data_9H9T
# 
_entry.id   9H9T 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_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   9H9T         pdb_00009h9t 10.2210/pdb9h9t/pdb 
WWPDB D_1292142908 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-06-04 
_pdbx_audit_revision_history.part_number         ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9H9T 
_pdbx_database_status.recvd_initial_deposition_date   2024-10-31 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           N 
# 
_pdbx_database_related.db_name        PDB 
_pdbx_database_related.details        'same protein with lead compound for design of this inhibitor' 
_pdbx_database_related.db_id          9H9O 
_pdbx_database_related.content_type   unspecified 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              simona.polo@ifom.eu 
_pdbx_contact_author.name_first         Simona 
_pdbx_contact_author.name_last          Polo 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0001-5536-9399 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Cecatiello, V.' 1 0000-0003-4015-7160 
'Maspero, E.'    2 0000-0001-6468-4796 
'Polo, S.'       3 0000-0001-5536-9399 
'Pasqualato, S.' 4 0000-0002-9038-7768 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   UK 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'Commun Chem' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           2399-3669 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            8 
_citation.language                  ? 
_citation.page_first                164 
_citation.page_last                 164 
_citation.title                     'Structure-based design of potent and selective inhibitors of the HECT ligase NEDD4.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1038/s42004-025-01557-4 
_citation.pdbx_database_id_PubMed   40437006 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Maspero, E.'     1  0000-0001-6468-4796 
primary 'Cappa, A.'       2  ?                   
primary 'Weber, J.'       3  ?                   
primary 'Trifiro, P.'     4  ?                   
primary 'Amici, R.'       5  ?                   
primary 'Bruno, A.'       6  ?                   
primary 'Faga, G.'        7  0000-0002-7674-2583 
primary 'Cecatiello, V.'  8  ?                   
primary 'Fattori, R.'     9  ?                   
primary 'Leuzzi, B.'      10 0000-0001-5237-2920 
primary 'Taibi, V.'       11 ?                   
primary 'Meroni, G.'      12 ?                   
primary 'Pasi, M.'        13 ?                   
primary 'Romussi, A.'     14 ?                   
primary 'Sartori, L.'     15 ?                   
primary 'Villa, M.'       16 ?                   
primary 'Vultaggio, S.'   17 ?                   
primary 'Ciro, M.'        18 ?                   
primary 'Soffientini, P.' 19 ?                   
primary 'Lombardo, L.'    20 0000-0002-8900-3560 
primary 'Dahe, S.'        21 ?                   
primary 'Bachi, A.'       22 ?                   
primary 'Varasi, M.'      23 ?                   
primary 'Rossi, M.'       24 ?                   
primary 'Pasqualato, S.'  25 0000-0002-9038-7768 
primary 'Mercurio, C.'    26 0000-0001-6240-4607 
primary 'Polo, S.'        27 0000-0001-5536-9399 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Isoform 4 of E3 ubiquitin-protein ligase NEDD4'                                      44739.031 1   2.3.2.26 ? ? 
? 
2 non-polymer syn 'ethyl 4-[4-(2-chloranyl-5,6-dihydrobenzo[b][1]benzazepin-11-yl)butylamino]butanoate' 414.968   1   ?        ? ? 
? 
3 water       nat water                                                                                 18.015    107 ?        ? ? 
? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        
;Cell proliferation-inducing gene 53 protein,HECT-type E3 ubiquitin transferase NEDD4,Neural precursor cell expressed developmentally down-regulated protein 4,NEDD-4
;
# 
_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       
;SRDYKRKYEFFRRKLKKQNDIPNKFEMKLRRATVLEDSYRRIMGVKRADFLKARLWIEFDGEKGLDYGGVAREWFFLISK
EMFNPYYGLFEYSATDNYTLQINPNSGLCNEDHLSYFKFIGRVAGMAVYHGKLLDGFFIRPFYKMMLHKPITLHDMESVD
SEYYNSLRWILENDPTELDLRFIIDEELFGQTHQHELKNGGSEIVVTNKNKKEYIYLVIQWRFVNRIQKQMAAFKEGFFE
LIPQDLIKIFDENELELLMCGLGDVDVNDWREHTKYKNGYSANHQVIQWFWKAVLMMDSEKRIRLLQFVTGTSRVPMNGF
AELYGSNGPQSFTVEQWGTPEKLPRAHTCFNRLDLPPYESFEELWDKLQMAIENT
;
_entity_poly.pdbx_seq_one_letter_code_can   
;SRDYKRKYEFFRRKLKKQNDIPNKFEMKLRRATVLEDSYRRIMGVKRADFLKARLWIEFDGEKGLDYGGVAREWFFLISK
EMFNPYYGLFEYSATDNYTLQINPNSGLCNEDHLSYFKFIGRVAGMAVYHGKLLDGFFIRPFYKMMLHKPITLHDMESVD
SEYYNSLRWILENDPTELDLRFIIDEELFGQTHQHELKNGGSEIVVTNKNKKEYIYLVIQWRFVNRIQKQMAAFKEGFFE
LIPQDLIKIFDENELELLMCGLGDVDVNDWREHTKYKNGYSANHQVIQWFWKAVLMMDSEKRIRLLQFVTGTSRVPMNGF
AELYGSNGPQSFTVEQWGTPEKLPRAHTCFNRLDLPPYESFEELWDKLQMAIENT
;
_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 'ethyl 4-[4-(2-chloranyl-5,6-dihydrobenzo[b][1]benzazepin-11-yl)butylamino]butanoate' A1ITT 
3 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   ARG n 
1 3   ASP n 
1 4   TYR n 
1 5   LYS n 
1 6   ARG n 
1 7   LYS n 
1 8   TYR n 
1 9   GLU n 
1 10  PHE n 
1 11  PHE n 
1 12  ARG n 
1 13  ARG n 
1 14  LYS n 
1 15  LEU n 
1 16  LYS n 
1 17  LYS n 
1 18  GLN n 
1 19  ASN n 
1 20  ASP n 
1 21  ILE n 
1 22  PRO n 
1 23  ASN n 
1 24  LYS n 
1 25  PHE n 
1 26  GLU n 
1 27  MET n 
1 28  LYS n 
1 29  LEU n 
1 30  ARG n 
1 31  ARG n 
1 32  ALA n 
1 33  THR n 
1 34  VAL n 
1 35  LEU n 
1 36  GLU n 
1 37  ASP n 
1 38  SER n 
1 39  TYR n 
1 40  ARG n 
1 41  ARG n 
1 42  ILE n 
1 43  MET n 
1 44  GLY n 
1 45  VAL n 
1 46  LYS n 
1 47  ARG n 
1 48  ALA n 
1 49  ASP n 
1 50  PHE n 
1 51  LEU n 
1 52  LYS n 
1 53  ALA n 
1 54  ARG n 
1 55  LEU n 
1 56  TRP n 
1 57  ILE n 
1 58  GLU n 
1 59  PHE n 
1 60  ASP n 
1 61  GLY n 
1 62  GLU n 
1 63  LYS n 
1 64  GLY n 
1 65  LEU n 
1 66  ASP n 
1 67  TYR n 
1 68  GLY n 
1 69  GLY n 
1 70  VAL n 
1 71  ALA n 
1 72  ARG n 
1 73  GLU n 
1 74  TRP n 
1 75  PHE n 
1 76  PHE n 
1 77  LEU n 
1 78  ILE n 
1 79  SER n 
1 80  LYS n 
1 81  GLU n 
1 82  MET n 
1 83  PHE n 
1 84  ASN n 
1 85  PRO n 
1 86  TYR n 
1 87  TYR n 
1 88  GLY n 
1 89  LEU n 
1 90  PHE n 
1 91  GLU n 
1 92  TYR n 
1 93  SER n 
1 94  ALA n 
1 95  THR n 
1 96  ASP n 
1 97  ASN n 
1 98  TYR n 
1 99  THR n 
1 100 LEU n 
1 101 GLN n 
1 102 ILE n 
1 103 ASN n 
1 104 PRO n 
1 105 ASN n 
1 106 SER n 
1 107 GLY n 
1 108 LEU n 
1 109 CYS n 
1 110 ASN n 
1 111 GLU n 
1 112 ASP n 
1 113 HIS n 
1 114 LEU n 
1 115 SER n 
1 116 TYR n 
1 117 PHE n 
1 118 LYS n 
1 119 PHE n 
1 120 ILE n 
1 121 GLY n 
1 122 ARG n 
1 123 VAL n 
1 124 ALA n 
1 125 GLY n 
1 126 MET n 
1 127 ALA n 
1 128 VAL n 
1 129 TYR n 
1 130 HIS n 
1 131 GLY n 
1 132 LYS n 
1 133 LEU n 
1 134 LEU n 
1 135 ASP n 
1 136 GLY n 
1 137 PHE n 
1 138 PHE n 
1 139 ILE n 
1 140 ARG n 
1 141 PRO n 
1 142 PHE n 
1 143 TYR n 
1 144 LYS n 
1 145 MET n 
1 146 MET n 
1 147 LEU n 
1 148 HIS n 
1 149 LYS n 
1 150 PRO n 
1 151 ILE n 
1 152 THR n 
1 153 LEU n 
1 154 HIS n 
1 155 ASP n 
1 156 MET n 
1 157 GLU n 
1 158 SER n 
1 159 VAL n 
1 160 ASP n 
1 161 SER n 
1 162 GLU n 
1 163 TYR n 
1 164 TYR n 
1 165 ASN n 
1 166 SER n 
1 167 LEU n 
1 168 ARG n 
1 169 TRP n 
1 170 ILE n 
1 171 LEU n 
1 172 GLU n 
1 173 ASN n 
1 174 ASP n 
1 175 PRO n 
1 176 THR n 
1 177 GLU n 
1 178 LEU n 
1 179 ASP n 
1 180 LEU n 
1 181 ARG n 
1 182 PHE n 
1 183 ILE n 
1 184 ILE n 
1 185 ASP n 
1 186 GLU n 
1 187 GLU n 
1 188 LEU n 
1 189 PHE n 
1 190 GLY n 
1 191 GLN n 
1 192 THR n 
1 193 HIS n 
1 194 GLN n 
1 195 HIS n 
1 196 GLU n 
1 197 LEU n 
1 198 LYS n 
1 199 ASN n 
1 200 GLY n 
1 201 GLY n 
1 202 SER n 
1 203 GLU n 
1 204 ILE n 
1 205 VAL n 
1 206 VAL n 
1 207 THR n 
1 208 ASN n 
1 209 LYS n 
1 210 ASN n 
1 211 LYS n 
1 212 LYS n 
1 213 GLU n 
1 214 TYR n 
1 215 ILE n 
1 216 TYR n 
1 217 LEU n 
1 218 VAL n 
1 219 ILE n 
1 220 GLN n 
1 221 TRP n 
1 222 ARG n 
1 223 PHE n 
1 224 VAL n 
1 225 ASN n 
1 226 ARG n 
1 227 ILE n 
1 228 GLN n 
1 229 LYS n 
1 230 GLN n 
1 231 MET n 
1 232 ALA n 
1 233 ALA n 
1 234 PHE n 
1 235 LYS n 
1 236 GLU n 
1 237 GLY n 
1 238 PHE n 
1 239 PHE n 
1 240 GLU n 
1 241 LEU n 
1 242 ILE n 
1 243 PRO n 
1 244 GLN n 
1 245 ASP n 
1 246 LEU n 
1 247 ILE n 
1 248 LYS n 
1 249 ILE n 
1 250 PHE n 
1 251 ASP n 
1 252 GLU n 
1 253 ASN n 
1 254 GLU n 
1 255 LEU n 
1 256 GLU n 
1 257 LEU n 
1 258 LEU n 
1 259 MET n 
1 260 CYS n 
1 261 GLY n 
1 262 LEU n 
1 263 GLY n 
1 264 ASP n 
1 265 VAL n 
1 266 ASP n 
1 267 VAL n 
1 268 ASN n 
1 269 ASP n 
1 270 TRP n 
1 271 ARG n 
1 272 GLU n 
1 273 HIS n 
1 274 THR n 
1 275 LYS n 
1 276 TYR n 
1 277 LYS n 
1 278 ASN n 
1 279 GLY n 
1 280 TYR n 
1 281 SER n 
1 282 ALA n 
1 283 ASN n 
1 284 HIS n 
1 285 GLN n 
1 286 VAL n 
1 287 ILE n 
1 288 GLN n 
1 289 TRP n 
1 290 PHE n 
1 291 TRP n 
1 292 LYS n 
1 293 ALA n 
1 294 VAL n 
1 295 LEU n 
1 296 MET n 
1 297 MET n 
1 298 ASP n 
1 299 SER n 
1 300 GLU n 
1 301 LYS n 
1 302 ARG n 
1 303 ILE n 
1 304 ARG n 
1 305 LEU n 
1 306 LEU n 
1 307 GLN n 
1 308 PHE n 
1 309 VAL n 
1 310 THR n 
1 311 GLY n 
1 312 THR n 
1 313 SER n 
1 314 ARG n 
1 315 VAL n 
1 316 PRO n 
1 317 MET n 
1 318 ASN n 
1 319 GLY n 
1 320 PHE n 
1 321 ALA n 
1 322 GLU n 
1 323 LEU n 
1 324 TYR n 
1 325 GLY n 
1 326 SER n 
1 327 ASN n 
1 328 GLY n 
1 329 PRO n 
1 330 GLN n 
1 331 SER n 
1 332 PHE n 
1 333 THR n 
1 334 VAL n 
1 335 GLU n 
1 336 GLN n 
1 337 TRP n 
1 338 GLY n 
1 339 THR n 
1 340 PRO n 
1 341 GLU n 
1 342 LYS n 
1 343 LEU n 
1 344 PRO n 
1 345 ARG n 
1 346 ALA n 
1 347 HIS n 
1 348 THR n 
1 349 CYS n 
1 350 PHE n 
1 351 ASN n 
1 352 ARG n 
1 353 LEU n 
1 354 ASP n 
1 355 LEU n 
1 356 PRO n 
1 357 PRO n 
1 358 TYR n 
1 359 GLU n 
1 360 SER n 
1 361 PHE n 
1 362 GLU n 
1 363 GLU n 
1 364 LEU n 
1 365 TRP n 
1 366 ASP n 
1 367 LYS n 
1 368 LEU n 
1 369 GLN n 
1 370 MET n 
1 371 ALA n 
1 372 ILE n 
1 373 GLU n 
1 374 ASN n 
1 375 THR 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                   375 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'NEDD4, KIAA0093, NEDD4-1, RPF1, PIG53' 
_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 
A1ITT non-polymer         . 'ethyl 4-[4-(2-chloranyl-5,6-dihydrobenzo[b][1]benzazepin-11-yl)butylamino]butanoate' ? 
'C24 H31 Cl N2 O2' 414.968 
ALA   'L-peptide linking' y ALANINE                                                                               ? 'C3 H7 N O2' 
89.093  
ARG   'L-peptide linking' y ARGININE                                                                              ? 
'C6 H15 N4 O2 1'   175.209 
ASN   'L-peptide linking' y ASPARAGINE                                                                            ? 'C4 H8 N2 O3' 
132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID'                                                                       ? 'C4 H7 N O4' 
133.103 
CYS   'L-peptide linking' y CYSTEINE                                                                              ? 'C3 H7 N O2 S' 
121.158 
GLN   'L-peptide linking' y GLUTAMINE                                                                             ? 'C5 H10 N2 O3' 
146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID'                                                                       ? 'C5 H9 N O4' 
147.129 
GLY   'peptide linking'   y GLYCINE                                                                               ? 'C2 H5 N O2' 
75.067  
HIS   'L-peptide linking' y HISTIDINE                                                                             ? 
'C6 H10 N3 O2 1'   156.162 
HOH   non-polymer         . WATER                                                                                 ? 'H2 O' 18.015  
ILE   'L-peptide linking' y ISOLEUCINE                                                                            ? 'C6 H13 N O2' 
131.173 
LEU   'L-peptide linking' y LEUCINE                                                                               ? 'C6 H13 N O2' 
131.173 
LYS   'L-peptide linking' y LYSINE                                                                                ? 
'C6 H15 N2 O2 1'   147.195 
MET   'L-peptide linking' y METHIONINE                                                                            ? 
'C5 H11 N O2 S'    149.211 
PHE   'L-peptide linking' y PHENYLALANINE                                                                         ? 'C9 H11 N O2' 
165.189 
PRO   'L-peptide linking' y PROLINE                                                                               ? 'C5 H9 N O2' 
115.130 
SER   'L-peptide linking' y SERINE                                                                                ? 'C3 H7 N O3' 
105.093 
THR   'L-peptide linking' y THREONINE                                                                             ? 'C4 H9 N O3' 
119.119 
TRP   'L-peptide linking' y TRYPTOPHAN                                                                            ? 
'C11 H12 N2 O2'    204.225 
TYR   'L-peptide linking' y TYROSINE                                                                              ? 'C9 H11 N O3' 
181.189 
VAL   'L-peptide linking' y VALINE                                                                                ? 'C5 H11 N O2' 
117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   SER 1   519 519 SER SER A . n 
A 1 2   ARG 2   520 520 ARG ARG A . n 
A 1 3   ASP 3   521 521 ASP ASP A . n 
A 1 4   TYR 4   522 522 TYR TYR A . n 
A 1 5   LYS 5   523 523 LYS LYS A . n 
A 1 6   ARG 6   524 524 ARG ARG A . n 
A 1 7   LYS 7   525 525 LYS LYS A . n 
A 1 8   TYR 8   526 526 TYR TYR A . n 
A 1 9   GLU 9   527 527 GLU GLU A . n 
A 1 10  PHE 10  528 528 PHE PHE A . n 
A 1 11  PHE 11  529 529 PHE PHE A . n 
A 1 12  ARG 12  530 530 ARG ARG A . n 
A 1 13  ARG 13  531 531 ARG ARG A . n 
A 1 14  LYS 14  532 532 LYS LYS A . n 
A 1 15  LEU 15  533 533 LEU LEU A . n 
A 1 16  LYS 16  534 534 LYS LYS A . n 
A 1 17  LYS 17  535 535 LYS LYS A . n 
A 1 18  GLN 18  536 536 GLN GLN A . n 
A 1 19  ASN 19  537 537 ASN ASN A . n 
A 1 20  ASP 20  538 538 ASP ASP A . n 
A 1 21  ILE 21  539 539 ILE ILE A . n 
A 1 22  PRO 22  540 540 PRO PRO A . n 
A 1 23  ASN 23  541 541 ASN ASN A . n 
A 1 24  LYS 24  542 542 LYS LYS A . n 
A 1 25  PHE 25  543 543 PHE PHE A . n 
A 1 26  GLU 26  544 544 GLU GLU A . n 
A 1 27  MET 27  545 545 MET MET A . n 
A 1 28  LYS 28  546 546 LYS LYS A . n 
A 1 29  LEU 29  547 547 LEU LEU A . n 
A 1 30  ARG 30  548 548 ARG ARG A . n 
A 1 31  ARG 31  549 549 ARG ARG A . n 
A 1 32  ALA 32  550 550 ALA ALA A . n 
A 1 33  THR 33  551 551 THR THR A . n 
A 1 34  VAL 34  552 552 VAL VAL A . n 
A 1 35  LEU 35  553 553 LEU LEU A . n 
A 1 36  GLU 36  554 554 GLU GLU A . n 
A 1 37  ASP 37  555 555 ASP ASP A . n 
A 1 38  SER 38  556 556 SER SER A . n 
A 1 39  TYR 39  557 557 TYR TYR A . n 
A 1 40  ARG 40  558 558 ARG ARG A . n 
A 1 41  ARG 41  559 559 ARG ARG A . n 
A 1 42  ILE 42  560 560 ILE ILE A . n 
A 1 43  MET 43  561 561 MET MET A . n 
A 1 44  GLY 44  562 562 GLY GLY A . n 
A 1 45  VAL 45  563 563 VAL VAL A . n 
A 1 46  LYS 46  564 564 LYS LYS A . n 
A 1 47  ARG 47  565 565 ARG ARG A . n 
A 1 48  ALA 48  566 566 ALA ALA A . n 
A 1 49  ASP 49  567 567 ASP ASP A . n 
A 1 50  PHE 50  568 568 PHE PHE A . n 
A 1 51  LEU 51  569 569 LEU LEU A . n 
A 1 52  LYS 52  570 570 LYS LYS A . n 
A 1 53  ALA 53  571 571 ALA ALA A . n 
A 1 54  ARG 54  572 572 ARG ARG A . n 
A 1 55  LEU 55  573 573 LEU LEU A . n 
A 1 56  TRP 56  574 574 TRP TRP A . n 
A 1 57  ILE 57  575 575 ILE ILE A . n 
A 1 58  GLU 58  576 576 GLU GLU A . n 
A 1 59  PHE 59  577 577 PHE PHE A . n 
A 1 60  ASP 60  578 578 ASP ASP A . n 
A 1 61  GLY 61  579 579 GLY GLY A . n 
A 1 62  GLU 62  580 580 GLU GLU A . n 
A 1 63  LYS 63  581 581 LYS LYS A . n 
A 1 64  GLY 64  582 582 GLY GLY A . n 
A 1 65  LEU 65  583 583 LEU LEU A . n 
A 1 66  ASP 66  584 584 ASP ASP A . n 
A 1 67  TYR 67  585 585 TYR TYR A . n 
A 1 68  GLY 68  586 586 GLY GLY A . n 
A 1 69  GLY 69  587 587 GLY GLY A . n 
A 1 70  VAL 70  588 588 VAL VAL A . n 
A 1 71  ALA 71  589 589 ALA ALA A . n 
A 1 72  ARG 72  590 590 ARG ARG A . n 
A 1 73  GLU 73  591 591 GLU GLU A . n 
A 1 74  TRP 74  592 592 TRP TRP A . n 
A 1 75  PHE 75  593 593 PHE PHE A . n 
A 1 76  PHE 76  594 594 PHE PHE A . n 
A 1 77  LEU 77  595 595 LEU LEU A . n 
A 1 78  ILE 78  596 596 ILE ILE A . n 
A 1 79  SER 79  597 597 SER SER A . n 
A 1 80  LYS 80  598 598 LYS LYS A . n 
A 1 81  GLU 81  599 599 GLU GLU A . n 
A 1 82  MET 82  600 600 MET MET A . n 
A 1 83  PHE 83  601 601 PHE PHE A . n 
A 1 84  ASN 84  602 602 ASN ASN A . n 
A 1 85  PRO 85  603 603 PRO PRO A . n 
A 1 86  TYR 86  604 604 TYR TYR A . n 
A 1 87  TYR 87  605 605 TYR TYR A . n 
A 1 88  GLY 88  606 606 GLY GLY A . n 
A 1 89  LEU 89  607 607 LEU LEU A . n 
A 1 90  PHE 90  608 608 PHE PHE A . n 
A 1 91  GLU 91  609 609 GLU GLU A . n 
A 1 92  TYR 92  610 610 TYR TYR A . n 
A 1 93  SER 93  611 611 SER SER A . n 
A 1 94  ALA 94  612 612 ALA ALA A . n 
A 1 95  THR 95  613 613 THR THR A . n 
A 1 96  ASP 96  614 614 ASP ASP A . n 
A 1 97  ASN 97  615 615 ASN ASN A . n 
A 1 98  TYR 98  616 616 TYR TYR A . n 
A 1 99  THR 99  617 617 THR THR A . n 
A 1 100 LEU 100 618 618 LEU LEU A . n 
A 1 101 GLN 101 619 619 GLN GLN A . n 
A 1 102 ILE 102 620 620 ILE ILE A . n 
A 1 103 ASN 103 621 621 ASN ASN A . n 
A 1 104 PRO 104 622 622 PRO PRO A . n 
A 1 105 ASN 105 623 623 ASN ASN A . n 
A 1 106 SER 106 624 624 SER SER A . n 
A 1 107 GLY 107 625 625 GLY GLY A . n 
A 1 108 LEU 108 626 626 LEU LEU A . n 
A 1 109 CYS 109 627 627 CYS CYS A . n 
A 1 110 ASN 110 628 628 ASN ASN A . n 
A 1 111 GLU 111 629 629 GLU GLU A . n 
A 1 112 ASP 112 630 630 ASP ASP A . n 
A 1 113 HIS 113 631 631 HIS HIS A . n 
A 1 114 LEU 114 632 632 LEU LEU A . n 
A 1 115 SER 115 633 633 SER SER A . n 
A 1 116 TYR 116 634 634 TYR TYR A . n 
A 1 117 PHE 117 635 635 PHE PHE A . n 
A 1 118 LYS 118 636 636 LYS LYS A . n 
A 1 119 PHE 119 637 637 PHE PHE A . n 
A 1 120 ILE 120 638 638 ILE ILE A . n 
A 1 121 GLY 121 639 639 GLY GLY A . n 
A 1 122 ARG 122 640 640 ARG ARG A . n 
A 1 123 VAL 123 641 641 VAL VAL A . n 
A 1 124 ALA 124 642 642 ALA ALA A . n 
A 1 125 GLY 125 643 643 GLY GLY A . n 
A 1 126 MET 126 644 644 MET MET A . n 
A 1 127 ALA 127 645 645 ALA ALA A . n 
A 1 128 VAL 128 646 646 VAL VAL A . n 
A 1 129 TYR 129 647 647 TYR TYR A . n 
A 1 130 HIS 130 648 648 HIS HIS A . n 
A 1 131 GLY 131 649 649 GLY GLY A . n 
A 1 132 LYS 132 650 650 LYS LYS A . n 
A 1 133 LEU 133 651 651 LEU LEU A . n 
A 1 134 LEU 134 652 652 LEU LEU A . n 
A 1 135 ASP 135 653 653 ASP ASP A . n 
A 1 136 GLY 136 654 654 GLY GLY A . n 
A 1 137 PHE 137 655 655 PHE PHE A . n 
A 1 138 PHE 138 656 656 PHE PHE A . n 
A 1 139 ILE 139 657 657 ILE ILE A . n 
A 1 140 ARG 140 658 658 ARG ARG A . n 
A 1 141 PRO 141 659 659 PRO PRO A . n 
A 1 142 PHE 142 660 660 PHE PHE A . n 
A 1 143 TYR 143 661 661 TYR TYR A . n 
A 1 144 LYS 144 662 662 LYS LYS A . n 
A 1 145 MET 145 663 663 MET MET A . n 
A 1 146 MET 146 664 664 MET MET A . n 
A 1 147 LEU 147 665 665 LEU LEU A . n 
A 1 148 HIS 148 666 666 HIS HIS A . n 
A 1 149 LYS 149 667 667 LYS LYS A . n 
A 1 150 PRO 150 668 668 PRO PRO A . n 
A 1 151 ILE 151 669 669 ILE ILE A . n 
A 1 152 THR 152 670 670 THR THR A . n 
A 1 153 LEU 153 671 671 LEU LEU A . n 
A 1 154 HIS 154 672 672 HIS HIS A . n 
A 1 155 ASP 155 673 673 ASP ASP A . n 
A 1 156 MET 156 674 674 MET MET A . n 
A 1 157 GLU 157 675 675 GLU GLU A . n 
A 1 158 SER 158 676 676 SER SER A . n 
A 1 159 VAL 159 677 677 VAL VAL A . n 
A 1 160 ASP 160 678 678 ASP ASP A . n 
A 1 161 SER 161 679 679 SER SER A . n 
A 1 162 GLU 162 680 680 GLU GLU A . n 
A 1 163 TYR 163 681 681 TYR TYR A . n 
A 1 164 TYR 164 682 682 TYR TYR A . n 
A 1 165 ASN 165 683 683 ASN ASN A . n 
A 1 166 SER 166 684 684 SER SER A . n 
A 1 167 LEU 167 685 685 LEU LEU A . n 
A 1 168 ARG 168 686 686 ARG ARG A . n 
A 1 169 TRP 169 687 687 TRP TRP A . n 
A 1 170 ILE 170 688 688 ILE ILE A . n 
A 1 171 LEU 171 689 689 LEU LEU A . n 
A 1 172 GLU 172 690 690 GLU GLU A . n 
A 1 173 ASN 173 691 691 ASN ASN A . n 
A 1 174 ASP 174 692 692 ASP ASP A . n 
A 1 175 PRO 175 693 693 PRO PRO A . n 
A 1 176 THR 176 694 694 THR THR A . n 
A 1 177 GLU 177 695 695 GLU GLU A . n 
A 1 178 LEU 178 696 696 LEU LEU A . n 
A 1 179 ASP 179 697 697 ASP ASP A . n 
A 1 180 LEU 180 698 698 LEU LEU A . n 
A 1 181 ARG 181 699 699 ARG ARG A . n 
A 1 182 PHE 182 700 700 PHE PHE A . n 
A 1 183 ILE 183 701 701 ILE ILE A . n 
A 1 184 ILE 184 702 702 ILE ILE A . n 
A 1 185 ASP 185 703 703 ASP ASP A . n 
A 1 186 GLU 186 704 704 GLU GLU A . n 
A 1 187 GLU 187 705 705 GLU GLU A . n 
A 1 188 LEU 188 706 706 LEU LEU A . n 
A 1 189 PHE 189 707 707 PHE PHE A . n 
A 1 190 GLY 190 708 708 GLY GLY A . n 
A 1 191 GLN 191 709 709 GLN GLN A . n 
A 1 192 THR 192 710 710 THR THR A . n 
A 1 193 HIS 193 711 711 HIS HIS A . n 
A 1 194 GLN 194 712 712 GLN GLN A . n 
A 1 195 HIS 195 713 713 HIS HIS A . n 
A 1 196 GLU 196 714 714 GLU GLU A . n 
A 1 197 LEU 197 715 715 LEU LEU A . n 
A 1 198 LYS 198 716 716 LYS LYS A . n 
A 1 199 ASN 199 717 717 ASN ASN A . n 
A 1 200 GLY 200 718 718 GLY GLY A . n 
A 1 201 GLY 201 719 719 GLY GLY A . n 
A 1 202 SER 202 720 720 SER SER A . n 
A 1 203 GLU 203 721 721 GLU GLU A . n 
A 1 204 ILE 204 722 722 ILE ILE A . n 
A 1 205 VAL 205 723 723 VAL VAL A . n 
A 1 206 VAL 206 724 724 VAL VAL A . n 
A 1 207 THR 207 725 725 THR THR A . n 
A 1 208 ASN 208 726 726 ASN ASN A . n 
A 1 209 LYS 209 727 727 LYS LYS A . n 
A 1 210 ASN 210 728 728 ASN ASN A . n 
A 1 211 LYS 211 729 729 LYS LYS A . n 
A 1 212 LYS 212 730 730 LYS LYS A . n 
A 1 213 GLU 213 731 731 GLU GLU A . n 
A 1 214 TYR 214 732 732 TYR TYR A . n 
A 1 215 ILE 215 733 733 ILE ILE A . n 
A 1 216 TYR 216 734 734 TYR TYR A . n 
A 1 217 LEU 217 735 735 LEU LEU A . n 
A 1 218 VAL 218 736 736 VAL VAL A . n 
A 1 219 ILE 219 737 737 ILE ILE A . n 
A 1 220 GLN 220 738 738 GLN GLN A . n 
A 1 221 TRP 221 739 739 TRP TRP A . n 
A 1 222 ARG 222 740 740 ARG ARG A . n 
A 1 223 PHE 223 741 741 PHE PHE A . n 
A 1 224 VAL 224 742 742 VAL VAL A . n 
A 1 225 ASN 225 743 743 ASN ASN A . n 
A 1 226 ARG 226 744 744 ARG ARG A . n 
A 1 227 ILE 227 745 745 ILE ILE A . n 
A 1 228 GLN 228 746 746 GLN GLN A . n 
A 1 229 LYS 229 747 747 LYS LYS A . n 
A 1 230 GLN 230 748 748 GLN GLN A . n 
A 1 231 MET 231 749 749 MET MET A . n 
A 1 232 ALA 232 750 750 ALA ALA A . n 
A 1 233 ALA 233 751 751 ALA ALA A . n 
A 1 234 PHE 234 752 752 PHE PHE A . n 
A 1 235 LYS 235 753 753 LYS LYS A . n 
A 1 236 GLU 236 754 754 GLU GLU A . n 
A 1 237 GLY 237 755 755 GLY GLY A . n 
A 1 238 PHE 238 756 756 PHE PHE A . n 
A 1 239 PHE 239 757 757 PHE PHE A . n 
A 1 240 GLU 240 758 758 GLU GLU A . n 
A 1 241 LEU 241 759 759 LEU LEU A . n 
A 1 242 ILE 242 760 760 ILE ILE A . n 
A 1 243 PRO 243 761 761 PRO PRO A . n 
A 1 244 GLN 244 762 762 GLN GLN A . n 
A 1 245 ASP 245 763 763 ASP ASP A . n 
A 1 246 LEU 246 764 764 LEU LEU A . n 
A 1 247 ILE 247 765 765 ILE ILE A . n 
A 1 248 LYS 248 766 766 LYS LYS A . n 
A 1 249 ILE 249 767 767 ILE ILE A . n 
A 1 250 PHE 250 768 768 PHE PHE A . n 
A 1 251 ASP 251 769 769 ASP ASP A . n 
A 1 252 GLU 252 770 770 GLU GLU A . n 
A 1 253 ASN 253 771 771 ASN ASN A . n 
A 1 254 GLU 254 772 772 GLU GLU A . n 
A 1 255 LEU 255 773 773 LEU LEU A . n 
A 1 256 GLU 256 774 774 GLU GLU A . n 
A 1 257 LEU 257 775 775 LEU LEU A . n 
A 1 258 LEU 258 776 776 LEU LEU A . n 
A 1 259 MET 259 777 777 MET MET A . n 
A 1 260 CYS 260 778 778 CYS CYS A . n 
A 1 261 GLY 261 779 779 GLY GLY A . n 
A 1 262 LEU 262 780 780 LEU LEU A . n 
A 1 263 GLY 263 781 781 GLY GLY A . n 
A 1 264 ASP 264 782 782 ASP ASP A . n 
A 1 265 VAL 265 783 783 VAL VAL A . n 
A 1 266 ASP 266 784 784 ASP ASP A . n 
A 1 267 VAL 267 785 785 VAL VAL A . n 
A 1 268 ASN 268 786 786 ASN ASN A . n 
A 1 269 ASP 269 787 787 ASP ASP A . n 
A 1 270 TRP 270 788 788 TRP TRP A . n 
A 1 271 ARG 271 789 789 ARG ARG A . n 
A 1 272 GLU 272 790 790 GLU GLU A . n 
A 1 273 HIS 273 791 791 HIS HIS A . n 
A 1 274 THR 274 792 792 THR THR A . n 
A 1 275 LYS 275 793 793 LYS LYS A . n 
A 1 276 TYR 276 794 794 TYR TYR A . n 
A 1 277 LYS 277 795 795 LYS LYS A . n 
A 1 278 ASN 278 796 796 ASN ASN A . n 
A 1 279 GLY 279 797 797 GLY GLY A . n 
A 1 280 TYR 280 798 798 TYR TYR A . n 
A 1 281 SER 281 799 799 SER SER A . n 
A 1 282 ALA 282 800 800 ALA ALA A . n 
A 1 283 ASN 283 801 801 ASN ASN A . n 
A 1 284 HIS 284 802 802 HIS HIS A . n 
A 1 285 GLN 285 803 803 GLN GLN A . n 
A 1 286 VAL 286 804 804 VAL VAL A . n 
A 1 287 ILE 287 805 805 ILE ILE A . n 
A 1 288 GLN 288 806 806 GLN GLN A . n 
A 1 289 TRP 289 807 807 TRP TRP A . n 
A 1 290 PHE 290 808 808 PHE PHE A . n 
A 1 291 TRP 291 809 809 TRP TRP A . n 
A 1 292 LYS 292 810 810 LYS LYS A . n 
A 1 293 ALA 293 811 811 ALA ALA A . n 
A 1 294 VAL 294 812 812 VAL VAL A . n 
A 1 295 LEU 295 813 813 LEU LEU A . n 
A 1 296 MET 296 814 814 MET MET A . n 
A 1 297 MET 297 815 815 MET MET A . n 
A 1 298 ASP 298 816 816 ASP ASP A . n 
A 1 299 SER 299 817 817 SER SER A . n 
A 1 300 GLU 300 818 818 GLU GLU A . n 
A 1 301 LYS 301 819 819 LYS LYS A . n 
A 1 302 ARG 302 820 820 ARG ARG A . n 
A 1 303 ILE 303 821 821 ILE ILE A . n 
A 1 304 ARG 304 822 822 ARG ARG A . n 
A 1 305 LEU 305 823 823 LEU LEU A . n 
A 1 306 LEU 306 824 824 LEU LEU A . n 
A 1 307 GLN 307 825 825 GLN GLN A . n 
A 1 308 PHE 308 826 826 PHE PHE A . n 
A 1 309 VAL 309 827 827 VAL VAL A . n 
A 1 310 THR 310 828 828 THR THR A . n 
A 1 311 GLY 311 829 829 GLY GLY A . n 
A 1 312 THR 312 830 830 THR THR A . n 
A 1 313 SER 313 831 831 SER SER A . n 
A 1 314 ARG 314 832 832 ARG ARG A . n 
A 1 315 VAL 315 833 833 VAL VAL A . n 
A 1 316 PRO 316 834 834 PRO PRO A . n 
A 1 317 MET 317 835 835 MET MET A . n 
A 1 318 ASN 318 836 836 ASN ASN A . n 
A 1 319 GLY 319 837 837 GLY GLY A . n 
A 1 320 PHE 320 838 838 PHE PHE A . n 
A 1 321 ALA 321 839 839 ALA ALA A . n 
A 1 322 GLU 322 840 840 GLU GLU A . n 
A 1 323 LEU 323 841 841 LEU LEU A . n 
A 1 324 TYR 324 842 842 TYR TYR A . n 
A 1 325 GLY 325 843 843 GLY GLY A . n 
A 1 326 SER 326 844 844 SER SER A . n 
A 1 327 ASN 327 845 845 ASN ASN A . n 
A 1 328 GLY 328 846 846 GLY GLY A . n 
A 1 329 PRO 329 847 847 PRO PRO A . n 
A 1 330 GLN 330 848 848 GLN GLN A . n 
A 1 331 SER 331 849 849 SER SER A . n 
A 1 332 PHE 332 850 850 PHE PHE A . n 
A 1 333 THR 333 851 851 THR THR A . n 
A 1 334 VAL 334 852 852 VAL VAL A . n 
A 1 335 GLU 335 853 853 GLU GLU A . n 
A 1 336 GLN 336 854 854 GLN GLN A . n 
A 1 337 TRP 337 855 855 TRP TRP A . n 
A 1 338 GLY 338 856 856 GLY GLY A . n 
A 1 339 THR 339 857 857 THR THR A . n 
A 1 340 PRO 340 858 858 PRO PRO A . n 
A 1 341 GLU 341 859 859 GLU GLU A . n 
A 1 342 LYS 342 860 860 LYS LYS A . n 
A 1 343 LEU 343 861 861 LEU LEU A . n 
A 1 344 PRO 344 862 862 PRO PRO A . n 
A 1 345 ARG 345 863 863 ARG ARG A . n 
A 1 346 ALA 346 864 864 ALA ALA A . n 
A 1 347 HIS 347 865 865 HIS HIS A . n 
A 1 348 THR 348 866 866 THR THR A . n 
A 1 349 CYS 349 867 867 CYS CYS A . n 
A 1 350 PHE 350 868 868 PHE PHE A . n 
A 1 351 ASN 351 869 869 ASN ASN A . n 
A 1 352 ARG 352 870 870 ARG ARG A . n 
A 1 353 LEU 353 871 871 LEU LEU A . n 
A 1 354 ASP 354 872 872 ASP ASP A . n 
A 1 355 LEU 355 873 873 LEU LEU A . n 
A 1 356 PRO 356 874 874 PRO PRO A . n 
A 1 357 PRO 357 875 875 PRO PRO A . n 
A 1 358 TYR 358 876 876 TYR TYR A . n 
A 1 359 GLU 359 877 877 GLU GLU A . n 
A 1 360 SER 360 878 878 SER SER A . n 
A 1 361 PHE 361 879 879 PHE PHE A . n 
A 1 362 GLU 362 880 880 GLU GLU A . n 
A 1 363 GLU 363 881 881 GLU GLU A . n 
A 1 364 LEU 364 882 882 LEU LEU A . n 
A 1 365 TRP 365 883 883 TRP TRP A . n 
A 1 366 ASP 366 884 884 ASP ASP A . n 
A 1 367 LYS 367 885 885 LYS LYS A . n 
A 1 368 LEU 368 886 886 LEU LEU A . n 
A 1 369 GLN 369 887 887 GLN GLN A . n 
A 1 370 MET 370 888 888 MET MET A . n 
A 1 371 ALA 371 889 889 ALA ALA A . n 
A 1 372 ILE 372 890 890 ILE ILE A . n 
A 1 373 GLU 373 891 891 GLU GLU A . n 
A 1 374 ASN 374 892 892 ASN ASN A . n 
A 1 375 THR 375 893 893 THR THR A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1ITT 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1ITT 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
B 2 A1ITT 1   901  1   A1ITT 612 A . 
C 3 HOH   1   1001 68  HOH   HOH A . 
C 3 HOH   2   1002 115 HOH   HOH A . 
C 3 HOH   3   1003 45  HOH   HOH A . 
C 3 HOH   4   1004 99  HOH   HOH A . 
C 3 HOH   5   1005 91  HOH   HOH A . 
C 3 HOH   6   1006 57  HOH   HOH A . 
C 3 HOH   7   1007 22  HOH   HOH A . 
C 3 HOH   8   1008 100 HOH   HOH A . 
C 3 HOH   9   1009 41  HOH   HOH A . 
C 3 HOH   10  1010 103 HOH   HOH A . 
C 3 HOH   11  1011 95  HOH   HOH A . 
C 3 HOH   12  1012 114 HOH   HOH A . 
C 3 HOH   13  1013 81  HOH   HOH A . 
C 3 HOH   14  1014 74  HOH   HOH A . 
C 3 HOH   15  1015 47  HOH   HOH A . 
C 3 HOH   16  1016 14  HOH   HOH A . 
C 3 HOH   17  1017 59  HOH   HOH A . 
C 3 HOH   18  1018 94  HOH   HOH A . 
C 3 HOH   19  1019 4   HOH   HOH A . 
C 3 HOH   20  1020 23  HOH   HOH A . 
C 3 HOH   21  1021 79  HOH   HOH A . 
C 3 HOH   22  1022 13  HOH   HOH A . 
C 3 HOH   23  1023 32  HOH   HOH A . 
C 3 HOH   24  1024 83  HOH   HOH A . 
C 3 HOH   25  1025 24  HOH   HOH A . 
C 3 HOH   26  1026 84  HOH   HOH A . 
C 3 HOH   27  1027 1   HOH   HOH A . 
C 3 HOH   28  1028 88  HOH   HOH A . 
C 3 HOH   29  1029 112 HOH   HOH A . 
C 3 HOH   30  1030 50  HOH   HOH A . 
C 3 HOH   31  1031 96  HOH   HOH A . 
C 3 HOH   32  1032 26  HOH   HOH A . 
C 3 HOH   33  1033 85  HOH   HOH A . 
C 3 HOH   34  1034 80  HOH   HOH A . 
C 3 HOH   35  1035 20  HOH   HOH A . 
C 3 HOH   36  1036 19  HOH   HOH A . 
C 3 HOH   37  1037 27  HOH   HOH A . 
C 3 HOH   38  1038 8   HOH   HOH A . 
C 3 HOH   39  1039 73  HOH   HOH A . 
C 3 HOH   40  1040 38  HOH   HOH A . 
C 3 HOH   41  1041 6   HOH   HOH A . 
C 3 HOH   42  1042 78  HOH   HOH A . 
C 3 HOH   43  1043 11  HOH   HOH A . 
C 3 HOH   44  1044 2   HOH   HOH A . 
C 3 HOH   45  1045 97  HOH   HOH A . 
C 3 HOH   46  1046 15  HOH   HOH A . 
C 3 HOH   47  1047 36  HOH   HOH A . 
C 3 HOH   48  1048 71  HOH   HOH A . 
C 3 HOH   49  1049 67  HOH   HOH A . 
C 3 HOH   50  1050 44  HOH   HOH A . 
C 3 HOH   51  1051 107 HOH   HOH A . 
C 3 HOH   52  1052 33  HOH   HOH A . 
C 3 HOH   53  1053 34  HOH   HOH A . 
C 3 HOH   54  1054 60  HOH   HOH A . 
C 3 HOH   55  1055 16  HOH   HOH A . 
C 3 HOH   56  1056 61  HOH   HOH A . 
C 3 HOH   57  1057 82  HOH   HOH A . 
C 3 HOH   58  1058 77  HOH   HOH A . 
C 3 HOH   59  1059 37  HOH   HOH A . 
C 3 HOH   60  1060 18  HOH   HOH A . 
C 3 HOH   61  1061 30  HOH   HOH A . 
C 3 HOH   62  1062 104 HOH   HOH A . 
C 3 HOH   63  1063 46  HOH   HOH A . 
C 3 HOH   64  1064 111 HOH   HOH A . 
C 3 HOH   65  1065 55  HOH   HOH A . 
C 3 HOH   66  1066 17  HOH   HOH A . 
C 3 HOH   67  1067 7   HOH   HOH A . 
C 3 HOH   68  1068 106 HOH   HOH A . 
C 3 HOH   69  1069 5   HOH   HOH A . 
C 3 HOH   70  1070 10  HOH   HOH A . 
C 3 HOH   71  1071 40  HOH   HOH A . 
C 3 HOH   72  1072 76  HOH   HOH A . 
C 3 HOH   73  1073 48  HOH   HOH A . 
C 3 HOH   74  1074 43  HOH   HOH A . 
C 3 HOH   75  1075 21  HOH   HOH A . 
C 3 HOH   76  1076 31  HOH   HOH A . 
C 3 HOH   77  1077 12  HOH   HOH A . 
C 3 HOH   78  1078 25  HOH   HOH A . 
C 3 HOH   79  1079 75  HOH   HOH A . 
C 3 HOH   80  1080 49  HOH   HOH A . 
C 3 HOH   81  1081 52  HOH   HOH A . 
C 3 HOH   82  1082 86  HOH   HOH A . 
C 3 HOH   83  1083 42  HOH   HOH A . 
C 3 HOH   84  1084 101 HOH   HOH A . 
C 3 HOH   85  1085 69  HOH   HOH A . 
C 3 HOH   86  1086 113 HOH   HOH A . 
C 3 HOH   87  1087 54  HOH   HOH A . 
C 3 HOH   88  1088 9   HOH   HOH A . 
C 3 HOH   89  1089 29  HOH   HOH A . 
C 3 HOH   90  1090 102 HOH   HOH A . 
C 3 HOH   91  1091 87  HOH   HOH A . 
C 3 HOH   92  1092 56  HOH   HOH A . 
C 3 HOH   93  1093 53  HOH   HOH A . 
C 3 HOH   94  1094 64  HOH   HOH A . 
C 3 HOH   95  1095 51  HOH   HOH A . 
C 3 HOH   96  1096 58  HOH   HOH A . 
C 3 HOH   97  1097 66  HOH   HOH A . 
C 3 HOH   98  1098 70  HOH   HOH A . 
C 3 HOH   99  1099 105 HOH   HOH A . 
C 3 HOH   100 1100 108 HOH   HOH A . 
C 3 HOH   101 1101 65  HOH   HOH A . 
C 3 HOH   102 1102 62  HOH   HOH A . 
C 3 HOH   103 1103 110 HOH   HOH A . 
C 3 HOH   104 1104 28  HOH   HOH A . 
C 3 HOH   105 1105 35  HOH   HOH A . 
C 3 HOH   106 1106 98  HOH   HOH A . 
C 3 HOH   107 1107 109 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 ARG 832 ? CG  ? A ARG 314 CG  
2 1 Y 1 A ARG 832 ? CD  ? A ARG 314 CD  
3 1 Y 1 A ARG 832 ? NE  ? A ARG 314 NE  
4 1 Y 1 A ARG 832 ? CZ  ? A ARG 314 CZ  
5 1 Y 1 A ARG 832 ? NH1 ? A ARG 314 NH1 
6 1 Y 1 A ARG 832 ? NH2 ? A ARG 314 NH2 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX  ? ? ? '(1.13_2998: ???)' 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? xia2    ? ? ? .                  2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? .                  3 
? 'model building' ? ? ? ? ? ? ? ? ? ? ? Coot    ? ? ? .                  4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   91.17 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9H9T 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     176.372 
_cell.length_a_esd                 ? 
_cell.length_b                     38.926 
_cell.length_b_esd                 ? 
_cell.length_c                     59.694 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        4 
_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                         9H9T 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                5 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'C 1 2 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9H9T 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             2.16 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          43 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              6 
_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    
;100 mM MES pH 6.0
8-10% PEG 400
20% glycerol
1-4 mM inhibitor (0.25-1% DMSO)
;
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS 2M-F' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2018-04-20 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.9999 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'SLS BEAMLINE X06DA' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.9999 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   X06DA 
_diffrn_source.pdbx_synchrotron_site       SLS 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9H9T 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.17 
_reflns.d_resolution_low                               59.7 
_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                                     21848 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           99.9 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                4.9 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          12.3 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.999 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.057 
_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                                    2.17 
_reflns_shell.d_res_low                                     2.21 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           1.8 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             2500 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               ? 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.605 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          97.2 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  0.666 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9H9T 
_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                            2.170 
_refine.ls_d_res_low                             59.7 
_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                     21844 
_refine.ls_number_reflns_R_free                  1090 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.83 
_refine.ls_percent_reflns_R_free                 4.99 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2202 
_refine.ls_R_factor_R_free                       0.2515 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2186 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.43 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.11 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_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                 29.29 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            0.31 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        3150 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         29 
_refine_hist.number_atoms_solvent             107 
_refine_hist.number_atoms_total               3286 
_refine_hist.d_res_high                       2.170 
_refine_hist.d_res_low                        59.7 
# 
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' ? 0.005 ? 3299 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.758 ? 4450 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 4.404 ? 2744 ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.044 ? 445  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.004 ? 572  ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 2.1701 2.2689 . . 148 2521 99.00  . . . . 0.3245 . . . . . . . . . . . 0.3429 
'X-RAY DIFFRACTION' 2.2689 2.3885 . . 141 2585 100.00 . . . . 0.2990 . . . . . . . . . . . 0.3369 
'X-RAY DIFFRACTION' 2.3885 2.5382 . . 165 2525 100.00 . . . . 0.2889 . . . . . . . . . . . 0.2949 
'X-RAY DIFFRACTION' 2.5382 2.7341 . . 117 2629 100.00 . . . . 0.2729 . . . . . . . . . . . 0.3629 
'X-RAY DIFFRACTION' 2.7341 3.0093 . . 117 2580 100.00 . . . . 0.2627 . . . . . . . . . . . 0.2956 
'X-RAY DIFFRACTION' 3.0093 3.4447 . . 127 2593 100.00 . . . . 0.2267 . . . . . . . . . . . 0.2626 
'X-RAY DIFFRACTION' 3.4447 4.3398 . . 133 2619 100.00 . . . . 0.1875 . . . . . . . . . . . 0.2135 
'X-RAY DIFFRACTION' 4.3398 59.7   . . 142 2702 100.00 . . . . 0.1867 . . . . . . . . . . . 0.2191 
# 
_struct.entry_id                     9H9T 
_struct.title                        'Crystal structure of NEDD4 HECT domain in complex with covalent 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        9H9T 
_struct_keywords.text            'Covalent Ihibitor, Complex, Ubiquitin, Ligase, E3' 
_struct_keywords.pdbx_keywords   LIGASE 
# 
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 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    NEDD4_HUMAN 
_struct_ref.pdbx_db_accession          P46934 
_struct_ref.pdbx_db_isoform            P46934-4 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;SRDYKRKYEFFRRKLKKQNDIPNKFEMKLRRATVLEDSYRRIMGVKRADFLKARLWIEFDGEKGLDYGGVAREWFFLISK
EMFNPYYGLFEYSATDNYTLQINPNSGLCNEDHLSYFKFIGRVAGMAVYHGKLLDGFFIRPFYKMMLHKPITLHDMESVD
SEYYNSLRWILENDPTELDLRFIIDEELFGQTHQHELKNGGSEIVVTNKNKKEYIYLVIQWRFVNRIQKQMAAFKEGFFE
LIPQDLIKIFDENELELLMCGLGDVDVNDWREHTKYKNGYSANHQVIQWFWKAVLMMDSEKRIRLLQFVTGTSRVPMNGF
AELYGSNGPQSFTVEQWGTPEKLPRAHTCFNRLDLPPYESFEELWDKLQMAIENT
;
_struct_ref.pdbx_align_begin           519 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              9H9T 
_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                 375 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             P46934 
_struct_ref_seq.db_align_beg                  519 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  893 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       519 
_struct_ref_seq.pdbx_auth_seq_align_end       893 
# 
_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   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
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)' 760   ? 
1 MORE         -3    ? 
1 'SSA (A^2)'  19800 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   none 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 ASP A 3   ? LEU A 15  ? ASP A 521 LEU A 533 1 ? 13 
HELX_P HELX_P2  AA2 ARG A 30  ? ALA A 32  ? ARG A 548 ALA A 550 5 ? 3  
HELX_P HELX_P3  AA3 THR A 33  ? MET A 43  ? THR A 551 MET A 561 1 ? 11 
HELX_P HELX_P4  AA4 ARG A 47  ? ALA A 53  ? ARG A 565 ALA A 571 5 ? 7  
HELX_P HELX_P5  AA5 GLY A 68  ? PHE A 83  ? GLY A 586 PHE A 601 1 ? 16 
HELX_P HELX_P6  AA6 ASN A 84  ? GLY A 88  ? ASN A 602 GLY A 606 5 ? 5  
HELX_P HELX_P7  AA7 ASN A 105 ? ASN A 110 ? ASN A 623 ASN A 628 1 ? 6  
HELX_P HELX_P8  AA8 ASP A 112 ? HIS A 130 ? ASP A 630 HIS A 648 1 ? 19 
HELX_P HELX_P9  AA9 ILE A 139 ? LEU A 147 ? ILE A 657 LEU A 665 1 ? 9  
HELX_P HELX_P10 AB1 THR A 152 ? SER A 158 ? THR A 670 SER A 676 1 ? 7  
HELX_P HELX_P11 AB2 ASP A 160 ? ASN A 173 ? ASP A 678 ASN A 691 1 ? 14 
HELX_P HELX_P12 AB3 PRO A 175 ? ASP A 179 ? PRO A 693 ASP A 697 5 ? 5  
HELX_P HELX_P13 AB4 GLY A 200 ? ILE A 204 ? GLY A 718 ILE A 722 5 ? 5  
HELX_P HELX_P14 AB5 ASN A 210 ? VAL A 224 ? ASN A 728 VAL A 742 1 ? 15 
HELX_P HELX_P15 AB6 ILE A 227 ? GLU A 240 ? ILE A 745 GLU A 758 1 ? 14 
HELX_P HELX_P16 AB7 PRO A 243 ? LYS A 248 ? PRO A 761 LYS A 766 1 ? 6  
HELX_P HELX_P17 AB8 ASP A 251 ? GLY A 261 ? ASP A 769 GLY A 779 1 ? 11 
HELX_P HELX_P18 AB9 ASP A 266 ? HIS A 273 ? ASP A 784 HIS A 791 1 ? 8  
HELX_P HELX_P19 AC1 HIS A 284 ? MET A 296 ? HIS A 802 MET A 814 1 ? 13 
HELX_P HELX_P20 AC2 ASP A 298 ? GLY A 311 ? ASP A 816 GLY A 829 1 ? 14 
HELX_P HELX_P21 AC3 GLY A 319 ? LEU A 323 ? GLY A 837 LEU A 841 5 ? 5  
HELX_P HELX_P22 AC4 SER A 360 ? GLU A 373 ? SER A 878 GLU A 891 1 ? 14 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
_struct_conn.id                            covale1 
_struct_conn.conn_type_id                  covale 
_struct_conn.pdbx_leaving_atom_flag        none 
_struct_conn.pdbx_PDB_id                   ? 
_struct_conn.ptnr1_label_asym_id           A 
_struct_conn.ptnr1_label_comp_id           CYS 
_struct_conn.ptnr1_label_seq_id            109 
_struct_conn.ptnr1_label_atom_id           SG 
_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                1_555 
_struct_conn.ptnr2_label_asym_id           B 
_struct_conn.ptnr2_label_comp_id           A1ITT 
_struct_conn.ptnr2_label_seq_id            . 
_struct_conn.ptnr2_label_atom_id           C12 
_struct_conn.pdbx_ptnr2_label_alt_id       ? 
_struct_conn.pdbx_ptnr2_PDB_ins_code       ? 
_struct_conn.ptnr1_auth_asym_id            A 
_struct_conn.ptnr1_auth_comp_id            CYS 
_struct_conn.ptnr1_auth_seq_id             627 
_struct_conn.ptnr2_auth_asym_id            A 
_struct_conn.ptnr2_auth_comp_id            A1ITT 
_struct_conn.ptnr2_auth_seq_id             901 
_struct_conn.ptnr2_symmetry                1_555 
_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               1.814 
_struct_conn.pdbx_value_order              ? 
_struct_conn.pdbx_role                     ? 
# 
_struct_conn_type.id          covale 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
_pdbx_modification_feature.ordinal                            1 
_pdbx_modification_feature.label_comp_id                      A1ITT 
_pdbx_modification_feature.label_asym_id                      B 
_pdbx_modification_feature.label_seq_id                       . 
_pdbx_modification_feature.label_alt_id                       ? 
_pdbx_modification_feature.modified_residue_label_comp_id     CYS 
_pdbx_modification_feature.modified_residue_label_asym_id     A 
_pdbx_modification_feature.modified_residue_label_seq_id      109 
_pdbx_modification_feature.modified_residue_label_alt_id      ? 
_pdbx_modification_feature.auth_comp_id                       A1ITT 
_pdbx_modification_feature.auth_asym_id                       A 
_pdbx_modification_feature.auth_seq_id                        901 
_pdbx_modification_feature.PDB_ins_code                       ? 
_pdbx_modification_feature.symmetry                           1_555 
_pdbx_modification_feature.modified_residue_auth_comp_id      CYS 
_pdbx_modification_feature.modified_residue_auth_asym_id      A 
_pdbx_modification_feature.modified_residue_auth_seq_id       627 
_pdbx_modification_feature.modified_residue_PDB_ins_code      ? 
_pdbx_modification_feature.modified_residue_symmetry          1_555 
_pdbx_modification_feature.comp_id_linking_atom               C12 
_pdbx_modification_feature.modified_residue_id_linking_atom   SG 
_pdbx_modification_feature.modified_residue_id                CYS 
_pdbx_modification_feature.ref_pcm_id                         1 
_pdbx_modification_feature.ref_comp_id                        A1ITT 
_pdbx_modification_feature.type                               None 
_pdbx_modification_feature.category                           'Covalent chemical modification' 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 2 ? 
AA2 ? 2 ? 
AA3 ? 2 ? 
AA4 ? 4 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? parallel      
AA2 1 2 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA4 1 2 ? parallel      
AA4 2 3 ? parallel      
AA4 3 4 ? 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 LYS A 24  ? LEU A 29  ? LYS A 542 LEU A 547 
AA1 2 ARG A 54  ? PHE A 59  ? ARG A 572 PHE A 577 
AA2 1 PHE A 90  ? TYR A 92  ? PHE A 608 TYR A 610 
AA2 2 LEU A 100 ? ILE A 102 ? LEU A 618 ILE A 620 
AA3 1 ILE A 183 ? LEU A 188 ? ILE A 701 LEU A 706 
AA3 2 GLN A 191 ? GLU A 196 ? GLN A 709 GLU A 714 
AA4 1 THR A 274 ? LYS A 277 ? THR A 792 LYS A 795 
AA4 2 PHE A 332 ? GLN A 336 ? PHE A 850 GLN A 854 
AA4 3 ARG A 352 ? LEU A 355 ? ARG A 870 LEU A 873 
AA4 4 ARG A 345 ? HIS A 347 ? ARG A 863 HIS A 865 
# 
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 LEU A 29  ? N LEU A 547 O GLU A 58  ? O GLU A 576 
AA2 1 2 N GLU A 91  ? N GLU A 609 O GLN A 101 ? O GLN A 619 
AA3 1 2 N ILE A 184 ? N ILE A 702 O HIS A 195 ? O HIS A 713 
AA4 1 2 N LYS A 275 ? N LYS A 793 O PHE A 332 ? O PHE A 850 
AA4 2 3 N THR A 333 ? N THR A 851 O LEU A 353 ? O LEU A 871 
AA4 3 4 O ASP A 354 ? O ASP A 872 N ARG A 345 ? N ARG A 863 
# 
_pdbx_entry_details.entry_id                   9H9T 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   Y 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 O   A LYS 793 ? ? O A HOH 1001 ? ? 1.93 
2 1 NZ  A LYS 546 ? ? O A HOH 1002 ? ? 2.08 
3 1 OE1 A GLN 854 ? ? O A HOH 1003 ? ? 2.08 
4 1 OE1 A GLU 591 ? ? O A HOH 1004 ? ? 2.10 
5 1 O   A LYS 535 ? ? O A HOH 1005 ? ? 2.13 
6 1 OE1 A GLU 695 ? ? O A HOH 1006 ? ? 2.15 
7 1 OD1 A ASP 630 ? ? O A HOH 1007 ? ? 2.19 
# 
loop_
_pdbx_validate_symm_contact.id 
_pdbx_validate_symm_contact.PDB_model_num 
_pdbx_validate_symm_contact.auth_atom_id_1 
_pdbx_validate_symm_contact.auth_asym_id_1 
_pdbx_validate_symm_contact.auth_comp_id_1 
_pdbx_validate_symm_contact.auth_seq_id_1 
_pdbx_validate_symm_contact.PDB_ins_code_1 
_pdbx_validate_symm_contact.label_alt_id_1 
_pdbx_validate_symm_contact.site_symmetry_1 
_pdbx_validate_symm_contact.auth_atom_id_2 
_pdbx_validate_symm_contact.auth_asym_id_2 
_pdbx_validate_symm_contact.auth_comp_id_2 
_pdbx_validate_symm_contact.auth_seq_id_2 
_pdbx_validate_symm_contact.PDB_ins_code_2 
_pdbx_validate_symm_contact.label_alt_id_2 
_pdbx_validate_symm_contact.site_symmetry_2 
_pdbx_validate_symm_contact.dist 
1 1 NZ A LYS 564  ? ? 1_555 O A GLU 714  ? ? 4_444 2.04 
2 1 O  A HOH 1028 ? ? 1_555 O A HOH 1083 ? ? 4_454 2.14 
# 
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 LEU A 533 ? ? -69.06  70.86  
2 1 ASP A 630 ? ? -90.93  30.80  
3 1 GLU A 714 ? ? -42.64  157.94 
4 1 VAL A 742 ? ? -123.98 -53.80 
5 1 ASN A 892 ? ? -103.09 42.64  
# 
loop_
_pdbx_refine_tls.id 
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[1][1]_esd 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][2]_esd 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[1][3]_esd 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[2][2]_esd 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.T[2][3]_esd 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[3][3]_esd 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[1][1]_esd 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][2]_esd 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[1][3]_esd 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[2][2]_esd 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.L[2][3]_esd 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[3][3]_esd 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][1]_esd 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][2]_esd 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[1][3]_esd 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][1]_esd 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][2]_esd 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[2][3]_esd 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][1]_esd 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][2]_esd 
_pdbx_refine_tls.S[3][3] 
_pdbx_refine_tls.S[3][3]_esd 
1 'X-RAY DIFFRACTION' ? refined -25.2142 13.2167 -34.2904 0.2617 ? -0.0168 ? 0.0220  ? 0.3752 ? -0.0984 ? 0.4074 ? 2.3161 ? 
-0.7134 ? 1.3803  ? 4.7322 ? -0.5369 ? 5.1898 ? 0.2468  ? 0.3457  ? -0.1956 ? -0.2958 ? -0.1166 ? -0.4295 ? 0.1954 ? 0.2759  ? 
-0.0726 ? 
2 'X-RAY DIFFRACTION' ? refined -36.0803 18.6022 -12.6517 0.4034 ? -0.0360 ? -0.0599 ? 0.2644 ? 0.0075  ? 0.3180 ? 5.1398 ? 
-1.9878 ? -3.5942 ? 2.0420 ? 2.2144  ? 4.8623 ? -0.0034 ? -0.3081 ? 0.3839  ? 0.3021  ? 0.2100  ? -0.2782 ? 0.0377 ? 0.2196  ? 
-0.1605 ? 
3 'X-RAY DIFFRACTION' ? refined -0.9433  24.0694 -16.5346 0.6404 ? 0.0186  ? -0.0080 ? 0.3700 ? -0.0507 ? 0.8727 ? 8.5155 ? 
-0.9757 ? 1.5295  ? 4.4629 ? 0.4390  ? 7.5234 ? -0.1412 ? 0.1454  ? 0.3112  ? -0.5797 ? -0.2192 ? -0.6877 ? 0.0019 ? -0.0229 ? 
0.2979  ? 
# 
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 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 519 through 647 )
;
2 'X-RAY DIFFRACTION' 2 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 648 through 784 )
;
3 'X-RAY DIFFRACTION' 3 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 785 through 893 )
;
# 
_pdbx_distant_solvent_atoms.id                                1 
_pdbx_distant_solvent_atoms.PDB_model_num                     1 
_pdbx_distant_solvent_atoms.auth_atom_id                      O 
_pdbx_distant_solvent_atoms.label_alt_id                      ? 
_pdbx_distant_solvent_atoms.auth_asym_id                      A 
_pdbx_distant_solvent_atoms.auth_comp_id                      HOH 
_pdbx_distant_solvent_atoms.auth_seq_id                       1107 
_pdbx_distant_solvent_atoms.PDB_ins_code                      ? 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance   7.79 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance          . 
# 
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 
A1ITT C12  C  N N 1   
A1ITT C11  C  N N 2   
A1ITT N10  N  N N 3   
A1ITT C02  C  Y N 4   
A1ITT C03  C  Y N 5   
A1ITT C04  C  Y N 6   
A1ITT C06  C  N N 7   
A1ITT C07  C  N N 8   
A1ITT C08  C  N N 9   
A1ITT C09  C  N N 10  
A1ITT C13  C  N N 11  
A1ITT C14  C  N N 12  
A1ITT C16  C  N N 13  
A1ITT C17  C  N N 14  
A1ITT C19  C  Y N 15  
A1ITT C20  C  Y N 16  
A1ITT C21  C  Y N 17  
A1ITT C22  C  Y N 18  
A1ITT C23  C  Y N 19  
A1ITT C24  C  Y N 20  
A1ITT C25  C  N N 21  
A1ITT C26  C  N N 22  
A1ITT C27  C  Y N 23  
A1ITT C28  C  Y N 24  
A1ITT C29  C  Y N 25  
A1ITT N05  N  N N 26  
A1ITT O15  O  N N 27  
A1ITT O18  O  N N 28  
A1ITT CL01 CL N N 29  
A1ITT H1   H  N N 30  
A1ITT H2   H  N N 31  
A1ITT H3   H  N N 32  
A1ITT H4   H  N N 33  
A1ITT H5   H  N N 34  
A1ITT H7   H  N N 35  
A1ITT H8   H  N N 36  
A1ITT H9   H  N N 37  
A1ITT H10  H  N N 38  
A1ITT H11  H  N N 39  
A1ITT H12  H  N N 40  
A1ITT H13  H  N N 41  
A1ITT H14  H  N N 42  
A1ITT H15  H  N N 43  
A1ITT H16  H  N N 44  
A1ITT H17  H  N N 45  
A1ITT H18  H  N N 46  
A1ITT H19  H  N N 47  
A1ITT H20  H  N N 48  
A1ITT H21  H  N N 49  
A1ITT H22  H  N N 50  
A1ITT H23  H  N N 51  
A1ITT H24  H  N N 52  
A1ITT H25  H  N N 53  
A1ITT H26  H  N N 54  
A1ITT H27  H  N N 55  
A1ITT H28  H  N N 56  
A1ITT H29  H  N N 57  
A1ITT H30  H  N N 58  
A1ITT H31  H  N N 59  
A1ITT H32  H  N N 60  
ALA   N    N  N N 61  
ALA   CA   C  N S 62  
ALA   C    C  N N 63  
ALA   O    O  N N 64  
ALA   CB   C  N N 65  
ALA   OXT  O  N N 66  
ALA   H    H  N N 67  
ALA   H2   H  N N 68  
ALA   HA   H  N N 69  
ALA   HB1  H  N N 70  
ALA   HB2  H  N N 71  
ALA   HB3  H  N N 72  
ALA   HXT  H  N N 73  
ARG   N    N  N N 74  
ARG   CA   C  N S 75  
ARG   C    C  N N 76  
ARG   O    O  N N 77  
ARG   CB   C  N N 78  
ARG   CG   C  N N 79  
ARG   CD   C  N N 80  
ARG   NE   N  N N 81  
ARG   CZ   C  N N 82  
ARG   NH1  N  N N 83  
ARG   NH2  N  N N 84  
ARG   OXT  O  N N 85  
ARG   H    H  N N 86  
ARG   H2   H  N N 87  
ARG   HA   H  N N 88  
ARG   HB2  H  N N 89  
ARG   HB3  H  N N 90  
ARG   HG2  H  N N 91  
ARG   HG3  H  N N 92  
ARG   HD2  H  N N 93  
ARG   HD3  H  N N 94  
ARG   HE   H  N N 95  
ARG   HH11 H  N N 96  
ARG   HH12 H  N N 97  
ARG   HH21 H  N N 98  
ARG   HH22 H  N N 99  
ARG   HXT  H  N N 100 
ASN   N    N  N N 101 
ASN   CA   C  N S 102 
ASN   C    C  N N 103 
ASN   O    O  N N 104 
ASN   CB   C  N N 105 
ASN   CG   C  N N 106 
ASN   OD1  O  N N 107 
ASN   ND2  N  N N 108 
ASN   OXT  O  N N 109 
ASN   H    H  N N 110 
ASN   H2   H  N N 111 
ASN   HA   H  N N 112 
ASN   HB2  H  N N 113 
ASN   HB3  H  N N 114 
ASN   HD21 H  N N 115 
ASN   HD22 H  N N 116 
ASN   HXT  H  N N 117 
ASP   N    N  N N 118 
ASP   CA   C  N S 119 
ASP   C    C  N N 120 
ASP   O    O  N N 121 
ASP   CB   C  N N 122 
ASP   CG   C  N N 123 
ASP   OD1  O  N N 124 
ASP   OD2  O  N N 125 
ASP   OXT  O  N N 126 
ASP   H    H  N N 127 
ASP   H2   H  N N 128 
ASP   HA   H  N N 129 
ASP   HB2  H  N N 130 
ASP   HB3  H  N N 131 
ASP   HD2  H  N N 132 
ASP   HXT  H  N N 133 
CYS   N    N  N N 134 
CYS   CA   C  N R 135 
CYS   C    C  N N 136 
CYS   O    O  N N 137 
CYS   CB   C  N N 138 
CYS   SG   S  N N 139 
CYS   OXT  O  N N 140 
CYS   H    H  N N 141 
CYS   H2   H  N N 142 
CYS   HA   H  N N 143 
CYS   HB2  H  N N 144 
CYS   HB3  H  N N 145 
CYS   HG   H  N N 146 
CYS   HXT  H  N N 147 
GLN   N    N  N N 148 
GLN   CA   C  N S 149 
GLN   C    C  N N 150 
GLN   O    O  N N 151 
GLN   CB   C  N N 152 
GLN   CG   C  N N 153 
GLN   CD   C  N N 154 
GLN   OE1  O  N N 155 
GLN   NE2  N  N N 156 
GLN   OXT  O  N N 157 
GLN   H    H  N N 158 
GLN   H2   H  N N 159 
GLN   HA   H  N N 160 
GLN   HB2  H  N N 161 
GLN   HB3  H  N N 162 
GLN   HG2  H  N N 163 
GLN   HG3  H  N N 164 
GLN   HE21 H  N N 165 
GLN   HE22 H  N N 166 
GLN   HXT  H  N N 167 
GLU   N    N  N N 168 
GLU   CA   C  N S 169 
GLU   C    C  N N 170 
GLU   O    O  N N 171 
GLU   CB   C  N N 172 
GLU   CG   C  N N 173 
GLU   CD   C  N N 174 
GLU   OE1  O  N N 175 
GLU   OE2  O  N N 176 
GLU   OXT  O  N N 177 
GLU   H    H  N N 178 
GLU   H2   H  N N 179 
GLU   HA   H  N N 180 
GLU   HB2  H  N N 181 
GLU   HB3  H  N N 182 
GLU   HG2  H  N N 183 
GLU   HG3  H  N N 184 
GLU   HE2  H  N N 185 
GLU   HXT  H  N N 186 
GLY   N    N  N N 187 
GLY   CA   C  N N 188 
GLY   C    C  N N 189 
GLY   O    O  N N 190 
GLY   OXT  O  N N 191 
GLY   H    H  N N 192 
GLY   H2   H  N N 193 
GLY   HA2  H  N N 194 
GLY   HA3  H  N N 195 
GLY   HXT  H  N N 196 
HIS   N    N  N N 197 
HIS   CA   C  N S 198 
HIS   C    C  N N 199 
HIS   O    O  N N 200 
HIS   CB   C  N N 201 
HIS   CG   C  Y N 202 
HIS   ND1  N  Y N 203 
HIS   CD2  C  Y N 204 
HIS   CE1  C  Y N 205 
HIS   NE2  N  Y N 206 
HIS   OXT  O  N N 207 
HIS   H    H  N N 208 
HIS   H2   H  N N 209 
HIS   HA   H  N N 210 
HIS   HB2  H  N N 211 
HIS   HB3  H  N N 212 
HIS   HD1  H  N N 213 
HIS   HD2  H  N N 214 
HIS   HE1  H  N N 215 
HIS   HE2  H  N N 216 
HIS   HXT  H  N N 217 
HOH   O    O  N N 218 
HOH   H1   H  N N 219 
HOH   H2   H  N N 220 
ILE   N    N  N N 221 
ILE   CA   C  N S 222 
ILE   C    C  N N 223 
ILE   O    O  N N 224 
ILE   CB   C  N S 225 
ILE   CG1  C  N N 226 
ILE   CG2  C  N N 227 
ILE   CD1  C  N N 228 
ILE   OXT  O  N N 229 
ILE   H    H  N N 230 
ILE   H2   H  N N 231 
ILE   HA   H  N N 232 
ILE   HB   H  N N 233 
ILE   HG12 H  N N 234 
ILE   HG13 H  N N 235 
ILE   HG21 H  N N 236 
ILE   HG22 H  N N 237 
ILE   HG23 H  N N 238 
ILE   HD11 H  N N 239 
ILE   HD12 H  N N 240 
ILE   HD13 H  N N 241 
ILE   HXT  H  N N 242 
LEU   N    N  N N 243 
LEU   CA   C  N S 244 
LEU   C    C  N N 245 
LEU   O    O  N N 246 
LEU   CB   C  N N 247 
LEU   CG   C  N N 248 
LEU   CD1  C  N N 249 
LEU   CD2  C  N N 250 
LEU   OXT  O  N N 251 
LEU   H    H  N N 252 
LEU   H2   H  N N 253 
LEU   HA   H  N N 254 
LEU   HB2  H  N N 255 
LEU   HB3  H  N N 256 
LEU   HG   H  N N 257 
LEU   HD11 H  N N 258 
LEU   HD12 H  N N 259 
LEU   HD13 H  N N 260 
LEU   HD21 H  N N 261 
LEU   HD22 H  N N 262 
LEU   HD23 H  N N 263 
LEU   HXT  H  N N 264 
LYS   N    N  N N 265 
LYS   CA   C  N S 266 
LYS   C    C  N N 267 
LYS   O    O  N N 268 
LYS   CB   C  N N 269 
LYS   CG   C  N N 270 
LYS   CD   C  N N 271 
LYS   CE   C  N N 272 
LYS   NZ   N  N N 273 
LYS   OXT  O  N N 274 
LYS   H    H  N N 275 
LYS   H2   H  N N 276 
LYS   HA   H  N N 277 
LYS   HB2  H  N N 278 
LYS   HB3  H  N N 279 
LYS   HG2  H  N N 280 
LYS   HG3  H  N N 281 
LYS   HD2  H  N N 282 
LYS   HD3  H  N N 283 
LYS   HE2  H  N N 284 
LYS   HE3  H  N N 285 
LYS   HZ1  H  N N 286 
LYS   HZ2  H  N N 287 
LYS   HZ3  H  N N 288 
LYS   HXT  H  N N 289 
MET   N    N  N N 290 
MET   CA   C  N S 291 
MET   C    C  N N 292 
MET   O    O  N N 293 
MET   CB   C  N N 294 
MET   CG   C  N N 295 
MET   SD   S  N N 296 
MET   CE   C  N N 297 
MET   OXT  O  N N 298 
MET   H    H  N N 299 
MET   H2   H  N N 300 
MET   HA   H  N N 301 
MET   HB2  H  N N 302 
MET   HB3  H  N N 303 
MET   HG2  H  N N 304 
MET   HG3  H  N N 305 
MET   HE1  H  N N 306 
MET   HE2  H  N N 307 
MET   HE3  H  N N 308 
MET   HXT  H  N N 309 
PHE   N    N  N N 310 
PHE   CA   C  N S 311 
PHE   C    C  N N 312 
PHE   O    O  N N 313 
PHE   CB   C  N N 314 
PHE   CG   C  Y N 315 
PHE   CD1  C  Y N 316 
PHE   CD2  C  Y N 317 
PHE   CE1  C  Y N 318 
PHE   CE2  C  Y N 319 
PHE   CZ   C  Y N 320 
PHE   OXT  O  N N 321 
PHE   H    H  N N 322 
PHE   H2   H  N N 323 
PHE   HA   H  N N 324 
PHE   HB2  H  N N 325 
PHE   HB3  H  N N 326 
PHE   HD1  H  N N 327 
PHE   HD2  H  N N 328 
PHE   HE1  H  N N 329 
PHE   HE2  H  N N 330 
PHE   HZ   H  N N 331 
PHE   HXT  H  N N 332 
PRO   N    N  N N 333 
PRO   CA   C  N S 334 
PRO   C    C  N N 335 
PRO   O    O  N N 336 
PRO   CB   C  N N 337 
PRO   CG   C  N N 338 
PRO   CD   C  N N 339 
PRO   OXT  O  N N 340 
PRO   H    H  N N 341 
PRO   HA   H  N N 342 
PRO   HB2  H  N N 343 
PRO   HB3  H  N N 344 
PRO   HG2  H  N N 345 
PRO   HG3  H  N N 346 
PRO   HD2  H  N N 347 
PRO   HD3  H  N N 348 
PRO   HXT  H  N N 349 
SER   N    N  N N 350 
SER   CA   C  N S 351 
SER   C    C  N N 352 
SER   O    O  N N 353 
SER   CB   C  N N 354 
SER   OG   O  N N 355 
SER   OXT  O  N N 356 
SER   H    H  N N 357 
SER   H2   H  N N 358 
SER   HA   H  N N 359 
SER   HB2  H  N N 360 
SER   HB3  H  N N 361 
SER   HG   H  N N 362 
SER   HXT  H  N N 363 
THR   N    N  N N 364 
THR   CA   C  N S 365 
THR   C    C  N N 366 
THR   O    O  N N 367 
THR   CB   C  N R 368 
THR   OG1  O  N N 369 
THR   CG2  C  N N 370 
THR   OXT  O  N N 371 
THR   H    H  N N 372 
THR   H2   H  N N 373 
THR   HA   H  N N 374 
THR   HB   H  N N 375 
THR   HG1  H  N N 376 
THR   HG21 H  N N 377 
THR   HG22 H  N N 378 
THR   HG23 H  N N 379 
THR   HXT  H  N N 380 
TRP   N    N  N N 381 
TRP   CA   C  N S 382 
TRP   C    C  N N 383 
TRP   O    O  N N 384 
TRP   CB   C  N N 385 
TRP   CG   C  Y N 386 
TRP   CD1  C  Y N 387 
TRP   CD2  C  Y N 388 
TRP   NE1  N  Y N 389 
TRP   CE2  C  Y N 390 
TRP   CE3  C  Y N 391 
TRP   CZ2  C  Y N 392 
TRP   CZ3  C  Y N 393 
TRP   CH2  C  Y N 394 
TRP   OXT  O  N N 395 
TRP   H    H  N N 396 
TRP   H2   H  N N 397 
TRP   HA   H  N N 398 
TRP   HB2  H  N N 399 
TRP   HB3  H  N N 400 
TRP   HD1  H  N N 401 
TRP   HE1  H  N N 402 
TRP   HE3  H  N N 403 
TRP   HZ2  H  N N 404 
TRP   HZ3  H  N N 405 
TRP   HH2  H  N N 406 
TRP   HXT  H  N N 407 
TYR   N    N  N N 408 
TYR   CA   C  N S 409 
TYR   C    C  N N 410 
TYR   O    O  N N 411 
TYR   CB   C  N N 412 
TYR   CG   C  Y N 413 
TYR   CD1  C  Y N 414 
TYR   CD2  C  Y N 415 
TYR   CE1  C  Y N 416 
TYR   CE2  C  Y N 417 
TYR   CZ   C  Y N 418 
TYR   OH   O  N N 419 
TYR   OXT  O  N N 420 
TYR   H    H  N N 421 
TYR   H2   H  N N 422 
TYR   HA   H  N N 423 
TYR   HB2  H  N N 424 
TYR   HB3  H  N N 425 
TYR   HD1  H  N N 426 
TYR   HD2  H  N N 427 
TYR   HE1  H  N N 428 
TYR   HE2  H  N N 429 
TYR   HH   H  N N 430 
TYR   HXT  H  N N 431 
VAL   N    N  N N 432 
VAL   CA   C  N S 433 
VAL   C    C  N N 434 
VAL   O    O  N N 435 
VAL   CB   C  N N 436 
VAL   CG1  C  N N 437 
VAL   CG2  C  N N 438 
VAL   OXT  O  N N 439 
VAL   H    H  N N 440 
VAL   H2   H  N N 441 
VAL   HA   H  N N 442 
VAL   HB   H  N N 443 
VAL   HG11 H  N N 444 
VAL   HG12 H  N N 445 
VAL   HG13 H  N N 446 
VAL   HG21 H  N N 447 
VAL   HG22 H  N N 448 
VAL   HG23 H  N N 449 
VAL   HXT  H  N N 450 
# 
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 
A1ITT C23 C22  doub Y N 1   
A1ITT C23 C24  sing Y N 2   
A1ITT C25 C24  sing N N 3   
A1ITT C25 C26  sing N N 4   
A1ITT C22 C21  sing Y N 5   
A1ITT C24 C19  doub Y N 6   
A1ITT C26 C27  sing N N 7   
A1ITT C21 C20  doub Y N 8   
A1ITT C19 C20  sing Y N 9   
A1ITT C19 N05  sing N N 10  
A1ITT C27 C28  sing Y N 11  
A1ITT C27 C04  doub Y N 12  
A1ITT C28 C29  doub Y N 13  
A1ITT N05 C04  sing N N 14  
A1ITT N05 C06  sing N N 15  
A1ITT C04 C03  sing Y N 16  
A1ITT C08 C07  sing N N 17  
A1ITT C08 C09  sing N N 18  
A1ITT C29 C02  sing Y N 19  
A1ITT C07 C06  sing N N 20  
A1ITT C03 C02  doub Y N 21  
A1ITT C09 N10  sing N N 22  
A1ITT C02 CL01 sing N N 23  
A1ITT N10 C11  sing N N 24  
A1ITT C11 C12  sing N N 25  
A1ITT C12 C13  sing N N 26  
A1ITT C13 C14  sing N N 27  
A1ITT O18 C14  doub N N 28  
A1ITT C14 O15  sing N N 29  
A1ITT C16 O15  sing N N 30  
A1ITT C16 C17  sing N N 31  
A1ITT C12 H1   sing N N 32  
A1ITT C12 H2   sing N N 33  
A1ITT C11 H3   sing N N 34  
A1ITT C11 H4   sing N N 35  
A1ITT N10 H5   sing N N 36  
A1ITT C03 H7   sing N N 37  
A1ITT C06 H8   sing N N 38  
A1ITT C06 H9   sing N N 39  
A1ITT C07 H10  sing N N 40  
A1ITT C07 H11  sing N N 41  
A1ITT C08 H12  sing N N 42  
A1ITT C08 H13  sing N N 43  
A1ITT C09 H14  sing N N 44  
A1ITT C09 H15  sing N N 45  
A1ITT C13 H16  sing N N 46  
A1ITT C13 H17  sing N N 47  
A1ITT C16 H18  sing N N 48  
A1ITT C16 H19  sing N N 49  
A1ITT C17 H20  sing N N 50  
A1ITT C17 H21  sing N N 51  
A1ITT C17 H22  sing N N 52  
A1ITT C20 H23  sing N N 53  
A1ITT C21 H24  sing N N 54  
A1ITT C22 H25  sing N N 55  
A1ITT C23 H26  sing N N 56  
A1ITT C25 H27  sing N N 57  
A1ITT C25 H28  sing N N 58  
A1ITT C26 H29  sing N N 59  
A1ITT C26 H30  sing N N 60  
A1ITT C28 H31  sing N N 61  
A1ITT C29 H32  sing N N 62  
ALA   N   CA   sing N N 63  
ALA   N   H    sing N N 64  
ALA   N   H2   sing N N 65  
ALA   CA  C    sing N N 66  
ALA   CA  CB   sing N N 67  
ALA   CA  HA   sing N N 68  
ALA   C   O    doub N N 69  
ALA   C   OXT  sing N N 70  
ALA   CB  HB1  sing N N 71  
ALA   CB  HB2  sing N N 72  
ALA   CB  HB3  sing N N 73  
ALA   OXT HXT  sing N N 74  
ARG   N   CA   sing N N 75  
ARG   N   H    sing N N 76  
ARG   N   H2   sing N N 77  
ARG   CA  C    sing N N 78  
ARG   CA  CB   sing N N 79  
ARG   CA  HA   sing N N 80  
ARG   C   O    doub N N 81  
ARG   C   OXT  sing N N 82  
ARG   CB  CG   sing N N 83  
ARG   CB  HB2  sing N N 84  
ARG   CB  HB3  sing N N 85  
ARG   CG  CD   sing N N 86  
ARG   CG  HG2  sing N N 87  
ARG   CG  HG3  sing N N 88  
ARG   CD  NE   sing N N 89  
ARG   CD  HD2  sing N N 90  
ARG   CD  HD3  sing N N 91  
ARG   NE  CZ   sing N N 92  
ARG   NE  HE   sing N N 93  
ARG   CZ  NH1  sing N N 94  
ARG   CZ  NH2  doub N N 95  
ARG   NH1 HH11 sing N N 96  
ARG   NH1 HH12 sing N N 97  
ARG   NH2 HH21 sing N N 98  
ARG   NH2 HH22 sing N N 99  
ARG   OXT HXT  sing N N 100 
ASN   N   CA   sing N N 101 
ASN   N   H    sing N N 102 
ASN   N   H2   sing N N 103 
ASN   CA  C    sing N N 104 
ASN   CA  CB   sing N N 105 
ASN   CA  HA   sing N N 106 
ASN   C   O    doub N N 107 
ASN   C   OXT  sing N N 108 
ASN   CB  CG   sing N N 109 
ASN   CB  HB2  sing N N 110 
ASN   CB  HB3  sing N N 111 
ASN   CG  OD1  doub N N 112 
ASN   CG  ND2  sing N N 113 
ASN   ND2 HD21 sing N N 114 
ASN   ND2 HD22 sing N N 115 
ASN   OXT HXT  sing N N 116 
ASP   N   CA   sing N N 117 
ASP   N   H    sing N N 118 
ASP   N   H2   sing N N 119 
ASP   CA  C    sing N N 120 
ASP   CA  CB   sing N N 121 
ASP   CA  HA   sing N N 122 
ASP   C   O    doub N N 123 
ASP   C   OXT  sing N N 124 
ASP   CB  CG   sing N N 125 
ASP   CB  HB2  sing N N 126 
ASP   CB  HB3  sing N N 127 
ASP   CG  OD1  doub N N 128 
ASP   CG  OD2  sing N N 129 
ASP   OD2 HD2  sing N N 130 
ASP   OXT HXT  sing N N 131 
CYS   N   CA   sing N N 132 
CYS   N   H    sing N N 133 
CYS   N   H2   sing N N 134 
CYS   CA  C    sing N N 135 
CYS   CA  CB   sing N N 136 
CYS   CA  HA   sing N N 137 
CYS   C   O    doub N N 138 
CYS   C   OXT  sing N N 139 
CYS   CB  SG   sing N N 140 
CYS   CB  HB2  sing N N 141 
CYS   CB  HB3  sing N N 142 
CYS   SG  HG   sing N N 143 
CYS   OXT HXT  sing N N 144 
GLN   N   CA   sing N N 145 
GLN   N   H    sing N N 146 
GLN   N   H2   sing N N 147 
GLN   CA  C    sing N N 148 
GLN   CA  CB   sing N N 149 
GLN   CA  HA   sing N N 150 
GLN   C   O    doub N N 151 
GLN   C   OXT  sing N N 152 
GLN   CB  CG   sing N N 153 
GLN   CB  HB2  sing N N 154 
GLN   CB  HB3  sing N N 155 
GLN   CG  CD   sing N N 156 
GLN   CG  HG2  sing N N 157 
GLN   CG  HG3  sing N N 158 
GLN   CD  OE1  doub N N 159 
GLN   CD  NE2  sing N N 160 
GLN   NE2 HE21 sing N N 161 
GLN   NE2 HE22 sing N N 162 
GLN   OXT HXT  sing N N 163 
GLU   N   CA   sing N N 164 
GLU   N   H    sing N N 165 
GLU   N   H2   sing N N 166 
GLU   CA  C    sing N N 167 
GLU   CA  CB   sing N N 168 
GLU   CA  HA   sing N N 169 
GLU   C   O    doub N N 170 
GLU   C   OXT  sing N N 171 
GLU   CB  CG   sing N N 172 
GLU   CB  HB2  sing N N 173 
GLU   CB  HB3  sing N N 174 
GLU   CG  CD   sing N N 175 
GLU   CG  HG2  sing N N 176 
GLU   CG  HG3  sing N N 177 
GLU   CD  OE1  doub N N 178 
GLU   CD  OE2  sing N N 179 
GLU   OE2 HE2  sing N N 180 
GLU   OXT HXT  sing N N 181 
GLY   N   CA   sing N N 182 
GLY   N   H    sing N N 183 
GLY   N   H2   sing N N 184 
GLY   CA  C    sing N N 185 
GLY   CA  HA2  sing N N 186 
GLY   CA  HA3  sing N N 187 
GLY   C   O    doub N N 188 
GLY   C   OXT  sing N N 189 
GLY   OXT HXT  sing N N 190 
HIS   N   CA   sing N N 191 
HIS   N   H    sing N N 192 
HIS   N   H2   sing N N 193 
HIS   CA  C    sing N N 194 
HIS   CA  CB   sing N N 195 
HIS   CA  HA   sing N N 196 
HIS   C   O    doub N N 197 
HIS   C   OXT  sing N N 198 
HIS   CB  CG   sing N N 199 
HIS   CB  HB2  sing N N 200 
HIS   CB  HB3  sing N N 201 
HIS   CG  ND1  sing Y N 202 
HIS   CG  CD2  doub Y N 203 
HIS   ND1 CE1  doub Y N 204 
HIS   ND1 HD1  sing N N 205 
HIS   CD2 NE2  sing Y N 206 
HIS   CD2 HD2  sing N N 207 
HIS   CE1 NE2  sing Y N 208 
HIS   CE1 HE1  sing N N 209 
HIS   NE2 HE2  sing N N 210 
HIS   OXT HXT  sing N N 211 
HOH   O   H1   sing N N 212 
HOH   O   H2   sing N N 213 
ILE   N   CA   sing N N 214 
ILE   N   H    sing N N 215 
ILE   N   H2   sing N N 216 
ILE   CA  C    sing N N 217 
ILE   CA  CB   sing N N 218 
ILE   CA  HA   sing N N 219 
ILE   C   O    doub N N 220 
ILE   C   OXT  sing N N 221 
ILE   CB  CG1  sing N N 222 
ILE   CB  CG2  sing N N 223 
ILE   CB  HB   sing N N 224 
ILE   CG1 CD1  sing N N 225 
ILE   CG1 HG12 sing N N 226 
ILE   CG1 HG13 sing N N 227 
ILE   CG2 HG21 sing N N 228 
ILE   CG2 HG22 sing N N 229 
ILE   CG2 HG23 sing N N 230 
ILE   CD1 HD11 sing N N 231 
ILE   CD1 HD12 sing N N 232 
ILE   CD1 HD13 sing N N 233 
ILE   OXT HXT  sing N N 234 
LEU   N   CA   sing N N 235 
LEU   N   H    sing N N 236 
LEU   N   H2   sing N N 237 
LEU   CA  C    sing N N 238 
LEU   CA  CB   sing N N 239 
LEU   CA  HA   sing N N 240 
LEU   C   O    doub N N 241 
LEU   C   OXT  sing N N 242 
LEU   CB  CG   sing N N 243 
LEU   CB  HB2  sing N N 244 
LEU   CB  HB3  sing N N 245 
LEU   CG  CD1  sing N N 246 
LEU   CG  CD2  sing N N 247 
LEU   CG  HG   sing N N 248 
LEU   CD1 HD11 sing N N 249 
LEU   CD1 HD12 sing N N 250 
LEU   CD1 HD13 sing N N 251 
LEU   CD2 HD21 sing N N 252 
LEU   CD2 HD22 sing N N 253 
LEU   CD2 HD23 sing N N 254 
LEU   OXT HXT  sing N N 255 
LYS   N   CA   sing N N 256 
LYS   N   H    sing N N 257 
LYS   N   H2   sing N N 258 
LYS   CA  C    sing N N 259 
LYS   CA  CB   sing N N 260 
LYS   CA  HA   sing N N 261 
LYS   C   O    doub N N 262 
LYS   C   OXT  sing N N 263 
LYS   CB  CG   sing N N 264 
LYS   CB  HB2  sing N N 265 
LYS   CB  HB3  sing N N 266 
LYS   CG  CD   sing N N 267 
LYS   CG  HG2  sing N N 268 
LYS   CG  HG3  sing N N 269 
LYS   CD  CE   sing N N 270 
LYS   CD  HD2  sing N N 271 
LYS   CD  HD3  sing N N 272 
LYS   CE  NZ   sing N N 273 
LYS   CE  HE2  sing N N 274 
LYS   CE  HE3  sing N N 275 
LYS   NZ  HZ1  sing N N 276 
LYS   NZ  HZ2  sing N N 277 
LYS   NZ  HZ3  sing N N 278 
LYS   OXT HXT  sing N N 279 
MET   N   CA   sing N N 280 
MET   N   H    sing N N 281 
MET   N   H2   sing N N 282 
MET   CA  C    sing N N 283 
MET   CA  CB   sing N N 284 
MET   CA  HA   sing N N 285 
MET   C   O    doub N N 286 
MET   C   OXT  sing N N 287 
MET   CB  CG   sing N N 288 
MET   CB  HB2  sing N N 289 
MET   CB  HB3  sing N N 290 
MET   CG  SD   sing N N 291 
MET   CG  HG2  sing N N 292 
MET   CG  HG3  sing N N 293 
MET   SD  CE   sing N N 294 
MET   CE  HE1  sing N N 295 
MET   CE  HE2  sing N N 296 
MET   CE  HE3  sing N N 297 
MET   OXT HXT  sing N N 298 
PHE   N   CA   sing N N 299 
PHE   N   H    sing N N 300 
PHE   N   H2   sing N N 301 
PHE   CA  C    sing N N 302 
PHE   CA  CB   sing N N 303 
PHE   CA  HA   sing N N 304 
PHE   C   O    doub N N 305 
PHE   C   OXT  sing N N 306 
PHE   CB  CG   sing N N 307 
PHE   CB  HB2  sing N N 308 
PHE   CB  HB3  sing N N 309 
PHE   CG  CD1  doub Y N 310 
PHE   CG  CD2  sing Y N 311 
PHE   CD1 CE1  sing Y N 312 
PHE   CD1 HD1  sing N N 313 
PHE   CD2 CE2  doub Y N 314 
PHE   CD2 HD2  sing N N 315 
PHE   CE1 CZ   doub Y N 316 
PHE   CE1 HE1  sing N N 317 
PHE   CE2 CZ   sing Y N 318 
PHE   CE2 HE2  sing N N 319 
PHE   CZ  HZ   sing N N 320 
PHE   OXT HXT  sing N N 321 
PRO   N   CA   sing N N 322 
PRO   N   CD   sing N N 323 
PRO   N   H    sing N N 324 
PRO   CA  C    sing N N 325 
PRO   CA  CB   sing N N 326 
PRO   CA  HA   sing N N 327 
PRO   C   O    doub N N 328 
PRO   C   OXT  sing N N 329 
PRO   CB  CG   sing N N 330 
PRO   CB  HB2  sing N N 331 
PRO   CB  HB3  sing N N 332 
PRO   CG  CD   sing N N 333 
PRO   CG  HG2  sing N N 334 
PRO   CG  HG3  sing N N 335 
PRO   CD  HD2  sing N N 336 
PRO   CD  HD3  sing N N 337 
PRO   OXT HXT  sing N N 338 
SER   N   CA   sing N N 339 
SER   N   H    sing N N 340 
SER   N   H2   sing N N 341 
SER   CA  C    sing N N 342 
SER   CA  CB   sing N N 343 
SER   CA  HA   sing N N 344 
SER   C   O    doub N N 345 
SER   C   OXT  sing N N 346 
SER   CB  OG   sing N N 347 
SER   CB  HB2  sing N N 348 
SER   CB  HB3  sing N N 349 
SER   OG  HG   sing N N 350 
SER   OXT HXT  sing N N 351 
THR   N   CA   sing N N 352 
THR   N   H    sing N N 353 
THR   N   H2   sing N N 354 
THR   CA  C    sing N N 355 
THR   CA  CB   sing N N 356 
THR   CA  HA   sing N N 357 
THR   C   O    doub N N 358 
THR   C   OXT  sing N N 359 
THR   CB  OG1  sing N N 360 
THR   CB  CG2  sing N N 361 
THR   CB  HB   sing N N 362 
THR   OG1 HG1  sing N N 363 
THR   CG2 HG21 sing N N 364 
THR   CG2 HG22 sing N N 365 
THR   CG2 HG23 sing N N 366 
THR   OXT HXT  sing N N 367 
TRP   N   CA   sing N N 368 
TRP   N   H    sing N N 369 
TRP   N   H2   sing N N 370 
TRP   CA  C    sing N N 371 
TRP   CA  CB   sing N N 372 
TRP   CA  HA   sing N N 373 
TRP   C   O    doub N N 374 
TRP   C   OXT  sing N N 375 
TRP   CB  CG   sing N N 376 
TRP   CB  HB2  sing N N 377 
TRP   CB  HB3  sing N N 378 
TRP   CG  CD1  doub Y N 379 
TRP   CG  CD2  sing Y N 380 
TRP   CD1 NE1  sing Y N 381 
TRP   CD1 HD1  sing N N 382 
TRP   CD2 CE2  doub Y N 383 
TRP   CD2 CE3  sing Y N 384 
TRP   NE1 CE2  sing Y N 385 
TRP   NE1 HE1  sing N N 386 
TRP   CE2 CZ2  sing Y N 387 
TRP   CE3 CZ3  doub Y N 388 
TRP   CE3 HE3  sing N N 389 
TRP   CZ2 CH2  doub Y N 390 
TRP   CZ2 HZ2  sing N N 391 
TRP   CZ3 CH2  sing Y N 392 
TRP   CZ3 HZ3  sing N N 393 
TRP   CH2 HH2  sing N N 394 
TRP   OXT HXT  sing N N 395 
TYR   N   CA   sing N N 396 
TYR   N   H    sing N N 397 
TYR   N   H2   sing N N 398 
TYR   CA  C    sing N N 399 
TYR   CA  CB   sing N N 400 
TYR   CA  HA   sing N N 401 
TYR   C   O    doub N N 402 
TYR   C   OXT  sing N N 403 
TYR   CB  CG   sing N N 404 
TYR   CB  HB2  sing N N 405 
TYR   CB  HB3  sing N N 406 
TYR   CG  CD1  doub Y N 407 
TYR   CG  CD2  sing Y N 408 
TYR   CD1 CE1  sing Y N 409 
TYR   CD1 HD1  sing N N 410 
TYR   CD2 CE2  doub Y N 411 
TYR   CD2 HD2  sing N N 412 
TYR   CE1 CZ   doub Y N 413 
TYR   CE1 HE1  sing N N 414 
TYR   CE2 CZ   sing Y N 415 
TYR   CE2 HE2  sing N N 416 
TYR   CZ  OH   sing N N 417 
TYR   OH  HH   sing N N 418 
TYR   OXT HXT  sing N N 419 
VAL   N   CA   sing N N 420 
VAL   N   H    sing N N 421 
VAL   N   H2   sing N N 422 
VAL   CA  C    sing N N 423 
VAL   CA  CB   sing N N 424 
VAL   CA  HA   sing N N 425 
VAL   C   O    doub N N 426 
VAL   C   OXT  sing N N 427 
VAL   CB  CG1  sing N N 428 
VAL   CB  CG2  sing N N 429 
VAL   CB  HB   sing N N 430 
VAL   CG1 HG11 sing N N 431 
VAL   CG1 HG12 sing N N 432 
VAL   CG1 HG13 sing N N 433 
VAL   CG2 HG21 sing N N 434 
VAL   CG2 HG22 sing N N 435 
VAL   CG2 HG23 sing N N 436 
VAL   OXT HXT  sing N N 437 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'Fondazione CARIPLO'        Italy            2017-0746 1 
'Worldwide Cancer Research' 'United Kingdom' 19-0003   2 
# 
_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   2xbf 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9H9T 
_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]   0.005670 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000116 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.025690 
_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]   0.016756 
_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  
CL 
N  
O  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N    . SER   A 1 1   ? -18.683 -4.446  -7.480  1.00 110.96 ? 519  SER   A N    1 
ATOM   2    C  CA   . SER   A 1 1   ? -19.337 -3.810  -8.617  1.00 104.74 ? 519  SER   A CA   1 
ATOM   3    C  C    . SER   A 1 1   ? -18.313 -3.323  -9.637  1.00 99.54  ? 519  SER   A C    1 
ATOM   4    O  O    . SER   A 1 1   ? -17.107 -3.477  -9.443  1.00 104.39 ? 519  SER   A O    1 
ATOM   5    C  CB   . SER   A 1 1   ? -20.211 -2.644  -8.151  1.00 102.49 ? 519  SER   A CB   1 
ATOM   6    O  OG   . SER   A 1 1   ? -20.868 -2.029  -9.246  1.00 97.47  ? 519  SER   A OG   1 
ATOM   7    N  N    . ARG   A 1 2   ? -18.802 -2.734  -10.724 1.00 87.42  ? 520  ARG   A N    1 
ATOM   8    C  CA   . ARG   A 1 2   ? -17.955 -2.239  -11.801 1.00 80.72  ? 520  ARG   A CA   1 
ATOM   9    C  C    . ARG   A 1 2   ? -17.777 -0.733  -11.666 1.00 78.64  ? 520  ARG   A C    1 
ATOM   10   O  O    . ARG   A 1 2   ? -18.757 -0.003  -11.484 1.00 76.78  ? 520  ARG   A O    1 
ATOM   11   C  CB   . ARG   A 1 2   ? -18.562 -2.570  -13.166 1.00 74.82  ? 520  ARG   A CB   1 
ATOM   12   C  CG   . ARG   A 1 2   ? -18.682 -4.056  -13.464 1.00 76.41  ? 520  ARG   A CG   1 
ATOM   13   C  CD   . ARG   A 1 2   ? -19.098 -4.292  -14.908 1.00 74.09  ? 520  ARG   A CD   1 
ATOM   14   N  NE   . ARG   A 1 2   ? -19.170 -5.714  -15.231 1.00 75.95  ? 520  ARG   A NE   1 
ATOM   15   C  CZ   . ARG   A 1 2   ? -20.271 -6.450  -15.127 1.00 77.84  ? 520  ARG   A CZ   1 
ATOM   16   N  NH1  . ARG   A 1 2   ? -21.403 -5.900  -14.709 1.00 77.65  ? 520  ARG   A NH1  1 
ATOM   17   N  NH2  . ARG   A 1 2   ? -20.242 -7.738  -15.442 1.00 79.28  ? 520  ARG   A NH2  1 
ATOM   18   N  N    . ASP   A 1 3   ? -16.532 -0.271  -11.758 1.00 75.73  ? 521  ASP   A N    1 
ATOM   19   C  CA   . ASP   A 1 3   ? -16.286 1.159   -11.857 1.00 68.89  ? 521  ASP   A CA   1 
ATOM   20   C  C    . ASP   A 1 3   ? -16.653 1.638   -13.262 1.00 63.33  ? 521  ASP   A C    1 
ATOM   21   O  O    . ASP   A 1 3   ? -17.158 0.878   -14.094 1.00 62.04  ? 521  ASP   A O    1 
ATOM   22   C  CB   . ASP   A 1 3   ? -14.835 1.484   -11.494 1.00 72.14  ? 521  ASP   A CB   1 
ATOM   23   C  CG   . ASP   A 1 3   ? -13.820 0.861   -12.446 1.00 73.79  ? 521  ASP   A CG   1 
ATOM   24   O  OD1  . ASP   A 1 3   ? -14.215 0.198   -13.428 1.00 72.81  ? 521  ASP   A OD1  1 
ATOM   25   O  OD2  . ASP   A 1 3   ? -12.608 1.040   -12.205 1.00 76.21  ? 521  ASP   A OD2  1 
ATOM   26   N  N    . TYR   A 1 4   ? -16.396 2.919   -13.539 1.00 56.74  ? 522  TYR   A N    1 
ATOM   27   C  CA   . TYR   A 1 4   ? -16.783 3.462   -14.838 1.00 54.42  ? 522  TYR   A CA   1 
ATOM   28   C  C    . TYR   A 1 4   ? -16.013 2.797   -15.972 1.00 54.98  ? 522  TYR   A C    1 
ATOM   29   O  O    . TYR   A 1 4   ? -16.588 2.493   -17.024 1.00 54.26  ? 522  TYR   A O    1 
ATOM   30   C  CB   . TYR   A 1 4   ? -16.571 4.973   -14.884 1.00 54.23  ? 522  TYR   A CB   1 
ATOM   31   C  CG   . TYR   A 1 4   ? -16.749 5.527   -16.280 1.00 57.96  ? 522  TYR   A CG   1 
ATOM   32   C  CD1  . TYR   A 1 4   ? -17.995 5.516   -16.893 1.00 64.68  ? 522  TYR   A CD1  1 
ATOM   33   C  CD2  . TYR   A 1 4   ? -15.672 6.033   -16.995 1.00 61.73  ? 522  TYR   A CD2  1 
ATOM   34   C  CE1  . TYR   A 1 4   ? -18.169 6.009   -18.171 1.00 66.95  ? 522  TYR   A CE1  1 
ATOM   35   C  CE2  . TYR   A 1 4   ? -15.836 6.529   -18.276 1.00 64.37  ? 522  TYR   A CE2  1 
ATOM   36   C  CZ   . TYR   A 1 4   ? -17.087 6.514   -18.858 1.00 67.40  ? 522  TYR   A CZ   1 
ATOM   37   O  OH   . TYR   A 1 4   ? -17.260 7.005   -20.132 1.00 67.34  ? 522  TYR   A OH   1 
ATOM   38   N  N    . LYS   A 1 5   ? -14.712 2.570   -15.781 1.00 56.45  ? 523  LYS   A N    1 
ATOM   39   C  CA   . LYS   A 1 5   ? -13.904 1.967   -16.835 1.00 60.55  ? 523  LYS   A CA   1 
ATOM   40   C  C    . LYS   A 1 5   ? -14.378 0.554   -17.152 1.00 60.87  ? 523  LYS   A C    1 
ATOM   41   O  O    . LYS   A 1 5   ? -14.521 0.180   -18.323 1.00 58.40  ? 523  LYS   A O    1 
ATOM   42   C  CB   . LYS   A 1 5   ? -12.434 1.964   -16.427 1.00 59.50  ? 523  LYS   A CB   1 
ATOM   43   C  CG   . LYS   A 1 5   ? -11.519 1.405   -17.486 1.00 61.32  ? 523  LYS   A CG   1 
ATOM   44   C  CD   . LYS   A 1 5   ? -10.072 1.478   -17.055 1.00 65.12  ? 523  LYS   A CD   1 
ATOM   45   C  CE   . LYS   A 1 5   ? -9.191  0.874   -18.119 1.00 67.42  ? 523  LYS   A CE   1 
ATOM   46   N  NZ   . LYS   A 1 5   ? -7.745  1.114   -17.870 1.00 71.32  ? 523  LYS   A NZ   1 
ATOM   47   N  N    . ARG   A 1 6   ? -14.627 -0.250  -16.116 1.00 60.11  ? 524  ARG   A N    1 
ATOM   48   C  CA   . ARG   A 1 6   ? -15.130 -1.599  -16.344 1.00 61.19  ? 524  ARG   A CA   1 
ATOM   49   C  C    . ARG   A 1 6   ? -16.542 -1.577  -16.917 1.00 59.40  ? 524  ARG   A C    1 
ATOM   50   O  O    . ARG   A 1 6   ? -16.887 -2.430  -17.743 1.00 59.40  ? 524  ARG   A O    1 
ATOM   51   C  CB   . ARG   A 1 6   ? -15.086 -2.403  -15.044 1.00 63.38  ? 524  ARG   A CB   1 
ATOM   52   C  CG   . ARG   A 1 6   ? -13.896 -3.351  -14.931 1.00 67.49  ? 524  ARG   A CG   1 
ATOM   53   C  CD   . ARG   A 1 6   ? -12.582 -2.677  -15.312 1.00 71.96  ? 524  ARG   A CD   1 
ATOM   54   N  NE   . ARG   A 1 6   ? -12.144 -1.697  -14.321 1.00 70.07  ? 524  ARG   A NE   1 
ATOM   55   C  CZ   . ARG   A 1 6   ? -10.976 -1.063  -14.362 1.00 74.24  ? 524  ARG   A CZ   1 
ATOM   56   N  NH1  . ARG   A 1 6   ? -10.121 -1.308  -15.346 1.00 75.95  ? 524  ARG   A NH1  1 
ATOM   57   N  NH2  . ARG   A 1 6   ? -10.659 -0.188  -13.418 1.00 73.98  ? 524  ARG   A NH2  1 
ATOM   58   N  N    . LYS   A 1 7   ? -17.363 -0.608  -16.503 1.00 57.90  ? 525  LYS   A N    1 
ATOM   59   C  CA   . LYS   A 1 7   ? -18.700 -0.476  -17.073 1.00 56.55  ? 525  LYS   A CA   1 
ATOM   60   C  C    . LYS   A 1 7   ? -18.636 -0.175  -18.565 1.00 54.13  ? 525  LYS   A C    1 
ATOM   61   O  O    . LYS   A 1 7   ? -19.407 -0.736  -19.352 1.00 53.09  ? 525  LYS   A O    1 
ATOM   62   C  CB   . LYS   A 1 7   ? -19.479 0.621   -16.349 1.00 64.18  ? 525  LYS   A CB   1 
ATOM   63   C  CG   . LYS   A 1 7   ? -20.152 0.192   -15.056 1.00 65.03  ? 525  LYS   A CG   1 
ATOM   64   C  CD   . LYS   A 1 7   ? -20.998 1.330   -14.506 1.00 62.60  ? 525  LYS   A CD   1 
ATOM   65   C  CE   . LYS   A 1 7   ? -21.688 0.953   -13.209 1.00 67.03  ? 525  LYS   A CE   1 
ATOM   66   N  NZ   . LYS   A 1 7   ? -22.576 2.051   -12.736 1.00 66.37  ? 525  LYS   A NZ   1 
ATOM   67   N  N    . TYR   A 1 8   ? -17.725 0.711   -18.974 1.00 56.26  ? 526  TYR   A N    1 
ATOM   68   C  CA   . TYR   A 1 8   ? -17.630 1.072   -20.385 1.00 55.08  ? 526  TYR   A CA   1 
ATOM   69   C  C    . TYR   A 1 8   ? -17.230 -0.129  -21.232 1.00 53.96  ? 526  TYR   A C    1 
ATOM   70   O  O    . TYR   A 1 8   ? -17.817 -0.378  -22.292 1.00 53.31  ? 526  TYR   A O    1 
ATOM   71   C  CB   . TYR   A 1 8   ? -16.636 2.217   -20.577 1.00 56.54  ? 526  TYR   A CB   1 
ATOM   72   C  CG   . TYR   A 1 8   ? -16.576 2.704   -22.005 1.00 59.79  ? 526  TYR   A CG   1 
ATOM   73   C  CD1  . TYR   A 1 8   ? -15.508 2.375   -22.830 1.00 65.70  ? 526  TYR   A CD1  1 
ATOM   74   C  CD2  . TYR   A 1 8   ? -17.598 3.477   -22.534 1.00 57.42  ? 526  TYR   A CD2  1 
ATOM   75   C  CE1  . TYR   A 1 8   ? -15.459 2.814   -24.142 1.00 70.14  ? 526  TYR   A CE1  1 
ATOM   76   C  CE2  . TYR   A 1 8   ? -17.558 3.920   -23.841 1.00 63.12  ? 526  TYR   A CE2  1 
ATOM   77   C  CZ   . TYR   A 1 8   ? -16.487 3.587   -24.641 1.00 72.18  ? 526  TYR   A CZ   1 
ATOM   78   O  OH   . TYR   A 1 8   ? -16.449 4.029   -25.943 1.00 78.42  ? 526  TYR   A OH   1 
ATOM   79   N  N    . GLU   A 1 9   ? -16.225 -0.883  -20.782 1.00 56.23  ? 527  GLU   A N    1 
ATOM   80   C  CA   . GLU   A 1 9   ? -15.821 -2.089  -21.498 1.00 57.76  ? 527  GLU   A CA   1 
ATOM   81   C  C    . GLU   A 1 9   ? -16.962 -3.097  -21.545 1.00 59.11  ? 527  GLU   A C    1 
ATOM   82   O  O    . GLU   A 1 9   ? -17.240 -3.692  -22.593 1.00 58.43  ? 527  GLU   A O    1 
ATOM   83   C  CB   . GLU   A 1 9   ? -14.586 -2.701  -20.835 1.00 61.55  ? 527  GLU   A CB   1 
ATOM   84   C  CG   . GLU   A 1 9   ? -13.327 -1.856  -20.950 1.00 66.17  ? 527  GLU   A CG   1 
ATOM   85   C  CD   . GLU   A 1 9   ? -12.232 -2.315  -20.005 1.00 75.74  ? 527  GLU   A CD   1 
ATOM   86   O  OE1  . GLU   A 1 9   ? -11.136 -1.716  -20.026 1.00 79.88  ? 527  GLU   A OE1  1 
ATOM   87   O  OE2  . GLU   A 1 9   ? -12.466 -3.273  -19.239 1.00 78.00  ? 527  GLU   A OE2  1 
ATOM   88   N  N    . PHE   A 1 10  ? -17.631 -3.301  -20.408 1.00 59.84  ? 528  PHE   A N    1 
ATOM   89   C  CA   . PHE   A 1 10  ? -18.814 -4.155  -20.373 1.00 58.07  ? 528  PHE   A CA   1 
ATOM   90   C  C    . PHE   A 1 10  ? -19.887 -3.646  -21.327 1.00 55.31  ? 528  PHE   A C    1 
ATOM   91   O  O    . PHE   A 1 10  ? -20.595 -4.437  -21.961 1.00 55.53  ? 528  PHE   A O    1 
ATOM   92   C  CB   . PHE   A 1 10  ? -19.348 -4.223  -18.941 1.00 61.59  ? 528  PHE   A CB   1 
ATOM   93   C  CG   . PHE   A 1 10  ? -20.524 -5.139  -18.767 1.00 66.91  ? 528  PHE   A CG   1 
ATOM   94   C  CD1  . PHE   A 1 10  ? -20.346 -6.506  -18.673 1.00 69.99  ? 528  PHE   A CD1  1 
ATOM   95   C  CD2  . PHE   A 1 10  ? -21.809 -4.628  -18.679 1.00 67.60  ? 528  PHE   A CD2  1 
ATOM   96   C  CE1  . PHE   A 1 10  ? -21.426 -7.351  -18.506 1.00 70.74  ? 528  PHE   A CE1  1 
ATOM   97   C  CE2  . PHE   A 1 10  ? -22.893 -5.468  -18.511 1.00 66.42  ? 528  PHE   A CE2  1 
ATOM   98   C  CZ   . PHE   A 1 10  ? -22.701 -6.830  -18.423 1.00 68.57  ? 528  PHE   A CZ   1 
ATOM   99   N  N    . PHE   A 1 11  ? -20.011 -2.324  -21.449 1.00 53.95  ? 529  PHE   A N    1 
ATOM   100  C  CA   . PHE   A 1 11  ? -21.016 -1.739  -22.330 1.00 50.27  ? 529  PHE   A CA   1 
ATOM   101  C  C    . PHE   A 1 11  ? -20.671 -1.978  -23.796 1.00 52.38  ? 529  PHE   A C    1 
ATOM   102  O  O    . PHE   A 1 11  ? -21.527 -2.394  -24.585 1.00 53.65  ? 529  PHE   A O    1 
ATOM   103  C  CB   . PHE   A 1 11  ? -21.147 -0.246  -22.029 1.00 48.76  ? 529  PHE   A CB   1 
ATOM   104  C  CG   . PHE   A 1 11  ? -21.904 0.530   -23.067 1.00 47.31  ? 529  PHE   A CG   1 
ATOM   105  C  CD1  . PHE   A 1 11  ? -23.271 0.362   -23.220 1.00 50.72  ? 529  PHE   A CD1  1 
ATOM   106  C  CD2  . PHE   A 1 11  ? -21.252 1.450   -23.871 1.00 48.81  ? 529  PHE   A CD2  1 
ATOM   107  C  CE1  . PHE   A 1 11  ? -23.970 1.087   -24.170 1.00 50.29  ? 529  PHE   A CE1  1 
ATOM   108  C  CE2  . PHE   A 1 11  ? -21.945 2.178   -24.821 1.00 49.07  ? 529  PHE   A CE2  1 
ATOM   109  C  CZ   . PHE   A 1 11  ? -23.306 1.996   -24.970 1.00 49.14  ? 529  PHE   A CZ   1 
ATOM   110  N  N    . ARG   A 1 12  ? -19.414 -1.729  -24.177 1.00 52.85  ? 530  ARG   A N    1 
ATOM   111  C  CA   . ARG   A 1 12  ? -19.013 -1.919  -25.568 1.00 56.22  ? 530  ARG   A CA   1 
ATOM   112  C  C    . ARG   A 1 12  ? -19.099 -3.381  -25.989 1.00 57.54  ? 530  ARG   A C    1 
ATOM   113  O  O    . ARG   A 1 12  ? -19.368 -3.671  -27.160 1.00 57.49  ? 530  ARG   A O    1 
ATOM   114  C  CB   . ARG   A 1 12  ? -17.593 -1.397  -25.789 1.00 62.40  ? 530  ARG   A CB   1 
ATOM   115  C  CG   . ARG   A 1 12  ? -17.404 0.074   -25.464 1.00 66.00  ? 530  ARG   A CG   1 
ATOM   116  C  CD   . ARG   A 1 12  ? -18.231 0.958   -26.382 1.00 70.00  ? 530  ARG   A CD   1 
ATOM   117  N  NE   . ARG   A 1 12  ? -17.873 0.791   -27.787 1.00 75.41  ? 530  ARG   A NE   1 
ATOM   118  C  CZ   . ARG   A 1 12  ? -18.213 1.645   -28.748 1.00 75.67  ? 530  ARG   A CZ   1 
ATOM   119  N  NH1  . ARG   A 1 12  ? -18.920 2.727   -28.454 1.00 70.08  ? 530  ARG   A NH1  1 
ATOM   120  N  NH2  . ARG   A 1 12  ? -17.847 1.417   -30.002 1.00 80.95  ? 530  ARG   A NH2  1 
ATOM   121  N  N    . ARG   A 1 13  ? -18.876 -4.312  -25.057 1.00 55.53  ? 531  ARG   A N    1 
ATOM   122  C  CA   A ARG   A 1 13  ? -18.909 -5.718  -25.437 0.51 63.90  ? 531  ARG   A CA   1 
ATOM   123  C  CA   B ARG   A 1 13  ? -18.922 -5.735  -25.382 0.49 63.96  ? 531  ARG   A CA   1 
ATOM   124  C  C    . ARG   A 1 13  ? -20.322 -6.181  -25.776 1.00 67.15  ? 531  ARG   A C    1 
ATOM   125  O  O    . ARG   A 1 13  ? -20.481 -7.111  -26.574 1.00 74.85  ? 531  ARG   A O    1 
ATOM   126  C  CB   A ARG   A 1 13  ? -18.294 -6.581  -24.333 0.51 67.51  ? 531  ARG   A CB   1 
ATOM   127  C  CB   B ARG   A 1 13  ? -18.437 -6.562  -24.192 0.49 67.30  ? 531  ARG   A CB   1 
ATOM   128  C  CG   A ARG   A 1 13  ? -19.245 -7.026  -23.241 0.51 69.80  ? 531  ARG   A CG   1 
ATOM   129  C  CG   B ARG   A 1 13  ? -16.938 -6.777  -24.134 0.49 69.78  ? 531  ARG   A CG   1 
ATOM   130  C  CD   A ARG   A 1 13  ? -18.468 -7.392  -21.988 0.51 74.12  ? 531  ARG   A CD   1 
ATOM   131  C  CD   B ARG   A 1 13  ? -16.596 -7.907  -23.177 0.49 71.55  ? 531  ARG   A CD   1 
ATOM   132  N  NE   A ARG   A 1 13  ? -19.041 -8.532  -21.282 0.51 76.57  ? 531  ARG   A NE   1 
ATOM   133  N  NE   B ARG   A 1 13  ? -15.836 -8.967  -23.833 0.49 77.78  ? 531  ARG   A NE   1 
ATOM   134  C  CZ   A ARG   A 1 13  ? -18.639 -8.938  -20.082 0.51 77.99  ? 531  ARG   A CZ   1 
ATOM   135  C  CZ   B ARG   A 1 13  ? -16.244 -10.228 -23.933 0.49 83.53  ? 531  ARG   A CZ   1 
ATOM   136  N  NH1  A ARG   A 1 13  ? -17.664 -8.293  -19.459 0.51 77.55  ? 531  ARG   A NH1  1 
ATOM   137  N  NH1  B ARG   A 1 13  ? -17.411 -10.595 -23.420 0.49 83.89  ? 531  ARG   A NH1  1 
ATOM   138  N  NH2  A ARG   A 1 13  ? -19.210 -9.984  -19.502 0.51 78.56  ? 531  ARG   A NH2  1 
ATOM   139  N  NH2  B ARG   A 1 13  ? -15.483 -11.124 -24.547 0.49 87.12  ? 531  ARG   A NH2  1 
ATOM   140  N  N    . LYS   A 1 14  ? -21.350 -5.545  -25.212 1.00 63.74  ? 532  LYS   A N    1 
ATOM   141  C  CA   . LYS   A 1 14  ? -22.724 -5.897  -25.539 1.00 61.09  ? 532  LYS   A CA   1 
ATOM   142  C  C    . LYS   A 1 14  ? -23.235 -5.186  -26.781 1.00 61.53  ? 532  LYS   A C    1 
ATOM   143  O  O    . LYS   A 1 14  ? -24.146 -5.698  -27.440 1.00 66.76  ? 532  LYS   A O    1 
ATOM   144  C  CB   . LYS   A 1 14  ? -23.651 -5.583  -24.362 1.00 55.72  ? 532  LYS   A CB   1 
ATOM   145  C  CG   . LYS   A 1 14  ? -23.532 -6.558  -23.208 1.00 57.16  ? 532  LYS   A CG   1 
ATOM   146  C  CD   . LYS   A 1 14  ? -24.549 -6.238  -22.132 1.00 60.37  ? 532  LYS   A CD   1 
ATOM   147  C  CE   . LYS   A 1 14  ? -24.753 -7.415  -21.204 1.00 62.49  ? 532  LYS   A CE   1 
ATOM   148  N  NZ   . LYS   A 1 14  ? -25.889 -7.183  -20.269 1.00 60.20  ? 532  LYS   A NZ   1 
ATOM   149  N  N    . LEU   A 1 15  ? -22.675 -4.025  -27.112 1.00 63.28  ? 533  LEU   A N    1 
ATOM   150  C  CA   . LEU   A 1 15  ? -23.034 -3.309  -28.328 1.00 64.46  ? 533  LEU   A CA   1 
ATOM   151  C  C    . LEU   A 1 15  ? -22.539 -4.073  -29.550 1.00 74.26  ? 533  LEU   A C    1 
ATOM   152  O  O    . LEU   A 1 15  ? -21.598 -3.636  -30.221 1.00 77.77  ? 533  LEU   A O    1 
ATOM   153  C  CB   . LEU   A 1 15  ? -22.448 -1.895  -28.296 1.00 61.18  ? 533  LEU   A CB   1 
ATOM   154  C  CG   . LEU   A 1 15  ? -23.164 -0.774  -29.048 1.00 60.01  ? 533  LEU   A CG   1 
ATOM   155  C  CD1  . LEU   A 1 15  ? -24.603 -0.641  -28.580 1.00 57.34  ? 533  LEU   A CD1  1 
ATOM   156  C  CD2  . LEU   A 1 15  ? -22.415 0.538   -28.861 1.00 60.02  ? 533  LEU   A CD2  1 
ATOM   157  N  N    . LYS   A 1 16  ? -23.163 -5.210  -29.847 1.00 79.62  ? 534  LYS   A N    1 
ATOM   158  C  CA   . LYS   A 1 16  ? -22.657 -6.092  -30.886 1.00 81.63  ? 534  LYS   A CA   1 
ATOM   159  C  C    . LYS   A 1 16  ? -22.910 -5.513  -32.276 1.00 86.44  ? 534  LYS   A C    1 
ATOM   160  O  O    . LYS   A 1 16  ? -23.788 -4.670  -32.486 1.00 87.51  ? 534  LYS   A O    1 
ATOM   161  C  CB   . LYS   A 1 16  ? -23.282 -7.481  -30.764 1.00 80.92  ? 534  LYS   A CB   1 
ATOM   162  C  CG   . LYS   A 1 16  ? -23.290 -8.030  -29.349 1.00 81.48  ? 534  LYS   A CG   1 
ATOM   163  C  CD   . LYS   A 1 16  ? -21.987 -8.735  -29.031 1.00 86.22  ? 534  LYS   A CD   1 
ATOM   164  C  CE   . LYS   A 1 16  ? -22.082 -9.526  -27.736 1.00 88.84  ? 534  LYS   A CE   1 
ATOM   165  N  NZ   . LYS   A 1 16  ? -20.781 -10.179 -27.409 1.00 93.71  ? 534  LYS   A NZ   1 
ATOM   166  N  N    . LYS   A 1 17  ? -22.125 -5.997  -33.235 1.00 93.60  ? 535  LYS   A N    1 
ATOM   167  C  CA   . LYS   A 1 17  ? -22.045 -5.400  -34.559 1.00 101.81 ? 535  LYS   A CA   1 
ATOM   168  C  C    . LYS   A 1 17  ? -23.223 -5.813  -35.434 1.00 107.82 ? 535  LYS   A C    1 
ATOM   169  O  O    . LYS   A 1 17  ? -23.772 -6.910  -35.306 1.00 117.15 ? 535  LYS   A O    1 
ATOM   170  C  CB   . LYS   A 1 17  ? -20.733 -5.801  -35.236 1.00 107.18 ? 535  LYS   A CB   1 
ATOM   171  C  CG   . LYS   A 1 17  ? -20.367 -4.983  -36.465 1.00 107.70 ? 535  LYS   A CG   1 
ATOM   172  C  CD   . LYS   A 1 17  ? -18.969 -5.334  -36.955 1.00 109.71 ? 535  LYS   A CD   1 
ATOM   173  C  CE   . LYS   A 1 17  ? -18.839 -5.138  -38.459 1.00 107.56 ? 535  LYS   A CE   1 
ATOM   174  N  NZ   . LYS   A 1 17  ? -18.323 -3.784  -38.807 1.00 101.41 ? 535  LYS   A NZ   1 
ATOM   175  N  N    . GLN   A 1 18  ? -23.602 -4.914  -36.336 1.00 103.57 ? 536  GLN   A N    1 
ATOM   176  C  CA   . GLN   A 1 18  ? -24.630 -5.184  -37.328 1.00 102.10 ? 536  GLN   A CA   1 
ATOM   177  C  C    . GLN   A 1 18  ? -23.989 -5.752  -38.588 1.00 102.19 ? 536  GLN   A C    1 
ATOM   178  O  O    . GLN   A 1 18  ? -22.946 -5.269  -39.038 1.00 101.76 ? 536  GLN   A O    1 
ATOM   179  C  CB   . GLN   A 1 18  ? -25.391 -3.901  -37.660 1.00 100.81 ? 536  GLN   A CB   1 
ATOM   180  C  CG   . GLN   A 1 18  ? -26.307 -3.387  -36.568 1.00 102.34 ? 536  GLN   A CG   1 
ATOM   181  C  CD   . GLN   A 1 18  ? -27.755 -3.761  -36.797 1.00 109.22 ? 536  GLN   A CD   1 
ATOM   182  O  OE1  . GLN   A 1 18  ? -28.207 -3.871  -37.936 1.00 112.97 ? 536  GLN   A OE1  1 
ATOM   183  N  NE2  . GLN   A 1 18  ? -28.497 -3.943  -35.713 1.00 110.57 ? 536  GLN   A NE2  1 
ATOM   184  N  N    . ASN   A 1 19  ? -24.612 -6.788  -39.155 1.00 103.65 ? 537  ASN   A N    1 
ATOM   185  C  CA   . ASN   A 1 19  ? -24.150 -7.360  -40.412 1.00 105.28 ? 537  ASN   A CA   1 
ATOM   186  C  C    . ASN   A 1 19  ? -25.203 -7.361  -41.510 1.00 105.37 ? 537  ASN   A C    1 
ATOM   187  O  O    . ASN   A 1 19  ? -24.879 -7.718  -42.649 1.00 109.65 ? 537  ASN   A O    1 
ATOM   188  C  CB   . ASN   A 1 19  ? -23.636 -8.795  -40.205 1.00 108.12 ? 537  ASN   A CB   1 
ATOM   189  C  CG   . ASN   A 1 19  ? -24.451 -9.571  -39.194 1.00 107.95 ? 537  ASN   A CG   1 
ATOM   190  O  OD1  . ASN   A 1 19  ? -25.555 -9.169  -38.827 1.00 105.73 ? 537  ASN   A OD1  1 
ATOM   191  N  ND2  . ASN   A 1 19  ? -23.910 -10.694 -38.737 1.00 110.23 ? 537  ASN   A ND2  1 
ATOM   192  N  N    . ASP   A 1 20  ? -26.445 -6.981  -41.210 1.00 99.61  ? 538  ASP   A N    1 
ATOM   193  C  CA   . ASP   A 1 20  ? -27.460 -6.747  -42.227 1.00 96.10  ? 538  ASP   A CA   1 
ATOM   194  C  C    . ASP   A 1 20  ? -27.451 -5.307  -42.725 1.00 89.77  ? 538  ASP   A C    1 
ATOM   195  O  O    . ASP   A 1 20  ? -28.465 -4.830  -43.248 1.00 89.08  ? 538  ASP   A O    1 
ATOM   196  C  CB   . ASP   A 1 20  ? -28.845 -7.107  -41.685 1.00 96.63  ? 538  ASP   A CB   1 
ATOM   197  C  CG   . ASP   A 1 20  ? -29.138 -6.442  -40.358 1.00 94.10  ? 538  ASP   A CG   1 
ATOM   198  O  OD1  . ASP   A 1 20  ? -28.200 -5.868  -39.769 1.00 92.28  ? 538  ASP   A OD1  1 
ATOM   199  O  OD2  . ASP   A 1 20  ? -30.302 -6.490  -39.906 1.00 94.28  ? 538  ASP   A OD2  1 
ATOM   200  N  N    . ILE   A 1 21  ? -26.333 -4.613  -42.572 1.00 87.65  ? 539  ILE   A N    1 
ATOM   201  C  CA   . ILE   A 1 21  ? -26.221 -3.200  -42.921 1.00 88.72  ? 539  ILE   A CA   1 
ATOM   202  C  C    . ILE   A 1 21  ? -25.189 -3.080  -44.032 1.00 92.87  ? 539  ILE   A C    1 
ATOM   203  O  O    . ILE   A 1 21  ? -24.304 -3.942  -44.174 1.00 97.76  ? 539  ILE   A O    1 
ATOM   204  C  CB   . ILE   A 1 21  ? -25.836 -2.338  -41.696 1.00 87.71  ? 539  ILE   A CB   1 
ATOM   205  C  CG1  . ILE   A 1 21  ? -24.468 -2.762  -41.154 1.00 93.13  ? 539  ILE   A CG1  1 
ATOM   206  C  CG2  . ILE   A 1 21  ? -26.885 -2.467  -40.603 1.00 86.21  ? 539  ILE   A CG2  1 
ATOM   207  C  CD1  . ILE   A 1 21  ? -23.286 -2.437  -42.039 1.00 97.47  ? 539  ILE   A CD1  1 
ATOM   208  N  N    . PRO   A 1 22  ? -25.273 -2.030  -44.851 1.00 92.18  ? 540  PRO   A N    1 
ATOM   209  C  CA   . PRO   A 1 22  ? -24.133 -1.687  -45.706 1.00 90.89  ? 540  PRO   A CA   1 
ATOM   210  C  C    . PRO   A 1 22  ? -22.946 -1.370  -44.817 1.00 84.51  ? 540  PRO   A C    1 
ATOM   211  O  O    . PRO   A 1 22  ? -23.106 -0.853  -43.712 1.00 78.63  ? 540  PRO   A O    1 
ATOM   212  C  CB   . PRO   A 1 22  ? -24.611 -0.442  -46.463 1.00 89.00  ? 540  PRO   A CB   1 
ATOM   213  C  CG   . PRO   A 1 22  ? -26.101 -0.457  -46.342 1.00 88.89  ? 540  PRO   A CG   1 
ATOM   214  C  CD   . PRO   A 1 22  ? -26.386 -1.078  -45.009 1.00 88.64  ? 540  PRO   A CD   1 
ATOM   215  N  N    . ASN   A 1 23  ? -21.739 -1.686  -45.284 1.00 87.08  ? 541  ASN   A N    1 
ATOM   216  C  CA   . ASN   A 1 23  ? -20.617 -1.546  -44.362 1.00 90.89  ? 541  ASN   A CA   1 
ATOM   217  C  C    . ASN   A 1 23  ? -20.189 -0.089  -44.222 1.00 88.45  ? 541  ASN   A C    1 
ATOM   218  O  O    . ASN   A 1 23  ? -19.655 0.303   -43.180 1.00 94.99  ? 541  ASN   A O    1 
ATOM   219  C  CB   . ASN   A 1 23  ? -19.441 -2.430  -44.770 1.00 99.06  ? 541  ASN   A CB   1 
ATOM   220  C  CG   . ASN   A 1 23  ? -18.363 -2.462  -43.703 1.00 102.18 ? 541  ASN   A CG   1 
ATOM   221  O  OD1  . ASN   A 1 23  ? -17.227 -2.046  -43.921 1.00 106.69 ? 541  ASN   A OD1  1 
ATOM   222  N  ND2  . ASN   A 1 23  ? -18.749 -2.893  -42.505 1.00 98.88  ? 541  ASN   A ND2  1 
ATOM   223  N  N    . LYS   A 1 24  ? -20.427 0.737   -45.238 1.00 81.24  ? 542  LYS   A N    1 
ATOM   224  C  CA   . LYS   A 1 24  ? -20.170 2.169   -45.132 1.00 77.67  ? 542  LYS   A CA   1 
ATOM   225  C  C    . LYS   A 1 24  ? -21.480 2.948   -45.084 1.00 71.39  ? 542  LYS   A C    1 
ATOM   226  O  O    . LYS   A 1 24  ? -22.465 2.585   -45.734 1.00 70.33  ? 542  LYS   A O    1 
ATOM   227  C  CB   . LYS   A 1 24  ? -19.332 2.706   -46.303 1.00 83.53  ? 542  LYS   A CB   1 
ATOM   228  C  CG   . LYS   A 1 24  ? -17.887 2.221   -46.414 1.00 91.02  ? 542  LYS   A CG   1 
ATOM   229  C  CD   . LYS   A 1 24  ? -17.336 1.574   -45.155 1.00 94.13  ? 542  LYS   A CD   1 
ATOM   230  C  CE   . LYS   A 1 24  ? -16.270 0.555   -45.538 1.00 101.39 ? 542  LYS   A CE   1 
ATOM   231  N  NZ   . LYS   A 1 24  ? -15.564 -0.045  -44.374 1.00 102.99 ? 542  LYS   A NZ   1 
ATOM   232  N  N    . PHE   A 1 25  ? -21.478 4.030   -44.303 1.00 66.80  ? 543  PHE   A N    1 
ATOM   233  C  CA   . PHE   A 1 25  ? -22.526 5.046   -44.340 1.00 62.27  ? 543  PHE   A CA   1 
ATOM   234  C  C    . PHE   A 1 25  ? -21.912 6.320   -44.906 1.00 63.92  ? 543  PHE   A C    1 
ATOM   235  O  O    . PHE   A 1 25  ? -21.145 7.005   -44.220 1.00 63.24  ? 543  PHE   A O    1 
ATOM   236  C  CB   . PHE   A 1 25  ? -23.126 5.310   -42.961 1.00 59.45  ? 543  PHE   A CB   1 
ATOM   237  C  CG   . PHE   A 1 25  ? -24.082 6.475   -42.939 1.00 58.41  ? 543  PHE   A CG   1 
ATOM   238  C  CD1  . PHE   A 1 25  ? -25.306 6.391   -43.583 1.00 59.00  ? 543  PHE   A CD1  1 
ATOM   239  C  CD2  . PHE   A 1 25  ? -23.750 7.658   -42.296 1.00 57.61  ? 543  PHE   A CD2  1 
ATOM   240  C  CE1  . PHE   A 1 25  ? -26.188 7.458   -43.576 1.00 58.36  ? 543  PHE   A CE1  1 
ATOM   241  C  CE2  . PHE   A 1 25  ? -24.628 8.731   -42.285 1.00 56.62  ? 543  PHE   A CE2  1 
ATOM   242  C  CZ   . PHE   A 1 25  ? -25.849 8.630   -42.928 1.00 56.49  ? 543  PHE   A CZ   1 
ATOM   243  N  N    . GLU   A 1 26  ? -22.253 6.637   -46.150 1.00 66.43  ? 544  GLU   A N    1 
ATOM   244  C  CA   . GLU   A 1 26  ? -21.698 7.794   -46.835 1.00 67.81  ? 544  GLU   A CA   1 
ATOM   245  C  C    . GLU   A 1 26  ? -22.625 8.991   -46.676 1.00 66.76  ? 544  GLU   A C    1 
ATOM   246  O  O    . GLU   A 1 26  ? -23.835 8.881   -46.904 1.00 69.47  ? 544  GLU   A O    1 
ATOM   247  C  CB   . GLU   A 1 26  ? -21.495 7.486   -48.319 1.00 71.20  ? 544  GLU   A CB   1 
ATOM   248  C  CG   . GLU   A 1 26  ? -20.076 7.113   -48.698 1.00 79.35  ? 544  GLU   A CG   1 
ATOM   249  C  CD   . GLU   A 1 26  ? -19.949 6.761   -50.167 1.00 89.14  ? 544  GLU   A CD   1 
ATOM   250  O  OE1  . GLU   A 1 26  ? -20.019 5.559   -50.500 1.00 93.06  ? 544  GLU   A OE1  1 
ATOM   251  O  OE2  . GLU   A 1 26  ? -19.783 7.687   -50.989 1.00 92.15  ? 544  GLU   A OE2  1 
ATOM   252  N  N    . MET   A 1 27  ? -22.060 10.131  -46.286 1.00 64.28  ? 545  MET   A N    1 
ATOM   253  C  CA   . MET   A 1 27  ? -22.794 11.387  -46.333 1.00 68.04  ? 545  MET   A CA   1 
ATOM   254  C  C    . MET   A 1 27  ? -21.853 12.497  -46.773 1.00 69.46  ? 545  MET   A C    1 
ATOM   255  O  O    . MET   A 1 27  ? -20.741 12.624  -46.251 1.00 73.55  ? 545  MET   A O    1 
ATOM   256  C  CB   . MET   A 1 27  ? -23.451 11.727  -44.985 1.00 68.32  ? 545  MET   A CB   1 
ATOM   257  C  CG   . MET   A 1 27  ? -22.542 11.710  -43.773 1.00 71.11  ? 545  MET   A CG   1 
ATOM   258  S  SD   . MET   A 1 27  ? -23.432 12.156  -42.261 1.00 68.40  ? 545  MET   A SD   1 
ATOM   259  C  CE   . MET   A 1 27  ? -24.783 13.133  -42.916 1.00 51.21  ? 545  MET   A CE   1 
ATOM   260  N  N    . LYS   A 1 28  ? -22.302 13.278  -47.749 1.00 67.15  ? 546  LYS   A N    1 
ATOM   261  C  CA   . LYS   A 1 28  ? -21.544 14.389  -48.309 1.00 69.85  ? 546  LYS   A CA   1 
ATOM   262  C  C    . LYS   A 1 28  ? -22.207 15.676  -47.858 1.00 69.08  ? 546  LYS   A C    1 
ATOM   263  O  O    . LYS   A 1 28  ? -23.419 15.849  -48.023 1.00 70.74  ? 546  LYS   A O    1 
ATOM   264  C  CB   . LYS   A 1 28  ? -21.472 14.356  -49.845 1.00 76.75  ? 546  LYS   A CB   1 
ATOM   265  C  CG   . LYS   A 1 28  ? -21.065 13.036  -50.514 1.00 89.24  ? 546  LYS   A CG   1 
ATOM   266  C  CD   . LYS   A 1 28  ? -22.089 11.968  -50.258 1.00 100.52 ? 546  LYS   A CD   1 
ATOM   267  C  CE   . LYS   A 1 28  ? -22.243 10.961  -51.340 1.00 118.44 ? 546  LYS   A CE   1 
ATOM   268  N  NZ   . LYS   A 1 28  ? -23.517 10.297  -51.009 1.00 126.89 ? 546  LYS   A NZ   1 
ATOM   269  N  N    . LEU   A 1 29  ? -21.416 16.566  -47.283 1.00 65.19  ? 547  LEU   A N    1 
ATOM   270  C  CA   . LEU   A 1 29  ? -21.946 17.767  -46.668 1.00 61.57  ? 547  LEU   A CA   1 
ATOM   271  C  C    . LEU   A 1 29  ? -21.185 18.983  -47.167 1.00 63.65  ? 547  LEU   A C    1 
ATOM   272  O  O    . LEU   A 1 29  ? -20.022 18.892  -47.571 1.00 69.22  ? 547  LEU   A O    1 
ATOM   273  C  CB   . LEU   A 1 29  ? -21.865 17.685  -45.139 1.00 60.59  ? 547  LEU   A CB   1 
ATOM   274  C  CG   . LEU   A 1 29  ? -22.297 16.351  -44.528 1.00 58.60  ? 547  LEU   A CG   1 
ATOM   275  C  CD1  . LEU   A 1 29  ? -21.779 16.218  -43.113 1.00 57.45  ? 547  LEU   A CD1  1 
ATOM   276  C  CD2  . LEU   A 1 29  ? -23.808 16.207  -44.562 1.00 54.61  ? 547  LEU   A CD2  1 
ATOM   277  N  N    . ARG   A 1 30  ? -21.867 20.120  -47.147 1.00 63.00  ? 548  ARG   A N    1 
ATOM   278  C  CA   . ARG   A 1 30  ? -21.257 21.415  -47.396 1.00 63.39  ? 548  ARG   A CA   1 
ATOM   279  C  C    . ARG   A 1 30  ? -21.175 22.161  -46.074 1.00 57.70  ? 548  ARG   A C    1 
ATOM   280  O  O    . ARG   A 1 30  ? -22.154 22.200  -45.319 1.00 50.93  ? 548  ARG   A O    1 
ATOM   281  C  CB   . ARG   A 1 30  ? -22.057 22.212  -48.429 1.00 66.13  ? 548  ARG   A CB   1 
ATOM   282  C  CG   . ARG   A 1 30  ? -22.224 21.493  -49.759 1.00 69.54  ? 548  ARG   A CG   1 
ATOM   283  C  CD   . ARG   A 1 30  ? -23.384 22.059  -50.563 1.00 73.14  ? 548  ARG   A CD   1 
ATOM   284  N  NE   . ARG   A 1 30  ? -24.677 21.771  -49.949 1.00 71.35  ? 548  ARG   A NE   1 
ATOM   285  C  CZ   . ARG   A 1 30  ? -25.840 22.214  -50.416 1.00 68.61  ? 548  ARG   A CZ   1 
ATOM   286  N  NH1  . ARG   A 1 30  ? -25.875 22.964  -51.509 1.00 71.07  ? 548  ARG   A NH1  1 
ATOM   287  N  NH2  . ARG   A 1 30  ? -26.970 21.905  -49.794 1.00 61.40  ? 548  ARG   A NH2  1 
ATOM   288  N  N    . ARG   A 1 31  ? -20.003 22.733  -45.788 1.00 62.07  ? 549  ARG   A N    1 
ATOM   289  C  CA   . ARG   A 1 31  ? -19.785 23.373  -44.493 1.00 61.41  ? 549  ARG   A CA   1 
ATOM   290  C  C    . ARG   A 1 31  ? -20.799 24.480  -44.238 1.00 54.84  ? 549  ARG   A C    1 
ATOM   291  O  O    . ARG   A 1 31  ? -21.296 24.630  -43.115 1.00 51.46  ? 549  ARG   A O    1 
ATOM   292  C  CB   . ARG   A 1 31  ? -18.363 23.924  -44.413 1.00 68.30  ? 549  ARG   A CB   1 
ATOM   293  C  CG   . ARG   A 1 31  ? -17.323 22.894  -44.021 1.00 69.16  ? 549  ARG   A CG   1 
ATOM   294  C  CD   . ARG   A 1 31  ? -15.948 23.525  -43.935 1.00 73.54  ? 549  ARG   A CD   1 
ATOM   295  N  NE   . ARG   A 1 31  ? -14.937 22.562  -43.517 1.00 77.19  ? 549  ARG   A NE   1 
ATOM   296  C  CZ   . ARG   A 1 31  ? -14.176 21.872  -44.359 1.00 84.80  ? 549  ARG   A CZ   1 
ATOM   297  N  NH1  . ARG   A 1 31  ? -14.312 22.042  -45.667 1.00 86.03  ? 549  ARG   A NH1  1 
ATOM   298  N  NH2  . ARG   A 1 31  ? -13.278 21.014  -43.896 1.00 89.68  ? 549  ARG   A NH2  1 
ATOM   299  N  N    . ALA   A 1 32  ? -21.127 25.259  -45.270 1.00 55.98  ? 550  ALA   A N    1 
ATOM   300  C  CA   . ALA   A 1 32  ? -22.086 26.344  -45.108 1.00 58.96  ? 550  ALA   A CA   1 
ATOM   301  C  C    . ALA   A 1 32  ? -23.480 25.841  -44.753 1.00 58.70  ? 550  ALA   A C    1 
ATOM   302  O  O    . ALA   A 1 32  ? -24.264 26.593  -44.164 1.00 58.92  ? 550  ALA   A O    1 
ATOM   303  C  CB   . ALA   A 1 32  ? -22.145 27.186  -46.384 1.00 59.35  ? 550  ALA   A CB   1 
ATOM   304  N  N    . THR   A 1 33  ? -23.807 24.596  -45.089 1.00 60.57  ? 551  THR   A N    1 
ATOM   305  C  CA   . THR   A 1 33  ? -25.126 24.028  -44.829 1.00 59.18  ? 551  THR   A CA   1 
ATOM   306  C  C    . THR   A 1 33  ? -25.009 22.675  -44.143 1.00 56.26  ? 551  THR   A C    1 
ATOM   307  O  O    . THR   A 1 33  ? -25.705 21.719  -44.494 1.00 50.12  ? 551  THR   A O    1 
ATOM   308  C  CB   . THR   A 1 33  ? -25.932 23.894  -46.121 1.00 60.74  ? 551  THR   A CB   1 
ATOM   309  O  OG1  . THR   A 1 33  ? -25.207 23.085  -47.057 1.00 62.13  ? 551  THR   A OG1  1 
ATOM   310  C  CG2  . THR   A 1 33  ? -26.198 25.261  -46.736 1.00 62.17  ? 551  THR   A CG2  1 
ATOM   311  N  N    . VAL   A 1 34  ? -24.136 22.575  -43.137 1.00 56.78  ? 552  VAL   A N    1 
ATOM   312  C  CA   . VAL   A 1 34  ? -23.863 21.272  -42.538 1.00 54.03  ? 552  VAL   A CA   1 
ATOM   313  C  C    . VAL   A 1 34  ? -25.072 20.744  -41.772 1.00 46.12  ? 552  VAL   A C    1 
ATOM   314  O  O    . VAL   A 1 34  ? -25.262 19.527  -41.672 1.00 47.02  ? 552  VAL   A O    1 
ATOM   315  C  CB   . VAL   A 1 34  ? -22.611 21.341  -41.642 1.00 54.15  ? 552  VAL   A CB   1 
ATOM   316  C  CG1  . VAL   A 1 34  ? -22.843 22.260  -40.452 1.00 50.42  ? 552  VAL   A CG1  1 
ATOM   317  C  CG2  . VAL   A 1 34  ? -22.207 19.942  -41.178 1.00 51.10  ? 552  VAL   A CG2  1 
ATOM   318  N  N    . LEU   A 1 35  ? -25.920 21.623  -41.235 1.00 42.74  ? 553  LEU   A N    1 
ATOM   319  C  CA   . LEU   A 1 35  ? -27.031 21.126  -40.430 1.00 43.36  ? 553  LEU   A CA   1 
ATOM   320  C  C    . LEU   A 1 35  ? -28.146 20.575  -41.311 1.00 44.88  ? 553  LEU   A C    1 
ATOM   321  O  O    . LEU   A 1 35  ? -28.650 19.473  -41.068 1.00 40.76  ? 553  LEU   A O    1 
ATOM   322  C  CB   . LEU   A 1 35  ? -27.557 22.214  -39.496 1.00 47.19  ? 553  LEU   A CB   1 
ATOM   323  C  CG   . LEU   A 1 35  ? -28.816 21.832  -38.716 1.00 51.61  ? 553  LEU   A CG   1 
ATOM   324  C  CD1  . LEU   A 1 35  ? -28.561 20.613  -37.840 1.00 52.59  ? 553  LEU   A CD1  1 
ATOM   325  C  CD2  . LEU   A 1 35  ? -29.229 23.003  -37.863 1.00 52.82  ? 553  LEU   A CD2  1 
ATOM   326  N  N    . GLU   A 1 36  ? -28.543 21.318  -42.347 1.00 49.91  ? 554  GLU   A N    1 
ATOM   327  C  CA   . GLU   A 1 36  ? -29.584 20.812  -43.239 1.00 53.04  ? 554  GLU   A CA   1 
ATOM   328  C  C    . GLU   A 1 36  ? -29.114 19.565  -43.978 1.00 50.48  ? 554  GLU   A C    1 
ATOM   329  O  O    . GLU   A 1 36  ? -29.859 18.585  -44.102 1.00 50.83  ? 554  GLU   A O    1 
ATOM   330  C  CB   . GLU   A 1 36  ? -30.025 21.885  -44.234 1.00 63.14  ? 554  GLU   A CB   1 
ATOM   331  C  CG   . GLU   A 1 36  ? -31.113 21.379  -45.178 1.00 77.41  ? 554  GLU   A CG   1 
ATOM   332  C  CD   . GLU   A 1 36  ? -32.262 22.351  -45.376 1.00 94.09  ? 554  GLU   A CD   1 
ATOM   333  O  OE1  . GLU   A 1 36  ? -32.059 23.389  -46.037 1.00 101.60 ? 554  GLU   A OE1  1 
ATOM   334  O  OE2  . GLU   A 1 36  ? -33.372 22.073  -44.871 1.00 98.71  ? 554  GLU   A OE2  1 
ATOM   335  N  N    . ASP   A 1 37  ? -27.874 19.582  -44.478 1.00 49.69  ? 555  ASP   A N    1 
ATOM   336  C  CA   . ASP   A 1 37  ? -27.357 18.422  -45.198 1.00 51.89  ? 555  ASP   A CA   1 
ATOM   337  C  C    . ASP   A 1 37  ? -27.305 17.190  -44.301 1.00 50.06  ? 555  ASP   A C    1 
ATOM   338  O  O    . ASP   A 1 37  ? -27.642 16.083  -44.737 1.00 52.56  ? 555  ASP   A O    1 
ATOM   339  C  CB   . ASP   A 1 37  ? -25.973 18.725  -45.771 1.00 53.81  ? 555  ASP   A CB   1 
ATOM   340  C  CG   . ASP   A 1 37  ? -25.995 19.843  -46.792 1.00 61.23  ? 555  ASP   A CG   1 
ATOM   341  O  OD1  . ASP   A 1 37  ? -27.094 20.353  -47.093 1.00 62.04  ? 555  ASP   A OD1  1 
ATOM   342  O  OD2  . ASP   A 1 37  ? -24.911 20.208  -47.297 1.00 64.15  ? 555  ASP   A OD2  1 
ATOM   343  N  N    . SER   A 1 38  ? -26.889 17.361  -43.044 1.00 47.87  ? 556  SER   A N    1 
ATOM   344  C  CA   . SER   A 1 38  ? -26.847 16.225  -42.127 1.00 48.00  ? 556  SER   A CA   1 
ATOM   345  C  C    . SER   A 1 38  ? -28.251 15.774  -41.750 1.00 42.15  ? 556  SER   A C    1 
ATOM   346  O  O    . SER   A 1 38  ? -28.527 14.570  -41.683 1.00 41.69  ? 556  SER   A O    1 
ATOM   347  C  CB   . SER   A 1 38  ? -26.050 16.585  -40.875 1.00 47.43  ? 556  SER   A CB   1 
ATOM   348  O  OG   . SER   A 1 38  ? -24.808 17.175  -41.214 1.00 51.49  ? 556  SER   A OG   1 
ATOM   349  N  N    . TYR   A 1 39  ? -29.150 16.728  -41.502 1.00 42.40  ? 557  TYR   A N    1 
ATOM   350  C  CA   . TYR   A 1 39  ? -30.518 16.389  -41.127 1.00 41.87  ? 557  TYR   A CA   1 
ATOM   351  C  C    . TYR   A 1 39  ? -31.223 15.616  -42.235 1.00 42.95  ? 557  TYR   A C    1 
ATOM   352  O  O    . TYR   A 1 39  ? -31.899 14.615  -41.970 1.00 42.58  ? 557  TYR   A O    1 
ATOM   353  C  CB   . TYR   A 1 39  ? -31.287 17.665  -40.782 1.00 38.84  ? 557  TYR   A CB   1 
ATOM   354  C  CG   . TYR   A 1 39  ? -32.771 17.470  -40.573 1.00 41.60  ? 557  TYR   A CG   1 
ATOM   355  C  CD1  . TYR   A 1 39  ? -33.260 16.905  -39.403 1.00 40.07  ? 557  TYR   A CD1  1 
ATOM   356  C  CD2  . TYR   A 1 39  ? -33.684 17.867  -41.540 1.00 42.90  ? 557  TYR   A CD2  1 
ATOM   357  C  CE1  . TYR   A 1 39  ? -34.617 16.733  -39.206 1.00 41.89  ? 557  TYR   A CE1  1 
ATOM   358  C  CE2  . TYR   A 1 39  ? -35.043 17.698  -41.353 1.00 44.08  ? 557  TYR   A CE2  1 
ATOM   359  C  CZ   . TYR   A 1 39  ? -35.504 17.130  -40.184 1.00 44.11  ? 557  TYR   A CZ   1 
ATOM   360  O  OH   . TYR   A 1 39  ? -36.856 16.960  -39.993 1.00 49.56  ? 557  TYR   A OH   1 
ATOM   361  N  N    . ARG   A 1 40  ? -31.068 16.059  -43.485 1.00 46.26  ? 558  ARG   A N    1 
ATOM   362  C  CA   A ARG   A 1 40  ? -31.727 15.401  -44.611 0.46 47.00  ? 558  ARG   A CA   1 
ATOM   363  C  CA   B ARG   A 1 40  ? -31.757 15.382  -44.578 0.54 46.83  ? 558  ARG   A CA   1 
ATOM   364  C  C    . ARG   A 1 40  ? -31.205 13.984  -44.816 1.00 48.77  ? 558  ARG   A C    1 
ATOM   365  O  O    . ARG   A 1 40  ? -31.958 13.082  -45.201 1.00 52.09  ? 558  ARG   A O    1 
ATOM   366  C  CB   A ARG   A 1 40  ? -31.522 16.224  -45.884 0.46 49.34  ? 558  ARG   A CB   1 
ATOM   367  C  CB   B ARG   A 1 40  ? -31.671 16.214  -45.855 0.54 49.27  ? 558  ARG   A CB   1 
ATOM   368  C  CG   A ARG   A 1 40  ? -32.789 16.818  -46.471 0.46 52.78  ? 558  ARG   A CG   1 
ATOM   369  C  CG   B ARG   A 1 40  ? -32.730 17.296  -45.944 0.54 51.71  ? 558  ARG   A CG   1 
ATOM   370  C  CD   A ARG   A 1 40  ? -33.254 18.031  -45.685 0.46 52.17  ? 558  ARG   A CD   1 
ATOM   371  C  CD   B ARG   A 1 40  ? -32.237 18.473  -46.756 0.54 53.88  ? 558  ARG   A CD   1 
ATOM   372  N  NE   A ARG   A 1 40  ? -34.686 17.975  -45.413 0.46 49.96  ? 558  ARG   A NE   1 
ATOM   373  N  NE   B ARG   A 1 40  ? -33.338 19.265  -47.295 0.54 58.01  ? 558  ARG   A NE   1 
ATOM   374  C  CZ   A ARG   A 1 40  ? -35.399 18.991  -44.941 0.46 49.48  ? 558  ARG   A CZ   1 
ATOM   375  C  CZ   B ARG   A 1 40  ? -33.186 20.251  -48.172 0.54 62.80  ? 558  ARG   A CZ   1 
ATOM   376  N  NH1  A ARG   A 1 40  ? -34.816 20.153  -44.683 0.46 48.91  ? 558  ARG   A NH1  1 
ATOM   377  N  NH1  B ARG   A 1 40  ? -31.975 20.570  -48.608 0.54 65.17  ? 558  ARG   A NH1  1 
ATOM   378  N  NH2  A ARG   A 1 40  ? -36.699 18.844  -44.725 0.46 49.09  ? 558  ARG   A NH2  1 
ATOM   379  N  NH2  B ARG   A 1 40  ? -34.242 20.920  -48.611 0.54 63.63  ? 558  ARG   A NH2  1 
ATOM   380  N  N    . ARG   A 1 41  ? -29.910 13.775  -44.584 1.00 47.25  ? 559  ARG   A N    1 
ATOM   381  C  CA   . ARG   A 1 41  ? -29.323 12.458  -44.798 1.00 48.68  ? 559  ARG   A CA   1 
ATOM   382  C  C    . ARG   A 1 41  ? -29.669 11.500  -43.664 1.00 50.15  ? 559  ARG   A C    1 
ATOM   383  O  O    . ARG   A 1 41  ? -30.100 10.368  -43.907 1.00 54.52  ? 559  ARG   A O    1 
ATOM   384  C  CB   . ARG   A 1 41  ? -27.806 12.582  -44.947 1.00 51.80  ? 559  ARG   A CB   1 
ATOM   385  C  CG   . ARG   A 1 41  ? -27.096 11.258  -45.152 1.00 52.53  ? 559  ARG   A CG   1 
ATOM   386  C  CD   . ARG   A 1 41  ? -27.304 10.741  -46.563 1.00 57.67  ? 559  ARG   A CD   1 
ATOM   387  N  NE   . ARG   A 1 41  ? -26.561 9.508   -46.801 1.00 61.72  ? 559  ARG   A NE   1 
ATOM   388  C  CZ   . ARG   A 1 41  ? -27.115 8.302   -46.869 1.00 64.76  ? 559  ARG   A CZ   1 
ATOM   389  N  NH1  . ARG   A 1 41  ? -28.425 8.162   -46.721 1.00 63.01  ? 559  ARG   A NH1  1 
ATOM   390  N  NH2  . ARG   A 1 41  ? -26.358 7.236   -47.088 1.00 67.70  ? 559  ARG   A NH2  1 
ATOM   391  N  N    . ILE   A 1 42  ? -29.489 11.942  -42.418 1.00 50.49  ? 560  ILE   A N    1 
ATOM   392  C  CA   . ILE   A 1 42  ? -29.649 11.044  -41.279 1.00 48.06  ? 560  ILE   A CA   1 
ATOM   393  C  C    . ILE   A 1 42  ? -31.120 10.721  -41.046 1.00 45.20  ? 560  ILE   A C    1 
ATOM   394  O  O    . ILE   A 1 42  ? -31.471 9.591   -40.688 1.00 45.72  ? 560  ILE   A O    1 
ATOM   395  C  CB   . ILE   A 1 42  ? -28.982 11.658  -40.034 1.00 46.28  ? 560  ILE   A CB   1 
ATOM   396  C  CG1  . ILE   A 1 42  ? -27.460 11.606  -40.188 1.00 45.51  ? 560  ILE   A CG1  1 
ATOM   397  C  CG2  . ILE   A 1 42  ? -29.416 10.939  -38.765 1.00 41.48  ? 560  ILE   A CG2  1 
ATOM   398  C  CD1  . ILE   A 1 42  ? -26.719 12.530  -39.261 1.00 38.06  ? 560  ILE   A CD1  1 
ATOM   399  N  N    . MET   A 1 43  ? -32.005 11.691  -41.255 1.00 42.51  ? 561  MET   A N    1 
ATOM   400  C  CA   . MET   A 1 43  ? -33.431 11.425  -41.126 1.00 48.07  ? 561  MET   A CA   1 
ATOM   401  C  C    . MET   A 1 43  ? -34.021 10.757  -42.360 1.00 50.44  ? 561  MET   A C    1 
ATOM   402  O  O    . MET   A 1 43  ? -35.213 10.430  -42.356 1.00 54.09  ? 561  MET   A O    1 
ATOM   403  C  CB   . MET   A 1 43  ? -34.187 12.721  -40.829 1.00 49.47  ? 561  MET   A CB   1 
ATOM   404  C  CG   . MET   A 1 43  ? -33.786 13.362  -39.516 1.00 53.01  ? 561  MET   A CG   1 
ATOM   405  S  SD   . MET   A 1 43  ? -34.006 12.245  -38.119 1.00 51.73  ? 561  MET   A SD   1 
ATOM   406  C  CE   . MET   A 1 43  ? -35.783 12.318  -37.911 1.00 52.09  ? 561  MET   A CE   1 
ATOM   407  N  N    . GLY   A 1 44  ? -33.224 10.536  -43.401 1.00 50.65  ? 562  GLY   A N    1 
ATOM   408  C  CA   . GLY   A 1 44  ? -33.741 9.981   -44.634 1.00 46.22  ? 562  GLY   A CA   1 
ATOM   409  C  C    . GLY   A 1 44  ? -33.455 8.510   -44.838 1.00 46.95  ? 562  GLY   A C    1 
ATOM   410  O  O    . GLY   A 1 44  ? -34.100 7.865   -45.670 1.00 48.65  ? 562  GLY   A O    1 
ATOM   411  N  N    . VAL   A 1 45  ? -32.505 7.961   -44.073 1.00 46.40  ? 563  VAL   A N    1 
ATOM   412  C  CA   . VAL   A 1 45  ? -32.076 6.588   -44.310 1.00 52.21  ? 563  VAL   A CA   1 
ATOM   413  C  C    . VAL   A 1 45  ? -33.221 5.598   -44.109 1.00 55.82  ? 563  VAL   A C    1 
ATOM   414  O  O    . VAL   A 1 45  ? -34.225 5.855   -43.433 1.00 54.81  ? 563  VAL   A O    1 
ATOM   415  C  CB   . VAL   A 1 45  ? -30.878 6.204   -43.427 1.00 54.73  ? 563  VAL   A CB   1 
ATOM   416  C  CG1  . VAL   A 1 45  ? -29.659 7.034   -43.793 1.00 58.11  ? 563  VAL   A CG1  1 
ATOM   417  C  CG2  . VAL   A 1 45  ? -31.228 6.351   -41.962 1.00 51.36  ? 563  VAL   A CG2  1 
ATOM   418  N  N    . LYS   A 1 46  ? -33.042 4.444   -44.727 1.00 60.97  ? 564  LYS   A N    1 
ATOM   419  C  CA   . LYS   A 1 46  ? -33.991 3.354   -44.638 1.00 66.46  ? 564  LYS   A CA   1 
ATOM   420  C  C    . LYS   A 1 46  ? -34.229 2.879   -43.218 1.00 68.77  ? 564  LYS   A C    1 
ATOM   421  O  O    . LYS   A 1 46  ? -35.370 2.854   -42.737 1.00 70.28  ? 564  LYS   A O    1 
ATOM   422  C  CB   . LYS   A 1 46  ? -33.496 2.257   -45.545 1.00 75.13  ? 564  LYS   A CB   1 
ATOM   423  C  CG   . LYS   A 1 46  ? -34.628 1.986   -46.420 1.00 87.34  ? 564  LYS   A CG   1 
ATOM   424  C  CD   . LYS   A 1 46  ? -35.324 3.169   -46.903 1.00 98.58  ? 564  LYS   A CD   1 
ATOM   425  C  CE   . LYS   A 1 46  ? -36.616 2.589   -47.262 1.00 108.78 ? 564  LYS   A CE   1 
ATOM   426  N  NZ   . LYS   A 1 46  ? -37.395 3.778   -47.586 1.00 106.61 ? 564  LYS   A NZ   1 
ATOM   427  N  N    . ARG   A 1 47  ? -33.166 2.530   -42.538 1.00 67.24  ? 565  ARG   A N    1 
ATOM   428  C  CA   . ARG   A 1 47  ? -33.181 1.998   -41.198 1.00 65.45  ? 565  ARG   A CA   1 
ATOM   429  C  C    . ARG   A 1 47  ? -32.157 2.812   -40.444 1.00 55.52  ? 565  ARG   A C    1 
ATOM   430  O  O    . ARG   A 1 47  ? -31.112 3.168   -40.999 1.00 49.50  ? 565  ARG   A O    1 
ATOM   431  C  CB   . ARG   A 1 47  ? -32.825 0.520   -41.213 1.00 67.67  ? 565  ARG   A CB   1 
ATOM   432  C  CG   . ARG   A 1 47  ? -33.772 -0.315  -42.045 1.00 71.12  ? 565  ARG   A CG   1 
ATOM   433  C  CD   . ARG   A 1 47  ? -33.713 -1.763  -41.612 1.00 78.42  ? 565  ARG   A CD   1 
ATOM   434  N  NE   . ARG   A 1 47  ? -32.623 -2.479  -42.268 1.00 84.08  ? 565  ARG   A NE   1 
ATOM   435  C  CZ   . ARG   A 1 47  ? -31.597 -3.034  -41.630 1.00 85.29  ? 565  ARG   A CZ   1 
ATOM   436  N  NH1  . ARG   A 1 47  ? -31.514 -2.958  -40.309 1.00 80.60  ? 565  ARG   A NH1  1 
ATOM   437  N  NH2  . ARG   A 1 47  ? -30.654 -3.667  -42.315 1.00 90.02  ? 565  ARG   A NH2  1 
ATOM   438  N  N    . ALA   A 1 48  ? -32.493 3.158   -39.208 1.00 51.35  ? 566  ALA   A N    1 
ATOM   439  C  CA   . ALA   A 1 48  ? -31.526 3.813   -38.347 1.00 49.10  ? 566  ALA   A CA   1 
ATOM   440  C  C    . ALA   A 1 48  ? -30.243 2.999   -38.239 1.00 50.42  ? 566  ALA   A C    1 
ATOM   441  O  O    . ALA   A 1 48  ? -29.171 3.558   -37.983 1.00 52.63  ? 566  ALA   A O    1 
ATOM   442  C  CB   . ALA   A 1 48  ? -32.145 4.040   -36.970 1.00 46.56  ? 566  ALA   A CB   1 
ATOM   443  N  N    . ASP   A 1 49  ? -30.331 1.681   -38.448 1.00 54.08  ? 567  ASP   A N    1 
ATOM   444  C  CA   . ASP   A 1 49  ? -29.159 0.816   -38.375 1.00 60.35  ? 567  ASP   A CA   1 
ATOM   445  C  C    . ASP   A 1 49  ? -28.102 1.172   -39.412 1.00 60.63  ? 567  ASP   A C    1 
ATOM   446  O  O    . ASP   A 1 49  ? -26.927 0.841   -39.218 1.00 58.13  ? 567  ASP   A O    1 
ATOM   447  C  CB   . ASP   A 1 49  ? -29.570 -0.648  -38.548 1.00 67.85  ? 567  ASP   A CB   1 
ATOM   448  C  CG   . ASP   A 1 49  ? -30.492 -1.129  -37.446 1.00 71.75  ? 567  ASP   A CG   1 
ATOM   449  O  OD1  . ASP   A 1 49  ? -30.291 -0.724  -36.282 1.00 70.77  ? 567  ASP   A OD1  1 
ATOM   450  O  OD2  . ASP   A 1 49  ? -31.417 -1.915  -37.744 1.00 74.01  ? 567  ASP   A OD2  1 
ATOM   451  N  N    . PHE   A 1 50  ? -28.489 1.827   -40.511 1.00 59.77  ? 568  PHE   A N    1 
ATOM   452  C  CA   . PHE   A 1 50  ? -27.504 2.266   -41.495 1.00 57.97  ? 568  PHE   A CA   1 
ATOM   453  C  C    . PHE   A 1 50  ? -26.482 3.209   -40.872 1.00 51.37  ? 568  PHE   A C    1 
ATOM   454  O  O    . PHE   A 1 50  ? -25.336 3.280   -41.333 1.00 50.30  ? 568  PHE   A O    1 
ATOM   455  C  CB   . PHE   A 1 50  ? -28.196 2.955   -42.675 1.00 58.13  ? 568  PHE   A CB   1 
ATOM   456  C  CG   . PHE   A 1 50  ? -28.907 2.012   -43.612 1.00 60.30  ? 568  PHE   A CG   1 
ATOM   457  C  CD1  . PHE   A 1 50  ? -29.015 0.660   -43.325 1.00 62.88  ? 568  PHE   A CD1  1 
ATOM   458  C  CD2  . PHE   A 1 50  ? -29.471 2.487   -44.786 1.00 57.94  ? 568  PHE   A CD2  1 
ATOM   459  C  CE1  . PHE   A 1 50  ? -29.671 -0.197  -44.190 1.00 66.36  ? 568  PHE   A CE1  1 
ATOM   460  C  CE2  . PHE   A 1 50  ? -30.123 1.634   -45.656 1.00 60.41  ? 568  PHE   A CE2  1 
ATOM   461  C  CZ   . PHE   A 1 50  ? -30.226 0.292   -45.356 1.00 65.16  ? 568  PHE   A CZ   1 
ATOM   462  N  N    . LEU   A 1 51  ? -26.876 3.934   -39.823 1.00 46.07  ? 569  LEU   A N    1 
ATOM   463  C  CA   . LEU   A 1 51  ? -25.991 4.881   -39.158 1.00 45.96  ? 569  LEU   A CA   1 
ATOM   464  C  C    . LEU   A 1 51  ? -24.922 4.201   -38.313 1.00 46.18  ? 569  LEU   A C    1 
ATOM   465  O  O    . LEU   A 1 51  ? -24.019 4.886   -37.820 1.00 47.40  ? 569  LEU   A O    1 
ATOM   466  C  CB   . LEU   A 1 51  ? -26.820 5.831   -38.292 1.00 43.58  ? 569  LEU   A CB   1 
ATOM   467  C  CG   . LEU   A 1 51  ? -28.027 6.429   -39.016 1.00 43.88  ? 569  LEU   A CG   1 
ATOM   468  C  CD1  . LEU   A 1 51  ? -28.943 7.171   -38.053 1.00 43.48  ? 569  LEU   A CD1  1 
ATOM   469  C  CD2  . LEU   A 1 51  ? -27.560 7.345   -40.135 1.00 42.47  ? 569  LEU   A CD2  1 
ATOM   470  N  N    . LYS   A 1 52  ? -25.001 2.883   -38.133 1.00 47.04  ? 570  LYS   A N    1 
ATOM   471  C  CA   . LYS   A 1 52  ? -23.985 2.136   -37.404 1.00 55.63  ? 570  LYS   A CA   1 
ATOM   472  C  C    . LYS   A 1 52  ? -22.801 1.743   -38.277 1.00 63.06  ? 570  LYS   A C    1 
ATOM   473  O  O    . LYS   A 1 52  ? -21.773 1.312   -37.743 1.00 66.78  ? 570  LYS   A O    1 
ATOM   474  C  CB   . LYS   A 1 52  ? -24.602 0.879   -36.788 1.00 60.00  ? 570  LYS   A CB   1 
ATOM   475  C  CG   . LYS   A 1 52  ? -25.776 1.156   -35.866 1.00 61.28  ? 570  LYS   A CG   1 
ATOM   476  C  CD   . LYS   A 1 52  ? -26.130 -0.077  -35.054 1.00 67.54  ? 570  LYS   A CD   1 
ATOM   477  C  CE   . LYS   A 1 52  ? -27.205 0.225   -34.027 1.00 69.09  ? 570  LYS   A CE   1 
ATOM   478  N  NZ   . LYS   A 1 52  ? -28.563 -0.091  -34.544 1.00 70.59  ? 570  LYS   A NZ   1 
ATOM   479  N  N    . ALA   A 1 53  ? -22.926 1.870   -39.595 1.00 62.16  ? 571  ALA   A N    1 
ATOM   480  C  CA   . ALA   A 1 53  ? -21.824 1.580   -40.494 1.00 64.57  ? 571  ALA   A CA   1 
ATOM   481  C  C    . ALA   A 1 53  ? -20.705 2.601   -40.303 1.00 62.95  ? 571  ALA   A C    1 
ATOM   482  O  O    . ALA   A 1 53  ? -20.884 3.655   -39.688 1.00 60.23  ? 571  ALA   A O    1 
ATOM   483  C  CB   . ALA   A 1 53  ? -22.305 1.583   -41.943 1.00 65.99  ? 571  ALA   A CB   1 
ATOM   484  N  N    . ARG   A 1 54  ? -19.532 2.277   -40.842 1.00 64.90  ? 572  ARG   A N    1 
ATOM   485  C  CA   . ARG   A 1 54  ? -18.394 3.179   -40.726 1.00 68.30  ? 572  ARG   A CA   1 
ATOM   486  C  C    . ARG   A 1 54  ? -18.681 4.484   -41.459 1.00 62.96  ? 572  ARG   A C    1 
ATOM   487  O  O    . ARG   A 1 54  ? -19.071 4.483   -42.631 1.00 62.92  ? 572  ARG   A O    1 
ATOM   488  C  CB   . ARG   A 1 54  ? -17.131 2.521   -41.277 1.00 82.01  ? 572  ARG   A CB   1 
ATOM   489  C  CG   . ARG   A 1 54  ? -16.145 2.081   -40.203 1.00 91.10  ? 572  ARG   A CG   1 
ATOM   490  C  CD   . ARG   A 1 54  ? -16.815 1.219   -39.133 1.00 94.52  ? 572  ARG   A CD   1 
ATOM   491  N  NE   . ARG   A 1 54  ? -15.966 0.990   -37.962 1.00 96.38  ? 572  ARG   A NE   1 
ATOM   492  C  CZ   . ARG   A 1 54  ? -14.787 0.371   -37.981 1.00 100.40 ? 572  ARG   A CZ   1 
ATOM   493  N  NH1  . ARG   A 1 54  ? -14.289 -0.114  -39.112 1.00 101.48 ? 572  ARG   A NH1  1 
ATOM   494  N  NH2  . ARG   A 1 54  ? -14.103 0.223   -36.854 1.00 102.79 ? 572  ARG   A NH2  1 
ATOM   495  N  N    . LEU   A 1 55  ? -18.488 5.598   -40.760 1.00 59.10  ? 573  LEU   A N    1 
ATOM   496  C  CA   . LEU   A 1 55  ? -18.872 6.905   -41.276 1.00 59.91  ? 573  LEU   A CA   1 
ATOM   497  C  C    . LEU   A 1 55  ? -17.859 7.381   -42.310 1.00 63.37  ? 573  LEU   A C    1 
ATOM   498  O  O    . LEU   A 1 55  ? -16.675 7.550   -42.000 1.00 60.63  ? 573  LEU   A O    1 
ATOM   499  C  CB   . LEU   A 1 55  ? -18.988 7.904   -40.129 1.00 57.84  ? 573  LEU   A CB   1 
ATOM   500  C  CG   . LEU   A 1 55  ? -19.915 7.451   -39.002 1.00 55.17  ? 573  LEU   A CG   1 
ATOM   501  C  CD1  . LEU   A 1 55  ? -19.768 8.343   -37.780 1.00 48.45  ? 573  LEU   A CD1  1 
ATOM   502  C  CD2  . LEU   A 1 55  ? -21.357 7.423   -39.486 1.00 55.05  ? 573  LEU   A CD2  1 
ATOM   503  N  N    . TRP   A 1 56  ? -18.328 7.597   -43.536 1.00 65.07  ? 574  TRP   A N    1 
ATOM   504  C  CA   . TRP   A 1 56  ? -17.513 8.139   -44.621 1.00 69.74  ? 574  TRP   A CA   1 
ATOM   505  C  C    . TRP   A 1 56  ? -18.122 9.483   -45.005 1.00 70.41  ? 574  TRP   A C    1 
ATOM   506  O  O    . TRP   A 1 56  ? -19.057 9.556   -45.807 1.00 73.05  ? 574  TRP   A O    1 
ATOM   507  C  CB   . TRP   A 1 56  ? -17.445 7.172   -45.801 1.00 76.29  ? 574  TRP   A CB   1 
ATOM   508  C  CG   . TRP   A 1 56  ? -16.380 6.134   -45.626 1.00 82.53  ? 574  TRP   A CG   1 
ATOM   509  C  CD1  . TRP   A 1 56  ? -15.686 5.862   -44.483 1.00 83.70  ? 574  TRP   A CD1  1 
ATOM   510  C  CD2  . TRP   A 1 56  ? -15.877 5.237   -46.623 1.00 89.98  ? 574  TRP   A CD2  1 
ATOM   511  N  NE1  . TRP   A 1 56  ? -14.786 4.849   -44.704 1.00 88.31  ? 574  TRP   A NE1  1 
ATOM   512  C  CE2  . TRP   A 1 56  ? -14.883 4.447   -46.010 1.00 92.36  ? 574  TRP   A CE2  1 
ATOM   513  C  CE3  . TRP   A 1 56  ? -16.171 5.022   -47.973 1.00 94.55  ? 574  TRP   A CE3  1 
ATOM   514  C  CZ2  . TRP   A 1 56  ? -14.182 3.461   -46.700 1.00 97.01  ? 574  TRP   A CZ2  1 
ATOM   515  C  CZ3  . TRP   A 1 56  ? -15.474 4.041   -48.656 1.00 98.32  ? 574  TRP   A CZ3  1 
ATOM   516  C  CH2  . TRP   A 1 56  ? -14.491 3.273   -48.018 1.00 99.87  ? 574  TRP   A CH2  1 
ATOM   517  N  N    . ILE   A 1 57  ? -17.584 10.548  -44.418 1.00 66.84  ? 575  ILE   A N    1 
ATOM   518  C  CA   . ILE   A 1 57  ? -18.117 11.897  -44.557 1.00 63.58  ? 575  ILE   A CA   1 
ATOM   519  C  C    . ILE   A 1 57  ? -17.170 12.710  -45.426 1.00 66.93  ? 575  ILE   A C    1 
ATOM   520  O  O    . ILE   A 1 57  ? -15.947 12.640  -45.265 1.00 75.33  ? 575  ILE   A O    1 
ATOM   521  C  CB   . ILE   A 1 57  ? -18.311 12.560  -43.180 1.00 59.94  ? 575  ILE   A CB   1 
ATOM   522  C  CG1  . ILE   A 1 57  ? -19.250 11.714  -42.317 1.00 53.56  ? 575  ILE   A CG1  1 
ATOM   523  C  CG2  . ILE   A 1 57  ? -18.841 13.976  -43.331 1.00 60.76  ? 575  ILE   A CG2  1 
ATOM   524  C  CD1  . ILE   A 1 57  ? -19.315 12.152  -40.873 1.00 46.97  ? 575  ILE   A CD1  1 
ATOM   525  N  N    . GLU   A 1 58  ? -17.737 13.481  -46.349 1.00 64.39  ? 576  GLU   A N    1 
ATOM   526  C  CA   . GLU   A 1 58  ? -16.955 14.318  -47.244 1.00 70.11  ? 576  GLU   A CA   1 
ATOM   527  C  C    . GLU   A 1 58  ? -17.506 15.735  -47.205 1.00 69.98  ? 576  GLU   A C    1 
ATOM   528  O  O    . GLU   A 1 58  ? -18.705 15.945  -47.414 1.00 67.33  ? 576  GLU   A O    1 
ATOM   529  C  CB   . GLU   A 1 58  ? -16.978 13.759  -48.666 1.00 76.87  ? 576  GLU   A CB   1 
ATOM   530  C  CG   . GLU   A 1 58  ? -16.582 14.746  -49.731 1.00 84.52  ? 576  GLU   A CG   1 
ATOM   531  C  CD   . GLU   A 1 58  ? -16.530 14.107  -51.095 1.00 96.34  ? 576  GLU   A CD   1 
ATOM   532  O  OE1  . GLU   A 1 58  ? -16.833 14.805  -52.081 1.00 101.89 ? 576  GLU   A OE1  1 
ATOM   533  O  OE2  . GLU   A 1 58  ? -16.186 12.909  -51.182 1.00 101.41 ? 576  GLU   A OE2  1 
ATOM   534  N  N    . PHE   A 1 59  ? -16.631 16.698  -46.930 1.00 71.47  ? 577  PHE   A N    1 
ATOM   535  C  CA   . PHE   A 1 59  ? -17.006 18.097  -46.773 1.00 70.08  ? 577  PHE   A CA   1 
ATOM   536  C  C    . PHE   A 1 59  ? -16.605 18.880  -48.015 1.00 72.24  ? 577  PHE   A C    1 
ATOM   537  O  O    . PHE   A 1 59  ? -15.439 18.847  -48.419 1.00 78.59  ? 577  PHE   A O    1 
ATOM   538  C  CB   . PHE   A 1 59  ? -16.335 18.708  -45.540 1.00 68.26  ? 577  PHE   A CB   1 
ATOM   539  C  CG   . PHE   A 1 59  ? -17.141 18.585  -44.279 1.00 64.66  ? 577  PHE   A CG   1 
ATOM   540  C  CD1  . PHE   A 1 59  ? -18.271 19.361  -44.083 1.00 62.89  ? 577  PHE   A CD1  1 
ATOM   541  C  CD2  . PHE   A 1 59  ? -16.758 17.703  -43.282 1.00 64.95  ? 577  PHE   A CD2  1 
ATOM   542  C  CE1  . PHE   A 1 59  ? -19.011 19.253  -42.919 1.00 58.95  ? 577  PHE   A CE1  1 
ATOM   543  C  CE2  . PHE   A 1 59  ? -17.492 17.590  -42.117 1.00 63.32  ? 577  PHE   A CE2  1 
ATOM   544  C  CZ   . PHE   A 1 59  ? -18.620 18.366  -41.934 1.00 59.46  ? 577  PHE   A CZ   1 
ATOM   545  N  N    . ASP   A 1 60  ? -17.574 19.577  -48.613 1.00 72.82  ? 578  ASP   A N    1 
ATOM   546  C  CA   . ASP   A 1 60  ? -17.324 20.506  -49.720 1.00 78.04  ? 578  ASP   A CA   1 
ATOM   547  C  C    . ASP   A 1 60  ? -16.531 19.855  -50.849 1.00 83.57  ? 578  ASP   A C    1 
ATOM   548  O  O    . ASP   A 1 60  ? -15.710 20.503  -51.504 1.00 87.62  ? 578  ASP   A O    1 
ATOM   549  C  CB   . ASP   A 1 60  ? -16.613 21.768  -49.226 1.00 80.96  ? 578  ASP   A CB   1 
ATOM   550  C  CG   . ASP   A 1 60  ? -17.439 22.544  -48.220 1.00 82.90  ? 578  ASP   A CG   1 
ATOM   551  O  OD1  . ASP   A 1 60  ? -18.615 22.842  -48.515 1.00 82.39  ? 578  ASP   A OD1  1 
ATOM   552  O  OD2  . ASP   A 1 60  ? -16.912 22.854  -47.132 1.00 84.31  ? 578  ASP   A OD2  1 
ATOM   553  N  N    . GLY   A 1 61  ? -16.766 18.567  -51.083 1.00 82.99  ? 579  GLY   A N    1 
ATOM   554  C  CA   . GLY   A 1 61  ? -16.065 17.869  -52.146 1.00 84.58  ? 579  GLY   A CA   1 
ATOM   555  C  C    . GLY   A 1 61  ? -14.570 17.775  -51.948 1.00 85.72  ? 579  GLY   A C    1 
ATOM   556  O  O    . GLY   A 1 61  ? -13.827 17.667  -52.929 1.00 90.77  ? 579  GLY   A O    1 
ATOM   557  N  N    . GLU   A 1 62  ? -14.101 17.822  -50.703 1.00 84.49  ? 580  GLU   A N    1 
ATOM   558  C  CA   . GLU   A 1 62  ? -12.677 17.688  -50.418 1.00 93.24  ? 580  GLU   A CA   1 
ATOM   559  C  C    . GLU   A 1 62  ? -12.318 16.207  -50.432 1.00 94.66  ? 580  GLU   A C    1 
ATOM   560  O  O    . GLU   A 1 62  ? -12.701 15.457  -49.529 1.00 90.43  ? 580  GLU   A O    1 
ATOM   561  C  CB   . GLU   A 1 62  ? -12.333 18.340  -49.081 1.00 94.64  ? 580  GLU   A CB   1 
ATOM   562  C  CG   . GLU   A 1 62  ? -12.283 19.861  -49.144 1.00 97.91  ? 580  GLU   A CG   1 
ATOM   563  C  CD   . GLU   A 1 62  ? -12.652 20.519  -47.830 1.00 95.53  ? 580  GLU   A CD   1 
ATOM   564  O  OE1  . GLU   A 1 62  ? -12.543 21.759  -47.735 1.00 97.36  ? 580  GLU   A OE1  1 
ATOM   565  O  OE2  . GLU   A 1 62  ? -13.051 19.797  -46.892 1.00 92.50  ? 580  GLU   A OE2  1 
ATOM   566  N  N    . LYS   A 1 63  ? -11.587 15.787  -51.460 1.00 101.11 ? 581  LYS   A N    1 
ATOM   567  C  CA   . LYS   A 1 63  ? -11.299 14.381  -51.692 1.00 106.33 ? 581  LYS   A CA   1 
ATOM   568  C  C    . LYS   A 1 63  ? -10.036 13.943  -50.958 1.00 111.64 ? 581  LYS   A C    1 
ATOM   569  O  O    . LYS   A 1 63  ? -9.149  14.743  -50.653 1.00 116.56 ? 581  LYS   A O    1 
ATOM   570  C  CB   . LYS   A 1 63  ? -11.137 14.102  -53.187 1.00 110.77 ? 581  LYS   A CB   1 
ATOM   571  C  CG   . LYS   A 1 63  ? -12.210 14.710  -54.069 1.00 110.90 ? 581  LYS   A CG   1 
ATOM   572  C  CD   . LYS   A 1 63  ? -13.536 13.997  -53.894 1.00 107.28 ? 581  LYS   A CD   1 
ATOM   573  C  CE   . LYS   A 1 63  ? -14.695 14.934  -54.165 1.00 104.78 ? 581  LYS   A CE   1 
ATOM   574  N  NZ   . LYS   A 1 63  ? -15.025 15.060  -55.608 1.00 109.02 ? 581  LYS   A NZ   1 
ATOM   575  N  N    . GLY   A 1 64  ? -9.969  12.642  -50.684 1.00 110.17 ? 582  GLY   A N    1 
ATOM   576  C  CA   . GLY   A 1 64  ? -8.762  12.014  -50.185 1.00 111.51 ? 582  GLY   A CA   1 
ATOM   577  C  C    . GLY   A 1 64  ? -8.291  12.484  -48.826 1.00 109.44 ? 582  GLY   A C    1 
ATOM   578  O  O    . GLY   A 1 64  ? -7.160  12.958  -48.687 1.00 114.42 ? 582  GLY   A O    1 
ATOM   579  N  N    . LEU   A 1 65  ? -9.138  12.350  -47.811 1.00 104.04 ? 583  LEU   A N    1 
ATOM   580  C  CA   . LEU   A 1 65  ? -8.749  12.669  -46.449 1.00 101.52 ? 583  LEU   A CA   1 
ATOM   581  C  C    . LEU   A 1 65  ? -9.174  11.542  -45.521 1.00 98.55  ? 583  LEU   A C    1 
ATOM   582  O  O    . LEU   A 1 65  ? -10.027 10.718  -45.859 1.00 97.50  ? 583  LEU   A O    1 
ATOM   583  C  CB   . LEU   A 1 65  ? -9.350  13.993  -45.991 1.00 97.77  ? 583  LEU   A CB   1 
ATOM   584  C  CG   . LEU   A 1 65  ? -8.351  15.128  -46.176 1.00 104.07 ? 583  LEU   A CG   1 
ATOM   585  C  CD1  . LEU   A 1 65  ? -9.028  16.404  -45.891 1.00 99.87  ? 583  LEU   A CD1  1 
ATOM   586  C  CD2  . LEU   A 1 65  ? -7.170  14.965  -45.273 1.00 108.12 ? 583  LEU   A CD2  1 
ATOM   587  N  N    . ASP   A 1 66  ? -8.553  11.514  -44.343 1.00 99.14  ? 584  ASP   A N    1 
ATOM   588  C  CA   . ASP   A 1 66  ? -8.799  10.463  -43.365 1.00 98.71  ? 584  ASP   A CA   1 
ATOM   589  C  C    . ASP   A 1 66  ? -10.258 10.470  -42.934 1.00 96.97  ? 584  ASP   A C    1 
ATOM   590  O  O    . ASP   A 1 66  ? -10.724 11.423  -42.301 1.00 92.87  ? 584  ASP   A O    1 
ATOM   591  C  CB   . ASP   A 1 66  ? -7.884  10.630  -42.151 1.00 98.23  ? 584  ASP   A CB   1 
ATOM   592  C  CG   . ASP   A 1 66  ? -8.158  9.610   -41.068 1.00 99.16  ? 584  ASP   A CG   1 
ATOM   593  O  OD1  . ASP   A 1 66  ? -7.966  8.404   -41.328 1.00 103.16 ? 584  ASP   A OD1  1 
ATOM   594  O  OD2  . ASP   A 1 66  ? -8.560  10.013  -39.957 1.00 98.04  ? 584  ASP   A OD2  1 
ATOM   595  N  N    . TYR   A 1 67  ? -10.985 9.405   -43.276 1.00 98.88  ? 585  TYR   A N    1 
ATOM   596  C  CA   . TYR   A 1 67  ? -12.401 9.309   -42.947 1.00 95.80  ? 585  TYR   A CA   1 
ATOM   597  C  C    . TYR   A 1 67  ? -12.659 9.235   -41.448 1.00 94.37  ? 585  TYR   A C    1 
ATOM   598  O  O    . TYR   A 1 67  ? -13.820 9.318   -41.034 1.00 91.82  ? 585  TYR   A O    1 
ATOM   599  C  CB   . TYR   A 1 67  ? -13.012 8.091   -43.642 1.00 94.92  ? 585  TYR   A CB   1 
ATOM   600  C  CG   . TYR   A 1 67  ? -13.503 8.365   -45.049 1.00 95.27  ? 585  TYR   A CG   1 
ATOM   601  C  CD1  . TYR   A 1 67  ? -14.316 9.458   -45.321 1.00 91.13  ? 585  TYR   A CD1  1 
ATOM   602  C  CD2  . TYR   A 1 67  ? -13.155 7.529   -46.103 1.00 99.48  ? 585  TYR   A CD2  1 
ATOM   603  C  CE1  . TYR   A 1 67  ? -14.770 9.711   -46.604 1.00 92.49  ? 585  TYR   A CE1  1 
ATOM   604  C  CE2  . TYR   A 1 67  ? -13.604 7.774   -47.389 1.00 100.35 ? 585  TYR   A CE2  1 
ATOM   605  C  CZ   . TYR   A 1 67  ? -14.410 8.866   -47.634 1.00 97.30  ? 585  TYR   A CZ   1 
ATOM   606  O  OH   . TYR   A 1 67  ? -14.860 9.115   -48.911 1.00 98.01  ? 585  TYR   A OH   1 
ATOM   607  N  N    . GLY   A 1 68  ? -11.620 9.079   -40.630 1.00 94.49  ? 586  GLY   A N    1 
ATOM   608  C  CA   . GLY   A 1 68  ? -11.794 9.066   -39.192 1.00 90.42  ? 586  GLY   A CA   1 
ATOM   609  C  C    . GLY   A 1 68  ? -11.746 10.458  -38.598 1.00 88.02  ? 586  GLY   A C    1 
ATOM   610  O  O    . GLY   A 1 68  ? -12.526 10.789  -37.700 1.00 79.67  ? 586  GLY   A O    1 
ATOM   611  N  N    . GLY   A 1 69  ? -10.835 11.287  -39.108 1.00 91.05  ? 587  GLY   A N    1 
ATOM   612  C  CA   . GLY   A 1 69  ? -10.693 12.630  -38.574 1.00 86.25  ? 587  GLY   A CA   1 
ATOM   613  C  C    . GLY   A 1 69  ? -11.843 13.546  -38.942 1.00 77.82  ? 587  GLY   A C    1 
ATOM   614  O  O    . GLY   A 1 69  ? -12.305 14.337  -38.114 1.00 76.00  ? 587  GLY   A O    1 
ATOM   615  N  N    . VAL   A 1 70  ? -12.314 13.464  -40.188 1.00 70.19  ? 588  VAL   A N    1 
ATOM   616  C  CA   . VAL   A 1 70  ? -13.409 14.332  -40.611 1.00 67.17  ? 588  VAL   A CA   1 
ATOM   617  C  C    . VAL   A 1 70  ? -14.684 13.986  -39.853 1.00 59.60  ? 588  VAL   A C    1 
ATOM   618  O  O    . VAL   A 1 70  ? -15.508 14.863  -39.568 1.00 59.55  ? 588  VAL   A O    1 
ATOM   619  C  CB   . VAL   A 1 70  ? -13.599 14.263  -42.139 1.00 68.40  ? 588  VAL   A CB   1 
ATOM   620  C  CG1  . VAL   A 1 70  ? -12.249 14.327  -42.839 1.00 70.94  ? 588  VAL   A CG1  1 
ATOM   621  C  CG2  . VAL   A 1 70  ? -14.352 13.011  -42.550 1.00 71.37  ? 588  VAL   A CG2  1 
ATOM   622  N  N    . ALA   A 1 71  ? -14.855 12.711  -39.493 1.00 56.20  ? 589  ALA   A N    1 
ATOM   623  C  CA   . ALA   A 1 71  ? -15.974 12.327  -38.641 1.00 58.51  ? 589  ALA   A CA   1 
ATOM   624  C  C    . ALA   A 1 71  ? -15.931 13.088  -37.323 1.00 59.89  ? 589  ALA   A C    1 
ATOM   625  O  O    . ALA   A 1 71  ? -16.952 13.602  -36.854 1.00 56.97  ? 589  ALA   A O    1 
ATOM   626  C  CB   . ALA   A 1 71  ? -15.955 10.818  -38.396 1.00 59.99  ? 589  ALA   A CB   1 
ATOM   627  N  N    . ARG   A 1 72  ? -14.745 13.178  -36.717 1.00 64.58  ? 590  ARG   A N    1 
ATOM   628  C  CA   . ARG   A 1 72  ? -14.604 13.920  -35.469 1.00 63.95  ? 590  ARG   A CA   1 
ATOM   629  C  C    . ARG   A 1 72  ? -14.921 15.398  -35.669 1.00 60.87  ? 590  ARG   A C    1 
ATOM   630  O  O    . ARG   A 1 72  ? -15.556 16.025  -34.812 1.00 56.05  ? 590  ARG   A O    1 
ATOM   631  C  CB   . ARG   A 1 72  ? -13.194 13.733  -34.908 1.00 69.75  ? 590  ARG   A CB   1 
ATOM   632  C  CG   . ARG   A 1 72  ? -12.589 14.982  -34.291 1.00 75.32  ? 590  ARG   A CG   1 
ATOM   633  C  CD   . ARG   A 1 72  ? -11.652 14.637  -33.144 1.00 82.16  ? 590  ARG   A CD   1 
ATOM   634  N  NE   . ARG   A 1 72  ? -10.759 15.745  -32.814 1.00 87.13  ? 590  ARG   A NE   1 
ATOM   635  C  CZ   . ARG   A 1 72  ? -11.129 16.831  -32.142 1.00 85.94  ? 590  ARG   A CZ   1 
ATOM   636  N  NH1  . ARG   A 1 72  ? -12.380 16.964  -31.721 1.00 79.38  ? 590  ARG   A NH1  1 
ATOM   637  N  NH2  . ARG   A 1 72  ? -10.245 17.787  -31.889 1.00 89.40  ? 590  ARG   A NH2  1 
ATOM   638  N  N    . GLU   A 1 73  ? -14.496 15.972  -36.798 1.00 60.35  ? 591  GLU   A N    1 
ATOM   639  C  CA   . GLU   A 1 73  ? -14.833 17.364  -37.075 1.00 62.42  ? 591  GLU   A CA   1 
ATOM   640  C  C    . GLU   A 1 73  ? -16.334 17.533  -37.272 1.00 59.62  ? 591  GLU   A C    1 
ATOM   641  O  O    . GLU   A 1 73  ? -16.924 18.509  -36.792 1.00 56.47  ? 591  GLU   A O    1 
ATOM   642  C  CB   . GLU   A 1 73  ? -14.067 17.870  -38.300 1.00 70.27  ? 591  GLU   A CB   1 
ATOM   643  C  CG   . GLU   A 1 73  ? -14.785 18.980  -39.060 1.00 81.03  ? 591  GLU   A CG   1 
ATOM   644  C  CD   . GLU   A 1 73  ? -13.878 19.726  -40.020 1.00 96.02  ? 591  GLU   A CD   1 
ATOM   645  O  OE1  . GLU   A 1 73  ? -13.467 19.130  -41.034 1.00 103.99 ? 591  GLU   A OE1  1 
ATOM   646  O  OE2  . GLU   A 1 73  ? -13.582 20.912  -39.766 1.00 101.21 ? 591  GLU   A OE2  1 
ATOM   647  N  N    . TRP   A 1 74  ? -16.972 16.586  -37.967 1.00 55.30  ? 592  TRP   A N    1 
ATOM   648  C  CA   . TRP   A 1 74  ? -18.415 16.667  -38.176 1.00 50.27  ? 592  TRP   A CA   1 
ATOM   649  C  C    . TRP   A 1 74  ? -19.160 16.669  -36.849 1.00 51.71  ? 592  TRP   A C    1 
ATOM   650  O  O    . TRP   A 1 74  ? -20.073 17.476  -36.638 1.00 52.46  ? 592  TRP   A O    1 
ATOM   651  C  CB   . TRP   A 1 74  ? -18.896 15.508  -39.050 1.00 48.67  ? 592  TRP   A CB   1 
ATOM   652  C  CG   . TRP   A 1 74  ? -20.396 15.437  -39.134 1.00 47.32  ? 592  TRP   A CG   1 
ATOM   653  C  CD1  . TRP   A 1 74  ? -21.214 16.281  -39.824 1.00 48.04  ? 592  TRP   A CD1  1 
ATOM   654  C  CD2  . TRP   A 1 74  ? -21.254 14.483  -38.492 1.00 47.84  ? 592  TRP   A CD2  1 
ATOM   655  N  NE1  . TRP   A 1 74  ? -22.527 15.909  -39.661 1.00 49.16  ? 592  TRP   A NE1  1 
ATOM   656  C  CE2  . TRP   A 1 74  ? -22.578 14.809  -38.847 1.00 47.75  ? 592  TRP   A CE2  1 
ATOM   657  C  CE3  . TRP   A 1 74  ? -21.030 13.385  -37.657 1.00 52.44  ? 592  TRP   A CE3  1 
ATOM   658  C  CZ2  . TRP   A 1 74  ? -23.674 14.077  -38.395 1.00 47.44  ? 592  TRP   A CZ2  1 
ATOM   659  C  CZ3  . TRP   A 1 74  ? -22.122 12.657  -37.210 1.00 49.54  ? 592  TRP   A CZ3  1 
ATOM   660  C  CH2  . TRP   A 1 74  ? -23.426 13.007  -37.579 1.00 47.28  ? 592  TRP   A CH2  1 
ATOM   661  N  N    . PHE   A 1 75  ? -18.782 15.768  -35.938 1.00 52.04  ? 593  PHE   A N    1 
ATOM   662  C  CA   . PHE   A 1 75  ? -19.429 15.719  -34.632 1.00 50.23  ? 593  PHE   A CA   1 
ATOM   663  C  C    . PHE   A 1 75  ? -19.264 17.029  -33.876 1.00 52.75  ? 593  PHE   A C    1 
ATOM   664  O  O    . PHE   A 1 75  ? -20.168 17.439  -33.140 1.00 53.78  ? 593  PHE   A O    1 
ATOM   665  C  CB   . PHE   A 1 75  ? -18.869 14.558  -33.811 1.00 45.59  ? 593  PHE   A CB   1 
ATOM   666  C  CG   . PHE   A 1 75  ? -19.560 13.253  -34.065 1.00 43.18  ? 593  PHE   A CG   1 
ATOM   667  C  CD1  . PHE   A 1 75  ? -20.894 13.087  -33.732 1.00 42.82  ? 593  PHE   A CD1  1 
ATOM   668  C  CD2  . PHE   A 1 75  ? -18.879 12.194  -34.640 1.00 48.55  ? 593  PHE   A CD2  1 
ATOM   669  C  CE1  . PHE   A 1 75  ? -21.536 11.886  -33.965 1.00 42.81  ? 593  PHE   A CE1  1 
ATOM   670  C  CE2  . PHE   A 1 75  ? -19.516 10.989  -34.877 1.00 45.78  ? 593  PHE   A CE2  1 
ATOM   671  C  CZ   . PHE   A 1 75  ? -20.844 10.835  -34.538 1.00 40.19  ? 593  PHE   A CZ   1 
ATOM   672  N  N    . PHE   A 1 76  ? -18.124 17.698  -34.044 1.00 51.16  ? 594  PHE   A N    1 
ATOM   673  C  CA   . PHE   A 1 76  ? -17.949 19.016  -33.446 1.00 53.13  ? 594  PHE   A CA   1 
ATOM   674  C  C    . PHE   A 1 76  ? -18.813 20.051  -34.154 1.00 51.74  ? 594  PHE   A C    1 
ATOM   675  O  O    . PHE   A 1 76  ? -19.528 20.826  -33.507 1.00 55.30  ? 594  PHE   A O    1 
ATOM   676  C  CB   . PHE   A 1 76  ? -16.473 19.419  -33.490 1.00 51.59  ? 594  PHE   A CB   1 
ATOM   677  C  CG   . PHE   A 1 76  ? -16.215 20.833  -33.050 1.00 55.69  ? 594  PHE   A CG   1 
ATOM   678  C  CD1  . PHE   A 1 76  ? -16.135 21.148  -31.703 1.00 60.43  ? 594  PHE   A CD1  1 
ATOM   679  C  CD2  . PHE   A 1 76  ? -16.042 21.845  -33.982 1.00 59.54  ? 594  PHE   A CD2  1 
ATOM   680  C  CE1  . PHE   A 1 76  ? -15.894 22.447  -31.293 1.00 67.84  ? 594  PHE   A CE1  1 
ATOM   681  C  CE2  . PHE   A 1 76  ? -15.802 23.147  -33.578 1.00 67.14  ? 594  PHE   A CE2  1 
ATOM   682  C  CZ   . PHE   A 1 76  ? -15.727 23.448  -32.232 1.00 69.61  ? 594  PHE   A CZ   1 
ATOM   683  N  N    . LEU   A 1 77  ? -18.768 20.068  -35.488 1.00 51.44  ? 595  LEU   A N    1 
ATOM   684  C  CA   . LEU   A 1 77  ? -19.526 21.059  -36.245 1.00 52.96  ? 595  LEU   A CA   1 
ATOM   685  C  C    . LEU   A 1 77  ? -21.026 20.889  -36.040 1.00 49.58  ? 595  LEU   A C    1 
ATOM   686  O  O    . LEU   A 1 77  ? -21.749 21.875  -35.856 1.00 50.83  ? 595  LEU   A O    1 
ATOM   687  C  CB   . LEU   A 1 77  ? -19.175 20.966  -37.729 1.00 54.36  ? 595  LEU   A CB   1 
ATOM   688  C  CG   . LEU   A 1 77  ? -17.776 21.449  -38.119 1.00 56.81  ? 595  LEU   A CG   1 
ATOM   689  C  CD1  . LEU   A 1 77  ? -17.550 21.289  -39.614 1.00 55.92  ? 595  LEU   A CD1  1 
ATOM   690  C  CD2  . LEU   A 1 77  ? -17.570 22.894  -37.693 1.00 57.92  ? 595  LEU   A CD2  1 
ATOM   691  N  N    . ILE   A 1 78  ? -21.513 19.647  -36.065 1.00 42.82  ? 596  ILE   A N    1 
ATOM   692  C  CA   . ILE   A 1 78  ? -22.947 19.428  -35.913 1.00 39.77  ? 596  ILE   A CA   1 
ATOM   693  C  C    . ILE   A 1 78  ? -23.390 19.725  -34.484 1.00 40.92  ? 596  ILE   A C    1 
ATOM   694  O  O    . ILE   A 1 78  ? -24.534 20.137  -34.256 1.00 39.54  ? 596  ILE   A O    1 
ATOM   695  C  CB   . ILE   A 1 78  ? -23.323 17.998  -36.355 1.00 41.80  ? 596  ILE   A CB   1 
ATOM   696  C  CG1  . ILE   A 1 78  ? -24.805 17.923  -36.728 1.00 45.14  ? 596  ILE   A CG1  1 
ATOM   697  C  CG2  . ILE   A 1 78  ? -22.980 16.970  -35.280 1.00 37.43  ? 596  ILE   A CG2  1 
ATOM   698  C  CD1  . ILE   A 1 78  ? -25.162 18.722  -37.962 1.00 45.01  ? 596  ILE   A CD1  1 
ATOM   699  N  N    . SER   A 1 79  ? -22.498 19.551  -33.505 1.00 43.02  ? 597  SER   A N    1 
ATOM   700  C  CA   . SER   A 1 79  ? -22.840 19.878  -32.123 1.00 44.12  ? 597  SER   A CA   1 
ATOM   701  C  C    . SER   A 1 79  ? -23.045 21.377  -31.949 1.00 47.50  ? 597  SER   A C    1 
ATOM   702  O  O    . SER   A 1 79  ? -24.006 21.815  -31.306 1.00 52.40  ? 597  SER   A O    1 
ATOM   703  C  CB   . SER   A 1 79  ? -21.749 19.378  -31.176 1.00 46.60  ? 597  SER   A CB   1 
ATOM   704  O  OG   . SER   A 1 79  ? -21.721 17.963  -31.124 1.00 50.00  ? 597  SER   A OG   1 
ATOM   705  N  N    . LYS   A 1 80  ? -22.144 22.184  -32.514 1.00 43.40  ? 598  LYS   A N    1 
ATOM   706  C  CA   . LYS   A 1 80  ? -22.279 23.630  -32.387 1.00 47.89  ? 598  LYS   A CA   1 
ATOM   707  C  C    . LYS   A 1 80  ? -23.541 24.130  -33.077 1.00 45.69  ? 598  LYS   A C    1 
ATOM   708  O  O    . LYS   A 1 80  ? -24.094 25.164  -32.685 1.00 47.85  ? 598  LYS   A O    1 
ATOM   709  C  CB   . LYS   A 1 80  ? -21.042 24.326  -32.957 1.00 51.99  ? 598  LYS   A CB   1 
ATOM   710  C  CG   . LYS   A 1 80  ? -19.783 24.152  -32.113 1.00 58.26  ? 598  LYS   A CG   1 
ATOM   711  C  CD   . LYS   A 1 80  ? -19.890 24.880  -30.787 1.00 64.03  ? 598  LYS   A CD   1 
ATOM   712  C  CE   . LYS   A 1 80  ? -18.541 25.429  -30.325 1.00 71.49  ? 598  LYS   A CE   1 
ATOM   713  N  NZ   . LYS   A 1 80  ? -18.563 26.911  -30.121 1.00 74.53  ? 598  LYS   A NZ   1 
ATOM   714  N  N    . GLU   A 1 81  ? -24.013 23.405  -34.093 1.00 42.57  ? 599  GLU   A N    1 
ATOM   715  C  CA   . GLU   A 1 81  ? -25.243 23.770  -34.785 1.00 41.45  ? 599  GLU   A CA   1 
ATOM   716  C  C    . GLU   A 1 81  ? -26.477 23.328  -34.006 1.00 43.89  ? 599  GLU   A C    1 
ATOM   717  O  O    . GLU   A 1 81  ? -27.359 24.143  -33.718 1.00 47.10  ? 599  GLU   A O    1 
ATOM   718  C  CB   . GLU   A 1 81  ? -25.254 23.159  -36.188 1.00 42.42  ? 599  GLU   A CB   1 
ATOM   719  C  CG   . GLU   A 1 81  ? -24.480 23.957  -37.218 1.00 45.79  ? 599  GLU   A CG   1 
ATOM   720  C  CD   . GLU   A 1 81  ? -25.077 25.330  -37.453 1.00 53.56  ? 599  GLU   A CD   1 
ATOM   721  O  OE1  . GLU   A 1 81  ? -25.963 25.454  -38.324 1.00 55.36  ? 599  GLU   A OE1  1 
ATOM   722  O  OE2  . GLU   A 1 81  ? -24.662 26.286  -36.765 1.00 58.76  ? 599  GLU   A OE2  1 
ATOM   723  N  N    . MET   A 1 82  ? -26.552 22.039  -33.656 1.00 40.28  ? 600  MET   A N    1 
ATOM   724  C  CA   . MET   A 1 82  ? -27.753 21.508  -33.015 1.00 40.48  ? 600  MET   A CA   1 
ATOM   725  C  C    . MET   A 1 82  ? -28.041 22.210  -31.695 1.00 40.89  ? 600  MET   A C    1 
ATOM   726  O  O    . MET   A 1 82  ? -29.205 22.425  -31.338 1.00 43.07  ? 600  MET   A O    1 
ATOM   727  C  CB   . MET   A 1 82  ? -27.610 20.005  -32.778 1.00 44.06  ? 600  MET   A CB   1 
ATOM   728  C  CG   . MET   A 1 82  ? -27.520 19.158  -34.030 1.00 46.48  ? 600  MET   A CG   1 
ATOM   729  S  SD   . MET   A 1 82  ? -27.327 17.413  -33.617 1.00 46.02  ? 600  MET   A SD   1 
ATOM   730  C  CE   . MET   A 1 82  ? -25.938 17.479  -32.487 1.00 50.77  ? 600  MET   A CE   1 
ATOM   731  N  N    . PHE   A 1 83  ? -26.996 22.566  -30.955 1.00 35.52  ? 601  PHE   A N    1 
ATOM   732  C  CA   . PHE   A 1 83  ? -27.140 23.133  -29.624 1.00 41.02  ? 601  PHE   A CA   1 
ATOM   733  C  C    . PHE   A 1 83  ? -27.035 24.651  -29.620 1.00 45.23  ? 601  PHE   A C    1 
ATOM   734  O  O    . PHE   A 1 83  ? -26.922 25.253  -28.548 1.00 50.57  ? 601  PHE   A O    1 
ATOM   735  C  CB   . PHE   A 1 83  ? -26.102 22.512  -28.691 1.00 41.40  ? 601  PHE   A CB   1 
ATOM   736  C  CG   . PHE   A 1 83  ? -26.137 21.011  -28.681 1.00 44.20  ? 601  PHE   A CG   1 
ATOM   737  C  CD1  . PHE   A 1 83  ? -24.967 20.271  -28.709 1.00 44.09  ? 601  PHE   A CD1  1 
ATOM   738  C  CD2  . PHE   A 1 83  ? -27.351 20.340  -28.661 1.00 43.05  ? 601  PHE   A CD2  1 
ATOM   739  C  CE1  . PHE   A 1 83  ? -25.007 18.888  -28.708 1.00 48.86  ? 601  PHE   A CE1  1 
ATOM   740  C  CE2  . PHE   A 1 83  ? -27.398 18.959  -28.660 1.00 44.40  ? 601  PHE   A CE2  1 
ATOM   741  C  CZ   . PHE   A 1 83  ? -26.224 18.231  -28.683 1.00 48.02  ? 601  PHE   A CZ   1 
ATOM   742  N  N    . ASN   A 1 84  ? -27.074 25.277  -30.788 1.00 42.09  ? 602  ASN   A N    1 
ATOM   743  C  CA   . ASN   A 1 84  ? -27.128 26.730  -30.870 1.00 41.50  ? 602  ASN   A CA   1 
ATOM   744  C  C    . ASN   A 1 84  ? -28.469 27.215  -30.334 1.00 40.20  ? 602  ASN   A C    1 
ATOM   745  O  O    . ASN   A 1 84  ? -29.514 26.865  -30.899 1.00 40.09  ? 602  ASN   A O    1 
ATOM   746  C  CB   . ASN   A 1 84  ? -26.934 27.184  -32.315 1.00 40.92  ? 602  ASN   A CB   1 
ATOM   747  C  CG   . ASN   A 1 84  ? -26.728 28.681  -32.435 1.00 47.77  ? 602  ASN   A CG   1 
ATOM   748  O  OD1  . ASN   A 1 84  ? -26.950 29.429  -31.485 1.00 48.04  ? 602  ASN   A OD1  1 
ATOM   749  N  ND2  . ASN   A 1 84  ? -26.306 29.126  -33.612 1.00 50.27  ? 602  ASN   A ND2  1 
ATOM   750  N  N    . PRO   A 1 85  ? -28.496 28.005  -29.258 1.00 41.45  ? 603  PRO   A N    1 
ATOM   751  C  CA   . PRO   A 1 85  ? -29.784 28.492  -28.739 1.00 44.11  ? 603  PRO   A CA   1 
ATOM   752  C  C    . PRO   A 1 85  ? -30.564 29.341  -29.726 1.00 48.21  ? 603  PRO   A C    1 
ATOM   753  O  O    . PRO   A 1 85  ? -31.791 29.439  -29.594 1.00 48.93  ? 603  PRO   A O    1 
ATOM   754  C  CB   . PRO   A 1 85  ? -29.378 29.304  -27.502 1.00 41.63  ? 603  PRO   A CB   1 
ATOM   755  C  CG   . PRO   A 1 85  ? -28.056 28.737  -27.099 1.00 42.88  ? 603  PRO   A CG   1 
ATOM   756  C  CD   . PRO   A 1 85  ? -27.372 28.388  -28.387 1.00 42.42  ? 603  PRO   A CD   1 
ATOM   757  N  N    . TYR   A 1 86  ? -29.904 29.952  -30.715 1.00 50.45  ? 604  TYR   A N    1 
ATOM   758  C  CA   A TYR   A 1 86  ? -30.626 30.786  -31.671 0.62 53.94  ? 604  TYR   A CA   1 
ATOM   759  C  CA   B TYR   A 1 86  ? -30.619 30.785  -31.677 0.38 53.94  ? 604  TYR   A CA   1 
ATOM   760  C  C    . TYR   A 1 86  ? -31.582 29.977  -32.537 1.00 48.43  ? 604  TYR   A C    1 
ATOM   761  O  O    . TYR   A 1 86  ? -32.481 30.556  -33.156 1.00 44.35  ? 604  TYR   A O    1 
ATOM   762  C  CB   A TYR   A 1 86  ? -29.644 31.558  -32.558 0.62 57.63  ? 604  TYR   A CB   1 
ATOM   763  C  CB   B TYR   A 1 86  ? -29.620 31.534  -32.563 0.38 57.58  ? 604  TYR   A CB   1 
ATOM   764  C  CG   A TYR   A 1 86  ? -28.851 32.616  -31.822 0.62 61.79  ? 604  TYR   A CG   1 
ATOM   765  C  CG   B TYR   A 1 86  ? -30.270 32.361  -33.647 0.38 62.76  ? 604  TYR   A CG   1 
ATOM   766  C  CD1  A TYR   A 1 86  ? -29.227 33.952  -31.865 0.62 65.21  ? 604  TYR   A CD1  1 
ATOM   767  C  CD1  B TYR   A 1 86  ? -30.884 33.570  -33.350 0.38 69.10  ? 604  TYR   A CD1  1 
ATOM   768  C  CD2  A TYR   A 1 86  ? -27.722 32.277  -31.090 0.62 63.69  ? 604  TYR   A CD2  1 
ATOM   769  C  CD2  B TYR   A 1 86  ? -30.273 31.929  -34.967 0.38 64.32  ? 604  TYR   A CD2  1 
ATOM   770  C  CE1  A TYR   A 1 86  ? -28.499 34.919  -31.194 0.62 68.12  ? 604  TYR   A CE1  1 
ATOM   771  C  CE1  B TYR   A 1 86  ? -31.483 34.327  -34.337 0.38 74.23  ? 604  TYR   A CE1  1 
ATOM   772  C  CE2  A TYR   A 1 86  ? -26.990 33.233  -30.419 0.62 66.16  ? 604  TYR   A CE2  1 
ATOM   773  C  CE2  B TYR   A 1 86  ? -30.869 32.679  -35.960 0.38 68.29  ? 604  TYR   A CE2  1 
ATOM   774  C  CZ   A TYR   A 1 86  ? -27.381 34.551  -30.473 0.62 69.92  ? 604  TYR   A CZ   1 
ATOM   775  C  CZ   B TYR   A 1 86  ? -31.472 33.877  -35.640 0.38 74.97  ? 604  TYR   A CZ   1 
ATOM   776  O  OH   A TYR   A 1 86  ? -26.649 35.502  -29.802 0.62 74.13  ? 604  TYR   A OH   1 
ATOM   777  O  OH   B TYR   A 1 86  ? -32.065 34.628  -36.628 0.38 82.11  ? 604  TYR   A OH   1 
ATOM   778  N  N    . TYR   A 1 87  ? -31.416 28.657  -32.595 1.00 46.89  ? 605  TYR   A N    1 
ATOM   779  C  CA   . TYR   A 1 87  ? -32.364 27.824  -33.321 1.00 45.44  ? 605  TYR   A CA   1 
ATOM   780  C  C    . TYR   A 1 87  ? -33.613 27.518  -32.507 1.00 49.12  ? 605  TYR   A C    1 
ATOM   781  O  O    . TYR   A 1 87  ? -34.612 27.070  -33.079 1.00 55.31  ? 605  TYR   A O    1 
ATOM   782  C  CB   . TYR   A 1 87  ? -31.687 26.526  -33.766 1.00 47.53  ? 605  TYR   A CB   1 
ATOM   783  C  CG   . TYR   A 1 87  ? -30.637 26.753  -34.828 1.00 53.37  ? 605  TYR   A CG   1 
ATOM   784  C  CD1  . TYR   A 1 87  ? -29.475 25.995  -34.865 1.00 49.08  ? 605  TYR   A CD1  1 
ATOM   785  C  CD2  . TYR   A 1 87  ? -30.805 27.740  -35.789 1.00 59.48  ? 605  TYR   A CD2  1 
ATOM   786  C  CE1  . TYR   A 1 87  ? -28.512 26.210  -35.837 1.00 49.74  ? 605  TYR   A CE1  1 
ATOM   787  C  CE2  . TYR   A 1 87  ? -29.850 27.966  -36.757 1.00 60.31  ? 605  TYR   A CE2  1 
ATOM   788  C  CZ   . TYR   A 1 87  ? -28.708 27.196  -36.782 1.00 56.54  ? 605  TYR   A CZ   1 
ATOM   789  O  OH   . TYR   A 1 87  ? -27.760 27.420  -37.753 1.00 60.11  ? 605  TYR   A OH   1 
ATOM   790  N  N    . GLY   A 1 88  ? -33.583 27.755  -31.196 1.00 47.45  ? 606  GLY   A N    1 
ATOM   791  C  CA   . GLY   A 1 88  ? -34.756 27.628  -30.360 1.00 45.08  ? 606  GLY   A CA   1 
ATOM   792  C  C    . GLY   A 1 88  ? -35.026 26.244  -29.816 1.00 43.88  ? 606  GLY   A C    1 
ATOM   793  O  O    . GLY   A 1 88  ? -36.030 26.061  -29.114 1.00 48.29  ? 606  GLY   A O    1 
ATOM   794  N  N    . LEU   A 1 89  ? -34.174 25.263  -30.111 1.00 36.41  ? 607  LEU   A N    1 
ATOM   795  C  CA   . LEU   A 1 89  ? -34.397 23.916  -29.596 1.00 37.81  ? 607  LEU   A CA   1 
ATOM   796  C  C    . LEU   A 1 89  ? -33.873 23.784  -28.170 1.00 39.76  ? 607  LEU   A C    1 
ATOM   797  O  O    . LEU   A 1 89  ? -34.617 23.417  -27.254 1.00 41.05  ? 607  LEU   A O    1 
ATOM   798  C  CB   . LEU   A 1 89  ? -33.744 22.890  -30.523 1.00 39.20  ? 607  LEU   A CB   1 
ATOM   799  C  CG   . LEU   A 1 89  ? -34.313 22.925  -31.943 1.00 47.00  ? 607  LEU   A CG   1 
ATOM   800  C  CD1  . LEU   A 1 89  ? -33.470 22.093  -32.883 1.00 49.04  ? 607  LEU   A CD1  1 
ATOM   801  C  CD2  . LEU   A 1 89  ? -35.761 22.455  -31.958 1.00 47.64  ? 607  LEU   A CD2  1 
ATOM   802  N  N    . PHE   A 1 90  ? -32.596 24.088  -27.963 1.00 39.85  ? 608  PHE   A N    1 
ATOM   803  C  CA   . PHE   A 1 90  ? -31.998 24.107  -26.637 1.00 41.26  ? 608  PHE   A CA   1 
ATOM   804  C  C    . PHE   A 1 90  ? -31.772 25.546  -26.194 1.00 45.07  ? 608  PHE   A C    1 
ATOM   805  O  O    . PHE   A 1 90  ? -31.652 26.457  -27.019 1.00 42.42  ? 608  PHE   A O    1 
ATOM   806  C  CB   . PHE   A 1 90  ? -30.673 23.336  -26.612 1.00 41.67  ? 608  PHE   A CB   1 
ATOM   807  C  CG   . PHE   A 1 90  ? -30.842 21.844  -26.654 1.00 42.16  ? 608  PHE   A CG   1 
ATOM   808  C  CD1  . PHE   A 1 90  ? -31.057 21.191  -27.856 1.00 43.83  ? 608  PHE   A CD1  1 
ATOM   809  C  CD2  . PHE   A 1 90  ? -30.799 21.096  -25.488 1.00 40.41  ? 608  PHE   A CD2  1 
ATOM   810  C  CE1  . PHE   A 1 90  ? -31.218 19.818  -27.897 1.00 39.18  ? 608  PHE   A CE1  1 
ATOM   811  C  CE2  . PHE   A 1 90  ? -30.961 19.725  -25.521 1.00 40.36  ? 608  PHE   A CE2  1 
ATOM   812  C  CZ   . PHE   A 1 90  ? -31.172 19.084  -26.729 1.00 39.36  ? 608  PHE   A CZ   1 
ATOM   813  N  N    . GLU   A 1 91  ? -31.727 25.744  -24.880 1.00 50.01  ? 609  GLU   A N    1 
ATOM   814  C  CA   . GLU   A 1 91  ? -31.477 27.054  -24.303 1.00 54.48  ? 609  GLU   A CA   1 
ATOM   815  C  C    . GLU   A 1 91  ? -30.584 26.894  -23.083 1.00 51.24  ? 609  GLU   A C    1 
ATOM   816  O  O    . GLU   A 1 91  ? -30.474 25.809  -22.507 1.00 50.20  ? 609  GLU   A O    1 
ATOM   817  C  CB   . GLU   A 1 91  ? -32.780 27.768  -23.913 1.00 58.80  ? 609  GLU   A CB   1 
ATOM   818  C  CG   . GLU   A 1 91  ? -33.380 27.299  -22.593 1.00 61.70  ? 609  GLU   A CG   1 
ATOM   819  C  CD   . GLU   A 1 91  ? -34.776 27.846  -22.357 1.00 66.69  ? 609  GLU   A CD   1 
ATOM   820  O  OE1  . GLU   A 1 91  ? -35.259 28.630  -23.201 1.00 68.06  ? 609  GLU   A OE1  1 
ATOM   821  O  OE2  . GLU   A 1 91  ? -35.391 27.490  -21.330 1.00 69.15  ? 609  GLU   A OE2  1 
ATOM   822  N  N    . TYR   A 1 92  ? -29.940 27.992  -22.698 1.00 48.06  ? 610  TYR   A N    1 
ATOM   823  C  CA   . TYR   A 1 92  ? -29.141 27.994  -21.482 1.00 48.79  ? 610  TYR   A CA   1 
ATOM   824  C  C    . TYR   A 1 92  ? -30.053 27.886  -20.267 1.00 49.07  ? 610  TYR   A C    1 
ATOM   825  O  O    . TYR   A 1 92  ? -31.076 28.573  -20.181 1.00 49.94  ? 610  TYR   A O    1 
ATOM   826  C  CB   . TYR   A 1 92  ? -28.291 29.259  -21.406 1.00 52.03  ? 610  TYR   A CB   1 
ATOM   827  C  CG   . TYR   A 1 92  ? -27.183 29.301  -22.432 1.00 52.66  ? 610  TYR   A CG   1 
ATOM   828  C  CD1  . TYR   A 1 92  ? -26.143 28.382  -22.396 1.00 54.00  ? 610  TYR   A CD1  1 
ATOM   829  C  CD2  . TYR   A 1 92  ? -27.182 30.255  -23.442 1.00 51.09  ? 610  TYR   A CD2  1 
ATOM   830  C  CE1  . TYR   A 1 92  ? -25.129 28.414  -23.334 1.00 57.50  ? 610  TYR   A CE1  1 
ATOM   831  C  CE2  . TYR   A 1 92  ? -26.174 30.295  -24.384 1.00 54.34  ? 610  TYR   A CE2  1 
ATOM   832  C  CZ   . TYR   A 1 92  ? -25.150 29.374  -24.326 1.00 59.65  ? 610  TYR   A CZ   1 
ATOM   833  O  OH   . TYR   A 1 92  ? -24.144 29.411  -25.262 1.00 64.77  ? 610  TYR   A OH   1 
ATOM   834  N  N    . SER   A 1 93  ? -29.679 27.016  -19.327 1.00 46.04  ? 611  SER   A N    1 
ATOM   835  C  CA   . SER   A 1 93  ? -30.518 26.758  -18.162 1.00 48.56  ? 611  SER   A CA   1 
ATOM   836  C  C    . SER   A 1 93  ? -30.702 27.989  -17.288 1.00 55.75  ? 611  SER   A C    1 
ATOM   837  O  O    . SER   A 1 93  ? -31.661 28.044  -16.510 1.00 64.28  ? 611  SER   A O    1 
ATOM   838  C  CB   . SER   A 1 93  ? -29.919 25.626  -17.332 1.00 46.86  ? 611  SER   A CB   1 
ATOM   839  O  OG   . SER   A 1 93  ? -28.571 25.903  -16.996 1.00 45.96  ? 611  SER   A OG   1 
ATOM   840  N  N    . ALA   A 1 94  ? -29.806 28.966  -17.389 1.00 55.21  ? 612  ALA   A N    1 
ATOM   841  C  CA   . ALA   A 1 94  ? -29.898 30.207  -16.633 1.00 58.54  ? 612  ALA   A CA   1 
ATOM   842  C  C    . ALA   A 1 94  ? -28.911 31.193  -17.236 1.00 60.09  ? 612  ALA   A C    1 
ATOM   843  O  O    . ALA   A 1 94  ? -27.952 30.799  -17.907 1.00 55.61  ? 612  ALA   A O    1 
ATOM   844  C  CB   . ALA   A 1 94  ? -29.609 29.995  -15.143 1.00 61.28  ? 612  ALA   A CB   1 
ATOM   845  N  N    . THR   A 1 95  ? -29.158 32.482  -16.987 1.00 61.06  ? 613  THR   A N    1 
ATOM   846  C  CA   . THR   A 1 95  ? -28.280 33.515  -17.526 1.00 65.29  ? 613  THR   A CA   1 
ATOM   847  C  C    . THR   A 1 95  ? -26.841 33.330  -17.062 1.00 60.99  ? 613  THR   A C    1 
ATOM   848  O  O    . THR   A 1 95  ? -25.907 33.621  -17.817 1.00 58.88  ? 613  THR   A O    1 
ATOM   849  C  CB   . THR   A 1 95  ? -28.790 34.905  -17.135 1.00 71.92  ? 613  THR   A CB   1 
ATOM   850  O  OG1  . THR   A 1 95  ? -28.648 35.092  -15.722 1.00 79.00  ? 613  THR   A OG1  1 
ATOM   851  C  CG2  . THR   A 1 95  ? -30.253 35.067  -17.525 1.00 67.57  ? 613  THR   A CG2  1 
ATOM   852  N  N    . ASP   A 1 96  ? -26.639 32.833  -15.842 1.00 62.42  ? 614  ASP   A N    1 
ATOM   853  C  CA   . ASP   A 1 96  ? -25.298 32.619  -15.313 1.00 67.02  ? 614  ASP   A CA   1 
ATOM   854  C  C    . ASP   A 1 96  ? -24.750 31.222  -15.590 1.00 61.97  ? 614  ASP   A C    1 
ATOM   855  O  O    . ASP   A 1 96  ? -23.576 30.970  -15.297 1.00 61.37  ? 614  ASP   A O    1 
ATOM   856  C  CB   . ASP   A 1 96  ? -25.277 32.884  -13.803 1.00 76.89  ? 614  ASP   A CB   1 
ATOM   857  C  CG   . ASP   A 1 96  ? -25.456 34.353  -13.465 1.00 89.95  ? 614  ASP   A CG   1 
ATOM   858  O  OD1  . ASP   A 1 96  ? -24.919 35.206  -14.203 1.00 93.75  ? 614  ASP   A OD1  1 
ATOM   859  O  OD2  . ASP   A 1 96  ? -26.128 34.656  -12.456 1.00 95.13  ? 614  ASP   A OD2  1 
ATOM   860  N  N    . ASN   A 1 97  ? -25.554 30.316  -16.139 1.00 56.56  ? 615  ASN   A N    1 
ATOM   861  C  CA   . ASN   A 1 97  ? -25.108 28.969  -16.464 1.00 57.32  ? 615  ASN   A CA   1 
ATOM   862  C  C    . ASN   A 1 97  ? -24.762 28.853  -17.944 1.00 57.88  ? 615  ASN   A C    1 
ATOM   863  O  O    . ASN   A 1 97  ? -25.274 29.590  -18.788 1.00 57.80  ? 615  ASN   A O    1 
ATOM   864  C  CB   . ASN   A 1 97  ? -26.180 27.929  -16.119 1.00 58.09  ? 615  ASN   A CB   1 
ATOM   865  C  CG   . ASN   A 1 97  ? -26.481 27.863  -14.638 1.00 61.68  ? 615  ASN   A CG   1 
ATOM   866  O  OD1  . ASN   A 1 97  ? -25.817 28.505  -13.825 1.00 63.55  ? 615  ASN   A OD1  1 
ATOM   867  N  ND2  . ASN   A 1 97  ? -27.486 27.071  -14.276 1.00 58.72  ? 615  ASN   A ND2  1 
ATOM   868  N  N    . TYR   A 1 98  ? -23.887 27.897  -18.250 1.00 56.00  ? 616  TYR   A N    1 
ATOM   869  C  CA   . TYR   A 1 98  ? -23.598 27.523  -19.626 1.00 58.48  ? 616  TYR   A CA   1 
ATOM   870  C  C    . TYR   A 1 98  ? -24.163 26.157  -19.992 1.00 51.85  ? 616  TYR   A C    1 
ATOM   871  O  O    . TYR   A 1 98  ? -24.092 25.768  -21.163 1.00 53.10  ? 616  TYR   A O    1 
ATOM   872  C  CB   . TYR   A 1 98  ? -22.081 27.549  -19.873 1.00 68.43  ? 616  TYR   A CB   1 
ATOM   873  C  CG   . TYR   A 1 98  ? -21.651 27.747  -21.318 1.00 81.65  ? 616  TYR   A CG   1 
ATOM   874  C  CD1  . TYR   A 1 98  ? -21.073 26.713  -22.024 1.00 84.24  ? 616  TYR   A CD1  1 
ATOM   875  C  CD2  . TYR   A 1 98  ? -21.799 28.965  -21.965 1.00 91.22  ? 616  TYR   A CD2  1 
ATOM   876  C  CE1  . TYR   A 1 98  ? -20.660 26.853  -23.322 1.00 86.69  ? 616  TYR   A CE1  1 
ATOM   877  C  CE2  . TYR   A 1 98  ? -21.386 29.123  -23.286 1.00 94.12  ? 616  TYR   A CE2  1 
ATOM   878  C  CZ   . TYR   A 1 98  ? -20.815 28.055  -23.954 1.00 91.76  ? 616  TYR   A CZ   1 
ATOM   879  O  OH   . TYR   A 1 98  ? -20.395 28.174  -25.257 1.00 93.92  ? 616  TYR   A OH   1 
ATOM   880  N  N    . THR   A 1 99  ? -24.724 25.427  -19.028 1.00 47.51  ? 617  THR   A N    1 
ATOM   881  C  CA   . THR   A 1 99  ? -25.388 24.163  -19.315 1.00 43.60  ? 617  THR   A CA   1 
ATOM   882  C  C    . THR   A 1 99  ? -26.683 24.401  -20.083 1.00 42.06  ? 617  THR   A C    1 
ATOM   883  O  O    . THR   A 1 99  ? -27.325 25.448  -19.958 1.00 43.26  ? 617  THR   A O    1 
ATOM   884  C  CB   . THR   A 1 99  ? -25.695 23.409  -18.022 1.00 46.14  ? 617  THR   A CB   1 
ATOM   885  O  OG1  . THR   A 1 99  ? -26.290 24.306  -17.076 1.00 42.99  ? 617  THR   A OG1  1 
ATOM   886  C  CG2  . THR   A 1 99  ? -24.423 22.819  -17.427 1.00 51.76  ? 617  THR   A CG2  1 
ATOM   887  N  N    . LEU   A 1 100 ? -27.075 23.405  -20.869 1.00 41.31  ? 618  LEU   A N    1 
ATOM   888  C  CA   . LEU   A 1 100 ? -28.226 23.511  -21.750 1.00 44.04  ? 618  LEU   A CA   1 
ATOM   889  C  C    . LEU   A 1 100 ? -29.396 22.686  -21.231 1.00 45.19  ? 618  LEU   A C    1 
ATOM   890  O  O    . LEU   A 1 100 ? -29.218 21.650  -20.583 1.00 40.76  ? 618  LEU   A O    1 
ATOM   891  C  CB   . LEU   A 1 100 ? -27.872 23.058  -23.169 1.00 42.32  ? 618  LEU   A CB   1 
ATOM   892  C  CG   . LEU   A 1 100 ? -26.770 23.860  -23.861 1.00 46.10  ? 618  LEU   A CG   1 
ATOM   893  C  CD1  . LEU   A 1 100 ? -26.402 23.223  -25.188 1.00 46.94  ? 618  LEU   A CD1  1 
ATOM   894  C  CD2  . LEU   A 1 100 ? -27.202 25.306  -24.056 1.00 46.58  ? 618  LEU   A CD2  1 
ATOM   895  N  N    . GLN   A 1 101 ? -30.599 23.172  -21.523 1.00 44.96  ? 619  GLN   A N    1 
ATOM   896  C  CA   . GLN   A 1 101 ? -31.836 22.443  -21.301 1.00 40.60  ? 619  GLN   A CA   1 
ATOM   897  C  C    . GLN   A 1 101 ? -32.696 22.577  -22.549 1.00 41.81  ? 619  GLN   A C    1 
ATOM   898  O  O    . GLN   A 1 101 ? -32.450 23.429  -23.406 1.00 43.67  ? 619  GLN   A O    1 
ATOM   899  C  CB   . GLN   A 1 101 ? -32.594 22.968  -20.073 1.00 40.36  ? 619  GLN   A CB   1 
ATOM   900  C  CG   . GLN   A 1 101 ? -33.149 24.375  -20.249 1.00 47.20  ? 619  GLN   A CG   1 
ATOM   901  C  CD   . GLN   A 1 101 ? -33.792 24.920  -18.987 1.00 53.82  ? 619  GLN   A CD   1 
ATOM   902  O  OE1  . GLN   A 1 101 ? -33.406 24.564  -17.873 1.00 55.67  ? 619  GLN   A OE1  1 
ATOM   903  N  NE2  . GLN   A 1 101 ? -34.778 25.792  -19.157 1.00 58.49  ? 619  GLN   A NE2  1 
ATOM   904  N  N    . ILE   A 1 102 ? -33.709 21.719  -22.656 1.00 38.08  ? 620  ILE   A N    1 
ATOM   905  C  CA   . ILE   A 1 102 ? -34.646 21.831  -23.765 1.00 36.93  ? 620  ILE   A CA   1 
ATOM   906  C  C    . ILE   A 1 102 ? -35.505 23.071  -23.566 1.00 37.79  ? 620  ILE   A C    1 
ATOM   907  O  O    . ILE   A 1 102 ? -35.997 23.337  -22.461 1.00 39.73  ? 620  ILE   A O    1 
ATOM   908  C  CB   . ILE   A 1 102 ? -35.503 20.562  -23.883 1.00 37.33  ? 620  ILE   A CB   1 
ATOM   909  C  CG1  . ILE   A 1 102 ? -34.639 19.377  -24.328 1.00 36.94  ? 620  ILE   A CG1  1 
ATOM   910  C  CG2  . ILE   A 1 102 ? -36.665 20.781  -24.851 1.00 35.55  ? 620  ILE   A CG2  1 
ATOM   911  C  CD1  . ILE   A 1 102 ? -35.388 18.061  -24.389 1.00 38.92  ? 620  ILE   A CD1  1 
ATOM   912  N  N    . ASN   A 1 103 ? -35.669 23.849  -24.627 1.00 36.48  ? 621  ASN   A N    1 
ATOM   913  C  CA   . ASN   A 1 103 ? -36.522 25.031  -24.577 1.00 41.13  ? 621  ASN   A CA   1 
ATOM   914  C  C    . ASN   A 1 103 ? -37.982 24.601  -24.525 1.00 45.68  ? 621  ASN   A C    1 
ATOM   915  O  O    . ASN   A 1 103 ? -38.436 23.881  -25.423 1.00 49.57  ? 621  ASN   A O    1 
ATOM   916  C  CB   . ASN   A 1 103 ? -36.261 25.911  -25.800 1.00 42.74  ? 621  ASN   A CB   1 
ATOM   917  C  CG   . ASN   A 1 103 ? -37.013 27.235  -25.756 1.00 51.13  ? 621  ASN   A CG   1 
ATOM   918  O  OD1  . ASN   A 1 103 ? -37.899 27.445  -24.927 1.00 54.89  ? 621  ASN   A OD1  1 
ATOM   919  N  ND2  . ASN   A 1 103 ? -36.658 28.137  -26.664 1.00 54.83  ? 621  ASN   A ND2  1 
ATOM   920  N  N    . PRO   A 1 104 ? -38.748 24.999  -23.505 1.00 52.43  ? 622  PRO   A N    1 
ATOM   921  C  CA   . PRO   A 1 104 ? -40.185 24.679  -23.511 1.00 57.74  ? 622  PRO   A CA   1 
ATOM   922  C  C    . PRO   A 1 104 ? -40.921 25.245  -24.712 1.00 60.52  ? 622  PRO   A C    1 
ATOM   923  O  O    . PRO   A 1 104 ? -41.838 24.595  -25.228 1.00 65.90  ? 622  PRO   A O    1 
ATOM   924  C  CB   . PRO   A 1 104 ? -40.689 25.292  -22.195 1.00 59.87  ? 622  PRO   A CB   1 
ATOM   925  C  CG   . PRO   A 1 104 ? -39.615 26.251  -21.765 1.00 58.51  ? 622  PRO   A CG   1 
ATOM   926  C  CD   . PRO   A 1 104 ? -38.335 25.672  -22.264 1.00 53.96  ? 622  PRO   A CD   1 
ATOM   927  N  N    . ASN   A 1 105 ? -40.540 26.434  -25.184 1.00 58.81  ? 623  ASN   A N    1 
ATOM   928  C  CA   . ASN   A 1 105 ? -41.154 27.051  -26.354 1.00 58.59  ? 623  ASN   A CA   1 
ATOM   929  C  C    . ASN   A 1 105 ? -40.507 26.601  -27.657 1.00 52.15  ? 623  ASN   A C    1 
ATOM   930  O  O    . ASN   A 1 105 ? -40.562 27.333  -28.656 1.00 51.34  ? 623  ASN   A O    1 
ATOM   931  C  CB   . ASN   A 1 105 ? -41.099 28.574  -26.232 1.00 62.05  ? 623  ASN   A CB   1 
ATOM   932  C  CG   . ASN   A 1 105 ? -41.704 29.076  -24.937 1.00 69.12  ? 623  ASN   A CG   1 
ATOM   933  O  OD1  . ASN   A 1 105 ? -42.760 28.608  -24.510 1.00 72.06  ? 623  ASN   A OD1  1 
ATOM   934  N  ND2  . ASN   A 1 105 ? -41.032 30.028  -24.299 1.00 72.67  ? 623  ASN   A ND2  1 
ATOM   935  N  N    . SER   A 1 106 ? -39.904 25.407  -27.671 1.00 44.23  ? 624  SER   A N    1 
ATOM   936  C  CA   A SER   A 1 106 ? -39.200 24.938  -28.860 0.41 41.84  ? 624  SER   A CA   1 
ATOM   937  C  CA   B SER   A 1 106 ? -39.202 24.932  -28.859 0.59 42.02  ? 624  SER   A CA   1 
ATOM   938  C  C    . SER   A 1 106 ? -40.110 24.886  -30.080 1.00 44.91  ? 624  SER   A C    1 
ATOM   939  O  O    . SER   A 1 106 ? -39.651 25.119  -31.204 1.00 48.42  ? 624  SER   A O    1 
ATOM   940  C  CB   A SER   A 1 106 ? -38.591 23.561  -28.595 0.41 38.20  ? 624  SER   A CB   1 
ATOM   941  C  CB   B SER   A 1 106 ? -38.608 23.547  -28.598 0.59 38.08  ? 624  SER   A CB   1 
ATOM   942  O  OG   A SER   A 1 106 ? -38.492 22.811  -29.791 0.41 35.90  ? 624  SER   A OG   1 
ATOM   943  O  OG   B SER   A 1 106 ? -39.628 22.602  -28.321 0.59 37.48  ? 624  SER   A OG   1 
ATOM   944  N  N    . GLY   A 1 107 ? -41.396 24.584  -29.886 1.00 47.96  ? 625  GLY   A N    1 
ATOM   945  C  CA   . GLY   A 1 107 ? -42.304 24.472  -31.013 1.00 51.16  ? 625  GLY   A CA   1 
ATOM   946  C  C    . GLY   A 1 107 ? -42.771 25.788  -31.594 1.00 52.34  ? 625  GLY   A C    1 
ATOM   947  O  O    . GLY   A 1 107 ? -43.221 25.814  -32.744 1.00 55.90  ? 625  GLY   A O    1 
ATOM   948  N  N    . LEU   A 1 108 ? -42.665 26.880  -30.831 1.00 53.43  ? 626  LEU   A N    1 
ATOM   949  C  CA   . LEU   A 1 108 ? -43.227 28.156  -31.267 1.00 60.26  ? 626  LEU   A CA   1 
ATOM   950  C  C    . LEU   A 1 108 ? -42.678 28.579  -32.623 1.00 66.73  ? 626  LEU   A C    1 
ATOM   951  O  O    . LEU   A 1 108 ? -43.430 29.044  -33.488 1.00 70.76  ? 626  LEU   A O    1 
ATOM   952  C  CB   . LEU   A 1 108 ? -42.957 29.234  -30.220 1.00 61.58  ? 626  LEU   A CB   1 
ATOM   953  C  CG   . LEU   A 1 108 ? -44.168 29.608  -29.364 1.00 67.08  ? 626  LEU   A CG   1 
ATOM   954  C  CD1  . LEU   A 1 108 ? -43.764 30.496  -28.198 1.00 69.44  ? 626  LEU   A CD1  1 
ATOM   955  C  CD2  . LEU   A 1 108 ? -45.223 30.284  -30.219 1.00 65.02  ? 626  LEU   A CD2  1 
ATOM   956  N  N    . CYS   A 1 109 ? -41.373 28.420  -32.835 1.00 72.83  ? 627  CYS   A N    1 
ATOM   957  C  CA   . CYS   A 1 109 ? -40.774 28.787  -34.109 1.00 83.21  ? 627  CYS   A CA   1 
ATOM   958  C  C    . CYS   A 1 109 ? -40.437 27.592  -34.983 1.00 75.90  ? 627  CYS   A C    1 
ATOM   959  O  O    . CYS   A 1 109 ? -40.243 27.763  -36.192 1.00 76.84  ? 627  CYS   A O    1 
ATOM   960  C  CB   . CYS   A 1 109 ? -39.508 29.619  -33.883 1.00 98.38  ? 627  CYS   A CB   1 
ATOM   961  S  SG   . CYS   A 1 109 ? -38.025 28.665  -33.558 1.00 107.50 ? 627  CYS   A SG   1 
ATOM   962  N  N    . ASN   A 1 110 ? -40.367 26.399  -34.408 1.00 68.29  ? 628  ASN   A N    1 
ATOM   963  C  CA   . ASN   A 1 110 ? -40.098 25.171  -35.146 1.00 60.88  ? 628  ASN   A CA   1 
ATOM   964  C  C    . ASN   A 1 110 ? -41.339 24.293  -35.026 1.00 58.10  ? 628  ASN   A C    1 
ATOM   965  O  O    . ASN   A 1 110 ? -41.474 23.508  -34.088 1.00 57.98  ? 628  ASN   A O    1 
ATOM   966  C  CB   . ASN   A 1 110 ? -38.855 24.474  -34.607 1.00 56.32  ? 628  ASN   A CB   1 
ATOM   967  C  CG   . ASN   A 1 110 ? -37.735 25.443  -34.305 1.00 56.99  ? 628  ASN   A CG   1 
ATOM   968  O  OD1  . ASN   A 1 110 ? -37.147 26.026  -35.212 1.00 60.33  ? 628  ASN   A OD1  1 
ATOM   969  N  ND2  . ASN   A 1 110 ? -37.441 25.633  -33.024 1.00 55.06  ? 628  ASN   A ND2  1 
ATOM   970  N  N    . GLU   A 1 111 ? -42.261 24.450  -35.979 1.00 57.21  ? 629  GLU   A N    1 
ATOM   971  C  CA   . GLU   A 1 111 ? -43.433 23.582  -36.016 1.00 62.85  ? 629  GLU   A CA   1 
ATOM   972  C  C    . GLU   A 1 111 ? -43.018 22.118  -36.094 1.00 61.97  ? 629  GLU   A C    1 
ATOM   973  O  O    . GLU   A 1 111 ? -43.642 21.251  -35.470 1.00 62.10  ? 629  GLU   A O    1 
ATOM   974  C  CB   . GLU   A 1 111 ? -44.326 23.958  -37.200 1.00 70.58  ? 629  GLU   A CB   1 
ATOM   975  C  CG   . GLU   A 1 111 ? -45.595 23.129  -37.316 1.00 81.20  ? 629  GLU   A CG   1 
ATOM   976  C  CD   . GLU   A 1 111 ? -46.758 23.909  -37.900 1.00 92.75  ? 629  GLU   A CD   1 
ATOM   977  O  OE1  . GLU   A 1 111 ? -47.133 23.636  -39.061 1.00 96.49  ? 629  GLU   A OE1  1 
ATOM   978  O  OE2  . GLU   A 1 111 ? -47.303 24.787  -37.199 1.00 97.18  ? 629  GLU   A OE2  1 
ATOM   979  N  N    . ASP   A 1 112 ? -41.948 21.829  -36.837 1.00 62.43  ? 630  ASP   A N    1 
ATOM   980  C  CA   . ASP   A 1 112 ? -41.412 20.480  -36.977 1.00 66.07  ? 630  ASP   A CA   1 
ATOM   981  C  C    . ASP   A 1 112 ? -40.347 20.159  -35.932 1.00 61.34  ? 630  ASP   A C    1 
ATOM   982  O  O    . ASP   A 1 112 ? -39.435 19.367  -36.207 1.00 58.37  ? 630  ASP   A O    1 
ATOM   983  C  CB   . ASP   A 1 112 ? -40.848 20.294  -38.387 1.00 73.91  ? 630  ASP   A CB   1 
ATOM   984  C  CG   . ASP   A 1 112 ? -40.826 18.843  -38.823 1.00 82.29  ? 630  ASP   A CG   1 
ATOM   985  O  OD1  . ASP   A 1 112 ? -41.514 18.018  -38.187 1.00 85.50  ? 630  ASP   A OD1  1 
ATOM   986  O  OD2  . ASP   A 1 112 ? -40.118 18.526  -39.802 1.00 84.87  ? 630  ASP   A OD2  1 
ATOM   987  N  N    . HIS   A 1 113 ? -40.441 20.743  -34.733 1.00 59.37  ? 631  HIS   A N    1 
ATOM   988  C  CA   . HIS   A 1 113 ? -39.359 20.601  -33.762 1.00 51.74  ? 631  HIS   A CA   1 
ATOM   989  C  C    . HIS   A 1 113 ? -39.195 19.162  -33.287 1.00 42.17  ? 631  HIS   A C    1 
ATOM   990  O  O    . HIS   A 1 113 ? -38.084 18.754  -32.934 1.00 41.44  ? 631  HIS   A O    1 
ATOM   991  C  CB   . HIS   A 1 113 ? -39.582 21.537  -32.569 1.00 54.93  ? 631  HIS   A CB   1 
ATOM   992  C  CG   . HIS   A 1 113 ? -40.789 21.208  -31.744 1.00 56.03  ? 631  HIS   A CG   1 
ATOM   993  N  ND1  . HIS   A 1 113 ? -40.804 21.332  -30.371 1.00 56.82  ? 631  HIS   A ND1  1 
ATOM   994  C  CD2  . HIS   A 1 113 ? -42.025 20.782  -32.095 1.00 59.23  ? 631  HIS   A CD2  1 
ATOM   995  C  CE1  . HIS   A 1 113 ? -41.993 20.986  -29.912 1.00 59.04  ? 631  HIS   A CE1  1 
ATOM   996  N  NE2  . HIS   A 1 113 ? -42.753 20.648  -30.937 1.00 58.17  ? 631  HIS   A NE2  1 
ATOM   997  N  N    . LEU   A 1 114 ? -40.271 18.373  -33.287 1.00 42.72  ? 632  LEU   A N    1 
ATOM   998  C  CA   . LEU   A 1 114 ? -40.170 17.018  -32.753 1.00 41.36  ? 632  LEU   A CA   1 
ATOM   999  C  C    . LEU   A 1 114 ? -39.286 16.133  -33.626 1.00 42.33  ? 632  LEU   A C    1 
ATOM   1000 O  O    . LEU   A 1 114 ? -38.556 15.279  -33.109 1.00 41.90  ? 632  LEU   A O    1 
ATOM   1001 C  CB   . LEU   A 1 114 ? -41.561 16.408  -32.589 1.00 38.17  ? 632  LEU   A CB   1 
ATOM   1002 C  CG   . LEU   A 1 114 ? -42.392 17.015  -31.453 1.00 47.66  ? 632  LEU   A CG   1 
ATOM   1003 C  CD1  . LEU   A 1 114 ? -43.559 16.110  -31.086 1.00 51.01  ? 632  LEU   A CD1  1 
ATOM   1004 C  CD2  . LEU   A 1 114 ? -41.527 17.305  -30.232 1.00 44.11  ? 632  LEU   A CD2  1 
ATOM   1005 N  N    . SER   A 1 115 ? -39.328 16.318  -34.947 1.00 44.70  ? 633  SER   A N    1 
ATOM   1006 C  CA   . SER   A 1 115 ? -38.411 15.570  -35.801 1.00 47.69  ? 633  SER   A CA   1 
ATOM   1007 C  C    . SER   A 1 115 ? -36.985 16.095  -35.678 1.00 43.63  ? 633  SER   A C    1 
ATOM   1008 O  O    . SER   A 1 115 ? -36.028 15.339  -35.883 1.00 38.81  ? 633  SER   A O    1 
ATOM   1009 C  CB   . SER   A 1 115 ? -38.878 15.612  -37.257 1.00 56.68  ? 633  SER   A CB   1 
ATOM   1010 O  OG   . SER   A 1 115 ? -38.706 16.900  -37.817 1.00 65.92  ? 633  SER   A OG   1 
ATOM   1011 N  N    . TYR   A 1 116 ? -36.820 17.377  -35.338 1.00 41.24  ? 634  TYR   A N    1 
ATOM   1012 C  CA   . TYR   A 1 116 ? -35.482 17.900  -35.076 1.00 41.71  ? 634  TYR   A CA   1 
ATOM   1013 C  C    . TYR   A 1 116 ? -34.865 17.225  -33.859 1.00 37.94  ? 634  TYR   A C    1 
ATOM   1014 O  O    . TYR   A 1 116 ? -33.678 16.877  -33.866 1.00 36.08  ? 634  TYR   A O    1 
ATOM   1015 C  CB   . TYR   A 1 116 ? -35.523 19.414  -34.863 1.00 44.19  ? 634  TYR   A CB   1 
ATOM   1016 C  CG   . TYR   A 1 116 ? -36.019 20.230  -36.037 1.00 46.98  ? 634  TYR   A CG   1 
ATOM   1017 C  CD1  . TYR   A 1 116 ? -36.182 19.663  -37.294 1.00 50.36  ? 634  TYR   A CD1  1 
ATOM   1018 C  CD2  . TYR   A 1 116 ? -36.315 21.578  -35.884 1.00 44.63  ? 634  TYR   A CD2  1 
ATOM   1019 C  CE1  . TYR   A 1 116 ? -36.635 20.415  -38.362 1.00 56.09  ? 634  TYR   A CE1  1 
ATOM   1020 C  CE2  . TYR   A 1 116 ? -36.766 22.337  -36.944 1.00 48.73  ? 634  TYR   A CE2  1 
ATOM   1021 C  CZ   . TYR   A 1 116 ? -36.924 21.752  -38.180 1.00 54.12  ? 634  TYR   A CZ   1 
ATOM   1022 O  OH   . TYR   A 1 116 ? -37.374 22.509  -39.238 1.00 57.09  ? 634  TYR   A OH   1 
ATOM   1023 N  N    . PHE   A 1 117 ? -35.656 17.034  -32.802 1.00 35.59  ? 635  PHE   A N    1 
ATOM   1024 C  CA   . PHE   A 1 117 ? -35.135 16.404  -31.594 1.00 38.70  ? 635  PHE   A CA   1 
ATOM   1025 C  C    . PHE   A 1 117 ? -34.809 14.935  -31.833 1.00 40.66  ? 635  PHE   A C    1 
ATOM   1026 O  O    . PHE   A 1 117 ? -33.818 14.420  -31.303 1.00 34.68  ? 635  PHE   A O    1 
ATOM   1027 C  CB   . PHE   A 1 117 ? -36.135 16.565  -30.450 1.00 35.54  ? 635  PHE   A CB   1 
ATOM   1028 C  CG   . PHE   A 1 117 ? -36.095 17.918  -29.807 1.00 35.88  ? 635  PHE   A CG   1 
ATOM   1029 C  CD1  . PHE   A 1 117 ? -35.019 18.293  -29.017 1.00 35.70  ? 635  PHE   A CD1  1 
ATOM   1030 C  CD2  . PHE   A 1 117 ? -37.121 18.826  -30.006 1.00 34.94  ? 635  PHE   A CD2  1 
ATOM   1031 C  CE1  . PHE   A 1 117 ? -34.974 19.545  -28.428 1.00 33.51  ? 635  PHE   A CE1  1 
ATOM   1032 C  CE2  . PHE   A 1 117 ? -37.078 20.079  -29.423 1.00 37.62  ? 635  PHE   A CE2  1 
ATOM   1033 C  CZ   . PHE   A 1 117 ? -36.006 20.437  -28.630 1.00 32.67  ? 635  PHE   A CZ   1 
ATOM   1034 N  N    . LYS   A 1 118 ? -35.632 14.243  -32.627 1.00 40.02  ? 636  LYS   A N    1 
ATOM   1035 C  CA   . LYS   A 1 118 ? -35.295 12.877  -33.010 1.00 39.77  ? 636  LYS   A CA   1 
ATOM   1036 C  C    . LYS   A 1 118 ? -33.985 12.838  -33.785 1.00 40.66  ? 636  LYS   A C    1 
ATOM   1037 O  O    . LYS   A 1 118 ? -33.176 11.920  -33.610 1.00 39.45  ? 636  LYS   A O    1 
ATOM   1038 C  CB   . LYS   A 1 118 ? -36.425 12.261  -33.833 1.00 42.17  ? 636  LYS   A CB   1 
ATOM   1039 C  CG   . LYS   A 1 118 ? -36.117 10.858  -34.338 1.00 46.76  ? 636  LYS   A CG   1 
ATOM   1040 C  CD   . LYS   A 1 118 ? -37.381 10.100  -34.699 1.00 54.27  ? 636  LYS   A CD   1 
ATOM   1041 C  CE   . LYS   A 1 118 ? -37.050 8.747   -35.307 1.00 57.19  ? 636  LYS   A CE   1 
ATOM   1042 N  NZ   . LYS   A 1 118 ? -38.271 8.028   -35.765 1.00 58.43  ? 636  LYS   A NZ   1 
ATOM   1043 N  N    . PHE   A 1 119 ? -33.757 13.835  -34.644 1.00 38.66  ? 637  PHE   A N    1 
ATOM   1044 C  CA   . PHE   A 1 119 ? -32.486 13.920  -35.355 1.00 39.59  ? 637  PHE   A CA   1 
ATOM   1045 C  C    . PHE   A 1 119 ? -31.330 14.120  -34.384 1.00 37.53  ? 637  PHE   A C    1 
ATOM   1046 O  O    . PHE   A 1 119 ? -30.285 13.469  -34.502 1.00 37.52  ? 637  PHE   A O    1 
ATOM   1047 C  CB   . PHE   A 1 119 ? -32.526 15.052  -36.380 1.00 38.52  ? 637  PHE   A CB   1 
ATOM   1048 C  CG   . PHE   A 1 119 ? -31.166 15.484  -36.851 1.00 37.41  ? 637  PHE   A CG   1 
ATOM   1049 C  CD1  . PHE   A 1 119 ? -30.419 14.670  -37.685 1.00 39.73  ? 637  PHE   A CD1  1 
ATOM   1050 C  CD2  . PHE   A 1 119 ? -30.633 16.700  -36.456 1.00 38.77  ? 637  PHE   A CD2  1 
ATOM   1051 C  CE1  . PHE   A 1 119 ? -29.166 15.060  -38.118 1.00 43.21  ? 637  PHE   A CE1  1 
ATOM   1052 C  CE2  . PHE   A 1 119 ? -29.381 17.096  -36.886 1.00 41.73  ? 637  PHE   A CE2  1 
ATOM   1053 C  CZ   . PHE   A 1 119 ? -28.647 16.274  -37.719 1.00 41.42  ? 637  PHE   A CZ   1 
ATOM   1054 N  N    . ILE   A 1 120 ? -31.499 15.027  -33.416 1.00 35.02  ? 638  ILE   A N    1 
ATOM   1055 C  CA   . ILE   A 1 120 ? -30.455 15.243  -32.418 1.00 37.32  ? 638  ILE   A CA   1 
ATOM   1056 C  C    . ILE   A 1 120 ? -30.204 13.963  -31.632 1.00 32.30  ? 638  ILE   A C    1 
ATOM   1057 O  O    . ILE   A 1 120 ? -29.057 13.630  -31.308 1.00 32.54  ? 638  ILE   A O    1 
ATOM   1058 C  CB   . ILE   A 1 120 ? -30.824 16.415  -31.489 1.00 36.31  ? 638  ILE   A CB   1 
ATOM   1059 C  CG1  . ILE   A 1 120 ? -31.094 17.683  -32.301 1.00 40.50  ? 638  ILE   A CG1  1 
ATOM   1060 C  CG2  . ILE   A 1 120 ? -29.707 16.670  -30.488 1.00 29.56  ? 638  ILE   A CG2  1 
ATOM   1061 C  CD1  . ILE   A 1 120 ? -31.507 18.870  -31.459 1.00 41.73  ? 638  ILE   A CD1  1 
ATOM   1062 N  N    . GLY   A 1 121 ? -31.270 13.222  -31.322 1.00 33.41  ? 639  GLY   A N    1 
ATOM   1063 C  CA   . GLY   A 1 121 ? -31.098 11.950  -30.639 1.00 37.06  ? 639  GLY   A CA   1 
ATOM   1064 C  C    . GLY   A 1 121 ? -30.281 10.961  -31.448 1.00 38.80  ? 639  GLY   A C    1 
ATOM   1065 O  O    . GLY   A 1 121 ? -29.397 10.284  -30.916 1.00 40.35  ? 639  GLY   A O    1 
ATOM   1066 N  N    . ARG   A 1 122 ? -30.566 10.864  -32.751 1.00 38.02  ? 640  ARG   A N    1 
ATOM   1067 C  CA   . ARG   A 1 122 ? -29.798 9.969   -33.612 1.00 37.09  ? 640  ARG   A CA   1 
ATOM   1068 C  C    . ARG   A 1 122 ? -28.326 10.361  -33.648 1.00 39.43  ? 640  ARG   A C    1 
ATOM   1069 O  O    . ARG   A 1 122 ? -27.445 9.496   -33.580 1.00 42.06  ? 640  ARG   A O    1 
ATOM   1070 C  CB   . ARG   A 1 122 ? -30.384 9.959   -35.025 1.00 34.20  ? 640  ARG   A CB   1 
ATOM   1071 C  CG   . ARG   A 1 122 ? -31.688 9.188   -35.157 1.00 35.05  ? 640  ARG   A CG   1 
ATOM   1072 C  CD   . ARG   A 1 122 ? -32.126 9.072   -36.611 1.00 39.42  ? 640  ARG   A CD   1 
ATOM   1073 N  NE   . ARG   A 1 122 ? -33.275 8.185   -36.764 1.00 44.66  ? 640  ARG   A NE   1 
ATOM   1074 C  CZ   . ARG   A 1 122 ? -33.752 7.768   -37.933 1.00 47.09  ? 640  ARG   A CZ   1 
ATOM   1075 N  NH1  . ARG   A 1 122 ? -33.181 8.157   -39.064 1.00 46.87  ? 640  ARG   A NH1  1 
ATOM   1076 N  NH2  . ARG   A 1 122 ? -34.805 6.961   -37.972 1.00 45.44  ? 640  ARG   A NH2  1 
ATOM   1077 N  N    . VAL   A 1 123 ? -28.037 11.661  -33.752 1.00 37.08  ? 641  VAL   A N    1 
ATOM   1078 C  CA   . VAL   A 1 123 ? -26.647 12.110  -33.757 1.00 37.01  ? 641  VAL   A CA   1 
ATOM   1079 C  C    . VAL   A 1 123 ? -25.980 11.785  -32.427 1.00 42.03  ? 641  VAL   A C    1 
ATOM   1080 O  O    . VAL   A 1 123 ? -24.827 11.336  -32.386 1.00 43.79  ? 641  VAL   A O    1 
ATOM   1081 C  CB   . VAL   A 1 123 ? -26.569 13.614  -34.078 1.00 42.70  ? 641  VAL   A CB   1 
ATOM   1082 C  CG1  . VAL   A 1 123 ? -25.141 14.120  -33.923 1.00 36.79  ? 641  VAL   A CG1  1 
ATOM   1083 C  CG2  . VAL   A 1 123 ? -27.083 13.885  -35.482 1.00 44.40  ? 641  VAL   A CG2  1 
ATOM   1084 N  N    . ALA   A 1 124 ? -26.693 12.004  -31.320 1.00 39.10  ? 642  ALA   A N    1 
ATOM   1085 C  CA   . ALA   A 1 124 ? -26.149 11.657  -30.011 1.00 40.26  ? 642  ALA   A CA   1 
ATOM   1086 C  C    . ALA   A 1 124 ? -25.901 10.159  -29.899 1.00 39.97  ? 642  ALA   A C    1 
ATOM   1087 O  O    . ALA   A 1 124 ? -24.860 9.731   -29.388 1.00 38.66  ? 642  ALA   A O    1 
ATOM   1088 C  CB   . ALA   A 1 124 ? -27.090 12.131  -28.905 1.00 39.21  ? 642  ALA   A CB   1 
ATOM   1089 N  N    . GLY   A 1 125 ? -26.846 9.347   -30.374 1.00 39.63  ? 643  GLY   A N    1 
ATOM   1090 C  CA   . GLY   A 1 125 ? -26.626 7.910   -30.391 1.00 38.98  ? 643  GLY   A CA   1 
ATOM   1091 C  C    . GLY   A 1 125 ? -25.483 7.511   -31.304 1.00 44.10  ? 643  GLY   A C    1 
ATOM   1092 O  O    . GLY   A 1 125 ? -24.739 6.573   -31.010 1.00 50.79  ? 643  GLY   A O    1 
ATOM   1093 N  N    . MET   A 1 126 ? -25.323 8.224   -32.422 1.00 42.86  ? 644  MET   A N    1 
ATOM   1094 C  CA   . MET   A 1 126 ? -24.215 7.937   -33.327 1.00 43.40  ? 644  MET   A CA   1 
ATOM   1095 C  C    . MET   A 1 126 ? -22.872 8.221   -32.664 1.00 43.80  ? 644  MET   A C    1 
ATOM   1096 O  O    . MET   A 1 126 ? -21.913 7.460   -32.838 1.00 48.96  ? 644  MET   A O    1 
ATOM   1097 C  CB   . MET   A 1 126 ? -24.358 8.753   -34.611 1.00 46.48  ? 644  MET   A CB   1 
ATOM   1098 C  CG   . MET   A 1 126 ? -25.364 8.190   -35.600 1.00 47.89  ? 644  MET   A CG   1 
ATOM   1099 S  SD   . MET   A 1 126 ? -25.724 9.340   -36.940 1.00 46.74  ? 644  MET   A SD   1 
ATOM   1100 C  CE   . MET   A 1 126 ? -24.196 9.259   -37.873 1.00 43.05  ? 644  MET   A CE   1 
ATOM   1101 N  N    . ALA   A 1 127 ? -22.784 9.316   -31.905 1.00 39.67  ? 645  ALA   A N    1 
ATOM   1102 C  CA   . ALA   A 1 127 ? -21.540 9.643   -31.215 1.00 42.51  ? 645  ALA   A CA   1 
ATOM   1103 C  C    . ALA   A 1 127 ? -21.171 8.556   -30.215 1.00 44.97  ? 645  ALA   A C    1 
ATOM   1104 O  O    . ALA   A 1 127 ? -20.014 8.125   -30.143 1.00 47.56  ? 645  ALA   A O    1 
ATOM   1105 C  CB   . ALA   A 1 127 ? -21.668 10.998  -30.519 1.00 37.55  ? 645  ALA   A CB   1 
ATOM   1106 N  N    . VAL   A 1 128 ? -22.150 8.093   -29.436 1.00 45.49  ? 646  VAL   A N    1 
ATOM   1107 C  CA   . VAL   A 1 128 ? -21.897 7.029   -28.470 1.00 49.45  ? 646  VAL   A CA   1 
ATOM   1108 C  C    . VAL   A 1 128 ? -21.521 5.738   -29.188 1.00 47.97  ? 646  VAL   A C    1 
ATOM   1109 O  O    . VAL   A 1 128 ? -20.560 5.055   -28.812 1.00 49.04  ? 646  VAL   A O    1 
ATOM   1110 C  CB   . VAL   A 1 128 ? -23.120 6.836   -27.557 1.00 45.48  ? 646  VAL   A CB   1 
ATOM   1111 C  CG1  . VAL   A 1 128 ? -22.937 5.619   -26.668 1.00 43.54  ? 646  VAL   A CG1  1 
ATOM   1112 C  CG2  . VAL   A 1 128 ? -23.348 8.082   -26.720 1.00 44.13  ? 646  VAL   A CG2  1 
ATOM   1113 N  N    . TYR   A 1 129 ? -22.265 5.392   -30.243 1.00 43.91  ? 647  TYR   A N    1 
ATOM   1114 C  CA   . TYR   A 1 129 ? -22.011 4.137   -30.946 1.00 46.03  ? 647  TYR   A CA   1 
ATOM   1115 C  C    . TYR   A 1 129 ? -20.631 4.125   -31.591 1.00 51.18  ? 647  TYR   A C    1 
ATOM   1116 O  O    . TYR   A 1 129 ? -19.960 3.086   -31.617 1.00 57.09  ? 647  TYR   A O    1 
ATOM   1117 C  CB   . TYR   A 1 129 ? -23.091 3.888   -32.002 1.00 41.97  ? 647  TYR   A CB   1 
ATOM   1118 C  CG   . TYR   A 1 129 ? -23.035 2.499   -32.603 1.00 41.95  ? 647  TYR   A CG   1 
ATOM   1119 C  CD1  . TYR   A 1 129 ? -23.751 1.450   -32.042 1.00 43.84  ? 647  TYR   A CD1  1 
ATOM   1120 C  CD2  . TYR   A 1 129 ? -22.255 2.235   -33.724 1.00 45.04  ? 647  TYR   A CD2  1 
ATOM   1121 C  CE1  . TYR   A 1 129 ? -23.695 0.177   -32.582 1.00 49.75  ? 647  TYR   A CE1  1 
ATOM   1122 C  CE2  . TYR   A 1 129 ? -22.192 0.965   -34.270 1.00 47.96  ? 647  TYR   A CE2  1 
ATOM   1123 C  CZ   . TYR   A 1 129 ? -22.916 -0.059  -33.697 1.00 53.45  ? 647  TYR   A CZ   1 
ATOM   1124 O  OH   . TYR   A 1 129 ? -22.860 -1.324  -34.239 1.00 60.18  ? 647  TYR   A OH   1 
ATOM   1125 N  N    . HIS   A 1 130 ? -20.189 5.264   -32.121 1.00 46.83  ? 648  HIS   A N    1 
ATOM   1126 C  CA   . HIS   A 1 130 ? -18.922 5.345   -32.834 1.00 48.28  ? 648  HIS   A CA   1 
ATOM   1127 C  C    . HIS   A 1 130 ? -17.774 5.821   -31.952 1.00 50.75  ? 648  HIS   A C    1 
ATOM   1128 O  O    . HIS   A 1 130 ? -16.692 6.118   -32.467 1.00 52.15  ? 648  HIS   A O    1 
ATOM   1129 C  CB   . HIS   A 1 130 ? -19.063 6.256   -34.054 1.00 46.87  ? 648  HIS   A CB   1 
ATOM   1130 C  CG   . HIS   A 1 130 ? -19.939 5.690   -35.128 1.00 54.10  ? 648  HIS   A CG   1 
ATOM   1131 N  ND1  . HIS   A 1 130 ? -19.524 4.682   -35.972 1.00 58.04  ? 648  HIS   A ND1  1 
ATOM   1132 C  CD2  . HIS   A 1 130 ? -21.209 5.987   -35.493 1.00 55.34  ? 648  HIS   A CD2  1 
ATOM   1133 C  CE1  . HIS   A 1 130 ? -20.499 4.383   -36.811 1.00 58.02  ? 648  HIS   A CE1  1 
ATOM   1134 N  NE2  . HIS   A 1 130 ? -21.533 5.161   -36.542 1.00 56.53  ? 648  HIS   A NE2  1 
ATOM   1135 N  N    . GLY   A 1 131 ? -17.982 5.896   -30.640 1.00 50.37  ? 649  GLY   A N    1 
ATOM   1136 C  CA   . GLY   A 1 131 ? -16.914 6.286   -29.740 1.00 50.05  ? 649  GLY   A CA   1 
ATOM   1137 C  C    . GLY   A 1 131 ? -16.453 7.718   -29.891 1.00 48.26  ? 649  GLY   A C    1 
ATOM   1138 O  O    . GLY   A 1 131 ? -15.292 8.021   -29.605 1.00 47.74  ? 649  GLY   A O    1 
ATOM   1139 N  N    . LYS   A 1 132 ? -17.330 8.608   -30.338 1.00 47.53  ? 650  LYS   A N    1 
ATOM   1140 C  CA   . LYS   A 1 132 ? -17.009 10.018  -30.474 1.00 50.51  ? 650  LYS   A CA   1 
ATOM   1141 C  C    . LYS   A 1 132 ? -17.822 10.829  -29.475 1.00 49.06  ? 650  LYS   A C    1 
ATOM   1142 O  O    . LYS   A 1 132 ? -18.845 10.375  -28.956 1.00 49.27  ? 650  LYS   A O    1 
ATOM   1143 C  CB   . LYS   A 1 132 ? -17.272 10.506  -31.903 1.00 56.21  ? 650  LYS   A CB   1 
ATOM   1144 C  CG   . LYS   A 1 132 ? -16.553 9.693   -32.973 1.00 62.98  ? 650  LYS   A CG   1 
ATOM   1145 C  CD   . LYS   A 1 132 ? -15.117 10.160  -33.164 1.00 66.56  ? 650  LYS   A CD   1 
ATOM   1146 C  CE   . LYS   A 1 132 ? -14.383 9.300   -34.185 1.00 69.18  ? 650  LYS   A CE   1 
ATOM   1147 N  NZ   . LYS   A 1 132 ? -13.622 8.189   -33.548 1.00 70.90  ? 650  LYS   A NZ   1 
ATOM   1148 N  N    . LEU   A 1 133 ? -17.350 12.037  -29.201 1.00 54.44  ? 651  LEU   A N    1 
ATOM   1149 C  CA   . LEU   A 1 133 ? -17.978 12.893  -28.209 1.00 57.34  ? 651  LEU   A CA   1 
ATOM   1150 C  C    . LEU   A 1 133 ? -18.794 13.991  -28.877 1.00 54.58  ? 651  LEU   A C    1 
ATOM   1151 O  O    . LEU   A 1 133 ? -18.463 14.467  -29.967 1.00 55.76  ? 651  LEU   A O    1 
ATOM   1152 C  CB   . LEU   A 1 133 ? -16.929 13.518  -27.287 1.00 59.01  ? 651  LEU   A CB   1 
ATOM   1153 C  CG   . LEU   A 1 133 ? -16.174 12.539  -26.387 1.00 59.19  ? 651  LEU   A CG   1 
ATOM   1154 C  CD1  . LEU   A 1 133 ? -15.045 13.244  -25.655 1.00 60.27  ? 651  LEU   A CD1  1 
ATOM   1155 C  CD2  . LEU   A 1 133 ? -17.124 11.877  -25.405 1.00 58.93  ? 651  LEU   A CD2  1 
ATOM   1156 N  N    . LEU   A 1 134 ? -19.878 14.375  -28.214 1.00 47.60  ? 652  LEU   A N    1 
ATOM   1157 C  CA   . LEU   A 1 134 ? -20.635 15.558  -28.585 1.00 45.14  ? 652  LEU   A CA   1 
ATOM   1158 C  C    . LEU   A 1 134 ? -20.035 16.778  -27.900 1.00 48.79  ? 652  LEU   A C    1 
ATOM   1159 O  O    . LEU   A 1 134 ? -19.470 16.684  -26.807 1.00 52.79  ? 652  LEU   A O    1 
ATOM   1160 C  CB   . LEU   A 1 134 ? -22.105 15.410  -28.192 1.00 47.77  ? 652  LEU   A CB   1 
ATOM   1161 C  CG   . LEU   A 1 134 ? -22.983 14.550  -29.100 1.00 52.22  ? 652  LEU   A CG   1 
ATOM   1162 C  CD1  . LEU   A 1 134 ? -24.446 14.743  -28.745 1.00 53.73  ? 652  LEU   A CD1  1 
ATOM   1163 C  CD2  . LEU   A 1 134 ? -22.732 14.887  -30.561 1.00 53.69  ? 652  LEU   A CD2  1 
ATOM   1164 N  N    . ASP   A 1 135 ? -20.154 17.928  -28.555 1.00 52.19  ? 653  ASP   A N    1 
ATOM   1165 C  CA   . ASP   A 1 135 ? -19.668 19.190  -28.001 1.00 59.03  ? 653  ASP   A CA   1 
ATOM   1166 C  C    . ASP   A 1 135 ? -20.861 19.949  -27.433 1.00 61.51  ? 653  ASP   A C    1 
ATOM   1167 O  O    . ASP   A 1 135 ? -21.587 20.632  -28.160 1.00 63.94  ? 653  ASP   A O    1 
ATOM   1168 C  CB   . ASP   A 1 135 ? -18.930 20.011  -29.050 1.00 67.87  ? 653  ASP   A CB   1 
ATOM   1169 C  CG   . ASP   A 1 135 ? -18.039 21.068  -28.430 1.00 80.94  ? 653  ASP   A CG   1 
ATOM   1170 O  OD1  . ASP   A 1 135 ? -17.022 20.696  -27.807 1.00 85.27  ? 653  ASP   A OD1  1 
ATOM   1171 O  OD2  . ASP   A 1 135 ? -18.360 22.268  -28.556 1.00 86.61  ? 653  ASP   A OD2  1 
ATOM   1172 N  N    . GLY   A 1 136 ? -21.053 19.829  -26.125 1.00 61.66  ? 654  GLY   A N    1 
ATOM   1173 C  CA   . GLY   A 1 136 ? -22.138 20.493  -25.437 1.00 65.30  ? 654  GLY   A CA   1 
ATOM   1174 C  C    . GLY   A 1 136 ? -22.442 19.778  -24.141 1.00 67.93  ? 654  GLY   A C    1 
ATOM   1175 O  O    . GLY   A 1 136 ? -22.281 18.557  -24.057 1.00 73.25  ? 654  GLY   A O    1 
ATOM   1176 N  N    . PHE   A 1 137 ? -22.863 20.510  -23.117 1.00 61.92  ? 655  PHE   A N    1 
ATOM   1177 C  CA   . PHE   A 1 137 ? -23.194 19.886  -21.846 1.00 62.09  ? 655  PHE   A CA   1 
ATOM   1178 C  C    . PHE   A 1 137 ? -24.566 20.335  -21.385 1.00 54.34  ? 655  PHE   A C    1 
ATOM   1179 O  O    . PHE   A 1 137 ? -24.912 21.518  -21.464 1.00 52.25  ? 655  PHE   A O    1 
ATOM   1180 C  CB   . PHE   A 1 137 ? -22.164 20.183  -20.760 1.00 70.73  ? 655  PHE   A CB   1 
ATOM   1181 C  CG   . PHE   A 1 137 ? -21.561 21.551  -20.832 1.00 80.58  ? 655  PHE   A CG   1 
ATOM   1182 C  CD1  . PHE   A 1 137 ? -22.004 22.557  -19.995 1.00 84.66  ? 655  PHE   A CD1  1 
ATOM   1183 C  CD2  . PHE   A 1 137 ? -20.527 21.824  -21.712 1.00 84.97  ? 655  PHE   A CD2  1 
ATOM   1184 C  CE1  . PHE   A 1 137 ? -21.436 23.801  -20.046 1.00 90.91  ? 655  PHE   A CE1  1 
ATOM   1185 C  CE2  . PHE   A 1 137 ? -19.957 23.061  -21.762 1.00 90.50  ? 655  PHE   A CE2  1 
ATOM   1186 C  CZ   . PHE   A 1 137 ? -20.402 24.040  -20.922 1.00 93.51  ? 655  PHE   A CZ   1 
ATOM   1187 N  N    . PHE   A 1 138 ? -25.333 19.374  -20.896 1.00 48.65  ? 656  PHE   A N    1 
ATOM   1188 C  CA   . PHE   A 1 138 ? -26.711 19.577  -20.497 1.00 50.08  ? 656  PHE   A CA   1 
ATOM   1189 C  C    . PHE   A 1 138 ? -26.819 19.553  -18.981 1.00 44.56  ? 656  PHE   A C    1 
ATOM   1190 O  O    . PHE   A 1 138 ? -25.911 19.104  -18.276 1.00 45.77  ? 656  PHE   A O    1 
ATOM   1191 C  CB   . PHE   A 1 138 ? -27.605 18.499  -21.117 1.00 51.80  ? 656  PHE   A CB   1 
ATOM   1192 C  CG   . PHE   A 1 138 ? -27.366 18.298  -22.584 1.00 58.83  ? 656  PHE   A CG   1 
ATOM   1193 C  CD1  . PHE   A 1 138 ? -27.648 19.310  -23.485 1.00 59.32  ? 656  PHE   A CD1  1 
ATOM   1194 C  CD2  . PHE   A 1 138 ? -26.841 17.109  -23.061 1.00 65.02  ? 656  PHE   A CD2  1 
ATOM   1195 C  CE1  . PHE   A 1 138 ? -27.425 19.137  -24.836 1.00 64.72  ? 656  PHE   A CE1  1 
ATOM   1196 C  CE2  . PHE   A 1 138 ? -26.615 16.930  -24.413 1.00 68.26  ? 656  PHE   A CE2  1 
ATOM   1197 C  CZ   . PHE   A 1 138 ? -26.907 17.946  -25.301 1.00 68.43  ? 656  PHE   A CZ   1 
ATOM   1198 N  N    . ILE   A 1 139 ? -27.948 20.060  -18.487 1.00 37.77  ? 657  ILE   A N    1 
ATOM   1199 C  CA   . ILE   A 1 139 ? -28.228 19.966  -17.065 1.00 38.90  ? 657  ILE   A CA   1 
ATOM   1200 C  C    . ILE   A 1 139 ? -28.330 18.497  -16.676 1.00 38.64  ? 657  ILE   A C    1 
ATOM   1201 O  O    . ILE   A 1 139 ? -28.630 17.628  -17.505 1.00 40.22  ? 657  ILE   A O    1 
ATOM   1202 C  CB   . ILE   A 1 139 ? -29.516 20.730  -16.716 1.00 38.76  ? 657  ILE   A CB   1 
ATOM   1203 C  CG1  . ILE   A 1 139 ? -30.675 20.245  -17.585 1.00 37.48  ? 657  ILE   A CG1  1 
ATOM   1204 C  CG2  . ILE   A 1 139 ? -29.309 22.212  -16.921 1.00 43.89  ? 657  ILE   A CG2  1 
ATOM   1205 C  CD1  . ILE   A 1 139 ? -32.014 20.805  -17.171 1.00 39.15  ? 657  ILE   A CD1  1 
ATOM   1206 N  N    . ARG   A 1 140 ? -28.057 18.210  -15.405 1.00 40.95  ? 658  ARG   A N    1 
ATOM   1207 C  CA   . ARG   A 1 140 ? -28.122 16.825  -14.949 1.00 45.64  ? 658  ARG   A CA   1 
ATOM   1208 C  C    . ARG   A 1 140 ? -29.499 16.191  -15.134 1.00 44.82  ? 658  ARG   A C    1 
ATOM   1209 O  O    . ARG   A 1 140 ? -29.547 14.998  -15.481 1.00 47.74  ? 658  ARG   A O    1 
ATOM   1210 C  CB   . ARG   A 1 140 ? -27.662 16.728  -13.489 1.00 52.69  ? 658  ARG   A CB   1 
ATOM   1211 C  CG   . ARG   A 1 140 ? -27.361 15.301  -13.050 1.00 64.71  ? 658  ARG   A CG   1 
ATOM   1212 C  CD   . ARG   A 1 140 ? -26.278 15.241  -11.981 1.00 77.75  ? 658  ARG   A CD   1 
ATOM   1213 N  NE   . ARG   A 1 140 ? -25.092 16.018  -12.338 1.00 87.56  ? 658  ARG   A NE   1 
ATOM   1214 C  CZ   . ARG   A 1 140 ? -24.056 15.538  -13.021 1.00 91.44  ? 658  ARG   A CZ   1 
ATOM   1215 N  NH1  . ARG   A 1 140 ? -24.055 14.277  -13.431 1.00 94.65  ? 658  ARG   A NH1  1 
ATOM   1216 N  NH2  . ARG   A 1 140 ? -23.019 16.319  -13.294 1.00 90.21  ? 658  ARG   A NH2  1 
ATOM   1217 N  N    . PRO   A 1 141 ? -30.628 16.889  -14.934 1.00 40.89  ? 659  PRO   A N    1 
ATOM   1218 C  CA   . PRO   A 1 141 ? -31.924 16.255  -15.237 1.00 41.24  ? 659  PRO   A CA   1 
ATOM   1219 C  C    . PRO   A 1 141 ? -32.030 15.720  -16.655 1.00 40.71  ? 659  PRO   A C    1 
ATOM   1220 O  O    . PRO   A 1 141 ? -32.752 14.741  -16.880 1.00 40.43  ? 659  PRO   A O    1 
ATOM   1221 C  CB   . PRO   A 1 141 ? -32.930 17.385  -14.985 1.00 40.63  ? 659  PRO   A CB   1 
ATOM   1222 C  CG   . PRO   A 1 141 ? -32.283 18.213  -13.946 1.00 44.38  ? 659  PRO   A CG   1 
ATOM   1223 C  CD   . PRO   A 1 141 ? -30.815 18.191  -14.264 1.00 41.75  ? 659  PRO   A CD   1 
ATOM   1224 N  N    . PHE   A 1 142 ? -31.333 16.328  -17.618 1.00 38.55  ? 660  PHE   A N    1 
ATOM   1225 C  CA   . PHE   A 1 142 ? -31.345 15.802  -18.980 1.00 38.63  ? 660  PHE   A CA   1 
ATOM   1226 C  C    . PHE   A 1 142 ? -30.810 14.376  -19.020 1.00 36.55  ? 660  PHE   A C    1 
ATOM   1227 O  O    . PHE   A 1 142 ? -31.447 13.477  -19.580 1.00 37.29  ? 660  PHE   A O    1 
ATOM   1228 C  CB   . PHE   A 1 142 ? -30.532 16.708  -19.904 1.00 39.31  ? 660  PHE   A CB   1 
ATOM   1229 C  CG   . PHE   A 1 142 ? -30.653 16.354  -21.359 1.00 39.39  ? 660  PHE   A CG   1 
ATOM   1230 C  CD1  . PHE   A 1 142 ? -31.609 16.964  -22.156 1.00 39.55  ? 660  PHE   A CD1  1 
ATOM   1231 C  CD2  . PHE   A 1 142 ? -29.814 15.410  -21.932 1.00 38.04  ? 660  PHE   A CD2  1 
ATOM   1232 C  CE1  . PHE   A 1 142 ? -31.726 16.640  -23.497 1.00 35.94  ? 660  PHE   A CE1  1 
ATOM   1233 C  CE2  . PHE   A 1 142 ? -29.927 15.080  -23.271 1.00 35.36  ? 660  PHE   A CE2  1 
ATOM   1234 C  CZ   . PHE   A 1 142 ? -30.885 15.696  -24.054 1.00 34.21  ? 660  PHE   A CZ   1 
ATOM   1235 N  N    . TYR   A 1 143 ? -29.634 14.149  -18.429 1.00 38.97  ? 661  TYR   A N    1 
ATOM   1236 C  CA   . TYR   A 1 143 ? -29.050 12.812  -18.442 1.00 38.52  ? 661  TYR   A CA   1 
ATOM   1237 C  C    . TYR   A 1 143 ? -29.892 11.820  -17.649 1.00 39.88  ? 661  TYR   A C    1 
ATOM   1238 O  O    . TYR   A 1 143 ? -29.922 10.630  -17.983 1.00 41.30  ? 661  TYR   A O    1 
ATOM   1239 C  CB   . TYR   A 1 143 ? -27.620 12.854  -17.900 1.00 37.77  ? 661  TYR   A CB   1 
ATOM   1240 C  CG   . TYR   A 1 143 ? -26.694 13.765  -18.678 1.00 42.48  ? 661  TYR   A CG   1 
ATOM   1241 C  CD1  . TYR   A 1 143 ? -26.372 15.031  -18.208 1.00 46.75  ? 661  TYR   A CD1  1 
ATOM   1242 C  CD2  . TYR   A 1 143 ? -26.139 13.358  -19.883 1.00 42.49  ? 661  TYR   A CD2  1 
ATOM   1243 C  CE1  . TYR   A 1 143 ? -25.528 15.866  -18.919 1.00 50.23  ? 661  TYR   A CE1  1 
ATOM   1244 C  CE2  . TYR   A 1 143 ? -25.301 14.183  -20.604 1.00 47.82  ? 661  TYR   A CE2  1 
ATOM   1245 C  CZ   . TYR   A 1 143 ? -24.995 15.435  -20.117 1.00 50.34  ? 661  TYR   A CZ   1 
ATOM   1246 O  OH   . TYR   A 1 143 ? -24.155 16.258  -20.831 1.00 54.63  ? 661  TYR   A OH   1 
ATOM   1247 N  N    . LYS   A 1 144 ? -30.589 12.287  -16.611 1.00 40.75  ? 662  LYS   A N    1 
ATOM   1248 C  CA   . LYS   A 1 144 ? -31.402 11.383  -15.804 1.00 43.86  ? 662  LYS   A CA   1 
ATOM   1249 C  C    . LYS   A 1 144 ? -32.668 10.963  -16.542 1.00 43.58  ? 662  LYS   A C    1 
ATOM   1250 O  O    . LYS   A 1 144 ? -33.123 9.821   -16.402 1.00 37.38  ? 662  LYS   A O    1 
ATOM   1251 C  CB   . LYS   A 1 144 ? -31.738 12.041  -14.468 1.00 47.58  ? 662  LYS   A CB   1 
ATOM   1252 C  CG   . LYS   A 1 144 ? -30.507 12.343  -13.626 1.00 57.09  ? 662  LYS   A CG   1 
ATOM   1253 C  CD   . LYS   A 1 144 ? -30.868 13.017  -12.315 1.00 63.53  ? 662  LYS   A CD   1 
ATOM   1254 C  CE   . LYS   A 1 144 ? -31.083 11.996  -11.214 1.00 67.80  ? 662  LYS   A CE   1 
ATOM   1255 N  NZ   . LYS   A 1 144 ? -32.450 11.418  -11.276 1.00 69.88  ? 662  LYS   A NZ   1 
ATOM   1256 N  N    . MET   A 1 145 ? -33.249 11.867  -17.335 1.00 40.56  ? 663  MET   A N    1 
ATOM   1257 C  CA   . MET   A 1 145 ? -34.401 11.492  -18.150 1.00 44.61  ? 663  MET   A CA   1 
ATOM   1258 C  C    . MET   A 1 145 ? -34.012 10.459  -19.200 1.00 44.27  ? 663  MET   A C    1 
ATOM   1259 O  O    . MET   A 1 145 ? -34.799 9.559   -19.515 1.00 45.21  ? 663  MET   A O    1 
ATOM   1260 C  CB   . MET   A 1 145 ? -35.012 12.730  -18.808 1.00 46.10  ? 663  MET   A CB   1 
ATOM   1261 C  CG   . MET   A 1 145 ? -35.748 13.643  -17.838 1.00 50.83  ? 663  MET   A CG   1 
ATOM   1262 S  SD   . MET   A 1 145 ? -36.500 15.083  -18.626 1.00 52.48  ? 663  MET   A SD   1 
ATOM   1263 C  CE   . MET   A 1 145 ? -37.947 14.346  -19.382 1.00 63.18  ? 663  MET   A CE   1 
ATOM   1264 N  N    . MET   A 1 146 ? -32.798 10.573  -19.747 1.00 45.25  ? 664  MET   A N    1 
ATOM   1265 C  CA   . MET   A 1 146 ? -32.297 9.560   -20.671 1.00 45.16  ? 664  MET   A CA   1 
ATOM   1266 C  C    . MET   A 1 146 ? -32.276 8.183   -20.019 1.00 43.76  ? 664  MET   A C    1 
ATOM   1267 O  O    . MET   A 1 146 ? -32.593 7.177   -20.663 1.00 43.70  ? 664  MET   A O    1 
ATOM   1268 C  CB   . MET   A 1 146 ? -30.896 9.937   -21.153 1.00 47.26  ? 664  MET   A CB   1 
ATOM   1269 C  CG   . MET   A 1 146 ? -30.865 10.963  -22.269 1.00 46.15  ? 664  MET   A CG   1 
ATOM   1270 S  SD   . MET   A 1 146 ? -29.247 11.047  -23.063 1.00 47.09  ? 664  MET   A SD   1 
ATOM   1271 C  CE   . MET   A 1 146 ? -28.394 12.126  -21.938 1.00 53.44  ? 664  MET   A CE   1 
ATOM   1272 N  N    . LEU   A 1 147 ? -31.908 8.122   -18.741 1.00 41.64  ? 665  LEU   A N    1 
ATOM   1273 C  CA   . LEU   A 1 147 ? -31.793 6.871   -18.005 1.00 44.33  ? 665  LEU   A CA   1 
ATOM   1274 C  C    . LEU   A 1 147 ? -33.072 6.491   -17.272 1.00 46.55  ? 665  LEU   A C    1 
ATOM   1275 O  O    . LEU   A 1 147 ? -33.066 5.517   -16.512 1.00 44.46  ? 665  LEU   A O    1 
ATOM   1276 C  CB   . LEU   A 1 147 ? -30.642 6.960   -17.001 1.00 45.56  ? 665  LEU   A CB   1 
ATOM   1277 C  CG   . LEU   A 1 147 ? -29.249 7.242   -17.560 1.00 49.15  ? 665  LEU   A CG   1 
ATOM   1278 C  CD1  . LEU   A 1 147 ? -28.350 7.784   -16.466 1.00 52.63  ? 665  LEU   A CD1  1 
ATOM   1279 C  CD2  . LEU   A 1 147 ? -28.659 5.981   -18.164 1.00 46.63  ? 665  LEU   A CD2  1 
ATOM   1280 N  N    . HIS   A 1 148 ? -34.159 7.238   -17.476 1.00 44.52  ? 666  HIS   A N    1 
ATOM   1281 C  CA   . HIS   A 1 148 ? -35.415 7.019   -16.758 1.00 48.60  ? 666  HIS   A CA   1 
ATOM   1282 C  C    . HIS   A 1 148 ? -35.205 7.085   -15.246 1.00 51.03  ? 666  HIS   A C    1 
ATOM   1283 O  O    . HIS   A 1 148 ? -35.829 6.347   -14.481 1.00 55.84  ? 666  HIS   A O    1 
ATOM   1284 C  CB   . HIS   A 1 148 ? -36.066 5.694   -17.162 1.00 59.58  ? 666  HIS   A CB   1 
ATOM   1285 C  CG   . HIS   A 1 148 ? -37.545 5.790   -17.373 1.00 73.86  ? 666  HIS   A CG   1 
ATOM   1286 N  ND1  . HIS   A 1 148 ? -38.446 5.796   -16.330 1.00 79.20  ? 666  HIS   A ND1  1 
ATOM   1287 C  CD2  . HIS   A 1 148 ? -38.279 5.890   -18.506 1.00 77.74  ? 666  HIS   A CD2  1 
ATOM   1288 C  CE1  . HIS   A 1 148 ? -39.672 5.893   -16.812 1.00 80.29  ? 666  HIS   A CE1  1 
ATOM   1289 N  NE2  . HIS   A 1 148 ? -39.599 5.951   -18.129 1.00 78.99  ? 666  HIS   A NE2  1 
ATOM   1290 N  N    . LYS   A 1 149 ? -34.305 7.967   -14.815 1.00 45.87  ? 667  LYS   A N    1 
ATOM   1291 C  CA   . LYS   A 1 149 ? -34.120 8.194   -13.387 1.00 50.60  ? 667  LYS   A CA   1 
ATOM   1292 C  C    . LYS   A 1 149 ? -34.992 9.361   -12.933 1.00 49.98  ? 667  LYS   A C    1 
ATOM   1293 O  O    . LYS   A 1 149 ? -35.176 10.325  -13.681 1.00 48.11  ? 667  LYS   A O    1 
ATOM   1294 C  CB   . LYS   A 1 149 ? -32.656 8.493   -13.066 1.00 54.52  ? 667  LYS   A CB   1 
ATOM   1295 C  CG   . LYS   A 1 149 ? -31.750 7.267   -13.005 1.00 59.59  ? 667  LYS   A CG   1 
ATOM   1296 C  CD   . LYS   A 1 149 ? -30.721 7.404   -11.887 1.00 66.84  ? 667  LYS   A CD   1 
ATOM   1297 C  CE   . LYS   A 1 149 ? -29.459 6.599   -12.170 1.00 74.77  ? 667  LYS   A CE   1 
ATOM   1298 N  NZ   . LYS   A 1 149 ? -29.674 5.128   -12.062 1.00 79.54  ? 667  LYS   A NZ   1 
ATOM   1299 N  N    . PRO   A 1 150 ? -35.548 9.302   -11.725 1.00 56.04  ? 668  PRO   A N    1 
ATOM   1300 C  CA   . PRO   A 1 150 ? -36.427 10.387  -11.271 1.00 53.92  ? 668  PRO   A CA   1 
ATOM   1301 C  C    . PRO   A 1 150 ? -35.651 11.668  -11.005 1.00 51.31  ? 668  PRO   A C    1 
ATOM   1302 O  O    . PRO   A 1 150 ? -34.530 11.644  -10.491 1.00 48.09  ? 668  PRO   A O    1 
ATOM   1303 C  CB   . PRO   A 1 150 ? -37.042 9.827   -9.983  1.00 59.85  ? 668  PRO   A CB   1 
ATOM   1304 C  CG   . PRO   A 1 150 ? -36.028 8.840   -9.490  1.00 62.93  ? 668  PRO   A CG   1 
ATOM   1305 C  CD   . PRO   A 1 150 ? -35.434 8.224   -10.726 1.00 61.11  ? 668  PRO   A CD   1 
ATOM   1306 N  N    . ILE   A 1 151 ? -36.260 12.794  -11.364 1.00 47.15  ? 669  ILE   A N    1 
ATOM   1307 C  CA   . ILE   A 1 151 ? -35.683 14.102  -11.071 1.00 44.31  ? 669  ILE   A CA   1 
ATOM   1308 C  C    . ILE   A 1 151 ? -35.955 14.441  -9.612  1.00 44.34  ? 669  ILE   A C    1 
ATOM   1309 O  O    . ILE   A 1 151 ? -37.107 14.428  -9.164  1.00 49.42  ? 669  ILE   A O    1 
ATOM   1310 C  CB   . ILE   A 1 151 ? -36.255 15.178  -12.007 1.00 41.48  ? 669  ILE   A CB   1 
ATOM   1311 C  CG1  . ILE   A 1 151 ? -36.302 14.668  -13.448 1.00 44.19  ? 669  ILE   A CG1  1 
ATOM   1312 C  CG2  . ILE   A 1 151 ? -35.424 16.451  -11.920 1.00 41.51  ? 669  ILE   A CG2  1 
ATOM   1313 C  CD1  . ILE   A 1 151 ? -34.942 14.353  -14.032 1.00 47.99  ? 669  ILE   A CD1  1 
ATOM   1314 N  N    . THR   A 1 152 ? -34.898 14.747  -8.869  1.00 46.78  ? 670  THR   A N    1 
ATOM   1315 C  CA   . THR   A 1 152 ? -34.994 15.006  -7.441  1.00 54.23  ? 670  THR   A CA   1 
ATOM   1316 C  C    . THR   A 1 152 ? -34.700 16.468  -7.136  1.00 58.43  ? 670  THR   A C    1 
ATOM   1317 O  O    . THR   A 1 152 ? -34.275 17.244  -7.998  1.00 53.97  ? 670  THR   A O    1 
ATOM   1318 C  CB   . THR   A 1 152 ? -34.033 14.109  -6.652  1.00 53.76  ? 670  THR   A CB   1 
ATOM   1319 O  OG1  . THR   A 1 152 ? -32.685 14.551  -6.862  1.00 52.85  ? 670  THR   A OG1  1 
ATOM   1320 C  CG2  . THR   A 1 152 ? -34.167 12.659  -7.094  1.00 55.09  ? 670  THR   A CG2  1 
ATOM   1321 N  N    . LEU   A 1 153 ? -34.928 16.831  -5.872  1.00 61.31  ? 671  LEU   A N    1 
ATOM   1322 C  CA   . LEU   A 1 153 ? -34.672 18.196  -5.433  1.00 61.78  ? 671  LEU   A CA   1 
ATOM   1323 C  C    . LEU   A 1 153 ? -33.187 18.531  -5.497  1.00 58.22  ? 671  LEU   A C    1 
ATOM   1324 O  O    . LEU   A 1 153 ? -32.823 19.691  -5.725  1.00 58.18  ? 671  LEU   A O    1 
ATOM   1325 C  CB   . LEU   A 1 153 ? -35.219 18.394  -4.018  1.00 64.28  ? 671  LEU   A CB   1 
ATOM   1326 C  CG   . LEU   A 1 153 ? -34.728 19.594  -3.210  1.00 65.41  ? 671  LEU   A CG   1 
ATOM   1327 C  CD1  . LEU   A 1 153 ? -35.133 20.882  -3.903  1.00 66.21  ? 671  LEU   A CD1  1 
ATOM   1328 C  CD2  . LEU   A 1 153 ? -35.293 19.546  -1.804  1.00 66.06  ? 671  LEU   A CD2  1 
ATOM   1329 N  N    . HIS   A 1 154 ? -32.318 17.533  -5.319  1.00 58.86  ? 672  HIS   A N    1 
ATOM   1330 C  CA   . HIS   A 1 154 ? -30.881 17.778  -5.418  1.00 63.58  ? 672  HIS   A CA   1 
ATOM   1331 C  C    . HIS   A 1 154 ? -30.504 18.292  -6.802  1.00 62.81  ? 672  HIS   A C    1 
ATOM   1332 O  O    . HIS   A 1 154 ? -29.599 19.124  -6.937  1.00 65.43  ? 672  HIS   A O    1 
ATOM   1333 C  CB   . HIS   A 1 154 ? -30.105 16.501  -5.088  1.00 68.82  ? 672  HIS   A CB   1 
ATOM   1334 C  CG   . HIS   A 1 154 ? -28.636 16.593  -5.371  1.00 76.28  ? 672  HIS   A CG   1 
ATOM   1335 N  ND1  . HIS   A 1 154 ? -28.116 16.543  -6.647  1.00 76.53  ? 672  HIS   A ND1  1 
ATOM   1336 C  CD2  . HIS   A 1 154 ? -27.575 16.732  -4.540  1.00 80.10  ? 672  HIS   A CD2  1 
ATOM   1337 C  CE1  . HIS   A 1 154 ? -26.800 16.649  -6.590  1.00 78.56  ? 672  HIS   A CE1  1 
ATOM   1338 N  NE2  . HIS   A 1 154 ? -26.447 16.764  -5.323  1.00 80.46  ? 672  HIS   A NE2  1 
ATOM   1339 N  N    . ASP   A 1 155 ? -31.187 17.807  -7.843  1.00 62.48  ? 673  ASP   A N    1 
ATOM   1340 C  CA   . ASP   A 1 155 ? -30.907 18.275  -9.197  1.00 62.30  ? 673  ASP   A CA   1 
ATOM   1341 C  C    . ASP   A 1 155 ? -31.166 19.768  -9.340  1.00 56.80  ? 673  ASP   A C    1 
ATOM   1342 O  O    . ASP   A 1 155 ? -30.556 20.426  -10.191 1.00 56.36  ? 673  ASP   A O    1 
ATOM   1343 C  CB   . ASP   A 1 155 ? -31.748 17.493  -10.207 1.00 62.21  ? 673  ASP   A CB   1 
ATOM   1344 C  CG   . ASP   A 1 155 ? -31.564 15.995  -10.082 1.00 64.85  ? 673  ASP   A CG   1 
ATOM   1345 O  OD1  . ASP   A 1 155 ? -32.560 15.292  -9.816  1.00 66.21  ? 673  ASP   A OD1  1 
ATOM   1346 O  OD2  . ASP   A 1 155 ? -30.421 15.521  -10.248 1.00 67.74  ? 673  ASP   A OD2  1 
ATOM   1347 N  N    . MET   A 1 156 ? -32.063 20.320  -8.520  1.00 53.62  ? 674  MET   A N    1 
ATOM   1348 C  CA   . MET   A 1 156 ? -32.327 21.752  -8.570  1.00 56.04  ? 674  MET   A CA   1 
ATOM   1349 C  C    . MET   A 1 156 ? -31.118 22.560  -8.112  1.00 62.13  ? 674  MET   A C    1 
ATOM   1350 O  O    . MET   A 1 156 ? -30.917 23.687  -8.579  1.00 65.01  ? 674  MET   A O    1 
ATOM   1351 C  CB   . MET   A 1 156 ? -33.552 22.085  -7.717  1.00 59.20  ? 674  MET   A CB   1 
ATOM   1352 C  CG   . MET   A 1 156 ? -33.882 23.563  -7.639  1.00 64.34  ? 674  MET   A CG   1 
ATOM   1353 S  SD   . MET   A 1 156 ? -34.611 24.168  -9.169  1.00 68.50  ? 674  MET   A SD   1 
ATOM   1354 C  CE   . MET   A 1 156 ? -36.106 23.186  -9.235  1.00 66.75  ? 674  MET   A CE   1 
ATOM   1355 N  N    . GLU   A 1 157 ? -30.299 22.000  -7.218  1.00 63.22  ? 675  GLU   A N    1 
ATOM   1356 C  CA   . GLU   A 1 157 ? -29.139 22.730  -6.714  1.00 65.28  ? 675  GLU   A CA   1 
ATOM   1357 C  C    . GLU   A 1 157 ? -28.149 23.029  -7.833  1.00 67.89  ? 675  GLU   A C    1 
ATOM   1358 O  O    . GLU   A 1 157 ? -27.669 24.161  -7.967  1.00 68.08  ? 675  GLU   A O    1 
ATOM   1359 C  CB   . GLU   A 1 157 ? -28.462 21.937  -5.595  1.00 66.83  ? 675  GLU   A CB   1 
ATOM   1360 C  CG   . GLU   A 1 157 ? -27.215 22.612  -5.038  1.00 74.21  ? 675  GLU   A CG   1 
ATOM   1361 C  CD   . GLU   A 1 157 ? -26.635 21.887  -3.838  1.00 79.12  ? 675  GLU   A CD   1 
ATOM   1362 O  OE1  . GLU   A 1 157 ? -26.511 20.645  -3.893  1.00 78.99  ? 675  GLU   A OE1  1 
ATOM   1363 O  OE2  . GLU   A 1 157 ? -26.302 22.560  -2.840  1.00 82.42  ? 675  GLU   A OE2  1 
ATOM   1364 N  N    . SER   A 1 158 ? -27.838 22.025  -8.655  1.00 70.24  ? 676  SER   A N    1 
ATOM   1365 C  CA   . SER   A 1 158 ? -26.878 22.202  -9.739  1.00 74.87  ? 676  SER   A CA   1 
ATOM   1366 C  C    . SER   A 1 158 ? -27.347 23.195  -10.795 1.00 77.19  ? 676  SER   A C    1 
ATOM   1367 O  O    . SER   A 1 158 ? -26.537 23.611  -11.629 1.00 81.42  ? 676  SER   A O    1 
ATOM   1368 C  CB   . SER   A 1 158 ? -26.581 20.854  -10.399 1.00 76.81  ? 676  SER   A CB   1 
ATOM   1369 O  OG   . SER   A 1 158 ? -27.762 20.273  -10.927 1.00 78.23  ? 676  SER   A OG   1 
ATOM   1370 N  N    . VAL   A 1 159 ? -28.618 23.586  -10.780 1.00 75.42  ? 677  VAL   A N    1 
ATOM   1371 C  CA   . VAL   A 1 159 ? -29.182 24.492  -11.771 1.00 73.31  ? 677  VAL   A CA   1 
ATOM   1372 C  C    . VAL   A 1 159 ? -29.520 25.848  -11.160 1.00 72.37  ? 677  VAL   A C    1 
ATOM   1373 O  O    . VAL   A 1 159 ? -29.072 26.886  -11.647 1.00 78.00  ? 677  VAL   A O    1 
ATOM   1374 C  CB   . VAL   A 1 159 ? -30.421 23.865  -12.449 1.00 68.66  ? 677  VAL   A CB   1 
ATOM   1375 C  CG1  . VAL   A 1 159 ? -31.086 24.871  -13.376 1.00 68.62  ? 677  VAL   A CG1  1 
ATOM   1376 C  CG2  . VAL   A 1 159 ? -30.029 22.605  -13.207 1.00 66.60  ? 677  VAL   A CG2  1 
ATOM   1377 N  N    . ASP   A 1 160 ? -30.313 25.856  -10.089 1.00 69.40  ? 678  ASP   A N    1 
ATOM   1378 C  CA   . ASP   A 1 160 ? -30.733 27.088  -9.424  1.00 70.82  ? 678  ASP   A CA   1 
ATOM   1379 C  C    . ASP   A 1 160 ? -30.548 26.914  -7.922  1.00 69.89  ? 678  ASP   A C    1 
ATOM   1380 O  O    . ASP   A 1 160 ? -31.299 26.171  -7.282  1.00 68.51  ? 678  ASP   A O    1 
ATOM   1381 C  CB   . ASP   A 1 160 ? -32.185 27.430  -9.763  1.00 72.16  ? 678  ASP   A CB   1 
ATOM   1382 C  CG   . ASP   A 1 160 ? -32.585 28.816  -9.292  1.00 76.35  ? 678  ASP   A CG   1 
ATOM   1383 O  OD1  . ASP   A 1 160 ? -31.732 29.527  -8.720  1.00 80.80  ? 678  ASP   A OD1  1 
ATOM   1384 O  OD2  . ASP   A 1 160 ? -33.756 29.197  -9.498  1.00 76.50  ? 678  ASP   A OD2  1 
ATOM   1385 N  N    . SER   A 1 161 ? -29.559 27.612  -7.360  1.00 74.53  ? 679  SER   A N    1 
ATOM   1386 C  CA   . SER   A 1 161 ? -29.232 27.434  -5.948  1.00 82.31  ? 679  SER   A CA   1 
ATOM   1387 C  C    . SER   A 1 161 ? -30.254 28.112  -5.043  1.00 84.59  ? 679  SER   A C    1 
ATOM   1388 O  O    . SER   A 1 161 ? -30.575 27.594  -3.968  1.00 86.67  ? 679  SER   A O    1 
ATOM   1389 C  CB   . SER   A 1 161 ? -27.830 27.973  -5.663  1.00 90.93  ? 679  SER   A CB   1 
ATOM   1390 O  OG   . SER   A 1 161 ? -26.834 27.059  -6.088  1.00 94.10  ? 679  SER   A OG   1 
ATOM   1391 N  N    . GLU   A 1 162 ? -30.771 29.272  -5.456  1.00 85.71  ? 680  GLU   A N    1 
ATOM   1392 C  CA   . GLU   A 1 162 ? -31.662 30.031  -4.583  1.00 84.82  ? 680  GLU   A CA   1 
ATOM   1393 C  C    . GLU   A 1 162 ? -33.016 29.346  -4.430  1.00 80.21  ? 680  GLU   A C    1 
ATOM   1394 O  O    . GLU   A 1 162 ? -33.575 29.309  -3.328  1.00 82.96  ? 680  GLU   A O    1 
ATOM   1395 C  CB   . GLU   A 1 162 ? -31.829 31.455  -5.114  1.00 86.04  ? 680  GLU   A CB   1 
ATOM   1396 C  CG   . GLU   A 1 162 ? -30.519 32.112  -5.519  1.00 92.57  ? 680  GLU   A CG   1 
ATOM   1397 C  CD   . GLU   A 1 162 ? -30.681 33.580  -5.865  1.00 102.73 ? 680  GLU   A CD   1 
ATOM   1398 O  OE1  . GLU   A 1 162 ? -31.820 34.088  -5.791  1.00 104.29 ? 680  GLU   A OE1  1 
ATOM   1399 O  OE2  . GLU   A 1 162 ? -29.669 34.225  -6.209  1.00 108.46 ? 680  GLU   A OE2  1 
ATOM   1400 N  N    . TYR   A 1 163 ? -33.564 28.800  -5.519  1.00 73.47  ? 681  TYR   A N    1 
ATOM   1401 C  CA   . TYR   A 1 163 ? -34.815 28.060  -5.398  1.00 74.17  ? 681  TYR   A CA   1 
ATOM   1402 C  C    . TYR   A 1 163 ? -34.602 26.716  -4.715  1.00 71.15  ? 681  TYR   A C    1 
ATOM   1403 O  O    . TYR   A 1 163 ? -35.491 26.239  -4.000  1.00 71.37  ? 681  TYR   A O    1 
ATOM   1404 C  CB   . TYR   A 1 163 ? -35.461 27.860  -6.770  1.00 73.35  ? 681  TYR   A CB   1 
ATOM   1405 C  CG   . TYR   A 1 163 ? -36.962 27.669  -6.703  1.00 71.30  ? 681  TYR   A CG   1 
ATOM   1406 C  CD1  . TYR   A 1 163 ? -37.680 28.060  -5.579  1.00 75.20  ? 681  TYR   A CD1  1 
ATOM   1407 C  CD2  . TYR   A 1 163 ? -37.660 27.096  -7.758  1.00 68.10  ? 681  TYR   A CD2  1 
ATOM   1408 C  CE1  . TYR   A 1 163 ? -39.049 27.888  -5.509  1.00 76.34  ? 681  TYR   A CE1  1 
ATOM   1409 C  CE2  . TYR   A 1 163 ? -39.033 26.920  -7.696  1.00 70.12  ? 681  TYR   A CE2  1 
ATOM   1410 C  CZ   . TYR   A 1 163 ? -39.721 27.318  -6.569  1.00 75.07  ? 681  TYR   A CZ   1 
ATOM   1411 O  OH   . TYR   A 1 163 ? -41.085 27.147  -6.499  1.00 76.66  ? 681  TYR   A OH   1 
ATOM   1412 N  N    . TYR   A 1 164 ? -33.439 26.093  -4.921  1.00 64.71  ? 682  TYR   A N    1 
ATOM   1413 C  CA   . TYR   A 1 164 ? -33.124 24.869  -4.192  1.00 57.77  ? 682  TYR   A CA   1 
ATOM   1414 C  C    . TYR   A 1 164 ? -33.106 25.121  -2.690  1.00 58.25  ? 682  TYR   A C    1 
ATOM   1415 O  O    . TYR   A 1 164 ? -33.617 24.308  -1.911  1.00 56.45  ? 682  TYR   A O    1 
ATOM   1416 C  CB   . TYR   A 1 164 ? -31.781 24.304  -4.657  1.00 55.69  ? 682  TYR   A CB   1 
ATOM   1417 C  CG   . TYR   A 1 164 ? -31.235 23.226  -3.748  1.00 59.13  ? 682  TYR   A CG   1 
ATOM   1418 C  CD1  . TYR   A 1 164 ? -31.688 21.918  -3.844  1.00 57.59  ? 682  TYR   A CD1  1 
ATOM   1419 C  CD2  . TYR   A 1 164 ? -30.269 23.516  -2.790  1.00 69.50  ? 682  TYR   A CD2  1 
ATOM   1420 C  CE1  . TYR   A 1 164 ? -31.198 20.928  -3.015  1.00 63.12  ? 682  TYR   A CE1  1 
ATOM   1421 C  CE2  . TYR   A 1 164 ? -29.773 22.532  -1.955  1.00 73.17  ? 682  TYR   A CE2  1 
ATOM   1422 C  CZ   . TYR   A 1 164 ? -30.240 21.240  -2.073  1.00 72.17  ? 682  TYR   A CZ   1 
ATOM   1423 O  OH   . TYR   A 1 164 ? -29.748 20.257  -1.245  1.00 76.02  ? 682  TYR   A OH   1 
ATOM   1424 N  N    . ASN   A 1 165 ? -32.518 26.245  -2.268  1.00 62.54  ? 683  ASN   A N    1 
ATOM   1425 C  CA   . ASN   A 1 165 ? -32.518 26.600  -0.852  1.00 68.15  ? 683  ASN   A CA   1 
ATOM   1426 C  C    . ASN   A 1 165 ? -33.937 26.778  -0.328  1.00 67.28  ? 683  ASN   A C    1 
ATOM   1427 O  O    . ASN   A 1 165 ? -34.258 26.337  0.782   1.00 65.23  ? 683  ASN   A O    1 
ATOM   1428 C  CB   . ASN   A 1 165 ? -31.711 27.879  -0.628  1.00 72.54  ? 683  ASN   A CB   1 
ATOM   1429 C  CG   . ASN   A 1 165 ? -30.227 27.683  -0.854  1.00 78.17  ? 683  ASN   A CG   1 
ATOM   1430 O  OD1  . ASN   A 1 165 ? -29.725 26.559  -0.826  1.00 79.70  ? 683  ASN   A OD1  1 
ATOM   1431 N  ND2  . ASN   A 1 165 ? -29.514 28.781  -1.077  1.00 80.16  ? 683  ASN   A ND2  1 
ATOM   1432 N  N    . SER   A 1 166 ? -34.799 27.430  -1.112  1.00 68.66  ? 684  SER   A N    1 
ATOM   1433 C  CA   . SER   A 1 166 ? -36.176 27.649  -0.682  1.00 70.10  ? 684  SER   A CA   1 
ATOM   1434 C  C    . SER   A 1 166 ? -36.916 26.328  -0.522  1.00 61.41  ? 684  SER   A C    1 
ATOM   1435 O  O    . SER   A 1 166 ? -37.608 26.105  0.478   1.00 61.41  ? 684  SER   A O    1 
ATOM   1436 C  CB   . SER   A 1 166 ? -36.899 28.554  -1.681  1.00 73.41  ? 684  SER   A CB   1 
ATOM   1437 O  OG   . SER   A 1 166 ? -36.349 29.859  -1.680  1.00 79.42  ? 684  SER   A OG   1 
ATOM   1438 N  N    . LEU   A 1 167 ? -36.779 25.433  -1.502  1.00 54.07  ? 685  LEU   A N    1 
ATOM   1439 C  CA   . LEU   A 1 167 ? -37.463 24.148  -1.422  1.00 51.82  ? 685  LEU   A CA   1 
ATOM   1440 C  C    . LEU   A 1 167 ? -36.887 23.272  -0.317  1.00 51.07  ? 685  LEU   A C    1 
ATOM   1441 O  O    . LEU   A 1 167 ? -37.628 22.509  0.314   1.00 48.82  ? 685  LEU   A O    1 
ATOM   1442 C  CB   . LEU   A 1 167 ? -37.396 23.435  -2.772  1.00 49.99  ? 685  LEU   A CB   1 
ATOM   1443 C  CG   . LEU   A 1 167 ? -38.126 24.140  -3.920  1.00 51.32  ? 685  LEU   A CG   1 
ATOM   1444 C  CD1  . LEU   A 1 167 ? -37.906 23.410  -5.236  1.00 48.59  ? 685  LEU   A CD1  1 
ATOM   1445 C  CD2  . LEU   A 1 167 ? -39.612 24.274  -3.619  1.00 50.73  ? 685  LEU   A CD2  1 
ATOM   1446 N  N    . ARG   A 1 168 ? -35.579 23.368  -0.059  1.00 53.62  ? 686  ARG   A N    1 
ATOM   1447 C  CA   . ARG   A 1 168 ? -34.997 22.608  1.044   1.00 60.33  ? 686  ARG   A CA   1 
ATOM   1448 C  C    . ARG   A 1 168 ? -35.496 23.125  2.388   1.00 60.76  ? 686  ARG   A C    1 
ATOM   1449 O  O    . ARG   A 1 168 ? -35.706 22.341  3.321   1.00 59.73  ? 686  ARG   A O    1 
ATOM   1450 C  CB   . ARG   A 1 168 ? -33.470 22.655  0.986   1.00 66.59  ? 686  ARG   A CB   1 
ATOM   1451 C  CG   . ARG   A 1 168 ? -32.808 21.505  1.732   1.00 75.11  ? 686  ARG   A CG   1 
ATOM   1452 C  CD   . ARG   A 1 168 ? -31.388 21.833  2.172   1.00 84.63  ? 686  ARG   A CD   1 
ATOM   1453 N  NE   . ARG   A 1 168 ? -30.765 22.864  1.349   1.00 88.61  ? 686  ARG   A NE   1 
ATOM   1454 C  CZ   . ARG   A 1 168 ? -30.318 24.026  1.817   1.00 91.62  ? 686  ARG   A CZ   1 
ATOM   1455 N  NH1  . ARG   A 1 168 ? -30.426 24.310  3.108   1.00 92.28  ? 686  ARG   A NH1  1 
ATOM   1456 N  NH2  . ARG   A 1 168 ? -29.762 24.904  0.993   1.00 91.65  ? 686  ARG   A NH2  1 
ATOM   1457 N  N    . TRP   A 1 169 ? -35.680 24.442  2.506   1.00 62.51  ? 687  TRP   A N    1 
ATOM   1458 C  CA   . TRP   A 1 169 ? -36.303 25.003  3.701   1.00 62.45  ? 687  TRP   A CA   1 
ATOM   1459 C  C    . TRP   A 1 169 ? -37.689 24.410  3.915   1.00 61.76  ? 687  TRP   A C    1 
ATOM   1460 O  O    . TRP   A 1 169 ? -38.026 23.970  5.021   1.00 65.66  ? 687  TRP   A O    1 
ATOM   1461 C  CB   . TRP   A 1 169 ? -36.377 26.527  3.579   1.00 60.16  ? 687  TRP   A CB   1 
ATOM   1462 C  CG   . TRP   A 1 169 ? -36.792 27.241  4.837   1.00 60.01  ? 687  TRP   A CG   1 
ATOM   1463 C  CD1  . TRP   A 1 169 ? -35.975 27.893  5.715   1.00 66.08  ? 687  TRP   A CD1  1 
ATOM   1464 C  CD2  . TRP   A 1 169 ? -38.125 27.393  5.345   1.00 62.90  ? 687  TRP   A CD2  1 
ATOM   1465 N  NE1  . TRP   A 1 169 ? -36.713 28.432  6.740   1.00 68.50  ? 687  TRP   A NE1  1 
ATOM   1466 C  CE2  . TRP   A 1 169 ? -38.036 28.142  6.535   1.00 67.39  ? 687  TRP   A CE2  1 
ATOM   1467 C  CE3  . TRP   A 1 169 ? -39.384 26.967  4.910   1.00 58.61  ? 687  TRP   A CE3  1 
ATOM   1468 C  CZ2  . TRP   A 1 169 ? -39.156 28.467  7.298   1.00 69.05  ? 687  TRP   A CZ2  1 
ATOM   1469 C  CZ3  . TRP   A 1 169 ? -40.492 27.289  5.668   1.00 60.15  ? 687  TRP   A CZ3  1 
ATOM   1470 C  CH2  . TRP   A 1 169 ? -40.372 28.035  6.847   1.00 66.35  ? 687  TRP   A CH2  1 
ATOM   1471 N  N    . ILE   A 1 170 ? -38.507 24.389  2.858   1.00 57.12  ? 688  ILE   A N    1 
ATOM   1472 C  CA   . ILE   A 1 170 ? -39.856 23.835  2.955   1.00 60.13  ? 688  ILE   A CA   1 
ATOM   1473 C  C    . ILE   A 1 170 ? -39.809 22.389  3.429   1.00 59.26  ? 688  ILE   A C    1 
ATOM   1474 O  O    . ILE   A 1 170 ? -40.606 21.970  4.277   1.00 62.98  ? 688  ILE   A O    1 
ATOM   1475 C  CB   . ILE   A 1 170 ? -40.581 23.957  1.601   1.00 57.90  ? 688  ILE   A CB   1 
ATOM   1476 C  CG1  . ILE   A 1 170 ? -40.801 25.425  1.233   1.00 59.93  ? 688  ILE   A CG1  1 
ATOM   1477 C  CG2  . ILE   A 1 170 ? -41.905 23.207  1.631   1.00 55.07  ? 688  ILE   A CG2  1 
ATOM   1478 C  CD1  . ILE   A 1 170 ? -41.392 25.614  -0.150  1.00 56.45  ? 688  ILE   A CD1  1 
ATOM   1479 N  N    . LEU   A 1 171 ? -38.872 21.606  2.893   1.00 55.64  ? 689  LEU   A N    1 
ATOM   1480 C  CA   . LEU   A 1 171 ? -38.777 20.201  3.267   1.00 58.06  ? 689  LEU   A CA   1 
ATOM   1481 C  C    . LEU   A 1 171 ? -38.405 20.027  4.734   1.00 71.95  ? 689  LEU   A C    1 
ATOM   1482 O  O    . LEU   A 1 171 ? -38.863 19.078  5.382   1.00 78.44  ? 689  LEU   A O    1 
ATOM   1483 C  CB   . LEU   A 1 171 ? -37.755 19.499  2.373   1.00 56.15  ? 689  LEU   A CB   1 
ATOM   1484 C  CG   . LEU   A 1 171 ? -37.618 17.983  2.509   1.00 61.67  ? 689  LEU   A CG   1 
ATOM   1485 C  CD1  . LEU   A 1 171 ? -38.794 17.284  1.849   1.00 62.17  ? 689  LEU   A CD1  1 
ATOM   1486 C  CD2  . LEU   A 1 171 ? -36.303 17.514  1.906   1.00 63.35  ? 689  LEU   A CD2  1 
ATOM   1487 N  N    . GLU   A 1 172 ? -37.595 20.933  5.281   1.00 73.13  ? 690  GLU   A N    1 
ATOM   1488 C  CA   . GLU   A 1 172 ? -37.055 20.759  6.622   1.00 77.86  ? 690  GLU   A CA   1 
ATOM   1489 C  C    . GLU   A 1 172 ? -37.901 21.403  7.713   1.00 77.66  ? 690  GLU   A C    1 
ATOM   1490 O  O    . GLU   A 1 172 ? -37.706 21.083  8.891   1.00 82.12  ? 690  GLU   A O    1 
ATOM   1491 C  CB   . GLU   A 1 172 ? -35.632 21.322  6.690   1.00 81.41  ? 690  GLU   A CB   1 
ATOM   1492 C  CG   . GLU   A 1 172 ? -34.646 20.598  5.789   1.00 83.47  ? 690  GLU   A CG   1 
ATOM   1493 C  CD   . GLU   A 1 172 ? -33.282 21.257  5.765   1.00 88.63  ? 690  GLU   A CD   1 
ATOM   1494 O  OE1  . GLU   A 1 172 ? -32.377 20.724  5.088   1.00 89.14  ? 690  GLU   A OE1  1 
ATOM   1495 O  OE2  . GLU   A 1 172 ? -33.113 22.305  6.422   1.00 92.72  ? 690  GLU   A OE2  1 
ATOM   1496 N  N    . ASN   A 1 173 ? -38.826 22.292  7.362   1.00 73.67  ? 691  ASN   A N    1 
ATOM   1497 C  CA   . ASN   A 1 173 ? -39.634 22.999  8.345   1.00 74.50  ? 691  ASN   A CA   1 
ATOM   1498 C  C    . ASN   A 1 173 ? -41.104 22.927  7.956   1.00 72.88  ? 691  ASN   A C    1 
ATOM   1499 O  O    . ASN   A 1 173 ? -41.451 22.640  6.808   1.00 76.00  ? 691  ASN   A O    1 
ATOM   1500 C  CB   . ASN   A 1 173 ? -39.198 24.466  8.474   1.00 81.37  ? 691  ASN   A CB   1 
ATOM   1501 C  CG   . ASN   A 1 173 ? -37.692 24.620  8.565   1.00 91.71  ? 691  ASN   A CG   1 
ATOM   1502 O  OD1  . ASN   A 1 173 ? -37.021 23.872  9.275   1.00 98.64  ? 691  ASN   A OD1  1 
ATOM   1503 N  ND2  . ASN   A 1 173 ? -37.153 25.589  7.839   1.00 92.72  ? 691  ASN   A ND2  1 
ATOM   1504 N  N    . ASP   A 1 174 ? -41.967 23.186  8.930   1.00 67.45  ? 692  ASP   A N    1 
ATOM   1505 C  CA   . ASP   A 1 174 ? -43.397 23.273  8.656   1.00 67.15  ? 692  ASP   A CA   1 
ATOM   1506 C  C    . ASP   A 1 174 ? -43.678 24.551  7.877   1.00 68.54  ? 692  ASP   A C    1 
ATOM   1507 O  O    . ASP   A 1 174 ? -43.445 25.648  8.404   1.00 73.54  ? 692  ASP   A O    1 
ATOM   1508 C  CB   . ASP   A 1 174 ? -44.201 23.251  9.954   1.00 72.05  ? 692  ASP   A CB   1 
ATOM   1509 C  CG   . ASP   A 1 174 ? -45.677 22.957  9.728   1.00 76.12  ? 692  ASP   A CG   1 
ATOM   1510 O  OD1  . ASP   A 1 174 ? -46.174 23.175  8.603   1.00 74.80  ? 692  ASP   A OD1  1 
ATOM   1511 O  OD2  . ASP   A 1 174 ? -46.344 22.501  10.680  1.00 80.28  ? 692  ASP   A OD2  1 
ATOM   1512 N  N    . PRO   A 1 175 ? -44.165 24.468  6.642   1.00 64.55  ? 693  PRO   A N    1 
ATOM   1513 C  CA   . PRO   A 1 175 ? -44.413 25.674  5.840   1.00 64.91  ? 693  PRO   A CA   1 
ATOM   1514 C  C    . PRO   A 1 175 ? -45.819 26.246  5.958   1.00 63.96  ? 693  PRO   A C    1 
ATOM   1515 O  O    . PRO   A 1 175 ? -46.145 27.168  5.205   1.00 67.48  ? 693  PRO   A O    1 
ATOM   1516 C  CB   . PRO   A 1 175 ? -44.170 25.170  4.407   1.00 63.90  ? 693  PRO   A CB   1 
ATOM   1517 C  CG   . PRO   A 1 175 ? -44.193 23.637  4.484   1.00 63.54  ? 693  PRO   A CG   1 
ATOM   1518 C  CD   . PRO   A 1 175 ? -44.503 23.248  5.896   1.00 65.52  ? 693  PRO   A CD   1 
ATOM   1519 N  N    . THR   A 1 176 ? -46.641 25.737  6.879   1.00 63.53  ? 694  THR   A N    1 
ATOM   1520 C  CA   . THR   A 1 176 ? -48.059 26.089  6.892   1.00 68.26  ? 694  THR   A CA   1 
ATOM   1521 C  C    . THR   A 1 176 ? -48.272 27.583  7.107   1.00 68.06  ? 694  THR   A C    1 
ATOM   1522 O  O    . THR   A 1 176 ? -49.137 28.191  6.465   1.00 67.25  ? 694  THR   A O    1 
ATOM   1523 C  CB   . THR   A 1 176 ? -48.789 25.289  7.971   1.00 72.68  ? 694  THR   A CB   1 
ATOM   1524 O  OG1  . THR   A 1 176 ? -48.320 23.935  7.964   1.00 74.97  ? 694  THR   A OG1  1 
ATOM   1525 C  CG2  . THR   A 1 176 ? -50.290 25.303  7.720   1.00 70.83  ? 694  THR   A CG2  1 
ATOM   1526 N  N    . GLU   A 1 177 ? -47.493 28.197  8.001   1.00 67.90  ? 695  GLU   A N    1 
ATOM   1527 C  CA   . GLU   A 1 177 ? -47.727 29.596  8.340   1.00 69.38  ? 695  GLU   A CA   1 
ATOM   1528 C  C    . GLU   A 1 177 ? -47.348 30.547  7.211   1.00 66.17  ? 695  GLU   A C    1 
ATOM   1529 O  O    . GLU   A 1 177 ? -47.811 31.692  7.206   1.00 71.10  ? 695  GLU   A O    1 
ATOM   1530 C  CB   . GLU   A 1 177 ? -46.968 29.965  9.614   1.00 77.81  ? 695  GLU   A CB   1 
ATOM   1531 C  CG   . GLU   A 1 177 ? -47.489 29.256  10.854  1.00 89.66  ? 695  GLU   A CG   1 
ATOM   1532 C  CD   . GLU   A 1 177 ? -47.124 29.974  12.136  1.00 103.67 ? 695  GLU   A CD   1 
ATOM   1533 O  OE1  . GLU   A 1 177 ? -48.043 30.447  12.836  1.00 108.20 ? 695  GLU   A OE1  1 
ATOM   1534 O  OE2  . GLU   A 1 177 ? -45.917 30.065  12.445  1.00 109.49 ? 695  GLU   A OE2  1 
ATOM   1535 N  N    . LEU   A 1 178 ? -46.526 30.107  6.256   1.00 62.53  ? 696  LEU   A N    1 
ATOM   1536 C  CA   . LEU   A 1 178 ? -46.231 30.950  5.104   1.00 61.89  ? 696  LEU   A CA   1 
ATOM   1537 C  C    . LEU   A 1 178 ? -47.397 31.040  4.131   1.00 59.01  ? 696  LEU   A C    1 
ATOM   1538 O  O    . LEU   A 1 178 ? -47.366 31.892  3.237   1.00 58.68  ? 696  LEU   A O    1 
ATOM   1539 C  CB   . LEU   A 1 178 ? -44.993 30.438  4.369   1.00 61.42  ? 696  LEU   A CB   1 
ATOM   1540 C  CG   . LEU   A 1 178 ? -43.646 30.781  5.004   1.00 65.05  ? 696  LEU   A CG   1 
ATOM   1541 C  CD1  . LEU   A 1 178 ? -42.612 29.753  4.595   1.00 66.54  ? 696  LEU   A CD1  1 
ATOM   1542 C  CD2  . LEU   A 1 178 ? -43.198 32.183  4.619   1.00 60.97  ? 696  LEU   A CD2  1 
ATOM   1543 N  N    . ASP   A 1 179 ? -48.409 30.183  4.283   1.00 58.66  ? 697  ASP   A N    1 
ATOM   1544 C  CA   . ASP   A 1 179 ? -49.601 30.201  3.435   1.00 56.35  ? 697  ASP   A CA   1 
ATOM   1545 C  C    . ASP   A 1 179 ? -49.237 30.046  1.961   1.00 51.23  ? 697  ASP   A C    1 
ATOM   1546 O  O    . ASP   A 1 179 ? -49.823 30.684  1.084   1.00 52.19  ? 697  ASP   A O    1 
ATOM   1547 C  CB   . ASP   A 1 179 ? -50.425 31.470  3.668   1.00 64.39  ? 697  ASP   A CB   1 
ATOM   1548 C  CG   . ASP   A 1 179 ? -51.876 31.305  3.261   1.00 68.78  ? 697  ASP   A CG   1 
ATOM   1549 O  OD1  . ASP   A 1 179 ? -52.510 32.318  2.898   1.00 72.39  ? 697  ASP   A OD1  1 
ATOM   1550 O  OD2  . ASP   A 1 179 ? -52.379 30.163  3.299   1.00 68.88  ? 697  ASP   A OD2  1 
ATOM   1551 N  N    . LEU   A 1 180 ? -48.249 29.199  1.687   1.00 51.27  ? 698  LEU   A N    1 
ATOM   1552 C  CA   . LEU   A 1 180 ? -47.919 28.867  0.310   1.00 48.35  ? 698  LEU   A CA   1 
ATOM   1553 C  C    . LEU   A 1 180 ? -49.047 28.057  -0.312  1.00 46.70  ? 698  LEU   A C    1 
ATOM   1554 O  O    . LEU   A 1 180 ? -49.665 27.214  0.344   1.00 51.01  ? 698  LEU   A O    1 
ATOM   1555 C  CB   . LEU   A 1 180 ? -46.613 28.078  0.244   1.00 45.68  ? 698  LEU   A CB   1 
ATOM   1556 C  CG   . LEU   A 1 180 ? -45.357 28.789  0.745   1.00 48.51  ? 698  LEU   A CG   1 
ATOM   1557 C  CD1  . LEU   A 1 180 ? -44.135 27.919  0.513   1.00 48.43  ? 698  LEU   A CD1  1 
ATOM   1558 C  CD2  . LEU   A 1 180 ? -45.198 30.136  0.060   1.00 50.21  ? 698  LEU   A CD2  1 
ATOM   1559 N  N    . ARG   A 1 181 ? -49.318 28.321  -1.583  1.00 44.31  ? 699  ARG   A N    1 
ATOM   1560 C  CA   . ARG   A 1 181 ? -50.348 27.613  -2.322  1.00 44.94  ? 699  ARG   A CA   1 
ATOM   1561 C  C    . ARG   A 1 181 ? -49.713 26.747  -3.399  1.00 45.30  ? 699  ARG   A C    1 
ATOM   1562 O  O    . ARG   A 1 181 ? -48.540 26.907  -3.747  1.00 45.88  ? 699  ARG   A O    1 
ATOM   1563 C  CB   . ARG   A 1 181 ? -51.348 28.592  -2.947  1.00 46.18  ? 699  ARG   A CB   1 
ATOM   1564 C  CG   . ARG   A 1 181 ? -51.920 29.588  -1.955  1.00 48.85  ? 699  ARG   A CG   1 
ATOM   1565 C  CD   . ARG   A 1 181 ? -52.628 28.872  -0.815  1.00 50.57  ? 699  ARG   A CD   1 
ATOM   1566 N  NE   . ARG   A 1 181 ? -53.212 29.805  0.145   1.00 52.84  ? 699  ARG   A NE   1 
ATOM   1567 C  CZ   . ARG   A 1 181 ? -54.406 30.371  0.004   1.00 53.17  ? 699  ARG   A CZ   1 
ATOM   1568 N  NH1  . ARG   A 1 181 ? -55.147 30.103  -1.064  1.00 51.19  ? 699  ARG   A NH1  1 
ATOM   1569 N  NH2  . ARG   A 1 181 ? -54.860 31.207  0.928   1.00 49.82  ? 699  ARG   A NH2  1 
ATOM   1570 N  N    . PHE   A 1 182 ? -50.507 25.814  -3.923  1.00 45.20  ? 700  PHE   A N    1 
ATOM   1571 C  CA   . PHE   A 1 182 ? -50.051 24.915  -4.981  1.00 44.75  ? 700  PHE   A CA   1 
ATOM   1572 C  C    . PHE   A 1 182 ? -50.086 25.633  -6.333  1.00 48.00  ? 700  PHE   A C    1 
ATOM   1573 O  O    . PHE   A 1 182 ? -50.811 25.268  -7.257  1.00 44.33  ? 700  PHE   A O    1 
ATOM   1574 C  CB   . PHE   A 1 182 ? -50.894 23.647  -4.994  1.00 42.31  ? 700  PHE   A CB   1 
ATOM   1575 C  CG   . PHE   A 1 182 ? -50.384 22.575  -4.073  1.00 41.69  ? 700  PHE   A CG   1 
ATOM   1576 C  CD1  . PHE   A 1 182 ? -49.874 21.391  -4.579  1.00 38.51  ? 700  PHE   A CD1  1 
ATOM   1577 C  CD2  . PHE   A 1 182 ? -50.407 22.756  -2.700  1.00 43.98  ? 700  PHE   A CD2  1 
ATOM   1578 C  CE1  . PHE   A 1 182 ? -49.403 20.406  -3.732  1.00 43.65  ? 700  PHE   A CE1  1 
ATOM   1579 C  CE2  . PHE   A 1 182 ? -49.937 21.774  -1.849  1.00 46.68  ? 700  PHE   A CE2  1 
ATOM   1580 C  CZ   . PHE   A 1 182 ? -49.434 20.598  -2.366  1.00 45.19  ? 700  PHE   A CZ   1 
ATOM   1581 N  N    . ILE   A 1 183 ? -49.279 26.693  -6.423  1.00 49.16  ? 701  ILE   A N    1 
ATOM   1582 C  CA   . ILE   A 1 183 ? -49.148 27.493  -7.633  1.00 52.58  ? 701  ILE   A CA   1 
ATOM   1583 C  C    . ILE   A 1 183 ? -47.675 27.806  -7.855  1.00 55.41  ? 701  ILE   A C    1 
ATOM   1584 O  O    . ILE   A 1 183 ? -46.848 27.701  -6.947  1.00 55.51  ? 701  ILE   A O    1 
ATOM   1585 C  CB   . ILE   A 1 183 ? -49.961 28.809  -7.572  1.00 57.09  ? 701  ILE   A CB   1 
ATOM   1586 C  CG1  . ILE   A 1 183 ? -49.437 29.710  -6.455  1.00 59.81  ? 701  ILE   A CG1  1 
ATOM   1587 C  CG2  . ILE   A 1 183 ? -51.442 28.534  -7.374  1.00 57.90  ? 701  ILE   A CG2  1 
ATOM   1588 C  CD1  . ILE   A 1 183 ? -50.106 31.066  -6.408  1.00 64.24  ? 701  ILE   A CD1  1 
ATOM   1589 N  N    . ILE   A 1 184 ? -47.356 28.203  -9.086  1.00 57.00  ? 702  ILE   A N    1 
ATOM   1590 C  CA   . ILE   A 1 184 ? -46.004 28.588  -9.473  1.00 60.97  ? 702  ILE   A CA   1 
ATOM   1591 C  C    . ILE   A 1 184 ? -46.077 29.926  -10.193 1.00 61.68  ? 702  ILE   A C    1 
ATOM   1592 O  O    . ILE   A 1 184 ? -46.872 30.089  -11.125 1.00 60.85  ? 702  ILE   A O    1 
ATOM   1593 C  CB   . ILE   A 1 184 ? -45.340 27.527  -10.372 1.00 64.10  ? 702  ILE   A CB   1 
ATOM   1594 C  CG1  . ILE   A 1 184 ? -44.814 26.367  -9.529  1.00 68.09  ? 702  ILE   A CG1  1 
ATOM   1595 C  CG2  . ILE   A 1 184 ? -44.211 28.139  -11.187 1.00 65.99  ? 702  ILE   A CG2  1 
ATOM   1596 C  CD1  . ILE   A 1 184 ? -43.711 26.764  -8.576  1.00 71.78  ? 702  ILE   A CD1  1 
ATOM   1597 N  N    . ASP   A 1 185 ? -45.257 30.883  -9.759  1.00 67.52  ? 703  ASP   A N    1 
ATOM   1598 C  CA   . ASP   A 1 185 ? -45.161 32.182  -10.412 1.00 77.67  ? 703  ASP   A CA   1 
ATOM   1599 C  C    . ASP   A 1 185 ? -43.817 32.304  -11.109 1.00 85.01  ? 703  ASP   A C    1 
ATOM   1600 O  O    . ASP   A 1 185 ? -42.767 32.115  -10.486 1.00 87.64  ? 703  ASP   A O    1 
ATOM   1601 C  CB   . ASP   A 1 185 ? -45.335 33.333  -9.424  1.00 80.26  ? 703  ASP   A CB   1 
ATOM   1602 C  CG   . ASP   A 1 185 ? -46.688 33.325  -8.785  1.00 86.18  ? 703  ASP   A CG   1 
ATOM   1603 O  OD1  . ASP   A 1 185 ? -47.352 32.276  -8.889  1.00 87.50  ? 703  ASP   A OD1  1 
ATOM   1604 O  OD2  . ASP   A 1 185 ? -47.117 34.365  -8.245  1.00 91.21  ? 703  ASP   A OD2  1 
ATOM   1605 N  N    . GLU   A 1 186 ? -43.859 32.632  -12.394 1.00 90.39  ? 704  GLU   A N    1 
ATOM   1606 C  CA   . GLU   A 1 186 ? -42.673 32.750  -13.224 1.00 91.88  ? 704  GLU   A CA   1 
ATOM   1607 C  C    . GLU   A 1 186 ? -42.559 34.180  -13.734 1.00 90.55  ? 704  GLU   A C    1 
ATOM   1608 O  O    . GLU   A 1 186 ? -43.564 34.806  -14.085 1.00 87.92  ? 704  GLU   A O    1 
ATOM   1609 C  CB   . GLU   A 1 186 ? -42.739 31.763  -14.389 1.00 94.17  ? 704  GLU   A CB   1 
ATOM   1610 C  CG   . GLU   A 1 186 ? -41.400 31.387  -14.975 1.00 97.11  ? 704  GLU   A CG   1 
ATOM   1611 C  CD   . GLU   A 1 186 ? -41.545 30.616  -16.268 1.00 99.68  ? 704  GLU   A CD   1 
ATOM   1612 O  OE1  . GLU   A 1 186 ? -42.695 30.423  -16.715 1.00 100.72 ? 704  GLU   A OE1  1 
ATOM   1613 O  OE2  . GLU   A 1 186 ? -40.513 30.210  -16.842 1.00 100.55 ? 704  GLU   A OE2  1 
ATOM   1614 N  N    . GLU   A 1 187 ? -41.331 34.695  -13.763 1.00 94.46  ? 705  GLU   A N    1 
ATOM   1615 C  CA   . GLU   A 1 187 ? -41.056 36.075  -14.158 1.00 98.17  ? 705  GLU   A CA   1 
ATOM   1616 C  C    . GLU   A 1 187 ? -40.580 36.079  -15.606 1.00 99.61  ? 705  GLU   A C    1 
ATOM   1617 O  O    . GLU   A 1 187 ? -39.397 35.866  -15.882 1.00 103.03 ? 705  GLU   A O    1 
ATOM   1618 C  CB   . GLU   A 1 187 ? -40.018 36.703  -13.234 1.00 98.58  ? 705  GLU   A CB   1 
ATOM   1619 C  CG   . GLU   A 1 187 ? -40.584 37.287  -11.951 1.00 99.02  ? 705  GLU   A CG   1 
ATOM   1620 C  CD   . GLU   A 1 187 ? -41.638 38.345  -12.206 1.00 103.98 ? 705  GLU   A CD   1 
ATOM   1621 O  OE1  . GLU   A 1 187 ? -42.833 37.991  -12.271 1.00 102.73 ? 705  GLU   A OE1  1 
ATOM   1622 O  OE2  . GLU   A 1 187 ? -41.270 39.530  -12.346 1.00 108.42 ? 705  GLU   A OE2  1 
ATOM   1623 N  N    . LEU   A 1 188 ? -41.502 36.332  -16.533 1.00 95.90  ? 706  LEU   A N    1 
ATOM   1624 C  CA   . LEU   A 1 188 ? -41.188 36.365  -17.955 1.00 93.24  ? 706  LEU   A CA   1 
ATOM   1625 C  C    . LEU   A 1 188 ? -41.651 37.685  -18.552 1.00 91.18  ? 706  LEU   A C    1 
ATOM   1626 O  O    . LEU   A 1 188 ? -42.823 38.053  -18.420 1.00 86.92  ? 706  LEU   A O    1 
ATOM   1627 C  CB   . LEU   A 1 188 ? -41.836 35.192  -18.700 1.00 93.11  ? 706  LEU   A CB   1 
ATOM   1628 C  CG   . LEU   A 1 188 ? -41.762 33.808  -18.051 1.00 92.33  ? 706  LEU   A CG   1 
ATOM   1629 C  CD1  . LEU   A 1 188 ? -42.410 32.766  -18.949 1.00 90.69  ? 706  LEU   A CD1  1 
ATOM   1630 C  CD2  . LEU   A 1 188 ? -40.319 33.432  -17.756 1.00 91.88  ? 706  LEU   A CD2  1 
ATOM   1631 N  N    . PHE   A 1 189 ? -40.722 38.390  -19.203 1.00 92.78  ? 707  PHE   A N    1 
ATOM   1632 C  CA   . PHE   A 1 189 ? -41.023 39.620  -19.939 1.00 93.74  ? 707  PHE   A CA   1 
ATOM   1633 C  C    . PHE   A 1 189 ? -41.615 40.690  -19.024 1.00 100.69 ? 707  PHE   A C    1 
ATOM   1634 O  O    . PHE   A 1 189 ? -42.532 41.422  -19.403 1.00 104.73 ? 707  PHE   A O    1 
ATOM   1635 C  CB   . PHE   A 1 189 ? -41.944 39.333  -21.128 1.00 87.82  ? 707  PHE   A CB   1 
ATOM   1636 C  CG   . PHE   A 1 189 ? -41.449 38.227  -22.020 1.00 84.61  ? 707  PHE   A CG   1 
ATOM   1637 C  CD1  . PHE   A 1 189 ? -41.837 36.915  -21.802 1.00 81.48  ? 707  PHE   A CD1  1 
ATOM   1638 C  CD2  . PHE   A 1 189 ? -40.585 38.500  -23.067 1.00 85.84  ? 707  PHE   A CD2  1 
ATOM   1639 C  CE1  . PHE   A 1 189 ? -41.377 35.895  -22.616 1.00 78.91  ? 707  PHE   A CE1  1 
ATOM   1640 C  CE2  . PHE   A 1 189 ? -40.123 37.484  -23.885 1.00 84.24  ? 707  PHE   A CE2  1 
ATOM   1641 C  CZ   . PHE   A 1 189 ? -40.520 36.180  -23.659 1.00 80.24  ? 707  PHE   A CZ   1 
ATOM   1642 N  N    . GLY   A 1 190 ? -41.078 40.784  -17.809 1.00 102.25 ? 708  GLY   A N    1 
ATOM   1643 C  CA   . GLY   A 1 190 ? -41.520 41.787  -16.862 1.00 106.05 ? 708  GLY   A CA   1 
ATOM   1644 C  C    . GLY   A 1 190 ? -42.916 41.585  -16.324 1.00 104.34 ? 708  GLY   A C    1 
ATOM   1645 O  O    . GLY   A 1 190 ? -43.544 42.550  -15.881 1.00 108.20 ? 708  GLY   A O    1 
ATOM   1646 N  N    . GLN   A 1 191 ? -43.423 40.354  -16.344 1.00 100.42 ? 709  GLN   A N    1 
ATOM   1647 C  CA   . GLN   A 1 191 ? -44.788 40.077  -15.926 1.00 98.47  ? 709  GLN   A CA   1 
ATOM   1648 C  C    . GLN   A 1 191 ? -44.834 38.773  -15.145 1.00 96.57  ? 709  GLN   A C    1 
ATOM   1649 O  O    . GLN   A 1 191 ? -44.061 37.847  -15.402 1.00 93.70  ? 709  GLN   A O    1 
ATOM   1650 C  CB   . GLN   A 1 191 ? -45.737 40.002  -17.130 1.00 97.17  ? 709  GLN   A CB   1 
ATOM   1651 C  CG   . GLN   A 1 191 ? -45.952 41.335  -17.825 1.00 100.85 ? 709  GLN   A CG   1 
ATOM   1652 C  CD   . GLN   A 1 191 ? -46.785 42.289  -16.994 1.00 100.99 ? 709  GLN   A CD   1 
ATOM   1653 O  OE1  . GLN   A 1 191 ? -47.667 41.869  -16.245 1.00 98.87  ? 709  GLN   A OE1  1 
ATOM   1654 N  NE2  . GLN   A 1 191 ? -46.506 43.581  -17.118 1.00 105.24 ? 709  GLN   A NE2  1 
ATOM   1655 N  N    . THR   A 1 192 ? -45.756 38.712  -14.187 1.00 97.00  ? 710  THR   A N    1 
ATOM   1656 C  CA   . THR   A 1 192 ? -45.959 37.506  -13.397 1.00 93.13  ? 710  THR   A CA   1 
ATOM   1657 C  C    . THR   A 1 192 ? -46.865 36.536  -14.144 1.00 86.45  ? 710  THR   A C    1 
ATOM   1658 O  O    . THR   A 1 192 ? -47.932 36.922  -14.634 1.00 91.13  ? 710  THR   A O    1 
ATOM   1659 C  CB   . THR   A 1 192 ? -46.573 37.850  -12.039 1.00 96.50  ? 710  THR   A CB   1 
ATOM   1660 O  OG1  . THR   A 1 192 ? -47.911 38.329  -12.227 1.00 100.37 ? 710  THR   A OG1  1 
ATOM   1661 C  CG2  . THR   A 1 192 ? -45.762 38.927  -11.341 1.00 99.42  ? 710  THR   A CG2  1 
ATOM   1662 N  N    . HIS   A 1 193 ? -46.435 35.278  -14.232 1.00 75.26  ? 711  HIS   A N    1 
ATOM   1663 C  CA   . HIS   A 1 193 ? -47.233 34.196  -14.800 1.00 68.66  ? 711  HIS   A CA   1 
ATOM   1664 C  C    . HIS   A 1 193 ? -47.530 33.200  -13.692 1.00 59.23  ? 711  HIS   A C    1 
ATOM   1665 O  O    . HIS   A 1 193 ? -46.620 32.513  -13.210 1.00 56.10  ? 711  HIS   A O    1 
ATOM   1666 C  CB   . HIS   A 1 193 ? -46.509 33.498  -15.952 1.00 70.50  ? 711  HIS   A CB   1 
ATOM   1667 C  CG   . HIS   A 1 193 ? -46.385 34.332  -17.188 1.00 77.80  ? 711  HIS   A CG   1 
ATOM   1668 N  ND1  . HIS   A 1 193 ? -46.085 33.789  -18.420 1.00 78.60  ? 711  HIS   A ND1  1 
ATOM   1669 C  CD2  . HIS   A 1 193 ? -46.493 35.668  -17.383 1.00 81.75  ? 711  HIS   A CD2  1 
ATOM   1670 C  CE1  . HIS   A 1 193 ? -46.032 34.751  -19.323 1.00 81.38  ? 711  HIS   A CE1  1 
ATOM   1671 N  NE2  . HIS   A 1 193 ? -46.272 35.902  -18.720 1.00 84.75  ? 711  HIS   A NE2  1 
ATOM   1672 N  N    . GLN   A 1 194 ? -48.796 33.106  -13.307 1.00 58.73  ? 712  GLN   A N    1 
ATOM   1673 C  CA   . GLN   A 1 194 ? -49.207 32.154  -12.293 1.00 56.73  ? 712  GLN   A CA   1 
ATOM   1674 C  C    . GLN   A 1 194 ? -49.732 30.879  -12.926 1.00 58.17  ? 712  GLN   A C    1 
ATOM   1675 O  O    . GLN   A 1 194 ? -50.501 30.906  -13.893 1.00 59.06  ? 712  GLN   A O    1 
ATOM   1676 C  CB   . GLN   A 1 194 ? -50.256 32.741  -11.354 1.00 61.62  ? 712  GLN   A CB   1 
ATOM   1677 C  CG   . GLN   A 1 194 ? -49.580 33.496  -10.259 1.00 70.12  ? 712  GLN   A CG   1 
ATOM   1678 C  CD   . GLN   A 1 194 ? -50.517 34.174  -9.312  1.00 77.49  ? 712  GLN   A CD   1 
ATOM   1679 O  OE1  . GLN   A 1 194 ? -50.967 33.570  -8.336  1.00 77.22  ? 712  GLN   A OE1  1 
ATOM   1680 N  NE2  . GLN   A 1 194 ? -50.777 35.454  -9.548  1.00 82.91  ? 712  GLN   A NE2  1 
ATOM   1681 N  N    . HIS   A 1 195 ? -49.303 29.762  -12.360 1.00 51.65  ? 713  HIS   A N    1 
ATOM   1682 C  CA   . HIS   A 1 195 ? -49.742 28.432  -12.750 1.00 55.20  ? 713  HIS   A CA   1 
ATOM   1683 C  C    . HIS   A 1 195 ? -50.037 27.690  -11.468 1.00 52.00  ? 713  HIS   A C    1 
ATOM   1684 O  O    . HIS   A 1 195 ? -49.114 27.376  -10.703 1.00 51.60  ? 713  HIS   A O    1 
ATOM   1685 C  CB   . HIS   A 1 195 ? -48.621 27.788  -13.592 1.00 53.69  ? 713  HIS   A CB   1 
ATOM   1686 C  CG   . HIS   A 1 195 ? -48.924 26.449  -14.213 1.00 58.03  ? 713  HIS   A CG   1 
ATOM   1687 N  ND1  . HIS   A 1 195 ? -48.169 25.318  -13.955 1.00 58.50  ? 713  HIS   A ND1  1 
ATOM   1688 C  CD2  . HIS   A 1 195 ? -49.881 26.061  -15.095 1.00 61.85  ? 713  HIS   A CD2  1 
ATOM   1689 C  CE1  . HIS   A 1 195 ? -48.626 24.306  -14.676 1.00 58.76  ? 713  HIS   A CE1  1 
ATOM   1690 N  NE2  . HIS   A 1 195 ? -49.673 24.726  -15.365 1.00 60.35  ? 713  HIS   A NE2  1 
ATOM   1691 N  N    . GLU   A 1 196 ? -51.320 27.494  -11.191 1.00 55.30  ? 714  GLU   A N    1 
ATOM   1692 C  CA   . GLU   A 1 196 ? -51.716 26.489  -10.206 1.00 59.05  ? 714  GLU   A CA   1 
ATOM   1693 C  C    . GLU   A 1 196 ? -50.882 25.228  -10.414 1.00 63.16  ? 714  GLU   A C    1 
ATOM   1694 O  O    . GLU   A 1 196 ? -50.336 25.038  -11.514 1.00 74.99  ? 714  GLU   A O    1 
ATOM   1695 C  CB   . GLU   A 1 196 ? -53.241 26.233  -10.267 1.00 60.37  ? 714  GLU   A CB   1 
ATOM   1696 C  CG   . GLU   A 1 196 ? -53.773 25.510  -11.482 1.00 61.19  ? 714  GLU   A CG   1 
ATOM   1697 C  CD   . GLU   A 1 196 ? -55.281 25.208  -11.428 1.00 61.32  ? 714  GLU   A CD   1 
ATOM   1698 O  OE1  . GLU   A 1 196 ? -55.965 25.769  -10.562 1.00 62.15  ? 714  GLU   A OE1  1 
ATOM   1699 O  OE2  . GLU   A 1 196 ? -55.784 24.393  -12.241 1.00 60.73  ? 714  GLU   A OE2  1 
ATOM   1700 N  N    . LEU   A 1 197 ? -50.771 24.392  -9.358  1.00 58.48  ? 715  LEU   A N    1 
ATOM   1701 C  CA   . LEU   A 1 197 ? -49.981 23.183  -9.532  1.00 51.97  ? 715  LEU   A CA   1 
ATOM   1702 C  C    . LEU   A 1 197 ? -50.793 21.911  -9.606  1.00 52.58  ? 715  LEU   A C    1 
ATOM   1703 O  O    . LEU   A 1 197 ? -50.252 20.878  -9.993  1.00 47.85  ? 715  LEU   A O    1 
ATOM   1704 C  CB   . LEU   A 1 197 ? -48.901 23.007  -8.484  1.00 52.97  ? 715  LEU   A CB   1 
ATOM   1705 C  CG   . LEU   A 1 197 ? -47.575 23.735  -8.726  1.00 50.67  ? 715  LEU   A CG   1 
ATOM   1706 C  CD1  . LEU   A 1 197 ? -46.764 23.730  -7.458  1.00 49.33  ? 715  LEU   A CD1  1 
ATOM   1707 C  CD2  . LEU   A 1 197 ? -46.748 23.114  -9.884  1.00 49.62  ? 715  LEU   A CD2  1 
ATOM   1708 N  N    . LYS   A 1 198 ? -52.035 21.949  -9.188  1.00 53.07  ? 716  LYS   A N    1 
ATOM   1709 C  CA   . LYS   A 1 198 ? -53.012 20.926  -9.476  1.00 54.18  ? 716  LYS   A CA   1 
ATOM   1710 C  C    . LYS   A 1 198 ? -54.317 21.677  -9.542  1.00 50.66  ? 716  LYS   A C    1 
ATOM   1711 O  O    . LYS   A 1 198 ? -54.346 22.887  -9.321  1.00 46.91  ? 716  LYS   A O    1 
ATOM   1712 C  CB   . LYS   A 1 198 ? -53.003 19.815  -8.428  1.00 55.86  ? 716  LYS   A CB   1 
ATOM   1713 C  CG   . LYS   A 1 198 ? -53.377 20.332  -7.078  1.00 56.76  ? 716  LYS   A CG   1 
ATOM   1714 C  CD   . LYS   A 1 198 ? -52.729 19.438  -6.088  1.00 60.34  ? 716  LYS   A CD   1 
ATOM   1715 C  CE   . LYS   A 1 198 ? -53.361 18.089  -6.237  1.00 62.84  ? 716  LYS   A CE   1 
ATOM   1716 N  NZ   . LYS   A 1 198 ? -53.583 17.454  -4.930  1.00 65.11  ? 716  LYS   A NZ   1 
ATOM   1717 N  N    . ASN   A 1 199 ? -55.381 20.969  -9.898  1.00 48.91  ? 717  ASN   A N    1 
ATOM   1718 C  CA   . ASN   A 1 199 ? -56.686 21.600  -10.014 1.00 46.83  ? 717  ASN   A CA   1 
ATOM   1719 C  C    . ASN   A 1 199 ? -57.070 22.282  -8.709  1.00 49.06  ? 717  ASN   A C    1 
ATOM   1720 O  O    . ASN   A 1 199 ? -57.012 21.672  -7.638  1.00 52.42  ? 717  ASN   A O    1 
ATOM   1721 C  CB   . ASN   A 1 199 ? -57.720 20.545  -10.384 1.00 57.41  ? 717  ASN   A CB   1 
ATOM   1722 C  CG   . ASN   A 1 199 ? -59.068 21.132  -10.662 1.00 68.74  ? 717  ASN   A CG   1 
ATOM   1723 O  OD1  . ASN   A 1 199 ? -59.188 22.169  -11.314 1.00 72.44  ? 717  ASN   A OD1  1 
ATOM   1724 N  ND2  . ASN   A 1 199 ? -60.109 20.475  -10.155 1.00 73.57  ? 717  ASN   A ND2  1 
ATOM   1725 N  N    . GLY   A 1 200 ? -57.475 23.546  -8.806  1.00 50.05  ? 718  GLY   A N    1 
ATOM   1726 C  CA   . GLY   A 1 200 ? -57.770 24.328  -7.621  1.00 47.03  ? 718  GLY   A CA   1 
ATOM   1727 C  C    . GLY   A 1 200 ? -56.567 24.620  -6.758  1.00 49.13  ? 718  GLY   A C    1 
ATOM   1728 O  O    . GLY   A 1 200 ? -56.719 24.827  -5.552  1.00 50.59  ? 718  GLY   A O    1 
ATOM   1729 N  N    . GLY   A 1 201 ? -55.370 24.656  -7.352  1.00 49.91  ? 719  GLY   A N    1 
ATOM   1730 C  CA   . GLY   A 1 201 ? -54.155 24.770  -6.562  1.00 48.36  ? 719  GLY   A CA   1 
ATOM   1731 C  C    . GLY   A 1 201 ? -54.065 26.044  -5.745  1.00 46.92  ? 719  GLY   A C    1 
ATOM   1732 O  O    . GLY   A 1 201 ? -53.456 26.053  -4.671  1.00 44.94  ? 719  GLY   A O    1 
ATOM   1733 N  N    . SER   A 1 202 ? -54.671 27.131  -6.229  1.00 48.24  ? 720  SER   A N    1 
ATOM   1734 C  CA   . SER   A 1 202 ? -54.574 28.403  -5.520  1.00 50.11  ? 720  SER   A CA   1 
ATOM   1735 C  C    . SER   A 1 202 ? -55.230 28.356  -4.147  1.00 49.13  ? 720  SER   A C    1 
ATOM   1736 O  O    . SER   A 1 202 ? -54.897 29.177  -3.286  1.00 51.59  ? 720  SER   A O    1 
ATOM   1737 C  CB   . SER   A 1 202 ? -55.194 29.527  -6.354  1.00 54.01  ? 720  SER   A CB   1 
ATOM   1738 O  OG   . SER   A 1 202 ? -56.490 29.180  -6.804  1.00 61.85  ? 720  SER   A OG   1 
ATOM   1739 N  N    . GLU   A 1 203 ? -56.142 27.414  -3.915  1.00 47.45  ? 721  GLU   A N    1 
ATOM   1740 C  CA   . GLU   A 1 203 ? -56.831 27.301  -2.637  1.00 51.81  ? 721  GLU   A CA   1 
ATOM   1741 C  C    . GLU   A 1 203 ? -56.256 26.213  -1.737  1.00 51.07  ? 721  GLU   A C    1 
ATOM   1742 O  O    . GLU   A 1 203 ? -56.773 26.006  -0.636  1.00 52.94  ? 721  GLU   A O    1 
ATOM   1743 C  CB   . GLU   A 1 203 ? -58.325 27.043  -2.867  1.00 56.69  ? 721  GLU   A CB   1 
ATOM   1744 C  CG   . GLU   A 1 203 ? -58.967 27.960  -3.902  1.00 65.88  ? 721  GLU   A CG   1 
ATOM   1745 C  CD   . GLU   A 1 203 ? -58.630 29.424  -3.684  1.00 76.56  ? 721  GLU   A CD   1 
ATOM   1746 O  OE1  . GLU   A 1 203 ? -58.207 30.087  -4.655  1.00 80.23  ? 721  GLU   A OE1  1 
ATOM   1747 O  OE2  . GLU   A 1 203 ? -58.790 29.912  -2.545  1.00 79.15  ? 721  GLU   A OE2  1 
ATOM   1748 N  N    . ILE   A 1 204 ? -55.202 25.525  -2.167  1.00 48.61  ? 722  ILE   A N    1 
ATOM   1749 C  CA   . ILE   A 1 204 ? -54.617 24.419  -1.414  1.00 44.99  ? 722  ILE   A CA   1 
ATOM   1750 C  C    . ILE   A 1 204 ? -53.370 24.922  -0.698  1.00 43.87  ? 722  ILE   A C    1 
ATOM   1751 O  O    . ILE   A 1 204 ? -52.403 25.349  -1.340  1.00 44.53  ? 722  ILE   A O    1 
ATOM   1752 C  CB   . ILE   A 1 204 ? -54.288 23.231  -2.330  1.00 44.94  ? 722  ILE   A CB   1 
ATOM   1753 C  CG1  . ILE   A 1 204 ? -55.535 22.801  -3.106  1.00 47.98  ? 722  ILE   A CG1  1 
ATOM   1754 C  CG2  . ILE   A 1 204 ? -53.731 22.072  -1.518  1.00 43.32  ? 722  ILE   A CG2  1 
ATOM   1755 C  CD1  . ILE   A 1 204 ? -55.256 21.820  -4.226  1.00 48.58  ? 722  ILE   A CD1  1 
ATOM   1756 N  N    . VAL   A 1 205 ? -53.388 24.861  0.630   1.00 43.50  ? 723  VAL   A N    1 
ATOM   1757 C  CA   . VAL   A 1 205 ? -52.277 25.349  1.441   1.00 48.26  ? 723  VAL   A CA   1 
ATOM   1758 C  C    . VAL   A 1 205 ? -51.214 24.262  1.545   1.00 50.13  ? 723  VAL   A C    1 
ATOM   1759 O  O    . VAL   A 1 205 ? -51.527 23.090  1.786   1.00 45.43  ? 723  VAL   A O    1 
ATOM   1760 C  CB   . VAL   A 1 205 ? -52.771 25.780  2.832   1.00 47.33  ? 723  VAL   A CB   1 
ATOM   1761 C  CG1  . VAL   A 1 205 ? -51.614 26.286  3.679   1.00 49.56  ? 723  VAL   A CG1  1 
ATOM   1762 C  CG2  . VAL   A 1 205 ? -53.848 26.846  2.704   1.00 46.34  ? 723  VAL   A CG2  1 
ATOM   1763 N  N    . VAL   A 1 206 ? -49.954 24.650  1.366   1.00 51.76  ? 724  VAL   A N    1 
ATOM   1764 C  CA   . VAL   A 1 206 ? -48.833 23.723  1.481   1.00 50.14  ? 724  VAL   A CA   1 
ATOM   1765 C  C    . VAL   A 1 206 ? -48.573 23.475  2.963   1.00 59.17  ? 724  VAL   A C    1 
ATOM   1766 O  O    . VAL   A 1 206 ? -48.128 24.371  3.683   1.00 64.87  ? 724  VAL   A O    1 
ATOM   1767 C  CB   . VAL   A 1 206 ? -47.580 24.262  0.783   1.00 49.89  ? 724  VAL   A CB   1 
ATOM   1768 C  CG1  . VAL   A 1 206 ? -46.417 23.295  0.961   1.00 49.31  ? 724  VAL   A CG1  1 
ATOM   1769 C  CG2  . VAL   A 1 206 ? -47.856 24.510  -0.692  1.00 49.85  ? 724  VAL   A CG2  1 
ATOM   1770 N  N    . THR   A 1 207 ? -48.850 22.260  3.420   1.00 59.50  ? 725  THR   A N    1 
ATOM   1771 C  CA   . THR   A 1 207 ? -48.635 21.861  4.804   1.00 59.56  ? 725  THR   A CA   1 
ATOM   1772 C  C    . THR   A 1 207 ? -47.629 20.715  4.854   1.00 60.30  ? 725  THR   A C    1 
ATOM   1773 O  O    . THR   A 1 207 ? -47.102 20.274  3.830   1.00 63.18  ? 725  THR   A O    1 
ATOM   1774 C  CB   . THR   A 1 207 ? -49.952 21.453  5.472   1.00 59.16  ? 725  THR   A CB   1 
ATOM   1775 O  OG1  . THR   A 1 207 ? -50.319 20.135  5.044   1.00 60.50  ? 725  THR   A OG1  1 
ATOM   1776 C  CG2  . THR   A 1 207 ? -51.063 22.429  5.109   1.00 57.49  ? 725  THR   A CG2  1 
ATOM   1777 N  N    . ASN   A 1 208 ? -47.366 20.231  6.070   1.00 60.68  ? 726  ASN   A N    1 
ATOM   1778 C  CA   . ASN   A 1 208 ? -46.454 19.105  6.236   1.00 62.66  ? 726  ASN   A CA   1 
ATOM   1779 C  C    . ASN   A 1 208 ? -46.986 17.848  5.564   1.00 56.62  ? 726  ASN   A C    1 
ATOM   1780 O  O    . ASN   A 1 208 ? -46.203 17.003  5.115   1.00 54.44  ? 726  ASN   A O    1 
ATOM   1781 C  CB   . ASN   A 1 208 ? -46.213 18.836  7.721   1.00 70.86  ? 726  ASN   A CB   1 
ATOM   1782 C  CG   . ASN   A 1 208 ? -44.976 19.529  8.247   1.00 76.11  ? 726  ASN   A CG   1 
ATOM   1783 O  OD1  . ASN   A 1 208 ? -43.970 19.647  7.548   1.00 75.18  ? 726  ASN   A OD1  1 
ATOM   1784 N  ND2  . ASN   A 1 208 ? -45.041 19.986  9.489   1.00 81.80  ? 726  ASN   A ND2  1 
ATOM   1785 N  N    . LYS   A 1 209 ? -48.309 17.710  5.477   1.00 54.74  ? 727  LYS   A N    1 
ATOM   1786 C  CA   . LYS   A 1 209 ? -48.911 16.488  4.962   1.00 53.35  ? 727  LYS   A CA   1 
ATOM   1787 C  C    . LYS   A 1 209 ? -48.834 16.372  3.445   1.00 51.36  ? 727  LYS   A C    1 
ATOM   1788 O  O    . LYS   A 1 209 ? -48.875 15.251  2.926   1.00 53.52  ? 727  LYS   A O    1 
ATOM   1789 C  CB   . LYS   A 1 209 ? -50.371 16.396  5.412   1.00 57.21  ? 727  LYS   A CB   1 
ATOM   1790 C  CG   . LYS   A 1 209 ? -50.557 15.735  6.770   1.00 64.62  ? 727  LYS   A CG   1 
ATOM   1791 C  CD   . LYS   A 1 209 ? -52.003 15.810  7.234   1.00 73.08  ? 727  LYS   A CD   1 
ATOM   1792 C  CE   . LYS   A 1 209 ? -52.236 17.024  8.119   1.00 79.93  ? 727  LYS   A CE   1 
ATOM   1793 N  NZ   . LYS   A 1 209 ? -53.685 17.338  8.260   1.00 83.79  ? 727  LYS   A NZ   1 
ATOM   1794 N  N    . ASN   A 1 210 ? -48.721 17.486  2.720   1.00 44.35  ? 728  ASN   A N    1 
ATOM   1795 C  CA   . ASN   A 1 210 ? -48.715 17.446  1.261   1.00 40.07  ? 728  ASN   A CA   1 
ATOM   1796 C  C    . ASN   A 1 210 ? -47.483 18.096  0.639   1.00 39.44  ? 728  ASN   A C    1 
ATOM   1797 O  O    . ASN   A 1 210 ? -47.463 18.312  -0.579  1.00 40.02  ? 728  ASN   A O    1 
ATOM   1798 C  CB   . ASN   A 1 210 ? -49.990 18.095  0.703   1.00 39.35  ? 728  ASN   A CB   1 
ATOM   1799 C  CG   . ASN   A 1 210 ? -50.136 19.565  1.092   1.00 42.41  ? 728  ASN   A CG   1 
ATOM   1800 O  OD1  . ASN   A 1 210 ? -49.193 20.203  1.560   1.00 42.78  ? 728  ASN   A OD1  1 
ATOM   1801 N  ND2  . ASN   A 1 210 ? -51.331 20.108  0.889   1.00 40.18  ? 728  ASN   A ND2  1 
ATOM   1802 N  N    . LYS   A 1 211 ? -46.450 18.401  1.430   1.00 41.24  ? 729  LYS   A N    1 
ATOM   1803 C  CA   . LYS   A 1 211 ? -45.322 19.156  0.891   1.00 45.10  ? 729  LYS   A CA   1 
ATOM   1804 C  C    . LYS   A 1 211 ? -44.430 18.303  -0.003  1.00 44.22  ? 729  LYS   A C    1 
ATOM   1805 O  O    . LYS   A 1 211 ? -43.828 18.828  -0.947  1.00 44.66  ? 729  LYS   A O    1 
ATOM   1806 C  CB   . LYS   A 1 211 ? -44.505 19.779  2.023   1.00 46.92  ? 729  LYS   A CB   1 
ATOM   1807 C  CG   . LYS   A 1 211 ? -43.842 18.794  2.970   1.00 48.63  ? 729  LYS   A CG   1 
ATOM   1808 C  CD   . LYS   A 1 211 ? -43.075 19.551  4.041   1.00 52.31  ? 729  LYS   A CD   1 
ATOM   1809 C  CE   . LYS   A 1 211 ? -42.335 18.623  4.984   1.00 59.83  ? 729  LYS   A CE   1 
ATOM   1810 N  NZ   . LYS   A 1 211 ? -41.616 19.403  6.030   1.00 66.38  ? 729  LYS   A NZ   1 
ATOM   1811 N  N    . LYS   A 1 212 ? -44.318 17.001  0.274   1.00 44.62  ? 730  LYS   A N    1 
ATOM   1812 C  CA   . LYS   A 1 212 ? -43.575 16.128  -0.630  1.00 44.83  ? 730  LYS   A CA   1 
ATOM   1813 C  C    . LYS   A 1 212 ? -44.192 16.145  -2.022  1.00 43.91  ? 730  LYS   A C    1 
ATOM   1814 O  O    . LYS   A 1 212 ? -43.477 16.227  -3.028  1.00 43.06  ? 730  LYS   A O    1 
ATOM   1815 C  CB   . LYS   A 1 212 ? -43.533 14.702  -0.079  1.00 47.54  ? 730  LYS   A CB   1 
ATOM   1816 C  CG   . LYS   A 1 212 ? -42.736 14.549  1.209   1.00 54.91  ? 730  LYS   A CG   1 
ATOM   1817 C  CD   . LYS   A 1 212 ? -41.246 14.748  0.971   1.00 57.09  ? 730  LYS   A CD   1 
ATOM   1818 C  CE   . LYS   A 1 212 ? -40.602 13.516  0.358   1.00 56.10  ? 730  LYS   A CE   1 
ATOM   1819 N  NZ   . LYS   A 1 212 ? -39.169 13.752  0.024   1.00 53.71  ? 730  LYS   A NZ   1 
ATOM   1820 N  N    . GLU   A 1 213 ? -45.523 16.072  -2.095  1.00 43.48  ? 731  GLU   A N    1 
ATOM   1821 C  CA   . GLU   A 1 213 ? -46.209 16.226  -3.373  1.00 41.29  ? 731  GLU   A CA   1 
ATOM   1822 C  C    . GLU   A 1 213 ? -45.944 17.601  -3.974  1.00 37.81  ? 731  GLU   A C    1 
ATOM   1823 O  O    . GLU   A 1 213 ? -45.711 17.724  -5.183  1.00 36.60  ? 731  GLU   A O    1 
ATOM   1824 C  CB   . GLU   A 1 213 ? -47.709 15.999  -3.185  1.00 45.15  ? 731  GLU   A CB   1 
ATOM   1825 C  CG   . GLU   A 1 213 ? -48.532 16.153  -4.450  1.00 48.76  ? 731  GLU   A CG   1 
ATOM   1826 C  CD   . GLU   A 1 213 ? -50.022 16.127  -4.176  1.00 55.31  ? 731  GLU   A CD   1 
ATOM   1827 O  OE1  . GLU   A 1 213 ? -50.807 16.309  -5.131  1.00 56.85  ? 731  GLU   A OE1  1 
ATOM   1828 O  OE2  . GLU   A 1 213 ? -50.409 15.929  -3.004  1.00 57.47  ? 731  GLU   A OE2  1 
ATOM   1829 N  N    . TYR   A 1 214 ? -45.970 18.646  -3.142  1.00 36.44  ? 732  TYR   A N    1 
ATOM   1830 C  CA   . TYR   A 1 214 ? -45.702 19.998  -3.626  1.00 36.95  ? 732  TYR   A CA   1 
ATOM   1831 C  C    . TYR   A 1 214 ? -44.324 20.087  -4.268  1.00 38.92  ? 732  TYR   A C    1 
ATOM   1832 O  O    . TYR   A 1 214 ? -44.186 20.548  -5.407  1.00 35.58  ? 732  TYR   A O    1 
ATOM   1833 C  CB   . TYR   A 1 214 ? -45.825 21.001  -2.477  1.00 37.97  ? 732  TYR   A CB   1 
ATOM   1834 C  CG   . TYR   A 1 214 ? -45.383 22.407  -2.830  1.00 40.03  ? 732  TYR   A CG   1 
ATOM   1835 C  CD1  . TYR   A 1 214 ? -46.201 23.245  -3.577  1.00 40.29  ? 732  TYR   A CD1  1 
ATOM   1836 C  CD2  . TYR   A 1 214 ? -44.154 22.897  -2.409  1.00 41.99  ? 732  TYR   A CD2  1 
ATOM   1837 C  CE1  . TYR   A 1 214 ? -45.806 24.529  -3.899  1.00 41.56  ? 732  TYR   A CE1  1 
ATOM   1838 C  CE2  . TYR   A 1 214 ? -43.749 24.181  -2.728  1.00 43.15  ? 732  TYR   A CE2  1 
ATOM   1839 C  CZ   . TYR   A 1 214 ? -44.580 24.992  -3.473  1.00 44.76  ? 732  TYR   A CZ   1 
ATOM   1840 O  OH   . TYR   A 1 214 ? -44.186 26.271  -3.794  1.00 47.58  ? 732  TYR   A OH   1 
ATOM   1841 N  N    . ILE   A 1 215 ? -43.290 19.644  -3.548  1.00 40.34  ? 733  ILE   A N    1 
ATOM   1842 C  CA   . ILE   A 1 215 ? -41.929 19.710  -4.075  1.00 39.86  ? 733  ILE   A CA   1 
ATOM   1843 C  C    . ILE   A 1 215 ? -41.817 18.903  -5.360  1.00 41.02  ? 733  ILE   A C    1 
ATOM   1844 O  O    . ILE   A 1 215 ? -41.216 19.354  -6.344  1.00 39.38  ? 733  ILE   A O    1 
ATOM   1845 C  CB   . ILE   A 1 215 ? -40.920 19.234  -3.014  1.00 41.47  ? 733  ILE   A CB   1 
ATOM   1846 C  CG1  . ILE   A 1 215 ? -40.776 20.284  -1.911  1.00 39.90  ? 733  ILE   A CG1  1 
ATOM   1847 C  CG2  . ILE   A 1 215 ? -39.569 18.939  -3.652  1.00 43.35  ? 733  ILE   A CG2  1 
ATOM   1848 C  CD1  . ILE   A 1 215 ? -40.223 19.734  -0.615  1.00 43.99  ? 733  ILE   A CD1  1 
ATOM   1849 N  N    . TYR   A 1 216 ? -42.403 17.702  -5.376  1.00 36.86  ? 734  TYR   A N    1 
ATOM   1850 C  CA   . TYR   A 1 216 ? -42.394 16.887  -6.586  1.00 36.79  ? 734  TYR   A CA   1 
ATOM   1851 C  C    . TYR   A 1 216 ? -43.027 17.630  -7.757  1.00 39.36  ? 734  TYR   A C    1 
ATOM   1852 O  O    . TYR   A 1 216 ? -42.482 17.635  -8.867  1.00 43.98  ? 734  TYR   A O    1 
ATOM   1853 C  CB   . TYR   A 1 216 ? -43.116 15.562  -6.325  1.00 38.34  ? 734  TYR   A CB   1 
ATOM   1854 C  CG   . TYR   A 1 216 ? -43.736 14.930  -7.552  1.00 44.28  ? 734  TYR   A CG   1 
ATOM   1855 C  CD1  . TYR   A 1 216 ? -42.958 14.226  -8.463  1.00 49.65  ? 734  TYR   A CD1  1 
ATOM   1856 C  CD2  . TYR   A 1 216 ? -45.101 15.030  -7.795  1.00 45.12  ? 734  TYR   A CD2  1 
ATOM   1857 C  CE1  . TYR   A 1 216 ? -43.522 13.643  -9.583  1.00 52.65  ? 734  TYR   A CE1  1 
ATOM   1858 C  CE2  . TYR   A 1 216 ? -45.672 14.453  -8.914  1.00 49.22  ? 734  TYR   A CE2  1 
ATOM   1859 C  CZ   . TYR   A 1 216 ? -44.878 13.762  -9.804  1.00 53.26  ? 734  TYR   A CZ   1 
ATOM   1860 O  OH   . TYR   A 1 216 ? -45.445 13.186  -10.918 1.00 56.78  ? 734  TYR   A OH   1 
ATOM   1861 N  N    . LEU   A 1 217 ? -44.167 18.286  -7.522  1.00 37.12  ? 735  LEU   A N    1 
ATOM   1862 C  CA   . LEU   A 1 217 ? -44.855 18.984  -8.605  1.00 38.23  ? 735  LEU   A CA   1 
ATOM   1863 C  C    . LEU   A 1 217 ? -44.053 20.185  -9.096  1.00 36.41  ? 735  LEU   A C    1 
ATOM   1864 O  O    . LEU   A 1 217 ? -44.064 20.495  -10.294 1.00 34.29  ? 735  LEU   A O    1 
ATOM   1865 C  CB   . LEU   A 1 217 ? -46.249 19.412  -8.149  1.00 38.22  ? 735  LEU   A CB   1 
ATOM   1866 C  CG   . LEU   A 1 217 ? -47.238 18.258  -7.967  1.00 36.17  ? 735  LEU   A CG   1 
ATOM   1867 C  CD1  . LEU   A 1 217 ? -48.523 18.734  -7.310  1.00 35.41  ? 735  LEU   A CD1  1 
ATOM   1868 C  CD2  . LEU   A 1 217 ? -47.526 17.588  -9.302  1.00 35.25  ? 735  LEU   A CD2  1 
ATOM   1869 N  N    . VAL   A 1 218 ? -43.355 20.874  -8.191  1.00 36.30  ? 736  VAL   A N    1 
ATOM   1870 C  CA   . VAL   A 1 218 ? -42.489 21.974  -8.607  1.00 38.44  ? 736  VAL   A CA   1 
ATOM   1871 C  C    . VAL   A 1 218 ? -41.322 21.448  -9.433  1.00 43.29  ? 736  VAL   A C    1 
ATOM   1872 O  O    . VAL   A 1 218 ? -40.935 22.050  -10.443 1.00 45.79  ? 736  VAL   A O    1 
ATOM   1873 C  CB   . VAL   A 1 218 ? -42.001 22.765  -7.378  1.00 38.75  ? 736  VAL   A CB   1 
ATOM   1874 C  CG1  . VAL   A 1 218 ? -40.970 23.809  -7.786  1.00 39.57  ? 736  VAL   A CG1  1 
ATOM   1875 C  CG2  . VAL   A 1 218 ? -43.171 23.417  -6.665  1.00 38.24  ? 736  VAL   A CG2  1 
ATOM   1876 N  N    . ILE   A 1 219 ? -40.747 20.316  -9.019  1.00 41.95  ? 737  ILE   A N    1 
ATOM   1877 C  CA   . ILE   A 1 219 ? -39.639 19.716  -9.758  1.00 40.63  ? 737  ILE   A CA   1 
ATOM   1878 C  C    . ILE   A 1 219 ? -40.074 19.362  -11.176 1.00 38.45  ? 737  ILE   A C    1 
ATOM   1879 O  O    . ILE   A 1 219 ? -39.375 19.659  -12.152 1.00 33.99  ? 737  ILE   A O    1 
ATOM   1880 C  CB   . ILE   A 1 219 ? -39.104 18.482  -9.008  1.00 46.12  ? 737  ILE   A CB   1 
ATOM   1881 C  CG1  . ILE   A 1 219 ? -38.425 18.891  -7.698  1.00 50.86  ? 737  ILE   A CG1  1 
ATOM   1882 C  CG2  . ILE   A 1 219 ? -38.143 17.697  -9.883  1.00 44.07  ? 737  ILE   A CG2  1 
ATOM   1883 C  CD1  . ILE   A 1 219 ? -37.370 19.957  -7.856  1.00 55.47  ? 737  ILE   A CD1  1 
ATOM   1884 N  N    . GLN   A 1 220 ? -41.240 18.723  -11.310 1.00 39.22  ? 738  GLN   A N    1 
ATOM   1885 C  CA   . GLN   A 1 220 ? -41.730 18.344  -12.633 1.00 42.08  ? 738  GLN   A CA   1 
ATOM   1886 C  C    . GLN   A 1 220 ? -41.987 19.567  -13.502 1.00 44.85  ? 738  GLN   A C    1 
ATOM   1887 O  O    . GLN   A 1 220 ? -41.653 19.572  -14.692 1.00 47.36  ? 738  GLN   A O    1 
ATOM   1888 C  CB   . GLN   A 1 220 ? -43.003 17.509  -12.508 1.00 44.81  ? 738  GLN   A CB   1 
ATOM   1889 C  CG   . GLN   A 1 220 ? -42.830 16.224  -11.725 1.00 46.88  ? 738  GLN   A CG   1 
ATOM   1890 C  CD   . GLN   A 1 220 ? -41.770 15.321  -12.319 1.00 52.45  ? 738  GLN   A CD   1 
ATOM   1891 O  OE1  . GLN   A 1 220 ? -40.849 14.886  -11.626 1.00 55.54  ? 738  GLN   A OE1  1 
ATOM   1892 N  NE2  . GLN   A 1 220 ? -41.892 15.035  -13.609 1.00 51.90  ? 738  GLN   A NE2  1 
ATOM   1893 N  N    . TRP   A 1 221 ? -42.586 20.613  -12.927 1.00 45.14  ? 739  TRP   A N    1 
ATOM   1894 C  CA   . TRP   A 1 221 ? -42.864 21.816  -13.704 1.00 46.89  ? 739  TRP   A CA   1 
ATOM   1895 C  C    . TRP   A 1 221 ? -41.580 22.459  -14.209 1.00 47.70  ? 739  TRP   A C    1 
ATOM   1896 O  O    . TRP   A 1 221 ? -41.547 23.015  -15.314 1.00 47.11  ? 739  TRP   A O    1 
ATOM   1897 C  CB   . TRP   A 1 221 ? -43.657 22.822  -12.870 1.00 45.26  ? 739  TRP   A CB   1 
ATOM   1898 C  CG   . TRP   A 1 221 ? -43.845 24.127  -13.583 1.00 56.02  ? 739  TRP   A CG   1 
ATOM   1899 C  CD1  . TRP   A 1 221 ? -44.860 24.456  -14.430 1.00 61.83  ? 739  TRP   A CD1  1 
ATOM   1900 C  CD2  . TRP   A 1 221 ? -42.979 25.269  -13.532 1.00 58.71  ? 739  TRP   A CD2  1 
ATOM   1901 N  NE1  . TRP   A 1 221 ? -44.687 25.735  -14.903 1.00 68.70  ? 739  TRP   A NE1  1 
ATOM   1902 C  CE2  . TRP   A 1 221 ? -43.539 26.255  -14.367 1.00 66.68  ? 739  TRP   A CE2  1 
ATOM   1903 C  CE3  . TRP   A 1 221 ? -41.786 25.553  -12.858 1.00 60.79  ? 739  TRP   A CE3  1 
ATOM   1904 C  CZ2  . TRP   A 1 221 ? -42.949 27.505  -14.546 1.00 71.88  ? 739  TRP   A CZ2  1 
ATOM   1905 C  CZ3  . TRP   A 1 221 ? -41.202 26.794  -13.037 1.00 65.91  ? 739  TRP   A CZ3  1 
ATOM   1906 C  CH2  . TRP   A 1 221 ? -41.784 27.755  -13.874 1.00 71.52  ? 739  TRP   A CH2  1 
ATOM   1907 N  N    . ARG   A 1 222 ? -40.512 22.401  -13.414 1.00 46.90  ? 740  ARG   A N    1 
ATOM   1908 C  CA   . ARG   A 1 222 ? -39.289 23.098  -13.793 1.00 45.35  ? 740  ARG   A CA   1 
ATOM   1909 C  C    . ARG   A 1 222 ? -38.525 22.347  -14.878 1.00 44.61  ? 740  ARG   A C    1 
ATOM   1910 O  O    . ARG   A 1 222 ? -37.950 22.973  -15.776 1.00 45.61  ? 740  ARG   A O    1 
ATOM   1911 C  CB   . ARG   A 1 222 ? -38.403 23.316  -12.563 1.00 41.32  ? 740  ARG   A CB   1 
ATOM   1912 C  CG   . ARG   A 1 222 ? -37.015 23.872  -12.871 1.00 42.78  ? 740  ARG   A CG   1 
ATOM   1913 C  CD   . ARG   A 1 222 ? -37.095 25.192  -13.628 1.00 44.66  ? 740  ARG   A CD   1 
ATOM   1914 N  NE   . ARG   A 1 222 ? -35.777 25.763  -13.896 1.00 43.29  ? 740  ARG   A NE   1 
ATOM   1915 C  CZ   . ARG   A 1 222 ? -35.029 25.456  -14.953 1.00 43.22  ? 740  ARG   A CZ   1 
ATOM   1916 N  NH1  . ARG   A 1 222 ? -35.464 24.575  -15.844 1.00 40.06  ? 740  ARG   A NH1  1 
ATOM   1917 N  NH2  . ARG   A 1 222 ? -33.844 26.027  -15.118 1.00 42.23  ? 740  ARG   A NH2  1 
ATOM   1918 N  N    . PHE   A 1 223 ? -38.523 21.013  -14.833 1.00 46.91  ? 741  PHE   A N    1 
ATOM   1919 C  CA   . PHE   A 1 223 ? -37.604 20.234  -15.649 1.00 48.34  ? 741  PHE   A CA   1 
ATOM   1920 C  C    . PHE   A 1 223 ? -38.252 19.280  -16.643 1.00 50.17  ? 741  PHE   A C    1 
ATOM   1921 O  O    . PHE   A 1 223 ? -37.567 18.854  -17.579 1.00 50.06  ? 741  PHE   A O    1 
ATOM   1922 C  CB   . PHE   A 1 223 ? -36.659 19.415  -14.754 1.00 39.79  ? 741  PHE   A CB   1 
ATOM   1923 C  CG   . PHE   A 1 223 ? -35.709 20.252  -13.946 1.00 42.77  ? 741  PHE   A CG   1 
ATOM   1924 C  CD1  . PHE   A 1 223 ? -34.744 21.027  -14.569 1.00 40.55  ? 741  PHE   A CD1  1 
ATOM   1925 C  CD2  . PHE   A 1 223 ? -35.778 20.261  -12.562 1.00 42.79  ? 741  PHE   A CD2  1 
ATOM   1926 C  CE1  . PHE   A 1 223 ? -33.868 21.798  -13.829 1.00 43.17  ? 741  PHE   A CE1  1 
ATOM   1927 C  CE2  . PHE   A 1 223 ? -34.904 21.030  -11.816 1.00 47.53  ? 741  PHE   A CE2  1 
ATOM   1928 C  CZ   . PHE   A 1 223 ? -33.948 21.800  -12.451 1.00 44.74  ? 741  PHE   A CZ   1 
ATOM   1929 N  N    . VAL   A 1 224 ? -39.528 18.922  -16.481 1.00 50.75  ? 742  VAL   A N    1 
ATOM   1930 C  CA   . VAL   A 1 224 ? -40.117 17.792  -17.191 1.00 55.02  ? 742  VAL   A CA   1 
ATOM   1931 C  C    . VAL   A 1 224 ? -41.352 18.195  -17.991 1.00 58.30  ? 742  VAL   A C    1 
ATOM   1932 O  O    . VAL   A 1 224 ? -41.433 17.938  -19.196 1.00 63.65  ? 742  VAL   A O    1 
ATOM   1933 C  CB   . VAL   A 1 224 ? -40.451 16.634  -16.225 1.00 54.40  ? 742  VAL   A CB   1 
ATOM   1934 C  CG1  . VAL   A 1 224 ? -41.165 15.515  -16.968 1.00 55.42  ? 742  VAL   A CG1  1 
ATOM   1935 C  CG2  . VAL   A 1 224 ? -39.187 16.116  -15.560 1.00 51.81  ? 742  VAL   A CG2  1 
ATOM   1936 N  N    . ASN   A 1 225 ? -42.328 18.831  -17.334 1.00 56.77  ? 743  ASN   A N    1 
ATOM   1937 C  CA   . ASN   A 1 225 ? -43.693 18.860  -17.859 1.00 57.55  ? 743  ASN   A CA   1 
ATOM   1938 C  C    . ASN   A 1 225 ? -43.772 19.484  -19.249 1.00 55.50  ? 743  ASN   A C    1 
ATOM   1939 O  O    . ASN   A 1 225 ? -44.450 18.950  -20.135 1.00 56.73  ? 743  ASN   A O    1 
ATOM   1940 C  CB   . ASN   A 1 225 ? -44.611 19.600  -16.887 1.00 57.19  ? 743  ASN   A CB   1 
ATOM   1941 C  CG   . ASN   A 1 225 ? -44.958 18.768  -15.668 1.00 58.32  ? 743  ASN   A CG   1 
ATOM   1942 O  OD1  . ASN   A 1 225 ? -44.842 17.542  -15.685 1.00 60.94  ? 743  ASN   A OD1  1 
ATOM   1943 N  ND2  . ASN   A 1 225 ? -45.393 19.432  -14.604 1.00 59.57  ? 743  ASN   A ND2  1 
ATOM   1944 N  N    . ARG   A 1 226 ? -43.096 20.609  -19.466 1.00 53.64  ? 744  ARG   A N    1 
ATOM   1945 C  CA   . ARG   A 1 226 ? -43.225 21.311  -20.737 1.00 54.43  ? 744  ARG   A CA   1 
ATOM   1946 C  C    . ARG   A 1 226 ? -42.289 20.788  -21.821 1.00 53.30  ? 744  ARG   A C    1 
ATOM   1947 O  O    . ARG   A 1 226 ? -42.288 21.343  -22.925 1.00 55.09  ? 744  ARG   A O    1 
ATOM   1948 C  CB   . ARG   A 1 226 ? -42.982 22.809  -20.539 1.00 56.74  ? 744  ARG   A CB   1 
ATOM   1949 C  CG   . ARG   A 1 226 ? -44.078 23.518  -19.762 1.00 61.14  ? 744  ARG   A CG   1 
ATOM   1950 C  CD   . ARG   A 1 226 ? -43.556 24.811  -19.163 1.00 65.24  ? 744  ARG   A CD   1 
ATOM   1951 N  NE   . ARG   A 1 226 ? -42.447 24.562  -18.248 1.00 67.96  ? 744  ARG   A NE   1 
ATOM   1952 C  CZ   . ARG   A 1 226 ? -41.667 25.511  -17.742 1.00 69.77  ? 744  ARG   A CZ   1 
ATOM   1953 N  NH1  . ARG   A 1 226 ? -41.872 26.781  -18.063 1.00 72.47  ? 744  ARG   A NH1  1 
ATOM   1954 N  NH2  . ARG   A 1 226 ? -40.680 25.190  -16.916 1.00 66.50  ? 744  ARG   A NH2  1 
ATOM   1955 N  N    . ILE   A 1 227 ? -41.503 19.746  -21.551 1.00 49.96  ? 745  ILE   A N    1 
ATOM   1956 C  CA   . ILE   A 1 227 ? -40.529 19.269  -22.529 1.00 52.76  ? 745  ILE   A CA   1 
ATOM   1957 C  C    . ILE   A 1 227 ? -40.656 17.765  -22.738 1.00 50.96  ? 745  ILE   A C    1 
ATOM   1958 O  O    . ILE   A 1 227 ? -39.744 17.130  -23.280 1.00 50.87  ? 745  ILE   A O    1 
ATOM   1959 C  CB   . ILE   A 1 227 ? -39.090 19.629  -22.109 1.00 46.47  ? 745  ILE   A CB   1 
ATOM   1960 C  CG1  . ILE   A 1 227 ? -38.722 18.935  -20.796 1.00 49.05  ? 745  ILE   A CG1  1 
ATOM   1961 C  CG2  . ILE   A 1 227 ? -38.923 21.137  -21.985 1.00 46.63  ? 745  ILE   A CG2  1 
ATOM   1962 C  CD1  . ILE   A 1 227 ? -37.288 18.461  -20.746 1.00 51.77  ? 745  ILE   A CD1  1 
ATOM   1963 N  N    . GLN   A 1 228 ? -41.785 17.184  -22.325 1.00 48.42  ? 746  GLN   A N    1 
ATOM   1964 C  CA   . GLN   A 1 228 ? -41.923 15.731  -22.385 1.00 49.88  ? 746  GLN   A CA   1 
ATOM   1965 C  C    . GLN   A 1 228 ? -41.928 15.224  -23.824 1.00 44.70  ? 746  GLN   A C    1 
ATOM   1966 O  O    . GLN   A 1 228 ? -41.367 14.162  -24.114 1.00 47.28  ? 746  GLN   A O    1 
ATOM   1967 C  CB   . GLN   A 1 228 ? -43.189 15.283  -21.654 1.00 63.01  ? 746  GLN   A CB   1 
ATOM   1968 C  CG   . GLN   A 1 228 ? -43.150 13.827  -21.198 1.00 78.27  ? 746  GLN   A CG   1 
ATOM   1969 C  CD   . GLN   A 1 228 ? -43.129 13.681  -19.686 1.00 87.63  ? 746  GLN   A CD   1 
ATOM   1970 O  OE1  . GLN   A 1 228 ? -43.944 14.278  -18.982 1.00 92.49  ? 746  GLN   A OE1  1 
ATOM   1971 N  NE2  . GLN   A 1 228 ? -42.194 12.882  -19.181 1.00 87.32  ? 746  GLN   A NE2  1 
ATOM   1972 N  N    . LYS   A 1 229 ? -42.553 15.965  -24.741 1.00 41.03  ? 747  LYS   A N    1 
ATOM   1973 C  CA   . LYS   A 1 229 ? -42.606 15.503  -26.125 1.00 49.57  ? 747  LYS   A CA   1 
ATOM   1974 C  C    . LYS   A 1 229 ? -41.260 15.661  -26.817 1.00 47.45  ? 747  LYS   A C    1 
ATOM   1975 O  O    . LYS   A 1 229 ? -40.844 14.784  -27.584 1.00 46.94  ? 747  LYS   A O    1 
ATOM   1976 C  CB   . LYS   A 1 229 ? -43.703 16.239  -26.894 1.00 58.91  ? 747  LYS   A CB   1 
ATOM   1977 C  CG   . LYS   A 1 229 ? -45.105 15.900  -26.412 1.00 70.42  ? 747  LYS   A CG   1 
ATOM   1978 C  CD   . LYS   A 1 229 ? -45.310 14.398  -26.467 1.00 82.91  ? 747  LYS   A CD   1 
ATOM   1979 C  CE   . LYS   A 1 229 ? -45.580 13.830  -25.083 1.00 89.48  ? 747  LYS   A CE   1 
ATOM   1980 N  NZ   . LYS   A 1 229 ? -45.136 12.428  -25.019 1.00 91.76  ? 747  LYS   A NZ   1 
ATOM   1981 N  N    . GLN   A 1 230 ? -40.567 16.771  -26.561 1.00 42.52  ? 748  GLN   A N    1 
ATOM   1982 C  CA   . GLN   A 1 230 ? -39.237 16.959  -27.126 1.00 35.67  ? 748  GLN   A CA   1 
ATOM   1983 C  C    . GLN   A 1 230 ? -38.272 15.898  -26.614 1.00 38.16  ? 748  GLN   A C    1 
ATOM   1984 O  O    . GLN   A 1 230 ? -37.509 15.309  -27.389 1.00 42.95  ? 748  GLN   A O    1 
ATOM   1985 C  CB   . GLN   A 1 230 ? -38.727 18.360  -26.795 1.00 35.22  ? 748  GLN   A CB   1 
ATOM   1986 C  CG   . GLN   A 1 230 ? -39.626 19.478  -27.294 1.00 35.90  ? 748  GLN   A CG   1 
ATOM   1987 C  CD   . GLN   A 1 230 ? -40.642 19.916  -26.264 1.00 38.07  ? 748  GLN   A CD   1 
ATOM   1988 O  OE1  . GLN   A 1 230 ? -41.233 19.091  -25.572 1.00 38.05  ? 748  GLN   A OE1  1 
ATOM   1989 N  NE2  . GLN   A 1 230 ? -40.849 21.224  -26.155 1.00 40.98  ? 748  GLN   A NE2  1 
ATOM   1990 N  N    . MET   A 1 231 ? -38.294 15.637  -25.305 1.00 36.64  ? 749  MET   A N    1 
ATOM   1991 C  CA   . MET   A 1 231 ? -37.394 14.636  -24.745 1.00 35.98  ? 749  MET   A CA   1 
ATOM   1992 C  C    . MET   A 1 231 ? -37.739 13.240  -25.246 1.00 40.09  ? 749  MET   A C    1 
ATOM   1993 O  O    . MET   A 1 231 ? -36.841 12.447  -25.552 1.00 40.39  ? 749  MET   A O    1 
ATOM   1994 C  CB   . MET   A 1 231 ? -37.430 14.683  -23.218 1.00 36.21  ? 749  MET   A CB   1 
ATOM   1995 C  CG   . MET   A 1 231 ? -36.269 13.956  -22.563 1.00 39.67  ? 749  MET   A CG   1 
ATOM   1996 S  SD   . MET   A 1 231 ? -34.665 14.534  -23.157 1.00 46.77  ? 749  MET   A SD   1 
ATOM   1997 C  CE   . MET   A 1 231 ? -33.563 13.479  -22.218 1.00 49.68  ? 749  MET   A CE   1 
ATOM   1998 N  N    . ALA   A 1 232 ? -39.033 12.921  -25.336 1.00 34.41  ? 750  ALA   A N    1 
ATOM   1999 C  CA   . ALA   A 1 232 ? -39.438 11.628  -25.878 1.00 35.90  ? 750  ALA   A CA   1 
ATOM   2000 C  C    . ALA   A 1 232 ? -38.940 11.450  -27.305 1.00 38.77  ? 750  ALA   A C    1 
ATOM   2001 O  O    . ALA   A 1 232 ? -38.481 10.365  -27.681 1.00 40.48  ? 750  ALA   A O    1 
ATOM   2002 C  CB   . ALA   A 1 232 ? -40.958 11.484  -25.819 1.00 33.91  ? 750  ALA   A CB   1 
ATOM   2003 N  N    . ALA   A 1 233 ? -39.014 12.509  -28.115 1.00 40.12  ? 751  ALA   A N    1 
ATOM   2004 C  CA   . ALA   A 1 233 ? -38.518 12.426  -29.485 1.00 38.92  ? 751  ALA   A CA   1 
ATOM   2005 C  C    . ALA   A 1 233 ? -37.003 12.265  -29.515 1.00 41.19  ? 751  ALA   A C    1 
ATOM   2006 O  O    . ALA   A 1 233 ? -36.468 11.526  -30.350 1.00 41.42  ? 751  ALA   A O    1 
ATOM   2007 C  CB   . ALA   A 1 233 ? -38.946 13.662  -30.274 1.00 35.94  ? 751  ALA   A CB   1 
ATOM   2008 N  N    . PHE   A 1 234 ? -36.296 12.947  -28.611 1.00 37.84  ? 752  PHE   A N    1 
ATOM   2009 C  CA   . PHE   A 1 234 ? -34.849 12.783  -28.526 1.00 37.78  ? 752  PHE   A CA   1 
ATOM   2010 C  C    . PHE   A 1 234 ? -34.487 11.355  -28.137 1.00 38.46  ? 752  PHE   A C    1 
ATOM   2011 O  O    . PHE   A 1 234 ? -33.629 10.726  -28.765 1.00 33.99  ? 752  PHE   A O    1 
ATOM   2012 C  CB   . PHE   A 1 234 ? -34.266 13.782  -27.524 1.00 36.18  ? 752  PHE   A CB   1 
ATOM   2013 C  CG   . PHE   A 1 234 ? -32.814 13.549  -27.201 1.00 36.64  ? 752  PHE   A CG   1 
ATOM   2014 C  CD1  . PHE   A 1 234 ? -32.443 12.702  -26.165 1.00 36.60  ? 752  PHE   A CD1  1 
ATOM   2015 C  CD2  . PHE   A 1 234 ? -31.820 14.186  -27.925 1.00 38.59  ? 752  PHE   A CD2  1 
ATOM   2016 C  CE1  . PHE   A 1 234 ? -31.110 12.487  -25.868 1.00 37.43  ? 752  PHE   A CE1  1 
ATOM   2017 C  CE2  . PHE   A 1 234 ? -30.484 13.978  -27.631 1.00 38.88  ? 752  PHE   A CE2  1 
ATOM   2018 C  CZ   . PHE   A 1 234 ? -30.130 13.127  -26.600 1.00 38.53  ? 752  PHE   A CZ   1 
ATOM   2019 N  N    . LYS   A 1 235 ? -35.131 10.833  -27.088 1.00 39.16  ? 753  LYS   A N    1 
ATOM   2020 C  CA   . LYS   A 1 235 ? -34.850 9.471   -26.644 1.00 43.75  ? 753  LYS   A CA   1 
ATOM   2021 C  C    . LYS   A 1 235 ? -35.171 8.458   -27.733 1.00 45.09  ? 753  LYS   A C    1 
ATOM   2022 O  O    . LYS   A 1 235 ? -34.468 7.451   -27.881 1.00 49.96  ? 753  LYS   A O    1 
ATOM   2023 C  CB   . LYS   A 1 235 ? -35.641 9.160   -25.373 1.00 49.75  ? 753  LYS   A CB   1 
ATOM   2024 C  CG   . LYS   A 1 235 ? -35.306 10.060  -24.197 1.00 54.81  ? 753  LYS   A CG   1 
ATOM   2025 C  CD   . LYS   A 1 235 ? -36.289 9.871   -23.054 1.00 60.93  ? 753  LYS   A CD   1 
ATOM   2026 C  CE   . LYS   A 1 235 ? -36.114 8.516   -22.389 1.00 65.94  ? 753  LYS   A CE   1 
ATOM   2027 N  NZ   . LYS   A 1 235 ? -37.020 8.353   -21.218 1.00 68.58  ? 753  LYS   A NZ   1 
ATOM   2028 N  N    . GLU   A 1 236 ? -36.230 8.708   -28.506 1.00 40.37  ? 754  GLU   A N    1 
ATOM   2029 C  CA   . GLU   A 1 236 ? -36.574 7.803   -29.597 1.00 45.51  ? 754  GLU   A CA   1 
ATOM   2030 C  C    . GLU   A 1 236 ? -35.435 7.700   -30.603 1.00 44.69  ? 754  GLU   A C    1 
ATOM   2031 O  O    . GLU   A 1 236 ? -35.080 6.599   -31.040 1.00 41.65  ? 754  GLU   A O    1 
ATOM   2032 C  CB   . GLU   A 1 236 ? -37.857 8.270   -30.283 1.00 50.59  ? 754  GLU   A CB   1 
ATOM   2033 C  CG   . GLU   A 1 236 ? -38.536 7.192   -31.106 1.00 63.68  ? 754  GLU   A CG   1 
ATOM   2034 C  CD   . GLU   A 1 236 ? -39.835 7.665   -31.722 1.00 79.53  ? 754  GLU   A CD   1 
ATOM   2035 O  OE1  . GLU   A 1 236 ? -39.786 8.340   -32.772 1.00 85.47  ? 754  GLU   A OE1  1 
ATOM   2036 O  OE2  . GLU   A 1 236 ? -40.906 7.360   -31.156 1.00 86.64  ? 754  GLU   A OE2  1 
ATOM   2037 N  N    . GLY   A 1 237 ? -34.842 8.836   -30.972 1.00 39.91  ? 755  GLY   A N    1 
ATOM   2038 C  CA   . GLY   A 1 237 ? -33.712 8.802   -31.885 1.00 38.14  ? 755  GLY   A CA   1 
ATOM   2039 C  C    . GLY   A 1 237 ? -32.477 8.179   -31.262 1.00 39.27  ? 755  GLY   A C    1 
ATOM   2040 O  O    . GLY   A 1 237 ? -31.736 7.451   -31.929 1.00 38.62  ? 755  GLY   A O    1 
ATOM   2041 N  N    . PHE   A 1 238 ? -32.236 8.456   -29.978 1.00 35.55  ? 756  PHE   A N    1 
ATOM   2042 C  CA   . PHE   A 1 238 ? -31.072 7.894   -29.302 1.00 34.66  ? 756  PHE   A CA   1 
ATOM   2043 C  C    . PHE   A 1 238 ? -31.170 6.377   -29.208 1.00 35.08  ? 756  PHE   A C    1 
ATOM   2044 O  O    . PHE   A 1 238 ? -30.204 5.661   -29.498 1.00 35.77  ? 756  PHE   A O    1 
ATOM   2045 C  CB   . PHE   A 1 238 ? -30.925 8.508   -27.909 1.00 37.63  ? 756  PHE   A CB   1 
ATOM   2046 C  CG   . PHE   A 1 238 ? -29.654 8.116   -27.204 1.00 39.99  ? 756  PHE   A CG   1 
ATOM   2047 C  CD1  . PHE   A 1 238 ? -28.483 8.823   -27.418 1.00 38.73  ? 756  PHE   A CD1  1 
ATOM   2048 C  CD2  . PHE   A 1 238 ? -29.631 7.038   -26.329 1.00 40.25  ? 756  PHE   A CD2  1 
ATOM   2049 C  CE1  . PHE   A 1 238 ? -27.310 8.464   -26.773 1.00 42.04  ? 756  PHE   A CE1  1 
ATOM   2050 C  CE2  . PHE   A 1 238 ? -28.461 6.674   -25.682 1.00 39.92  ? 756  PHE   A CE2  1 
ATOM   2051 C  CZ   . PHE   A 1 238 ? -27.300 7.388   -25.904 1.00 38.95  ? 756  PHE   A CZ   1 
ATOM   2052 N  N    . PHE   A 1 239 ? -32.335 5.866   -28.808 1.00 39.97  ? 757  PHE   A N    1 
ATOM   2053 C  CA   . PHE   A 1 239 ? -32.491 4.428   -28.637 1.00 46.42  ? 757  PHE   A CA   1 
ATOM   2054 C  C    . PHE   A 1 239 ? -32.533 3.678   -29.960 1.00 54.61  ? 757  PHE   A C    1 
ATOM   2055 O  O    . PHE   A 1 239 ? -32.436 2.447   -29.955 1.00 63.47  ? 757  PHE   A O    1 
ATOM   2056 C  CB   . PHE   A 1 239 ? -33.741 4.142   -27.805 1.00 42.09  ? 757  PHE   A CB   1 
ATOM   2057 C  CG   . PHE   A 1 239 ? -33.684 4.738   -26.427 1.00 46.70  ? 757  PHE   A CG   1 
ATOM   2058 C  CD1  . PHE   A 1 239 ? -32.463 4.914   -25.792 1.00 48.27  ? 757  PHE   A CD1  1 
ATOM   2059 C  CD2  . PHE   A 1 239 ? -34.837 5.133   -25.771 1.00 45.31  ? 757  PHE   A CD2  1 
ATOM   2060 C  CE1  . PHE   A 1 239 ? -32.392 5.468   -24.529 1.00 48.66  ? 757  PHE   A CE1  1 
ATOM   2061 C  CE2  . PHE   A 1 239 ? -34.773 5.689   -24.505 1.00 47.13  ? 757  PHE   A CE2  1 
ATOM   2062 C  CZ   . PHE   A 1 239 ? -33.548 5.855   -23.883 1.00 49.72  ? 757  PHE   A CZ   1 
ATOM   2063 N  N    . GLU   A 1 240 ? -32.658 4.384   -31.085 1.00 53.37  ? 758  GLU   A N    1 
ATOM   2064 C  CA   . GLU   A 1 240 ? -32.481 3.745   -32.383 1.00 56.05  ? 758  GLU   A CA   1 
ATOM   2065 C  C    . GLU   A 1 240 ? -31.026 3.377   -32.640 1.00 56.55  ? 758  GLU   A C    1 
ATOM   2066 O  O    . GLU   A 1 240 ? -30.750 2.566   -33.531 1.00 56.24  ? 758  GLU   A O    1 
ATOM   2067 C  CB   . GLU   A 1 240 ? -32.994 4.658   -33.497 1.00 56.23  ? 758  GLU   A CB   1 
ATOM   2068 C  CG   . GLU   A 1 240 ? -34.508 4.764   -33.564 1.00 60.17  ? 758  GLU   A CG   1 
ATOM   2069 C  CD   . GLU   A 1 240 ? -34.983 5.677   -34.678 1.00 65.13  ? 758  GLU   A CD   1 
ATOM   2070 O  OE1  . GLU   A 1 240 ? -34.339 6.722   -34.911 1.00 64.88  ? 758  GLU   A OE1  1 
ATOM   2071 O  OE2  . GLU   A 1 240 ? -36.002 5.350   -35.321 1.00 70.11  ? 758  GLU   A OE2  1 
ATOM   2072 N  N    . LEU   A 1 241 ? -30.095 3.954   -31.883 1.00 50.45  ? 759  LEU   A N    1 
ATOM   2073 C  CA   . LEU   A 1 241 ? -28.670 3.676   -32.013 1.00 49.31  ? 759  LEU   A CA   1 
ATOM   2074 C  C    . LEU   A 1 241 ? -28.112 2.878   -30.847 1.00 47.41  ? 759  LEU   A C    1 
ATOM   2075 O  O    . LEU   A 1 241 ? -27.257 2.014   -31.048 1.00 52.55  ? 759  LEU   A O    1 
ATOM   2076 C  CB   . LEU   A 1 241 ? -27.884 4.989   -32.141 1.00 46.36  ? 759  LEU   A CB   1 
ATOM   2077 C  CG   . LEU   A 1 241 ? -27.723 5.655   -33.513 1.00 45.45  ? 759  LEU   A CG   1 
ATOM   2078 C  CD1  . LEU   A 1 241 ? -26.747 4.874   -34.380 1.00 46.01  ? 759  LEU   A CD1  1 
ATOM   2079 C  CD2  . LEU   A 1 241 ? -29.060 5.835   -34.226 1.00 44.63  ? 759  LEU   A CD2  1 
ATOM   2080 N  N    . ILE   A 1 242 ? -28.575 3.152   -29.633 1.00 43.94  ? 760  ILE   A N    1 
ATOM   2081 C  CA   . ILE   A 1 242 ? -28.116 2.484   -28.424 1.00 45.50  ? 760  ILE   A CA   1 
ATOM   2082 C  C    . ILE   A 1 242 ? -29.337 1.878   -27.743 1.00 47.74  ? 760  ILE   A C    1 
ATOM   2083 O  O    . ILE   A 1 242 ? -30.275 2.605   -27.405 1.00 51.26  ? 760  ILE   A O    1 
ATOM   2084 C  CB   . ILE   A 1 242 ? -27.390 3.446   -27.469 1.00 44.38  ? 760  ILE   A CB   1 
ATOM   2085 C  CG1  . ILE   A 1 242 ? -26.352 4.280   -28.225 1.00 43.66  ? 760  ILE   A CG1  1 
ATOM   2086 C  CG2  . ILE   A 1 242 ? -26.743 2.677   -26.324 1.00 48.95  ? 760  ILE   A CG2  1 
ATOM   2087 C  CD1  . ILE   A 1 242 ? -25.120 3.499   -28.632 1.00 50.30  ? 760  ILE   A CD1  1 
ATOM   2088 N  N    . PRO   A 1 243 ? -29.383 0.564   -27.528 1.00 52.21  ? 761  PRO   A N    1 
ATOM   2089 C  CA   . PRO   A 1 243 ? -30.512 -0.018  -26.792 1.00 50.09  ? 761  PRO   A CA   1 
ATOM   2090 C  C    . PRO   A 1 243 ? -30.613 0.589   -25.402 1.00 50.62  ? 761  PRO   A C    1 
ATOM   2091 O  O    . PRO   A 1 243 ? -29.610 0.769   -24.707 1.00 52.24  ? 761  PRO   A O    1 
ATOM   2092 C  CB   . PRO   A 1 243 ? -30.172 -1.512  -26.738 1.00 52.67  ? 761  PRO   A CB   1 
ATOM   2093 C  CG   . PRO   A 1 243 ? -29.214 -1.727  -27.867 1.00 54.09  ? 761  PRO   A CG   1 
ATOM   2094 C  CD   . PRO   A 1 243 ? -28.422 -0.459  -27.972 1.00 52.41  ? 761  PRO   A CD   1 
ATOM   2095 N  N    . GLN   A 1 244 ? -31.842 0.914   -25.000 1.00 53.92  ? 762  GLN   A N    1 
ATOM   2096 C  CA   . GLN   A 1 244 ? -32.026 1.706   -23.792 1.00 55.77  ? 762  GLN   A CA   1 
ATOM   2097 C  C    . GLN   A 1 244 ? -31.753 0.915   -22.519 1.00 64.85  ? 762  GLN   A C    1 
ATOM   2098 O  O    . GLN   A 1 244 ? -31.467 1.523   -21.483 1.00 71.44  ? 762  GLN   A O    1 
ATOM   2099 C  CB   . GLN   A 1 244 ? -33.432 2.310   -23.774 1.00 52.60  ? 762  GLN   A CB   1 
ATOM   2100 C  CG   . GLN   A 1 244 ? -34.505 1.510   -23.083 1.00 66.46  ? 762  GLN   A CG   1 
ATOM   2101 C  CD   . GLN   A 1 244 ? -35.662 2.393   -22.652 1.00 74.30  ? 762  GLN   A CD   1 
ATOM   2102 O  OE1  . GLN   A 1 244 ? -35.746 2.804   -21.495 1.00 75.62  ? 762  GLN   A OE1  1 
ATOM   2103 N  NE2  . GLN   A 1 244 ? -36.548 2.709   -23.590 1.00 76.72  ? 762  GLN   A NE2  1 
ATOM   2104 N  N    . ASP   A 1 245 ? -31.814 -0.417  -22.562 1.00 67.91  ? 763  ASP   A N    1 
ATOM   2105 C  CA   . ASP   A 1 245 ? -31.377 -1.185  -21.403 1.00 74.07  ? 763  ASP   A CA   1 
ATOM   2106 C  C    . ASP   A 1 245 ? -29.859 -1.261  -21.303 1.00 69.15  ? 763  ASP   A C    1 
ATOM   2107 O  O    . ASP   A 1 245 ? -29.333 -1.454  -20.202 1.00 75.28  ? 763  ASP   A O    1 
ATOM   2108 C  CB   . ASP   A 1 245 ? -31.973 -2.597  -21.422 1.00 84.29  ? 763  ASP   A CB   1 
ATOM   2109 C  CG   . ASP   A 1 245 ? -31.955 -3.226  -22.799 1.00 97.16  ? 763  ASP   A CG   1 
ATOM   2110 O  OD1  . ASP   A 1 245 ? -30.889 -3.728  -23.213 1.00 102.86 ? 763  ASP   A OD1  1 
ATOM   2111 O  OD2  . ASP   A 1 245 ? -33.013 -3.231  -23.463 1.00 102.14 ? 763  ASP   A OD2  1 
ATOM   2112 N  N    . LEU   A 1 246 ? -29.146 -1.102  -22.421 1.00 56.26  ? 764  LEU   A N    1 
ATOM   2113 C  CA   . LEU   A 1 246 ? -27.689 -1.062  -22.364 1.00 52.19  ? 764  LEU   A CA   1 
ATOM   2114 C  C    . LEU   A 1 246 ? -27.196 0.235   -21.735 1.00 51.65  ? 764  LEU   A C    1 
ATOM   2115 O  O    . LEU   A 1 246 ? -26.237 0.226   -20.954 1.00 50.38  ? 764  LEU   A O    1 
ATOM   2116 C  CB   . LEU   A 1 246 ? -27.099 -1.233  -23.763 1.00 50.74  ? 764  LEU   A CB   1 
ATOM   2117 C  CG   . LEU   A 1 246 ? -26.465 -2.595  -24.045 1.00 59.55  ? 764  LEU   A CG   1 
ATOM   2118 C  CD1  . LEU   A 1 246 ? -27.483 -3.705  -23.839 1.00 61.63  ? 764  LEU   A CD1  1 
ATOM   2119 C  CD2  . LEU   A 1 246 ? -25.887 -2.644  -25.451 1.00 61.89  ? 764  LEU   A CD2  1 
ATOM   2120 N  N    . ILE   A 1 247 ? -27.837 1.361   -22.060 1.00 49.38  ? 765  ILE   A N    1 
ATOM   2121 C  CA   . ILE   A 1 247 ? -27.405 2.642   -21.515 1.00 51.31  ? 765  ILE   A CA   1 
ATOM   2122 C  C    . ILE   A 1 247 ? -27.630 2.722   -20.012 1.00 53.90  ? 765  ILE   A C    1 
ATOM   2123 O  O    . ILE   A 1 247 ? -26.975 3.522   -19.334 1.00 56.92  ? 765  ILE   A O    1 
ATOM   2124 C  CB   . ILE   A 1 247 ? -28.118 3.805   -22.236 1.00 47.68  ? 765  ILE   A CB   1 
ATOM   2125 C  CG1  . ILE   A 1 247 ? -27.249 5.064   -22.210 1.00 47.30  ? 765  ILE   A CG1  1 
ATOM   2126 C  CG2  . ILE   A 1 247 ? -29.474 4.091   -21.605 1.00 46.44  ? 765  ILE   A CG2  1 
ATOM   2127 C  CD1  . ILE   A 1 247 ? -25.951 4.928   -22.967 1.00 48.11  ? 765  ILE   A CD1  1 
ATOM   2128 N  N    . LYS   A 1 248 ? -28.522 1.897   -19.464 1.00 54.42  ? 766  LYS   A N    1 
ATOM   2129 C  CA   . LYS   A 1 248 ? -28.884 1.981   -18.055 1.00 59.24  ? 766  LYS   A CA   1 
ATOM   2130 C  C    . LYS   A 1 248 ? -27.833 1.396   -17.121 1.00 60.69  ? 766  LYS   A C    1 
ATOM   2131 O  O    . LYS   A 1 248 ? -28.023 1.449   -15.901 1.00 67.46  ? 766  LYS   A O    1 
ATOM   2132 C  CB   . LYS   A 1 248 ? -30.226 1.286   -17.815 1.00 66.74  ? 766  LYS   A CB   1 
ATOM   2133 C  CG   . LYS   A 1 248 ? -31.432 2.126   -18.198 1.00 69.79  ? 766  LYS   A CG   1 
ATOM   2134 C  CD   . LYS   A 1 248 ? -32.727 1.442   -17.797 1.00 74.91  ? 766  LYS   A CD   1 
ATOM   2135 C  CE   . LYS   A 1 248 ? -33.937 2.244   -18.242 1.00 76.26  ? 766  LYS   A CE   1 
ATOM   2136 N  NZ   . LYS   A 1 248 ? -35.205 1.636   -17.757 1.00 77.96  ? 766  LYS   A NZ   1 
ATOM   2137 N  N    . ILE   A 1 249 ? -26.738 0.837   -17.641 1.00 55.21  ? 767  ILE   A N    1 
ATOM   2138 C  CA   . ILE   A 1 249 ? -25.669 0.412   -16.747 1.00 62.05  ? 767  ILE   A CA   1 
ATOM   2139 C  C    . ILE   A 1 249 ? -24.910 1.611   -16.192 1.00 60.32  ? 767  ILE   A C    1 
ATOM   2140 O  O    . ILE   A 1 249 ? -24.240 1.492   -15.160 1.00 64.79  ? 767  ILE   A O    1 
ATOM   2141 C  CB   . ILE   A 1 249 ? -24.707 -0.567  -17.447 1.00 65.57  ? 767  ILE   A CB   1 
ATOM   2142 C  CG1  . ILE   A 1 249 ? -23.620 0.187   -18.213 1.00 63.67  ? 767  ILE   A CG1  1 
ATOM   2143 C  CG2  . ILE   A 1 249 ? -25.468 -1.511  -18.369 1.00 71.33  ? 767  ILE   A CG2  1 
ATOM   2144 C  CD1  . ILE   A 1 249 ? -22.439 -0.676  -18.569 1.00 65.00  ? 767  ILE   A CD1  1 
ATOM   2145 N  N    . PHE   A 1 250 ? -25.013 2.767   -16.840 1.00 57.06  ? 768  PHE   A N    1 
ATOM   2146 C  CA   . PHE   A 1 250 ? -24.345 3.978   -16.391 1.00 54.10  ? 768  PHE   A CA   1 
ATOM   2147 C  C    . PHE   A 1 250 ? -25.279 4.821   -15.535 1.00 55.23  ? 768  PHE   A C    1 
ATOM   2148 O  O    . PHE   A 1 250 ? -26.502 4.785   -15.695 1.00 52.97  ? 768  PHE   A O    1 
ATOM   2149 C  CB   . PHE   A 1 250 ? -23.871 4.810   -17.584 1.00 48.52  ? 768  PHE   A CB   1 
ATOM   2150 C  CG   . PHE   A 1 250 ? -22.973 4.068   -18.526 1.00 48.16  ? 768  PHE   A CG   1 
ATOM   2151 C  CD1  . PHE   A 1 250 ? -21.663 3.790   -18.177 1.00 45.18  ? 768  PHE   A CD1  1 
ATOM   2152 C  CD2  . PHE   A 1 250 ? -23.437 3.654   -19.763 1.00 45.46  ? 768  PHE   A CD2  1 
ATOM   2153 C  CE1  . PHE   A 1 250 ? -20.831 3.110   -19.043 1.00 46.28  ? 768  PHE   A CE1  1 
ATOM   2154 C  CE2  . PHE   A 1 250 ? -22.610 2.973   -20.634 1.00 45.22  ? 768  PHE   A CE2  1 
ATOM   2155 C  CZ   . PHE   A 1 250 ? -21.304 2.702   -20.273 1.00 47.06  ? 768  PHE   A CZ   1 
ATOM   2156 N  N    . ASP   A 1 251 ? -24.691 5.589   -14.620 1.00 55.79  ? 769  ASP   A N    1 
ATOM   2157 C  CA   . ASP   A 1 251 ? -25.447 6.615   -13.925 1.00 56.82  ? 769  ASP   A CA   1 
ATOM   2158 C  C    . ASP   A 1 251 ? -25.346 7.923   -14.709 1.00 51.85  ? 769  ASP   A C    1 
ATOM   2159 O  O    . ASP   A 1 251 ? -24.707 7.998   -15.762 1.00 53.45  ? 769  ASP   A O    1 
ATOM   2160 C  CB   . ASP   A 1 251 ? -24.978 6.756   -12.472 1.00 60.04  ? 769  ASP   A CB   1 
ATOM   2161 C  CG   . ASP   A 1 251 ? -23.525 7.201   -12.342 1.00 61.71  ? 769  ASP   A CG   1 
ATOM   2162 O  OD1  . ASP   A 1 251 ? -22.961 7.783   -13.292 1.00 59.47  ? 769  ASP   A OD1  1 
ATOM   2163 O  OD2  . ASP   A 1 251 ? -22.942 6.971   -11.261 1.00 65.96  ? 769  ASP   A OD2  1 
ATOM   2164 N  N    . GLU   A 1 252 ? -25.982 8.973   -14.186 1.00 48.90  ? 770  GLU   A N    1 
ATOM   2165 C  CA   . GLU   A 1 252 ? -26.040 10.239  -14.911 1.00 47.47  ? 770  GLU   A CA   1 
ATOM   2166 C  C    . GLU   A 1 252 ? -24.647 10.819  -15.139 1.00 43.28  ? 770  GLU   A C    1 
ATOM   2167 O  O    . GLU   A 1 252 ? -24.353 11.334  -16.225 1.00 43.41  ? 770  GLU   A O    1 
ATOM   2168 C  CB   . GLU   A 1 252 ? -26.930 11.233  -14.159 1.00 52.64  ? 770  GLU   A CB   1 
ATOM   2169 C  CG   . GLU   A 1 252 ? -26.547 11.467  -12.700 1.00 64.07  ? 770  GLU   A CG   1 
ATOM   2170 C  CD   . GLU   A 1 252 ? -27.099 10.407  -11.762 1.00 72.90  ? 770  GLU   A CD   1 
ATOM   2171 O  OE1  . GLU   A 1 252 ? -28.157 9.823   -12.073 1.00 74.76  ? 770  GLU   A OE1  1 
ATOM   2172 O  OE2  . GLU   A 1 252 ? -26.471 10.159  -10.711 1.00 80.61  ? 770  GLU   A OE2  1 
ATOM   2173 N  N    . ASN   A 1 253 ? -23.770 10.731  -14.134 1.00 43.99  ? 771  ASN   A N    1 
ATOM   2174 C  CA   . ASN   A 1 253 ? -22.424 11.285  -14.269 1.00 49.53  ? 771  ASN   A CA   1 
ATOM   2175 C  C    . ASN   A 1 253 ? -21.600 10.501  -15.280 1.00 52.81  ? 771  ASN   A C    1 
ATOM   2176 O  O    . ASN   A 1 253 ? -20.880 11.092  -16.095 1.00 53.66  ? 771  ASN   A O    1 
ATOM   2177 C  CB   . ASN   A 1 253 ? -21.717 11.294  -12.914 1.00 59.83  ? 771  ASN   A CB   1 
ATOM   2178 C  CG   . ASN   A 1 253 ? -22.556 11.916  -11.822 1.00 71.51  ? 771  ASN   A CG   1 
ATOM   2179 O  OD1  . ASN   A 1 253 ? -22.819 13.116  -11.833 1.00 74.16  ? 771  ASN   A OD1  1 
ATOM   2180 N  ND2  . ASN   A 1 253 ? -22.980 11.099  -10.866 1.00 76.64  ? 771  ASN   A ND2  1 
ATOM   2181 N  N    . GLU   A 1 254 ? -21.671 9.170   -15.226 1.00 48.96  ? 772  GLU   A N    1 
ATOM   2182 C  CA   . GLU   A 1 254 ? -20.952 8.355   -16.196 1.00 47.84  ? 772  GLU   A CA   1 
ATOM   2183 C  C    . GLU   A 1 254 ? -21.465 8.611   -17.607 1.00 45.48  ? 772  GLU   A C    1 
ATOM   2184 O  O    . GLU   A 1 254 ? -20.676 8.709   -18.555 1.00 45.34  ? 772  GLU   A O    1 
ATOM   2185 C  CB   . GLU   A 1 254 ? -21.076 6.876   -15.825 1.00 54.17  ? 772  GLU   A CB   1 
ATOM   2186 C  CG   . GLU   A 1 254 ? -20.378 6.519   -14.517 1.00 62.64  ? 772  GLU   A CG   1 
ATOM   2187 C  CD   . GLU   A 1 254 ? -20.885 5.226   -13.898 1.00 67.42  ? 772  GLU   A CD   1 
ATOM   2188 O  OE1  . GLU   A 1 254 ? -22.032 4.827   -14.189 1.00 63.37  ? 772  GLU   A OE1  1 
ATOM   2189 O  OE2  . GLU   A 1 254 ? -20.133 4.613   -13.111 1.00 71.56  ? 772  GLU   A OE2  1 
ATOM   2190 N  N    . LEU   A 1 255 ? -22.785 8.752   -17.759 1.00 44.38  ? 773  LEU   A N    1 
ATOM   2191 C  CA   . LEU   A 1 255 ? -23.363 8.993   -19.077 1.00 43.92  ? 773  LEU   A CA   1 
ATOM   2192 C  C    . LEU   A 1 255 ? -22.881 10.314  -19.666 1.00 45.00  ? 773  LEU   A C    1 
ATOM   2193 O  O    . LEU   A 1 255 ? -22.567 10.389  -20.860 1.00 44.70  ? 773  LEU   A O    1 
ATOM   2194 C  CB   . LEU   A 1 255 ? -24.889 8.966   -18.990 1.00 41.88  ? 773  LEU   A CB   1 
ATOM   2195 C  CG   . LEU   A 1 255 ? -25.641 9.210   -20.301 1.00 42.79  ? 773  LEU   A CG   1 
ATOM   2196 C  CD1  . LEU   A 1 255 ? -25.271 8.158   -21.333 1.00 44.75  ? 773  LEU   A CD1  1 
ATOM   2197 C  CD2  . LEU   A 1 255 ? -27.142 9.228   -20.064 1.00 40.12  ? 773  LEU   A CD2  1 
ATOM   2198 N  N    . GLU   A 1 256 ? -22.818 11.369  -18.848 1.00 42.63  ? 774  GLU   A N    1 
ATOM   2199 C  CA   . GLU   A 1 256 ? -22.324 12.649  -19.349 1.00 46.16  ? 774  GLU   A CA   1 
ATOM   2200 C  C    . GLU   A 1 256 ? -20.868 12.541  -19.785 1.00 45.12  ? 774  GLU   A C    1 
ATOM   2201 O  O    . GLU   A 1 256 ? -20.483 13.071  -20.834 1.00 42.28  ? 774  GLU   A O    1 
ATOM   2202 C  CB   . GLU   A 1 256 ? -22.484 13.739  -18.289 1.00 49.18  ? 774  GLU   A CB   1 
ATOM   2203 C  CG   . GLU   A 1 256 ? -21.692 15.003  -18.599 1.00 60.90  ? 774  GLU   A CG   1 
ATOM   2204 C  CD   . GLU   A 1 256 ? -22.067 16.175  -17.713 1.00 70.61  ? 774  GLU   A CD   1 
ATOM   2205 O  OE1  . GLU   A 1 256 ? -22.143 17.311  -18.229 1.00 74.20  ? 774  GLU   A OE1  1 
ATOM   2206 O  OE2  . GLU   A 1 256 ? -22.279 15.964  -16.501 1.00 74.89  ? 774  GLU   A OE2  1 
ATOM   2207 N  N    . LEU   A 1 257 ? -20.043 11.858  -18.989 1.00 45.92  ? 775  LEU   A N    1 
ATOM   2208 C  CA   . LEU   A 1 257 ? -18.655 11.634  -19.378 1.00 52.22  ? 775  LEU   A CA   1 
ATOM   2209 C  C    . LEU   A 1 257 ? -18.572 10.847  -20.680 1.00 53.71  ? 775  LEU   A C    1 
ATOM   2210 O  O    . LEU   A 1 257 ? -17.742 11.144  -21.546 1.00 54.72  ? 775  LEU   A O    1 
ATOM   2211 C  CB   . LEU   A 1 257 ? -17.917 10.903  -18.257 1.00 57.51  ? 775  LEU   A CB   1 
ATOM   2212 C  CG   . LEU   A 1 257 ? -16.392 10.866  -18.311 1.00 65.89  ? 775  LEU   A CG   1 
ATOM   2213 C  CD1  . LEU   A 1 257 ? -15.831 12.262  -18.526 1.00 70.87  ? 775  LEU   A CD1  1 
ATOM   2214 C  CD2  . LEU   A 1 257 ? -15.837 10.253  -17.034 1.00 67.34  ? 775  LEU   A CD2  1 
ATOM   2215 N  N    . LEU   A 1 258 ? -19.441 9.849   -20.841 1.00 53.89  ? 776  LEU   A N    1 
ATOM   2216 C  CA   . LEU   A 1 258 ? -19.410 9.015   -22.037 1.00 58.94  ? 776  LEU   A CA   1 
ATOM   2217 C  C    . LEU   A 1 258 ? -19.845 9.793   -23.275 1.00 57.42  ? 776  LEU   A C    1 
ATOM   2218 O  O    . LEU   A 1 258 ? -19.216 9.686   -24.334 1.00 56.85  ? 776  LEU   A O    1 
ATOM   2219 C  CB   . LEU   A 1 258 ? -20.298 7.790   -21.821 1.00 63.18  ? 776  LEU   A CB   1 
ATOM   2220 C  CG   . LEU   A 1 258 ? -20.647 6.881   -22.997 1.00 66.67  ? 776  LEU   A CG   1 
ATOM   2221 C  CD1  . LEU   A 1 258 ? -20.471 5.431   -22.594 1.00 70.84  ? 776  LEU   A CD1  1 
ATOM   2222 C  CD2  . LEU   A 1 258 ? -22.073 7.131   -23.441 1.00 63.39  ? 776  LEU   A CD2  1 
ATOM   2223 N  N    . MET   A 1 259 ? -20.911 10.588  -23.158 1.00 52.43  ? 777  MET   A N    1 
ATOM   2224 C  CA   . MET   A 1 259 ? -21.481 11.270  -24.317 1.00 51.41  ? 777  MET   A CA   1 
ATOM   2225 C  C    . MET   A 1 259 ? -20.714 12.534  -24.679 1.00 49.70  ? 777  MET   A C    1 
ATOM   2226 O  O    . MET   A 1 259 ? -20.459 12.794  -25.860 1.00 47.98  ? 777  MET   A O    1 
ATOM   2227 C  CB   . MET   A 1 259 ? -22.939 11.634  -24.050 1.00 52.02  ? 777  MET   A CB   1 
ATOM   2228 C  CG   . MET   A 1 259 ? -23.912 10.483  -24.091 1.00 55.29  ? 777  MET   A CG   1 
ATOM   2229 S  SD   . MET   A 1 259 ? -25.598 11.113  -24.016 1.00 57.93  ? 777  MET   A SD   1 
ATOM   2230 C  CE   . MET   A 1 259 ? -25.608 12.186  -25.450 1.00 57.87  ? 777  MET   A CE   1 
ATOM   2231 N  N    . CYS   A 1 260 ? -20.373 13.347  -23.683 1.00 45.99  ? 778  CYS   A N    1 
ATOM   2232 C  CA   . CYS   A 1 260 ? -19.835 14.674  -23.923 1.00 50.39  ? 778  CYS   A CA   1 
ATOM   2233 C  C    . CYS   A 1 260 ? -18.427 14.855  -23.381 1.00 52.15  ? 778  CYS   A C    1 
ATOM   2234 O  O    . CYS   A 1 260 ? -17.843 15.928  -23.570 1.00 52.98  ? 778  CYS   A O    1 
ATOM   2235 C  CB   . CYS   A 1 260 ? -20.769 15.729  -23.313 1.00 53.63  ? 778  CYS   A CB   1 
ATOM   2236 S  SG   . CYS   A 1 260 ? -22.522 15.451  -23.690 1.00 56.45  ? 778  CYS   A SG   1 
ATOM   2237 N  N    . GLY   A 1 261 ? -17.863 13.841  -22.728 1.00 57.87  ? 779  GLY   A N    1 
ATOM   2238 C  CA   . GLY   A 1 261 ? -16.534 13.937  -22.158 1.00 65.30  ? 779  GLY   A CA   1 
ATOM   2239 C  C    . GLY   A 1 261 ? -16.439 15.016  -21.104 1.00 73.42  ? 779  GLY   A C    1 
ATOM   2240 O  O    . GLY   A 1 261 ? -15.579 15.898  -21.190 1.00 76.55  ? 779  GLY   A O    1 
ATOM   2241 N  N    . LEU   A 1 262 ? -17.311 14.962  -20.100 1.00 75.66  ? 780  LEU   A N    1 
ATOM   2242 C  CA   . LEU   A 1 262 ? -17.412 16.076  -19.172 1.00 78.77  ? 780  LEU   A CA   1 
ATOM   2243 C  C    . LEU   A 1 262 ? -17.778 15.600  -17.776 1.00 74.67  ? 780  LEU   A C    1 
ATOM   2244 O  O    . LEU   A 1 262 ? -18.430 14.568  -17.595 1.00 74.79  ? 780  LEU   A O    1 
ATOM   2245 C  CB   . LEU   A 1 262 ? -18.436 17.099  -19.659 1.00 80.29  ? 780  LEU   A CB   1 
ATOM   2246 C  CG   . LEU   A 1 262 ? -17.776 18.255  -20.400 1.00 85.12  ? 780  LEU   A CG   1 
ATOM   2247 C  CD1  . LEU   A 1 262 ? -18.769 19.339  -20.603 1.00 84.08  ? 780  LEU   A CD1  1 
ATOM   2248 C  CD2  . LEU   A 1 262 ? -16.590 18.777  -19.616 1.00 93.12  ? 780  LEU   A CD2  1 
ATOM   2249 N  N    . GLY   A 1 263 ? -17.356 16.390  -16.797 1.00 67.64  ? 781  GLY   A N    1 
ATOM   2250 C  CA   . GLY   A 1 263 ? -17.611 16.098  -15.404 1.00 69.77  ? 781  GLY   A CA   1 
ATOM   2251 C  C    . GLY   A 1 263 ? -16.859 17.086  -14.536 1.00 80.87  ? 781  GLY   A C    1 
ATOM   2252 O  O    . GLY   A 1 263 ? -16.316 18.079  -15.024 1.00 88.25  ? 781  GLY   A O    1 
ATOM   2253 N  N    . ASP   A 1 264 ? -16.834 16.794  -13.241 1.00 86.07  ? 782  ASP   A N    1 
ATOM   2254 C  CA   . ASP   A 1 264 ? -16.088 17.623  -12.307 1.00 92.97  ? 782  ASP   A CA   1 
ATOM   2255 C  C    . ASP   A 1 264 ? -14.606 17.274  -12.359 1.00 96.09  ? 782  ASP   A C    1 
ATOM   2256 O  O    . ASP   A 1 264 ? -14.230 16.099  -12.400 1.00 100.00 ? 782  ASP   A O    1 
ATOM   2257 C  CB   . ASP   A 1 264 ? -16.618 17.446  -10.885 1.00 97.80  ? 782  ASP   A CB   1 
ATOM   2258 C  CG   . ASP   A 1 264 ? -17.958 18.123  -10.676 1.00 99.94  ? 782  ASP   A CG   1 
ATOM   2259 O  OD1  . ASP   A 1 264 ? -18.310 19.011  -11.480 1.00 99.41  ? 782  ASP   A OD1  1 
ATOM   2260 O  OD2  . ASP   A 1 264 ? -18.657 17.769  -9.703  1.00 101.13 ? 782  ASP   A OD2  1 
ATOM   2261 N  N    . VAL   A 1 265 ? -13.768 18.304  -12.370 1.00 94.55  ? 783  VAL   A N    1 
ATOM   2262 C  CA   . VAL   A 1 265 ? -12.320 18.150  -12.320 1.00 93.57  ? 783  VAL   A CA   1 
ATOM   2263 C  C    . VAL   A 1 265 ? -11.875 18.652  -10.953 1.00 98.66  ? 783  VAL   A C    1 
ATOM   2264 O  O    . VAL   A 1 265 ? -11.805 19.863  -10.717 1.00 102.88 ? 783  VAL   A O    1 
ATOM   2265 C  CB   . VAL   A 1 265 ? -11.616 18.906  -13.451 1.00 87.90  ? 783  VAL   A CB   1 
ATOM   2266 C  CG1  . VAL   A 1 265 ? -10.113 18.672  -13.389 1.00 86.63  ? 783  VAL   A CG1  1 
ATOM   2267 C  CG2  . VAL   A 1 265 ? -12.169 18.477  -14.794 1.00 84.84  ? 783  VAL   A CG2  1 
ATOM   2268 N  N    . ASP   A 1 266 ? -11.583 17.723  -10.044 1.00 99.22  ? 784  ASP   A N    1 
ATOM   2269 C  CA   . ASP   A 1 266 ? -11.123 18.092  -8.712  1.00 103.93 ? 784  ASP   A CA   1 
ATOM   2270 C  C    . ASP   A 1 266 ? -9.788  18.820  -8.814  1.00 110.35 ? 784  ASP   A C    1 
ATOM   2271 O  O    . ASP   A 1 266 ? -8.742  18.191  -9.004  1.00 112.66 ? 784  ASP   A O    1 
ATOM   2272 C  CB   . ASP   A 1 266 ? -11.009 16.854  -7.819  1.00 103.22 ? 784  ASP   A CB   1 
ATOM   2273 C  CG   . ASP   A 1 266 ? -10.854 17.203  -6.350  1.00 106.08 ? 784  ASP   A CG   1 
ATOM   2274 O  OD1  . ASP   A 1 266 ? -11.540 16.579  -5.515  1.00 105.44 ? 784  ASP   A OD1  1 
ATOM   2275 O  OD2  . ASP   A 1 266 ? -10.045 18.095  -6.025  1.00 110.77 ? 784  ASP   A OD2  1 
ATOM   2276 N  N    . VAL   A 1 267 ? -9.824  20.149  -8.690  1.00 84.52  ? 785  VAL   A N    1 
ATOM   2277 C  CA   . VAL   A 1 267 ? -8.618  20.957  -8.853  1.00 83.73  ? 785  VAL   A CA   1 
ATOM   2278 C  C    . VAL   A 1 267 ? -7.590  20.625  -7.781  1.00 89.57  ? 785  VAL   A C    1 
ATOM   2279 O  O    . VAL   A 1 267 ? -6.380  20.738  -8.014  1.00 90.40  ? 785  VAL   A O    1 
ATOM   2280 C  CB   . VAL   A 1 267 ? -8.984  22.455  -8.849  1.00 80.62  ? 785  VAL   A CB   1 
ATOM   2281 C  CG1  . VAL   A 1 267 ? -7.748  23.314  -9.073  1.00 78.65  ? 785  VAL   A CG1  1 
ATOM   2282 C  CG2  . VAL   A 1 267 ? -10.029 22.742  -9.913  1.00 80.22  ? 785  VAL   A CG2  1 
ATOM   2283 N  N    . ASN   A 1 268 ? -8.042  20.208  -6.597  1.00 95.89  ? 786  ASN   A N    1 
ATOM   2284 C  CA   . ASN   A 1 268 ? -7.106  19.774  -5.565  1.00 100.50 ? 786  ASN   A CA   1 
ATOM   2285 C  C    . ASN   A 1 268 ? -6.296  18.575  -6.043  1.00 100.65 ? 786  ASN   A C    1 
ATOM   2286 O  O    . ASN   A 1 268 ? -5.068  18.647  -6.154  1.00 102.02 ? 786  ASN   A O    1 
ATOM   2287 C  CB   . ASN   A 1 268 ? -7.854  19.448  -4.272  1.00 106.79 ? 786  ASN   A CB   1 
ATOM   2288 C  CG   . ASN   A 1 268 ? -8.226  20.689  -3.488  1.00 109.98 ? 786  ASN   A CG   1 
ATOM   2289 O  OD1  . ASN   A 1 268 ? -7.427  21.617  -3.358  1.00 110.62 ? 786  ASN   A OD1  1 
ATOM   2290 N  ND2  . ASN   A 1 268 ? -9.444  20.713  -2.960  1.00 112.79 ? 786  ASN   A ND2  1 
ATOM   2291 N  N    . ASP   A 1 269 ? -6.978  17.464  -6.346  1.00 99.04  ? 787  ASP   A N    1 
ATOM   2292 C  CA   . ASP   A 1 269 ? -6.300  16.270  -6.849  1.00 95.76  ? 787  ASP   A CA   1 
ATOM   2293 C  C    . ASP   A 1 269 ? -5.358  16.606  -7.999  1.00 87.79  ? 787  ASP   A C    1 
ATOM   2294 O  O    . ASP   A 1 269 ? -4.286  16.004  -8.134  1.00 87.22  ? 787  ASP   A O    1 
ATOM   2295 C  CB   . ASP   A 1 269 ? -7.333  15.232  -7.291  1.00 98.81  ? 787  ASP   A CB   1 
ATOM   2296 C  CG   . ASP   A 1 269 ? -6.709  13.891  -7.614  1.00 103.50 ? 787  ASP   A CG   1 
ATOM   2297 O  OD1  . ASP   A 1 269 ? -6.254  13.204  -6.676  1.00 107.44 ? 787  ASP   A OD1  1 
ATOM   2298 O  OD2  . ASP   A 1 269 ? -6.673  13.525  -8.807  1.00 104.40 ? 787  ASP   A OD2  1 
ATOM   2299 N  N    . TRP   A 1 270 ? -5.745  17.570  -8.835  1.00 81.38  ? 788  TRP   A N    1 
ATOM   2300 C  CA   . TRP   A 1 270 ? -4.839  18.099  -9.847  1.00 75.77  ? 788  TRP   A CA   1 
ATOM   2301 C  C    . TRP   A 1 270 ? -3.603  18.724  -9.208  1.00 76.83  ? 788  TRP   A C    1 
ATOM   2302 O  O    . TRP   A 1 270 ? -2.476  18.499  -9.665  1.00 76.30  ? 788  TRP   A O    1 
ATOM   2303 C  CB   . TRP   A 1 270 ? -5.584  19.125  -10.700 1.00 71.62  ? 788  TRP   A CB   1 
ATOM   2304 C  CG   . TRP   A 1 270 ? -4.951  19.446  -12.011 1.00 71.31  ? 788  TRP   A CG   1 
ATOM   2305 C  CD1  . TRP   A 1 270 ? -3.716  19.066  -12.448 1.00 74.95  ? 788  TRP   A CD1  1 
ATOM   2306 C  CD2  . TRP   A 1 270 ? -5.529  20.223  -13.065 1.00 72.64  ? 788  TRP   A CD2  1 
ATOM   2307 N  NE1  . TRP   A 1 270 ? -3.490  19.559  -13.710 1.00 75.81  ? 788  TRP   A NE1  1 
ATOM   2308 C  CE2  . TRP   A 1 270 ? -4.589  20.273  -14.111 1.00 75.10  ? 788  TRP   A CE2  1 
ATOM   2309 C  CE3  . TRP   A 1 270 ? -6.752  20.880  -13.224 1.00 74.27  ? 788  TRP   A CE3  1 
ATOM   2310 C  CZ2  . TRP   A 1 270 ? -4.832  20.954  -15.300 1.00 78.44  ? 788  TRP   A CZ2  1 
ATOM   2311 C  CZ3  . TRP   A 1 270 ? -6.993  21.556  -14.405 1.00 77.32  ? 788  TRP   A CZ3  1 
ATOM   2312 C  CH2  . TRP   A 1 270 ? -6.038  21.587  -15.428 1.00 79.38  ? 788  TRP   A CH2  1 
ATOM   2313 N  N    . ARG   A 1 271 ? -3.798  19.501  -8.138  1.00 80.45  ? 789  ARG   A N    1 
ATOM   2314 C  CA   . ARG   A 1 271 ? -2.699  20.247  -7.530  1.00 82.92  ? 789  ARG   A CA   1 
ATOM   2315 C  C    . ARG   A 1 271 ? -1.667  19.319  -6.900  1.00 86.59  ? 789  ARG   A C    1 
ATOM   2316 O  O    . ARG   A 1 271 ? -0.468  19.427  -7.182  1.00 89.48  ? 789  ARG   A O    1 
ATOM   2317 C  CB   . ARG   A 1 271 ? -3.245  21.209  -6.475  1.00 86.39  ? 789  ARG   A CB   1 
ATOM   2318 C  CG   . ARG   A 1 271 ? -3.676  22.562  -6.994  1.00 87.86  ? 789  ARG   A CG   1 
ATOM   2319 C  CD   . ARG   A 1 271 ? -3.841  23.553  -5.852  1.00 93.34  ? 789  ARG   A CD   1 
ATOM   2320 N  NE   . ARG   A 1 271 ? -4.327  22.904  -4.636  1.00 100.34 ? 789  ARG   A NE   1 
ATOM   2321 C  CZ   . ARG   A 1 271 ? -3.615  22.771  -3.521  1.00 104.90 ? 789  ARG   A CZ   1 
ATOM   2322 N  NH1  . ARG   A 1 271 ? -2.376  23.241  -3.462  1.00 105.46 ? 789  ARG   A NH1  1 
ATOM   2323 N  NH2  . ARG   A 1 271 ? -4.140  22.163  -2.466  1.00 106.95 ? 789  ARG   A NH2  1 
ATOM   2324 N  N    . GLU   A 1 272 ? -2.115  18.409  -6.029  1.00 88.42  ? 790  GLU   A N    1 
ATOM   2325 C  CA   . GLU   A 1 272 ? -1.184  17.615  -5.233  1.00 89.75  ? 790  GLU   A CA   1 
ATOM   2326 C  C    . GLU   A 1 272 ? -0.321  16.692  -6.081  1.00 86.54  ? 790  GLU   A C    1 
ATOM   2327 O  O    . GLU   A 1 272 ? 0.750   16.275  -5.627  1.00 90.11  ? 790  GLU   A O    1 
ATOM   2328 C  CB   . GLU   A 1 272 ? -1.941  16.789  -4.192  1.00 97.71  ? 790  GLU   A CB   1 
ATOM   2329 C  CG   . GLU   A 1 272 ? -2.632  17.615  -3.123  1.00 103.71 ? 790  GLU   A CG   1 
ATOM   2330 C  CD   . GLU   A 1 272 ? -4.125  17.370  -3.082  1.00 109.69 ? 790  GLU   A CD   1 
ATOM   2331 O  OE1  . GLU   A 1 272 ? -4.688  16.976  -4.122  1.00 110.25 ? 790  GLU   A OE1  1 
ATOM   2332 O  OE2  . GLU   A 1 272 ? -4.736  17.567  -2.012  1.00 113.51 ? 790  GLU   A OE2  1 
ATOM   2333 N  N    . HIS   A 1 273 ? -0.756  16.360  -7.294  1.00 80.56  ? 791  HIS   A N    1 
ATOM   2334 C  CA   . HIS   A 1 273 ? -0.009  15.474  -8.177  1.00 79.79  ? 791  HIS   A CA   1 
ATOM   2335 C  C    . HIS   A 1 273 ? 0.603   16.236  -9.348  1.00 77.54  ? 791  HIS   A C    1 
ATOM   2336 O  O    . HIS   A 1 273 ? 0.708   15.715  -10.461 1.00 80.24  ? 791  HIS   A O    1 
ATOM   2337 C  CB   . HIS   A 1 273 ? -0.906  14.337  -8.654  1.00 78.40  ? 791  HIS   A CB   1 
ATOM   2338 C  CG   . HIS   A 1 273 ? -1.583  13.613  -7.532  1.00 80.83  ? 791  HIS   A CG   1 
ATOM   2339 N  ND1  . HIS   A 1 273 ? -2.879  13.881  -7.147  1.00 80.63  ? 791  HIS   A ND1  1 
ATOM   2340 C  CD2  . HIS   A 1 273 ? -1.131  12.656  -6.689  1.00 84.59  ? 791  HIS   A CD2  1 
ATOM   2341 C  CE1  . HIS   A 1 273 ? -3.202  13.106  -6.127  1.00 83.85  ? 791  HIS   A CE1  1 
ATOM   2342 N  NE2  . HIS   A 1 273 ? -2.159  12.353  -5.830  1.00 86.62  ? 791  HIS   A NE2  1 
ATOM   2343 N  N    . THR   A 1 274 ? 1.017   17.472  -9.090  1.00 70.79  ? 792  THR   A N    1 
ATOM   2344 C  CA   . THR   A 1 274 ? 1.669   18.335  -10.060 1.00 65.12  ? 792  THR   A CA   1 
ATOM   2345 C  C    . THR   A 1 274 ? 3.130   18.520  -9.666  1.00 68.88  ? 792  THR   A C    1 
ATOM   2346 O  O    . THR   A 1 274 ? 3.442   18.688  -8.483  1.00 71.26  ? 792  THR   A O    1 
ATOM   2347 C  CB   . THR   A 1 274 ? 0.952   19.689  -10.126 1.00 64.81  ? 792  THR   A CB   1 
ATOM   2348 O  OG1  . THR   A 1 274 ? -0.389  19.503  -10.596 1.00 61.20  ? 792  THR   A OG1  1 
ATOM   2349 C  CG2  . THR   A 1 274 ? 1.663   20.633  -11.040 1.00 61.71  ? 792  THR   A CG2  1 
ATOM   2350 N  N    . LYS   A 1 275 ? 4.027   18.470  -10.652 1.00 74.65  ? 793  LYS   A N    1 
ATOM   2351 C  CA   . LYS   A 1 275 ? 5.458   18.642  -10.433 1.00 81.05  ? 793  LYS   A CA   1 
ATOM   2352 C  C    . LYS   A 1 275 ? 5.960   19.863  -11.191 1.00 85.48  ? 793  LYS   A C    1 
ATOM   2353 O  O    . LYS   A 1 275 ? 5.401   20.249  -12.216 1.00 92.94  ? 793  LYS   A O    1 
ATOM   2354 C  CB   . LYS   A 1 275 ? 6.244   17.404  -10.877 1.00 80.96  ? 793  LYS   A CB   1 
ATOM   2355 C  CG   . LYS   A 1 275 ? 5.966   16.170  -10.047 1.00 84.78  ? 793  LYS   A CG   1 
ATOM   2356 C  CD   . LYS   A 1 275 ? 6.023   16.495  -8.566  1.00 87.81  ? 793  LYS   A CD   1 
ATOM   2357 C  CE   . LYS   A 1 275 ? 7.127   15.714  -7.873  1.00 92.48  ? 793  LYS   A CE   1 
ATOM   2358 N  NZ   . LYS   A 1 275 ? 6.678   15.168  -6.563  1.00 93.83  ? 793  LYS   A NZ   1 
ATOM   2359 N  N    . TYR   A 1 276 ? 7.037   20.468  -10.696 1.00 86.05  ? 794  TYR   A N    1 
ATOM   2360 C  CA   . TYR   A 1 276 ? 7.526   21.722  -11.252 1.00 80.08  ? 794  TYR   A CA   1 
ATOM   2361 C  C    . TYR   A 1 276 ? 8.985   21.597  -11.663 1.00 79.71  ? 794  TYR   A C    1 
ATOM   2362 O  O    . TYR   A 1 276 ? 9.766   20.873  -11.041 1.00 79.85  ? 794  TYR   A O    1 
ATOM   2363 C  CB   . TYR   A 1 276 ? 7.356   22.867  -10.252 1.00 77.79  ? 794  TYR   A CB   1 
ATOM   2364 C  CG   . TYR   A 1 276 ? 5.947   22.970  -9.731  1.00 71.89  ? 794  TYR   A CG   1 
ATOM   2365 C  CD1  . TYR   A 1 276 ? 4.979   23.672  -10.434 1.00 69.81  ? 794  TYR   A CD1  1 
ATOM   2366 C  CD2  . TYR   A 1 276 ? 5.576   22.345  -8.549  1.00 68.87  ? 794  TYR   A CD2  1 
ATOM   2367 C  CE1  . TYR   A 1 276 ? 3.684   23.754  -9.973  1.00 69.57  ? 794  TYR   A CE1  1 
ATOM   2368 C  CE2  . TYR   A 1 276 ? 4.284   22.424  -8.077  1.00 67.77  ? 794  TYR   A CE2  1 
ATOM   2369 C  CZ   . TYR   A 1 276 ? 3.341   23.131  -8.792  1.00 68.21  ? 794  TYR   A CZ   1 
ATOM   2370 O  OH   . TYR   A 1 276 ? 2.051   23.213  -8.324  1.00 66.82  ? 794  TYR   A OH   1 
ATOM   2371 N  N    . LYS   A 1 277 ? 9.342   22.323  -12.719 1.00 80.89  ? 795  LYS   A N    1 
ATOM   2372 C  CA   . LYS   A 1 277 ? 10.677  22.281  -13.293 1.00 84.86  ? 795  LYS   A CA   1 
ATOM   2373 C  C    . LYS   A 1 277 ? 11.274  23.679  -13.347 1.00 82.68  ? 795  LYS   A C    1 
ATOM   2374 O  O    . LYS   A 1 277 ? 10.552  24.679  -13.408 1.00 78.64  ? 795  LYS   A O    1 
ATOM   2375 C  CB   . LYS   A 1 277 ? 10.661  21.741  -14.712 1.00 89.24  ? 795  LYS   A CB   1 
ATOM   2376 C  CG   . LYS   A 1 277 ? 10.107  20.375  -14.902 1.00 92.38  ? 795  LYS   A CG   1 
ATOM   2377 C  CD   . LYS   A 1 277 ? 11.125  19.526  -15.567 1.00 101.73 ? 795  LYS   A CD   1 
ATOM   2378 C  CE   . LYS   A 1 277 ? 11.168  19.774  -17.056 1.00 109.99 ? 795  LYS   A CE   1 
ATOM   2379 N  NZ   . LYS   A 1 277 ? 10.171  18.965  -17.807 1.00 110.30 ? 795  LYS   A NZ   1 
ATOM   2380 N  N    . ASN   A 1 278 ? 12.605  23.724  -13.363 1.00 87.83  ? 796  ASN   A N    1 
ATOM   2381 C  CA   . ASN   A 1 278 ? 13.372  24.940  -13.636 1.00 92.11  ? 796  ASN   A CA   1 
ATOM   2382 C  C    . ASN   A 1 278 ? 12.934  26.105  -12.750 1.00 86.69  ? 796  ASN   A C    1 
ATOM   2383 O  O    . ASN   A 1 278 ? 12.675  27.215  -13.220 1.00 86.15  ? 796  ASN   A O    1 
ATOM   2384 C  CB   . ASN   A 1 278 ? 13.286  25.318  -15.117 1.00 96.12  ? 796  ASN   A CB   1 
ATOM   2385 C  CG   . ASN   A 1 278 ? 14.459  26.172  -15.568 1.00 102.49 ? 796  ASN   A CG   1 
ATOM   2386 O  OD1  . ASN   A 1 278 ? 15.431  26.347  -14.833 1.00 105.32 ? 796  ASN   A OD1  1 
ATOM   2387 N  ND2  . ASN   A 1 278 ? 14.371  26.710  -16.780 1.00 105.19 ? 796  ASN   A ND2  1 
ATOM   2388 N  N    . GLY   A 1 279 ? 12.851  25.845  -11.448 1.00 83.51  ? 797  GLY   A N    1 
ATOM   2389 C  CA   . GLY   A 1 279 ? 12.681  26.886  -10.462 1.00 84.00  ? 797  GLY   A CA   1 
ATOM   2390 C  C    . GLY   A 1 279 ? 11.271  27.064  -9.937  1.00 84.12  ? 797  GLY   A C    1 
ATOM   2391 O  O    . GLY   A 1 279 ? 11.098  27.696  -8.888  1.00 85.57  ? 797  GLY   A O    1 
ATOM   2392 N  N    . TYR   A 1 280 ? 10.262  26.544  -10.632 1.00 81.46  ? 798  TYR   A N    1 
ATOM   2393 C  CA   . TYR   A 1 280 ? 8.896   26.664  -10.142 1.00 76.97  ? 798  TYR   A CA   1 
ATOM   2394 C  C    . TYR   A 1 280 ? 8.691   25.786  -8.912  1.00 75.68  ? 798  TYR   A C    1 
ATOM   2395 O  O    . TYR   A 1 280 ? 9.389   24.789  -8.705  1.00 74.90  ? 798  TYR   A O    1 
ATOM   2396 C  CB   . TYR   A 1 280 ? 7.888   26.276  -11.227 1.00 72.06  ? 798  TYR   A CB   1 
ATOM   2397 C  CG   . TYR   A 1 280 ? 7.494   27.395  -12.171 1.00 73.44  ? 798  TYR   A CG   1 
ATOM   2398 C  CD1  . TYR   A 1 280 ? 7.038   27.111  -13.452 1.00 72.04  ? 798  TYR   A CD1  1 
ATOM   2399 C  CD2  . TYR   A 1 280 ? 7.568   28.730  -11.783 1.00 79.17  ? 798  TYR   A CD2  1 
ATOM   2400 C  CE1  . TYR   A 1 280 ? 6.670   28.119  -14.324 1.00 70.60  ? 798  TYR   A CE1  1 
ATOM   2401 C  CE2  . TYR   A 1 280 ? 7.201   29.751  -12.652 1.00 76.60  ? 798  TYR   A CE2  1 
ATOM   2402 C  CZ   . TYR   A 1 280 ? 6.758   29.435  -13.923 1.00 73.02  ? 798  TYR   A CZ   1 
ATOM   2403 O  OH   . TYR   A 1 280 ? 6.397   30.434  -14.799 1.00 69.75  ? 798  TYR   A OH   1 
ATOM   2404 N  N    . SER   A 1 281 ? 7.719   26.171  -8.090  1.00 74.76  ? 799  SER   A N    1 
ATOM   2405 C  CA   . SER   A 1 281 ? 7.379   25.429  -6.884  1.00 73.68  ? 799  SER   A CA   1 
ATOM   2406 C  C    . SER   A 1 281 ? 5.930   25.736  -6.532  1.00 72.61  ? 799  SER   A C    1 
ATOM   2407 O  O    . SER   A 1 281 ? 5.321   26.656  -7.081  1.00 73.17  ? 799  SER   A O    1 
ATOM   2408 C  CB   . SER   A 1 281 ? 8.315   25.783  -5.724  1.00 75.06  ? 799  SER   A CB   1 
ATOM   2409 O  OG   . SER   A 1 281 ? 8.216   27.158  -5.395  1.00 76.20  ? 799  SER   A OG   1 
ATOM   2410 N  N    . ALA   A 1 282 ? 5.384   24.952  -5.599  1.00 74.76  ? 800  ALA   A N    1 
ATOM   2411 C  CA   . ALA   A 1 282 ? 3.994   25.151  -5.197  1.00 77.96  ? 800  ALA   A CA   1 
ATOM   2412 C  C    . ALA   A 1 282 ? 3.788   26.523  -4.568  1.00 81.43  ? 800  ALA   A C    1 
ATOM   2413 O  O    . ALA   A 1 282 ? 2.735   27.145  -4.749  1.00 80.29  ? 800  ALA   A O    1 
ATOM   2414 C  CB   . ALA   A 1 282 ? 3.562   24.047  -4.233  1.00 72.01  ? 800  ALA   A CB   1 
ATOM   2415 N  N    . ASN   A 1 283 ? 4.782   27.015  -3.830  1.00 88.00  ? 801  ASN   A N    1 
ATOM   2416 C  CA   . ASN   A 1 283 ? 4.691   28.313  -3.175  1.00 93.69  ? 801  ASN   A CA   1 
ATOM   2417 C  C    . ASN   A 1 283 ? 5.109   29.469  -4.073  1.00 91.99  ? 801  ASN   A C    1 
ATOM   2418 O  O    . ASN   A 1 283 ? 4.935   30.629  -3.680  1.00 91.73  ? 801  ASN   A O    1 
ATOM   2419 C  CB   . ASN   A 1 283 ? 5.545   28.323  -1.902  1.00 99.51  ? 801  ASN   A CB   1 
ATOM   2420 C  CG   . ASN   A 1 283 ? 6.847   27.565  -2.069  1.00 102.83 ? 801  ASN   A CG   1 
ATOM   2421 O  OD1  . ASN   A 1 283 ? 6.853   26.341  -2.205  1.00 101.07 ? 801  ASN   A OD1  1 
ATOM   2422 N  ND2  . ASN   A 1 283 ? 7.959   28.290  -2.060  1.00 106.65 ? 801  ASN   A ND2  1 
ATOM   2423 N  N    . HIS   A 1 284 ? 5.659   29.187  -5.253  1.00 88.13  ? 802  HIS   A N    1 
ATOM   2424 C  CA   . HIS   A 1 284 ? 6.024   30.244  -6.187  1.00 84.21  ? 802  HIS   A CA   1 
ATOM   2425 C  C    . HIS   A 1 284 ? 4.794   31.057  -6.571  1.00 81.64  ? 802  HIS   A C    1 
ATOM   2426 O  O    . HIS   A 1 284 ? 3.693   30.518  -6.713  1.00 78.73  ? 802  HIS   A O    1 
ATOM   2427 C  CB   . HIS   A 1 284 ? 6.676   29.643  -7.433  1.00 80.50  ? 802  HIS   A CB   1 
ATOM   2428 C  CG   . HIS   A 1 284 ? 7.410   30.639  -8.274  1.00 79.83  ? 802  HIS   A CG   1 
ATOM   2429 N  ND1  . HIS   A 1 284 ? 6.767   31.501  -9.137  1.00 78.66  ? 802  HIS   A ND1  1 
ATOM   2430 C  CD2  . HIS   A 1 284 ? 8.732   30.908  -8.390  1.00 82.65  ? 802  HIS   A CD2  1 
ATOM   2431 C  CE1  . HIS   A 1 284 ? 7.662   32.259  -9.746  1.00 82.41  ? 802  HIS   A CE1  1 
ATOM   2432 N  NE2  . HIS   A 1 284 ? 8.861   31.919  -9.310  1.00 85.21  ? 802  HIS   A NE2  1 
ATOM   2433 N  N    . GLN   A 1 285 ? 4.988   32.368  -6.744  1.00 83.79  ? 803  GLN   A N    1 
ATOM   2434 C  CA   . GLN   A 1 285 ? 3.840   33.255  -6.905  1.00 84.64  ? 803  GLN   A CA   1 
ATOM   2435 C  C    . GLN   A 1 285 ? 3.170   33.082  -8.264  1.00 80.15  ? 803  GLN   A C    1 
ATOM   2436 O  O    . GLN   A 1 285 ? 1.944   33.205  -8.366  1.00 78.75  ? 803  GLN   A O    1 
ATOM   2437 C  CB   . GLN   A 1 285 ? 4.253   34.710  -6.678  1.00 91.30  ? 803  GLN   A CB   1 
ATOM   2438 C  CG   . GLN   A 1 285 ? 3.410   35.726  -7.433  1.00 95.46  ? 803  GLN   A CG   1 
ATOM   2439 C  CD   . GLN   A 1 285 ? 3.338   37.062  -6.724  1.00 106.02 ? 803  GLN   A CD   1 
ATOM   2440 O  OE1  . GLN   A 1 285 ? 2.689   37.191  -5.686  1.00 109.07 ? 803  GLN   A OE1  1 
ATOM   2441 N  NE2  . GLN   A 1 285 ? 4.005   38.066  -7.281  1.00 112.25 ? 803  GLN   A NE2  1 
ATOM   2442 N  N    . VAL   A 1 286 ? 3.940   32.782  -9.310  1.00 78.08  ? 804  VAL   A N    1 
ATOM   2443 C  CA   . VAL   A 1 286 ? 3.329   32.487  -10.603 1.00 73.06  ? 804  VAL   A CA   1 
ATOM   2444 C  C    . VAL   A 1 286 ? 2.487   31.221  -10.513 1.00 69.90  ? 804  VAL   A C    1 
ATOM   2445 O  O    . VAL   A 1 286 ? 1.415   31.123  -11.124 1.00 66.61  ? 804  VAL   A O    1 
ATOM   2446 C  CB   . VAL   A 1 286 ? 4.407   32.380  -11.697 1.00 68.69  ? 804  VAL   A CB   1 
ATOM   2447 C  CG1  . VAL   A 1 286 ? 3.777   32.027  -13.036 1.00 65.78  ? 804  VAL   A CG1  1 
ATOM   2448 C  CG2  . VAL   A 1 286 ? 5.179   33.685  -11.804 1.00 71.22  ? 804  VAL   A CG2  1 
ATOM   2449 N  N    . ILE   A 1 287 ? 2.943   30.241  -9.730  1.00 69.40  ? 805  ILE   A N    1 
ATOM   2450 C  CA   . ILE   A 1 287 ? 2.210   28.984  -9.618  1.00 68.60  ? 805  ILE   A CA   1 
ATOM   2451 C  C    . ILE   A 1 287 ? 0.907   29.185  -8.852  1.00 71.27  ? 805  ILE   A C    1 
ATOM   2452 O  O    . ILE   A 1 287 ? -0.141  28.652  -9.240  1.00 66.72  ? 805  ILE   A O    1 
ATOM   2453 C  CB   . ILE   A 1 287 ? 3.095   27.904  -8.971  1.00 69.74  ? 805  ILE   A CB   1 
ATOM   2454 C  CG1  . ILE   A 1 287 ? 4.229   27.512  -9.922  1.00 73.54  ? 805  ILE   A CG1  1 
ATOM   2455 C  CG2  . ILE   A 1 287 ? 2.266   26.686  -8.593  1.00 67.70  ? 805  ILE   A CG2  1 
ATOM   2456 C  CD1  . ILE   A 1 287 ? 3.756   27.055  -11.284 1.00 73.37  ? 805  ILE   A CD1  1 
ATOM   2457 N  N    . GLN   A 1 288 ? 0.938   29.956  -7.760  1.00 79.02  ? 806  GLN   A N    1 
ATOM   2458 C  CA   . GLN   A 1 288 ? -0.305  30.217  -7.042  1.00 81.54  ? 806  GLN   A CA   1 
ATOM   2459 C  C    . GLN   A 1 288 ? -1.234  31.134  -7.827  1.00 81.91  ? 806  GLN   A C    1 
ATOM   2460 O  O    . GLN   A 1 288 ? -2.440  31.145  -7.562  1.00 87.19  ? 806  GLN   A O    1 
ATOM   2461 C  CB   . GLN   A 1 288 ? -0.026  30.800  -5.651  1.00 85.99  ? 806  GLN   A CB   1 
ATOM   2462 C  CG   . GLN   A 1 288 ? 0.935   31.967  -5.613  1.00 95.26  ? 806  GLN   A CG   1 
ATOM   2463 C  CD   . GLN   A 1 288 ? 1.560   32.166  -4.241  1.00 101.60 ? 806  GLN   A CD   1 
ATOM   2464 O  OE1  . GLN   A 1 288 ? 2.562   32.865  -4.094  1.00 105.58 ? 806  GLN   A OE1  1 
ATOM   2465 N  NE2  . GLN   A 1 288 ? 0.965   31.550  -3.227  1.00 103.00 ? 806  GLN   A NE2  1 
ATOM   2466 N  N    . TRP   A 1 289 ? -0.704  31.897  -8.787  1.00 78.24  ? 807  TRP   A N    1 
ATOM   2467 C  CA   . TRP   A 1 289 ? -1.573  32.586  -9.737  1.00 76.40  ? 807  TRP   A CA   1 
ATOM   2468 C  C    . TRP   A 1 289 ? -2.176  31.600  -10.728 1.00 72.98  ? 807  TRP   A C    1 
ATOM   2469 O  O    . TRP   A 1 289 ? -3.361  31.698  -11.070 1.00 72.11  ? 807  TRP   A O    1 
ATOM   2470 C  CB   . TRP   A 1 289 ? -0.796  33.673  -10.480 1.00 72.84  ? 807  TRP   A CB   1 
ATOM   2471 C  CG   . TRP   A 1 289 ? -0.686  34.966  -9.736  1.00 74.86  ? 807  TRP   A CG   1 
ATOM   2472 C  CD1  . TRP   A 1 289 ? -1.497  35.408  -8.733  1.00 75.18  ? 807  TRP   A CD1  1 
ATOM   2473 C  CD2  . TRP   A 1 289 ? 0.293   35.992  -9.942  1.00 76.25  ? 807  TRP   A CD2  1 
ATOM   2474 N  NE1  . TRP   A 1 289 ? -1.083  36.643  -8.299  1.00 76.78  ? 807  TRP   A NE1  1 
ATOM   2475 C  CE2  . TRP   A 1 289 ? 0.015   37.024  -9.025  1.00 79.73  ? 807  TRP   A CE2  1 
ATOM   2476 C  CE3  . TRP   A 1 289 ? 1.379   36.137  -10.812 1.00 75.75  ? 807  TRP   A CE3  1 
ATOM   2477 C  CZ2  . TRP   A 1 289 ? 0.783   38.186  -8.953  1.00 84.30  ? 807  TRP   A CZ2  1 
ATOM   2478 C  CZ3  . TRP   A 1 289 ? 2.140   37.290  -10.738 1.00 79.34  ? 807  TRP   A CZ3  1 
ATOM   2479 C  CH2  . TRP   A 1 289 ? 1.838   38.300  -9.816  1.00 83.98  ? 807  TRP   A CH2  1 
ATOM   2480 N  N    . PHE   A 1 290 ? -1.369  30.646  -11.199 1.00 71.27  ? 808  PHE   A N    1 
ATOM   2481 C  CA   . PHE   A 1 290 ? -1.864  29.627  -12.118 1.00 69.46  ? 808  PHE   A CA   1 
ATOM   2482 C  C    . PHE   A 1 290 ? -3.009  28.835  -11.501 1.00 67.68  ? 808  PHE   A C    1 
ATOM   2483 O  O    . PHE   A 1 290 ? -4.021  28.574  -12.163 1.00 65.42  ? 808  PHE   A O    1 
ATOM   2484 C  CB   . PHE   A 1 290 ? -0.721  28.691  -12.519 1.00 65.85  ? 808  PHE   A CB   1 
ATOM   2485 C  CG   . PHE   A 1 290 ? -1.178  27.394  -13.130 1.00 63.99  ? 808  PHE   A CG   1 
ATOM   2486 C  CD1  . PHE   A 1 290 ? -1.511  27.326  -14.472 1.00 67.19  ? 808  PHE   A CD1  1 
ATOM   2487 C  CD2  . PHE   A 1 290 ? -1.266  26.241  -12.363 1.00 56.39  ? 808  PHE   A CD2  1 
ATOM   2488 C  CE1  . PHE   A 1 290 ? -1.928  26.135  -15.039 1.00 63.61  ? 808  PHE   A CE1  1 
ATOM   2489 C  CE2  . PHE   A 1 290 ? -1.685  25.048  -12.922 1.00 57.42  ? 808  PHE   A CE2  1 
ATOM   2490 C  CZ   . PHE   A 1 290 ? -2.015  24.995  -14.263 1.00 60.90  ? 808  PHE   A CZ   1 
ATOM   2491 N  N    . TRP   A 1 291 ? -2.875  28.451  -10.230 1.00 66.57  ? 809  TRP   A N    1 
ATOM   2492 C  CA   . TRP   A 1 291 ? -3.892  27.604  -9.621  1.00 67.68  ? 809  TRP   A CA   1 
ATOM   2493 C  C    . TRP   A 1 291 ? -5.180  28.359  -9.336  1.00 68.97  ? 809  TRP   A C    1 
ATOM   2494 O  O    . TRP   A 1 291 ? -6.264  27.768  -9.409  1.00 69.28  ? 809  TRP   A O    1 
ATOM   2495 C  CB   . TRP   A 1 291 ? -3.359  26.959  -8.346  1.00 71.05  ? 809  TRP   A CB   1 
ATOM   2496 C  CG   . TRP   A 1 291 ? -2.473  25.802  -8.635  1.00 71.27  ? 809  TRP   A CG   1 
ATOM   2497 C  CD1  . TRP   A 1 291 ? -1.189  25.632  -8.220  1.00 70.68  ? 809  TRP   A CD1  1 
ATOM   2498 C  CD2  . TRP   A 1 291 ? -2.798  24.650  -9.426  1.00 73.64  ? 809  TRP   A CD2  1 
ATOM   2499 N  NE1  . TRP   A 1 291 ? -0.694  24.441  -8.692  1.00 73.36  ? 809  TRP   A NE1  1 
ATOM   2500 C  CE2  . TRP   A 1 291 ? -1.662  23.819  -9.435  1.00 74.09  ? 809  TRP   A CE2  1 
ATOM   2501 C  CE3  . TRP   A 1 291 ? -3.944  24.235  -10.117 1.00 76.51  ? 809  TRP   A CE3  1 
ATOM   2502 C  CZ2  . TRP   A 1 291 ? -1.634  22.600  -10.110 1.00 75.48  ? 809  TRP   A CZ2  1 
ATOM   2503 C  CZ3  . TRP   A 1 291 ? -3.913  23.026  -10.788 1.00 76.56  ? 809  TRP   A CZ3  1 
ATOM   2504 C  CH2  . TRP   A 1 291 ? -2.766  22.223  -10.779 1.00 77.49  ? 809  TRP   A CH2  1 
ATOM   2505 N  N    . LYS   A 1 292 ? -5.107  29.648  -9.008  1.00 71.95  ? 810  LYS   A N    1 
ATOM   2506 C  CA   . LYS   A 1 292 ? -6.363  30.352  -8.787  1.00 75.61  ? 810  LYS   A CA   1 
ATOM   2507 C  C    . LYS   A 1 292 ? -6.969  30.810  -10.110 1.00 75.50  ? 810  LYS   A C    1 
ATOM   2508 O  O    . LYS   A 1 292 ? -8.182  31.028  -10.193 1.00 75.40  ? 810  LYS   A O    1 
ATOM   2509 C  CB   . LYS   A 1 292 ? -6.173  31.504  -7.798  1.00 80.84  ? 810  LYS   A CB   1 
ATOM   2510 C  CG   . LYS   A 1 292 ? -5.757  32.839  -8.351  1.00 84.23  ? 810  LYS   A CG   1 
ATOM   2511 C  CD   . LYS   A 1 292 ? -6.655  33.911  -7.748  1.00 87.51  ? 810  LYS   A CD   1 
ATOM   2512 C  CE   . LYS   A 1 292 ? -6.282  35.300  -8.217  1.00 87.98  ? 810  LYS   A CE   1 
ATOM   2513 N  NZ   . LYS   A 1 292 ? -6.781  36.361  -7.307  1.00 93.28  ? 810  LYS   A NZ   1 
ATOM   2514 N  N    . ALA   A 1 293 ? -6.155  30.919  -11.162 1.00 74.70  ? 811  ALA   A N    1 
ATOM   2515 C  CA   . ALA   A 1 293 ? -6.714  31.050  -12.503 1.00 76.98  ? 811  ALA   A CA   1 
ATOM   2516 C  C    . ALA   A 1 293 ? -7.546  29.823  -12.859 1.00 76.54  ? 811  ALA   A C    1 
ATOM   2517 O  O    . ALA   A 1 293 ? -8.695  29.941  -13.301 1.00 78.88  ? 811  ALA   A O    1 
ATOM   2518 C  CB   . ALA   A 1 293 ? -5.595  31.261  -13.524 1.00 76.58  ? 811  ALA   A CB   1 
ATOM   2519 N  N    . VAL   A 1 294 ? -6.982  28.630  -12.657 1.00 75.41  ? 812  VAL   A N    1 
ATOM   2520 C  CA   . VAL   A 1 294 ? -7.703  27.398  -12.968 1.00 75.34  ? 812  VAL   A CA   1 
ATOM   2521 C  C    . VAL   A 1 294 ? -8.906  27.240  -12.048 1.00 75.64  ? 812  VAL   A C    1 
ATOM   2522 O  O    . VAL   A 1 294 ? -9.956  26.725  -12.454 1.00 75.15  ? 812  VAL   A O    1 
ATOM   2523 C  CB   . VAL   A 1 294 ? -6.753  26.189  -12.879 1.00 76.12  ? 812  VAL   A CB   1 
ATOM   2524 C  CG1  . VAL   A 1 294 ? -7.532  24.877  -12.865 1.00 74.90  ? 812  VAL   A CG1  1 
ATOM   2525 C  CG2  . VAL   A 1 294 ? -5.766  26.222  -14.023 1.00 76.19  ? 812  VAL   A CG2  1 
ATOM   2526 N  N    . LEU   A 1 295 ? -8.779  27.690  -10.797 1.00 78.02  ? 813  LEU   A N    1 
ATOM   2527 C  CA   . LEU   A 1 295 ? -9.901  27.609  -9.868  1.00 84.17  ? 813  LEU   A CA   1 
ATOM   2528 C  C    . LEU   A 1 295 ? -11.099 28.392  -10.390 1.00 89.75  ? 813  LEU   A C    1 
ATOM   2529 O  O    . LEU   A 1 295 ? -12.217 27.868  -10.454 1.00 92.83  ? 813  LEU   A O    1 
ATOM   2530 C  CB   . LEU   A 1 295 ? -9.479  28.114  -8.486  1.00 87.68  ? 813  LEU   A CB   1 
ATOM   2531 C  CG   . LEU   A 1 295 ? -10.296 27.671  -7.262  1.00 93.18  ? 813  LEU   A CG   1 
ATOM   2532 C  CD1  . LEU   A 1 295 ? -11.731 28.202  -7.270  1.00 98.24  ? 813  LEU   A CD1  1 
ATOM   2533 C  CD2  . LEU   A 1 295 ? -10.291 26.154  -7.145  1.00 91.52  ? 813  LEU   A CD2  1 
ATOM   2534 N  N    . MET   A 1 296 ? -10.887 29.650  -10.774 1.00 88.81  ? 814  MET   A N    1 
ATOM   2535 C  CA   . MET   A 1 296 ? -11.988 30.476  -11.252 1.00 89.40  ? 814  MET   A CA   1 
ATOM   2536 C  C    . MET   A 1 296 ? -12.344 30.212  -12.710 1.00 86.31  ? 814  MET   A C    1 
ATOM   2537 O  O    . MET   A 1 296 ? -13.221 30.897  -13.248 1.00 89.71  ? 814  MET   A O    1 
ATOM   2538 C  CB   . MET   A 1 296 ? -11.665 31.959  -11.043 1.00 93.01  ? 814  MET   A CB   1 
ATOM   2539 C  CG   . MET   A 1 296 ? -10.594 32.522  -11.958 1.00 94.64  ? 814  MET   A CG   1 
ATOM   2540 S  SD   . MET   A 1 296 ? -10.476 34.319  -11.833 1.00 98.52  ? 814  MET   A SD   1 
ATOM   2541 C  CE   . MET   A 1 296 ? -10.029 34.511  -10.110 1.00 98.76  ? 814  MET   A CE   1 
ATOM   2542 N  N    . MET   A 1 297 ? -11.700 29.245  -13.359 1.00 80.57  ? 815  MET   A N    1 
ATOM   2543 C  CA   . MET   A 1 297 ? -12.109 28.826  -14.691 1.00 81.20  ? 815  MET   A CA   1 
ATOM   2544 C  C    . MET   A 1 297 ? -13.333 27.926  -14.598 1.00 80.79  ? 815  MET   A C    1 
ATOM   2545 O  O    . MET   A 1 297 ? -13.465 27.130  -13.664 1.00 78.45  ? 815  MET   A O    1 
ATOM   2546 C  CB   . MET   A 1 297 ? -10.971 28.089  -15.400 1.00 82.76  ? 815  MET   A CB   1 
ATOM   2547 C  CG   . MET   A 1 297 ? -9.955  29.003  -16.064 1.00 88.70  ? 815  MET   A CG   1 
ATOM   2548 S  SD   . MET   A 1 297 ? -8.376  28.203  -16.416 1.00 88.41  ? 815  MET   A SD   1 
ATOM   2549 C  CE   . MET   A 1 297 ? -8.923  26.658  -17.129 1.00 84.45  ? 815  MET   A CE   1 
ATOM   2550 N  N    . ASP   A 1 298 ? -14.235 28.061  -15.567 1.00 84.36  ? 816  ASP   A N    1 
ATOM   2551 C  CA   . ASP   A 1 298 ? -15.415 27.212  -15.591 1.00 88.90  ? 816  ASP   A CA   1 
ATOM   2552 C  C    . ASP   A 1 298 ? -15.015 25.759  -15.840 1.00 85.22  ? 816  ASP   A C    1 
ATOM   2553 O  O    . ASP   A 1 298 ? -13.917 25.461  -16.319 1.00 80.96  ? 816  ASP   A O    1 
ATOM   2554 C  CB   . ASP   A 1 298 ? -16.407 27.686  -16.655 1.00 95.76  ? 816  ASP   A CB   1 
ATOM   2555 C  CG   . ASP   A 1 298 ? -15.784 27.788  -18.034 1.00 99.64  ? 816  ASP   A CG   1 
ATOM   2556 O  OD1  . ASP   A 1 298 ? -15.234 28.860  -18.362 1.00 101.87 ? 816  ASP   A OD1  1 
ATOM   2557 O  OD2  . ASP   A 1 298 ? -15.852 26.799  -18.792 1.00 100.62 ? 816  ASP   A OD2  1 
ATOM   2558 N  N    . SER   A 1 299 ? -15.930 24.848  -15.498 1.00 88.37  ? 817  SER   A N    1 
ATOM   2559 C  CA   . SER   A 1 299 ? -15.623 23.422  -15.570 1.00 89.19  ? 817  SER   A CA   1 
ATOM   2560 C  C    . SER   A 1 299 ? -15.247 22.991  -16.981 1.00 87.80  ? 817  SER   A C    1 
ATOM   2561 O  O    . SER   A 1 299 ? -14.462 22.052  -17.153 1.00 84.06  ? 817  SER   A O    1 
ATOM   2562 C  CB   . SER   A 1 299 ? -16.811 22.603  -15.064 1.00 93.04  ? 817  SER   A CB   1 
ATOM   2563 O  OG   . SER   A 1 299 ? -16.858 21.334  -15.691 1.00 93.73  ? 817  SER   A OG   1 
ATOM   2564 N  N    . GLU   A 1 300 ? -15.787 23.663  -18.001 1.00 90.23  ? 818  GLU   A N    1 
ATOM   2565 C  CA   . GLU   A 1 300 ? -15.433 23.317  -19.373 1.00 93.52  ? 818  GLU   A CA   1 
ATOM   2566 C  C    . GLU   A 1 300 ? -14.005 23.735  -19.699 1.00 89.42  ? 818  GLU   A C    1 
ATOM   2567 O  O    . GLU   A 1 300 ? -13.262 22.977  -20.333 1.00 89.88  ? 818  GLU   A O    1 
ATOM   2568 C  CB   . GLU   A 1 300 ? -16.413 23.964  -20.352 1.00 102.76 ? 818  GLU   A CB   1 
ATOM   2569 C  CG   . GLU   A 1 300 ? -16.091 23.689  -21.814 1.00 108.66 ? 818  GLU   A CG   1 
ATOM   2570 C  CD   . GLU   A 1 300 ? -15.761 24.951  -22.589 1.00 112.63 ? 818  GLU   A CD   1 
ATOM   2571 O  OE1  . GLU   A 1 300 ? -15.662 26.028  -21.964 1.00 112.77 ? 818  GLU   A OE1  1 
ATOM   2572 O  OE2  . GLU   A 1 300 ? -15.597 24.864  -23.825 1.00 115.05 ? 818  GLU   A OE2  1 
ATOM   2573 N  N    . LYS   A 1 301 ? -13.600 24.934  -19.273 1.00 87.17  ? 819  LYS   A N    1 
ATOM   2574 C  CA   . LYS   A 1 301 ? -12.260 25.410  -19.600 1.00 83.40  ? 819  LYS   A CA   1 
ATOM   2575 C  C    . LYS   A 1 301 ? -11.190 24.681  -18.796 1.00 78.29  ? 819  LYS   A C    1 
ATOM   2576 O  O    . LYS   A 1 301 ? -10.054 24.547  -19.265 1.00 76.58  ? 819  LYS   A O    1 
ATOM   2577 C  CB   . LYS   A 1 301 ? -12.167 26.920  -19.384 1.00 85.40  ? 819  LYS   A CB   1 
ATOM   2578 C  CG   . LYS   A 1 301 ? -12.847 27.740  -20.476 1.00 92.94  ? 819  LYS   A CG   1 
ATOM   2579 C  CD   . LYS   A 1 301 ? -11.850 28.235  -21.518 1.00 96.55  ? 819  LYS   A CD   1 
ATOM   2580 C  CE   . LYS   A 1 301 ? -12.060 27.555  -22.866 1.00 100.48 ? 819  LYS   A CE   1 
ATOM   2581 N  NZ   . LYS   A 1 301 ? -11.400 28.303  -23.975 1.00 103.13 ? 819  LYS   A NZ   1 
ATOM   2582 N  N    . ARG   A 1 302 ? -11.523 24.214  -17.588 1.00 76.59  ? 820  ARG   A N    1 
ATOM   2583 C  CA   . ARG   A 1 302 ? -10.620 23.312  -16.878 1.00 73.44  ? 820  ARG   A CA   1 
ATOM   2584 C  C    . ARG   A 1 302 ? -10.335 22.071  -17.711 1.00 73.31  ? 820  ARG   A C    1 
ATOM   2585 O  O    . ARG   A 1 302 ? -9.200  21.581  -17.747 1.00 69.25  ? 820  ARG   A O    1 
ATOM   2586 C  CB   . ARG   A 1 302 ? -11.214 22.909  -15.529 1.00 72.13  ? 820  ARG   A CB   1 
ATOM   2587 C  CG   . ARG   A 1 302 ? -11.272 24.008  -14.485 1.00 71.71  ? 820  ARG   A CG   1 
ATOM   2588 C  CD   . ARG   A 1 302 ? -11.860 23.464  -13.191 1.00 73.58  ? 820  ARG   A CD   1 
ATOM   2589 N  NE   . ARG   A 1 302 ? -12.213 24.518  -12.246 1.00 74.77  ? 820  ARG   A NE   1 
ATOM   2590 C  CZ   . ARG   A 1 302 ? -12.906 24.315  -11.130 1.00 75.42  ? 820  ARG   A CZ   1 
ATOM   2591 N  NH1  . ARG   A 1 302 ? -13.322 23.096  -10.819 1.00 77.43  ? 820  ARG   A NH1  1 
ATOM   2592 N  NH2  . ARG   A 1 302 ? -13.184 25.331  -10.325 1.00 75.06  ? 820  ARG   A NH2  1 
ATOM   2593 N  N    . ILE   A 1 303 ? -11.359 21.550  -18.388 1.00 77.34  ? 821  ILE   A N    1 
ATOM   2594 C  CA   . ILE   A 1 303 ? -11.176 20.392  -19.256 1.00 80.92  ? 821  ILE   A CA   1 
ATOM   2595 C  C    . ILE   A 1 303 ? -10.329 20.763  -20.466 1.00 82.35  ? 821  ILE   A C    1 
ATOM   2596 O  O    . ILE   A 1 303 ? -9.372  20.061  -20.813 1.00 80.59  ? 821  ILE   A O    1 
ATOM   2597 C  CB   . ILE   A 1 303 ? -12.543 19.821  -19.674 1.00 86.59  ? 821  ILE   A CB   1 
ATOM   2598 C  CG1  . ILE   A 1 303 ? -13.242 19.178  -18.475 1.00 91.07  ? 821  ILE   A CG1  1 
ATOM   2599 C  CG2  . ILE   A 1 303 ? -12.383 18.827  -20.816 1.00 86.16  ? 821  ILE   A CG2  1 
ATOM   2600 C  CD1  . ILE   A 1 303 ? -12.832 17.745  -18.221 1.00 94.20  ? 821  ILE   A CD1  1 
ATOM   2601 N  N    . ARG   A 1 304 ? -10.665 21.879  -21.123 1.00 84.45  ? 822  ARG   A N    1 
ATOM   2602 C  CA   . ARG   A 1 304 ? -9.913  22.299  -22.303 1.00 84.31  ? 822  ARG   A CA   1 
ATOM   2603 C  C    . ARG   A 1 304 ? -8.452  22.569  -21.970 1.00 79.75  ? 822  ARG   A C    1 
ATOM   2604 O  O    . ARG   A 1 304 ? -7.579  22.398  -22.829 1.00 81.72  ? 822  ARG   A O    1 
ATOM   2605 C  CB   . ARG   A 1 304 ? -10.553 23.541  -22.928 1.00 87.23  ? 822  ARG   A CB   1 
ATOM   2606 C  CG   . ARG   A 1 304 ? -12.038 23.402  -23.251 1.00 91.98  ? 822  ARG   A CG   1 
ATOM   2607 C  CD   . ARG   A 1 304 ? -12.289 22.474  -24.433 1.00 96.22  ? 822  ARG   A CD   1 
ATOM   2608 N  NE   . ARG   A 1 304 ? -13.451 21.616  -24.214 1.00 100.20 ? 822  ARG   A NE   1 
ATOM   2609 C  CZ   . ARG   A 1 304 ? -13.882 20.699  -25.075 1.00 103.90 ? 822  ARG   A CZ   1 
ATOM   2610 N  NH1  . ARG   A 1 304 ? -13.249 20.511  -26.224 1.00 106.30 ? 822  ARG   A NH1  1 
ATOM   2611 N  NH2  . ARG   A 1 304 ? -14.950 19.967  -24.785 1.00 105.44 ? 822  ARG   A NH2  1 
ATOM   2612 N  N    . LEU   A 1 305 ? -8.163  22.988  -20.736 1.00 75.35  ? 823  LEU   A N    1 
ATOM   2613 C  CA   . LEU   A 1 305 ? -6.775  23.175  -20.330 1.00 70.05  ? 823  LEU   A CA   1 
ATOM   2614 C  C    . LEU   A 1 305 ? -6.048  21.840  -20.238 1.00 73.70  ? 823  LEU   A C    1 
ATOM   2615 O  O    . LEU   A 1 305 ? -4.919  21.701  -20.723 1.00 77.32  ? 823  LEU   A O    1 
ATOM   2616 C  CB   . LEU   A 1 305 ? -6.709  23.909  -18.993 1.00 63.85  ? 823  LEU   A CB   1 
ATOM   2617 C  CG   . LEU   A 1 305 ? -5.319  23.944  -18.359 1.00 61.65  ? 823  LEU   A CG   1 
ATOM   2618 C  CD1  . LEU   A 1 305 ? -4.315  24.644  -19.265 1.00 63.81  ? 823  LEU   A CD1  1 
ATOM   2619 C  CD2  . LEU   A 1 305 ? -5.381  24.620  -17.020 1.00 59.69  ? 823  LEU   A CD2  1 
ATOM   2620 N  N    . LEU   A 1 306 ? -6.679  20.847  -19.605 1.00 73.51  ? 824  LEU   A N    1 
ATOM   2621 C  CA   . LEU   A 1 306 ? -6.067  19.526  -19.503 1.00 76.56  ? 824  LEU   A CA   1 
ATOM   2622 C  C    . LEU   A 1 306 ? -5.798  18.935  -20.880 1.00 75.42  ? 824  LEU   A C    1 
ATOM   2623 O  O    . LEU   A 1 306 ? -4.724  18.373  -21.121 1.00 73.77  ? 824  LEU   A O    1 
ATOM   2624 C  CB   . LEU   A 1 306 ? -6.963  18.596  -18.687 1.00 79.97  ? 824  LEU   A CB   1 
ATOM   2625 C  CG   . LEU   A 1 306 ? -6.595  18.413  -17.215 1.00 80.05  ? 824  LEU   A CG   1 
ATOM   2626 C  CD1  . LEU   A 1 306 ? -7.695  17.656  -16.495 1.00 81.26  ? 824  LEU   A CD1  1 
ATOM   2627 C  CD2  . LEU   A 1 306 ? -5.263  17.691  -17.084 1.00 82.10  ? 824  LEU   A CD2  1 
ATOM   2628 N  N    . GLN   A 1 307 ? -6.763  19.057  -21.798 1.00 76.44  ? 825  GLN   A N    1 
ATOM   2629 C  CA   . GLN   A 1 307 ? -6.551  18.593  -23.166 1.00 80.73  ? 825  GLN   A CA   1 
ATOM   2630 C  C    . GLN   A 1 307 ? -5.340  19.268  -23.793 1.00 80.89  ? 825  GLN   A C    1 
ATOM   2631 O  O    . GLN   A 1 307 ? -4.546  18.621  -24.487 1.00 79.67  ? 825  GLN   A O    1 
ATOM   2632 C  CB   . GLN   A 1 307 ? -7.794  18.860  -24.016 1.00 85.27  ? 825  GLN   A CB   1 
ATOM   2633 C  CG   . GLN   A 1 307 ? -9.089  18.316  -23.451 1.00 88.44  ? 825  GLN   A CG   1 
ATOM   2634 C  CD   . GLN   A 1 307 ? -10.295 18.760  -24.256 1.00 95.55  ? 825  GLN   A CD   1 
ATOM   2635 O  OE1  . GLN   A 1 307 ? -11.277 18.028  -24.385 1.00 100.35 ? 825  GLN   A OE1  1 
ATOM   2636 N  NE2  . GLN   A 1 307 ? -10.224 19.965  -24.807 1.00 96.04  ? 825  GLN   A NE2  1 
ATOM   2637 N  N    . PHE   A 1 308 ? -5.185  20.572  -23.557 1.00 81.31  ? 826  PHE   A N    1 
ATOM   2638 C  CA   . PHE   A 1 308 ? -4.075  21.316  -24.141 1.00 81.89  ? 826  PHE   A CA   1 
ATOM   2639 C  C    . PHE   A 1 308 ? -2.733  20.780  -23.657 1.00 78.76  ? 826  PHE   A C    1 
ATOM   2640 O  O    . PHE   A 1 308 ? -1.775  20.693  -24.434 1.00 80.33  ? 826  PHE   A O    1 
ATOM   2641 C  CB   . PHE   A 1 308 ? -4.230  22.801  -23.807 1.00 80.82  ? 826  PHE   A CB   1 
ATOM   2642 C  CG   . PHE   A 1 308 ? -3.045  23.644  -24.182 1.00 83.01  ? 826  PHE   A CG   1 
ATOM   2643 C  CD1  . PHE   A 1 308 ? -2.757  23.909  -25.511 1.00 86.87  ? 826  PHE   A CD1  1 
ATOM   2644 C  CD2  . PHE   A 1 308 ? -2.232  24.190  -23.203 1.00 82.51  ? 826  PHE   A CD2  1 
ATOM   2645 C  CE1  . PHE   A 1 308 ? -1.672  24.693  -25.855 1.00 90.08  ? 826  PHE   A CE1  1 
ATOM   2646 C  CE2  . PHE   A 1 308 ? -1.147  24.975  -23.540 1.00 85.27  ? 826  PHE   A CE2  1 
ATOM   2647 C  CZ   . PHE   A 1 308 ? -0.866  25.226  -24.868 1.00 88.81  ? 826  PHE   A CZ   1 
ATOM   2648 N  N    . VAL   A 1 309 ? -2.650  20.396  -22.386 1.00 76.26  ? 827  VAL   A N    1 
ATOM   2649 C  CA   . VAL   A 1 309 ? -1.395  19.910  -21.818 1.00 76.68  ? 827  VAL   A CA   1 
ATOM   2650 C  C    . VAL   A 1 309 ? -1.239  18.405  -22.008 1.00 85.70  ? 827  VAL   A C    1 
ATOM   2651 O  O    . VAL   A 1 309 ? -0.128  17.914  -22.224 1.00 91.85  ? 827  VAL   A O    1 
ATOM   2652 C  CB   . VAL   A 1 309 ? -1.307  20.304  -20.330 1.00 67.39  ? 827  VAL   A CB   1 
ATOM   2653 C  CG1  . VAL   A 1 309 ? 0.046   19.917  -19.753 1.00 65.74  ? 827  VAL   A CG1  1 
ATOM   2654 C  CG2  . VAL   A 1 309 ? -1.555  21.794  -20.162 1.00 66.14  ? 827  VAL   A CG2  1 
ATOM   2655 N  N    . THR   A 1 310 ? -2.334  17.650  -21.938 1.00 86.34  ? 828  THR   A N    1 
ATOM   2656 C  CA   . THR   A 1 310 ? -2.261  16.198  -22.055 1.00 89.67  ? 828  THR   A CA   1 
ATOM   2657 C  C    . THR   A 1 310 ? -2.353  15.724  -23.501 1.00 93.69  ? 828  THR   A C    1 
ATOM   2658 O  O    . THR   A 1 310 ? -1.600  14.833  -23.910 1.00 94.63  ? 828  THR   A O    1 
ATOM   2659 C  CB   . THR   A 1 310 ? -3.374  15.547  -21.224 1.00 88.01  ? 828  THR   A CB   1 
ATOM   2660 O  OG1  . THR   A 1 310 ? -3.075  15.682  -19.829 1.00 86.41  ? 828  THR   A OG1  1 
ATOM   2661 C  CG2  . THR   A 1 310 ? -3.518  14.069  -21.566 1.00 88.49  ? 828  THR   A CG2  1 
ATOM   2662 N  N    . GLY   A 1 311 ? -3.249  16.314  -24.288 1.00 94.54  ? 829  GLY   A N    1 
ATOM   2663 C  CA   . GLY   A 1 311 ? -3.567  15.809  -25.605 1.00 99.67  ? 829  GLY   A CA   1 
ATOM   2664 C  C    . GLY   A 1 311 ? -4.803  14.940  -25.652 1.00 104.23 ? 829  GLY   A C    1 
ATOM   2665 O  O    . GLY   A 1 311 ? -5.200  14.512  -26.743 1.00 107.56 ? 829  GLY   A O    1 
ATOM   2666 N  N    . THR   A 1 312 ? -5.413  14.656  -24.502 1.00 105.54 ? 830  THR   A N    1 
ATOM   2667 C  CA   . THR   A 1 312 ? -6.641  13.881  -24.414 1.00 109.96 ? 830  THR   A CA   1 
ATOM   2668 C  C    . THR   A 1 312 ? -7.641  14.628  -23.543 1.00 109.07 ? 830  THR   A C    1 
ATOM   2669 O  O    . THR   A 1 312 ? -7.287  15.548  -22.802 1.00 104.53 ? 830  THR   A O    1 
ATOM   2670 C  CB   . THR   A 1 312 ? -6.397  12.477  -23.835 1.00 109.94 ? 830  THR   A CB   1 
ATOM   2671 O  OG1  . THR   A 1 312 ? -6.283  12.561  -22.409 1.00 105.04 ? 830  THR   A OG1  1 
ATOM   2672 C  CG2  . THR   A 1 312 ? -5.125  11.865  -24.407 1.00 113.03 ? 830  THR   A CG2  1 
ATOM   2673 N  N    . SER   A 1 313 ? -8.904  14.210  -23.628 1.00 112.07 ? 831  SER   A N    1 
ATOM   2674 C  CA   . SER   A 1 313 ? -9.978  14.894  -22.919 1.00 107.36 ? 831  SER   A CA   1 
ATOM   2675 C  C    . SER   A 1 313 ? -10.251 14.318  -21.536 1.00 110.67 ? 831  SER   A C    1 
ATOM   2676 O  O    . SER   A 1 313 ? -10.725 15.045  -20.655 1.00 109.61 ? 831  SER   A O    1 
ATOM   2677 C  CB   . SER   A 1 313 ? -11.267 14.849  -23.745 1.00 102.75 ? 831  SER   A CB   1 
ATOM   2678 O  OG   . SER   A 1 313 ? -11.103 14.049  -24.903 1.00 102.43 ? 831  SER   A OG   1 
ATOM   2679 N  N    . ARG   A 1 314 ? -9.958  13.041  -21.321 1.00 113.27 ? 832  ARG   A N    1 
ATOM   2680 C  CA   . ARG   A 1 314 ? -10.370 12.349  -20.110 1.00 113.23 ? 832  ARG   A CA   1 
ATOM   2681 C  C    . ARG   A 1 314 ? -9.355  12.529  -18.986 1.00 111.91 ? 832  ARG   A C    1 
ATOM   2682 O  O    . ARG   A 1 314 ? -8.175  12.807  -19.212 1.00 112.74 ? 832  ARG   A O    1 
ATOM   2683 C  CB   . ARG   A 1 314 ? -10.571 10.859  -20.391 1.00 117.22 ? 832  ARG   A CB   1 
ATOM   2684 N  N    . VAL   A 1 315 ? -9.840  12.369  -17.758 1.00 110.37 ? 833  VAL   A N    1 
ATOM   2685 C  CA   . VAL   A 1 315 ? -8.974  12.295  -16.585 1.00 107.63 ? 833  VAL   A CA   1 
ATOM   2686 C  C    . VAL   A 1 315 ? -8.758  10.817  -16.281 1.00 114.62 ? 833  VAL   A C    1 
ATOM   2687 O  O    . VAL   A 1 315 ? -9.687  10.009  -16.436 1.00 120.42 ? 833  VAL   A O    1 
ATOM   2688 C  CB   . VAL   A 1 315 ? -9.566  13.066  -15.390 1.00 102.36 ? 833  VAL   A CB   1 
ATOM   2689 C  CG1  . VAL   A 1 315 ? -10.127 14.404  -15.848 1.00 96.38  ? 833  VAL   A CG1  1 
ATOM   2690 C  CG2  . VAL   A 1 315 ? -10.644 12.257  -14.676 1.00 107.38 ? 833  VAL   A CG2  1 
ATOM   2691 N  N    . PRO   A 1 316 ? -7.553  10.405  -15.899 1.00 114.75 ? 834  PRO   A N    1 
ATOM   2692 C  CA   . PRO   A 1 316 ? -7.317  8.982   -15.637 1.00 119.01 ? 834  PRO   A CA   1 
ATOM   2693 C  C    . PRO   A 1 316 ? -8.000  8.531   -14.357 1.00 119.48 ? 834  PRO   A C    1 
ATOM   2694 O  O    . PRO   A 1 316 ? -8.190  9.308   -13.418 1.00 115.45 ? 834  PRO   A O    1 
ATOM   2695 C  CB   . PRO   A 1 316 ? -5.791  8.889   -15.519 1.00 118.29 ? 834  PRO   A CB   1 
ATOM   2696 C  CG   . PRO   A 1 316 ? -5.360  10.262  -15.131 1.00 112.78 ? 834  PRO   A CG   1 
ATOM   2697 C  CD   . PRO   A 1 316 ? -6.319  11.204  -15.796 1.00 110.32 ? 834  PRO   A CD   1 
ATOM   2698 N  N    . MET   A 1 317 ? -8.379  7.255   -14.337 1.00 124.75 ? 835  MET   A N    1 
ATOM   2699 C  CA   . MET   A 1 317 ? -9.027  6.684   -13.164 1.00 126.89 ? 835  MET   A CA   1 
ATOM   2700 C  C    . MET   A 1 317 ? -8.119  6.802   -11.946 1.00 123.86 ? 835  MET   A C    1 
ATOM   2701 O  O    . MET   A 1 317 ? -6.891  6.863   -12.061 1.00 124.56 ? 835  MET   A O    1 
ATOM   2702 C  CB   . MET   A 1 317 ? -9.389  5.218   -13.411 1.00 133.96 ? 835  MET   A CB   1 
ATOM   2703 C  CG   . MET   A 1 317 ? -10.153 4.967   -14.703 1.00 137.25 ? 835  MET   A CG   1 
ATOM   2704 S  SD   . MET   A 1 317 ? -11.901 5.400   -14.597 1.00 138.44 ? 835  MET   A SD   1 
ATOM   2705 C  CE   . MET   A 1 317 ? -12.504 4.130   -13.487 1.00 142.32 ? 835  MET   A CE   1 
ATOM   2706 N  N    . ASN   A 1 318 ? -8.742  6.849   -10.768 1.00 120.35 ? 836  ASN   A N    1 
ATOM   2707 C  CA   . ASN   A 1 318 ? -8.104  7.003   -9.464  1.00 117.71 ? 836  ASN   A CA   1 
ATOM   2708 C  C    . ASN   A 1 318 ? -7.456  8.371   -9.278  1.00 109.36 ? 836  ASN   A C    1 
ATOM   2709 O  O    . ASN   A 1 318 ? -6.806  8.596   -8.250  1.00 107.64 ? 836  ASN   A O    1 
ATOM   2710 C  CB   . ASN   A 1 318 ? -7.056  5.913   -9.190  1.00 122.21 ? 836  ASN   A CB   1 
ATOM   2711 C  CG   . ASN   A 1 318 ? -7.596  4.517   -9.428  1.00 130.87 ? 836  ASN   A CG   1 
ATOM   2712 O  OD1  . ASN   A 1 318 ? -8.665  4.161   -8.934  1.00 134.30 ? 836  ASN   A OD1  1 
ATOM   2713 N  ND2  . ASN   A 1 318 ? -6.860  3.721   -10.195 1.00 134.66 ? 836  ASN   A ND2  1 
ATOM   2714 N  N    . GLY   A 1 319 ? -7.606  9.287   -10.224 1.00 103.49 ? 837  GLY   A N    1 
ATOM   2715 C  CA   . GLY   A 1 319 ? -7.122  10.640  -10.073 1.00 97.02  ? 837  GLY   A CA   1 
ATOM   2716 C  C    . GLY   A 1 319 ? -5.930  10.948  -10.958 1.00 91.07  ? 837  GLY   A C    1 
ATOM   2717 O  O    . GLY   A 1 319 ? -5.617  10.237  -11.916 1.00 88.36  ? 837  GLY   A O    1 
ATOM   2718 N  N    . PHE   A 1 320 ? -5.250  12.041  -10.615 1.00 89.51  ? 838  PHE   A N    1 
ATOM   2719 C  CA   . PHE   A 1 320 ? -4.121  12.539  -11.390 1.00 87.92  ? 838  PHE   A CA   1 
ATOM   2720 C  C    . PHE   A 1 320 ? -2.809  11.838  -11.062 1.00 89.18  ? 838  PHE   A C    1 
ATOM   2721 O  O    . PHE   A 1 320 ? -1.802  12.109  -11.724 1.00 88.19  ? 838  PHE   A O    1 
ATOM   2722 C  CB   . PHE   A 1 320 ? -3.966  14.046  -11.171 1.00 84.66  ? 838  PHE   A CB   1 
ATOM   2723 C  CG   . PHE   A 1 320 ? -4.940  14.873  -11.955 1.00 86.87  ? 838  PHE   A CG   1 
ATOM   2724 C  CD1  . PHE   A 1 320 ? -4.594  15.386  -13.194 1.00 88.48  ? 838  PHE   A CD1  1 
ATOM   2725 C  CD2  . PHE   A 1 320 ? -6.205  15.134  -11.456 1.00 86.88  ? 838  PHE   A CD2  1 
ATOM   2726 C  CE1  . PHE   A 1 320 ? -5.490  16.146  -13.918 1.00 87.61  ? 838  PHE   A CE1  1 
ATOM   2727 C  CE2  . PHE   A 1 320 ? -7.106  15.893  -12.176 1.00 86.83  ? 838  PHE   A CE2  1 
ATOM   2728 C  CZ   . PHE   A 1 320 ? -6.747  16.400  -13.407 1.00 87.44  ? 838  PHE   A CZ   1 
ATOM   2729 N  N    . ALA   A 1 321 ? -2.790  10.952  -10.064 1.00 91.70  ? 839  ALA   A N    1 
ATOM   2730 C  CA   . ALA   A 1 321 ? -1.567  10.238  -9.722  1.00 91.58  ? 839  ALA   A CA   1 
ATOM   2731 C  C    . ALA   A 1 321 ? -1.228  9.139   -10.720 1.00 97.13  ? 839  ALA   A C    1 
ATOM   2732 O  O    . ALA   A 1 321 ? -0.066  8.723   -10.790 1.00 102.78 ? 839  ALA   A O    1 
ATOM   2733 C  CB   . ALA   A 1 321 ? -1.678  9.642   -8.317  1.00 91.28  ? 839  ALA   A CB   1 
ATOM   2734 N  N    . GLU   A 1 322 ? -2.209  8.658   -11.485 1.00 97.60  ? 840  GLU   A N    1 
ATOM   2735 C  CA   . GLU   A 1 322 ? -1.992  7.633   -12.497 1.00 101.44 ? 840  GLU   A CA   1 
ATOM   2736 C  C    . GLU   A 1 322 ? -2.003  8.205   -13.906 1.00 96.45  ? 840  GLU   A C    1 
ATOM   2737 O  O    . GLU   A 1 322 ? -2.282  7.480   -14.867 1.00 103.14 ? 840  GLU   A O    1 
ATOM   2738 C  CB   . GLU   A 1 322 ? -3.044  6.531   -12.371 1.00 110.62 ? 840  GLU   A CB   1 
ATOM   2739 C  CG   . GLU   A 1 322 ? -2.653  5.420   -11.418 1.00 119.24 ? 840  GLU   A CG   1 
ATOM   2740 C  CD   . GLU   A 1 322 ? -2.657  5.873   -9.973  1.00 120.45 ? 840  GLU   A CD   1 
ATOM   2741 O  OE1  . GLU   A 1 322 ? -1.587  6.276   -9.471  1.00 119.07 ? 840  GLU   A OE1  1 
ATOM   2742 O  OE2  . GLU   A 1 322 ? -3.733  5.831   -9.342  1.00 122.26 ? 840  GLU   A OE2  1 
ATOM   2743 N  N    . LEU   A 1 323 ? -1.709  9.490   -14.044 1.00 86.82  ? 841  LEU   A N    1 
ATOM   2744 C  CA   . LEU   A 1 323 ? -1.730  10.130  -15.347 1.00 83.81  ? 841  LEU   A CA   1 
ATOM   2745 C  C    . LEU   A 1 323 ? -0.554  9.622   -16.181 1.00 87.58  ? 841  LEU   A C    1 
ATOM   2746 O  O    . LEU   A 1 323 ? 0.547   9.412   -15.665 1.00 83.74  ? 841  LEU   A O    1 
ATOM   2747 C  CB   . LEU   A 1 323 ? -1.692  11.648  -15.151 1.00 78.24  ? 841  LEU   A CB   1 
ATOM   2748 C  CG   . LEU   A 1 323 ? -1.956  12.614  -16.302 1.00 76.92  ? 841  LEU   A CG   1 
ATOM   2749 C  CD1  . LEU   A 1 323 ? -2.286  14.013  -15.794 1.00 69.69  ? 841  LEU   A CD1  1 
ATOM   2750 C  CD2  . LEU   A 1 323 ? -0.764  12.670  -17.146 1.00 79.70  ? 841  LEU   A CD2  1 
ATOM   2751 N  N    . TYR   A 1 324 ? -0.798  9.399   -17.474 1.00 94.43  ? 842  TYR   A N    1 
ATOM   2752 C  CA   . TYR   A 1 324 ? 0.193   8.826   -18.377 1.00 96.80  ? 842  TYR   A CA   1 
ATOM   2753 C  C    . TYR   A 1 324 ? 0.519   9.793   -19.508 1.00 98.88  ? 842  TYR   A C    1 
ATOM   2754 O  O    . TYR   A 1 324 ? -0.323  10.589  -19.932 1.00 95.21  ? 842  TYR   A O    1 
ATOM   2755 C  CB   . TYR   A 1 324 ? -0.296  7.499   -18.977 1.00 95.28  ? 842  TYR   A CB   1 
ATOM   2756 C  CG   . TYR   A 1 324 ? 0.260   6.269   -18.299 1.00 98.21  ? 842  TYR   A CG   1 
ATOM   2757 C  CD1  . TYR   A 1 324 ? 0.232   6.142   -16.917 1.00 94.97  ? 842  TYR   A CD1  1 
ATOM   2758 C  CD2  . TYR   A 1 324 ? 0.808   5.231   -19.042 1.00 101.94 ? 842  TYR   A CD2  1 
ATOM   2759 C  CE1  . TYR   A 1 324 ? 0.736   5.019   -16.293 1.00 95.75  ? 842  TYR   A CE1  1 
ATOM   2760 C  CE2  . TYR   A 1 324 ? 1.316   4.104   -18.427 1.00 104.82 ? 842  TYR   A CE2  1 
ATOM   2761 C  CZ   . TYR   A 1 324 ? 1.277   4.003   -17.053 1.00 102.20 ? 842  TYR   A CZ   1 
ATOM   2762 O  OH   . TYR   A 1 324 ? 1.782   2.882   -16.434 1.00 104.97 ? 842  TYR   A OH   1 
ATOM   2763 N  N    . GLY   A 1 325 ? 1.754   9.707   -20.000 1.00 104.48 ? 843  GLY   A N    1 
ATOM   2764 C  CA   . GLY   A 1 325 ? 2.173   10.479  -21.153 1.00 105.50 ? 843  GLY   A CA   1 
ATOM   2765 C  C    . GLY   A 1 325 ? 2.270   9.628   -22.403 1.00 111.43 ? 843  GLY   A C    1 
ATOM   2766 O  O    . GLY   A 1 325 ? 1.318   8.924   -22.753 1.00 114.65 ? 843  GLY   A O    1 
ATOM   2767 N  N    . SER   A 1 326 ? 3.416   9.677   -23.085 1.00 112.50 ? 844  SER   A N    1 
ATOM   2768 C  CA   . SER   A 1 326 ? 3.638   8.863   -24.271 1.00 118.05 ? 844  SER   A CA   1 
ATOM   2769 C  C    . SER   A 1 326 ? 4.735   7.822   -24.103 1.00 124.03 ? 844  SER   A C    1 
ATOM   2770 O  O    . SER   A 1 326 ? 4.810   6.897   -24.917 1.00 131.12 ? 844  SER   A O    1 
ATOM   2771 C  CB   . SER   A 1 326 ? 3.980   9.750   -25.477 1.00 118.62 ? 844  SER   A CB   1 
ATOM   2772 O  OG   . SER   A 1 326 ? 4.167   8.975   -26.648 1.00 125.83 ? 844  SER   A OG   1 
ATOM   2773 N  N    . ASN   A 1 327 ? 5.577   7.946   -23.081 1.00 122.67 ? 845  ASN   A N    1 
ATOM   2774 C  CA   . ASN   A 1 327 ? 6.655   6.999   -22.821 1.00 128.03 ? 845  ASN   A CA   1 
ATOM   2775 C  C    . ASN   A 1 327 ? 6.581   6.478   -21.393 1.00 123.81 ? 845  ASN   A C    1 
ATOM   2776 O  O    . ASN   A 1 327 ? 7.602   6.276   -20.730 1.00 126.72 ? 845  ASN   A O    1 
ATOM   2777 C  CB   . ASN   A 1 327 ? 8.018   7.632   -23.095 1.00 130.49 ? 845  ASN   A CB   1 
ATOM   2778 C  CG   . ASN   A 1 327 ? 8.278   7.842   -24.574 1.00 134.75 ? 845  ASN   A CG   1 
ATOM   2779 O  OD1  . ASN   A 1 327 ? 7.789   7.088   -25.416 1.00 139.53 ? 845  ASN   A OD1  1 
ATOM   2780 N  ND2  . ASN   A 1 327 ? 9.052   8.872   -24.899 1.00 133.50 ? 845  ASN   A ND2  1 
ATOM   2781 N  N    . GLY   A 1 328 ? 5.367   6.254   -20.896 1.00 115.10 ? 846  GLY   A N    1 
ATOM   2782 C  CA   . GLY   A 1 328 ? 5.176   5.735   -19.563 1.00 109.45 ? 846  GLY   A CA   1 
ATOM   2783 C  C    . GLY   A 1 328 ? 4.494   6.723   -18.639 1.00 100.96 ? 846  GLY   A C    1 
ATOM   2784 O  O    . GLY   A 1 328 ? 3.950   7.744   -19.073 1.00 100.47 ? 846  GLY   A O    1 
ATOM   2785 N  N    . PRO   A 1 329 ? 4.506   6.432   -17.341 1.00 94.60  ? 847  PRO   A N    1 
ATOM   2786 C  CA   . PRO   A 1 329 ? 3.836   7.316   -16.382 1.00 88.07  ? 847  PRO   A CA   1 
ATOM   2787 C  C    . PRO   A 1 329 ? 4.513   8.673   -16.275 1.00 85.78  ? 847  PRO   A C    1 
ATOM   2788 O  O    . PRO   A 1 329 ? 5.739   8.797   -16.350 1.00 87.98  ? 847  PRO   A O    1 
ATOM   2789 C  CB   . PRO   A 1 329 ? 3.930   6.546   -15.058 1.00 89.55  ? 847  PRO   A CB   1 
ATOM   2790 C  CG   . PRO   A 1 329 ? 4.194   5.133   -15.449 1.00 96.03  ? 847  PRO   A CG   1 
ATOM   2791 C  CD   . PRO   A 1 329 ? 4.993   5.195   -16.710 1.00 99.86  ? 847  PRO   A CD   1 
ATOM   2792 N  N    . GLN   A 1 330 ? 3.682   9.698   -16.091 1.00 83.38  ? 848  GLN   A N    1 
ATOM   2793 C  CA   . GLN   A 1 330 ? 4.145   11.070  -15.931 1.00 80.16  ? 848  GLN   A CA   1 
ATOM   2794 C  C    . GLN   A 1 330 ? 3.071   11.952  -15.318 1.00 75.91  ? 848  GLN   A C    1 
ATOM   2795 O  O    . GLN   A 1 330 ? 1.989   12.100  -15.891 1.00 75.13  ? 848  GLN   A O    1 
ATOM   2796 C  CB   . GLN   A 1 330 ? 4.574   11.671  -17.268 1.00 82.30  ? 848  GLN   A CB   1 
ATOM   2797 C  CG   . GLN   A 1 330 ? 5.139   13.058  -17.100 1.00 85.20  ? 848  GLN   A CG   1 
ATOM   2798 C  CD   . GLN   A 1 330 ? 6.036   13.141  -15.895 1.00 90.41  ? 848  GLN   A CD   1 
ATOM   2799 O  OE1  . GLN   A 1 330 ? 5.648   13.655  -14.841 1.00 87.46  ? 848  GLN   A OE1  1 
ATOM   2800 N  NE2  . GLN   A 1 330 ? 7.242   12.615  -16.034 1.00 97.09  ? 848  GLN   A NE2  1 
ATOM   2801 N  N    . SER   A 1 331 ? 3.363   12.570  -14.180 1.00 75.93  ? 849  SER   A N    1 
ATOM   2802 C  CA   . SER   A 1 331 ? 2.386   13.468  -13.591 1.00 73.82  ? 849  SER   A CA   1 
ATOM   2803 C  C    . SER   A 1 331 ? 2.347   14.798  -14.344 1.00 72.17  ? 849  SER   A C    1 
ATOM   2804 O  O    . SER   A 1 331 ? 3.202   15.113  -15.180 1.00 76.28  ? 849  SER   A O    1 
ATOM   2805 C  CB   . SER   A 1 331 ? 2.687   13.704  -12.110 1.00 75.11  ? 849  SER   A CB   1 
ATOM   2806 O  OG   . SER   A 1 331 ? 3.717   12.848  -11.654 1.00 85.34  ? 849  SER   A OG   1 
ATOM   2807 N  N    . PHE   A 1 332 ? 1.322   15.578  -14.025 1.00 64.12  ? 850  PHE   A N    1 
ATOM   2808 C  CA   . PHE   A 1 332 ? 1.148   16.910  -14.584 1.00 57.92  ? 850  PHE   A CA   1 
ATOM   2809 C  C    . PHE   A 1 332 ? 2.292   17.814  -14.125 1.00 58.12  ? 850  PHE   A C    1 
ATOM   2810 O  O    . PHE   A 1 332 ? 2.642   17.830  -12.943 1.00 60.51  ? 850  PHE   A O    1 
ATOM   2811 C  CB   . PHE   A 1 332 ? -0.214  17.444  -14.139 1.00 57.77  ? 850  PHE   A CB   1 
ATOM   2812 C  CG   . PHE   A 1 332 ? -0.476  18.861  -14.520 1.00 65.82  ? 850  PHE   A CG   1 
ATOM   2813 C  CD1  . PHE   A 1 332 ? -0.902  19.182  -15.793 1.00 71.17  ? 850  PHE   A CD1  1 
ATOM   2814 C  CD2  . PHE   A 1 332 ? -0.332  19.871  -13.595 1.00 68.48  ? 850  PHE   A CD2  1 
ATOM   2815 C  CE1  . PHE   A 1 332 ? -1.158  20.487  -16.139 1.00 72.50  ? 850  PHE   A CE1  1 
ATOM   2816 C  CE2  . PHE   A 1 332 ? -0.582  21.180  -13.931 1.00 71.85  ? 850  PHE   A CE2  1 
ATOM   2817 C  CZ   . PHE   A 1 332 ? -0.998  21.489  -15.207 1.00 72.05  ? 850  PHE   A CZ   1 
ATOM   2818 N  N    . THR   A 1 333 ? 2.897   18.550  -15.061 1.00 58.56  ? 851  THR   A N    1 
ATOM   2819 C  CA   . THR   A 1 333 ? 4.147   19.266  -14.806 1.00 60.68  ? 851  THR   A CA   1 
ATOM   2820 C  C    . THR   A 1 333 ? 4.088   20.682  -15.373 1.00 59.23  ? 851  THR   A C    1 
ATOM   2821 O  O    . THR   A 1 333 ? 3.684   20.873  -16.523 1.00 60.84  ? 851  THR   A O    1 
ATOM   2822 C  CB   . THR   A 1 333 ? 5.336   18.503  -15.414 1.00 67.36  ? 851  THR   A CB   1 
ATOM   2823 O  OG1  . THR   A 1 333 ? 5.608   17.333  -14.634 1.00 76.43  ? 851  THR   A OG1  1 
ATOM   2824 C  CG2  . THR   A 1 333 ? 6.575   19.367  -15.446 1.00 69.48  ? 851  THR   A CG2  1 
ATOM   2825 N  N    . VAL   A 1 334 ? 4.496   21.669  -14.574 1.00 58.24  ? 852  VAL   A N    1 
ATOM   2826 C  CA   . VAL   A 1 334 ? 4.595   23.065  -15.009 1.00 59.82  ? 852  VAL   A CA   1 
ATOM   2827 C  C    . VAL   A 1 334 ? 6.056   23.484  -14.962 1.00 62.56  ? 852  VAL   A C    1 
ATOM   2828 O  O    . VAL   A 1 334 ? 6.692   23.433  -13.902 1.00 63.07  ? 852  VAL   A O    1 
ATOM   2829 C  CB   . VAL   A 1 334 ? 3.745   24.003  -14.137 1.00 58.99  ? 852  VAL   A CB   1 
ATOM   2830 C  CG1  . VAL   A 1 334 ? 3.879   25.441  -14.616 1.00 57.97  ? 852  VAL   A CG1  1 
ATOM   2831 C  CG2  . VAL   A 1 334 ? 2.288   23.561  -14.141 1.00 55.18  ? 852  VAL   A CG2  1 
ATOM   2832 N  N    . GLU   A 1 335 ? 6.577   23.920  -16.103 1.00 68.12  ? 853  GLU   A N    1 
ATOM   2833 C  CA   . GLU   A 1 335 ? 7.963   24.339  -16.228 1.00 75.03  ? 853  GLU   A CA   1 
ATOM   2834 C  C    . GLU   A 1 335 ? 8.082   25.810  -16.586 1.00 75.40  ? 853  GLU   A C    1 
ATOM   2835 O  O    . GLU   A 1 335 ? 7.364   26.313  -17.459 1.00 74.89  ? 853  GLU   A O    1 
ATOM   2836 C  CB   . GLU   A 1 335 ? 8.707   23.526  -17.277 1.00 78.17  ? 853  GLU   A CB   1 
ATOM   2837 C  CG   . GLU   A 1 335 ? 10.191  23.706  -17.164 1.00 85.82  ? 853  GLU   A CG   1 
ATOM   2838 C  CD   . GLU   A 1 335 ? 10.944  23.183  -18.350 1.00 93.97  ? 853  GLU   A CD   1 
ATOM   2839 O  OE1  . GLU   A 1 335 ? 10.371  23.146  -19.458 1.00 97.46  ? 853  GLU   A OE1  1 
ATOM   2840 O  OE2  . GLU   A 1 335 ? 12.108  22.771  -18.160 1.00 96.89  ? 853  GLU   A OE2  1 
ATOM   2841 N  N    . GLN   A 1 336 ? 9.016   26.478  -15.906 1.00 78.23  ? 854  GLN   A N    1 
ATOM   2842 C  CA   . GLN   A 1 336 ? 9.460   27.807  -16.301 1.00 81.28  ? 854  GLN   A CA   1 
ATOM   2843 C  C    . GLN   A 1 336 ? 10.038  27.757  -17.698 1.00 83.28  ? 854  GLN   A C    1 
ATOM   2844 O  O    . GLN   A 1 336 ? 11.120  27.201  -17.910 1.00 90.82  ? 854  GLN   A O    1 
ATOM   2845 C  CB   . GLN   A 1 336 ? 10.533  28.326  -15.353 1.00 89.79  ? 854  GLN   A CB   1 
ATOM   2846 C  CG   . GLN   A 1 336 ? 10.047  28.919  -14.090 1.00 98.45  ? 854  GLN   A CG   1 
ATOM   2847 C  CD   . GLN   A 1 336 ? 10.969  30.003  -13.603 1.00 113.60 ? 854  GLN   A CD   1 
ATOM   2848 O  OE1  . GLN   A 1 336 ? 11.246  30.963  -14.322 1.00 130.43 ? 854  GLN   A OE1  1 
ATOM   2849 N  NE2  . GLN   A 1 336 ? 11.489  29.839  -12.394 1.00 107.73 ? 854  GLN   A NE2  1 
ATOM   2850 N  N    . TRP   A 1 337 ? 9.348   28.350  -18.654 1.00 79.64  ? 855  TRP   A N    1 
ATOM   2851 C  CA   . TRP   A 1 337 ? 9.957   28.425  -19.970 1.00 86.31  ? 855  TRP   A CA   1 
ATOM   2852 C  C    . TRP   A 1 337 ? 9.599   29.752  -20.610 1.00 90.41  ? 855  TRP   A C    1 
ATOM   2853 O  O    . TRP   A 1 337 ? 8.427   30.143  -20.635 1.00 88.65  ? 855  TRP   A O    1 
ATOM   2854 C  CB   . TRP   A 1 337 ? 9.520   27.258  -20.849 1.00 88.79  ? 855  TRP   A CB   1 
ATOM   2855 C  CG   . TRP   A 1 337 ? 9.723   27.530  -22.274 1.00 96.23  ? 855  TRP   A CG   1 
ATOM   2856 C  CD1  . TRP   A 1 337 ? 10.865  27.345  -22.996 1.00 100.96 ? 855  TRP   A CD1  1 
ATOM   2857 C  CD2  . TRP   A 1 337 ? 8.765   28.086  -23.163 1.00 98.76  ? 855  TRP   A CD2  1 
ATOM   2858 N  NE1  . TRP   A 1 337 ? 10.664  27.733  -24.297 1.00 105.09 ? 855  TRP   A NE1  1 
ATOM   2859 C  CE2  . TRP   A 1 337 ? 9.380   28.197  -24.422 1.00 102.99 ? 855  TRP   A CE2  1 
ATOM   2860 C  CE3  . TRP   A 1 337 ? 7.438   28.499  -23.017 1.00 96.04  ? 855  TRP   A CE3  1 
ATOM   2861 C  CZ2  . TRP   A 1 337 ? 8.712   28.698  -25.526 1.00 103.27 ? 855  TRP   A CZ2  1 
ATOM   2862 C  CZ3  . TRP   A 1 337 ? 6.780   28.993  -24.106 1.00 95.69  ? 855  TRP   A CZ3  1 
ATOM   2863 C  CH2  . TRP   A 1 337 ? 7.413   29.089  -25.346 1.00 99.30  ? 855  TRP   A CH2  1 
ATOM   2864 N  N    . GLY   A 1 338 ? 10.613  30.440  -21.091 1.00 94.17  ? 856  GLY   A N    1 
ATOM   2865 C  CA   . GLY   A 1 338 ? 10.400  31.599  -21.908 1.00 99.63  ? 856  GLY   A CA   1 
ATOM   2866 C  C    . GLY   A 1 338 ? 10.320  32.890  -21.133 1.00 102.59 ? 856  GLY   A C    1 
ATOM   2867 O  O    . GLY   A 1 338 ? 10.725  33.028  -19.972 1.00 102.32 ? 856  GLY   A O    1 
ATOM   2868 N  N    . THR   A 1 339 ? 9.761   33.862  -21.833 1.00 105.66 ? 857  THR   A N    1 
ATOM   2869 C  CA   . THR   A 1 339 ? 9.681   35.267  -21.517 1.00 108.00 ? 857  THR   A CA   1 
ATOM   2870 C  C    . THR   A 1 339 ? 8.222   35.683  -21.396 1.00 107.39 ? 857  THR   A C    1 
ATOM   2871 O  O    . THR   A 1 339 ? 7.352   35.099  -22.055 1.00 102.79 ? 857  THR   A O    1 
ATOM   2872 C  CB   . THR   A 1 339 ? 10.373  36.093  -22.609 1.00 113.01 ? 857  THR   A CB   1 
ATOM   2873 O  OG1  . THR   A 1 339 ? 10.039  37.479  -22.475 1.00 115.88 ? 857  THR   A OG1  1 
ATOM   2874 C  CG2  . THR   A 1 339 ? 9.940   35.608  -23.993 1.00 113.43 ? 857  THR   A CG2  1 
ATOM   2875 N  N    . PRO   A 1 340 ? 7.924   36.682  -20.560 1.00 112.54 ? 858  PRO   A N    1 
ATOM   2876 C  CA   . PRO   A 1 340 ? 6.529   37.111  -20.364 1.00 109.97 ? 858  PRO   A CA   1 
ATOM   2877 C  C    . PRO   A 1 340 ? 5.753   37.432  -21.631 1.00 109.38 ? 858  PRO   A C    1 
ATOM   2878 O  O    . PRO   A 1 340 ? 4.516   37.381  -21.610 1.00 106.13 ? 858  PRO   A O    1 
ATOM   2879 C  CB   . PRO   A 1 340 ? 6.701   38.359  -19.487 1.00 114.22 ? 858  PRO   A CB   1 
ATOM   2880 C  CG   . PRO   A 1 340 ? 7.871   37.996  -18.649 1.00 114.93 ? 858  PRO   A CG   1 
ATOM   2881 C  CD   . PRO   A 1 340 ? 8.828   37.334  -19.596 1.00 116.45 ? 858  PRO   A CD   1 
ATOM   2882 N  N    . GLU   A 1 341 ? 6.415   37.773  -22.734 1.00 113.03 ? 859  GLU   A N    1 
ATOM   2883 C  CA   . GLU   A 1 341 ? 5.647   38.156  -23.914 1.00 116.09 ? 859  GLU   A CA   1 
ATOM   2884 C  C    . GLU   A 1 341 ? 5.088   36.943  -24.641 1.00 112.54 ? 859  GLU   A C    1 
ATOM   2885 O  O    . GLU   A 1 341 ? 4.192   37.087  -25.477 1.00 115.46 ? 859  GLU   A O    1 
ATOM   2886 C  CB   . GLU   A 1 341 ? 6.484   39.033  -24.853 1.00 125.83 ? 859  GLU   A CB   1 
ATOM   2887 C  CG   . GLU   A 1 341 ? 7.087   40.273  -24.184 1.00 135.70 ? 859  GLU   A CG   1 
ATOM   2888 C  CD   . GLU   A 1 341 ? 8.330   39.978  -23.370 1.00 139.59 ? 859  GLU   A CD   1 
ATOM   2889 O  OE1  . GLU   A 1 341 ? 8.391   40.396  -22.194 1.00 140.33 ? 859  GLU   A OE1  1 
ATOM   2890 O  OE2  . GLU   A 1 341 ? 9.253   39.339  -23.915 1.00 142.15 ? 859  GLU   A OE2  1 
ATOM   2891 N  N    . LYS   A 1 342 ? 5.566   35.747  -24.330 1.00 106.59 ? 860  LYS   A N    1 
ATOM   2892 C  CA   . LYS   A 1 342 ? 5.001   34.594  -25.008 1.00 100.11 ? 860  LYS   A CA   1 
ATOM   2893 C  C    . LYS   A 1 342 ? 3.904   33.928  -24.185 1.00 88.60  ? 860  LYS   A C    1 
ATOM   2894 O  O    . LYS   A 1 342 ? 3.856   34.014  -22.954 1.00 82.17  ? 860  LYS   A O    1 
ATOM   2895 C  CB   . LYS   A 1 342 ? 6.078   33.574  -25.374 1.00 102.71 ? 860  LYS   A CB   1 
ATOM   2896 C  CG   . LYS   A 1 342 ? 5.529   32.552  -26.342 1.00 104.29 ? 860  LYS   A CG   1 
ATOM   2897 C  CD   . LYS   A 1 342 ? 6.155   32.712  -27.698 1.00 111.22 ? 860  LYS   A CD   1 
ATOM   2898 C  CE   . LYS   A 1 342 ? 5.247   32.144  -28.809 1.00 110.18 ? 860  LYS   A CE   1 
ATOM   2899 N  NZ   . LYS   A 1 342 ? 3.850   32.662  -28.827 1.00 107.24 ? 860  LYS   A NZ   1 
ATOM   2900 N  N    . LEU   A 1 343 ? 3.017   33.278  -24.903 1.00 87.23  ? 861  LEU   A N    1 
ATOM   2901 C  CA   . LEU   A 1 343 ? 1.941   32.394  -24.516 1.00 83.77  ? 861  LEU   A CA   1 
ATOM   2902 C  C    . LEU   A 1 343 ? 2.508   31.051  -24.099 1.00 83.26  ? 861  LEU   A C    1 
ATOM   2903 O  O    . LEU   A 1 343 ? 3.571   30.638  -24.577 1.00 85.68  ? 861  LEU   A O    1 
ATOM   2904 C  CB   . LEU   A 1 343 ? 0.988   32.215  -25.690 1.00 87.22  ? 861  LEU   A CB   1 
ATOM   2905 C  CG   . LEU   A 1 343 ? 0.355   33.551  -26.064 1.00 93.20  ? 861  LEU   A CG   1 
ATOM   2906 C  CD1  . LEU   A 1 343 ? -0.743  33.411  -27.095 1.00 91.97  ? 861  LEU   A CD1  1 
ATOM   2907 C  CD2  . LEU   A 1 343 ? -0.162  34.211  -24.842 1.00 93.91  ? 861  LEU   A CD2  1 
ATOM   2908 N  N    . PRO   A 1 344 ? 1.831   30.343  -23.202 1.00 83.25  ? 862  PRO   A N    1 
ATOM   2909 C  CA   . PRO   A 1 344 ? 2.327   29.028  -22.792 1.00 84.60  ? 862  PRO   A CA   1 
ATOM   2910 C  C    . PRO   A 1 344 ? 2.252   28.040  -23.944 1.00 86.85  ? 862  PRO   A C    1 
ATOM   2911 O  O    . PRO   A 1 344 ? 1.329   28.073  -24.760 1.00 87.53  ? 862  PRO   A O    1 
ATOM   2912 C  CB   . PRO   A 1 344 ? 1.380   28.630  -21.653 1.00 81.37  ? 862  PRO   A CB   1 
ATOM   2913 C  CG   . PRO   A 1 344 ? 0.660   29.905  -21.274 1.00 81.90  ? 862  PRO   A CG   1 
ATOM   2914 C  CD   . PRO   A 1 344 ? 0.562   30.674  -22.541 1.00 83.89  ? 862  PRO   A CD   1 
ATOM   2915 N  N    . ARG   A 1 345 ? 3.245   27.165  -24.009 1.00 88.56  ? 863  ARG   A N    1 
ATOM   2916 C  CA   . ARG   A 1 345 ? 3.214   26.011  -24.888 1.00 88.21  ? 863  ARG   A CA   1 
ATOM   2917 C  C    . ARG   A 1 345 ? 3.165   24.752  -24.035 1.00 87.61  ? 863  ARG   A C    1 
ATOM   2918 O  O    . ARG   A 1 345 ? 3.650   24.732  -22.900 1.00 85.28  ? 863  ARG   A O    1 
ATOM   2919 C  CB   . ARG   A 1 345 ? 4.433   25.979  -25.817 1.00 90.18  ? 863  ARG   A CB   1 
ATOM   2920 C  CG   . ARG   A 1 345 ? 5.742   25.750  -25.094 1.00 91.12  ? 863  ARG   A CG   1 
ATOM   2921 C  CD   . ARG   A 1 345 ? 6.908   25.633  -26.052 1.00 97.80  ? 863  ARG   A CD   1 
ATOM   2922 N  NE   . ARG   A 1 345 ? 8.017   24.901  -25.449 1.00 99.35  ? 863  ARG   A NE   1 
ATOM   2923 C  CZ   . ARG   A 1 345 ? 9.233   24.811  -25.978 1.00 106.01 ? 863  ARG   A CZ   1 
ATOM   2924 N  NH1  . ARG   A 1 345 ? 9.507   25.413  -27.125 1.00 111.60 ? 863  ARG   A NH1  1 
ATOM   2925 N  NH2  . ARG   A 1 345 ? 10.177  24.120  -25.357 1.00 108.20 ? 863  ARG   A NH2  1 
ATOM   2926 N  N    . ALA   A 1 346 ? 2.545   23.711  -24.575 1.00 90.55  ? 864  ALA   A N    1 
ATOM   2927 C  CA   . ALA   A 1 346 ? 2.440   22.431  -23.897 1.00 89.00  ? 864  ALA   A CA   1 
ATOM   2928 C  C    . ALA   A 1 346 ? 3.088   21.361  -24.757 1.00 91.51  ? 864  ALA   A C    1 
ATOM   2929 O  O    . ALA   A 1 346 ? 3.003   21.406  -25.988 1.00 93.78  ? 864  ALA   A O    1 
ATOM   2930 C  CB   . ALA   A 1 346 ? 0.981   22.070  -23.612 1.00 88.35  ? 864  ALA   A CB   1 
ATOM   2931 N  N    . HIS   A 1 347 ? 3.749   20.410  -24.107 1.00 93.10  ? 865  HIS   A N    1 
ATOM   2932 C  CA   . HIS   A 1 347 ? 4.365   19.282  -24.789 1.00 96.13  ? 865  HIS   A CA   1 
ATOM   2933 C  C    . HIS   A 1 347 ? 3.539   18.038  -24.498 1.00 92.27  ? 865  HIS   A C    1 
ATOM   2934 O  O    . HIS   A 1 347 ? 3.440   17.609  -23.342 1.00 84.87  ? 865  HIS   A O    1 
ATOM   2935 C  CB   . HIS   A 1 347 ? 5.821   19.108  -24.361 1.00 100.49 ? 865  HIS   A CB   1 
ATOM   2936 C  CG   . HIS   A 1 347 ? 6.788   19.864  -25.220 1.00 107.08 ? 865  HIS   A CG   1 
ATOM   2937 N  ND1  . HIS   A 1 347 ? 7.410   21.021  -24.803 1.00 107.20 ? 865  HIS   A ND1  1 
ATOM   2938 C  CD2  . HIS   A 1 347 ? 7.226   19.635  -26.481 1.00 112.62 ? 865  HIS   A CD2  1 
ATOM   2939 C  CE1  . HIS   A 1 347 ? 8.196   21.468  -25.766 1.00 112.24 ? 865  HIS   A CE1  1 
ATOM   2940 N  NE2  . HIS   A 1 347 ? 8.103   20.645  -26.795 1.00 115.10 ? 865  HIS   A NE2  1 
ATOM   2941 N  N    . THR   A 1 348 ? 2.948   17.473  -25.554 1.00 97.54  ? 866  THR   A N    1 
ATOM   2942 C  CA   . THR   A 1 348 ? 1.969   16.398  -25.411 1.00 96.33  ? 866  THR   A CA   1 
ATOM   2943 C  C    . THR   A 1 348 ? 2.529   15.224  -24.620 1.00 91.42  ? 866  THR   A C    1 
ATOM   2944 O  O    . THR   A 1 348 ? 1.926   14.774  -23.638 1.00 86.99  ? 866  THR   A O    1 
ATOM   2945 C  CB   . THR   A 1 348 ? 1.523   15.925  -26.795 1.00 102.66 ? 866  THR   A CB   1 
ATOM   2946 O  OG1  . THR   A 1 348 ? 2.648   15.936  -27.685 1.00 108.44 ? 866  THR   A OG1  1 
ATOM   2947 C  CG2  . THR   A 1 348 ? 0.436   16.827  -27.351 1.00 102.27 ? 866  THR   A CG2  1 
ATOM   2948 N  N    . CYS   A 1 349 ? 3.692   14.719  -25.034 1.00 92.84  ? 867  CYS   A N    1 
ATOM   2949 C  CA   . CYS   A 1 349 ? 4.150   13.411  -24.582 1.00 92.55  ? 867  CYS   A CA   1 
ATOM   2950 C  C    . CYS   A 1 349 ? 4.514   13.397  -23.103 1.00 87.47  ? 867  CYS   A C    1 
ATOM   2951 O  O    . CYS   A 1 349 ? 4.427   12.345  -22.459 1.00 84.39  ? 867  CYS   A O    1 
ATOM   2952 C  CB   . CYS   A 1 349 ? 5.342   12.968  -25.428 1.00 98.27  ? 867  CYS   A CB   1 
ATOM   2953 S  SG   . CYS   A 1 349 ? 5.006   12.964  -27.203 1.00 106.08 ? 867  CYS   A SG   1 
ATOM   2954 N  N    . PHE   A 1 350 ? 4.923   14.536  -22.547 1.00 84.31  ? 868  PHE   A N    1 
ATOM   2955 C  CA   . PHE   A 1 350 ? 5.355   14.597  -21.157 1.00 81.87  ? 868  PHE   A CA   1 
ATOM   2956 C  C    . PHE   A 1 350 ? 4.381   15.353  -20.268 1.00 76.67  ? 868  PHE   A C    1 
ATOM   2957 O  O    . PHE   A 1 350 ? 4.701   15.608  -19.101 1.00 76.68  ? 868  PHE   A O    1 
ATOM   2958 C  CB   . PHE   A 1 350 ? 6.746   15.221  -21.062 1.00 84.92  ? 868  PHE   A CB   1 
ATOM   2959 C  CG   . PHE   A 1 350 ? 7.713   14.670  -22.060 1.00 91.32  ? 868  PHE   A CG   1 
ATOM   2960 C  CD1  . PHE   A 1 350 ? 8.292   13.431  -21.862 1.00 95.98  ? 868  PHE   A CD1  1 
ATOM   2961 C  CD2  . PHE   A 1 350 ? 8.046   15.389  -23.195 1.00 92.64  ? 868  PHE   A CD2  1 
ATOM   2962 C  CE1  . PHE   A 1 350 ? 9.169   12.912  -22.785 1.00 104.23 ? 868  PHE   A CE1  1 
ATOM   2963 C  CE2  . PHE   A 1 350 ? 8.937   14.878  -24.116 1.00 99.04  ? 868  PHE   A CE2  1 
ATOM   2964 C  CZ   . PHE   A 1 350 ? 9.504   13.638  -23.907 1.00 105.60 ? 868  PHE   A CZ   1 
ATOM   2965 N  N    . ASN   A 1 351 ? 3.210   15.724  -20.794 1.00 75.39  ? 869  ASN   A N    1 
ATOM   2966 C  CA   . ASN   A 1 351 ? 2.164   16.354  -19.993 1.00 72.26  ? 869  ASN   A CA   1 
ATOM   2967 C  C    . ASN   A 1 351 ? 2.713   17.587  -19.286 1.00 69.65  ? 869  ASN   A C    1 
ATOM   2968 O  O    . ASN   A 1 351 ? 2.403   17.864  -18.126 1.00 62.43  ? 869  ASN   A O    1 
ATOM   2969 C  CB   . ASN   A 1 351 ? 1.594   15.338  -19.013 1.00 74.51  ? 869  ASN   A CB   1 
ATOM   2970 C  CG   . ASN   A 1 351 ? 0.923   14.192  -19.725 1.00 81.23  ? 869  ASN   A CG   1 
ATOM   2971 O  OD1  . ASN   A 1 351 ? 0.318   14.375  -20.777 1.00 87.57  ? 869  ASN   A OD1  1 
ATOM   2972 N  ND2  . ASN   A 1 351 ? 1.182   12.987  -19.259 1.00 80.37  ? 869  ASN   A ND2  1 
ATOM   2973 N  N    . ARG   A 1 352 ? 3.564   18.315  -20.000 1.00 76.72  ? 870  ARG   A N    1 
ATOM   2974 C  CA   . ARG   A 1 352 ? 4.294   19.450  -19.460 1.00 77.24  ? 870  ARG   A CA   1 
ATOM   2975 C  C    . ARG   A 1 352 ? 3.731   20.736  -20.044 1.00 73.81  ? 870  ARG   A C    1 
ATOM   2976 O  O    . ARG   A 1 352 ? 3.492   20.824  -21.253 1.00 72.96  ? 870  ARG   A O    1 
ATOM   2977 C  CB   . ARG   A 1 352 ? 5.787   19.336  -19.771 1.00 79.96  ? 870  ARG   A CB   1 
ATOM   2978 C  CG   . ARG   A 1 352 ? 6.651   20.325  -19.012 1.00 78.50  ? 870  ARG   A CG   1 
ATOM   2979 C  CD   . ARG   A 1 352 ? 8.113   20.155  -19.372 1.00 80.38  ? 870  ARG   A CD   1 
ATOM   2980 N  NE   . ARG   A 1 352 ? 8.352   20.394  -20.791 1.00 84.49  ? 870  ARG   A NE   1 
ATOM   2981 C  CZ   . ARG   A 1 352 ? 9.200   19.689  -21.532 1.00 92.55  ? 870  ARG   A CZ   1 
ATOM   2982 N  NH1  . ARG   A 1 352 ? 9.891   18.697  -20.989 1.00 94.92  ? 870  ARG   A NH1  1 
ATOM   2983 N  NH2  . ARG   A 1 352 ? 9.357   19.975  -22.817 1.00 97.93  ? 870  ARG   A NH2  1 
ATOM   2984 N  N    . LEU   A 1 353 ? 3.517   21.721  -19.181 1.00 73.94  ? 871  LEU   A N    1 
ATOM   2985 C  CA   . LEU   A 1 353 ? 3.037   23.039  -19.571 1.00 73.75  ? 871  LEU   A CA   1 
ATOM   2986 C  C    . LEU   A 1 353 ? 4.189   24.015  -19.379 1.00 77.72  ? 871  LEU   A C    1 
ATOM   2987 O  O    . LEU   A 1 353 ? 4.587   24.300  -18.244 1.00 78.07  ? 871  LEU   A O    1 
ATOM   2988 C  CB   . LEU   A 1 353 ? 1.813   23.434  -18.745 1.00 68.27  ? 871  LEU   A CB   1 
ATOM   2989 C  CG   . LEU   A 1 353 ? 1.056   24.737  -19.032 1.00 68.23  ? 871  LEU   A CG   1 
ATOM   2990 C  CD1  . LEU   A 1 353 ? 1.680   25.919  -18.311 1.00 67.76  ? 871  LEU   A CD1  1 
ATOM   2991 C  CD2  . LEU   A 1 353 ? 0.964   25.006  -20.527 1.00 70.15  ? 871  LEU   A CD2  1 
ATOM   2992 N  N    . ASP   A 1 354 ? 4.738   24.509  -20.484 1.00 78.60  ? 872  ASP   A N    1 
ATOM   2993 C  CA   . ASP   A 1 354 ? 5.824   25.483  -20.429 1.00 82.26  ? 872  ASP   A CA   1 
ATOM   2994 C  C    . ASP   A 1 354 ? 5.209   26.853  -20.180 1.00 79.98  ? 872  ASP   A C    1 
ATOM   2995 O  O    . ASP   A 1 354 ? 4.638   27.468  -21.084 1.00 80.85  ? 872  ASP   A O    1 
ATOM   2996 C  CB   . ASP   A 1 354 ? 6.638   25.447  -21.715 1.00 89.94  ? 872  ASP   A CB   1 
ATOM   2997 C  CG   . ASP   A 1 354 ? 7.328   24.113  -21.931 1.00 93.07  ? 872  ASP   A CG   1 
ATOM   2998 O  OD1  . ASP   A 1 354 ? 7.901   23.577  -20.960 1.00 92.76  ? 872  ASP   A OD1  1 
ATOM   2999 O  OD2  . ASP   A 1 354 ? 7.299   23.602  -23.071 1.00 95.29  ? 872  ASP   A OD2  1 
ATOM   3000 N  N    . LEU   A 1 355 ? 5.318   27.333  -18.942 1.00 77.65  ? 873  LEU   A N    1 
ATOM   3001 C  CA   . LEU   A 1 355 ? 4.669   28.565  -18.517 1.00 81.55  ? 873  LEU   A CA   1 
ATOM   3002 C  C    . LEU   A 1 355 ? 5.691   29.680  -18.398 1.00 80.35  ? 873  LEU   A C    1 
ATOM   3003 O  O    . LEU   A 1 355 ? 6.651   29.552  -17.622 1.00 82.34  ? 873  LEU   A O    1 
ATOM   3004 C  CB   . LEU   A 1 355 ? 3.956   28.358  -17.182 1.00 84.80  ? 873  LEU   A CB   1 
ATOM   3005 C  CG   . LEU   A 1 355 ? 3.157   29.542  -16.633 1.00 89.77  ? 873  LEU   A CG   1 
ATOM   3006 C  CD1  . LEU   A 1 355 ? 1.967   29.856  -17.529 1.00 87.45  ? 873  LEU   A CD1  1 
ATOM   3007 C  CD2  . LEU   A 1 355 ? 2.703   29.261  -15.210 1.00 89.26  ? 873  LEU   A CD2  1 
ATOM   3008 N  N    . PRO   A 1 356 ? 5.539   30.781  -19.131 1.00 77.75  ? 874  PRO   A N    1 
ATOM   3009 C  CA   . PRO   A 1 356 ? 6.440   31.913  -18.949 1.00 77.83  ? 874  PRO   A CA   1 
ATOM   3010 C  C    . PRO   A 1 356 ? 6.230   32.551  -17.584 1.00 74.08  ? 874  PRO   A C    1 
ATOM   3011 O  O    . PRO   A 1 356 ? 5.134   32.461  -17.007 1.00 69.80  ? 874  PRO   A O    1 
ATOM   3012 C  CB   . PRO   A 1 356 ? 6.053   32.872  -20.085 1.00 83.20  ? 874  PRO   A CB   1 
ATOM   3013 C  CG   . PRO   A 1 356 ? 5.298   32.025  -21.069 1.00 81.85  ? 874  PRO   A CG   1 
ATOM   3014 C  CD   . PRO   A 1 356 ? 4.599   30.997  -20.248 1.00 76.79  ? 874  PRO   A CD   1 
ATOM   3015 N  N    . PRO   A 1 357 ? 7.250   33.201  -17.030 1.00 78.22  ? 875  PRO   A N    1 
ATOM   3016 C  CA   . PRO   A 1 357 ? 7.075   33.872  -15.736 1.00 81.91  ? 875  PRO   A CA   1 
ATOM   3017 C  C    . PRO   A 1 357 ? 6.337   35.190  -15.887 1.00 86.38  ? 875  PRO   A C    1 
ATOM   3018 O  O    . PRO   A 1 357 ? 6.932   36.205  -16.258 1.00 91.44  ? 875  PRO   A O    1 
ATOM   3019 C  CB   . PRO   A 1 357 ? 8.514   34.087  -15.243 1.00 86.00  ? 875  PRO   A CB   1 
ATOM   3020 C  CG   . PRO   A 1 357 ? 9.421   33.606  -16.357 1.00 89.07  ? 875  PRO   A CG   1 
ATOM   3021 C  CD   . PRO   A 1 357 ? 8.599   33.405  -17.578 1.00 86.27  ? 875  PRO   A CD   1 
ATOM   3022 N  N    . TYR   A 1 358 ? 5.041   35.188  -15.590 1.00 83.25  ? 876  TYR   A N    1 
ATOM   3023 C  CA   . TYR   A 1 358 ? 4.202   36.358  -15.807 1.00 84.70  ? 876  TYR   A CA   1 
ATOM   3024 C  C    . TYR   A 1 358 ? 4.278   37.307  -14.620 1.00 85.42  ? 876  TYR   A C    1 
ATOM   3025 O  O    . TYR   A 1 358 ? 4.358   36.877  -13.465 1.00 80.24  ? 876  TYR   A O    1 
ATOM   3026 C  CB   . TYR   A 1 358 ? 2.758   35.932  -16.065 1.00 79.31  ? 876  TYR   A CB   1 
ATOM   3027 C  CG   . TYR   A 1 358 ? 2.595   35.238  -17.396 1.00 78.06  ? 876  TYR   A CG   1 
ATOM   3028 C  CD1  . TYR   A 1 358 ? 3.040   35.838  -18.566 1.00 83.22  ? 876  TYR   A CD1  1 
ATOM   3029 C  CD2  . TYR   A 1 358 ? 2.019   33.978  -17.481 1.00 71.91  ? 876  TYR   A CD2  1 
ATOM   3030 C  CE1  . TYR   A 1 358 ? 2.905   35.209  -19.787 1.00 83.80  ? 876  TYR   A CE1  1 
ATOM   3031 C  CE2  . TYR   A 1 358 ? 1.880   33.340  -18.699 1.00 71.45  ? 876  TYR   A CE2  1 
ATOM   3032 C  CZ   . TYR   A 1 358 ? 2.325   33.960  -19.848 1.00 74.77  ? 876  TYR   A CZ   1 
ATOM   3033 O  OH   . TYR   A 1 358 ? 2.189   33.331  -21.064 1.00 75.82  ? 876  TYR   A OH   1 
ATOM   3034 N  N    . GLU   A 1 359 ? 4.249   38.603  -14.918 1.00 92.96  ? 877  GLU   A N    1 
ATOM   3035 C  CA   . GLU   A 1 359 ? 4.441   39.652  -13.928 1.00 98.78  ? 877  GLU   A CA   1 
ATOM   3036 C  C    . GLU   A 1 359 ? 3.145   40.110  -13.272 1.00 97.46  ? 877  GLU   A C    1 
ATOM   3037 O  O    . GLU   A 1 359 ? 3.174   41.052  -12.473 1.00 101.90 ? 877  GLU   A O    1 
ATOM   3038 C  CB   . GLU   A 1 359 ? 5.133   40.855  -14.576 1.00 107.17 ? 877  GLU   A CB   1 
ATOM   3039 C  CG   . GLU   A 1 359 ? 6.628   40.698  -14.784 1.00 111.86 ? 877  GLU   A CG   1 
ATOM   3040 C  CD   . GLU   A 1 359 ? 7.424   41.812  -14.132 1.00 122.73 ? 877  GLU   A CD   1 
ATOM   3041 O  OE1  . GLU   A 1 359 ? 6.817   42.839  -13.761 1.00 127.85 ? 877  GLU   A OE1  1 
ATOM   3042 O  OE2  . GLU   A 1 359 ? 8.656   41.664  -13.995 1.00 127.57 ? 877  GLU   A OE2  1 
ATOM   3043 N  N    . SER   A 1 360 ? 2.015   39.480  -13.588 1.00 89.64  ? 878  SER   A N    1 
ATOM   3044 C  CA   . SER   A 1 360 ? 0.742   39.859  -12.992 1.00 91.25  ? 878  SER   A CA   1 
ATOM   3045 C  C    . SER   A 1 360 ? -0.244  38.715  -13.168 1.00 87.39  ? 878  SER   A C    1 
ATOM   3046 O  O    . SER   A 1 360 ? -0.142  37.931  -14.116 1.00 77.65  ? 878  SER   A O    1 
ATOM   3047 C  CB   . SER   A 1 360 ? 0.183   41.142  -13.617 1.00 99.12  ? 878  SER   A CB   1 
ATOM   3048 O  OG   . SER   A 1 360 ? -1.166  41.347  -13.236 1.00 101.91 ? 878  SER   A OG   1 
ATOM   3049 N  N    . PHE   A 1 361 ? -1.200  38.627  -12.239 1.00 86.28  ? 879  PHE   A N    1 
ATOM   3050 C  CA   . PHE   A 1 361 ? -2.220  37.588  -12.335 1.00 86.15  ? 879  PHE   A CA   1 
ATOM   3051 C  C    . PHE   A 1 361 ? -3.080  37.780  -13.575 1.00 84.21  ? 879  PHE   A C    1 
ATOM   3052 O  O    . PHE   A 1 361 ? -3.321  36.833  -14.333 1.00 78.89  ? 879  PHE   A O    1 
ATOM   3053 C  CB   . PHE   A 1 361 ? -3.101  37.577  -11.086 1.00 88.58  ? 879  PHE   A CB   1 
ATOM   3054 C  CG   . PHE   A 1 361 ? -4.384  36.818  -11.274 1.00 85.86  ? 879  PHE   A CG   1 
ATOM   3055 C  CD1  . PHE   A 1 361 ? -5.576  37.482  -11.525 1.00 88.43  ? 879  PHE   A CD1  1 
ATOM   3056 C  CD2  . PHE   A 1 361 ? -4.390  35.434  -11.235 1.00 81.62  ? 879  PHE   A CD2  1 
ATOM   3057 C  CE1  . PHE   A 1 361 ? -6.751  36.779  -11.713 1.00 87.81  ? 879  PHE   A CE1  1 
ATOM   3058 C  CE2  . PHE   A 1 361 ? -5.560  34.724  -11.426 1.00 79.52  ? 879  PHE   A CE2  1 
ATOM   3059 C  CZ   . PHE   A 1 361 ? -6.743  35.398  -11.662 1.00 85.21  ? 879  PHE   A CZ   1 
ATOM   3060 N  N    . GLU   A 1 362 ? -3.570  39.005  -13.786 1.00 86.61  ? 880  GLU   A N    1 
ATOM   3061 C  CA   . GLU   A 1 362 ? -4.436  39.269  -14.928 1.00 85.51  ? 880  GLU   A CA   1 
ATOM   3062 C  C    . GLU   A 1 362 ? -3.727  38.976  -16.243 1.00 84.10  ? 880  GLU   A C    1 
ATOM   3063 O  O    . GLU   A 1 362 ? -4.356  38.491  -17.188 1.00 84.20  ? 880  GLU   A O    1 
ATOM   3064 C  CB   . GLU   A 1 362 ? -4.933  40.714  -14.880 1.00 91.60  ? 880  GLU   A CB   1 
ATOM   3065 C  CG   . GLU   A 1 362 ? -6.430  40.865  -15.112 1.00 94.73  ? 880  GLU   A CG   1 
ATOM   3066 C  CD   . GLU   A 1 362 ? -7.270  40.148  -14.068 1.00 91.38  ? 880  GLU   A CD   1 
ATOM   3067 O  OE1  . GLU   A 1 362 ? -7.136  40.467  -12.869 1.00 92.96  ? 880  GLU   A OE1  1 
ATOM   3068 O  OE2  . GLU   A 1 362 ? -8.066  39.264  -14.450 1.00 84.69  ? 880  GLU   A OE2  1 
ATOM   3069 N  N    . GLU   A 1 363 ? -2.418  39.235  -16.317 1.00 84.13  ? 881  GLU   A N    1 
ATOM   3070 C  CA   . GLU   A 1 363 ? -1.666  38.861  -17.512 1.00 85.24  ? 881  GLU   A CA   1 
ATOM   3071 C  C    . GLU   A 1 363 ? -1.593  37.348  -17.668 1.00 79.84  ? 881  GLU   A C    1 
ATOM   3072 O  O    . GLU   A 1 363 ? -1.771  36.825  -18.774 1.00 77.96  ? 881  GLU   A O    1 
ATOM   3073 C  CB   . GLU   A 1 363 ? -0.260  39.456  -17.469 1.00 91.11  ? 881  GLU   A CB   1 
ATOM   3074 C  CG   . GLU   A 1 363 ? 0.574   39.119  -18.697 1.00 94.35  ? 881  GLU   A CG   1 
ATOM   3075 C  CD   . GLU   A 1 363 ? 2.045   39.430  -18.512 1.00 100.10 ? 881  GLU   A CD   1 
ATOM   3076 O  OE1  . GLU   A 1 363 ? 2.463   39.670  -17.360 1.00 101.65 ? 881  GLU   A OE1  1 
ATOM   3077 O  OE2  . GLU   A 1 363 ? 2.784   39.432  -19.519 1.00 103.58 ? 881  GLU   A OE2  1 
ATOM   3078 N  N    . LEU   A 1 364 ? -1.317  36.628  -16.575 1.00 74.16  ? 882  LEU   A N    1 
ATOM   3079 C  CA   . LEU   A 1 364 ? -1.333  35.170  -16.638 1.00 71.30  ? 882  LEU   A CA   1 
ATOM   3080 C  C    . LEU   A 1 364 ? -2.685  34.664  -17.117 1.00 68.60  ? 882  LEU   A C    1 
ATOM   3081 O  O    . LEU   A 1 364 ? -2.754  33.754  -17.949 1.00 65.25  ? 882  LEU   A O    1 
ATOM   3082 C  CB   . LEU   A 1 364 ? -0.994  34.570  -15.273 1.00 67.05  ? 882  LEU   A CB   1 
ATOM   3083 C  CG   . LEU   A 1 364 ? -1.086  33.041  -15.208 1.00 66.49  ? 882  LEU   A CG   1 
ATOM   3084 C  CD1  . LEU   A 1 364 ? 0.169   32.446  -14.590 1.00 67.11  ? 882  LEU   A CD1  1 
ATOM   3085 C  CD2  . LEU   A 1 364 ? -2.327  32.584  -14.450 1.00 67.52  ? 882  LEU   A CD2  1 
ATOM   3086 N  N    . TRP   A 1 365 ? -3.770  35.252  -16.607 1.00 69.71  ? 883  TRP   A N    1 
ATOM   3087 C  CA   . TRP   A 1 365 ? -5.110  34.868  -17.037 1.00 71.53  ? 883  TRP   A CA   1 
ATOM   3088 C  C    . TRP   A 1 365 ? -5.259  34.967  -18.550 1.00 72.49  ? 883  TRP   A C    1 
ATOM   3089 O  O    . TRP   A 1 365 ? -5.628  33.993  -19.212 1.00 69.62  ? 883  TRP   A O    1 
ATOM   3090 C  CB   . TRP   A 1 365 ? -6.156  35.736  -16.332 1.00 81.01  ? 883  TRP   A CB   1 
ATOM   3091 C  CG   . TRP   A 1 365 ? -7.570  35.457  -16.757 1.00 80.55  ? 883  TRP   A CG   1 
ATOM   3092 C  CD1  . TRP   A 1 365 ? -8.305  36.163  -17.664 1.00 81.93  ? 883  TRP   A CD1  1 
ATOM   3093 C  CD2  . TRP   A 1 365 ? -8.415  34.393  -16.298 1.00 77.15  ? 883  TRP   A CD2  1 
ATOM   3094 N  NE1  . TRP   A 1 365 ? -9.556  35.609  -17.795 1.00 81.68  ? 883  TRP   A NE1  1 
ATOM   3095 C  CE2  . TRP   A 1 365 ? -9.648  34.521  -16.969 1.00 79.08  ? 883  TRP   A CE2  1 
ATOM   3096 C  CE3  . TRP   A 1 365 ? -8.248  33.346  -15.387 1.00 70.50  ? 883  TRP   A CE3  1 
ATOM   3097 C  CZ2  . TRP   A 1 365 ? -10.709 33.640  -16.756 1.00 77.78  ? 883  TRP   A CZ2  1 
ATOM   3098 C  CZ3  . TRP   A 1 365 ? -9.302  32.473  -15.177 1.00 70.81  ? 883  TRP   A CZ3  1 
ATOM   3099 C  CH2  . TRP   A 1 365 ? -10.518 32.627  -15.857 1.00 74.87  ? 883  TRP   A CH2  1 
ATOM   3100 N  N    . ASP   A 1 366 ? -4.956  36.133  -19.122 1.00 78.46  ? 884  ASP   A N    1 
ATOM   3101 C  CA   . ASP   A 1 366 ? -5.199  36.327  -20.549 1.00 87.22  ? 884  ASP   A CA   1 
ATOM   3102 C  C    . ASP   A 1 366 ? -4.238  35.507  -21.399 1.00 87.23  ? 884  ASP   A C    1 
ATOM   3103 O  O    . ASP   A 1 366 ? -4.663  34.757  -22.285 1.00 86.11  ? 884  ASP   A O    1 
ATOM   3104 C  CB   . ASP   A 1 366 ? -5.134  37.809  -20.919 1.00 96.33  ? 884  ASP   A CB   1 
ATOM   3105 C  CG   . ASP   A 1 366 ? -5.824  38.689  -19.907 1.00 102.49 ? 884  ASP   A CG   1 
ATOM   3106 O  OD1  . ASP   A 1 366 ? -5.211  39.646  -19.383 1.00 106.81 ? 884  ASP   A OD1  1 
ATOM   3107 O  OD2  . ASP   A 1 366 ? -6.984  38.364  -19.593 1.00 102.27 ? 884  ASP   A OD2  1 
ATOM   3108 N  N    . LYS   A 1 367 ? -2.935  35.624  -21.143 1.00 88.93  ? 885  LYS   A N    1 
ATOM   3109 C  CA   . LYS   A 1 367 ? -1.979  34.897  -21.970 1.00 89.41  ? 885  LYS   A CA   1 
ATOM   3110 C  C    . LYS   A 1 367 ? -2.160  33.381  -21.869 1.00 87.25  ? 885  LYS   A C    1 
ATOM   3111 O  O    . LYS   A 1 367 ? -1.808  32.665  -22.810 1.00 89.16  ? 885  LYS   A O    1 
ATOM   3112 C  CB   . LYS   A 1 367 ? -0.547  35.328  -21.618 1.00 89.62  ? 885  LYS   A CB   1 
ATOM   3113 C  CG   . LYS   A 1 367 ? -0.279  36.823  -21.882 1.00 92.05  ? 885  LYS   A CG   1 
ATOM   3114 C  CD   . LYS   A 1 367 ? 0.489   37.087  -23.187 1.00 94.81  ? 885  LYS   A CD   1 
ATOM   3115 C  CE   . LYS   A 1 367 ? -0.109  38.260  -23.972 1.00 97.12  ? 885  LYS   A CE   1 
ATOM   3116 N  NZ   . LYS   A 1 367 ? 0.004   38.112  -25.457 1.00 100.05 ? 885  LYS   A NZ   1 
ATOM   3117 N  N    . LEU   A 1 368 ? -2.745  32.878  -20.779 1.00 82.45  ? 886  LEU   A N    1 
ATOM   3118 C  CA   . LEU   A 1 368 ? -3.042  31.450  -20.698 1.00 78.48  ? 886  LEU   A CA   1 
ATOM   3119 C  C    . LEU   A 1 368 ? -4.310  31.095  -21.470 1.00 82.32  ? 886  LEU   A C    1 
ATOM   3120 O  O    . LEU   A 1 368 ? -4.337  30.105  -22.209 1.00 80.90  ? 886  LEU   A O    1 
ATOM   3121 C  CB   . LEU   A 1 368 ? -3.173  31.020  -19.236 1.00 74.12  ? 886  LEU   A CB   1 
ATOM   3122 C  CG   . LEU   A 1 368 ? -3.462  29.550  -18.928 1.00 71.14  ? 886  LEU   A CG   1 
ATOM   3123 C  CD1  . LEU   A 1 368 ? -2.173  28.781  -18.683 1.00 69.41  ? 886  LEU   A CD1  1 
ATOM   3124 C  CD2  . LEU   A 1 368 ? -4.390  29.441  -17.728 1.00 68.81  ? 886  LEU   A CD2  1 
ATOM   3125 N  N    . GLN   A 1 369 ? -5.372  31.893  -21.309 1.00 86.43  ? 887  GLN   A N    1 
ATOM   3126 C  CA   . GLN   A 1 369 ? -6.641  31.581  -21.964 1.00 87.47  ? 887  GLN   A CA   1 
ATOM   3127 C  C    . GLN   A 1 369 ? -6.550  31.707  -23.479 1.00 88.47  ? 887  GLN   A C    1 
ATOM   3128 O  O    . GLN   A 1 369 ? -7.267  31.005  -24.201 1.00 89.65  ? 887  GLN   A O    1 
ATOM   3129 C  CB   . GLN   A 1 369 ? -7.752  32.486  -21.432 1.00 89.16  ? 887  GLN   A CB   1 
ATOM   3130 C  CG   . GLN   A 1 369 ? -8.011  32.347  -19.944 1.00 90.29  ? 887  GLN   A CG   1 
ATOM   3131 C  CD   . GLN   A 1 369 ? -9.365  31.758  -19.634 1.00 93.76  ? 887  GLN   A CD   1 
ATOM   3132 O  OE1  . GLN   A 1 369 ? -10.302 31.874  -20.422 1.00 96.95  ? 887  GLN   A OE1  1 
ATOM   3133 N  NE2  . GLN   A 1 369 ? -9.479  31.121  -18.477 1.00 94.65  ? 887  GLN   A NE2  1 
ATOM   3134 N  N    . MET   A 1 370 ? -5.689  32.594  -23.980 1.00 90.39  ? 888  MET   A N    1 
ATOM   3135 C  CA   . MET   A 1 370 ? -5.527  32.723  -25.422 1.00 96.84  ? 888  MET   A CA   1 
ATOM   3136 C  C    . MET   A 1 370 ? -4.810  31.526  -26.030 1.00 98.23  ? 888  MET   A C    1 
ATOM   3137 O  O    . MET   A 1 370 ? -4.997  31.247  -27.218 1.00 103.51 ? 888  MET   A O    1 
ATOM   3138 C  CB   . MET   A 1 370 ? -4.777  34.013  -25.757 1.00 104.42 ? 888  MET   A CB   1 
ATOM   3139 C  CG   . MET   A 1 370 ? -5.610  35.277  -25.587 1.00 112.16 ? 888  MET   A CG   1 
ATOM   3140 S  SD   . MET   A 1 370 ? -7.049  35.330  -26.675 1.00 118.27 ? 888  MET   A SD   1 
ATOM   3141 C  CE   . MET   A 1 370 ? -8.374  35.003  -25.512 1.00 114.25 ? 888  MET   A CE   1 
ATOM   3142 N  N    . ALA   A 1 371 ? -3.997  30.815  -25.247 1.00 94.19  ? 889  ALA   A N    1 
ATOM   3143 C  CA   . ALA   A 1 371 ? -3.329  29.612  -25.723 1.00 93.55  ? 889  ALA   A CA   1 
ATOM   3144 C  C    . ALA   A 1 371 ? -4.245  28.397  -25.738 1.00 91.99  ? 889  ALA   A C    1 
ATOM   3145 O  O    . ALA   A 1 371 ? -3.907  27.392  -26.373 1.00 91.85  ? 889  ALA   A O    1 
ATOM   3146 C  CB   . ALA   A 1 371 ? -2.101  29.314  -24.859 1.00 91.31  ? 889  ALA   A CB   1 
ATOM   3147 N  N    . ILE   A 1 372 ? -5.389  28.468  -25.061 1.00 91.92  ? 890  ILE   A N    1 
ATOM   3148 C  CA   . ILE   A 1 372 ? -6.320  27.356  -25.004 1.00 93.24  ? 890  ILE   A CA   1 
ATOM   3149 C  C    . ILE   A 1 372 ? -7.521  27.567  -25.925 1.00 97.86  ? 890  ILE   A C    1 
ATOM   3150 O  O    . ILE   A 1 372 ? -8.096  26.584  -26.411 1.00 97.51  ? 890  ILE   A O    1 
ATOM   3151 C  CB   . ILE   A 1 372 ? -6.767  27.114  -23.541 1.00 90.56  ? 890  ILE   A CB   1 
ATOM   3152 C  CG1  . ILE   A 1 372 ? -5.744  26.233  -22.810 1.00 89.93  ? 890  ILE   A CG1  1 
ATOM   3153 C  CG2  . ILE   A 1 372 ? -8.143  26.465  -23.455 1.00 90.27  ? 890  ILE   A CG2  1 
ATOM   3154 C  CD1  . ILE   A 1 372 ? -4.432  26.928  -22.487 1.00 91.03  ? 890  ILE   A CD1  1 
ATOM   3155 N  N    . GLU   A 1 373 ? -7.872  28.820  -26.232 1.00 105.07 ? 891  GLU   A N    1 
ATOM   3156 C  CA   . GLU   A 1 373 ? -8.939  29.115  -27.183 1.00 113.21 ? 891  GLU   A CA   1 
ATOM   3157 C  C    . GLU   A 1 373 ? -8.705  28.473  -28.547 1.00 120.03 ? 891  GLU   A C    1 
ATOM   3158 O  O    . GLU   A 1 373 ? -9.656  28.331  -29.323 1.00 123.49 ? 891  GLU   A O    1 
ATOM   3159 C  CB   . GLU   A 1 373 ? -9.089  30.631  -27.338 1.00 116.70 ? 891  GLU   A CB   1 
ATOM   3160 C  CG   . GLU   A 1 373 ? -10.366 31.072  -28.032 1.00 120.95 ? 891  GLU   A CG   1 
ATOM   3161 C  CD   . GLU   A 1 373 ? -10.209 32.392  -28.762 1.00 126.42 ? 891  GLU   A CD   1 
ATOM   3162 O  OE1  . GLU   A 1 373 ? -11.142 32.781  -29.496 1.00 130.60 ? 891  GLU   A OE1  1 
ATOM   3163 O  OE2  . GLU   A 1 373 ? -9.156  33.043  -28.597 1.00 127.09 ? 891  GLU   A OE2  1 
ATOM   3164 N  N    . ASN   A 1 374 ? -7.473  28.079  -28.859 1.00 122.28 ? 892  ASN   A N    1 
ATOM   3165 C  CA   . ASN   A 1 374 ? -7.169  27.391  -30.112 1.00 127.60 ? 892  ASN   A CA   1 
ATOM   3166 C  C    . ASN   A 1 374 ? -6.975  25.900  -29.917 1.00 128.30 ? 892  ASN   A C    1 
ATOM   3167 O  O    . ASN   A 1 374 ? -6.080  25.279  -30.501 1.00 130.74 ? 892  ASN   A O    1 
ATOM   3168 C  CB   . ASN   A 1 374 ? -5.964  28.023  -30.777 1.00 129.90 ? 892  ASN   A CB   1 
ATOM   3169 C  CG   . ASN   A 1 374 ? -5.971  29.494  -30.616 1.00 132.55 ? 892  ASN   A CG   1 
ATOM   3170 O  OD1  . ASN   A 1 374 ? -5.721  30.010  -29.533 1.00 129.64 ? 892  ASN   A OD1  1 
ATOM   3171 N  ND2  . ASN   A 1 374 ? -6.410  30.180  -31.649 1.00 138.76 ? 892  ASN   A ND2  1 
ATOM   3172 N  N    . THR   A 1 375 ? -7.837  25.302  -29.112 1.00 126.66 ? 893  THR   A N    1 
ATOM   3173 C  CA   . THR   A 1 375 ? -7.868  23.864  -28.959 1.00 126.34 ? 893  THR   A CA   1 
ATOM   3174 C  C    . THR   A 1 375 ? -9.283  23.357  -29.205 1.00 128.93 ? 893  THR   A C    1 
ATOM   3175 O  O    . THR   A 1 375 ? -10.100 23.313  -28.287 1.00 127.92 ? 893  THR   A O    1 
ATOM   3176 C  CB   . THR   A 1 375 ? -7.395  23.440  -27.561 1.00 121.66 ? 893  THR   A CB   1 
ATOM   3177 O  OG1  . THR   A 1 375 ? -8.210  24.076  -26.568 1.00 120.86 ? 893  THR   A OG1  1 
ATOM   3178 C  CG2  . THR   A 1 375 ? -5.940  23.834  -27.350 1.00 119.60 ? 893  THR   A CG2  1 
HETATM 3179 C  C12  . A1ITT B 2 .   ? -36.791 29.810  -34.234 1.00 76.32  ? 901  A1ITT A C12  1 
HETATM 3180 C  C11  . A1ITT B 2 .   ? -36.291 29.602  -35.664 1.00 72.95  ? 901  A1ITT A C11  1 
HETATM 3181 N  N10  . A1ITT B 2 .   ? -36.424 28.231  -36.129 1.00 71.43  ? 901  A1ITT A N10  1 
HETATM 3182 C  C02  . A1ITT B 2 .   ? -32.270 21.045  -36.629 1.00 55.81  ? 901  A1ITT A C02  1 
HETATM 3183 C  C03  . A1ITT B 2 .   ? -32.348 22.422  -36.826 1.00 55.54  ? 901  A1ITT A C03  1 
HETATM 3184 C  C04  . A1ITT B 2 .   ? -32.862 22.906  -38.056 1.00 60.66  ? 901  A1ITT A C04  1 
HETATM 3185 C  C06  . A1ITT B 2 .   ? -33.409 25.217  -37.278 1.00 68.82  ? 901  A1ITT A C06  1 
HETATM 3186 C  C07  . A1ITT B 2 .   ? -34.930 25.385  -37.342 1.00 71.56  ? 901  A1ITT A C07  1 
HETATM 3187 C  C08  . A1ITT B 2 .   ? -35.382 26.767  -37.844 1.00 72.20  ? 901  A1ITT A C08  1 
HETATM 3188 C  C09  . A1ITT B 2 .   ? -35.180 27.877  -36.805 1.00 73.34  ? 901  A1ITT A C09  1 
HETATM 3189 C  C13  . A1ITT B 2 .   ? -35.790 30.366  -33.231 1.00 88.23  ? 901  A1ITT A C13  1 
HETATM 3190 C  C14  . A1ITT B 2 .   ? -36.492 31.335  -32.284 1.00 101.49 ? 901  A1ITT A C14  1 
HETATM 3191 C  C16  . A1ITT B 2 .   ? -34.561 31.856  -31.054 1.00 104.93 ? 901  A1ITT A C16  1 
HETATM 3192 C  C17  . A1ITT B 2 .   ? -34.042 31.716  -29.625 1.00 104.11 ? 901  A1ITT A C17  1 
HETATM 3193 C  C19  . A1ITT B 2 .   ? -32.086 24.988  -39.364 1.00 68.23  ? 901  A1ITT A C19  1 
HETATM 3194 C  C20  . A1ITT B 2 .   ? -31.342 26.126  -38.969 1.00 73.34  ? 901  A1ITT A C20  1 
HETATM 3195 C  C21  . A1ITT B 2 .   ? -30.504 26.771  -39.873 1.00 75.07  ? 901  A1ITT A C21  1 
HETATM 3196 C  C22  . A1ITT B 2 .   ? -30.391 26.290  -41.183 1.00 72.87  ? 901  A1ITT A C22  1 
HETATM 3197 C  C23  . A1ITT B 2 .   ? -31.117 25.166  -41.574 1.00 72.27  ? 901  A1ITT A C23  1 
HETATM 3198 C  C24  . A1ITT B 2 .   ? -31.976 24.507  -40.659 1.00 70.90  ? 901  A1ITT A C24  1 
HETATM 3199 C  C25  . A1ITT B 2 .   ? -32.723 23.266  -41.207 1.00 70.31  ? 901  A1ITT A C25  1 
HETATM 3200 C  C26  . A1ITT B 2 .   ? -33.806 22.638  -40.344 1.00 68.72  ? 901  A1ITT A C26  1 
HETATM 3201 C  C27  . A1ITT B 2 .   ? -33.265 22.049  -39.032 1.00 62.19  ? 901  A1ITT A C27  1 
HETATM 3202 C  C28  . A1ITT B 2 .   ? -33.194 20.647  -38.838 1.00 54.99  ? 901  A1ITT A C28  1 
HETATM 3203 C  C29  . A1ITT B 2 .   ? -32.694 20.160  -37.630 1.00 52.40  ? 901  A1ITT A C29  1 
HETATM 3204 N  N05  . A1ITT B 2 .   ? -32.946 24.345  -38.348 1.00 64.22  ? 901  A1ITT A N05  1 
HETATM 3205 O  O15  . A1ITT B 2 .   ? -35.942 31.631  -31.033 1.00 103.55 ? 901  A1ITT A O15  1 
HETATM 3206 O  O18  . A1ITT B 2 .   ? -37.513 31.840  -32.616 1.00 111.68 ? 901  A1ITT A O18  1 
HETATM 3207 CL CL01 . A1ITT B 2 .   ? -31.632 20.403  -35.093 1.00 59.42  ? 901  A1ITT A CL01 1 
HETATM 3208 O  O    . HOH   C 3 .   ? 4.059   21.637  -12.327 1.00 55.71  ? 1001 HOH   A O    1 
HETATM 3209 O  O    . HOH   C 3 .   ? -24.654 8.562   -50.872 1.00 76.02  ? 1002 HOH   A O    1 
HETATM 3210 O  O    . HOH   C 3 .   ? 12.146  32.625  -15.199 1.00 58.71  ? 1003 HOH   A O    1 
HETATM 3211 O  O    . HOH   C 3 .   ? -13.130 18.006  -42.780 1.00 57.37  ? 1004 HOH   A O    1 
HETATM 3212 O  O    . HOH   C 3 .   ? -24.635 -7.895  -33.625 1.00 63.44  ? 1005 HOH   A O    1 
HETATM 3213 O  O    . HOH   C 3 .   ? -49.183 32.266  12.955  1.00 47.84  ? 1006 HOH   A O    1 
HETATM 3214 O  O    . HOH   C 3 .   ? -42.223 17.063  -36.352 1.00 50.34  ? 1007 HOH   A O    1 
HETATM 3215 O  O    . HOH   C 3 .   ? -39.034 33.499  -32.507 1.00 104.42 ? 1008 HOH   A O    1 
HETATM 3216 O  O    . HOH   C 3 .   ? -16.378 -7.640  -17.697 1.00 81.20  ? 1009 HOH   A O    1 
HETATM 3217 O  O    . HOH   C 3 .   ? -20.792 27.491  -29.682 1.00 106.37 ? 1010 HOH   A O    1 
HETATM 3218 O  O    . HOH   C 3 .   ? 6.859   23.987  -2.400  1.00 97.88  ? 1011 HOH   A O    1 
HETATM 3219 O  O    . HOH   C 3 .   ? -25.005 11.261  -49.439 1.00 98.48  ? 1012 HOH   A O    1 
HETATM 3220 O  O    . HOH   C 3 .   ? -38.320 18.208  -41.479 1.00 71.77  ? 1013 HOH   A O    1 
HETATM 3221 O  O    . HOH   C 3 .   ? -41.132 23.653  -38.230 1.00 92.77  ? 1014 HOH   A O    1 
HETATM 3222 O  O    . HOH   C 3 .   ? -48.304 40.147  -14.643 1.00 71.22  ? 1015 HOH   A O    1 
HETATM 3223 O  O    . HOH   C 3 .   ? -42.959 19.085  -34.545 1.00 56.89  ? 1016 HOH   A O    1 
HETATM 3224 O  O    . HOH   C 3 .   ? -46.141 25.562  -16.885 1.00 64.04  ? 1017 HOH   A O    1 
HETATM 3225 O  O    . HOH   C 3 .   ? 6.682   23.040  -4.738  1.00 99.03  ? 1018 HOH   A O    1 
HETATM 3226 O  O    . HOH   C 3 .   ? -47.744 27.302  3.213   1.00 56.01  ? 1019 HOH   A O    1 
HETATM 3227 O  O    . HOH   C 3 .   ? -5.173  11.077  -7.434  1.00 73.28  ? 1020 HOH   A O    1 
HETATM 3228 O  O    . HOH   C 3 .   ? -30.436 9.635   -46.429 1.00 97.10  ? 1021 HOH   A O    1 
HETATM 3229 O  O    . HOH   C 3 .   ? -19.584 13.532  -15.600 1.00 47.71  ? 1022 HOH   A O    1 
HETATM 3230 O  O    . HOH   C 3 .   ? -26.745 23.385  -14.744 1.00 52.80  ? 1023 HOH   A O    1 
HETATM 3231 O  O    . HOH   C 3 .   ? -18.656 17.074  -50.204 1.00 83.19  ? 1024 HOH   A O    1 
HETATM 3232 O  O    . HOH   C 3 .   ? -0.965  14.506  -12.107 1.00 56.86  ? 1025 HOH   A O    1 
HETATM 3233 O  O    . HOH   C 3 .   ? -13.368 17.715  -45.417 1.00 85.54  ? 1026 HOH   A O    1 
HETATM 3234 O  O    . HOH   C 3 .   ? -30.910 24.750  -30.437 1.00 38.45  ? 1027 HOH   A O    1 
HETATM 3235 O  O    . HOH   C 3 .   ? -48.944 40.299  -17.854 1.00 134.15 ? 1028 HOH   A O    1 
HETATM 3236 O  O    . HOH   C 3 .   ? 1.115   21.018  -5.880  1.00 97.99  ? 1029 HOH   A O    1 
HETATM 3237 O  O    . HOH   C 3 .   ? -11.132 0.744   -20.864 1.00 65.71  ? 1030 HOH   A O    1 
HETATM 3238 O  O    . HOH   C 3 .   ? 9.904   28.923  -6.288  1.00 98.82  ? 1031 HOH   A O    1 
HETATM 3239 O  O    . HOH   C 3 .   ? -16.110 10.098  -42.102 1.00 61.08  ? 1032 HOH   A O    1 
HETATM 3240 O  O    . HOH   C 3 .   ? -41.634 22.001  -17.780 1.00 80.81  ? 1033 HOH   A O    1 
HETATM 3241 O  O    . HOH   C 3 .   ? -15.031 23.081  -40.909 1.00 96.18  ? 1034 HOH   A O    1 
HETATM 3242 O  O    . HOH   C 3 .   ? -33.348 28.786  -27.524 1.00 52.49  ? 1035 HOH   A O    1 
HETATM 3243 O  O    . HOH   C 3 .   ? -34.738 7.303   -41.244 1.00 49.99  ? 1036 HOH   A O    1 
HETATM 3244 O  O    . HOH   C 3 .   ? -18.962 5.528   -26.697 1.00 73.05  ? 1037 HOH   A O    1 
HETATM 3245 O  O    . HOH   C 3 .   ? -47.194 34.589  3.239   1.00 44.82  ? 1038 HOH   A O    1 
HETATM 3246 O  O    . HOH   C 3 .   ? -39.080 24.428  -38.376 1.00 91.00  ? 1039 HOH   A O    1 
HETATM 3247 O  O    . HOH   C 3 .   ? -46.068 19.826  -11.989 1.00 47.20  ? 1040 HOH   A O    1 
HETATM 3248 O  O    . HOH   C 3 .   ? -37.142 10.648  -15.546 1.00 49.49  ? 1041 HOH   A O    1 
HETATM 3249 O  O    . HOH   C 3 .   ? -28.238 5.256   -47.219 1.00 64.87  ? 1042 HOH   A O    1 
HETATM 3250 O  O    . HOH   C 3 .   ? -32.400 0.961   -35.036 1.00 56.29  ? 1043 HOH   A O    1 
HETATM 3251 O  O    . HOH   C 3 .   ? -35.174 2.740   -38.734 1.00 56.01  ? 1044 HOH   A O    1 
HETATM 3252 O  O    . HOH   C 3 .   ? 7.520   33.369  -6.312  1.00 73.56  ? 1045 HOH   A O    1 
HETATM 3253 O  O    . HOH   C 3 .   ? -46.144 28.271  -3.910  1.00 47.18  ? 1046 HOH   A O    1 
HETATM 3254 O  O    . HOH   C 3 .   ? -45.468 27.125  9.582   1.00 67.87  ? 1047 HOH   A O    1 
HETATM 3255 O  O    . HOH   C 3 .   ? -36.942 34.561  -32.633 1.00 100.40 ? 1048 HOH   A O    1 
HETATM 3256 O  O    . HOH   C 3 .   ? -3.522  9.172   -17.997 1.00 66.41  ? 1049 HOH   A O    1 
HETATM 3257 O  O    . HOH   C 3 .   ? -35.569 20.646  -18.340 1.00 48.17  ? 1050 HOH   A O    1 
HETATM 3258 O  O    . HOH   C 3 .   ? -44.301 22.107  -24.704 1.00 95.90  ? 1051 HOH   A O    1 
HETATM 3259 O  O    . HOH   C 3 .   ? -6.832  6.536   -43.105 1.00 76.19  ? 1052 HOH   A O    1 
HETATM 3260 O  O    . HOH   C 3 .   ? -49.948 14.845  -0.435  1.00 51.08  ? 1053 HOH   A O    1 
HETATM 3261 O  O    . HOH   C 3 .   ? -36.445 22.963  -19.692 1.00 47.87  ? 1054 HOH   A O    1 
HETATM 3262 O  O    . HOH   C 3 .   ? -53.735 18.774  0.175   1.00 54.30  ? 1055 HOH   A O    1 
HETATM 3263 O  O    . HOH   C 3 .   ? -43.863 18.484  -24.566 1.00 46.83  ? 1056 HOH   A O    1 
HETATM 3264 O  O    . HOH   C 3 .   ? -33.248 0.232   -38.127 1.00 55.51  ? 1057 HOH   A O    1 
HETATM 3265 O  O    . HOH   C 3 .   ? -22.248 35.574  -13.282 1.00 54.98  ? 1058 HOH   A O    1 
HETATM 3266 O  O    . HOH   C 3 .   ? -19.012 8.400   -26.869 1.00 49.15  ? 1059 HOH   A O    1 
HETATM 3267 O  O    . HOH   C 3 .   ? -47.954 30.470  -2.870  1.00 51.73  ? 1060 HOH   A O    1 
HETATM 3268 O  O    . HOH   C 3 .   ? -49.332 12.510  3.661   1.00 67.34  ? 1061 HOH   A O    1 
HETATM 3269 O  O    . HOH   C 3 .   ? -38.620 22.836  -18.604 1.00 77.10  ? 1062 HOH   A O    1 
HETATM 3270 O  O    . HOH   C 3 .   ? -18.237 6.469   -11.896 1.00 75.55  ? 1063 HOH   A O    1 
HETATM 3271 O  O    . HOH   C 3 .   ? -52.911 34.613  -6.420  1.00 91.75  ? 1064 HOH   A O    1 
HETATM 3272 O  O    . HOH   C 3 .   ? -23.107 26.433  -15.836 1.00 58.37  ? 1065 HOH   A O    1 
HETATM 3273 O  O    . HOH   C 3 .   ? -23.437 26.810  -30.346 1.00 52.79  ? 1066 HOH   A O    1 
HETATM 3274 O  O    . HOH   C 3 .   ? -34.002 19.614  -20.631 1.00 33.56  ? 1067 HOH   A O    1 
HETATM 3275 O  O    . HOH   C 3 .   ? -18.178 -8.801  -27.728 1.00 100.43 ? 1068 HOH   A O    1 
HETATM 3276 O  O    . HOH   C 3 .   ? -55.089 18.132  -10.713 1.00 49.91  ? 1069 HOH   A O    1 
HETATM 3277 O  O    . HOH   C 3 .   ? -26.961 20.546  -13.898 1.00 44.23  ? 1070 HOH   A O    1 
HETATM 3278 O  O    . HOH   C 3 .   ? -38.590 15.841  -2.033  1.00 52.97  ? 1071 HOH   A O    1 
HETATM 3279 O  O    . HOH   C 3 .   ? -40.250 12.311  -22.048 1.00 62.85  ? 1072 HOH   A O    1 
HETATM 3280 O  O    . HOH   C 3 .   ? -28.518 -6.053  -21.141 1.00 61.66  ? 1073 HOH   A O    1 
HETATM 3281 O  O    . HOH   C 3 .   ? -30.688 30.513  -24.130 1.00 53.79  ? 1074 HOH   A O    1 
HETATM 3282 O  O    . HOH   C 3 .   ? -51.150 34.628  4.237   1.00 48.69  ? 1075 HOH   A O    1 
HETATM 3283 O  O    . HOH   C 3 .   ? -45.849 15.473  2.526   1.00 52.04  ? 1076 HOH   A O    1 
HETATM 3284 O  O    . HOH   C 3 .   ? -13.739 15.853  -46.584 1.00 92.96  ? 1077 HOH   A O    1 
HETATM 3285 O  O    . HOH   C 3 .   ? -47.206 14.751  0.356   1.00 51.59  ? 1078 HOH   A O    1 
HETATM 3286 O  O    . HOH   C 3 .   ? -39.450 9.702   -22.615 1.00 60.59  ? 1079 HOH   A O    1 
HETATM 3287 O  O    . HOH   C 3 .   ? -14.613 -2.644  -11.105 1.00 64.60  ? 1080 HOH   A O    1 
HETATM 3288 O  O    . HOH   C 3 .   ? -25.054 -6.588  -45.786 1.00 72.42  ? 1081 HOH   A O    1 
HETATM 3289 O  O    . HOH   C 3 .   ? 8.775   35.033  -8.485  1.00 70.04  ? 1082 HOH   A O    1 
HETATM 3290 O  O    . HOH   C 3 .   ? -35.895 20.660  -41.679 1.00 135.24 ? 1083 HOH   A O    1 
HETATM 3291 O  O    . HOH   C 3 .   ? -41.372 28.685  -3.619  1.00 95.92  ? 1084 HOH   A O    1 
HETATM 3292 O  O    . HOH   C 3 .   ? -33.095 30.191  -36.400 1.00 64.58  ? 1085 HOH   A O    1 
HETATM 3293 O  O    . HOH   C 3 .   ? 2.123   16.687  -2.622  1.00 91.87  ? 1086 HOH   A O    1 
HETATM 3294 O  O    . HOH   C 3 .   ? -36.865 5.811   -40.350 1.00 69.87  ? 1087 HOH   A O    1 
HETATM 3295 O  O    . HOH   C 3 .   ? -48.812 34.423  5.519   1.00 39.94  ? 1088 HOH   A O    1 
HETATM 3296 O  O    . HOH   C 3 .   ? 9.573   43.737  -16.514 1.00 73.53  ? 1089 HOH   A O    1 
HETATM 3297 O  O    . HOH   C 3 .   ? -47.572 34.514  -4.847  1.00 92.72  ? 1090 HOH   A O    1 
HETATM 3298 O  O    . HOH   C 3 .   ? -1.942  40.226  -9.160  1.00 70.10  ? 1091 HOH   A O    1 
HETATM 3299 O  O    . HOH   C 3 .   ? -40.438 12.418  -34.197 1.00 53.30  ? 1092 HOH   A O    1 
HETATM 3300 O  O    . HOH   C 3 .   ? -30.799 11.380  -48.180 1.00 73.14  ? 1093 HOH   A O    1 
HETATM 3301 O  O    . HOH   C 3 .   ? 14.229  26.757  -20.451 1.00 74.37  ? 1094 HOH   A O    1 
HETATM 3302 O  O    . HOH   C 3 .   ? -19.454 -1.242  -32.080 1.00 64.99  ? 1095 HOH   A O    1 
HETATM 3303 O  O    . HOH   C 3 .   ? -49.370 32.736  -17.043 1.00 79.26  ? 1096 HOH   A O    1 
HETATM 3304 O  O    . HOH   C 3 .   ? 8.947   22.366  -5.915  1.00 66.97  ? 1097 HOH   A O    1 
HETATM 3305 O  O    . HOH   C 3 .   ? -39.378 31.816  -29.272 1.00 77.09  ? 1098 HOH   A O    1 
HETATM 3306 O  O    . HOH   C 3 .   ? -18.910 -6.664  -30.102 1.00 75.07  ? 1099 HOH   A O    1 
HETATM 3307 O  O    . HOH   C 3 .   ? 11.871  25.558  -5.632  1.00 102.64 ? 1100 HOH   A O    1 
HETATM 3308 O  O    . HOH   C 3 .   ? -14.916 24.727  -39.280 1.00 74.61  ? 1101 HOH   A O    1 
HETATM 3309 O  O    . HOH   C 3 .   ? -30.418 -5.498  -27.111 1.00 68.82  ? 1102 HOH   A O    1 
HETATM 3310 O  O    . HOH   C 3 .   ? 16.337  29.334  -11.398 1.00 96.41  ? 1103 HOH   A O    1 
HETATM 3311 O  O    . HOH   C 3 .   ? -13.069 5.078   -20.932 1.00 70.18  ? 1104 HOH   A O    1 
HETATM 3312 O  O    . HOH   C 3 .   ? -11.824 5.009   -18.715 1.00 69.09  ? 1105 HOH   A O    1 
HETATM 3313 O  O    . HOH   C 3 .   ? -5.960  34.953  -2.284  1.00 62.46  ? 1106 HOH   A O    1 
HETATM 3314 O  O    . HOH   C 3 .   ? 17.418  27.952  -4.333  1.00 93.84  ? 1107 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 1   ? 1.9090 1.0010 1.3059 0.0262  -0.5075 0.1279  519 SER A N   
2    C CA  . SER A 1   ? 1.7988 0.9369 1.2441 0.0151  -0.4794 0.1237  519 SER A CA  
3    C C   . SER A 1   ? 1.6771 0.8871 1.2177 0.0433  -0.4890 0.0948  519 SER A C   
4    O O   . SER A 1   ? 1.7290 0.9440 1.2935 0.0729  -0.5240 0.0844  519 SER A O   
5    C CB  . SER A 1   ? 1.7662 0.9388 1.1889 -0.0109 -0.4437 0.1287  519 SER A CB  
6    O OG  . SER A 1   ? 1.6587 0.9007 1.1440 -0.0247 -0.4044 0.1150  519 SER A OG  
7    N N   . ARG A 2   ? 1.4821 0.7575 1.0818 0.0320  -0.4529 0.0804  520 ARG A N   
8    C CA  . ARG A 2   ? 1.3430 0.6916 1.0325 0.0542  -0.4527 0.0546  520 ARG A CA  
9    C C   . ARG A 2   ? 1.2840 0.6994 1.0045 0.0473  -0.4398 0.0444  520 ARG A C   
10   O O   . ARG A 2   ? 1.2643 0.6917 0.9612 0.0213  -0.4089 0.0498  520 ARG A O   
11   C CB  . ARG A 2   ? 1.2473 0.6188 0.9767 0.0477  -0.4236 0.0447  520 ARG A CB  
12   C CG  . ARG A 2   ? 1.2995 0.6017 1.0019 0.0557  -0.4389 0.0507  520 ARG A CG  
13   C CD  . ARG A 2   ? 1.2468 0.5754 0.9929 0.0543  -0.4154 0.0354  520 ARG A CD  
14   N NE  . ARG A 2   ? 1.3048 0.5593 1.0216 0.0634  -0.4338 0.0384  520 ARG A NE  
15   C CZ  . ARG A 2   ? 1.3658 0.5599 1.0319 0.0327  -0.4269 0.0556  520 ARG A CZ  
16   N NH1 . ARG A 2   ? 1.3659 0.5743 1.0101 -0.0071 -0.3989 0.0718  520 ARG A NH1 
17   N NH2 . ARG A 2   ? 1.4120 0.5465 1.0538 0.0405  -0.4436 0.0547  520 ARG A NH2 
18   N N   . ASP A 3   ? 1.2147 0.6734 0.9893 0.0705  -0.4641 0.0301  521 ASP A N   
19   C CA  . ASP A 3   ? 1.0927 0.6168 0.9078 0.0625  -0.4529 0.0184  521 ASP A CA  
20   C C   . ASP A 3   ? 0.9802 0.5673 0.8588 0.0557  -0.4144 0.0044  521 ASP A C   
21   O O   . ASP A 3   ? 0.9645 0.5427 0.8502 0.0564  -0.3971 0.0034  521 ASP A O   
22   C CB  . ASP A 3   ? 1.1106 0.6630 0.9675 0.0848  -0.4934 0.0099  521 ASP A CB  
23   C CG  . ASP A 3   ? 1.0921 0.6847 1.0270 0.1151  -0.5055 -0.0027 521 ASP A CG  
24   O OD1 . ASP A 3   ? 1.0740 0.6672 1.0253 0.1203  -0.4829 -0.0070 521 ASP A OD1 
25   O OD2 . ASP A 3   ? 1.0968 0.7218 1.0770 0.1348  -0.5387 -0.0088 521 ASP A OD2 
26   N N   . TYR A 4   ? 0.8627 0.5091 0.7838 0.0486  -0.4029 -0.0063 522 TYR A N   
27   C CA  . TYR A 4   ? 0.7976 0.4995 0.7706 0.0412  -0.3662 -0.0176 522 TYR A CA  
28   C C   . TYR A 4   ? 0.7723 0.5074 0.8092 0.0652  -0.3678 -0.0294 522 TYR A C   
29   O O   . TYR A 4   ? 0.7553 0.5004 0.8058 0.0636  -0.3411 -0.0347 522 TYR A O   
30   C CB  . TYR A 4   ? 0.7688 0.5203 0.7712 0.0291  -0.3570 -0.0253 522 TYR A CB  
31   C CG  . TYR A 4   ? 0.7778 0.5872 0.8373 0.0251  -0.3238 -0.0364 522 TYR A CG  
32   C CD1 . TYR A 4   ? 0.8710 0.6753 0.9111 0.0113  -0.2896 -0.0348 522 TYR A CD1 
33   C CD2 . TYR A 4   ? 0.7807 0.6510 0.9137 0.0348  -0.3270 -0.0471 522 TYR A CD2 
34   C CE1 . TYR A 4   ? 0.8690 0.7207 0.9542 0.0090  -0.2619 -0.0445 522 TYR A CE1 
35   C CE2 . TYR A 4   ? 0.7833 0.7019 0.9607 0.0311  -0.2954 -0.0554 522 TYR A CE2 
36   C CZ  . TYR A 4   ? 0.8352 0.7408 0.9848 0.0192  -0.2641 -0.0545 522 TYR A CZ  
37   O OH  . TYR A 4   ? 0.8077 0.7563 0.9946 0.0167  -0.2353 -0.0623 522 TYR A OH  
38   N N   . LYS A 5   ? 0.7716 0.5254 0.8477 0.0894  -0.3993 -0.0341 523 LYS A N   
39   C CA  . LYS A 5   ? 0.7901 0.5816 0.9290 0.1177  -0.3988 -0.0463 523 LYS A CA  
40   C C   . LYS A 5   ? 0.8261 0.5585 0.9281 0.1316  -0.3994 -0.0446 523 LYS A C   
41   O O   . LYS A 5   ? 0.7811 0.5298 0.9080 0.1415  -0.3778 -0.0553 523 LYS A O   
42   C CB  . LYS A 5   ? 0.7484 0.5741 0.9381 0.1425  -0.4351 -0.0499 523 LYS A CB  
43   C CG  . LYS A 5   ? 0.7314 0.6065 0.9918 0.1762  -0.4318 -0.0629 523 LYS A CG  
44   C CD  . LYS A 5   ? 0.7445 0.6660 1.0638 0.1984  -0.4647 -0.0653 523 LYS A CD  
45   C CE  . LYS A 5   ? 0.7358 0.7086 1.1174 0.2310  -0.4486 -0.0779 523 LYS A CE  
46   N NZ  . LYS A 5   ? 0.7431 0.7804 1.1865 0.2419  -0.4593 -0.0793 523 LYS A NZ  
47   N N   . ARG A 6   ? 0.8631 0.5208 0.9000 0.1317  -0.4253 -0.0309 524 ARG A N   
48   C CA  . ARG A 6   ? 0.9135 0.5033 0.9080 0.1399  -0.4289 -0.0269 524 ARG A CA  
49   C C   . ARG A 6   ? 0.9059 0.4799 0.8711 0.1095  -0.3932 -0.0235 524 ARG A C   
50   O O   . ARG A 6   ? 0.9162 0.4642 0.8766 0.1161  -0.3860 -0.0290 524 ARG A O   
51   C CB  . ARG A 6   ? 0.9908 0.5001 0.9171 0.1432  -0.4651 -0.0094 524 ARG A CB  
52   C CG  . ARG A 6   ? 1.0441 0.5333 0.9870 0.1860  -0.5046 -0.0142 524 ARG A CG  
53   C CD  . ARG A 6   ? 1.0411 0.6197 1.0733 0.2121  -0.5130 -0.0301 524 ARG A CD  
54   N NE  . ARG A 6   ? 1.0061 0.6133 1.0428 0.1980  -0.5284 -0.0246 524 ARG A NE  
55   C CZ  . ARG A 6   ? 1.0106 0.6928 1.1175 0.2084  -0.5343 -0.0353 524 ARG A CZ  
56   N NH1 . ARG A 6   ? 0.9879 0.7303 1.1677 0.2346  -0.5234 -0.0503 524 ARG A NH1 
57   N NH2 . ARG A 6   ? 1.0047 0.7002 1.1059 0.1915  -0.5491 -0.0305 524 ARG A NH2 
58   N N   . LYS A 7   ? 0.8883 0.4776 0.8342 0.0778  -0.3722 -0.0154 525 LYS A N   
59   C CA  . LYS A 7   ? 0.8771 0.4652 0.8063 0.0501  -0.3382 -0.0124 525 LYS A CA  
60   C C   . LYS A 7   ? 0.8092 0.4521 0.7955 0.0579  -0.3144 -0.0310 525 LYS A C   
61   O O   . LYS A 7   ? 0.8053 0.4300 0.7818 0.0502  -0.3002 -0.0333 525 LYS A O   
62   C CB  . LYS A 7   ? 0.9771 0.5804 0.8811 0.0219  -0.3199 -0.0025 525 LYS A CB  
63   C CG  . LYS A 7   ? 1.0340 0.5741 0.8627 0.0046  -0.3282 0.0195  525 LYS A CG  
64   C CD  . LYS A 7   ? 1.0034 0.5654 0.8095 -0.0189 -0.3031 0.0260  525 LYS A CD  
65   C CE  . LYS A 7   ? 1.1051 0.6090 0.8327 -0.0354 -0.3056 0.0488  525 LYS A CE  
66   N NZ  . LYS A 7   ? 1.0962 0.6243 0.8012 -0.0537 -0.2767 0.0533  525 LYS A NZ  
67   N N   . TYR A 8   ? 0.7950 0.5036 0.8389 0.0716  -0.3106 -0.0434 526 TYR A N   
68   C CA  . TYR A 8   ? 0.7460 0.5075 0.8392 0.0787  -0.2853 -0.0591 526 TYR A CA  
69   C C   . TYR A 8   ? 0.7365 0.4762 0.8377 0.1070  -0.2923 -0.0703 526 TYR A C   
70   O O   . TYR A 8   ? 0.7291 0.4674 0.8289 0.1050  -0.2730 -0.0788 526 TYR A O   
71   C CB  . TYR A 8   ? 0.7203 0.5545 0.8736 0.0858  -0.2811 -0.0668 526 TYR A CB  
72   C CG  . TYR A 8   ? 0.7283 0.6170 0.9264 0.0901  -0.2512 -0.0799 526 TYR A CG  
73   C CD1 . TYR A 8   ? 0.7739 0.7005 1.0219 0.1203  -0.2507 -0.0924 526 TYR A CD1 
74   C CD2 . TYR A 8   ? 0.6972 0.5993 0.8850 0.0660  -0.2228 -0.0792 526 TYR A CD2 
75   C CE1 . TYR A 8   ? 0.8034 0.7771 1.0846 0.1244  -0.2208 -0.1030 526 TYR A CE1 
76   C CE2 . TYR A 8   ? 0.7439 0.6898 0.9646 0.0701  -0.1969 -0.0898 526 TYR A CE2 
77   C CZ  . TYR A 8   ? 0.8327 0.8126 1.0972 0.0984  -0.1951 -0.1013 526 TYR A CZ  
78   O OH  . TYR A 8   ? 0.8896 0.9106 1.1794 0.1026  -0.1669 -0.1105 526 TYR A OH  
79   N N   . GLU A 9   ? 0.7701 0.4898 0.8767 0.1361  -0.3221 -0.0716 527 GLU A N   
80   C CA  . GLU A 9   ? 0.7997 0.4887 0.9062 0.1687  -0.3318 -0.0833 527 GLU A CA  
81   C C   . GLU A 9   ? 0.8660 0.4724 0.9076 0.1526  -0.3346 -0.0769 527 GLU A C   
82   O O   . GLU A 9   ? 0.8650 0.4537 0.9013 0.1621  -0.3254 -0.0894 527 GLU A O   
83   C CB  . GLU A 9   ? 0.8465 0.5249 0.9671 0.2041  -0.3672 -0.0837 527 GLU A CB  
84   C CG  . GLU A 9   ? 0.8496 0.6172 1.0475 0.2231  -0.3669 -0.0915 527 GLU A CG  
85   C CD  . GLU A 9   ? 0.9693 0.7285 1.1798 0.2511  -0.4078 -0.0874 527 GLU A CD  
86   O OE1 . GLU A 9   ? 0.9738 0.8081 1.2534 0.2668  -0.4130 -0.0925 527 GLU A OE1 
87   O OE2 . GLU A 9   ? 1.0447 0.7224 1.1965 0.2564  -0.4361 -0.0779 527 GLU A OE2 
88   N N   . PHE A 10  ? 0.9100 0.4639 0.8996 0.1268  -0.3477 -0.0568 528 PHE A N   
89   C CA  . PHE A 10  ? 0.9310 0.4127 0.8628 0.1020  -0.3482 -0.0461 528 PHE A CA  
90   C C   . PHE A 10  ? 0.8825 0.3948 0.8242 0.0757  -0.3155 -0.0511 528 PHE A C   
91   O O   . PHE A 10  ? 0.9081 0.3767 0.8250 0.0669  -0.3152 -0.0536 528 PHE A O   
92   C CB  . PHE A 10  ? 1.0082 0.4446 0.8873 0.0755  -0.3603 -0.0207 528 PHE A CB  
93   C CG  . PHE A 10  ? 1.1191 0.4823 0.9407 0.0459  -0.3615 -0.0047 528 PHE A CG  
94   C CD1 . PHE A 10  ? 1.1999 0.4784 0.9810 0.0586  -0.3902 -0.0010 528 PHE A CD1 
95   C CD2 . PHE A 10  ? 1.1265 0.5059 0.9359 0.0049  -0.3349 0.0077  528 PHE A CD2 
96   C CE1 . PHE A 10  ? 1.2501 0.4587 0.9792 0.0261  -0.3929 0.0161  528 PHE A CE1 
97   C CE2 . PHE A 10  ? 1.1464 0.4664 0.9108 -0.0263 -0.3357 0.0248  528 PHE A CE2 
98   C CZ  . PHE A 10  ? 1.2160 0.4493 0.9399 -0.0182 -0.3650 0.0298  528 PHE A CZ  
99   N N   . PHE A 11  ? 0.8298 0.4138 0.8062 0.0632  -0.2909 -0.0529 529 PHE A N   
100  C CA  . PHE A 11  ? 0.7689 0.3853 0.7557 0.0406  -0.2617 -0.0571 529 PHE A CA  
101  C C   . PHE A 11  ? 0.7810 0.4150 0.7943 0.0635  -0.2531 -0.0789 529 PHE A C   
102  O O   . PHE A 11  ? 0.8101 0.4221 0.8064 0.0513  -0.2461 -0.0832 529 PHE A O   
103  C CB  . PHE A 11  ? 0.7201 0.4006 0.7321 0.0258  -0.2408 -0.0535 529 PHE A CB  
104  C CG  . PHE A 11  ? 0.6800 0.4047 0.7128 0.0122  -0.2119 -0.0609 529 PHE A CG  
105  C CD1 . PHE A 11  ? 0.7366 0.4449 0.7456 -0.0157 -0.2010 -0.0528 529 PHE A CD1 
106  C CD2 . PHE A 11  ? 0.6641 0.4488 0.7416 0.0263  -0.1965 -0.0743 529 PHE A CD2 
107  C CE1 . PHE A 11  ? 0.7111 0.4603 0.7394 -0.0259 -0.1781 -0.0596 529 PHE A CE1 
108  C CE2 . PHE A 11  ? 0.6514 0.4710 0.7419 0.0150  -0.1720 -0.0799 529 PHE A CE2 
109  C CZ  . PHE A 11  ? 0.6669 0.4680 0.7322 -0.0095 -0.1642 -0.0732 529 PHE A CZ  
110  N N   . ARG A 12  ? 0.7597 0.4344 0.8141 0.0969  -0.2537 -0.0925 530 ARG A N   
111  C CA  . ARG A 12  ? 0.7882 0.4833 0.8646 0.1225  -0.2412 -0.1132 530 ARG A CA  
112  C C   . ARG A 12  ? 0.8429 0.4629 0.8804 0.1405  -0.2603 -0.1220 530 ARG A C   
113  O O   . ARG A 12  ? 0.8475 0.4597 0.8773 0.1489  -0.2501 -0.1374 530 ARG A O   
114  C CB  . ARG A 12  ? 0.8263 0.5858 0.9589 0.1546  -0.2365 -0.1231 530 ARG A CB  
115  C CG  . ARG A 12  ? 0.8354 0.6651 1.0071 0.1363  -0.2203 -0.1158 530 ARG A CG  
116  C CD  . ARG A 12  ? 0.8742 0.7363 1.0494 0.1150  -0.1896 -0.1187 530 ARG A CD  
117  N NE  . ARG A 12  ? 0.9299 0.8143 1.1212 0.1384  -0.1719 -0.1358 530 ARG A NE  
118  C CZ  . ARG A 12  ? 0.9161 0.8399 1.1189 0.1291  -0.1446 -0.1402 530 ARG A CZ  
119  N NH1 . ARG A 12  ? 0.8380 0.7832 1.0414 0.0982  -0.1334 -0.1293 530 ARG A NH1 
120  N NH2 . ARG A 12  ? 0.9761 0.9147 1.1851 0.1529  -0.1286 -0.1556 530 ARG A NH2 
121  N N   . ARG A 13  ? 0.8484 0.4061 0.8553 0.1472  -0.2900 -0.1128 531 ARG A N   
122  C CA  A ARG A 13  ? 0.9956 0.4716 0.9608 0.1659  -0.3117 -0.1215 531 ARG A CA  
123  C CA  B ARG A 13  ? 0.9975 0.4713 0.9613 0.1650  -0.3126 -0.1206 531 ARG A CA  
124  C C   . ARG A 13  ? 1.0696 0.4917 0.9900 0.1288  -0.3110 -0.1161 531 ARG A C   
125  O O   . ARG A 13  ? 1.1958 0.5618 1.0865 0.1414  -0.3217 -0.1299 531 ARG A O   
126  C CB  A ARG A 13  ? 1.0692 0.4866 1.0094 0.1830  -0.3461 -0.1112 531 ARG A CB  
127  C CB  B ARG A 13  ? 1.0694 0.4826 1.0049 0.1764  -0.3467 -0.1077 531 ARG A CB  
128  C CG  A ARG A 13  ? 1.1385 0.4885 1.0252 0.1437  -0.3622 -0.0858 531 ARG A CG  
129  C CG  B ARG A 13  ? 1.0822 0.5175 1.0515 0.2282  -0.3610 -0.1197 531 ARG A CG  
130  C CD  A ARG A 13  ? 1.2085 0.5272 1.0806 0.1599  -0.3914 -0.0725 531 ARG A CD  
131  C CD  B ARG A 13  ? 1.1422 0.5081 1.0683 0.2380  -0.3947 -0.1083 531 ARG A CD  
132  N NE  A ARG A 13  ? 1.2887 0.5251 1.0954 0.1392  -0.4111 -0.0543 531 ARG A NE  
133  N NE  B ARG A 13  ? 1.2290 0.5785 1.1476 0.2766  -0.4014 -0.1254 531 ARG A NE  
134  C CZ  A ARG A 13  ? 1.3274 0.5308 1.1048 0.1418  -0.4339 -0.0380 531 ARG A CZ  
135  C CZ  B ARG A 13  ? 1.3472 0.6191 1.2074 0.2729  -0.4162 -0.1242 531 ARG A CZ  
136  N NH1 A ARG A 13  ? 1.2982 0.5415 1.1069 0.1647  -0.4436 -0.0384 531 ARG A NH1 
137  N NH1 B ARG A 13  ? 1.3892 0.5999 1.1982 0.2294  -0.4242 -0.1051 531 ARG A NH1 
138  N NH2 A ARG A 13  ? 1.3784 0.5110 1.0956 0.1204  -0.4478 -0.0211 531 ARG A NH2 
139  N NH2 B ARG A 13  ? 1.3992 0.6576 1.2534 0.3118  -0.4221 -0.1413 531 ARG A NH2 
140  N N   . LYS A 14  ? 1.0220 0.4616 0.9382 0.0843  -0.2993 -0.0970 532 LYS A N   
141  C CA  . LYS A 14  ? 1.0102 0.4143 0.8964 0.0462  -0.2974 -0.0902 532 LYS A CA  
142  C C   . LYS A 14  ? 0.9906 0.4465 0.9008 0.0402  -0.2730 -0.1047 532 LYS A C   
143  O O   . LYS A 14  ? 1.0763 0.4971 0.9633 0.0210  -0.2778 -0.1079 532 LYS A O   
144  C CB  . LYS A 14  ? 0.9472 0.3508 0.8193 0.0030  -0.2937 -0.0620 532 LYS A CB  
145  C CG  . LYS A 14  ? 1.0057 0.3331 0.8331 -0.0021 -0.3207 -0.0433 532 LYS A CG  
146  C CD  . LYS A 14  ? 1.0515 0.3817 0.8607 -0.0462 -0.3110 -0.0147 532 LYS A CD  
147  C CE  . LYS A 14  ? 1.1263 0.3684 0.8797 -0.0609 -0.3360 0.0069  532 LYS A CE  
148  N NZ  . LYS A 14  ? 1.1032 0.3478 0.8365 -0.1073 -0.3218 0.0362  532 LYS A NZ  
149  N N   . LEU A 15  ? 0.9716 0.5069 0.9258 0.0548  -0.2494 -0.1125 533 LEU A N   
150  C CA  . LEU A 15  ? 0.9646 0.5469 0.9377 0.0535  -0.2264 -0.1260 533 LEU A CA  
151  C C   . LEU A 15  ? 1.1041 0.6555 1.0619 0.0870  -0.2321 -0.1504 533 LEU A C   
152  O O   . LEU A 15  ? 1.1250 0.7208 1.1093 0.1196  -0.2165 -0.1654 533 LEU A O   
153  C CB  . LEU A 15  ? 0.8792 0.5462 0.8991 0.0605  -0.2015 -0.1258 533 LEU A CB  
154  C CG  . LEU A 15  ? 0.8408 0.5614 0.8780 0.0430  -0.1759 -0.1274 533 LEU A CG  
155  C CD1 . LEU A 15  ? 0.8155 0.5263 0.8369 0.0024  -0.1760 -0.1111 533 LEU A CD1 
156  C CD2 . LEU A 15  ? 0.8036 0.5944 0.8825 0.0504  -0.1564 -0.1254 533 LEU A CD2 
157  N N   . LYS A 16  ? 1.2126 0.6868 1.1257 0.0789  -0.2539 -0.1543 534 LYS A N   
158  C CA  . LYS A 16  ? 1.2629 0.6900 1.1486 0.1148  -0.2643 -0.1791 534 LYS A CA  
159  C C   . LYS A 16  ? 1.3104 0.7741 1.1998 0.1210  -0.2434 -0.1968 534 LYS A C   
160  O O   . LYS A 16  ? 1.3054 0.8109 1.2088 0.0898  -0.2289 -0.1887 534 LYS A O   
161  C CB  . LYS A 16  ? 1.2973 0.6446 1.1326 0.0984  -0.2903 -0.1711 534 LYS A CB  
162  C CG  . LYS A 16  ? 1.3204 0.6314 1.1440 0.0823  -0.3089 -0.1474 534 LYS A CG  
163  C CD  . LYS A 16  ? 1.3907 0.6776 1.2076 0.1270  -0.3226 -0.1544 534 LYS A CD  
164  C CE  . LYS A 16  ? 1.4505 0.6853 1.2397 0.1108  -0.3460 -0.1310 534 LYS A CE  
165  N NZ  . LYS A 16  ? 1.5198 0.7358 1.3049 0.1562  -0.3614 -0.1381 534 LYS A NZ  
166  N N   . LYS A 17  ? 1.4116 0.8596 1.2850 0.1638  -0.2412 -0.2200 535 LYS A N   
167  C CA  . LYS A 17  ? 1.5030 0.9879 1.3773 0.1808  -0.2179 -0.2388 535 LYS A CA  
168  C C   . LYS A 17  ? 1.6060 1.0535 1.4373 0.1550  -0.2271 -0.2412 535 LYS A C   
169  O O   . LYS A 17  ? 1.7560 1.1429 1.5521 0.1392  -0.2511 -0.2345 535 LYS A O   
170  C CB  . LYS A 17  ? 1.5668 1.0647 1.4408 0.2341  -0.2051 -0.2557 535 LYS A CB  
171  C CG  . LYS A 17  ? 1.5515 1.1054 1.4352 0.2558  -0.1723 -0.2710 535 LYS A CG  
172  C CD  . LYS A 17  ? 1.5644 1.1454 1.4586 0.3059  -0.1549 -0.2822 535 LYS A CD  
173  C CE  . LYS A 17  ? 1.5397 1.1387 1.4085 0.3250  -0.1286 -0.2970 535 LYS A CE  
174  N NZ  . LYS A 17  ? 1.4164 1.1047 1.3321 0.3314  -0.0912 -0.2954 535 LYS A NZ  
175  N N   . GLN A 18  ? 1.5379 1.0239 1.3734 0.1509  -0.2087 -0.2500 536 GLN A N   
176  C CA  . GLN A 18  ? 1.5406 1.0004 1.3385 0.1318  -0.2170 -0.2543 536 GLN A CA  
177  C C   . GLN A 18  ? 1.5616 1.0006 1.3206 0.1716  -0.2101 -0.2749 536 GLN A C   
178  O O   . GLN A 18  ? 1.5381 1.0178 1.3104 0.2087  -0.1837 -0.2863 536 GLN A O   
179  C CB  . GLN A 18  ? 1.5003 1.0113 1.3186 0.1081  -0.2030 -0.2522 536 GLN A CB  
180  C CG  . GLN A 18  ? 1.4976 1.0391 1.3519 0.0618  -0.2065 -0.2255 536 GLN A CG  
181  C CD  . GLN A 18  ? 1.6006 1.1127 1.4364 0.0221  -0.2290 -0.2192 536 GLN A CD  
182  O OE1 . GLN A 18  ? 1.6606 1.1624 1.4692 0.0244  -0.2326 -0.2299 536 GLN A OE1 
183  N NE2 . GLN A 18  ? 1.6114 1.1233 1.4665 -0.0151 -0.2392 -0.1962 536 GLN A NE2 
184  N N   . ASN A 19  ? 1.6158 0.9943 1.3282 0.1630  -0.2328 -0.2782 537 ASN A N   
185  C CA  . ASN A 19  ? 1.6604 1.0122 1.3277 0.1977  -0.2289 -0.2980 537 ASN A CA  
186  C C   . ASN A 19  ? 1.6806 1.0120 1.3109 0.1786  -0.2389 -0.3035 537 ASN A C   
187  O O   . ASN A 19  ? 1.7560 1.0660 1.3440 0.2067  -0.2345 -0.3203 537 ASN A O   
188  C CB  . ASN A 19  ? 1.7284 1.0155 1.3642 0.2186  -0.2500 -0.3022 537 ASN A CB  
189  C CG  . ASN A 19  ? 1.7432 0.9821 1.3763 0.1802  -0.2823 -0.2837 537 ASN A CG  
190  O OD1 . ASN A 19  ? 1.7057 0.9561 1.3554 0.1355  -0.2899 -0.2684 537 ASN A OD1 
191  N ND2 . ASN A 19  ? 1.7963 0.9835 1.4085 0.1976  -0.3002 -0.2837 537 ASN A ND2 
192  N N   . ASP A 20  ? 1.5997 0.9397 1.2454 0.1327  -0.2523 -0.2895 538 ASP A N   
193  C CA  . ASP A 20  ? 1.5643 0.9009 1.1863 0.1141  -0.2608 -0.2933 538 ASP A CA  
194  C C   . ASP A 20  ? 1.4567 0.8574 1.0969 0.1180  -0.2339 -0.2963 538 ASP A C   
195  O O   . ASP A 20  ? 1.4451 0.8580 1.0814 0.0936  -0.2419 -0.2933 538 ASP A O   
196  C CB  . ASP A 20  ? 1.5718 0.8927 1.2069 0.0627  -0.2890 -0.2749 538 ASP A CB  
197  C CG  . ASP A 20  ? 1.5060 0.8725 1.1971 0.0330  -0.2818 -0.2539 538 ASP A CG  
198  O OD1 . ASP A 20  ? 1.4643 0.8618 1.1801 0.0533  -0.2608 -0.2545 538 ASP A OD1 
199  O OD2 . ASP A 20  ? 1.4987 0.8729 1.2105 -0.0098 -0.2963 -0.2363 538 ASP A OD2 
200  N N   . ILE A 21  ? 1.4086 0.8518 1.0699 0.1483  -0.2030 -0.3012 539 ILE A N   
201  C CA  . ILE A 21  ? 1.3947 0.9005 1.0757 0.1523  -0.1751 -0.3018 539 ILE A CA  
202  C C   . ILE A 21  ? 1.4535 0.9700 1.1051 0.1964  -0.1466 -0.3169 539 ILE A C   
203  O O   . ILE A 21  ? 1.5291 1.0208 1.1645 0.2272  -0.1432 -0.3257 539 ILE A O   
204  C CB  . ILE A 21  ? 1.3447 0.9026 1.0852 0.1449  -0.1604 -0.2907 539 ILE A CB  
205  C CG1 . ILE A 21  ? 1.4058 0.9684 1.1645 0.1791  -0.1471 -0.2943 539 ILE A CG1 
206  C CG2 . ILE A 21  ? 1.3196 0.8691 1.0870 0.0996  -0.1857 -0.2730 539 ILE A CG2 
207  C CD1 . ILE A 21  ? 1.4512 1.0481 1.2041 0.2225  -0.1128 -0.3059 539 ILE A CD1 
208  N N   . PRO A 22  ? 1.4349 0.9893 1.0781 0.2003  -0.1248 -0.3186 540 PRO A N   
209  C CA  . PRO A 22  ? 1.4132 0.9971 1.0430 0.2394  -0.0875 -0.3263 540 PRO A CA  
210  C C   . PRO A 22  ? 1.2967 0.9315 0.9827 0.2576  -0.0621 -0.3210 540 PRO A C   
211  O O   . PRO A 22  ? 1.1969 0.8596 0.9311 0.2383  -0.0661 -0.3109 540 PRO A O   
212  C CB  . PRO A 22  ? 1.3813 1.0003 0.9999 0.2297  -0.0709 -0.3221 540 PRO A CB  
213  C CG  . PRO A 22  ? 1.3923 0.9835 1.0016 0.1913  -0.1075 -0.3178 540 PRO A CG  
214  C CD  . PRO A 22  ? 1.3814 0.9574 1.0292 0.1692  -0.1318 -0.3109 540 PRO A CD  
215  N N   . ASN A 23  ? 1.3250 0.9751 1.0085 0.2948  -0.0368 -0.3274 541 ASN A N   
216  C CA  . ASN A 23  ? 1.3367 1.0357 1.0810 0.3110  -0.0192 -0.3211 541 ASN A CA  
217  C C   . ASN A 23  ? 1.2616 1.0437 1.0554 0.3060  0.0153  -0.3087 541 ASN A C   
218  O O   . ASN A 23  ? 1.3089 1.1362 1.1641 0.3037  0.0205  -0.2996 541 ASN A O   
219  C CB  . ASN A 23  ? 1.4445 1.1386 1.1807 0.3515  -0.0061 -0.3304 541 ASN A CB  
220  C CG  . ASN A 23  ? 1.4470 1.1862 1.2490 0.3665  0.0023  -0.3232 541 ASN A CG  
221  O OD1 . ASN A 23  ? 1.4707 1.2733 1.3099 0.3891  0.0362  -0.3195 541 ASN A OD1 
222  N ND2 . ASN A 23  ? 1.4089 1.1190 1.2291 0.3499  -0.0295 -0.3185 541 ASN A ND2 
223  N N   . LYS A 24  ? 1.1724 0.9742 0.9402 0.3025  0.0369  -0.3066 542 LYS A N   
224  C CA  . LYS A 24  ? 1.0894 0.9636 0.8982 0.2917  0.0670  -0.2919 542 LYS A CA  
225  C C   . LYS A 24  ? 1.0166 0.8820 0.8138 0.2530  0.0506  -0.2814 542 LYS A C   
226  O O   . LYS A 24  ? 1.0407 0.8515 0.7801 0.2473  0.0282  -0.2923 542 LYS A O   
227  C CB  . LYS A 24  ? 1.1547 1.0680 0.9511 0.3098  0.1093  -0.2873 542 LYS A CB  
228  C CG  . LYS A 24  ? 1.2279 1.1754 1.0552 0.3405  0.1348  -0.2883 542 LYS A CG  
229  C CD  . LYS A 24  ? 1.2463 1.2025 1.1277 0.3484  0.1180  -0.2887 542 LYS A CD  
230  C CE  . LYS A 24  ? 1.3408 1.2921 1.2196 0.3851  0.1279  -0.2986 542 LYS A CE  
231  N NZ  . LYS A 24  ? 1.3384 1.3033 1.2714 0.3970  0.1135  -0.2971 542 LYS A NZ  
232  N N   . PHE A 25  ? 0.9209 0.8414 0.7760 0.2246  0.0600  -0.2578 543 PHE A N   
233  C CA  . PHE A 25  ? 0.8617 0.7903 0.7139 0.1911  0.0541  -0.2428 543 PHE A CA  
234  C C   . PHE A 25  ? 0.8613 0.8426 0.7247 0.1920  0.0916  -0.2289 543 PHE A C   
235  O O   . PHE A 25  ? 0.8160 0.8500 0.7369 0.1839  0.1093  -0.2134 543 PHE A O   
236  C CB  . PHE A 25  ? 0.8058 0.7461 0.7069 0.1576  0.0334  -0.2269 543 PHE A CB  
237  C CG  . PHE A 25  ? 0.7855 0.7432 0.6907 0.1288  0.0319  -0.2109 543 PHE A CG  
238  C CD1 . PHE A 25  ? 0.8185 0.7420 0.6811 0.1190  0.0116  -0.2160 543 PHE A CD1 
239  C CD2 . PHE A 25  ? 0.7440 0.7503 0.6945 0.1132  0.0485  -0.1916 543 PHE A CD2 
240  C CE1 . PHE A 25  ? 0.8025 0.7441 0.6707 0.0974  0.0092  -0.2018 543 PHE A CE1 
241  C CE2 . PHE A 25  ? 0.7284 0.7447 0.6782 0.0914  0.0464  -0.1783 543 PHE A CE2 
242  C CZ  . PHE A 25  ? 0.7501 0.7362 0.6601 0.0853  0.0274  -0.1833 543 PHE A CZ  
243  N N   . GLU A 26  ? 0.9183 0.8820 0.7239 0.2001  0.1015  -0.2335 544 GLU A N   
244  C CA  . GLU A 26  ? 0.9229 0.9272 0.7265 0.2011  0.1380  -0.2192 544 GLU A CA  
245  C C   . GLU A 26  ? 0.9062 0.9166 0.7138 0.1688  0.1295  -0.2003 544 GLU A C   
246  O O   . GLU A 26  ? 0.9649 0.9370 0.7375 0.1587  0.1014  -0.2050 544 GLU A O   
247  C CB  . GLU A 26  ? 0.9998 0.9771 0.7283 0.2313  0.1561  -0.2338 544 GLU A CB  
248  C CG  . GLU A 26  ? 1.0879 1.0972 0.8299 0.2607  0.1917  -0.2377 544 GLU A CG  
249  C CD  . GLU A 26  ? 1.2449 1.2225 0.9194 0.2781  0.2038  -0.2455 544 GLU A CD  
250  O OE1 . GLU A 26  ? 1.3212 1.2525 0.9621 0.2969  0.1857  -0.2648 544 GLU A OE1 
251  O OE2 . GLU A 26  ? 1.2841 1.2806 0.9365 0.2726  0.2302  -0.2319 544 GLU A OE2 
252  N N   . MET A 27  ? 0.8443 0.9025 0.6956 0.1533  0.1520  -0.1791 545 MET A N   
253  C CA  . MET A 27  ? 0.8934 0.9533 0.7384 0.1292  0.1493  -0.1613 545 MET A CA  
254  C C   . MET A 27  ? 0.8958 0.9932 0.7502 0.1257  0.1869  -0.1426 545 MET A C   
255  O O   . MET A 27  ? 0.9149 1.0567 0.8229 0.1242  0.2067  -0.1351 545 MET A O   
256  C CB  . MET A 27  ? 0.8788 0.9456 0.7717 0.1030  0.1247  -0.1521 545 MET A CB  
257  C CG  . MET A 27  ? 0.8794 0.9830 0.8394 0.0958  0.1301  -0.1456 545 MET A CG  
258  S SD  . MET A 27  ? 0.8325 0.9354 0.8310 0.0676  0.1024  -0.1356 545 MET A SD  
259  C CE  . MET A 27  ? 0.6365 0.7170 0.5923 0.0569  0.0935  -0.1282 545 MET A CE  
260  N N   . LYS A 28  ? 0.8903 0.9690 0.6922 0.1234  0.1950  -0.1341 546 LYS A N   
261  C CA  . LYS A 28  ? 0.9171 1.0215 0.7152 0.1164  0.2302  -0.1133 546 LYS A CA  
262  C C   . LYS A 28  ? 0.9068 1.0041 0.7139 0.0887  0.2177  -0.0936 546 LYS A C   
263  O O   . LYS A 28  ? 0.9520 1.0125 0.7234 0.0861  0.1912  -0.0965 546 LYS A O   
264  C CB  . LYS A 28  ? 1.0386 1.1197 0.7577 0.1371  0.2519  -0.1163 546 LYS A CB  
265  C CG  . LYS A 28  ? 1.2122 1.2818 0.8967 0.1718  0.2603  -0.1408 546 LYS A CG  
266  C CD  . LYS A 28  ? 1.3770 1.4007 1.0416 0.1793  0.2172  -0.1645 546 LYS A CD  
267  C CE  . LYS A 28  ? 1.6446 1.6230 1.2325 0.2106  0.2139  -0.1884 546 LYS A CE  
268  N NZ  . LYS A 28  ? 1.7716 1.7038 1.3457 0.2029  0.1644  -0.2034 546 LYS A NZ  
269  N N   . LEU A 29  ? 0.8296 0.9618 0.6855 0.0688  0.2348  -0.0743 547 LEU A N   
270  C CA  . LEU A 29  ? 0.7833 0.9047 0.6514 0.0437  0.2210  -0.0575 547 LEU A CA  
271  C C   . LEU A 29  ? 0.8075 0.9405 0.6703 0.0274  0.2504  -0.0325 547 LEU A C   
272  O O   . LEU A 29  ? 0.8600 1.0299 0.7402 0.0292  0.2831  -0.0258 547 LEU A O   
273  C CB  . LEU A 29  ? 0.7419 0.8830 0.6772 0.0294  0.2021  -0.0591 547 LEU A CB  
274  C CG  . LEU A 29  ? 0.7128 0.8500 0.6635 0.0427  0.1788  -0.0808 547 LEU A CG  
275  C CD1 . LEU A 29  ? 0.6677 0.8313 0.6837 0.0309  0.1696  -0.0797 547 LEU A CD1 
276  C CD2 . LEU A 29  ? 0.6869 0.7857 0.6023 0.0445  0.1490  -0.0889 547 LEU A CD2 
277  N N   . ARG A 30  ? 0.8181 0.9192 0.6563 0.0121  0.2386  -0.0179 548 ARG A N   
278  C CA  . ARG A 30  ? 0.8241 0.9253 0.6591 -0.0103 0.2591  0.0086  548 ARG A CA  
279  C C   . ARG A 30  ? 0.7329 0.8384 0.6209 -0.0348 0.2420  0.0169  548 ARG A C   
280  O O   . ARG A 30  ? 0.6545 0.7365 0.5440 -0.0328 0.2113  0.0077  548 ARG A O   
281  C CB  . ARG A 30  ? 0.9022 0.9519 0.6585 -0.0073 0.2568  0.0198  548 ARG A CB  
282  C CG  . ARG A 30  ? 0.9716 1.0078 0.6630 0.0183  0.2695  0.0102  548 ARG A CG  
283  C CD  . ARG A 30  ? 1.0622 1.0408 0.6759 0.0264  0.2503  0.0143  548 ARG A CD  
284  N NE  . ARG A 30  ? 1.0436 1.0031 0.6643 0.0343  0.2081  -0.0021 548 ARG A NE  
285  C CZ  . ARG A 30  ? 1.0400 0.9572 0.6096 0.0428  0.1827  -0.0012 548 ARG A CZ  
286  N NH1 . ARG A 30  ? 1.1064 0.9876 0.6065 0.0454  0.1930  0.0151  548 ARG A NH1 
287  N NH2 . ARG A 30  ? 0.9440 0.8566 0.5325 0.0490  0.1471  -0.0153 548 ARG A NH2 
288  N N   . ARG A 31  ? 0.7631 0.9003 0.6948 -0.0578 0.2616  0.0340  549 ARG A N   
289  C CA  . ARG A 31  ? 0.7372 0.8774 0.7188 -0.0815 0.2433  0.0399  549 ARG A CA  
290  C C   . ARG A 31  ? 0.6869 0.7681 0.6287 -0.0899 0.2196  0.0472  549 ARG A C   
291  O O   . ARG A 31  ? 0.6421 0.7096 0.6035 -0.0929 0.1931  0.0393  549 ARG A O   
292  C CB  . ARG A 31  ? 0.7944 0.9758 0.8251 -0.1087 0.2670  0.0601  549 ARG A CB  
293  C CG  . ARG A 31  ? 0.7602 1.0087 0.8589 -0.1019 0.2786  0.0503  549 ARG A CG  
294  C CD  . ARG A 31  ? 0.7806 1.0774 0.9363 -0.1316 0.3001  0.0724  549 ARG A CD  
295  N NE  . ARG A 31  ? 0.7797 1.1461 1.0071 -0.1223 0.3087  0.0631  549 ARG A NE  
296  C CZ  . ARG A 31  ? 0.8543 1.2722 1.0954 -0.1044 0.3434  0.0626  549 ARG A CZ  
297  N NH1 . ARG A 31  ? 0.8936 1.2987 1.0764 -0.0958 0.3737  0.0711  549 ARG A NH1 
298  N NH2 . ARG A 31  ? 0.8725 1.3530 1.1820 -0.0925 0.3477  0.0532  549 ARG A NH2 
299  N N   . ALA A 32  ? 0.7339 0.7775 0.6154 -0.0910 0.2290  0.0622  550 ALA A N   
300  C CA  . ALA A 32  ? 0.8056 0.7894 0.6452 -0.0943 0.2061  0.0695  550 ALA A CA  
301  C C   . ALA A 32  ? 0.8139 0.7791 0.6372 -0.0687 0.1767  0.0484  550 ALA A C   
302  O O   . ALA A 32  ? 0.8330 0.7619 0.6437 -0.0682 0.1538  0.0491  550 ALA A O   
303  C CB  . ALA A 32  ? 0.8460 0.7906 0.6185 -0.0978 0.2215  0.0907  550 ALA A CB  
304  N N   . THR A 33  ? 0.8295 0.8185 0.6533 -0.0474 0.1766  0.0301  551 THR A N   
305  C CA  . THR A 33  ? 0.8191 0.7971 0.6325 -0.0268 0.1494  0.0118  551 THR A CA  
306  C C   . THR A 33  ? 0.7537 0.7702 0.6138 -0.0200 0.1444  -0.0080 551 THR A C   
307  O O   . THR A 33  ? 0.6799 0.6981 0.5264 -0.0027 0.1338  -0.0234 551 THR A O   
308  C CB  . THR A 33  ? 0.8687 0.8205 0.6186 -0.0076 0.1457  0.0099  551 THR A CB  
309  O OG1 . THR A 33  ? 0.8851 0.8556 0.6200 -0.0009 0.1692  0.0065  551 THR A OG1 
310  C CG2 . THR A 33  ? 0.9200 0.8247 0.6173 -0.0118 0.1453  0.0303  551 THR A CG2 
311  N N   . VAL A 34  ? 0.7331 0.7771 0.6472 -0.0342 0.1487  -0.0075 552 VAL A N   
312  C CA  . VAL A 34  ? 0.6735 0.7507 0.6285 -0.0272 0.1452  -0.0241 552 VAL A CA  
313  C C   . VAL A 34  ? 0.5751 0.6429 0.5342 -0.0181 0.1181  -0.0382 552 VAL A C   
314  O O   . VAL A 34  ? 0.5785 0.6593 0.5489 -0.0078 0.1115  -0.0529 552 VAL A O   
315  C CB  . VAL A 34  ? 0.6456 0.7546 0.6572 -0.0441 0.1533  -0.0188 552 VAL A CB  
316  C CG1 . VAL A 34  ? 0.5993 0.6903 0.6262 -0.0598 0.1352  -0.0130 552 VAL A CG1 
317  C CG2 . VAL A 34  ? 0.5841 0.7249 0.6327 -0.0330 0.1510  -0.0349 552 VAL A CG2 
318  N N   . LEU A 35  ? 0.5434 0.5881 0.4926 -0.0211 0.1026  -0.0335 553 LEU A N   
319  C CA  . LEU A 35  ? 0.5471 0.5928 0.5074 -0.0134 0.0812  -0.0449 553 LEU A CA  
320  C C   . LEU A 35  ? 0.5786 0.6175 0.5092 0.0021  0.0702  -0.0530 553 LEU A C   
321  O O   . LEU A 35  ? 0.5172 0.5693 0.4623 0.0067  0.0589  -0.0653 553 LEU A O   
322  C CB  . LEU A 35  ? 0.6017 0.6289 0.5626 -0.0176 0.0701  -0.0389 553 LEU A CB  
323  C CG  . LEU A 35  ? 0.6525 0.6856 0.6229 -0.0078 0.0524  -0.0482 553 LEU A CG  
324  C CD1 . LEU A 35  ? 0.6444 0.7028 0.6511 -0.0124 0.0496  -0.0578 553 LEU A CD1 
325  C CD2 . LEU A 35  ? 0.6771 0.6889 0.6410 -0.0071 0.0455  -0.0430 553 LEU A CD2 
326  N N   . GLU A 36  ? 0.6646 0.6801 0.5517 0.0089  0.0708  -0.0456 554 GLU A N   
327  C CA  . GLU A 36  ? 0.7167 0.7249 0.5738 0.0234  0.0561  -0.0535 554 GLU A CA  
328  C C   . GLU A 36  ? 0.6849 0.7006 0.5327 0.0283  0.0623  -0.0650 554 GLU A C   
329  O O   . GLU A 36  ? 0.6880 0.7071 0.5362 0.0345  0.0446  -0.0781 554 GLU A O   
330  C CB  . GLU A 36  ? 0.8722 0.8488 0.6781 0.0315  0.0537  -0.0423 554 GLU A CB  
331  C CG  . GLU A 36  ? 1.0662 1.0350 0.8401 0.0469  0.0334  -0.0508 554 GLU A CG  
332  C CD  . GLU A 36  ? 1.2907 1.2415 1.0428 0.0586  0.0136  -0.0440 554 GLU A CD  
333  O OE1 . GLU A 36  ? 1.4113 1.3292 1.1199 0.0621  0.0196  -0.0303 554 GLU A OE1 
334  O OE2 . GLU A 36  ? 1.3336 1.3043 1.1128 0.0649  -0.0078 -0.0513 554 GLU A OE2 
335  N N   . ASP A 37  ? 0.6767 0.6949 0.5163 0.0257  0.0873  -0.0603 555 ASP A N   
336  C CA  . ASP A 37  ? 0.7075 0.7306 0.5335 0.0358  0.0960  -0.0727 555 ASP A CA  
337  C C   . ASP A 37  ? 0.6641 0.7056 0.5325 0.0352  0.0856  -0.0874 555 ASP A C   
338  O O   . ASP A 37  ? 0.7042 0.7365 0.5564 0.0454  0.0742  -0.1026 555 ASP A O   
339  C CB  . ASP A 37  ? 0.7309 0.7639 0.5497 0.0342  0.1295  -0.0631 555 ASP A CB  
340  C CG  . ASP A 37  ? 0.8505 0.8588 0.6173 0.0337  0.1416  -0.0467 555 ASP A CG  
341  O OD1 . ASP A 37  ? 0.8811 0.8615 0.6146 0.0381  0.1212  -0.0445 555 ASP A OD1 
342  O OD2 . ASP A 37  ? 0.8865 0.9046 0.6464 0.0289  0.1716  -0.0348 555 ASP A OD2 
343  N N   . SER A 38  ? 0.6133 0.6746 0.5308 0.0231  0.0869  -0.0830 556 SER A N   
344  C CA  . SER A 38  ? 0.5990 0.6726 0.5522 0.0220  0.0758  -0.0944 556 SER A CA  
345  C C   . SER A 38  ? 0.5276 0.5928 0.4810 0.0205  0.0491  -0.1010 556 SER A C   
346  O O   . SER A 38  ? 0.5224 0.5830 0.4788 0.0231  0.0360  -0.1131 556 SER A O   
347  C CB  . SER A 38  ? 0.5695 0.6633 0.5693 0.0096  0.0818  -0.0870 556 SER A CB  
348  O OG  . SER A 38  ? 0.6137 0.7217 0.6210 0.0063  0.1052  -0.0776 556 SER A OG  
349  N N   . TYR A 39  ? 0.5323 0.5955 0.4833 0.0165  0.0405  -0.0925 557 TYR A N   
350  C CA  . TYR A 39  ? 0.5215 0.5882 0.4812 0.0149  0.0177  -0.0964 557 TYR A CA  
351  C C   . TYR A 39  ? 0.5497 0.6031 0.4792 0.0223  0.0016  -0.1067 557 TYR A C   
352  O O   . TYR A 39  ? 0.5393 0.5959 0.4826 0.0171  -0.0167 -0.1148 557 TYR A O   
353  C CB  . TYR A 39  ? 0.4821 0.5511 0.4425 0.0155  0.0141  -0.0858 557 TYR A CB  
354  C CG  . TYR A 39  ? 0.5089 0.5910 0.4807 0.0172  -0.0069 -0.0881 557 TYR A CG  
355  C CD1 . TYR A 39  ? 0.4700 0.5732 0.4792 0.0084  -0.0130 -0.0893 557 TYR A CD1 
356  C CD2 . TYR A 39  ? 0.5357 0.6119 0.4822 0.0274  -0.0206 -0.0875 557 TYR A CD2 
357  C CE1 . TYR A 39  ? 0.4800 0.6047 0.5070 0.0081  -0.0292 -0.0891 557 TYR A CE1 
358  C CE2 . TYR A 39  ? 0.5368 0.6347 0.5031 0.0287  -0.0408 -0.0887 557 TYR A CE2 
359  C CZ  . TYR A 39  ? 0.5136 0.6391 0.5233 0.0183  -0.0435 -0.0890 557 TYR A CZ  
360  O OH  . TYR A 39  ? 0.5635 0.7196 0.6000 0.0178  -0.0606 -0.0881 557 TYR A OH  
361  N N   . ARG A 40  ? 0.6127 0.6476 0.4974 0.0328  0.0068  -0.1059 558 ARG A N   
362  C CA  A ARG A 40  ? 0.6414 0.6570 0.4875 0.0411  -0.0116 -0.1167 558 ARG A CA  
363  C CA  B ARG A 40  ? 0.6385 0.6547 0.4860 0.0408  -0.0123 -0.1168 558 ARG A CA  
364  C C   . ARG A 40  ? 0.6702 0.6735 0.5095 0.0435  -0.0136 -0.1324 558 ARG A C   
365  O O   . ARG A 40  ? 0.7216 0.7101 0.5473 0.0431  -0.0385 -0.1441 558 ARG A O   
366  C CB  A ARG A 40  ? 0.6972 0.6902 0.4874 0.0533  -0.0024 -0.1111 558 ARG A CB  
367  C CB  B ARG A 40  ? 0.6955 0.6892 0.4873 0.0530  -0.0057 -0.1114 558 ARG A CB  
368  C CG  A ARG A 40  ? 0.7516 0.7357 0.5179 0.0591  -0.0266 -0.1077 558 ARG A CG  
369  C CG  B ARG A 40  ? 0.7282 0.7224 0.5142 0.0555  -0.0205 -0.1010 558 ARG A CG  
370  C CD  A ARG A 40  ? 0.7294 0.7290 0.5237 0.0563  -0.0260 -0.0933 558 ARG A CD  
371  C CD  B ARG A 40  ? 0.7787 0.7499 0.5187 0.0633  -0.0038 -0.0879 558 ARG A CD  
372  N NE  A ARG A 40  ? 0.6876 0.7054 0.5053 0.0572  -0.0547 -0.0953 558 ARG A NE  
373  N NE  B ARG A 40  ? 0.8443 0.8023 0.5575 0.0730  -0.0252 -0.0817 558 ARG A NE  
374  C CZ  A ARG A 40  ? 0.6718 0.7019 0.5062 0.0623  -0.0602 -0.0855 558 ARG A CZ  
375  C CZ  B ARG A 40  ? 0.9324 0.8606 0.5932 0.0816  -0.0188 -0.0698 558 ARG A CZ  
376  N NH1 A ARG A 40  ? 0.6727 0.6890 0.4968 0.0651  -0.0415 -0.0735 558 ARG A NH1 
377  N NH1 B ARG A 40  ? 0.9771 0.8895 0.6094 0.0786  0.0115  -0.0615 558 ARG A NH1 
378  N NH2 A ARG A 40  ? 0.6488 0.7051 0.5111 0.0647  -0.0848 -0.0876 558 ARG A NH2 
379  N NH2 B ARG A 40  ? 0.9547 0.8702 0.5929 0.0932  -0.0426 -0.0649 558 ARG A NH2 
380  N N   . ARG A 41  ? 0.6463 0.6540 0.4948 0.0467  0.0105  -0.1330 559 ARG A N   
381  C CA  . ARG A 41  ? 0.6726 0.6653 0.5116 0.0549  0.0098  -0.1488 559 ARG A CA  
382  C C   . ARG A 41  ? 0.6764 0.6732 0.5559 0.0427  -0.0082 -0.1537 559 ARG A C   
383  O O   . ARG A 41  ? 0.7451 0.7172 0.6093 0.0432  -0.0293 -0.1671 559 ARG A O   
384  C CB  . ARG A 41  ? 0.7078 0.7116 0.5488 0.0654  0.0426  -0.1470 559 ARG A CB  
385  C CG  . ARG A 41  ? 0.7249 0.7144 0.5566 0.0805  0.0445  -0.1642 559 ARG A CG  
386  C CD  . ARG A 41  ? 0.8249 0.7776 0.5886 0.0990  0.0399  -0.1789 559 ARG A CD  
387  N NE  . ARG A 41  ? 0.8877 0.8213 0.6360 0.1187  0.0435  -0.1972 559 ARG A NE  
388  C CZ  . ARG A 41  ? 0.9464 0.8407 0.6735 0.1219  0.0146  -0.2149 559 ARG A CZ  
389  N NH1 . ARG A 41  ? 0.9302 0.8080 0.6557 0.1033  -0.0192 -0.2151 559 ARG A NH1 
390  N NH2 . ARG A 41  ? 0.9973 0.8689 0.7061 0.1439  0.0188  -0.2320 559 ARG A NH2 
391  N N   . ILE A 42  ? 0.6564 0.6793 0.5827 0.0308  -0.0014 -0.1424 560 ILE A N   
392  C CA  . ILE A 42  ? 0.6138 0.6386 0.5739 0.0196  -0.0143 -0.1445 560 ILE A CA  
393  C C   . ILE A 42  ? 0.5754 0.5994 0.5427 0.0051  -0.0405 -0.1438 560 ILE A C   
394  O O   . ILE A 42  ? 0.5846 0.5939 0.5586 -0.0038 -0.0582 -0.1498 560 ILE A O   
395  C CB  . ILE A 42  ? 0.5695 0.6192 0.5698 0.0124  0.0002  -0.1328 560 ILE A CB  
396  C CG1 . ILE A 42  ? 0.5565 0.6117 0.5609 0.0244  0.0212  -0.1350 560 ILE A CG1 
397  C CG2 . ILE A 42  ? 0.4985 0.5496 0.5279 -0.0013 -0.0142 -0.1308 560 ILE A CG2 
398  C CD1 . ILE A 42  ? 0.4426 0.5228 0.4809 0.0169  0.0351  -0.1224 560 ILE A CD1 
399  N N   . MET A 43  ? 0.5359 0.5760 0.5034 0.0025  -0.0441 -0.1357 561 MET A N   
400  C CA  . MET A 43  ? 0.5983 0.6484 0.5797 -0.0100 -0.0684 -0.1342 561 MET A CA  
401  C C   . MET A 43  ? 0.6485 0.6734 0.5944 -0.0072 -0.0920 -0.1464 561 MET A C   
402  O O   . MET A 43  ? 0.6864 0.7214 0.6472 -0.0200 -0.1165 -0.1457 561 MET A O   
403  C CB  . MET A 43  ? 0.6003 0.6804 0.5990 -0.0095 -0.0647 -0.1216 561 MET A CB  
404  C CG  . MET A 43  ? 0.6284 0.7280 0.6578 -0.0133 -0.0464 -0.1111 561 MET A CG  
405  S SD  . MET A 43  ? 0.5966 0.7059 0.6629 -0.0321 -0.0522 -0.1090 561 MET A SD  
406  C CE  . MET A 43  ? 0.5802 0.7246 0.6746 -0.0426 -0.0691 -0.1021 561 MET A CE  
407  N N   . GLY A 44  ? 0.6771 0.6707 0.5765 0.0090  -0.0857 -0.1574 562 GLY A N   
408  C CA  . GLY A 44  ? 0.6469 0.6087 0.5004 0.0146  -0.1091 -0.1705 562 GLY A CA  
409  C C   . GLY A 44  ? 0.6769 0.5984 0.5088 0.0142  -0.1242 -0.1874 562 GLY A C   
410  O O   . GLY A 44  ? 0.7201 0.6106 0.5179 0.0129  -0.1526 -0.1995 562 GLY A O   
411  N N   . VAL A 45  ? 0.6652 0.5828 0.5149 0.0159  -0.1088 -0.1888 563 VAL A N   
412  C CA  . VAL A 45  ? 0.7635 0.6346 0.5856 0.0219  -0.1214 -0.2060 563 VAL A CA  
413  C C   . VAL A 45  ? 0.8141 0.6637 0.6430 -0.0020 -0.1598 -0.2097 563 VAL A C   
414  O O   . VAL A 45  ? 0.7761 0.6584 0.6482 -0.0260 -0.1714 -0.1961 563 VAL A O   
415  C CB  . VAL A 45  ? 0.7866 0.6606 0.6322 0.0294  -0.1006 -0.2051 563 VAL A CB  
416  C CG1 . VAL A 45  ? 0.8249 0.7195 0.6634 0.0521  -0.0646 -0.2030 563 VAL A CG1 
417  C CG2 . VAL A 45  ? 0.7144 0.6198 0.6174 0.0065  -0.1013 -0.1885 563 VAL A CG2 
418  N N   . LYS A 46  ? 0.9131 0.7059 0.6975 0.0052  -0.1792 -0.2286 564 LYS A N   
419  C CA  . LYS A 46  ? 0.9943 0.7535 0.7774 -0.0191 -0.2188 -0.2339 564 LYS A CA  
420  C C   . LYS A 46  ? 1.0003 0.7750 0.8377 -0.0455 -0.2219 -0.2193 564 LYS A C   
421  O O   . LYS A 46  ? 0.9985 0.7982 0.8737 -0.0760 -0.2403 -0.2067 564 LYS A O   
422  C CB  . LYS A 46  ? 1.1513 0.8365 0.8669 -0.0002 -0.2350 -0.2589 564 LYS A CB  
423  C CG  . LYS A 46  ? 1.3165 0.9885 1.0137 -0.0146 -0.2637 -0.2581 564 LYS A CG  
424  C CD  . LYS A 46  ? 1.4439 1.1558 1.1459 -0.0166 -0.2666 -0.2527 564 LYS A CD  
425  C CE  . LYS A 46  ? 1.5717 1.2784 1.2832 -0.0423 -0.3011 -0.2473 564 LYS A CE  
426  N NZ  . LYS A 46  ? 1.5233 1.2767 1.2506 -0.0449 -0.3065 -0.2394 564 LYS A NZ  
427  N N   . ARG A 47  ? 0.9828 0.7466 0.8254 -0.0334 -0.2032 -0.2195 565 ARG A N   
428  C CA  . ARG A 47  ? 0.9463 0.7132 0.8273 -0.0535 -0.2049 -0.2065 565 ARG A CA  
429  C C   . ARG A 47  ? 0.7981 0.6047 0.7067 -0.0374 -0.1690 -0.1968 565 ARG A C   
430  O O   . ARG A 47  ? 0.7284 0.5352 0.6170 -0.0080 -0.1481 -0.2061 565 ARG A O   
431  C CB  . ARG A 47  ? 1.0102 0.7042 0.8569 -0.0517 -0.2276 -0.2202 565 ARG A CB  
432  C CG  . ARG A 47  ? 1.0758 0.7324 0.8940 -0.0667 -0.2580 -0.2250 565 ARG A CG  
433  C CD  . ARG A 47  ? 1.1895 0.7935 0.9965 -0.0762 -0.2732 -0.2218 565 ARG A CD  
434  N NE  . ARG A 47  ? 1.2971 0.8454 1.0521 -0.0399 -0.2708 -0.2414 565 ARG A NE  
435  C CZ  . ARG A 47  ? 1.3224 0.8449 1.0733 -0.0219 -0.2624 -0.2439 565 ARG A CZ  
436  N NH1 . ARG A 47  ? 1.2432 0.7850 1.0344 -0.0384 -0.2572 -0.2279 565 ARG A NH1 
437  N NH2 . ARG A 47  ? 1.4118 0.8906 1.1179 0.0145  -0.2591 -0.2619 565 ARG A NH2 
438  N N   . ALA A 48  ? 0.7179 0.5610 0.6723 -0.0575 -0.1618 -0.1774 566 ALA A N   
439  C CA  . ALA A 48  ? 0.6713 0.5440 0.6501 -0.0457 -0.1341 -0.1685 566 ALA A CA  
440  C C   . ALA A 48  ? 0.7062 0.5420 0.6675 -0.0238 -0.1313 -0.1794 566 ALA A C   
441  O O   . ALA A 48  ? 0.7220 0.5812 0.6965 -0.0052 -0.1086 -0.1781 566 ALA A O   
442  C CB  . ALA A 48  ? 0.6158 0.5185 0.6347 -0.0709 -0.1320 -0.1481 566 ALA A CB  
443  N N   . ASP A 49  ? 0.7816 0.5591 0.7140 -0.0252 -0.1558 -0.1904 567 ASP A N   
444  C CA  . ASP A 49  ? 0.8810 0.6181 0.7939 0.0003  -0.1562 -0.2024 567 ASP A CA  
445  C C   . ASP A 49  ? 0.8892 0.6336 0.7809 0.0381  -0.1352 -0.2186 567 ASP A C   
446  O O   . ASP A 49  ? 0.8587 0.5975 0.7523 0.0643  -0.1246 -0.2250 567 ASP A O   
447  C CB  . ASP A 49  ? 1.0132 0.6754 0.8895 -0.0076 -0.1901 -0.2128 567 ASP A CB  
448  C CG  . ASP A 49  ? 1.0585 0.7113 0.9563 -0.0469 -0.2087 -0.1937 567 ASP A CG  
449  O OD1 . ASP A 49  ? 1.0236 0.7096 0.9556 -0.0553 -0.1949 -0.1759 567 ASP A OD1 
450  O OD2 . ASP A 49  ? 1.1061 0.7204 0.9856 -0.0701 -0.2358 -0.1945 567 ASP A OD2 
451  N N   . PHE A 50  ? 0.8804 0.6386 0.7519 0.0422  -0.1286 -0.2246 568 PHE A N   
452  C CA  . PHE A 50  ? 0.8609 0.6310 0.7107 0.0760  -0.1033 -0.2364 568 PHE A CA  
453  C C   . PHE A 50  ? 0.7429 0.5712 0.6378 0.0845  -0.0716 -0.2237 568 PHE A C   
454  O O   . PHE A 50  ? 0.7266 0.5672 0.6175 0.1135  -0.0494 -0.2314 568 PHE A O   
455  C CB  . PHE A 50  ? 0.8712 0.6473 0.6901 0.0746  -0.1021 -0.2401 568 PHE A CB  
456  C CG  . PHE A 50  ? 0.9383 0.6520 0.7007 0.0755  -0.1328 -0.2585 568 PHE A CG  
457  C CD1 . PHE A 50  ? 0.9969 0.6514 0.7411 0.0724  -0.1608 -0.2692 568 PHE A CD1 
458  C CD2 . PHE A 50  ? 0.9232 0.6320 0.6463 0.0787  -0.1367 -0.2650 568 PHE A CD2 
459  C CE1 . PHE A 50  ? 1.0771 0.6737 0.7707 0.0697  -0.1900 -0.2829 568 PHE A CE1 
460  C CE2 . PHE A 50  ? 0.9933 0.6412 0.6608 0.0788  -0.1691 -0.2831 568 PHE A CE2 
461  C CZ  . PHE A 50  ? 1.0724 0.6711 0.7322 0.0718  -0.1927 -0.2874 568 PHE A CZ  
462  N N   . LEU A 51  ? 0.6492 0.5141 0.5872 0.0597  -0.0694 -0.2042 569 LEU A N   
463  C CA  . LEU A 51  ? 0.6174 0.5323 0.5967 0.0629  -0.0449 -0.1918 569 LEU A CA  
464  C C   . LEU A 51  ? 0.6143 0.5250 0.6155 0.0763  -0.0456 -0.1930 569 LEU A C   
465  O O   . LEU A 51  ? 0.6043 0.5559 0.6408 0.0813  -0.0281 -0.1848 569 LEU A O   
466  C CB  . LEU A 51  ? 0.5672 0.5128 0.5758 0.0348  -0.0455 -0.1731 569 LEU A CB  
467  C CG  . LEU A 51  ? 0.5753 0.5253 0.5668 0.0223  -0.0504 -0.1710 569 LEU A CG  
468  C CD1 . LEU A 51  ? 0.5512 0.5287 0.5722 -0.0018 -0.0531 -0.1542 569 LEU A CD1 
469  C CD2 . LEU A 51  ? 0.5576 0.5249 0.5310 0.0384  -0.0289 -0.1737 569 LEU A CD2 
470  N N   . LYS A 52  ? 0.6489 0.5088 0.6295 0.0816  -0.0681 -0.2027 570 LYS A N   
471  C CA  . LYS A 52  ? 0.7566 0.6049 0.7521 0.0993  -0.0726 -0.2052 570 LYS A CA  
472  C C   . LYS A 52  ? 0.8547 0.7026 0.8387 0.1400  -0.0580 -0.2227 570 LYS A C   
473  O O   . LYS A 52  ? 0.8924 0.7463 0.8986 0.1608  -0.0574 -0.2246 570 LYS A O   
474  C CB  . LYS A 52  ? 0.8399 0.6260 0.8139 0.0870  -0.1046 -0.2060 570 LYS A CB  
475  C CG  . LYS A 52  ? 0.8503 0.6406 0.8376 0.0470  -0.1161 -0.1871 570 LYS A CG  
476  C CD  . LYS A 52  ? 0.9538 0.6867 0.9256 0.0340  -0.1440 -0.1831 570 LYS A CD  
477  C CE  . LYS A 52  ? 0.9633 0.7095 0.9522 -0.0049 -0.1494 -0.1614 570 LYS A CE  
478  N NZ  . LYS A 52  ? 0.9944 0.7212 0.9666 -0.0317 -0.1647 -0.1608 570 LYS A NZ  
479  N N   . ALA A 53  ? 0.8571 0.6991 0.8057 0.1538  -0.0465 -0.2354 571 ALA A N   
480  C CA  . ALA A 53  ? 0.8905 0.7380 0.8248 0.1947  -0.0264 -0.2517 571 ALA A CA  
481  C C   . ALA A 53  ? 0.8265 0.7508 0.8146 0.2027  0.0062  -0.2400 571 ALA A C   
482  O O   . ALA A 53  ? 0.7659 0.7317 0.7909 0.1756  0.0127  -0.2212 571 ALA A O   
483  C CB  . ALA A 53  ? 0.9367 0.7580 0.8125 0.2050  -0.0208 -0.2662 571 ALA A CB  
484  N N   . ARG A 54  ? 0.8434 0.7865 0.8361 0.2407  0.0264  -0.2515 572 ARG A N   
485  C CA  . ARG A 54  ? 0.8413 0.8627 0.8911 0.2472  0.0575  -0.2398 572 ARG A CA  
486  C C   . ARG A 54  ? 0.7633 0.8206 0.8084 0.2284  0.0832  -0.2281 572 ARG A C   
487  O O   . ARG A 54  ? 0.7880 0.8227 0.7799 0.2381  0.0935  -0.2377 572 ARG A O   
488  C CB  . ARG A 54  ? 1.0065 1.0466 1.0629 0.2946  0.0769  -0.2548 572 ARG A CB  
489  C CG  . ARG A 54  ? 1.0932 1.1602 1.2081 0.3090  0.0672  -0.2517 572 ARG A CG  
490  C CD  . ARG A 54  ? 1.1626 1.1655 1.2633 0.2958  0.0247  -0.2523 572 ARG A CD  
491  N NE  . ARG A 54  ? 1.1593 1.1877 1.3150 0.3030  0.0117  -0.2448 572 ARG A NE  
492  C CZ  . ARG A 54  ? 1.1938 1.2443 1.3767 0.3450  0.0167  -0.2546 572 ARG A CZ  
493  N NH1 . ARG A 54  ? 1.2179 1.2654 1.3724 0.3748  0.0382  -0.2649 572 ARG A NH1 
494  N NH2 . ARG A 54  ? 1.2000 1.2728 1.4329 0.3483  -0.0005 -0.2460 572 ARG A NH2 
495  N N   . LEU A 55  ? 0.6810 0.7880 0.7764 0.2018  0.0911  -0.2075 573 LEU A N   
496  C CA  . LEU A 55  ? 0.6851 0.8164 0.7748 0.1792  0.1097  -0.1936 573 LEU A CA  
497  C C   . LEU A 55  ? 0.7121 0.8892 0.8067 0.1984  0.1492  -0.1922 573 LEU A C   
498  O O   . LEU A 55  ? 0.6404 0.8727 0.7905 0.2071  0.1664  -0.1859 573 LEU A O   
499  C CB  . LEU A 55  ? 0.6341 0.7935 0.7703 0.1458  0.1022  -0.1734 573 LEU A CB  
500  C CG  . LEU A 55  ? 0.6139 0.7349 0.7476 0.1276  0.0678  -0.1725 573 LEU A CG  
501  C CD1 . LEU A 55  ? 0.5042 0.6537 0.6828 0.1023  0.0623  -0.1552 573 LEU A CD1 
502  C CD2 . LEU A 55  ? 0.6435 0.7212 0.7269 0.1144  0.0546  -0.1759 573 LEU A CD2 
503  N N   . TRP A 56  ? 0.7597 0.9159 0.7968 0.2044  0.1634  -0.1968 574 TRP A N   
504  C CA  . TRP A 56  ? 0.8085 1.0036 0.8379 0.2195  0.2046  -0.1926 574 TRP A CA  
505  C C   . TRP A 56  ? 0.8217 1.0204 0.8333 0.1894  0.2137  -0.1738 574 TRP A C   
506  O O   . TRP A 56  ? 0.8911 1.0460 0.8384 0.1887  0.2071  -0.1789 574 TRP A O   
507  C CB  . TRP A 56  ? 0.9250 1.0847 0.8892 0.2587  0.2147  -0.2155 574 TRP A CB  
508  C CG  . TRP A 56  ? 0.9905 1.1621 0.9831 0.2888  0.2193  -0.2257 574 TRP A CG  
509  C CD1 . TRP A 56  ? 0.9705 1.1771 1.0326 0.2914  0.2099  -0.2227 574 TRP A CD1 
510  C CD2 . TRP A 56  ? 1.1066 1.2526 1.0595 0.3184  0.2313  -0.2389 574 TRP A CD2 
511  N NE1 . TRP A 56  ? 1.0279 1.2317 1.0958 0.3224  0.2155  -0.2320 574 TRP A NE1 
512  C CE2 . TRP A 56  ? 1.1130 1.2809 1.1153 0.3396  0.2297  -0.2430 574 TRP A CE2 
513  C CE3 . TRP A 56  ? 1.2023 1.3089 1.0813 0.3297  0.2413  -0.2483 574 TRP A CE3 
514  C CZ2 . TRP A 56  ? 1.1840 1.3367 1.1651 0.3728  0.2396  -0.2568 574 TRP A CZ2 
515  C CZ3 . TRP A 56  ? 1.2623 1.3541 1.1195 0.3615  0.2508  -0.2626 574 TRP A CZ3 
516  C CH2 . TRP A 56  ? 1.2571 1.3722 1.1654 0.3833  0.2509  -0.2671 574 TRP A CH2 
517  N N   . ILE A 57  ? 0.7414 0.9892 0.8090 0.1648  0.2256  -0.1522 575 ILE A N   
518  C CA  . ILE A 57  ? 0.7041 0.9510 0.7608 0.1342  0.2298  -0.1325 575 ILE A CA  
519  C C   . ILE A 57  ? 0.7300 1.0210 0.7920 0.1341  0.2721  -0.1170 575 ILE A C   
520  O O   . ILE A 57  ? 0.7991 1.1471 0.9159 0.1411  0.2943  -0.1121 575 ILE A O   
521  C CB  . ILE A 57  ? 0.6375 0.8946 0.7454 0.1032  0.2077  -0.1193 575 ILE A CB  
522  C CG1 . ILE A 57  ? 0.5727 0.7889 0.6735 0.1028  0.1700  -0.1324 575 ILE A CG1 
523  C CG2 . ILE A 57  ? 0.6556 0.9052 0.7480 0.0753  0.2112  -0.1002 575 ILE A CG2 
524  C CD1 . ILE A 57  ? 0.4702 0.6964 0.6180 0.0789  0.1498  -0.1222 575 ILE A CD1 
525  N N   . GLU A 58  ? 0.7246 0.9910 0.7307 0.1258  0.2830  -0.1079 576 GLU A N   
526  C CA  . GLU A 58  ? 0.7880 1.0882 0.7877 0.1218  0.3243  -0.0896 576 GLU A CA  
527  C C   . GLU A 58  ? 0.7965 1.0794 0.7831 0.0875  0.3199  -0.0667 576 GLU A C   
528  O O   . GLU A 58  ? 0.7984 1.0280 0.7318 0.0838  0.2968  -0.0701 576 GLU A O   
529  C CB  . GLU A 58  ? 0.9058 1.1842 0.8306 0.1538  0.3474  -0.1020 576 GLU A CB  
530  C CG  . GLU A 58  ? 1.0095 1.2983 0.9034 0.1412  0.3801  -0.0816 576 GLU A CG  
531  C CD  . GLU A 58  ? 1.1916 1.4525 1.0164 0.1661  0.3914  -0.0965 576 GLU A CD  
532  O OE1 . GLU A 58  ? 1.2899 1.5270 1.0544 0.1590  0.4028  -0.0847 576 GLU A OE1 
533  O OE2 . GLU A 58  ? 1.2555 1.5141 1.0836 0.1931  0.3877  -0.1191 576 GLU A OE2 
534  N N   . PHE A 59  ? 0.7839 1.1112 0.8204 0.0626  0.3399  -0.0434 577 PHE A N   
535  C CA  . PHE A 59  ? 0.7753 1.0832 0.8041 0.0286  0.3344  -0.0204 577 PHE A CA  
536  C C   . PHE A 59  ? 0.8155 1.1270 0.8023 0.0229  0.3723  0.0000  577 PHE A C   
537  O O   . PHE A 59  ? 0.8669 1.2338 0.8854 0.0246  0.4095  0.0099  577 PHE A O   
538  C CB  . PHE A 59  ? 0.7136 1.0576 0.8224 -0.0008 0.3250  -0.0071 577 PHE A CB  
539  C CG  . PHE A 59  ? 0.6725 0.9871 0.7973 -0.0079 0.2826  -0.0178 577 PHE A CG  
540  C CD1 . PHE A 59  ? 0.6808 0.9429 0.7658 -0.0213 0.2599  -0.0134 577 PHE A CD1 
541  C CD2 . PHE A 59  ? 0.6498 0.9899 0.8280 0.0006  0.2663  -0.0314 577 PHE A CD2 
542  C CE1 . PHE A 59  ? 0.6336 0.8735 0.7327 -0.0261 0.2254  -0.0225 577 PHE A CE1 
543  C CE2 . PHE A 59  ? 0.6354 0.9477 0.8228 -0.0064 0.2303  -0.0394 577 PHE A CE2 
544  C CZ  . PHE A 59  ? 0.6154 0.8799 0.7638 -0.0199 0.2117  -0.0349 577 PHE A CZ  
545  N N   . ASP A 60  ? 0.8653 1.1198 0.7815 0.0168  0.3632  0.0073  578 ASP A N   
546  C CA  . ASP A 60  ? 0.9514 1.1958 0.8178 0.0063  0.3945  0.0312  578 ASP A CA  
547  C C   . ASP A 60  ? 1.0190 1.2946 0.8618 0.0300  0.4320  0.0270  578 ASP A C   
548  O O   . ASP A 60  ? 1.0607 1.3634 0.9052 0.0134  0.4576  0.0470  578 ASP A O   
549  C CB  . ASP A 60  ? 0.9645 1.2321 0.8796 -0.0344 0.4048  0.0612  578 ASP A CB  
550  C CG  . ASP A 60  ? 1.0004 1.2255 0.9241 -0.0562 0.3638  0.0640  578 ASP A CG  
551  O OD1 . ASP A 60  ? 1.0353 1.1999 0.8954 -0.0491 0.3417  0.0604  578 ASP A OD1 
552  O OD2 . ASP A 60  ? 0.9860 1.2385 0.9791 -0.0787 0.3530  0.0693  578 ASP A OD2 
553  N N   . GLY A 61  ? 1.0206 1.2890 0.8436 0.0647  0.4230  -0.0025 579 GLY A N   
554  C CA  . GLY A 61  ? 1.0422 1.3294 0.8420 0.0864  0.4447  -0.0141 579 GLY A CA  
555  C C   . GLY A 61  ? 1.0047 1.3690 0.8832 0.0787  0.4714  -0.0085 579 GLY A C   
556  O O   . GLY A 61  ? 1.0672 1.4534 0.9282 0.0859  0.5001  -0.0076 579 GLY A O   
557  N N   . GLU A 62  ? 0.9463 1.3527 0.9113 0.0639  0.4619  -0.0051 580 GLU A N   
558  C CA  . GLU A 62  ? 1.0049 1.4861 1.0517 0.0567  0.4813  -0.0022 580 GLU A CA  
559  C C   . GLU A 62  ? 1.0146 1.5070 1.0749 0.0964  0.4801  -0.0329 580 GLU A C   
560  O O   . GLU A 62  ? 0.9572 1.4372 1.0416 0.1108  0.4530  -0.0494 580 GLU A O   
561  C CB  . GLU A 62  ? 0.9833 1.4991 1.1136 0.0245  0.4652  0.0132  580 GLU A CB  
562  C CG  . GLU A 62  ? 1.0264 1.5391 1.1546 -0.0190 0.4718  0.0466  580 GLU A CG  
563  C CD  . GLU A 62  ? 0.9851 1.4872 1.1574 -0.0463 0.4423  0.0585  580 GLU A CD  
564  O OE1 . GLU A 62  ? 1.0095 1.5034 1.1864 -0.0840 0.4430  0.0852  580 GLU A OE1 
565  O OE2 . GLU A 62  ? 0.9395 1.4358 1.1392 -0.0310 0.4176  0.0409  580 GLU A OE2 
566  N N   . LYS A 63  ? 1.0960 1.6078 1.1379 0.1146  0.5096  -0.0397 581 LYS A N   
567  C CA  . LYS A 63  ? 1.1647 1.6733 1.2019 0.1562  0.5101  -0.0685 581 LYS A CA  
568  C C   . LYS A 63  ? 1.1760 1.7542 1.3117 0.1607  0.5180  -0.0720 581 LYS A C   
569  O O   . LYS A 63  ? 1.1961 1.8346 1.3979 0.1321  0.5336  -0.0524 581 LYS A O   
570  C CB  . LYS A 63  ? 1.2507 1.7428 1.2153 0.1774  0.5379  -0.0750 581 LYS A CB  
571  C CG  . LYS A 63  ? 1.3054 1.7352 1.1731 0.1701  0.5333  -0.0669 581 LYS A CG  
572  C CD  . LYS A 63  ? 1.3033 1.6588 1.1142 0.1894  0.4941  -0.0880 581 LYS A CD  
573  C CE  . LYS A 63  ? 1.3098 1.6137 1.0578 0.1699  0.4785  -0.0732 581 LYS A CE  
574  N NZ  . LYS A 63  ? 1.4083 1.6711 1.0627 0.1805  0.4899  -0.0728 581 LYS A NZ  
575  N N   . GLY A 64  ? 1.1592 1.7244 1.3022 0.1970  0.5044  -0.0971 582 GLY A N   
576  C CA  . GLY A 64  ? 1.1294 1.7534 1.3542 0.2124  0.5124  -0.1039 582 GLY A CA  
577  C C   . GLY A 64  ? 1.0555 1.7268 1.3761 0.1862  0.4951  -0.0907 582 GLY A C   
578  O O   . GLY A 64  ? 1.0713 1.8125 1.4637 0.1700  0.5139  -0.0783 582 GLY A O   
579  N N   . LEU A 65  ? 0.9987 1.6331 1.3212 0.1815  0.4581  -0.0936 583 LEU A N   
580  C CA  . LEU A 65  ? 0.9261 1.5974 1.3338 0.1604  0.4359  -0.0833 583 LEU A CA  
581  C C   . LEU A 65  ? 0.8977 1.5347 1.3120 0.1879  0.4016  -0.0995 583 LEU A C   
582  O O   . LEU A 65  ? 0.9275 1.5039 1.2731 0.2140  0.3902  -0.1171 583 LEU A O   
583  C CB  . LEU A 65  ? 0.8812 1.5458 1.2879 0.1156  0.4243  -0.0616 583 LEU A CB  
584  C CG  . LEU A 65  ? 0.9243 1.6501 1.3799 0.0793  0.4466  -0.0394 583 LEU A CG  
585  C CD1 . LEU A 65  ? 0.8848 1.5888 1.3211 0.0380  0.4349  -0.0176 583 LEU A CD1 
586  C CD2 . LEU A 65  ? 0.9209 1.7112 1.4759 0.0744  0.4380  -0.0391 583 LEU A CD2 
587  N N   . ASP A 66  ? 0.8657 1.5402 1.3610 0.1805  0.3825  -0.0923 584 ASP A N   
588  C CA  . ASP A 66  ? 0.8657 1.5141 1.3707 0.2062  0.3482  -0.1022 584 ASP A CA  
589  C C   . ASP A 66  ? 0.8844 1.4709 1.3290 0.1994  0.3184  -0.1069 584 ASP A C   
590  O O   . ASP A 66  ? 0.8271 1.4181 1.2833 0.1656  0.3041  -0.0920 584 ASP A O   
591  C CB  . ASP A 66  ? 0.8107 1.5124 1.4093 0.1951  0.3297  -0.0866 584 ASP A CB  
592  C CG  . ASP A 66  ? 0.8306 1.5074 1.4295 0.2184  0.2885  -0.0966 584 ASP A CG  
593  O OD1 . ASP A 66  ? 0.8943 1.5502 1.4751 0.2573  0.2878  -0.1164 584 ASP A OD1 
594  O OD2 . ASP A 66  ? 0.8123 1.4867 1.4259 0.1949  0.2548  -0.0896 584 ASP A OD2 
595  N N   . TYR A 67  ? 0.9496 1.4778 1.3295 0.2292  0.3065  -0.1309 585 TYR A N   
596  C CA  . TYR A 67  ? 0.9486 1.4183 1.2732 0.2220  0.2774  -0.1427 585 TYR A CA  
597  C C   . TYR A 67  ? 0.9157 1.3867 1.2834 0.2070  0.2388  -0.1451 585 TYR A C   
598  O O   . TYR A 67  ? 0.9164 1.3285 1.2437 0.1874  0.2116  -0.1470 585 TYR A O   
599  C CB  . TYR A 67  ? 0.9848 1.3875 1.2345 0.2557  0.2696  -0.1682 585 TYR A CB  
600  C CG  . TYR A 67  ? 1.0240 1.3957 1.2001 0.2580  0.2931  -0.1709 585 TYR A CG  
601  C CD1 . TYR A 67  ? 0.9842 1.3480 1.1305 0.2302  0.2973  -0.1591 585 TYR A CD1 
602  C CD2 . TYR A 67  ? 1.0996 1.4476 1.2326 0.2881  0.3085  -0.1860 585 TYR A CD2 
603  C CE1 . TYR A 67  ? 1.0362 1.3676 1.1105 0.2328  0.3148  -0.1606 585 TYR A CE1 
604  C CE2 . TYR A 67  ? 1.1445 1.4624 1.2059 0.2892  0.3258  -0.1894 585 TYR A CE2 
605  C CZ  . TYR A 67  ? 1.1187 1.4278 1.1506 0.2614  0.3281  -0.1761 585 TYR A CZ  
606  O OH  . TYR A 67  ? 1.1634 1.4398 1.1205 0.2633  0.3417  -0.1781 585 TYR A OH  
607  N N   . GLY A 68  ? 0.8792 1.3945 1.3166 0.2094  0.2306  -0.1367 586 GLY A N   
608  C CA  . GLY A 68  ? 0.8163 1.3277 1.2916 0.1927  0.1930  -0.1374 586 GLY A CA  
609  C C   . GLY A 68  ? 0.7651 1.3029 1.2762 0.1470  0.1896  -0.1147 586 GLY A C   
610  O O   . GLY A 68  ? 0.6790 1.1743 1.1737 0.1216  0.1602  -0.1108 586 GLY A O   
611  N N   . GLY A 69  ? 0.7714 1.3680 1.3202 0.1352  0.2178  -0.0950 587 GLY A N   
612  C CA  . GLY A 69  ? 0.6919 1.3108 1.2742 0.0911  0.2126  -0.0736 587 GLY A CA  
613  C C   . GLY A 69  ? 0.6193 1.1913 1.1463 0.0640  0.2173  -0.0698 587 GLY A C   
614  O O   . GLY A 69  ? 0.6055 1.1512 1.1310 0.0327  0.1938  -0.0607 587 GLY A O   
615  N N   . VAL A 70  ? 0.5485 1.1000 1.0182 0.0778  0.2439  -0.0740 588 VAL A N   
616  C CA  . VAL A 70  ? 0.5483 1.0481 0.9559 0.0553  0.2441  -0.0665 588 VAL A CA  
617  C C   . VAL A 70  ? 0.4889 0.9210 0.8546 0.0524  0.2069  -0.0780 588 VAL A C   
618  O O   . VAL A 70  ? 0.5085 0.9059 0.8482 0.0274  0.1945  -0.0694 588 VAL A O   
619  C CB  . VAL A 70  ? 0.5852 1.0769 0.9366 0.0732  0.2784  -0.0689 588 VAL A CB  
620  C CG1 . VAL A 70  ? 0.5791 1.1424 0.9738 0.0837  0.3177  -0.0581 588 VAL A CG1 
621  C CG2 . VAL A 70  ? 0.6588 1.1009 0.9521 0.1074  0.2679  -0.0938 588 VAL A CG2 
622  N N   . ALA A 71  ? 0.4544 0.8670 0.8139 0.0781  0.1890  -0.0965 589 ALA A N   
623  C CA  . ALA A 71  ? 0.5124 0.8687 0.8419 0.0719  0.1546  -0.1043 589 ALA A CA  
624  C C   . ALA A 71  ? 0.5172 0.8774 0.8810 0.0434  0.1325  -0.0923 589 ALA A C   
625  O O   . ALA A 71  ? 0.5033 0.8245 0.8369 0.0252  0.1166  -0.0890 589 ALA A O   
626  C CB  . ALA A 71  ? 0.5399 0.8761 0.8633 0.1015  0.1387  -0.1231 589 ALA A CB  
627  N N   . ARG A 72  ? 0.5394 0.9480 0.9663 0.0406  0.1306  -0.0862 590 ARG A N   
628  C CA  . ARG A 72  ? 0.5214 0.9309 0.9773 0.0137  0.1070  -0.0759 590 ARG A CA  
629  C C   . ARG A 72  ? 0.4897 0.8911 0.9320 -0.0175 0.1152  -0.0604 590 ARG A C   
630  O O   . ARG A 72  ? 0.4464 0.8125 0.8709 -0.0367 0.0941  -0.0568 590 ARG A O   
631  C CB  . ARG A 72  ? 0.5508 1.0187 1.0806 0.0170  0.1017  -0.0722 590 ARG A CB  
632  C CG  . ARG A 72  ? 0.5986 1.0928 1.1703 -0.0175 0.0938  -0.0553 590 ARG A CG  
633  C CD  . ARG A 72  ? 0.6556 1.1804 1.2857 -0.0167 0.0660  -0.0555 590 ARG A CD  
634  N NE  . ARG A 72  ? 0.6881 1.2530 1.3694 -0.0480 0.0616  -0.0387 590 ARG A NE  
635  C CZ  . ARG A 72  ? 0.6893 1.2207 1.3553 -0.0809 0.0432  -0.0308 590 ARG A CZ  
636  N NH1 . ARG A 72  ? 0.6525 1.1131 1.2504 -0.0833 0.0302  -0.0369 590 ARG A NH1 
637  N NH2 . ARG A 72  ? 0.7155 1.2717 1.4094 -0.1088 0.0357  -0.0145 590 ARG A NH2 
638  N N   . GLU A 73  ? 0.4727 0.9024 0.9181 -0.0214 0.1465  -0.0510 591 GLU A N   
639  C CA  . GLU A 73  ? 0.5118 0.9240 0.9359 -0.0502 0.1537  -0.0352 591 GLU A CA  
640  C C   . GLU A 73  ? 0.5210 0.8698 0.8744 -0.0481 0.1455  -0.0408 591 GLU A C   
641  O O   . GLU A 73  ? 0.4991 0.8144 0.8321 -0.0683 0.1322  -0.0335 591 GLU A O   
642  C CB  . GLU A 73  ? 0.5931 1.0467 1.0300 -0.0548 0.1911  -0.0217 591 GLU A CB  
643  C CG  . GLU A 73  ? 0.7604 1.1754 1.1431 -0.0722 0.2034  -0.0091 591 GLU A CG  
644  C CD  . GLU A 73  ? 0.9303 1.3862 1.3318 -0.0877 0.2381  0.0111  591 GLU A CD  
645  O OE1 . GLU A 73  ? 1.0217 1.5095 1.4198 -0.0662 0.2689  0.0086  591 GLU A OE1 
646  O OE2 . GLU A 73  ? 0.9921 1.4452 1.4082 -0.1217 0.2351  0.0299  591 GLU A OE2 
647  N N   . TRP A 74  ? 0.4847 0.8159 0.8005 -0.0228 0.1513  -0.0545 592 TRP A N   
648  C CA  . TRP A 74  ? 0.4581 0.7371 0.7146 -0.0207 0.1411  -0.0599 592 TRP A CA  
649  C C   . TRP A 74  ? 0.4866 0.7366 0.7416 -0.0293 0.1110  -0.0634 592 TRP A C   
650  O O   . TRP A 74  ? 0.5164 0.7350 0.7419 -0.0405 0.1025  -0.0587 592 TRP A O   
651  C CB  . TRP A 74  ? 0.4542 0.7195 0.6756 0.0063  0.1465  -0.0755 592 TRP A CB  
652  C CG  . TRP A 74  ? 0.4694 0.6877 0.6408 0.0072  0.1299  -0.0817 592 TRP A CG  
653  C CD1 . TRP A 74  ? 0.5001 0.6948 0.6302 0.0010  0.1339  -0.0752 592 TRP A CD1 
654  C CD2 . TRP A 74  ? 0.4879 0.6805 0.6493 0.0137  0.1059  -0.0940 592 TRP A CD2 
655  N NE1 . TRP A 74  ? 0.5348 0.6975 0.6356 0.0046  0.1136  -0.0836 592 TRP A NE1 
656  C CE2 . TRP A 74  ? 0.5108 0.6726 0.6310 0.0102  0.0974  -0.0944 592 TRP A CE2 
657  C CE3 . TRP A 74  ? 0.5391 0.7312 0.7221 0.0214  0.0902  -0.1033 592 TRP A CE3 
658  C CZ2 . TRP A 74  ? 0.5193 0.6573 0.6259 0.0115  0.0757  -0.1028 592 TRP A CZ2 
659  C CZ3 . TRP A 74  ? 0.5202 0.6802 0.6820 0.0217  0.0690  -0.1109 592 TRP A CZ3 
660  C CH2 . TRP A 74  ? 0.5108 0.6476 0.6379 0.0154  0.0629  -0.1102 592 TRP A CH2 
661  N N   . PHE A 75  ? 0.4782 0.7373 0.7618 -0.0221 0.0951  -0.0712 593 PHE A N   
662  C CA  . PHE A 75  ? 0.4662 0.6980 0.7442 -0.0298 0.0689  -0.0733 593 PHE A CA  
663  C C   . PHE A 75  ? 0.4971 0.7235 0.7836 -0.0530 0.0610  -0.0617 593 PHE A C   
664  O O   . PHE A 75  ? 0.5300 0.7235 0.7900 -0.0595 0.0468  -0.0618 593 PHE A O   
665  C CB  . PHE A 75  ? 0.3953 0.6361 0.7006 -0.0183 0.0533  -0.0811 593 PHE A CB  
666  C CG  . PHE A 75  ? 0.3815 0.5987 0.6604 0.0004  0.0479  -0.0937 593 PHE A CG  
667  C CD1 . PHE A 75  ? 0.4014 0.5819 0.6438 -0.0044 0.0359  -0.0960 593 PHE A CD1 
668  C CD2 . PHE A 75  ? 0.4407 0.6723 0.7315 0.0228  0.0543  -0.1032 593 PHE A CD2 
669  C CE1 . PHE A 75  ? 0.4165 0.5734 0.6365 0.0075  0.0282  -0.1060 593 PHE A CE1 
670  C CE2 . PHE A 75  ? 0.4261 0.6260 0.6872 0.0383  0.0457  -0.1154 593 PHE A CE2 
671  C CZ  . PHE A 75  ? 0.3796 0.5413 0.6060 0.0281  0.0315  -0.1161 593 PHE A CZ  
672  N N   . PHE A 76  ? 0.4544 0.7122 0.7771 -0.0658 0.0698  -0.0518 594 PHE A N   
673  C CA  . PHE A 76  ? 0.4829 0.7274 0.8085 -0.0907 0.0604  -0.0407 594 PHE A CA  
674  C C   . PHE A 76  ? 0.4915 0.7029 0.7714 -0.0976 0.0707  -0.0340 594 PHE A C   
675  O O   . PHE A 76  ? 0.5594 0.7316 0.8102 -0.1055 0.0564  -0.0329 594 PHE A O   
676  C CB  . PHE A 76  ? 0.4290 0.7196 0.8114 -0.1065 0.0657  -0.0301 594 PHE A CB  
677  C CG  . PHE A 76  ? 0.4865 0.7592 0.8703 -0.1365 0.0555  -0.0174 594 PHE A CG  
678  C CD1 . PHE A 76  ? 0.5529 0.8029 0.9401 -0.1480 0.0251  -0.0197 594 PHE A CD1 
679  C CD2 . PHE A 76  ? 0.5381 0.8102 0.9139 -0.1534 0.0749  -0.0030 594 PHE A CD2 
680  C CE1 . PHE A 76  ? 0.6569 0.8814 1.0393 -0.1754 0.0122  -0.0099 594 PHE A CE1 
681  C CE2 . PHE A 76  ? 0.6438 0.8903 1.0168 -0.1828 0.0626  0.0090  594 PHE A CE2 
682  C CZ  . PHE A 76  ? 0.6823 0.9037 1.0587 -0.1936 0.0302  0.0045  594 PHE A CZ  
683  N N   . LEU A 77  ? 0.4873 0.7113 0.7558 -0.0919 0.0953  -0.0299 595 LEU A N   
684  C CA  . LEU A 77  ? 0.5330 0.7237 0.7554 -0.0971 0.1038  -0.0219 595 LEU A CA  
685  C C   . LEU A 77  ? 0.5178 0.6700 0.6959 -0.0829 0.0907  -0.0317 595 LEU A C   
686  O O   . LEU A 77  ? 0.5560 0.6723 0.7030 -0.0884 0.0829  -0.0270 595 LEU A O   
687  C CB  . LEU A 77  ? 0.5474 0.7581 0.7601 -0.0909 0.1328  -0.0159 595 LEU A CB  
688  C CG  . LEU A 77  ? 0.5510 0.8028 0.8048 -0.1090 0.1526  -0.0004 595 LEU A CG  
689  C CD1 . LEU A 77  ? 0.5408 0.8098 0.7741 -0.0988 0.1852  0.0051  595 LEU A CD1 
690  C CD2 . LEU A 77  ? 0.5733 0.8008 0.8268 -0.1397 0.1438  0.0161  595 LEU A CD2 
691  N N   . ILE A 78  ? 0.4306 0.5899 0.6064 -0.0645 0.0874  -0.0448 596 ILE A N   
692  C CA  . ILE A 78  ? 0.4123 0.5444 0.5544 -0.0540 0.0757  -0.0524 596 ILE A CA  
693  C C   . ILE A 78  ? 0.4319 0.5467 0.5761 -0.0599 0.0567  -0.0538 596 ILE A C   
694  O O   . ILE A 78  ? 0.4311 0.5232 0.5479 -0.0553 0.0498  -0.0548 596 ILE A O   
695  C CB  . ILE A 78  ? 0.4362 0.5770 0.5751 -0.0371 0.0754  -0.0649 596 ILE A CB  
696  C CG1 . ILE A 78  ? 0.4975 0.6168 0.6010 -0.0290 0.0677  -0.0693 596 ILE A CG1 
697  C CG2 . ILE A 78  ? 0.3683 0.5186 0.5355 -0.0352 0.0623  -0.0722 596 ILE A CG2 
698  C CD1 . ILE A 78  ? 0.5113 0.6182 0.5806 -0.0258 0.0779  -0.0633 596 ILE A CD1 
699  N N   . SER A 79  ? 0.4446 0.5705 0.6195 -0.0683 0.0480  -0.0537 597 SER A N   
700  C CA  . SER A 79  ? 0.4680 0.5723 0.6362 -0.0733 0.0300  -0.0551 597 SER A CA  
701  C C   . SER A 79  ? 0.5290 0.6026 0.6733 -0.0831 0.0270  -0.0481 597 SER A C   
702  O O   . SER A 79  ? 0.6100 0.6560 0.7251 -0.0773 0.0189  -0.0509 597 SER A O   
703  C CB  . SER A 79  ? 0.4826 0.6025 0.6854 -0.0797 0.0179  -0.0564 597 SER A CB  
704  O OG  . SER A 79  ? 0.5158 0.6519 0.7322 -0.0673 0.0161  -0.0639 597 SER A OG  
705  N N   . LYS A 80  ? 0.4723 0.5491 0.6277 -0.0978 0.0339  -0.0383 598 LYS A N   
706  C CA  . LYS A 80  ? 0.5511 0.5889 0.6794 -0.1091 0.0284  -0.0307 598 LYS A CA  
707  C C   . LYS A 80  ? 0.5469 0.5578 0.6313 -0.0946 0.0345  -0.0305 598 LYS A C   
708  O O   . LYS A 80  ? 0.5989 0.5685 0.6506 -0.0935 0.0254  -0.0292 598 LYS A O   
709  C CB  . LYS A 80  ? 0.5917 0.6404 0.7434 -0.1321 0.0359  -0.0172 598 LYS A CB  
710  C CG  . LYS A 80  ? 0.6473 0.7203 0.8458 -0.1495 0.0234  -0.0159 598 LYS A CG  
711  C CD  . LYS A 80  ? 0.7412 0.7711 0.9205 -0.1584 -0.0032 -0.0195 598 LYS A CD  
712  C CE  . LYS A 80  ? 0.8201 0.8592 1.0372 -0.1874 -0.0176 -0.0112 598 LYS A CE  
713  N NZ  . LYS A 80  ? 0.8885 0.8709 1.0723 -0.2072 -0.0310 -0.0039 598 LYS A NZ  
714  N N   . GLU A 81  ? 0.5015 0.5330 0.5830 -0.0815 0.0473  -0.0327 599 GLU A N   
715  C CA  . GLU A 81  ? 0.5065 0.5180 0.5503 -0.0662 0.0493  -0.0329 599 GLU A CA  
716  C C   . GLU A 81  ? 0.5406 0.5506 0.5764 -0.0501 0.0389  -0.0432 599 GLU A C   
717  O O   . GLU A 81  ? 0.5990 0.5827 0.6078 -0.0404 0.0326  -0.0433 599 GLU A O   
718  C CB  . GLU A 81  ? 0.5136 0.5450 0.5532 -0.0593 0.0639  -0.0318 599 GLU A CB  
719  C CG  . GLU A 81  ? 0.5631 0.5863 0.5906 -0.0709 0.0785  -0.0177 599 GLU A CG  
720  C CD  . GLU A 81  ? 0.6910 0.6675 0.6764 -0.0711 0.0731  -0.0084 599 GLU A CD  
721  O OE1 . GLU A 81  ? 0.7299 0.6924 0.6810 -0.0559 0.0738  -0.0078 599 GLU A OE1 
722  O OE2 . GLU A 81  ? 0.7662 0.7161 0.7503 -0.0856 0.0654  -0.0020 599 GLU A OE2 
723  N N   . MET A 82  ? 0.4778 0.5159 0.5368 -0.0466 0.0376  -0.0512 600 MET A N   
724  C CA  . MET A 82  ? 0.4801 0.5230 0.5349 -0.0348 0.0308  -0.0580 600 MET A CA  
725  C C   . MET A 82  ? 0.4966 0.5180 0.5389 -0.0335 0.0228  -0.0589 600 MET A C   
726  O O   . MET A 82  ? 0.5301 0.5486 0.5577 -0.0201 0.0213  -0.0613 600 MET A O   
727  C CB  . MET A 82  ? 0.5088 0.5771 0.5883 -0.0361 0.0292  -0.0641 600 MET A CB  
728  C CG  . MET A 82  ? 0.5327 0.6166 0.6167 -0.0325 0.0352  -0.0670 600 MET A CG  
729  S SD  . MET A 82  ? 0.5141 0.6138 0.6206 -0.0329 0.0291  -0.0750 600 MET A SD  
730  C CE  . MET A 82  ? 0.5662 0.6669 0.6959 -0.0422 0.0259  -0.0727 600 MET A CE  
731  N N   . PHE A 83  ? 0.4314 0.4391 0.4793 -0.0462 0.0171  -0.0574 601 PHE A N   
732  C CA  . PHE A 83  ? 0.5160 0.4973 0.5454 -0.0448 0.0070  -0.0603 601 PHE A CA  
733  C C   . PHE A 83  ? 0.5939 0.5319 0.5928 -0.0462 0.0019  -0.0571 601 PHE A C   
734  O O   . PHE A 83  ? 0.6792 0.5854 0.6568 -0.0467 -0.0091 -0.0606 601 PHE A O   
735  C CB  . PHE A 83  ? 0.5120 0.4993 0.5618 -0.0575 -0.0025 -0.0620 601 PHE A CB  
736  C CG  . PHE A 83  ? 0.5281 0.5483 0.6030 -0.0556 0.0001  -0.0647 601 PHE A CG  
737  C CD1 . PHE A 83  ? 0.5101 0.5488 0.6165 -0.0650 -0.0039 -0.0642 601 PHE A CD1 
738  C CD2 . PHE A 83  ? 0.5116 0.5440 0.5800 -0.0443 0.0054  -0.0671 601 PHE A CD2 
739  C CE1 . PHE A 83  ? 0.5579 0.6173 0.6814 -0.0608 -0.0037 -0.0673 601 PHE A CE1 
740  C CE2 . PHE A 83  ? 0.5153 0.5690 0.6026 -0.0453 0.0052  -0.0687 601 PHE A CE2 
741  C CZ  . PHE A 83  ? 0.5503 0.6128 0.6614 -0.0523 0.0001  -0.0694 601 PHE A CZ  
742  N N   . ASN A 84  ? 0.5597 0.4896 0.5500 -0.0465 0.0082  -0.0505 602 ASN A N   
743  C CA  . ASN A 84  ? 0.5807 0.4609 0.5351 -0.0461 0.0022  -0.0462 602 ASN A CA  
744  C C   . ASN A 84  ? 0.5826 0.4415 0.5035 -0.0195 -0.0008 -0.0534 602 ASN A C   
745  O O   . ASN A 84  ? 0.5727 0.4554 0.4952 -0.0015 0.0064  -0.0546 602 ASN A O   
746  C CB  . ASN A 84  ? 0.5768 0.4527 0.5253 -0.0514 0.0110  -0.0354 602 ASN A CB  
747  C CG  . ASN A 84  ? 0.6955 0.5127 0.6070 -0.0579 0.0031  -0.0275 602 ASN A CG  
748  O OD1 . ASN A 84  ? 0.7219 0.4970 0.6062 -0.0524 -0.0101 -0.0330 602 ASN A OD1 
749  N ND2 . ASN A 84  ? 0.7322 0.5411 0.6369 -0.0692 0.0111  -0.0144 602 ASN A ND2 
750  N N   . PRO A 85  ? 0.6227 0.4389 0.5132 -0.0149 -0.0118 -0.0588 603 PRO A N   
751  C CA  . PRO A 85  ? 0.6730 0.4721 0.5308 0.0157  -0.0113 -0.0665 603 PRO A CA  
752  C C   . PRO A 85  ? 0.7392 0.5186 0.5738 0.0342  -0.0098 -0.0625 603 PRO A C   
753  O O   . PRO A 85  ? 0.7483 0.5381 0.5726 0.0634  -0.0057 -0.0678 603 PRO A O   
754  C CB  . PRO A 85  ? 0.6726 0.4163 0.4930 0.0150  -0.0254 -0.0735 603 PRO A CB  
755  C CG  . PRO A 85  ? 0.6758 0.4298 0.5235 -0.0156 -0.0333 -0.0711 603 PRO A CG  
756  C CD  . PRO A 85  ? 0.6470 0.4322 0.5327 -0.0356 -0.0261 -0.0597 603 PRO A CD  
757  N N   . TYR A 86  ? 0.7790 0.5324 0.6056 0.0187  -0.0127 -0.0521 604 TYR A N   
758  C CA  A TYR A 86  ? 0.8418 0.5686 0.6390 0.0370  -0.0138 -0.0468 604 TYR A CA  
759  C CA  B TYR A 86  ? 0.8417 0.5685 0.6390 0.0368  -0.0138 -0.0467 604 TYR A CA  
760  C C   . TYR A 86  ? 0.7463 0.5273 0.5666 0.0533  -0.0047 -0.0464 604 TYR A C   
761  O O   . TYR A 86  ? 0.7064 0.4740 0.5046 0.0769  -0.0081 -0.0447 604 TYR A O   
762  C CB  A TYR A 86  ? 0.9076 0.5936 0.6884 0.0125  -0.0172 -0.0325 604 TYR A CB  
763  C CB  B TYR A 86  ? 0.9063 0.5934 0.6882 0.0118  -0.0170 -0.0324 604 TYR A CB  
764  C CG  A TYR A 86  ? 0.9922 0.6121 0.7433 -0.0038 -0.0318 -0.0314 604 TYR A CG  
765  C CG  B TYR A 86  ? 0.9951 0.6488 0.7408 0.0285  -0.0192 -0.0240 604 TYR A CG  
766  C CD1 A TYR A 86  ? 1.0788 0.6240 0.7749 0.0099  -0.0446 -0.0298 604 TYR A CD1 
767  C CD1 B TYR A 86  ? 1.1132 0.7028 0.8094 0.0515  -0.0322 -0.0267 604 TYR A CD1 
768  C CD2 A TYR A 86  ? 1.0049 0.6335 0.7814 -0.0326 -0.0362 -0.0323 604 TYR A CD2 
769  C CD2 B TYR A 86  ? 1.0023 0.6837 0.7577 0.0240  -0.0099 -0.0141 604 TYR A CD2 
770  C CE1 A TYR A 86  ? 1.1490 0.6255 0.8138 -0.0074 -0.0617 -0.0296 604 TYR A CE1 
771  C CE1 B TYR A 86  ? 1.2017 0.7566 0.8621 0.0692  -0.0371 -0.0183 604 TYR A CE1 
772  C CE2 A TYR A 86  ? 1.0655 0.6327 0.8158 -0.0506 -0.0541 -0.0316 604 TYR A CE2 
773  C CE2 B TYR A 86  ? 1.0770 0.7240 0.7938 0.0402  -0.0145 -0.0055 604 TYR A CE2 
774  C CZ  A TYR A 86  ? 1.1583 0.6472 0.8513 -0.0392 -0.0670 -0.0305 604 TYR A CZ  
775  C CZ  B TYR A 86  ? 1.1977 0.7820 0.8686 0.0626  -0.0287 -0.0070 604 TYR A CZ  
776  O OH  A TYR A 86  ? 1.2445 0.6644 0.9075 -0.0594 -0.0885 -0.0306 604 TYR A OH  
777  O OH  B TYR A 86  ? 1.3147 0.8607 0.9445 0.0810  -0.0360 0.0022  604 TYR A OH  
778  N N   . TYR A 87  ? 0.6936 0.5318 0.5561 0.0417  0.0037  -0.0482 605 TYR A N   
779  C CA  . TYR A 87  ? 0.6521 0.5386 0.5360 0.0548  0.0082  -0.0493 605 TYR A CA  
780  C C   . TYR A 87  ? 0.6845 0.6017 0.5801 0.0782  0.0091  -0.0578 605 TYR A C   
781  O O   . TYR A 87  ? 0.7448 0.6994 0.6571 0.0919  0.0089  -0.0582 605 TYR A O   
782  C CB  . TYR A 87  ? 0.6530 0.5806 0.5722 0.0335  0.0152  -0.0484 605 TYR A CB  
783  C CG  . TYR A 87  ? 0.7353 0.6464 0.6461 0.0155  0.0194  -0.0389 605 TYR A CG  
784  C CD1 . TYR A 87  ? 0.6654 0.5967 0.6027 -0.0065 0.0267  -0.0376 605 TYR A CD1 
785  C CD2 . TYR A 87  ? 0.8364 0.7121 0.7117 0.0221  0.0172  -0.0301 605 TYR A CD2 
786  C CE1 . TYR A 87  ? 0.6778 0.6017 0.6104 -0.0218 0.0351  -0.0277 605 TYR A CE1 
787  C CE2 . TYR A 87  ? 0.8551 0.7167 0.7197 0.0043  0.0247  -0.0188 605 TYR A CE2 
788  C CZ  . TYR A 87  ? 0.7879 0.6773 0.6831 -0.0177 0.0354  -0.0176 605 TYR A CZ  
789  O OH  . TYR A 87  ? 0.8377 0.7208 0.7252 -0.0342 0.0473  -0.0053 605 TYR A OH  
790  N N   . GLY A 88  ? 0.6709 0.5742 0.5575 0.0826  0.0098  -0.0640 606 GLY A N   
791  C CA  . GLY A 88  ? 0.6302 0.5605 0.5222 0.1070  0.0150  -0.0706 606 GLY A CA  
792  C C   . GLY A 88  ? 0.5830 0.5701 0.5144 0.0968  0.0237  -0.0718 606 GLY A C   
793  O O   . GLY A 88  ? 0.6256 0.6433 0.5659 0.1142  0.0315  -0.0747 606 GLY A O   
794  N N   . LEU A 89  ? 0.4757 0.4775 0.4303 0.0699  0.0233  -0.0690 607 LEU A N   
795  C CA  . LEU A 89  ? 0.4679 0.5137 0.4548 0.0589  0.0290  -0.0693 607 LEU A CA  
796  C C   . LEU A 89  ? 0.5024 0.5317 0.4768 0.0526  0.0313  -0.0721 607 LEU A C   
797  O O   . LEU A 89  ? 0.5104 0.5617 0.4875 0.0608  0.0395  -0.0728 607 LEU A O   
798  C CB  . LEU A 89  ? 0.4718 0.5343 0.4832 0.0378  0.0259  -0.0667 607 LEU A CB  
799  C CG  . LEU A 89  ? 0.5643 0.6406 0.5808 0.0445  0.0220  -0.0647 607 LEU A CG  
800  C CD1 . LEU A 89  ? 0.5857 0.6652 0.6125 0.0268  0.0201  -0.0641 607 LEU A CD1 
801  C CD2 . LEU A 89  ? 0.5495 0.6710 0.5895 0.0563  0.0217  -0.0649 607 LEU A CD2 
802  N N   . PHE A 90  ? 0.5206 0.5128 0.4809 0.0377  0.0238  -0.0727 608 PHE A N   
803  C CA  . PHE A 90  ? 0.5528 0.5205 0.4945 0.0322  0.0202  -0.0761 608 PHE A CA  
804  C C   . PHE A 90  ? 0.6344 0.5462 0.5320 0.0429  0.0127  -0.0807 608 PHE A C   
805  O O   . PHE A 90  ? 0.6132 0.4997 0.4989 0.0458  0.0082  -0.0790 608 PHE A O   
806  C CB  . PHE A 90  ? 0.5511 0.5193 0.5130 0.0068  0.0123  -0.0739 608 PHE A CB  
807  C CG  . PHE A 90  ? 0.5330 0.5419 0.5269 -0.0018 0.0167  -0.0714 608 PHE A CG  
808  C CD1 . PHE A 90  ? 0.5352 0.5735 0.5565 -0.0055 0.0200  -0.0690 608 PHE A CD1 
809  C CD2 . PHE A 90  ? 0.5115 0.5224 0.5014 -0.0060 0.0159  -0.0712 608 PHE A CD2 
810  C CE1 . PHE A 90  ? 0.4590 0.5251 0.5045 -0.0140 0.0208  -0.0676 608 PHE A CE1 
811  C CE2 . PHE A 90  ? 0.4930 0.5327 0.5078 -0.0153 0.0180  -0.0675 608 PHE A CE2 
812  C CZ  . PHE A 90  ? 0.4621 0.5280 0.5053 -0.0196 0.0197  -0.0662 608 PHE A CZ  
813  N N   . GLU A 91  ? 0.7155 0.6021 0.5827 0.0488  0.0103  -0.0864 609 GLU A N   
814  C CA  . GLU A 91  ? 0.8098 0.6332 0.6269 0.0589  -0.0004 -0.0933 609 GLU A CA  
815  C C   . GLU A 91  ? 0.7860 0.5795 0.5815 0.0457  -0.0130 -0.0976 609 GLU A C   
816  O O   . GLU A 91  ? 0.7575 0.5802 0.5695 0.0373  -0.0094 -0.0955 609 GLU A O   
817  C CB  . GLU A 91  ? 0.8784 0.6933 0.6624 0.0953  0.0102  -0.0998 609 GLU A CB  
818  C CG  . GLU A 91  ? 0.9170 0.7451 0.6823 0.1098  0.0221  -0.1045 609 GLU A CG  
819  C CD  . GLU A 91  ? 0.9822 0.8229 0.7289 0.1486  0.0389  -0.1094 609 GLU A CD  
820  O OE1 . GLU A 91  ? 1.0019 0.8356 0.7483 0.1660  0.0373  -0.1102 609 GLU A OE1 
821  O OE2 . GLU A 91  ? 1.0122 0.8710 0.7442 0.1631  0.0542  -0.1117 609 GLU A OE2 
822  N N   . TYR A 92  ? 0.7803 0.5102 0.5357 0.0430  -0.0307 -0.1033 610 TYR A N   
823  C CA  . TYR A 92  ? 0.8114 0.5044 0.5378 0.0326  -0.0480 -0.1091 610 TYR A CA  
824  C C   . TYR A 92  ? 0.8329 0.5173 0.5145 0.0597  -0.0373 -0.1173 610 TYR A C   
825  O O   . TYR A 92  ? 0.8590 0.5300 0.5086 0.0900  -0.0253 -0.1234 610 TYR A O   
826  C CB  . TYR A 92  ? 0.8873 0.5098 0.5798 0.0213  -0.0728 -0.1134 610 TYR A CB  
827  C CG  . TYR A 92  ? 0.8759 0.5103 0.6146 -0.0115 -0.0826 -0.1026 610 TYR A CG  
828  C CD1 . TYR A 92  ? 0.8651 0.5363 0.6504 -0.0378 -0.0899 -0.0968 610 TYR A CD1 
829  C CD2 . TYR A 92  ? 0.8655 0.4755 0.6004 -0.0145 -0.0833 -0.0974 610 TYR A CD2 
830  C CE1 . TYR A 92  ? 0.8879 0.5781 0.7187 -0.0653 -0.0946 -0.0865 610 TYR A CE1 
831  C CE2 . TYR A 92  ? 0.8883 0.5125 0.6638 -0.0452 -0.0879 -0.0854 610 TYR A CE2 
832  C CZ  . TYR A 92  ? 0.9243 0.5923 0.7498 -0.0700 -0.0919 -0.0802 610 TYR A CZ  
833  O OH  . TYR A 92  ? 0.9674 0.6572 0.8365 -0.0981 -0.0924 -0.0679 610 TYR A OH  
834  N N   . SER A 93  ? 0.7927 0.4856 0.4708 0.0504  -0.0410 -0.1169 611 SER A N   
835  C CA  . SER A 93  ? 0.8399 0.5303 0.4749 0.0735  -0.0267 -0.1215 611 SER A CA  
836  C C   . SER A 93  ? 0.9811 0.5990 0.5382 0.0974  -0.0352 -0.1361 611 SER A C   
837  O O   . SER A 93  ? 1.1029 0.7201 0.6194 0.1265  -0.0159 -0.1413 611 SER A O   
838  C CB  . SER A 93  ? 0.8135 0.5149 0.4520 0.0562  -0.0337 -0.1166 611 SER A CB  
839  O OG  . SER A 93  ? 0.8202 0.4781 0.4479 0.0351  -0.0662 -0.1203 611 SER A OG  
840  N N   . ALA A 94  ? 1.0023 0.5588 0.5365 0.0856  -0.0632 -0.1425 612 ALA A N   
841  C CA  . ALA A 94  ? 1.0986 0.5724 0.5531 0.1067  -0.0771 -0.1581 612 ALA A CA  
842  C C   . ALA A 94  ? 1.1361 0.5563 0.5907 0.0834  -0.1074 -0.1592 612 ALA A C   
843  O O   . ALA A 94  ? 1.0512 0.4987 0.5629 0.0482  -0.1193 -0.1483 612 ALA A O   
844  C CB  . ALA A 94  ? 1.1673 0.6009 0.5604 0.1111  -0.0887 -0.1670 612 ALA A CB  
845  N N   . THR A 95  ? 1.1883 0.5432 0.5883 0.1022  -0.1172 -0.1674 613 THR A N   
846  C CA  . THR A 95  ? 1.2561 0.5648 0.6599 0.0775  -0.1442 -0.1623 613 THR A CA  
847  C C   . THR A 95  ? 1.1990 0.4976 0.6209 0.0374  -0.1748 -0.1572 613 THR A C   
848  O O   . THR A 95  ? 1.1595 0.4573 0.6204 0.0037  -0.1911 -0.1478 613 THR A O   
849  C CB  . THR A 95  ? 1.3803 0.6276 0.7248 0.1045  -0.1505 -0.1671 613 THR A CB  
850  O OG1 . THR A 95  ? 1.4982 0.7112 0.7921 0.1141  -0.1623 -0.1737 613 THR A OG1 
851  C CG2 . THR A 95  ? 1.3214 0.5902 0.6559 0.1482  -0.1202 -0.1709 613 THR A CG2 
852  N N   . ASP A 96  ? 1.2260 0.5221 0.6236 0.0406  -0.1819 -0.1615 614 ASP A N   
853  C CA  . ASP A 96  ? 1.2792 0.5712 0.6960 0.0070  -0.2126 -0.1564 614 ASP A CA  
854  C C   . ASP A 96  ? 1.1738 0.5289 0.6517 -0.0154 -0.2103 -0.1503 614 ASP A C   
855  O O   . ASP A 96  ? 1.1526 0.5177 0.6616 -0.0431 -0.2351 -0.1441 614 ASP A O   
856  C CB  . ASP A 96  ? 1.4409 0.6876 0.7930 0.0227  -0.2269 -0.1634 614 ASP A CB  
857  C CG  . ASP A 96  ? 1.6492 0.8251 0.9433 0.0374  -0.2403 -0.1683 614 ASP A CG  
858  O OD1 . ASP A 96  ? 1.6983 0.8533 1.0104 0.0171  -0.2557 -0.1627 614 ASP A OD1 
859  O OD2 . ASP A 96  ? 1.7487 0.8886 0.9774 0.0690  -0.2350 -0.1769 614 ASP A OD2 
860  N N   . ASN A 97  ? 1.0844 0.4834 0.5813 -0.0029 -0.1826 -0.1517 615 ASN A N   
861  C CA  . ASN A 97  ? 1.0473 0.5187 0.6121 -0.0212 -0.1758 -0.1404 615 ASN A CA  
862  C C   . ASN A 97  ? 1.0114 0.5348 0.6531 -0.0411 -0.1655 -0.1273 615 ASN A C   
863  O O   . ASN A 97  ? 1.0138 0.5284 0.6539 -0.0335 -0.1532 -0.1260 615 ASN A O   
864  C CB  . ASN A 97  ? 1.0433 0.5598 0.6043 0.0033  -0.1439 -0.1380 615 ASN A CB  
865  C CG  . ASN A 97  ? 1.1285 0.6015 0.6136 0.0221  -0.1493 -0.1479 615 ASN A CG  
866  O OD1 . ASN A 97  ? 1.1884 0.5999 0.6263 0.0170  -0.1796 -0.1564 615 ASN A OD1 
867  N ND2 . ASN A 97  ? 1.0822 0.5909 0.5580 0.0426  -0.1189 -0.1441 615 ASN A ND2 
868  N N   . TYR A 98  ? 0.9487 0.5250 0.6542 -0.0640 -0.1705 -0.1177 616 TYR A N   
869  C CA  . TYR A 98  ? 0.9366 0.5715 0.7139 -0.0786 -0.1550 -0.1055 616 TYR A CA  
870  C C   . TYR A 98  ? 0.8183 0.5187 0.6329 -0.0679 -0.1291 -0.0997 616 TYR A C   
871  O O   . TYR A 98  ? 0.8017 0.5485 0.6673 -0.0746 -0.1136 -0.0915 616 TYR A O   
872  C CB  . TYR A 98  ? 1.0412 0.6897 0.8692 -0.1129 -0.1793 -0.0986 616 TYR A CB  
873  C CG  . TYR A 98  ? 1.1772 0.8634 1.0618 -0.1305 -0.1661 -0.0865 616 TYR A CG  
874  C CD1 . TYR A 98  ? 1.1641 0.9197 1.1169 -0.1398 -0.1547 -0.0776 616 TYR A CD1 
875  C CD2 . TYR A 98  ? 1.3177 0.9657 1.1823 -0.1364 -0.1651 -0.0837 616 TYR A CD2 
876  C CE1 . TYR A 98  ? 1.1682 0.9588 1.1670 -0.1538 -0.1398 -0.0667 616 TYR A CE1 
877  C CE2 . TYR A 98  ? 1.3281 1.0091 1.2389 -0.1534 -0.1512 -0.0705 616 TYR A CE2 
878  C CZ  . TYR A 98  ? 1.2515 1.0060 1.2290 -0.1617 -0.1373 -0.0621 616 TYR A CZ  
879  O OH  . TYR A 98  ? 1.2540 1.0424 1.2722 -0.1762 -0.1204 -0.0492 616 TYR A OH  
880  N N   . THR A 99  ? 0.7726 0.4735 0.5588 -0.0524 -0.1245 -0.1033 617 THR A N   
881  C CA  . THR A 99  ? 0.6956 0.4502 0.5107 -0.0440 -0.1011 -0.0971 617 THR A CA  
882  C C   . THR A 99  ? 0.6703 0.4439 0.4841 -0.0257 -0.0729 -0.0962 617 THR A C   
883  O O   . THR A 99  ? 0.7106 0.4497 0.4833 -0.0097 -0.0690 -0.1025 617 THR A O   
884  C CB  . THR A 99  ? 0.7438 0.4876 0.5217 -0.0344 -0.1030 -0.0986 617 THR A CB  
885  O OG1 . THR A 99  ? 0.7453 0.4365 0.4517 -0.0165 -0.1042 -0.1080 617 THR A OG1 
886  C CG2 . THR A 99  ? 0.8118 0.5508 0.6040 -0.0516 -0.1316 -0.0970 617 THR A CG2 
887  N N   . LEU A 100 ? 0.6284 0.4552 0.4861 -0.0266 -0.0554 -0.0892 618 LEU A N   
888  C CA  . LEU A 100 ? 0.6506 0.5041 0.5184 -0.0125 -0.0329 -0.0872 618 LEU A CA  
889  C C   . LEU A 100 ? 0.6584 0.5393 0.5194 0.0011  -0.0146 -0.0849 618 LEU A C   
890  O O   . LEU A 100 ? 0.5975 0.4890 0.4621 -0.0062 -0.0163 -0.0810 618 LEU A O   
891  C CB  . LEU A 100 ? 0.5986 0.4903 0.5191 -0.0247 -0.0280 -0.0811 618 LEU A CB  
892  C CG  . LEU A 100 ? 0.6476 0.5226 0.5816 -0.0403 -0.0398 -0.0796 618 LEU A CG  
893  C CD1 . LEU A 100 ? 0.6283 0.5450 0.6100 -0.0499 -0.0309 -0.0734 618 LEU A CD1 
894  C CD2 . LEU A 100 ? 0.6796 0.5134 0.5769 -0.0306 -0.0405 -0.0824 618 LEU A CD2 
895  N N   . GLN A 101 ? 0.6545 0.5473 0.5064 0.0208  0.0026  -0.0861 619 GLN A N   
896  C CA  . GLN A 101 ? 0.5830 0.5167 0.4431 0.0315  0.0233  -0.0812 619 GLN A CA  
897  C C   . GLN A 101 ? 0.5746 0.5459 0.4682 0.0394  0.0343  -0.0789 619 GLN A C   
898  O O   . GLN A 101 ? 0.6032 0.5583 0.4977 0.0425  0.0278  -0.0818 619 GLN A O   
899  C CB  . GLN A 101 ? 0.6035 0.5176 0.4125 0.0541  0.0344  -0.0857 619 GLN A CB  
900  C CG  . GLN A 101 ? 0.7084 0.5972 0.4878 0.0803  0.0379  -0.0946 619 GLN A CG  
901  C CD  . GLN A 101 ? 0.8201 0.6833 0.5414 0.1069  0.0491  -0.1016 619 GLN A CD  
902  O OE1 . GLN A 101 ? 0.8631 0.7028 0.5495 0.1024  0.0457  -0.1023 619 GLN A OE1 
903  N NE2 . GLN A 101 ? 0.8829 0.7492 0.5901 0.1377  0.0624  -0.1071 619 GLN A NE2 
904  N N   . ILE A 102 ? 0.5021 0.5225 0.4224 0.0409  0.0493  -0.0723 620 ILE A N   
905  C CA  . ILE A 102 ? 0.4643 0.5230 0.4158 0.0497  0.0566  -0.0703 620 ILE A CA  
906  C C   . ILE A 102 ? 0.4867 0.5371 0.4119 0.0805  0.0652  -0.0758 620 ILE A C   
907  O O   . ILE A 102 ? 0.5228 0.5680 0.4186 0.0968  0.0769  -0.0781 620 ILE A O   
908  C CB  . ILE A 102 ? 0.4381 0.5519 0.4283 0.0394  0.0666  -0.0613 620 ILE A CB  
909  C CG1 . ILE A 102 ? 0.4255 0.5391 0.4391 0.0128  0.0547  -0.0578 620 ILE A CG1 
910  C CG2 . ILE A 102 ? 0.3909 0.5481 0.4118 0.0519  0.0723  -0.0597 620 ILE A CG2 
911  C CD1 . ILE A 102 ? 0.4262 0.5810 0.4718 -0.0017 0.0601  -0.0487 620 ILE A CD1 
912  N N   . ASN A 103 ? 0.4701 0.5153 0.4008 0.0908  0.0595  -0.0782 621 ASN A N   
913  C CA  . ASN A 103 ? 0.5403 0.5754 0.4472 0.1241  0.0651  -0.0837 621 ASN A CA  
914  C C   . ASN A 103 ? 0.5646 0.6669 0.5041 0.1406  0.0826  -0.0792 621 ASN A C   
915  O O   . ASN A 103 ? 0.5826 0.7324 0.5684 0.1295  0.0811  -0.0726 621 ASN A O   
916  C CB  . ASN A 103 ? 0.5713 0.5789 0.4736 0.1286  0.0518  -0.0849 621 ASN A CB  
917  C CG  . ASN A 103 ? 0.6971 0.6791 0.5666 0.1654  0.0529  -0.0912 621 ASN A CG  
918  O OD1 . ASN A 103 ? 0.7430 0.7412 0.6014 0.1919  0.0666  -0.0954 621 ASN A OD1 
919  N ND2 . ASN A 103 ? 0.7639 0.7041 0.6153 0.1687  0.0393  -0.0914 621 ASN A ND2 
920  N N   . PRO A 104 ? 0.6545 0.7649 0.5725 0.1666  0.0993  -0.0824 622 PRO A N   
921  C CA  . PRO A 104 ? 0.6835 0.8687 0.6416 0.1835  0.1179  -0.0765 622 PRO A CA  
922  C C   . PRO A 104 ? 0.7012 0.9114 0.6871 0.2026  0.1101  -0.0771 622 PRO A C   
923  O O   . PRO A 104 ? 0.7277 1.0077 0.7683 0.1991  0.1144  -0.0693 622 PRO A O   
924  C CB  . PRO A 104 ? 0.7276 0.9034 0.6438 0.2148  0.1382  -0.0824 622 PRO A CB  
925  C CG  . PRO A 104 ? 0.7637 0.8477 0.6118 0.2209  0.1233  -0.0946 622 PRO A CG  
926  C CD  . PRO A 104 ? 0.7127 0.7680 0.5695 0.1808  0.1025  -0.0911 622 PRO A CD  
927  N N   . ASN A 105 ? 0.7112 0.8635 0.6598 0.2213  0.0963  -0.0853 623 ASN A N   
928  C CA  . ASN A 105 ? 0.6992 0.8630 0.6640 0.2411  0.0853  -0.0852 623 ASN A CA  
929  C C   . ASN A 105 ? 0.6138 0.7702 0.5975 0.2116  0.0665  -0.0798 623 ASN A C   
930  O O   . ASN A 105 ? 0.6150 0.7479 0.5878 0.2242  0.0524  -0.0803 623 ASN A O   
931  C CB  . ASN A 105 ? 0.7844 0.8811 0.6922 0.2767  0.0790  -0.0953 623 ASN A CB  
932  C CG  . ASN A 105 ? 0.8840 0.9797 0.7625 0.3113  0.0982  -0.1036 623 ASN A CG  
933  O OD1 . ASN A 105 ? 0.8844 1.0538 0.7998 0.3263  0.1186  -0.1002 623 ASN A OD1 
934  N ND2 . ASN A 105 ? 0.9797 0.9913 0.7901 0.3235  0.0920  -0.1142 623 ASN A ND2 
935  N N   . SER A 106 ? 0.5001 0.6731 0.5074 0.1749  0.0662  -0.0746 624 SER A N   
936  C CA  A SER A 106 ? 0.4693 0.6320 0.4884 0.1494  0.0509  -0.0712 624 SER A CA  
937  C CA  B SER A 106 ? 0.4715 0.6344 0.4908 0.1493  0.0509  -0.0712 624 SER A CA  
938  C C   . SER A 106 ? 0.4852 0.6867 0.5344 0.1591  0.0412  -0.0680 624 SER A C   
939  O O   . SER A 106 ? 0.5428 0.7171 0.5799 0.1536  0.0274  -0.0671 624 SER A O   
940  C CB  A SER A 106 ? 0.4098 0.5898 0.4518 0.1147  0.0530  -0.0673 624 SER A CB  
941  C CB  B SER A 106 ? 0.4078 0.5888 0.4504 0.1147  0.0530  -0.0673 624 SER A CB  
942  O OG  A SER A 106 ? 0.3662 0.5639 0.4341 0.0969  0.0417  -0.0643 624 SER A OG  
943  O OG  B SER A 106 ? 0.3646 0.6099 0.4496 0.1103  0.0615  -0.0618 624 SER A OG  
944  N N   . GLY A 107 ? 0.4891 0.7556 0.5777 0.1731  0.0478  -0.0653 625 GLY A N   
945  C CA  . GLY A 107 ? 0.5043 0.8129 0.6265 0.1811  0.0342  -0.0623 625 GLY A CA  
946  C C   . GLY A 107 ? 0.5346 0.8209 0.6333 0.2182  0.0244  -0.0653 625 GLY A C   
947  O O   . GLY A 107 ? 0.5707 0.8710 0.6824 0.2232  0.0066  -0.0629 625 GLY A O   
948  N N   . LEU A 108 ? 0.5752 0.8206 0.6341 0.2453  0.0331  -0.0707 626 LEU A N   
949  C CA  . LEU A 108 ? 0.6782 0.8993 0.7124 0.2860  0.0235  -0.0738 626 LEU A CA  
950  C C   . LEU A 108 ? 0.7867 0.9570 0.7917 0.2794  0.0015  -0.0706 626 LEU A C   
951  O O   . LEU A 108 ? 0.8328 1.0137 0.8422 0.3035  -0.0138 -0.0686 626 LEU A O   
952  C CB  . LEU A 108 ? 0.7313 0.8953 0.7133 0.3119  0.0338  -0.0820 626 LEU A CB  
953  C CG  . LEU A 108 ? 0.7795 0.9911 0.7780 0.3540  0.0500  -0.0868 626 LEU A CG  
954  C CD1 . LEU A 108 ? 0.8510 0.9984 0.7888 0.3757  0.0612  -0.0972 626 LEU A CD1 
955  C CD2 . LEU A 108 ? 0.7399 0.9761 0.7546 0.3930  0.0362  -0.0863 626 LEU A CD2 
956  N N   . CYS A 109 ? 0.8915 1.0089 0.8669 0.2477  -0.0002 -0.0690 627 CYS A N   
957  C CA  . CYS A 109 ? 1.0488 1.1192 0.9935 0.2387  -0.0161 -0.0638 627 CYS A CA  
958  C C   . CYS A 109 ? 0.9377 1.0375 0.9085 0.2066  -0.0210 -0.0598 627 CYS A C   
959  O O   . CYS A 109 ? 0.9645 1.0407 0.9143 0.2041  -0.0340 -0.0553 627 CYS A O   
960  C CB  . CYS A 109 ? 1.2868 1.2741 1.1770 0.2274  -0.0148 -0.0633 627 CYS A CB  
961  S SG  . CYS A 109 ? 1.4020 1.3822 1.3003 0.1798  -0.0049 -0.0620 627 CYS A SG  
962  N N   . ASN A 110 ? 0.8133 0.9582 0.8230 0.1837  -0.0112 -0.0615 628 ASN A N   
963  C CA  . ASN A 110 ? 0.7035 0.8731 0.7364 0.1554  -0.0169 -0.0598 628 ASN A CA  
964  C C   . ASN A 110 ? 0.6250 0.8695 0.7130 0.1567  -0.0206 -0.0597 628 ASN A C   
965  O O   . ASN A 110 ? 0.6016 0.8809 0.7204 0.1429  -0.0086 -0.0597 628 ASN A O   
966  C CB  . ASN A 110 ? 0.6533 0.8040 0.6827 0.1251  -0.0056 -0.0609 628 ASN A CB  
967  C CG  . ASN A 110 ? 0.6971 0.7848 0.6835 0.1237  -0.0001 -0.0604 628 ASN A CG  
968  O OD1 . ASN A 110 ? 0.7633 0.8106 0.7183 0.1218  -0.0057 -0.0565 628 ASN A OD1 
969  N ND2 . ASN A 110 ? 0.6773 0.7548 0.6598 0.1232  0.0100  -0.0634 628 ASN A ND2 
970  N N   . GLU A 111 ? 0.6017 0.8704 0.7016 0.1724  -0.0386 -0.0583 629 GLU A N   
971  C CA  . GLU A 111 ? 0.6285 0.9724 0.7871 0.1686  -0.0467 -0.0568 629 GLU A CA  
972  C C   . GLU A 111 ? 0.6059 0.9635 0.7852 0.1303  -0.0480 -0.0571 629 GLU A C   
973  O O   . GLU A 111 ? 0.5737 0.9852 0.8006 0.1160  -0.0436 -0.0544 629 GLU A O   
974  C CB  . GLU A 111 ? 0.7195 1.0795 0.8828 0.1889  -0.0725 -0.0557 629 GLU A CB  
975  C CG  . GLU A 111 ? 0.8041 1.2468 1.0345 0.1839  -0.0860 -0.0534 629 GLU A CG  
976  C CD  . GLU A 111 ? 0.9334 1.4093 1.1815 0.2192  -0.1059 -0.0518 629 GLU A CD  
977  O OE1 . GLU A 111 ? 0.9785 1.4598 1.2279 0.2166  -0.1351 -0.0518 629 GLU A OE1 
978  O OE2 . GLU A 111 ? 0.9796 1.4748 1.2379 0.2519  -0.0939 -0.0512 629 GLU A OE2 
979  N N   . ASP A 112 ? 0.6407 0.9482 0.7830 0.1139  -0.0529 -0.0598 630 ASP A N   
980  C CA  . ASP A 112 ? 0.6836 0.9912 0.8355 0.0823  -0.0551 -0.0622 630 ASP A CA  
981  C C   . ASP A 112 ? 0.6340 0.9187 0.7779 0.0664  -0.0346 -0.0627 630 ASP A C   
982  O O   . ASP A 112 ? 0.6087 0.8687 0.7403 0.0469  -0.0349 -0.0658 630 ASP A O   
983  C CB  . ASP A 112 ? 0.8083 1.0771 0.9229 0.0777  -0.0704 -0.0660 630 ASP A CB  
984  C CG  . ASP A 112 ? 0.9064 1.1849 1.0354 0.0527  -0.0830 -0.0707 630 ASP A CG  
985  O OD1 . ASP A 112 ? 0.9177 1.2389 1.0918 0.0380  -0.0857 -0.0690 630 ASP A OD1 
986  O OD2 . ASP A 112 ? 0.9640 1.2045 1.0562 0.0477  -0.0897 -0.0758 630 ASP A OD2 
987  N N   . HIS A 113 ? 0.6054 0.8966 0.7538 0.0766  -0.0178 -0.0603 631 HIS A N   
988  C CA  . HIS A 113 ? 0.5239 0.7855 0.6565 0.0641  -0.0023 -0.0611 631 HIS A CA  
989  C C   . HIS A 113 ? 0.3882 0.6681 0.5459 0.0370  -0.0009 -0.0600 631 HIS A C   
990  O O   . HIS A 113 ? 0.3943 0.6435 0.5368 0.0231  0.0041  -0.0617 631 HIS A O   
991  C CB  . HIS A 113 ? 0.5677 0.8275 0.6918 0.0829  0.0126  -0.0602 631 HIS A CB  
992  C CG  . HIS A 113 ? 0.5496 0.8676 0.7117 0.0887  0.0213  -0.0562 631 HIS A CG  
993  N ND1 . HIS A 113 ? 0.5599 0.8816 0.7174 0.0928  0.0397  -0.0550 631 HIS A ND1 
994  C CD2 . HIS A 113 ? 0.5556 0.9333 0.7615 0.0907  0.0148  -0.0523 631 HIS A CD2 
995  C CE1 . HIS A 113 ? 0.5543 0.9378 0.7511 0.0974  0.0481  -0.0495 631 HIS A CE1 
996  N NE2 . HIS A 113 ? 0.5191 0.9406 0.7505 0.0949  0.0327  -0.0473 631 HIS A NE2 
997  N N   . LEU A 114 ? 0.3659 0.6945 0.5628 0.0283  -0.0072 -0.0563 632 LEU A N   
998  C CA  . LEU A 114 ? 0.3384 0.6776 0.5554 0.0008  -0.0066 -0.0532 632 LEU A CA  
999  C C   . LEU A 114 ? 0.3682 0.6714 0.5686 -0.0157 -0.0202 -0.0594 632 LEU A C   
1000 O O   . LEU A 114 ? 0.3709 0.6541 0.5669 -0.0323 -0.0173 -0.0596 632 LEU A O   
1001 C CB  . LEU A 114 ? 0.2612 0.6619 0.5270 -0.0088 -0.0110 -0.0455 632 LEU A CB  
1002 C CG  . LEU A 114 ? 0.3600 0.8042 0.6466 0.0058  0.0096  -0.0380 632 LEU A CG  
1003 C CD1 . LEU A 114 ? 0.3630 0.8716 0.7036 -0.0139 0.0102  -0.0267 632 LEU A CD1 
1004 C CD2 . LEU A 114 ? 0.3375 0.7471 0.5913 0.0090  0.0300  -0.0379 632 LEU A CD2 
1005 N N   . SER A 115 ? 0.4064 0.6986 0.5934 -0.0088 -0.0354 -0.0650 633 SER A N   
1006 C CA  . SER A 115 ? 0.4650 0.7194 0.6278 -0.0187 -0.0445 -0.0727 633 SER A CA  
1007 C C   . SER A 115 ? 0.4374 0.6517 0.5685 -0.0123 -0.0301 -0.0753 633 SER A C   
1008 O O   . SER A 115 ? 0.3888 0.5779 0.5080 -0.0212 -0.0302 -0.0804 633 SER A O   
1009 C CB  . SER A 115 ? 0.5842 0.8355 0.7339 -0.0121 -0.0645 -0.0779 633 SER A CB  
1010 O OG  . SER A 115 ? 0.7154 0.9517 0.8377 0.0099  -0.0603 -0.0774 633 SER A OG  
1011 N N   . TYR A 116 ? 0.4134 0.6214 0.5321 0.0030  -0.0187 -0.0720 634 TYR A N   
1012 C CA  . TYR A 116 ? 0.4384 0.6123 0.5341 0.0039  -0.0065 -0.0726 634 TYR A CA  
1013 C C   . TYR A 116 ? 0.3873 0.5590 0.4952 -0.0091 0.0005  -0.0718 634 TYR A C   
1014 O O   . TYR A 116 ? 0.3733 0.5239 0.4737 -0.0157 0.0035  -0.0745 634 TYR A O   
1015 C CB  . TYR A 116 ? 0.4802 0.6409 0.5578 0.0205  0.0004  -0.0688 634 TYR A CB  
1016 C CG  . TYR A 116 ? 0.5248 0.6778 0.5823 0.0359  -0.0074 -0.0678 634 TYR A CG  
1017 C CD1 . TYR A 116 ? 0.5700 0.7236 0.6198 0.0340  -0.0189 -0.0708 634 TYR A CD1 
1018 C CD2 . TYR A 116 ? 0.5060 0.6443 0.5455 0.0540  -0.0052 -0.0641 634 TYR A CD2 
1019 C CE1 . TYR A 116 ? 0.6547 0.7970 0.6797 0.0491  -0.0281 -0.0689 634 TYR A CE1 
1020 C CE2 . TYR A 116 ? 0.5699 0.6954 0.5864 0.0696  -0.0144 -0.0618 634 TYR A CE2 
1021 C CZ  . TYR A 116 ? 0.6395 0.7682 0.6488 0.0668  -0.0259 -0.0635 634 TYR A CZ  
1022 O OH  . TYR A 116 ? 0.6922 0.8043 0.6727 0.0832  -0.0371 -0.0604 634 TYR A OH  
1023 N N   . PHE A 117 ? 0.3435 0.5388 0.4700 -0.0118 0.0036  -0.0674 635 PHE A N   
1024 C CA  . PHE A 117 ? 0.3836 0.5725 0.5143 -0.0235 0.0091  -0.0651 635 PHE A CA  
1025 C C   . PHE A 117 ? 0.4071 0.5905 0.5472 -0.0403 -0.0001 -0.0671 635 PHE A C   
1026 O O   . PHE A 117 ? 0.3403 0.5025 0.4747 -0.0468 0.0005  -0.0681 635 PHE A O   
1027 C CB  . PHE A 117 ? 0.3309 0.5464 0.4732 -0.0212 0.0178  -0.0584 635 PHE A CB  
1028 C CG  . PHE A 117 ? 0.3455 0.5501 0.4675 -0.0029 0.0280  -0.0586 635 PHE A CG  
1029 C CD1 . PHE A 117 ? 0.3626 0.5326 0.4612 -0.0037 0.0313  -0.0603 635 PHE A CD1 
1030 C CD2 . PHE A 117 ? 0.3257 0.5513 0.4505 0.0165  0.0313  -0.0579 635 PHE A CD2 
1031 C CE1 . PHE A 117 ? 0.3498 0.5002 0.4234 0.0124  0.0370  -0.0621 635 PHE A CE1 
1032 C CE2 . PHE A 117 ? 0.3748 0.5806 0.4740 0.0362  0.0389  -0.0598 635 PHE A CE2 
1033 C CZ  . PHE A 117 ? 0.3350 0.5001 0.4061 0.0331  0.0414  -0.0623 635 PHE A CZ  
1034 N N   . LYS A 118 ? 0.3895 0.5887 0.5425 -0.0467 -0.0116 -0.0683 636 LYS A N   
1035 C CA  . LYS A 118 ? 0.3919 0.5740 0.5453 -0.0608 -0.0238 -0.0726 636 LYS A CA  
1036 C C   . LYS A 118 ? 0.4210 0.5716 0.5523 -0.0526 -0.0237 -0.0818 636 LYS A C   
1037 O O   . LYS A 118 ? 0.4143 0.5431 0.5416 -0.0577 -0.0271 -0.0855 636 LYS A O   
1038 C CB  . LYS A 118 ? 0.4117 0.6115 0.5789 -0.0695 -0.0403 -0.0735 636 LYS A CB  
1039 C CG  . LYS A 118 ? 0.4821 0.6532 0.6414 -0.0830 -0.0568 -0.0802 636 LYS A CG  
1040 C CD  . LYS A 118 ? 0.5642 0.7539 0.7440 -0.1009 -0.0760 -0.0776 636 LYS A CD  
1041 C CE  . LYS A 118 ? 0.6208 0.7691 0.7830 -0.1126 -0.0963 -0.0867 636 LYS A CE  
1042 N NZ  . LYS A 118 ? 0.6259 0.7875 0.8066 -0.1335 -0.1203 -0.0849 636 LYS A NZ  
1043 N N   . PHE A 119 ? 0.4014 0.5497 0.5178 -0.0389 -0.0190 -0.0847 637 PHE A N   
1044 C CA  . PHE A 119 ? 0.4268 0.5527 0.5247 -0.0315 -0.0133 -0.0908 637 PHE A CA  
1045 C C   . PHE A 119 ? 0.4012 0.5195 0.5050 -0.0328 -0.0032 -0.0881 637 PHE A C   
1046 O O   . PHE A 119 ? 0.4051 0.5115 0.5090 -0.0321 -0.0023 -0.0930 637 PHE A O   
1047 C CB  . PHE A 119 ? 0.4208 0.5444 0.4985 -0.0192 -0.0084 -0.0903 637 PHE A CB  
1048 C CG  . PHE A 119 ? 0.4166 0.5249 0.4798 -0.0139 0.0047  -0.0912 637 PHE A CG  
1049 C CD1 . PHE A 119 ? 0.4537 0.5507 0.5052 -0.0105 0.0061  -0.0991 637 PHE A CD1 
1050 C CD2 . PHE A 119 ? 0.4356 0.5408 0.4968 -0.0125 0.0159  -0.0839 637 PHE A CD2 
1051 C CE1 . PHE A 119 ? 0.5015 0.5943 0.5459 -0.0056 0.0219  -0.0983 637 PHE A CE1 
1052 C CE2 . PHE A 119 ? 0.4778 0.5751 0.5326 -0.0122 0.0284  -0.0821 637 PHE A CE2 
1053 C CZ  . PHE A 119 ? 0.4761 0.5721 0.5256 -0.0086 0.0332  -0.0885 637 PHE A CZ  
1054 N N   . ILE A 120 ? 0.3660 0.4906 0.4740 -0.0328 0.0030  -0.0813 638 ILE A N   
1055 C CA  . ILE A 120 ? 0.3971 0.5121 0.5086 -0.0355 0.0076  -0.0791 638 ILE A CA  
1056 C C   . ILE A 120 ? 0.3320 0.4417 0.4533 -0.0438 0.0003  -0.0797 638 ILE A C   
1057 O O   . ILE A 120 ? 0.3368 0.4367 0.4629 -0.0440 -0.0010 -0.0815 638 ILE A O   
1058 C CB  . ILE A 120 ? 0.3868 0.5013 0.4916 -0.0327 0.0124  -0.0736 638 ILE A CB  
1059 C CG1 . ILE A 120 ? 0.4459 0.5569 0.5362 -0.0229 0.0169  -0.0724 638 ILE A CG1 
1060 C CG2 . ILE A 120 ? 0.3064 0.4061 0.4107 -0.0369 0.0123  -0.0723 638 ILE A CG2 
1061 C CD1 . ILE A 120 ? 0.4686 0.5711 0.5460 -0.0158 0.0201  -0.0691 638 ILE A CD1 
1062 N N   . GLY A 121 ? 0.3424 0.4590 0.4681 -0.0514 -0.0056 -0.0770 639 GLY A N   
1063 C CA  . GLY A 121 ? 0.3917 0.4955 0.5208 -0.0612 -0.0140 -0.0755 639 GLY A CA  
1064 C C   . GLY A 121 ? 0.4207 0.5059 0.5477 -0.0579 -0.0222 -0.0845 639 GLY A C   
1065 O O   . GLY A 121 ? 0.4458 0.5139 0.5734 -0.0571 -0.0273 -0.0855 639 GLY A O   
1066 N N   . ARG A 122 ? 0.4125 0.4986 0.5335 -0.0530 -0.0244 -0.0918 640 ARG A N   
1067 C CA  . ARG A 122 ? 0.4107 0.4762 0.5222 -0.0449 -0.0300 -0.1027 640 ARG A CA  
1068 C C   . ARG A 122 ? 0.4381 0.5055 0.5545 -0.0321 -0.0193 -0.1057 640 ARG A C   
1069 O O   . ARG A 122 ? 0.4755 0.5287 0.5938 -0.0248 -0.0236 -0.1114 640 ARG A O   
1070 C CB  . ARG A 122 ? 0.3800 0.4439 0.4756 -0.0402 -0.0338 -0.1104 640 ARG A CB  
1071 C CG  . ARG A 122 ? 0.3924 0.4518 0.4874 -0.0545 -0.0514 -0.1100 640 ARG A CG  
1072 C CD  . ARG A 122 ? 0.4580 0.5085 0.5315 -0.0484 -0.0607 -0.1201 640 ARG A CD  
1073 N NE  . ARG A 122 ? 0.5260 0.5692 0.6016 -0.0652 -0.0829 -0.1208 640 ARG A NE  
1074 C CZ  . ARG A 122 ? 0.5697 0.5960 0.6234 -0.0640 -0.0999 -0.1310 640 ARG A CZ  
1075 N NH1 . ARG A 122 ? 0.5815 0.5953 0.6043 -0.0441 -0.0941 -0.1413 640 ARG A NH1 
1076 N NH2 . ARG A 122 ? 0.5480 0.5692 0.6093 -0.0840 -0.1233 -0.1301 640 ARG A NH2 
1077 N N   . VAL A 123 ? 0.4013 0.4862 0.5213 -0.0293 -0.0062 -0.1012 641 VAL A N   
1078 C CA  . VAL A 123 ? 0.3936 0.4868 0.5257 -0.0223 0.0038  -0.1014 641 VAL A CA  
1079 C C   . VAL A 123 ? 0.4526 0.5429 0.6014 -0.0262 -0.0038 -0.0978 641 VAL A C   
1080 O O   . VAL A 123 ? 0.4687 0.5623 0.6326 -0.0182 -0.0043 -0.1013 641 VAL A O   
1081 C CB  . VAL A 123 ? 0.4624 0.5680 0.5921 -0.0237 0.0164  -0.0949 641 VAL A CB  
1082 C CG1 . VAL A 123 ? 0.3767 0.4949 0.5262 -0.0231 0.0251  -0.0920 641 VAL A CG1 
1083 C CG2 . VAL A 123 ? 0.4917 0.5960 0.5993 -0.0172 0.0227  -0.0979 641 VAL A CG2 
1084 N N   . ALA A 124 ? 0.4184 0.5037 0.5636 -0.0365 -0.0097 -0.0906 642 ALA A N   
1085 C CA  . ALA A 124 ? 0.4341 0.5101 0.5855 -0.0401 -0.0192 -0.0867 642 ALA A CA  
1086 C C   . ALA A 124 ? 0.4370 0.4940 0.5877 -0.0365 -0.0316 -0.0906 642 ALA A C   
1087 O O   . ALA A 124 ? 0.4184 0.4704 0.5800 -0.0302 -0.0396 -0.0916 642 ALA A O   
1088 C CB  . ALA A 124 ? 0.4268 0.4982 0.5649 -0.0498 -0.0202 -0.0784 642 ALA A CB  
1089 N N   . GLY A 125 ? 0.4412 0.4854 0.5792 -0.0405 -0.0361 -0.0928 643 GLY A N   
1090 C CA  . GLY A 125 ? 0.4448 0.4605 0.5759 -0.0371 -0.0501 -0.0975 643 GLY A CA  
1091 C C   . GLY A 125 ? 0.5077 0.5228 0.6452 -0.0167 -0.0484 -0.1097 643 GLY A C   
1092 O O   . GLY A 125 ? 0.5985 0.5941 0.7372 -0.0061 -0.0594 -0.1137 643 GLY A O   
1093 N N   . MET A 126 ? 0.4841 0.5205 0.6239 -0.0090 -0.0337 -0.1153 644 MET A N   
1094 C CA  . MET A 126 ? 0.4867 0.5298 0.6324 0.0122  -0.0259 -0.1259 644 MET A CA  
1095 C C   . MET A 126 ? 0.4736 0.5395 0.6510 0.0200  -0.0233 -0.1227 644 MET A C   
1096 O O   . MET A 126 ? 0.5355 0.6010 0.7238 0.0392  -0.0256 -0.1303 644 MET A O   
1097 C CB  . MET A 126 ? 0.5228 0.5840 0.6593 0.0164  -0.0082 -0.1291 644 MET A CB  
1098 C CG  . MET A 126 ? 0.5599 0.5964 0.6634 0.0171  -0.0145 -0.1376 644 MET A CG  
1099 S SD  . MET A 126 ? 0.5456 0.5993 0.6309 0.0195  0.0029  -0.1374 644 MET A SD  
1100 C CE  . MET A 126 ? 0.4935 0.5619 0.5804 0.0442  0.0243  -0.1455 644 MET A CE  
1101 N N   . ALA A 127 ? 0.4097 0.4951 0.6024 0.0065  -0.0202 -0.1121 645 ALA A N   
1102 C CA  . ALA A 127 ? 0.4276 0.5351 0.6527 0.0098  -0.0227 -0.1084 645 ALA A CA  
1103 C C   . ALA A 127 ? 0.4655 0.5507 0.6925 0.0163  -0.0440 -0.1090 645 ALA A C   
1104 O O   . ALA A 127 ? 0.4847 0.5842 0.7381 0.0324  -0.0488 -0.1127 645 ALA A O   
1105 C CB  . ALA A 127 ? 0.3591 0.4782 0.5895 -0.0081 -0.0208 -0.0980 645 ALA A CB  
1106 N N   . VAL A 128 ? 0.4925 0.5438 0.6922 0.0046  -0.0568 -0.1042 646 VAL A N   
1107 C CA  . VAL A 128 ? 0.5555 0.5761 0.7474 0.0089  -0.0780 -0.1023 646 VAL A CA  
1108 C C   . VAL A 128 ? 0.5452 0.5450 0.7326 0.0297  -0.0843 -0.1136 646 VAL A C   
1109 O O   . VAL A 128 ? 0.5568 0.5499 0.7566 0.0473  -0.0976 -0.1165 646 VAL A O   
1110 C CB  . VAL A 128 ? 0.5260 0.5158 0.6862 -0.0110 -0.0856 -0.0921 646 VAL A CB  
1111 C CG1 . VAL A 128 ? 0.5207 0.4696 0.6639 -0.0080 -0.1073 -0.0881 646 VAL A CG1 
1112 C CG2 . VAL A 128 ? 0.5037 0.5094 0.6634 -0.0248 -0.0803 -0.0831 646 VAL A CG2 
1113 N N   . TYR A 129 ? 0.5047 0.4914 0.6721 0.0300  -0.0769 -0.1210 647 TYR A N   
1114 C CA  . TYR A 129 ? 0.5473 0.5025 0.6993 0.0505  -0.0850 -0.1340 647 TYR A CA  
1115 C C   . TYR A 129 ? 0.5931 0.5788 0.7727 0.0806  -0.0748 -0.1446 647 TYR A C   
1116 O O   . TYR A 129 ? 0.6761 0.6396 0.8536 0.1050  -0.0864 -0.1535 647 TYR A O   
1117 C CB  . TYR A 129 ? 0.5124 0.4474 0.6348 0.0435  -0.0813 -0.1410 647 TYR A CB  
1118 C CG  . TYR A 129 ? 0.5384 0.4234 0.6321 0.0609  -0.0958 -0.1549 647 TYR A CG  
1119 C CD1 . TYR A 129 ? 0.5896 0.4197 0.6562 0.0473  -0.1191 -0.1510 647 TYR A CD1 
1120 C CD2 . TYR A 129 ? 0.5771 0.4668 0.6675 0.0911  -0.0857 -0.1717 647 TYR A CD2 
1121 C CE1 . TYR A 129 ? 0.6937 0.4678 0.7288 0.0625  -0.1359 -0.1644 647 TYR A CE1 
1122 C CE2 . TYR A 129 ? 0.6430 0.4792 0.7001 0.1108  -0.1003 -0.1869 647 TYR A CE2 
1123 C CZ  . TYR A 129 ? 0.7425 0.5175 0.7710 0.0960  -0.1273 -0.1837 647 TYR A CZ  
1124 O OH  . TYR A 129 ? 0.8618 0.5733 0.8516 0.1147  -0.1452 -0.1995 647 TYR A OH  
1125 N N   . HIS A 130 ? 0.5230 0.6253 0.6309 0.0035  -0.0094 -0.0634 648 HIS A N   
1126 C CA  . HIS A 130 ? 0.5238 0.6575 0.6529 0.0079  -0.0070 -0.0696 648 HIS A CA  
1127 C C   . HIS A 130 ? 0.5450 0.6906 0.6928 0.0168  -0.0166 -0.0698 648 HIS A C   
1128 O O   . HIS A 130 ? 0.5440 0.7220 0.7154 0.0171  -0.0136 -0.0769 648 HIS A O   
1129 C CB  . HIS A 130 ? 0.4939 0.6590 0.6279 -0.0036 0.0022  -0.0650 648 HIS A CB  
1130 C CG  . HIS A 130 ? 0.5867 0.7626 0.7061 -0.0075 0.0102  -0.0721 648 HIS A CG  
1131 N ND1 . HIS A 130 ? 0.6306 0.8201 0.7545 -0.0038 0.0170  -0.0888 648 HIS A ND1 
1132 C CD2 . HIS A 130 ? 0.6058 0.7886 0.7081 -0.0138 0.0124  -0.0690 648 HIS A CD2 
1133 C CE1 . HIS A 130 ? 0.6287 0.8355 0.7403 -0.0097 0.0229  -0.0986 648 HIS A CE1 
1134 N NE2 . HIS A 130 ? 0.6143 0.8208 0.7126 -0.0147 0.0194  -0.0869 648 HIS A NE2 
1135 N N   . GLY A 131 ? 0.5495 0.6756 0.6886 0.0243  -0.0273 -0.0652 649 GLY A N   
1136 C CA  . GLY A 131 ? 0.5314 0.6814 0.6889 0.0352  -0.0385 -0.0717 649 GLY A CA  
1137 C C   . GLY A 131 ? 0.4888 0.6701 0.6748 0.0171  -0.0358 -0.0761 649 GLY A C   
1138 O O   . GLY A 131 ? 0.4602 0.6789 0.6749 0.0208  -0.0399 -0.0913 649 GLY A O   
1139 N N   . LYS A 132 ? 0.4858 0.6540 0.6660 -0.0015 -0.0261 -0.0646 650 LYS A N   
1140 C CA  . LYS A 132 ? 0.5104 0.6941 0.7149 -0.0189 -0.0153 -0.0655 650 LYS A CA  
1141 C C   . LYS A 132 ? 0.5019 0.6643 0.6978 -0.0257 -0.0197 -0.0590 650 LYS A C   
1142 O O   . LYS A 132 ? 0.5232 0.6583 0.6904 -0.0193 -0.0287 -0.0494 650 LYS A O   
1143 C CB  . LYS A 132 ? 0.5830 0.7676 0.7851 -0.0293 0.0056  -0.0535 650 LYS A CB  
1144 C CG  . LYS A 132 ? 0.6594 0.8663 0.8674 -0.0229 0.0110  -0.0604 650 LYS A CG  
1145 C CD  . LYS A 132 ? 0.6804 0.9212 0.9276 -0.0290 0.0205  -0.0756 650 LYS A CD  
1146 C CE  . LYS A 132 ? 0.7036 0.9681 0.9566 -0.0211 0.0252  -0.0833 650 LYS A CE  
1147 N NZ  . LYS A 132 ? 0.7176 0.9972 0.9791 -0.0032 0.0073  -0.1005 650 LYS A NZ  
1148 N N   . LEU A 133 ? 0.5568 0.7314 0.7804 -0.0403 -0.0103 -0.0670 651 LEU A N   
1149 C CA  . LEU A 133 ? 0.6000 0.7577 0.8211 -0.0478 -0.0127 -0.0657 651 LEU A CA  
1150 C C   . LEU A 133 ? 0.5764 0.7068 0.7905 -0.0610 0.0101  -0.0463 651 LEU A C   
1151 O O   . LEU A 133 ? 0.5873 0.7203 0.8111 -0.0678 0.0326  -0.0394 651 LEU A O   
1152 C CB  . LEU A 133 ? 0.5969 0.7887 0.8566 -0.0551 -0.0159 -0.0940 651 LEU A CB  
1153 C CG  . LEU A 133 ? 0.5867 0.8136 0.8487 -0.0335 -0.0412 -0.1126 651 LEU A CG  
1154 C CD1 . LEU A 133 ? 0.5677 0.8476 0.8748 -0.0415 -0.0433 -0.1481 651 LEU A CD1 
1155 C CD2 . LEU A 133 ? 0.6058 0.8057 0.8275 -0.0149 -0.0598 -0.0995 651 LEU A CD2 
1156 N N   . LEU A 134 ? 0.5036 0.6075 0.6974 -0.0611 0.0056  -0.0357 652 LEU A N   
1157 C CA  . LEU A 134 ? 0.4833 0.5611 0.6708 -0.0693 0.0274  -0.0181 652 LEU A CA  
1158 C C   . LEU A 134 ? 0.5185 0.5945 0.7407 -0.0866 0.0423  -0.0342 652 LEU A C   
1159 O O   . LEU A 134 ? 0.5556 0.6525 0.7978 -0.0903 0.0268  -0.0595 652 LEU A O   
1160 C CB  . LEU A 134 ? 0.5362 0.5904 0.6885 -0.0610 0.0167  -0.0019 652 LEU A CB  
1161 C CG  . LEU A 134 ? 0.6024 0.6583 0.7235 -0.0490 0.0124  0.0127  652 LEU A CG  
1162 C CD1 . LEU A 134 ? 0.6363 0.6747 0.7306 -0.0445 0.0081  0.0255  652 LEU A CD1 
1163 C CD2 . LEU A 134 ? 0.6174 0.6845 0.7380 -0.0461 0.0336  0.0251  652 LEU A CD2 
1164 N N   . ASP A 135 ? 0.5673 0.6197 0.7962 -0.0957 0.0753  -0.0209 653 ASP A N   
1165 C CA  . ASP A 135 ? 0.6455 0.6868 0.9105 -0.1163 0.0992  -0.0378 653 ASP A CA  
1166 C C   . ASP A 135 ? 0.6964 0.6999 0.9408 -0.1142 0.1042  -0.0227 653 ASP A C   
1167 O O   . ASP A 135 ? 0.7458 0.7146 0.9691 -0.1071 0.1294  0.0066  653 ASP A O   
1168 C CB  . ASP A 135 ? 0.7532 0.7836 1.0420 -0.1286 0.1417  -0.0333 653 ASP A CB  
1169 C CG  . ASP A 135 ? 0.9006 0.9321 1.2426 -0.1569 0.1676  -0.0662 653 ASP A CG  
1170 O OD1 . ASP A 135 ? 0.9270 1.0067 1.3062 -0.1681 0.1512  -0.1050 653 ASP A OD1 
1171 O OD2 . ASP A 135 ? 0.9857 0.9721 1.3331 -0.1670 0.2061  -0.0555 653 ASP A OD2 
1172 N N   . GLY A 136 ? 0.6938 0.7067 0.9422 -0.1169 0.0807  -0.0421 654 GLY A N   
1173 C CA  . GLY A 136 ? 0.7560 0.7376 0.9875 -0.1156 0.0826  -0.0326 654 GLY A CA  
1174 C C   . GLY A 136 ? 0.7865 0.7878 1.0069 -0.1091 0.0462  -0.0480 654 GLY A C   
1175 O O   . GLY A 136 ? 0.8508 0.8760 1.0565 -0.0963 0.0198  -0.0495 654 GLY A O   
1176 N N   . PHE A 137 ? 0.7124 0.7019 0.9382 -0.1161 0.0471  -0.0592 655 PHE A N   
1177 C CA  . PHE A 137 ? 0.7137 0.7212 0.9242 -0.1070 0.0152  -0.0714 655 PHE A CA  
1178 C C   . PHE A 137 ? 0.6362 0.6092 0.8192 -0.1023 0.0165  -0.0537 655 PHE A C   
1179 O O   . PHE A 137 ? 0.6159 0.5598 0.8096 -0.1121 0.0424  -0.0503 655 PHE A O   
1180 C CB  . PHE A 137 ? 0.7969 0.8458 1.0446 -0.1180 0.0073  -0.1142 655 PHE A CB  
1181 C CG  . PHE A 137 ? 0.9074 0.9518 1.2022 -0.1449 0.0407  -0.1386 655 PHE A CG  
1182 C CD1 . PHE A 137 ? 0.9608 0.9890 1.2670 -0.1570 0.0522  -0.1535 655 PHE A CD1 
1183 C CD2 . PHE A 137 ? 0.9478 1.0028 1.2779 -0.1595 0.0641  -0.1492 655 PHE A CD2 
1184 C CE1 . PHE A 137 ? 1.0274 1.0461 1.3806 -0.1845 0.0888  -0.1797 655 PHE A CE1 
1185 C CE2 . PHE A 137 ? 1.0053 1.0513 1.3821 -0.1873 0.1014  -0.1742 655 PHE A CE2 
1186 C CZ  . PHE A 137 ? 1.0455 1.0724 1.4350 -0.2004 0.1147  -0.1906 655 PHE A CZ  
1187 N N   . PHE A 138 ? 0.5753 0.5497 0.7236 -0.0865 -0.0085 -0.0430 656 PHE A N   
1188 C CA  . PHE A 138 ? 0.6117 0.5596 0.7315 -0.0803 -0.0102 -0.0261 656 PHE A CA  
1189 C C   . PHE A 138 ? 0.5393 0.4983 0.6556 -0.0789 -0.0276 -0.0451 656 PHE A C   
1190 O O   . PHE A 138 ? 0.5400 0.5320 0.6671 -0.0761 -0.0434 -0.0678 656 PHE A O   
1191 C CB  . PHE A 138 ? 0.6470 0.5892 0.7319 -0.0662 -0.0203 -0.0023 656 PHE A CB  
1192 C CG  . PHE A 138 ? 0.7346 0.6799 0.8208 -0.0641 -0.0083 0.0117  656 PHE A CG  
1193 C CD1 . PHE A 138 ? 0.7451 0.6744 0.8344 -0.0645 0.0168  0.0278  656 PHE A CD1 
1194 C CD2 . PHE A 138 ? 0.8083 0.7717 0.8906 -0.0588 -0.0198 0.0095  656 PHE A CD2 
1195 C CE1 . PHE A 138 ? 0.8121 0.7485 0.8982 -0.0587 0.0285  0.0418  656 PHE A CE1 
1196 C CE2 . PHE A 138 ? 0.8465 0.8173 0.9297 -0.0566 -0.0089 0.0200  656 PHE A CE2 
1197 C CZ  . PHE A 138 ? 0.8520 0.8119 0.9362 -0.0561 0.0144  0.0362  656 PHE A CZ  
1198 N N   . ILE A 139 ? 0.4666 0.4022 0.5662 -0.0776 -0.0242 -0.0359 657 ILE A N   
1199 C CA  . ILE A 139 ? 0.4815 0.4265 0.5702 -0.0734 -0.0405 -0.0503 657 ILE A CA  
1200 C C   . ILE A 139 ? 0.4849 0.4408 0.5425 -0.0560 -0.0630 -0.0427 657 ILE A C   
1201 O O   . ILE A 139 ? 0.5136 0.4596 0.5549 -0.0500 -0.0633 -0.0239 657 ILE A O   
1202 C CB  . ILE A 139 ? 0.4941 0.4100 0.5688 -0.0742 -0.0310 -0.0391 657 ILE A CB  
1203 C CG1 . ILE A 139 ? 0.4938 0.3902 0.5402 -0.0647 -0.0281 -0.0082 657 ILE A CG1 
1204 C CG2 . ILE A 139 ? 0.5546 0.4530 0.6602 -0.0891 -0.0039 -0.0486 657 ILE A CG2 
1205 C CD1 . ILE A 139 ? 0.5270 0.4040 0.5566 -0.0610 -0.0227 0.0021  657 ILE A CD1 
1206 N N   . ARG A 140 ? 0.5102 0.4869 0.5589 -0.0463 -0.0791 -0.0586 658 ARG A N   
1207 C CA  . ARG A 140 ? 0.5802 0.5590 0.5950 -0.0252 -0.0942 -0.0480 658 ARG A CA  
1208 C C   . ARG A 140 ? 0.5933 0.5347 0.5749 -0.0220 -0.0889 -0.0221 658 ARG A C   
1209 O O   . ARG A 140 ? 0.6403 0.5708 0.6030 -0.0124 -0.0897 -0.0095 658 ARG A O   
1210 C CB  . ARG A 140 ? 0.6625 0.6725 0.6671 -0.0091 -0.1102 -0.0668 658 ARG A CB  
1211 C CG  . ARG A 140 ? 0.8249 0.8390 0.7948 0.0198  -0.1217 -0.0552 658 ARG A CG  
1212 C CD  . ARG A 140 ? 0.9715 1.0406 0.9422 0.0418  -0.1393 -0.0794 658 ARG A CD  
1213 N NE  . ARG A 140 ? 1.0631 1.1805 1.0832 0.0276  -0.1420 -0.1118 658 ARG A NE  
1214 C CZ  . ARG A 140 ? 1.0985 1.2397 1.1362 0.0327  -0.1448 -0.1173 658 ARG A CZ  
1215 N NH1 . ARG A 140 ? 1.1564 1.2748 1.1650 0.0530  -0.1456 -0.0917 658 ARG A NH1 
1216 N NH2 . ARG A 140 ? 1.0513 1.2382 1.1381 0.0161  -0.1438 -0.1506 658 ARG A NH2 
1217 N N   . PRO A 141 ? 0.5517 0.4743 0.5275 -0.0300 -0.0813 -0.0161 659 PRO A N   
1218 C CA  . PRO A 141 ? 0.5727 0.4703 0.5239 -0.0293 -0.0751 0.0032  659 PRO A CA  
1219 C C   . PRO A 141 ? 0.5653 0.4599 0.5214 -0.0338 -0.0677 0.0138  659 PRO A C   
1220 O O   . PRO A 141 ? 0.5717 0.4546 0.5099 -0.0323 -0.0640 0.0219  659 PRO A O   
1221 C CB  . PRO A 141 ? 0.5672 0.4556 0.5212 -0.0371 -0.0676 0.0043  659 PRO A CB  
1222 C CG  . PRO A 141 ? 0.6061 0.5080 0.5723 -0.0375 -0.0730 -0.0153 659 PRO A CG  
1223 C CD  . PRO A 141 ? 0.5566 0.4826 0.5472 -0.0387 -0.0776 -0.0300 659 PRO A CD  
1224 N N   . PHE A 142 ? 0.5260 0.4320 0.5069 -0.0400 -0.0626 0.0117  660 PHE A N   
1225 C CA  . PHE A 142 ? 0.5247 0.4347 0.5084 -0.0415 -0.0565 0.0203  660 PHE A CA  
1226 C C   . PHE A 142 ? 0.5016 0.4119 0.4753 -0.0346 -0.0626 0.0184  660 PHE A C   
1227 O O   . PHE A 142 ? 0.5169 0.4210 0.4790 -0.0354 -0.0576 0.0231  660 PHE A O   
1228 C CB  . PHE A 142 ? 0.5214 0.4412 0.5310 -0.0469 -0.0471 0.0195  660 PHE A CB  
1229 C CG  . PHE A 142 ? 0.5197 0.4481 0.5289 -0.0456 -0.0393 0.0299  660 PHE A CG  
1230 C CD1 . PHE A 142 ? 0.5233 0.4532 0.5261 -0.0424 -0.0281 0.0434  660 PHE A CD1 
1231 C CD2 . PHE A 142 ? 0.4973 0.4371 0.5111 -0.0441 -0.0433 0.0255  660 PHE A CD2 
1232 C CE1 . PHE A 142 ? 0.4726 0.4208 0.4723 -0.0373 -0.0222 0.0509  660 PHE A CE1 
1233 C CE2 . PHE A 142 ? 0.4592 0.4120 0.4724 -0.0427 -0.0363 0.0320  660 PHE A CE2 
1234 C CZ  . PHE A 142 ? 0.4448 0.4046 0.4504 -0.0391 -0.0264 0.0440  660 PHE A CZ  
1235 N N   . TYR A 143 ? 0.5271 0.4473 0.5064 -0.0268 -0.0717 0.0089  661 TYR A N   
1236 C CA  . TYR A 143 ? 0.5263 0.4436 0.4937 -0.0143 -0.0751 0.0097  661 TYR A CA  
1237 C C   . TYR A 143 ? 0.5640 0.4526 0.4986 -0.0052 -0.0715 0.0182  661 TYR A C   
1238 O O   . TYR A 143 ? 0.5919 0.4628 0.5144 0.0000  -0.0636 0.0228  661 TYR A O   
1239 C CB  . TYR A 143 ? 0.5039 0.4476 0.4834 -0.0022 -0.0867 -0.0034 661 TYR A CB  
1240 C CG  . TYR A 143 ? 0.5422 0.5131 0.5589 -0.0146 -0.0847 -0.0155 661 TYR A CG  
1241 C CD1 . TYR A 143 ? 0.5827 0.5707 0.6229 -0.0247 -0.0846 -0.0307 661 TYR A CD1 
1242 C CD2 . TYR A 143 ? 0.5358 0.5133 0.5653 -0.0174 -0.0791 -0.0136 661 TYR A CD2 
1243 C CE1 . TYR A 143 ? 0.6086 0.6148 0.6851 -0.0388 -0.0753 -0.0428 661 TYR A CE1 
1244 C CE2 . TYR A 143 ? 0.5853 0.5840 0.6477 -0.0291 -0.0725 -0.0232 661 TYR A CE2 
1245 C CZ  . TYR A 143 ? 0.6052 0.6159 0.6916 -0.0404 -0.0688 -0.0374 661 TYR A CZ  
1246 O OH  . TYR A 143 ? 0.6429 0.6685 0.7644 -0.0545 -0.0551 -0.0481 661 TYR A OH  
1247 N N   . LYS A 144 ? 0.5823 0.4627 0.5031 -0.0041 -0.0733 0.0197  662 LYS A N   
1248 C CA  . LYS A 144 ? 0.6427 0.4924 0.5314 0.0042  -0.0652 0.0289  662 LYS A CA  
1249 C C   . LYS A 144 ? 0.6453 0.4777 0.5329 -0.0127 -0.0495 0.0320  662 LYS A C   
1250 O O   . LYS A 144 ? 0.5824 0.3858 0.4522 -0.0109 -0.0345 0.0360  662 LYS A O   
1251 C CB  . LYS A 144 ? 0.6940 0.5454 0.5683 0.0111  -0.0716 0.0280  662 LYS A CB  
1252 C CG  . LYS A 144 ? 0.8046 0.6851 0.6795 0.0299  -0.0877 0.0181  662 LYS A CG  
1253 C CD  . LYS A 144 ? 0.8878 0.7769 0.7489 0.0365  -0.0942 0.0128  662 LYS A CD  
1254 C CE  . LYS A 144 ? 0.9640 0.8321 0.7799 0.0633  -0.0898 0.0269  662 LYS A CE  
1255 N NZ  . LYS A 144 ? 1.0123 0.8344 0.8084 0.0530  -0.0694 0.0426  662 LYS A NZ  
1256 N N   . MET A 145 ? 0.5941 0.4459 0.5011 -0.0277 -0.0500 0.0286  663 MET A N   
1257 C CA  . MET A 145 ? 0.6438 0.4975 0.5536 -0.0412 -0.0379 0.0259  663 MET A CA  
1258 C C   . MET A 145 ? 0.6365 0.4921 0.5535 -0.0444 -0.0305 0.0204  663 MET A C   
1259 O O   . MET A 145 ? 0.6518 0.4995 0.5664 -0.0543 -0.0158 0.0125  663 MET A O   
1260 C CB  . MET A 145 ? 0.6486 0.5295 0.5733 -0.0475 -0.0407 0.0260  663 MET A CB  
1261 C CG  . MET A 145 ? 0.7126 0.5885 0.6303 -0.0467 -0.0427 0.0290  663 MET A CG  
1262 S SD  . MET A 145 ? 0.7207 0.6220 0.6515 -0.0470 -0.0409 0.0333  663 MET A SD  
1263 C CE  . MET A 145 ? 0.8483 0.7752 0.7770 -0.0532 -0.0324 0.0255  663 MET A CE  
1264 N N   . MET A 146 ? 0.6408 0.5088 0.5698 -0.0381 -0.0384 0.0208  664 MET A N   
1265 C CA  . MET A 146 ? 0.6374 0.5060 0.5725 -0.0390 -0.0315 0.0150  664 MET A CA  
1266 C C   . MET A 146 ? 0.6393 0.4682 0.5552 -0.0324 -0.0180 0.0156  664 MET A C   
1267 O O   . MET A 146 ? 0.6410 0.4596 0.5598 -0.0409 -0.0019 0.0063  664 MET A O   
1268 C CB  . MET A 146 ? 0.6527 0.5399 0.6029 -0.0311 -0.0419 0.0157  664 MET A CB  
1269 C CG  . MET A 146 ? 0.6215 0.5409 0.5910 -0.0384 -0.0440 0.0157  664 MET A CG  
1270 S SD  . MET A 146 ? 0.6203 0.5588 0.6100 -0.0333 -0.0479 0.0131  664 MET A SD  
1271 C CE  . MET A 146 ? 0.6967 0.6378 0.6961 -0.0288 -0.0579 0.0123  664 MET A CE  
1272 N N   . LEU A 147 ? 0.6268 0.4333 0.5221 -0.0156 -0.0215 0.0259  665 LEU A N   
1273 C CA  . LEU A 147 ? 0.6843 0.4465 0.5534 -0.0005 -0.0051 0.0335  665 LEU A CA  
1274 C C   . LEU A 147 ? 0.7299 0.4584 0.5803 -0.0086 0.0145  0.0363  665 LEU A C   
1275 O O   . LEU A 147 ? 0.7279 0.4105 0.5511 0.0061  0.0341  0.0468  665 LEU A O   
1276 C CB  . LEU A 147 ? 0.7052 0.4690 0.5568 0.0298  -0.0190 0.0441  665 LEU A CB  
1277 C CG  . LEU A 147 ? 0.7319 0.5318 0.6036 0.0396  -0.0363 0.0383  665 LEU A CG  
1278 C CD1 . LEU A 147 ? 0.7704 0.5957 0.6335 0.0639  -0.0554 0.0395  665 LEU A CD1 
1279 C CD2 . LEU A 147 ? 0.7082 0.4869 0.5765 0.0501  -0.0225 0.0396  665 LEU A CD2 
1280 N N   . HIS A 148 ? 0.6930 0.4425 0.5561 -0.0290 0.0124  0.0281  666 HIS A N   
1281 C CA  . HIS A 148 ? 0.7569 0.4829 0.6068 -0.0388 0.0301  0.0278  666 HIS A CA  
1282 C C   . HIS A 148 ? 0.8080 0.5063 0.6246 -0.0162 0.0290  0.0455  666 HIS A C   
1283 O O   . HIS A 148 ? 0.8906 0.5471 0.6838 -0.0139 0.0533  0.0523  666 HIS A O   
1284 C CB  . HIS A 148 ? 0.9059 0.5999 0.7581 -0.0545 0.0633  0.0161  666 HIS A CB  
1285 C CG  . HIS A 148 ? 1.0764 0.7862 0.9437 -0.0813 0.0768  -0.0022 666 HIS A CG  
1286 N ND1 . HIS A 148 ? 1.1574 0.8434 1.0085 -0.0846 0.0911  0.0022  666 HIS A ND1 
1287 C CD2 . HIS A 148 ? 1.1004 0.8553 0.9979 -0.1040 0.0778  -0.0271 666 HIS A CD2 
1288 C CE1 . HIS A 148 ? 1.1535 0.8696 1.0276 -0.1101 0.1005  -0.0207 666 HIS A CE1 
1289 N NE2 . HIS A 148 ? 1.1126 0.8741 1.0146 -0.1209 0.0917  -0.0395 666 HIS A NE2 
1290 N N   . LYS A 149 ? 0.7346 0.4589 0.5495 0.0009  0.0031  0.0511  667 LYS A N   
1291 C CA  . LYS A 149 ? 0.8075 0.5226 0.5926 0.0236  -0.0024 0.0628  667 LYS A CA  
1292 C C   . LYS A 149 ? 0.7908 0.5261 0.5822 0.0110  -0.0117 0.0575  667 LYS A C   
1293 O O   . LYS A 149 ? 0.7468 0.5138 0.5673 -0.0057 -0.0236 0.0472  667 LYS A O   
1294 C CB  . LYS A 149 ? 0.8487 0.5912 0.6317 0.0493  -0.0249 0.0640  667 LYS A CB  
1295 C CG  . LYS A 149 ? 0.9278 0.6466 0.6897 0.0763  -0.0151 0.0751  667 LYS A CG  
1296 C CD  . LYS A 149 ? 1.0198 0.7621 0.7575 0.1147  -0.0321 0.0809  667 LYS A CD  
1297 C CE  . LYS A 149 ? 1.1205 0.8674 0.8529 0.1425  -0.0340 0.0852  667 LYS A CE  
1298 N NZ  . LYS A 149 ? 1.2141 0.8964 0.9118 0.1613  -0.0013 0.1064  667 LYS A NZ  
1299 N N   . PRO A 150 ? 0.8838 0.5994 0.6462 0.0211  -0.0039 0.0658  668 PRO A N   
1300 C CA  . PRO A 150 ? 0.8489 0.5824 0.6175 0.0094  -0.0109 0.0598  668 PRO A CA  
1301 C C   . PRO A 150 ? 0.7978 0.5711 0.5807 0.0160  -0.0376 0.0512  668 PRO A C   
1302 O O   . PRO A 150 ? 0.7553 0.5427 0.5291 0.0372  -0.0504 0.0509  668 PRO A O   
1303 C CB  . PRO A 150 ? 0.9484 0.6479 0.6777 0.0227  0.0069  0.0721  668 PRO A CB  
1304 C CG  . PRO A 150 ? 1.0057 0.6819 0.7034 0.0539  0.0125  0.0872  668 PRO A CG  
1305 C CD  . PRO A 150 ? 0.9764 0.6494 0.6962 0.0463  0.0153  0.0833  668 PRO A CD  
1306 N N   . ILE A 151 ? 0.7305 0.5238 0.5373 -0.0016 -0.0434 0.0421  669 ILE A N   
1307 C CA  . ILE A 151 ? 0.6790 0.5018 0.5030 -0.0002 -0.0607 0.0308  669 ILE A CA  
1308 C C   . ILE A 151 ? 0.6867 0.5107 0.4873 0.0118  -0.0640 0.0287  669 ILE A C   
1309 O O   . ILE A 151 ? 0.7611 0.5691 0.5476 0.0068  -0.0532 0.0336  669 ILE A O   
1310 C CB  . ILE A 151 ? 0.6289 0.4640 0.4831 -0.0189 -0.0596 0.0257  669 ILE A CB  
1311 C CG1 . ILE A 151 ? 0.6578 0.4941 0.5270 -0.0283 -0.0532 0.0296  669 ILE A CG1 
1312 C CG2 . ILE A 151 ? 0.6142 0.4707 0.4923 -0.0202 -0.0697 0.0128  669 ILE A CG2 
1313 C CD1 . ILE A 151 ? 0.6991 0.5443 0.5800 -0.0233 -0.0603 0.0275  669 ILE A CD1 
1314 N N   . THR A 152 ? 0.7101 0.5595 0.5076 0.0280  -0.0789 0.0185  670 THR A N   
1315 C CA  . THR A 152 ? 0.8091 0.6700 0.5812 0.0445  -0.0843 0.0134  670 THR A CA  
1316 C C   . THR A 152 ? 0.8410 0.7365 0.6427 0.0344  -0.0961 -0.0123 670 THR A C   
1317 O O   . THR A 152 ? 0.7679 0.6743 0.6082 0.0170  -0.0978 -0.0242 670 THR A O   
1318 C CB  . THR A 152 ? 0.8101 0.6829 0.5496 0.0781  -0.0911 0.0186  670 THR A CB  
1319 O OG1 . THR A 152 ? 0.7744 0.6931 0.5407 0.0829  -0.1096 -0.0021 670 THR A OG1 
1320 C CG2 . THR A 152 ? 0.8495 0.6794 0.5643 0.0876  -0.0736 0.0436  670 THR A CG2 
1321 N N   . LEU A 153 ? 0.8790 0.7894 0.6610 0.0461  -0.1007 -0.0214 671 LEU A N   
1322 C CA  . LEU A 153 ? 0.8647 0.8076 0.6751 0.0358  -0.1085 -0.0512 671 LEU A CA  
1323 C C   . LEU A 153 ? 0.7945 0.7844 0.6332 0.0386  -0.1228 -0.0783 671 LEU A C   
1324 O O   . LEU A 153 ? 0.7742 0.7818 0.6547 0.0185  -0.1217 -0.1050 671 LEU A O   
1325 C CB  . LEU A 153 ? 0.9026 0.8570 0.6829 0.0499  -0.1107 -0.0575 671 LEU A CB  
1326 C CG  . LEU A 153 ? 0.8940 0.8946 0.6968 0.0466  -0.1209 -0.0960 671 LEU A CG  
1327 C CD1 . LEU A 153 ? 0.8946 0.8786 0.7426 0.0154  -0.1093 -0.1095 671 LEU A CD1 
1328 C CD2 . LEU A 153 ? 0.9109 0.9245 0.6746 0.0660  -0.1233 -0.0984 671 LEU A CD2 
1329 N N   . HIS A 154 ? 0.8028 0.8126 0.6209 0.0636  -0.1330 -0.0728 672 HIS A N   
1330 C CA  . HIS A 154 ? 0.8347 0.8986 0.6824 0.0674  -0.1472 -0.1013 672 HIS A CA  
1331 C C   . HIS A 154 ? 0.8129 0.8646 0.7089 0.0379  -0.1390 -0.1066 672 HIS A C   
1332 O O   . HIS A 154 ? 0.8189 0.9092 0.7578 0.0240  -0.1422 -0.1399 672 HIS A O   
1333 C CB  . HIS A 154 ? 0.9064 0.9898 0.7187 0.1053  -0.1577 -0.0882 672 HIS A CB  
1334 C CG  . HIS A 154 ? 0.9706 1.1126 0.8151 0.1105  -0.1721 -0.1156 672 HIS A CG  
1335 N ND1 . HIS A 154 ? 0.9661 1.0964 0.8452 0.0914  -0.1670 -0.1140 672 HIS A ND1 
1336 C CD2 . HIS A 154 ? 0.9915 1.2115 0.8402 0.1335  -0.1913 -0.1481 672 HIS A CD2 
1337 C CE1 . HIS A 154 ? 0.9617 1.1563 0.8669 0.1002  -0.1810 -0.1439 672 HIS A CE1 
1338 N NE2 . HIS A 154 ? 0.9716 1.2251 0.8604 0.1258  -0.1968 -0.1667 672 HIS A NE2 
1339 N N   . ASP A 155 ? 0.8275 0.8287 0.7179 0.0280  -0.1261 -0.0762 673 ASP A N   
1340 C CA  . ASP A 155 ? 0.8163 0.8055 0.7455 0.0045  -0.1165 -0.0768 673 ASP A CA  
1341 C C   . ASP A 155 ? 0.7357 0.7215 0.7007 -0.0200 -0.1048 -0.0952 673 ASP A C   
1342 O O   . ASP A 155 ? 0.7168 0.7049 0.7197 -0.0372 -0.0952 -0.1059 673 ASP A O   
1343 C CB  . ASP A 155 ? 0.8353 0.7797 0.7485 0.0010  -0.1053 -0.0440 673 ASP A CB  
1344 C CG  . ASP A 155 ? 0.8832 0.8187 0.7621 0.0231  -0.1091 -0.0260 673 ASP A CG  
1345 O OD1 . ASP A 155 ? 0.9219 0.8250 0.7689 0.0287  -0.1003 -0.0063 673 ASP A OD1 
1346 O OD2 . ASP A 155 ? 0.9098 0.8692 0.7947 0.0351  -0.1176 -0.0324 673 ASP A OD2 
1347 N N   . MET A 156 ? 0.7027 0.6791 0.6556 -0.0210 -0.1017 -0.0982 674 MET A N   
1348 C CA  . MET A 156 ? 0.7255 0.6930 0.7107 -0.0416 -0.0868 -0.1160 674 MET A CA  
1349 C C   . MET A 156 ? 0.7747 0.7861 0.7997 -0.0521 -0.0885 -0.1602 674 MET A C   
1350 O O   . MET A 156 ? 0.8022 0.8011 0.8670 -0.0743 -0.0684 -0.1766 674 MET A O   
1351 C CB  . MET A 156 ? 0.7787 0.7297 0.7408 -0.0380 -0.0837 -0.1111 674 MET A CB  
1352 C CG  . MET A 156 ? 0.8383 0.7758 0.8306 -0.0556 -0.0658 -0.1296 674 MET A CG  
1353 S SD  . MET A 156 ? 0.9033 0.7897 0.9098 -0.0660 -0.0402 -0.1003 674 MET A SD  
1354 C CE  . MET A 156 ? 0.9022 0.7705 0.8635 -0.0508 -0.0465 -0.0642 674 MET A CE  
1355 N N   . GLU A 157 ? 0.7739 0.8387 0.7894 -0.0352 -0.1095 -0.1812 675 GLU A N   
1356 C CA  . GLU A 157 ? 0.7664 0.8900 0.8238 -0.0453 -0.1131 -0.2322 675 GLU A CA  
1357 C C   . GLU A 157 ? 0.7830 0.9101 0.8865 -0.0653 -0.1009 -0.2437 675 GLU A C   
1358 O O   . GLU A 157 ? 0.7662 0.9011 0.9196 -0.0922 -0.0821 -0.2785 675 GLU A O   
1359 C CB  . GLU A 157 ? 0.7720 0.9632 0.8039 -0.0145 -0.1408 -0.2495 675 GLU A CB  
1360 C CG  . GLU A 157 ? 0.8233 1.0954 0.9011 -0.0227 -0.1482 -0.3102 675 GLU A CG  
1361 C CD  . GLU A 157 ? 0.8709 1.2181 0.9174 0.0162  -0.1752 -0.3246 675 GLU A CD  
1362 O OE1 . GLU A 157 ? 0.8835 1.2318 0.8861 0.0495  -0.1908 -0.2937 675 GLU A OE1 
1363 O OE2 . GLU A 157 ? 0.8901 1.2861 0.9555 0.0168  -0.1725 -0.3566 675 GLU A OE2 
1364 N N   . SER A 158 ? 0.8205 0.9389 0.9093 -0.0537 -0.1075 -0.2157 676 SER A N   
1365 C CA  . SER A 158 ? 0.8640 0.9879 0.9930 -0.0702 -0.0962 -0.2244 676 SER A CA  
1366 C C   . SER A 158 ? 0.9040 0.9703 1.0585 -0.0967 -0.0637 -0.2117 676 SER A C   
1367 O O   . SER A 158 ? 0.9442 1.0121 1.1373 -0.1143 -0.0468 -0.2234 676 SER A O   
1368 C CB  . SER A 158 ? 0.8980 1.0199 1.0004 -0.0497 -0.1093 -0.1940 676 SER A CB  
1369 O OG  . SER A 158 ? 0.9483 1.0120 1.0122 -0.0428 -0.1044 -0.1486 676 SER A OG  
1370 N N   . VAL A 159 ? 0.9051 0.9224 1.0380 -0.0970 -0.0527 -0.1875 677 VAL A N   
1371 C CA  . VAL A 159 ? 0.8922 0.8540 1.0394 -0.1121 -0.0211 -0.1686 677 VAL A CA  
1372 C C   . VAL A 159 ? 0.8778 0.8230 1.0489 -0.1282 0.0009  -0.1931 677 VAL A C   
1373 O O   . VAL A 159 ? 0.9426 0.8671 1.1538 -0.1492 0.0326  -0.2087 677 VAL A O   
1374 C CB  . VAL A 159 ? 0.8608 0.7825 0.9654 -0.0962 -0.0229 -0.1199 677 VAL A CB  
1375 C CG1 . VAL A 159 ? 0.8739 0.7464 0.9871 -0.1030 0.0087  -0.0995 677 VAL A CG1 
1376 C CG2 . VAL A 159 ? 0.8363 0.7693 0.9247 -0.0850 -0.0375 -0.1000 677 VAL A CG2 
1377 N N   . ASP A 160 ? 0.8465 0.7967 0.9936 -0.1189 -0.0116 -0.1969 678 ASP A N   
1378 C CA  . ASP A 160 ? 0.8634 0.7974 1.0300 -0.1323 0.0085  -0.2210 678 ASP A CA  
1379 C C   . ASP A 160 ? 0.8351 0.8249 0.9956 -0.1266 -0.0159 -0.2575 678 ASP A C   
1380 O O   . ASP A 160 ? 0.8305 0.8264 0.9461 -0.1052 -0.0377 -0.2382 678 ASP A O   
1381 C CB  . ASP A 160 ? 0.9087 0.7857 1.0474 -0.1227 0.0230  -0.1823 678 ASP A CB  
1382 C CG  . ASP A 160 ? 0.9635 0.8116 1.1258 -0.1361 0.0519  -0.2035 678 ASP A CG  
1383 O OD1 . ASP A 160 ? 0.9985 0.8692 1.2023 -0.1569 0.0629  -0.2516 678 ASP A OD1 
1384 O OD2 . ASP A 160 ? 0.9866 0.7922 1.1280 -0.1254 0.0649  -0.1749 678 ASP A OD2 
1385 N N   . SER A 161 ? 0.8643 0.8972 1.0703 -0.1456 -0.0098 -0.3124 679 SER A N   
1386 C CA  . SER A 161 ? 0.9410 1.0442 1.1422 -0.1366 -0.0354 -0.3530 679 SER A CA  
1387 C C   . SER A 161 ? 0.9802 1.0655 1.1681 -0.1362 -0.0286 -0.3596 679 SER A C   
1388 O O   . SER A 161 ? 1.0057 1.1288 1.1585 -0.1154 -0.0543 -0.3649 679 SER A O   
1389 C CB  . SER A 161 ? 1.0138 1.1782 1.2627 -0.1467 -0.0266 -0.3927 679 SER A CB  
1390 O OG  . SER A 161 ? 1.0398 1.2455 1.2902 -0.1367 -0.0450 -0.3921 679 SER A OG  
1391 N N   . GLU A 162 ? 1.0060 1.0331 1.2175 -0.1544 0.0080  -0.3547 680 GLU A N   
1392 C CA  . GLU A 162 ? 1.0019 1.0142 1.2065 -0.1545 0.0176  -0.3645 680 GLU A CA  
1393 C C   . GLU A 162 ? 0.9726 0.9540 1.1210 -0.1321 0.0016  -0.3236 680 GLU A C   
1394 O O   . GLU A 162 ? 1.0079 1.0114 1.1327 -0.1213 -0.0117 -0.3348 680 GLU A O   
1395 C CB  . GLU A 162 ? 1.0237 0.9806 1.2648 -0.1735 0.0643  -0.3631 680 GLU A CB  
1396 C CG  . GLU A 162 ? 1.0817 1.0610 1.3747 -0.1922 0.0884  -0.3876 680 GLU A CG  
1397 C CD  . GLU A 162 ? 1.2163 1.1447 1.5422 -0.2080 0.1384  -0.3894 680 GLU A CD  
1398 O OE1 . GLU A 162 ? 1.2596 1.1358 1.5670 -0.2018 0.1525  -0.3695 680 GLU A OE1 
1399 O OE2 . GLU A 162 ? 1.2700 1.2112 1.6399 -0.2251 0.1657  -0.4112 680 GLU A OE2 
1400 N N   . TYR A 163 ? 0.9105 0.8464 1.0347 -0.1216 0.0044  -0.2705 681 TYR A N   
1401 C CA  . TYR A 163 ? 0.9430 0.8597 1.0154 -0.0992 -0.0094 -0.2283 681 TYR A CA  
1402 C C   . TYR A 163 ? 0.9024 0.8647 0.9362 -0.0788 -0.0435 -0.2226 681 TYR A C   
1403 O O   . TYR A 163 ? 0.9182 0.8806 0.9129 -0.0629 -0.0542 -0.2075 681 TYR A O   
1404 C CB  . TYR A 163 ? 0.9530 0.8198 1.0142 -0.0939 0.0036  -0.1802 681 TYR A CB  
1405 C CG  . TYR A 163 ? 0.9475 0.7889 0.9727 -0.0785 0.0033  -0.1477 681 TYR A CG  
1406 C CD1 . TYR A 163 ? 0.9990 0.8456 1.0126 -0.0752 0.0021  -0.1621 681 TYR A CD1 
1407 C CD2 . TYR A 163 ? 0.9209 0.7405 0.9261 -0.0677 0.0044  -0.1069 681 TYR A CD2 
1408 C CE1 . TYR A 163 ? 1.0293 0.8577 1.0136 -0.0622 0.0029  -0.1355 681 TYR A CE1 
1409 C CE2 . TYR A 163 ? 0.9597 0.7671 0.9376 -0.0551 0.0045  -0.0836 681 TYR A CE2 
1410 C CZ  . TYR A 163 ? 1.0244 0.8352 0.9925 -0.0527 0.0042  -0.0974 681 TYR A CZ  
1411 O OH  . TYR A 163 ? 1.0550 0.8583 0.9992 -0.0412 0.0054  -0.0770 681 TYR A OH  
1412 N N   . TYR A 164 ? 0.8056 0.8047 0.8485 -0.0769 -0.0577 -0.2332 682 TYR A N   
1413 C CA  . TYR A 164 ? 0.7161 0.7583 0.7206 -0.0519 -0.0864 -0.2287 682 TYR A CA  
1414 C C   . TYR A 164 ? 0.7099 0.8006 0.7027 -0.0417 -0.0989 -0.2627 682 TYR A C   
1415 O O   . TYR A 164 ? 0.7004 0.8002 0.6441 -0.0165 -0.1132 -0.2445 682 TYR A O   
1416 C CB  . TYR A 164 ? 0.6717 0.7510 0.6933 -0.0496 -0.0980 -0.2395 682 TYR A CB  
1417 C CG  . TYR A 164 ? 0.7091 0.8430 0.6946 -0.0185 -0.1255 -0.2432 682 TYR A CG  
1418 C CD1 . TYR A 164 ? 0.7143 0.8247 0.6492 0.0065  -0.1339 -0.1994 682 TYR A CD1 
1419 C CD2 . TYR A 164 ? 0.8093 1.0202 0.8111 -0.0121 -0.1402 -0.2919 682 TYR A CD2 
1420 C CE1 . TYR A 164 ? 0.7835 0.9352 0.6796 0.0408  -0.1534 -0.1972 682 TYR A CE1 
1421 C CE2 . TYR A 164 ? 0.8508 1.1160 0.8133 0.0250  -0.1649 -0.2918 682 TYR A CE2 
1422 C CZ  . TYR A 164 ? 0.8683 1.0985 0.7754 0.0532  -0.1700 -0.2410 682 TYR A CZ  
1423 O OH  . TYR A 164 ? 0.9167 1.1925 0.7792 0.0956  -0.1890 -0.2357 682 TYR A OH  
1424 N N   . ASN A 165 ? 0.7386 0.8611 0.7765 -0.0613 -0.0907 -0.3141 683 ASN A N   
1425 C CA  . ASN A 165 ? 0.7942 0.9702 0.8251 -0.0532 -0.1016 -0.3534 683 ASN A CA  
1426 C C   . ASN A 165 ? 0.8080 0.9436 0.8049 -0.0465 -0.0944 -0.3307 683 ASN A C   
1427 O O   . ASN A 165 ? 0.7846 0.9529 0.7412 -0.0233 -0.1104 -0.3325 683 ASN A O   
1428 C CB  . ASN A 165 ? 0.8183 1.0251 0.9129 -0.0795 -0.0831 -0.4036 683 ASN A CB  
1429 C CG  . ASN A 165 ? 0.8594 1.1228 0.9879 -0.0802 -0.0884 -0.4230 683 ASN A CG  
1430 O OD1 . ASN A 165 ? 0.8769 1.1749 0.9765 -0.0551 -0.1131 -0.4093 683 ASN A OD1 
1431 N ND2 . ASN A 165 ? 0.8612 1.1336 1.0509 -0.1072 -0.0621 -0.4547 683 ASN A ND2 
1432 N N   . SER A 166 ? 0.8435 0.9108 0.8547 -0.0637 -0.0692 -0.3086 684 SER A N   
1433 C CA  . SER A 166 ? 0.8827 0.9148 0.8661 -0.0575 -0.0612 -0.2886 684 SER A CA  
1434 C C   . SER A 166 ? 0.7951 0.8180 0.7199 -0.0318 -0.0764 -0.2432 684 SER A C   
1435 O O   . SER A 166 ? 0.8033 0.8369 0.6930 -0.0169 -0.0822 -0.2408 684 SER A O   
1436 C CB  . SER A 166 ? 0.9383 0.9039 0.9471 -0.0745 -0.0311 -0.2706 684 SER A CB  
1437 O OG  . SER A 166 ? 0.9982 0.9604 1.0590 -0.0983 -0.0080 -0.3129 684 SER A OG  
1438 N N   . LEU A 167 ? 0.7127 0.7142 0.6274 -0.0274 -0.0795 -0.2085 685 LEU A N   
1439 C CA  . LEU A 167 ? 0.7061 0.6924 0.5706 -0.0073 -0.0869 -0.1685 685 LEU A CA  
1440 C C   . LEU A 167 ? 0.6942 0.7259 0.5204 0.0194  -0.1063 -0.1749 685 LEU A C   
1441 O O   . LEU A 167 ? 0.6848 0.7057 0.4644 0.0380  -0.1063 -0.1513 685 LEU A O   
1442 C CB  . LEU A 167 ? 0.6921 0.6474 0.5599 -0.0111 -0.0833 -0.1362 685 LEU A CB  
1443 C CG  . LEU A 167 ? 0.7144 0.6277 0.6079 -0.0281 -0.0640 -0.1212 685 LEU A CG  
1444 C CD1 . LEU A 167 ? 0.6846 0.5804 0.5813 -0.0299 -0.0630 -0.0950 685 LEU A CD1 
1445 C CD2 . LEU A 167 ? 0.7213 0.6116 0.5944 -0.0250 -0.0544 -0.1052 685 LEU A CD2 
1446 N N   . ARG A 168 ? 0.7028 0.7876 0.5468 0.0240  -0.1205 -0.2067 686 ARG A N   
1447 C CA  . ARG A 168 ? 0.7831 0.9219 0.5873 0.0575  -0.1398 -0.2141 686 ARG A CA  
1448 C C   . ARG A 168 ? 0.7850 0.9541 0.5694 0.0676  -0.1424 -0.2368 686 ARG A C   
1449 O O   . ARG A 168 ? 0.7846 0.9705 0.5142 0.1004  -0.1497 -0.2211 686 ARG A O   
1450 C CB  . ARG A 168 ? 0.8314 1.0343 0.6645 0.0614  -0.1559 -0.2489 686 ARG A CB  
1451 C CG  . ARG A 168 ? 0.9396 1.1905 0.7235 0.1058  -0.1756 -0.2398 686 ARG A CG  
1452 C CD  . ARG A 168 ? 1.0197 1.3538 0.8421 0.1119  -0.1873 -0.2807 686 ARG A CD  
1453 N NE  . ARG A 168 ? 1.0437 1.3858 0.9374 0.0718  -0.1798 -0.3176 686 ARG A NE  
1454 C CZ  . ARG A 168 ? 1.0506 1.4339 0.9967 0.0510  -0.1716 -0.3628 686 ARG A CZ  
1455 N NH1 . ARG A 168 ? 1.0472 1.4757 0.9835 0.0669  -0.1749 -0.3802 686 ARG A NH1 
1456 N NH2 . ARG A 168 ? 1.0319 1.4094 1.0408 0.0148  -0.1567 -0.3895 686 ARG A NH2 
1457 N N   . TRP A 169 ? 0.7914 0.9655 0.6183 0.0412  -0.1333 -0.2733 687 TRP A N   
1458 C CA  . TRP A 169 ? 0.7886 0.9846 0.5995 0.0472  -0.1326 -0.2950 687 TRP A CA  
1459 C C   . TRP A 169 ? 0.8136 0.9576 0.5755 0.0591  -0.1222 -0.2490 687 TRP A C   
1460 O O   . TRP A 169 ? 0.8712 1.0383 0.5854 0.0855  -0.1279 -0.2444 687 TRP A O   
1461 C CB  . TRP A 169 ? 0.7417 0.9329 0.6111 0.0128  -0.1167 -0.3377 687 TRP A CB  
1462 C CG  . TRP A 169 ? 0.7305 0.9546 0.5951 0.0160  -0.1155 -0.3702 687 TRP A CG  
1463 C CD1 . TRP A 169 ? 0.7747 1.0624 0.6737 0.0143  -0.1174 -0.4083 687 TRP A CD1 
1464 C CD2 . TRP A 169 ? 0.7886 0.9793 0.6222 0.0207  -0.1057 -0.3540 687 TRP A CD2 
1465 N NE1 . TRP A 169 ? 0.8058 1.1030 0.6937 0.0180  -0.1121 -0.4210 687 TRP A NE1 
1466 C CE2 . TRP A 169 ? 0.8255 1.0638 0.6712 0.0219  -0.1055 -0.3904 687 TRP A CE2 
1467 C CE3 . TRP A 169 ? 0.7653 0.8903 0.5713 0.0229  -0.0929 -0.3031 687 TRP A CE3 
1468 C CZ2 . TRP A 169 ? 0.8592 1.0841 0.6801 0.0269  -0.0974 -0.3892 687 TRP A CZ2 
1469 C CZ3 . TRP A 169 ? 0.7957 0.9095 0.5801 0.0272  -0.0840 -0.3013 687 TRP A CZ3 
1470 C CH2 . TRP A 169 ? 0.8565 1.0202 0.6442 0.0300  -0.0876 -0.3480 687 TRP A CH2 
1471 N N   . ILE A 170 ? 0.7729 0.8508 0.5464 0.0408  -0.1056 -0.2162 688 ILE A N   
1472 C CA  . ILE A 170 ? 0.8382 0.8719 0.5745 0.0472  -0.0933 -0.1779 688 ILE A CA  
1473 C C   . ILE A 170 ? 0.8461 0.8810 0.5247 0.0773  -0.0982 -0.1465 688 ILE A C   
1474 O O   . ILE A 170 ? 0.9100 0.9373 0.5456 0.0932  -0.0910 -0.1311 688 ILE A O   
1475 C CB  . ILE A 170 ? 0.8200 0.7982 0.5818 0.0255  -0.0775 -0.1520 688 ILE A CB  
1476 C CG1 . ILE A 170 ? 0.8336 0.8004 0.6430 0.0030  -0.0655 -0.1763 688 ILE A CG1 
1477 C CG2 . ILE A 170 ? 0.8073 0.7505 0.5347 0.0308  -0.0651 -0.1167 688 ILE A CG2 
1478 C CD1 . ILE A 170 ? 0.7971 0.7185 0.6291 -0.0108 -0.0507 -0.1506 688 ILE A CD1 
1479 N N   . LEU A 171 ? 0.7990 0.8399 0.4749 0.0869  -0.1070 -0.1354 689 LEU A N   
1480 C CA  . LEU A 171 ? 0.8512 0.8833 0.4715 0.1184  -0.1061 -0.1022 689 LEU A CA  
1481 C C   . LEU A 171 ? 1.0251 1.1089 0.5997 0.1553  -0.1168 -0.1141 689 LEU A C   
1482 O O   . LEU A 171 ? 1.1332 1.1969 0.6502 0.1831  -0.1057 -0.0825 689 LEU A O   
1483 C CB  . LEU A 171 ? 0.8238 0.8552 0.4546 0.1226  -0.1134 -0.0919 689 LEU A CB  
1484 C CG  . LEU A 171 ? 0.9193 0.9269 0.4969 0.1541  -0.1063 -0.0534 689 LEU A CG  
1485 C CD1 . LEU A 171 ? 0.9525 0.8887 0.5209 0.1377  -0.0803 -0.0180 689 LEU A CD1 
1486 C CD2 . LEU A 171 ? 0.9288 0.9595 0.5189 0.1654  -0.1201 -0.0561 689 LEU A CD2 
1487 N N   . GLU A 172 ? 1.0092 1.1611 0.6083 0.1567  -0.1355 -0.1609 690 GLU A N   
1488 C CA  . GLU A 172 ? 1.0570 1.2704 0.6309 0.1908  -0.1450 -0.1721 690 GLU A CA  
1489 C C   . GLU A 172 ? 1.0543 1.2797 0.6168 0.1909  -0.1385 -0.1852 690 GLU A C   
1490 O O   . GLU A 172 ? 1.1064 1.3697 0.6443 0.2213  -0.1400 -0.1815 690 GLU A O   
1491 C CB  . GLU A 172 ? 1.0599 1.3468 0.6866 0.1881  -0.1626 -0.2141 690 GLU A CB  
1492 C CG  . GLU A 172 ? 1.0827 1.3698 0.7190 0.1946  -0.1698 -0.2019 690 GLU A CG  
1493 C CD  . GLU A 172 ? 1.1038 1.4640 0.7998 0.1864  -0.1832 -0.2478 690 GLU A CD  
1494 O OE1 . GLU A 172 ? 1.1029 1.4728 0.8111 0.1924  -0.1894 -0.2425 690 GLU A OE1 
1495 O OE2 . GLU A 172 ? 1.1274 1.5353 0.8600 0.1732  -0.1849 -0.2900 690 GLU A OE2 
1496 N N   . ASN A 173 ? 1.0081 1.2034 0.5878 0.1607  -0.1305 -0.2007 691 ASN A N   
1497 C CA  . ASN A 173 ? 1.0167 1.2233 0.5909 0.1583  -0.1235 -0.2169 691 ASN A CA  
1498 C C   . ASN A 173 ? 1.0245 1.1609 0.5836 0.1428  -0.1018 -0.1874 691 ASN A C   
1499 O O   . ASN A 173 ? 1.0751 1.1573 0.6552 0.1224  -0.0910 -0.1610 691 ASN A O   
1500 C CB  . ASN A 173 ? 1.0683 1.3163 0.7069 0.1309  -0.1290 -0.2733 691 ASN A CB  
1501 C CG  . ASN A 173 ? 1.1645 1.4768 0.8432 0.1343  -0.1443 -0.3019 691 ASN A CG  
1502 O OD1 . ASN A 173 ? 1.2455 1.6021 0.9002 0.1680  -0.1543 -0.2914 691 ASN A OD1 
1503 N ND2 . ASN A 173 ? 1.1545 1.4715 0.8968 0.1007  -0.1425 -0.3379 691 ASN A ND2 
1504 N N   . ASP A 174 ? 0.9633 1.1046 0.4950 0.1509  -0.0934 -0.1907 692 ASP A N   
1505 C CA  . ASP A 174 ? 0.9782 1.0619 0.5114 0.1320  -0.0706 -0.1673 692 ASP A CA  
1506 C C   . ASP A 174 ? 0.9789 1.0477 0.5776 0.0959  -0.0670 -0.1930 692 ASP A C   
1507 O O   . ASP A 174 ? 1.0221 1.1259 0.6463 0.0888  -0.0723 -0.2360 692 ASP A O   
1508 C CB  . ASP A 174 ? 1.0512 1.1484 0.5380 0.1515  -0.0615 -0.1664 692 ASP A CB  
1509 C CG  . ASP A 174 ? 1.1249 1.1648 0.6026 0.1379  -0.0353 -0.1350 692 ASP A CG  
1510 O OD1 . ASP A 174 ? 1.1071 1.1087 0.6262 0.1098  -0.0272 -0.1265 692 ASP A OD1 
1511 O OD2 . ASP A 174 ? 1.1946 1.2324 0.6233 0.1570  -0.0216 -0.1198 692 ASP A OD2 
1512 N N   . PRO A 175 ? 0.9358 0.9547 0.5620 0.0746  -0.0559 -0.1694 693 PRO A N   
1513 C CA  . PRO A 175 ? 0.9277 0.9284 0.6103 0.0475  -0.0489 -0.1876 693 PRO A CA  
1514 C C   . PRO A 175 ? 0.9225 0.8985 0.6090 0.0396  -0.0314 -0.1829 693 PRO A C   
1515 O O   . PRO A 175 ? 0.9609 0.9147 0.6884 0.0231  -0.0217 -0.1896 693 PRO A O   
1516 C CB  . PRO A 175 ? 0.9190 0.8868 0.6220 0.0362  -0.0473 -0.1611 693 PRO A CB  
1517 C CG  . PRO A 175 ? 0.9332 0.8912 0.5898 0.0532  -0.0480 -0.1260 693 PRO A CG  
1518 C CD  . PRO A 175 ? 0.9682 0.9465 0.5746 0.0763  -0.0468 -0.1258 693 PRO A CD  
1519 N N   . THR A 176 ? 0.9300 0.9095 0.5742 0.0533  -0.0248 -0.1709 694 THR A N   
1520 C CA  . THR A 176 ? 0.9961 0.9538 0.6437 0.0462  -0.0071 -0.1625 694 THR A CA  
1521 C C   . THR A 176 ? 0.9795 0.9438 0.6627 0.0369  -0.0028 -0.1969 694 THR A C   
1522 O O   . THR A 176 ? 0.9688 0.9081 0.6783 0.0275  0.0107  -0.1910 694 THR A O   
1523 C CB  . THR A 176 ? 1.0679 1.0309 0.6628 0.0624  0.0019  -0.1473 694 THR A CB  
1524 O OG1 . THR A 176 ? 1.1120 1.0670 0.6693 0.0757  0.0010  -0.1192 694 THR A OG1 
1525 C CG2 . THR A 176 ? 1.0504 0.9899 0.6509 0.0524  0.0223  -0.1321 694 THR A CG2 
1526 N N   . GLU A 177 ? 0.9646 0.9652 0.6500 0.0412  -0.0123 -0.2350 695 GLU A N   
1527 C CA  . GLU A 177 ? 0.9711 0.9753 0.6898 0.0313  -0.0030 -0.2722 695 GLU A CA  
1528 C C   . GLU A 177 ? 0.9222 0.8956 0.6964 0.0123  0.0065  -0.2821 695 GLU A C   
1529 O O   . GLU A 177 ? 0.9811 0.9361 0.7845 0.0045  0.0236  -0.3012 695 GLU A O   
1530 C CB  . GLU A 177 ? 1.0625 1.1222 0.7716 0.0391  -0.0147 -0.3174 695 GLU A CB  
1531 C CG  . GLU A 177 ? 1.2225 1.3115 0.8727 0.0627  -0.0186 -0.3087 695 GLU A CG  
1532 C CD  . GLU A 177 ? 1.3823 1.5284 1.0284 0.0703  -0.0252 -0.3598 695 GLU A CD  
1533 O OE1 . GLU A 177 ? 1.4426 1.5891 1.0795 0.0725  -0.0136 -0.3688 695 GLU A OE1 
1534 O OE2 . GLU A 177 ? 1.4359 1.6246 1.0995 0.0714  -0.0405 -0.3811 695 GLU A OE2 
1535 N N   . LEU A 178 ? 0.8748 0.8386 0.6625 0.0065  -0.0008 -0.2681 696 LEU A N   
1536 C CA  . LEU A 178 ? 0.8626 0.7911 0.6980 -0.0090 0.0130  -0.2705 696 LEU A CA  
1537 C C   . LEU A 178 ? 0.8388 0.7249 0.6783 -0.0062 0.0286  -0.2336 696 LEU A C   
1538 O O   . LEU A 178 ? 0.8346 0.6872 0.7079 -0.0123 0.0456  -0.2321 696 LEU A O   
1539 C CB  . LEU A 178 ? 0.8503 0.7851 0.6981 -0.0151 0.0011  -0.2670 696 LEU A CB  
1540 C CG  . LEU A 178 ? 0.8751 0.8546 0.7420 -0.0222 -0.0093 -0.3148 696 LEU A CG  
1541 C CD1 . LEU A 178 ? 0.8900 0.8916 0.7467 -0.0174 -0.0289 -0.3024 696 LEU A CD1 
1542 C CD2 . LEU A 178 ? 0.8113 0.7697 0.7355 -0.0444 0.0132  -0.3506 696 LEU A CD2 
1543 N N   . ASP A 179 ? 0.8444 0.7340 0.6503 0.0041  0.0257  -0.2054 697 ASP A N   
1544 C CA  . ASP A 179 ? 0.8213 0.6883 0.6315 0.0085  0.0383  -0.1764 697 ASP A CA  
1545 C C   . ASP A 179 ? 0.7565 0.6032 0.5868 0.0054  0.0393  -0.1536 697 ASP A C   
1546 O O   . ASP A 179 ? 0.7691 0.5955 0.6184 0.0109  0.0535  -0.1407 697 ASP A O   
1547 C CB  . ASP A 179 ? 0.9216 0.7745 0.7503 0.0129  0.0574  -0.1905 697 ASP A CB  
1548 C CG  . ASP A 179 ? 0.9801 0.8317 0.8015 0.0238  0.0665  -0.1655 697 ASP A CG  
1549 O OD1 . ASP A 179 ? 1.0251 0.8590 0.8663 0.0329  0.0837  -0.1656 697 ASP A OD1 
1550 O OD2 . ASP A 179 ? 0.9834 0.8530 0.7805 0.0243  0.0590  -0.1472 697 ASP A OD2 
1551 N N   . LEU A 180 ? 0.7566 0.6111 0.5803 0.0002  0.0248  -0.1480 698 LEU A N   
1552 C CA  . LEU A 180 ? 0.7197 0.5596 0.5576 -0.0023 0.0243  -0.1253 698 LEU A CA  
1553 C C   . LEU A 180 ? 0.7021 0.5460 0.5262 0.0033  0.0262  -0.0967 698 LEU A C   
1554 O O   . LEU A 180 ? 0.7608 0.6189 0.5585 0.0044  0.0236  -0.0918 698 LEU A O   
1555 C CB  . LEU A 180 ? 0.6840 0.5350 0.5169 -0.0081 0.0082  -0.1279 698 LEU A CB  
1556 C CG  . LEU A 180 ? 0.7095 0.5706 0.5629 -0.0159 0.0047  -0.1626 698 LEU A CG  
1557 C CD1 . LEU A 180 ? 0.7041 0.5826 0.5532 -0.0177 -0.0121 -0.1616 698 LEU A CD1 
1558 C CD2 . LEU A 180 ? 0.7272 0.5586 0.6218 -0.0240 0.0255  -0.1737 698 LEU A CD2 
1559 N N   . ARG A 181 ? 0.6690 0.5031 0.5115 0.0074  0.0333  -0.0797 699 ARG A N   
1560 C CA  . ARG A 181 ? 0.6735 0.5238 0.5102 0.0123  0.0347  -0.0594 699 ARG A CA  
1561 C C   . ARG A 181 ? 0.6764 0.5287 0.5160 0.0070  0.0266  -0.0446 699 ARG A C   
1562 O O   . ARG A 181 ? 0.6853 0.5229 0.5348 0.0026  0.0220  -0.0462 699 ARG A O   
1563 C CB  . ARG A 181 ? 0.6836 0.5353 0.5356 0.0286  0.0488  -0.0525 699 ARG A CB  
1564 C CG  . ARG A 181 ? 0.7197 0.5642 0.5723 0.0354  0.0597  -0.0682 699 ARG A CG  
1565 C CD  . ARG A 181 ? 0.7415 0.6082 0.5720 0.0292  0.0554  -0.0771 699 ARG A CD  
1566 N NE  . ARG A 181 ? 0.7712 0.6349 0.6017 0.0360  0.0656  -0.0934 699 ARG A NE  
1567 C CZ  . ARG A 181 ? 0.7694 0.6444 0.6065 0.0509  0.0773  -0.0905 699 ARG A CZ  
1568 N NH1 . ARG A 181 ? 0.7343 0.6318 0.5788 0.0617  0.0789  -0.0733 699 ARG A NH1 
1569 N NH2 . ARG A 181 ? 0.7287 0.5986 0.5656 0.0567  0.0872  -0.1070 699 ARG A NH2 
1570 N N   . PHE A 182 ? 0.6698 0.5437 0.5037 0.0057  0.0264  -0.0336 700 PHE A N   
1571 C CA  . PHE A 182 ? 0.6608 0.5408 0.4985 0.0001  0.0205  -0.0223 700 PHE A CA  
1572 C C   . PHE A 182 ? 0.6937 0.5789 0.5511 0.0131  0.0241  -0.0113 700 PHE A C   
1573 O O   . PHE A 182 ? 0.6352 0.5507 0.4982 0.0189  0.0254  -0.0044 700 PHE A O   
1574 C CB  . PHE A 182 ? 0.6259 0.5279 0.4539 -0.0092 0.0236  -0.0212 700 PHE A CB  
1575 C CG  . PHE A 182 ? 0.6319 0.5166 0.4356 -0.0200 0.0227  -0.0222 700 PHE A CG  
1576 C CD1 . PHE A 182 ? 0.5952 0.4741 0.3941 -0.0290 0.0218  -0.0153 700 PHE A CD1 
1577 C CD2 . PHE A 182 ? 0.6714 0.5455 0.4543 -0.0176 0.0245  -0.0290 700 PHE A CD2 
1578 C CE1 . PHE A 182 ? 0.6764 0.5341 0.4479 -0.0325 0.0250  -0.0117 700 PHE A CE1 
1579 C CE2 . PHE A 182 ? 0.7204 0.5795 0.4739 -0.0198 0.0258  -0.0256 700 PHE A CE2 
1580 C CZ  . PHE A 182 ? 0.7074 0.5557 0.4541 -0.0257 0.0271  -0.0151 700 PHE A CZ  
1581 N N   . ILE A 183 ? 0.7140 0.5714 0.5823 0.0185  0.0285  -0.0115 701 ILE A N   
1582 C CA  . ILE A 183 ? 0.7553 0.6050 0.6376 0.0343  0.0382  0.0030  701 ILE A CA  
1583 C C   . ILE A 183 ? 0.7978 0.6161 0.6915 0.0251  0.0393  0.0009  701 ILE A C   
1584 O O   . ILE A 183 ? 0.8028 0.6096 0.6968 0.0098  0.0329  -0.0164 701 ILE A O   
1585 C CB  . ILE A 183 ? 0.8139 0.6538 0.7013 0.0558  0.0559  0.0062  701 ILE A CB  
1586 C CG1 . ILE A 183 ? 0.8583 0.6621 0.7520 0.0475  0.0647  -0.0122 701 ILE A CG1 
1587 C CG2 . ILE A 183 ? 0.8134 0.6936 0.6931 0.0662  0.0545  0.0053  701 ILE A CG2 
1588 C CD1 . ILE A 183 ? 0.9193 0.7017 0.8198 0.0685  0.0875  -0.0095 701 ILE A CD1 
1589 N N   . ILE A 184 ? 0.8178 0.6276 0.7206 0.0365  0.0485  0.0175  702 ILE A N   
1590 C CA  . ILE A 184 ? 0.8729 0.6530 0.7908 0.0279  0.0552  0.0161  702 ILE A CA  
1591 C C   . ILE A 184 ? 0.8895 0.6367 0.8175 0.0474  0.0836  0.0307  702 ILE A C   
1592 O O   . ILE A 184 ? 0.8777 0.6382 0.7961 0.0733  0.0909  0.0537  702 ILE A O   
1593 C CB  . ILE A 184 ? 0.9073 0.7046 0.8235 0.0212  0.0418  0.0252  702 ILE A CB  
1594 C CG1 . ILE A 184 ? 0.9561 0.7668 0.8643 0.0015  0.0211  0.0097  702 ILE A CG1 
1595 C CG2 . ILE A 184 ? 0.9349 0.7044 0.8679 0.0204  0.0560  0.0312  702 ILE A CG2 
1596 C CD1 . ILE A 184 ? 1.0049 0.7990 0.9235 -0.0122 0.0197  -0.0125 702 ILE A CD1 
1597 N N   . ASP A 185 ? 0.9706 0.6770 0.9177 0.0368  0.1022  0.0159  703 ASP A N   
1598 C CA  . ASP A 185 ? 1.1111 0.7709 1.0692 0.0530  0.1383  0.0296  703 ASP A CA  
1599 C C   . ASP A 185 ? 1.2060 0.8412 1.1826 0.0394  0.1507  0.0296  703 ASP A C   
1600 O O   . ASP A 185 ? 1.2327 0.8686 1.2288 0.0107  0.1431  0.0007  703 ASP A O   
1601 C CB  . ASP A 185 ? 1.1513 0.7754 1.1230 0.0495  0.1610  0.0091  703 ASP A CB  
1602 C CG  . ASP A 185 ? 1.2247 0.8711 1.1788 0.0654  0.1526  0.0104  703 ASP A CG  
1603 O OD1 . ASP A 185 ? 1.2316 0.9260 1.1670 0.0701  0.1258  0.0189  703 ASP A OD1 
1604 O OD2 . ASP A 185 ? 1.2963 0.9122 1.2569 0.0733  0.1758  0.0025  703 ASP A OD2 
1605 N N   . GLU A 186 ? 1.2820 0.9005 1.2518 0.0624  0.1706  0.0611  704 GLU A N   
1606 C CA  . GLU A 186 ? 1.3040 0.8984 1.2887 0.0531  0.1867  0.0664  704 GLU A CA  
1607 C C   . GLU A 186 ? 1.3064 0.8344 1.2997 0.0693  0.2383  0.0824  704 GLU A C   
1608 O O   . GLU A 186 ? 1.2850 0.7977 1.2580 0.1051  0.2571  0.1093  704 GLU A O   
1609 C CB  . GLU A 186 ? 1.3265 0.9598 1.2918 0.0671  0.1676  0.0916  704 GLU A CB  
1610 C CG  . GLU A 186 ? 1.3600 0.9884 1.3413 0.0477  0.1682  0.0874  704 GLU A CG  
1611 C CD  . GLU A 186 ? 1.3883 1.0499 1.3493 0.0669  0.1569  0.1147  704 GLU A CD  
1612 O OE1 . GLU A 186 ? 1.3993 1.0917 1.3357 0.0957  0.1493  0.1343  704 GLU A OE1 
1613 O OE2 . GLU A 186 ? 1.3955 1.0580 1.3668 0.0536  0.1558  0.1134  704 GLU A OE2 
1614 N N   . GLU A 187 ? 1.3564 0.8523 1.3802 0.0436  0.2616  0.0641  705 GLU A N   
1615 C CA  . GLU A 187 ? 1.4100 0.8735 1.4464 0.0487  0.3054  0.0690  705 GLU A CA  
1616 C C   . GLU A 187 ? 1.4315 0.8957 1.4576 0.0647  0.3206  0.0992  705 GLU A C   
1617 O O   . GLU A 187 ? 1.4664 0.9337 1.5146 0.0402  0.3225  0.0846  705 GLU A O   
1618 C CB  . GLU A 187 ? 1.4046 0.8569 1.4841 0.0083  0.3197  0.0226  705 GLU A CB  
1619 C CG  . GLU A 187 ? 1.4097 0.8534 1.4992 0.0003  0.3226  -0.0044 705 GLU A CG  
1620 C CD  . GLU A 187 ? 1.4896 0.9004 1.5607 0.0328  0.3549  0.0234  705 GLU A CD  
1621 O OE1 . GLU A 187 ? 1.4819 0.9005 1.5208 0.0638  0.3397  0.0483  705 GLU A OE1 
1622 O OE2 . GLU A 187 ? 1.5504 0.9295 1.6397 0.0283  0.3975  0.0198  705 GLU A OE2 
1623 N N   . LEU A 188 ? 1.3950 0.8619 1.3871 0.1077  0.3317  0.1391  706 LEU A N   
1624 C CA  . LEU A 188 ? 1.3646 0.8373 1.3407 0.1297  0.3470  0.1686  706 LEU A CA  
1625 C C   . LEU A 188 ? 1.3538 0.7959 1.3147 0.1626  0.3938  0.1934  706 LEU A C   
1626 O O   . LEU A 188 ? 1.3064 0.7523 1.2438 0.1935  0.3966  0.2099  706 LEU A O   
1627 C CB  . LEU A 188 ? 1.3564 0.8806 1.3007 0.1556  0.3114  0.1930  706 LEU A CB  
1628 C CG  . LEU A 188 ? 1.3347 0.8894 1.2841 0.1319  0.2660  0.1753  706 LEU A CG  
1629 C CD1 . LEU A 188 ? 1.3059 0.9154 1.2246 0.1596  0.2384  0.2000  706 LEU A CD1 
1630 C CD2 . LEU A 188 ? 1.3217 0.8653 1.3040 0.0884  0.2616  0.1469  706 LEU A CD2 
1631 N N   . PHE A 189 ? 1.3799 0.7918 1.3537 0.1570  0.4328  0.1959  707 PHE A N   
1632 C CA  . PHE A 189 ? 1.4093 0.7870 1.3656 0.1908  0.4848  0.2232  707 PHE A CA  
1633 C C   . PHE A 189 ? 1.5072 0.8483 1.4705 0.1911  0.5118  0.2147  707 PHE A C   
1634 O O   . PHE A 189 ? 1.5724 0.9012 1.5058 0.2316  0.5374  0.2437  707 PHE A O   
1635 C CB  . PHE A 189 ? 1.3382 0.7517 1.2467 0.2448  0.4780  0.2649  707 PHE A CB  
1636 C CG  . PHE A 189 ? 1.2860 0.7414 1.1873 0.2452  0.4492  0.2716  707 PHE A CG  
1637 C CD1 . PHE A 189 ? 1.2306 0.7392 1.1259 0.2393  0.3953  0.2652  707 PHE A CD1 
1638 C CD2 . PHE A 189 ? 1.3067 0.7466 1.2081 0.2513  0.4788  0.2836  707 PHE A CD2 
1639 C CE1 . PHE A 189 ? 1.1873 0.7342 1.0767 0.2384  0.3707  0.2702  707 PHE A CE1 
1640 C CE2 . PHE A 189 ? 1.2755 0.7542 1.1708 0.2514  0.4525  0.2889  707 PHE A CE2 
1641 C CZ  . PHE A 189 ? 1.2088 0.7417 1.0983 0.2443  0.3981  0.2819  707 PHE A CZ  
1642 N N   . GLY A 190 ? 1.5183 0.8458 1.5211 0.1465  0.5063  0.1733  708 GLY A N   
1643 C CA  . GLY A 190 ? 1.5732 0.8675 1.5888 0.1406  0.5318  0.1587  708 GLY A CA  
1644 C C   . GLY A 190 ? 1.5545 0.8665 1.5434 0.1660  0.5060  0.1700  708 GLY A C   
1645 O O   . GLY A 190 ? 1.6142 0.8964 1.6004 0.1778  0.5341  0.1727  708 GLY A O   
1646 N N   . GLN A 191 ? 1.4950 0.8552 1.4654 0.1748  0.4552  0.1758  709 GLN A N   
1647 C CA  . GLN A 191 ? 1.4706 0.8554 1.4155 0.2024  0.4308  0.1868  709 GLN A CA  
1648 C C   . GLN A 191 ? 1.4315 0.8532 1.3845 0.1797  0.3788  0.1631  709 GLN A C   
1649 O O   . GLN A 191 ? 1.3855 0.8275 1.3470 0.1593  0.3555  0.1550  709 GLN A O   
1650 C CB  . GLN A 191 ? 1.4586 0.8749 1.3583 0.2576  0.4315  0.2312  709 GLN A CB  
1651 C CG  . GLN A 191 ? 1.5236 0.9028 1.4053 0.2900  0.4859  0.2589  709 GLN A CG  
1652 C CD  . GLN A 191 ? 1.5360 0.8854 1.4159 0.3004  0.5071  0.2568  709 GLN A CD  
1653 O OE1 . GLN A 191 ? 1.5017 0.8779 1.3769 0.3054  0.4759  0.2480  709 GLN A OE1 
1654 N NE2 . GLN A 191 ? 1.6071 0.8999 1.4916 0.3040  0.5630  0.2641  709 GLN A NE2 
1655 N N   . THR A 192 ? 1.4360 0.8646 1.3851 0.1849  0.3636  0.1524  710 THR A N   
1656 C CA  . THR A 192 ? 1.3758 0.8356 1.3272 0.1692  0.3199  0.1319  710 THR A CA  
1657 C C   . THR A 192 ? 1.2846 0.7972 1.2030 0.2055  0.2913  0.1613  710 THR A C   
1658 O O   . THR A 192 ? 1.3451 0.8788 1.2384 0.2477  0.2983  0.1869  710 THR A O   
1659 C CB  . THR A 192 ? 1.4195 0.8668 1.3803 0.1608  0.3186  0.1051  710 THR A CB  
1660 O OG1 . THR A 192 ? 1.4740 0.9308 1.4089 0.2049  0.3270  0.1308  710 THR A OG1 
1661 C CG2 . THR A 192 ? 1.4588 0.8650 1.4537 0.1275  0.3488  0.0738  710 THR A CG2 
1662 N N   . HIS A 193 ? 1.1289 0.6817 1.0490 0.1845  0.2553  0.1518  711 HIS A N   
1663 C CA  . HIS A 193 ? 1.0266 0.6578 0.9243 0.2021  0.2190  0.1636  711 HIS A CA  
1664 C C   . HIS A 193 ? 0.8894 0.5667 0.7946 0.1695  0.1797  0.1304  711 HIS A C   
1665 O O   . HIS A 193 ? 0.8441 0.5231 0.7642 0.1315  0.1618  0.1073  711 HIS A O   
1666 C CB  . HIS A 193 ? 1.0449 0.6965 0.9374 0.2015  0.2105  0.1782  711 HIS A CB  
1667 C CG  . HIS A 193 ? 1.1516 0.7760 1.0284 0.2391  0.2461  0.2144  711 HIS A CG  
1668 N ND1 . HIS A 193 ? 1.1537 0.8151 1.0175 0.2513  0.2385  0.2313  711 HIS A ND1 
1669 C CD2 . HIS A 193 ? 1.2145 0.8026 1.0891 0.2554  0.2850  0.2247  711 HIS A CD2 
1670 C CE1 . HIS A 193 ? 1.1972 0.8452 1.0498 0.2763  0.2715  0.2512  711 HIS A CE1 
1671 N NE2 . HIS A 193 ? 1.2535 0.8552 1.1113 0.2794  0.3014  0.2493  711 HIS A NE2 
1672 N N   . GLN A 194 ? 0.8740 0.5901 0.7674 0.1870  0.1683  0.1291  712 GLN A N   
1673 C CA  . GLN A 194 ? 0.8337 0.5914 0.7302 0.1598  0.1368  0.1015  712 GLN A CA  
1674 C C   . GLN A 194 ? 0.8315 0.6604 0.7182 0.1614  0.1087  0.1034  712 GLN A C   
1675 O O   . GLN A 194 ? 0.8332 0.7033 0.7076 0.1952  0.1100  0.1216  712 GLN A O   
1676 C CB  . GLN A 194 ? 0.8961 0.6548 0.7903 0.1707  0.1428  0.0922  712 GLN A CB  
1677 C CG  . GLN A 194 ? 1.0174 0.7190 0.9280 0.1474  0.1583  0.0705  712 GLN A CG  
1678 C CD  . GLN A 194 ? 1.1129 0.8090 1.0223 0.1575  0.1676  0.0597  712 GLN A CD  
1679 O OE1 . GLN A 194 ? 1.0996 0.8275 1.0069 0.1401  0.1466  0.0386  712 GLN A OE1 
1680 N NE2 . GLN A 194 ? 1.1966 0.8467 1.1067 0.1859  0.2029  0.0742  712 GLN A NE2 
1681 N N   . HIS A 195 ? 0.7417 0.5866 0.6340 0.1260  0.0853  0.0826  713 HIS A N   
1682 C CA  . HIS A 195 ? 0.7684 0.6725 0.6564 0.1178  0.0625  0.0765  713 HIS A CA  
1683 C C   . HIS A 195 ? 0.7251 0.6371 0.6136 0.0902  0.0489  0.0528  713 HIS A C   
1684 O O   . HIS A 195 ? 0.7293 0.6109 0.6203 0.0649  0.0431  0.0413  713 HIS A O   
1685 C CB  . HIS A 195 ? 0.7497 0.6493 0.6408 0.1056  0.0560  0.0820  713 HIS A CB  
1686 C CG  . HIS A 195 ? 0.7867 0.7420 0.6762 0.0973  0.0377  0.0753  713 HIS A CG  
1687 N ND1 . HIS A 195 ? 0.7929 0.7437 0.6862 0.0669  0.0242  0.0625  713 HIS A ND1 
1688 C CD2 . HIS A 195 ? 0.8149 0.8339 0.7012 0.1160  0.0328  0.0765  713 HIS A CD2 
1689 C CE1 . HIS A 195 ? 0.7793 0.7800 0.6732 0.0646  0.0149  0.0565  713 HIS A CE1 
1690 N NE2 . HIS A 195 ? 0.7845 0.8322 0.6762 0.0923  0.0188  0.0618  713 HIS A NE2 
1691 N N   . GLU A 196 ? 0.7541 0.7079 0.6394 0.0981  0.0461  0.0456  714 GLU A N   
1692 C CA  . GLU A 196 ? 0.7968 0.7667 0.6802 0.0719  0.0357  0.0255  714 GLU A CA  
1693 C C   . GLU A 196 ? 0.8495 0.8178 0.7324 0.0469  0.0244  0.0210  714 GLU A C   
1694 O O   . GLU A 196 ? 0.9956 0.9712 0.8824 0.0519  0.0217  0.0307  714 GLU A O   
1695 C CB  . GLU A 196 ? 0.7927 0.8228 0.6783 0.0822  0.0360  0.0163  714 GLU A CB  
1696 C CG  . GLU A 196 ? 0.7792 0.8737 0.6721 0.0893  0.0301  0.0137  714 GLU A CG  
1697 C CD  . GLU A 196 ? 0.7543 0.9193 0.6562 0.0947  0.0308  -0.0048 714 GLU A CD  
1698 O OE1 . GLU A 196 ? 0.7667 0.9279 0.6668 0.1005  0.0372  -0.0094 714 GLU A OE1 
1699 O OE2 . GLU A 196 ? 0.7218 0.9505 0.6353 0.0914  0.0259  -0.0189 714 GLU A OE2 
1700 N N   . LEU A 197 ? 0.7966 0.7532 0.6721 0.0234  0.0200  0.0081  715 LEU A N   
1701 C CA  . LEU A 197 ? 0.7176 0.6673 0.5899 0.0042  0.0129  0.0063  715 LEU A CA  
1702 C C   . LEU A 197 ? 0.7144 0.6962 0.5872 -0.0106 0.0156  -0.0051 715 LEU A C   
1703 O O   . LEU A 197 ? 0.6558 0.6338 0.5283 -0.0241 0.0137  -0.0063 715 LEU A O   
1704 C CB  . LEU A 197 ? 0.7480 0.6562 0.6085 -0.0078 0.0084  0.0037  715 LEU A CB  
1705 C CG  . LEU A 197 ? 0.7259 0.6059 0.5935 -0.0044 0.0048  0.0084  715 LEU A CG  
1706 C CD1 . LEU A 197 ? 0.7200 0.5768 0.5776 -0.0125 -0.0003 -0.0023 715 LEU A CD1 
1707 C CD2 . LEU A 197 ? 0.7091 0.5926 0.5837 -0.0077 -0.0004 0.0165  715 LEU A CD2 
1708 N N   . LYS A 198 ? 0.7104 0.7205 0.5856 -0.0101 0.0229  -0.0156 716 LYS A N   
1709 C CA  . LYS A 198 ? 0.7065 0.7597 0.5922 -0.0242 0.0306  -0.0324 716 LYS A CA  
1710 C C   . LYS A 198 ? 0.6420 0.7443 0.5387 -0.0080 0.0341  -0.0408 716 LYS A C   
1711 O O   . LYS A 198 ? 0.5999 0.6906 0.4918 0.0139  0.0320  -0.0299 716 LYS A O   
1712 C CB  . LYS A 198 ? 0.7422 0.7651 0.6150 -0.0487 0.0423  -0.0397 716 LYS A CB  
1713 C CG  . LYS A 198 ? 0.7659 0.7676 0.6230 -0.0457 0.0477  -0.0391 716 LYS A CG  
1714 C CD  . LYS A 198 ? 0.8354 0.7895 0.6677 -0.0587 0.0551  -0.0340 716 LYS A CD  
1715 C CE  . LYS A 198 ? 0.8623 0.8250 0.7004 -0.0809 0.0755  -0.0459 716 LYS A CE  
1716 N NZ  . LYS A 198 ? 0.9115 0.8385 0.7238 -0.0895 0.0953  -0.0437 716 LYS A NZ  
1717 N N   . ASN A 199 ? 0.5950 0.7546 0.5089 -0.0182 0.0414  -0.0626 717 ASN A N   
1718 C CA  . ASN A 199 ? 0.5436 0.7649 0.4708 -0.0008 0.0438  -0.0747 717 ASN A CA  
1719 C C   . ASN A 199 ? 0.5860 0.7772 0.5009 0.0029  0.0502  -0.0713 717 ASN A C   
1720 O O   . ASN A 199 ? 0.6441 0.7993 0.5484 -0.0201 0.0600  -0.0761 717 ASN A O   
1721 C CB  . ASN A 199 ? 0.6465 0.9358 0.5990 -0.0218 0.0538  -0.1078 717 ASN A CB  
1722 C CG  . ASN A 199 ? 0.7564 1.1284 0.7272 -0.0012 0.0539  -0.1252 717 ASN A CG  
1723 O OD1 . ASN A 199 ? 0.7946 1.1958 0.7619 0.0372  0.0428  -0.1113 717 ASN A OD1 
1724 N ND2 . ASN A 199 ? 0.7983 1.2088 0.7882 -0.0249 0.0694  -0.1557 717 ASN A ND2 
1725 N N   . GLY A 200 ? 0.5940 0.7994 0.5082 0.0346  0.0469  -0.0622 718 GLY A N   
1726 C CA  . GLY A 200 ? 0.5695 0.7448 0.4728 0.0407  0.0530  -0.0596 718 GLY A CA  
1727 C C   . GLY A 200 ? 0.6288 0.7260 0.5119 0.0328  0.0510  -0.0459 718 GLY A C   
1728 O O   . GLY A 200 ? 0.6594 0.7316 0.5312 0.0266  0.0567  -0.0506 718 GLY A O   
1729 N N   . GLY A 201 ? 0.6507 0.7156 0.5301 0.0337  0.0431  -0.0317 719 GLY A N   
1730 C CA  . GLY A 201 ? 0.6563 0.6602 0.5210 0.0233  0.0399  -0.0255 719 GLY A CA  
1731 C C   . GLY A 201 ? 0.6496 0.6233 0.5097 0.0364  0.0444  -0.0249 719 GLY A C   
1732 O O   . GLY A 201 ? 0.6397 0.5805 0.4873 0.0254  0.0432  -0.0307 719 GLY A O   
1733 N N   . SER A 202 ? 0.6591 0.6456 0.5283 0.0623  0.0510  -0.0192 720 SER A N   
1734 C CA  . SER A 202 ? 0.6949 0.6462 0.5629 0.0746  0.0604  -0.0203 720 SER A CA  
1735 C C   . SER A 202 ? 0.6842 0.6387 0.5436 0.0655  0.0637  -0.0368 720 SER A C   
1736 O O   . SER A 202 ? 0.7273 0.6491 0.5838 0.0665  0.0693  -0.0446 720 SER A O   
1737 C CB  . SER A 202 ? 0.7384 0.6994 0.6143 0.1098  0.0722  -0.0071 720 SER A CB  
1738 O OG  . SER A 202 ? 0.8151 0.8403 0.6948 0.1240  0.0706  -0.0093 720 SER A OG  
1739 N N   . GLU A 203 ? 0.6508 0.6446 0.5074 0.0551  0.0630  -0.0449 721 GLU A N   
1740 C CA  . GLU A 203 ? 0.7080 0.7062 0.5543 0.0468  0.0694  -0.0588 721 GLU A CA  
1741 C C   . GLU A 203 ? 0.7123 0.6902 0.5380 0.0223  0.0671  -0.0630 721 GLU A C   
1742 O O   . GLU A 203 ? 0.7402 0.7195 0.5517 0.0160  0.0747  -0.0722 721 GLU A O   
1743 C CB  . GLU A 203 ? 0.7467 0.8027 0.6046 0.0523  0.0766  -0.0674 721 GLU A CB  
1744 C CG  . GLU A 203 ? 0.8462 0.9362 0.7207 0.0845  0.0779  -0.0608 721 GLU A CG  
1745 C CD  . GLU A 203 ? 0.9964 1.0443 0.8683 0.1086  0.0845  -0.0521 721 GLU A CD  
1746 O OE1 . GLU A 203 ? 1.0457 1.0803 0.9222 0.1304  0.0862  -0.0356 721 GLU A OE1 
1747 O OE2 . GLU A 203 ? 1.0386 1.0648 0.9038 0.1056  0.0913  -0.0625 721 GLU A OE2 
1748 N N   . ILE A 204 ? 0.6890 0.6478 0.5100 0.0119  0.0586  -0.0549 722 ILE A N   
1749 C CA  . ILE A 204 ? 0.6577 0.5966 0.4551 -0.0045 0.0583  -0.0542 722 ILE A CA  
1750 C C   . ILE A 204 ? 0.6587 0.5657 0.4424 -0.0008 0.0485  -0.0560 722 ILE A C   
1751 O O   . ILE A 204 ? 0.6675 0.5612 0.4632 0.0020  0.0394  -0.0527 722 ILE A O   
1752 C CB  . ILE A 204 ? 0.6546 0.5970 0.4558 -0.0170 0.0571  -0.0465 722 ILE A CB  
1753 C CG1 . ILE A 204 ? 0.6712 0.6584 0.4934 -0.0223 0.0667  -0.0537 722 ILE A CG1 
1754 C CG2 . ILE A 204 ? 0.6529 0.5678 0.4254 -0.0285 0.0622  -0.0420 722 ILE A CG2 
1755 C CD1 . ILE A 204 ? 0.6709 0.6699 0.5051 -0.0339 0.0656  -0.0519 722 ILE A CD1 
1756 N N   . VAL A 205 ? 0.6644 0.5646 0.4239 -0.0007 0.0516  -0.0637 723 VAL A N   
1757 C CA  . VAL A 205 ? 0.7336 0.6192 0.4810 0.0040  0.0416  -0.0734 723 VAL A CA  
1758 C C   . VAL A 205 ? 0.7680 0.6432 0.4937 0.0012  0.0334  -0.0644 723 VAL A C   
1759 O O   . VAL A 205 ? 0.7177 0.5884 0.4200 -0.0021 0.0422  -0.0525 723 VAL A O   
1760 C CB  . VAL A 205 ? 0.7260 0.6182 0.4542 0.0098  0.0475  -0.0877 723 VAL A CB  
1761 C CG1 . VAL A 205 ? 0.7580 0.6487 0.4765 0.0149  0.0360  -0.1052 723 VAL A CG1 
1762 C CG2 . VAL A 205 ? 0.7029 0.6044 0.4532 0.0150  0.0572  -0.0961 723 VAL A CG2 
1763 N N   . VAL A 206 ? 0.7873 0.6576 0.5217 0.0032  0.0198  -0.0710 724 VAL A N   
1764 C CA  . VAL A 206 ? 0.7747 0.6410 0.4895 0.0055  0.0099  -0.0644 724 VAL A CA  
1765 C C   . VAL A 206 ? 0.8984 0.7748 0.5751 0.0182  0.0077  -0.0721 724 VAL A C   
1766 O O   . VAL A 206 ? 0.9637 0.8570 0.6440 0.0234  -0.0002 -0.0955 724 VAL A O   
1767 C CB  . VAL A 206 ? 0.7629 0.6289 0.5039 0.0030  -0.0031 -0.0728 724 VAL A CB  
1768 C CG1 . VAL A 206 ? 0.7614 0.6307 0.4816 0.0091  -0.0145 -0.0676 724 VAL A CG1 
1769 C CG2 . VAL A 206 ? 0.7551 0.6116 0.5274 -0.0046 0.0012  -0.0615 724 VAL A CG2 
1770 N N   . THR A 207 ? 0.9182 0.7847 0.5578 0.0242  0.0176  -0.0536 725 THR A N   
1771 C CA  . THR A 207 ? 0.9317 0.8064 0.5249 0.0433  0.0191  -0.0536 725 THR A CA  
1772 C C   . THR A 207 ? 0.9543 0.8205 0.5163 0.0583  0.0153  -0.0359 725 THR A C   
1773 O O   . THR A 207 ? 0.9889 0.8425 0.5690 0.0508  0.0111  -0.0267 725 THR A O   
1774 C CB  . THR A 207 ? 0.9384 0.8026 0.5070 0.0428  0.0427  -0.0435 725 THR A CB  
1775 O OG1 . THR A 207 ? 0.9701 0.8047 0.5241 0.0369  0.0629  -0.0185 725 THR A OG1 
1776 C CG2 . THR A 207 ? 0.9023 0.7746 0.5073 0.0276  0.0482  -0.0570 725 THR A CG2 
1777 N N   . ASN A 208 ? 0.9731 0.8475 0.4850 0.0836  0.0180  -0.0302 726 ASN A N   
1778 C CA  . ASN A 208 ? 1.0140 0.8794 0.4876 0.1068  0.0178  -0.0094 726 ASN A CA  
1779 C C   . ASN A 208 ? 0.9573 0.7723 0.4218 0.0973  0.0446  0.0214  726 ASN A C   
1780 O O   . ASN A 208 ? 0.9385 0.7371 0.3928 0.1066  0.0444  0.0372  726 ASN A O   
1781 C CB  . ASN A 208 ? 1.1309 1.0167 0.5449 0.1427  0.0195  -0.0057 726 ASN A CB  
1782 C CG  . ASN A 208 ? 1.1770 1.1224 0.5922 0.1625  -0.0118 -0.0349 726 ASN A CG  
1783 O OD1 . ASN A 208 ? 1.1505 1.1117 0.5944 0.1587  -0.0306 -0.0456 726 ASN A OD1 
1784 N ND2 . ASN A 208 ? 1.2459 1.2302 0.6319 0.1831  -0.0166 -0.0516 726 ASN A ND2 
1785 N N   . LYS A 209 ? 0.9385 0.7314 0.4101 0.0779  0.0694  0.0265  727 LYS A N   
1786 C CA  . LYS A 209 ? 0.9377 0.6860 0.4032 0.0653  0.1011  0.0486  727 LYS A CA  
1787 C C   . LYS A 209 ? 0.8978 0.6414 0.4124 0.0397  0.0954  0.0440  727 LYS A C   
1788 O O   . LYS A 209 ? 0.9379 0.6475 0.4480 0.0326  0.1169  0.0592  727 LYS A O   
1789 C CB  . LYS A 209 ? 0.9918 0.7282 0.4536 0.0507  0.1313  0.0487  727 LYS A CB  
1790 C CG  . LYS A 209 ? 1.1143 0.8280 0.5129 0.0760  0.1576  0.0687  727 LYS A CG  
1791 C CD  . LYS A 209 ? 1.2226 0.9308 0.6232 0.0591  0.1867  0.0640  727 LYS A CD  
1792 C CE  . LYS A 209 ? 1.2968 1.0471 0.6931 0.0698  0.1674  0.0448  727 LYS A CE  
1793 N NZ  . LYS A 209 ? 1.3370 1.0931 0.7537 0.0476  0.1887  0.0331  727 LYS A NZ  
1794 N N   . ASN A 210 ? 0.7835 0.5584 0.3433 0.0271  0.0703  0.0237  728 ASN A N   
1795 C CA  . ASN A 210 ? 0.7144 0.4904 0.3176 0.0065  0.0655  0.0203  728 ASN A CA  
1796 C C   . ASN A 210 ? 0.6933 0.4868 0.3185 0.0115  0.0365  0.0124  728 ASN A C   
1797 O O   . ASN A 210 ? 0.6865 0.4860 0.3482 -0.0029 0.0305  0.0086  728 ASN A O   
1798 C CB  . ASN A 210 ? 0.6867 0.4817 0.3268 -0.0138 0.0716  0.0068  728 ASN A CB  
1799 C CG  . ASN A 210 ? 0.7119 0.5335 0.3662 -0.0081 0.0550  -0.0097 728 ASN A CG  
1800 O OD1 . ASN A 210 ? 0.7160 0.5456 0.3638 0.0050  0.0368  -0.0167 728 ASN A OD1 
1801 N ND2 . ASN A 210 ? 0.6706 0.5089 0.3470 -0.0180 0.0633  -0.0190 728 ASN A ND2 
1802 N N   . LYS A 211 ? 0.7185 0.5253 0.3232 0.0320  0.0198  0.0077  729 LYS A N   
1803 C CA  . LYS A 211 ? 0.7505 0.5793 0.3837 0.0322  -0.0047 -0.0070 729 LYS A CA  
1804 C C   . LYS A 211 ? 0.7420 0.5589 0.3795 0.0328  -0.0085 0.0052  729 LYS A C   
1805 O O   . LYS A 211 ? 0.7322 0.5596 0.4051 0.0231  -0.0213 -0.0036 729 LYS A O   
1806 C CB  . LYS A 211 ? 0.7687 0.6285 0.3856 0.0514  -0.0212 -0.0251 729 LYS A CB  
1807 C CG  . LYS A 211 ? 0.8066 0.6695 0.3718 0.0812  -0.0214 -0.0120 729 LYS A CG  
1808 C CD  . LYS A 211 ? 0.8402 0.7520 0.3953 0.1004  -0.0411 -0.0384 729 LYS A CD  
1809 C CE  . LYS A 211 ? 0.9489 0.8760 0.4483 0.1392  -0.0441 -0.0253 729 LYS A CE  
1810 N NZ  . LYS A 211 ? 1.0130 1.0039 0.5054 0.1586  -0.0655 -0.0583 729 LYS A NZ  
1811 N N   . LYS A 212 ? 0.7675 0.5592 0.3688 0.0453  0.0056  0.0261  730 LYS A N   
1812 C CA  . LYS A 212 ? 0.7737 0.5495 0.3802 0.0452  0.0058  0.0377  730 LYS A CA  
1813 C C   . LYS A 212 ? 0.7507 0.5195 0.3983 0.0170  0.0121  0.0354  730 LYS A C   
1814 O O   . LYS A 212 ? 0.7286 0.5051 0.4023 0.0112  0.0001  0.0323  730 LYS A O   
1815 C CB  . LYS A 212 ? 0.8362 0.5751 0.3950 0.0640  0.0288  0.0626  730 LYS A CB  
1816 C CG  . LYS A 212 ? 0.9412 0.6935 0.4517 0.1024  0.0212  0.0692  730 LYS A CG  
1817 C CD  . LYS A 212 ? 0.9543 0.7411 0.4740 0.1190  -0.0072 0.0595  730 LYS A CD  
1818 C CE  . LYS A 212 ? 0.9563 0.7122 0.4632 0.1302  0.0033  0.0808  730 LYS A CE  
1819 N NZ  . LYS A 212 ? 0.9074 0.7032 0.4301 0.1438  -0.0249 0.0682  730 LYS A NZ  
1820 N N   . GLU A 213 ? 0.7457 0.5066 0.3997 0.0009  0.0310  0.0349  731 GLU A N   
1821 C CA  . GLU A 213 ? 0.7013 0.4727 0.3949 -0.0218 0.0343  0.0276  731 GLU A CA  
1822 C C   . GLU A 213 ? 0.6366 0.4369 0.3632 -0.0236 0.0127  0.0155  731 GLU A C   
1823 O O   . GLU A 213 ? 0.6090 0.4190 0.3628 -0.0312 0.0068  0.0142  731 GLU A O   
1824 C CB  . GLU A 213 ? 0.7496 0.5204 0.4455 -0.0363 0.0575  0.0235  731 GLU A CB  
1825 C CG  . GLU A 213 ? 0.7730 0.5705 0.5091 -0.0556 0.0601  0.0116  731 GLU A CG  
1826 C CD  . GLU A 213 ? 0.8486 0.6607 0.5922 -0.0685 0.0799  0.0009  731 GLU A CD  
1827 O OE1 . GLU A 213 ? 0.8454 0.6930 0.6217 -0.0805 0.0810  -0.0127 731 GLU A OE1 
1828 O OE2 . GLU A 213 ? 0.8912 0.6846 0.6076 -0.0646 0.0947  0.0051  731 GLU A OE2 
1829 N N   . TYR A 214 ? 0.6163 0.4283 0.3399 -0.0158 0.0042  0.0063  732 TYR A N   
1830 C CA  . TYR A 214 ? 0.6070 0.4358 0.3613 -0.0172 -0.0085 -0.0054 732 TYR A CA  
1831 C C   . TYR A 214 ? 0.6265 0.4571 0.3952 -0.0155 -0.0222 -0.0068 732 TYR A C   
1832 O O   . TYR A 214 ? 0.5736 0.4081 0.3702 -0.0217 -0.0239 -0.0061 732 TYR A O   
1833 C CB  . TYR A 214 ? 0.6193 0.4564 0.3671 -0.0100 -0.0119 -0.0193 732 TYR A CB  
1834 C CG  . TYR A 214 ? 0.6323 0.4771 0.4115 -0.0118 -0.0188 -0.0339 732 TYR A CG  
1835 C CD1 . TYR A 214 ? 0.6277 0.4723 0.4309 -0.0153 -0.0105 -0.0327 732 TYR A CD1 
1836 C CD2 . TYR A 214 ? 0.6521 0.5055 0.4377 -0.0087 -0.0302 -0.0503 732 TYR A CD2 
1837 C CE1 . TYR A 214 ? 0.6366 0.4765 0.4660 -0.0150 -0.0089 -0.0427 732 TYR A CE1 
1838 C CE2 . TYR A 214 ? 0.6559 0.5094 0.4743 -0.0144 -0.0288 -0.0666 732 TYR A CE2 
1839 C CZ  . TYR A 214 ? 0.6739 0.5143 0.5126 -0.0173 -0.0158 -0.0604 732 TYR A CZ  
1840 O OH  . TYR A 214 ? 0.7032 0.5326 0.5720 -0.0210 -0.0069 -0.0733 732 TYR A OH  
1841 N N   . ILE A 215 ? 0.6509 0.4825 0.3994 -0.0042 -0.0311 -0.0086 733 ILE A N   
1842 C CA  . ILE A 215 ? 0.6365 0.4771 0.4008 -0.0023 -0.0443 -0.0139 733 ILE A CA  
1843 C C   . ILE A 215 ? 0.6516 0.4807 0.4263 -0.0096 -0.0403 0.0003  733 ILE A C   
1844 O O   . ILE A 215 ? 0.6195 0.4546 0.4222 -0.0160 -0.0454 -0.0028 733 ILE A O   
1845 C CB  . ILE A 215 ? 0.6615 0.5160 0.3981 0.0169  -0.0552 -0.0190 733 ILE A CB  
1846 C CG1 . ILE A 215 ? 0.6327 0.5133 0.3701 0.0222  -0.0631 -0.0433 733 ILE A CG1 
1847 C CG2 . ILE A 215 ? 0.6768 0.5429 0.4274 0.0202  -0.0669 -0.0219 733 ILE A CG2 
1848 C CD1 . ILE A 215 ? 0.6904 0.5930 0.3879 0.0479  -0.0714 -0.0467 733 ILE A CD1 
1849 N N   . TYR A 216 ? 0.6120 0.4232 0.3653 -0.0099 -0.0277 0.0145  734 TYR A N   
1850 C CA  . TYR A 216 ? 0.6098 0.4129 0.3752 -0.0192 -0.0214 0.0227  734 TYR A CA  
1851 C C   . TYR A 216 ? 0.6261 0.4453 0.4242 -0.0318 -0.0208 0.0185  734 TYR A C   
1852 O O   . TYR A 216 ? 0.6757 0.5020 0.4933 -0.0353 -0.0254 0.0199  734 TYR A O   
1853 C CB  . TYR A 216 ? 0.6456 0.4239 0.3871 -0.0218 -0.0004 0.0329  734 TYR A CB  
1854 C CG  . TYR A 216 ? 0.7136 0.4927 0.4762 -0.0397 0.0121  0.0314  734 TYR A CG  
1855 C CD1 . TYR A 216 ? 0.7805 0.5543 0.5516 -0.0415 0.0108  0.0343  734 TYR A CD1 
1856 C CD2 . TYR A 216 ? 0.7152 0.5079 0.4911 -0.0542 0.0249  0.0233  734 TYR A CD2 
1857 C CE1 . TYR A 216 ? 0.8089 0.5909 0.6008 -0.0582 0.0221  0.0276  734 TYR A CE1 
1858 C CE2 . TYR A 216 ? 0.7549 0.5621 0.5531 -0.0702 0.0352  0.0149  734 TYR A CE2 
1859 C CZ  . TYR A 216 ? 0.8053 0.6072 0.6113 -0.0726 0.0338  0.0163  734 TYR A CZ  
1860 O OH  . TYR A 216 ? 0.8348 0.6582 0.6644 -0.0889 0.0440  0.0030  734 TYR A OH  
1861 N N   . LEU A 217 ? 0.5932 0.4214 0.3958 -0.0351 -0.0146 0.0144  735 LEU A N   
1862 C CA  . LEU A 217 ? 0.5919 0.4405 0.4200 -0.0389 -0.0128 0.0130  735 LEU A CA  
1863 C C   . LEU A 217 ? 0.5618 0.4124 0.4090 -0.0330 -0.0210 0.0124  735 LEU A C   
1864 O O   . LEU A 217 ? 0.5256 0.3875 0.3899 -0.0316 -0.0197 0.0175  735 LEU A O   
1865 C CB  . LEU A 217 ? 0.5881 0.4490 0.4151 -0.0394 -0.0038 0.0082  735 LEU A CB  
1866 C CG  . LEU A 217 ? 0.5640 0.4282 0.3821 -0.0505 0.0112  0.0051  735 LEU A CG  
1867 C CD1 . LEU A 217 ? 0.5501 0.4285 0.3670 -0.0507 0.0201  -0.0020 735 LEU A CD1 
1868 C CD2 . LEU A 217 ? 0.5383 0.4255 0.3756 -0.0597 0.0155  0.0012  735 LEU A CD2 
1869 N N   . VAL A 218 ? 0.5644 0.4056 0.4094 -0.0293 -0.0265 0.0045  736 VAL A N   
1870 C CA  . VAL A 218 ? 0.5848 0.4229 0.4527 -0.0286 -0.0280 -0.0008 736 VAL A CA  
1871 C C   . VAL A 218 ? 0.6429 0.4820 0.5202 -0.0314 -0.0340 0.0024  736 VAL A C   
1872 O O   . VAL A 218 ? 0.6682 0.5057 0.5658 -0.0320 -0.0290 0.0065  736 VAL A O   
1873 C CB  . VAL A 218 ? 0.5893 0.4251 0.4577 -0.0280 -0.0310 -0.0193 736 VAL A CB  
1874 C CG1 . VAL A 218 ? 0.5914 0.4224 0.4896 -0.0328 -0.0272 -0.0311 736 VAL A CG1 
1875 C CG2 . VAL A 218 ? 0.5857 0.4197 0.4476 -0.0248 -0.0231 -0.0229 736 VAL A CG2 
1876 N N   . ILE A 219 ? 0.6313 0.4711 0.4917 -0.0305 -0.0422 0.0025  737 ILE A N   
1877 C CA  . ILE A 219 ? 0.6111 0.4534 0.4793 -0.0314 -0.0480 0.0050  737 ILE A CA  
1878 C C   . ILE A 219 ? 0.5793 0.4244 0.4572 -0.0354 -0.0417 0.0169  737 ILE A C   
1879 O O   . ILE A 219 ? 0.5154 0.3644 0.4115 -0.0368 -0.0416 0.0191  737 ILE A O   
1880 C CB  . ILE A 219 ? 0.6901 0.5298 0.5324 -0.0234 -0.0546 0.0065  737 ILE A CB  
1881 C CG1 . ILE A 219 ? 0.7491 0.6011 0.5822 -0.0138 -0.0645 -0.0084 737 ILE A CG1 
1882 C CG2 . ILE A 219 ? 0.6615 0.5025 0.5104 -0.0228 -0.0584 0.0113  737 ILE A CG2 
1883 C CD1 . ILE A 219 ? 0.7908 0.6613 0.6557 -0.0190 -0.0708 -0.0282 737 ILE A CD1 
1884 N N   . GLN A 220 ? 0.5917 0.4397 0.4587 -0.0377 -0.0349 0.0220  738 GLN A N   
1885 C CA  . GLN A 220 ? 0.6191 0.4833 0.4964 -0.0409 -0.0299 0.0268  738 GLN A CA  
1886 C C   . GLN A 220 ? 0.6442 0.5219 0.5380 -0.0336 -0.0266 0.0319  738 GLN A C   
1887 O O   . GLN A 220 ? 0.6686 0.5585 0.5725 -0.0306 -0.0256 0.0377  738 GLN A O   
1888 C CB  . GLN A 220 ? 0.6535 0.5268 0.5221 -0.0475 -0.0208 0.0230  738 GLN A CB  
1889 C CG  . GLN A 220 ? 0.6942 0.5438 0.5433 -0.0529 -0.0150 0.0221  738 GLN A CG  
1890 C CD  . GLN A 220 ? 0.7679 0.6074 0.6175 -0.0536 -0.0169 0.0249  738 GLN A CD  
1891 O OE1 . GLN A 220 ? 0.8195 0.6376 0.6533 -0.0458 -0.0204 0.0295  738 GLN A OE1 
1892 N NE2 . GLN A 220 ? 0.7482 0.6086 0.6152 -0.0599 -0.0148 0.0212  738 GLN A NE2 
1893 N N   . TRP A 221 ? 0.6492 0.5229 0.5432 -0.0278 -0.0223 0.0314  739 TRP A N   
1894 C CA  . TRP A 221 ? 0.6662 0.5441 0.5711 -0.0152 -0.0134 0.0404  739 TRP A CA  
1895 C C   . TRP A 221 ? 0.6780 0.5373 0.5972 -0.0150 -0.0093 0.0442  739 TRP A C   
1896 O O   . TRP A 221 ? 0.6675 0.5299 0.5927 -0.0037 0.0007  0.0572  739 TRP A O   
1897 C CB  . TRP A 221 ? 0.6492 0.5186 0.5518 -0.0085 -0.0064 0.0381  739 TRP A CB  
1898 C CG  . TRP A 221 ? 0.7851 0.6474 0.6961 0.0088  0.0083  0.0505  739 TRP A CG  
1899 C CD1 . TRP A 221 ? 0.8516 0.7392 0.7585 0.0291  0.0153  0.0629  739 TRP A CD1 
1900 C CD2 . TRP A 221 ? 0.8263 0.6537 0.7506 0.0097  0.0219  0.0515  739 TRP A CD2 
1901 N NE1 . TRP A 221 ? 0.9451 0.8089 0.8561 0.0473  0.0337  0.0775  739 TRP A NE1 
1902 C CE2 . TRP A 221 ? 0.9292 0.7514 0.8530 0.0327  0.0406  0.0699  739 TRP A CE2 
1903 C CE3 . TRP A 221 ? 0.8561 0.6597 0.7941 -0.0060 0.0222  0.0360  739 TRP A CE3 
1904 C CZ2 . TRP A 221 ? 1.0047 0.7859 0.9406 0.0383  0.0648  0.0759  739 TRP A CZ2 
1905 C CZ3 . TRP A 221 ? 0.9253 0.6973 0.8816 -0.0052 0.0440  0.0353  739 TRP A CZ3 
1906 C CH2 . TRP A 221 ? 1.0027 0.7574 0.9575 0.0158  0.0676  0.0565  739 TRP A CH2 
1907 N N   . ARG A 222 ? 0.6714 0.5150 0.5957 -0.0256 -0.0152 0.0321  740 ARG A N   
1908 C CA  . ARG A 222 ? 0.6497 0.4793 0.5942 -0.0294 -0.0082 0.0290  740 ARG A CA  
1909 C C   . ARG A 222 ? 0.6353 0.4754 0.5843 -0.0309 -0.0120 0.0358  740 ARG A C   
1910 O O   . ARG A 222 ? 0.6458 0.4780 0.6089 -0.0287 0.0007  0.0430  740 ARG A O   
1911 C CB  . ARG A 222 ? 0.5975 0.4220 0.5505 -0.0397 -0.0145 0.0063  740 ARG A CB  
1912 C CG  . ARG A 222 ? 0.6083 0.4281 0.5890 -0.0489 -0.0075 -0.0061 740 ARG A CG  
1913 C CD  . ARG A 222 ? 0.6349 0.4281 0.6338 -0.0474 0.0199  0.0021  740 ARG A CD  
1914 N NE  . ARG A 222 ? 0.6098 0.3951 0.6399 -0.0607 0.0332  -0.0131 740 ARG A NE  
1915 C CZ  . ARG A 222 ? 0.6052 0.3932 0.6439 -0.0620 0.0374  -0.0041 740 ARG A CZ  
1916 N NH1 . ARG A 222 ? 0.5680 0.3682 0.5858 -0.0501 0.0279  0.0191  740 ARG A NH1 
1917 N NH2 . ARG A 222 ? 0.5838 0.3659 0.6548 -0.0768 0.0527  -0.0217 740 ARG A NH2 
1918 N N   . PHE A 223 ? 0.6639 0.5182 0.6003 -0.0340 -0.0256 0.0343  741 PHE A N   
1919 C CA  . PHE A 223 ? 0.6775 0.5397 0.6194 -0.0369 -0.0301 0.0359  741 PHE A CA  
1920 C C   . PHE A 223 ? 0.6973 0.5783 0.6305 -0.0343 -0.0309 0.0438  741 PHE A C   
1921 O O   . PHE A 223 ? 0.6910 0.5803 0.6309 -0.0348 -0.0312 0.0464  741 PHE A O   
1922 C CB  . PHE A 223 ? 0.5710 0.4322 0.5087 -0.0413 -0.0430 0.0236  741 PHE A CB  
1923 C CG  . PHE A 223 ? 0.6041 0.4636 0.5573 -0.0448 -0.0447 0.0075  741 PHE A CG  
1924 C CD1 . PHE A 223 ? 0.5670 0.4265 0.5474 -0.0508 -0.0360 0.0017  741 PHE A CD1 
1925 C CD2 . PHE A 223 ? 0.6073 0.4691 0.5494 -0.0427 -0.0528 -0.0051 741 PHE A CD2 
1926 C CE1 . PHE A 223 ? 0.5913 0.4558 0.5933 -0.0585 -0.0346 -0.0215 741 PHE A CE1 
1927 C CE2 . PHE A 223 ? 0.6579 0.5301 0.6180 -0.0468 -0.0550 -0.0275 741 PHE A CE2 
1928 C CZ  . PHE A 223 ? 0.6106 0.4856 0.6036 -0.0566 -0.0456 -0.0384 741 PHE A CZ  
1929 N N   . VAL A 224 ? 0.7046 0.5973 0.6262 -0.0330 -0.0300 0.0436  742 VAL A N   
1930 C CA  . VAL A 224 ? 0.7524 0.6681 0.6701 -0.0365 -0.0301 0.0402  742 VAL A CA  
1931 C C   . VAL A 224 ? 0.7817 0.7329 0.7005 -0.0271 -0.0248 0.0423  742 VAL A C   
1932 O O   . VAL A 224 ? 0.8376 0.8201 0.7609 -0.0218 -0.0238 0.0426  742 VAL A O   
1933 C CB  . VAL A 224 ? 0.7531 0.6555 0.6582 -0.0468 -0.0304 0.0310  742 VAL A CB  
1934 C CG1 . VAL A 224 ? 0.7577 0.6825 0.6653 -0.0554 -0.0237 0.0212  742 VAL A CG1 
1935 C CG2 . VAL A 224 ? 0.7312 0.6071 0.6301 -0.0475 -0.0362 0.0312  742 VAL A CG2 
1936 N N   . ASN A 225 ? 0.7631 0.7165 0.6773 -0.0221 -0.0218 0.0423  743 ASN A N   
1937 C CA  . ASN A 225 ? 0.7580 0.7561 0.6724 -0.0139 -0.0186 0.0375  743 ASN A CA  
1938 C C   . ASN A 225 ? 0.7200 0.7526 0.6362 0.0080  -0.0159 0.0488  743 ASN A C   
1939 O O   . ASN A 225 ? 0.7169 0.8026 0.6360 0.0126  -0.0174 0.0387  743 ASN A O   
1940 C CB  . ASN A 225 ? 0.7570 0.7497 0.6664 -0.0088 -0.0153 0.0375  743 ASN A CB  
1941 C CG  . ASN A 225 ? 0.7789 0.7546 0.6825 -0.0274 -0.0151 0.0244  743 ASN A CG  
1942 O OD1 . ASN A 225 ? 0.8123 0.7873 0.7159 -0.0428 -0.0137 0.0142  743 ASN A OD1 
1943 N ND2 . ASN A 225 ? 0.8025 0.7614 0.6996 -0.0248 -0.0131 0.0253  743 ASN A ND2 
1944 N N   . ARG A 226 ? 0.7060 0.7114 0.6205 0.0225  -0.0092 0.0681  744 ARG A N   
1945 C CA  . ARG A 226 ? 0.7092 0.7407 0.6183 0.0500  -0.0010 0.0851  744 ARG A CA  
1946 C C   . ARG A 226 ? 0.6907 0.7320 0.6025 0.0487  -0.0020 0.0881  744 ARG A C   
1947 O O   . ARG A 226 ? 0.7093 0.7713 0.6127 0.0741  0.0066  0.1049  744 ARG A O   
1948 C CB  . ARG A 226 ? 0.7538 0.7432 0.6590 0.0677  0.0158  0.1066  744 ARG A CB  
1949 C CG  . ARG A 226 ? 0.8115 0.8002 0.7114 0.0789  0.0200  0.1071  744 ARG A CG  
1950 C CD  . ARG A 226 ? 0.8825 0.8107 0.7855 0.0825  0.0383  0.1191  744 ARG A CD  
1951 N NE  . ARG A 226 ? 0.9254 0.8142 0.8427 0.0518  0.0334  0.1041  744 ARG A NE  
1952 C CZ  . ARG A 226 ? 0.9603 0.8013 0.8892 0.0454  0.0487  0.1041  744 ARG A CZ  
1953 N NH1 . ARG A 226 ? 1.0044 0.8177 0.9314 0.0661  0.0746  0.1214  744 ARG A NH1 
1954 N NH2 . ARG A 226 ? 0.9204 0.7431 0.8632 0.0197  0.0404  0.0851  744 ARG A NH2 
1955 N N   . ILE A 227 ? 0.6502 0.6775 0.5707 0.0237  -0.0106 0.0741  745 ILE A N   
1956 C CA  . ILE A 227 ? 0.6821 0.7158 0.6067 0.0220  -0.0109 0.0761  745 ILE A CA  
1957 C C   . ILE A 227 ? 0.6483 0.7095 0.5784 0.0044  -0.0202 0.0534  745 ILE A C   
1958 O O   . ILE A 227 ? 0.6464 0.7048 0.5817 -0.0028 -0.0218 0.0502  745 ILE A O   
1959 C CB  . ILE A 227 ? 0.6165 0.5992 0.5499 0.0114  -0.0072 0.0825  745 ILE A CB  
1960 C CG1 . ILE A 227 ? 0.6566 0.6123 0.5948 -0.0104 -0.0174 0.0670  745 ILE A CG1 
1961 C CG2 . ILE A 227 ? 0.6289 0.5803 0.5624 0.0249  0.0094  0.1005  745 ILE A CG2 
1962 C CD1 . ILE A 227 ? 0.6941 0.6308 0.6422 -0.0217 -0.0213 0.0624  745 ILE A CD1 
1963 N N   . GLN A 228 ? 0.6075 0.6937 0.5384 -0.0035 -0.0228 0.0357  746 GLN A N   
1964 C CA  . GLN A 228 ? 0.6185 0.7189 0.5578 -0.0248 -0.0239 0.0110  746 GLN A CA  
1965 C C   . GLN A 228 ? 0.5327 0.6876 0.4781 -0.0195 -0.0244 -0.0003 746 GLN A C   
1966 O O   . GLN A 228 ? 0.5645 0.7143 0.5178 -0.0352 -0.0232 -0.0143 746 GLN A O   
1967 C CB  . GLN A 228 ? 0.7787 0.8944 0.7212 -0.0369 -0.0204 -0.0081 746 GLN A CB  
1968 C CG  . GLN A 228 ? 0.9765 1.0717 0.9258 -0.0639 -0.0126 -0.0293 746 GLN A CG  
1969 C CD  . GLN A 228 ? 1.1173 1.1560 1.0561 -0.0739 -0.0079 -0.0234 746 GLN A CD  
1970 O OE1 . GLN A 228 ? 1.1794 1.2207 1.1140 -0.0707 -0.0071 -0.0216 746 GLN A OE1 
1971 N NE2 . GLN A 228 ? 1.1319 1.1220 1.0640 -0.0824 -0.0042 -0.0197 746 GLN A NE2 
1972 N N   . LYS A 229 ? 0.4699 0.6793 0.4097 0.0059  -0.0252 0.0055  747 LYS A N   
1973 C CA  . LYS A 229 ? 0.5558 0.8289 0.4987 0.0150  -0.0268 -0.0076 747 LYS A CA  
1974 C C   . LYS A 229 ? 0.5392 0.7868 0.4769 0.0219  -0.0253 0.0115  747 LYS A C   
1975 O O   . LYS A 229 ? 0.5223 0.7938 0.4676 0.0135  -0.0263 -0.0048 747 LYS A O   
1976 C CB  . LYS A 229 ? 0.6520 1.0008 0.5857 0.0475  -0.0285 -0.0063 747 LYS A CB  
1977 C CG  . LYS A 229 ? 0.7781 1.1741 0.7236 0.0388  -0.0304 -0.0352 747 LYS A CG  
1978 C CD  . LYS A 229 ? 0.9202 1.3397 0.8902 0.0031  -0.0280 -0.0783 747 LYS A CD  
1979 C CE  . LYS A 229 ? 1.0187 1.3823 0.9988 -0.0291 -0.0202 -0.0894 747 LYS A CE  
1980 N NZ  . LYS A 229 ? 1.0507 1.3891 1.0468 -0.0626 -0.0104 -0.1145 747 LYS A NZ  
1981 N N   . GLN A 230 ? 0.4961 0.6958 0.4237 0.0354  -0.0202 0.0429  748 GLN A N   
1982 C CA  . GLN A 230 ? 0.4188 0.5910 0.3457 0.0383  -0.0151 0.0590  748 GLN A CA  
1983 C C   . GLN A 230 ? 0.4576 0.5935 0.3989 0.0095  -0.0200 0.0442  748 GLN A C   
1984 O O   . GLN A 230 ? 0.5133 0.6594 0.4592 0.0064  -0.0199 0.0391  748 GLN A O   
1985 C CB  . GLN A 230 ? 0.4317 0.5548 0.3516 0.0522  -0.0030 0.0894  748 GLN A CB  
1986 C CG  . GLN A 230 ? 0.4384 0.5864 0.3393 0.0872  0.0073  0.1102  748 GLN A CG  
1987 C CD  . GLN A 230 ? 0.4691 0.6089 0.3687 0.0878  0.0050  0.1077  748 GLN A CD  
1988 O OE1 . GLN A 230 ? 0.4611 0.6142 0.3702 0.0672  -0.0072 0.0833  748 GLN A OE1 
1989 N NE2 . GLN A 230 ? 0.5185 0.6324 0.4062 0.1116  0.0206  0.1333  748 GLN A NE2 
1990 N N   . MET A 231 ? 0.4506 0.5453 0.3963 -0.0082 -0.0234 0.0381  749 MET A N   
1991 C CA  . MET A 231 ? 0.4513 0.5112 0.4048 -0.0277 -0.0265 0.0278  749 MET A CA  
1992 C C   . MET A 231 ? 0.4922 0.5788 0.4520 -0.0404 -0.0254 0.0028  749 MET A C   
1993 O O   . MET A 231 ? 0.4981 0.5728 0.4636 -0.0475 -0.0246 -0.0032 749 MET A O   
1994 C CB  . MET A 231 ? 0.4699 0.4856 0.4204 -0.0372 -0.0289 0.0287  749 MET A CB  
1995 C CG  . MET A 231 ? 0.5254 0.5038 0.4783 -0.0462 -0.0320 0.0260  749 MET A CG  
1996 S SD  . MET A 231 ? 0.6138 0.5857 0.5777 -0.0401 -0.0331 0.0365  749 MET A SD  
1997 C CE  . MET A 231 ? 0.6606 0.6024 0.6248 -0.0457 -0.0395 0.0285  749 MET A CE  
1998 N N   . ALA A 232 ? 0.4070 0.5314 0.3688 -0.0445 -0.0231 -0.0152 750 ALA A N   
1999 C CA  . ALA A 232 ? 0.4118 0.5665 0.3857 -0.0606 -0.0171 -0.0465 750 ALA A CA  
2000 C C   . ALA A 232 ? 0.4320 0.6307 0.4102 -0.0518 -0.0187 -0.0524 750 ALA A C   
2001 O O   . ALA A 232 ? 0.4513 0.6471 0.4396 -0.0657 -0.0132 -0.0713 750 ALA A O   
2002 C CB  . ALA A 232 ? 0.3684 0.5707 0.3494 -0.0667 -0.0133 -0.0702 750 ALA A CB  
2003 N N   . ALA A 233 ? 0.4398 0.6769 0.4078 -0.0264 -0.0235 -0.0352 751 ALA A N   
2004 C CA  . ALA A 233 ? 0.4106 0.6910 0.3773 -0.0135 -0.0237 -0.0369 751 ALA A CA  
2005 C C   . ALA A 233 ? 0.4553 0.6858 0.4239 -0.0181 -0.0221 -0.0225 751 ALA A C   
2006 O O   . ALA A 233 ? 0.4493 0.6999 0.4244 -0.0219 -0.0204 -0.0364 751 ALA A O   
2007 C CB  . ALA A 233 ? 0.3637 0.6896 0.3122 0.0212  -0.0246 -0.0149 751 ALA A CB  
2008 N N   . PHE A 234 ? 0.4339 0.6048 0.3990 -0.0180 -0.0223 0.0016  752 PHE A N   
2009 C CA  . PHE A 234 ? 0.4443 0.5755 0.4156 -0.0232 -0.0215 0.0102  752 PHE A CA  
2010 C C   . PHE A 234 ? 0.4568 0.5668 0.4378 -0.0421 -0.0217 -0.0112 752 PHE A C   
2011 O O   . PHE A 234 ? 0.3970 0.5098 0.3847 -0.0440 -0.0199 -0.0177 752 PHE A O   
2012 C CB  . PHE A 234 ? 0.4406 0.5229 0.4113 -0.0215 -0.0214 0.0313  752 PHE A CB  
2013 C CG  . PHE A 234 ? 0.4537 0.5029 0.4354 -0.0286 -0.0225 0.0329  752 PHE A CG  
2014 C CD1 . PHE A 234 ? 0.4624 0.4810 0.4472 -0.0394 -0.0284 0.0228  752 PHE A CD1 
2015 C CD2 . PHE A 234 ? 0.4757 0.5270 0.4638 -0.0218 -0.0155 0.0447  752 PHE A CD2 
2016 C CE1 . PHE A 234 ? 0.4761 0.4756 0.4704 -0.0405 -0.0312 0.0226  752 PHE A CE1 
2017 C CE2 . PHE A 234 ? 0.4812 0.5122 0.4839 -0.0286 -0.0169 0.0415  752 PHE A CE2 
2018 C CZ  . PHE A 234 ? 0.4828 0.4922 0.4888 -0.0366 -0.0267 0.0296  752 PHE A CZ  
2019 N N   . LYS A 235 ? 0.4742 0.5592 0.4544 -0.0543 -0.0206 -0.0208 753 LYS A N   
2020 C CA  . LYS A 235 ? 0.5414 0.5950 0.5261 -0.0686 -0.0138 -0.0369 753 LYS A CA  
2021 C C   . LYS A 235 ? 0.5419 0.6332 0.5381 -0.0781 -0.0051 -0.0652 753 LYS A C   
2022 O O   . LYS A 235 ? 0.6089 0.6783 0.6109 -0.0844 0.0025  -0.0753 753 LYS A O   
2023 C CB  . LYS A 235 ? 0.6307 0.6507 0.6088 -0.0781 -0.0083 -0.0400 753 LYS A CB  
2024 C CG  . LYS A 235 ? 0.7101 0.6955 0.6769 -0.0693 -0.0169 -0.0170 753 LYS A CG  
2025 C CD  . LYS A 235 ? 0.7983 0.7606 0.7560 -0.0766 -0.0109 -0.0199 753 LYS A CD  
2026 C CE  . LYS A 235 ? 0.8790 0.7964 0.8301 -0.0840 0.0038  -0.0271 753 LYS A CE  
2027 N NZ  . LYS A 235 ? 0.9258 0.8153 0.8647 -0.0898 0.0137  -0.0266 753 LYS A NZ  
2028 N N   . GLU A 236 ? 0.4604 0.6130 0.4606 -0.0774 -0.0055 -0.0807 754 GLU A N   
2029 C CA  . GLU A 236 ? 0.5038 0.7071 0.5181 -0.0868 0.0020  -0.1149 754 GLU A CA  
2030 C C   . GLU A 236 ? 0.4892 0.7044 0.5044 -0.0772 -0.0007 -0.1103 754 GLU A C   
2031 O O   . GLU A 236 ? 0.4472 0.6608 0.4745 -0.0894 0.0090  -0.1340 754 GLU A O   
2032 C CB  . GLU A 236 ? 0.5403 0.8247 0.5572 -0.0805 -0.0021 -0.1323 754 GLU A CB  
2033 C CG  . GLU A 236 ? 0.6790 1.0231 0.7174 -0.0979 0.0080  -0.1815 754 GLU A CG  
2034 C CD  . GLU A 236 ? 0.8470 1.2859 0.8891 -0.0883 0.0016  -0.2030 754 GLU A CD  
2035 O OE1 . GLU A 236 ? 0.9048 1.4079 0.9349 -0.0610 -0.0095 -0.1949 754 GLU A OE1 
2036 O OE2 . GLU A 236 ? 0.9280 1.3799 0.9840 -0.1056 0.0090  -0.2279 754 GLU A OE2 
2037 N N   . GLY A 237 ? 0.4300 0.6533 0.4331 -0.0561 -0.0100 -0.0804 755 GLY A N   
2038 C CA  . GLY A 237 ? 0.4044 0.6364 0.4084 -0.0473 -0.0100 -0.0741 755 GLY A CA  
2039 C C   . GLY A 237 ? 0.4369 0.6079 0.4474 -0.0553 -0.0076 -0.0687 755 GLY A C   
2040 O O   . GLY A 237 ? 0.4241 0.6008 0.4425 -0.0573 -0.0033 -0.0805 755 GLY A O   
2041 N N   . PHE A 238 ? 0.4089 0.5265 0.4154 -0.0570 -0.0106 -0.0520 756 PHE A N   
2042 C CA  . PHE A 238 ? 0.4128 0.4815 0.4225 -0.0578 -0.0101 -0.0466 756 PHE A CA  
2043 C C   . PHE A 238 ? 0.4237 0.4708 0.4382 -0.0691 0.0024  -0.0698 756 PHE A C   
2044 O O   . PHE A 238 ? 0.4351 0.4689 0.4551 -0.0663 0.0067  -0.0742 756 PHE A O   
2045 C CB  . PHE A 238 ? 0.4666 0.4943 0.4688 -0.0544 -0.0167 -0.0279 756 PHE A CB  
2046 C CG  . PHE A 238 ? 0.5077 0.5003 0.5114 -0.0479 -0.0196 -0.0217 756 PHE A CG  
2047 C CD1 . PHE A 238 ? 0.4854 0.4874 0.4988 -0.0402 -0.0260 -0.0120 756 PHE A CD1 
2048 C CD2 . PHE A 238 ? 0.5272 0.4799 0.5224 -0.0473 -0.0133 -0.0262 756 PHE A CD2 
2049 C CE1 . PHE A 238 ? 0.5320 0.5158 0.5495 -0.0318 -0.0306 -0.0109 756 PHE A CE1 
2050 C CE2 . PHE A 238 ? 0.5318 0.4605 0.5244 -0.0335 -0.0170 -0.0194 756 PHE A CE2 
2051 C CZ  . PHE A 238 ? 0.5083 0.4584 0.5134 -0.0256 -0.0279 -0.0137 756 PHE A CZ  
2052 N N   . PHE A 239 ? 0.4878 0.5293 0.5016 -0.0823 0.0121  -0.0858 757 PHE A N   
2053 C CA  . PHE A 239 ? 0.5784 0.5876 0.5979 -0.0956 0.0327  -0.1083 757 PHE A CA  
2054 C C   . PHE A 239 ? 0.6626 0.7130 0.6992 -0.1054 0.0425  -0.1399 757 PHE A C   
2055 O O   . PHE A 239 ? 0.7827 0.8015 0.8274 -0.1162 0.0636  -0.1602 757 PHE A O   
2056 C CB  . PHE A 239 ? 0.5307 0.5205 0.5479 -0.1102 0.0456  -0.1185 757 PHE A CB  
2057 C CG  . PHE A 239 ? 0.6098 0.5563 0.6081 -0.0999 0.0381  -0.0896 757 PHE A CG  
2058 C CD1 . PHE A 239 ? 0.6455 0.5569 0.6317 -0.0812 0.0287  -0.0646 757 PHE A CD1 
2059 C CD2 . PHE A 239 ? 0.5928 0.5416 0.5870 -0.1079 0.0400  -0.0907 757 PHE A CD2 
2060 C CE1 . PHE A 239 ? 0.6658 0.5476 0.6353 -0.0707 0.0208  -0.0430 757 PHE A CE1 
2061 C CE2 . PHE A 239 ? 0.6342 0.5464 0.6103 -0.0978 0.0331  -0.0661 757 PHE A CE2 
2062 C CZ  . PHE A 239 ? 0.6820 0.5620 0.6453 -0.0791 0.0232  -0.0431 757 PHE A CZ  
2063 N N   . GLU A 240 ? 0.6228 0.7415 0.6635 -0.0996 0.0302  -0.1442 758 GLU A N   
2064 C CA  . GLU A 240 ? 0.6369 0.8015 0.6912 -0.1041 0.0365  -0.1728 758 GLU A CA  
2065 C C   . GLU A 240 ? 0.6524 0.7889 0.7072 -0.0942 0.0370  -0.1617 758 GLU A C   
2066 O O   . GLU A 240 ? 0.6376 0.7946 0.7046 -0.0999 0.0469  -0.1876 758 GLU A O   
2067 C CB  . GLU A 240 ? 0.6120 0.8614 0.6633 -0.0930 0.0235  -0.1757 758 GLU A CB  
2068 C CG  . GLU A 240 ? 0.6427 0.9443 0.6993 -0.1018 0.0245  -0.2004 758 GLU A CG  
2069 C CD  . GLU A 240 ? 0.6787 1.0698 0.7260 -0.0810 0.0114  -0.1998 758 GLU A CD  
2070 O OE1 . GLU A 240 ? 0.6824 1.0714 0.7112 -0.0573 0.0014  -0.1621 758 GLU A OE1 
2071 O OE2 . GLU A 240 ? 0.7132 1.1789 0.7719 -0.0870 0.0136  -0.2381 758 GLU A OE2 
2072 N N   . LEU A 241 ? 0.5923 0.6882 0.6365 -0.0798 0.0268  -0.1280 759 LEU A N   
2073 C CA  . LEU A 241 ? 0.5839 0.6589 0.6308 -0.0684 0.0257  -0.1179 759 LEU A CA  
2074 C C   . LEU A 241 ? 0.5846 0.5909 0.6257 -0.0633 0.0338  -0.1098 759 LEU A C   
2075 O O   . LEU A 241 ? 0.6548 0.6412 0.7006 -0.0570 0.0428  -0.1160 759 LEU A O   
2076 C CB  . LEU A 241 ? 0.5415 0.6350 0.5849 -0.0540 0.0096  -0.0902 759 LEU A CB  
2077 C CG  . LEU A 241 ? 0.5098 0.6619 0.5553 -0.0481 0.0069  -0.0899 759 LEU A CG  
2078 C CD1 . LEU A 241 ? 0.5095 0.6732 0.5656 -0.0459 0.0132  -0.1037 759 LEU A CD1 
2079 C CD2 . LEU A 241 ? 0.4837 0.6880 0.5241 -0.0520 0.0080  -0.1050 759 LEU A CD2 
2080 N N   . ILE A 242 ? 0.5564 0.5280 0.5850 -0.0620 0.0317  -0.0949 760 ILE A N   
2081 C CA  . ILE A 242 ? 0.6014 0.5108 0.6167 -0.0500 0.0396  -0.0823 760 ILE A CA  
2082 C C   . ILE A 242 ? 0.6444 0.5177 0.6518 -0.0637 0.0592  -0.0913 760 ILE A C   
2083 O O   . ILE A 242 ? 0.6850 0.5735 0.6893 -0.0726 0.0523  -0.0886 760 ILE A O   
2084 C CB  . ILE A 242 ? 0.5921 0.4965 0.5976 -0.0321 0.0193  -0.0553 760 ILE A CB  
2085 C CG1 . ILE A 242 ? 0.5637 0.5115 0.5837 -0.0259 0.0034  -0.0507 760 ILE A CG1 
2086 C CG2 . ILE A 242 ? 0.6729 0.5258 0.6611 -0.0108 0.0257  -0.0428 760 ILE A CG2 
2087 C CD1 . ILE A 242 ? 0.6462 0.5912 0.6738 -0.0130 0.0072  -0.0556 760 ILE A CD1 
2088 N N   . PRO A 243 ? 0.7188 0.5415 0.7234 -0.0659 0.0873  -0.1024 761 PRO A N   
2089 C CA  . PRO A 243 ? 0.7085 0.4886 0.7062 -0.0804 0.1126  -0.1101 761 PRO A CA  
2090 C C   . PRO A 243 ? 0.7332 0.4841 0.7058 -0.0650 0.1024  -0.0797 761 PRO A C   
2091 O O   . PRO A 243 ? 0.7660 0.4979 0.7209 -0.0374 0.0900  -0.0542 761 PRO A O   
2092 C CB  . PRO A 243 ? 0.7631 0.4797 0.7585 -0.0777 0.1490  -0.1196 761 PRO A CB  
2093 C CG  . PRO A 243 ? 0.7652 0.5136 0.7763 -0.0724 0.1417  -0.1312 761 PRO A CG  
2094 C CD  . PRO A 243 ? 0.7281 0.5268 0.7365 -0.0555 0.1020  -0.1090 761 PRO A CD  
2095 N N   . GLN A 244 ? 0.7738 0.5286 0.7462 -0.0825 0.1073  -0.0858 762 GLN A N   
2096 C CA  . GLN A 244 ? 0.8089 0.5501 0.7599 -0.0700 0.0934  -0.0600 762 GLN A CA  
2097 C C   . GLN A 244 ? 0.9588 0.6258 0.8795 -0.0497 0.1143  -0.0390 762 GLN A C   
2098 O O   . GLN A 244 ? 1.0522 0.7116 0.9508 -0.0291 0.0983  -0.0146 762 GLN A O   
2099 C CB  . GLN A 244 ? 0.7557 0.5272 0.7156 -0.0927 0.0925  -0.0730 762 GLN A CB  
2100 C CG  . GLN A 244 ? 0.9479 0.6746 0.9028 -0.1088 0.1258  -0.0836 762 GLN A CG  
2101 C CD  . GLN A 244 ? 1.0370 0.7928 0.9932 -0.1205 0.1165  -0.0853 762 GLN A CD  
2102 O OE1 . GLN A 244 ? 1.0709 0.7981 1.0041 -0.1080 0.1122  -0.0620 762 GLN A OE1 
2103 N NE2 . GLN A 244 ? 1.0379 0.8570 1.0200 -0.1416 0.1125  -0.1139 762 GLN A NE2 
2104 N N   . ASP A 245 ? 1.0169 0.6291 0.9344 -0.0524 0.1518  -0.0478 763 ASP A N   
2105 C CA  . ASP A 245 ? 1.1316 0.6694 1.0131 -0.0228 0.1743  -0.0209 763 ASP A CA  
2106 C C   . ASP A 245 ? 1.0740 0.6123 0.9410 0.0159  0.1569  -0.0003 763 ASP A C   
2107 O O   . ASP A 245 ? 1.1752 0.6782 1.0071 0.0520  0.1592  0.0281  763 ASP A O   
2108 C CB  . ASP A 245 ? 1.2850 0.7517 1.1661 -0.0370 0.2290  -0.0350 763 ASP A CB  
2109 C CG  . ASP A 245 ? 1.4297 0.9153 1.3467 -0.0625 0.2431  -0.0715 763 ASP A CG  
2110 O OD1 . ASP A 245 ? 1.5064 0.9803 1.4215 -0.0423 0.2439  -0.0668 763 ASP A OD1 
2111 O OD2 . ASP A 245 ? 1.4718 0.9893 1.4197 -0.1014 0.2534  -0.1075 763 ASP A OD2 
2112 N N   . LEU A 246 ? 0.8871 0.4709 0.7797 0.0114  0.1396  -0.0147 764 LEU A N   
2113 C CA  . LEU A 246 ? 0.8336 0.4308 0.7184 0.0462  0.1204  0.0008  764 LEU A CA  
2114 C C   . LEU A 246 ? 0.8120 0.4585 0.6921 0.0610  0.0807  0.0156  764 LEU A C   
2115 O O   . LEU A 246 ? 0.8027 0.4486 0.6628 0.0975  0.0695  0.0336  764 LEU A O   
2116 C CB  . LEU A 246 ? 0.7930 0.4265 0.7084 0.0346  0.1156  -0.0207 764 LEU A CB  
2117 C CG  . LEU A 246 ? 0.9228 0.5071 0.8327 0.0513  0.1459  -0.0231 764 LEU A CG  
2118 C CD1 . LEU A 246 ? 0.9758 0.4876 0.8782 0.0352  0.1942  -0.0325 764 LEU A CD1 
2119 C CD2 . LEU A 246 ? 0.9268 0.5564 0.8682 0.0387  0.1378  -0.0464 764 LEU A CD2 
2120 N N   . ILE A 247 ? 0.7615 0.4540 0.6607 0.0346  0.0608  0.0060  765 ILE A N   
2121 C CA  . ILE A 247 ? 0.7714 0.5068 0.6715 0.0437  0.0285  0.0155  765 ILE A CA  
2122 C C   . ILE A 247 ? 0.8240 0.5322 0.6918 0.0646  0.0285  0.0342  765 ILE A C   
2123 O O   . ILE A 247 ? 0.8528 0.5931 0.7170 0.0819  0.0043  0.0406  765 ILE A O   
2124 C CB  . ILE A 247 ? 0.7020 0.4831 0.6267 0.0136  0.0140  0.0038  765 ILE A CB  
2125 C CG1 . ILE A 247 ? 0.6765 0.5054 0.6154 0.0199  -0.0139 0.0069  765 ILE A CG1 
2126 C CG2 . ILE A 247 ? 0.6953 0.4601 0.6092 -0.0010 0.0213  0.0054  765 ILE A CG2 
2127 C CD1 . ILE A 247 ? 0.6720 0.5274 0.6285 0.0293  -0.0208 0.0013  765 ILE A CD1 
2128 N N   . LYS A 248 ? 0.8572 0.5086 0.7021 0.0634  0.0576  0.0407  766 LYS A N   
2129 C CA  . LYS A 248 ? 0.9387 0.5629 0.7493 0.0826  0.0611  0.0597  766 LYS A CA  
2130 C C   . LYS A 248 ? 0.9753 0.5801 0.7507 0.1319  0.0621  0.0814  766 LYS A C   
2131 O O   . LYS A 248 ? 1.0781 0.6658 0.8193 0.1554  0.0640  0.0990  766 LYS A O   
2132 C CB  . LYS A 248 ? 1.0563 0.6245 0.8553 0.0630  0.0975  0.0588  766 LYS A CB  
2133 C CG  . LYS A 248 ? 1.0762 0.6758 0.8998 0.0242  0.0904  0.0412  766 LYS A CG  
2134 C CD  . LYS A 248 ? 1.1609 0.7107 0.9746 0.0058  0.1274  0.0375  766 LYS A CD  
2135 C CE  . LYS A 248 ? 1.1550 0.7468 0.9956 -0.0301 0.1193  0.0167  766 LYS A CE  
2136 N NZ  . LYS A 248 ? 1.1922 0.7429 1.0269 -0.0495 0.1556  0.0094  766 LYS A NZ  
2137 N N   . ILE A 249 ? 0.9020 0.5130 0.6826 0.1521  0.0610  0.0808  767 ILE A N   
2138 C CA  . ILE A 249 ? 1.0002 0.6097 0.7475 0.2057  0.0565  0.1004  767 ILE A CA  
2139 C C   . ILE A 249 ? 0.9496 0.6367 0.7055 0.2195  0.0144  0.0947  767 ILE A C   
2140 O O   . ILE A 249 ? 1.0118 0.7134 0.7366 0.2649  0.0055  0.1082  767 ILE A O   
2141 C CB  . ILE A 249 ? 1.0484 0.6440 0.7991 0.2265  0.0690  0.1005  767 ILE A CB  
2142 C CG1 . ILE A 249 ? 0.9850 0.6594 0.7745 0.2218  0.0337  0.0813  767 ILE A CG1 
2143 C CG2 . ILE A 249 ? 1.1374 0.6729 0.8999 0.1959  0.1076  0.0912  767 ILE A CG2 
2144 C CD1 . ILE A 249 ? 1.0030 0.6773 0.7896 0.2562  0.0392  0.0843  767 ILE A CD1 
2145 N N   . PHE A 250 ? 0.8775 0.6162 0.6744 0.1827  -0.0091 0.0737  768 PHE A N   
2146 C CA  . PHE A 250 ? 0.8109 0.6199 0.6247 0.1870  -0.0429 0.0618  768 PHE A CA  
2147 C C   . PHE A 250 ? 0.8282 0.6380 0.6321 0.1742  -0.0489 0.0633  768 PHE A C   
2148 O O   . PHE A 250 ? 0.8140 0.5844 0.6143 0.1478  -0.0322 0.0673  768 PHE A O   
2149 C CB  . PHE A 250 ? 0.7075 0.5648 0.5712 0.1555  -0.0583 0.0397  768 PHE A CB  
2150 C CG  . PHE A 250 ? 0.6968 0.5587 0.5745 0.1641  -0.0530 0.0353  768 PHE A CG  
2151 C CD1 . PHE A 250 ? 0.6475 0.5460 0.5230 0.2011  -0.0654 0.0330  768 PHE A CD1 
2152 C CD2 . PHE A 250 ? 0.6656 0.5024 0.5594 0.1366  -0.0363 0.0307  768 PHE A CD2 
2153 C CE1 . PHE A 250 ? 0.6552 0.5590 0.5443 0.2101  -0.0601 0.0285  768 PHE A CE1 
2154 C CE2 . PHE A 250 ? 0.6564 0.4984 0.5633 0.1443  -0.0308 0.0249  768 PHE A CE2 
2155 C CZ  . PHE A 250 ? 0.6703 0.5428 0.5748 0.1808  -0.0422 0.0250  768 PHE A CZ  
2156 N N   . ASP A 251 ? 0.8188 0.6800 0.6209 0.1927  -0.0727 0.0561  769 ASP A N   
2157 C CA  . ASP A 251 ? 0.8276 0.7011 0.6301 0.1761  -0.0817 0.0507  769 ASP A CA  
2158 C C   . ASP A 251 ? 0.7338 0.6496 0.5867 0.1377  -0.0964 0.0274  769 ASP A C   
2159 O O   . ASP A 251 ? 0.7373 0.6720 0.6214 0.1251  -0.0986 0.0172  769 ASP A O   
2160 C CB  . ASP A 251 ? 0.8673 0.7742 0.6399 0.2159  -0.0963 0.0522  769 ASP A CB  
2161 C CG  . ASP A 251 ? 0.8537 0.8408 0.6501 0.2356  -0.1225 0.0290  769 ASP A CG  
2162 O OD1 . ASP A 251 ? 0.7986 0.8187 0.6423 0.2089  -0.1309 0.0081  769 ASP A OD1 
2163 O OD2 . ASP A 251 ? 0.9056 0.9276 0.6727 0.2799  -0.1337 0.0303  769 ASP A OD2 
2164 N N   . GLU A 252 ? 0.6906 0.6179 0.5497 0.1206  -0.1032 0.0200  770 GLU A N   
2165 C CA  . GLU A 252 ? 0.6495 0.6024 0.5516 0.0857  -0.1089 0.0027  770 GLU A CA  
2166 C C   . GLU A 252 ? 0.5649 0.5764 0.5032 0.0872  -0.1234 -0.0210 770 GLU A C   
2167 O O   . GLU A 252 ? 0.5517 0.5730 0.5248 0.0635  -0.1194 -0.0295 770 GLU A O   
2168 C CB  . GLU A 252 ? 0.7163 0.6679 0.6158 0.0724  -0.1111 -0.0010 770 GLU A CB  
2169 C CG  . GLU A 252 ? 0.8565 0.8398 0.7380 0.0975  -0.1253 -0.0102 770 GLU A CG  
2170 C CD  . GLU A 252 ? 0.9981 0.9457 0.8263 0.1275  -0.1173 0.0130  770 GLU A CD  
2171 O OE1 . GLU A 252 ? 1.0458 0.9384 0.8563 0.1169  -0.0979 0.0322  770 GLU A OE1 
2172 O OE2 . GLU A 252 ? 1.0939 1.0712 0.8978 0.1629  -0.1282 0.0109  770 GLU A OE2 
2173 N N   . ASN A 253 ? 0.5618 0.6171 0.4923 0.1165  -0.1387 -0.0331 771 ASN A N   
2174 C CA  . ASN A 253 ? 0.5962 0.7189 0.5666 0.1167  -0.1522 -0.0632 771 ASN A CA  
2175 C C   . ASN A 253 ? 0.6329 0.7589 0.6149 0.1237  -0.1487 -0.0600 771 ASN A C   
2176 O O   . ASN A 253 ? 0.6187 0.7758 0.6445 0.1026  -0.1483 -0.0793 771 ASN A O   
2177 C CB  . ASN A 253 ? 0.7112 0.8935 0.6687 0.1513  -0.1714 -0.0809 771 ASN A CB  
2178 C CG  . ASN A 253 ? 0.8666 1.0450 0.8055 0.1496  -0.1746 -0.0829 771 ASN A CG  
2179 O OD1 . ASN A 253 ? 0.8855 1.0754 0.8569 0.1172  -0.1734 -0.1035 771 ASN A OD1 
2180 N ND2 . ASN A 253 ? 0.9561 1.1149 0.8410 0.1860  -0.1753 -0.0607 771 ASN A ND2 
2181 N N   . GLU A 254 ? 0.6082 0.7002 0.5518 0.1537  -0.1427 -0.0361 772 GLU A N   
2182 C CA  . GLU A 254 ? 0.5917 0.6814 0.5445 0.1613  -0.1370 -0.0327 772 GLU A CA  
2183 C C   . GLU A 254 ? 0.5639 0.6226 0.5416 0.1215  -0.1224 -0.0298 772 GLU A C   
2184 O O   . GLU A 254 ? 0.5431 0.6270 0.5524 0.1116  -0.1220 -0.0414 772 GLU A O   
2185 C CB  . GLU A 254 ? 0.7031 0.7482 0.6068 0.2008  -0.1262 -0.0060 772 GLU A CB  
2186 C CG  . GLU A 254 ? 0.8077 0.8913 0.6808 0.2524  -0.1400 -0.0054 772 GLU A CG  
2187 C CD  . GLU A 254 ? 0.9100 0.9291 0.7226 0.2916  -0.1209 0.0294  772 GLU A CD  
2188 O OE1 . GLU A 254 ? 0.8889 0.8340 0.6850 0.2706  -0.0975 0.0484  772 GLU A OE1 
2189 O OE2 . GLU A 254 ? 0.9643 1.0087 0.7459 0.3450  -0.1269 0.0369  772 GLU A OE2 
2190 N N   . LEU A 255 ? 0.5705 0.5813 0.5343 0.1003  -0.1105 -0.0155 773 LEU A N   
2191 C CA  . LEU A 255 ? 0.5652 0.5558 0.5477 0.0685  -0.0977 -0.0128 773 LEU A CA  
2192 C C   . LEU A 255 ? 0.5524 0.5807 0.5767 0.0440  -0.1010 -0.0296 773 LEU A C   
2193 O O   . LEU A 255 ? 0.5395 0.5738 0.5850 0.0303  -0.0932 -0.0317 773 LEU A O   
2194 C CB  . LEU A 255 ? 0.5616 0.5073 0.5225 0.0540  -0.0862 0.0013  773 LEU A CB  
2195 C CG  . LEU A 255 ? 0.5717 0.5068 0.5472 0.0265  -0.0745 0.0030  773 LEU A CG  
2196 C CD1 . LEU A 255 ? 0.5982 0.5259 0.5762 0.0291  -0.0650 0.0029  773 LEU A CD1 
2197 C CD2 . LEU A 255 ? 0.5544 0.4587 0.5113 0.0148  -0.0654 0.0117  773 LEU A CD2 
2198 N N   . GLU A 256 ? 0.5105 0.5622 0.5471 0.0382  -0.1088 -0.0426 774 GLU A N   
2199 C CA  . GLU A 256 ? 0.5319 0.6113 0.6105 0.0136  -0.1043 -0.0603 774 GLU A CA  
2200 C C   . GLU A 256 ? 0.4929 0.6182 0.6034 0.0175  -0.1076 -0.0799 774 GLU A C   
2201 O O   . GLU A 256 ? 0.4451 0.5764 0.5848 -0.0024 -0.0947 -0.0846 774 GLU A O   
2202 C CB  . GLU A 256 ? 0.5615 0.6571 0.6501 0.0060  -0.1091 -0.0763 774 GLU A CB  
2203 C CG  . GLU A 256 ? 0.6827 0.8103 0.8208 -0.0180 -0.1001 -0.1026 774 GLU A CG  
2204 C CD  . GLU A 256 ? 0.8002 0.9320 0.9506 -0.0318 -0.0976 -0.1190 774 GLU A CD  
2205 O OE1 . GLU A 256 ? 0.8403 0.9593 1.0195 -0.0575 -0.0772 -0.1251 774 GLU A OE1 
2206 O OE2 . GLU A 256 ? 0.8567 1.0023 0.9865 -0.0152 -0.1133 -0.1253 774 GLU A OE2 
2207 N N   . LEU A 257 ? 0.4937 0.6540 0.5971 0.0459  -0.1234 -0.0909 775 LEU A N   
2208 C CA  . LEU A 257 ? 0.5466 0.7577 0.6798 0.0540  -0.1280 -0.1110 775 LEU A CA  
2209 C C   . LEU A 257 ? 0.5751 0.7604 0.7054 0.0525  -0.1167 -0.0948 775 LEU A C   
2210 O O   . LEU A 257 ? 0.5671 0.7798 0.7324 0.0393  -0.1099 -0.1084 775 LEU A O   
2211 C CB  . LEU A 257 ? 0.6047 0.8594 0.7210 0.0948  -0.1480 -0.1210 775 LEU A CB  
2212 C CG  . LEU A 257 ? 0.6732 1.0046 0.8257 0.1074  -0.1581 -0.1520 775 LEU A CG  
2213 C CD1 . LEU A 257 ? 0.7014 1.0782 0.9130 0.0698  -0.1518 -0.1886 775 LEU A CD1 
2214 C CD2 . LEU A 257 ? 0.6831 1.0643 0.8111 0.1550  -0.1796 -0.1604 775 LEU A CD2 
2215 N N   . LEU A 258 ? 0.6077 0.7412 0.6987 0.0639  -0.1119 -0.0686 776 LEU A N   
2216 C CA  . LEU A 258 ? 0.6799 0.7915 0.7680 0.0627  -0.1005 -0.0579 776 LEU A CA  
2217 C C   . LEU A 258 ? 0.6571 0.7593 0.7651 0.0302  -0.0860 -0.0553 776 LEU A C   
2218 O O   . LEU A 258 ? 0.6383 0.7559 0.7658 0.0241  -0.0786 -0.0599 776 LEU A O   
2219 C CB  . LEU A 258 ? 0.7660 0.8238 0.8110 0.0791  -0.0940 -0.0365 776 LEU A CB  
2220 C CG  . LEU A 258 ? 0.8228 0.8488 0.8615 0.0728  -0.0783 -0.0282 776 LEU A CG  
2221 C CD1 . LEU A 258 ? 0.8956 0.8909 0.9052 0.1040  -0.0721 -0.0189 776 LEU A CD1 
2222 C CD2 . LEU A 258 ? 0.7957 0.7883 0.8244 0.0480  -0.0673 -0.0191 776 LEU A CD2 
2223 N N   . MET A 259 ? 0.6040 0.6830 0.7050 0.0128  -0.0808 -0.0468 777 MET A N   
2224 C CA  . MET A 259 ? 0.5919 0.6597 0.7016 -0.0093 -0.0654 -0.0385 777 MET A CA  
2225 C C   . MET A 259 ? 0.5492 0.6429 0.6961 -0.0263 -0.0558 -0.0506 777 MET A C   
2226 O O   . MET A 259 ? 0.5217 0.6198 0.6815 -0.0358 -0.0411 -0.0468 777 MET A O   
2227 C CB  . MET A 259 ? 0.6180 0.6538 0.7048 -0.0168 -0.0621 -0.0241 777 MET A CB  
2228 C CG  . MET A 259 ? 0.6793 0.6862 0.7352 -0.0095 -0.0614 -0.0135 777 MET A CG  
2229 S SD  . MET A 259 ? 0.7260 0.7106 0.7645 -0.0218 -0.0555 -0.0016 777 MET A SD  
2230 C CE  . MET A 259 ? 0.7130 0.7165 0.7691 -0.0338 -0.0423 0.0038  777 MET A CE  
2231 N N   . CYS A 260 ? 0.4908 0.6012 0.6553 -0.0310 -0.0605 -0.0665 778 CYS A N   
2232 C CA  . CYS A 260 ? 0.5292 0.6539 0.7314 -0.0528 -0.0438 -0.0806 778 CYS A CA  
2233 C C   . CYS A 260 ? 0.5206 0.6987 0.7622 -0.0541 -0.0499 -0.1149 778 CYS A C   
2234 O O   . CYS A 260 ? 0.5130 0.7060 0.7942 -0.0763 -0.0314 -0.1337 778 CYS A O   
2235 C CB  . CYS A 260 ? 0.5806 0.6791 0.7779 -0.0643 -0.0367 -0.0761 778 CYS A CB  
2236 S SG  . CYS A 260 ? 0.6479 0.6982 0.7988 -0.0581 -0.0349 -0.0413 778 CYS A SG  
2237 N N   . GLY A 261 ? 0.5858 0.7946 0.8183 -0.0297 -0.0724 -0.1247 779 GLY A N   
2238 C CA  . GLY A 261 ? 0.6459 0.9205 0.9146 -0.0248 -0.0823 -0.1607 779 GLY A CA  
2239 C C   . GLY A 261 ? 0.7312 1.0334 1.0251 -0.0384 -0.0836 -0.1895 779 GLY A C   
2240 O O   . GLY A 261 ? 0.7410 1.0821 1.0856 -0.0611 -0.0706 -0.2228 779 GLY A O   
2241 N N   . LEU A 262 ? 0.7767 1.0602 1.0381 -0.0267 -0.0966 -0.1802 780 LEU A N   
2242 C CA  . LEU A 262 ? 0.8025 1.1044 1.0859 -0.0429 -0.0947 -0.2065 780 LEU A CA  
2243 C C   . LEU A 262 ? 0.7562 1.0754 1.0054 -0.0144 -0.1203 -0.2082 780 LEU A C   
2244 O O   . LEU A 262 ? 0.7854 1.0716 0.9848 0.0122  -0.1313 -0.1766 780 LEU A O   
2245 C CB  . LEU A 262 ? 0.8425 1.0828 1.1255 -0.0707 -0.0691 -0.1884 780 LEU A CB  
2246 C CG  . LEU A 262 ? 0.8843 1.1294 1.2203 -0.1044 -0.0376 -0.2092 780 LEU A CG  
2247 C CD1 . LEU A 262 ? 0.8920 1.0784 1.2241 -0.1241 -0.0116 -0.1927 780 LEU A CD1 
2248 C CD2 . LEU A 262 ? 0.9436 1.2623 1.3321 -0.1157 -0.0407 -0.2644 780 LEU A CD2 
2249 N N   . GLY A 263 ? 0.6404 1.0118 0.9180 -0.0213 -0.1262 -0.2475 781 GLY A N   
2250 C CA  . GLY A 263 ? 0.6679 1.0677 0.9153 0.0067  -0.1496 -0.2544 781 GLY A CA  
2251 C C   . GLY A 263 ? 0.7666 1.2443 1.0617 -0.0068 -0.1538 -0.3114 781 GLY A C   
2252 O O   . GLY A 263 ? 0.8404 1.3260 1.1869 -0.0425 -0.1294 -0.3383 781 GLY A O   
2253 N N   . ASP A 264 ? 0.8294 1.3459 1.0949 0.0250  -0.1736 -0.3200 782 ASP A N   
2254 C CA  . ASP A 264 ? 0.8882 1.4632 1.1809 0.0202  -0.1673 -0.3635 782 ASP A CA  
2255 C C   . ASP A 264 ? 0.8972 1.5420 1.2120 0.0364  -0.1694 -0.3909 782 ASP A C   
2256 O O   . ASP A 264 ? 0.9518 1.6128 1.2351 0.0749  -0.1865 -0.3722 782 ASP A O   
2257 C CB  . ASP A 264 ? 0.9582 1.5497 1.2081 0.0507  -0.1842 -0.3611 782 ASP A CB  
2258 C CG  . ASP A 264 ? 1.0081 1.5421 1.2470 0.0280  -0.1778 -0.3481 782 ASP A CG  
2259 O OD1 . ASP A 264 ? 1.0041 1.4951 1.2781 -0.0143 -0.1554 -0.3516 782 ASP A OD1 
2260 O OD2 . ASP A 264 ? 1.0402 1.5693 1.2330 0.0545  -0.1921 -0.3331 782 ASP A OD2 
2261 N N   . VAL A 265 ? 0.8472 1.5302 1.2152 0.0079  -0.1488 -0.4358 783 VAL A N   
2262 C CA  . VAL A 265 ? 0.8008 1.5593 1.1950 0.0198  -0.1483 -0.4723 783 VAL A CA  
2263 C C   . VAL A 265 ? 0.8390 1.6693 1.2403 0.0333  -0.1518 -0.5155 783 VAL A C   
2264 O O   . VAL A 265 ? 0.8757 1.7149 1.3185 -0.0003 -0.1296 -0.5515 783 VAL A O   
2265 C CB  . VAL A 265 ? 0.7127 1.4633 1.1637 -0.0228 -0.1181 -0.4944 783 VAL A CB  
2266 C CG1 . VAL A 265 ? 0.6613 1.4936 1.1368 -0.0088 -0.1192 -0.5344 783 VAL A CG1 
2267 C CG2 . VAL A 265 ? 0.6998 1.3800 1.1436 -0.0363 -0.1125 -0.4508 783 VAL A CG2 
2268 N N   . ASP A 266 ? 0.8433 1.7237 1.2027 0.0847  -0.1766 -0.5119 784 ASP A N   
2269 C CA  . ASP A 266 ? 0.8754 1.8352 1.2384 0.1046  -0.1812 -0.5535 784 ASP A CA  
2270 C C   . ASP A 266 ? 0.9112 1.9467 1.3349 0.0847  -0.1639 -0.6159 784 ASP A C   
2271 O O   . ASP A 266 ? 0.9224 2.0110 1.3472 0.1081  -0.1709 -0.6299 784 ASP A O   
2272 C CB  . ASP A 266 ? 0.8753 1.8707 1.1759 0.1694  -0.2071 -0.5322 784 ASP A CB  
2273 C CG  . ASP A 266 ? 0.8894 1.9582 1.1831 0.1943  -0.2127 -0.5661 784 ASP A CG  
2274 O OD1 . ASP A 266 ? 0.9048 1.9599 1.1415 0.2328  -0.2268 -0.5345 784 ASP A OD1 
2275 O OD2 . ASP A 266 ? 0.9073 2.0487 1.2528 0.1761  -0.2009 -0.6252 784 ASP A OD2 
2276 N N   . VAL A 267 ? 0.9674 1.1009 1.1431 -0.0791 -0.0563 -0.0869 785 VAL A N   
2277 C CA  . VAL A 267 ? 0.9718 1.0579 1.1518 -0.0496 -0.0647 -0.0951 785 VAL A CA  
2278 C C   . VAL A 267 ? 1.0480 1.1301 1.2252 -0.0464 -0.0646 -0.0739 785 VAL A C   
2279 O O   . VAL A 267 ? 1.0729 1.1032 1.2587 -0.0339 -0.0674 -0.0685 785 VAL A O   
2280 C CB  . VAL A 267 ? 0.9172 1.0390 1.1071 -0.0190 -0.0792 -0.1299 785 VAL A CB  
2281 C CG1 . VAL A 267 ? 0.9068 0.9742 1.1074 0.0033  -0.0887 -0.1360 785 VAL A CG1 
2282 C CG2 . VAL A 267 ? 0.9087 1.0389 1.1003 -0.0180 -0.0826 -0.1467 785 VAL A CG2 
2283 N N   . ASN A 268 ? 1.1112 1.2555 1.2767 -0.0575 -0.0613 -0.0597 786 ASN A N   
2284 C CA  . ASN A 268 ? 1.1728 1.3170 1.3289 -0.0541 -0.0636 -0.0339 786 ASN A CA  
2285 C C   . ASN A 268 ? 1.2020 1.2639 1.3585 -0.0671 -0.0566 0.0003  786 ASN A C   
2286 O O   . ASN A 268 ? 1.2298 1.2491 1.3976 -0.0490 -0.0626 0.0043  786 ASN A O   
2287 C CB  . ASN A 268 ? 1.2307 1.4614 1.3655 -0.0664 -0.0583 -0.0183 786 ASN A CB  
2288 C CG  . ASN A 268 ? 1.2440 1.5592 1.3755 -0.0398 -0.0684 -0.0568 786 ASN A CG  
2289 O OD1 . ASN A 268 ? 1.2536 1.5558 1.3938 -0.0119 -0.0852 -0.0830 786 ASN A OD1 
2290 N ND2 . ASN A 268 ? 1.2530 1.6575 1.3751 -0.0488 -0.0586 -0.0628 786 ASN A ND2 
2291 N N   . ASP A 269 ? 1.1917 1.2311 1.3404 -0.0982 -0.0449 0.0227  787 ASP A N   
2292 C CA  . ASP A 269 ? 1.1797 1.1302 1.3286 -0.1079 -0.0399 0.0497  787 ASP A CA  
2293 C C   . ASP A 269 ? 1.0948 0.9818 1.2590 -0.0847 -0.0412 0.0286  787 ASP A C   
2294 O O   . ASP A 269 ? 1.1042 0.9349 1.2748 -0.0723 -0.0404 0.0446  787 ASP A O   
2295 C CB  . ASP A 269 ? 1.2276 1.1551 1.3716 -0.1477 -0.0305 0.0623  787 ASP A CB  
2296 C CG  . ASP A 269 ? 1.3204 1.1498 1.4624 -0.1578 -0.0278 0.0904  787 ASP A CG  
2297 O OD1 . ASP A 269 ? 1.3775 1.1942 1.5105 -0.1596 -0.0292 0.1310  787 ASP A OD1 
2298 O OD2 . ASP A 269 ? 1.3518 1.1160 1.4988 -0.1609 -0.0257 0.0709  787 ASP A OD2 
2299 N N   . TRP A 270 ? 1.0072 0.9072 1.1776 -0.0768 -0.0425 -0.0053 788 TRP A N   
2300 C CA  . TRP A 270 ? 0.9469 0.8025 1.1294 -0.0551 -0.0416 -0.0214 788 TRP A CA  
2301 C C   . TRP A 270 ? 0.9502 0.8173 1.1517 -0.0311 -0.0493 -0.0179 788 TRP A C   
2302 O O   . TRP A 270 ? 0.9519 0.7786 1.1687 -0.0178 -0.0448 -0.0116 788 TRP A O   
2303 C CB  . TRP A 270 ? 0.8886 0.7629 1.0698 -0.0510 -0.0446 -0.0512 788 TRP A CB  
2304 C CG  . TRP A 270 ? 0.9004 0.7258 1.0833 -0.0381 -0.0390 -0.0614 788 TRP A CG  
2305 C CD1 . TRP A 270 ? 0.9589 0.7383 1.1507 -0.0269 -0.0296 -0.0518 788 TRP A CD1 
2306 C CD2 . TRP A 270 ? 0.9200 0.7460 1.0940 -0.0330 -0.0413 -0.0809 788 TRP A CD2 
2307 N NE1 . TRP A 270 ? 0.9794 0.7349 1.1659 -0.0180 -0.0226 -0.0636 788 TRP A NE1 
2308 C CE2 . TRP A 270 ? 0.9672 0.7466 1.1397 -0.0218 -0.0309 -0.0792 788 TRP A CE2 
2309 C CE3 . TRP A 270 ? 0.9293 0.7961 1.0964 -0.0341 -0.0516 -0.0983 788 TRP A CE3 
2310 C CZ2 . TRP A 270 ? 1.0181 0.7870 1.1755 -0.0142 -0.0301 -0.0896 788 TRP A CZ2 
2311 C CZ3 . TRP A 270 ? 0.9767 0.8288 1.1324 -0.0232 -0.0546 -0.1099 788 TRP A CZ3 
2312 C CH2 . TRP A 270 ? 1.0223 0.8240 1.1698 -0.0147 -0.0438 -0.1033 788 TRP A CH2 
2313 N N   . ARG A 271 ? 0.9751 0.9039 1.1778 -0.0248 -0.0617 -0.0251 789 ARG A N   
2314 C CA  . ARG A 271 ? 0.9935 0.9399 1.2172 -0.0047 -0.0746 -0.0303 789 ARG A CA  
2315 C C   . ARG A 271 ? 1.0422 0.9764 1.2713 0.0010  -0.0763 -0.0001 789 ARG A C   
2316 O O   . ARG A 271 ? 1.0762 0.9902 1.3333 0.0154  -0.0783 0.0018  789 ARG A O   
2317 C CB  . ARG A 271 ? 1.0163 1.0322 1.2339 0.0022  -0.0899 -0.0520 789 ARG A CB  
2318 C CG  . ARG A 271 ? 1.0294 1.0504 1.2583 0.0123  -0.0977 -0.0880 789 ARG A CG  
2319 C CD  . ARG A 271 ? 1.0789 1.1596 1.3079 0.0275  -0.1172 -0.1162 789 ARG A CD  
2320 N NE  . ARG A 271 ? 1.1557 1.2999 1.3569 0.0230  -0.1161 -0.1043 789 ARG A NE  
2321 C CZ  . ARG A 271 ? 1.2043 1.3826 1.3990 0.0301  -0.1279 -0.0968 789 ARG A CZ  
2322 N NH1 . ARG A 271 ? 1.2093 1.3667 1.4311 0.0409  -0.1436 -0.1043 789 ARG A NH1 
2323 N NH2 . ARG A 271 ? 1.2208 1.4603 1.3825 0.0249  -0.1243 -0.0799 789 ARG A NH2 
2324 N N   . GLU A 272 ? 1.0681 1.0190 1.2725 -0.0097 -0.0760 0.0269  790 GLU A N   
2325 C CA  . GLU A 272 ? 1.0863 1.0323 1.2914 0.0007  -0.0834 0.0599  790 GLU A CA  
2326 C C   . GLU A 272 ? 1.0646 0.9360 1.2877 0.0094  -0.0745 0.0760  790 GLU A C   
2327 O O   . GLU A 272 ? 1.1061 0.9734 1.3444 0.0292  -0.0835 0.0959  790 GLU A O   
2328 C CB  . GLU A 272 ? 1.1900 1.1633 1.3590 -0.0160 -0.0828 0.0937  790 GLU A CB  
2329 C CG  . GLU A 272 ? 1.2426 1.3074 1.3904 -0.0172 -0.0910 0.0790  790 GLU A CG  
2330 C CD  . GLU A 272 ? 1.3159 1.4110 1.4407 -0.0453 -0.0761 0.0822  790 GLU A CD  
2331 O OE1 . GLU A 272 ? 1.3363 1.3834 1.4694 -0.0636 -0.0633 0.0787  790 GLU A OE1 
2332 O OE2 . GLU A 272 ? 1.3464 1.5212 1.4454 -0.0491 -0.0772 0.0865  790 GLU A OE2 
2333 N N   . HIS A 273 ? 1.0072 0.8248 1.2287 -0.0013 -0.0586 0.0651  791 HIS A N   
2334 C CA  . HIS A 273 ? 1.0166 0.7640 1.2511 0.0106  -0.0484 0.0717  791 HIS A CA  
2335 C C   . HIS A 273 ? 0.9825 0.7225 1.2410 0.0241  -0.0386 0.0428  791 HIS A C   
2336 O O   . HIS A 273 ? 1.0346 0.7233 1.2910 0.0273  -0.0240 0.0337  791 HIS A O   
2337 C CB  . HIS A 273 ? 1.0273 0.7145 1.2370 -0.0124 -0.0388 0.0809  791 HIS A CB  
2338 C CG  . HIS A 273 ? 1.0626 0.7590 1.2496 -0.0337 -0.0452 0.1164  791 HIS A CG  
2339 N ND1 . HIS A 273 ? 1.0510 0.7946 1.2182 -0.0643 -0.0437 0.1151  791 HIS A ND1 
2340 C CD2 . HIS A 273 ? 1.1206 0.7917 1.3017 -0.0281 -0.0527 0.1580  791 HIS A CD2 
2341 C CE1 . HIS A 273 ? 1.0957 0.8454 1.2447 -0.0809 -0.0466 0.1559  791 HIS A CE1 
2342 N NE2 . HIS A 273 ? 1.1454 0.8462 1.2996 -0.0595 -0.0533 0.1848  791 HIS A NE2 
2343 N N   . THR A 274 ? 0.8728 0.6640 1.1529 0.0311  -0.0470 0.0285  792 THR A N   
2344 C CA  . THR A 274 ? 0.7920 0.5836 1.0987 0.0393  -0.0384 0.0094  792 THR A CA  
2345 C C   . THR A 274 ? 0.8150 0.6345 1.1675 0.0590  -0.0447 0.0170  792 THR A C   
2346 O O   . THR A 274 ? 0.8280 0.6889 1.1907 0.0635  -0.0649 0.0246  792 THR A O   
2347 C CB  . THR A 274 ? 0.7798 0.6008 1.0818 0.0280  -0.0456 -0.0126 792 THR A CB  
2348 O OG1 . THR A 274 ? 0.7515 0.5565 1.0174 0.0128  -0.0402 -0.0208 792 THR A OG1 
2349 C CG2 . THR A 274 ? 0.7323 0.5503 1.0622 0.0325  -0.0381 -0.0232 792 THR A CG2 
2350 N N   . LYS A 275 ? 0.8835 0.6893 1.2636 0.0712  -0.0276 0.0139  793 LYS A N   
2351 C CA  . LYS A 275 ? 0.9338 0.7775 1.3683 0.0888  -0.0306 0.0198  793 LYS A CA  
2352 C C   . LYS A 275 ? 0.9705 0.8388 1.4386 0.0794  -0.0211 0.0069  793 LYS A C   
2353 O O   . LYS A 275 ? 1.0816 0.9231 1.5267 0.0685  -0.0046 -0.0017 793 LYS A O   
2354 C CB  . LYS A 275 ? 0.9370 0.7542 1.3850 0.1156  -0.0160 0.0309  793 LYS A CB  
2355 C CG  . LYS A 275 ? 1.0044 0.7891 1.4278 0.1265  -0.0289 0.0517  793 LYS A CG  
2356 C CD  . LYS A 275 ? 1.0248 0.8593 1.4522 0.1241  -0.0582 0.0663  793 LYS A CD  
2357 C CE  . LYS A 275 ? 1.0682 0.9194 1.5263 0.1562  -0.0722 0.0895  793 LYS A CE  
2358 N NZ  . LYS A 275 ? 1.0960 0.9498 1.5194 0.1555  -0.0956 0.1179  793 LYS A NZ  
2359 N N   . TYR A 276 ? 0.9416 0.8623 1.4656 0.0819  -0.0328 0.0080  794 TYR A N   
2360 C CA  . TYR A 276 ? 0.8452 0.7891 1.4081 0.0648  -0.0275 0.0004  794 TYR A CA  
2361 C C   . TYR A 276 ? 0.8042 0.7924 1.4321 0.0755  -0.0127 0.0093  794 TYR A C   
2362 O O   . TYR A 276 ? 0.7848 0.8060 1.4432 0.0973  -0.0217 0.0165  794 TYR A O   
2363 C CB  . TYR A 276 ? 0.8023 0.7731 1.3802 0.0479  -0.0596 -0.0137 794 TYR A CB  
2364 C CG  . TYR A 276 ? 0.7560 0.7006 1.2748 0.0430  -0.0734 -0.0251 794 TYR A CG  
2365 C CD1 . TYR A 276 ? 0.7517 0.6606 1.2403 0.0305  -0.0666 -0.0351 794 TYR A CD1 
2366 C CD2 . TYR A 276 ? 0.7204 0.6828 1.2135 0.0525  -0.0924 -0.0231 794 TYR A CD2 
2367 C CE1 . TYR A 276 ? 0.7677 0.6661 1.2095 0.0289  -0.0781 -0.0475 794 TYR A CE1 
2368 C CE2 . TYR A 276 ? 0.7263 0.6796 1.1691 0.0470  -0.1006 -0.0326 794 TYR A CE2 
2369 C CZ  . TYR A 276 ? 0.7487 0.6734 1.1697 0.0359  -0.0933 -0.0471 794 TYR A CZ  
2370 O OH  . TYR A 276 ? 0.7439 0.6728 1.1222 0.0331  -0.1008 -0.0586 794 TYR A OH  
2371 N N   . LYS A 277 ? 0.8098 0.8040 1.4596 0.0607  0.0104  0.0113  795 LYS A N   
2372 C CA  . LYS A 277 ? 0.8210 0.8687 1.5346 0.0669  0.0326  0.0208  795 LYS A CA  
2373 C C   . LYS A 277 ? 0.7613 0.8471 1.5331 0.0331  0.0275  0.0241  795 LYS A C   
2374 O O   . LYS A 277 ? 0.7300 0.7789 1.4792 0.0075  0.0168  0.0202  795 LYS A O   
2375 C CB  . LYS A 277 ? 0.8928 0.9200 1.5780 0.0793  0.0743  0.0250  795 LYS A CB  
2376 C CG  . LYS A 277 ? 0.9668 0.9455 1.5976 0.1092  0.0820  0.0178  795 LYS A CG  
2377 C CD  . LYS A 277 ? 1.0648 1.0746 1.7258 0.1413  0.1107  0.0175  795 LYS A CD  
2378 C CE  . LYS A 277 ? 1.1756 1.1881 1.8154 0.1375  0.1507  0.0160  795 LYS A CE  
2379 N NZ  . LYS A 277 ? 1.2302 1.1715 1.7893 0.1503  0.1620  0.0001  795 LYS A NZ  
2380 N N   . ASN A 278 ? 0.7758 0.9350 1.6265 0.0335  0.0352  0.0316  796 ASN A N   
2381 C CA  . ASN A 278 ? 0.7926 0.9950 1.7121 -0.0039 0.0386  0.0401  796 ASN A CA  
2382 C C   . ASN A 278 ? 0.7295 0.9081 1.6562 -0.0352 -0.0027 0.0261  796 ASN A C   
2383 O O   . ASN A 278 ? 0.7328 0.8785 1.6618 -0.0682 -0.0009 0.0318  796 ASN A O   
2384 C CB  . ASN A 278 ? 0.8558 1.0402 1.7560 -0.0189 0.0817  0.0594  796 ASN A CB  
2385 C CG  . ASN A 278 ? 0.8846 1.1380 1.8715 -0.0524 0.0993  0.0789  796 ASN A CG  
2386 O OD1 . ASN A 278 ? 0.8694 1.1930 1.9393 -0.0613 0.0809  0.0747  796 ASN A OD1 
2387 N ND2 . ASN A 278 ? 0.9298 1.1685 1.8983 -0.0730 0.1342  0.1026  796 ASN A ND2 
2388 N N   . GLY A 279 ? 0.6840 0.8776 1.6112 -0.0220 -0.0413 0.0074  797 GLY A N   
2389 C CA  . GLY A 279 ? 0.6852 0.8764 1.6302 -0.0460 -0.0838 -0.0146 797 GLY A CA  
2390 C C   . GLY A 279 ? 0.7353 0.8605 1.6003 -0.0397 -0.1045 -0.0335 797 GLY A C   
2391 O O   . GLY A 279 ? 0.7495 0.8816 1.6202 -0.0474 -0.1434 -0.0595 797 GLY A O   
2392 N N   . TYR A 280 ? 0.7441 0.8134 1.5374 -0.0256 -0.0805 -0.0245 798 TYR A N   
2393 C CA  . TYR A 280 ? 0.7264 0.7478 1.4502 -0.0190 -0.0980 -0.0420 798 TYR A CA  
2394 C C   . TYR A 280 ? 0.7090 0.7593 1.4070 0.0045  -0.1199 -0.0507 798 TYR A C   
2395 O O   . TYR A 280 ? 0.6820 0.7673 1.3965 0.0232  -0.1146 -0.0363 798 TYR A O   
2396 C CB  . TYR A 280 ? 0.7045 0.6694 1.3642 -0.0120 -0.0685 -0.0302 798 TYR A CB  
2397 C CG  . TYR A 280 ? 0.7386 0.6587 1.3929 -0.0327 -0.0599 -0.0256 798 TYR A CG  
2398 C CD1 . TYR A 280 ? 0.7461 0.6322 1.3589 -0.0293 -0.0282 -0.0078 798 TYR A CD1 
2399 C CD2 . TYR A 280 ? 0.8043 0.7118 1.4918 -0.0542 -0.0861 -0.0392 798 TYR A CD2 
2400 C CE1 . TYR A 280 ? 0.7451 0.5904 1.3470 -0.0453 -0.0220 0.0030  798 TYR A CE1 
2401 C CE2 . TYR A 280 ? 0.7913 0.6467 1.4726 -0.0712 -0.0803 -0.0289 798 TYR A CE2 
2402 C CZ  . TYR A 280 ? 0.7702 0.5969 1.4072 -0.0660 -0.0478 -0.0043 798 TYR A CZ  
2403 O OH  . TYR A 280 ? 0.7497 0.5255 1.3749 -0.0803 -0.0435 0.0124  798 TYR A OH  
2404 N N   . SER A 281 ? 0.7158 0.7531 1.3718 0.0058  -0.1445 -0.0729 799 SER A N   
2405 C CA  . SER A 281 ? 0.7038 0.7712 1.3243 0.0249  -0.1640 -0.0774 799 SER A CA  
2406 C C   . SER A 281 ? 0.7197 0.7613 1.2778 0.0263  -0.1713 -0.0959 799 SER A C   
2407 O O   . SER A 281 ? 0.7412 0.7455 1.2934 0.0157  -0.1695 -0.1108 799 SER A O   
2408 C CB  . SER A 281 ? 0.6850 0.8168 1.3499 0.0253  -0.1999 -0.0933 799 SER A CB  
2409 O OG  . SER A 281 ? 0.6935 0.8226 1.3791 0.0067  -0.2257 -0.1283 799 SER A OG  
2410 N N   . ALA A 282 ? 0.7538 0.8199 1.2669 0.0408  -0.1795 -0.0922 800 ALA A N   
2411 C CA  . ALA A 282 ? 0.8149 0.8754 1.2721 0.0429  -0.1832 -0.1088 800 ALA A CA  
2412 C C   . ALA A 282 ? 0.8500 0.9267 1.3171 0.0407  -0.2122 -0.1522 800 ALA A C   
2413 O O   . ALA A 282 ? 0.8512 0.9067 1.2926 0.0419  -0.2118 -0.1731 800 ALA A O   
2414 C CB  . ALA A 282 ? 0.7438 0.8379 1.1546 0.0545  -0.1852 -0.0905 800 ALA A CB  
2415 N N   . ASN A 283 ? 0.9074 1.0219 1.4142 0.0392  -0.2401 -0.1695 801 ASN A N   
2416 C CA  . ASN A 283 ? 0.9718 1.0965 1.4913 0.0370  -0.2729 -0.2180 801 ASN A CA  
2417 C C   . ASN A 283 ? 0.9504 1.0209 1.5240 0.0167  -0.2754 -0.2301 801 ASN A C   
2418 O O   . ASN A 283 ? 0.9475 1.0044 1.5335 0.0141  -0.3029 -0.2722 801 ASN A O   
2419 C CB  . ASN A 283 ? 1.0173 1.2112 1.5525 0.0427  -0.3075 -0.2362 801 ASN A CB  
2420 C CG  . ASN A 283 ? 1.0349 1.2556 1.6164 0.0390  -0.3037 -0.2017 801 ASN A CG  
2421 O OD1 . ASN A 283 ? 1.0184 1.2447 1.5769 0.0508  -0.2826 -0.1614 801 ASN A OD1 
2422 N ND2 . ASN A 283 ? 1.0541 1.2919 1.7060 0.0227  -0.3252 -0.2184 801 ASN A ND2 
2423 N N   . HIS A 284 ? 0.9018 0.9405 1.5064 0.0028  -0.2475 -0.1941 802 HIS A N   
2424 C CA  . HIS A 284 ? 0.8538 0.8410 1.5048 -0.0201 -0.2448 -0.1943 802 HIS A CA  
2425 C C   . HIS A 284 ? 0.8530 0.7809 1.4679 -0.0143 -0.2465 -0.2123 802 HIS A C   
2426 O O   . HIS A 284 ? 0.8369 0.7596 1.3950 0.0037  -0.2315 -0.2075 802 HIS A O   
2427 C CB  . HIS A 284 ? 0.8030 0.7779 1.4777 -0.0311 -0.2071 -0.1491 802 HIS A CB  
2428 C CG  . HIS A 284 ? 0.7851 0.7291 1.5191 -0.0607 -0.2029 -0.1394 802 HIS A CG  
2429 N ND1 . HIS A 284 ? 0.7979 0.6727 1.5181 -0.0701 -0.1958 -0.1348 802 HIS A ND1 
2430 C CD2 . HIS A 284 ? 0.7848 0.7613 1.5943 -0.0849 -0.2044 -0.1293 802 HIS A CD2 
2431 C CE1 . HIS A 284 ? 0.8303 0.6897 1.6110 -0.1012 -0.1919 -0.1184 802 HIS A CE1 
2432 N NE2 . HIS A 284 ? 0.8247 0.7492 1.6636 -0.1127 -0.1958 -0.1160 802 HIS A NE2 
2433 N N   . GLN A 285 ? 0.8828 0.7653 1.5356 -0.0299 -0.2668 -0.2326 803 GLN A N   
2434 C CA  . GLN A 285 ? 0.9223 0.7489 1.5449 -0.0164 -0.2779 -0.2570 803 GLN A CA  
2435 C C   . GLN A 285 ? 0.8915 0.6690 1.4848 -0.0143 -0.2458 -0.2196 803 GLN A C   
2436 O O   . GLN A 285 ? 0.8947 0.6545 1.4428 0.0085  -0.2464 -0.2321 803 GLN A O   
2437 C CB  . GLN A 285 ? 1.0061 0.7843 1.6786 -0.0325 -0.3131 -0.2898 803 GLN A CB  
2438 C CG  . GLN A 285 ? 1.0917 0.7823 1.7528 -0.0259 -0.3172 -0.2924 803 GLN A CG  
2439 C CD  . GLN A 285 ? 1.2309 0.8979 1.8995 -0.0181 -0.3501 -0.3319 803 GLN A CD  
2440 O OE1 . GLN A 285 ? 1.2689 0.9659 1.9095 0.0113  -0.3723 -0.3815 803 GLN A OE1 
2441 N NE2 . GLN A 285 ? 1.3151 0.9298 2.0200 -0.0444 -0.3522 -0.3103 803 GLN A NE2 
2442 N N   . VAL A 286 ? 0.8615 0.6263 1.4789 -0.0355 -0.2179 -0.1755 804 VAL A N   
2443 C CA  . VAL A 286 ? 0.8223 0.5515 1.4022 -0.0313 -0.1872 -0.1410 804 VAL A CA  
2444 C C   . VAL A 286 ? 0.7892 0.5546 1.3120 -0.0092 -0.1696 -0.1385 804 VAL A C   
2445 O O   . VAL A 286 ? 0.7697 0.5130 1.2480 0.0042  -0.1605 -0.1341 804 VAL A O   
2446 C CB  . VAL A 286 ? 0.7577 0.4797 1.3723 -0.0572 -0.1580 -0.0968 804 VAL A CB  
2447 C CG1 . VAL A 286 ? 0.7470 0.4394 1.3129 -0.0501 -0.1271 -0.0643 804 VAL A CG1 
2448 C CG2 . VAL A 286 ? 0.7822 0.4660 1.4578 -0.0870 -0.1751 -0.0942 804 VAL A CG2 
2449 N N   . ILE A 287 ? 0.7635 0.5846 1.2888 -0.0062 -0.1673 -0.1403 805 ILE A N   
2450 C CA  . ILE A 287 ? 0.7611 0.6086 1.2368 0.0087  -0.1511 -0.1326 805 ILE A CA  
2451 C C   . ILE A 287 ? 0.8028 0.6657 1.2393 0.0263  -0.1682 -0.1629 805 ILE A C   
2452 O O   . ILE A 287 ? 0.7592 0.6215 1.1544 0.0343  -0.1547 -0.1574 805 ILE A O   
2453 C CB  . ILE A 287 ? 0.7550 0.6498 1.2449 0.0091  -0.1464 -0.1204 805 ILE A CB  
2454 C CG1 . ILE A 287 ? 0.7936 0.6818 1.3186 -0.0015 -0.1216 -0.0900 805 ILE A CG1 
2455 C CG2 . ILE A 287 ? 0.7393 0.6544 1.1787 0.0215  -0.1366 -0.1136 805 ILE A CG2 
2456 C CD1 . ILE A 287 ? 0.8150 0.6660 1.3067 -0.0006 -0.0901 -0.0685 805 ILE A CD1 
2457 N N   . GLN A 288 ? 0.8895 0.7732 1.3399 0.0328  -0.1983 -0.1986 806 GLN A N   
2458 C CA  . GLN A 288 ? 0.9249 0.8338 1.3392 0.0539  -0.2120 -0.2316 806 GLN A CA  
2459 C C   . GLN A 288 ? 0.9485 0.8090 1.3546 0.0651  -0.2157 -0.2428 806 GLN A C   
2460 O O   . GLN A 288 ? 1.0172 0.9038 1.3919 0.0852  -0.2181 -0.2625 806 GLN A O   
2461 C CB  . GLN A 288 ? 0.9644 0.9133 1.3896 0.0630  -0.2439 -0.2736 806 GLN A CB  
2462 C CG  . GLN A 288 ? 1.0770 0.9875 1.5550 0.0513  -0.2698 -0.2943 806 GLN A CG  
2463 C CD  . GLN A 288 ? 1.1354 1.0985 1.6265 0.0542  -0.3004 -0.3303 806 GLN A CD  
2464 O OE1 . GLN A 288 ? 1.1745 1.1210 1.7161 0.0374  -0.3226 -0.3445 806 GLN A OE1 
2465 N NE2 . GLN A 288 ? 1.1454 1.1773 1.5907 0.0732  -0.3022 -0.3443 806 GLN A NE2 
2466 N N   . TRP A 289 ? 0.9141 0.7097 1.3488 0.0533  -0.2159 -0.2275 807 TRP A N   
2467 C CA  . TRP A 289 ? 0.9127 0.6576 1.3324 0.0652  -0.2164 -0.2238 807 TRP A CA  
2468 C C   . TRP A 289 ? 0.8794 0.6320 1.2614 0.0644  -0.1870 -0.1914 807 TRP A C   
2469 O O   . TRP A 289 ? 0.8771 0.6323 1.2304 0.0829  -0.1888 -0.1990 807 TRP A O   
2470 C CB  . TRP A 289 ? 0.8798 0.5503 1.3375 0.0491  -0.2245 -0.2081 807 TRP A CB  
2471 C CG  . TRP A 289 ? 0.9061 0.5425 1.3958 0.0558  -0.2617 -0.2487 807 TRP A CG  
2472 C CD1 . TRP A 289 ? 0.9071 0.5650 1.3843 0.0856  -0.2876 -0.3010 807 TRP A CD1 
2473 C CD2 . TRP A 289 ? 0.9261 0.5090 1.4620 0.0313  -0.2746 -0.2396 807 TRP A CD2 
2474 N NE1 . TRP A 289 ? 0.9295 0.5521 1.4358 0.0835  -0.3151 -0.3243 807 TRP A NE1 
2475 C CE2 . TRP A 289 ? 0.9701 0.5479 1.5113 0.0479  -0.3068 -0.2842 807 TRP A CE2 
2476 C CE3 . TRP A 289 ? 0.9187 0.4726 1.4869 -0.0040 -0.2570 -0.1938 807 TRP A CE3 
2477 C CZ2 . TRP A 289 ? 1.0299 0.5653 1.6080 0.0284  -0.3241 -0.2845 807 TRP A CZ2 
2478 C CZ3 . TRP A 289 ? 0.9630 0.4821 1.5693 -0.0256 -0.2726 -0.1920 807 TRP A CZ3 
2479 C CH2 . TRP A 289 ? 1.0248 0.5302 1.6357 -0.0103 -0.3069 -0.2372 807 TRP A CH2 
2480 N N   . PHE A 290 ? 0.8549 0.6140 1.2391 0.0449  -0.1618 -0.1589 808 PHE A N   
2481 C CA  . PHE A 290 ? 0.8427 0.6059 1.1905 0.0432  -0.1358 -0.1348 808 PHE A CA  
2482 C C   . PHE A 290 ? 0.8145 0.6274 1.1298 0.0535  -0.1359 -0.1511 808 PHE A C   
2483 O O   . PHE A 290 ? 0.7948 0.6099 1.0809 0.0592  -0.1299 -0.1489 808 PHE A O   
2484 C CB  . PHE A 290 ? 0.7922 0.5580 1.1517 0.0262  -0.1110 -0.1064 808 PHE A CB  
2485 C CG  . PHE A 290 ? 0.7783 0.5528 1.1004 0.0257  -0.0879 -0.0926 808 PHE A CG  
2486 C CD1 . PHE A 290 ? 0.8375 0.5835 1.1320 0.0256  -0.0726 -0.0773 808 PHE A CD1 
2487 C CD2 . PHE A 290 ? 0.6741 0.4819 0.9866 0.0246  -0.0835 -0.0945 808 PHE A CD2 
2488 C CE1 . PHE A 290 ? 0.8019 0.5524 1.0625 0.0239  -0.0552 -0.0722 808 PHE A CE1 
2489 C CE2 . PHE A 290 ? 0.6987 0.5023 0.9807 0.0209  -0.0654 -0.0841 808 PHE A CE2 
2490 C CZ  . PHE A 290 ? 0.7606 0.5354 1.0180 0.0203  -0.0521 -0.0768 808 PHE A CZ  
2491 N N   . TRP A 291 ? 0.7832 0.6425 1.1037 0.0542  -0.1433 -0.1658 809 TRP A N   
2492 C CA  . TRP A 291 ? 0.7893 0.7020 1.0802 0.0573  -0.1385 -0.1724 809 TRP A CA  
2493 C C   . TRP A 291 ? 0.7995 0.7415 1.0795 0.0777  -0.1535 -0.2036 809 TRP A C   
2494 O O   . TRP A 291 ? 0.7978 0.7785 1.0559 0.0776  -0.1450 -0.2039 809 TRP A O   
2495 C CB  . TRP A 291 ? 0.8163 0.7739 1.1094 0.0528  -0.1410 -0.1718 809 TRP A CB  
2496 C CG  . TRP A 291 ? 0.8237 0.7648 1.1193 0.0379  -0.1229 -0.1381 809 TRP A CG  
2497 C CD1 . TRP A 291 ? 0.8075 0.7486 1.1292 0.0351  -0.1262 -0.1276 809 TRP A CD1 
2498 C CD2 . TRP A 291 ? 0.8673 0.7890 1.1418 0.0267  -0.1008 -0.1143 809 TRP A CD2 
2499 N NE1 . TRP A 291 ? 0.8487 0.7717 1.1671 0.0278  -0.1064 -0.0979 809 TRP A NE1 
2500 C CE2 . TRP A 291 ? 0.8740 0.7793 1.1617 0.0219  -0.0908 -0.0910 809 TRP A CE2 
2501 C CE3 . TRP A 291 ? 0.9134 0.8323 1.1615 0.0211  -0.0911 -0.1139 809 TRP A CE3 
2502 C CZ2 . TRP A 291 ? 0.9062 0.7824 1.1791 0.0142  -0.0713 -0.0701 809 TRP A CZ2 
2503 C CZ3 . TRP A 291 ? 0.9279 0.8197 1.1614 0.0079  -0.0730 -0.0937 809 TRP A CZ3 
2504 C CH2 . TRP A 291 ? 0.9447 0.8105 1.1891 0.0057  -0.0631 -0.0732 809 TRP A CH2 
2505 N N   . LYS A 292 ? 0.8363 0.7624 1.1352 0.0959  -0.1768 -0.2322 810 LYS A N   
2506 C CA  . LYS A 292 ? 0.8758 0.8307 1.1665 0.1233  -0.1912 -0.2652 810 LYS A CA  
2507 C C   . LYS A 292 ? 0.8910 0.8009 1.1767 0.1327  -0.1919 -0.2540 810 LYS A C   
2508 O O   . LYS A 292 ? 0.8812 0.8265 1.1572 0.1543  -0.1983 -0.2720 810 LYS A O   
2509 C CB  . LYS A 292 ? 0.9352 0.8920 1.2443 0.1455  -0.2190 -0.3088 810 LYS A CB  
2510 C CG  . LYS A 292 ? 0.9970 0.8705 1.3329 0.1556  -0.2409 -0.3188 810 LYS A CG  
2511 C CD  . LYS A 292 ? 1.0334 0.9194 1.3723 0.1957  -0.2675 -0.3712 810 LYS A CD  
2512 C CE  . LYS A 292 ? 1.0622 0.8509 1.4295 0.2071  -0.2943 -0.3822 810 LYS A CE  
2513 N NZ  . LYS A 292 ? 1.1247 0.9177 1.5016 0.2459  -0.3257 -0.4444 810 LYS A NZ  
2514 N N   . ALA A 293 ? 0.9017 0.7436 1.1929 0.1177  -0.1847 -0.2226 811 ALA A N   
2515 C CA  . ALA A 293 ? 0.9474 0.7571 1.2205 0.1229  -0.1807 -0.2025 811 ALA A CA  
2516 C C   . ALA A 293 ? 0.9344 0.7944 1.1794 0.1134  -0.1631 -0.1940 811 ALA A C   
2517 O O   . ALA A 293 ? 0.9600 0.8452 1.1917 0.1292  -0.1704 -0.2028 811 ALA A O   
2518 C CB  . ALA A 293 ? 0.9635 0.7040 1.2422 0.1048  -0.1701 -0.1663 811 ALA A CB  
2519 N N   . VAL A 294 ? 0.9171 0.7916 1.1565 0.0876  -0.1424 -0.1779 812 VAL A N   
2520 C CA  . VAL A 294 ? 0.9121 0.8220 1.1286 0.0725  -0.1273 -0.1702 812 VAL A CA  
2521 C C   . VAL A 294 ? 0.8895 0.8778 1.1067 0.0792  -0.1339 -0.1941 812 VAL A C   
2522 O O   . VAL A 294 ? 0.8742 0.9007 1.0803 0.0737  -0.1311 -0.1965 812 VAL A O   
2523 C CB  . VAL A 294 ? 0.9277 0.8229 1.1415 0.0473  -0.1064 -0.1480 812 VAL A CB  
2524 C CG1 . VAL A 294 ? 0.9073 0.8357 1.1030 0.0281  -0.0948 -0.1440 812 VAL A CG1 
2525 C CG2 . VAL A 294 ? 0.9498 0.7846 1.1603 0.0425  -0.0945 -0.1260 812 VAL A CG2 
2526 N N   . LEU A 295 ? 0.9038 0.9256 1.1351 0.0905  -0.1428 -0.2139 813 LEU A N   
2527 C CA  . LEU A 295 ? 0.9524 1.0625 1.1832 0.0995  -0.1455 -0.2375 813 LEU A CA  
2528 C C   . LEU A 295 ? 1.0126 1.1491 1.2482 0.1275  -0.1600 -0.2604 813 LEU A C   
2529 O O   . LEU A 295 ? 1.0295 1.2344 1.2633 0.1222  -0.1544 -0.2646 813 LEU A O   
2530 C CB  . LEU A 295 ? 0.9840 1.1249 1.2226 0.1133  -0.1549 -0.2603 813 LEU A CB  
2531 C CG  . LEU A 295 ? 1.0221 1.2666 1.2517 0.1138  -0.1480 -0.2748 813 LEU A CG  
2532 C CD1 . LEU A 295 ? 1.0601 1.3759 1.2965 0.1394  -0.1539 -0.3056 813 LEU A CD1 
2533 C CD2 . LEU A 295 ? 0.9991 1.2648 1.2136 0.0746  -0.1246 -0.2364 813 LEU A CD2 
2534 N N   . MET A 296 ? 1.0151 1.0985 1.2606 0.1570  -0.1802 -0.2738 814 MET A N   
2535 C CA  . MET A 296 ? 1.0144 1.1166 1.2657 0.1920  -0.1986 -0.2946 814 MET A CA  
2536 C C   . MET A 296 ? 0.9900 1.0634 1.2260 0.1854  -0.1977 -0.2692 814 MET A C   
2537 O O   . MET A 296 ? 1.0281 1.1133 1.2673 0.2168  -0.2162 -0.2808 814 MET A O   
2538 C CB  . MET A 296 ? 1.0734 1.1197 1.3410 0.2291  -0.2246 -0.3186 814 MET A CB  
2539 C CG  . MET A 296 ? 1.1315 1.0658 1.3987 0.2207  -0.2302 -0.2894 814 MET A CG  
2540 S SD  . MET A 296 ? 1.1980 1.0566 1.4887 0.2629  -0.2660 -0.3160 814 MET A SD  
2541 C CE  . MET A 296 ? 1.1820 1.0795 1.4909 0.2669  -0.2725 -0.3629 814 MET A CE  
2542 N N   . MET A 297 ? 0.9347 0.9739 1.1526 0.1497  -0.1786 -0.2375 815 MET A N   
2543 C CA  . MET A 297 ? 0.9543 0.9806 1.1503 0.1417  -0.1770 -0.2196 815 MET A CA  
2544 C C   . MET A 297 ? 0.9186 1.0344 1.1165 0.1280  -0.1733 -0.2318 815 MET A C   
2545 O O   . MET A 297 ? 0.8686 1.0358 1.0762 0.1051  -0.1592 -0.2361 815 MET A O   
2546 C CB  . MET A 297 ? 1.0024 0.9643 1.1779 0.1117  -0.1571 -0.1887 815 MET A CB  
2547 C CG  . MET A 297 ? 1.1066 0.9861 1.2777 0.1221  -0.1602 -0.1682 815 MET A CG  
2548 S SD  . MET A 297 ? 1.1232 0.9492 1.2867 0.0904  -0.1318 -0.1387 815 MET A SD  
2549 C CE  . MET A 297 ? 1.0743 0.9276 1.2067 0.0676  -0.1161 -0.1371 815 MET A CE  
2550 N N   . ASP A 298 ? 0.9593 1.0970 1.1489 0.1404  -0.1872 -0.2348 816 ASP A N   
2551 C CA  . ASP A 298 ? 0.9839 1.2115 1.1825 0.1221  -0.1862 -0.2470 816 ASP A CA  
2552 C C   . ASP A 298 ? 0.9489 1.1577 1.1315 0.0718  -0.1651 -0.2302 816 ASP A C   
2553 O O   . ASP A 298 ? 0.9299 1.0573 1.0890 0.0596  -0.1536 -0.2104 816 ASP A O   
2554 C CB  . ASP A 298 ? 1.0627 1.3193 1.2565 0.1479  -0.2106 -0.2547 816 ASP A CB  
2555 C CG  . ASP A 298 ? 1.1536 1.3262 1.3062 0.1492  -0.2151 -0.2305 816 ASP A CG  
2556 O OD1 . ASP A 298 ? 1.2074 1.3139 1.3491 0.1799  -0.2253 -0.2174 816 ASP A OD1 
2557 O OD2 . ASP A 298 ? 1.1733 1.3463 1.3035 0.1187  -0.2085 -0.2250 816 ASP A OD2 
2558 N N   . SER A 299 ? 0.9572 1.2439 1.1566 0.0424  -0.1598 -0.2389 817 SER A N   
2559 C CA  . SER A 299 ? 0.9787 1.2417 1.1684 -0.0071 -0.1419 -0.2246 817 SER A CA  
2560 C C   . SER A 299 ? 0.9952 1.1901 1.1508 -0.0159 -0.1452 -0.2190 817 SER A C   
2561 O O   . SER A 299 ? 0.9739 1.1073 1.1128 -0.0425 -0.1297 -0.2066 817 SER A O   
2562 C CB  . SER A 299 ? 0.9855 1.3459 1.2038 -0.0413 -0.1389 -0.2332 817 SER A CB  
2563 O OG  . SER A 299 ? 1.0073 1.3383 1.2156 -0.0866 -0.1339 -0.2268 817 SER A OG  
2564 N N   . GLU A 300 ? 1.0266 1.2329 1.1688 0.0100  -0.1661 -0.2286 818 GLU A N   
2565 C CA  . GLU A 300 ? 1.1009 1.2510 1.2013 0.0056  -0.1693 -0.2245 818 GLU A CA  
2566 C C   . GLU A 300 ? 1.0894 1.1463 1.1617 0.0213  -0.1552 -0.2023 818 GLU A C   
2567 O O   . GLU A 300 ? 1.1229 1.1251 1.1669 0.0046  -0.1411 -0.1961 818 GLU A O   
2568 C CB  . GLU A 300 ? 1.2066 1.4022 1.2957 0.0319  -0.1980 -0.2365 818 GLU A CB  
2569 C CG  . GLU A 300 ? 1.3151 1.4627 1.3509 0.0319  -0.2032 -0.2332 818 GLU A CG  
2570 C CD  . GLU A 300 ? 1.3883 1.4996 1.3916 0.0771  -0.2154 -0.2137 818 GLU A CD  
2571 O OE1 . GLU A 300 ? 1.3843 1.4902 1.4104 0.1069  -0.2200 -0.2037 818 GLU A OE1 
2572 O OE2 . GLU A 300 ? 1.4441 1.5302 1.3972 0.0825  -0.2211 -0.2082 818 GLU A OE2 
2573 N N   . LYS A 301 ? 1.0630 1.1030 1.1462 0.0531  -0.1590 -0.1923 819 LYS A N   
2574 C CA  . LYS A 301 ? 1.0480 1.0078 1.1130 0.0632  -0.1462 -0.1689 819 LYS A CA  
2575 C C   . LYS A 301 ? 0.9894 0.9170 1.0684 0.0399  -0.1220 -0.1608 819 LYS A C   
2576 O O   . LYS A 301 ? 0.9919 0.8627 1.0552 0.0371  -0.1057 -0.1439 819 LYS A O   
2577 C CB  . LYS A 301 ? 1.0745 1.0182 1.1523 0.0995  -0.1614 -0.1617 819 LYS A CB  
2578 C CG  . LYS A 301 ? 1.1779 1.1229 1.2305 0.1294  -0.1849 -0.1561 819 LYS A CG  
2579 C CD  . LYS A 301 ? 1.2608 1.1312 1.2766 0.1358  -0.1769 -0.1227 819 LYS A CD  
2580 C CE  . LYS A 301 ? 1.3260 1.2020 1.2896 0.1281  -0.1750 -0.1181 819 LYS A CE  
2581 N NZ  . LYS A 301 ? 1.3918 1.2141 1.3128 0.1437  -0.1722 -0.0819 819 LYS A NZ  
2582 N N   . ARG A 302 ? 0.9441 0.9136 1.0524 0.0250  -0.1190 -0.1702 820 ARG A N   
2583 C CA  . ARG A 302 ? 0.9105 0.8530 1.0270 0.0023  -0.0990 -0.1594 820 ARG A CA  
2584 C C   . ARG A 302 ? 0.9297 0.8338 1.0219 -0.0209 -0.0865 -0.1568 820 ARG A C   
2585 O O   . ARG A 302 ? 0.8967 0.7497 0.9846 -0.0249 -0.0698 -0.1443 820 ARG A O   
2586 C CB  . ARG A 302 ? 0.8652 0.8674 1.0078 -0.0125 -0.0985 -0.1654 820 ARG A CB  
2587 C CG  . ARG A 302 ? 0.8405 0.8787 1.0053 0.0124  -0.1077 -0.1738 820 ARG A CG  
2588 C CD  . ARG A 302 ? 0.8352 0.9437 1.0167 -0.0042 -0.1023 -0.1776 820 ARG A CD  
2589 N NE  . ARG A 302 ? 0.8266 0.9891 1.0253 0.0241  -0.1131 -0.1968 820 ARG A NE  
2590 C CZ  . ARG A 302 ? 0.8032 1.0488 1.0138 0.0184  -0.1090 -0.2052 820 ARG A CZ  
2591 N NH1 . ARG A 302 ? 0.8174 1.0972 1.0274 -0.0199 -0.0943 -0.1888 820 ARG A NH1 
2592 N NH2 . ARG A 302 ? 0.7785 1.0724 1.0010 0.0506  -0.1192 -0.2300 820 ARG A NH2 
2593 N N   . ILE A 303 ? 0.9762 0.9074 1.0549 -0.0346 -0.0962 -0.1725 821 ILE A N   
2594 C CA  . ILE A 303 ? 1.0435 0.9346 1.0963 -0.0551 -0.0888 -0.1794 821 ILE A CA  
2595 C C   . ILE A 303 ? 1.0905 0.9328 1.1058 -0.0332 -0.0818 -0.1747 821 ILE A C   
2596 O O   . ILE A 303 ? 1.0902 0.8810 1.0910 -0.0366 -0.0639 -0.1718 821 ILE A O   
2597 C CB  . ILE A 303 ? 1.0995 1.0393 1.1512 -0.0781 -0.1058 -0.2022 821 ILE A CB  
2598 C CG1 . ILE A 303 ? 1.1278 1.1143 1.2182 -0.1103 -0.1047 -0.2009 821 ILE A CG1 
2599 C CG2 . ILE A 303 ? 1.1212 1.0146 1.1378 -0.0930 -0.1045 -0.2188 821 ILE A CG2 
2600 C CD1 . ILE A 303 ? 1.1849 1.1179 1.2764 -0.1458 -0.0917 -0.1953 821 ILE A CD1 
2601 N N   . ARG A 304 ? 1.1166 0.9769 1.1153 -0.0082 -0.0951 -0.1717 822 ARG A N   
2602 C CA  . ARG A 304 ? 1.1410 0.9630 1.0992 0.0106  -0.0867 -0.1598 822 ARG A CA  
2603 C C   . ARG A 304 ? 1.0936 0.8714 1.0653 0.0174  -0.0631 -0.1365 822 ARG A C   
2604 O O   . ARG A 304 ? 1.1383 0.8849 1.0819 0.0231  -0.0447 -0.1283 822 ARG A O   
2605 C CB  . ARG A 304 ? 1.1761 1.0215 1.1165 0.0371  -0.1079 -0.1515 822 ARG A CB  
2606 C CG  . ARG A 304 ? 1.2184 1.1235 1.1529 0.0356  -0.1357 -0.1749 822 ARG A CG  
2607 C CD  . ARG A 304 ? 1.2878 1.1926 1.1755 0.0233  -0.1384 -0.1947 822 ARG A CD  
2608 N NE  . ARG A 304 ? 1.3146 1.2706 1.2220 -0.0035 -0.1558 -0.2258 822 ARG A NE  
2609 C CZ  . ARG A 304 ? 1.3691 1.3318 1.2467 -0.0216 -0.1651 -0.2533 822 ARG A CZ  
2610 N NH1 . ARG A 304 ? 1.4318 1.3562 1.2510 -0.0104 -0.1574 -0.2563 822 ARG A NH1 
2611 N NH2 . ARG A 304 ? 1.3625 1.3744 1.2693 -0.0525 -0.1821 -0.2796 822 ARG A NH2 
2612 N N   . LEU A 305 ? 1.0215 0.8047 1.0367 0.0172  -0.0632 -0.1278 823 LEU A N   
2613 C CA  . LEU A 305 ? 0.9580 0.7088 0.9946 0.0201  -0.0444 -0.1088 823 LEU A CA  
2614 C C   . LEU A 305 ? 1.0118 0.7391 1.0495 0.0070  -0.0246 -0.1131 823 LEU A C   
2615 O O   . LEU A 305 ? 1.0676 0.7688 1.1013 0.0137  -0.0042 -0.1025 823 LEU A O   
2616 C CB  . LEU A 305 ? 0.8596 0.6270 0.9395 0.0235  -0.0547 -0.1053 823 LEU A CB  
2617 C CG  . LEU A 305 ? 0.8285 0.5745 0.9394 0.0218  -0.0401 -0.0906 823 LEU A CG  
2618 C CD1 . LEU A 305 ? 0.8673 0.5837 0.9735 0.0296  -0.0268 -0.0696 823 LEU A CD1 
2619 C CD2 . LEU A 305 ? 0.7841 0.5526 0.9311 0.0252  -0.0552 -0.0952 823 LEU A CD2 
2620 N N   . LEU A 306 ? 1.0034 0.7403 1.0493 -0.0113 -0.0302 -0.1269 824 LEU A N   
2621 C CA  . LEU A 306 ? 1.0535 0.7550 1.1004 -0.0217 -0.0156 -0.1301 824 LEU A CA  
2622 C C   . LEU A 306 ? 1.0628 0.7332 1.0696 -0.0160 -0.0043 -0.1449 824 LEU A C   
2623 O O   . LEU A 306 ? 1.0527 0.6906 1.0596 -0.0062 0.0151  -0.1433 824 LEU A O   
2624 C CB  . LEU A 306 ? 1.0889 0.8015 1.1480 -0.0478 -0.0258 -0.1377 824 LEU A CB  
2625 C CG  . LEU A 306 ? 1.0756 0.7969 1.1691 -0.0537 -0.0245 -0.1190 824 LEU A CG  
2626 C CD1 . LEU A 306 ? 1.0803 0.8258 1.1812 -0.0836 -0.0336 -0.1207 824 LEU A CD1 
2627 C CD2 . LEU A 306 ? 1.1147 0.7876 1.2170 -0.0444 -0.0088 -0.1070 824 LEU A CD2 
2628 N N   . GLN A 307 ? 1.0819 0.7688 1.0536 -0.0186 -0.0171 -0.1621 825 GLN A N   
2629 C CA  . GLN A 307 ? 1.1593 0.8252 1.0829 -0.0101 -0.0084 -0.1804 825 GLN A CA  
2630 C C   . GLN A 307 ? 1.1679 0.8267 1.0788 0.0142  0.0150  -0.1605 825 GLN A C   
2631 O O   . GLN A 307 ? 1.1673 0.8035 1.0565 0.0250  0.0356  -0.1712 825 GLN A O   
2632 C CB  . GLN A 307 ? 1.2181 0.9165 1.1052 -0.0136 -0.0310 -0.1985 825 GLN A CB  
2633 C CG  . GLN A 307 ? 1.2428 0.9671 1.1504 -0.0417 -0.0546 -0.2171 825 GLN A CG  
2634 C CD  . GLN A 307 ? 1.3258 1.0986 1.2062 -0.0406 -0.0803 -0.2332 825 GLN A CD  
2635 O OE1 . GLN A 307 ? 1.3796 1.1722 1.2611 -0.0653 -0.0985 -0.2602 825 GLN A OE1 
2636 N NE2 . GLN A 307 ? 1.3329 1.1250 1.1910 -0.0129 -0.0839 -0.2147 825 GLN A NE2 
2637 N N   . PHE A 308 ? 1.1612 0.8403 1.0878 0.0227  0.0125  -0.1324 826 PHE A N   
2638 C CA  . PHE A 308 ? 1.1714 0.8479 1.0921 0.0382  0.0347  -0.1067 826 PHE A CA  
2639 C C   . PHE A 308 ? 1.1241 0.7865 1.0817 0.0412  0.0596  -0.1007 826 PHE A C   
2640 O O   . PHE A 308 ? 1.1481 0.8119 1.0920 0.0534  0.0861  -0.0947 826 PHE A O   
2641 C CB  . PHE A 308 ? 1.1473 0.8357 1.0878 0.0416  0.0217  -0.0782 826 PHE A CB  
2642 C CG  . PHE A 308 ? 1.1735 0.8566 1.1238 0.0478  0.0435  -0.0449 826 PHE A CG  
2643 C CD1 . PHE A 308 ? 1.2376 0.9247 1.1384 0.0568  0.0602  -0.0295 826 PHE A CD1 
2644 C CD2 . PHE A 308 ? 1.1486 0.8285 1.1578 0.0421  0.0465  -0.0279 826 PHE A CD2 
2645 C CE1 . PHE A 308 ? 1.2734 0.9620 1.1873 0.0566  0.0833  0.0069  826 PHE A CE1 
2646 C CE2 . PHE A 308 ? 1.1777 0.8571 1.2050 0.0408  0.0656  0.0036  826 PHE A CE2 
2647 C CZ  . PHE A 308 ? 1.2363 0.9202 1.2179 0.0463  0.0858  0.0236  826 PHE A CZ  
2648 N N   . VAL A 309 ? 1.0792 0.7356 1.0829 0.0322  0.0517  -0.1017 827 VAL A N   
2649 C CA  . VAL A 309 ? 1.0737 0.7222 1.1173 0.0387  0.0697  -0.0940 827 VAL A CA  
2650 C C   . VAL A 309 ? 1.2029 0.8198 1.2337 0.0435  0.0781  -0.1184 827 VAL A C   
2651 O O   . VAL A 309 ? 1.2783 0.8889 1.3225 0.0607  0.1000  -0.1190 827 VAL A O   
2652 C CB  . VAL A 309 ? 0.9350 0.5952 1.0301 0.0303  0.0543  -0.0801 827 VAL A CB  
2653 C CG1 . VAL A 309 ? 0.8990 0.5608 1.0381 0.0397  0.0688  -0.0695 827 VAL A CG1 
2654 C CG2 . VAL A 309 ? 0.9087 0.5890 1.0153 0.0275  0.0416  -0.0644 827 VAL A CG2 
2655 N N   . THR A 310 ? 1.2249 0.8215 1.2342 0.0287  0.0604  -0.1400 828 THR A N   
2656 C CA  . THR A 310 ? 1.2852 0.8361 1.2856 0.0294  0.0635  -0.1643 828 THR A CA  
2657 C C   . THR A 310 ? 1.3592 0.8950 1.3058 0.0406  0.0729  -0.1968 828 THR A C   
2658 O O   . THR A 310 ? 1.3837 0.8877 1.3242 0.0596  0.0890  -0.2161 828 THR A O   
2659 C CB  . THR A 310 ? 1.2670 0.8011 1.2759 0.0007  0.0398  -0.1696 828 THR A CB  
2660 O OG1 . THR A 310 ? 1.2285 0.7727 1.2820 -0.0043 0.0352  -0.1417 828 THR A OG1 
2661 C CG2 . THR A 310 ? 1.2986 0.7720 1.2916 -0.0049 0.0382  -0.1980 828 THR A CG2 
2662 N N   . GLY A 311 ? 1.3751 0.9364 1.2807 0.0333  0.0618  -0.2052 829 GLY A N   
2663 C CA  . GLY A 311 ? 1.4626 1.0151 1.3091 0.0405  0.0631  -0.2412 829 GLY A CA  
2664 C C   . GLY A 311 ? 1.5334 1.0625 1.3644 0.0147  0.0356  -0.2753 829 GLY A C   
2665 O O   . GLY A 311 ? 1.5942 1.1183 1.3741 0.0176  0.0299  -0.3120 829 GLY A O   
2666 N N   . THR A 312 ? 1.5389 1.0586 1.4125 -0.0123 0.0184  -0.2647 830 THR A N   
2667 C CA  . THR A 312 ? 1.5998 1.1066 1.4715 -0.0461 -0.0074 -0.2902 830 THR A CA  
2668 C C   . THR A 312 ? 1.5600 1.1213 1.4630 -0.0691 -0.0256 -0.2664 830 THR A C   
2669 O O   . THR A 312 ? 1.4838 1.0744 1.4135 -0.0585 -0.0189 -0.2330 830 THR A O   
2670 C CB  . THR A 312 ? 1.6158 1.0499 1.5115 -0.0605 -0.0075 -0.3015 830 THR A CB  
2671 O OG1 . THR A 312 ? 1.5359 0.9732 1.4818 -0.0730 -0.0070 -0.2619 830 THR A OG1 
2672 C CG2 . THR A 312 ? 1.6773 1.0603 1.5571 -0.0251 0.0151  -0.3188 830 THR A CG2 
2673 N N   . SER A 313 ? 1.5924 1.1709 1.4948 -0.1007 -0.0495 -0.2878 831 SER A N   
2674 C CA  . SER A 313 ? 1.5005 1.1463 1.4324 -0.1195 -0.0664 -0.2720 831 SER A CA  
2675 C C   . SER A 313 ? 1.5275 1.1692 1.5081 -0.1504 -0.0667 -0.2521 831 SER A C   
2676 O O   . SER A 313 ? 1.4850 1.1854 1.4945 -0.1543 -0.0705 -0.2303 831 SER A O   
2677 C CB  . SER A 313 ? 1.4341 1.1240 1.3461 -0.1374 -0.0930 -0.3038 831 SER A CB  
2678 O OG  . SER A 313 ? 1.4592 1.1055 1.3272 -0.1364 -0.0963 -0.3426 831 SER A OG  
2679 N N   . ARG A 314 ? 1.5809 1.1541 1.5687 -0.1702 -0.0629 -0.2582 832 ARG A N   
2680 C CA  . ARG A 314 ? 1.5695 1.1360 1.5968 -0.2069 -0.0654 -0.2355 832 ARG A CA  
2681 C C   . ARG A 314 ? 1.5510 1.1021 1.5991 -0.1877 -0.0482 -0.1955 832 ARG A C   
2682 O O   . ARG A 314 ? 1.5746 1.0967 1.6122 -0.1504 -0.0339 -0.1909 832 ARG A O   
2683 C CB  . ARG A 314 ? 1.6466 1.1343 1.6731 -0.2401 -0.0734 -0.2570 832 ARG A CB  
2684 N N   . VAL A 315 ? 1.5114 1.0920 1.5901 -0.2147 -0.0498 -0.1662 833 VAL A N   
2685 C CA  . VAL A 315 ? 1.4765 1.0409 1.5722 -0.2027 -0.0383 -0.1278 833 VAL A CA  
2686 C C   . VAL A 315 ? 1.5920 1.0693 1.6937 -0.2265 -0.0384 -0.1153 833 VAL A C   
2687 O O   . VAL A 315 ? 1.6695 1.1292 1.7766 -0.2700 -0.0487 -0.1244 833 VAL A O   
2688 C CB  . VAL A 315 ? 1.3729 1.0264 1.4900 -0.2119 -0.0392 -0.1022 833 VAL A CB  
2689 C CG1 . VAL A 315 ? 1.2727 1.0033 1.3860 -0.1937 -0.0457 -0.1227 833 VAL A CG1 
2690 C CG2 . VAL A 315 ? 1.4229 1.0987 1.5584 -0.2632 -0.0437 -0.0858 833 VAL A CG2 
2691 N N   . PRO A 316 ? 1.6127 1.0306 1.7165 -0.1994 -0.0295 -0.0956 834 PRO A N   
2692 C CA  . PRO A 316 ? 1.6972 1.0186 1.8062 -0.2161 -0.0326 -0.0821 834 PRO A CA  
2693 C C   . PRO A 316 ? 1.6911 1.0302 1.8185 -0.2585 -0.0364 -0.0366 834 PRO A C   
2694 O O   . PRO A 316 ? 1.6093 1.0327 1.7447 -0.2585 -0.0323 -0.0095 834 PRO A O   
2695 C CB  . PRO A 316 ? 1.7030 0.9783 1.8133 -0.1652 -0.0226 -0.0712 834 PRO A CB  
2696 C CG  . PRO A 316 ? 1.6015 0.9658 1.7177 -0.1380 -0.0152 -0.0601 834 PRO A CG  
2697 C CD  . PRO A 316 ? 1.5514 0.9843 1.6561 -0.1510 -0.0183 -0.0875 834 PRO A CD  
2698 N N   . MET A 317 ? 1.7831 1.0409 1.9161 -0.2959 -0.0442 -0.0289 835 MET A N   
2699 C CA  . MET A 317 ? 1.8019 1.0687 1.9509 -0.3428 -0.0456 0.0220  835 MET A CA  
2700 C C   . MET A 317 ? 1.7614 1.0353 1.9095 -0.3138 -0.0386 0.0742  835 MET A C   
2701 O O   . MET A 317 ? 1.7859 1.0184 1.9284 -0.2626 -0.0365 0.0717  835 MET A O   
2702 C CB  . MET A 317 ? 1.9270 1.0794 2.0837 -0.3864 -0.0568 0.0243  835 MET A CB  
2703 C CG  . MET A 317 ? 1.9757 1.1077 2.1314 -0.4126 -0.0691 -0.0359 835 MET A CG  
2704 S SD  . MET A 317 ? 1.9409 1.1985 2.1207 -0.4793 -0.0741 -0.0400 835 MET A SD  
2705 C CE  . MET A 317 ? 1.9916 1.2144 2.2013 -0.5415 -0.0690 0.0198  835 MET A CE  
2706 N N   . ASN A 318 ? 1.6936 1.0319 1.8475 -0.3466 -0.0349 0.1208  836 ASN A N   
2707 C CA  . ASN A 318 ? 1.6524 1.0204 1.7995 -0.3263 -0.0306 0.1733  836 ASN A CA  
2708 C C   . ASN A 318 ? 1.5195 0.9742 1.6615 -0.2758 -0.0266 0.1557  836 ASN A C   
2709 O O   . ASN A 318 ? 1.4899 0.9745 1.6254 -0.2528 -0.0266 0.1904  836 ASN A O   
2710 C CB  . ASN A 318 ? 1.7510 0.9985 1.8941 -0.3053 -0.0371 0.2075  836 ASN A CB  
2711 C CG  . ASN A 318 ? 1.8956 1.0314 2.0454 -0.3533 -0.0446 0.2230  836 ASN A CG  
2712 O OD1 . ASN A 318 ? 1.9277 1.0912 2.0840 -0.4135 -0.0424 0.2530  836 ASN A OD1 
2713 N ND2 . ASN A 318 ? 1.9830 1.0035 2.1299 -0.3235 -0.0495 0.1972  836 ASN A ND2 
2714 N N   . GLY A 319 ? 1.4313 0.9252 1.5756 -0.2591 -0.0255 0.1046  837 GLY A N   
2715 C CA  . GLY A 319 ? 1.3237 0.8950 1.4674 -0.2193 -0.0234 0.0881  837 GLY A CA  
2716 C C   . GLY A 319 ? 1.2637 0.7881 1.4085 -0.1729 -0.0224 0.0605  837 GLY A C   
2717 O O   . GLY A 319 ? 1.2573 0.7006 1.3995 -0.1678 -0.0218 0.0412  837 GLY A O   
2718 N N   . PHE A 320 ? 1.2233 0.8041 1.3735 -0.1393 -0.0220 0.0570  838 PHE A N   
2719 C CA  . PHE A 320 ? 1.2076 0.7675 1.3655 -0.0990 -0.0182 0.0344  838 PHE A CA  
2720 C C   . PHE A 320 ? 1.2374 0.7443 1.4068 -0.0698 -0.0184 0.0565  838 PHE A C   
2721 O O   . PHE A 320 ? 1.2253 0.7185 1.4070 -0.0368 -0.0123 0.0393  838 PHE A O   
2722 C CB  . PHE A 320 ? 1.1371 0.7767 1.3031 -0.0809 -0.0200 0.0213  838 PHE A CB  
2723 C CG  . PHE A 320 ? 1.1556 0.8316 1.3134 -0.0915 -0.0200 -0.0096 838 PHE A CG  
2724 C CD1 . PHE A 320 ? 1.1833 0.8410 1.3375 -0.0740 -0.0147 -0.0359 838 PHE A CD1 
2725 C CD2 . PHE A 320 ? 1.1374 0.8727 1.2910 -0.1168 -0.0251 -0.0103 838 PHE A CD2 
2726 C CE1 . PHE A 320 ? 1.1653 0.8551 1.3084 -0.0801 -0.0181 -0.0596 838 PHE A CE1 
2727 C CE2 . PHE A 320 ? 1.1256 0.8984 1.2752 -0.1208 -0.0284 -0.0386 838 PHE A CE2 
2728 C CZ  . PHE A 320 ? 1.1445 0.8906 1.2872 -0.1016 -0.0268 -0.0620 838 PHE A CZ  
2729 N N   . ALA A 321 ? 1.2785 0.7604 1.4454 -0.0797 -0.0250 0.0968  839 ALA A N   
2730 C CA  . ALA A 321 ? 1.2898 0.7208 1.4690 -0.0467 -0.0292 0.1206  839 ALA A CA  
2731 C C   . ALA A 321 ? 1.3945 0.7208 1.5752 -0.0357 -0.0252 0.1046  839 ALA A C   
2732 O O   . ALA A 321 ? 1.4727 0.7621 1.6702 0.0049  -0.0259 0.1089  839 ALA A O   
2733 C CB  . ALA A 321 ? 1.2877 0.7230 1.4574 -0.0587 -0.0399 0.1748  839 ALA A CB  
2734 N N   . GLU A 322 ? 1.4202 0.7023 1.5859 -0.0687 -0.0227 0.0826  840 GLU A N   
2735 C CA  . GLU A 322 ? 1.5038 0.6840 1.6664 -0.0597 -0.0213 0.0564  840 GLU A CA  
2736 C C   . GLU A 322 ? 1.4387 0.6337 1.5924 -0.0476 -0.0102 0.0007  840 GLU A C   
2737 O O   . GLU A 322 ? 1.5508 0.6771 1.6910 -0.0536 -0.0103 -0.0328 840 GLU A O   
2738 C CB  . GLU A 322 ? 1.6476 0.7560 1.7997 -0.1086 -0.0305 0.0695  840 GLU A CB  
2739 C CG  . GLU A 322 ? 1.7802 0.8121 1.9381 -0.1068 -0.0410 0.1215  840 GLU A CG  
2740 C CD  . GLU A 322 ? 1.7702 0.8790 1.9274 -0.1135 -0.0441 0.1773  840 GLU A CD  
2741 O OE1 . GLU A 322 ? 1.7379 0.8814 1.9047 -0.0687 -0.0460 0.1920  840 GLU A OE1 
2742 O OE2 . GLU A 322 ? 1.7851 0.9277 1.9325 -0.1636 -0.0448 0.2047  840 GLU A OE2 
2743 N N   . LEU A 323 ? 1.2865 0.5674 1.4449 -0.0316 -0.0022 -0.0091 841 LEU A N   
2744 C CA  . LEU A 323 ? 1.2461 0.5476 1.3908 -0.0212 0.0089  -0.0522 841 LEU A CA  
2745 C C   . LEU A 323 ? 1.3080 0.5623 1.4573 0.0229  0.0215  -0.0747 841 LEU A C   
2746 O O   . LEU A 323 ? 1.2520 0.5017 1.4280 0.0561  0.0239  -0.0553 841 LEU A O   
2747 C CB  . LEU A 323 ? 1.1413 0.5381 1.2935 -0.0172 0.0124  -0.0482 841 LEU A CB  
2748 C CG  . LEU A 323 ? 1.1179 0.5522 1.2525 -0.0142 0.0207  -0.0790 841 LEU A CG  
2749 C CD1 . LEU A 323 ? 0.9971 0.5103 1.1405 -0.0208 0.0158  -0.0681 841 LEU A CD1 
2750 C CD2 . LEU A 323 ? 1.1550 0.5791 1.2941 0.0229  0.0382  -0.0935 841 LEU A CD2 
2751 N N   . TYR A 324 ? 1.4131 0.6391 1.5358 0.0256  0.0287  -0.1180 842 TYR A N   
2752 C CA  . TYR A 324 ? 1.4579 0.6418 1.5782 0.0686  0.0430  -0.1483 842 TYR A CA  
2753 C C   . TYR A 324 ? 1.4693 0.7158 1.5719 0.0867  0.0630  -0.1748 842 TYR A C   
2754 O O   . TYR A 324 ? 1.4166 0.7062 1.4947 0.0615  0.0605  -0.1823 842 TYR A O   
2755 C CB  . TYR A 324 ? 1.4802 0.5625 1.5774 0.0603  0.0337  -0.1825 842 TYR A CB  
2756 C CG  . TYR A 324 ? 1.5397 0.5507 1.6410 0.0770  0.0222  -0.1597 842 TYR A CG  
2757 C CD1 . TYR A 324 ? 1.4909 0.5007 1.6167 0.0623  0.0106  -0.1063 842 TYR A CD1 
2758 C CD2 . TYR A 324 ? 1.6178 0.5615 1.6940 0.1099  0.0240  -0.1918 842 TYR A CD2 
2759 C CE1 . TYR A 324 ? 1.5241 0.4655 1.6484 0.0791  0.0013  -0.0815 842 TYR A CE1 
2760 C CE2 . TYR A 324 ? 1.6782 0.5493 1.7551 0.1280  0.0157  -0.1702 842 TYR A CE2 
2761 C CZ  . TYR A 324 ? 1.6376 0.5070 1.7385 0.1122  0.0042  -0.1133 842 TYR A CZ  
2762 O OH  . TYR A 324 ? 1.6978 0.4931 1.7976 0.1320  -0.0031 -0.0882 842 TYR A OH  
2763 N N   . GLY A 325 ? 1.5330 0.7877 1.6490 0.1320  0.0832  -0.1864 843 GLY A N   
2764 C CA  . GLY A 325 ? 1.5334 0.8450 1.6301 0.1503  0.1071  -0.2081 843 GLY A CA  
2765 C C   . GLY A 325 ? 1.6367 0.9023 1.6948 0.1745  0.1184  -0.2602 843 GLY A C   
2766 O O   . GLY A 325 ? 1.7092 0.9138 1.7330 0.1531  0.1018  -0.2892 843 GLY A O   
2767 N N   . SER A 326 ? 1.6367 0.9362 1.7017 0.2186  0.1466  -0.2754 844 SER A N   
2768 C CA  . SER A 326 ? 1.7316 0.9957 1.7582 0.2507  0.1605  -0.3308 844 SER A CA  
2769 C C   . SER A 326 ? 1.8098 1.0316 1.8714 0.3026  0.1691  -0.3469 844 SER A C   
2770 O O   . SER A 326 ? 1.9275 1.0992 1.9553 0.3302  0.1705  -0.3971 844 SER A O   
2771 C CB  . SER A 326 ? 1.7222 1.0710 1.7137 0.2643  0.1913  -0.3438 844 SER A CB  
2772 O OG  . SER A 326 ? 1.8370 1.1612 1.7826 0.2979  0.2056  -0.4024 844 SER A OG  
2773 N N   . ASN A 327 ? 1.7634 1.0101 1.8874 0.3184  0.1691  -0.3058 845 ASN A N   
2774 C CA  . ASN A 327 ? 1.8285 1.0521 1.9841 0.3697  0.1679  -0.3104 845 ASN A CA  
2775 C C   . ASN A 327 ? 1.7820 0.9576 1.9646 0.3566  0.1333  -0.2642 845 ASN A C   
2776 O O   . ASN A 327 ? 1.7957 0.9949 2.0242 0.3912  0.1319  -0.2405 845 ASN A O   
2777 C CB  . ASN A 327 ? 1.8086 1.1343 2.0150 0.4130  0.2060  -0.3067 845 ASN A CB  
2778 C CG  . ASN A 327 ? 1.8596 1.2340 2.0264 0.4364  0.2431  -0.3524 845 ASN A CG  
2779 O OD1 . ASN A 327 ? 1.9591 1.2747 2.0676 0.4455  0.2381  -0.4018 845 ASN A OD1 
2780 N ND2 . ASN A 327 ? 1.7965 1.2882 1.9876 0.4412  0.2745  -0.3317 845 ASN A ND2 
2781 N N   . GLY A 328 ? 1.7017 0.8164 1.8553 0.3066  0.1064  -0.2496 846 GLY A N   
2782 C CA  . GLY A 328 ? 1.6403 0.7098 1.8083 0.2896  0.0786  -0.2034 846 GLY A CA  
2783 C C   . GLY A 328 ? 1.5106 0.6264 1.6992 0.2428  0.0708  -0.1622 846 GLY A C   
2784 O O   . GLY A 328 ? 1.4896 0.6546 1.6734 0.2174  0.0833  -0.1718 846 GLY A O   
2785 N N   . PRO A 329 ? 1.4291 0.5285 1.6368 0.2335  0.0506  -0.1157 847 PRO A N   
2786 C CA  . PRO A 329 ? 1.3259 0.4700 1.5502 0.1922  0.0419  -0.0784 847 PRO A CA  
2787 C C   . PRO A 329 ? 1.2490 0.4998 1.5103 0.2032  0.0564  -0.0691 847 PRO A C   
2788 O O   . PRO A 329 ? 1.2506 0.5426 1.5498 0.2452  0.0679  -0.0694 847 PRO A O   
2789 C CB  . PRO A 329 ? 1.3552 0.4595 1.5877 0.1913  0.0190  -0.0310 847 PRO A CB  
2790 C CG  . PRO A 329 ? 1.4780 0.4885 1.6821 0.2155  0.0135  -0.0467 847 PRO A CG  
2791 C CD  . PRO A 329 ? 1.5199 0.5490 1.7254 0.2588  0.0340  -0.0961 847 PRO A CD  
2792 N N   . GLN A 330 ? 1.2062 0.5102 1.4514 0.1621  0.0533  -0.0607 848 GLN A N   
2793 C CA  . GLN A 330 ? 1.1252 0.5266 1.3941 0.1612  0.0606  -0.0503 848 GLN A CA  
2794 C C   . GLN A 330 ? 1.0647 0.5025 1.3169 0.1179  0.0469  -0.0355 848 GLN A C   
2795 O O   . GLN A 330 ? 1.0714 0.4956 1.2877 0.0903  0.0470  -0.0529 848 GLN A O   
2796 C CB  . GLN A 330 ? 1.1421 0.5796 1.4053 0.1755  0.0872  -0.0807 848 GLN A CB  
2797 C CG  . GLN A 330 ? 1.1383 0.6658 1.4331 0.1712  0.0941  -0.0653 848 GLN A CG  
2798 C CD  . GLN A 330 ? 1.1740 0.7394 1.5218 0.1859  0.0808  -0.0365 848 GLN A CD  
2799 O OE1 . GLN A 330 ? 1.1271 0.7158 1.4804 0.1638  0.0599  -0.0150 848 GLN A OE1 
2800 N NE2 . GLN A 330 ? 1.2415 0.8191 1.6283 0.2264  0.0915  -0.0386 848 GLN A NE2 
2801 N N   . SER A 331 ? 1.0386 0.5292 1.3171 0.1148  0.0340  -0.0074 849 SER A N   
2802 C CA  . SER A 331 ? 1.0030 0.5349 1.2668 0.0807  0.0220  0.0002  849 SER A CA  
2803 C C   . SER A 331 ? 0.9654 0.5466 1.2303 0.0749  0.0323  -0.0179 849 SER A C   
2804 O O   . SER A 331 ? 1.0072 0.6028 1.2883 0.0941  0.0497  -0.0286 849 SER A O   
2805 C CB  . SER A 331 ? 0.9984 0.5723 1.2831 0.0814  0.0031  0.0306  849 SER A CB  
2806 O OG  . SER A 331 ? 1.1263 0.6801 1.4360 0.1121  -0.0015 0.0495  849 SER A OG  
2807 N N   . PHE A 332 ? 0.8600 0.4685 1.1076 0.0487  0.0216  -0.0190 850 PHE A N   
2808 C CA  . PHE A 332 ? 0.7689 0.4156 1.0162 0.0426  0.0251  -0.0308 850 PHE A CA  
2809 C C   . PHE A 332 ? 0.7409 0.4342 1.0333 0.0551  0.0235  -0.0210 850 PHE A C   
2810 O O   . PHE A 332 ? 0.7550 0.4739 1.0702 0.0577  0.0078  -0.0076 850 PHE A O   
2811 C CB  . PHE A 332 ? 0.7678 0.4345 0.9927 0.0183  0.0099  -0.0348 850 PHE A CB  
2812 C CG  . PHE A 332 ? 0.8586 0.5576 1.0846 0.0158  0.0070  -0.0443 850 PHE A CG  
2813 C CD1 . PHE A 332 ? 0.9395 0.6248 1.1397 0.0146  0.0162  -0.0574 850 PHE A CD1 
2814 C CD2 . PHE A 332 ? 0.8709 0.6105 1.1207 0.0159  -0.0077 -0.0409 850 PHE A CD2 
2815 C CE1 . PHE A 332 ? 0.9496 0.6557 1.1494 0.0142  0.0111  -0.0600 850 PHE A CE1 
2816 C CE2 . PHE A 332 ? 0.9072 0.6624 1.1601 0.0149  -0.0134 -0.0498 850 PHE A CE2 
2817 C CZ  . PHE A 332 ? 0.9245 0.6601 1.1529 0.0144  -0.0039 -0.0560 850 PHE A CZ  
2818 N N   . THR A 333 ? 0.7373 0.4450 1.0428 0.0607  0.0392  -0.0263 851 THR A N   
2819 C CA  . THR A 333 ? 0.7320 0.4832 1.0904 0.0687  0.0413  -0.0167 851 THR A CA  
2820 C C   . THR A 333 ? 0.7054 0.4752 1.0697 0.0542  0.0442  -0.0175 851 THR A C   
2821 O O   . THR A 333 ? 0.7427 0.4941 1.0747 0.0514  0.0599  -0.0217 851 THR A O   
2822 C CB  . THR A 333 ? 0.8073 0.5612 1.1910 0.0936  0.0640  -0.0148 851 THR A CB  
2823 O OG1 . THR A 333 ? 0.9252 0.6616 1.3170 0.1115  0.0543  -0.0086 851 THR A OG1 
2824 C CG2 . THR A 333 ? 0.7953 0.6064 1.2382 0.0956  0.0715  -0.0056 851 THR A CG2 
2825 N N   . VAL A 334 ? 0.6686 0.4715 1.0726 0.0454  0.0270  -0.0134 852 VAL A N   
2826 C CA  . VAL A 334 ? 0.6806 0.4914 1.1008 0.0302  0.0263  -0.0107 852 VAL A CA  
2827 C C   . VAL A 334 ? 0.6796 0.5314 1.1660 0.0276  0.0337  0.0008  852 VAL A C   
2828 O O   . VAL A 334 ? 0.6608 0.5462 1.1893 0.0301  0.0155  -0.0010 852 VAL A O   
2829 C CB  . VAL A 334 ? 0.6726 0.4817 1.0870 0.0193  -0.0040 -0.0224 852 VAL A CB  
2830 C CG1 . VAL A 334 ? 0.6562 0.4567 1.0898 0.0051  -0.0076 -0.0184 852 VAL A CG1 
2831 C CG2 . VAL A 334 ? 0.6508 0.4369 1.0087 0.0212  -0.0101 -0.0336 852 VAL A CG2 
2832 N N   . GLU A 335 ? 0.7452 0.6020 1.2410 0.0212  0.0596  0.0138  853 GLU A N   
2833 C CA  . GLU A 335 ? 0.7934 0.6997 1.3578 0.0135  0.0726  0.0279  853 GLU A CA  
2834 C C   . GLU A 335 ? 0.7918 0.6936 1.3796 -0.0164 0.0700  0.0421  853 GLU A C   
2835 O O   . GLU A 335 ? 0.8133 0.6767 1.3556 -0.0234 0.0787  0.0512  853 GLU A O   
2836 C CB  . GLU A 335 ? 0.8245 0.7553 1.3904 0.0311  0.1121  0.0358  853 GLU A CB  
2837 C CG  . GLU A 335 ? 0.8701 0.8721 1.5186 0.0283  0.1242  0.0475  853 GLU A CG  
2838 C CD  . GLU A 335 ? 0.9594 0.9985 1.6126 0.0441  0.1689  0.0556  853 GLU A CD  
2839 O OE1 . GLU A 335 ? 1.0339 1.0436 1.6257 0.0459  0.1920  0.0582  853 GLU A OE1 
2840 O OE2 . GLU A 335 ? 0.9531 1.0576 1.6706 0.0585  0.1801  0.0571  853 GLU A OE2 
2841 N N   . GLN A 336 ? 0.7903 0.7306 1.4514 -0.0343 0.0557  0.0449  854 GLN A N   
2842 C CA  . GLN A 336 ? 0.8157 0.7548 1.5179 -0.0682 0.0569  0.0634  854 GLN A CA  
2843 C C   . GLN A 336 ? 0.8338 0.7948 1.5355 -0.0741 0.1025  0.0938  854 GLN A C   
2844 O O   . GLN A 336 ? 0.8920 0.9189 1.6398 -0.0681 0.1275  0.1010  854 GLN A O   
2845 C CB  . GLN A 336 ? 0.8770 0.8663 1.6682 -0.0883 0.0348  0.0579  854 GLN A CB  
2846 C CG  . GLN A 336 ? 0.9925 0.9591 1.7891 -0.0937 -0.0125 0.0295  854 GLN A CG  
2847 C CD  . GLN A 336 ? 1.1478 1.1399 2.0287 -0.1293 -0.0342 0.0274  854 GLN A CD  
2848 O OE1 . GLN A 336 ? 1.3589 1.3293 2.2676 -0.1616 -0.0237 0.0498  854 GLN A OE1 
2849 N NE2 . GLN A 336 ? 1.0431 1.0834 1.9665 -0.1256 -0.0654 0.0027  854 GLN A NE2 
2850 N N   . TRP A 337 ? 0.8207 0.7344 1.4711 -0.0832 0.1138  0.1122  855 TRP A N   
2851 C CA  . TRP A 337 ? 0.8962 0.8396 1.5437 -0.0919 0.1582  0.1455  855 TRP A CA  
2852 C C   . TRP A 337 ? 0.9693 0.8641 1.6019 -0.1221 0.1561  0.1784  855 TRP A C   
2853 O O   . TRP A 337 ? 0.9886 0.8155 1.5640 -0.1152 0.1329  0.1726  855 TRP A O   
2854 C CB  . TRP A 337 ? 0.9516 0.8966 1.5254 -0.0573 0.1869  0.1367  855 TRP A CB  
2855 C CG  . TRP A 337 ? 1.0521 1.0120 1.5922 -0.0641 0.2270  0.1689  855 TRP A CG  
2856 C CD1 . TRP A 337 ? 1.0759 1.1102 1.6500 -0.0672 0.2705  0.1892  855 TRP A CD1 
2857 C CD2 . TRP A 337 ? 1.1268 1.0345 1.5912 -0.0677 0.2277  0.1875  855 TRP A CD2 
2858 N NE1 . TRP A 337 ? 1.1481 1.1797 1.6649 -0.0738 0.3009  0.2206  855 TRP A NE1 
2859 C CE2 . TRP A 337 ? 1.1714 1.1226 1.6190 -0.0739 0.2731  0.2213  855 TRP A CE2 
2860 C CE3 . TRP A 337 ? 1.1346 0.9704 1.5440 -0.0638 0.1940  0.1791  855 TRP A CE3 
2861 C CZ2 . TRP A 337 ? 1.2109 1.1308 1.5823 -0.0764 0.2835  0.2497  855 TRP A CZ2 
2862 C CZ3 . TRP A 337 ? 1.1630 0.9683 1.5044 -0.0642 0.2023  0.2049  855 TRP A CZ3 
2863 C CH2 . TRP A 337 ? 1.2030 1.0475 1.5225 -0.0706 0.2455  0.2413  855 TRP A CH2 
2864 N N   . GLY A 338 ? 0.9859 0.9175 1.6746 -0.1554 0.1790  0.2146  856 GLY A N   
2865 C CA  . GLY A 338 ? 1.0761 0.9622 1.7470 -0.1848 0.1852  0.2580  856 GLY A CA  
2866 C C   . GLY A 338 ? 1.1164 0.9438 1.8379 -0.2184 0.1434  0.2606  856 GLY A C   
2867 O O   . GLY A 338 ? 1.0865 0.9270 1.8743 -0.2285 0.1132  0.2311  856 GLY A O   
2868 N N   . THR A 339 ? 1.1909 0.9487 1.8750 -0.2335 0.1400  0.2962  857 THR A N   
2869 C CA  . THR A 339 ? 1.2329 0.9155 1.9551 -0.2681 0.1073  0.3131  857 THR A CA  
2870 C C   . THR A 339 ? 1.2800 0.8683 1.9319 -0.2390 0.0701  0.2960  857 THR A C   
2871 O O   . THR A 339 ? 1.2518 0.8347 1.8190 -0.2043 0.0815  0.2962  857 THR A O   
2872 C CB  . THR A 339 ? 1.2903 0.9718 2.0316 -0.3120 0.1402  0.3835  857 THR A CB  
2873 O OG1 . THR A 339 ? 1.3571 0.9406 2.1052 -0.3365 0.1041  0.4000  857 THR A OG1 
2874 C CG2 . THR A 339 ? 1.3226 1.0188 1.9686 -0.2885 0.1813  0.4193  857 THR A CG2 
2875 N N   . PRO A 340 ? 1.3570 0.8746 2.0444 -0.2505 0.0241  0.2768  858 PRO A N   
2876 C CA  . PRO A 340 ? 1.3713 0.8073 1.9999 -0.2168 -0.0131 0.2548  858 PRO A CA  
2877 C C   . PRO A 340 ? 1.4061 0.7931 1.9566 -0.2025 -0.0007 0.3012  858 PRO A C   
2878 O O   . PRO A 340 ? 1.3971 0.7481 1.8874 -0.1631 -0.0235 0.2793  858 PRO A O   
2879 C CB  . PRO A 340 ? 1.4284 0.8201 2.0913 -0.2319 -0.0547 0.2277  858 PRO A CB  
2880 C CG  . PRO A 340 ? 1.3869 0.8499 2.1298 -0.2577 -0.0528 0.2049  858 PRO A CG  
2881 C CD  . PRO A 340 ? 1.3749 0.9043 2.1454 -0.2833 -0.0004 0.2552  858 PRO A CD  
2882 N N   . GLU A 341 ? 1.4515 0.8431 2.0001 -0.2326 0.0341  0.3659  859 GLU A N   
2883 C CA  . GLU A 341 ? 1.5335 0.8764 2.0010 -0.2170 0.0409  0.4134  859 GLU A CA  
2884 C C   . GLU A 341 ? 1.4963 0.9013 1.8784 -0.1786 0.0683  0.4036  859 GLU A C   
2885 O O   . GLU A 341 ? 1.5700 0.9432 1.8738 -0.1536 0.0643  0.4261  859 GLU A O   
2886 C CB  . GLU A 341 ? 1.6586 0.9894 2.1330 -0.2602 0.0668  0.4839  859 GLU A CB  
2887 C CG  . GLU A 341 ? 1.7797 1.0663 2.3100 -0.2945 0.0385  0.4724  859 GLU A CG  
2888 C CD  . GLU A 341 ? 1.7736 1.1339 2.3963 -0.3287 0.0476  0.4458  859 GLU A CD  
2889 O OE1 . GLU A 341 ? 1.7748 1.1146 2.4424 -0.3302 0.0088  0.3934  859 GLU A OE1 
2890 O OE2 . GLU A 341 ? 1.7685 1.2143 2.4182 -0.3514 0.0942  0.4771  859 GLU A OE2 
2891 N N   . LYS A 342 ? 1.3883 0.8778 1.7838 -0.1712 0.0919  0.3681  860 LYS A N   
2892 C CA  . LYS A 342 ? 1.3173 0.8532 1.6331 -0.1358 0.1135  0.3529  860 LYS A CA  
2893 C C   . LYS A 342 ? 1.1823 0.7104 1.4738 -0.0991 0.0805  0.2908  860 LYS A C   
2894 O O   . LYS A 342 ? 1.0872 0.6049 1.4299 -0.0995 0.0517  0.2519  860 LYS A O   
2895 C CB  . LYS A 342 ? 1.3143 0.9427 1.6454 -0.1425 0.1621  0.3534  860 LYS A CB  
2896 C CG  . LYS A 342 ? 1.3531 1.0162 1.5934 -0.1089 0.1858  0.3443  860 LYS A CG  
2897 C CD  . LYS A 342 ? 1.4403 1.1417 1.6438 -0.1216 0.2319  0.3994  860 LYS A CD  
2898 C CE  . LYS A 342 ? 1.4625 1.1703 1.5534 -0.0874 0.2403  0.3970  860 LYS A CE  
2899 N NZ  . LYS A 342 ? 1.4671 1.1037 1.5040 -0.0676 0.1954  0.3940  860 LYS A NZ  
2900 N N   . LEU A 343 ? 1.1881 0.7266 1.3996 -0.0693 0.0852  0.2829  861 LEU A N   
2901 C CA  . LEU A 343 ? 1.1535 0.7028 1.3266 -0.0372 0.0661  0.2323  861 LEU A CA  
2902 C C   . LEU A 343 ? 1.1210 0.7300 1.3127 -0.0345 0.0883  0.1974  861 LEU A C   
2903 O O   . LEU A 343 ? 1.1326 0.7845 1.3386 -0.0458 0.1256  0.2143  861 LEU A O   
2904 C CB  . LEU A 343 ? 1.2282 0.7744 1.3112 -0.0139 0.0675  0.2448  861 LEU A CB  
2905 C CG  . LEU A 343 ? 1.3319 0.8139 1.3953 -0.0095 0.0399  0.2819  861 LEU A CG  
2906 C CD1 . LEU A 343 ? 1.3454 0.8287 1.3204 0.0194  0.0308  0.2898  861 LEU A CD1 
2907 C CD2 . LEU A 343 ? 1.3387 0.7768 1.4527 -0.0037 -0.0022 0.2522  861 LEU A CD2 
2908 N N   . PRO A 344 ? 1.1182 0.7332 1.3118 -0.0183 0.0667  0.1506  862 PRO A N   
2909 C CA  . PRO A 344 ? 1.1155 0.7752 1.3239 -0.0135 0.0845  0.1217  862 PRO A CA  
2910 C C   . PRO A 344 ? 1.1565 0.8407 1.3026 0.0008  0.1138  0.1199  862 PRO A C   
2911 O O   . PRO A 344 ? 1.1915 0.8621 1.2721 0.0129  0.1076  0.1217  862 PRO A O   
2912 C CB  . PRO A 344 ? 1.0757 0.7280 1.2880 -0.0015 0.0518  0.0805  862 PRO A CB  
2913 C CG  . PRO A 344 ? 1.0932 0.7053 1.3133 -0.0012 0.0180  0.0841  862 PRO A CG  
2914 C CD  . PRO A 344 ? 1.1401 0.7255 1.3217 -0.0023 0.0266  0.1239  862 PRO A CD  
2915 N N   . ARG A 345 ? 1.1579 0.8812 1.3256 0.0021  0.1437  0.1132  863 ARG A N   
2916 C CA  . ARG A 345 ? 1.1640 0.9089 1.2785 0.0210  0.1687  0.0955  863 ARG A CA  
2917 C C   . ARG A 345 ? 1.1494 0.8964 1.2828 0.0330  0.1612  0.0549  863 ARG A C   
2918 O O   . ARG A 345 ? 1.0974 0.8503 1.2927 0.0269  0.1503  0.0503  863 ARG A O   
2919 C CB  . ARG A 345 ? 1.1723 0.9630 1.2913 0.0193  0.2139  0.1207  863 ARG A CB  
2920 C CG  . ARG A 345 ? 1.1430 0.9734 1.3457 0.0128  0.2299  0.1213  863 ARG A CG  
2921 C CD  . ARG A 345 ? 1.2046 1.0968 1.4145 0.0143  0.2785  0.1427  863 ARG A CD  
2922 N NE  . ARG A 345 ? 1.1849 1.1252 1.4647 0.0238  0.2938  0.1262  863 ARG A NE  
2923 C CZ  . ARG A 345 ? 1.2333 1.2455 1.5492 0.0252  0.3353  0.1419  863 ARG A CZ  
2924 N NH1 . ARG A 345 ? 1.3037 1.3484 1.5883 0.0137  0.3688  0.1777  863 ARG A NH1 
2925 N NH2 . ARG A 345 ? 1.2232 1.2809 1.6070 0.0395  0.3435  0.1239  863 ARG A NH2 
2926 N N   . ALA A 346 ? 1.2077 0.9469 1.2858 0.0492  0.1640  0.0261  864 ALA A N   
2927 C CA  . ALA A 346 ? 1.1879 0.9165 1.2771 0.0592  0.1572  -0.0086 864 ALA A CA  
2928 C C   . ALA A 346 ? 1.2232 0.9655 1.2882 0.0799  0.1887  -0.0273 864 ALA A C   
2929 O O   . ALA A 346 ? 1.2668 1.0210 1.2757 0.0880  0.2072  -0.0274 864 ALA A O   
2930 C CB  . ALA A 346 ? 1.2019 0.9002 1.2550 0.0560  0.1258  -0.0328 864 ALA A CB  
2931 N N   . HIS A 347 ? 1.2302 0.9721 1.3351 0.0922  0.1939  -0.0436 865 HIS A N   
2932 C CA  . HIS A 347 ? 1.2723 1.0197 1.3607 0.1192  0.2204  -0.0694 865 HIS A CA  
2933 C C   . HIS A 347 ? 1.2507 0.9426 1.3124 0.1256  0.1994  -0.1066 865 HIS A C   
2934 O O   . HIS A 347 ? 1.1524 0.8200 1.2522 0.1206  0.1789  -0.1067 865 HIS A O   
2935 C CB  . HIS A 347 ? 1.2900 1.0790 1.4489 0.1336  0.2423  -0.0591 865 HIS A CB  
2936 C CG  . HIS A 347 ? 1.3482 1.2016 1.5188 0.1340  0.2791  -0.0339 865 HIS A CG  
2937 N ND1 . HIS A 347 ? 1.3178 1.2092 1.5462 0.1101  0.2811  0.0050  865 HIS A ND1 
2938 C CD2 . HIS A 347 ? 1.4195 1.3090 1.5506 0.1528  0.3162  -0.0413 865 HIS A CD2 
2939 C CE1 . HIS A 347 ? 1.3627 1.3110 1.5911 0.1102  0.3192  0.0259  865 HIS A CE1 
2940 N NE2 . HIS A 347 ? 1.4177 1.3708 1.5847 0.1377  0.3428  -0.0010 865 HIS A NE2 
2941 N N   . THR A 348 ? 1.3460 1.0193 1.3408 0.1344  0.2037  -0.1369 866 THR A N   
2942 C CA  . THR A 348 ? 1.3593 0.9756 1.3251 0.1306  0.1796  -0.1729 866 THR A CA  
2943 C C   . THR A 348 ? 1.2961 0.8741 1.3035 0.1456  0.1779  -0.1872 866 THR A C   
2944 O O   . THR A 348 ? 1.2467 0.7855 1.2730 0.1288  0.1519  -0.1854 866 THR A O   
2945 C CB  . THR A 348 ? 1.4669 1.0763 1.3574 0.1423  0.1874  -0.2101 866 THR A CB  
2946 O OG1 . THR A 348 ? 1.5303 1.1804 1.4096 0.1715  0.2261  -0.2131 866 THR A OG1 
2947 C CG2 . THR A 348 ? 1.4722 1.0996 1.3139 0.1227  0.1704  -0.2000 866 THR A CG2 
2948 N N   . CYS A 349 ? 1.3042 0.8967 1.3265 0.1792  0.2062  -0.1988 867 CYS A N   
2949 C CA  . CYS A 349 ? 1.3087 0.8517 1.3561 0.2036  0.2035  -0.2216 867 CYS A CA  
2950 C C   . CYS A 349 ? 1.2240 0.7615 1.3380 0.1976  0.1865  -0.1892 867 CYS A C   
2951 O O   . CYS A 349 ? 1.2006 0.6780 1.3280 0.2050  0.1702  -0.1978 867 CYS A O   
2952 C CB  . CYS A 349 ? 1.3701 0.9433 1.4203 0.2484  0.2394  -0.2442 867 CYS A CB  
2953 S SG  . CYS A 349 ? 1.4925 1.0846 1.4533 0.2609  0.2622  -0.2847 867 CYS A SG  
2954 N N   . PHE A 350 ? 1.1509 0.7474 1.3053 0.1841  0.1880  -0.1517 868 PHE A N   
2955 C CA  . PHE A 350 ? 1.0973 0.7016 1.3119 0.1809  0.1709  -0.1239 868 PHE A CA  
2956 C C   . PHE A 350 ? 1.0323 0.6357 1.2452 0.1434  0.1427  -0.1026 868 PHE A C   
2957 O O   . PHE A 350 ? 1.0116 0.6336 1.2683 0.1385  0.1275  -0.0796 868 PHE A O   
2958 C CB  . PHE A 350 ? 1.0910 0.7697 1.3659 0.1975  0.1914  -0.1039 868 PHE A CB  
2959 C CG  . PHE A 350 ? 1.1626 0.8663 1.4407 0.2360  0.2257  -0.1254 868 PHE A CG  
2960 C CD1 . PHE A 350 ? 1.2253 0.8981 1.5234 0.2753  0.2267  -0.1449 868 PHE A CD1 
2961 C CD2 . PHE A 350 ? 1.1670 0.9263 1.4267 0.2354  0.2575  -0.1249 868 PHE A CD2 
2962 C CE1 . PHE A 350 ? 1.3193 1.0201 1.6210 0.3172  0.2591  -0.1711 868 PHE A CE1 
2963 C CE2 . PHE A 350 ? 1.2357 1.0313 1.4960 0.2732  0.2930  -0.1467 868 PHE A CE2 
2964 C CZ  . PHE A 350 ? 1.3201 1.0891 1.6031 0.3162  0.2941  -0.1734 868 PHE A CZ  
2965 N N   . ASN A 351 ? 1.0373 0.6267 1.2006 0.1202  0.1346  -0.1121 869 ASN A N   
2966 C CA  . ASN A 351 ? 0.9979 0.5896 1.1581 0.0898  0.1082  -0.0985 869 ASN A CA  
2967 C C   . ASN A 351 ? 0.9331 0.5754 1.1378 0.0834  0.1044  -0.0713 869 ASN A C   
2968 O O   . ASN A 351 ? 0.8318 0.4823 1.0581 0.0706  0.0829  -0.0591 869 ASN A O   
2969 C CB  . ASN A 351 ? 1.0396 0.5883 1.2032 0.0804  0.0875  -0.0991 869 ASN A CB  
2970 C CG  . ASN A 351 ? 1.1580 0.6480 1.2804 0.0782  0.0864  -0.1285 869 ASN A CG  
2971 O OD1 . ASN A 351 ? 1.2522 0.7423 1.3327 0.0724  0.0902  -0.1505 869 ASN A OD1 
2972 N ND2 . ASN A 351 ? 1.1606 0.5980 1.2949 0.0874  0.0817  -0.1307 869 ASN A ND2 
2973 N N   . ARG A 352 ? 1.0060 0.6844 1.2246 0.0914  0.1260  -0.0627 870 ARG A N   
2974 C CA  . ARG A 352 ? 0.9807 0.7039 1.2503 0.0831  0.1242  -0.0390 870 ARG A CA  
2975 C C   . ARG A 352 ? 0.9422 0.6728 1.1894 0.0648  0.1221  -0.0284 870 ARG A C   
2976 O O   . ARG A 352 ? 0.9476 0.6739 1.1506 0.0678  0.1390  -0.0312 870 ARG A O   
2977 C CB  . ARG A 352 ? 0.9859 0.7505 1.3017 0.1017  0.1507  -0.0312 870 ARG A CB  
2978 C CG  . ARG A 352 ? 0.9286 0.7419 1.3120 0.0895  0.1438  -0.0093 870 ARG A CG  
2979 C CD  . ARG A 352 ? 0.9163 0.7850 1.3528 0.1066  0.1717  -0.0022 870 ARG A CD  
2980 N NE  . ARG A 352 ? 0.9708 0.8587 1.3807 0.1089  0.2076  0.0009  870 ARG A NE  
2981 C CZ  . ARG A 352 ? 1.0591 0.9802 1.4770 0.1367  0.2405  -0.0082 870 ARG A CZ  
2982 N NH1 . ARG A 352 ? 1.0727 1.0045 1.5294 0.1669  0.2394  -0.0210 870 ARG A NH1 
2983 N NH2 . ARG A 352 ? 1.1297 1.0762 1.5148 0.1376  0.2743  -0.0040 870 ARG A NH2 
2984 N N   . LEU A 353 ? 0.9316 0.6716 1.2063 0.0488  0.0997  -0.0173 871 LEU A N   
2985 C CA  . LEU A 353 ? 0.9339 0.6716 1.1967 0.0344  0.0922  -0.0051 871 LEU A CA  
2986 C C   . LEU A 353 ? 0.9548 0.7212 1.2768 0.0238  0.0983  0.0169  871 LEU A C   
2987 O O   . LEU A 353 ? 0.9378 0.7193 1.3090 0.0177  0.0796  0.0155  871 LEU A O   
2988 C CB  . LEU A 353 ? 0.8740 0.5963 1.1238 0.0268  0.0594  -0.0161 871 LEU A CB  
2989 C CG  . LEU A 353 ? 0.8826 0.5928 1.1170 0.0197  0.0436  -0.0093 871 LEU A CG  
2990 C CD1 . LEU A 353 ? 0.8570 0.5730 1.1446 0.0095  0.0300  0.0015  871 LEU A CD1 
2991 C CD2 . LEU A 353 ? 0.9248 0.6245 1.1159 0.0224  0.0623  0.0050  871 LEU A CD2 
2992 N N   . ASP A 354 ? 0.9636 0.7420 1.2808 0.0195  0.1243  0.0374  872 ASP A N   
2993 C CA  . ASP A 354 ? 0.9801 0.7875 1.3579 0.0012  0.1326  0.0630  872 ASP A CA  
2994 C C   . ASP A 354 ? 0.9620 0.7352 1.3418 -0.0181 0.1058  0.0744  872 ASP A C   
2995 O O   . ASP A 354 ? 0.9965 0.7428 1.3326 -0.0216 0.1096  0.0915  872 ASP A O   
2996 C CB  . ASP A 354 ? 1.0687 0.9090 1.4397 0.0019  0.1749  0.0850  872 ASP A CB  
2997 C CG  . ASP A 354 ? 1.0950 0.9704 1.4707 0.0280  0.2009  0.0673  872 ASP A CG  
2998 O OD1 . ASP A 354 ? 1.0672 0.9625 1.4946 0.0363  0.1908  0.0551  872 ASP A OD1 
2999 O OD2 . ASP A 354 ? 1.1374 1.0202 1.4630 0.0433  0.2296  0.0643  872 ASP A OD2 
3000 N N   . LEU A 355 ? 0.9164 0.6893 1.3446 -0.0274 0.0763  0.0632  873 LEU A N   
3001 C CA  . LEU A 355 ? 0.9774 0.7114 1.4096 -0.0390 0.0450  0.0623  873 LEU A CA  
3002 C C   . LEU A 355 ? 0.9386 0.6767 1.4377 -0.0672 0.0426  0.0831  873 LEU A C   
3003 O O   . LEU A 355 ? 0.9296 0.7079 1.4912 -0.0764 0.0384  0.0756  873 LEU A O   
3004 C CB  . LEU A 355 ? 1.0192 0.7509 1.4522 -0.0284 0.0112  0.0280  873 LEU A CB  
3005 C CG  . LEU A 355 ? 1.0940 0.7893 1.5276 -0.0307 -0.0235 0.0150  873 LEU A CG  
3006 C CD1 . LEU A 355 ? 1.0970 0.7546 1.4710 -0.0190 -0.0250 0.0214  873 LEU A CD1 
3007 C CD2 . LEU A 355 ? 1.0786 0.7939 1.5189 -0.0200 -0.0511 -0.0200 873 LEU A CD2 
3008 N N   . PRO A 356 ? 0.9216 0.6195 1.4131 -0.0830 0.0429  0.1109  874 PRO A N   
3009 C CA  . PRO A 356 ? 0.9021 0.5924 1.4626 -0.1169 0.0360  0.1312  874 PRO A CA  
3010 C C   . PRO A 356 ? 0.8490 0.5166 1.4490 -0.1206 -0.0096 0.0959  874 PRO A C   
3011 O O   . PRO A 356 ? 0.8161 0.4593 1.3768 -0.0962 -0.0352 0.0646  874 PRO A O   
3012 C CB  . PRO A 356 ? 0.9999 0.6356 1.5256 -0.1281 0.0435  0.1724  874 PRO A CB  
3013 C CG  . PRO A 356 ? 1.0086 0.6513 1.4499 -0.1001 0.0663  0.1772  874 PRO A CG  
3014 C CD  . PRO A 356 ? 0.9465 0.6055 1.3658 -0.0720 0.0504  0.1298  874 PRO A CD  
3015 N N   . PRO A 357 ? 0.8708 0.5525 1.5489 -0.1508 -0.0211 0.0969  875 PRO A N   
3016 C CA  . PRO A 357 ? 0.9132 0.5732 1.6257 -0.1537 -0.0676 0.0568  875 PRO A CA  
3017 C C   . PRO A 357 ? 1.0037 0.5741 1.7043 -0.1590 -0.0948 0.0582  875 PRO A C   
3018 O O   . PRO A 357 ? 1.0658 0.6000 1.8085 -0.1928 -0.0973 0.0848  875 PRO A O   
3019 C CB  . PRO A 357 ? 0.9173 0.6287 1.7216 -0.1878 -0.0701 0.0584  875 PRO A CB  
3020 C CG  . PRO A 357 ? 0.9339 0.6950 1.7554 -0.2029 -0.0209 0.1041  875 PRO A CG  
3021 C CD  . PRO A 357 ? 0.9377 0.6614 1.6789 -0.1856 0.0071  0.1328  875 PRO A CD  
3022 N N   . TYR A 358 ? 0.9940 0.5312 1.6377 -0.1246 -0.1156 0.0302  876 TYR A N   
3023 C CA  . TYR A 358 ? 1.0469 0.5064 1.6648 -0.1157 -0.1401 0.0299  876 TYR A CA  
3024 C C   . TYR A 358 ? 1.0506 0.4992 1.6959 -0.1162 -0.1796 -0.0139 876 TYR A C   
3025 O O   . TYR A 358 ? 0.9639 0.4569 1.6279 -0.1071 -0.1975 -0.0575 876 TYR A O   
3026 C CB  . TYR A 358 ? 1.0071 0.4506 1.5558 -0.0749 -0.1437 0.0180  876 TYR A CB  
3027 C CG  . TYR A 358 ? 1.0037 0.4621 1.5001 -0.0709 -0.1055 0.0607  876 TYR A CG  
3028 C CD1 . TYR A 358 ? 1.0820 0.5035 1.5766 -0.0922 -0.0865 0.1147  876 TYR A CD1 
3029 C CD2 . TYR A 358 ? 0.9249 0.4347 1.3727 -0.0478 -0.0886 0.0473  876 TYR A CD2 
3030 C CE1 . TYR A 358 ? 1.1007 0.5432 1.5403 -0.0860 -0.0519 0.1499  876 TYR A CE1 
3031 C CE2 . TYR A 358 ? 0.9313 0.4538 1.3295 -0.0434 -0.0569 0.0782  876 TYR A CE2 
3032 C CZ  . TYR A 358 ? 0.9856 0.4782 1.3770 -0.0603 -0.0385 0.1274  876 TYR A CZ  
3033 O OH  . TYR A 358 ? 1.0114 0.5236 1.3458 -0.0532 -0.0074 0.1544  876 TYR A OH  
3034 N N   . GLU A 359 ? 1.1667 0.5531 1.8124 -0.1261 -0.1936 -0.0015 877 GLU A N   
3035 C CA  . GLU A 359 ? 1.2374 0.6019 1.9139 -0.1307 -0.2297 -0.0398 877 GLU A CA  
3036 C C   . GLU A 359 ? 1.2428 0.5813 1.8789 -0.0866 -0.2603 -0.0856 877 GLU A C   
3037 O O   . GLU A 359 ? 1.3006 0.6144 1.9566 -0.0843 -0.2913 -0.1211 877 GLU A O   
3038 C CB  . GLU A 359 ? 1.3547 0.6590 2.0580 -0.1669 -0.2289 -0.0026 877 GLU A CB  
3039 C CG  . GLU A 359 ? 1.3792 0.7245 2.1466 -0.2169 -0.2086 0.0269  877 GLU A CG  
3040 C CD  . GLU A 359 ? 1.5065 0.8279 2.3288 -0.2483 -0.2357 0.0084  877 GLU A CD  
3041 O OE1 . GLU A 359 ? 1.5993 0.8534 2.4050 -0.2334 -0.2663 -0.0171 877 GLU A OE1 
3042 O OE2 . GLU A 359 ? 1.5301 0.9019 2.4151 -0.2874 -0.2269 0.0182  877 GLU A OE2 
3043 N N   . SER A 360 ? 1.1585 0.5059 1.7417 -0.0515 -0.2524 -0.0874 878 SER A N   
3044 C CA  . SER A 360 ? 1.1928 0.5313 1.7430 -0.0079 -0.2785 -0.1306 878 SER A CA  
3045 C C   . SER A 360 ? 1.1438 0.5264 1.6501 0.0217  -0.2647 -0.1356 878 SER A C   
3046 O O   . SER A 360 ? 1.0242 0.4126 1.5134 0.0124  -0.2367 -0.0963 878 SER A O   
3047 C CB  . SER A 360 ? 1.3252 0.5821 1.8587 0.0038  -0.2926 -0.1148 878 SER A CB  
3048 O OG  . SER A 360 ? 1.3706 0.6300 1.8714 0.0517  -0.3127 -0.1517 878 SER A OG  
3049 N N   . PHE A 361 ? 1.1242 0.5405 1.6137 0.0570  -0.2846 -0.1858 879 PHE A N   
3050 C CA  . PHE A 361 ? 1.1200 0.5816 1.5716 0.0839  -0.2738 -0.1943 879 PHE A CA  
3051 C C   . PHE A 361 ? 1.1205 0.5431 1.5359 0.1017  -0.2674 -0.1620 879 PHE A C   
3052 O O   . PHE A 361 ? 1.0561 0.4940 1.4475 0.1016  -0.2467 -0.1375 879 PHE A O   
3053 C CB  . PHE A 361 ? 1.1367 0.6490 1.5798 0.1182  -0.2956 -0.2545 879 PHE A CB  
3054 C CG  . PHE A 361 ? 1.1006 0.6545 1.5072 0.1496  -0.2886 -0.2648 879 PHE A CG  
3055 C CD1 . PHE A 361 ? 1.1428 0.6872 1.5298 0.1864  -0.3037 -0.2781 879 PHE A CD1 
3056 C CD2 . PHE A 361 ? 1.0326 0.6451 1.4234 0.1396  -0.2644 -0.2561 879 PHE A CD2 
3057 C CE1 . PHE A 361 ? 1.1270 0.7210 1.4883 0.2147  -0.2985 -0.2892 879 PHE A CE1 
3058 C CE2 . PHE A 361 ? 0.9994 0.6682 1.3538 0.1585  -0.2529 -0.2580 879 PHE A CE2 
3059 C CZ  . PHE A 361 ? 1.0774 0.7396 1.4208 0.1959  -0.2709 -0.2770 879 PHE A CZ  
3060 N N   . GLU A 362 ? 1.1699 0.5400 1.5807 0.1198  -0.2881 -0.1634 880 GLU A N   
3061 C CA  . GLU A 362 ? 1.1799 0.5130 1.5560 0.1426  -0.2883 -0.1332 880 GLU A CA  
3062 C C   . GLU A 362 ? 1.1781 0.4748 1.5427 0.1133  -0.2623 -0.0694 880 GLU A C   
3063 O O   . GLU A 362 ? 1.1914 0.4877 1.5199 0.1291  -0.2549 -0.0441 880 GLU A O   
3064 C CB  . GLU A 362 ? 1.2756 0.5505 1.6543 0.1661  -0.3162 -0.1431 880 GLU A CB  
3065 C CG  . GLU A 362 ? 1.3203 0.6089 1.6700 0.2173  -0.3328 -0.1596 880 GLU A CG  
3066 C CD  . GLU A 362 ? 1.2478 0.6275 1.5966 0.2450  -0.3386 -0.2170 880 GLU A CD  
3067 O OE1 . GLU A 362 ? 1.2523 0.6567 1.6229 0.2487  -0.3517 -0.2629 880 GLU A OE1 
3068 O OE2 . GLU A 362 ? 1.1540 0.5837 1.4800 0.2632  -0.3307 -0.2162 880 GLU A OE2 
3069 N N   . GLU A 363 ? 1.1759 0.4492 1.5715 0.0713  -0.2492 -0.0439 881 GLU A N   
3070 C CA  . GLU A 363 ? 1.1987 0.4536 1.5866 0.0417  -0.2194 0.0162  881 GLU A CA  
3071 C C   . GLU A 363 ? 1.1139 0.4282 1.4915 0.0383  -0.1949 0.0172  881 GLU A C   
3072 O O   . GLU A 363 ? 1.1013 0.4239 1.4371 0.0394  -0.1724 0.0540  881 GLU A O   
3073 C CB  . GLU A 363 ? 1.2654 0.4977 1.6988 -0.0042 -0.2100 0.0395  881 GLU A CB  
3074 C CG  . GLU A 363 ? 1.3099 0.5351 1.7400 -0.0367 -0.1748 0.1041  881 GLU A CG  
3075 C CD  . GLU A 363 ? 1.3607 0.5942 1.8485 -0.0853 -0.1614 0.1208  881 GLU A CD  
3076 O OE1 . GLU A 363 ? 1.3595 0.6121 1.8906 -0.0932 -0.1807 0.0778  881 GLU A OE1 
3077 O OE2 . GLU A 363 ? 1.4057 0.6334 1.8966 -0.1153 -0.1320 0.1774  881 GLU A OE2 
3078 N N   . LEU A 364 ? 1.0145 0.3859 1.4175 0.0340  -0.1944 -0.0231 882 LEU A N   
3079 C CA  . LEU A 364 ? 0.9619 0.4085 1.3386 0.0326  -0.1656 -0.0249 882 LEU A CA  
3080 C C   . LEU A 364 ? 0.9389 0.4092 1.2583 0.0632  -0.1657 -0.0315 882 LEU A C   
3081 O O   . LEU A 364 ? 0.8994 0.3986 1.1814 0.0591  -0.1396 -0.0106 882 LEU A O   
3082 C CB  . LEU A 364 ? 0.8799 0.3822 1.2856 0.0290  -0.1709 -0.0660 882 LEU A CB  
3083 C CG  . LEU A 364 ? 0.8589 0.4304 1.2370 0.0294  -0.1449 -0.0680 882 LEU A CG  
3084 C CD1 . LEU A 364 ? 0.8415 0.4492 1.2590 0.0070  -0.1326 -0.0674 882 LEU A CD1 
3085 C CD2 . LEU A 364 ? 0.8670 0.4809 1.2177 0.0553  -0.1583 -0.1053 882 LEU A CD2 
3086 N N   . TRP A 365 ? 0.9571 0.4199 1.2719 0.0952  -0.1962 -0.0643 883 TRP A N   
3087 C CA  . TRP A 365 ? 0.9839 0.4794 1.2543 0.1244  -0.2003 -0.0725 883 TRP A CA  
3088 C C   . TRP A 365 ? 1.0203 0.4850 1.2491 0.1255  -0.1898 -0.0257 883 TRP A C   
3089 O O   . TRP A 365 ? 0.9827 0.4907 1.1719 0.1240  -0.1714 -0.0177 883 TRP A O   
3090 C CB  . TRP A 365 ? 1.1024 0.5920 1.3836 0.1632  -0.2361 -0.1127 883 TRP A CB  
3091 C CG  . TRP A 365 ? 1.0934 0.6271 1.3399 0.1952  -0.2438 -0.1225 883 TRP A CG  
3092 C CD1 . TRP A 365 ? 1.1301 0.6284 1.3545 0.2239  -0.2621 -0.1041 883 TRP A CD1 
3093 C CD2 . TRP A 365 ? 1.0240 0.6499 1.2573 0.1999  -0.2351 -0.1505 883 TRP A CD2 
3094 N NE1 . TRP A 365 ? 1.1101 0.6810 1.3122 0.2476  -0.2668 -0.1234 883 TRP A NE1 
3095 C CE2 . TRP A 365 ? 1.0487 0.6982 1.2579 0.2301  -0.2492 -0.1517 883 TRP A CE2 
3096 C CE3 . TRP A 365 ? 0.9157 0.6065 1.1566 0.1801  -0.2178 -0.1711 883 TRP A CE3 
3097 C CZ2 . TRP A 365 ? 1.0051 0.7459 1.2042 0.2360  -0.2454 -0.1754 883 TRP A CZ2 
3098 C CZ3 . TRP A 365 ? 0.8977 0.6692 1.1237 0.1852  -0.2127 -0.1896 883 TRP A CZ3 
3099 C CH2 . TRP A 365 ? 0.9459 0.7443 1.1545 0.2106  -0.2259 -0.1930 883 TRP A CH2 
3100 N N   . ASP A 366 ? 1.1193 0.5073 1.3544 0.1266  -0.2023 0.0066  884 ASP A N   
3101 C CA  . ASP A 366 ? 1.2554 0.6162 1.4422 0.1325  -0.1958 0.0550  884 ASP A CA  
3102 C C   . ASP A 366 ? 1.2553 0.6390 1.4199 0.0993  -0.1543 0.0920  884 ASP A C   
3103 O O   . ASP A 366 ? 1.2465 0.6670 1.3582 0.1058  -0.1395 0.1027  884 ASP A O   
3104 C CB  . ASP A 366 ? 1.3990 0.6645 1.5966 0.1420  -0.2208 0.0873  884 ASP A CB  
3105 C CG  . ASP A 366 ? 1.4760 0.7096 1.7085 0.1750  -0.2617 0.0420  884 ASP A CG  
3106 O OD1 . ASP A 366 ? 1.5328 0.7261 1.7992 0.1586  -0.2668 0.0381  884 ASP A OD1 
3107 O OD2 . ASP A 366 ? 1.4605 0.7475 1.6778 0.2111  -0.2764 0.0039  884 ASP A OD2 
3108 N N   . LYS A 367 ? 1.2680 0.6366 1.4745 0.0649  -0.1359 0.1077  885 LYS A N   
3109 C CA  . LYS A 367 ? 1.2697 0.6677 1.4598 0.0381  -0.0943 0.1415  885 LYS A CA  
3110 C C   . LYS A 367 ? 1.2260 0.6968 1.3924 0.0417  -0.0738 0.1111  885 LYS A C   
3111 O O   . LYS A 367 ? 1.2536 0.7509 1.3831 0.0349  -0.0434 0.1312  885 LYS A O   
3112 C CB  . LYS A 367 ? 1.2571 0.6384 1.5098 0.0006  -0.0803 0.1606  885 LYS A CB  
3113 C CG  . LYS A 367 ? 1.3077 0.6051 1.5848 -0.0121 -0.0983 0.1993  885 LYS A CG  
3114 C CD  . LYS A 367 ? 1.3537 0.6388 1.6098 -0.0383 -0.0654 0.2689  885 LYS A CD  
3115 C CE  . LYS A 367 ? 1.4216 0.6247 1.6439 -0.0262 -0.0869 0.3152  885 LYS A CE  
3116 N NZ  . LYS A 367 ? 1.4764 0.6936 1.6313 -0.0299 -0.0556 0.3766  885 LYS A NZ  
3117 N N   . LEU A 368 ? 1.1492 0.6511 1.3325 0.0532  -0.0900 0.0634  886 LEU A N   
3118 C CA  . LEU A 368 ? 1.0877 0.6466 1.2475 0.0547  -0.0741 0.0388  886 LEU A CA  
3119 C C   . LEU A 368 ? 1.1498 0.7258 1.2520 0.0755  -0.0828 0.0324  886 LEU A C   
3120 O O   . LEU A 368 ? 1.1360 0.7382 1.1995 0.0718  -0.0628 0.0332  886 LEU A O   
3121 C CB  . LEU A 368 ? 1.0097 0.5996 1.2069 0.0547  -0.0862 -0.0019 886 LEU A CB  
3122 C CG  . LEU A 368 ? 0.9608 0.6001 1.1422 0.0520  -0.0729 -0.0243 886 LEU A CG  
3123 C CD1 . LEU A 368 ? 0.9262 0.5776 1.1333 0.0337  -0.0476 -0.0169 886 LEU A CD1 
3124 C CD2 . LEU A 368 ? 0.9161 0.5880 1.1104 0.0627  -0.0952 -0.0602 886 LEU A CD2 
3125 N N   . GLN A 369 ? 1.2070 0.7714 1.3054 0.0997  -0.1148 0.0222  887 GLN A N   
3126 C CA  . GLN A 369 ? 1.2257 0.8198 1.2782 0.1208  -0.1282 0.0126  887 GLN A CA  
3127 C C   . GLN A 369 ? 1.2630 0.8397 1.2588 0.1239  -0.1183 0.0516  887 GLN A C   
3128 O O   . GLN A 369 ? 1.2810 0.8945 1.2309 0.1313  -0.1191 0.0423  887 GLN A O   
3129 C CB  . GLN A 369 ? 1.2422 0.8349 1.3107 0.1522  -0.1656 -0.0075 887 GLN A CB  
3130 C CG  . GLN A 369 ? 1.2301 0.8560 1.3447 0.1540  -0.1752 -0.0505 887 GLN A CG  
3131 C CD  . GLN A 369 ? 1.2523 0.9503 1.3600 0.1693  -0.1879 -0.0851 887 GLN A CD  
3132 O OE1 . GLN A 369 ? 1.2959 1.0123 1.3755 0.1894  -0.2030 -0.0823 887 GLN A OE1 
3133 N NE2 . GLN A 369 ? 1.2385 0.9845 1.3731 0.1587  -0.1825 -0.1158 887 GLN A NE2 
3134 N N   . MET A 370 ? 1.3042 0.8289 1.3013 0.1163  -0.1097 0.0957  888 MET A N   
3135 C CA  . MET A 370 ? 1.4094 0.9240 1.3460 0.1180  -0.0962 0.1393  888 MET A CA  
3136 C C   . MET A 370 ? 1.4236 0.9778 1.3308 0.0992  -0.0571 0.1381  888 MET A C   
3137 O O   . MET A 370 ? 1.5066 1.0776 1.3488 0.1066  -0.0476 0.1549  888 MET A O   
3138 C CB  . MET A 370 ? 1.5234 0.9715 1.4727 0.1097  -0.0951 0.1935  888 MET A CB  
3139 C CG  . MET A 370 ? 1.6369 1.0304 1.5944 0.1379  -0.1375 0.2031  888 MET A CG  
3140 S SD  . MET A 370 ? 1.7325 1.1475 1.6138 0.1800  -0.1652 0.2120  888 MET A SD  
3141 C CE  . MET A 370 ? 1.6528 1.1166 1.5716 0.2083  -0.1992 0.1402  888 MET A CE  
3142 N N   . ALA A 371 ? 1.3521 0.9228 1.3038 0.0790  -0.0360 0.1166  889 ALA A N   
3143 C CA  . ALA A 371 ? 1.3395 0.9449 1.2700 0.0679  -0.0011 0.1078  889 ALA A CA  
3144 C C   . ALA A 371 ? 1.3181 0.9587 1.2183 0.0762  -0.0089 0.0631  889 ALA A C   
3145 O O   . ALA A 371 ? 1.3204 0.9818 1.1878 0.0733  0.0146  0.0516  889 ALA A O   
3146 C CB  . ALA A 371 ? 1.2886 0.8982 1.2826 0.0475  0.0205  0.1035  889 ALA A CB  
3147 N N   . ILE A 372 ? 1.3099 0.9594 1.2232 0.0859  -0.0412 0.0361  890 ILE A N   
3148 C CA  . ILE A 372 ? 1.3207 1.0065 1.2155 0.0862  -0.0506 -0.0041 890 ILE A CA  
3149 C C   . ILE A 372 ? 1.3898 1.0961 1.2325 0.1045  -0.0754 -0.0070 890 ILE A C   
3150 O O   . ILE A 372 ? 1.3863 1.1227 1.1960 0.1009  -0.0778 -0.0348 890 ILE A O   
3151 C CB  . ILE A 372 ? 1.2632 0.9647 1.2131 0.0799  -0.0653 -0.0334 890 ILE A CB  
3152 C CG1 . ILE A 372 ? 1.2454 0.9428 1.2285 0.0611  -0.0407 -0.0413 890 ILE A CG1 
3153 C CG2 . ILE A 372 ? 1.2491 0.9936 1.1871 0.0815  -0.0865 -0.0666 890 ILE A CG2 
3154 C CD1 . ILE A 372 ? 1.2559 0.9273 1.2756 0.0560  -0.0252 -0.0147 890 ILE A CD1 
3155 N N   . GLU A 373 ? 1.4901 1.1780 1.3241 0.1244  -0.0959 0.0218  891 GLU A N   
3156 C CA  . GLU A 373 ? 1.6033 1.3127 1.3855 0.1474  -0.1223 0.0258  891 GLU A CA  
3157 C C   . GLU A 373 ? 1.7093 1.4340 1.4174 0.1455  -0.1056 0.0328  891 GLU A C   
3158 O O   . GLU A 373 ? 1.7575 1.5164 1.4182 0.1607  -0.1287 0.0223  891 GLU A O   
3159 C CB  . GLU A 373 ? 1.6603 1.3296 1.4440 0.1716  -0.1440 0.0662  891 GLU A CB  
3160 C CG  . GLU A 373 ? 1.7184 1.4135 1.4634 0.2043  -0.1817 0.0683  891 GLU A CG  
3161 C CD  . GLU A 373 ? 1.8155 1.4575 1.5303 0.2272  -0.1942 0.1260  891 GLU A CD  
3162 O OE1 . GLU A 373 ? 1.8762 1.5365 1.5495 0.2580  -0.2253 0.1370  891 GLU A OE1 
3163 O OE2 . GLU A 373 ? 1.8373 1.4196 1.5719 0.2133  -0.1747 0.1625  891 GLU A OE2 
3164 N N   . ASN A 374 ? 1.7468 1.4552 1.4443 0.1297  -0.0669 0.0468  892 ASN A N   
3165 C CA  . ASN A 374 ? 1.8311 1.5604 1.4566 0.1307  -0.0465 0.0456  892 ASN A CA  
3166 C C   . ASN A 374 ? 1.8325 1.5792 1.4631 0.1153  -0.0299 -0.0048 892 ASN A C   
3167 O O   . ASN A 374 ? 1.8722 1.6208 1.4747 0.1119  0.0030  -0.0076 892 ASN A O   
3168 C CB  . ASN A 374 ? 1.8746 1.5832 1.4777 0.1285  -0.0129 0.0981  892 ASN A CB  
3169 C CG  . ASN A 374 ? 1.9147 1.5840 1.5376 0.1351  -0.0283 0.1497  892 ASN A CG  
3170 O OD1 . ASN A 374 ? 1.8645 1.5027 1.5584 0.1261  -0.0341 0.1523  892 ASN A OD1 
3171 N ND2 . ASN A 374 ? 2.0150 1.6835 1.5738 0.1539  -0.0421 0.1871  892 ASN A ND2 
3172 N N   . THR A 375 ? 1.7952 1.5555 1.4618 0.1069  -0.0527 -0.0448 893 THR A N   
3173 C CA  . THR A 375 ? 1.7878 1.5555 1.4571 0.0905  -0.0447 -0.0917 893 THR A CA  
3174 C C   . THR A 375 ? 1.8147 1.6192 1.4650 0.0878  -0.0798 -0.1294 893 THR A C   
3175 O O   . THR A 375 ? 1.7796 1.6017 1.4789 0.0777  -0.1012 -0.1444 893 THR A O   
3176 C CB  . THR A 375 ? 1.7106 1.4583 1.4537 0.0728  -0.0338 -0.1005 893 THR A CB  
3177 O OG1 . THR A 375 ? 1.6806 1.4413 1.4704 0.0718  -0.0603 -0.0982 893 THR A OG1 
3178 C CG2 . THR A 375 ? 1.6852 1.4066 1.4524 0.0736  -0.0008 -0.0685 893 THR A CG2 
# 
