563  59.054  1.00 62.70  ?  283 ASN A CA    1 
ATOM   2089 C  C     . ASN A 1 282 ? 16.119  76.591  59.573  1.00 60.42  ?  283 ASN A C     1 
ATOM   2090 O  O     . ASN A 1 282 ? 15.616  77.694  59.828  1.00 60.61  ?  283 ASN A O     1 
ATOM   2091 C  CB    . ASN A 1 282 ? 17.989  77.952  58.585  1.00 64.73  ?  283 ASN A CB    1 
ATOM   2092 C  CG    . ASN A 1 282 ? 18.265  78.929  59.705  1.00 68.69  ?  283 ASN A CG    1 
ATOM   2093 O  OD1   . ASN A 1 282 ? 17.594  79.952  59.813  1.00 69.96  ?  283 ASN A OD1   1 
ATOM   2094 N  ND2   . ASN A 1 282 ? 19.256  78.631  60.530  1.00 69.49  ?  283 ASN A ND2   1 
ATOM   2095 N  N     . HIS A 1 283 ? 15.492  75.426  59.750  1.00 58.08  ?  284 HIS A N     1 
ATOM   2096 C  CA    . HIS A 1 283 ? 14.047  75.469  60.105  1.00 56.14  ?  284 HIS A CA    1 
ATOM   2097 C  C     . HIS A 1 283 ? 13.881  76.156  61.461  1.00 53.81  ?  284 HIS A C     1 
ATOM   2098 O  O     . HIS A 1 283 ? 14.595  75.815  62.410  1.00 53.45  ?  284 HIS A O     1 
ATOM   2099 C  CB    . HIS A 1 283 ? 13.420  74.078  59.969  1.00 56.65  ?  284 HIS A CB    1 
ATOM   2100 C  CG    . HIS A 1 283 ? 11.953  74.059  60.228  1.00 58.37  ?  284 HIS A CG    1 
ATOM   2101 N  ND1   . HIS A 1 283 ? 11.360  73.170  61.096  1.00 59.63  ?  284 HIS A ND1   1 
ATOM   2102 C  CD2   . HIS A 1 283 ? 10.968  74.816  59.742  1.00 59.53  ?  284 HIS A CD2   1 
ATOM   2103 C  CE1   . HIS A 1 283 ? 10.058  73.392  61.123  1.00 60.15  ?  284 HIS A CE1   1 
ATOM   2104 N  NE2   . HIS A 1 283 ? 9.800   74.386  60.309  1.00 60.37  ?  284 HIS A NE2   1 
ATOM   2105 N  N     . ASN A 1 284 ? 12.892  77.041  61.553  1.00 52.08  ?  285 ASN A N     1 
ATOM   2106 C  CA    . ASN A 1 284 ? 12.680  77.838  62.785  1.00 50.70  ?  285 ASN A CA    1 
ATOM   2107 C  C     . ASN A 1 284 ? 11.214  78.260  62.797  1.00 48.14  ?  285 ASN A C     1 
ATOM   2108 O  O     . ASN A 1 284 ? 10.901  79.299  63.399  1.00 48.16  ?  285 ASN A O     1 
ATOM   2109 C  CB    . ASN A 1 284 ? 13.641  79.025  62.877  1.00 52.90  ?  285 ASN A CB    1 
ATOM   2110 C  CG    . ASN A 1 284 ? 15.018  78.648  63.379  1.00 58.24  ?  285 ASN A CG    1 
ATOM   2111 O  OD1   . ASN A 1 284 ? 15.154  78.036  64.435  1.00 59.88  ?  285 ASN A OD1   1 
ATOM   2112 N  ND2   . ASN A 1 284 ? 16.046  79.003  62.627  1.00 59.91  ?  285 ASN A ND2   1 
ATOM   2113 N  N     . GLY A 1 285 ? 10.364  77.477  62.138  1.00 45.76  ?  286 GLY A N     1 
ATOM   2114 C  CA    . GLY A 1 285 ? 8.939   77.762  62.118  1.00 44.15  ?  286 GLY A CA    1 
ATOM   2115 C  C     . GLY A 1 285 ? 8.059   76.746  62.817  1.00 41.92  ?  286 GLY A C     1 
ATOM   2116 O  O     . GLY A 1 285 ? 8.367   76.296  63.921  1.00 41.66  ?  286 GLY A O     1 
ATOM   2117 N  N     . PHE A 1 286 ? 6.939   76.393  62.181  1.00 39.94  ?  287 PHE A N     1 
ATOM   2118 C  CA    . PHE A 1 286 ? 5.971   75.466  62.756  1.00 38.29  ?  287 PHE A CA    1 
ATOM   2119 C  C     . PHE A 1 286 ? 6.058   74.016  62.241  1.00 35.95  ?  287 PHE A C     1 
ATOM   2120 O  O     . PHE A 1 286 ? 6.659   73.724  61.216  1.00 36.32  ?  287 PHE A O     1 
ATOM   2121 C  CB    . PHE A 1 286 ? 4.539   75.992  62.509  1.00 38.64  ?  287 PHE A CB    1 
ATOM   2122 C  CG    . PHE A 1 286 ? 4.037   77.061  63.444  1.00 39.58  ?  287 PHE A CG    1 
ATOM   2123 C  CD1   . PHE A 1 286 ? 4.233   76.957  64.812  1.00 40.09  ?  287 PHE A CD1   1 
ATOM   2124 C  CD2   . PHE A 1 286 ? 3.288   78.127  62.967  1.00 40.86  ?  287 PHE A CD2   1 
ATOM   2125 C  CE1   . PHE A 1 286 ? 3.740   77.924  65.678  1.00 40.67  ?  287 PHE A CE1   1 
ATOM   2126 C  CE2   . PHE A 1 286 ? 2.777   79.088  63.840  1.00 41.54  ?  287 PHE A CE2   1 
ATOM   2127 C  CZ    . PHE A 1 286 ? 3.017   78.985  65.189  1.00 40.98  ?  287 PHE A CZ    1 
ATOM   2128 N  N     . PHE A 1 287 ? 5.430   73.115  62.973  1.00 33.63  ?  288 PHE A N     1 
ATOM   2129 C  CA    . PHE A 1 287 ? 5.228   71.722  62.604  1.00 32.06  ?  288 PHE A CA    1 
ATOM   2130 C  C     . PHE A 1 287 ? 3.745   71.508  62.792  1.00 30.21  ?  288 PHE A C     1 
ATOM   2131 O  O     . PHE A 1 287 ? 3.202   71.836  63.854  1.00 29.54  ?  288 PHE A O     1 
ATOM   2132 C  CB    . PHE A 1 287 ? 5.997   70.763  63.517  1.00 31.56  ?  288 PHE A CB    1 
ATOM   2133 C  CG    . PHE A 1 287 ? 7.416   70.510  63.090  1.00 32.01  ?  288 PHE A CG    1 
ATOM   2134 C  CD1   . PHE A 1 287 ? 7.692   69.872  61.895  1.00 32.84  ?  288 PHE A CD1   1 
ATOM   2135 C  CD2   . PHE A 1 287 ? 8.477   70.910  63.884  1.00 32.41  ?  288 PHE A CD2   1 
ATOM   2136 C  CE1   . PHE A 1 287 ? 9.006   69.628  61.504  1.00 33.35  ?  288 PHE A CE1   1 
ATOM   2137 C  CE2   . PHE A 1 287 ? 9.785   70.669  63.489  1.00 33.01  ?  288 PHE A CE2   1 
ATOM   2138 C  CZ    . PHE A 1 287 ? 10.042  70.021  62.308  1.00 32.84  ?  288 PHE A CZ    1 
ATOM   2139 N  N     . LEU A 1 288 ? 3.073   71.008  61.758  1.00 29.09  ?  289 LEU A N     1 
ATOM   2140 C  CA    . LEU A 1 288 ? 1.658   70.732  61.847  1.00 28.07  ?  289 LEU A CA    1 
ATOM   2141 C  C     . LEU A 1 288 ? 1.498   69.218  61.889  1.00 27.47  ?  289 LEU A C     1 
ATOM   2142 O  O     . LEU A 1 288 ? 1.772   68.544  60.908  1.00 27.55  ?  289 LEU A O     1 
ATOM   2143 C  CB    . LEU A 1 288 ? 0.912   71.365  60.667  1.00 28.55  ?  289 LEU A CB    1 
ATOM   2144 C  CG    . LEU A 1 288 ? -0.577  71.024  60.522  1.00 30.58  ?  289 LEU A CG    1 
ATOM   2145 C  CD1   . LEU A 1 288 ? -1.370  71.427  61.737  1.00 31.01  ?  289 LEU A CD1   1 
ATOM   2146 C  CD2   . LEU A 1 288 ? -1.159  71.716  59.330  1.00 31.43  ?  289 LEU A CD2   1 
ATOM   2147 N  N     . VAL A 1 289 ? 1.079   68.677  63.043  1.00 26.52  ?  290 VAL A N     1 
ATOM   2148 C  CA    . VAL A 1 289 ? 0.895   67.240  63.209  1.00 25.71  ?  290 VAL A CA    1 
ATOM   2149 C  C     . VAL A 1 289 ? -0.588  66.930  63.120  1.00 25.81  ?  290 VAL A C     1 
ATOM   2150 O  O     . VAL A 1 289 ? -1.374  67.516  63.846  1.00 25.53  ?  290 VAL A O     1 
ATOM   2151 C  CB    . VAL A 1 289 ? 1.535   66.742  64.522  1.00 25.40  ?  290 VAL A CB    1 
ATOM   2152 C  CG1   . VAL A 1 289 ? 1.447   65.224  64.628  1.00 25.79  ?  290 VAL A CG1   1 
ATOM   2153 C  CG2   . VAL A 1 289 ? 2.986   67.208  64.619  1.00 25.43  ?  290 VAL A CG2   1 
ATOM   2154 N  N     . ARG A 1 290 ? -0.972  66.048  62.194  1.00 26.25  ?  291 ARG A N     1 
ATOM   2155 C  CA    . ARG A 1 290 ? -2.360  65.708  61.927  1.00 27.42  ?  291 ARG A CA    1 
ATOM   2156 C  C     . ARG A 1 290 ? -2.532  64.190  61.805  1.00 27.35  ?  291 ARG A C     1 
ATOM   2157 O  O     . ARG A 1 290 ? -1.702  63.532  61.181  1.00 27.42  ?  291 ARG A O     1 
ATOM   2158 C  CB    . ARG A 1 290 ? -2.815  66.409  60.620  1.00 30.89  ?  291 ARG A CB    1 
ATOM   2159 C  CG    . ARG A 1 290 ? -3.999  65.743  59.886  1.00 38.83  ?  291 ARG A CG    1 
ATOM   2160 C  CD    . ARG A 1 290 ? -4.474  66.464  58.630  1.00 46.87  ?  291 ARG A CD    1 
ATOM   2161 N  NE    . ARG A 1 290 ? -3.624  66.235  57.458  1.00 53.77  ?  291 ARG A NE    1 
ATOM   2162 C  CZ    . ARG A 1 290 ? -2.799  67.143  56.938  1.00 58.59  ?  291 ARG A CZ    1 
ATOM   2163 N  NH1   . ARG A 1 290 ? -2.699  68.351  57.484  1.00 58.12  1  291 ARG A NH1   1 
ATOM   2164 N  NH2   . ARG A 1 290 ? -2.066  66.849  55.870  1.00 60.12  ?  291 ARG A NH2   1 
ATOM   2165 N  N     . MET A 1 291 ? -3.607  63.636  62.385  1.00 26.96  ?  292 MET A N     1 
ATOM   2166 C  CA    . MET A 1 291 ? -3.919  62.221  62.203  1.00 28.01  ?  292 MET A CA    1 
ATOM   2167 C  C     . MET A 1 291 ? -5.333  62.117  61.661  1.00 29.25  ?  292 MET A C     1 
ATOM   2168 O  O     . MET A 1 291 ? -6.243  62.753  62.194  1.00 28.89  ?  292 MET A O     1 
ATOM   2169 C  CB    . MET A 1 291 ? -3.769  61.355  63.466  1.00 28.27  ?  292 MET A CB    1 
ATOM   2170 C  CG    . MET A 1 291 ? -3.978  59.878  63.153  1.00 30.23  ?  292 MET A CG    1 
ATOM   2171 S  SD    . MET A 1 291 ? -4.316  58.791  64.552  1.00 36.29  ?  292 MET A SD    1 
ATOM   2172 C  CE    . MET A 1 291 ? -2.776  58.433  65.034  1.00 34.17  ?  292 MET A CE    1 
ATOM   2173 N  N     . ARG A 1 292 ? -5.508  61.363  60.581  1.00 30.65  ?  293 ARG A N     1 
ATOM   2174 C  CA    . ARG A 1 292 ? -6.830  61.192  60.004  1.00 33.11  ?  293 ARG A CA    1 
ATOM   2175 C  C     . ARG A 1 292 ? -7.149  59.754  59.639  1.00 34.95  ?  293 ARG A C     1 
ATOM   2176 O  O     . ARG A 1 292 ? -6.250  58.938  59.471  1.00 34.87  ?  293 ARG A O     1 
ATOM   2177 C  CB    . ARG A 1 292 ? -7.011  62.106  58.793  1.00 35.09  ?  293 ARG A CB    1 
ATOM   2178 C  CG    . ARG A 1 292 ? -6.126  61.735  57.609  1.00 39.20  ?  293 ARG A CG    1 
ATOM   2179 C  CD    . ARG A 1 292 ? -6.828  61.975  56.282  1.00 44.30  ?  293 ARG A CD    1 
ATOM   2180 N  NE    . ARG A 1 292 ? -7.478  63.284  56.246  1.00 48.92  ?  293 ARG A NE    1 
ATOM   2181 C  CZ    . ARG A 1 292 ? -6.868  64.420  55.931  1.00 51.98  ?  293 ARG A CZ    1 
ATOM   2182 N  NH1   . ARG A 1 292 ? -5.594  64.415  55.556  1.00 51.98  1  293 ARG A NH1   1 
ATOM   2183 N  NH2   . ARG A 1 292 ? -7.530  65.570  55.976  1.00 51.90  ?  293 ARG A NH2   1 
ATOM   2184 N  N     . ASN A 1 293 ? -8.435  59.441  59.520  1.00 36.70  ?  294 ASN A N     1 
ATOM   2185 C  CA    . ASN A 1 293 ? -8.873  58.121  59.099  1.00 38.76  ?  294 ASN A CA    1 
ATOM   2186 C  C     . ASN A 1 293 ? -8.525  57.915  57.624  1.00 40.37  ?  294 ASN A C     1 
ATOM   2187 O  O     . ASN A 1 293 ? -8.587  58.849  56.832  1.00 40.43  ?  294 ASN A O     1 
ATOM   2188 C  CB    . ASN A 1 293 ? -10.389 58.030  59.247  1.00 41.36  ?  294 ASN A CB    1 
ATOM   2189 C  CG    . ASN A 1 293 ? -10.869 57.605  60.617  1.00 46.70  ?  294 ASN A CG    1 
ATOM   2190 O  OD1   . ASN A 1 293 ? -11.108 56.408  60.876  1.00 48.79  ?  294 ASN A OD1   1 
ATOM   2191 N  ND2   . ASN A 1 293 ? -11.040 58.575  61.514  1.00 47.17  ?  294 ASN A ND2   1 
ATOM   2192 N  N     . ALA A 1 294 ? -8.172  56.699  57.251  1.00 42.01  ?  295 ALA A N     1 
ATOM   2193 C  CA    . ALA A 1 294 ? -7.933  56.342  55.854  1.00 44.41  ?  295 ALA A CA    1 
ATOM   2194 C  C     . ALA A 1 294 ? -9.238  55.748  55.285  1.00 47.19  ?  295 ALA A C     1 
ATOM   2195 O  O     . ALA A 1 294 ? -10.118 55.343  56.057  1.00 47.46  ?  295 ALA A O     1 
ATOM   2196 C  CB    . ALA A 1 294 ? -6.819  55.313  55.759  1.00 44.52  ?  295 ALA A CB    1 
ATOM   2197 N  N     . ILE A 1 295 ? -9.375  55.687  53.941  1.00 49.05  ?  296 ILE A N     1 
ATOM   2198 C  CA    . ILE A 1 295 ? -10.567 55.094  53.334  1.00 50.95  ?  296 ILE A CA    1 
ATOM   2199 C  C     . ILE A 1 295 ? -10.495 53.570  53.418  1.00 52.13  ?  296 ILE A C     1 
ATOM   2200 O  O     . ILE A 1 295 ? -11.388 52.940  53.990  1.00 52.88  ?  296 ILE A O     1 
ATOM   2201 C  CB    . ILE A 1 295 ? -10.790 55.546  51.876  1.00 52.23  ?  296 ILE A CB    1 
ATOM   2202 C  CG1   . ILE A 1 295 ? -10.677 57.068  51.725  1.00 53.01  ?  296 ILE A CG1   1 
ATOM   2203 C  CG2   . ILE A 1 295 ? -12.146 55.031  51.381  1.00 53.25  ?  296 ILE A CG2   1 
ATOM   2204 C  CD1   . ILE A 1 295 ? -10.769 57.547  50.279  1.00 54.53  ?  296 ILE A CD1   1 
ATOM   2205 N  N     . GLY A 1 303 ? -10.213 49.897  59.297  1.00 39.84  ?  304 GLY A N     1 
ATOM   2206 C  CA    . GLY A 1 303 ? -9.452  50.641  60.286  1.00 39.49  ?  304 GLY A CA    1 
ATOM   2207 C  C     . GLY A 1 303 ? -8.017  50.854  59.861  1.00 39.59  ?  304 GLY A C     1 
ATOM   2208 O  O     . GLY A 1 303 ? -7.206  49.924  59.886  1.00 40.88  ?  304 GLY A O     1 
ATOM   2209 N  N     . LYS A 1 304 ? -7.693  52.084  59.457  1.00 37.94  ?  305 LYS A N     1 
ATOM   2210 C  CA    . LYS A 1 304 ? -6.354  52.498  59.025  1.00 36.39  ?  305 LYS A CA    1 
ATOM   2211 C  C     . LYS A 1 304 ? -6.271  54.019  59.208  1.00 33.53  ?  305 LYS A C     1 
ATOM   2212 O  O     . LYS A 1 304 ? -7.278  54.717  59.103  1.00 32.76  ?  305 LYS A O     1 
ATOM   2213 C  CB    . LYS A 1 304 ? -6.101  52.098  57.564  1.00 39.53  ?  305 LYS A CB    1 
ATOM   2214 C  CG    . LYS A 1 304 ? -4.740  51.447  57.299  1.00 44.25  ?  305 LYS A CG    1 
ATOM   2215 C  CD    . LYS A 1 304 ? -4.861  49.947  56.989  1.00 49.60  ?  305 LYS A CD    1 
ATOM   2216 C  CE    . LYS A 1 304 ? -5.792  49.651  55.830  1.00 54.17  ?  305 LYS A CE    1 
ATOM   2217 N  NZ    . LYS A 1 304 ? -5.932  48.189  55.587  1.00 56.64  1  305 LYS A NZ    1 
ATOM   2218 N  N     . PHE A 1 305 ? -5.099  54.520  59.574  1.00 32.00  ?  306 PHE A N     1 
ATOM   2219 C  CA    . PHE A 1 305 ? -4.929  55.942  59.874  1.00 30.89  ?  306 PHE A CA    1 
ATOM   2220 C  C     . PHE A 1 305 ? -3.688  56.495  59.230  1.00 30.08  ?  306 PHE A C     1 
ATOM   2221 O  O     . PHE A 1 305 ? -2.715  55.776  59.069  1.00 30.02  ?  306 PHE A O     1 
ATOM   2222 C  CB    . PHE A 1 305 ? -4.864  56.166  61.402  1.00 30.02  ?  306 PHE A CB    1 
ATOM   2223 C  CG    . PHE A 1 305 ? -6.168  55.927  62.130  1.00 29.79  ?  306 PHE A CG    1 
ATOM   2224 C  CD1   . PHE A 1 305 ? -6.478  54.680  62.642  1.00 30.41  ?  306 PHE A CD1   1 
ATOM   2225 C  CD2   . PHE A 1 305 ? -7.085  56.946  62.292  1.00 29.84  ?  306 PHE A CD2   1 
ATOM   2226 C  CE1   . PHE A 1 305 ? -7.689  54.454  63.279  1.00 30.72  ?  306 PHE A CE1   1 
ATOM   2227 C  CE2   . PHE A 1 305 ? -8.282  56.721  62.947  1.00 30.49  ?  306 PHE A CE2   1 
ATOM   2228 C  CZ    . PHE A 1 305 ? -8.575  55.477  63.439  1.00 30.36  ?  306 PHE A CZ    1 
ATOM   2229 N  N     . LEU A 1 306 ? -3.721  57.765  58.837  1.00 29.63  ?  307 LEU A N     1 
ATOM   2230 C  CA    . LEU A 1 306 ? -2.552  58.411  58.247  1.00 29.69  ?  307 LEU A CA    1 
ATOM   2231 C  C     . LEU A 1 306 ? -2.115  59.530  59.184  1.00 28.36  ?  307 LEU A C     1 
ATOM   2232 O  O     . LEU A 1 306 ? -2.934  60.335  59.604  1.00 27.93  ?  307 LEU A O     1 
ATOM   2233 C  CB    . LEU A 1 306 ? -2.833  58.969  56.838  1.00 30.62  ?  307 LEU A CB    1 
ATOM   2234 C  CG    . LEU A 1 306 ? -2.689  58.040  55.599  1.00 32.51  ?  307 LEU A CG    1 
ATOM   2235 C  CD1   . LEU A 1 306 ? -1.364  57.342  55.546  1.00 33.20  ?  307 LEU A CD1   1 
ATOM   2236 C  CD2   . LEU A 1 306 ? -3.791  57.058  55.512  1.00 33.18  ?  307 LEU A CD2   1 
ATOM   2237 N  N     . VAL A 1 307 ? -0.833  59.545  59.541  1.00 27.60  ?  308 VAL A N     1 
ATOM   2238 C  CA    . VAL A 1 307 ? -0.241  60.556  60.397  1.00 26.98  ?  308 VAL A CA    1 
ATOM   2239 C  C     . VAL A 1 307 ? 0.753   61.341  59.559  1.00 27.12  ?  308 VAL A C     1 
ATOM   2240 O  O     . VAL A 1 307 ? 1.615   60.736  58.940  1.00 27.01  ?  308 VAL A O     1 
ATOM   2241 C  CB    . VAL A 1 307 ? 0.483   59.901  61.600  1.00 26.60  ?  308 VAL A CB    1 
ATOM   2242 C  CG1   . VAL A 1 307 ? 1.188   60.946  62.474  1.00 26.49  ?  308 VAL A CG1   1 
ATOM   2243 C  CG2   . VAL A 1 307 ? -0.471  59.044  62.407  1.00 26.50  ?  308 VAL A CG2   1 
ATOM   2244 N  N     . SER A 1 308 ? 0.658   62.676  59.550  1.00 27.51  ?  309 SER A N     1 
ATOM   2245 C  CA    . SER A 1 308 ? 1.608   63.503  58.819  1.00 28.86  ?  309 SER A CA    1 
ATOM   2246 C  C     . SER A 1 308 ? 2.190   64.616  59.691  1.00 29.42  ?  309 SER A C     1 
ATOM   2247 O  O     . SER A 1 308 ? 1.528   65.097  60.607  1.00 29.56  ?  309 SER A O     1 
ATOM   2248 C  CB    . SER A 1 308 ? 0.962   64.104  57.576  1.00 31.23  ?  309 SER A CB    1 
ATOM   2249 O  OG    . SER A 1 308 ? -0.257  64.748  57.910  1.00 34.82  ?  309 SER A OG    1 
ATOM   2250 N  N     . VAL A 1 309 ? 3.432   65.015  59.417  1.00 29.55  ?  310 VAL A N     1 
ATOM   2251 C  CA    . VAL A 1 309 ? 4.061   66.120  60.128  1.00 30.53  ?  310 VAL A CA    1 
ATOM   2252 C  C     . VAL A 1 309 ? 4.469   67.080  59.047  1.00 32.20  ?  310 VAL A C     1 
ATOM   2253 O  O     . VAL A 1 309 ? 5.295   66.731  58.223  1.00 32.87  ?  310 VAL A O     1 
ATOM   2254 C  CB    . VAL A 1 309 ? 5.277   65.720  60.989  1.00 30.91  ?  310 VAL A CB    1 
ATOM   2255 C  CG1   . VAL A 1 309 ? 5.924   66.953  61.576  1.00 31.37  ?  310 VAL A CG1   1 
ATOM   2256 C  CG2   . VAL A 1 309 ? 4.888   64.750  62.095  1.00 31.05  ?  310 VAL A CG2   1 
ATOM   2257 N  N     . LYS A 1 310 ? 3.865   68.260  59.009  1.00 32.79  ?  311 LYS A N     1 
ATOM   2258 C  CA    . LYS A 1 310 ? 4.111   69.221  57.959  1.00 34.17  ?  311 LYS A CA    1 
ATOM   2259 C  C     . LYS A 1 310 ? 4.959   70.401  58.407  1.00 35.20  ?  311 LYS A C     1 
ATOM   2260 O  O     . LYS A 1 310 ? 4.521   71.224  59.206  1.00 35.37  ?  311 LYS A O     1 
ATOM   2261 C  CB    . LYS A 1 310 ? 2.774   69.686  57.372  1.00 36.40  ?  311 LYS A CB    1 
ATOM   2262 C  CG    . LYS A 1 310 ? 2.903   70.620  56.191  1.00 42.17  ?  311 LYS A CG    1 
ATOM   2263 C  CD    . LYS A 1 310 ? 1.528   70.942  55.589  1.00 48.70  ?  311 LYS A CD    1 
ATOM   2264 C  CE    . LYS A 1 310 ? 1.618   71.767  54.319  1.00 53.77  ?  311 LYS A CE    1 
ATOM   2265 N  NZ    . LYS A 1 310 ? 0.279   72.265  53.896  1.00 56.43  1  311 LYS A NZ    1 
ATOM   2266 N  N     . PRO A 1 311 ? 6.182   70.516  57.872  1.00 35.86  ?  312 PRO A N     1 
ATOM   2267 C  CA    . PRO A 1 311 ? 7.042   71.645  58.247  1.00 36.62  ?  312 PRO A CA    1 
ATOM   2268 C  C     . PRO A 1 311 ? 6.577   72.945  57.609  1.00 38.47  ?  312 PRO A C     1 
ATOM   2269 O  O     . PRO A 1 311 ? 6.045   72.946  56.507  1.00 39.03  ?  312 PRO A O     1 
ATOM   2270 C  CB    . PRO A 1 311 ? 8.421   71.239  57.713  1.00 36.86  ?  312 PRO A CB    1 
ATOM   2271 C  CG    . PRO A 1 311 ? 8.293   69.824  57.279  1.00 37.01  ?  312 PRO A CG    1 
ATOM   2272 C  CD    . PRO A 1 311 ? 6.862   69.617  56.930  1.00 35.47  ?  312 PRO A CD    1 
ATOM   2273 N  N     . PHE A 1 312 ? 6.764   74.050  58.309  1.00 39.41  ?  313 PHE A N     1 
ATOM   2274 C  CA    . PHE A 1 312 ? 6.396   75.368  57.810  1.00 41.09  ?  313 PHE A CA    1 
ATOM   2275 C  C     . PHE A 1 312 ? 7.490   76.347  58.180  1.00 43.97  ?  313 PHE A C     1 
ATOM   2276 O  O     . PHE A 1 312 ? 8.018   76.279  59.294  1.00 44.19  ?  313 PHE A O     1 
ATOM   2277 C  CB    . PHE A 1 312 ? 5.089   75.854  58.450  1.00 40.15  ?  313 PHE A CB    1 
ATOM   2278 C  CG    . PHE A 1 312 ? 3.826   75.341  57.807  1.00 39.98  ?  313 PHE A CG    1 
ATOM   2279 C  CD1   . PHE A 1 312 ? 3.291   75.969  56.698  1.00 40.40  ?  313 PHE A CD1   1 
ATOM   2280 C  CD2   . PHE A 1 312 ? 3.151   74.257  58.338  1.00 40.07  ?  313 PHE A CD2   1 
ATOM   2281 C  CE1   . PHE A 1 312 ? 2.119   75.506  56.120  1.00 40.97  ?  313 PHE A CE1   1 
ATOM   2282 C  CE2   . PHE A 1 312 ? 1.983   73.793  57.752  1.00 40.59  ?  313 PHE A CE2   1 
ATOM   2283 C  CZ    . PHE A 1 312 ? 1.473   74.420  56.650  1.00 40.51  ?  313 PHE A CZ    1 
ATOM   2284 N  N     . ARG A 1 313 ? 7.825   77.270  57.273  1.00 45.91  ?  314 ARG A N     1 
ATOM   2285 C  CA    . ARG A 1 313 ? 8.800   78.310  57.590  1.00 48.09  ?  314 ARG A CA    1 
ATOM   2286 C  C     . ARG A 1 313 ? 8.107   79.346  58.480  1.00 49.72  ?  314 ARG A C     1 
ATOM   2287 O  O     . ARG A 1 313 ? 6.876   79.442  58.458  1.00 49.81  ?  314 ARG A O     1 
ATOM   2288 C  CB    . ARG A 1 313 ? 9.352   78.959  56.310  1.00 50.45  ?  314 ARG A CB    1 
ATOM   2289 C  CG    . ARG A 1 313 ? 10.037  77.952  55.400  1.00 54.85  ?  314 ARG A CG    1 
ATOM   2290 C  CD    . ARG A 1 313 ? 10.926  78.610  54.373  1.00 59.76  ?  314 ARG A CD    1 
ATOM   2291 N  NE    . ARG A 1 313 ? 10.174  79.174  53.249  1.00 64.29  ?  314 ARG A NE    1 
ATOM   2292 C  CZ    . ARG A 1 313 ? 10.331  80.416  52.792  1.00 67.61  ?  314 ARG A CZ    1 
ATOM   2293 N  NH1   . ARG A 1 313 ? 11.179  81.250  53.387  1.00 67.58  1  314 ARG A NH1   1 
ATOM   2294 N  NH2   . ARG A 1 313 ? 9.617   80.845  51.758  1.00 67.56  ?  314 ARG A NH2   1 
ATOM   2295 N  N     . LYS A 1 314 ? 8.874   80.124  59.260  1.00 51.04  ?  315 LYS A N     1 
ATOM   2296 C  CA    . LYS A 1 314 ? 8.287   81.133  60.148  1.00 52.97  ?  315 LYS A CA    1 
ATOM   2297 C  C     . LYS A 1 314 ? 7.459   82.175  59.396  1.00 54.83  ?  315 LYS A C     1 
ATOM   2298 O  O     . LYS A 1 314 ? 6.478   82.686  59.933  1.00 54.89  ?  315 LYS A O     1 
ATOM   2299 C  CB    . LYS A 1 314 ? 9.363   81.822  60.986  1.00 55.42  ?  315 LYS A CB    1 
ATOM   2300 C  CG    . LYS A 1 314 ? 8.862   82.219  62.366  1.00 60.68  ?  315 LYS A CG    1 
ATOM   2301 C  CD    . LYS A 1 314 ? 9.344   83.603  62.754  1.00 66.74  ?  315 LYS A CD    1 
ATOM   2302 C  CE    . LYS A 1 314 ? 8.636   84.674  61.954  1.00 71.75  ?  315 LYS A CE    1 
ATOM   2303 N  NZ    . LYS A 1 314 ? 9.240   86.017  62.164  1.00 74.47  1  315 LYS A NZ    1 
ATOM   2304 N  N     . LYS A 1 315 ? 7.844   82.475  58.148  1.00 56.19  ?  316 LYS A N     1 
ATOM   2305 C  CA    . LYS A 1 315 ? 7.124   83.432  57.308  1.00 57.98  ?  316 LYS A CA    1 
ATOM   2306 C  C     . LYS A 1 315 ? 5.757   82.890  56.865  1.00 59.08  ?  316 LYS A C     1 
ATOM   2307 O  O     . LYS A 1 315 ? 4.837   83.673  56.626  1.00 59.80  ?  316 LYS A O     1 
ATOM   2308 C  CB    . LYS A 1 315 ? 7.975   83.825  56.084  1.00 60.70  ?  316 LYS A CB    1 
ATOM   2309 C  CG    . LYS A 1 315 ? 9.410   84.210  56.443  1.00 65.19  ?  316 LYS A CG    1 
ATOM   2310 C  CD    . LYS A 1 315 ? 9.995   85.242  55.491  1.00 69.96  ?  316 LYS A CD    1 
ATOM   2311 C  CE    . LYS A 1 315 ? 11.192  85.932  56.103  1.00 73.37  ?  316 LYS A CE    1 
ATOM   2312 N  NZ    . LYS A 1 315 ? 11.476  87.232  55.440  1.00 75.81  ?  316 LYS A NZ    1 
ATOM   2313 N  N     . GLU A 1 316 ? 5.617   81.552  56.776  1.00 59.13  ?  317 GLU A N     1 
ATOM   2314 C  CA    . GLU A 1 316 ? 4.382   80.885  56.374  1.00 59.55  ?  317 GLU A CA    1 
ATOM   2315 C  C     . GLU A 1 316 ? 3.470   80.555  57.557  1.00 58.99  ?  317 GLU A C     1 
ATOM   2316 O  O     . GLU A 1 316 ? 2.656   79.643  57.440  1.00 58.96  ?  317 GLU A O     1 
ATOM   2317 C  CB    . GLU A 1 316 ? 4.701   79.593  55.601  1.00 62.53  ?  317 GLU A CB    1 
ATOM   2318 C  CG    . GLU A 1 316 ? 5.688   79.778  54.462  1.00 68.90  ?  317 GLU A CG    1 
ATOM   2319 C  CD    . GLU A 1 316 ? 6.328   78.496  53.959  1.00 76.29  ?  317 GLU A CD    1 
ATOM   2320 O  OE1   . GLU A 1 316 ? 5.802   77.400  54.266  1.00 77.37  ?  317 GLU A OE1   1 
ATOM   2321 O  OE2   . GLU A 1 316 ? 7.361   78.588  53.256  1.00 78.91  -1 317 GLU A OE2   1 
ATOM   2322 N  N     . SER A 1 317 ? 3.592   81.280  58.683  1.00 58.65  ?  318 SER A N     1 
ATOM   2323 C  CA    . SER A 1 317 ? 2.782   81.023  59.880  1.00 59.03  ?  318 SER A CA    1 
ATOM   2324 C  C     . SER A 1 317 ? 1.275   81.218  59.669  1.00 59.52  ?  318 SER A C     1 
ATOM   2325 O  O     . SER A 1 317 ? 0.471   80.489  60.256  1.00 59.53  ?  318 SER A O     1 
ATOM   2326 C  CB    . SER A 1 317 ? 3.276   81.847  61.068  1.00 60.24  ?  318 SER A CB    1 
ATOM   2327 O  OG    . SER A 1 317 ? 4.419   81.266  61.676  1.00 62.16  ?  318 SER A OG    1 
ATOM   2328 N  N     . GLU A 1 318 ? 0.890   82.177  58.823  1.00 59.69  ?  319 GLU A N     1 
ATOM   2329 C  CA    . GLU A 1 318 ? -0.524  82.420  58.518  1.00 60.12  ?  319 GLU A CA    1 
ATOM   2330 C  C     . GLU A 1 318 ? -1.108  81.263  57.699  1.00 59.34  ?  319 GLU A C     1 
ATOM   2331 O  O     . GLU A 1 318 ? -2.263  80.883  57.893  1.00 59.49  ?  319 GLU A O     1 
ATOM   2332 C  CB    . GLU A 1 318 ? -0.688  83.755  57.773  1.00 63.66  ?  319 GLU A CB    1 
ATOM   2333 C  CG    . GLU A 1 318 ? -0.891  84.933  58.704  1.00 69.83  ?  319 GLU A CG    1 
ATOM   2334 C  CD    . GLU A 1 318 ? -2.174  84.837  59.506  1.00 78.48  ?  319 GLU A CD    1 
ATOM   2335 O  OE1   . GLU A 1 318 ? -2.091  84.628  60.739  1.00 80.09  ?  319 GLU A OE1   1 
ATOM   2336 O  OE2   . GLU A 1 318 ? -3.264  84.961  58.901  1.00 81.61  -1 319 GLU A OE2   1 
ATOM   2337 N  N     . GLN A 1 319 ? -0.294  80.706  56.785  1.00 58.47  ?  320 GLN A N     1 
ATOM   2338 C  CA    . GLN A 1 319 ? -0.638  79.556  55.950  1.00 58.02  ?  320 GLN A CA    1 
ATOM   2339 C  C     . GLN A 1 319 ? -0.782  78.289  56.812  1.00 56.51  ?  320 GLN A C     1 
ATOM   2340 O  O     . GLN A 1 319 ? -1.613  77.436  56.506  1.00 56.68  ?  320 GLN A O     1 
ATOM   2341 C  CB    . GLN A 1 319 ? 0.461   79.335  54.903  1.00 59.87  ?  320 GLN A CB    1 
ATOM   2342 C  CG    . GLN A 1 319 ? 0.571   80.475  53.904  1.00 63.93  ?  320 GLN A CG    1 
ATOM   2343 C  CD    . GLN A 1 319 ? 1.608   81.539  54.194  1.00 67.72  ?  320 GLN A CD    1 
ATOM   2344 O  OE1   . GLN A 1 319 ? 1.519   82.297  55.171  1.00 69.00  ?  320 GLN A OE1   1 
ATOM   2345 N  NE2   . GLN A 1 319 ? 2.600   81.640  53.321  1.00 68.01  ?  320 GLN A NE2   1 
ATOM   2346 N  N     . ALA A 1 320 ? 0.043   78.172  57.879  1.00 54.75  ?  321 ALA A N     1 
ATOM   2347 C  CA    . ALA A 1 320 ? 0.050   77.063  58.823  1.00 53.41  ?  321 ALA A CA    1 
ATOM   2348 C  C     . ALA A 1 320 ? -1.218  77.081  59.669  1.00 52.39  ?  321 ALA A C     1 
ATOM   2349 O  O     . ALA A 1 320 ? -1.810  76.029  59.904  1.00 52.04  ?  321 ALA A O     1 
ATOM   2350 C  CB    . ALA A 1 320 ? 1.282   77.149  59.715  1.00 53.10  ?  321 ALA A CB    1 
ATOM   2351 N  N     . LEU A 1 321 ? -1.640  78.276  60.114  1.00 51.76  ?  322 LEU A N     1 
ATOM   2352 C  CA    . LEU A 1 321 ? -2.843  78.460  60.920  1.00 51.70  ?  322 LEU A CA    1 
ATOM   2353 C  C     . LEU A 1 321 ? -4.105  78.201  60.081  1.00 51.70  ?  322 LEU A C     1 
ATOM   2354 O  O     . LEU A 1 321 ? -5.072  77.615  60.574  1.00 51.69  ?  322 LEU A O     1 
ATOM   2355 C  CB    . LEU A 1 321 ? -2.853  79.877  61.511  1.00 52.14  ?  322 LEU A CB    1 
ATOM   2356 C  CG    . LEU A 1 321 ? -4.109  80.284  62.266  1.00 54.11  ?  322 LEU A CG    1 
ATOM   2357 C  CD1   . LEU A 1 321 ? -4.298  79.434  63.512  1.00 54.75  ?  322 LEU A CD1   1 
ATOM   2358 C  CD2   . LEU A 1 321 ? -4.076  81.750  62.618  1.00 54.93  ?  322 LEU A CD2   1 
ATOM   2359 N  N     . GLN A 1 322 ? -4.078  78.601  58.808  1.00 51.71  ?  323 GLN A N     1 
ATOM   2360 C  CA    . GLN A 1 322 ? -5.184  78.375  57.892  1.00 52.31  ?  323 GLN A CA    1 
ATOM   2361 C  C     . GLN A 1 322 ? -5.361  76.866  57.670  1.00 51.40  ?  323 GLN A C     1 
ATOM   2362 O  O     . GLN A 1 322 ? -6.487  76.360  57.724  1.00 51.46  ?  323 GLN A O     1 
ATOM   2363 C  CB    . GLN A 1 322 ? -4.932  79.122  56.564  1.00 55.45  ?  323 GLN A CB    1 
ATOM   2364 C  CG    . GLN A 1 322 ? -5.813  78.695  55.384  1.00 61.45  ?  323 GLN A CG    1 
ATOM   2365 C  CD    . GLN A 1 322 ? -7.193  79.316  55.388  1.00 68.84  ?  323 GLN A CD    1 
ATOM   2366 O  OE1   . GLN A 1 322 ? -7.851  79.470  56.435  1.00 71.16  ?  323 GLN A OE1   1 
ATOM   2367 N  NE2   . GLN A 1 322 ? -7.673  79.670  54.200  1.00 69.90  ?  323 GLN A NE2   1 
ATOM   2368 N  N     . GLU A 1 323 ? -4.239  76.148  57.469  1.00 50.16  ?  324 GLU A N     1 
ATOM   2369 C  CA    . GLU A 1 323 ? -4.231  74.700  57.257  1.00 49.38  ?  324 GLU A CA    1 
ATOM   2370 C  C     . GLU A 1 323 ? -4.654  73.922  58.526  1.00 47.37  ?  324 GLU A C     1 
ATOM   2371 O  O     . GLU A 1 323 ? -5.234  72.849  58.419  1.00 46.80  ?  324 GLU A O     1 
ATOM   2372 C  CB    . GLU A 1 323 ? -2.864  74.252  56.708  1.00 52.48  ?  324 GLU A CB    1 
ATOM   2373 C  CG    . GLU A 1 323 ? -2.719  72.751  56.531  1.00 60.22  ?  324 GLU A CG    1 
ATOM   2374 C  CD    . GLU A 1 323 ? -3.074  72.155  55.185  1.00 69.84  ?  324 GLU A CD    1 
ATOM   2375 O  OE1   . GLU A 1 323 ? -2.591  72.682  54.156  1.00 73.30  ?  324 GLU A OE1   1 
ATOM   2376 O  OE2   . GLU A 1 323 ? -3.801  71.133  55.160  1.00 71.74  -1 324 GLU A OE2   1 
ATOM   2377 N  N     . LEU A 1 324 ? -4.424  74.506  59.716  1.00 46.16  ?  325 LEU A N     1 
ATOM   2378 C  CA    . LEU A 1 324 ? -4.791  73.943  61.012  1.00 45.41  ?  325 LEU A CA    1 
ATOM   2379 C  C     . LEU A 1 324 ? -6.299  74.037  61.221  1.00 45.56  ?  325 LEU A C     1 
ATOM   2380 O  O     . LEU A 1 324 ? -6.902  73.088  61.718  1.00 44.97  ?  325 LEU A O     1 
ATOM   2381 C  CB    . LEU A 1 324 ? -4.053  74.695  62.133  1.00 44.94  ?  325 LEU A CB    1 
ATOM   2382 C  CG    . LEU A 1 324 ? -4.434  74.335  63.561  1.00 45.82  ?  325 LEU A CG    1 
ATOM   2383 C  CD1   . LEU A 1 324 ? -4.006  72.938  63.897  1.00 46.37  ?  325 LEU A CD1   1 
ATOM   2384 C  CD2   . LEU A 1 324 ? -3.842  75.301  64.536  1.00 45.98  ?  325 LEU A CD2   1 
ATOM   2385 N  N     . ASN A 1 325 ? -6.912  75.174  60.827  1.00 46.31  ?  326 ASN A N     1 
ATOM   2386 C  CA    . ASN A 1 325 ? -8.363  75.373  60.957  1.00 47.40  ?  326 ASN A CA    1 
ATOM   2387 C  C     . ASN A 1 325 ? -9.181  74.519  59.985  1.00 47.45  ?  326 ASN A C     1 
ATOM   2388 O  O     . ASN A 1 325 ? -10.318 74.167  60.292  1.00 47.43  ?  326 ASN A O     1 
ATOM   2389 C  CB    . ASN A 1 325 ? -8.744  76.851  60.865  1.00 49.70  ?  326 ASN A CB    1 
ATOM   2390 C  CG    . ASN A 1 325 ? -8.744  77.515  62.221  1.00 54.04  ?  326 ASN A CG    1 
ATOM   2391 O  OD1   . ASN A 1 325 ? -7.887  78.354  62.538  1.00 55.28  ?  326 ASN A OD1   1 
ATOM   2392 N  ND2   . ASN A 1 325 ? -9.693  77.116  63.069  1.00 55.16  ?  326 ASN A ND2   1 
ATOM   2393 N  N     . LYS A 1 326 ? -8.594  74.162  58.837  1.00 47.67  ?  327 LYS A N     1 
ATOM   2394 C  CA    . LYS A 1 326 ? -9.211  73.274  57.851  1.00 48.64  ?  327 LYS A CA    1 
ATOM   2395 C  C     . LYS A 1 326 ? -9.257  71.845  58.415  1.00 48.96  ?  327 LYS A C     1 
ATOM   2396 O  O     . LYS A 1 326 ? -10.245 71.133  58.216  1.00 49.22  ?  327 LYS A O     1 
ATOM   2397 C  CB    . LYS A 1 326 ? -8.407  73.288  56.537  1.00 51.02  ?  327 LYS A CB    1 
ATOM   2398 C  CG    . LYS A 1 326 ? -8.682  74.507  55.670  1.00 56.16  ?  327 LYS A CG    1 
ATOM   2399 C  CD    . LYS A 1 326 ? -7.823  74.544  54.401  1.00 61.19  ?  327 LYS A CD    1 
ATOM   2400 C  CE    . LYS A 1 326 ? -6.350  74.726  54.690  1.00 64.48  ?  327 LYS A CE    1 
ATOM   2401 N  NZ    . LYS A 1 326 ? -5.626  75.288  53.519  1.00 66.69  1  327 LYS A NZ    1 
ATOM   2402 N  N     . ASP A 1 327 ? -8.178  71.427  59.114  1.00 48.59  ?  328 ASP A N     1 
ATOM   2403 C  CA    . ASP A 1 327 ? -8.091  70.108  59.742  1.00 48.88  ?  328 ASP A CA    1 
ATOM   2404 C  C     . ASP A 1 327 ? -8.967  70.028  61.003  1.00 48.10  ?  328 ASP A C     1 
ATOM   2405 O  O     . ASP A 1 327 ? -9.515  68.967  61.301  1.00 47.89  ?  328 ASP A O     1 
ATOM   2406 C  CB    . ASP A 1 327 ? -6.632  69.733  60.041  1.00 51.19  ?  328 ASP A CB    1 
ATOM   2407 C  CG    . ASP A 1 327 ? -5.758  69.684  58.797  1.00 57.53  ?  328 ASP A CG    1 
ATOM   2408 O  OD1   . ASP A 1 327 ? -6.308  69.451  57.685  1.00 58.72  ?  328 ASP A OD1   1 
ATOM   2409 O  OD2   . ASP A 1 327 ? -4.526  69.884  58.929  1.00 59.81  -1 328 ASP A OD2   1 
ATOM   2410 N  N     . ASP A 1 328 ? -9.135  71.157  61.717  1.00 47.62  ?  329 ASP A N     1 
ATOM   2411 C  CA    . ASP A 1 328 ? -10.004 71.226  62.893  1.00 47.59  ?  329 ASP A CA    1 
ATOM   2412 C  C     . ASP A 1 328 ? -11.484 71.067  62.483  1.00 47.65  ?  329 ASP A C     1 
ATOM   2413 O  O     . ASP A 1 328 ? -12.259 70.454  63.211  1.00 47.42  ?  329 ASP A O     1 
ATOM   2414 C  CB    . ASP A 1 328 ? -9.794  72.555  63.639  1.00 49.01  ?  329 ASP A CB    1 
ATOM   2415 C  CG    . ASP A 1 328 ? -10.673 72.714  64.872  1.00 52.93  ?  329 ASP A CG    1 
ATOM   2416 O  OD1   . ASP A 1 328 ? -10.749 71.753  65.680  1.00 53.07  ?  329 ASP A OD1   1 
ATOM   2417 O  OD2   . ASP A 1 328 ? -11.288 73.794  65.027  1.00 55.00  -1 329 ASP A OD2   1 
ATOM   2418 N  N     . ALA A 1 329 ? -11.868 71.600  61.309  1.00 47.75  ?  330 ALA A N     1 
ATOM   2419 C  CA    . ALA A 1 329 ? -13.242 71.499  60.809  1.00 48.24  ?  330 ALA A CA    1 
ATOM   2420 C  C     . ALA A 1 329 ? -13.571 70.133  60.180  1.00 48.47  ?  330 ALA A C     1 
ATOM   2421 O  O     . ALA A 1 329 ? -14.755 69.799  60.050  1.00 49.24  ?  330 ALA A O     1 
ATOM   2422 C  CB    . ALA A 1 329 ? -13.519 72.608  59.807  1.00 48.57  ?  330 ALA A CB    1 
ATOM   2423 N  N     . ASP A 1 330 ? -12.540 69.353  59.785  1.00 47.43  ?  331 ASP A N     1 
ATOM   2424 C  CA    . ASP A 1 330 ? -12.689 68.033  59.156  1.00 47.10  ?  331 ASP A CA    1 
ATOM   2425 C  C     . ASP A 1 330 ? -13.075 66.942  60.175  1.00 46.77  ?  331 ASP A C     1 
ATOM   2426 O  O     . ASP A 1 330 ? -12.322 66.690  61.109  1.00 46.77  ?  331 ASP A O     1 
ATOM   2427 C  CB    . ASP A 1 330 ? -11.368 67.661  58.463  1.00 48.27  ?  331 ASP A CB    1 
ATOM   2428 C  CG    . ASP A 1 330 ? -11.435 66.564  57.415  1.00 51.69  ?  331 ASP A CG    1 
ATOM   2429 O  OD1   . ASP A 1 330 ? -12.157 65.569  57.637  1.00 51.93  ?  331 ASP A OD1   1 
ATOM   2430 O  OD2   . ASP A 1 330 ? -10.733 66.682  56.392  1.00 53.81  -1 331 ASP A OD2   1 
ATOM   2431 N  N     . PRO A 1 331 ? -14.192 66.218  59.970  1.00 46.42  ?  332 PRO A N     1 
ATOM   2432 C  CA    . PRO A 1 331 ? -14.575 65.166  60.938  1.00 45.83  ?  332 PRO A CA    1 
ATOM   2433 C  C     . PRO A 1 331 ? -13.709 63.902  60.901  1.00 44.87  ?  332 PRO A C     1 
ATOM   2434 O  O     . PRO A 1 331 ? -13.734 63.119  61.852  1.00 44.77  ?  332 PRO A O     1 
ATOM   2435 C  CB    . PRO A 1 331 ? -16.032 64.866  60.576  1.00 46.88  ?  332 PRO A CB    1 
ATOM   2436 C  CG    . PRO A 1 331 ? -16.123 65.200  59.125  1.00 47.71  ?  332 PRO A CG    1 
ATOM   2437 C  CD    . PRO A 1 331 ? -15.200 66.369  58.900  1.00 46.15  ?  332 PRO A CD    1 
ATOM   2438 N  N     . GLU A 1 332 ? -12.947 63.700  59.807  1.00 43.84  ?  333 GLU A N     1 
ATOM   2439 C  CA    . GLU A 1 332 ? -12.041 62.552  59.649  1.00 42.81  ?  333 GLU A CA    1 
ATOM   2440 C  C     . GLU A 1 332 ? -10.688 62.723  60.384  1.00 39.81  ?  333 GLU A C     1 
ATOM   2441 O  O     . GLU A 1 332 ? -9.933  61.762  60.498  1.00 39.35  ?  333 GLU A O     1 
ATOM   2442 C  CB    . GLU A 1 332 ? -11.792 62.273  58.162  1.00 47.01  ?  333 GLU A CB    1 
ATOM   2443 C  CG    . GLU A 1 332 ? -13.017 61.761  57.435  1.00 54.92  ?  333 GLU A CG    1 
ATOM   2444 C  CD    . GLU A 1 332 ? -13.280 60.285  57.660  1.00 64.00  ?  333 GLU A CD    1 
ATOM   2445 O  OE1   . GLU A 1 332 ? -12.792 59.465  56.847  1.00 66.37  ?  333 GLU A OE1   1 
ATOM   2446 O  OE2   . GLU A 1 332 ? -13.971 59.947  58.648  1.00 66.62  -1 333 GLU A OE2   1 
ATOM   2447 N  N     . VAL A 1 333 ? -10.393 63.942  60.867  1.00 37.49  ?  334 VAL A N     1 
ATOM   2448 C  CA    . VAL A 1 333 ? -9.188  64.283  61.609  1.00 35.44  ?  334 VAL A CA    1 
ATOM   2449 C  C     . VAL A 1 333 ? -9.412  64.125  63.133  1.00 33.50  ?  334 VAL A C     1 
ATOM   2450 O  O     . VAL A 1 333 ? -10.352 64.694  63.683  1.00 33.60  ?  334 VAL A O     1 
ATOM   2451 C  CB    . VAL A 1 333 ? -8.749  65.713  61.229  1.00 35.60  ?  334 VAL A CB    1 
ATOM   2452 C  CG1   . VAL A 1 333 ? -7.638  66.205  62.139  1.00 35.54  ?  334 VAL A CG1   1 
ATOM   2453 C  CG2   . VAL A 1 333 ? -8.331  65.783  59.759  1.00 36.02  ?  334 VAL A CG2   1 
ATOM   2454 N  N     . LEU A 1 334 ? -8.549  63.340  63.802  1.00 31.41  ?  335 LEU A N     1 
ATOM   2455 C  CA    . LEU A 1 334 ? -8.615  63.052  65.239  1.00 29.75  ?  335 LEU A CA    1 
ATOM   2456 C  C     . LEU A 1 334 ? -7.599  63.869  66.051  1.00 28.07  ?  335 LEU A C     1 
ATOM   2457 O  O     . LEU A 1 334 ? -7.817  64.123  67.236  1.00 28.32  ?  335 LEU A O     1 
ATOM   2458 C  CB    . LEU A 1 334 ? -8.359  61.556  65.499  1.00 29.64  ?  335 LEU A CB    1 
ATOM   2459 C  CG    . LEU A 1 334 ? -9.287  60.589  64.810  1.00 31.67  ?  335 LEU A CG    1 
ATOM   2460 C  CD1   . LEU A 1 334 ? -8.732  60.201  63.485  1.00 32.78  ?  335 LEU A CD1   1 
ATOM   2461 C  CD2   . LEU A 1 334 ? -9.445  59.328  65.625  1.00 32.32  ?  335 LEU A CD2   1 
ATOM   2462 N  N     . ILE A 1 335 ? -6.460  64.206  65.427  1.00 26.11  ?  336 ILE A N     1 
ATOM   2463 C  CA    . ILE A 1 335 ? -5.367  64.980  66.002  1.00 24.30  ?  336 ILE A CA    1 
ATOM   2464 C  C     . ILE A 1 335 ? -5.062  66.128  65.046  1.00 23.15  ?  336 ILE A C     1 
ATOM   2465 O  O     . ILE A 1 335 ? -4.908  65.898  63.865  1.00 23.22  ?  336 ILE A O     1 
ATOM   2466 C  CB    . ILE A 1 335 ? -4.109  64.069  66.192  1.00 23.67  ?  336 ILE A CB    1 
ATOM   2467 C  CG1   . ILE A 1 335 ? -4.338  63.053  67.324  1.00 24.21  ?  336 ILE A CG1   1 
ATOM   2468 C  CG2   . ILE A 1 335 ? -2.865  64.903  66.457  1.00 23.51  ?  336 ILE A CG2   1 
ATOM   2469 C  CD1   . ILE A 1 335 ? -3.339  61.978  67.409  1.00 25.41  ?  336 ILE A CD1   1 
ATOM   2470 N  N     . ALA A 1 336 ? -4.949  67.339  65.552  1.00 22.60  ?  337 ALA A N     1 
ATOM   2471 C  CA    . ALA A 1 336 ? -4.599  68.525  64.778  1.00 22.82  ?  337 ALA A CA    1 
ATOM   2472 C  C     . ALA A 1 336 ? -3.923  69.462  65.759  1.00 23.04  ?  337 ALA A C     1 
ATOM   2473 O  O     . ALA A 1 336 ? -4.568  69.922  66.693  1.00 23.41  ?  337 ALA A O     1 
ATOM   2474 C  CB    . ALA A 1 336 ? -5.848  69.172  64.201  1.00 23.04  ?  337 ALA A CB    1 
ATOM   2475 N  N     . VAL A 1 337 ? -2.606  69.648  65.631  1.00 22.98  ?  338 VAL A N     1 
ATOM   2476 C  CA    . VAL A 1 337 ? -1.845  70.497  66.544  1.00 23.49  ?  338 VAL A CA    1 
ATOM   2477 C  C     . VAL A 1 337 ? -0.739  71.231  65.771  1.00 24.72  ?  338 VAL A C     1 
ATOM   2478 O  O     . VAL A 1 337 ? -0.164  70.670  64.832  1.00 24.74  ?  338 VAL A O     1 
ATOM   2479 C  CB    . VAL A 1 337 ? -1.305  69.707  67.794  1.00 23.57  ?  338 VAL A CB    1 
ATOM   2480 C  CG1   . VAL A 1 337 ? -0.447  68.510  67.396  1.00 23.20  ?  338 VAL A CG1   1 
ATOM   2481 C  CG2   . VAL A 1 337 ? -0.543  70.613  68.761  1.00 24.07  ?  338 VAL A CG2   1 
ATOM   2482 N  N     . LEU A 1 338 ? -0.452  72.488  66.165  1.00 25.30  ?  339 LEU A N     1 
ATOM   2483 C  CA    . LEU A 1 338 ? 0.584   73.329  65.572  1.00 26.50  ?  339 LEU A CA    1 
ATOM   2484 C  C     . LEU A 1 338 ? 1.661   73.591  66.637  1.00 26.82  ?  339 LEU A C     1 
ATOM   2485 O  O     . LEU A 1 338 ? 1.332   74.138  67.678  1.00 26.71  ?  339 LEU A O     1 
ATOM   2486 C  CB    . LEU A 1 338 ? -0.056  74.661  65.180  1.00 27.69  ?  339 LEU A CB    1 
ATOM   2487 C  CG    . LEU A 1 338 ? 0.543   75.383  63.989  1.00 30.31  ?  339 LEU A CG    1 
ATOM   2488 C  CD1   . LEU A 1 338 ? 0.312   74.581  62.718  1.00 31.44  ?  339 LEU A CD1   1 
ATOM   2489 C  CD2   . LEU A 1 338 ? -0.112  76.742  63.825  1.00 31.14  ?  339 LEU A CD2   1 
ATOM   2490 N  N     . LEU A 1 339 ? 2.930   73.220  66.394  1.00 27.25  ?  340 LEU A N     1 
ATOM   2491 C  CA    . LEU A 1 339 ? 3.991   73.417  67.384  1.00 27.95  ?  340 LEU A CA    1 
ATOM   2492 C  C     . LEU A 1 339 ? 5.210   74.116  66.819  1.00 28.57  ?  340 LEU A C     1 
ATOM   2493 O  O     . LEU A 1 339 ? 5.735   73.691  65.801  1.00 29.26  ?  340 LEU A O     1 
ATOM   2494 C  CB    . LEU A 1 339 ? 4.423   72.068  67.987  1.00 28.32  ?  340 LEU A CB    1 
ATOM   2495 C  CG    . LEU A 1 339 ? 3.426   71.414  68.955  1.00 29.96  ?  340 LEU A CG    1 
ATOM   2496 C  CD1   . LEU A 1 339 ? 3.917   70.053  69.401  1.00 30.40  ?  340 LEU A CD1   1 
ATOM   2497 C  CD2   . LEU A 1 339 ? 3.163   72.308  70.161  1.00 30.27  ?  340 LEU A CD2   1 
ATOM   2498 N  N     . ALA A 1 340 ? 5.704   75.139  67.508  1.00 28.31  ?  341 ALA A N     1 
ATOM   2499 C  CA    . ALA A 1 340 ? 6.903   75.853  67.087  1.00 28.94  ?  341 ALA A CA    1 
ATOM   2500 C  C     . ALA A 1 340 ? 8.119   74.975  67.350  1.00 29.77  ?  341 ALA A C     1 
ATOM   2501 O  O     . ALA A 1 340 ? 8.259   74.437  68.447  1.00 29.88  ?  341 ALA A O     1 
ATOM   2502 C  CB    . ALA A 1 340 ? 7.019   77.153  67.854  1.00 29.03  ?  341 ALA A CB    1 
ATOM   2503 N  N     . THR A 1 341 ? 8.984   74.803  66.345  1.00 30.30  ?  342 THR A N     1 
ATOM   2504 C  CA    . THR A 1 341 ? 10.145  73.926  66.461  1.00 31.09  ?  342 THR A CA    1 
ATOM   2505 C  C     . THR A 1 341 ? 11.129  74.320  67.554  1.00 31.56  ?  342 THR A C     1 
ATOM   2506 O  O     . THR A 1 341 ? 11.739  73.427  68.143  1.00 31.94  ?  342 THR A O     1 
ATOM   2507 C  CB    . THR A 1 341 ? 10.857  73.769  65.118  1.00 33.21  ?  342 THR A CB    1 
ATOM   2508 O  OG1   . THR A 1 341 ? 11.936  72.843  65.280  1.00 35.25  ?  342 THR A OG1   1 
ATOM   2509 C  CG2   . THR A 1 341 ? 11.409  75.061  64.596  1.00 33.41  ?  342 THR A CG2   1 
ATOM   2510 N  N     . ASN A 1 342 ? 11.304  75.627  67.830  1.00 31.26  ?  343 ASN A N     1 
ATOM   2511 C  CA    . ASN A 1 342 ? 12.250  76.057  68.852  1.00 31.40  ?  343 ASN A CA    1 
ATOM   2512 C  C     . ASN A 1 342 ? 11.829  75.607  70.252  1.00 30.52  ?  343 ASN A C     1 
ATOM   2513 O  O     . ASN A 1 342 ? 12.669  75.187  71.053  1.00 30.36  ?  343 ASN A O     1 
ATOM   2514 C  CB    . ASN A 1 342 ? 12.486  77.563  68.771  1.00 33.66  ?  343 ASN A CB    1 
ATOM   2515 C  CG    . ASN A 1 342 ? 13.338  77.954  67.578  1.00 38.82  ?  343 ASN A CG    1 
ATOM   2516 O  OD1   . ASN A 1 342 ? 14.044  77.122  66.980  1.00 40.50  ?  343 ASN A OD1   1 
ATOM   2517 N  ND2   . ASN A 1 342 ? 13.289  79.229  67.198  1.00 39.89  ?  343 ASN A ND2   1 
ATOM   2518 N  N     . ASN A 1 343 ? 10.520  75.643  70.523  1.00 29.73  ?  344 ASN A N     1 
ATOM   2519 C  CA    . ASN A 1 343 ? 9.979   75.214  71.801  1.00 29.35  ?  344 ASN A CA    1 
ATOM   2520 C  C     . ASN A 1 343 ? 10.114  73.717  71.987  1.00 28.08  ?  344 ASN A C     1 
ATOM   2521 O  O     . ASN A 1 343 ? 10.497  73.287  73.065  1.00 27.50  ?  344 ASN A O     1 
ATOM   2522 C  CB    . ASN A 1 343 ? 8.553   75.702  71.965  1.00 31.41  ?  344 ASN A CB    1 
ATOM   2523 C  CG    . ASN A 1 343 ? 8.545   77.201  72.047  1.00 36.64  ?  344 ASN A CG    1 
ATOM   2524 O  OD1   . ASN A 1 343 ? 8.886   77.787  73.081  1.00 38.85  ?  344 ASN A OD1   1 
ATOM   2525 N  ND2   . ASN A 1 343 ? 8.235   77.862  70.944  1.00 37.89  ?  344 ASN A ND2   1 
ATOM   2526 N  N     . ILE A 1 344 ? 9.913   72.934  70.911  1.00 27.78  ?  345 ILE A N     1 
ATOM   2527 C  CA    . ILE A 1 344 ? 10.070  71.480  70.929  1.00 27.96  ?  345 ILE A CA    1 
ATOM   2528 C  C     . ILE A 1 344 ? 11.513  71.141  71.285  1.00 27.76  ?  345 ILE A C     1 
ATOM   2529 O  O     . ILE A 1 344 ? 11.756  70.327  72.178  1.00 28.12  ?  345 ILE A O     1 
ATOM   2530 C  CB    . ILE A 1 344 ? 9.688   70.857  69.556  1.00 28.85  ?  345 ILE A CB    1 
ATOM   2531 C  CG1   . ILE A 1 344 ? 8.272   71.198  69.140  1.00 29.67  ?  345 ILE A CG1   1 
ATOM   2532 C  CG2   . ILE A 1 344 ? 9.904   69.351  69.545  1.00 29.50  ?  345 ILE A CG2   1 
ATOM   2533 C  CD1   . ILE A 1 344 ? 8.012   70.878  67.607  1.00 31.01  ?  345 ILE A CD1   1 
ATOM   2534 N  N     . LYS A 1 345 ? 12.463  71.831  70.627  1.00 27.01  ?  346 LYS A N     1 
ATOM   2535 C  CA    . LYS A 1 345 ? 13.899  71.692  70.814  1.00 26.83  ?  346 LYS A CA    1 
ATOM   2536 C  C     . LYS A 1 345 ? 14.358  71.929  72.255  1.00 25.45  ?  346 LYS A C     1 
ATOM   2537 O  O     . LYS A 1 345 ? 15.077  71.089  72.806  1.00 25.84  ?  346 LYS A O     1 
ATOM   2538 C  CB    . LYS A 1 345 ? 14.633  72.652  69.867  1.00 30.16  ?  346 LYS A CB    1 
ATOM   2539 C  CG    . LYS A 1 345 ? 15.657  71.978  68.983  1.00 35.61  ?  346 LYS A CG    1 
ATOM   2540 C  CD    . LYS A 1 345 ? 16.098  72.926  67.893  1.00 40.87  ?  346 LYS A CD    1 
ATOM   2541 C  CE    . LYS A 1 345 ? 15.033  73.093  66.840  1.00 44.50  ?  346 LYS A CE    1 
ATOM   2542 N  NZ    . LYS A 1 345 ? 14.711  71.800  66.187  1.00 46.84  1  346 LYS A NZ    1 
ATOM   2543 N  N     . SER A 1 346 ? 13.966  73.059  72.863  1.00 24.04  ?  347 SER A N     1 
ATOM   2544 C  CA    . SER A 1 346 ? 14.362  73.341  74.241  1.00 23.66  ?  347 SER A CA    1 
ATOM   2545 C  C     . SER A 1 346 ? 13.732  72.402  75.258  1.00 22.63  ?  347 SER A C     1 
ATOM   2546 O  O     . SER A 1 346 ? 14.404  72.075  76.225  1.00 23.63  ?  347 SER A O     1 
ATOM   2547 C  CB    . SER A 1 346 ? 14.113  74.799  74.612  1.00 26.05  ?  347 SER A CB    1 
ATOM   2548 O  OG    . SER A 1 346 ? 12.822  75.225  74.222  1.00 29.96  ?  347 SER A OG    1 
ATOM   2549 N  N     . LEU A 1 347 ? 12.483  71.929  75.046  1.00 20.66  ?  348 LEU A N     1 
ATOM   2550 C  CA    . LEU A 1 347 ? 11.867  70.992  75.980  1.00 19.70  ?  348 LEU A CA    1 
ATOM   2551 C  C     . LEU A 1 347 ? 12.568  69.640  75.916  1.00 19.80  ?  348 LEU A C     1 
ATOM   2552 O  O     . LEU A 1 347 ? 12.812  69.036  76.948  1.00 19.25  ?  348 LEU A O     1 
ATOM   2553 C  CB    . LEU A 1 347 ? 10.356  70.833  75.747  1.00 19.46  ?  348 LEU A CB    1 
ATOM   2554 C  CG    . LEU A 1 347 ? 9.504   72.039  76.072  1.00 20.60  ?  348 LEU A CG    1 
ATOM   2555 C  CD1   . LEU A 1 347 ? 8.195   72.005  75.292  1.00 21.36  ?  348 LEU A CD1   1 
ATOM   2556 C  CD2   . LEU A 1 347 ? 9.248   72.151  77.566  1.00 21.11  ?  348 LEU A CD2   1 
ATOM   2557 N  N     . LYS A 1 348 ? 12.951  69.194  74.719  1.00 20.47  ?  349 LYS A N     1 
ATOM   2558 C  CA    . LYS A 1 348 ? 13.666  67.931  74.556  1.00 21.65  ?  349 LYS A CA    1 
ATOM   2559 C  C     . LYS A 1 348 ? 15.046  67.960  75.226  1.00 22.69  ?  349 LYS A C     1 
ATOM   2560 O  O     . LYS A 1 348 ? 15.511  66.932  75.711  1.00 22.60  ?  349 LYS A O     1 
ATOM   2561 C  CB    . LYS A 1 348 ? 13.815  67.603  73.064  1.00 23.95  ?  349 LYS A CB    1 
ATOM   2562 C  CG    . LYS A 1 348 ? 12.545  67.054  72.456  1.00 28.27  ?  349 LYS A CG    1 
ATOM   2563 C  CD    . LYS A 1 348 ? 12.734  66.719  71.000  1.00 33.59  ?  349 LYS A CD    1 
ATOM   2564 C  CE    . LYS A 1 348 ? 11.451  66.161  70.433  1.00 37.28  ?  349 LYS A CE    1 
ATOM   2565 N  NZ    . LYS A 1 348 ? 11.419  66.230  68.953  1.00 38.78  1  349 LYS A NZ    1 
ATOM   2566 N  N     . LYS A 1 349 ? 15.695  69.138  75.237  1.00 23.27  ?  350 LYS A N     1 
ATOM   2567 C  CA    . LYS A 1 349 ? 17.022  69.365  75.805  1.00 24.11  ?  350 LYS A CA    1 
ATOM   2568 C  C     . LYS A 1 349 ? 16.948  69.446  77.328  1.00 23.00  ?  350 LYS A C     1 
ATOM   2569 O  O     . LYS A 1 349 ? 17.754  68.820  78.021  1.00 23.24  ?  350 LYS A O     1 
ATOM   2570 C  CB    . LYS A 1 349 ? 17.620  70.664  75.219  1.00 27.96  ?  350 LYS A CB    1 
ATOM   2571 C  CG    . LYS A 1 349 ? 19.115  70.817  75.446  1.00 34.45  ?  350 LYS A CG    1 
ATOM   2572 C  CD    . LYS A 1 349 ? 19.708  71.833  74.473  1.00 41.39  ?  350 LYS A CD    1 
ATOM   2573 C  CE    . LYS A 1 349 ? 19.711  71.300  73.053  1.00 47.19  ?  350 LYS A CE    1 
ATOM   2574 N  NZ    . LYS A 1 349 ? 20.598  70.105  72.901  1.00 50.13  1  350 LYS A NZ    1 
ATOM   2575 N  N     . ALA A 1 350 ? 15.970  70.199  77.846  1.00 21.76  ?  351 ALA A N     1 
ATOM   2576 C  CA    . ALA A 1 350 ? 15.722  70.333  79.282  1.00 20.76  ?  351 ALA A CA    1 
ATOM   2577 C  C     . ALA A 1 350 ? 15.250  69.004  79.892  1.00 20.27  ?  351 ALA A C     1 
ATOM   2578 O  O     . ALA A 1 350 ? 15.630  68.663  81.022  1.00 20.07  ?  351 ALA A O     1 
ATOM   2579 C  CB    . ALA A 1 350 ? 14.680  71.403  79.510  1.00 20.35  ?  351 ALA A CB    1 
ATOM   2580 N  N     . TYR A 1 351 ? 14.444  68.240  79.132  1.00 19.84  ?  352 TYR A N     1 
ATOM   2581 C  CA    . TYR A 1 351 ? 13.903  66.969  79.598  1.00 20.72  ?  352 TYR A CA    1 
ATOM   2582 C  C     . TYR A 1 351 ? 14.204  65.785  78.672  1.00 21.80  ?  352 TYR A C     1 
ATOM   2583 O  O     . TYR A 1 351 ? 13.363  65.399  77.862  1.00 21.33  ?  352 TYR A O     1 
ATOM   2584 C  CB    . TYR A 1 351 ? 12.393  67.089  79.802  1.00 20.50  ?  352 TYR A CB    1 
ATOM   2585 C  CG    . TYR A 1 351 ? 12.034  68.193  80.766  1.00 21.13  ?  352 TYR A CG    1 
ATOM   2586 C  CD1   . TYR A 1 351 ? 12.266  68.055  82.127  1.00 21.49  ?  352 TYR A CD1   1 
ATOM   2587 C  CD2   . TYR A 1 351 ? 11.513  69.394  80.312  1.00 22.00  ?  352 TYR A CD2   1 
ATOM   2588 C  CE1   . TYR A 1 351 ? 11.931  69.056  83.015  1.00 22.28  ?  352 TYR A CE1   1 
ATOM   2589 C  CE2   . TYR A 1 351 ? 11.203  70.417  81.190  1.00 22.95  ?  352 TYR A CE2   1 
ATOM   2590 C  CZ    . TYR A 1 351 ? 11.422  70.247  82.540  1.00 23.80  ?  352 TYR A CZ    1 
ATOM   2591 O  OH    . TYR A 1 351 ? 11.095  71.249  83.411  1.00 26.01  ?  352 TYR A OH    1 
ATOM   2592 N  N     . PRO A 1 352 ? 15.380  65.164  78.816  1.00 22.54  ?  353 PRO A N     1 
ATOM   2593 C  CA    . PRO A 1 352 ? 15.708  64.015  77.955  1.00 23.44  ?  353 PRO A CA    1 
ATOM   2594 C  C     . PRO A 1 352 ? 14.676  62.883  78.013  1.00 24.62  ?  353 PRO A C     1 
ATOM   2595 O  O     . PRO A 1 352 ? 14.385  62.253  77.001  1.00 25.42  ?  353 PRO A O     1 
ATOM   2596 C  CB    . PRO A 1 352 ? 17.063  63.539  78.489  1.00 24.08  ?  353 PRO A CB    1 
ATOM   2597 C  CG    . PRO A 1 352 ? 17.613  64.663  79.284  1.00 24.04  ?  353 PRO A CG    1 
ATOM   2598 C  CD    . PRO A 1 352 ? 16.485  65.522  79.731  1.00 22.12  ?  353 PRO A CD    1 
ATOM   2599 N  N     . ASN A 1 353 ? 14.124  62.620  79.196  1.00 24.52  ?  354 ASN A N     1 
ATOM   2600 C  CA    . ASN A 1 353 ? 13.145  61.560  79.383  1.00 24.50  ?  354 ASN A CA    1 
ATOM   2601 C  C     . ASN A 1 353 ? 11.731  62.151  79.523  1.00 23.71  ?  354 ASN A C     1 
ATOM   2602 O  O     . ASN A 1 353 ? 10.954  61.674  80.343  1.00 24.16  ?  354 ASN A O     1 
ATOM   2603 C  CB    . ASN A 1 353 ? 13.520  60.740  80.624  1.00 26.45  ?  354 ASN A CB    1 
ATOM   2604 C  CG    . ASN A 1 353 ? 12.674  59.506  80.841  1.00 31.35  ?  354 ASN A CG    1 
ATOM   2605 O  OD1   . ASN A 1 353 ? 12.084  58.957  79.905  1.00 34.02  ?  354 ASN A OD1   1 
ATOM   2606 N  ND2   . ASN A 1 353 ? 12.568  59.065  82.089  1.00 31.60  ?  354 ASN A ND2   1 
ATOM   2607 N  N     . TYR A 1 354 ? 11.393  63.188  78.733  1.00 22.39  ?  355 TYR A N     1 
ATOM   2608 C  CA    . TYR A 1 354 ? 10.076  63.818  78.794  1.00 22.00  ?  355 TYR A CA    1 
ATOM   2609 C  C     . TYR A 1 354 ? 8.911   62.816  78.561  1.00 22.33  ?  355 TYR A C     1 
ATOM   2610 O  O     . TYR A 1 354 ? 7.853   62.958  79.173  1.00 22.44  ?  355 TYR A O     1 
ATOM   2611 C  CB    . TYR A 1 354 ? 9.978   65.015  77.801  1.00 21.74  ?  355 TYR A CB    1 
ATOM   2612 C  CG    . TYR A 1 354 ? 9.961   64.600  76.341  1.00 21.94  ?  355 TYR A CG    1 
ATOM   2613 C  CD1   . TYR A 1 354 ? 11.143  64.459  75.620  1.00 22.62  ?  355 TYR A CD1   1 
ATOM   2614 C  CD2   . TYR A 1 354 ? 8.767   64.337  75.685  1.00 22.44  ?  355 TYR A CD2   1 
ATOM   2615 C  CE1   . TYR A 1 354 ? 11.137  64.049  74.294  1.00 23.31  ?  355 TYR A CE1   1 
ATOM   2616 C  CE2   . TYR A 1 354 ? 8.750   63.875  74.373  1.00 23.38  ?  355 TYR A CE2   1 
ATOM   2617 C  CZ    . TYR A 1 354 ? 9.936   63.760  73.672  1.00 24.22  ?  355 TYR A CZ    1 
ATOM   2618 O  OH    . TYR A 1 354 ? 9.920   63.336  72.367  1.00 25.66  ?  355 TYR A OH    1 
ATOM   2619 N  N     . PHE A 1 355 ? 9.100   61.819  77.680  1.00 22.15  ?  356 PHE A N     1 
ATOM   2620 C  CA    . PHE A 1 355 ? 8.017   60.891  77.338  1.00 22.53  ?  356 PHE A CA    1 
ATOM   2621 C  C     . PHE A 1 355 ? 7.750   59.881  78.415  1.00 22.18  ?  356 PHE A C     1 
ATOM   2622 O  O     . PHE A 1 355 ? 6.593   59.535  78.641  1.00 22.55  ?  356 PHE A O     1 
ATOM   2623 C  CB    . PHE A 1 355 ? 8.224   60.222  75.980  1.00 23.17  ?  356 PHE A CB    1 
ATOM   2624 C  CG    . PHE A 1 355 ? 9.591   59.630  75.771  1.00 24.41  ?  356 PHE A CG    1 
ATOM   2625 C  CD1   . PHE A 1 355 ? 10.659  60.428  75.391  1.00 25.62  ?  356 PHE A CD1   1 
ATOM   2626 C  CD2   . PHE A 1 355 ? 9.799   58.272  75.900  1.00 25.36  ?  356 PHE A CD2   1 
ATOM   2627 C  CE1   . PHE A 1 355 ? 11.914  59.882  75.181  1.00 26.57  ?  356 PHE A CE1   1 
ATOM   2628 C  CE2   . PHE A 1 355 ? 11.042  57.721  75.641  1.00 26.46  ?  356 PHE A CE2   1 
ATOM   2629 C  CZ    . PHE A 1 355 ? 12.098  58.529  75.299  1.00 26.51  ?  356 PHE A CZ    1 
ATOM   2630 N  N     . GLY A 1 356 ? 8.789   59.460  79.134  1.00 21.32  ?  357 GLY A N     1 
ATOM   2631 C  CA    . GLY A 1 356 ? 8.605   58.586  80.284  1.00 20.62  ?  357 GLY A CA    1 
ATOM   2632 C  C     . GLY A 1 356 ? 7.823   59.306  81.373  1.00 19.81  ?  357 GLY A C     1 
ATOM   2633 O  O     . GLY A 1 356 ? 6.910   58.738  81.963  1.00 20.28  ?  357 GLY A O     1 
ATOM   2634 N  N     . SER A 1 357 ? 8.120   60.600  81.577  1.00 18.87  ?  358 SER A N     1 
ATOM   2635 C  CA    . SER A 1 357 ? 7.441   61.448  82.551  1.00 18.53  ?  358 SER A CA    1 
ATOM   2636 C  C     . SER A 1 357 ? 5.990   61.749  82.207  1.00 18.56  ?  358 SER A C     1 
ATOM   2637 O  O     . SER A 1 357 ? 5.138   61.625  83.083  1.00 18.82  ?  358 SER A O     1 
ATOM   2638 C  CB    . SER A 1 357 ? 8.204   62.752  82.759  1.00 18.96  ?  358 SER A CB    1 
ATOM   2639 O  OG    . SER A 1 357 ? 9.420   62.545  83.464  1.00 19.49  ?  358 SER A OG    1 
ATOM   2640 N  N     . THR A 1 358 ? 5.691   62.168  80.960  1.00 18.21  ?  359 THR A N     1 
ATOM   2641 C  CA    . THR A 1 358 ? 4.304   62.481  80.606  1.00 17.83  ?  359 THR A CA    1 
ATOM   2642 C  C     . THR A 1 358 ? 3.437   61.228  80.639  1.00 17.59  ?  359 THR A C     1 
ATOM   2643 O  O     . THR A 1 358 ? 2.277   61.334  81.026  1.00 16.86  ?  359 THR A O     1 
ATOM   2644 C  CB    . THR A 1 358 ? 4.199   63.257  79.310  1.00 17.95  ?  359 THR A CB    1 
ATOM   2645 O  OG1   . THR A 1 358 ? 4.749   62.447  78.295  1.00 18.98  ?  359 THR A OG1   1 
ATOM   2646 C  CG2   . THR A 1 358 ? 4.906   64.582  79.372  1.00 17.67  ?  359 THR A CG2   1 
ATOM   2647 N  N     . ASN A 1 359 ? 3.998   60.051  80.284  1.00 18.15  ?  360 ASN A N     1 
ATOM   2648 C  CA    . ASN A 1 359 ? 3.285   58.772  80.371  1.00 19.62  ?  360 ASN A CA    1 
ATOM   2649 C  C     . ASN A 1 359 ? 2.944   58.470  81.835  1.00 18.69  ?  360 ASN A C     1 
ATOM   2650 O  O     . ASN A 1 359 ? 1.788   58.156  82.153  1.00 19.30  ?  360 ASN A O     1 
ATOM   2651 C  CB    . ASN A 1 359 ? 4.127   57.610  79.811  1.00 24.38  ?  360 ASN A CB    1 
ATOM   2652 C  CG    . ASN A 1 359 ? 4.260   57.574  78.308  1.00 34.08  ?  360 ASN A CG    1 
ATOM   2653 O  OD1   . ASN A 1 359 ? 3.576   58.304  77.566  1.00 36.91  ?  360 ASN A OD1   1 
ATOM   2654 N  ND2   . ASN A 1 359 ? 5.176   56.724  77.821  1.00 36.78  ?  360 ASN A ND2   1 
ATOM   2655 N  N     . GLN A 1 360 ? 3.943   58.581  82.729  1.00 17.20  ?  361 GLN A N     1 
ATOM   2656 C  CA    . GLN A 1 360 ? 3.761   58.338  84.153  1.00 16.93  ?  361 GLN A CA    1 
ATOM   2657 C  C     . GLN A 1 360 ? 2.739   59.308  84.778  1.00 15.51  ?  361 GLN A C     1 
ATOM   2658 O  O     . GLN A 1 360 ? 1.877   58.887  85.549  1.00 16.19  ?  361 GLN A O     1 
ATOM   2659 C  CB    . GLN A 1 360 ? 5.117   58.407  84.874  1.00 19.44  ?  361 GLN A CB    1 
ATOM   2660 C  CG    . GLN A 1 360 ? 5.025   58.018  86.339  1.00 25.22  ?  361 GLN A CG    1 
ATOM   2661 C  CD    . GLN A 1 360 ? 6.350   58.054  87.056  1.00 32.89  ?  361 GLN A CD    1 
ATOM   2662 O  OE1   . GLN A 1 360 ? 7.259   58.839  86.720  1.00 36.52  ?  361 GLN A OE1   1 
ATOM   2663 N  NE2   . GLN A 1 360 ? 6.483   57.212  88.078  1.00 32.97  ?  361 GLN A NE2   1 
ATOM   2664 N  N     . PHE A 1 361 ? 2.813   60.586  84.430  1.00 13.79  ?  362 PHE A N     1 
ATOM   2665 C  CA    . PHE A 1 361 ? 1.872   61.579  84.941  1.00 13.17  ?  362 PHE A CA    1 
ATOM   2666 C  C     . PHE A 1 361 ? 0.427   61.317  84.443  1.00 13.84  ?  362 PHE A C     1 
ATOM   2667 O  O     . PHE A 1 361 ? -0.519  61.404  85.227  1.00 14.77  ?  362 PHE A O     1 
ATOM   2668 C  CB    . PHE A 1 361 ? 2.352   63.011  84.639  1.00 12.02  ?  362 PHE A CB    1 
ATOM   2669 C  CG    . PHE A 1 361 ? 1.560   64.055  85.386  1.00 12.14  ?  362 PHE A CG    1 
ATOM   2670 C  CD1   . PHE A 1 361 ? 1.594   64.116  86.769  1.00 12.24  ?  362 PHE A CD1   1 
ATOM   2671 C  CD2   . PHE A 1 361 ? 0.733   64.938  84.711  1.00 13.07  ?  362 PHE A CD2   1 
ATOM   2672 C  CE1   . PHE A 1 361 ? 0.822   65.044  87.460  1.00 12.93  ?  362 PHE A CE1   1 
ATOM   2673 C  CE2   . PHE A 1 361 ? -0.002  65.905  85.405  1.00 13.50  ?  362 PHE A CE2   1 
ATOM   2674 C  CZ    . PHE A 1 361 ? 0.058   65.956  86.773  1.00 13.03  ?  362 PHE A CZ    1 
ATOM   2675 N  N     . GLY A 1 362 ? 0.268   60.941  83.176  1.00 13.36  ?  363 GLY A N     1 
ATOM   2676 C  CA    . GLY A 1 362 ? -1.042  60.596  82.626  1.00 13.30  ?  363 GLY A CA    1 
ATOM   2677 C  C     . GLY A 1 362 ? -1.657  59.370  83.295  1.00 13.76  ?  363 GLY A C     1 
ATOM   2678 O  O     . GLY A 1 362 ? -2.859  59.359  83.578  1.00 13.85  ?  363 GLY A O     1 
ATOM   2679 N  N     . ARG A 1 363 ? -0.825  58.342  83.605  1.00 13.89  ?  364 ARG A N     1 
ATOM   2680 C  CA    . ARG A 1 363 ? -1.260  57.124  84.307  1.00 14.67  ?  364 ARG A CA    1 
ATOM   2681 C  C     . ARG A 1 363 ? -1.664  57.468  85.737  1.00 14.97  ?  364 ARG A C     1 
ATOM   2682 O  O     . ARG A 1 363 ? -2.648  56.938  86.236  1.00 16.31  ?  364 ARG A O     1 
ATOM   2683 C  CB    . ARG A 1 363 ? -0.140  56.057  84.345  1.00 16.35  ?  364 ARG A CB    1 
ATOM   2684 C  CG    . ARG A 1 363 ? 0.182   55.408  83.008  1.00 21.17  ?  364 ARG A CG    1 
ATOM   2685 C  CD    . ARG A 1 363 ? 1.510   54.652  83.058  1.00 27.33  ?  364 ARG A CD    1 
ATOM   2686 N  NE    . ARG A 1 363 ? 1.992   54.294  81.718  1.00 33.46  ?  364 ARG A NE    1 
ATOM   2687 C  CZ    . ARG A 1 363 ? 2.724   53.214  81.443  1.00 36.81  ?  364 ARG A CZ    1 
ATOM   2688 N  NH1   . ARG A 1 363 ? 3.063   52.370  82.410  1.00 36.94  1  364 ARG A NH1   1 
ATOM   2689 N  NH2   . ARG A 1 363 ? 3.101   52.959  80.195  1.00 36.62  ?  364 ARG A NH2   1 
ATOM   2690 N  N     . PHE A 1 364 ? -0.910  58.351  86.395  1.00 13.84  ?  365 PHE A N     1 
ATOM   2691 C  CA    . PHE A 1 364 ? -1.202  58.824  87.740  1.00 13.27  ?  365 PHE A CA    1 
ATOM   2692 C  C     . PHE A 1 364 ? -2.560  59.546  87.760  1.00 14.37  ?  365 PHE A C     1 
ATOM   2693 O  O     . PHE A 1 364 ? -3.356  59.347  88.687  1.00 14.87  ?  365 PHE A O     1 
ATOM   2694 C  CB    . PHE A 1 364 ? -0.050  59.741  88.218  1.00 12.06  ?  365 PHE A CB    1 
ATOM   2695 C  CG    . PHE A 1 364 ? -0.381  60.635  89.384  1.00 11.84  ?  365 PHE A CG    1 
ATOM   2696 C  CD1   . PHE A 1 364 ? -0.279  60.172  90.683  1.00 11.88  ?  365 PHE A CD1   1 
ATOM   2697 C  CD2   . PHE A 1 364 ? -0.871  61.917  89.179  1.00 12.45  ?  365 PHE A CD2   1 
ATOM   2698 C  CE1   . PHE A 1 364 ? -0.647  60.975  91.750  1.00 12.31  ?  365 PHE A CE1   1 
ATOM   2699 C  CE2   . PHE A 1 364 ? -1.283  62.697  90.250  1.00 12.89  ?  365 PHE A CE2   1 
ATOM   2700 C  CZ    . PHE A 1 364 ? -1.138  62.232  91.529  1.00 12.04  ?  365 PHE A CZ    1 
ATOM   2701 N  N     . LEU A 1 365 ? -2.812  60.411  86.754  1.00 14.65  ?  366 LEU A N     1 
ATOM   2702 C  CA    . LEU A 1 365 ? -4.087  61.137  86.647  1.00 15.47  ?  366 LEU A CA    1 
ATOM   2703 C  C     . LEU A 1 365 ? -5.263  60.169  86.473  1.00 17.61  ?  366 LEU A C     1 
ATOM   2704 O  O     . LEU A 1 365 ? -6.280  60.344  87.131  1.00 18.98  ?  366 LEU A O     1 
ATOM   2705 C  CB    . LEU A 1 365 ? -4.062  62.134  85.476  1.00 14.43  ?  366 LEU A CB    1 
ATOM   2706 C  CG    . LEU A 1 365 ? -3.146  63.334  85.639  1.00 13.73  ?  366 LEU A CG    1 
ATOM   2707 C  CD1   . LEU A 1 365 ? -3.137  64.145  84.393  1.00 14.13  ?  366 LEU A CD1   1 
ATOM   2708 C  CD2   . LEU A 1 365 ? -3.561  64.190  86.835  1.00 12.93  ?  366 LEU A CD2   1 
ATOM   2709 N  N     . SER A 1 366 ? -5.110  59.121  85.637  1.00 17.72  ?  367 SER A N     1 
ATOM   2710 C  CA    . SER A 1 366 ? -6.155  58.133  85.432  1.00 18.54  ?  367 SER A CA    1 
ATOM   2711 C  C     . SER A 1 366 ? -6.491  57.356  86.700  1.00 19.29  ?  367 SER A C     1 
ATOM   2712 O  O     . SER A 1 366 ? -7.668  57.091  86.936  1.00 19.45  ?  367 SER A O     1 
ATOM   2713 C  CB    . SER A 1 366 ? -5.784  57.189  84.302  1.00 20.21  ?  367 SER A CB    1 
ATOM   2714 O  OG    . SER A 1 366 ? -5.731  57.895  83.072  1.00 22.97  ?  367 SER A OG    1 
ATOM   2715 N  N     . ARG A 1 367 ? -5.488  57.045  87.547  1.00 19.43  ?  368 ARG A N     1 
ATOM   2716 C  CA    . ARG A 1 367 ? -5.714  56.339  88.818  1.00 20.13  ?  368 ARG A CA    1 
ATOM   2717 C  C     . ARG A 1 367 ? -6.553  57.148  89.811  1.00 21.90  ?  368 ARG A C     1 
ATOM   2718 O  O     . ARG A 1 367 ? -7.320  56.564  90.575  1.00 23.46  ?  368 ARG A O     1 
ATOM   2719 C  CB    . ARG A 1 367 ? -4.391  55.958  89.484  1.00 20.69  ?  368 ARG A CB    1 
ATOM   2720 C  CG    . ARG A 1 367 ? -3.666  54.847  88.744  1.00 22.44  ?  368 ARG A CG    1 
ATOM   2721 C  CD    . ARG A 1 367 ? -2.564  54.214  89.575  1.00 22.33  ?  368 ARG A CD    1 
ATOM   2722 N  NE    . ARG A 1 367 ? -1.449  55.133  89.823  1.00 21.57  ?  368 ARG A NE    1 
ATOM   2723 C  CZ    . ARG A 1 367 ? -0.436  55.332  88.982  1.00 20.55  ?  368 ARG A CZ    1 
ATOM   2724 N  NH1   . ARG A 1 367 ? -0.395  54.696  87.818  1.00 18.46  1  368 ARG A NH1   1 
ATOM   2725 N  NH2   . ARG A 1 367 ? 0.540   56.178  89.296  1.00 19.85  ?  368 ARG A NH2   1 
ATOM   2726 N  N     . HIS A 1 368 ? -6.405  58.471  89.821  1.00 21.44  ?  369 HIS A N     1 
ATOM   2727 C  CA    . HIS A 1 368 ? -7.164  59.322  90.724  1.00 21.59  ?  369 HIS A CA    1 
ATOM   2728 C  C     . HIS A 1 368 ? -8.513  59.756  90.145  1.00 23.02  ?  369 HIS A C     1 
ATOM   2729 O  O     . HIS A 1 368 ? -9.443  59.969  90.907  1.00 23.62  ?  369 HIS A O     1 
ATOM   2730 C  CB    . HIS A 1 368 ? -6.330  60.534  91.157  1.00 20.91  ?  369 HIS A CB    1 
ATOM   2731 C  CG    . HIS A 1 368 ? -5.227  60.160  92.095  1.00 20.02  ?  369 HIS A CG    1 
ATOM   2732 N  ND1   . HIS A 1 368 ? -5.466  59.937  93.441  1.00 21.11  ?  369 HIS A ND1   1 
ATOM   2733 C  CD2   . HIS A 1 368 ? -3.929  59.911  91.838  1.00 20.46  ?  369 HIS A CD2   1 
ATOM   2734 C  CE1   . HIS A 1 368 ? -4.302  59.600  93.961  1.00 21.34  ?  369 HIS A CE1   1 
ATOM   2735 N  NE2   . HIS A 1 368 ? -3.346  59.580  93.039  1.00 21.47  ?  369 HIS A NE2   1 
ATOM   2736 N  N     . ILE A 1 369 ? -8.628  59.886  88.823  1.00 23.80  ?  370 ILE A N     1 
ATOM   2737 C  CA    . ILE A 1 369 ? -9.885  60.296  88.192  1.00 25.88  ?  370 ILE A CA    1 
ATOM   2738 C  C     . ILE A 1 369 ? -10.887 59.134  88.124  1.00 29.46  ?  370 ILE A C     1 
ATOM   2739 O  O     . ILE A 1 369 ? -12.072 59.324  88.415  1.00 30.00  ?  370 ILE A O     1 
ATOM   2740 C  CB    . ILE A 1 369 ? -9.609  60.927  86.801  1.00 25.01  ?  370 ILE A CB    1 
ATOM   2741 C  CG1   . ILE A 1 369 ? -9.072  62.348  86.968  1.00 24.88  ?  370 ILE A CG1   1 
ATOM   2742 C  CG2   . ILE A 1 369 ? -10.851 60.905  85.883  1.00 25.07  ?  370 ILE A CG2   1 
ATOM   2743 C  CD1   . ILE A 1 369 ? -8.389  62.807  85.854  1.00 25.50  ?  370 ILE A CD1   1 
ATOM   2744 N  N     . ASP A 1 370 ? -10.409 57.938  87.745  1.00 31.61  ?  371 ASP A N     1 
ATOM   2745 C  CA    . ASP A 1 370 ? -11.247 56.748  87.606  1.00 34.54  ?  371 ASP A CA    1 
ATOM   2746 C  C     . ASP A 1 370 ? -11.373 55.952  88.926  1.00 37.56  ?  371 ASP A C     1 
ATOM   2747 O  O     . ASP A 1 370 ? -11.383 54.722  88.893  1.00 38.77  ?  371 ASP A O     1 
ATOM   2748 C  CB    . ASP A 1 370 ? -10.713 55.838  86.469  1.00 36.42  ?  371 ASP A CB    1 
ATOM   2749 C  CG    . ASP A 1 370 ? -10.409 56.562  85.157  1.00 42.97  ?  371 ASP A CG    1 
ATOM   2750 O  OD1   . ASP A 1 370 ? -11.099 57.561  84.851  1.00 44.05  ?  371 ASP A OD1   1 
ATOM   2751 O  OD2   . ASP A 1 370 ? -9.478  56.129  84.437  1.00 46.00  ?  371 ASP A OD2   1 
ATOM   2752 N  N     . THR A 1 371 ? -11.452 56.633  90.081  1.00 38.53  ?  372 THR A N     1 
ATOM   2753 C  CA    . THR A 1 371 ? -11.596 55.953  91.371  1.00 39.96  ?  372 THR A CA    1 
ATOM   2754 C  C     . THR A 1 371 ? -13.073 55.754  91.725  1.00 41.20  ?  372 THR A C     1 
ATOM   2755 O  O     . THR A 1 371 ? -13.956 55.898  90.880  1.00 41.95  ?  372 THR A O     1 
ATOM   2756 C  CB    . THR A 1 371 ? -10.830 56.701  92.488  1.00 41.52  ?  372 THR A CB    1 
ATOM   2757 O  OG1   . THR A 1 371 ? -9.434  56.477  92.342  1.00 42.41  ?  372 THR A OG1   1 
ATOM   2758 C  CG2   . THR A 1 371 ? -11.244 56.267  93.891  1.00 42.24  ?  372 THR A CG2   1 
ATOM   2759 N  N     . GLU B 2 27  ? 9.103   84.552  69.440  1.00 80.57  ?  15  GLU B N     1 
ATOM   2760 C  CA    . GLU B 2 27  ? 8.073   85.589  69.343  1.00 81.63  ?  15  GLU B CA    1 
ATOM   2761 C  C     . GLU B 2 27  ? 6.697   85.001  68.954  1.00 79.44  ?  15  GLU B C     1 
ATOM   2762 O  O     . GLU B 2 27  ? 5.661   85.526  69.366  1.00 80.18  ?  15  GLU B O     1 
ATOM   2763 C  CB    . GLU B 2 27  ? 8.517   86.744  68.408  1.00 86.02  ?  15  GLU B CB    1 
ATOM   2764 C  CG    . GLU B 2 27  ? 8.307   86.519  66.914  1.00 91.57  ?  15  GLU B CG    1 
ATOM   2765 C  CD    . GLU B 2 27  ? 9.363   85.729  66.158  1.00 98.94  ?  15  GLU B CD    1 
ATOM   2766 O  OE1   . GLU B 2 27  ? 9.909   84.755  66.725  1.00 99.99  ?  15  GLU B OE1   1 
ATOM   2767 O  OE2   . GLU B 2 27  ? 9.637   86.079  64.987  1.00 101.48 ?  15  GLU B OE2   1 
ATOM   2768 N  N     . LEU B 2 28  ? 6.720   83.853  68.277  1.00 76.55  ?  16  LEU B N     1 
ATOM   2769 C  CA    . LEU B 2 28  ? 5.448   83.233  67.823  1.00 74.29  ?  16  LEU B CA    1 
ATOM   2770 C  C     . LEU B 2 28  ? 4.841   82.349  68.923  1.00 71.55  ?  16  LEU B C     1 
ATOM   2771 O  O     . LEU B 2 28  ? 5.560   82.020  69.880  1.00 71.76  ?  16  LEU B O     1 
ATOM   2772 C  CB    . LEU B 2 28  ? 5.656   82.478  66.497  1.00 73.75  ?  16  LEU B CB    1 
ATOM   2773 N  N     . THR B 2 29  ? 3.557   82.007  68.787  1.00 68.69  ?  17  THR B N     1 
ATOM   2774 C  CA    . THR B 2 29  ? 2.859   81.163  69.758  1.00 66.23  ?  17  THR B CA    1 
ATOM   2775 C  C     . THR B 2 29  ? 3.516   79.776  69.782  1.00 63.41  ?  17  THR B C     1 
ATOM   2776 O  O     . THR B 2 29  ? 3.725   79.179  68.729  1.00 62.98  ?  17  THR B O     1 
ATOM   2777 C  CB    . THR B 2 29  ? 1.357   81.107  69.426  1.00 66.61  ?  17  THR B CB    1 
ATOM   2778 O  OG1   . THR B 2 29  ? 0.869   82.437  69.252  1.00 68.97  ?  17  THR B OG1   1 
ATOM   2779 C  CG2   . THR B 2 29  ? 0.544   80.403  70.501  1.00 65.88  ?  17  THR B CG2   1 
ATOM   2780 N  N     . PRO B 2 30  ? 3.896   79.265  70.966  1.00 61.24  ?  18  PRO B N     1 
ATOM   2781 C  CA    . PRO B 2 30  ? 4.598   77.974  71.013  1.00 58.74  ?  18  PRO B CA    1 
ATOM   2782 C  C     . PRO B 2 30  ? 3.755   76.775  70.572  1.00 55.24  ?  18  PRO B C     1 
ATOM   2783 O  O     . PRO B 2 30  ? 4.286   75.800  70.035  1.00 54.05  ?  18  PRO B O     1 
ATOM   2784 C  CB    . PRO B 2 30  ? 5.057   77.875  72.475  1.00 60.16  ?  18  PRO B CB    1 
ATOM   2785 C  CG    . PRO B 2 30  ? 4.966   79.282  73.015  1.00 62.50  ?  18  PRO B CG    1 
ATOM   2786 C  CD    . PRO B 2 30  ? 3.782   79.861  72.308  1.00 61.24  ?  18  PRO B CD    1 
ATOM   2787 N  N     . GLY B 2 31  ? 2.445   76.865  70.781  1.00 53.27  ?  19  GLY B N     1 
ATOM   2788 C  CA    . GLY B 2 31  ? 1.544   75.792  70.391  1.00 50.38  ?  19  GLY B CA    1 
ATOM   2789 C  C     . GLY B 2 31  ? 0.095   76.202  70.247  1.00 48.04  ?  19  GLY B C     1 
ATOM   2790 O  O     . GLY B 2 31  ? -0.396  77.057  70.988  1.00 49.68  ?  19  GLY B O     1 
ATOM   2791 N  N     . ILE B 2 32  ? -0.593  75.610  69.271  1.00 44.16  ?  20  ILE B N     1 
ATOM   2792 C  CA    . ILE B 2 32  ? -2.014  75.834  69.066  1.00 41.84  ?  20  ILE B CA    1 
ATOM   2793 C  C     . ILE B 2 32  ? -2.655  74.457  69.002  1.00 38.25  ?  20  ILE B C     1 
ATOM   2794 O  O     . ILE B 2 32  ? -2.383  73.695  68.074  1.00 38.01  ?  20  ILE B O     1 
ATOM   2795 C  CB    . ILE B 2 32  ? -2.334  76.685  67.811  1.00 43.01  ?  20  ILE B CB    1 
ATOM   2796 C  CG1   . ILE B 2 32  ? -1.540  78.012  67.821  1.00 45.43  ?  20  ILE B CG1   1 
ATOM   2797 C  CG2   . ILE B 2 32  ? -3.844  76.935  67.719  1.00 43.42  ?  20  ILE B CG2   1 
ATOM   2798 C  CD1   . ILE B 2 32  ? -1.827  78.987  66.674  1.00 47.47  ?  20  ILE B CD1   1 
ATOM   2799 N  N     . PHE B 2 33  ? -3.452  74.103  70.010  1.00 35.49  ?  21  PHE B N     1 
ATOM   2800 C  CA    . PHE B 2 33  ? -4.083  72.785  70.053  1.00 32.21  ?  21  PHE B CA    1 
ATOM   2801 C  C     . PHE B 2 33  ? -5.531  72.852  69.588  1.00 30.27  ?  21  PHE B C     1 
ATOM   2802 O  O     . PHE B 2 33  ? -6.339  73.579  70.168  1.00 30.95  ?  21  PHE B O     1 
ATOM   2803 C  CB    . PHE B 2 33  ? -3.999  72.205  71.469  1.00 31.15  ?  21  PHE B CB    1 
ATOM   2804 C  CG    . PHE B 2 33  ? -4.606  70.833  71.657  1.00 30.10  ?  21  PHE B CG    1 
ATOM   2805 C  CD1   . PHE B 2 33  ? -5.940  70.687  72.005  1.00 30.09  ?  21  PHE B CD1   1 
ATOM   2806 C  CD2   . PHE B 2 33  ? -3.823  69.695  71.577  1.00 29.54  ?  21  PHE B CD2   1 
ATOM   2807 C  CE1   . PHE B 2 33  ? -6.480  69.430  72.227  1.00 29.81  ?  21  PHE B CE1   1 
ATOM   2808 C  CE2   . PHE B 2 33  ? -4.370  68.442  71.794  1.00 29.01  ?  21  PHE B CE2   1 
ATOM   2809 C  CZ    . PHE B 2 33  ? -5.688  68.318  72.135  1.00 28.76  ?  21  PHE B CZ    1 
ATOM   2810 N  N     . LYS B 2 34  ? -5.864  72.071  68.569  1.00 27.84  ?  22  LYS B N     1 
ATOM   2811 C  CA    . LYS B 2 34  ? -7.230  72.014  68.072  1.00 26.53  ?  22  LYS B CA    1 
ATOM   2812 C  C     . LYS B 2 34  ? -7.872  70.680  68.440  1.00 24.16  ?  22  LYS B C     1 
ATOM   2813 O  O     . LYS B 2 34  ? -8.960  70.668  69.004  1.00 24.60  ?  22  LYS B O     1 
ATOM   2814 C  CB    . LYS B 2 34  ? -7.293  72.272  66.548  1.00 28.10  ?  22  LYS B CB    1 
ATOM   2815 C  CG    . LYS B 2 34  ? -7.008  73.715  66.141  1.00 32.70  ?  22  LYS B CG    1 
ATOM   2816 C  CD    . LYS B 2 34  ? -7.997  74.696  66.763  1.00 37.79  ?  22  LYS B CD    1 
ATOM   2817 C  CE    . LYS B 2 34  ? -7.681  76.129  66.415  1.00 42.77  ?  22  LYS B CE    1 
ATOM   2818 N  NZ    . LYS B 2 34  ? -8.634  77.064  67.072  1.00 45.56  1  22  LYS B NZ    1 
ATOM   2819 N  N     . LYS B 2 35  ? -7.193  69.565  68.148  1.00 21.80  ?  23  LYS B N     1 
ATOM   2820 C  CA    . LYS B 2 35  ? -7.724  68.231  68.409  1.00 20.33  ?  23  LYS B CA    1 
ATOM   2821 C  C     . LYS B 2 35  ? -6.637  67.300  68.926  1.00 19.49  ?  23  LYS B C     1 
ATOM   2822 O  O     . LYS B 2 35  ? -5.477  67.417  68.537  1.00 19.32  ?  23  LYS B O     1 
ATOM   2823 C  CB    . LYS B 2 35  ? -8.253  67.611  67.104  1.00 20.62  ?  23  LYS B CB    1 
ATOM   2824 C  CG    . LYS B 2 35  ? -9.615  68.068  66.674  1.00 23.24  ?  23  LYS B CG    1 
ATOM   2825 C  CD    . LYS B 2 35  ? -9.790  67.723  65.220  1.00 25.55  ?  23  LYS B CD    1 
ATOM   2826 C  CE    . LYS B 2 35  ? -11.218 67.783  64.792  1.00 27.31  ?  23  LYS B CE    1 
ATOM   2827 N  NZ    . LYS B 2 35  ? -11.313 67.840  63.322  1.00 27.82  1  23  LYS B NZ    1 
ATOM   2828 N  N     . GLY B 2 36  ? -7.043  66.316  69.703  1.00 18.86  ?  24  GLY B N     1 
ATOM   2829 C  CA    . GLY B 2 36  ? -6.129  65.321  70.215  1.00 18.97  ?  24  GLY B CA    1 
ATOM   2830 C  C     . GLY B 2 36  ? -6.837  64.211  70.937  1.00 19.69  ?  24  GLY B C     1 
ATOM   2831 O  O     . GLY B 2 36  ? -8.009  64.334  71.293  1.00 20.54  ?  24  GLY B O     1 
ATOM   2832 N  N     . ILE B 2 37  ? -6.139  63.110  71.129  1.00 19.63  ?  25  ILE B N     1 
ATOM   2833 C  CA    . ILE B 2 37  ? -6.645  61.923  71.829  1.00 20.53  ?  25  ILE B CA    1 
ATOM   2834 C  C     . ILE B 2 37  ? -5.504  61.358  72.720  1.00 21.35  ?  25  ILE B C     1 
ATOM   2835 O  O     . ILE B 2 37  ? -4.370  61.851  72.667  1.00 20.75  ?  25  ILE B O     1 
ATOM   2836 C  CB    . ILE B 2 37  ? -7.133  60.841  70.798  1.00 20.83  ?  25  ILE B CB    1 
ATOM   2837 C  CG1   . ILE B 2 37  ? -5.981  60.387  69.876  1.00 20.80  ?  25  ILE B CG1   1 
ATOM   2838 C  CG2   . ILE B 2 37  ? -8.377  61.270  70.008  1.00 21.16  ?  25  ILE B CG2   1 
ATOM   2839 C  CD1   . ILE B 2 37  ? -6.273  59.166  69.102  1.00 21.74  ?  25  ILE B CD1   1 
ATOM   2840 N  N     . GLU B 2 38  ? -5.797  60.336  73.536  1.00 22.62  ?  26  GLU B N     1 
ATOM   2841 C  CA    . GLU B 2 38  ? -4.749  59.675  74.302  1.00 24.11  ?  26  GLU B CA    1 
ATOM   2842 C  C     . GLU B 2 38  ? -4.094  58.710  73.318  1.00 23.93  ?  26  GLU B C     1 
ATOM   2843 O  O     . GLU B 2 38  ? -4.772  57.879  72.715  1.00 24.42  ?  26  GLU B O     1 
ATOM   2844 C  CB    . GLU B 2 38  ? -5.287  59.010  75.584  1.00 27.81  ?  26  GLU B CB    1 
ATOM   2845 C  CG    . GLU B 2 38  ? -5.474  60.039  76.679  1.00 35.28  ?  26  GLU B CG    1 
ATOM   2846 C  CD    . GLU B 2 38  ? -6.206  59.572  77.919  1.00 48.55  ?  26  GLU B CD    1 
ATOM   2847 O  OE1   . GLU B 2 38  ? -5.540  59.064  78.852  1.00 52.38  ?  26  GLU B OE1   1 
ATOM   2848 O  OE2   . GLU B 2 38  ? -7.445  59.745  77.975  1.00 52.90  -1 26  GLU B OE2   1 
ATOM   2849 N  N     . ILE B 2 39  ? -2.815  58.936  73.039  1.00 23.46  ?  27  ILE B N     1 
ATOM   2850 C  CA    . ILE B 2 39  ? -2.039  58.167  72.083  1.00 23.50  ?  27  ILE B CA    1 
ATOM   2851 C  C     . ILE B 2 39  ? -0.577  58.076  72.512  1.00 24.59  ?  27  ILE B C     1 
ATOM   2852 O  O     . ILE B 2 39  ? -0.040  59.013  73.101  1.00 24.89  ?  27  ILE B O     1 
ATOM   2853 C  CB    . ILE B 2 39  ? -2.165  58.837  70.682  1.00 23.09  ?  27  ILE B CB    1 
ATOM   2854 C  CG1   . ILE B 2 39  ? -1.394  58.068  69.618  1.00 23.71  ?  27  ILE B CG1   1 
ATOM   2855 C  CG2   . ILE B 2 39  ? -1.768  60.327  70.692  1.00 22.67  ?  27  ILE B CG2   1 
ATOM   2856 C  CD1   . ILE B 2 39  ? -1.887  58.334  68.340  1.00 24.74  ?  27  ILE B CD1   1 
ATOM   2857 N  N     . THR B 2 40  ? 0.055   56.935  72.258  1.00 25.36  ?  28  THR B N     1 
ATOM   2858 C  CA    . THR B 2 40  ? 1.484   56.757  72.475  1.00 26.80  ?  28  THR B CA    1 
ATOM   2859 C  C     . THR B 2 40  ? 2.089   56.141  71.228  1.00 27.34  ?  28  THR B C     1 
ATOM   2860 O  O     . THR B 2 40  ? 1.456   55.313  70.584  1.00 27.49  ?  28  THR B O     1 
ATOM   2861 C  CB    . THR B 2 40  ? 1.858   55.936  73.729  1.00 29.61  ?  28  THR B CB    1 
ATOM   2862 O  OG1   . THR B 2 40  ? 1.433   54.584  73.580  1.00 32.24  ?  28  THR B OG1   1 
ATOM   2863 C  CG2   . THR B 2 40  ? 1.376   56.548  75.039  1.00 29.85  ?  28  THR B CG2   1 
ATOM   2864 N  N     . ILE B 2 41  ? 3.306   56.534  70.886  1.00 28.09  ?  29  ILE B N     1 
ATOM   2865 C  CA    . ILE B 2 41  ? 4.003   55.975  69.734  1.00 29.60  ?  29  ILE B CA    1 
ATOM   2866 C  C     . ILE B 2 41  ? 5.465   55.647  70.076  1.00 32.31  ?  29  ILE B C     1 
ATOM   2867 O  O     . ILE B 2 41  ? 6.099   56.374  70.819  1.00 32.40  ?  29  ILE B O     1 
ATOM   2868 C  CB    . ILE B 2 41  ? 3.854   56.859  68.464  1.00 29.02  ?  29  ILE B CB    1 
ATOM   2869 C  CG1   . ILE B 2 41  ? 4.229   56.064  67.198  1.00 29.55  ?  29  ILE B CG1   1 
ATOM   2870 C  CG2   . ILE B 2 41  ? 4.652   58.177  68.575  1.00 28.90  ?  29  ILE B CG2   1 
ATOM   2871 C  CD1   . ILE B 2 41  ? 3.813   56.684  65.974  1.00 30.05  ?  29  ILE B CD1   1 
ATOM   2872 N  N     . ASP B 2 42  ? 5.970   54.514  69.588  1.00 34.81  ?  30  ASP B N     1 
ATOM   2873 C  CA    . ASP B 2 42  ? 7.357   54.101  69.778  1.00 37.54  ?  30  ASP B CA    1 
ATOM   2874 C  C     . ASP B 2 42  ? 7.904   53.820  68.371  1.00 37.90  ?  30  ASP B C     1 
ATOM   2875 O  O     . ASP B 2 42  ? 7.500   52.837  67.764  1.00 37.88  ?  30  ASP B O     1 
ATOM   2876 C  CB    . ASP B 2 42  ? 7.420   52.827  70.631  1.00 42.27  ?  30  ASP B CB    1 
ATOM   2877 C  CG    . ASP B 2 42  ? 8.828   52.405  71.037  1.00 52.06  ?  30  ASP B CG    1 
ATOM   2878 O  OD1   . ASP B 2 42  ? 9.782   53.188  70.797  1.00 53.83  ?  30  ASP B OD1   1 
ATOM   2879 O  OD2   . ASP B 2 42  ? 8.974   51.302  71.618  1.00 56.28  ?  30  ASP B OD2   1 
ATOM   2880 N  N     . LEU B 2 43  ? 8.769   54.697  67.834  1.00 38.00  ?  31  LEU B N     1 
ATOM   2881 C  CA    . LEU B 2 43  ? 9.303   54.517  66.486  1.00 39.02  ?  31  LEU B CA    1 
ATOM   2882 C  C     . LEU B 2 43  ? 10.465  53.493  66.393  1.00 41.57  ?  31  LEU B C     1 
ATOM   2883 O  O     . LEU B 2 43  ? 10.917  53.184  65.282  1.00 42.13  ?  31  LEU B O     1 
ATOM   2884 C  CB    . LEU B 2 43  ? 9.688   55.858  65.853  1.00 38.64  ?  31  LEU B CB    1 
ATOM   2885 C  CG    . LEU B 2 43  ? 8.542   56.880  65.720  1.00 39.58  ?  31  LEU B CG    1 
ATOM   2886 C  CD1   . LEU B 2 43  ? 9.044   58.202  65.133  1.00 40.08  ?  31  LEU B CD1   1 
ATOM   2887 C  CD2   . LEU B 2 43  ? 7.381   56.327  64.881  1.00 39.58  ?  31  LEU B CD2   1 
ATOM   2888 N  N     . GLU B 2 44  ? 10.921  52.938  67.536  1.00 42.78  ?  32  GLU B N     1 
ATOM   2889 C  CA    . GLU B 2 44  ? 11.934  51.886  67.509  1.00 45.04  ?  32  GLU B CA    1 
ATOM   2890 C  C     . GLU B 2 44  ? 11.183  50.570  67.281  1.00 45.26  ?  32  GLU B C     1 
ATOM   2891 O  O     . GLU B 2 44  ? 11.517  49.818  66.366  1.00 46.14  ?  32  GLU B O     1 
ATOM   2892 C  CB    . GLU B 2 44  ? 12.750  51.825  68.816  1.00 49.67  ?  32  GLU B CB    1 
ATOM   2893 C  CG    . GLU B 2 44  ? 13.567  53.067  69.090  1.00 57.33  ?  32  GLU B CG    1 
ATOM   2894 C  CD    . GLU B 2 44  ? 13.203  53.714  70.410  1.00 67.68  ?  32  GLU B CD    1 
ATOM   2895 O  OE1   . GLU B 2 44  ? 12.278  54.560  70.420  1.00 69.07  ?  32  GLU B OE1   1 
ATOM   2896 O  OE2   . GLU B 2 44  ? 13.833  53.365  71.436  1.00 71.88  ?  32  GLU B OE2   1 
ATOM   2897 N  N     . GLU B 2 45  ? 10.147  50.313  68.099  1.00 44.40  ?  33  GLU B N     1 
ATOM   2898 C  CA    . GLU B 2 45  ? 9.293   49.134  67.970  1.00 44.64  ?  33  GLU B CA    1 
ATOM   2899 C  C     . GLU B 2 45  ? 8.308   49.262  66.782  1.00 42.56  ?  33  GLU B C     1 
ATOM   2900 O  O     . GLU B 2 45  ? 7.732   48.256  66.369  1.00 43.60  ?  33  GLU B O     1 
ATOM   2901 C  CB    . GLU B 2 45  ? 8.496   48.915  69.264  1.00 48.75  ?  33  GLU B CB    1 
ATOM   2902 C  CG    . GLU B 2 45  ? 8.995   47.771  70.124  1.00 59.08  ?  33  GLU B CG    1 
ATOM   2903 C  CD    . GLU B 2 45  ? 7.891   46.938  70.755  1.00 70.15  ?  33  GLU B CD    1 
ATOM   2904 O  OE1   . GLU B 2 45  ? 7.463   47.273  71.885  1.00 72.49  ?  33  GLU B OE1   1 
ATOM   2905 O  OE2   . GLU B 2 45  ? 7.458   45.947  70.122  1.00 73.59  ?  33  GLU B OE2   1 
ATOM   2906 N  N     . MET B 2 46  ? 8.120   50.492  66.246  1.00 39.64  ?  34  MET B N     1 
ATOM   2907 C  CA    . MET B 2 46  ? 7.204   50.850  65.172  1.00 37.25  ?  34  MET B CA    1 
ATOM   2908 C  C     . MET B 2 46  ? 5.792   50.415  65.522  1.00 35.98  ?  34  MET B C     1 
ATOM   2909 O  O     . MET B 2 46  ? 5.131   49.726  64.744  1.00 36.49  ?  34  MET B O     1 
ATOM   2910 C  CB    . MET B 2 46  ? 7.689   50.355  63.807  1.00 37.84  ?  34  MET B CB    1 
ATOM   2911 C  CG    . MET B 2 46  ? 8.913   51.108  63.301  1.00 40.40  ?  34  MET B CG    1 
ATOM   2912 S  SD    . MET B 2 46  ? 8.642   52.867  62.892  1.00 45.32  ?  34  MET B SD    1 
ATOM   2913 C  CE    . MET B 2 46  ? 8.086   52.734  61.211  1.00 42.27  ?  34  MET B CE    1 
ATOM   2914 N  N     . VAL B 2 47  ? 5.359   50.773  66.740  1.00 34.50  ?  35  VAL B N     1 
ATOM   2915 C  CA    . VAL B 2 47  ? 4.027   50.484  67.268  1.00 34.09  ?  35  VAL B CA    1 
ATOM   2916 C  C     . VAL B 2 47  ? 3.366   51.756  67.789  1.00 31.88  ?  35  VAL B C     1 
ATOM   2917 O  O     . VAL B 2 47  ? 4.036   52.681  68.240  1.00 31.75  ?  35  VAL B O     1 
ATOM   2918 C  CB    . VAL B 2 47  ? 3.978   49.364  68.348  1.00 36.45  ?  35  VAL B CB    1 
ATOM   2919 C  CG1   . VAL B 2 47  ? 4.312   47.999  67.755  1.00 38.81  ?  35  VAL B CG1   1 
ATOM   2920 C  CG2   . VAL B 2 47  ? 4.874   49.682  69.536  1.00 36.88  ?  35  VAL B CG2   1 
ATOM   2921 N  N     . CYS B 2 48  ? 2.042   51.785  67.745  1.00 30.25  ?  36  CYS B N     1 
ATOM   2922 C  CA    . CYS B 2 48  ? 1.254   52.910  68.232  1.00 28.58  ?  36  CYS B CA    1 
ATOM   2923 C  C     . CYS B 2 48  ? 0.050   52.406  68.997  1.00 27.87  ?  36  CYS B C     1 
ATOM   2924 O  O     . CYS B 2 48  ? -0.487  51.359  68.677  1.00 28.79  ?  36  CYS B O     1 
ATOM   2925 C  CB    . CYS B 2 48  ? 0.840   53.827  67.086  1.00 27.76  ?  36  CYS B CB    1 
ATOM   2926 S  SG    . CYS B 2 48  ? 0.087   55.376  67.627  1.00 25.51  ?  36  CYS B SG    1 
ATOM   2927 N  N     . TYR B 2 49  ? -0.377  53.149  70.007  1.00 26.81  ?  37  TYR B N     1 
ATOM   2928 C  CA    . TYR B 2 49  ? -1.503  52.765  70.840  1.00 26.45  ?  37  TYR B CA    1 
ATOM   2929 C  C     . TYR B 2 49  ? -2.526  53.876  70.915  1.00 25.50  ?  37  TYR B C     1 
ATOM   2930 O  O     . TYR B 2 49  ? -2.234  54.941  71.450  1.00 25.12  ?  37  TYR B O     1 
ATOM   2931 C  CB    . TYR B 2 49  ? -1.025  52.431  72.261  1.00 26.69  ?  37  TYR B CB    1 
ATOM   2932 C  CG    . TYR B 2 49  ? -0.097  51.242  72.334  1.00 28.12  ?  37  TYR B CG    1 
ATOM   2933 C  CD1   . TYR B 2 49  ? -0.588  49.945  72.261  1.00 29.97  ?  37  TYR B CD1   1 
ATOM   2934 C  CD2   . TYR B 2 49  ? 1.271   51.412  72.498  1.00 29.05  ?  37  TYR B CD2   1 
ATOM   2935 C  CE1   . TYR B 2 49  ? 0.257   48.846  72.362  1.00 31.79  ?  37  TYR B CE1   1 
ATOM   2936 C  CE2   . TYR B 2 49  ? 2.129   50.321  72.583  1.00 30.80  ?  37  TYR B CE2   1 
ATOM   2937 C  CZ    . TYR B 2 49  ? 1.617   49.037  72.517  1.00 33.00  ?  37  TYR B CZ    1 
ATOM   2938 O  OH    . TYR B 2 49  ? 2.460   47.950  72.589  1.00 36.45  ?  37  TYR B OH    1 
ATOM   2939 N  N     . HIS B 2 50  ? -3.732  53.619  70.417  1.00 25.41  ?  38  HIS B N     1 
ATOM   2940 C  CA    . HIS B 2 50  ? -4.844  54.555  70.501  1.00 25.58  ?  38  HIS B CA    1 
ATOM   2941 C  C     . HIS B 2 50  ? -6.178  53.849  70.314  1.00 27.91  ?  38  HIS B C     1 
ATOM   2942 O  O     . HIS B 2 50  ? -6.240  52.804  69.666  1.00 28.48  ?  38  HIS B O     1 
ATOM   2943 C  CB    . HIS B 2 50  ? -4.697  55.776  69.564  1.00 24.15  ?  38  HIS B CB    1 
ATOM   2944 C  CG    . HIS B 2 50  ? -4.865  55.487  68.103  1.00 23.19  ?  38  HIS B CG    1 
ATOM   2945 N  ND1   . HIS B 2 50  ? -6.116  55.451  67.511  1.00 24.11  ?  38  HIS B ND1   1 
ATOM   2946 C  CD2   . HIS B 2 50  ? -3.926  55.281  67.150  1.00 23.46  ?  38  HIS B CD2   1 
ATOM   2947 C  CE1   . HIS B 2 50  ? -5.899  55.204  66.232  1.00 24.32  ?  38  HIS B CE1   1 
ATOM   2948 N  NE2   . HIS B 2 50  ? -4.598  55.079  65.970  1.00 24.27  ?  38  HIS B NE2   1 
ATOM   2949 N  N     . SER B 2 51  ? -7.241  54.403  70.923  1.00 29.19  ?  39  SER B N     1 
ATOM   2950 C  CA    . SER B 2 51  ? -8.616  53.905  70.808  1.00 30.96  ?  39  SER B CA    1 
ATOM   2951 C  C     . SER B 2 51  ? -8.806  52.473  71.333  1.00 33.62  ?  39  SER B C     1 
ATOM   2952 O  O     . SER B 2 51  ? -9.659  51.736  70.834  1.00 35.21  ?  39  SER B O     1 
ATOM   2953 C  CB    . SER B 2 51  ? -9.093  54.016  69.363  1.00 31.57  ?  39  SER B CB    1 
ATOM   2954 O  OG    . SER B 2 51  ? -8.768  55.278  68.795  1.00 32.92  ?  39  SER B OG    1 
ATOM   2955 N  N     . GLY B 2 52  ? -8.005  52.082  72.316  1.00 33.94  ?  40  GLY B N     1 
ATOM   2956 C  CA    . GLY B 2 52  ? -8.041  50.730  72.863  1.00 35.66  ?  40  GLY B CA    1 
ATOM   2957 C  C     . GLY B 2 52  ? -7.464  49.664  71.942  1.00 36.70  ?  40  GLY B C     1 
ATOM   2958 O  O     . GLY B 2 52  ? -7.661  48.472  72.179  1.00 38.24  ?  40  GLY B O     1 
ATOM   2959 N  N     . LEU B 2 53  ? -6.724  50.073  70.891  1.00 35.98  ?  41  LEU B N     1 
ATOM   2960 C  CA    . LEU B 2 53  ? -6.150  49.146  69.910  1.00 36.82  ?  41  LEU B CA    1 
ATOM   2961 C  C     . LEU B 2 53  ? -4.622  49.280  69.701  1.00 36.24  ?  41  LEU B C     1 
ATOM   2962 O  O     . LEU B 2 53  ? -4.028  50.298  70.053  1.00 35.30  ?  41  LEU B O     1 
ATOM   2963 C  CB    . LEU B 2 53  ? -6.893  49.313  68.572  1.00 37.24  ?  41  LEU B CB    1 
ATOM   2964 C  CG    . LEU B 2 53  ? -8.373  48.888  68.573  1.00 40.14  ?  41  LEU B CG    1 
ATOM   2965 C  CD1   . LEU B 2 53  ? -9.113  49.456  67.367  1.00 40.17  ?  41  LEU B CD1   1 
ATOM   2966 C  CD2   . LEU B 2 53  ? -8.524  47.356  68.683  1.00 41.86  ?  41  LEU B CD2   1 
ATOM   2967 N  N     . THR B 2 54  ? -3.984  48.241  69.132  1.00 36.85  ?  42  THR B N     1 
ATOM   2968 C  CA    . THR B 2 54  ? -2.548  48.279  68.835  1.00 37.01  ?  42  THR B CA    1 
ATOM   2969 C  C     . THR B 2 54  ? -2.365  48.425  67.334  1.00 36.04  ?  42  THR B C     1 
ATOM   2970 O  O     . THR B 2 54  ? -2.929  47.637  66.579  1.00 37.07  ?  42  THR B O     1 
ATOM   2971 C  CB    . THR B 2 54  ? -1.847  47.032  69.348  1.00 40.27  ?  42  THR B CB    1 
ATOM   2972 O  OG1   . THR B 2 54  ? -2.009  46.973  70.766  1.00 42.42  ?  42  THR B OG1   1 
ATOM   2973 C  CG2   . THR B 2 54  ? -0.362  47.023  69.005  1.00 40.52  ?  42  THR B CG2   1 
ATOM   2974 N  N     . TRP B 2 55  ? -1.595  49.430  66.895  1.00 33.99  ?  43  TRP B N     1 
ATOM   2975 C  CA    . TRP B 2 55  ? -1.406  49.730  65.475  1.00 32.97  ?  43  TRP B CA    1 
ATOM   2976 C  C     . TRP B 2 55  ? 0.037   49.563  65.059  1.00 32.53  ?  43  TRP B C     1 
ATOM   2977 O  O     . TRP B 2 55  ? 0.927   50.051  65.736  1.00 31.98  ?  43  TRP B O     1 
ATOM   2978 C  CB    . TRP B 2 55  ? -1.841  51.180  65.172  1.00 31.79  ?  43  TRP B CB    1 
ATOM   2979 C  CG    . TRP B 2 55  ? -3.175  51.534  65.746  1.00 32.01  ?  43  TRP B CG    1 
ATOM   2980 C  CD1   . TRP B 2 55  ? -3.431  51.995  67.006  1.00 32.46  ?  43  TRP B CD1   1 
ATOM   2981 C  CD2   . TRP B 2 55  ? -4.448  51.328  65.127  1.00 32.39  ?  43  TRP B CD2   1 
ATOM   2982 N  NE1   . TRP B 2 55  ? -4.785  52.109  67.199  1.00 32.81  ?  43  TRP B NE1   1 
ATOM   2983 C  CE2   . TRP B 2 55  ? -5.434  51.717  66.056  1.00 32.74  ?  43  TRP B CE2   1 
ATOM   2984 C  CE3   . TRP B 2 55  ? -4.849  50.876  63.863  1.00 33.78  ?  43  TRP B CE3   1 
ATOM   2985 C  CZ2   . TRP B 2 55  ? -6.790  51.673  65.762  1.00 33.74  ?  43  TRP B CZ2   1 
ATOM   2986 C  CZ3   . TRP B 2 55  ? -6.199  50.815  63.578  1.00 35.29  ?  43  TRP B CZ3   1 
ATOM   2987 C  CH2   . TRP B 2 55  ? -7.153  51.190  64.531  1.00 35.01  ?  43  TRP B CH2   1 
ATOM   2988 N  N     . LYS B 2 56  ? 0.269   48.926  63.915  1.00 32.82  ?  44  LYS B N     1 
ATOM   2989 C  CA    . LYS B 2 56  ? 1.610   48.751  63.371  1.00 32.76  ?  44  LYS B CA    1 
ATOM   2990 C  C     . LYS B 2 56  ? 1.954   49.997  62.573  1.00 30.85  ?  44  LYS B C     1 
ATOM   2991 O  O     . LYS B 2 56  ? 1.175   50.410  61.727  1.00 30.08  ?  44  LYS B O     1 
ATOM   2992 C  CB    . LYS B 2 56  ? 1.684   47.496  62.480  1.00 36.03  ?  44  LYS B CB    1 
ATOM   2993 C  CG    . LYS B 2 56  ? 3.118   47.100  62.126  1.00 42.65  ?  44  LYS B CG    1 
ATOM   2994 C  CD    . LYS B 2 56  ? 3.920   46.704  63.386  1.00 49.65  ?  44  LYS B CD    1 
ATOM   2995 C  CE    . LYS B 2 56  ? 5.421   46.712  63.215  1.00 53.66  ?  44  LYS B CE    1 
ATOM   2996 N  NZ    . LYS B 2 56  ? 6.094   47.037  64.501  1.00 55.64  1  44  LYS B NZ    1 
ATOM   2997 N  N     . VAL B 2 57  ? 3.109   50.599  62.845  1.00 30.39  ?  45  VAL B N     1 
ATOM   2998 C  CA    . VAL B 2 57  ? 3.535   51.818  62.163  1.00 30.01  ?  45  VAL B CA    1 
ATOM   2999 C  C     . VAL B 2 57  ? 4.428   51.533  60.938  1.00 30.59  ?  45  VAL B C     1 
ATOM   3000 O  O     . VAL B 2 57  ? 5.300   50.663  60.975  1.00 31.05  ?  45  VAL B O     1 
ATOM   3001 C  CB    . VAL B 2 57  ? 4.211   52.799  63.166  1.00 30.05  ?  45  VAL B CB    1 
ATOM   3002 C  CG1   . VAL B 2 57  ? 4.578   54.131  62.510  1.00 29.58  ?  45  VAL B CG1   1 
ATOM   3003 C  CG2   . VAL B 2 57  ? 3.323   53.033  64.381  1.00 30.30  ?  45  VAL B CG2   1 
ATOM   3004 N  N     . LYS B 2 58  ? 4.214   52.280  59.858  1.00 30.38  ?  46  LYS B N     1 
ATOM   3005 C  CA    . LYS B 2 58  ? 5.053   52.171  58.665  1.00 31.14  ?  46  LYS B CA    1 
ATOM   3006 C  C     . LYS B 2 58  ? 5.257   53.576  58.090  1.00 30.15  ?  46  LYS B C     1 
ATOM   3007 O  O     . LYS B 2 58  ? 4.295   54.327  57.971  1.00 29.49  ?  46  LYS B O     1 
ATOM   3008 C  CB    . LYS B 2 58  ? 4.424   51.234  57.620  1.00 34.03  ?  46  LYS B CB    1 
ATOM   3009 C  CG    . LYS B 2 58  ? 5.345   50.951  56.439  1.00 38.78  ?  46  LYS B CG    1 
ATOM   3010 C  CD    . LYS B 2 58  ? 4.571   50.423  55.240  1.00 43.72  ?  46  LYS B CD    1 
ATOM   3011 N  N     . GLN B 2 59  ? 6.503   53.950  57.786  1.00 30.23  ?  47  GLN B N     1 
ATOM   3012 C  CA    . GLN B 2 59  ? 6.780   55.263  57.218  1.00 30.10  ?  47  GLN B CA    1 
ATOM   3013 C  C     . GLN B 2 59  ? 6.602   55.179  55.728  1.00 30.72  ?  47  GLN B C     1 
ATOM   3014 O  O     . GLN B 2 59  ? 7.274   54.375  55.089  1.00 32.07  ?  47  GLN B O     1 
ATOM   3015 C  CB    . GLN B 2 59  ? 8.206   55.713  57.533  1.00 31.80  ?  47  GLN B CB    1 
ATOM   3016 C  CG    . GLN B 2 59  ? 8.344   57.235  57.567  1.00 33.76  ?  47  GLN B CG    1 
ATOM   3017 C  CD    . GLN B 2 59  ? 9.650   57.707  58.148  1.00 37.43  ?  47  GLN B CD    1 
ATOM   3018 O  OE1   . GLN B 2 59  ? 10.588  56.928  58.360  1.00 40.72  ?  47  GLN B OE1   1 
ATOM   3019 N  NE2   . GLN B 2 59  ? 9.745   59.000  58.413  1.00 36.37  ?  47  GLN B NE2   1 
ATOM   3020 N  N     . LEU B 2 60  ? 5.700   55.988  55.162  1.00 29.73  ?  48  LEU B N     1 
ATOM   3021 C  CA    . LEU B 2 60  ? 5.480   55.991  53.723  1.00 29.89  ?  48  LEU B CA    1 
ATOM   3022 C  C     . LEU B 2 60  ? 6.423   57.000  53.064  1.00 28.90  ?  48  LEU B C     1 
ATOM   3023 O  O     . LEU B 2 60  ? 7.038   56.687  52.058  1.00 29.36  ?  48  LEU B O     1 
ATOM   3024 C  CB    . LEU B 2 60  ? 4.007   56.296  53.395  1.00 30.27  ?  48  LEU B CB    1 
ATOM   3025 C  CG    . LEU B 2 60  ? 2.953   55.452  54.128  1.00 32.16  ?  48  LEU B CG    1 
ATOM   3026 C  CD1   . LEU B 2 60  ? 1.547   55.822  53.663  1.00 33.04  ?  48  LEU B CD1   1 
ATOM   3027 C  CD2   . LEU B 2 60  ? 3.189   53.953  53.933  1.00 33.13  ?  48  LEU B CD2   1 
ATOM   3028 N  N     . THR B 2 61  ? 6.526   58.210  53.626  1.00 27.84  ?  49  THR B N     1 
ATOM   3029 C  CA    . THR B 2 61  ? 7.426   59.285  53.176  1.00 28.17  ?  49  THR B CA    1 
ATOM   3030 C  C     . THR B 2 61  ? 8.155   59.907  54.421  1.00 27.97  ?  49  THR B C     1 
ATOM   3031 O  O     . THR B 2 61  ? 7.864   59.522  55.554  1.00 27.32  ?  49  THR B O     1 
ATOM   3032 C  CB    . THR B 2 61  ? 6.678   60.340  52.298  1.00 29.70  ?  49  THR B CB    1 
ATOM   3033 O  OG1   . THR B 2 61  ? 5.958   61.256  53.117  1.00 30.70  ?  49  THR B OG1   1 
ATOM   3034 C  CG2   . THR B 2 61  ? 5.745   59.734  51.293  1.00 30.14  ?  49  THR B CG2   1 
ATOM   3035 N  N     . ASN B 2 62  ? 9.084   60.862  54.229  1.00 28.68  ?  50  ASN B N     1 
ATOM   3036 C  CA    . ASN B 2 62  ? 9.808   61.491  55.352  1.00 29.44  ?  50  ASN B CA    1 
ATOM   3037 C  C     . ASN B 2 62  ? 8.883   62.149  56.382  1.00 28.69  ?  50  ASN B C     1 
ATOM   3038 O  O     . ASN B 2 62  ? 9.221   62.239  57.555  1.00 29.17  ?  50  ASN B O     1 
ATOM   3039 C  CB    . ASN B 2 62  ? 10.779  62.545  54.834  1.00 32.03  ?  50  ASN B CB    1 
ATOM   3040 C  CG    . ASN B 2 62  ? 11.878  61.980  53.995  1.00 38.70  ?  50  ASN B CG    1 
ATOM   3041 O  OD1   . ASN B 2 62  ? 12.390  60.889  54.263  1.00 41.66  ?  50  ASN B OD1   1 
ATOM   3042 N  ND2   . ASN B 2 62  ? 12.286  62.716  52.970  1.00 40.43  ?  50  ASN B ND2   1 
ATOM   3043 N  N     . THR B 2 63  ? 7.717   62.603  55.933  1.00 27.34  ?  51  THR B N     1 
ATOM   3044 C  CA    . THR B 2 63  ? 6.747   63.298  56.745  1.00 26.25  ?  51  THR B CA    1 
ATOM   3045 C  C     . THR B 2 63  ? 5.400   62.556  56.839  1.00 24.61  ?  51  THR B C     1 
ATOM   3046 O  O     . THR B 2 63  ? 4.430   63.163  57.286  1.00 24.35  ?  51  THR B O     1 
ATOM   3047 C  CB    . THR B 2 63  ? 6.543   64.693  56.129  1.00 28.50  ?  51  THR B CB    1 
ATOM   3048 O  OG1   . THR B 2 63  ? 6.152   64.567  54.757  1.00 29.79  ?  51  THR B OG1   1 
ATOM   3049 C  CG2   . THR B 2 63  ? 7.801   65.554  56.200  1.00 29.97  ?  51  THR B CG2   1 
ATOM   3050 N  N     . LEU B 2 64  ? 5.318   61.273  56.418  1.00 23.13  ?  52  LEU B N     1 
ATOM   3051 C  CA    . LEU B 2 64  ? 4.040   60.558  56.438  1.00 21.92  ?  52  LEU B CA    1 
ATOM   3052 C  C     . LEU B 2 64  ? 4.136   59.112  56.943  1.00 20.77  ?  52  LEU B C     1 
ATOM   3053 O  O     . LEU B 2 64  ? 5.052   58.396  56.584  1.00 20.83  ?  52  LEU B O     1 
ATOM   3054 C  CB    . LEU B 2 64  ? 3.388   60.624  55.051  1.00 22.36  ?  52  LEU B CB    1 
ATOM   3055 C  CG    . LEU B 2 64  ? 2.006   59.979  54.892  1.00 23.58  ?  52  LEU B CG    1 
ATOM   3056 C  CD1   . LEU B 2 64  ? 0.907   60.856  55.489  1.00 22.90  ?  52  LEU B CD1   1 
ATOM   3057 C  CD2   . LEU B 2 64  ? 1.732   59.644  53.436  1.00 24.50  ?  52  LEU B CD2   1 
ATOM   3058 N  N     . TRP B 2 65  ? 3.185   58.700  57.789  1.00 20.06  ?  53  TRP B N     1 
ATOM   3059 C  CA    . TRP B 2 65  ? 3.111   57.365  58.391  1.00 20.33  ?  53  TRP B CA    1 
ATOM   3060 C  C     . TRP B 2 65  ? 1.706   56.795  58.293  1.00 20.73  ?  53  TRP B C     1 
ATOM   3061 O  O     . TRP B 2 65  ? 0.743   57.538  58.289  1.00 19.99  ?  53  TRP B O     1 
ATOM   3062 C  CB    . TRP B 2 65  ? 3.448   57.426  59.902  1.00 19.38  ?  53  TRP B CB    1 
ATOM   3063 C  CG    . TRP B 2 65  ? 4.861   57.778  60.217  1.00 18.88  ?  53  TRP B CG    1 
ATOM   3064 C  CD1   . TRP B 2 65  ? 5.886   56.913  60.450  1.00 19.96  ?  53  TRP B CD1   1 
ATOM   3065 C  CD2   . TRP B 2 65  ? 5.400   59.095  60.374  1.00 18.29  ?  53  TRP B CD2   1 
ATOM   3066 N  NE1   . TRP B 2 65  ? 7.022   57.609  60.773  1.00 20.44  ?  53  TRP B NE1   1 
ATOM   3067 C  CE2   . TRP B 2 65  ? 6.762   58.953  60.696  1.00 19.49  ?  53  TRP B CE2   1 
ATOM   3068 C  CE3   . TRP B 2 65  ? 4.863   60.383  60.267  1.00 18.36  ?  53  TRP B CE3   1 
ATOM   3069 C  CZ2   . TRP B 2 65  ? 7.600   60.050  60.902  1.00 20.12  ?  53  TRP B CZ2   1 
ATOM   3070 C  CZ3   . TRP B 2 65  ? 5.703   61.469  60.425  1.00 19.57  ?  53  TRP B CZ3   1 
ATOM   3071 C  CH2   . TRP B 2 65  ? 7.056   61.299  60.744  1.00 20.13  ?  53  TRP B CH2   1 
ATOM   3072 N  N     . SER B 2 66  ? 1.589   55.472  58.294  1.00 22.25  ?  54  SER B N     1 
ATOM   3073 C  CA    . SER B 2 66  ? 0.292   54.810  58.325  1.00 23.71  ?  54  SER B CA    1 
ATOM   3074 C  C     . SER B 2 66  ? 0.221   53.891  59.539  1.00 24.80  ?  54  SER B C     1 
ATOM   3075 O  O     . SER B 2 66  ? 1.224   53.314  59.952  1.00 24.97  ?  54  SER B O     1 
ATOM   3076 C  CB    . SER B 2 66  ? 0.006   54.050  57.027  1.00 26.14  ?  54  SER B CB    1 
ATOM   3077 O  OG    . SER B 2 66  ? 0.633   52.779  56.959  1.00 29.70  ?  54  SER B OG    1 
ATOM   3078 N  N     . LEU B 2 67  ? -0.956  53.792  60.136  1.00 25.81  ?  55  LEU B N     1 
ATOM   3079 C  CA    . LEU B 2 67  ? -1.184  52.918  61.268  1.00 27.55  ?  55  LEU B CA    1 
ATOM   3080 C  C     . LEU B 2 67  ? -2.180  51.887  60.808  1.00 30.08  ?  55  LEU B C     1 
ATOM   3081 O  O     . LEU B 2 67  ? -3.289  52.242  60.398  1.00 30.02  ?  55  LEU B O     1 
ATOM   3082 C  CB    . LEU B 2 67  ? -1.780  53.692  62.447  1.00 27.36  ?  55  LEU B CB    1 
ATOM   3083 C  CG    . LEU B 2 67  ? -1.048  54.908  62.992  1.00 28.12  ?  55  LEU B CG    1 
ATOM   3084 C  CD1   . LEU B 2 67  ? -1.636  55.299  64.325  1.00 28.29  ?  55  LEU B CD1   1 
ATOM   3085 C  CD2   . LEU B 2 67  ? 0.442   54.652  63.159  1.00 28.78  ?  55  LEU B CD2   1 
ATOM   3086 N  N     . ALA B 2 68  ? -1.797  50.616  60.850  1.00 32.27  ?  56  ALA B N     1 
ATOM   3087 C  CA    . ALA B 2 68  ? -2.680  49.536  60.405  1.00 35.08  ?  56  ALA B CA    1 
ATOM   3088 C  C     . ALA B 2 68  ? -2.940  48.550  61.533  1.00 38.41  ?  56  ALA B C     1 
ATOM   3089 O  O     . ALA B 2 68  ? -2.112  48.403  62.426  1.00 38.37  ?  56  ALA B O     1 
ATOM   3090 C  CB    . ALA B 2 68  ? -2.055  48.812  59.223  1.00 35.45  ?  56  ALA B CB    1 
ATOM   3091 N  N     . GLY B 2 69  ? -4.070  47.850  61.470  1.00 41.36  ?  57  GLY B N     1 
ATOM   3092 C  CA    . GLY B 2 69  ? -4.422  46.853  62.478  1.00 44.17  ?  57  GLY B CA    1 
ATOM   3093 C  C     . GLY B 2 69  ? -3.448  45.688  62.547  1.00 46.69  ?  57  GLY B C     1 
ATOM   3094 O  O     . GLY B 2 69  ? -2.720  45.413  61.585  1.00 47.77  ?  57  GLY B O     1 
HETATM 3095 C  C1    . GOL C 3 .   ? 18.649  64.470  83.532  1.00 41.58  ?  401 GOL A C1    1 
HETATM 3096 O  O1    . GOL C 3 .   ? 17.271  64.828  83.604  1.00 41.05  ?  401 GOL A O1    1 
HETATM 3097 C  C2    . GOL C 3 .   ? 19.190  64.515  82.121  1.00 42.27  ?  401 GOL A C2    1 
HETATM 3098 O  O2    . GOL C 3 .   ? 19.767  65.809  81.843  1.00 42.21  ?  401 GOL A O2    1 
HETATM 3099 C  C3    . GOL C 3 .   ? 20.246  63.442  81.981  1.00 42.79  ?  401 GOL A C3    1 
HETATM 3100 O  O3    . GOL C 3 .   ? 19.724  62.272  81.348  1.00 42.98  ?  401 GOL A O3    1 
HETATM 3101 P  PG    . ATP D 4 .   ? 13.190  80.561  88.501  1.00 37.72  ?  402 ATP A PG    1 
HETATM 3102 O  O1G   . ATP D 4 .   ? 14.195  80.739  89.669  1.00 37.93  ?  402 ATP A O1G   1 
HETATM 3103 O  O2G   . ATP D 4 .   ? 11.745  80.845  88.960  1.00 38.34  ?  402 ATP A O2G   1 
HETATM 3104 O  O3G   . ATP D 4 .   ? 13.544  81.493  87.273  1.00 37.45  ?  402 ATP A O3G   1 
HETATM 3105 P  PB    . ATP D 4 .   ? 13.959  78.189  86.938  1.00 33.65  ?  402 ATP A PB    1 
HETATM 3106 O  O1B   . ATP D 4 .   ? 15.328  78.106  87.489  1.00 33.35  ?  402 ATP A O1B   1 
HETATM 3107 O  O2B   . ATP D 4 .   ? 13.367  76.784  86.892  1.00 33.83  ?  402 ATP A O2B   1 
HETATM 3108 O  O3B   . ATP D 4 .   ? 13.073  79.072  87.929  1.00 35.77  ?  402 ATP A O3B   1 
HETATM 3109 P  PA    . ATP D 4 .   ? 15.018  78.554  84.229  1.00 29.17  ?  402 ATP A PA    1 
HETATM 3110 O  O1A   . ATP D 4 .   ? 16.402  78.804  84.685  1.00 28.89  ?  402 ATP A O1A   1 
HETATM 3111 O  O2A   . ATP D 4 .   ? 14.662  79.483  83.072  1.00 28.73  ?  402 ATP A O2A   1 
HETATM 3112 O  O3A   . ATP D 4 .   ? 14.007  78.773  85.449  1.00 31.73  ?  402 ATP A O3A   1 
HETATM 3113 O  "O5'" . ATP D 4 .   ? 14.793  77.033  83.737  1.00 27.70  ?  402 ATP A "O5'" 1 
HETATM 3114 C  "C5'" . ATP D 4 .   ? 15.546  76.397  82.687  1.00 26.18  ?  402 ATP A "C5'" 1 
HETATM 3115 C  "C4'" . ATP D 4 .   ? 15.464  74.902  82.873  1.00 25.29  ?  402 ATP A "C4'" 1 
HETATM 3116 O  "O4'" . ATP D 4 .   ? 16.425  74.472  83.866  1.00 24.43  ?  402 ATP A "O4'" 1 
HETATM 3117 C  "C3'" . ATP D 4 .   ? 14.107  74.349  83.319  1.00 25.06  ?  402 ATP A "C3'" 1 
HETATM 3118 O  "O3'" . ATP D 4 .   ? 13.799  73.160  82.601  1.00 25.42  ?  402 ATP A "O3'" 1 
HETATM 3119 C  "C2'" . ATP D 4 .   ? 14.325  74.045  84.803  1.00 24.20  ?  402 ATP A "C2'" 1 
HETATM 3120 O  "O2'" . ATP D 4 .   ? 13.517  72.990  85.303  1.00 24.31  ?  402 ATP A "O2'" 1 
HETATM 3121 C  "C1'" . ATP D 4 .   ? 15.786  73.622  84.797  1.00 23.61  ?  402 ATP A "C1'" 1 
HETATM 3122 N  N9    . ATP D 4 .   ? 16.441  73.768  86.092  1.00 21.84  ?  402 ATP A N9    1 
HETATM 3123 C  C8    . ATP D 4 .   ? 16.209  74.734  87.037  1.00 20.87  ?  402 ATP A C8    1 
HETATM 3124 N  N7    . ATP D 4 .   ? 16.854  74.544  88.163  1.00 20.20  ?  402 ATP A N7    1 
HETATM 3125 C  C5    . ATP D 4 .   ? 17.577  73.381  87.936  1.00 19.40  ?  402 ATP A C5    1 
HETATM 3126 C  C6    . ATP D 4 .   ? 18.481  72.657  88.736  1.00 18.22  ?  402 ATP A C6    1 
HETATM 3127 N  N6    . ATP D 4 .   ? 18.688  72.905  90.036  1.00 17.25  ?  402 ATP A N6    1 
HETATM 3128 N  N1    . ATP D 4 .   ? 19.100  71.595  88.172  1.00 18.37  ?  402 ATP A N1    1 
HETATM 3129 C  C2    . ATP D 4 .   ? 18.795  71.260  86.915  1.00 18.63  ?  402 ATP A C2    1 
HETATM 3130 N  N3    . ATP D 4 .   ? 17.921  71.834  86.084  1.00 19.42  ?  402 ATP A N3    1 
HETATM 3131 C  C4    . ATP D 4 .   ? 17.345  72.901  86.659  1.00 20.20  ?  402 ATP A C4    1 
HETATM 3132 MG MG    . MG  E 5 .   ? 15.374  78.387  89.980  1.00 28.70  2  403 MG  A MG    1 
HETATM 3133 NA NA    . NA  F 6 .   ? 13.986  64.323  82.115  1.00 8.98   1  404 NA  A NA    1 
HETATM 3134 O  O     . HOH G 7 .   ? 30.368  64.773  85.149  1.00 35.55  ?  501 HOH A O     1 
HETATM 3135 O  O     . HOH G 7 .   ? -10.640 71.391  97.929  1.00 41.28  ?  502 HOH A O     1 
HETATM 3136 O  O     . HOH G 7 .   ? 22.764  104.659 86.235  1.00 28.43  ?  503 HOH A O     1 
HETATM 3137 O  O     . HOH G 7 .   ? 15.897  75.433  64.561  1.00 70.04  ?  504 HOH A O     1 
HETATM 3138 O  O     . HOH G 7 .   ? -11.200 53.859  61.069  1.00 52.93  ?  505 HOH A O     1 
HETATM 3139 O  O     . HOH G 7 .   ? 34.042  84.286  94.459  1.00 25.56  ?  506 HOH A O     1 
HETATM 3140 O  O     . HOH G 7 .   ? 31.909  83.080  105.828 1.00 34.10  ?  507 HOH A O     1 
HETATM 3141 O  O     . HOH G 7 .   ? -16.644 63.897  96.199  1.00 19.93  ?  508 HOH A O     1 
HETATM 3142 O  O     . HOH G 7 .   ? -1.401  77.439  92.476  1.00 38.30  ?  509 HOH A O     1 
HETATM 3143 O  O     . HOH G 7 .   ? -10.649 58.930  100.420 1.00 35.06  ?  510 HOH A O     1 
HETATM 3144 O  O     . HOH G 7 .   ? 8.171   72.620  85.999  1.00 16.76  ?  511 HOH A O     1 
HETATM 3145 O  O     . HOH G 7 .   ? 8.768   58.259  92.226  1.00 20.48  ?  512 HOH A O     1 
HETATM 3146 O  O     . HOH G 7 .   ? 31.754  89.357  80.031  1.00 24.10  ?  513 HOH A O     1 
HETATM 3147 O  O     . HOH G 7 .   ? 22.201  58.186  103.699 1.00 26.34  ?  514 HOH A O     1 
HETATM 3148 O  O     . HOH G 7 .   ? 23.495  91.265  97.574  1.00 63.92  ?  515 HOH A O     1 
HETATM 3149 O  O     . HOH G 7 .   ? 11.101  70.753  85.995  1.00 19.36  ?  516 HOH A O     1 
HETATM 3150 O  O     . HOH G 7 .   ? -11.459 63.956  84.341  1.00 18.00  ?  517 HOH A O     1 
HETATM 3151 O  O     . HOH G 7 .   ? 10.130  69.983  54.275  1.00 49.39  ?  518 HOH A O     1 
HETATM 3152 O  O     . HOH G 7 .   ? -8.014  56.535  100.715 1.00 55.01  ?  519 HOH A O     1 
HETATM 3153 O  O     . HOH G 7 .   ? 20.733  50.309  95.488  1.00 65.81  ?  520 HOH A O     1 
HETATM 3154 O  O     . HOH G 7 .   ? 24.473  84.612  93.831  1.00 21.23  ?  521 HOH A O     1 
HETATM 3155 O  O     . HOH G 7 .   ? 27.215  100.267 82.974  1.00 31.65  ?  522 HOH A O     1 
HETATM 3156 O  O     . HOH G 7 .   ? 23.940  81.252  92.289  1.00 16.65  ?  523 HOH A O     1 
HETATM 3157 O  O     . HOH G 7 .   ? -12.112 58.084  54.691  1.00 50.72  ?  524 HOH A O     1 
HETATM 3158 O  O     . HOH G 7 .   ? 34.157  84.887  85.295  1.00 25.37  ?  525 HOH A O     1 
HETATM 3159 O  O     . HOH G 7 .   ? 35.750  70.473  97.002  1.00 23.70  ?  526 HOH A O     1 
HETATM 3160 O  O     . HOH G 7 .   ? -1.276  58.139  76.668  1.00 43.85  ?  527 HOH A O     1 
HETATM 3161 O  O     . HOH G 7 .   ? 13.026  67.431  106.790 1.00 57.31  ?  528 HOH A O     1 
HETATM 3162 O  O     . HOH G 7 .   ? 35.256  82.681  102.170 1.00 56.47  ?  529 HOH A O     1 
HETATM 3163 O  O     . HOH G 7 .   ? 11.183  64.129  82.250  1.00 18.02  ?  530 HOH A O     1 
HETATM 3164 O  O     . HOH G 7 .   ? 32.806  65.255  100.907 1.00 28.83  ?  531 HOH A O     1 
HETATM 3165 O  O     . HOH G 7 .   ? 29.512  99.927  76.769  1.00 21.63  ?  532 HOH A O     1 
HETATM 3166 O  O     . HOH G 7 .   ? 12.239  62.756  71.179  1.00 36.96  ?  533 HOH A O     1 
HETATM 3167 O  O     . HOH G 7 .   ? 8.007   57.487  97.368  1.00 20.14  ?  534 HOH A O     1 
HETATM 3168 O  O     . HOH G 7 .   ? 8.808   55.655  86.297  1.00 52.85  ?  535 HOH A O     1 
HETATM 3169 O  O     . HOH G 7 .   ? -6.783  78.423  91.178  1.00 23.52  ?  536 HOH A O     1 
HETATM 3170 O  O     . HOH G 7 .   ? 7.847   80.406  70.207  1.00 30.00  ?  537 HOH A O     1 
HETATM 3171 O  O     . HOH G 7 .   ? -7.343  77.956  83.180  1.00 14.62  ?  538 HOH A O     1 
HETATM 3172 O  O     . HOH G 7 .   ? 10.991  77.062  74.894  1.00 51.73  ?  539 HOH A O     1 
HETATM 3173 O  O     . HOH G 7 .   ? -8.237  64.521  78.485  1.00 29.75  ?  540 HOH A O     1 
HETATM 3174 O  O     . HOH G 7 .   ? 25.207  61.307  85.614  1.00 45.44  ?  541 HOH A O     1 
HETATM 3175 O  O     . HOH G 7 .   ? 27.321  67.787  100.292 1.00 17.96  ?  542 HOH A O     1 
HETATM 3176 O  O     . HOH G 7 .   ? 9.835   56.393  61.452  1.00 25.77  ?  543 HOH A O     1 
HETATM 3177 O  O     . HOH G 7 .   ? -8.139  68.463  55.978  1.00 48.72  ?  544 HOH A O     1 
HETATM 3178 O  O     . HOH G 7 .   ? -14.276 77.981  84.454  1.00 28.63  ?  545 HOH A O     1 
HETATM 3179 O  O     . HOH G 7 .   ? 28.403  82.451  103.199 1.00 30.75  ?  546 HOH A O     1 
HETATM 3180 O  O     . HOH G 7 .   ? 0.327   71.855  100.361 1.00 20.49  ?  547 HOH A O     1 
HETATM 3181 O  O     . HOH G 7 .   ? 5.559   80.641  83.129  1.00 52.26  ?  548 HOH A O     1 
HETATM 3182 O  O     . HOH G 7 .   ? 27.467  82.441  99.762  1.00 42.91  ?  549 HOH A O     1 
HETATM 3183 O  O     . HOH G 7 .   ? -9.429  77.476  57.350  1.00 64.54  ?  550 HOH A O     1 
HETATM 3184 O  O     . HOH G 7 .   ? 19.515  68.473  81.455  1.00 76.73  ?  551 HOH A O     1 
HETATM 3185 O  O     . HOH G 7 .   ? -4.938  76.798  77.782  1.00 40.60  ?  552 HOH A O     1 
HETATM 3186 O  O     . HOH G 7 .   ? 30.943  70.470  104.709 1.00 37.99  ?  553 HOH A O     1 
HETATM 3187 O  O     . HOH G 7 .   ? 29.364  69.499  101.496 1.00 24.25  ?  554 HOH A O     1 
HETATM 3188 O  O     . HOH G 7 .   ? 17.147  93.475  95.427  1.00 87.86  ?  555 HOH A O     1 
HETATM 3189 O  O     . HOH G 7 .   ? 16.907  55.282  91.478  1.00 31.21  ?  556 HOH A O     1 
HETATM 3190 O  O     . HOH G 7 .   ? 10.074  61.167  85.720  1.00 28.80  ?  557 HOH A O     1 
HETATM 3191 O  O     . HOH G 7 .   ? 4.091   67.539  94.017  1.00 17.24  ?  558 HOH A O     1 
HETATM 3192 O  O     . HOH G 7 .   ? 14.628  82.334  100.716 1.00 63.63  ?  559 HOH A O     1 
HETATM 3193 O  O     . HOH G 7 .   ? 19.470  68.754  108.493 1.00 42.72  ?  560 HOH A O     1 
HETATM 3194 O  O     . HOH G 7 .   ? -2.363  63.007  58.001  1.00 26.90  ?  561 HOH A O     1 
HETATM 3195 O  O     . HOH G 7 .   ? 11.133  59.577  68.300  1.00 42.89  ?  562 HOH A O     1 
HETATM 3196 O  O     . HOH G 7 .   ? 13.183  71.937  63.011  1.00 32.19  ?  563 HOH A O     1 
HETATM 3197 O  O     . HOH G 7 .   ? -16.299 66.516  96.710  1.00 23.84  ?  564 HOH A O     1 
HETATM 3198 O  O     . HOH G 7 .   ? 1.053   57.064  91.993  1.00 30.07  ?  565 HOH A O     1 
HETATM 3199 O  O     . HOH G 7 .   ? 5.712   66.950  104.884 1.00 32.58  ?  566 HOH A O     1 
HETATM 3200 O  O     . HOH G 7 .   ? 16.509  89.226  78.520  1.00 41.63  ?  567 HOH A O     1 
HETATM 3201 O  O     . HOH G 7 .   ? 16.559  69.270  71.337  1.00 33.86  ?  568 HOH A O     1 
HETATM 3202 O  O     . HOH G 7 .   ? 11.015  75.876  85.741  1.00 43.87  ?  569 HOH A O     1 
HETATM 3203 O  O     . HOH G 7 .   ? 19.529  65.557  106.898 1.00 67.99  ?  570 HOH A O     1 
HETATM 3204 O  O     . HOH G 7 .   ? 24.544  103.024 89.354  1.00 38.40  ?  571 HOH A O     1 
HETATM 3205 O  O     . HOH G 7 .   ? -0.281  75.652  90.079  1.00 14.76  ?  572 HOH A O     1 
HETATM 3206 O  O     . HOH G 7 .   ? -3.455  56.757  95.789  1.00 40.50  ?  573 HOH A O     1 
HETATM 3207 O  O     . HOH G 7 .   ? -2.259  56.231  92.430  1.00 35.22  ?  574 HOH A O     1 
HETATM 3208 O  O     . HOH G 7 .   ? -12.127 59.807  91.617  1.00 42.45  ?  575 HOH A O     1 
HETATM 3209 O  O     . HOH G 7 .   ? 42.961  84.053  92.150  1.00 45.58  ?  576 HOH A O     1 
HETATM 3210 O  O     . HOH G 7 .   ? -10.918 71.222  76.914  1.00 30.55  ?  577 HOH A O     1 
HETATM 3211 O  O     . HOH G 7 .   ? 25.303  83.739  77.178  1.00 32.98  ?  578 HOH A O     1 
HETATM 3212 O  O     . HOH G 7 .   ? 12.823  81.292  65.372  1.00 60.04  ?  579 HOH A O     1 
HETATM 3213 O  O     . HOH G 7 .   ? 15.029  70.636  82.916  1.00 30.70  ?  580 HOH A O     1 
HETATM 3214 O  O     . HOH G 7 .   ? 34.660  76.220  103.238 1.00 20.84  ?  581 HOH A O     1 
HETATM 3215 O  O     . HOH G 7 .   ? 9.716   52.147  95.411  1.00 36.92  ?  582 HOH A O     1 
HETATM 3216 O  O     . HOH G 7 .   ? 7.180   56.717  90.757  1.00 50.25  ?  583 HOH A O     1 
HETATM 3217 O  O     . HOH G 7 .   ? 21.039  76.503  80.270  1.00 36.73  ?  584 HOH A O     1 
HETATM 3218 O  O     . HOH G 7 .   ? -10.376 63.999  68.400  1.00 26.85  ?  585 HOH A O     1 
HETATM 3219 O  O     . HOH G 7 .   ? -0.183  66.436  99.859  1.00 18.01  ?  586 HOH A O     1 
HETATM 3220 O  O     . HOH G 7 .   ? 9.276   55.058  99.788  1.00 37.87  ?  587 HOH A O     1 
HETATM 3221 O  O     . HOH G 7 .   ? 15.220  65.610  68.485  1.00 44.98  ?  588 HOH A O     1 
HETATM 3222 O  O     . HOH G 7 .   ? 17.187  77.109  96.723  1.00 24.86  ?  589 HOH A O     1 
HETATM 3223 O  O     . HOH G 7 .   ? 15.928  79.191  80.217  1.00 57.06  ?  590 HOH A O     1 
HETATM 3224 O  O     . HOH G 7 .   ? 26.892  83.145  93.769  1.00 23.59  ?  591 HOH A O     1 
HETATM 3225 O  O     . HOH G 7 .   ? -1.685  82.517  84.159  1.00 57.50  ?  592 HOH A O     1 
HETATM 3226 O  O     . HOH G 7 .   ? 27.617  69.126  104.057 1.00 27.02  ?  593 HOH A O     1 
HETATM 3227 O  O     . HOH G 7 .   ? 16.336  67.307  84.615  1.00 21.60  ?  594 HOH A O     1 
HETATM 3228 O  O     . HOH G 7 .   ? 11.253  76.532  94.926  1.00 45.82  ?  595 HOH A O     1 
HETATM 3229 O  O     . HOH G 7 .   ? 27.394  86.204  95.826  1.00 49.85  ?  596 HOH A O     1 
HETATM 3230 O  O     . HOH G 7 .   ? -18.567 66.820  81.764  1.00 48.95  ?  597 HOH A O     1 
HETATM 3231 O  O     . HOH G 7 .   ? 16.524  62.954  105.708 1.00 43.22  ?  598 HOH A O     1 
HETATM 3232 O  O     . HOH G 7 .   ? 3.238   84.934  72.907  1.00 46.13  ?  599 HOH A O     1 
HETATM 3233 O  O     . HOH G 7 .   ? 17.079  83.914  100.317 1.00 58.69  ?  600 HOH A O     1 
HETATM 3234 O  O     . HOH G 7 .   ? 17.387  65.565  74.057  1.00 36.92  ?  601 HOH A O     1 
HETATM 3235 O  O     . HOH G 7 .   ? 29.933  67.531  85.373  1.00 48.02  ?  602 HOH A O     1 
HETATM 3236 O  O     . HOH G 7 .   ? 26.982  71.795  104.626 1.00 20.36  ?  603 HOH A O     1 
HETATM 3237 O  O     . HOH G 7 .   ? 17.981  79.432  82.394  1.00 23.76  ?  604 HOH A O     1 
HETATM 3238 O  O     . HOH G 7 .   ? 30.319  56.767  93.950  1.00 25.30  ?  605 HOH A O     1 
HETATM 3239 O  O     . HOH G 7 .   ? -3.689  79.512  75.930  1.00 44.01  ?  606 HOH A O     1 
HETATM 3240 O  O     . HOH G 7 .   ? 18.074  70.562  83.529  1.00 43.46  ?  607 HOH A O     1 
HETATM 3241 O  O     . HOH G 7 .   ? 33.663  87.720  80.949  1.00 40.11  ?  608 HOH A O     1 
HETATM 3242 O  O     . HOH G 7 .   ? 30.958  62.343  107.462 1.00 58.76  ?  609 HOH A O     1 
HETATM 3243 O  O     . HOH G 7 .   ? 28.235  66.211  83.395  1.00 65.56  ?  610 HOH A O     1 
HETATM 3244 O  O     . HOH G 7 .   ? 11.540  72.179  88.154  1.00 28.33  ?  611 HOH A O     1 
HETATM 3245 O  O     . HOH G 7 .   ? 36.106  70.421  99.622  1.00 8.87   ?  612 HOH A O     1 
HETATM 3246 O  O     . HOH G 7 .   ? 30.446  63.359  96.954  1.00 18.73  ?  613 HOH A O     1 
HETATM 3247 O  O     . HOH G 7 .   ? -1.771  61.815  79.281  1.00 22.86  ?  614 HOH A O     1 
HETATM 3248 O  O     . HOH G 7 .   ? 33.946  78.889  86.222  1.00 10.47  ?  615 HOH A O     1 
HETATM 3249 O  O     . HOH G 7 .   ? 16.689  73.169  61.173  1.00 73.03  ?  616 HOH A O     1 
HETATM 3250 O  O     . HOH G 7 .   ? 27.303  54.218  86.201  1.00 53.71  ?  617 HOH A O     1 
HETATM 3251 O  O     . HOH G 7 .   ? 0.758   61.137  78.592  1.00 32.46  ?  618 HOH A O     1 
HETATM 3252 O  O     . HOH G 7 .   ? -10.098 62.780  55.170  1.00 78.64  ?  619 HOH A O     1 
HETATM 3253 O  O     . HOH G 7 .   ? 32.366  63.401  104.313 1.00 35.94  ?  620 HOH A O     1 
HETATM 3254 O  O     . HOH G 7 .   ? -3.567  70.018  101.077 1.00 28.19  ?  621 HOH A O     1 
HETATM 3255 O  O     . HOH G 7 .   ? 21.312  95.215  95.800  1.00 55.83  ?  622 HOH A O     1 
HETATM 3256 O  O     . HOH G 7 .   ? 26.630  90.370  98.651  1.00 62.11  ?  623 HOH A O     1 
HETATM 3257 O  O     . HOH G 7 .   ? 29.083  67.494  80.483  1.00 52.45  ?  624 HOH A O     1 
HETATM 3258 O  O     . HOH G 7 .   ? 22.658  60.854  85.196  1.00 24.02  ?  625 HOH A O     1 
HETATM 3259 O  O     . HOH G 7 .   ? 24.018  77.732  79.458  1.00 64.29  ?  626 HOH A O     1 
HETATM 3260 O  O     . HOH G 7 .   ? 21.517  93.515  92.999  1.00 41.16  ?  627 HOH A O     1 
HETATM 3261 O  O     . HOH G 7 .   ? 4.251   80.478  78.929  1.00 36.97  ?  628 HOH A O     1 
HETATM 3262 O  O     . HOH G 7 .   ? 0.088   67.528  58.779  1.00 24.27  ?  629 HOH A O     1 
HETATM 3263 O  O     . HOH G 7 .   ? 13.052  74.387  88.494  1.00 41.63  ?  630 HOH A O     1 
HETATM 3264 O  O     . HOH G 7 .   ? 24.194  58.534  89.624  1.00 38.81  ?  631 HOH A O     1 
HETATM 3265 O  O     . HOH G 7 .   ? -9.948  59.610  54.384  1.00 72.88  ?  632 HOH A O     1 
HETATM 3266 O  O     . HOH G 7 .   ? -9.893  47.010  59.130  1.00 53.38  ?  633 HOH A O     1 
HETATM 3267 O  O     . HOH G 7 .   ? -11.857 66.386  78.153  1.00 34.50  ?  634 HOH A O     1 
HETATM 3268 O  O     . HOH G 7 .   ? 36.446  66.443  108.047 1.00 48.75  ?  635 HOH A O     1 
HETATM 3269 O  O     . HOH G 7 .   ? 27.611  68.882  108.194 1.00 86.55  ?  636 HOH A O     1 
HETATM 3270 O  O     . HOH G 7 .   ? 21.325  81.355  100.688 1.00 28.76  ?  637 HOH A O     1 
HETATM 3271 O  O     . HOH G 7 .   ? 22.795  78.415  96.709  1.00 23.46  ?  638 HOH A O     1 
HETATM 3272 O  O     . HOH G 7 .   ? 15.538  57.543  89.050  1.00 30.35  ?  639 HOH A O     1 
HETATM 3273 O  O     . HOH G 7 .   ? 10.455  75.602  78.076  1.00 27.86  ?  640 HOH A O     1 
HETATM 3274 O  O     . HOH G 7 .   ? 44.105  80.009  98.145  1.00 47.88  ?  641 HOH A O     1 
HETATM 3275 O  O     . HOH G 7 .   ? 17.601  82.506  94.762  1.00 26.78  ?  642 HOH A O     1 
HETATM 3276 O  O     . HOH G 7 .   ? 18.346  53.537  98.027  1.00 40.31  ?  643 HOH A O     1 
HETATM 3277 O  O     . HOH G 7 .   ? 21.592  60.511  82.796  1.00 37.26  ?  644 HOH A O     1 
HETATM 3278 O  O     . HOH G 7 .   ? 23.442  56.479  102.027 1.00 54.73  ?  645 HOH A O     1 
HETATM 3279 O  O     . HOH G 7 .   ? -11.269 58.333  97.812  1.00 30.56  ?  646 HOH A O     1 
HETATM 3280 O  O     . HOH G 7 .   ? 19.377  82.757  75.316  1.00 61.66  ?  647 HOH A O     1 
HETATM 3281 O  O     . HOH G 7 .   ? -2.702  76.920  96.076  1.00 22.59  ?  648 HOH A O     1 
HETATM 3282 O  O     . HOH G 7 .   ? 35.334  74.782  105.441 1.00 38.98  ?  649 HOH A O     1 
HETATM 3283 O  O     . HOH G 7 .   ? 37.425  85.596  95.208  1.00 51.10  ?  650 HOH A O     1 
HETATM 3284 O  O     . HOH G 7 .   ? 22.088  68.097  82.375  1.00 19.06  ?  651 HOH A O     1 
HETATM 3285 O  O     . HOH G 7 .   ? 14.528  58.396  52.986  1.00 75.74  ?  652 HOH A O     1 
HETATM 3286 O  O     . HOH G 7 .   ? 38.229  84.730  98.838  1.00 53.23  ?  653 HOH A O     1 
HETATM 3287 O  O     . HOH G 7 .   ? 23.293  82.607  78.034  1.00 18.00  ?  654 HOH A O     1 
HETATM 3288 O  O     . HOH G 7 .   ? -15.876 69.752  84.003  1.00 23.10  ?  655 HOH A O     1 
HETATM 3289 O  O     . HOH G 7 .   ? 6.824   68.191  92.309  1.00 35.51  ?  656 HOH A O     1 
HETATM 3290 O  O     . HOH G 7 .   ? 23.609  92.017  93.806  1.00 40.83  ?  657 HOH A O     1 
HETATM 3291 O  O     . HOH G 7 .   ? -14.670 68.323  95.712  1.00 24.58  ?  658 HOH A O     1 
HETATM 3292 O  O     . HOH G 7 .   ? 40.143  76.666  98.489  1.00 26.91  ?  659 HOH A O     1 
HETATM 3293 O  O     . HOH G 7 .   ? 9.985   78.004  65.978  1.00 42.87  ?  660 HOH A O     1 
HETATM 3294 O  O     . HOH G 7 .   ? 22.737  56.044  91.268  1.00 35.62  ?  661 HOH A O     1 
HETATM 3295 O  O     . HOH G 7 .   ? 11.598  70.050  66.440  1.00 33.44  ?  662 HOH A O     1 
HETATM 3296 O  O     . HOH G 7 .   ? -5.400  82.846  89.263  1.00 38.82  ?  663 HOH A O     1 
HETATM 3297 O  O     . HOH G 7 .   ? 17.228  61.808  65.024  1.00 38.17  ?  664 HOH A O     1 
HETATM 3298 O  O     . HOH G 7 .   ? 12.608  81.983  84.388  1.00 57.15  ?  665 HOH A O     1 
HETATM 3299 O  O     . HOH G 7 .   ? 21.026  84.073  77.004  1.00 22.70  ?  666 HOH A O     1 
HETATM 3300 O  O     . HOH G 7 .   ? 14.361  77.196  96.483  1.00 44.17  ?  667 HOH A O     1 
HETATM 3301 O  O     . HOH G 7 .   ? 7.169   56.056  102.035 1.00 55.35  ?  668 HOH A O     1 
HETATM 3302 O  O     . HOH G 7 .   ? 13.311  97.559  84.618  1.00 46.93  ?  669 HOH A O     1 
HETATM 3303 O  O     . HOH G 7 .   ? -12.286 59.666  82.596  1.00 55.96  ?  670 HOH A O     1 
HETATM 3304 O  O     . HOH G 7 .   ? -14.520 58.675  86.231  1.00 43.41  ?  671 HOH A O     1 
HETATM 3305 O  O     . HOH G 7 .   ? 5.471   57.819  74.557  1.00 25.51  ?  672 HOH A O     1 
HETATM 3306 O  O     . HOH G 7 .   ? 27.872  73.092  80.755  1.00 63.67  ?  673 HOH A O     1 
HETATM 3307 O  O     . HOH G 7 .   ? 19.752  102.607 85.446  1.00 58.55  ?  674 HOH A O     1 
HETATM 3308 O  O     . HOH G 7 .   ? -11.405 64.517  79.831  1.00 27.53  ?  675 HOH A O     1 
HETATM 3309 O  O     . HOH G 7 .   ? 17.334  70.029  66.405  1.00 51.94  ?  676 HOH A O     1 
HETATM 3310 O  O     . HOH G 7 .   ? 15.981  63.660  70.013  1.00 45.71  ?  677 HOH A O     1 
HETATM 3311 O  O     . HOH G 7 .   ? -5.921  56.068  93.382  1.00 36.06  ?  678 HOH A O     1 
HETATM 3312 O  O     . HOH G 7 .   ? 28.852  98.768  87.601  1.00 35.54  ?  679 HOH A O     1 
HETATM 3313 O  O     . HOH G 7 .   ? 24.255  74.654  80.857  1.00 31.77  ?  680 HOH A O     1 
HETATM 3314 O  O     . HOH G 7 .   ? 14.450  104.079 83.267  1.00 40.31  ?  681 HOH A O     1 
HETATM 3315 O  O     . HOH G 7 .   ? -5.303  76.596  93.936  1.00 38.68  ?  682 HOH A O     1 
HETATM 3316 O  O     . HOH G 7 .   ? 13.236  68.505  67.616  1.00 36.81  ?  683 HOH A O     1 
HETATM 3317 O  O     . HOH G 7 .   ? 25.561  70.485  106.520 1.00 32.68  ?  684 HOH A O     1 
HETATM 3318 O  O     . HOH G 7 .   ? 15.790  77.266  55.919  1.00 44.54  ?  685 HOH A O     1 
HETATM 3319 O  O     . HOH G 7 .   ? 31.449  61.976  89.556  1.00 27.32  ?  686 HOH A O     1 
HETATM 3320 O  O     . HOH G 7 .   ? 21.943  49.112  85.744  1.00 57.18  ?  687 HOH A O     1 
HETATM 3321 O  O     . HOH G 7 .   ? -8.183  53.572  89.676  1.00 40.06  ?  688 HOH A O     1 
HETATM 3322 O  O     . HOH G 7 .   ? 5.873   57.578  103.734 1.00 49.06  ?  689 HOH A O     1 
HETATM 3323 O  O     . HOH G 7 .   ? 13.921  57.344  60.339  1.00 40.14  ?  690 HOH A O     1 
HETATM 3324 O  O     . HOH G 7 .   ? 40.215  85.125  104.314 1.00 55.98  ?  691 HOH A O     1 
HETATM 3325 O  O     . HOH G 7 .   ? 16.831  60.788  81.537  1.00 28.22  ?  692 HOH A O     1 
HETATM 3326 O  O     . HOH G 7 .   ? 0.330   56.775  100.416 1.00 28.42  ?  693 HOH A O     1 
HETATM 3327 O  O     . HOH G 7 .   ? 11.575  91.054  81.957  1.00 53.82  ?  694 HOH A O     1 
HETATM 3328 O  O     . HOH G 7 .   ? 14.014  69.491  63.962  1.00 48.75  ?  695 HOH A O     1 
HETATM 3329 O  O     . HOH G 7 .   ? -15.591 58.647  90.143  1.00 48.91  ?  696 HOH A O     1 
HETATM 3330 O  O     . HOH G 7 .   ? 5.715   80.023  76.562  1.00 49.10  ?  697 HOH A O     1 
HETATM 3331 O  O     . HOH G 7 .   ? 20.777  80.507  75.006  1.00 66.70  ?  698 HOH A O     1 
HETATM 3332 O  O     . HOH G 7 .   ? 4.551   78.227  94.500  1.00 16.19  ?  699 HOH A O     1 
HETATM 3333 O  O     . HOH G 7 .   ? 15.944  65.682  108.637 1.00 46.19  ?  700 HOH A O     1 
HETATM 3334 O  O     . HOH G 7 .   ? -9.502  61.273  73.968  1.00 45.57  ?  701 HOH A O     1 
HETATM 3335 O  O     . HOH G 7 .   ? 7.974   67.560  105.682 1.00 39.71  ?  702 HOH A O     1 
HETATM 3336 O  O     . HOH G 7 .   ? 12.157  79.081  59.075  1.00 38.45  ?  703 HOH A O     1 
HETATM 3337 O  O     . HOH G 7 .   ? -7.657  78.023  93.644  1.00 19.77  ?  704 HOH A O     1 
HETATM 3338 O  O     . HOH G 7 .   ? -14.332 72.795  78.367  1.00 34.94  ?  705 HOH A O     1 
HETATM 3339 O  O     . HOH G 7 .   ? 21.914  68.739  70.188  1.00 41.56  ?  706 HOH A O     1 
HETATM 3340 O  O     . HOH G 7 .   ? 21.029  106.021 84.322  1.00 23.43  ?  707 HOH A O     1 
HETATM 3341 O  O     . HOH G 7 .   ? 7.335   76.449  92.415  1.00 46.49  ?  708 HOH A O     1 
HETATM 3342 O  O     . HOH G 7 .   ? 12.948  76.933  80.293  1.00 66.69  ?  709 HOH A O     1 
HETATM 3343 O  O     . HOH G 7 .   ? 38.988  62.024  107.369 1.00 46.67  ?  710 HOH A O     1 
HETATM 3344 O  O     . HOH G 7 .   ? 25.303  105.293 78.122  1.00 33.82  ?  711 HOH A O     1 
HETATM 3345 O  O     . HOH G 7 .   ? 1.961   75.884  100.716 1.00 57.58  ?  712 HOH A O     1 
HETATM 3346 O  O     . HOH G 7 .   ? -13.143 81.674  86.041  1.00 33.90  ?  713 HOH A O     1 
HETATM 3347 O  O     . HOH G 7 .   ? 11.228  79.026  91.758  1.00 59.97  ?  714 HOH A O     1 
HETATM 3348 O  O     . HOH G 7 .   ? 36.200  62.010  111.104 1.00 47.33  ?  715 HOH A O     1 
HETATM 3349 O  O     . HOH G 7 .   ? 28.226  69.730  77.653  1.00 37.80  ?  716 HOH A O     1 
HETATM 3350 O  O     . HOH G 7 .   ? 11.102  57.933  104.652 1.00 59.59  ?  717 HOH A O     1 
HETATM 3351 O  O     . HOH G 7 .   ? 12.634  84.495  81.183  1.00 46.76  ?  718 HOH A O     1 
HETATM 3352 O  O     . HOH G 7 .   ? 8.851   73.492  54.672  1.00 56.95  ?  719 HOH A O     1 
HETATM 3353 O  O     . HOH G 7 .   ? 23.647  69.780  79.833  1.00 60.38  ?  720 HOH A O     1 
HETATM 3354 O  O     . HOH G 7 .   ? 5.348   70.850  53.926  1.00 49.78  ?  721 HOH A O     1 
HETATM 3355 O  O     . HOH G 7 .   ? 30.293  101.928 78.871  1.00 55.91  ?  722 HOH A O     1 
HETATM 3356 O  O     . HOH G 7 .   ? 0.491   78.492  90.238  1.00 42.21  ?  723 HOH A O     1 
HETATM 3357 O  O     . HOH G 7 .   ? 43.664  81.430  91.335  1.00 28.70  ?  724 HOH A O     1 
HETATM 3358 O  O     . HOH G 7 .   ? 29.437  66.862  108.863 1.00 48.56  ?  725 HOH A O     1 
HETATM 3359 O  O     . HOH G 7 .   ? 27.920  105.278 86.776  1.00 45.45  ?  726 HOH A O     1 
HETATM 3360 O  O     . HOH G 7 .   ? 45.391  80.483  94.087  1.00 75.67  ?  727 HOH A O     1 
HETATM 3361 O  O     . HOH G 7 .   ? -11.275 69.228  100.812 1.00 15.63  ?  728 HOH A O     1 
HETATM 3362 O  O     . HOH G 7 .   ? 6.069   55.155  74.470  1.00 44.94  ?  729 HOH A O     1 
HETATM 3363 O  O     . HOH G 7 .   ? 14.736  81.613  97.856  1.00 40.11  ?  730 HOH A O     1 
HETATM 3364 O  O     . HOH G 7 .   ? 47.498  84.070  99.841  1.00 58.77  ?  731 HOH A O     1 
HETATM 3365 O  O     . HOH G 7 .   ? 33.071  66.912  84.482  1.00 19.97  ?  732 HOH A O     1 
HETATM 3366 O  O     . HOH G 7 .   ? 30.447  59.497  89.987  1.00 39.49  ?  733 HOH A O     1 
HETATM 3367 O  O     . HOH G 7 .   ? -8.959  81.256  82.121  1.00 37.99  ?  734 HOH A O     1 
HETATM 3368 O  O     . HOH G 7 .   ? 19.622  75.988  107.419 1.00 31.07  ?  735 HOH A O     1 
HETATM 3369 O  O     . HOH G 7 .   ? 1.026   56.165  78.936  1.00 73.91  ?  736 HOH A O     1 
HETATM 3370 O  O     . HOH G 7 .   ? -0.673  75.639  100.518 1.00 46.71  ?  737 HOH A O     1 
HETATM 3371 O  O     . HOH G 7 .   ? 13.322  60.622  85.123  1.00 32.04  ?  738 HOH A O     1 
HETATM 3372 O  O     . HOH G 7 .   ? -6.709  74.488  73.639  1.00 36.68  ?  739 HOH A O     1 
HETATM 3373 O  O     . HOH G 7 .   ? 13.650  97.469  81.868  1.00 43.81  ?  740 HOH A O     1 
HETATM 3374 O  O     . HOH G 7 .   ? 14.465  58.954  67.399  1.00 42.89  ?  741 HOH A O     1 
HETATM 3375 O  O     . HOH G 7 .   ? 28.719  55.916  84.546  1.00 59.28  ?  742 HOH A O     1 
HETATM 3376 O  O     . HOH G 7 .   ? 13.744  57.979  85.554  1.00 40.34  ?  743 HOH A O     1 
HETATM 3377 O  O     . HOH G 7 .   ? 6.400   75.586  89.977  1.00 42.14  ?  744 HOH A O     1 
HETATM 3378 O  O     . HOH G 7 .   ? 11.191  77.263  83.035  1.00 45.90  ?  745 HOH A O     1 
HETATM 3379 O  O     . HOH G 7 .   ? 20.670  70.876  80.261  1.00 55.94  ?  746 HOH A O     1 
HETATM 3380 O  O     . HOH G 7 .   ? 17.845  86.563  95.608  1.00 41.06  ?  747 HOH A O     1 
HETATM 3381 O  O     . HOH G 7 .   ? 17.084  84.464  74.429  1.00 54.28  ?  748 HOH A O     1 
HETATM 3382 O  O     . HOH G 7 .   ? 9.868   79.791  68.055  1.00 54.76  ?  749 HOH A O     1 
HETATM 3383 O  O     . HOH G 7 .   ? 46.086  81.699  99.651  1.00 60.73  ?  750 HOH A O     1 
HETATM 3384 O  O     . HOH G 7 .   ? -13.339 58.857  101.891 1.00 36.03  ?  751 HOH A O     1 
HETATM 3385 O  O     . HOH G 7 .   ? 11.925  52.954  87.520  1.00 52.60  ?  752 HOH A O     1 
HETATM 3386 O  O     . HOH G 7 .   ? -11.106 75.670  79.933  1.00 45.22  ?  753 HOH A O     1 
HETATM 3387 O  O     . HOH G 7 .   ? 15.251  61.834  83.703  1.00 38.94  ?  754 HOH A O     1 
HETATM 3388 O  O     . HOH G 7 .   ? -11.677 77.110  58.681  1.00 45.49  ?  755 HOH A O     1 
HETATM 3389 O  O     . HOH G 7 .   ? -2.201  83.807  78.102  1.00 50.19  ?  756 HOH A O     1 
HETATM 3390 O  O     . HOH G 7 .   ? -14.888 61.735  91.330  1.00 39.72  ?  757 HOH A O     1 
HETATM 3391 O  O     . HOH G 7 .   ? 18.004  72.866  81.006  1.00 40.86  ?  758 HOH A O     1 
HETATM 3392 O  O     . HOH G 7 .   ? -14.772 70.304  77.612  1.00 52.72  ?  759 HOH A O     1 
HETATM 3393 O  O     . HOH G 7 .   ? 33.206  81.093  77.891  1.00 49.25  ?  760 HOH A O     1 
HETATM 3394 O  O     . HOH G 7 .   ? 25.861  66.963  110.017 1.00 65.74  ?  761 HOH A O     1 
HETATM 3395 O  O     . HOH G 7 .   ? -16.350 70.079  81.416  1.00 29.41  ?  762 HOH A O     1 
HETATM 3396 O  O     . HOH G 7 .   ? 14.708  104.151 92.004  1.00 32.67  ?  763 HOH A O     1 
HETATM 3397 O  O     . HOH G 7 .   ? -6.809  53.541  86.344  1.00 40.28  ?  764 HOH A O     1 
HETATM 3398 O  O     . HOH G 7 .   ? 13.743  78.116  92.970  1.00 66.45  ?  765 HOH A O     1 
HETATM 3399 O  O     . HOH G 7 .   ? -5.326  67.738  53.941  1.00 58.23  ?  766 HOH A O     1 
HETATM 3400 O  O     . HOH G 7 .   ? 15.100  58.399  77.792  1.00 56.22  ?  767 HOH A O     1 
HETATM 3401 O  O     . HOH G 7 .   ? 34.176  79.429  82.446  1.00 37.27  ?  768 HOH A O     1 
HETATM 3402 O  O     . HOH G 7 .   ? 33.667  73.246  84.567  1.00 28.64  ?  769 HOH A O     1 
HETATM 3403 O  O     . HOH G 7 .   ? 27.946  98.586  85.012  1.00 33.21  ?  770 HOH A O     1 
HETATM 3404 O  O     . HOH G 7 .   ? -0.691  55.396  97.345  1.00 36.04  ?  771 HOH A O     1 
HETATM 3405 O  O     . HOH G 7 .   ? -1.280  56.572  102.887 1.00 43.02  ?  772 HOH A O     1 
HETATM 3406 O  O     . HOH G 7 .   ? 23.234  79.827  76.977  1.00 39.50  ?  773 HOH A O     1 
HETATM 3407 O  O     . HOH G 7 .   ? -2.069  76.593  98.658  1.00 28.52  ?  774 HOH A O     1 
HETATM 3408 O  O     . HOH G 7 .   ? 4.906   54.935  84.518  1.00 46.94  ?  775 HOH A O     1 
HETATM 3409 O  O     . HOH G 7 .   ? 16.273  71.931  52.056  1.00 47.38  ?  776 HOH A O     1 
HETATM 3410 O  O     . HOH G 7 .   ? 10.917  54.823  107.582 1.00 63.11  ?  777 HOH A O     1 
HETATM 3411 O  O     . HOH G 7 .   ? -11.019 78.195  80.394  1.00 40.65  ?  778 HOH A O     1 
HETATM 3412 O  O     . HOH G 7 .   ? 38.034  67.293  105.382 1.00 61.55  ?  779 HOH A O     1 
HETATM 3413 O  O     . HOH G 7 .   ? 10.002  76.500  92.039  1.00 60.54  ?  780 HOH A O     1 
HETATM 3414 O  O     . HOH G 7 .   ? -6.554  78.639  96.012  1.00 35.16  ?  781 HOH A O     1 
HETATM 3415 O  O     . HOH G 7 .   ? -7.838  84.387  88.479  1.00 46.05  ?  782 HOH A O     1 
HETATM 3416 O  O     . HOH G 7 .   ? 12.471  58.398  65.908  1.00 51.84  ?  783 HOH A O     1 
HETATM 3417 O  O     . HOH G 7 .   ? 36.362  85.480  86.636  1.00 40.54  ?  784 HOH A O     1 
HETATM 3418 O  O     . HOH G 7 .   ? 17.991  67.208  72.135  1.00 37.68  ?  785 HOH A O     1 
HETATM 3419 O  O     . HOH G 7 .   ? -13.261 52.048  60.715  1.00 46.99  ?  786 HOH A O     1 
HETATM 3420 O  O     . HOH G 7 .   ? 23.276  93.782  97.070  1.00 33.39  ?  787 HOH A O     1 
HETATM 3421 O  O     . HOH G 7 .   ? 5.238   55.456  91.594  1.00 43.73  ?  788 HOH A O     1 
HETATM 3422 O  O     . HOH G 7 .   ? 21.013  102.606 88.534  1.00 30.45  ?  789 HOH A O     1 
HETATM 3423 O  O     . HOH G 7 .   ? 30.763  89.196  77.086  1.00 45.84  ?  790 HOH A O     1 
HETATM 3424 O  O     . HOH G 7 .   ? 21.837  73.321  80.017  1.00 59.05  ?  791 HOH A O     1 
HETATM 3425 O  O     . HOH G 7 .   ? 18.512  77.142  81.066  1.00 47.70  ?  792 HOH A O     1 
HETATM 3426 O  O     . HOH G 7 .   ? -8.078  70.405  102.854 1.00 52.67  ?  793 HOH A O     1 
HETATM 3427 O  O     . HOH G 7 .   ? 18.987  50.331  97.370  1.00 57.55  ?  794 HOH A O     1 
HETATM 3428 O  O     . HOH G 7 .   ? 0.087   73.063  102.639 1.00 22.90  ?  795 HOH A O     1 
HETATM 3429 O  O     . HOH G 7 .   ? -6.238  53.400  93.043  1.00 44.97  ?  796 HOH A O     1 
HETATM 3430 O  O     . HOH G 7 .   ? -12.012 75.525  77.354  1.00 52.34  ?  797 HOH A O     1 
HETATM 3431 O  O     . HOH G 7 .   ? 35.366  75.359  83.802  1.00 29.13  ?  798 HOH A O     1 
HETATM 3432 O  O     . HOH G 7 .   ? -13.436 62.326  83.563  1.00 35.78  ?  799 HOH A O     1 
HETATM 3433 O  O     . HOH G 7 .   ? 13.709  49.591  89.184  1.00 55.87  ?  800 HOH A O     1 
HETATM 3434 O  O     . HOH G 7 .   ? 21.846  81.931  103.203 1.00 35.02  ?  801 HOH A O     1 
HETATM 3435 O  O     . HOH G 7 .   ? 19.601  66.947  64.101  1.00 51.03  ?  802 HOH A O     1 
HETATM 3436 O  O     . HOH G 7 .   ? -0.835  69.236  101.029 1.00 24.75  ?  803 HOH A O     1 
HETATM 3437 O  O     . HOH G 7 .   ? -14.788 74.633  80.559  1.00 51.57  ?  804 HOH A O     1 
HETATM 3438 O  O     . HOH G 7 .   ? -12.717 60.515  78.955  1.00 57.88  ?  805 HOH A O     1 
HETATM 3439 O  O     . HOH G 7 .   ? 3.896   77.528  88.574  1.00 37.72  ?  806 HOH A O     1 
HETATM 3440 O  O     . HOH G 7 .   ? 15.399  68.179  68.947  1.00 30.41  ?  807 HOH A O     1 
HETATM 3441 O  O     . HOH G 7 .   ? 15.455  75.365  79.033  1.00 38.85  ?  808 HOH A O     1 
HETATM 3442 O  O     . HOH G 7 .   ? 23.982  72.390  78.281  1.00 50.95  ?  809 HOH A O     1 
HETATM 3443 O  O     . HOH G 7 .   ? -7.627  45.485  58.723  1.00 44.37  ?  810 HOH A O     1 
HETATM 3444 O  O     . HOH G 7 .   ? 35.757  81.635  81.258  1.00 59.58  ?  811 HOH A O     1 
HETATM 3445 O  O     . HOH G 7 .   ? 17.832  59.398  78.154  1.00 53.83  ?  812 HOH A O     1 
HETATM 3446 O  O     . HOH G 7 .   ? 48.537  80.608  99.325  1.00 40.69  ?  813 HOH A O     1 
HETATM 3447 O  O     . HOH G 7 .   ? 8.648   73.084  88.589  1.00 24.79  ?  814 HOH A O     1 
HETATM 3448 O  O     . HOH G 7 .   ? 18.551  68.675  62.314  1.00 67.59  ?  815 HOH A O     1 
HETATM 3449 O  O     . HOH G 7 .   ? 28.702  59.976  107.966 1.00 40.17  ?  816 HOH A O     1 
HETATM 3450 O  O     . HOH G 7 .   ? 22.294  76.935  77.486  1.00 49.61  ?  817 HOH A O     1 
HETATM 3451 O  O     . HOH G 7 .   ? 27.779  76.081  79.986  1.00 43.88  ?  818 HOH A O     1 
HETATM 3452 O  O     . HOH G 7 .   ? -10.314 84.291  87.297  1.00 39.44  ?  819 HOH A O     1 
HETATM 3453 O  O     . HOH G 7 .   ? -1.082  69.330  103.819 1.00 24.66  ?  820 HOH A O     1 
HETATM 3454 O  O     . HOH G 7 .   ? 32.871  72.905  82.005  1.00 38.13  ?  821 HOH A O     1 
HETATM 3455 O  O     . HOH G 7 .   ? 20.054  97.585  98.763  1.00 46.22  ?  822 HOH A O     1 
HETATM 3456 O  O     . HOH G 7 .   ? -9.684  53.989  98.827  1.00 52.38  ?  823 HOH A O     1 
HETATM 3457 O  O     . HOH G 7 .   ? -9.413  78.977  77.356  1.00 47.72  ?  824 HOH A O     1 
HETATM 3458 O  O     . HOH G 7 .   ? -13.903 78.126  77.218  1.00 43.31  ?  825 HOH A O     1 
HETATM 3459 O  O     . HOH H 7 .   ? 2.007   60.343  73.734  1.00 19.26  ?  101 HOH B O     1 
HETATM 3460 O  O     . HOH H 7 .   ? 7.139   49.125  59.865  1.00 47.81  ?  102 HOH B O     1 
HETATM 3461 O  O     . HOH H 7 .   ? -7.192  56.803  72.570  1.00 24.33  ?  103 HOH B O     1 
HETATM 3462 O  O     . HOH H 7 .   ? -10.389 63.645  72.331  1.00 55.38  ?  104 HOH B O     1 
HETATM 3463 O  O     . HOH H 7 .   ? -0.175  53.450  75.459  1.00 30.58  ?  105 HOH B O     1 
HETATM 3464 O  O     . HOH H 7 .   ? 1.055   50.555  58.578  1.00 33.29  ?  106 HOH B O     1 
HETATM 3465 O  O     . HOH H 7 .   ? -5.577  47.735  65.616  1.00 43.85  ?  107 HOH B O     1 
HETATM 3466 O  O     . HOH H 7 .   ? -11.621 71.590  68.468  1.00 51.29  ?  108 HOH B O     1 
HETATM 3467 O  O     . HOH H 7 .   ? 10.092  56.863  69.221  1.00 38.79  ?  109 HOH B O     1 
HETATM 3468 O  O     . HOH H 7 .   ? 7.737   63.992  52.389  1.00 42.60  ?  110 HOH B O     1 
HETATM 3469 O  O     . HOH H 7 .   ? -0.726  44.595  71.877  1.00 36.78  ?  111 HOH B O     1 
HETATM 3470 O  O     . HOH H 7 .   ? 4.001   59.032  72.453  1.00 16.42  ?  112 HOH B O     1 
HETATM 3471 O  O     . HOH H 7 .   ? 10.739  82.225  68.226  1.00 72.53  ?  113 HOH B O     1 
HETATM 3472 O  O     . HOH H 7 .   ? -4.463  50.860  73.051  1.00 18.17  ?  114 HOH B O     1 
HETATM 3473 O  O     . HOH H 7 .   ? 8.739   47.271  74.701  1.00 50.01  ?  115 HOH B O     1 
HETATM 3474 O  O     . HOH H 7 .   ? -1.078  45.477  65.323  1.00 40.83  ?  116 HOH B O     1 
HETATM 3475 O  O     . HOH H 7 .   ? -3.559  76.117  72.465  1.00 32.57  ?  117 HOH B O     1 
HETATM 3476 O  O     . HOH H 7 .   ? -7.360  54.559  74.204  1.00 37.99  ?  118 HOH B O     1 
HETATM 3477 O  O     . HOH H 7 .   ? -5.325  45.330  68.930  1.00 32.63  ?  119 HOH B O     1 
HETATM 3478 O  O     . HOH H 7 .   ? -2.747  55.062  74.687  1.00 31.50  ?  120 HOH B O     1 
HETATM 3479 O  O     . HOH H 7 .   ? -5.340  53.192  73.922  1.00 23.82  ?  121 HOH B O     1 
HETATM 3480 O  O     . HOH H 7 .   ? -3.862  47.329  73.551  1.00 40.27  ?  122 HOH B O     1 
HETATM 3481 O  O     . HOH H 7 .   ? -10.306 75.994  69.818  1.00 45.76  ?  123 HOH B O     1 
HETATM 3482 O  O     . HOH H 7 .   ? -8.764  58.978  74.941  1.00 50.36  ?  124 HOH B O     1 
HETATM 3483 O  O     . HOH H 7 .   ? 13.154  57.451  72.003  1.00 46.46  ?  125 HOH B O     1 
HETATM 3484 O  O     . HOH H 7 .   ? -9.219  72.287  72.326  1.00 54.65  ?  126 HOH B O     1 
HETATM 3485 O  O     . HOH H 7 .   ? -9.788  57.997  71.680  1.00 48.72  ?  127 HOH B O     1 
HETATM 3486 O  O     . HOH H 7 .   ? -11.819 61.791  69.337  1.00 51.98  ?  128 HOH B O     1 
HETATM 3487 O  O     . HOH H 7 .   ? -13.381 64.306  70.855  1.00 52.88  ?  129 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   . LEU A 12  ? 0.8001 0.8604 0.8453 -0.0612 0.0115  -0.0059 13  LEU A N   
2    C CA  . LEU A 12  ? 0.8001 0.8702 0.8441 -0.0582 0.0122  -0.0098 13  LEU A CA  
3    C C   . LEU A 12  ? 0.7970 0.8666 0.8428 -0.0566 0.0110  -0.0152 13  LEU A C   
4    O O   . LEU A 12  ? 0.7964 0.8704 0.8409 -0.0524 0.0107  -0.0179 13  LEU A O   
5    C CB  . LEU A 12  ? 0.8012 0.8828 0.8466 -0.0618 0.0140  -0.0089 13  LEU A CB  
6    N N   . LYS A 13  ? 0.7921 0.8566 0.8412 -0.0603 0.0101  -0.0165 14  LYS A N   
7    C CA  . LYS A 13  ? 0.7911 0.8561 0.8416 -0.0598 0.0090  -0.0219 14  LYS A CA  
8    C C   . LYS A 13  ? 0.7875 0.8412 0.8394 -0.0603 0.0081  -0.0240 14  LYS A C   
9    O O   . LYS A 13  ? 0.7967 0.8466 0.8526 -0.0650 0.0078  -0.0248 14  LYS A O   
10   C CB  . LYS A 13  ? 0.8129 0.8864 0.8670 -0.0644 0.0090  -0.0235 14  LYS A CB  
11   N N   . TYR A 14  ? 0.7691 0.8175 0.8184 -0.0556 0.0076  -0.0250 15  TYR A N   
12   C CA  . TYR A 14  ? 0.7566 0.7950 0.8078 -0.0555 0.0071  -0.0277 15  TYR A CA  
13   C C   . TYR A 14  ? 0.7424 0.7835 0.7923 -0.0538 0.0065  -0.0338 15  TYR A C   
14   O O   . TYR A 14  ? 0.7417 0.7883 0.7879 -0.0500 0.0062  -0.0341 15  TYR A O   
15   C CB  . TYR A 14  ? 0.7529 0.7834 0.8029 -0.0519 0.0071  -0.0245 15  TYR A CB  
16   C CG  . TYR A 14  ? 0.7555 0.7845 0.8056 -0.0533 0.0074  -0.0177 15  TYR A CG  
17   C CD1 . TYR A 14  ? 0.7676 0.7913 0.8223 -0.0580 0.0072  -0.0147 15  TYR A CD1 
18   C CD2 . TYR A 14  ? 0.7630 0.7959 0.8087 -0.0502 0.0078  -0.0142 15  TYR A CD2 
19   C CE1 . TYR A 14  ? 0.7804 0.8036 0.8347 -0.0598 0.0073  -0.0077 15  TYR A CE1 
20   C CE2 . TYR A 14  ? 0.7761 0.8088 0.8211 -0.0520 0.0081  -0.0081 15  TYR A CE2 
21   C CZ  . TYR A 14  ? 0.7893 0.8175 0.8385 -0.0569 0.0078  -0.0045 15  TYR A CZ  
22   O OH  . TYR A 14  ? 0.8049 0.8339 0.8530 -0.0592 0.0078  0.0023  15  TYR A OH  
23   N N   . SER A 15  ? 0.7285 0.7658 0.7816 -0.0567 0.0062  -0.0385 16  SER A N   
24   C CA  . SER A 15  ? 0.7177 0.7580 0.7694 -0.0561 0.0057  -0.0447 16  SER A CA  
25   C C   . SER A 15  ? 0.7025 0.7369 0.7522 -0.0517 0.0060  -0.0462 16  SER A C   
26   O O   . SER A 15  ? 0.7051 0.7313 0.7564 -0.0499 0.0064  -0.0433 16  SER A O   
27   C CB  . SER A 15  ? 0.7392 0.7778 0.7952 -0.0614 0.0057  -0.0500 16  SER A CB  
28   O OG  . SER A 15  ? 0.7682 0.7957 0.8295 -0.0632 0.0062  -0.0494 16  SER A OG  
29   N N   . LYS A 16  ? 0.6839 0.7230 0.7304 -0.0502 0.0056  -0.0505 17  LYS A N   
30   C CA  . LYS A 16  ? 0.6753 0.7101 0.7199 -0.0463 0.0060  -0.0523 17  LYS A CA  
31   C C   . LYS A 16  ? 0.6682 0.6932 0.7177 -0.0473 0.0070  -0.0564 17  LYS A C   
32   O O   . LYS A 16  ? 0.6724 0.6925 0.7220 -0.0438 0.0076  -0.0568 17  LYS A O   
33   C CB  . LYS A 16  ? 0.6952 0.7382 0.7351 -0.0451 0.0054  -0.0555 17  LYS A CB  
34   C CG  . LYS A 16  ? 0.7369 0.7786 0.7733 -0.0401 0.0056  -0.0538 17  LYS A CG  
35   C CD  . LYS A 16  ? 0.7830 0.8323 0.8151 -0.0396 0.0049  -0.0568 17  LYS A CD  
36   C CE  . LYS A 16  ? 0.8284 0.8769 0.8615 -0.0423 0.0058  -0.0642 17  LYS A CE  
37   N NZ  . LYS A 16  ? 0.8538 0.9092 0.8819 -0.0415 0.0054  -0.0665 17  LYS A NZ  
38   N N   . SER A 17  ? 0.6561 0.6784 0.7107 -0.0519 0.0072  -0.0595 18  SER A N   
39   C CA  . SER A 17  ? 0.6501 0.6625 0.7113 -0.0529 0.0080  -0.0635 18  SER A CA  
40   C C   . SER A 17  ? 0.6265 0.6295 0.6919 -0.0515 0.0079  -0.0568 18  SER A C   
41   O O   . SER A 17  ? 0.6338 0.6287 0.7029 -0.0489 0.0083  -0.0574 18  SER A O   
42   C CB  . SER A 17  ? 0.6822 0.6947 0.7479 -0.0587 0.0082  -0.0692 18  SER A CB  
43   O OG  . SER A 17  ? 0.7247 0.7381 0.7921 -0.0622 0.0075  -0.0645 18  SER A OG  
44   N N   . GLN A 18  ? 0.5970 0.6019 0.6616 -0.0532 0.0072  -0.0503 19  GLN A N   
45   C CA  . GLN A 18  ? 0.5796 0.5779 0.6469 -0.0526 0.0068  -0.0428 19  GLN A CA  
46   C C   . GLN A 18  ? 0.5515 0.5488 0.6151 -0.0471 0.0067  -0.0390 19  GLN A C   
47   O O   . GLN A 18  ? 0.5520 0.5417 0.6190 -0.0457 0.0063  -0.0348 19  GLN A O   
48   C CB  . GLN A 18  ? 0.6042 0.6080 0.6699 -0.0559 0.0065  -0.0372 19  GLN A CB  
49   C CG  . GLN A 18  ? 0.6544 0.6574 0.7253 -0.0620 0.0064  -0.0389 19  GLN A CG  
50   C CD  . GLN A 18  ? 0.7140 0.7223 0.7839 -0.0653 0.0063  -0.0327 19  GLN A CD  
51   O OE1 . GLN A 18  ? 0.7413 0.7440 0.8152 -0.0681 0.0060  -0.0273 19  GLN A OE1 
52   N NE2 . GLN A 18  ? 0.7164 0.7359 0.7815 -0.0652 0.0066  -0.0330 19  GLN A NE2 
53   N N   . ILE A 19  ? 0.5262 0.5313 0.5831 -0.0441 0.0069  -0.0401 20  ILE A N   
54   C CA  . ILE A 19  ? 0.5089 0.5139 0.5620 -0.0392 0.0068  -0.0370 20  ILE A CA  
55   C C   . ILE A 19  ? 0.4937 0.4929 0.5493 -0.0363 0.0072  -0.0410 20  ILE A C   
56   O O   . ILE A 19  ? 0.4924 0.4863 0.5493 -0.0333 0.0069  -0.0375 20  ILE A O   
57   C CB  . ILE A 19  ? 0.5105 0.5256 0.5567 -0.0374 0.0067  -0.0364 20  ILE A CB  
58   C CG1 . ILE A 19  ? 0.5223 0.5421 0.5672 -0.0392 0.0066  -0.0311 20  ILE A CG1 
59   C CG2 . ILE A 19  ? 0.5114 0.5267 0.5539 -0.0324 0.0067  -0.0354 20  ILE A CG2 
60   C CD1 . ILE A 19  ? 0.5396 0.5691 0.5800 -0.0379 0.0065  -0.0309 20  ILE A CD1 
61   N N   . GLU A 20  ? 0.4821 0.4824 0.5389 -0.0374 0.0079  -0.0484 21  GLU A N   
62   C CA  . GLU A 20  ? 0.4760 0.4715 0.5359 -0.0351 0.0088  -0.0534 21  GLU A CA  
63   C C   . GLU A 20  ? 0.4664 0.4508 0.5355 -0.0355 0.0087  -0.0525 21  GLU A C   
64   O O   . GLU A 20  ? 0.4620 0.4412 0.5345 -0.0320 0.0088  -0.0523 21  GLU A O   
65   C CB  . GLU A 20  ? 0.5082 0.5088 0.5673 -0.0372 0.0097  -0.0622 21  GLU A CB  
66   N N   . LYS A 21  ? 0.4600 0.4410 0.5337 -0.0397 0.0082  -0.0514 22  LYS A N   
67   C CA  . LYS A 21  ? 0.4671 0.4372 0.5504 -0.0406 0.0077  -0.0493 22  LYS A CA  
68   C C   . LYS A 21  ? 0.4594 0.4260 0.5428 -0.0384 0.0063  -0.0396 22  LYS A C   
69   O O   . LYS A 21  ? 0.4650 0.4230 0.5557 -0.0365 0.0057  -0.0378 22  LYS A O   
70   C CB  . LYS A 21  ? 0.5065 0.4744 0.5945 -0.0463 0.0075  -0.0504 22  LYS A CB  
71   C CG  . LYS A 21  ? 0.5822 0.5379 0.6820 -0.0475 0.0070  -0.0502 22  LYS A CG  
72   C CD  . LYS A 21  ? 0.6491 0.6024 0.7538 -0.0537 0.0068  -0.0514 22  LYS A CD  
73   C CE  . LYS A 21  ? 0.6995 0.6486 0.8072 -0.0562 0.0051  -0.0413 22  LYS A CE  
74   N NZ  . LYS A 21  ? 0.7293 0.6837 0.8347 -0.0620 0.0051  -0.0403 22  LYS A NZ  
75   N N   . ALA A 22  ? 0.4410 0.4145 0.5165 -0.0384 0.0058  -0.0337 23  ALA A N   
76   C CA  . ALA A 22  ? 0.4275 0.3999 0.5015 -0.0367 0.0046  -0.0249 23  ALA A CA  
77   C C   . ALA A 22  ? 0.4172 0.3883 0.4903 -0.0314 0.0045  -0.0250 23  ALA A C   
78   O O   . ALA A 22  ? 0.4185 0.3843 0.4951 -0.0297 0.0032  -0.0196 23  ALA A O   
79   C CB  . ALA A 22  ? 0.4224 0.4038 0.4883 -0.0380 0.0046  -0.0207 23  ALA A CB  
80   N N   . ALA A 23  ? 0.4112 0.3874 0.4798 -0.0290 0.0056  -0.0309 24  ALA A N   
81   C CA  . ALA A 23  ? 0.4146 0.3904 0.4823 -0.0242 0.0058  -0.0318 24  ALA A CA  
82   C C   . ALA A 23  ? 0.4138 0.3811 0.4911 -0.0226 0.0060  -0.0352 24  ALA A C   
83   O O   . ALA A 23  ? 0.4069 0.3712 0.4867 -0.0191 0.0054  -0.0325 24  ALA A O   
84   C CB  . ALA A 23  ? 0.4113 0.3951 0.4721 -0.0229 0.0070  -0.0370 24  ALA A CB  
85   N N   . ARG A 24  ? 0.4195 0.3832 0.5029 -0.0252 0.0069  -0.0413 25  ARG A N   
86   C CA  . ARG A 24  ? 0.4329 0.3881 0.5271 -0.0238 0.0073  -0.0454 25  ARG A CA  
87   C C   . ARG A 24  ? 0.4387 0.3853 0.5408 -0.0234 0.0051  -0.0373 25  ARG A C   
88   O O   . ARG A 24  ? 0.4428 0.3839 0.5520 -0.0199 0.0046  -0.0369 25  ARG A O   
89   C CB  . ARG A 24  ? 0.4633 0.4168 0.5626 -0.0272 0.0087  -0.0543 25  ARG A CB  
90   C CG  . ARG A 24  ? 0.5234 0.4853 0.6166 -0.0272 0.0108  -0.0632 25  ARG A CG  
91   C CD  . ARG A 24  ? 0.5798 0.5407 0.6781 -0.0307 0.0124  -0.0730 25  ARG A CD  
92   N NE  . ARG A 24  ? 0.6261 0.5971 0.7155 -0.0341 0.0129  -0.0765 25  ARG A NE  
93   C CZ  . ARG A 24  ? 0.6509 0.6232 0.7398 -0.0388 0.0123  -0.0765 25  ARG A CZ  
94   N NH1 . ARG A 24  ? 0.6411 0.6049 0.7378 -0.0411 0.0114  -0.0735 25  ARG A NH1 
95   N NH2 . ARG A 24  ? 0.6468 0.6290 0.7278 -0.0414 0.0125  -0.0793 25  ARG A NH2 
96   N N   . LYS A 25  ? 0.4354 0.3815 0.5358 -0.0270 0.0037  -0.0303 26  LYS A N   
97   C CA  . LYS A 25  ? 0.4397 0.3790 0.5462 -0.0275 0.0013  -0.0210 26  LYS A CA  
98   C C   . LYS A 25  ? 0.4500 0.3904 0.5545 -0.0234 -0.0002 -0.0146 26  LYS A C   
99   O O   . LYS A 25  ? 0.4479 0.3810 0.5612 -0.0215 -0.0019 -0.0108 26  LYS A O   
100  C CB  . LYS A 25  ? 0.4487 0.3904 0.5515 -0.0327 0.0004  -0.0148 26  LYS A CB  
101  C CG  . LYS A 25  ? 0.4791 0.4174 0.5871 -0.0373 0.0011  -0.0194 26  LYS A CG  
102  C CD  . LYS A 25  ? 0.5279 0.4691 0.6327 -0.0425 0.0003  -0.0128 26  LYS A CD  
103  C CE  . LYS A 25  ? 0.5857 0.5255 0.6942 -0.0474 0.0012  -0.0182 26  LYS A CE  
104  N NZ  . LYS A 25  ? 0.6266 0.5548 0.7483 -0.0480 0.0008  -0.0216 26  LYS A NZ  
105  N N   . ILE A 26  ? 0.4554 0.4046 0.5487 -0.0219 0.0004  -0.0136 27  ILE A N   
106  C CA  . ILE A 26  ? 0.4677 0.4194 0.5578 -0.0184 -0.0008 -0.0083 27  ILE A CA  
107  C C   . ILE A 26  ? 0.4965 0.4451 0.5924 -0.0136 -0.0004 -0.0130 27  ILE A C   
108  O O   . ILE A 26  ? 0.4983 0.4447 0.5976 -0.0109 -0.0021 -0.0080 27  ILE A O   
109  C CB  . ILE A 26  ? 0.4617 0.4235 0.5393 -0.0183 0.0000  -0.0077 27  ILE A CB  
110  C CG1 . ILE A 26  ? 0.4668 0.4327 0.5392 -0.0229 -0.0002 -0.0034 27  ILE A CG1 
111  C CG2 . ILE A 26  ? 0.4621 0.4266 0.5361 -0.0148 -0.0011 -0.0034 27  ILE A CG2 
112  C CD1 . ILE A 26  ? 0.4751 0.4398 0.5482 -0.0249 -0.0023 0.0064  27  ILE A CD1 
113  N N   . ARG A 27  ? 0.5152 0.4645 0.6124 -0.0129 0.0020  -0.0228 28  ARG A N   
114  C CA  . ARG A 27  ? 0.5429 0.4905 0.6458 -0.0089 0.0030  -0.0285 28  ARG A CA  
115  C C   . ARG A 27  ? 0.5648 0.5024 0.6819 -0.0075 0.0018  -0.0272 28  ARG A C   
116  O O   . ARG A 27  ? 0.5617 0.4975 0.6841 -0.0036 0.0009  -0.0255 28  ARG A O   
117  C CB  . ARG A 27  ? 0.5726 0.5241 0.6734 -0.0095 0.0060  -0.0393 28  ARG A CB  
118  C CG  . ARG A 27  ? 0.6441 0.6055 0.7324 -0.0095 0.0070  -0.0407 28  ARG A CG  
119  C CD  . ARG A 27  ? 0.7108 0.6767 0.7983 -0.0082 0.0095  -0.0500 28  ARG A CD  
120  N NE  . ARG A 27  ? 0.7673 0.7387 0.8492 -0.0117 0.0108  -0.0555 28  ARG A NE  
121  C CZ  . ARG A 27  ? 0.8045 0.7734 0.8913 -0.0146 0.0119  -0.0620 28  ARG A CZ  
122  N NH1 . ARG A 27  ? 0.7988 0.7590 0.8971 -0.0143 0.0119  -0.0638 28  ARG A NH1 
123  N NH2 . ARG A 27  ? 0.8087 0.7840 0.8896 -0.0180 0.0128  -0.0665 28  ARG A NH2 
124  N N   . HIS A 28  ? 0.5816 0.5128 0.7055 -0.0108 0.0014  -0.0275 29  HIS A N   
125  C CA  . HIS A 28  ? 0.6014 0.5222 0.7403 -0.0099 0.0000  -0.0262 29  HIS A CA  
126  C C   . HIS A 28  ? 0.6074 0.5240 0.7498 -0.0100 -0.0038 -0.0134 29  HIS A C   
127  O O   . HIS A 28  ? 0.6165 0.5242 0.7722 -0.0089 -0.0057 -0.0106 29  HIS A O   
128  C CB  . HIS A 28  ? 0.6232 0.5384 0.7689 -0.0136 0.0012  -0.0326 29  HIS A CB  
129  C CG  . HIS A 28  ? 0.6671 0.5873 0.8098 -0.0137 0.0047  -0.0452 29  HIS A CG  
130  N ND1 . HIS A 28  ? 0.6936 0.6150 0.8403 -0.0095 0.0066  -0.0526 29  HIS A ND1 
131  C CD2 . HIS A 28  ? 0.6866 0.6120 0.8220 -0.0176 0.0065  -0.0508 29  HIS A CD2 
132  C CE1 . HIS A 28  ? 0.7025 0.6300 0.8438 -0.0114 0.0095  -0.0624 29  HIS A CE1 
133  N NE2 . HIS A 28  ? 0.7011 0.6311 0.8356 -0.0162 0.0093  -0.0616 29  HIS A NE2 
134  N N   . GLY A 29  ? 0.6010 0.5243 0.7320 -0.0113 -0.0050 -0.0059 30  GLY A N   
135  C CA  . GLY A 29  ? 0.6004 0.5223 0.7323 -0.0119 -0.0085 0.0063  30  GLY A CA  
136  C C   . GLY A 29  ? 0.5989 0.5165 0.7337 -0.0170 -0.0104 0.0135  30  GLY A C   
137  O O   . GLY A 29  ? 0.6135 0.5234 0.7591 -0.0171 -0.0133 0.0202  30  GLY A O   
138  N N   . CYS A 30  ? 0.5752 0.4980 0.7007 -0.0215 -0.0090 0.0128  31  CYS A N   
139  C CA  . CYS A 30  ? 0.5636 0.4840 0.6905 -0.0270 -0.0105 0.0198  31  CYS A CA  
140  C C   . CYS A 30  ? 0.5423 0.4671 0.6637 -0.0286 -0.0133 0.0320  31  CYS A C   
141  O O   . CYS A 30  ? 0.5420 0.4729 0.6565 -0.0257 -0.0136 0.0338  31  CYS A O   
142  C CB  . CYS A 30  ? 0.5768 0.5021 0.6963 -0.0312 -0.0080 0.0144  31  CYS A CB  
143  S SG  . CYS A 30  ? 0.6300 0.5694 0.7323 -0.0309 -0.0061 0.0132  31  CYS A SG  
144  N N   . GLU A 31  ? 0.5242 0.4462 0.6486 -0.0336 -0.0153 0.0404  32  GLU A N   
145  C CA  . GLU A 31  ? 0.5039 0.4308 0.6232 -0.0362 -0.0180 0.0524  32  GLU A CA  
146  C C   . GLU A 31  ? 0.4754 0.4054 0.5907 -0.0432 -0.0178 0.0571  32  GLU A C   
147  O O   . GLU A 31  ? 0.4728 0.3998 0.5910 -0.0458 -0.0160 0.0516  32  GLU A O   
148  C CB  . GLU A 31  ? 0.5380 0.4568 0.6692 -0.0346 -0.0221 0.0612  32  GLU A CB  
149  C CG  . GLU A 31  ? 0.6148 0.5328 0.7493 -0.0279 -0.0227 0.0585  32  GLU A CG  
150  C CD  . GLU A 31  ? 0.7207 0.6359 0.8625 -0.0264 -0.0272 0.0694  32  GLU A CD  
151  O OE1 . GLU A 31  ? 0.7394 0.6455 0.8939 -0.0279 -0.0301 0.0756  32  GLU A OE1 
152  O OE2 . GLU A 31  ? 0.7475 0.6696 0.8829 -0.0238 -0.0280 0.0718  32  GLU A OE2 
153  N N   . GLY A 32  ? 0.4590 0.3958 0.5676 -0.0466 -0.0195 0.0670  33  GLY A N   
154  C CA  . GLY A 32  ? 0.4500 0.3910 0.5550 -0.0537 -0.0197 0.0736  33  GLY A CA  
155  C C   . GLY A 32  ? 0.4364 0.3851 0.5330 -0.0566 -0.0160 0.0669  33  GLY A C   
156  O O   . GLY A 32  ? 0.4378 0.3950 0.5247 -0.0542 -0.0136 0.0610  33  GLY A O   
157  N N   . ALA A 33  ? 0.4264 0.3725 0.5270 -0.0621 -0.0158 0.0684  34  ALA A N   
158  C CA  . ALA A 33  ? 0.4232 0.3767 0.5173 -0.0654 -0.0126 0.0626  34  ALA A CA  
159  C C   . ALA A 33  ? 0.4242 0.3761 0.5187 -0.0611 -0.0100 0.0497  34  ALA A C   
160  O O   . ALA A 33  ? 0.4273 0.3880 0.5137 -0.0613 -0.0074 0.0439  34  ALA A O   
161  C CB  . ALA A 33  ? 0.4211 0.3712 0.5209 -0.0724 -0.0133 0.0673  34  ALA A CB  
162  N N   . GLU A 34  ? 0.4197 0.3608 0.5238 -0.0575 -0.0107 0.0452  35  GLU A N   
163  C CA  . GLU A 34  ? 0.4217 0.3613 0.5267 -0.0537 -0.0084 0.0332  35  GLU A CA  
164  C C   . GLU A 34  ? 0.4127 0.3605 0.5079 -0.0487 -0.0070 0.0292  35  GLU A C   
165  O O   . GLU A 34  ? 0.4131 0.3671 0.5023 -0.0479 -0.0046 0.0215  35  GLU A O   
166  C CB  . GLU A 34  ? 0.4607 0.3877 0.5789 -0.0509 -0.0096 0.0302  35  GLU A CB  
167  C CG  . GLU A 34  ? 0.5366 0.4619 0.6565 -0.0481 -0.0071 0.0173  35  GLU A CG  
168  C CD  . GLU A 34  ? 0.6438 0.5573 0.7774 -0.0454 -0.0078 0.0131  35  GLU A CD  
169  O OE1 . GLU A 34  ? 0.6658 0.5726 0.8072 -0.0437 -0.0104 0.0202  35  GLU A OE1 
170  O OE2 . GLU A 34  ? 0.6744 0.5858 0.8114 -0.0452 -0.0057 0.0026  35  GLU A OE2 
171  N N   . ARG A 35  ? 0.3989 0.3473 0.4926 -0.0456 -0.0088 0.0350  36  ARG A N   
172  C CA  . ARG A 35  ? 0.3973 0.3530 0.4821 -0.0412 -0.0077 0.0321  36  ARG A CA  
173  C C   . ARG A 35  ? 0.4027 0.3702 0.4762 -0.0436 -0.0060 0.0323  36  ARG A C   
174  O O   . ARG A 35  ? 0.4017 0.3750 0.4690 -0.0408 -0.0040 0.0259  36  ARG A O   
175  C CB  . ARG A 35  ? 0.4072 0.3612 0.4936 -0.0381 -0.0103 0.0387  36  ARG A CB  
176  C CG  . ARG A 35  ? 0.4372 0.3994 0.5142 -0.0342 -0.0093 0.0366  36  ARG A CG  
177  C CD  . ARG A 35  ? 0.4728 0.4327 0.5525 -0.0306 -0.0117 0.0412  36  ARG A CD  
178  N NE  . ARG A 35  ? 0.5187 0.4741 0.6033 -0.0253 -0.0109 0.0337  36  ARG A NE  
179  C CZ  . ARG A 35  ? 0.5408 0.5010 0.6197 -0.0214 -0.0097 0.0292  36  ARG A CZ  
180  N NH1 . ARG A 35  ? 0.5275 0.4965 0.5962 -0.0219 -0.0094 0.0313  36  ARG A NH1 
181  N NH2 . ARG A 35  ? 0.5523 0.5088 0.6360 -0.0171 -0.0088 0.0225  36  ARG A NH2 
182  N N   . GLU A 36  ? 0.4128 0.3842 0.4842 -0.0488 -0.0066 0.0396  37  GLU A N   
183  C CA  . GLU A 36  ? 0.4227 0.4059 0.4844 -0.0512 -0.0047 0.0396  37  GLU A CA  
184  C C   . GLU A 36  ? 0.4151 0.4019 0.4754 -0.0525 -0.0022 0.0319  37  GLU A C   
185  O O   . GLU A 36  ? 0.4206 0.4169 0.4735 -0.0521 -0.0004 0.0290  37  GLU A O   
186  C CB  . GLU A 36  ? 0.4696 0.4573 0.5291 -0.0569 -0.0059 0.0495  37  GLU A CB  
187  C CG  . GLU A 36  ? 0.5691 0.5561 0.6281 -0.0558 -0.0086 0.0576  37  GLU A CG  
188  C CD  . GLU A 36  ? 0.6935 0.6843 0.7469 -0.0504 -0.0083 0.0545  37  GLU A CD  
189  O OE1 . GLU A 36  ? 0.7282 0.7276 0.7738 -0.0493 -0.0059 0.0492  37  GLU A OE1 
190  O OE2 . GLU A 36  ? 0.7232 0.7084 0.7806 -0.0473 -0.0107 0.0576  37  GLU A OE2 
191  N N   . GLU A 37  ? 0.4053 0.3848 0.4729 -0.0539 -0.0022 0.0283  38  GLU A N   
192  C CA  . GLU A 37  ? 0.3986 0.3820 0.4651 -0.0551 -0.0001 0.0207  38  GLU A CA  
193  C C   . GLU A 37  ? 0.3772 0.3612 0.4417 -0.0496 0.0009  0.0122  38  GLU A C   
194  O O   . GLU A 37  ? 0.3745 0.3664 0.4335 -0.0490 0.0025  0.0076  38  GLU A O   
195  C CB  . GLU A 37  ? 0.4455 0.4220 0.5205 -0.0595 -0.0006 0.0198  38  GLU A CB  
196  C CG  . GLU A 37  ? 0.5431 0.5255 0.6165 -0.0621 0.0013  0.0133  38  GLU A CG  
197  C CD  . GLU A 37  ? 0.6746 0.6696 0.7406 -0.0645 0.0027  0.0152  38  GLU A CD  
198  O OE1 . GLU A 37  ? 0.6971 0.6995 0.7583 -0.0622 0.0042  0.0093  38  GLU A OE1 
199  O OE2 . GLU A 37  ? 0.7193 0.7169 0.7843 -0.0685 0.0023  0.0228  38  GLU A OE2 
200  N N   . ALA A 38  ? 0.3635 0.3395 0.4325 -0.0458 0.0000  0.0105  39  ALA A N   
201  C CA  . ALA A 38  ? 0.3578 0.3341 0.4251 -0.0408 0.0010  0.0031  39  ALA A CA  
202  C C   . ALA A 38  ? 0.3554 0.3405 0.4137 -0.0378 0.0017  0.0033  39  ALA A C   
203  O O   . ALA A 38  ? 0.3549 0.3451 0.4091 -0.0361 0.0030  -0.0024 39  ALA A O   
204  C CB  . ALA A 38  ? 0.3564 0.3234 0.4309 -0.0375 -0.0002 0.0026  39  ALA A CB  
205  N N   . ILE A 39  ? 0.3537 0.3407 0.4090 -0.0375 0.0007  0.0102  40  ILE A N   
206  C CA  . ILE A 39  ? 0.3537 0.3484 0.4011 -0.0350 0.0013  0.0106  40  ILE A CA  
207  C C   . ILE A 39  ? 0.3623 0.3667 0.4043 -0.0372 0.0029  0.0090  40  ILE A C   
208  O O   . ILE A 39  ? 0.3674 0.3775 0.4044 -0.0345 0.0039  0.0057  40  ILE A O   
209  C CB  . ILE A 39  ? 0.3560 0.3502 0.4024 -0.0348 -0.0005 0.0182  40  ILE A CB  
210  C CG1 . ILE A 39  ? 0.3688 0.3548 0.4207 -0.0309 -0.0020 0.0183  40  ILE A CG1 
211  C CG2 . ILE A 39  ? 0.3553 0.3589 0.3934 -0.0339 0.0004  0.0191  40  ILE A CG2 
212  C CD1 . ILE A 39  ? 0.3875 0.3731 0.4391 -0.0301 -0.0042 0.0257  40  ILE A CD1 
213  N N   . LYS A 40  ? 0.3640 0.3700 0.4077 -0.0421 0.0033  0.0111  41  LYS A N   
214  C CA  . LYS A 40  ? 0.3694 0.3850 0.4093 -0.0446 0.0049  0.0097  41  LYS A CA  
215  C C   . LYS A 40  ? 0.3699 0.3878 0.4101 -0.0431 0.0059  0.0021  41  LYS A C   
216  O O   . LYS A 40  ? 0.3780 0.4042 0.4145 -0.0420 0.0071  -0.0005 41  LYS A O   
217  C CB  . LYS A 40  ? 0.4049 0.4210 0.4476 -0.0507 0.0048  0.0145  41  LYS A CB  
218  C CG  . LYS A 40  ? 0.4790 0.5064 0.5177 -0.0539 0.0066  0.0152  41  LYS A CG  
219  C CD  . LYS A 40  ? 0.5572 0.5847 0.5989 -0.0605 0.0063  0.0206  41  LYS A CD  
220  C CE  . LYS A 40  ? 0.6231 0.6629 0.6616 -0.0641 0.0084  0.0210  41  LYS A CE  
221  N NZ  . LYS A 40  ? 0.6544 0.7022 0.6866 -0.0634 0.0093  0.0238  41  LYS A NZ  
222  N N   . MET A 41  ? 0.3563 0.3672 0.4014 -0.0431 0.0054  -0.0015 42  MET A N   
223  C CA  . MET A 41  ? 0.3457 0.3588 0.3911 -0.0421 0.0060  -0.0086 42  MET A CA  
224  C C   . MET A 41  ? 0.3259 0.3406 0.3675 -0.0368 0.0061  -0.0118 42  MET A C   
225  O O   . MET A 41  ? 0.3232 0.3437 0.3624 -0.0357 0.0066  -0.0158 42  MET A O   
226  C CB  . MET A 41  ? 0.3612 0.3663 0.4128 -0.0438 0.0056  -0.0120 42  MET A CB  
227  C CG  . MET A 41  ? 0.4113 0.4139 0.4677 -0.0494 0.0053  -0.0092 42  MET A CG  
228  S SD  . MET A 41  ? 0.5108 0.5051 0.5752 -0.0519 0.0051  -0.0152 42  MET A SD  
229  C CE  . MET A 41  ? 0.4770 0.4708 0.5459 -0.0590 0.0048  -0.0104 42  MET A CE  
230  N N   . ILE A 42  ? 0.3124 0.3218 0.3540 -0.0338 0.0054  -0.0097 43  ILE A N   
231  C CA  . ILE A 42  ? 0.2996 0.3101 0.3378 -0.0291 0.0055  -0.0122 43  ILE A CA  
232  C C   . ILE A 42  ? 0.2874 0.3056 0.3201 -0.0276 0.0060  -0.0105 43  ILE A C   
233  O O   . ILE A 42  ? 0.2832 0.3049 0.3132 -0.0248 0.0062  -0.0135 43  ILE A O   
234  C CB  . ILE A 42  ? 0.3026 0.3054 0.3436 -0.0266 0.0047  -0.0109 43  ILE A CB  
235  C CG1 . ILE A 42  ? 0.3147 0.3109 0.3619 -0.0273 0.0047  -0.0152 43  ILE A CG1 
236  C CG2 . ILE A 42  ? 0.3046 0.3093 0.3419 -0.0221 0.0047  -0.0121 43  ILE A CG2 
237  C CD1 . ILE A 42  ? 0.3343 0.3219 0.3872 -0.0257 0.0037  -0.0131 43  ILE A CD1 
238  N N   . GLN A 43  ? 0.2826 0.3038 0.3141 -0.0298 0.0062  -0.0058 44  GLN A N   
239  C CA  . GLN A 43  ? 0.2880 0.3170 0.3149 -0.0289 0.0070  -0.0050 44  GLN A CA  
240  C C   . GLN A 43  ? 0.2824 0.3186 0.3092 -0.0296 0.0080  -0.0088 44  GLN A C   
241  O O   . GLN A 43  ? 0.2880 0.3292 0.3127 -0.0268 0.0084  -0.0109 44  GLN A O   
242  C CB  . GLN A 43  ? 0.3179 0.3492 0.3433 -0.0319 0.0071  0.0006  44  GLN A CB  
243  C CG  . GLN A 43  ? 0.3771 0.4180 0.3985 -0.0318 0.0085  0.0005  44  GLN A CG  
244  C CD  . GLN A 43  ? 0.4584 0.5001 0.4764 -0.0278 0.0084  -0.0005 44  GLN A CD  
245  O OE1 . GLN A 43  ? 0.4993 0.5440 0.5143 -0.0284 0.0086  0.0023  44  GLN A OE1 
246  N NE2 . GLN A 43  ? 0.4595 0.4993 0.4779 -0.0240 0.0082  -0.0044 44  GLN A NE2 
247  N N   . ASN A 44  ? 0.2645 0.3010 0.2945 -0.0331 0.0081  -0.0096 45  ASN A N   
248  C CA  . ASN A 44  ? 0.2522 0.2956 0.2830 -0.0341 0.0086  -0.0130 45  ASN A CA  
249  C C   . ASN A 44  ? 0.2385 0.2822 0.2688 -0.0306 0.0080  -0.0173 45  ASN A C   
250  O O   . ASN A 44  ? 0.2461 0.2966 0.2758 -0.0290 0.0081  -0.0190 45  ASN A O   
251  C CB  . ASN A 44  ? 0.2747 0.3166 0.3094 -0.0388 0.0085  -0.0132 45  ASN A CB  
252  C CG  . ASN A 44  ? 0.3155 0.3657 0.3515 -0.0407 0.0090  -0.0158 45  ASN A CG  
253  O OD1 . ASN A 44  ? 0.3301 0.3813 0.3675 -0.0406 0.0083  -0.0198 45  ASN A OD1 
254  N ND2 . ASN A 44  ? 0.3211 0.3785 0.3571 -0.0428 0.0101  -0.0137 45  ASN A ND2 
255  N N   . PHE A 45  ? 0.2162 0.2528 0.2472 -0.0295 0.0072  -0.0190 46  PHE A N   
256  C CA  . PHE A 45  ? 0.2033 0.2402 0.2333 -0.0269 0.0067  -0.0228 46  PHE A CA  
257  C C   . PHE A 45  ? 0.2025 0.2415 0.2293 -0.0226 0.0065  -0.0219 46  PHE A C   
258  O O   . PHE A 45  ? 0.2016 0.2452 0.2275 -0.0209 0.0061  -0.0237 46  PHE A O   
259  C CB  . PHE A 45  ? 0.1964 0.2256 0.2282 -0.0269 0.0064  -0.0248 46  PHE A CB  
260  C CG  . PHE A 45  ? 0.1953 0.2258 0.2259 -0.0250 0.0060  -0.0290 46  PHE A CG  
261  C CD1 . PHE A 45  ? 0.1923 0.2288 0.2227 -0.0267 0.0057  -0.0322 46  PHE A CD1 
262  C CD2 . PHE A 45  ? 0.1968 0.2232 0.2265 -0.0220 0.0060  -0.0297 46  PHE A CD2 
263  C CE1 . PHE A 45  ? 0.1947 0.2333 0.2233 -0.0256 0.0052  -0.0357 46  PHE A CE1 
264  C CE2 . PHE A 45  ? 0.1987 0.2271 0.2269 -0.0209 0.0059  -0.0335 46  PHE A CE2 
265  C CZ  . PHE A 45  ? 0.1944 0.2290 0.2218 -0.0228 0.0055  -0.0363 46  PHE A CZ  
266  N N   . ARG A 46  ? 0.1963 0.2322 0.2218 -0.0214 0.0068  -0.0188 47  ARG A N   
267  C CA  . ARG A 46  ? 0.1974 0.2349 0.2202 -0.0179 0.0068  -0.0180 47  ARG A CA  
268  C C   . ARG A 46  ? 0.2143 0.2597 0.2367 -0.0174 0.0073  -0.0184 47  ARG A C   
269  O O   . ARG A 46  ? 0.2147 0.2625 0.2364 -0.0145 0.0069  -0.0197 47  ARG A O   
270  C CB  . ARG A 46  ? 0.1946 0.2282 0.2162 -0.0177 0.0068  -0.0144 47  ARG A CB  
271  C CG  . ARG A 46  ? 0.2150 0.2504 0.2338 -0.0147 0.0069  -0.0138 47  ARG A CG  
272  C CD  . ARG A 46  ? 0.2306 0.2638 0.2480 -0.0151 0.0067  -0.0101 47  ARG A CD  
273  N NE  . ARG A 46  ? 0.2369 0.2735 0.2515 -0.0129 0.0070  -0.0103 47  ARG A NE  
274  C CZ  . ARG A 46  ? 0.2622 0.3050 0.2754 -0.0139 0.0081  -0.0101 47  ARG A CZ  
275  N NH1 . ARG A 46  ? 0.2546 0.3013 0.2685 -0.0171 0.0090  -0.0093 47  ARG A NH1 
276  N NH2 . ARG A 46  ? 0.2668 0.3122 0.2782 -0.0118 0.0084  -0.0112 47  ARG A NH2 
277  N N   . GLU A 47  ? 0.2242 0.2738 0.2478 -0.0203 0.0082  -0.0174 48  GLU A N   
278  C CA  . GLU A 47  ? 0.2336 0.2915 0.2582 -0.0199 0.0090  -0.0183 48  GLU A CA  
279  C C   . GLU A 47  ? 0.2267 0.2889 0.2537 -0.0191 0.0081  -0.0209 48  GLU A C   
280  O O   . GLU A 47  ? 0.2376 0.3053 0.2662 -0.0169 0.0082  -0.0219 48  GLU A O   
281  C CB  . GLU A 47  ? 0.2818 0.3438 0.3072 -0.0238 0.0103  -0.0166 48  GLU A CB  
282  C CG  . GLU A 47  ? 0.3817 0.4418 0.4043 -0.0248 0.0110  -0.0134 48  GLU A CG  
283  C CD  . GLU A 47  ? 0.5145 0.5780 0.5374 -0.0295 0.0121  -0.0107 48  GLU A CD  
284  O OE1 . GLU A 47  ? 0.5234 0.5875 0.5490 -0.0325 0.0121  -0.0109 48  GLU A OE1 
285  O OE2 . GLU A 47  ? 0.5731 0.6392 0.5934 -0.0306 0.0130  -0.0083 48  GLU A OE2 
286  N N   . LEU A 48  ? 0.2078 0.2677 0.2356 -0.0207 0.0072  -0.0221 49  LEU A N   
287  C CA  . LEU A 48  ? 0.2009 0.2655 0.2304 -0.0204 0.0059  -0.0242 49  LEU A CA  
288  C C   . LEU A 48  ? 0.2006 0.2653 0.2289 -0.0164 0.0048  -0.0245 49  LEU A C   
289  O O   . LEU A 48  ? 0.2097 0.2798 0.2399 -0.0154 0.0035  -0.0250 49  LEU A O   
290  C CB  . LEU A 48  ? 0.2034 0.2653 0.2331 -0.0234 0.0053  -0.0260 49  LEU A CB  
291  C CG  . LEU A 48  ? 0.2234 0.2920 0.2549 -0.0246 0.0039  -0.0280 49  LEU A CG  
292  C CD1 . LEU A 48  ? 0.2211 0.2974 0.2561 -0.0266 0.0043  -0.0276 49  LEU A CD1 
293  C CD2 . LEU A 48  ? 0.2305 0.2963 0.2615 -0.0274 0.0033  -0.0309 49  LEU A CD2 
294  N N   . HIS A 49  ? 0.1850 0.2439 0.2107 -0.0142 0.0050  -0.0237 50  HIS A N   
295  C CA  . HIS A 49  ? 0.1691 0.2276 0.1937 -0.0108 0.0040  -0.0236 50  HIS A CA  
296  C C   . HIS A 49  ? 0.1582 0.2200 0.1845 -0.0080 0.0042  -0.0229 50  HIS A C   
297  O O   . HIS A 49  ? 0.1527 0.2146 0.1793 -0.0054 0.0031  -0.0226 50  HIS A O   
298  C CB  . HIS A 49  ? 0.1640 0.2155 0.1857 -0.0099 0.0041  -0.0234 50  HIS A CB  
299  C CG  . HIS A 49  ? 0.1808 0.2297 0.2021 -0.0120 0.0039  -0.0252 50  HIS A CG  
300  N ND1 . HIS A 49  ? 0.2128 0.2598 0.2354 -0.0151 0.0045  -0.0258 50  HIS A ND1 
301  C CD2 . HIS A 49  ? 0.2005 0.2492 0.2205 -0.0118 0.0031  -0.0269 50  HIS A CD2 
302  C CE1 . HIS A 49  ? 0.2294 0.2746 0.2519 -0.0165 0.0043  -0.0284 50  HIS A CE1 
303  N NE2 . HIS A 49  ? 0.2303 0.2769 0.2510 -0.0146 0.0035  -0.0293 50  HIS A NE2 
304  N N   . LEU A 50  ? 0.1561 0.2208 0.1837 -0.0088 0.0057  -0.0228 51  LEU A N   
305  C CA  . LEU A 50  ? 0.1616 0.2296 0.1914 -0.0063 0.0064  -0.0232 51  LEU A CA  
306  C C   . LEU A 50  ? 0.1578 0.2312 0.1925 -0.0041 0.0051  -0.0238 51  LEU A C   
307  O O   . LEU A 50  ? 0.1606 0.2329 0.1965 -0.0011 0.0044  -0.0237 51  LEU A O   
308  C CB  . LEU A 50  ? 0.1703 0.2417 0.2003 -0.0082 0.0085  -0.0235 51  LEU A CB  
309  C CG  . LEU A 50  ? 0.2017 0.2765 0.2336 -0.0057 0.0097  -0.0250 51  LEU A CG  
310  C CD1 . LEU A 50  ? 0.2095 0.2786 0.2385 -0.0034 0.0093  -0.0246 51  LEU A CD1 
311  C CD2 . LEU A 50  ? 0.2126 0.2926 0.2444 -0.0082 0.0121  -0.0257 51  LEU A CD2 
312  N N   . TYR A 51  ? 0.1464 0.2255 0.1843 -0.0057 0.0046  -0.0242 52  TYR A N   
313  C CA  . TYR A 51  ? 0.1349 0.2197 0.1784 -0.0036 0.0029  -0.0242 52  TYR A CA  
314  C C   . TYR A 51  ? 0.1397 0.2218 0.1821 -0.0020 0.0003  -0.0225 52  TYR A C   
315  O O   . TYR A 51  ? 0.1456 0.2281 0.1914 0.0012  -0.0008 -0.0217 52  TYR A O   
316  C CB  . TYR A 51  ? 0.1183 0.2103 0.1655 -0.0061 0.0025  -0.0246 52  TYR A CB  
317  C CG  . TYR A 51  ? 0.1087 0.2067 0.1620 -0.0039 0.0001  -0.0238 52  TYR A CG  
318  C CD1 . TYR A 51  ? 0.1121 0.2123 0.1713 0.0000  0.0000  -0.0240 52  TYR A CD1 
319  C CD2 . TYR A 51  ? 0.1071 0.2087 0.1608 -0.0057 -0.0023 -0.0227 52  TYR A CD2 
320  C CE1 . TYR A 51  ? 0.1129 0.2179 0.1788 0.0023  -0.0027 -0.0225 52  TYR A CE1 
321  C CE2 . TYR A 51  ? 0.1072 0.2147 0.1667 -0.0038 -0.0051 -0.0211 52  TYR A CE2 
322  C CZ  . TYR A 51  ? 0.1182 0.2271 0.1841 0.0004  -0.0054 -0.0205 52  TYR A CZ  
323  O OH  . TYR A 51  ? 0.1363 0.2507 0.2094 0.0027  -0.0084 -0.0183 52  TYR A OH  
324  N N   . PRO A 52  ? 0.1381 0.2176 0.1761 -0.0042 -0.0006 -0.0221 53  PRO A N   
325  C CA  . PRO A 52  ? 0.1294 0.2075 0.1657 -0.0032 -0.0028 -0.0206 53  PRO A CA  
326  C C   . PRO A 52  ? 0.1253 0.1977 0.1598 -0.0006 -0.0025 -0.0198 53  PRO A C   
327  O O   . PRO A 52  ? 0.1296 0.2025 0.1653 0.0011  -0.0044 -0.0179 53  PRO A O   
328  C CB  . PRO A 52  ? 0.1398 0.2163 0.1716 -0.0066 -0.0028 -0.0217 53  PRO A CB  
329  C CG  . PRO A 52  ? 0.1491 0.2279 0.1821 -0.0094 -0.0016 -0.0232 53  PRO A CG  
330  C CD  . PRO A 52  ? 0.1319 0.2098 0.1667 -0.0080 0.0004  -0.0232 53  PRO A CD  
331  N N   . LEU A 53  ? 0.1172 0.1848 0.1492 -0.0004 -0.0003 -0.0208 54  LEU A N   
332  C CA  . LEU A 53  ? 0.1151 0.1779 0.1458 0.0019  -0.0001 -0.0203 54  LEU A CA  
333  C C   . LEU A 53  ? 0.1014 0.1664 0.1373 0.0049  -0.0006 -0.0201 54  LEU A C   
334  O O   . LEU A 53  ? 0.0962 0.1592 0.1330 0.0068  -0.0019 -0.0187 54  LEU A O   
335  C CB  . LEU A 53  ? 0.1276 0.1862 0.1550 0.0012  0.0021  -0.0213 54  LEU A CB  
336  C CG  . LEU A 53  ? 0.1427 0.1974 0.1689 0.0033  0.0025  -0.0211 54  LEU A CG  
337  C CD1 . LEU A 53  ? 0.1548 0.2060 0.1786 0.0039  0.0013  -0.0200 54  LEU A CD1 
338  C CD2 . LEU A 53  ? 0.1507 0.2032 0.1741 0.0022  0.0043  -0.0216 54  LEU A CD2 
339  N N   . MET A 54  ? 0.1027 0.1721 0.1429 0.0052  0.0005  -0.0216 55  MET A N   
340  C CA  . MET A 54  ? 0.1082 0.1799 0.1549 0.0083  0.0004  -0.0224 55  MET A CA  
341  C C   . MET A 54  ? 0.1018 0.1769 0.1543 0.0099  -0.0026 -0.0201 55  MET A C   
342  O O   . MET A 54  ? 0.1041 0.1787 0.1620 0.0128  -0.0036 -0.0195 55  MET A O   
343  C CB  . MET A 54  ? 0.1324 0.2089 0.1821 0.0078  0.0028  -0.0252 55  MET A CB  
344  C CG  . MET A 54  ? 0.1863 0.2603 0.2303 0.0059  0.0054  -0.0266 55  MET A CG  
345  S SD  . MET A 54  ? 0.3229 0.3909 0.3642 0.0077  0.0059  -0.0273 55  MET A SD  
346  C CE  . MET A 54  ? 0.3343 0.4077 0.3819 0.0095  0.0081  -0.0316 55  MET A CE  
347  N N   . LEU A 55  ? 0.0941 0.1729 0.1458 0.0078  -0.0040 -0.0187 56  LEU A N   
348  C CA  . LEU A 55  ? 0.0933 0.1764 0.1494 0.0085  -0.0072 -0.0158 56  LEU A CA  
349  C C   . LEU A 55  ? 0.1146 0.1938 0.1680 0.0091  -0.0094 -0.0126 56  LEU A C   
350  O O   . LEU A 55  ? 0.1198 0.1999 0.1789 0.0113  -0.0117 -0.0099 56  LEU A O   
351  C CB  . LEU A 55  ? 0.0785 0.1670 0.1331 0.0053  -0.0080 -0.0156 56  LEU A CB  
352  C CG  . LEU A 55  ? 0.0773 0.1717 0.1352 0.0050  -0.0116 -0.0123 56  LEU A CG  
353  C CD1 . LEU A 55  ? 0.0806 0.1789 0.1488 0.0086  -0.0133 -0.0108 56  LEU A CD1 
354  C CD2 . LEU A 55  ? 0.0762 0.1761 0.1322 0.0013  -0.0119 -0.0132 56  LEU A CD2 
355  N N   . MET A 56  ? 0.1152 0.1900 0.1607 0.0070  -0.0084 -0.0130 57  MET A N   
356  C CA  . MET A 56  ? 0.1207 0.1924 0.1629 0.0070  -0.0099 -0.0106 57  MET A CA  
357  C C   . MET A 56  ? 0.1304 0.1971 0.1751 0.0099  -0.0096 -0.0102 57  MET A C   
358  O O   . MET A 56  ? 0.1389 0.2046 0.1846 0.0106  -0.0116 -0.0071 57  MET A O   
359  C CB  . MET A 56  ? 0.1373 0.2061 0.1715 0.0042  -0.0084 -0.0121 57  MET A CB  
360  C CG  . MET A 56  ? 0.1798 0.2536 0.2115 0.0010  -0.0094 -0.0123 57  MET A CG  
361  S SD  . MET A 56  ? 0.2954 0.3766 0.3292 0.0002  -0.0135 -0.0079 57  MET A SD  
362  C CE  . MET A 56  ? 0.2483 0.3255 0.2788 0.0008  -0.0141 -0.0054 57  MET A CE  
363  N N   . LYS A 57  ? 0.1243 0.1886 0.1701 0.0111  -0.0071 -0.0134 58  LYS A N   
364  C CA  . LYS A 57  ? 0.1287 0.1890 0.1774 0.0136  -0.0065 -0.0141 58  LYS A CA  
365  C C   . LYS A 57  ? 0.1216 0.1839 0.1796 0.0163  -0.0086 -0.0125 58  LYS A C   
366  O O   . LYS A 57  ? 0.1280 0.1868 0.1886 0.0178  -0.0099 -0.0107 58  LYS A O   
367  C CB  . LYS A 57  ? 0.1683 0.2272 0.2154 0.0136  -0.0034 -0.0181 58  LYS A CB  
368  C CG  . LYS A 57  ? 0.2450 0.2985 0.2903 0.0145  -0.0026 -0.0189 58  LYS A CG  
369  C CD  . LYS A 57  ? 0.3335 0.3874 0.3837 0.0164  -0.0010 -0.0223 58  LYS A CD  
370  C CE  . LYS A 57  ? 0.4116 0.4661 0.4710 0.0192  -0.0028 -0.0218 58  LYS A CE  
371  N NZ  . LYS A 57  ? 0.4615 0.5213 0.5277 0.0204  -0.0016 -0.0248 58  LYS A NZ  
372  N N   . ASN A 58  ? 0.1145 0.1824 0.1784 0.0170  -0.0090 -0.0130 59  ASN A N   
373  C CA  . ASN A 58  ? 0.1201 0.1903 0.1945 0.0200  -0.0112 -0.0114 59  ASN A CA  
374  C C   . ASN A 58  ? 0.1248 0.1963 0.2003 0.0196  -0.0153 -0.0053 59  ASN A C   
375  O O   . ASN A 58  ? 0.1260 0.1959 0.2087 0.0219  -0.0177 -0.0025 59  ASN A O   
376  C CB  . ASN A 58  ? 0.1398 0.2167 0.2207 0.0208  -0.0105 -0.0137 59  ASN A CB  
377  C CG  . ASN A 58  ? 0.1849 0.2618 0.2669 0.0215  -0.0066 -0.0195 59  ASN A CG  
378  O OD1 . ASN A 58  ? 0.2133 0.2858 0.2956 0.0228  -0.0050 -0.0220 59  ASN A OD1 
379  N ND2 . ASN A 58  ? 0.1924 0.2751 0.2749 0.0203  -0.0049 -0.0218 59  ASN A ND2 
380  N N   . HIS A 59  ? 0.1307 0.2051 0.1991 0.0163  -0.0163 -0.0034 60  HIS A N   
381  C CA  . HIS A 59  ? 0.1363 0.2131 0.2032 0.0147  -0.0199 0.0022  60  HIS A CA  
382  C C   . HIS A 59  ? 0.1469 0.2179 0.2115 0.0150  -0.0204 0.0046  60  HIS A C   
383  O O   . HIS A 59  ? 0.1461 0.2176 0.2146 0.0155  -0.0237 0.0097  60  HIS A O   
384  C CB  . HIS A 59  ? 0.1386 0.2192 0.1968 0.0107  -0.0194 0.0016  60  HIS A CB  
385  C CG  . HIS A 59  ? 0.1710 0.2555 0.2260 0.0082  -0.0227 0.0065  60  HIS A CG  
386  N ND1 . HIS A 59  ? 0.2001 0.2924 0.2594 0.0075  -0.0262 0.0104  60  HIS A ND1 
387  C CD2 . HIS A 59  ? 0.1852 0.2680 0.2333 0.0060  -0.0228 0.0081  60  HIS A CD2 
388  C CE1 . HIS A 59  ? 0.2047 0.2997 0.2590 0.0047  -0.0285 0.0144  60  HIS A CE1 
389  N NE2 . HIS A 59  ? 0.1995 0.2891 0.2470 0.0037  -0.0264 0.0130  60  HIS A NE2 
390  N N   . LEU A 60  ? 0.1591 0.2247 0.2175 0.0144  -0.0174 0.0011  61  LEU A N   
391  C CA  . LEU A 60  ? 0.1697 0.2300 0.2253 0.0143  -0.0175 0.0026  61  LEU A CA  
392  C C   . LEU A 60  ? 0.1805 0.2364 0.2445 0.0175  -0.0181 0.0030  61  LEU A C   
393  O O   . LEU A 60  ? 0.1911 0.2446 0.2567 0.0175  -0.0202 0.0070  61  LEU A O   
394  C CB  . LEU A 60  ? 0.1731 0.2298 0.2205 0.0129  -0.0142 -0.0015 61  LEU A CB  
395  C CG  . LEU A 60  ? 0.1947 0.2466 0.2385 0.0125  -0.0138 -0.0006 61  LEU A CG  
396  C CD1 . LEU A 60  ? 0.1964 0.2509 0.2373 0.0102  -0.0162 0.0042  61  LEU A CD1 
397  C CD2 . LEU A 60  ? 0.1965 0.2453 0.2340 0.0117  -0.0106 -0.0047 61  LEU A CD2 
398  N N   . ASP A 61  ? 0.1773 0.2325 0.2470 0.0200  -0.0163 -0.0013 62  ASP A N   
399  C CA  . ASP A 61  ? 0.1933 0.2448 0.2722 0.0232  -0.0165 -0.0025 62  ASP A CA  
400  C C   . ASP A 61  ? 0.1993 0.2528 0.2887 0.0251  -0.0205 0.0026  62  ASP A C   
401  O O   . ASP A 61  ? 0.1973 0.2465 0.2939 0.0269  -0.0220 0.0043  62  ASP A O   
402  C CB  . ASP A 61  ? 0.2448 0.2977 0.3270 0.0248  -0.0133 -0.0089 62  ASP A CB  
403  C CG  . ASP A 61  ? 0.3909 0.4390 0.4753 0.0263  -0.0111 -0.0134 62  ASP A CG  
404  O OD1 . ASP A 61  ? 0.4351 0.4784 0.5241 0.0274  -0.0127 -0.0116 62  ASP A OD1 
405  O OD2 . ASP A 61  ? 0.4352 0.4843 0.5166 0.0259  -0.0077 -0.0188 62  ASP A OD2 
406  N N   . ARG A 62  ? 0.1956 0.2557 0.2866 0.0246  -0.0223 0.0050  63  ARG A N   
407  C CA  . ARG A 62  ? 0.2030 0.2663 0.3039 0.0262  -0.0265 0.0106  63  ARG A CA  
408  C C   . ARG A 62  ? 0.2083 0.2705 0.3061 0.0240  -0.0300 0.0180  63  ARG A C   
409  O O   . ARG A 62  ? 0.2182 0.2784 0.3250 0.0257  -0.0333 0.0228  63  ARG A O   
410  C CB  . ARG A 62  ? 0.2214 0.2932 0.3234 0.0255  -0.0275 0.0111  63  ARG A CB  
411  C CG  . ARG A 62  ? 0.2653 0.3414 0.3792 0.0277  -0.0320 0.0168  63  ARG A CG  
412  C CD  . ARG A 62  ? 0.3227 0.4070 0.4399 0.0278  -0.0321 0.0152  63  ARG A CD  
413  N NE  . ARG A 62  ? 0.3644 0.4522 0.4967 0.0314  -0.0354 0.0184  63  ARG A NE  
414  C CZ  . ARG A 62  ? 0.3702 0.4661 0.5085 0.0322  -0.0364 0.0183  63  ARG A CZ  
415  N NH1 . ARG A 62  ? 0.3378 0.4390 0.4679 0.0292  -0.0343 0.0150  63  ARG A NH1 
416  N NH2 . ARG A 62  ? 0.3718 0.4706 0.5251 0.0358  -0.0397 0.0214  63  ARG A NH2 
417  N N   . ALA A 63  ? 0.1971 0.2608 0.2827 0.0202  -0.0293 0.0187  64  ALA A N   
418  C CA  . ALA A 63  ? 0.1941 0.2580 0.2753 0.0174  -0.0319 0.0251  64  ALA A CA  
419  C C   . ALA A 63  ? 0.2052 0.2612 0.2868 0.0180  -0.0312 0.0253  64  ALA A C   
420  O O   . ALA A 63  ? 0.2054 0.2607 0.2894 0.0170  -0.0344 0.0317  64  ALA A O   
421  C CB  . ALA A 63  ? 0.1854 0.2538 0.2542 0.0132  -0.0308 0.0244  64  ALA A CB  
422  N N   . ALA A 64  ? 0.2100 0.2605 0.2899 0.0193  -0.0273 0.0186  65  ALA A N   
423  C CA  . ALA A 64  ? 0.2304 0.2738 0.3110 0.0197  -0.0266 0.0180  65  ALA A CA  
424  C C   . ALA A 64  ? 0.2549 0.2941 0.3489 0.0230  -0.0286 0.0195  65  ALA A C   
425  O O   . ALA A 64  ? 0.2600 0.2943 0.3568 0.0227  -0.0300 0.0225  65  ALA A O   
426  C CB  . ALA A 64  ? 0.2314 0.2715 0.3063 0.0199  -0.0222 0.0107  65  ALA A CB  
427  N N   . LYS A 65  ? 0.2662 0.3073 0.3690 0.0261  -0.0287 0.0171  66  LYS A N   
428  C CA  . LYS A 65  ? 0.2913 0.3287 0.4086 0.0296  -0.0307 0.0181  66  LYS A CA  
429  C C   . LYS A 65  ? 0.3105 0.3495 0.4341 0.0291  -0.0362 0.0279  66  LYS A C   
430  O O   . LYS A 65  ? 0.3125 0.3463 0.4468 0.0310  -0.0385 0.0308  66  LYS A O   
431  C CB  . LYS A 65  ? 0.3162 0.3561 0.4419 0.0331  -0.0289 0.0121  66  LYS A CB  
432  C CG  . LYS A 65  ? 0.3844 0.4215 0.5063 0.0336  -0.0239 0.0029  66  LYS A CG  
433  C CD  . LYS A 65  ? 0.4488 0.4900 0.5769 0.0362  -0.0215 -0.0035 66  LYS A CD  
434  C CE  . LYS A 65  ? 0.5088 0.5480 0.6319 0.0358  -0.0167 -0.0119 66  LYS A CE  
435  N NZ  . LYS A 65  ? 0.5458 0.5907 0.6724 0.0373  -0.0138 -0.0182 66  LYS A NZ  
436  N N   . LYS A 66  ? 0.3275 0.3735 0.4442 0.0262  -0.0383 0.0332  67  LYS A N   
437  C CA  . LYS A 66  ? 0.3578 0.4067 0.4786 0.0249  -0.0436 0.0433  67  LYS A CA  
438  C C   . LYS A 66  ? 0.3897 0.4347 0.5053 0.0217  -0.0446 0.0480  67  LYS A C   
439  O O   . LYS A 66  ? 0.3981 0.4397 0.5228 0.0223  -0.0483 0.0544  67  LYS A O   
440  C CB  . LYS A 66  ? 0.3847 0.4436 0.4991 0.0222  -0.0454 0.0467  67  LYS A CB  
441  C CG  . LYS A 66  ? 0.4521 0.5159 0.5783 0.0240  -0.0505 0.0535  67  LYS A CG  
442  C CD  . LYS A 66  ? 0.5236 0.5960 0.6487 0.0241  -0.0502 0.0511  67  LYS A CD  
443  C CE  . LYS A 66  ? 0.5766 0.6466 0.7055 0.0277  -0.0457 0.0413  67  LYS A CE  
444  N NZ  . LYS A 66  ? 0.6010 0.6796 0.7314 0.0280  -0.0459 0.0397  67  LYS A NZ  
445  N N   . VAL A 67  ? 0.4084 0.4535 0.5106 0.0186  -0.0414 0.0447  68  VAL A N   
446  C CA  . VAL A 67  ? 0.4380 0.4804 0.5349 0.0153  -0.0419 0.0487  68  VAL A CA  
447  C C   . VAL A 67  ? 0.4721 0.5049 0.5760 0.0173  -0.0410 0.0464  68  VAL A C   
448  O O   . VAL A 67  ? 0.4814 0.5114 0.5868 0.0153  -0.0431 0.0521  68  VAL A O   
449  C CB  . VAL A 67  ? 0.4447 0.4910 0.5264 0.0113  -0.0389 0.0462  68  VAL A CB  
450  C CG1 . VAL A 67  ? 0.4485 0.5034 0.5235 0.0097  -0.0387 0.0455  68  VAL A CG1 
451  C CG2 . VAL A 67  ? 0.4475 0.4881 0.5247 0.0123  -0.0341 0.0378  68  VAL A CG2 
452  N N   . ASP A 68  ? 0.4888 0.5172 0.5970 0.0208  -0.0378 0.0381  69  ASP A N   
453  C CA  . ASP A 68  ? 0.5144 0.5342 0.6294 0.0225  -0.0368 0.0348  69  ASP A CA  
454  C C   . ASP A 68  ? 0.5330 0.5498 0.6624 0.0272  -0.0372 0.0314  69  ASP A C   
455  O O   . ASP A 68  ? 0.5335 0.5517 0.6628 0.0294  -0.0339 0.0237  69  ASP A O   
456  C CB  . ASP A 68  ? 0.5472 0.5647 0.6528 0.0215  -0.0321 0.0270  69  ASP A CB  
457  C CG  . ASP A 68  ? 0.6213 0.6307 0.7326 0.0224  -0.0311 0.0235  69  ASP A CG  
458  O OD1 . ASP A 68  ? 0.6351 0.6403 0.7544 0.0222  -0.0342 0.0290  69  ASP A OD1 
459  O OD2 . ASP A 68  ? 0.6488 0.6565 0.7568 0.0232  -0.0273 0.0156  69  ASP A OD2 
460  N N   . LYS A 69  ? 0.5407 0.5535 0.6831 0.0287  -0.0412 0.0372  70  LYS A N   
461  C CA  . LYS A 69  ? 0.5497 0.5596 0.7079 0.0335  -0.0417 0.0339  70  LYS A CA  
462  C C   . LYS A 69  ? 0.5588 0.5618 0.7217 0.0356  -0.0379 0.0240  70  LYS A C   
463  O O   . LYS A 69  ? 0.5586 0.5606 0.7326 0.0395  -0.0367 0.0181  70  LYS A O   
464  C CB  . LYS A 69  ? 0.5723 0.5803 0.7442 0.0346  -0.0475 0.0437  70  LYS A CB  
465  C CG  . LYS A 69  ? 0.6153 0.6320 0.7832 0.0325  -0.0515 0.0530  70  LYS A CG  
466  N N   . GLU A 70  ? 0.5621 0.5613 0.7162 0.0327  -0.0357 0.0217  71  GLU A N   
467  C CA  . GLU A 70  ? 0.5648 0.5587 0.7206 0.0337  -0.0319 0.0120  71  GLU A CA  
468  C C   . GLU A 70  ? 0.5519 0.5509 0.6997 0.0344  -0.0272 0.0029  71  GLU A C   
469  O O   . GLU A 70  ? 0.5568 0.5534 0.7076 0.0357  -0.0240 -0.0058 71  GLU A O   
470  C CB  . GLU A 70  ? 0.6081 0.5976 0.7567 0.0301  -0.0315 0.0132  71  GLU A CB  
471  C CG  . GLU A 70  ? 0.6973 0.6793 0.8573 0.0298  -0.0350 0.0186  71  GLU A CG  
472  C CD  . GLU A 70  ? 0.8065 0.7901 0.9637 0.0267  -0.0393 0.0306  71  GLU A CD  
473  O OE1 . GLU A 70  ? 0.8208 0.8102 0.9773 0.0269  -0.0417 0.0366  71  GLU A OE1 
474  O OE2 . GLU A 70  ? 0.8490 0.8285 1.0046 0.0236  -0.0402 0.0340  71  GLU A OE2 
475  N N   . ASN A 71  ? 0.5346 0.5405 0.6721 0.0331  -0.0267 0.0049  72  ASN A N   
476  C CA  . ASN A 71  ? 0.5205 0.5316 0.6498 0.0331  -0.0227 -0.0019 72  ASN A CA  
477  C C   . ASN A 71  ? 0.4820 0.4913 0.6004 0.0306  -0.0193 -0.0070 72  ASN A C   
478  O O   . ASN A 71  ? 0.4785 0.4896 0.5943 0.0311  -0.0158 -0.0145 72  ASN A O   
479  C CB  . ASN A 71  ? 0.5553 0.5684 0.6949 0.0368  -0.0210 -0.0084 72  ASN A CB  
480  C CG  . ASN A 71  ? 0.6274 0.6437 0.7772 0.0392  -0.0245 -0.0032 72  ASN A CG  
481  O OD1 . ASN A 71  ? 0.6571 0.6742 0.8066 0.0380  -0.0285 0.0058  72  ASN A OD1 
482  N ND2 . ASN A 71  ? 0.6363 0.6556 0.7956 0.0426  -0.0230 -0.0086 72  ASN A ND2 
483  N N   . LYS A 72  ? 0.4487 0.4555 0.5608 0.0277  -0.0206 -0.0023 73  LYS A N   
484  C CA  . LYS A 72  ? 0.4201 0.4254 0.5225 0.0253  -0.0180 -0.0059 73  LYS A CA  
485  C C   . LYS A 72  ? 0.3740 0.3843 0.4629 0.0230  -0.0165 -0.0050 73  LYS A C   
486  O O   . LYS A 72  ? 0.3795 0.3893 0.4610 0.0213  -0.0145 -0.0078 73  LYS A O   
487  C CB  . LYS A 72  ? 0.4509 0.4508 0.5552 0.0235  -0.0197 -0.0024 73  LYS A CB  
488  C CG  . LYS A 72  ? 0.5125 0.5063 0.6310 0.0255  -0.0216 -0.0027 73  LYS A CG  
489  C CD  . LYS A 72  ? 0.5791 0.5707 0.7025 0.0273  -0.0185 -0.0125 73  LYS A CD  
490  C CE  . LYS A 72  ? 0.6382 0.6228 0.7762 0.0290  -0.0203 -0.0133 73  LYS A CE  
491  N NZ  . LYS A 72  ? 0.6714 0.6508 0.8097 0.0262  -0.0227 -0.0075 73  LYS A NZ  
492  N N   . ILE A 73  ? 0.3272 0.3424 0.4136 0.0228  -0.0177 -0.0010 74  ILE A N   
493  C CA  . ILE A 73  ? 0.2896 0.3092 0.3645 0.0207  -0.0163 -0.0009 74  ILE A CA  
494  C C   . ILE A 73  ? 0.2724 0.2939 0.3442 0.0215  -0.0129 -0.0077 74  ILE A C   
495  O O   . ILE A 73  ? 0.2728 0.2964 0.3500 0.0235  -0.0124 -0.0102 74  ILE A O   
496  C CB  . ILE A 73  ? 0.2727 0.2977 0.3461 0.0199  -0.0184 0.0043  74  ILE A CB  
497  C CG1 . ILE A 73  ? 0.2762 0.3009 0.3527 0.0187  -0.0222 0.0122  74  ILE A CG1 
498  C CG2 . ILE A 73  ? 0.2693 0.2984 0.3317 0.0177  -0.0165 0.0032  74  ILE A CG2 
499  C CD1 . ILE A 73  ? 0.2838 0.3070 0.3556 0.0163  -0.0223 0.0146  74  ILE A CD1 
500  N N   . ILE A 74  ? 0.2551 0.2764 0.3186 0.0198  -0.0107 -0.0103 75  ILE A N   
501  C CA  . ILE A 74  ? 0.2439 0.2675 0.3035 0.0199  -0.0078 -0.0156 75  ILE A CA  
502  C C   . ILE A 74  ? 0.2137 0.2415 0.2667 0.0187  -0.0074 -0.0141 75  ILE A C   
503  O O   . ILE A 74  ? 0.1940 0.2222 0.2418 0.0171  -0.0082 -0.0108 75  ILE A O   
504  C CB  . ILE A 74  ? 0.2543 0.2757 0.3097 0.0189  -0.0060 -0.0191 75  ILE A CB  
505  C CG1 . ILE A 74  ? 0.2651 0.2829 0.3281 0.0201  -0.0061 -0.0222 75  ILE A CG1 
506  C CG2 . ILE A 74  ? 0.2570 0.2815 0.3069 0.0182  -0.0034 -0.0231 75  ILE A CG2 
507  C CD1 . ILE A 74  ? 0.2902 0.3045 0.3527 0.0189  -0.0072 -0.0201 75  ILE A CD1 
508  N N   . VAL A 75  ? 0.2071 0.2383 0.2614 0.0195  -0.0061 -0.0168 76  VAL A N   
509  C CA  . VAL A 75  ? 0.2018 0.2368 0.2510 0.0182  -0.0057 -0.0158 76  VAL A CA  
510  C C   . VAL A 75  ? 0.1996 0.2359 0.2441 0.0173  -0.0029 -0.0198 76  VAL A C   
511  O O   . VAL A 75  ? 0.2101 0.2472 0.2577 0.0182  -0.0013 -0.0237 76  VAL A O   
512  C CB  . VAL A 75  ? 0.1958 0.2346 0.2504 0.0192  -0.0074 -0.0136 76  VAL A CB  
513  C CG1 . VAL A 75  ? 0.2047 0.2478 0.2548 0.0176  -0.0065 -0.0140 76  VAL A CG1 
514  C CG2 . VAL A 75  ? 0.1898 0.2280 0.2469 0.0190  -0.0106 -0.0081 76  VAL A CG2 
515  N N   . ALA A 76  ? 0.1789 0.2155 0.2164 0.0154  -0.0022 -0.0189 77  ALA A N   
516  C CA  . ALA A 76  ? 0.1678 0.2053 0.2007 0.0142  -0.0001 -0.0213 77  ALA A CA  
517  C C   . ALA A 76  ? 0.1626 0.2024 0.1924 0.0127  0.0001  -0.0201 77  ALA A C   
518  O O   . ALA A 76  ? 0.1647 0.2048 0.1939 0.0122  -0.0013 -0.0177 77  ALA A O   
519  C CB  . ALA A 76  ? 0.1662 0.2007 0.1944 0.0133  0.0003  -0.0212 77  ALA A CB  
520  N N   . ARG A 77  ? 0.1544 0.1960 0.1820 0.0115  0.0018  -0.0218 78  ARG A N   
521  C CA  . ARG A 77  ? 0.1569 0.2001 0.1820 0.0098  0.0020  -0.0210 78  ARG A CA  
522  C C   . ARG A 77  ? 0.1515 0.1943 0.1728 0.0080  0.0036  -0.0216 78  ARG A C   
523  O O   . ARG A 77  ? 0.1524 0.1957 0.1732 0.0080  0.0047  -0.0230 78  ARG A O   
524  C CB  . ARG A 77  ? 0.1787 0.2263 0.2079 0.0099  0.0016  -0.0212 78  ARG A CB  
525  C CG  . ARG A 77  ? 0.2354 0.2869 0.2659 0.0091  0.0034  -0.0232 78  ARG A CG  
526  C CD  . ARG A 77  ? 0.3043 0.3579 0.3392 0.0108  0.0044  -0.0259 78  ARG A CD  
527  N NE  . ARG A 77  ? 0.3921 0.4490 0.4253 0.0091  0.0067  -0.0281 78  ARG A NE  
528  C CZ  . ARG A 77  ? 0.4537 0.5142 0.4901 0.0098  0.0084  -0.0315 78  ARG A CZ  
529  N NH1 . ARG A 77  ? 0.4585 0.5189 0.5011 0.0125  0.0080  -0.0334 78  ARG A NH1 
530  N NH2 . ARG A 77  ? 0.4672 0.5316 0.5009 0.0075  0.0106  -0.0331 78  ARG A NH2 
531  N N   . ARG A 78  ? 0.1483 0.1903 0.1670 0.0063  0.0037  -0.0206 79  ARG A N   
532  C CA  . ARG A 78  ? 0.1528 0.1941 0.1688 0.0045  0.0047  -0.0202 79  ARG A CA  
533  C C   . ARG A 78  ? 0.1658 0.2068 0.1812 0.0026  0.0048  -0.0195 79  ARG A C   
534  O O   . ARG A 78  ? 0.1763 0.2158 0.1916 0.0025  0.0040  -0.0194 79  ARG A O   
535  C CB  . ARG A 78  ? 0.1564 0.1942 0.1697 0.0049  0.0045  -0.0193 79  ARG A CB  
536  C CG  . ARG A 78  ? 0.1942 0.2286 0.2054 0.0037  0.0043  -0.0176 79  ARG A CG  
537  C CD  . ARG A 78  ? 0.2049 0.2373 0.2167 0.0045  0.0036  -0.0177 79  ARG A CD  
538  N NE  . ARG A 78  ? 0.2088 0.2381 0.2202 0.0037  0.0035  -0.0172 79  ARG A NE  
539  C CZ  . ARG A 78  ? 0.1927 0.2216 0.2048 0.0030  0.0035  -0.0182 79  ARG A CZ  
540  N NH1 . ARG A 78  ? 0.1303 0.1624 0.1431 0.0025  0.0034  -0.0191 79  ARG A NH1 
541  N NH2 . ARG A 78  ? 0.2156 0.2415 0.2284 0.0027  0.0037  -0.0185 79  ARG A NH2 
542  N N   . LEU A 79  ? 0.1712 0.2141 0.1862 0.0006  0.0058  -0.0193 80  LEU A N   
543  C CA  . LEU A 79  ? 0.1812 0.2232 0.1961 -0.0017 0.0059  -0.0186 80  LEU A CA  
544  C C   . LEU A 79  ? 0.1896 0.2269 0.2025 -0.0023 0.0058  -0.0167 80  LEU A C   
545  O O   . LEU A 79  ? 0.1960 0.2336 0.2073 -0.0024 0.0060  -0.0155 80  LEU A O   
546  C CB  . LEU A 79  ? 0.1767 0.2234 0.1927 -0.0038 0.0070  -0.0188 80  LEU A CB  
547  C CG  . LEU A 79  ? 0.1929 0.2390 0.2097 -0.0066 0.0071  -0.0182 80  LEU A CG  
548  C CD1 . LEU A 79  ? 0.2049 0.2507 0.2231 -0.0063 0.0061  -0.0196 80  LEU A CD1 
549  C CD2 . LEU A 79  ? 0.1964 0.2479 0.2144 -0.0090 0.0083  -0.0182 80  LEU A CD2 
550  N N   . LYS A 80  ? 0.1884 0.2218 0.2018 -0.0026 0.0052  -0.0166 81  LYS A N   
551  C CA  . LYS A 80  ? 0.2016 0.2303 0.2149 -0.0027 0.0049  -0.0150 81  LYS A CA  
552  C C   . LYS A 80  ? 0.2221 0.2505 0.2354 -0.0052 0.0051  -0.0124 81  LYS A C   
553  O O   . LYS A 80  ? 0.2270 0.2567 0.2414 -0.0073 0.0055  -0.0125 81  LYS A O   
554  C CB  . LYS A 80  ? 0.2182 0.2435 0.2332 -0.0027 0.0046  -0.0166 81  LYS A CB  
555  C CG  . LYS A 80  ? 0.2504 0.2714 0.2664 -0.0014 0.0042  -0.0160 81  LYS A CG  
556  C CD  . LYS A 80  ? 0.2733 0.2914 0.2919 -0.0017 0.0045  -0.0185 81  LYS A CD  
557  C CE  . LYS A 80  ? 0.2901 0.3054 0.3101 0.0003  0.0043  -0.0189 81  LYS A CE  
558  N NZ  . LYS A 80  ? 0.3014 0.3195 0.3188 0.0021  0.0042  -0.0195 81  LYS A NZ  
559  N N   . ARG A 81  ? 0.2341 0.2615 0.2462 -0.0052 0.0046  -0.0096 82  ARG A N   
560  C CA  . ARG A 81  ? 0.2615 0.2892 0.2732 -0.0079 0.0045  -0.0060 82  ARG A CA  
561  C C   . ARG A 81  ? 0.2577 0.2807 0.2728 -0.0097 0.0040  -0.0044 82  ARG A C   
562  O O   . ARG A 81  ? 0.2478 0.2661 0.2657 -0.0082 0.0035  -0.0057 82  ARG A O   
563  C CB  . ARG A 81  ? 0.3161 0.3437 0.3260 -0.0074 0.0035  -0.0031 82  ARG A CB  
564  C CG  . ARG A 81  ? 0.4072 0.4411 0.4134 -0.0078 0.0043  -0.0037 82  ARG A CG  
565  C CD  . ARG A 81  ? 0.4956 0.5297 0.5001 -0.0060 0.0035  -0.0037 82  ARG A CD  
566  N NE  . ARG A 81  ? 0.5815 0.6113 0.5875 -0.0055 0.0017  -0.0003 82  ARG A NE  
567  C CZ  . ARG A 81  ? 0.6327 0.6640 0.6373 -0.0071 0.0005  0.0039  82  ARG A CZ  
568  N NH1 . ARG A 81  ? 0.6392 0.6766 0.6401 -0.0099 0.0010  0.0050  82  ARG A NH1 
569  N NH2 . ARG A 81  ? 0.6288 0.6561 0.6360 -0.0062 -0.0014 0.0071  82  ARG A NH2 
570  N N   . LEU A 82  ? 0.2703 0.2947 0.2856 -0.0130 0.0042  -0.0016 83  LEU A N   
571  C CA  . LEU A 82  ? 0.2844 0.3039 0.3038 -0.0151 0.0036  0.0003  83  LEU A CA  
572  C C   . LEU A 82  ? 0.3046 0.3178 0.3270 -0.0139 0.0019  0.0033  83  LEU A C   
573  O O   . LEU A 82  ? 0.3088 0.3164 0.3358 -0.0130 0.0016  0.0016  83  LEU A O   
574  C CB  . LEU A 82  ? 0.2856 0.3082 0.3044 -0.0193 0.0039  0.0036  83  LEU A CB  
575  C CG  . LEU A 82  ? 0.3063 0.3236 0.3301 -0.0220 0.0033  0.0055  83  LEU A CG  
576  C CD1 . LEU A 82  ? 0.3044 0.3195 0.3311 -0.0215 0.0040  0.0001  83  LEU A CD1 
577  C CD2 . LEU A 82  ? 0.3146 0.3359 0.3375 -0.0267 0.0037  0.0096  83  LEU A CD2 
578  N N   . SER A 83  ? 0.3121 0.3269 0.3324 -0.0136 0.0009  0.0072  84  SER A N   
579  C CA  . SER A 83  ? 0.3337 0.3436 0.3575 -0.0122 -0.0010 0.0106  84  SER A CA  
580  C C   . SER A 83  ? 0.3401 0.3461 0.3668 -0.0083 -0.0009 0.0064  84  SER A C   
581  O O   . SER A 83  ? 0.3464 0.3467 0.3789 -0.0072 -0.0019 0.0072  84  SER A O   
582  C CB  . SER A 83  ? 0.3619 0.3762 0.3818 -0.0127 -0.0022 0.0149  84  SER A CB  
583  O OG  . SER A 83  ? 0.4015 0.4194 0.4176 -0.0103 -0.0014 0.0112  84  SER A OG  
584  N N   . THR A 84  ? 0.3314 0.3408 0.3545 -0.0063 0.0003  0.0020  85  THR A N   
585  C CA  . THR A 84  ? 0.3292 0.3366 0.3541 -0.0032 0.0006  -0.0021 85  THR A CA  
586  C C   . THR A 84  ? 0.3359 0.3396 0.3648 -0.0036 0.0015  -0.0057 85  THR A C   
587  O O   . THR A 84  ? 0.3376 0.3375 0.3711 -0.0019 0.0014  -0.0075 85  THR A O   
588  C CB  . THR A 84  ? 0.3375 0.3496 0.3576 -0.0019 0.0016  -0.0052 85  THR A CB  
589  O OG1 . THR A 84  ? 0.3564 0.3724 0.3729 -0.0022 0.0011  -0.0027 85  THR A OG1 
590  C CG2 . THR A 84  ? 0.3339 0.3449 0.3552 0.0008  0.0018  -0.0085 85  THR A CG2 
591  N N   . ILE A 85  ? 0.3378 0.3432 0.3655 -0.0059 0.0024  -0.0073 86  ILE A N   
592  C CA  . ILE A 85  ? 0.3485 0.3514 0.3797 -0.0069 0.0031  -0.0111 86  ILE A CA  
593  C C   . ILE A 85  ? 0.3658 0.3620 0.4036 -0.0077 0.0023  -0.0093 86  ILE A C   
594  O O   . ILE A 85  ? 0.3667 0.3591 0.4092 -0.0066 0.0028  -0.0130 86  ILE A O   
595  C CB  . ILE A 85  ? 0.3453 0.3521 0.3742 -0.0096 0.0039  -0.0123 86  ILE A CB  
596  C CG1 . ILE A 85  ? 0.3497 0.3628 0.3737 -0.0084 0.0045  -0.0142 86  ILE A CG1 
597  C CG2 . ILE A 85  ? 0.3444 0.3487 0.3771 -0.0114 0.0045  -0.0163 86  ILE A CG2 
598  C CD1 . ILE A 85  ? 0.3580 0.3761 0.3804 -0.0107 0.0050  -0.0143 86  ILE A CD1 
599  N N   . ILE A 86  ? 0.3816 0.3767 0.4203 -0.0097 0.0012  -0.0036 87  ILE A N   
600  C CA  . ILE A 86  ? 0.4101 0.3985 0.4559 -0.0107 -0.0001 -0.0004 87  ILE A CA  
601  C C   . ILE A 86  ? 0.4389 0.4231 0.4897 -0.0071 -0.0010 -0.0004 87  ILE A C   
602  O O   . ILE A 86  ? 0.4415 0.4199 0.4999 -0.0064 -0.0010 -0.0027 87  ILE A O   
603  C CB  . ILE A 86  ? 0.4156 0.4049 0.4603 -0.0139 -0.0014 0.0070  87  ILE A CB  
604  C CG1 . ILE A 86  ? 0.4179 0.4113 0.4591 -0.0176 -0.0002 0.0064  87  ILE A CG1 
605  C CG2 . ILE A 86  ? 0.4257 0.4077 0.4786 -0.0147 -0.0034 0.0118  87  ILE A CG2 
606  C CD1 . ILE A 86  ? 0.4328 0.4225 0.4788 -0.0193 0.0006  0.0020  87  ILE A CD1 
607  N N   . ASP A 87  ? 0.4565 0.4442 0.5036 -0.0048 -0.0015 0.0013  88  ASP A N   
608  C CA  . ASP A 87  ? 0.4795 0.4646 0.5314 -0.0015 -0.0024 0.0013  88  ASP A CA  
609  C C   . ASP A 87  ? 0.4852 0.4692 0.5399 0.0008  -0.0006 -0.0061 88  ASP A C   
610  O O   . ASP A 87  ? 0.4922 0.4721 0.5545 0.0029  -0.0008 -0.0075 88  ASP A O   
611  C CB  . ASP A 87  ? 0.5245 0.5146 0.5711 0.0000  -0.0033 0.0042  88  ASP A CB  
612  C CG  . ASP A 87  ? 0.6347 0.6258 0.6805 -0.0017 -0.0056 0.0120  88  ASP A CG  
613  O OD1 . ASP A 87  ? 0.6585 0.6457 0.7091 -0.0036 -0.0070 0.0162  88  ASP A OD1 
614  O OD2 . ASP A 87  ? 0.6767 0.6729 0.7171 -0.0014 -0.0062 0.0139  88  ASP A OD2 
615  N N   . LYS A 88  ? 0.4805 0.4689 0.5295 0.0003  0.0012  -0.0108 89  LYS A N   
616  C CA  . LYS A 88  ? 0.4870 0.4762 0.5370 0.0016  0.0029  -0.0176 89  LYS A CA  
617  C C   . LYS A 88  ? 0.4982 0.4824 0.5553 0.0005  0.0038  -0.0216 89  LYS A C   
618  O O   . LYS A 88  ? 0.5033 0.4857 0.5659 0.0023  0.0047  -0.0261 89  LYS A O   
619  C CB  . LYS A 88  ? 0.5032 0.4985 0.5455 0.0006  0.0041  -0.0204 89  LYS A CB  
620  C CG  . LYS A 88  ? 0.5480 0.5465 0.5890 0.0023  0.0054  -0.0253 89  LYS A CG  
621  C CD  . LYS A 88  ? 0.6004 0.6049 0.6342 0.0015  0.0057  -0.0261 89  LYS A CD  
622  C CE  . LYS A 88  ? 0.6386 0.6468 0.6708 0.0030  0.0066  -0.0293 89  LYS A CE  
623  N NZ  . LYS A 88  ? 0.6623 0.6691 0.6969 0.0055  0.0062  -0.0276 89  LYS A NZ  
624  N N   . LEU A 89  ? 0.5011 0.4833 0.5587 -0.0025 0.0034  -0.0202 90  LEU A N   
625  C CA  . LEU A 89  ? 0.5168 0.4938 0.5817 -0.0041 0.0041  -0.0240 90  LEU A CA  
626  C C   . LEU A 89  ? 0.5445 0.5139 0.6199 -0.0025 0.0029  -0.0220 90  LEU A C   
627  O O   . LEU A 89  ? 0.5496 0.5148 0.6325 -0.0023 0.0040  -0.0275 90  LEU A O   
628  C CB  . LEU A 89  ? 0.5115 0.4885 0.5745 -0.0081 0.0039  -0.0225 90  LEU A CB  
629  C CG  . LEU A 89  ? 0.5181 0.5022 0.5733 -0.0099 0.0051  -0.0257 90  LEU A CG  
630  C CD1 . LEU A 89  ? 0.5205 0.5061 0.5732 -0.0134 0.0045  -0.0219 90  LEU A CD1 
631  C CD2 . LEU A 89  ? 0.5207 0.5057 0.5774 -0.0106 0.0068  -0.0339 90  LEU A CD2 
632  N N   . GLU A 90  ? 0.5610 0.5289 0.6375 -0.0014 0.0007  -0.0145 91  GLU A N   
633  C CA  . GLU A 90  ? 0.5858 0.5465 0.6731 0.0002  -0.0010 -0.0113 91  GLU A CA  
634  C C   . GLU A 90  ? 0.6079 0.5691 0.6994 0.0046  -0.0013 -0.0118 91  GLU A C   
635  O O   . GLU A 90  ? 0.6168 0.5743 0.7151 0.0061  -0.0037 -0.0060 91  GLU A O   
636  C CB  . GLU A 90  ? 0.6147 0.5731 0.7026 -0.0022 -0.0037 -0.0017 91  GLU A CB  
637  C CG  . GLU A 90  ? 0.6713 0.6360 0.7505 -0.0022 -0.0051 0.0046  91  GLU A CG  
638  C CD  . GLU A 90  ? 0.7487 0.7134 0.8263 -0.0056 -0.0073 0.0135  91  GLU A CD  
639  O OE1 . GLU A 90  ? 0.7607 0.7204 0.8434 -0.0084 -0.0079 0.0153  91  GLU A OE1 
640  O OE2 . GLU A 90  ? 0.7785 0.7486 0.8496 -0.0059 -0.0085 0.0185  91  GLU A OE2 
641  N N   . ARG A 91  ? 0.6156 0.5814 0.7039 0.0064  0.0009  -0.0185 92  ARG A N   
642  C CA  . ARG A 91  ? 0.6253 0.5923 0.7179 0.0104  0.0009  -0.0196 92  ARG A CA  
643  C C   . ARG A 91  ? 0.6329 0.5977 0.7344 0.0123  0.0032  -0.0283 92  ARG A C   
644  O O   . ARG A 91  ? 0.6360 0.5997 0.7384 0.0103  0.0051  -0.0345 92  ARG A O   
645  C CB  . ARG A 91  ? 0.6384 0.6131 0.7210 0.0112  0.0013  -0.0191 92  ARG A CB  
646  C CG  . ARG A 91  ? 0.6734 0.6497 0.7519 0.0110  -0.0014 -0.0105 92  ARG A CG  
647  N N   . ALA A 102 ? 0.6231 0.6171 0.6995 0.0023  0.0173  -0.0699 103 ALA A N   
648  C CA  . ALA A 102 ? 0.6308 0.6198 0.7078 -0.0002 0.0159  -0.0675 103 ALA A CA  
649  C C   . ALA A 102 ? 0.6278 0.6230 0.6941 -0.0035 0.0155  -0.0664 103 ALA A C   
650  O O   . ALA A 102 ? 0.6370 0.6359 0.7018 -0.0066 0.0169  -0.0726 103 ALA A O   
651  C CB  . ALA A 102 ? 0.6377 0.6218 0.7242 -0.0015 0.0174  -0.0748 103 ALA A CB  
652  N N   . ILE A 103 ? 0.6071 0.6040 0.6667 -0.0030 0.0136  -0.0589 104 ILE A N   
653  C CA  . ILE A 103 ? 0.5909 0.5938 0.6417 -0.0055 0.0130  -0.0572 104 ILE A CA  
654  C C   . ILE A 103 ? 0.5657 0.5659 0.6174 -0.0086 0.0123  -0.0566 104 ILE A C   
655  O O   . ILE A 103 ? 0.5804 0.5741 0.6366 -0.0084 0.0112  -0.0525 104 ILE A O   
656  C CB  . ILE A 103 ? 0.5976 0.6026 0.6426 -0.0036 0.0114  -0.0501 104 ILE A CB  
657  N N   . ALA A 104 ? 0.5238 0.5295 0.5716 -0.0118 0.0128  -0.0604 105 ALA A N   
658  C CA  . ALA A 104 ? 0.4930 0.4972 0.5416 -0.0151 0.0121  -0.0598 105 ALA A CA  
659  C C   . ALA A 104 ? 0.4588 0.4665 0.5011 -0.0153 0.0104  -0.0531 105 ALA A C   
660  O O   . ALA A 104 ? 0.4529 0.4670 0.4893 -0.0144 0.0101  -0.0519 105 ALA A O   
661  C CB  . ALA A 104 ? 0.4917 0.5007 0.5393 -0.0187 0.0132  -0.0672 105 ALA A CB  
662  N N   . LEU A 105 ? 0.4315 0.4354 0.4758 -0.0165 0.0094  -0.0487 106 LEU A N   
663  C CA  . LEU A 105 ? 0.4082 0.4159 0.4475 -0.0167 0.0082  -0.0431 106 LEU A CA  
664  C C   . LEU A 105 ? 0.3825 0.3988 0.4166 -0.0185 0.0080  -0.0449 106 LEU A C   
665  O O   . LEU A 105 ? 0.3757 0.3966 0.4053 -0.0168 0.0073  -0.0418 106 LEU A O   
666  C CB  . LEU A 105 ? 0.4078 0.4111 0.4501 -0.0186 0.0076  -0.0388 106 LEU A CB  
667  C CG  . LEU A 105 ? 0.4190 0.4270 0.4570 -0.0191 0.0068  -0.0337 106 LEU A CG  
668  C CD1 . LEU A 105 ? 0.4195 0.4284 0.4540 -0.0157 0.0063  -0.0296 106 LEU A CD1 
669  C CD2 . LEU A 105 ? 0.4248 0.4300 0.4658 -0.0222 0.0064  -0.0304 106 LEU A CD2 
670  N N   . THR A 106 ? 0.3687 0.3872 0.4039 -0.0217 0.0085  -0.0499 107 THR A N   
671  C CA  . THR A 106 ? 0.3663 0.3936 0.3971 -0.0236 0.0078  -0.0513 107 THR A CA  
672  C C   . THR A 106 ? 0.3649 0.3980 0.3916 -0.0225 0.0080  -0.0540 107 THR A C   
673  O O   . THR A 106 ? 0.3672 0.4081 0.3901 -0.0240 0.0071  -0.0542 107 THR A O   
674  C CB  . THR A 106 ? 0.3777 0.4062 0.4110 -0.0280 0.0079  -0.0551 107 THR A CB  
675  O OG1 . THR A 106 ? 0.3886 0.4129 0.4259 -0.0292 0.0093  -0.0614 107 THR A OG1 
676  C CG2 . THR A 106 ? 0.3746 0.3997 0.4108 -0.0295 0.0075  -0.0511 107 THR A CG2 
677  N N   . ARG A 107 ? 0.3593 0.3891 0.3870 -0.0201 0.0091  -0.0554 108 ARG A N   
678  C CA  . ARG A 107 ? 0.3562 0.3912 0.3800 -0.0191 0.0094  -0.0570 108 ARG A CA  
679  C C   . ARG A 107 ? 0.3403 0.3748 0.3617 -0.0154 0.0086  -0.0512 108 ARG A C   
680  O O   . ARG A 107 ? 0.3475 0.3868 0.3655 -0.0146 0.0085  -0.0511 108 ARG A O   
681  C CB  . ARG A 107 ? 0.3837 0.4168 0.4108 -0.0193 0.0115  -0.0636 108 ARG A CB  
682  C CG  . ARG A 107 ? 0.4444 0.4796 0.4733 -0.0233 0.0124  -0.0706 108 ARG A CG  
683  C CD  . ARG A 107 ? 0.5178 0.5525 0.5501 -0.0236 0.0148  -0.0783 108 ARG A CD  
684  N NE  . ARG A 107 ? 0.5756 0.6172 0.6063 -0.0280 0.0156  -0.0855 108 ARG A NE  
685  C CZ  . ARG A 107 ? 0.6163 0.6546 0.6524 -0.0306 0.0169  -0.0921 108 ARG A CZ  
686  N NH1 . ARG A 107 ? 0.6153 0.6430 0.6595 -0.0290 0.0173  -0.0919 108 ARG A NH1 
687  N NH2 . ARG A 107 ? 0.6125 0.6583 0.6464 -0.0350 0.0176  -0.0989 108 ARG A NH2 
688  N N   . MET A 108 ? 0.3198 0.3489 0.3430 -0.0135 0.0081  -0.0465 109 MET A N   
689  C CA  . MET A 108 ? 0.3085 0.3371 0.3297 -0.0104 0.0074  -0.0416 109 MET A CA  
690  C C   . MET A 108 ? 0.2865 0.3216 0.3034 -0.0103 0.0061  -0.0390 109 MET A C   
691  O O   . MET A 108 ? 0.2837 0.3217 0.3003 -0.0117 0.0052  -0.0378 109 MET A O   
692  C CB  . MET A 108 ? 0.3230 0.3458 0.3466 -0.0092 0.0070  -0.0376 109 MET A CB  
693  C CG  . MET A 108 ? 0.3757 0.3919 0.4038 -0.0078 0.0077  -0.0381 109 MET A CG  
694  S SD  . MET A 108 ? 0.4868 0.4972 0.5174 -0.0071 0.0068  -0.0323 109 MET A SD  
695  C CE  . MET A 108 ? 0.4613 0.4758 0.4865 -0.0051 0.0060  -0.0280 109 MET A CE  
696  N N   . GLN A 109 ? 0.2705 0.3081 0.2850 -0.0087 0.0058  -0.0381 110 GLN A N   
697  C CA  . GLN A 109 ? 0.2619 0.3052 0.2734 -0.0084 0.0044  -0.0353 110 GLN A CA  
698  C C   . GLN A 109 ? 0.2452 0.2871 0.2568 -0.0060 0.0034  -0.0308 110 GLN A C   
699  O O   . GLN A 109 ? 0.2448 0.2909 0.2554 -0.0057 0.0021  -0.0285 110 GLN A O   
700  C CB  . GLN A 109 ? 0.2738 0.3205 0.2829 -0.0082 0.0045  -0.0361 110 GLN A CB  
701  C CG  . GLN A 109 ? 0.3189 0.3696 0.3270 -0.0111 0.0055  -0.0412 110 GLN A CG  
702  C CD  . GLN A 109 ? 0.3619 0.4164 0.3677 -0.0113 0.0062  -0.0425 110 GLN A CD  
703  O OE1 . GLN A 109 ? 0.3810 0.4417 0.3847 -0.0141 0.0068  -0.0460 110 GLN A OE1 
704  N NE2 . GLN A 109 ? 0.3575 0.4093 0.3635 -0.0086 0.0064  -0.0398 110 GLN A NE2 
705  N N   . ASP A 110 ? 0.2340 0.2704 0.2471 -0.0045 0.0041  -0.0296 111 ASP A N   
706  C CA  . ASP A 110 ? 0.2266 0.2621 0.2396 -0.0024 0.0035  -0.0262 111 ASP A CA  
707  C C   . ASP A 110 ? 0.2226 0.2556 0.2369 -0.0026 0.0038  -0.0247 111 ASP A C   
708  O O   . ASP A 110 ? 0.2329 0.2645 0.2468 -0.0010 0.0038  -0.0226 111 ASP A O   
709  C CB  . ASP A 110 ? 0.2541 0.2870 0.2664 -0.0003 0.0037  -0.0253 111 ASP A CB  
710  C CG  . ASP A 110 ? 0.3378 0.3656 0.3520 0.0001  0.0046  -0.0261 111 ASP A CG  
711  O OD1 . ASP A 110 ? 0.3578 0.3840 0.3740 -0.0014 0.0053  -0.0283 111 ASP A OD1 
712  O OD2 . ASP A 110 ? 0.3689 0.3944 0.3833 0.0018  0.0045  -0.0243 111 ASP A OD2 
713  N N   . ILE A 111 ? 0.2147 0.2481 0.2304 -0.0048 0.0041  -0.0255 112 ILE A N   
714  C CA  . ILE A 111 ? 0.2138 0.2463 0.2304 -0.0054 0.0045  -0.0235 112 ILE A CA  
715  C C   . ILE A 111 ? 0.1985 0.2349 0.2144 -0.0039 0.0041  -0.0218 112 ILE A C   
716  O O   . ILE A 111 ? 0.2040 0.2394 0.2194 -0.0030 0.0045  -0.0202 112 ILE A O   
717  C CB  . ILE A 111 ? 0.2267 0.2603 0.2451 -0.0084 0.0047  -0.0244 112 ILE A CB  
718  C CG1 . ILE A 111 ? 0.2530 0.2829 0.2730 -0.0101 0.0051  -0.0272 112 ILE A CG1 
719  C CG2 . ILE A 111 ? 0.2257 0.2590 0.2447 -0.0095 0.0052  -0.0218 112 ILE A CG2 
720  C CD1 . ILE A 111 ? 0.2704 0.2942 0.2925 -0.0100 0.0055  -0.0264 112 ILE A CD1 
721  N N   . GLY A 112 ? 0.1733 0.2141 0.1895 -0.0034 0.0033  -0.0224 113 GLY A N   
722  C CA  . GLY A 112 ? 0.1510 0.1947 0.1679 -0.0014 0.0027  -0.0213 113 GLY A CA  
723  C C   . GLY A 112 ? 0.1286 0.1716 0.1445 0.0003  0.0018  -0.0208 113 GLY A C   
724  O O   . GLY A 112 ? 0.1224 0.1660 0.1371 -0.0007 0.0013  -0.0216 113 GLY A O   
725  N N   . GLY A 113 ? 0.1191 0.1610 0.1351 0.0023  0.0017  -0.0198 114 GLY A N   
726  C CA  . GLY A 113 ? 0.1130 0.1541 0.1285 0.0037  0.0008  -0.0189 114 GLY A CA  
727  C C   . GLY A 113 ? 0.1180 0.1601 0.1360 0.0057  0.0001  -0.0179 114 GLY A C   
728  O O   . GLY A 113 ? 0.1357 0.1773 0.1546 0.0065  0.0009  -0.0185 114 GLY A O   
729  N N   . CYS A 114 ? 0.1041 0.1479 0.1233 0.0063  -0.0015 -0.0163 115 CYS A N   
730  C CA  . CYS A 114 ? 0.1064 0.1505 0.1293 0.0083  -0.0027 -0.0149 115 CYS A CA  
731  C C   . CYS A 114 ? 0.0963 0.1380 0.1179 0.0086  -0.0034 -0.0134 115 CYS A C   
732  O O   . CYS A 114 ? 0.0946 0.1367 0.1130 0.0073  -0.0035 -0.0129 115 CYS A O   
733  C CB  . CYS A 114 ? 0.1325 0.1812 0.1590 0.0083  -0.0046 -0.0132 115 CYS A CB  
734  S SG  . CYS A 114 ? 0.2691 0.3216 0.2992 0.0084  -0.0039 -0.0150 115 CYS A SG  
735  N N   . ARG A 115 ? 0.0982 0.1380 0.1228 0.0103  -0.0039 -0.0128 116 ARG A N   
736  C CA  . ARG A 115 ? 0.1068 0.1443 0.1308 0.0104  -0.0046 -0.0112 116 ARG A CA  
737  C C   . ARG A 115 ? 0.1099 0.1466 0.1393 0.0119  -0.0063 -0.0094 116 ARG A C   
738  O O   . ARG A 115 ? 0.1153 0.1512 0.1487 0.0135  -0.0059 -0.0112 116 ARG A O   
739  C CB  . ARG A 115 ? 0.1265 0.1607 0.1478 0.0105  -0.0030 -0.0132 116 ARG A CB  
740  C CG  . ARG A 115 ? 0.1715 0.2035 0.1922 0.0105  -0.0035 -0.0119 116 ARG A CG  
741  C CD  . ARG A 115 ? 0.2145 0.2442 0.2333 0.0106  -0.0022 -0.0137 116 ARG A CD  
742  N NE  . ARG A 115 ? 0.2445 0.2744 0.2598 0.0097  -0.0011 -0.0144 116 ARG A NE  
743  C CZ  . ARG A 115 ? 0.2340 0.2626 0.2477 0.0097  -0.0002 -0.0155 116 ARG A CZ  
744  N NH1 . ARG A 115 ? 0.2106 0.2383 0.2247 0.0102  0.0000  -0.0164 116 ARG A NH1 
745  N NH2 . ARG A 115 ? 0.2264 0.2547 0.2383 0.0091  0.0005  -0.0158 116 ARG A NH2 
746  N N   . ALA A 116 ? 0.1080 0.1451 0.1379 0.0113  -0.0081 -0.0059 117 ALA A N   
747  C CA  . ALA A 116 ? 0.1171 0.1525 0.1531 0.0125  -0.0100 -0.0035 117 ALA A CA  
748  C C   . ALA A 116 ? 0.1404 0.1726 0.1751 0.0118  -0.0101 -0.0024 117 ALA A C   
749  O O   . ALA A 116 ? 0.1555 0.1892 0.1855 0.0099  -0.0101 -0.0008 117 ALA A O   
750  C CB  . ALA A 116 ? 0.1198 0.1588 0.1587 0.0120  -0.0128 0.0011  117 ALA A CB  
751  N N   . ILE A 117 ? 0.1464 0.1747 0.1851 0.0132  -0.0099 -0.0039 118 ILE A N   
752  C CA  . ILE A 117 ? 0.1617 0.1870 0.2002 0.0124  -0.0101 -0.0030 118 ILE A CA  
753  C C   . ILE A 117 ? 0.1767 0.1999 0.2220 0.0127  -0.0127 0.0008  118 ILE A C   
754  O O   . ILE A 117 ? 0.1767 0.1975 0.2291 0.0147  -0.0132 -0.0006 118 ILE A O   
755  C CB  . ILE A 117 ? 0.1673 0.1899 0.2047 0.0130  -0.0081 -0.0077 118 ILE A CB  
756  C CG1 . ILE A 117 ? 0.1676 0.1923 0.1989 0.0125  -0.0060 -0.0102 118 ILE A CG1 
757  C CG2 . ILE A 117 ? 0.1771 0.1972 0.2141 0.0119  -0.0083 -0.0069 118 ILE A CG2 
758  C CD1 . ILE A 117 ? 0.1767 0.2006 0.2080 0.0132  -0.0045 -0.0142 118 ILE A CD1 
759  N N   . VAL A 118 ? 0.1820 0.2068 0.2257 0.0106  -0.0143 0.0058  119 VAL A N   
760  C CA  . VAL A 118 ? 0.1874 0.2107 0.2370 0.0102  -0.0172 0.0111  119 VAL A CA  
761  C C   . VAL A 118 ? 0.2078 0.2273 0.2584 0.0089  -0.0173 0.0119  119 VAL A C   
762  O O   . VAL A 118 ? 0.2068 0.2260 0.2525 0.0081  -0.0152 0.0088  119 VAL A O   
763  C CB  . VAL A 118 ? 0.1864 0.2153 0.2335 0.0081  -0.0193 0.0168  119 VAL A CB  
764  C CG1 . VAL A 118 ? 0.1881 0.2209 0.2354 0.0092  -0.0196 0.0160  119 VAL A CG1 
765  C CG2 . VAL A 118 ? 0.1864 0.2191 0.2251 0.0051  -0.0179 0.0171  119 VAL A CG2 
766  N N   . ARG A 119 ? 0.2176 0.2341 0.2754 0.0087  -0.0199 0.0162  120 ARG A N   
767  C CA  . ARG A 119 ? 0.2325 0.2450 0.2927 0.0073  -0.0204 0.0173  120 ARG A CA  
768  C C   . ARG A 119 ? 0.2233 0.2397 0.2770 0.0037  -0.0203 0.0211  120 ARG A C   
769  O O   . ARG A 119 ? 0.2318 0.2473 0.2826 0.0026  -0.0187 0.0187  120 ARG A O   
770  C CB  . ARG A 119 ? 0.2776 0.2855 0.3487 0.0081  -0.0235 0.0213  120 ARG A CB  
771  C CG  . ARG A 119 ? 0.3803 0.3827 0.4560 0.0067  -0.0241 0.0219  120 ARG A CG  
772  C CD  . ARG A 119 ? 0.4832 0.4811 0.5700 0.0069  -0.0278 0.0278  120 ARG A CD  
773  N NE  . ARG A 119 ? 0.5697 0.5662 0.6647 0.0105  -0.0289 0.0269  120 ARG A NE  
774  C CZ  . ARG A 119 ? 0.6315 0.6238 0.7383 0.0118  -0.0322 0.0311  120 ARG A CZ  
775  N NH1 . ARG A 119 ? 0.6338 0.6221 0.7456 0.0094  -0.0347 0.0369  120 ARG A NH1 
776  N NH2 . ARG A 119 ? 0.6410 0.6329 0.7556 0.0154  -0.0329 0.0296  120 ARG A NH2 
777  N N   . ASN A 120 ? 0.2100 0.2315 0.2613 0.0018  -0.0220 0.0267  121 ASN A N   
778  C CA  . ASN A 120 ? 0.2119 0.2383 0.2573 -0.0020 -0.0219 0.0304  121 ASN A CA  
779  C C   . ASN A 120 ? 0.2116 0.2462 0.2506 -0.0038 -0.0219 0.0325  121 ASN A C   
780  O O   . ASN A 120 ? 0.2020 0.2379 0.2413 -0.0020 -0.0222 0.0312  121 ASN A O   
781  C CB  . ASN A 120 ? 0.2284 0.2525 0.2794 -0.0043 -0.0247 0.0370  121 ASN A CB  
782  C CG  . ASN A 120 ? 0.2701 0.2924 0.3290 -0.0034 -0.0284 0.0427  121 ASN A CG  
783  O OD1 . ASN A 120 ? 0.2863 0.3140 0.3433 -0.0040 -0.0299 0.0462  121 ASN A OD1 
784  N ND2 . ASN A 120 ? 0.2761 0.2909 0.3447 -0.0018 -0.0300 0.0433  121 ASN A ND2 
785  N N   . ILE A 121 ? 0.2185 0.2591 0.2516 -0.0075 -0.0213 0.0349  122 ILE A N   
786  C CA  . ILE A 121 ? 0.2379 0.2872 0.2643 -0.0100 -0.0209 0.0359  122 ILE A CA  
787  C C   . ILE A 121 ? 0.2510 0.3037 0.2799 -0.0111 -0.0246 0.0427  122 ILE A C   
788  O O   . ILE A 121 ? 0.2465 0.3049 0.2717 -0.0116 -0.0247 0.0421  122 ILE A O   
789  C CB  . ILE A 121 ? 0.2482 0.3039 0.2684 -0.0138 -0.0190 0.0361  122 ILE A CB  
790  C CG1 . ILE A 121 ? 0.2651 0.3190 0.2824 -0.0121 -0.0152 0.0286  122 ILE A CG1 
791  C CG2 . ILE A 121 ? 0.2565 0.3224 0.2704 -0.0173 -0.0190 0.0380  122 ILE A CG2 
792  C CD1 . ILE A 121 ? 0.2816 0.3367 0.2955 -0.0099 -0.0131 0.0224  122 ILE A CD1 
793  N N   . GLU A 122 ? 0.2672 0.3165 0.3030 -0.0116 -0.0279 0.0493  123 GLU A N   
794  C CA  . GLU A 122 ? 0.2863 0.3385 0.3260 -0.0125 -0.0321 0.0568  123 GLU A CA  
795  C C   . GLU A 122 ? 0.2845 0.3340 0.3287 -0.0082 -0.0327 0.0537  123 GLU A C   
796  O O   . GLU A 122 ? 0.2856 0.3411 0.3287 -0.0089 -0.0345 0.0563  123 GLU A O   
797  C CB  . GLU A 122 ? 0.3489 0.3967 0.3965 -0.0137 -0.0356 0.0646  123 GLU A CB  
798  C CG  . GLU A 122 ? 0.4855 0.5415 0.5295 -0.0193 -0.0381 0.0736  123 GLU A CG  
799  C CD  . GLU A 122 ? 0.6577 0.7161 0.6967 -0.0234 -0.0362 0.0743  123 GLU A CD  
800  O OE1 . GLU A 122 ? 0.6874 0.7453 0.7217 -0.0225 -0.0320 0.0664  123 GLU A OE1 
801  O OE2 . GLU A 122 ? 0.7079 0.7694 0.7481 -0.0276 -0.0390 0.0830  123 GLU A OE2 
802  N N   . GLN A 123 ? 0.2795 0.3211 0.3287 -0.0041 -0.0311 0.0479  124 GLN A N   
803  C CA  . GLN A 123 ? 0.2810 0.3205 0.3345 -0.0002 -0.0309 0.0439  124 GLN A CA  
804  C C   . GLN A 123 ? 0.2704 0.3154 0.3155 -0.0004 -0.0283 0.0388  124 GLN A C   
805  O O   . GLN A 123 ? 0.2684 0.3170 0.3147 0.0004  -0.0295 0.0393  124 GLN A O   
806  C CB  . GLN A 123 ? 0.3129 0.3437 0.3723 0.0034  -0.0292 0.0382  124 GLN A CB  
807  C CG  . GLN A 123 ? 0.3872 0.4160 0.4534 0.0074  -0.0295 0.0351  124 GLN A CG  
808  C CD  . GLN A 123 ? 0.4741 0.4949 0.5493 0.0103  -0.0291 0.0318  124 GLN A CD  
809  O OE1 . GLN A 123 ? 0.4880 0.5054 0.5607 0.0111  -0.0261 0.0253  124 GLN A OE1 
810  N NE2 . GLN A 123 ? 0.5042 0.5220 0.5904 0.0119  -0.0324 0.0360  124 GLN A NE2 
811  N N   . LEU A 124 ? 0.2657 0.3118 0.3031 -0.0018 -0.0249 0.0342  125 LEU A N   
812  C CA  . LEU A 124 ? 0.2622 0.3128 0.2923 -0.0023 -0.0222 0.0291  125 LEU A CA  
813  C C   . LEU A 124 ? 0.2577 0.3171 0.2838 -0.0052 -0.0239 0.0326  125 LEU A C   
814  O O   . LEU A 124 ? 0.2533 0.3153 0.2783 -0.0045 -0.0235 0.0299  125 LEU A O   
815  C CB  . LEU A 124 ? 0.2622 0.3127 0.2863 -0.0034 -0.0188 0.0247  125 LEU A CB  
816  C CG  . LEU A 124 ? 0.2811 0.3322 0.3006 -0.0023 -0.0156 0.0178  125 LEU A CG  
817  C CD1 . LEU A 124 ? 0.2862 0.3347 0.3031 -0.0021 -0.0128 0.0137  125 LEU A CD1 
818  C CD2 . LEU A 124 ? 0.2961 0.3550 0.3099 -0.0051 -0.0152 0.0174  125 LEU A CD2 
819  N N   . LYS A 125 ? 0.2582 0.3229 0.2819 -0.0091 -0.0256 0.0383  126 LYS A N   
820  C CA  . LYS A 125 ? 0.2626 0.3372 0.2816 -0.0128 -0.0273 0.0420  126 LYS A CA  
821  C C   . LYS A 125 ? 0.2502 0.3261 0.2752 -0.0117 -0.0314 0.0472  126 LYS A C   
822  O O   . LYS A 125 ? 0.2530 0.3360 0.2751 -0.0132 -0.0322 0.0472  126 LYS A O   
823  C CB  . LYS A 125 ? 0.2968 0.3773 0.3119 -0.0176 -0.0282 0.0476  126 LYS A CB  
824  C CG  . LYS A 125 ? 0.3577 0.4404 0.3661 -0.0195 -0.0240 0.0422  126 LYS A CG  
825  C CD  . LYS A 125 ? 0.4213 0.5120 0.4255 -0.0249 -0.0249 0.0480  126 LYS A CD  
826  C CE  . LYS A 125 ? 0.4630 0.5601 0.4597 -0.0277 -0.0208 0.0424  126 LYS A CE  
827  N NZ  . LYS A 125 ? 0.4921 0.5827 0.4904 -0.0257 -0.0180 0.0384  126 LYS A NZ  
828  N N   . LYS A 126 ? 0.2409 0.3103 0.2752 -0.0090 -0.0339 0.0512  127 LYS A N   
829  C CA  . LYS A 126 ? 0.2508 0.3203 0.2934 -0.0070 -0.0378 0.0560  127 LYS A CA  
830  C C   . LYS A 126 ? 0.2478 0.3166 0.2918 -0.0036 -0.0362 0.0494  127 LYS A C   
831  O O   . LYS A 126 ? 0.2527 0.3269 0.2987 -0.0037 -0.0386 0.0519  127 LYS A O   
832  C CB  . LYS A 126 ? 0.2865 0.3473 0.3397 -0.0043 -0.0399 0.0595  127 LYS A CB  
833  C CG  . LYS A 126 ? 0.3628 0.4226 0.4272 -0.0019 -0.0443 0.0651  127 LYS A CG  
834  C CD  . LYS A 126 ? 0.4506 0.5011 0.5253 0.0001  -0.0459 0.0681  127 LYS A CD  
835  C CE  . LYS A 126 ? 0.5198 0.5680 0.6082 0.0032  -0.0502 0.0733  127 LYS A CE  
836  N NZ  . LYS A 126 ? 0.5598 0.5985 0.6589 0.0050  -0.0516 0.0757  127 LYS A NZ  
837  N N   . LEU A 127 ? 0.2364 0.2993 0.2790 -0.0011 -0.0321 0.0414  128 LEU A N   
838  C CA  . LEU A 127 ? 0.2394 0.3020 0.2825 0.0014  -0.0302 0.0353  128 LEU A CA  
839  C C   . LEU A 127 ? 0.2427 0.3128 0.2771 -0.0016 -0.0289 0.0327  128 LEU A C   
840  O O   . LEU A 127 ? 0.2418 0.3155 0.2774 -0.0011 -0.0295 0.0316  128 LEU A O   
841  C CB  . LEU A 127 ? 0.2355 0.2902 0.2796 0.0045  -0.0266 0.0283  128 LEU A CB  
842  C CG  . LEU A 127 ? 0.2333 0.2876 0.2782 0.0069  -0.0245 0.0222  128 LEU A CG  
843  C CD1 . LEU A 127 ? 0.2337 0.2900 0.2869 0.0090  -0.0271 0.0246  128 LEU A CD1 
844  C CD2 . LEU A 127 ? 0.2348 0.2822 0.2806 0.0093  -0.0214 0.0165  128 LEU A CD2 
845  N N   . LYS A 128 ? 0.2486 0.3215 0.2749 -0.0049 -0.0270 0.0315  129 LYS A N   
846  C CA  . LYS A 128 ? 0.2643 0.3444 0.2828 -0.0079 -0.0255 0.0283  129 LYS A CA  
847  C C   . LYS A 128 ? 0.2787 0.3680 0.2968 -0.0108 -0.0291 0.0336  129 LYS A C   
848  O O   . LYS A 128 ? 0.2778 0.3718 0.2937 -0.0117 -0.0288 0.0306  129 LYS A O   
849  C CB  . LYS A 128 ? 0.2850 0.3669 0.2961 -0.0108 -0.0227 0.0257  129 LYS A CB  
850  C CG  . LYS A 128 ? 0.3427 0.4323 0.3467 -0.0141 -0.0211 0.0215  129 LYS A CG  
851  C CD  . LYS A 128 ? 0.4040 0.4956 0.4019 -0.0164 -0.0177 0.0173  129 LYS A CD  
852  C CE  . LYS A 128 ? 0.4508 0.5485 0.4458 -0.0202 -0.0190 0.0226  129 LYS A CE  
853  N NZ  . LYS A 128 ? 0.4752 0.5846 0.4647 -0.0250 -0.0201 0.0239  129 LYS A NZ  
854  N N   . ASP A 129 ? 0.2902 0.3824 0.3105 -0.0125 -0.0328 0.0416  130 ASP A N   
855  C CA  . ASP A 129 ? 0.3083 0.4102 0.3285 -0.0156 -0.0369 0.0481  130 ASP A CA  
856  C C   . ASP A 129 ? 0.3066 0.4087 0.3341 -0.0127 -0.0393 0.0489  130 ASP A C   
857  O O   . ASP A 129 ? 0.3225 0.4330 0.3475 -0.0150 -0.0408 0.0495  130 ASP A O   
858  C CB  . ASP A 129 ? 0.3574 0.4610 0.3801 -0.0177 -0.0407 0.0578  130 ASP A CB  
859  C CG  . ASP A 129 ? 0.4955 0.6044 0.5093 -0.0226 -0.0391 0.0584  130 ASP A CG  
860  O OD1 . ASP A 129 ? 0.5247 0.6374 0.5304 -0.0246 -0.0353 0.0513  130 ASP A OD1 
861  O OD2 . ASP A 129 ? 0.5469 0.6563 0.5624 -0.0245 -0.0415 0.0660  130 ASP A OD2 
862  N N   . ARG A 130 ? 0.2841 0.3774 0.3205 -0.0077 -0.0394 0.0484  131 ARG A N   
863  C CA  . ARG A 130 ? 0.2657 0.3588 0.3105 -0.0043 -0.0411 0.0483  131 ARG A CA  
864  C C   . ARG A 130 ? 0.2468 0.3421 0.2875 -0.0042 -0.0379 0.0404  131 ARG A C   
865  O O   . ARG A 130 ? 0.2545 0.3562 0.2970 -0.0048 -0.0399 0.0414  131 ARG A O   
866  C CB  . ARG A 130 ? 0.2835 0.3667 0.3386 0.0007  -0.0410 0.0481  131 ARG A CB  
867  C CG  . ARG A 130 ? 0.3430 0.4269 0.4088 0.0043  -0.0433 0.0491  131 ARG A CG  
868  C CD  . ARG A 130 ? 0.4000 0.4753 0.4773 0.0088  -0.0439 0.0497  131 ARG A CD  
869  N NE  . ARG A 130 ? 0.4572 0.5324 0.5411 0.0083  -0.0486 0.0590  131 ARG A NE  
870  C CZ  . ARG A 130 ? 0.4919 0.5712 0.5851 0.0093  -0.0534 0.0659  131 ARG A CZ  
871  N NH1 . ARG A 130 ? 0.4745 0.5590 0.5714 0.0110  -0.0541 0.0641  131 ARG A NH1 
872  N NH2 . ARG A 130 ? 0.5054 0.5839 0.6047 0.0086  -0.0579 0.0750  131 ARG A NH2 
873  N N   . LEU A 131 ? 0.2306 0.3209 0.2658 -0.0039 -0.0334 0.0332  132 LEU A N   
874  C CA  . LEU A 131 ? 0.2205 0.3119 0.2518 -0.0042 -0.0303 0.0261  132 LEU A CA  
875  C C   . LEU A 131 ? 0.2244 0.3253 0.2482 -0.0091 -0.0309 0.0258  132 LEU A C   
876  O O   . LEU A 131 ? 0.2202 0.3251 0.2437 -0.0098 -0.0307 0.0229  132 LEU A O   
877  C CB  . LEU A 131 ? 0.2128 0.2965 0.2404 -0.0029 -0.0257 0.0196  132 LEU A CB  
878  C CG  . LEU A 131 ? 0.2113 0.2863 0.2454 0.0015  -0.0247 0.0183  132 LEU A CG  
879  C CD1 . LEU A 131 ? 0.2103 0.2792 0.2400 0.0019  -0.0209 0.0133  132 LEU A CD1 
880  C CD2 . LEU A 131 ? 0.2000 0.2750 0.2406 0.0042  -0.0247 0.0162  132 LEU A CD2 
881  N N   . VAL A 132 ? 0.2306 0.3359 0.2485 -0.0127 -0.0315 0.0286  133 VAL A N   
882  C CA  . VAL A 132 ? 0.2442 0.3595 0.2544 -0.0179 -0.0318 0.0278  133 VAL A CA  
883  C C   . VAL A 132 ? 0.2525 0.3773 0.2653 -0.0199 -0.0366 0.0340  133 VAL A C   
884  O O   . VAL A 132 ? 0.2460 0.3786 0.2548 -0.0230 -0.0368 0.0314  133 VAL A O   
885  C CB  . VAL A 132 ? 0.2586 0.3766 0.2615 -0.0214 -0.0304 0.0282  133 VAL A CB  
886  C CG1 . VAL A 132 ? 0.2671 0.3977 0.2627 -0.0274 -0.0314 0.0284  133 VAL A CG1 
887  C CG2 . VAL A 132 ? 0.2615 0.3722 0.2615 -0.0200 -0.0254 0.0207  133 VAL A CG2 
888  N N   . LYS A 133 ? 0.2681 0.3920 0.2883 -0.0179 -0.0406 0.0420  134 LYS A N   
889  C CA  . LYS A 133 ? 0.2931 0.4258 0.3175 -0.0192 -0.0458 0.0489  134 LYS A CA  
890  C C   . LYS A 133 ? 0.3044 0.4361 0.3367 -0.0156 -0.0465 0.0469  134 LYS A C   
891  O O   . LYS A 133 ? 0.3096 0.4491 0.3460 -0.0165 -0.0507 0.0520  134 LYS A O   
892  C CB  . LYS A 133 ? 0.3439 0.4766 0.3739 -0.0188 -0.0503 0.0592  134 LYS A CB  
893  C CG  . LYS A 133 ? 0.4386 0.5803 0.4604 -0.0248 -0.0521 0.0645  134 LYS A CG  
894  C CD  . LYS A 133 ? 0.5149 0.6707 0.5316 -0.0299 -0.0548 0.0663  134 LYS A CD  
895  C CE  . LYS A 133 ? 0.5708 0.7374 0.5794 -0.0364 -0.0570 0.0723  134 LYS A CE  
896  N NZ  . LYS A 133 ? 0.5976 0.7788 0.6017 -0.0414 -0.0600 0.0741  134 LYS A NZ  
897  N N   . SER A 134 ? 0.3116 0.4347 0.3463 -0.0118 -0.0426 0.0399  135 SER A N   
898  C CA  . SER A 134 ? 0.3199 0.4426 0.3621 -0.0086 -0.0427 0.0375  135 SER A CA  
899  C C   . SER A 134 ? 0.3287 0.4605 0.3669 -0.0122 -0.0430 0.0347  135 SER A C   
900  O O   . SER A 134 ? 0.3409 0.4742 0.3701 -0.0156 -0.0401 0.0293  135 SER A O   
901  C CB  . SER A 134 ? 0.3334 0.4457 0.3774 -0.0048 -0.0381 0.0306  135 SER A CB  
902  O OG  . SER A 134 ? 0.3567 0.4699 0.4058 -0.0028 -0.0372 0.0269  135 SER A OG  
903  N N   . ARG A 135 ? 0.3181 0.4561 0.3637 -0.0113 -0.0466 0.0383  136 ARG A N   
904  C CA  . ARG A 135 ? 0.3112 0.4585 0.3540 -0.0147 -0.0473 0.0359  136 ARG A CA  
905  C C   . ARG A 135 ? 0.2940 0.4378 0.3418 -0.0119 -0.0445 0.0297  136 ARG A C   
906  O O   . ARG A 135 ? 0.3112 0.4580 0.3684 -0.0093 -0.0468 0.0321  136 ARG A O   
907  C CB  . ARG A 135 ? 0.3343 0.4929 0.3812 -0.0166 -0.0535 0.0443  136 ARG A CB  
908  C CG  . ARG A 135 ? 0.4021 0.5684 0.4398 -0.0223 -0.0556 0.0485  136 ARG A CG  
909  C CD  . ARG A 135 ? 0.4720 0.6429 0.5151 -0.0223 -0.0615 0.0599  136 ARG A CD  
910  N NE  . ARG A 135 ? 0.5369 0.7139 0.5907 -0.0203 -0.0664 0.0655  136 ARG A NE  
911  C CZ  . ARG A 135 ? 0.5779 0.7499 0.6447 -0.0148 -0.0689 0.0707  136 ARG A CZ  
912  N NH1 . ARG A 135 ? 0.5813 0.7418 0.6513 -0.0111 -0.0670 0.0709  136 ARG A NH1 
913  N NH2 . ARG A 135 ? 0.5682 0.7468 0.6454 -0.0130 -0.0734 0.0754  136 ARG A NH2 
914  N N   . SER A 136 ? 0.2641 0.4015 0.3063 -0.0122 -0.0395 0.0222  137 SER A N   
915  C CA  . SER A 136 ? 0.2422 0.3765 0.2880 -0.0103 -0.0366 0.0165  137 SER A CA  
916  C C   . SER A 136 ? 0.2180 0.3544 0.2560 -0.0147 -0.0338 0.0100  137 SER A C   
917  O O   . SER A 136 ? 0.2249 0.3652 0.2553 -0.0188 -0.0341 0.0093  137 SER A O   
918  C CB  . SER A 136 ? 0.2477 0.3709 0.2965 -0.0057 -0.0332 0.0140  137 SER A CB  
919  O OG  . SER A 136 ? 0.2619 0.3782 0.3027 -0.0068 -0.0294 0.0094  137 SER A OG  
920  N N   . LYS A 137 ? 0.1866 0.3213 0.2271 -0.0141 -0.0314 0.0052  138 LYS A N   
921  C CA  . LYS A 137 ? 0.1784 0.3138 0.2130 -0.0181 -0.0288 -0.0010 138 LYS A CA  
922  C C   . LYS A 137 ? 0.1741 0.3000 0.2022 -0.0183 -0.0247 -0.0056 138 LYS A C   
923  O O   . LYS A 137 ? 0.1809 0.3061 0.2046 -0.0214 -0.0224 -0.0108 138 LYS A O   
924  C CB  . LYS A 137 ? 0.2001 0.3366 0.2399 -0.0177 -0.0276 -0.0039 138 LYS A CB  
925  C CG  . LYS A 137 ? 0.2486 0.3957 0.2950 -0.0181 -0.0315 -0.0002 138 LYS A CG  
926  C CD  . LYS A 137 ? 0.3149 0.4632 0.3673 -0.0174 -0.0299 -0.0031 138 LYS A CD  
927  C CE  . LYS A 137 ? 0.3514 0.5100 0.4125 -0.0166 -0.0338 0.0009  138 LYS A CE  
928  N NZ  . LYS A 137 ? 0.3681 0.5267 0.4370 -0.0142 -0.0318 -0.0014 138 LYS A NZ  
929  N N   . HIS A 138 ? 0.1646 0.2834 0.1928 -0.0149 -0.0238 -0.0037 139 HIS A N   
930  C CA  . HIS A 138 ? 0.1583 0.2684 0.1818 -0.0144 -0.0202 -0.0074 139 HIS A CA  
931  C C   . HIS A 138 ? 0.1741 0.2858 0.1917 -0.0164 -0.0208 -0.0061 139 HIS A C   
932  O O   . HIS A 138 ? 0.1843 0.2977 0.2031 -0.0153 -0.0233 -0.0008 139 HIS A O   
933  C CB  . HIS A 138 ? 0.1410 0.2430 0.1688 -0.0097 -0.0186 -0.0069 139 HIS A CB  
934  C CG  . HIS A 138 ? 0.1594 0.2631 0.1941 -0.0079 -0.0187 -0.0070 139 HIS A CG  
935  N ND1 . HIS A 138 ? 0.1734 0.2788 0.2081 -0.0100 -0.0172 -0.0107 139 HIS A ND1 
936  C CD2 . HIS A 138 ? 0.1653 0.2705 0.2076 -0.0045 -0.0204 -0.0038 139 HIS A CD2 
937  C CE1 . HIS A 138 ? 0.1623 0.2703 0.2040 -0.0079 -0.0177 -0.0098 139 HIS A CE1 
938  N NE2 . HIS A 138 ? 0.1638 0.2719 0.2105 -0.0044 -0.0195 -0.0059 139 HIS A NE2 
939  N N   . LYS A 139 ? 0.1724 0.2844 0.1840 -0.0198 -0.0187 -0.0111 140 LYS A N   
940  C CA  . LYS A 139 ? 0.1840 0.2995 0.1897 -0.0225 -0.0189 -0.0109 140 LYS A CA  
941  C C   . LYS A 139 ? 0.1931 0.3007 0.1960 -0.0211 -0.0157 -0.0136 140 LYS A C   
942  O O   . LYS A 139 ? 0.1910 0.2918 0.1944 -0.0201 -0.0128 -0.0182 140 LYS A O   
943  C CB  . LYS A 139 ? 0.2165 0.3403 0.2177 -0.0279 -0.0190 -0.0151 140 LYS A CB  
944  C CG  . LYS A 139 ? 0.2722 0.4052 0.2759 -0.0300 -0.0224 -0.0128 140 LYS A CG  
945  C CD  . LYS A 139 ? 0.3518 0.4910 0.3581 -0.0290 -0.0268 -0.0043 140 LYS A CD  
946  C CE  . LYS A 139 ? 0.4180 0.5652 0.4290 -0.0299 -0.0303 -0.0015 140 LYS A CE  
947  N NZ  . LYS A 139 ? 0.4658 0.6231 0.4719 -0.0358 -0.0311 -0.0048 140 LYS A NZ  
948  N N   . ILE A 140 ? 0.1924 0.3015 0.1927 -0.0213 -0.0165 -0.0104 141 ILE A N   
949  C CA  . ILE A 140 ? 0.1926 0.2960 0.1901 -0.0204 -0.0137 -0.0128 141 ILE A CA  
950  C C   . ILE A 140 ? 0.2050 0.3129 0.1973 -0.0246 -0.0116 -0.0189 141 ILE A C   
951  O O   . ILE A 140 ? 0.2114 0.3285 0.1997 -0.0283 -0.0130 -0.0179 141 ILE A O   
952  C CB  . ILE A 140 ? 0.1998 0.3043 0.1969 -0.0196 -0.0155 -0.0068 141 ILE A CB  
953  C CG1 . ILE A 140 ? 0.2055 0.3061 0.2090 -0.0157 -0.0179 -0.0010 141 ILE A CG1 
954  C CG2 . ILE A 140 ? 0.2061 0.3055 0.2006 -0.0189 -0.0125 -0.0094 141 ILE A CG2 
955  C CD1 . ILE A 140 ? 0.2096 0.3099 0.2143 -0.0148 -0.0201 0.0054  141 ILE A CD1 
956  N N   . LEU A 141 ? 0.2062 0.3084 0.1990 -0.0242 -0.0084 -0.0252 142 LEU A N   
957  C CA  . LEU A 141 ? 0.2184 0.3237 0.2079 -0.0277 -0.0060 -0.0321 142 LEU A CA  
958  C C   . LEU A 141 ? 0.2338 0.3389 0.2204 -0.0278 -0.0040 -0.0337 142 LEU A C   
959  O O   . LEU A 141 ? 0.2506 0.3623 0.2334 -0.0315 -0.0027 -0.0382 142 LEU A O   
960  C CB  . LEU A 141 ? 0.2228 0.3211 0.2152 -0.0271 -0.0036 -0.0380 142 LEU A CB  
961  C CG  . LEU A 141 ? 0.2403 0.3394 0.2356 -0.0278 -0.0051 -0.0375 142 LEU A CG  
962  C CD1 . LEU A 141 ? 0.2440 0.3373 0.2418 -0.0285 -0.0026 -0.0436 142 LEU A CD1 
963  C CD2 . LEU A 141 ? 0.2491 0.3599 0.2418 -0.0320 -0.0077 -0.0366 142 LEU A CD2 
964  N N   . LYS A 142 ? 0.2282 0.3264 0.2167 -0.0239 -0.0036 -0.0305 143 LYS A N   
965  C CA  . LYS A 142 ? 0.2263 0.3241 0.2130 -0.0237 -0.0017 -0.0314 143 LYS A CA  
966  C C   . LYS A 142 ? 0.2134 0.3076 0.2014 -0.0207 -0.0032 -0.0248 143 LYS A C   
967  O O   . LYS A 142 ? 0.2036 0.2907 0.1953 -0.0172 -0.0039 -0.0222 143 LYS A O   
968  C CB  . LYS A 142 ? 0.2629 0.3536 0.2520 -0.0220 0.0019  -0.0380 143 LYS A CB  
969  C CG  . LYS A 142 ? 0.3272 0.4218 0.3152 -0.0254 0.0041  -0.0459 143 LYS A CG  
970  C CD  . LYS A 142 ? 0.4109 0.4989 0.4024 -0.0236 0.0074  -0.0517 143 LYS A CD  
971  C CE  . LYS A 142 ? 0.4756 0.5591 0.4707 -0.0241 0.0086  -0.0571 143 LYS A CE  
972  N NZ  . LYS A 142 ? 0.5198 0.5968 0.5195 -0.0223 0.0116  -0.0627 143 LYS A NZ  
973  N N   . GLU A 143 ? 0.2189 0.3185 0.2039 -0.0224 -0.0035 -0.0223 144 GLU A N   
974  C CA  . GLU A 143 ? 0.2367 0.3329 0.2231 -0.0202 -0.0047 -0.0165 144 GLU A CA  
975  C C   . GLU A 143 ? 0.2208 0.3146 0.2067 -0.0196 -0.0015 -0.0204 144 GLU A C   
976  O O   . GLU A 143 ? 0.2249 0.3256 0.2073 -0.0227 0.0003  -0.0240 144 GLU A O   
977  C CB  . GLU A 143 ? 0.2981 0.4023 0.2820 -0.0230 -0.0078 -0.0098 144 GLU A CB  
978  C CG  . GLU A 143 ? 0.4386 0.5505 0.4212 -0.0258 -0.0105 -0.0079 144 GLU A CG  
979  C CD  . GLU A 143 ? 0.6035 0.7225 0.5851 -0.0280 -0.0145 0.0005  144 GLU A CD  
980  O OE1 . GLU A 143 ? 0.6274 0.7489 0.6069 -0.0295 -0.0145 0.0037  144 GLU A OE1 
981  O OE2 . GLU A 143 ? 0.6656 0.7879 0.6492 -0.0284 -0.0177 0.0043  144 GLU A OE2 
982  N N   . TYR A 144 ? 0.2036 0.2886 0.1930 -0.0157 -0.0005 -0.0203 145 TYR A N   
983  C CA  . TYR A 144 ? 0.2066 0.2894 0.1965 -0.0148 0.0022  -0.0234 145 TYR A CA  
984  C C   . TYR A 144 ? 0.2118 0.2943 0.2018 -0.0142 0.0010  -0.0180 145 TYR A C   
985  O O   . TYR A 144 ? 0.2047 0.2809 0.1976 -0.0114 -0.0005 -0.0143 145 TYR A O   
986  C CB  . TYR A 144 ? 0.2076 0.2814 0.2015 -0.0112 0.0037  -0.0267 145 TYR A CB  
987  C CG  . TYR A 144 ? 0.2261 0.2992 0.2208 -0.0119 0.0053  -0.0325 145 TYR A CG  
988  C CD1 . TYR A 144 ? 0.2439 0.3189 0.2391 -0.0129 0.0082  -0.0388 145 TYR A CD1 
989  C CD2 . TYR A 144 ? 0.2379 0.3086 0.2337 -0.0116 0.0040  -0.0320 145 TYR A CD2 
990  C CE1 . TYR A 144 ? 0.2562 0.3295 0.2532 -0.0136 0.0096  -0.0445 145 TYR A CE1 
991  C CE2 . TYR A 144 ? 0.2552 0.3249 0.2522 -0.0126 0.0054  -0.0373 145 TYR A CE2 
992  C CZ  . TYR A 144 ? 0.2683 0.3389 0.2660 -0.0136 0.0081  -0.0435 145 TYR A CZ  
993  O OH  . TYR A 144 ? 0.2926 0.3613 0.2925 -0.0146 0.0095  -0.0490 145 TYR A OH  
994  N N   . ASP A 145 ? 0.2250 0.3146 0.2120 -0.0171 0.0018  -0.0177 146 ASP A N   
995  C CA  . ASP A 145 ? 0.2326 0.3223 0.2198 -0.0172 0.0008  -0.0126 146 ASP A CA  
996  C C   . ASP A 145 ? 0.2270 0.3129 0.2166 -0.0151 0.0035  -0.0160 146 ASP A C   
997  O O   . ASP A 145 ? 0.2341 0.3249 0.2225 -0.0166 0.0063  -0.0208 146 ASP A O   
998  C CB  . ASP A 145 ? 0.2784 0.3788 0.2611 -0.0220 0.0001  -0.0096 146 ASP A CB  
999  C CG  . ASP A 145 ? 0.3898 0.4904 0.3731 -0.0227 -0.0018 -0.0026 146 ASP A CG  
1000 O OD1 . ASP A 145 ? 0.4038 0.5002 0.3894 -0.0209 -0.0003 -0.0034 146 ASP A OD1 
1001 O OD2 . ASP A 145 ? 0.4610 0.5662 0.4429 -0.0252 -0.0048 0.0039  146 ASP A OD2 
1002 N N   . TYR A 146 ? 0.2142 0.2919 0.2073 -0.0117 0.0027  -0.0138 147 TYR A N   
1003 C CA  . TYR A 146 ? 0.2081 0.2826 0.2037 -0.0098 0.0045  -0.0159 147 TYR A CA  
1004 C C   . TYR A 146 ? 0.2064 0.2806 0.2027 -0.0103 0.0031  -0.0106 147 TYR A C   
1005 O O   . TYR A 146 ? 0.2065 0.2757 0.2056 -0.0080 0.0035  -0.0108 147 TYR A O   
1006 C CB  . TYR A 146 ? 0.2084 0.2742 0.2075 -0.0059 0.0048  -0.0181 147 TYR A CB  
1007 C CG  . TYR A 146 ? 0.2161 0.2807 0.2156 -0.0054 0.0059  -0.0226 147 TYR A CG  
1008 C CD1 . TYR A 146 ? 0.2207 0.2890 0.2201 -0.0066 0.0084  -0.0282 147 TYR A CD1 
1009 C CD2 . TYR A 146 ? 0.2304 0.2896 0.2310 -0.0037 0.0046  -0.0217 147 TYR A CD2 
1010 C CE1 . TYR A 146 ? 0.2339 0.3002 0.2345 -0.0062 0.0094  -0.0326 147 TYR A CE1 
1011 C CE2 . TYR A 146 ? 0.2430 0.3006 0.2444 -0.0035 0.0055  -0.0256 147 TYR A CE2 
1012 C CZ  . TYR A 146 ? 0.2552 0.3159 0.2567 -0.0048 0.0078  -0.0309 147 TYR A CZ  
1013 O OH  . TYR A 146 ? 0.2889 0.3472 0.2920 -0.0047 0.0087  -0.0349 147 TYR A OH  
1014 N N   . LEU A 147 ? 0.2084 0.2879 0.2023 -0.0134 0.0013  -0.0056 148 LEU A N   
1015 C CA  . LEU A 147 ? 0.2178 0.2966 0.2131 -0.0142 -0.0001 -0.0003 148 LEU A CA  
1016 C C   . LEU A 147 ? 0.2245 0.3068 0.2197 -0.0152 0.0025  -0.0027 148 LEU A C   
1017 O O   . LEU A 147 ? 0.2288 0.3082 0.2266 -0.0146 0.0020  -0.0003 148 LEU A O   
1018 C CB  . LEU A 147 ? 0.2202 0.3035 0.2138 -0.0173 -0.0030 0.0065  148 LEU A CB  
1019 C CG  . LEU A 147 ? 0.2319 0.3109 0.2276 -0.0156 -0.0060 0.0095  148 LEU A CG  
1020 C CD1 . LEU A 147 ? 0.2346 0.3191 0.2293 -0.0189 -0.0092 0.0166  148 LEU A CD1 
1021 C CD2 . LEU A 147 ? 0.2348 0.3038 0.2358 -0.0116 -0.0069 0.0100  148 LEU A CD2 
1022 N N   . THR A 148 ? 0.2218 0.3104 0.2152 -0.0164 0.0054  -0.0082 149 THR A N   
1023 C CA  . THR A 148 ? 0.2196 0.3110 0.2145 -0.0163 0.0083  -0.0120 149 THR A CA  
1024 C C   . THR A 148 ? 0.2037 0.2876 0.2026 -0.0119 0.0094  -0.0168 149 THR A C   
1025 O O   . THR A 148 ? 0.1972 0.2794 0.1958 -0.0108 0.0099  -0.0203 149 THR A O   
1026 C CB  . THR A 148 ? 0.2317 0.3340 0.2235 -0.0199 0.0111  -0.0160 149 THR A CB  
1027 O OG1 . THR A 148 ? 0.2439 0.3536 0.2315 -0.0245 0.0096  -0.0104 149 THR A OG1 
1028 C CG2 . THR A 148 ? 0.2360 0.3413 0.2309 -0.0191 0.0144  -0.0211 149 THR A CG2 
1029 N N   . PRO A 149 ? 0.1998 0.2787 0.2024 -0.0094 0.0092  -0.0160 150 PRO A N   
1030 C CA  . PRO A 149 ? 0.2031 0.2749 0.2093 -0.0054 0.0096  -0.0192 150 PRO A CA  
1031 C C   . PRO A 149 ? 0.2179 0.2913 0.2262 -0.0043 0.0123  -0.0257 150 PRO A C   
1032 O O   . PRO A 149 ? 0.2210 0.3010 0.2300 -0.0056 0.0148  -0.0293 150 PRO A O   
1033 C CB  . PRO A 149 ? 0.2010 0.2701 0.2104 -0.0041 0.0091  -0.0174 150 PRO A CB  
1034 C CG  . PRO A 149 ? 0.2046 0.2769 0.2123 -0.0070 0.0079  -0.0127 150 PRO A CG  
1035 C CD  . PRO A 149 ? 0.1855 0.2652 0.1891 -0.0106 0.0084  -0.0120 150 PRO A CD  
1036 N N   . LYS A 150 ? 0.2263 0.2932 0.2362 -0.0017 0.0118  -0.0272 151 LYS A N   
1037 C CA  . LYS A 150 ? 0.2297 0.2952 0.2431 0.0000  0.0137  -0.0327 151 LYS A CA  
1038 C C   . LYS A 150 ? 0.2352 0.3001 0.2543 0.0024  0.0147  -0.0343 151 LYS A C   
1039 O O   . LYS A 150 ? 0.2302 0.2945 0.2498 0.0028  0.0136  -0.0308 151 LYS A O   
1040 C CB  . LYS A 150 ? 0.2469 0.3049 0.2607 0.0019  0.0121  -0.0318 151 LYS A CB  
1041 C CG  . LYS A 150 ? 0.3022 0.3612 0.3118 -0.0001 0.0111  -0.0310 151 LYS A CG  
1042 C CD  . LYS A 150 ? 0.3670 0.4243 0.3782 0.0002  0.0123  -0.0357 151 LYS A CD  
1043 C CE  . LYS A 150 ? 0.4067 0.4562 0.4199 0.0025  0.0109  -0.0341 151 LYS A CE  
1044 N NZ  . LYS A 150 ? 0.4379 0.4854 0.4484 0.0026  0.0085  -0.0289 151 LYS A NZ  
1045 N N   . PRO A 151 ? 0.2363 0.3010 0.2604 0.0041  0.0168  -0.0395 152 PRO A N   
1046 C CA  . PRO A 151 ? 0.2215 0.2858 0.2523 0.0066  0.0174  -0.0407 152 PRO A CA  
1047 C C   . PRO A 151 ? 0.2043 0.2622 0.2366 0.0090  0.0147  -0.0359 152 PRO A C   
1048 O O   . PRO A 151 ? 0.2145 0.2735 0.2511 0.0105  0.0146  -0.0352 152 PRO A O   
1049 C CB  . PRO A 151 ? 0.2311 0.2943 0.2677 0.0083  0.0194  -0.0467 152 PRO A CB  
1050 C CG  . PRO A 151 ? 0.2417 0.3095 0.2738 0.0052  0.0211  -0.0504 152 PRO A CG  
1051 C CD  . PRO A 151 ? 0.2276 0.2929 0.2525 0.0035  0.0185  -0.0448 152 PRO A CD  
1052 N N   . SER A 152 ? 0.1737 0.2259 0.2028 0.0092  0.0126  -0.0327 153 SER A N   
1053 C CA  . SER A 152 ? 0.1557 0.2030 0.1854 0.0108  0.0102  -0.0286 153 SER A CA  
1054 C C   . SER A 152 ? 0.1428 0.1918 0.1692 0.0093  0.0090  -0.0249 153 SER A C   
1055 O O   . SER A 152 ? 0.1365 0.1834 0.1641 0.0103  0.0074  -0.0224 153 SER A O   
1056 C CB  . SER A 152 ? 0.1632 0.2047 0.1905 0.0111  0.0088  -0.0270 153 SER A CB  
1057 O OG  . SER A 152 ? 0.1862 0.2285 0.2081 0.0091  0.0083  -0.0257 153 SER A OG  
1058 N N   . GLY A 153 ? 0.1420 0.1947 0.1644 0.0068  0.0094  -0.0244 154 GLY A N   
1059 C CA  . GLY A 153 ? 0.1457 0.1993 0.1653 0.0050  0.0080  -0.0206 154 GLY A CA  
1060 C C   . GLY A 153 ? 0.1463 0.1969 0.1621 0.0041  0.0064  -0.0181 154 GLY A C   
1061 O O   . GLY A 153 ? 0.1400 0.1905 0.1542 0.0027  0.0051  -0.0148 154 GLY A O   
1062 N N   . TYR A 154 ? 0.1532 0.2012 0.1682 0.0049  0.0065  -0.0196 155 TYR A N   
1063 C CA  . TYR A 154 ? 0.1710 0.2166 0.1833 0.0044  0.0051  -0.0177 155 TYR A CA  
1064 C C   . TYR A 154 ? 0.1814 0.2317 0.1907 0.0018  0.0050  -0.0164 155 TYR A C   
1065 O O   . TYR A 154 ? 0.1905 0.2459 0.1987 0.0002  0.0066  -0.0188 155 TYR A O   
1066 C CB  . TYR A 154 ? 0.1729 0.2153 0.1856 0.0057  0.0054  -0.0199 155 TYR A CB  
1067 C CG  . TYR A 154 ? 0.1828 0.2233 0.1934 0.0054  0.0041  -0.0181 155 TYR A CG  
1068 C CD1 . TYR A 154 ? 0.1993 0.2357 0.2103 0.0066  0.0027  -0.0163 155 TYR A CD1 
1069 C CD2 . TYR A 154 ? 0.1955 0.2390 0.2039 0.0037  0.0041  -0.0186 155 TYR A CD2 
1070 C CE1 . TYR A 154 ? 0.2136 0.2490 0.2237 0.0064  0.0016  -0.0151 155 TYR A CE1 
1071 C CE2 . TYR A 154 ? 0.2090 0.2515 0.2164 0.0035  0.0027  -0.0168 155 TYR A CE2 
1072 C CZ  . TYR A 154 ? 0.2279 0.2661 0.2365 0.0051  0.0016  -0.0152 155 TYR A CZ  
1073 O OH  . TYR A 154 ? 0.2532 0.2909 0.2618 0.0051  0.0004  -0.0139 155 TYR A OH  
1074 N N   . SER A 155 ? 0.1767 0.2256 0.1851 0.0012  0.0030  -0.0126 156 SER A N   
1075 C CA  . SER A 155 ? 0.1831 0.2363 0.1892 -0.0014 0.0021  -0.0100 156 SER A CA  
1076 C C   . SER A 155 ? 0.1940 0.2438 0.2003 -0.0007 -0.0001 -0.0074 156 SER A C   
1077 O O   . SER A 155 ? 0.1991 0.2436 0.2076 0.0013  -0.0010 -0.0069 156 SER A O   
1078 C CB  . SER A 155 ? 0.1947 0.2519 0.2004 -0.0037 0.0018  -0.0071 156 SER A CB  
1079 O OG  . SER A 155 ? 0.2305 0.2838 0.2384 -0.0033 0.0000  -0.0036 156 SER A OG  
1080 N N   . GLY A 156 ? 0.1901 0.2439 0.1944 -0.0025 -0.0009 -0.0060 157 GLY A N   
1081 C CA  . GLY A 156 ? 0.1854 0.2376 0.1906 -0.0020 -0.0030 -0.0036 157 GLY A CA  
1082 C C   . GLY A 156 ? 0.1796 0.2372 0.1821 -0.0039 -0.0030 -0.0044 157 GLY A C   
1083 O O   . GLY A 156 ? 0.1751 0.2385 0.1746 -0.0063 -0.0017 -0.0061 157 GLY A O   
1084 N N   . ILE A 157 ? 0.1767 0.2334 0.1803 -0.0031 -0.0045 -0.0035 158 ILE A N   
1085 C CA  . ILE A 157 ? 0.1715 0.2337 0.1727 -0.0052 -0.0049 -0.0042 158 ILE A CA  
1086 C C   . ILE A 157 ? 0.1574 0.2166 0.1599 -0.0035 -0.0044 -0.0071 158 ILE A C   
1087 O O   . ILE A 157 ? 0.1513 0.2062 0.1570 -0.0013 -0.0054 -0.0059 158 ILE A O   
1088 C CB  . ILE A 157 ? 0.1861 0.2529 0.1875 -0.0071 -0.0079 0.0017  158 ILE A CB  
1089 C CG1 . ILE A 157 ? 0.2086 0.2808 0.2073 -0.0102 -0.0081 0.0045  158 ILE A CG1 
1090 C CG2 . ILE A 157 ? 0.1991 0.2711 0.1992 -0.0086 -0.0091 0.0015  158 ILE A CG2 
1091 C CD1 . ILE A 157 ? 0.2296 0.3075 0.2281 -0.0129 -0.0114 0.0113  158 ILE A CD1 
1092 N N   . HIS A 158 ? 0.1537 0.2154 0.1540 -0.0048 -0.0029 -0.0113 159 HIS A N   
1093 C CA  . HIS A 158 ? 0.1506 0.2100 0.1522 -0.0039 -0.0026 -0.0137 159 HIS A CA  
1094 C C   . HIS A 158 ? 0.1547 0.2205 0.1547 -0.0065 -0.0039 -0.0135 159 HIS A C   
1095 O O   . HIS A 158 ? 0.1644 0.2365 0.1612 -0.0094 -0.0036 -0.0144 159 HIS A O   
1096 C CB  . HIS A 158 ? 0.1608 0.2165 0.1627 -0.0031 0.0000  -0.0187 159 HIS A CB  
1097 C CG  . HIS A 158 ? 0.1907 0.2404 0.1944 -0.0006 0.0008  -0.0185 159 HIS A CG  
1098 N ND1 . HIS A 158 ? 0.2155 0.2612 0.2205 0.0005  0.0025  -0.0217 159 HIS A ND1 
1099 C CD2 . HIS A 158 ? 0.1976 0.2452 0.2024 0.0008  -0.0001 -0.0154 159 HIS A CD2 
1100 C CE1 . HIS A 158 ? 0.2136 0.2557 0.2200 0.0024  0.0025  -0.0202 159 HIS A CE1 
1101 N NE2 . HIS A 158 ? 0.2099 0.2531 0.2161 0.0025  0.0011  -0.0169 159 HIS A NE2 
1102 N N   . LEU A 159 ? 0.1490 0.2143 0.1514 -0.0056 -0.0053 -0.0123 160 LEU A N   
1103 C CA  . LEU A 159 ? 0.1470 0.2185 0.1486 -0.0079 -0.0068 -0.0120 160 LEU A CA  
1104 C C   . LEU A 159 ? 0.1545 0.2236 0.1571 -0.0078 -0.0053 -0.0163 160 LEU A C   
1105 O O   . LEU A 159 ? 0.1605 0.2243 0.1660 -0.0053 -0.0049 -0.0163 160 LEU A O   
1106 C CB  . LEU A 159 ? 0.1430 0.2164 0.1480 -0.0070 -0.0100 -0.0065 160 LEU A CB  
1107 C CG  . LEU A 159 ? 0.1506 0.2255 0.1559 -0.0071 -0.0120 -0.0012 160 LEU A CG  
1108 C CD1 . LEU A 159 ? 0.1368 0.2125 0.1473 -0.0056 -0.0152 0.0040  160 LEU A CD1 
1109 C CD2 . LEU A 159 ? 0.1617 0.2445 0.1618 -0.0112 -0.0123 -0.0005 160 LEU A CD2 
1110 N N   . ALA A 160 ? 0.1521 0.2248 0.1521 -0.0106 -0.0042 -0.0203 161 ALA A N   
1111 C CA  . ALA A 160 ? 0.1561 0.2264 0.1575 -0.0110 -0.0029 -0.0243 161 ALA A CA  
1112 C C   . ALA A 160 ? 0.1568 0.2328 0.1589 -0.0128 -0.0050 -0.0232 161 ALA A C   
1113 O O   . ALA A 160 ? 0.1639 0.2470 0.1633 -0.0161 -0.0057 -0.0242 161 ALA A O   
1114 C CB  . ALA A 160 ? 0.1593 0.2295 0.1590 -0.0129 -0.0005 -0.0301 161 ALA A CB  
1115 N N   . TYR A 161 ? 0.1473 0.2212 0.1530 -0.0109 -0.0058 -0.0212 162 TYR A N   
1116 C CA  . TYR A 161 ? 0.1412 0.2207 0.1488 -0.0122 -0.0078 -0.0200 162 TYR A CA  
1117 C C   . TYR A 161 ? 0.1358 0.2147 0.1439 -0.0141 -0.0064 -0.0242 162 TYR A C   
1118 O O   . TYR A 161 ? 0.1381 0.2105 0.1473 -0.0130 -0.0043 -0.0265 162 TYR A O   
1119 C CB  . TYR A 161 ? 0.1347 0.2130 0.1471 -0.0091 -0.0092 -0.0160 162 TYR A CB  
1120 C CG  . TYR A 161 ? 0.1458 0.2265 0.1596 -0.0077 -0.0118 -0.0109 162 TYR A CG  
1121 C CD1 . TYR A 161 ? 0.1539 0.2298 0.1675 -0.0056 -0.0113 -0.0093 162 TYR A CD1 
1122 C CD2 . TYR A 161 ? 0.1558 0.2437 0.1721 -0.0085 -0.0150 -0.0072 162 TYR A CD2 
1123 C CE1 . TYR A 161 ? 0.1609 0.2383 0.1766 -0.0046 -0.0137 -0.0043 162 TYR A CE1 
1124 C CE2 . TYR A 161 ? 0.1659 0.2554 0.1845 -0.0072 -0.0177 -0.0016 162 TYR A CE2 
1125 C CZ  . TYR A 161 ? 0.1738 0.2576 0.1922 -0.0053 -0.0170 -0.0003 162 TYR A CZ  
1126 O OH  . TYR A 161 ? 0.1897 0.2743 0.2112 -0.0042 -0.0197 0.0054  162 TYR A OH  
1127 N N   . SER A 162 ? 0.1346 0.2207 0.1427 -0.0169 -0.0080 -0.0246 163 SER A N   
1128 C CA  . SER A 162 ? 0.1362 0.2234 0.1459 -0.0192 -0.0073 -0.0279 163 SER A CA  
1129 C C   . SER A 162 ? 0.1342 0.2266 0.1478 -0.0184 -0.0098 -0.0241 163 SER A C   
1130 O O   . SER A 162 ? 0.1261 0.2263 0.1395 -0.0197 -0.0126 -0.0214 163 SER A O   
1131 C CB  . SER A 162 ? 0.1493 0.2419 0.1555 -0.0237 -0.0073 -0.0321 163 SER A CB  
1132 O OG  . SER A 162 ? 0.1661 0.2588 0.1743 -0.0261 -0.0065 -0.0357 163 SER A OG  
1133 N N   . CYS A 163 ? 0.1442 0.2329 0.1619 -0.0161 -0.0090 -0.0234 164 CYS A N   
1134 C CA  . CYS A 163 ? 0.1656 0.2591 0.1884 -0.0149 -0.0108 -0.0205 164 CYS A CA  
1135 C C   . CYS A 163 ? 0.1795 0.2794 0.2034 -0.0185 -0.0115 -0.0225 164 CYS A C   
1136 O O   . CYS A 163 ? 0.1787 0.2761 0.2008 -0.0211 -0.0097 -0.0265 164 CYS A O   
1137 C CB  . CYS A 163 ? 0.1821 0.2702 0.2084 -0.0117 -0.0090 -0.0202 164 CYS A CB  
1138 S SG  . CYS A 163 ? 0.2400 0.3209 0.2655 -0.0077 -0.0082 -0.0183 164 CYS A SG  
1139 N N   . PHE A 164 ? 0.1866 0.2950 0.2140 -0.0187 -0.0145 -0.0195 165 PHE A N   
1140 C CA  . PHE A 164 ? 0.1960 0.3124 0.2248 -0.0224 -0.0158 -0.0209 165 PHE A CA  
1141 C C   . PHE A 164 ? 0.2135 0.3309 0.2365 -0.0270 -0.0152 -0.0252 165 PHE A C   
1142 O O   . PHE A 164 ? 0.2073 0.3241 0.2303 -0.0301 -0.0137 -0.0294 165 PHE A O   
1143 C CB  . PHE A 164 ? 0.1911 0.3066 0.2246 -0.0222 -0.0142 -0.0225 165 PHE A CB  
1144 C CG  . PHE A 164 ? 0.1884 0.3041 0.2281 -0.0178 -0.0145 -0.0193 165 PHE A CG  
1145 C CD1 . PHE A 164 ? 0.1915 0.3148 0.2366 -0.0161 -0.0177 -0.0154 165 PHE A CD1 
1146 C CD2 . PHE A 164 ? 0.1943 0.3029 0.2348 -0.0153 -0.0116 -0.0202 165 PHE A CD2 
1147 C CE1 . PHE A 164 ? 0.1959 0.3190 0.2478 -0.0118 -0.0178 -0.0133 165 PHE A CE1 
1148 C CE2 . PHE A 164 ? 0.2008 0.3101 0.2472 -0.0114 -0.0115 -0.0184 165 PHE A CE2 
1149 C CZ  . PHE A 164 ? 0.1935 0.3099 0.2460 -0.0096 -0.0144 -0.0153 165 PHE A CZ  
1150 N N   . ASP A 165 ? 0.2357 0.3540 0.2541 -0.0275 -0.0159 -0.0245 166 ASP A N   
1151 C CA  . ASP A 165 ? 0.2712 0.3905 0.2839 -0.0315 -0.0148 -0.0292 166 ASP A CA  
1152 C C   . ASP A 165 ? 0.3103 0.4388 0.3218 -0.0368 -0.0163 -0.0322 166 ASP A C   
1153 O O   . ASP A 165 ? 0.3128 0.4390 0.3234 -0.0398 -0.0141 -0.0382 166 ASP A O   
1154 C CB  . ASP A 165 ? 0.2922 0.4126 0.3006 -0.0309 -0.0156 -0.0270 166 ASP A CB  
1155 C CG  . ASP A 165 ? 0.3679 0.4874 0.3709 -0.0340 -0.0132 -0.0328 166 ASP A CG  
1156 O OD1 . ASP A 165 ? 0.3794 0.4907 0.3830 -0.0335 -0.0101 -0.0375 166 ASP A OD1 
1157 O OD2 . ASP A 165 ? 0.4007 0.5282 0.3993 -0.0370 -0.0146 -0.0326 166 ASP A OD2 
1158 N N   . GLU A 166 ? 0.3330 0.4721 0.3453 -0.0380 -0.0201 -0.0279 167 GLU A N   
1159 C CA  . GLU A 166 ? 0.3579 0.5076 0.3688 -0.0433 -0.0221 -0.0301 167 GLU A CA  
1160 C C   . GLU A 166 ? 0.3717 0.5270 0.3887 -0.0434 -0.0243 -0.0278 167 GLU A C   
1161 O O   . GLU A 166 ? 0.3579 0.5191 0.3749 -0.0478 -0.0247 -0.0314 167 GLU A O   
1162 C CB  . GLU A 166 ? 0.3991 0.5587 0.4053 -0.0456 -0.0252 -0.0268 167 GLU A CB  
1163 C CG  . GLU A 166 ? 0.4806 0.6362 0.4806 -0.0460 -0.0229 -0.0292 167 GLU A CG  
1164 C CD  . GLU A 166 ? 0.5877 0.7529 0.5830 -0.0480 -0.0258 -0.0247 167 GLU A CD  
1165 O OE1 . GLU A 166 ? 0.6065 0.7796 0.6043 -0.0479 -0.0302 -0.0178 167 GLU A OE1 
1166 O OE2 . GLU A 166 ? 0.6285 0.7935 0.6180 -0.0498 -0.0238 -0.0278 167 GLU A OE2 
1167 N N   . GLU A 167 ? 0.3978 0.5521 0.4207 -0.0386 -0.0257 -0.0220 168 GLU A N   
1168 C CA  . GLU A 167 ? 0.4253 0.5853 0.4556 -0.0378 -0.0276 -0.0196 168 GLU A CA  
1169 C C   . GLU A 167 ? 0.4615 0.6129 0.4954 -0.0357 -0.0239 -0.0225 168 GLU A C   
1170 O O   . GLU A 167 ? 0.4620 0.6056 0.4976 -0.0313 -0.0222 -0.0210 168 GLU A O   
1171 C CB  . GLU A 167 ? 0.4435 0.6079 0.4792 -0.0338 -0.0312 -0.0121 168 GLU A CB  
1172 C CG  . GLU A 167 ? 0.4939 0.6687 0.5265 -0.0367 -0.0355 -0.0081 168 GLU A CG  
1173 C CD  . GLU A 167 ? 0.5678 0.7471 0.6066 -0.0330 -0.0397 0.0002  168 GLU A CD  
1174 O OE1 . GLU A 167 ? 0.5896 0.7697 0.6374 -0.0295 -0.0406 0.0025  168 GLU A OE1 
1175 O OE2 . GLU A 167 ? 0.5884 0.7707 0.6235 -0.0338 -0.0422 0.0045  168 GLU A OE2 
1176 N N   . ASN A 168 ? 0.4940 0.6472 0.5285 -0.0396 -0.0228 -0.0269 169 ASN A N   
1177 C CA  . ASN A 168 ? 0.5202 0.6658 0.5569 -0.0394 -0.0192 -0.0300 169 ASN A CA  
1178 C C   . ASN A 168 ? 0.5224 0.6747 0.5655 -0.0411 -0.0197 -0.0301 169 ASN A C   
1179 O O   . ASN A 168 ? 0.5279 0.6817 0.5769 -0.0375 -0.0199 -0.0270 169 ASN A O   
1180 C CB  . ASN A 168 ? 0.5534 0.6914 0.5846 -0.0427 -0.0163 -0.0359 169 ASN A CB  
1181 C CG  . ASN A 168 ? 0.6167 0.7613 0.6448 -0.0488 -0.0174 -0.0404 169 ASN A CG  
1182 O OD1 . ASN A 168 ? 0.6531 0.7932 0.6806 -0.0522 -0.0151 -0.0458 169 ASN A OD1 
1183 N ND2 . ASN A 168 ? 0.6083 0.7636 0.6347 -0.0505 -0.0208 -0.0384 169 ASN A ND2 
1184 N N   . GLY A 169 ? 0.5127 0.6692 0.5549 -0.0466 -0.0199 -0.0341 170 GLY A N   
1185 C CA  . GLY A 169 ? 0.5019 0.6645 0.5499 -0.0491 -0.0201 -0.0347 170 GLY A CA  
1186 C C   . GLY A 169 ? 0.4897 0.6432 0.5390 -0.0492 -0.0161 -0.0370 170 GLY A C   
1187 O O   . GLY A 169 ? 0.4961 0.6415 0.5417 -0.0517 -0.0139 -0.0409 170 GLY A O   
1188 N N   . ASN A 170 ? 0.4708 0.6258 0.5259 -0.0464 -0.0153 -0.0344 171 ASN A N   
1189 C CA  . ASN A 170 ? 0.4616 0.6099 0.5183 -0.0465 -0.0117 -0.0353 171 ASN A CA  
1190 C C   . ASN A 170 ? 0.4244 0.5647 0.4799 -0.0410 -0.0099 -0.0330 171 ASN A C   
1191 O O   . ASN A 170 ? 0.4294 0.5687 0.4880 -0.0394 -0.0077 -0.0320 171 ASN A O   
1192 C CB  . ASN A 170 ? 0.4961 0.6535 0.5600 -0.0476 -0.0117 -0.0344 171 ASN A CB  
1193 C CG  . ASN A 170 ? 0.5695 0.7345 0.6353 -0.0536 -0.0131 -0.0369 171 ASN A CG  
1194 O OD1 . ASN A 170 ? 0.5994 0.7614 0.6611 -0.0579 -0.0132 -0.0402 171 ASN A OD1 
1195 N ND2 . ASN A 170 ? 0.5801 0.7557 0.6529 -0.0542 -0.0139 -0.0356 171 ASN A ND2 
1196 N N   . ASN A 171 ? 0.3810 0.5167 0.4320 -0.0384 -0.0107 -0.0323 172 ASN A N   
1197 C CA  . ASN A 171 ? 0.3431 0.4717 0.3929 -0.0334 -0.0093 -0.0303 172 ASN A CA  
1198 C C   . ASN A 171 ? 0.3164 0.4337 0.3617 -0.0342 -0.0064 -0.0322 172 ASN A C   
1199 O O   . ASN A 171 ? 0.3273 0.4402 0.3682 -0.0359 -0.0064 -0.0344 172 ASN A O   
1200 C CB  . ASN A 171 ? 0.3360 0.4656 0.3837 -0.0304 -0.0118 -0.0280 172 ASN A CB  
1201 C CG  . ASN A 171 ? 0.3358 0.4610 0.3846 -0.0249 -0.0111 -0.0253 172 ASN A CG  
1202 O OD1 . ASN A 171 ? 0.3455 0.4641 0.3938 -0.0234 -0.0084 -0.0259 172 ASN A OD1 
1203 N ND2 . ASN A 171 ? 0.3307 0.4596 0.3813 -0.0220 -0.0138 -0.0221 172 ASN A ND2 
1204 N N   . PRO A 172 ? 0.2792 0.3922 0.3258 -0.0329 -0.0039 -0.0314 173 PRO A N   
1205 C CA  . PRO A 172 ? 0.2596 0.3621 0.3025 -0.0334 -0.0016 -0.0322 173 PRO A CA  
1206 C C   . PRO A 172 ? 0.2299 0.3256 0.2687 -0.0298 -0.0016 -0.0315 173 PRO A C   
1207 O O   . PRO A 172 ? 0.2282 0.3157 0.2641 -0.0303 -0.0003 -0.0325 173 PRO A O   
1208 C CB  . PRO A 172 ? 0.2699 0.3723 0.3153 -0.0329 0.0006  -0.0306 173 PRO A CB  
1209 C CG  . PRO A 172 ? 0.2756 0.3862 0.3252 -0.0297 -0.0002 -0.0292 173 PRO A CG  
1210 C CD  . PRO A 172 ? 0.2601 0.3785 0.3119 -0.0309 -0.0030 -0.0297 173 PRO A CD  
1211 N N   . TRP A 173 ? 0.2035 0.3027 0.2427 -0.0262 -0.0032 -0.0297 174 TRP A N   
1212 C CA  . TRP A 173 ? 0.1919 0.2856 0.2277 -0.0230 -0.0034 -0.0287 174 TRP A CA  
1213 C C   . TRP A 173 ? 0.2020 0.2965 0.2342 -0.0241 -0.0051 -0.0299 174 TRP A C   
1214 O O   . TRP A 173 ? 0.2083 0.2993 0.2377 -0.0217 -0.0053 -0.0289 174 TRP A O   
1215 C CB  . TRP A 173 ? 0.1741 0.2701 0.2127 -0.0185 -0.0039 -0.0260 174 TRP A CB  
1216 C CG  . TRP A 173 ? 0.1558 0.2505 0.1967 -0.0174 -0.0016 -0.0258 174 TRP A CG  
1217 C CD1 . TRP A 173 ? 0.1600 0.2477 0.1981 -0.0173 0.0006  -0.0260 174 TRP A CD1 
1218 C CD2 . TRP A 173 ? 0.1495 0.2513 0.1961 -0.0169 -0.0013 -0.0255 174 TRP A CD2 
1219 N NE1 . TRP A 173 ? 0.1589 0.2492 0.1997 -0.0171 0.0024  -0.0257 174 TRP A NE1 
1220 C CE2 . TRP A 173 ? 0.1541 0.2531 0.2003 -0.0167 0.0015  -0.0258 174 TRP A CE2 
1221 C CE3 . TRP A 173 ? 0.1487 0.2598 0.2011 -0.0165 -0.0031 -0.0250 174 TRP A CE3 
1222 C CZ2 . TRP A 173 ? 0.1552 0.2605 0.2063 -0.0162 0.0029  -0.0262 174 TRP A CZ2 
1223 C CZ3 . TRP A 173 ? 0.1507 0.2675 0.2088 -0.0156 -0.0018 -0.0253 174 TRP A CZ3 
1224 C CH2 . TRP A 173 ? 0.1522 0.2662 0.2095 -0.0155 0.0014  -0.0262 174 TRP A CH2 
1225 N N   . SER A 174 ? 0.2036 0.3030 0.2357 -0.0281 -0.0061 -0.0321 175 SER A N   
1226 C CA  . SER A 174 ? 0.2151 0.3169 0.2434 -0.0302 -0.0075 -0.0340 175 SER A CA  
1227 C C   . SER A 174 ? 0.2203 0.3136 0.2444 -0.0297 -0.0056 -0.0363 175 SER A C   
1228 O O   . SER A 174 ? 0.2282 0.3141 0.2528 -0.0303 -0.0034 -0.0381 175 SER A O   
1229 C CB  . SER A 174 ? 0.2335 0.3407 0.2622 -0.0354 -0.0081 -0.0375 175 SER A CB  
1230 O OG  . SER A 174 ? 0.2789 0.3941 0.3121 -0.0358 -0.0097 -0.0353 175 SER A OG  
1231 N N   . LYS A 175 ? 0.2107 0.3056 0.2314 -0.0288 -0.0067 -0.0358 176 LYS A N   
1232 C CA  . LYS A 175 ? 0.2150 0.3039 0.2322 -0.0282 -0.0051 -0.0379 176 LYS A CA  
1233 C C   . LYS A 175 ? 0.2096 0.2888 0.2275 -0.0248 -0.0030 -0.0368 176 LYS A C   
1234 O O   . LYS A 175 ? 0.2173 0.2900 0.2344 -0.0251 -0.0012 -0.0397 176 LYS A O   
1235 C CB  . LYS A 175 ? 0.2451 0.3338 0.2608 -0.0324 -0.0040 -0.0439 176 LYS A CB  
1236 C CG  . LYS A 175 ? 0.2905 0.3897 0.3038 -0.0361 -0.0061 -0.0454 176 LYS A CG  
1237 C CD  . LYS A 175 ? 0.3212 0.4202 0.3332 -0.0405 -0.0046 -0.0525 176 LYS A CD  
1238 C CE  . LYS A 175 ? 0.3550 0.4656 0.3636 -0.0446 -0.0066 -0.0542 176 LYS A CE  
1239 N NZ  . LYS A 175 ? 0.3623 0.4772 0.3663 -0.0435 -0.0075 -0.0521 176 LYS A NZ  
1240 N N   . THR A 176 ? 0.1957 0.2743 0.2157 -0.0215 -0.0034 -0.0328 177 THR A N   
1241 C CA  . THR A 176 ? 0.1888 0.2599 0.2091 -0.0185 -0.0017 -0.0313 177 THR A CA  
1242 C C   . THR A 176 ? 0.1651 0.2338 0.1827 -0.0159 -0.0020 -0.0302 177 THR A C   
1243 O O   . THR A 176 ? 0.1543 0.2274 0.1717 -0.0146 -0.0037 -0.0277 177 THR A O   
1244 C CB  . THR A 176 ? 0.2117 0.2843 0.2354 -0.0165 -0.0018 -0.0285 177 THR A CB  
1245 O OG1 . THR A 176 ? 0.2335 0.3068 0.2593 -0.0192 -0.0009 -0.0297 177 THR A OG1 
1246 C CG2 . THR A 176 ? 0.2190 0.2856 0.2423 -0.0134 -0.0005 -0.0269 177 THR A CG2 
1247 N N   . LYS A 177 ? 0.1583 0.2203 0.1745 -0.0152 -0.0003 -0.0316 178 LYS A N   
1248 C CA  . LYS A 177 ? 0.1471 0.2073 0.1610 -0.0131 -0.0003 -0.0309 178 LYS A CA  
1249 C C   . LYS A 177 ? 0.1269 0.1837 0.1414 -0.0096 -0.0002 -0.0275 178 LYS A C   
1250 O O   . LYS A 177 ? 0.1269 0.1791 0.1426 -0.0087 0.0009  -0.0272 178 LYS A O   
1251 C CB  . LYS A 177 ? 0.1611 0.2168 0.1739 -0.0141 0.0014  -0.0346 178 LYS A CB  
1252 C CG  . LYS A 177 ? 0.2141 0.2746 0.2257 -0.0177 0.0013  -0.0387 178 LYS A CG  
1253 C CD  . LYS A 177 ? 0.2998 0.3550 0.3127 -0.0191 0.0034  -0.0437 178 LYS A CD  
1254 C CE  . LYS A 177 ? 0.3568 0.4167 0.3675 -0.0216 0.0039  -0.0484 178 LYS A CE  
1255 N NZ  . LYS A 177 ? 0.4097 0.4700 0.4181 -0.0196 0.0044  -0.0479 178 LYS A NZ  
1256 N N   . ILE A 178 ? 0.1106 0.1701 0.1246 -0.0079 -0.0017 -0.0250 179 ILE A N   
1257 C CA  . ILE A 178 ? 0.1049 0.1616 0.1200 -0.0047 -0.0018 -0.0223 179 ILE A CA  
1258 C C   . ILE A 178 ? 0.1163 0.1724 0.1291 -0.0038 -0.0022 -0.0213 179 ILE A C   
1259 O O   . ILE A 178 ? 0.1166 0.1775 0.1280 -0.0053 -0.0036 -0.0207 179 ILE A O   
1260 C CB  . ILE A 178 ? 0.0987 0.1593 0.1174 -0.0033 -0.0032 -0.0200 179 ILE A CB  
1261 C CG1 . ILE A 178 ? 0.0990 0.1613 0.1202 -0.0043 -0.0024 -0.0211 179 ILE A CG1 
1262 C CG2 . ILE A 178 ? 0.0971 0.1547 0.1173 -0.0001 -0.0032 -0.0180 179 ILE A CG2 
1263 C CD1 . ILE A 178 ? 0.0993 0.1568 0.1204 -0.0039 -0.0003 -0.0219 179 ILE A CD1 
1264 N N   . GLU A 179 ? 0.1215 0.1725 0.1338 -0.0019 -0.0013 -0.0210 180 GLU A N   
1265 C CA  . GLU A 179 ? 0.1387 0.1893 0.1493 -0.0013 -0.0015 -0.0200 180 GLU A CA  
1266 C C   . GLU A 179 ? 0.1518 0.2025 0.1642 0.0008  -0.0029 -0.0166 180 GLU A C   
1267 O O   . GLU A 179 ? 0.1612 0.2095 0.1759 0.0026  -0.0027 -0.0162 180 GLU A O   
1268 C CB  . GLU A 179 ? 0.1690 0.2145 0.1786 -0.0006 0.0003  -0.0217 180 GLU A CB  
1269 C CG  . GLU A 179 ? 0.2461 0.2918 0.2540 -0.0002 0.0003  -0.0211 180 GLU A CG  
1270 C CD  . GLU A 179 ? 0.3573 0.3983 0.3654 0.0010  0.0017  -0.0223 180 GLU A CD  
1271 O OE1 . GLU A 179 ? 0.3793 0.4173 0.3884 0.0028  0.0016  -0.0207 180 GLU A OE1 
1272 O OE2 . GLU A 179 ? 0.3953 0.4362 0.4032 0.0000  0.0030  -0.0252 180 GLU A OE2 
1273 N N   . VAL A 180 ? 0.1487 0.2023 0.1603 0.0004  -0.0044 -0.0143 181 VAL A N   
1274 C CA  . VAL A 180 ? 0.1500 0.2028 0.1643 0.0023  -0.0059 -0.0109 181 VAL A CA  
1275 C C   . VAL A 180 ? 0.1439 0.1946 0.1562 0.0024  -0.0056 -0.0101 181 VAL A C   
1276 O O   . VAL A 180 ? 0.1569 0.2111 0.1664 0.0004  -0.0058 -0.0096 181 VAL A O   
1277 C CB  . VAL A 180 ? 0.1614 0.2194 0.1782 0.0019  -0.0087 -0.0075 181 VAL A CB  
1278 C CG1 . VAL A 180 ? 0.1744 0.2310 0.1945 0.0035  -0.0105 -0.0036 181 VAL A CG1 
1279 C CG2 . VAL A 180 ? 0.1588 0.2186 0.1791 0.0025  -0.0089 -0.0083 181 VAL A CG2 
1280 N N   . GLN A 181 ? 0.1256 0.1716 0.1392 0.0043  -0.0049 -0.0101 182 GLN A N   
1281 C CA  . GLN A 181 ? 0.1180 0.1622 0.1303 0.0044  -0.0046 -0.0093 182 GLN A CA  
1282 C C   . GLN A 181 ? 0.1246 0.1685 0.1400 0.0051  -0.0066 -0.0056 182 GLN A C   
1283 O O   . GLN A 181 ? 0.1238 0.1656 0.1432 0.0070  -0.0072 -0.0052 182 GLN A O   
1284 C CB  . GLN A 181 ? 0.1240 0.1636 0.1361 0.0057  -0.0028 -0.0117 182 GLN A CB  
1285 C CG  . GLN A 181 ? 0.1291 0.1682 0.1391 0.0049  -0.0010 -0.0147 182 GLN A CG  
1286 C CD  . GLN A 181 ? 0.1262 0.1611 0.1365 0.0062  0.0001  -0.0159 182 GLN A CD  
1287 O OE1 . GLN A 181 ? 0.1426 0.1754 0.1540 0.0074  -0.0003 -0.0150 182 GLN A OE1 
1288 N NE2 . GLN A 181 ? 0.0802 0.1138 0.0899 0.0058  0.0013  -0.0179 182 GLN A NE2 
1289 N N   . LEU A 182 ? 0.1316 0.1777 0.1456 0.0036  -0.0074 -0.0030 183 LEU A N   
1290 C CA  . LEU A 182 ? 0.1406 0.1860 0.1579 0.0038  -0.0095 0.0012  183 LEU A CA  
1291 C C   . LEU A 182 ? 0.1436 0.1866 0.1597 0.0035  -0.0086 0.0011  183 LEU A C   
1292 O O   . LEU A 182 ? 0.1453 0.1908 0.1576 0.0019  -0.0073 0.0000  183 LEU A O   
1293 C CB  . LEU A 182 ? 0.1467 0.1979 0.1634 0.0015  -0.0118 0.0056  183 LEU A CB  
1294 C CG  . LEU A 182 ? 0.1716 0.2264 0.1898 0.0015  -0.0133 0.0063  183 LEU A CG  
1295 C CD1 . LEU A 182 ? 0.1738 0.2353 0.1910 -0.0012 -0.0159 0.0112  183 LEU A CD1 
1296 C CD2 . LEU A 182 ? 0.1856 0.2368 0.2107 0.0046  -0.0143 0.0067  183 LEU A CD2 
1297 N N   . ARG A 183 ? 0.1481 0.1864 0.1680 0.0052  -0.0090 0.0015  184 ARG A N   
1298 C CA  . ARG A 183 ? 0.1518 0.1877 0.1712 0.0049  -0.0082 0.0011  184 ARG A CA  
1299 C C   . ARG A 183 ? 0.1456 0.1783 0.1700 0.0053  -0.0100 0.0039  184 ARG A C   
1300 O O   . ARG A 183 ? 0.1430 0.1733 0.1719 0.0071  -0.0110 0.0039  184 ARG A O   
1301 C CB  . ARG A 183 ? 0.1702 0.2027 0.1892 0.0067  -0.0064 -0.0032 184 ARG A CB  
1302 C CG  . ARG A 183 ? 0.2326 0.2664 0.2477 0.0061  -0.0045 -0.0056 184 ARG A CG  
1303 C CD  . ARG A 183 ? 0.2612 0.2939 0.2758 0.0073  -0.0035 -0.0084 184 ARG A CD  
1304 N NE  . ARG A 183 ? 0.2456 0.2752 0.2608 0.0085  -0.0027 -0.0103 184 ARG A NE  
1305 C CZ  . ARG A 183 ? 0.2322 0.2612 0.2457 0.0088  -0.0015 -0.0123 184 ARG A CZ  
1306 N NH1 . ARG A 183 ? 0.1834 0.2139 0.1952 0.0082  -0.0006 -0.0132 184 ARG A NH1 
1307 N NH2 . ARG A 183 ? 0.2457 0.2728 0.2594 0.0094  -0.0012 -0.0134 184 ARG A NH2 
1308 N N   . THR A 184 ? 0.1386 0.1707 0.1627 0.0040  -0.0100 0.0054  185 THR A N   
1309 C CA  . THR A 184 ? 0.1441 0.1721 0.1734 0.0042  -0.0115 0.0072  185 THR A CA  
1310 C C   . THR A 184 ? 0.1519 0.1758 0.1821 0.0059  -0.0100 0.0025  185 THR A C   
1311 O O   . THR A 184 ? 0.1458 0.1706 0.1723 0.0064  -0.0081 -0.0010 185 THR A O   
1312 C CB  . THR A 184 ? 0.1409 0.1707 0.1699 0.0014  -0.0125 0.0115  185 THR A CB  
1313 O OG1 . THR A 184 ? 0.1500 0.1809 0.1755 0.0006  -0.0104 0.0090  185 THR A OG1 
1314 C CG2 . THR A 184 ? 0.1363 0.1718 0.1631 -0.0009 -0.0138 0.0161  185 THR A CG2 
1315 N N   . GLU A 185 ? 0.1691 0.1888 0.2046 0.0064  -0.0109 0.0024  186 GLU A N   
1316 C CA  . GLU A 185 ? 0.1885 0.2053 0.2248 0.0074  -0.0097 -0.0021 186 GLU A CA  
1317 C C   . GLU A 185 ? 0.1848 0.2031 0.2169 0.0060  -0.0085 -0.0032 186 GLU A C   
1318 O O   . GLU A 185 ? 0.1931 0.2115 0.2229 0.0068  -0.0071 -0.0068 186 GLU A O   
1319 C CB  . GLU A 185 ? 0.2346 0.2469 0.2781 0.0077  -0.0111 -0.0022 186 GLU A CB  
1320 C CG  . GLU A 185 ? 0.3493 0.3598 0.3985 0.0099  -0.0118 -0.0030 186 GLU A CG  
1321 C CD  . GLU A 185 ? 0.5057 0.5112 0.5633 0.0106  -0.0129 -0.0043 186 GLU A CD  
1322 O OE1 . GLU A 185 ? 0.5369 0.5402 0.5948 0.0094  -0.0123 -0.0066 186 GLU A OE1 
1323 O OE2 . GLU A 185 ? 0.5632 0.5669 0.6278 0.0122  -0.0142 -0.0032 186 GLU A OE2 
1324 N N   . LEU A 186 ? 0.1710 0.1911 0.2021 0.0039  -0.0090 0.0002  187 LEU A N   
1325 C CA  . LEU A 186 ? 0.1567 0.1791 0.1847 0.0027  -0.0078 -0.0007 187 LEU A CA  
1326 C C   . LEU A 186 ? 0.1474 0.1736 0.1707 0.0032  -0.0062 -0.0022 187 LEU A C   
1327 O O   . LEU A 186 ? 0.1557 0.1825 0.1773 0.0037  -0.0051 -0.0048 187 LEU A O   
1328 C CB  . LEU A 186 ? 0.1564 0.1801 0.1857 0.0000  -0.0088 0.0032  187 LEU A CB  
1329 C CG  . LEU A 186 ? 0.1670 0.1933 0.1949 -0.0015 -0.0077 0.0023  187 LEU A CG  
1330 C CD1 . LEU A 186 ? 0.1653 0.1883 0.1953 -0.0009 -0.0078 -0.0010 187 LEU A CD1 
1331 C CD2 . LEU A 186 ? 0.1673 0.1965 0.1959 -0.0046 -0.0084 0.0068  187 LEU A CD2 
1332 N N   . GLN A 187 ? 0.1372 0.1658 0.1587 0.0031  -0.0061 -0.0009 188 GLN A N   
1333 C CA  . GLN A 187 ? 0.1344 0.1658 0.1522 0.0037  -0.0045 -0.0031 188 GLN A CA  
1334 C C   . GLN A 187 ? 0.1446 0.1733 0.1622 0.0058  -0.0038 -0.0064 188 GLN A C   
1335 O O   . GLN A 187 ? 0.1551 0.1847 0.1710 0.0063  -0.0026 -0.0084 188 GLN A O   
1336 C CB  . GLN A 187 ? 0.1349 0.1695 0.1510 0.0029  -0.0048 -0.0016 188 GLN A CB  
1337 C CG  . GLN A 187 ? 0.1388 0.1785 0.1530 0.0003  -0.0046 0.0008  188 GLN A CG  
1338 C CD  . GLN A 187 ? 0.1516 0.1949 0.1646 -0.0012 -0.0058 0.0036  188 GLN A CD  
1339 O OE1 . GLN A 187 ? 0.1555 0.1969 0.1703 -0.0002 -0.0073 0.0048  188 GLN A OE1 
1340 N NE2 . GLN A 187 ? 0.1501 0.1996 0.1600 -0.0039 -0.0051 0.0046  188 GLN A NE2 
1341 N N   . HIS A 188 ? 0.1449 0.1707 0.1648 0.0068  -0.0047 -0.0068 189 HIS A N   
1342 C CA  . HIS A 188 ? 0.1332 0.1575 0.1530 0.0083  -0.0040 -0.0098 189 HIS A CA  
1343 C C   . HIS A 188 ? 0.1339 0.1572 0.1534 0.0082  -0.0036 -0.0117 189 HIS A C   
1344 O O   . HIS A 188 ? 0.1431 0.1670 0.1606 0.0087  -0.0028 -0.0133 189 HIS A O   
1345 C CB  . HIS A 188 ? 0.1210 0.1436 0.1441 0.0093  -0.0047 -0.0102 189 HIS A CB  
1346 C CG  . HIS A 188 ? 0.1296 0.1521 0.1521 0.0104  -0.0036 -0.0133 189 HIS A CG  
1347 N ND1 . HIS A 188 ? 0.1452 0.1695 0.1648 0.0105  -0.0027 -0.0139 189 HIS A ND1 
1348 C CD2 . HIS A 188 ? 0.1413 0.1627 0.1659 0.0109  -0.0033 -0.0160 189 HIS A CD2 
1349 C CE1 . HIS A 188 ? 0.1524 0.1766 0.1720 0.0110  -0.0019 -0.0163 189 HIS A CE1 
1350 N NE2 . HIS A 188 ? 0.1569 0.1799 0.1793 0.0112  -0.0021 -0.0179 189 HIS A NE2 
1351 N N   . ALA A 189 ? 0.1298 0.1521 0.1515 0.0074  -0.0044 -0.0111 190 ALA A N   
1352 C CA  . ALA A 189 ? 0.1337 0.1559 0.1554 0.0068  -0.0043 -0.0127 190 ALA A CA  
1353 C C   . ALA A 189 ? 0.1404 0.1654 0.1596 0.0066  -0.0037 -0.0123 190 ALA A C   
1354 O O   . ALA A 189 ? 0.1430 0.1687 0.1611 0.0067  -0.0036 -0.0136 190 ALA A O   
1355 C CB  . ALA A 189 ? 0.1347 0.1553 0.1598 0.0055  -0.0054 -0.0117 190 ALA A CB  
1356 N N   . TRP A 190 ? 0.1387 0.1656 0.1573 0.0062  -0.0033 -0.0105 191 TRP A N   
1357 C CA  . TRP A 190 ? 0.1350 0.1647 0.1526 0.0064  -0.0024 -0.0107 191 TRP A CA  
1358 C C   . TRP A 190 ? 0.1507 0.1799 0.1668 0.0078  -0.0018 -0.0120 191 TRP A C   
1359 O O   . TRP A 190 ? 0.1588 0.1888 0.1751 0.0084  -0.0017 -0.0124 191 TRP A O   
1360 C CB  . TRP A 190 ? 0.1218 0.1543 0.1390 0.0054  -0.0017 -0.0093 191 TRP A CB  
1361 C CG  . TRP A 190 ? 0.0989 0.1347 0.1162 0.0057  -0.0004 -0.0104 191 TRP A CG  
1362 C CD1 . TRP A 190 ? 0.1003 0.1390 0.1193 0.0052  0.0000  -0.0105 191 TRP A CD1 
1363 C CD2 . TRP A 190 ? 0.0839 0.1203 0.1004 0.0068  0.0007  -0.0121 191 TRP A CD2 
1364 N NE1 . TRP A 190 ? 0.1019 0.1430 0.1218 0.0063  0.0013  -0.0122 191 TRP A NE1 
1365 C CE2 . TRP A 190 ? 0.0927 0.1319 0.1112 0.0072  0.0018  -0.0133 191 TRP A CE2 
1366 C CE3 . TRP A 190 ? 0.0776 0.1123 0.0926 0.0074  0.0010  -0.0129 191 TRP A CE3 
1367 C CZ2 . TRP A 190 ? 0.0906 0.1306 0.1102 0.0084  0.0031  -0.0155 191 TRP A CZ2 
1368 C CZ3 . TRP A 190 ? 0.0837 0.1191 0.0992 0.0082  0.0022  -0.0148 191 TRP A CZ3 
1369 C CH2 . TRP A 190 ? 0.0826 0.1202 0.1005 0.0087  0.0032  -0.0162 191 TRP A CH2 
1370 N N   . ALA A 191 ? 0.1584 0.1866 0.1735 0.0082  -0.0015 -0.0122 192 ALA A N   
1371 C CA  . ALA A 191 ? 0.1614 0.1891 0.1753 0.0091  -0.0009 -0.0131 192 ALA A CA  
1372 C C   . ALA A 191 ? 0.1720 0.1986 0.1854 0.0094  -0.0013 -0.0138 192 ALA A C   
1373 O O   . ALA A 191 ? 0.1751 0.2018 0.1880 0.0098  -0.0011 -0.0137 192 ALA A O   
1374 C CB  . ALA A 191 ? 0.1528 0.1803 0.1660 0.0090  -0.0007 -0.0131 192 ALA A CB  
1375 N N   . THR A 192 ? 0.1695 0.1954 0.1833 0.0091  -0.0018 -0.0144 193 THR A N   
1376 C CA  . THR A 192 ? 0.1665 0.1927 0.1793 0.0088  -0.0020 -0.0157 193 THR A CA  
1377 C C   . THR A 192 ? 0.1654 0.1932 0.1780 0.0083  -0.0027 -0.0151 193 THR A C   
1378 O O   . THR A 192 ? 0.1722 0.2013 0.1834 0.0081  -0.0029 -0.0146 193 THR A O   
1379 C CB  . THR A 192 ? 0.1753 0.2006 0.1898 0.0085  -0.0022 -0.0175 193 THR A CB  
1380 O OG1 . THR A 192 ? 0.1826 0.2068 0.1984 0.0092  -0.0019 -0.0176 193 THR A OG1 
1381 C CG2 . THR A 192 ? 0.1797 0.2065 0.1930 0.0077  -0.0021 -0.0197 193 THR A CG2 
1382 N N   . SER A 193 ? 0.1572 0.1854 0.1713 0.0079  -0.0031 -0.0146 194 SER A N   
1383 C CA  . SER A 193 ? 0.1597 0.1902 0.1744 0.0075  -0.0039 -0.0139 194 SER A CA  
1384 C C   . SER A 193 ? 0.1669 0.1983 0.1822 0.0085  -0.0038 -0.0123 194 SER A C   
1385 O O   . SER A 193 ? 0.1715 0.2047 0.1869 0.0085  -0.0048 -0.0113 194 SER A O   
1386 C CB  . SER A 193 ? 0.1736 0.2046 0.1903 0.0066  -0.0043 -0.0137 194 SER A CB  
1387 O OG  . SER A 193 ? 0.1986 0.2279 0.2159 0.0056  -0.0046 -0.0151 194 SER A OG  
1388 N N   . LEU A 194 ? 0.1659 0.1964 0.1818 0.0094  -0.0028 -0.0123 195 LEU A N   
1389 C CA  . LEU A 194 ? 0.1717 0.2024 0.1893 0.0106  -0.0024 -0.0116 195 LEU A CA  
1390 C C   . LEU A 194 ? 0.1921 0.2216 0.2085 0.0107  -0.0029 -0.0108 195 LEU A C   
1391 O O   . LEU A 194 ? 0.2014 0.2315 0.2196 0.0112  -0.0037 -0.0091 195 LEU A O   
1392 C CB  . LEU A 194 ? 0.1639 0.1944 0.1823 0.0110  -0.0009 -0.0127 195 LEU A CB  
1393 C CG  . LEU A 194 ? 0.1752 0.2049 0.1956 0.0122  -0.0002 -0.0132 195 LEU A CG  
1394 C CD1 . LEU A 194 ? 0.1749 0.2063 0.1998 0.0133  -0.0005 -0.0128 195 LEU A CD1 
1395 C CD2 . LEU A 194 ? 0.1823 0.2121 0.2022 0.0119  0.0013  -0.0150 195 LEU A CD2 
1396 N N   . GLU A 195 ? 0.2014 0.2297 0.2152 0.0101  -0.0025 -0.0115 196 GLU A N   
1397 C CA  . GLU A 195 ? 0.2180 0.2459 0.2304 0.0097  -0.0027 -0.0105 196 GLU A CA  
1398 C C   . GLU A 195 ? 0.2181 0.2486 0.2291 0.0086  -0.0041 -0.0092 196 GLU A C   
1399 O O   . GLU A 195 ? 0.2101 0.2412 0.2213 0.0083  -0.0050 -0.0067 196 GLU A O   
1400 C CB  . GLU A 195 ? 0.2669 0.2940 0.2774 0.0092  -0.0018 -0.0118 196 GLU A CB  
1401 C CG  . GLU A 195 ? 0.3783 0.4051 0.3880 0.0086  -0.0018 -0.0104 196 GLU A CG  
1402 C CD  . GLU A 195 ? 0.5529 0.5788 0.5620 0.0084  -0.0007 -0.0115 196 GLU A CD  
1403 O OE1 . GLU A 195 ? 0.6057 0.6305 0.6158 0.0091  -0.0001 -0.0127 196 GLU A OE1 
1404 O OE2 . GLU A 195 ? 0.5971 0.6241 0.6045 0.0072  -0.0005 -0.0111 196 GLU A OE2 
1405 N N   . ILE A 196 ? 0.2236 0.2556 0.2335 0.0077  -0.0044 -0.0106 197 ILE A N   
1406 C CA  . ILE A 196 ? 0.2351 0.2706 0.2434 0.0062  -0.0057 -0.0100 197 ILE A CA  
1407 C C   . ILE A 196 ? 0.2518 0.2890 0.2624 0.0067  -0.0073 -0.0070 197 ILE A C   
1408 O O   . ILE A 196 ? 0.2593 0.2985 0.2692 0.0059  -0.0086 -0.0043 197 ILE A O   
1409 C CB  . ILE A 196 ? 0.2373 0.2738 0.2449 0.0051  -0.0055 -0.0130 197 ILE A CB  
1410 C CG1 . ILE A 196 ? 0.2478 0.2832 0.2540 0.0048  -0.0041 -0.0158 197 ILE A CG1 
1411 C CG2 . ILE A 196 ? 0.2397 0.2806 0.2456 0.0032  -0.0070 -0.0128 197 ILE A CG2 
1412 C CD1 . ILE A 196 ? 0.2578 0.2927 0.2652 0.0043  -0.0038 -0.0192 197 ILE A CD1 
1413 N N   . ILE A 197 ? 0.2526 0.2893 0.2665 0.0079  -0.0073 -0.0071 198 ILE A N   
1414 C CA  . ILE A 197 ? 0.2582 0.2970 0.2759 0.0087  -0.0088 -0.0047 198 ILE A CA  
1415 C C   . ILE A 197 ? 0.2674 0.3044 0.2876 0.0101  -0.0091 -0.0021 198 ILE A C   
1416 O O   . ILE A 197 ? 0.2669 0.3058 0.2890 0.0101  -0.0110 0.0012  198 ILE A O   
1417 C CB  . ILE A 197 ? 0.2668 0.3058 0.2879 0.0097  -0.0080 -0.0060 198 ILE A CB  
1418 C CG1 . ILE A 197 ? 0.2831 0.3239 0.3027 0.0080  -0.0083 -0.0076 198 ILE A CG1 
1419 C CG2 . ILE A 197 ? 0.2652 0.3062 0.2918 0.0113  -0.0090 -0.0039 198 ILE A CG2 
1420 C CD1 . ILE A 197 ? 0.3027 0.3477 0.3219 0.0065  -0.0104 -0.0065 198 ILE A CD1 
1421 N N   . ASP A 198 ? 0.2722 0.3056 0.2929 0.0111  -0.0074 -0.0035 199 ASP A N   
1422 C CA  . ASP A 198 ? 0.2902 0.3211 0.3142 0.0123  -0.0074 -0.0018 199 ASP A CA  
1423 C C   . ASP A 198 ? 0.2972 0.3284 0.3191 0.0108  -0.0088 0.0015  199 ASP A C   
1424 O O   . ASP A 198 ? 0.3076 0.3381 0.3332 0.0114  -0.0103 0.0049  199 ASP A O   
1425 C CB  . ASP A 198 ? 0.3297 0.3574 0.3537 0.0129  -0.0052 -0.0046 199 ASP A CB  
1426 C CG  . ASP A 198 ? 0.4235 0.4483 0.4522 0.0142  -0.0050 -0.0040 199 ASP A CG  
1427 O OD1 . ASP A 198 ? 0.4439 0.4689 0.4781 0.0158  -0.0052 -0.0040 199 ASP A OD1 
1428 O OD2 . ASP A 198 ? 0.4744 0.4967 0.5017 0.0134  -0.0046 -0.0037 199 ASP A OD2 
1429 N N   . THR A 199 ? 0.2923 0.3246 0.3087 0.0089  -0.0083 0.0006  200 THR A N   
1430 C CA  . THR A 199 ? 0.3021 0.3361 0.3156 0.0068  -0.0093 0.0034  200 THR A CA  
1431 C C   . THR A 199 ? 0.3183 0.3571 0.3310 0.0054  -0.0118 0.0067  200 THR A C   
1432 O O   . THR A 199 ? 0.3164 0.3558 0.3315 0.0052  -0.0138 0.0114  200 THR A O   
1433 C CB  . THR A 199 ? 0.3113 0.3459 0.3198 0.0052  -0.0076 0.0005  200 THR A CB  
1434 O OG1 . THR A 199 ? 0.3219 0.3526 0.3317 0.0064  -0.0059 -0.0014 200 THR A OG1 
1435 C CG2 . THR A 199 ? 0.3185 0.3567 0.3233 0.0025  -0.0083 0.0029  200 THR A CG2 
1436 N N   . LEU A 200 ? 0.3334 0.3758 0.3435 0.0044  -0.0120 0.0045  201 LEU A N   
1437 C CA  . LEU A 200 ? 0.3582 0.4062 0.3667 0.0025  -0.0143 0.0069  201 LEU A CA  
1438 C C   . LEU A 200 ? 0.3820 0.4312 0.3961 0.0040  -0.0168 0.0106  201 LEU A C   
1439 O O   . LEU A 200 ? 0.3890 0.4427 0.4027 0.0024  -0.0194 0.0148  201 LEU A O   
1440 C CB  . LEU A 200 ? 0.3590 0.4101 0.3639 0.0008  -0.0136 0.0024  201 LEU A CB  
1441 C CG  . LEU A 200 ? 0.3747 0.4254 0.3753 -0.0005 -0.0113 -0.0016 201 LEU A CG  
1442 C CD1 . LEU A 200 ? 0.3785 0.4315 0.3772 -0.0018 -0.0107 -0.0063 201 LEU A CD1 
1443 C CD2 . LEU A 200 ? 0.3829 0.4371 0.3795 -0.0030 -0.0116 0.0008  201 LEU A CD2 
1444 N N   . GLU A 201 ? 0.3959 0.4417 0.4154 0.0069  -0.0159 0.0092  202 GLU A N   
1445 C CA  . GLU A 201 ? 0.4201 0.4671 0.4464 0.0087  -0.0179 0.0123  202 GLU A CA  
1446 C C   . GLU A 201 ? 0.4436 0.4869 0.4755 0.0106  -0.0187 0.0159  202 GLU A C   
1447 O O   . GLU A 201 ? 0.4447 0.4888 0.4837 0.0125  -0.0205 0.0187  202 GLU A O   
1448 C CB  . GLU A 201 ? 0.4519 0.4985 0.4820 0.0107  -0.0165 0.0087  202 GLU A CB  
1449 C CG  . GLU A 201 ? 0.5134 0.5637 0.5400 0.0088  -0.0165 0.0062  202 GLU A CG  
1450 C CD  . GLU A 201 ? 0.6057 0.6618 0.6351 0.0083  -0.0192 0.0088  202 GLU A CD  
1451 O OE1 . GLU A 201 ? 0.6393 0.6963 0.6748 0.0103  -0.0194 0.0088  202 GLU A OE1 
1452 O OE2 . GLU A 201 ? 0.6273 0.6877 0.6527 0.0056  -0.0212 0.0106  202 GLU A OE2 
1453 N N   . ASN A 202 ? 0.4637 0.5030 0.4935 0.0101  -0.0173 0.0157  203 ASN A N   
1454 C CA  . ASN A 202 ? 0.4917 0.5266 0.5268 0.0114  -0.0178 0.0187  203 ASN A CA  
1455 C C   . ASN A 202 ? 0.5073 0.5386 0.5508 0.0149  -0.0168 0.0164  203 ASN A C   
1456 O O   . ASN A 202 ? 0.5156 0.5440 0.5663 0.0165  -0.0179 0.0193  203 ASN A O   
1457 C CB  . ASN A 202 ? 0.5170 0.5545 0.5538 0.0100  -0.0214 0.0259  203 ASN A CB  
1458 C CG  . ASN A 202 ? 0.5748 0.6078 0.6140 0.0097  -0.0219 0.0294  203 ASN A CG  
1459 O OD1 . ASN A 202 ? 0.5947 0.6224 0.6354 0.0107  -0.0194 0.0261  203 ASN A OD1 
1460 N ND2 . ASN A 202 ? 0.5939 0.6293 0.6339 0.0078  -0.0251 0.0365  203 ASN A ND2 
1461 N N   . ILE A 203 ? 0.5103 0.5421 0.5535 0.0160  -0.0145 0.0113  204 ILE A N   
1462 C CA  . ILE A 203 ? 0.5206 0.5503 0.5710 0.0189  -0.0129 0.0082  204 ILE A CA  
1463 C C   . ILE A 203 ? 0.5443 0.5691 0.5931 0.0187  -0.0104 0.0050  204 ILE A C   
1464 O O   . ILE A 203 ? 0.5557 0.5806 0.5977 0.0171  -0.0088 0.0024  204 ILE A O   
1465 C CB  . ILE A 203 ? 0.5218 0.5553 0.5723 0.0194  -0.0118 0.0049  204 ILE A CB  
1466 C CG1 . ILE A 203 ? 0.5318 0.5665 0.5737 0.0171  -0.0105 0.0023  204 ILE A CG1 
1467 C CG2 . ILE A 203 ? 0.5269 0.5652 0.5816 0.0199  -0.0146 0.0084  204 ILE A CG2 
1468 C CD1 . ILE A 203 ? 0.5465 0.5841 0.5886 0.0173  -0.0092 -0.0007 204 ILE A CD1 
1469 N N   . LYS A 204 ? 0.5503 0.5710 0.6056 0.0202  -0.0103 0.0054  205 LYS A N   
1470 C CA  . LYS A 204 ? 0.5615 0.5780 0.6156 0.0197  -0.0081 0.0022  205 LYS A CA  
1471 C C   . LYS A 204 ? 0.5578 0.5747 0.6135 0.0209  -0.0051 -0.0041 205 LYS A C   
1472 O O   . LYS A 204 ? 0.5591 0.5736 0.6219 0.0226  -0.0041 -0.0067 205 LYS A O   
1473 C CB  . LYS A 204 ? 0.5974 0.6090 0.6578 0.0201  -0.0094 0.0051  205 LYS A CB  
1474 C CG  . LYS A 204 ? 0.6681 0.6798 0.7246 0.0177  -0.0119 0.0114  205 LYS A CG  
1475 C CD  . LYS A 204 ? 0.7411 0.7475 0.8042 0.0177  -0.0133 0.0151  205 LYS A CD  
1476 C CE  . LYS A 204 ? 0.8004 0.8051 0.8578 0.0146  -0.0129 0.0165  205 LYS A CE  
1477 N NZ  . LYS A 204 ? 0.8312 0.8298 0.8960 0.0146  -0.0136 0.0188  205 LYS A NZ  
1478 N N   . LEU A 205 ? 0.5533 0.5734 0.6027 0.0198  -0.0038 -0.0066 206 LEU A N   
1479 C CA  . LEU A 205 ? 0.5607 0.5825 0.6107 0.0203  -0.0012 -0.0118 206 LEU A CA  
1480 C C   . LEU A 205 ? 0.5809 0.6000 0.6301 0.0196  0.0009  -0.0154 206 LEU A C   
1481 O O   . LEU A 205 ? 0.5864 0.6063 0.6395 0.0205  0.0029  -0.0198 206 LEU A O   
1482 C CB  . LEU A 205 ? 0.5574 0.5832 0.6014 0.0190  -0.0007 -0.0126 206 LEU A CB  
1483 C CG  . LEU A 205 ? 0.5667 0.5962 0.6118 0.0193  -0.0022 -0.0103 206 LEU A CG  
1484 C CD1 . LEU A 205 ? 0.5713 0.6038 0.6114 0.0178  -0.0014 -0.0117 206 LEU A CD1 
1485 C CD2 . LEU A 205 ? 0.5682 0.5996 0.6220 0.0217  -0.0022 -0.0110 206 LEU A CD2 
1486 N N   . LYS A 206 ? 0.5918 0.6084 0.6362 0.0179  0.0005  -0.0140 207 LYS A N   
1487 C CA  . LYS A 206 ? 0.6079 0.6224 0.6516 0.0170  0.0021  -0.0173 207 LYS A CA  
1488 C C   . LYS A 206 ? 0.6216 0.6315 0.6725 0.0179  0.0019  -0.0173 207 LYS A C   
1489 O O   . LYS A 206 ? 0.6237 0.6326 0.6782 0.0181  0.0037  -0.0219 207 LYS A O   
1490 C CB  . LYS A 206 ? 0.6351 0.6493 0.6717 0.0148  0.0018  -0.0160 207 LYS A CB  
1491 C CG  . LYS A 206 ? 0.6855 0.7034 0.7166 0.0139  0.0028  -0.0179 207 LYS A CG  
1492 C CD  . LYS A 206 ? 0.7443 0.7617 0.7708 0.0121  0.0031  -0.0183 207 LYS A CD  
1493 C CE  . LYS A 206 ? 0.7918 0.8082 0.8157 0.0113  0.0018  -0.0148 207 LYS A CE  
1494 N NZ  . LYS A 206 ? 0.8199 0.8333 0.8454 0.0104  0.0017  -0.0140 207 LYS A NZ  
1495 N N   . THR A 207 ? 0.6251 0.6326 0.6786 0.0182  -0.0005 -0.0122 208 THR A N   
1496 C CA  . THR A 207 ? 0.6331 0.6356 0.6943 0.0189  -0.0015 -0.0105 208 THR A CA  
1497 C C   . THR A 207 ? 0.6415 0.6428 0.7124 0.0215  -0.0002 -0.0147 208 THR A C   
1498 O O   . THR A 207 ? 0.6520 0.6490 0.7286 0.0216  0.0007  -0.0175 208 THR A O   
1499 C CB  . THR A 207 ? 0.6455 0.6475 0.7077 0.0188  -0.0047 -0.0033 208 THR A CB  
1500 O OG1 . THR A 207 ? 0.6531 0.6568 0.7065 0.0162  -0.0053 -0.0005 208 THR A OG1 
1501 C CG2 . THR A 207 ? 0.6552 0.6518 0.7263 0.0195  -0.0063 -0.0002 208 THR A CG2 
1502 N N   . SER A 208 ? 0.6351 0.6404 0.7082 0.0233  0.0000  -0.0157 209 SER A N   
1503 C CA  . SER A 208 ? 0.6323 0.6378 0.7151 0.0259  0.0015  -0.0203 209 SER A CA  
1504 C C   . SER A 208 ? 0.6272 0.6391 0.7072 0.0260  0.0040  -0.0253 209 SER A C   
1505 O O   . SER A 208 ? 0.6294 0.6451 0.7012 0.0246  0.0038  -0.0237 209 SER A O   
1506 C CB  . SER A 208 ? 0.6462 0.6507 0.7384 0.0286  -0.0012 -0.0157 209 SER A CB  
1507 O OG  . SER A 208 ? 0.6683 0.6758 0.7555 0.0279  -0.0039 -0.0094 209 SER A OG  
1508 N N   . ASN A 209 ? 0.6193 0.6326 0.7062 0.0274  0.0066  -0.0316 210 ASN A N   
1509 C CA  . ASN A 209 ? 0.6170 0.6374 0.7023 0.0273  0.0090  -0.0361 210 ASN A CA  
1510 C C   . ASN A 209 ? 0.5944 0.6180 0.6885 0.0303  0.0086  -0.0357 210 ASN A C   
1511 O O   . ASN A 209 ? 0.5950 0.6251 0.6900 0.0305  0.0108  -0.0396 210 ASN A O   
1512 C CB  . ASN A 209 ? 0.6484 0.6708 0.7336 0.0261  0.0126  -0.0440 210 ASN A CB  
1513 C CG  . ASN A 209 ? 0.7152 0.7393 0.7889 0.0226  0.0133  -0.0444 210 ASN A CG  
1514 O OD1 . ASN A 209 ? 0.7373 0.7606 0.8034 0.0213  0.0113  -0.0390 210 ASN A OD1 
1515 N ND2 . ASN A 209 ? 0.7274 0.7545 0.8000 0.0210  0.0161  -0.0509 210 ASN A ND2 
1516 N N   . GLU A 210 ? 0.5702 0.5900 0.6710 0.0324  0.0054  -0.0302 211 GLU A N   
1517 C CA  . GLU A 210 ? 0.5504 0.5727 0.6609 0.0355  0.0040  -0.0283 211 GLU A CA  
1518 C C   . GLU A 210 ? 0.5093 0.5329 0.6153 0.0349  0.0003  -0.0203 211 GLU A C   
1519 O O   . GLU A 210 ? 0.5178 0.5388 0.6154 0.0326  -0.0015 -0.0159 211 GLU A O   
1520 C CB  . GLU A 210 ? 0.5957 0.6124 0.7201 0.0386  0.0033  -0.0289 211 GLU A CB  
1521 C CG  . GLU A 210 ? 0.6774 0.6859 0.8011 0.0374  0.0021  -0.0267 211 GLU A CG  
1522 C CD  . GLU A 210 ? 0.7824 0.7848 0.9207 0.0401  0.0018  -0.0283 211 GLU A CD  
1523 O OE1 . GLU A 210 ? 0.8026 0.8059 0.9528 0.0436  0.0005  -0.0271 211 GLU A OE1 
1524 O OE2 . GLU A 210 ? 0.8070 0.8037 0.9456 0.0388  0.0028  -0.0308 211 GLU A OE2 
1525 N N   . GLY A 211 ? 0.4591 0.4876 0.5708 0.0368  -0.0007 -0.0190 212 GLY A N   
1526 C CA  . GLY A 211 ? 0.4159 0.4471 0.5241 0.0361  -0.0043 -0.0122 212 GLY A CA  
1527 C C   . GLY A 211 ? 0.3636 0.3997 0.4608 0.0332  -0.0033 -0.0128 212 GLY A C   
1528 O O   . GLY A 211 ? 0.3572 0.3940 0.4485 0.0316  -0.0003 -0.0174 212 GLY A O   
1529 N N   . HIS A 212 ? 0.3262 0.3658 0.4211 0.0325  -0.0061 -0.0081 213 HIS A N   
1530 C CA  . HIS A 212 ? 0.2959 0.3398 0.3816 0.0298  -0.0059 -0.0079 213 HIS A CA  
1531 C C   . HIS A 212 ? 0.2543 0.3018 0.3379 0.0290  -0.0022 -0.0137 213 HIS A C   
1532 O O   . HIS A 212 ? 0.2527 0.2995 0.3275 0.0265  -0.0009 -0.0150 213 HIS A O   
1533 C CB  . HIS A 212 ? 0.3139 0.3542 0.3891 0.0270  -0.0071 -0.0051 213 HIS A CB  
1534 C CG  . HIS A 212 ? 0.3555 0.3939 0.4318 0.0271  -0.0107 0.0010  213 HIS A CG  
1535 N ND1 . HIS A 212 ? 0.3827 0.4155 0.4597 0.0272  -0.0113 0.0027  213 HIS A ND1 
1536 C CD2 . HIS A 212 ? 0.3732 0.4154 0.4509 0.0268  -0.0140 0.0057  213 HIS A CD2 
1537 C CE1 . HIS A 212 ? 0.3910 0.4244 0.4691 0.0268  -0.0149 0.0089  213 HIS A CE1 
1538 N NE2 . HIS A 212 ? 0.3880 0.4272 0.4663 0.0266  -0.0167 0.0109  213 HIS A NE2 
1539 N N   . PRO A 213 ? 0.2191 0.2712 0.3114 0.0310  -0.0004 -0.0172 214 PRO A N   
1540 C CA  . PRO A 213 ? 0.1917 0.2485 0.2817 0.0296  0.0032  -0.0225 214 PRO A CA  
1541 C C   . PRO A 213 ? 0.1647 0.2255 0.2470 0.0266  0.0029  -0.0209 214 PRO A C   
1542 O O   . PRO A 213 ? 0.1594 0.2219 0.2358 0.0243  0.0053  -0.0235 214 PRO A O   
1543 C CB  . PRO A 213 ? 0.2020 0.2637 0.3040 0.0325  0.0048  -0.0260 214 PRO A CB  
1544 C CG  . PRO A 213 ? 0.2082 0.2696 0.3179 0.0350  0.0011  -0.0210 214 PRO A CG  
1545 C CD  . PRO A 213 ? 0.1993 0.2531 0.3043 0.0345  -0.0017 -0.0163 214 PRO A CD  
1546 N N   . GLU A 214 ? 0.1500 0.2124 0.2324 0.0263  -0.0001 -0.0165 215 GLU A N   
1547 C CA  . GLU A 214 ? 0.1513 0.2170 0.2275 0.0234  -0.0006 -0.0151 215 GLU A CA  
1548 C C   . GLU A 214 ? 0.1439 0.2049 0.2098 0.0208  -0.0009 -0.0140 215 GLU A C   
1549 O O   . GLU A 214 ? 0.1367 0.1992 0.1975 0.0183  0.0003  -0.0151 215 GLU A O   
1550 C CB  . GLU A 214 ? 0.1885 0.2577 0.2679 0.0235  -0.0039 -0.0112 215 GLU A CB  
1551 C CG  . GLU A 214 ? 0.2731 0.3482 0.3638 0.0262  -0.0040 -0.0119 215 GLU A CG  
1552 C CD  . GLU A 214 ? 0.4036 0.4762 0.5028 0.0297  -0.0060 -0.0097 215 GLU A CD  
1553 O OE1 . GLU A 214 ? 0.4314 0.4981 0.5269 0.0297  -0.0080 -0.0066 215 GLU A OE1 
1554 O OE2 . GLU A 214 ? 0.4452 0.5221 0.5554 0.0326  -0.0057 -0.0109 215 GLU A OE2 
1555 N N   . TRP A 215 ? 0.1417 0.1971 0.2050 0.0212  -0.0027 -0.0117 216 TRP A N   
1556 C CA  . TRP A 215 ? 0.1460 0.1971 0.2005 0.0191  -0.0029 -0.0111 216 TRP A CA  
1557 C C   . TRP A 215 ? 0.1456 0.1950 0.1974 0.0186  0.0000  -0.0145 216 TRP A C   
1558 O O   . TRP A 215 ? 0.1498 0.1986 0.1954 0.0164  0.0006  -0.0148 216 TRP A O   
1559 C CB  . TRP A 215 ? 0.1475 0.1942 0.2004 0.0196  -0.0051 -0.0080 216 TRP A CB  
1560 C CG  . TRP A 215 ? 0.1494 0.1978 0.2000 0.0183  -0.0080 -0.0044 216 TRP A CG  
1561 C CD1 . TRP A 215 ? 0.1567 0.2062 0.2110 0.0192  -0.0108 -0.0006 216 TRP A CD1 
1562 C CD2 . TRP A 215 ? 0.1457 0.1949 0.1898 0.0156  -0.0086 -0.0043 216 TRP A CD2 
1563 N NE1 . TRP A 215 ? 0.1598 0.2116 0.2094 0.0169  -0.0130 0.0016  216 TRP A NE1 
1564 C CE2 . TRP A 215 ? 0.1532 0.2046 0.1968 0.0148  -0.0115 -0.0011 216 TRP A CE2 
1565 C CE3 . TRP A 215 ? 0.1482 0.1966 0.1874 0.0137  -0.0071 -0.0065 216 TRP A CE3 
1566 C CZ2 . TRP A 215 ? 0.1567 0.2095 0.1948 0.0121  -0.0125 -0.0011 216 TRP A CZ2 
1567 C CZ3 . TRP A 215 ? 0.1576 0.2064 0.1924 0.0114  -0.0083 -0.0061 216 TRP A CZ3 
1568 C CH2 . TRP A 215 ? 0.1593 0.2105 0.1936 0.0106  -0.0108 -0.0040 216 TRP A CH2 
1569 N N   . ARG A 216 ? 0.1368 0.1858 0.1938 0.0205  0.0017  -0.0172 217 ARG A N   
1570 C CA  . ARG A 216 ? 0.1394 0.1881 0.1940 0.0197  0.0045  -0.0210 217 ARG A CA  
1571 C C   . ARG A 216 ? 0.1305 0.1846 0.1825 0.0176  0.0063  -0.0228 217 ARG A C   
1572 O O   . ARG A 216 ? 0.1374 0.1911 0.1833 0.0154  0.0071  -0.0230 217 ARG A O   
1573 C CB  . ARG A 216 ? 0.1611 0.2093 0.2229 0.0220  0.0062  -0.0246 217 ARG A CB  
1574 C CG  . ARG A 216 ? 0.2098 0.2516 0.2727 0.0231  0.0048  -0.0231 217 ARG A CG  
1575 C CD  . ARG A 216 ? 0.2536 0.2941 0.3250 0.0254  0.0063  -0.0268 217 ARG A CD  
1576 N NE  . ARG A 216 ? 0.3099 0.3444 0.3847 0.0268  0.0040  -0.0235 217 ARG A NE  
1577 C CZ  . ARG A 216 ? 0.3590 0.3882 0.4304 0.0259  0.0038  -0.0231 217 ARG A CZ  
1578 N NH1 . ARG A 216 ? 0.3599 0.3893 0.4246 0.0237  0.0057  -0.0260 217 ARG A NH1 
1579 N NH2 . ARG A 216 ? 0.3721 0.3964 0.4468 0.0268  0.0015  -0.0192 217 ARG A NH2 
1580 N N   . ARG A 217 ? 0.1154 0.1750 0.1724 0.0180  0.0068  -0.0233 218 ARG A N   
1581 C CA  . ARG A 217 ? 0.1122 0.1780 0.1677 0.0157  0.0085  -0.0245 218 ARG A CA  
1582 C C   . ARG A 217 ? 0.1131 0.1779 0.1623 0.0130  0.0067  -0.0209 218 ARG A C   
1583 O O   . ARG A 217 ? 0.1201 0.1869 0.1649 0.0103  0.0078  -0.0209 218 ARG A O   
1584 C CB  . ARG A 217 ? 0.1241 0.1965 0.1877 0.0170  0.0095  -0.0263 218 ARG A CB  
1585 C CG  . ARG A 217 ? 0.1815 0.2613 0.2438 0.0142  0.0118  -0.0278 218 ARG A CG  
1586 C CD  . ARG A 217 ? 0.2355 0.3229 0.3060 0.0156  0.0145  -0.0322 218 ARG A CD  
1587 N NE  . ARG A 217 ? 0.2785 0.3738 0.3464 0.0121  0.0172  -0.0339 218 ARG A NE  
1588 C CZ  . ARG A 217 ? 0.3272 0.4251 0.3910 0.0101  0.0198  -0.0369 218 ARG A CZ  
1589 N NH1 . ARG A 217 ? 0.3305 0.4235 0.3927 0.0113  0.0203  -0.0392 218 ARG A NH1 
1590 N NH2 . ARG A 217 ? 0.3457 0.4517 0.4068 0.0064  0.0220  -0.0376 218 ARG A NH2 
1591 N N   . PHE A 218 ? 0.1094 0.1711 0.1581 0.0135  0.0040  -0.0178 219 PHE A N   
1592 C CA  . PHE A 218 ? 0.1132 0.1732 0.1566 0.0110  0.0024  -0.0153 219 PHE A CA  
1593 C C   . PHE A 218 ? 0.1183 0.1741 0.1555 0.0097  0.0028  -0.0152 219 PHE A C   
1594 O O   . PHE A 218 ? 0.1131 0.1699 0.1474 0.0073  0.0030  -0.0143 219 PHE A O   
1595 C CB  . PHE A 218 ? 0.1081 0.1658 0.1518 0.0116  -0.0005 -0.0128 219 PHE A CB  
1596 C CG  . PHE A 218 ? 0.1195 0.1746 0.1579 0.0093  -0.0019 -0.0114 219 PHE A CG  
1597 C CD1 . PHE A 218 ? 0.1231 0.1811 0.1618 0.0070  -0.0023 -0.0108 219 PHE A CD1 
1598 C CD2 . PHE A 218 ? 0.1260 0.1759 0.1599 0.0092  -0.0024 -0.0111 219 PHE A CD2 
1599 C CE1 . PHE A 218 ? 0.1234 0.1784 0.1585 0.0048  -0.0033 -0.0101 219 PHE A CE1 
1600 C CE2 . PHE A 218 ? 0.1283 0.1759 0.1586 0.0073  -0.0033 -0.0106 219 PHE A CE2 
1601 C CZ  . PHE A 218 ? 0.1237 0.1735 0.1550 0.0052  -0.0038 -0.0102 219 PHE A CZ  
1602 N N   . PHE A 219 ? 0.1240 0.1755 0.1599 0.0112  0.0027  -0.0157 220 PHE A N   
1603 C CA  . PHE A 219 ? 0.1254 0.1734 0.1563 0.0102  0.0029  -0.0156 220 PHE A CA  
1604 C C   . PHE A 219 ? 0.1224 0.1735 0.1519 0.0089  0.0050  -0.0173 220 PHE A C   
1605 O O   . PHE A 219 ? 0.1257 0.1759 0.1512 0.0071  0.0047  -0.0161 220 PHE A O   
1606 C CB  . PHE A 219 ? 0.1287 0.1720 0.1590 0.0119  0.0023  -0.0156 220 PHE A CB  
1607 C CG  . PHE A 219 ? 0.1419 0.1825 0.1704 0.0118  0.0001  -0.0134 220 PHE A CG  
1608 C CD1 . PHE A 219 ? 0.1511 0.1900 0.1758 0.0102  -0.0006 -0.0126 220 PHE A CD1 
1609 C CD2 . PHE A 219 ? 0.1541 0.1945 0.1852 0.0130  -0.0013 -0.0122 220 PHE A CD2 
1610 C CE1 . PHE A 219 ? 0.1590 0.1964 0.1823 0.0098  -0.0022 -0.0116 220 PHE A CE1 
1611 C CE2 . PHE A 219 ? 0.1601 0.1994 0.1888 0.0123  -0.0032 -0.0104 220 PHE A CE2 
1612 C CZ  . PHE A 219 ? 0.1546 0.1927 0.1794 0.0106  -0.0034 -0.0107 220 PHE A CZ  
1613 N N   . TYR A 220 ? 0.1166 0.1719 0.1498 0.0095  0.0070  -0.0201 221 TYR A N   
1614 C CA  . TYR A 220 ? 0.1228 0.1829 0.1542 0.0076  0.0092  -0.0221 221 TYR A CA  
1615 C C   . TYR A 220 ? 0.1181 0.1825 0.1474 0.0046  0.0091  -0.0198 221 TYR A C   
1616 O O   . TYR A 220 ? 0.1259 0.1911 0.1509 0.0022  0.0091  -0.0184 221 TYR A O   
1617 C CB  . TYR A 220 ? 0.1198 0.1842 0.1561 0.0088  0.0118  -0.0268 221 TYR A CB  
1618 C CG  . TYR A 220 ? 0.1334 0.2043 0.1671 0.0061  0.0142  -0.0293 221 TYR A CG  
1619 C CD1 . TYR A 220 ? 0.1434 0.2135 0.1719 0.0044  0.0143  -0.0293 221 TYR A CD1 
1620 C CD2 . TYR A 220 ? 0.1509 0.2298 0.1865 0.0045  0.0162  -0.0307 221 TYR A CD2 
1621 C CE1 . TYR A 220 ? 0.1542 0.2312 0.1794 0.0013  0.0162  -0.0310 221 TYR A CE1 
1622 C CE2 . TYR A 220 ? 0.1622 0.2483 0.1945 0.0012  0.0184  -0.0325 221 TYR A CE2 
1623 C CZ  . TYR A 220 ? 0.1714 0.2566 0.1982 -0.0004 0.0183  -0.0326 221 TYR A CZ  
1624 O OH  . TYR A 220 ? 0.1944 0.2877 0.2172 -0.0042 0.0202  -0.0339 221 TYR A OH  
1625 N N   . LEU A 221 ? 0.1046 0.1719 0.1373 0.0045  0.0089  -0.0191 222 LEU A N   
1626 C CA  . LEU A 221 ? 0.1098 0.1812 0.1413 0.0013  0.0088  -0.0168 222 LEU A CA  
1627 C C   . LEU A 221 ? 0.1108 0.1773 0.1388 -0.0002 0.0064  -0.0129 222 LEU A C   
1628 O O   . LEU A 221 ? 0.1204 0.1887 0.1459 -0.0031 0.0063  -0.0106 222 LEU A O   
1629 C CB  . LEU A 221 ? 0.1238 0.2001 0.1605 0.0015  0.0092  -0.0173 222 LEU A CB  
1630 C CG  . LEU A 221 ? 0.1516 0.2337 0.1934 0.0032  0.0119  -0.0216 222 LEU A CG  
1631 C CD1 . LEU A 221 ? 0.1551 0.2421 0.2028 0.0037  0.0119  -0.0217 222 LEU A CD1 
1632 C CD2 . LEU A 221 ? 0.1632 0.2517 0.2027 0.0008  0.0148  -0.0240 222 LEU A CD2 
1633 N N   . SER A 222 ? 0.1084 0.1687 0.1365 0.0016  0.0044  -0.0122 223 SER A N   
1634 C CA  . SER A 222 ? 0.1086 0.1638 0.1343 0.0005  0.0024  -0.0095 223 SER A CA  
1635 C C   . SER A 222 ? 0.1066 0.1597 0.1288 0.0000  0.0024  -0.0088 223 SER A C   
1636 O O   . SER A 222 ? 0.1155 0.1675 0.1365 -0.0019 0.0014  -0.0061 223 SER A O   
1637 C CB  . SER A 222 ? 0.1285 0.1791 0.1550 0.0023  0.0007  -0.0098 223 SER A CB  
1638 O OG  . SER A 222 ? 0.1703 0.2184 0.1962 0.0048  0.0009  -0.0113 223 SER A OG  
1639 N N   . GLY A 223 ? 0.1005 0.1538 0.1218 0.0016  0.0036  -0.0110 224 GLY A N   
1640 C CA  . GLY A 223 ? 0.1070 0.1598 0.1250 0.0009  0.0038  -0.0107 224 GLY A CA  
1641 C C   . GLY A 223 ? 0.1110 0.1694 0.1272 -0.0022 0.0044  -0.0090 224 GLY A C   
1642 O O   . GLY A 223 ? 0.1136 0.1710 0.1278 -0.0038 0.0031  -0.0059 224 GLY A O   
1643 N N   . CYS A 224 ? 0.1166 0.1815 0.1338 -0.0034 0.0064  -0.0107 225 CYS A N   
1644 C CA  . CYS A 224 ? 0.1267 0.1988 0.1421 -0.0071 0.0074  -0.0092 225 CYS A CA  
1645 C C   . CYS A 224 ? 0.1261 0.1971 0.1415 -0.0095 0.0053  -0.0040 225 CYS A C   
1646 O O   . CYS A 224 ? 0.1245 0.1982 0.1375 -0.0125 0.0046  -0.0004 225 CYS A O   
1647 C CB  . CYS A 224 ? 0.1432 0.2228 0.1609 -0.0075 0.0102  -0.0128 225 CYS A CB  
1648 S SG  . CYS A 224 ? 0.1886 0.2708 0.2069 -0.0055 0.0130  -0.0193 225 CYS A SG  
1649 N N   . LEU A 225 ? 0.1291 0.1963 0.1476 -0.0085 0.0043  -0.0034 226 LEU A N   
1650 C CA  . LEU A 225 ? 0.1348 0.2001 0.1544 -0.0108 0.0023  0.0009  226 LEU A CA  
1651 C C   . LEU A 225 ? 0.1456 0.2038 0.1647 -0.0103 -0.0002 0.0036  226 LEU A C   
1652 O O   . LEU A 225 ? 0.1561 0.2130 0.1761 -0.0127 -0.0019 0.0079  226 LEU A O   
1653 C CB  . LEU A 225 ? 0.1331 0.1973 0.1564 -0.0103 0.0020  0.0000  226 LEU A CB  
1654 C CG  . LEU A 225 ? 0.1494 0.2215 0.1746 -0.0115 0.0041  -0.0016 226 LEU A CG  
1655 C CD1 . LEU A 225 ? 0.1521 0.2229 0.1811 -0.0101 0.0034  -0.0030 226 LEU A CD1 
1656 C CD2 . LEU A 225 ? 0.1538 0.2319 0.1782 -0.0160 0.0045  0.0019  226 LEU A CD2 
1657 N N   . VAL A 226 ? 0.1368 0.1906 0.1551 -0.0072 -0.0004 0.0012  227 VAL A N   
1658 C CA  . VAL A 226 ? 0.1418 0.1897 0.1601 -0.0063 -0.0023 0.0030  227 VAL A CA  
1659 C C   . VAL A 226 ? 0.1443 0.1958 0.1603 -0.0084 -0.0028 0.0062  227 VAL A C   
1660 O O   . VAL A 226 ? 0.1449 0.1944 0.1624 -0.0098 -0.0049 0.0105  227 VAL A O   
1661 C CB  . VAL A 226 ? 0.1536 0.1972 0.1715 -0.0029 -0.0021 -0.0005 227 VAL A CB  
1662 C CG1 . VAL A 226 ? 0.1589 0.1993 0.1765 -0.0021 -0.0035 0.0008  227 VAL A CG1 
1663 C CG2 . VAL A 226 ? 0.1581 0.1979 0.1782 -0.0014 -0.0026 -0.0024 227 VAL A CG2 
1664 N N   . ALA A 227 ? 0.1470 0.2041 0.1598 -0.0088 -0.0010 0.0042  228 ALA A N   
1665 C CA  . ALA A 227 ? 0.1601 0.2221 0.1699 -0.0114 -0.0014 0.0069  228 ALA A CA  
1666 C C   . ALA A 227 ? 0.1830 0.2503 0.1925 -0.0156 -0.0021 0.0119  228 ALA A C   
1667 O O   . ALA A 227 ? 0.1902 0.2601 0.1982 -0.0180 -0.0038 0.0164  228 ALA A O   
1668 C CB  . ALA A 227 ? 0.1518 0.2191 0.1585 -0.0112 0.0010  0.0025  228 ALA A CB  
1669 N N   . HIS A 228 ? 0.1885 0.2577 0.1996 -0.0167 -0.0010 0.0115  229 HIS A N   
1670 C CA  . HIS A 228 ? 0.2018 0.2757 0.2131 -0.0211 -0.0017 0.0165  229 HIS A CA  
1671 C C   . HIS A 228 ? 0.2187 0.2851 0.2336 -0.0214 -0.0051 0.0218  229 HIS A C   
1672 O O   . HIS A 228 ? 0.2212 0.2891 0.2358 -0.0241 -0.0071 0.0276  229 HIS A O   
1673 C CB  . HIS A 228 ? 0.2000 0.2784 0.2126 -0.0223 0.0005  0.0144  229 HIS A CB  
1674 C CG  . HIS A 228 ? 0.2272 0.3103 0.2402 -0.0272 -0.0003 0.0200  229 HIS A CG  
1675 N ND1 . HIS A 228 ? 0.2566 0.3346 0.2739 -0.0280 -0.0021 0.0231  229 HIS A ND1 
1676 C CD2 . HIS A 228 ? 0.2347 0.3272 0.2444 -0.0318 0.0005  0.0232  229 HIS A CD2 
1677 C CE1 . HIS A 228 ? 0.2567 0.3404 0.2735 -0.0330 -0.0026 0.0285  229 HIS A CE1 
1678 N NE2 . HIS A 228 ? 0.2501 0.3429 0.2620 -0.0355 -0.0011 0.0290  229 HIS A NE2 
1679 N N   . ASP A 229 ? 0.2300 0.2886 0.2488 -0.0186 -0.0057 0.0197  230 ASP A N   
1680 C CA  . ASP A 229 ? 0.2506 0.3016 0.2742 -0.0185 -0.0086 0.0231  230 ASP A CA  
1681 C C   . ASP A 229 ? 0.2641 0.3118 0.2885 -0.0174 -0.0108 0.0260  230 ASP A C   
1682 O O   . ASP A 229 ? 0.2745 0.3189 0.3029 -0.0188 -0.0135 0.0313  230 ASP A O   
1683 C CB  . ASP A 229 ? 0.2797 0.3241 0.3064 -0.0154 -0.0084 0.0186  230 ASP A CB  
1684 C CG  . ASP A 229 ? 0.3393 0.3854 0.3676 -0.0171 -0.0075 0.0175  230 ASP A CG  
1685 O OD1 . ASP A 229 ? 0.3531 0.4064 0.3799 -0.0202 -0.0064 0.0194  230 ASP A OD1 
1686 O OD2 . ASP A 229 ? 0.3568 0.3979 0.3880 -0.0156 -0.0080 0.0147  230 ASP A OD2 
1687 N N   . GLU A 230 ? 0.2580 0.3065 0.2794 -0.0149 -0.0098 0.0227  231 GLU A N   
1688 C CA  . GLU A 230 ? 0.2513 0.2977 0.2735 -0.0137 -0.0118 0.0250  231 GLU A CA  
1689 C C   . GLU A 230 ? 0.2481 0.3012 0.2678 -0.0172 -0.0132 0.0308  231 GLU A C   
1690 O O   . GLU A 230 ? 0.2560 0.3078 0.2776 -0.0167 -0.0156 0.0343  231 GLU A O   
1691 C CB  . GLU A 230 ? 0.2764 0.3219 0.2962 -0.0103 -0.0103 0.0195  231 GLU A CB  
1692 C CG  . GLU A 230 ? 0.3510 0.3894 0.3741 -0.0068 -0.0100 0.0153  231 GLU A CG  
1693 C CD  . GLU A 230 ? 0.4804 0.5122 0.5097 -0.0059 -0.0125 0.0175  231 GLU A CD  
1694 O OE1 . GLU A 230 ? 0.5024 0.5315 0.5337 -0.0036 -0.0134 0.0170  231 GLU A OE1 
1695 O OE2 . GLU A 230 ? 0.5277 0.5571 0.5604 -0.0074 -0.0134 0.0195  231 GLU A OE2 
1696 N N   . GLY A 231 ? 0.2359 0.2971 0.2514 -0.0208 -0.0117 0.0317  232 GLY A N   
1697 C CA  . GLY A 231 ? 0.2413 0.3109 0.2531 -0.0248 -0.0126 0.0367  232 GLY A CA  
1698 C C   . GLY A 231 ? 0.2560 0.3312 0.2626 -0.0242 -0.0111 0.0328  232 GLY A C   
1699 O O   . GLY A 231 ? 0.2635 0.3463 0.2665 -0.0276 -0.0120 0.0364  232 GLY A O   
1700 N N   . ALA A 232 ? 0.2604 0.3323 0.2665 -0.0204 -0.0088 0.0256  233 ALA A N   
1701 C CA  . ALA A 232 ? 0.2706 0.3465 0.2728 -0.0197 -0.0072 0.0211  233 ALA A CA  
1702 C C   . ALA A 232 ? 0.2835 0.3693 0.2809 -0.0228 -0.0042 0.0179  233 ALA A C   
1703 O O   . ALA A 232 ? 0.2875 0.3800 0.2807 -0.0247 -0.0036 0.0167  233 ALA A O   
1704 C CB  . ALA A 232 ? 0.2679 0.3367 0.2719 -0.0150 -0.0059 0.0151  233 ALA A CB  
1705 N N   . CYS A 233 ? 0.2884 0.3754 0.2866 -0.0233 -0.0021 0.0160  234 CYS A N   
1706 C CA  . CYS A 233 ? 0.2911 0.3876 0.2862 -0.0259 0.0013  0.0123  234 CYS A CA  
1707 C C   . CYS A 233 ? 0.3055 0.4039 0.3027 -0.0278 0.0019  0.0144  234 CYS A C   
1708 O O   . CYS A 233 ? 0.3106 0.4044 0.3114 -0.0251 0.0030  0.0114  234 CYS A O   
1709 C CB  . CYS A 233 ? 0.2904 0.3860 0.2859 -0.0226 0.0043  0.0039  234 CYS A CB  
1710 S SG  . CYS A 233 ? 0.3251 0.4318 0.3191 -0.0249 0.0089  -0.0023 234 CYS A SG  
1711 N N   . ILE A 234 ? 0.3078 0.4137 0.3027 -0.0329 0.0011  0.0199  235 ILE A N   
1712 C CA  . ILE A 234 ? 0.3203 0.4289 0.3170 -0.0356 0.0016  0.0228  235 ILE A CA  
1713 C C   . ILE A 234 ? 0.3209 0.4383 0.3167 -0.0367 0.0059  0.0168  235 ILE A C   
1714 O O   . ILE A 234 ? 0.3267 0.4546 0.3183 -0.0397 0.0082  0.0143  235 ILE A O   
1715 C CB  . ILE A 234 ? 0.3339 0.4471 0.3288 -0.0410 -0.0012 0.0320  235 ILE A CB  
1716 C CG1 . ILE A 234 ? 0.3528 0.4564 0.3508 -0.0392 -0.0057 0.0380  235 ILE A CG1 
1717 C CG2 . ILE A 234 ? 0.3366 0.4535 0.3333 -0.0447 -0.0007 0.0354  235 ILE A CG2 
1718 C CD1 . ILE A 234 ? 0.3748 0.4663 0.3793 -0.0353 -0.0070 0.0374  235 ILE A CD1 
1719 N N   . LEU A 235 ? 0.3085 0.4222 0.3088 -0.0345 0.0069  0.0144  236 LEU A N   
1720 C CA  . LEU A 235 ? 0.3010 0.4226 0.3025 -0.0351 0.0107  0.0092  236 LEU A CA  
1721 C C   . LEU A 235 ? 0.3037 0.4325 0.3051 -0.0405 0.0108  0.0143  236 LEU A C   
1722 O O   . LEU A 235 ? 0.3034 0.4270 0.3063 -0.0421 0.0076  0.0213  236 LEU A O   
1723 C CB  . LEU A 235 ? 0.2958 0.4098 0.3027 -0.0301 0.0112  0.0048  236 LEU A CB  
1724 C CG  . LEU A 235 ? 0.3078 0.4138 0.3155 -0.0249 0.0109  0.0006  236 LEU A CG  
1725 C CD1 . LEU A 235 ? 0.3152 0.4127 0.3278 -0.0209 0.0098  -0.0006 236 LEU A CD1 
1726 C CD2 . LEU A 235 ? 0.3124 0.4243 0.3193 -0.0238 0.0142  -0.0064 236 LEU A CD2 
1727 N N   . ASP A 236 ? 0.3041 0.4450 0.3044 -0.0434 0.0145  0.0109  237 ASP A N   
1728 C CA  . ASP A 236 ? 0.3188 0.4677 0.3192 -0.0488 0.0149  0.0155  237 ASP A CA  
1729 C C   . ASP A 236 ? 0.3116 0.4549 0.3185 -0.0468 0.0145  0.0153  237 ASP A C   
1730 O O   . ASP A 236 ? 0.3079 0.4439 0.3187 -0.0413 0.0147  0.0104  237 ASP A O   
1731 C CB  . ASP A 236 ? 0.3678 0.5327 0.3651 -0.0528 0.0193  0.0113  237 ASP A CB  
1732 C CG  . ASP A 236 ? 0.4782 0.6456 0.4790 -0.0485 0.0234  0.0009  237 ASP A CG  
1733 O OD1 . ASP A 236 ? 0.5126 0.6809 0.5112 -0.0465 0.0248  -0.0046 237 ASP A OD1 
1734 O OD2 . ASP A 236 ? 0.5092 0.6773 0.5157 -0.0469 0.0249  -0.0017 237 ASP A OD2 
1735 N N   . ASP A 237 ? 0.3124 0.4593 0.3205 -0.0514 0.0138  0.0209  238 ASP A N   
1736 C CA  . ASP A 237 ? 0.3208 0.4628 0.3350 -0.0503 0.0130  0.0213  238 ASP A CA  
1737 C C   . ASP A 237 ? 0.3065 0.4526 0.3251 -0.0471 0.0163  0.0136  238 ASP A C   
1738 O O   . ASP A 237 ? 0.3144 0.4533 0.3379 -0.0440 0.0150  0.0126  238 ASP A O   
1739 C CB  . ASP A 237 ? 0.3713 0.5179 0.3859 -0.0568 0.0119  0.0288  238 ASP A CB  
1740 C CG  . ASP A 237 ? 0.4783 0.6170 0.4917 -0.0589 0.0074  0.0374  238 ASP A CG  
1741 O OD1 . ASP A 237 ? 0.4966 0.6222 0.5127 -0.0548 0.0046  0.0377  238 ASP A OD1 
1742 O OD2 . ASP A 237 ? 0.5201 0.6660 0.5302 -0.0649 0.0068  0.0440  238 ASP A OD2 
1743 N N   . GLU A 238 ? 0.2868 0.4447 0.3043 -0.0480 0.0204  0.0083  239 GLU A N   
1744 C CA  . GLU A 238 ? 0.2824 0.4447 0.3056 -0.0446 0.0235  0.0010  239 GLU A CA  
1745 C C   . GLU A 238 ? 0.2685 0.4205 0.2943 -0.0375 0.0227  -0.0040 239 GLU A C   
1746 O O   . GLU A 238 ? 0.2660 0.4139 0.2974 -0.0339 0.0222  -0.0061 239 GLU A O   
1747 C CB  . GLU A 238 ? 0.3201 0.4978 0.3424 -0.0473 0.0284  -0.0043 239 GLU A CB  
1748 C CG  . GLU A 238 ? 0.3750 0.5610 0.4044 -0.0469 0.0313  -0.0084 239 GLU A CG  
1749 N N   . THR A 239 ? 0.2546 0.4023 0.2760 -0.0359 0.0221  -0.0049 240 THR A N   
1750 C CA  . THR A 239 ? 0.2554 0.3932 0.2784 -0.0298 0.0212  -0.0088 240 THR A CA  
1751 C C   . THR A 239 ? 0.2421 0.3677 0.2672 -0.0274 0.0173  -0.0049 240 THR A C   
1752 O O   . THR A 239 ? 0.2435 0.3642 0.2728 -0.0230 0.0169  -0.0081 240 THR A O   
1753 C CB  . THR A 239 ? 0.2806 0.4169 0.2981 -0.0297 0.0211  -0.0097 240 THR A CB  
1754 O OG1 . THR A 239 ? 0.3042 0.4531 0.3187 -0.0334 0.0245  -0.0125 240 THR A OG1 
1755 C CG2 . THR A 239 ? 0.2799 0.4085 0.2996 -0.0239 0.0211  -0.0147 240 THR A CG2 
1756 N N   . ILE A 240 ? 0.2264 0.3476 0.2489 -0.0305 0.0143  0.0019  241 ILE A N   
1757 C CA  . ILE A 240 ? 0.2222 0.3324 0.2469 -0.0287 0.0108  0.0050  241 ILE A CA  
1758 C C   . ILE A 240 ? 0.2068 0.3178 0.2371 -0.0277 0.0110  0.0032  241 ILE A C   
1759 O O   . ILE A 240 ? 0.2059 0.3099 0.2388 -0.0240 0.0096  0.0013  241 ILE A O   
1760 C CB  . ILE A 240 ? 0.2355 0.3421 0.2584 -0.0328 0.0079  0.0125  241 ILE A CB  
1761 C CG1 . ILE A 240 ? 0.2501 0.3568 0.2679 -0.0341 0.0070  0.0153  241 ILE A CG1 
1762 C CG2 . ILE A 240 ? 0.2377 0.3331 0.2638 -0.0310 0.0047  0.0143  241 ILE A CG2 
1763 C CD1 . ILE A 240 ? 0.2722 0.3714 0.2889 -0.0296 0.0062  0.0126  241 ILE A CD1 
1764 N N   . LYS A 241 ? 0.1984 0.3189 0.2305 -0.0314 0.0128  0.0038  242 LYS A N   
1765 C CA  . LYS A 241 ? 0.1932 0.3169 0.2309 -0.0314 0.0132  0.0026  242 LYS A CA  
1766 C C   . LYS A 241 ? 0.1681 0.2928 0.2102 -0.0262 0.0146  -0.0036 242 LYS A C   
1767 O O   . LYS A 241 ? 0.1652 0.2858 0.2112 -0.0240 0.0128  -0.0041 242 LYS A O   
1768 C CB  . LYS A 241 ? 0.2241 0.3597 0.2623 -0.0370 0.0153  0.0045  242 LYS A CB  
1769 C CG  . LYS A 241 ? 0.3001 0.4406 0.3445 -0.0378 0.0158  0.0036  242 LYS A CG  
1770 C CD  . LYS A 241 ? 0.3665 0.5193 0.4147 -0.0367 0.0199  -0.0022 242 LYS A CD  
1771 C CE  . LYS A 241 ? 0.4106 0.5726 0.4639 -0.0400 0.0211  -0.0017 242 LYS A CE  
1772 N NZ  . LYS A 241 ? 0.4513 0.6176 0.5013 -0.0471 0.0208  0.0044  242 LYS A NZ  
1773 N N   . ASN A 242 ? 0.1538 0.2839 0.1957 -0.0244 0.0175  -0.0082 243 ASN A N   
1774 C CA  . ASN A 242 ? 0.1382 0.2689 0.1853 -0.0193 0.0188  -0.0138 243 ASN A CA  
1775 C C   . ASN A 242 ? 0.1232 0.2423 0.1695 -0.0147 0.0163  -0.0142 243 ASN A C   
1776 O O   . ASN A 242 ? 0.1101 0.2267 0.1612 -0.0110 0.0153  -0.0160 243 ASN A O   
1777 C CB  . ASN A 242 ? 0.1377 0.2776 0.1853 -0.0192 0.0230  -0.0191 243 ASN A CB  
1778 C CG  . ASN A 242 ? 0.1659 0.3190 0.2155 -0.0234 0.0260  -0.0198 243 ASN A CG  
1779 O OD1 . ASN A 242 ? 0.1860 0.3430 0.2409 -0.0240 0.0258  -0.0191 243 ASN A OD1 
1780 N ND2 . ASN A 242 ? 0.1629 0.3240 0.2082 -0.0268 0.0288  -0.0211 243 ASN A ND2 
1781 N N   . TYR A 243 ? 0.1210 0.2335 0.1614 -0.0153 0.0149  -0.0119 244 TYR A N   
1782 C CA  . TYR A 243 ? 0.1297 0.2318 0.1687 -0.0116 0.0126  -0.0120 244 TYR A CA  
1783 C C   . TYR A 243 ? 0.1413 0.2371 0.1818 -0.0111 0.0096  -0.0094 244 TYR A C   
1784 O O   . TYR A 243 ? 0.1435 0.2343 0.1858 -0.0076 0.0082  -0.0107 244 TYR A O   
1785 C CB  . TYR A 243 ? 0.1259 0.2236 0.1588 -0.0126 0.0120  -0.0102 244 TYR A CB  
1786 C CG  . TYR A 243 ? 0.1364 0.2375 0.1677 -0.0115 0.0145  -0.0142 244 TYR A CG  
1787 C CD1 . TYR A 243 ? 0.1437 0.2532 0.1786 -0.0110 0.0178  -0.0190 244 TYR A CD1 
1788 C CD2 . TYR A 243 ? 0.1546 0.2509 0.1812 -0.0112 0.0137  -0.0136 244 TYR A CD2 
1789 C CE1 . TYR A 243 ? 0.1629 0.2754 0.1968 -0.0103 0.0202  -0.0236 244 TYR A CE1 
1790 C CE2 . TYR A 243 ? 0.1689 0.2686 0.1941 -0.0106 0.0159  -0.0177 244 TYR A CE2 
1791 C CZ  . TYR A 243 ? 0.1790 0.2865 0.2077 -0.0102 0.0192  -0.0229 244 TYR A CZ  
1792 O OH  . TYR A 243 ? 0.1846 0.2953 0.2126 -0.0098 0.0216  -0.0279 244 TYR A OH  
1793 N N   . GLN A 244 ? 0.1454 0.2419 0.1855 -0.0150 0.0084  -0.0056 245 GLN A N   
1794 C CA  . GLN A 244 ? 0.1440 0.2354 0.1858 -0.0154 0.0057  -0.0037 245 GLN A CA  
1795 C C   . GLN A 244 ? 0.1283 0.2241 0.1757 -0.0138 0.0057  -0.0059 245 GLN A C   
1796 O O   . GLN A 244 ? 0.1257 0.2169 0.1742 -0.0118 0.0036  -0.0063 245 GLN A O   
1797 C CB  . GLN A 244 ? 0.1747 0.2664 0.2158 -0.0203 0.0047  0.0006  245 GLN A CB  
1798 C CG  . GLN A 244 ? 0.2106 0.2952 0.2476 -0.0213 0.0031  0.0038  245 GLN A CG  
1799 C CD  . GLN A 244 ? 0.2441 0.3298 0.2811 -0.0264 0.0023  0.0088  245 GLN A CD  
1800 O OE1 . GLN A 244 ? 0.2523 0.3459 0.2909 -0.0298 0.0036  0.0100  245 GLN A OE1 
1801 N NE2 . GLN A 244 ? 0.2398 0.3180 0.2754 -0.0271 0.0001  0.0121  245 GLN A NE2 
1802 N N   . THR A 245 ? 0.1213 0.2266 0.1722 -0.0146 0.0082  -0.0075 246 THR A N   
1803 C CA  . THR A 245 ? 0.1186 0.2293 0.1759 -0.0127 0.0083  -0.0097 246 THR A CA  
1804 C C   . THR A 245 ? 0.1127 0.2201 0.1723 -0.0074 0.0078  -0.0123 246 THR A C   
1805 O O   . THR A 245 ? 0.1105 0.2170 0.1736 -0.0056 0.0057  -0.0122 246 THR A O   
1806 C CB  . THR A 245 ? 0.1382 0.2606 0.1994 -0.0146 0.0115  -0.0113 246 THR A CB  
1807 O OG1 . THR A 245 ? 0.1646 0.2897 0.2237 -0.0200 0.0114  -0.0078 246 THR A OG1 
1808 C CG2 . THR A 245 ? 0.1270 0.2559 0.1963 -0.0123 0.0118  -0.0137 246 THR A CG2 
1809 N N   . GLU A 246 ? 0.1154 0.2212 0.1730 -0.0053 0.0095  -0.0145 247 GLU A N   
1810 C CA  . GLU A 246 ? 0.1231 0.2248 0.1829 -0.0006 0.0090  -0.0166 247 GLU A CA  
1811 C C   . GLU A 246 ? 0.1267 0.2192 0.1826 0.0002  0.0058  -0.0142 247 GLU A C   
1812 O O   . GLU A 246 ? 0.1245 0.2149 0.1833 0.0030  0.0041  -0.0143 247 GLU A O   
1813 C CB  . GLU A 246 ? 0.1467 0.2482 0.2049 0.0007  0.0116  -0.0197 247 GLU A CB  
1814 C CG  . GLU A 246 ? 0.2001 0.3113 0.2626 0.0004  0.0152  -0.0235 247 GLU A CG  
1815 C CD  . GLU A 246 ? 0.3127 0.4234 0.3771 0.0034  0.0174  -0.0281 247 GLU A CD  
1816 O OE1 . GLU A 246 ? 0.3269 0.4319 0.3945 0.0073  0.0159  -0.0287 247 GLU A OE1 
1817 O OE2 . GLU A 246 ? 0.3621 0.4788 0.4251 0.0016  0.0206  -0.0313 247 GLU A OE2 
1818 N N   . LEU A 247 ? 0.1394 0.2269 0.1894 -0.0023 0.0050  -0.0121 248 LEU A N   
1819 C CA  . LEU A 247 ? 0.1510 0.2303 0.1974 -0.0016 0.0024  -0.0106 248 LEU A CA  
1820 C C   . LEU A 247 ? 0.1505 0.2298 0.1991 -0.0022 -0.0001 -0.0095 248 LEU A C   
1821 O O   . LEU A 247 ? 0.1579 0.2336 0.2061 -0.0003 -0.0019 -0.0095 248 LEU A O   
1822 C CB  . LEU A 247 ? 0.1652 0.2400 0.2065 -0.0042 0.0021  -0.0087 248 LEU A CB  
1823 C CG  . LEU A 247 ? 0.2055 0.2722 0.2435 -0.0030 0.0002  -0.0082 248 LEU A CG  
1824 C CD1 . LEU A 247 ? 0.2091 0.2730 0.2448 -0.0004 0.0011  -0.0095 248 LEU A CD1 
1825 C CD2 . LEU A 247 ? 0.2322 0.2949 0.2679 -0.0059 -0.0010 -0.0060 248 LEU A CD2 
1826 N N   . LYS A 248 ? 0.1435 0.2276 0.1945 -0.0051 -0.0002 -0.0087 249 LYS A N   
1827 C CA  . LYS A 248 ? 0.1385 0.2240 0.1921 -0.0061 -0.0024 -0.0081 249 LYS A CA  
1828 C C   . LYS A 248 ? 0.1362 0.2259 0.1947 -0.0028 -0.0032 -0.0090 249 LYS A C   
1829 O O   . LYS A 248 ? 0.1345 0.2229 0.1932 -0.0022 -0.0057 -0.0084 249 LYS A O   
1830 C CB  . LYS A 248 ? 0.1473 0.2383 0.2033 -0.0101 -0.0020 -0.0070 249 LYS A CB  
1831 C CG  . LYS A 248 ? 0.1963 0.2907 0.2560 -0.0114 -0.0041 -0.0068 249 LYS A CG  
1832 C CD  . LYS A 248 ? 0.2380 0.3389 0.3010 -0.0153 -0.0034 -0.0059 249 LYS A CD  
1833 C CE  . LYS A 248 ? 0.2706 0.3748 0.3371 -0.0170 -0.0059 -0.0059 249 LYS A CE  
1834 N NZ  . LYS A 248 ? 0.3015 0.4077 0.3693 -0.0221 -0.0060 -0.0046 249 LYS A NZ  
1835 N N   . THR A 249 ? 0.1339 0.2287 0.1968 -0.0008 -0.0010 -0.0104 250 THR A N   
1836 C CA  . THR A 249 ? 0.1370 0.2356 0.2063 0.0028  -0.0016 -0.0111 250 THR A CA  
1837 C C   . THR A 249 ? 0.1386 0.2308 0.2062 0.0060  -0.0032 -0.0106 250 THR A C   
1838 O O   . THR A 249 ? 0.1381 0.2310 0.2082 0.0073  -0.0059 -0.0090 250 THR A O   
1839 C CB  . THR A 249 ? 0.1448 0.2499 0.2197 0.0043  0.0016  -0.0136 250 THR A CB  
1840 O OG1 . THR A 249 ? 0.1598 0.2715 0.2356 0.0007  0.0032  -0.0138 250 THR A OG1 
1841 C CG2 . THR A 249 ? 0.1384 0.2473 0.2219 0.0083  0.0009  -0.0144 250 THR A CG2 
1842 N N   . LEU A 250 ? 0.1336 0.2203 0.1969 0.0069  -0.0017 -0.0116 251 LEU A N   
1843 C CA  . LEU A 250 ? 0.1376 0.2182 0.1990 0.0095  -0.0027 -0.0111 251 LEU A CA  
1844 C C   . LEU A 250 ? 0.1616 0.2378 0.2179 0.0080  -0.0055 -0.0091 251 LEU A C   
1845 O O   . LEU A 250 ? 0.1657 0.2406 0.2227 0.0096  -0.0076 -0.0076 251 LEU A O   
1846 C CB  . LEU A 250 ? 0.1312 0.2075 0.1888 0.0099  -0.0004 -0.0129 251 LEU A CB  
1847 C CG  . LEU A 250 ? 0.1424 0.2226 0.2048 0.0117  0.0026  -0.0160 251 LEU A CG  
1848 C CD1 . LEU A 250 ? 0.1455 0.2238 0.2028 0.0104  0.0049  -0.0177 251 LEU A CD1 
1849 C CD2 . LEU A 250 ? 0.1478 0.2270 0.2167 0.0157  0.0019  -0.0165 251 LEU A CD2 
1850 N N   . GLU A 251 ? 0.1743 0.2487 0.2259 0.0048  -0.0056 -0.0090 252 GLU A N   
1851 C CA  . GLU A 251 ? 0.1987 0.2693 0.2459 0.0033  -0.0077 -0.0082 252 GLU A CA  
1852 C C   . GLU A 251 ? 0.2196 0.2945 0.2692 0.0026  -0.0104 -0.0071 252 GLU A C   
1853 O O   . GLU A 251 ? 0.2264 0.2995 0.2732 0.0024  -0.0123 -0.0065 252 GLU A O   
1854 C CB  . GLU A 251 ? 0.2315 0.2990 0.2751 0.0002  -0.0072 -0.0087 252 GLU A CB  
1855 C CG  . GLU A 251 ? 0.3019 0.3644 0.3411 -0.0010 -0.0087 -0.0091 252 GLU A CG  
1856 C CD  . GLU A 251 ? 0.3724 0.4374 0.4122 -0.0033 -0.0109 -0.0094 252 GLU A CD  
1857 O OE1 . GLU A 251 ? 0.3737 0.4434 0.4170 -0.0050 -0.0112 -0.0091 252 GLU A OE1 
1858 O OE2 . GLU A 251 ? 0.3917 0.4548 0.4285 -0.0036 -0.0122 -0.0102 252 GLU A OE2 
1859 N N   . GLU A 252 ? 0.2276 0.3090 0.2824 0.0019  -0.0106 -0.0069 253 GLU A N   
1860 C CA  . GLU A 252 ? 0.2420 0.3286 0.2997 0.0011  -0.0134 -0.0056 253 GLU A CA  
1861 C C   . GLU A 252 ? 0.2389 0.3271 0.3000 0.0045  -0.0150 -0.0037 253 GLU A C   
1862 O O   . GLU A 252 ? 0.2522 0.3418 0.3121 0.0039  -0.0178 -0.0019 253 GLU A O   
1863 C CB  . GLU A 252 ? 0.2948 0.3886 0.3580 -0.0005 -0.0130 -0.0058 253 GLU A CB  
1864 C CG  . GLU A 252 ? 0.4380 0.5347 0.5006 -0.0043 -0.0153 -0.0057 253 GLU A CG  
1865 C CD  . GLU A 252 ? 0.6029 0.7069 0.6699 -0.0042 -0.0183 -0.0041 253 GLU A CD  
1866 O OE1 . GLU A 252 ? 0.6444 0.7483 0.7114 -0.0018 -0.0202 -0.0024 253 GLU A OE1 
1867 O OE2 . GLU A 252 ? 0.6525 0.7626 0.7230 -0.0067 -0.0191 -0.0043 253 GLU A OE2 
1868 N N   . ALA A 253 ? 0.2205 0.3087 0.2860 0.0077  -0.0132 -0.0040 254 ALA A N   
1869 C CA  . ALA A 253 ? 0.2032 0.2919 0.2735 0.0112  -0.0146 -0.0020 254 ALA A CA  
1870 C C   . ALA A 253 ? 0.1967 0.2793 0.2610 0.0114  -0.0159 -0.0005 254 ALA A C   
1871 O O   . ALA A 253 ? 0.2035 0.2875 0.2693 0.0121  -0.0188 0.0027  254 ALA A O   
1872 C CB  . ALA A 253 ? 0.1928 0.2816 0.2690 0.0143  -0.0118 -0.0039 254 ALA A CB  
1873 N N   . LEU A 254 ? 0.1812 0.2578 0.2390 0.0104  -0.0140 -0.0024 255 LEU A N   
1874 C CA  . LEU A 254 ? 0.1659 0.2372 0.2184 0.0106  -0.0147 -0.0014 255 LEU A CA  
1875 C C   . LEU A 254 ? 0.1862 0.2570 0.2321 0.0074  -0.0163 -0.0013 255 LEU A C   
1876 O O   . LEU A 254 ? 0.2069 0.2750 0.2487 0.0073  -0.0171 -0.0002 255 LEU A O   
1877 C CB  . LEU A 254 ? 0.1377 0.2032 0.1875 0.0115  -0.0118 -0.0035 255 LEU A CB  
1878 C CG  . LEU A 254 ? 0.1126 0.1782 0.1682 0.0144  -0.0098 -0.0047 255 LEU A CG  
1879 C CD1 . LEU A 254 ? 0.1122 0.1738 0.1641 0.0141  -0.0069 -0.0074 255 LEU A CD1 
1880 C CD2 . LEU A 254 ? 0.0998 0.1646 0.1604 0.0172  -0.0113 -0.0024 255 LEU A CD2 
1881 N N   . SER A 255 ? 0.1819 0.2552 0.2267 0.0047  -0.0165 -0.0028 256 SER A N   
1882 C CA  . SER A 255 ? 0.1940 0.2667 0.2333 0.0014  -0.0175 -0.0042 256 SER A CA  
1883 C C   . SER A 255 ? 0.2023 0.2685 0.2362 0.0013  -0.0158 -0.0061 256 SER A C   
1884 O O   . SER A 255 ? 0.2202 0.2856 0.2497 0.0000  -0.0167 -0.0065 256 SER A O   
1885 C CB  . SER A 255 ? 0.2116 0.2893 0.2500 0.0001  -0.0207 -0.0021 256 SER A CB  
1886 O OG  . SER A 255 ? 0.2353 0.3198 0.2793 0.0000  -0.0226 -0.0003 256 SER A OG  
1887 N N   . VAL A 256 ? 0.1897 0.2518 0.2240 0.0025  -0.0133 -0.0071 257 VAL A N   
1888 C CA  . VAL A 256 ? 0.1784 0.2346 0.2087 0.0027  -0.0117 -0.0085 257 VAL A CA  
1889 C C   . VAL A 256 ? 0.1759 0.2299 0.2027 0.0002  -0.0119 -0.0109 257 VAL A C   
1890 O O   . VAL A 256 ? 0.1690 0.2209 0.1923 0.0002  -0.0119 -0.0117 257 VAL A O   
1891 C CB  . VAL A 256 ? 0.1802 0.2339 0.2118 0.0040  -0.0094 -0.0090 257 VAL A CB  
1892 C CG1 . VAL A 256 ? 0.1858 0.2341 0.2135 0.0046  -0.0082 -0.0099 257 VAL A CG1 
1893 C CG2 . VAL A 256 ? 0.1792 0.2354 0.2150 0.0065  -0.0088 -0.0079 257 VAL A CG2 
1894 N N   . ARG A 257 ? 0.1828 0.2374 0.2112 -0.0019 -0.0120 -0.0121 258 ARG A N   
1895 C CA  . ARG A 257 ? 0.1970 0.2488 0.2235 -0.0042 -0.0121 -0.0149 258 ARG A CA  
1896 C C   . ARG A 257 ? 0.2111 0.2654 0.2345 -0.0056 -0.0136 -0.0165 258 ARG A C   
1897 O O   . ARG A 257 ? 0.2161 0.2677 0.2370 -0.0061 -0.0130 -0.0191 258 ARG A O   
1898 C CB  . ARG A 257 ? 0.1990 0.2507 0.2284 -0.0065 -0.0122 -0.0156 258 ARG A CB  
1899 C CG  . ARG A 257 ? 0.2117 0.2595 0.2424 -0.0059 -0.0106 -0.0144 258 ARG A CG  
1900 C CD  . ARG A 257 ? 0.2240 0.2728 0.2582 -0.0085 -0.0108 -0.0138 258 ARG A CD  
1901 N NE  . ARG A 257 ? 0.2330 0.2884 0.2695 -0.0093 -0.0116 -0.0129 258 ARG A NE  
1902 C CZ  . ARG A 257 ? 0.2473 0.3054 0.2871 -0.0119 -0.0119 -0.0124 258 ARG A CZ  
1903 N NH1 . ARG A 257 ? 0.2323 0.2864 0.2734 -0.0143 -0.0117 -0.0124 258 ARG A NH1 
1904 N NH2 . ARG A 257 ? 0.2372 0.3020 0.2796 -0.0123 -0.0126 -0.0116 258 ARG A NH2 
1905 N N   . SER A 258 ? 0.2095 0.2699 0.2333 -0.0062 -0.0155 -0.0149 259 SER A N   
1906 C CA  . SER A 258 ? 0.2073 0.2721 0.2279 -0.0081 -0.0172 -0.0156 259 SER A CA  
1907 C C   . SER A 258 ? 0.2135 0.2775 0.2305 -0.0066 -0.0169 -0.0143 259 SER A C   
1908 O O   . SER A 258 ? 0.2216 0.2860 0.2347 -0.0083 -0.0167 -0.0169 259 SER A O   
1909 C CB  . SER A 258 ? 0.2079 0.2800 0.2306 -0.0091 -0.0197 -0.0132 259 SER A CB  
1910 O OG  . SER A 258 ? 0.2562 0.3298 0.2804 -0.0121 -0.0201 -0.0160 259 SER A OG  
1911 N N   . LYS A 259 ? 0.2075 0.2704 0.2262 -0.0037 -0.0167 -0.0107 260 LYS A N   
1912 C CA  . LYS A 259 ? 0.2091 0.2707 0.2250 -0.0025 -0.0164 -0.0091 260 LYS A CA  
1913 C C   . LYS A 259 ? 0.2157 0.2721 0.2288 -0.0024 -0.0141 -0.0123 260 LYS A C   
1914 O O   . LYS A 259 ? 0.2240 0.2814 0.2332 -0.0037 -0.0140 -0.0137 260 LYS A O   
1915 C CB  . LYS A 259 ? 0.2241 0.2844 0.2436 0.0007  -0.0165 -0.0053 260 LYS A CB  
1916 C CG  . LYS A 259 ? 0.2594 0.3251 0.2819 0.0009  -0.0192 -0.0013 260 LYS A CG  
1917 C CD  . LYS A 259 ? 0.2993 0.3632 0.3269 0.0043  -0.0191 0.0019  260 LYS A CD  
1918 C CE  . LYS A 259 ? 0.3499 0.4195 0.3826 0.0048  -0.0221 0.0059  260 LYS A CE  
1919 N NZ  . LYS A 259 ? 0.3794 0.4479 0.4198 0.0084  -0.0215 0.0070  260 LYS A NZ  
1920 N N   . LEU A 260 ? 0.2205 0.2723 0.2358 -0.0012 -0.0125 -0.0137 261 LEU A N   
1921 C CA  . LEU A 260 ? 0.2405 0.2875 0.2544 -0.0009 -0.0106 -0.0164 261 LEU A CA  
1922 C C   . LEU A 260 ? 0.2434 0.2910 0.2555 -0.0032 -0.0105 -0.0206 261 LEU A C   
1923 O O   . LEU A 260 ? 0.2527 0.2991 0.2626 -0.0032 -0.0095 -0.0226 261 LEU A O   
1924 C CB  . LEU A 260 ? 0.2532 0.2962 0.2701 0.0003  -0.0095 -0.0162 261 LEU A CB  
1925 C CG  . LEU A 260 ? 0.2890 0.3274 0.3052 0.0018  -0.0079 -0.0168 261 LEU A CG  
1926 C CD1 . LEU A 260 ? 0.2902 0.3287 0.3045 0.0034  -0.0075 -0.0150 261 LEU A CD1 
1927 C CD2 . LEU A 260 ? 0.3107 0.3468 0.3295 0.0024  -0.0072 -0.0157 261 LEU A CD2 
1928 N N   . SER A 261 ? 0.2361 0.2859 0.2494 -0.0054 -0.0115 -0.0224 262 SER A N   
1929 C CA  . SER A 261 ? 0.2328 0.2835 0.2451 -0.0080 -0.0113 -0.0273 262 SER A CA  
1930 C C   . SER A 261 ? 0.2349 0.2914 0.2424 -0.0097 -0.0119 -0.0284 262 SER A C   
1931 O O   . SER A 261 ? 0.2383 0.2947 0.2441 -0.0106 -0.0105 -0.0325 262 SER A O   
1932 C CB  . SER A 261 ? 0.2343 0.2865 0.2494 -0.0103 -0.0125 -0.0289 262 SER A CB  
1933 O OG  . SER A 261 ? 0.2635 0.3099 0.2822 -0.0104 -0.0115 -0.0315 262 SER A OG  
1934 N N   . THR A 262 ? 0.2298 0.2919 0.2357 -0.0104 -0.0139 -0.0246 263 THR A N   
1935 C CA  . THR A 262 ? 0.2347 0.3035 0.2358 -0.0127 -0.0150 -0.0241 263 THR A CA  
1936 C C   . THR A 262 ? 0.2297 0.2972 0.2279 -0.0116 -0.0135 -0.0233 263 THR A C   
1937 O O   . THR A 262 ? 0.2389 0.3100 0.2333 -0.0138 -0.0127 -0.0266 263 THR A O   
1938 C CB  . THR A 262 ? 0.2544 0.3288 0.2560 -0.0131 -0.0178 -0.0189 263 THR A CB  
1939 O OG1 . THR A 262 ? 0.2674 0.3434 0.2719 -0.0145 -0.0189 -0.0204 263 THR A OG1 
1940 C CG2 . THR A 262 ? 0.2635 0.3458 0.2600 -0.0159 -0.0196 -0.0172 263 THR A CG2 
1941 N N   . TYR A 263 ? 0.2191 0.2821 0.2192 -0.0084 -0.0130 -0.0195 264 TYR A N   
1942 C CA  . TYR A 263 ? 0.2185 0.2796 0.2165 -0.0073 -0.0116 -0.0186 264 TYR A CA  
1943 C C   . TYR A 263 ? 0.2013 0.2600 0.1988 -0.0075 -0.0092 -0.0241 264 TYR A C   
1944 O O   . TYR A 263 ? 0.2004 0.2617 0.1947 -0.0086 -0.0081 -0.0252 264 TYR A O   
1945 C CB  . TYR A 263 ? 0.2258 0.2816 0.2268 -0.0039 -0.0113 -0.0147 264 TYR A CB  
1946 C CG  . TYR A 263 ? 0.2473 0.3053 0.2499 -0.0032 -0.0135 -0.0092 264 TYR A CG  
1947 C CD1 . TYR A 263 ? 0.2626 0.3267 0.2625 -0.0054 -0.0156 -0.0062 264 TYR A CD1 
1948 C CD2 . TYR A 263 ? 0.2683 0.3228 0.2754 -0.0004 -0.0135 -0.0069 264 TYR A CD2 
1949 C CE1 . TYR A 263 ? 0.2843 0.3502 0.2869 -0.0044 -0.0180 -0.0006 264 TYR A CE1 
1950 C CE2 . TYR A 263 ? 0.2887 0.3451 0.2988 0.0007  -0.0154 -0.0024 264 TYR A CE2 
1951 C CZ  . TYR A 263 ? 0.3049 0.3666 0.3132 -0.0012 -0.0178 0.0011  264 TYR A CZ  
1952 O OH  . TYR A 263 ? 0.3328 0.3961 0.3452 0.0001  -0.0201 0.0062  264 TYR A OH  
1953 N N   . THR A 264 ? 0.1916 0.2456 0.1928 -0.0065 -0.0082 -0.0272 265 THR A N   
1954 C CA  . THR A 264 ? 0.1907 0.2419 0.1933 -0.0062 -0.0062 -0.0323 265 THR A CA  
1955 C C   . THR A 264 ? 0.1925 0.2488 0.1930 -0.0093 -0.0057 -0.0379 265 THR A C   
1956 O O   . THR A 264 ? 0.1980 0.2554 0.1977 -0.0096 -0.0038 -0.0416 265 THR A O   
1957 C CB  . THR A 264 ? 0.2125 0.2573 0.2203 -0.0045 -0.0060 -0.0328 265 THR A CB  
1958 O OG1 . THR A 264 ? 0.2255 0.2671 0.2343 -0.0020 -0.0061 -0.0282 265 THR A OG1 
1959 C CG2 . THR A 264 ? 0.2176 0.2590 0.2287 -0.0039 -0.0043 -0.0377 265 THR A CG2 
1960 N N   . PHE A 265 ? 0.1866 0.2467 0.1865 -0.0118 -0.0072 -0.0389 266 PHE A N   
1961 C CA  . PHE A 265 ? 0.1941 0.2602 0.1917 -0.0154 -0.0070 -0.0446 266 PHE A CA  
1962 C C   . PHE A 265 ? 0.2144 0.2881 0.2057 -0.0176 -0.0067 -0.0439 266 PHE A C   
1963 O O   . PHE A 265 ? 0.2274 0.3048 0.2170 -0.0194 -0.0048 -0.0497 266 PHE A O   
1964 C CB  . PHE A 265 ? 0.1813 0.2504 0.1792 -0.0177 -0.0093 -0.0441 266 PHE A CB  
1965 C CG  . PHE A 265 ? 0.1738 0.2514 0.1680 -0.0222 -0.0098 -0.0488 266 PHE A CG  
1966 C CD1 . PHE A 265 ? 0.1810 0.2581 0.1775 -0.0241 -0.0083 -0.0570 266 PHE A CD1 
1967 C CD2 . PHE A 265 ? 0.1715 0.2575 0.1607 -0.0247 -0.0120 -0.0449 266 PHE A CD2 
1968 C CE1 . PHE A 265 ? 0.1877 0.2733 0.1806 -0.0287 -0.0086 -0.0621 266 PHE A CE1 
1969 C CE2 . PHE A 265 ? 0.1783 0.2732 0.1635 -0.0294 -0.0127 -0.0491 266 PHE A CE2 
1970 C CZ  . PHE A 265 ? 0.1778 0.2727 0.1645 -0.0315 -0.0108 -0.0580 266 PHE A CZ  
1971 N N   . ALA A 266 ? 0.2150 0.2914 0.2034 -0.0174 -0.0086 -0.0369 267 ALA A N   
1972 C CA  . ALA A 266 ? 0.2181 0.3016 0.2007 -0.0197 -0.0088 -0.0345 267 ALA A CA  
1973 C C   . ALA A 266 ? 0.2309 0.3122 0.2132 -0.0184 -0.0061 -0.0362 267 ALA A C   
1974 O O   . ALA A 266 ? 0.2325 0.3206 0.2105 -0.0212 -0.0048 -0.0385 267 ALA A O   
1975 C CB  . ALA A 266 ? 0.2102 0.2948 0.1920 -0.0190 -0.0117 -0.0259 267 ALA A CB  
1976 N N   . MET A 267 ? 0.2348 0.3078 0.2215 -0.0144 -0.0051 -0.0349 268 MET A N   
1977 C CA  . MET A 267 ? 0.2480 0.3188 0.2353 -0.0129 -0.0027 -0.0363 268 MET A CA  
1978 C C   . MET A 267 ? 0.2542 0.3262 0.2432 -0.0137 -0.0002 -0.0446 268 MET A C   
1979 O O   . MET A 267 ? 0.2607 0.3370 0.2478 -0.0148 0.0018  -0.0474 268 MET A O   
1980 C CB  . MET A 267 ? 0.2673 0.3295 0.2591 -0.0088 -0.0026 -0.0332 268 MET A CB  
1981 C CG  . MET A 267 ? 0.3033 0.3642 0.2942 -0.0078 -0.0043 -0.0259 268 MET A CG  
1982 S SD  . MET A 267 ? 0.4010 0.4529 0.3971 -0.0036 -0.0041 -0.0237 268 MET A SD  
1983 C CE  . MET A 267 ? 0.3659 0.4162 0.3626 -0.0026 -0.0016 -0.0263 268 MET A CE  
1984 N N   . LYS A 268 ? 0.2577 0.3265 0.2508 -0.0133 -0.0002 -0.0489 269 LYS A N   
1985 C CA  . LYS A 268 ? 0.2679 0.3370 0.2644 -0.0138 0.0020  -0.0574 269 LYS A CA  
1986 C C   . LYS A 268 ? 0.2859 0.3653 0.2772 -0.0181 0.0033  -0.0624 269 LYS A C   
1987 O O   . LYS A 268 ? 0.2916 0.3738 0.2836 -0.0183 0.0060  -0.0676 269 LYS A O   
1988 C CB  . LYS A 268 ? 0.2837 0.3476 0.2855 -0.0133 0.0012  -0.0601 269 LYS A CB  
1989 C CG  . LYS A 268 ? 0.3213 0.3756 0.3302 -0.0094 0.0013  -0.0590 269 LYS A CG  
1990 C CD  . LYS A 268 ? 0.3666 0.4192 0.3814 -0.0085 0.0037  -0.0663 269 LYS A CD  
1991 C CE  . LYS A 268 ? 0.3882 0.4318 0.4113 -0.0053 0.0034  -0.0659 269 LYS A CE  
1992 N NZ  . LYS A 268 ? 0.3880 0.4275 0.4151 -0.0062 0.0019  -0.0669 269 LYS A NZ  
1993 N N   . LEU A 269 ? 0.2870 0.3729 0.2731 -0.0216 0.0013  -0.0605 270 LEU A N   
1994 C CA  . LEU A 269 ? 0.2965 0.3936 0.2765 -0.0265 0.0021  -0.0648 270 LEU A CA  
1995 C C   . LEU A 269 ? 0.3153 0.4190 0.2901 -0.0279 0.0034  -0.0625 270 LEU A C   
1996 O O   . LEU A 269 ? 0.3198 0.4314 0.2921 -0.0310 0.0059  -0.0690 270 LEU A O   
1997 C CB  . LEU A 269 ? 0.2932 0.3965 0.2687 -0.0300 -0.0009 -0.0620 270 LEU A CB  
1998 C CG  . LEU A 269 ? 0.3026 0.4017 0.2826 -0.0299 -0.0022 -0.0651 270 LEU A CG  
1999 C CD1 . LEU A 269 ? 0.3135 0.4167 0.2902 -0.0318 -0.0059 -0.0589 270 LEU A CD1 
2000 C CD2 . LEU A 269 ? 0.3012 0.4039 0.2827 -0.0326 0.0000  -0.0760 270 LEU A CD2 
2001 N N   . THR A 270 ? 0.3254 0.4263 0.2990 -0.0261 0.0020  -0.0539 271 THR A N   
2002 C CA  . THR A 270 ? 0.3416 0.4479 0.3107 -0.0277 0.0031  -0.0508 271 THR A CA  
2003 C C   . THR A 270 ? 0.3614 0.4663 0.3338 -0.0260 0.0068  -0.0563 271 THR A C   
2004 O O   . THR A 270 ? 0.3640 0.4753 0.3329 -0.0281 0.0083  -0.0555 271 THR A O   
2005 C CB  . THR A 270 ? 0.3519 0.4547 0.3200 -0.0263 0.0005  -0.0405 271 THR A CB  
2006 O OG1 . THR A 270 ? 0.3606 0.4524 0.3348 -0.0212 0.0006  -0.0390 271 THR A OG1 
2007 C CG2 . THR A 270 ? 0.3504 0.4563 0.3155 -0.0282 -0.0033 -0.0345 271 THR A CG2 
2008 N N   . SER A 271 ? 0.3755 0.4728 0.3553 -0.0223 0.0080  -0.0613 272 SER A N   
2009 C CA  . SER A 271 ? 0.3914 0.4873 0.3761 -0.0203 0.0113  -0.0670 272 SER A CA  
2010 C C   . SER A 271 ? 0.4107 0.5139 0.3962 -0.0228 0.0142  -0.0776 272 SER A C   
2011 O O   . SER A 271 ? 0.4136 0.5167 0.4044 -0.0211 0.0171  -0.0835 272 SER A O   
2012 C CB  . SER A 271 ? 0.4079 0.4924 0.4009 -0.0152 0.0109  -0.0670 272 SER A CB  
2013 O OG  . SER A 271 ? 0.4409 0.5199 0.4345 -0.0125 0.0098  -0.0597 272 SER A OG  
2014 N N   . ASP A 272 ? 0.4207 0.5302 0.4021 -0.0268 0.0135  -0.0807 273 ASP A N   
2015 C CA  . ASP A 272 ? 0.4384 0.5554 0.4205 -0.0297 0.0164  -0.0916 273 ASP A CA  
2016 C C   . ASP A 272 ? 0.4548 0.5826 0.4326 -0.0326 0.0196  -0.0946 273 ASP A C   
2017 O O   . ASP A 272 ? 0.4591 0.5922 0.4299 -0.0349 0.0185  -0.0872 273 ASP A O   
2018 C CB  . ASP A 272 ? 0.4611 0.5838 0.4379 -0.0341 0.0144  -0.0930 273 ASP A CB  
2019 C CG  . ASP A 272 ? 0.5305 0.6607 0.5084 -0.0374 0.0174  -0.1052 273 ASP A CG  
2020 O OD1 . ASP A 272 ? 0.5458 0.6690 0.5324 -0.0349 0.0184  -0.1123 273 ASP A OD1 
2021 O OD2 . ASP A 272 ? 0.5591 0.7024 0.5294 -0.0426 0.0186  -0.1079 273 ASP A OD2 
2022 N N   . ALA A 273 ? 0.4602 0.5914 0.4432 -0.0324 0.0235  -0.1052 274 ALA A N   
2023 C CA  . ALA A 273 ? 0.4744 0.6170 0.4543 -0.0352 0.0271  -0.1091 274 ALA A CA  
2024 C C   . ALA A 273 ? 0.4838 0.6413 0.4527 -0.0424 0.0274  -0.1099 274 ALA A C   
2025 O O   . ALA A 273 ? 0.4832 0.6489 0.4456 -0.0454 0.0280  -0.1052 274 ALA A O   
2026 C CB  . ALA A 273 ? 0.4777 0.6204 0.4672 -0.0329 0.0313  -0.1210 274 ALA A CB  
2027 N N   . ASN A 274 ? 0.4930 0.6544 0.4599 -0.0455 0.0268  -0.1155 275 ASN A N   
2028 C CA  . ASN A 274 ? 0.5095 0.6861 0.4658 -0.0529 0.0267  -0.1166 275 ASN A CA  
2029 C C   . ASN A 274 ? 0.5240 0.7024 0.4715 -0.0551 0.0223  -0.1029 275 ASN A C   
2030 O O   . ASN A 274 ? 0.5290 0.7200 0.4677 -0.0605 0.0225  -0.0998 275 ASN A O   
2031 C CB  . ASN A 274 ? 0.5280 0.7072 0.4849 -0.0555 0.0266  -0.1253 275 ASN A CB  
2032 C CG  . ASN A 274 ? 0.5724 0.7528 0.5373 -0.0547 0.0313  -0.1403 275 ASN A CG  
2033 O OD1 . ASN A 274 ? 0.5801 0.7637 0.5486 -0.0535 0.0353  -0.1453 275 ASN A OD1 
2034 N ND2 . ASN A 274 ? 0.5873 0.7651 0.5562 -0.0554 0.0310  -0.1480 275 ASN A ND2 
2035 N N   . LEU A 275 ? 0.5295 0.6958 0.4800 -0.0511 0.0184  -0.0946 276 LEU A N   
2036 C CA  . LEU A 275 ? 0.5428 0.7091 0.4873 -0.0522 0.0141  -0.0816 276 LEU A CA  
2037 C C   . LEU A 275 ? 0.5624 0.7311 0.5039 -0.0526 0.0147  -0.0746 276 LEU A C   
2038 O O   . LEU A 275 ? 0.5616 0.7385 0.4955 -0.0569 0.0126  -0.0670 276 LEU A O   
2039 C CB  . LEU A 275 ? 0.5421 0.6939 0.4926 -0.0468 0.0108  -0.0758 276 LEU A CB  
2040 C CG  . LEU A 275 ? 0.5529 0.7026 0.4998 -0.0467 0.0063  -0.0629 276 LEU A CG  
2041 C CD1 . LEU A 275 ? 0.5579 0.7020 0.5072 -0.0453 0.0030  -0.0608 276 LEU A CD1 
2042 C CD2 . LEU A 275 ? 0.5563 0.6969 0.5068 -0.0422 0.0063  -0.0562 276 LEU A CD2 
2043 N N   . LYS A 276 ? 0.5810 0.7428 0.5290 -0.0482 0.0174  -0.0770 277 LYS A N   
2044 C CA  . LYS A 276 ? 0.6065 0.7693 0.5533 -0.0480 0.0184  -0.0713 277 LYS A CA  
2045 C C   . LYS A 276 ? 0.6369 0.8156 0.5765 -0.0543 0.0212  -0.0739 277 LYS A C   
2046 O O   . LYS A 276 ? 0.6422 0.8244 0.5775 -0.0565 0.0204  -0.0658 277 LYS A O   
2047 C CB  . LYS A 276 ? 0.6239 0.7761 0.5800 -0.0419 0.0205  -0.0740 277 LYS A CB  
2048 C CG  . LYS A 276 ? 0.6649 0.8023 0.6265 -0.0363 0.0173  -0.0684 277 LYS A CG  
2049 C CD  . LYS A 276 ? 0.7107 0.8393 0.6816 -0.0309 0.0194  -0.0725 277 LYS A CD  
2050 C CE  . LYS A 276 ? 0.7535 0.8688 0.7289 -0.0259 0.0165  -0.0661 277 LYS A CE  
2051 N NZ  . LYS A 276 ? 0.7802 0.8881 0.7641 -0.0211 0.0182  -0.0691 277 LYS A NZ  
2052 N N   . LYS A 277 ? 0.6523 0.8409 0.5908 -0.0576 0.0244  -0.0851 278 LYS A N   
2053 C CA  . LYS A 277 ? 0.6761 0.8817 0.6071 -0.0643 0.0274  -0.0883 278 LYS A CA  
2054 C C   . LYS A 277 ? 0.6962 0.9112 0.6165 -0.0705 0.0235  -0.0792 278 LYS A C   
2055 O O   . LYS A 277 ? 0.7038 0.9282 0.6173 -0.0751 0.0235  -0.0731 278 LYS A O   
2056 C CB  . LYS A 277 ? 0.7043 0.9187 0.6371 -0.0663 0.0319  -0.1036 278 LYS A CB  
2057 C CG  . LYS A 277 ? 0.7515 0.9554 0.6968 -0.0598 0.0348  -0.1133 278 LYS A CG  
2058 C CD  . LYS A 277 ? 0.7997 1.0118 0.7474 -0.0621 0.0388  -0.1287 278 LYS A CD  
2059 C CE  . LYS A 277 ? 0.8458 1.0606 0.7887 -0.0656 0.0362  -0.1305 278 LYS A CE  
2060 N NZ  . LYS A 277 ? 0.8735 1.0992 0.8172 -0.0694 0.0404  -0.1458 278 LYS A NZ  
2061 N N   . SER A 278 ? 0.7040 0.9164 0.6230 -0.0708 0.0199  -0.0777 279 SER A N   
2062 C CA  . SER A 278 ? 0.7210 0.9419 0.6309 -0.0763 0.0155  -0.0689 279 SER A CA  
2063 C C   . SER A 278 ? 0.7346 0.9477 0.6443 -0.0743 0.0108  -0.0535 279 SER A C   
2064 O O   . SER A 278 ? 0.7368 0.9510 0.6432 -0.0760 0.0061  -0.0455 279 SER A O   
2065 C CB  . SER A 278 ? 0.7417 0.9623 0.6516 -0.0768 0.0133  -0.0729 279 SER A CB  
2066 O OG  . SER A 278 ? 0.7734 0.9778 0.6909 -0.0702 0.0104  -0.0688 279 SER A OG  
2067 N N   . LEU A 279 ? 0.7408 0.9459 0.6550 -0.0705 0.0121  -0.0499 280 LEU A N   
2068 C CA  . LEU A 279 ? 0.7557 0.9529 0.6708 -0.0685 0.0081  -0.0365 280 LEU A CA  
2069 C C   . LEU A 279 ? 0.7729 0.9803 0.6815 -0.0741 0.0083  -0.0292 280 LEU A C   
2070 O O   . LEU A 279 ? 0.7768 0.9949 0.6821 -0.0778 0.0125  -0.0356 280 LEU A O   
2071 C CB  . LEU A 279 ? 0.7539 0.9345 0.6785 -0.0607 0.0089  -0.0366 280 LEU A CB  
2072 C CG  . LEU A 279 ? 0.7661 0.9347 0.6968 -0.0553 0.0067  -0.0380 280 LEU A CG  
2073 C CD1 . LEU A 279 ? 0.7731 0.9277 0.7123 -0.0485 0.0079  -0.0385 280 LEU A CD1 
2074 C CD2 . LEU A 279 ? 0.7704 0.9371 0.6992 -0.0558 0.0014  -0.0278 280 LEU A CD2 
2075 N N   . PRO A 280 ? 0.7786 0.9829 0.6861 -0.0746 0.0038  -0.0159 281 PRO A N   
2076 C CA  . PRO A 280 ? 0.7845 0.9981 0.6863 -0.0803 0.0035  -0.0079 281 PRO A CA  
2077 C C   . PRO A 280 ? 0.7910 1.0017 0.6959 -0.0790 0.0073  -0.0091 281 PRO A C   
2078 O O   . PRO A 280 ? 0.7980 1.0126 0.7000 -0.0828 0.0062  0.0000  281 PRO A O   
2079 C CB  . PRO A 280 ? 0.7934 1.0016 0.6957 -0.0801 -0.0027 0.0065  281 PRO A CB  
2080 C CG  . PRO A 280 ? 0.7964 0.9974 0.7024 -0.0759 -0.0055 0.0049  281 PRO A CG  
2081 C CD  . PRO A 280 ? 0.7735 0.9667 0.6851 -0.0706 -0.0013 -0.0075 281 PRO A CD  
2082 N N   . LYS A 281 ? 0.7854 0.9895 0.6967 -0.0740 0.0115  -0.0195 282 LYS A N   
2083 C CA  . LYS A 281 ? 0.7866 0.9881 0.7022 -0.0720 0.0154  -0.0226 282 LYS A CA  
2084 C C   . LYS A 281 ? 0.7842 0.9720 0.7055 -0.0678 0.0130  -0.0137 282 LYS A C   
2085 O O   . LYS A 281 ? 0.7891 0.9687 0.7170 -0.0630 0.0154  -0.0179 282 LYS A O   
2086 C CB  . LYS A 281 ? 0.8113 1.0292 0.7204 -0.0791 0.0189  -0.0242 282 LYS A CB  
2087 N N   . ASN A 282 ? 0.7716 0.9573 0.6907 -0.0697 0.0084  -0.0015 283 ASN A N   
2088 C CA  . ASN A 282 ? 0.7616 0.9341 0.6865 -0.0659 0.0058  0.0071  283 ASN A CA  
2089 C C   . ASN A 282 ? 0.7350 0.8977 0.6630 -0.0621 0.0011  0.0121  283 ASN A C   
2090 O O   . ASN A 282 ? 0.7387 0.8954 0.6689 -0.0617 -0.0027 0.0223  283 ASN A O   
2091 C CB  . ASN A 282 ? 0.7867 0.9651 0.7079 -0.0716 0.0044  0.0175  283 ASN A CB  
2092 C CG  . ASN A 282 ? 0.8389 1.0047 0.7664 -0.0686 0.0023  0.0255  283 ASN A CG  
2093 O OD1 . ASN A 282 ? 0.8560 1.0177 0.7844 -0.0694 -0.0022 0.0361  283 ASN A OD1 
2094 N ND2 . ASN A 282 ? 0.8493 1.0090 0.7820 -0.0652 0.0055  0.0204  283 ASN A ND2 
2095 N N   . HIS A 283 ? 0.7054 0.8670 0.6342 -0.0594 0.0013  0.0049  284 HIS A N   
2096 C CA  . HIS A 283 ? 0.6824 0.8366 0.6140 -0.0562 -0.0027 0.0084  284 HIS A CA  
2097 C C   . HIS A 283 ? 0.6553 0.7943 0.5949 -0.0501 -0.0043 0.0126  284 HIS A C   
2098 O O   . HIS A 283 ? 0.6517 0.7829 0.5963 -0.0456 -0.0017 0.0068  284 HIS A O   
2099 C CB  . HIS A 283 ? 0.6885 0.8442 0.6199 -0.0547 -0.0014 -0.0014 284 HIS A CB  
2100 C CG  . HIS A 283 ? 0.7111 0.8623 0.6444 -0.0526 -0.0055 0.0023  284 HIS A CG  
2101 N ND1 . HIS A 283 ? 0.7281 0.8710 0.6666 -0.0477 -0.0051 -0.0038 284 HIS A ND1 
2102 C CD2 . HIS A 283 ? 0.7255 0.8798 0.6567 -0.0550 -0.0102 0.0117  284 HIS A CD2 
2103 C CE1 . HIS A 283 ? 0.7349 0.8765 0.6740 -0.0472 -0.0092 0.0016  284 HIS A CE1 
2104 N NE2 . HIS A 283 ? 0.7367 0.8850 0.6719 -0.0513 -0.0124 0.0109  284 HIS A NE2 
2105 N N   . ASN A 284 ? 0.6340 0.7693 0.5753 -0.0501 -0.0087 0.0227  285 ASN A N   
2106 C CA  . ASN A 284 ? 0.6185 0.7402 0.5675 -0.0447 -0.0104 0.0269  285 ASN A CA  
2107 C C   . ASN A 284 ? 0.5862 0.7045 0.5382 -0.0430 -0.0151 0.0332  285 ASN A C   
2108 O O   . ASN A 284 ? 0.5873 0.6972 0.5453 -0.0404 -0.0175 0.0397  285 ASN A O   
2109 C CB  . ASN A 284 ? 0.6468 0.7658 0.5975 -0.0461 -0.0104 0.0333  285 ASN A CB  
2110 C CG  . ASN A 284 ? 0.7147 0.8316 0.6666 -0.0450 -0.0060 0.0267  285 ASN A CG  
2111 O OD1 . ASN A 284 ? 0.7364 0.8464 0.6923 -0.0402 -0.0040 0.0196  285 ASN A OD1 
2112 N ND2 . ASN A 284 ? 0.7348 0.8582 0.6835 -0.0495 -0.0046 0.0292  285 ASN A ND2 
2113 N N   . GLY A 285 ? 0.5551 0.6799 0.5037 -0.0444 -0.0162 0.0308  286 GLY A N   
2114 C CA  . GLY A 285 ? 0.5343 0.6576 0.4858 -0.0430 -0.0207 0.0364  286 GLY A CA  
2115 C C   . GLY A 285 ? 0.5064 0.6251 0.4612 -0.0388 -0.0203 0.0297  286 GLY A C   
2116 O O   . GLY A 285 ? 0.5047 0.6146 0.4637 -0.0344 -0.0176 0.0239  286 GLY A O   
2117 N N   . PHE A 286 ? 0.4799 0.6048 0.4328 -0.0405 -0.0231 0.0310  287 PHE A N   
2118 C CA  . PHE A 286 ? 0.4591 0.5805 0.4154 -0.0372 -0.0232 0.0257  287 PHE A CA  
2119 C C   . PHE A 286 ? 0.4288 0.5570 0.3800 -0.0396 -0.0206 0.0158  287 PHE A C   
2120 O O   . PHE A 286 ? 0.4325 0.5706 0.3768 -0.0446 -0.0193 0.0134  287 PHE A O   
2121 C CB  . PHE A 286 ? 0.4619 0.5852 0.4212 -0.0370 -0.0283 0.0332  287 PHE A CB  
2122 C CG  . PHE A 286 ? 0.4742 0.5875 0.4422 -0.0322 -0.0305 0.0397  287 PHE A CG  
2123 C CD1 . PHE A 286 ? 0.4824 0.5845 0.4564 -0.0268 -0.0280 0.0354  287 PHE A CD1 
2124 C CD2 . PHE A 286 ? 0.4885 0.6043 0.4596 -0.0330 -0.0353 0.0500  287 PHE A CD2 
2125 C CE1 . PHE A 286 ? 0.4897 0.5834 0.4720 -0.0226 -0.0297 0.0403  287 PHE A CE1 
2126 C CE2 . PHE A 286 ? 0.4971 0.6037 0.4777 -0.0282 -0.0372 0.0551  287 PHE A CE2 
2127 C CZ  . PHE A 286 ? 0.4918 0.5875 0.4778 -0.0232 -0.0341 0.0497  287 PHE A CZ  
2128 N N   . PHE A 287 ? 0.4000 0.5228 0.3551 -0.0362 -0.0199 0.0101  288 PHE A N   
2129 C CA  . PHE A 287 ? 0.3794 0.5068 0.3319 -0.0379 -0.0182 0.0011  288 PHE A CA  
2130 C C   . PHE A 287 ? 0.3551 0.4818 0.3109 -0.0367 -0.0214 0.0030  288 PHE A C   
2131 O O   . PHE A 287 ? 0.3475 0.4651 0.3099 -0.0320 -0.0224 0.0057  288 PHE A O   
2132 C CB  . PHE A 287 ? 0.3746 0.4942 0.3304 -0.0345 -0.0139 -0.0079 288 PHE A CB  
2133 C CG  . PHE A 287 ? 0.3802 0.5036 0.3325 -0.0366 -0.0101 -0.0130 288 PHE A CG  
2134 C CD1 . PHE A 287 ? 0.3889 0.5236 0.3351 -0.0417 -0.0088 -0.0183 288 PHE A CD1 
2135 C CD2 . PHE A 287 ? 0.3865 0.5031 0.3418 -0.0336 -0.0079 -0.0128 288 PHE A CD2 
2136 C CE1 . PHE A 287 ? 0.3948 0.5339 0.3385 -0.0435 -0.0049 -0.0237 288 PHE A CE1 
2137 C CE2 . PHE A 287 ? 0.3936 0.5144 0.3463 -0.0355 -0.0044 -0.0176 288 PHE A CE2 
2138 C CZ  . PHE A 287 ? 0.3894 0.5215 0.3367 -0.0403 -0.0028 -0.0232 288 PHE A CZ  
2139 N N   . LEU A 288 ? 0.3391 0.4760 0.2903 -0.0411 -0.0232 0.0017  289 LEU A N   
2140 C CA  . LEU A 288 ? 0.3249 0.4626 0.2792 -0.0405 -0.0264 0.0031  289 LEU A CA  
2141 C C   . LEU A 288 ? 0.3172 0.4552 0.2713 -0.0412 -0.0239 -0.0075 289 LEU A C   
2142 O O   . LEU A 288 ? 0.3171 0.4641 0.2654 -0.0459 -0.0228 -0.0131 289 LEU A O   
2143 C CB  . LEU A 288 ? 0.3284 0.4778 0.2785 -0.0451 -0.0309 0.0106  289 LEU A CB  
2144 C CG  . LEU A 288 ? 0.3520 0.5053 0.3046 -0.0456 -0.0346 0.0119  289 LEU A CG  
2145 C CD1 . LEU A 288 ? 0.3578 0.5008 0.3198 -0.0396 -0.0359 0.0156  289 LEU A CD1 
2146 C CD2 . LEU A 288 ? 0.3601 0.5257 0.3084 -0.0504 -0.0393 0.0201  289 LEU A CD2 
2147 N N   . VAL A 289 ? 0.3063 0.4345 0.2670 -0.0367 -0.0230 -0.0104 290 VAL A N   
2148 C CA  . VAL A 289 ? 0.2960 0.4227 0.2580 -0.0371 -0.0209 -0.0198 290 VAL A CA  
2149 C C   . VAL A 289 ? 0.2956 0.4253 0.2598 -0.0380 -0.0242 -0.0184 290 VAL A C   
2150 O O   . VAL A 289 ? 0.2918 0.4171 0.2611 -0.0347 -0.0264 -0.0125 290 VAL A O   
2151 C CB  . VAL A 289 ? 0.2943 0.4089 0.2620 -0.0322 -0.0176 -0.0240 290 VAL A CB  
2152 C CG1 . VAL A 289 ? 0.2992 0.4119 0.2689 -0.0328 -0.0156 -0.0334 290 VAL A CG1 
2153 C CG2 . VAL A 289 ? 0.2959 0.4082 0.2619 -0.0312 -0.0149 -0.0242 290 VAL A CG2 
2154 N N   . ARG A 290 ? 0.2996 0.4378 0.2601 -0.0427 -0.0245 -0.0241 291 ARG A N   
2155 C CA  . ARG A 290 ? 0.3122 0.4554 0.2741 -0.0446 -0.0278 -0.0232 291 ARG A CA  
2156 C C   . ARG A 290 ? 0.3111 0.4544 0.2736 -0.0468 -0.0258 -0.0338 291 ARG A C   
2157 O O   . ARG A 290 ? 0.3122 0.4588 0.2709 -0.0497 -0.0230 -0.0414 291 ARG A O   
2158 C CB  . ARG A 290 ? 0.3537 0.5106 0.3094 -0.0496 -0.0316 -0.0175 291 ARG A CB  
2159 C CG  . ARG A 290 ? 0.4516 0.6180 0.4059 -0.0541 -0.0345 -0.0197 291 ARG A CG  
2160 C CD  . ARG A 290 ? 0.5506 0.7314 0.4989 -0.0592 -0.0388 -0.0130 291 ARG A CD  
2161 N NE  . ARG A 290 ? 0.6376 0.8286 0.5767 -0.0650 -0.0372 -0.0175 291 ARG A NE  
2162 C CZ  . ARG A 290 ? 0.6990 0.8943 0.6330 -0.0665 -0.0373 -0.0122 291 ARG A CZ  
2163 N NH1 . ARG A 290 ? 0.6937 0.8830 0.6314 -0.0625 -0.0390 -0.0021 291 ARG A NH1 
2164 N NH2 . ARG A 290 ? 0.7176 0.9236 0.6432 -0.0723 -0.0354 -0.0171 291 ARG A NH2 
2165 N N   . MET A 291 ? 0.3054 0.4454 0.2734 -0.0457 -0.0271 -0.0344 292 MET A N   
2166 C CA  . MET A 291 ? 0.3182 0.4586 0.2875 -0.0485 -0.0258 -0.0438 292 MET A CA  
2167 C C   . MET A 291 ? 0.3310 0.4800 0.3002 -0.0519 -0.0298 -0.0418 292 MET A C   
2168 O O   . MET A 291 ? 0.3255 0.4734 0.2987 -0.0495 -0.0326 -0.0343 292 MET A O   
2169 C CB  . MET A 291 ? 0.3233 0.4508 0.2999 -0.0445 -0.0232 -0.0481 292 MET A CB  
2170 C CG  . MET A 291 ? 0.3474 0.4753 0.3259 -0.0478 -0.0219 -0.0581 292 MET A CG  
2171 S SD  . MET A 291 ? 0.4254 0.5400 0.4135 -0.0445 -0.0204 -0.0611 292 MET A SD  
2172 C CE  . MET A 291 ? 0.4008 0.5067 0.3907 -0.0413 -0.0163 -0.0656 292 MET A CE  
2173 N N   . ARG A 292 ? 0.3471 0.5055 0.3119 -0.0577 -0.0300 -0.0485 293 ARG A N   
2174 C CA  . ARG A 292 ? 0.3753 0.5430 0.3397 -0.0617 -0.0339 -0.0472 293 ARG A CA  
2175 C C   . ARG A 292 ? 0.3977 0.5672 0.3629 -0.0659 -0.0326 -0.0581 293 ARG A C   
2176 O O   . ARG A 292 ? 0.3979 0.5645 0.3624 -0.0669 -0.0289 -0.0673 293 ARG A O   
2177 C CB  . ARG A 292 ? 0.3981 0.5800 0.3550 -0.0659 -0.0374 -0.0412 293 ARG A CB  
2178 C CG  . ARG A 292 ? 0.4499 0.6411 0.3983 -0.0714 -0.0353 -0.0484 293 ARG A CG  
2179 C CD  . ARG A 292 ? 0.5112 0.7195 0.4526 -0.0783 -0.0394 -0.0460 293 ARG A CD  
2180 N NE  . ARG A 292 ? 0.5681 0.7806 0.5099 -0.0769 -0.0443 -0.0326 293 ARG A NE  
2181 C CZ  . ARG A 292 ? 0.6073 0.8227 0.5451 -0.0764 -0.0453 -0.0245 293 ARG A CZ  
2182 N NH1 . ARG A 292 ? 0.6090 0.8251 0.5411 -0.0778 -0.0417 -0.0286 293 ARG A NH1 
2183 N NH2 . ARG A 292 ? 0.6046 0.8225 0.5447 -0.0747 -0.0500 -0.0123 293 ARG A NH2 
2184 N N   . ASN A 293 ? 0.4175 0.5919 0.3852 -0.0684 -0.0358 -0.0572 294 ASN A N   
2185 C CA  . ASN A 293 ? 0.4424 0.6195 0.4110 -0.0731 -0.0352 -0.0673 294 ASN A CA  
2186 C C   . ASN A 293 ? 0.4611 0.6519 0.4210 -0.0799 -0.0352 -0.0734 294 ASN A C   
2187 O O   . ASN A 293 ? 0.4604 0.6623 0.4136 -0.0822 -0.0379 -0.0671 294 ASN A O   
2188 C CB  . ASN A 293 ? 0.4725 0.6537 0.4453 -0.0745 -0.0392 -0.0635 294 ASN A CB  
2189 C CG  . ASN A 293 ? 0.5412 0.7099 0.5234 -0.0701 -0.0382 -0.0624 294 ASN A CG  
2190 O OD1 . ASN A 293 ? 0.5677 0.7316 0.5544 -0.0718 -0.0368 -0.0699 294 ASN A OD1 
2191 N ND2 . ASN A 293 ? 0.5477 0.7113 0.5334 -0.0645 -0.0392 -0.0530 294 ASN A ND2 
2192 N N   . ALA A 294 ? 0.4819 0.6723 0.4420 -0.0833 -0.0322 -0.0857 295 ALA A N   
2193 C CA  . ALA A 294 ? 0.5103 0.7146 0.4625 -0.0905 -0.0318 -0.0936 295 ALA A CA  
2194 C C   . ALA A 294 ? 0.5423 0.7560 0.4947 -0.0963 -0.0352 -0.0965 295 ALA A C   
2195 O O   . ALA A 294 ? 0.5455 0.7523 0.5054 -0.0945 -0.0366 -0.0950 295 ALA A O   
2196 C CB  . ALA A 294 ? 0.5129 0.7118 0.4667 -0.0909 -0.0263 -0.1066 295 ALA A CB  
2197 N N   . ILE A 295 ? 0.5632 0.7934 0.5072 -0.1038 -0.0366 -0.1007 296 ILE A N   
2198 C CA  . ILE A 295 ? 0.5840 0.8242 0.5275 -0.1100 -0.0398 -0.1042 296 ILE A CA  
2199 C C   . ILE A 295 ? 0.5992 0.8331 0.5483 -0.1123 -0.0363 -0.1189 296 ILE A C   
2200 O O   . ILE A 295 ? 0.6081 0.8362 0.5647 -0.1120 -0.0376 -0.1199 296 ILE A O   
2201 C CB  . ILE A 295 ? 0.5969 0.8581 0.5294 -0.1177 -0.0429 -0.1034 296 ILE A CB  
2202 C CG1 . ILE A 295 ? 0.6067 0.8737 0.5339 -0.1156 -0.0462 -0.0887 296 ILE A CG1 
2203 C CG2 . ILE A 295 ? 0.6062 0.8777 0.5392 -0.1237 -0.0470 -0.1053 296 ILE A CG2 
2204 C CD1 . ILE A 295 ? 0.6228 0.9108 0.5385 -0.1235 -0.0493 -0.0869 296 ILE A CD1 
2205 N N   . GLY A 303 ? 0.4538 0.6053 0.4546 -0.0901 -0.0260 -0.1275 304 GLY A N   
2206 C CA  . GLY A 303 ? 0.4522 0.5942 0.4541 -0.0829 -0.0246 -0.1193 304 GLY A CA  
2207 C C   . GLY A 303 ? 0.4548 0.5967 0.4527 -0.0812 -0.0212 -0.1237 304 GLY A C   
2208 O O   . GLY A 303 ? 0.4719 0.6068 0.4747 -0.0809 -0.0178 -0.1331 304 GLY A O   
2209 N N   . LYS A 304 ? 0.4340 0.5839 0.4236 -0.0802 -0.0221 -0.1169 305 LYS A N   
2210 C CA  . LYS A 304 ? 0.4154 0.5671 0.4000 -0.0788 -0.0191 -0.1194 305 LYS A CA  
2211 C C   . LYS A 304 ? 0.3800 0.5352 0.3589 -0.0755 -0.0211 -0.1068 305 LYS A C   
2212 O O   . LYS A 304 ? 0.3689 0.5306 0.3452 -0.0766 -0.0251 -0.0988 305 LYS A O   
2213 C CB  . LYS A 304 ? 0.4529 0.6179 0.4311 -0.0856 -0.0180 -0.1299 305 LYS A CB  
2214 C CG  . LYS A 304 ? 0.5132 0.6748 0.4931 -0.0850 -0.0129 -0.1409 305 LYS A CG  
2215 C CD  . LYS A 304 ? 0.5797 0.7388 0.5663 -0.0886 -0.0109 -0.1549 305 LYS A CD  
2216 C CE  . LYS A 304 ? 0.6345 0.8081 0.6156 -0.0967 -0.0130 -0.1606 305 LYS A CE  
2217 N NZ  . LYS A 304 ? 0.6645 0.8346 0.6531 -0.1003 -0.0110 -0.1746 305 LYS A NZ  
2218 N N   . PHE A 305 ? 0.3626 0.5124 0.3408 -0.0712 -0.0185 -0.1049 306 PHE A N   
2219 C CA  . PHE A 305 ? 0.3496 0.5004 0.3237 -0.0677 -0.0201 -0.0932 306 PHE A CA  
2220 C C   . PHE A 305 ? 0.3397 0.4956 0.3075 -0.0680 -0.0178 -0.0946 306 PHE A C   
2221 O O   . PHE A 305 ? 0.3394 0.4925 0.3087 -0.0681 -0.0139 -0.1037 306 PHE A O   
2222 C CB  . PHE A 305 ? 0.3409 0.4774 0.3223 -0.0608 -0.0198 -0.0866 306 PHE A CB  
2223 C CG  . PHE A 305 ? 0.3373 0.4701 0.3243 -0.0602 -0.0224 -0.0825 306 PHE A CG  
2224 C CD1 . PHE A 305 ? 0.3453 0.4705 0.3396 -0.0607 -0.0214 -0.0886 306 PHE A CD1 
2225 C CD2 . PHE A 305 ? 0.3369 0.4742 0.3226 -0.0593 -0.0260 -0.0726 306 PHE A CD2 
2226 C CE1 . PHE A 305 ? 0.3483 0.4712 0.3476 -0.0608 -0.0237 -0.0848 306 PHE A CE1 
2227 C CE2 . PHE A 305 ? 0.3441 0.4792 0.3353 -0.0589 -0.0282 -0.0693 306 PHE A CE2 
2228 C CZ  . PHE A 305 ? 0.3426 0.4708 0.3402 -0.0598 -0.0270 -0.0754 306 PHE A CZ  
2229 N N   . LEU A 306 ? 0.3337 0.4972 0.2949 -0.0683 -0.0201 -0.0855 307 LEU A N   
2230 C CA  . LEU A 306 ? 0.3348 0.5036 0.2897 -0.0689 -0.0180 -0.0853 307 LEU A CA  
2231 C C   . LEU A 306 ? 0.3202 0.4807 0.2768 -0.0629 -0.0184 -0.0750 307 LEU A C   
2232 O O   . LEU A 306 ? 0.3146 0.4742 0.2722 -0.0610 -0.0219 -0.0653 307 LEU A O   
2233 C CB  . LEU A 306 ? 0.3442 0.5304 0.2891 -0.0755 -0.0204 -0.0835 307 LEU A CB  
2234 C CG  . LEU A 306 ? 0.3658 0.5638 0.3057 -0.0826 -0.0186 -0.0957 307 LEU A CG  
2235 C CD1 . LEU A 306 ? 0.3751 0.5696 0.3167 -0.0819 -0.0130 -0.1065 307 LEU A CD1 
2236 C CD2 . LEU A 306 ? 0.3728 0.5717 0.3163 -0.0855 -0.0202 -0.1013 307 LEU A CD2 
2237 N N   . VAL A 307 ? 0.3122 0.4667 0.2699 -0.0599 -0.0147 -0.0776 308 VAL A N   
2238 C CA  . VAL A 307 ? 0.3063 0.4532 0.2655 -0.0546 -0.0145 -0.0692 308 VAL A CA  
2239 C C   . VAL A 307 ? 0.3077 0.4631 0.2596 -0.0569 -0.0133 -0.0678 308 VAL A C   
2240 O O   . VAL A 307 ? 0.3056 0.4653 0.2554 -0.0594 -0.0099 -0.0766 308 VAL A O   
2241 C CB  . VAL A 307 ? 0.3035 0.4363 0.2707 -0.0492 -0.0113 -0.0731 308 VAL A CB  
2242 C CG1 . VAL A 307 ? 0.3042 0.4300 0.2725 -0.0442 -0.0109 -0.0653 308 VAL A CG1 
2243 C CG2 . VAL A 307 ? 0.3026 0.4275 0.2769 -0.0477 -0.0124 -0.0746 308 VAL A CG2 
2244 N N   . SER A 308 ? 0.3130 0.4707 0.2617 -0.0561 -0.0159 -0.0569 309 SER A N   
2245 C CA  . SER A 308 ? 0.3298 0.4951 0.2718 -0.0584 -0.0150 -0.0542 309 SER A CA  
2246 C C   . SER A 308 ? 0.3388 0.4956 0.2833 -0.0534 -0.0151 -0.0455 309 SER A C   
2247 O O   . SER A 308 ? 0.3417 0.4904 0.2911 -0.0493 -0.0173 -0.0389 309 SER A O   
2248 C CB  . SER A 308 ? 0.3574 0.5376 0.2915 -0.0645 -0.0186 -0.0491 309 SER A CB  
2249 O OG  . SER A 308 ? 0.4026 0.5813 0.3391 -0.0630 -0.0234 -0.0396 309 SER A OG  
2250 N N   . VAL A 309 ? 0.3408 0.4997 0.2821 -0.0540 -0.0124 -0.0462 310 VAL A N   
2251 C CA  . VAL A 309 ? 0.3550 0.5070 0.2981 -0.0501 -0.0124 -0.0383 310 VAL A CA  
2252 C C   . VAL A 309 ? 0.3749 0.5383 0.3103 -0.0549 -0.0135 -0.0327 310 VAL A C   
2253 O O   . VAL A 309 ? 0.3822 0.5541 0.3126 -0.0588 -0.0106 -0.0387 310 VAL A O   
2254 C CB  . VAL A 309 ? 0.3613 0.5039 0.3091 -0.0460 -0.0081 -0.0438 310 VAL A CB  
2255 C CG1 . VAL A 309 ? 0.3686 0.5061 0.3173 -0.0431 -0.0084 -0.0356 310 VAL A CG1 
2256 C CG2 . VAL A 309 ? 0.3642 0.4956 0.3199 -0.0415 -0.0073 -0.0484 310 VAL A CG2 
2257 N N   . LYS A 310 ? 0.3822 0.5466 0.3169 -0.0549 -0.0176 -0.0214 311 LYS A N   
2258 C CA  . LYS A 310 ? 0.3983 0.5738 0.3260 -0.0598 -0.0196 -0.0142 311 LYS A CA  
2259 C C   . LYS A 310 ? 0.4129 0.5827 0.3419 -0.0575 -0.0193 -0.0067 311 LYS A C   
2260 O O   . LYS A 310 ? 0.4161 0.5771 0.3506 -0.0533 -0.0218 0.0010  311 LYS A O   
2261 C CB  . LYS A 310 ? 0.4249 0.6075 0.3508 -0.0625 -0.0251 -0.0063 311 LYS A CB  
2262 C CG  . LYS A 310 ? 0.4961 0.6917 0.4146 -0.0685 -0.0279 0.0020  311 LYS A CG  
2263 C CD  . LYS A 310 ? 0.5765 0.7800 0.4939 -0.0712 -0.0338 0.0094  311 LYS A CD  
2264 C CE  . LYS A 310 ? 0.6385 0.8567 0.5479 -0.0780 -0.0370 0.0180  311 LYS A CE  
2265 N NZ  . LYS A 310 ? 0.6698 0.8941 0.5802 -0.0796 -0.0435 0.0275  311 LYS A NZ  
2266 N N   . PRO A 311 ? 0.4209 0.5964 0.3452 -0.0605 -0.0161 -0.0092 312 PRO A N   
2267 C CA  . PRO A 311 ? 0.4317 0.6025 0.3573 -0.0590 -0.0158 -0.0021 312 PRO A CA  
2268 C C   . PRO A 311 ? 0.4542 0.6308 0.3769 -0.0622 -0.0206 0.0108  312 PRO A C   
2269 O O   . PRO A 311 ? 0.4592 0.6482 0.3757 -0.0677 -0.0231 0.0134  312 PRO A O   
2270 C CB  . PRO A 311 ? 0.4339 0.6115 0.3550 -0.0621 -0.0109 -0.0094 312 PRO A CB  
2271 C CG  . PRO A 311 ? 0.4346 0.6178 0.3539 -0.0639 -0.0083 -0.0215 312 PRO A CG  
2272 C CD  . PRO A 311 ? 0.4143 0.6010 0.3325 -0.0655 -0.0124 -0.0191 312 PRO A CD  
2273 N N   . PHE A 312 ? 0.4675 0.6350 0.3951 -0.0588 -0.0221 0.0191  313 PHE A N   
2274 C CA  . PHE A 312 ? 0.4877 0.6587 0.4147 -0.0612 -0.0268 0.0321  313 PHE A CA  
2275 C C   . PHE A 312 ? 0.5255 0.6908 0.4542 -0.0603 -0.0254 0.0368  313 PHE A C   
2276 O O   . PHE A 312 ? 0.5302 0.6840 0.4647 -0.0551 -0.0226 0.0327  313 PHE A O   
2277 C CB  . PHE A 312 ? 0.4759 0.6391 0.4105 -0.0567 -0.0313 0.0387  313 PHE A CB  
2278 C CG  . PHE A 312 ? 0.4716 0.6431 0.4042 -0.0590 -0.0347 0.0390  313 PHE A CG  
2279 C CD1 . PHE A 312 ? 0.4746 0.6576 0.4029 -0.0643 -0.0394 0.0482  313 PHE A CD1 
2280 C CD2 . PHE A 312 ? 0.4730 0.6409 0.4084 -0.0561 -0.0335 0.0308  313 PHE A CD2 
2281 C CE1 . PHE A 312 ? 0.4796 0.6709 0.4063 -0.0666 -0.0428 0.0487  313 PHE A CE1 
2282 C CE2 . PHE A 312 ? 0.4775 0.6533 0.4114 -0.0585 -0.0368 0.0310  313 PHE A CE2 
2283 C CZ  . PHE A 312 ? 0.4740 0.6616 0.4035 -0.0637 -0.0414 0.0397  313 PHE A CZ  
2284 N N   . ARG A 313 ? 0.5489 0.7225 0.4730 -0.0657 -0.0275 0.0456  314 ARG A N   
2285 C CA  . ARG A 313 ? 0.5774 0.7458 0.5039 -0.0654 -0.0267 0.0513  314 ARG A CA  
2286 C C   . ARG A 313 ? 0.5992 0.7548 0.5353 -0.0601 -0.0305 0.0598  314 ARG A C   
2287 O O   . ARG A 313 ? 0.5993 0.7544 0.5387 -0.0586 -0.0346 0.0640  314 ARG A O   
2288 C CB  . ARG A 313 ? 0.6054 0.7872 0.5240 -0.0733 -0.0279 0.0586  314 ARG A CB  
2289 C CG  . ARG A 313 ? 0.6597 0.8555 0.5688 -0.0788 -0.0237 0.0492  314 ARG A CG  
2290 C CD  . ARG A 313 ? 0.7203 0.9282 0.6221 -0.0864 -0.0233 0.0550  314 ARG A CD  
2291 N NE  . ARG A 313 ? 0.7755 0.9953 0.6718 -0.0926 -0.0286 0.0657  314 ARG A NE  
2292 C CZ  . ARG A 313 ? 0.8169 1.0394 0.7127 -0.0964 -0.0322 0.0790  314 ARG A CZ  
2293 N NH1 . ARG A 313 ? 0.8179 1.0312 0.7186 -0.0946 -0.0311 0.0830  314 ARG A NH1 
2294 N NH2 . ARG A 313 ? 0.8141 1.0482 0.7049 -0.1022 -0.0374 0.0889  314 ARG A NH2 
2295 N N   . LYS A 314 ? 0.6175 0.7631 0.5588 -0.0573 -0.0292 0.0621  315 LYS A N   
2296 C CA  . LYS A 314 ? 0.6426 0.7759 0.5940 -0.0523 -0.0323 0.0690  315 LYS A CA  
2297 C C   . LYS A 314 ? 0.6643 0.8016 0.6174 -0.0550 -0.0384 0.0821  315 LYS A C   
2298 O O   . LYS A 314 ? 0.6647 0.7947 0.6263 -0.0507 -0.0418 0.0866  315 LYS A O   
2299 C CB  . LYS A 314 ? 0.6755 0.7990 0.6313 -0.0501 -0.0298 0.0690  315 LYS A CB  
2300 C CG  . LYS A 314 ? 0.7435 0.8524 0.7097 -0.0430 -0.0302 0.0684  315 LYS A CG  
2301 C CD  . LYS A 314 ? 0.8207 0.9217 0.7933 -0.0424 -0.0315 0.0758  315 LYS A CD  
2302 C CE  . LYS A 314 ? 0.8824 0.9863 0.8576 -0.0451 -0.0372 0.0884  315 LYS A CE  
2303 N NZ  . LYS A 314 ? 0.9171 1.0140 0.8983 -0.0457 -0.0384 0.0960  315 LYS A NZ  
2304 N N   . LYS A 315 ? 0.6799 0.8296 0.6254 -0.0622 -0.0398 0.0882  316 LYS A N   
2305 C CA  . LYS A 315 ? 0.7004 0.8556 0.6469 -0.0656 -0.0461 0.1017  316 LYS A CA  
2306 C C   . LYS A 315 ? 0.7124 0.8743 0.6582 -0.0656 -0.0498 0.1024  316 LYS A C   
2307 O O   . LYS A 315 ? 0.7196 0.8814 0.6709 -0.0652 -0.0555 0.1129  316 LYS A O   
2308 C CB  . LYS A 315 ? 0.7337 0.9017 0.6711 -0.0742 -0.0464 0.1079  316 LYS A CB  
2309 C CG  . LYS A 315 ? 0.7921 0.9556 0.7292 -0.0750 -0.0421 0.1059  316 LYS A CG  
2310 C CD  . LYS A 315 ? 0.8512 1.0223 0.7847 -0.0822 -0.0446 0.1178  316 LYS A CD  
2311 C CE  . LYS A 315 ? 0.8960 1.0584 0.8333 -0.0815 -0.0417 0.1181  316 LYS A CE  
2312 N NZ  . LYS A 315 ? 0.9257 1.0907 0.8641 -0.0869 -0.0456 0.1325  316 LYS A NZ  
2313 N N   . GLU A 316 ? 0.7132 0.8806 0.6531 -0.0659 -0.0466 0.0912  317 GLU A N   
2314 C CA  . GLU A 316 ? 0.7166 0.8908 0.6552 -0.0663 -0.0495 0.0901  317 GLU A CA  
2315 C C   . GLU A 316 ? 0.7103 0.8727 0.6584 -0.0585 -0.0495 0.0855  317 GLU A C   
2316 O O   . GLU A 316 ? 0.7090 0.8758 0.6556 -0.0583 -0.0499 0.0802  317 GLU A O   
2317 C CB  . GLU A 316 ? 0.7538 0.9407 0.6814 -0.0713 -0.0461 0.0800  317 GLU A CB  
2318 C CG  . GLU A 316 ? 0.8335 1.0335 0.7509 -0.0793 -0.0449 0.0823  317 GLU A CG  
2319 C CD  . GLU A 316 ? 0.9269 1.1366 0.8351 -0.0830 -0.0396 0.0693  317 GLU A CD  
2320 O OE1 . GLU A 316 ? 0.9408 1.1492 0.8497 -0.0805 -0.0380 0.0595  317 GLU A OE1 
2321 O OE2 . GLU A 316 ? 0.9595 1.1783 0.8604 -0.0886 -0.0371 0.0688  317 GLU A OE2 
2322 N N   . SER A 317 ? 0.7075 0.8556 0.6653 -0.0525 -0.0490 0.0873  318 SER A N   
2323 C CA  . SER A 317 ? 0.7129 0.8502 0.6798 -0.0453 -0.0486 0.0827  318 SER A CA  
2324 C C   . SER A 317 ? 0.7162 0.8566 0.6887 -0.0440 -0.0540 0.0888  318 SER A C   
2325 O O   . SER A 317 ? 0.7161 0.8539 0.6919 -0.0404 -0.0533 0.0827  318 SER A O   
2326 C CB  . SER A 317 ? 0.7301 0.8530 0.7058 -0.0400 -0.0469 0.0834  318 SER A CB  
2327 O OG  . SER A 317 ? 0.7571 0.8753 0.7294 -0.0392 -0.0413 0.0741  318 SER A OG  
2328 N N   . GLU A 318 ? 0.7159 0.8623 0.6898 -0.0471 -0.0594 0.1009  319 GLU A N   
2329 C CA  . GLU A 318 ? 0.7180 0.8687 0.6977 -0.0461 -0.0651 0.1078  319 GLU A CA  
2330 C C   . GLU A 318 ? 0.7066 0.8706 0.6776 -0.0504 -0.0657 0.1031  319 GLU A C   
2331 O O   . GLU A 318 ? 0.7065 0.8717 0.6821 -0.0480 -0.0679 0.1021  319 GLU A O   
2332 C CB  . GLU A 318 ? 0.7604 0.9145 0.7440 -0.0487 -0.0711 0.1229  319 GLU A CB  
2333 C CG  . GLU A 318 ? 0.8384 0.9785 0.8364 -0.0424 -0.0727 0.1285  319 GLU A CG  
2334 C CD  . GLU A 318 ? 0.9459 1.0808 0.9551 -0.0359 -0.0742 0.1265  319 GLU A CD  
2335 O OE1 . GLU A 318 ? 0.9682 1.0920 0.9828 -0.0302 -0.0700 0.1181  319 GLU A OE1 
2336 O OE2 . GLU A 318 ? 0.9819 1.1246 0.9944 -0.0367 -0.0795 0.1333  319 GLU A OE2 
2337 N N   . GLN A 319 ? 0.6962 0.8705 0.6549 -0.0570 -0.0636 0.0999  320 GLN A N   
2338 C CA  . GLN A 319 ? 0.6892 0.8767 0.6384 -0.0620 -0.0633 0.0937  320 GLN A CA  
2339 C C   . GLN A 319 ? 0.6719 0.8532 0.6221 -0.0581 -0.0585 0.0798  320 GLN A C   
2340 O O   . GLN A 319 ? 0.6725 0.8605 0.6206 -0.0595 -0.0595 0.0755  320 GLN A O   
2341 C CB  . GLN A 319 ? 0.7131 0.9119 0.6498 -0.0696 -0.0610 0.0922  320 GLN A CB  
2342 C CG  . GLN A 319 ? 0.7624 0.9700 0.6967 -0.0750 -0.0661 0.1063  320 GLN A CG  
2343 C CD  . GLN A 319 ? 0.8122 1.0118 0.7492 -0.0744 -0.0650 0.1124  320 GLN A CD  
2344 O OE1 . GLN A 319 ? 0.8294 1.0149 0.7774 -0.0681 -0.0656 0.1159  320 GLN A OE1 
2345 N NE2 . GLN A 319 ? 0.8158 1.0251 0.7430 -0.0812 -0.0635 0.1139  320 GLN A NE2 
2346 N N   . ALA A 320 ? 0.6528 0.8215 0.6061 -0.0535 -0.0535 0.0732  321 ALA A N   
2347 C CA  . ALA A 320 ? 0.6377 0.7989 0.5927 -0.0494 -0.0489 0.0612  321 ALA A CA  
2348 C C   . ALA A 320 ? 0.6237 0.7784 0.5885 -0.0439 -0.0512 0.0622  321 ALA A C   
2349 O O   . ALA A 320 ? 0.6190 0.7746 0.5838 -0.0432 -0.0500 0.0547  321 ALA A O   
2350 C CB  . ALA A 320 ? 0.6370 0.7874 0.5933 -0.0462 -0.0439 0.0563  321 ALA A CB  
2351 N N   . LEU A 321 ? 0.6148 0.7633 0.5886 -0.0402 -0.0544 0.0712  322 LEU A N   
2352 C CA  . LEU A 321 ? 0.6124 0.7553 0.5968 -0.0348 -0.0565 0.0727  322 LEU A CA  
2353 C C   . LEU A 321 ? 0.6086 0.7630 0.5928 -0.0376 -0.0614 0.0766  322 LEU A C   
2354 O O   . LEU A 321 ? 0.6072 0.7609 0.5961 -0.0349 -0.0616 0.0727  322 LEU A O   
2355 C CB  . LEU A 321 ? 0.6175 0.7514 0.6121 -0.0305 -0.0585 0.0810  322 LEU A CB  
2356 C CG  . LEU A 321 ? 0.6399 0.7691 0.6470 -0.0248 -0.0610 0.0836  322 LEU A CG  
2357 C CD1 . LEU A 321 ? 0.6496 0.7711 0.6596 -0.0204 -0.0565 0.0732  322 LEU A CD1 
2358 C CD2 . LEU A 321 ? 0.6493 0.7711 0.6666 -0.0214 -0.0634 0.0922  322 LEU A CD2 
2359 N N   . GLN A 322 ? 0.6068 0.7728 0.5852 -0.0433 -0.0653 0.0842  323 GLN A N   
2360 C CA  . GLN A 322 ? 0.6105 0.7893 0.5875 -0.0470 -0.0704 0.0885  323 GLN A CA  
2361 C C   . GLN A 322 ? 0.5994 0.7844 0.5689 -0.0500 -0.0675 0.0770  323 GLN A C   
2362 O O   . GLN A 322 ? 0.5979 0.7865 0.5708 -0.0493 -0.0696 0.0755  323 GLN A O   
2363 C CB  . GLN A 322 ? 0.6484 0.8389 0.6194 -0.0534 -0.0749 0.0992  323 GLN A CB  
2364 C CG  . GLN A 322 ? 0.7208 0.9280 0.6862 -0.0593 -0.0796 0.1023  323 GLN A CG  
2365 C CD  . GLN A 322 ? 0.8100 1.0196 0.7861 -0.0566 -0.0861 0.1117  323 GLN A CD  
2366 O OE1 . GLN A 322 ? 0.8389 1.0384 0.8265 -0.0497 -0.0858 0.1105  323 GLN A OE1 
2367 N NE2 . GLN A 322 ? 0.8198 1.0437 0.7924 -0.0623 -0.0921 0.1214  323 GLN A NE2 
2368 N N   . GLU A 323 ? 0.5866 0.7723 0.5469 -0.0530 -0.0626 0.0686  324 GLU A N   
2369 C CA  . GLU A 323 ? 0.5774 0.7678 0.5311 -0.0559 -0.0593 0.0568  324 GLU A CA  
2370 C C   . GLU A 323 ? 0.5534 0.7325 0.5141 -0.0501 -0.0562 0.0484  324 GLU A C   
2371 O O   . GLU A 323 ? 0.5453 0.7283 0.5044 -0.0517 -0.0556 0.0414  324 GLU A O   
2372 C CB  . GLU A 323 ? 0.6189 0.8128 0.5624 -0.0603 -0.0549 0.0504  324 GLU A CB  
2373 C CG  . GLU A 323 ? 0.7176 0.9151 0.6556 -0.0629 -0.0509 0.0371  324 GLU A CG  
2374 C CD  . GLU A 323 ? 0.8368 1.0511 0.7658 -0.0707 -0.0528 0.0349  324 GLU A CD  
2375 O OE1 . GLU A 323 ? 0.8794 1.1046 0.8009 -0.0762 -0.0543 0.0400  324 GLU A OE1 
2376 O OE2 . GLU A 323 ? 0.8599 1.0769 0.7891 -0.0716 -0.0526 0.0276  324 GLU A OE2 
2377 N N   . LEU A 324 ? 0.5398 0.7055 0.5085 -0.0437 -0.0545 0.0498  325 LEU A N   
2378 C CA  . LEU A 324 ? 0.5315 0.6867 0.5073 -0.0382 -0.0516 0.0434  325 LEU A CA  
2379 C C   . LEU A 324 ? 0.5300 0.6875 0.5135 -0.0361 -0.0556 0.0471  325 LEU A C   
2380 O O   . LEU A 324 ? 0.5223 0.6784 0.5080 -0.0351 -0.0541 0.0405  325 LEU A O   
2381 C CB  . LEU A 324 ? 0.5281 0.6702 0.5094 -0.0327 -0.0490 0.0445  325 LEU A CB  
2382 C CG  . LEU A 324 ? 0.5401 0.6715 0.5291 -0.0270 -0.0464 0.0395  325 LEU A CG  
2383 C CD1 . LEU A 324 ? 0.5492 0.6784 0.5341 -0.0277 -0.0420 0.0288  325 LEU A CD1 
2384 C CD2 . LEU A 324 ? 0.5439 0.6645 0.5387 -0.0222 -0.0448 0.0422  325 LEU A CD2 
2385 N N   . ASN A 325 ? 0.5366 0.6980 0.5250 -0.0357 -0.0606 0.0579  326 ASN A N   
2386 C CA  . ASN A 325 ? 0.5464 0.7113 0.5434 -0.0336 -0.0648 0.0624  326 ASN A CA  
2387 C C   . ASN A 325 ? 0.5443 0.7225 0.5362 -0.0390 -0.0676 0.0607  326 ASN A C   
2388 O O   . ASN A 325 ? 0.5413 0.7215 0.5393 -0.0374 -0.0693 0.0598  326 ASN A O   
2389 C CB  . ASN A 325 ? 0.5728 0.7372 0.5782 -0.0310 -0.0695 0.0744  326 ASN A CB  
2390 C CG  . ASN A 325 ? 0.6287 0.7797 0.6450 -0.0237 -0.0673 0.0742  326 ASN A CG  
2391 O OD1 . ASN A 325 ? 0.6464 0.7898 0.6643 -0.0218 -0.0660 0.0770  326 ASN A OD1 
2392 N ND2 . ASN A 325 ? 0.6411 0.7895 0.6650 -0.0199 -0.0666 0.0703  326 ASN A ND2 
2393 N N   . LYS A 326 ? 0.5475 0.7352 0.5283 -0.0455 -0.0679 0.0596  327 LYS A N   
2394 C CA  . LYS A 326 ? 0.5576 0.7587 0.5320 -0.0516 -0.0700 0.0565  327 LYS A CA  
2395 C C   . LYS A 326 ? 0.5633 0.7603 0.5365 -0.0514 -0.0654 0.0436  327 LYS A C   
2396 O O   . LYS A 326 ? 0.5643 0.7675 0.5385 -0.0534 -0.0672 0.0408  327 LYS A O   
2397 C CB  . LYS A 326 ? 0.5879 0.8003 0.5503 -0.0589 -0.0706 0.0576  327 LYS A CB  
2398 C CG  . LYS A 326 ? 0.6500 0.8713 0.6126 -0.0613 -0.0768 0.0714  327 LYS A CG  
2399 C CD  . LYS A 326 ? 0.7140 0.9471 0.6640 -0.0690 -0.0771 0.0728  327 LYS A CD  
2400 C CE  . LYS A 326 ? 0.7597 0.9846 0.7055 -0.0682 -0.0718 0.0694  327 LYS A CE  
2401 N NZ  . LYS A 326 ? 0.7870 1.0232 0.7235 -0.0749 -0.0735 0.0758  327 LYS A NZ  
2402 N N   . ASP A 327 ? 0.5629 0.7492 0.5342 -0.0492 -0.0597 0.0362  328 ASP A N   
2403 C CA  . ASP A 327 ? 0.5684 0.7490 0.5396 -0.0485 -0.0552 0.0247  328 ASP A CA  
2404 C C   . ASP A 327 ? 0.5580 0.7299 0.5397 -0.0428 -0.0549 0.0245  328 ASP A C   
2405 O O   . ASP A 327 ? 0.5550 0.7265 0.5381 -0.0435 -0.0537 0.0177  328 ASP A O   
2406 C CB  . ASP A 327 ? 0.6018 0.7748 0.5684 -0.0480 -0.0497 0.0178  328 ASP A CB  
2407 C CG  . ASP A 327 ? 0.6823 0.8651 0.6385 -0.0541 -0.0492 0.0165  328 ASP A CG  
2408 O OD1 . ASP A 327 ? 0.6947 0.8907 0.6457 -0.0598 -0.0523 0.0171  328 ASP A OD1 
2409 O OD2 . ASP A 327 ? 0.7138 0.8918 0.6670 -0.0534 -0.0458 0.0147  328 ASP A OD2 
2410 N N   . ASP A 328 ? 0.5515 0.7171 0.5408 -0.0376 -0.0562 0.0319  329 ASP A N   
2411 C CA  . ASP A 328 ? 0.5500 0.7088 0.5495 -0.0323 -0.0559 0.0321  329 ASP A CA  
2412 C C   . ASP A 328 ? 0.5460 0.7146 0.5500 -0.0338 -0.0604 0.0350  329 ASP A C   
2413 O O   . ASP A 328 ? 0.5420 0.7084 0.5514 -0.0321 -0.0594 0.0312  329 ASP A O   
2414 C CB  . ASP A 328 ? 0.5681 0.7190 0.5750 -0.0267 -0.0562 0.0389  329 ASP A CB  
2415 C CG  . ASP A 328 ? 0.6161 0.7610 0.6338 -0.0212 -0.0556 0.0388  329 ASP A CG  
2416 O OD1 . ASP A 328 ? 0.6193 0.7594 0.6376 -0.0203 -0.0521 0.0314  329 ASP A OD1 
2417 O OD2 . ASP A 328 ? 0.6394 0.7847 0.6656 -0.0179 -0.0586 0.0460  329 ASP A OD2 
2418 N N   . ALA A 329 ? 0.5443 0.7244 0.5457 -0.0375 -0.0654 0.0420  330 ALA A N   
2419 C CA  . ALA A 329 ? 0.5455 0.7365 0.5510 -0.0395 -0.0702 0.0455  330 ALA A CA  
2420 C C   . ALA A 329 ? 0.5479 0.7470 0.5467 -0.0454 -0.0699 0.0375  330 ALA A C   
2421 O O   . ALA A 329 ? 0.5539 0.7601 0.5569 -0.0466 -0.0728 0.0380  330 ALA A O   
2422 C CB  . ALA A 329 ? 0.5463 0.7469 0.5521 -0.0412 -0.0762 0.0569  330 ALA A CB  
2423 N N   . ASP A 330 ? 0.5383 0.7365 0.5273 -0.0492 -0.0662 0.0298  331 ASP A N   
2424 C CA  . ASP A 330 ? 0.5340 0.7390 0.5166 -0.0551 -0.0653 0.0208  331 ASP A CA  
2425 C C   . ASP A 330 ? 0.5309 0.7276 0.5186 -0.0530 -0.0618 0.0124  331 ASP A C   
2426 O O   . ASP A 330 ? 0.5345 0.7190 0.5236 -0.0494 -0.0572 0.0080  331 ASP A O   
2427 C CB  . ASP A 330 ? 0.5520 0.7580 0.5239 -0.0591 -0.0621 0.0152  331 ASP A CB  
2428 C CG  . ASP A 330 ? 0.5944 0.8113 0.5583 -0.0665 -0.0620 0.0071  331 ASP A CG  
2429 O OD1 . ASP A 330 ? 0.5965 0.8136 0.5632 -0.0678 -0.0616 0.0007  331 ASP A OD1 
2430 O OD2 . ASP A 330 ? 0.6215 0.8467 0.5764 -0.0713 -0.0621 0.0067  331 ASP A OD2 
2431 N N   . PRO A 331 ? 0.5233 0.7269 0.5134 -0.0559 -0.0640 0.0099  332 PRO A N   
2432 C CA  . PRO A 331 ? 0.5167 0.7127 0.5120 -0.0545 -0.0608 0.0025  332 PRO A CA  
2433 C C   . PRO A 331 ? 0.5082 0.6989 0.4979 -0.0573 -0.0562 -0.0087 332 PRO A C   
2434 O O   . PRO A 331 ? 0.5085 0.6899 0.5027 -0.0553 -0.0530 -0.0141 332 PRO A O   
2435 C CB  . PRO A 331 ? 0.5250 0.7316 0.5244 -0.0574 -0.0650 0.0039  332 PRO A CB  
2436 C CG  . PRO A 331 ? 0.5332 0.7542 0.5255 -0.0630 -0.0693 0.0074  332 PRO A CG  
2437 C CD  . PRO A 331 ? 0.5151 0.7343 0.5041 -0.0607 -0.0697 0.0144  332 PRO A CD  
2438 N N   . GLU A 332 ? 0.4961 0.6932 0.4766 -0.0622 -0.0558 -0.0123 333 GLU A N   
2439 C CA  . GLU A 332 ? 0.4859 0.6790 0.4618 -0.0649 -0.0514 -0.0234 333 GLU A CA  
2440 C C   . GLU A 332 ? 0.4522 0.6327 0.4277 -0.0603 -0.0467 -0.0251 333 GLU A C   
2441 O O   . GLU A 332 ? 0.4487 0.6236 0.4229 -0.0612 -0.0428 -0.0341 333 GLU A O   
2442 C CB  . GLU A 332 ? 0.5377 0.7442 0.5041 -0.0721 -0.0526 -0.0273 333 GLU A CB  
2443 C CG  . GLU A 332 ? 0.6339 0.8527 0.6001 -0.0777 -0.0565 -0.0287 333 GLU A CG  
2444 C CD  . GLU A 332 ? 0.7493 0.9642 0.7181 -0.0802 -0.0539 -0.0400 333 GLU A CD  
2445 O OE1 . GLU A 332 ? 0.7797 0.9995 0.7426 -0.0856 -0.0520 -0.0494 333 GLU A OE1 
2446 O OE2 . GLU A 332 ? 0.7823 0.9896 0.7593 -0.0771 -0.0537 -0.0396 333 GLU A OE2 
2447 N N   . VAL A 333 ? 0.4236 0.5999 0.4010 -0.0555 -0.0474 -0.0166 334 VAL A N   
2448 C CA  . VAL A 333 ? 0.4013 0.5664 0.3789 -0.0511 -0.0436 -0.0168 334 VAL A CA  
2449 C C   . VAL A 333 ? 0.3781 0.5307 0.3642 -0.0454 -0.0415 -0.0168 334 VAL A C   
2450 O O   . VAL A 333 ? 0.3774 0.5299 0.3695 -0.0426 -0.0438 -0.0108 334 VAL A O   
2451 C CB  . VAL A 333 ? 0.4032 0.5714 0.3782 -0.0498 -0.0456 -0.0076 334 VAL A CB  
2452 C CG1 . VAL A 333 ? 0.4058 0.5622 0.3824 -0.0448 -0.0421 -0.0069 334 VAL A CG1 
2453 C CG2 . VAL A 333 ? 0.4074 0.5881 0.3731 -0.0560 -0.0470 -0.0081 334 VAL A CG2 
2454 N N   . LEU A 334 ? 0.3547 0.4975 0.3413 -0.0438 -0.0372 -0.0235 335 LEU A N   
2455 C CA  . LEU A 334 ? 0.3351 0.4666 0.3286 -0.0392 -0.0349 -0.0241 335 LEU A CA  
2456 C C   . LEU A 334 ? 0.3165 0.4393 0.3107 -0.0342 -0.0326 -0.0208 335 LEU A C   
2457 O O   . LEU A 334 ? 0.3202 0.4359 0.3200 -0.0301 -0.0318 -0.0183 335 LEU A O   
2458 C CB  . LEU A 334 ? 0.3351 0.4612 0.3298 -0.0409 -0.0320 -0.0333 335 LEU A CB  
2459 C CG  . LEU A 334 ? 0.3585 0.4916 0.3533 -0.0460 -0.0337 -0.0381 335 LEU A CG  
2460 C CD1 . LEU A 334 ? 0.3723 0.5131 0.3600 -0.0510 -0.0335 -0.0439 335 LEU A CD1 
2461 C CD2 . LEU A 334 ? 0.3676 0.4925 0.3679 -0.0459 -0.0316 -0.0439 335 LEU A CD2 
2462 N N   . ILE A 335 ? 0.2933 0.4171 0.2817 -0.0351 -0.0314 -0.0216 336 ILE A N   
2463 C CA  . ILE A 335 ? 0.2727 0.3896 0.2609 -0.0313 -0.0293 -0.0190 336 ILE A CA  
2464 C C   . ILE A 335 ? 0.2574 0.3816 0.2407 -0.0328 -0.0315 -0.0131 336 ILE A C   
2465 O O   . ILE A 335 ? 0.2573 0.3902 0.2346 -0.0375 -0.0323 -0.0151 336 ILE A O   
2466 C CB  . ILE A 335 ? 0.2673 0.3782 0.2538 -0.0313 -0.0252 -0.0268 336 ILE A CB  
2467 C CG1 . ILE A 335 ? 0.2751 0.3773 0.2675 -0.0293 -0.0234 -0.0308 336 ILE A CG1 
2468 C CG2 . ILE A 335 ? 0.2673 0.3739 0.2519 -0.0287 -0.0234 -0.0243 336 ILE A CG2 
2469 C CD1 . ILE A 335 ? 0.2920 0.3892 0.2844 -0.0297 -0.0201 -0.0386 336 ILE A CD1 
2470 N N   . ALA A 336 ? 0.2507 0.3713 0.2367 -0.0292 -0.0323 -0.0060 337 ALA A N   
2471 C CA  . ALA A 336 ? 0.2530 0.3787 0.2355 -0.0303 -0.0344 0.0008  337 ALA A CA  
2472 C C   . ALA A 336 ? 0.2576 0.3740 0.2438 -0.0254 -0.0329 0.0045  337 ALA A C   
2473 O O   . ALA A 336 ? 0.2617 0.3731 0.2547 -0.0215 -0.0335 0.0076  337 ALA A O   
2474 C CB  . ALA A 336 ? 0.2523 0.3863 0.2369 -0.0315 -0.0394 0.0080  337 ALA A CB  
2475 N N   . VAL A 337 ? 0.2590 0.3730 0.2411 -0.0257 -0.0304 0.0030  338 VAL A N   
2476 C CA  . VAL A 337 ? 0.2673 0.3727 0.2525 -0.0217 -0.0287 0.0058  338 VAL A CA  
2477 C C   . VAL A 337 ? 0.2837 0.3921 0.2635 -0.0239 -0.0285 0.0086  338 VAL A C   
2478 O O   . VAL A 337 ? 0.2840 0.3988 0.2572 -0.0280 -0.0274 0.0048  338 VAL A O   
2479 C CB  . VAL A 337 ? 0.2706 0.3663 0.2586 -0.0184 -0.0249 -0.0006 338 VAL A CB  
2480 C CG1 . VAL A 337 ? 0.2671 0.3637 0.2506 -0.0210 -0.0220 -0.0086 338 VAL A CG1 
2481 C CG2 . VAL A 337 ? 0.2787 0.3663 0.2696 -0.0146 -0.0233 0.0021  338 VAL A CG2 
2482 N N   . LEU A 338 ? 0.2915 0.3955 0.2744 -0.0214 -0.0293 0.0150  339 LEU A N   
2483 C CA  . LEU A 338 ? 0.3074 0.4132 0.2863 -0.0233 -0.0291 0.0188  339 LEU A CA  
2484 C C   . LEU A 338 ? 0.3139 0.4099 0.2952 -0.0198 -0.0257 0.0166  339 LEU A C   
2485 O O   . LEU A 338 ? 0.3128 0.4014 0.3006 -0.0157 -0.0258 0.0186  339 LEU A O   
2486 C CB  . LEU A 338 ? 0.3206 0.4288 0.3027 -0.0232 -0.0335 0.0290  339 LEU A CB  
2487 C CG  . LEU A 338 ? 0.3532 0.4689 0.3297 -0.0277 -0.0352 0.0349  339 LEU A CG  
2488 C CD1 . LEU A 338 ? 0.3659 0.4940 0.3346 -0.0335 -0.0362 0.0326  339 LEU A CD1 
2489 C CD2 . LEU A 338 ? 0.3618 0.4776 0.3439 -0.0267 -0.0397 0.0456  339 LEU A CD2 
2490 N N   . LEU A 339 ? 0.3208 0.4174 0.2973 -0.0216 -0.0226 0.0123  340 LEU A N   
2491 C CA  . LEU A 339 ? 0.3317 0.4200 0.3104 -0.0186 -0.0196 0.0101  340 LEU A CA  
2492 C C   . LEU A 339 ? 0.3399 0.4306 0.3148 -0.0210 -0.0186 0.0124  340 LEU A C   
2493 O O   . LEU A 339 ? 0.3481 0.4467 0.3170 -0.0251 -0.0177 0.0101  340 LEU A O   
2494 C CB  . LEU A 339 ? 0.3374 0.4224 0.3162 -0.0173 -0.0162 0.0012  340 LEU A CB  
2495 C CG  . LEU A 339 ? 0.3582 0.4382 0.3421 -0.0143 -0.0164 -0.0011 340 LEU A CG  
2496 C CD1 . LEU A 339 ? 0.3646 0.4418 0.3487 -0.0137 -0.0135 -0.0091 340 LEU A CD1 
2497 C CD2 . LEU A 339 ? 0.3626 0.4350 0.3525 -0.0101 -0.0168 0.0027  340 LEU A CD2 
2498 N N   . ALA A 340 ? 0.3376 0.4218 0.3162 -0.0187 -0.0184 0.0162  341 ALA A N   
2499 C CA  . ALA A 340 ? 0.3461 0.4318 0.3217 -0.0210 -0.0174 0.0187  341 ALA A CA  
2500 C C   . ALA A 340 ? 0.3575 0.4427 0.3309 -0.0210 -0.0132 0.0109  341 ALA A C   
2501 O O   . ALA A 340 ? 0.3600 0.4383 0.3370 -0.0174 -0.0113 0.0062  341 ALA A O   
2502 C CB  . ALA A 340 ? 0.3479 0.4259 0.3293 -0.0183 -0.0184 0.0243  341 ALA A CB  
2503 N N   . THR A 341 ? 0.3636 0.4566 0.3311 -0.0251 -0.0118 0.0094  342 THR A N   
2504 C CA  . THR A 341 ? 0.3738 0.4677 0.3399 -0.0252 -0.0078 0.0016  342 THR A CA  
2505 C C   . THR A 341 ? 0.3810 0.4670 0.3511 -0.0221 -0.0058 0.0009  342 THR A C   
2506 O O   . THR A 341 ? 0.3860 0.4695 0.3580 -0.0201 -0.0031 -0.0057 342 THR A O   
2507 C CB  . THR A 341 ? 0.3991 0.5043 0.3584 -0.0306 -0.0064 0.0001  342 THR A CB  
2508 O OG1 . THR A 341 ? 0.4246 0.5306 0.3841 -0.0301 -0.0024 -0.0084 342 THR A OG1 
2509 C CG2 . THR A 341 ? 0.4014 0.5098 0.3584 -0.0337 -0.0075 0.0077  342 THR A CG2 
2510 N N   . ASN A 342 ? 0.3778 0.4601 0.3498 -0.0219 -0.0072 0.0077  343 ASN A N   
2511 C CA  . ASN A 342 ? 0.3805 0.4561 0.3563 -0.0194 -0.0054 0.0069  343 ASN A CA  
2512 C C   . ASN A 342 ? 0.3706 0.4375 0.3516 -0.0145 -0.0050 0.0036  343 ASN A C   
2513 O O   . ASN A 342 ? 0.3690 0.4327 0.3519 -0.0126 -0.0027 -0.0007 343 ASN A O   
2514 C CB  . ASN A 342 ? 0.4095 0.4831 0.3865 -0.0208 -0.0071 0.0146  343 ASN A CB  
2515 C CG  . ASN A 342 ? 0.4737 0.5559 0.4455 -0.0260 -0.0065 0.0172  343 ASN A CG  
2516 O OD1 . ASN A 342 ? 0.4940 0.5832 0.4616 -0.0282 -0.0040 0.0119  343 ASN A OD1 
2517 N ND2 . ASN A 342 ? 0.4871 0.5691 0.4595 -0.0281 -0.0089 0.0254  343 ASN A ND2 
2518 N N   . ASN A 343 ? 0.3607 0.4250 0.3440 -0.0128 -0.0073 0.0057  344 ASN A N   
2519 C CA  . ASN A 343 ? 0.3566 0.4141 0.3445 -0.0087 -0.0070 0.0029  344 ASN A CA  
2520 C C   . ASN A 343 ? 0.3405 0.3989 0.3277 -0.0080 -0.0051 -0.0039 344 ASN A C   
2521 O O   . ASN A 343 ? 0.3338 0.3872 0.3239 -0.0054 -0.0037 -0.0070 344 ASN A O   
2522 C CB  . ASN A 343 ? 0.3823 0.4378 0.3733 -0.0073 -0.0097 0.0070  344 ASN A CB  
2523 C CG  . ASN A 343 ? 0.4485 0.5011 0.4426 -0.0071 -0.0114 0.0133  344 ASN A CG  
2524 O OD1 . ASN A 343 ? 0.4772 0.5236 0.4753 -0.0048 -0.0105 0.0130  344 ASN A OD1 
2525 N ND2 . ASN A 343 ? 0.4633 0.5205 0.4558 -0.0098 -0.0138 0.0190  344 ASN A ND2 
2526 N N   . ILE A 344 ? 0.3357 0.4006 0.3191 -0.0106 -0.0051 -0.0064 345 ILE A N   
2527 C CA  . ILE A 344 ? 0.3376 0.4036 0.3211 -0.0103 -0.0033 -0.0133 345 ILE A CA  
2528 C C   . ILE A 344 ? 0.3351 0.4001 0.3196 -0.0096 -0.0005 -0.0174 345 ILE A C   
2529 O O   . ILE A 344 ? 0.3399 0.4004 0.3280 -0.0070 0.0007  -0.0211 345 ILE A O   
2530 C CB  . ILE A 344 ? 0.3476 0.4220 0.3266 -0.0140 -0.0036 -0.0157 345 ILE A CB  
2531 C CG1 . ILE A 344 ? 0.3575 0.4341 0.3357 -0.0150 -0.0068 -0.0112 345 ILE A CG1 
2532 C CG2 . ILE A 344 ? 0.3553 0.4302 0.3354 -0.0137 -0.0016 -0.0237 345 ILE A CG2 
2533 C CD1 . ILE A 344 ? 0.3729 0.4600 0.3453 -0.0198 -0.0075 -0.0123 345 ILE A CD1 
2534 N N   . LYS A 345 ? 0.3251 0.3944 0.3067 -0.0119 0.0005  -0.0159 346 LYS A N   
2535 C CA  . LYS A 345 ? 0.3223 0.3924 0.3049 -0.0118 0.0031  -0.0192 346 LYS A CA  
2536 C C   . LYS A 345 ? 0.3058 0.3681 0.2931 -0.0082 0.0034  -0.0186 346 LYS A C   
2537 O O   . LYS A 345 ? 0.3102 0.3711 0.3006 -0.0064 0.0051  -0.0232 346 LYS A O   
2538 C CB  . LYS A 345 ? 0.3637 0.4401 0.3423 -0.0155 0.0035  -0.0159 346 LYS A CB  
2539 C CG  . LYS A 345 ? 0.4307 0.5152 0.4071 -0.0180 0.0064  -0.0215 346 LYS A CG  
2540 C CD  . LYS A 345 ? 0.4965 0.5888 0.4677 -0.0227 0.0064  -0.0174 346 LYS A CD  
2541 C CE  . LYS A 345 ? 0.5422 0.6402 0.5085 -0.0260 0.0042  -0.0141 346 LYS A CE  
2542 N NZ  . LYS A 345 ? 0.5705 0.6740 0.5350 -0.0271 0.0054  -0.0213 346 LYS A NZ  
2543 N N   . SER A 346 ? 0.2891 0.3469 0.2774 -0.0073 0.0018  -0.0132 347 SER A N   
2544 C CA  . SER A 346 ? 0.2851 0.3365 0.2773 -0.0045 0.0021  -0.0131 347 SER A CA  
2545 C C   . SER A 346 ? 0.2725 0.3194 0.2679 -0.0015 0.0018  -0.0156 347 SER A C   
2546 O O   . SER A 346 ? 0.2852 0.3292 0.2833 0.0003  0.0027  -0.0175 347 SER A O   
2547 C CB  . SER A 346 ? 0.3163 0.3641 0.3095 -0.0045 0.0007  -0.0077 347 SER A CB  
2548 O OG  . SER A 346 ? 0.3659 0.4134 0.3588 -0.0048 -0.0016 -0.0040 347 SER A OG  
2549 N N   . LEU A 347 ? 0.2477 0.2945 0.2427 -0.0013 0.0005  -0.0155 348 LEU A N   
2550 C CA  . LEU A 347 ? 0.2359 0.2789 0.2339 0.0010  0.0003  -0.0176 348 LEU A CA  
2551 C C   . LEU A 347 ? 0.2363 0.2803 0.2358 0.0013  0.0018  -0.0227 348 LEU A C   
2552 O O   . LEU A 347 ? 0.2293 0.2697 0.2322 0.0033  0.0020  -0.0240 348 LEU A O   
2553 C CB  . LEU A 347 ? 0.2328 0.2760 0.2306 0.0008  -0.0015 -0.0161 348 LEU A CB  
2554 C CG  . LEU A 347 ? 0.2476 0.2889 0.2463 0.0014  -0.0031 -0.0114 348 LEU A CG  
2555 C CD1 . LEU A 347 ? 0.2565 0.3007 0.2543 0.0004  -0.0050 -0.0096 348 LEU A CD1 
2556 C CD2 . LEU A 347 ? 0.2546 0.2908 0.2568 0.0040  -0.0029 -0.0113 348 LEU A CD2 
2557 N N   . LYS A 348 ? 0.2437 0.2930 0.2411 -0.0008 0.0027  -0.0257 349 LYS A N   
2558 C CA  . LYS A 348 ? 0.2574 0.3078 0.2574 -0.0003 0.0044  -0.0314 349 LYS A CA  
2559 C C   . LYS A 348 ? 0.2698 0.3192 0.2730 0.0013  0.0058  -0.0325 349 LYS A C   
2560 O O   . LYS A 348 ? 0.2678 0.3153 0.2757 0.0031  0.0064  -0.0358 349 LYS A O   
2561 C CB  . LYS A 348 ? 0.2852 0.3429 0.2820 -0.0033 0.0055  -0.0350 349 LYS A CB  
2562 C CG  . LYS A 348 ? 0.3400 0.3992 0.3352 -0.0047 0.0043  -0.0360 349 LYS A CG  
2563 C CD  . LYS A 348 ? 0.4058 0.4731 0.3973 -0.0082 0.0055  -0.0402 349 LYS A CD  
2564 C CE  . LYS A 348 ? 0.4524 0.5216 0.4424 -0.0099 0.0040  -0.0413 349 LYS A CE  
2565 N NZ  . LYS A 348 ? 0.4701 0.5489 0.4545 -0.0142 0.0045  -0.0434 349 LYS A NZ  
2566 N N   . LYS A 349 ? 0.2775 0.3281 0.2787 0.0004  0.0060  -0.0294 350 LYS A N   
2567 C CA  . LYS A 349 ? 0.2872 0.3379 0.2909 0.0014  0.0072  -0.0300 350 LYS A CA  
2568 C C   . LYS A 349 ? 0.2741 0.3188 0.2809 0.0039  0.0061  -0.0278 350 LYS A C   
2569 O O   . LYS A 349 ? 0.2761 0.3200 0.2870 0.0056  0.0065  -0.0296 350 LYS A O   
2570 C CB  . LYS A 349 ? 0.3360 0.3902 0.3362 -0.0011 0.0077  -0.0271 350 LYS A CB  
2571 C CG  . LYS A 349 ? 0.4166 0.4732 0.4191 -0.0010 0.0094  -0.0286 350 LYS A CG  
2572 C CD  . LYS A 349 ? 0.5040 0.5660 0.5028 -0.0044 0.0103  -0.0267 350 LYS A CD  
2573 C CE  . LYS A 349 ? 0.5759 0.6454 0.5718 -0.0070 0.0118  -0.0299 350 LYS A CE  
2574 N NZ  . LYS A 349 ? 0.6106 0.6837 0.6105 -0.0058 0.0141  -0.0366 350 LYS A NZ  
2575 N N   . ALA A 350 ? 0.2601 0.3015 0.2653 0.0041  0.0046  -0.0240 351 ALA A N   
2576 C CA  . ALA A 350 ? 0.2483 0.2851 0.2556 0.0059  0.0036  -0.0222 351 ALA A CA  
2577 C C   . ALA A 350 ? 0.2418 0.2763 0.2521 0.0075  0.0031  -0.0238 351 ALA A C   
2578 O O   . ALA A 350 ? 0.2389 0.2715 0.2520 0.0089  0.0027  -0.0234 351 ALA A O   
2579 C CB  . ALA A 350 ? 0.2445 0.2790 0.2499 0.0056  0.0025  -0.0187 351 ALA A CB  
2580 N N   . TYR A 351 ? 0.2363 0.2715 0.2462 0.0070  0.0029  -0.0255 352 TYR A N   
2581 C CA  . TYR A 351 ? 0.2471 0.2798 0.2603 0.0081  0.0022  -0.0268 352 TYR A CA  
2582 C C   . TYR A 351 ? 0.2594 0.2939 0.2749 0.0078  0.0030  -0.0314 352 TYR A C   
2583 O O   . TYR A 351 ? 0.2535 0.2892 0.2676 0.0065  0.0029  -0.0330 352 TYR A O   
2584 C CB  . TYR A 351 ? 0.2453 0.2764 0.2570 0.0077  0.0009  -0.0246 352 TYR A CB  
2585 C CG  . TYR A 351 ? 0.2542 0.2837 0.2648 0.0082  0.0004  -0.0211 352 TYR A CG  
2586 C CD1 . TYR A 351 ? 0.2589 0.2862 0.2715 0.0093  0.0001  -0.0199 352 TYR A CD1 
2587 C CD2 . TYR A 351 ? 0.2659 0.2963 0.2738 0.0074  0.0001  -0.0190 352 TYR A CD2 
2588 C CE1 . TYR A 351 ? 0.2694 0.2960 0.2810 0.0095  -0.0001 -0.0177 352 TYR A CE1 
2589 C CE2 . TYR A 351 ? 0.2784 0.3071 0.2864 0.0080  -0.0001 -0.0167 352 TYR A CE2 
2590 C CZ  . TYR A 351 ? 0.2892 0.3162 0.2989 0.0090  0.0000  -0.0165 352 TYR A CZ  
2591 O OH  . TYR A 351 ? 0.3175 0.3435 0.3273 0.0093  0.0000  -0.0152 352 TYR A OH  
2592 N N   . PRO A 352 ? 0.2673 0.3022 0.2871 0.0090  0.0039  -0.0339 353 PRO A N   
2593 C CA  . PRO A 352 ? 0.2769 0.3134 0.3002 0.0090  0.0050  -0.0393 353 PRO A CA  
2594 C C   . PRO A 352 ? 0.2920 0.3252 0.3181 0.0090  0.0040  -0.0406 353 PRO A C   
2595 O O   . PRO A 352 ? 0.3014 0.3366 0.3277 0.0078  0.0048  -0.0451 353 PRO A O   
2596 C CB  . PRO A 352 ? 0.2831 0.3195 0.3125 0.0110  0.0056  -0.0408 353 PRO A CB  
2597 C CG  . PRO A 352 ? 0.2832 0.3199 0.3104 0.0113  0.0052  -0.0366 353 PRO A CG  
2598 C CD  . PRO A 352 ? 0.2613 0.2958 0.2833 0.0103  0.0040  -0.0323 353 PRO A CD  
2599 N N   . ASN A 353 ? 0.2916 0.3202 0.3197 0.0101  0.0023  -0.0370 354 ASN A N   
2600 C CA  . ASN A 353 ? 0.2916 0.3167 0.3227 0.0099  0.0012  -0.0374 354 ASN A CA  
2601 C C   . ASN A 353 ? 0.2832 0.3082 0.3094 0.0085  0.0001  -0.0341 354 ASN A C   
2602 O O   . ASN A 353 ? 0.2893 0.3112 0.3174 0.0085  -0.0012 -0.0316 354 ASN A O   
2603 C CB  . ASN A 353 ? 0.3155 0.3364 0.3530 0.0117  -0.0001 -0.0351 354 ASN A CB  
2604 C CG  . ASN A 353 ? 0.3775 0.3943 0.4196 0.0114  -0.0014 -0.0354 354 ASN A CG  
2605 O OD1 . ASN A 353 ? 0.4110 0.4280 0.4535 0.0101  -0.0009 -0.0393 354 ASN A OD1 
2606 N ND2 . ASN A 353 ? 0.3806 0.3940 0.4261 0.0121  -0.0031 -0.0309 354 ASN A ND2 
2607 N N   . TYR A 354 ? 0.2672 0.2959 0.2877 0.0071  0.0005  -0.0337 355 TYR A N   
2608 C CA  . TYR A 354 ? 0.2632 0.2923 0.2802 0.0061  -0.0006 -0.0307 355 TYR A CA  
2609 C C   . TYR A 354 ? 0.2672 0.2954 0.2859 0.0049  -0.0015 -0.0320 355 TYR A C   
2610 O O   . TYR A 354 ? 0.2690 0.2961 0.2874 0.0047  -0.0026 -0.0290 355 TYR A O   
2611 C CB  . TYR A 354 ? 0.2603 0.2938 0.2719 0.0047  -0.0003 -0.0298 355 TYR A CB  
2612 C CG  . TYR A 354 ? 0.2620 0.2999 0.2717 0.0026  0.0003  -0.0338 355 TYR A CG  
2613 C CD1 . TYR A 354 ? 0.2696 0.3106 0.2792 0.0021  0.0020  -0.0375 355 TYR A CD1 
2614 C CD2 . TYR A 354 ? 0.2681 0.3081 0.2763 0.0008  -0.0007 -0.0343 355 TYR A CD2 
2615 C CE1 . TYR A 354 ? 0.2774 0.3235 0.2850 -0.0002 0.0029  -0.0418 355 TYR A CE1 
2616 C CE2 . TYR A 354 ? 0.2790 0.3238 0.2853 -0.0016 -0.0002 -0.0385 355 TYR A CE2 
2617 C CZ  . TYR A 354 ? 0.2888 0.3369 0.2945 -0.0022 0.0017  -0.0424 355 TYR A CZ  
2618 O OH  . TYR A 354 ? 0.3058 0.3599 0.3091 -0.0050 0.0026  -0.0472 355 TYR A OH  
2619 N N   . PHE A 355 ? 0.2640 0.2929 0.2848 0.0039  -0.0009 -0.0370 356 PHE A N   
2620 C CA  . PHE A 355 ? 0.2685 0.2968 0.2909 0.0023  -0.0017 -0.0389 356 PHE A CA  
2621 C C   . PHE A 355 ? 0.2639 0.2867 0.2921 0.0031  -0.0027 -0.0376 356 PHE A C   
2622 O O   . PHE A 355 ? 0.2686 0.2907 0.2974 0.0019  -0.0038 -0.0362 356 PHE A O   
2623 C CB  . PHE A 355 ? 0.2754 0.3070 0.2980 0.0005  -0.0007 -0.0453 356 PHE A CB  
2624 C CG  . PHE A 355 ? 0.2899 0.3209 0.3167 0.0018  0.0010  -0.0499 356 PHE A CG  
2625 C CD1 . PHE A 355 ? 0.3049 0.3395 0.3289 0.0023  0.0025  -0.0503 356 PHE A CD1 
2626 C CD2 . PHE A 355 ? 0.3008 0.3278 0.3351 0.0024  0.0012  -0.0539 356 PHE A CD2 
2627 C CE1 . PHE A 355 ? 0.3154 0.3504 0.3439 0.0035  0.0042  -0.0548 356 PHE A CE1 
2628 C CE2 . PHE A 355 ? 0.3131 0.3400 0.3524 0.0038  0.0028  -0.0586 356 PHE A CE2 
2629 C CZ  . PHE A 355 ? 0.3132 0.3444 0.3496 0.0044  0.0044  -0.0592 356 PHE A CZ  
2630 N N   . GLY A 356 ? 0.2526 0.2722 0.2852 0.0051  -0.0024 -0.0373 357 GLY A N   
2631 C CA  . GLY A 356 ? 0.2435 0.2582 0.2816 0.0057  -0.0037 -0.0345 357 GLY A CA  
2632 C C   . GLY A 356 ? 0.2343 0.2492 0.2691 0.0055  -0.0047 -0.0287 357 GLY A C   
2633 O O   . GLY A 356 ? 0.2403 0.2534 0.2770 0.0044  -0.0058 -0.0264 357 GLY A O   
2634 N N   . SER A 357 ? 0.2231 0.2406 0.2531 0.0063  -0.0041 -0.0266 358 SER A N   
2635 C CA  . SER A 357 ? 0.2194 0.2380 0.2465 0.0062  -0.0045 -0.0222 358 SER A CA  
2636 C C   . SER A 357 ? 0.2199 0.2406 0.2447 0.0047  -0.0049 -0.0216 358 SER A C   
2637 O O   . SER A 357 ? 0.2229 0.2435 0.2485 0.0040  -0.0055 -0.0189 358 SER A O   
2638 C CB  . SER A 357 ? 0.2254 0.2459 0.2490 0.0074  -0.0037 -0.0210 358 SER A CB  
2639 O OG  . SER A 357 ? 0.2319 0.2509 0.2578 0.0086  -0.0037 -0.0203 358 SER A OG  
2640 N N   . THR A 358 ? 0.2154 0.2390 0.2375 0.0039  -0.0047 -0.0240 359 THR A N   
2641 C CA  . THR A 358 ? 0.2102 0.2366 0.2308 0.0026  -0.0054 -0.0230 359 THR A CA  
2642 C C   . THR A 358 ? 0.2064 0.2315 0.2304 0.0009  -0.0062 -0.0240 359 THR A C   
2643 O O   . THR A 358 ? 0.1966 0.2232 0.2208 0.0000  -0.0069 -0.0219 359 THR A O   
2644 C CB  . THR A 358 ? 0.2116 0.2420 0.2285 0.0019  -0.0054 -0.0243 359 THR A CB  
2645 O OG1 . THR A 358 ? 0.2244 0.2552 0.2416 0.0008  -0.0050 -0.0286 359 THR A OG1 
2646 C CG2 . THR A 358 ? 0.2087 0.2400 0.2228 0.0033  -0.0048 -0.0224 359 THR A CG2 
2647 N N   . ASN A 359 ? 0.2133 0.2356 0.2406 0.0004  -0.0062 -0.0273 360 ASN A N   
2648 C CA  . ASN A 359 ? 0.2313 0.2511 0.2630 -0.0014 -0.0070 -0.0283 360 ASN A CA  
2649 C C   . ASN A 359 ? 0.2195 0.2368 0.2538 -0.0013 -0.0077 -0.0236 360 ASN A C   
2650 O O   . ASN A 359 ? 0.2265 0.2448 0.2619 -0.0031 -0.0084 -0.0219 360 ASN A O   
2651 C CB  . ASN A 359 ? 0.2912 0.3076 0.3274 -0.0014 -0.0067 -0.0330 360 ASN A CB  
2652 C CG  . ASN A 359 ? 0.4136 0.4334 0.4479 -0.0026 -0.0059 -0.0388 360 ASN A CG  
2653 O OD1 . ASN A 359 ? 0.4494 0.4744 0.4788 -0.0039 -0.0061 -0.0389 360 ASN A OD1 
2654 N ND2 . ASN A 359 ? 0.4472 0.4648 0.4856 -0.0022 -0.0050 -0.0438 360 ASN A ND2 
2655 N N   . GLN A 360 ? 0.2011 0.2162 0.2363 0.0004  -0.0075 -0.0214 361 GLN A N   
2656 C CA  . GLN A 360 ? 0.1974 0.2114 0.2344 0.0001  -0.0081 -0.0166 361 GLN A CA  
2657 C C   . GLN A 360 ? 0.1793 0.1976 0.2124 -0.0005 -0.0078 -0.0137 361 GLN A C   
2658 O O   . GLN A 360 ? 0.1872 0.2062 0.2218 -0.0022 -0.0083 -0.0109 361 GLN A O   
2659 C CB  . GLN A 360 ? 0.2295 0.2415 0.2675 0.0021  -0.0081 -0.0149 361 GLN A CB  
2660 C CG  . GLN A 360 ? 0.3024 0.3138 0.3422 0.0012  -0.0092 -0.0096 361 GLN A CG  
2661 C CD  . GLN A 360 ? 0.3994 0.4098 0.4405 0.0029  -0.0096 -0.0076 361 GLN A CD  
2662 O OE1 . GLN A 360 ? 0.4458 0.4573 0.4846 0.0047  -0.0086 -0.0096 361 GLN A OE1 
2663 N NE2 . GLN A 360 ? 0.3997 0.4083 0.4446 0.0019  -0.0112 -0.0031 361 GLN A NE2 
2664 N N   . PHE A 361 ? 0.1579 0.1792 0.1869 0.0008  -0.0069 -0.0144 362 PHE A N   
2665 C CA  . PHE A 361 ? 0.1494 0.1748 0.1761 0.0007  -0.0064 -0.0125 362 PHE A CA  
2666 C C   . PHE A 361 ? 0.1566 0.1847 0.1844 -0.0011 -0.0070 -0.0129 362 PHE A C   
2667 O O   . PHE A 361 ? 0.1673 0.1981 0.1958 -0.0021 -0.0069 -0.0108 362 PHE A O   
2668 C CB  . PHE A 361 ? 0.1354 0.1625 0.1587 0.0026  -0.0056 -0.0131 362 PHE A CB  
2669 C CG  . PHE A 361 ? 0.1361 0.1667 0.1585 0.0030  -0.0049 -0.0115 362 PHE A CG  
2670 C CD1 . PHE A 361 ? 0.1370 0.1687 0.1595 0.0027  -0.0042 -0.0095 362 PHE A CD1 
2671 C CD2 . PHE A 361 ? 0.1470 0.1806 0.1690 0.0035  -0.0049 -0.0119 362 PHE A CD2 
2672 C CE1 . PHE A 361 ? 0.1445 0.1800 0.1668 0.0029  -0.0032 -0.0091 362 PHE A CE1 
2673 C CE2 . PHE A 361 ? 0.1512 0.1879 0.1738 0.0042  -0.0041 -0.0110 362 PHE A CE2 
2674 C CZ  . PHE A 361 ? 0.1449 0.1826 0.1677 0.0039  -0.0031 -0.0101 362 PHE A CZ  
2675 N N   . GLY A 362 ? 0.1506 0.1785 0.1785 -0.0018 -0.0076 -0.0158 363 GLY A N   
2676 C CA  . GLY A 362 ? 0.1485 0.1793 0.1776 -0.0038 -0.0084 -0.0164 363 GLY A CA  
2677 C C   . GLY A 362 ? 0.1536 0.1827 0.1866 -0.0061 -0.0090 -0.0151 363 GLY A C   
2678 O O   . GLY A 362 ? 0.1532 0.1858 0.1873 -0.0077 -0.0093 -0.0137 363 GLY A O   
2679 N N   . ARG A 363 ? 0.1561 0.1799 0.1918 -0.0064 -0.0093 -0.0153 364 ARG A N   
2680 C CA  . ARG A 363 ? 0.1653 0.1866 0.2055 -0.0088 -0.0101 -0.0132 364 ARG A CA  
2681 C C   . ARG A 363 ? 0.1684 0.1924 0.2079 -0.0093 -0.0098 -0.0084 364 ARG A C   
2682 O O   . ARG A 363 ? 0.1841 0.2098 0.2257 -0.0119 -0.0102 -0.0062 364 ARG A O   
2683 C CB  . ARG A 363 ? 0.1873 0.2021 0.2316 -0.0084 -0.0107 -0.0140 364 ARG A CB  
2684 C CG  . ARG A 363 ? 0.2485 0.2608 0.2950 -0.0086 -0.0109 -0.0197 364 ARG A CG  
2685 C CD  . ARG A 363 ? 0.3270 0.3334 0.3780 -0.0070 -0.0110 -0.0211 364 ARG A CD  
2686 N NE  . ARG A 363 ? 0.4045 0.4099 0.4567 -0.0067 -0.0104 -0.0277 364 ARG A NE  
2687 C CZ  . ARG A 363 ? 0.4464 0.4467 0.5053 -0.0064 -0.0106 -0.0310 364 ARG A CZ  
2688 N NH1 . ARG A 363 ? 0.4478 0.4427 0.5130 -0.0061 -0.0118 -0.0273 364 ARG A NH1 
2689 N NH2 . ARG A 363 ? 0.4437 0.4445 0.5033 -0.0064 -0.0096 -0.0380 364 ARG A NH2 
2690 N N   . PHE A 364 ? 0.1548 0.1797 0.1914 -0.0072 -0.0089 -0.0070 365 PHE A N   
2691 C CA  . PHE A 364 ? 0.1468 0.1754 0.1819 -0.0078 -0.0082 -0.0033 365 PHE A CA  
2692 C C   . PHE A 364 ? 0.1591 0.1938 0.1932 -0.0085 -0.0073 -0.0036 365 PHE A C   
2693 O O   . PHE A 364 ? 0.1639 0.2024 0.1988 -0.0107 -0.0069 -0.0010 365 PHE A O   
2694 C CB  . PHE A 364 ? 0.1326 0.1611 0.1645 -0.0053 -0.0073 -0.0031 365 PHE A CB  
2695 C CG  . PHE A 364 ? 0.1289 0.1627 0.1583 -0.0055 -0.0061 -0.0012 365 PHE A CG  
2696 C CD1 . PHE A 364 ? 0.1288 0.1642 0.1583 -0.0075 -0.0063 0.0026  365 PHE A CD1 
2697 C CD2 . PHE A 364 ? 0.1360 0.1737 0.1634 -0.0040 -0.0047 -0.0033 365 PHE A CD2 
2698 C CE1 . PHE A 364 ? 0.1331 0.1746 0.1600 -0.0082 -0.0047 0.0036  365 PHE A CE1 
2699 C CE2 . PHE A 364 ? 0.1403 0.1832 0.1664 -0.0044 -0.0032 -0.0025 365 PHE A CE2 
2700 C CZ  . PHE A 364 ? 0.1289 0.1740 0.1543 -0.0066 -0.0030 0.0005  365 PHE A CZ  
2701 N N   . LEU A 365 ? 0.1624 0.1989 0.1952 -0.0068 -0.0070 -0.0064 366 LEU A N   
2702 C CA  . LEU A 365 ? 0.1707 0.2132 0.2039 -0.0069 -0.0065 -0.0067 366 LEU A CA  
2703 C C   . LEU A 365 ? 0.1961 0.2404 0.2324 -0.0100 -0.0074 -0.0062 366 LEU A C   
2704 O O   . LEU A 365 ? 0.2113 0.2609 0.2490 -0.0113 -0.0066 -0.0049 366 LEU A O   
2705 C CB  . LEU A 365 ? 0.1576 0.2010 0.1894 -0.0047 -0.0067 -0.0091 366 LEU A CB  
2706 C CG  . LEU A 365 ? 0.1500 0.1925 0.1792 -0.0018 -0.0058 -0.0094 366 LEU A CG  
2707 C CD1 . LEU A 365 ? 0.1551 0.1984 0.1833 -0.0003 -0.0064 -0.0108 366 LEU A CD1 
2708 C CD2 . LEU A 365 ? 0.1384 0.1849 0.1681 -0.0012 -0.0042 -0.0084 366 LEU A CD2 
2709 N N   . SER A 366 ? 0.1983 0.2387 0.2363 -0.0115 -0.0087 -0.0077 367 SER A N   
2710 C CA  . SER A 366 ? 0.2072 0.2487 0.2486 -0.0148 -0.0097 -0.0076 367 SER A CA  
2711 C C   . SER A 366 ? 0.2159 0.2575 0.2595 -0.0175 -0.0095 -0.0038 367 SER A C   
2712 O O   . SER A 366 ? 0.2157 0.2619 0.2616 -0.0201 -0.0095 -0.0026 367 SER A O   
2713 C CB  . SER A 366 ? 0.2295 0.2661 0.2723 -0.0158 -0.0110 -0.0108 367 SER A CB  
2714 O OG  . SER A 366 ? 0.2646 0.3033 0.3049 -0.0143 -0.0113 -0.0140 367 SER A OG  
2715 N N   . ARG A 367 ? 0.2192 0.2569 0.2623 -0.0172 -0.0094 -0.0013 368 ARG A N   
2716 C CA  . ARG A 367 ? 0.2272 0.2657 0.2720 -0.0201 -0.0095 0.0033  368 ARG A CA  
2717 C C   . ARG A 367 ? 0.2475 0.2943 0.2904 -0.0209 -0.0078 0.0052  368 ARG A C   
2718 O O   . ARG A 367 ? 0.2655 0.3158 0.3102 -0.0245 -0.0077 0.0083  368 ARG A O   
2719 C CB  . ARG A 367 ? 0.2361 0.2694 0.2806 -0.0193 -0.0101 0.0059  368 ARG A CB  
2720 C CG  . ARG A 367 ? 0.2597 0.2848 0.3083 -0.0192 -0.0118 0.0046  368 ARG A CG  
2721 C CD  . ARG A 367 ? 0.2591 0.2796 0.3097 -0.0191 -0.0130 0.0086  368 ARG A CD  
2722 N NE  . ARG A 367 ? 0.2506 0.2716 0.2973 -0.0157 -0.0122 0.0081  368 ARG A NE  
2723 C CZ  . ARG A 367 ? 0.2390 0.2560 0.2858 -0.0126 -0.0122 0.0043  368 ARG A CZ  
2724 N NH1 . ARG A 367 ? 0.2128 0.2255 0.2630 -0.0124 -0.0127 0.0003  368 ARG A NH1 
2725 N NH2 . ARG A 367 ? 0.2310 0.2490 0.2744 -0.0101 -0.0115 0.0043  368 ARG A NH2 
2726 N N   . HIS A 368 ? 0.2415 0.2918 0.2813 -0.0179 -0.0063 0.0031  369 HIS A N   
2727 C CA  . HIS A 368 ? 0.2409 0.2994 0.2799 -0.0182 -0.0042 0.0036  369 HIS A CA  
2728 C C   . HIS A 368 ? 0.2562 0.3206 0.2978 -0.0183 -0.0037 0.0015  369 HIS A C   
2729 O O   . HIS A 368 ? 0.2610 0.3327 0.3038 -0.0200 -0.0023 0.0022  369 HIS A O   
2730 C CB  . HIS A 368 ? 0.2332 0.2925 0.2687 -0.0151 -0.0028 0.0022  369 HIS A CB  
2731 C CG  . HIS A 368 ? 0.2236 0.2804 0.2567 -0.0158 -0.0030 0.0051  369 HIS A CG  
2732 N ND1 . HIS A 368 ? 0.2360 0.2981 0.2680 -0.0189 -0.0022 0.0083  369 HIS A ND1 
2733 C CD2 . HIS A 368 ? 0.2317 0.2819 0.2637 -0.0143 -0.0043 0.0054  369 HIS A CD2 
2734 C CE1 . HIS A 368 ? 0.2407 0.2993 0.2709 -0.0190 -0.0032 0.0108  369 HIS A CE1 
2735 N NE2 . HIS A 368 ? 0.2447 0.2960 0.2752 -0.0160 -0.0044 0.0091  369 HIS A NE2 
2736 N N   . ILE A 369 ? 0.2666 0.3286 0.3091 -0.0167 -0.0050 -0.0011 370 ILE A N   
2737 C CA  . ILE A 369 ? 0.2900 0.3579 0.3354 -0.0166 -0.0051 -0.0027 370 ILE A CA  
2738 C C   . ILE A 369 ? 0.3335 0.4034 0.3823 -0.0209 -0.0061 -0.0014 370 ILE A C   
2739 O O   . ILE A 369 ? 0.3369 0.4144 0.3886 -0.0223 -0.0053 -0.0011 370 ILE A O   
2740 C CB  . ILE A 369 ? 0.2800 0.3457 0.3246 -0.0137 -0.0064 -0.0053 370 ILE A CB  
2741 C CG1 . ILE A 369 ? 0.2788 0.3451 0.3216 -0.0098 -0.0052 -0.0062 370 ILE A CG1 
2742 C CG2 . ILE A 369 ? 0.2780 0.3487 0.3259 -0.0147 -0.0077 -0.0063 370 ILE A CG2 
2743 C CD1 . ILE A 369 ? 0.2885 0.3511 0.3294 -0.0075 -0.0064 -0.0076 370 ILE A CD1 
2744 N N   . ASP A 370 ? 0.3628 0.4261 0.4120 -0.0230 -0.0077 -0.0009 371 ASP A N   
2745 C CA  . ASP A 370 ? 0.3986 0.4622 0.4515 -0.0273 -0.0089 0.0001  371 ASP A CA  
2746 C C   . ASP A 370 ? 0.4363 0.5006 0.4904 -0.0310 -0.0083 0.0045  371 ASP A C   
2747 O O   . ASP A 370 ? 0.4522 0.5119 0.5090 -0.0343 -0.0097 0.0061  371 ASP A O   
2748 C CB  . ASP A 370 ? 0.4247 0.4807 0.4784 -0.0280 -0.0109 -0.0023 371 ASP A CB  
2749 C CG  . ASP A 370 ? 0.5085 0.5642 0.5600 -0.0249 -0.0115 -0.0063 371 ASP A CG  
2750 O OD1 . ASP A 370 ? 0.5200 0.5823 0.5712 -0.0234 -0.0112 -0.0070 371 ASP A OD1 
2751 O OD2 . ASP A 370 ? 0.5493 0.5986 0.5998 -0.0242 -0.0124 -0.0087 371 ASP A OD2 
2752 N N   . THR A 371 ? 0.4473 0.5172 0.4995 -0.0307 -0.0063 0.0065  372 THR A N   
2753 C CA  . THR A 371 ? 0.4646 0.5368 0.5170 -0.0346 -0.0057 0.0112  372 THR A CA  
2754 C C   . THR A 371 ? 0.4762 0.5574 0.5319 -0.0384 -0.0047 0.0122  372 THR A C   
2755 O O   . THR A 371 ? 0.4836 0.5679 0.5422 -0.0383 -0.0051 0.0095  372 THR A O   
2756 C CB  . THR A 371 ? 0.4850 0.5595 0.5331 -0.0331 -0.0039 0.0126  372 THR A CB  
2757 O OG1 . THR A 371 ? 0.4998 0.5657 0.5460 -0.0310 -0.0053 0.0132  372 THR A OG1 
2758 C CG2 . THR A 371 ? 0.4920 0.5730 0.5398 -0.0377 -0.0029 0.0173  372 THR A CG2 
2759 N N   . GLU B 27  ? 1.2950 0.7428 1.0233 -0.4602 0.1613  -0.1898 15  GLU B N   
2760 C CA  . GLU B 27  ? 1.3737 0.6860 1.0417 -0.4366 0.1650  -0.1785 15  GLU B CA  
2761 C C   . GLU B 27  ? 1.3502 0.6559 1.0123 -0.3662 0.1518  -0.1488 15  GLU B C   
2762 O O   . GLU B 27  ? 1.3925 0.6299 1.0241 -0.3274 0.1455  -0.1491 15  GLU B O   
2763 C CB  . GLU B 27  ? 1.4856 0.6847 1.0982 -0.4829 0.1892  -0.1657 15  GLU B CB  
2764 C CG  . GLU B 27  ? 1.5712 0.7461 1.1622 -0.4725 0.1986  -0.1232 15  GLU B CG  
2765 C CD  . GLU B 27  ? 1.6179 0.8931 1.2482 -0.5081 0.2073  -0.1166 15  GLU B CD  
2766 O OE1 . GLU B 27  ? 1.5688 0.9700 1.2604 -0.5093 0.1961  -0.1363 15  GLU B OE1 
2767 O OE2 . GLU B 27  ? 1.6772 0.9047 1.2739 -0.5320 0.2255  -0.0911 15  GLU B OE2 
2768 N N   . LEU B 28  ? 1.2778 0.6602 0.9703 -0.3496 0.1472  -0.1264 16  LEU B N   
2769 C CA  . LEU B 28  ? 1.2475 0.6365 0.9388 -0.2896 0.1347  -0.1008 16  LEU B CA  
2770 C C   . LEU B 28  ? 1.1726 0.6421 0.9038 -0.2525 0.1152  -0.1154 16  LEU B C   
2771 O O   . LEU B 28  ? 1.1418 0.6781 0.9066 -0.2725 0.1103  -0.1415 16  LEU B O   
2772 C CB  . LEU B 28  ? 1.2265 0.6506 0.9250 -0.2880 0.1390  -0.0707 16  LEU B CB  
2773 N N   . THR B 29  ? 1.1406 0.6039 0.8653 -0.1995 0.1044  -0.0992 17  THR B N   
2774 C CA  . THR B 29  ? 1.0759 0.6087 0.8319 -0.1649 0.0884  -0.1092 17  THR B CA  
2775 C C   . THR B 29  ? 0.9887 0.6281 0.7925 -0.1745 0.0819  -0.1087 17  THR B C   
2776 O O   . THR B 29  ? 0.9735 0.6348 0.7845 -0.1772 0.0845  -0.0886 17  THR B O   
2777 C CB  . THR B 29  ? 1.0940 0.6035 0.8334 -0.1117 0.0808  -0.0902 17  THR B CB  
2778 O OG1 . THR B 29  ? 1.1760 0.5792 0.8653 -0.1000 0.0873  -0.0887 17  THR B OG1 
2779 C CG2 . THR B 29  ? 1.0549 0.6279 0.8204 -0.0797 0.0675  -0.1019 17  THR B CG2 
2780 N N   . PRO B 30  ? 0.9302 0.6339 0.7629 -0.1788 0.0734  -0.1314 18  PRO B N   
2781 C CA  . PRO B 30  ? 0.8543 0.6513 0.7261 -0.1846 0.0667  -0.1311 18  PRO B CA  
2782 C C   . PRO B 30  ? 0.7935 0.6277 0.6777 -0.1495 0.0579  -0.1087 18  PRO B C   
2783 O O   . PRO B 30  ? 0.7547 0.6395 0.6596 -0.1535 0.0561  -0.1000 18  PRO B O   
2784 C CB  . PRO B 30  ? 0.8509 0.6949 0.7400 -0.1917 0.0586  -0.1601 18  PRO B CB  
2785 C CG  . PRO B 30  ? 0.9140 0.6865 0.7742 -0.2059 0.0651  -0.1799 18  PRO B CG  
2786 C CD  . PRO B 30  ? 0.9357 0.6285 0.7627 -0.1783 0.0695  -0.1593 18  PRO B CD  
2787 N N   . GLY B 31  ? 0.7811 0.5909 0.6520 -0.1160 0.0529  -0.1013 19  GLY B N   
2788 C CA  . GLY B 31  ? 0.7294 0.5738 0.6109 -0.0872 0.0453  -0.0826 19  GLY B CA  
2789 C C   . GLY B 31  ? 0.7176 0.5276 0.5801 -0.0539 0.0432  -0.0730 19  GLY B C   
2790 O O   . GLY B 31  ? 0.7544 0.5317 0.6014 -0.0426 0.0436  -0.0860 19  GLY B O   
2791 N N   . ILE B 32  ? 0.6649 0.4853 0.5279 -0.0368 0.0406  -0.0523 20  ILE B N   
2792 C CA  . ILE B 32  ? 0.6439 0.4516 0.4944 -0.0025 0.0366  -0.0435 20  ILE B CA  
2793 C C   . ILE B 32  ? 0.5686 0.4421 0.4427 0.0086  0.0287  -0.0353 20  ILE B C   
2794 O O   . ILE B 32  ? 0.5573 0.4486 0.4384 0.0009  0.0281  -0.0223 20  ILE B O   
2795 C CB  . ILE B 32  ? 0.6893 0.4360 0.5088 0.0082  0.0411  -0.0265 20  ILE B CB  
2796 C CG1 . ILE B 32  ? 0.7556 0.4247 0.5456 -0.0116 0.0515  -0.0332 20  ILE B CG1 
2797 C CG2 . ILE B 32  ? 0.6987 0.4436 0.5073 0.0502  0.0344  -0.0208 20  ILE B CG2 
2798 C CD1 . ILE B 32  ? 0.8216 0.4129 0.5690 -0.0006 0.0574  -0.0144 20  ILE B CD1 
2799 N N   . PHE B 33  ? 0.5183 0.4275 0.4029 0.0236  0.0240  -0.0440 21  PHE B N   
2800 C CA  . PHE B 33  ? 0.4512 0.4180 0.3545 0.0282  0.0184  -0.0370 21  PHE B CA  
2801 C C   . PHE B 33  ? 0.4228 0.4038 0.3235 0.0548  0.0152  -0.0298 21  PHE B C   
2802 O O   . PHE B 33  ? 0.4345 0.4126 0.3286 0.0764  0.0151  -0.0387 21  PHE B O   
2803 C CB  . PHE B 33  ? 0.4215 0.4259 0.3363 0.0229  0.0167  -0.0495 21  PHE B CB  
2804 C CG  . PHE B 33  ? 0.3873 0.4414 0.3149 0.0225  0.0131  -0.0419 21  PHE B CG  
2805 C CD1 . PHE B 33  ? 0.3758 0.4610 0.3064 0.0379  0.0127  -0.0424 21  PHE B CD1 
2806 C CD2 . PHE B 33  ? 0.3728 0.4424 0.3072 0.0061  0.0110  -0.0361 21  PHE B CD2 
2807 C CE1 . PHE B 33  ? 0.3556 0.4825 0.2948 0.0304  0.0116  -0.0360 21  PHE B CE1 
2808 C CE2 . PHE B 33  ? 0.3539 0.4555 0.2927 0.0035  0.0088  -0.0290 21  PHE B CE2 
2809 C CZ  . PHE B 33  ? 0.3413 0.4697 0.2818 0.0124  0.0099  -0.0287 21  PHE B CZ  
2810 N N   . LYS B 34  ? 0.3830 0.3854 0.2894 0.0543  0.0119  -0.0162 22  LYS B N   
2811 C CA  . LYS B 34  ? 0.3565 0.3872 0.2642 0.0774  0.0072  -0.0111 22  LYS B CA  
2812 C C   . LYS B 34  ? 0.2989 0.3917 0.2272 0.0680  0.0045  -0.0119 22  LYS B C   
2813 O O   . LYS B 34  ? 0.2886 0.4210 0.2249 0.0814  0.0036  -0.0184 22  LYS B O   
2814 C CB  . LYS B 34  ? 0.3887 0.3969 0.2821 0.0854  0.0049  0.0038  22  LYS B CB  
2815 C CG  . LYS B 34  ? 0.4794 0.4197 0.3433 0.0997  0.0083  0.0077  22  LYS B CG  
2816 C CD  . LYS B 34  ? 0.5504 0.4816 0.4039 0.1334  0.0065  -0.0012 22  LYS B CD  
2817 C CE  . LYS B 34  ? 0.6538 0.5013 0.4701 0.1474  0.0106  0.0027  22  LYS B CE  
2818 N NZ  . LYS B 34  ? 0.6978 0.5323 0.5011 0.1852  0.0083  -0.0084 22  LYS B NZ  
2819 N N   . LYS B 35  ? 0.2646 0.3644 0.1992 0.0448  0.0042  -0.0062 23  LYS B N   
2820 C CA  . LYS B 35  ? 0.2275 0.3708 0.1740 0.0316  0.0028  -0.0054 23  LYS B CA  
2821 C C   . LYS B 35  ? 0.2205 0.3535 0.1667 0.0105  0.0042  -0.0048 23  LYS B C   
2822 O O   . LYS B 35  ? 0.2293 0.3335 0.1712 0.0044  0.0047  -0.0030 23  LYS B O   
2823 C CB  . LYS B 35  ? 0.2250 0.3852 0.1732 0.0296  -0.0017 0.0025  23  LYS B CB  
2824 C CG  . LYS B 35  ? 0.2450 0.4407 0.1974 0.0499  -0.0057 0.0011  23  LYS B CG  
2825 C CD  . LYS B 35  ? 0.2738 0.4749 0.2221 0.0498  -0.0114 0.0086  23  LYS B CD  
2826 C CE  . LYS B 35  ? 0.2748 0.5311 0.2318 0.0655  -0.0176 0.0053  23  LYS B CE  
2827 N NZ  . LYS B 35  ? 0.2852 0.5400 0.2317 0.0739  -0.0246 0.0128  23  LYS B NZ  
2828 N N   . GLY B 36  ? 0.2029 0.3618 0.1518 -0.0002 0.0052  -0.0054 24  GLY B N   
2829 C CA  . GLY B 36  ? 0.2102 0.3575 0.1529 -0.0148 0.0052  -0.0029 24  GLY B CA  
2830 C C   . GLY B 36  ? 0.2137 0.3827 0.1518 -0.0274 0.0074  0.0000  24  GLY B C   
2831 O O   . GLY B 36  ? 0.2114 0.4139 0.1552 -0.0271 0.0106  -0.0028 24  GLY B O   
2832 N N   . ILE B 37  ? 0.2234 0.3733 0.1491 -0.0384 0.0064  0.0056  25  ILE B N   
2833 C CA  . ILE B 37  ? 0.2384 0.3921 0.1497 -0.0539 0.0097  0.0116  25  ILE B CA  
2834 C C   . ILE B 37  ? 0.2638 0.3914 0.1561 -0.0517 0.0077  0.0156  25  ILE B C   
2835 O O   . ILE B 37  ? 0.2585 0.3751 0.1548 -0.0398 0.0032  0.0112  25  ILE B O   
2836 C CB  . ILE B 37  ? 0.2464 0.3922 0.1528 -0.0701 0.0093  0.0165  25  ILE B CB  
2837 C CG1 . ILE B 37  ? 0.2605 0.3696 0.1601 -0.0656 0.0038  0.0185  25  ILE B CG1 
2838 C CG2 . ILE B 37  ? 0.2318 0.4160 0.1561 -0.0726 0.0098  0.0117  25  ILE B CG2 
2839 C CD1 . ILE B 37  ? 0.2831 0.3734 0.1696 -0.0812 0.0033  0.0212  25  ILE B CD1 
2840 N N   . GLU B 38  ? 0.2901 0.4095 0.1598 -0.0632 0.0111  0.0238  26  GLU B N   
2841 C CA  . GLU B 38  ? 0.3264 0.4181 0.1717 -0.0564 0.0074  0.0299  26  GLU B CA  
2842 C C   . GLU B 38  ? 0.3403 0.3940 0.1749 -0.0559 0.0026  0.0347  26  GLU B C   
2843 O O   . GLU B 38  ? 0.3554 0.3922 0.1804 -0.0720 0.0058  0.0394  26  GLU B O   
2844 C CB  . GLU B 38  ? 0.3828 0.4735 0.2003 -0.0665 0.0134  0.0394  26  GLU B CB  
2845 C CG  . GLU B 38  ? 0.4623 0.5903 0.2878 -0.0585 0.0159  0.0312  26  GLU B CG  
2846 C CD  . GLU B 38  ? 0.6349 0.7746 0.4352 -0.0701 0.0246  0.0393  26  GLU B CD  
2847 O OE1 . GLU B 38  ? 0.6998 0.8206 0.4696 -0.0636 0.0220  0.0475  26  GLU B OE1 
2848 O OE2 . GLU B 38  ? 0.6756 0.8484 0.4859 -0.0847 0.0342  0.0369  26  GLU B OE2 
2849 N N   . ILE B 39  ? 0.3350 0.3815 0.1749 -0.0385 -0.0045 0.0299  27  ILE B N   
2850 C CA  . ILE B 39  ? 0.3474 0.3654 0.1800 -0.0320 -0.0091 0.0307  27  ILE B CA  
2851 C C   . ILE B 39  ? 0.3636 0.3801 0.1906 -0.0100 -0.0168 0.0276  27  ILE B C   
2852 O O   . ILE B 39  ? 0.3521 0.3989 0.1947 -0.0028 -0.0189 0.0198  27  ILE B O   
2853 C CB  . ILE B 39  ? 0.3288 0.3607 0.1877 -0.0351 -0.0083 0.0231  27  ILE B CB  
2854 C CG1 . ILE B 39  ? 0.3470 0.3551 0.1987 -0.0283 -0.0119 0.0217  27  ILE B CG1 
2855 C CG2 . ILE B 39  ? 0.3046 0.3667 0.1899 -0.0283 -0.0081 0.0142  27  ILE B CG2 
2856 C CD1 . ILE B 39  ? 0.3535 0.3683 0.2182 -0.0364 -0.0100 0.0182  27  ILE B CD1 
2857 N N   . THR B 40  ? 0.3926 0.3752 0.1958 0.0014  -0.0214 0.0322  28  THR B N   
2858 C CA  . THR B 40  ? 0.4097 0.3990 0.2097 0.0273  -0.0300 0.0272  28  THR B CA  
2859 C C   . THR B 40  ? 0.4224 0.3944 0.2221 0.0371  -0.0322 0.0225  28  THR B C   
2860 O O   . THR B 40  ? 0.4435 0.3759 0.2250 0.0279  -0.0292 0.0275  28  THR B O   
2861 C CB  . THR B 40  ? 0.4649 0.4327 0.2276 0.0444  -0.0360 0.0372  28  THR B CB  
2862 O OG1 . THR B 40  ? 0.5324 0.4381 0.2543 0.0432  -0.0347 0.0503  28  THR B OG1 
2863 C CG2 . THR B 40  ? 0.4611 0.4519 0.2212 0.0371  -0.0340 0.0404  28  THR B CG2 
2864 N N   . ILE B 41  ? 0.4142 0.4193 0.2337 0.0538  -0.0366 0.0108  29  ILE B N   
2865 C CA  . ILE B 41  ? 0.4356 0.4337 0.2555 0.0667  -0.0380 0.0039  29  ILE B CA  
2866 C C   . ILE B 41  ? 0.4623 0.4849 0.2805 0.0990  -0.0471 -0.0042 29  ILE B C   
2867 O O   . ILE B 41  ? 0.4421 0.5107 0.2782 0.1036  -0.0507 -0.0108 29  ILE B O   
2868 C CB  . ILE B 41  ? 0.4095 0.4329 0.2604 0.0497  -0.0307 -0.0040 29  ILE B CB  
2869 C CG1 . ILE B 41  ? 0.4247 0.4310 0.2670 0.0593  -0.0304 -0.0095 29  ILE B CG1 
2870 C CG2 . ILE B 41  ? 0.3783 0.4567 0.2630 0.0465  -0.0291 -0.0145 29  ILE B CG2 
2871 C CD1 . ILE B 41  ? 0.4211 0.4397 0.2811 0.0419  -0.0234 -0.0128 29  ILE B CD1 
2872 N N   . ASP B 42  ? 0.5121 0.5043 0.3064 0.1228  -0.0515 -0.0053 30  ASP B N   
2873 C CA  . ASP B 42  ? 0.5379 0.5581 0.3302 0.1602  -0.0610 -0.0149 30  ASP B CA  
2874 C C   . ASP B 42  ? 0.5361 0.5651 0.3390 0.1690  -0.0577 -0.0277 30  ASP B C   
2875 O O   . ASP B 42  ? 0.5652 0.5358 0.3382 0.1746  -0.0569 -0.0243 30  ASP B O   
2876 C CB  . ASP B 42  ? 0.6341 0.5970 0.3748 0.1897  -0.0703 -0.0026 30  ASP B CB  
2877 C CG  . ASP B 42  ? 0.7488 0.7454 0.4837 0.2363  -0.0832 -0.0116 30  ASP B CG  
2878 O OD1 . ASP B 42  ? 0.7300 0.8079 0.5073 0.2411  -0.0846 -0.0293 30  ASP B OD1 
2879 O OD2 . ASP B 42  ? 0.8364 0.7792 0.5227 0.2679  -0.0919 -0.0009 30  ASP B OD2 
2880 N N   . LEU B 43  ? 0.5001 0.6004 0.3433 0.1665  -0.0544 -0.0431 31  LEU B N   
2881 C CA  . LEU B 43  ? 0.5037 0.6213 0.3576 0.1728  -0.0491 -0.0556 31  LEU B CA  
2882 C C   . LEU B 43  ? 0.5371 0.6661 0.3763 0.2196  -0.0579 -0.0673 31  LEU B C   
2883 O O   . LEU B 43  ? 0.5388 0.6800 0.3819 0.2300  -0.0535 -0.0793 31  LEU B O   
2884 C CB  . LEU B 43  ? 0.4621 0.6461 0.3598 0.1464  -0.0389 -0.0655 31  LEU B CB  
2885 C CG  . LEU B 43  ? 0.4763 0.6431 0.3843 0.1064  -0.0302 -0.0549 31  LEU B CG  
2886 C CD1 . LEU B 43  ? 0.4529 0.6742 0.3956 0.0827  -0.0197 -0.0633 31  LEU B CD1 
2887 C CD2 . LEU B 43  ? 0.5034 0.6116 0.3888 0.0957  -0.0265 -0.0457 31  LEU B CD2 
2888 N N   . GLU B 44  ? 0.5611 0.6848 0.3796 0.2512  -0.0705 -0.0638 32  GLU B N   
2889 C CA  . GLU B 44  ? 0.5961 0.7218 0.3933 0.3034  -0.0808 -0.0733 32  GLU B CA  
2890 C C   . GLU B 44  ? 0.6545 0.6704 0.3947 0.3165  -0.0825 -0.0613 32  GLU B C   
2891 O O   . GLU B 44  ? 0.6780 0.6723 0.4030 0.3391  -0.0818 -0.0720 32  GLU B O   
2892 C CB  . GLU B 44  ? 0.6425 0.8084 0.4362 0.3363  -0.0953 -0.0739 32  GLU B CB  
2893 C CG  . GLU B 44  ? 0.6844 0.9610 0.5329 0.3216  -0.0945 -0.0899 32  GLU B CG  
2894 C CD  . GLU B 44  ? 0.8122 1.0972 0.6622 0.3044  -0.0995 -0.0803 32  GLU B CD  
2895 O OE1 . GLU B 44  ? 0.8312 1.0991 0.6941 0.2594  -0.0892 -0.0724 32  GLU B OE1 
2896 O OE2 . GLU B 44  ? 0.8620 1.1713 0.6978 0.3389  -0.1142 -0.0812 32  GLU B OE2 
2897 N N   . GLU B 45  ? 0.6775 0.6242 0.3853 0.2990  -0.0833 -0.0405 33  GLU B N   
2898 C CA  . GLU B 45  ? 0.7358 0.5728 0.3875 0.2990  -0.0824 -0.0278 33  GLU B CA  
2899 C C   . GLU B 45  ? 0.7152 0.5261 0.3757 0.2581  -0.0700 -0.0308 33  GLU B C   
2900 O O   . GLU B 45  ? 0.7700 0.4980 0.3885 0.2565  -0.0684 -0.0278 33  GLU B O   
2901 C CB  . GLU B 45  ? 0.8174 0.6007 0.4343 0.2868  -0.0847 -0.0045 33  GLU B CB  
2902 C CG  . GLU B 45  ? 0.9881 0.7107 0.5460 0.3335  -0.0968 0.0063  33  GLU B CG  
2903 C CD  . GLU B 45  ? 1.1847 0.7991 0.6818 0.3147  -0.0931 0.0304  33  GLU B CD  
2904 O OE1 . GLU B 45  ? 1.2156 0.8339 0.7049 0.3005  -0.0933 0.0468  33  GLU B OE1 
2905 O OE2 . GLU B 45  ? 1.2715 0.7976 0.7271 0.3123  -0.0892 0.0317  33  GLU B OE2 
2906 N N   . MET B 46  ? 0.6385 0.5176 0.3501 0.2256  -0.0616 -0.0370 34  MET B N   
2907 C CA  . MET B 46  ? 0.6062 0.4780 0.3311 0.1882  -0.0512 -0.0391 34  MET B CA  
2908 C C   . MET B 46  ? 0.6234 0.4250 0.3187 0.1582  -0.0484 -0.0237 34  MET B C   
2909 O O   . MET B 46  ? 0.6546 0.4049 0.3268 0.1452  -0.0451 -0.0264 34  MET B O   
2910 C CB  . MET B 46  ? 0.6147 0.4864 0.3365 0.2031  -0.0486 -0.0563 34  MET B CB  
2911 C CG  . MET B 46  ? 0.6032 0.5656 0.3662 0.2182  -0.0464 -0.0721 34  MET B CG  
2912 S SD  . MET B 46  ? 0.6228 0.6597 0.4393 0.1741  -0.0350 -0.0706 34  MET B SD  
2913 C CE  . MET B 46  ? 0.5912 0.6128 0.4022 0.1569  -0.0259 -0.0776 34  MET B CE  
2914 N N   . VAL B 47  ? 0.6049 0.4069 0.2990 0.1469  -0.0496 -0.0091 35  VAL B N   
2915 C CA  . VAL B 47  ? 0.6247 0.3756 0.2950 0.1155  -0.0452 0.0060  35  VAL B CA  
2916 C C   . VAL B 47  ? 0.5667 0.3709 0.2736 0.0871  -0.0403 0.0117  35  VAL B C   
2917 O O   . VAL B 47  ? 0.5358 0.3981 0.2726 0.0964  -0.0427 0.0081  35  VAL B O   
2918 C CB  . VAL B 47  ? 0.6978 0.3749 0.3122 0.1307  -0.0498 0.0211  35  VAL B CB  
2919 C CG1 . VAL B 47  ? 0.7694 0.3689 0.3364 0.1538  -0.0530 0.0164  35  VAL B CG1 
2920 C CG2 . VAL B 47  ? 0.6910 0.4028 0.3073 0.1607  -0.0583 0.0265  35  VAL B CG2 
2921 N N   . CYS B 48  ? 0.5537 0.3388 0.2570 0.0524  -0.0335 0.0186  36  CYS B N   
2922 C CA  . CYS B 48  ? 0.5076 0.3375 0.2407 0.0282  -0.0286 0.0231  36  CYS B CA  
2923 C C   . CYS B 48  ? 0.5193 0.3134 0.2263 0.0030  -0.0235 0.0361  36  CYS B C   
2924 O O   . CYS B 48  ? 0.5600 0.2988 0.2348 -0.0100 -0.0210 0.0387  36  CYS B O   
2925 C CB  . CYS B 48  ? 0.4713 0.3427 0.2408 0.0115  -0.0242 0.0140  36  CYS B CB  
2926 S SG  . CYS B 48  ? 0.4124 0.3388 0.2182 -0.0068 -0.0196 0.0170  36  CYS B SG  
2927 N N   . TYR B 49  ? 0.4911 0.3170 0.2106 -0.0060 -0.0210 0.0427  37  TYR B N   
2928 C CA  . TYR B 49  ? 0.5012 0.3057 0.1981 -0.0311 -0.0141 0.0548  37  TYR B CA  
2929 C C   . TYR B 49  ? 0.4583 0.3194 0.1913 -0.0534 -0.0079 0.0516  37  TYR B C   
2930 O O   . TYR B 49  ? 0.4304 0.3359 0.1882 -0.0431 -0.0093 0.0485  37  TYR B O   
2931 C CB  . TYR B 49  ? 0.5211 0.3062 0.1866 -0.0148 -0.0170 0.0675  37  TYR B CB  
2932 C CG  . TYR B 49  ? 0.5753 0.2973 0.1959 0.0127  -0.0241 0.0733  37  TYR B CG  
2933 C CD1 . TYR B 49  ? 0.6422 0.2842 0.2125 0.0000  -0.0199 0.0833  37  TYR B CD1 
2934 C CD2 . TYR B 49  ? 0.5785 0.3206 0.2047 0.0520  -0.0350 0.0677  37  TYR B CD2 
2935 C CE1 . TYR B 49  ? 0.7042 0.2778 0.2261 0.0305  -0.0269 0.0893  37  TYR B CE1 
2936 C CE2 . TYR B 49  ? 0.6330 0.3207 0.2165 0.0846  -0.0429 0.0722  37  TYR B CE2 
2937 C CZ  . TYR B 49  ? 0.7088 0.3072 0.2378 0.0762  -0.0391 0.0837  37  TYR B CZ  
2938 O OH  . TYR B 49  ? 0.7901 0.3243 0.2706 0.1134  -0.0474 0.0883  37  TYR B OH  
2939 N N   . HIS B 50  ? 0.4571 0.3173 0.1912 -0.0829 -0.0012 0.0507  38  HIS B N   
2940 C CA  . HIS B 50  ? 0.4303 0.3464 0.1953 -0.1012 0.0044  0.0473  38  HIS B CA  
2941 C C   . HIS B 50  ? 0.4654 0.3757 0.2193 -0.1369 0.0123  0.0484  38  HIS B C   
2942 O O   . HIS B 50  ? 0.4959 0.3604 0.2258 -0.1499 0.0125  0.0473  38  HIS B O   
2943 C CB  . HIS B 50  ? 0.3828 0.3457 0.1889 -0.0897 0.0007  0.0360  38  HIS B CB  
2944 C CG  . HIS B 50  ? 0.3705 0.3283 0.1823 -0.0958 -0.0014 0.0283  38  HIS B CG  
2945 N ND1 . HIS B 50  ? 0.3711 0.3528 0.1924 -0.1188 0.0015  0.0238  38  HIS B ND1 
2946 C CD2 . HIS B 50  ? 0.3807 0.3203 0.1905 -0.0807 -0.0064 0.0228  38  HIS B CD2 
2947 C CE1 . HIS B 50  ? 0.3762 0.3493 0.1983 -0.1171 -0.0025 0.0163  38  HIS B CE1 
2948 N NE2 . HIS B 50  ? 0.3872 0.3333 0.2016 -0.0947 -0.0065 0.0156  38  HIS B NE2 
2949 N N   . SER B 51  ? 0.4602 0.4186 0.2302 -0.1536 0.0195  0.0488  39  SER B N   
2950 C CA  . SER B 51  ? 0.4774 0.4534 0.2457 -0.1911 0.0283  0.0468  39  SER B CA  
2951 C C   . SER B 51  ? 0.5490 0.4603 0.2680 -0.2187 0.0361  0.0580  39  SER B C   
2952 O O   . SER B 51  ? 0.5750 0.4780 0.2849 -0.2537 0.0419  0.0536  39  SER B O   
2953 C CB  . SER B 51  ? 0.4690 0.4697 0.2607 -0.1990 0.0239  0.0332  39  SER B CB  
2954 O OG  . SER B 51  ? 0.4603 0.5034 0.2871 -0.1709 0.0166  0.0264  39  SER B OG  
2955 N N   . GLY B 52  ? 0.5806 0.4440 0.2649 -0.2034 0.0360  0.0721  40  GLY B N   
2956 C CA  . GLY B 52  ? 0.6476 0.4331 0.2743 -0.2235 0.0430  0.0866  40  GLY B CA  
2957 C C   . GLY B 52  ? 0.6974 0.4044 0.2929 -0.2209 0.0375  0.0842  40  GLY B C   
2958 O O   . GLY B 52  ? 0.7591 0.3907 0.3030 -0.2432 0.0442  0.0940  40  GLY B O   
2959 N N   . LEU B 53  ? 0.6751 0.3945 0.2973 -0.1933 0.0262  0.0711  41  LEU B N   
2960 C CA  . LEU B 53  ? 0.7162 0.3700 0.3126 -0.1864 0.0206  0.0646  41  LEU B CA  
2961 C C   . LEU B 53  ? 0.7152 0.3514 0.3104 -0.1364 0.0086  0.0631  41  LEU B C   
2962 O O   . LEU B 53  ? 0.6751 0.3642 0.3017 -0.1106 0.0036  0.0629  41  LEU B O   
2963 C CB  . LEU B 53  ? 0.6990 0.3898 0.3260 -0.2089 0.0203  0.0460  41  LEU B CB  
2964 C CG  . LEU B 53  ? 0.7321 0.4370 0.3561 -0.2619 0.0313  0.0427  41  LEU B CG  
2965 C CD1 . LEU B 53  ? 0.6945 0.4694 0.3623 -0.2752 0.0278  0.0233  41  LEU B CD1 
2966 C CD2 . LEU B 53  ? 0.8080 0.4126 0.3700 -0.2910 0.0382  0.0477  41  LEU B CD2 
2967 N N   . THR B 54  ? 0.7597 0.3227 0.3176 -0.1233 0.0043  0.0600  42  THR B N   
2968 C CA  . THR B 54  ? 0.7645 0.3190 0.3225 -0.0752 -0.0066 0.0553  42  THR B CA  
2969 C C   . THR B 54  ? 0.7370 0.3120 0.3203 -0.0717 -0.0102 0.0355  42  THR B C   
2970 O O   . THR B 54  ? 0.7710 0.3041 0.3333 -0.0947 -0.0073 0.0272  42  THR B O   
2971 C CB  . THR B 54  ? 0.8586 0.3184 0.3529 -0.0523 -0.0098 0.0658  42  THR B CB  
2972 O OG1 . THR B 54  ? 0.8992 0.3448 0.3677 -0.0544 -0.0065 0.0863  42  THR B OG1 
2973 C CG2 . THR B 54  ? 0.8604 0.3221 0.3571 0.0008  -0.0216 0.0578  42  THR B CG2 
2974 N N   . TRP B 55  ? 0.6756 0.3145 0.3012 -0.0462 -0.0157 0.0273  43  TRP B N   
2975 C CA  . TRP B 55  ? 0.6448 0.3128 0.2953 -0.0428 -0.0178 0.0104  43  TRP B CA  
2976 C C   . TRP B 55  ? 0.6418 0.3050 0.2891 -0.0013 -0.0244 0.0023  43  TRP B C   
2977 O O   . TRP B 55  ? 0.6214 0.3127 0.2810 0.0248  -0.0282 0.0067  43  TRP B O   
2978 C CB  . TRP B 55  ? 0.5842 0.3362 0.2873 -0.0532 -0.0161 0.0078  43  TRP B CB  
2979 C CG  . TRP B 55  ? 0.5761 0.3509 0.2893 -0.0858 -0.0104 0.0148  43  TRP B CG  
2980 C CD1 . TRP B 55  ? 0.5744 0.3668 0.2923 -0.0887 -0.0075 0.0266  43  TRP B CD1 
2981 C CD2 . TRP B 55  ? 0.5765 0.3611 0.2929 -0.1200 -0.0066 0.0086  43  TRP B CD2 
2982 N NE1 . TRP B 55  ? 0.5689 0.3836 0.2943 -0.1217 -0.0010 0.0282  43  TRP B NE1 
2983 C CE2 . TRP B 55  ? 0.5678 0.3818 0.2944 -0.1417 -0.0008 0.0170  43  TRP B CE2 
2984 C CE3 . TRP B 55  ? 0.5972 0.3760 0.3101 -0.1341 -0.0080 -0.0052 43  TRP B CE3 
2985 C CZ2 . TRP B 55  ? 0.5674 0.4110 0.3038 -0.1764 0.0037  0.0116  43  TRP B CZ2 
2986 C CZ3 . TRP B 55  ? 0.6049 0.4100 0.3258 -0.1699 -0.0047 -0.0106 43  TRP B CZ3 
2987 C CH2 . TRP B 55  ? 0.5860 0.4248 0.3194 -0.1909 0.0012  -0.0023 43  TRP B CH2 
2988 N N   . LYS B 56  ? 0.6587 0.2958 0.2923 0.0045  -0.0257 -0.0121 44  LYS B N   
2989 C CA  . LYS B 56  ? 0.6566 0.2988 0.2893 0.0447  -0.0306 -0.0234 44  LYS B CA  
2990 C C   . LYS B 56  ? 0.5877 0.3141 0.2703 0.0458  -0.0289 -0.0313 44  LYS B C   
2991 O O   . LYS B 56  ? 0.5649 0.3145 0.2633 0.0210  -0.0255 -0.0361 44  LYS B O   
2992 C CB  . LYS B 56  ? 0.7346 0.3084 0.3262 0.0512  -0.0317 -0.0374 44  LYS B CB  
2993 C CG  . LYS B 56  ? 0.8225 0.3937 0.4045 0.1004  -0.0371 -0.0493 44  LYS B CG  
2994 C CD  . LYS B 56  ? 0.9281 0.4716 0.4865 0.1356  -0.0434 -0.0372 44  LYS B CD  
2995 C CE  . LYS B 56  ? 0.9634 0.5443 0.5312 0.1870  -0.0496 -0.0488 44  LYS B CE  
2996 N NZ  . LYS B 56  ? 0.9773 0.5856 0.5511 0.2116  -0.0560 -0.0363 44  LYS B NZ  
2997 N N   . VAL B 57  ? 0.5591 0.3316 0.2640 0.0734  -0.0312 -0.0327 45  VAL B N   
2998 C CA  . VAL B 57  ? 0.5153 0.3619 0.2631 0.0715  -0.0274 -0.0386 45  VAL B CA  
2999 C C   . VAL B 57  ? 0.5175 0.3797 0.2650 0.0918  -0.0263 -0.0556 45  VAL B C   
3000 O O   . VAL B 57  ? 0.5379 0.3777 0.2643 0.1236  -0.0305 -0.0641 45  VAL B O   
3001 C CB  . VAL B 57  ? 0.4897 0.3863 0.2658 0.0801  -0.0284 -0.0324 45  VAL B CB  
3002 C CG1 . VAL B 57  ? 0.4485 0.4115 0.2641 0.0709  -0.0224 -0.0369 45  VAL B CG1 
3003 C CG2 . VAL B 57  ? 0.4989 0.3807 0.2715 0.0623  -0.0290 -0.0175 45  VAL B CG2 
3004 N N   . LYS B 58  ? 0.4945 0.3965 0.2631 0.0761  -0.0206 -0.0603 46  LYS B N   
3005 C CA  . LYS B 58  ? 0.4948 0.4232 0.2653 0.0922  -0.0171 -0.0759 46  LYS B CA  
3006 C C   . LYS B 58  ? 0.4486 0.4433 0.2538 0.0777  -0.0092 -0.0729 46  LYS B C   
3007 O O   . LYS B 58  ? 0.4353 0.4353 0.2498 0.0523  -0.0072 -0.0626 46  LYS B O   
3008 C CB  . LYS B 58  ? 0.5560 0.4409 0.2962 0.0864  -0.0177 -0.0872 46  LYS B CB  
3009 C CG  . LYS B 58  ? 0.6097 0.5182 0.3456 0.1080  -0.0142 -0.1058 46  LYS B CG  
3010 C CD  . LYS B 58  ? 0.6884 0.5714 0.4012 0.0936  -0.0137 -0.1174 46  LYS B CD  
3011 N N   . GLN B 59  ? 0.4269 0.4720 0.2495 0.0938  -0.0043 -0.0815 47  GLN B N   
3012 C CA  . GLN B 59  ? 0.3982 0.4982 0.2473 0.0766  0.0057  -0.0778 47  GLN B CA  
3013 C C   . GLN B 59  ? 0.4079 0.5147 0.2448 0.0716  0.0116  -0.0846 47  GLN B C   
3014 O O   . GLN B 59  ? 0.4276 0.5390 0.2518 0.0924  0.0125  -0.1005 47  GLN B O   
3015 C CB  . GLN B 59  ? 0.3921 0.5504 0.2657 0.0895  0.0103  -0.0856 47  GLN B CB  
3016 C CG  . GLN B 59  ? 0.3944 0.5935 0.2947 0.0628  0.0198  -0.0766 47  GLN B CG  
3017 C CD  . GLN B 59  ? 0.4126 0.6700 0.3397 0.0681  0.0234  -0.0853 47  GLN B CD  
3018 O OE1 . GLN B 59  ? 0.4451 0.7278 0.3744 0.0963  0.0191  -0.0997 47  GLN B OE1 
3019 N NE2 . GLN B 59  ? 0.3846 0.6658 0.3315 0.0418  0.0309  -0.0784 47  GLN B NE2 
3020 N N   . LEU B 60  ? 0.3945 0.5026 0.2323 0.0476  0.0150  -0.0734 48  LEU B N   
3021 C CA  . LEU B 60  ? 0.3982 0.5164 0.2211 0.0428  0.0199  -0.0781 48  LEU B CA  
3022 C C   . LEU B 60  ? 0.3634 0.5346 0.2000 0.0378  0.0335  -0.0762 48  LEU B C   
3023 O O   . LEU B 60  ? 0.3644 0.5599 0.1914 0.0465  0.0402  -0.0880 48  LEU B O   
3024 C CB  . LEU B 60  ? 0.4135 0.5102 0.2264 0.0232  0.0151  -0.0673 48  LEU B CB  
3025 C CG  . LEU B 60  ? 0.4560 0.5072 0.2587 0.0184  0.0040  -0.0677 48  LEU B CG  
3026 C CD1 . LEU B 60  ? 0.4692 0.5192 0.2668 -0.0007 -0.0002 -0.0604 48  LEU B CD1 
3027 C CD2 . LEU B 60  ? 0.4887 0.5036 0.2664 0.0327  -0.0006 -0.0859 48  LEU B CD2 
3028 N N   . THR B 61  ? 0.3382 0.5251 0.1944 0.0219  0.0388  -0.0622 49  THR B N   
3029 C CA  . THR B 61  ? 0.3240 0.5544 0.1920 0.0093  0.0537  -0.0585 49  THR B CA  
3030 C C   . THR B 61  ? 0.3054 0.5556 0.2016 0.0036  0.0555  -0.0577 49  THR B C   
3031 O O   . THR B 61  ? 0.3020 0.5309 0.2051 0.0119  0.0445  -0.0581 49  THR B O   
3032 C CB  . THR B 61  ? 0.3519 0.5725 0.2042 -0.0106 0.0603  -0.0406 49  THR B CB  
3033 O OG1 . THR B 61  ? 0.3707 0.5656 0.2301 -0.0231 0.0569  -0.0248 49  THR B OG1 
3034 C CG2 . THR B 61  ? 0.3724 0.5746 0.1981 -0.0048 0.0540  -0.0416 49  THR B CG2 
3035 N N   . ASN B 62  ? 0.2961 0.5873 0.2063 -0.0131 0.0697  -0.0573 50  ASN B N   
3036 C CA  . ASN B 62  ? 0.2885 0.6045 0.2257 -0.0227 0.0715  -0.0603 50  ASN B CA  
3037 C C   . ASN B 62  ? 0.2927 0.5656 0.2316 -0.0333 0.0638  -0.0469 50  ASN B C   
3038 O O   . ASN B 62  ? 0.2896 0.5723 0.2465 -0.0318 0.0583  -0.0523 50  ASN B O   
3039 C CB  . ASN B 62  ? 0.3030 0.6636 0.2504 -0.0491 0.0905  -0.0608 50  ASN B CB  
3040 C CG  . ASN B 62  ? 0.3656 0.7867 0.3182 -0.0397 0.1002  -0.0774 50  ASN B CG  
3041 O OD1 . ASN B 62  ? 0.3914 0.8384 0.3530 -0.0099 0.0916  -0.0949 50  ASN B OD1 
3042 N ND2 . ASN B 62  ? 0.3824 0.8271 0.3267 -0.0635 0.1190  -0.0723 50  ASN B ND2 
3043 N N   . THR B 63  ? 0.2965 0.5265 0.2157 -0.0413 0.0629  -0.0308 51  THR B N   
3044 C CA  . THR B 63  ? 0.2956 0.4877 0.2140 -0.0488 0.0570  -0.0187 51  THR B CA  
3045 C C   . THR B 63  ? 0.2909 0.4483 0.1961 -0.0354 0.0436  -0.0136 51  THR B C   
3046 O O   . THR B 63  ? 0.2973 0.4285 0.1994 -0.0400 0.0396  -0.0031 51  THR B O   
3047 C CB  . THR B 63  ? 0.3342 0.5091 0.2395 -0.0700 0.0688  -0.0036 51  THR B CB  
3048 O OG1 . THR B 63  ? 0.3606 0.5298 0.2416 -0.0674 0.0726  0.0042  51  THR B OG1 
3049 C CG2 . THR B 63  ? 0.3392 0.5427 0.2568 -0.0927 0.0839  -0.0085 51  THR B CG2 
3050 N N   . LEU B 64  ? 0.2750 0.4325 0.1713 -0.0200 0.0373  -0.0225 52  LEU B N   
3051 C CA  . LEU B 64  ? 0.2745 0.4010 0.1573 -0.0146 0.0263  -0.0197 52  LEU B CA  
3052 C C   . LEU B 64  ? 0.2661 0.3788 0.1441 0.0005  0.0175  -0.0314 52  LEU B C   
3053 O O   . LEU B 64  ? 0.2637 0.3892 0.1386 0.0139  0.0191  -0.0436 52  LEU B O   
3054 C CB  . LEU B 64  ? 0.2875 0.4117 0.1503 -0.0176 0.0278  -0.0154 52  LEU B CB  
3055 C CG  . LEU B 64  ? 0.3141 0.4176 0.1643 -0.0169 0.0169  -0.0149 52  LEU B CG  
3056 C CD1 . LEU B 64  ? 0.3065 0.4010 0.1625 -0.0235 0.0129  -0.0018 52  LEU B CD1 
3057 C CD2 . LEU B 64  ? 0.3301 0.4414 0.1593 -0.0156 0.0170  -0.0189 52  LEU B CD2 
3058 N N   . TRP B 65  ? 0.2677 0.3524 0.1422 -0.0011 0.0090  -0.0273 53  TRP B N   
3059 C CA  . TRP B 65  ? 0.2848 0.3410 0.1466 0.0095  0.0013  -0.0342 53  TRP B CA  
3060 C C   . TRP B 65  ? 0.3047 0.3314 0.1513 -0.0022 -0.0044 -0.0315 53  TRP B C   
3061 O O   . TRP B 65  ? 0.2902 0.3253 0.1439 -0.0153 -0.0046 -0.0229 53  TRP B O   
3062 C CB  . TRP B 65  ? 0.2705 0.3237 0.1422 0.0148  -0.0020 -0.0308 53  TRP B CB  
3063 C CG  . TRP B 65  ? 0.2473 0.3350 0.1351 0.0266  0.0011  -0.0373 53  TRP B CG  
3064 C CD1 . TRP B 65  ? 0.2605 0.3541 0.1437 0.0497  -0.0024 -0.0479 53  TRP B CD1 
3065 C CD2 . TRP B 65  ? 0.2203 0.3436 0.1309 0.0155  0.0080  -0.0353 53  TRP B CD2 
3066 N NE1 . TRP B 65  ? 0.2426 0.3849 0.1491 0.0530  0.0013  -0.0537 53  TRP B NE1 
3067 C CE2 . TRP B 65  ? 0.2194 0.3785 0.1425 0.0288  0.0087  -0.0466 53  TRP B CE2 
3068 C CE3 . TRP B 65  ? 0.2175 0.3435 0.1365 -0.0038 0.0137  -0.0259 53  TRP B CE3 
3069 C CZ2 . TRP B 65  ? 0.2056 0.4069 0.1518 0.0168  0.0159  -0.0502 53  TRP B CZ2 
3070 C CZ3 . TRP B 65  ? 0.2176 0.3721 0.1537 -0.0142 0.0215  -0.0279 53  TRP B CZ3 
3071 C CH2 . TRP B 65  ? 0.2068 0.4004 0.1576 -0.0072 0.0231  -0.0406 53  TRP B CH2 
3072 N N   . SER B 66  ? 0.3430 0.3347 0.1678 0.0026  -0.0090 -0.0397 54  SER B N   
3073 C CA  . SER B 66  ? 0.3761 0.3393 0.1855 -0.0145 -0.0134 -0.0395 54  SER B CA  
3074 C C   . SER B 66  ? 0.4095 0.3297 0.2030 -0.0133 -0.0165 -0.0369 54  SER B C   
3075 O O   . SER B 66  ? 0.4218 0.3224 0.2044 0.0076  -0.0178 -0.0402 54  SER B O   
3076 C CB  . SER B 66  ? 0.4175 0.3691 0.2067 -0.0182 -0.0149 -0.0528 54  SER B CB  
3077 O OG  . SER B 66  ? 0.4854 0.3943 0.2486 -0.0046 -0.0166 -0.0651 54  SER B OG  
3078 N N   . LEU B 67  ? 0.4267 0.3361 0.2178 -0.0345 -0.0175 -0.0304 55  LEU B N   
3079 C CA  . LEU B 67  ? 0.4708 0.3356 0.2406 -0.0391 -0.0185 -0.0251 55  LEU B CA  
3080 C C   . LEU B 67  ? 0.5232 0.3517 0.2680 -0.0630 -0.0189 -0.0321 55  LEU B C   
3081 O O   . LEU B 67  ? 0.5083 0.3666 0.2658 -0.0862 -0.0185 -0.0338 55  LEU B O   
3082 C CB  . LEU B 67  ? 0.4548 0.3426 0.2421 -0.0493 -0.0167 -0.0123 55  LEU B CB  
3083 C CG  . LEU B 67  ? 0.4424 0.3694 0.2566 -0.0338 -0.0159 -0.0069 55  LEU B CG  
3084 C CD1 . LEU B 67  ? 0.4404 0.3745 0.2601 -0.0423 -0.0145 0.0030  55  LEU B CD1 
3085 C CD2 . LEU B 67  ? 0.4547 0.3749 0.2641 -0.0071 -0.0179 -0.0107 55  LEU B CD2 
3086 N N   . ALA B 68  ? 0.5845 0.3491 0.2923 -0.0572 -0.0201 -0.0377 56  ALA B N   
3087 C CA  . ALA B 68  ? 0.6456 0.3640 0.3234 -0.0842 -0.0196 -0.0471 56  ALA B CA  
3088 C C   . ALA B 68  ? 0.7232 0.3723 0.3641 -0.0958 -0.0171 -0.0377 56  ALA B C   
3089 O O   . ALA B 68  ? 0.7358 0.3586 0.3636 -0.0706 -0.0181 -0.0271 56  ALA B O   
3090 C CB  . ALA B 68  ? 0.6672 0.3566 0.3232 -0.0694 -0.0223 -0.0654 56  ALA B CB  
3091 N N   . GLY B 69  ? 0.7768 0.3967 0.3979 -0.1348 -0.0136 -0.0418 57  GLY B N   
3092 C CA  . GLY B 69  ? 0.8513 0.3970 0.4298 -0.1537 -0.0085 -0.0316 57  GLY B CA  
3093 C C   . GLY B 69  ? 0.9331 0.3825 0.4586 -0.1269 -0.0109 -0.0331 57  GLY B C   
3094 O O   . GLY B 69  ? 0.9532 0.3897 0.4720 -0.1022 -0.0158 -0.0488 57  GLY B O   
3095 C C1  . GOL C .   ? 0.5047 0.5351 0.5401 0.0152  0.0005  -0.0260 401 GOL A C1  
3096 O O1  . GOL C .   ? 0.5002 0.5286 0.5308 0.0140  0.0001  -0.0243 401 GOL A O1  
3097 C C2  . GOL C .   ? 0.5123 0.5458 0.5478 0.0149  0.0026  -0.0306 401 GOL A C2  
3098 O O2  . GOL C .   ? 0.5119 0.5488 0.5431 0.0136  0.0037  -0.0301 401 GOL A O2  
3099 C C3  . GOL C .   ? 0.5159 0.5506 0.5595 0.0168  0.0029  -0.0335 401 GOL A C3  
3100 O O3  . GOL C .   ? 0.5177 0.5503 0.5652 0.0174  0.0031  -0.0369 401 GOL A O3  
# 
