data_9DI9
# 
_entry.id   9DI9 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.402 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   9DI9         pdb_00009di9 10.2210/pdb9di9/pdb 
WWPDB D_1000288144 ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
_pdbx_audit_revision_history.part_number 
1 'Structure model' 1 0 2024-11-27 ? 
2 'Structure model' 1 1 2024-12-04 ? 
3 'Structure model' 1 2 2025-02-26 ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
loop_
_pdbx_audit_revision_group.ordinal 
_pdbx_audit_revision_group.revision_ordinal 
_pdbx_audit_revision_group.data_content_type 
_pdbx_audit_revision_group.group 
1 2 'Structure model' 'Database references' 
2 3 'Structure model' 'Database references' 
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 2 'Structure model' citation        
2 2 'Structure model' citation_author 
3 3 'Structure model' citation        
4 3 'Structure model' citation_author 
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1  2 'Structure model' '_citation.journal_abbrev'          
2  2 'Structure model' '_citation.journal_id_ISSN'         
3  2 'Structure model' '_citation.pdbx_database_id_DOI'    
4  2 'Structure model' '_citation.pdbx_database_id_PubMed' 
5  2 'Structure model' '_citation.title'                   
6  2 'Structure model' '_citation.year'                    
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.year'                    
11 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                        9DI9 
_pdbx_database_status.recvd_initial_deposition_date   2024-09-05 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           N 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              shenping.liu@pfizer.com 
_pdbx_contact_author.name_first         Shenping 
_pdbx_contact_author.name_last          Liu 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0001-9400-3007 
# 
_audit_author.name               'Liu, S.' 
_audit_author.pdbx_ordinal       1 
_audit_author.identifier_ORCID   0000-0001-9400-3007 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            J.Med.Chem. 
_citation.journal_id_ASTM           JMCMAR 
_citation.journal_id_CSD            0151 
_citation.journal_id_ISSN           0022-2623 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            68 
_citation.language                  ? 
_citation.page_first                2466 
_citation.page_last                 2482 
_citation.title                     
'Discovery of First Branched-Chain Ketoacid Dehydrogenase Kinase (BDK) Inhibitor Clinical Candidate PF-07328948.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1021/acs.jmedchem.4c02230 
_citation.pdbx_database_id_PubMed   39560668 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Filipski, K.J.'            1  ? 
primary 'Martinez-Alsina, L.A.'     2  ? 
primary 'Reese, M.R.'               3  ? 
primary 'Evrard, E.'                4  ? 
primary 'Buzon, L.M.'               5  ? 
primary 'Cameron, K.O.'             6  ? 
primary 'Zhang, Y.'                 7  ? 
primary 'Coffman, K.J.'             8  ? 
primary 'Bradow, J.'                9  ? 
primary 'Kormos, B.L.'              10 ? 
primary 'Liu, S.'                   11 ? 
primary 'Knafels, J.D.'             12 ? 
primary 'Sahasrabudhe, P.V.'        13 ? 
primary 'Chen, J.'                  14 ? 
primary 'Kalgutkar, A.S.'           15 ? 
primary 'Bessire, A.J.'             16 ? 
primary 'Orozco, C.C.'              17 ? 
primary 'Balesano, A.'              18 ? 
primary 'Cerny, M.A.'               19 ? 
primary 'Bollinger, E.'             20 ? 
primary 'Reyes, A.R.'               21 ? 
primary 'Laforest, B.'              22 ? 
primary 'Rosado, A.'                23 ? 
primary 'Williams, G.'              24 ? 
primary 'Marshall, M.'              25 ? 
primary 'Tam Neale, K.'             26 ? 
primary 'Chen, X.'                  27 ? 
primary 'Hirenallur-Shanthappa, D.' 28 ? 
primary 'Stansfield, J.C.'          29 ? 
primary 'Groarke, J.'               30 ? 
primary 'Qiu, R.'                   31 ? 
primary 'Karas, S.'                 32 ? 
primary 'Roth Flach, R.J.'          33 ? 
primary 'Esler, W.P.'               34 ? 
# 
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 'Branched-chain alpha-ketoacid dehydrogenase kinase'                                   44261.582 1   
2.7.11.1,2.7.11.4 ? ? ? 
2 non-polymer syn "ADENOSINE-5'-DIPHOSPHATE"                                                             427.201   1   ? ? ? ? 
3 non-polymer syn 'MAGNESIUM ION'                                                                        24.305    1   ? ? ? ? 
4 non-polymer syn 'POTASSIUM ION'                                                                        39.098    1   ? ? ? ? 
5 non-polymer syn '(3M)-6-fluoro-3-(2,4,5-trifluoro-3-methoxyphenyl)-1-benzothiophene-2-carboxylic acid' 356.292   1   ? ? ? ? 
6 non-polymer syn 'PHOSPHATE ION'                                                                        94.971    1   ? ? ? ? 
7 water       nat water                                                                                  18.015    130 ? ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'BCKDH kinase,BCKDHKIN,BDK,[3-methyl-2-oxobutanoate dehydrogenase [lipoamide]] kinase,mitochondrial' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;STSATDTHHVELARERSKTVTSFYNQSAIDVVAEKPSVRLTPTMMLYSGRSQDGSHLLKSGRYLQQELPVRIAHRIKGFR
SLPFIIGCNPTILHVHELYIRAFQKLTDFPPIKDQADEAQYCQLVRQLLDDHKDVVTLLAEGLRESRKHIEDEKLVRYFL
DKTLTSRLGIRMLATHHLALHEDKPDFVGIICTRLSPKKIIEKWVDFARRLCEHKYGNAPRVRINGHVAARFPFIPMPLD
YILPELLKNAMRATMESHLDTPYNVPDVVITIANNDVDLIIRISDRGGGIAHKDLDRVMDYHFTTAEASTQDPRISPLFG
HLDMHSGGQSGPMHGFGFGLPTSRAYAEYLGGSLQLQSLQGIGTDVYLRLRHIDGREESFRIHHHHHH
;
_entity_poly.pdbx_seq_one_letter_code_can   
;STSATDTHHVELARERSKTVTSFYNQSAIDVVAEKPSVRLTPTMMLYSGRSQDGSHLLKSGRYLQQELPVRIAHRIKGFR
SLPFIIGCNPTILHVHELYIRAFQKLTDFPPIKDQADEAQYCQLVRQLLDDHKDVVTLLAEGLRESRKHIEDEKLVRYFL
DKTLTSRLGIRMLATHHLALHEDKPDFVGIICTRLSPKKIIEKWVDFARRLCEHKYGNAPRVRINGHVAARFPFIPMPLD
YILPELLKNAMRATMESHLDTPYNVPDVVITIANNDVDLIIRISDRGGGIAHKDLDRVMDYHFTTAEASTQDPRISPLFG
HLDMHSGGQSGPMHGFGFGLPTSRAYAEYLGGSLQLQSLQGIGTDVYLRLRHIDGREESFRIHHHHHH
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 "ADENOSINE-5'-DIPHOSPHATE"                                                             ADP   
3 'MAGNESIUM ION'                                                                        MG    
4 'POTASSIUM ION'                                                                        K     
5 '(3M)-6-fluoro-3-(2,4,5-trifluoro-3-methoxyphenyl)-1-benzothiophene-2-carboxylic acid' A1A40 
6 'PHOSPHATE ION'                                                                        PO4   
7 water                                                                                  HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   SER n 
1 2   THR n 
1 3   SER n 
1 4   ALA n 
1 5   THR n 
1 6   ASP n 
1 7   THR n 
1 8   HIS n 
1 9   HIS n 
1 10  VAL n 
1 11  GLU n 
1 12  LEU n 
1 13  ALA n 
1 14  ARG n 
1 15  GLU n 
1 16  ARG n 
1 17  SER n 
1 18  LYS n 
1 19  THR n 
1 20  VAL n 
1 21  THR n 
1 22  SER n 
1 23  PHE n 
1 24  TYR n 
1 25  ASN n 
1 26  GLN n 
1 27  SER n 
1 28  ALA n 
1 29  ILE n 
1 30  ASP n 
1 31  VAL n 
1 32  VAL n 
1 33  ALA n 
1 34  GLU n 
1 35  LYS n 
1 36  PRO n 
1 37  SER n 
1 38  VAL n 
1 39  ARG n 
1 40  LEU n 
1 41  THR n 
1 42  PRO n 
1 43  THR n 
1 44  MET n 
1 45  MET n 
1 46  LEU n 
1 47  TYR n 
1 48  SER n 
1 49  GLY n 
1 50  ARG n 
1 51  SER n 
1 52  GLN n 
1 53  ASP n 
1 54  GLY n 
1 55  SER n 
1 56  HIS n 
1 57  LEU n 
1 58  LEU n 
1 59  LYS n 
1 60  SER n 
1 61  GLY n 
1 62  ARG n 
1 63  TYR n 
1 64  LEU n 
1 65  GLN n 
1 66  GLN n 
1 67  GLU n 
1 68  LEU n 
1 69  PRO n 
1 70  VAL n 
1 71  ARG n 
1 72  ILE n 
1 73  ALA n 
1 74  HIS n 
1 75  ARG n 
1 76  ILE n 
1 77  LYS n 
1 78  GLY n 
1 79  PHE n 
1 80  ARG n 
1 81  SER n 
1 82  LEU n 
1 83  PRO n 
1 84  PHE n 
1 85  ILE n 
1 86  ILE n 
1 87  GLY n 
1 88  CYS n 
1 89  ASN n 
1 90  PRO n 
1 91  THR n 
1 92  ILE n 
1 93  LEU n 
1 94  HIS n 
1 95  VAL n 
1 96  HIS n 
1 97  GLU n 
1 98  LEU n 
1 99  TYR n 
1 100 ILE n 
1 101 ARG n 
1 102 ALA n 
1 103 PHE n 
1 104 GLN n 
1 105 LYS n 
1 106 LEU n 
1 107 THR n 
1 108 ASP n 
1 109 PHE n 
1 110 PRO n 
1 111 PRO n 
1 112 ILE n 
1 113 LYS n 
1 114 ASP n 
1 115 GLN n 
1 116 ALA n 
1 117 ASP n 
1 118 GLU n 
1 119 ALA n 
1 120 GLN n 
1 121 TYR n 
1 122 CYS n 
1 123 GLN n 
1 124 LEU n 
1 125 VAL n 
1 126 ARG n 
1 127 GLN n 
1 128 LEU n 
1 129 LEU n 
1 130 ASP n 
1 131 ASP n 
1 132 HIS n 
1 133 LYS n 
1 134 ASP n 
1 135 VAL n 
1 136 VAL n 
1 137 THR n 
1 138 LEU n 
1 139 LEU n 
1 140 ALA n 
1 141 GLU n 
1 142 GLY n 
1 143 LEU n 
1 144 ARG n 
1 145 GLU n 
1 146 SER n 
1 147 ARG n 
1 148 LYS n 
1 149 HIS n 
1 150 ILE n 
1 151 GLU n 
1 152 ASP n 
1 153 GLU n 
1 154 LYS n 
1 155 LEU n 
1 156 VAL n 
1 157 ARG n 
1 158 TYR n 
1 159 PHE n 
1 160 LEU n 
1 161 ASP n 
1 162 LYS n 
1 163 THR n 
1 164 LEU n 
1 165 THR n 
1 166 SER n 
1 167 ARG n 
1 168 LEU n 
1 169 GLY n 
1 170 ILE n 
1 171 ARG n 
1 172 MET n 
1 173 LEU n 
1 174 ALA n 
1 175 THR n 
1 176 HIS n 
1 177 HIS n 
1 178 LEU n 
1 179 ALA n 
1 180 LEU n 
1 181 HIS n 
1 182 GLU n 
1 183 ASP n 
1 184 LYS n 
1 185 PRO n 
1 186 ASP n 
1 187 PHE n 
1 188 VAL n 
1 189 GLY n 
1 190 ILE n 
1 191 ILE n 
1 192 CYS n 
1 193 THR n 
1 194 ARG n 
1 195 LEU n 
1 196 SER n 
1 197 PRO n 
1 198 LYS n 
1 199 LYS n 
1 200 ILE n 
1 201 ILE n 
1 202 GLU n 
1 203 LYS n 
1 204 TRP n 
1 205 VAL n 
1 206 ASP n 
1 207 PHE n 
1 208 ALA n 
1 209 ARG n 
1 210 ARG n 
1 211 LEU n 
1 212 CYS n 
1 213 GLU n 
1 214 HIS n 
1 215 LYS n 
1 216 TYR n 
1 217 GLY n 
1 218 ASN n 
1 219 ALA n 
1 220 PRO n 
1 221 ARG n 
1 222 VAL n 
1 223 ARG n 
1 224 ILE n 
1 225 ASN n 
1 226 GLY n 
1 227 HIS n 
1 228 VAL n 
1 229 ALA n 
1 230 ALA n 
1 231 ARG n 
1 232 PHE n 
1 233 PRO n 
1 234 PHE n 
1 235 ILE n 
1 236 PRO n 
1 237 MET n 
1 238 PRO n 
1 239 LEU n 
1 240 ASP n 
1 241 TYR n 
1 242 ILE n 
1 243 LEU n 
1 244 PRO n 
1 245 GLU n 
1 246 LEU n 
1 247 LEU n 
1 248 LYS n 
1 249 ASN n 
1 250 ALA n 
1 251 MET n 
1 252 ARG n 
1 253 ALA n 
1 254 THR n 
1 255 MET n 
1 256 GLU n 
1 257 SER n 
1 258 HIS n 
1 259 LEU n 
1 260 ASP n 
1 261 THR n 
1 262 PRO n 
1 263 TYR n 
1 264 ASN n 
1 265 VAL n 
1 266 PRO n 
1 267 ASP n 
1 268 VAL n 
1 269 VAL n 
1 270 ILE n 
1 271 THR n 
1 272 ILE n 
1 273 ALA n 
1 274 ASN n 
1 275 ASN n 
1 276 ASP n 
1 277 VAL n 
1 278 ASP n 
1 279 LEU n 
1 280 ILE n 
1 281 ILE n 
1 282 ARG n 
1 283 ILE n 
1 284 SER n 
1 285 ASP n 
1 286 ARG n 
1 287 GLY n 
1 288 GLY n 
1 289 GLY n 
1 290 ILE n 
1 291 ALA n 
1 292 HIS n 
1 293 LYS n 
1 294 ASP n 
1 295 LEU n 
1 296 ASP n 
1 297 ARG n 
1 298 VAL n 
1 299 MET n 
1 300 ASP n 
1 301 TYR n 
1 302 HIS n 
1 303 PHE n 
1 304 THR n 
1 305 THR n 
1 306 ALA n 
1 307 GLU n 
1 308 ALA n 
1 309 SER n 
1 310 THR n 
1 311 GLN n 
1 312 ASP n 
1 313 PRO n 
1 314 ARG n 
1 315 ILE n 
1 316 SER n 
1 317 PRO n 
1 318 LEU n 
1 319 PHE n 
1 320 GLY n 
1 321 HIS n 
1 322 LEU n 
1 323 ASP n 
1 324 MET n 
1 325 HIS n 
1 326 SER n 
1 327 GLY n 
1 328 GLY n 
1 329 GLN n 
1 330 SER n 
1 331 GLY n 
1 332 PRO n 
1 333 MET n 
1 334 HIS n 
1 335 GLY n 
1 336 PHE n 
1 337 GLY n 
1 338 PHE n 
1 339 GLY n 
1 340 LEU n 
1 341 PRO n 
1 342 THR n 
1 343 SER n 
1 344 ARG n 
1 345 ALA n 
1 346 TYR n 
1 347 ALA n 
1 348 GLU n 
1 349 TYR n 
1 350 LEU n 
1 351 GLY n 
1 352 GLY n 
1 353 SER n 
1 354 LEU n 
1 355 GLN n 
1 356 LEU n 
1 357 GLN n 
1 358 SER n 
1 359 LEU n 
1 360 GLN n 
1 361 GLY n 
1 362 ILE n 
1 363 GLY n 
1 364 THR n 
1 365 ASP n 
1 366 VAL n 
1 367 TYR n 
1 368 LEU n 
1 369 ARG n 
1 370 LEU n 
1 371 ARG n 
1 372 HIS n 
1 373 ILE n 
1 374 ASP n 
1 375 GLY n 
1 376 ARG n 
1 377 GLU n 
1 378 GLU n 
1 379 SER n 
1 380 PHE n 
1 381 ARG n 
1 382 ILE n 
1 383 HIS n 
1 384 HIS n 
1 385 HIS n 
1 386 HIS n 
1 387 HIS n 
1 388 HIS n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   388 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 BCKDK 
_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      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_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      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_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                   ? 
# 
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 
A1A40 non-polymer         . '(3M)-6-fluoro-3-(2,4,5-trifluoro-3-methoxyphenyl)-1-benzothiophene-2-carboxylic acid' ? 
'C16 H8 F4 O3 S'    356.292 
ADP   non-polymer         n "ADENOSINE-5'-DIPHOSPHATE"                                                             ? 
'C10 H15 N5 O10 P2' 427.201 
ALA   'L-peptide linking' y ALANINE                                                                                ? 'C3 H7 N O2' 
89.093  
ARG   'L-peptide linking' y ARGININE                                                                               ? 
'C6 H15 N4 O2 1'    175.209 
ASN   'L-peptide linking' y ASPARAGINE                                                                             ? 'C4 H8 N2 O3' 
132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID'                                                                        ? 'C4 H7 N O4' 
133.103 
CYS   'L-peptide linking' y CYSTEINE                                                                               ? 
'C3 H7 N O2 S'      121.158 
GLN   'L-peptide linking' y GLUTAMINE                                                                              ? 
'C5 H10 N2 O3'      146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID'                                                                        ? 'C5 H9 N O4' 
147.129 
GLY   'peptide linking'   y GLYCINE                                                                                ? 'C2 H5 N O2' 
75.067  
HIS   'L-peptide linking' y HISTIDINE                                                                              ? 
'C6 H10 N3 O2 1'    156.162 
HOH   non-polymer         . WATER                                                                                  ? 'H2 O' 18.015 
ILE   'L-peptide linking' y ISOLEUCINE                                                                             ? 'C6 H13 N O2' 
131.173 
K     non-polymer         . 'POTASSIUM ION'                                                                        ? 'K 1' 39.098  
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 
PHE   'L-peptide linking' y PHENYLALANINE                                                                          ? 'C9 H11 N O2' 
165.189 
PO4   non-polymer         . 'PHOSPHATE ION'                                                                        ? 'O4 P -3' 
94.971  
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   SER 1   1   ?   ?   ?   A . n 
A 1 2   THR 2   2   ?   ?   ?   A . n 
A 1 3   SER 3   3   ?   ?   ?   A . n 
A 1 4   ALA 4   4   ?   ?   ?   A . n 
A 1 5   THR 5   5   ?   ?   ?   A . n 
A 1 6   ASP 6   6   ?   ?   ?   A . n 
A 1 7   THR 7   7   ?   ?   ?   A . n 
A 1 8   HIS 8   8   ?   ?   ?   A . n 
A 1 9   HIS 9   9   ?   ?   ?   A . n 
A 1 10  VAL 10  10  ?   ?   ?   A . n 
A 1 11  GLU 11  11  ?   ?   ?   A . n 
A 1 12  LEU 12  12  ?   ?   ?   A . n 
A 1 13  ALA 13  13  ?   ?   ?   A . n 
A 1 14  ARG 14  14  ?   ?   ?   A . n 
A 1 15  GLU 15  15  ?   ?   ?   A . n 
A 1 16  ARG 16  16  ?   ?   ?   A . n 
A 1 17  SER 17  17  ?   ?   ?   A . n 
A 1 18  LYS 18  18  ?   ?   ?   A . n 
A 1 19  THR 19  19  ?   ?   ?   A . n 
A 1 20  VAL 20  20  ?   ?   ?   A . n 
A 1 21  THR 21  21  ?   ?   ?   A . n 
A 1 22  SER 22  22  ?   ?   ?   A . n 
A 1 23  PHE 23  23  ?   ?   ?   A . n 
A 1 24  TYR 24  24  ?   ?   ?   A . n 
A 1 25  ASN 25  25  ?   ?   ?   A . n 
A 1 26  GLN 26  26  ?   ?   ?   A . n 
A 1 27  SER 27  27  27  SER SER A . n 
A 1 28  ALA 28  28  28  ALA ALA A . n 
A 1 29  ILE 29  29  29  ILE ILE A . n 
A 1 30  ASP 30  30  30  ASP ASP A . n 
A 1 31  VAL 31  31  31  VAL VAL A . n 
A 1 32  VAL 32  32  32  VAL VAL A . n 
A 1 33  ALA 33  33  33  ALA ALA A . n 
A 1 34  GLU 34  34  34  GLU GLU A . n 
A 1 35  LYS 35  35  35  LYS LYS A . n 
A 1 36  PRO 36  36  36  PRO PRO A . n 
A 1 37  SER 37  37  37  SER SER A . n 
A 1 38  VAL 38  38  38  VAL VAL A . n 
A 1 39  ARG 39  39  39  ARG ARG A . n 
A 1 40  LEU 40  40  40  LEU LEU A . n 
A 1 41  THR 41  41  41  THR THR A . n 
A 1 42  PRO 42  42  42  PRO PRO A . n 
A 1 43  THR 43  43  43  THR THR A . n 
A 1 44  MET 44  44  44  MET MET A . n 
A 1 45  MET 45  45  45  MET MET A . n 
A 1 46  LEU 46  46  46  LEU LEU A . n 
A 1 47  TYR 47  47  47  TYR ALA A . n 
A 1 48  SER 48  48  ?   ?   ?   A . n 
A 1 49  GLY 49  49  ?   ?   ?   A . n 
A 1 50  ARG 50  50  ?   ?   ?   A . n 
A 1 51  SER 51  51  ?   ?   ?   A . n 
A 1 52  GLN 52  52  ?   ?   ?   A . n 
A 1 53  ASP 53  53  53  ASP ASP A . n 
A 1 54  GLY 54  54  54  GLY GLY A . n 
A 1 55  SER 55  55  55  SER SER A . n 
A 1 56  HIS 56  56  56  HIS HIS A . n 
A 1 57  LEU 57  57  57  LEU LEU A . n 
A 1 58  LEU 58  58  58  LEU LEU A . n 
A 1 59  LYS 59  59  59  LYS LYS A . n 
A 1 60  SER 60  60  60  SER SER A . n 
A 1 61  GLY 61  61  61  GLY GLY A . n 
A 1 62  ARG 62  62  62  ARG ARG A . n 
A 1 63  TYR 63  63  63  TYR TYR A . n 
A 1 64  LEU 64  64  64  LEU LEU A . n 
A 1 65  GLN 65  65  65  GLN GLN A . n 
A 1 66  GLN 66  66  66  GLN GLN A . n 
A 1 67  GLU 67  67  67  GLU GLU A . n 
A 1 68  LEU 68  68  68  LEU LEU A . n 
A 1 69  PRO 69  69  69  PRO PRO A . n 
A 1 70  VAL 70  70  70  VAL VAL A . n 
A 1 71  ARG 71  71  71  ARG ARG A . n 
A 1 72  ILE 72  72  72  ILE ILE A . n 
A 1 73  ALA 73  73  73  ALA ALA A . n 
A 1 74  HIS 74  74  74  HIS HIS A . n 
A 1 75  ARG 75  75  75  ARG ARG A . n 
A 1 76  ILE 76  76  76  ILE ILE A . n 
A 1 77  LYS 77  77  77  LYS LYS A . n 
A 1 78  GLY 78  78  78  GLY GLY A . n 
A 1 79  PHE 79  79  79  PHE PHE A . n 
A 1 80  ARG 80  80  80  ARG ARG A . n 
A 1 81  SER 81  81  81  SER SER A . n 
A 1 82  LEU 82  82  82  LEU LEU A . n 
A 1 83  PRO 83  83  83  PRO PRO A . n 
A 1 84  PHE 84  84  84  PHE PHE A . n 
A 1 85  ILE 85  85  85  ILE ILE A . n 
A 1 86  ILE 86  86  86  ILE ILE A . n 
A 1 87  GLY 87  87  87  GLY GLY A . n 
A 1 88  CYS 88  88  88  CYS CYS A . n 
A 1 89  ASN 89  89  89  ASN ASN A . n 
A 1 90  PRO 90  90  90  PRO PRO A . n 
A 1 91  THR 91  91  91  THR THR A . n 
A 1 92  ILE 92  92  92  ILE ILE A . n 
A 1 93  LEU 93  93  93  LEU LEU A . n 
A 1 94  HIS 94  94  94  HIS HIS A . n 
A 1 95  VAL 95  95  95  VAL VAL A . n 
A 1 96  HIS 96  96  96  HIS HIS A . n 
A 1 97  GLU 97  97  97  GLU GLU A . n 
A 1 98  LEU 98  98  98  LEU LEU A . n 
A 1 99  TYR 99  99  99  TYR TYR A . n 
A 1 100 ILE 100 100 100 ILE ILE A . n 
A 1 101 ARG 101 101 101 ARG ARG A . n 
A 1 102 ALA 102 102 102 ALA ALA A . n 
A 1 103 PHE 103 103 103 PHE PHE A . n 
A 1 104 GLN 104 104 104 GLN GLN A . n 
A 1 105 LYS 105 105 105 LYS LYS A . n 
A 1 106 LEU 106 106 106 LEU LEU A . n 
A 1 107 THR 107 107 107 THR THR A . n 
A 1 108 ASP 108 108 108 ASP ASP A . n 
A 1 109 PHE 109 109 109 PHE PHE A . n 
A 1 110 PRO 110 110 110 PRO PRO A . n 
A 1 111 PRO 111 111 111 PRO PRO A . n 
A 1 112 ILE 112 112 112 ILE ILE A . n 
A 1 113 LYS 113 113 113 LYS LYS A . n 
A 1 114 ASP 114 114 114 ASP ASP A . n 
A 1 115 GLN 115 115 115 GLN GLN A . n 
A 1 116 ALA 116 116 116 ALA ALA A . n 
A 1 117 ASP 117 117 117 ASP ASP A . n 
A 1 118 GLU 118 118 118 GLU GLU A . n 
A 1 119 ALA 119 119 119 ALA ALA A . n 
A 1 120 GLN 120 120 120 GLN GLN A . n 
A 1 121 TYR 121 121 121 TYR TYR A . n 
A 1 122 CYS 122 122 122 CYS CYS A . n 
A 1 123 GLN 123 123 123 GLN GLN A . n 
A 1 124 LEU 124 124 124 LEU LEU A . n 
A 1 125 VAL 125 125 125 VAL VAL A . n 
A 1 126 ARG 126 126 126 ARG ARG A . n 
A 1 127 GLN 127 127 127 GLN GLN A . n 
A 1 128 LEU 128 128 128 LEU LEU A . n 
A 1 129 LEU 129 129 129 LEU LEU A . n 
A 1 130 ASP 130 130 130 ASP ASP A . n 
A 1 131 ASP 131 131 131 ASP ASP A . n 
A 1 132 HIS 132 132 132 HIS HIS A . n 
A 1 133 LYS 133 133 133 LYS LYS A . n 
A 1 134 ASP 134 134 134 ASP ASP A . n 
A 1 135 VAL 135 135 135 VAL VAL A . n 
A 1 136 VAL 136 136 136 VAL VAL A . n 
A 1 137 THR 137 137 137 THR THR A . n 
A 1 138 LEU 138 138 138 LEU LEU A . n 
A 1 139 LEU 139 139 139 LEU LEU A . n 
A 1 140 ALA 140 140 140 ALA ALA A . n 
A 1 141 GLU 141 141 141 GLU GLU A . n 
A 1 142 GLY 142 142 142 GLY GLY A . n 
A 1 143 LEU 143 143 143 LEU LEU A . n 
A 1 144 ARG 144 144 144 ARG ARG A . n 
A 1 145 GLU 145 145 145 GLU GLU A . n 
A 1 146 SER 146 146 146 SER SER A . n 
A 1 147 ARG 147 147 147 ARG ARG A . n 
A 1 148 LYS 148 148 148 LYS LYS A . n 
A 1 149 HIS 149 149 149 HIS HIS A . n 
A 1 150 ILE 150 150 150 ILE ILE A . n 
A 1 151 GLU 151 151 151 GLU GLU A . n 
A 1 152 ASP 152 152 152 ASP ASP A . n 
A 1 153 GLU 153 153 153 GLU GLU A . n 
A 1 154 LYS 154 154 154 LYS LYS A . n 
A 1 155 LEU 155 155 155 LEU LEU A . n 
A 1 156 VAL 156 156 156 VAL VAL A . n 
A 1 157 ARG 157 157 157 ARG ARG A . n 
A 1 158 TYR 158 158 158 TYR TYR A . n 
A 1 159 PHE 159 159 159 PHE PHE A . n 
A 1 160 LEU 160 160 160 LEU LEU A . n 
A 1 161 ASP 161 161 161 ASP ASP A . n 
A 1 162 LYS 162 162 162 LYS LYS A . n 
A 1 163 THR 163 163 163 THR THR A . n 
A 1 164 LEU 164 164 164 LEU LEU A . n 
A 1 165 THR 165 165 165 THR THR A . n 
A 1 166 SER 166 166 166 SER SER A . n 
A 1 167 ARG 167 167 167 ARG ARG A . n 
A 1 168 LEU 168 168 168 LEU LEU A . n 
A 1 169 GLY 169 169 169 GLY GLY A . n 
A 1 170 ILE 170 170 170 ILE ILE A . n 
A 1 171 ARG 171 171 171 ARG ARG A . n 
A 1 172 MET 172 172 172 MET MET A . n 
A 1 173 LEU 173 173 173 LEU LEU A . n 
A 1 174 ALA 174 174 174 ALA ALA A . n 
A 1 175 THR 175 175 175 THR THR A . n 
A 1 176 HIS 176 176 176 HIS HIS A . n 
A 1 177 HIS 177 177 177 HIS HIS A . n 
A 1 178 LEU 178 178 178 LEU LEU A . n 
A 1 179 ALA 179 179 179 ALA ALA A . n 
A 1 180 LEU 180 180 180 LEU LEU A . n 
A 1 181 HIS 181 181 181 HIS HIS A . n 
A 1 182 GLU 182 182 182 GLU GLU A . n 
A 1 183 ASP 183 183 183 ASP ASP A . n 
A 1 184 LYS 184 184 184 LYS LYS A . n 
A 1 185 PRO 185 185 185 PRO PRO A . n 
A 1 186 ASP 186 186 186 ASP ASP A . n 
A 1 187 PHE 187 187 187 PHE PHE A . n 
A 1 188 VAL 188 188 188 VAL VAL A . n 
A 1 189 GLY 189 189 189 GLY GLY A . n 
A 1 190 ILE 190 190 190 ILE ILE A . n 
A 1 191 ILE 191 191 191 ILE ILE A . n 
A 1 192 CYS 192 192 192 CYS CYS A . n 
A 1 193 THR 193 193 193 THR THR A . n 
A 1 194 ARG 194 194 194 ARG ARG A . n 
A 1 195 LEU 195 195 195 LEU LEU A . n 
A 1 196 SER 196 196 196 SER SER A . n 
A 1 197 PRO 197 197 197 PRO PRO A . n 
A 1 198 LYS 198 198 198 LYS LYS A . n 
A 1 199 LYS 199 199 199 LYS LYS A . n 
A 1 200 ILE 200 200 200 ILE ILE A . n 
A 1 201 ILE 201 201 201 ILE ILE A . n 
A 1 202 GLU 202 202 202 GLU GLU A . n 
A 1 203 LYS 203 203 203 LYS LYS A . n 
A 1 204 TRP 204 204 204 TRP TRP A . n 
A 1 205 VAL 205 205 205 VAL VAL A . n 
A 1 206 ASP 206 206 206 ASP ASP A . n 
A 1 207 PHE 207 207 207 PHE PHE A . n 
A 1 208 ALA 208 208 208 ALA ALA A . n 
A 1 209 ARG 209 209 209 ARG ARG A . n 
A 1 210 ARG 210 210 210 ARG ARG A . n 
A 1 211 LEU 211 211 211 LEU LEU A . n 
A 1 212 CYS 212 212 212 CYS CYS A . n 
A 1 213 GLU 213 213 213 GLU GLU A . n 
A 1 214 HIS 214 214 214 HIS HIS A . n 
A 1 215 LYS 215 215 215 LYS LYS A . n 
A 1 216 TYR 216 216 216 TYR TYR A . n 
A 1 217 GLY 217 217 217 GLY GLY A . n 
A 1 218 ASN 218 218 218 ASN ASN A . n 
A 1 219 ALA 219 219 219 ALA ALA A . n 
A 1 220 PRO 220 220 220 PRO PRO A . n 
A 1 221 ARG 221 221 221 ARG ARG A . n 
A 1 222 VAL 222 222 222 VAL VAL A . n 
A 1 223 ARG 223 223 223 ARG ARG A . n 
A 1 224 ILE 224 224 224 ILE ILE A . n 
A 1 225 ASN 225 225 225 ASN ASN A . n 
A 1 226 GLY 226 226 226 GLY GLY A . n 
A 1 227 HIS 227 227 227 HIS HIS A . n 
A 1 228 VAL 228 228 228 VAL VAL A . n 
A 1 229 ALA 229 229 229 ALA ALA A . n 
A 1 230 ALA 230 230 230 ALA ALA A . n 
A 1 231 ARG 231 231 231 ARG ARG A . n 
A 1 232 PHE 232 232 232 PHE PHE A . n 
A 1 233 PRO 233 233 233 PRO PRO A . n 
A 1 234 PHE 234 234 234 PHE PHE A . n 
A 1 235 ILE 235 235 235 ILE ILE A . n 
A 1 236 PRO 236 236 236 PRO PRO A . n 
A 1 237 MET 237 237 237 MET MET A . n 
A 1 238 PRO 238 238 238 PRO PRO A . n 
A 1 239 LEU 239 239 239 LEU LEU A . n 
A 1 240 ASP 240 240 240 ASP ASP A . n 
A 1 241 TYR 241 241 241 TYR TYR A . n 
A 1 242 ILE 242 242 242 ILE ILE A . n 
A 1 243 LEU 243 243 243 LEU LEU A . n 
A 1 244 PRO 244 244 244 PRO PRO A . n 
A 1 245 GLU 245 245 245 GLU GLU A . n 
A 1 246 LEU 246 246 246 LEU LEU A . n 
A 1 247 LEU 247 247 247 LEU LEU A . n 
A 1 248 LYS 248 248 248 LYS LYS A . n 
A 1 249 ASN 249 249 249 ASN ASN A . n 
A 1 250 ALA 250 250 250 ALA ALA A . n 
A 1 251 MET 251 251 251 MET MET A . n 
A 1 252 ARG 252 252 252 ARG ARG A . n 
A 1 253 ALA 253 253 253 ALA ALA A . n 
A 1 254 THR 254 254 254 THR THR A . n 
A 1 255 MET 255 255 255 MET MET A . n 
A 1 256 GLU 256 256 256 GLU GLU A . n 
A 1 257 SER 257 257 257 SER SER A . n 
A 1 258 HIS 258 258 258 HIS HIS A . n 
A 1 259 LEU 259 259 259 LEU LEU A . n 
A 1 260 ASP 260 260 260 ASP ASP A . n 
A 1 261 THR 261 261 261 THR THR A . n 
A 1 262 PRO 262 262 262 PRO PRO A . n 
A 1 263 TYR 263 263 263 TYR TYR A . n 
A 1 264 ASN 264 264 264 ASN ASN A . n 
A 1 265 VAL 265 265 265 VAL VAL A . n 
A 1 266 PRO 266 266 266 PRO PRO A . n 
A 1 267 ASP 267 267 267 ASP ASP A . n 
A 1 268 VAL 268 268 268 VAL VAL A . n 
A 1 269 VAL 269 269 269 VAL VAL A . n 
A 1 270 ILE 270 270 270 ILE ILE A . n 
A 1 271 THR 271 271 271 THR THR A . n 
A 1 272 ILE 272 272 272 ILE ILE A . n 
A 1 273 ALA 273 273 273 ALA ALA A . n 
A 1 274 ASN 274 274 274 ASN ASN A . n 
A 1 275 ASN 275 275 275 ASN ASN A . n 
A 1 276 ASP 276 276 276 ASP ASP A . n 
A 1 277 VAL 277 277 277 VAL VAL A . n 
A 1 278 ASP 278 278 278 ASP ASP A . n 
A 1 279 LEU 279 279 279 LEU LEU A . n 
A 1 280 ILE 280 280 280 ILE ILE A . n 
A 1 281 ILE 281 281 281 ILE ILE A . n 
A 1 282 ARG 282 282 282 ARG ARG A . n 
A 1 283 ILE 283 283 283 ILE ILE A . n 
A 1 284 SER 284 284 284 SER SER A . n 
A 1 285 ASP 285 285 285 ASP ASP A . n 
A 1 286 ARG 286 286 286 ARG ARG A . n 
A 1 287 GLY 287 287 287 GLY GLY A . n 
A 1 288 GLY 288 288 288 GLY GLY A . n 
A 1 289 GLY 289 289 289 GLY GLY A . n 
A 1 290 ILE 290 290 290 ILE ILE A . n 
A 1 291 ALA 291 291 291 ALA ALA A . n 
A 1 292 HIS 292 292 292 HIS HIS A . n 
A 1 293 LYS 293 293 293 LYS LYS A . n 
A 1 294 ASP 294 294 294 ASP ASP A . n 
A 1 295 LEU 295 295 295 LEU LEU A . n 
A 1 296 ASP 296 296 296 ASP ASP A . n 
A 1 297 ARG 297 297 297 ARG ARG A . n 
A 1 298 VAL 298 298 298 VAL VAL A . n 
A 1 299 MET 299 299 299 MET MET A . n 
A 1 300 ASP 300 300 300 ASP ASP A . n 
A 1 301 TYR 301 301 301 TYR TYR A . n 
A 1 302 HIS 302 302 302 HIS HIS A . n 
A 1 303 PHE 303 303 303 PHE PHE A . n 
A 1 304 THR 304 304 304 THR THR A . n 
A 1 305 THR 305 305 305 THR THR A . n 
A 1 306 ALA 306 306 306 ALA ALA A . n 
A 1 307 GLU 307 307 ?   ?   ?   A . n 
A 1 308 ALA 308 308 ?   ?   ?   A . n 
A 1 309 SER 309 309 ?   ?   ?   A . n 
A 1 310 THR 310 310 ?   ?   ?   A . n 
A 1 311 GLN 311 311 ?   ?   ?   A . n 
A 1 312 ASP 312 312 ?   ?   ?   A . n 
A 1 313 PRO 313 313 ?   ?   ?   A . n 
A 1 314 ARG 314 314 ?   ?   ?   A . n 
A 1 315 ILE 315 315 ?   ?   ?   A . n 
A 1 316 SER 316 316 ?   ?   ?   A . n 
A 1 317 PRO 317 317 ?   ?   ?   A . n 
A 1 318 LEU 318 318 ?   ?   ?   A . n 
A 1 319 PHE 319 319 ?   ?   ?   A . n 
A 1 320 GLY 320 320 ?   ?   ?   A . n 
A 1 321 HIS 321 321 ?   ?   ?   A . n 
A 1 322 LEU 322 322 ?   ?   ?   A . n 
A 1 323 ASP 323 323 ?   ?   ?   A . n 
A 1 324 MET 324 324 ?   ?   ?   A . n 
A 1 325 HIS 325 325 ?   ?   ?   A . n 
A 1 326 SER 326 326 ?   ?   ?   A . n 
A 1 327 GLY 327 327 ?   ?   ?   A . n 
A 1 328 GLY 328 328 ?   ?   ?   A . n 
A 1 329 GLN 329 329 ?   ?   ?   A . n 
A 1 330 SER 330 330 ?   ?   ?   A . n 
A 1 331 GLY 331 331 ?   ?   ?   A . n 
A 1 332 PRO 332 332 ?   ?   ?   A . n 
A 1 333 MET 333 333 ?   ?   ?   A . n 
A 1 334 HIS 334 334 ?   ?   ?   A . n 
A 1 335 GLY 335 335 335 GLY GLY A . n 
A 1 336 PHE 336 336 336 PHE PHE A . n 
A 1 337 GLY 337 337 337 GLY GLY A . n 
A 1 338 PHE 338 338 338 PHE PHE A . n 
A 1 339 GLY 339 339 339 GLY GLY A . n 
A 1 340 LEU 340 340 340 LEU LEU A . n 
A 1 341 PRO 341 341 341 PRO PRO A . n 
A 1 342 THR 342 342 342 THR THR A . n 
A 1 343 SER 343 343 343 SER SER A . n 
A 1 344 ARG 344 344 344 ARG ARG A . n 
A 1 345 ALA 345 345 345 ALA ALA A . n 
A 1 346 TYR 346 346 346 TYR TYR A . n 
A 1 347 ALA 347 347 347 ALA ALA A . n 
A 1 348 GLU 348 348 348 GLU GLU A . n 
A 1 349 TYR 349 349 349 TYR TYR A . n 
A 1 350 LEU 350 350 350 LEU LEU A . n 
A 1 351 GLY 351 351 351 GLY GLY A . n 
A 1 352 GLY 352 352 352 GLY GLY A . n 
A 1 353 SER 353 353 353 SER SER A . n 
A 1 354 LEU 354 354 354 LEU LEU A . n 
A 1 355 GLN 355 355 355 GLN GLN A . n 
A 1 356 LEU 356 356 356 LEU LEU A . n 
A 1 357 GLN 357 357 357 GLN GLN A . n 
A 1 358 SER 358 358 358 SER SER A . n 
A 1 359 LEU 359 359 359 LEU LEU A . n 
A 1 360 GLN 360 360 360 GLN GLN A . n 
A 1 361 GLY 361 361 361 GLY GLY A . n 
A 1 362 ILE 362 362 362 ILE ILE A . n 
A 1 363 GLY 363 363 363 GLY GLY A . n 
A 1 364 THR 364 364 364 THR THR A . n 
A 1 365 ASP 365 365 365 ASP ASP A . n 
A 1 366 VAL 366 366 366 VAL VAL A . n 
A 1 367 TYR 367 367 367 TYR TYR A . n 
A 1 368 LEU 368 368 368 LEU LEU A . n 
A 1 369 ARG 369 369 369 ARG ARG A . n 
A 1 370 LEU 370 370 370 LEU LEU A . n 
A 1 371 ARG 371 371 371 ARG ARG A . n 
A 1 372 HIS 372 372 372 HIS HIS A . n 
A 1 373 ILE 373 373 373 ILE ILE A . n 
A 1 374 ASP 374 374 374 ASP ASP A . n 
A 1 375 GLY 375 375 ?   ?   ?   A . n 
A 1 376 ARG 376 376 ?   ?   ?   A . n 
A 1 377 GLU 377 377 ?   ?   ?   A . n 
A 1 378 GLU 378 378 ?   ?   ?   A . n 
A 1 379 SER 379 379 ?   ?   ?   A . n 
A 1 380 PHE 380 380 ?   ?   ?   A . n 
A 1 381 ARG 381 381 ?   ?   ?   A . n 
A 1 382 ILE 382 382 ?   ?   ?   A . n 
A 1 383 HIS 383 383 ?   ?   ?   A . n 
A 1 384 HIS 384 384 ?   ?   ?   A . n 
A 1 385 HIS 385 385 ?   ?   ?   A . n 
A 1 386 HIS 386 386 ?   ?   ?   A . n 
A 1 387 HIS 387 387 ?   ?   ?   A . n 
A 1 388 HIS 388 388 ?   ?   ?   A . n 
# 
loop_
_pdbx_entity_instance_feature.ordinal 
_pdbx_entity_instance_feature.comp_id 
_pdbx_entity_instance_feature.asym_id 
_pdbx_entity_instance_feature.seq_num 
_pdbx_entity_instance_feature.auth_comp_id 
_pdbx_entity_instance_feature.auth_asym_id 
_pdbx_entity_instance_feature.auth_seq_num 
_pdbx_entity_instance_feature.feature_type 
_pdbx_entity_instance_feature.details 
1 A1A40 ? ? A1A40 ? ? 'SUBJECT OF INVESTIGATION' ? 
2 PO4   ? ? PO4   ? ? 'SUBJECT OF INVESTIGATION' ? 
# 
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 
B 2 ADP   1   401 401 ADP   ADP A . 
C 3 MG    1   402 402 MG    MG  A . 
D 4 K     1   403 403 K     K   A . 
E 5 A1A40 1   404 501 A1A40 PFE A . 
F 6 PO4   1   405 1   PO4   PO4 A . 
G 7 HOH   1   501 8   HOH   HOH A . 
G 7 HOH   2   502 21  HOH   HOH A . 
G 7 HOH   3   503 95  HOH   HOH A . 
G 7 HOH   4   504 11  HOH   HOH A . 
G 7 HOH   5   505 31  HOH   HOH A . 
G 7 HOH   6   506 154 HOH   HOH A . 
G 7 HOH   7   507 93  HOH   HOH A . 
G 7 HOH   8   508 57  HOH   HOH A . 
G 7 HOH   9   509 47  HOH   HOH A . 
G 7 HOH   10  510 149 HOH   HOH A . 
G 7 HOH   11  511 150 HOH   HOH A . 
G 7 HOH   12  512 130 HOH   HOH A . 
G 7 HOH   13  513 23  HOH   HOH A . 
G 7 HOH   14  514 19  HOH   HOH A . 
G 7 HOH   15  515 18  HOH   HOH A . 
G 7 HOH   16  516 159 HOH   HOH A . 
G 7 HOH   17  517 25  HOH   HOH A . 
G 7 HOH   18  518 94  HOH   HOH A . 
G 7 HOH   19  519 110 HOH   HOH A . 
G 7 HOH   20  520 92  HOH   HOH A . 
G 7 HOH   21  521 99  HOH   HOH A . 
G 7 HOH   22  522 16  HOH   HOH A . 
G 7 HOH   23  523 152 HOH   HOH A . 
G 7 HOH   24  524 6   HOH   HOH A . 
G 7 HOH   25  525 37  HOH   HOH A . 
G 7 HOH   26  526 82  HOH   HOH A . 
G 7 HOH   27  527 104 HOH   HOH A . 
G 7 HOH   28  528 85  HOH   HOH A . 
G 7 HOH   29  529 108 HOH   HOH A . 
G 7 HOH   30  530 29  HOH   HOH A . 
G 7 HOH   31  531 22  HOH   HOH A . 
G 7 HOH   32  532 148 HOH   HOH A . 
G 7 HOH   33  533 5   HOH   HOH A . 
G 7 HOH   34  534 146 HOH   HOH A . 
G 7 HOH   35  535 136 HOH   HOH A . 
G 7 HOH   36  536 129 HOH   HOH A . 
G 7 HOH   37  537 69  HOH   HOH A . 
G 7 HOH   38  538 161 HOH   HOH A . 
G 7 HOH   39  539 52  HOH   HOH A . 
G 7 HOH   40  540 79  HOH   HOH A . 
G 7 HOH   41  541 13  HOH   HOH A . 
G 7 HOH   42  542 119 HOH   HOH A . 
G 7 HOH   43  543 40  HOH   HOH A . 
G 7 HOH   44  544 97  HOH   HOH A . 
G 7 HOH   45  545 39  HOH   HOH A . 
G 7 HOH   46  546 127 HOH   HOH A . 
G 7 HOH   47  547 28  HOH   HOH A . 
G 7 HOH   48  548 112 HOH   HOH A . 
G 7 HOH   49  549 137 HOH   HOH A . 
G 7 HOH   50  550 45  HOH   HOH A . 
G 7 HOH   51  551 66  HOH   HOH A . 
G 7 HOH   52  552 126 HOH   HOH A . 
G 7 HOH   53  553 107 HOH   HOH A . 
G 7 HOH   54  554 12  HOH   HOH A . 
G 7 HOH   55  555 128 HOH   HOH A . 
G 7 HOH   56  556 89  HOH   HOH A . 
G 7 HOH   57  557 59  HOH   HOH A . 
G 7 HOH   58  558 65  HOH   HOH A . 
G 7 HOH   59  559 58  HOH   HOH A . 
G 7 HOH   60  560 131 HOH   HOH A . 
G 7 HOH   61  561 86  HOH   HOH A . 
G 7 HOH   62  562 41  HOH   HOH A . 
G 7 HOH   63  563 77  HOH   HOH A . 
G 7 HOH   64  564 145 HOH   HOH A . 
G 7 HOH   65  565 71  HOH   HOH A . 
G 7 HOH   66  566 132 HOH   HOH A . 
G 7 HOH   67  567 67  HOH   HOH A . 
G 7 HOH   68  568 160 HOH   HOH A . 
G 7 HOH   69  569 49  HOH   HOH A . 
G 7 HOH   70  570 114 HOH   HOH A . 
G 7 HOH   71  571 34  HOH   HOH A . 
G 7 HOH   72  572 55  HOH   HOH A . 
G 7 HOH   73  573 144 HOH   HOH A . 
G 7 HOH   74  574 151 HOH   HOH A . 
G 7 HOH   75  575 68  HOH   HOH A . 
G 7 HOH   76  576 124 HOH   HOH A . 
G 7 HOH   77  577 38  HOH   HOH A . 
G 7 HOH   78  578 44  HOH   HOH A . 
G 7 HOH   79  579 84  HOH   HOH A . 
G 7 HOH   80  580 33  HOH   HOH A . 
G 7 HOH   81  581 118 HOH   HOH A . 
G 7 HOH   82  582 50  HOH   HOH A . 
G 7 HOH   83  583 63  HOH   HOH A . 
G 7 HOH   84  584 43  HOH   HOH A . 
G 7 HOH   85  585 158 HOH   HOH A . 
G 7 HOH   86  586 51  HOH   HOH A . 
G 7 HOH   87  587 75  HOH   HOH A . 
G 7 HOH   88  588 115 HOH   HOH A . 
G 7 HOH   89  589 123 HOH   HOH A . 
G 7 HOH   90  590 64  HOH   HOH A . 
G 7 HOH   91  591 78  HOH   HOH A . 
G 7 HOH   92  592 20  HOH   HOH A . 
G 7 HOH   93  593 24  HOH   HOH A . 
G 7 HOH   94  594 122 HOH   HOH A . 
G 7 HOH   95  595 111 HOH   HOH A . 
G 7 HOH   96  596 42  HOH   HOH A . 
G 7 HOH   97  597 138 HOH   HOH A . 
G 7 HOH   98  598 80  HOH   HOH A . 
G 7 HOH   99  599 98  HOH   HOH A . 
G 7 HOH   100 600 105 HOH   HOH A . 
G 7 HOH   101 601 139 HOH   HOH A . 
G 7 HOH   102 602 120 HOH   HOH A . 
G 7 HOH   103 603 76  HOH   HOH A . 
G 7 HOH   104 604 157 HOH   HOH A . 
G 7 HOH   105 605 48  HOH   HOH A . 
G 7 HOH   106 606 135 HOH   HOH A . 
G 7 HOH   107 607 153 HOH   HOH A . 
G 7 HOH   108 608 53  HOH   HOH A . 
G 7 HOH   109 609 101 HOH   HOH A . 
G 7 HOH   110 610 113 HOH   HOH A . 
G 7 HOH   111 611 156 HOH   HOH A . 
G 7 HOH   112 612 134 HOH   HOH A . 
G 7 HOH   113 613 106 HOH   HOH A . 
G 7 HOH   114 614 32  HOH   HOH A . 
G 7 HOH   115 615 125 HOH   HOH A . 
G 7 HOH   116 616 141 HOH   HOH A . 
G 7 HOH   117 617 103 HOH   HOH A . 
G 7 HOH   118 618 26  HOH   HOH A . 
G 7 HOH   119 619 155 HOH   HOH A . 
G 7 HOH   120 620 147 HOH   HOH A . 
G 7 HOH   121 621 60  HOH   HOH A . 
G 7 HOH   122 622 83  HOH   HOH A . 
G 7 HOH   123 623 81  HOH   HOH A . 
G 7 HOH   124 624 61  HOH   HOH A . 
G 7 HOH   125 625 142 HOH   HOH A . 
G 7 HOH   126 626 117 HOH   HOH A . 
G 7 HOH   127 627 109 HOH   HOH A . 
G 7 HOH   128 628 140 HOH   HOH A . 
G 7 HOH   129 629 88  HOH   HOH A . 
G 7 HOH   130 630 72  HOH   HOH A . 
# 
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 TYR 47 ? CG  ? A TYR 47 CG  
2 1 Y 1 A TYR 47 ? CD1 ? A TYR 47 CD1 
3 1 Y 1 A TYR 47 ? CD2 ? A TYR 47 CD2 
4 1 Y 1 A TYR 47 ? CE1 ? A TYR 47 CE1 
5 1 Y 1 A TYR 47 ? CE2 ? A TYR 47 CE2 
6 1 Y 1 A TYR 47 ? CZ  ? A TYR 47 CZ  
7 1 Y 1 A TYR 47 ? OH  ? A TYR 47 OH  
# 
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    ? ? ? 2.11.8 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS       ? ? ? .      2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? STARANISO ? ? ? .      3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? BUSTER    ? ? ? .      4 
# 
_cell.angle_alpha                  90 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9DI9 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     126.35 
_cell.length_a_esd                 ? 
_cell.length_b                     126.35 
_cell.length_b_esd                 ? 
_cell.length_c                     74.68 
_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                         9DI9 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                94 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 42 21 2' 
_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                   9DI9 
_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             3.37 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          63.47 
_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              6.0 
_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    
;16% PEG-3350 and 8% tacsimate pH 6.0 (Hampton Research).   Fully grown crystals were soaked overnight in a solution of 8% tacsimate pH 6.0, 25% PEG-3350, 50 mM KCl, 50 mM MgCl2, 2 mM ADP, 20% glycerol, 5% DMSO, and 1.5 mM 6 (PF-07328948) and flash frozen in liquid nitrogen
;
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER X 16M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2020-11-14 
_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   1.0 
_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                        'APS BEAMLINE 17-ID' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.0 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   17-ID 
_diffrn_source.pdbx_synchrotron_site       APS 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9DI9 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.155 
_reflns.d_resolution_low                               89.35 
_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                                     26167 
_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                           86.8 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                13.2 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          15.6 
_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                                0.030 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.999 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.103 
_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                                    2.155 
_reflns_shell.d_res_low                                     2.292 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           1.1 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             1308 
_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                               13.5 
_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                               0.761 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.439 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          46.0 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  2.728 
_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]                            -1.4241 
_refine.aniso_B[1][2]                            0 
_refine.aniso_B[1][3]                            0 
_refine.aniso_B[2][2]                            -1.4241 
_refine.aniso_B[2][3]                            0 
_refine.aniso_B[3][3]                            2.8481 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               58.18 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.95 
_refine.correlation_coeff_Fo_to_Fc_free          0.941 
_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                                 9DI9 
_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                            2.155 
_refine.ls_d_res_low                             25.27 
_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                     26142 
_refine.ls_number_reflns_R_free                  1327 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    78.8 
_refine.ls_percent_reflns_R_free                 ? 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2074 
_refine.ls_R_factor_R_free                       0.2357 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2059 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    ? 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_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   0.177 
_refine.pdbx_overall_SU_R_free_Blow_DPI          0.178 
_refine.pdbx_overall_SU_R_Blow_DPI               0.207 
_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             0.202 
_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                        9DI9 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
_refine_analyze.Luzzati_coordinate_error_free   ? 
_refine_analyze.Luzzati_coordinate_error_obs    0.29 
_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                       2.155 
_refine_hist.d_res_low                        25.27 
_refine_hist.number_atoms_solvent             130 
_refine_hist.number_atoms_total               2714 
_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        2526 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         58 
_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' ? 0.007 ? 2639 ? t_bond_d                  2  HARMONIC     
'X-RAY DIFFRACTION' ? 0.84  ? 3580 ? t_angle_deg               2  HARMONIC     
'X-RAY DIFFRACTION' ? ?     ? 928  ? t_dihedral_angle_d        2  SINUSOIDAL   
'X-RAY DIFFRACTION' ? ?     ? 465  ? t_gen_planes              5  HARMONIC     
'X-RAY DIFFRACTION' ? ?     ? 2639 ? t_it                      10 HARMONIC     
'X-RAY DIFFRACTION' ? ?     ? 341  ? t_chiral_improper_torsion 5  SEMIHARMONIC 
'X-RAY DIFFRACTION' ? ?     ? 2053 ? t_ideal_dist_contact      4  SEMIHARMONIC 
'X-RAY DIFFRACTION' ? 2.77  ? ?    ? t_omega_torsion           ?  ?            
'X-RAY DIFFRACTION' ? 17.94 ? ?    ? t_other_torsion           ?  ?            
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       2.155 
_refine_ls_shell.d_res_low                        2.23 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             30 
_refine_ls_shell.number_reflns_R_work             ? 
_refine_ls_shell.percent_reflns_obs               15.61 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.R_factor_obs                     ? 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.R_factor_R_work                  0.2973 
_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                  0.3007 
# 
_struct.entry_id                     9DI9 
_struct.title                        'Rat branched chain ketoacid dehydrogenase kinase in complex with inhibitor' 
_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        9DI9 
_struct_keywords.text            
;branch chain ketoacid dehydrogenase, branch chain ketoacid dehydrogenase kinase, inhibitor, TRANSFERASE, TRANSFERASE-TRANSFERASE INHIBITOR complex
;
_struct_keywords.pdbx_keywords   'TRANSFERASE/TRANSFERASE INHIBITOR' 
# 
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 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    BCKD_HUMAN 
_struct_ref.pdbx_db_accession          O14874 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;STSATDTHHVEMARERSKTVTSFYNQSAIDAAAEKPSVRLTPTMMLYAGRSQDGSHLLKSARYLQQELPVRIAHRIKGFR
CLPFIIGCNPTILHVHELYIRAFQKLTDFPPIKDQADEAQYCQLVRQLLDDHKDVVTLLAEGLRESRKHIEDEKLVRYFL
DKTLTSRLGIRMLATHHLALHEDKPDFVGIICTRLSPKKIIEKWVDFARRLCEHKYGNAPRVRINGHVAARFPFIPMPLD
YILPELLKNAMRATMESHLDTPYNVPDVVITIANNDVDLIIRISDRGGGIAHKDLDRVMDYHFTTAEASTQDPRISPLFG
HLDMHSGAQSGPMHGFGFGLPTSRAYAEYLGGSLQLQSLQGIGTDVYLRLRHIDGREESFRI
;
_struct_ref.pdbx_align_begin           31 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              9DI9 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 1 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 382 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             O14874 
_struct_ref_seq.db_align_beg                  31 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  412 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       1 
_struct_ref_seq.pdbx_auth_seq_align_end       382 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 9DI9 LEU A 12  ? UNP O14874 MET 42  conflict         12  1  
1 9DI9 VAL A 31  ? UNP O14874 ALA 61  conflict         31  2  
1 9DI9 VAL A 32  ? UNP O14874 ALA 62  conflict         32  3  
1 9DI9 SER A 48  ? UNP O14874 ALA 78  conflict         48  4  
1 9DI9 GLY A 61  ? UNP O14874 ALA 91  conflict         61  5  
1 9DI9 SER A 81  ? UNP O14874 CYS 111 conflict         81  6  
1 9DI9 GLY A 328 ? UNP O14874 ALA 358 conflict         328 7  
1 9DI9 HIS A 383 ? UNP O14874 ?   ?   'expression tag' 383 8  
1 9DI9 HIS A 384 ? UNP O14874 ?   ?   'expression tag' 384 9  
1 9DI9 HIS A 385 ? UNP O14874 ?   ?   'expression tag' 385 10 
1 9DI9 HIS A 386 ? UNP O14874 ?   ?   'expression tag' 386 11 
1 9DI9 HIS A 387 ? UNP O14874 ?   ?   'expression tag' 387 12 
1 9DI9 HIS A 388 ? UNP O14874 ?   ?   'expression tag' 388 13 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 5720  ? 
1 MORE         -64   ? 
1 'SSA (A^2)'  29640 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1,2 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G 
# 
_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                ? 
# 
loop_
_pdbx_struct_oper_list.id 
_pdbx_struct_oper_list.type 
_pdbx_struct_oper_list.name 
_pdbx_struct_oper_list.symmetry_operation 
_pdbx_struct_oper_list.matrix[1][1] 
_pdbx_struct_oper_list.matrix[1][2] 
_pdbx_struct_oper_list.matrix[1][3] 
_pdbx_struct_oper_list.vector[1] 
_pdbx_struct_oper_list.matrix[2][1] 
_pdbx_struct_oper_list.matrix[2][2] 
_pdbx_struct_oper_list.matrix[2][3] 
_pdbx_struct_oper_list.vector[2] 
_pdbx_struct_oper_list.matrix[3][1] 
_pdbx_struct_oper_list.matrix[3][2] 
_pdbx_struct_oper_list.matrix[3][3] 
_pdbx_struct_oper_list.vector[3] 
1 'identity operation'         1_555 x,y,z  1.0000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000 
0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000  0.0000000000 
2 'crystal symmetry operation' 7_555 y,x,-z 0.0000000000 1.0000000000 0.0000000000 0.0000000000 1.0000000000 0.0000000000 
0.0000000000 0.0000000000 0.0000000000 0.0000000000 -1.0000000000 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 27  ? GLU A 34  ? SER A 27  GLU A 34  1 ? 8  
HELX_P HELX_P2  AA2 THR A 41  ? TYR A 47  ? THR A 41  TYR A 47  1 ? 7  
HELX_P HELX_P3  AA3 GLY A 54  ? SER A 81  ? GLY A 54  SER A 81  1 ? 28 
HELX_P HELX_P4  AA4 PRO A 83  ? CYS A 88  ? PRO A 83  CYS A 88  1 ? 6  
HELX_P HELX_P5  AA5 ASN A 89  ? PHE A 109 ? ASN A 89  PHE A 109 1 ? 21 
HELX_P HELX_P6  AA6 ASP A 114 ? HIS A 132 ? ASP A 114 HIS A 132 1 ? 19 
HELX_P HELX_P7  AA7 ASP A 134 ? GLU A 145 ? ASP A 134 GLU A 145 1 ? 12 
HELX_P HELX_P8  AA8 SER A 146 ? ILE A 150 ? SER A 146 ILE A 150 5 ? 5  
HELX_P HELX_P9  AA9 GLU A 153 ? LEU A 180 ? GLU A 153 LEU A 180 1 ? 28 
HELX_P HELX_P10 AB1 SER A 196 ? GLY A 217 ? SER A 196 GLY A 217 1 ? 22 
HELX_P HELX_P11 AB2 PRO A 236 ? SER A 257 ? PRO A 236 SER A 257 1 ? 22 
HELX_P HELX_P12 AB3 ALA A 291 ? ASP A 296 ? ALA A 291 ASP A 296 1 ? 6  
HELX_P HELX_P13 AB4 PHE A 338 ? LEU A 350 ? PHE A 338 LEU A 350 1 ? 13 
# 
_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 ASN 249 OD1 ? ? ? 1_555 C MG  . MG ? ? A ASN 249 A MG  402 1_555 ? ? ? ? ? ? ? 2.086 ? ? 
metalc2  metalc ? ? A VAL 298 O   ? ? ? 1_555 D K   . K  ? ? A VAL 298 A K   403 1_555 ? ? ? ? ? ? ? 2.891 ? ? 
metalc3  metalc ? ? A ASP 300 O   ? ? ? 1_555 D K   . K  ? ? A ASP 300 A K   403 1_555 ? ? ? ? ? ? ? 2.923 ? ? 
metalc4  metalc ? ? A PHE 303 O   ? ? ? 1_555 D K   . K  ? ? A PHE 303 A K   403 1_555 ? ? ? ? ? ? ? 2.639 ? ? 
metalc5  metalc ? ? A GLY 337 O   ? ? ? 1_555 D K   . K  ? ? A GLY 337 A K   403 1_555 ? ? ? ? ? ? ? 3.052 ? ? 
metalc6  metalc ? ? B ADP .   O3B ? ? ? 1_555 C MG  . MG ? ? A ADP 401 A MG  402 1_555 ? ? ? ? ? ? ? 2.108 ? ? 
metalc7  metalc ? ? B ADP .   O1A ? ? ? 1_555 C MG  . MG ? ? A ADP 401 A MG  402 1_555 ? ? ? ? ? ? ? 2.127 ? ? 
metalc8  metalc ? ? B ADP .   O2A ? ? ? 1_555 D K   . K  ? ? A ADP 401 A K   403 1_555 ? ? ? ? ? ? ? 2.830 ? ? 
metalc9  metalc ? ? C MG  .   MG  ? ? ? 1_555 F PO4 . O3 ? ? A MG  402 A PO4 405 1_555 ? ? ? ? ? ? ? 2.215 ? ? 
metalc10 metalc ? ? C MG  .   MG  ? ? ? 1_555 G HOH . O  ? ? A MG  402 A HOH 510 1_555 ? ? ? ? ? ? ? 2.055 ? ? 
metalc11 metalc ? ? C MG  .   MG  ? ? ? 1_555 G HOH . O  ? ? A MG  402 A HOH 523 1_555 ? ? ? ? ? ? ? 2.203 ? ? 
# 
_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  OD1 ? A ASN 249 ? A ASN 249 ? 1_555 MG ? C MG . ? A MG 402 ? 1_555 O3B ? B ADP .   ? A ADP 401 ? 1_555 100.9 ? 
2  OD1 ? A ASN 249 ? A ASN 249 ? 1_555 MG ? C MG . ? A MG 402 ? 1_555 O1A ? B ADP .   ? A ADP 401 ? 1_555 91.7  ? 
3  O3B ? B ADP .   ? A ADP 401 ? 1_555 MG ? C MG . ? A MG 402 ? 1_555 O1A ? B ADP .   ? A ADP 401 ? 1_555 84.0  ? 
4  OD1 ? A ASN 249 ? A ASN 249 ? 1_555 MG ? C MG . ? A MG 402 ? 1_555 O3  ? F PO4 .   ? A PO4 405 ? 1_555 161.6 ? 
5  O3B ? B ADP .   ? A ADP 401 ? 1_555 MG ? C MG . ? A MG 402 ? 1_555 O3  ? F PO4 .   ? A PO4 405 ? 1_555 92.6  ? 
6  O1A ? B ADP .   ? A ADP 401 ? 1_555 MG ? C MG . ? A MG 402 ? 1_555 O3  ? F PO4 .   ? A PO4 405 ? 1_555 77.3  ? 
7  OD1 ? A ASN 249 ? A ASN 249 ? 1_555 MG ? C MG . ? A MG 402 ? 1_555 O   ? G HOH .   ? A HOH 510 ? 1_555 86.5  ? 
8  O3B ? B ADP .   ? A ADP 401 ? 1_555 MG ? C MG . ? A MG 402 ? 1_555 O   ? G HOH .   ? A HOH 510 ? 1_555 172.5 ? 
9  O1A ? B ADP .   ? A ADP 401 ? 1_555 MG ? C MG . ? A MG 402 ? 1_555 O   ? G HOH .   ? A HOH 510 ? 1_555 94.4  ? 
10 O3  ? F PO4 .   ? A PO4 405 ? 1_555 MG ? C MG . ? A MG 402 ? 1_555 O   ? G HOH .   ? A HOH 510 ? 1_555 79.9  ? 
11 OD1 ? A ASN 249 ? A ASN 249 ? 1_555 MG ? C MG . ? A MG 402 ? 1_555 O   ? G HOH .   ? A HOH 523 ? 1_555 100.6 ? 
12 O3B ? B ADP .   ? A ADP 401 ? 1_555 MG ? C MG . ? A MG 402 ? 1_555 O   ? G HOH .   ? A HOH 523 ? 1_555 91.2  ? 
13 O1A ? B ADP .   ? A ADP 401 ? 1_555 MG ? C MG . ? A MG 402 ? 1_555 O   ? G HOH .   ? A HOH 523 ? 1_555 167.5 ? 
14 O3  ? F PO4 .   ? A PO4 405 ? 1_555 MG ? C MG . ? A MG 402 ? 1_555 O   ? G HOH .   ? A HOH 523 ? 1_555 91.5  ? 
15 O   ? G HOH .   ? A HOH 510 ? 1_555 MG ? C MG . ? A MG 402 ? 1_555 O   ? G HOH .   ? A HOH 523 ? 1_555 88.9  ? 
16 O   ? A VAL 298 ? A VAL 298 ? 1_555 K  ? D K  . ? A K  403 ? 1_555 O   ? A ASP 300 ? A ASP 300 ? 1_555 85.7  ? 
17 O   ? A VAL 298 ? A VAL 298 ? 1_555 K  ? D K  . ? A K  403 ? 1_555 O   ? A PHE 303 ? A PHE 303 ? 1_555 124.4 ? 
18 O   ? A ASP 300 ? A ASP 300 ? 1_555 K  ? D K  . ? A K  403 ? 1_555 O   ? A PHE 303 ? A PHE 303 ? 1_555 104.1 ? 
19 O   ? A VAL 298 ? A VAL 298 ? 1_555 K  ? D K  . ? A K  403 ? 1_555 O   ? A GLY 337 ? A GLY 337 ? 1_555 143.1 ? 
20 O   ? A ASP 300 ? A ASP 300 ? 1_555 K  ? D K  . ? A K  403 ? 1_555 O   ? A GLY 337 ? A GLY 337 ? 1_555 75.6  ? 
21 O   ? A PHE 303 ? A PHE 303 ? 1_555 K  ? D K  . ? A K  403 ? 1_555 O   ? A GLY 337 ? A GLY 337 ? 1_555 91.2  ? 
22 O   ? A VAL 298 ? A VAL 298 ? 1_555 K  ? D K  . ? A K  403 ? 1_555 O2A ? B ADP .   ? A ADP 401 ? 1_555 95.2  ? 
23 O   ? A ASP 300 ? A ASP 300 ? 1_555 K  ? D K  . ? A K  403 ? 1_555 O2A ? B ADP .   ? A ADP 401 ? 1_555 141.8 ? 
24 O   ? A PHE 303 ? A PHE 303 ? 1_555 K  ? D K  . ? A K  403 ? 1_555 O2A ? B ADP .   ? A ADP 401 ? 1_555 106.5 ? 
25 O   ? A GLY 337 ? A GLY 337 ? 1_555 K  ? D K  . ? A K  403 ? 1_555 O2A ? B ADP .   ? A ADP 401 ? 1_555 81.4  ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 3 ? 
AA2 ? 5 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA2 1 2 ? parallel      
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 PHE A 187 ? VAL A 188 ? PHE A 187 VAL A 188 
AA1 2 ILE A 191 ? LEU A 195 ? ILE A 191 LEU A 195 
AA1 3 PHE A 232 ? PHE A 234 ? PHE A 232 PHE A 234 
AA2 1 VAL A 222 ? GLY A 226 ? VAL A 222 GLY A 226 
AA2 2 VAL A 268 ? ASN A 274 ? VAL A 268 ASN A 274 
AA2 3 ASP A 278 ? SER A 284 ? ASP A 278 SER A 284 
AA2 4 GLY A 363 ? ARG A 371 ? GLY A 363 ARG A 371 
AA2 5 SER A 353 ? LEU A 359 ? SER A 353 LEU A 359 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N VAL A 188 ? N VAL A 188 O ILE A 191 ? O ILE A 191 
AA1 2 3 N CYS A 192 ? N CYS A 192 O PHE A 234 ? O PHE A 234 
AA2 1 2 N ARG A 223 ? N ARG A 223 O ILE A 270 ? O ILE A 270 
AA2 2 3 N VAL A 269 ? N VAL A 269 O SER A 284 ? O SER A 284 
AA2 3 4 N ILE A 281 ? N ILE A 281 O LEU A 368 ? O LEU A 368 
AA2 4 5 O TYR A 367 ? O TYR A 367 N GLN A 355 ? N GLN A 355 
# 
_pdbx_entry_details.entry_id                   9DI9 
_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 PRO A 36  ? ? -57.57  -92.41 
2 1 SER A 37  ? ? 138.14  102.98 
3 1 ASP A 183 ? ? -118.57 67.85  
4 1 HIS A 258 ? ? -140.11 42.12  
5 1 HIS A 302 ? ? 79.14   -13.03 
# 
_pdbx_struct_special_symmetry.id              1 
_pdbx_struct_special_symmetry.PDB_model_num   1 
_pdbx_struct_special_symmetry.auth_asym_id    A 
_pdbx_struct_special_symmetry.auth_comp_id    HOH 
_pdbx_struct_special_symmetry.auth_seq_id     611 
_pdbx_struct_special_symmetry.PDB_ins_code    ? 
_pdbx_struct_special_symmetry.label_asym_id   G 
_pdbx_struct_special_symmetry.label_comp_id   HOH 
_pdbx_struct_special_symmetry.label_seq_id    . 
# 
_pdbx_refine_tls.id               1 
_pdbx_refine_tls.pdbx_refine_id   'X-RAY DIFFRACTION' 
_pdbx_refine_tls.details          ? 
_pdbx_refine_tls.method           ? 
_pdbx_refine_tls.origin_x         29.5687 
_pdbx_refine_tls.origin_y         -1.8098 
_pdbx_refine_tls.origin_z         -10.3305 
_pdbx_refine_tls.T[1][1]          -0.0884 
_pdbx_refine_tls.T[1][1]_esd      ? 
_pdbx_refine_tls.T[1][2]          -0.003 
_pdbx_refine_tls.T[1][2]_esd      ? 
_pdbx_refine_tls.T[1][3]          0.0364 
_pdbx_refine_tls.T[1][3]_esd      ? 
_pdbx_refine_tls.T[2][2]          -0.0879 
_pdbx_refine_tls.T[2][2]_esd      ? 
_pdbx_refine_tls.T[2][3]          0.0185 
_pdbx_refine_tls.T[2][3]_esd      ? 
_pdbx_refine_tls.T[3][3]          -0.0564 
_pdbx_refine_tls.T[3][3]_esd      ? 
_pdbx_refine_tls.L[1][1]          0.6319 
_pdbx_refine_tls.L[1][1]_esd      ? 
_pdbx_refine_tls.L[1][2]          0.2834 
_pdbx_refine_tls.L[1][2]_esd      ? 
_pdbx_refine_tls.L[1][3]          -0.1713 
_pdbx_refine_tls.L[1][3]_esd      ? 
_pdbx_refine_tls.L[2][2]          1.9643 
_pdbx_refine_tls.L[2][2]_esd      ? 
_pdbx_refine_tls.L[2][3]          -0.4268 
_pdbx_refine_tls.L[2][3]_esd      ? 
_pdbx_refine_tls.L[3][3]          0.6114 
_pdbx_refine_tls.L[3][3]_esd      ? 
_pdbx_refine_tls.S[1][1]          -0.0409 
_pdbx_refine_tls.S[1][1]_esd      ? 
_pdbx_refine_tls.S[1][2]          -0.2407 
_pdbx_refine_tls.S[1][2]_esd      ? 
_pdbx_refine_tls.S[1][3]          0.011 
_pdbx_refine_tls.S[1][3]_esd      ? 
_pdbx_refine_tls.S[2][1]          -0.2407 
_pdbx_refine_tls.S[2][1]_esd      ? 
_pdbx_refine_tls.S[2][2]          -0.0021 
_pdbx_refine_tls.S[2][2]_esd      ? 
_pdbx_refine_tls.S[2][3]          -0.0148 
_pdbx_refine_tls.S[2][3]_esd      ? 
_pdbx_refine_tls.S[3][1]          0.011 
_pdbx_refine_tls.S[3][1]_esd      ? 
_pdbx_refine_tls.S[3][2]          -0.0148 
_pdbx_refine_tls.S[3][2]_esd      ? 
_pdbx_refine_tls.S[3][3]          0.043 
_pdbx_refine_tls.S[3][3]_esd      ? 
# 
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 27  ? ? ? A 374 ? ? '{ A|* }' 
2 'X-RAY DIFFRACTION' 1 ? ? A 401 ? ? ? A 501 ? ? '{ A|* }' 
# 
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 628 ? 10.48 . 
2 1 O ? A HOH 629 ? 11.26 . 
3 1 O ? A HOH 630 ? 13.70 . 
# 
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 SER 1   ? A SER 1   
2  1 Y 1 A THR 2   ? A THR 2   
3  1 Y 1 A SER 3   ? A SER 3   
4  1 Y 1 A ALA 4   ? A ALA 4   
5  1 Y 1 A THR 5   ? A THR 5   
6  1 Y 1 A ASP 6   ? A ASP 6   
7  1 Y 1 A THR 7   ? A THR 7   
8  1 Y 1 A HIS 8   ? A HIS 8   
9  1 Y 1 A HIS 9   ? A HIS 9   
10 1 Y 1 A VAL 10  ? A VAL 10  
11 1 Y 1 A GLU 11  ? A GLU 11  
12 1 Y 1 A LEU 12  ? A LEU 12  
13 1 Y 1 A ALA 13  ? A ALA 13  
14 1 Y 1 A ARG 14  ? A ARG 14  
15 1 Y 1 A GLU 15  ? A GLU 15  
16 1 Y 1 A ARG 16  ? A ARG 16  
17 1 Y 1 A SER 17  ? A SER 17  
18 1 Y 1 A LYS 18  ? A LYS 18  
19 1 Y 1 A THR 19  ? A THR 19  
20 1 Y 1 A VAL 20  ? A VAL 20  
21 1 Y 1 A THR 21  ? A THR 21  
22 1 Y 1 A SER 22  ? A SER 22  
23 1 Y 1 A PHE 23  ? A PHE 23  
24 1 Y 1 A TYR 24  ? A TYR 24  
25 1 Y 1 A ASN 25  ? A ASN 25  
26 1 Y 1 A GLN 26  ? A GLN 26  
27 1 Y 1 A SER 48  ? A SER 48  
28 1 Y 1 A GLY 49  ? A GLY 49  
29 1 Y 1 A ARG 50  ? A ARG 50  
30 1 Y 1 A SER 51  ? A SER 51  
31 1 Y 1 A GLN 52  ? A GLN 52  
32 1 Y 1 A GLU 307 ? A GLU 307 
33 1 Y 1 A ALA 308 ? A ALA 308 
34 1 Y 1 A SER 309 ? A SER 309 
35 1 Y 1 A THR 310 ? A THR 310 
36 1 Y 1 A GLN 311 ? A GLN 311 
37 1 Y 1 A ASP 312 ? A ASP 312 
38 1 Y 1 A PRO 313 ? A PRO 313 
39 1 Y 1 A ARG 314 ? A ARG 314 
40 1 Y 1 A ILE 315 ? A ILE 315 
41 1 Y 1 A SER 316 ? A SER 316 
42 1 Y 1 A PRO 317 ? A PRO 317 
43 1 Y 1 A LEU 318 ? A LEU 318 
44 1 Y 1 A PHE 319 ? A PHE 319 
45 1 Y 1 A GLY 320 ? A GLY 320 
46 1 Y 1 A HIS 321 ? A HIS 321 
47 1 Y 1 A LEU 322 ? A LEU 322 
48 1 Y 1 A ASP 323 ? A ASP 323 
49 1 Y 1 A MET 324 ? A MET 324 
50 1 Y 1 A HIS 325 ? A HIS 325 
51 1 Y 1 A SER 326 ? A SER 326 
52 1 Y 1 A GLY 327 ? A GLY 327 
53 1 Y 1 A GLY 328 ? A GLY 328 
54 1 Y 1 A GLN 329 ? A GLN 329 
55 1 Y 1 A SER 330 ? A SER 330 
56 1 Y 1 A GLY 331 ? A GLY 331 
57 1 Y 1 A PRO 332 ? A PRO 332 
58 1 Y 1 A MET 333 ? A MET 333 
59 1 Y 1 A HIS 334 ? A HIS 334 
60 1 Y 1 A GLY 375 ? A GLY 375 
61 1 Y 1 A ARG 376 ? A ARG 376 
62 1 Y 1 A GLU 377 ? A GLU 377 
63 1 Y 1 A GLU 378 ? A GLU 378 
64 1 Y 1 A SER 379 ? A SER 379 
65 1 Y 1 A PHE 380 ? A PHE 380 
66 1 Y 1 A ARG 381 ? A ARG 381 
67 1 Y 1 A ILE 382 ? A ILE 382 
68 1 Y 1 A HIS 383 ? A HIS 383 
69 1 Y 1 A HIS 384 ? A HIS 384 
70 1 Y 1 A HIS 385 ? A HIS 385 
71 1 Y 1 A HIS 386 ? A HIS 386 
72 1 Y 1 A HIS 387 ? A HIS 387 
73 1 Y 1 A HIS 388 ? A HIS 388 
# 
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 
A1A40 C4     C  Y N 1   
A1A40 C7     C  Y N 2   
A1A40 C6     C  Y N 3   
A1A40 C13    C  Y N 4   
A1A40 C20    C  N N 5   
A1A40 C8     C  Y N 6   
A1A40 C16    C  Y N 7   
A1A40 C19    C  Y N 8   
A1A40 C1     C  N N 9   
A1A40 O2     O  N N 10  
A1A40 C3     C  Y N 11  
A1A40 C5     C  Y N 12  
A1A40 F9     F  N N 13  
A1A40 F10    F  N N 14  
A1A40 C11    C  Y N 15  
A1A40 C12    C  Y N 16  
A1A40 C14    C  Y N 17  
A1A40 C15    C  Y N 18  
A1A40 C17    C  Y N 19  
A1A40 S18    S  Y N 20  
A1A40 O21    O  N N 21  
A1A40 O22    O  N N 22  
A1A40 F23    F  N N 23  
A1A40 F24    F  N N 24  
A1A40 H28    H  N N 25  
A1A40 H29    H  N N 26  
A1A40 H31    H  N N 27  
A1A40 H25    H  N N 28  
A1A40 H26    H  N N 29  
A1A40 H27    H  N N 30  
A1A40 H30    H  N N 31  
A1A40 H32    H  N N 32  
ADP   PB     P  N N 33  
ADP   O1B    O  N N 34  
ADP   O2B    O  N N 35  
ADP   O3B    O  N N 36  
ADP   PA     P  N S 37  
ADP   O1A    O  N N 38  
ADP   O2A    O  N N 39  
ADP   O3A    O  N N 40  
ADP   "O5'"  O  N N 41  
ADP   "C5'"  C  N N 42  
ADP   "C4'"  C  N R 43  
ADP   "O4'"  O  N N 44  
ADP   "C3'"  C  N S 45  
ADP   "O3'"  O  N N 46  
ADP   "C2'"  C  N R 47  
ADP   "O2'"  O  N N 48  
ADP   "C1'"  C  N R 49  
ADP   N9     N  Y N 50  
ADP   C8     C  Y N 51  
ADP   N7     N  Y N 52  
ADP   C5     C  Y N 53  
ADP   C6     C  Y N 54  
ADP   N6     N  N N 55  
ADP   N1     N  Y N 56  
ADP   C2     C  Y N 57  
ADP   N3     N  Y N 58  
ADP   C4     C  Y N 59  
ADP   HOB2   H  N N 60  
ADP   HOB3   H  N N 61  
ADP   HOA2   H  N N 62  
ADP   "H5'1" H  N N 63  
ADP   "H5'2" H  N N 64  
ADP   "H4'"  H  N N 65  
ADP   "H3'"  H  N N 66  
ADP   "HO3'" H  N N 67  
ADP   "H2'"  H  N N 68  
ADP   "HO2'" H  N N 69  
ADP   "H1'"  H  N N 70  
ADP   H8     H  N N 71  
ADP   HN61   H  N N 72  
ADP   HN62   H  N N 73  
ADP   H2     H  N N 74  
ALA   N      N  N N 75  
ALA   CA     C  N S 76  
ALA   C      C  N N 77  
ALA   O      O  N N 78  
ALA   CB     C  N N 79  
ALA   OXT    O  N N 80  
ALA   H      H  N N 81  
ALA   H2     H  N N 82  
ALA   HA     H  N N 83  
ALA   HB1    H  N N 84  
ALA   HB2    H  N N 85  
ALA   HB3    H  N N 86  
ALA   HXT    H  N N 87  
ARG   N      N  N N 88  
ARG   CA     C  N S 89  
ARG   C      C  N N 90  
ARG   O      O  N N 91  
ARG   CB     C  N N 92  
ARG   CG     C  N N 93  
ARG   CD     C  N N 94  
ARG   NE     N  N N 95  
ARG   CZ     C  N N 96  
ARG   NH1    N  N N 97  
ARG   NH2    N  N N 98  
ARG   OXT    O  N N 99  
ARG   H      H  N N 100 
ARG   H2     H  N N 101 
ARG   HA     H  N N 102 
ARG   HB2    H  N N 103 
ARG   HB3    H  N N 104 
ARG   HG2    H  N N 105 
ARG   HG3    H  N N 106 
ARG   HD2    H  N N 107 
ARG   HD3    H  N N 108 
ARG   HE     H  N N 109 
ARG   HH11   H  N N 110 
ARG   HH12   H  N N 111 
ARG   HH21   H  N N 112 
ARG   HH22   H  N N 113 
ARG   HXT    H  N N 114 
ASN   N      N  N N 115 
ASN   CA     C  N S 116 
ASN   C      C  N N 117 
ASN   O      O  N N 118 
ASN   CB     C  N N 119 
ASN   CG     C  N N 120 
ASN   OD1    O  N N 121 
ASN   ND2    N  N N 122 
ASN   OXT    O  N N 123 
ASN   H      H  N N 124 
ASN   H2     H  N N 125 
ASN   HA     H  N N 126 
ASN   HB2    H  N N 127 
ASN   HB3    H  N N 128 
ASN   HD21   H  N N 129 
ASN   HD22   H  N N 130 
ASN   HXT    H  N N 131 
ASP   N      N  N N 132 
ASP   CA     C  N S 133 
ASP   C      C  N N 134 
ASP   O      O  N N 135 
ASP   CB     C  N N 136 
ASP   CG     C  N N 137 
ASP   OD1    O  N N 138 
ASP   OD2    O  N N 139 
ASP   OXT    O  N N 140 
ASP   H      H  N N 141 
ASP   H2     H  N N 142 
ASP   HA     H  N N 143 
ASP   HB2    H  N N 144 
ASP   HB3    H  N N 145 
ASP   HD2    H  N N 146 
ASP   HXT    H  N N 147 
CYS   N      N  N N 148 
CYS   CA     C  N R 149 
CYS   C      C  N N 150 
CYS   O      O  N N 151 
CYS   CB     C  N N 152 
CYS   SG     S  N N 153 
CYS   OXT    O  N N 154 
CYS   H      H  N N 155 
CYS   H2     H  N N 156 
CYS   HA     H  N N 157 
CYS   HB2    H  N N 158 
CYS   HB3    H  N N 159 
CYS   HG     H  N N 160 
CYS   HXT    H  N N 161 
GLN   N      N  N N 162 
GLN   CA     C  N S 163 
GLN   C      C  N N 164 
GLN   O      O  N N 165 
GLN   CB     C  N N 166 
GLN   CG     C  N N 167 
GLN   CD     C  N N 168 
GLN   OE1    O  N N 169 
GLN   NE2    N  N N 170 
GLN   OXT    O  N N 171 
GLN   H      H  N N 172 
GLN   H2     H  N N 173 
GLN   HA     H  N N 174 
GLN   HB2    H  N N 175 
GLN   HB3    H  N N 176 
GLN   HG2    H  N N 177 
GLN   HG3    H  N N 178 
GLN   HE21   H  N N 179 
GLN   HE22   H  N N 180 
GLN   HXT    H  N N 181 
GLU   N      N  N N 182 
GLU   CA     C  N S 183 
GLU   C      C  N N 184 
GLU   O      O  N N 185 
GLU   CB     C  N N 186 
GLU   CG     C  N N 187 
GLU   CD     C  N N 188 
GLU   OE1    O  N N 189 
GLU   OE2    O  N N 190 
GLU   OXT    O  N N 191 
GLU   H      H  N N 192 
GLU   H2     H  N N 193 
GLU   HA     H  N N 194 
GLU   HB2    H  N N 195 
GLU   HB3    H  N N 196 
GLU   HG2    H  N N 197 
GLU   HG3    H  N N 198 
GLU   HE2    H  N N 199 
GLU   HXT    H  N N 200 
GLY   N      N  N N 201 
GLY   CA     C  N N 202 
GLY   C      C  N N 203 
GLY   O      O  N N 204 
GLY   OXT    O  N N 205 
GLY   H      H  N N 206 
GLY   H2     H  N N 207 
GLY   HA2    H  N N 208 
GLY   HA3    H  N N 209 
GLY   HXT    H  N N 210 
HIS   N      N  N N 211 
HIS   CA     C  N S 212 
HIS   C      C  N N 213 
HIS   O      O  N N 214 
HIS   CB     C  N N 215 
HIS   CG     C  Y N 216 
HIS   ND1    N  Y N 217 
HIS   CD2    C  Y N 218 
HIS   CE1    C  Y N 219 
HIS   NE2    N  Y N 220 
HIS   OXT    O  N N 221 
HIS   H      H  N N 222 
HIS   H2     H  N N 223 
HIS   HA     H  N N 224 
HIS   HB2    H  N N 225 
HIS   HB3    H  N N 226 
HIS   HD1    H  N N 227 
HIS   HD2    H  N N 228 
HIS   HE1    H  N N 229 
HIS   HE2    H  N N 230 
HIS   HXT    H  N N 231 
HOH   O      O  N N 232 
HOH   H1     H  N N 233 
HOH   H2     H  N N 234 
ILE   N      N  N N 235 
ILE   CA     C  N S 236 
ILE   C      C  N N 237 
ILE   O      O  N N 238 
ILE   CB     C  N S 239 
ILE   CG1    C  N N 240 
ILE   CG2    C  N N 241 
ILE   CD1    C  N N 242 
ILE   OXT    O  N N 243 
ILE   H      H  N N 244 
ILE   H2     H  N N 245 
ILE   HA     H  N N 246 
ILE   HB     H  N N 247 
ILE   HG12   H  N N 248 
ILE   HG13   H  N N 249 
ILE   HG21   H  N N 250 
ILE   HG22   H  N N 251 
ILE   HG23   H  N N 252 
ILE   HD11   H  N N 253 
ILE   HD12   H  N N 254 
ILE   HD13   H  N N 255 
ILE   HXT    H  N N 256 
K     K      K  N N 257 
LEU   N      N  N N 258 
LEU   CA     C  N S 259 
LEU   C      C  N N 260 
LEU   O      O  N N 261 
LEU   CB     C  N N 262 
LEU   CG     C  N N 263 
LEU   CD1    C  N N 264 
LEU   CD2    C  N N 265 
LEU   OXT    O  N N 266 
LEU   H      H  N N 267 
LEU   H2     H  N N 268 
LEU   HA     H  N N 269 
LEU   HB2    H  N N 270 
LEU   HB3    H  N N 271 
LEU   HG     H  N N 272 
LEU   HD11   H  N N 273 
LEU   HD12   H  N N 274 
LEU   HD13   H  N N 275 
LEU   HD21   H  N N 276 
LEU   HD22   H  N N 277 
LEU   HD23   H  N N 278 
LEU   HXT    H  N N 279 
LYS   N      N  N N 280 
LYS   CA     C  N S 281 
LYS   C      C  N N 282 
LYS   O      O  N N 283 
LYS   CB     C  N N 284 
LYS   CG     C  N N 285 
LYS   CD     C  N N 286 
LYS   CE     C  N N 287 
LYS   NZ     N  N N 288 
LYS   OXT    O  N N 289 
LYS   H      H  N N 290 
LYS   H2     H  N N 291 
LYS   HA     H  N N 292 
LYS   HB2    H  N N 293 
LYS   HB3    H  N N 294 
LYS   HG2    H  N N 295 
LYS   HG3    H  N N 296 
LYS   HD2    H  N N 297 
LYS   HD3    H  N N 298 
LYS   HE2    H  N N 299 
LYS   HE3    H  N N 300 
LYS   HZ1    H  N N 301 
LYS   HZ2    H  N N 302 
LYS   HZ3    H  N N 303 
LYS   HXT    H  N N 304 
MET   N      N  N N 305 
MET   CA     C  N S 306 
MET   C      C  N N 307 
MET   O      O  N N 308 
MET   CB     C  N N 309 
MET   CG     C  N N 310 
MET   SD     S  N N 311 
MET   CE     C  N N 312 
MET   OXT    O  N N 313 
MET   H      H  N N 314 
MET   H2     H  N N 315 
MET   HA     H  N N 316 
MET   HB2    H  N N 317 
MET   HB3    H  N N 318 
MET   HG2    H  N N 319 
MET   HG3    H  N N 320 
MET   HE1    H  N N 321 
MET   HE2    H  N N 322 
MET   HE3    H  N N 323 
MET   HXT    H  N N 324 
MG    MG     MG N N 325 
PHE   N      N  N N 326 
PHE   CA     C  N S 327 
PHE   C      C  N N 328 
PHE   O      O  N N 329 
PHE   CB     C  N N 330 
PHE   CG     C  Y N 331 
PHE   CD1    C  Y N 332 
PHE   CD2    C  Y N 333 
PHE   CE1    C  Y N 334 
PHE   CE2    C  Y N 335 
PHE   CZ     C  Y N 336 
PHE   OXT    O  N N 337 
PHE   H      H  N N 338 
PHE   H2     H  N N 339 
PHE   HA     H  N N 340 
PHE   HB2    H  N N 341 
PHE   HB3    H  N N 342 
PHE   HD1    H  N N 343 
PHE   HD2    H  N N 344 
PHE   HE1    H  N N 345 
PHE   HE2    H  N N 346 
PHE   HZ     H  N N 347 
PHE   HXT    H  N N 348 
PO4   P      P  N N 349 
PO4   O1     O  N N 350 
PO4   O2     O  N N 351 
PO4   O3     O  N N 352 
PO4   O4     O  N N 353 
PRO   N      N  N N 354 
PRO   CA     C  N S 355 
PRO   C      C  N N 356 
PRO   O      O  N N 357 
PRO   CB     C  N N 358 
PRO   CG     C  N N 359 
PRO   CD     C  N N 360 
PRO   OXT    O  N N 361 
PRO   H      H  N N 362 
PRO   HA     H  N N 363 
PRO   HB2    H  N N 364 
PRO   HB3    H  N N 365 
PRO   HG2    H  N N 366 
PRO   HG3    H  N N 367 
PRO   HD2    H  N N 368 
PRO   HD3    H  N N 369 
PRO   HXT    H  N N 370 
SER   N      N  N N 371 
SER   CA     C  N S 372 
SER   C      C  N N 373 
SER   O      O  N N 374 
SER   CB     C  N N 375 
SER   OG     O  N N 376 
SER   OXT    O  N N 377 
SER   H      H  N N 378 
SER   H2     H  N N 379 
SER   HA     H  N N 380 
SER   HB2    H  N N 381 
SER   HB3    H  N N 382 
SER   HG     H  N N 383 
SER   HXT    H  N N 384 
THR   N      N  N N 385 
THR   CA     C  N S 386 
THR   C      C  N N 387 
THR   O      O  N N 388 
THR   CB     C  N R 389 
THR   OG1    O  N N 390 
THR   CG2    C  N N 391 
THR   OXT    O  N N 392 
THR   H      H  N N 393 
THR   H2     H  N N 394 
THR   HA     H  N N 395 
THR   HB     H  N N 396 
THR   HG1    H  N N 397 
THR   HG21   H  N N 398 
THR   HG22   H  N N 399 
THR   HG23   H  N N 400 
THR   HXT    H  N N 401 
TRP   N      N  N N 402 
TRP   CA     C  N S 403 
TRP   C      C  N N 404 
TRP   O      O  N N 405 
TRP   CB     C  N N 406 
TRP   CG     C  Y N 407 
TRP   CD1    C  Y N 408 
TRP   CD2    C  Y N 409 
TRP   NE1    N  Y N 410 
TRP   CE2    C  Y N 411 
TRP   CE3    C  Y N 412 
TRP   CZ2    C  Y N 413 
TRP   CZ3    C  Y N 414 
TRP   CH2    C  Y N 415 
TRP   OXT    O  N N 416 
TRP   H      H  N N 417 
TRP   H2     H  N N 418 
TRP   HA     H  N N 419 
TRP   HB2    H  N N 420 
TRP   HB3    H  N N 421 
TRP   HD1    H  N N 422 
TRP   HE1    H  N N 423 
TRP   HE3    H  N N 424 
TRP   HZ2    H  N N 425 
TRP   HZ3    H  N N 426 
TRP   HH2    H  N N 427 
TRP   HXT    H  N N 428 
TYR   N      N  N N 429 
TYR   CA     C  N S 430 
TYR   C      C  N N 431 
TYR   O      O  N N 432 
TYR   CB     C  N N 433 
TYR   CG     C  Y N 434 
TYR   CD1    C  Y N 435 
TYR   CD2    C  Y N 436 
TYR   CE1    C  Y N 437 
TYR   CE2    C  Y N 438 
TYR   CZ     C  Y N 439 
TYR   OH     O  N N 440 
TYR   OXT    O  N N 441 
TYR   H      H  N N 442 
TYR   H2     H  N N 443 
TYR   HA     H  N N 444 
TYR   HB2    H  N N 445 
TYR   HB3    H  N N 446 
TYR   HD1    H  N N 447 
TYR   HD2    H  N N 448 
TYR   HE1    H  N N 449 
TYR   HE2    H  N N 450 
TYR   HH     H  N N 451 
TYR   HXT    H  N N 452 
VAL   N      N  N N 453 
VAL   CA     C  N S 454 
VAL   C      C  N N 455 
VAL   O      O  N N 456 
VAL   CB     C  N N 457 
VAL   CG1    C  N N 458 
VAL   CG2    C  N N 459 
VAL   OXT    O  N N 460 
VAL   H      H  N N 461 
VAL   H2     H  N N 462 
VAL   HA     H  N N 463 
VAL   HB     H  N N 464 
VAL   HG11   H  N N 465 
VAL   HG12   H  N N 466 
VAL   HG13   H  N N 467 
VAL   HG21   H  N N 468 
VAL   HG22   H  N N 469 
VAL   HG23   H  N N 470 
VAL   HXT    H  N N 471 
# 
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 
A1A40 C1    O2     sing N N 1   
A1A40 O2    C3     sing N N 2   
A1A40 C3    C8     doub Y N 3   
A1A40 C3    C4     sing Y N 4   
A1A40 C4    C5     doub Y N 5   
A1A40 C4    F24    sing N N 6   
A1A40 C5    C6     sing Y N 7   
A1A40 C5    C11    sing N N 8   
A1A40 C6    C7     doub Y N 9   
A1A40 C7    C8     sing Y N 10  
A1A40 C7    F10    sing N N 11  
A1A40 C8    F9     sing N N 12  
A1A40 C11   C19    doub Y N 13  
A1A40 C11   C12    sing Y N 14  
A1A40 C12   C17    doub Y N 15  
A1A40 C12   C13    sing Y N 16  
A1A40 C13   C14    doub Y N 17  
A1A40 C14   C15    sing Y N 18  
A1A40 C15   C16    doub Y N 19  
A1A40 C15   F23    sing N N 20  
A1A40 C16   C17    sing Y N 21  
A1A40 C17   S18    sing Y N 22  
A1A40 S18   C19    sing Y N 23  
A1A40 C19   C20    sing N N 24  
A1A40 C20   O21    doub N N 25  
A1A40 C20   O22    sing N N 26  
A1A40 C6    H28    sing N N 27  
A1A40 C13   H29    sing N N 28  
A1A40 C16   H31    sing N N 29  
A1A40 C1    H25    sing N N 30  
A1A40 C1    H26    sing N N 31  
A1A40 C1    H27    sing N N 32  
A1A40 C14   H30    sing N N 33  
A1A40 O22   H32    sing N N 34  
ADP   PB    O1B    doub N N 35  
ADP   PB    O2B    sing N N 36  
ADP   PB    O3B    sing N N 37  
ADP   PB    O3A    sing N N 38  
ADP   O2B   HOB2   sing N N 39  
ADP   O3B   HOB3   sing N N 40  
ADP   PA    O1A    doub N N 41  
ADP   PA    O2A    sing N N 42  
ADP   PA    O3A    sing N N 43  
ADP   PA    "O5'"  sing N N 44  
ADP   O2A   HOA2   sing N N 45  
ADP   "O5'" "C5'"  sing N N 46  
ADP   "C5'" "C4'"  sing N N 47  
ADP   "C5'" "H5'1" sing N N 48  
ADP   "C5'" "H5'2" sing N N 49  
ADP   "C4'" "O4'"  sing N N 50  
ADP   "C4'" "C3'"  sing N N 51  
ADP   "C4'" "H4'"  sing N N 52  
ADP   "O4'" "C1'"  sing N N 53  
ADP   "C3'" "O3'"  sing N N 54  
ADP   "C3'" "C2'"  sing N N 55  
ADP   "C3'" "H3'"  sing N N 56  
ADP   "O3'" "HO3'" sing N N 57  
ADP   "C2'" "O2'"  sing N N 58  
ADP   "C2'" "C1'"  sing N N 59  
ADP   "C2'" "H2'"  sing N N 60  
ADP   "O2'" "HO2'" sing N N 61  
ADP   "C1'" N9     sing N N 62  
ADP   "C1'" "H1'"  sing N N 63  
ADP   N9    C8     sing Y N 64  
ADP   N9    C4     sing Y N 65  
ADP   C8    N7     doub Y N 66  
ADP   C8    H8     sing N N 67  
ADP   N7    C5     sing Y N 68  
ADP   C5    C6     sing Y N 69  
ADP   C5    C4     doub Y N 70  
ADP   C6    N6     sing N N 71  
ADP   C6    N1     doub Y N 72  
ADP   N6    HN61   sing N N 73  
ADP   N6    HN62   sing N N 74  
ADP   N1    C2     sing Y N 75  
ADP   C2    N3     doub Y N 76  
ADP   C2    H2     sing N N 77  
ADP   N3    C4     sing Y N 78  
ALA   N     CA     sing N N 79  
ALA   N     H      sing N N 80  
ALA   N     H2     sing N N 81  
ALA   CA    C      sing N N 82  
ALA   CA    CB     sing N N 83  
ALA   CA    HA     sing N N 84  
ALA   C     O      doub N N 85  
ALA   C     OXT    sing N N 86  
ALA   CB    HB1    sing N N 87  
ALA   CB    HB2    sing N N 88  
ALA   CB    HB3    sing N N 89  
ALA   OXT   HXT    sing N N 90  
ARG   N     CA     sing N N 91  
ARG   N     H      sing N N 92  
ARG   N     H2     sing N N 93  
ARG   CA    C      sing N N 94  
ARG   CA    CB     sing N N 95  
ARG   CA    HA     sing N N 96  
ARG   C     O      doub N N 97  
ARG   C     OXT    sing N N 98  
ARG   CB    CG     sing N N 99  
ARG   CB    HB2    sing N N 100 
ARG   CB    HB3    sing N N 101 
ARG   CG    CD     sing N N 102 
ARG   CG    HG2    sing N N 103 
ARG   CG    HG3    sing N N 104 
ARG   CD    NE     sing N N 105 
ARG   CD    HD2    sing N N 106 
ARG   CD    HD3    sing N N 107 
ARG   NE    CZ     sing N N 108 
ARG   NE    HE     sing N N 109 
ARG   CZ    NH1    sing N N 110 
ARG   CZ    NH2    doub N N 111 
ARG   NH1   HH11   sing N N 112 
ARG   NH1   HH12   sing N N 113 
ARG   NH2   HH21   sing N N 114 
ARG   NH2   HH22   sing N N 115 
ARG   OXT   HXT    sing N N 116 
ASN   N     CA     sing N N 117 
ASN   N     H      sing N N 118 
ASN   N     H2     sing N N 119 
ASN   CA    C      sing N N 120 
ASN   CA    CB     sing N N 121 
ASN   CA    HA     sing N N 122 
ASN   C     O      doub N N 123 
ASN   C     OXT    sing N N 124 
ASN   CB    CG     sing N N 125 
ASN   CB    HB2    sing N N 126 
ASN   CB    HB3    sing N N 127 
ASN   CG    OD1    doub N N 128 
ASN   CG    ND2    sing N N 129 
ASN   ND2   HD21   sing N N 130 
ASN   ND2   HD22   sing N N 131 
ASN   OXT   HXT    sing N N 132 
ASP   N     CA     sing N N 133 
ASP   N     H      sing N N 134 
ASP   N     H2     sing N N 135 
ASP   CA    C      sing N N 136 
ASP   CA    CB     sing N N 137 
ASP   CA    HA     sing N N 138 
ASP   C     O      doub N N 139 
ASP   C     OXT    sing N N 140 
ASP   CB    CG     sing N N 141 
ASP   CB    HB2    sing N N 142 
ASP   CB    HB3    sing N N 143 
ASP   CG    OD1    doub N N 144 
ASP   CG    OD2    sing N N 145 
ASP   OD2   HD2    sing N N 146 
ASP   OXT   HXT    sing N N 147 
CYS   N     CA     sing N N 148 
CYS   N     H      sing N N 149 
CYS   N     H2     sing N N 150 
CYS   CA    C      sing N N 151 
CYS   CA    CB     sing N N 152 
CYS   CA    HA     sing N N 153 
CYS   C     O      doub N N 154 
CYS   C     OXT    sing N N 155 
CYS   CB    SG     sing N N 156 
CYS   CB    HB2    sing N N 157 
CYS   CB    HB3    sing N N 158 
CYS   SG    HG     sing N N 159 
CYS   OXT   HXT    sing N N 160 
GLN   N     CA     sing N N 161 
GLN   N     H      sing N N 162 
GLN   N     H2     sing N N 163 
GLN   CA    C      sing N N 164 
GLN   CA    CB     sing N N 165 
GLN   CA    HA     sing N N 166 
GLN   C     O      doub N N 167 
GLN   C     OXT    sing N N 168 
GLN   CB    CG     sing N N 169 
GLN   CB    HB2    sing N N 170 
GLN   CB    HB3    sing N N 171 
GLN   CG    CD     sing N N 172 
GLN   CG    HG2    sing N N 173 
GLN   CG    HG3    sing N N 174 
GLN   CD    OE1    doub N N 175 
GLN   CD    NE2    sing N N 176 
GLN   NE2   HE21   sing N N 177 
GLN   NE2   HE22   sing N N 178 
GLN   OXT   HXT    sing N N 179 
GLU   N     CA     sing N N 180 
GLU   N     H      sing N N 181 
GLU   N     H2     sing N N 182 
GLU   CA    C      sing N N 183 
GLU   CA    CB     sing N N 184 
GLU   CA    HA     sing N N 185 
GLU   C     O      doub N N 186 
GLU   C     OXT    sing N N 187 
GLU   CB    CG     sing N N 188 
GLU   CB    HB2    sing N N 189 
GLU   CB    HB3    sing N N 190 
GLU   CG    CD     sing N N 191 
GLU   CG    HG2    sing N N 192 
GLU   CG    HG3    sing N N 193 
GLU   CD    OE1    doub N N 194 
GLU   CD    OE2    sing N N 195 
GLU   OE2   HE2    sing N N 196 
GLU   OXT   HXT    sing N N 197 
GLY   N     CA     sing N N 198 
GLY   N     H      sing N N 199 
GLY   N     H2     sing N N 200 
GLY   CA    C      sing N N 201 
GLY   CA    HA2    sing N N 202 
GLY   CA    HA3    sing N N 203 
GLY   C     O      doub N N 204 
GLY   C     OXT    sing N N 205 
GLY   OXT   HXT    sing N N 206 
HIS   N     CA     sing N N 207 
HIS   N     H      sing N N 208 
HIS   N     H2     sing N N 209 
HIS   CA    C      sing N N 210 
HIS   CA    CB     sing N N 211 
HIS   CA    HA     sing N N 212 
HIS   C     O      doub N N 213 
HIS   C     OXT    sing N N 214 
HIS   CB    CG     sing N N 215 
HIS   CB    HB2    sing N N 216 
HIS   CB    HB3    sing N N 217 
HIS   CG    ND1    sing Y N 218 
HIS   CG    CD2    doub Y N 219 
HIS   ND1   CE1    doub Y N 220 
HIS   ND1   HD1    sing N N 221 
HIS   CD2   NE2    sing Y N 222 
HIS   CD2   HD2    sing N N 223 
HIS   CE1   NE2    sing Y N 224 
HIS   CE1   HE1    sing N N 225 
HIS   NE2   HE2    sing N N 226 
HIS   OXT   HXT    sing N N 227 
HOH   O     H1     sing N N 228 
HOH   O     H2     sing N N 229 
ILE   N     CA     sing N N 230 
ILE   N     H      sing N N 231 
ILE   N     H2     sing N N 232 
ILE   CA    C      sing N N 233 
ILE   CA    CB     sing N N 234 
ILE   CA    HA     sing N N 235 
ILE   C     O      doub N N 236 
ILE   C     OXT    sing N N 237 
ILE   CB    CG1    sing N N 238 
ILE   CB    CG2    sing N N 239 
ILE   CB    HB     sing N N 240 
ILE   CG1   CD1    sing N N 241 
ILE   CG1   HG12   sing N N 242 
ILE   CG1   HG13   sing N N 243 
ILE   CG2   HG21   sing N N 244 
ILE   CG2   HG22   sing N N 245 
ILE   CG2   HG23   sing N N 246 
ILE   CD1   HD11   sing N N 247 
ILE   CD1   HD12   sing N N 248 
ILE   CD1   HD13   sing N N 249 
ILE   OXT   HXT    sing N N 250 
LEU   N     CA     sing N N 251 
LEU   N     H      sing N N 252 
LEU   N     H2     sing N N 253 
LEU   CA    C      sing N N 254 
LEU   CA    CB     sing N N 255 
LEU   CA    HA     sing N N 256 
LEU   C     O      doub N N 257 
LEU   C     OXT    sing N N 258 
LEU   CB    CG     sing N N 259 
LEU   CB    HB2    sing N N 260 
LEU   CB    HB3    sing N N 261 
LEU   CG    CD1    sing N N 262 
LEU   CG    CD2    sing N N 263 
LEU   CG    HG     sing N N 264 
LEU   CD1   HD11   sing N N 265 
LEU   CD1   HD12   sing N N 266 
LEU   CD1   HD13   sing N N 267 
LEU   CD2   HD21   sing N N 268 
LEU   CD2   HD22   sing N N 269 
LEU   CD2   HD23   sing N N 270 
LEU   OXT   HXT    sing N N 271 
LYS   N     CA     sing N N 272 
LYS   N     H      sing N N 273 
LYS   N     H2     sing N N 274 
LYS   CA    C      sing N N 275 
LYS   CA    CB     sing N N 276 
LYS   CA    HA     sing N N 277 
LYS   C     O      doub N N 278 
LYS   C     OXT    sing N N 279 
LYS   CB    CG     sing N N 280 
LYS   CB    HB2    sing N N 281 
LYS   CB    HB3    sing N N 282 
LYS   CG    CD     sing N N 283 
LYS   CG    HG2    sing N N 284 
LYS   CG    HG3    sing N N 285 
LYS   CD    CE     sing N N 286 
LYS   CD    HD2    sing N N 287 
LYS   CD    HD3    sing N N 288 
LYS   CE    NZ     sing N N 289 
LYS   CE    HE2    sing N N 290 
LYS   CE    HE3    sing N N 291 
LYS   NZ    HZ1    sing N N 292 
LYS   NZ    HZ2    sing N N 293 
LYS   NZ    HZ3    sing N N 294 
LYS   OXT   HXT    sing N N 295 
MET   N     CA     sing N N 296 
MET   N     H      sing N N 297 
MET   N     H2     sing N N 298 
MET   CA    C      sing N N 299 
MET   CA    CB     sing N N 300 
MET   CA    HA     sing N N 301 
MET   C     O      doub N N 302 
MET   C     OXT    sing N N 303 
MET   CB    CG     sing N N 304 
MET   CB    HB2    sing N N 305 
MET   CB    HB3    sing N N 306 
MET   CG    SD     sing N N 307 
MET   CG    HG2    sing N N 308 
MET   CG    HG3    sing N N 309 
MET   SD    CE     sing N N 310 
MET   CE    HE1    sing N N 311 
MET   CE    HE2    sing N N 312 
MET   CE    HE3    sing N N 313 
MET   OXT   HXT    sing N N 314 
PHE   N     CA     sing N N 315 
PHE   N     H      sing N N 316 
PHE   N     H2     sing N N 317 
PHE   CA    C      sing N N 318 
PHE   CA    CB     sing N N 319 
PHE   CA    HA     sing N N 320 
PHE   C     O      doub N N 321 
PHE   C     OXT    sing N N 322 
PHE   CB    CG     sing N N 323 
PHE   CB    HB2    sing N N 324 
PHE   CB    HB3    sing N N 325 
PHE   CG    CD1    doub Y N 326 
PHE   CG    CD2    sing Y N 327 
PHE   CD1   CE1    sing Y N 328 
PHE   CD1   HD1    sing N N 329 
PHE   CD2   CE2    doub Y N 330 
PHE   CD2   HD2    sing N N 331 
PHE   CE1   CZ     doub Y N 332 
PHE   CE1   HE1    sing N N 333 
PHE   CE2   CZ     sing Y N 334 
PHE   CE2   HE2    sing N N 335 
PHE   CZ    HZ     sing N N 336 
PHE   OXT   HXT    sing N N 337 
PO4   P     O1     doub N N 338 
PO4   P     O2     sing N N 339 
PO4   P     O3     sing N N 340 
PO4   P     O4     sing N N 341 
PRO   N     CA     sing N N 342 
PRO   N     CD     sing N N 343 
PRO   N     H      sing N N 344 
PRO   CA    C      sing N N 345 
PRO   CA    CB     sing N N 346 
PRO   CA    HA     sing N N 347 
PRO   C     O      doub N N 348 
PRO   C     OXT    sing N N 349 
PRO   CB    CG     sing N N 350 
PRO   CB    HB2    sing N N 351 
PRO   CB    HB3    sing N N 352 
PRO   CG    CD     sing N N 353 
PRO   CG    HG2    sing N N 354 
PRO   CG    HG3    sing N N 355 
PRO   CD    HD2    sing N N 356 
PRO   CD    HD3    sing N N 357 
PRO   OXT   HXT    sing N N 358 
SER   N     CA     sing N N 359 
SER   N     H      sing N N 360 
SER   N     H2     sing N N 361 
SER   CA    C      sing N N 362 
SER   CA    CB     sing N N 363 
SER   CA    HA     sing N N 364 
SER   C     O      doub N N 365 
SER   C     OXT    sing N N 366 
SER   CB    OG     sing N N 367 
SER   CB    HB2    sing N N 368 
SER   CB    HB3    sing N N 369 
SER   OG    HG     sing N N 370 
SER   OXT   HXT    sing N N 371 
THR   N     CA     sing N N 372 
THR   N     H      sing N N 373 
THR   N     H2     sing N N 374 
THR   CA    C      sing N N 375 
THR   CA    CB     sing N N 376 
THR   CA    HA     sing N N 377 
THR   C     O      doub N N 378 
THR   C     OXT    sing N N 379 
THR   CB    OG1    sing N N 380 
THR   CB    CG2    sing N N 381 
THR   CB    HB     sing N N 382 
THR   OG1   HG1    sing N N 383 
THR   CG2   HG21   sing N N 384 
THR   CG2   HG22   sing N N 385 
THR   CG2   HG23   sing N N 386 
THR   OXT   HXT    sing N N 387 
TRP   N     CA     sing N N 388 
TRP   N     H      sing N N 389 
TRP   N     H2     sing N N 390 
TRP   CA    C      sing N N 391 
TRP   CA    CB     sing N N 392 
TRP   CA    HA     sing N N 393 
TRP   C     O      doub N N 394 
TRP   C     OXT    sing N N 395 
TRP   CB    CG     sing N N 396 
TRP   CB    HB2    sing N N 397 
TRP   CB    HB3    sing N N 398 
TRP   CG    CD1    doub Y N 399 
TRP   CG    CD2    sing Y N 400 
TRP   CD1   NE1    sing Y N 401 
TRP   CD1   HD1    sing N N 402 
TRP   CD2   CE2    doub Y N 403 
TRP   CD2   CE3    sing Y N 404 
TRP   NE1   CE2    sing Y N 405 
TRP   NE1   HE1    sing N N 406 
TRP   CE2   CZ2    sing Y N 407 
TRP   CE3   CZ3    doub Y N 408 
TRP   CE3   HE3    sing N N 409 
TRP   CZ2   CH2    doub Y N 410 
TRP   CZ2   HZ2    sing N N 411 
TRP   CZ3   CH2    sing Y N 412 
TRP   CZ3   HZ3    sing N N 413 
TRP   CH2   HH2    sing N N 414 
TRP   OXT   HXT    sing N N 415 
TYR   N     CA     sing N N 416 
TYR   N     H      sing N N 417 
TYR   N     H2     sing N N 418 
TYR   CA    C      sing N N 419 
TYR   CA    CB     sing N N 420 
TYR   CA    HA     sing N N 421 
TYR   C     O      doub N N 422 
TYR   C     OXT    sing N N 423 
TYR   CB    CG     sing N N 424 
TYR   CB    HB2    sing N N 425 
TYR   CB    HB3    sing N N 426 
TYR   CG    CD1    doub Y N 427 
TYR   CG    CD2    sing Y N 428 
TYR   CD1   CE1    sing Y N 429 
TYR   CD1   HD1    sing N N 430 
TYR   CD2   CE2    doub Y N 431 
TYR   CD2   HD2    sing N N 432 
TYR   CE1   CZ     doub Y N 433 
TYR   CE1   HE1    sing N N 434 
TYR   CE2   CZ     sing Y N 435 
TYR   CE2   HE2    sing N N 436 
TYR   CZ    OH     sing N N 437 
TYR   OH    HH     sing N N 438 
TYR   OXT   HXT    sing N N 439 
VAL   N     CA     sing N N 440 
VAL   N     H      sing N N 441 
VAL   N     H2     sing N N 442 
VAL   CA    C      sing N N 443 
VAL   CA    CB     sing N N 444 
VAL   CA    HA     sing N N 445 
VAL   C     O      doub N N 446 
VAL   C     OXT    sing N N 447 
VAL   CB    CG1    sing N N 448 
VAL   CB    CG2    sing N N 449 
VAL   CB    HB     sing N N 450 
VAL   CG1   HG11   sing N N 451 
VAL   CG1   HG12   sing N N 452 
VAL   CG1   HG13   sing N N 453 
VAL   CG2   HG21   sing N N 454 
VAL   CG2   HG22   sing N N 455 
VAL   CG2   HG23   sing N N 456 
VAL   OXT   HXT    sing N N 457 
# 
_pdbx_audit_support.funding_organization   'Not funded' 
_pdbx_audit_support.country                ? 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   4E00 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9DI9 
_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]   0.007915 
_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]   0.007915 
_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]   0.013390 
_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  
F  
K  
MG 
N  
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_site.pdbx_tls_group_id 
ATOM   1    N  N     . SER   A 1 27  ? 21.745 26.651  -16.674 1    81.5   ? 27  SER   A N     1 1 
ATOM   2    C  CA    . SER   A 1 27  ? 20.375 26.419  -17.149 1    81.88  ? 27  SER   A CA    1 1 
ATOM   3    C  C     . SER   A 1 27  ? 20.284 25.3    -18.197 1    81.58  ? 27  SER   A C     1 1 
ATOM   4    O  O     . SER   A 1 27  ? 19.207 24.735  -18.394 1    81.6   ? 27  SER   A O     1 1 
ATOM   5    C  CB    . SER   A 1 27  ? 19.756 27.707  -17.689 1    83.55  ? 27  SER   A CB    1 1 
ATOM   6    O  OG    . SER   A 1 27  ? 20.396 28.15   -18.877 1    86.27  ? 27  SER   A OG    1 1 
ATOM   7    N  N     . ALA   A 1 28  ? 21.411 24.98   -18.864 1    81.11  ? 28  ALA   A N     1 1 
ATOM   8    C  CA    . ALA   A 1 28  ? 21.476 23.927  -19.876 1    81.02  ? 28  ALA   A CA    1 1 
ATOM   9    C  C     . ALA   A 1 28  ? 21.173 22.544  -19.279 1    80.59  ? 28  ALA   A C     1 1 
ATOM   10   O  O     . ALA   A 1 28  ? 20.624 21.7    -19.977 1    80.65  ? 28  ALA   A O     1 1 
ATOM   11   C  CB    . ALA   A 1 28  ? 22.846 23.927  -20.545 1    81.01  ? 28  ALA   A CB    1 1 
ATOM   12   N  N     . ILE   A 1 29  ? 21.504 22.328  -17.99  1    79.89  ? 29  ILE   A N     1 1 
ATOM   13   C  CA    . ILE   A 1 29  ? 21.248 21.064  -17.299 1    79.61  ? 29  ILE   A CA    1 1 
ATOM   14   C  C     . ILE   A 1 29  ? 19.744 20.801  -17.211 1    79.82  ? 29  ILE   A C     1 1 
ATOM   15   O  O     . ILE   A 1 29  ? 19.315 19.694  -17.527 1    79.82  ? 29  ILE   A O     1 1 
ATOM   16   C  CB    . ILE   A 1 29  ? 21.995 20.97   -15.919 1    79.47  ? 29  ILE   A CB    1 1 
ATOM   17   C  CG1   . ILE   A 1 29  ? 23.435 20.489  -16.11  1    79.78  ? 29  ILE   A CG1   1 1 
ATOM   18   C  CG2   . ILE   A 1 29  ? 21.276 20.08   -14.887 1    79.91  ? 29  ILE   A CG2   1 1 
ATOM   19   C  CD1   . ILE   A 1 29  ? 24.409 21.577  -16.247 1    80.8   ? 29  ILE   A CD1   1 1 
ATOM   20   N  N     . ASP   A 1 30  ? 18.941 21.817  -16.834 1    79.67  ? 30  ASP   A N     1 1 
ATOM   21   C  CA    . ASP   A 1 30  ? 17.488 21.646  -16.731 1    80.16  ? 30  ASP   A CA    1 1 
ATOM   22   C  C     . ASP   A 1 30  ? 16.84  21.342  -18.083 1    79.77  ? 30  ASP   A C     1 1 
ATOM   23   O  O     . ASP   A 1 30  ? 15.879 20.577  -18.152 1    79.86  ? 30  ASP   A O     1 1 
ATOM   24   C  CB    . ASP   A 1 30  ? 16.828 22.871  -16.079 1    82.96  ? 30  ASP   A CB    1 1 
ATOM   25   C  CG    . ASP   A 1 30  ? 16.724 22.798  -14.563 1    89.19  ? 30  ASP   A CG    1 1 
ATOM   26   O  OD1   . ASP   A 1 30  ? 16.19  21.782  -14.046 1    90.01  ? 30  ASP   A OD1   1 1 
ATOM   27   O  OD2   . ASP   A 1 30  ? 17.163 23.761  -13.892 1    91.93  ? 30  ASP   A OD2   1 1 
ATOM   28   N  N     . VAL   A 1 31  ? 17.384 21.912  -19.155 1    79.39  ? 31  VAL   A N     1 1 
ATOM   29   C  CA    . VAL   A 1 31  ? 16.862 21.684  -20.495 1    79.8   ? 31  VAL   A CA    1 1 
ATOM   30   C  C     . VAL   A 1 31  ? 17.162 20.262  -20.975 1    79.9   ? 31  VAL   A C     1 1 
ATOM   31   O  O     . VAL   A 1 31  ? 16.249 19.556  -21.404 1    79.87  ? 31  VAL   A O     1 1 
ATOM   32   C  CB    . VAL   A 1 31  ? 17.379 22.753  -21.481 1    80.43  ? 31  VAL   A CB    1 1 
ATOM   33   C  CG1   . VAL   A 1 31  ? 16.896 22.47   -22.895 1    80.91  ? 31  VAL   A CG1   1 1 
ATOM   34   C  CG2   . VAL   A 1 31  ? 16.95  24.143  -21.031 1    80.97  ? 31  VAL   A CG2   1 1 
ATOM   35   N  N     . VAL   A 1 32  ? 18.432 19.827  -20.855 1    79.75  ? 32  VAL   A N     1 1 
ATOM   36   C  CA    . VAL   A 1 32  ? 18.861 18.488  -21.271 1    79.77  ? 32  VAL   A CA    1 1 
ATOM   37   C  C     . VAL   A 1 32  ? 18.249 17.387  -20.382 1    80.15  ? 32  VAL   A C     1 1 
ATOM   38   O  O     . VAL   A 1 32  ? 17.883 16.342  -20.905 1    79.88  ? 32  VAL   A O     1 1 
ATOM   39   C  CB    . VAL   A 1 32  ? 20.405 18.389  -21.396 1    80     ? 32  VAL   A CB    1 1 
ATOM   40   C  CG1   . VAL   A 1 32  ? 20.827 17.033  -21.941 1    80.33  ? 32  VAL   A CG1   1 1 
ATOM   41   C  CG2   . VAL   A 1 32  ? 20.947 19.501  -22.292 1    80.19  ? 32  VAL   A CG2   1 1 
ATOM   42   N  N     . ALA   A 1 33  ? 18.028 17.647  -19.078 1    81     ? 33  ALA   A N     1 1 
ATOM   43   C  CA    . ALA   A 1 33  ? 17.395 16.651  -18.192 1    82.46  ? 33  ALA   A CA    1 1 
ATOM   44   C  C     . ALA   A 1 33  ? 15.923 16.371  -18.525 1    84.42  ? 33  ALA   A C     1 1 
ATOM   45   O  O     . ALA   A 1 33  ? 15.386 15.346  -18.111 1    84.62  ? 33  ALA   A O     1 1 
ATOM   46   C  CB    . ALA   A 1 33  ? 17.528 17.055  -16.736 1    82.27  ? 33  ALA   A CB    1 1 
ATOM   47   N  N     . GLU   A 1 34  ? 15.27  17.267  -19.272 1    85.83  ? 34  GLU   A N     1 1 
ATOM   48   C  CA    . GLU   A 1 34  ? 13.879 17.056  -19.688 1    87.8   ? 34  GLU   A CA    1 1 
ATOM   49   C  C     . GLU   A 1 34  ? 13.745 16.123  -20.91  1    89.26  ? 34  GLU   A C     1 1 
ATOM   50   O  O     . GLU   A 1 34  ? 12.629 15.774  -21.286 1    89.53  ? 34  GLU   A O     1 1 
ATOM   51   C  CB    . GLU   A 1 34  ? 13.172 18.404  -19.931 1    90.62  ? 34  GLU   A CB    1 1 
ATOM   52   C  CG    . GLU   A 1 34  ? 11.955 18.635  -19.046 1    97.02  ? 34  GLU   A CG    1 1 
ATOM   53   C  CD    . GLU   A 1 34  ? 12.136 18.331  -17.568 1    105.41 ? 34  GLU   A CD    1 1 
ATOM   54   O  OE1   . GLU   A 1 34  ? 13.115 18.833  -16.965 1    106.92 ? 34  GLU   A OE1   1 1 
ATOM   55   O  OE2   . GLU   A 1 34  ? 11.299 17.579  -17.016 1    107.85 ? 34  GLU   A OE2   1 1 
ATOM   56   N  N     . LYS   A 1 35  ? 14.869 15.725  -21.526 1    89.97  ? 35  LYS   A N     1 1 
ATOM   57   C  CA    . LYS   A 1 35  ? 14.861 14.819  -22.662 1    91.28  ? 35  LYS   A CA    1 1 
ATOM   58   C  C     . LYS   A 1 35  ? 14.648 13.373  -22.184 1    92.74  ? 35  LYS   A C     1 1 
ATOM   59   O  O     . LYS   A 1 35  ? 14.928 13.042  -21.025 1    92.53  ? 35  LYS   A O     1 1 
ATOM   60   C  CB    . LYS   A 1 35  ? 16.136 14.996  -23.494 1    92.79  ? 35  LYS   A CB    1 1 
ATOM   61   C  CG    . LYS   A 1 35  ? 16.278 16.427  -24.004 1    96.22  ? 35  LYS   A CG    1 1 
ATOM   62   C  CD    . LYS   A 1 35  ? 17.475 16.605  -24.909 1    100.3  ? 35  LYS   A CD    1 1 
ATOM   63   C  CE    . LYS   A 1 35  ? 17.622 18.042  -25.344 1    103.78 ? 35  LYS   A CE    1 1 
ATOM   64   N  NZ    . LYS   A 1 35  ? 18.732 18.216  -26.319 1    105.93 ? 35  LYS   A NZ    1 1 
ATOM   65   N  N     . PRO   A 1 36  ? 14.066 12.514  -23.044 1    93.91  ? 36  PRO   A N     1 1 
ATOM   66   C  CA    . PRO   A 1 36  ? 13.756 11.143  -22.605 1    94.5   ? 36  PRO   A CA    1 1 
ATOM   67   C  C     . PRO   A 1 36  ? 14.981 10.356  -22.103 1    95.1   ? 36  PRO   A C     1 1 
ATOM   68   O  O     . PRO   A 1 36  ? 15.281 10.492  -20.919 1    95.37  ? 36  PRO   A O     1 1 
ATOM   69   C  CB    . PRO   A 1 36  ? 13.045 10.523  -23.826 1    95.22  ? 36  PRO   A CB    1 1 
ATOM   70   C  CG    . PRO   A 1 36  ? 13.481 11.369  -24.997 1    95.55  ? 36  PRO   A CG    1 1 
ATOM   71   C  CD    . PRO   A 1 36  ? 13.619 12.757  -24.432 1    93.73  ? 36  PRO   A CD    1 1 
ATOM   72   N  N     . SER   A 1 37  ? 15.679 9.579   -22.975 1    95.12  ? 37  SER   A N     1 1 
ATOM   73   C  CA    . SER   A 1 37  ? 16.835 8.708   -22.72  1    95.6   ? 37  SER   A CA    1 1 
ATOM   74   C  C     . SER   A 1 37  ? 16.646 7.399   -23.501 1    96     ? 37  SER   A C     1 1 
ATOM   75   O  O     . SER   A 1 37  ? 15.856 6.552   -23.083 1    96.36  ? 37  SER   A O     1 1 
ATOM   76   C  CB    . SER   A 1 37  ? 16.982 8.385   -21.233 1    96.58  ? 37  SER   A CB    1 1 
ATOM   77   O  OG    . SER   A 1 37  ? 17.988 7.419   -20.977 1    98.62  ? 37  SER   A OG    1 1 
ATOM   78   N  N     . VAL   A 1 38  ? 17.347 7.234   -24.631 1    95.74  ? 38  VAL   A N     1 1 
ATOM   79   C  CA    . VAL   A 1 38  ? 17.256 6       -25.409 1    96.22  ? 38  VAL   A CA    1 1 
ATOM   80   C  C     . VAL   A 1 38  ? 18.136 4.919   -24.774 1    96.55  ? 38  VAL   A C     1 1 
ATOM   81   O  O     . VAL   A 1 38  ? 19.357 4.967   -24.898 1    96.45  ? 38  VAL   A O     1 1 
ATOM   82   C  CB    . VAL   A 1 38  ? 17.627 6.219   -26.89  1    96.98  ? 38  VAL   A CB    1 1 
ATOM   83   C  CG1   . VAL   A 1 38  ? 17.395 4.949   -27.702 1    97.49  ? 38  VAL   A CG1   1 1 
ATOM   84   C  CG2   . VAL   A 1 38  ? 16.85  7.389   -27.479 1    97.57  ? 38  VAL   A CG2   1 1 
ATOM   85   N  N     . ARG   A 1 39  ? 17.522 3.951   -24.086 1    96.79  ? 39  ARG   A N     1 1 
ATOM   86   C  CA    . ARG   A 1 39  ? 18.268 2.876   -23.44  1    97.33  ? 39  ARG   A CA    1 1 
ATOM   87   C  C     . ARG   A 1 39  ? 18.753 1.825   -24.432 1    96.97  ? 39  ARG   A C     1 1 
ATOM   88   O  O     . ARG   A 1 39  ? 18.017 1.431   -25.342 1    96.88  ? 39  ARG   A O     1 1 
ATOM   89   C  CB    . ARG   A 1 39  ? 17.438 2.231   -22.328 1    99.61  ? 39  ARG   A CB    1 1 
ATOM   90   C  CG    . ARG   A 1 39  ? 17.139 3.196   -21.194 1    104.15 ? 39  ARG   A CG    1 1 
ATOM   91   C  CD    . ARG   A 1 39  ? 15.92  2.765   -20.401 1    108.49 ? 39  ARG   A CD    1 1 
ATOM   92   N  NE    . ARG   A 1 39  ? 15.132 3.918   -19.961 1    112.19 ? 39  ARG   A NE    1 1 
ATOM   93   C  CZ    . ARG   A 1 39  ? 14.182 4.499   -20.688 1    114.94 ? 39  ARG   A CZ    1 1 
ATOM   94   N  NH1   . ARG   A 1 39  ? 13.892 4.043   -21.902 1    114.93 ? 39  ARG   A NH1   1 1 
ATOM   95   N  NH2   . ARG   A 1 39  ? 13.519 5.544   -20.211 1    114.91 ? 39  ARG   A NH2   1 1 
ATOM   96   N  N     . LEU   A 1 40  ? 20.006 1.382   -24.26  1    96.46  ? 40  LEU   A N     1 1 
ATOM   97   C  CA    . LEU   A 1 40  ? 20.599 0.371   -25.125 1    96.26  ? 40  LEU   A CA    1 1 
ATOM   98   C  C     . LEU   A 1 40  ? 20.642 -0.966  -24.407 1    95.68  ? 40  LEU   A C     1 1 
ATOM   99   O  O     . LEU   A 1 40  ? 21.212 -1.076  -23.325 1    95.79  ? 40  LEU   A O     1 1 
ATOM   100  C  CB    . LEU   A 1 40  ? 22.003 0.794   -25.561 1    96.6   ? 40  LEU   A CB    1 1 
ATOM   101  C  CG    . LEU   A 1 40  ? 22.483 0.227   -26.888 1    98.31  ? 40  LEU   A CG    1 1 
ATOM   102  C  CD1   . LEU   A 1 40  ? 21.552 0.627   -28.029 1    98.88  ? 40  LEU   A CD1   1 1 
ATOM   103  C  CD2   . LEU   A 1 40  ? 23.88  0.711   -27.197 1    99.09  ? 40  LEU   A CD2   1 1 
ATOM   104  N  N     . THR   A 1 41  ? 20     -1.972  -24.984 1    94.98  ? 41  THR   A N     1 1 
ATOM   105  C  CA    . THR   A 1 41  ? 19.945 -3.301  -24.387 1    94.54  ? 41  THR   A CA    1 1 
ATOM   106  C  C     . THR   A 1 41  ? 21.157 -4.121  -24.876 1    93.72  ? 41  THR   A C     1 1 
ATOM   107  O  O     . THR   A 1 41  ? 21.612 -3.931  -26.008 1    93.82  ? 41  THR   A O     1 1 
ATOM   108  C  CB    . THR   A 1 41  ? 18.538 -3.889  -24.633 1    95.76  ? 41  THR   A CB    1 1 
ATOM   109  O  OG1   . THR   A 1 41  ? 17.869 -4.017  -23.38  1    96.93  ? 41  THR   A OG1   1 1 
ATOM   110  C  CG2   . THR   A 1 41  ? 18.536 -5.203  -25.394 1    95.87  ? 41  THR   A CG2   1 1 
ATOM   111  N  N     . PRO   A 1 42  ? 21.726 -5.006  -24.029 1    92.6   ? 42  PRO   A N     1 1 
ATOM   112  C  CA    . PRO   A 1 42  ? 22.921 -5.768  -24.447 1    91.93  ? 42  PRO   A CA    1 1 
ATOM   113  C  C     . PRO   A 1 42  ? 22.768 -6.58   -25.734 1    91.23  ? 42  PRO   A C     1 1 
ATOM   114  O  O     . PRO   A 1 42  ? 23.763 -6.878  -26.39  1    90.88  ? 42  PRO   A O     1 1 
ATOM   115  C  CB    . PRO   A 1 42  ? 23.22  -6.649  -23.231 1    92.64  ? 42  PRO   A CB    1 1 
ATOM   116  C  CG    . PRO   A 1 42  ? 22.617 -5.907  -22.078 1    93.15  ? 42  PRO   A CG    1 1 
ATOM   117  C  CD    . PRO   A 1 42  ? 21.353 -5.317  -22.638 1    91.83  ? 42  PRO   A CD    1 1 
ATOM   118  N  N     . THR   A 1 43  ? 21.524 -6.896  -26.122 1    90.97  ? 43  THR   A N     1 1 
ATOM   119  C  CA    . THR   A 1 43  ? 21.24  -7.608  -27.371 1    91.21  ? 43  THR   A CA    1 1 
ATOM   120  C  C     . THR   A 1 43  ? 21.413 -6.647  -28.56  1    91.18  ? 43  THR   A C     1 1 
ATOM   121  O  O     . THR   A 1 43  ? 21.963 -7.037  -29.589 1    91.11  ? 43  THR   A O     1 1 
ATOM   122  C  CB    . THR   A 1 43  ? 19.855 -8.279  -27.339 1    92.21  ? 43  THR   A CB    1 1 
ATOM   123  O  OG1   . THR   A 1 43  ? 19.649 -8.915  -26.075 1    93.14  ? 43  THR   A OG1   1 1 
ATOM   124  C  CG2   . THR   A 1 43  ? 19.678 -9.286  -28.461 1    92.51  ? 43  THR   A CG2   1 1 
ATOM   125  N  N     . MET   A 1 44  ? 20.976 -5.385  -28.402 1    91.2   ? 44  MET   A N     1 1 
ATOM   126  C  CA    . MET   A 1 44  ? 21.155 -4.35   -29.425 1    91.84  ? 44  MET   A CA    1 1 
ATOM   127  C  C     . MET   A 1 44  ? 22.661 -4.089  -29.611 1    91.8   ? 44  MET   A C     1 1 
ATOM   128  O  O     . MET   A 1 44  ? 23.112 -3.922  -30.741 1    91.98  ? 44  MET   A O     1 1 
ATOM   129  C  CB    . MET   A 1 44  ? 20.456 -3.035  -29.02  1    92.9   ? 44  MET   A CB    1 1 
ATOM   130  C  CG    . MET   A 1 44  ? 19.02  -3.203  -28.573 1    95.93  ? 44  MET   A CG    1 1 
ATOM   131  S  SD    . MET   A 1 44  ? 18.371 -1.709  -27.765 1    102.42 ? 44  MET   A SD    1 1 
ATOM   132  C  CE    . MET   A 1 44  ? 18.213 -0.629  -29.164 1    101.38 ? 44  MET   A CE    1 1 
ATOM   133  N  N     . MET   A 1 45  ? 23.434 -4.08   -28.497 1    91.51  ? 45  MET   A N     1 1 
ATOM   134  C  CA    . MET   A 1 45  ? 24.884 -3.877  -28.491 1    91.73  ? 45  MET   A CA    1 1 
ATOM   135  C  C     . MET   A 1 45  ? 25.596 -4.985  -29.274 1    92.77  ? 45  MET   A C     1 1 
ATOM   136  O  O     . MET   A 1 45  ? 26.555 -4.707  -29.996 1    92.93  ? 45  MET   A O     1 1 
ATOM   137  C  CB    . MET   A 1 45  ? 25.416 -3.847  -27.053 1    91.43  ? 45  MET   A CB    1 1 
ATOM   138  C  CG    . MET   A 1 45  ? 25.199 -2.551  -26.334 1    92.36  ? 45  MET   A CG    1 1 
ATOM   139  S  SD    . MET   A 1 45  ? 25.899 -2.635  -24.667 1    94.6   ? 45  MET   A SD    1 1 
ATOM   140  C  CE    . MET   A 1 45  ? 26.865 -1.18   -24.648 1    93     ? 45  MET   A CE    1 1 
ATOM   141  N  N     . LEU   A 1 46  ? 25.124 -6.239  -29.127 1    93.25  ? 46  LEU   A N     1 1 
ATOM   142  C  CA    . LEU   A 1 46  ? 25.678 -7.403  -29.82  1    94.18  ? 46  LEU   A CA    1 1 
ATOM   143  C  C     . LEU   A 1 46  ? 25.497 -7.274  -31.338 1    95.3   ? 46  LEU   A C     1 1 
ATOM   144  O  O     . LEU   A 1 46  ? 26.403 -7.627  -32.089 1    95.79  ? 46  LEU   A O     1 1 
ATOM   145  C  CB    . LEU   A 1 46  ? 24.998 -8.689  -29.325 1    94.22  ? 46  LEU   A CB    1 1 
ATOM   146  C  CG    . LEU   A 1 46  ? 25.897 -9.772  -28.733 1    95.3   ? 46  LEU   A CG    1 1 
ATOM   147  C  CD1   . LEU   A 1 46  ? 25.079 -10.97  -28.316 1    95.68  ? 46  LEU   A CD1   1 1 
ATOM   148  C  CD2   . LEU   A 1 46  ? 26.967 -10.213 -29.717 1    95.88  ? 46  LEU   A CD2   1 1 
ATOM   149  N  N     . TYR   A 1 47  ? 24.341 -6.754  -31.793 1    95.56  ? 47  TYR   A N     1 1 
ATOM   150  C  CA    . TYR   A 1 47  ? 24.079 -6.574  -33.222 1    96.24  ? 47  TYR   A CA    1 1 
ATOM   151  C  C     . TYR   A 1 47  ? 24.431 -5.159  -33.692 1    97.07  ? 47  TYR   A C     1 1 
ATOM   152  O  O     . TYR   A 1 47  ? 25.597 -4.759  -33.659 1    97.51  ? 47  TYR   A O     1 1 
ATOM   153  C  CB    . TYR   A 1 47  ? 22.622 -6.874  -33.528 1    96.26  ? 47  TYR   A CB    1 1 
ATOM   154  N  N     . ASP   A 1 53  ? 34.644 -1.221  -42.786 1    97.02  ? 53  ASP   A N     1 1 
ATOM   155  C  CA    . ASP   A 1 53  ? 34.49  0.156   -43.26  1    97.4   ? 53  ASP   A CA    1 1 
ATOM   156  C  C     . ASP   A 1 53  ? 34.608 1.194   -42.124 1    96.77  ? 53  ASP   A C     1 1 
ATOM   157  O  O     . ASP   A 1 53  ? 35.204 2.253   -42.323 1    96.91  ? 53  ASP   A O     1 1 
ATOM   158  C  CB    . ASP   A 1 53  ? 33.161 0.32    -44.015 1    99.9   ? 53  ASP   A CB    1 1 
ATOM   159  C  CG    . ASP   A 1 53  ? 32.9   1.733   -44.505 1    105.97 ? 53  ASP   A CG    1 1 
ATOM   160  O  OD1   . ASP   A 1 53  ? 33.769 2.285   -45.221 1    106.79 ? 53  ASP   A OD1   1 1 
ATOM   161  O  OD2   . ASP   A 1 53  ? 31.834 2.29    -44.163 1    108.79 ? 53  ASP   A OD2   1 1 
ATOM   162  N  N     . GLY   A 1 54  ? 34.026 0.89    -40.966 1    95.73  ? 54  GLY   A N     1 1 
ATOM   163  C  CA    . GLY   A 1 54  ? 34.053 1.789   -39.814 1    95.04  ? 54  GLY   A CA    1 1 
ATOM   164  C  C     . GLY   A 1 54  ? 32.858 2.723   -39.699 1    93.88  ? 54  GLY   A C     1 1 
ATOM   165  O  O     . GLY   A 1 54  ? 32.898 3.698   -38.943 1    94.06  ? 54  GLY   A O     1 1 
ATOM   166  N  N     . SER   A 1 55  ? 31.786 2.447   -40.457 1    92.36  ? 55  SER   A N     1 1 
ATOM   167  C  CA    . SER   A 1 55  ? 30.558 3.247   -40.437 1    91     ? 55  SER   A CA    1 1 
ATOM   168  C  C     . SER   A 1 55  ? 29.817 3.083   -39.091 1    88.77  ? 55  SER   A C     1 1 
ATOM   169  O  O     . SER   A 1 55  ? 29.222 4.039   -38.587 1    88.89  ? 55  SER   A O     1 1 
ATOM   170  C  CB    . SER   A 1 55  ? 29.647 2.832   -41.59  1    92.36  ? 55  SER   A CB    1 1 
ATOM   171  O  OG    . SER   A 1 55  ? 28.433 3.565   -41.601 1    94.6   ? 55  SER   A OG    1 1 
ATOM   172  N  N     . HIS   A 1 56  ? 29.867 1.871   -38.515 1    86.36  ? 56  HIS   A N     1 1 
ATOM   173  C  CA    . HIS   A 1 56  ? 29.234 1.551   -37.238 1    84.58  ? 56  HIS   A CA    1 1 
ATOM   174  C  C     . HIS   A 1 56  ? 29.838 2.356   -36.067 1    82.3   ? 56  HIS   A C     1 1 
ATOM   175  O  O     . HIS   A 1 56  ? 29.147 2.62    -35.081 1    81.93  ? 56  HIS   A O     1 1 
ATOM   176  C  CB    . HIS   A 1 56  ? 29.318 0.037   -36.97  1    85.29  ? 56  HIS   A CB    1 1 
ATOM   177  C  CG    . HIS   A 1 56  ? 30.706 -0.463  -36.692 1    87.53  ? 56  HIS   A CG    1 1 
ATOM   178  N  ND1   . HIS   A 1 56  ? 31.723 -0.336  -37.624 1    89.52  ? 56  HIS   A ND1   1 1 
ATOM   179  C  CD2   . HIS   A 1 56  ? 31.195 -1.093  -35.596 1    88.49  ? 56  HIS   A CD2   1 1 
ATOM   180  C  CE1   . HIS   A 1 56  ? 32.793 -0.878  -37.063 1    89.91  ? 56  HIS   A CE1   1 1 
ATOM   181  N  NE2   . HIS   A 1 56  ? 32.525 -1.34   -35.839 1    89.52  ? 56  HIS   A NE2   1 1 
ATOM   182  N  N     . LEU   A 1 57  ? 31.124 2.738   -36.189 1    80.42  ? 57  LEU   A N     1 1 
ATOM   183  C  CA    . LEU   A 1 57  ? 31.857 3.541   -35.215 1    79.19  ? 57  LEU   A CA    1 1 
ATOM   184  C  C     . LEU   A 1 57  ? 31.276 4.963   -35.166 1    77.71  ? 57  LEU   A C     1 1 
ATOM   185  O  O     . LEU   A 1 57  ? 31.166 5.545   -34.088 1    77.81  ? 57  LEU   A O     1 1 
ATOM   186  C  CB    . LEU   A 1 57  ? 33.334 3.596   -35.644 1    79.37  ? 57  LEU   A CB    1 1 
ATOM   187  C  CG    . LEU   A 1 57  ? 34.384 2.79    -34.858 1    81.01  ? 57  LEU   A CG    1 1 
ATOM   188  C  CD1   . LEU   A 1 57  ? 33.858 1.446   -34.356 1    81.52  ? 57  LEU   A CD1   1 1 
ATOM   189  C  CD2   . LEU   A 1 57  ? 35.629 2.579   -35.701 1    81.45  ? 57  LEU   A CD2   1 1 
ATOM   190  N  N     . LEU   A 1 58  ? 30.888 5.511   -36.328 1    76.03  ? 58  LEU   A N     1 1 
ATOM   191  C  CA    . LEU   A 1 58  ? 30.313 6.848   -36.409 1    75.06  ? 58  LEU   A CA    1 1 
ATOM   192  C  C     . LEU   A 1 58  ? 28.895 6.868   -35.855 1    73.47  ? 58  LEU   A C     1 1 
ATOM   193  O  O     . LEU   A 1 58  ? 28.505 7.84    -35.21  1    73.41  ? 58  LEU   A O     1 1 
ATOM   194  C  CB    . LEU   A 1 58  ? 30.332 7.359   -37.855 1    75.58  ? 58  LEU   A CB    1 1 
ATOM   195  C  CG    . LEU   A 1 58  ? 31.474 8.298   -38.218 1    77.67  ? 58  LEU   A CG    1 1 
ATOM   196  C  CD1   . LEU   A 1 58  ? 32.833 7.646   -37.977 1    78.44  ? 58  LEU   A CD1   1 1 
ATOM   197  C  CD2   . LEU   A 1 58  ? 31.36  8.741   -39.661 1    78.46  ? 58  LEU   A CD2   1 1 
ATOM   198  N  N     . LYS   A 1 59  ? 28.123 5.803   -36.106 1    72     ? 59  LYS   A N     1 1 
ATOM   199  C  CA    . LYS   A 1 59  ? 26.769 5.686   -35.587 1    71.38  ? 59  LYS   A CA    1 1 
ATOM   200  C  C     . LYS   A 1 59  ? 26.822 5.518   -34.052 1    69.15  ? 59  LYS   A C     1 1 
ATOM   201  O  O     . LYS   A 1 59  ? 25.999 6.103   -33.347 1    69.24  ? 59  LYS   A O     1 1 
ATOM   202  C  CB    . LYS   A 1 59  ? 26.038 4.501   -36.255 1    74.98  ? 59  LYS   A CB    1 1 
ATOM   203  C  CG    . LYS   A 1 59  ? 24.664 4.193   -35.646 1    81.31  ? 59  LYS   A CG    1 1 
ATOM   204  C  CD    . LYS   A 1 59  ? 23.989 2.961   -36.251 1    87.21  ? 59  LYS   A CD    1 1 
ATOM   205  C  CE    . LYS   A 1 59  ? 22.832 2.504   -35.387 1    92     ? 59  LYS   A CE    1 1 
ATOM   206  N  NZ    . LYS   A 1 59  ? 22.127 1.329   -35.968 1    94.87  ? 59  LYS   A NZ    1 1 
ATOM   207  N  N     . SER   A 1 60  ? 27.808 4.756   -33.543 1    66.98  ? 60  SER   A N     1 1 
ATOM   208  C  CA    . SER   A 1 60  ? 28.001 4.545   -32.111 1    65.9   ? 60  SER   A CA    1 1 
ATOM   209  C  C     . SER   A 1 60  ? 28.433 5.845   -31.428 1    65.06  ? 60  SER   A C     1 1 
ATOM   210  O  O     . SER   A 1 60  ? 27.886 6.206   -30.387 1    64.82  ? 60  SER   A O     1 1 
ATOM   211  C  CB    . SER   A 1 60  ? 29.03  3.446   -31.869 1    66.92  ? 60  SER   A CB    1 1 
ATOM   212  O  OG    . SER   A 1 60  ? 29.282 3.245   -30.487 1    69     ? 60  SER   A OG    1 1 
ATOM   213  N  N     . GLY   A 1 61  ? 29.356 6.567   -32.061 1    64.36  ? 61  GLY   A N     1 1 
ATOM   214  C  CA    . GLY   A 1 61  ? 29.855 7.842   -31.568 1    63.93  ? 61  GLY   A CA    1 1 
ATOM   215  C  C     . GLY   A 1 61  ? 28.749 8.866   -31.45  1    63.86  ? 61  GLY   A C     1 1 
ATOM   216  O  O     . GLY   A 1 61  ? 28.643 9.551   -30.429 1    63.94  ? 61  GLY   A O     1 1 
ATOM   217  N  N     . ARG   A 1 62  ? 27.89  8.947   -32.482 1    63.59  ? 62  ARG   A N     1 1 
ATOM   218  C  CA    . ARG   A 1 62  ? 26.756 9.871   -32.501 1    63.88  ? 62  ARG   A CA    1 1 
ATOM   219  C  C     . ARG   A 1 62  ? 25.71  9.504   -31.453 1    63.37  ? 62  ARG   A C     1 1 
ATOM   220  O  O     . ARG   A 1 62  ? 25.107 10.393  -30.861 1    63.55  ? 62  ARG   A O     1 1 
ATOM   221  C  CB    . ARG   A 1 62  ? 26.113 9.92    -33.882 1    65.96  ? 62  ARG   A CB    1 1 
ATOM   222  C  CG    . ARG   A 1 62  ? 26.945 10.659  -34.91  1    70.69  ? 62  ARG   A CG    1 1 
ATOM   223  C  CD    . ARG   A 1 62  ? 26.28  10.593  -36.261 1    75.54  ? 62  ARG   A CD    1 1 
ATOM   224  N  NE    . ARG   A 1 62  ? 27.079 11.265  -37.284 1    80.81  ? 62  ARG   A NE    1 1 
ATOM   225  C  CZ    . ARG   A 1 62  ? 27.544 10.676  -38.382 1    84.15  ? 62  ARG   A CZ    1 1 
ATOM   226  N  NH1   . ARG   A 1 62  ? 27.294 9.39    -38.611 1    84.6   ? 62  ARG   A NH1   1 1 
ATOM   227  N  NH2   . ARG   A 1 62  ? 28.263 11.366  -39.258 1    84.41  ? 62  ARG   A NH2   1 1 
ATOM   228  N  N     . TYR   A 1 63  ? 25.524 8.205   -31.181 1    62.73  ? 63  TYR   A N     1 1 
ATOM   229  C  CA    . TYR   A 1 63  ? 24.577 7.765   -30.16  1    62.36  ? 63  TYR   A CA    1 1 
ATOM   230  C  C     . TYR   A 1 63  ? 25.05  8.252   -28.795 1    61.37  ? 63  TYR   A C     1 1 
ATOM   231  O  O     . TYR   A 1 63  ? 24.245 8.799   -28.053 1    60.94  ? 63  TYR   A O     1 1 
ATOM   232  C  CB    . TYR   A 1 63  ? 24.387 6.231   -30.174 1    62.7   ? 63  TYR   A CB    1 1 
ATOM   233  C  CG    . TYR   A 1 63  ? 23.654 5.724   -28.947 1    64.17  ? 63  TYR   A CG    1 1 
ATOM   234  C  CD1   . TYR   A 1 63  ? 22.295 5.951   -28.782 1    65.57  ? 63  TYR   A CD1   1 1 
ATOM   235  C  CD2   . TYR   A 1 63  ? 24.343 5.135   -27.897 1    65.07  ? 63  TYR   A CD2   1 1 
ATOM   236  C  CE1   . TYR   A 1 63  ? 21.626 5.536   -27.636 1    66.7   ? 63  TYR   A CE1   1 1 
ATOM   237  C  CE2   . TYR   A 1 63  ? 23.691 4.741   -26.736 1    66.33  ? 63  TYR   A CE2   1 1 
ATOM   238  C  CZ    . TYR   A 1 63  ? 22.33  4.93    -26.613 1    67.66  ? 63  TYR   A CZ    1 1 
ATOM   239  O  OH    . TYR   A 1 63  ? 21.68  4.518   -25.471 1    69.6   ? 63  TYR   A OH    1 1 
ATOM   240  N  N     . LEU   A 1 64  ? 26.351 8.063   -28.482 1    61.04  ? 64  LEU   A N     1 1 
ATOM   241  C  CA    . LEU   A 1 64  ? 26.976 8.492   -27.221 1    61.6   ? 64  LEU   A CA    1 1 
ATOM   242  C  C     . LEU   A 1 64  ? 26.901 9.996   -27.041 1    62.24  ? 64  LEU   A C     1 1 
ATOM   243  O  O     . LEU   A 1 64  ? 26.639 10.484  -25.939 1    62.36  ? 64  LEU   A O     1 1 
ATOM   244  C  CB    . LEU   A 1 64  ? 28.451 8.062   -27.179 1    61.8   ? 64  LEU   A CB    1 1 
ATOM   245  C  CG    . LEU   A 1 64  ? 28.793 6.961   -26.193 1    62.92  ? 64  LEU   A CG    1 1 
ATOM   246  C  CD1   . LEU   A 1 64  ? 28.037 5.69    -26.513 1    63.11  ? 64  LEU   A CD1   1 1 
ATOM   247  C  CD2   . LEU   A 1 64  ? 30.284 6.705   -26.166 1    63.64  ? 64  LEU   A CD2   1 1 
ATOM   248  N  N     . GLN   A 1 65  ? 27.097 10.728  -28.141 1    62.2   ? 65  GLN   A N     1 1 
ATOM   249  C  CA    . GLN   A 1 65  ? 27.059 12.174  -28.168 1    62.87  ? 65  GLN   A CA    1 1 
ATOM   250  C  C     . GLN   A 1 65  ? 25.706 12.705  -27.748 1    63.46  ? 65  GLN   A C     1 1 
ATOM   251  O  O     . GLN   A 1 65  ? 25.634 13.735  -27.088 1    64.08  ? 65  GLN   A O     1 1 
ATOM   252  C  CB    . GLN   A 1 65  ? 27.391 12.652  -29.578 1    64.67  ? 65  GLN   A CB    1 1 
ATOM   253  C  CG    . GLN   A 1 65  ? 27.857 14.076  -29.643 1    67.93  ? 65  GLN   A CG    1 1 
ATOM   254  C  CD    . GLN   A 1 65  ? 28.617 14.316  -30.921 1    72.21  ? 65  GLN   A CD    1 1 
ATOM   255  O  OE1   . GLN   A 1 65  ? 28.266 13.798  -32.001 1    73.23  ? 65  GLN   A OE1   1 1 
ATOM   256  N  NE2   . GLN   A 1 65  ? 29.68  15.106  -30.821 1    71.82  ? 65  GLN   A NE2   1 1 
ATOM   257  N  N     . GLN   A 1 66  ? 24.632 12.016  -28.124 1    63.27  ? 66  GLN   A N     1 1 
ATOM   258  C  CA    . GLN   A 1 66  ? 23.29  12.448  -27.773 1    63.67  ? 66  GLN   A CA    1 1 
ATOM   259  C  C     . GLN   A 1 66  ? 22.829 11.864  -26.43  1    62.22  ? 66  GLN   A C     1 1 
ATOM   260  O  O     . GLN   A 1 66  ? 22.164 12.549  -25.659 1    62.98  ? 66  GLN   A O     1 1 
ATOM   261  C  CB    . GLN   A 1 66  ? 22.329 12.084  -28.908 1    67.14  ? 66  GLN   A CB    1 1 
ATOM   262  C  CG    . GLN   A 1 66  ? 22.73  12.738  -30.233 1    74.19  ? 66  GLN   A CG    1 1 
ATOM   263  C  CD    . GLN   A 1 66  ? 22.301 14.188  -30.299 1    82.15  ? 66  GLN   A CD    1 1 
ATOM   264  O  OE1   . GLN   A 1 66  ? 21.112 14.514  -30.151 1    84.62  ? 66  GLN   A OE1   1 1 
ATOM   265  N  NE2   . GLN   A 1 66  ? 23.255 15.093  -30.536 1    83.25  ? 66  GLN   A NE2   1 1 
ATOM   266  N  N     . GLU   A 1 67  ? 23.233 10.63   -26.127 1    60.05  ? 67  GLU   A N     1 1 
ATOM   267  C  CA    . GLU   A 1 67  ? 22.829 9.932   -24.922 1    58.77  ? 67  GLU   A CA    1 1 
ATOM   268  C  C     . GLU   A 1 67  ? 23.553 10.348  -23.625 1    57.81  ? 67  GLU   A C     1 1 
ATOM   269  O  O     . GLU   A 1 67  ? 22.891 10.535  -22.6   1    58.06  ? 67  GLU   A O     1 1 
ATOM   270  C  CB    . GLU   A 1 67  ? 22.953 8.416   -25.134 1    60.11  ? 67  GLU   A CB    1 1 
ATOM   271  C  CG    . GLU   A 1 67  ? 22.337 7.59    -24.025 1    64.86  ? 67  GLU   A CG    1 1 
ATOM   272  C  CD    . GLU   A 1 67  ? 20.837 7.769   -23.868 1    71.22  ? 67  GLU   A CD    1 1 
ATOM   273  O  OE1   . GLU   A 1 67  ? 20.31  7.476   -22.771 1    70.55  ? 67  GLU   A OE1   1 1 
ATOM   274  O  OE2   . GLU   A 1 67  ? 20.178 8.182   -24.853 1    75.03  ? 67  GLU   A OE2   1 1 
ATOM   275  N  N     . LEU   A 1 68  ? 24.889 10.447  -23.646 1    56.32  ? 68  LEU   A N     1 1 
ATOM   276  C  CA    . LEU   A 1 68  ? 25.636 10.765  -22.435 1    55.39  ? 68  LEU   A CA    1 1 
ATOM   277  C  C     . LEU   A 1 68  ? 25.207 12.065  -21.745 1    54.98  ? 68  LEU   A C     1 1 
ATOM   278  O  O     . LEU   A 1 68  ? 24.986 12.002  -20.532 1    55.59  ? 68  LEU   A O     1 1 
ATOM   279  C  CB    . LEU   A 1 68  ? 27.155 10.738  -22.64  1    54.92  ? 68  LEU   A CB    1 1 
ATOM   280  C  CG    . LEU   A 1 68  ? 27.773 9.363   -22.904 1    55.34  ? 68  LEU   A CG    1 1 
ATOM   281  C  CD1   . LEU   A 1 68  ? 29.272 9.474   -23.03  1    55.25  ? 68  LEU   A CD1   1 1 
ATOM   282  C  CD2   . LEU   A 1 68  ? 27.41  8.361   -21.811 1    55.57  ? 68  LEU   A CD2   1 1 
ATOM   283  N  N     . PRO   A 1 69  ? 25.045 13.224  -22.433 1    53.48  ? 69  PRO   A N     1 1 
ATOM   284  C  CA    . PRO   A 1 69  ? 24.651 14.443  -21.712 1    52.81  ? 69  PRO   A CA    1 1 
ATOM   285  C  C     . PRO   A 1 69  ? 23.287 14.353  -21.044 1    52.22  ? 69  PRO   A C     1 1 
ATOM   286  O  O     . PRO   A 1 69  ? 23.104 14.958  -20.003 1    52.24  ? 69  PRO   A O     1 1 
ATOM   287  C  CB    . PRO   A 1 69  ? 24.678 15.538  -22.798 1    53.75  ? 69  PRO   A CB    1 1 
ATOM   288  C  CG    . PRO   A 1 69  ? 25.506 14.983  -23.899 1    54.35  ? 69  PRO   A CG    1 1 
ATOM   289  C  CD    . PRO   A 1 69  ? 25.25  13.505  -23.868 1    53.05  ? 69  PRO   A CD    1 1 
ATOM   290  N  N     . VAL   A 1 70  ? 22.343 13.603  -21.628 1    51.79  ? 70  VAL   A N     1 1 
ATOM   291  C  CA    . VAL   A 1 70  ? 21.008 13.394  -21.067 1    51.54  ? 70  VAL   A CA    1 1 
ATOM   292  C  C     . VAL   A 1 70  ? 21.121 12.64   -19.749 1    50.47  ? 70  VAL   A C     1 1 
ATOM   293  O  O     . VAL   A 1 70  ? 20.585 13.103  -18.751 1    50.72  ? 70  VAL   A O     1 1 
ATOM   294  C  CB    . VAL   A 1 70  ? 20.063 12.7    -22.087 1    52.58  ? 70  VAL   A CB    1 1 
ATOM   295  C  CG1   . VAL   A 1 70  ? 18.82  12.106  -21.42  1    52.95  ? 70  VAL   A CG1   1 1 
ATOM   296  C  CG2   . VAL   A 1 70  ? 19.676 13.668  -23.21  1    52.87  ? 70  VAL   A CG2   1 1 
ATOM   297  N  N     . ARG   A 1 71  ? 21.871 11.535  -19.723 1    49.45  ? 71  ARG   A N     1 1 
ATOM   298  C  CA    . ARG   A 1 71  ? 22.068 10.759  -18.495 1    48.97  ? 71  ARG   A CA    1 1 
ATOM   299  C  C     . ARG   A 1 71  ? 22.826 11.568  -17.444 1    49.66  ? 71  ARG   A C     1 1 
ATOM   300  O  O     . ARG   A 1 71  ? 22.497 11.515  -16.258 1    50.2   ? 71  ARG   A O     1 1 
ATOM   301  C  CB    . ARG   A 1 71  ? 22.822 9.466   -18.789 1    48.62  ? 71  ARG   A CB    1 1 
ATOM   302  C  CG    . ARG   A 1 71  ? 22.144 8.626   -19.838 1    49.87  ? 71  ARG   A CG    1 1 
ATOM   303  C  CD    . ARG   A 1 71  ? 22.684 7.228   -19.805 1    51.93  ? 71  ARG   A CD    1 1 
ATOM   304  N  NE    . ARG   A 1 71  ? 22.029 6.402   -20.811 1    55.5   ? 71  ARG   A NE    1 1 
ATOM   305  C  CZ    . ARG   A 1 71  ? 22.128 5.078   -20.887 1    57.8   ? 71  ARG   A CZ    1 1 
ATOM   306  N  NH1   . ARG   A 1 71  ? 22.858 4.407   -20.004 1    55.95  ? 71  ARG   A NH1   1 1 
ATOM   307  N  NH2   . ARG   A 1 71  ? 21.516 4.419   -21.859 1    59.03  ? 71  ARG   A NH2   1 1 
ATOM   308  N  N     . ILE   A 1 72  ? 23.817 12.335  -17.88  1    49.36  ? 72  ILE   A N     1 1 
ATOM   309  C  CA    . ILE   A 1 72  ? 24.596 13.171  -16.982 1    49.95  ? 72  ILE   A CA    1 1 
ATOM   310  C  C     . ILE   A 1 72  ? 23.735 14.296  -16.368 1    50.7   ? 72  ILE   A C     1 1 
ATOM   311  O  O     . ILE   A 1 72  ? 23.795 14.498  -15.152 1    50.95  ? 72  ILE   A O     1 1 
ATOM   312  C  CB    . ILE   A 1 72  ? 25.871 13.667  -17.693 1    49.94  ? 72  ILE   A CB    1 1 
ATOM   313  C  CG1   . ILE   A 1 72  ? 26.81  12.455  -17.921 1    50.99  ? 72  ILE   A CG1   1 1 
ATOM   314  C  CG2   . ILE   A 1 72  ? 26.563 14.767  -16.882 1    50.12  ? 72  ILE   A CG2   1 1 
ATOM   315  C  CD1   . ILE   A 1 72  ? 27.934 12.704  -18.747 1    52.18  ? 72  ILE   A CD1   1 1 
ATOM   316  N  N     . ALA   A 1 73  ? 22.884 14.962  -17.174 1    50.34  ? 73  ALA   A N     1 1 
ATOM   317  C  CA    . ALA   A 1 73  ? 22     16.02   -16.673 1    50.61  ? 73  ALA   A CA    1 1 
ATOM   318  C  C     . ALA   A 1 73  ? 21.033 15.509  -15.606 1    51.49  ? 73  ALA   A C     1 1 
ATOM   319  O  O     . ALA   A 1 73  ? 20.833 16.205  -14.612 1    52.39  ? 73  ALA   A O     1 1 
ATOM   320  C  CB    . ALA   A 1 73  ? 21.247 16.698  -17.812 1    50.26  ? 73  ALA   A CB    1 1 
ATOM   321  N  N     . HIS   A 1 74  ? 20.506 14.276  -15.743 1    51.15  ? 74  HIS   A N     1 1 
ATOM   322  C  CA    . HIS   A 1 74  ? 19.638 13.714  -14.704 1    51.74  ? 74  HIS   A CA    1 1 
ATOM   323  C  C     . HIS   A 1 74  ? 20.435 13.542  -13.398 1    51.56  ? 74  HIS   A C     1 1 
ATOM   324  O  O     . HIS   A 1 74  ? 19.911 13.836  -12.325 1    52.56  ? 74  HIS   A O     1 1 
ATOM   325  C  CB    . HIS   A 1 74  ? 19.038 12.352  -15.114 1    52.97  ? 74  HIS   A CB    1 1 
ATOM   326  C  CG    . HIS   A 1 74  ? 18.164 12.399  -16.325 1    57.11  ? 74  HIS   A CG    1 1 
ATOM   327  N  ND1   . HIS   A 1 74  ? 18.116 11.343  -17.224 1    59.92  ? 74  HIS   A ND1   1 1 
ATOM   328  C  CD2   . HIS   A 1 74  ? 17.328 13.369  -16.751 1    58.84  ? 74  HIS   A CD2   1 1 
ATOM   329  C  CE1   . HIS   A 1 74  ? 17.256 11.708  -18.161 1    60.53  ? 74  HIS   A CE1   1 1 
ATOM   330  N  NE2   . HIS   A 1 74  ? 16.755 12.919  -17.919 1    60.23  ? 74  HIS   A NE2   1 1 
ATOM   331  N  N     . ARG   A 1 75  ? 21.696 13.063  -13.487 1    49.91  ? 75  ARG   A N     1 1 
ATOM   332  C  CA    . ARG   A 1 75  ? 22.545 12.876  -12.311 1    48.69  ? 75  ARG   A CA    1 1 
ATOM   333  C  C     . ARG   A 1 75  ? 22.945 14.185  -11.653 1    48.36  ? 75  ARG   A C     1 1 
ATOM   334  O  O     . ARG   A 1 75  ? 22.965 14.263  -10.43  1    48.33  ? 75  ARG   A O     1 1 
ATOM   335  C  CB    . ARG   A 1 75  ? 23.774 12.005  -12.625 1    49.52  ? 75  ARG   A CB    1 1 
ATOM   336  C  CG    . ARG   A 1 75  ? 23.464 10.526  -12.891 1    51.05  ? 75  ARG   A CG    1 1 
ATOM   337  C  CD    . ARG   A 1 75  ? 22.554 9.869   -11.857 1    53.81  ? 75  ARG   A CD    1 1 
ATOM   338  N  NE    . ARG   A 1 75  ? 21.193 9.743   -12.378 1    58.59  ? 75  ARG   A NE    1 1 
ATOM   339  C  CZ    . ARG   A 1 75  ? 20.098 10.137  -11.735 1    61.95  ? 75  ARG   A CZ    1 1 
ATOM   340  N  NH1   . ARG   A 1 75  ? 18.902 9.986   -12.294 1    61.95  ? 75  ARG   A NH1   1 1 
ATOM   341  N  NH2   . ARG   A 1 75  ? 20.187 10.674  -10.523 1    62.18  ? 75  ARG   A NH2   1 1 
ATOM   342  N  N     . ILE   A 1 76  ? 23.192 15.239  -12.445 1    48.16  ? 76  ILE   A N     1 1 
ATOM   343  C  CA    . ILE   A 1 76  ? 23.494 16.56   -11.893 1    48.23  ? 76  ILE   A CA    1 1 
ATOM   344  C  C     . ILE   A 1 76  ? 22.263 17.11   -11.157 1    48.91  ? 76  ILE   A C     1 1 
ATOM   345  O  O     . ILE   A 1 76  ? 22.404 17.635  -10.059 1    49.52  ? 76  ILE   A O     1 1 
ATOM   346  C  CB    . ILE   A 1 76  ? 24.052 17.511  -12.982 1    47.72  ? 76  ILE   A CB    1 1 
ATOM   347  C  CG1   . ILE   A 1 76  ? 25.446 17.025  -13.438 1    48.22  ? 76  ILE   A CG1   1 1 
ATOM   348  C  CG2   . ILE   A 1 76  ? 24.082 18.964  -12.499 1    47.34  ? 76  ILE   A CG2   1 1 
ATOM   349  C  CD1   . ILE   A 1 76  ? 26.019 17.792  -14.624 1    48.67  ? 76  ILE   A CD1   1 1 
ATOM   350  N  N     . LYS   A 1 77  ? 21.056 16.874  -11.687 1    49.01  ? 77  LYS   A N     1 1 
ATOM   351  C  CA    . LYS   A 1 77  ? 19.8   17.264  -11.032 1    50.08  ? 77  LYS   A CA    1 1 
ATOM   352  C  C     . LYS   A 1 77  ? 19.677 16.527  -9.663  1    49.82  ? 77  LYS   A C     1 1 
ATOM   353  O  O     . LYS   A 1 77  ? 19.268 17.128  -8.677  1    50.34  ? 77  LYS   A O     1 1 
ATOM   354  C  CB    . LYS   A 1 77  ? 18.603 16.957  -11.966 1    53.42  ? 77  LYS   A CB    1 1 
ATOM   355  C  CG    . LYS   A 1 77  ? 17.259 17.521  -11.517 1    60.67  ? 77  LYS   A CG    1 1 
ATOM   356  C  CD    . LYS   A 1 77  ? 16.513 18.203  -12.683 1    67.32  ? 77  LYS   A CD    1 1 
ATOM   357  C  CE    . LYS   A 1 77  ? 15.017 18.247  -12.471 1    73.53  ? 77  LYS   A CE    1 1 
ATOM   358  N  NZ    . LYS   A 1 77  ? 14.38  19.442  -13.114 1    77.59  ? 77  LYS   A NZ    1 1 
ATOM   359  N  N     . GLY   A 1 78  ? 20.1   15.267  -9.608  1    48.75  ? 78  GLY   A N     1 1 
ATOM   360  C  CA    . GLY   A 1 78  ? 20.159 14.487  -8.376  1    48.33  ? 78  GLY   A CA    1 1 
ATOM   361  C  C     . GLY   A 1 78  ? 21.074 15.101  -7.327  1    48.14  ? 78  GLY   A C     1 1 
ATOM   362  O  O     . GLY   A 1 78  ? 20.737 15.088  -6.146  1    48.91  ? 78  GLY   A O     1 1 
ATOM   363  N  N     . PHE   A 1 79  ? 22.207 15.699  -7.739  1    47.07  ? 79  PHE   A N     1 1 
ATOM   364  C  CA    . PHE   A 1 79  ? 23.148 16.387  -6.837  1    46.85  ? 79  PHE   A CA    1 1 
ATOM   365  C  C     . PHE   A 1 79  ? 22.544 17.692  -6.32   1    47.28  ? 79  PHE   A C     1 1 
ATOM   366  O  O     . PHE   A 1 79  ? 22.744 18.048  -5.157  1    47.36  ? 79  PHE   A O     1 1 
ATOM   367  C  CB    . PHE   A 1 79  ? 24.501 16.681  -7.54   1    46.42  ? 79  PHE   A CB    1 1 
ATOM   368  C  CG    . PHE   A 1 79  ? 25.505 15.55   -7.504  1    46.55  ? 79  PHE   A CG    1 1 
ATOM   369  C  CD1   . PHE   A 1 79  ? 25.482 14.551  -8.459  1    47.3   ? 79  PHE   A CD1   1 1 
ATOM   370  C  CD2   . PHE   A 1 79  ? 26.482 15.498  -6.524  1    47.01  ? 79  PHE   A CD2   1 1 
ATOM   371  C  CE1   . PHE   A 1 79  ? 26.404 13.508  -8.425  1    47.96  ? 79  PHE   A CE1   1 1 
ATOM   372  C  CE2   . PHE   A 1 79  ? 27.39  14.442  -6.48   1    47.62  ? 79  PHE   A CE2   1 1 
ATOM   373  C  CZ    . PHE   A 1 79  ? 27.352 13.461  -7.436  1    47.44  ? 79  PHE   A CZ    1 1 
ATOM   374  N  N     . ARG   A 1 80  ? 21.809 18.414  -7.177  1    47.57  ? 80  ARG   A N     1 1 
ATOM   375  C  CA    . ARG   A 1 80  ? 21.119 19.654  -6.781  1    48.48  ? 80  ARG   A CA    1 1 
ATOM   376  C  C     . ARG   A 1 80  ? 20.004 19.393  -5.755  1    49.55  ? 80  ARG   A C     1 1 
ATOM   377  O  O     . ARG   A 1 80  ? 19.639 20.295  -4.996  1    50.34  ? 80  ARG   A O     1 1 
ATOM   378  C  CB    . ARG   A 1 80  ? 20.49  20.326  -8.006  1    49.32  ? 80  ARG   A CB    1 1 
ATOM   379  C  CG    . ARG   A 1 80  ? 21.513 20.857  -8.995  1    51.9   ? 80  ARG   A CG    1 1 
ATOM   380  C  CD    . ARG   A 1 80  ? 20.813 21.302  -10.254 1    54.87  ? 80  ARG   A CD    1 1 
ATOM   381  N  NE    . ARG   A 1 80  ? 21.724 22.033  -11.125 1    58.8   ? 80  ARG   A NE    1 1 
ATOM   382  C  CZ    . ARG   A 1 80  ? 21.363 22.646  -12.247 1    61.68  ? 80  ARG   A CZ    1 1 
ATOM   383  N  NH1   . ARG   A 1 80  ? 20.098 22.624  -12.647 1    62.05  ? 80  ARG   A NH1   1 1 
ATOM   384  N  NH2   . ARG   A 1 80  ? 22.263 23.292  -12.976 1    61.66  ? 80  ARG   A NH2   1 1 
ATOM   385  N  N     . SER   A 1 81  ? 19.454 18.171  -5.745  1    48.91  ? 81  SER   A N     1 1 
ATOM   386  C  CA    . SER   A 1 81  ? 18.376 17.77   -4.857  1    49.09  ? 81  SER   A CA    1 1 
ATOM   387  C  C     . SER   A 1 81  ? 18.82  17.136  -3.552  1    48.5   ? 81  SER   A C     1 1 
ATOM   388  O  O     . SER   A 1 81  ? 17.983 16.932  -2.683  1    48.86  ? 81  SER   A O     1 1 
ATOM   389  C  CB    . SER   A 1 81  ? 17.428 16.829  -5.589  1    51.17  ? 81  SER   A CB    1 1 
ATOM   390  O  OG    . SER   A 1 81  ? 16.982 17.464  -6.778  1    55.1   ? 81  SER   A OG    1 1 
ATOM   391  N  N     . LEU   A 1 82  ? 20.108 16.811  -3.406  1    48.16  ? 82  LEU   A N     1 1 
ATOM   392  C  CA    . LEU   A 1 82  ? 20.675 16.2    -2.193  1    48.17  ? 82  LEU   A CA    1 1 
ATOM   393  C  C     . LEU   A 1 82  ? 20.392 17.072  -0.965  1    47.04  ? 82  LEU   A C     1 1 
ATOM   394  O  O     . LEU   A 1 82  ? 20.458 18.285  -1.077  1    46.03  ? 82  LEU   A O     1 1 
ATOM   395  C  CB    . LEU   A 1 82  ? 22.211 16.135  -2.343  1    48.72  ? 82  LEU   A CB    1 1 
ATOM   396  C  CG    . LEU   A 1 82  ? 22.815 14.867  -2.923  1    50.91  ? 82  LEU   A CG    1 1 
ATOM   397  C  CD1   . LEU   A 1 82  ? 24.313 15.062  -3.171  1    51.65  ? 82  LEU   A CD1   1 1 
ATOM   398  C  CD2   . LEU   A 1 82  ? 22.562 13.66   -2.006  1    51.35  ? 82  LEU   A CD2   1 1 
ATOM   399  N  N     . PRO   A 1 83  ? 20.222 16.494  0.239   1    47.05  ? 83  PRO   A N     1 1 
ATOM   400  C  CA    . PRO   A 1 83  ? 20.048 17.336  1.441   1    47.36  ? 83  PRO   A CA    1 1 
ATOM   401  C  C     . PRO   A 1 83  ? 21.183 18.363  1.589   1    48.33  ? 83  PRO   A C     1 1 
ATOM   402  O  O     . PRO   A 1 83  ? 22.339 18.055  1.299   1    49.14  ? 83  PRO   A O     1 1 
ATOM   403  C  CB    . PRO   A 1 83  ? 19.998 16.319  2.575   1    47.68  ? 83  PRO   A CB    1 1 
ATOM   404  C  CG    . PRO   A 1 83  ? 19.48  15.065  1.915   1    48.14  ? 83  PRO   A CG    1 1 
ATOM   405  C  CD    . PRO   A 1 83  ? 20.14  15.058  0.566   1    46.33  ? 83  PRO   A CD    1 1 
ATOM   406  N  N     . PHE   A 1 84  ? 20.827 19.6    1.906   1    47.91  ? 84  PHE   A N     1 1 
ATOM   407  C  CA    . PHE   A 1 84  ? 21.735 20.734  1.977   1    48.95  ? 84  PHE   A CA    1 1 
ATOM   408  C  C     . PHE   A 1 84  ? 23.056 20.473  2.695   1    49.49  ? 84  PHE   A C     1 1 
ATOM   409  O  O     . PHE   A 1 84  ? 24.113 20.812  2.161   1    49.81  ? 84  PHE   A O     1 1 
ATOM   410  C  CB    . PHE   A 1 84  ? 21.02  21.938  2.598   1    49.09  ? 84  PHE   A CB    1 1 
ATOM   411  C  CG    . PHE   A 1 84  ? 21.858 23.186  2.712   1    50.46  ? 84  PHE   A CG    1 1 
ATOM   412  C  CD1   . PHE   A 1 84  ? 22.23  23.897  1.578   1    51.55  ? 84  PHE   A CD1   1 1 
ATOM   413  C  CD2   . PHE   A 1 84  ? 22.245 23.668  3.952   1    51.29  ? 84  PHE   A CD2   1 1 
ATOM   414  C  CE1   . PHE   A 1 84  ? 22.982 25.064  1.688   1    52.72  ? 84  PHE   A CE1   1 1 
ATOM   415  C  CE2   . PHE   A 1 84  ? 22.961 24.856  4.063   1    52.4   ? 84  PHE   A CE2   1 1 
ATOM   416  C  CZ    . PHE   A 1 84  ? 23.318 25.552  2.931   1    52.61  ? 84  PHE   A CZ    1 1 
ATOM   417  N  N     . ILE   A 1 85  ? 23.006 19.9    3.897   1    49.75  ? 85  ILE   A N     1 1 
ATOM   418  C  CA    . ILE   A 1 85  ? 24.21  19.635  4.668   1    51.09  ? 85  ILE   A CA    1 1 
ATOM   419  C  C     . ILE   A 1 85  ? 25.144 18.646  3.941   1    51.36  ? 85  ILE   A C     1 1 
ATOM   420  O  O     . ILE   A 1 85  ? 26.365 18.769  4.054   1    52.32  ? 85  ILE   A O     1 1 
ATOM   421  C  CB    . ILE   A 1 85  ? 23.815 19.2    6.097   1    52.37  ? 85  ILE   A CB    1 1 
ATOM   422  C  CG1   . ILE   A 1 85  ? 25.03  19.131  7.024   1    53.85  ? 85  ILE   A CG1   1 1 
ATOM   423  C  CG2   . ILE   A 1 85  ? 23.004 17.919  6.104   1    52.46  ? 85  ILE   A CG2   1 1 
ATOM   424  C  CD1   . ILE   A 1 85  ? 25.179 20.356  7.819   1    55.58  ? 85  ILE   A CD1   1 1 
ATOM   425  N  N     . ILE   A 1 86  ? 24.581 17.732  3.126   1    50.5   ? 86  ILE   A N     1 1 
ATOM   426  C  CA    . ILE   A 1 86  ? 25.361 16.784  2.333   1    50.38  ? 86  ILE   A CA    1 1 
ATOM   427  C  C     . ILE   A 1 86  ? 25.95  17.472  1.093   1    50.62  ? 86  ILE   A C     1 1 
ATOM   428  O  O     . ILE   A 1 86  ? 27.142 17.343  0.839   1    51.35  ? 86  ILE   A O     1 1 
ATOM   429  C  CB    . ILE   A 1 86  ? 24.532 15.537  1.985   1    50.22  ? 86  ILE   A CB    1 1 
ATOM   430  C  CG1   . ILE   A 1 86  ? 24.245 14.709  3.241   1    50.35  ? 86  ILE   A CG1   1 1 
ATOM   431  C  CG2   . ILE   A 1 86  ? 25.225 14.702  0.913   1    50.89  ? 86  ILE   A CG2   1 1 
ATOM   432  C  CD1   . ILE   A 1 86  ? 23.29  13.541  3.013   1    51.03  ? 86  ILE   A CD1   1 1 
ATOM   433  N  N     . GLY   A 1 87  ? 25.142 18.25   0.382   1    49.91  ? 87  GLY   A N     1 1 
ATOM   434  C  CA    . GLY   A 1 87  ? 25.585 18.957  -0.809  1    50.02  ? 87  GLY   A CA    1 1 
ATOM   435  C  C     . GLY   A 1 87  ? 26.711 19.935  -0.542  1    51.18  ? 87  GLY   A C     1 1 
ATOM   436  O  O     . GLY   A 1 87  ? 27.527 20.186  -1.425  1    51.21  ? 87  GLY   A O     1 1 
ATOM   437  N  N     . CYS   A 1 88  ? 26.753 20.499  0.686   1    51.5   ? 88  CYS   A N     1 1 
ATOM   438  C  CA    . CYS   A 1 88  ? 27.778 21.428  1.151   1    51.96  ? 88  CYS   A CA    1 1 
ATOM   439  C  C     . CYS   A 1 88  ? 29.094 20.734  1.508   1    52.15  ? 88  CYS   A C     1 1 
ATOM   440  O  O     . CYS   A 1 88  ? 30.08  21.428  1.709   1    52.74  ? 88  CYS   A O     1 1 
ATOM   441  C  CB    . CYS   A 1 88  ? 27.267 22.239  2.337   1    52.63  ? 88  CYS   A CB    1 1 
ATOM   442  S  SG    . CYS   A 1 88  ? 26.011 23.456  1.906   1    58.17  ? 88  CYS   A SG    1 1 
ATOM   443  N  N     . ASN   A 1 89  ? 29.118 19.4    1.667   1    51.58  ? 89  ASN   A N     1 1 
ATOM   444  C  CA    . ASN   A 1 89  ? 30.355 18.708  2.022   1    51.57  ? 89  ASN   A CA    1 1 
ATOM   445  C  C     . ASN   A 1 89  ? 31.424 18.943  0.915   1    52.13  ? 89  ASN   A C     1 1 
ATOM   446  O  O     . ASN   A 1 89  ? 31.103 18.872  -0.275  1    52.37  ? 89  ASN   A O     1 1 
ATOM   447  C  CB    . ASN   A 1 89  ? 30.096 17.235  2.286   1    51.85  ? 89  ASN   A CB    1 1 
ATOM   448  C  CG    . ASN   A 1 89  ? 31.358 16.415  2.451   1    54.73  ? 89  ASN   A CG    1 1 
ATOM   449  O  OD1   . ASN   A 1 89  ? 31.944 15.938  1.48    1    56.66  ? 89  ASN   A OD1   1 1 
ATOM   450  N  ND2   . ASN   A 1 89  ? 31.814 16.244  3.669   1    54.55  ? 89  ASN   A ND2   1 1 
ATOM   451  N  N     . PRO   A 1 90  ? 32.666 19.294  1.302   1    51.66  ? 90  PRO   A N     1 1 
ATOM   452  C  CA    . PRO   A 1 90  ? 33.697 19.579  0.289   1    51.48  ? 90  PRO   A CA    1 1 
ATOM   453  C  C     . PRO   A 1 90  ? 33.933 18.463  -0.726  1    51.03  ? 90  PRO   A C     1 1 
ATOM   454  O  O     . PRO   A 1 90  ? 34.185 18.751  -1.893  1    51.56  ? 90  PRO   A O     1 1 
ATOM   455  C  CB    . PRO   A 1 90  ? 34.961 19.89   1.126   1    52.18  ? 90  PRO   A CB    1 1 
ATOM   456  C  CG    . PRO   A 1 90  ? 34.433 20.292  2.477   1    52.73  ? 90  PRO   A CG    1 1 
ATOM   457  C  CD    . PRO   A 1 90  ? 33.184 19.463  2.675   1    51.19  ? 90  PRO   A CD    1 1 
ATOM   458  N  N     . THR   A 1 91  ? 33.841 17.206  -0.304  1    50.36  ? 91  THR   A N     1 1 
ATOM   459  C  CA    . THR   A 1 91  ? 34.067 16.071  -1.209  1    50.37  ? 91  THR   A CA    1 1 
ATOM   460  C  C     . THR   A 1 91  ? 32.883 15.875  -2.163  1    49.81  ? 91  THR   A C     1 1 
ATOM   461  O  O     . THR   A 1 91  ? 33.086 15.64   -3.359  1    49.86  ? 91  THR   A O     1 1 
ATOM   462  C  CB    . THR   A 1 91  ? 34.432 14.822  -0.41   1    51.47  ? 91  THR   A CB    1 1 
ATOM   463  O  OG1   . THR   A 1 91  ? 35.566 15.128  0.4     1    52.45  ? 91  THR   A OG1   1 1 
ATOM   464  C  CG2   . THR   A 1 91  ? 34.752 13.661  -1.286  1    51.88  ? 91  THR   A CG2   1 1 
ATOM   465  N  N     . ILE   A 1 92  ? 31.65  16.018  -1.648  1    48.78  ? 92  ILE   A N     1 1 
ATOM   466  C  CA    . ILE   A 1 92  ? 30.452 15.935  -2.472  1    48.66  ? 92  ILE   A CA    1 1 
ATOM   467  C  C     . ILE   A 1 92  ? 30.461 17.079  -3.509  1    48.41  ? 92  ILE   A C     1 1 
ATOM   468  O  O     . ILE   A 1 92  ? 30.238 16.828  -4.688  1    48.24  ? 92  ILE   A O     1 1 
ATOM   469  C  CB    . ILE   A 1 92  ? 29.177 15.945  -1.584  1    49.18  ? 92  ILE   A CB    1 1 
ATOM   470  C  CG1   . ILE   A 1 92  ? 29.153 14.729  -0.617  1    49.71  ? 92  ILE   A CG1   1 1 
ATOM   471  C  CG2   . ILE   A 1 92  ? 27.923 15.977  -2.439  1    49.63  ? 92  ILE   A CG2   1 1 
ATOM   472  C  CD1   . ILE   A 1 92  ? 29.307 13.357  -1.31   1    50.13  ? 92  ILE   A CD1   1 1 
ATOM   473  N  N     . LEU   A 1 93  ? 30.829 18.302  -3.085  1    48.33  ? 93  LEU   A N     1 1 
ATOM   474  C  CA    . LEU   A 1 93  ? 30.935 19.459  -3.983  1    49.19  ? 93  LEU   A CA    1 1 
ATOM   475  C  C     . LEU   A 1 93  ? 31.959 19.186  -5.089  1    49.06  ? 93  LEU   A C     1 1 
ATOM   476  O  O     . LEU   A 1 93  ? 31.721 19.547  -6.232  1    49.2   ? 93  LEU   A O     1 1 
ATOM   477  C  CB    . LEU   A 1 93  ? 31.364 20.726  -3.225  1    49.44  ? 93  LEU   A CB    1 1 
ATOM   478  C  CG    . LEU   A 1 93  ? 30.265 21.586  -2.653  1    52.14  ? 93  LEU   A CG    1 1 
ATOM   479  C  CD1   . LEU   A 1 93  ? 30.865 22.79   -1.915  1    52.9   ? 93  LEU   A CD1   1 1 
ATOM   480  C  CD2   . LEU   A 1 93  ? 29.331 22.086  -3.75   1    52.77  ? 93  LEU   A CD2   1 1 
ATOM   481  N  N     . HIS   A 1 94  ? 33.092 18.571  -4.746  1    48.85  ? 94  HIS   A N     1 1 
ATOM   482  C  CA    . HIS   A 1 94  ? 34.126 18.233  -5.712  1    50     ? 94  HIS   A CA    1 1 
ATOM   483  C  C     . HIS   A 1 94  ? 33.581 17.289  -6.806  1    50.01  ? 94  HIS   A C     1 1 
ATOM   484  O  O     . HIS   A 1 94  ? 33.752 17.59   -7.987  1    50.39  ? 94  HIS   A O     1 1 
ATOM   485  C  CB    . HIS   A 1 94  ? 35.346 17.62   -5.006  1    51.61  ? 94  HIS   A CB    1 1 
ATOM   486  C  CG    . HIS   A 1 94  ? 36.418 17.171  -5.947  1    55.91  ? 94  HIS   A CG    1 1 
ATOM   487  N  ND1   . HIS   A 1 94  ? 36.749 15.831  -6.083  1    58.39  ? 94  HIS   A ND1   1 1 
ATOM   488  C  CD2   . HIS   A 1 94  ? 37.203 17.901  -6.777  1    57.66  ? 94  HIS   A CD2   1 1 
ATOM   489  C  CE1   . HIS   A 1 94  ? 37.728 15.786  -6.975  1    58.64  ? 94  HIS   A CE1   1 1 
ATOM   490  N  NE2   . HIS   A 1 94  ? 38.039 17.005  -7.421  1    58.98  ? 94  HIS   A NE2   1 1 
ATOM   491  N  N     . VAL   A 1 95  ? 32.883 16.191  -6.418  1    49.14  ? 95  VAL   A N     1 1 
ATOM   492  C  CA    . VAL   A 1 95  ? 32.284 15.262  -7.38   1    49.09  ? 95  VAL   A CA    1 1 
ATOM   493  C  C     . VAL   A 1 95  ? 31.214 15.993  -8.225  1    49.41  ? 95  VAL   A C     1 1 
ATOM   494  O  O     . VAL   A 1 95  ? 31.171 15.836  -9.454  1    49.85  ? 95  VAL   A O     1 1 
ATOM   495  C  CB    . VAL   A 1 95  ? 31.713 14.009  -6.687  1    49.09  ? 95  VAL   A CB    1 1 
ATOM   496  C  CG1   . VAL   A 1 95  ? 31.006 13.106  -7.684  1    49.28  ? 95  VAL   A CG1   1 1 
ATOM   497  C  CG2   . VAL   A 1 95  ? 32.811 13.252  -5.949  1    49.51  ? 95  VAL   A CG2   1 1 
ATOM   498  N  N     . HIS   A 1 96  ? 30.403 16.849  -7.576  1    48.56  ? 96  HIS   A N     1 1 
ATOM   499  C  CA    . HIS   A 1 96  ? 29.397 17.673  -8.257  1    48.52  ? 96  HIS   A CA    1 1 
ATOM   500  C  C     . HIS   A 1 96  ? 30.094 18.562  -9.343  1    48.31  ? 96  HIS   A C     1 1 
ATOM   501  O  O     . HIS   A 1 96  ? 29.662 18.563  -10.49  1    47.83  ? 96  HIS   A O     1 1 
ATOM   502  C  CB    . HIS   A 1 96  ? 28.657 18.53   -7.209  1    49.19  ? 96  HIS   A CB    1 1 
ATOM   503  C  CG    . HIS   A 1 96  ? 27.429 19.227  -7.701  1    51.19  ? 96  HIS   A CG    1 1 
ATOM   504  N  ND1   . HIS   A 1 96  ? 26.619 19.939  -6.834  1    53.21  ? 96  HIS   A ND1   1 1 
ATOM   505  C  CD2   . HIS   A 1 96  ? 26.908 19.304  -8.948  1    52.38  ? 96  HIS   A CD2   1 1 
ATOM   506  C  CE1   . HIS   A 1 96  ? 25.638 20.428  -7.574  1    53.72  ? 96  HIS   A CE1   1 1 
ATOM   507  N  NE2   . HIS   A 1 96  ? 25.768 20.074  -8.854  1    53.88  ? 96  HIS   A NE2   1 1 
ATOM   508  N  N     . GLU   A 1 97  ? 31.21  19.225  -8.997  1    48.64  ? 97  GLU   A N     1 1 
ATOM   509  C  CA    . GLU   A 1 97  ? 31.986 20.052  -9.938  1    49.72  ? 97  GLU   A CA    1 1 
ATOM   510  C  C     . GLU   A 1 97  ? 32.564 19.201  -11.082 1    48.74  ? 97  GLU   A C     1 1 
ATOM   511  O  O     . GLU   A 1 97  ? 32.481 19.61   -12.239 1    48.87  ? 97  GLU   A O     1 1 
ATOM   512  C  CB    . GLU   A 1 97  ? 33.129 20.804  -9.23   1    53.31  ? 97  GLU   A CB    1 1 
ATOM   513  C  CG    . GLU   A 1 97  ? 32.654 21.816  -8.203  1    62.19  ? 97  GLU   A CG    1 1 
ATOM   514  C  CD    . GLU   A 1 97  ? 33.732 22.485  -7.363  1    73.24  ? 97  GLU   A CD    1 1 
ATOM   515  O  OE1   . GLU   A 1 97  ? 34.936 22.214  -7.595  1    77.76  ? 97  GLU   A OE1   1 1 
ATOM   516  O  OE2   . GLU   A 1 97  ? 33.369 23.282  -6.468  1    74.95  ? 97  GLU   A OE2   1 1 
ATOM   517  N  N     . LEU   A 1 98  ? 33.095 18.008  -10.772 1    47.89  ? 98  LEU   A N     1 1 
ATOM   518  C  CA    . LEU   A 1 98  ? 33.64  17.075  -11.775 1    47.66  ? 98  LEU   A CA    1 1 
ATOM   519  C  C     . LEU   A 1 98  ? 32.558 16.732  -12.804 1    47.58  ? 98  LEU   A C     1 1 
ATOM   520  O  O     . LEU   A 1 98  ? 32.805 16.76   -14.009 1    47.67  ? 98  LEU   A O     1 1 
ATOM   521  C  CB    . LEU   A 1 98  ? 34.094 15.754  -11.103 1    47.9   ? 98  LEU   A CB    1 1 
ATOM   522  C  CG    . LEU   A 1 98  ? 35.365 15.759  -10.257 1    49.79  ? 98  LEU   A CG    1 1 
ATOM   523  C  CD1   . LEU   A 1 98  ? 35.711 14.344  -9.81   1    49.81  ? 98  LEU   A CD1   1 1 
ATOM   524  C  CD2   . LEU   A 1 98  ? 36.547 16.327  -11.028 1    50.27  ? 98  LEU   A CD2   1 1 
ATOM   525  N  N     . TYR   A 1 99  ? 31.341 16.447  -12.311 1    47.08  ? 99  TYR   A N     1 1 
ATOM   526  C  CA    . TYR   A 1 99  ? 30.203 16.084  -13.146 1    47.15  ? 99  TYR   A CA    1 1 
ATOM   527  C  C     . TYR   A 1 99  ? 29.701 17.244  -14.006 1    47.77  ? 99  TYR   A C     1 1 
ATOM   528  O  O     . TYR   A 1 99  ? 29.342 17.015  -15.157 1    48.37  ? 99  TYR   A O     1 1 
ATOM   529  C  CB    . TYR   A 1 99  ? 29.095 15.44   -12.288 1    46.53  ? 99  TYR   A CB    1 1 
ATOM   530  C  CG    . TYR   A 1 99  ? 29.371 13.98   -11.93  1    46.68  ? 99  TYR   A CG    1 1 
ATOM   531  C  CD1   . TYR   A 1 99  ? 30.578 13.369  -12.267 1    47.28  ? 99  TYR   A CD1   1 1 
ATOM   532  C  CD2   . TYR   A 1 99  ? 28.414 13.208  -11.293 1    47.32  ? 99  TYR   A CD2   1 1 
ATOM   533  C  CE1   . TYR   A 1 99  ? 30.808 12.026  -12.012 1    47.81  ? 99  TYR   A CE1   1 1 
ATOM   534  C  CE2   . TYR   A 1 99  ? 28.645 11.866  -11.008 1    48.23  ? 99  TYR   A CE2   1 1 
ATOM   535  C  CZ    . TYR   A 1 99  ? 29.843 11.279  -11.375 1    48.74  ? 99  TYR   A CZ    1 1 
ATOM   536  O  OH    . TYR   A 1 99  ? 30.074 9.947   -11.146 1    50.13  ? 99  TYR   A OH    1 1 
ATOM   537  N  N     . ILE   A 1 100 ? 29.747 18.48   -13.5   1    47.62  ? 100 ILE   A N     1 1 
ATOM   538  C  CA    . ILE   A 1 100 ? 29.361 19.648  -14.283 1    48.43  ? 100 ILE   A CA    1 1 
ATOM   539  C  C     . ILE   A 1 100 ? 30.41  19.842  -15.398 1    49.65  ? 100 ILE   A C     1 1 
ATOM   540  O  O     . ILE   A 1 100 ? 30.055 19.991  -16.567 1    49.68  ? 100 ILE   A O     1 1 
ATOM   541  C  CB    . ILE   A 1 100 ? 29.268 20.883  -13.357 1    48.73  ? 100 ILE   A CB    1 1 
ATOM   542  C  CG1   . ILE   A 1 100 ? 28.066 20.761  -12.395 1    49.92  ? 100 ILE   A CG1   1 1 
ATOM   543  C  CG2   . ILE   A 1 100 ? 29.206 22.182  -14.156 1    48.56  ? 100 ILE   A CG2   1 1 
ATOM   544  C  CD1   . ILE   A 1 100 ? 28.093 21.827  -11.239 1    51.33  ? 100 ILE   A CD1   1 1 
ATOM   545  N  N     . ARG   A 1 101 ? 31.691 19.75   -15.039 1    50.09  ? 101 ARG   A N     1 1 
ATOM   546  C  CA    . ARG   A 1 101 ? 32.797 19.853  -15.98  1    51.93  ? 101 ARG   A CA    1 1 
ATOM   547  C  C     . ARG   A 1 101 ? 32.702 18.766  -17.081 1    51.56  ? 101 ARG   A C     1 1 
ATOM   548  O  O     . ARG   A 1 101 ? 32.942 19.061  -18.259 1    51.5   ? 101 ARG   A O     1 1 
ATOM   549  C  CB    . ARG   A 1 101 ? 34.123 19.819  -15.195 1    56.06  ? 101 ARG   A CB    1 1 
ATOM   550  C  CG    . ARG   A 1 101 ? 35.359 19.362  -15.952 1    65.96  ? 101 ARG   A CG    1 1 
ATOM   551  C  CD    . ARG   A 1 101 ? 36.509 19.133  -14.97  1    75.48  ? 101 ARG   A CD    1 1 
ATOM   552  N  NE    . ARG   A 1 101 ? 37.732 18.635  -15.612 1    83.44  ? 101 ARG   A NE    1 1 
ATOM   553  C  CZ    . ARG   A 1 101 ? 38.502 17.673  -15.108 1    89.21  ? 101 ARG   A CZ    1 1 
ATOM   554  N  NH1   . ARG   A 1 101 ? 38.175 17.081  -13.964 1    89.24  ? 101 ARG   A NH1   1 1 
ATOM   555  N  NH2   . ARG   A 1 101 ? 39.6   17.286  -15.751 1    90.91  ? 101 ARG   A NH2   1 1 
ATOM   556  N  N     . ALA   A 1 102 ? 32.279 17.539  -16.712 1    50.88  ? 102 ALA   A N     1 1 
ATOM   557  C  CA    . ALA   A 1 102 ? 32.104 16.456  -17.679 1    50.66  ? 102 ALA   A CA    1 1 
ATOM   558  C  C     . ALA   A 1 102 ? 30.983 16.809  -18.651 1    50.04  ? 102 ALA   A C     1 1 
ATOM   559  O  O     . ALA   A 1 102 ? 31.145 16.604  -19.849 1    50.17  ? 102 ALA   A O     1 1 
ATOM   560  C  CB    . ALA   A 1 102 ? 31.791 15.14   -16.968 1    50.62  ? 102 ALA   A CB    1 1 
ATOM   561  N  N     . PHE   A 1 103 ? 29.876 17.376  -18.144 1    49.45  ? 103 PHE   A N     1 1 
ATOM   562  C  CA    . PHE   A 1 103 ? 28.74  17.803  -18.958 1    49.89  ? 103 PHE   A CA    1 1 
ATOM   563  C  C     . PHE   A 1 103 ? 29.183 18.906  -19.928 1    51.17  ? 103 PHE   A C     1 1 
ATOM   564  O  O     . PHE   A 1 103 ? 28.814 18.884  -21.105 1    50.96  ? 103 PHE   A O     1 1 
ATOM   565  C  CB    . PHE   A 1 103 ? 27.597 18.324  -18.063 1    49.35  ? 103 PHE   A CB    1 1 
ATOM   566  C  CG    . PHE   A 1 103 ? 26.359 18.744  -18.821 1    49.59  ? 103 PHE   A CG    1 1 
ATOM   567  C  CD1   . PHE   A 1 103 ? 25.452 17.802  -19.271 1    50.12  ? 103 PHE   A CD1   1 1 
ATOM   568  C  CD2   . PHE   A 1 103 ? 26.11  20.077  -19.088 1    50.68  ? 103 PHE   A CD2   1 1 
ATOM   569  C  CE1   . PHE   A 1 103 ? 24.316 18.185  -19.976 1    51.37  ? 103 PHE   A CE1   1 1 
ATOM   570  C  CE2   . PHE   A 1 103 ? 24.979 20.464  -19.803 1    51.94  ? 103 PHE   A CE2   1 1 
ATOM   571  C  CZ    . PHE   A 1 103 ? 24.083 19.514  -20.238 1    51.86  ? 103 PHE   A CZ    1 1 
ATOM   572  N  N     . GLN   A 1 104 ? 29.966 19.874  -19.43  1    52.03  ? 104 GLN   A N     1 1 
ATOM   573  C  CA    . GLN   A 1 104 ? 30.465 20.962  -20.26  1    53.73  ? 104 GLN   A CA    1 1 
ATOM   574  C  C     . GLN   A 1 104 ? 31.344 20.429  -21.406 1    53.98  ? 104 GLN   A C     1 1 
ATOM   575  O  O     . GLN   A 1 104 ? 31.057 20.725  -22.557 1    54.39  ? 104 GLN   A O     1 1 
ATOM   576  C  CB    . GLN   A 1 104 ? 31.192 22.021  -19.42  1    56.64  ? 104 GLN   A CB    1 1 
ATOM   577  C  CG    . GLN   A 1 104 ? 30.28  22.726  -18.421 1    63.52  ? 104 GLN   A CG    1 1 
ATOM   578  C  CD    . GLN   A 1 104 ? 31.034 23.698  -17.535 1    71.31  ? 104 GLN   A CD    1 1 
ATOM   579  O  OE1   . GLN   A 1 104 ? 32.193 23.465  -17.134 1    73.53  ? 104 GLN   A OE1   1 1 
ATOM   580  N  NE2   . GLN   A 1 104 ? 30.381 24.81   -17.201 1    72.21  ? 104 GLN   A NE2   1 1 
ATOM   581  N  N     . LYS   A 1 105 ? 32.35  19.598  -21.11  1    53.39  ? 105 LYS   A N     1 1 
ATOM   582  C  CA    . LYS   A 1 105 ? 33.212 19.03   -22.149 1    53.56  ? 105 LYS   A CA    1 1 
ATOM   583  C  C     . LYS   A 1 105 ? 32.429 18.244  -23.195 1    54.56  ? 105 LYS   A C     1 1 
ATOM   584  O  O     . LYS   A 1 105 ? 32.677 18.409  -24.386 1    55.19  ? 105 LYS   A O     1 1 
ATOM   585  C  CB    . LYS   A 1 105 ? 34.28  18.119  -21.537 1    54.25  ? 105 LYS   A CB    1 1 
ATOM   586  C  CG    . LYS   A 1 105 ? 35.346 18.83   -20.739 1    56.98  ? 105 LYS   A CG    1 1 
ATOM   587  C  CD    . LYS   A 1 105 ? 36.259 17.794  -20.118 1    60.39  ? 105 LYS   A CD    1 1 
ATOM   588  C  CE    . LYS   A 1 105 ? 37.459 18.421  -19.477 1    64.52  ? 105 LYS   A CE    1 1 
ATOM   589  N  NZ    . LYS   A 1 105 ? 38.333 17.391  -18.869 1    67.81  ? 105 LYS   A NZ    1 1 
ATOM   590  N  N     . LEU   A 1 106 ? 31.489 17.391  -22.762 1    54.61  ? 106 LEU   A N     1 1 
ATOM   591  C  CA    . LEU   A 1 106 ? 30.681 16.615  -23.698 1    55.15  ? 106 LEU   A CA    1 1 
ATOM   592  C  C     . LEU   A 1 106 ? 29.766 17.512  -24.55  1    56.64  ? 106 LEU   A C     1 1 
ATOM   593  O  O     . LEU   A 1 106 ? 29.673 17.293  -25.761 1    57.61  ? 106 LEU   A O     1 1 
ATOM   594  C  CB    . LEU   A 1 106 ? 29.879 15.527  -22.97  1    54.56  ? 106 LEU   A CB    1 1 
ATOM   595  C  CG    . LEU   A 1 106 ? 30.736 14.355  -22.478 1    54.98  ? 106 LEU   A CG    1 1 
ATOM   596  C  CD1   . LEU   A 1 106 ? 30.104 13.662  -21.318 1    55.01  ? 106 LEU   A CD1   1 1 
ATOM   597  C  CD2   . LEU   A 1 106 ? 31.048 13.376  -23.604 1    54.96  ? 106 LEU   A CD2   1 1 
ATOM   598  N  N     . THR   A 1 107 ? 29.125 18.525  -23.944 1    56.41  ? 107 THR   A N     1 1 
ATOM   599  C  CA    . THR   A 1 107 ? 28.245 19.41   -24.702 1    57.89  ? 107 THR   A CA    1 1 
ATOM   600  C  C     . THR   A 1 107 ? 29.037 20.386  -25.602 1    59.42  ? 107 THR   A C     1 1 
ATOM   601  O  O     . THR   A 1 107 ? 28.498 20.848  -26.599 1    59.54  ? 107 THR   A O     1 1 
ATOM   602  C  CB    . THR   A 1 107 ? 27.218 20.112  -23.804 1    58.92  ? 107 THR   A CB    1 1 
ATOM   603  O  OG1   . THR   A 1 107 ? 27.885 20.748  -22.714 1    60.25  ? 107 THR   A OG1   1 1 
ATOM   604  C  CG2   . THR   A 1 107 ? 26.156 19.155  -23.282 1    58.74  ? 107 THR   A CG2   1 1 
ATOM   605  N  N     . ASP   A 1 108 ? 30.309 20.669  -25.275 1    60.08  ? 108 ASP   A N     1 1 
ATOM   606  C  CA    . ASP   A 1 108 ? 31.154 21.525  -26.096 1    60.92  ? 108 ASP   A CA    1 1 
ATOM   607  C  C     . ASP   A 1 108 ? 31.645 20.789  -27.338 1    61.15  ? 108 ASP   A C     1 1 
ATOM   608  O  O     . ASP   A 1 108 ? 31.993 21.449  -28.3   1    61.72  ? 108 ASP   A O     1 1 
ATOM   609  C  CB    . ASP   A 1 108 ? 32.365 22.045  -25.304 1    63.17  ? 108 ASP   A CB    1 1 
ATOM   610  C  CG    . ASP   A 1 108 ? 32.043 23.151  -24.316 1    70.4   ? 108 ASP   A CG    1 1 
ATOM   611  O  OD1   . ASP   A 1 108 ? 30.942 23.744  -24.421 1    71.93  ? 108 ASP   A OD1   1 1 
ATOM   612  O  OD2   . ASP   A 1 108 ? 32.879 23.405  -23.414 1    73.11  ? 108 ASP   A OD2   1 1 
ATOM   613  N  N     . PHE   A 1 109 ? 31.73  19.446  -27.316 1    60.8   ? 109 PHE   A N     1 1 
ATOM   614  C  CA    . PHE   A 1 109 ? 32.217 18.675  -28.449 1    61.08  ? 109 PHE   A CA    1 1 
ATOM   615  C  C     . PHE   A 1 109 ? 31.291 18.82   -29.653 1    62.91  ? 109 PHE   A C     1 1 
ATOM   616  O  O     . PHE   A 1 109 ? 30.094 18.587  -29.544 1    63.63  ? 109 PHE   A O     1 1 
ATOM   617  C  CB    . PHE   A 1 109 ? 32.436 17.199  -28.066 1    60.13  ? 109 PHE   A CB    1 1 
ATOM   618  C  CG    . PHE   A 1 109 ? 33.507 16.547  -28.911 1    59.89  ? 109 PHE   A CG    1 1 
ATOM   619  C  CD1   . PHE   A 1 109 ? 33.202 15.999  -30.146 1    60.26  ? 109 PHE   A CD1   1 1 
ATOM   620  C  CD2   . PHE   A 1 109 ? 34.831 16.557  -28.508 1    60.06  ? 109 PHE   A CD2   1 1 
ATOM   621  C  CE1   . PHE   A 1 109 ? 34.195 15.457  -30.952 1    60.58  ? 109 PHE   A CE1   1 1 
ATOM   622  C  CE2   . PHE   A 1 109 ? 35.815 15.974  -29.296 1    60.55  ? 109 PHE   A CE2   1 1 
ATOM   623  C  CZ    . PHE   A 1 109 ? 35.493 15.442  -30.519 1    60.27  ? 109 PHE   A CZ    1 1 
ATOM   624  N  N     . PRO   A 1 110 ? 31.824 19.264  -30.801 1    63.7   ? 110 PRO   A N     1 1 
ATOM   625  C  CA    . PRO   A 1 110 ? 30.971 19.452  -31.982 1    64.89  ? 110 PRO   A CA    1 1 
ATOM   626  C  C     . PRO   A 1 110 ? 30.42  18.141  -32.534 1    66.64  ? 110 PRO   A C     1 1 
ATOM   627  O  O     . PRO   A 1 110 ? 31.045 17.098  -32.379 1    66.65  ? 110 PRO   A O     1 1 
ATOM   628  C  CB    . PRO   A 1 110 ? 31.909 20.126  -32.997 1    65.21  ? 110 PRO   A CB    1 1 
ATOM   629  C  CG    . PRO   A 1 110 ? 33.105 20.548  -32.224 1    65.38  ? 110 PRO   A CG    1 1 
ATOM   630  C  CD    . PRO   A 1 110 ? 33.227 19.601  -31.089 1    63.35  ? 110 PRO   A CD    1 1 
ATOM   631  N  N     . PRO   A 1 111 ? 29.274 18.173  -33.234 1    67.98  ? 111 PRO   A N     1 1 
ATOM   632  C  CA    . PRO   A 1 111 ? 28.734 16.926  -33.812 1    69.21  ? 111 PRO   A CA    1 1 
ATOM   633  C  C     . PRO   A 1 111 ? 29.761 16.123  -34.62  1    70.52  ? 111 PRO   A C     1 1 
ATOM   634  O  O     . PRO   A 1 111 ? 30.552 16.694  -35.367 1    71.03  ? 111 PRO   A O     1 1 
ATOM   635  C  CB    . PRO   A 1 111 ? 27.586 17.411  -34.705 1    70.06  ? 111 PRO   A CB    1 1 
ATOM   636  C  CG    . PRO   A 1 111 ? 27.206 18.76   -34.166 1    70.09  ? 111 PRO   A CG    1 1 
ATOM   637  C  CD    . PRO   A 1 111 ? 28.432 19.348  -33.544 1    67.93  ? 111 PRO   A CD    1 1 
ATOM   638  N  N     . ILE   A 1 112 ? 29.795 14.812  -34.409 1    71.16  ? 112 ILE   A N     1 1 
ATOM   639  C  CA    . ILE   A 1 112 ? 30.717 13.922  -35.103 1    72.29  ? 112 ILE   A CA    1 1 
ATOM   640  C  C     . ILE   A 1 112 ? 30.261 13.77   -36.549 1    73.99  ? 112 ILE   A C     1 1 
ATOM   641  O  O     . ILE   A 1 112 ? 29.167 13.272  -36.8   1    74.23  ? 112 ILE   A O     1 1 
ATOM   642  C  CB    . ILE   A 1 112 ? 30.812 12.557  -34.375 1    72.26  ? 112 ILE   A CB    1 1 
ATOM   643  C  CG1   . ILE   A 1 112 ? 31.46  12.711  -32.988 1    72.65  ? 112 ILE   A CG1   1 1 
ATOM   644  C  CG2   . ILE   A 1 112 ? 31.548 11.523  -35.222 1    72.73  ? 112 ILE   A CG2   1 1 
ATOM   645  C  CD1   . ILE   A 1 112 ? 31.423 11.412  -32.137 1    73.64  ? 112 ILE   A CD1   1 1 
ATOM   646  N  N     . LYS   A 1 113 ? 31.069 14.251  -37.492 1    74.99  ? 113 LYS   A N     1 1 
ATOM   647  C  CA    . LYS   A 1 113 ? 30.725 14.166  -38.907 1    76.43  ? 113 LYS   A CA    1 1 
ATOM   648  C  C     . LYS   A 1 113 ? 31.565 13.102  -39.62  1    77.42  ? 113 LYS   A C     1 1 
ATOM   649  O  O     . LYS   A 1 113 ? 31.089 12.493  -40.581 1    78.3   ? 113 LYS   A O     1 1 
ATOM   650  C  CB    . LYS   A 1 113 ? 30.912 15.523  -39.613 1    78.69  ? 113 LYS   A CB    1 1 
ATOM   651  C  CG    . LYS   A 1 113 ? 30.457 16.748  -38.823 1    83.55  ? 113 LYS   A CG    1 1 
ATOM   652  C  CD    . LYS   A 1 113 ? 29.065 17.251  -39.213 1    88.33  ? 113 LYS   A CD    1 1 
ATOM   653  C  CE    . LYS   A 1 113 ? 28.837 18.659  -38.696 1    91.99  ? 113 LYS   A CE    1 1 
ATOM   654  N  NZ    . LYS   A 1 113 ? 27.404 19.065  -38.747 1    94.13  ? 113 LYS   A NZ    1 1 
ATOM   655  N  N     . ASP   A 1 114 ? 32.818 12.89   -39.176 1    76.8   ? 114 ASP   A N     1 1 
ATOM   656  C  CA    . ASP   A 1 114 ? 33.708 11.946  -39.844 1    76.29  ? 114 ASP   A CA    1 1 
ATOM   657  C  C     . ASP   A 1 114 ? 34.583 11.126  -38.864 1    75.53  ? 114 ASP   A C     1 1 
ATOM   658  O  O     . ASP   A 1 114 ? 34.463 11.282  -37.65  1    75.9   ? 114 ASP   A O     1 1 
ATOM   659  C  CB    . ASP   A 1 114 ? 34.552 12.702  -40.898 1    77.58  ? 114 ASP   A CB    1 1 
ATOM   660  C  CG    . ASP   A 1 114 ? 35.368 13.847  -40.33  1    82.28  ? 114 ASP   A CG    1 1 
ATOM   661  O  OD1   . ASP   A 1 114 ? 35.948 13.678  -39.241 1    82.54  ? 114 ASP   A OD1   1 1 
ATOM   662  O  OD2   . ASP   A 1 114 ? 35.442 14.909  -40.989 1    85.36  ? 114 ASP   A OD2   1 1 
ATOM   663  N  N     . GLN   A 1 115 ? 35.459 10.261  -39.402 1    74.44  ? 115 GLN   A N     1 1 
ATOM   664  C  CA    . GLN   A 1 115 ? 36.363 9.397   -38.656 1    74.04  ? 115 GLN   A CA    1 1 
ATOM   665  C  C     . GLN   A 1 115 ? 37.338 10.17   -37.754 1    72.55  ? 115 GLN   A C     1 1 
ATOM   666  O  O     . GLN   A 1 115 ? 37.616 9.727   -36.638 1    73.1   ? 115 GLN   A O     1 1 
ATOM   667  C  CB    . GLN   A 1 115 ? 37.127 8.493   -39.631 1    76.54  ? 115 GLN   A CB    1 1 
ATOM   668  C  CG    . GLN   A 1 115 ? 37.458 7.132   -39.063 1    83.28  ? 115 GLN   A CG    1 1 
ATOM   669  C  CD    . GLN   A 1 115 ? 36.224 6.266   -38.88  1    91.09  ? 115 GLN   A CD    1 1 
ATOM   670  O  OE1   . GLN   A 1 115 ? 35.464 6.026   -39.829 1    94.71  ? 115 GLN   A OE1   1 1 
ATOM   671  N  NE2   . GLN   A 1 115 ? 36.007 5.764   -37.665 1    90.53  ? 115 GLN   A NE2   1 1 
ATOM   672  N  N     . ALA   A 1 116 ? 37.849 11.315  -38.225 1    70.58  ? 116 ALA   A N     1 1 
ATOM   673  C  CA    . ALA   A 1 116 ? 38.777 12.147  -37.45  1    69.34  ? 116 ALA   A CA    1 1 
ATOM   674  C  C     . ALA   A 1 116 ? 38.107 12.76   -36.211 1    67.91  ? 116 ALA   A C     1 1 
ATOM   675  O  O     . ALA   A 1 116 ? 38.759 12.906  -35.182 1    68.18  ? 116 ALA   A O     1 1 
ATOM   676  C  CB    . ALA   A 1 116 ? 39.363 13.243  -38.328 1    69.1   ? 116 ALA   A CB    1 1 
ATOM   677  N  N     . ASP   A 1 117 ? 36.812 13.114  -36.315 1    66.33  ? 117 ASP   A N     1 1 
ATOM   678  C  CA    . ASP   A 1 117 ? 36.018 13.662  -35.219 1    65.72  ? 117 ASP   A CA    1 1 
ATOM   679  C  C     . ASP   A 1 117 ? 35.776 12.55   -34.181 1    64.61  ? 117 ASP   A C     1 1 
ATOM   680  O  O     . ASP   A 1 117 ? 35.939 12.769  -32.977 1    64.34  ? 117 ASP   A O     1 1 
ATOM   681  C  CB    . ASP   A 1 117 ? 34.654 14.154  -35.741 1    67.91  ? 117 ASP   A CB    1 1 
ATOM   682  C  CG    . ASP   A 1 117 ? 34.65  15.485  -36.461 1    73.92  ? 117 ASP   A CG    1 1 
ATOM   683  O  OD1   . ASP   A 1 117 ? 35.713 16.145  -36.499 1    75.01  ? 117 ASP   A OD1   1 1 
ATOM   684  O  OD2   . ASP   A 1 117 ? 33.579 15.876  -36.978 1    76.56  ? 117 ASP   A OD2   1 1 
ATOM   685  N  N     . GLU   A 1 118 ? 35.406 11.346  -34.657 1    63.52  ? 118 GLU   A N     1 1 
ATOM   686  C  CA    . GLU   A 1 118 ? 35.128 10.216  -33.781 1    62.96  ? 118 GLU   A CA    1 1 
ATOM   687  C  C     . GLU   A 1 118 ? 36.387 9.79    -33.026 1    62.63  ? 118 GLU   A C     1 1 
ATOM   688  O  O     . GLU   A 1 118 ? 36.293 9.425   -31.855 1    62.75  ? 118 GLU   A O     1 1 
ATOM   689  C  CB    . GLU   A 1 118 ? 34.509 9.065   -34.588 1    64.76  ? 118 GLU   A CB    1 1 
ATOM   690  C  CG    . GLU   A 1 118 ? 33.904 7.935   -33.769 1    68.53  ? 118 GLU   A CG    1 1 
ATOM   691  C  CD    . GLU   A 1 118 ? 34.888 6.845   -33.409 1    74.56  ? 118 GLU   A CD    1 1 
ATOM   692  O  OE1   . GLU   A 1 118 ? 35.907 6.701   -34.122 1    75.98  ? 118 GLU   A OE1   1 1 
ATOM   693  O  OE2   . GLU   A 1 118 ? 34.657 6.151   -32.395 1    77.97  ? 118 GLU   A OE2   1 1 
ATOM   694  N  N     . ALA   A 1 119 ? 37.569 9.891   -33.666 1    62.26  ? 119 ALA   A N     1 1 
ATOM   695  C  CA    . ALA   A 1 119 ? 38.829 9.527   -33.021 1    62.13  ? 119 ALA   A CA    1 1 
ATOM   696  C  C     . ALA   A 1 119 ? 39.13  10.472  -31.867 1    62.7   ? 119 ALA   A C     1 1 
ATOM   697  O  O     . ALA   A 1 119 ? 39.558 10.021  -30.801 1    63.4   ? 119 ALA   A O     1 1 
ATOM   698  C  CB    . ALA   A 1 119 ? 39.966 9.539   -34.026 1    61.54  ? 119 ALA   A CB    1 1 
ATOM   699  N  N     . GLN   A 1 120 ? 38.857 11.772  -32.048 1    61.91  ? 120 GLN   A N     1 1 
ATOM   700  C  CA    . GLN   A 1 120 ? 39.087 12.742  -30.985 1    61.29  ? 120 GLN   A CA    1 1 
ATOM   701  C  C     . GLN   A 1 120 ? 38.071 12.603  -29.858 1    60.16  ? 120 GLN   A C     1 1 
ATOM   702  O  O     . GLN   A 1 120 ? 38.425 12.761  -28.696 1    60.19  ? 120 GLN   A O     1 1 
ATOM   703  C  CB    . GLN   A 1 120 ? 39.153 14.166  -31.538 1    62.8   ? 120 GLN   A CB    1 1 
ATOM   704  C  CG    . GLN   A 1 120 ? 40.307 14.373  -32.514 1    66.72  ? 120 GLN   A CG    1 1 
ATOM   705  C  CD    . GLN   A 1 120 ? 41.685 14.075  -31.945 1    72.97  ? 120 GLN   A CD    1 1 
ATOM   706  O  OE1   . GLN   A 1 120 ? 42.576 13.58   -32.65  1    75.07  ? 120 GLN   A OE1   1 1 
ATOM   707  N  NE2   . GLN   A 1 120 ? 41.921 14.381  -30.674 1    74.02  ? 120 GLN   A NE2   1 1 
ATOM   708  N  N     . TYR   A 1 121 ? 36.832 12.241  -30.185 1    59.14  ? 121 TYR   A N     1 1 
ATOM   709  C  CA    . TYR   A 1 121 ? 35.801 12.01   -29.179 1    58.67  ? 121 TYR   A CA    1 1 
ATOM   710  C  C     . TYR   A 1 121 ? 36.191 10.818  -28.285 1    58.2   ? 121 TYR   A C     1 1 
ATOM   711  O  O     . TYR   A 1 121 ? 35.923 10.848  -27.085 1    58.32  ? 121 TYR   A O     1 1 
ATOM   712  C  CB    . TYR   A 1 121 ? 34.445 11.775  -29.852 1    59     ? 121 TYR   A CB    1 1 
ATOM   713  C  CG    . TYR   A 1 121 ? 33.273 11.769  -28.89  1    59.98  ? 121 TYR   A CG    1 1 
ATOM   714  C  CD1   . TYR   A 1 121 ? 32.806 12.949  -28.324 1    60.88  ? 121 TYR   A CD1   1 1 
ATOM   715  C  CD2   . TYR   A 1 121 ? 32.615 10.59   -28.569 1    60.65  ? 121 TYR   A CD2   1 1 
ATOM   716  C  CE1   . TYR   A 1 121 ? 31.723 12.954  -27.455 1    61.69  ? 121 TYR   A CE1   1 1 
ATOM   717  C  CE2   . TYR   A 1 121 ? 31.529 10.583  -27.703 1    61.68  ? 121 TYR   A CE2   1 1 
ATOM   718  C  CZ    . TYR   A 1 121 ? 31.08  11.771  -27.155 1    62.93  ? 121 TYR   A CZ    1 1 
ATOM   719  O  OH    . TYR   A 1 121 ? 30.007 11.782  -26.294 1    65.21  ? 121 TYR   A OH    1 1 
ATOM   720  N  N     . CYS   A 1 122 ? 36.874 9.8     -28.853 1    57.27  ? 122 CYS   A N     1 1 
ATOM   721  C  CA    . CYS   A 1 122 ? 37.376 8.651   -28.107 1    56.72  ? 122 CYS   A CA    1 1 
ATOM   722  C  C     . CYS   A 1 122 ? 38.373 9.109   -27.031 1    55.47  ? 122 CYS   A C     1 1 
ATOM   723  O  O     . CYS   A 1 122 ? 38.335 8.601   -25.918 1    56.23  ? 122 CYS   A O     1 1 
ATOM   724  C  CB    . CYS   A 1 122 ? 38.001 7.622   -29.05  1    57.95  ? 122 CYS   A CB    1 1 
ATOM   725  S  SG    . CYS   A 1 122 ? 36.799 6.618   -29.97  1    61.94  ? 122 CYS   A SG    1 1 
ATOM   726  N  N     . GLN   A 1 123 ? 39.223 10.089  -27.34  1    54.05  ? 123 GLN   A N     1 1 
ATOM   727  C  CA    . GLN   A 1 123 ? 40.188 10.666  -26.399 1    53.34  ? 123 GLN   A CA    1 1 
ATOM   728  C  C     . GLN   A 1 123 ? 39.491 11.341  -25.211 1    52.04  ? 123 GLN   A C     1 1 
ATOM   729  O  O     . GLN   A 1 123 ? 39.96  11.235  -24.079 1    51.59  ? 123 GLN   A O     1 1 
ATOM   730  C  CB    . GLN   A 1 123 ? 41.1   11.675  -27.115 1    55.17  ? 123 GLN   A CB    1 1 
ATOM   731  C  CG    . GLN   A 1 123 ? 42.038 11.043  -28.149 1    60.5   ? 123 GLN   A CG    1 1 
ATOM   732  C  CD    . GLN   A 1 123 ? 43.052 10.117  -27.509 1    67.74  ? 123 GLN   A CD    1 1 
ATOM   733  O  OE1   . GLN   A 1 123 ? 42.76  8.973   -27.184 1    71.29  ? 123 GLN   A OE1   1 1 
ATOM   734  N  NE2   . GLN   A 1 123 ? 44.274 10.583  -27.306 1    68.92  ? 123 GLN   A NE2   1 1 
ATOM   735  N  N     . LEU   A 1 124 ? 38.381 12.037  -25.474 1    51.06  ? 124 LEU   A N     1 1 
ATOM   736  C  CA    . LEU   A 1 124 ? 37.592 12.681  -24.432 1    50.84  ? 124 LEU   A CA    1 1 
ATOM   737  C  C     . LEU   A 1 124 ? 36.969 11.59   -23.538 1    51.07  ? 124 LEU   A C     1 1 
ATOM   738  O  O     . LEU   A 1 124 ? 37.019 11.692  -22.308 1    51.58  ? 124 LEU   A O     1 1 
ATOM   739  C  CB    . LEU   A 1 124 ? 36.519 13.586  -25.065 1    50.52  ? 124 LEU   A CB    1 1 
ATOM   740  C  CG    . LEU   A 1 124 ? 35.371 14.058  -24.166 1    51.62  ? 124 LEU   A CG    1 1 
ATOM   741  C  CD1   . LEU   A 1 124 ? 35.879 14.853  -22.982 1    51.54  ? 124 LEU   A CD1   1 1 
ATOM   742  C  CD2   . LEU   A 1 124 ? 34.367 14.879  -24.964 1    52.17  ? 124 LEU   A CD2   1 1 
ATOM   743  N  N     . VAL   A 1 125 ? 36.428 10.537  -24.152 1    50.3   ? 125 VAL   A N     1 1 
ATOM   744  C  CA    . VAL   A 1 125 ? 35.842 9.432   -23.421 1    50.23  ? 125 VAL   A CA    1 1 
ATOM   745  C  C     . VAL   A 1 125 ? 36.884 8.733   -22.523 1    51.4   ? 125 VAL   A C     1 1 
ATOM   746  O  O     . VAL   A 1 125 ? 36.571 8.436   -21.368 1    51.89  ? 125 VAL   A O     1 1 
ATOM   747  C  CB    . VAL   A 1 125 ? 35.142 8.459   -24.381 1    50.07  ? 125 VAL   A CB    1 1 
ATOM   748  C  CG1   . VAL   A 1 125 ? 34.681 7.213   -23.647 1    50.61  ? 125 VAL   A CG1   1 1 
ATOM   749  C  CG2   . VAL   A 1 125 ? 33.967 9.132   -25.072 1    49.96  ? 125 VAL   A CG2   1 1 
ATOM   750  N  N     . ARG   A 1 126 ? 38.127 8.524   -23.019 1    51.41  ? 126 ARG   A N     1 1 
ATOM   751  C  CA    . ARG   A 1 126 ? 39.195 7.918   -22.215 1    52.46  ? 126 ARG   A CA    1 1 
ATOM   752  C  C     . ARG   A 1 126 ? 39.53  8.816   -21.023 1    52.32  ? 126 ARG   A C     1 1 
ATOM   753  O  O     . ARG   A 1 126 ? 39.66  8.327   -19.907 1    52.84  ? 126 ARG   A O     1 1 
ATOM   754  C  CB    . ARG   A 1 126 ? 40.477 7.685   -23.05  1    55.46  ? 126 ARG   A CB    1 1 
ATOM   755  C  CG    . ARG   A 1 126 ? 40.299 6.702   -24.186 1    62.25  ? 126 ARG   A CG    1 1 
ATOM   756  C  CD    . ARG   A 1 126 ? 41.524 6.593   -25.094 1    67.87  ? 126 ARG   A CD    1 1 
ATOM   757  N  NE    . ARG   A 1 126 ? 41.357 5.517   -26.079 1    73.09  ? 126 ARG   A NE    1 1 
ATOM   758  C  CZ    . ARG   A 1 126 ? 41.254 5.711   -27.394 1    76.79  ? 126 ARG   A CZ    1 1 
ATOM   759  N  NH1   . ARG   A 1 126 ? 41.328 6.936   -27.899 1    76.9   ? 126 ARG   A NH1   1 1 
ATOM   760  N  NH2   . ARG   A 1 126 ? 41.099 4.68    -28.214 1    77.26  ? 126 ARG   A NH2   1 1 
ATOM   761  N  N     . GLN   A 1 127 ? 39.66  10.132  -21.264 1    51.34  ? 127 GLN   A N     1 1 
ATOM   762  C  CA    . GLN   A 1 127 ? 39.965 11.101  -20.227 1    50.82  ? 127 GLN   A CA    1 1 
ATOM   763  C  C     . GLN   A 1 127 ? 38.871 11.091  -19.14  1    50.86  ? 127 GLN   A C     1 1 
ATOM   764  O  O     . GLN   A 1 127 ? 39.199 11.028  -17.961 1    51.58  ? 127 GLN   A O     1 1 
ATOM   765  C  CB    . GLN   A 1 127 ? 40.12  12.489  -20.844 1    51.9   ? 127 GLN   A CB    1 1 
ATOM   766  C  CG    . GLN   A 1 127 ? 40.587 13.542  -19.869 1    55.76  ? 127 GLN   A CG    1 1 
ATOM   767  C  CD    . GLN   A 1 127 ? 40.476 14.942  -20.428 1    61.09  ? 127 GLN   A CD    1 1 
ATOM   768  O  OE1   . GLN   A 1 127 ? 39.375 15.492  -20.622 1    61.98  ? 127 GLN   A OE1   1 1 
ATOM   769  N  NE2   . GLN   A 1 127 ? 41.618 15.566  -20.677 1    62.42  ? 127 GLN   A NE2   1 1 
ATOM   770  N  N     . LEU   A 1 128 ? 37.591 11.087  -19.523 1    50.02  ? 128 LEU   A N     1 1 
ATOM   771  C  CA    . LEU   A 1 128 ? 36.497 11.063  -18.548 1    49.88  ? 128 LEU   A CA    1 1 
ATOM   772  C  C     . LEU   A 1 128 ? 36.464 9.765   -17.753 1    50.34  ? 128 LEU   A C     1 1 
ATOM   773  O  O     . LEU   A 1 128 ? 36.229 9.786   -16.549 1    50.46  ? 128 LEU   A O     1 1 
ATOM   774  C  CB    . LEU   A 1 128 ? 35.154 11.308  -19.235 1    49.41  ? 128 LEU   A CB    1 1 
ATOM   775  C  CG    . LEU   A 1 128 ? 34.997 12.697  -19.862 1    49.8   ? 128 LEU   A CG    1 1 
ATOM   776  C  CD1   . LEU   A 1 128 ? 33.64  12.844  -20.508 1    49.34  ? 128 LEU   A CD1   1 1 
ATOM   777  C  CD2   . LEU   A 1 128 ? 35.243 13.825  -18.825 1    50.24  ? 128 LEU   A CD2   1 1 
ATOM   778  N  N     . LEU   A 1 129 ? 36.75  8.631   -18.41  1    50.16  ? 129 LEU   A N     1 1 
ATOM   779  C  CA    . LEU   A 1 129 ? 36.788 7.339   -17.734 1    50.43  ? 129 LEU   A CA    1 1 
ATOM   780  C  C     . LEU   A 1 129 ? 37.884 7.353   -16.661 1    51.76  ? 129 LEU   A C     1 1 
ATOM   781  O  O     . LEU   A 1 129 ? 37.663 6.877   -15.549 1    52.13  ? 129 LEU   A O     1 1 
ATOM   782  C  CB    . LEU   A 1 129 ? 37.077 6.21    -18.747 1    49.87  ? 129 LEU   A CB    1 1 
ATOM   783  C  CG    . LEU   A 1 129 ? 35.895 5.674   -19.536 1    50.5   ? 129 LEU   A CG    1 1 
ATOM   784  C  CD1   . LEU   A 1 129 ? 36.365 4.712   -20.625 1    50.29  ? 129 LEU   A CD1   1 1 
ATOM   785  C  CD2   . LEU   A 1 129 ? 34.916 4.942   -18.619 1    50.93  ? 129 LEU   A CD2   1 1 
ATOM   786  N  N     . ASP   A 1 130 ? 39.038 7.943   -16.985 1    52.41  ? 130 ASP   A N     1 1 
ATOM   787  C  CA    . ASP   A 1 130 ? 40.178 8.039   -16.082 1    54.23  ? 130 ASP   A CA    1 1 
ATOM   788  C  C     . ASP   A 1 130 ? 39.974 9.077   -14.959 1    54.69  ? 130 ASP   A C     1 1 
ATOM   789  O  O     . ASP   A 1 130 ? 40.297 8.798   -13.806 1    55.12  ? 130 ASP   A O     1 1 
ATOM   790  C  CB    . ASP   A 1 130 ? 41.445 8.356   -16.881 1    57.89  ? 130 ASP   A CB    1 1 
ATOM   791  C  CG    . ASP   A 1 130 ? 42.699 8.364   -16.03  1    67.59  ? 130 ASP   A CG    1 1 
ATOM   792  O  OD1   . ASP   A 1 130 ? 43.043 7.294   -15.473 1    69.42  ? 130 ASP   A OD1   1 1 
ATOM   793  O  OD2   . ASP   A 1 130 ? 43.339 9.446   -15.914 1    71.29  ? 130 ASP   A OD2   1 1 
ATOM   794  N  N     . ASP   A 1 131 ? 39.46  10.27   -15.289 1    53.75  ? 131 ASP   A N     1 1 
ATOM   795  C  CA    . ASP   A 1 131 ? 39.228 11.319  -14.293 1    53.23  ? 131 ASP   A CA    1 1 
ATOM   796  C  C     . ASP   A 1 131 ? 38.221 10.921  -13.23  1    52.84  ? 131 ASP   A C     1 1 
ATOM   797  O  O     . ASP   A 1 131 ? 38.279 11.45   -12.119 1    53.46  ? 131 ASP   A O     1 1 
ATOM   798  C  CB    . ASP   A 1 131 ? 38.741 12.616  -14.963 1    54.15  ? 131 ASP   A CB    1 1 
ATOM   799  C  CG    . ASP   A 1 131 ? 39.798 13.359  -15.758 1    58.85  ? 131 ASP   A CG    1 1 
ATOM   800  O  OD1   . ASP   A 1 131 ? 40.967 12.918  -15.749 1    59.42  ? 131 ASP   A OD1   1 1 
ATOM   801  O  OD2   . ASP   A 1 131 ? 39.451 14.382  -16.398 1    61.59  ? 131 ASP   A OD2   1 1 
ATOM   802  N  N     . HIS   A 1 132 ? 37.276 10.035  -13.564 1    51.76  ? 132 HIS   A N     1 1 
ATOM   803  C  CA    . HIS   A 1 132 ? 36.245 9.64    -12.612 1    51.86  ? 132 HIS   A CA    1 1 
ATOM   804  C  C     . HIS   A 1 132 ? 36.378 8.198   -12.074 1    51.66  ? 132 HIS   A C     1 1 
ATOM   805  O  O     . HIS   A 1 132 ? 35.412 7.668   -11.53  1    51.39  ? 132 HIS   A O     1 1 
ATOM   806  C  CB    . HIS   A 1 132 ? 34.857 9.865   -13.229 1    52.69  ? 132 HIS   A CB    1 1 
ATOM   807  C  CG    . HIS   A 1 132 ? 34.652 11.26   -13.711 1    56.25  ? 132 HIS   A CG    1 1 
ATOM   808  N  ND1   . HIS   A 1 132 ? 34.963 11.623  -14.997 1    58.15  ? 132 HIS   A ND1   1 1 
ATOM   809  C  CD2   . HIS   A 1 132 ? 34.266 12.362  -13.033 1    57.83  ? 132 HIS   A CD2   1 1 
ATOM   810  C  CE1   . HIS   A 1 132 ? 34.722 12.916  -15.079 1    58.46  ? 132 HIS   A CE1   1 1 
ATOM   811  N  NE2   . HIS   A 1 132 ? 34.296 13.404  -13.927 1    58.54  ? 132 HIS   A NE2   1 1 
ATOM   812  N  N     . LYS   A 1 133 ? 37.56  7.569   -12.2   1    51.55  ? 133 LYS   A N     1 1 
ATOM   813  C  CA    . LYS   A 1 133 ? 37.727 6.186   -11.729 1    51.82  ? 133 LYS   A CA    1 1 
ATOM   814  C  C     . LYS   A 1 133 ? 37.538 6.017   -10.197 1    52.01  ? 133 LYS   A C     1 1 
ATOM   815  O  O     . LYS   A 1 133 ? 37.111 4.962   -9.76   1    51.38  ? 133 LYS   A O     1 1 
ATOM   816  C  CB    . LYS   A 1 133 ? 39.063 5.59    -12.203 1    53.1   ? 133 LYS   A CB    1 1 
ATOM   817  C  CG    . LYS   A 1 133 ? 40.296 6.341   -11.737 1    57.69  ? 133 LYS   A CG    1 1 
ATOM   818  C  CD    . LYS   A 1 133 ? 41.545 5.764   -12.418 1    64.42  ? 133 LYS   A CD    1 1 
ATOM   819  C  CE    . LYS   A 1 133 ? 42.781 6.63    -12.268 1    69.74  ? 133 LYS   A CE    1 1 
ATOM   820  N  NZ    . LYS   A 1 133 ? 43.07  6.955   -10.849 1    72.92  ? 133 LYS   A NZ    1 1 
ATOM   821  N  N     . ASP   A 1 134 ? 37.785 7.068   -9.403  1    52.89  ? 134 ASP   A N     1 1 
ATOM   822  C  CA    . ASP   A 1 134 ? 37.663 6.988   -7.946  1    53.96  ? 134 ASP   A CA    1 1 
ATOM   823  C  C     . ASP   A 1 134 ? 36.391 7.595   -7.372  1    53.74  ? 134 ASP   A C     1 1 
ATOM   824  O  O     . ASP   A 1 134 ? 36.324 7.797   -6.161  1    54.41  ? 134 ASP   A O     1 1 
ATOM   825  C  CB    . ASP   A 1 134 ? 38.899 7.621   -7.283  1    56.67  ? 134 ASP   A CB    1 1 
ATOM   826  C  CG    . ASP   A 1 134 ? 40.165 6.847   -7.615  1    65.22  ? 134 ASP   A CG    1 1 
ATOM   827  O  OD1   . ASP   A 1 134 ? 40.164 5.601   -7.448  1    66.76  ? 134 ASP   A OD1   1 1 
ATOM   828  O  OD2   . ASP   A 1 134 ? 41.151 7.48    -8.067  1    69.22  ? 134 ASP   A OD2   1 1 
ATOM   829  N  N     . VAL   A 1 135 ? 35.386 7.882   -8.214  1    52.54  ? 135 VAL   A N     1 1 
ATOM   830  C  CA    . VAL   A 1 135 ? 34.13  8.505   -7.786  1    51.7   ? 135 VAL   A CA    1 1 
ATOM   831  C  C     . VAL   A 1 135 ? 33.443 7.77    -6.618  1    51.17  ? 135 VAL   A C     1 1 
ATOM   832  O  O     . VAL   A 1 135 ? 32.947 8.449   -5.731  1    51.83  ? 135 VAL   A O     1 1 
ATOM   833  C  CB    . VAL   A 1 135 ? 33.161 8.731   -8.98   1    51.78  ? 135 VAL   A CB    1 1 
ATOM   834  C  CG1   . VAL   A 1 135 ? 31.727 8.985   -8.52   1    52.4   ? 135 VAL   A CG1   1 1 
ATOM   835  C  CG2   . VAL   A 1 135 ? 33.637 9.878   -9.833  1    51.81  ? 135 VAL   A CG2   1 1 
ATOM   836  N  N     . VAL   A 1 136 ? 33.411 6.436   -6.599  1    50.26  ? 136 VAL   A N     1 1 
ATOM   837  C  CA    . VAL   A 1 136 ? 32.741 5.703   -5.519  1    50.55  ? 136 VAL   A CA    1 1 
ATOM   838  C  C     . VAL   A 1 136 ? 33.393 5.972   -4.159  1    50.66  ? 136 VAL   A C     1 1 
ATOM   839  O  O     . VAL   A 1 136 ? 32.695 6.188   -3.176  1    50.48  ? 136 VAL   A O     1 1 
ATOM   840  C  CB    . VAL   A 1 136 ? 32.568 4.203   -5.802  1    51.42  ? 136 VAL   A CB    1 1 
ATOM   841  C  CG1   . VAL   A 1 136 ? 31.64  3.562   -4.768  1    52.14  ? 136 VAL   A CG1   1 1 
ATOM   842  C  CG2   . VAL   A 1 136 ? 32.022 3.987   -7.21   1    51.71  ? 136 VAL   A CG2   1 1 
ATOM   843  N  N     . THR   A 1 137 ? 34.718 6.046   -4.129  1    50.53  ? 137 THR   A N     1 1 
ATOM   844  C  CA    . THR   A 1 137 ? 35.457 6.36    -2.925  1    50.98  ? 137 THR   A CA    1 1 
ATOM   845  C  C     . THR   A 1 137 ? 35.148 7.778   -2.441  1    50.9   ? 137 THR   A C     1 1 
ATOM   846  O  O     . THR   A 1 137 ? 34.934 7.988   -1.248  1    51.4   ? 137 THR   A O     1 1 
ATOM   847  C  CB    . THR   A 1 137 ? 36.945 6.161   -3.193  1    52.52  ? 137 THR   A CB    1 1 
ATOM   848  O  OG1   . THR   A 1 137 ? 37.159 4.755   -3.267  1    55.04  ? 137 THR   A OG1   1 1 
ATOM   849  C  CG2   . THR   A 1 137 ? 37.827 6.782   -2.111  1    52.25  ? 137 THR   A CG2   1 1 
ATOM   850  N  N     . LEU   A 1 138 ? 35.141 8.749   -3.359  1    50.14  ? 138 LEU   A N     1 1 
ATOM   851  C  CA    . LEU   A 1 138 ? 34.832 10.126  -3.005  1    50.18  ? 138 LEU   A CA    1 1 
ATOM   852  C  C     . LEU   A 1 138 ? 33.397 10.231  -2.467  1    49.83  ? 138 LEU   A C     1 1 
ATOM   853  O  O     . LEU   A 1 138 ? 33.199 10.843  -1.424  1    50.39  ? 138 LEU   A O     1 1 
ATOM   854  C  CB    . LEU   A 1 138 ? 35.04  11.057  -4.206  1    50.41  ? 138 LEU   A CB    1 1 
ATOM   855  C  CG    . LEU   A 1 138 ? 36.477 11.148  -4.723  1    51.89  ? 138 LEU   A CG    1 1 
ATOM   856  C  CD1   . LEU   A 1 138 ? 36.516 11.751  -6.139  1    52.62  ? 138 LEU   A CD1   1 1 
ATOM   857  C  CD2   . LEU   A 1 138 ? 37.345 11.917  -3.764  1    51.85  ? 138 LEU   A CD2   1 1 
ATOM   858  N  N     . LEU   A 1 139 ? 32.419 9.578   -3.118  1    49.04  ? 139 LEU   A N     1 1 
ATOM   859  C  CA    . LEU   A 1 139 ? 31.039 9.618   -2.649  1    49.35  ? 139 LEU   A CA    1 1 
ATOM   860  C  C     . LEU   A 1 139 ? 30.9   8.96    -1.293  1    50.48  ? 139 LEU   A C     1 1 
ATOM   861  O  O     . LEU   A 1 139 ? 30.237 9.516   -0.407  1    51.64  ? 139 LEU   A O     1 1 
ATOM   862  C  CB    . LEU   A 1 139 ? 30.079 8.974   -3.639  1    49.35  ? 139 LEU   A CB    1 1 
ATOM   863  C  CG    . LEU   A 1 139 ? 29.865 9.734   -4.945  1    50.34  ? 139 LEU   A CG    1 1 
ATOM   864  C  CD1   . LEU   A 1 139 ? 28.998 8.921   -5.889  1    51.07  ? 139 LEU   A CD1   1 1 
ATOM   865  C  CD2   . LEU   A 1 139 ? 29.275 11.108  -4.697  1    49.84  ? 139 LEU   A CD2   1 1 
ATOM   866  N  N     . ALA   A 1 140 ? 31.57  7.824   -1.092  1    49.85  ? 140 ALA   A N     1 1 
ATOM   867  C  CA    . ALA   A 1 140 ? 31.515 7.121   0.185   1    50.11  ? 140 ALA   A CA    1 1 
ATOM   868  C  C     . ALA   A 1 140 ? 32.032 7.983   1.34    1    50.6   ? 140 ALA   A C     1 1 
ATOM   869  O  O     . ALA   A 1 140 ? 31.391 8.047   2.387   1    50.41  ? 140 ALA   A O     1 1 
ATOM   870  C  CB    . ALA   A 1 140 ? 32.299 5.815   0.107   1    50     ? 140 ALA   A CB    1 1 
ATOM   871  N  N     . GLU   A 1 141 ? 33.164 8.668   1.138   1    50.97  ? 141 GLU   A N     1 1 
ATOM   872  C  CA    . GLU   A 1 141 ? 33.742 9.49    2.183   1    52.45  ? 141 GLU   A CA    1 1 
ATOM   873  C  C     . GLU   A 1 141 ? 33.025 10.84   2.373   1    52.29  ? 141 GLU   A C     1 1 
ATOM   874  O  O     . GLU   A 1 141 ? 32.885 11.289  3.505   1    52.21  ? 141 GLU   A O     1 1 
ATOM   875  C  CB    . GLU   A 1 141 ? 35.253 9.648   1.972   1    56.68  ? 141 GLU   A CB    1 1 
ATOM   876  C  CG    . GLU   A 1 141 ? 35.95  8.29    2.057   1    65.96  ? 141 GLU   A CG    1 1 
ATOM   877  C  CD    . GLU   A 1 141 ? 35.616 7.457   3.291   1    76.68  ? 141 GLU   A CD    1 1 
ATOM   878  O  OE1   . GLU   A 1 141 ? 35.839 7.967   4.416   1    80     ? 141 GLU   A OE1   1 1 
ATOM   879  O  OE2   . GLU   A 1 141 ? 35.106 6.319   3.137   1    77.7   ? 141 GLU   A OE2   1 1 
ATOM   880  N  N     . GLY   A 1 142 ? 32.531 11.431  1.298   1    51.65  ? 142 GLY   A N     1 1 
ATOM   881  C  CA    . GLY   A 1 142 ? 31.767 12.67   1.402   1    51.87  ? 142 GLY   A CA    1 1 
ATOM   882  C  C     . GLY   A 1 142 ? 30.416 12.462  2.065   1    52.16  ? 142 GLY   A C     1 1 
ATOM   883  O  O     . GLY   A 1 142 ? 29.854 13.401  2.622   1    52.55  ? 142 GLY   A O     1 1 
ATOM   884  N  N     . LEU   A 1 143 ? 29.881 11.231  2.03    1    51.98  ? 143 LEU   A N     1 1 
ATOM   885  C  CA    . LEU   A 1 143 ? 28.587 10.937  2.634   1    52.54  ? 143 LEU   A CA    1 1 
ATOM   886  C  C     . LEU   A 1 143 ? 28.662 10.337  4.038   1    52.46  ? 143 LEU   A C     1 1 
ATOM   887  O  O     . LEU   A 1 143 ? 27.653 10.326  4.723   1    51.62  ? 143 LEU   A O     1 1 
ATOM   888  C  CB    . LEU   A 1 143 ? 27.811 9.972   1.731   1    52.66  ? 143 LEU   A CB    1 1 
ATOM   889  C  CG    . LEU   A 1 143 ? 27.117 10.628  0.562   1    54.22  ? 143 LEU   A CG    1 1 
ATOM   890  C  CD1   . LEU   A 1 143 ? 26.787 9.625   -0.49   1    54.28  ? 143 LEU   A CD1   1 1 
ATOM   891  C  CD2   . LEU   A 1 143 ? 25.878 11.296  1.014   1    55.12  ? 143 LEU   A CD2   1 1 
ATOM   892  N  N     . ARG   A 1 144 ? 29.815 9.8     4.439   1    52.99  ? 144 ARG   A N     1 1 
ATOM   893  C  CA    . ARG   A 1 144 ? 29.967 9.065   5.697   1    54.57  ? 144 ARG   A CA    1 1 
ATOM   894  C  C     . ARG   A 1 144 ? 29.55  9.82    6.98    1    55.68  ? 144 ARG   A C     1 1 
ATOM   895  O  O     . ARG   A 1 144 ? 28.792 9.262   7.784   1    55.63  ? 144 ARG   A O     1 1 
ATOM   896  C  CB    . ARG   A 1 144 ? 31.395 8.54    5.833   1    56.18  ? 144 ARG   A CB    1 1 
ATOM   897  C  CG    . ARG   A 1 144 ? 31.525 7.316   6.73    1    59.92  ? 144 ARG   A CG    1 1 
ATOM   898  C  CD    . ARG   A 1 144 ? 32.985 7.017   7.006   1    65.59  ? 144 ARG   A CD    1 1 
ATOM   899  N  NE    . ARG   A 1 144 ? 33.542 7.939   8.006   1    72.43  ? 144 ARG   A NE    1 1 
ATOM   900  C  CZ    . ARG   A 1 144 ? 34.33  8.977   7.726   1    75.06  ? 144 ARG   A CZ    1 1 
ATOM   901  N  NH1   . ARG   A 1 144 ? 34.68  9.233   6.469   1    74.44  ? 144 ARG   A NH1   1 1 
ATOM   902  N  NH2   . ARG   A 1 144 ? 34.777 9.76    8.7     1    74.46  ? 144 ARG   A NH2   1 1 
ATOM   903  N  N     . GLU   A 1 145 ? 30.039 11.055  7.188   1    56.09  ? 145 GLU   A N     1 1 
ATOM   904  C  CA    . GLU   A 1 145 ? 29.645 11.806  8.379   1    56.99  ? 145 GLU   A CA    1 1 
ATOM   905  C  C     . GLU   A 1 145 ? 28.41  12.652  8.142   1    56.93  ? 145 GLU   A C     1 1 
ATOM   906  O  O     . GLU   A 1 145 ? 27.51  12.642  8.988   1    57.01  ? 145 GLU   A O     1 1 
ATOM   907  C  CB    . GLU   A 1 145 ? 30.793 12.66   8.935   1    60.49  ? 145 GLU   A CB    1 1 
ATOM   908  C  CG    . GLU   A 1 145 ? 31.966 11.833  9.428   1    69.47  ? 145 GLU   A CG    1 1 
ATOM   909  C  CD    . GLU   A 1 145 ? 31.629 10.79   10.48   1    80.46  ? 145 GLU   A CD    1 1 
ATOM   910  O  OE1   . GLU   A 1 145 ? 30.847 11.109  11.409  1    81.96  ? 145 GLU   A OE1   1 1 
ATOM   911  O  OE2   . GLU   A 1 145 ? 32.147 9.651   10.371  1    83.91  ? 145 GLU   A OE2   1 1 
ATOM   912  N  N     . SER   A 1 146 ? 28.365 13.383  6.995   1    56.33  ? 146 SER   A N     1 1 
ATOM   913  C  CA    . SER   A 1 146 ? 27.268 14.285  6.639   1    56.38  ? 146 SER   A CA    1 1 
ATOM   914  C  C     . SER   A 1 146 ? 25.875 13.602  6.655   1    57.53  ? 146 SER   A C     1 1 
ATOM   915  O  O     . SER   A 1 146 ? 24.875 14.216  7.029   1    57.8   ? 146 SER   A O     1 1 
ATOM   916  C  CB    . SER   A 1 146 ? 27.545 14.965  5.305   1    55.85  ? 146 SER   A CB    1 1 
ATOM   917  O  OG    . SER   A 1 146 ? 27.582 14.023  4.251   1    56.42  ? 146 SER   A OG    1 1 
ATOM   918  N  N     . ARG   A 1 147 ? 25.856 12.324  6.307   1    57.92  ? 147 ARG   A N     1 1 
ATOM   919  C  CA    . ARG   A 1 147 ? 24.725 11.4    6.29    1    59.38  ? 147 ARG   A CA    1 1 
ATOM   920  C  C     . ARG   A 1 147 ? 23.98  11.384  7.638   1    60.48  ? 147 ARG   A C     1 1 
ATOM   921  O  O     . ARG   A 1 147 ? 22.783 11.127  7.679   1    60.19  ? 147 ARG   A O     1 1 
ATOM   922  C  CB    . ARG   A 1 147 ? 25.32  9.994   6.106   1    61.18  ? 147 ARG   A CB    1 1 
ATOM   923  C  CG    . ARG   A 1 147 ? 24.392 9.009   5.521   1    65.37  ? 147 ARG   A CG    1 1 
ATOM   924  C  CD    . ARG   A 1 147 ? 24.753 7.614   5.957   1    68.39  ? 147 ARG   A CD    1 1 
ATOM   925  N  NE    . ARG   A 1 147 ? 23.571 6.764   5.849   1    70.29  ? 147 ARG   A NE    1 1 
ATOM   926  C  CZ    . ARG   A 1 147 ? 23.412 5.804   4.951   1    71.8   ? 147 ARG   A CZ    1 1 
ATOM   927  N  NH1   . ARG   A 1 147 ? 24.396 5.504   4.109   1    70.51  ? 147 ARG   A NH1   1 1 
ATOM   928  N  NH2   . ARG   A 1 147 ? 22.285 5.103   4.915   1    71.89  ? 147 ARG   A NH2   1 1 
ATOM   929  N  N     . LYS   A 1 148 ? 24.716 11.57   8.742   1    61.48  ? 148 LYS   A N     1 1 
ATOM   930  C  CA    . LYS   A 1 148 ? 24.16  11.505  10.086  1    63.04  ? 148 LYS   A CA    1 1 
ATOM   931  C  C     . LYS   A 1 148 ? 23.383 12.748  10.504  1    64.15  ? 148 LYS   A C     1 1 
ATOM   932  O  O     . LYS   A 1 148 ? 22.681 12.7    11.501  1    64.77  ? 148 LYS   A O     1 1 
ATOM   933  C  CB    . LYS   A 1 148 ? 25.283 11.209  11.103  1    65.14  ? 148 LYS   A CB    1 1 
ATOM   934  C  CG    . LYS   A 1 148 ? 26.068 9.929   10.777  1    69.14  ? 148 LYS   A CG    1 1 
ATOM   935  C  CD    . LYS   A 1 148 ? 27.278 9.759   11.689  1    73.41  ? 148 LYS   A CD    1 1 
ATOM   936  C  CE    . LYS   A 1 148 ? 28.088 8.529   11.353  1    76.48  ? 148 LYS   A CE    1 1 
ATOM   937  N  NZ    . LYS   A 1 148 ? 29.343 8.457   12.15   1    78.48  ? 148 LYS   A NZ    1 1 
ATOM   938  N  N     . HIS   A 1 149 ? 23.5   13.853  9.767   1    64.5   ? 149 HIS   A N     1 1 
ATOM   939  C  CA    . HIS   A 1 149 ? 22.844 15.106  10.13   1    65.26  ? 149 HIS   A CA    1 1 
ATOM   940  C  C     . HIS   A 1 149 ? 21.534 15.387  9.397   1    64.88  ? 149 HIS   A C     1 1 
ATOM   941  O  O     . HIS   A 1 149 ? 21.038 16.507  9.459   1    65.25  ? 149 HIS   A O     1 1 
ATOM   942  C  CB    . HIS   A 1 149 ? 23.809 16.268  9.919   1    67.53  ? 149 HIS   A CB    1 1 
ATOM   943  C  CG    . HIS   A 1 149 ? 25.139 16.032  10.554  1    72.85  ? 149 HIS   A CG    1 1 
ATOM   944  N  ND1   . HIS   A 1 149 ? 25.256 15.798  11.917  1    75.77  ? 149 HIS   A ND1   1 1 
ATOM   945  C  CD2   . HIS   A 1 149 ? 26.363 15.941  9.985   1    74.54  ? 149 HIS   A CD2   1 1 
ATOM   946  C  CE1   . HIS   A 1 149 ? 26.546 15.6    12.136  1    76.57  ? 149 HIS   A CE1   1 1 
ATOM   947  N  NE2   . HIS   A 1 149 ? 27.252 15.678  11.003  1    76.23  ? 149 HIS   A NE2   1 1 
ATOM   948  N  N     . ILE   A 1 150 ? 20.976 14.395  8.707   1    64.14  ? 150 ILE   A N     1 1 
ATOM   949  C  CA    . ILE   A 1 150 ? 19.734 14.577  7.966   1    63.69  ? 150 ILE   A CA    1 1 
ATOM   950  C  C     . ILE   A 1 150 ? 18.559 13.87   8.644   1    64.49  ? 150 ILE   A C     1 1 
ATOM   951  O  O     . ILE   A 1 150 ? 18.761 12.959  9.451   1    64.79  ? 150 ILE   A O     1 1 
ATOM   952  C  CB    . ILE   A 1 150 ? 19.907 14.159  6.483   1    62.82  ? 150 ILE   A CB    1 1 
ATOM   953  C  CG1   . ILE   A 1 150 ? 20.116 12.637  6.34    1    62.78  ? 150 ILE   A CG1   1 1 
ATOM   954  C  CG2   . ILE   A 1 150 ? 21     14.97   5.797   1    62.44  ? 150 ILE   A CG2   1 1 
ATOM   955  C  CD1   . ILE   A 1 150 ? 20.063 12.15   4.924   1    63.61  ? 150 ILE   A CD1   1 1 
ATOM   956  N  N     . GLU   A 1 151 ? 17.334 14.276  8.307   1    64.59  ? 151 GLU   A N     1 1 
ATOM   957  C  CA    . GLU   A 1 151 ? 16.149 13.687  8.913   1    65.39  ? 151 GLU   A CA    1 1 
ATOM   958  C  C     . GLU   A 1 151 ? 15.751 12.326  8.317   1    65.98  ? 151 GLU   A C     1 1 
ATOM   959  O  O     . GLU   A 1 151 ? 15.267 11.472  9.052   1    66.48  ? 151 GLU   A O     1 1 
ATOM   960  C  CB    . GLU   A 1 151 ? 14.977 14.677  8.88    1    67.05  ? 151 GLU   A CB    1 1 
ATOM   961  C  CG    . GLU   A 1 151 ? 14.651 15.141  7.48    1    70.11  ? 151 GLU   A CG    1 1 
ATOM   962  C  CD    . GLU   A 1 151 ? 13.627 16.253  7.372   1    73.59  ? 151 GLU   A CD    1 1 
ATOM   963  O  OE1   . GLU   A 1 151 ? 13.105 16.702  8.42    1    72.69  ? 151 GLU   A OE1   1 1 
ATOM   964  O  OE2   . GLU   A 1 151 ? 13.35  16.677  6.228   1    75.19  ? 151 GLU   A OE2   1 1 
ATOM   965  N  N     . ASP   A 1 152 ? 15.955 12.109  7.011   1    65.67  ? 152 ASP   A N     1 1 
ATOM   966  C  CA    . ASP   A 1 152 ? 15.578 10.847  6.367   1    65.41  ? 152 ASP   A CA    1 1 
ATOM   967  C  C     . ASP   A 1 152 ? 16.771 10.273  5.621   1    64.98  ? 152 ASP   A C     1 1 
ATOM   968  O  O     . ASP   A 1 152 ? 17.028 10.663  4.487   1    64.7   ? 152 ASP   A O     1 1 
ATOM   969  C  CB    . ASP   A 1 152 ? 14.4   11.076  5.404   1    67.1   ? 152 ASP   A CB    1 1 
ATOM   970  C  CG    . ASP   A 1 152 ? 13.957 9.847   4.627   1    72.33  ? 152 ASP   A CG    1 1 
ATOM   971  O  OD1   . ASP   A 1 152 ? 14.256 8.715   5.077   1    72.87  ? 152 ASP   A OD1   1 1 
ATOM   972  O  OD2   . ASP   A 1 152 ? 13.312 10.016  3.569   1    74.86  ? 152 ASP   A OD2   1 1 
ATOM   973  N  N     . GLU   A 1 153 ? 17.48  9.317   6.246   1    65.01  ? 153 GLU   A N     1 1 
ATOM   974  C  CA    . GLU   A 1 153 ? 18.681 8.698   5.673   1    65.31  ? 153 GLU   A CA    1 1 
ATOM   975  C  C     . GLU   A 1 153 ? 18.41  7.88    4.416   1    64.44  ? 153 GLU   A C     1 1 
ATOM   976  O  O     . GLU   A 1 153 ? 19.334 7.659   3.637   1    64.17  ? 153 GLU   A O     1 1 
ATOM   977  C  CB    . GLU   A 1 153 ? 19.43  7.862   6.726   1    69.11  ? 153 GLU   A CB    1 1 
ATOM   978  C  CG    . GLU   A 1 153 ? 20.796 8.417   7.112   1    76.22  ? 153 GLU   A CG    1 1 
ATOM   979  C  CD    . GLU   A 1 153 ? 21.322 7.882   8.433   1    85.41  ? 153 GLU   A CD    1 1 
ATOM   980  O  OE1   . GLU   A 1 153 ? 20.699 8.172   9.482   1    88.26  ? 153 GLU   A OE1   1 1 
ATOM   981  O  OE2   . GLU   A 1 153 ? 22.353 7.171   8.42    1    87     ? 153 GLU   A OE2   1 1 
ATOM   982  N  N     . LYS   A 1 154 ? 17.136 7.457   4.194   1    63.66  ? 154 LYS   A N     1 1 
ATOM   983  C  CA    . LYS   A 1 154 ? 16.748 6.703   2.999   1    62.74  ? 154 LYS   A CA    1 1 
ATOM   984  C  C     . LYS   A 1 154 ? 16.968 7.496   1.712   1    60.43  ? 154 LYS   A C     1 1 
ATOM   985  O  O     . LYS   A 1 154 ? 17.098 6.879   0.657   1    60.49  ? 154 LYS   A O     1 1 
ATOM   986  C  CB    . LYS   A 1 154 ? 15.311 6.184   3.092   1    65.76  ? 154 LYS   A CB    1 1 
ATOM   987  C  CG    . LYS   A 1 154 ? 15.081 5.263   4.279   1    72.41  ? 154 LYS   A CG    1 1 
ATOM   988  C  CD    . LYS   A 1 154 ? 13.606 4.884   4.408   1    79.97  ? 154 LYS   A CD    1 1 
ATOM   989  C  CE    . LYS   A 1 154 ? 13.245 4.442   5.811   1    85.85  ? 154 LYS   A CE    1 1 
ATOM   990  N  NZ    . LYS   A 1 154 ? 13.287 5.573   6.787   1    89.18  ? 154 LYS   A NZ    1 1 
ATOM   991  N  N     . LEU   A 1 155 ? 17.071 8.849   1.783   1    58.16  ? 155 LEU   A N     1 1 
ATOM   992  C  CA    . LEU   A 1 155 ? 17.391 9.636   0.594   1    57.16  ? 155 LEU   A CA    1 1 
ATOM   993  C  C     . LEU   A 1 155 ? 18.799 9.244   0.081   1    55.84  ? 155 LEU   A C     1 1 
ATOM   994  O  O     . LEU   A 1 155 ? 19.018 9.222   -1.134  1    55.88  ? 155 LEU   A O     1 1 
ATOM   995  C  CB    . LEU   A 1 155 ? 17.373 11.152  0.866   1    57.33  ? 155 LEU   A CB    1 1 
ATOM   996  C  CG    . LEU   A 1 155 ? 16.046 11.78   1.279   1    59.09  ? 155 LEU   A CG    1 1 
ATOM   997  C  CD1   . LEU   A 1 155 ? 16.22  13.239  1.563   1    59.17  ? 155 LEU   A CD1   1 1 
ATOM   998  C  CD2   . LEU   A 1 155 ? 14.962 11.569  0.222   1    59.89  ? 155 LEU   A CD2   1 1 
ATOM   999  N  N     . VAL   A 1 156 ? 19.736 8.933   1.018   1    54.16  ? 156 VAL   A N     1 1 
ATOM   1000 C  CA    . VAL   A 1 156 ? 21.102 8.536   0.711   1    53.13  ? 156 VAL   A CA    1 1 
ATOM   1001 C  C     . VAL   A 1 156 ? 21.112 7.203   -0.029  1    52.53  ? 156 VAL   A C     1 1 
ATOM   1002 O  O     . VAL   A 1 156 ? 21.779 7.091   -1.053  1    52.64  ? 156 VAL   A O     1 1 
ATOM   1003 C  CB    . VAL   A 1 156 ? 21.985 8.532   1.977   1    53.5   ? 156 VAL   A CB    1 1 
ATOM   1004 C  CG1   . VAL   A 1 156 ? 23.405 8.044   1.667   1    53.91  ? 156 VAL   A CG1   1 1 
ATOM   1005 C  CG2   . VAL   A 1 156 ? 22.007 9.921   2.613   1    53.35  ? 156 VAL   A CG2   1 1 
ATOM   1006 N  N     . ARG   A 1 157 ? 20.294 6.227   0.408   1    51.95  ? 157 ARG   A N     1 1 
ATOM   1007 C  CA    . ARG   A 1 157 ? 20.2   4.954   -0.305  1    52.04  ? 157 ARG   A CA    1 1 
ATOM   1008 C  C     . ARG   A 1 157 ? 19.715 5.167   -1.758  1    51.88  ? 157 ARG   A C     1 1 
ATOM   1009 O  O     . ARG   A 1 157 ? 20.336 4.635   -2.671  1    51.43  ? 157 ARG   A O     1 1 
ATOM   1010 C  CB    . ARG   A 1 157 ? 19.293 3.954   0.429   1    53.16  ? 157 ARG   A CB    1 1 
ATOM   1011 C  CG    . ARG   A 1 157 ? 19.027 2.686   -0.365  1    56.77  ? 157 ARG   A CG    1 1 
ATOM   1012 C  CD    . ARG   A 1 157 ? 20.016 1.583   -0.044  1    63.19  ? 157 ARG   A CD    1 1 
ATOM   1013 N  NE    . ARG   A 1 157 ? 19.303 0.421   0.495   1    69.65  ? 157 ARG   A NE    1 1 
ATOM   1014 C  CZ    . ARG   A 1 157 ? 19.192 0.144   1.79    1    74.33  ? 157 ARG   A CZ    1 1 
ATOM   1015 N  NH1   . ARG   A 1 157 ? 19.791 0.908   2.694   1    76.14  ? 157 ARG   A NH1   1 1 
ATOM   1016 N  NH2   . ARG   A 1 157 ? 18.5   -0.91   2.191   1    74.79  ? 157 ARG   A NH2   1 1 
ATOM   1017 N  N     . TYR   A 1 158 ? 18.645 5.955   -1.959  1    52.17  ? 158 TYR   A N     1 1 
ATOM   1018 C  CA    . TYR   A 1 158 ? 18.104 6.23    -3.284  1    53.98  ? 158 TYR   A CA    1 1 
ATOM   1019 C  C     . TYR   A 1 158 ? 19.134 6.921   -4.15   1    51.23  ? 158 TYR   A C     1 1 
ATOM   1020 O  O     . TYR   A 1 158 ? 19.27  6.568   -5.317  1    50.95  ? 158 TYR   A O     1 1 
ATOM   1021 C  CB    . TYR   A 1 158 ? 16.816 7.094   -3.219  1    57.68  ? 158 TYR   A CB    1 1 
ATOM   1022 C  CG    . TYR   A 1 158 ? 16.248 7.426   -4.59   1    63.5   ? 158 TYR   A CG    1 1 
ATOM   1023 C  CD1   . TYR   A 1 158 ? 15.412 6.532   -5.254  1    66.77  ? 158 TYR   A CD1   1 1 
ATOM   1024 C  CD2   . TYR   A 1 158 ? 16.606 8.599   -5.255  1    66.25  ? 158 TYR   A CD2   1 1 
ATOM   1025 C  CE1   . TYR   A 1 158 ? 14.938 6.798   -6.538  1    68.75  ? 158 TYR   A CE1   1 1 
ATOM   1026 C  CE2   . TYR   A 1 158 ? 16.16  8.863   -6.55   1    68.42  ? 158 TYR   A CE2   1 1 
ATOM   1027 C  CZ    . TYR   A 1 158 ? 15.312 7.964   -7.182  1    70.61  ? 158 TYR   A CZ    1 1 
ATOM   1028 O  OH    . TYR   A 1 158 ? 14.812 8.214   -8.444  1    74.2   ? 158 TYR   A OH    1 1 
ATOM   1029 N  N     . PHE   A 1 159 ? 19.834 7.93    -3.59   1    48.95  ? 159 PHE   A N     1 1 
ATOM   1030 C  CA    . PHE   A 1 159 ? 20.833 8.69    -4.324  1    46.97  ? 159 PHE   A CA    1 1 
ATOM   1031 C  C     . PHE   A 1 159 ? 21.993 7.792   -4.761  1    45.89  ? 159 PHE   A C     1 1 
ATOM   1032 O  O     . PHE   A 1 159 ? 22.4   7.855   -5.917  1    45.98  ? 159 PHE   A O     1 1 
ATOM   1033 C  CB    . PHE   A 1 159 ? 21.348 9.901   -3.498  1    45.74  ? 159 PHE   A CB    1 1 
ATOM   1034 C  CG    . PHE   A 1 159 ? 22.528 10.624  -4.125  1    45.25  ? 159 PHE   A CG    1 1 
ATOM   1035 C  CD1   . PHE   A 1 159 ? 22.334 11.581  -5.105  1    45.85  ? 159 PHE   A CD1   1 1 
ATOM   1036 C  CD2   . PHE   A 1 159 ? 23.826 10.332  -3.742  1    45.45  ? 159 PHE   A CD2   1 1 
ATOM   1037 C  CE1   . PHE   A 1 159 ? 23.417 12.229  -5.689  1    46.44  ? 159 PHE   A CE1   1 1 
ATOM   1038 C  CE2   . PHE   A 1 159 ? 24.904 10.979  -4.326  1    46.05  ? 159 PHE   A CE2   1 1 
ATOM   1039 C  CZ    . PHE   A 1 159 ? 24.696 11.919  -5.301  1    45.94  ? 159 PHE   A CZ    1 1 
ATOM   1040 N  N     . LEU   A 1 160 ? 22.556 7.01    -3.833  1    44.38  ? 160 LEU   A N     1 1 
ATOM   1041 C  CA    . LEU   A 1 160 ? 23.692 6.158   -4.156  1    43.88  ? 160 LEU   A CA    1 1 
ATOM   1042 C  C     . LEU   A 1 160 ? 23.267 5.082   -5.17   1    43.96  ? 160 LEU   A C     1 1 
ATOM   1043 O  O     . LEU   A 1 160 ? 23.932 4.935   -6.187  1    44.13  ? 160 LEU   A O     1 1 
ATOM   1044 C  CB    . LEU   A 1 160 ? 24.315 5.575   -2.889  1    43.67  ? 160 LEU   A CB    1 1 
ATOM   1045 C  CG    . LEU   A 1 160 ? 25.153 6.572   -2.091  1    45.27  ? 160 LEU   A CG    1 1 
ATOM   1046 C  CD1   . LEU   A 1 160 ? 25.577 5.999   -0.755  1    45.63  ? 160 LEU   A CD1   1 1 
ATOM   1047 C  CD2   . LEU   A 1 160 ? 26.388 7.009   -2.882  1    45.27  ? 160 LEU   A CD2   1 1 
ATOM   1048 N  N     . ASP   A 1 161 ? 22.094 4.459   -4.984  1    43.09  ? 161 ASP   A N     1 1 
ATOM   1049 C  CA    . ASP   A 1 161 ? 21.601 3.468   -5.943  1    43.57  ? 161 ASP   A CA    1 1 
ATOM   1050 C  C     . ASP   A 1 161 ? 21.453 4.064   -7.352  1    44.21  ? 161 ASP   A C     1 1 
ATOM   1051 O  O     . ASP   A 1 161 ? 21.943 3.478   -8.311  1    44.86  ? 161 ASP   A O     1 1 
ATOM   1052 C  CB    . ASP   A 1 161 ? 20.263 2.857   -5.482  1    44.41  ? 161 ASP   A CB    1 1 
ATOM   1053 C  CG    . ASP   A 1 161 ? 20.368 1.855   -4.36   1    47.96  ? 161 ASP   A CG    1 1 
ATOM   1054 O  OD1   . ASP   A 1 161 ? 21.499 1.41    -4.061  1    48.26  ? 161 ASP   A OD1   1 1 
ATOM   1055 O  OD2   . ASP   A 1 161 ? 19.332 1.514   -3.786  1    50.14  ? 161 ASP   A OD2   1 1 
ATOM   1056 N  N     . LYS   A 1 162 ? 20.784 5.214   -7.475  1    43.99  ? 162 LYS   A N     1 1 
ATOM   1057 C  CA    . LYS   A 1 162 ? 20.609 5.879   -8.761  1    44.84  ? 162 LYS   A CA    1 1 
ATOM   1058 C  C     . LYS   A 1 162 ? 21.944 6.327   -9.398  1    44.12  ? 162 LYS   A C     1 1 
ATOM   1059 O  O     . LYS   A 1 162 ? 22.175 6.052   -10.572 1    45.26  ? 162 LYS   A O     1 1 
ATOM   1060 C  CB    . LYS   A 1 162 ? 19.655 7.083   -8.626  1    48.65  ? 162 LYS   A CB    1 1 
ATOM   1061 C  CG    . LYS   A 1 162 ? 18.276 6.84    -9.208  1    56.71  ? 162 LYS   A CG    1 1 
ATOM   1062 C  CD    . LYS   A 1 162 ? 18.341 6.657   -10.74  1    63.81  ? 162 LYS   A CD    1 1 
ATOM   1063 C  CE    . LYS   A 1 162 ? 16.975 6.728   -11.387 1    69.59  ? 162 LYS   A CE    1 1 
ATOM   1064 N  NZ    . LYS   A 1 162 ? 16.799 5.694   -12.45  1    72.66  ? 162 LYS   A NZ    1 1 
ATOM   1065 N  N     . THR   A 1 163 ? 22.818 6.998   -8.635  1    42.21  ? 163 THR   A N     1 1 
ATOM   1066 C  CA    . THR   A 1 163 ? 24.098 7.508   -9.123  1    41.15  ? 163 THR   A CA    1 1 
ATOM   1067 C  C     . THR   A 1 163 ? 25.074 6.399   -9.526  1    41.2   ? 163 THR   A C     1 1 
ATOM   1068 O  O     . THR   A 1 163 ? 25.667 6.487   -10.604 1    41.4   ? 163 THR   A O     1 1 
ATOM   1069 C  CB    . THR   A 1 163 ? 24.745 8.421   -8.056  1    41.53  ? 163 THR   A CB    1 1 
ATOM   1070 O  OG1   . THR   A 1 163 ? 23.82  9.435   -7.68   1    42.87  ? 163 THR   A OG1   1 1 
ATOM   1071 C  CG2   . THR   A 1 163 ? 26.057 9.023   -8.502  1    40.51  ? 163 THR   A CG2   1 1 
ATOM   1072 N  N     . LEU   A 1 164 ? 25.269 5.379   -8.668  1    40.81  ? 164 LEU   A N     1 1 
ATOM   1073 C  CA    . LEU   A 1 164 ? 26.214 4.293   -8.938  1    41.8   ? 164 LEU   A CA    1 1 
ATOM   1074 C  C     . LEU   A 1 164 ? 25.791 3.393   -10.11  1    42.53  ? 164 LEU   A C     1 1 
ATOM   1075 O  O     . LEU   A 1 164 ? 26.646 3.011   -10.906 1    43.91  ? 164 LEU   A O     1 1 
ATOM   1076 C  CB    . LEU   A 1 164 ? 26.521 3.472   -7.663  1    42.55  ? 164 LEU   A CB    1 1 
ATOM   1077 C  CG    . LEU   A 1 164 ? 27.13  4.301   -6.484  1    44.75  ? 164 LEU   A CG    1 1 
ATOM   1078 C  CD1   . LEU   A 1 164 ? 27.398 3.439   -5.277  1    45.56  ? 164 LEU   A CD1   1 1 
ATOM   1079 C  CD2   . LEU   A 1 164 ? 28.414 4.978   -6.885  1    45.42  ? 164 LEU   A CD2   1 1 
ATOM   1080 N  N     . THR   A 1 165 ? 24.5   3.086   -10.248 1    41.74  ? 165 THR   A N     1 1 
ATOM   1081 C  CA    . THR   A 1 165 ? 24.015 2.278   -11.366 1    41.69  ? 165 THR   A CA    1 1 
ATOM   1082 C  C     . THR   A 1 165 ? 24.048 3.054   -12.68  1    41.99  ? 165 THR   A C     1 1 
ATOM   1083 O  O     . THR   A 1 165 ? 24.438 2.476   -13.697 1    41.78  ? 165 THR   A O     1 1 
ATOM   1084 C  CB    . THR   A 1 165 ? 22.635 1.699   -11.084 1    42.16  ? 165 THR   A CB    1 1 
ATOM   1085 O  OG1   . THR   A 1 165 ? 21.696 2.766   -10.957 1    42.27  ? 165 THR   A OG1   1 1 
ATOM   1086 C  CG2   . THR   A 1 165 ? 22.631 0.792   -9.85   1    42.62  ? 165 THR   A CG2   1 1 
ATOM   1087 N  N     . SER   A 1 166 ? 23.704 4.376   -12.667 1    42.15  ? 166 SER   A N     1 1 
ATOM   1088 C  CA    . SER   A 1 166 ? 23.823 5.205   -13.876 1    43.02  ? 166 SER   A CA    1 1 
ATOM   1089 C  C     . SER   A 1 166 ? 25.295 5.293   -14.256 1    43.23  ? 166 SER   A C     1 1 
ATOM   1090 O  O     . SER   A 1 166 ? 25.607 5.174   -15.43  1    44.07  ? 166 SER   A O     1 1 
ATOM   1091 C  CB    . SER   A 1 166 ? 23.306 6.62    -13.645 1    44.89  ? 166 SER   A CB    1 1 
ATOM   1092 O  OG    . SER   A 1 166 ? 21.924 6.585   -13.346 1    49.15  ? 166 SER   A OG    1 1 
ATOM   1093 N  N     . ARG   A 1 167 ? 26.2   5.441   -13.258 1    42.3   ? 167 ARG   A N     1 1 
ATOM   1094 C  CA    . ARG   A 1 167 ? 27.634 5.474   -13.492 1    41.98  ? 167 ARG   A CA    1 1 
ATOM   1095 C  C     . ARG   A 1 167 ? 28.105 4.161   -14.139 1    42.53  ? 167 ARG   A C     1 1 
ATOM   1096 O  O     . ARG   A 1 167 ? 28.908 4.212   -15.079 1    42.88  ? 167 ARG   A O     1 1 
ATOM   1097 C  CB    . ARG   A 1 167 ? 28.397 5.753   -12.196 1    41.52  ? 167 ARG   A CB    1 1 
ATOM   1098 C  CG    . ARG   A 1 167 ? 29.901 5.746   -12.381 1    42.47  ? 167 ARG   A CG    1 1 
ATOM   1099 C  CD    . ARG   A 1 167 ? 30.607 6.14    -11.109 1    43.68  ? 167 ARG   A CD    1 1 
ATOM   1100 N  NE    . ARG   A 1 167 ? 32.064 6.055   -11.242 1    44.78  ? 167 ARG   A NE    1 1 
ATOM   1101 C  CZ    . ARG   A 1 167 ? 32.775 4.952   -11.033 1    44.42  ? 167 ARG   A CZ    1 1 
ATOM   1102 N  NH1   . ARG   A 1 167 ? 32.174 3.821   -10.682 1    42.73  ? 167 ARG   A NH1   1 1 
ATOM   1103 N  NH2   . ARG   A 1 167 ? 34.096 4.981   -11.135 1    44.04  ? 167 ARG   A NH2   1 1 
ATOM   1104 N  N     . LEU   A 1 168 ? 27.586 2.997   -13.678 1    42.36  ? 168 LEU   A N     1 1 
ATOM   1105 C  CA    . LEU   A 1 168 ? 27.948 1.691   -14.263 1    42.21  ? 168 LEU   A CA    1 1 
ATOM   1106 C  C     . LEU   A 1 168 ? 27.503 1.643   -15.729 1    43.07  ? 168 LEU   A C     1 1 
ATOM   1107 O  O     . LEU   A 1 168 ? 28.294 1.271   -16.583 1    43.36  ? 168 LEU   A O     1 1 
ATOM   1108 C  CB    . LEU   A 1 168 ? 27.326 0.505   -13.484 1    41.6   ? 168 LEU   A CB    1 1 
ATOM   1109 C  CG    . LEU   A 1 168 ? 27.608 -0.89   -14.091 1    42.2   ? 168 LEU   A CG    1 1 
ATOM   1110 C  CD1   . LEU   A 1 168 ? 29.091 -1.245  -13.992 1    42.56  ? 168 LEU   A CD1   1 1 
ATOM   1111 C  CD2   . LEU   A 1 168 ? 26.742 -1.983  -13.459 1    41.87  ? 168 LEU   A CD2   1 1 
ATOM   1112 N  N     . GLY   A 1 169 ? 26.256 2.043   -16.005 1    43.51  ? 169 GLY   A N     1 1 
ATOM   1113 C  CA    . GLY   A 1 169 ? 25.691 2.064   -17.348 1    43.98  ? 169 GLY   A CA    1 1 
ATOM   1114 C  C     . GLY   A 1 169 ? 26.457 2.977   -18.286 1    45.17  ? 169 GLY   A C     1 1 
ATOM   1115 O  O     . GLY   A 1 169 ? 26.735 2.609   -19.432 1    45.86  ? 169 GLY   A O     1 1 
ATOM   1116 N  N     . ILE   A 1 170 ? 26.856 4.15    -17.787 1    45.06  ? 170 ILE   A N     1 1 
ATOM   1117 C  CA    . ILE   A 1 170 ? 27.628 5.12    -18.551 1    45.77  ? 170 ILE   A CA    1 1 
ATOM   1118 C  C     . ILE   A 1 170 ? 29.02  4.546   -18.85  1    46.73  ? 170 ILE   A C     1 1 
ATOM   1119 O  O     . ILE   A 1 170 ? 29.479 4.625   -19.993 1    47.62  ? 170 ILE   A O     1 1 
ATOM   1120 C  CB    . ILE   A 1 170 ? 27.689 6.482   -17.796 1    45.72  ? 170 ILE   A CB    1 1 
ATOM   1121 C  CG1   . ILE   A 1 170 ? 26.372 7.268   -17.968 1    46.24  ? 170 ILE   A CG1   1 1 
ATOM   1122 C  CG2   . ILE   A 1 170 ? 28.885 7.327   -18.235 1    45.37  ? 170 ILE   A CG2   1 1 
ATOM   1123 C  CD1   . ILE   A 1 170 ? 26.228 8.386   -17.024 1    47.35  ? 170 ILE   A CD1   1 1 
ATOM   1124 N  N     . ARG   A 1 171 ? 29.684 3.968   -17.836 1    46.19  ? 171 ARG   A N     1 1 
ATOM   1125 C  CA    . ARG   A 1 171 ? 31.012 3.402   -18.042 1    46.63  ? 171 ARG   A CA    1 1 
ATOM   1126 C  C     . ARG   A 1 171 ? 30.968 2.215   -19.016 1    48.57  ? 171 ARG   A C     1 1 
ATOM   1127 O  O     . ARG   A 1 171 ? 31.892 2.06    -19.803 1    50.04  ? 171 ARG   A O     1 1 
ATOM   1128 C  CB    . ARG   A 1 171 ? 31.695 3.059   -16.705 1    46.02  ? 171 ARG   A CB    1 1 
ATOM   1129 C  CG    . ARG   A 1 171 ? 32.038 4.285   -15.883 1    45.84  ? 171 ARG   A CG    1 1 
ATOM   1130 C  CD    . ARG   A 1 171 ? 32.807 3.978   -14.608 1    46.72  ? 171 ARG   A CD    1 1 
ATOM   1131 N  NE    . ARG   A 1 171 ? 34.172 3.555   -14.893 1    47.49  ? 171 ARG   A NE    1 1 
ATOM   1132 C  CZ    . ARG   A 1 171 ? 35.223 4.368   -14.954 1    48.16  ? 171 ARG   A CZ    1 1 
ATOM   1133 N  NH1   . ARG   A 1 171 ? 35.08  5.671   -14.723 1    45.89  ? 171 ARG   A NH1   1 1 
ATOM   1134 N  NH2   . ARG   A 1 171 ? 36.423 3.888   -15.251 1    47.32  ? 171 ARG   A NH2   1 1 
ATOM   1135 N  N     . MET   A 1 172 ? 29.881 1.429   -19.017 1    48.62  ? 172 MET   A N     1 1 
ATOM   1136 C  CA    . MET   A 1 172 ? 29.698 0.313   -19.949 1    49.29  ? 172 MET   A CA    1 1 
ATOM   1137 C  C     . MET   A 1 172 ? 29.516 0.858   -21.392 1    50.17  ? 172 MET   A C     1 1 
ATOM   1138 O  O     . MET   A 1 172 ? 30.12  0.317   -22.314 1    50.68  ? 172 MET   A O     1 1 
ATOM   1139 C  CB    . MET   A 1 172 ? 28.47  -0.553  -19.556 1    49.09  ? 172 MET   A CB    1 1 
ATOM   1140 C  CG    . MET   A 1 172 ? 28.71  -1.494  -18.374 1    51.41  ? 172 MET   A CG    1 1 
ATOM   1141 S  SD    . MET   A 1 172 ? 27.18  -2.322  -17.812 1    54.47  ? 172 MET   A SD    1 1 
ATOM   1142 C  CE    . MET   A 1 172 ? 27.054 -3.545  -18.981 1    54.9   ? 172 MET   A CE    1 1 
ATOM   1143 N  N     . LEU   A 1 173 ? 28.673 1.897   -21.588 1    49.9   ? 173 LEU   A N     1 1 
ATOM   1144 C  CA    . LEU   A 1 173 ? 28.485 2.479   -22.914 1    50.86  ? 173 LEU   A CA    1 1 
ATOM   1145 C  C     . LEU   A 1 173 ? 29.794 3.074   -23.445 1    50.16  ? 173 LEU   A C     1 1 
ATOM   1146 O  O     . LEU   A 1 173 ? 30.104 2.906   -24.618 1    50.58  ? 173 LEU   A O     1 1 
ATOM   1147 C  CB    . LEU   A 1 173 ? 27.419 3.587   -22.906 1    52.26  ? 173 LEU   A CB    1 1 
ATOM   1148 C  CG    . LEU   A 1 173 ? 25.964 3.171   -22.756 1    56.53  ? 173 LEU   A CG    1 1 
ATOM   1149 C  CD1   . LEU   A 1 173 ? 25.052 4.388   -22.89  1    57.6   ? 173 LEU   A CD1   1 1 
ATOM   1150 C  CD2   . LEU   A 1 173 ? 25.569 2.12    -23.802 1    58.23  ? 173 LEU   A CD2   1 1 
ATOM   1151 N  N     . ALA   A 1 174 ? 30.551 3.768   -22.585 1    49.17  ? 174 ALA   A N     1 1 
ATOM   1152 C  CA    . ALA   A 1 174 ? 31.814 4.399   -22.96  1    48.71  ? 174 ALA   A CA    1 1 
ATOM   1153 C  C     . ALA   A 1 174 ? 32.917 3.366   -23.264 1    49.31  ? 174 ALA   A C     1 1 
ATOM   1154 O  O     . ALA   A 1 174 ? 33.629 3.506   -24.252 1    49.66  ? 174 ALA   A O     1 1 
ATOM   1155 C  CB    . ALA   A 1 174 ? 32.264 5.353   -21.864 1    47.82  ? 174 ALA   A CB    1 1 
ATOM   1156 N  N     . THR   A 1 175 ? 33.058 2.342   -22.426 1    49.45  ? 175 THR   A N     1 1 
ATOM   1157 C  CA    . THR   A 1 175 ? 34.072 1.301   -22.607 1    50.22  ? 175 THR   A CA    1 1 
ATOM   1158 C  C     . THR   A 1 175 ? 33.752 0.454   -23.857 1    50.26  ? 175 THR   A C     1 1 
ATOM   1159 O  O     . THR   A 1 175 ? 34.649 0.133   -24.626 1    50.41  ? 175 THR   A O     1 1 
ATOM   1160 C  CB    . THR   A 1 175 ? 34.235 0.489   -21.295 1    52.47  ? 175 THR   A CB    1 1 
ATOM   1161 O  OG1   . THR   A 1 175 ? 34.639 1.375   -20.239 1    53.53  ? 175 THR   A OG1   1 1 
ATOM   1162 C  CG2   . THR   A 1 175 ? 35.271 -0.597  -21.404 1    53.44  ? 175 THR   A CG2   1 1 
ATOM   1163 N  N     . HIS   A 1 176 ? 32.467 0.15    -24.086 1    50.1   ? 176 HIS   A N     1 1 
ATOM   1164 C  CA    . HIS   A 1 176 ? 32.017 -0.593  -25.247 1    50.42  ? 176 HIS   A CA    1 1 
ATOM   1165 C  C     . HIS   A 1 176 ? 32.373 0.159   -26.531 1    51.69  ? 176 HIS   A C     1 1 
ATOM   1166 O  O     . HIS   A 1 176 ? 32.966 -0.435  -27.43  1    52.26  ? 176 HIS   A O     1 1 
ATOM   1167 C  CB    . HIS   A 1 176 ? 30.507 -0.86   -25.162 1    50.67  ? 176 HIS   A CB    1 1 
ATOM   1168 C  CG    . HIS   A 1 176 ? 29.959 -1.629  -26.321 1    53.27  ? 176 HIS   A CG    1 1 
ATOM   1169 N  ND1   . HIS   A 1 176 ? 30.167 -2.996  -26.45  1    55.31  ? 176 HIS   A ND1   1 1 
ATOM   1170 C  CD2   . HIS   A 1 176 ? 29.221 -1.2    -27.369 1    54.28  ? 176 HIS   A CD2   1 1 
ATOM   1171 C  CE1   . HIS   A 1 176 ? 29.564 -3.346  -27.571 1    55.44  ? 176 HIS   A CE1   1 1 
ATOM   1172 N  NE2   . HIS   A 1 176 ? 28.979 -2.299  -28.158 1    55.39  ? 176 HIS   A NE2   1 1 
ATOM   1173 N  N     . HIS   A 1 177 ? 32.077 1.465   -26.607 1    51.73  ? 177 HIS   A N     1 1 
ATOM   1174 C  CA    . HIS   A 1 177 ? 32.407 2.252   -27.794 1    52.28  ? 177 HIS   A CA    1 1 
ATOM   1175 C  C     . HIS   A 1 177 ? 33.917 2.22    -28.099 1    52.96  ? 177 HIS   A C     1 1 
ATOM   1176 O  O     . HIS   A 1 177 ? 34.303 1.992   -29.253 1    52.87  ? 177 HIS   A O     1 1 
ATOM   1177 C  CB    . HIS   A 1 177 ? 31.902 3.688   -27.662 1    53.07  ? 177 HIS   A CB    1 1 
ATOM   1178 C  CG    . HIS   A 1 177 ? 32.319 4.551   -28.809 1    56.17  ? 177 HIS   A CG    1 1 
ATOM   1179 N  ND1   . HIS   A 1 177 ? 31.792 4.369   -30.073 1    58.3   ? 177 HIS   A ND1   1 1 
ATOM   1180 C  CD2   . HIS   A 1 177 ? 33.267 5.514   -28.867 1    57.55  ? 177 HIS   A CD2   1 1 
ATOM   1181 C  CE1   . HIS   A 1 177 ? 32.407 5.241   -30.853 1    58.66  ? 177 HIS   A CE1   1 1 
ATOM   1182 N  NE2   . HIS   A 1 177 ? 33.304 5.955   -30.173 1    58.84  ? 177 HIS   A NE2   1 1 
ATOM   1183 N  N     . LEU   A 1 178 ? 34.761 2.419   -27.062 1    52.84  ? 178 LEU   A N     1 1 
ATOM   1184 C  CA    . LEU   A 1 178 ? 36.214 2.374   -27.234 1    52.9   ? 178 LEU   A CA    1 1 
ATOM   1185 C  C     . LEU   A 1 178 ? 36.658 0.999   -27.716 1    53.41  ? 178 LEU   A C     1 1 
ATOM   1186 O  O     . LEU   A 1 178 ? 37.439 0.915   -28.656 1    53.95  ? 178 LEU   A O     1 1 
ATOM   1187 C  CB    . LEU   A 1 178 ? 36.948 2.718   -25.922 1    52.45  ? 178 LEU   A CB    1 1 
ATOM   1188 C  CG    . LEU   A 1 178 ? 36.687 4.097   -25.316 1    52.71  ? 178 LEU   A CG    1 1 
ATOM   1189 C  CD1   . LEU   A 1 178 ? 37.477 4.27    -24.055 1    52.54  ? 178 LEU   A CD1   1 1 
ATOM   1190 C  CD2   . LEU   A 1 178 ? 36.995 5.22    -26.311 1    52.97  ? 178 LEU   A CD2   1 1 
ATOM   1191 N  N     . ALA   A 1 179 ? 36.134 -0.079  -27.104 1    53.27  ? 179 ALA   A N     1 1 
ATOM   1192 C  CA    . ALA   A 1 179 ? 36.496 -1.448  -27.457 1    54.03  ? 179 ALA   A CA    1 1 
ATOM   1193 C  C     . ALA   A 1 179 ? 36.012 -1.877  -28.84  1    56.29  ? 179 ALA   A C     1 1 
ATOM   1194 O  O     . ALA   A 1 179 ? 36.538 -2.839  -29.383 1    56.89  ? 179 ALA   A O     1 1 
ATOM   1195 C  CB    . ALA   A 1 179 ? 36.035 -2.421  -26.39  1    53.56  ? 179 ALA   A CB    1 1 
ATOM   1196 N  N     . LEU   A 1 180 ? 35.065 -1.142  -29.449 1    57.66  ? 180 LEU   A N     1 1 
ATOM   1197 C  CA    . LEU   A 1 180 ? 34.674 -1.389  -30.837 1    59.18  ? 180 LEU   A CA    1 1 
ATOM   1198 C  C     . LEU   A 1 180 ? 35.858 -1.039  -31.791 1    62.48  ? 180 LEU   A C     1 1 
ATOM   1199 O  O     . LEU   A 1 180 ? 35.856 -1.482  -32.936 1    63.44  ? 180 LEU   A O     1 1 
ATOM   1200 C  CB    . LEU   A 1 180 ? 33.432 -0.583  -31.228 1    58.42  ? 180 LEU   A CB    1 1 
ATOM   1201 C  CG    . LEU   A 1 180 ? 32.09  -1.051  -30.67  1    58.84  ? 180 LEU   A CG    1 1 
ATOM   1202 C  CD1   . LEU   A 1 180 ? 30.974 -0.154  -31.151 1    58.93  ? 180 LEU   A CD1   1 1 
ATOM   1203 C  CD2   . LEU   A 1 180 ? 31.794 -2.481  -31.06  1    59.03  ? 180 LEU   A CD2   1 1 
ATOM   1204 N  N     . HIS   A 1 181 ? 36.862 -0.251  -31.328 1    64.07  ? 181 HIS   A N     1 1 
ATOM   1205 C  CA    . HIS   A 1 181 ? 38.056 0.068   -32.11  1    66.56  ? 181 HIS   A CA    1 1 
ATOM   1206 C  C     . HIS   A 1 181 ? 39.152 -1.028  -31.975 1    69.62  ? 181 HIS   A C     1 1 
ATOM   1207 O  O     . HIS   A 1 181 ? 40.168 -0.937  -32.647 1    70.22  ? 181 HIS   A O     1 1 
ATOM   1208 C  CB    . HIS   A 1 181 ? 38.627 1.438   -31.71  1    66.75  ? 181 HIS   A CB    1 1 
ATOM   1209 C  CG    . HIS   A 1 181 ? 37.705 2.59    -31.976 1    67.94  ? 181 HIS   A CG    1 1 
ATOM   1210 N  ND1   . HIS   A 1 181 ? 37.975 3.514   -32.97  1    69.25  ? 181 HIS   A ND1   1 1 
ATOM   1211 C  CD2   . HIS   A 1 181 ? 36.541 2.928   -31.368 1    68.73  ? 181 HIS   A CD2   1 1 
ATOM   1212 C  CE1   . HIS   A 1 181 ? 36.976 4.383   -32.932 1    69.66  ? 181 HIS   A CE1   1 1 
ATOM   1213 N  NE2   . HIS   A 1 181 ? 36.085 4.068   -31.992 1    69.63  ? 181 HIS   A NE2   1 1 
ATOM   1214 N  N     . GLU   A 1 182 ? 38.965 -2.038  -31.103 1    71.38  ? 182 GLU   A N     1 1 
ATOM   1215 C  CA    . GLU   A 1 182 ? 39.912 -3.142  -30.929 1    73.72  ? 182 GLU   A CA    1 1 
ATOM   1216 C  C     . GLU   A 1 182 ? 39.474 -4.367  -31.755 1    75.8   ? 182 GLU   A C     1 1 
ATOM   1217 O  O     . GLU   A 1 182 ? 38.291 -4.518  -32.085 1    75.42  ? 182 GLU   A O     1 1 
ATOM   1218 C  CB    . GLU   A 1 182 ? 39.999 -3.563  -29.447 1    76.21  ? 182 GLU   A CB    1 1 
ATOM   1219 C  CG    . GLU   A 1 182 ? 40.61  -2.526  -28.525 1    82.17  ? 182 GLU   A CG    1 1 
ATOM   1220 C  CD    . GLU   A 1 182 ? 40.149 -2.649  -27.083 1    90.74  ? 182 GLU   A CD    1 1 
ATOM   1221 O  OE1   . GLU   A 1 182 ? 39.838 -3.783  -26.648 1    92.48  ? 182 GLU   A OE1   1 1 
ATOM   1222 O  OE2   . GLU   A 1 182 ? 40.085 -1.608  -26.388 1    93.55  ? 182 GLU   A OE2   1 1 
ATOM   1223 N  N     . ASP   A 1 183 ? 40.433 -5.252  -32.068 1    77.69  ? 183 ASP   A N     1 1 
ATOM   1224 C  CA    . ASP   A 1 183 ? 40.162 -6.498  -32.783 1    79.78  ? 183 ASP   A CA    1 1 
ATOM   1225 C  C     . ASP   A 1 183 ? 40.57  -7.629  -31.853 1    80.74  ? 183 ASP   A C     1 1 
ATOM   1226 O  O     . ASP   A 1 183 ? 41.56  -8.32   -32.089 1    81.55  ? 183 ASP   A O     1 1 
ATOM   1227 C  CB    . ASP   A 1 183 ? 40.93  -6.574  -34.118 1    83.17  ? 183 ASP   A CB    1 1 
ATOM   1228 C  CG    . ASP   A 1 183 ? 40.548 -7.772  -34.98  1    90.66  ? 183 ASP   A CG    1 1 
ATOM   1229 O  OD1   . ASP   A 1 183 ? 39.488 -8.388  -34.71  1    92.34  ? 183 ASP   A OD1   1 1 
ATOM   1230 O  OD2   . ASP   A 1 183 ? 41.305 -8.09   -35.927 1    93.52  ? 183 ASP   A OD2   1 1 
ATOM   1231 N  N     . LYS   A 1 184 ? 39.83  -7.782  -30.765 1    80.57  ? 184 LYS   A N     1 1 
ATOM   1232 C  CA    . LYS   A 1 184 ? 40.112 -8.791  -29.771 1    81.09  ? 184 LYS   A CA    1 1 
ATOM   1233 C  C     . LYS   A 1 184 ? 39.277 -10.029 -30.074 1    81.26  ? 184 LYS   A C     1 1 
ATOM   1234 O  O     . LYS   A 1 184 ? 38.054 -9.934  -30.198 1    81.78  ? 184 LYS   A O     1 1 
ATOM   1235 C  CB    . LYS   A 1 184 ? 39.73  -8.255  -28.378 1    83.39  ? 184 LYS   A CB    1 1 
ATOM   1236 C  CG    . LYS   A 1 184 ? 40.883 -8.18   -27.382 1    88.24  ? 184 LYS   A CG    1 1 
ATOM   1237 C  CD    . LYS   A 1 184 ? 40.387 -8.082  -25.927 1    93.51  ? 184 LYS   A CD    1 1 
ATOM   1238 C  CE    . LYS   A 1 184 ? 39.496 -6.878  -25.682 1    97.77  ? 184 LYS   A CE    1 1 
ATOM   1239 N  NZ    . LYS   A 1 184 ? 39.192 -6.669  -24.236 1    100.09 ? 184 LYS   A NZ    1 1 
ATOM   1240 N  N     . PRO   A 1 185 ? 39.909 -11.208 -30.149 1    80.25  ? 185 PRO   A N     1 1 
ATOM   1241 C  CA    . PRO   A 1 185 ? 39.137 -12.44  -30.383 1    78.95  ? 185 PRO   A CA    1 1 
ATOM   1242 C  C     . PRO   A 1 185 ? 38.137 -12.717 -29.26  1    76.86  ? 185 PRO   A C     1 1 
ATOM   1243 O  O     . PRO   A 1 185 ? 38.418 -12.442 -28.088 1    76.81  ? 185 PRO   A O     1 1 
ATOM   1244 C  CB    . PRO   A 1 185 ? 40.216 -13.533 -30.435 1    80.27  ? 185 PRO   A CB    1 1 
ATOM   1245 C  CG    . PRO   A 1 185 ? 41.505 -12.787 -30.757 1    81.36  ? 185 PRO   A CG    1 1 
ATOM   1246 C  CD    . PRO   A 1 185 ? 41.353 -11.481 -30.028 1    80     ? 185 PRO   A CD    1 1 
ATOM   1247 N  N     . ASP   A 1 186 ? 36.96  -13.244 -29.634 1    74.67  ? 186 ASP   A N     1 1 
ATOM   1248 C  CA    . ASP   A 1 186 ? 35.87  -13.565 -28.715 1    73.21  ? 186 ASP   A CA    1 1 
ATOM   1249 C  C     . ASP   A 1 186 ? 35.198 -12.329 -28.124 1    70.93  ? 186 ASP   A C     1 1 
ATOM   1250 O  O     . ASP   A 1 186 ? 34.565 -12.448 -27.085 1    70.82  ? 186 ASP   A O     1 1 
ATOM   1251 C  CB    . ASP   A 1 186 ? 36.346 -14.48  -27.576 1    75.25  ? 186 ASP   A CB    1 1 
ATOM   1252 C  CG    . ASP   A 1 186 ? 37.032 -15.749 -28.015 1    81.49  ? 186 ASP   A CG    1 1 
ATOM   1253 O  OD1   . ASP   A 1 186 ? 36.955 -16.082 -29.225 1    82.9   ? 186 ASP   A OD1   1 1 
ATOM   1254 O  OD2   . ASP   A 1 186 ? 37.639 -16.423 -27.15  1    84.03  ? 186 ASP   A OD2   1 1 
ATOM   1255 N  N     . PHE   A 1 187 ? 35.343 -11.152 -28.751 1    68.89  ? 187 PHE   A N     1 1 
ATOM   1256 C  CA    . PHE   A 1 187 ? 34.749 -9.931  -28.217 1    67.44  ? 187 PHE   A CA    1 1 
ATOM   1257 C  C     . PHE   A 1 187 ? 34.102 -9.088  -29.279 1    66     ? 187 PHE   A C     1 1 
ATOM   1258 O  O     . PHE   A 1 187 ? 34.634 -8.963  -30.376 1    66.54  ? 187 PHE   A O     1 1 
ATOM   1259 C  CB    . PHE   A 1 187 ? 35.815 -9.08   -27.507 1    67.01  ? 187 PHE   A CB    1 1 
ATOM   1260 C  CG    . PHE   A 1 187 ? 36.005 -9.387  -26.043 1    67.4   ? 187 PHE   A CG    1 1 
ATOM   1261 C  CD1   . PHE   A 1 187 ? 35.243 -8.749  -25.082 1    67.88  ? 187 PHE   A CD1   1 1 
ATOM   1262 C  CD2   . PHE   A 1 187 ? 36.955 -10.305 -25.628 1    68.37  ? 187 PHE   A CD2   1 1 
ATOM   1263 C  CE1   . PHE   A 1 187 ? 35.415 -9.033  -23.734 1    68.68  ? 187 PHE   A CE1   1 1 
ATOM   1264 C  CE2   . PHE   A 1 187 ? 37.129 -10.586 -24.276 1    69.05  ? 187 PHE   A CE2   1 1 
ATOM   1265 C  CZ    . PHE   A 1 187 ? 36.349 -9.957  -23.338 1    68.61  ? 187 PHE   A CZ    1 1 
ATOM   1266 N  N     . VAL   A 1 188 ? 32.969 -8.471  -28.933 1    64.17  ? 188 VAL   A N     1 1 
ATOM   1267 C  CA    . VAL   A 1 188 ? 32.267 -7.479  -29.735 1    62.71  ? 188 VAL   A CA    1 1 
ATOM   1268 C  C     . VAL   A 1 188 ? 32.115 -6.298  -28.782 1    61.24  ? 188 VAL   A C     1 1 
ATOM   1269 O  O     . VAL   A 1 188 ? 31.153 -6.235  -28.016 1    61.05  ? 188 VAL   A O     1 1 
ATOM   1270 C  CB    . VAL   A 1 188 ? 30.901 -7.946  -30.267 1    63.57  ? 188 VAL   A CB    1 1 
ATOM   1271 C  CG1   . VAL   A 1 188 ? 30.198 -6.805  -30.992 1    64.05  ? 188 VAL   A CG1   1 1 
ATOM   1272 C  CG2   . VAL   A 1 188 ? 31.053 -9.152  -31.191 1    64.47  ? 188 VAL   A CG2   1 1 
ATOM   1273 N  N     . GLY   A 1 189 ? 33.113 -5.42   -28.778 1    60.11  ? 189 GLY   A N     1 1 
ATOM   1274 C  CA    . GLY   A 1 189 ? 33.163 -4.282  -27.868 1    59.37  ? 189 GLY   A CA    1 1 
ATOM   1275 C  C     . GLY   A 1 189 ? 33.523 -4.848  -26.513 1    58.46  ? 189 GLY   A C     1 1 
ATOM   1276 O  O     . GLY   A 1 189 ? 34.511 -5.581  -26.406 1    58.39  ? 189 GLY   A O     1 1 
ATOM   1277 N  N     . ILE   A 1 190 ? 32.682 -4.605  -25.494 1    57.32  ? 190 ILE   A N     1 1 
ATOM   1278 C  CA    . ILE   A 1 190 ? 32.903 -5.217  -24.187 1    56.72  ? 190 ILE   A CA    1 1 
ATOM   1279 C  C     . ILE   A 1 190 ? 32.138 -6.539  -24     1    56.72  ? 190 ILE   A C     1 1 
ATOM   1280 O  O     . ILE   A 1 190 ? 32.235 -7.139  -22.929 1    56.85  ? 190 ILE   A O     1 1 
ATOM   1281 C  CB    . ILE   A 1 190 ? 32.642 -4.253  -23.014 1    56.35  ? 190 ILE   A CB    1 1 
ATOM   1282 C  CG1   . ILE   A 1 190 ? 31.187 -3.774  -22.976 1    56.06  ? 190 ILE   A CG1   1 1 
ATOM   1283 C  CG2   . ILE   A 1 190 ? 33.638 -3.117  -23.029 1    56.61  ? 190 ILE   A CG2   1 1 
ATOM   1284 C  CD1   . ILE   A 1 190 ? 30.851 -3.049  -21.706 1    56.66  ? 190 ILE   A CD1   1 1 
ATOM   1285 N  N     . ILE   A 1 191 ? 31.373 -6.985  -25.007 1    56.53  ? 191 ILE   A N     1 1 
ATOM   1286 C  CA    . ILE   A 1 191 ? 30.63  -8.232  -24.893 1    57.23  ? 191 ILE   A CA    1 1 
ATOM   1287 C  C     . ILE   A 1 191 ? 31.519 -9.399  -25.287 1    57.69  ? 191 ILE   A C     1 1 
ATOM   1288 O  O     . ILE   A 1 191 ? 31.944 -9.487  -26.44  1    57.39  ? 191 ILE   A O     1 1 
ATOM   1289 C  CB    . ILE   A 1 191 ? 29.345 -8.22   -25.75  1    57.82  ? 191 ILE   A CB    1 1 
ATOM   1290 C  CG1   . ILE   A 1 191 ? 28.489 -6.978  -25.454 1    58.98  ? 191 ILE   A CG1   1 1 
ATOM   1291 C  CG2   . ILE   A 1 191 ? 28.563 -9.518  -25.563 1    58.24  ? 191 ILE   A CG2   1 1 
ATOM   1292 C  CD1   . ILE   A 1 191 ? 27.279 -6.846  -26.318 1    60.12  ? 191 ILE   A CD1   1 1 
ATOM   1293 N  N     . CYS   A 1 192 ? 31.812 -10.287 -24.339 1    58.1   ? 192 CYS   A N     1 1 
ATOM   1294 C  CA    . CYS   A 1 192 ? 32.58  -11.484 -24.644 1    59.09  ? 192 CYS   A CA    1 1 
ATOM   1295 C  C     . CYS   A 1 192 ? 31.579 -12.486 -25.233 1    60.09  ? 192 CYS   A C     1 1 
ATOM   1296 O  O     . CYS   A 1 192 ? 30.563 -12.741 -24.607 1    60.67  ? 192 CYS   A O     1 1 
ATOM   1297 C  CB    . CYS   A 1 192 ? 33.258 -12.028 -23.393 1    59.59  ? 192 CYS   A CB    1 1 
ATOM   1298 S  SG    . CYS   A 1 192 ? 34.302 -13.476 -23.691 1    63.29  ? 192 CYS   A SG    1 1 
ATOM   1299 N  N     . THR   A 1 193 ? 31.811 -12.993 -26.44  1    60.45  ? 193 THR   A N     1 1 
ATOM   1300 C  CA    . THR   A 1 193 ? 30.876 -13.935 -27.069 1    61.85  ? 193 THR   A CA    1 1 
ATOM   1301 C  C     . THR   A 1 193 ? 30.949 -15.368 -26.507 1    62.11  ? 193 THR   A C     1 1 
ATOM   1302 O  O     . THR   A 1 193 ? 30.053 -16.165 -26.768 1    62.77  ? 193 THR   A O     1 1 
ATOM   1303 C  CB    . THR   A 1 193 ? 31.044 -13.93  -28.598 1    63.9   ? 193 THR   A CB    1 1 
ATOM   1304 O  OG1   . THR   A 1 193 ? 32.389 -14.298 -28.921 1    65.27  ? 193 THR   A OG1   1 1 
ATOM   1305 C  CG2   . THR   A 1 193 ? 30.716 -12.572 -29.203 1    64.48  ? 193 THR   A CG2   1 1 
ATOM   1306 N  N     . ARG   A 1 194 ? 31.996 -15.696 -25.745 1    61.44  ? 194 ARG   A N     1 1 
ATOM   1307 C  CA    . ARG   A 1 194 ? 32.188 -17.047 -25.22  1    61.18  ? 194 ARG   A CA    1 1 
ATOM   1308 C  C     . ARG   A 1 194 ? 32.628 -16.979 -23.747 1    59.75  ? 194 ARG   A C     1 1 
ATOM   1309 O  O     . ARG   A 1 194 ? 33.548 -17.7   -23.334 1    60.02  ? 194 ARG   A O     1 1 
ATOM   1310 C  CB    . ARG   A 1 194 ? 33.31  -17.733 -26.027 1    63.74  ? 194 ARG   A CB    1 1 
ATOM   1311 C  CG    . ARG   A 1 194 ? 33.007 -18.152 -27.438 1    69.05  ? 194 ARG   A CG    1 1 
ATOM   1312 C  CD    . ARG   A 1 194 ? 34.272 -18.746 -28.064 1    74.41  ? 194 ARG   A CD    1 1 
ATOM   1313 N  NE    . ARG   A 1 194 ? 34.753 -19.942 -27.36  1    78.41  ? 194 ARG   A NE    1 1 
ATOM   1314 C  CZ    . ARG   A 1 194 ? 35.848 -19.981 -26.599 1    81.68  ? 194 ARG   A CZ    1 1 
ATOM   1315 N  NH1   . ARG   A 1 194 ? 36.591 -18.891 -26.433 1    81.13  ? 194 ARG   A NH1   1 1 
ATOM   1316 N  NH2   . ARG   A 1 194 ? 36.207 -21.111 -25.998 1    81.72  ? 194 ARG   A NH2   1 1 
ATOM   1317 N  N     . LEU   A 1 195 ? 31.987 -16.106 -22.954 1    58.28  ? 195 LEU   A N     1 1 
ATOM   1318 C  CA    . LEU   A 1 195 ? 32.377 -15.931 -21.562 1    56.83  ? 195 LEU   A CA    1 1 
ATOM   1319 C  C     . LEU   A 1 195 ? 32.268 -17.198 -20.749 1    55.53  ? 195 LEU   A C     1 1 
ATOM   1320 O  O     . LEU   A 1 195 ? 31.252 -17.895 -20.79  1    55.79  ? 195 LEU   A O     1 1 
ATOM   1321 C  CB    . LEU   A 1 195 ? 31.633 -14.777 -20.891 1    56.78  ? 195 LEU   A CB    1 1 
ATOM   1322 C  CG    . LEU   A 1 195 ? 32.072 -14.481 -19.457 1    58.16  ? 195 LEU   A CG    1 1 
ATOM   1323 C  CD1   . LEU   A 1 195 ? 32.477 -13.051 -19.297 1    58.79  ? 195 LEU   A CD1   1 1 
ATOM   1324 C  CD2   . LEU   A 1 195 ? 30.977 -14.833 -18.461 1    58.69  ? 195 LEU   A CD2   1 1 
ATOM   1325 N  N     . SER   A 1 196 ? 33.335 -17.503 -20.015 1    54.03  ? 196 SER   A N     1 1 
ATOM   1326 C  CA    . SER   A 1 196 ? 33.374 -18.653 -19.131 1    52.93  ? 196 SER   A CA    1 1 
ATOM   1327 C  C     . SER   A 1 196 ? 33.24  -18.16  -17.694 1    52.27  ? 196 SER   A C     1 1 
ATOM   1328 O  O     . SER   A 1 196 ? 34.187 -17.568 -17.173 1    52.05  ? 196 SER   A O     1 1 
ATOM   1329 C  CB    . SER   A 1 196 ? 34.705 -19.377 -19.286 1    53.7   ? 196 SER   A CB    1 1 
ATOM   1330 O  OG    . SER   A 1 196 ? 34.859 -20.355 -18.273 1    56.3   ? 196 SER   A OG    1 1 
ATOM   1331 N  N     . PRO   A 1 197 ? 32.096 -18.398 -17.022 1    51.74  ? 197 PRO   A N     1 1 
ATOM   1332 C  CA    . PRO   A 1 197 ? 31.982 -17.964 -15.621 1    51.6   ? 197 PRO   A CA    1 1 
ATOM   1333 C  C     . PRO   A 1 197 ? 33.053 -18.586 -14.717 1    51.28  ? 197 PRO   A C     1 1 
ATOM   1334 O  O     . PRO   A 1 197 ? 33.532 -17.899 -13.829 1    51.71  ? 197 PRO   A O     1 1 
ATOM   1335 C  CB    . PRO   A 1 197 ? 30.551 -18.351 -15.21  1    52.53  ? 197 PRO   A CB    1 1 
ATOM   1336 C  CG    . PRO   A 1 197 ? 30.069 -19.275 -16.256 1    53.24  ? 197 PRO   A CG    1 1 
ATOM   1337 C  CD    . PRO   A 1 197 ? 30.865 -19.046 -17.506 1    51.35  ? 197 PRO   A CD    1 1 
ATOM   1338 N  N     . LYS   A 1 198 ? 33.472 -19.845 -14.955 1    50.61  ? 198 LYS   A N     1 1 
ATOM   1339 C  CA    . LYS   A 1 198 ? 34.525 -20.455 -14.137 1    50.92  ? 198 LYS   A CA    1 1 
ATOM   1340 C  C     . LYS   A 1 198 ? 35.833 -19.647 -14.21  1    52.26  ? 198 LYS   A C     1 1 
ATOM   1341 O  O     . LYS   A 1 198 ? 36.394 -19.342 -13.163 1    53.26  ? 198 LYS   A O     1 1 
ATOM   1342 C  CB    . LYS   A 1 198 ? 34.748 -21.93  -14.501 1    52.2   ? 198 LYS   A CB    1 1 
ATOM   1343 C  CG    . LYS   A 1 198 ? 35.995 -22.551 -13.869 1    56.53  ? 198 LYS   A CG    1 1 
ATOM   1344 C  CD    . LYS   A 1 198 ? 35.969 -24.042 -13.961 1    62.62  ? 198 LYS   A CD    1 1 
ATOM   1345 C  CE    . LYS   A 1 198 ? 37.06  -24.687 -13.141 1    68.58  ? 198 LYS   A CE    1 1 
ATOM   1346 N  NZ    . LYS   A 1 198 ? 38.338 -24.737 -13.894 1    73.13  ? 198 LYS   A NZ    1 1 
ATOM   1347 N  N     . LYS   A 1 199 ? 36.286 -19.258 -15.424 1    51.95  ? 199 LYS   A N     1 1 
ATOM   1348 C  CA    . LYS   A 1 199 ? 37.526 -18.497 -15.608 1    52.22  ? 199 LYS   A CA    1 1 
ATOM   1349 C  C     . LYS   A 1 199 ? 37.482 -17.11  -14.993 1    51.45  ? 199 LYS   A C     1 1 
ATOM   1350 O  O     . LYS   A 1 199 ? 38.479 -16.684 -14.406 1    52.39  ? 199 LYS   A O     1 1 
ATOM   1351 C  CB    . LYS   A 1 199 ? 37.93  -18.435 -17.089 1    55.56  ? 199 LYS   A CB    1 1 
ATOM   1352 C  CG    . LYS   A 1 199 ? 38.032 -19.835 -17.693 1    62.83  ? 199 LYS   A CG    1 1 
ATOM   1353 C  CD    . LYS   A 1 199 ? 39.341 -20.098 -18.434 1    70.29  ? 199 LYS   A CD    1 1 
ATOM   1354 C  CE    . LYS   A 1 199 ? 39.675 -21.576 -18.405 1    75.97  ? 199 LYS   A CE    1 1 
ATOM   1355 N  NZ    . LYS   A 1 199 ? 40.955 -21.88  -19.11  1    79.59  ? 199 LYS   A NZ    1 1 
ATOM   1356 N  N     . ILE   A 1 200 ? 36.343 -16.407 -15.098 1    49.65  ? 200 ILE   A N     1 1 
ATOM   1357 C  CA    . ILE   A 1 200 ? 36.229 -15.086 -14.478 1    49.08  ? 200 ILE   A CA    1 1 
ATOM   1358 C  C     . ILE   A 1 200 ? 36.184 -15.22  -12.941 1    48.78  ? 200 ILE   A C     1 1 
ATOM   1359 O  O     . ILE   A 1 200 ? 36.805 -14.416 -12.237 1    49.06  ? 200 ILE   A O     1 1 
ATOM   1360 C  CB    . ILE   A 1 200 ? 35.078 -14.236 -15.071 1    49.25  ? 200 ILE   A CB    1 1 
ATOM   1361 C  CG1   . ILE   A 1 200 ? 35.229 -12.775 -14.684 1    50.34  ? 200 ILE   A CG1   1 1 
ATOM   1362 C  CG2   . ILE   A 1 200 ? 33.714 -14.775 -14.676 1    49.15  ? 200 ILE   A CG2   1 1 
ATOM   1363 C  CD1   . ILE   A 1 200 ? 34.331 -11.86  -15.468 1    52.3   ? 200 ILE   A CD1   1 1 
ATOM   1364 N  N     . ILE   A 1 201 ? 35.546 -16.291 -12.428 1    47.61  ? 201 ILE   A N     1 1 
ATOM   1365 C  CA    . ILE   A 1 201 ? 35.526 -16.544 -10.996 1    47.58  ? 201 ILE   A CA    1 1 
ATOM   1366 C  C     . ILE   A 1 201 ? 36.959 -16.815 -10.497 1    48.64  ? 201 ILE   A C     1 1 
ATOM   1367 O  O     . ILE   A 1 201 ? 37.393 -16.204 -9.518  1    49.14  ? 201 ILE   A O     1 1 
ATOM   1368 C  CB    . ILE   A 1 201 ? 34.548 -17.68  -10.62  1    46.37  ? 201 ILE   A CB    1 1 
ATOM   1369 C  CG1   . ILE   A 1 201 ? 33.09  -17.266 -10.877 1    46.24  ? 201 ILE   A CG1   1 1 
ATOM   1370 C  CG2   . ILE   A 1 201 ? 34.728 -18.068 -9.163  1    46.43  ? 201 ILE   A CG2   1 1 
ATOM   1371 C  CD1   . ILE   A 1 201 ? 32.1   -18.437 -10.786 1    46.46  ? 201 ILE   A CD1   1 1 
ATOM   1372 N  N     . GLU   A 1 202 ? 37.703 -17.653 -11.222 1    48.17  ? 202 GLU   A N     1 1 
ATOM   1373 C  CA    . GLU   A 1 202 ? 39.076 -17.983 -10.867 1    49.21  ? 202 GLU   A CA    1 1 
ATOM   1374 C  C     . GLU   A 1 202 ? 39.965 -16.774 -10.85  1    50.01  ? 202 GLU   A C     1 1 
ATOM   1375 O  O     . GLU   A 1 202 ? 40.78  -16.632 -9.939  1    50.44  ? 202 GLU   A O     1 1 
ATOM   1376 C  CB    . GLU   A 1 202 ? 39.66  -19.032 -11.814 1    49.93  ? 202 GLU   A CB    1 1 
ATOM   1377 C  CG    . GLU   A 1 202 ? 39.03  -20.382 -11.608 1    53.63  ? 202 GLU   A CG    1 1 
ATOM   1378 C  CD    . GLU   A 1 202 ? 39.62  -21.468 -12.472 1    61.12  ? 202 GLU   A CD    1 1 
ATOM   1379 O  OE1   . GLU   A 1 202 ? 40.117 -21.14  -13.571 1    63.81  ? 202 GLU   A OE1   1 1 
ATOM   1380 O  OE2   . GLU   A 1 202 ? 39.578 -22.649 -12.055 1    63.96  ? 202 GLU   A OE2   1 1 
ATOM   1381 N  N     . LYS   A 1 203 ? 39.78  -15.867 -11.813 1    50.18  ? 203 LYS   A N     1 1 
ATOM   1382 C  CA    . LYS   A 1 203 ? 40.574 -14.64  -11.888 1    50.43  ? 203 LYS   A CA    1 1 
ATOM   1383 C  C     . LYS   A 1 203 ? 40.405 -13.805 -10.595 1    50.74  ? 203 LYS   A C     1 1 
ATOM   1384 O  O     . LYS   A 1 203 ? 41.392 -13.364 -10     1    51.22  ? 203 LYS   A O     1 1 
ATOM   1385 C  CB    . LYS   A 1 203 ? 40.158 -13.834 -13.131 1    51.69  ? 203 LYS   A CB    1 1 
ATOM   1386 C  CG    . LYS   A 1 203 ? 40.884 -12.511 -13.29  1    54.75  ? 203 LYS   A CG    1 1 
ATOM   1387 C  CD    . LYS   A 1 203 ? 40.104 -11.533 -14.153 1    59.99  ? 203 LYS   A CD    1 1 
ATOM   1388 C  CE    . LYS   A 1 203 ? 40.811 -10.192 -14.183 1    65.31  ? 203 LYS   A CE    1 1 
ATOM   1389 N  NZ    . LYS   A 1 203 ? 40.067 -9.144  -14.943 1    68.24  ? 203 LYS   A NZ    1 1 
ATOM   1390 N  N     . TRP   A 1 204 ? 39.164 -13.686 -10.113 1    50.19  ? 204 TRP   A N     1 1 
ATOM   1391 C  CA    . TRP   A 1 204 ? 38.896 -12.914 -8.91   1    49.87  ? 204 TRP   A CA    1 1 
ATOM   1392 C  C     . TRP   A 1 204 ? 39.163 -13.681 -7.612  1    50.48  ? 204 TRP   A C     1 1 
ATOM   1393 O  O     . TRP   A 1 204 ? 39.429 -13.045 -6.597  1    50.91  ? 204 TRP   A O     1 1 
ATOM   1394 C  CB    . TRP   A 1 204 ? 37.503 -12.307 -8.967  1    49.24  ? 204 TRP   A CB    1 1 
ATOM   1395 C  CG    . TRP   A 1 204 ? 37.42  -11.242 -10.026 1    49.83  ? 204 TRP   A CG    1 1 
ATOM   1396 C  CD1   . TRP   A 1 204 ? 36.692 -11.289 -11.18  1    50.72  ? 204 TRP   A CD1   1 1 
ATOM   1397 C  CD2   . TRP   A 1 204 ? 38.134 -9.996  -10.052 1    49.78  ? 204 TRP   A CD2   1 1 
ATOM   1398 N  NE1   . TRP   A 1 204 ? 36.878 -10.135 -11.903 1    50.96  ? 204 TRP   A NE1   1 1 
ATOM   1399 C  CE2   . TRP   A 1 204 ? 37.773 -9.332  -11.243 1    50.77  ? 204 TRP   A CE2   1 1 
ATOM   1400 C  CE3   . TRP   A 1 204 ? 39.078 -9.399  -9.204  1    50.56  ? 204 TRP   A CE3   1 1 
ATOM   1401 C  CZ2   . TRP   A 1 204 ? 38.286 -8.077  -11.584 1    51.7   ? 204 TRP   A CZ2   1 1 
ATOM   1402 C  CZ3   . TRP   A 1 204 ? 39.575 -8.148  -9.533  1    52.05  ? 204 TRP   A CZ3   1 1 
ATOM   1403 C  CH2   . TRP   A 1 204 ? 39.184 -7.501  -10.715 1    52.1   ? 204 TRP   A CH2   1 1 
ATOM   1404 N  N     . VAL   A 1 205 ? 39.165 -15.023 -7.644  1    50.2   ? 205 VAL   A N     1 1 
ATOM   1405 C  CA    . VAL   A 1 205 ? 39.545 -15.833 -6.493  1    50.9   ? 205 VAL   A CA    1 1 
ATOM   1406 C  C     . VAL   A 1 205 ? 41.057 -15.6   -6.249  1    52.44  ? 205 VAL   A C     1 1 
ATOM   1407 O  O     . VAL   A 1 205 ? 41.448 -15.331 -5.12   1    52.3   ? 205 VAL   A O     1 1 
ATOM   1408 C  CB    . VAL   A 1 205 ? 39.228 -17.338 -6.72   1    51.19  ? 205 VAL   A CB    1 1 
ATOM   1409 C  CG1   . VAL   A 1 205 ? 40.078 -18.248 -5.819  1    51.46  ? 205 VAL   A CG1   1 1 
ATOM   1410 C  CG2   . VAL   A 1 205 ? 37.742 -17.627 -6.532  1    51.23  ? 205 VAL   A CG2   1 1 
ATOM   1411 N  N     . ASP   A 1 206 ? 41.897 -15.656 -7.313  1    53.54  ? 206 ASP   A N     1 1 
ATOM   1412 C  CA    . ASP   A 1 206 ? 43.347 -15.437 -7.155  1    54.86  ? 206 ASP   A CA    1 1 
ATOM   1413 C  C     . ASP   A 1 206 ? 43.638 -14.038 -6.591  1    54.6   ? 206 ASP   A C     1 1 
ATOM   1414 O  O     . ASP   A 1 206 ? 44.506 -13.892 -5.738  1    54.93  ? 206 ASP   A O     1 1 
ATOM   1415 C  CB    . ASP   A 1 206 ? 44.107 -15.684 -8.469  1    58.21  ? 206 ASP   A CB    1 1 
ATOM   1416 C  CG    . ASP   A 1 206 ? 45.605 -15.429 -8.374  1    69.12  ? 206 ASP   A CG    1 1 
ATOM   1417 O  OD1   . ASP   A 1 206 ? 46.35  -16.374 -8.005  1    71.72  ? 206 ASP   A OD1   1 1 
ATOM   1418 O  OD2   . ASP   A 1 206 ? 46.04  -14.28  -8.675  1    73.38  ? 206 ASP   A OD2   1 1 
ATOM   1419 N  N     . PHE   A 1 207 ? 42.893 -13.028 -7.038  1    53.89  ? 207 PHE   A N     1 1 
ATOM   1420 C  CA    . PHE   A 1 207 ? 43.048 -11.667 -6.553  1    53.97  ? 207 PHE   A CA    1 1 
ATOM   1421 C  C     . PHE   A 1 207 ? 42.652 -11.552 -5.074  1    54.68  ? 207 PHE   A C     1 1 
ATOM   1422 O  O     . PHE   A 1 207 ? 43.384 -10.935 -4.302  1    55.49  ? 207 PHE   A O     1 1 
ATOM   1423 C  CB    . PHE   A 1 207 ? 42.202 -10.718 -7.411  1    53.74  ? 207 PHE   A CB    1 1 
ATOM   1424 C  CG    . PHE   A 1 207 ? 42.04  -9.318  -6.867  1    54.26  ? 207 PHE   A CG    1 1 
ATOM   1425 C  CD1   . PHE   A 1 207 ? 42.998 -8.35   -7.107  1    55.42  ? 207 PHE   A CD1   1 1 
ATOM   1426 C  CD2   . PHE   A 1 207 ? 40.914 -8.966  -6.143  1    54.86  ? 207 PHE   A CD2   1 1 
ATOM   1427 C  CE1   . PHE   A 1 207 ? 42.831 -7.053  -6.637  1    55.92  ? 207 PHE   A CE1   1 1 
ATOM   1428 C  CE2   . PHE   A 1 207 ? 40.756 -7.677  -5.661  1    55.66  ? 207 PHE   A CE2   1 1 
ATOM   1429 C  CZ    . PHE   A 1 207 ? 41.712 -6.726  -5.918  1    55.58  ? 207 PHE   A CZ    1 1 
ATOM   1430 N  N     . ALA   A 1 208 ? 41.483 -12.102 -4.689  1    53.97  ? 208 ALA   A N     1 1 
ATOM   1431 C  CA    . ALA   A 1 208 ? 41.013 -12.034 -3.315  1    53.62  ? 208 ALA   A CA    1 1 
ATOM   1432 C  C     . ALA   A 1 208 ? 41.902 -12.856 -2.373  1    53.81  ? 208 ALA   A C     1 1 
ATOM   1433 O  O     . ALA   A 1 208 ? 42.23  -12.377 -1.298  1    53.72  ? 208 ALA   A O     1 1 
ATOM   1434 C  CB    . ALA   A 1 208 ? 39.559 -12.482 -3.222  1    53.07  ? 208 ALA   A CB    1 1 
ATOM   1435 N  N     . ARG   A 1 209 ? 42.33  -14.055 -2.78   1    54.35  ? 209 ARG   A N     1 1 
ATOM   1436 C  CA    . ARG   A 1 209 ? 43.216 -14.891 -1.955  1    55.69  ? 209 ARG   A CA    1 1 
ATOM   1437 C  C     . ARG   A 1 209 ? 44.514 -14.168 -1.631  1    57.75  ? 209 ARG   A C     1 1 
ATOM   1438 O  O     . ARG   A 1 209 ? 44.976 -14.266 -0.504  1    58.43  ? 209 ARG   A O     1 1 
ATOM   1439 C  CB    . ARG   A 1 209 ? 43.519 -16.252 -2.604  1    56     ? 209 ARG   A CB    1 1 
ATOM   1440 C  CG    . ARG   A 1 209 ? 42.317 -17.182 -2.595  1    59.97  ? 209 ARG   A CG    1 1 
ATOM   1441 C  CD    . ARG   A 1 209 ? 42.646 -18.637 -2.872  1    63.34  ? 209 ARG   A CD    1 1 
ATOM   1442 N  NE    . ARG   A 1 209 ? 43.111 -19.313 -1.661  1    66.82  ? 209 ARG   A NE    1 1 
ATOM   1443 C  CZ    . ARG   A 1 209 ? 44.274 -19.95  -1.559  1    69.94  ? 209 ARG   A CZ    1 1 
ATOM   1444 N  NH1   . ARG   A 1 209 ? 45.088 -20.031 -2.604  1    70.26  ? 209 ARG   A NH1   1 1 
ATOM   1445 N  NH2   . ARG   A 1 209 ? 44.626 -20.521 -0.415  1    70.01  ? 209 ARG   A NH2   1 1 
ATOM   1446 N  N     . ARG   A 1 210 ? 45.076 -13.414 -2.593  1    58.37  ? 210 ARG   A N     1 1 
ATOM   1447 C  CA    . ARG   A 1 210 ? 46.302 -12.657 -2.361  1    59.7   ? 210 ARG   A CA    1 1 
ATOM   1448 C  C     . ARG   A 1 210 ? 46.092 -11.53  -1.344  1    59.47  ? 210 ARG   A C     1 1 
ATOM   1449 O  O     . ARG   A 1 210 ? 46.92  -11.374 -0.451  1    59.7   ? 210 ARG   A O     1 1 
ATOM   1450 C  CB    . ARG   A 1 210 ? 46.88  -12.118 -3.677  1    62.54  ? 210 ARG   A CB    1 1 
ATOM   1451 C  CG    . ARG   A 1 210 ? 47.444 -13.222 -4.55   1    68.73  ? 210 ARG   A CG    1 1 
ATOM   1452 C  CD    . ARG   A 1 210 ? 47.688 -12.775 -5.979  1    75.67  ? 210 ARG   A CD    1 1 
ATOM   1453 N  NE    . ARG   A 1 210 ? 48.966 -13.292 -6.466  1    82.9   ? 210 ARG   A NE    1 1 
ATOM   1454 C  CZ    . ARG   A 1 210 ? 49.338 -13.306 -7.74   1    87.49  ? 210 ARG   A CZ    1 1 
ATOM   1455 N  NH1   . ARG   A 1 210 ? 50.531 -13.774 -8.083  1    87.04  ? 210 ARG   A NH1   1 1 
ATOM   1456 N  NH2   . ARG   A 1 210 ? 48.527 -12.835 -8.682  1    88.86  ? 210 ARG   A NH2   1 1 
ATOM   1457 N  N     . LEU   A 1 211 ? 44.983 -10.762 -1.453  1    58.65  ? 211 LEU   A N     1 1 
ATOM   1458 C  CA    . LEU   A 1 211 ? 44.71  -9.687  -0.494  1    58.53  ? 211 LEU   A CA    1 1 
ATOM   1459 C  C     . LEU   A 1 211 ? 44.554 -10.252 0.924   1    58.37  ? 211 LEU   A C     1 1 
ATOM   1460 O  O     . LEU   A 1 211 ? 45.121 -9.719  1.873   1    58.29  ? 211 LEU   A O     1 1 
ATOM   1461 C  CB    . LEU   A 1 211 ? 43.435 -8.923  -0.878  1    58.73  ? 211 LEU   A CB    1 1 
ATOM   1462 C  CG    . LEU   A 1 211 ? 43.547 -7.942  -2.043  1    60.39  ? 211 LEU   A CG    1 1 
ATOM   1463 C  CD1   . LEU   A 1 211 ? 42.207 -7.298  -2.324  1    60.51  ? 211 LEU   A CD1   1 1 
ATOM   1464 C  CD2   . LEU   A 1 211 ? 44.589 -6.873  -1.761  1    60.76  ? 211 LEU   A CD2   1 1 
ATOM   1465 N  N     . CYS   A 1 212 ? 43.815 -11.362 1.041   1    58.1   ? 212 CYS   A N     1 1 
ATOM   1466 C  CA    . CYS   A 1 212 ? 43.529 -12.073 2.279   1    58.25  ? 212 CYS   A CA    1 1 
ATOM   1467 C  C     . CYS   A 1 212 ? 44.807 -12.682 2.91    1    58.92  ? 212 CYS   A C     1 1 
ATOM   1468 O  O     . CYS   A 1 212 ? 45.006 -12.553 4.116   1    58.38  ? 212 CYS   A O     1 1 
ATOM   1469 C  CB    . CYS   A 1 212 ? 42.469 -13.137 2.015   1    58.33  ? 212 CYS   A CB    1 1 
ATOM   1470 S  SG    . CYS   A 1 212 ? 41.953 -14.049 3.482   1    59.4   ? 212 CYS   A SG    1 1 
ATOM   1471 N  N     . GLU   A 1 213 ? 45.672 -13.319 2.099   1    59.84  ? 213 GLU   A N     1 1 
ATOM   1472 C  CA    . GLU   A 1 213 ? 46.94  -13.886 2.579   1    61.54  ? 213 GLU   A CA    1 1 
ATOM   1473 C  C     . GLU   A 1 213 ? 47.854 -12.784 3.113   1    62.55  ? 213 GLU   A C     1 1 
ATOM   1474 O  O     . GLU   A 1 213 ? 48.551 -13.003 4.085   1    62.69  ? 213 GLU   A O     1 1 
ATOM   1475 C  CB    . GLU   A 1 213 ? 47.671 -14.658 1.469   1    65.1   ? 213 GLU   A CB    1 1 
ATOM   1476 C  CG    . GLU   A 1 213 ? 47.114 -16.048 1.222   1    74.1   ? 213 GLU   A CG    1 1 
ATOM   1477 C  CD    . GLU   A 1 213 ? 47.679 -16.772 0.012   1    84.4   ? 213 GLU   A CD    1 1 
ATOM   1478 O  OE1   . GLU   A 1 213 ? 48.118 -16.09  -0.943  1    86.49  ? 213 GLU   A OE1   1 1 
ATOM   1479 O  OE2   . GLU   A 1 213 ? 47.669 -18.025 0.015   1    87.61  ? 213 GLU   A OE2   1 1 
ATOM   1480 N  N     . HIS   A 1 214 ? 47.834 -11.605 2.504   1    63.47  ? 214 HIS   A N     1 1 
ATOM   1481 C  CA    . HIS   A 1 214 ? 48.642 -10.471 2.941   1    65.26  ? 214 HIS   A CA    1 1 
ATOM   1482 C  C     . HIS   A 1 214 ? 48.252 -9.972  4.344   1    65.18  ? 214 HIS   A C     1 1 
ATOM   1483 O  O     . HIS   A 1 214 ? 49.115 -9.533  5.097   1    65.67  ? 214 HIS   A O     1 1 
ATOM   1484 C  CB    . HIS   A 1 214 ? 48.524 -9.324  1.917   1    67.6   ? 214 HIS   A CB    1 1 
ATOM   1485 C  CG    . HIS   A 1 214 ? 49.453 -8.182  2.172   1    72.44  ? 214 HIS   A CG    1 1 
ATOM   1486 N  ND1   . HIS   A 1 214 ? 48.989 -6.875  2.252   1    75.48  ? 214 HIS   A ND1   1 1 
ATOM   1487 C  CD2   . HIS   A 1 214 ? 50.793 -8.182  2.366   1    74.34  ? 214 HIS   A CD2   1 1 
ATOM   1488 C  CE1   . HIS   A 1 214 ? 50.058 -6.124  2.487   1    76.08  ? 214 HIS   A CE1   1 1 
ATOM   1489 N  NE2   . HIS   A 1 214 ? 51.167 -6.867  2.566   1    75.93  ? 214 HIS   A NE2   1 1 
ATOM   1490 N  N     . LYS   A 1 215 ? 46.96  -10.031 4.691   1    64.34  ? 215 LYS   A N     1 1 
ATOM   1491 C  CA    . LYS   A 1 215 ? 46.465 -9.562  5.982   1    63.69  ? 215 LYS   A CA    1 1 
ATOM   1492 C  C     . LYS   A 1 215 ? 46.45  -10.646 7.071   1    62.64  ? 215 LYS   A C     1 1 
ATOM   1493 O  O     . LYS   A 1 215 ? 46.757 -10.359 8.228   1    63.2   ? 215 LYS   A O     1 1 
ATOM   1494 C  CB    . LYS   A 1 215 ? 45.066 -8.971  5.795   1    65.87  ? 215 LYS   A CB    1 1 
ATOM   1495 C  CG    . LYS   A 1 215 ? 44.372 -8.49   7.067   1    71.46  ? 215 LYS   A CG    1 1 
ATOM   1496 C  CD    . LYS   A 1 215 ? 43.039 -7.841  6.699   1    77.58  ? 215 LYS   A CD    1 1 
ATOM   1497 C  CE    . LYS   A 1 215 ? 42.204 -7.374  7.871   1    82.44  ? 215 LYS   A CE    1 1 
ATOM   1498 N  NZ    . LYS   A 1 215 ? 40.851 -6.908  7.418   1    84.96  ? 215 LYS   A NZ    1 1 
ATOM   1499 N  N     . TYR   A 1 216 ? 46.104 -11.884 6.713   1    61.04  ? 216 TYR   A N     1 1 
ATOM   1500 C  CA    . TYR   A 1 216 ? 45.96  -12.953 7.694   1    59.64  ? 216 TYR   A CA    1 1 
ATOM   1501 C  C     . TYR   A 1 216 ? 47.006 -14.047 7.668   1    59.81  ? 216 TYR   A C     1 1 
ATOM   1502 O  O     . TYR   A 1 216 ? 46.971 -14.904 8.545   1    60.69  ? 216 TYR   A O     1 1 
ATOM   1503 C  CB    . TYR   A 1 216 ? 44.576 -13.608 7.572   1    58.23  ? 216 TYR   A CB    1 1 
ATOM   1504 C  CG    . TYR   A 1 216 ? 43.416 -12.66  7.759   1    57.17  ? 216 TYR   A CG    1 1 
ATOM   1505 C  CD1   . TYR   A 1 216 ? 42.939 -12.353 9.029   1    57.22  ? 216 TYR   A CD1   1 1 
ATOM   1506 C  CD2   . TYR   A 1 216 ? 42.739 -12.135 6.667   1    57.15  ? 216 TYR   A CD2   1 1 
ATOM   1507 C  CE1   . TYR   A 1 216 ? 41.86  -11.494 9.206   1    57.42  ? 216 TYR   A CE1   1 1 
ATOM   1508 C  CE2   . TYR   A 1 216 ? 41.661 -11.275 6.831   1    57.45  ? 216 TYR   A CE2   1 1 
ATOM   1509 C  CZ    . TYR   A 1 216 ? 41.218 -10.963 8.101   1    58.14  ? 216 TYR   A CZ    1 1 
ATOM   1510 O  OH    . TYR   A 1 216 ? 40.139 -10.128 8.249   1    59.32  ? 216 TYR   A OH    1 1 
ATOM   1511 N  N     . GLY   A 1 217 ? 47.872 -14.076 6.664   1    59.16  ? 217 GLY   A N     1 1 
ATOM   1512 C  CA    . GLY   A 1 217 ? 48.884 -15.129 6.561   1    59.15  ? 217 GLY   A CA    1 1 
ATOM   1513 C  C     . GLY   A 1 217 ? 48.423 -16.374 5.815   1    59.08  ? 217 GLY   A C     1 1 
ATOM   1514 O  O     . GLY   A 1 217 ? 49.229 -17.257 5.511   1    59.87  ? 217 GLY   A O     1 1 
ATOM   1515 N  N     . ASN   A 1 218 ? 47.117 -16.474 5.538   1    57.7   ? 218 ASN   A N     1 1 
ATOM   1516 C  CA    . ASN   A 1 218 ? 46.493 -17.565 4.787   1    56.82  ? 218 ASN   A CA    1 1 
ATOM   1517 C  C     . ASN   A 1 218 ? 45.15  -17.081 4.231   1    55.44  ? 218 ASN   A C     1 1 
ATOM   1518 O  O     . ASN   A 1 218 ? 44.674 -15.997 4.581   1    55.24  ? 218 ASN   A O     1 1 
ATOM   1519 C  CB    . ASN   A 1 218 ? 46.307 -18.839 5.655   1    58.09  ? 218 ASN   A CB    1 1 
ATOM   1520 C  CG    . ASN   A 1 218 ? 46.029 -20.117 4.856   1    60.23  ? 218 ASN   A CG    1 1 
ATOM   1521 O  OD1   . ASN   A 1 218 ? 46.53  -20.31  3.736   1    61.02  ? 218 ASN   A OD1   1 1 
ATOM   1522 N  ND2   . ASN   A 1 218 ? 45.232 -21.027 5.415   1    60.33  ? 218 ASN   A ND2   1 1 
ATOM   1523 N  N     . ALA   A 1 219 ? 44.557 -17.871 3.34    1    54.4   ? 219 ALA   A N     1 1 
ATOM   1524 C  CA    . ALA   A 1 219 ? 43.273 -17.59  2.709   1    53.29  ? 219 ALA   A CA    1 1 
ATOM   1525 C  C     . ALA   A 1 219 ? 42.587 -18.925 2.458   1    52.4   ? 219 ALA   A C     1 1 
ATOM   1526 O  O     . ALA   A 1 219 ? 43.247 -19.944 2.185   1    51.98  ? 219 ALA   A O     1 1 
ATOM   1527 C  CB    . ALA   A 1 219 ? 43.485 -16.862 1.383   1    53.07  ? 219 ALA   A CB    1 1 
ATOM   1528 N  N     . PRO   A 1 220 ? 41.247 -18.943 2.528   1    51.67  ? 220 PRO   A N     1 1 
ATOM   1529 C  CA    . PRO   A 1 220 ? 40.53  -20.193 2.269   1    51.75  ? 220 PRO   A CA    1 1 
ATOM   1530 C  C     . PRO   A 1 220 ? 40.71  -20.664 0.833   1    52.78  ? 220 PRO   A C     1 1 
ATOM   1531 O  O     . PRO   A 1 220 ? 40.826 -19.84  -0.081  1    53.05  ? 220 PRO   A O     1 1 
ATOM   1532 C  CB    . PRO   A 1 220 ? 39.065 -19.817 2.51    1    51.83  ? 220 PRO   A CB    1 1 
ATOM   1533 C  CG    . PRO   A 1 220 ? 39.096 -18.542 3.247   1    51.99  ? 220 PRO   A CG    1 1 
ATOM   1534 C  CD    . PRO   A 1 220 ? 40.324 -17.839 2.847   1    50.73  ? 220 PRO   A CD    1 1 
ATOM   1535 N  N     . ARG   A 1 221 ? 40.706 -21.982 0.627   1    53.11  ? 221 ARG   A N     1 1 
ATOM   1536 C  CA    . ARG   A 1 221 ? 40.728 -22.533 -0.725  1    54.45  ? 221 ARG   A CA    1 1 
ATOM   1537 C  C     . ARG   A 1 221 ? 39.312 -22.342 -1.293  1    53.58  ? 221 ARG   A C     1 1 
ATOM   1538 O  O     . ARG   A 1 221 ? 38.332 -22.315 -0.542  1    53.24  ? 221 ARG   A O     1 1 
ATOM   1539 C  CB    . ARG   A 1 221 ? 41.05  -24.038 -0.724  1    58.43  ? 221 ARG   A CB    1 1 
ATOM   1540 C  CG    . ARG   A 1 221 ? 42.532 -24.364 -0.544  1    66.52  ? 221 ARG   A CG    1 1 
ATOM   1541 C  CD    . ARG   A 1 221 ? 42.955 -25.456 -1.517  1    73.18  ? 221 ARG   A CD    1 1 
ATOM   1542 N  NE    . ARG   A 1 221 ? 44.297 -25.979 -1.251  1    78.46  ? 221 ARG   A NE    1 1 
ATOM   1543 C  CZ    . ARG   A 1 221 ? 45.415 -25.485 -1.774  1    82.15  ? 221 ARG   A CZ    1 1 
ATOM   1544 N  NH1   . ARG   A 1 221 ? 45.371 -24.427 -2.578  1    82.09  ? 221 ARG   A NH1   1 1 
ATOM   1545 N  NH2   . ARG   A 1 221 ? 46.587 -26.033 -1.484  1    82.49  ? 221 ARG   A NH2   1 1 
ATOM   1546 N  N     . VAL   A 1 222 ? 39.212 -22.184 -2.608  1    52.44  ? 222 VAL   A N     1 1 
ATOM   1547 C  CA    . VAL   A 1 222 ? 37.93  -22.03  -3.246  1    51.82  ? 222 VAL   A CA    1 1 
ATOM   1548 C  C     . VAL   A 1 222 ? 37.69  -23.189 -4.173  1    52.26  ? 222 VAL   A C     1 1 
ATOM   1549 O  O     . VAL   A 1 222 ? 38.528 -23.475 -5.022  1    53.05  ? 222 VAL   A O     1 1 
ATOM   1550 C  CB    . VAL   A 1 222 ? 37.789 -20.677 -3.962  1    51.82  ? 222 VAL   A CB    1 1 
ATOM   1551 C  CG1   . VAL   A 1 222 ? 36.4   -20.533 -4.569  1    51.97  ? 222 VAL   A CG1   1 1 
ATOM   1552 C  CG2   . VAL   A 1 222 ? 38.08  -19.525 -3.003  1    52.12  ? 222 VAL   A CG2   1 1 
ATOM   1553 N  N     . ARG   A 1 223 ? 36.583 -23.9   -3.981  1    51.63  ? 223 ARG   A N     1 1 
ATOM   1554 C  CA    . ARG   A 1 223 ? 36.206 -24.976 -4.877  1    51.5   ? 223 ARG   A CA    1 1 
ATOM   1555 C  C     . ARG   A 1 223 ? 35.092 -24.431 -5.748  1    51.24  ? 223 ARG   A C     1 1 
ATOM   1556 O  O     . ARG   A 1 223 ? 34.187 -23.752 -5.256  1    51.39  ? 223 ARG   A O     1 1 
ATOM   1557 C  CB    . ARG   A 1 223 ? 35.67  -26.192 -4.11   1    53.13  ? 223 ARG   A CB    1 1 
ATOM   1558 C  CG    . ARG   A 1 223 ? 36.675 -26.816 -3.161  1    57.14  ? 223 ARG   A CG    1 1 
ATOM   1559 C  CD    . ARG   A 1 223 ? 36.358 -28.259 -2.813  1    60.7   ? 223 ARG   A CD    1 1 
ATOM   1560 N  NE    . ARG   A 1 223 ? 34.948 -28.492 -2.484  1    64.66  ? 223 ARG   A NE    1 1 
ATOM   1561 C  CZ    . ARG   A 1 223 ? 34.442 -28.443 -1.256  1    67.36  ? 223 ARG   A CZ    1 1 
ATOM   1562 N  NH1   . ARG   A 1 223 ? 35.217 -28.135 -0.22   1    66.3   ? 223 ARG   A NH1   1 1 
ATOM   1563 N  NH2   . ARG   A 1 223 ? 33.156 -28.695 -1.053  1    67.75  ? 223 ARG   A NH2   1 1 
ATOM   1564 N  N     . ILE   A 1 224 ? 35.146 -24.725 -7.035  1    50.61  ? 224 ILE   A N     1 1 
ATOM   1565 C  CA    . ILE   A 1 224 ? 34.117 -24.299 -7.966  1    50.3   ? 224 ILE   A CA    1 1 
ATOM   1566 C  C     . ILE   A 1 224 ? 33.461 -25.556 -8.509  1    50.18  ? 224 ILE   A C     1 1 
ATOM   1567 O  O     . ILE   A 1 224 ? 34.163 -26.458 -8.954  1    50.28  ? 224 ILE   A O     1 1 
ATOM   1568 C  CB    . ILE   A 1 224 ? 34.733 -23.44  -9.086  1    50.93  ? 224 ILE   A CB    1 1 
ATOM   1569 C  CG1   . ILE   A 1 224 ? 35.515 -22.24  -8.484  1    51.5   ? 224 ILE   A CG1   1 1 
ATOM   1570 C  CG2   . ILE   A 1 224 ? 33.65  -22.987 -10.073 1    51.48  ? 224 ILE   A CG2   1 1 
ATOM   1571 C  CD1   . ILE   A 1 224 ? 36.298 -21.409 -9.495  1    52.59  ? 224 ILE   A CD1   1 1 
ATOM   1572 N  N     . ASN   A 1 225 ? 32.13  -25.649 -8.413  1    49.33  ? 225 ASN   A N     1 1 
ATOM   1573 C  CA    . ASN   A 1 225 ? 31.381 -26.798 -8.919  1    48.83  ? 225 ASN   A CA    1 1 
ATOM   1574 C  C     . ASN   A 1 225 ? 30.17  -26.345 -9.761  1    48.34  ? 225 ASN   A C     1 1 
ATOM   1575 O  O     . ASN   A 1 225 ? 29.969 -25.145 -9.948  1    49.16  ? 225 ASN   A O     1 1 
ATOM   1576 C  CB    . ASN   A 1 225 ? 31.014 -27.785 -7.781  1    49.43  ? 225 ASN   A CB    1 1 
ATOM   1577 C  CG    . ASN   A 1 225 ? 30.156 -27.239 -6.655  1    52.57  ? 225 ASN   A CG    1 1 
ATOM   1578 O  OD1   . ASN   A 1 225 ? 29.156 -26.553 -6.867  1    54.23  ? 225 ASN   A OD1   1 1 
ATOM   1579 N  ND2   . ASN   A 1 225 ? 30.506 -27.566 -5.417  1    52.37  ? 225 ASN   A ND2   1 1 
ATOM   1580 N  N     . GLY   A 1 226 ? 29.414 -27.288 -10.299 1    47.38  ? 226 GLY   A N     1 1 
ATOM   1581 C  CA    . GLY   A 1 226 ? 28.244 -27.003 -11.111 1    47.84  ? 226 GLY   A CA    1 1 
ATOM   1582 C  C     . GLY   A 1 226 ? 28.588 -26.977 -12.584 1    48.8   ? 226 GLY   A C     1 1 
ATOM   1583 O  O     . GLY   A 1 226 ? 29.387 -27.794 -13.051 1    49.04  ? 226 GLY   A O     1 1 
ATOM   1584 N  N     . HIS   A 1 227 ? 28.013 -26.014 -13.325 1    48.3   ? 227 HIS   A N     1 1 
ATOM   1585 C  CA    . HIS   A 1 227 ? 28.267 -25.876 -14.745 1    47.91  ? 227 HIS   A CA    1 1 
ATOM   1586 C  C     . HIS   A 1 227 ? 29.593 -25.187 -15.03  1    48.33  ? 227 HIS   A C     1 1 
ATOM   1587 O  O     . HIS   A 1 227 ? 29.615 -24.115 -15.633 1    48.45  ? 227 HIS   A O     1 1 
ATOM   1588 C  CB    . HIS   A 1 227 ? 27.091 -25.194 -15.46  1    47.97  ? 227 HIS   A CB    1 1 
ATOM   1589 C  CG    . HIS   A 1 227 ? 25.814 -25.973 -15.357 1    49.5   ? 227 HIS   A CG    1 1 
ATOM   1590 N  ND1   . HIS   A 1 227 ? 24.586 -25.341 -15.213 1    50.91  ? 227 HIS   A ND1   1 1 
ATOM   1591 C  CD2   . HIS   A 1 227 ? 25.618 -27.312 -15.333 1    50.15  ? 227 HIS   A CD2   1 1 
ATOM   1592 C  CE1   . HIS   A 1 227 ? 23.686 -26.306 -15.135 1    51.19  ? 227 HIS   A CE1   1 1 
ATOM   1593 N  NE2   . HIS   A 1 227 ? 24.257 -27.511 -15.2   1    51.05  ? 227 HIS   A NE2   1 1 
ATOM   1594 N  N     . VAL   A 1 228 ? 30.702 -25.831 -14.638 1    48.65  ? 228 VAL   A N     1 1 
ATOM   1595 C  CA    . VAL   A 1 228 ? 32.064 -25.352 -14.825 1    49.89  ? 228 VAL   A CA    1 1 
ATOM   1596 C  C     . VAL   A 1 228 ? 32.464 -25.238 -16.3   1    51.83  ? 228 VAL   A C     1 1 
ATOM   1597 O  O     . VAL   A 1 228 ? 33.413 -24.514 -16.608 1    52.38  ? 228 VAL   A O     1 1 
ATOM   1598 C  CB    . VAL   A 1 228 ? 33.078 -26.221 -14.042 1    50.59  ? 228 VAL   A CB    1 1 
ATOM   1599 C  CG1   . VAL   A 1 228 ? 32.841 -26.12  -12.541 1    51.32  ? 228 VAL   A CG1   1 1 
ATOM   1600 C  CG2   . VAL   A 1 228 ? 33.021 -27.676 -14.491 1    50     ? 228 VAL   A CG2   1 1 
ATOM   1601 N  N     . ALA   A 1 229 ? 31.759 -25.929 -17.219 1    52.28  ? 229 ALA   A N     1 1 
ATOM   1602 C  CA    . ALA   A 1 229 ? 32.093 -25.847 -18.646 1    53.21  ? 229 ALA   A CA    1 1 
ATOM   1603 C  C     . ALA   A 1 229 ? 31.216 -24.84  -19.442 1    53.62  ? 229 ALA   A C     1 1 
ATOM   1604 O  O     . ALA   A 1 229 ? 31.387 -24.7   -20.662 1    53.62  ? 229 ALA   A O     1 1 
ATOM   1605 C  CB    . ALA   A 1 229 ? 32.015 -27.237 -19.283 1    53.65  ? 229 ALA   A CB    1 1 
ATOM   1606 N  N     . ALA   A 1 230 ? 30.293 -24.136 -18.76  1    53.5   ? 230 ALA   A N     1 1 
ATOM   1607 C  CA    . ALA   A 1 230 ? 29.404 -23.195 -19.437 1    53.82  ? 230 ALA   A CA    1 1 
ATOM   1608 C  C     . ALA   A 1 230 ? 30.158 -22.083 -20.16  1    54.05  ? 230 ALA   A C     1 1 
ATOM   1609 O  O     . ALA   A 1 230 ? 31.19  -21.608 -19.685 1    53.77  ? 230 ALA   A O     1 1 
ATOM   1610 C  CB    . ALA   A 1 230 ? 28.393 -22.606 -18.459 1    53.67  ? 230 ALA   A CB    1 1 
ATOM   1611 N  N     . ARG   A 1 231 ? 29.646 -21.708 -21.335 1    53.96  ? 231 ARG   A N     1 1 
ATOM   1612 C  CA    . ARG   A 1 231 ? 30.187 -20.645 -22.17  1    54.01  ? 231 ARG   A CA    1 1 
ATOM   1613 C  C     . ARG   A 1 231 ? 29.028 -20.008 -22.905 1    53.14  ? 231 ARG   A C     1 1 
ATOM   1614 O  O     . ARG   A 1 231 ? 28.223 -20.703 -23.511 1    52.87  ? 231 ARG   A O     1 1 
ATOM   1615 C  CB    . ARG   A 1 231 ? 31.274 -21.157 -23.128 1    56.19  ? 231 ARG   A CB    1 1 
ATOM   1616 C  CG    . ARG   A 1 231 ? 32.674 -21.011 -22.541 1    60.92  ? 231 ARG   A CG    1 1 
ATOM   1617 C  CD    . ARG   A 1 231 ? 33.752 -21.541 -23.464 1    66.23  ? 231 ARG   A CD    1 1 
ATOM   1618 N  NE    . ARG   A 1 231 ? 34.95  -20.706 -23.391 1    72.03  ? 231 ARG   A NE    1 1 
ATOM   1619 C  CZ    . ARG   A 1 231 ? 35.996 -20.956 -22.61  1    75.27  ? 231 ARG   A CZ    1 1 
ATOM   1620 N  NH1   . ARG   A 1 231 ? 36.03  -22.056 -21.868 1    75.59  ? 231 ARG   A NH1   1 1 
ATOM   1621 N  NH2   . ARG   A 1 231 ? 37.027 -20.122 -22.585 1    75.35  ? 231 ARG   A NH2   1 1 
ATOM   1622 N  N     . PHE   A 1 232 ? 28.919 -18.688 -22.817 1    52.59  ? 232 PHE   A N     1 1 
ATOM   1623 C  CA    . PHE   A 1 232 ? 27.807 -17.964 -23.415 1    52.53  ? 232 PHE   A CA    1 1 
ATOM   1624 C  C     . PHE   A 1 232 ? 28.191 -16.494 -23.608 1    54.18  ? 232 PHE   A C     1 1 
ATOM   1625 O  O     . PHE   A 1 232 ? 29.101 -15.993 -22.935 1    54.37  ? 232 PHE   A O     1 1 
ATOM   1626 C  CB    . PHE   A 1 232 ? 26.549 -18.091 -22.487 1    51.57  ? 232 PHE   A CB    1 1 
ATOM   1627 C  CG    . PHE   A 1 232 ? 26.826 -17.906 -21.006 1    51.25  ? 232 PHE   A CG    1 1 
ATOM   1628 C  CD1   . PHE   A 1 232 ? 26.948 -16.64  -20.459 1    51.17  ? 232 PHE   A CD1   1 1 
ATOM   1629 C  CD2   . PHE   A 1 232 ? 27.008 -18.999 -20.175 1    51.52  ? 232 PHE   A CD2   1 1 
ATOM   1630 C  CE1   . PHE   A 1 232 ? 27.259 -16.473 -19.121 1    51.82  ? 232 PHE   A CE1   1 1 
ATOM   1631 C  CE2   . PHE   A 1 232 ? 27.331 -18.827 -18.838 1    51.87  ? 232 PHE   A CE2   1 1 
ATOM   1632 C  CZ    . PHE   A 1 232 ? 27.444 -17.566 -18.316 1    51.68  ? 232 PHE   A CZ    1 1 
ATOM   1633 N  N     . PRO   A 1 233 ? 27.469 -15.754 -24.472 1    55.12  ? 233 PRO   A N     1 1 
ATOM   1634 C  CA    . PRO   A 1 233 ? 27.749 -14.317 -24.612 1    55.18  ? 233 PRO   A CA    1 1 
ATOM   1635 C  C     . PRO   A 1 233 ? 27.419 -13.585 -23.32  1    55.34  ? 233 PRO   A C     1 1 
ATOM   1636 O  O     . PRO   A 1 233 ? 26.376 -13.835 -22.718 1    55.83  ? 233 PRO   A O     1 1 
ATOM   1637 C  CB    . PRO   A 1 233 ? 26.807 -13.878 -25.737 1    56.08  ? 233 PRO   A CB    1 1 
ATOM   1638 C  CG    . PRO   A 1 233 ? 26.432 -15.146 -26.448 1    56.72  ? 233 PRO   A CG    1 1 
ATOM   1639 C  CD    . PRO   A 1 233 ? 26.368 -16.172 -25.358 1    54.91  ? 233 PRO   A CD    1 1 
ATOM   1640 N  N     . PHE   A 1 234 ? 28.304 -12.685 -22.885 1    54.7   ? 234 PHE   A N     1 1 
ATOM   1641 C  CA    . PHE   A 1 234 ? 28.109 -11.958 -21.64  1    54.19  ? 234 PHE   A CA    1 1 
ATOM   1642 C  C     . PHE   A 1 234 ? 29.033 -10.762 -21.536 1    53.57  ? 234 PHE   A C     1 1 
ATOM   1643 O  O     . PHE   A 1 234 ? 30.128 -10.787 -22.075 1    53.58  ? 234 PHE   A O     1 1 
ATOM   1644 C  CB    . PHE   A 1 234 ? 28.386 -12.901 -20.457 1    54.28  ? 234 PHE   A CB    1 1 
ATOM   1645 C  CG    . PHE   A 1 234 ? 27.533 -12.67  -19.233 1    55.38  ? 234 PHE   A CG    1 1 
ATOM   1646 C  CD1   . PHE   A 1 234 ? 26.189 -13.003 -19.233 1    56.17  ? 234 PHE   A CD1   1 1 
ATOM   1647 C  CD2   . PHE   A 1 234 ? 28.085 -12.165 -18.067 1    56.41  ? 234 PHE   A CD2   1 1 
ATOM   1648 C  CE1   . PHE   A 1 234 ? 25.415 -12.834 -18.093 1    57     ? 234 PHE   A CE1   1 1 
ATOM   1649 C  CE2   . PHE   A 1 234 ? 27.313 -12.012 -16.922 1    57.11  ? 234 PHE   A CE2   1 1 
ATOM   1650 C  CZ    . PHE   A 1 234 ? 25.981 -12.342 -16.945 1    56.9   ? 234 PHE   A CZ    1 1 
ATOM   1651 N  N     . ILE   A 1 235 ? 28.631 -9.742  -20.778 1    53.52  ? 235 ILE   A N     1 1 
ATOM   1652 C  CA    . ILE   A 1 235 ? 29.476 -8.572  -20.532 1    53.66  ? 235 ILE   A CA    1 1 
ATOM   1653 C  C     . ILE   A 1 235 ? 30.187 -8.791  -19.196 1    54.06  ? 235 ILE   A C     1 1 
ATOM   1654 O  O     . ILE   A 1 235 ? 29.535 -8.727  -18.166 1    54.51  ? 235 ILE   A O     1 1 
ATOM   1655 C  CB    . ILE   A 1 235 ? 28.617 -7.274  -20.492 1    53.54  ? 235 ILE   A CB    1 1 
ATOM   1656 C  CG1   . ILE   A 1 235 ? 27.869 -7.07   -21.816 1    54.49  ? 235 ILE   A CG1   1 1 
ATOM   1657 C  CG2   . ILE   A 1 235 ? 29.459 -6.046  -20.115 1    53.19  ? 235 ILE   A CG2   1 1 
ATOM   1658 C  CD1   . ILE   A 1 235 ? 26.884 -5.94   -21.81  1    55.89  ? 235 ILE   A CD1   1 1 
ATOM   1659 N  N     . PRO   A 1 236 ? 31.518 -9.001  -19.175 1    54     ? 236 PRO   A N     1 1 
ATOM   1660 C  CA    . PRO   A 1 236 ? 32.203 -9.231  -17.891 1    53.86  ? 236 PRO   A CA    1 1 
ATOM   1661 C  C     . PRO   A 1 236 ? 32.207 -8.092  -16.868 1    53.92  ? 236 PRO   A C     1 1 
ATOM   1662 O  O     . PRO   A 1 236 ? 32.264 -8.378  -15.681 1    53.99  ? 236 PRO   A O     1 1 
ATOM   1663 C  CB    . PRO   A 1 236 ? 33.648 -9.561  -18.311 1    54.29  ? 236 PRO   A CB    1 1 
ATOM   1664 C  CG    . PRO   A 1 236 ? 33.787 -9.101  -19.693 1    54.15  ? 236 PRO   A CG    1 1 
ATOM   1665 C  CD    . PRO   A 1 236 ? 32.446 -9.137  -20.319 1    53.03  ? 236 PRO   A CD    1 1 
ATOM   1666 N  N     . MET   A 1 237 ? 32.22  -6.828  -17.312 1    53.82  ? 237 MET   A N     1 1 
ATOM   1667 C  CA    . MET   A 1 237 ? 32.347 -5.63   -16.46  1    54.21  ? 237 MET   A CA    1 1 
ATOM   1668 C  C     . MET   A 1 237 ? 31.598 -5.679  -15.104 1    54.1   ? 237 MET   A C     1 1 
ATOM   1669 O  O     . MET   A 1 237 ? 32.27  -5.497  -14.094 1    54.55  ? 237 MET   A O     1 1 
ATOM   1670 C  CB    . MET   A 1 237 ? 31.989 -4.344  -17.222 1    55.06  ? 237 MET   A CB    1 1 
ATOM   1671 C  CG    . MET   A 1 237 ? 32.293 -3.093  -16.445 1    58.51  ? 237 MET   A CG    1 1 
ATOM   1672 S  SD    . MET   A 1 237 ? 32.463 -1.632  -17.501 1    67.22  ? 237 MET   A SD    1 1 
ATOM   1673 C  CE    . MET   A 1 237 ? 31.754 -0.484  -16.456 1    65.66  ? 237 MET   A CE    1 1 
ATOM   1674 N  N     . PRO   A 1 238 ? 30.273 -5.913  -15.01  1    53.62  ? 238 PRO   A N     1 1 
ATOM   1675 C  CA    . PRO   A 1 238 ? 29.639 -5.964  -13.682 1    53.54  ? 238 PRO   A CA    1 1 
ATOM   1676 C  C     . PRO   A 1 238 ? 30.158 -7.129  -12.812 1    52.95  ? 238 PRO   A C     1 1 
ATOM   1677 O  O     . PRO   A 1 238 ? 30.297 -6.955  -11.594 1    53.49  ? 238 PRO   A O     1 1 
ATOM   1678 C  CB    . PRO   A 1 238 ? 28.152 -6.1    -14.01  1    54.45  ? 238 PRO   A CB    1 1 
ATOM   1679 C  CG    . PRO   A 1 238 ? 28.128 -6.716  -15.37  1    54.81  ? 238 PRO   A CG    1 1 
ATOM   1680 C  CD    . PRO   A 1 238 ? 29.283 -6.129  -16.084 1    53.08  ? 238 PRO   A CD    1 1 
ATOM   1681 N  N     . LEU   A 1 239 ? 30.484 -8.295  -13.418 1    51.05  ? 239 LEU   A N     1 1 
ATOM   1682 C  CA    . LEU   A 1 239 ? 31.063 -9.408  -12.657 1    50.21  ? 239 LEU   A CA    1 1 
ATOM   1683 C  C     . LEU   A 1 239 ? 32.419 -8.982  -12.046 1    50.18  ? 239 LEU   A C     1 1 
ATOM   1684 O  O     . LEU   A 1 239 ? 32.749 -9.381  -10.93  1    49.8   ? 239 LEU   A O     1 1 
ATOM   1685 C  CB    . LEU   A 1 239 ? 31.261 -10.652 -13.541 1    49.78  ? 239 LEU   A CB    1 1 
ATOM   1686 C  CG    . LEU   A 1 239 ? 29.994 -11.429 -13.876 1    50.94  ? 239 LEU   A CG    1 1 
ATOM   1687 C  CD1   . LEU   A 1 239 ? 30.299 -12.578 -14.862 1    51.36  ? 239 LEU   A CD1   1 1 
ATOM   1688 C  CD2   . LEU   A 1 239 ? 29.315 -11.949 -12.602 1    50.66  ? 239 LEU   A CD2   1 1 
ATOM   1689 N  N     . ASP   A 1 240 ? 33.179 -8.142  -12.784 1    49.79  ? 240 ASP   A N     1 1 
ATOM   1690 C  CA    . ASP   A 1 240 ? 34.445 -7.605  -12.334 1    50.24  ? 240 ASP   A CA    1 1 
ATOM   1691 C  C     . ASP   A 1 240 ? 34.294 -6.721  -11.091 1    50.43  ? 240 ASP   A C     1 1 
ATOM   1692 O  O     . ASP   A 1 240 ? 35.277 -6.562  -10.381 1    51.22  ? 240 ASP   A O     1 1 
ATOM   1693 C  CB    . ASP   A 1 240 ? 35.191 -6.877  -13.46  1    51.54  ? 240 ASP   A CB    1 1 
ATOM   1694 C  CG    . ASP   A 1 240 ? 35.765 -7.785  -14.536 1    54.93  ? 240 ASP   A CG    1 1 
ATOM   1695 O  OD1   . ASP   A 1 240 ? 35.897 -8.999  -14.288 1    54.48  ? 240 ASP   A OD1   1 1 
ATOM   1696 O  OD2   . ASP   A 1 240 ? 36.09  -7.279  -15.614 1    58.56  ? 240 ASP   A OD2   1 1 
ATOM   1697 N  N     . TYR   A 1 241 ? 33.106 -6.158  -10.819 1    49.97  ? 241 TYR   A N     1 1 
ATOM   1698 C  CA    . TYR   A 1 241 ? 32.928 -5.44   -9.565  1    51.21  ? 241 TYR   A CA    1 1 
ATOM   1699 C  C     . TYR   A 1 241 ? 32.384 -6.381  -8.499  1    50.1   ? 241 TYR   A C     1 1 
ATOM   1700 O  O     . TYR   A 1 241 ? 32.932 -6.419  -7.402  1    50.79  ? 241 TYR   A O     1 1 
ATOM   1701 C  CB    . TYR   A 1 241 ? 32.015 -4.217  -9.639  1    52.93  ? 241 TYR   A CB    1 1 
ATOM   1702 C  CG    . TYR   A 1 241 ? 31.862 -3.595  -8.256  1    56.04  ? 241 TYR   A CG    1 1 
ATOM   1703 C  CD1   . TYR   A 1 241 ? 32.876 -2.819  -7.705  1    57.27  ? 241 TYR   A CD1   1 1 
ATOM   1704 C  CD2   . TYR   A 1 241 ? 30.773 -3.909  -7.444  1    57.91  ? 241 TYR   A CD2   1 1 
ATOM   1705 C  CE1   . TYR   A 1 241 ? 32.753 -2.265  -6.437  1    58.46  ? 241 TYR   A CE1   1 1 
ATOM   1706 C  CE2   . TYR   A 1 241 ? 30.64  -3.363  -6.173  1    59.23  ? 241 TYR   A CE2   1 1 
ATOM   1707 C  CZ    . TYR   A 1 241 ? 31.622 -2.515  -5.684  1    60.19  ? 241 TYR   A CZ    1 1 
ATOM   1708 O  OH    . TYR   A 1 241 ? 31.513 -1.98   -4.421  1    62.54  ? 241 TYR   A OH    1 1 
ATOM   1709 N  N     . ILE   A 1 242 ? 31.265 -7.073  -8.798  1    47.32  ? 242 ILE   A N     1 1 
ATOM   1710 C  CA    . ILE   A 1 242 ? 30.575 -7.878  -7.818  1    45.51  ? 242 ILE   A CA    1 1 
ATOM   1711 C  C     . ILE   A 1 242 ? 31.412 -9.004  -7.241  1    44.97  ? 242 ILE   A C     1 1 
ATOM   1712 O  O     . ILE   A 1 242 ? 31.496 -9.12   -6.016  1    45     ? 242 ILE   A O     1 1 
ATOM   1713 C  CB    . ILE   A 1 242 ? 29.233 -8.388  -8.409  1    44.55  ? 242 ILE   A CB    1 1 
ATOM   1714 C  CG1   . ILE   A 1 242 ? 28.348 -7.184  -8.832  1    43.98  ? 242 ILE   A CG1   1 1 
ATOM   1715 C  CG2   . ILE   A 1 242 ? 28.52  -9.293  -7.404  1    43.86  ? 242 ILE   A CG2   1 1 
ATOM   1716 C  CD1   . ILE   A 1 242 ? 27.259 -7.529  -9.814  1    44.34  ? 242 ILE   A CD1   1 1 
ATOM   1717 N  N     . LEU   A 1 243 ? 32.012 -9.838  -8.098  1    44.41  ? 243 LEU   A N     1 1 
ATOM   1718 C  CA    . LEU   A 1 243 ? 32.76  -10.996 -7.629  1    44.73  ? 243 LEU   A CA    1 1 
ATOM   1719 C  C     . LEU   A 1 243 ? 33.847 -10.679 -6.588  1    44.12  ? 243 LEU   A C     1 1 
ATOM   1720 O  O     . LEU   A 1 243 ? 33.762 -11.275 -5.522  1    43.83  ? 243 LEU   A O     1 1 
ATOM   1721 C  CB    . LEU   A 1 243 ? 33.338 -11.844 -8.781  1    45.12  ? 243 LEU   A CB    1 1 
ATOM   1722 C  CG    . LEU   A 1 243 ? 32.311 -12.511 -9.68   1    46.49  ? 243 LEU   A CG    1 1 
ATOM   1723 C  CD1   . LEU   A 1 243 ? 32.994 -13.19  -10.871 1    47.19  ? 243 LEU   A CD1   1 1 
ATOM   1724 C  CD2   . LEU   A 1 243 ? 31.413 -13.464 -8.884  1    46.19  ? 243 LEU   A CD2   1 1 
ATOM   1725 N  N     . PRO   A 1 244 ? 34.839 -9.777  -6.815  1    43.69  ? 244 PRO   A N     1 1 
ATOM   1726 C  CA    . PRO   A 1 244 ? 35.833 -9.518  -5.76   1    43.45  ? 244 PRO   A CA    1 1 
ATOM   1727 C  C     . PRO   A 1 244 ? 35.201 -8.995  -4.484  1    43.85  ? 244 PRO   A C     1 1 
ATOM   1728 O  O     . PRO   A 1 244 ? 35.678 -9.327  -3.409  1    44.98  ? 244 PRO   A O     1 1 
ATOM   1729 C  CB    . PRO   A 1 244 ? 36.769 -8.485  -6.389  1    44.37  ? 244 PRO   A CB    1 1 
ATOM   1730 C  CG    . PRO   A 1 244 ? 35.974 -7.845  -7.456  1    44.76  ? 244 PRO   A CG    1 1 
ATOM   1731 C  CD    . PRO   A 1 244 ? 35.109 -8.948  -8.004  1    43.32  ? 244 PRO   A CD    1 1 
ATOM   1732 N  N     . GLU   A 1 245 ? 34.094 -8.244  -4.592  1    42.78  ? 245 GLU   A N     1 1 
ATOM   1733 C  CA    . GLU   A 1 245 ? 33.408 -7.754  -3.426  1    42.32  ? 245 GLU   A CA    1 1 
ATOM   1734 C  C     . GLU   A 1 245 ? 32.842 -8.892  -2.588  1    43.23  ? 245 GLU   A C     1 1 
ATOM   1735 O  O     . GLU   A 1 245 ? 33.041 -8.905  -1.37   1    43.69  ? 245 GLU   A O     1 1 
ATOM   1736 C  CB    . GLU   A 1 245 ? 32.334 -6.728  -3.806  1    42.92  ? 245 GLU   A CB    1 1 
ATOM   1737 C  CG    . GLU   A 1 245 ? 32.918 -5.406  -4.277  1    45.94  ? 245 GLU   A CG    1 1 
ATOM   1738 C  CD    . GLU   A 1 245 ? 33.936 -4.74   -3.361  1    52.62  ? 245 GLU   A CD    1 1 
ATOM   1739 O  OE1   . GLU   A 1 245 ? 33.724 -4.734  -2.125  1    49.93  ? 245 GLU   A OE1   1 1 
ATOM   1740 O  OE2   . GLU   A 1 245 ? 34.952 -4.224  -3.886  1    57.51  ? 245 GLU   A OE2   1 1 
ATOM   1741 N  N     . LEU   A 1 246 ? 32.158 -9.854  -3.225  1    42.85  ? 246 LEU   A N     1 1 
ATOM   1742 C  CA    . LEU   A 1 246 ? 31.576 -10.973 -2.492  1    43.18  ? 246 LEU   A CA    1 1 
ATOM   1743 C  C     . LEU   A 1 246 ? 32.629 -11.979 -2.014  1    43.13  ? 246 LEU   A C     1 1 
ATOM   1744 O  O     . LEU   A 1 246 ? 32.422 -12.627 -0.987  1    43.18  ? 246 LEU   A O     1 1 
ATOM   1745 C  CB    . LEU   A 1 246 ? 30.488 -11.675 -3.331  1    42.99  ? 246 LEU   A CB    1 1 
ATOM   1746 C  CG    . LEU   A 1 246 ? 29.378 -10.771 -3.879  1    43.54  ? 246 LEU   A CG    1 1 
ATOM   1747 C  CD1   . LEU   A 1 246 ? 28.383 -11.576 -4.695  1    43.73  ? 246 LEU   A CD1   1 1 
ATOM   1748 C  CD2   . LEU   A 1 246 ? 28.666 -10.027 -2.758  1    43.82  ? 246 LEU   A CD2   1 1 
ATOM   1749 N  N     . LEU   A 1 247 ? 33.755 -12.095 -2.746  1    42.35  ? 247 LEU   A N     1 1 
ATOM   1750 C  CA    . LEU   A 1 247 ? 34.862 -12.984 -2.394  1    42.59  ? 247 LEU   A CA    1 1 
ATOM   1751 C  C     . LEU   A 1 247 ? 35.65  -12.432 -1.195  1    43.44  ? 247 LEU   A C     1 1 
ATOM   1752 O  O     . LEU   A 1 247 ? 35.985 -13.183 -0.282  1    43.96  ? 247 LEU   A O     1 1 
ATOM   1753 C  CB    . LEU   A 1 247 ? 35.789 -13.196 -3.595  1    42.47  ? 247 LEU   A CB    1 1 
ATOM   1754 C  CG    . LEU   A 1 247 ? 35.229 -14.136 -4.679  1    43.91  ? 247 LEU   A CG    1 1 
ATOM   1755 C  CD1   . LEU   A 1 247 ? 36.023 -14.015 -5.961  1    43.78  ? 247 LEU   A CD1   1 1 
ATOM   1756 C  CD2   . LEU   A 1 247 ? 35.234 -15.616 -4.214  1    44.56  ? 247 LEU   A CD2   1 1 
ATOM   1757 N  N     . LYS   A 1 248 ? 35.915 -11.122 -1.172  1    43.18  ? 248 LYS   A N     1 1 
ATOM   1758 C  CA    . LYS   A 1 248 ? 36.603 -10.49  -0.049  1    43.32  ? 248 LYS   A CA    1 1 
ATOM   1759 C  C     . LYS   A 1 248 ? 35.787 -10.656 1.24    1    44.13  ? 248 LYS   A C     1 1 
ATOM   1760 O  O     . LYS   A 1 248 ? 36.366 -10.934 2.285   1    45.34  ? 248 LYS   A O     1 1 
ATOM   1761 C  CB    . LYS   A 1 248 ? 36.81  -9.007  -0.332  1    44.6   ? 248 LYS   A CB    1 1 
ATOM   1762 C  CG    . LYS   A 1 248 ? 38.104 -8.71   -1.112  1    48.69  ? 248 LYS   A CG    1 1 
ATOM   1763 C  CD    . LYS   A 1 248 ? 38     -7.451  -2.007  1    52.69  ? 248 LYS   A CD    1 1 
ATOM   1764 C  CE    . LYS   A 1 248 ? 37.344 -6.262  -1.359  1    55.82  ? 248 LYS   A CE    1 1 
ATOM   1765 N  NZ    . LYS   A 1 248 ? 37.299 -5.098  -2.271  1    58.62  ? 248 LYS   A NZ    1 1 
ATOM   1766 N  N     . ASN   A 1 249 ? 34.448 -10.524 1.16    1    43     ? 249 ASN   A N     1 1 
ATOM   1767 C  CA    . ASN   A 1 249 ? 33.563 -10.701 2.304   1    42.98  ? 249 ASN   A CA    1 1 
ATOM   1768 C  C     . ASN   A 1 249 ? 33.593 -12.128 2.861   1    43.39  ? 249 ASN   A C     1 1 
ATOM   1769 O  O     . ASN   A 1 249 ? 33.675 -12.291 4.075   1    43.93  ? 249 ASN   A O     1 1 
ATOM   1770 C  CB    . ASN   A 1 249 ? 32.12  -10.351 1.937   1    43.29  ? 249 ASN   A CB    1 1 
ATOM   1771 C  CG    . ASN   A 1 249 ? 31.871 -8.887  1.731   1    44.56  ? 249 ASN   A CG    1 1 
ATOM   1772 O  OD1   . ASN   A 1 249 ? 32.75  -8.05   1.95    1    45     ? 249 ASN   A OD1   1 1 
ATOM   1773 N  ND2   . ASN   A 1 249 ? 30.668 -8.544  1.272   1    43.4   ? 249 ASN   A ND2   1 1 
ATOM   1774 N  N     . ALA   A 1 250 ? 33.483 -13.146 1.988   1    42.94  ? 250 ALA   A N     1 1 
ATOM   1775 C  CA    . ALA   A 1 250 ? 33.47  -14.545 2.382   1    43.51  ? 250 ALA   A CA    1 1 
ATOM   1776 C  C     . ALA   A 1 250 ? 34.803 -14.93  3.015   1    44.56  ? 250 ALA   A C     1 1 
ATOM   1777 O  O     . ALA   A 1 250 ? 34.805 -15.565 4.058   1    45.17  ? 250 ALA   A O     1 1 
ATOM   1778 C  CB    . ALA   A 1 250 ? 33.182 -15.425 1.173   1    43.31  ? 250 ALA   A CB    1 1 
ATOM   1779 N  N     . MET   A 1 251 ? 35.93  -14.493 2.421   1    44.67  ? 251 MET   A N     1 1 
ATOM   1780 C  CA    . MET   A 1 251 ? 37.281 -14.775 2.93    1    45.46  ? 251 MET   A CA    1 1 
ATOM   1781 C  C     . MET   A 1 251 ? 37.562 -14.1   4.271   1    45.54  ? 251 MET   A C     1 1 
ATOM   1782 O  O     . MET   A 1 251 ? 38.121 -14.74  5.152   1    45.94  ? 251 MET   A O     1 1 
ATOM   1783 C  CB    . MET   A 1 251 ? 38.342 -14.376 1.898   1    45.91  ? 251 MET   A CB    1 1 
ATOM   1784 C  CG    . MET   A 1 251 ? 38.246 -15.207 0.655   1    48.73  ? 251 MET   A CG    1 1 
ATOM   1785 S  SD    . MET   A 1 251 ? 39.657 -15.069 -0.46   1    54.28  ? 251 MET   A SD    1 1 
ATOM   1786 C  CE    . MET   A 1 251 ? 39.168 -16.293 -1.645  1    56.34  ? 251 MET   A CE    1 1 
ATOM   1787 N  N     . ARG   A 1 252 ? 37.156 -12.839 4.439   1    45.18  ? 252 ARG   A N     1 1 
ATOM   1788 C  CA    . ARG   A 1 252 ? 37.343 -12.144 5.704   1    46.24  ? 252 ARG   A CA    1 1 
ATOM   1789 C  C     . ARG   A 1 252 ? 36.525 -12.802 6.802   1    45.56  ? 252 ARG   A C     1 1 
ATOM   1790 O  O     . ARG   A 1 252 ? 37.05  -13.047 7.875   1    45.25  ? 252 ARG   A O     1 1 
ATOM   1791 C  CB    . ARG   A 1 252 ? 36.944 -10.68  5.565   1    49.21  ? 252 ARG   A CB    1 1 
ATOM   1792 C  CG    . ARG   A 1 252 ? 36.941 -9.863  6.865   1    55.5   ? 252 ARG   A CG    1 1 
ATOM   1793 C  CD    . ARG   A 1 252 ? 36.798 -8.361  6.607   1    63.89  ? 252 ARG   A CD    1 1 
ATOM   1794 N  NE    . ARG   A 1 252 ? 36.78  -8.075  5.169   1    72.91  ? 252 ARG   A NE    1 1 
ATOM   1795 C  CZ    . ARG   A 1 252 ? 36.898 -6.88   4.621   1    78.88  ? 252 ARG   A CZ    1 1 
ATOM   1796 N  NH1   . ARG   A 1 252 ? 37.029 -5.798  5.387   1    79.97  ? 252 ARG   A NH1   1 1 
ATOM   1797 N  NH2   . ARG   A 1 252 ? 36.871 -6.746  3.303   1    80.01  ? 252 ARG   A NH2   1 1 
ATOM   1798 N  N     . ALA   A 1 253 ? 35.24  -13.113 6.54    1    45.22  ? 253 ALA   A N     1 1 
ATOM   1799 C  CA    . ALA   A 1 253 ? 34.386 -13.767 7.538   1    44.68  ? 253 ALA   A CA    1 1 
ATOM   1800 C  C     . ALA   A 1 253 ? 34.98  -15.116 7.945   1    45.08  ? 253 ALA   A C     1 1 
ATOM   1801 O  O     . ALA   A 1 253 ? 34.953 -15.475 9.126   1    45.54  ? 253 ALA   A O     1 1 
ATOM   1802 C  CB    . ALA   A 1 253 ? 32.99  -13.97  6.979   1    43.68  ? 253 ALA   A CB    1 1 
ATOM   1803 N  N     . THR   A 1 254 ? 35.542 -15.857 6.967   1    44.42  ? 254 THR   A N     1 1 
ATOM   1804 C  CA    . THR   A 1 254 ? 36.154 -17.139 7.264   1    44.66  ? 254 THR   A CA    1 1 
ATOM   1805 C  C     . THR   A 1 254 ? 37.373 -16.946 8.153   1    45.75  ? 254 THR   A C     1 1 
ATOM   1806 O  O     . THR   A 1 254 ? 37.495 -17.63  9.155   1    46.33  ? 254 THR   A O     1 1 
ATOM   1807 C  CB    . THR   A 1 254 ? 36.517 -17.867 5.975   1    45.28  ? 254 THR   A CB    1 1 
ATOM   1808 O  OG1   . THR   A 1 254 ? 35.342 -18.024 5.156   1    45.83  ? 254 THR   A OG1   1 1 
ATOM   1809 C  CG2   . THR   A 1 254 ? 37.175 -19.204 6.244   1    45.67  ? 254 THR   A CG2   1 1 
ATOM   1810 N  N     . MET   A 1 255 ? 38.254 -15.996 7.825   1    46.5   ? 255 MET   A N     1 1 
ATOM   1811 C  CA    . MET   A 1 255 ? 39.47  -15.767 8.623   1    47.43  ? 255 MET   A CA    1 1 
ATOM   1812 C  C     . MET   A 1 255 ? 39.16  -15.255 10.024  1    48.86  ? 255 MET   A C     1 1 
ATOM   1813 O  O     . MET   A 1 255 ? 39.724 -15.758 10.99   1    48.87  ? 255 MET   A O     1 1 
ATOM   1814 C  CB    . MET   A 1 255 ? 40.453 -14.815 7.909   1    47.39  ? 255 MET   A CB    1 1 
ATOM   1815 C  CG    . MET   A 1 255 ? 40.949 -15.32  6.558   1    48.56  ? 255 MET   A CG    1 1 
ATOM   1816 S  SD    . MET   A 1 255 ? 41.455 -17.072 6.435   1    51.1   ? 255 MET   A SD    1 1 
ATOM   1817 C  CE    . MET   A 1 255 ? 42.942 -17.098 7.516   1    48.44  ? 255 MET   A CE    1 1 
ATOM   1818 N  N     . GLU   A 1 256 ? 38.244 -14.281 10.144  1    49.71  ? 256 GLU   A N     1 1 
ATOM   1819 C  CA    . GLU   A 1 256 ? 37.869 -13.684 11.435  1    50.72  ? 256 GLU   A CA    1 1 
ATOM   1820 C  C     . GLU   A 1 256 ? 37.18  -14.655 12.388  1    51.82  ? 256 GLU   A C     1 1 
ATOM   1821 O  O     . GLU   A 1 256 ? 37.127 -14.39  13.595  1    52.99  ? 256 GLU   A O     1 1 
ATOM   1822 C  CB    . GLU   A 1 256 ? 36.969 -12.451 11.233  1    52.63  ? 256 GLU   A CB    1 1 
ATOM   1823 C  CG    . GLU   A 1 256 ? 37.635 -11.269 10.556  1    58.9   ? 256 GLU   A CG    1 1 
ATOM   1824 C  CD    . GLU   A 1 256 ? 38.744 -10.576 11.319  1    71.02  ? 256 GLU   A CD    1 1 
ATOM   1825 O  OE1   . GLU   A 1 256 ? 38.973 -10.9   12.508  1    74.39  ? 256 GLU   A OE1   1 1 
ATOM   1826 O  OE2   . GLU   A 1 256 ? 39.397 -9.697  10.713  1    75.09  ? 256 GLU   A OE2   1 1 
ATOM   1827 N  N     . SER   A 1 257 ? 36.595 -15.732 11.859  1    51.25  ? 257 SER   A N     1 1 
ATOM   1828 C  CA    . SER   A 1 257 ? 35.916 -16.712 12.698  1    51.94  ? 257 SER   A CA    1 1 
ATOM   1829 C  C     . SER   A 1 257 ? 36.759 -17.967 12.942  1    53.12  ? 257 SER   A C     1 1 
ATOM   1830 O  O     . SER   A 1 257 ? 36.241 -18.936 13.489  1    53.56  ? 257 SER   A O     1 1 
ATOM   1831 C  CB    . SER   A 1 257 ? 34.572 -17.098 12.092  1    51.76  ? 257 SER   A CB    1 1 
ATOM   1832 O  OG    . SER   A 1 257 ? 34.791 -17.685 10.825  1    53.25  ? 257 SER   A OG    1 1 
ATOM   1833 N  N     . HIS   A 1 258 ? 38.043 -17.967 12.527  1    53.27  ? 258 HIS   A N     1 1 
ATOM   1834 C  CA    . HIS   A 1 258 ? 38.946 -19.1   12.712  1    53.59  ? 258 HIS   A CA    1 1 
ATOM   1835 C  C     . HIS   A 1 258 ? 40.332 -18.567 13.094  1    55.24  ? 258 HIS   A C     1 1 
ATOM   1836 O  O     . HIS   A 1 258 ? 41.336 -19.077 12.606  1    55.48  ? 258 HIS   A O     1 1 
ATOM   1837 C  CB    . HIS   A 1 258 ? 39.019 -19.942 11.425  1    52.91  ? 258 HIS   A CB    1 1 
ATOM   1838 C  CG    . HIS   A 1 258 ? 37.731 -20.63  11.085  1    53.2   ? 258 HIS   A CG    1 1 
ATOM   1839 N  ND1   . HIS   A 1 258 ? 36.752 -20.008 10.319  1    54.28  ? 258 HIS   A ND1   1 1 
ATOM   1840 C  CD2   . HIS   A 1 258 ? 37.299 -21.866 11.424  1    53.31  ? 258 HIS   A CD2   1 1 
ATOM   1841 C  CE1   . HIS   A 1 258 ? 35.756 -20.871 10.248  1    54.52  ? 258 HIS   A CE1   1 1 
ATOM   1842 N  NE2   . HIS   A 1 258 ? 36.042 -22.002 10.9    1    54.31  ? 258 HIS   A NE2   1 1 
ATOM   1843 N  N     . LEU   A 1 259 ? 40.39  -17.553 13.981  1    56.13  ? 259 LEU   A N     1 1 
ATOM   1844 C  CA    . LEU   A 1 259 ? 41.646 -16.926 14.387  1    58.09  ? 259 LEU   A CA    1 1 
ATOM   1845 C  C     . LEU   A 1 259 ? 42.628 -17.858 15.13   1    60.23  ? 259 LEU   A C     1 1 
ATOM   1846 O  O     . LEU   A 1 259 ? 43.828 -17.609 15.089  1    60.63  ? 259 LEU   A O     1 1 
ATOM   1847 C  CB    . LEU   A 1 259 ? 41.382 -15.652 15.195  1    58.33  ? 259 LEU   A CB    1 1 
ATOM   1848 C  CG    . LEU   A 1 259 ? 40.716 -14.535 14.391  1    60.26  ? 259 LEU   A CG    1 1 
ATOM   1849 C  CD1   . LEU   A 1 259 ? 40.271 -13.4   15.296  1    61.11  ? 259 LEU   A CD1   1 1 
ATOM   1850 C  CD2   . LEU   A 1 259 ? 41.63  -14.025 13.275  1    60.34  ? 259 LEU   A CD2   1 1 
ATOM   1851 N  N     . ASP   A 1 260 ? 42.138 -18.93  15.764  1    61.57  ? 260 ASP   A N     1 1 
ATOM   1852 C  CA    . ASP   A 1 260 ? 42.996 -19.897 16.453  1    63.43  ? 260 ASP   A CA    1 1 
ATOM   1853 C  C     . ASP   A 1 260 ? 43.683 -20.867 15.471  1    63.34  ? 260 ASP   A C     1 1 
ATOM   1854 O  O     . ASP   A 1 260 ? 44.714 -21.458 15.812  1    64.32  ? 260 ASP   A O     1 1 
ATOM   1855 C  CB    . ASP   A 1 260 ? 42.177 -20.731 17.448  1    67.86  ? 260 ASP   A CB    1 1 
ATOM   1856 C  CG    . ASP   A 1 260 ? 41.594 -19.961 18.619  1    78.68  ? 260 ASP   A CG    1 1 
ATOM   1857 O  OD1   . ASP   A 1 260 ? 42.096 -18.844 18.913  1    81.12  ? 260 ASP   A OD1   1 1 
ATOM   1858 O  OD2   . ASP   A 1 260 ? 40.645 -20.478 19.253  1    82.75  ? 260 ASP   A OD2   1 1 
ATOM   1859 N  N     . THR   A 1 261 ? 43.083 -21.096 14.29   1    61.71  ? 261 THR   A N     1 1 
ATOM   1860 C  CA    . THR   A 1 261 ? 43.643 -22.02  13.307  1    60.53  ? 261 THR   A CA    1 1 
ATOM   1861 C  C     . THR   A 1 261 ? 43.704 -21.366 11.916  1    59.51  ? 261 THR   A C     1 1 
ATOM   1862 O  O     . THR   A 1 261 ? 43.06  -21.861 10.992  1    59.92  ? 261 THR   A O     1 1 
ATOM   1863 C  CB    . THR   A 1 261 ? 42.826 -23.334 13.297  1    61.16  ? 261 THR   A CB    1 1 
ATOM   1864 O  OG1   . THR   A 1 261 ? 41.497 -23.072 12.83   1    62.13  ? 261 THR   A OG1   1 1 
ATOM   1865 C  CG2   . THR   A 1 261 ? 42.772 -24.003 14.649  1    61.25  ? 261 THR   A CG2   1 1 
ATOM   1866 N  N     . PRO   A 1 262 ? 44.44  -20.244 11.729  1    58.3   ? 262 PRO   A N     1 1 
ATOM   1867 C  CA    . PRO   A 1 262 ? 44.467 -19.602 10.394  1    57.15  ? 262 PRO   A CA    1 1 
ATOM   1868 C  C     . PRO   A 1 262 ? 45.068 -20.462 9.287   1    56.62  ? 262 PRO   A C     1 1 
ATOM   1869 O  O     . PRO   A 1 262 ? 44.789 -20.228 8.122   1    56.48  ? 262 PRO   A O     1 1 
ATOM   1870 C  CB    . PRO   A 1 262 ? 45.266 -18.314 10.621  1    57.8   ? 262 PRO   A CB    1 1 
ATOM   1871 C  CG    . PRO   A 1 262 ? 46.111 -18.599 11.814  1    58.69  ? 262 PRO   A CG    1 1 
ATOM   1872 C  CD    . PRO   A 1 262 ? 45.307 -19.53  12.691  1    57.65  ? 262 PRO   A CD    1 1 
ATOM   1873 N  N     . TYR   A 1 263 ? 45.848 -21.48  9.66    1    56.22  ? 263 TYR   A N     1 1 
ATOM   1874 C  CA    . TYR   A 1 263 ? 46.487 -22.445 8.768   1    56.58  ? 263 TYR   A CA    1 1 
ATOM   1875 C  C     . TYR   A 1 263 ? 45.51  -23.521 8.216   1    56.17  ? 263 TYR   A C     1 1 
ATOM   1876 O  O     . TYR   A 1 263 ? 45.893 -24.303 7.336   1    56.63  ? 263 TYR   A O     1 1 
ATOM   1877 C  CB    . TYR   A 1 263 ? 47.68  -23.134 9.491   1    56.85  ? 263 TYR   A CB    1 1 
ATOM   1878 C  CG    . TYR   A 1 263 ? 47.341 -23.563 10.904  1    58.14  ? 263 TYR   A CG    1 1 
ATOM   1879 C  CD1   . TYR   A 1 263 ? 46.532 -24.666 11.141  1    58.94  ? 263 TYR   A CD1   1 1 
ATOM   1880 C  CD2   . TYR   A 1 263 ? 47.738 -22.802 11.996  1    59.39  ? 263 TYR   A CD2   1 1 
ATOM   1881 C  CE1   . TYR   A 1 263 ? 46.152 -25.019 12.429  1    60.11  ? 263 TYR   A CE1   1 1 
ATOM   1882 C  CE2   . TYR   A 1 263 ? 47.371 -23.15  13.29   1    60.35  ? 263 TYR   A CE2   1 1 
ATOM   1883 C  CZ    . TYR   A 1 263 ? 46.565 -24.251 13.5    1    61.39  ? 263 TYR   A CZ    1 1 
ATOM   1884 O  OH    . TYR   A 1 263 ? 46.209 -24.608 14.777  1    63.34  ? 263 TYR   A OH    1 1 
ATOM   1885 N  N     . ASN   A 1 264 ? 44.292 -23.613 8.774   1    54.88  ? 264 ASN   A N     1 1 
ATOM   1886 C  CA    . ASN   A 1 264 ? 43.336 -24.63  8.348   1    54.61  ? 264 ASN   A CA    1 1 
ATOM   1887 C  C     . ASN   A 1 264 ? 41.954 -24.069 8.539   1    54.05  ? 264 ASN   A C     1 1 
ATOM   1888 O  O     . ASN   A 1 264 ? 41.377 -24.19  9.617   1    55.03  ? 264 ASN   A O     1 1 
ATOM   1889 C  CB    . ASN   A 1 264 ? 43.5   -25.921 9.163   1    55.74  ? 264 ASN   A CB    1 1 
ATOM   1890 C  CG    . ASN   A 1 264 ? 42.581 -27.065 8.752   1    59.9   ? 264 ASN   A CG    1 1 
ATOM   1891 O  OD1   . ASN   A 1 264 ? 41.934 -27.047 7.69    1    61.54  ? 264 ASN   A OD1   1 1 
ATOM   1892 N  ND2   . ASN   A 1 264 ? 42.509 -28.102 9.586   1    59.69  ? 264 ASN   A ND2   1 1 
ATOM   1893 N  N     . VAL   A 1 265 ? 41.44  -23.417 7.519   1    52.4   ? 265 VAL   A N     1 1 
ATOM   1894 C  CA    . VAL   A 1 265 ? 40.109 -22.82  7.563   1    51.32  ? 265 VAL   A CA    1 1 
ATOM   1895 C  C     . VAL   A 1 265 ? 39.209 -23.517 6.519   1    50.54  ? 265 VAL   A C     1 1 
ATOM   1896 O  O     . VAL   A 1 265 ? 39.703 -24.047 5.514   1    50.7   ? 265 VAL   A O     1 1 
ATOM   1897 C  CB    . VAL   A 1 265 ? 40.215 -21.292 7.327   1    51.51  ? 265 VAL   A CB    1 1 
ATOM   1898 C  CG1   . VAL   A 1 265 ? 41.084 -20.63  8.39    1    51.77  ? 265 VAL   A CG1   1 1 
ATOM   1899 C  CG2   . VAL   A 1 265 ? 40.759 -20.99  5.94    1    51.99  ? 265 VAL   A CG2   1 1 
ATOM   1900 N  N     . PRO   A 1 266 ? 37.881 -23.532 6.727   1    49.38  ? 266 PRO   A N     1 1 
ATOM   1901 C  CA    . PRO   A 1 266 ? 37.002 -24.174 5.733   1    48.41  ? 266 PRO   A CA    1 1 
ATOM   1902 C  C     . PRO   A 1 266 ? 37.047 -23.501 4.364   1    48.16  ? 266 PRO   A C     1 1 
ATOM   1903 O  O     . PRO   A 1 266 ? 37.268 -22.293 4.252   1    48.2   ? 266 PRO   A O     1 1 
ATOM   1904 C  CB    . PRO   A 1 266 ? 35.605 -24.106 6.356   1    48.99  ? 266 PRO   A CB    1 1 
ATOM   1905 C  CG    . PRO   A 1 266 ? 35.752 -23.48  7.674   1    49.72  ? 266 PRO   A CG    1 1 
ATOM   1906 C  CD    . PRO   A 1 266 ? 37.128 -22.944 7.848   1    48.51  ? 266 PRO   A CD    1 1 
ATOM   1907 N  N     . ASP   A 1 267 ? 36.875 -24.301 3.312   1    47.83  ? 267 ASP   A N     1 1 
ATOM   1908 C  CA    . ASP   A 1 267 ? 36.86  -23.786 1.955   1    47.75  ? 267 ASP   A CA    1 1 
ATOM   1909 C  C     . ASP   A 1 267 ? 35.627 -22.914 1.713   1    47.4   ? 267 ASP   A C     1 1 
ATOM   1910 O  O     . ASP   A 1 267 ? 34.583 -23.09  2.355   1    47.73  ? 267 ASP   A O     1 1 
ATOM   1911 C  CB    . ASP   A 1 267 ? 36.764 -24.948 0.956   1    50.11  ? 267 ASP   A CB    1 1 
ATOM   1912 C  CG    . ASP   A 1 267 ? 37.937 -25.9   0.933   1    56.63  ? 267 ASP   A CG    1 1 
ATOM   1913 O  OD1   . ASP   A 1 267 ? 39.011 -25.549 1.505   1    57.59  ? 267 ASP   A OD1   1 1 
ATOM   1914 O  OD2   . ASP   A 1 267 ? 37.79  -26.996 0.356   1    59.08  ? 267 ASP   A OD2   1 1 
ATOM   1915 N  N     . VAL   A 1 268 ? 35.743 -22.01  0.747   1    45.9   ? 268 VAL   A N     1 1 
ATOM   1916 C  CA    . VAL   A 1 268 ? 34.64  -21.227 0.245   1    45.21  ? 268 VAL   A CA    1 1 
ATOM   1917 C  C     . VAL   A 1 268 ? 34.207 -22.017 -0.994  1    45.28  ? 268 VAL   A C     1 1 
ATOM   1918 O  O     . VAL   A 1 268 ? 35.049 -22.392 -1.821  1    45.61  ? 268 VAL   A O     1 1 
ATOM   1919 C  CB    . VAL   A 1 268 ? 35.081 -19.786 -0.1    1    45.18  ? 268 VAL   A CB    1 1 
ATOM   1920 C  CG1   . VAL   A 1 268 ? 34.024 -19.07  -0.936  1    45.42  ? 268 VAL   A CG1   1 1 
ATOM   1921 C  CG2   . VAL   A 1 268 ? 35.399 -19.004 1.169   1    44.9   ? 268 VAL   A CG2   1 1 
ATOM   1922 N  N     . VAL   A 1 269 ? 32.92  -22.368 -1.079  1    44.53  ? 269 VAL   A N     1 1 
ATOM   1923 C  CA    . VAL   A 1 269 ? 32.414 -23.177 -2.177  1    43.95  ? 269 VAL   A CA    1 1 
ATOM   1924 C  C     . VAL   A 1 269 ? 31.527 -22.39  -3.103  1    44.59  ? 269 VAL   A C     1 1 
ATOM   1925 O  O     . VAL   A 1 269 ? 30.473 -21.911 -2.689  1    45.04  ? 269 VAL   A O     1 1 
ATOM   1926 C  CB    . VAL   A 1 269 ? 31.687 -24.44  -1.672  1    43.69  ? 269 VAL   A CB    1 1 
ATOM   1927 C  CG1   . VAL   A 1 269 ? 31.272 -25.329 -2.848  1    43.93  ? 269 VAL   A CG1   1 1 
ATOM   1928 C  CG2   . VAL   A 1 269 ? 32.554 -25.216 -0.669  1    43.35  ? 269 VAL   A CG2   1 1 
ATOM   1929 N  N     . ILE   A 1 270 ? 31.905 -22.321 -4.38   1    44.53  ? 270 ILE   A N     1 1 
ATOM   1930 C  CA    . ILE   A 1 270 ? 31.137 -21.611 -5.391  1    44.7   ? 270 ILE   A CA    1 1 
ATOM   1931 C  C     . ILE   A 1 270 ? 30.447 -22.563 -6.355  1    44.64  ? 270 ILE   A C     1 1 
ATOM   1932 O  O     . ILE   A 1 270 ? 31.089 -23.439 -6.927  1    44.87  ? 270 ILE   A O     1 1 
ATOM   1933 C  CB    . ILE   A 1 270 ? 32.03  -20.591 -6.123  1    45.29  ? 270 ILE   A CB    1 1 
ATOM   1934 C  CG1   . ILE   A 1 270 ? 32.7   -19.637 -5.108  1    46.09  ? 270 ILE   A CG1   1 1 
ATOM   1935 C  CG2   . ILE   A 1 270 ? 31.233 -19.838 -7.197  1    45.62  ? 270 ILE   A CG2   1 1 
ATOM   1936 C  CD1   . ILE   A 1 270 ? 33.604 -18.533 -5.722  1    47.75  ? 270 ILE   A CD1   1 1 
ATOM   1937 N  N     . THR   A 1 271 ? 29.13  -22.398 -6.54   1    44.01  ? 271 THR   A N     1 1 
ATOM   1938 C  CA    . THR   A 1 271 ? 28.388 -23.237 -7.473  1    43.73  ? 271 THR   A CA    1 1 
ATOM   1939 C  C     . THR   A 1 271 ? 27.873 -22.347 -8.605  1    43.2   ? 271 THR   A C     1 1 
ATOM   1940 O  O     . THR   A 1 271 ? 27.292 -21.294 -8.332  1    42.76  ? 271 THR   A O     1 1 
ATOM   1941 C  CB    . THR   A 1 271 ? 27.218 -23.942 -6.764  1    45.04  ? 271 THR   A CB    1 1 
ATOM   1942 O  OG1   . THR   A 1 271 ? 27.714 -24.77  -5.696  1    45.99  ? 271 THR   A OG1   1 1 
ATOM   1943 C  CG2   . THR   A 1 271 ? 26.343 -24.751 -7.732  1    45.02  ? 271 THR   A CG2   1 1 
ATOM   1944 N  N     . ILE   A 1 272 ? 28.068 -22.789 -9.856  1    42.87  ? 272 ILE   A N     1 1 
ATOM   1945 C  CA    . ILE   A 1 272 ? 27.604 -22.116 -11.062 1    43.94  ? 272 ILE   A CA    1 1 
ATOM   1946 C  C     . ILE   A 1 272 ? 26.409 -22.89  -11.603 1    45.12  ? 272 ILE   A C     1 1 
ATOM   1947 O  O     . ILE   A 1 272 ? 26.536 -24.088 -11.843 1    46.11  ? 272 ILE   A O     1 1 
ATOM   1948 C  CB    . ILE   A 1 272 ? 28.718 -22.124 -12.163 1    44.09  ? 272 ILE   A CB    1 1 
ATOM   1949 C  CG1   . ILE   A 1 272 ? 30.009 -21.449 -11.696 1    44.35  ? 272 ILE   A CG1   1 1 
ATOM   1950 C  CG2   . ILE   A 1 272 ? 28.198 -21.489 -13.448 1    44.34  ? 272 ILE   A CG2   1 1 
ATOM   1951 C  CD1   . ILE   A 1 272 ? 31.238 -21.719 -12.666 1    45.74  ? 272 ILE   A CD1   1 1 
ATOM   1952 N  N     . ALA   A 1 273 ? 25.27  -22.238 -11.799 1    44.81  ? 273 ALA   A N     1 1 
ATOM   1953 C  CA    . ALA   A 1 273 ? 24.11  -22.884 -12.403 1    45.73  ? 273 ALA   A CA    1 1 
ATOM   1954 C  C     . ALA   A 1 273 ? 23.777 -22.038 -13.624 1    47.2   ? 273 ALA   A C     1 1 
ATOM   1955 O  O     . ALA   A 1 273 ? 23.594 -20.829 -13.52  1    47.57  ? 273 ALA   A O     1 1 
ATOM   1956 C  CB    . ALA   A 1 273 ? 22.929 -22.919 -11.437 1    45.42  ? 273 ALA   A CB    1 1 
ATOM   1957 N  N     . ASN   A 1 274 ? 23.811 -22.645 -14.784 1    47.98  ? 274 ASN   A N     1 1 
ATOM   1958 C  CA    . ASN   A 1 274 ? 23.534 -21.959 -16.031 1    49.55  ? 274 ASN   A CA    1 1 
ATOM   1959 C  C     . ASN   A 1 274 ? 22.277 -22.543 -16.665 1    50.57  ? 274 ASN   A C     1 1 
ATOM   1960 O  O     . ASN   A 1 274 ? 22.102 -23.771 -16.735 1    51.51  ? 274 ASN   A O     1 1 
ATOM   1961 C  CB    . ASN   A 1 274 ? 24.735 -22.042 -16.976 1    51.12  ? 274 ASN   A CB    1 1 
ATOM   1962 C  CG    . ASN   A 1 274 ? 24.507 -21.318 -18.278 1    55.27  ? 274 ASN   A CG    1 1 
ATOM   1963 O  OD1   . ASN   A 1 274 ? 23.873 -20.263 -18.311 1    56.67  ? 274 ASN   A OD1   1 1 
ATOM   1964 N  ND2   . ASN   A 1 274 ? 25.014 -21.872 -19.377 1    55.82  ? 274 ASN   A ND2   1 1 
ATOM   1965 N  N     . ASN   A 1 275 ? 21.378 -21.665 -17.072 1    50.13  ? 275 ASN   A N     1 1 
ATOM   1966 C  CA    . ASN   A 1 275 ? 20.14  -22.085 -17.729 1    50.2   ? 275 ASN   A CA    1 1 
ATOM   1967 C  C     . ASN   A 1 275 ? 19.774 -21.043 -18.813 1    51.16  ? 275 ASN   A C     1 1 
ATOM   1968 O  O     . ASN   A 1 275 ? 20.538 -20.105 -19.041 1    50.9   ? 275 ASN   A O     1 1 
ATOM   1969 C  CB    . ASN   A 1 275 ? 19.02  -22.32  -16.688 1    49.52  ? 275 ASN   A CB    1 1 
ATOM   1970 C  CG    . ASN   A 1 275 ? 18.678 -21.078 -15.916 1    50.92  ? 275 ASN   A CG    1 1 
ATOM   1971 O  OD1   . ASN   A 1 275 ? 17.971 -20.198 -16.415 1    51.47  ? 275 ASN   A OD1   1 1 
ATOM   1972 N  ND2   . ASN   A 1 275 ? 19.188 -20.962 -14.691 1    50.39  ? 275 ASN   A ND2   1 1 
ATOM   1973 N  N     . ASP   A 1 276 ? 18.629 -21.196 -19.478 1    52.26  ? 276 ASP   A N     1 1 
ATOM   1974 C  CA    . ASP   A 1 276 ? 18.229 -20.281 -20.542 1    53.63  ? 276 ASP   A CA    1 1 
ATOM   1975 C  C     . ASP   A 1 276 ? 17.85  -18.906 -20.08  1    53.1   ? 276 ASP   A C     1 1 
ATOM   1976 O  O     . ASP   A 1 276 ? 18.001 -17.961 -20.841 1    54.44  ? 276 ASP   A O     1 1 
ATOM   1977 C  CB    . ASP   A 1 276 ? 17.096 -20.893 -21.365 1    57.76  ? 276 ASP   A CB    1 1 
ATOM   1978 C  CG    . ASP   A 1 276 ? 17.536 -22.107 -22.163 1    66.74  ? 276 ASP   A CG    1 1 
ATOM   1979 O  OD1   . ASP   A 1 276 ? 18.758 -22.215 -22.469 1    67.83  ? 276 ASP   A OD1   1 1 
ATOM   1980 O  OD2   . ASP   A 1 276 ? 16.663 -22.95  -22.492 1    71.08  ? 276 ASP   A OD2   1 1 
ATOM   1981 N  N     . VAL   A 1 277 ? 17.338 -18.778 -18.865 1    51.5   ? 277 VAL   A N     1 1 
ATOM   1982 C  CA    . VAL   A 1 277 ? 16.897 -17.492 -18.349 1    50.34  ? 277 VAL   A CA    1 1 
ATOM   1983 C  C     . VAL   A 1 277 ? 18.038 -16.722 -17.69  1    49.9   ? 277 VAL   A C     1 1 
ATOM   1984 O  O     . VAL   A 1 277 ? 18.294 -15.577 -18.067 1    50.44  ? 277 VAL   A O     1 1 
ATOM   1985 C  CB    . VAL   A 1 277 ? 15.692 -17.682 -17.388 1    50.4   ? 277 VAL   A CB    1 1 
ATOM   1986 C  CG1   . VAL   A 1 277 ? 15.294 -16.369 -16.721 1    50.6   ? 277 VAL   A CG1   1 1 
ATOM   1987 C  CG2   . VAL   A 1 277 ? 14.508 -18.333 -18.096 1    49.99  ? 277 VAL   A CG2   1 1 
ATOM   1988 N  N     . ASP   A 1 278 ? 18.739 -17.334 -16.723 1    48.88  ? 278 ASP   A N     1 1 
ATOM   1989 C  CA    . ASP   A 1 278 ? 19.789 -16.617 -16     1    48.38  ? 278 ASP   A CA    1 1 
ATOM   1990 C  C     . ASP   A 1 278 ? 21.044 -17.439 -15.69  1    47.64  ? 278 ASP   A C     1 1 
ATOM   1991 O  O     . ASP   A 1 278 ? 21.059 -18.654 -15.852 1    47.7   ? 278 ASP   A O     1 1 
ATOM   1992 C  CB    . ASP   A 1 278 ? 19.192 -16.022 -14.691 1    49.92  ? 278 ASP   A CB    1 1 
ATOM   1993 C  CG    . ASP   A 1 278 ? 18.511 -17.005 -13.737 1    55.83  ? 278 ASP   A CG    1 1 
ATOM   1994 O  OD1   . ASP   A 1 278 ? 18.53  -18.225 -14.014 1    57.35  ? 278 ASP   A OD1   1 1 
ATOM   1995 O  OD2   . ASP   A 1 278 ? 17.965 -16.556 -12.713 1    58.25  ? 278 ASP   A OD2   1 1 
ATOM   1996 N  N     . LEU   A 1 279 ? 22.1   -16.758 -15.237 1    46.79  ? 279 LEU   A N     1 1 
ATOM   1997 C  CA    . LEU   A 1 279 ? 23.316 -17.365 -14.725 1    46.11  ? 279 LEU   A CA    1 1 
ATOM   1998 C  C     . LEU   A 1 279 ? 23.214 -17.176 -13.201 1    45.35  ? 279 LEU   A C     1 1 
ATOM   1999 O  O     . LEU   A 1 279 ? 22.966 -16.058 -12.741 1    45.97  ? 279 LEU   A O     1 1 
ATOM   2000 C  CB    . LEU   A 1 279 ? 24.548 -16.61  -15.242 1    46.29  ? 279 LEU   A CB    1 1 
ATOM   2001 C  CG    . LEU   A 1 279 ? 25.867 -16.925 -14.536 1    47.67  ? 279 LEU   A CG    1 1 
ATOM   2002 C  CD1   . LEU   A 1 279 ? 26.278 -18.378 -14.754 1    47.95  ? 279 LEU   A CD1   1 1 
ATOM   2003 C  CD2   . LEU   A 1 279 ? 26.957 -15.925 -14.915 1    48.21  ? 279 LEU   A CD2   1 1 
ATOM   2004 N  N     . ILE   A 1 280 ? 23.376 -18.249 -12.427 1    43.97  ? 280 ILE   A N     1 1 
ATOM   2005 C  CA    . ILE   A 1 280 ? 23.382 -18.156 -10.974 1    43.65  ? 280 ILE   A CA    1 1 
ATOM   2006 C  C     . ILE   A 1 280 ? 24.743 -18.522 -10.419 1    43.64  ? 280 ILE   A C     1 1 
ATOM   2007 O  O     . ILE   A 1 280 ? 25.254 -19.599 -10.712 1    44.04  ? 280 ILE   A O     1 1 
ATOM   2008 C  CB    . ILE   A 1 280 ? 22.325 -19.056 -10.313 1    43.72  ? 280 ILE   A CB    1 1 
ATOM   2009 C  CG1   . ILE   A 1 280 ? 20.947 -18.854 -10.953 1    45.26  ? 280 ILE   A CG1   1 1 
ATOM   2010 C  CG2   . ILE   A 1 280 ? 22.302 -18.819 -8.794  1    43.63  ? 280 ILE   A CG2   1 1 
ATOM   2011 C  CD1   . ILE   A 1 280 ? 20.297 -20.108 -11.301 1    46.47  ? 280 ILE   A CD1   1 1 
ATOM   2012 N  N     . ILE   A 1 281 ? 25.301 -17.673 -9.561  1    43.08  ? 281 ILE   A N     1 1 
ATOM   2013 C  CA    . ILE   A 1 281 ? 26.546 -17.982 -8.88   1    42.73  ? 281 ILE   A CA    1 1 
ATOM   2014 C  C     . ILE   A 1 281 ? 26.271 -17.926 -7.393  1    42.62  ? 281 ILE   A C     1 1 
ATOM   2015 O  O     . ILE   A 1 281 ? 25.89  -16.88  -6.883  1    43.4   ? 281 ILE   A O     1 1 
ATOM   2016 C  CB    . ILE   A 1 281 ? 27.678 -17.02  -9.289  1    42.81  ? 281 ILE   A CB    1 1 
ATOM   2017 C  CG1   . ILE   A 1 281 ? 27.966 -17.132 -10.806 1    43.44  ? 281 ILE   A CG1   1 1 
ATOM   2018 C  CG2   . ILE   A 1 281 ? 28.929 -17.284 -8.448  1    43.12  ? 281 ILE   A CG2   1 1 
ATOM   2019 C  CD1   . ILE   A 1 281 ? 28.842 -16.011 -11.369 1    44.77  ? 281 ILE   A CD1   1 1 
ATOM   2020 N  N     . ARG   A 1 282 ? 26.406 -19.052 -6.699  1    41.69  ? 282 ARG   A N     1 1 
ATOM   2021 C  CA    . ARG   A 1 282 ? 26.226 -19.096 -5.257  1    41.1   ? 282 ARG   A CA    1 1 
ATOM   2022 C  C     . ARG   A 1 282 ? 27.614 -19.188 -4.59   1    42.02  ? 282 ARG   A C     1 1 
ATOM   2023 O  O     . ARG   A 1 282 ? 28.389 -20.07  -4.928  1    42.75  ? 282 ARG   A O     1 1 
ATOM   2024 C  CB    . ARG   A 1 282 ? 25.339 -20.275 -4.862  1    40.82  ? 282 ARG   A CB    1 1 
ATOM   2025 C  CG    . ARG   A 1 282 ? 25.248 -20.512 -3.356  1    42.47  ? 282 ARG   A CG    1 1 
ATOM   2026 C  CD    . ARG   A 1 282 ? 24.496 -21.795 -3.005  1    43.77  ? 282 ARG   A CD    1 1 
ATOM   2027 N  NE    . ARG   A 1 282 ? 25.226 -23.002 -3.403  1    46.4   ? 282 ARG   A NE    1 1 
ATOM   2028 C  CZ    . ARG   A 1 282 ? 24.664 -24.196 -3.585  1    48.28  ? 282 ARG   A CZ    1 1 
ATOM   2029 N  NH1   . ARG   A 1 282 ? 23.361 -24.358 -3.409  1    46.97  ? 282 ARG   A NH1   1 1 
ATOM   2030 N  NH2   . ARG   A 1 282 ? 25.398 -25.229 -3.973  1    48.58  ? 282 ARG   A NH2   1 1 
ATOM   2031 N  N     . ILE   A 1 283 ? 27.931 -18.285 -3.667  1    42.05  ? 283 ILE   A N     1 1 
ATOM   2032 C  CA    . ILE   A 1 283 ? 29.204 -18.296 -2.958  1    42.91  ? 283 ILE   A CA    1 1 
ATOM   2033 C  C     . ILE   A 1 283 ? 28.874 -18.65  -1.524  1    43.74  ? 283 ILE   A C     1 1 
ATOM   2034 O  O     . ILE   A 1 283 ? 28.219 -17.87  -0.837  1    43.73  ? 283 ILE   A O     1 1 
ATOM   2035 C  CB    . ILE   A 1 283 ? 29.909 -16.915 -3.056  1    43.4   ? 283 ILE   A CB    1 1 
ATOM   2036 C  CG1   . ILE   A 1 283 ? 30.088 -16.51  -4.514  1    44.59  ? 283 ILE   A CG1   1 1 
ATOM   2037 C  CG2   . ILE   A 1 283 ? 31.247 -16.923 -2.319  1    43.74  ? 283 ILE   A CG2   1 1 
ATOM   2038 C  CD1   . ILE   A 1 283 ? 30.581 -15.112 -4.698  1    46.59  ? 283 ILE   A CD1   1 1 
ATOM   2039 N  N     . SER   A 1 284 ? 29.265 -19.857 -1.094  1    44.19  ? 284 SER   A N     1 1 
ATOM   2040 C  CA    . SER   A 1 284 ? 28.954 -20.4   0.235   1    44.61  ? 284 SER   A CA    1 1 
ATOM   2041 C  C     . SER   A 1 284 ? 30.18  -20.469 1.083   1    44.25  ? 284 SER   A C     1 1 
ATOM   2042 O  O     . SER   A 1 284 ? 31.188 -21.069 0.686   1    44.99  ? 284 SER   A O     1 1 
ATOM   2043 C  CB    . SER   A 1 284 ? 28.38  -21.808 0.129   1    46.79  ? 284 SER   A CB    1 1 
ATOM   2044 O  OG    . SER   A 1 284 ? 27.337 -21.852 -0.831  1    51.27  ? 284 SER   A OG    1 1 
ATOM   2045 N  N     . ASP   A 1 285 ? 30.09  -19.904 2.266   1    42.89  ? 285 ASP   A N     1 1 
ATOM   2046 C  CA    . ASP   A 1 285 ? 31.216 -19.915 3.18    1    42.35  ? 285 ASP   A CA    1 1 
ATOM   2047 C  C     . ASP   A 1 285 ? 30.809 -20.529 4.533   1    42.83  ? 285 ASP   A C     1 1 
ATOM   2048 O  O     . ASP   A 1 285 ? 29.628 -20.757 4.81    1    41.98  ? 285 ASP   A O     1 1 
ATOM   2049 C  CB    . ASP   A 1 285 ? 31.768 -18.479 3.347   1    41.35  ? 285 ASP   A CB    1 1 
ATOM   2050 C  CG    . ASP   A 1 285 ? 30.843 -17.533 4.111   1    42.35  ? 285 ASP   A CG    1 1 
ATOM   2051 O  OD1   . ASP   A 1 285 ? 30.503 -17.845 5.295   1    40.34  ? 285 ASP   A OD1   1 1 
ATOM   2052 O  OD2   . ASP   A 1 285 ? 30.488 -16.463 3.549   1    42.97  ? 285 ASP   A OD2   1 1 
ATOM   2053 N  N     . ARG   A 1 286 ? 31.804 -20.76  5.38    1    44     ? 286 ARG   A N     1 1 
ATOM   2054 C  CA    . ARG   A 1 286 ? 31.607 -21.233 6.743   1    45.14  ? 286 ARG   A CA    1 1 
ATOM   2055 C  C     . ARG   A 1 286 ? 32.232 -20.215 7.695   1    45.33  ? 286 ARG   A C     1 1 
ATOM   2056 O  O     . ARG   A 1 286 ? 32.933 -20.586 8.62    1    46.39  ? 286 ARG   A O     1 1 
ATOM   2057 C  CB    . ARG   A 1 286 ? 32.211 -22.627 6.911   1    46.64  ? 286 ARG   A CB    1 1 
ATOM   2058 C  CG    . ARG   A 1 286 ? 31.53  -23.65  6.018   1    50.71  ? 286 ARG   A CG    1 1 
ATOM   2059 C  CD    . ARG   A 1 286 ? 30.896 -24.711 6.855   1    57.21  ? 286 ARG   A CD    1 1 
ATOM   2060 N  NE    . ARG   A 1 286 ? 29.691 -25.25  6.231   1    61.81  ? 286 ARG   A NE    1 1 
ATOM   2061 C  CZ    . ARG   A 1 286 ? 28.938 -26.212 6.757   1    62.36  ? 286 ARG   A CZ    1 1 
ATOM   2062 N  NH1   . ARG   A 1 286 ? 29.244 -26.736 7.935   1    59.43  ? 286 ARG   A NH1   1 1 
ATOM   2063 N  NH2   . ARG   A 1 286 ? 27.872 -26.652 6.11    1    63.75  ? 286 ARG   A NH2   1 1 
ATOM   2064 N  N     . GLY   A 1 287 ? 31.955 -18.942 7.469   1    44.6   ? 287 GLY   A N     1 1 
ATOM   2065 C  CA    . GLY   A 1 287 ? 32.515 -17.875 8.271   1    45.15  ? 287 GLY   A CA    1 1 
ATOM   2066 C  C     . GLY   A 1 287 ? 31.668 -17.373 9.419   1    45.84  ? 287 GLY   A C     1 1 
ATOM   2067 O  O     . GLY   A 1 287 ? 31.851 -16.231 9.836   1    46.68  ? 287 GLY   A O     1 1 
ATOM   2068 N  N     . GLY   A 1 288 ? 30.75  -18.195 9.933   1    45.26  ? 288 GLY   A N     1 1 
ATOM   2069 C  CA    . GLY   A 1 288 ? 29.925 -17.834 11.096  1    44.83  ? 288 GLY   A CA    1 1 
ATOM   2070 C  C     . GLY   A 1 288 ? 28.573 -17.175 10.855  1    44.73  ? 288 GLY   A C     1 1 
ATOM   2071 O  O     . GLY   A 1 288 ? 27.75  -17.073 11.77   1    44.97  ? 288 GLY   A O     1 1 
ATOM   2072 N  N     . GLY   A 1 289 ? 28.331 -16.714 9.634   1    44.09  ? 289 GLY   A N     1 1 
ATOM   2073 C  CA    . GLY   A 1 289 ? 27.064 -16.08  9.285   1    43.4   ? 289 GLY   A CA    1 1 
ATOM   2074 C  C     . GLY   A 1 289 ? 26.967 -14.612 9.642   1    42.76  ? 289 GLY   A C     1 1 
ATOM   2075 O  O     . GLY   A 1 289 ? 27.89  -14.031 10.214  1    41.99  ? 289 GLY   A O     1 1 
ATOM   2076 N  N     . ILE   A 1 290 ? 25.851 -13.993 9.285   1    43.05  ? 290 ILE   A N     1 1 
ATOM   2077 C  CA    . ILE   A 1 290 ? 25.578 -12.585 9.581   1    43.57  ? 290 ILE   A CA    1 1 
ATOM   2078 C  C     . ILE   A 1 290 ? 24.573 -12.62  10.707  1    44.8   ? 290 ILE   A C     1 1 
ATOM   2079 O  O     . ILE   A 1 290 ? 23.5   -13.213 10.543  1    45.16  ? 290 ILE   A O     1 1 
ATOM   2080 C  CB    . ILE   A 1 290 ? 24.979 -11.872 8.35    1    43.59  ? 290 ILE   A CB    1 1 
ATOM   2081 C  CG1   . ILE   A 1 290 ? 25.961 -11.864 7.172   1    43.94  ? 290 ILE   A CG1   1 1 
ATOM   2082 C  CG2   . ILE   A 1 290 ? 24.479 -10.463 8.7     1    43.77  ? 290 ILE   A CG2   1 1 
ATOM   2083 C  CD1   . ILE   A 1 290 ? 25.288 -11.506 5.882   1    44.99  ? 290 ILE   A CD1   1 1 
ATOM   2084 N  N     . ALA   A 1 291 ? 24.924 -12.019 11.85   1    44.98  ? 291 ALA   A N     1 1 
ATOM   2085 C  CA    . ALA   A 1 291 ? 24.106 -12.033 13.053  1    45.65  ? 291 ALA   A CA    1 1 
ATOM   2086 C  C     . ALA   A 1 291 ? 22.742 -11.413 12.857  1    47.08  ? 291 ALA   A C     1 1 
ATOM   2087 O  O     . ALA   A 1 291 ? 22.581 -10.508 12.042  1    47     ? 291 ALA   A O     1 1 
ATOM   2088 C  CB    . ALA   A 1 291 ? 24.841 -11.348 14.194  1    45.35  ? 291 ALA   A CB    1 1 
ATOM   2089 N  N     . HIS   A 1 292 ? 21.75  -11.901 13.614  1    48.08  ? 292 HIS   A N     1 1 
ATOM   2090 C  CA    . HIS   A 1 292 ? 20.381 -11.394 13.557  1    49.49  ? 292 HIS   A CA    1 1 
ATOM   2091 C  C     . HIS   A 1 292 ? 20.304 -9.883  13.782  1    51.64  ? 292 HIS   A C     1 1 
ATOM   2092 O  O     . HIS   A 1 292 ? 19.57  -9.197  13.064  1    51.76  ? 292 HIS   A O     1 1 
ATOM   2093 C  CB    . HIS   A 1 292 ? 19.501 -12.133 14.574  1    49.48  ? 292 HIS   A CB    1 1 
ATOM   2094 C  CG    . HIS   A 1 292 ? 19.057 -13.483 14.109  1    50.29  ? 292 HIS   A CG    1 1 
ATOM   2095 N  ND1   . HIS   A 1 292 ? 19.588 -14.642 14.645  1    52.12  ? 292 HIS   A ND1   1 1 
ATOM   2096 C  CD2   . HIS   A 1 292 ? 18.157 -13.814 13.16   1    50.8   ? 292 HIS   A CD2   1 1 
ATOM   2097 C  CE1   . HIS   A 1 292 ? 18.991 -15.637 14.013  1    52.29  ? 292 HIS   A CE1   1 1 
ATOM   2098 N  NE2   . HIS   A 1 292 ? 18.113 -15.186 13.119  1    52.08  ? 292 HIS   A NE2   1 1 
ATOM   2099 N  N     . LYS   A 1 293 ? 21.075 -9.357  14.749  1    53.13  ? 293 LYS   A N     1 1 
ATOM   2100 C  CA    . LYS   A 1 293 ? 21.076 -7.915  15.017  1    55.61  ? 293 LYS   A CA    1 1 
ATOM   2101 C  C     . LYS   A 1 293 ? 21.685 -7.059  13.871  1    56.7   ? 293 LYS   A C     1 1 
ATOM   2102 O  O     . LYS   A 1 293 ? 21.372 -5.87   13.769  1    57.89  ? 293 LYS   A O     1 1 
ATOM   2103 C  CB    . LYS   A 1 293 ? 21.766 -7.602  16.353  1    58.49  ? 293 LYS   A CB    1 1 
ATOM   2104 C  CG    . LYS   A 1 293 ? 23.233 -7.982  16.371  1    64.6   ? 293 LYS   A CG    1 1 
ATOM   2105 C  CD    . LYS   A 1 293 ? 23.906 -7.579  17.674  1    71.32  ? 293 LYS   A CD    1 1 
ATOM   2106 C  CE    . LYS   A 1 293 ? 25.409 -7.666  17.565  1    76.78  ? 293 LYS   A CE    1 1 
ATOM   2107 N  NZ    . LYS   A 1 293 ? 25.898 -7.029  16.304  1    80.31  ? 293 LYS   A NZ    1 1 
ATOM   2108 N  N     . ASP   A 1 294 ? 22.523 -7.658  13.009  1    55.97  ? 294 ASP   A N     1 1 
ATOM   2109 C  CA    . ASP   A 1 294 ? 23.161 -6.956  11.891  1    55.75  ? 294 ASP   A CA    1 1 
ATOM   2110 C  C     . ASP   A 1 294 ? 22.43  -7.106  10.572  1    55.83  ? 294 ASP   A C     1 1 
ATOM   2111 O  O     . ASP   A 1 294 ? 22.634 -6.293  9.688   1    55.99  ? 294 ASP   A O     1 1 
ATOM   2112 C  CB    . ASP   A 1 294 ? 24.587 -7.485  11.68   1    56.8   ? 294 ASP   A CB    1 1 
ATOM   2113 C  CG    . ASP   A 1 294 ? 25.527 -7.198  12.823  1    62.6   ? 294 ASP   A CG    1 1 
ATOM   2114 O  OD1   . ASP   A 1 294 ? 25.322 -6.184  13.52   1    63.95  ? 294 ASP   A OD1   1 1 
ATOM   2115 O  OD2   . ASP   A 1 294 ? 26.468 -7.99   13.026  1    65.46  ? 294 ASP   A OD2   1 1 
ATOM   2116 N  N     . LEU   A 1 295 ? 21.658 -8.173  10.403  1    56.04  ? 295 LEU   A N     1 1 
ATOM   2117 C  CA    . LEU   A 1 295 ? 20.991 -8.553  9.158   1    57.45  ? 295 LEU   A CA    1 1 
ATOM   2118 C  C     . LEU   A 1 295 ? 20.184 -7.442  8.472   1    58.6   ? 295 LEU   A C     1 1 
ATOM   2119 O  O     . LEU   A 1 295 ? 20.194 -7.317  7.247   1    58.59  ? 295 LEU   A O     1 1 
ATOM   2120 C  CB    . LEU   A 1 295 ? 20.108 -9.789  9.415   1    58.02  ? 295 LEU   A CB    1 1 
ATOM   2121 C  CG    . LEU   A 1 295 ? 19.811 -10.706 8.218   1    60.16  ? 295 LEU   A CG    1 1 
ATOM   2122 C  CD1   . LEU   A 1 295 ? 21.074 -11.071 7.442   1    60.55  ? 295 LEU   A CD1   1 1 
ATOM   2123 C  CD2   . LEU   A 1 295 ? 19.139 -11.956 8.672   1    60.99  ? 295 LEU   A CD2   1 1 
ATOM   2124 N  N     . ASP   A 1 296 ? 19.514 -6.626  9.258   1    59.36  ? 296 ASP   A N     1 1 
ATOM   2125 C  CA    . ASP   A 1 296 ? 18.707 -5.507  8.769   1    60.87  ? 296 ASP   A CA    1 1 
ATOM   2126 C  C     . ASP   A 1 296 ? 19.557 -4.243  8.415   1    59.95  ? 296 ASP   A C     1 1 
ATOM   2127 O  O     . ASP   A 1 296 ? 19     -3.234  7.996   1    60.71  ? 296 ASP   A O     1 1 
ATOM   2128 C  CB    . ASP   A 1 296 ? 17.653 -5.154  9.837   1    65.57  ? 296 ASP   A CB    1 1 
ATOM   2129 C  CG    . ASP   A 1 296 ? 18.247 -5.169  11.246  1    76.23  ? 296 ASP   A CG    1 1 
ATOM   2130 O  OD1   . ASP   A 1 296 ? 18.457 -6.301  11.803  1    77.66  ? 296 ASP   A OD1   1 1 
ATOM   2131 O  OD2   . ASP   A 1 296 ? 18.559 -4.065  11.775  1    80.31  ? 296 ASP   A OD2   1 1 
ATOM   2132 N  N     . ARG   A 1 297 ? 20.886 -4.307  8.555   1    57.97  ? 297 ARG   A N     1 1 
ATOM   2133 C  CA    . ARG   A 1 297 ? 21.756 -3.179  8.264   1    56.48  ? 297 ARG   A CA    1 1 
ATOM   2134 C  C     . ARG   A 1 297 ? 22.854 -3.513  7.258   1    53.57  ? 297 ARG   A C     1 1 
ATOM   2135 O  O     . ARG   A 1 297 ? 23.452 -2.583  6.728   1    53.58  ? 297 ARG   A O     1 1 
ATOM   2136 C  CB    . ARG   A 1 297 ? 22.402 -2.656  9.559   1    58.63  ? 297 ARG   A CB    1 1 
ATOM   2137 C  CG    . ARG   A 1 297 ? 21.459 -1.889  10.468  1    63.8   ? 297 ARG   A CG    1 1 
ATOM   2138 C  CD    . ARG   A 1 297 ? 22.147 -1.503  11.763  1    69.53  ? 297 ARG   A CD    1 1 
ATOM   2139 N  NE    . ARG   A 1 297 ? 22.485 -2.682  12.569  1    75.43  ? 297 ARG   A NE    1 1 
ATOM   2140 C  CZ    . ARG   A 1 297 ? 23.246 -2.652  13.664  1    79.17  ? 297 ARG   A CZ    1 1 
ATOM   2141 N  NH1   . ARG   A 1 297 ? 23.763 -1.504  14.093  1    79.19  ? 297 ARG   A NH1   1 1 
ATOM   2142 N  NH2   . ARG   A 1 297 ? 23.508 -3.772  14.33   1    78.85  ? 297 ARG   A NH2   1 1 
ATOM   2143 N  N     . VAL   A 1 298 ? 23.158 -4.808  7.003   1    50.77  ? 298 VAL   A N     1 1 
ATOM   2144 C  CA    . VAL   A 1 298 ? 24.256 -5.155  6.079   1    48.35  ? 298 VAL   A CA    1 1 
ATOM   2145 C  C     . VAL   A 1 298 ? 24.04  -4.583  4.673   1    46.75  ? 298 VAL   A C     1 1 
ATOM   2146 O  O     . VAL   A 1 298 ? 25.019 -4.321  3.969   1    46.6   ? 298 VAL   A O     1 1 
ATOM   2147 C  CB    . VAL   A 1 298 ? 24.62  -6.673  6.017   1    47.88  ? 298 VAL   A CB    1 1 
ATOM   2148 C  CG1   . VAL   A 1 298 ? 25.189 -7.167  7.335   1    47.8   ? 298 VAL   A CG1   1 1 
ATOM   2149 C  CG2   . VAL   A 1 298 ? 23.432 -7.52   5.575   1    47.96  ? 298 VAL   A CG2   1 1 
ATOM   2150 N  N     . MET   A 1 299 ? 22.776 -4.395  4.258   1    45.53  ? 299 MET   A N     1 1 
ATOM   2151 C  CA    . MET   A 1 299 ? 22.495 -3.836  2.934   1    45.28  ? 299 MET   A CA    1 1 
ATOM   2152 C  C     . MET   A 1 299 ? 22.485 -2.3    2.886   1    45.17  ? 299 MET   A C     1 1 
ATOM   2153 O  O     . MET   A 1 299 ? 22.144 -1.724  1.849   1    45.05  ? 299 MET   A O     1 1 
ATOM   2154 C  CB    . MET   A 1 299 ? 21.203 -4.401  2.335   1    45.69  ? 299 MET   A CB    1 1 
ATOM   2155 C  CG    . MET   A 1 299 ? 21.222 -5.9    2.154   1    48.44  ? 299 MET   A CG    1 1 
ATOM   2156 S  SD    . MET   A 1 299 ? 22.585 -6.555  1.146   1    54.85  ? 299 MET   A SD    1 1 
ATOM   2157 C  CE    . MET   A 1 299 ? 22.382 -5.694  -0.314  1    44.96  ? 299 MET   A CE    1 1 
ATOM   2158 N  N     . ASP   A 1 300 ? 22.843 -1.641  3.993   1    44.97  ? 300 ASP   A N     1 1 
ATOM   2159 C  CA    . ASP   A 1 300 ? 22.928 -0.19   4.056   1    45.35  ? 300 ASP   A CA    1 1 
ATOM   2160 C  C     . ASP   A 1 300 ? 24.307 0.226   3.631   1    44.66  ? 300 ASP   A C     1 1 
ATOM   2161 O  O     . ASP   A 1 300 ? 25.28  -0.375  4.074   1    44.74  ? 300 ASP   A O     1 1 
ATOM   2162 C  CB    . ASP   A 1 300 ? 22.788 0.311   5.5     1    47.77  ? 300 ASP   A CB    1 1 
ATOM   2163 C  CG    . ASP   A 1 300 ? 21.421 0.213   6.108   1    53.92  ? 300 ASP   A CG    1 1 
ATOM   2164 O  OD1   . ASP   A 1 300 ? 20.457 -0.109  5.365   1    54.69  ? 300 ASP   A OD1   1 1 
ATOM   2165 O  OD2   . ASP   A 1 300 ? 21.303 0.461   7.324   1    57.41  ? 300 ASP   A OD2   1 1 
ATOM   2166 N  N     . TYR   A 1 301 ? 24.417 1.339   2.9     1    44     ? 301 TYR   A N     1 1 
ATOM   2167 C  CA    . TYR   A 1 301 ? 25.728 1.889   2.559   1    43.82  ? 301 TYR   A CA    1 1 
ATOM   2168 C  C     . TYR   A 1 301 ? 26.392 2.382   3.837   1    44.31  ? 301 TYR   A C     1 1 
ATOM   2169 O  O     . TYR   A 1 301 ? 25.694 2.818   4.74    1    44.53  ? 301 TYR   A O     1 1 
ATOM   2170 C  CB    . TYR   A 1 301 ? 25.565 3.063   1.591   1    43.41  ? 301 TYR   A CB    1 1 
ATOM   2171 C  CG    . TYR   A 1 301 ? 25.168 2.64    0.194   1    42.84  ? 301 TYR   A CG    1 1 
ATOM   2172 C  CD1   . TYR   A 1 301 ? 26.129 2.291   -0.746  1    43.35  ? 301 TYR   A CD1   1 1 
ATOM   2173 C  CD2   . TYR   A 1 301 ? 23.842 2.657   -0.205  1    42.71  ? 301 TYR   A CD2   1 1 
ATOM   2174 C  CE1   . TYR   A 1 301 ? 25.776 1.945   -2.045  1    43.99  ? 301 TYR   A CE1   1 1 
ATOM   2175 C  CE2   . TYR   A 1 301 ? 23.477 2.325   -1.503  1    43.62  ? 301 TYR   A CE2   1 1 
ATOM   2176 C  CZ    . TYR   A 1 301 ? 24.448 1.968   -2.423  1    44.61  ? 301 TYR   A CZ    1 1 
ATOM   2177 O  OH    . TYR   A 1 301 ? 24.098 1.62    -3.707  1    45.96  ? 301 TYR   A OH    1 1 
ATOM   2178 N  N     . HIS   A 1 302 ? 27.714 2.235   3.947   1    44.91  ? 302 HIS   A N     1 1 
ATOM   2179 C  CA    . HIS   A 1 302 ? 28.508 2.638   5.108   1    46.27  ? 302 HIS   A CA    1 1 
ATOM   2180 C  C     . HIS   A 1 302 ? 28.441 1.646   6.285   1    47.97  ? 302 HIS   A C     1 1 
ATOM   2181 O  O     . HIS   A 1 302 ? 29.25  1.79    7.2     1    48.72  ? 302 HIS   A O     1 1 
ATOM   2182 C  CB    . HIS   A 1 302 ? 28.185 4.074   5.592   1    46.21  ? 302 HIS   A CB    1 1 
ATOM   2183 C  CG    . HIS   A 1 302 ? 28.408 5.127   4.545   1    47.77  ? 302 HIS   A CG    1 1 
ATOM   2184 N  ND1   . HIS   A 1 302 ? 27.346 5.681   3.836   1    48.9   ? 302 HIS   A ND1   1 1 
ATOM   2185 C  CD2   . HIS   A 1 302 ? 29.567 5.675   4.098   1    48.42  ? 302 HIS   A CD2   1 1 
ATOM   2186 C  CE1   . HIS   A 1 302 ? 27.891 6.545   2.991   1    49.29  ? 302 HIS   A CE1   1 1 
ATOM   2187 N  NE2   . HIS   A 1 302 ? 29.222 6.581   3.116   1    49.37  ? 302 HIS   A NE2   1 1 
ATOM   2188 N  N     . PHE   A 1 303 ? 27.501 0.671   6.291   1    48.26  ? 303 PHE   A N     1 1 
ATOM   2189 C  CA    . PHE   A 1 303 ? 27.465 -0.283  7.399   1    49.3   ? 303 PHE   A CA    1 1 
ATOM   2190 C  C     . PHE   A 1 303 ? 28.581 -1.326  7.286   1    50.25  ? 303 PHE   A C     1 1 
ATOM   2191 O  O     . PHE   A 1 303 ? 28.679 -2.048  6.291   1    49.92  ? 303 PHE   A O     1 1 
ATOM   2192 C  CB    . PHE   A 1 303 ? 26.091 -0.938  7.626   1    49.31  ? 303 PHE   A CB    1 1 
ATOM   2193 C  CG    . PHE   A 1 303 ? 26.112 -1.892  8.813   1    50.08  ? 303 PHE   A CG    1 1 
ATOM   2194 C  CD1   . PHE   A 1 303 ? 25.891 -1.431  10.101  1    51.03  ? 303 PHE   A CD1   1 1 
ATOM   2195 C  CD2   . PHE   A 1 303 ? 26.425 -3.23   8.645   1    50.15  ? 303 PHE   A CD2   1 1 
ATOM   2196 C  CE1   . PHE   A 1 303 ? 25.945 -2.298  11.187  1    51.53  ? 303 PHE   A CE1   1 1 
ATOM   2197 C  CE2   . PHE   A 1 303 ? 26.528 -4.08   9.735   1    50.82  ? 303 PHE   A CE2   1 1 
ATOM   2198 C  CZ    . PHE   A 1 303 ? 26.264 -3.617  10.996  1    50.86  ? 303 PHE   A CZ    1 1 
ATOM   2199 N  N     . THR   A 1 304 ? 29.397 -1.423  8.335   1    50.99  ? 304 THR   A N     1 1 
ATOM   2200 C  CA    . THR   A 1 304 ? 30.46  -2.416  8.384   1    52.66  ? 304 THR   A CA    1 1 
ATOM   2201 C  C     . THR   A 1 304 ? 30.698 -2.867  9.82    1    54.69  ? 304 THR   A C     1 1 
ATOM   2202 O  O     . THR   A 1 304 ? 30.483 -2.1    10.751  1    55.74  ? 304 THR   A O     1 1 
ATOM   2203 C  CB    . THR   A 1 304 ? 31.75  -1.852  7.736   1    53.67  ? 304 THR   A CB    1 1 
ATOM   2204 O  OG1   . THR   A 1 304 ? 32.805 -2.801  7.869   1    54.26  ? 304 THR   A OG1   1 1 
ATOM   2205 C  CG2   . THR   A 1 304 ? 32.185 -0.538  8.35    1    53.93  ? 304 THR   A CG2   1 1 
ATOM   2206 N  N     . THR   A 1 305 ? 31.111 -4.114  10.016  1    55.59  ? 305 THR   A N     1 1 
ATOM   2207 C  CA    . THR   A 1 305 ? 31.493 -4.588  11.35   1    56.53  ? 305 THR   A CA    1 1 
ATOM   2208 C  C     . THR   A 1 305 ? 33.021 -4.542  11.537  1    59.37  ? 305 THR   A C     1 1 
ATOM   2209 O  O     . THR   A 1 305 ? 33.514 -4.998  12.568  1    60.39  ? 305 THR   A O     1 1 
ATOM   2210 C  CB    . THR   A 1 305 ? 30.927 -5.96   11.662  1    55.95  ? 305 THR   A CB    1 1 
ATOM   2211 O  OG1   . THR   A 1 305 ? 31.318 -6.858  10.628  1    56.22  ? 305 THR   A OG1   1 1 
ATOM   2212 C  CG2   . THR   A 1 305 ? 29.421 -5.937  11.852  1    55.41  ? 305 THR   A CG2   1 1 
ATOM   2213 N  N     . ALA   A 1 306 ? 33.773 -3.98   10.569  1    60.6   ? 306 ALA   A N     1 1 
ATOM   2214 C  CA    . ALA   A 1 306 ? 35.217 -3.85   10.67   1    62.63  ? 306 ALA   A CA    1 1 
ATOM   2215 C  C     . ALA   A 1 306 ? 35.508 -2.634  11.534  1    64.31  ? 306 ALA   A C     1 1 
ATOM   2216 O  O     . ALA   A 1 306 ? 35.225 -2.65   12.734  1    65.38  ? 306 ALA   A O     1 1 
ATOM   2217 C  CB    . ALA   A 1 306 ? 35.826 -3.66   9.286   1    62.78  ? 306 ALA   A CB    1 1 
ATOM   2218 N  N     . GLY   A 1 335 ? 36.144 -1.967  5.783   1    64.72  ? 335 GLY   A N     1 1 
ATOM   2219 C  CA    . GLY   A 1 335 ? 35.677 -0.812  6.547   1    64.95  ? 335 GLY   A CA    1 1 
ATOM   2220 C  C     . GLY   A 1 335 ? 34.882 0.224   5.763   1    64.62  ? 335 GLY   A C     1 1 
ATOM   2221 O  O     . GLY   A 1 335 ? 34.366 1.194   6.327   1    65.64  ? 335 GLY   A O     1 1 
ATOM   2222 N  N     . PHE   A 1 336 ? 34.755 0.02    4.471   1    63.03  ? 336 PHE   A N     1 1 
ATOM   2223 C  CA    . PHE   A 1 336 ? 34.052 0.92    3.587   1    62.32  ? 336 PHE   A CA    1 1 
ATOM   2224 C  C     . PHE   A 1 336 ? 32.522 0.742   3.698   1    58.22  ? 336 PHE   A C     1 1 
ATOM   2225 O  O     . PHE   A 1 336 ? 31.783 1.726   3.678   1    58.51  ? 336 PHE   A O     1 1 
ATOM   2226 C  CB    . PHE   A 1 336 ? 34.528 0.606   2.169   1    64.71  ? 336 PHE   A CB    1 1 
ATOM   2227 C  CG    . PHE   A 1 336 ? 34.774 1.775   1.272   1    68.08  ? 336 PHE   A CG    1 1 
ATOM   2228 C  CD1   . PHE   A 1 336 ? 35.759 2.7     1.572   1    70.12  ? 336 PHE   A CD1   1 1 
ATOM   2229 C  CD2   . PHE   A 1 336 ? 34.073 1.914   0.083   1    70.29  ? 336 PHE   A CD2   1 1 
ATOM   2230 C  CE1   . PHE   A 1 336 ? 36.01  3.763   0.723   1    71.83  ? 336 PHE   A CE1   1 1 
ATOM   2231 C  CE2   . PHE   A 1 336 ? 34.325 2.976   -0.769  1    71.68  ? 336 PHE   A CE2   1 1 
ATOM   2232 C  CZ    . PHE   A 1 336 ? 35.293 3.892   -0.442  1    71.97  ? 336 PHE   A CZ    1 1 
ATOM   2233 N  N     . GLY   A 1 337 ? 32.061 -0.499  3.785   1    54.19  ? 337 GLY   A N     1 1 
ATOM   2234 C  CA    . GLY   A 1 337 ? 30.634 -0.783  3.864   1    51.69  ? 337 GLY   A CA    1 1 
ATOM   2235 C  C     . GLY   A 1 337 ? 29.838 -0.536  2.589   1    48.64  ? 337 GLY   A C     1 1 
ATOM   2236 O  O     . GLY   A 1 337 ? 28.652 -0.215  2.65    1    47.8   ? 337 GLY   A O     1 1 
ATOM   2237 N  N     . PHE   A 1 338 ? 30.465 -0.697  1.429   1    46.81  ? 338 PHE   A N     1 1 
ATOM   2238 C  CA    . PHE   A 1 338 ? 29.813 -0.48   0.144   1    45.73  ? 338 PHE   A CA    1 1 
ATOM   2239 C  C     . PHE   A 1 338 ? 29.616 -1.748  -0.706  1    44.54  ? 338 PHE   A C     1 1 
ATOM   2240 O  O     . PHE   A 1 338 ? 28.823 -1.715  -1.627  1    45.18  ? 338 PHE   A O     1 1 
ATOM   2241 C  CB    . PHE   A 1 338 ? 30.609 0.554   -0.686  1    45.16  ? 338 PHE   A CB    1 1 
ATOM   2242 C  CG    . PHE   A 1 338 ? 30.095 1.97    -0.558  1    44.82  ? 338 PHE   A CG    1 1 
ATOM   2243 C  CD1   . PHE   A 1 338 ? 29.942 2.56    0.687   1    45.02  ? 338 PHE   A CD1   1 1 
ATOM   2244 C  CD2   . PHE   A 1 338 ? 29.779 2.713   -1.683  1    45.12  ? 338 PHE   A CD2   1 1 
ATOM   2245 C  CE1   . PHE   A 1 338 ? 29.437 3.847   0.805   1    45.38  ? 338 PHE   A CE1   1 1 
ATOM   2246 C  CE2   . PHE   A 1 338 ? 29.282 4.001   -1.566  1    45.49  ? 338 PHE   A CE2   1 1 
ATOM   2247 C  CZ    . PHE   A 1 338 ? 29.097 4.553   -0.322  1    45.25  ? 338 PHE   A CZ    1 1 
ATOM   2248 N  N     . GLY   A 1 339 ? 30.361 -2.808  -0.44   1    42.67  ? 339 GLY   A N     1 1 
ATOM   2249 C  CA    . GLY   A 1 339 ? 30.344 -4.022  -1.245  1    41.87  ? 339 GLY   A CA    1 1 
ATOM   2250 C  C     . GLY   A 1 339 ? 29.001 -4.67   -1.468  1    41.86  ? 339 GLY   A C     1 1 
ATOM   2251 O  O     . GLY   A 1 339 ? 28.662 -4.998  -2.605  1    41.49  ? 339 GLY   A O     1 1 
ATOM   2252 N  N     . LEU   A 1 340 ? 28.229 -4.877  -0.388  1    41.93  ? 340 LEU   A N     1 1 
ATOM   2253 C  CA    . LEU   A 1 340 ? 26.903 -5.481  -0.478  1    41.76  ? 340 LEU   A CA    1 1 
ATOM   2254 C  C     . LEU   A 1 340 ? 25.847 -4.564  -1.126  1    41.04  ? 340 LEU   A C     1 1 
ATOM   2255 O  O     . LEU   A 1 340 ? 25.228 -4.998  -2.107  1    40.95  ? 340 LEU   A O     1 1 
ATOM   2256 C  CB    . LEU   A 1 340 ? 26.422 -6.03   0.88    1    42.11  ? 340 LEU   A CB    1 1 
ATOM   2257 C  CG    . LEU   A 1 340 ? 27.007 -7.386  1.292   1    43.6   ? 340 LEU   A CG    1 1 
ATOM   2258 C  CD1   . LEU   A 1 340 ? 26.572 -7.754  2.716   1    43.79  ? 340 LEU   A CD1   1 1 
ATOM   2259 C  CD2   . LEU   A 1 340 ? 26.602 -8.467  0.299   1    43.78  ? 340 LEU   A CD2   1 1 
ATOM   2260 N  N     . PRO   A 1 341 ? 25.604 -3.316  -0.638  1    40.24  ? 341 PRO   A N     1 1 
ATOM   2261 C  CA    . PRO   A 1 341 ? 24.584 -2.472  -1.298  1    40.09  ? 341 PRO   A CA    1 1 
ATOM   2262 C  C     . PRO   A 1 341 ? 24.916 -2.138  -2.753  1    40.41  ? 341 PRO   A C     1 1 
ATOM   2263 O  O     . PRO   A 1 341 ? 23.999 -2.08   -3.571  1    41.27  ? 341 PRO   A O     1 1 
ATOM   2264 C  CB    . PRO   A 1 341 ? 24.522 -1.209  -0.418  1    41.09  ? 341 PRO   A CB    1 1 
ATOM   2265 C  CG    . PRO   A 1 341 ? 25.866 -1.193  0.315   1    41.46  ? 341 PRO   A CG    1 1 
ATOM   2266 C  CD    . PRO   A 1 341 ? 26.21  -2.633  0.527   1    39.51  ? 341 PRO   A CD    1 1 
ATOM   2267 N  N     . THR   A 1 342 ? 26.2   -1.936  -3.097  1    39.85  ? 342 THR   A N     1 1 
ATOM   2268 C  CA    . THR   A 1 342 ? 26.578 -1.663  -4.49   1    40.66  ? 342 THR   A CA    1 1 
ATOM   2269 C  C     . THR   A 1 342 ? 26.369 -2.914  -5.359  1    39.54  ? 342 THR   A C     1 1 
ATOM   2270 O  O     . THR   A 1 342 ? 25.809 -2.811  -6.445  1    38.9   ? 342 THR   A O     1 1 
ATOM   2271 C  CB    . THR   A 1 342 ? 28.023 -1.153  -4.611  1    44.41  ? 342 THR   A CB    1 1 
ATOM   2272 O  OG1   . THR   A 1 342 ? 28.208 -0.011  -3.777  1    46.77  ? 342 THR   A OG1   1 1 
ATOM   2273 C  CG2   . THR   A 1 342 ? 28.339 -0.711  -6.001  1    46.37  ? 342 THR   A CG2   1 1 
ATOM   2274 N  N     . SER   A 1 343 ? 26.813 -4.101  -4.888  1    39.01  ? 343 SER   A N     1 1 
ATOM   2275 C  CA    . SER   A 1 343 ? 26.603 -5.338  -5.653  1    39.35  ? 343 SER   A CA    1 1 
ATOM   2276 C  C     . SER   A 1 343 ? 25.129 -5.595  -5.948  1    39.78  ? 343 SER   A C     1 1 
ATOM   2277 O  O     . SER   A 1 343 ? 24.8   -5.971  -7.064  1    40.14  ? 343 SER   A O     1 1 
ATOM   2278 C  CB    . SER   A 1 343 ? 27.193 -6.542  -4.934  1    40.36  ? 343 SER   A CB    1 1 
ATOM   2279 O  OG    . SER   A 1 343 ? 28.601 -6.408  -4.844  1    43.27  ? 343 SER   A OG    1 1 
ATOM   2280 N  N     . ARG   A 1 344 ? 24.244 -5.358  -4.967  1    39.59  ? 344 ARG   A N     1 1 
ATOM   2281 C  CA    . ARG   A 1 344 ? 22.819 -5.573  -5.173  1    40.73  ? 344 ARG   A CA    1 1 
ATOM   2282 C  C     . ARG   A 1 344 ? 22.216 -4.535  -6.137  1    40.87  ? 344 ARG   A C     1 1 
ATOM   2283 O  O     . ARG   A 1 344 ? 21.419 -4.895  -7.002  1    41.5   ? 344 ARG   A O     1 1 
ATOM   2284 C  CB    . ARG   A 1 344 ? 22.075 -5.564  -3.844  1    42.49  ? 344 ARG   A CB    1 1 
ATOM   2285 C  CG    . ARG   A 1 344 ? 20.648 -6.06   -3.976  1    46.55  ? 344 ARG   A CG    1 1 
ATOM   2286 C  CD    . ARG   A 1 344 ? 19.783 -5.316  -3.015  1    50.32  ? 344 ARG   A CD    1 1 
ATOM   2287 N  NE    . ARG   A 1 344 ? 19.327 -6.129  -1.892  1    54.13  ? 344 ARG   A NE    1 1 
ATOM   2288 C  CZ    . ARG   A 1 344 ? 18.832 -5.62   -0.761  1    56.64  ? 344 ARG   A CZ    1 1 
ATOM   2289 N  NH1   . ARG   A 1 344 ? 18.815 -4.292  -0.562  1    53.07  ? 344 ARG   A NH1   1 1 
ATOM   2290 N  NH2   . ARG   A 1 344 ? 18.378 -6.426  0.19    1    56.77  ? 344 ARG   A NH2   1 1 
ATOM   2291 N  N     . ALA   A 1 345 ? 22.619 -3.254  -6.018  1    39.98  ? 345 ALA   A N     1 1 
ATOM   2292 C  CA    . ALA   A 1 345 ? 22.146 -2.225  -6.944  1    39.73  ? 345 ALA   A CA    1 1 
ATOM   2293 C  C     . ALA   A 1 345 ? 22.6   -2.572  -8.38   1    40.51  ? 345 ALA   A C     1 1 
ATOM   2294 O  O     . ALA   A 1 345 ? 21.776 -2.544  -9.292  1    41.18  ? 345 ALA   A O     1 1 
ATOM   2295 C  CB    . ALA   A 1 345 ? 22.658 -0.845  -6.534  1    38.76  ? 345 ALA   A CB    1 1 
ATOM   2296 N  N     . TYR   A 1 346 ? 23.867 -2.961  -8.567  1    40.63  ? 346 TYR   A N     1 1 
ATOM   2297 C  CA    . TYR   A 1 346 ? 24.362 -3.355  -9.895  1    42.7   ? 346 TYR   A CA    1 1 
ATOM   2298 C  C     . TYR   A 1 346 ? 23.585 -4.509  -10.489 1    43.81  ? 346 TYR   A C     1 1 
ATOM   2299 O  O     . TYR   A 1 346 ? 23.142 -4.409  -11.632 1    44.34  ? 346 TYR   A O     1 1 
ATOM   2300 C  CB    . TYR   A 1 346 ? 25.862 -3.706  -9.876  1    43.46  ? 346 TYR   A CB    1 1 
ATOM   2301 C  CG    . TYR   A 1 346 ? 26.801 -2.535  -9.674  1    45.48  ? 346 TYR   A CG    1 1 
ATOM   2302 C  CD1   . TYR   A 1 346 ? 26.34  -1.226  -9.728  1    46.92  ? 346 TYR   A CD1   1 1 
ATOM   2303 C  CD2   . TYR   A 1 346 ? 28.143 -2.737  -9.43   1    47.68  ? 346 TYR   A CD2   1 1 
ATOM   2304 C  CE1   . TYR   A 1 346 ? 27.197 -0.15   -9.546  1    48.36  ? 346 TYR   A CE1   1 1 
ATOM   2305 C  CE2   . TYR   A 1 346 ? 29.018 -1.671  -9.286  1    49.54  ? 346 TYR   A CE2   1 1 
ATOM   2306 C  CZ    . TYR   A 1 346 ? 28.541 -0.376  -9.339  1    50.51  ? 346 TYR   A CZ    1 1 
ATOM   2307 O  OH    . TYR   A 1 346 ? 29.409 0.662   -9.114  1    52.9   ? 346 TYR   A OH    1 1 
ATOM   2308 N  N     . ALA   A 1 347 ? 23.395 -5.591  -9.708  1    44.28  ? 347 ALA   A N     1 1 
ATOM   2309 C  CA    . ALA   A 1 347 ? 22.659 -6.781  -10.148 1    44.99  ? 347 ALA   A CA    1 1 
ATOM   2310 C  C     . ALA   A 1 347 ? 21.21  -6.445  -10.528 1    45.86  ? 347 ALA   A C     1 1 
ATOM   2311 O  O     . ALA   A 1 347 ? 20.764 -6.843  -11.606 1    46.34  ? 347 ALA   A O     1 1 
ATOM   2312 C  CB    . ALA   A 1 347 ? 22.707 -7.872  -9.084  1    44.34  ? 347 ALA   A CB    1 1 
ATOM   2313 N  N     . GLU   A 1 348 ? 20.497 -5.684  -9.69   1    45.87  ? 348 GLU   A N     1 1 
ATOM   2314 C  CA    . GLU   A 1 348 ? 19.109 -5.321  -10.002 1    46.66  ? 348 GLU   A CA    1 1 
ATOM   2315 C  C     . GLU   A 1 348 ? 19.02  -4.404  -11.218 1    47.42  ? 348 GLU   A C     1 1 
ATOM   2316 O  O     . GLU   A 1 348 ? 18.116 -4.552  -12.026 1    47.25  ? 348 GLU   A O     1 1 
ATOM   2317 C  CB    . GLU   A 1 348 ? 18.392 -4.729  -8.79   1    47.66  ? 348 GLU   A CB    1 1 
ATOM   2318 C  CG    . GLU   A 1 348 ? 18.25  -5.749  -7.677  1    51.37  ? 348 GLU   A CG    1 1 
ATOM   2319 C  CD    . GLU   A 1 348 ? 17.423 -5.306  -6.487  1    56.41  ? 348 GLU   A CD    1 1 
ATOM   2320 O  OE1   . GLU   A 1 348 ? 16.94  -4.152  -6.492  1    57.8   ? 348 GLU   A OE1   1 1 
ATOM   2321 O  OE2   . GLU   A 1 348 ? 17.248 -6.119  -5.551  1    57.84  ? 348 GLU   A OE2   1 1 
ATOM   2322 N  N     . TYR   A 1 349 ? 20.002 -3.524  -11.398 1    47.64  ? 349 TYR   A N     1 1 
ATOM   2323 C  CA    . TYR   A 1 349 ? 20.055 -2.622  -12.545 1    48.07  ? 349 TYR   A CA    1 1 
ATOM   2324 C  C     . TYR   A 1 349 ? 20.12  -3.419  -13.859 1    49.33  ? 349 TYR   A C     1 1 
ATOM   2325 O  O     . TYR   A 1 349 ? 19.487 -3.047  -14.84  1    49.83  ? 349 TYR   A O     1 1 
ATOM   2326 C  CB    . TYR   A 1 349 ? 21.28  -1.705  -12.404 1    47.53  ? 349 TYR   A CB    1 1 
ATOM   2327 C  CG    . TYR   A 1 349 ? 21.501 -0.792  -13.58  1    48.06  ? 349 TYR   A CG    1 1 
ATOM   2328 C  CD1   . TYR   A 1 349 ? 20.649 0.277   -13.823 1    48.66  ? 349 TYR   A CD1   1 1 
ATOM   2329 C  CD2   . TYR   A 1 349 ? 22.602 -0.954  -14.415 1    48.92  ? 349 TYR   A CD2   1 1 
ATOM   2330 C  CE1   . TYR   A 1 349 ? 20.887 1.163   -14.867 1    49.81  ? 349 TYR   A CE1   1 1 
ATOM   2331 C  CE2   . TYR   A 1 349 ? 22.821 -0.105  -15.493 1    49.92  ? 349 TYR   A CE2   1 1 
ATOM   2332 C  CZ    . TYR   A 1 349 ? 21.965 0.96    -15.713 1    51.02  ? 349 TYR   A CZ    1 1 
ATOM   2333 O  OH    . TYR   A 1 349 ? 22.182 1.818   -16.775 1    52.96  ? 349 TYR   A OH    1 1 
ATOM   2334 N  N     . LEU   A 1 350 ? 20.845 -4.542  -13.861 1    49.77  ? 350 LEU   A N     1 1 
ATOM   2335 C  CA    . LEU   A 1 350 ? 20.974 -5.396  -15.045 1    50.05  ? 350 LEU   A CA    1 1 
ATOM   2336 C  C     . LEU   A 1 350 ? 19.897 -6.491  -15.158 1    50.89  ? 350 LEU   A C     1 1 
ATOM   2337 O  O     . LEU   A 1 350 ? 20.039 -7.388  -15.984 1    53.03  ? 350 LEU   A O     1 1 
ATOM   2338 C  CB    . LEU   A 1 350 ? 22.368 -6.024  -15.058 1    50.29  ? 350 LEU   A CB    1 1 
ATOM   2339 C  CG    . LEU   A 1 350 ? 23.519 -5      -15.065 1    51.71  ? 350 LEU   A CG    1 1 
ATOM   2340 C  CD1   . LEU   A 1 350 ? 24.807 -5.648  -14.776 1    52.14  ? 350 LEU   A CD1   1 1 
ATOM   2341 C  CD2   . LEU   A 1 350 ? 23.585 -4.242  -16.372 1    52.05  ? 350 LEU   A CD2   1 1 
ATOM   2342 N  N     . GLY   A 1 351 ? 18.843 -6.427  -14.354 1    49.45  ? 351 GLY   A N     1 1 
ATOM   2343 C  CA    . GLY   A 1 351 ? 17.768 -7.411  -14.428 1    49     ? 351 GLY   A CA    1 1 
ATOM   2344 C  C     . GLY   A 1 351 ? 17.935 -8.655  -13.57  1    48.78  ? 351 GLY   A C     1 1 
ATOM   2345 O  O     . GLY   A 1 351 ? 17.134 -9.585  -13.669 1    50.2   ? 351 GLY   A O     1 1 
ATOM   2346 N  N     . GLY   A 1 352 ? 18.936 -8.668  -12.706 1    46.71  ? 352 GLY   A N     1 1 
ATOM   2347 C  CA    . GLY   A 1 352 ? 19.169 -9.795  -11.822 1    45.59  ? 352 GLY   A CA    1 1 
ATOM   2348 C  C     . GLY   A 1 352 ? 18.869 -9.471  -10.372 1    44.24  ? 352 GLY   A C     1 1 
ATOM   2349 O  O     . GLY   A 1 352 ? 18.012 -8.627  -10.095 1    44.21  ? 352 GLY   A O     1 1 
ATOM   2350 N  N     . SER   A 1 353 ? 19.608 -10.108 -9.443  1    42.57  ? 353 SER   A N     1 1 
ATOM   2351 C  CA    . SER   A 1 353 ? 19.409 -9.922  -8.013  1    42.08  ? 353 SER   A CA    1 1 
ATOM   2352 C  C     . SER   A 1 353 ? 20.572 -10.437 -7.162  1    41.1   ? 353 SER   A C     1 1 
ATOM   2353 O  O     . SER   A 1 353 ? 21.409 -11.203 -7.64   1    41.26  ? 353 SER   A O     1 1 
ATOM   2354 C  CB    . SER   A 1 353 ? 18.114 -10.603 -7.563  1    42.97  ? 353 SER   A CB    1 1 
ATOM   2355 O  OG    . SER   A 1 353 ? 18.178 -11.998 -7.786  1    45     ? 353 SER   A OG    1 1 
ATOM   2356 N  N     . LEU   A 1 354 ? 20.639 -9.989  -5.902  1    39.86  ? 354 LEU   A N     1 1 
ATOM   2357 C  CA    . LEU   A 1 354 ? 21.646 -10.461 -4.962  1    39.62  ? 354 LEU   A CA    1 1 
ATOM   2358 C  C     . LEU   A 1 354 ? 20.849 -10.782 -3.71   1    40.12  ? 354 LEU   A C     1 1 
ATOM   2359 O  O     . LEU   A 1 354 ? 20.195 -9.893  -3.153  1    39.8   ? 354 LEU   A O     1 1 
ATOM   2360 C  CB    . LEU   A 1 354 ? 22.694 -9.399  -4.631  1    39.19  ? 354 LEU   A CB    1 1 
ATOM   2361 C  CG    . LEU   A 1 354 ? 23.84  -9.91   -3.763  1    41.03  ? 354 LEU   A CG    1 1 
ATOM   2362 C  CD1   . LEU   A 1 354 ? 24.758 -10.841 -4.569  1    42.22  ? 354 LEU   A CD1   1 1 
ATOM   2363 C  CD2   . LEU   A 1 354 ? 24.673 -8.761  -3.217  1    41.27  ? 354 LEU   A CD2   1 1 
ATOM   2364 N  N     . GLN   A 1 355 ? 20.865 -12.056 -3.295  1    39.49  ? 355 GLN   A N     1 1 
ATOM   2365 C  CA    . GLN   A 1 355 ? 20.117 -12.527 -2.14   1    39.42  ? 355 GLN   A CA    1 1 
ATOM   2366 C  C     . GLN   A 1 355 ? 21.019 -13.194 -1.145  1    40.16  ? 355 GLN   A C     1 1 
ATOM   2367 O  O     . GLN   A 1 355 ? 21.952 -13.883 -1.528  1    41.01  ? 355 GLN   A O     1 1 
ATOM   2368 C  CB    . GLN   A 1 355 ? 19.018 -13.472 -2.593  1    39.92  ? 355 GLN   A CB    1 1 
ATOM   2369 C  CG    . GLN   A 1 355 ? 17.974 -12.715 -3.401  1    43.3   ? 355 GLN   A CG    1 1 
ATOM   2370 C  CD    . GLN   A 1 355 ? 16.919 -13.59  -4.013  1    46.91  ? 355 GLN   A CD    1 1 
ATOM   2371 O  OE1   . GLN   A 1 355 ? 16.921 -14.815 -3.876  1    48.05  ? 355 GLN   A OE1   1 1 
ATOM   2372 N  NE2   . GLN   A 1 355 ? 15.993 -12.966 -4.713  1    46.62  ? 355 GLN   A NE2   1 1 
ATOM   2373 N  N     . LEU   A 1 356 ? 20.766 -12.972 0.132   1    40.46  ? 356 LEU   A N     1 1 
ATOM   2374 C  CA    . LEU   A 1 356 ? 21.604 -13.494 1.191   1    42.18  ? 356 LEU   A CA    1 1 
ATOM   2375 C  C     . LEU   A 1 356 ? 20.841 -14.489 2.047   1    41.37  ? 356 LEU   A C     1 1 
ATOM   2376 O  O     . LEU   A 1 356 ? 19.721 -14.206 2.457   1    41.16  ? 356 LEU   A O     1 1 
ATOM   2377 C  CB    . LEU   A 1 356 ? 22.056 -12.337 2.104   1    44.48  ? 356 LEU   A CB    1 1 
ATOM   2378 C  CG    . LEU   A 1 356 ? 23.357 -11.589 1.742   1    49.36  ? 356 LEU   A CG    1 1 
ATOM   2379 C  CD1   . LEU   A 1 356 ? 23.319 -11.053 0.322   1    50.55  ? 356 LEU   A CD1   1 1 
ATOM   2380 C  CD2   . LEU   A 1 356 ? 23.548 -10.389 2.671   1    50.86  ? 356 LEU   A CD2   1 1 
ATOM   2381 N  N     . GLN   A 1 357 ? 21.474 -15.615 2.37    1    40.74  ? 357 GLN   A N     1 1 
ATOM   2382 C  CA    . GLN   A 1 357 ? 20.935 -16.592 3.3     1    40.71  ? 357 GLN   A CA    1 1 
ATOM   2383 C  C     . GLN   A 1 357 ? 21.944 -16.775 4.421   1    41.6   ? 357 GLN   A C     1 1 
ATOM   2384 O  O     . GLN   A 1 357 ? 23.053 -17.29  4.205   1    42.63  ? 357 GLN   A O     1 1 
ATOM   2385 C  CB    . GLN   A 1 357 ? 20.612 -17.924 2.614   1    40.07  ? 357 GLN   A CB    1 1 
ATOM   2386 C  CG    . GLN   A 1 357 ? 19.343 -17.851 1.783   1    39.2   ? 357 GLN   A CG    1 1 
ATOM   2387 C  CD    . GLN   A 1 357 ? 18.077 -17.839 2.608   1    39.28  ? 357 GLN   A CD    1 1 
ATOM   2388 O  OE1   . GLN   A 1 357 ? 18.065 -18.182 3.786   1    40.96  ? 357 GLN   A OE1   1 1 
ATOM   2389 N  NE2   . GLN   A 1 357 ? 16.975 -17.467 2.005   1    36.02  ? 357 GLN   A NE2   1 1 
ATOM   2390 N  N     . SER   A 1 358 ? 21.572 -16.352 5.618   1    41.21  ? 358 SER   A N     1 1 
ATOM   2391 C  CA    . SER   A 1 358 ? 22.46  -16.448 6.771   1    41.2   ? 358 SER   A CA    1 1 
ATOM   2392 C  C     . SER   A 1 358 ? 22.124 -17.628 7.651   1    41.3   ? 358 SER   A C     1 1 
ATOM   2393 O  O     . SER   A 1 358 ? 20.962 -17.828 7.985   1    40.46  ? 358 SER   A O     1 1 
ATOM   2394 C  CB    . SER   A 1 358 ? 22.388 -15.167 7.592   1    42.78  ? 358 SER   A CB    1 1 
ATOM   2395 O  OG    . SER   A 1 358 ? 23.313 -15.224 8.664   1    45.38  ? 358 SER   A OG    1 1 
ATOM   2396 N  N     . LEU   A 1 359 ? 23.151 -18.406 8.047   1    41.58  ? 359 LEU   A N     1 1 
ATOM   2397 C  CA    . LEU   A 1 359 ? 23.008 -19.538 8.941   1    42.96  ? 359 LEU   A CA    1 1 
ATOM   2398 C  C     . LEU   A 1 359 ? 23.857 -19.187 10.133  1    43.96  ? 359 LEU   A C     1 1 
ATOM   2399 O  O     . LEU   A 1 359 ? 25.032 -19.539 10.167  1    44.56  ? 359 LEU   A O     1 1 
ATOM   2400 C  CB    . LEU   A 1 359 ? 23.513 -20.841 8.291   1    44.17  ? 359 LEU   A CB    1 1 
ATOM   2401 C  CG    . LEU   A 1 359 ? 22.619 -21.437 7.199   1    47.37  ? 359 LEU   A CG    1 1 
ATOM   2402 C  CD1   . LEU   A 1 359 ? 22.9   -20.77  5.849   1    48.64  ? 359 LEU   A CD1   1 1 
ATOM   2403 C  CD2   . LEU   A 1 359 ? 22.888 -22.914 7.057   1    48.58  ? 359 LEU   A CD2   1 1 
ATOM   2404 N  N     . GLN   A 1 360 ? 23.309 -18.405 11.069  1    43.79  ? 360 GLN   A N     1 1 
ATOM   2405 C  CA    . GLN   A 1 360 ? 24.063 -17.908 12.218  1    43.77  ? 360 GLN   A CA    1 1 
ATOM   2406 C  C     . GLN   A 1 360 ? 24.702 -19.022 13.027  1    44.75  ? 360 GLN   A C     1 1 
ATOM   2407 O  O     . GLN   A 1 360 ? 24.038 -19.98  13.431  1    44.89  ? 360 GLN   A O     1 1 
ATOM   2408 C  CB    . GLN   A 1 360 ? 23.208 -16.978 13.095  1    43.75  ? 360 GLN   A CB    1 1 
ATOM   2409 C  CG    . GLN   A 1 360 ? 22.763 -15.696 12.403  1    43.55  ? 360 GLN   A CG    1 1 
ATOM   2410 C  CD    . GLN   A 1 360 ? 21.476 -15.823 11.615  1    46.56  ? 360 GLN   A CD    1 1 
ATOM   2411 O  OE1   . GLN   A 1 360 ? 20.88  -16.907 11.501  1    47.29  ? 360 GLN   A OE1   1 1 
ATOM   2412 N  NE2   . GLN   A 1 360 ? 21.026 -14.708 11.026  1    45.51  ? 360 GLN   A NE2   1 1 
ATOM   2413 N  N     . GLY   A 1 361 ? 26.003 -18.89  13.24   1    44.94  ? 361 GLY   A N     1 1 
ATOM   2414 C  CA    . GLY   A 1 361 ? 26.779 -19.917 13.918  1    45.36  ? 361 GLY   A CA    1 1 
ATOM   2415 C  C     . GLY   A 1 361 ? 27.55  -20.779 12.931  1    46.01  ? 361 GLY   A C     1 1 
ATOM   2416 O  O     . GLY   A 1 361 ? 28.544 -21.401 13.317  1    46.75  ? 361 GLY   A O     1 1 
ATOM   2417 N  N     . ILE   A 1 362 ? 27.123 -20.818 11.628  1    44.85  ? 362 ILE   A N     1 1 
ATOM   2418 C  CA    . ILE   A 1 362 ? 27.769 -21.649 10.611  1    44.44  ? 362 ILE   A CA    1 1 
ATOM   2419 C  C     . ILE   A 1 362 ? 28.399 -20.851 9.454   1    44.32  ? 362 ILE   A C     1 1 
ATOM   2420 O  O     . ILE   A 1 362 ? 29.612 -20.934 9.259   1    44.9   ? 362 ILE   A O     1 1 
ATOM   2421 C  CB    . ILE   A 1 362 ? 26.813 -22.769 10.078  1    44.88  ? 362 ILE   A CB    1 1 
ATOM   2422 C  CG1   . ILE   A 1 362 ? 26.402 -23.75  11.199  1    45.32  ? 362 ILE   A CG1   1 1 
ATOM   2423 C  CG2   . ILE   A 1 362 ? 27.434 -23.517 8.874   1    45.09  ? 362 ILE   A CG2   1 1 
ATOM   2424 C  CD1   . ILE   A 1 362 ? 27.525 -24.544 11.767  1    46.13  ? 362 ILE   A CD1   1 1 
ATOM   2425 N  N     . GLY   A 1 363 ? 27.603 -20.108 8.687   1    43.4   ? 363 GLY   A N     1 1 
ATOM   2426 C  CA    . GLY   A 1 363 ? 28.102 -19.407 7.516   1    42.63  ? 363 GLY   A CA    1 1 
ATOM   2427 C  C     . GLY   A 1 363 ? 27.016 -18.739 6.707   1    42.31  ? 363 GLY   A C     1 1 
ATOM   2428 O  O     . GLY   A 1 363 ? 25.885 -18.594 7.172   1    41.65  ? 363 GLY   A O     1 1 
ATOM   2429 N  N     . THR   A 1 364 ? 27.367 -18.274 5.51    1    42.06  ? 364 THR   A N     1 1 
ATOM   2430 C  CA    . THR   A 1 364 ? 26.45  -17.534 4.666   1    41.9   ? 364 THR   A CA    1 1 
ATOM   2431 C  C     . THR   A 1 364 ? 26.486 -18.029 3.229   1    42.07  ? 364 THR   A C     1 1 
ATOM   2432 O  O     . THR   A 1 364 ? 27.549 -18.362 2.712   1    42.53  ? 364 THR   A O     1 1 
ATOM   2433 C  CB    . THR   A 1 364 ? 26.852 -16.04  4.71    1    42.99  ? 364 THR   A CB    1 1 
ATOM   2434 O  OG1   . THR   A 1 364 ? 26.861 -15.606 6.065   1    44.03  ? 364 THR   A OG1   1 1 
ATOM   2435 C  CG2   . THR   A 1 364 ? 25.928 -15.125 3.885   1    43.4   ? 364 THR   A CG2   1 1 
ATOM   2436 N  N     . ASP   A 1 365 ? 25.321 -18.069 2.578   1    41.96  ? 365 ASP   A N     1 1 
ATOM   2437 C  CA    . ASP   A 1 365 ? 25.214 -18.363 1.152   1    42.06  ? 365 ASP   A CA    1 1 
ATOM   2438 C  C     . ASP   A 1 365 ? 24.809 -17.075 0.473   1    41.64  ? 365 ASP   A C     1 1 
ATOM   2439 O  O     . ASP   A 1 365 ? 23.831 -16.449 0.885   1    41.33  ? 365 ASP   A O     1 1 
ATOM   2440 C  CB    . ASP   A 1 365 ? 24.157 -19.417 0.868   1    43.6   ? 365 ASP   A CB    1 1 
ATOM   2441 C  CG    . ASP   A 1 365 ? 24.511 -20.763 1.423   1    50.74  ? 365 ASP   A CG    1 1 
ATOM   2442 O  OD1   . ASP   A 1 365 ? 25.712 -21.079 1.489   1    50.51  ? 365 ASP   A OD1   1 1 
ATOM   2443 O  OD2   . ASP   A 1 365 ? 23.585 -21.494 1.842   1    56.28  ? 365 ASP   A OD2   1 1 
ATOM   2444 N  N     . VAL   A 1 366 ? 25.58  -16.645 -0.525  1    41.17  ? 366 VAL   A N     1 1 
ATOM   2445 C  CA    . VAL   A 1 366 ? 25.244 -15.442 -1.27   1    41.11  ? 366 VAL   A CA    1 1 
ATOM   2446 C  C     . VAL   A 1 366 ? 24.855 -15.876 -2.675  1    40     ? 366 VAL   A C     1 1 
ATOM   2447 O  O     . VAL   A 1 366 ? 25.594 -16.633 -3.293  1    39.02  ? 366 VAL   A O     1 1 
ATOM   2448 C  CB    . VAL   A 1 366 ? 26.401 -14.417 -1.26   1    42.47  ? 366 VAL   A CB    1 1 
ATOM   2449 C  CG1   . VAL   A 1 366 ? 26.048 -13.194 -2.095  1    42.94  ? 366 VAL   A CG1   1 1 
ATOM   2450 C  CG2   . VAL   A 1 366 ? 26.726 -13.999 0.172   1    43.52  ? 366 VAL   A CG2   1 1 
ATOM   2451 N  N     . TYR   A 1 367 ? 23.69  -15.428 -3.176  1    39.66  ? 367 TYR   A N     1 1 
ATOM   2452 C  CA    . TYR   A 1 367 ? 23.244 -15.835 -4.507  1    39.68  ? 367 TYR   A CA    1 1 
ATOM   2453 C  C     . TYR   A 1 367 ? 23.228 -14.651 -5.456  1    40.29  ? 367 TYR   A C     1 1 
ATOM   2454 O  O     . TYR   A 1 367 ? 22.397 -13.747 -5.311  1    40.71  ? 367 TYR   A O     1 1 
ATOM   2455 C  CB    . TYR   A 1 367 ? 21.849 -16.491 -4.473  1    39.08  ? 367 TYR   A CB    1 1 
ATOM   2456 C  CG    . TYR   A 1 367 ? 21.746 -17.742 -3.619  1    39.23  ? 367 TYR   A CG    1 1 
ATOM   2457 C  CD1   . TYR   A 1 367 ? 21.664 -17.655 -2.237  1    39.78  ? 367 TYR   A CD1   1 1 
ATOM   2458 C  CD2   . TYR   A 1 367 ? 21.59  -18.994 -4.199  1    39.75  ? 367 TYR   A CD2   1 1 
ATOM   2459 C  CE1   . TYR   A 1 367 ? 21.51  -18.78  -1.452  1    40.58  ? 367 TYR   A CE1   1 1 
ATOM   2460 C  CE2   . TYR   A 1 367 ? 21.425 -20.133 -3.419  1    40.46  ? 367 TYR   A CE2   1 1 
ATOM   2461 C  CZ    . TYR   A 1 367 ? 21.403 -20.02  -2.043  1    41.68  ? 367 TYR   A CZ    1 1 
ATOM   2462 O  OH    . TYR   A 1 367 ? 21.244 -21.109 -1.221  1    43.53  ? 367 TYR   A OH    1 1 
ATOM   2463 N  N     . LEU   A 1 368 ? 24.093 -14.711 -6.478  1    39.65  ? 368 LEU   A N     1 1 
ATOM   2464 C  CA    . LEU   A 1 368 ? 24.177 -13.717 -7.52   1    39.83  ? 368 LEU   A CA    1 1 
ATOM   2465 C  C     . LEU   A 1 368 ? 23.457 -14.253 -8.76   1    40.84  ? 368 LEU   A C     1 1 
ATOM   2466 O  O     . LEU   A 1 368 ? 23.774 -15.341 -9.244  1    41.51  ? 368 LEU   A O     1 1 
ATOM   2467 C  CB    . LEU   A 1 368 ? 25.64  -13.373 -7.843  1    39.42  ? 368 LEU   A CB    1 1 
ATOM   2468 C  CG    . LEU   A 1 368 ? 25.802 -12.344 -8.987  1    41.43  ? 368 LEU   A CG    1 1 
ATOM   2469 C  CD1   . LEU   A 1 368 ? 25.131 -10.995 -8.638  1    41.35  ? 368 LEU   A CD1   1 1 
ATOM   2470 C  CD2   . LEU   A 1 368 ? 27.284 -12.135 -9.346  1    41.87  ? 368 LEU   A CD2   1 1 
ATOM   2471 N  N     . ARG   A 1 369 ? 22.454 -13.53  -9.243  1    40.99  ? 369 ARG   A N     1 1 
ATOM   2472 C  CA    . ARG   A 1 369 ? 21.718 -13.947 -10.436 1    41.77  ? 369 ARG   A CA    1 1 
ATOM   2473 C  C     . ARG   A 1 369 ? 21.791 -12.831 -11.443 1    43.58  ? 369 ARG   A C     1 1 
ATOM   2474 O  O     . ARG   A 1 369 ? 21.521 -11.674 -11.112 1    42.98  ? 369 ARG   A O     1 1 
ATOM   2475 C  CB    . ARG   A 1 369 ? 20.253 -14.258 -10.11  1    41.81  ? 369 ARG   A CB    1 1 
ATOM   2476 C  CG    . ARG   A 1 369 ? 20.089 -15.439 -9.158  1    42.67  ? 369 ARG   A CG    1 1 
ATOM   2477 C  CD    . ARG   A 1 369 ? 18.62  -15.725 -8.857  1    43.61  ? 369 ARG   A CD    1 1 
ATOM   2478 N  NE    . ARG   A 1 369 ? 18.442 -17.073 -8.307  1    45.61  ? 369 ARG   A NE    1 1 
ATOM   2479 C  CZ    . ARG   A 1 369 ? 18.526 -17.364 -7.012  1    47.22  ? 369 ARG   A CZ    1 1 
ATOM   2480 N  NH1   . ARG   A 1 369 ? 18.762 -16.403 -6.119  1    46.45  ? 369 ARG   A NH1   1 1 
ATOM   2481 N  NH2   . ARG   A 1 369 ? 18.346 -18.612 -6.593  1    45.5   ? 369 ARG   A NH2   1 1 
ATOM   2482 N  N     . LEU   A 1 370 ? 22.196 -13.167 -12.669 1    45.07  ? 370 LEU   A N     1 1 
ATOM   2483 C  CA    . LEU   A 1 370 ? 22.282 -12.196 -13.748 1    46.54  ? 370 LEU   A CA    1 1 
ATOM   2484 C  C     . LEU   A 1 370 ? 21.596 -12.757 -14.977 1    48.62  ? 370 LEU   A C     1 1 
ATOM   2485 O  O     . LEU   A 1 370 ? 21.756 -13.93  -15.286 1    48.84  ? 370 LEU   A O     1 1 
ATOM   2486 C  CB    . LEU   A 1 370 ? 23.75  -11.845 -14.045 1    46.39  ? 370 LEU   A CB    1 1 
ATOM   2487 C  CG    . LEU   A 1 370 ? 24.442 -11.007 -12.958 1    47.59  ? 370 LEU   A CG    1 1 
ATOM   2488 C  CD1   . LEU   A 1 370 ? 25.92  -10.846 -13.25  1    47.1   ? 370 LEU   A CD1   1 1 
ATOM   2489 C  CD2   . LEU   A 1 370 ? 23.729 -9.648  -12.746 1    47.79  ? 370 LEU   A CD2   1 1 
ATOM   2490 N  N     . ARG   A 1 371 ? 20.817 -11.941 -15.66  1    50.64  ? 371 ARG   A N     1 1 
ATOM   2491 C  CA    . ARG   A 1 371 ? 20.101 -12.366 -16.859 1    53.72  ? 371 ARG   A CA    1 1 
ATOM   2492 C  C     . ARG   A 1 371 ? 21.032 -12.611 -18.041 1    54.98  ? 371 ARG   A C     1 1 
ATOM   2493 O  O     . ARG   A 1 371 ? 22.091 -11.998 -18.145 1    54.82  ? 371 ARG   A O     1 1 
ATOM   2494 C  CB    . ARG   A 1 371 ? 19.061 -11.312 -17.26  1    57.17  ? 371 ARG   A CB    1 1 
ATOM   2495 C  CG    . ARG   A 1 371 ? 17.661 -11.641 -16.801 1    65.14  ? 371 ARG   A CG    1 1 
ATOM   2496 C  CD    . ARG   A 1 371 ? 16.745 -10.441 -16.962 1    73.15  ? 371 ARG   A CD    1 1 
ATOM   2497 N  NE    . ARG   A 1 371 ? 15.971 -10.487 -18.208 1    80.07  ? 371 ARG   A NE    1 1 
ATOM   2498 C  CZ    . ARG   A 1 371 ? 15.271 -9.464  -18.692 1    84.8   ? 371 ARG   A CZ    1 1 
ATOM   2499 N  NH1   . ARG   A 1 371 ? 15.262 -8.294  -18.057 1    85.74  ? 371 ARG   A NH1   1 1 
ATOM   2500 N  NH2   . ARG   A 1 371 ? 14.586 -9.596  -19.822 1    85.13  ? 371 ARG   A NH2   1 1 
ATOM   2501 N  N     . HIS   A 1 372 ? 20.622 -13.506 -18.937 1    55.66  ? 372 HIS   A N     1 1 
ATOM   2502 C  CA    . HIS   A 1 372 ? 21.371 -13.769 -20.147 1    57.33  ? 372 HIS   A CA    1 1 
ATOM   2503 C  C     . HIS   A 1 372 ? 21.034 -12.706 -21.212 1    60.73  ? 372 HIS   A C     1 1 
ATOM   2504 O  O     . HIS   A 1 372 ? 20.047 -11.98  -21.083 1    60.02  ? 372 HIS   A O     1 1 
ATOM   2505 C  CB    . HIS   A 1 372 ? 21.032 -15.168 -20.678 1    56.56  ? 372 HIS   A CB    1 1 
ATOM   2506 C  CG    . HIS   A 1 372 ? 21.803 -16.256 -20.01  1    56.43  ? 372 HIS   A CG    1 1 
ATOM   2507 N  ND1   . HIS   A 1 372 ? 23.174 -16.38  -20.181 1    57.65  ? 372 HIS   A ND1   1 1 
ATOM   2508 C  CD2   . HIS   A 1 372 ? 21.377 -17.236 -19.191 1    56.72  ? 372 HIS   A CD2   1 1 
ATOM   2509 C  CE1   . HIS   A 1 372 ? 23.532 -17.417 -19.45  1    57.65  ? 372 HIS   A CE1   1 1 
ATOM   2510 N  NE2   . HIS   A 1 372 ? 22.485 -17.973 -18.848 1    57.54  ? 372 HIS   A NE2   1 1 
ATOM   2511 N  N     . ILE   A 1 373 ? 21.851 -12.626 -22.269 1    64     ? 373 ILE   A N     1 1 
ATOM   2512 C  CA    . ILE   A 1 373 ? 21.597 -11.721 -23.379 1    67.53  ? 373 ILE   A CA    1 1 
ATOM   2513 C  C     . ILE   A 1 373 ? 20.702 -12.484 -24.355 1    71.69  ? 373 ILE   A C     1 1 
ATOM   2514 O  O     . ILE   A 1 373 ? 21.15  -13.489 -24.908 1    72.29  ? 373 ILE   A O     1 1 
ATOM   2515 C  CB    . ILE   A 1 373 ? 22.933 -11.334 -24.037 1    68.02  ? 373 ILE   A CB    1 1 
ATOM   2516 C  CG1   . ILE   A 1 373 ? 23.878 -10.675 -23.015 1    68.41  ? 373 ILE   A CG1   1 1 
ATOM   2517 C  CG2   . ILE   A 1 373 ? 22.699 -10.459 -25.276 1    68.72  ? 373 ILE   A CG2   1 1 
ATOM   2518 C  CD1   . ILE   A 1 373 ? 25.234 -10.274 -23.551 1    69.23  ? 373 ILE   A CD1   1 1 
ATOM   2519 N  N     . ASP   A 1 374 ? 19.43  -12.046 -24.517 1    74.33  ? 374 ASP   A N     1 1 
ATOM   2520 C  CA    . ASP   A 1 374 ? 18.392 -12.656 -25.373 1    77.36  ? 374 ASP   A CA    1 1 
ATOM   2521 C  C     . ASP   A 1 374 ? 18.939 -13.334 -26.662 1    78.85  ? 374 ASP   A C     1 1 
ATOM   2522 O  O     . ASP   A 1 374 ? 19.046 -12.717 -27.729 1    79.66  ? 374 ASP   A O     1 1 
ATOM   2523 C  CB    . ASP   A 1 374 ? 17.296 -11.609 -25.707 1    81.07  ? 374 ASP   A CB    1 1 
ATOM   2524 C  CG    . ASP   A 1 374 ? 16.187 -12.074 -26.651 1    89.08  ? 374 ASP   A CG    1 1 
ATOM   2525 O  OD1   . ASP   A 1 374 ? 15.761 -13.255 -26.541 1    91.06  ? 374 ASP   A OD1   1 1 
ATOM   2526 O  OD2   . ASP   A 1 374 ? 15.741 -11.256 -27.497 1    91.49  ? 374 ASP   A OD2   1 1 
HETATM 2527 P  PB    . ADP   B 2 .   ? 32.531 -4.12   4.359   1    43.74  ? 401 ADP   A PB    1 1 
HETATM 2528 O  O1B   . ADP   B 2 .   ? 32.325 -4.366  5.835   1    43.74  ? 401 ADP   A O1B   1 1 
HETATM 2529 O  O2B   . ADP   B 2 .   ? 33.303 -2.847  4.072   1    44.14  ? 401 ADP   A O2B   1 1 
HETATM 2530 O  O3B   . ADP   B 2 .   ? 33.115 -5.32   3.644   1    44.16  ? 401 ADP   A O3B   1 1 
HETATM 2531 P  PA    . ADP   B 2 .   ? 30.039 -4.874  2.908   1    42.88  ? 401 ADP   A PA    1 1 
HETATM 2532 O  O1A   . ADP   B 2 .   ? 30.85  -5.699  1.984   1    41.64  ? 401 ADP   A O1A   1 1 
HETATM 2533 O  O2A   . ADP   B 2 .   ? 28.93  -4.037  2.393   1    41.86  ? 401 ADP   A O2A   1 1 
HETATM 2534 O  O3A   . ADP   B 2 .   ? 31.044 -3.929  3.72    1    43.76  ? 401 ADP   A O3A   1 1 
HETATM 2535 O  "O5'" . ADP   B 2 .   ? 29.503 -5.852  4.065   1    42.87  ? 401 ADP   A "O5'" 1 ? 
HETATM 2536 C  "C5'" . ADP   B 2 .   ? 28.747 -5.329  5.18    1    43.18  ? 401 ADP   A "C5'" 1 ? 
HETATM 2537 C  "C4'" . ADP   B 2 .   ? 28.854 -6.239  6.379   1    43.65  ? 401 ADP   A "C4'" 1 ? 
HETATM 2538 O  "O4'" . ADP   B 2 .   ? 28.115 -7.454  6.127   1    43.88  ? 401 ADP   A "O4'" 1 ? 
HETATM 2539 C  "C3'" . ADP   B 2 .   ? 30.251 -6.729  6.731   1    44.58  ? 401 ADP   A "C3'" 1 ? 
HETATM 2540 O  "O3'" . ADP   B 2 .   ? 31.021 -5.789  7.479   1    45.19  ? 401 ADP   A "O3'" 1 ? 
HETATM 2541 C  "C2'" . ADP   B 2 .   ? 29.942 -7.984  7.55    1    44.77  ? 401 ADP   A "C2'" 1 ? 
HETATM 2542 O  "O2'" . ADP   B 2 .   ? 29.524 -7.666  8.876   1    45.1   ? 401 ADP   A "O2'" 1 ? 
HETATM 2543 C  "C1'" . ADP   B 2 .   ? 28.728 -8.542  6.802   1    44.26  ? 401 ADP   A "C1'" 1 ? 
HETATM 2544 N  N9    . ADP   B 2 .   ? 29.042 -9.592  5.837   1    44.04  ? 401 ADP   A N9    1 1 
HETATM 2545 C  C8    . ADP   B 2 .   ? 29.12  -9.48   4.473   1    44.19  ? 401 ADP   A C8    1 1 
HETATM 2546 N  N7    . ADP   B 2 .   ? 29.382 -10.608 3.858   1    43.95  ? 401 ADP   A N7    1 1 
HETATM 2547 C  C5    . ADP   B 2 .   ? 29.485 -11.528 4.891   1    43.7   ? 401 ADP   A C5    1 1 
HETATM 2548 C  C6    . ADP   B 2 .   ? 29.74  -12.914 4.905   1    43.37  ? 401 ADP   A C6    1 1 
HETATM 2549 N  N6    . ADP   B 2 .   ? 29.965 -13.641 3.806   1    42.66  ? 401 ADP   A N6    1 1 
HETATM 2550 N  N1    . ADP   B 2 .   ? 29.756 -13.536 6.106   1    43.74  ? 401 ADP   A N1    1 1 
HETATM 2551 C  C2    . ADP   B 2 .   ? 29.535 -12.814 7.211   1    43.67  ? 401 ADP   A C2    1 1 
HETATM 2552 N  N3    . ADP   B 2 .   ? 29.287 -11.506 7.318   1    43.83  ? 401 ADP   A N3    1 1 
HETATM 2553 C  C4    . ADP   B 2 .   ? 29.277 -10.916 6.116   1    43.72  ? 401 ADP   A C4    1 1 
HETATM 2554 MG MG    . MG    C 3 .   ? 32.931 -5.993  1.655   1    50.74  2 402 MG    A MG    1 1 
HETATM 2555 K  K     . K     D 4 .   ? 27.272 -2.514  4.108   1    78.21  1 403 K     A K     1 1 
HETATM 2556 C  C4    . A1A40 E 5 .   ? 29.02  9.631   -14.923 0.99 49.47  ? 404 A1A40 A C4    1 1 
HETATM 2557 C  C7    . A1A40 E 5 .   ? 29.061 12.359  -15.084 0.99 49.76  ? 404 A1A40 A C7    1 1 
HETATM 2558 C  C6    . A1A40 E 5 .   ? 30.134 11.654  -15.551 0.99 48.99  ? 404 A1A40 A C6    1 1 
HETATM 2559 C  C13   . A1A40 E 5 .   ? 30.808 10.302  -18.554 0.99 48.42  ? 404 A1A40 A C13   1 1 
HETATM 2560 C  C20   . A1A40 E 5 .   ? 32.13  8.178   -14.053 0.99 47.4   ? 404 A1A40 A C20   1 1 
HETATM 2561 C  C8    . A1A40 E 5 .   ? 27.969 11.725  -14.542 0.99 49.88  ? 404 A1A40 A C8    1 1 
HETATM 2562 C  C16   . A1A40 E 5 .   ? 32.824 8.523   -19.308 0.99 48.64  ? 404 A1A40 A C16   1 1 
HETATM 2563 C  C19   . A1A40 E 5 .   ? 32.08  8.606   -15.494 0.99 47.7   ? 404 A1A40 A C19   1 1 
HETATM 2564 C  C1    . A1A40 E 5 .   ? 26.954 9.182   -12.615 0.99 49.81  ? 404 A1A40 A C1    1 1 
HETATM 2565 O  O2    . A1A40 E 5 .   ? 26.844 9.649   -13.954 0.99 50.44  ? 404 A1A40 A O2    1 1 
HETATM 2566 C  C3    . A1A40 E 5 .   ? 27.932 10.346  -14.448 0.99 50.11  ? 404 A1A40 A C3    1 1 
HETATM 2567 C  C5    . A1A40 E 5 .   ? 30.124 10.262  -15.489 0.99 48.82  ? 404 A1A40 A C5    1 1 
HETATM 2568 F  F9    . A1A40 E 5 .   ? 26.944 12.456  -14.075 0.99 50.48  ? 404 A1A40 A F9    1 1 
HETATM 2569 F  F10   . A1A40 E 5 .   ? 29.084 13.716  -15.101 0.99 50.04  ? 404 A1A40 A F10   1 1 
HETATM 2570 C  C11   . A1A40 E 5 .   ? 31.237 9.49    -16.117 0.99 48.33  ? 404 A1A40 A C11   1 1 
HETATM 2571 C  C12   . A1A40 E 5 .   ? 31.459 9.56    -17.57  0.99 48.35  ? 404 A1A40 A C12   1 1 
HETATM 2572 C  C14   . A1A40 E 5 .   ? 31.138 10.164  -19.89  0.99 48.73  ? 404 A1A40 A C14   1 1 
HETATM 2573 C  C15   . A1A40 E 5 .   ? 32.137 9.289   -20.227 0.99 49.4   ? 404 A1A40 A C15   1 1 
HETATM 2574 C  C17   . A1A40 E 5 .   ? 32.471 8.672   -17.969 0.99 48.29  ? 404 A1A40 A C17   1 1 
HETATM 2575 S  S18   . A1A40 E 5 .   ? 33.153 7.8     -16.622 0.99 47.66  ? 404 A1A40 A S18   1 1 
HETATM 2576 O  O21   . A1A40 E 5 .   ? 31.575 8.814   -13.171 0.99 46.94  ? 404 A1A40 A O21   1 1 
HETATM 2577 O  O22   . A1A40 E 5 .   ? 32.911 7.169   -13.752 0.99 47.84  ? 404 A1A40 A O22   1 1 
HETATM 2578 F  F23   . A1A40 E 5 .   ? 32.505 9.2     -21.539 0.99 50.09  ? 404 A1A40 A F23   1 1 
HETATM 2579 F  F24   . A1A40 E 5 .   ? 29.01  8.29    -14.816 0.99 49.45  ? 404 A1A40 A F24   1 1 
HETATM 2580 P  P     . PO4   F 6 .   ? 33.523 -2.726  0.655   1    93.73  ? 405 PO4   A P     1 ? 
HETATM 2581 O  O1    . PO4   F 6 .   ? 34.967 -3.122  0.941   1    93.72  ? 405 PO4   A O1    1 ? 
HETATM 2582 O  O2    . PO4   F 6 .   ? 33.406 -2.252  -0.812  1    94.22  ? 405 PO4   A O2    1 ? 
HETATM 2583 O  O3    . PO4   F 6 .   ? 32.6   -3.942  0.886   1    93.41  ? 405 PO4   A O3    1 ? 
HETATM 2584 O  O4    . PO4   F 6 .   ? 33.047 -1.577  1.562   1    93.59  ? 405 PO4   A O4    1 ? 
HETATM 2585 O  O     . HOH   G 7 .   ? 20.939 -1.938  -0.346  1    42.37  ? 501 HOH   A O     1 ? 
HETATM 2586 O  O     . HOH   G 7 .   ? 18.227 -8.393  -5.104  1    47.04  ? 502 HOH   A O     1 ? 
HETATM 2587 O  O     . HOH   G 7 .   ? 29.454 2.978   -10.128 1    38.18  ? 503 HOH   A O     1 ? 
HETATM 2588 O  O     . HOH   G 7 .   ? 35.274 4.392   -8.081  1    50.63  ? 504 HOH   A O     1 ? 
HETATM 2589 O  O     . HOH   G 7 .   ? 24.033 -14.781 -22.312 1    56.47  ? 505 HOH   A O     1 ? 
HETATM 2590 O  O     . HOH   G 7 .   ? 29.517 -16.214 7.03    1    49.72  ? 506 HOH   A O     1 ? 
HETATM 2591 O  O     . HOH   G 7 .   ? 40.376 -23.891 2.948   1    49.14  ? 507 HOH   A O     1 ? 
HETATM 2592 O  O     . HOH   G 7 .   ? 30.378 -14.24  10.933  1    51.72  ? 508 HOH   A O     1 ? 
HETATM 2593 O  O     . HOH   G 7 .   ? 37.955 6.483   -35.719 1    79.18  ? 509 HOH   A O     1 ? 
HETATM 2594 O  O     . HOH   G 7 .   ? 32.719 -6.39   -0.35   1    42.36  ? 510 HOH   A O     1 ? 
HETATM 2595 O  O     . HOH   G 7 .   ? 18.938 -8.778  -1.124  1    54.74  ? 511 HOH   A O     1 ? 
HETATM 2596 O  O     . HOH   G 7 .   ? 35.135 15.936  -14.928 1    50.32  ? 512 HOH   A O     1 ? 
HETATM 2597 O  O     . HOH   G 7 .   ? 21.64  -1.066  -2.889  1    40.69  ? 513 HOH   A O     1 ? 
HETATM 2598 O  O     . HOH   G 7 .   ? 27.4   -10.246 11.977  1    47.03  ? 514 HOH   A O     1 ? 
HETATM 2599 O  O     . HOH   G 7 .   ? 18.418 -17.281 10.542  1    42.51  ? 515 HOH   A O     1 ? 
HETATM 2600 O  O     . HOH   G 7 .   ? 17.523 10.727  -2.756  1    58.28  ? 516 HOH   A O     1 ? 
HETATM 2601 O  O     . HOH   G 7 .   ? 31.316 3.444   7.638   1    68.36  ? 517 HOH   A O     1 ? 
HETATM 2602 O  O     . HOH   G 7 .   ? 27.023 -21.696 3.749   1    52.88  ? 518 HOH   A O     1 ? 
HETATM 2603 O  O     . HOH   G 7 .   ? 28.553 19.549  5.418   1    64.3   ? 519 HOH   A O     1 ? 
HETATM 2604 O  O     . HOH   G 7 .   ? 16.586 -12.627 -9.872  1    55.7   ? 520 HOH   A O     1 ? 
HETATM 2605 O  O     . HOH   G 7 .   ? 19.074 13.518  -4.708  1    52.04  ? 521 HOH   A O     1 ? 
HETATM 2606 O  O     . HOH   G 7 .   ? 28.161 -23.154 -3.365  1    42.62  ? 522 HOH   A O     1 ? 
HETATM 2607 O  O     . HOH   G 7 .   ? 35.105 -5.819  1.347   1    44.32  ? 523 HOH   A O     1 ? 
HETATM 2608 O  O     . HOH   G 7 .   ? 21.871 3.242   2.958   1    29.35  ? 524 HOH   A O     1 ? 
HETATM 2609 O  O     . HOH   G 7 .   ? 29.682 -16.057 0.961   1    40.47  ? 525 HOH   A O     1 ? 
HETATM 2610 O  O     . HOH   G 7 .   ? 23.137 1.448   9.122   1    57.24  ? 526 HOH   A O     1 ? 
HETATM 2611 O  O     . HOH   G 7 .   ? 26.816 19.593  -4.02   1    64.4   ? 527 HOH   A O     1 ? 
HETATM 2612 O  O     . HOH   G 7 .   ? 17.338 -3.334  2.816   1    74.91  ? 528 HOH   A O     1 ? 
HETATM 2613 O  O     . HOH   G 7 .   ? 20.376 -25.863 -17.256 1    60.09  ? 529 HOH   A O     1 ? 
HETATM 2614 O  O     . HOH   G 7 .   ? 20.152 -5.256  5.408   1    62.06  ? 530 HOH   A O     1 ? 
HETATM 2615 O  O     . HOH   G 7 .   ? 32.764 -21.863 -17.243 1    59.07  ? 531 HOH   A O     1 ? 
HETATM 2616 O  O     . HOH   G 7 .   ? 31.314 -22.398 10.914  1    62.49  ? 532 HOH   A O     1 ? 
HETATM 2617 O  O     . HOH   G 7 .   ? 19.761 -13.712 -6.254  1    36.4   ? 533 HOH   A O     1 ? 
HETATM 2618 O  O     . HOH   G 7 .   ? 18.937 8.663   -17.18  1    74.53  ? 534 HOH   A O     1 ? 
HETATM 2619 O  O     . HOH   G 7 .   ? 39.187 -29.327 -0.342  1    89.53  ? 535 HOH   A O     1 ? 
HETATM 2620 O  O     . HOH   G 7 .   ? 41.756 -26.097 5.053   1    65.47  ? 536 HOH   A O     1 ? 
HETATM 2621 O  O     . HOH   G 7 .   ? 37.781 -10.11  -16.311 1    66.57  ? 537 HOH   A O     1 ? 
HETATM 2622 O  O     . HOH   G 7 .   ? 24.485 22.118  -10.342 1    57.98  ? 538 HOH   A O     1 ? 
HETATM 2623 O  O     . HOH   G 7 .   ? 16.774 2.558   -4.465  1    60.04  ? 539 HOH   A O     1 ? 
HETATM 2624 O  O     . HOH   G 7 .   ? 38.146 10.212  -9.56   1    67.92  ? 540 HOH   A O     1 ? 
HETATM 2625 O  O     . HOH   G 7 .   ? 34.495 -20.637 4.4     1    43.08  ? 541 HOH   A O     1 ? 
HETATM 2626 O  O     . HOH   G 7 .   ? 28.407 -5.967  15.462  1    79.53  ? 542 HOH   A O     1 ? 
HETATM 2627 O  O     . HOH   G 7 .   ? 30.131 -13.353 0.553   1    40.56  ? 543 HOH   A O     1 ? 
HETATM 2628 O  O     . HOH   G 7 .   ? 18.361 -1.68   -6.301  1    51.44  ? 544 HOH   A O     1 ? 
HETATM 2629 O  O     . HOH   G 7 .   ? 28.925 -10.863 1.047   1    40.46  ? 545 HOH   A O     1 ? 
HETATM 2630 O  O     . HOH   G 7 .   ? 27.345 -28.133 3.72    1    53.56  ? 546 HOH   A O     1 ? 
HETATM 2631 O  O     . HOH   G 7 .   ? 32.672 -10.203 5.766   1    41.14  ? 547 HOH   A O     1 ? 
HETATM 2632 O  O     . HOH   G 7 .   ? 40.999 18.242  -18.068 1    96.66  ? 548 HOH   A O     1 ? 
HETATM 2633 O  O     . HOH   G 7 .   ? 14.291 14.843  4.187   1    66.04  ? 549 HOH   A O     1 ? 
HETATM 2634 O  O     . HOH   G 7 .   ? 16.912 -13.785 -19.906 1    70.63  ? 550 HOH   A O     1 ? 
HETATM 2635 O  O     . HOH   G 7 .   ? 20.018 4.272   -12.814 1    80.52  ? 551 HOH   A O     1 ? 
HETATM 2636 O  O     . HOH   G 7 .   ? 33.465 -25.5   3.571   1    78.62  ? 552 HOH   A O     1 ? 
HETATM 2637 O  O     . HOH   G 7 .   ? 16.743 13.928  4.861   1    60.99  ? 553 HOH   A O     1 ? 
HETATM 2638 O  O     . HOH   G 7 .   ? 19.092 -14.974 6.349   1    43.18  ? 554 HOH   A O     1 ? 
HETATM 2639 O  O     . HOH   G 7 .   ? 17.438 -13.704 -12.252 1    74.89  ? 555 HOH   A O     1 ? 
HETATM 2640 O  O     . HOH   G 7 .   ? 15.284 -7.549  -10.271 1    75.56  ? 556 HOH   A O     1 ? 
HETATM 2641 O  O     . HOH   G 7 .   ? 42.113 -19.033 -8.863  1    63.03  ? 557 HOH   A O     1 ? 
HETATM 2642 O  O     . HOH   G 7 .   ? 33.146 -28.785 -4.806  1    57.5   ? 558 HOH   A O     1 ? 
HETATM 2643 O  O     . HOH   G 7 .   ? 35.334 -5.161  -30.788 1    68.18  ? 559 HOH   A O     1 ? 
HETATM 2644 O  O     . HOH   G 7 .   ? 22.907 -15.863 -24.604 1    75.44  ? 560 HOH   A O     1 ? 
HETATM 2645 O  O     . HOH   G 7 .   ? 33.061 4.596   4.449   1    68.91  ? 561 HOH   A O     1 ? 
HETATM 2646 O  O     . HOH   G 7 .   ? 22.356 -11.249 16.679  1    65.04  ? 562 HOH   A O     1 ? 
HETATM 2647 O  O     . HOH   G 7 .   ? 27.443 1.457   -28.922 1    65.81  ? 563 HOH   A O     1 ? 
HETATM 2648 O  O     . HOH   G 7 .   ? 39.584 -21.962 14.871  1    72.48  ? 564 HOH   A O     1 ? 
HETATM 2649 O  O     . HOH   G 7 .   ? 19.914 -18.012 -23.173 1    66.29  ? 565 HOH   A O     1 ? 
HETATM 2650 O  O     . HOH   G 7 .   ? 19.284 -0.977  -8.624  1    54.24  ? 566 HOH   A O     1 ? 
HETATM 2651 O  O     . HOH   G 7 .   ? 43.044 -23.566 4.963   1    59.74  ? 567 HOH   A O     1 ? 
HETATM 2652 O  O     . HOH   G 7 .   ? 15.146 -16.562 -5.589  1    53.82  ? 568 HOH   A O     1 ? 
HETATM 2653 O  O     . HOH   G 7 .   ? 24.285 -28.048 -3.797  1    52.78  ? 569 HOH   A O     1 ? 
HETATM 2654 O  O     . HOH   G 7 .   ? 39.092 -20.686 -25.145 1    89.12  ? 570 HOH   A O     1 ? 
HETATM 2655 O  O     . HOH   G 7 .   ? 29.02  -10.374 10.167  1    46.93  ? 571 HOH   A O     1 ? 
HETATM 2656 O  O     . HOH   G 7 .   ? 41.744 -21.872 -4.266  1    58.44  ? 572 HOH   A O     1 ? 
HETATM 2657 O  O     . HOH   G 7 .   ? 33.689 -5.806  -19.779 1    67.03  ? 573 HOH   A O     1 ? 
HETATM 2658 O  O     . HOH   G 7 .   ? 33.736 -19.121 15.225  1    73.91  ? 574 HOH   A O     1 ? 
HETATM 2659 O  O     . HOH   G 7 .   ? 38.989 -23.728 -9.259  1    73.12  ? 575 HOH   A O     1 ? 
HETATM 2660 O  O     . HOH   G 7 .   ? 18.626 -10.964 1.006   1    59.51  ? 576 HOH   A O     1 ? 
HETATM 2661 O  O     . HOH   G 7 .   ? 36.876 -27.331 3.775   1    60.96  ? 577 HOH   A O     1 ? 
HETATM 2662 O  O     . HOH   G 7 .   ? 18.555 -15.173 9.269   1    50.73  ? 578 HOH   A O     1 ? 
HETATM 2663 O  O     . HOH   G 7 .   ? 38.193 -1.926  13.111  1    85.57  ? 579 HOH   A O     1 ? 
HETATM 2664 O  O     . HOH   G 7 .   ? 29.115 -27.471 -17.586 1    57.03  ? 580 HOH   A O     1 ? 
HETATM 2665 O  O     . HOH   G 7 .   ? 35.975 -15.922 -19.776 1    69.25  ? 581 HOH   A O     1 ? 
HETATM 2666 O  O     . HOH   G 7 .   ? 19.921 4.34    6.751   1    83.58  ? 582 HOH   A O     1 ? 
HETATM 2667 O  O     . HOH   G 7 .   ? 37.505 -4.634  -5.617  1    68.54  ? 583 HOH   A O     1 ? 
HETATM 2668 O  O     . HOH   G 7 .   ? 15.718 -4.889  -3.122  1    66.91  ? 584 HOH   A O     1 ? 
HETATM 2669 O  O     . HOH   G 7 .   ? 34.375 1.917   -9.541  1    67.7   ? 585 HOH   A O     1 ? 
HETATM 2670 O  O     . HOH   G 7 .   ? 37.907 -16.671 15.783  1    63.02  ? 586 HOH   A O     1 ? 
HETATM 2671 O  O     . HOH   G 7 .   ? 47.912 -16.636 -4.094  1    79.19  ? 587 HOH   A O     1 ? 
HETATM 2672 O  O     . HOH   G 7 .   ? 37.686 -26.314 -8.183  1    75.04  ? 588 HOH   A O     1 ? 
HETATM 2673 O  O     . HOH   G 7 .   ? 16.653 -13.697 1.62    1    85.67  ? 589 HOH   A O     1 ? 
HETATM 2674 O  O     . HOH   G 7 .   ? 15.802 -9.758  -4.421  1    55.33  ? 590 HOH   A O     1 ? 
HETATM 2675 O  O     . HOH   G 7 .   ? 35.844 2.314   -11.755 1    66.93  ? 591 HOH   A O     1 ? 
HETATM 2676 O  O     . HOH   G 7 .   ? 22.88  -14.065 15.762  1    50.58  ? 592 HOH   A O     1 ? 
HETATM 2677 O  O     . HOH   G 7 .   ? 35.444 0.608   -15.617 1    68.22  ? 593 HOH   A O     1 ? 
HETATM 2678 O  O     . HOH   G 7 .   ? 40.057 -27.45  -2.018  1    81.54  ? 594 HOH   A O     1 ? 
HETATM 2679 O  O     . HOH   G 7 .   ? 17.77  -15.081 -29.671 1    94.71  ? 595 HOH   A O     1 ? 
HETATM 2680 O  O     . HOH   G 7 .   ? 25.64  -9.36   -19.298 1    73.15  ? 596 HOH   A O     1 ? 
HETATM 2681 O  O     . HOH   G 7 .   ? 14.956 5.036   -1.19   1    83.97  ? 597 HOH   A O     1 ? 
HETATM 2682 O  O     . HOH   G 7 .   ? 16.591 -23.884 -19.215 1    72.52  ? 598 HOH   A O     1 ? 
HETATM 2683 O  O     . HOH   G 7 .   ? 20.481 4.746   -15.826 1    63.72  ? 599 HOH   A O     1 ? 
HETATM 2684 O  O     . HOH   G 7 .   ? 27.823 -25.507 -1.554  1    50.39  ? 600 HOH   A O     1 ? 
HETATM 2685 O  O     . HOH   G 7 .   ? 31.413 10.512  -43.386 1    88.34  ? 601 HOH   A O     1 ? 
HETATM 2686 O  O     . HOH   G 7 .   ? 29.027 -2.096  13.885  1    71.47  ? 602 HOH   A O     1 ? 
HETATM 2687 O  O     . HOH   G 7 .   ? 38.687 -19.107 16.752  1    84.27  ? 603 HOH   A O     1 ? 
HETATM 2688 O  O     . HOH   G 7 .   ? 38.495 -27.033 8.483   1    70.77  ? 604 HOH   A O     1 ? 
HETATM 2689 O  O     . HOH   G 7 .   ? 25.575 -25.458 -19.226 1    60.65  ? 605 HOH   A O     1 ? 
HETATM 2690 O  O     . HOH   G 7 .   ? 50.153 -9.575  -1.162  1    79.48  ? 606 HOH   A O     1 ? 
HETATM 2691 O  O     . HOH   G 7 .   ? 19.423 -2.275  -3.88   1    50.66  ? 607 HOH   A O     1 ? 
HETATM 2692 O  O     . HOH   G 7 .   ? 33.045 -10.519 8.332   1    49.49  ? 608 HOH   A O     1 ? 
HETATM 2693 O  O     . HOH   G 7 .   ? 31.483 -11.391 10.478  1    70.8   ? 609 HOH   A O     1 ? 
HETATM 2694 O  O     . HOH   G 7 .   ? 23.064 -19.816 -22.216 1    75.1   ? 610 HOH   A O     1 ? 
HETATM 2695 O  O     . HOH   G 7 .   ? 25.116 -25.116 -0      0.50 95.33  ? 611 HOH   A O     1 ? 
HETATM 2696 O  O     . HOH   G 7 .   ? 35.842 1.676   9.915   1    82.01  ? 612 HOH   A O     1 ? 
HETATM 2697 O  O     . HOH   G 7 .   ? 14.391 -8.373  -7.043  1    79.39  ? 613 HOH   A O     1 ? 
HETATM 2698 O  O     . HOH   G 7 .   ? 25.761 -15.365 15.327  1    58.57  ? 614 HOH   A O     1 ? 
HETATM 2699 O  O     . HOH   G 7 .   ? 11.585 5.616   -8.252  1    94.24  ? 615 HOH   A O     1 ? 
HETATM 2700 O  O     . HOH   G 7 .   ? 23.246 3.246   -31.973 1    84.54  ? 616 HOH   A O     1 ? 
HETATM 2701 O  O     . HOH   G 7 .   ? 29.756 -24.828 1.893   1    65.29  ? 617 HOH   A O     1 ? 
HETATM 2702 O  O     . HOH   G 7 .   ? 40.781 -9.208  3.089   1    60.26  ? 618 HOH   A O     1 ? 
HETATM 2703 O  O     . HOH   G 7 .   ? 25.17  -30.2   -18.54  1    90.44  ? 619 HOH   A O     1 ? 
HETATM 2704 O  O     . HOH   G 7 .   ? 15.363 2.624   -2.255  1    84.6   ? 620 HOH   A O     1 ? 
HETATM 2705 O  O     . HOH   G 7 .   ? 19.373 -9.344  3.405   1    65.62  ? 621 HOH   A O     1 ? 
HETATM 2706 O  O     . HOH   G 7 .   ? 15.868 -14.029 9.462   1    64.44  ? 622 HOH   A O     1 ? 
HETATM 2707 O  O     . HOH   G 7 .   ? 38.237 11.559  0.211   1    79.53  ? 623 HOH   A O     1 ? 
HETATM 2708 O  O     . HOH   G 7 .   ? 11.957 6.272   -4.951  1    91.74  ? 624 HOH   A O     1 ? 
HETATM 2709 O  O     . HOH   G 7 .   ? 16.527 -6.944  -29.883 1    104.09 ? 625 HOH   A O     1 ? 
HETATM 2710 O  O     . HOH   G 7 .   ? 43.511 -8.181  -11.028 1    84.55  ? 626 HOH   A O     1 ? 
HETATM 2711 O  O     . HOH   G 7 .   ? 36.751 22.556  -19.714 1    70.37  ? 627 HOH   A O     1 ? 
HETATM 2712 O  O     . HOH   G 7 .   ? 22.555 -6.223  -43.581 1    85.32  ? 628 HOH   A O     1 ? 
HETATM 2713 O  O     . HOH   G 7 .   ? 9.311  4.582   -32.179 1    76.2   ? 629 HOH   A O     1 ? 
HETATM 2714 O  O     . HOH   G 7 .   ? 37.939 35.224  -12.501 1    84.68  ? 630 HOH   A 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     . SER   A 27  ? 1.0364 0.8842 1.1762 0.0397  0.0063  0.0566  27  SER   A N     
2    C  CA    . SER   A 27  ? 1.0376 0.8897 1.1839 0.0442  -0.0026 0.065   27  SER   A CA    
3    C  C     . SER   A 27  ? 1.0395 0.8926 1.1677 0.0401  -0.0104 0.0723  27  SER   A C     
4    O  O     . SER   A 27  ? 1.0356 0.8967 1.1683 0.0423  -0.0184 0.0772  27  SER   A O     
5    C  CB    . SER   A 27  ? 1.0591 0.8991 1.2163 0.049   -0.0056 0.0731  27  SER   A CB    
6    O  OG    . SER   A 27  ? 1.1042 0.9279 1.2457 0.0452  -0.0077 0.0807  27  SER   A OG    
7    N  N     . ALA   A 28  ? 1.0432 0.8874 1.1512 0.0339  -0.0077 0.0729  28  ALA   A N     
8    C  CA    . ALA   A 28  ? 1.0502 0.8915 1.1368 0.0293  -0.013  0.0787  28  ALA   A CA    
9    C  C     . ALA   A 28  ? 1.0394 0.8972 1.1255 0.0284  -0.0146 0.0737  28  ALA   A C     
10   O  O     . ALA   A 28  ? 1.0436 0.9019 1.1188 0.0267  -0.0225 0.0794  28  ALA   A O     
11   C  CB    . ALA   A 28  ? 1.0606 0.8892 1.1283 0.0234  -0.006  0.0787  28  ALA   A CB    
12   N  N     . ILE   A 29  ? 1.0227 0.893  1.1199 0.0293  -0.0076 0.0633  29  ILE   A N     
13   C  CA    . ILE   A 29  ? 1.0136 0.8996 1.1115 0.0287  -0.0081 0.0582  29  ILE   A CA    
14   C  C     . ILE   A 29  ? 1.0091 0.9044 1.1195 0.033   -0.0162 0.0624  29  ILE   A C     
15   O  O     . ILE   A 29  ? 1.0097 0.9108 1.1125 0.0308  -0.0219 0.065   29  ILE   A O     
16   C  CB    . ILE   A 29  ? 1.0063 0.9015 1.1117 0.0283  0.0007  0.0466  29  ILE   A CB    
17   C  CG1   . ILE   A 29  ? 1.0161 0.9076 1.1075 0.0224  0.0062  0.0437  29  ILE   A CG1   
18   C  CG2   . ILE   A 29  ? 1.0035 0.9153 1.1174 0.0304  0.0002  0.0414  29  ILE   A CG2   
19   C  CD1   . ILE   A 29  ? 1.0326 0.9127 1.1249 0.0207  0.0118  0.0428  29  ILE   A CD1   
20   N  N     . ASP   A 30  ? 1.0003 0.8963 1.1305 0.0389  -0.0167 0.0636  30  ASP   A N     
21   C  CA    . ASP   A 30  ? 0.9977 0.9035 1.1447 0.0435  -0.0237 0.0685  30  ASP   A CA    
22   C  C     . ASP   A 30  ? 0.9975 0.8976 1.1359 0.0415  -0.0366 0.0806  30  ASP   A C     
23   O  O     . ASP   A 30  ? 0.9932 0.9033 1.1377 0.0419  -0.0442 0.0844  30  ASP   A O     
24   C  CB    . ASP   A 30  ? 1.0249 0.9309 1.1962 0.0507  -0.0199 0.0677  30  ASP   A CB    
25   C  CG    . ASP   A 30  ? 1.0959 1.0127 1.2802 0.0538  -0.0101 0.0567  30  ASP   A CG    
26   O  OD1   . ASP   A 30  ? 1.1004 1.031  1.2887 0.0539  -0.0108 0.0546  30  ASP   A OD1   
27   O  OD2   . ASP   A 30  ? 1.1311 1.0414 1.3204 0.0558  -0.0017 0.0504  30  ASP   A OD2   
28   N  N     . VAL   A 31  ? 1.0036 0.8868 1.1262 0.0388  -0.0392 0.0867  31  VAL   A N     
29   C  CA    . VAL   A 31  ? 1.0164 0.8902 1.1255 0.036   -0.0519 0.0984  31  VAL   A CA    
30   C  C     . VAL   A 31  ? 1.0254 0.8995 1.111  0.0294  -0.0552 0.0979  31  VAL   A C     
31   O  O     . VAL   A 31  ? 1.024  0.9021 1.1085 0.028   -0.0664 0.1038  31  VAL   A O     
32   C  CB    . VAL   A 31  ? 1.0353 0.8885 1.1322 0.035   -0.0527 0.1052  31  VAL   A CB    
33   C  CG1   . VAL   A 31  ? 1.0518 0.8926 1.1297 0.0312  -0.0665 0.1174  31  VAL   A CG1   
34   C  CG2   . VAL   A 31  ? 1.0343 0.8865 1.1559 0.042   -0.0502 0.1063  31  VAL   A CG2   
35   N  N     . VAL   A 32  ? 1.0305 0.9007 1.099  0.0253  -0.0453 0.0908  32  VAL   A N     
36   C  CA    . VAL   A 32  ? 1.0387 0.9076 1.0846 0.0193  -0.0458 0.0894  32  VAL   A CA    
37   C  C     . VAL   A 32  ? 1.0334 0.9214 1.0904 0.02    -0.0471 0.0843  32  VAL   A C     
38   O  O     . VAL   A 32  ? 1.0345 0.9222 1.0784 0.0161  -0.0541 0.0872  32  VAL   A O     
39   C  CB    . VAL   A 32  ? 1.0506 0.9101 1.079  0.0154  -0.0339 0.0841  32  VAL   A CB    
40   C  CG1   . VAL   A 32  ? 1.0642 0.9196 1.0685 0.0096  -0.0335 0.0835  32  VAL   A CG1   
41   C  CG2   . VAL   A 32  ? 1.0627 0.903  1.0811 0.0146  -0.0321 0.0898  32  VAL   A CG2   
42   N  N     . ALA   A 33  ? 1.0312 0.9344 1.1119 0.0248  -0.0411 0.0773  33  ALA   A N     
43   C  CA    . ALA   A 33  ? 1.0401 0.961  1.132  0.0257  -0.0416 0.0729  33  ALA   A CA    
44   C  C     . ALA   A 33  ? 1.0587 0.9863 1.1627 0.0271  -0.0538 0.0808  33  ALA   A C     
45   O  O     . ALA   A 33  ? 1.0556 0.9953 1.1641 0.0261  -0.0561 0.0792  33  ALA   A O     
46   C  CB    . ALA   A 33  ? 1.0275 0.96   1.1385 0.0302  -0.0315 0.0637  33  ALA   A CB    
47   N  N     . GLU   A 34  ? 1.077  0.9969 1.1874 0.0293  -0.0622 0.0899  34  GLU   A N     
48   C  CA    . GLU   A 34  ? 1.0954 1.0214 1.2193 0.0302  -0.0758 0.0991  34  GLU   A CA    
49   C  C     . GLU   A 34  ? 1.1256 1.0418 1.2241 0.0227  -0.0882 0.106   34  GLU   A C     
50   O  O     . GLU   A 34  ? 1.1244 1.0456 1.232  0.0219  -0.1013 0.1138  34  GLU   A O     
51   C  CB    . GLU   A 34  ? 1.1254 1.0481 1.2698 0.036   -0.0805 0.1069  34  GLU   A CB    
52   C  CG    . GLU   A 34  ? 1.1884 1.1287 1.3693 0.0428  -0.0809 0.1079  34  GLU   A CG    
53   C  CD    . GLU   A 34  ? 1.2857 1.2401 1.4795 0.0461  -0.0666 0.096   34  GLU   A CD    
54   O  OE1   . GLU   A 34  ? 1.3085 1.2581 1.496  0.0471  -0.0545 0.0874  34  GLU   A OE1   
55   O  OE2   . GLU   A 34  ? 1.3061 1.276  1.516  0.0471  -0.0678 0.0957  34  GLU   A OE2   
56   N  N     . LYS   A 35  ? 1.1499 1.0516 1.217  0.0171  -0.0841 0.1034  35  LYS   A N     
57   C  CA    . LYS   A 35  ? 1.1803 1.0693 1.2187 0.0096  -0.0936 0.1084  35  LYS   A CA    
58   C  C     . LYS   A 35  ? 1.1952 1.0963 1.2322 0.0065  -0.0936 0.1034  35  LYS   A C     
59   O  O     . LYS   A 35  ? 1.1832 1.0989 1.2337 0.0094  -0.0829 0.0946  35  LYS   A O     
60   C  CB    . LYS   A 35  ? 1.2173 1.0847 1.2235 0.0054  -0.0868 0.1077  35  LYS   A CB    
61   C  CG    . LYS   A 35  ? 1.2645 1.1192 1.2721 0.0082  -0.0873 0.1135  35  LYS   A CG    
62   C  CD    . LYS   A 35  ? 1.3341 1.1666 1.3102 0.0037  -0.0801 0.1137  35  LYS   A CD    
63   C  CE    . LYS   A 35  ? 1.3813 1.2016 1.3602 0.0065  -0.0798 0.1195  35  LYS   A CE    
64   N  NZ    . LYS   A 35  ? 1.4268 1.2239 1.3743 0.0018  -0.0725 0.1209  35  LYS   A NZ    
65   N  N     . PRO   A 36  ? 1.2171 1.1121 1.2388 0.0006  -0.1066 0.1093  36  PRO   A N     
66   C  CA    . PRO   A 36  ? 1.2207 1.1269 1.2429 -0.0026 -0.1075 0.1052  36  PRO   A CA    
67   C  C     . PRO   A 36  ? 1.2338 1.1392 1.2401 -0.0043 -0.0928 0.0949  36  PRO   A C     
68   O  O     . PRO   A 36  ? 1.2256 1.1467 1.2512 0.0003  -0.0823 0.0875  36  PRO   A O     
69   C  CB    . PRO   A 36  ? 1.2404 1.1343 1.2434 -0.0099 -0.1251 0.1141  36  PRO   A CB    
70   C  CG    . PRO   A 36  ? 1.2604 1.1308 1.2395 -0.012  -0.1293 0.1206  36  PRO   A CG    
71   C  CD    . PRO   A 36  ? 1.2271 1.1039 1.2301 -0.004  -0.1219 0.1204  36  PRO   A CD    
72   N  N     . SER   A 37  ? 1.2518 1.1386 1.2237 -0.0107 -0.0918 0.0945  37  SER   A N     
73   C  CA    . SER   A 37  ? 1.2649 1.1479 1.2195 -0.013  -0.0788 0.0864  37  SER   A CA    
74   C  C     . SER   A 37  ? 1.2826 1.1541 1.211  -0.0205 -0.0855 0.0879  37  SER   A C     
75   O  O     . SER   A 37  ? 1.2795 1.1632 1.2185 -0.0218 -0.0919 0.0876  37  SER   A O     
76   C  CB    . SER   A 37  ? 1.2619 1.167  1.2408 -0.0084 -0.0688 0.078   37  SER   A CB    
77   O  OG    . SER   A 37  ? 1.293  1.1962 1.2578 -0.0108 -0.0585 0.0714  37  SER   A OG    
78   N  N     . VAL   A 38  ? 1.2989 1.146  1.1927 -0.0256 -0.0833 0.0894  38  VAL   A N     
79   C  CA    . VAL   A 38  ? 1.3197 1.1519 1.1843 -0.0331 -0.0881 0.0899  38  VAL   A CA    
80   C  C     . VAL   A 38  ? 1.3234 1.1603 1.1845 -0.0332 -0.0739 0.081   38  VAL   A C     
81   O  O     . VAL   A 38  ? 1.3295 1.1569 1.1783 -0.0325 -0.0598 0.0772  38  VAL   A O     
82   C  CB    . VAL   A 38  ? 1.3527 1.1537 1.1783 -0.0389 -0.0911 0.0952  38  VAL   A CB    
83   C  CG1   . VAL   A 38  ? 1.3757 1.1592 1.1692 -0.0473 -0.0974 0.0955  38  VAL   A CG1   
84   C  CG2   . VAL   A 38  ? 1.3603 1.1565 1.1904 -0.0384 -0.1051 0.1047  38  VAL   A CG2   
85   N  N     . ARG   A 39  ? 1.3176 1.1692 1.1909 -0.0339 -0.0776 0.0784  39  ARG   A N     
86   C  CA    . ARG   A 39  ? 1.3234 1.18   1.1948 -0.0339 -0.0655 0.0708  39  ARG   A CA    
87   C  C     . ARG   A 39  ? 1.3393 1.1716 1.1737 -0.0407 -0.0631 0.0701  39  ARG   A C     
88   O  O     . ARG   A 39  ? 1.3495 1.1675 1.1638 -0.0471 -0.0757 0.0747  39  ARG   A O     
89   C  CB    . ARG   A 39  ? 1.3354 1.216  1.2333 -0.0321 -0.0693 0.0685  39  ARG   A CB    
90   C  CG    . ARG   A 39  ? 1.3738 1.2769 1.3067 -0.0248 -0.0675 0.0675  39  ARG   A CG    
91   C  CD    . ARG   A 39  ? 1.4137 1.3369 1.3714 -0.0238 -0.0752 0.0684  39  ARG   A CD    
92   N  NE    . ARG   A 39  ? 1.447  1.3834 1.4323 -0.0186 -0.0799 0.0719  39  ARG   A NE    
93   C  CZ    . ARG   A 39  ? 1.4818 1.4143 1.4709 -0.0198 -0.0935 0.08    39  ARG   A CZ    
94   N  NH1   . ARG   A 39  ? 1.4957 1.4107 1.4604 -0.0268 -0.1048 0.0854  39  ARG   A NH1   
95   N  NH2   . ARG   A 39  ? 1.4679 1.4131 1.4849 -0.0141 -0.0959 0.0829  39  ARG   A NH2   
96   N  N     . LEU   A 40  ? 1.3376 1.1645 1.1631 -0.0396 -0.0468 0.0645  40  LEU   A N     
97   C  CA    . LEU   A 40  ? 1.3544 1.1574 1.1457 -0.0451 -0.0407 0.0629  40  LEU   A CA    
98   C  C     . LEU   A 40  ? 1.3418 1.1545 1.1392 -0.0455 -0.0365 0.0576  40  LEU   A C     
99   O  O     . LEU   A 40  ? 1.3293 1.1605 1.1497 -0.0403 -0.0269 0.0531  40  LEU   A O     
100  C  CB    . LEU   A 40  ? 1.3682 1.1563 1.1459 -0.0435 -0.0242 0.0612  40  LEU   A CB    
101  C  CG    . LEU   A 40  ? 1.4151 1.1699 1.1504 -0.0496 -0.0191 0.0622  40  LEU   A CG    
102  C  CD1   . LEU   A 40  ? 1.4369 1.1724 1.1475 -0.0555 -0.035  0.069   40  LEU   A CD1   
103  C  CD2   . LEU   A 40  ? 1.4311 1.1745 1.1593 -0.0471 -0.0007 0.0608  40  LEU   A CD2   
104  N  N     . THR   A 41  ? 1.344  1.1441 1.1209 -0.0521 -0.0446 0.0585  41  THR   A N     
105  C  CA    . THR   A 41  ? 1.3347 1.1419 1.1155 -0.0532 -0.0416 0.0541  41  THR   A CA    
106  C  C     . THR   A 41  ? 1.3396 1.1261 1.095  -0.0546 -0.0255 0.0499  41  THR   A C     
107  O  O     . THR   A 41  ? 1.3599 1.12   1.0847 -0.058  -0.0217 0.0513  41  THR   A O     
108  C  CB    . THR   A 41  ? 1.3511 1.1586 1.1288 -0.0594 -0.0596 0.0574  41  THR   A CB    
109  O  OG1   . THR   A 41  ? 1.344  1.1811 1.1577 -0.0555 -0.0636 0.0567  41  THR   A OG1   
110  C  CG2   . THR   A 41  ? 1.3704 1.1556 1.1168 -0.0669 -0.0598 0.0555  41  THR   A CG2   
111  N  N     . PRO   A 42  ? 1.3177 1.1151 1.0856 -0.0517 -0.015  0.045   42  PRO   A N     
112  C  CA    . PRO   A 42  ? 1.3221 1.1009 1.0701 -0.0521 0.0017  0.0414  42  PRO   A CA    
113  C  C     . PRO   A 42  ? 1.3381 1.0838 1.0444 -0.0599 0.0006  0.0416  42  PRO   A C     
114  O  O     . PRO   A 42  ? 1.3482 1.0722 1.0324 -0.0604 0.0153  0.0397  42  PRO   A O     
115  C  CB    . PRO   A 42  ? 1.3164 1.1153 1.0881 -0.0482 0.0082  0.0374  42  PRO   A CB    
116  C  CG    . PRO   A 42  ? 1.3012 1.1303 1.1076 -0.0437 0       0.0383  42  PRO   A CG    
117  C  CD    . PRO   A 42  ? 1.2871 1.1137 1.0882 -0.0476 -0.0168 0.0428  42  PRO   A CD    
118  N  N     . THR   A 43  ? 1.3402 1.0809 1.0353 -0.0664 -0.0167 0.0441  43  THR   A N     
119  C  CA    . THR   A 43  ? 1.3686 1.076  1.0211 -0.0753 -0.021  0.0445  43  THR   A CA    
120  C  C     . THR   A 43  ? 1.3855 1.069  1.01   -0.0781 -0.0224 0.0484  43  THR   A C     
121  O  O     . THR   A 43  ? 1.4081 1.0593 0.9943 -0.0824 -0.0138 0.0471  43  THR   A O     
122  C  CB    . THR   A 43  ? 1.3801 1.0913 1.0324 -0.0819 -0.0405 0.0463  43  THR   A CB    
123  O  OG1   . THR   A 43  ? 1.3722 1.1101 1.0565 -0.0782 -0.0389 0.0435  43  THR   A OG1   
124  C  CG2   . THR   A 43  ? 1.4103 1.0865 1.0183 -0.0917 -0.0437 0.0451  43  THR   A CG2   
125  N  N     . MET   A 44  ? 1.3746 1.0729 1.0178 -0.0753 -0.0321 0.0532  44  MET   A N     
126  C  CA    . MET   A 44  ? 1.3968 1.0751 1.0176 -0.077  -0.0335 0.0578  44  MET   A CA    
127  C  C     . MET   A 44  ? 1.4026 1.0697 1.0158 -0.0725 -0.0103 0.0549  44  MET   A C     
128  O  O     . MET   A 44  ? 1.4271 1.0635 1.0042 -0.0764 -0.0044 0.0563  44  MET   A O     
129  C  CB    . MET   A 44  ? 1.3931 1.0936 1.043  -0.0732 -0.0465 0.0633  44  MET   A CB    
130  C  CG    . MET   A 44  ? 1.4182 1.1379 1.089  -0.0753 -0.0669 0.0664  44  MET   A CG    
131  S  SD    . MET   A 44  ? 1.4755 1.2261 1.1898 -0.0681 -0.0762 0.0715  44  MET   A SD    
132  C  CE    . MET   A 44  ? 1.4813 1.205  1.1656 -0.0725 -0.0863 0.0795  44  MET   A CE    
133  N  N     . MET   A 45  ? 1.3794 1.0711 1.0266 -0.0647 0.0026  0.0511  45  MET   A N     
134  C  CA    . MET   A 45  ? 1.3833 1.0698 1.0321 -0.06   0.0243  0.0487  45  MET   A CA    
135  C  C     . MET   A 45  ? 1.4177 1.0744 1.0326 -0.0636 0.039   0.0453  45  MET   A C     
136  O  O     . MET   A 45  ? 1.4329 1.0689 1.0291 -0.0633 0.0544  0.0456  45  MET   A O     
137  C  CB    . MET   A 45  ? 1.354  1.0736 1.0465 -0.0521 0.0316  0.0455  45  MET   A CB    
138  C  CG    . MET   A 45  ? 1.3469 1.0912 1.071  -0.0473 0.0245  0.0479  45  MET   A CG    
139  S  SD    . MET   A 45  ? 1.3489 1.1275 1.1178 -0.0394 0.0329  0.0436  45  MET   A SD    
140  C  CE    . MET   A 45  ? 1.3229 1.1049 1.1059 -0.0349 0.042   0.0452  45  MET   A CE    
141  N  N     . LEU   A 46  ? 1.4272 1.0813 1.0346 -0.067  0.0352  0.0422  46  LEU   A N     
142  C  CA    . LEU   A 46  ? 1.4594 1.0845 1.0344 -0.0707 0.0484  0.0384  46  LEU   A CA    
143  C  C     . LEU   A 46  ? 1.504  1.0889 1.0281 -0.0787 0.0465  0.0405  46  LEU   A C     
144  O  O     . LEU   A 46  ? 1.5289 1.0856 1.0249 -0.0797 0.0646  0.0384  46  LEU   A O     
145  C  CB    . LEU   A 46  ? 1.4569 1.0881 1.0349 -0.0735 0.0409  0.0352  46  LEU   A CB    
146  C  CG    . LEU   A 46  ? 1.4657 1.1003 1.055  -0.0693 0.0586  0.0303  46  LEU   A CG    
147  C  CD1   . LEU   A 46  ? 1.4692 1.1077 1.0585 -0.0731 0.0489  0.0279  46  LEU   A CD1   
148  C  CD2   . LEU   A 46  ? 1.4954 1.0957 1.052  -0.0703 0.0797  0.0281  46  LEU   A CD2   
149  N  N     . TYR   A 47  ? 1.5123 1.0939 1.0245 -0.0843 0.0248  0.0451  47  TYR   A N     
150  C  CA    . TYR   A 47  ? 1.5505 1.0935 1.0127 -0.0927 0.0197  0.048   47  TYR   A CA    
151  C  C     . TYR   A 47  ? 1.5636 1.1018 1.0229 -0.0904 0.0223  0.0532  47  TYR   A C     
152  O  O     . TYR   A 47  ? 1.5669 1.1043 1.0336 -0.0848 0.0427  0.052   47  TYR   A O     
153  C  CB    . TYR   A 47  ? 1.5562 1.0958 1.0054 -0.1011 -0.0068 0.0511  47  TYR   A CB    
154  N  N     . ASP   A 53  ? 1.7582 0.9913 0.9368 -0.0933 0.247   0.0676  53  ASP   A N     
155  C  CA    . ASP   A 53  ? 1.7673 0.9951 0.9381 -0.095  0.2402  0.0756  53  ASP   A CA    
156  C  C     . ASP   A 53  ? 1.7209 0.9981 0.958  -0.0872 0.232   0.0788  53  ASP   A C     
157  O  O     . ASP   A 53  ? 1.7192 0.9964 0.9666 -0.0849 0.2422  0.0839  53  ASP   A O     
158  C  CB    . ASP   A 53  ? 1.8227 1.0272 0.9456 -0.1046 0.2117  0.0794  53  ASP   A CB    
159  C  CG    . ASP   A 53  ? 1.9048 1.1029 1.0185 -0.1065 0.2024  0.0884  53  ASP   A CG    
160  O  OD1   . ASP   A 53  ? 1.9329 1.1027 1.0219 -0.1072 0.2245  0.0915  53  ASP   A OD1   
161  O  OD2   . ASP   A 53  ? 1.9267 1.1477 1.059  -0.107  0.1738  0.0926  53  ASP   A OD2   
162  N  N     . GLY   A 54  ? 1.6805 0.9972 0.9597 -0.0835 0.2139  0.0757  54  GLY   A N     
163  C  CA    . GLY   A 54  ? 1.6362 0.9989 0.976  -0.0766 0.2046  0.0776  54  GLY   A CA    
164  C  C     . GLY   A 54  ? 1.6162 0.9915 0.9593 -0.0788 0.1749  0.0829  54  GLY   A C     
165  O  O     . GLY   A 54  ? 1.5944 0.9998 0.9796 -0.0738 0.1688  0.0856  54  GLY   A O     
166  N  N     . SER   A 55  ? 1.6196 0.971  0.9187 -0.0866 0.1559  0.0846  55  SER   A N     
167  C  CA    . SER   A 55  ? 1.5988 0.9597 0.8991 -0.0893 0.1263  0.0904  55  SER   A CA    
168  C  C     . SER   A 55  ? 1.5383 0.9449 0.8897 -0.0845 0.1073  0.0877  55  SER   A C     
169  O  O     . SER   A 55  ? 1.5224 0.9528 0.9023 -0.0818 0.0908  0.0919  55  SER   A O     
170  C  CB    . SER   A 55  ? 1.6491 0.9714 0.8887 -0.0995 0.1111  0.093   55  SER   A CB    
171  O  OG    . SER   A 55  ? 1.6735 1.005  0.9159 -0.1022 0.0814  0.0996  55  SER   A OG    
172  N  N     . HIS   A 56  ? 1.5003 0.9181 0.8627 -0.0833 0.111   0.0806  56  HIS   A N     
173  C  CA    . HIS   A 56  ? 1.4493 0.9076 0.8567 -0.0791 0.0961  0.0774  56  HIS   A CA    
174  C  C     . HIS   A 56  ? 1.3887 0.8853 0.8532 -0.0701 0.1023  0.0769  56  HIS   A C     
175  O  O     . HIS   A 56  ? 1.361  0.8904 0.8618 -0.0668 0.0861  0.0767  56  HIS   A O     
176  C  CB    . HIS   A 56  ? 1.4605 0.9172 0.8628 -0.08   0.1023  0.0701  56  HIS   A CB    
177  C  CG    . HIS   A 56  ? 1.4842 0.9414 0.9001 -0.0748 0.1309  0.0655  56  HIS   A CG    
178  N  ND1   . HIS   A 56  ? 1.5294 0.9551 0.9168 -0.0759 0.1541  0.0666  56  HIS   A ND1   
179  C  CD2   . HIS   A 56  ? 1.474  0.959  0.9293 -0.0687 0.1392  0.0605  56  HIS   A CD2   
180  C  CE1   . HIS   A 56  ? 1.5219 0.9588 0.9354 -0.0701 0.1757  0.0624  56  HIS   A CE1   
181  N  NE2   . HIS   A 56  ? 1.4916 0.964  0.9459 -0.0657 0.1668  0.0588  56  HIS   A NE2   
182  N  N     . LEU   A 57  ? 1.3643 0.8555 0.8358 -0.0667 0.1259  0.0769  57  LEU   A N     
183  C  CA    . LEU   A 57  ? 1.3217 0.844  0.843  -0.0594 0.1334  0.0769  57  LEU   A CA    
184  C  C     . LEU   A 57  ? 1.296  0.8277 0.829  -0.0588 0.1181  0.0828  57  LEU   A C     
185  O  O     . LEU   A 57  ? 1.2717 0.8364 0.8481 -0.0536 0.1111  0.0821  57  LEU   A O     
186  C  CB    . LEU   A 57  ? 1.3301 0.837  0.8485 -0.0575 0.1625  0.0768  57  LEU   A CB    
187  C  CG    . LEU   A 57  ? 1.3347 0.8587 0.8845 -0.0523 0.1809  0.0715  57  LEU   A CG    
188  C  CD1   . LEU   A 57  ? 1.3385 0.8706 0.8881 -0.0527 0.1734  0.0659  57  LEU   A CD1   
189  C  CD2   . LEU   A 57  ? 1.3561 0.8522 0.8866 -0.0527 0.2096  0.0722  57  LEU   A CD2   
190  N  N     . LEU   A 58  ? 1.2981 0.7994 0.7911 -0.0642 0.1128  0.0888  58  LEU   A N     
191  C  CA    . LEU   A 58  ? 1.282  0.7879 0.7821 -0.0639 0.0983  0.0955  58  LEU   A CA    
192  C  C     . LEU   A 58  ? 1.25   0.7766 0.7648 -0.064  0.0708  0.0964  58  LEU   A C     
193  O  O     . LEU   A 58  ? 1.2309 0.7804 0.7779 -0.0599 0.0603  0.0989  58  LEU   A O     
194  C  CB    . LEU   A 58  ? 1.319  0.7838 0.769  -0.07   0.1008  0.1024  58  LEU   A CB    
195  C  CG    . LEU   A 58  ? 1.3486 0.8022 0.8001 -0.0682 0.1214  0.1057  58  LEU   A CG    
196  C  CD1   . LEU   A 58  ? 1.3549 0.8085 0.8169 -0.0654 0.1493  0.1001  58  LEU   A CD1   
197  C  CD2   . LEU   A 58  ? 1.3905 0.802  0.7887 -0.0748 0.1216  0.113   58  LEU   A CD2   
198  N  N     . LYS   A 59  ? 1.242  0.7599 0.7338 -0.0686 0.0597  0.0945  59  LYS   A N     
199  C  CA    . LYS   A 59  ? 1.2223 0.7601 0.7295 -0.0691 0.0344  0.0955  59  LYS   A CA    
200  C  C     . LYS   A 59  ? 1.1625 0.7421 0.7229 -0.0619 0.0348  0.0897  59  LYS   A C     
201  O  O     . LYS   A 59  ? 1.1456 0.7496 0.7357 -0.0588 0.0191  0.0916  59  LYS   A O     
202  C  CB    . LYS   A 59  ? 1.2878 0.8045 0.7567 -0.0768 0.024   0.0946  59  LYS   A CB    
203  C  CG    . LYS   A 59  ? 1.3538 0.8931 0.8424 -0.0775 -0.0011 0.0954  59  LYS   A CG    
204  C  CD    . LYS   A 59  ? 1.447  0.9663 0.9003 -0.0857 -0.0113 0.094   59  LYS   A CD    
205  C  CE    . LYS   A 59  ? 1.488  1.0362 0.9713 -0.0852 -0.0314 0.0934  59  LYS   A CE    
206  N  NZ    . LYS   A 59  ? 1.5415 1.0709 0.9923 -0.0938 -0.0425 0.0921  59  LYS   A NZ    
207  N  N     . SER   A 60  ? 1.1287 0.7154 0.7009 -0.059  0.0533  0.0831  60  SER   A N     
208  C  CA    . SER   A 60  ? 1.0873 0.7104 0.7061 -0.0527 0.0552  0.0776  60  SER   A CA    
209  C  C     . SER   A 60  ? 1.058  0.7015 0.7125 -0.047  0.0581  0.0791  60  SER   A C     
210  O  O     . SER   A 60  ? 1.0342 0.706  0.7226 -0.043  0.0472  0.0778  60  SER   A O     
211  C  CB    . SER   A 60  ? 1.1002 0.7222 0.7201 -0.0514 0.0745  0.0715  60  SER   A CB    
212  O  OG    . SER   A 60  ? 1.1007 0.7566 0.7644 -0.0455 0.0764  0.0669  60  SER   A OG    
213  N  N     . GLY   A 61  ? 1.0581 0.6848 0.7024 -0.0471 0.0723  0.082   61  GLY   A N     
214  C  CA    . GLY   A 61  ? 1.0381 0.679  0.7119 -0.0428 0.0762  0.0837  61  GLY   A CA    
215  C  C     . GLY   A 61  ? 1.0315 0.6806 0.7142 -0.0421 0.0565  0.0884  61  GLY   A C     
216  O  O     . GLY   A 61  ? 1.0117 0.6866 0.7313 -0.0373 0.0521  0.0869  61  GLY   A O     
217  N  N     . ARG   A 62  ? 1.047  0.6734 0.6958 -0.0469 0.0441  0.0943  62  ARG   A N     
218  C  CA    . ARG   A 62  ? 1.0464 0.6783 0.7023 -0.0465 0.0242  0.1002  62  ARG   A CA    
219  C  C     . ARG   A 62  ? 1.0205 0.6816 0.7057 -0.0436 0.0085  0.0973  62  ARG   A C     
220  O  O     . ARG   A 62  ? 1.0078 0.6865 0.7203 -0.0397 -0.0017 0.0994  62  ARG   A O     
221  C  CB    . ARG   A 62  ? 1.0985 0.6981 0.7095 -0.0531 0.0136  0.1078  62  ARG   A CB    
222  C  CG    . ARG   A 62  ? 1.1771 0.7479 0.7611 -0.0554 0.0264  0.1128  62  ARG   A CG    
223  C  CD    . ARG   A 62  ? 1.266  0.8029 0.8015 -0.0627 0.0147  0.1202  62  ARG   A CD    
224  N  NE    . ARG   A 62  ? 1.3527 0.8592 0.8584 -0.0653 0.0282  0.1253  62  ARG   A NE    
225  C  CZ    . ARG   A 62  ? 1.4227 0.8939 0.8805 -0.0715 0.039   0.1259  62  ARG   A CZ    
226  N  NH1   . ARG   A 62  ? 1.4399 0.9011 0.8736 -0.0758 0.0373  0.1216  62  ARG   A NH1   
227  N  NH2   . ARG   A 62  ? 1.4433 0.8877 0.8761 -0.0734 0.0522  0.1309  62  ARG   A NH2   
228  N  N     . TYR   A 63  ? 1.0121 0.6781 0.6931 -0.0453 0.0079  0.0922  63  TYR   A N     
229  C  CA    . TYR   A 63  ? 0.9891 0.6825 0.6978 -0.0429 -0.005  0.0893  63  TYR   A CA    
230  C  C     . TYR   A 63  ? 0.9523 0.6754 0.7042 -0.0359 0.0021  0.0842  63  TYR   A C     
231  O  O     . TYR   A 63  ? 0.9313 0.6743 0.7099 -0.0323 -0.009  0.0849  63  TYR   A O     
232  C  CB    . TYR   A 63  ? 0.9993 0.6899 0.6932 -0.0466 -0.0054 0.0849  63  TYR   A CB    
233  C  CG    . TYR   A 63  ? 0.9968 0.718  0.7234 -0.0434 -0.0142 0.081   63  TYR   A CG    
234  C  CD1   . TYR   A 63  ? 1.0073 0.7391 0.745  -0.0437 -0.0337 0.085   63  TYR   A CD1   
235  C  CD2   . TYR   A 63  ? 0.9942 0.7345 0.7437 -0.0395 -0.0026 0.0738  63  TYR   A CD2   
236  C  CE1   . TYR   A 63  ? 1.0021 0.7616 0.7708 -0.0406 -0.04   0.0817  63  TYR   A CE1   
237  C  CE2   . TYR   A 63  ? 0.9914 0.7587 0.7699 -0.0364 -0.0097 0.0704  63  TYR   A CE2   
238  C  CZ    . TYR   A 63  ? 1.0023 0.7788 0.7898 -0.037  -0.0276 0.0742  63  TYR   A CZ    
239  O  OH    . TYR   A 63  ? 1.0089 0.8111 0.8246 -0.0341 -0.0331 0.071   63  TYR   A OH    
240  N  N     . LEU   A 64  ? 0.9455 0.6702 0.7038 -0.0341 0.0205  0.0795  64  LEU   A N     
241  C  CA    . LEU   A 64  ? 0.9314 0.6815 0.7277 -0.0285 0.0277  0.0745  64  LEU   A CA    
242  C  C     . LEU   A 64  ? 0.932  0.687  0.7457 -0.0255 0.0245  0.0777  64  LEU   A C     
243  O  O     . LEU   A 64  ? 0.9155 0.6933 0.7604 -0.0212 0.0205  0.0748  64  LEU   A O     
244  C  CB    . LEU   A 64  ? 0.9349 0.6813 0.7317 -0.0282 0.0475  0.0708  64  LEU   A CB    
245  C  CG    . LEU   A 64  ? 0.9373 0.7021 0.7513 -0.0264 0.0522  0.0643  64  LEU   A CG    
246  C  CD1   . LEU   A 64  ? 0.949  0.7069 0.7419 -0.0296 0.0455  0.0635  64  LEU   A CD1   
247  C  CD2   . LEU   A 64  ? 0.9456 0.7076 0.7649 -0.0256 0.0713  0.0621  64  LEU   A CD2   
248  N  N     . GLN   A 65  ? 0.9466 0.6784 0.7383 -0.028  0.0264  0.0839  65  GLN   A N     
249  C  CA    . GLN   A 65  ? 0.9513 0.6826 0.7549 -0.0257 0.0241  0.088   65  GLN   A CA    
250  C  C     . GLN   A 65  ? 0.949  0.6935 0.7687 -0.0231 0.0061  0.0906  65  GLN   A C     
251  O  O     . GLN   A 65  ? 0.9441 0.7011 0.7896 -0.0189 0.0048  0.0903  65  GLN   A O     
252  C  CB    . GLN   A 65  ? 0.9956 0.6958 0.7657 -0.0298 0.0284  0.0951  65  GLN   A CB    
253  C  CG    . GLN   A 65  ? 1.0343 0.731  0.8158 -0.0278 0.0327  0.0987  65  GLN   A CG    
254  C  CD    . GLN   A 65  ? 1.1097 0.7757 0.8584 -0.032  0.0441  0.1039  65  GLN   A CD    
255  O  OE1   . GLN   A 65  ? 1.143  0.7853 0.8543 -0.0367 0.0405  0.1082  65  GLN   A OE1   
256  N  NE2   . GLN   A 65  ? 1.1008 0.7657 0.8622 -0.0308 0.0583  0.1037  65  GLN   A NE2   
257  N  N     . GLN   A 66  ? 0.9523 0.6936 0.758  -0.0256 -0.0075 0.0933  66  GLN   A N     
258  C  CA    . GLN   A 66  ? 0.9472 0.7015 0.7704 -0.0232 -0.0246 0.0968  66  GLN   A CA    
259  C  C     . GLN   A 66  ? 0.9093 0.6922 0.7627 -0.0195 -0.0269 0.09    66  GLN   A C     
260  O  O     . GLN   A 66  ? 0.9039 0.7038 0.7851 -0.0148 -0.0329 0.09    66  GLN   A O     
261  C  CB    . GLN   A 66  ? 1.0068 0.7429 0.8012 -0.0285 -0.0396 0.1043  66  GLN   A CB    
262  C  CG    . GLN   A 66  ? 1.1169 0.8229 0.8792 -0.0323 -0.0382 0.1117  66  GLN   A CG    
263  C  CD    . GLN   A 66  ? 1.2121 0.9191 0.9902 -0.0287 -0.0453 0.1183  66  GLN   A CD    
264  O  OE1   . GLN   A 66  ? 1.2349 0.9518 1.0285 -0.0268 -0.0615 0.123   66  GLN   A OE1   
265  N  NE2   . GLN   A 66  ? 1.2301 0.9268 1.0061 -0.0276 -0.0329 0.1191  66  GLN   A NE2   
266  N  N     . GLU   A 67  ? 0.8823 0.6695 0.7299 -0.0213 -0.0208 0.0843  67  GLU   A N     
267  C  CA    . GLU   A 67  ? 0.85   0.6617 0.7214 -0.0186 -0.0226 0.0783  67  GLU   A CA    
268  C  C     . GLU   A 67  ? 0.8215 0.6528 0.7222 -0.0136 -0.0124 0.0715  67  GLU   A C     
269  O  O     . GLU   A 67  ? 0.8098 0.6608 0.7355 -0.0098 -0.0173 0.0689  67  GLU   A O     
270  C  CB    . GLU   A 67  ? 0.8747 0.6817 0.7274 -0.0228 -0.0205 0.0754  67  GLU   A CB    
271  C  CG    . GLU   A 67  ? 0.9203 0.7502 0.7938 -0.0209 -0.0245 0.0706  67  GLU   A CG    
272  C  CD    . GLU   A 67  ? 0.9931 0.8333 0.8797 -0.0202 -0.0409 0.0748  67  GLU   A CD    
273  O  OE1   . GLU   A 67  ? 0.9691 0.831  0.8804 -0.017  -0.0428 0.0712  67  GLU   A OE1   
274  O  OE2   . GLU   A 67  ? 1.0508 0.8769 0.9231 -0.0229 -0.0519 0.0821  67  GLU   A OE2   
275  N  N     . LEU   A 68  ? 0.8056 0.6311 0.703  -0.0139 0.0016  0.0686  68  LEU   A N     
276  C  CA    . LEU   A 68  ? 0.7793 0.6223 0.7029 -0.0104 0.0099  0.0623  68  LEU   A CA    
277  C  C     . LEU   A 68  ? 0.7628 0.6162 0.71   -0.0061 0.0056  0.0621  68  LEU   A C     
278  O  O     . LEU   A 68  ? 0.7571 0.6294 0.7258 -0.0031 0.0048  0.0568  68  LEU   A O     
279  C  CB    . LEU   A 68  ? 0.7776 0.6127 0.6966 -0.0118 0.0249  0.0605  68  LEU   A CB    
280  C  CG    . LEU   A 68  ? 0.7896 0.6194 0.6936 -0.0145 0.0327  0.0585  68  LEU   A CG    
281  C  CD1   . LEU   A 68  ? 0.7898 0.6138 0.6957 -0.0151 0.0482  0.0574  68  LEU   A CD1   
282  C  CD2   . LEU   A 68  ? 0.7814 0.631  0.6992 -0.013  0.0293  0.0532  68  LEU   A CD2   
283  N  N     . PRO   A 69  ? 0.7491 0.5903 0.6928 -0.0057 0.003   0.0676  69  PRO   A N     
284  C  CA    . PRO   A 69  ? 0.7296 0.5802 0.697  -0.0013 0       0.0668  69  PRO   A CA    
285  C  C     . PRO   A 69  ? 0.7118 0.5773 0.695  0.002   -0.0107 0.0665  69  PRO   A C     
286  O  O     . PRO   A 69  ? 0.7003 0.5787 0.706  0.006   -0.0096 0.0623  69  PRO   A O     
287  C  CB    . PRO   A 69  ? 0.7516 0.5829 0.7078 -0.0021 -0.0014 0.0743  69  PRO   A CB    
288  C  CG    . PRO   A 69  ? 0.7748 0.5872 0.7029 -0.007  0.0053  0.0772  69  PRO   A CG    
289  C  CD    . PRO   A 69  ? 0.7605 0.5773 0.6777 -0.0093 0.0033  0.0748  69  PRO   A CD    
290  N  N     . VAL   A 70  ? 0.711  0.5741 0.6828 0.0002  -0.0204 0.071   70  VAL   A N     
291  C  CA    . VAL   A 70  ? 0.6975 0.5752 0.6857 0.0029  -0.0304 0.0717  70  VAL   A CA    
292  C  C     . VAL   A 70  ? 0.6724 0.5694 0.6757 0.0046  -0.0252 0.0634  70  VAL   A C     
293  O  O     . VAL   A 70  ? 0.6635 0.5744 0.6894 0.009   -0.0256 0.0604  70  VAL   A O     
294  C  CB    . VAL   A 70  ? 0.7191 0.5883 0.6904 -0.0008 -0.043  0.079   70  VAL   A CB    
295  C  CG1   . VAL   A 70  ? 0.7118 0.5988 0.7011 0.0009  -0.0518 0.0789  70  VAL   A CG1   
296  C  CG2   . VAL   A 70  ? 0.7315 0.584  0.6932 -0.0014 -0.0511 0.0884  70  VAL   A CG2   
297  N  N     . ARG   A 71  ? 0.6639 0.5604 0.6545 0.0013  -0.0194 0.0596  71  ARG   A N     
298  C  CA    . ARG   A 71  ? 0.6481 0.5616 0.651  0.0025  -0.0146 0.0523  71  ARG   A CA    
299  C  C     . ARG   A 71  ? 0.6485 0.5699 0.6683 0.0055  -0.0065 0.0462  71  ARG   A C     
300  O  O     . ARG   A 71  ? 0.645  0.5811 0.6811 0.0083  -0.0059 0.0413  71  ARG   A O     
301  C  CB    . ARG   A 71  ? 0.6509 0.56   0.6365 -0.0015 -0.0095 0.0504  71  ARG   A CB    
302  C  CG    . ARG   A 71  ? 0.6771 0.5754 0.6423 -0.0055 -0.0173 0.0555  71  ARG   A CG    
303  C  CD    . ARG   A 71  ? 0.7075 0.6052 0.6606 -0.0086 -0.0121 0.0522  71  ARG   A CD    
304  N  NE    . ARG   A 71  ? 0.7641 0.6494 0.6954 -0.0131 -0.0198 0.0565  71  ARG   A NE    
305  C  CZ    . ARG   A 71  ? 0.7978 0.6811 0.7171 -0.0163 -0.0182 0.0545  71  ARG   A CZ    
306  N  NH1   . ARG   A 71  ? 0.768  0.6619 0.696  -0.0148 -0.0092 0.0488  71  ARG   A NH1   
307  N  NH2   . ARG   A 71  ? 0.8253 0.6947 0.7228 -0.0212 -0.026  0.0584  71  ARG   A NH2   
308  N  N     . ILE   A 72  ? 0.65   0.5605 0.6651 0.0046  -0.0005 0.0468  72  ILE   A N     
309  C  CA    . ILE   A 72  ? 0.6508 0.5664 0.6808 0.0064  0.0061  0.0415  72  ILE   A CA    
310  C  C     . ILE   A 72  ? 0.6528 0.5735 0.7002 0.0108  0.0023  0.0408  72  ILE   A C     
311  O  O     . ILE   A 72  ? 0.6476 0.5791 0.709  0.0129  0.005   0.0344  72  ILE   A O     
312  C  CB    . ILE   A 72  ? 0.6579 0.5601 0.6795 0.0037  0.0136  0.0432  72  ILE   A CB    
313  C  CG1   . ILE   A 72  ? 0.6753 0.5763 0.6857 0.0003  0.02    0.042   72  ILE   A CG1   
314  C  CG2   . ILE   A 72  ? 0.6537 0.5591 0.6917 0.005   0.0183  0.0388  72  ILE   A CG2   
315  C  CD1   . ILE   A 72  ? 0.698  0.5855 0.6991 -0.0024 0.0282  0.0445  72  ILE   A CD1   
316  N  N     . ALA   A 73  ? 0.6513 0.5639 0.6974 0.0123  -0.0042 0.0475  73  ALA   A N     
317  C  CA    . ALA   A 73  ? 0.6475 0.564  0.7116 0.0172  -0.0073 0.0478  73  ALA   A CA    
318  C  C     . ALA   A 73  ? 0.6482 0.5812 0.727  0.0203  -0.0093 0.044   73  ALA   A C     
319  O  O     . ALA   A 73  ? 0.6525 0.5913 0.7469 0.024   -0.0058 0.0391  73  ALA   A O     
320  C  CB    . ALA   A 73  ? 0.6481 0.553  0.7085 0.0181  -0.0151 0.0571  73  ALA   A CB    
321  N  N     . HIS   A 74  ? 0.6437 0.5832 0.7167 0.0186  -0.0138 0.0455  74  HIS   A N     
322  C  CA    . HIS   A 74  ? 0.6412 0.5964 0.7281 0.0211  -0.0144 0.042   74  HIS   A CA    
323  C  C     . HIS   A 74  ? 0.635  0.598  0.7258 0.0213  -0.0058 0.0326  74  HIS   A C     
324  O  O     . HIS   A 74  ? 0.6403 0.6119 0.745  0.0248  -0.0031 0.0282  74  HIS   A O     
325  C  CB    . HIS   A 74  ? 0.658  0.6178 0.7369 0.0182  -0.0206 0.0452  74  HIS   A CB    
326  C  CG    . HIS   A 74  ? 0.7144 0.6669 0.7887 0.0171  -0.0313 0.0545  74  HIS   A CG    
327  N  ND1   . HIS   A 74  ? 0.7581 0.7046 0.8138 0.012   -0.0372 0.0584  74  HIS   A ND1   
328  C  CD2   . HIS   A 74  ? 0.7335 0.683  0.819  0.0202  -0.0376 0.0607  74  HIS   A CD2   
329  C  CE1   . HIS   A 74  ? 0.7684 0.7083 0.8234 0.0116  -0.0478 0.0668  74  HIS   A CE1   
330  N  NE2   . HIS   A 74  ? 0.7576 0.6997 0.8314 0.0166  -0.0486 0.069   74  HIS   A NE2   
331  N  N     . ARG   A 75  ? 0.6195 0.5789 0.6979 0.0174  -0.0014 0.0299  75  ARG   A N     
332  C  CA    . ARG   A 75  ? 0.6008 0.5669 0.6823 0.0167  0.005   0.022   75  ARG   A CA    
333  C  C     . ARG   A 75  ? 0.5946 0.5575 0.6855 0.0185  0.0091  0.0176  75  ARG   A C     
334  O  O     . ARG   A 75  ? 0.5898 0.5594 0.6873 0.0196  0.0121  0.0111  75  ARG   A O     
335  C  CB    . ARG   A 75  ? 0.6161 0.5799 0.6854 0.0123  0.0082  0.0215  75  ARG   A CB    
336  C  CG    . ARG   A 75  ? 0.6372 0.6052 0.6972 0.0104  0.0057  0.0235  75  ARG   A CG    
337  C  CD    . ARG   A 75  ? 0.665  0.6465 0.7329 0.0122  0.004   0.0206  75  ARG   A CD    
338  N  NE    . ARG   A 75  ? 0.7243 0.707  0.7948 0.0136  -0.0026 0.0256  75  ARG   A NE    
339  C  CZ    . ARG   A 75  ? 0.7593 0.7499 0.8444 0.0173  -0.0042 0.0251  75  ARG   A CZ    
340  N  NH1   . ARG   A 75  ? 0.7572 0.7497 0.8471 0.0181  -0.0111 0.0309  75  ARG   A NH1   
341  N  NH2   . ARG   A 75  ? 0.7571 0.7532 0.8521 0.0199  0.0011  0.019   75  ARG   A NH2   
342  N  N     . ILE   A 76  ? 0.596  0.5473 0.6865 0.0187  0.0089  0.0212  76  ILE   A N     
343  C  CA    . ILE   A 76  ? 0.5955 0.5418 0.6951 0.0203  0.0125  0.0173  76  ILE   A CA    
344  C  C     . ILE   A 76  ? 0.5983 0.5491 0.711  0.0256  0.0121  0.0154  76  ILE   A C     
345  O  O     . ILE   A 76  ? 0.6036 0.5556 0.7224 0.0267  0.0165  0.0083  76  ILE   A O     
346  C  CB    . ILE   A 76  ? 0.5951 0.5271 0.6909 0.0192  0.0128  0.0224  76  ILE   A CB    
347  C  CG1   . ILE   A 76  ? 0.6063 0.5342 0.6917 0.014   0.0164  0.0227  76  ILE   A CG1   
348  C  CG2   . ILE   A 76  ? 0.5889 0.5144 0.6953 0.0215  0.0156  0.0193  76  ILE   A CG2   
349  C  CD1   . ILE   A 76  ? 0.6191 0.532  0.6982 0.0123  0.018   0.0286  76  ILE   A CD1   
350  N  N     . LYS   A 77  ? 0.597  0.5508 0.7142 0.0285  0.007   0.0214  77  LYS   A N     
351  C  CA    . LYS   A 77  ? 0.6035 0.5631 0.7364 0.034   0.0074  0.0208  77  LYS   A CA    
352  C  C     . LYS   A 77  ? 0.5958 0.5666 0.7306 0.0342  0.0121  0.013   77  LYS   A C     
353  O  O     . LYS   A 77  ? 0.599  0.5707 0.743  0.0377  0.0174  0.0078  77  LYS   A O     
354  C  CB    . LYS   A 77  ? 0.6431 0.6052 0.7815 0.036   -0.0007 0.0302  77  LYS   A CB    
355  C  CG    . LYS   A 77  ? 0.726  0.6935 0.8855 0.0424  -0.0005 0.0318  77  LYS   A CG    
356  C  CD    . LYS   A 77  ? 0.8098 0.7713 0.9769 0.0447  -0.0088 0.0425  77  LYS   A CD    
357  C  CE    . LYS   A 77  ? 0.8774 0.8482 1.068  0.0504  -0.0108 0.0466  77  LYS   A CE    
358  N  NZ    . LYS   A 77  ? 0.9269 0.89   1.1313 0.0549  -0.015  0.0544  77  LYS   A NZ    
359  N  N     . GLY   A 78  ? 0.5835 0.5609 0.708  0.0304  0.0108  0.0122  78  GLY   A N     
360  C  CA    . GLY   A 78  ? 0.5756 0.5622 0.6987 0.0297  0.0147  0.0056  78  GLY   A CA    
361  C  C     . GLY   A 78  ? 0.5756 0.558  0.6957 0.0284  0.0203  -0.0028 78  GLY   A C     
362  O  O     . GLY   A 78  ? 0.5834 0.5693 0.7057 0.0299  0.0248  -0.0087 78  GLY   A O     
363  N  N     . PHE   A 79  ? 0.5665 0.5402 0.6816 0.0254  0.0203  -0.0033 79  PHE   A N     
364  C  CA    . PHE   A 79  ? 0.5662 0.5346 0.6792 0.0231  0.0239  -0.0107 79  PHE   A CA    
365  C  C     . PHE   A 79  ? 0.5716 0.5324 0.6926 0.0271  0.0278  -0.0144 79  PHE   A C     
366  O  O     . PHE   A 79  ? 0.5742 0.5323 0.6929 0.0265  0.0316  -0.0222 79  PHE   A O     
367  C  CB    . PHE   A 79  ? 0.5645 0.526  0.6731 0.0186  0.0227  -0.0089 79  PHE   A CB    
368  C  CG    . PHE   A 79  ? 0.5665 0.5341 0.668  0.014   0.0216  -0.0089 79  PHE   A CG    
369  C  CD1   . PHE   A 79  ? 0.5766 0.5475 0.673  0.0133  0.0196  -0.0028 79  PHE   A CD1   
370  C  CD2   . PHE   A 79  ? 0.5724 0.5414 0.6722 0.0103  0.0222  -0.0148 79  PHE   A CD2   
371  C  CE1   . PHE   A 79  ? 0.5851 0.5609 0.6764 0.0096  0.0197  -0.0027 79  PHE   A CE1   
372  C  CE2   . PHE   A 79  ? 0.5793 0.5547 0.6755 0.0065  0.0209  -0.0139 79  PHE   A CE2   
373  C  CZ    . PHE   A 79  ? 0.5771 0.5559 0.6697 0.0066  0.0204  -0.0079 79  PHE   A CZ    
374  N  N     . ARG   A 80  ? 0.5738 0.5299 0.7036 0.0311  0.0268  -0.0086 80  ARG   A N     
375  C  CA    . ARG   A 80  ? 0.5845 0.533  0.7245 0.0359  0.0312  -0.011  80  ARG   A CA    
376  C  C     . ARG   A 80  ? 0.5938 0.5488 0.7402 0.0403  0.0361  -0.0148 80  ARG   A C     
377  O  O     . ARG   A 80  ? 0.6045 0.5523 0.7558 0.0436  0.0426  -0.0201 80  ARG   A O     
378  C  CB    . ARG   A 80  ? 0.5937 0.5373 0.7431 0.0396  0.0278  -0.0021 80  ARG   A CB    
379  C  CG    . ARG   A 80  ? 0.6318 0.5653 0.775  0.0359  0.0251  0.0015  80  ARG   A CG    
380  C  CD    . ARG   A 80  ? 0.669  0.5979 0.8181 0.039   0.0203  0.0115  80  ARG   A CD    
381  N  NE    . ARG   A 80  ? 0.7248 0.6414 0.8681 0.0361  0.0195  0.0149  80  ARG   A NE    
382  C  CZ    . ARG   A 80  ? 0.7634 0.6715 0.9088 0.0379  0.0156  0.0235  80  ARG   A CZ    
383  N  NH1   . ARG   A 80  ? 0.7637 0.6753 0.9185 0.0427  0.0108  0.0301  80  ARG   A NH1   
384  N  NH2   . ARG   A 80  ? 0.7693 0.6654 0.9081 0.0348  0.0161  0.0263  80  ARG   A NH2   
385  N  N     . SER   A 81  ? 0.5816 0.549  0.7278 0.0404  0.0339  -0.012  81  SER   A N     
386  C  CA    . SER   A 81  ? 0.5791 0.5539 0.7322 0.0442  0.039   -0.0143 81  SER   A CA    
387  C  C     . SER   A 81  ? 0.575  0.5521 0.7156 0.0412  0.0435  -0.0227 81  SER   A C     
388  O  O     . SER   A 81  ? 0.5772 0.5578 0.7216 0.0442  0.0497  -0.0257 81  SER   A O     
389  C  CB    . SER   A 81  ? 0.5987 0.5853 0.7602 0.0458  0.0337  -0.0059 81  SER   A CB    
390  O  OG    . SER   A 81  ? 0.6461 0.6293 0.818  0.0483  0.0284  0.0024  81  SER   A OG    
391  N  N     . LEU   A 82  ? 0.5762 0.5512 0.7026 0.0352  0.0404  -0.026  82  LEU   A N     
392  C  CA    . LEU   A 82  ? 0.5802 0.5565 0.6933 0.0313  0.0425  -0.0331 82  LEU   A CA    
393  C  C     . LEU   A 82  ? 0.5705 0.5367 0.6803 0.0331  0.0505  -0.0417 82  LEU   A C     
394  O  O     . LEU   A 82  ? 0.5601 0.5152 0.6738 0.0347  0.0529  -0.0438 82  LEU   A O     
395  C  CB    . LEU   A 82  ? 0.5916 0.5646 0.6947 0.0249  0.0373  -0.0345 82  LEU   A CB    
396  C  CG    . LEU   A 82  ? 0.6177 0.6002 0.7166 0.0213  0.0316  -0.0296 82  LEU   A CG    
397  C  CD1   . LEU   A 82  ? 0.6299 0.6082 0.7243 0.0159  0.0279  -0.0301 82  LEU   A CD1   
398  C  CD2   . LEU   A 82  ? 0.6227 0.614  0.7145 0.0204  0.0325  -0.0317 82  LEU   A CD2   
399  N  N     . PRO   A 83  ? 0.5735 0.541  0.6731 0.0321  0.0548  -0.0473 83  PRO   A N     
400  C  CA    . PRO   A 83  ? 0.5846 0.5388 0.676  0.0329  0.0632  -0.0564 83  PRO   A CA    
401  C  C     . PRO   A 83  ? 0.6044 0.5445 0.6872 0.0283  0.0604  -0.0619 83  PRO   A C     
402  O  O     . PRO   A 83  ? 0.6159 0.5582 0.6931 0.0225  0.0523  -0.0608 83  PRO   A O     
403  C  CB    . PRO   A 83  ? 0.5923 0.5502 0.6691 0.0304  0.0656  -0.0604 83  PRO   A CB    
404  C  CG    . PRO   A 83  ? 0.5895 0.5643 0.6755 0.0318  0.0621  -0.0522 83  PRO   A CG    
405  C  CD    . PRO   A 83  ? 0.5625 0.5417 0.6559 0.0301  0.053   -0.0456 83  PRO   A CD    
406  N  N     . PHE   A 84  ? 0.6032 0.5293 0.6879 0.0313  0.0673  -0.0668 84  PHE   A N     
407  C  CA    . PHE   A 84  ? 0.6232 0.5342 0.7024 0.0275  0.0655  -0.0718 84  PHE   A CA    
408  C  C     . PHE   A 84  ? 0.6376 0.5443 0.6985 0.0185  0.0588  -0.0772 84  PHE   A C     
409  O  O     . PHE   A 84  ? 0.6416 0.5465 0.7044 0.0138  0.0516  -0.0757 84  PHE   A O     
410  C  CB    . PHE   A 84  ? 0.6304 0.5249 0.7098 0.0319  0.0762  -0.0784 84  PHE   A CB    
411  C  CG    . PHE   A 84  ? 0.6557 0.5324 0.7293 0.028   0.0751  -0.0841 84  PHE   A CG    
412  C  CD1   . PHE   A 84  ? 0.6653 0.5409 0.7523 0.0285  0.0707  -0.0786 84  PHE   A CD1   
413  C  CD2   . PHE   A 84  ? 0.6785 0.5381 0.7321 0.0236  0.0787  -0.095  84  PHE   A CD2   
414  C  CE1   . PHE   A 84  ? 0.6872 0.546  0.77   0.0247  0.07    -0.0837 84  PHE   A CE1   
415  C  CE2   . PHE   A 84  ? 0.7002 0.5421 0.7487 0.0197  0.0775  -0.1005 84  PHE   A CE2   
416  C  CZ    . PHE   A 84  ? 0.6975 0.5396 0.7619 0.0203  0.0734  -0.0947 84  PHE   A CZ    
417  N  N     . ILE   A 85  ? 0.6473 0.5518 0.6912 0.016   0.0609  -0.0831 85  ILE   A N     
418  C  CA    . ILE   A 85  ? 0.6717 0.5716 0.698  0.0073  0.0533  -0.0878 85  ILE   A CA    
419  C  C     . ILE   A 85  ? 0.6676 0.5836 0.7003 0.0033  0.0426  -0.0803 85  ILE   A C     
420  O  O     . ILE   A 85  ? 0.682  0.5952 0.7105 -0.0036 0.0344  -0.0814 85  ILE   A O     
421  C  CB    . ILE   A 85  ? 0.6973 0.5902 0.7023 0.0059  0.0584  -0.0949 85  ILE   A CB    
422  C  CG1   . ILE   A 85  ? 0.7259 0.61   0.7101 -0.0038 0.0495  -0.1005 85  ILE   A CG1   
423  C  CG2   . ILE   A 85  ? 0.6923 0.6007 0.7004 0.0099  0.0614  -0.0899 85  ILE   A CG2   
424  C  CD1   . ILE   A 85  ? 0.7606 0.6214 0.7296 -0.0069 0.0529  -0.1104 85  ILE   A CD1   
425  N  N     . ILE   A 86  ? 0.6476 0.5792 0.6919 0.0077  0.0428  -0.0723 86  ILE   A N     
426  C  CA    . ILE   A 86  ? 0.6395 0.5847 0.69   0.0049  0.0348  -0.0651 86  ILE   A CA    
427  C  C     . ILE   A 86  ? 0.6385 0.5827 0.7022 0.0046  0.0317  -0.0603 86  ILE   A C     
428  O  O     . ILE   A 86  ? 0.6468 0.5927 0.7116 -0.0008 0.0253  -0.0585 86  ILE   A O     
429  C  CB    . ILE   A 86  ? 0.6312 0.591  0.6861 0.0089  0.0363  -0.0591 86  ILE   A CB    
430  C  CG1   . ILE   A 86  ? 0.6372 0.5983 0.6775 0.0076  0.0383  -0.0632 86  ILE   A CG1   
431  C  CG2   . ILE   A 86  ? 0.6334 0.6045 0.6958 0.007   0.0297  -0.0513 86  ILE   A CG2   
432  C  CD1   . ILE   A 86  ? 0.6399 0.6141 0.685  0.0115  0.041   -0.0579 86  ILE   A CD1   
433  N  N     . GLY   A 87  ? 0.6273 0.5676 0.7013 0.0101  0.0365  -0.0581 87  GLY   A N     
434  C  CA    . GLY   A 87  ? 0.6261 0.5636 0.7111 0.0102  0.0344  -0.0531 87  GLY   A CA    
435  C  C     . GLY   A 87  ? 0.6455 0.5713 0.7279 0.0045  0.0317  -0.0576 87  GLY   A C     
436  O  O     . GLY   A 87  ? 0.6434 0.5693 0.7332 0.002   0.0284  -0.053  87  GLY   A O     
437  N  N     . CYS   A 88  ? 0.6569 0.5715 0.7283 0.0021  0.0335  -0.0667 88  CYS   A N     
438  C  CA    . CYS   A 88  ? 0.6687 0.5704 0.7354 -0.0045 0.0301  -0.0723 88  CYS   A CA    
439  C  C     . CYS   A 88  ? 0.6704 0.5783 0.733  -0.0126 0.0209  -0.0719 88  CYS   A C     
440  O  O     . CYS   A 88  ? 0.6805 0.5803 0.7432 -0.0189 0.0163  -0.0747 88  CYS   A O     
441  C  CB    . CYS   A 88  ? 0.6871 0.5722 0.7405 -0.0044 0.0354  -0.0824 88  CYS   A CB    
442  S  SG    . CYS   A 88  ? 0.7579 0.6317 0.8208 0.0044  0.0463  -0.0831 88  CYS   A SG    
443  N  N     . ASN   A 89  ? 0.6595 0.5812 0.7191 -0.0128 0.0181  -0.0687 89  ASN   A N     
444  C  CA    . ASN   A 89  ? 0.6577 0.5859 0.7158 -0.0199 0.0093  -0.0674 89  ASN   A CA    
445  C  C     . ASN   A 89  ? 0.658  0.5901 0.7326 -0.0227 0.0059  -0.061  89  ASN   A C     
446  O  O     . ASN   A 89  ? 0.6561 0.5929 0.7409 -0.0181 0.01    -0.0546 89  ASN   A O     
447  C  CB    . ASN   A 89  ? 0.6583 0.6    0.7118 -0.0185 0.0081  -0.0642 89  ASN   A CB    
448  C  CG    . ASN   A 89  ? 0.6909 0.6414 0.7473 -0.0246 -0.0008 -0.0607 89  ASN   A CG    
449  O  OD1   . ASN   A 89  ? 0.7075 0.6677 0.7776 -0.0244 -0.002  -0.0535 89  ASN   A OD1   
450  N  ND2   . ASN   A 89  ? 0.6941 0.6406 0.7379 -0.0303 -0.007  -0.0654 89  ASN   A ND2   
451  N  N     . PRO   A 90  ? 0.6523 0.5811 0.7295 -0.0305 -0.0012 -0.0626 90  PRO   A N     
452  C  CA    . PRO   A 90  ? 0.6431 0.5751 0.7377 -0.0333 -0.003  -0.0564 90  PRO   A CA    
453  C  C     . PRO   A 90  ? 0.6291 0.5758 0.7341 -0.0305 -0.0014 -0.0472 90  PRO   A C     
454  O  O     . PRO   A 90  ? 0.632  0.5789 0.7481 -0.029  0.0024  -0.0416 90  PRO   A O     
455  C  CB    . PRO   A 90  ? 0.6528 0.5813 0.7486 -0.0428 -0.0125 -0.0595 90  PRO   A CB    
456  C  CG    . PRO   A 90  ? 0.6706 0.5868 0.7461 -0.0448 -0.0144 -0.0693 90  PRO   A CG    
457  C  CD    . PRO   A 90  ? 0.6532 0.5744 0.7173 -0.0375 -0.0084 -0.0697 90  PRO   A CD    
458  N  N     . THR   A 91  ? 0.6188 0.5762 0.7187 -0.0298 -0.0038 -0.0458 91  THR   A N     
459  C  CA    . THR   A 91  ? 0.612  0.5818 0.7201 -0.0274 -0.0019 -0.0377 91  THR   A CA    
460  C  C     . THR   A 91  ? 0.6056 0.576  0.711  -0.02   0.0054  -0.0346 91  THR   A C     
461  O  O     . THR   A 91  ? 0.6029 0.5758 0.7156 -0.0183 0.0089  -0.0281 91  THR   A O     
462  C  CB    . THR   A 91  ? 0.6237 0.6037 0.7282 -0.0295 -0.0073 -0.0369 91  THR   A CB    
463  O  OG1   . THR   A 91  ? 0.6353 0.614  0.7437 -0.0369 -0.0157 -0.039  91  THR   A OG1   
464  C  CG2   . THR   A 91  ? 0.6222 0.6135 0.7354 -0.0273 -0.0049 -0.0291 91  THR   A CG2   
465  N  N     . ILE   A 92  ? 0.5972 0.5642 0.6921 -0.016  0.0079  -0.039  92  ILE   A N     
466  C  CA    . ILE   A 92  ? 0.5957 0.5632 0.69   -0.0094 0.0133  -0.0359 92  ILE   A CA    
467  C  C     . ILE   A 92  ? 0.5931 0.5515 0.6948 -0.008  0.0164  -0.0333 92  ILE   A C     
468  O  O     . ILE   A 92  ? 0.5893 0.5493 0.6943 -0.0053 0.0187  -0.0268 92  ILE   A O     
469  C  CB    . ILE   A 92  ? 0.606  0.5718 0.6909 -0.0056 0.0159  -0.0412 92  ILE   A CB    
470  C  CG1   . ILE   A 92  ? 0.6129 0.5871 0.689  -0.007  0.0134  -0.0428 92  ILE   A CG1   
471  C  CG2   . ILE   A 92  ? 0.6102 0.5769 0.6985 0.001   0.0205  -0.0373 92  ILE   A CG2   
472  C  CD1   . ILE   A 92  ? 0.6131 0.5993 0.6924 -0.0062 0.0123  -0.0358 92  ILE   A CD1   
473  N  N     . LEU   A 93  ? 0.5951 0.5429 0.6984 -0.0107 0.0159  -0.0381 93  LEU   A N     
474  C  CA    . LEU   A 93  ? 0.6069 0.5448 0.7173 -0.01   0.0187  -0.0357 93  LEU   A CA    
475  C  C     . LEU   A 93  ? 0.6014 0.5423 0.7203 -0.0127 0.0188  -0.0283 93  LEU   A C     
476  O  O     . LEU   A 93  ? 0.6038 0.5401 0.7254 -0.01   0.0222  -0.0229 93  LEU   A O     
477  C  CB    . LEU   A 93  ? 0.6142 0.5396 0.7246 -0.0139 0.0175  -0.0426 93  LEU   A CB    
478  C  CG    . LEU   A 93  ? 0.6538 0.5688 0.7584 -0.0098 0.0213  -0.0486 93  LEU   A CG    
479  C  CD1   . LEU   A 93  ? 0.6688 0.5695 0.7717 -0.0149 0.02    -0.0558 93  LEU   A CD1   
480  C  CD2   . LEU   A 93  ? 0.6609 0.5724 0.7715 -0.0031 0.0262  -0.0432 93  LEU   A CD2   
481  N  N     . HIS   A 94  ? 0.5951 0.543  0.7181 -0.0178 0.0153  -0.0278 94  HIS   A N     
482  C  CA    . HIS   A 94  ? 0.6053 0.5565 0.738  -0.0202 0.0171  -0.0209 94  HIS   A CA    
483  C  C     . HIS   A 94  ? 0.6054 0.5609 0.7337 -0.0156 0.0213  -0.0143 94  HIS   A C     
484  O  O     . HIS   A 94  ? 0.6115 0.5611 0.742  -0.0148 0.0258  -0.0087 94  HIS   A O     
485  C  CB    . HIS   A 94  ? 0.6204 0.58   0.7607 -0.026  0.0122  -0.0213 94  HIS   A CB    
486  C  CG    . HIS   A 94  ? 0.6692 0.6332 0.8219 -0.028  0.0156  -0.0139 94  HIS   A CG    
487  N  ND1   . HIS   A 94  ? 0.6964 0.671  0.851  -0.0273 0.0162  -0.0098 94  HIS   A ND1   
488  C  CD2   . HIS   A 94  ? 0.6897 0.6477 0.8534 -0.0303 0.0196  -0.0099 94  HIS   A CD2   
489  C  CE1   . HIS   A 94  ? 0.6955 0.6701 0.8625 -0.029  0.0212  -0.0037 94  HIS   A CE1   
490  N  NE2   . HIS   A 94  ? 0.701  0.666  0.8738 -0.0311 0.0235  -0.0034 94  HIS   A NE2   
491  N  N     . VAL   A 95  ? 0.5943 0.5582 0.7148 -0.0129 0.0199  -0.015  95  VAL   A N     
492  C  CA    . VAL   A 95  ? 0.5945 0.5613 0.7092 -0.0091 0.0229  -0.0094 95  VAL   A CA    
493  C  C     . VAL   A 95  ? 0.6031 0.5612 0.7133 -0.0049 0.0249  -0.0071 95  VAL   A C     
494  O  O     . VAL   A 95  ? 0.6112 0.5648 0.7183 -0.0039 0.0278  -0.0009 95  VAL   A O     
495  C  CB    . VAL   A 95  ? 0.5933 0.5704 0.7015 -0.0075 0.0205  -0.011  95  VAL   A CB    
496  C  CG1   . VAL   A 95  ? 0.5975 0.576  0.6989 -0.0042 0.0228  -0.0057 95  VAL   A CG1   
497  C  CG2   . VAL   A 95  ? 0.5942 0.5794 0.7074 -0.0116 0.0178  -0.0118 95  VAL   A CG2   
498  N  N     . HIS   A 96  ? 0.5936 0.5479 0.7035 -0.0027 0.0237  -0.0119 96  HIS   A N     
499  C  CA    . HIS   A 96  ? 0.5961 0.5422 0.7052 0.0016  0.025   -0.0095 96  HIS   A CA    
500  C  C     . HIS   A 96  ? 0.5959 0.5311 0.7084 -0.0002 0.0275  -0.0047 96  HIS   A C     
501  O  O     . HIS   A 96  ? 0.5929 0.5231 0.7013 0.002   0.0285  0.0017  96  HIS   A O     
502  C  CB    . HIS   A 96  ? 0.6052 0.5479 0.716  0.0038  0.0248  -0.0163 96  HIS   A CB    
503  C  CG    . HIS   A 96  ? 0.6318 0.5687 0.7446 0.0094  0.026   -0.0139 96  HIS   A CG    
504  N  ND1   . HIS   A 96  ? 0.6576 0.5911 0.7729 0.0126  0.0276  -0.0195 96  HIS   A ND1   
505  C  CD2   . HIS   A 96  ? 0.648  0.5814 0.7609 0.0121  0.0255  -0.0063 96  HIS   A CD2   
506  C  CE1   . HIS   A 96  ? 0.6639 0.5935 0.7839 0.0177  0.0282  -0.0146 96  HIS   A CE1   
507  N  NE2   . HIS   A 96  ? 0.6665 0.5959 0.7846 0.0172  0.026   -0.0065 96  HIS   A NE2   
508  N  N     . GLU   A 97  ? 0.599  0.5306 0.7184 -0.0047 0.0282  -0.0073 97  GLU   A N     
509  C  CA    . GLU   A 97  ? 0.6145 0.536  0.7384 -0.007  0.0316  -0.0027 97  GLU   A CA    
510  C  C     . GLU   A 97  ? 0.603  0.5255 0.7236 -0.0081 0.0352  0.0046  97  GLU   A C     
511  O  O     . GLU   A 97  ? 0.6092 0.5218 0.7258 -0.0073 0.0385  0.0106  97  GLU   A O     
512  C  CB    . GLU   A 97  ? 0.6575 0.5766 0.7915 -0.0126 0.031   -0.0071 97  GLU   A CB    
513  C  CG    . GLU   A 97  ? 0.7718 0.6848 0.9065 -0.0123 0.0286  -0.0146 97  GLU   A CG    
514  C  CD    . GLU   A 97  ? 0.9102 0.8202 1.0525 -0.0189 0.0261  -0.0198 97  GLU   A CD    
515  O  OE1   . GLU   A 97  ? 0.9633 0.877  1.1142 -0.0238 0.0262  -0.0166 97  GLU   A OE1   
516  O  OE2   . GLU   A 97  ? 0.9348 0.8381 1.0748 -0.0192 0.0243  -0.027  97  GLU   A OE2   
517  N  N     . LEU   A 98  ? 0.5886 0.5216 0.7095 -0.0098 0.035   0.0044  98  LEU   A N     
518  C  CA    . LEU   A 98  ? 0.5868 0.5202 0.7039 -0.0106 0.0398  0.0106  98  LEU   A CA    
519  C  C     . LEU   A 98  ? 0.5927 0.5201 0.6951 -0.0068 0.0402  0.0153  98  LEU   A C     
520  O  O     . LEU   A 98  ? 0.5995 0.517  0.6948 -0.0073 0.0449  0.0213  98  LEU   A O     
521  C  CB    . LEU   A 98  ? 0.5848 0.5311 0.7042 -0.0118 0.0386  0.009   98  LEU   A CB    
522  C  CG    . LEU   A 98  ? 0.6013 0.5548 0.7358 -0.0164 0.0375  0.0066  98  LEU   A CG    
523  C  CD1   . LEU   A 98  ? 0.5971 0.5624 0.7329 -0.0166 0.0365  0.0069  98  LEU   A CD1   
524  C  CD2   . LEU   A 98  ? 0.6059 0.5531 0.7511 -0.0197 0.0438  0.0113  98  LEU   A CD2   
525  N  N     . TYR   A 99  ? 0.5862 0.5188 0.6838 -0.0033 0.035   0.0127  99  TYR   A N     
526  C  CA    . TYR   A 99  ? 0.5924 0.521  0.6781 -0.0001 0.033   0.0171  99  TYR   A CA    
527  C  C     . TYR   A 99  ? 0.6055 0.521  0.6886 0.0015  0.0326  0.0214  99  TYR   A C     
528  O  O     . TYR   A 99  ? 0.6198 0.5271 0.6911 0.0019  0.0325  0.0277  99  TYR   A O     
529  C  CB    . TYR   A 99  ? 0.581  0.5205 0.6665 0.0029  0.028   0.0134  99  TYR   A CB    
530  C  CG    . TYR   A 99  ? 0.5807 0.5303 0.6627 0.0016  0.0281  0.0123  99  TYR   A CG    
531  C  CD1   . TYR   A 99  ? 0.5884 0.5378 0.6701 -0.0016 0.0327  0.0141  99  TYR   A CD1   
532  C  CD2   . TYR   A 99  ? 0.5863 0.5451 0.6664 0.0038  0.0244  0.0101  99  TYR   A CD2   
533  C  CE1   . TYR   A 99  ? 0.5935 0.5509 0.6724 -0.0023 0.0332  0.0139  99  TYR   A CE1   
534  C  CE2   . TYR   A 99  ? 0.5963 0.5632 0.6729 0.0026  0.0247  0.0097  99  TYR   A CE2   
535  C  CZ    . TYR   A 99  ? 0.6034 0.5694 0.6792 -0.0003 0.0289  0.0116  99  TYR   A CZ    
536  O  OH    . TYR   A 99  ? 0.6197 0.5926 0.6925 -0.001  0.0295  0.0116  99  TYR   A OH    
537  N  N     . ILE   A 100 ? 0.6015 0.5135 0.6943 0.002   0.0325  0.0184  100 ILE   A N     
538  C  CA    . ILE   A 100 ? 0.6164 0.5153 0.7084 0.0036  0.0324  0.0228  100 ILE   A CA    
539  C  C     . ILE   A 100 ? 0.6374 0.5249 0.7239 0       0.0382  0.0285  100 ILE   A C     
540  O  O     . ILE   A 100 ? 0.6454 0.5216 0.7206 0.0007  0.0382  0.0355  100 ILE   A O     
541  C  CB    . ILE   A 100 ? 0.6168 0.5139 0.721  0.0047  0.032   0.0172  100 ILE   A CB    
542  C  CG1   . ILE   A 100 ? 0.6278 0.5332 0.7357 0.0092  0.0281  0.0124  100 ILE   A CG1   
543  C  CG2   . ILE   A 100 ? 0.6193 0.5013 0.7245 0.0055  0.0333  0.0219  100 ILE   A CG2   
544  C  CD1   . ILE   A 100 ? 0.6432 0.5462 0.7608 0.0096  0.0292  0.0046  100 ILE   A CD1   
545  N  N     . ARG   A 101 ? 0.6395 0.5301 0.7336 -0.004  0.043   0.026   101 ARG   A N     
546  C  CA    . ARG   A 101 ? 0.6665 0.5479 0.7586 -0.0076 0.0505  0.0312  101 ARG   A CA    
547  C  C     . ARG   A 101 ? 0.6692 0.546  0.7439 -0.0076 0.0535  0.0369  101 ARG   A C     
548  O  O     . ARG   A 101 ? 0.677  0.5391 0.7408 -0.0087 0.0585  0.0433  101 ARG   A O     
549  C  CB    . ARG   A 101 ? 0.7109 0.6002 0.8189 -0.0118 0.0538  0.0272  101 ARG   A CB    
550  C  CG    . ARG   A 101 ? 0.8369 0.7231 0.9463 -0.0153 0.0628  0.0319  101 ARG   A CG    
551  C  CD    . ARG   A 101 ? 0.9469 0.8453 1.0756 -0.0191 0.0633  0.028   101 ARG   A CD    
552  N  NE    . ARG   A 101 ? 1.046  0.9434 1.1809 -0.022  0.0728  0.0328  101 ARG   A NE    
553  C  CZ    . ARG   A 101 ? 1.1114 1.021  1.2571 -0.0235 0.074   0.032   101 ARG   A CZ    
554  N  NH1   . ARG   A 101 ? 1.1062 1.0292 1.2553 -0.0227 0.0658  0.0265  101 ARG   A NH1   
555  N  NH2   . ARG   A 101 ? 1.131  1.0388 1.2844 -0.0256 0.0841  0.037   101 ARG   A NH2   
556  N  N     . ALA   A 102 ? 0.6586 0.5459 0.7287 -0.0064 0.0505  0.0347  102 ALA   A N     
557  C  CA    . ALA   A 102 ? 0.6636 0.5455 0.7158 -0.0066 0.0527  0.0393  102 ALA   A CA    
558  C  C     . ALA   A 102 ? 0.6653 0.5346 0.7012 -0.0048 0.0478  0.0447  102 ALA   A C     
559  O  O     . ALA   A 102 ? 0.6777 0.5325 0.696  -0.0065 0.0517  0.0505  102 ALA   A O     
560  C  CB    . ALA   A 102 ? 0.6585 0.5543 0.7105 -0.0057 0.0495  0.0354  102 ALA   A CB    
561  N  N     . PHE   A 103 ? 0.6544 0.5283 0.6962 -0.0015 0.0394  0.0432  103 PHE   A N     
562  C  CA    . PHE   A 103 ? 0.6668 0.5308 0.6979 0.0006  0.0328  0.049   103 PHE   A CA    
563  C  C     . PHE   A 103 ? 0.691  0.5371 0.7162 -0.0008 0.0366  0.0549  103 PHE   A C     
564  O  O     . PHE   A 103 ? 0.6993 0.531  0.7059 -0.0016 0.0348  0.062   103 PHE   A O     
565  C  CB    . PHE   A 103 ? 0.652  0.5259 0.6971 0.005   0.025   0.0459  103 PHE   A CB    
566  C  CG    . PHE   A 103 ? 0.6596 0.5259 0.6988 0.0076  0.0169  0.0527  103 PHE   A CG    
567  C  CD1   . PHE   A 103 ? 0.6693 0.5374 0.6977 0.0077  0.01    0.0561  103 PHE   A CD1   
568  C  CD2   . PHE   A 103 ? 0.6745 0.5314 0.7196 0.0096  0.0156  0.056   103 PHE   A CD2   
569  C  CE1   . PHE   A 103 ? 0.6886 0.55   0.7131 0.0096  0.0009  0.0633  103 PHE   A CE1   
570  C  CE2   . PHE   A 103 ? 0.694  0.5441 0.7352 0.0121  0.0072  0.0634  103 PHE   A CE2   
571  C  CZ    . PHE   A 103 ? 0.6953 0.5482 0.7268 0.012   -0.0007 0.0671  103 PHE   A CZ    
572  N  N     . GLN   A 104 ? 0.6969 0.543  0.737  -0.0015 0.0415  0.0521  104 GLN   A N     
573  C  CA    . GLN   A 104 ? 0.7252 0.5546 0.7618 -0.003  0.0461  0.0575  104 GLN   A CA    
574  C  C     . GLN   A 104 ? 0.7385 0.555  0.7575 -0.0069 0.0549  0.0627  104 GLN   A C     
575  O  O     . GLN   A 104 ? 0.7554 0.5548 0.7563 -0.0076 0.0547  0.0701  104 GLN   A O     
576  C  CB    . GLN   A 104 ? 0.7542 0.5867 0.8113 -0.0038 0.0497  0.0527  104 GLN   A CB    
577  C  CG    . GLN   A 104 ? 0.8342 0.6742 0.9052 0.0002  0.0426  0.0478  104 GLN   A CG    
578  C  CD    . GLN   A 104 ? 0.9266 0.7678 1.0151 -0.0015 0.0459  0.0421  104 GLN   A CD    
579  O  OE1   . GLN   A 104 ? 0.9506 0.7969 1.0465 -0.0057 0.0509  0.0387  104 GLN   A OE1   
580  N  NE2   . GLN   A 104 ? 0.937  0.7733 1.0332 0.0014  0.0428  0.0411  104 GLN   A NE2   
581  N  N     . LYS   A 105 ? 0.7271 0.5509 0.7504 -0.0094 0.0624  0.0594  105 LYS   A N     
582  C  CA    . LYS   A 105 ? 0.7386 0.5499 0.7465 -0.0126 0.073   0.064   105 LYS   A CA    
583  C  C     . LYS   A 105 ? 0.765  0.564  0.7442 -0.0127 0.07    0.0689  105 LYS   A C     
584  O  O     . LYS   A 105 ? 0.7864 0.5653 0.7453 -0.0149 0.0757  0.0752  105 LYS   A O     
585  C  CB    . LYS   A 105 ? 0.739  0.5629 0.7594 -0.0143 0.0806  0.0596  105 LYS   A CB    
586  C  CG    . LYS   A 105 ? 0.762  0.5943 0.8085 -0.0161 0.0851  0.0564  105 LYS   A CG    
587  C  CD    . LYS   A 105 ? 0.7962 0.6426 0.8557 -0.0174 0.09    0.0529  105 LYS   A CD    
588  C  CE    . LYS   A 105 ? 0.8376 0.6911 0.9229 -0.0204 0.0946  0.0513  105 LYS   A CE    
589  N  NZ    . LYS   A 105 ? 0.8696 0.7375 0.9693 -0.0214 0.0978  0.0489  105 LYS   A NZ    
590  N  N     . LEU   A 106 ? 0.763  0.5726 0.7393 -0.0107 0.0609  0.0661  106 LEU   A N     
591  C  CA    . LEU   A 106 ? 0.7825 0.5809 0.7322 -0.0115 0.0559  0.0704  106 LEU   A CA    
592  C  C     . LEU   A 106 ? 0.811  0.5941 0.747  -0.0111 0.0475  0.0775  106 LEU   A C     
593  O  O     . LEU   A 106 ? 0.8391 0.6022 0.7476 -0.0138 0.0484  0.0837  106 LEU   A O     
594  C  CB    . LEU   A 106 ? 0.7685 0.5831 0.7216 -0.0098 0.0477  0.0659  106 LEU   A CB    
595  C  CG    . LEU   A 106 ? 0.7691 0.5933 0.7266 -0.011  0.0559  0.061   106 LEU   A CG    
596  C  CD1   . LEU   A 106 ? 0.7578 0.6028 0.7294 -0.0086 0.0484  0.0552  106 LEU   A CD1   
597  C  CD2   . LEU   A 106 ? 0.7835 0.591  0.7138 -0.0141 0.0625  0.0643  106 LEU   A CD2   
598  N  N     . THR   A 107 ? 0.7995 0.5903 0.7537 -0.0077 0.0398  0.077   107 THR   A N     
599  C  CA    . THR   A 107 ? 0.8257 0.6032 0.7707 -0.0066 0.0312  0.0845  107 THR   A CA    
600  C  C     . THR   A 107 ? 0.8552 0.6122 0.7903 -0.009  0.0394  0.0904  107 THR   A C     
601  O  O     . THR   A 107 ? 0.8685 0.6082 0.7856 -0.0097 0.0339  0.0984  107 THR   A O     
602  C  CB    . THR   A 107 ? 0.8264 0.6179 0.7945 -0.0017 0.0211  0.0826  107 THR   A CB    
603  O  OG1   . THR   A 107 ? 0.8315 0.6341 0.8238 -0.0002 0.0274  0.0758  107 THR   A OG1   
604  C  CG2   . THR   A 107 ? 0.8178 0.6244 0.7897 0.0003  0.0117  0.0799  107 THR   A CG2   
605  N  N     . ASP   A 108 ? 0.8592 0.6179 0.8059 -0.0106 0.0521  0.0869  108 ASP   A N     
606  C  CA    . ASP   A 108 ? 0.8785 0.6186 0.8176 -0.0132 0.0618  0.0923  108 ASP   A CA    
607  C  C     . ASP   A 108 ? 0.8985 0.6186 0.8063 -0.0173 0.0702  0.0973  108 ASP   A C     
608  O  O     . ASP   A 108 ? 0.9179 0.6171 0.81   -0.0196 0.0758  0.1041  108 ASP   A O     
609  C  CB    . ASP   A 108 ? 0.8954 0.6449 0.8601 -0.0141 0.0723  0.087   108 ASP   A CB    
610  C  CG    . ASP   A 108 ? 0.975  0.7347 0.9653 -0.0113 0.0664  0.0834  108 ASP   A CG    
611  O  OD1   . ASP   A 108 ? 0.9961 0.7523 0.9846 -0.0081 0.0563  0.0865  108 ASP   A OD1   
612  O  OD2   . ASP   A 108 ? 0.9981 0.7692 1.0106 -0.0123 0.0717  0.0774  108 ASP   A OD2   
613  N  N     . PHE   A 109 ? 0.8957 0.6207 0.7938 -0.0184 0.0724  0.094   109 PHE   A N     
614  C  CA    . PHE   A 109 ? 0.9162 0.6209 0.7834 -0.0223 0.082   0.0977  109 PHE   A CA    
615  C  C     . PHE   A 109 ? 0.9585 0.64   0.7917 -0.0241 0.0731  0.1059  109 PHE   A C     
616  O  O     . PHE   A 109 ? 0.9672 0.6538 0.7966 -0.0228 0.0575  0.1066  109 PHE   A O     
617  C  CB    . PHE   A 109 ? 0.9011 0.6165 0.767  -0.0226 0.0855  0.0919  109 PHE   A CB    
618  C  CG    . PHE   A 109 ? 0.9103 0.6084 0.7569 -0.026  0.1029  0.0935  109 PHE   A CG    
619  C  CD1   . PHE   A 109 ? 0.9366 0.6095 0.7436 -0.0293 0.1043  0.0983  109 PHE   A CD1   
620  C  CD2   . PHE   A 109 ? 0.9029 0.6085 0.7708 -0.0262 0.1181  0.0909  109 PHE   A CD2   
621  C  CE1   . PHE   A 109 ? 0.9533 0.6075 0.741  -0.0322 0.1224  0.0997  109 PHE   A CE1   
622  C  CE2   . PHE   A 109 ? 0.9195 0.6091 0.7721 -0.0288 0.1358  0.0929  109 PHE   A CE2   
623  C  CZ    . PHE   A 109 ? 0.9383 0.6015 0.7501 -0.0315 0.1388  0.097   109 PHE   A CZ    
624  N  N     . PRO   A 110 ? 0.9853 0.6407 0.7943 -0.0275 0.0824  0.1126  110 PRO   A N     
625  C  CA    . PRO   A 110 ? 1.0205 0.6512 0.794  -0.03   0.073   0.1211  110 PRO   A CA    
626  C  C     . PRO   A 110 ? 1.0557 0.6774 0.7989 -0.0329 0.0677  0.1208  110 PRO   A C     
627  O  O     . PRO   A 110 ? 1.0554 0.6807 0.7962 -0.0339 0.0781  0.1153  110 PRO   A O     
628  C  CB    . PRO   A 110 ? 1.0396 0.6441 0.794  -0.0333 0.0882  0.1273  110 PRO   A CB    
629  C  CG    . PRO   A 110 ? 1.0254 0.645  0.8136 -0.0318 0.1026  0.1225  110 PRO   A CG    
630  C  CD    . PRO   A 110 ? 0.9828 0.6293 0.7951 -0.0295 0.1021  0.1132  110 PRO   A CD    
631  N  N     . PRO   A 111 ? 1.0853 0.6935 0.8042 -0.0346 0.0514  0.1272  111 PRO   A N     
632  C  CA    . PRO   A 111 ? 1.1149 0.7122 0.8024 -0.0385 0.0452  0.1271  111 PRO   A CA    
633  C  C     . PRO   A 111 ? 1.1498 0.724  0.8055 -0.043  0.064   0.1259  111 PRO   A C     
634  O  O     . PRO   A 111 ? 1.169  0.7217 0.8081 -0.0451 0.0773  0.1303  111 PRO   A O     
635  C  CB    . PRO   A 111 ? 1.1399 0.7192 0.8027 -0.041  0.0265  0.1367  111 PRO   A CB    
636  C  CG    . PRO   A 111 ? 1.1258 0.7179 0.8196 -0.0361 0.0191  0.1402  111 PRO   A CG    
637  C  CD    . PRO   A 111 ? 1.0868 0.6883 0.806  -0.0334 0.0376  0.1354  111 PRO   A CD    
638  N  N     . ILE   A 112 ? 1.1582 0.7375 0.8081 -0.0441 0.0666  0.1198  112 ILE   A N     
639  C  CA    . ILE   A 112 ? 1.189  0.7472 0.8105 -0.0477 0.0852  0.1178  112 ILE   A CA    
640  C  C     . ILE   A 112 ? 1.241  0.7616 0.8086 -0.0542 0.0806  0.1247  112 ILE   A C     
641  O  O     . ILE   A 112 ? 1.2514 0.7679 0.801  -0.0569 0.0625  0.1262  112 ILE   A O     
642  C  CB    . ILE   A 112 ? 1.1789 0.7546 0.8119 -0.0466 0.0879  0.1093  112 ILE   A CB    
643  C  CG1   . ILE   A 112 ? 1.1559 0.7655 0.839  -0.0408 0.0945  0.1029  112 ILE   A CG1   
644  C  CG2   . ILE   A 112 ? 1.2053 0.7551 0.8032 -0.0506 0.1051  0.1077  112 ILE   A CG2   
645  C  CD1   . ILE   A 112 ? 1.1568 0.7866 0.8546 -0.0392 0.0937  0.0952  112 ILE   A CD1   
646  N  N     . LYS   A 113 ? 1.2714 0.7642 0.8137 -0.057  0.096   0.1295  113 LYS   A N     
647  C  CA    . LYS   A 113 ? 1.3215 0.7745 0.8081 -0.0637 0.093   0.1364  113 LYS   A CA    
648  C  C     . LYS   A 113 ? 1.3545 0.7816 0.8056 -0.0677 0.1137  0.1328  113 LYS   A C     
649  O  O     . LYS   A 113 ? 1.3914 0.789  0.7945 -0.0739 0.1082  0.1351  113 LYS   A O     
650  C  CB    . LYS   A 113 ? 1.3603 0.7941 0.8354 -0.0647 0.0954  0.1455  113 LYS   A CB    
651  C  CG    . LYS   A 113 ? 1.3994 0.8587 0.9162 -0.0596 0.0821  0.1484  113 LYS   A CG    
652  C  CD    . LYS   A 113 ? 1.4666 0.9198 0.9697 -0.0612 0.0553  0.1564  113 LYS   A CD    
653  C  CE    . LYS   A 113 ? 1.4959 0.9652 1.034  -0.0562 0.0476  0.1609  113 LYS   A CE    
654  N  NZ    . LYS   A 113 ? 1.5218 0.9944 1.0603 -0.0559 0.0205  0.1677  113 LYS   A NZ    
655  N  N     . ASP   A 114 ? 1.3358 0.7725 0.8099 -0.0645 0.1375  0.1276  114 ASP   A N     
656  C  CA    . ASP   A 114 ? 1.3475 0.7594 0.7919 -0.0673 0.1604  0.1247  114 ASP   A CA    
657  C  C     . ASP   A 114 ? 1.3164 0.7545 0.7991 -0.0625 0.1759  0.1162  114 ASP   A C     
658  O  O     . ASP   A 114 ? 1.2929 0.7679 0.8228 -0.0574 0.1674  0.1125  114 ASP   A O     
659  C  CB    . ASP   A 114 ? 1.3836 0.7631 0.8008 -0.0701 0.1799  0.1312  114 ASP   A CB    
660  C  CG    . ASP   A 114 ? 1.4221 0.8213 0.8829 -0.0656 0.1898  0.1333  114 ASP   A CG    
661  O  OD1   . ASP   A 114 ? 1.3987 0.8303 0.9071 -0.0605 0.1958  0.1275  114 ASP   A OD1   
662  O  OD2   . ASP   A 114 ? 1.4721 0.8529 0.9182 -0.0675 0.1913  0.1409  114 ASP   A OD2   
663  N  N     . GLN   A 115 ? 1.3166 0.734  0.7779 -0.064  0.1989  0.1135  115 GLN   A N     
664  C  CA    . GLN   A 115 ? 1.2949 0.7312 0.7873 -0.0598 0.2158  0.1067  115 GLN   A CA    
665  C  C     . GLN   A 115 ? 1.2481 0.7136 0.795  -0.0544 0.2261  0.1068  115 GLN   A C     
666  O  O     . GLN   A 115 ? 1.2305 0.7278 0.8191 -0.0499 0.2256  0.1015  115 GLN   A O     
667  C  CB    . GLN   A 115 ? 1.351  0.7523 0.805  -0.0627 0.2409  0.1057  115 GLN   A CB    
668  C  CG    . GLN   A 115 ? 1.4284 0.8408 0.8949 -0.0602 0.2492  0.0981  115 GLN   A CG    
669  C  CD    . GLN   A 115 ? 1.5332 0.9472 0.9808 -0.0629 0.2266  0.0944  115 GLN   A CD    
670  O  OE1   . GLN   A 115 ? 1.6061 0.9892 1.0032 -0.0692 0.2173  0.0965  115 GLN   A OE1   
671  N  NE2   . GLN   A 115 ? 1.5013 0.9503 0.9881 -0.0586 0.2172  0.089   115 GLN   A NE2   
672  N  N     . ALA   A 116 ? 1.2271 0.6813 0.7733 -0.0552 0.2347  0.1129  116 ALA   A N     
673  C  CA    . ALA   A 116 ? 1.1865 0.6655 0.7825 -0.0513 0.2437  0.1136  116 ALA   A CA    
674  C  C     . ALA   A 116 ? 1.1422 0.6584 0.7798 -0.0477 0.2208  0.1113  116 ALA   A C     
675  O  O     . ALA   A 116 ? 1.1205 0.6657 0.8044 -0.044  0.2246  0.1081  116 ALA   A O     
676  C  CB    . ALA   A 116 ? 1.1964 0.6515 0.7776 -0.0538 0.2567  0.1212  116 ALA   A CB    
677  N  N     . ASP   A 117 ? 1.1282 0.6427 0.7492 -0.0491 0.1972  0.1132  117 ASP   A N     
678  C  CA    . ASP   A 117 ? 1.0983 0.6446 0.7541 -0.0457 0.1756  0.1111  117 ASP   A CA    
679  C  C     . ASP   A 117 ? 1.068  0.6408 0.7461 -0.0428 0.1693  0.1032  117 ASP   A C     
680  O  O     . ASP   A 117 ? 1.0398 0.6439 0.7607 -0.0389 0.1648  0.0992  117 ASP   A O     
681  C  CB    . ASP   A 117 ? 1.1388 0.6734 0.7681 -0.0479 0.1532  0.116   117 ASP   A CB    
682  C  CG    . ASP   A 117 ? 1.2264 0.7411 0.8412 -0.0498 0.1532  0.1244  117 ASP   A CG    
683  O  OD1   . ASP   A 117 ? 1.2367 0.7483 0.8652 -0.0494 0.1706  0.1262  117 ASP   A OD1   
684  O  OD2   . ASP   A 117 ? 1.2718 0.7741 0.863  -0.0518 0.1353  0.1296  117 ASP   A OD2   
685  N  N     . GLU   A 118 ? 1.0692 0.6277 0.7165 -0.0451 0.1692  0.101   118 GLU   A N     
686  C  CA    . GLU   A 118 ? 1.0495 0.6296 0.7133 -0.0429 0.1633  0.0942  118 GLU   A CA    
687  C  C     . GLU   A 118 ? 1.0273 0.6258 0.7264 -0.0393 0.1811  0.09    118 GLU   A C     
688  O  O     . GLU   A 118 ? 1.008  0.636  0.7403 -0.0359 0.1737  0.0851  118 GLU   A O     
689  C  CB    . GLU   A 118 ? 1.095  0.6512 0.7146 -0.0471 0.1605  0.0932  118 GLU   A CB    
690  C  CG    . GLU   A 118 ? 1.1322 0.7083 0.7634 -0.0456 0.1495  0.0871  118 GLU   A CG    
691  C  CD    . GLU   A 118 ? 1.2024 0.7842 0.8462 -0.0435 0.1676  0.0818  118 GLU   A CD    
692  O  OE1   . GLU   A 118 ? 1.2315 0.793  0.8622 -0.0443 0.1897  0.0831  118 GLU   A OE1   
693  O  OE2   . GLU   A 118 ? 1.2291 0.8358 0.8975 -0.0407 0.1604  0.0769  118 GLU   A OE2   
694  N  N     . ALA   A 119 ? 1.03   0.6115 0.724  -0.0401 0.2043  0.0925  119 ALA   A N     
695  C  CA    . ALA   A 119 ? 1.0107 0.609  0.7408 -0.0369 0.2217  0.09    119 ALA   A CA    
696  C  C     . ALA   A 119 ? 0.9911 0.6212 0.7698 -0.0339 0.2146  0.0893  119 ALA   A C     
697  O  O     . ALA   A 119 ? 0.9793 0.636  0.7937 -0.0308 0.2143  0.0852  119 ALA   A O     
698  C  CB    . ALA   A 119 ? 1.0173 0.5892 0.7319 -0.0385 0.2484  0.0939  119 ALA   A CB    
699  N  N     . GLN   A 120 ? 0.9821 0.609  0.7613 -0.035  0.2076  0.0934  120 GLN   A N     
700  C  CA    . GLN   A 120 ? 0.9509 0.6048 0.7729 -0.0327 0.2003  0.0925  120 GLN   A CA    
701  C  C     . GLN   A 120 ? 0.9224 0.6021 0.7612 -0.0303 0.1781  0.0873  120 GLN   A C     
702  O  O     . GLN   A 120 ? 0.9013 0.6076 0.7779 -0.028  0.1745  0.0836  120 GLN   A O     
703  C  CB    . GLN   A 120 ? 0.9761 0.6167 0.7934 -0.0346 0.2011  0.0984  120 GLN   A CB    
704  C  CG    . GLN   A 120 ? 1.0367 0.6545 0.8438 -0.0369 0.2254  0.1035  120 GLN   A CG    
705  C  CD    . GLN   A 120 ? 1.0977 0.7317 0.9431 -0.0354 0.2425  0.102   120 GLN   A CD    
706  O  OE1   . GLN   A 120 ? 1.1326 0.7505 0.969  -0.0362 0.2642  0.1043  120 GLN   A OE1   
707  N  NE2   . GLN   A 120 ? 1.0861 0.7513 0.9751 -0.0333 0.2337  0.0985  120 GLN   A NE2   
708  N  N     . TYR   A 121 ? 0.9216 0.5931 0.7325 -0.0311 0.1637  0.0872  121 TYR   A N     
709  C  CA    . TYR   A 121 ? 0.9032 0.5976 0.7283 -0.0288 0.1441  0.0827  121 TYR   A CA    
710  C  C     . TYR   A 121 ? 0.8843 0.5982 0.7289 -0.0267 0.1474  0.0767  121 TYR   A C     
711  O  O     . TYR   A 121 ? 0.8678 0.6077 0.7405 -0.0241 0.137   0.0725  121 TYR   A O     
712  C  CB    . TYR   A 121 ? 0.9238 0.6034 0.7145 -0.0308 0.1293  0.0849  121 TYR   A CB    
713  C  CG    . TYR   A 121 ? 0.9233 0.6254 0.7302 -0.0284 0.1089  0.0817  121 TYR   A CG    
714  C  CD1   . TYR   A 121 ? 0.9235 0.6383 0.7514 -0.0262 0.0982  0.0826  121 TYR   A CD1   
715  C  CD2   . TYR   A 121 ? 0.931  0.6408 0.7324 -0.0283 0.1014  0.0778  121 TYR   A CD2   
716  C  CE1   . TYR   A 121 ? 0.9222 0.6565 0.7652 -0.0236 0.0815  0.0798  121 TYR   A CE1   
717  C  CE2   . TYR   A 121 ? 0.9322 0.6622 0.7491 -0.0261 0.0841  0.0753  121 TYR   A CE2   
718  C  CZ    . TYR   A 121 ? 0.9371 0.6793 0.7748 -0.0236 0.0746  0.0764  121 TYR   A CZ    
719  O  OH    . TYR   A 121 ? 0.9541 0.7155 0.8079 -0.0211 0.0594  0.074   121 TYR   A OH    
720  N  N     . CYS   A 122 ? 0.8818 0.5824 0.7117 -0.0277 0.1628  0.0766  122 CYS   A N     
721  C  CA    . CYS   A 122 ? 0.8633 0.5799 0.7118 -0.0256 0.1681  0.072   122 CYS   A CA    
722  C  C     . CYS   A 122 ? 0.824  0.5658 0.7178 -0.0231 0.1723  0.0707  122 CYS   A C     
723  O  O     . CYS   A 122 ? 0.8178 0.583  0.7356 -0.0209 0.1652  0.0665  122 CYS   A O     
724  C  CB    . CYS   A 122 ? 0.8947 0.5884 0.7185 -0.0269 0.1864  0.0729  122 CYS   A CB    
725  S  SG    . CYS   A 122 ? 0.9705 0.6394 0.7437 -0.0303 0.1784  0.0721  122 CYS   A SG    
726  N  N     . GLN   A 123 ? 0.8041 0.5406 0.7091 -0.024  0.1827  0.0744  123 GLN   A N     
727  C  CA    . GLN   A 123 ? 0.7736 0.5319 0.7212 -0.0229 0.1855  0.0739  123 GLN   A CA    
728  C  C     . GLN   A 123 ? 0.7424 0.5236 0.7111 -0.0218 0.1659  0.0701  123 GLN   A C     
729  O  O     . GLN   A 123 ? 0.7185 0.5226 0.719  -0.0206 0.1625  0.0669  123 GLN   A O     
730  C  CB    . GLN   A 123 ? 0.8    0.5446 0.7516 -0.025  0.1999  0.0793  123 GLN   A CB    
731  C  CG    . GLN   A 123 ? 0.8789 0.6029 0.817  -0.0257 0.2232  0.083   123 GLN   A CG    
732  C  CD    . GLN   A 123 ? 0.9547 0.6954 0.9236 -0.0236 0.2334  0.0815  123 GLN   A CD    
733  O  OE1   . GLN   A 123 ? 0.9992 0.7456 0.964  -0.0217 0.2306  0.0781  123 GLN   A OE1   
734  N  NE2   . GLN   A 123 ? 0.9557 0.7049 0.958  -0.0239 0.2451  0.0846  123 GLN   A NE2   
735  N  N     . LEU   A 124 ? 0.7386 0.5125 0.6891 -0.0222 0.1534  0.0707  124 LEU   A N     
736  C  CA    . LEU   A 124 ? 0.724  0.5165 0.6911 -0.0207 0.1361  0.0671  124 LEU   A CA    
737  C  C     . LEU   A 124 ? 0.7198 0.5295 0.6913 -0.0186 0.1262  0.0618  124 LEU   A C     
738  O  O     . LEU   A 124 ? 0.7104 0.5417 0.7078 -0.0173 0.1189  0.0576  124 LEU   A O     
739  C  CB    . LEU   A 124 ? 0.7317 0.5101 0.6775 -0.0212 0.1263  0.0702  124 LEU   A CB    
740  C  CG    . LEU   A 124 ? 0.7372 0.5309 0.6931 -0.0189 0.1083  0.0668  124 LEU   A CG    
741  C  CD1   . LEU   A 124 ? 0.7186 0.5312 0.7084 -0.0181 0.106   0.063   124 LEU   A CD1   
742  C  CD2   . LEU   A 124 ? 0.7565 0.5342 0.6915 -0.0192 0.1     0.0714  124 LEU   A CD2   
743  N  N     . VAL   A 125 ? 0.7222 0.5211 0.6677 -0.0189 0.1265  0.0621  125 VAL   A N     
744  C  CA    . VAL   A 125 ? 0.7161 0.5289 0.6636 -0.0173 0.1184  0.0577  125 VAL   A CA    
745  C  C     . VAL   A 125 ? 0.7161 0.5463 0.6906 -0.016  0.1253  0.055   125 VAL   A C     
746  O  O     . VAL   A 125 ? 0.7099 0.5602 0.7015 -0.0144 0.1157  0.0509  125 VAL   A O     
747  C  CB    . VAL   A 125 ? 0.7319 0.5263 0.6444 -0.0188 0.1183  0.059   125 VAL   A CB    
748  C  CG1   . VAL   A 125 ? 0.733  0.541  0.6489 -0.0175 0.1123  0.0547  125 VAL   A CG1   
749  C  CG2   . VAL   A 125 ? 0.7425 0.5237 0.632  -0.0202 0.1068  0.062   125 VAL   A CG2   
750  N  N     . ARG   A 126 ? 0.717  0.5395 0.6968 -0.0167 0.142   0.0577  126 ARG   A N     
751  C  CA    . ARG   A 126 ? 0.7151 0.5541 0.7241 -0.0154 0.1486  0.0566  126 ARG   A CA    
752  C  C     . ARG   A 126 ? 0.6953 0.5555 0.737  -0.0154 0.1401  0.0547  126 ARG   A C     
753  O  O     . ARG   A 126 ? 0.6888 0.5684 0.7504 -0.0143 0.1336  0.0516  126 ARG   A O     
754  C  CB    . ARG   A 126 ? 0.7566 0.5824 0.7681 -0.016  0.1694  0.061   126 ARG   A CB    
755  C  CG    . ARG   A 126 ? 0.8612 0.6643 0.8399 -0.0162 0.1802  0.0621  126 ARG   A CG    
756  C  CD    . ARG   A 126 ? 0.9378 0.7246 0.9165 -0.0166 0.203   0.0666  126 ARG   A CD    
757  N  NE    . ARG   A 126 ? 1.0229 0.7862 0.968  -0.0168 0.2139  0.0668  126 ARG   A NE    
758  C  CZ    . ARG   A 126 ? 1.0913 0.8249 1.0014 -0.0192 0.2241  0.0696  126 ARG   A CZ    
759  N  NH1   . ARG   A 126 ? 1.0971 0.8216 1.003  -0.0212 0.2253  0.0731  126 ARG   A NH1   
760  N  NH2   . ARG   A 126 ? 1.1154 0.8266 0.9933 -0.0199 0.2334  0.069   126 ARG   A NH2   
761  N  N     . GLN   A 127 ? 0.6832 0.5383 0.729  -0.017  0.1399  0.0565  127 GLN   A N     
762  C  CA    . GLN   A 127 ? 0.662  0.5334 0.7357 -0.0178 0.1319  0.0544  127 GLN   A CA    
763  C  C     . GLN   A 127 ? 0.6574 0.5432 0.7319 -0.0163 0.1147  0.0488  127 GLN   A C     
764  O  O     . GLN   A 127 ? 0.6531 0.5568 0.7499 -0.0164 0.1084  0.0455  127 GLN   A O     
765  C  CB    . GLN   A 127 ? 0.6803 0.5393 0.7522 -0.0198 0.1349  0.0575  127 GLN   A CB    
766  C  CG    . GLN   A 127 ? 0.7151 0.5879 0.8157 -0.0214 0.1287  0.0555  127 GLN   A CG    
767  C  CD    . GLN   A 127 ? 0.7884 0.6482 0.8845 -0.0231 0.1293  0.058   127 GLN   A CD    
768  O  OE1   . GLN   A 127 ? 0.8079 0.6606 0.8867 -0.0219 0.1208  0.0572  127 GLN   A OE1   
769  N  NE2   . GLN   A 127 ? 0.8003 0.6572 0.9141 -0.0258 0.1393  0.0616  127 GLN   A NE2   
770  N  N     . LEU   A 128 ? 0.6574 0.5353 0.708  -0.0151 0.1072  0.048   128 LEU   A N     
771  C  CA    . LEU   A 128 ? 0.6509 0.5417 0.7027 -0.0134 0.0927  0.0432  128 LEU   A CA    
772  C  C     . LEU   A 128 ? 0.6502 0.555  0.7073 -0.0122 0.0899  0.0401  128 LEU   A C     
773  O  O     . LEU   A 128 ? 0.6421 0.5626 0.7127 -0.0115 0.081   0.0359  128 LEU   A O     
774  C  CB    . LEU   A 128 ? 0.6569 0.536  0.6845 -0.0125 0.0859  0.0445  128 LEU   A CB    
775  C  CG    . LEU   A 128 ? 0.6673 0.5339 0.6907 -0.0132 0.0856  0.0476  128 LEU   A CG    
776  C  CD1   . LEU   A 128 ? 0.6725 0.5286 0.6736 -0.0122 0.0773  0.0498  128 LEU   A CD1   
777  C  CD2   . LEU   A 128 ? 0.6611 0.5393 0.7085 -0.0131 0.0807  0.0442  128 LEU   A CD2   
778  N  N     . LEU   A 129 ? 0.6541 0.5518 0.7    -0.012  0.0983  0.0423  129 LEU   A N     
779  C  CA    . LEU   A 129 ? 0.652  0.5613 0.7028 -0.0108 0.0969  0.0401  129 LEU   A CA    
780  C  C     . LEU   A 129 ? 0.6532 0.5794 0.7341 -0.0111 0.0974  0.0391  129 LEU   A C     
781  O  O     . LEU   A 129 ? 0.6497 0.591  0.7401 -0.0103 0.0891  0.0358  129 LEU   A O     
782  C  CB    . LEU   A 129 ? 0.6553 0.5506 0.6888 -0.0108 0.1082  0.0429  129 LEU   A CB    
783  C  CG    . LEU   A 129 ? 0.6782 0.5598 0.6807 -0.011  0.1044  0.0429  129 LEU   A CG    
784  C  CD1   . LEU   A 129 ? 0.6881 0.5511 0.6714 -0.0118 0.1178  0.0455  129 LEU   A CD1   
785  C  CD2   . LEU   A 129 ? 0.6788 0.5743 0.6819 -0.0098 0.0925  0.0391  129 LEU   A CD2   
786  N  N     . ASP   A 130 ? 0.6574 0.5807 0.7534 -0.0126 0.1064  0.0423  130 ASP   A N     
787  C  CA    . ASP   A 130 ? 0.6651 0.6035 0.7918 -0.0137 0.1065  0.0425  130 ASP   A CA    
788  C  C     . ASP   A 130 ? 0.6627 0.6126 0.8028 -0.0154 0.0936  0.0385  130 ASP   A C     
789  O  O     . ASP   A 130 ? 0.6574 0.6226 0.8142 -0.016  0.0863  0.0364  130 ASP   A O     
790  C  CB    . ASP   A 130 ? 0.7096 0.6405 0.8494 -0.0151 0.1211  0.0479  130 ASP   A CB    
791  C  CG    . ASP   A 130 ? 0.8154 0.7623 0.9902 -0.0167 0.1211  0.0495  130 ASP   A CG    
792  O  OD1   . ASP   A 130 ? 0.8313 0.7892 1.017  -0.0153 0.1202  0.0498  130 ASP   A OD1   
793  O  OD2   . ASP   A 130 ? 0.8559 0.8045 1.0483 -0.0195 0.1213  0.0508  130 ASP   A OD2   
794  N  N     . ASP   A 131 ? 0.6564 0.5977 0.7883 -0.0162 0.091   0.0377  131 ASP   A N     
795  C  CA    . ASP   A 131 ? 0.6439 0.5927 0.786  -0.0177 0.0802  0.0334  131 ASP   A CA    
796  C  C     . ASP   A 131 ? 0.6376 0.5965 0.7735 -0.0161 0.0685  0.0279  131 ASP   A C     
797  O  O     . ASP   A 131 ? 0.6388 0.6065 0.7858 -0.0176 0.0602  0.0238  131 ASP   A O     
798  C  CB    . ASP   A 131 ? 0.6632 0.5987 0.7957 -0.0181 0.0807  0.034   131 ASP   A CB    
799  C  CG    . ASP   A 131 ? 0.7224 0.6487 0.8649 -0.0207 0.091   0.0388  131 ASP   A CG    
800  O  OD1   . ASP   A 131 ? 0.7221 0.6536 0.882  -0.0222 0.0982  0.0417  131 ASP   A OD1   
801  O  OD2   . ASP   A 131 ? 0.7641 0.678  0.8979 -0.0211 0.0922  0.0402  131 ASP   A OD2   
802  N  N     . HIS   A 132 ? 0.631  0.5873 0.7483 -0.0133 0.0679  0.0278  132 HIS   A N     
803  C  CA    . HIS   A 132 ? 0.6312 0.5965 0.7427 -0.0116 0.058   0.0231  132 HIS   A CA    
804  C  C     . HIS   A 132 ? 0.6249 0.6001 0.7378 -0.0108 0.0574  0.0229  132 HIS   A C     
805  O  O     . HIS   A 132 ? 0.6229 0.603  0.7268 -0.0091 0.0513  0.02    132 HIS   A O     
806  C  CB    . HIS   A 132 ? 0.6512 0.6078 0.743  -0.0094 0.0552  0.0229  132 HIS   A CB    
807  C  CG    . HIS   A 132 ? 0.6999 0.6467 0.7906 -0.0097 0.0551  0.0236  132 HIS   A CG    
808  N  ND1   . HIS   A 132 ? 0.7315 0.6638 0.8143 -0.0105 0.0626  0.0286  132 HIS   A ND1   
809  C  CD2   . HIS   A 132 ? 0.7172 0.6659 0.8142 -0.0096 0.0492  0.0199  132 HIS   A CD2   
810  C  CE1   . HIS   A 132 ? 0.7366 0.6632 0.8216 -0.0107 0.0603  0.0283  132 HIS   A CE1   
811  N  NE2   . HIS   A 132 ? 0.7315 0.6674 0.8254 -0.01   0.0525  0.023   132 HIS   A NE2   
812  N  N     . LYS   A 133 ? 0.6183 0.5965 0.7438 -0.0117 0.0639  0.0262  133 LYS   A N     
813  C  CA    . LYS   A 133 ? 0.6182 0.6048 0.746  -0.0106 0.0637  0.0267  133 LYS   A CA    
814  C  C     . LYS   A 133 ? 0.6131 0.6142 0.7488 -0.0112 0.0525  0.0227  133 LYS   A C     
815  O  O     . LYS   A 133 ? 0.6053 0.6117 0.7353 -0.0097 0.05    0.022   133 LYS   A O     
816  C  CB    . LYS   A 133 ? 0.6297 0.616  0.7719 -0.0109 0.0741  0.0318  133 LYS   A CB    
817  C  CG    . LYS   A 133 ? 0.6767 0.6702 0.8451 -0.0136 0.0738  0.0335  133 LYS   A CG    
818  C  CD    . LYS   A 133 ? 0.7577 0.7488 0.9411 -0.0133 0.0868  0.0396  133 LYS   A CD    
819  C  CE    . LYS   A 133 ? 0.8141 0.8106 1.0252 -0.0165 0.0882  0.0425  133 LYS   A CE    
820  N  NZ    . LYS   A 133 ? 0.8435 0.8554 1.0716 -0.0192 0.074   0.0401  133 LYS   A NZ    
821  N  N     . ASP   A 134 ? 0.6195 0.6248 0.7654 -0.0136 0.0459  0.0198  134 ASP   A N     
822  C  CA    . ASP   A 134 ? 0.6281 0.644  0.7781 -0.0149 0.0355  0.0158  134 ASP   A CA    
823  C  C     . ASP   A 134 ? 0.6306 0.6447 0.7665 -0.0141 0.0292  0.01    134 ASP   A C     
824  O  O     . ASP   A 134 ? 0.6367 0.6564 0.7743 -0.0158 0.0214  0.006   134 ASP   A O     
825  C  CB    . ASP   A 134 ? 0.6534 0.675  0.8246 -0.0191 0.0315  0.0164  134 ASP   A CB    
826  C  CG    . ASP   A 134 ? 0.7538 0.7807 0.9436 -0.0196 0.037   0.0227  134 ASP   A CG    
827  O  OD1   . ASP   A 134 ? 0.772  0.8041 0.9605 -0.0175 0.0378  0.0248  134 ASP   A OD1   
828  O  OD2   . ASP   A 134 ? 0.7993 0.8248 1.006  -0.0219 0.0413  0.026   134 ASP   A OD2   
829  N  N     . VAL   A 135 ? 0.6228 0.6284 0.745  -0.0115 0.0324  0.0098  135 VAL   A N     
830  C  CA    . VAL   A 135 ? 0.6162 0.6199 0.7281 -0.0099 0.0277  0.0052  135 VAL   A CA    
831  C  C     . VAL   A 135 ? 0.6085 0.6207 0.7149 -0.0091 0.0222  0.0017  135 VAL   A C     
832  O  O     . VAL   A 135 ? 0.6175 0.6301 0.7218 -0.0093 0.0178  -0.0032 135 VAL   A O     
833  C  CB    . VAL   A 135 ? 0.6244 0.6185 0.7243 -0.0073 0.0312  0.0074  135 VAL   A CB    
834  C  CG1   . VAL   A 135 ? 0.6348 0.6298 0.7264 -0.0047 0.0267  0.0039  135 VAL   A CG1   
835  C  CG2   . VAL   A 135 ? 0.6269 0.6111 0.7305 -0.0083 0.0351  0.0095  135 VAL   A CG2   
836  N  N     . VAL   A 136 ? 0.5962 0.6137 0.6996 -0.0082 0.023   0.0039  136 VAL   A N     
837  C  CA    . VAL   A 136 ? 0.5995 0.6242 0.6968 -0.0075 0.0184  0.0011  136 VAL   A CA    
838  C  C     . VAL   A 136 ? 0.5972 0.6273 0.7005 -0.0105 0.0123  -0.0021 136 VAL   A C     
839  O  O     . VAL   A 136 ? 0.597  0.6281 0.6929 -0.0105 0.0085  -0.0067 136 VAL   A O     
840  C  CB    . VAL   A 136 ? 0.611  0.6391 0.7036 -0.0061 0.0206  0.0044  136 VAL   A CB    
841  C  CG1   . VAL   A 136 ? 0.6207 0.6548 0.7055 -0.0052 0.0166  0.0016  136 VAL   A CG1   
842  C  CG2   . VAL   A 136 ? 0.62   0.6401 0.7045 -0.0043 0.0259  0.0076  136 VAL   A CG2   
843  N  N     . THR   A 137 ? 0.5904 0.6226 0.7068 -0.0133 0.0114  0.0004  137 THR   A N     
844  C  CA    . THR   A 137 ? 0.5926 0.6289 0.7153 -0.0173 0.0038  -0.0019 137 THR   A CA    
845  C  C     . THR   A 137 ? 0.5951 0.6247 0.714  -0.0191 0.0007  -0.0077 137 THR   A C     
846  O  O     . THR   A 137 ? 0.6039 0.6334 0.7156 -0.0212 -0.0054 -0.0124 137 THR   A O     
847  C  CB    . THR   A 137 ? 0.6045 0.645  0.7462 -0.0199 0.0038  0.0034  137 THR   A CB    
848  O  OG1   . THR   A 137 ? 0.6335 0.6803 0.7775 -0.0181 0.0056  0.0079  137 THR   A OG1   
849  C  CG2   . THR   A 137 ? 0.5971 0.6402 0.7481 -0.0252 -0.0055 0.0016  137 THR   A CG2   
850  N  N     . LEU   A 138 ? 0.5867 0.6093 0.7092 -0.0185 0.0052  -0.0074 138 LEU   A N     
851  C  CA    . LEU   A 138 ? 0.5908 0.6056 0.7104 -0.0198 0.0033  -0.0127 138 LEU   A CA    
852  C  C     . LEU   A 138 ? 0.5922 0.6043 0.6966 -0.0166 0.0035  -0.0178 138 LEU   A C     
853  O  O     . LEU   A 138 ? 0.6026 0.6109 0.7009 -0.0185 -0.0002 -0.0236 138 LEU   A O     
854  C  CB    . LEU   A 138 ? 0.594  0.6013 0.7202 -0.0193 0.0089  -0.0103 138 LEU   A CB    
855  C  CG    . LEU   A 138 ? 0.6065 0.6154 0.7497 -0.0227 0.0103  -0.0054 138 LEU   A CG    
856  C  CD1   . LEU   A 138 ? 0.6177 0.6183 0.7635 -0.0211 0.0183  -0.0016 138 LEU   A CD1   
857  C  CD2   . LEU   A 138 ? 0.6029 0.6118 0.7553 -0.0284 0.003   -0.0085 138 LEU   A CD2   
858  N  N     . LEU   A 139 ? 0.5838 0.5974 0.6821 -0.0121 0.0079  -0.0155 139 LEU   A N     
859  C  CA    . LEU   A 139 ? 0.5916 0.6041 0.6794 -0.0088 0.0088  -0.0192 139 LEU   A CA    
860  C  C     . LEU   A 139 ? 0.607  0.6241 0.687  -0.0102 0.0051  -0.0227 139 LEU   A C     
861  O  O     . LEU   A 139 ? 0.6257 0.6385 0.6978 -0.0098 0.005   -0.0283 139 LEU   A O     
862  C  CB    . LEU   A 139 ? 0.5921 0.6061 0.6769 -0.0047 0.0127  -0.0152 139 LEU   A CB    
863  C  CG    . LEU   A 139 ? 0.6061 0.6129 0.6938 -0.0029 0.0158  -0.012  139 LEU   A CG    
864  C  CD1   . LEU   A 139 ? 0.6166 0.6245 0.6993 0       0.0176  -0.0075 139 LEU   A CD1   
865  C  CD2   . LEU   A 139 ? 0.6018 0.6015 0.6902 -0.0015 0.0162  -0.016  139 LEU   A CD2   
866  N  N     . ALA   A 140 ? 0.596  0.6204 0.6778 -0.0119 0.0025  -0.0193 140 ALA   A N     
867  C  CA    . ALA   A 140 ? 0.6009 0.6291 0.6742 -0.0136 -0.0016 -0.0216 140 ALA   A CA    
868  C  C     . ALA   A 140 ? 0.6104 0.6329 0.6793 -0.0181 -0.0073 -0.027  140 ALA   A C     
869  O  O     . ALA   A 140 ? 0.6136 0.6326 0.6691 -0.0184 -0.008  -0.032  140 ALA   A O     
870  C  CB    . ALA   A 140 ? 0.5948 0.6313 0.6736 -0.0146 -0.0038 -0.0159 140 ALA   A CB    
871  N  N     . GLU   A 141 ? 0.6122 0.6328 0.6917 -0.0218 -0.0109 -0.0263 141 GLU   A N     
872  C  CA    . GLU   A 141 ? 0.6345 0.6486 0.7098 -0.0273 -0.0178 -0.0313 141 GLU   A CA    
873  C  C     . GLU   A 141 ? 0.6391 0.6412 0.7064 -0.0266 -0.0146 -0.0383 141 GLU   A C     
874  O  O     . GLU   A 141 ? 0.6453 0.6395 0.6991 -0.0296 -0.0178 -0.0445 141 GLU   A O     
875  C  CB    . GLU   A 141 ? 0.6814 0.6988 0.7735 -0.0323 -0.0238 -0.0272 141 GLU   A CB    
876  C  CG    . GLU   A 141 ? 0.7925 0.8212 0.8925 -0.0328 -0.0273 -0.0206 141 GLU   A CG    
877  C  CD    . GLU   A 141 ? 0.9328 0.9632 1.0177 -0.034  -0.0328 -0.0222 141 GLU   A CD    
878  O  OE1   . GLU   A 141 ? 0.9802 1.0043 1.055  -0.039  -0.0407 -0.0267 141 GLU   A OE1   
879  O  OE2   . GLU   A 141 ? 0.9448 0.9812 1.0263 -0.0301 -0.0292 -0.019  141 GLU   A OE2   
880  N  N     . GLY   A 142 ? 0.6297 0.6293 0.7037 -0.0227 -0.0079 -0.0371 142 GLY   A N     
881  C  CA    . GLY   A 142 ? 0.638  0.6263 0.7064 -0.021  -0.0039 -0.0429 142 GLY   A CA    
882  C  C     . GLY   A 142 ? 0.647  0.6331 0.7018 -0.0169 0.0007  -0.047  142 GLY   A C     
883  O  O     . GLY   A 142 ? 0.6581 0.6336 0.7052 -0.0163 0.0037  -0.0533 142 GLY   A O     
884  N  N     . LEU   A 143 ? 0.6424 0.6379 0.6947 -0.0141 0.0023  -0.0435 143 LEU   A N     
885  C  CA    . LEU   A 143 ? 0.6533 0.648  0.695  -0.0103 0.0075  -0.0465 143 LEU   A CA    
886  C  C     . LEU   A 143 ? 0.6579 0.6514 0.6839 -0.0136 0.0046  -0.0501 143 LEU   A C     
887  O  O     . LEU   A 143 ? 0.6521 0.6417 0.6675 -0.0111 0.0101  -0.054  143 LEU   A O     
888  C  CB    . LEU   A 143 ? 0.6493 0.654  0.6975 -0.0055 0.0112  -0.0404 143 LEU   A CB    
889  C  CG    . LEU   A 143 ? 0.6664 0.6695 0.7243 -0.001  0.0157  -0.038  143 LEU   A CG    
890  C  CD1   . LEU   A 143 ? 0.6623 0.674  0.726  0.0013  0.0162  -0.031  143 LEU   A CD1   
891  C  CD2   . LEU   A 143 ? 0.6805 0.6783 0.7355 0.0029  0.0216  -0.0422 143 LEU   A CD2   
892  N  N     . ARG   A 144 ? 0.6639 0.6606 0.6889 -0.0188 -0.0037 -0.0482 144 ARG   A N     
893  C  CA    . ARG   A 144 ? 0.6893 0.6854 0.6989 -0.0222 -0.0081 -0.0499 144 ARG   A CA    
894  C  C     . ARG   A 144 ? 0.7152 0.6964 0.704  -0.0246 -0.0069 -0.0585 144 ARG   A C     
895  O  O     . ARG   A 144 ? 0.7202 0.6994 0.6942 -0.0234 -0.003  -0.0605 144 ARG   A O     
896  C  CB    . ARG   A 144 ? 0.7057 0.7073 0.7214 -0.0277 -0.0187 -0.0455 144 ARG   A CB    
897  C  CG    . ARG   A 144 ? 0.7551 0.7613 0.7604 -0.0297 -0.0233 -0.0431 144 ARG   A CG    
898  C  CD    . ARG   A 144 ? 0.8233 0.8333 0.8357 -0.0356 -0.0352 -0.039  144 ARG   A CD    
899  N  NE    . ARG   A 144 ? 0.9178 0.9158 0.9183 -0.0424 -0.0432 -0.0447 144 ARG   A NE    
900  C  CZ    . ARG   A 144 ? 0.9492 0.943  0.9598 -0.0462 -0.0476 -0.0463 144 ARG   A CZ    
901  N  NH1   . ARG   A 144 ? 0.9316 0.9323 0.9644 -0.0436 -0.0439 -0.0422 144 ARG   A NH1   
902  N  NH2   . ARG   A 144 ? 0.9502 0.9316 0.9473 -0.053  -0.0555 -0.0519 144 ARG   A NH2   
903  N  N     . GLU   A 145 ? 0.725  0.6947 0.7116 -0.0283 -0.0095 -0.0637 145 GLU   A N     
904  C  CA    . GLU   A 145 ? 0.7494 0.7021 0.714  -0.0308 -0.0075 -0.0726 145 GLU   A CA    
905  C  C     . GLU   A 145 ? 0.7512 0.6962 0.7156 -0.0245 0.0051  -0.0772 145 GLU   A C     
906  O  O     . GLU   A 145 ? 0.7604 0.6971 0.7084 -0.0227 0.0125  -0.0821 145 GLU   A O     
907  C  CB    . GLU   A 145 ? 0.7995 0.7409 0.7579 -0.039  -0.0176 -0.0768 145 GLU   A CB    
908  C  CG    . GLU   A 145 ? 0.9117 0.8592 0.8686 -0.0458 -0.0311 -0.0724 145 GLU   A CG    
909  C  CD    . GLU   A 145 ? 1.0579 1.0049 0.9945 -0.0468 -0.0326 -0.0722 145 GLU   A CD    
910  O  OE1   . GLU   A 145 ? 1.0896 1.0223 1.0023 -0.0468 -0.0267 -0.0793 145 GLU   A OE1   
911  O  OE2   . GLU   A 145 ? 1.0945 1.0547 1.039  -0.0474 -0.0388 -0.0648 145 GLU   A OE2   
912  N  N     . SER   A 146 ? 0.7366 0.684  0.7198 -0.0212 0.0079  -0.0751 146 SER   A N     
913  C  CA    . SER   A 146 ? 0.738  0.6786 0.7255 -0.015  0.0187  -0.0782 146 SER   A CA    
914  C  C     . SER   A 146 ? 0.7503 0.6974 0.7383 -0.0081 0.0284  -0.0765 146 SER   A C     
915  O  O     . SER   A 146 ? 0.7579 0.6962 0.7419 -0.0039 0.0383  -0.0811 146 SER   A O     
916  C  CB    . SER   A 146 ? 0.7233 0.6673 0.7314 -0.0129 0.0181  -0.074  146 SER   A CB    
917  O  OG    . SER   A 146 ? 0.7203 0.6804 0.7429 -0.0103 0.0165  -0.0653 146 SER   A OG    
918  N  N     . ARG   A 147 ? 0.7485 0.7104 0.7418 -0.0072 0.0258  -0.0698 147 ARG   A N     
919  C  CA    . ARG   A 147 ? 0.7633 0.7342 0.7587 -0.0022 0.0325  -0.0666 147 ARG   A CA    
920  C  C     . ARG   A 147 ? 0.7869 0.7479 0.7631 -0.002  0.0401  -0.0729 147 ARG   A C     
921  O  O     . ARG   A 147 ? 0.781  0.745  0.7609 0.0033  0.0495  -0.0721 147 ARG   A O     
922  C  CB    . ARG   A 147 ? 0.7813 0.7653 0.7781 -0.0046 0.0254  -0.0601 147 ARG   A CB    
923  C  CG    . ARG   A 147 ? 0.8274 0.8233 0.833  0.0001  0.0298  -0.0545 147 ARG   A CG    
924  C  CD    . ARG   A 147 ? 0.8653 0.8691 0.864  -0.0027 0.0254  -0.0509 147 ARG   A CD    
925  N  NE    . ARG   A 147 ? 0.8857 0.8972 0.8879 0.0014  0.0318  -0.0477 147 ARG   A NE    
926  C  CZ    . ARG   A 147 ? 0.8973 0.9203 0.9105 0.0028  0.03    -0.0409 147 ARG   A CZ    
927  N  NH1   . ARG   A 147 ? 0.8771 0.9046 0.8974 0.0009  0.0231  -0.0367 147 ARG   A NH1   
928  N  NH2   . ARG   A 147 ? 0.8952 0.9244 0.912  0.0059  0.0355  -0.0383 147 ARG   A NH2   
929  N  N     . LYS   A 148 ? 0.8105 0.7596 0.7657 -0.0082 0.0356  -0.0785 148 LYS   A N     
930  C  CA    . LYS   A 148 ? 0.8423 0.779  0.7738 -0.0092 0.0423  -0.0847 148 LYS   A CA    
931  C  C     . LYS   A 148 ? 0.8641 0.784  0.7892 -0.0061 0.0539  -0.0926 148 LYS   A C     
932  O  O     . LYS   A 148 ? 0.8814 0.7906 0.7888 -0.0054 0.0633  -0.0975 148 LYS   A O     
933  C  CB    . LYS   A 148 ? 0.8792 0.8077 0.7881 -0.0179 0.0315  -0.0872 148 LYS   A CB    
934  C  CG    . LYS   A 148 ? 0.922  0.8667 0.8383 -0.0205 0.0205  -0.079  148 LYS   A CG    
935  C  CD    . LYS   A 148 ? 0.9843 0.9218 0.8833 -0.0293 0.0075  -0.0803 148 LYS   A CD    
936  C  CE    . LYS   A 148 ? 1.0145 0.9679 0.9235 -0.0312 -0.0027 -0.0716 148 LYS   A CE    
937  N  NZ    . LYS   A 148 ? 1.0462 0.9936 0.9422 -0.0398 -0.0168 -0.0717 148 LYS   A NZ    
938  N  N     . HIS   A 149 ? 0.8652 0.7814 0.8041 -0.0043 0.0542  -0.0938 149 HIS   A N     
939  C  CA    . HIS   A 149 ? 0.8821 0.7811 0.8163 -0.0012 0.0652  -0.1013 149 HIS   A CA    
940  C  C     . HIS   A 149 ? 0.8676 0.7733 0.8243 0.0083  0.077   -0.0981 149 HIS   A C     
941  O  O     . HIS   A 149 ? 0.8758 0.7688 0.8349 0.0118  0.0858  -0.1029 149 HIS   A O     
942  C  CB    . HIS   A 149 ? 0.9151 0.8024 0.8484 -0.0058 0.0582  -0.1054 149 HIS   A CB    
943  C  CG    . HIS   A 149 ? 0.9901 0.8721 0.9057 -0.0156 0.0448  -0.1075 149 HIS   A CG    
944  N  ND1   . HIS   A 149 ? 1.0421 0.9096 0.9274 -0.0209 0.0447  -0.1139 149 HIS   A ND1   
945  C  CD2   . HIS   A 149 ? 1.0056 0.8957 0.9308 -0.0208 0.0312  -0.1032 149 HIS   A CD2   
946  C  CE1   . HIS   A 149 ? 1.0544 0.922  0.9328 -0.0294 0.0295  -0.113  149 HIS   A CE1   
947  N  NE2   . HIS   A 149 ? 1.0372 0.9188 0.9405 -0.0294 0.0215  -0.1065 149 HIS   A NE2   
948  N  N     . ILE   A 150 ? 0.8462 0.771  0.8197 0.0122  0.0769  -0.0898 150 ILE   A N     
949  C  CA    . ILE   A 150 ? 0.83   0.7629 0.8269 0.0206  0.0858  -0.0854 150 ILE   A CA    
950  C  C     . ILE   A 150 ? 0.8397 0.7758 0.8348 0.0245  0.0974  -0.0851 150 ILE   A C     
951  O  O     . ILE   A 150 ? 0.8494 0.7856 0.8267 0.0206  0.0967  -0.0862 150 ILE   A O     
952  C  CB    . ILE   A 150 ? 0.8054 0.7561 0.8254 0.0221  0.0768  -0.0757 150 ILE   A CB    
953  C  CG1   . ILE   A 150 ? 0.8003 0.7663 0.8189 0.0195  0.0703  -0.0697 150 ILE   A CG1   
954  C  CG2   . ILE   A 150 ? 0.8011 0.7472 0.8242 0.0188  0.0679  -0.0759 150 ILE   A CG2   
955  C  CD1   . ILE   A 150 ? 0.799  0.7801 0.8376 0.0214  0.0637  -0.0607 150 ILE   A CD1   
956  N  N     . GLU   A 151 ? 0.8335 0.7724 0.8484 0.0321  0.1082  -0.083  151 GLU   A N     
957  C  CA    . GLU   A 151 ? 0.8416 0.7839 0.859  0.0362  0.1208  -0.0823 151 GLU   A CA    
958  C  C     . GLU   A 151 ? 0.8372 0.8009 0.8688 0.0367  0.1158  -0.073  151 GLU   A C     
959  O  O     . GLU   A 151 ? 0.8454 0.8115 0.8691 0.0363  0.1222  -0.0729 151 GLU   A O     
960  C  CB    . GLU   A 151 ? 0.8586 0.7952 0.8939 0.0443  0.1352  -0.0835 151 GLU   A CB    
961  C  CG    . GLU   A 151 ? 0.8831 0.8313 0.9495 0.0491  0.1298  -0.0759 151 GLU   A CG    
962  C  CD    . GLU   A 151 ? 0.9226 0.8645 1.009  0.0572  0.1422  -0.0764 151 GLU   A CD    
963  O  OE1   . GLU   A 151 ? 0.919  0.8468 0.9962 0.0599  0.1576  -0.0833 151 GLU   A OE1   
964  O  OE2   . GLU   A 151 ? 0.9319 0.882  1.043  0.0611  0.1367  -0.0695 151 GLU   A OE2   
965  N  N     . ASP   A 152 ? 0.8224 0.8    0.8729 0.0371  0.1049  -0.0654 152 ASP   A N     
966  C  CA    . ASP   A 152 ? 0.8088 0.8046 0.8718 0.0371  0.0996  -0.0569 152 ASP   A CA    
967  C  C     . ASP   A 152 ? 0.803  0.805  0.861  0.0317  0.0847  -0.0534 152 ASP   A C     
968  O  O     . ASP   A 152 ? 0.794  0.7995 0.8647 0.0325  0.0777  -0.0494 152 ASP   A O     
969  C  CB    . ASP   A 152 ? 0.8164 0.823  0.91   0.0435  0.1021  -0.0498 152 ASP   A CB    
970  C  CG    . ASP   A 152 ? 0.8723 0.8965 0.9795 0.0429  0.0953  -0.0408 152 ASP   A CG    
971  O  OD1   . ASP   A 152 ? 0.882  0.9105 0.9765 0.0389  0.0934  -0.0405 152 ASP   A OD1   
972  O  OD2   . ASP   A 152 ? 0.8939 0.9266 1.0238 0.0461  0.0914  -0.034  152 ASP   A OD2   
973  N  N     . GLU   A 153 ? 0.8091 0.8119 0.8489 0.0265  0.0805  -0.0544 153 GLU   A N     
974  C  CA    . GLU   A 153 ? 0.8127 0.8208 0.848  0.0215  0.0678  -0.0512 153 GLU   A CA    
975  C  C     . GLU   A 153 ? 0.7911 0.8137 0.8434 0.0227  0.0619  -0.0425 153 GLU   A C     
976  O  O     . GLU   A 153 ? 0.7867 0.8121 0.8394 0.0198  0.0529  -0.0396 153 GLU   A O     
977  C  CB    . GLU   A 153 ? 0.8691 0.8743 0.8823 0.0161  0.0649  -0.0537 153 GLU   A CB    
978  C  CG    . GLU   A 153 ? 0.9678 0.9625 0.9659 0.0108  0.0575  -0.0585 153 GLU   A CG    
979  C  CD    . GLU   A 153 ? 1.0946 1.0822 1.0684 0.0057  0.0561  -0.0622 153 GLU   A CD    
980  O  OE1   . GLU   A 153 ? 1.1391 1.1158 1.0985 0.0064  0.0653  -0.0678 153 GLU   A OE1   
981  O  OE2   . GLU   A 153 ? 1.1149 1.1069 1.0837 0.0012  0.0461  -0.0593 153 GLU   A OE2   
982  N  N     . LYS   A 154 ? 0.7737 0.8047 0.8403 0.0266  0.0672  -0.0383 154 LYS   A N     
983  C  CA    . LYS   A 154 ? 0.753  0.7961 0.8347 0.0271  0.0611  -0.0302 154 LYS   A CA    
984  C  C     . LYS   A 154 ? 0.7202 0.7625 0.8133 0.0284  0.0548  -0.027  154 LYS   A C     
985  O  O     . LYS   A 154 ? 0.7173 0.7658 0.8153 0.0269  0.0473  -0.0211 154 LYS   A O     
986  C  CB    . LYS   A 154 ? 0.7834 0.8353 0.88   0.0305  0.0675  -0.0263 154 LYS   A CB    
987  C  CG    . LYS   A 154 ? 0.8711 0.9243 0.956  0.0287  0.0738  -0.0282 154 LYS   A CG    
988  C  CD    . LYS   A 154 ? 0.9581 1.0197 1.0607 0.0323  0.0819  -0.0244 154 LYS   A CD    
989  C  CE    . LYS   A 154 ? 1.0375 1.0968 1.1275 0.0314  0.0918  -0.0274 154 LYS   A CE    
990  N  NZ    . LYS   A 154 ? 1.0894 1.1343 1.1647 0.0328  0.1019  -0.0356 154 LYS   A NZ    
991  N  N     . LEU   A 155 ? 0.6939 0.7268 0.7892 0.0307  0.0578  -0.0309 155 LEU   A N     
992  C  CA    . LEU   A 155 ? 0.6791 0.7095 0.783  0.0315  0.0518  -0.0277 155 LEU   A CA    
993  C  C     . LEU   A 155 ? 0.6666 0.6957 0.7592 0.0262  0.0433  -0.027  155 LEU   A C     
994  O  O     . LEU   A 155 ? 0.6648 0.6955 0.7629 0.0257  0.0372  -0.0217 155 LEU   A O     
995  C  CB    . LEU   A 155 ? 0.6842 0.7032 0.791  0.0345  0.0569  -0.0325 155 LEU   A CB    
996  C  CG    . LEU   A 155 ? 0.7022 0.7203 0.8228 0.0406  0.0668  -0.0333 155 LEU   A CG    
997  C  CD1   . LEU   A 155 ? 0.7078 0.7123 0.8281 0.0429  0.0719  -0.0388 155 LEU   A CD1   
998  C  CD2   . LEU   A 155 ? 0.7012 0.73   0.8444 0.0444  0.064   -0.0243 155 LEU   A CD2   
999  N  N     . VAL   A 156 ? 0.6517 0.6774 0.7286 0.0223  0.0432  -0.032  156 VAL   A N     
1000 C  CA    . VAL   A 156 ? 0.6415 0.6667 0.7103 0.0175  0.0361  -0.0313 156 VAL   A CA    
1001 C  C     . VAL   A 156 ? 0.6302 0.6648 0.7008 0.0162  0.0317  -0.0248 156 VAL   A C     
1002 O  O     . VAL   A 156 ? 0.631  0.6656 0.7036 0.0147  0.0269  -0.0211 156 VAL   A O     
1003 C  CB    . VAL   A 156 ? 0.6532 0.6728 0.7066 0.0136  0.0359  -0.0375 156 VAL   A CB    
1004 C  CG1   . VAL   A 156 ? 0.6592 0.6804 0.7087 0.0088  0.0283  -0.0354 156 VAL   A CG1   
1005 C  CG2   . VAL   A 156 ? 0.6567 0.6641 0.7064 0.0142  0.0399  -0.0443 156 VAL   A CG2   
1006 N  N     . ARG   A 157 ? 0.6207 0.6622 0.6911 0.0169  0.0343  -0.0234 157 ARG   A N     
1007 C  CA    . ARG   A 157 ? 0.6187 0.6678 0.6906 0.0155  0.0304  -0.0175 157 ARG   A CA    
1008 C  C     . ARG   A 157 ? 0.613  0.663  0.6954 0.017   0.0268  -0.0118 157 ARG   A C     
1009 O  O     . ARG   A 157 ? 0.6084 0.6579 0.6877 0.0147  0.0222  -0.0082 157 ARG   A O     
1010 C  CB    . ARG   A 157 ? 0.6309 0.6867 0.7023 0.016   0.0342  -0.0168 157 ARG   A CB    
1011 C  CG    . ARG   A 157 ? 0.6734 0.736  0.7476 0.0145  0.0303  -0.0107 157 ARG   A CG    
1012 C  CD    . ARG   A 157 ? 0.7581 0.8217 0.8211 0.0109  0.0277  -0.0103 157 ARG   A CD    
1013 N  NE    . ARG   A 157 ? 0.8383 0.908  0.9001 0.0103  0.03    -0.0084 157 ARG   A NE    
1014 C  CZ    . ARG   A 157 ? 0.9    0.97   0.9543 0.0099  0.0344  -0.0113 157 ARG   A CZ    
1015 N  NH1   . ARG   A 157 ? 0.928  0.9917 0.9733 0.0097  0.0362  -0.0166 157 ARG   A NH1   
1016 N  NH2   . ARG   A 157 ? 0.9041 0.9793 0.9582 0.0093  0.0369  -0.0089 157 ARG   A NH2   
1017 N  N     . TYR   A 158 ? 0.6126 0.6627 0.7068 0.0208  0.0291  -0.0109 158 TYR   A N     
1018 C  CA    . TYR   A 158 ? 0.6324 0.6824 0.7362 0.0221  0.0244  -0.0049 158 TYR   A CA    
1019 C  C     . TYR   A 158 ? 0.6019 0.6436 0.701  0.0207  0.0207  -0.0044 158 TYR   A C     
1020 O  O     . TYR   A 158 ? 0.5996 0.6396 0.6967 0.019   0.0155  0.0007  158 TYR   A O     
1021 C  CB    . TYR   A 158 ? 0.6733 0.7249 0.7934 0.027   0.0276  -0.0038 158 TYR   A CB    
1022 C  CG    . TYR   A 158 ? 0.7438 0.7948 0.874  0.028   0.0208  0.0033  158 TYR   A CG    
1023 C  CD1   . TYR   A 158 ? 0.7809 0.8387 0.9173 0.0268  0.0154  0.0097  158 TYR   A CD1   
1024 C  CD2   . TYR   A 158 ? 0.7809 0.8235 0.9128 0.0294  0.0189  0.004   158 TYR   A CD2   
1025 C  CE1   . TYR   A 158 ? 0.8046 0.8603 0.9472 0.0267  0.0074  0.0167  158 TYR   A CE1   
1026 C  CE2   . TYR   A 158 ? 0.807  0.8475 0.945  0.0297  0.0117  0.0112  158 TYR   A CE2   
1027 C  CZ    . TYR   A 158 ? 0.8311 0.8779 0.9738 0.0282  0.0055  0.0176  158 TYR   A CZ    
1028 O  OH    . TYR   A 158 ? 0.8762 0.9198 1.0233 0.0279  -0.0031 0.0251  158 TYR   A OH    
1029 N  N     . PHE   A 159 ? 0.576  0.6112 0.6725 0.0211  0.0237  -0.0096 159 PHE   A N     
1030 C  CA    . PHE   A 159 ? 0.5546 0.5817 0.6482 0.0196  0.0212  -0.0092 159 PHE   A CA    
1031 C  C     . PHE   A 159 ? 0.544  0.5712 0.6283 0.0154  0.0183  -0.0075 159 PHE   A C     
1032 O  O     . PHE   A 159 ? 0.5472 0.5698 0.63   0.0142  0.0157  -0.0033 159 PHE   A O     
1033 C  CB    . PHE   A 159 ? 0.5417 0.5616 0.6346 0.0201  0.0248  -0.0157 159 PHE   A CB    
1034 C  CG    . PHE   A 159 ? 0.5388 0.5508 0.6296 0.0177  0.0226  -0.0155 159 PHE   A CG    
1035 C  CD1   . PHE   A 159 ? 0.5466 0.552  0.6434 0.0196  0.0217  -0.0122 159 PHE   A CD1   
1036 C  CD2   . PHE   A 159 ? 0.5439 0.5552 0.6277 0.0135  0.0214  -0.0179 159 PHE   A CD2   
1037 C  CE1   . PHE   A 159 ? 0.5573 0.555  0.6523 0.0171  0.0206  -0.0116 159 PHE   A CE1   
1038 C  CE2   . PHE   A 159 ? 0.5535 0.5583 0.6379 0.0111  0.0201  -0.0172 159 PHE   A CE2   
1039 C  CZ    . PHE   A 159 ? 0.5528 0.5506 0.6423 0.0129  0.0202  -0.0142 159 PHE   A CZ    
1040 N  N     . LEU   A 160 ? 0.5257 0.557  0.6037 0.0131  0.0193  -0.0106 160 LEU   A N     
1041 C  CA    . LEU   A 160 ? 0.5212 0.553  0.5932 0.0097  0.0173  -0.0087 160 LEU   A CA    
1042 C  C     . LEU   A 160 ? 0.5221 0.556  0.592  0.0092  0.0153  -0.003  160 LEU   A C     
1043 O  O     . LEU   A 160 ? 0.5271 0.5559 0.5938 0.0077  0.0143  0.0002  160 LEU   A O     
1044 C  CB    . LEU   A 160 ? 0.519  0.5547 0.5857 0.0076  0.0177  -0.0125 160 LEU   A CB    
1045 C  CG    . LEU   A 160 ? 0.5411 0.5719 0.6069 0.0061  0.0176  -0.0176 160 LEU   A CG    
1046 C  CD1   . LEU   A 160 ? 0.5472 0.5809 0.6057 0.0037  0.0167  -0.021  160 LEU   A CD1   
1047 C  CD2   . LEU   A 160 ? 0.5415 0.5678 0.6106 0.0038  0.0158  -0.0157 160 LEU   A CD2   
1048 N  N     . ASP   A 161 ? 0.5086 0.5482 0.5804 0.0105  0.0151  -0.0017 161 ASP   A N     
1049 C  CA    . ASP   A 161 ? 0.5152 0.5555 0.5845 0.0093  0.0121  0.0035  161 ASP   A CA    
1050 C  C     . ASP   A 161 ? 0.5262 0.5586 0.5951 0.0093  0.0089  0.0078  161 ASP   A C     
1051 O  O     . ASP   A 161 ? 0.5392 0.5657 0.5995 0.0069  0.0075  0.0109  161 ASP   A O     
1052 C  CB    . ASP   A 161 ? 0.5215 0.5697 0.5961 0.0104  0.0119  0.0045  161 ASP   A CB    
1053 C  CG    . ASP   A 161 ? 0.5655 0.6201 0.6366 0.0094  0.0147  0.0022  161 ASP   A CG    
1054 O  OD1   . ASP   A 161 ? 0.5722 0.6254 0.636  0.0075  0.0153  0.0007  161 ASP   A OD1   
1055 O  OD2   . ASP   A 161 ? 0.5893 0.6501 0.6656 0.0105  0.0163  0.0023  161 ASP   A OD2   
1056 N  N     . LYS   A 162 ? 0.5212 0.5519 0.5983 0.0121  0.0081  0.0081  162 LYS   A N     
1057 C  CA    . LYS   A 162 ? 0.535  0.5573 0.6114 0.0122  0.0043  0.0127  162 LYS   A CA    
1058 C  C     . LYS   A 162 ? 0.5319 0.5443 0.6001 0.0103  0.0061  0.0127  162 LYS   A C     
1059 O  O     . LYS   A 162 ? 0.5522 0.5564 0.611  0.0081  0.0041  0.0169  162 LYS   A O     
1060 C  CB    . LYS   A 162 ? 0.5787 0.6016 0.6681 0.0161  0.0037  0.0133  162 LYS   A CB    
1061 C  CG    . LYS   A 162 ? 0.6771 0.7036 0.7741 0.017   -0.0021 0.0191  162 LYS   A CG    
1062 C  CD    . LYS   A 162 ? 0.7737 0.7906 0.8602 0.014   -0.009  0.0255  162 LYS   A CD    
1063 C  CE    . LYS   A 162 ? 0.8431 0.8621 0.9389 0.0146  -0.017  0.0321  162 LYS   A CE    
1064 N  NZ    . LYS   A 162 ? 0.8886 0.9018 0.9705 0.0097  -0.0243 0.0371  162 LYS   A NZ    
1065 N  N     . THR   A 163 ? 0.5067 0.5191 0.5779 0.0107  0.01    0.008   163 THR   A N     
1066 C  CA    . THR   A 163 ? 0.4972 0.5016 0.5647 0.0088  0.0123  0.008   163 THR   A CA    
1067 C  C     . THR   A 163 ? 0.5011 0.5041 0.5602 0.0058  0.0141  0.0095  163 THR   A C     
1068 O  O     . THR   A 163 ? 0.5089 0.5025 0.5616 0.0042  0.0156  0.0129  163 THR   A O     
1069 C  CB    . THR   A 163 ? 0.4994 0.5049 0.5735 0.0092  0.0149  0.0023  163 THR   A CB    
1070 O  OG1   . THR   A 163 ? 0.5142 0.5192 0.5954 0.0125  0.0147  0.0006  163 THR   A OG1   
1071 C  CG2   . THR   A 163 ? 0.4891 0.4873 0.5628 0.007   0.017   0.0027  163 THR   A CG2   
1072 N  N     . LEU   A 164 ? 0.4936 0.5047 0.5525 0.005   0.0149  0.0073  164 LEU   A N     
1073 C  CA    . LEU   A 164 ? 0.5081 0.5185 0.5615 0.0027  0.0174  0.0088  164 LEU   A CA    
1074 C  C     . LEU   A 164 ? 0.5232 0.5272 0.5657 0.0015  0.0168  0.0133  164 LEU   A C     
1075 O  O     . LEU   A 164 ? 0.5455 0.5416 0.5813 -0.0002 0.0205  0.0155  164 LEU   A O     
1076 C  CB    . LEU   A 164 ? 0.5134 0.5337 0.5698 0.0023  0.0176  0.0058  164 LEU   A CB    
1077 C  CG    . LEU   A 164 ? 0.5375 0.5616 0.6012 0.0022  0.0174  0.0013  164 LEU   A CG    
1078 C  CD1   . LEU   A 164 ? 0.545  0.5772 0.6087 0.0013  0.0165  -0.0008 164 LEU   A CD1   
1079 C  CD2   . LEU   A 164 ? 0.5463 0.5652 0.6144 0.0006  0.0193  0.0019  164 LEU   A CD2   
1080 N  N     . THR   A 165 ? 0.5131 0.5192 0.5537 0.002   0.0124  0.0147  165 THR   A N     
1081 C  CA    . THR   A 165 ? 0.519  0.5174 0.5476 -0.0001 0.0101  0.0188  165 THR   A CA    
1082 C  C     . THR   A 165 ? 0.5301 0.5148 0.5504 -0.0009 0.0089  0.0225  165 THR   A C     
1083 O  O     . THR   A 165 ? 0.5362 0.5093 0.5421 -0.0035 0.0106  0.0251  165 THR   A O     
1084 C  CB    . THR   A 165 ? 0.5218 0.5272 0.553  0       0.0047  0.0197  165 THR   A CB    
1085 O  OG1   . THR   A 165 ? 0.5187 0.5274 0.5599 0.0024  0.001   0.0203  165 THR   A OG1   
1086 C  CG2   . THR   A 165 ? 0.5221 0.539  0.5584 0.0004  0.0068  0.0167  165 THR   A CG2   
1087 N  N     . SER   A 166 ? 0.5297 0.5141 0.5577 0.0012  0.0068  0.0227  166 SER   A N     
1088 C  CA    . SER   A 166 ? 0.5479 0.5186 0.568  0.0004  0.0058  0.0266  166 SER   A CA    
1089 C  C     . SER   A 166 ? 0.5553 0.5177 0.5697 -0.001  0.0136  0.0262  166 SER   A C     
1090 O  O     . SER   A 166 ? 0.5755 0.5237 0.575  -0.0033 0.0154  0.0297  166 SER   A O     
1091 C  CB    . SER   A 166 ? 0.5671 0.5395 0.599  0.0034  0.0032  0.0267  166 SER   A CB    
1092 O  OG    . SER   A 166 ? 0.6158 0.5959 0.6558 0.0052  -0.0031 0.0279  166 SER   A OG    
1093 N  N     . ARG   A 167 ? 0.5368 0.5076 0.5626 -0.0001 0.0183  0.022   167 ARG   A N     
1094 C  CA    . ARG   A 167 ? 0.5346 0.5003 0.5603 -0.0014 0.0258  0.022   167 ARG   A CA    
1095 C  C     . ARG   A 167 ? 0.5477 0.5071 0.5611 -0.0035 0.0303  0.024   167 ARG   A C     
1096 O  O     . ARG   A 167 ? 0.559  0.506  0.5643 -0.0049 0.0367  0.0265  167 ARG   A O     
1097 C  CB    . ARG   A 167 ? 0.5196 0.4969 0.5609 -0.0007 0.0274  0.0176  167 ARG   A CB    
1098 C  CG    . ARG   A 167 ? 0.5313 0.5053 0.5771 -0.0023 0.0344  0.0184  167 ARG   A CG    
1099 C  CD    . ARG   A 167 ? 0.5378 0.5227 0.5992 -0.0024 0.0335  0.0145  167 ARG   A CD    
1100 N  NE    . ARG   A 167 ? 0.5493 0.5333 0.619  -0.0042 0.0394  0.0161  167 ARG   A NE    
1101 C  CZ    . ARG   A 167 ? 0.542  0.5305 0.6151 -0.0046 0.0425  0.0173  167 ARG   A CZ    
1102 N  NH1   . ARG   A 167 ? 0.521  0.5145 0.588  -0.0038 0.0402  0.0167  167 ARG   A NH1   
1103 N  NH2   . ARG   A 167 ? 0.5334 0.522  0.6181 -0.0059 0.0479  0.0193  167 ARG   A NH2   
1104 N  N     . LEU   A 168 ? 0.544  0.5102 0.5553 -0.0036 0.0279  0.0229  168 LEU   A N     
1105 C  CA    . LEU   A 168 ? 0.5485 0.5075 0.5477 -0.0054 0.0323  0.0245  168 LEU   A CA    
1106 C  C     . LEU   A 168 ? 0.5724 0.5133 0.5507 -0.0078 0.0317  0.0282  168 LEU   A C     
1107 O  O     . LEU   A 168 ? 0.5845 0.512  0.551  -0.0093 0.0393  0.0298  168 LEU   A O     
1108 C  CB    . LEU   A 168 ? 0.537  0.5061 0.5377 -0.0054 0.0289  0.0228  168 LEU   A CB    
1109 C  CG    . LEU   A 168 ? 0.5519 0.5121 0.5392 -0.0073 0.0333  0.0242  168 LEU   A CG    
1110 C  CD1   . LEU   A 168 ? 0.555  0.514  0.5481 -0.0067 0.043   0.0242  168 LEU   A CD1   
1111 C  CD2   . LEU   A 168 ? 0.5449 0.5136 0.5323 -0.0078 0.0286  0.0232  168 LEU   A CD2   
1112 N  N     . GLY   A 169 ? 0.5796 0.5197 0.5539 -0.0082 0.0227  0.0297  169 GLY   A N     
1113 C  CA    . GLY   A 169 ? 0.5982 0.521  0.5519 -0.011  0.019   0.0339  169 GLY   A CA    
1114 C  C     . GLY   A 169 ? 0.6212 0.5289 0.5661 -0.0116 0.0245  0.0364  169 GLY   A C     
1115 O  O     . GLY   A 169 ? 0.6436 0.5324 0.5666 -0.0146 0.0283  0.039   169 GLY   A O     
1116 N  N     . ILE   A 170 ? 0.6122 0.5267 0.573  -0.0091 0.0261  0.0355  170 ILE   A N     
1117 C  CA    . ILE   A 170 ? 0.6271 0.5288 0.5831 -0.0096 0.0319  0.0379  170 ILE   A CA    
1118 C  C     . ILE   A 170 ? 0.643  0.5375 0.595  -0.0106 0.0448  0.0375  170 ILE   A C     
1119 O  O     . ILE   A 170 ? 0.6664 0.5421 0.6007 -0.0127 0.0512  0.0407  170 ILE   A O     
1120 C  CB    . ILE   A 170 ? 0.6164 0.5281 0.5928 -0.0068 0.03    0.0364  170 ILE   A CB    
1121 C  CG1   . ILE   A 170 ? 0.6227 0.5345 0.5997 -0.0056 0.0194  0.0388  170 ILE   A CG1   
1122 C  CG2   . ILE   A 170 ? 0.6145 0.5171 0.5924 -0.0073 0.0389  0.0377  170 ILE   A CG2   
1123 C  CD1   . ILE   A 170 ? 0.6263 0.5492 0.6237 -0.0024 0.0176  0.0362  170 ILE   A CD1   
1124 N  N     . ARG   A 171 ? 0.626  0.5347 0.5944 -0.0092 0.0488  0.0341  171 ARG   A N     
1125 C  CA    . ARG   A 171 ? 0.6327 0.5368 0.6024 -0.0096 0.061   0.0343  171 ARG   A CA    
1126 C  C     . ARG   A 171 ? 0.6704 0.5583 0.6166 -0.0117 0.0661  0.0359  171 ARG   A C     
1127 O  O     . ARG   A 171 ? 0.6966 0.5705 0.6344 -0.0126 0.0778  0.0378  171 ARG   A O     
1128 C  CB    . ARG   A 171 ? 0.6106 0.5339 0.6041 -0.0077 0.0622  0.0312  171 ARG   A CB    
1129 C  CG    . ARG   A 171 ? 0.5979 0.5322 0.6115 -0.0066 0.0594  0.0296  171 ARG   A CG    
1130 C  CD    . ARG   A 171 ? 0.5964 0.5474 0.6312 -0.0057 0.0595  0.027   171 ARG   A CD    
1131 N  NE    . ARG   A 171 ? 0.6045 0.5527 0.6472 -0.0062 0.07    0.0293  171 ARG   A NE    
1132 C  CZ    . ARG   A 171 ? 0.6083 0.5563 0.6652 -0.0069 0.0752  0.0307  171 ARG   A CZ    
1133 N  NH1   . ARG   A 171 ? 0.5769 0.5265 0.6401 -0.0075 0.0706  0.0295  171 ARG   A NH1   
1134 N  NH2   . ARG   A 171 ? 0.5954 0.5413 0.6614 -0.0071 0.0856  0.0336  171 ARG   A NH2   
1135 N  N     . MET   A 172 ? 0.6748 0.5629 0.6097 -0.0128 0.0579  0.0352  172 MET   A N     
1136 C  CA    . MET   A 172 ? 0.6975 0.5682 0.6072 -0.0157 0.0611  0.0363  172 MET   A CA    
1137 C  C     . MET   A 172 ? 0.7256 0.5718 0.6087 -0.0188 0.0622  0.0399  172 MET   A C     
1138 O  O     . MET   A 172 ? 0.7453 0.5719 0.6085 -0.0208 0.0726  0.0409  172 MET   A O     
1139 C  CB    . MET   A 172 ? 0.694  0.5714 0.5996 -0.0169 0.0501  0.0349  172 MET   A CB    
1140 C  CG    . MET   A 172 ? 0.712  0.6066 0.6348 -0.0148 0.0515  0.0319  172 MET   A CG    
1141 S  SD    . MET   A 172 ? 0.7477 0.6524 0.6695 -0.0163 0.0384  0.0308  172 MET   A SD    
1142 C  CE    . MET   A 172 ? 0.7707 0.6525 0.663  -0.0207 0.0415  0.0318  172 MET   A CE    
1143 N  N     . LEU   A 173 ? 0.7226 0.569  0.6045 -0.0192 0.0517  0.0421  173 LEU   A N     
1144 C  CA    . LEU   A 173 ? 0.7508 0.5741 0.6075 -0.0223 0.0511  0.0464  173 LEU   A CA    
1145 C  C     . LEU   A 173 ? 0.7465 0.5581 0.6014 -0.0218 0.0659  0.0478  173 LEU   A C     
1146 O  O     . LEU   A 173 ? 0.7689 0.5561 0.5967 -0.0249 0.0732  0.0503  173 LEU   A O     
1147 C  CB    . LEU   A 173 ? 0.7653 0.5935 0.627  -0.0219 0.0373  0.0492  173 LEU   A CB    
1148 C  CG    . LEU   A 173 ? 0.8181 0.6523 0.6775 -0.0233 0.0218  0.05    173 LEU   A CG    
1149 C  CD1   . LEU   A 173 ? 0.8286 0.6654 0.6946 -0.0224 0.0101  0.054   173 LEU   A CD1   
1150 C  CD2   . LEU   A 173 ? 0.8574 0.6705 0.6845 -0.0288 0.0193  0.0517  173 LEU   A CD2   
1151 N  N     . ALA   A 174 ? 0.719  0.547  0.6021 -0.0185 0.0704  0.0464  174 ALA   A N     
1152 C  CA    . ALA   A 174 ? 0.7144 0.5346 0.6019 -0.0181 0.0841  0.048   174 ALA   A CA    
1153 C  C     . ALA   A 174 ? 0.7263 0.538  0.6093 -0.0183 0.1     0.0474  174 ALA   A C     
1154 O  O     . ALA   A 174 ? 0.7424 0.5342 0.6101 -0.0198 0.1125  0.0502  174 ALA   A O     
1155 C  CB    . ALA   A 174 ? 0.6852 0.5263 0.6056 -0.0151 0.0827  0.0464  174 ALA   A CB    
1156 N  N     . THR   A 175 ? 0.7189 0.5449 0.6151 -0.0167 0.1002  0.0442  175 THR   A N     
1157 C  CA    . THR   A 175 ? 0.7309 0.5506 0.6267 -0.0161 0.1151  0.0438  175 THR   A CA    
1158 C  C     . THR   A 175 ? 0.7531 0.5453 0.6114 -0.0194 0.1204  0.0447  175 THR   A C     
1159 O  O     . THR   A 175 ? 0.7645 0.539  0.6118 -0.0198 0.1366  0.046   175 THR   A O     
1160 C  CB    . THR   A 175 ? 0.7431 0.5863 0.6643 -0.0133 0.1121  0.0408  175 THR   A CB    
1161 O  OG1   . THR   A 175 ? 0.7391 0.6037 0.691  -0.0112 0.1076  0.0401  175 THR   A OG1   
1162 C  CG2   . THR   A 175 ? 0.7555 0.5941 0.6808 -0.012  0.127   0.041   175 THR   A CG2   
1163 N  N     . HIS   A 176 ? 0.7594 0.5466 0.5977 -0.022  0.1069  0.044   176 HIS   A N     
1164 C  CA    . HIS   A 176 ? 0.7853 0.5452 0.5853 -0.0264 0.1085  0.0446  176 HIS   A CA    
1165 C  C     . HIS   A 176 ? 0.8189 0.5521 0.5932 -0.029  0.1166  0.0484  176 HIS   A C     
1166 O  O     . HIS   A 176 ? 0.8421 0.5511 0.5924 -0.0309 0.1309  0.0486  176 HIS   A O     
1167 C  CB    . HIS   A 176 ? 0.7914 0.5541 0.5798 -0.0292 0.0894  0.0442  176 HIS   A CB    
1168 C  CG    . HIS   A 176 ? 0.8472 0.5816 0.5954 -0.0348 0.0881  0.0448  176 HIS   A CG    
1169 N  ND1   . HIS   A 176 ? 0.8805 0.6051 0.616  -0.0362 0.0954  0.0418  176 HIS   A ND1   
1170 C  CD2   . HIS   A 176 ? 0.8772 0.5904 0.5949 -0.0397 0.0797  0.048   176 HIS   A CD2   
1171 C  CE1   . HIS   A 176 ? 0.9043 0.6012 0.6008 -0.0421 0.0915  0.0428  176 HIS   A CE1   
1172 N  NE2   . HIS   A 176 ? 0.9103 0.5996 0.5946 -0.0446 0.0815  0.0468  176 HIS   A NE2   
1173 N  N     . HIS   A 177 ? 0.8164 0.553  0.5959 -0.029  0.1091  0.0513  177 HIS   A N     
1174 C  CA    . HIS   A 177 ? 0.84   0.5513 0.5953 -0.0316 0.1163  0.0555  177 HIS   A CA    
1175 C  C     . HIS   A 177 ? 0.8497 0.5521 0.6104 -0.0299 0.1393  0.056   177 HIS   A C     
1176 O  O     . HIS   A 177 ? 0.8689 0.5419 0.5981 -0.0328 0.1519  0.0578  177 HIS   A O     
1177 C  CB    . HIS   A 177 ? 0.8435 0.5631 0.6097 -0.0309 0.1048  0.0587  177 HIS   A CB    
1178 C  CG    . HIS   A 177 ? 0.8985 0.5931 0.6424 -0.0333 0.1129  0.0636  177 HIS   A CG    
1179 N  ND1   . HIS   A 177 ? 0.9501 0.6143 0.6509 -0.0385 0.1103  0.0667  177 HIS   A ND1   
1180 C  CD2   . HIS   A 177 ? 0.9114 0.6059 0.6693 -0.0316 0.1243  0.0658  177 HIS   A CD2   
1181 C  CE1   . HIS   A 177 ? 0.9645 0.6109 0.6535 -0.0395 0.1205  0.0709  177 HIS   A CE1   
1182 N  NE2   . HIS   A 177 ? 0.9494 0.6134 0.6728 -0.0354 0.1294  0.0706  177 HIS   A NE2   
1183 N  N     . LEU   A 178 ? 0.8268 0.5539 0.6271 -0.0255 0.1449  0.0547  178 LEU   A N     
1184 C  CA    . LEU   A 178 ? 0.8247 0.5475 0.6377 -0.0236 0.166   0.0559  178 LEU   A CA    
1185 C  C     . LEU   A 178 ? 0.8422 0.5488 0.6382 -0.0239 0.1803  0.0542  178 LEU   A C     
1186 O  O     . LEU   A 178 ? 0.8623 0.5458 0.6418 -0.0248 0.1987  0.0563  178 LEU   A O     
1187 C  CB    . LEU   A 178 ? 0.7928 0.5471 0.6531 -0.0195 0.1658  0.0548  178 LEU   A CB    
1188 C  CG    . LEU   A 178 ? 0.7837 0.5544 0.6646 -0.019  0.154   0.0556  178 LEU   A CG    
1189 C  CD1   . LEU   A 178 ? 0.7583 0.5566 0.6816 -0.0159 0.1541  0.0541  178 LEU   A CD1   
1190 C  CD2   . LEU   A 178 ? 0.7978 0.5494 0.6653 -0.021  0.1611  0.0601  178 LEU   A CD2   
1191 N  N     . ALA   A 179 ? 0.8362 0.5531 0.6348 -0.0232 0.1726  0.0506  179 ALA   A N     
1192 C  CA    . ALA   A 179 ? 0.8555 0.5578 0.6396 -0.0232 0.1853  0.0486  179 ALA   A CA    
1193 C  C     . ALA   A 179 ? 0.9134 0.5786 0.6467 -0.0284 0.1893  0.0487  179 ALA   A C     
1194 O  O     . ALA   A 179 ? 0.933  0.5788 0.6498 -0.0286 0.2051  0.0474  179 ALA   A O     
1195 C  CB    . ALA   A 179 ? 0.8368 0.5603 0.638  -0.0213 0.175   0.0451  179 ALA   A CB    
1196 N  N     . LEU   A 180 ? 0.9433 0.5967 0.651  -0.0326 0.1758  0.0505  180 LEU   A N     
1197 C  CA    . LEU   A 180 ? 0.9922 0.6075 0.6489 -0.0384 0.1789  0.0515  180 LEU   A CA    
1198 C  C     . LEU   A 180 ? 1.0472 0.6373 0.6895 -0.0384 0.2034  0.0541  180 LEU   A C     
1199 O  O     . LEU   A 180 ? 1.0854 0.6403 0.6845 -0.0426 0.2129  0.0541  180 LEU   A O     
1200 C  CB    . LEU   A 180 ? 0.9908 0.6012 0.6276 -0.0428 0.1576  0.0542  180 LEU   A CB    
1201 C  CG    . LEU   A 180 ? 0.9906 0.6158 0.6294 -0.0446 0.1346  0.0522  180 LEU   A CG    
1202 C  CD1   . LEU   A 180 ? 0.9993 0.6187 0.6213 -0.0486 0.1152  0.0563  180 LEU   A CD1   
1203 C  CD2   . LEU   A 180 ? 1.008  0.6154 0.6194 -0.0482 0.1364  0.0487  180 LEU   A CD2   
1204 N  N     . HIS   A 181 ? 1.0499 0.6569 0.7277 -0.034  0.2138  0.0565  181 HIS   A N     
1205 C  CA    . HIS   A 181 ? 1.09   0.677  0.7619 -0.0334 0.2384  0.0595  181 HIS   A CA    
1206 C  C     . HIS   A 181 ? 1.1248 0.71   0.8106 -0.0297 0.2607  0.0575  181 HIS   A C     
1207 O  O     . HIS   A 181 ? 1.1409 0.7069 0.8202 -0.029  0.2839  0.0598  181 HIS   A O     
1208 C  CB    . HIS   A 181 ? 1.0751 0.6807 0.7806 -0.031  0.2392  0.0634  181 HIS   A CB    
1209 C  CG    . HIS   A 181 ? 1.0953 0.6987 0.7872 -0.0341 0.2214  0.0662  181 HIS   A CG    
1210 N  ND1   . HIS   A 181 ? 1.1268 0.7071 0.7973 -0.0368 0.2298  0.071   181 HIS   A ND1   
1211 C  CD2   . HIS   A 181 ? 1.0974 0.7186 0.7953 -0.0347 0.1967  0.0653  181 HIS   A CD2   
1212 C  CE1   . HIS   A 181 ? 1.1323 0.7173 0.7971 -0.0387 0.2092  0.073   181 HIS   A CE1   
1213 N  NE2   . HIS   A 181 ? 1.1183 0.7276 0.7997 -0.0374 0.1893  0.0697  181 HIS   A NE2   
1214 N  N     . GLU   A 182 ? 1.1335 0.7388 0.8399 -0.0269 0.2545  0.0538  182 GLU   A N     
1215 C  CA    . GLU   A 182 ? 1.1584 0.763  0.8795 -0.023  0.2737  0.0524  182 GLU   A CA    
1216 C  C     . GLU   A 182 ? 1.2106 0.783  0.8866 -0.0263 0.2797  0.0487  182 GLU   A C     
1217 O  O     . GLU   A 182 ? 1.2208 0.7814 0.8633 -0.0315 0.2628  0.0466  182 GLU   A O     
1218 C  CB    . GLU   A 182 ? 1.1615 0.8047 0.9294 -0.0183 0.2633  0.0509  182 GLU   A CB    
1219 C  CG    . GLU   A 182 ? 1.2109 0.8855 1.0257 -0.015  0.2592  0.0539  182 GLU   A CG    
1220 C  CD    . GLU   A 182 ? 1.2966 1.0068 1.1445 -0.0127 0.2393  0.0519  182 GLU   A CD    
1221 O  OE1   . GLU   A 182 ? 1.3171 1.0319 1.1647 -0.0117 0.2356  0.0491  182 GLU   A OE1   
1222 O  OE2   . GLU   A 182 ? 1.3166 1.0487 1.1893 -0.0123 0.2277  0.0532  182 GLU   A OE2   
1223 N  N     . ASP   A 183 ? 1.239  0.797  0.9156 -0.0234 0.3038  0.048   183 ASP   A N     
1224 C  CA    . ASP   A 183 ? 1.2894 0.816  0.9258 -0.0261 0.3122  0.044   183 ASP   A CA    
1225 C  C     . ASP   A 183 ? 1.2839 0.8303 0.9536 -0.0206 0.3165  0.0419  183 ASP   A C     
1226 O  O     . ASP   A 183 ? 1.2947 0.8307 0.9732 -0.0166 0.3406  0.0423  183 ASP   A O     
1227 C  CB    . ASP   A 183 ? 1.3579 0.843  0.9593 -0.0275 0.3402  0.0449  183 ASP   A CB    
1228 C  CG    . ASP   A 183 ? 1.4825 0.9289 1.0333 -0.0317 0.3483  0.04    183 ASP   A CG    
1229 O  OD1   . ASP   A 183 ? 1.5082 0.9567 1.0435 -0.0353 0.3282  0.0363  183 ASP   A OD1   
1230 O  OD2   . ASP   A 183 ? 1.5379 0.951  1.0643 -0.0316 0.3751  0.0399  183 ASP   A OD2   
1231 N  N     . LYS   A 184 ? 1.265  0.8407 0.9558 -0.0201 0.2936  0.0403  184 LYS   A N     
1232 C  CA    . LYS   A 184 ? 1.2536 0.8506 0.9767 -0.0153 0.2942  0.039   184 LYS   A CA    
1233 C  C     . LYS   A 184 ? 1.2739 0.851  0.9624 -0.0189 0.2895  0.0341  184 LYS   A C     
1234 O  O     . LYS   A 184 ? 1.2905 0.8636 0.9531 -0.0246 0.2692  0.0319  184 LYS   A O     
1235 C  CB    . LYS   A 184 ? 1.2545 0.8944 1.0193 -0.013  0.2717  0.0401  184 LYS   A CB    
1236 C  CG    . LYS   A 184 ? 1.2881 0.9574 1.1071 -0.0062 0.2795  0.0435  184 LYS   A CG    
1237 C  CD    . LYS   A 184 ? 1.3311 1.0383 1.1837 -0.0046 0.257   0.0433  184 LYS   A CD    
1238 C  CE    . LYS   A 184 ? 1.3819 1.1015 1.2313 -0.008  0.2363  0.0431  184 LYS   A CE    
1239 N  NZ    . LYS   A 184 ? 1.3876 1.1432 1.2722 -0.0059 0.218   0.0429  184 LYS   A NZ    
1240 N  N     . PRO   A 185 ? 1.2645 0.8298 0.9548 -0.0156 0.3074  0.0325  185 PRO   A N     
1241 C  CA    . PRO   A 185 ? 1.265  0.8111 0.9236 -0.0193 0.3031  0.0276  185 PRO   A CA    
1242 C  C     . PRO   A 185 ? 1.2226 0.7985 0.8993 -0.0201 0.2769  0.0262  185 PRO   A C     
1243 O  O     . PRO   A 185 ? 1.1946 0.8069 0.9169 -0.0151 0.2693  0.0288  185 PRO   A O     
1244 C  CB    . PRO   A 185 ? 1.281  0.8166 0.9523 -0.0135 0.3288  0.0273  185 PRO   A CB    
1245 C  CG    . PRO   A 185 ? 1.2879 0.8231 0.9804 -0.0088 0.3507  0.0319  185 PRO   A CG    
1246 C  CD    . PRO   A 185 ? 1.2492 0.8182 0.9721 -0.0085 0.3325  0.0356  185 PRO   A CD    
1247 N  N     . ASP   A 186 ? 1.2128 0.772  0.8524 -0.0269 0.2629  0.0224  186 ASP   A N     
1248 C  CA    . ASP   A 186 ? 1.1829 0.7654 0.8334 -0.0289 0.2386  0.021   186 ASP   A CA    
1249 C  C     . ASP   A 186 ? 1.1383 0.7492 0.8074 -0.0297 0.2171  0.0236  186 ASP   A C     
1250 O  O     . ASP   A 186 ? 1.1196 0.7586 0.8125 -0.0288 0.2004  0.0235  186 ASP   A O     
1251 C  CB    . ASP   A 186 ? 1.1884 0.7941 0.8767 -0.0227 0.242   0.0211  186 ASP   A CB    
1252 C  CG    . ASP   A 186 ? 1.2798 0.8603 0.9562 -0.0206 0.2639  0.019   186 ASP   A CG    
1253 O  OD1   . ASP   A 186 ? 1.3257 0.867  0.957  -0.0254 0.2744  0.016   186 ASP   A OD1   
1254 O  OD2   . ASP   A 186 ? 1.2944 0.8928 1.0054 -0.0143 0.2704  0.0205  186 ASP   A OD2   
1255 N  N     . PHE   A 187 ? 1.1183 0.7218 0.7773 -0.0312 0.2183  0.026   187 PHE   A N     
1256 C  CA    . PHE   A 187 ? 1.0855 0.7143 0.7625 -0.0315 0.1993  0.0285  187 PHE   A CA    
1257 C  C     . PHE   A 187 ? 1.0869 0.6935 0.7272 -0.0377 0.1919  0.0297  187 PHE   A C     
1258 O  O     . PHE   A 187 ? 1.1137 0.6898 0.7249 -0.0397 0.2073  0.0302  187 PHE   A O     
1259 C  CB    . PHE   A 187 ? 1.0571 0.7114 0.7774 -0.0249 0.2072  0.0319  187 PHE   A CB    
1260 C  CG    . PHE   A 187 ? 1.0352 0.7255 0.8002 -0.0196 0.2007  0.032   187 PHE   A CG    
1261 C  CD1   . PHE   A 187 ? 1.025  0.7437 0.8105 -0.0196 0.1801  0.0323  187 PHE   A CD1   
1262 C  CD2   . PHE   A 187 ? 1.039  0.7336 0.8253 -0.0147 0.2155  0.0323  187 PHE   A CD2   
1263 C  CE1   . PHE   A 187 ? 1.0125 0.7617 0.8352 -0.0153 0.1742  0.0325  187 PHE   A CE1   
1264 C  CE2   . PHE   A 187 ? 1.0238 0.7504 0.8494 -0.0103 0.2082  0.0331  187 PHE   A CE2   
1265 C  CZ    . PHE   A 187 ? 1.004  0.757  0.8458 -0.0109 0.1875  0.033   187 PHE   A CZ    
1266 N  N     . VAL   A 188 ? 1.0577 0.6797 0.7006 -0.0406 0.1687  0.0306  188 VAL   A N     
1267 C  CA    . VAL   A 188 ? 1.0523 0.6608 0.6694 -0.0457 0.1573  0.0332  188 VAL   A CA    
1268 C  C     . VAL   A 188 ? 1.0092 0.6523 0.6653 -0.0416 0.1455  0.0359  188 VAL   A C     
1269 O  O     . VAL   A 188 ? 0.9942 0.6595 0.6661 -0.0419 0.1268  0.0356  188 VAL   A O     
1270 C  CB    . VAL   A 188 ? 1.0799 0.6725 0.6627 -0.0536 0.1388  0.0321  188 VAL   A CB    
1271 C  CG1   . VAL   A 188 ? 1.0961 0.679  0.6586 -0.0581 0.125   0.0362  188 VAL   A CG1   
1272 C  CG2   . VAL   A 188 ? 1.1173 0.6731 0.6589 -0.0583 0.1505  0.0287  188 VAL   A CG2   
1273 N  N     . GLY   A 189 ? 0.9876 0.6354 0.6608 -0.0377 0.1578  0.0383  189 GLY   A N     
1274 C  CA    . GLY   A 189 ? 0.9557 0.634  0.6662 -0.0338 0.1494  0.0404  189 GLY   A CA    
1275 C  C     . GLY   A 189 ? 0.9209 0.6294 0.6709 -0.0286 0.1494  0.0383  189 GLY   A C     
1276 O  O     . GLY   A 189 ? 0.9175 0.6239 0.6771 -0.0256 0.1657  0.0375  189 GLY   A O     
1277 N  N     . ILE   A 190 ? 0.8904 0.6255 0.6618 -0.0277 0.1314  0.0376  190 ILE   A N     
1278 C  CA    . ILE   A 190 ? 0.863  0.6249 0.6673 -0.0235 0.1298  0.0356  190 ILE   A CA    
1279 C  C     . ILE   A 190 ? 0.8677 0.6273 0.6603 -0.0256 0.1235  0.0329  190 ILE   A C     
1280 O  O     . ILE   A 190 ? 0.8544 0.6345 0.6713 -0.0225 0.1215  0.0316  190 ILE   A O     
1281 C  CB    . ILE   A 190 ? 0.8371 0.6297 0.6744 -0.0206 0.1174  0.036   190 ILE   A CB    
1282 C  CG1   . ILE   A 190 ? 0.8349 0.6319 0.6632 -0.0235 0.0982  0.0361  190 ILE   A CG1   
1283 C  CG2   . ILE   A 190 ? 0.8332 0.63   0.6878 -0.0182 0.1258  0.0383  190 ILE   A CG2   
1284 C  CD1   . ILE   A 190 ? 0.8222 0.6486 0.682  -0.0204 0.0872  0.0355  190 ILE   A CD1   
1285 N  N     . ILE   A 191 ? 0.8859 0.6204 0.6415 -0.0312 0.1197  0.0323  191 ILE   A N     
1286 C  CA    . ILE   A 191 ? 0.9002 0.6305 0.6436 -0.0342 0.1134  0.0298  191 ILE   A CA    
1287 C  C     . ILE   A 191 ? 0.9163 0.6277 0.6481 -0.0334 0.1318  0.0279  191 ILE   A C     
1288 O  O     . ILE   A 191 ? 0.9324 0.6138 0.6343 -0.0359 0.1439  0.0279  191 ILE   A O     
1289 C  CB    . ILE   A 191 ? 0.925  0.6372 0.6348 -0.0415 0.0986  0.0302  191 ILE   A CB    
1290 C  CG1   . ILE   A 191 ? 0.9295 0.6593 0.6522 -0.0417 0.0813  0.033   191 ILE   A CG1   
1291 C  CG2   . ILE   A 191 ? 0.935  0.6436 0.6343 -0.0451 0.0916  0.0277  191 ILE   A CG2   
1292 C  CD1   . ILE   A 191 ? 0.959  0.6724 0.6527 -0.0487 0.0657  0.0348  191 ILE   A CD1   
1293 N  N     . CYS   A 192 ? 0.9084 0.636  0.6632 -0.0298 0.1346  0.0265  192 CYS   A N     
1294 C  CA    . CYS   A 192 ? 0.9295 0.6399 0.6758 -0.0285 0.1515  0.0249  192 CYS   A CA    
1295 C  C     . CYS   A 192 ? 0.9607 0.6497 0.6727 -0.0351 0.1445  0.0221  192 CYS   A C     
1296 O  O     . CYS   A 192 ? 0.9609 0.6649 0.6794 -0.0372 0.1279  0.0215  192 CYS   A O     
1297 C  CB    . CYS   A 192 ? 0.9144 0.6504 0.6992 -0.0222 0.1559  0.0254  192 CYS   A CB    
1298 S  SG    . CYS   A 192 ? 0.9689 0.6859 0.7499 -0.0192 0.1781  0.0244  192 CYS   A SG    
1299 N  N     . THR   A 193 ? 0.9896 0.6428 0.6644 -0.0388 0.1563  0.0204  193 THR   A N     
1300 C  CA    . THR   A 193 ? 1.0272 0.6567 0.6661 -0.0462 0.149   0.0174  193 THR   A CA    
1301 C  C     . THR   A 193 ? 1.0273 0.6586 0.6741 -0.0448 0.1535  0.0148  193 THR   A C     
1302 O  O     . THR   A 193 ? 1.0473 0.6659 0.6719 -0.051  0.1439  0.0124  193 THR   A O     
1303 C  CB    . THR   A 193 ? 1.0833 0.6702 0.6742 -0.0517 0.1591  0.0162  193 THR   A CB    
1304 O  OG1   . THR   A 193 ? 1.1055 0.6775 0.6969 -0.0468 0.1851  0.0155  193 THR   A OG1   
1305 C  CG2   . THR   A 193 ? 1.0962 0.6793 0.6745 -0.0546 0.1505  0.0193  193 THR   A CG2   
1306 N  N     . ARG   A 194 ? 1.0032 0.6497 0.6817 -0.0371 0.1674  0.0157  194 ARG   A N     
1307 C  CA    . ARG   A 194 ? 0.9967 0.6439 0.684  -0.035  0.1735  0.014   194 ARG   A CA    
1308 C  C     . ARG   A 194 ? 0.9495 0.6352 0.6857 -0.0276 0.1708  0.0169  194 ARG   A C     
1309 O  O     . ARG   A 194 ? 0.9454 0.6342 0.7007 -0.022  0.1845  0.0177  194 ARG   A O     
1310 C  CB    . ARG   A 194 ? 1.0442 0.6617 0.7159 -0.0326 0.199   0.0126  194 ARG   A CB    
1311 C  CG    . ARG   A 194 ? 1.1435 0.7172 0.7629 -0.0399 0.2055  0.0088  194 ARG   A CG    
1312 C  CD    . ARG   A 194 ? 1.2226 0.7706 0.834  -0.0356 0.2341  0.0078  194 ARG   A CD    
1313 N  NE    . ARG   A 194 ? 1.2636 0.8183 0.8974 -0.0303 0.2435  0.0074  194 ARG   A NE    
1314 C  CZ    . ARG   A 194 ? 1.2837 0.8599 0.9598 -0.0212 0.2558  0.0111  194 ARG   A CZ    
1315 N  NH1   . ARG   A 194 ? 1.2628 0.856  0.9638 -0.0166 0.2604  0.0151  194 ARG   A NH1   
1316 N  NH2   . ARG   A 194 ? 1.2767 0.8572 0.971  -0.0169 0.2629  0.0112  194 ARG   A NH2   
1317 N  N     . LEU   A 195 ? 0.9147 0.6286 0.671  -0.0276 0.1533  0.0186  195 LEU   A N     
1318 C  CA    . LEU   A 195 ? 0.8708 0.6191 0.6693 -0.0214 0.1497  0.0211  195 LEU   A CA    
1319 C  C     . LEU   A 195 ? 0.8477 0.6039 0.6581 -0.0199 0.1489  0.0208  195 LEU   A C     
1320 O  O     . LEU   A 195 ? 0.8586 0.6084 0.6526 -0.0249 0.1395  0.0187  195 LEU   A O     
1321 C  CB    . LEU   A 195 ? 0.8566 0.6303 0.6705 -0.0221 0.1319  0.0223  195 LEU   A CB    
1322 C  CG    . LEU   A 195 ? 0.8495 0.6564 0.7037 -0.0163 0.1282  0.0246  195 LEU   A CG    
1323 C  CD1   . LEU   A 195 ? 0.8478 0.6683 0.7176 -0.0142 0.1261  0.0263  195 LEU   A CD1   
1324 C  CD2   . LEU   A 195 ? 0.8471 0.6727 0.7101 -0.0179 0.1124  0.024   195 LEU   A CD2   
1325 N  N     . SER   A 196 ? 0.8145 0.5842 0.6543 -0.0132 0.1588  0.0234  196 SER   A N     
1326 C  CA    . SER   A 196 ? 0.7921 0.5713 0.6475 -0.0108 0.1586  0.0242  196 SER   A CA    
1327 C  C     . SER   A 196 ? 0.7612 0.5755 0.6496 -0.0078 0.1455  0.027   196 SER   A C     
1328 O  O     . SER   A 196 ? 0.7443 0.5743 0.6592 -0.0028 0.1495  0.0301  196 SER   A O     
1329 C  CB    . SER   A 196 ? 0.8015 0.5707 0.6682 -0.0051 0.1787  0.0262  196 SER   A CB    
1330 O  OG    . SER   A 196 ? 0.8226 0.6056 0.711  -0.0016 0.1775  0.0285  196 SER   A OG    
1331 N  N     . PRO   A 197 ? 0.7507 0.577  0.6381 -0.011  0.1303  0.026   197 PRO   A N     
1332 C  CA    . PRO   A 197 ? 0.7292 0.5863 0.6452 -0.0082 0.1193  0.0283  197 PRO   A CA    
1333 C  C     . PRO   A 197 ? 0.712  0.5812 0.6551 -0.0022 0.1262  0.0321  197 PRO   A C     
1334 O  O     . PRO   A 197 ? 0.7022 0.5928 0.6697 0.001   0.1218  0.0347  197 PRO   A O     
1335 C  CB    . PRO   A 197 ? 0.7423 0.6047 0.6489 -0.013  0.1052  0.0266  197 PRO   A CB    
1336 C  CG    . PRO   A 197 ? 0.7698 0.6054 0.6475 -0.0178 0.1091  0.0241  197 PRO   A CG    
1337 C  CD    . PRO   A 197 ? 0.7596 0.5713 0.6201 -0.0176 0.1225  0.023   197 PRO   A CD    
1338 N  N     . LYS   A 198 ? 0.7095 0.5644 0.6489 -0.0007 0.1368  0.0329  198 LYS   A N     
1339 C  CA    . LYS   A 198 ? 0.7006 0.5664 0.6677 0.0053  0.1432  0.0376  198 LYS   A CA    
1340 C  C     . LYS   A 198 ? 0.7079 0.5805 0.6971 0.0101  0.1519  0.0408  198 LYS   A C     
1341 O  O     . LYS   A 198 ? 0.7038 0.5986 0.7212 0.0135  0.1466  0.0449  198 LYS   A O     
1342 C  CB    . LYS   A 198 ? 0.7261 0.5725 0.6847 0.0064  0.1547  0.0378  198 LYS   A CB    
1343 C  CG    . LYS   A 198 ? 0.7684 0.6228 0.7568 0.0134  0.1639  0.0436  198 LYS   A CG    
1344 C  CD    . LYS   A 198 ? 0.853  0.6919 0.8345 0.0142  0.1714  0.044   198 LYS   A CD    
1345 C  CE    . LYS   A 198 ? 0.9138 0.7641 0.9279 0.0213  0.1773  0.0509  198 LYS   A CE    
1346 N  NZ    . LYS   A 198 ? 0.9716 0.81   0.9972 0.0265  0.1963  0.0532  198 LYS   A NZ    
1347 N  N     . LYS   A 199 ? 0.715  0.5683 0.6907 0.0098  0.1643  0.0392  199 LYS   A N     
1348 C  CA    . LYS   A 199 ? 0.7099 0.5678 0.7065 0.0138  0.1742  0.0425  199 LYS   A CA    
1349 C  C     . LYS   A 199 ? 0.6875 0.5678 0.6995 0.0132  0.1618  0.0432  199 LYS   A C     
1350 O  O     . LYS   A 199 ? 0.6841 0.5804 0.7262 0.0169  0.1632  0.0475  199 LYS   A O     
1351 C  CB    . LYS   A 199 ? 0.7693 0.5987 0.7432 0.0129  0.191   0.0402  199 LYS   A CB    
1352 C  CG    . LYS   A 199 ? 0.8755 0.6794 0.8325 0.0136  0.2052  0.0389  199 LYS   A CG    
1353 C  CD    . LYS   A 199 ? 0.9663 0.762  0.9424 0.0199  0.2266  0.0429  199 LYS   A CD    
1354 C  CE    . LYS   A 199 ? 1.0484 0.8233 1.0148 0.0217  0.2395  0.0423  199 LYS   A CE    
1355 N  NZ    . LYS   A 199 ? 1.0915 0.8561 1.0764 0.0283  0.2627  0.0462  199 LYS   A NZ    
1356 N  N     . ILE   A 200 ? 0.6707 0.5521 0.6636 0.0084  0.1494  0.0393  200 ILE   A N     
1357 C  CA    . ILE   A 200 ? 0.6523 0.5537 0.6586 0.0078  0.1379  0.0395  200 ILE   A CA    
1358 C  C     . ILE   A 200 ? 0.6323 0.559  0.662  0.0094  0.1256  0.0417  200 ILE   A C     
1359 O  O     . ILE   A 200 ? 0.6227 0.5665 0.675  0.0111  0.1212  0.044   200 ILE   A O     
1360 C  CB    . ILE   A 200 ? 0.6651 0.5598 0.6466 0.0028  0.1292  0.0353  200 ILE   A CB    
1361 C  CG1   . ILE   A 200 ? 0.6689 0.5792 0.6646 0.003   0.1221  0.0357  200 ILE   A CG1   
1362 C  CG2   . ILE   A 200 ? 0.6677 0.5647 0.635  -0.0007 0.1169  0.0328  200 ILE   A CG2   
1363 C  CD1   . ILE   A 200 ? 0.7043 0.605  0.6777 -0.001  0.1169  0.0328  200 ILE   A CD1   
1364 N  N     . ILE   A 201 ? 0.6192 0.5466 0.6432 0.0088  0.1211  0.0415  201 ILE   A N     
1365 C  CA    . ILE   A 201 ? 0.6056 0.5538 0.6484 0.0102  0.1108  0.0441  201 ILE   A CA    
1366 C  C     . ILE   A 201 ? 0.6065 0.5633 0.6784 0.0151  0.1169  0.05    201 ILE   A C     
1367 O  O     . ILE   A 201 ? 0.5998 0.5753 0.6922 0.0161  0.1085  0.0525  201 ILE   A O     
1368 C  CB    . ILE   A 201 ? 0.5955 0.5408 0.6254 0.0083  0.106   0.043   201 ILE   A CB    
1369 C  CG1   . ILE   A 201 ? 0.6021 0.5447 0.6099 0.0033  0.0968  0.0383  201 ILE   A CG1   
1370 C  CG2   . ILE   A 201 ? 0.5836 0.5478 0.6327 0.0103  0.0979  0.0468  201 ILE   A CG2   
1371 C  CD1   . ILE   A 201 ? 0.612  0.5479 0.6053 0.0005  0.0939  0.0372  201 ILE   A CD1   
1372 N  N     . GLU   A 202 ? 0.6048 0.5469 0.6786 0.018   0.1317  0.0521  202 GLU   A N     
1373 C  CA    . GLU   A 202 ? 0.6055 0.5547 0.7097 0.0231  0.139   0.0586  202 GLU   A CA    
1374 C  C     . GLU   A 202 ? 0.6051 0.5651 0.73   0.024   0.1393  0.0608  202 GLU   A C     
1375 O  O     . GLU   A 202 ? 0.5951 0.5726 0.749  0.0263  0.134   0.0661  202 GLU   A O     
1376 C  CB    . GLU   A 202 ? 0.6228 0.551  0.7235 0.0263  0.1576  0.0599  202 GLU   A CB    
1377 C  CG    . GLU   A 202 ? 0.6766 0.5965 0.7647 0.0261  0.1572  0.0594  202 GLU   A CG    
1378 C  CD    . GLU   A 202 ? 0.7797 0.6778 0.8649 0.0295  0.176   0.0606  202 GLU   A CD    
1379 O  OE1   . GLU   A 202 ? 0.8211 0.7034 0.8999 0.0303  0.1904  0.0592  202 GLU   A OE1   
1380 O  OE2   . GLU   A 202 ? 0.8154 0.7111 0.9038 0.0314  0.177   0.0629  202 GLU   A OE2   
1381 N  N     . LYS   A 203 ? 0.6157 0.5653 0.7257 0.0218  0.144   0.0569  203 LYS   A N     
1382 C  CA    . LYS   A 203 ? 0.61   0.5681 0.738  0.022   0.1448  0.0587  203 LYS   A CA    
1383 C  C     . LYS   A 203 ? 0.6013 0.5829 0.7437 0.0202  0.1266  0.0591  203 LYS   A C     
1384 O  O     . LYS   A 203 ? 0.593  0.5889 0.764  0.0216  0.124   0.0637  203 LYS   A O     
1385 C  CB    . LYS   A 203 ? 0.6398 0.5808 0.7432 0.0192  0.1514  0.0541  203 LYS   A CB    
1386 C  CG    . LYS   A 203 ? 0.671  0.6189 0.7904 0.0189  0.1527  0.0556  203 LYS   A CG    
1387 C  CD    . LYS   A 203 ? 0.7503 0.6861 0.843  0.0151  0.1517  0.0507  203 LYS   A CD    
1388 C  CE    . LYS   A 203 ? 0.809  0.7532 0.9192 0.0146  0.1515  0.0523  203 LYS   A CE    
1389 N  NZ    . LYS   A 203 ? 0.8578 0.7911 0.944  0.0111  0.1497  0.0484  203 LYS   A NZ    
1390 N  N     . TRP   A 204 ? 0.5996 0.5846 0.7228 0.017   0.1141  0.0546  204 TRP   A N     
1391 C  CA    . TRP   A 204 ? 0.5865 0.5902 0.7182 0.0151  0.0982  0.0541  204 TRP   A CA    
1392 C  C     . TRP   A 204 ? 0.5843 0.6019 0.7317 0.0165  0.0898  0.0583  204 TRP   A C     
1393 O  O     . TRP   A 204 ? 0.5803 0.613  0.7411 0.0153  0.0786  0.0596  204 TRP   A O     
1394 C  CB    . TRP   A 204 ? 0.5874 0.5889 0.6945 0.0114  0.0899  0.0479  204 TRP   A CB    
1395 C  CG    . TRP   A 204 ? 0.6015 0.5933 0.6986 0.0099  0.0948  0.045   204 TRP   A CG    
1396 C  CD1   . TRP   A 204 ? 0.6269 0.6012 0.699  0.0082  0.1004  0.0418  204 TRP   A CD1   
1397 C  CD2   . TRP   A 204 ? 0.594  0.5918 0.7057 0.0096  0.0945  0.0458  204 TRP   A CD2   
1398 N  NE1   . TRP   A 204 ? 0.6327 0.6017 0.7019 0.0071  0.1033  0.0407  204 TRP   A NE1   
1399 C  CE2   . TRP   A 204 ? 0.6172 0.6005 0.7112 0.0081  0.1005  0.043   204 TRP   A CE2   
1400 C  CE3   . TRP   A 204 ? 0.5901 0.6032 0.728  0.01    0.0893  0.0489  204 TRP   A CE3   
1401 C  CZ2   . TRP   A 204 ? 0.6262 0.6102 0.728  0.0073  0.1021  0.0431  204 TRP   A CZ2   
1402 C  CZ3   . TRP   A 204 ? 0.6058 0.6199 0.752  0.0088  0.0904  0.0486  204 TRP   A CZ3   
1403 C  CH2   . TRP   A 204 ? 0.6171 0.6168 0.7457 0.0077  0.0974  0.0458  204 TRP   A CH2   
1404 N  N     . VAL   A 205 ? 0.5834 0.5948 0.7291 0.0187  0.0952  0.0608  205 VAL   A N     
1405 C  CA    . VAL   A 205 ? 0.5831 0.606  0.7449 0.0205  0.0883  0.0662  205 VAL   A CA    
1406 C  C     . VAL   A 205 ? 0.588  0.6208 0.7837 0.0233  0.0903  0.0732  205 VAL   A C     
1407 O  O     . VAL   A 205 ? 0.5758 0.624  0.7874 0.0225  0.078   0.0768  205 VAL   A O     
1408 C  CB    . VAL   A 205 ? 0.5936 0.6054 0.746  0.0225  0.0953  0.0675  205 VAL   A CB    
1409 C  CG1   . VAL   A 205 ? 0.586  0.6069 0.7623 0.0259  0.093   0.0754  205 VAL   A CG1   
1410 C  CG2   . VAL   A 205 ? 0.6045 0.6124 0.7296 0.0189  0.0886  0.0622  205 VAL   A CG2   
1411 N  N     . ASP   A 206 ? 0.6016 0.6248 0.8079 0.0262  0.1058  0.0753  206 ASP   A N     
1412 C  CA    . ASP   A 206 ? 0.6031 0.636  0.8453 0.029   0.1091  0.0826  206 ASP   A CA    
1413 C  C     . ASP   A 206 ? 0.5911 0.6383 0.8451 0.0255  0.0971  0.0822  206 ASP   A C     
1414 O  O     . ASP   A 206 ? 0.5811 0.6432 0.8627 0.0256  0.0886  0.0884  206 ASP   A O     
1415 C  CB    . ASP   A 206 ? 0.6482 0.6663 0.8973 0.0325  0.1301  0.0842  206 ASP   A CB    
1416 C  CG    . ASP   A 206 ? 0.7694 0.7979 1.059  0.0355  0.1351  0.0923  206 ASP   A CG    
1417 O  OD1   . ASP   A 206 ? 0.7926 0.8257 1.1066 0.0398  0.1382  0.0997  206 ASP   A OD1   
1418 O  OD2   . ASP   A 206 ? 0.819  0.8513 1.1178 0.0336  0.1359  0.0918  206 ASP   A OD2   
1419 N  N     . PHE   A 207 ? 0.5908 0.633  0.8238 0.022   0.0956  0.0752  207 PHE   A N     
1420 C  CA    . PHE   A 207 ? 0.5857 0.6388 0.8261 0.0184  0.085   0.0737  207 PHE   A CA    
1421 C  C     . PHE   A 207 ? 0.5905 0.6574 0.8298 0.0156  0.0661  0.0735  207 PHE   A C     
1422 O  O     . PHE   A 207 ? 0.5899 0.6692 0.8493 0.0137  0.0562  0.0767  207 PHE   A O     
1423 C  CB    . PHE   A 207 ? 0.5947 0.6371 0.8101 0.0159  0.0884  0.0663  207 PHE   A CB    
1424 C  CG    . PHE   A 207 ? 0.5982 0.6494 0.8143 0.012   0.0767  0.0631  207 PHE   A CG    
1425 C  CD1   . PHE   A 207 ? 0.6046 0.6598 0.8412 0.011   0.0789  0.0654  207 PHE   A CD1   
1426 C  CD2   . PHE   A 207 ? 0.6111 0.6656 0.8075 0.0092  0.0644  0.0578  207 PHE   A CD2   
1427 C  CE1   . PHE   A 207 ? 0.6092 0.6705 0.8452 0.0071  0.0685  0.062   207 PHE   A CE1   
1428 C  CE2   . PHE   A 207 ? 0.6194 0.6799 0.8154 0.0058  0.055   0.0544  207 PHE   A CE2   
1429 C  CZ    . PHE   A 207 ? 0.6111 0.6745 0.8262 0.0047  0.0568  0.0563  207 PHE   A CZ    
1430 N  N     . ALA   A 208 ? 0.5907 0.6543 0.8054 0.0148  0.0611  0.0696  208 ALA   A N     
1431 C  CA    . ALA   A 208 ? 0.5847 0.6586 0.794  0.0122  0.0452  0.0689  208 ALA   A CA    
1432 C  C     . ALA   A 208 ? 0.5765 0.6602 0.8078 0.0136  0.0387  0.0772  208 ALA   A C     
1433 O  O     . ALA   A 208 ? 0.5691 0.6634 0.8086 0.0108  0.025   0.0791  208 ALA   A O     
1434 C  CB    . ALA   A 208 ? 0.5896 0.657  0.7695 0.0112  0.0439  0.0634  208 ALA   A CB    
1435 N  N     . ARG   A 209 ? 0.5816 0.6609 0.8227 0.0179  0.0481  0.0824  209 ARG   A N     
1436 C  CA    . ARG   A 209 ? 0.5877 0.676  0.8524 0.0199  0.0424  0.0915  209 ARG   A CA    
1437 C  C     . ARG   A 209 ? 0.599  0.6994 0.896  0.0191  0.0365  0.0975  209 ARG   A C     
1438 O  O     . ARG   A 209 ? 0.5996 0.7109 0.9096 0.0175  0.0223  0.1031  209 ARG   A O     
1439 C  CB    . ARG   A 209 ? 0.592  0.6717 0.8639 0.0253  0.0563  0.0961  209 ARG   A CB    
1440 C  CG    . ARG   A 209 ? 0.6551 0.7249 0.8986 0.0254  0.0581  0.0922  209 ARG   A CG    
1441 C  CD    . ARG   A 209 ? 0.6975 0.7599 0.9491 0.0303  0.0682  0.0977  209 ARG   A CD    
1442 N  NE    . ARG   A 209 ? 0.7327 0.8057 1.0004 0.0313  0.057   0.1059  209 ARG   A NE    
1443 C  CZ    . ARG   A 209 ? 0.7605 0.8378 1.0591 0.0357  0.0601  0.1154  209 ARG   A CZ    
1444 N  NH1   . ARG   A 209 ? 0.7602 0.8318 1.0775 0.0398  0.076   0.1176  209 ARG   A NH1   
1445 N  NH2   . ARG   A 209 ? 0.754  0.8409 1.0653 0.0361  0.0477  0.1233  209 ARG   A NH2   
1446 N  N     . ARG   A 210 ? 0.6036 0.7015 0.9126 0.0196  0.0465  0.0966  210 ARG   A N     
1447 C  CA    . ARG   A 210 ? 0.6057 0.7152 0.9474 0.0183  0.0416  0.1022  210 ARG   A CA    
1448 C  C     . ARG   A 210 ? 0.602  0.7202 0.9373 0.0119  0.0229  0.0989  210 ARG   A C     
1449 O  O     . ARG   A 210 ? 0.5935 0.7236 0.9512 0.0096  0.0098  0.1053  210 ARG   A O     
1450 C  CB    . ARG   A 210 ? 0.6397 0.7428 0.9936 0.0201  0.0585  0.1017  210 ARG   A CB    
1451 C  CG    . ARG   A 210 ? 0.7159 0.8111 1.0842 0.0265  0.077   0.1069  210 ARG   A CG    
1452 C  CD    . ARG   A 210 ? 0.8081 0.8911 1.1759 0.0282  0.0965  0.1043  210 ARG   A CD    
1453 N  NE    . ARG   A 210 ? 0.8875 0.9715 1.2909 0.0332  0.1107  0.1131  210 ARG   A NE    
1454 C  CZ    . ARG   A 210 ? 0.9495 1.02   1.3547 0.0362  0.132   0.1127  210 ARG   A CZ    
1455 N  NH1   . ARG   A 210 ? 0.9313 1.0038 1.372  0.0411  0.1453  0.1212  210 ARG   A NH1   
1456 N  NH2   . ARG   A 210 ? 0.9833 1.0378 1.3552 0.0344  0.1406  0.1042  210 ARG   A NH2   
1457 N  N     . LEU   A 211 ? 0.6041 0.7156 0.9086 0.0089  0.0214  0.0892  211 LEU   A N     
1458 C  CA    . LEU   A 211 ? 0.6039 0.721  0.8991 0.003   0.0054  0.0851  211 LEU   A CA    
1459 C  C     . LEU   A 211 ? 0.6018 0.725  0.8911 0.0009  -0.0104 0.088   211 LEU   A C     
1460 O  O     . LEU   A 211 ? 0.5948 0.7259 0.894  -0.0034 -0.0253 0.0907  211 LEU   A O     
1461 C  CB    . LEU   A 211 ? 0.6201 0.728  0.8833 0.0013  0.0084  0.0747  211 LEU   A CB    
1462 C  CG    . LEU   A 211 ? 0.6425 0.7444 0.9076 0.0013  0.019   0.071   211 LEU   A CG    
1463 C  CD1   . LEU   A 211 ? 0.6574 0.7506 0.8913 0       0.0202  0.0618  211 LEU   A CD1   
1464 C  CD2   . LEU   A 211 ? 0.6367 0.7465 0.9255 -0.0023 0.0121  0.0735  211 LEU   A CD2   
1465 N  N     . CYS   A 212 ? 0.6055 0.7239 0.8782 0.0037  -0.0071 0.088   212 CYS   A N     
1466 C  CA    . CYS   A 212 ? 0.6096 0.731  0.8725 0.0024  -0.0194 0.0909  212 CYS   A CA    
1467 C  C     . CYS   A 212 ? 0.6044 0.7358 0.8983 0.003   -0.0281 0.1024  212 CYS   A C     
1468 O  O     . CYS   A 212 ? 0.5964 0.7332 0.8887 -0.0011 -0.0448 0.1053  212 CYS   A O     
1469 C  CB    . CYS   A 212 ? 0.6207 0.7337 0.8618 0.0056  -0.0107 0.0885  212 CYS   A CB    
1470 S  SG    . CYS   A 212 ? 0.6392 0.7538 0.8641 0.0039  -0.0236 0.0917  212 CYS   A SG    
1471 N  N     . GLU   A 213 ? 0.6064 0.7393 0.9281 0.0081  -0.0168 0.1092  213 GLU   A N     
1472 C  CA    . GLU   A 213 ? 0.6127 0.7559 0.9696 0.0096  -0.0236 0.1213  213 GLU   A CA    
1473 C  C     . GLU   A 213 ? 0.6149 0.7687 0.9929 0.0042  -0.0376 0.1241  213 GLU   A C     
1474 O  O     . GLU   A 213 ? 0.6084 0.771  1.0026 0.0019  -0.0534 0.1323  213 GLU   A O     
1475 C  CB    . GLU   A 213 ? 0.6494 0.7908 1.0332 0.0166  -0.0055 0.1271  213 GLU   A CB    
1476 C  CG    . GLU   A 213 ? 0.7706 0.9031 1.1417 0.0217  0.0045  0.128   213 GLU   A CG    
1477 C  CD    . GLU   A 213 ? 0.8965 1.0226 1.2875 0.0285  0.0252  0.1318  213 GLU   A CD    
1478 O  OE1   . GLU   A 213 ? 0.9204 1.044  1.3217 0.0293  0.0372  0.1294  213 GLU   A OE1   
1479 O  OE2   . GLU   A 213 ? 0.9371 1.0595 1.3322 0.0331  0.0303  0.1369  213 GLU   A OE2   
1480 N  N     . HIS   A 214 ? 0.6277 0.7797 1.0042 0.0018  -0.033  0.1177  214 HIS   A N     
1481 C  CA    . HIS   A 214 ? 0.6414 0.8019 1.0363 -0.004  -0.0457 0.1194  214 HIS   A CA    
1482 C  C     . HIS   A 214 ? 0.6474 0.8089 1.0203 -0.0112 -0.0673 0.1165  214 HIS   A C     
1483 O  O     . HIS   A 214 ? 0.6446 0.8144 1.0363 -0.0163 -0.0834 0.122   214 HIS   A O     
1484 C  CB    . HIS   A 214 ? 0.6731 0.829  1.0662 -0.0049 -0.0344 0.112   214 HIS   A CB    
1485 C  CG    . HIS   A 214 ? 0.724  0.888  1.1406 -0.0105 -0.0447 0.1143  214 HIS   A CG    
1486 N  ND1   . HIS   A 214 ? 0.7701 0.9298 1.168  -0.0161 -0.05   0.1054  214 HIS   A ND1   
1487 C  CD2   . HIS   A 214 ? 0.7301 0.9062 1.1883 -0.0115 -0.0508 0.1247  214 HIS   A CD2   
1488 C  CE1   . HIS   A 214 ? 0.7651 0.9335 1.192  -0.0208 -0.0593 0.1103  214 HIS   A CE1   
1489 N  NE2   . HIS   A 214 ? 0.747  0.9261 1.2117 -0.0184 -0.0605 0.1221  214 HIS   A NE2   
1490 N  N     . LYS   A 215 ? 0.6529 0.8052 0.9864 -0.012  -0.0674 0.108   215 LYS   A N     
1491 C  CA    . LYS   A 215 ? 0.6542 0.8041 0.9616 -0.0185 -0.0847 0.1041  215 LYS   A CA    
1492 C  C     . LYS   A 215 ? 0.6428 0.7939 0.9433 -0.0188 -0.0963 0.1109  215 LYS   A C     
1493 O  O     . LYS   A 215 ? 0.6512 0.8038 0.9463 -0.0249 -0.1149 0.1134  215 LYS   A O     
1494 C  CB    . LYS   A 215 ? 0.6979 0.8369 0.9678 -0.0192 -0.0776 0.0915  215 LYS   A CB    
1495 C  CG    . LYS   A 215 ? 0.7811 0.9146 1.0195 -0.0253 -0.0915 0.0859  215 LYS   A CG    
1496 C  CD    . LYS   A 215 ? 0.8718 0.9957 1.0802 -0.0249 -0.0817 0.074   215 LYS   A CD    
1497 C  CE    . LYS   A 215 ? 0.947  1.0633 1.1221 -0.0299 -0.0913 0.0674  215 LYS   A CE    
1498 N  NZ    . LYS   A 215 ? 0.9898 1.098  1.1402 -0.028  -0.0797 0.0571  215 LYS   A NZ    
1499 N  N     . TYR   A 216 ? 0.6236 0.7728 0.923  -0.0126 -0.0859 0.1142  216 TYR   A N     
1500 C  CA    . TYR   A 216 ? 0.6091 0.7578 0.899  -0.0125 -0.0952 0.1204  216 TYR   A CA    
1501 C  C     . TYR   A 216 ? 0.5972 0.7539 0.9213 -0.0082 -0.0965 0.1338  216 TYR   A C     
1502 O  O     . TYR   A 216 ? 0.6105 0.767  0.9284 -0.0085 -0.1063 0.1402  216 TYR   A O     
1503 C  CB    . TYR   A 216 ? 0.6056 0.7443 0.8625 -0.0096 -0.0845 0.1138  216 TYR   A CB    
1504 C  CG    . TYR   A 216 ? 0.6063 0.7371 0.8287 -0.0135 -0.0837 0.1016  216 TYR   A CG    
1505 C  CD1   . TYR   A 216 ? 0.6174 0.7438 0.8129 -0.0191 -0.0971 0.099   216 TYR   A CD1   
1506 C  CD2   . TYR   A 216 ? 0.61   0.7363 0.8252 -0.0112 -0.0689 0.093   216 TYR   A CD2   
1507 C  CE1   . TYR   A 216 ? 0.6325 0.7511 0.7979 -0.022  -0.0947 0.0878  216 TYR   A CE1   
1508 C  CE2   . TYR   A 216 ? 0.6255 0.7451 0.8121 -0.0141 -0.0679 0.0825  216 TYR   A CE2   
1509 C  CZ    . TYR   A 216 ? 0.6435 0.7594 0.8061 -0.0192 -0.0801 0.0799  216 TYR   A CZ    
1510 O  OH    . TYR   A 216 ? 0.6697 0.7785 0.8057 -0.0215 -0.0773 0.0697  216 TYR   A OH    
1511 N  N     . GLY   A 217 ? 0.5754 0.7379 0.9343 -0.0038 -0.0856 0.1382  217 GLY   A N     
1512 C  CA    . GLY   A 217 ? 0.5608 0.7307 0.956  0.0013  -0.0844 0.1512  217 GLY   A CA    
1513 C  C     . GLY   A 217 ? 0.5634 0.7261 0.9554 0.0091  -0.066  0.1519  217 GLY   A C     
1514 O  O     . GLY   A 217 ? 0.5616 0.7286 0.9847 0.0147  -0.0604 0.1618  217 GLY   A O     
1515 N  N     . ASN   A 218 ? 0.5619 0.7134 0.9169 0.0095  -0.0568 0.1416  218 ASN   A N     
1516 C  CA    . ASN   A 218 ? 0.5572 0.6992 0.9024 0.0155  -0.0396 0.14    218 ASN   A CA    
1517 C  C     . ASN   A 218 ? 0.5554 0.6869 0.8643 0.014   -0.0303 0.1267  218 ASN   A C     
1518 O  O     . ASN   A 218 ? 0.5588 0.6906 0.8496 0.0088  -0.0379 0.1195  218 ASN   A O     
1519 C  CB    . ASN   A 218 ? 0.5757 0.7163 0.915  0.0171  -0.0465 0.1473  218 ASN   A CB    
1520 C  CG    . ASN   A 218 ? 0.6055 0.7373 0.9457 0.024   -0.0289 0.1487  218 ASN   A CG    
1521 O  OD1   . ASN   A 218 ? 0.6096 0.739  0.9699 0.029   -0.0129 0.1495  218 ASN   A OD1   
1522 N  ND2   . ASN   A 218 ? 0.6163 0.7417 0.9341 0.0241  -0.0309 0.149   218 ASN   A ND2   
1523 N  N     . ALA   A 219 ? 0.5487 0.6704 0.8478 0.0185  -0.014  0.1237  219 ALA   A N     
1524 C  CA    . ALA   A 219 ? 0.5487 0.66   0.816  0.0174  -0.0048 0.1125  219 ALA   A CA    
1525 C  C     . ALA   A 219 ? 0.5451 0.6469 0.7991 0.0209  0.0043  0.113   219 ALA   A C     
1526 O  O     . ALA   A 219 ? 0.5338 0.6341 0.8072 0.0257  0.0111  0.1204  219 ALA   A O     
1527 C  CB    . ALA   A 219 ? 0.5449 0.6523 0.819  0.0188  0.0088  0.1075  219 ALA   A CB    
1528 N  N     . PRO   A 220 ? 0.5486 0.6435 0.771  0.0185  0.0052  0.1052  220 PRO   A N     
1529 C  CA    . PRO   A 220 ? 0.5573 0.6425 0.7665 0.0208  0.0136  0.1052  220 PRO   A CA    
1530 C  C     . PRO   A 220 ? 0.5717 0.6465 0.7871 0.025   0.0313  0.1039  220 PRO   A C     
1531 O  O     . PRO   A 220 ? 0.5757 0.6479 0.7922 0.0248  0.0384  0.099   220 PRO   A O     
1532 C  CB    . PRO   A 220 ? 0.5704 0.6517 0.7473 0.0167  0.0112  0.0964  220 PRO   A CB    
1533 C  CG    . PRO   A 220 ? 0.5709 0.6603 0.7442 0.0125  -0.0006 0.0934  220 PRO   A CG    
1534 C  CD    . PRO   A 220 ? 0.5444 0.6397 0.7432 0.0135  -0.0009 0.0964  220 PRO   A CD    
1535 N  N     . ARG   A 221 ? 0.5778 0.6449 0.7951 0.0285  0.0388  0.108   221 ARG   A N     
1536 C  CA    . ARG   A 221 ? 0.5998 0.6528 0.8164 0.0319  0.0565  0.1056  221 ARG   A CA    
1537 C  C     . ARG   A 221 ? 0.603  0.6459 0.7869 0.0281  0.0601  0.0955  221 ARG   A C     
1538 O  O     . ARG   A 221 ? 0.6038 0.6496 0.7694 0.0245  0.0511  0.0927  221 ARG   A O     
1539 C  CB    . ARG   A 221 ? 0.6496 0.6953 0.8752 0.0363  0.0634  0.1124  221 ARG   A CB    
1540 C  CG    . ARG   A 221 ? 0.7373 0.7902 0.9999 0.0415  0.0646  0.123   221 ARG   A CG    
1541 C  CD    . ARG   A 221 ? 0.8236 0.8618 1.0952 0.0472  0.0831  0.1254  221 ARG   A CD    
1542 N  NE    . ARG   A 221 ? 0.8756 0.9205 1.1849 0.053   0.0848  0.1369  221 ARG   A NE    
1543 C  CZ    . ARG   A 221 ? 0.9113 0.9608 1.2493 0.0562  0.0919  0.1406  221 ARG   A CZ    
1544 N  NH1   . ARG   A 221 ? 0.9133 0.9609 1.2448 0.054   0.0979  0.1334  221 ARG   A NH1   
1545 N  NH2   . ARG   A 221 ? 0.9009 0.9574 1.2759 0.0616  0.0931  0.152   221 ARG   A NH2   
1546 N  N     . VAL   A 222 ? 0.595  0.6256 0.772  0.0288  0.0731  0.0904  222 VAL   A N     
1547 C  CA    . VAL   A 222 ? 0.6002 0.6205 0.7482 0.0252  0.0759  0.0818  222 VAL   A CA    
1548 C  C     . VAL   A 222 ? 0.6154 0.6172 0.7529 0.0267  0.0889  0.0808  222 VAL   A C     
1549 O  O     . VAL   A 222 ? 0.6251 0.6175 0.773  0.0303  0.1016  0.0826  222 VAL   A O     
1550 C  CB    . VAL   A 222 ? 0.6023 0.6226 0.744  0.0229  0.0768  0.0756  222 VAL   A CB    
1551 C  CG1   . VAL   A 222 ? 0.617  0.6275 0.73   0.0189  0.0776  0.0677  222 VAL   A CG1   
1552 C  CG2   . VAL   A 222 ? 0.597  0.6343 0.7492 0.0212  0.0639  0.0764  222 VAL   A CG2   
1553 N  N     . ARG   A 223 ? 0.616  0.6119 0.7338 0.0239  0.0864  0.0782  223 ARG   A N     
1554 C  CA    . ARG   A 223 ? 0.6254 0.6019 0.7293 0.024   0.0976  0.0762  223 ARG   A CA    
1555 C  C     . ARG   A 223 ? 0.6339 0.6009 0.712  0.0189  0.0981  0.0677  223 ARG   A C     
1556 O  O     . ARG   A 223 ? 0.6357 0.6122 0.7045 0.0151  0.0877  0.0645  223 ARG   A O     
1557 C  CB    . ARG   A 223 ? 0.6481 0.6233 0.7475 0.0234  0.0939  0.0795  223 ARG   A CB    
1558 C  CG    . ARG   A 223 ? 0.6878 0.672  0.8113 0.0281  0.0914  0.0889  223 ARG   A CG    
1559 C  CD    . ARG   A 223 ? 0.7372 0.7126 0.8567 0.0289  0.0938  0.0926  223 ARG   A CD    
1560 N  NE    . ARG   A 223 ? 0.7955 0.7692 0.892  0.0233  0.0876  0.0884  223 ARG   A NE    
1561 C  CZ    . ARG   A 223 ? 0.8262 0.8123 0.9207 0.0212  0.0759  0.0909  223 ARG   A CZ    
1562 N  NH1   . ARG   A 223 ? 0.8024 0.803  0.9138 0.0235  0.0674  0.0974  223 ARG   A NH1   
1563 N  NH2   . ARG   A 223 ? 0.8384 0.822  0.9139 0.0163  0.0725  0.0872  223 ARG   A NH2   
1564 N  N     . ILE   A 224 ? 0.6365 0.584  0.7027 0.0188  0.1102  0.0643  224 ILE   A N     
1565 C  CA    . ILE   A 224 ? 0.6449 0.5808 0.6854 0.0136  0.1101  0.057   224 ILE   A CA    
1566 C  C     . ILE   A 224 ? 0.6563 0.5726 0.6779 0.0112  0.1157  0.055   224 ILE   A C     
1567 O  O     . ILE   A 224 ? 0.6612 0.5633 0.6858 0.0144  0.1275  0.0571  224 ILE   A O     
1568 C  CB    . ILE   A 224 ? 0.6565 0.5836 0.6948 0.0145  0.1188  0.0544  224 ILE   A CB    
1569 C  CG1   . ILE   A 224 ? 0.6497 0.5966 0.7103 0.017   0.1135  0.0571  224 ILE   A CG1   
1570 C  CG2   . ILE   A 224 ? 0.6773 0.5914 0.6874 0.0087  0.1172  0.0475  224 ILE   A CG2   
1571 C  CD1   . ILE   A 224 ? 0.665  0.6047 0.7285 0.0185  0.1232  0.0559  224 ILE   A CD1   
1572 N  N     . ASN   A 225 ? 0.6515 0.5672 0.6556 0.0055  0.1072  0.0514  225 ASN   A N     
1573 C  CA    . ASN   A 225 ? 0.6577 0.5548 0.6428 0.0016  0.1104  0.0491  225 ASN   A CA    
1574 C  C     . ASN   A 225 ? 0.6625 0.5505 0.6235 -0.0054 0.1051  0.0429  225 ASN   A C     
1575 O  O     . ASN   A 225 ? 0.6705 0.5667 0.6305 -0.0065 0.0998  0.0407  225 ASN   A O     
1576 C  CB    . ASN   A 225 ? 0.6601 0.5654 0.6528 0.0017  0.1052  0.0534  225 ASN   A CB    
1577 C  CG    . ASN   A 225 ? 0.6913 0.6177 0.6882 -0.0007 0.0916  0.0541  225 ASN   A CG    
1578 O  OD1   . ASN   A 225 ? 0.715  0.6446 0.7009 -0.0054 0.0848  0.0499  225 ASN   A OD1   
1579 N  ND2   . ASN   A 225 ? 0.679  0.6192 0.6915 0.0023  0.0877  0.0598  225 ASN   A ND2   
1580 N  N     . GLY   A 226 ? 0.6626 0.533  0.6048 -0.0103 0.1062  0.0404  226 GLY   A N     
1581 C  CA    . GLY   A 226 ? 0.6792 0.5396 0.5989 -0.0177 0.0998  0.0354  226 GLY   A CA    
1582 C  C     . GLY   A 226 ? 0.7073 0.5413 0.6054 -0.0195 0.1091  0.0314  226 GLY   A C     
1583 O  O     . GLY   A 226 ? 0.7178 0.5337 0.6119 -0.0169 0.1221  0.0315  226 GLY   A O     
1584 N  N     . HIS   A 227 ? 0.7068 0.5377 0.5907 -0.0238 0.1032  0.028   227 HIS   A N     
1585 C  CA    . HIS   A 227 ? 0.7188 0.5234 0.5783 -0.0263 0.1109  0.0242  227 HIS   A CA    
1586 C  C     . HIS   A 227 ? 0.7208 0.5253 0.59   -0.0198 0.1225  0.0253  227 HIS   A C     
1587 O  O     . HIS   A 227 ? 0.7251 0.5284 0.5872 -0.0207 0.1211  0.0238  227 HIS   A O     
1588 C  CB    . HIS   A 227 ? 0.728  0.5275 0.5673 -0.034  0.0989  0.021   227 HIS   A CB    
1589 C  CG    . HIS   A 227 ? 0.7516 0.548  0.5812 -0.0412 0.0884  0.0201  227 HIS   A CG    
1590 N  ND1   . HIS   A 227 ? 0.7652 0.5742 0.5951 -0.0464 0.0731  0.02    227 HIS   A ND1   
1591 C  CD2   . HIS   A 227 ? 0.7667 0.5498 0.589  -0.0439 0.0915  0.0197  227 HIS   A CD2   
1592 C  CE1   . HIS   A 227 ? 0.7728 0.5761 0.596  -0.0524 0.0672  0.0197  227 HIS   A CE1   
1593 N  NE2   . HIS   A 227 ? 0.7782 0.5656 0.5958 -0.0513 0.0777  0.0193  227 HIS   A NE2   
1594 N  N     . VAL   A 228 ? 0.7193 0.5241 0.6052 -0.0132 0.1344  0.0285  228 VAL   A N     
1595 C  CA    . VAL   A 228 ? 0.7298 0.5354 0.6306 -0.0065 0.1469  0.0308  228 VAL   A CA    
1596 C  C     . VAL   A 228 ? 0.7724 0.5486 0.6483 -0.008  0.1602  0.0271  228 VAL   A C     
1597 O  O     . VAL   A 228 ? 0.7757 0.5531 0.6613 -0.0038 0.169   0.0284  228 VAL   A O     
1598 C  CB    . VAL   A 228 ? 0.7277 0.5401 0.6542 0.0006  0.1556  0.036   228 VAL   A CB    
1599 C  CG1   . VAL   A 228 ? 0.7191 0.561  0.6698 0.0023  0.1423  0.0403  228 VAL   A CG1   
1600 C  CG2   . VAL   A 228 ? 0.7337 0.521  0.645  -0.0004 0.1655  0.0347  228 VAL   A CG2   
1601 N  N     . ALA   A 229 ? 0.7982 0.5469 0.6414 -0.0144 0.1617  0.0225  229 ALA   A N     
1602 C  CA    . ALA   A 229 ? 0.8303 0.5472 0.6442 -0.0167 0.1744  0.0186  229 ALA   A CA    
1603 C  C     . ALA   A 229 ? 0.8461 0.5565 0.6347 -0.0239 0.1634  0.0153  229 ALA   A C     
1604 O  O     . ALA   A 229 ? 0.8651 0.5474 0.6247 -0.0269 0.1721  0.0121  229 ALA   A O     
1605 C  CB    . ALA   A 229 ? 0.8545 0.5398 0.6441 -0.0195 0.1847  0.0154  229 ALA   A CB    
1606 N  N     . ALA   A 230 ? 0.8328 0.5679 0.6319 -0.0264 0.1448  0.0164  230 ALA   A N     
1607 C  CA    . ALA   A 230 ? 0.845  0.576  0.6239 -0.0328 0.133   0.0143  230 ALA   A CA    
1608 C  C     . ALA   A 230 ? 0.8514 0.5762 0.6259 -0.0305 0.141   0.0144  230 ALA   A C     
1609 O  O     . ALA   A 230 ? 0.8345 0.574  0.6346 -0.0233 0.1493  0.0173  230 ALA   A O     
1610 C  CB    . ALA   A 230 ? 0.8271 0.5879 0.6243 -0.0343 0.114   0.0161  230 ALA   A CB    
1611 N  N     . ARG   A 231 ? 0.8691 0.5706 0.6103 -0.037  0.1384  0.0116  231 ARG   A N     
1612 C  CA    . ARG   A 231 ? 0.8768 0.5682 0.6071 -0.0363 0.1449  0.0117  231 ARG   A CA    
1613 C  C     . ARG   A 231 ? 0.8779 0.5597 0.5814 -0.0446 0.1293  0.0104  231 ARG   A C     
1614 O  O     . ARG   A 231 ? 0.8911 0.5519 0.566  -0.052  0.1233  0.0078  231 ARG   A O     
1615 C  CB    . ARG   A 231 ? 0.9211 0.5812 0.6325 -0.0344 0.1676  0.01    231 ARG   A CB    
1616 C  CG    . ARG   A 231 ? 0.9645 0.6399 0.7104 -0.0247 0.1833  0.0135  231 ARG   A CG    
1617 C  CD    . ARG   A 231 ? 1.0468 0.692  0.7777 -0.022  0.2077  0.0123  231 ARG   A CD    
1618 N  NE    . ARG   A 231 ? 1.1082 0.7644 0.8641 -0.0152 0.2201  0.0159  231 ARG   A NE    
1619 C  CZ    . ARG   A 231 ? 1.1307 0.8049 0.9244 -0.0071 0.23    0.0199  231 ARG   A CZ    
1620 N  NH1   . ARG   A 231 ? 1.1273 0.8086 0.9363 -0.0044 0.2301  0.0208  231 ARG   A NH1   
1621 N  NH2   . ARG   A 231 ? 1.1205 0.805  0.9374 -0.0019 0.2397  0.0235  231 ARG   A NH2   
1622 N  N     . PHE   A 232 ? 0.8622 0.5598 0.5761 -0.0435 0.1217  0.0126  232 PHE   A N     
1623 C  CA    . PHE   A 232 ? 0.8698 0.5623 0.5639 -0.0505 0.1053  0.0127  232 PHE   A CA    
1624 C  C     . PHE   A 232 ? 0.8854 0.5861 0.587  -0.0476 0.1055  0.015   232 PHE   A C     
1625 O  O     . PHE   A 232 ? 0.8719 0.5916 0.6023 -0.0403 0.1136  0.0168  232 PHE   A O     
1626 C  CB    . PHE   A 232 ? 0.8437 0.5608 0.5551 -0.053  0.0856  0.0137  232 PHE   A CB    
1627 C  CG    . PHE   A 232 ? 0.8138 0.5665 0.5669 -0.0458 0.0847  0.0158  232 PHE   A CG    
1628 C  CD1   . PHE   A 232 ? 0.7975 0.5733 0.5733 -0.0416 0.0802  0.0181  232 PHE   A CD1   
1629 C  CD2   . PHE   A 232 ? 0.8096 0.5705 0.5774 -0.0433 0.0887  0.0156  232 PHE   A CD2   
1630 C  CE1   . PHE   A 232 ? 0.7846 0.5897 0.5946 -0.0355 0.0796  0.0196  232 PHE   A CE1   
1631 C  CE2   . PHE   A 232 ? 0.7924 0.5833 0.5951 -0.037  0.0879  0.0178  232 PHE   A CE2   
1632 C  CZ    . PHE   A 232 ? 0.7763 0.5886 0.5989 -0.0334 0.083   0.0196  232 PHE   A CZ    
1633 N  N     . PRO   A 233 ? 0.9095 0.5975 0.5873 -0.0534 0.0951  0.0156  233 PRO   A N     
1634 C  CA    . PRO   A 233 ? 0.9045 0.6012 0.5908 -0.0507 0.0941  0.0183  233 PRO   A CA    
1635 C  C     . PRO   A 233 ? 0.8806 0.6156 0.6064 -0.0461 0.0831  0.0204  233 PRO   A C     
1636 O  O     . PRO   A 233 ? 0.8787 0.6286 0.6139 -0.0484 0.0686  0.0207  233 PRO   A O     
1637 C  CB    . PRO   A 233 ? 0.9348 0.6096 0.5863 -0.0589 0.0817  0.019   233 PRO   A CB    
1638 C  CG    . PRO   A 233 ? 0.9638 0.6097 0.5816 -0.0659 0.0823  0.0159  233 PRO   A CG    
1639 C  CD    . PRO   A 233 ? 0.9262 0.591  0.5689 -0.063  0.0827  0.0145  233 PRO   A CD    
1640 N  N     . PHE   A 234 ? 0.8597 0.6099 0.6089 -0.0398 0.0905  0.022   234 PHE   A N     
1641 C  CA    . PHE   A 234 ? 0.8301 0.6141 0.6147 -0.0355 0.0817  0.0234  234 PHE   A CA    
1642 C  C     . PHE   A 234 ? 0.814  0.6066 0.6149 -0.0307 0.0887  0.0251  234 PHE   A C     
1643 O  O     . PHE   A 234 ? 0.8205 0.5992 0.6161 -0.0288 0.1041  0.0253  234 PHE   A O     
1644 C  CB    . PHE   A 234 ? 0.8171 0.6194 0.6257 -0.0316 0.0844  0.0226  234 PHE   A CB    
1645 C  CG    . PHE   A 234 ? 0.8135 0.6443 0.6463 -0.0306 0.0704  0.0232  234 PHE   A CG    
1646 C  CD1   . PHE   A 234 ? 0.8259 0.6578 0.6506 -0.0355 0.0566  0.023   234 PHE   A CD1   
1647 C  CD2   . PHE   A 234 ? 0.8081 0.6637 0.6716 -0.0249 0.0715  0.024   234 PHE   A CD2   
1648 C  CE1   . PHE   A 234 ? 0.8204 0.6777 0.6679 -0.0342 0.0461  0.0236  234 PHE   A CE1   
1649 C  CE2   . PHE   A 234 ? 0.8026 0.6818 0.6854 -0.024  0.0604  0.0241  234 PHE   A CE2   
1650 C  CZ    . PHE   A 234 ? 0.8023 0.6823 0.6773 -0.0284 0.0486  0.024   234 PHE   A CZ    
1651 N  N     . ILE   A 235 ? 0.7984 0.6141 0.6211 -0.0287 0.0782  0.0263  235 ILE   A N     
1652 C  CA    . ILE   A 235 ? 0.7907 0.6166 0.6317 -0.0245 0.0834  0.0277  235 ILE   A CA    
1653 C  C     . ILE   A 235 ? 0.7767 0.6267 0.6505 -0.0192 0.0869  0.0274  235 ILE   A C     
1654 O  O     . ILE   A 235 ? 0.7702 0.6407 0.6604 -0.0183 0.0763  0.0268  235 ILE   A O     
1655 C  CB    . ILE   A 235 ? 0.7848 0.6199 0.6295 -0.0255 0.07    0.0291  235 ILE   A CB    
1656 C  CG1   . ILE   A 235 ? 0.8158 0.6268 0.6278 -0.0312 0.0643  0.0304  235 ILE   A CG1   
1657 C  CG2   . ILE   A 235 ? 0.7695 0.6163 0.6351 -0.0214 0.0746  0.0301  235 ILE   A CG2   
1658 C  CD1   . ILE   A 235 ? 0.8296 0.6487 0.6454 -0.0323 0.05    0.0326  235 ILE   A CD1   
1659 N  N     . PRO   A 236 ? 0.7731 0.621  0.6576 -0.0157 0.1013  0.0282  236 PRO   A N     
1660 C  CA    . PRO   A 236 ? 0.7533 0.624  0.6692 -0.0111 0.1026  0.0288  236 PRO   A CA    
1661 C  C     . PRO   A 236 ? 0.7379 0.6324 0.6785 -0.009  0.0939  0.0291  236 PRO   A C     
1662 O  O     . PRO   A 236 ? 0.7258 0.6392 0.6863 -0.0069 0.0893  0.0289  236 PRO   A O     
1663 C  CB    . PRO   A 236 ? 0.7598 0.6209 0.682  -0.0082 0.1203  0.0306  236 PRO   A CB    
1664 C  CG    . PRO   A 236 ? 0.7745 0.611  0.672  -0.0107 0.1285  0.0308  236 PRO   A CG    
1665 C  CD    . PRO   A 236 ? 0.7742 0.5981 0.6426 -0.0159 0.1175  0.029   236 PRO   A CD    
1666 N  N     . MET   A 237 ? 0.738  0.6302 0.6767 -0.0097 0.0923  0.0296  237 MET   A N     
1667 C  CA    . MET   A 237 ? 0.7294 0.6404 0.6899 -0.0079 0.0857  0.0296  237 MET   A CA    
1668 C  C     . MET   A 237 ? 0.7161 0.6486 0.691  -0.0071 0.0736  0.0278  237 MET   A C     
1669 O  O     . MET   A 237 ? 0.7094 0.6572 0.706  -0.0048 0.0733  0.0279  237 MET   A O     
1670 C  CB    . MET   A 237 ? 0.7463 0.649  0.6967 -0.0096 0.0828  0.0301  237 MET   A CB    
1671 C  CG    . MET   A 237 ? 0.7773 0.6961 0.7495 -0.0078 0.0784  0.0299  237 MET   A CG    
1672 S  SD    . MET   A 237 ? 0.8949 0.8002 0.8587 -0.009  0.0814  0.0318  237 MET   A SD    
1673 C  CE    . MET   A 237 ? 0.8637 0.7874 0.8436 -0.008  0.0685  0.03    237 MET   A CE    
1674 N  N     . PRO   A 238 ? 0.713  0.6469 0.6775 -0.009  0.0638  0.0265  238 PRO   A N     
1675 C  CA    . PRO   A 238 ? 0.7007 0.6542 0.6795 -0.008  0.0547  0.025   238 PRO   A CA    
1676 C  C     . PRO   A 238 ? 0.687  0.6487 0.676  -0.0064 0.0578  0.0252  238 PRO   A C     
1677 O  O     . PRO   A 238 ? 0.6829 0.661  0.6883 -0.0047 0.0536  0.0246  238 PRO   A O     
1678 C  CB    . PRO   A 238 ? 0.7178 0.668  0.6829 -0.0107 0.0458  0.0245  238 PRO   A CB    
1679 C  CG    . PRO   A 238 ? 0.7375 0.6657 0.6793 -0.0137 0.0503  0.0256  238 PRO   A CG    
1680 C  CD    . PRO   A 238 ? 0.7198 0.6374 0.6596 -0.0127 0.0601  0.0267  238 PRO   A CD    
1681 N  N     . LEU   A 239 ? 0.6706 0.6198 0.6493 -0.007  0.0651  0.0262  239 LEU   A N     
1682 C  CA    . LEU   A 239 ? 0.6542 0.61   0.6436 -0.0051 0.0686  0.0273  239 LEU   A CA    
1683 C  C     . LEU   A 239 ? 0.6429 0.6089 0.6549 -0.0019 0.0732  0.0291  239 LEU   A C     
1684 O  O     . LEU   A 239 ? 0.6285 0.608  0.6557 -0.0003 0.0702  0.0301  239 LEU   A O     
1685 C  CB    . LEU   A 239 ? 0.6599 0.5975 0.6339 -0.006  0.0775  0.028   239 LEU   A CB    
1686 C  CG    . LEU   A 239 ? 0.6837 0.6131 0.6385 -0.0097 0.0718  0.0265  239 LEU   A CG    
1687 C  CD1   . LEU   A 239 ? 0.7025 0.6098 0.6391 -0.0111 0.0817  0.0266  239 LEU   A CD1   
1688 C  CD2   . LEU   A 239 ? 0.6708 0.6174 0.6365 -0.0094 0.0634  0.0263  239 LEU   A CD2   
1689 N  N     . ASP   A 240 ? 0.6397 0.5987 0.6536 -0.0015 0.0797  0.03    240 ASP   A N     
1690 C  CA    . ASP   A 240 ? 0.6348 0.6028 0.6714 0.0007  0.0835  0.0322  240 ASP   A CA    
1691 C  C     . ASP   A 240 ? 0.626  0.6126 0.6777 0.0007  0.0724  0.0308  240 ASP   A C     
1692 O  O     . ASP   A 240 ? 0.6257 0.6227 0.6978 0.0019  0.0724  0.0328  240 ASP   A O     
1693 C  CB    . ASP   A 240 ? 0.6563 0.6114 0.6905 0.0006  0.0935  0.0335  240 ASP   A CB    
1694 C  CG    . ASP   A 240 ? 0.7089 0.6455 0.7328 0.0013  0.1078  0.0353  240 ASP   A CG    
1695 O  OD1   . ASP   A 240 ? 0.703  0.6389 0.728  0.0026  0.111   0.0361  240 ASP   A OD1   
1696 O  OD2   . ASP   A 240 ? 0.763  0.6847 0.7771 0.0005  0.1166  0.0359  240 ASP   A OD2   
1697 N  N     . TYR   A 241 ? 0.622  0.6121 0.6645 -0.0008 0.0632  0.0278  241 TYR   A N     
1698 C  CA    . TYR   A 241 ? 0.6285 0.6342 0.6829 -0.0007 0.054   0.026   241 TYR   A CA    
1699 C  C     . TYR   A 241 ? 0.6114 0.6262 0.6659 -0.0005 0.0484  0.0255  241 TYR   A C     
1700 O  O     . TYR   A 241 ? 0.6121 0.6381 0.6796 0       0.0447  0.0261  241 TYR   A O     
1701 C  CB    . TYR   A 241 ? 0.6523 0.6582 0.7006 -0.0017 0.048   0.023   241 TYR   A CB    
1702 C  CG    . TYR   A 241 ? 0.6836 0.7034 0.7423 -0.0016 0.04    0.0205  241 TYR   A CG    
1703 C  CD1   . TYR   A 241 ? 0.6923 0.718  0.7658 -0.0018 0.0391  0.0206  241 TYR   A CD1   
1704 C  CD2   . TYR   A 241 ? 0.7068 0.7332 0.7604 -0.0017 0.034   0.0184  241 TYR   A CD2   
1705 C  CE1   . TYR   A 241 ? 0.7021 0.7377 0.7815 -0.0024 0.0316  0.0179  241 TYR   A CE1   
1706 C  CE2   . TYR   A 241 ? 0.7181 0.7545 0.778  -0.0018 0.028   0.0158  241 TYR   A CE2   
1707 C  CZ    . TYR   A 241 ? 0.7252 0.7653 0.7964 -0.0023 0.0266  0.0153  241 TYR   A CZ    
1708 O  OH    . TYR   A 241 ? 0.7516 0.7989 0.8257 -0.0031 0.0205  0.0123  241 TYR   A OH    
1709 N  N     . ILE   A 242 ? 0.5827 0.5927 0.6226 -0.0014 0.0471  0.0246  242 ILE   A N     
1710 C  CA    . ILE   A 242 ? 0.5573 0.5754 0.5963 -0.0016 0.042   0.0241  242 ILE   A CA    
1711 C  C     . ILE   A 242 ? 0.5466 0.5681 0.5938 -0.0003 0.0447  0.0271  242 ILE   A C     
1712 O  O     . ILE   A 242 ? 0.5408 0.5734 0.5958 0       0.0395  0.0274  242 ILE   A O     
1713 C  CB    . ILE   A 242 ? 0.5527 0.564  0.5759 -0.0034 0.0402  0.0231  242 ILE   A CB    
1714 C  CG1   . ILE   A 242 ? 0.5474 0.5576 0.566  -0.0043 0.0358  0.021   242 ILE   A CG1   
1715 C  CG2   . ILE   A 242 ? 0.5412 0.5607 0.5647 -0.0038 0.0362  0.0231  242 ILE   A CG2   
1716 C  CD1   . ILE   A 242 ? 0.5602 0.5605 0.564  -0.0067 0.0339  0.0213  242 ILE   A CD1   
1717 N  N     . LEU   A 243 ? 0.5438 0.5548 0.5886 0.0004  0.053   0.0295  243 LEU   A N     
1718 C  CA    . LEU   A 243 ? 0.5442 0.5575 0.5979 0.0021  0.0562  0.033   243 LEU   A CA    
1719 C  C     . LEU   A 243 ? 0.5252 0.5515 0.5997 0.0036  0.0529  0.0356  243 LEU   A C     
1720 O  O     . LEU   A 243 ? 0.5174 0.5521 0.5958 0.0038  0.0475  0.0371  243 LEU   A O     
1721 C  CB    . LEU   A 243 ? 0.5559 0.5539 0.6047 0.0031  0.0677  0.035   243 LEU   A CB    
1722 C  CG    . LEU   A 243 ? 0.5855 0.5689 0.6119 0.0008  0.0698  0.0329  243 LEU   A CG    
1723 C  CD1   . LEU   A 243 ? 0.603  0.568  0.622  0.0015  0.0825  0.0342  243 LEU   A CD1   
1724 C  CD2   . LEU   A 243 ? 0.5814 0.5701 0.6035 -0.0003 0.0638  0.0328  243 LEU   A CD2   
1725 N  N     . PRO   A 244 ? 0.5149 0.5428 0.6024 0.0042  0.0551  0.0367  244 PRO   A N     
1726 C  CA    . PRO   A 244 ? 0.5009 0.5415 0.6088 0.0046  0.0498  0.0396  244 PRO   A CA    
1727 C  C     . PRO   A 244 ? 0.5035 0.5544 0.6082 0.0027  0.038   0.0369  244 PRO   A C     
1728 O  O     . PRO   A 244 ? 0.5118 0.5714 0.6258 0.0026  0.0319  0.0395  244 PRO   A O     
1729 C  CB    . PRO   A 244 ? 0.5089 0.5479 0.6291 0.0046  0.0542  0.0404  244 PRO   A CB    
1730 C  CG    . PRO   A 244 ? 0.5233 0.5512 0.626  0.0036  0.0582  0.0364  244 PRO   A CG    
1731 C  CD    . PRO   A 244 ? 0.5144 0.5326 0.599  0.0039  0.062   0.0357  244 PRO   A CD    
1732 N  N     . GLU   A 245 ? 0.4953 0.5442 0.586  0.0012  0.0352  0.0319  245 GLU   A N     
1733 C  CA    . GLU   A 245 ? 0.4885 0.545  0.5745 -0.0003 0.0264  0.0288  245 GLU   A CA    
1734 C  C     . GLU   A 245 ? 0.501  0.5609 0.5806 -0.0002 0.0235  0.03    245 GLU   A C     
1735 O  O     . GLU   A 245 ? 0.5037 0.5706 0.5858 -0.0012 0.0168  0.0307  245 GLU   A O     
1736 C  CB    . GLU   A 245 ? 0.5009 0.5541 0.576  -0.0011 0.0255  0.0238  245 GLU   A CB    
1737 C  CG    . GLU   A 245 ? 0.5374 0.5888 0.6194 -0.0016 0.0262  0.0225  245 GLU   A CG    
1738 C  CD    . GLU   A 245 ? 0.6151 0.6737 0.7105 -0.0029 0.0207  0.0229  245 GLU   A CD    
1739 O  OE1   . GLU   A 245 ? 0.5799 0.6444 0.6729 -0.0041 0.0136  0.0214  245 GLU   A OE1   
1740 O  OE2   . GLU   A 245 ? 0.6733 0.7307 0.7811 -0.0031 0.0235  0.0249  245 GLU   A OE2   
1741 N  N     . LEU   A 246 ? 0.5014 0.555  0.5716 0.0003  0.0283  0.0305  246 LEU   A N     
1742 C  CA    . LEU   A 246 ? 0.5068 0.5627 0.5711 0.0002  0.0264  0.032   246 LEU   A CA    
1743 C  C     . LEU   A 246 ? 0.5018 0.5602 0.5769 0.0015  0.0266  0.0376  246 LEU   A C     
1744 O  O     . LEU   A 246 ? 0.5016 0.5646 0.5745 0.0011  0.0222  0.0394  246 LEU   A O     
1745 C  CB    . LEU   A 246 ? 0.5113 0.5592 0.5629 -0.0004 0.0306  0.0309  246 LEU   A CB    
1746 C  CG    . LEU   A 246 ? 0.522  0.5676 0.5649 -0.0017 0.0295  0.0266  246 LEU   A CG    
1747 C  CD1   . LEU   A 246 ? 0.5308 0.5685 0.5624 -0.0031 0.0319  0.0265  246 LEU   A CD1   
1748 C  CD2   . LEU   A 246 ? 0.5229 0.5772 0.5648 -0.0024 0.0237  0.0238  246 LEU   A CD2   
1749 N  N     . LEU   A 247 ? 0.4889 0.544  0.5762 0.0033  0.0322  0.0407  247 LEU   A N     
1750 C  CA    . LEU   A 247 ? 0.486  0.5438 0.5882 0.0053  0.0331  0.0469  247 LEU   A CA    
1751 C  C     . LEU   A 247 ? 0.4889 0.5579 0.6039 0.0043  0.0233  0.0493  247 LEU   A C     
1752 O  O     . LEU   A 247 ? 0.4922 0.566  0.6122 0.0045  0.0183  0.0538  247 LEU   A O     
1753 C  CB    . LEU   A 247 ? 0.4836 0.5338 0.5962 0.0077  0.0437  0.0495  247 LEU   A CB    
1754 C  CG    . LEU   A 247 ? 0.511  0.5473 0.61   0.0085  0.0535  0.0485  247 LEU   A CG    
1755 C  CD1   . LEU   A 247 ? 0.5112 0.5371 0.6153 0.0102  0.0651  0.0494  247 LEU   A CD1   
1756 C  CD2   . LEU   A 247 ? 0.5193 0.5546 0.6192 0.0099  0.0545  0.0526  247 LEU   A CD2   
1757 N  N     . LYS   A 248 ? 0.4832 0.5553 0.6022 0.0027  0.0199  0.0464  248 LYS   A N     
1758 C  CA    . LYS   A 248 ? 0.4789 0.5598 0.6074 0.0006  0.0094  0.0479  248 LYS   A CA    
1759 C  C     . LYS   A 248 ? 0.4934 0.577  0.6064 -0.0016 0.0009  0.0461  248 LYS   A C     
1760 O  O     . LYS   A 248 ? 0.5052 0.594  0.6234 -0.0028 -0.0075 0.0501  248 LYS   A O     
1761 C  CB    . LYS   A 248 ? 0.4939 0.5751 0.6255 -0.0013 0.0079  0.0438  248 LYS   A CB    
1762 C  CG    . LYS   A 248 ? 0.538  0.6201 0.6921 -0.0003 0.0126  0.0478  248 LYS   A CG    
1763 C  CD    . LYS   A 248 ? 0.5907 0.6679 0.7433 -0.001  0.0173  0.0433  248 LYS   A CD    
1764 C  CE    . LYS   A 248 ? 0.6338 0.7121 0.7749 -0.0041 0.0096  0.0372  248 LYS   A CE    
1765 N  NZ    . LYS   A 248 ? 0.6709 0.744  0.8125 -0.0045 0.0144  0.034   248 LYS   A NZ    
1766 N  N     . ASN   A 249 ? 0.4866 0.5663 0.581  -0.0021 0.0033  0.0407  249 ASN   A N     
1767 C  CA    . ASN   A 249 ? 0.491  0.572  0.57   -0.0038 -0.002  0.0387  249 ASN   A CA    
1768 C  C     . ASN   A 249 ? 0.4964 0.5781 0.5741 -0.003  -0.0028 0.0443  249 ASN   A C     
1769 O  O     . ASN   A 249 ? 0.5042 0.5885 0.5765 -0.0049 -0.0103 0.0461  249 ASN   A O     
1770 C  CB    . ASN   A 249 ? 0.5011 0.5784 0.5652 -0.004  0.0025  0.0328  249 ASN   A CB    
1771 C  CG    . ASN   A 249 ? 0.518  0.5946 0.5805 -0.0049 0.0018  0.0272  249 ASN   A CG    
1772 O  OD1   . ASN   A 249 ? 0.5203 0.5987 0.5908 -0.0061 -0.0025 0.027   249 ASN   A OD1   
1773 N  ND2   . ASN   A 249 ? 0.5072 0.581  0.5607 -0.0045 0.0058  0.023   249 ASN   A ND2   
1774 N  N     . ALA   A 250 ? 0.4912 0.5689 0.5716 -0.0006 0.005   0.0467  250 ALA   A N     
1775 C  CA    . ALA   A 250 ? 0.4989 0.5757 0.5784 0.0004  0.0054  0.052   250 ALA   A CA    
1776 C  C     . ALA   A 250 ? 0.5054 0.587  0.6008 0.0011  -0.0005 0.0592  250 ALA   A C     
1777 O  O     . ALA   A 250 ? 0.5138 0.5974 0.605  0.0003  -0.0066 0.0631  250 ALA   A O     
1778 C  CB    . ALA   A 250 ? 0.4991 0.5684 0.5783 0.0025  0.0155  0.0525  250 ALA   A CB    
1779 N  N     . MET   A 251 ? 0.4997 0.5835 0.614  0.0025  0.0007  0.0614  251 MET   A N     
1780 C  CA    . MET   A 251 ? 0.5009 0.5907 0.6357 0.0032  -0.0053 0.0692  251 MET   A CA    
1781 C  C     . MET   A 251 ? 0.5009 0.5967 0.6329 -0.0007 -0.0195 0.0698  251 MET   A C     
1782 O  O     . MET   A 251 ? 0.5029 0.6021 0.6405 -0.0011 -0.0275 0.0765  251 MET   A O     
1783 C  CB    . MET   A 251 ? 0.4989 0.5894 0.6559 0.0054  0.0009  0.0711  251 MET   A CB    
1784 C  CG    . MET   A 251 ? 0.5369 0.619  0.6956 0.0092  0.015   0.0716  251 MET   A CG    
1785 S  SD    . MET   A 251 ? 0.598  0.6795 0.7847 0.0126  0.0249  0.0759  251 MET   A SD    
1786 C  CE    . MET   A 251 ? 0.6326 0.6994 0.8088 0.016   0.0409  0.0749  251 MET   A CE    
1787 N  N     . ARG   A 252 ? 0.4997 0.5954 0.6216 -0.0037 -0.0228 0.0629  252 ARG   A N     
1788 C  CA    . ARG   A 252 ? 0.5146 0.6129 0.6293 -0.0081 -0.0357 0.0623  252 ARG   A CA    
1789 C  C     . ARG   A 252 ? 0.5143 0.6096 0.6074 -0.0097 -0.0398 0.0625  252 ARG   A C     
1790 O  O     . ARG   A 252 ? 0.5102 0.607  0.6019 -0.0121 -0.0508 0.0674  252 ARG   A O     
1791 C  CB    . ARG   A 252 ? 0.5558 0.6521 0.6621 -0.0106 -0.0359 0.0539  252 ARG   A CB    
1792 C  CG    . ARG   A 252 ? 0.6402 0.7355 0.733  -0.0157 -0.048  0.0512  252 ARG   A CG    
1793 C  CD    . ARG   A 252 ? 0.7484 0.8413 0.838  -0.0179 -0.0477 0.0435  252 ARG   A CD    
1794 N  NE    . ARG   A 252 ? 0.8584 0.9516 0.9602 -0.0145 -0.0368 0.0417  252 ARG   A NE    
1795 C  CZ    . ARG   A 252 ? 0.9327 1.0247 1.0396 -0.0155 -0.0352 0.0374  252 ARG   A CZ    
1796 N  NH1   . ARG   A 252 ? 0.9488 1.0393 1.0505 -0.0198 -0.0437 0.0337  252 ARG   A NH1   
1797 N  NH2   . ARG   A 252 ? 0.9445 1.0354 1.0601 -0.0124 -0.025  0.0366  252 ARG   A NH2   
1798 N  N     . ALA   A 253 ? 0.5171 0.6076 0.5934 -0.0085 -0.0314 0.0579  253 ALA   A N     
1799 C  CA    . ALA   A 253 ? 0.5181 0.6054 0.5743 -0.0099 -0.0333 0.0582  253 ALA   A CA    
1800 C  C     . ALA   A 253 ? 0.5204 0.6088 0.5837 -0.0086 -0.0366 0.0675  253 ALA   A C     
1801 O  O     . ALA   A 253 ? 0.5308 0.6176 0.5819 -0.011  -0.0443 0.0708  253 ALA   A O     
1802 C  CB    . ALA   A 253 ? 0.5107 0.5943 0.5546 -0.0086 -0.0227 0.053   253 ALA   A CB    
1803 N  N     . THR   A 254 ? 0.5051 0.595  0.5876 -0.0047 -0.0303 0.072   254 THR   A N     
1804 C  CA    . THR   A 254 ? 0.5047 0.5952 0.5971 -0.0027 -0.0323 0.0812  254 THR   A CA    
1805 C  C     . THR   A 254 ? 0.5126 0.6085 0.6171 -0.0046 -0.046  0.0881  254 THR   A C     
1806 O  O     . THR   A 254 ? 0.5222 0.6174 0.6206 -0.0058 -0.054  0.0942  254 THR   A O     
1807 C  CB    . THR   A 254 ? 0.5071 0.5962 0.6172 0.002   -0.0212 0.0837  254 THR   A CB    
1808 O  OG1   . THR   A 254 ? 0.5206 0.6035 0.6172 0.0026  -0.0103 0.0772  254 THR   A OG1   
1809 C  CG2   . THR   A 254 ? 0.508  0.597  0.6304 0.0048  -0.0221 0.0935  254 THR   A CG2   
1810 N  N     . MET   A 255 ? 0.5148 0.6157 0.6361 -0.0053 -0.0497 0.0876  255 MET   A N     
1811 C  CA    . MET   A 255 ? 0.5197 0.6265 0.6558 -0.0077 -0.0641 0.0947  255 MET   A CA    
1812 C  C     . MET   A 255 ? 0.5469 0.6505 0.6589 -0.0137 -0.0775 0.0929  255 MET   A C     
1813 O  O     . MET   A 255 ? 0.5467 0.6511 0.6592 -0.0157 -0.0896 0.1007  255 MET   A O     
1814 C  CB    . MET   A 255 ? 0.5091 0.6219 0.6698 -0.0077 -0.0643 0.0943  255 MET   A CB    
1815 C  CG    . MET   A 255 ? 0.5151 0.6296 0.7004 -0.0019 -0.0507 0.0971  255 MET   A CG    
1816 S  SD    . MET   A 255 ? 0.5414 0.6561 0.7441 0.0037  -0.046  0.1081  255 MET   A SD    
1817 C  CE    . MET   A 255 ? 0.4955 0.6206 0.7244 0.0015  -0.065  0.1204  255 MET   A CE    
1818 N  N     . GLU   A 256 ? 0.5667 0.6654 0.6566 -0.0165 -0.075  0.0828  256 GLU   A N     
1819 C  CA    . GLU   A 256 ? 0.5904 0.6831 0.6537 -0.0223 -0.0853 0.0794  256 GLU   A CA    
1820 C  C     . GLU   A 256 ? 0.614  0.7005 0.6545 -0.0231 -0.0867 0.0825  256 GLU   A C     
1821 O  O     . GLU   A 256 ? 0.6379 0.7183 0.657  -0.0281 -0.0971 0.0825  256 GLU   A O     
1822 C  CB    . GLU   A 256 ? 0.6217 0.7097 0.6683 -0.024  -0.0793 0.0677  256 GLU   A CB    
1823 C  CG    . GLU   A 256 ? 0.6941 0.7861 0.7579 -0.0248 -0.0804 0.0642  256 GLU   A CG    
1824 C  CD    . GLU   A 256 ? 0.8452 0.9384 0.9149 -0.0303 -0.0966 0.0671  256 GLU   A CD    
1825 O  OE1   . GLU   A 256 ? 0.8934 0.9831 0.9499 -0.0343 -0.1089 0.0713  256 GLU   A OE1   
1826 O  OE2   . GLU   A 256 ? 0.8895 0.9867 0.977  -0.031  -0.0973 0.0653  256 GLU   A OE2   
1827 N  N     . SER   A 257 ? 0.6061 0.6926 0.6487 -0.0186 -0.0758 0.0845  257 SER   A N     
1828 C  CA    . SER   A 257 ? 0.6235 0.704  0.646  -0.0193 -0.0758 0.0879  257 SER   A CA    
1829 C  C     . SER   A 257 ? 0.6325 0.7156 0.6701 -0.0173 -0.0818 0.1     257 SER   A C     
1830 O  O     . SER   A 257 ? 0.6442 0.7224 0.6684 -0.017  -0.0804 0.1039  257 SER   A O     
1831 C  CB    . SER   A 257 ? 0.6256 0.703  0.6381 -0.0166 -0.0604 0.0822  257 SER   A CB    
1832 O  OG    . SER   A 257 ? 0.6355 0.7172 0.6703 -0.0117 -0.0515 0.0842  257 SER   A OG    
1833 N  N     . HIS   A 258 ? 0.6221 0.7129 0.6891 -0.0156 -0.0877 0.1064  258 HIS   A N     
1834 C  CA    . HIS   A 258 ? 0.6186 0.7127 0.7049 -0.013  -0.0934 0.1187  258 HIS   A CA    
1835 C  C     . HIS   A 258 ? 0.6301 0.7312 0.7375 -0.0154 -0.1091 0.1253  258 HIS   A C     
1836 O  O     . HIS   A 258 ? 0.6201 0.7284 0.7593 -0.0116 -0.1098 0.1338  258 HIS   A O     
1837 C  CB    . HIS   A 258 ? 0.6016 0.6983 0.7104 -0.0062 -0.0787 0.1205  258 HIS   A CB    
1838 C  CG    . HIS   A 258 ? 0.6138 0.7034 0.7041 -0.0045 -0.0654 0.1157  258 HIS   A CG    
1839 N  ND1   . HIS   A 258 ? 0.6319 0.7191 0.7113 -0.0045 -0.0542 0.105   258 HIS   A ND1   
1840 C  CD2   . HIS   A 258 ? 0.6197 0.7042 0.7019 -0.0031 -0.0626 0.1209  258 HIS   A CD2   
1841 C  CE1   . HIS   A 258 ? 0.6414 0.7229 0.7072 -0.0035 -0.0457 0.104   258 HIS   A CE1   
1842 N  NE2   . HIS   A 258 ? 0.6391 0.7185 0.7057 -0.0027 -0.05   0.1131  258 HIS   A NE2   
1843 N  N     . LEU   A 259 ? 0.6482 0.7465 0.738  -0.022  -0.1217 0.1217  259 LEU   A N     
1844 C  CA    . LEU   A 259 ? 0.6651 0.7693 0.7728 -0.0259 -0.1384 0.1272  259 LEU   A CA    
1845 C  C     . LEU   A 259 ? 0.686  0.7936 0.8088 -0.0262 -0.1534 0.1419  259 LEU   A C     
1846 O  O     . LEU   A 259 ? 0.6783 0.7948 0.8307 -0.027  -0.1641 0.149   259 LEU   A O     
1847 C  CB    . LEU   A 259 ? 0.6796 0.7768 0.7601 -0.0336 -0.1483 0.1192  259 LEU   A CB    
1848 C  CG    . LEU   A 259 ? 0.7065 0.8023 0.7806 -0.0332 -0.1359 0.1061  259 LEU   A CG    
1849 C  CD1   . LEU   A 259 ? 0.7314 0.8171 0.7734 -0.0404 -0.1437 0.0977  259 LEU   A CD1   
1850 C  CD2   . LEU   A 259 ? 0.6918 0.7984 0.8025 -0.0306 -0.1327 0.1068  259 LEU   A CD2   
1851 N  N     . ASP   A 260 ? 0.7112 0.8121 0.8162 -0.0254 -0.154  0.147   260 ASP   A N     
1852 C  CA    . ASP   A 260 ? 0.7293 0.8326 0.8481 -0.0252 -0.1678 0.1617  260 ASP   A CA    
1853 C  C     . ASP   A 260 ? 0.7114 0.8241 0.8711 -0.0168 -0.1584 0.1703  260 ASP   A C     
1854 O  O     . ASP   A 260 ? 0.7136 0.8321 0.8982 -0.0156 -0.1701 0.1835  260 ASP   A O     
1855 C  CB    . ASP   A 260 ? 0.8009 0.8924 0.8851 -0.0271 -0.1701 0.1644  260 ASP   A CB    
1856 C  CG    . ASP   A 260 ? 0.9563 1.0356 0.9974 -0.0354 -0.1795 0.1579  260 ASP   A CG    
1857 O  OD1   . ASP   A 260 ? 0.9876 1.0674 1.027  -0.0411 -0.1914 0.1547  260 ASP   A OD1   
1858 O  OD2   . ASP   A 260 ? 1.0224 1.0906 1.0311 -0.0365 -0.1746 0.1562  260 ASP   A OD2   
1859 N  N     . THR   A 261 ? 0.6889 0.8016 0.8543 -0.011  -0.1375 0.1633  261 THR   A N     
1860 C  CA    . THR   A 261 ? 0.6608 0.7789 0.8602 -0.0031 -0.126  0.1698  261 THR   A CA    
1861 C  C     . THR   A 261 ? 0.6407 0.7629 0.8577 0.0003  -0.1104 0.1615  261 THR   A C     
1862 O  O     . THR   A 261 ? 0.6484 0.766  0.8623 0.0048  -0.0927 0.1565  261 THR   A O     
1863 C  CB    . THR   A 261 ? 0.6764 0.7861 0.8614 0.0007  -0.1154 0.1716  261 THR   A CB    
1864 O  OG1   . THR   A 261 ? 0.7004 0.8028 0.8575 0       -0.1015 0.1588  261 THR   A OG1   
1865 C  CG2   . THR   A 261 ? 0.685  0.7896 0.8524 -0.0025 -0.13   0.1806  261 THR   A CG2   
1866 N  N     . PRO   A 262 ? 0.6172 0.747  0.851  -0.0023 -0.1166 0.1599  262 PRO   A N     
1867 C  CA    . PRO   A 262 ? 0.5971 0.7293 0.8452 0.0007  -0.1011 0.1522  262 PRO   A CA    
1868 C  C     . PRO   A 262 ? 0.5786 0.7135 0.8591 0.0086  -0.0863 0.1579  262 PRO   A C     
1869 O  O     . PRO   A 262 ? 0.5769 0.7091 0.8601 0.0117  -0.0699 0.1509  262 PRO   A O     
1870 C  CB    . PRO   A 262 ? 0.5985 0.7382 0.8596 -0.0044 -0.1134 0.1516  262 PRO   A CB    
1871 C  CG    . PRO   A 262 ? 0.6049 0.7493 0.8758 -0.0079 -0.1346 0.1633  262 PRO   A CG    
1872 C  CD    . PRO   A 262 ? 0.6047 0.7402 0.8457 -0.0085 -0.1382 0.1655  262 PRO   A CD    
1873 N  N     . TYR   A 263 ? 0.5648 0.7034 0.868  0.0119  -0.0917 0.1708  263 TYR   A N     
1874 C  CA    . TYR   A 263 ? 0.5583 0.698  0.8933 0.0199  -0.078  0.1778  263 TYR   A CA    
1875 C  C     . TYR   A 263 ? 0.5636 0.6911 0.8795 0.0244  -0.0612 0.1739  263 TYR   A C     
1876 O  O     . TYR   A 263 ? 0.5634 0.6881 0.9002 0.031   -0.0465 0.1773  263 TYR   A O     
1877 C  CB    . TYR   A 263 ? 0.548  0.6963 0.9156 0.0218  -0.0917 0.1942  263 TYR   A CB    
1878 C  CG    . TYR   A 263 ? 0.5731 0.7186 0.9175 0.0173  -0.1101 0.1996  263 TYR   A CG    
1879 C  CD1   . TYR   A 263 ? 0.5936 0.7292 0.9165 0.0195  -0.1045 0.2004  263 TYR   A CD1   
1880 C  CD2   . TYR   A 263 ? 0.5887 0.7396 0.9283 0.0099  -0.1326 0.2028  263 TYR   A CD2   
1881 C  CE1   . TYR   A 263 ? 0.6183 0.7495 0.9161 0.015   -0.12   0.2048  263 TYR   A CE1   
1882 C  CE2   . TYR   A 263 ? 0.6117 0.7571 0.9243 0.0051  -0.1488 0.207   263 TYR   A CE2   
1883 C  CZ    . TYR   A 263 ? 0.6351 0.7708 0.9265 0.0078  -0.1419 0.208   263 TYR   A CZ    
1884 O  OH    . TYR   A 263 ? 0.6712 0.8004 0.935  0.0031  -0.157  0.2126  263 TYR   A OH    
1885 N  N     . ASN   A 264 ? 0.5627 0.6824 0.8402 0.0206  -0.0635 0.1674  264 ASN   A N     
1886 C  CA    . ASN   A 264 ? 0.569  0.6774 0.8286 0.0236  -0.0498 0.1641  264 ASN   A CA    
1887 C  C     . ASN   A 264 ? 0.5769 0.6792 0.7977 0.0185  -0.0487 0.1523  264 ASN   A C     
1888 O  O     . ASN   A 264 ? 0.5978 0.6978 0.7954 0.0145  -0.0588 0.153   264 ASN   A O     
1889 C  CB    . ASN   A 264 ? 0.5832 0.6892 0.8454 0.0256  -0.056  0.1754  264 ASN   A CB    
1890 C  CG    . ASN   A 264 ? 0.6454 0.7391 0.8915 0.0285  -0.0421 0.173   264 ASN   A CG    
1891 O  OD1   . ASN   A 264 ? 0.6713 0.7581 0.9087 0.0299  -0.0263 0.1638  264 ASN   A OD1   
1892 N  ND2   . ASN   A 264 ? 0.6454 0.7356 0.8869 0.0291  -0.0482 0.1817  264 ASN   A ND2   
1893 N  N     . VAL   A 265 ? 0.5591 0.6585 0.7732 0.0187  -0.0367 0.1418  265 VAL   A N     
1894 C  CA    . VAL   A 265 ? 0.5581 0.6525 0.7394 0.0145  -0.0343 0.1306  265 VAL   A CA    
1895 C  C     . VAL   A 265 ? 0.555  0.6393 0.726  0.0171  -0.0175 0.125   265 VAL   A C     
1896 O  O     . VAL   A 265 ? 0.5523 0.6332 0.7408 0.0218  -0.0062 0.1269  265 VAL   A O     
1897 C  CB    . VAL   A 265 ? 0.5589 0.6584 0.7397 0.0112  -0.0373 0.1231  265 VAL   A CB    
1898 C  CG1   . VAL   A 265 ? 0.5568 0.6645 0.7458 0.0075  -0.0551 0.1283  265 VAL   A CG1   
1899 C  CG2   . VAL   A 265 ? 0.5579 0.6577 0.7596 0.015   -0.0248 0.1208  265 VAL   A CG2   
1900 N  N     . PRO   A 266 ? 0.5516 0.6304 0.6943 0.014   -0.0155 0.1181  266 PRO   A N     
1901 C  CA    . PRO   A 266 ? 0.5457 0.6149 0.6787 0.0155  -0.0014 0.113   266 PRO   A CA    
1902 C  C     . PRO   A 266 ? 0.5415 0.6083 0.68   0.0167  0.0089  0.1059  266 PRO   A C     
1903 O  O     . PRO   A 266 ? 0.5394 0.6119 0.6803 0.0151  0.0054  0.1018  266 PRO   A O     
1904 C  CB    . PRO   A 266 ? 0.5634 0.6299 0.6681 0.011   -0.0034 0.1074  266 PRO   A CB    
1905 C  CG    . PRO   A 266 ? 0.573  0.6457 0.6703 0.0077  -0.0171 0.1098  266 PRO   A CG    
1906 C  CD    . PRO   A 266 ? 0.5479 0.6283 0.6668 0.0087  -0.0253 0.1147  266 PRO   A CD    
1907 N  N     . ASP   A 267 ? 0.5403 0.597  0.6799 0.0195  0.0218  0.1048  267 ASP   A N     
1908 C  CA    . ASP   A 267 ? 0.5409 0.5921 0.6815 0.0203  0.0324  0.0983  267 ASP   A CA    
1909 C  C     . ASP   A 267 ? 0.5442 0.5943 0.6624 0.016   0.0317  0.0887  267 ASP   A C     
1910 O  O     . ASP   A 267 ? 0.5541 0.6045 0.6551 0.0129  0.0275  0.0866  267 ASP   A O     
1911 C  CB    . ASP   A 267 ? 0.5757 0.6127 0.7154 0.0232  0.046   0.0986  267 ASP   A CB    
1912 C  CG    . ASP   A 267 ? 0.6513 0.6862 0.8143 0.0285  0.0506  0.1077  267 ASP   A CG    
1913 O  OD1   . ASP   A 267 ? 0.6524 0.6983 0.8376 0.0305  0.0437  0.1143  267 ASP   A OD1   
1914 O  OD2   . ASP   A 267 ? 0.6876 0.7098 0.8475 0.0306  0.0607  0.1084  267 ASP   A OD2   
1915 N  N     . VAL   A 268 ? 0.5253 0.5739 0.645  0.0159  0.0367  0.0834  268 VAL   A N     
1916 C  CA    . VAL   A 268 ? 0.5235 0.5694 0.6248 0.0126  0.0378  0.0748  268 VAL   A CA    
1917 C  C     . VAL   A 268 ? 0.5321 0.5633 0.6249 0.0132  0.0494  0.0723  268 VAL   A C     
1918 O  O     . VAL   A 268 ? 0.5353 0.5591 0.6386 0.0164  0.0584  0.0744  268 VAL   A O     
1919 C  CB    . VAL   A 268 ? 0.5193 0.5706 0.6268 0.012   0.036   0.0712  268 VAL   A CB    
1920 C  CG1   . VAL   A 268 ? 0.5298 0.5756 0.6205 0.0095  0.0393  0.0632  268 VAL   A CG1   
1921 C  CG2   . VAL   A 268 ? 0.5101 0.5737 0.6221 0.0103  0.0236  0.0728  268 VAL   A CG2   
1922 N  N     . VAL   A 269 ? 0.5306 0.5566 0.6049 0.01    0.0495  0.0683  269 VAL   A N     
1923 C  CA    . VAL   A 269 ? 0.5319 0.5427 0.5952 0.0093  0.0585  0.0658  269 VAL   A CA    
1924 C  C     . VAL   A 269 ? 0.5466 0.5523 0.5953 0.0059  0.0596  0.0586  269 VAL   A C     
1925 O  O     . VAL   A 269 ? 0.5533 0.565  0.5929 0.0026  0.0533  0.0555  269 VAL   A O     
1926 C  CB    . VAL   A 269 ? 0.5327 0.5392 0.588  0.0078  0.0581  0.0682  269 VAL   A CB    
1927 C  CG1   . VAL   A 269 ? 0.5457 0.5341 0.5894 0.0065  0.0672  0.0656  269 VAL   A CG1   
1928 C  CG2   . VAL   A 269 ? 0.522  0.5336 0.5915 0.0111  0.0558  0.0763  269 VAL   A CG2   
1929 N  N     . ILE   A 270 ? 0.551  0.5442 0.5967 0.0066  0.0681  0.0564  270 ILE   A N     
1930 C  CA    . ILE   A 270 ? 0.5606 0.5465 0.5913 0.0033  0.0689  0.0503  270 ILE   A CA    
1931 C  C     . ILE   A 270 ? 0.5717 0.5394 0.5851 0.0004  0.0745  0.048   270 ILE   A C     
1932 O  O     . ILE   A 270 ? 0.5793 0.5334 0.5923 0.0023  0.0837  0.0496  270 ILE   A O     
1933 C  CB    . ILE   A 270 ? 0.5664 0.551  0.6036 0.0053  0.0733  0.0492  270 ILE   A CB    
1934 C  CG1   . ILE   A 270 ? 0.5648 0.5672 0.6193 0.0073  0.0663  0.0514  270 ILE   A CG1   
1935 C  CG2   . ILE   A 270 ? 0.5793 0.5548 0.5994 0.0018  0.0736  0.0436  270 ILE   A CG2   
1936 C  CD1   . ILE   A 270 ? 0.5824 0.5854 0.6464 0.0089  0.0699  0.0508  270 ILE   A CD1   
1937 N  N     . THR   A 271 ? 0.5688 0.5354 0.5681 -0.0044 0.0688  0.0443  271 THR   A N     
1938 C  CA    . THR   A 271 ? 0.577  0.5258 0.5585 -0.0086 0.0718  0.0419  271 THR   A CA    
1939 C  C     . THR   A 271 ? 0.5776 0.5183 0.5453 -0.0119 0.0704  0.0373  271 THR   A C     
1940 O  O     . THR   A 271 ? 0.5673 0.5201 0.5375 -0.0131 0.0629  0.0359  271 THR   A O     
1941 C  CB    . THR   A 271 ? 0.5932 0.5468 0.5712 -0.0123 0.0655  0.0426  271 THR   A CB    
1942 O  OG1   . THR   A 271 ? 0.5993 0.5594 0.5886 -0.0092 0.0666  0.0474  271 THR   A OG1   
1943 C  CG2   . THR   A 271 ? 0.6052 0.5406 0.5648 -0.0179 0.0665  0.0399  271 THR   A CG2   
1944 N  N     . ILE   A 272 ? 0.586  0.5049 0.538  -0.0136 0.0778  0.0353  272 ILE   A N     
1945 C  CA    . ILE   A 272 ? 0.6096 0.516  0.544  -0.0175 0.0767  0.0315  272 ILE   A CA    
1946 C  C     . ILE   A 272 ? 0.6353 0.5284 0.5508 -0.0243 0.0721  0.0294  272 ILE   A C     
1947 O  O     . ILE   A 272 ? 0.6554 0.5338 0.5628 -0.0254 0.0779  0.0295  272 ILE   A O     
1948 C  CB    . ILE   A 272 ? 0.6206 0.5077 0.5468 -0.0153 0.0895  0.0306  272 ILE   A CB    
1949 C  CG1   . ILE   A 272 ? 0.6127 0.5121 0.5603 -0.0088 0.0948  0.0334  272 ILE   A CG1   
1950 C  CG2   . ILE   A 272 ? 0.637  0.5076 0.5401 -0.0201 0.0881  0.027   272 ILE   A CG2   
1951 C  CD1   . ILE   A 272 ? 0.6377 0.5182 0.5821 -0.0056 0.1107  0.0338  272 ILE   A CD1   
1952 N  N     . ALA   A 273 ? 0.6318 0.5294 0.5413 -0.029  0.0617  0.0278  273 ALA   A N     
1953 C  CA    . ALA   A 273 ? 0.6532 0.5384 0.546  -0.0364 0.0556  0.0263  273 ALA   A CA    
1954 C  C     . ALA   A 273 ? 0.6818 0.5544 0.5572 -0.0402 0.0518  0.0239  273 ALA   A C     
1955 O  O     . ALA   A 273 ? 0.6797 0.5649 0.5627 -0.0389 0.0464  0.0242  273 ALA   A O     
1956 C  CB    . ALA   A 273 ? 0.6388 0.5428 0.544  -0.0388 0.0453  0.028   273 ALA   A CB    
1957 N  N     . ASN   A 274 ? 0.7086 0.5548 0.5595 -0.0447 0.0555  0.0217  274 ASN   A N     
1958 C  CA    . ASN   A 274 ? 0.7412 0.5709 0.5706 -0.0491 0.0519  0.0198  274 ASN   A CA    
1959 C  C     . ASN   A 274 ? 0.7648 0.581  0.5756 -0.0585 0.0411  0.0188  274 ASN   A C     
1960 O  O     . ASN   A 274 ? 0.7844 0.5874 0.5855 -0.0621 0.0434  0.0178  274 ASN   A O     
1961 C  CB    . ASN   A 274 ? 0.7746 0.5809 0.587  -0.0469 0.0662  0.0179  274 ASN   A CB    
1962 C  CG    . ASN   A 274 ? 0.842  0.6291 0.629  -0.0515 0.0633  0.0162  274 ASN   A CG    
1963 O  OD1   . ASN   A 274 ? 0.8544 0.653  0.6458 -0.0529 0.0525  0.0174  274 ASN   A OD1   
1964 N  ND2   . ASN   A 274 ? 0.8685 0.6247 0.6277 -0.054  0.0733  0.0136  274 ASN   A ND2   
1965 N  N     . ASN   A 275 ? 0.7589 0.5793 0.5666 -0.0626 0.0287  0.0195  275 ASN   A N     
1966 C  CA    . ASN   A 275 ? 0.7689 0.5776 0.5608 -0.0723 0.0159  0.0195  275 ASN   A CA    
1967 C  C     . ASN   A 275 ? 0.7903 0.5884 0.5653 -0.0762 0.0074  0.0197  275 ASN   A C     
1968 O  O     . ASN   A 275 ? 0.787  0.5855 0.5617 -0.0712 0.0135  0.0195  275 ASN   A O     
1969 C  CB    . ASN   A 275 ? 0.7443 0.5771 0.5603 -0.0739 0.0056  0.0222  275 ASN   A CB    
1970 C  CG    . ASN   A 275 ? 0.744  0.6049 0.5857 -0.0691 0.0001  0.0248  275 ASN   A CG    
1971 O  OD1   . ASN   A 275 ? 0.7505 0.6137 0.5912 -0.072  -0.0103 0.0262  275 ASN   A OD1   
1972 N  ND2   . ASN   A 275 ? 0.7229 0.6044 0.5872 -0.0618 0.0069  0.0255  275 ASN   A ND2   
1973 N  N     . ASP   A 276 ? 0.8118 0.6003 0.5734 -0.0853 -0.0069 0.0206  276 ASP   A N     
1974 C  CA    . ASP   A 276 ? 0.839  0.6158 0.5829 -0.0897 -0.0167 0.0217  276 ASP   A CA    
1975 C  C     . ASP   A 276 ? 0.8157 0.6179 0.5841 -0.0853 -0.024  0.0252  276 ASP   A C     
1976 O  O     . ASP   A 276 ? 0.8394 0.6333 0.5959 -0.0854 -0.0264 0.026   276 ASP   A O     
1977 C  CB    . ASP   A 276 ? 0.9043 0.6629 0.6272 -0.1015 -0.0317 0.0223  276 ASP   A CB    
1978 C  CG    . ASP   A 276 ? 1.0409 0.7653 0.7295 -0.1071 -0.0242 0.018   276 ASP   A CG    
1979 O  OD1   . ASP   A 276 ? 1.0649 0.7735 0.7389 -0.1022 -0.0074 0.0148  276 ASP   A OD1   
1980 O  OD2   . ASP   A 276 ? 1.1039 0.8164 0.7806 -0.1164 -0.0347 0.0179  276 ASP   A OD2   
1981 N  N     . VAL   A 277 ? 0.7747 0.6063 0.5757 -0.0816 -0.0271 0.0273  277 VAL   A N     
1982 C  CA    . VAL   A 277 ? 0.7438 0.5994 0.5693 -0.0773 -0.0334 0.0303  277 VAL   A CA    
1983 C  C     . VAL   A 277 ? 0.7299 0.5976 0.5685 -0.0675 -0.0208 0.0289  277 VAL   A C     
1984 O  O     . VAL   A 277 ? 0.737  0.605  0.5747 -0.065  -0.0216 0.0296  277 VAL   A O     
1985 C  CB    . VAL   A 277 ? 0.7272 0.6071 0.5807 -0.0785 -0.0425 0.0333  277 VAL   A CB    
1986 C  CG1   . VAL   A 277 ? 0.7125 0.6172 0.593  -0.0728 -0.0461 0.0359  277 VAL   A CG1   
1987 C  CG2   . VAL   A 277 ? 0.7289 0.5979 0.5724 -0.0889 -0.0571 0.0356  277 VAL   A CG2   
1988 N  N     . ASP   A 278 ? 0.7099 0.5869 0.5606 -0.0624 -0.0099 0.0272  278 ASP   A N     
1989 C  CA    . ASP   A 278 ? 0.6942 0.5844 0.5598 -0.0539 0.0002  0.0264  278 ASP   A CA    
1990 C  C     . ASP   A 278 ? 0.6877 0.5716 0.5509 -0.0499 0.0144  0.0244  278 ASP   A C     
1991 O  O     . ASP   A 278 ? 0.6962 0.5676 0.5485 -0.053  0.0175  0.0235  278 ASP   A O     
1992 C  CB    . ASP   A 278 ? 0.6939 0.6134 0.5894 -0.0498 -0.0041 0.0281  278 ASP   A CB    
1993 C  CG    . ASP   A 278 ? 0.7604 0.6919 0.669  -0.0512 -0.0058 0.029   278 ASP   A CG    
1994 O  OD1   . ASP   A 278 ? 0.7882 0.7064 0.6844 -0.0553 -0.004  0.0284  278 ASP   A OD1   
1995 O  OD2   . ASP   A 278 ? 0.7766 0.7295 0.707  -0.0483 -0.0082 0.0302  278 ASP   A OD2   
1996 N  N     . LEU   A 279 ? 0.6702 0.5628 0.5448 -0.0431 0.0227  0.0241  279 LEU   A N     
1997 C  CA    . LEU   A 279 ? 0.6596 0.5523 0.5402 -0.0381 0.0351  0.0235  279 LEU   A CA    
1998 C  C     . LEU   A 279 ? 0.6321 0.5516 0.5393 -0.0337 0.0331  0.0248  279 LEU   A C     
1999 O  O     . LEU   A 279 ? 0.6307 0.5654 0.5507 -0.0314 0.0284  0.0251  279 LEU   A O     
2000 C  CB    . LEU   A 279 ? 0.6653 0.5506 0.5429 -0.034  0.0446  0.0229  279 LEU   A CB    
2001 C  CG    . LEU   A 279 ? 0.6754 0.5675 0.5684 -0.0277 0.056   0.0236  279 LEU   A CG    
2002 C  CD1   . LEU   A 279 ? 0.687  0.5641 0.5709 -0.0283 0.0645  0.0233  279 LEU   A CD1   
2003 C  CD2   . LEU   A 279 ? 0.6817 0.5719 0.5781 -0.0239 0.0634  0.0237  279 LEU   A CD2   
2004 N  N     . ILE   A 280 ? 0.6111 0.5347 0.5249 -0.0326 0.0366  0.0255  280 ILE   A N     
2005 C  CA    . ILE   A 280 ? 0.5925 0.5384 0.5276 -0.0287 0.0355  0.0269  280 ILE   A CA    
2006 C  C     . ILE   A 280 ? 0.5889 0.5366 0.5325 -0.0234 0.0448  0.0279  280 ILE   A C     
2007 O  O     . ILE   A 280 ? 0.6005 0.5355 0.5374 -0.0235 0.0515  0.0284  280 ILE   A O     
2008 C  CB    . ILE   A 280 ? 0.5901 0.5424 0.5288 -0.032  0.0304  0.0281  280 ILE   A CB    
2009 C  CG1   . ILE   A 280 ? 0.6126 0.5622 0.5449 -0.0381 0.0207  0.028   280 ILE   A CG1   
2010 C  CG2   . ILE   A 280 ? 0.5752 0.5492 0.5332 -0.0281 0.0297  0.0296  280 ILE   A CG2   
2011 C  CD1   . ILE   A 280 ? 0.6352 0.5733 0.5572 -0.0439 0.0186  0.0284  280 ILE   A CD1   
2012 N  N     . ILE   A 281 ? 0.5713 0.5349 0.5307 -0.0189 0.0446  0.0286  281 ILE   A N     
2013 C  CA    . ILE   A 281 ? 0.5613 0.5297 0.5325 -0.0142 0.051   0.0306  281 ILE   A CA    
2014 C  C     . ILE   A 281 ? 0.549  0.5363 0.5339 -0.0127 0.0459  0.0321  281 ILE   A C     
2015 O  O     . ILE   A 281 ? 0.553  0.5521 0.5439 -0.0122 0.0406  0.0309  281 ILE   A O     
2016 C  CB    . ILE   A 281 ? 0.561  0.5282 0.5374 -0.0109 0.0558  0.0304  281 ILE   A CB    
2017 C  CG1   . ILE   A 281 ? 0.5818 0.5274 0.5415 -0.0126 0.0627  0.0291  281 ILE   A CG1   
2018 C  CG2   . ILE   A 281 ? 0.5566 0.532  0.5499 -0.0063 0.0603  0.0334  281 ILE   A CG2   
2019 C  CD1   . ILE   A 281 ? 0.5982 0.5416 0.5611 -0.0103 0.0672  0.0288  281 ILE   A CD1   
2020 N  N     . ARG   A 282 ? 0.5357 0.5243 0.5238 -0.0121 0.0476  0.0346  282 ARG   A N     
2021 C  CA    . ARG   A 282 ? 0.5198 0.5239 0.518  -0.0109 0.0434  0.0365  282 ARG   A CA    
2022 C  C     . ARG   A 282 ? 0.5259 0.5348 0.536  -0.0065 0.0462  0.0397  282 ARG   A C     
2023 O  O     . ARG   A 282 ? 0.5375 0.5377 0.549  -0.0048 0.0522  0.0421  282 ARG   A O     
2024 C  CB    . ARG   A 282 ? 0.5182 0.5209 0.5119 -0.0137 0.0423  0.038   282 ARG   A CB    
2025 C  CG    . ARG   A 282 ? 0.5321 0.5478 0.5336 -0.0124 0.0397  0.0407  282 ARG   A CG    
2026 C  CD    . ARG   A 282 ? 0.551  0.5636 0.5485 -0.0152 0.0401  0.043   282 ARG   A CD    
2027 N  NE    . ARG   A 282 ? 0.589  0.5894 0.5844 -0.0143 0.0456  0.0456  282 ARG   A NE    
2028 C  CZ    . ARG   A 282 ? 0.618  0.6094 0.6071 -0.0173 0.0474  0.0467  282 ARG   A CZ    
2029 N  NH1   . ARG   A 282 ? 0.6015 0.5959 0.5873 -0.0218 0.0436  0.046   282 ARG   A NH1   
2030 N  NH2   . ARG   A 282 ? 0.6265 0.6054 0.6139 -0.016  0.0534  0.0488  282 ARG   A NH2   
2031 N  N     . ILE   A 283 ? 0.5189 0.5409 0.538  -0.0047 0.0418  0.0398  283 ILE   A N     
2032 C  CA    . ILE   A 283 ? 0.5236 0.5514 0.5553 -0.0014 0.0419  0.0434  283 ILE   A CA    
2033 C  C     . ILE   A 283 ? 0.5306 0.5679 0.5635 -0.0018 0.0365  0.0457  283 ILE   A C     
2034 O  O     . ILE   A 283 ? 0.5287 0.5739 0.5588 -0.0032 0.0316  0.0433  283 ILE   A O     
2035 C  CB    . ILE   A 283 ? 0.5255 0.5587 0.565  -0.0001 0.0402  0.0417  283 ILE   A CB    
2036 C  CG1   . ILE   A 283 ? 0.5455 0.5678 0.5808 -0.0002 0.0461  0.0394  283 ILE   A CG1   
2037 C  CG2   . ILE   A 283 ? 0.5224 0.5623 0.5772 0.0026  0.0388  0.0461  283 ILE   A CG2   
2038 C  CD1   . ILE   A 283 ? 0.5674 0.5939 0.6089 0.0005  0.0447  0.0375  283 ILE   A CD1   
2039 N  N     . SER   A 284 ? 0.5361 0.5712 0.5718 -0.0008 0.0381  0.0505  284 SER   A N     
2040 C  CA    . SER   A 284 ? 0.5398 0.5813 0.5741 -0.0014 0.0336  0.0537  284 SER   A CA    
2041 C  C     . SER   A 284 ? 0.5295 0.5767 0.575  0.0011  0.0299  0.0589  284 SER   A C     
2042 O  O     . SER   A 284 ? 0.5368 0.5799 0.5926 0.0039  0.0335  0.063   284 SER   A O     
2043 C  CB    . SER   A 284 ? 0.5719 0.6058 0.6003 -0.0026 0.0372  0.056   284 SER   A CB    
2044 O  OG    . SER   A 284 ? 0.634  0.661  0.6531 -0.0056 0.0399  0.0518  284 SER   A OG    
2045 N  N     . ASP   A 285 ? 0.5102 0.5659 0.5535 0.0001  0.0229  0.0591  285 ASP   A N     
2046 C  CA    . ASP   A 285 ? 0.4985 0.5595 0.5511 0.0015  0.0168  0.0645  285 ASP   A CA    
2047 C  C     . ASP   A 285 ? 0.507  0.57   0.5504 -0.0001 0.0117  0.0681  285 ASP   A C     
2048 O  O     . ASP   A 285 ? 0.5009 0.5625 0.5315 -0.0023 0.0136  0.0658  285 ASP   A O     
2049 C  CB    . ASP   A 285 ? 0.4821 0.5494 0.5396 0.0011  0.0115  0.0615  285 ASP   A CB    
2050 C  CG    . ASP   A 285 ? 0.4982 0.569  0.5421 -0.0018 0.0073  0.0562  285 ASP   A CG    
2051 O  OD1   . ASP   A 285 ? 0.4755 0.5477 0.5098 -0.0035 0.003   0.0581  285 ASP   A OD1   
2052 O  OD2   . ASP   A 285 ? 0.5062 0.5776 0.5488 -0.0024 0.0088  0.0504  285 ASP   A OD2   
2053 N  N     . ARG   A 286 ? 0.5183 0.5847 0.5689 0.0007  0.005   0.0744  286 ARG   A N     
2054 C  CA    . ARG   A 286 ? 0.5359 0.6031 0.5762 -0.0011 -0.0013 0.0786  286 ARG   A CA    
2055 C  C     . ARG   A 286 ? 0.5371 0.6096 0.5759 -0.0029 -0.0116 0.0787  286 ARG   A C     
2056 O  O     . ARG   A 286 ? 0.5496 0.6232 0.5896 -0.0034 -0.0198 0.0854  286 ARG   A O     
2057 C  CB    . ARG   A 286 ? 0.5532 0.6172 0.6016 0.0012  -0.0011 0.0874  286 ARG   A CB    
2058 C  CG    . ARG   A 286 ? 0.6077 0.6642 0.6548 0.0022  0.0091  0.0866  286 ARG   A CG    
2059 C  CD    . ARG   A 286 ? 0.6949 0.7477 0.7311 0.0007  0.0088  0.091   286 ARG   A CD    
2060 N  NE    . ARG   A 286 ? 0.7581 0.805  0.7856 -0.0009 0.017   0.087   286 ARG   A NE    
2061 C  CZ    . ARG   A 286 ? 0.7695 0.8123 0.7877 -0.0028 0.0189  0.0899  286 ARG   A CZ    
2062 N  NH1   . ARG   A 286 ? 0.7337 0.7767 0.7479 -0.0029 0.0136  0.0968  286 ARG   A NH1   
2063 N  NH2   . ARG   A 286 ? 0.7906 0.8284 0.8032 -0.0048 0.0256  0.0863  286 ARG   A NH2   
2064 N  N     . GLY   A 287 ? 0.5281 0.6029 0.5635 -0.0042 -0.0118 0.0715  287 GLY   A N     
2065 C  CA    . GLY   A 287 ? 0.5348 0.6128 0.5678 -0.0066 -0.0212 0.0704  287 GLY   A CA    
2066 C  C     . GLY   A 287 ? 0.5521 0.6275 0.5622 -0.0102 -0.0244 0.0666  287 GLY   A C     
2067 O  O     . GLY   A 287 ? 0.5642 0.6401 0.5692 -0.0124 -0.0296 0.0624  287 GLY   A O     
2068 N  N     . GLY   A 288 ? 0.5506 0.6222 0.5469 -0.0109 -0.0205 0.0679  288 GLY   A N     
2069 C  CA    . GLY   A 288 ? 0.5542 0.6216 0.5275 -0.0142 -0.0215 0.0649  288 GLY   A CA    
2070 C  C     . GLY   A 288 ? 0.5564 0.6228 0.5203 -0.0147 -0.0126 0.0568  288 GLY   A C     
2071 O  O     . GLY   A 288 ? 0.5669 0.6291 0.5127 -0.0168 -0.0103 0.0548  288 GLY   A O     
2072 N  N     . GLY   A 289 ? 0.543  0.6128 0.5194 -0.0127 -0.0072 0.0524  289 GLY   A N     
2073 C  CA    . GLY   A 289 ? 0.5357 0.6057 0.5075 -0.0128 0.0004  0.0456  289 GLY   A CA    
2074 C  C     . GLY   A 289 ? 0.53   0.5994 0.4952 -0.0138 -0.0011 0.039   289 GLY   A C     
2075 O  O     . GLY   A 289 ? 0.5218 0.5898 0.4838 -0.0153 -0.0089 0.039   289 GLY   A O     
2076 N  N     . ILE   A 290 ? 0.5339 0.6038 0.4979 -0.0133 0.006   0.0334  290 ILE   A N     
2077 C  CA    . ILE   A 290 ? 0.543  0.6113 0.5012 -0.0138 0.0065  0.0266  290 ILE   A CA    
2078 C  C     . ILE   A 290 ? 0.5659 0.6296 0.5069 -0.0152 0.0119  0.0249  290 ILE   A C     
2079 O  O     . ILE   A 290 ? 0.5693 0.6347 0.5118 -0.0146 0.0194  0.0257  290 ILE   A O     
2080 C  CB    . ILE   A 290 ? 0.5378 0.6096 0.5087 -0.0116 0.0114  0.0223  290 ILE   A CB    
2081 C  CG1   . ILE   A 290 ? 0.5363 0.6107 0.5223 -0.0102 0.0078  0.0241  290 ILE   A CG1   
2082 C  CG2   . ILE   A 290 ? 0.5429 0.6123 0.508  -0.0116 0.0139  0.0155  290 ILE   A CG2   
2083 C  CD1   . ILE   A 290 ? 0.5457 0.622  0.5416 -0.0085 0.0125  0.0216  290 ILE   A CD1   
2084 N  N     . ALA   A 291 ? 0.576  0.633  0.5    -0.0176 0.0082  0.0226  291 ALA   A N     
2085 C  CA    . ALA   A 291 ? 0.5938 0.6434 0.4971 -0.0194 0.0138  0.021   291 ALA   A CA    
2086 C  C     . ALA   A 291 ? 0.6112 0.6613 0.5165 -0.0175 0.0256  0.0156  291 ALA   A C     
2087 O  O     . ALA   A 291 ? 0.6047 0.6585 0.5226 -0.0155 0.0269  0.0113  291 ALA   A O     
2088 C  CB    . ALA   A 291 ? 0.6001 0.6399 0.483  -0.0228 0.0067  0.0188  291 ALA   A CB    
2089 N  N     . HIS   A 292 ? 0.6287 0.6752 0.5229 -0.0181 0.0343  0.0163  292 HIS   A N     
2090 C  CA    . HIS   A 292 ? 0.645  0.6924 0.543  -0.0162 0.0467  0.0122  292 HIS   A CA    
2091 C  C     . HIS   A 292 ? 0.6758 0.7177 0.5684 -0.0155 0.0491  0.0044  292 HIS   A C     
2092 O  O     . HIS   A 292 ? 0.6705 0.7175 0.5787 -0.0126 0.0549  0.0012  292 HIS   A O     
2093 C  CB    . HIS   A 292 ? 0.6514 0.6935 0.535  -0.0176 0.056   0.0146  292 HIS   A CB    
2094 C  CG    . HIS   A 292 ? 0.6553 0.7045 0.5509 -0.0176 0.0579  0.0213  292 HIS   A CG    
2095 N  ND1   . HIS   A 292 ? 0.6831 0.729  0.5682 -0.0199 0.0535  0.0276  292 HIS   A ND1   
2096 C  CD2   . HIS   A 292 ? 0.6515 0.7102 0.5685 -0.016  0.0629  0.0226  292 HIS   A CD2   
2097 C  CE1   . HIS   A 292 ? 0.678  0.7308 0.578  -0.0195 0.0569  0.032   292 HIS   A CE1   
2098 N  NE2   . HIS   A 292 ? 0.6665 0.727  0.5854 -0.0175 0.0622  0.0291  292 HIS   A NE2   
2099 N  N     . LYS   A 293 ? 0.7057 0.7365 0.5766 -0.0183 0.0441  0.0016  293 LYS   A N     
2100 C  CA    . LYS   A 293 ? 0.7421 0.7652 0.6056 -0.0181 0.0461  -0.0063 293 LYS   A CA    
2101 C  C     . LYS   A 293 ? 0.7472 0.777  0.6303 -0.0163 0.0394  -0.0086 293 LYS   A C     
2102 O  O     . LYS   A 293 ? 0.7629 0.7891 0.6475 -0.0148 0.0437  -0.0148 293 LYS   A O     
2103 C  CB    . LYS   A 293 ? 0.7941 0.8015 0.6267 -0.0226 0.0412  -0.0088 293 LYS   A CB    
2104 C  CG    . LYS   A 293 ? 0.8719 0.8801 0.7024 -0.0259 0.0247  -0.0045 293 LYS   A CG    
2105 C  CD    . LYS   A 293 ? 0.9728 0.9646 0.7724 -0.0313 0.0177  -0.007  293 LYS   A CD    
2106 C  CE    . LYS   A 293 ? 1.0398 1.0341 0.8433 -0.0346 -0.0001 -0.003  293 LYS   A CE    
2107 N  NZ    . LYS   A 293 ? 1.0718 1.077  0.9027 -0.032  -0.0041 -0.0045 293 LYS   A NZ    
2108 N  N     . ASP   A 294 ? 0.73   0.7687 0.628  -0.0162 0.03    -0.0036 294 ASP   A N     
2109 C  CA    . ASP   A 294 ? 0.7193 0.7636 0.6351 -0.0148 0.0243  -0.0049 294 ASP   A CA    
2110 C  C     . ASP   A 294 ? 0.7097 0.764  0.6478 -0.0112 0.0292  -0.0034 294 ASP   A C     
2111 O  O     . ASP   A 294 ? 0.7068 0.7635 0.6572 -0.0096 0.0275  -0.0057 294 ASP   A O     
2112 C  CB    . ASP   A 294 ? 0.7304 0.7775 0.6503 -0.0168 0.0121  0.0001  294 ASP   A CB    
2113 C  CG    . ASP   A 294 ? 0.8131 0.8511 0.7142 -0.0212 0.0034  -0.0008 294 ASP   A CG    
2114 O  OD1   . ASP   A 294 ? 0.8385 0.8668 0.7247 -0.0227 0.0053  -0.0072 294 ASP   A OD1   
2115 O  OD2   . ASP   A 294 ? 0.8486 0.8884 0.75   -0.0231 -0.0057 0.0052  294 ASP   A OD2   
2116 N  N     . LEU   A 295 ? 0.7091 0.7683 0.652  -0.0104 0.034   0.0009  295 LEU   A N     
2117 C  CA    . LEU   A 295 ? 0.7176 0.7854 0.6799 -0.0082 0.0366  0.0034  295 LEU   A CA    
2118 C  C     . LEU   A 295 ? 0.7274 0.7974 0.7018 -0.0054 0.0412  -0.0007 295 LEU   A C     
2119 O  O     . LEU   A 295 ? 0.7207 0.7955 0.7098 -0.0041 0.0386  0.0005  295 LEU   A O     
2120 C  CB    . LEU   A 295 ? 0.7239 0.7945 0.686  -0.0087 0.0421  0.0078  295 LEU   A CB    
2121 C  CG    . LEU   A 295 ? 0.7434 0.821  0.7213 -0.0083 0.041   0.0124  295 LEU   A CG    
2122 C  CD1   . LEU   A 295 ? 0.747  0.8249 0.7289 -0.0087 0.0326  0.0149  295 LEU   A CD1   
2123 C  CD2   . LEU   A 295 ? 0.7546 0.8332 0.7297 -0.0098 0.0453  0.0168  295 LEU   A CD2   
2124 N  N     . ASP   A 296 ? 0.7408 0.8061 0.7084 -0.0045 0.0483  -0.0053 296 ASP   A N     
2125 C  CA    . ASP   A 296 ? 0.7557 0.8221 0.735  -0.0014 0.0536  -0.009  296 ASP   A CA    
2126 C  C     . ASP   A 296 ? 0.7455 0.8075 0.725  -0.001  0.0484  -0.0134 296 ASP   A C     
2127 O  O     . ASP   A 296 ? 0.7518 0.8138 0.7409 0.0018  0.0521  -0.0163 296 ASP   A O     
2128 C  CB    . ASP   A 296 ? 0.8194 0.8809 0.7911 -0.0003 0.0653  -0.0122 296 ASP   A CB    
2129 C  CG    . ASP   A 296 ? 0.9671 1.017  0.9123 -0.0032 0.0658  -0.0151 296 ASP   A CG    
2130 O  OD1   . ASP   A 296 ? 0.989  1.0384 0.9234 -0.0058 0.0641  -0.0111 296 ASP   A OD1   
2131 O  OD2   . ASP   A 296 ? 1.0257 1.066  0.9597 -0.0033 0.0669  -0.0212 296 ASP   A OD2   
2132 N  N     . ARG   A 297 ? 0.7243 0.7831 0.6953 -0.0036 0.0397  -0.0133 297 ARG   A N     
2133 C  CA    . ARG   A 297 ? 0.7064 0.7611 0.6784 -0.0039 0.0345  -0.017  297 ARG   A CA    
2134 C  C     . ARG   A 297 ? 0.6646 0.724  0.6466 -0.0047 0.0258  -0.0131 297 ARG   A C     
2135 O  O     . ARG   A 297 ? 0.6635 0.7211 0.6512 -0.0046 0.0225  -0.0152 297 ARG   A O     
2136 C  CB    . ARG   A 297 ? 0.7441 0.7879 0.6956 -0.007  0.0323  -0.0215 297 ARG   A CB    
2137 C  CG    . ARG   A 297 ? 0.8164 0.8514 0.7563 -0.0059 0.0421  -0.0274 297 ARG   A CG    
2138 C  CD    . ARG   A 297 ? 0.9018 0.9235 0.8166 -0.0101 0.039   -0.0318 297 ARG   A CD    
2139 N  NE    . ARG   A 297 ? 0.9817 1.0023 0.8819 -0.0134 0.0354  -0.0275 297 ARG   A NE    
2140 C  CZ    . ARG   A 297 ? 1.0403 1.0501 0.9176 -0.0181 0.0291  -0.0291 297 ARG   A CZ    
2141 N  NH1   . ARG   A 297 ? 1.0481 1.0468 0.914  -0.0206 0.0257  -0.0353 297 ARG   A NH1   
2142 N  NH2   . ARG   A 297 ? 1.0405 1.0497 0.9058 -0.0207 0.0255  -0.0241 297 ARG   A NH2   
2143 N  N     . VAL   A 298 ? 0.6268 0.6911 0.611  -0.0056 0.023   -0.0074 298 VAL   A N     
2144 C  CA    . VAL   A 298 ? 0.5921 0.6594 0.5857 -0.0061 0.0166  -0.0037 298 VAL   A CA    
2145 C  C     . VAL   A 298 ? 0.5665 0.636  0.574  -0.004  0.0177  -0.0038 298 VAL   A C     
2146 O  O     . VAL   A 298 ? 0.5626 0.6317 0.5764 -0.0043 0.0137  -0.0028 298 VAL   A O     
2147 C  CB    . VAL   A 298 ? 0.5848 0.6556 0.5788 -0.007  0.0144  0.0025  298 VAL   A CB    
2148 C  CG1   . VAL   A 298 ? 0.5892 0.6571 0.57   -0.0096 0.0106  0.0038  298 VAL   A CG1   
2149 C  CG2   . VAL   A 298 ? 0.5833 0.6578 0.5811 -0.0058 0.0201  0.0049  298 VAL   A CG2   
2150 N  N     . MET   A 299 ? 0.5488 0.6201 0.5612 -0.0019 0.0229  -0.0045 299 MET   A N     
2151 C  CA    . MET   A 299 ? 0.5415 0.6137 0.5654 -0.0002 0.0229  -0.004  299 MET   A CA    
2152 C  C     . MET   A 299 ? 0.5405 0.6088 0.5669 0.0012  0.0236  -0.0086 299 MET   A C     
2153 O  O     . MET   A 299 ? 0.5361 0.6043 0.5713 0.0029  0.0236  -0.0081 299 MET   A O     
2154 C  CB    . MET   A 299 ? 0.543  0.6194 0.5737 0.0009  0.026   -0.0013 299 MET   A CB    
2155 C  CG    . MET   A 299 ? 0.5776 0.6564 0.6066 -0.0008 0.0251  0.0033  299 MET   A CG    
2156 S  SD    . MET   A 299 ? 0.6597 0.7355 0.6888 -0.0021 0.0204  0.0066  299 MET   A SD    
2157 C  CE    . MET   A 299 ? 0.5331 0.6061 0.5693 -0.0011 0.0194  0.0065  299 MET   A CE    
2158 N  N     . ASP   A 300 ? 0.5426 0.6063 0.5599 0.0003  0.0239  -0.0131 300 ASP   A N     
2159 C  CA    . ASP   A 300 ? 0.5489 0.607  0.5671 0.0012  0.0246  -0.018  300 ASP   A CA    
2160 C  C     . ASP   A 300 ? 0.5403 0.5961 0.5606 -0.0008 0.0183  -0.0178 300 ASP   A C     
2161 O  O     . ASP   A 300 ? 0.5427 0.599  0.5583 -0.0035 0.0136  -0.0161 300 ASP   A O     
2162 C  CB    . ASP   A 300 ? 0.5865 0.6378 0.5907 0.0002  0.0276  -0.0234 300 ASP   A CB    
2163 C  CG    . ASP   A 300 ? 0.6651 0.7166 0.6671 0.0025  0.0364  -0.0249 300 ASP   A CG    
2164 O  OD1   . ASP   A 300 ? 0.6684 0.7265 0.6831 0.0051  0.0396  -0.0215 300 ASP   A OD1   
2165 O  OD2   . ASP   A 300 ? 0.7166 0.7608 0.704  0.0014  0.0401  -0.0292 300 ASP   A OD2   
2166 N  N     . TYR   A 301 ? 0.5305 0.5831 0.5581 0.0004  0.0183  -0.0194 301 TYR   A N     
2167 C  CA    . TYR   A 301 ? 0.5281 0.5779 0.5589 -0.0018 0.0133  -0.0195 301 TYR   A CA    
2168 C  C     . TYR   A 301 ? 0.5396 0.5839 0.5601 -0.0051 0.01    -0.024  301 TYR   A C     
2169 O  O     . TYR   A 301 ? 0.5472 0.5866 0.5581 -0.0047 0.0136  -0.0287 301 TYR   A O     
2170 C  CB    . TYR   A 301 ? 0.5213 0.5674 0.5607 0.0001  0.0148  -0.0204 301 TYR   A CB    
2171 C  CG    . TYR   A 301 ? 0.5104 0.5596 0.5579 0.0021  0.0158  -0.0154 301 TYR   A CG    
2172 C  CD1   . TYR   A 301 ? 0.5154 0.5646 0.5671 0.0008  0.0136  -0.0115 301 TYR   A CD1   
2173 C  CD2   . TYR   A 301 ? 0.5071 0.5579 0.5579 0.005   0.019   -0.0144 301 TYR   A CD2   
2174 C  CE1   . TYR   A 301 ? 0.5225 0.5712 0.5775 0.002   0.0147  -0.0073 301 TYR   A CE1   
2175 C  CE2   . TYR   A 301 ? 0.5165 0.5682 0.5726 0.0059  0.0183  -0.0097 301 TYR   A CE2   
2176 C  CZ    . TYR   A 301 ? 0.5298 0.5794 0.5859 0.0043  0.0162  -0.0065 301 TYR   A CZ    
2177 O  OH    . TYR   A 301 ? 0.5471 0.5948 0.6043 0.0046  0.0156  -0.0022 301 TYR   A OH    
2178 N  N     . HIS   A 302 ? 0.5464 0.5912 0.5687 -0.0085 0.0034  -0.0223 302 HIS   A N     
2179 C  CA    . HIS   A 302 ? 0.5686 0.608  0.5813 -0.0128 -0.0025 -0.0256 302 HIS   A CA    
2180 C  C     . HIS   A 302 ? 0.5946 0.6345 0.5935 -0.0148 -0.0049 -0.0247 302 HIS   A C     
2181 O  O     . HIS   A 302 ? 0.6083 0.644  0.5989 -0.0192 -0.0121 -0.0259 302 HIS   A O     
2182 C  CB    . HIS   A 302 ? 0.5736 0.6028 0.5793 -0.0134 -0.0007 -0.0329 302 HIS   A CB    
2183 C  CG    . HIS   A 302 ? 0.5896 0.617  0.6083 -0.0122 0.0005  -0.0334 302 HIS   A CG    
2184 N  ND1   . HIS   A 302 ? 0.6027 0.629  0.6264 -0.0076 0.0076  -0.0344 302 HIS   A ND1   
2185 C  CD2   . HIS   A 302 ? 0.595  0.6216 0.6231 -0.0149 -0.0047 -0.0323 302 HIS   A CD2   
2186 C  CE1   . HIS   A 302 ? 0.6049 0.6289 0.6388 -0.0078 0.0065  -0.0339 302 HIS   A CE1   
2187 N  NE2   . HIS   A 302 ? 0.605  0.6289 0.642  -0.0122 -0.0002 -0.0329 302 HIS   A NE2   
2188 N  N     . PHE   A 303 ? 0.5978 0.642  0.5938 -0.0121 0.0004  -0.0224 303 PHE   A N     
2189 C  CA    . PHE   A 303 ? 0.6157 0.6595 0.598  -0.0141 -0.0015 -0.021  303 PHE   A CA    
2190 C  C     . PHE   A 303 ? 0.6235 0.6735 0.6124 -0.016  -0.0089 -0.0143 303 PHE   A C     
2191 O  O     . PHE   A 303 ? 0.6126 0.6695 0.6144 -0.0137 -0.0073 -0.0094 303 PHE   A O     
2192 C  CB    . PHE   A 303 ? 0.6172 0.6626 0.5938 -0.0113 0.007   -0.0209 303 PHE   A CB    
2193 C  CG    . PHE   A 303 ? 0.633  0.6763 0.5936 -0.0137 0.0053  -0.0192 303 PHE   A CG    
2194 C  CD1   . PHE   A 303 ? 0.6553 0.6882 0.5954 -0.0162 0.0063  -0.0241 303 PHE   A CD1   
2195 C  CD2   . PHE   A 303 ? 0.6303 0.6804 0.5949 -0.0139 0.0025  -0.0125 303 PHE   A CD2   
2196 C  CE1   . PHE   A 303 ? 0.6685 0.6979 0.5916 -0.0189 0.0043  -0.0221 303 PHE   A CE1   
2197 C  CE2   . PHE   A 303 ? 0.6445 0.692  0.5944 -0.0163 0.0001  -0.0102 303 PHE   A CE2   
2198 C  CZ    . PHE   A 303 ? 0.6555 0.6927 0.5842 -0.0189 0.0009  -0.0148 303 PHE   A CZ    
2199 N  N     . THR   A 304 ? 0.6373 0.6837 0.6163 -0.0203 -0.0171 -0.014  304 THR   A N     
2200 C  CA    . THR   A 304 ? 0.6541 0.7063 0.6404 -0.022  -0.0247 -0.0069 304 THR   A CA    
2201 C  C     . THR   A 304 ? 0.6877 0.7347 0.6554 -0.0261 -0.0316 -0.0062 304 THR   A C     
2202 O  O     . THR   A 304 ? 0.7104 0.7474 0.6601 -0.0291 -0.0332 -0.0118 304 THR   A O     
2203 C  CB    . THR   A 304 ? 0.6599 0.7152 0.6642 -0.0236 -0.031  -0.0049 304 THR   A CB    
2204 O  OG1   . THR   A 304 ? 0.6623 0.7234 0.6759 -0.0251 -0.0383 0.0024  304 THR   A OG1   
2205 C  CG2   . THR   A 304 ? 0.6681 0.7154 0.6657 -0.0278 -0.0367 -0.0106 304 THR   A CG2   
2206 N  N     . THR   A 305 ? 0.6966 0.7487 0.6668 -0.0262 -0.0354 0.0009  305 THR   A N     
2207 C  CA    . THR   A 305 ? 0.7161 0.7628 0.669  -0.0305 -0.044  0.0031  305 THR   A CA    
2208 C  C     . THR   A 305 ? 0.7473 0.7968 0.7115 -0.0345 -0.0579 0.0081  305 THR   A C     
2209 O  O     . THR   A 305 ? 0.7653 0.8113 0.7179 -0.0384 -0.0676 0.0117  305 THR   A O     
2210 C  CB    . THR   A 305 ? 0.7103 0.7591 0.6564 -0.0287 -0.0403 0.0081  305 THR   A CB    
2211 O  OG1   . THR   A 305 ? 0.7031 0.7621 0.6711 -0.0253 -0.0388 0.0146  305 THR   A OG1   
2212 C  CG2   . THR   A 305 ? 0.7097 0.7542 0.6415 -0.0265 -0.0282 0.0032  305 THR   A CG2   
2213 N  N     . ALA   A 306 ? 0.7533 0.8089 0.7404 -0.0336 -0.059  0.0089  306 ALA   A N     
2214 C  CA    . ALA   A 306 ? 0.7724 0.832  0.7752 -0.0372 -0.0713 0.014   306 ALA   A CA    
2215 C  C     . ALA   A 306 ? 0.8017 0.8515 0.7905 -0.0434 -0.08   0.008   306 ALA   A C     
2216 O  O     . ALA   A 306 ? 0.827  0.867  0.7903 -0.0474 -0.0851 0.0056  306 ALA   A O     
2217 C  CB    . ALA   A 306 ? 0.7618 0.8302 0.7934 -0.034  -0.0668 0.0166  306 ALA   A CB    
2218 N  N     . GLY   A 335 ? 0.769  0.8439 0.8461 -0.0268 -0.0466 0.0129  335 GLY   A N     
2219 C  CA    . GLY   A 335 ? 0.7807 0.847  0.8402 -0.0302 -0.0498 0.0051  335 GLY   A CA    
2220 C  C     . GLY   A 335 ? 0.7788 0.8403 0.8362 -0.0278 -0.0409 -0.0011 335 GLY   A C     
2221 O  O     . GLY   A 335 ? 0.799  0.8524 0.8426 -0.0297 -0.0416 -0.0079 335 GLY   A O     
2222 N  N     . PHE   A 336 ? 0.7534 0.8184 0.8231 -0.0236 -0.0325 0.0014  336 PHE   A N     
2223 C  CA    . PHE   A 336 ? 0.7459 0.8067 0.8153 -0.0211 -0.0248 -0.0029 336 PHE   A CA    
2224 C  C     . PHE   A 336 ? 0.7003 0.7581 0.7537 -0.0179 -0.0184 -0.0067 336 PHE   A C     
2225 O  O     . PHE   A 336 ? 0.708  0.76   0.755  -0.0172 -0.0152 -0.0122 336 PHE   A O     
2226 C  CB    . PHE   A 336 ? 0.7693 0.8337 0.8556 -0.0183 -0.0187 0.0021  336 PHE   A CB    
2227 C  CG    . PHE   A 336 ? 0.8105 0.8709 0.9053 -0.0183 -0.0153 0.0004  336 PHE   A CG    
2228 C  CD1   . PHE   A 336 ? 0.8335 0.8928 0.9377 -0.0224 -0.0211 -0.0003 336 PHE   A CD1   
2229 C  CD2   . PHE   A 336 ? 0.8399 0.8971 0.9337 -0.0147 -0.0068 0.0003  336 PHE   A CD2   
2230 C  CE1   . PHE   A 336 ? 0.8538 0.909  0.9664 -0.0225 -0.0174 -0.0014 336 PHE   A CE1   
2231 C  CE2   . PHE   A 336 ? 0.8568 0.9093 0.9576 -0.0148 -0.0037 -0.0005 336 PHE   A CE2   
2232 C  CZ    . PHE   A 336 ? 0.8575 0.9091 0.9679 -0.0185 -0.0084 -0.0014 336 PHE   A CZ    
2233 N  N     . GLY   A 337 ? 0.6494 0.7111 0.6985 -0.016  -0.0162 -0.0035 337 GLY   A N     
2234 C  CA    . GLY   A 337 ? 0.6221 0.6824 0.6595 -0.0132 -0.0101 -0.006  337 GLY   A CA    
2235 C  C     . GLY   A 337 ? 0.5819 0.6418 0.6245 -0.0097 -0.0028 -0.0063 337 GLY   A C     
2236 O  O     . GLY   A 337 ? 0.574  0.6319 0.6101 -0.0078 0.0014  -0.0095 337 GLY   A O     
2237 N  N     . PHE   A 338 ? 0.5543 0.6155 0.6086 -0.0088 -0.0012 -0.0024 338 PHE   A N     
2238 C  CA    . PHE   A 338 ? 0.5405 0.5994 0.5975 -0.0061 0.0045  -0.002  338 PHE   A CA    
2239 C  C     . PHE   A 338 ? 0.5247 0.5851 0.5825 -0.0045 0.008   0.0028  338 PHE   A C     
2240 O  O     . PHE   A 338 ? 0.5344 0.5921 0.5903 -0.0029 0.0115  0.003   338 PHE   A O     
2241 C  CB    . PHE   A 338 ? 0.5314 0.5866 0.5978 -0.0066 0.0049  -0.0019 338 PHE   A CB    
2242 C  CG    . PHE   A 338 ? 0.5295 0.5798 0.5936 -0.0065 0.005   -0.007  338 PHE   A CG    
2243 C  CD1   . PHE   A 338 ? 0.5349 0.5836 0.5922 -0.0082 0.0017  -0.0119 338 PHE   A CD1   
2244 C  CD2   . PHE   A 338 ? 0.5338 0.5795 0.6012 -0.0048 0.0085  -0.0068 338 PHE   A CD2   
2245 C  CE1   . PHE   A 338 ? 0.5422 0.585  0.5972 -0.0077 0.003   -0.0169 338 PHE   A CE1   
2246 C  CE2   . PHE   A 338 ? 0.5404 0.5812 0.6068 -0.0043 0.0088  -0.011  338 PHE   A CE2   
2247 C  CZ    . PHE   A 338 ? 0.5397 0.5791 0.6005 -0.0055 0.0066  -0.0162 338 PHE   A CZ    
2248 N  N     . GLY   A 339 ? 0.499  0.5626 0.5597 -0.0052 0.0068  0.0066  339 GLY   A N     
2249 C  CA    . GLY   A 339 ? 0.4888 0.5518 0.5502 -0.0039 0.0107  0.0109  339 GLY   A CA    
2250 C  C     . GLY   A 339 ? 0.4919 0.5543 0.5442 -0.003  0.0132  0.0105  339 GLY   A C     
2251 O  O     . GLY   A 339 ? 0.4892 0.5471 0.54   -0.0023 0.0168  0.0121  339 GLY   A O     
2252 N  N     . LEU   A 340 ? 0.4939 0.5597 0.5396 -0.0033 0.0114  0.0087  340 LEU   A N     
2253 C  CA    . LEU   A 340 ? 0.4934 0.5599 0.5333 -0.0027 0.0137  0.0087  340 LEU   A CA    
2254 C  C     . LEU   A 340 ? 0.4849 0.5494 0.5249 -0.0016 0.0151  0.0062  340 LEU   A C     
2255 O  O     . LEU   A 340 ? 0.4848 0.547  0.5242 -0.0015 0.0165  0.0082  340 LEU   A O     
2256 C  CB    . LEU   A 340 ? 0.4988 0.5691 0.5321 -0.0034 0.0127  0.0081  340 LEU   A CB    
2257 C  CG    . LEU   A 340 ? 0.5175 0.5894 0.5496 -0.0041 0.0117  0.0125  340 LEU   A CG    
2258 C  CD1   . LEU   A 340 ? 0.5221 0.5963 0.5455 -0.0051 0.0105  0.0119  340 LEU   A CD1   
2259 C  CD2   . LEU   A 340 ? 0.5203 0.5901 0.553  -0.0037 0.015   0.0157  340 LEU   A CD2   
2260 N  N     . PRO   A 341 ? 0.4746 0.539  0.5153 -0.001  0.0146  0.0022  341 PRO   A N     
2261 C  CA    . PRO   A 341 ? 0.4724 0.535  0.5157 0.0005  0.0159  0.0008  341 PRO   A CA    
2262 C  C     . PRO   A 341 ? 0.4774 0.5346 0.5236 0.0006  0.0158  0.003   341 PRO   A C     
2263 O  O     . PRO   A 341 ? 0.4886 0.5442 0.5353 0.0012  0.0157  0.0044  341 PRO   A O     
2264 C  CB    . PRO   A 341 ? 0.4854 0.5472 0.5287 0.0012  0.0161  -0.0041 341 PRO   A CB    
2265 C  CG    . PRO   A 341 ? 0.491  0.5523 0.5321 -0.0009 0.0132  -0.005  341 PRO   A CG    
2266 C  CD    . PRO   A 341 ? 0.4659 0.5306 0.5046 -0.002  0.0123  -0.0012 341 PRO   A CD    
2267 N  N     . THR   A 342 ? 0.4706 0.5247 0.5188 -0.0002 0.0156  0.0037  342 THR   A N     
2268 C  CA    . THR   A 342 ? 0.483  0.5301 0.5319 -0.0002 0.017   0.0061  342 THR   A CA    
2269 C  C     . THR   A 342 ? 0.4718 0.5154 0.515  -0.001  0.0186  0.0097  342 THR   A C     
2270 O  O     . THR   A 342 ? 0.4673 0.5046 0.5061 -0.0012 0.0186  0.0112  342 THR   A O     
2271 C  CB    . THR   A 342 ? 0.5294 0.5741 0.5838 -0.0009 0.0179  0.0063  342 THR   A CB    
2272 O  OG1   . THR   A 342 ? 0.5573 0.6039 0.6158 -0.0011 0.0156  0.0026  342 THR   A OG1   
2273 C  CG2   . THR   A 342 ? 0.5573 0.5934 0.6112 -0.0009 0.0207  0.0085  342 THR   A CG2   
2274 N  N     . SER   A 343 ? 0.4645 0.5109 0.5068 -0.0016 0.0195  0.0113  343 SER   A N     
2275 C  CA    . SER   A 343 ? 0.4726 0.5141 0.5085 -0.0025 0.0215  0.0142  343 SER   A CA    
2276 C  C     . SER   A 343 ? 0.4798 0.521  0.5106 -0.0032 0.0192  0.0144  343 SER   A C     
2277 O  O     . SER   A 343 ? 0.4894 0.5225 0.5132 -0.0046 0.0193  0.0163  343 SER   A O     
2278 C  CB    . SER   A 343 ? 0.4839 0.5289 0.5209 -0.0026 0.0227  0.0159  343 SER   A CB    
2279 O  OG    . SER   A 343 ? 0.5183 0.5632 0.5625 -0.0021 0.0245  0.0171  343 SER   A OG    
2280 N  N     . ARG   A 344 ? 0.4734 0.523  0.5079 -0.0026 0.0171  0.0126  344 ARG   A N     
2281 C  CA    . ARG   A 344 ? 0.4873 0.5386 0.5215 -0.0033 0.015   0.0134  344 ARG   A CA    
2282 C  C     . ARG   A 344 ? 0.4901 0.5372 0.5257 -0.0029 0.0124  0.0138  344 ARG   A C     
2283 O  O     . ARG   A 344 ? 0.5003 0.5435 0.5328 -0.0047 0.0094  0.0163  344 ARG   A O     
2284 C  CB    . ARG   A 344 ? 0.5049 0.5656 0.5438 -0.0023 0.0154  0.0117  344 ARG   A CB    
2285 C  CG    . ARG   A 344 ? 0.5543 0.6184 0.596  -0.0033 0.0141  0.0135  344 ARG   A CG    
2286 C  CD    . ARG   A 344 ? 0.597  0.6685 0.6465 -0.0012 0.0157  0.0114  344 ARG   A CD    
2287 N  NE    . ARG   A 344 ? 0.6434 0.7207 0.6927 -0.0016 0.0187  0.0114  344 ARG   A NE    
2288 C  CZ    . ARG   A 344 ? 0.6725 0.7545 0.7248 0.0002  0.0226  0.0088  344 ARG   A CZ    
2289 N  NH1   . ARG   A 344 ? 0.6265 0.7076 0.6823 0.0026  0.0238  0.0056  344 ARG   A NH1   
2290 N  NH2   . ARG   A 344 ? 0.6735 0.7594 0.724  -0.0005 0.0259  0.0094  344 ARG   A NH2   
2291 N  N     . ALA   A 345 ? 0.4774 0.5242 0.5173 -0.001  0.0128  0.0117  345 ALA   A N     
2292 C  CA    . ALA   A 345 ? 0.4754 0.5172 0.5168 -0.0004 0.0104  0.0126  345 ALA   A CA    
2293 C  C     . ALA   A 345 ? 0.4927 0.5226 0.5237 -0.0027 0.0098  0.0157  345 ALA   A C     
2294 O  O     . ALA   A 345 ? 0.5041 0.529  0.5314 -0.004  0.0057  0.0184  345 ALA   A O     
2295 C  CB    . ALA   A 345 ? 0.4611 0.5032 0.5082 0.0017  0.0117  0.0097  345 ALA   A CB    
2296 N  N     . TYR   A 346 ? 0.4976 0.5225 0.5238 -0.0033 0.014   0.0156  346 TYR   A N     
2297 C  CA    . TYR   A 346 ? 0.5322 0.5437 0.5467 -0.0053 0.0158  0.0181  346 TYR   A CA    
2298 C  C     . TYR   A 346 ? 0.5513 0.5576 0.5557 -0.0081 0.0134  0.0202  346 TYR   A C     
2299 O  O     . TYR   A 346 ? 0.565  0.5605 0.559  -0.0103 0.0104  0.0224  346 TYR   A O     
2300 C  CB    . TYR   A 346 ? 0.543  0.5511 0.5573 -0.0049 0.0224  0.018   346 TYR   A CB    
2301 C  CG    . TYR   A 346 ? 0.5653 0.5747 0.5881 -0.0034 0.0247  0.0167  346 TYR   A CG    
2302 C  CD1   . TYR   A 346 ? 0.5821 0.5919 0.6085 -0.0025 0.0217  0.0158  346 TYR   A CD1   
2303 C  CD2   . TYR   A 346 ? 0.5909 0.601  0.6196 -0.003  0.0296  0.017   346 TYR   A CD2   
2304 C  CE1   . TYR   A 346 ? 0.5978 0.6077 0.6318 -0.0016 0.0236  0.0145  346 TYR   A CE1   
2305 C  CE2   . TYR   A 346 ? 0.6112 0.6222 0.6488 -0.0024 0.0311  0.0162  346 TYR   A CE2   
2306 C  CZ    . TYR   A 346 ? 0.6231 0.6336 0.6626 -0.0019 0.0281  0.0147  346 TYR   A CZ    
2307 O  OH    . TYR   A 346 ? 0.65   0.6613 0.6987 -0.0017 0.0292  0.0137  346 TYR   A OH    
2308 N  N     . ALA   A 347 ? 0.5543 0.5673 0.5608 -0.0085 0.014   0.0198  347 ALA   A N     
2309 C  CA    . ALA   A 347 ? 0.5677 0.5761 0.5657 -0.0117 0.0116  0.0216  347 ALA   A CA    
2310 C  C     . ALA   A 347 ? 0.5776 0.5876 0.5771 -0.0134 0.0038  0.0233  347 ALA   A C     
2311 O  O     . ALA   A 347 ? 0.5915 0.5902 0.5791 -0.017  -0.0001 0.0255  347 ALA   A O     
2312 C  CB    . ALA   A 347 ? 0.5551 0.5719 0.5576 -0.0114 0.0137  0.021   347 ALA   A CB    
2313 N  N     . GLU   A 348 ? 0.5688 0.5914 0.5826 -0.011  0.0015  0.0226  348 GLU   A N     
2314 C  CA    . GLU   A 348 ? 0.5757 0.6015 0.5958 -0.012  -0.0056 0.025   348 GLU   A CA    
2315 C  C     . GLU   A 348 ? 0.5907 0.6062 0.6048 -0.0128 -0.0102 0.0273  348 GLU   A C     
2316 O  O     . GLU   A 348 ? 0.5912 0.6021 0.6021 -0.0159 -0.0177 0.0308  348 GLU   A O     
2317 C  CB    . GLU   A 348 ? 0.5775 0.6183 0.6152 -0.0087 -0.0047 0.0237  348 GLU   A CB    
2318 C  CG    . GLU   A 348 ? 0.6204 0.6698 0.6616 -0.0089 -0.0012 0.0225  348 GLU   A CG    
2319 C  CD    . GLU   A 348 ? 0.6751 0.7373 0.7311 -0.006  0.0011  0.0212  348 GLU   A CD    
2320 O  OE1   . GLU   A 348 ? 0.6885 0.7535 0.754  -0.0034 0.0002  0.0211  348 GLU   A OE1   
2321 O  OE2   . GLU   A 348 ? 0.6905 0.7589 0.7481 -0.0063 0.0045  0.0206  348 GLU   A OE2   
2322 N  N     . TYR   A 349 ? 0.596  0.6066 0.6075 -0.0106 -0.0061 0.0258  349 TYR   A N     
2323 C  CA    . TYR   A 349 ? 0.6077 0.6068 0.6118 -0.0112 -0.0094 0.0282  349 TYR   A CA    
2324 C  C     . TYR   A 349 ? 0.6365 0.6185 0.6194 -0.0161 -0.0119 0.0308  349 TYR   A C     
2325 O  O     . TYR   A 349 ? 0.6482 0.6214 0.6238 -0.0186 -0.0193 0.0344  349 TYR   A O     
2326 C  CB    . TYR   A 349 ? 0.6014 0.5981 0.6065 -0.0084 -0.0028 0.0258  349 TYR   A CB    
2327 C  CG    . TYR   A 349 ? 0.6155 0.5989 0.6116 -0.0091 -0.0044 0.0284  349 TYR   A CG    
2328 C  CD1   . TYR   A 349 ? 0.6203 0.605  0.6237 -0.0078 -0.0106 0.0308  349 TYR   A CD1   
2329 C  CD2   . TYR   A 349 ? 0.6362 0.6052 0.6172 -0.0107 0.0013  0.0287  349 TYR   A CD2   
2330 C  CE1   . TYR   A 349 ? 0.642  0.6138 0.6366 -0.0083 -0.0121 0.0336  349 TYR   A CE1   
2331 C  CE2   . TYR   A 349 ? 0.6569 0.6123 0.6278 -0.0115 0.0007  0.0314  349 TYR   A CE2   
2332 C  CZ    . TYR   A 349 ? 0.6683 0.625  0.6455 -0.0105 -0.0065 0.0339  349 TYR   A CZ    
2333 O  OH    . TYR   A 349 ? 0.7012 0.6435 0.6676 -0.0114 -0.0074 0.0371  349 TYR   A OH    
2334 N  N     . LEU   A 350 ? 0.6473 0.6238 0.62   -0.0178 -0.0062 0.0292  350 LEU   A N     
2335 C  CA    . LEU   A 350 ? 0.6646 0.6224 0.6147 -0.0225 -0.0067 0.0308  350 LEU   A CA    
2336 C  C     . LEU   A 350 ? 0.6767 0.6342 0.6227 -0.027  -0.0139 0.0323  350 LEU   A C     
2337 O  O     . LEU   A 350 ? 0.7158 0.6572 0.642  -0.0313 -0.0136 0.0326  350 LEU   A O     
2338 C  CB    . LEU   A 350 ? 0.6728 0.6231 0.6149 -0.0217 0.0046  0.0285  350 LEU   A CB    
2339 C  CG    . LEU   A 350 ? 0.6897 0.6389 0.6362 -0.0182 0.0118  0.0275  350 LEU   A CG    
2340 C  CD1   . LEU   A 350 ? 0.6959 0.6429 0.6423 -0.0167 0.0223  0.0259  350 LEU   A CD1   
2341 C  CD2   . LEU   A 350 ? 0.7047 0.6371 0.6358 -0.0201 0.0104  0.03    350 LEU   A CD2   
2342 N  N     . GLY   A 351 ? 0.6469 0.6207 0.6111 -0.0261 -0.0196 0.0331  351 GLY   A N     
2343 C  CA    . GLY   A 351 ? 0.641  0.616  0.6049 -0.0307 -0.0269 0.0352  351 GLY   A CA    
2344 C  C     . GLY   A 351 ? 0.635  0.6163 0.602  -0.031  -0.0216 0.033   351 GLY   A C     
2345 O  O     . GLY   A 351 ? 0.6536 0.6343 0.6193 -0.0353 -0.0268 0.0346  351 GLY   A O     
2346 N  N     . GLY   A 352 ? 0.6049 0.5925 0.5773 -0.0266 -0.012  0.0299  352 GLY   A N     
2347 C  CA    . GLY   A 352 ? 0.5877 0.5811 0.5634 -0.0264 -0.007  0.0285  352 GLY   A CA    
2348 C  C     . GLY   A 352 ? 0.5575 0.5704 0.5531 -0.0224 -0.0051 0.0274  352 GLY   A C     
2349 O  O     . GLY   A 352 ? 0.5497 0.5722 0.558  -0.021  -0.0092 0.0283  352 GLY   A O     
2350 N  N     . SER   A 353 ? 0.534  0.5517 0.5318 -0.0204 0.0015  0.0257  353 SER   A N     
2351 C  CA    . SER   A 353 ? 0.5178 0.5511 0.5298 -0.0172 0.0039  0.0245  353 SER   A CA    
2352 C  C     . SER   A 353 ? 0.5051 0.5403 0.5162 -0.015  0.0104  0.023   353 SER   A C     
2353 O  O     . SER   A 353 ? 0.5134 0.539  0.5154 -0.0159 0.0135  0.0235  353 SER   A O     
2354 C  CB    . SER   A 353 ? 0.5241 0.5651 0.5436 -0.0196 0.0008  0.0264  353 SER   A CB    
2355 O  OG    . SER   A 353 ? 0.5549 0.5891 0.5656 -0.0231 0.0013  0.0276  353 SER   A OG    
2356 N  N     . LEU   A 354 ? 0.4825 0.529  0.5028 -0.0121 0.0123  0.0215  354 LEU   A N     
2357 C  CA    . LEU   A 354 ? 0.4785 0.528  0.4988 -0.0104 0.0164  0.0209  354 LEU   A CA    
2358 C  C     . LEU   A 354 ? 0.4798 0.5393 0.5054 -0.0102 0.0169  0.0209  354 LEU   A C     
2359 O  O     . LEU   A 354 ? 0.4712 0.5376 0.5035 -0.0088 0.0166  0.0193  354 LEU   A O     
2360 C  CB    . LEU   A 354 ? 0.4715 0.5225 0.495  -0.0076 0.0178  0.0188  354 LEU   A CB    
2361 C  CG    . LEU   A 354 ? 0.4939 0.5472 0.5181 -0.0064 0.0202  0.0192  354 LEU   A CG    
2362 C  CD1   . LEU   A 354 ? 0.5133 0.5576 0.5333 -0.007  0.0232  0.0215  354 LEU   A CD1   
2363 C  CD2   . LEU   A 354 ? 0.494  0.5507 0.5232 -0.0045 0.0198  0.017   354 LEU   A CD2   
2364 N  N     . GLN   A 355 ? 0.4729 0.5321 0.4955 -0.0117 0.0185  0.0229  355 GLN   A N     
2365 C  CA    . GLN   A 355 ? 0.4683 0.5353 0.4941 -0.012  0.0199  0.0236  355 GLN   A CA    
2366 C  C     . GLN   A 355 ? 0.4787 0.5465 0.5008 -0.0111 0.0222  0.0245  355 GLN   A C     
2367 O  O     . GLN   A 355 ? 0.4926 0.5545 0.5111 -0.0112 0.0228  0.0261  355 GLN   A O     
2368 C  CB    . GLN   A 355 ? 0.4748 0.5407 0.5014 -0.0156 0.0186  0.0261  355 GLN   A CB    
2369 C  CG    . GLN   A 355 ? 0.5151 0.5822 0.5479 -0.0167 0.0146  0.0261  355 GLN   A CG    
2370 C  CD    . GLN   A 355 ? 0.5609 0.6262 0.5953 -0.0211 0.0112  0.029   355 GLN   A CD    
2371 O  OE1   . GLN   A 355 ? 0.5777 0.6399 0.6079 -0.0237 0.0124  0.0307  355 GLN   A OE1   
2372 N  NE2   . GLN   A 355 ? 0.5543 0.6212 0.5957 -0.0224 0.0062  0.0299  355 GLN   A NE2   
2373 N  N     . LEU   A 356 ? 0.48   0.5544 0.5028 -0.0102 0.0238  0.0237  356 LEU   A N     
2374 C  CA    . LEU   A 356 ? 0.5032 0.5781 0.5212 -0.0096 0.0246  0.025   356 LEU   A CA    
2375 C  C     . LEU   A 356 ? 0.493  0.5703 0.5084 -0.0112 0.0271  0.0275  356 LEU   A C     
2376 O  O     . LEU   A 356 ? 0.4881 0.5698 0.5061 -0.0116 0.0295  0.0266  356 LEU   A O     
2377 C  CB    . LEU   A 356 ? 0.532  0.6096 0.5486 -0.0078 0.0238  0.0219  356 LEU   A CB    
2378 C  CG    . LEU   A 356 ? 0.5939 0.669  0.6126 -0.0065 0.021   0.0207  356 LEU   A CG    
2379 C  CD1   . LEU   A 356 ? 0.6083 0.6807 0.6316 -0.0061 0.0207  0.0191  356 LEU   A CD1   
2380 C  CD2   . LEU   A 356 ? 0.6132 0.6902 0.6292 -0.0058 0.0194  0.0175  356 LEU   A CD2   
2381 N  N     . GLN   A 357 ? 0.4874 0.5617 0.4987 -0.0117 0.0271  0.031   357 GLN   A N     
2382 C  CA    . GLN   A 357 ? 0.488  0.5634 0.4954 -0.0132 0.0296  0.034   357 GLN   A CA    
2383 C  C     . GLN   A 357 ? 0.5018 0.5765 0.5023 -0.0122 0.0281  0.0359  357 GLN   A C     
2384 O  O     . GLN   A 357 ? 0.5157 0.5872 0.517  -0.0114 0.0257  0.0386  357 GLN   A O     
2385 C  CB    . GLN   A 357 ? 0.4811 0.552  0.4895 -0.0155 0.0305  0.0374  357 GLN   A CB    
2386 C  CG    . GLN   A 357 ? 0.4678 0.5399 0.4819 -0.0179 0.0308  0.0364  357 GLN   A CG    
2387 C  CD    . GLN   A 357 ? 0.4653 0.544  0.483  -0.0192 0.0341  0.0369  357 GLN   A CD    
2388 O  OE1   . GLN   A 357 ? 0.4877 0.5679 0.5006 -0.019  0.0373  0.0385  357 GLN   A OE1   
2389 N  NE2   . GLN   A 357 ? 0.42   0.5022 0.4465 -0.0207 0.0336  0.0362  357 GLN   A NE2   
2390 N  N     . SER   A 358 ? 0.4983 0.5753 0.4922 -0.0124 0.0295  0.0348  358 SER   A N     
2391 C  CA    . SER   A 358 ? 0.5018 0.577  0.4864 -0.0123 0.0266  0.0366  358 SER   A CA    
2392 C  C     . SER   A 358 ? 0.5064 0.5795 0.4832 -0.0139 0.0288  0.0414  358 SER   A C     
2393 O  O     . SER   A 358 ? 0.496  0.5703 0.4709 -0.0152 0.0344  0.0411  358 SER   A O     
2394 C  CB    . SER   A 358 ? 0.5241 0.5998 0.5016 -0.012  0.0264  0.0319  358 SER   A CB    
2395 O  OG    . SER   A 358 ? 0.5617 0.6341 0.5283 -0.0128 0.0217  0.0338  358 SER   A OG    
2396 N  N     . LEU   A 359 ? 0.5121 0.5822 0.4858 -0.0138 0.0246  0.0463  359 LEU   A N     
2397 C  CA    . LEU   A 359 ? 0.5333 0.6002 0.4987 -0.0152 0.0257  0.0518  359 LEU   A CA    
2398 C  C     . LEU   A 359 ? 0.5507 0.6152 0.5042 -0.0156 0.0199  0.0532  359 LEU   A C     
2399 O  O     . LEU   A 359 ? 0.5577 0.6211 0.5144 -0.0148 0.0134  0.0574  359 LEU   A O     
2400 C  CB    . LEU   A 359 ? 0.5471 0.6113 0.5199 -0.0147 0.025   0.0572  359 LEU   A CB    
2401 C  CG    . LEU   A 359 ? 0.5853 0.6489 0.5658 -0.0157 0.0301  0.0564  359 LEU   A CG    
2402 C  CD1   . LEU   A 359 ? 0.5979 0.6622 0.5879 -0.0143 0.0291  0.0523  359 LEU   A CD1   
2403 C  CD2   . LEU   A 359 ? 0.6019 0.66   0.5838 -0.0161 0.031   0.0623  359 LEU   A CD2   
2404 N  N     . GLN   A 360 ? 0.5535 0.6164 0.4939 -0.0169 0.022   0.0496  360 GLN   A N     
2405 C  CA    . GLN   A 360 ? 0.5598 0.6181 0.4851 -0.0183 0.0157  0.0499  360 GLN   A CA    
2406 C  C     . GLN   A 360 ? 0.5766 0.6303 0.4935 -0.0195 0.0106  0.0579  360 GLN   A C     
2407 O  O     . GLN   A 360 ? 0.5814 0.6323 0.4921 -0.0205 0.0156  0.0618  360 GLN   A O     
2408 C  CB    . GLN   A 360 ? 0.5662 0.6205 0.4756 -0.0197 0.0212  0.0443  360 GLN   A CB    
2409 C  CG    . GLN   A 360 ? 0.5595 0.6176 0.4776 -0.0181 0.0246  0.0367  360 GLN   A CG    
2410 C  CD    . GLN   A 360 ? 0.5916 0.6551 0.5224 -0.0169 0.0338  0.035   360 GLN   A CD    
2411 O  OE1   . GLN   A 360 ? 0.5994 0.664  0.5335 -0.0175 0.0379  0.0393  360 GLN   A OE1   
2412 N  NE2   . GLN   A 360 ? 0.5744 0.6411 0.5135 -0.0153 0.0365  0.0292  360 GLN   A NE2   
2413 N  N     . GLY   A 361 ? 0.5787 0.632  0.497  -0.0195 0.0002  0.0609  361 GLY   A N     
2414 C  CA    . GLY   A 361 ? 0.5866 0.6363 0.5005 -0.0202 -0.0068 0.0696  361 GLY   A CA    
2415 C  C     . GLY   A 361 ? 0.5861 0.6402 0.5219 -0.0172 -0.0087 0.0749  361 GLY   A C     
2416 O  O     . GLY   A 361 ? 0.5948 0.6478 0.5337 -0.0169 -0.0166 0.0824  361 GLY   A O     
2417 N  N     . ILE   A 362 ? 0.5649 0.6231 0.5159 -0.015  -0.0015 0.0714  362 ILE   A N     
2418 C  CA    . ILE   A 362 ? 0.5532 0.6128 0.5224 -0.0122 -0.0009 0.0755  362 ILE   A CA    
2419 C  C     . ILE   A 362 ? 0.545  0.6088 0.5301 -0.01   -0.0013 0.0714  362 ILE   A C     
2420 O  O     . ILE   A 362 ? 0.5477 0.6132 0.5452 -0.0082 -0.0066 0.0755  362 ILE   A O     
2421 C  CB    . ILE   A 362 ? 0.5593 0.6161 0.5298 -0.0122 0.0078  0.0767  362 ILE   A CB    
2422 C  CG1   . ILE   A 362 ? 0.571  0.6229 0.5281 -0.0141 0.0082  0.0827  362 ILE   A CG1   
2423 C  CG2   . ILE   A 362 ? 0.5567 0.6123 0.5441 -0.0094 0.01    0.0793  362 ILE   A CG2   
2424 C  CD1   . ILE   A 362 ? 0.5815 0.6306 0.5405 -0.013  0.0009  0.0915  362 ILE   A CD1   
2425 N  N     . GLY   A 363 ? 0.5325 0.598  0.5186 -0.0101 0.0043  0.0643  363 GLY   A N     
2426 C  CA    . GLY   A 363 ? 0.5175 0.5853 0.5168 -0.0082 0.005   0.0607  363 GLY   A CA    
2427 C  C     . GLY   A 363 ? 0.5136 0.5821 0.5118 -0.0087 0.011   0.0538  363 GLY   A C     
2428 O  O     . GLY   A 363 ? 0.5082 0.5771 0.497  -0.0104 0.0141  0.0512  363 GLY   A O     
2429 N  N     . THR   A 364 ? 0.507  0.5757 0.5154 -0.0072 0.0126  0.0512  364 THR   A N     
2430 C  CA    . THR   A 364 ? 0.5049 0.574  0.5132 -0.0077 0.0165  0.0453  364 THR   A CA    
2431 C  C     . THR   A 364 ? 0.5064 0.5708 0.5212 -0.0069 0.0207  0.0455  364 THR   A C     
2432 O  O     . THR   A 364 ? 0.5107 0.5722 0.5331 -0.005  0.021   0.0481  364 THR   A O     
2433 C  CB    . THR   A 364 ? 0.517  0.5892 0.5271 -0.0072 0.0132  0.0409  364 THR   A CB    
2434 O  OG1   . THR   A 364 ? 0.5327 0.6065 0.5336 -0.0086 0.0092  0.0404  364 THR   A OG1   
2435 C  CG2   . THR   A 364 ? 0.5218 0.5944 0.5326 -0.0073 0.0165  0.0352  364 THR   A CG2   
2436 N  N     . ASP   A 365 ? 0.5066 0.5693 0.5185 -0.0084 0.024   0.0427  365 ASP   A N     
2437 C  CA    . ASP   A 365 ? 0.5094 0.5654 0.5233 -0.0087 0.0271  0.0418  365 ASP   A CA    
2438 C  C     . ASP   A 365 ? 0.5032 0.5609 0.5181 -0.0088 0.0263  0.0369  365 ASP   A C     
2439 O  O     . ASP   A 365 ? 0.4981 0.5608 0.5114 -0.0098 0.0254  0.0344  365 ASP   A O     
2440 C  CB    . ASP   A 365 ? 0.5317 0.5836 0.5413 -0.0114 0.0296  0.0429  365 ASP   A CB    
2441 C  CG    . ASP   A 365 ? 0.6237 0.6722 0.6321 -0.0113 0.031   0.048   365 ASP   A CG    
2442 O  OD1   . ASP   A 365 ? 0.6201 0.6664 0.6328 -0.0088 0.0311  0.0509  365 ASP   A OD1   
2443 O  OD2   . ASP   A 365 ? 0.695  0.7435 0.6997 -0.0137 0.0322  0.0495  365 ASP   A OD2   
2444 N  N     . VAL   A 366 ? 0.4978 0.5508 0.5158 -0.0076 0.0272  0.0359  366 VAL   A N     
2445 C  CA    . VAL   A 366 ? 0.4969 0.5499 0.5153 -0.0077 0.0264  0.0319  366 VAL   A CA    
2446 C  C     . VAL   A 366 ? 0.4878 0.5307 0.5014 -0.0094 0.0287  0.0316  366 VAL   A C     
2447 O  O     . VAL   A 366 ? 0.4787 0.5131 0.4908 -0.009  0.0323  0.0334  366 VAL   A O     
2448 C  CB    . VAL   A 366 ? 0.5114 0.5664 0.5359 -0.0055 0.0253  0.031   366 VAL   A CB    
2449 C  CG1   . VAL   A 366 ? 0.5179 0.5715 0.5422 -0.0057 0.0249  0.0273  366 VAL   A CG1   
2450 C  CG2   . VAL   A 366 ? 0.5214 0.5844 0.5477 -0.005  0.0215  0.0311  366 VAL   A CG2   
2451 N  N     . TYR   A 367 ? 0.4844 0.5273 0.4953 -0.0116 0.0266  0.0295  367 TYR   A N     
2452 C  CA    . TYR   A 367 ? 0.4907 0.5226 0.4944 -0.0143 0.027   0.0293  367 TYR   A CA    
2453 C  C     . TYR   A 367 ? 0.5    0.5285 0.5022 -0.0141 0.0253  0.0271  367 TYR   A C     
2454 O  O     . TYR   A 367 ? 0.5018 0.537  0.508  -0.0144 0.0216  0.0257  367 TYR   A O     
2455 C  CB    . TYR   A 367 ? 0.4833 0.5163 0.4852 -0.018  0.0244  0.0301  367 TYR   A CB    
2456 C  CG    . TYR   A 367 ? 0.4846 0.5193 0.4868 -0.0187 0.0264  0.0328  367 TYR   A CG    
2457 C  CD1   . TYR   A 367 ? 0.4862 0.5317 0.4937 -0.0171 0.0267  0.0336  367 TYR   A CD1   
2458 C  CD2   . TYR   A 367 ? 0.4969 0.521  0.4923 -0.0217 0.0278  0.0344  367 TYR   A CD2   
2459 C  CE1   . TYR   A 367 ? 0.4963 0.5427 0.503  -0.018  0.0284  0.0366  367 TYR   A CE1   
2460 C  CE2   . TYR   A 367 ? 0.5053 0.5305 0.5014 -0.0226 0.0296  0.0371  367 TYR   A CE2   
2461 C  CZ    . TYR   A 367 ? 0.515  0.5518 0.517  -0.0206 0.0299  0.0385  367 TYR   A CZ    
2462 O  OH    . TYR   A 367 ? 0.5383 0.5757 0.54   -0.0214 0.0317  0.0418  367 TYR   A OH    
2463 N  N     . LEU   A 368 ? 0.4979 0.5147 0.4941 -0.0139 0.0288  0.0271  368 LEU   A N     
2464 C  CA    . LEU   A 368 ? 0.5037 0.5139 0.4956 -0.0141 0.0281  0.0256  368 LEU   A CA    
2465 C  C     . LEU   A 368 ? 0.526  0.522  0.5039 -0.0184 0.0265  0.0258  368 LEU   A C     
2466 O  O     . LEU   A 368 ? 0.5414 0.5256 0.5102 -0.02   0.0305  0.0265  368 LEU   A O     
2467 C  CB    . LEU   A 368 ? 0.4996 0.5048 0.4934 -0.0113 0.0339  0.0258  368 LEU   A CB    
2468 C  CG    . LEU   A 368 ? 0.53   0.5264 0.5179 -0.0116 0.0345  0.0246  368 LEU   A CG    
2469 C  CD1   . LEU   A 368 ? 0.5234 0.5298 0.5177 -0.0111 0.0285  0.023   368 LEU   A CD1   
2470 C  CD2   . LEU   A 368 ? 0.5362 0.5272 0.5276 -0.009  0.042   0.0253  368 LEU   A CD2   
2471 N  N     . ARG   A 369 ? 0.5282 0.5248 0.5044 -0.0206 0.0203  0.0253  369 ARG   A N     
2472 C  CA    . ARG   A 369 ? 0.5474 0.5301 0.5094 -0.0256 0.0163  0.0259  369 ARG   A CA    
2473 C  C     . ARG   A 369 ? 0.5752 0.5502 0.5305 -0.0259 0.0141  0.0256  369 ARG   A C     
2474 O  O     . ARG   A 369 ? 0.5606 0.546  0.5264 -0.0236 0.0109  0.0254  369 ARG   A O     
2475 C  CB    . ARG   A 369 ? 0.5434 0.534  0.511  -0.029  0.0088  0.0272  369 ARG   A CB    
2476 C  CG    . ARG   A 369 ? 0.5506 0.5472 0.5233 -0.0294 0.0112  0.028   369 ARG   A CG    
2477 C  CD    . ARG   A 369 ? 0.5573 0.5621 0.5376 -0.0331 0.0046  0.0298  369 ARG   A CD    
2478 N  NE    . ARG   A 369 ? 0.5828 0.5874 0.5629 -0.0351 0.0069  0.0309  369 ARG   A NE    
2479 C  CZ    . ARG   A 369 ? 0.5958 0.6124 0.586  -0.0323 0.0108  0.0316  369 ARG   A CZ    
2480 N  NH1   . ARG   A 369 ? 0.5784 0.6077 0.5787 -0.0278 0.0125  0.0307  369 ARG   A NH1   
2481 N  NH2   . ARG   A 369 ? 0.5749 0.5898 0.564  -0.0345 0.0127  0.0332  369 ARG   A NH2   
2482 N  N     . LEU   A 370 ? 0.607  0.5621 0.5436 -0.0286 0.0166  0.0255  370 LEU   A N     
2483 C  CA    . LEU   A 370 ? 0.6328 0.5769 0.5588 -0.0296 0.0149  0.0256  370 LEU   A CA    
2484 C  C     . LEU   A 370 ? 0.6729 0.5976 0.5769 -0.0361 0.0096  0.0264  370 LEU   A C     
2485 O  O     . LEU   A 370 ? 0.684  0.5962 0.5754 -0.0389 0.0131  0.0257  370 LEU   A O     
2486 C  CB    . LEU   A 370 ? 0.6343 0.5709 0.5574 -0.026  0.0254  0.0247  370 LEU   A CB    
2487 C  CG    . LEU   A 370 ? 0.6365 0.5909 0.5806 -0.0205 0.0283  0.0242  370 LEU   A CG    
2488 C  CD1   . LEU   A 370 ? 0.6327 0.5801 0.5767 -0.0176 0.0387  0.0241  370 LEU   A CD1   
2489 C  CD2   . LEU   A 370 ? 0.6324 0.5976 0.5859 -0.0196 0.0208  0.0243  370 LEU   A CD2   
2490 N  N     . ARG   A 371 ? 0.7011 0.6226 0.6002 -0.0387 0.0006  0.0281  371 ARG   A N     
2491 C  CA    . ARG   A 371 ? 0.754  0.6562 0.6308 -0.0459 -0.0071 0.0294  371 ARG   A CA    
2492 C  C     . ARG   A 371 ? 0.7882 0.6636 0.6372 -0.0478 0.0008  0.028   371 ARG   A C     
2493 O  O     . ARG   A 371 ? 0.787  0.6598 0.636  -0.0436 0.0101  0.0272  371 ARG   A O     
2494 C  CB    . ARG   A 371 ? 0.7949 0.7015 0.6759 -0.0478 -0.0198 0.0325  371 ARG   A CB    
2495 C  CG    . ARG   A 371 ? 0.8864 0.8066 0.7821 -0.0509 -0.0311 0.0349  371 ARG   A CG    
2496 C  CD    . ARG   A 371 ? 0.9806 0.9101 0.8889 -0.0506 -0.0419 0.0386  371 ARG   A CD    
2497 N  NE    . ARG   A 371 ? 1.0796 0.9926 0.97   -0.058  -0.0546 0.0421  371 ARG   A NE    
2498 C  CZ    . ARG   A 371 ? 1.1372 1.052  1.0327 -0.0587 -0.0652 0.0464  371 ARG   A CZ    
2499 N  NH1   . ARG   A 371 ? 1.1361 1.0678 1.0539 -0.0521 -0.0634 0.0471  371 ARG   A NH1   
2500 N  NH2   . ARG   A 371 ? 1.1529 1.0514 1.0304 -0.0661 -0.0781 0.0501  371 ARG   A NH2   
2501 N  N     . HIS   A 372 ? 0.8119 0.6664 0.6367 -0.0547 -0.0026 0.0278  372 HIS   A N     
2502 C  CA    . HIS   A 372 ? 0.8531 0.6782 0.6469 -0.0574 0.005   0.0264  372 HIS   A CA    
2503 C  C     . HIS   A 372 ? 0.9059 0.7183 0.6832 -0.0606 -0.0027 0.0287  372 HIS   A C     
2504 O  O     . HIS   A 372 ? 0.8886 0.714  0.678  -0.0616 -0.016  0.0318  372 HIS   A O     
2505 C  CB    . HIS   A 372 ? 0.8576 0.6625 0.6289 -0.0642 0.004   0.0248  372 HIS   A CB    
2506 C  CG    . HIS   A 372 ? 0.8531 0.6598 0.6313 -0.0608 0.0167  0.0222  372 HIS   A CG    
2507 N  ND1   . HIS   A 372 ? 0.8737 0.6699 0.6468 -0.056  0.0334  0.0204  372 HIS   A ND1   
2508 C  CD2   . HIS   A 372 ? 0.849  0.6664 0.6398 -0.0614 0.0149  0.022   372 HIS   A CD2   
2509 C  CE1   . HIS   A 372 ? 0.8685 0.6701 0.6521 -0.0536 0.0404  0.0193  372 HIS   A CE1   
2510 N  NE2   . HIS   A 372 ? 0.8599 0.6734 0.6529 -0.0569 0.0298  0.0201  372 HIS   A NE2   
2511 N  N     . ILE   A 373 ? 0.9651 0.7515 0.7149 -0.0619 0.0061  0.0277  373 ILE   A N     
2512 C  CA    . ILE   A 373 ? 1.0224 0.7922 0.7511 -0.0656 -0.0004 0.0303  373 ILE   A CA    
2513 C  C     . ILE   A 373 ? 1.0935 0.8393 0.791  -0.0755 -0.0117 0.0308  373 ILE   A C     
2514 O  O     . ILE   A 373 ? 1.1177 0.8396 0.7894 -0.079  -0.0032 0.0276  373 ILE   A O     
2515 C  CB    . ILE   A 373 ? 1.04   0.7917 0.7528 -0.0626 0.0161  0.029   373 ILE   A CB    
2516 C  CG1   . ILE   A 373 ? 1.026  0.8019 0.7715 -0.0535 0.0266  0.0286  373 ILE   A CG1   
2517 C  CG2   . ILE   A 373 ? 1.0651 0.7953 0.7507 -0.0671 0.0101  0.0319  373 ILE   A CG2   
2518 C  CD1   . ILE   A 373 ? 1.0441 0.8058 0.7807 -0.0501 0.0437  0.0279  373 ILE   A CD1   
2519 N  N     . ASP   A 374 ? 1.1235 0.8758 0.8247 -0.0802 -0.031  0.0348  374 ASP   A N     
2520 C  CA    . ASP   A 374 ? 1.1769 0.9098 0.8527 -0.0907 -0.0464 0.0365  374 ASP   A CA    
2521 C  C     . ASP   A 374 ? 1.2255 0.9173 0.8532 -0.0973 -0.0396 0.0337  374 ASP   A C     
2522 O  O     . ASP   A 374 ? 1.2521 0.9222 0.8526 -0.1005 -0.042  0.0357  374 ASP   A O     
2523 C  CB    . ASP   A 374 ? 1.2186 0.9597 0.9021 -0.0936 -0.0661 0.0429  374 ASP   A CB    
2524 C  CG    . ASP   A 374 ? 1.3352 1.0563 0.9933 -0.1051 -0.0852 0.046   374 ASP   A CG    
2525 O  OD1   . ASP   A 374 ? 1.3639 1.0798 1.0162 -0.1108 -0.0886 0.0439  374 ASP   A OD1   
2526 O  OD2   . ASP   A 374 ? 1.3738 1.0842 1.0181 -0.1089 -0.0974 0.0509  374 ASP   A OD2   
2527 P  PB    . ADP   B .   ? 0.5126 0.5861 0.5632 -0.0143 -0.0186 0.0108  401 ADP   A PB    
2528 O  O1B   . ADP   B .   ? 0.5185 0.5901 0.5534 -0.0171 -0.0246 0.0098  401 ADP   A O1B   
2529 O  O2B   . ADP   B .   ? 0.515  0.587  0.5751 -0.0162 -0.0215 0.0085  401 ADP   A O2B   
2530 O  O3B   . ADP   B .   ? 0.5123 0.5901 0.5755 -0.0122 -0.0162 0.0176  401 ADP   A O3B   
2531 P  PA    . ADP   B .   ? 0.5055 0.5772 0.5465 -0.0083 -0.0025 0.0085  401 ADP   A PA    
2532 O  O1A   . ADP   B .   ? 0.4855 0.5587 0.5379 -0.0071 -0.0008 0.014   401 ADP   A O1A   
2533 O  O2A   . ADP   B .   ? 0.4947 0.5636 0.5322 -0.0068 0.0021  0.004   401 ADP   A O2A   
2534 O  O3A   . ADP   B .   ? 0.5165 0.5873 0.559  -0.0114 -0.0098 0.0066  401 ADP   A O3A   
2535 O  "O5'" . ADP   B .   ? 0.509  0.5818 0.538  -0.0091 -0.0038 0.0097  401 ADP   A "O5'" 
2536 C  "C5'" . ADP   B .   ? 0.5187 0.5885 0.5336 -0.0104 -0.0042 0.005   401 ADP   A "C5'" 
2537 C  "C4'" . ADP   B .   ? 0.5283 0.598  0.5324 -0.0123 -0.0078 0.0077  401 ADP   A "C4'" 
2538 O  "O4'" . ADP   B .   ? 0.5306 0.6028 0.534  -0.0106 -0.0028 0.0112  401 ADP   A "O4'" 
2539 C  "C3'" . ADP   B .   ? 0.5374 0.6091 0.5475 -0.0142 -0.0161 0.013   401 ADP   A "C3'" 
2540 O  "O3'" . ADP   B .   ? 0.5473 0.6159 0.5538 -0.0177 -0.0239 0.0106  401 ADP   A "O3'" 
2541 C  "C2'" . ADP   B .   ? 0.5431 0.6149 0.5432 -0.0147 -0.0167 0.0171  401 ADP   A "C2'" 
2542 O  "O2'" . ADP   B .   ? 0.5557 0.6218 0.5362 -0.0174 -0.019  0.0139  401 ADP   A "O2'" 
2543 C  "C1'" . ADP   B .   ? 0.536  0.6091 0.5366 -0.0118 -0.0072 0.0166  401 ADP   A "C1'" 
2544 N  N9    . ADP   B .   ? 0.5281 0.6044 0.5408 -0.0098 -0.005  0.0219  401 ADP   A N9    
2545 C  C8    . ADP   B .   ? 0.526  0.6029 0.5502 -0.0078 -0.0009 0.0219  401 ADP   A C8    
2546 N  N7    . ADP   B .   ? 0.5209 0.598  0.5512 -0.0065 0.0015  0.0266  401 ADP   A N7    
2547 C  C5    . ADP   B .   ? 0.5193 0.5972 0.5437 -0.0075 -0.0015 0.0305  401 ADP   A C5    
2548 C  C6    . ADP   B .   ? 0.5145 0.5922 0.5413 -0.0067 -0.0008 0.0364  401 ADP   A C6    
2549 N  N6    . ADP   B .   ? 0.503  0.579  0.5387 -0.0048 0.0041  0.039   401 ADP   A N6    
2550 N  N1    . ADP   B .   ? 0.522  0.5997 0.5402 -0.0081 -0.0048 0.0396  401 ADP   A N1    
2551 C  C2    . ADP   B .   ? 0.5254 0.6023 0.5314 -0.0105 -0.0091 0.0366  401 ADP   A C2    
2552 N  N3    . ADP   B .   ? 0.5292 0.6051 0.5309 -0.0114 -0.0096 0.0304  401 ADP   A N3    
2553 C  C4    . ADP   B .   ? 0.5238 0.6009 0.5364 -0.0097 -0.0058 0.0277  401 ADP   A C4    
2554 MG MG    . MG    C .   ? 0.5926 0.6691 0.6662 -0.0077 -0.0042 0.0207  402 MG    A MG    
2555 K  K     . K     D .   ? 0.9634 1.0267 0.9814 -0.0073 0.0042  -0.0065 403 K     A K     
2556 C  C4    . A1A40 E .   ? 0.6351 0.5747 0.67   -0.0015 0.0324  0.0263  404 A1A40 A C4    
2557 C  C7    . A1A40 E .   ? 0.638  0.5673 0.6853 -0.0001 0.0316  0.0272  404 A1A40 A C7    
2558 C  C6    . A1A40 E .   ? 0.6312 0.5568 0.6736 -0.0027 0.0385  0.0287  404 A1A40 A C6    
2559 C  C13   . A1A40 E .   ? 0.6498 0.5413 0.6487 -0.0073 0.0511  0.0401  404 A1A40 A C13   
2560 C  C20   . A1A40 E .   ? 0.5989 0.5498 0.6524 -0.0052 0.0478  0.0238  404 A1A40 A C20   
2561 C  C8    . A1A40 E .   ? 0.6365 0.575  0.6836 0.0019  0.0256  0.0254  404 A1A40 A C8    
2562 C  C16   . A1A40 E .   ? 0.6584 0.5406 0.6489 -0.0104 0.0719  0.0417  404 A1A40 A C16   
2563 C  C19   . A1A40 E .   ? 0.6132 0.5468 0.6523 -0.006  0.0522  0.0286  404 A1A40 A C19   
2564 C  C1    . A1A40 E .   ? 0.625  0.5917 0.6757 0.0032  0.0203  0.0184  404 A1A40 A C1    
2565 O  O2    . A1A40 E .   ? 0.6409 0.5939 0.6818 0.0026  0.0202  0.0238  404 A1A40 A O2    
2566 C  C3    . A1A40 E .   ? 0.6397 0.5837 0.6805 0.001   0.0257  0.025   404 A1A40 A C3    
2567 C  C5    . A1A40 E .   ? 0.6294 0.5599 0.6654 -0.0032 0.0392  0.0283  404 A1A40 A C5    
2568 F  F9    . A1A40 E .   ? 0.6406 0.5825 0.695  0.0049  0.0204  0.0242  404 A1A40 A F9    
2569 F  F10   . A1A40 E .   ? 0.6411 0.5648 0.6952 0.0007  0.0313  0.0273  404 A1A40 A F10   
2570 C  C11   . A1A40 E .   ? 0.6271 0.5516 0.6575 -0.0054 0.0481  0.0306  404 A1A40 A C11   
2571 C  C12   . A1A40 E .   ? 0.6394 0.5452 0.6523 -0.007  0.0539  0.036   404 A1A40 A C12   
2572 C  C14   . A1A40 E .   ? 0.6668 0.5391 0.6455 -0.0095 0.0576  0.045   404 A1A40 A C14   
2573 C  C15   . A1A40 E .   ? 0.6785 0.546  0.6526 -0.0111 0.0684  0.0454  404 A1A40 A C15   
2574 C  C17   . A1A40 E .   ? 0.6413 0.5428 0.6507 -0.0085 0.0637  0.0372  404 A1A40 A C17   
2575 S  S18   . A1A40 E .   ? 0.6201 0.5412 0.6496 -0.0078 0.0644  0.0328  404 A1A40 A S18   
2576 O  O21   . A1A40 E .   ? 0.5881 0.5466 0.649  -0.0041 0.0415  0.0203  404 A1A40 A O21   
2577 O  O22   . A1A40 E .   ? 0.6009 0.5575 0.6593 -0.0059 0.0518  0.0238  404 A1A40 A O22   
2578 F  F23   . A1A40 E .   ? 0.7015 0.5478 0.6538 -0.0133 0.0766  0.0499  404 A1A40 A F23   
2579 F  F24   . A1A40 E .   ? 0.6352 0.5793 0.6645 -0.0022 0.033   0.0259  404 A1A40 A F24   
# 
