data_9H9O
# 
_entry.id   9H9O 
# 
_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   9H9O         pdb_00009h9o 10.2210/pdb9h9o/pdb 
WWPDB D_1292142849 ?            ?                   
# 
_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                        9H9O 
_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_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 
# 
_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 1,2-ETHANEDIOL                                   62.068    4  ?        ? ? ? 
3 non-polymer syn Norclomipramine                                  300.826   1  ?        ? ? ? 
4 water       nat water                                            18.015    95 ?        ? ? ? 
# 
_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 1,2-ETHANEDIOL  EDO   
3 Norclomipramine A1ITH 
4 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 
A1ITH non-polymer         . Norclomipramine 
'3-(2-chloranyl-5,6-dihydrobenzo[b][1]benzazepin-11-yl)-N-methyl-propan-1-amine; Desmethylclomipramine' 'C18 H21 Cl N2'  300.826 
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 
EDO   non-polymer         . 1,2-ETHANEDIOL  'ETHYLENE GLYCOL' 'C2 H6 O2'       62.068  
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        A1ITH 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1ITH 
_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 EDO   1  901  2   EDO   EDO A . 
C 2 EDO   1  902  3   EDO   EDO A . 
D 2 EDO   1  903  5   EDO   EDO A . 
E 2 EDO   1  904  6   EDO   EDO A . 
F 3 A1ITH 1  905  1   A1ITH NOR A . 
G 4 HOH   1  1001 146 HOH   HOH A . 
G 4 HOH   2  1002 46  HOH   HOH A . 
G 4 HOH   3  1003 71  HOH   HOH A . 
G 4 HOH   4  1004 24  HOH   HOH A . 
G 4 HOH   5  1005 26  HOH   HOH A . 
G 4 HOH   6  1006 32  HOH   HOH A . 
G 4 HOH   7  1007 36  HOH   HOH A . 
G 4 HOH   8  1008 41  HOH   HOH A . 
G 4 HOH   9  1009 102 HOH   HOH A . 
G 4 HOH   10 1010 14  HOH   HOH A . 
G 4 HOH   11 1011 44  HOH   HOH A . 
G 4 HOH   12 1012 67  HOH   HOH A . 
G 4 HOH   13 1013 88  HOH   HOH A . 
G 4 HOH   14 1014 54  HOH   HOH A . 
G 4 HOH   15 1015 147 HOH   HOH A . 
G 4 HOH   16 1016 111 HOH   HOH A . 
G 4 HOH   17 1017 81  HOH   HOH A . 
G 4 HOH   18 1018 37  HOH   HOH A . 
G 4 HOH   19 1019 2   HOH   HOH A . 
G 4 HOH   20 1020 3   HOH   HOH A . 
G 4 HOH   21 1021 22  HOH   HOH A . 
G 4 HOH   22 1022 48  HOH   HOH A . 
G 4 HOH   23 1023 63  HOH   HOH A . 
G 4 HOH   24 1024 8   HOH   HOH A . 
G 4 HOH   25 1025 65  HOH   HOH A . 
G 4 HOH   26 1026 15  HOH   HOH A . 
G 4 HOH   27 1027 122 HOH   HOH A . 
G 4 HOH   28 1028 7   HOH   HOH A . 
G 4 HOH   29 1029 104 HOH   HOH A . 
G 4 HOH   30 1030 56  HOH   HOH A . 
G 4 HOH   31 1031 5   HOH   HOH A . 
G 4 HOH   32 1032 18  HOH   HOH A . 
G 4 HOH   33 1033 75  HOH   HOH A . 
G 4 HOH   34 1034 25  HOH   HOH A . 
G 4 HOH   35 1035 42  HOH   HOH A . 
G 4 HOH   36 1036 4   HOH   HOH A . 
G 4 HOH   37 1037 52  HOH   HOH A . 
G 4 HOH   38 1038 64  HOH   HOH A . 
G 4 HOH   39 1039 82  HOH   HOH A . 
G 4 HOH   40 1040 66  HOH   HOH A . 
G 4 HOH   41 1041 61  HOH   HOH A . 
G 4 HOH   42 1042 60  HOH   HOH A . 
G 4 HOH   43 1043 27  HOH   HOH A . 
G 4 HOH   44 1044 28  HOH   HOH A . 
G 4 HOH   45 1045 119 HOH   HOH A . 
G 4 HOH   46 1046 47  HOH   HOH A . 
G 4 HOH   47 1047 43  HOH   HOH A . 
G 4 HOH   48 1048 49  HOH   HOH A . 
G 4 HOH   49 1049 103 HOH   HOH A . 
G 4 HOH   50 1050 21  HOH   HOH A . 
G 4 HOH   51 1051 31  HOH   HOH A . 
G 4 HOH   52 1052 50  HOH   HOH A . 
G 4 HOH   53 1053 72  HOH   HOH A . 
G 4 HOH   54 1054 34  HOH   HOH A . 
G 4 HOH   55 1055 148 HOH   HOH A . 
G 4 HOH   56 1056 20  HOH   HOH A . 
G 4 HOH   57 1057 38  HOH   HOH A . 
G 4 HOH   58 1058 55  HOH   HOH A . 
G 4 HOH   59 1059 144 HOH   HOH A . 
G 4 HOH   60 1060 19  HOH   HOH A . 
G 4 HOH   61 1061 78  HOH   HOH A . 
G 4 HOH   62 1062 74  HOH   HOH A . 
G 4 HOH   63 1063 76  HOH   HOH A . 
G 4 HOH   64 1064 106 HOH   HOH A . 
G 4 HOH   65 1065 16  HOH   HOH A . 
G 4 HOH   66 1066 17  HOH   HOH A . 
G 4 HOH   67 1067 59  HOH   HOH A . 
G 4 HOH   68 1068 45  HOH   HOH A . 
G 4 HOH   69 1069 35  HOH   HOH A . 
G 4 HOH   70 1070 11  HOH   HOH A . 
G 4 HOH   71 1071 87  HOH   HOH A . 
G 4 HOH   72 1072 126 HOH   HOH A . 
G 4 HOH   73 1073 51  HOH   HOH A . 
G 4 HOH   74 1074 133 HOH   HOH A . 
G 4 HOH   75 1075 9   HOH   HOH A . 
G 4 HOH   76 1076 97  HOH   HOH A . 
G 4 HOH   77 1077 13  HOH   HOH A . 
G 4 HOH   78 1078 30  HOH   HOH A . 
G 4 HOH   79 1079 29  HOH   HOH A . 
G 4 HOH   80 1080 39  HOH   HOH A . 
G 4 HOH   81 1081 85  HOH   HOH A . 
G 4 HOH   82 1082 12  HOH   HOH A . 
G 4 HOH   83 1083 128 HOH   HOH A . 
G 4 HOH   84 1084 136 HOH   HOH A . 
G 4 HOH   85 1085 69  HOH   HOH A . 
G 4 HOH   86 1086 6   HOH   HOH A . 
G 4 HOH   87 1087 140 HOH   HOH A . 
G 4 HOH   88 1088 145 HOH   HOH A . 
G 4 HOH   89 1089 143 HOH   HOH A . 
G 4 HOH   90 1090 141 HOH   HOH A . 
G 4 HOH   91 1091 138 HOH   HOH A . 
G 4 HOH   92 1092 116 HOH   HOH A . 
G 4 HOH   93 1093 68  HOH   HOH A . 
G 4 HOH   94 1094 77  HOH   HOH A . 
G 4 HOH   95 1095 142 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 
7 1 Y 1 A THR 893 ? OG1 ? A THR 375 OG1 
8 1 Y 1 A THR 893 ? CG2 ? A THR 375 CG2 
# 
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  ? ? ? dev_1839 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? xia2    ? ? ? 0.3.8.0  2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? 0.3.11   3 
? 'model building' ? ? ? ? ? ? ? ? ? ? ? Coot    ? ? ? .        4 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER  ? ? ? .        5 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   92.85 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9H9O 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     175.750 
_cell.length_a_esd                 ? 
_cell.length_b                     38.890 
_cell.length_b_esd                 ? 
_cell.length_c                     60.070 
_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                         9H9O 
_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                   9H9O 
_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             2.29 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          46.32 
_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              6.0 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    
;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         2015-02-23 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1.00002 
_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        1.00002 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   X06DA 
_diffrn_source.pdbx_synchrotron_site       SLS 
# 
_reflns.B_iso_Wilson_estimate                          38.6 
_reflns.entry_id                                       9H9O 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.12 
_reflns.d_resolution_low                               60.00 
_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                                     23416 
_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                           99.8 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                3.7 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          17.1 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_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                              0.040 
_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                                    2.12 
_reflns_shell.d_res_low                                     2.18 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           2.3 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             1725 
_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                               3.7 
_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                                  0.699 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          99.7 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  0.519 
_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                                 9H9O 
_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                            2.120 
_refine.ls_d_res_low                             60 
_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                     23413 
_refine.ls_number_reflns_R_free                  1194 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.77 
_refine.ls_percent_reflns_R_free                 5.10 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1885 
_refine.ls_R_factor_R_free                       0.2365 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1858 
_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                          1.36 
_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                      2xbf 
_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                 26.03 
_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                            0.29 
_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        3148 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         37 
_refine_hist.number_atoms_solvent             95 
_refine_hist.number_atoms_total               3280 
_refine_hist.d_res_high                       2.120 
_refine_hist.d_res_low                        60 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.008  ? 3280 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.055  ? 4414 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 14.645 ? 1221 ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.042  ? 441  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.005  ? 567  ? 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' 2.1201 2.2049 . . 145 2424 100.00 . . . . 0.2512 . . . . . . . . . . . 0.3398 
'X-RAY DIFFRACTION' 2.2049 2.3053 . . 133 2464 100.00 . . . . 0.2471 . . . . . . . . . . . 0.3604 
'X-RAY DIFFRACTION' 2.3053 2.4268 . . 102 2470 100.00 . . . . 0.2246 . . . . . . . . . . . 0.3109 
'X-RAY DIFFRACTION' 2.4268 2.5789 . . 136 2459 100.00 . . . . 0.2197 . . . . . . . . . . . 0.2749 
'X-RAY DIFFRACTION' 2.5789 2.7780 . . 144 2424 100.00 . . . . 0.2138 . . . . . . . . . . . 0.2668 
'X-RAY DIFFRACTION' 2.7780 3.0576 . . 117 2470 100.00 . . . . 0.2182 . . . . . . . . . . . 0.3301 
'X-RAY DIFFRACTION' 3.0576 3.5000 . . 133 2465 99.00  . . . . 0.1937 . . . . . . . . . . . 0.2365 
'X-RAY DIFFRACTION' 3.5000 4.4094 . . 142 2489 100.00 . . . . 0.1615 . . . . . . . . . . . 0.2039 
'X-RAY DIFFRACTION' 4.4094 60.0   . . 142 2554 99.00  . . . . 0.1526 . . . . . . . . . . . 0.1872 
# 
_struct.entry_id                     9H9O 
_struct.title                        'Crystal structure of NEDD4 HECT domain in complex with norclomipramine' 
_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        9H9O 
_struct_keywords.text            '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 2 ? 
D N N 2 ? 
E N N 2 ? 
F N N 3 ? 
G N N 4 ? 
# 
_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              9H9O 
_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_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_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)' 750   ? 
1 MORE         11    ? 
1 'SSA (A^2)'  19640 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'isothermal titration calorimetry' 
_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  ? VAL A 45  ? THR A 551 VAL A 563 1 ? 13 
HELX_P HELX_P4  AA4 ARG A 47  ? ALA A 53  ? ARG A 565 ALA A 571 5 ? 7  
HELX_P HELX_P5  AA5 ASP A 66  ? PHE A 83  ? ASP A 584 PHE A 601 1 ? 18 
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 ? ASP A 160 ? THR A 670 ASP A 678 1 ? 9  
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 ? ILE A 242 ? ILE A 745 ILE A 760 1 ? 16 
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 THR A 348 ? PHE A 350 ? THR A 866 PHE A 868 5 ? 3  
HELX_P HELX_P23 AC5 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   ? 
# 
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 PHE A 25  ? N PHE A 543 O TRP A 56  ? O TRP A 574 
AA2 1 2 N GLU A 91  ? N GLU A 609 O GLN A 101 ? O GLN A 619 
AA3 1 2 N GLU A 186 ? N GLU A 704 O HIS A 193 ? O HIS A 711 
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                   9H9O 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 ND1 A HIS 713 ? A O A HOH 1001 ? ? 2.16 
2 1 OE1 A GLU 695 ? ? O A HOH 1002 ? ? 2.18 
# 
_pdbx_validate_symm_contact.id                1 
_pdbx_validate_symm_contact.PDB_model_num     1 
_pdbx_validate_symm_contact.auth_atom_id_1    NH1 
_pdbx_validate_symm_contact.auth_asym_id_1    A 
_pdbx_validate_symm_contact.auth_comp_id_1    ARG 
_pdbx_validate_symm_contact.auth_seq_id_1     863 
_pdbx_validate_symm_contact.PDB_ins_code_1    ? 
_pdbx_validate_symm_contact.label_alt_id_1    ? 
_pdbx_validate_symm_contact.site_symmetry_1   1_555 
_pdbx_validate_symm_contact.auth_atom_id_2    O 
_pdbx_validate_symm_contact.auth_asym_id_2    A 
_pdbx_validate_symm_contact.auth_comp_id_2    ASN 
_pdbx_validate_symm_contact.auth_seq_id_2     892 
_pdbx_validate_symm_contact.PDB_ins_code_2    ? 
_pdbx_validate_symm_contact.label_alt_id_2    ? 
_pdbx_validate_symm_contact.site_symmetry_2   2_555 
_pdbx_validate_symm_contact.dist              2.11 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ASP A 538 ? ? -87.66  38.16  
2 1 TRP A 574 ? ? -119.08 76.03  
3 1 VAL A 742 ? ? -125.35 -54.32 
# 
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 -25.5867 -24.6306 -3.9435 0.1936 ? -0.0564 ? 0.0215  ? 0.2576 ? -0.0239 ? 0.3025 ? 1.4967 ? 
-0.4859 ? 0.5718  ? 3.1465 ? -0.4481 ? 4.3981 ? 0.0899  ? 0.1729  ? -0.0602 ? -0.3558 ? -0.0818 ? -0.3501 ? 0.0152 ? 0.2309  ? 
-0.0289 ? 
2 'X-RAY DIFFRACTION' ? refined -37.0374 -18.8881 17.4021 0.3179 ? -0.0252 ? -0.0402 ? 0.2630 ? 0.0111  ? 0.2312 ? 2.1197 ? 
-1.2893 ? -1.8819 ? 2.1626 ? 1.6976  ? 2.8759 ? -0.0512 ? -0.1795 ? 0.1748  ? 0.3665  ? 0.0805  ? -0.1281 ? 0.0595 ? 0.1375  ? 
-0.0219 ? 
3 'X-RAY DIFFRACTION' ? refined -1.6482  -13.5556 13.6963 0.4894 ? 0.0769  ? 0.0921  ? 0.3980 ? 0.0087  ? 0.6174 ? 6.3275 ? 
-1.8077 ? 1.7253  ? 8.8262 ? -0.2048 ? 7.5621 ? 0.1324  ? 0.1320  ? 0.2172  ? -0.7760 ? -0.2859 ? -0.7830 ? 0.3321 ? -0.2952 ? 
0.1573  ? 
# 
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 )
;
# 
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 
A1ITH C01  C  N N 1   
A1ITH N02  N  N N 2   
A1ITH C03  C  N N 3   
A1ITH C04  C  N N 4   
A1ITH C05  C  N N 5   
A1ITH N06  N  N N 6   
A1ITH C07  C  Y N 7   
A1ITH C08  C  Y N 8   
A1ITH C09  C  Y N 9   
A1ITH C10  C  Y N 10  
A1ITH C11  C  Y N 11  
A1ITH C12  C  Y N 12  
A1ITH C13  C  N N 13  
A1ITH C14  C  N N 14  
A1ITH C15  C  Y N 15  
A1ITH C16  C  Y N 16  
A1ITH C17  C  Y N 17  
A1ITH C18  C  Y N 18  
A1ITH C19  C  Y N 19  
A1ITH C20  C  Y N 20  
A1ITH CL21 CL N N 21  
A1ITH H1   H  N N 22  
A1ITH H2   H  N N 23  
A1ITH H3   H  N N 24  
A1ITH H4   H  N N 25  
A1ITH H6   H  N N 26  
A1ITH H7   H  N N 27  
A1ITH H8   H  N N 28  
A1ITH H9   H  N N 29  
A1ITH H10  H  N N 30  
A1ITH H11  H  N N 31  
A1ITH H12  H  N N 32  
A1ITH H13  H  N N 33  
A1ITH H14  H  N N 34  
A1ITH H15  H  N N 35  
A1ITH H16  H  N N 36  
A1ITH H17  H  N N 37  
A1ITH H18  H  N N 38  
A1ITH H19  H  N N 39  
A1ITH H20  H  N N 40  
A1ITH H21  H  N N 41  
A1ITH H22  H  N N 42  
ALA   N    N  N N 43  
ALA   CA   C  N S 44  
ALA   C    C  N N 45  
ALA   O    O  N N 46  
ALA   CB   C  N N 47  
ALA   OXT  O  N N 48  
ALA   H    H  N N 49  
ALA   H2   H  N N 50  
ALA   HA   H  N N 51  
ALA   HB1  H  N N 52  
ALA   HB2  H  N N 53  
ALA   HB3  H  N N 54  
ALA   HXT  H  N N 55  
ARG   N    N  N N 56  
ARG   CA   C  N S 57  
ARG   C    C  N N 58  
ARG   O    O  N N 59  
ARG   CB   C  N N 60  
ARG   CG   C  N N 61  
ARG   CD   C  N N 62  
ARG   NE   N  N N 63  
ARG   CZ   C  N N 64  
ARG   NH1  N  N N 65  
ARG   NH2  N  N N 66  
ARG   OXT  O  N N 67  
ARG   H    H  N N 68  
ARG   H2   H  N N 69  
ARG   HA   H  N N 70  
ARG   HB2  H  N N 71  
ARG   HB3  H  N N 72  
ARG   HG2  H  N N 73  
ARG   HG3  H  N N 74  
ARG   HD2  H  N N 75  
ARG   HD3  H  N N 76  
ARG   HE   H  N N 77  
ARG   HH11 H  N N 78  
ARG   HH12 H  N N 79  
ARG   HH21 H  N N 80  
ARG   HH22 H  N N 81  
ARG   HXT  H  N N 82  
ASN   N    N  N N 83  
ASN   CA   C  N S 84  
ASN   C    C  N N 85  
ASN   O    O  N N 86  
ASN   CB   C  N N 87  
ASN   CG   C  N N 88  
ASN   OD1  O  N N 89  
ASN   ND2  N  N N 90  
ASN   OXT  O  N N 91  
ASN   H    H  N N 92  
ASN   H2   H  N N 93  
ASN   HA   H  N N 94  
ASN   HB2  H  N N 95  
ASN   HB3  H  N N 96  
ASN   HD21 H  N N 97  
ASN   HD22 H  N N 98  
ASN   HXT  H  N N 99  
ASP   N    N  N N 100 
ASP   CA   C  N S 101 
ASP   C    C  N N 102 
ASP   O    O  N N 103 
ASP   CB   C  N N 104 
ASP   CG   C  N N 105 
ASP   OD1  O  N N 106 
ASP   OD2  O  N N 107 
ASP   OXT  O  N N 108 
ASP   H    H  N N 109 
ASP   H2   H  N N 110 
ASP   HA   H  N N 111 
ASP   HB2  H  N N 112 
ASP   HB3  H  N N 113 
ASP   HD2  H  N N 114 
ASP   HXT  H  N N 115 
CYS   N    N  N N 116 
CYS   CA   C  N R 117 
CYS   C    C  N N 118 
CYS   O    O  N N 119 
CYS   CB   C  N N 120 
CYS   SG   S  N N 121 
CYS   OXT  O  N N 122 
CYS   H    H  N N 123 
CYS   H2   H  N N 124 
CYS   HA   H  N N 125 
CYS   HB2  H  N N 126 
CYS   HB3  H  N N 127 
CYS   HG   H  N N 128 
CYS   HXT  H  N N 129 
EDO   C1   C  N N 130 
EDO   O1   O  N N 131 
EDO   C2   C  N N 132 
EDO   O2   O  N N 133 
EDO   H11  H  N N 134 
EDO   H12  H  N N 135 
EDO   HO1  H  N N 136 
EDO   H21  H  N N 137 
EDO   H22  H  N N 138 
EDO   HO2  H  N N 139 
GLN   N    N  N N 140 
GLN   CA   C  N S 141 
GLN   C    C  N N 142 
GLN   O    O  N N 143 
GLN   CB   C  N N 144 
GLN   CG   C  N N 145 
GLN   CD   C  N N 146 
GLN   OE1  O  N N 147 
GLN   NE2  N  N N 148 
GLN   OXT  O  N N 149 
GLN   H    H  N N 150 
GLN   H2   H  N N 151 
GLN   HA   H  N N 152 
GLN   HB2  H  N N 153 
GLN   HB3  H  N N 154 
GLN   HG2  H  N N 155 
GLN   HG3  H  N N 156 
GLN   HE21 H  N N 157 
GLN   HE22 H  N N 158 
GLN   HXT  H  N N 159 
GLU   N    N  N N 160 
GLU   CA   C  N S 161 
GLU   C    C  N N 162 
GLU   O    O  N N 163 
GLU   CB   C  N N 164 
GLU   CG   C  N N 165 
GLU   CD   C  N N 166 
GLU   OE1  O  N N 167 
GLU   OE2  O  N N 168 
GLU   OXT  O  N N 169 
GLU   H    H  N N 170 
GLU   H2   H  N N 171 
GLU   HA   H  N N 172 
GLU   HB2  H  N N 173 
GLU   HB3  H  N N 174 
GLU   HG2  H  N N 175 
GLU   HG3  H  N N 176 
GLU   HE2  H  N N 177 
GLU   HXT  H  N N 178 
GLY   N    N  N N 179 
GLY   CA   C  N N 180 
GLY   C    C  N N 181 
GLY   O    O  N N 182 
GLY   OXT  O  N N 183 
GLY   H    H  N N 184 
GLY   H2   H  N N 185 
GLY   HA2  H  N N 186 
GLY   HA3  H  N N 187 
GLY   HXT  H  N N 188 
HIS   N    N  N N 189 
HIS   CA   C  N S 190 
HIS   C    C  N N 191 
HIS   O    O  N N 192 
HIS   CB   C  N N 193 
HIS   CG   C  Y N 194 
HIS   ND1  N  Y N 195 
HIS   CD2  C  Y N 196 
HIS   CE1  C  Y N 197 
HIS   NE2  N  Y N 198 
HIS   OXT  O  N N 199 
HIS   H    H  N N 200 
HIS   H2   H  N N 201 
HIS   HA   H  N N 202 
HIS   HB2  H  N N 203 
HIS   HB3  H  N N 204 
HIS   HD1  H  N N 205 
HIS   HD2  H  N N 206 
HIS   HE1  H  N N 207 
HIS   HE2  H  N N 208 
HIS   HXT  H  N N 209 
HOH   O    O  N N 210 
HOH   H1   H  N N 211 
HOH   H2   H  N N 212 
ILE   N    N  N N 213 
ILE   CA   C  N S 214 
ILE   C    C  N N 215 
ILE   O    O  N N 216 
ILE   CB   C  N S 217 
ILE   CG1  C  N N 218 
ILE   CG2  C  N N 219 
ILE   CD1  C  N N 220 
ILE   OXT  O  N N 221 
ILE   H    H  N N 222 
ILE   H2   H  N N 223 
ILE   HA   H  N N 224 
ILE   HB   H  N N 225 
ILE   HG12 H  N N 226 
ILE   HG13 H  N N 227 
ILE   HG21 H  N N 228 
ILE   HG22 H  N N 229 
ILE   HG23 H  N N 230 
ILE   HD11 H  N N 231 
ILE   HD12 H  N N 232 
ILE   HD13 H  N N 233 
ILE   HXT  H  N N 234 
LEU   N    N  N N 235 
LEU   CA   C  N S 236 
LEU   C    C  N N 237 
LEU   O    O  N N 238 
LEU   CB   C  N N 239 
LEU   CG   C  N N 240 
LEU   CD1  C  N N 241 
LEU   CD2  C  N N 242 
LEU   OXT  O  N N 243 
LEU   H    H  N N 244 
LEU   H2   H  N N 245 
LEU   HA   H  N N 246 
LEU   HB2  H  N N 247 
LEU   HB3  H  N N 248 
LEU   HG   H  N N 249 
LEU   HD11 H  N N 250 
LEU   HD12 H  N N 251 
LEU   HD13 H  N N 252 
LEU   HD21 H  N N 253 
LEU   HD22 H  N N 254 
LEU   HD23 H  N N 255 
LEU   HXT  H  N N 256 
LYS   N    N  N N 257 
LYS   CA   C  N S 258 
LYS   C    C  N N 259 
LYS   O    O  N N 260 
LYS   CB   C  N N 261 
LYS   CG   C  N N 262 
LYS   CD   C  N N 263 
LYS   CE   C  N N 264 
LYS   NZ   N  N N 265 
LYS   OXT  O  N N 266 
LYS   H    H  N N 267 
LYS   H2   H  N N 268 
LYS   HA   H  N N 269 
LYS   HB2  H  N N 270 
LYS   HB3  H  N N 271 
LYS   HG2  H  N N 272 
LYS   HG3  H  N N 273 
LYS   HD2  H  N N 274 
LYS   HD3  H  N N 275 
LYS   HE2  H  N N 276 
LYS   HE3  H  N N 277 
LYS   HZ1  H  N N 278 
LYS   HZ2  H  N N 279 
LYS   HZ3  H  N N 280 
LYS   HXT  H  N N 281 
MET   N    N  N N 282 
MET   CA   C  N S 283 
MET   C    C  N N 284 
MET   O    O  N N 285 
MET   CB   C  N N 286 
MET   CG   C  N N 287 
MET   SD   S  N N 288 
MET   CE   C  N N 289 
MET   OXT  O  N N 290 
MET   H    H  N N 291 
MET   H2   H  N N 292 
MET   HA   H  N N 293 
MET   HB2  H  N N 294 
MET   HB3  H  N N 295 
MET   HG2  H  N N 296 
MET   HG3  H  N N 297 
MET   HE1  H  N N 298 
MET   HE2  H  N N 299 
MET   HE3  H  N N 300 
MET   HXT  H  N N 301 
PHE   N    N  N N 302 
PHE   CA   C  N S 303 
PHE   C    C  N N 304 
PHE   O    O  N N 305 
PHE   CB   C  N N 306 
PHE   CG   C  Y N 307 
PHE   CD1  C  Y N 308 
PHE   CD2  C  Y N 309 
PHE   CE1  C  Y N 310 
PHE   CE2  C  Y N 311 
PHE   CZ   C  Y N 312 
PHE   OXT  O  N N 313 
PHE   H    H  N N 314 
PHE   H2   H  N N 315 
PHE   HA   H  N N 316 
PHE   HB2  H  N N 317 
PHE   HB3  H  N N 318 
PHE   HD1  H  N N 319 
PHE   HD2  H  N N 320 
PHE   HE1  H  N N 321 
PHE   HE2  H  N N 322 
PHE   HZ   H  N N 323 
PHE   HXT  H  N N 324 
PRO   N    N  N N 325 
PRO   CA   C  N S 326 
PRO   C    C  N N 327 
PRO   O    O  N N 328 
PRO   CB   C  N N 329 
PRO   CG   C  N N 330 
PRO   CD   C  N N 331 
PRO   OXT  O  N N 332 
PRO   H    H  N N 333 
PRO   HA   H  N N 334 
PRO   HB2  H  N N 335 
PRO   HB3  H  N N 336 
PRO   HG2  H  N N 337 
PRO   HG3  H  N N 338 
PRO   HD2  H  N N 339 
PRO   HD3  H  N N 340 
PRO   HXT  H  N N 341 
SER   N    N  N N 342 
SER   CA   C  N S 343 
SER   C    C  N N 344 
SER   O    O  N N 345 
SER   CB   C  N N 346 
SER   OG   O  N N 347 
SER   OXT  O  N N 348 
SER   H    H  N N 349 
SER   H2   H  N N 350 
SER   HA   H  N N 351 
SER   HB2  H  N N 352 
SER   HB3  H  N N 353 
SER   HG   H  N N 354 
SER   HXT  H  N N 355 
THR   N    N  N N 356 
THR   CA   C  N S 357 
THR   C    C  N N 358 
THR   O    O  N N 359 
THR   CB   C  N R 360 
THR   OG1  O  N N 361 
THR   CG2  C  N N 362 
THR   OXT  O  N N 363 
THR   H    H  N N 364 
THR   H2   H  N N 365 
THR   HA   H  N N 366 
THR   HB   H  N N 367 
THR   HG1  H  N N 368 
THR   HG21 H  N N 369 
THR   HG22 H  N N 370 
THR   HG23 H  N N 371 
THR   HXT  H  N N 372 
TRP   N    N  N N 373 
TRP   CA   C  N S 374 
TRP   C    C  N N 375 
TRP   O    O  N N 376 
TRP   CB   C  N N 377 
TRP   CG   C  Y N 378 
TRP   CD1  C  Y N 379 
TRP   CD2  C  Y N 380 
TRP   NE1  N  Y N 381 
TRP   CE2  C  Y N 382 
TRP   CE3  C  Y N 383 
TRP   CZ2  C  Y N 384 
TRP   CZ3  C  Y N 385 
TRP   CH2  C  Y N 386 
TRP   OXT  O  N N 387 
TRP   H    H  N N 388 
TRP   H2   H  N N 389 
TRP   HA   H  N N 390 
TRP   HB2  H  N N 391 
TRP   HB3  H  N N 392 
TRP   HD1  H  N N 393 
TRP   HE1  H  N N 394 
TRP   HE3  H  N N 395 
TRP   HZ2  H  N N 396 
TRP   HZ3  H  N N 397 
TRP   HH2  H  N N 398 
TRP   HXT  H  N N 399 
TYR   N    N  N N 400 
TYR   CA   C  N S 401 
TYR   C    C  N N 402 
TYR   O    O  N N 403 
TYR   CB   C  N N 404 
TYR   CG   C  Y N 405 
TYR   CD1  C  Y N 406 
TYR   CD2  C  Y N 407 
TYR   CE1  C  Y N 408 
TYR   CE2  C  Y N 409 
TYR   CZ   C  Y N 410 
TYR   OH   O  N N 411 
TYR   OXT  O  N N 412 
TYR   H    H  N N 413 
TYR   H2   H  N N 414 
TYR   HA   H  N N 415 
TYR   HB2  H  N N 416 
TYR   HB3  H  N N 417 
TYR   HD1  H  N N 418 
TYR   HD2  H  N N 419 
TYR   HE1  H  N N 420 
TYR   HE2  H  N N 421 
TYR   HH   H  N N 422 
TYR   HXT  H  N N 423 
VAL   N    N  N N 424 
VAL   CA   C  N S 425 
VAL   C    C  N N 426 
VAL   O    O  N N 427 
VAL   CB   C  N N 428 
VAL   CG1  C  N N 429 
VAL   CG2  C  N N 430 
VAL   OXT  O  N N 431 
VAL   H    H  N N 432 
VAL   H2   H  N N 433 
VAL   HA   H  N N 434 
VAL   HB   H  N N 435 
VAL   HG11 H  N N 436 
VAL   HG12 H  N N 437 
VAL   HG13 H  N N 438 
VAL   HG21 H  N N 439 
VAL   HG22 H  N N 440 
VAL   HG23 H  N N 441 
VAL   HXT  H  N N 442 
# 
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 
A1ITH C11 C10  doub Y N 1   
A1ITH C11 C12  sing Y N 2   
A1ITH C10 C09  sing Y N 3   
A1ITH C13 C12  sing N N 4   
A1ITH C13 C14  sing N N 5   
A1ITH C12 C07  doub Y N 6   
A1ITH C14 C15  sing N N 7   
A1ITH C09 C08  doub Y N 8   
A1ITH C07 C08  sing Y N 9   
A1ITH C07 N06  sing N N 10  
A1ITH C15 C20  sing Y N 11  
A1ITH C15 C16  doub Y N 12  
A1ITH C01 N02  sing N N 13  
A1ITH C20 C19  doub Y N 14  
A1ITH N06 C16  sing N N 15  
A1ITH N06 C05  sing N N 16  
A1ITH N02 C03  sing N N 17  
A1ITH C03 C04  sing N N 18  
A1ITH C04 C05  sing N N 19  
A1ITH C16 C17  sing Y N 20  
A1ITH C19 C18  sing Y N 21  
A1ITH C17 C18  doub Y N 22  
A1ITH C18 CL21 sing N N 23  
A1ITH C01 H1   sing N N 24  
A1ITH C01 H2   sing N N 25  
A1ITH C01 H3   sing N N 26  
A1ITH N02 H4   sing N N 27  
A1ITH C03 H6   sing N N 28  
A1ITH C03 H7   sing N N 29  
A1ITH C04 H8   sing N N 30  
A1ITH C04 H9   sing N N 31  
A1ITH C05 H10  sing N N 32  
A1ITH C05 H11  sing N N 33  
A1ITH C08 H12  sing N N 34  
A1ITH C09 H13  sing N N 35  
A1ITH C10 H14  sing N N 36  
A1ITH C11 H15  sing N N 37  
A1ITH C13 H16  sing N N 38  
A1ITH C13 H17  sing N N 39  
A1ITH C14 H18  sing N N 40  
A1ITH C14 H19  sing N N 41  
A1ITH C17 H20  sing N N 42  
A1ITH C19 H21  sing N N 43  
A1ITH C20 H22  sing N N 44  
ALA   N   CA   sing N N 45  
ALA   N   H    sing N N 46  
ALA   N   H2   sing N N 47  
ALA   CA  C    sing N N 48  
ALA   CA  CB   sing N N 49  
ALA   CA  HA   sing N N 50  
ALA   C   O    doub N N 51  
ALA   C   OXT  sing N N 52  
ALA   CB  HB1  sing N N 53  
ALA   CB  HB2  sing N N 54  
ALA   CB  HB3  sing N N 55  
ALA   OXT HXT  sing N N 56  
ARG   N   CA   sing N N 57  
ARG   N   H    sing N N 58  
ARG   N   H2   sing N N 59  
ARG   CA  C    sing N N 60  
ARG   CA  CB   sing N N 61  
ARG   CA  HA   sing N N 62  
ARG   C   O    doub N N 63  
ARG   C   OXT  sing N N 64  
ARG   CB  CG   sing N N 65  
ARG   CB  HB2  sing N N 66  
ARG   CB  HB3  sing N N 67  
ARG   CG  CD   sing N N 68  
ARG   CG  HG2  sing N N 69  
ARG   CG  HG3  sing N N 70  
ARG   CD  NE   sing N N 71  
ARG   CD  HD2  sing N N 72  
ARG   CD  HD3  sing N N 73  
ARG   NE  CZ   sing N N 74  
ARG   NE  HE   sing N N 75  
ARG   CZ  NH1  sing N N 76  
ARG   CZ  NH2  doub N N 77  
ARG   NH1 HH11 sing N N 78  
ARG   NH1 HH12 sing N N 79  
ARG   NH2 HH21 sing N N 80  
ARG   NH2 HH22 sing N N 81  
ARG   OXT HXT  sing N N 82  
ASN   N   CA   sing N N 83  
ASN   N   H    sing N N 84  
ASN   N   H2   sing N N 85  
ASN   CA  C    sing N N 86  
ASN   CA  CB   sing N N 87  
ASN   CA  HA   sing N N 88  
ASN   C   O    doub N N 89  
ASN   C   OXT  sing N N 90  
ASN   CB  CG   sing N N 91  
ASN   CB  HB2  sing N N 92  
ASN   CB  HB3  sing N N 93  
ASN   CG  OD1  doub N N 94  
ASN   CG  ND2  sing N N 95  
ASN   ND2 HD21 sing N N 96  
ASN   ND2 HD22 sing N N 97  
ASN   OXT HXT  sing N N 98  
ASP   N   CA   sing N N 99  
ASP   N   H    sing N N 100 
ASP   N   H2   sing N N 101 
ASP   CA  C    sing N N 102 
ASP   CA  CB   sing N N 103 
ASP   CA  HA   sing N N 104 
ASP   C   O    doub N N 105 
ASP   C   OXT  sing N N 106 
ASP   CB  CG   sing N N 107 
ASP   CB  HB2  sing N N 108 
ASP   CB  HB3  sing N N 109 
ASP   CG  OD1  doub N N 110 
ASP   CG  OD2  sing N N 111 
ASP   OD2 HD2  sing N N 112 
ASP   OXT HXT  sing N N 113 
CYS   N   CA   sing N N 114 
CYS   N   H    sing N N 115 
CYS   N   H2   sing N N 116 
CYS   CA  C    sing N N 117 
CYS   CA  CB   sing N N 118 
CYS   CA  HA   sing N N 119 
CYS   C   O    doub N N 120 
CYS   C   OXT  sing N N 121 
CYS   CB  SG   sing N N 122 
CYS   CB  HB2  sing N N 123 
CYS   CB  HB3  sing N N 124 
CYS   SG  HG   sing N N 125 
CYS   OXT HXT  sing N N 126 
EDO   C1  O1   sing N N 127 
EDO   C1  C2   sing N N 128 
EDO   C1  H11  sing N N 129 
EDO   C1  H12  sing N N 130 
EDO   O1  HO1  sing N N 131 
EDO   C2  O2   sing N N 132 
EDO   C2  H21  sing N N 133 
EDO   C2  H22  sing N N 134 
EDO   O2  HO2  sing N N 135 
GLN   N   CA   sing N N 136 
GLN   N   H    sing N N 137 
GLN   N   H2   sing N N 138 
GLN   CA  C    sing N N 139 
GLN   CA  CB   sing N N 140 
GLN   CA  HA   sing N N 141 
GLN   C   O    doub N N 142 
GLN   C   OXT  sing N N 143 
GLN   CB  CG   sing N N 144 
GLN   CB  HB2  sing N N 145 
GLN   CB  HB3  sing N N 146 
GLN   CG  CD   sing N N 147 
GLN   CG  HG2  sing N N 148 
GLN   CG  HG3  sing N N 149 
GLN   CD  OE1  doub N N 150 
GLN   CD  NE2  sing N N 151 
GLN   NE2 HE21 sing N N 152 
GLN   NE2 HE22 sing N N 153 
GLN   OXT HXT  sing N N 154 
GLU   N   CA   sing N N 155 
GLU   N   H    sing N N 156 
GLU   N   H2   sing N N 157 
GLU   CA  C    sing N N 158 
GLU   CA  CB   sing N N 159 
GLU   CA  HA   sing N N 160 
GLU   C   O    doub N N 161 
GLU   C   OXT  sing N N 162 
GLU   CB  CG   sing N N 163 
GLU   CB  HB2  sing N N 164 
GLU   CB  HB3  sing N N 165 
GLU   CG  CD   sing N N 166 
GLU   CG  HG2  sing N N 167 
GLU   CG  HG3  sing N N 168 
GLU   CD  OE1  doub N N 169 
GLU   CD  OE2  sing N N 170 
GLU   OE2 HE2  sing N N 171 
GLU   OXT HXT  sing N N 172 
GLY   N   CA   sing N N 173 
GLY   N   H    sing N N 174 
GLY   N   H2   sing N N 175 
GLY   CA  C    sing N N 176 
GLY   CA  HA2  sing N N 177 
GLY   CA  HA3  sing N N 178 
GLY   C   O    doub N N 179 
GLY   C   OXT  sing N N 180 
GLY   OXT HXT  sing N N 181 
HIS   N   CA   sing N N 182 
HIS   N   H    sing N N 183 
HIS   N   H2   sing N N 184 
HIS   CA  C    sing N N 185 
HIS   CA  CB   sing N N 186 
HIS   CA  HA   sing N N 187 
HIS   C   O    doub N N 188 
HIS   C   OXT  sing N N 189 
HIS   CB  CG   sing N N 190 
HIS   CB  HB2  sing N N 191 
HIS   CB  HB3  sing N N 192 
HIS   CG  ND1  sing Y N 193 
HIS   CG  CD2  doub Y N 194 
HIS   ND1 CE1  doub Y N 195 
HIS   ND1 HD1  sing N N 196 
HIS   CD2 NE2  sing Y N 197 
HIS   CD2 HD2  sing N N 198 
HIS   CE1 NE2  sing Y N 199 
HIS   CE1 HE1  sing N N 200 
HIS   NE2 HE2  sing N N 201 
HIS   OXT HXT  sing N N 202 
HOH   O   H1   sing N N 203 
HOH   O   H2   sing N N 204 
ILE   N   CA   sing N N 205 
ILE   N   H    sing N N 206 
ILE   N   H2   sing N N 207 
ILE   CA  C    sing N N 208 
ILE   CA  CB   sing N N 209 
ILE   CA  HA   sing N N 210 
ILE   C   O    doub N N 211 
ILE   C   OXT  sing N N 212 
ILE   CB  CG1  sing N N 213 
ILE   CB  CG2  sing N N 214 
ILE   CB  HB   sing N N 215 
ILE   CG1 CD1  sing N N 216 
ILE   CG1 HG12 sing N N 217 
ILE   CG1 HG13 sing N N 218 
ILE   CG2 HG21 sing N N 219 
ILE   CG2 HG22 sing N N 220 
ILE   CG2 HG23 sing N N 221 
ILE   CD1 HD11 sing N N 222 
ILE   CD1 HD12 sing N N 223 
ILE   CD1 HD13 sing N N 224 
ILE   OXT HXT  sing N N 225 
LEU   N   CA   sing N N 226 
LEU   N   H    sing N N 227 
LEU   N   H2   sing N N 228 
LEU   CA  C    sing N N 229 
LEU   CA  CB   sing N N 230 
LEU   CA  HA   sing N N 231 
LEU   C   O    doub N N 232 
LEU   C   OXT  sing N N 233 
LEU   CB  CG   sing N N 234 
LEU   CB  HB2  sing N N 235 
LEU   CB  HB3  sing N N 236 
LEU   CG  CD1  sing N N 237 
LEU   CG  CD2  sing N N 238 
LEU   CG  HG   sing N N 239 
LEU   CD1 HD11 sing N N 240 
LEU   CD1 HD12 sing N N 241 
LEU   CD1 HD13 sing N N 242 
LEU   CD2 HD21 sing N N 243 
LEU   CD2 HD22 sing N N 244 
LEU   CD2 HD23 sing N N 245 
LEU   OXT HXT  sing N N 246 
LYS   N   CA   sing N N 247 
LYS   N   H    sing N N 248 
LYS   N   H2   sing N N 249 
LYS   CA  C    sing N N 250 
LYS   CA  CB   sing N N 251 
LYS   CA  HA   sing N N 252 
LYS   C   O    doub N N 253 
LYS   C   OXT  sing N N 254 
LYS   CB  CG   sing N N 255 
LYS   CB  HB2  sing N N 256 
LYS   CB  HB3  sing N N 257 
LYS   CG  CD   sing N N 258 
LYS   CG  HG2  sing N N 259 
LYS   CG  HG3  sing N N 260 
LYS   CD  CE   sing N N 261 
LYS   CD  HD2  sing N N 262 
LYS   CD  HD3  sing N N 263 
LYS   CE  NZ   sing N N 264 
LYS   CE  HE2  sing N N 265 
LYS   CE  HE3  sing N N 266 
LYS   NZ  HZ1  sing N N 267 
LYS   NZ  HZ2  sing N N 268 
LYS   NZ  HZ3  sing N N 269 
LYS   OXT HXT  sing N N 270 
MET   N   CA   sing N N 271 
MET   N   H    sing N N 272 
MET   N   H2   sing N N 273 
MET   CA  C    sing N N 274 
MET   CA  CB   sing N N 275 
MET   CA  HA   sing N N 276 
MET   C   O    doub N N 277 
MET   C   OXT  sing N N 278 
MET   CB  CG   sing N N 279 
MET   CB  HB2  sing N N 280 
MET   CB  HB3  sing N N 281 
MET   CG  SD   sing N N 282 
MET   CG  HG2  sing N N 283 
MET   CG  HG3  sing N N 284 
MET   SD  CE   sing N N 285 
MET   CE  HE1  sing N N 286 
MET   CE  HE2  sing N N 287 
MET   CE  HE3  sing N N 288 
MET   OXT HXT  sing N N 289 
PHE   N   CA   sing N N 290 
PHE   N   H    sing N N 291 
PHE   N   H2   sing N N 292 
PHE   CA  C    sing N N 293 
PHE   CA  CB   sing N N 294 
PHE   CA  HA   sing N N 295 
PHE   C   O    doub N N 296 
PHE   C   OXT  sing N N 297 
PHE   CB  CG   sing N N 298 
PHE   CB  HB2  sing N N 299 
PHE   CB  HB3  sing N N 300 
PHE   CG  CD1  doub Y N 301 
PHE   CG  CD2  sing Y N 302 
PHE   CD1 CE1  sing Y N 303 
PHE   CD1 HD1  sing N N 304 
PHE   CD2 CE2  doub Y N 305 
PHE   CD2 HD2  sing N N 306 
PHE   CE1 CZ   doub Y N 307 
PHE   CE1 HE1  sing N N 308 
PHE   CE2 CZ   sing Y N 309 
PHE   CE2 HE2  sing N N 310 
PHE   CZ  HZ   sing N N 311 
PHE   OXT HXT  sing N N 312 
PRO   N   CA   sing N N 313 
PRO   N   CD   sing N N 314 
PRO   N   H    sing N N 315 
PRO   CA  C    sing N N 316 
PRO   CA  CB   sing N N 317 
PRO   CA  HA   sing N N 318 
PRO   C   O    doub N N 319 
PRO   C   OXT  sing N N 320 
PRO   CB  CG   sing N N 321 
PRO   CB  HB2  sing N N 322 
PRO   CB  HB3  sing N N 323 
PRO   CG  CD   sing N N 324 
PRO   CG  HG2  sing N N 325 
PRO   CG  HG3  sing N N 326 
PRO   CD  HD2  sing N N 327 
PRO   CD  HD3  sing N N 328 
PRO   OXT HXT  sing N N 329 
SER   N   CA   sing N N 330 
SER   N   H    sing N N 331 
SER   N   H2   sing N N 332 
SER   CA  C    sing N N 333 
SER   CA  CB   sing N N 334 
SER   CA  HA   sing N N 335 
SER   C   O    doub N N 336 
SER   C   OXT  sing N N 337 
SER   CB  OG   sing N N 338 
SER   CB  HB2  sing N N 339 
SER   CB  HB3  sing N N 340 
SER   OG  HG   sing N N 341 
SER   OXT HXT  sing N N 342 
THR   N   CA   sing N N 343 
THR   N   H    sing N N 344 
THR   N   H2   sing N N 345 
THR   CA  C    sing N N 346 
THR   CA  CB   sing N N 347 
THR   CA  HA   sing N N 348 
THR   C   O    doub N N 349 
THR   C   OXT  sing N N 350 
THR   CB  OG1  sing N N 351 
THR   CB  CG2  sing N N 352 
THR   CB  HB   sing N N 353 
THR   OG1 HG1  sing N N 354 
THR   CG2 HG21 sing N N 355 
THR   CG2 HG22 sing N N 356 
THR   CG2 HG23 sing N N 357 
THR   OXT HXT  sing N N 358 
TRP   N   CA   sing N N 359 
TRP   N   H    sing N N 360 
TRP   N   H2   sing N N 361 
TRP   CA  C    sing N N 362 
TRP   CA  CB   sing N N 363 
TRP   CA  HA   sing N N 364 
TRP   C   O    doub N N 365 
TRP   C   OXT  sing N N 366 
TRP   CB  CG   sing N N 367 
TRP   CB  HB2  sing N N 368 
TRP   CB  HB3  sing N N 369 
TRP   CG  CD1  doub Y N 370 
TRP   CG  CD2  sing Y N 371 
TRP   CD1 NE1  sing Y N 372 
TRP   CD1 HD1  sing N N 373 
TRP   CD2 CE2  doub Y N 374 
TRP   CD2 CE3  sing Y N 375 
TRP   NE1 CE2  sing Y N 376 
TRP   NE1 HE1  sing N N 377 
TRP   CE2 CZ2  sing Y N 378 
TRP   CE3 CZ3  doub Y N 379 
TRP   CE3 HE3  sing N N 380 
TRP   CZ2 CH2  doub Y N 381 
TRP   CZ2 HZ2  sing N N 382 
TRP   CZ3 CH2  sing Y N 383 
TRP   CZ3 HZ3  sing N N 384 
TRP   CH2 HH2  sing N N 385 
TRP   OXT HXT  sing N N 386 
TYR   N   CA   sing N N 387 
TYR   N   H    sing N N 388 
TYR   N   H2   sing N N 389 
TYR   CA  C    sing N N 390 
TYR   CA  CB   sing N N 391 
TYR   CA  HA   sing N N 392 
TYR   C   O    doub N N 393 
TYR   C   OXT  sing N N 394 
TYR   CB  CG   sing N N 395 
TYR   CB  HB2  sing N N 396 
TYR   CB  HB3  sing N N 397 
TYR   CG  CD1  doub Y N 398 
TYR   CG  CD2  sing Y N 399 
TYR   CD1 CE1  sing Y N 400 
TYR   CD1 HD1  sing N N 401 
TYR   CD2 CE2  doub Y N 402 
TYR   CD2 HD2  sing N N 403 
TYR   CE1 CZ   doub Y N 404 
TYR   CE1 HE1  sing N N 405 
TYR   CE2 CZ   sing Y N 406 
TYR   CE2 HE2  sing N N 407 
TYR   CZ  OH   sing N N 408 
TYR   OH  HH   sing N N 409 
TYR   OXT HXT  sing N N 410 
VAL   N   CA   sing N N 411 
VAL   N   H    sing N N 412 
VAL   N   H2   sing N N 413 
VAL   CA  C    sing N N 414 
VAL   CA  CB   sing N N 415 
VAL   CA  HA   sing N N 416 
VAL   C   O    doub N N 417 
VAL   C   OXT  sing N N 418 
VAL   CB  CG1  sing N N 419 
VAL   CB  CG2  sing N N 420 
VAL   CB  HB   sing N N 421 
VAL   CG1 HG11 sing N N 422 
VAL   CG1 HG12 sing N N 423 
VAL   CG1 HG13 sing N N 424 
VAL   CG2 HG21 sing N N 425 
VAL   CG2 HG22 sing N N 426 
VAL   CG2 HG23 sing N N 427 
VAL   OXT HXT  sing N N 428 
# 
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                    9H9O 
_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]   0.005690 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000283 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.025714 
_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]   0.016668 
_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   ? -19.800 -42.263 22.945  1.00 89.66  ? 519  SER   A N    1 
ATOM   2    C  CA   . SER   A 1 1   ? -20.303 -41.556 21.770  1.00 89.06  ? 519  SER   A CA   1 
ATOM   3    C  C    . SER   A 1 1   ? -19.185 -41.090 20.840  1.00 87.27  ? 519  SER   A C    1 
ATOM   4    O  O    . SER   A 1 1   ? -18.006 -41.397 21.048  1.00 88.85  ? 519  SER   A O    1 
ATOM   5    C  CB   . SER   A 1 1   ? -21.150 -40.348 22.185  1.00 87.18  ? 519  SER   A CB   1 
ATOM   6    O  OG   . SER   A 1 1   ? -21.652 -39.661 21.044  1.00 81.47  ? 519  SER   A OG   1 
ATOM   7    N  N    . ARG   A 1 2   ? -19.570 -40.335 19.815  1.00 76.14  ? 520  ARG   A N    1 
ATOM   8    C  CA   . ARG   A 1 2   ? -18.620 -39.845 18.830  1.00 64.34  ? 520  ARG   A CA   1 
ATOM   9    C  C    . ARG   A 1 2   ? -18.465 -38.332 18.905  1.00 53.52  ? 520  ARG   A C    1 
ATOM   10   O  O    . ARG   A 1 2   ? -19.451 -37.607 19.025  1.00 48.79  ? 520  ARG   A O    1 
ATOM   11   C  CB   . ARG   A 1 2   ? -19.054 -40.259 17.422  1.00 60.70  ? 520  ARG   A CB   1 
ATOM   12   C  CG   . ARG   A 1 2   ? -18.803 -41.733 17.104  1.00 64.63  ? 520  ARG   A CG   1 
ATOM   13   C  CD   . ARG   A 1 2   ? -19.132 -42.023 15.650  1.00 66.96  ? 520  ARG   A CD   1 
ATOM   14   N  NE   . ARG   A 1 2   ? -20.484 -42.541 15.525  1.00 69.24  ? 520  ARG   A NE   1 
ATOM   15   C  CZ   . ARG   A 1 2   ? -20.784 -43.822 15.348  1.00 67.14  ? 520  ARG   A CZ   1 
ATOM   16   N  NH1  . ARG   A 1 2   ? -19.823 -44.726 15.245  1.00 72.48  ? 520  ARG   A NH1  1 
ATOM   17   N  NH2  . ARG   A 1 2   ? -22.051 -44.195 15.260  1.00 67.31  ? 520  ARG   A NH2  1 
ATOM   18   N  N    . ASP   A 1 3   ? -17.224 -37.864 18.837  1.00 46.38  ? 521  ASP   A N    1 
ATOM   19   C  CA   . ASP   A 1 3   ? -16.968 -36.439 18.723  1.00 49.13  ? 521  ASP   A CA   1 
ATOM   20   C  C    . ASP   A 1 3   ? -17.253 -36.009 17.285  1.00 46.38  ? 521  ASP   A C    1 
ATOM   21   O  O    . ASP   A 1 3   ? -17.673 -36.825 16.458  1.00 42.55  ? 521  ASP   A O    1 
ATOM   22   C  CB   . ASP   A 1 3   ? -15.531 -36.094 19.138  1.00 52.02  ? 521  ASP   A CB   1 
ATOM   23   C  CG   . ASP   A 1 3   ? -14.482 -36.802 18.290  1.00 56.13  ? 521  ASP   A CG   1 
ATOM   24   O  OD1  . ASP   A 1 3   ? -14.835 -37.500 17.306  1.00 50.70  ? 521  ASP   A OD1  1 
ATOM   25   O  OD2  . ASP   A 1 3   ? -13.290 -36.639 18.611  1.00 58.06  ? 521  ASP   A OD2  1 
ATOM   26   N  N    . TYR   A 1 4   ? -17.015 -34.739 16.985  1.00 42.85  ? 522  TYR   A N    1 
ATOM   27   C  CA   . TYR   A 1 4   ? -17.400 -34.189 15.690  1.00 37.96  ? 522  TYR   A CA   1 
ATOM   28   C  C    . TYR   A 1 4   ? -16.686 -34.882 14.539  1.00 35.22  ? 522  TYR   A C    1 
ATOM   29   O  O    . TYR   A 1 4   ? -17.321 -35.263 13.560  1.00 43.55  ? 522  TYR   A O    1 
ATOM   30   C  CB   . TYR   A 1 4   ? -17.119 -32.680 15.615  1.00 33.88  ? 522  TYR   A CB   1 
ATOM   31   C  CG   . TYR   A 1 4   ? -17.366 -32.139 14.227  1.00 42.76  ? 522  TYR   A CG   1 
ATOM   32   C  CD1  . TYR   A 1 4   ? -18.629 -32.184 13.673  1.00 41.20  ? 522  TYR   A CD1  1 
ATOM   33   C  CD2  . TYR   A 1 4   ? -16.337 -31.605 13.465  1.00 53.57  ? 522  TYR   A CD2  1 
ATOM   34   C  CE1  . TYR   A 1 4   ? -18.878 -31.698 12.413  1.00 46.03  ? 522  TYR   A CE1  1 
ATOM   35   C  CE2  . TYR   A 1 4   ? -16.580 -31.113 12.186  1.00 45.58  ? 522  TYR   A CE2  1 
ATOM   36   C  CZ   . TYR   A 1 4   ? -17.851 -31.171 11.672  1.00 43.82  ? 522  TYR   A CZ   1 
ATOM   37   O  OH   . TYR   A 1 4   ? -18.122 -30.701 10.407  1.00 53.44  ? 522  TYR   A OH   1 
ATOM   38   N  N    . LYS   A 1 5   ? -15.367 -35.026 14.649  1.00 42.80  ? 523  LYS   A N    1 
ATOM   39   C  CA   . LYS   A 1 5   ? -14.593 -35.645 13.573  1.00 44.58  ? 523  LYS   A CA   1 
ATOM   40   C  C    . LYS   A 1 5   ? -15.042 -37.086 13.292  1.00 44.62  ? 523  LYS   A C    1 
ATOM   41   O  O    . LYS   A 1 5   ? -15.170 -37.487 12.143  1.00 40.55  ? 523  LYS   A O    1 
ATOM   42   C  CB   . LYS   A 1 5   ? -13.116 -35.620 13.900  1.00 41.04  ? 523  LYS   A CB   1 
ATOM   43   C  CG   . LYS   A 1 5   ? -12.221 -36.144 12.785  1.00 42.92  ? 523  LYS   A CG   1 
ATOM   44   C  CD   . LYS   A 1 5   ? -10.778 -36.174 13.252  1.00 45.67  ? 523  LYS   A CD   1 
ATOM   45   C  CE   . LYS   A 1 5   ? -9.848  -36.618 12.141  1.00 47.49  ? 523  LYS   A CE   1 
ATOM   46   N  NZ   . LYS   A 1 5   ? -8.423  -36.424 12.515  1.00 50.74  ? 523  LYS   A NZ   1 
ATOM   47   N  N    . ARG   A 1 6   ? -15.304 -37.860 14.335  1.00 44.94  ? 524  ARG   A N    1 
ATOM   48   C  CA   . ARG   A 1 6   ? -15.747 -39.234 14.120  1.00 45.18  ? 524  ARG   A CA   1 
ATOM   49   C  C    . ARG   A 1 6   ? -17.168 -39.271 13.549  1.00 44.86  ? 524  ARG   A C    1 
ATOM   50   O  O    . ARG   A 1 6   ? -17.467 -40.088 12.688  1.00 38.68  ? 524  ARG   A O    1 
ATOM   51   C  CB   . ARG   A 1 6   ? -15.643 -40.040 15.405  1.00 42.85  ? 524  ARG   A CB   1 
ATOM   52   C  CG   . ARG   A 1 6   ? -14.456 -40.965 15.408  1.00 49.10  ? 524  ARG   A CG   1 
ATOM   53   C  CD   . ARG   A 1 6   ? -13.145 -40.244 15.083  1.00 55.00  ? 524  ARG   A CD   1 
ATOM   54   N  NE   . ARG   A 1 6   ? -12.756 -39.271 16.104  1.00 47.08  ? 524  ARG   A NE   1 
ATOM   55   C  CZ   . ARG   A 1 6   ? -11.568 -38.676 16.153  1.00 56.05  ? 524  ARG   A CZ   1 
ATOM   56   N  NH1  . ARG   A 1 6   ? -10.637 -38.969 15.256  1.00 60.45  ? 524  ARG   A NH1  1 
ATOM   57   N  NH2  . ARG   A 1 6   ? -11.296 -37.798 17.108  1.00 55.69  ? 524  ARG   A NH2  1 
ATOM   58   N  N    . LYS   A 1 7   ? -18.025 -38.351 13.987  1.00 38.26  ? 525  LYS   A N    1 
ATOM   59   C  CA   . LYS   A 1 7   ? -19.356 -38.213 13.395  1.00 38.22  ? 525  LYS   A CA   1 
ATOM   60   C  C    . LYS   A 1 7   ? -19.298 -37.903 11.902  1.00 37.60  ? 525  LYS   A C    1 
ATOM   61   O  O    . LYS   A 1 7   ? -20.073 -38.452 11.110  1.00 39.15  ? 525  LYS   A O    1 
ATOM   62   C  CB   . LYS   A 1 7   ? -20.145 -37.109 14.086  1.00 42.89  ? 525  LYS   A CB   1 
ATOM   63   C  CG   . LYS   A 1 7   ? -20.768 -37.463 15.410  1.00 42.40  ? 525  LYS   A CG   1 
ATOM   64   C  CD   . LYS   A 1 7   ? -21.605 -36.266 15.852  1.00 48.54  ? 525  LYS   A CD   1 
ATOM   65   C  CE   . LYS   A 1 7   ? -22.341 -36.516 17.135  1.00 47.70  ? 525  LYS   A CE   1 
ATOM   66   N  NZ   . LYS   A 1 7   ? -23.384 -35.496 17.278  1.00 41.38  ? 525  LYS   A NZ   1 
ATOM   67   N  N    . TYR   A 1 8   ? -18.386 -37.016 11.518  1.00 35.77  ? 526  TYR   A N    1 
ATOM   68   C  CA   . TYR   A 1 8   ? -18.278 -36.627 10.117  1.00 40.80  ? 526  TYR   A CA   1 
ATOM   69   C  C    . TYR   A 1 8   ? -17.829 -37.811 9.253   1.00 36.13  ? 526  TYR   A C    1 
ATOM   70   O  O    . TYR   A 1 8   ? -18.308 -37.988 8.138   1.00 35.94  ? 526  TYR   A O    1 
ATOM   71   C  CB   . TYR   A 1 8   ? -17.312 -35.457 9.923   1.00 41.03  ? 526  TYR   A CB   1 
ATOM   72   C  CG   . TYR   A 1 8   ? -17.257 -35.024 8.474   1.00 46.08  ? 526  TYR   A CG   1 
ATOM   73   C  CD1  . TYR   A 1 8   ? -18.258 -34.230 7.942   1.00 44.99  ? 526  TYR   A CD1  1 
ATOM   74   C  CD2  . TYR   A 1 8   ? -16.234 -35.448 7.626   1.00 49.14  ? 526  TYR   A CD2  1 
ATOM   75   C  CE1  . TYR   A 1 8   ? -18.239 -33.840 6.614   1.00 48.18  ? 526  TYR   A CE1  1 
ATOM   76   C  CE2  . TYR   A 1 8   ? -16.207 -35.058 6.285   1.00 41.23  ? 526  TYR   A CE2  1 
ATOM   77   C  CZ   . TYR   A 1 8   ? -17.220 -34.244 5.794   1.00 54.02  ? 526  TYR   A CZ   1 
ATOM   78   O  OH   . TYR   A 1 8   ? -17.246 -33.829 4.478   1.00 57.89  ? 526  TYR   A OH   1 
ATOM   79   N  N    . GLU   A 1 9   ? -16.908 -38.608 9.781   1.00 37.22  ? 527  GLU   A N    1 
ATOM   80   C  CA   . GLU   A 1 9   ? -16.410 -39.786 9.079   1.00 42.91  ? 527  GLU   A CA   1 
ATOM   81   C  C    . GLU   A 1 9   ? -17.531 -40.812 8.898   1.00 45.34  ? 527  GLU   A C    1 
ATOM   82   O  O    . GLU   A 1 9   ? -17.796 -41.273 7.800   1.00 38.64  ? 527  GLU   A O    1 
ATOM   83   C  CB   . GLU   A 1 9   ? -15.241 -40.402 9.843   1.00 46.20  ? 527  GLU   A CB   1 
ATOM   84   C  CG   . GLU   A 1 9   ? -14.039 -39.476 9.955   1.00 51.63  ? 527  GLU   A CG   1 
ATOM   85   C  CD   . GLU   A 1 9   ? -12.839 -40.120 10.626  1.00 55.22  ? 527  GLU   A CD   1 
ATOM   86   O  OE1  . GLU   A 1 9   ? -12.861 -41.341 10.899  1.00 65.52  ? 527  GLU   A OE1  1 
ATOM   87   O  OE2  . GLU   A 1 9   ? -11.863 -39.395 10.886  1.00 62.07  ? 527  GLU   A OE2  1 
ATOM   88   N  N    . PHE   A 1 10  ? -18.184 -41.146 10.001  1.00 38.05  ? 528  PHE   A N    1 
ATOM   89   C  CA   . PHE   A 1 10  ? -19.410 -41.926 9.995   1.00 37.89  ? 528  PHE   A CA   1 
ATOM   90   C  C    . PHE   A 1 10  ? -20.429 -41.421 8.956   1.00 35.77  ? 528  PHE   A C    1 
ATOM   91   O  O    . PHE   A 1 10  ? -20.897 -42.182 8.119   1.00 39.78  ? 528  PHE   A O    1 
ATOM   92   C  CB   . PHE   A 1 10  ? -20.005 -41.895 11.398  1.00 37.86  ? 528  PHE   A CB   1 
ATOM   93   C  CG   . PHE   A 1 10  ? -21.143 -42.831 11.601  1.00 44.15  ? 528  PHE   A CG   1 
ATOM   94   C  CD1  . PHE   A 1 10  ? -20.914 -44.179 11.843  1.00 43.30  ? 528  PHE   A CD1  1 
ATOM   95   C  CD2  . PHE   A 1 10  ? -22.447 -42.366 11.569  1.00 49.20  ? 528  PHE   A CD2  1 
ATOM   96   C  CE1  . PHE   A 1 10  ? -21.961 -45.046 12.041  1.00 47.31  ? 528  PHE   A CE1  1 
ATOM   97   C  CE2  . PHE   A 1 10  ? -23.503 -43.226 11.770  1.00 49.64  ? 528  PHE   A CE2  1 
ATOM   98   C  CZ   . PHE   A 1 10  ? -23.257 -44.576 12.012  1.00 50.28  ? 528  PHE   A CZ   1 
ATOM   99   N  N    . PHE   A 1 11  ? -20.768 -40.137 9.023   1.00 45.85  ? 529  PHE   A N    1 
ATOM   100  C  CA   . PHE   A 1 11  ? -21.666 -39.483 8.054   1.00 31.68  ? 529  PHE   A CA   1 
ATOM   101  C  C    . PHE   A 1 11  ? -21.290 -39.720 6.569   1.00 34.05  ? 529  PHE   A C    1 
ATOM   102  O  O    . PHE   A 1 11  ? -22.124 -40.132 5.755   1.00 36.94  ? 529  PHE   A O    1 
ATOM   103  C  CB   . PHE   A 1 11  ? -21.689 -37.987 8.366   1.00 34.15  ? 529  PHE   A CB   1 
ATOM   104  C  CG   . PHE   A 1 11  ? -22.401 -37.138 7.349   1.00 34.90  ? 529  PHE   A CG   1 
ATOM   105  C  CD1  . PHE   A 1 11  ? -23.778 -37.210 7.188   1.00 40.07  ? 529  PHE   A CD1  1 
ATOM   106  C  CD2  . PHE   A 1 11  ? -21.690 -36.204 6.599   1.00 34.33  ? 529  PHE   A CD2  1 
ATOM   107  C  CE1  . PHE   A 1 11  ? -24.438 -36.376 6.267   1.00 40.95  ? 529  PHE   A CE1  1 
ATOM   108  C  CE2  . PHE   A 1 11  ? -22.341 -35.365 5.680   1.00 33.82  ? 529  PHE   A CE2  1 
ATOM   109  C  CZ   . PHE   A 1 11  ? -23.713 -35.457 5.513   1.00 32.44  ? 529  PHE   A CZ   1 
ATOM   110  N  N    . ARG   A 1 12  ? -20.037 -39.456 6.217   1.00 35.69  ? 530  ARG   A N    1 
ATOM   111  C  CA   . ARG   A 1 12  ? -19.576 -39.689 4.850   1.00 39.00  ? 530  ARG   A CA   1 
ATOM   112  C  C    . ARG   A 1 12  ? -19.650 -41.163 4.439   1.00 46.54  ? 530  ARG   A C    1 
ATOM   113  O  O    . ARG   A 1 12  ? -19.953 -41.480 3.289   1.00 46.35  ? 530  ARG   A O    1 
ATOM   114  C  CB   . ARG   A 1 12  ? -18.145 -39.194 4.692   1.00 50.30  ? 530  ARG   A CB   1 
ATOM   115  C  CG   . ARG   A 1 12  ? -17.976 -37.726 5.006   1.00 53.56  ? 530  ARG   A CG   1 
ATOM   116  C  CD   . ARG   A 1 12  ? -18.809 -36.849 4.104   1.00 58.19  ? 530  ARG   A CD   1 
ATOM   117  N  NE   . ARG   A 1 12  ? -18.465 -37.005 2.695   1.00 60.86  ? 530  ARG   A NE   1 
ATOM   118  C  CZ   . ARG   A 1 12  ? -18.806 -36.136 1.748   1.00 65.38  ? 530  ARG   A CZ   1 
ATOM   119  N  NH1  . ARG   A 1 12  ? -19.483 -35.034 2.064   1.00 57.71  ? 530  ARG   A NH1  1 
ATOM   120  N  NH2  . ARG   A 1 12  ? -18.456 -36.361 0.488   1.00 72.05  ? 530  ARG   A NH2  1 
ATOM   121  N  N    . ARG   A 1 13  ? -19.344 -42.054 5.378   1.00 37.24  ? 531  ARG   A N    1 
ATOM   122  C  CA   . ARG   A 1 13  ? -19.477 -43.477 5.143   1.00 48.49  ? 531  ARG   A CA   1 
ATOM   123  C  C    . ARG   A 1 13  ? -20.911 -43.847 4.771   1.00 53.17  ? 531  ARG   A C    1 
ATOM   124  O  O    . ARG   A 1 13  ? -21.119 -44.726 3.936   1.00 49.94  ? 531  ARG   A O    1 
ATOM   125  C  CB   . ARG   A 1 13  ? -19.035 -44.267 6.369   1.00 44.63  ? 531  ARG   A CB   1 
ATOM   126  C  CG   . ARG   A 1 13  ? -17.816 -45.138 6.141   1.00 60.17  ? 531  ARG   A CG   1 
ATOM   127  C  CD   . ARG   A 1 13  ? -16.826 -45.013 7.285   1.00 68.95  ? 531  ARG   A CD   1 
ATOM   128  N  NE   . ARG   A 1 13  ? -17.433 -45.234 8.598   1.00 77.36  ? 531  ARG   A NE   1 
ATOM   129  C  CZ   . ARG   A 1 13  ? -16.845 -44.923 9.753   1.00 80.07  ? 531  ARG   A CZ   1 
ATOM   130  N  NH1  . ARG   A 1 13  ? -15.639 -44.365 9.761   1.00 79.00  ? 531  ARG   A NH1  1 
ATOM   131  N  NH2  . ARG   A 1 13  ? -17.465 -45.156 10.902  1.00 79.32  ? 531  ARG   A NH2  1 
ATOM   132  N  N    . LYS   A 1 14  ? -21.900 -43.187 5.374   1.00 36.80  ? 532  LYS   A N    1 
ATOM   133  C  CA   . LYS   A 1 14  ? -23.278 -43.536 5.063   1.00 42.57  ? 532  LYS   A CA   1 
ATOM   134  C  C    . LYS   A 1 14  ? -23.743 -42.842 3.801   1.00 39.85  ? 532  LYS   A C    1 
ATOM   135  O  O    . LYS   A 1 14  ? -24.642 -43.317 3.145   1.00 39.53  ? 532  LYS   A O    1 
ATOM   136  C  CB   . LYS   A 1 14  ? -24.210 -43.200 6.214   1.00 40.73  ? 532  LYS   A CB   1 
ATOM   137  C  CG   . LYS   A 1 14  ? -24.154 -44.196 7.355   1.00 37.48  ? 532  LYS   A CG   1 
ATOM   138  C  CD   . LYS   A 1 14  ? -25.260 -43.925 8.347   1.00 36.81  ? 532  LYS   A CD   1 
ATOM   139  C  CE   . LYS   A 1 14  ? -25.368 -45.052 9.354   1.00 44.94  ? 532  LYS   A CE   1 
ATOM   140  N  NZ   . LYS   A 1 14  ? -26.574 -44.892 10.197  1.00 42.22  ? 532  LYS   A NZ   1 
ATOM   141  N  N    . LEU   A 1 15  ? -23.132 -41.712 3.466   1.00 36.50  ? 533  LEU   A N    1 
ATOM   142  C  CA   . LEU   A 1 15  ? -23.473 -40.992 2.250   1.00 41.17  ? 533  LEU   A CA   1 
ATOM   143  C  C    . LEU   A 1 15  ? -22.929 -41.751 1.031   1.00 48.81  ? 533  LEU   A C    1 
ATOM   144  O  O    . LEU   A 1 15  ? -21.858 -41.444 0.523   1.00 61.28  ? 533  LEU   A O    1 
ATOM   145  C  CB   . LEU   A 1 15  ? -22.915 -39.569 2.328   1.00 44.19  ? 533  LEU   A CB   1 
ATOM   146  C  CG   . LEU   A 1 15  ? -23.593 -38.415 1.598   1.00 42.96  ? 533  LEU   A CG   1 
ATOM   147  C  CD1  . LEU   A 1 15  ? -25.071 -38.236 1.984   1.00 33.24  ? 533  LEU   A CD1  1 
ATOM   148  C  CD2  . LEU   A 1 15  ? -22.790 -37.152 1.890   1.00 33.54  ? 533  LEU   A CD2  1 
ATOM   149  N  N    . LYS   A 1 16  ? -23.665 -42.765 0.589   1.00 55.43  ? 534  LYS   A N    1 
ATOM   150  C  CA   . LYS   A 1 16  ? -23.237 -43.640 -0.506  1.00 51.41  ? 534  LYS   A CA   1 
ATOM   151  C  C    . LYS   A 1 16  ? -23.203 -42.922 -1.853  1.00 54.96  ? 534  LYS   A C    1 
ATOM   152  O  O    . LYS   A 1 16  ? -23.896 -41.924 -2.056  1.00 69.31  ? 534  LYS   A O    1 
ATOM   153  C  CB   . LYS   A 1 16  ? -24.160 -44.850 -0.587  1.00 49.87  ? 534  LYS   A CB   1 
ATOM   154  C  CG   . LYS   A 1 16  ? -24.156 -45.686 0.684   1.00 58.92  ? 534  LYS   A CG   1 
ATOM   155  C  CD   . LYS   A 1 16  ? -22.734 -46.068 1.036   1.00 62.87  ? 534  LYS   A CD   1 
ATOM   156  C  CE   . LYS   A 1 16  ? -22.698 -47.308 1.898   1.00 73.71  ? 534  LYS   A CE   1 
ATOM   157  N  NZ   . LYS   A 1 16  ? -23.592 -47.145 3.059   1.00 71.02  ? 534  LYS   A NZ   1 
ATOM   158  N  N    . LYS   A 1 17  ? -22.376 -43.410 -2.770  1.00 62.23  ? 535  LYS   A N    1 
ATOM   159  C  CA   . LYS   A 1 17  ? -22.249 -42.774 -4.084  1.00 72.30  ? 535  LYS   A CA   1 
ATOM   160  C  C    . LYS   A 1 17  ? -23.383 -43.197 -5.038  1.00 74.37  ? 535  LYS   A C    1 
ATOM   161  O  O    . LYS   A 1 17  ? -23.729 -44.403 -5.058  1.00 67.82  ? 535  LYS   A O    1 
ATOM   162  C  CB   . LYS   A 1 17  ? -20.855 -43.087 -4.680  1.00 72.41  ? 535  LYS   A CB   1 
ATOM   163  C  CG   . LYS   A 1 17  ? -20.522 -44.574 -4.823  1.00 80.55  ? 535  LYS   A CG   1 
ATOM   164  C  CD   . LYS   A 1 17  ? -19.100 -44.808 -5.353  1.00 84.07  ? 535  LYS   A CD   1 
ATOM   165  C  CE   . LYS   A 1 17  ? -18.809 -46.285 -5.553  1.00 93.21  ? 535  LYS   A CE   1 
ATOM   166  N  NZ   . LYS   A 1 17  ? -19.019 -47.014 -4.285  1.00 94.62  ? 535  LYS   A NZ   1 
ATOM   167  N  N    . GLN   A 1 18  ? -23.981 -42.240 -5.794  1.00 73.57  ? 536  GLN   A N    1 
ATOM   168  C  CA   . GLN   A 1 18  ? -24.907 -42.651 -6.885  1.00 79.42  ? 536  GLN   A CA   1 
ATOM   169  C  C    . GLN   A 1 18  ? -24.255 -43.293 -8.104  1.00 75.23  ? 536  GLN   A C    1 
ATOM   170  O  O    . GLN   A 1 18  ? -23.464 -42.683 -8.773  1.00 76.48  ? 536  GLN   A O    1 
ATOM   171  C  CB   . GLN   A 1 18  ? -25.764 -41.551 -7.507  1.00 87.48  ? 536  GLN   A CB   1 
ATOM   172  C  CG   . GLN   A 1 18  ? -26.705 -40.718 -6.650  1.00 86.58  ? 536  GLN   A CG   1 
ATOM   173  C  CD   . GLN   A 1 18  ? -27.794 -41.499 -6.021  1.00 84.26  ? 536  GLN   A CD   1 
ATOM   174  O  OE1  . GLN   A 1 18  ? -27.869 -42.745 -6.098  1.00 92.98  ? 536  GLN   A OE1  1 
ATOM   175  N  NE2  . GLN   A 1 18  ? -28.768 -40.758 -5.518  1.00 82.54  ? 536  GLN   A NE2  1 
ATOM   176  N  N    . ASN   A 1 19  ? -24.706 -44.480 -8.474  1.00 76.41  ? 537  ASN   A N    1 
ATOM   177  C  CA   . ASN   A 1 19  ? -24.205 -45.074 -9.708  1.00 80.07  ? 537  ASN   A CA   1 
ATOM   178  C  C    . ASN   A 1 19  ? -25.110 -44.871 -10.917 1.00 75.23  ? 537  ASN   A C    1 
ATOM   179  O  O    . ASN   A 1 19  ? -24.626 -44.867 -12.040 1.00 75.55  ? 537  ASN   A O    1 
ATOM   180  C  CB   . ASN   A 1 19  ? -23.939 -46.554 -9.505  1.00 88.86  ? 537  ASN   A CB   1 
ATOM   181  C  CG   . ASN   A 1 19  ? -22.692 -46.799 -8.685  1.00 91.38  ? 537  ASN   A CG   1 
ATOM   182  O  OD1  . ASN   A 1 19  ? -21.801 -45.950 -8.612  1.00 87.63  ? 537  ASN   A OD1  1 
ATOM   183  N  ND2  . ASN   A 1 19  ? -22.622 -47.965 -8.060  1.00 94.24  ? 537  ASN   A ND2  1 
ATOM   184  N  N    . ASP   A 1 20  ? -26.401 -44.649 -10.685 1.00 65.37  ? 538  ASP   A N    1 
ATOM   185  C  CA   . ASP   A 1 20  ? -27.375 -44.527 -11.767 1.00 58.70  ? 538  ASP   A CA   1 
ATOM   186  C  C    . ASP   A 1 20  ? -27.489 -43.085 -12.288 1.00 64.73  ? 538  ASP   A C    1 
ATOM   187  O  O    . ASP   A 1 20  ? -28.577 -42.618 -12.630 1.00 60.98  ? 538  ASP   A O    1 
ATOM   188  C  CB   . ASP   A 1 20  ? -28.737 -45.030 -11.290 1.00 50.40  ? 538  ASP   A CB   1 
ATOM   189  C  CG   . ASP   A 1 20  ? -29.268 -44.235 -10.105 1.00 58.72  ? 538  ASP   A CG   1 
ATOM   190  O  OD1  . ASP   A 1 20  ? -28.543 -43.336 -9.616  1.00 58.43  ? 538  ASP   A OD1  1 
ATOM   191  O  OD2  . ASP   A 1 20  ? -30.399 -44.514 -9.648  1.00 59.41  ? 538  ASP   A OD2  1 
ATOM   192  N  N    . ILE   A 1 21  ? -26.344 -42.409 -12.353 1.00 62.97  ? 539  ILE   A N    1 
ATOM   193  C  CA   . ILE   A 1 21  ? -26.232 -40.968 -12.608 1.00 62.74  ? 539  ILE   A CA   1 
ATOM   194  C  C    . ILE   A 1 21  ? -25.150 -40.730 -13.660 1.00 63.68  ? 539  ILE   A C    1 
ATOM   195  O  O    . ILE   A 1 21  ? -24.211 -41.520 -13.748 1.00 53.90  ? 539  ILE   A O    1 
ATOM   196  C  CB   . ILE   A 1 21  ? -25.885 -40.220 -11.283 1.00 61.96  ? 539  ILE   A CB   1 
ATOM   197  C  CG1  . ILE   A 1 21  ? -27.079 -40.243 -10.341 1.00 62.28  ? 539  ILE   A CG1  1 
ATOM   198  C  CG2  . ILE   A 1 21  ? -25.438 -38.803 -11.506 1.00 65.46  ? 539  ILE   A CG2  1 
ATOM   199  C  CD1  . ILE   A 1 21  ? -28.318 -39.707 -10.949 1.00 62.63  ? 539  ILE   A CD1  1 
ATOM   200  N  N    . PRO   A 1 22  ? -25.273 -39.666 -14.481 1.00 67.44  ? 540  PRO   A N    1 
ATOM   201  C  CA   . PRO   A 1 22  ? -24.119 -39.392 -15.354 1.00 65.75  ? 540  PRO   A CA   1 
ATOM   202  C  C    . PRO   A 1 22  ? -22.857 -39.096 -14.525 1.00 57.15  ? 540  PRO   A C    1 
ATOM   203  O  O    . PRO   A 1 22  ? -22.973 -38.675 -13.375 1.00 57.71  ? 540  PRO   A O    1 
ATOM   204  C  CB   . PRO   A 1 22  ? -24.566 -38.170 -16.164 1.00 66.31  ? 540  PRO   A CB   1 
ATOM   205  C  CG   . PRO   A 1 22  ? -26.066 -38.208 -16.128 1.00 69.54  ? 540  PRO   A CG   1 
ATOM   206  C  CD   . PRO   A 1 22  ? -26.428 -38.800 -14.788 1.00 66.96  ? 540  PRO   A CD   1 
ATOM   207  N  N    . ASN   A 1 23  ? -21.677 -39.321 -15.090 1.00 47.27  ? 541  ASN   A N    1 
ATOM   208  C  CA   . ASN   A 1 23  ? -20.444 -39.293 -14.304 1.00 54.75  ? 541  ASN   A CA   1 
ATOM   209  C  C    . ASN   A 1 23  ? -20.033 -37.873 -13.945 1.00 55.86  ? 541  ASN   A C    1 
ATOM   210  O  O    . ASN   A 1 23  ? -19.181 -37.661 -13.080 1.00 61.82  ? 541  ASN   A O    1 
ATOM   211  C  CB   . ASN   A 1 23  ? -19.300 -40.001 -15.052 1.00 67.24  ? 541  ASN   A CB   1 
ATOM   212  C  CG   . ASN   A 1 23  ? -18.854 -39.248 -16.292 1.00 84.75  ? 541  ASN   A CG   1 
ATOM   213  O  OD1  . ASN   A 1 23  ? -19.675 -38.782 -17.085 1.00 91.96  ? 541  ASN   A OD1  1 
ATOM   214  N  ND2  . ASN   A 1 23  ? -17.540 -39.126 -16.466 1.00 88.23  ? 541  ASN   A ND2  1 
ATOM   215  N  N    . LYS   A 1 24  ? -20.647 -36.898 -14.607 1.00 45.00  ? 542  LYS   A N    1 
ATOM   216  C  CA   . LYS   A 1 24  ? -20.439 -35.505 -14.238 1.00 51.76  ? 542  LYS   A CA   1 
ATOM   217  C  C    . LYS   A 1 24  ? -21.712 -34.674 -14.353 1.00 49.60  ? 542  LYS   A C    1 
ATOM   218  O  O    . LYS   A 1 24  ? -22.649 -34.999 -15.094 1.00 49.52  ? 542  LYS   A O    1 
ATOM   219  C  CB   . LYS   A 1 24  ? -19.322 -34.883 -15.086 1.00 58.69  ? 542  LYS   A CB   1 
ATOM   220  C  CG   . LYS   A 1 24  ? -19.453 -35.112 -16.588 1.00 70.01  ? 542  LYS   A CG   1 
ATOM   221  C  CD   . LYS   A 1 24  ? -18.175 -34.693 -17.322 1.00 69.64  ? 542  LYS   A CD   1 
ATOM   222  C  CE   . LYS   A 1 24  ? -18.329 -34.768 -18.835 1.00 73.36  ? 542  LYS   A CE   1 
ATOM   223  N  NZ   . LYS   A 1 24  ? -17.080 -34.343 -19.541 1.00 74.76  ? 542  LYS   A NZ   1 
ATOM   224  N  N    . PHE   A 1 25  ? -21.749 -33.607 -13.575 1.00 37.97  ? 543  PHE   A N    1 
ATOM   225  C  CA   . PHE   A 1 25  ? -22.799 -32.630 -13.715 1.00 42.89  ? 543  PHE   A CA   1 
ATOM   226  C  C    . PHE   A 1 25  ? -22.255 -31.377 -14.412 1.00 45.29  ? 543  PHE   A C    1 
ATOM   227  O  O    . PHE   A 1 25  ? -21.515 -30.607 -13.819 1.00 38.19  ? 543  PHE   A O    1 
ATOM   228  C  CB   . PHE   A 1 25  ? -23.387 -32.275 -12.358 1.00 38.47  ? 543  PHE   A CB   1 
ATOM   229  C  CG   . PHE   A 1 25  ? -24.432 -31.223 -12.441 1.00 44.68  ? 543  PHE   A CG   1 
ATOM   230  C  CD1  . PHE   A 1 25  ? -25.629 -31.483 -13.099 1.00 40.01  ? 543  PHE   A CD1  1 
ATOM   231  C  CD2  . PHE   A 1 25  ? -24.208 -29.960 -11.913 1.00 36.90  ? 543  PHE   A CD2  1 
ATOM   232  C  CE1  . PHE   A 1 25  ? -26.600 -30.501 -13.206 1.00 41.32  ? 543  PHE   A CE1  1 
ATOM   233  C  CE2  . PHE   A 1 25  ? -25.176 -28.973 -12.014 1.00 37.83  ? 543  PHE   A CE2  1 
ATOM   234  C  CZ   . PHE   A 1 25  ? -26.375 -29.240 -12.669 1.00 34.96  ? 543  PHE   A CZ   1 
ATOM   235  N  N    . GLU   A 1 26  ? -22.610 -31.183 -15.677 1.00 48.38  ? 544  GLU   A N    1 
ATOM   236  C  CA   . GLU   A 1 26  ? -22.088 -30.044 -16.420 1.00 46.39  ? 544  GLU   A CA   1 
ATOM   237  C  C    . GLU   A 1 26  ? -22.950 -28.813 -16.233 1.00 41.34  ? 544  GLU   A C    1 
ATOM   238  O  O    . GLU   A 1 26  ? -24.174 -28.876 -16.305 1.00 39.80  ? 544  GLU   A O    1 
ATOM   239  C  CB   . GLU   A 1 26  ? -21.964 -30.372 -17.902 1.00 41.79  ? 544  GLU   A CB   1 
ATOM   240  C  CG   . GLU   A 1 26  ? -20.825 -31.314 -18.196 1.00 54.59  ? 544  GLU   A CG   1 
ATOM   241  C  CD   . GLU   A 1 26  ? -20.487 -31.355 -19.664 1.00 69.42  ? 544  GLU   A CD   1 
ATOM   242  O  OE1  . GLU   A 1 26  ? -21.425 -31.468 -20.479 1.00 70.88  ? 544  GLU   A OE1  1 
ATOM   243  O  OE2  . GLU   A 1 26  ? -19.287 -31.264 -20.004 1.00 78.47  ? 544  GLU   A OE2  1 
ATOM   244  N  N    . MET   A 1 27  ? -22.296 -27.686 -15.986 1.00 36.36  ? 545  MET   A N    1 
ATOM   245  C  CA   . MET   A 1 27  ? -22.999 -26.435 -15.740 1.00 33.78  ? 545  MET   A CA   1 
ATOM   246  C  C    . MET   A 1 27  ? -22.192 -25.274 -16.303 1.00 43.37  ? 545  MET   A C    1 
ATOM   247  O  O    . MET   A 1 27  ? -21.131 -24.929 -15.781 1.00 50.93  ? 545  MET   A O    1 
ATOM   248  C  CB   . MET   A 1 27  ? -23.261 -26.255 -14.237 1.00 40.86  ? 545  MET   A CB   1 
ATOM   249  C  CG   . MET   A 1 27  ? -24.110 -25.019 -13.903 1.00 46.05  ? 545  MET   A CG   1 
ATOM   250  S  SD   . MET   A 1 27  ? -24.864 -25.040 -12.265 1.00 44.01  ? 545  MET   A SD   1 
ATOM   251  C  CE   . MET   A 1 27  ? -23.455 -25.489 -11.265 1.00 33.33  ? 545  MET   A CE   1 
ATOM   252  N  N    . LYS   A 1 28  ? -22.681 -24.693 -17.392 1.00 39.22  ? 546  LYS   A N    1 
ATOM   253  C  CA   . LYS   A 1 28  ? -22.022 -23.552 -17.993 1.00 37.04  ? 546  LYS   A CA   1 
ATOM   254  C  C    . LYS   A 1 28  ? -22.701 -22.267 -17.516 1.00 53.68  ? 546  LYS   A C    1 
ATOM   255  O  O    . LYS   A 1 28  ? -23.927 -22.140 -17.576 1.00 47.92  ? 546  LYS   A O    1 
ATOM   256  C  CB   . LYS   A 1 28  ? -22.050 -23.652 -19.515 1.00 43.64  ? 546  LYS   A CB   1 
ATOM   257  C  CG   . LYS   A 1 28  ? -21.433 -24.929 -20.051 1.00 44.98  ? 546  LYS   A CG   1 
ATOM   258  C  CD   . LYS   A 1 28  ? -21.253 -24.864 -21.568 1.00 54.50  ? 546  LYS   A CD   1 
ATOM   259  C  CE   . LYS   A 1 28  ? -20.564 -26.113 -22.102 1.00 53.34  ? 546  LYS   A CE   1 
ATOM   260  N  NZ   . LYS   A 1 28  ? -20.765 -26.257 -23.565 1.00 58.54  ? 546  LYS   A NZ   1 
ATOM   261  N  N    . LEU   A 1 29  ? -21.901 -21.329 -17.021 1.00 40.16  ? 547  LEU   A N    1 
ATOM   262  C  CA   . LEU   A 1 29  ? -22.431 -20.136 -16.384 1.00 40.92  ? 547  LEU   A CA   1 
ATOM   263  C  C    . LEU   A 1 29  ? -21.695 -18.904 -16.862 1.00 40.91  ? 547  LEU   A C    1 
ATOM   264  O  O    . LEU   A 1 29  ? -20.540 -18.990 -17.260 1.00 41.69  ? 547  LEU   A O    1 
ATOM   265  C  CB   . LEU   A 1 29  ? -22.308 -20.231 -14.856 1.00 42.12  ? 547  LEU   A CB   1 
ATOM   266  C  CG   . LEU   A 1 29  ? -22.822 -21.464 -14.113 1.00 35.12  ? 547  LEU   A CG   1 
ATOM   267  C  CD1  . LEU   A 1 29  ? -22.181 -21.526 -12.732 1.00 36.46  ? 547  LEU   A CD1  1 
ATOM   268  C  CD2  . LEU   A 1 29  ? -24.338 -21.436 -13.993 1.00 31.16  ? 547  LEU   A CD2  1 
ATOM   269  N  N    . ARG   A 1 30  ? -22.365 -17.758 -16.798 1.00 41.21  ? 548  ARG   A N    1 
ATOM   270  C  CA   . ARG   A 1 30  ? -21.724 -16.463 -17.008 1.00 43.10  ? 548  ARG   A CA   1 
ATOM   271  C  C    . ARG   A 1 30  ? -21.689 -15.707 -15.676 1.00 38.56  ? 548  ARG   A C    1 
ATOM   272  O  O    . ARG   A 1 30  ? -22.686 -15.678 -14.953 1.00 35.54  ? 548  ARG   A O    1 
ATOM   273  C  CB   . ARG   A 1 30  ? -22.461 -15.664 -18.085 1.00 50.44  ? 548  ARG   A CB   1 
ATOM   274  C  CG   . ARG   A 1 30  ? -22.505 -16.357 -19.461 1.00 55.53  ? 548  ARG   A CG   1 
ATOM   275  C  CD   . ARG   A 1 30  ? -23.685 -15.863 -20.303 1.00 61.37  ? 548  ARG   A CD   1 
ATOM   276  N  NE   . ARG   A 1 30  ? -24.960 -16.278 -19.714 1.00 70.82  ? 548  ARG   A NE   1 
ATOM   277  C  CZ   . ARG   A 1 30  ? -26.160 -15.901 -20.151 1.00 68.49  ? 548  ARG   A CZ   1 
ATOM   278  N  NH1  . ARG   A 1 30  ? -26.269 -15.086 -21.194 1.00 56.16  ? 548  ARG   A NH1  1 
ATOM   279  N  NH2  . ARG   A 1 30  ? -27.255 -16.337 -19.536 1.00 64.34  ? 548  ARG   A NH2  1 
ATOM   280  N  N    . ARG   A 1 31  ? -20.535 -15.141 -15.334 1.00 38.16  ? 549  ARG   A N    1 
ATOM   281  C  CA   . ARG   A 1 31  ? -20.370 -14.428 -14.062 1.00 51.12  ? 549  ARG   A CA   1 
ATOM   282  C  C    . ARG   A 1 31  ? -21.367 -13.284 -13.864 1.00 42.62  ? 549  ARG   A C    1 
ATOM   283  O  O    . ARG   A 1 31  ? -21.881 -13.082 -12.765 1.00 40.33  ? 549  ARG   A O    1 
ATOM   284  C  CB   . ARG   A 1 31  ? -18.950 -13.878 -13.936 1.00 52.03  ? 549  ARG   A CB   1 
ATOM   285  C  CG   . ARG   A 1 31  ? -17.898 -14.928 -13.620 1.00 53.61  ? 549  ARG   A CG   1 
ATOM   286  C  CD   . ARG   A 1 31  ? -16.517 -14.289 -13.513 1.00 56.34  ? 549  ARG   A CD   1 
ATOM   287  N  NE   . ARG   A 1 31  ? -15.495 -15.259 -13.143 1.00 60.66  ? 549  ARG   A NE   1 
ATOM   288  C  CZ   . ARG   A 1 31  ? -14.649 -15.814 -14.004 1.00 65.89  ? 549  ARG   A CZ   1 
ATOM   289  N  NH1  . ARG   A 1 31  ? -14.701 -15.492 -15.294 1.00 56.13  ? 549  ARG   A NH1  1 
ATOM   290  N  NH2  . ARG   A 1 31  ? -13.747 -16.686 -13.570 1.00 72.43  ? 549  ARG   A NH2  1 
ATOM   291  N  N    . ALA   A 1 32  ? -21.640 -12.542 -14.927 1.00 41.41  ? 550  ALA   A N    1 
ATOM   292  C  CA   . ALA   A 1 32  ? -22.578 -11.428 -14.849 1.00 44.58  ? 550  ALA   A CA   1 
ATOM   293  C  C    . ALA   A 1 32  ? -23.973 -11.915 -14.473 1.00 51.11  ? 550  ALA   A C    1 
ATOM   294  O  O    . ALA   A 1 32  ? -24.763 -11.163 -13.907 1.00 56.28  ? 550  ALA   A O    1 
ATOM   295  C  CB   . ALA   A 1 32  ? -22.617 -10.674 -16.173 1.00 42.70  ? 550  ALA   A CB   1 
ATOM   296  N  N    . THR   A 1 33  ? -24.272 -13.179 -14.776 1.00 46.22  ? 551  THR   A N    1 
ATOM   297  C  CA   . THR   A 1 33  ? -25.574 -13.745 -14.459 1.00 40.04  ? 551  THR   A CA   1 
ATOM   298  C  C    . THR   A 1 33  ? -25.470 -15.098 -13.755 1.00 46.02  ? 551  THR   A C    1 
ATOM   299  O  O    . THR   A 1 33  ? -26.204 -16.033 -14.110 1.00 36.48  ? 551  THR   A O    1 
ATOM   300  C  CB   . THR   A 1 33  ? -26.429 -13.937 -15.727 1.00 48.41  ? 551  THR   A CB   1 
ATOM   301  O  OG1  . THR   A 1 33  ? -25.711 -14.739 -16.671 1.00 44.02  ? 551  THR   A OG1  1 
ATOM   302  C  CG2  . THR   A 1 33  ? -26.776 -12.597 -16.378 1.00 58.87  ? 551  THR   A CG2  1 
ATOM   303  N  N    . VAL   A 1 34  ? -24.571 -15.214 -12.774 1.00 43.81  ? 552  VAL   A N    1 
ATOM   304  C  CA   . VAL   A 1 34  ? -24.351 -16.502 -12.104 1.00 35.03  ? 552  VAL   A CA   1 
ATOM   305  C  C    . VAL   A 1 34  ? -25.602 -17.024 -11.423 1.00 27.34  ? 552  VAL   A C    1 
ATOM   306  O  O    . VAL   A 1 34  ? -25.878 -18.218 -11.453 1.00 33.53  ? 552  VAL   A O    1 
ATOM   307  C  CB   . VAL   A 1 34  ? -23.260 -16.459 -10.997 1.00 41.51  ? 552  VAL   A CB   1 
ATOM   308  C  CG1  . VAL   A 1 34  ? -22.844 -17.886 -10.625 1.00 36.62  ? 552  VAL   A CG1  1 
ATOM   309  C  CG2  . VAL   A 1 34  ? -22.072 -15.740 -11.444 1.00 66.08  ? 552  VAL   A CG2  1 
ATOM   310  N  N    . LEU   A 1 35  ? -26.333 -16.135 -10.766 1.00 30.38  ? 553  LEU   A N    1 
ATOM   311  C  CA   . LEU   A 1 35  ? -27.490 -16.569 -9.983  1.00 32.20  ? 553  LEU   A CA   1 
ATOM   312  C  C    . LEU   A 1 35  ? -28.556 -17.125 -10.898 1.00 34.57  ? 553  LEU   A C    1 
ATOM   313  O  O    . LEU   A 1 35  ? -29.045 -18.218 -10.675 1.00 29.07  ? 553  LEU   A O    1 
ATOM   314  C  CB   . LEU   A 1 35  ? -28.064 -15.416 -9.137  1.00 34.29  ? 553  LEU   A CB   1 
ATOM   315  C  CG   . LEU   A 1 35  ? -29.246 -15.710 -8.198  1.00 29.17  ? 553  LEU   A CG   1 
ATOM   316  C  CD1  . LEU   A 1 35  ? -28.913 -16.831 -7.235  1.00 31.88  ? 553  LEU   A CD1  1 
ATOM   317  C  CD2  . LEU   A 1 35  ? -29.631 -14.462 -7.424  1.00 30.66  ? 553  LEU   A CD2  1 
ATOM   318  N  N    . GLU   A 1 36  ? -28.913 -16.374 -11.937 1.00 34.95  ? 554  GLU   A N    1 
ATOM   319  C  CA   . GLU   A 1 36  ? -29.976 -16.830 -12.820 1.00 42.85  ? 554  GLU   A CA   1 
ATOM   320  C  C    . GLU   A 1 36  ? -29.551 -18.092 -13.584 1.00 37.07  ? 554  GLU   A C    1 
ATOM   321  O  O    . GLU   A 1 36  ? -30.334 -19.025 -13.717 1.00 31.79  ? 554  GLU   A O    1 
ATOM   322  C  CB   . GLU   A 1 36  ? -30.397 -15.730 -13.794 1.00 47.07  ? 554  GLU   A CB   1 
ATOM   323  C  CG   . GLU   A 1 36  ? -31.770 -15.986 -14.435 1.00 66.52  ? 554  GLU   A CG   1 
ATOM   324  C  CD   . GLU   A 1 36  ? -32.572 -14.698 -14.700 1.00 79.53  ? 554  GLU   A CD   1 
ATOM   325  O  OE1  . GLU   A 1 36  ? -32.001 -13.585 -14.582 1.00 70.29  ? 554  GLU   A OE1  1 
ATOM   326  O  OE2  . GLU   A 1 36  ? -33.781 -14.807 -15.024 1.00 86.73  ? 554  GLU   A OE2  1 
ATOM   327  N  N    . ASP   A 1 37  ? -28.323 -18.124 -14.091 1.00 37.61  ? 555  ASP   A N    1 
ATOM   328  C  CA   . ASP   A 1 37  ? -27.869 -19.310 -14.808 1.00 38.56  ? 555  ASP   A CA   1 
ATOM   329  C  C    . ASP   A 1 37  ? -27.807 -20.557 -13.896 1.00 33.03  ? 555  ASP   A C    1 
ATOM   330  O  O    . ASP   A 1 37  ? -28.133 -21.660 -14.333 1.00 32.12  ? 555  ASP   A O    1 
ATOM   331  C  CB   . ASP   A 1 37  ? -26.500 -19.076 -15.438 1.00 37.95  ? 555  ASP   A CB   1 
ATOM   332  C  CG   . ASP   A 1 37  ? -26.517 -18.024 -16.533 1.00 39.94  ? 555  ASP   A CG   1 
ATOM   333  O  OD1  . ASP   A 1 37  ? -27.591 -17.690 -17.062 1.00 38.66  ? 555  ASP   A OD1  1 
ATOM   334  O  OD2  . ASP   A 1 37  ? -25.426 -17.541 -16.873 1.00 43.90  ? 555  ASP   A OD2  1 
ATOM   335  N  N    . SER   A 1 38  ? -27.352 -20.387 -12.651 1.00 33.36  ? 556  SER   A N    1 
ATOM   336  C  CA   . SER   A 1 38  ? -27.267 -21.508 -11.710 1.00 30.12  ? 556  SER   A CA   1 
ATOM   337  C  C    . SER   A 1 38  ? -28.662 -22.010 -11.363 1.00 27.64  ? 556  SER   A C    1 
ATOM   338  O  O    . SER   A 1 38  ? -28.907 -23.207 -11.291 1.00 30.95  ? 556  SER   A O    1 
ATOM   339  C  CB   . SER   A 1 38  ? -26.544 -21.114 -10.413 1.00 27.95  ? 556  SER   A CB   1 
ATOM   340  O  OG   . SER   A 1 38  ? -25.223 -20.688 -10.647 1.00 30.60  ? 556  SER   A OG   1 
ATOM   341  N  N    . TYR   A 1 39  ? -29.562 -21.072 -11.102 1.00 34.05  ? 557  TYR   A N    1 
ATOM   342  C  CA   . TYR   A 1 39  ? -30.938 -21.401 -10.754 1.00 31.24  ? 557  TYR   A CA   1 
ATOM   343  C  C    . TYR   A 1 39  ? -31.597 -22.206 -11.868 1.00 28.97  ? 557  TYR   A C    1 
ATOM   344  O  O    . TYR   A 1 39  ? -32.242 -23.211 -11.627 1.00 30.74  ? 557  TYR   A O    1 
ATOM   345  C  CB   . TYR   A 1 39  ? -31.743 -20.124 -10.485 1.00 25.16  ? 557  TYR   A CB   1 
ATOM   346  C  CG   . TYR   A 1 39  ? -33.241 -20.359 -10.362 1.00 29.29  ? 557  TYR   A CG   1 
ATOM   347  C  CD1  . TYR   A 1 39  ? -33.792 -20.856 -9.192  1.00 26.43  ? 557  TYR   A CD1  1 
ATOM   348  C  CD2  . TYR   A 1 39  ? -34.104 -20.034 -11.404 1.00 27.35  ? 557  TYR   A CD2  1 
ATOM   349  C  CE1  . TYR   A 1 39  ? -35.185 -21.054 -9.072  1.00 23.27  ? 557  TYR   A CE1  1 
ATOM   350  C  CE2  . TYR   A 1 39  ? -35.478 -20.225 -11.290 1.00 35.55  ? 557  TYR   A CE2  1 
ATOM   351  C  CZ   . TYR   A 1 39  ? -36.007 -20.750 -10.109 1.00 26.25  ? 557  TYR   A CZ   1 
ATOM   352  O  OH   . TYR   A 1 39  ? -37.366 -20.964 -10.004 1.00 31.38  ? 557  TYR   A OH   1 
ATOM   353  N  N    . ARG   A 1 40  ? -31.437 -21.747 -13.102 1.00 25.74  ? 558  ARG   A N    1 
ATOM   354  C  CA   . ARG   A 1 40  ? -32.072 -22.409 -14.228 1.00 27.05  ? 558  ARG   A CA   1 
ATOM   355  C  C    . ARG   A 1 40  ? -31.513 -23.818 -14.410 1.00 34.08  ? 558  ARG   A C    1 
ATOM   356  O  O    . ARG   A 1 40  ? -32.253 -24.764 -14.684 1.00 34.75  ? 558  ARG   A O    1 
ATOM   357  C  CB   . ARG   A 1 40  ? -31.881 -21.586 -15.506 1.00 38.09  ? 558  ARG   A CB   1 
ATOM   358  C  CG   . ARG   A 1 40  ? -32.709 -20.284 -15.546 1.00 44.74  ? 558  ARG   A CG   1 
ATOM   359  C  CD   . ARG   A 1 40  ? -32.488 -19.498 -16.842 1.00 56.98  ? 558  ARG   A CD   1 
ATOM   360  N  NE   . ARG   A 1 40  ? -33.337 -18.304 -16.915 1.00 72.69  ? 558  ARG   A NE   1 
ATOM   361  C  CZ   . ARG   A 1 40  ? -33.228 -17.353 -17.844 1.00 74.52  ? 558  ARG   A CZ   1 
ATOM   362  N  NH1  . ARG   A 1 40  ? -32.297 -17.444 -18.784 1.00 78.95  ? 558  ARG   A NH1  1 
ATOM   363  N  NH2  . ARG   A 1 40  ? -34.047 -16.306 -17.832 1.00 73.38  ? 558  ARG   A NH2  1 
ATOM   364  N  N    . ARG   A 1 41  ? -30.202 -23.968 -14.269 1.00 31.02  ? 559  ARG   A N    1 
ATOM   365  C  CA   . ARG   A 1 41  ? -29.615 -25.302 -14.409 1.00 31.32  ? 559  ARG   A CA   1 
ATOM   366  C  C    . ARG   A 1 41  ? -30.015 -26.217 -13.246 1.00 28.99  ? 559  ARG   A C    1 
ATOM   367  O  O    . ARG   A 1 41  ? -30.509 -27.316 -13.447 1.00 33.77  ? 559  ARG   A O    1 
ATOM   368  C  CB   . ARG   A 1 41  ? -28.087 -25.211 -14.500 1.00 35.43  ? 559  ARG   A CB   1 
ATOM   369  C  CG   . ARG   A 1 41  ? -27.391 -26.553 -14.679 1.00 33.25  ? 559  ARG   A CG   1 
ATOM   370  C  CD   . ARG   A 1 41  ? -27.587 -27.101 -16.073 1.00 34.60  ? 559  ARG   A CD   1 
ATOM   371  N  NE   . ARG   A 1 41  ? -26.796 -28.306 -16.262 1.00 41.79  ? 559  ARG   A NE   1 
ATOM   372  C  CZ   . ARG   A 1 41  ? -27.297 -29.529 -16.417 1.00 52.28  ? 559  ARG   A CZ   1 
ATOM   373  N  NH1  . ARG   A 1 41  ? -28.609 -29.717 -16.436 1.00 49.89  ? 559  ARG   A NH1  1 
ATOM   374  N  NH2  . ARG   A 1 41  ? -26.475 -30.567 -16.578 1.00 47.68  ? 559  ARG   A NH2  1 
ATOM   375  N  N    . ILE   A 1 42  ? -29.821 -25.752 -12.015 1.00 26.37  ? 560  ILE   A N    1 
ATOM   376  C  CA   . ILE   A 1 42  ? -29.979 -26.649 -10.867 1.00 26.14  ? 560  ILE   A CA   1 
ATOM   377  C  C    . ILE   A 1 42  ? -31.463 -26.989 -10.609 1.00 31.42  ? 560  ILE   A C    1 
ATOM   378  O  O    . ILE   A 1 42  ? -31.789 -28.102 -10.204 1.00 31.64  ? 560  ILE   A O    1 
ATOM   379  C  CB   . ILE   A 1 42  ? -29.290 -26.027 -9.636  1.00 34.37  ? 560  ILE   A CB   1 
ATOM   380  C  CG1  . ILE   A 1 42  ? -27.764 -26.104 -9.835  1.00 34.71  ? 560  ILE   A CG1  1 
ATOM   381  C  CG2  . ILE   A 1 42  ? -29.752 -26.660 -8.324  1.00 27.34  ? 560  ILE   A CG2  1 
ATOM   382  C  CD1  . ILE   A 1 42  ? -26.974 -25.387 -8.774  1.00 30.87  ? 560  ILE   A CD1  1 
ATOM   383  N  N    . MET   A 1 43  ? -32.369 -26.063 -10.897 1.00 26.84  ? 561  MET   A N    1 
ATOM   384  C  CA   . MET   A 1 43  ? -33.791 -26.373 -10.748 1.00 26.59  ? 561  MET   A CA   1 
ATOM   385  C  C    . MET   A 1 43  ? -34.376 -27.076 -11.978 1.00 30.88  ? 561  MET   A C    1 
ATOM   386  O  O    . MET   A 1 43  ? -35.466 -27.632 -11.919 1.00 37.83  ? 561  MET   A O    1 
ATOM   387  C  CB   . MET   A 1 43  ? -34.574 -25.101 -10.443 1.00 25.80  ? 561  MET   A CB   1 
ATOM   388  C  CG   . MET   A 1 43  ? -34.144 -24.506 -9.119  1.00 28.31  ? 561  MET   A CG   1 
ATOM   389  S  SD   . MET   A 1 43  ? -34.286 -25.702 -7.756  1.00 38.44  ? 561  MET   A SD   1 
ATOM   390  C  CE   . MET   A 1 43  ? -36.061 -25.766 -7.609  1.00 32.68  ? 561  MET   A CE   1 
ATOM   391  N  N    . GLY   A 1 44  ? -33.649 -27.060 -13.085 1.00 27.49  ? 562  GLY   A N    1 
ATOM   392  C  CA   . GLY   A 1 44  ? -34.149 -27.685 -14.304 1.00 29.00  ? 562  GLY   A CA   1 
ATOM   393  C  C    . GLY   A 1 44  ? -33.805 -29.170 -14.465 1.00 29.90  ? 562  GLY   A C    1 
ATOM   394  O  O    . GLY   A 1 44  ? -34.366 -29.818 -15.344 1.00 33.32  ? 562  GLY   A O    1 
ATOM   395  N  N    . VAL   A 1 45  ? -32.892 -29.704 -13.644 1.00 35.71  ? 563  VAL   A N    1 
ATOM   396  C  CA   . VAL   A 1 45  ? -32.425 -31.097 -13.795 1.00 36.16  ? 563  VAL   A CA   1 
ATOM   397  C  C    . VAL   A 1 45  ? -33.576 -32.103 -13.713 1.00 36.65  ? 563  VAL   A C    1 
ATOM   398  O  O    . VAL   A 1 45  ? -34.541 -31.895 -12.986 1.00 37.53  ? 563  VAL   A O    1 
ATOM   399  C  CB   . VAL   A 1 45  ? -31.350 -31.474 -12.731 1.00 37.54  ? 563  VAL   A CB   1 
ATOM   400  C  CG1  . VAL   A 1 45  ? -30.091 -30.664 -12.939 1.00 37.27  ? 563  VAL   A CG1  1 
ATOM   401  C  CG2  . VAL   A 1 45  ? -31.885 -31.315 -11.278 1.00 30.94  ? 563  VAL   A CG2  1 
ATOM   402  N  N    . LYS   A 1 46  ? -33.472 -33.185 -14.480 1.00 33.29  ? 564  LYS   A N    1 
ATOM   403  C  CA   . LYS   A 1 46  ? -34.521 -34.192 -14.520 1.00 34.71  ? 564  LYS   A CA   1 
ATOM   404  C  C    . LYS   A 1 46  ? -34.649 -34.828 -13.130 1.00 37.11  ? 564  LYS   A C    1 
ATOM   405  O  O    . LYS   A 1 46  ? -35.741 -35.090 -12.649 1.00 40.04  ? 564  LYS   A O    1 
ATOM   406  C  CB   . LYS   A 1 46  ? -34.210 -35.240 -15.591 1.00 37.18  ? 564  LYS   A CB   1 
ATOM   407  C  CG   . LYS   A 1 46  ? -35.434 -35.927 -16.232 1.00 61.40  ? 564  LYS   A CG   1 
ATOM   408  C  CD   . LYS   A 1 46  ? -36.112 -36.929 -15.324 1.00 56.43  ? 564  LYS   A CD   1 
ATOM   409  C  CE   . LYS   A 1 46  ? -37.530 -37.289 -15.789 1.00 57.88  ? 564  LYS   A CE   1 
ATOM   410  N  NZ   . LYS   A 1 46  ? -37.637 -37.918 -17.148 1.00 66.99  ? 564  LYS   A NZ   1 
ATOM   411  N  N    . ARG   A 1 47  ? -33.513 -35.048 -12.486 1.00 35.66  ? 565  ARG   A N    1 
ATOM   412  C  CA   . ARG   A 1 47  ? -33.461 -35.675 -11.166 1.00 39.29  ? 565  ARG   A CA   1 
ATOM   413  C  C    . ARG   A 1 47  ? -32.481 -34.924 -10.307 1.00 40.62  ? 565  ARG   A C    1 
ATOM   414  O  O    . ARG   A 1 47  ? -31.397 -34.556 -10.765 1.00 41.23  ? 565  ARG   A O    1 
ATOM   415  C  CB   . ARG   A 1 47  ? -33.036 -37.146 -11.251 1.00 35.07  ? 565  ARG   A CB   1 
ATOM   416  C  CG   . ARG   A 1 47  ? -33.975 -38.058 -12.006 1.00 38.89  ? 565  ARG   A CG   1 
ATOM   417  C  CD   . ARG   A 1 47  ? -33.331 -39.436 -12.205 1.00 45.04  ? 565  ARG   A CD   1 
ATOM   418  N  NE   . ARG   A 1 47  ? -32.747 -39.933 -10.960 1.00 54.21  ? 565  ARG   A NE   1 
ATOM   419  C  CZ   . ARG   A 1 47  ? -31.745 -40.809 -10.893 1.00 53.37  ? 565  ARG   A CZ   1 
ATOM   420  N  NH1  . ARG   A 1 47  ? -31.204 -41.290 -12.005 1.00 45.06  ? 565  ARG   A NH1  1 
ATOM   421  N  NH2  . ARG   A 1 47  ? -31.278 -41.202 -9.711  1.00 47.49  ? 565  ARG   A NH2  1 
ATOM   422  N  N    . ALA   A 1 48  ? -32.847 -34.701 -9.053  1.00 38.04  ? 566  ALA   A N    1 
ATOM   423  C  CA   . ALA   A 1 48  ? -31.954 -33.998 -8.143  1.00 31.75  ? 566  ALA   A CA   1 
ATOM   424  C  C    . ALA   A 1 48  ? -30.660 -34.794 -7.937  1.00 31.91  ? 566  ALA   A C    1 
ATOM   425  O  O    . ALA   A 1 48  ? -29.608 -34.220 -7.684  1.00 33.98  ? 566  ALA   A O    1 
ATOM   426  C  CB   . ALA   A 1 48  ? -32.651 -33.736 -6.808  1.00 35.22  ? 566  ALA   A CB   1 
ATOM   427  N  N    . ASP   A 1 49  ? -30.747 -36.113 -8.070  1.00 34.21  ? 567  ASP   A N    1 
ATOM   428  C  CA   . ASP   A 1 49  ? -29.582 -36.987 -7.965  1.00 38.97  ? 567  ASP   A CA   1 
ATOM   429  C  C    . ASP   A 1 49  ? -28.475 -36.642 -8.964  1.00 42.28  ? 567  ASP   A C    1 
ATOM   430  O  O    . ASP   A 1 49  ? -27.302 -36.882 -8.689  1.00 39.82  ? 567  ASP   A O    1 
ATOM   431  C  CB   . ASP   A 1 49  ? -29.999 -38.453 -8.153  1.00 44.49  ? 567  ASP   A CB   1 
ATOM   432  C  CG   . ASP   A 1 49  ? -30.852 -38.979 -7.002  1.00 49.06  ? 567  ASP   A CG   1 
ATOM   433  O  OD1  . ASP   A 1 49  ? -30.600 -38.571 -5.842  1.00 49.52  ? 567  ASP   A OD1  1 
ATOM   434  O  OD2  . ASP   A 1 49  ? -31.762 -39.814 -7.265  1.00 49.29  ? 567  ASP   A OD2  1 
ATOM   435  N  N    . PHE   A 1 50  ? -28.845 -36.075 -10.116 1.00 45.91  ? 568  PHE   A N    1 
ATOM   436  C  CA   . PHE   A 1 50  ? -27.857 -35.596 -11.097 1.00 43.98  ? 568  PHE   A CA   1 
ATOM   437  C  C    . PHE   A 1 50  ? -26.850 -34.635 -10.457 1.00 37.01  ? 568  PHE   A C    1 
ATOM   438  O  O    . PHE   A 1 50  ? -25.698 -34.533 -10.877 1.00 35.07  ? 568  PHE   A O    1 
ATOM   439  C  CB   . PHE   A 1 50  ? -28.543 -34.902 -12.285 1.00 31.75  ? 568  PHE   A CB   1 
ATOM   440  C  CG   . PHE   A 1 50  ? -29.282 -35.847 -13.214 1.00 33.87  ? 568  PHE   A CG   1 
ATOM   441  C  CD1  . PHE   A 1 50  ? -29.226 -37.217 -13.029 1.00 35.42  ? 568  PHE   A CD1  1 
ATOM   442  C  CD2  . PHE   A 1 50  ? -30.014 -35.354 -14.289 1.00 48.73  ? 568  PHE   A CD2  1 
ATOM   443  C  CE1  . PHE   A 1 50  ? -29.893 -38.089 -13.885 1.00 51.61  ? 568  PHE   A CE1  1 
ATOM   444  C  CE2  . PHE   A 1 50  ? -30.689 -36.226 -15.161 1.00 47.53  ? 568  PHE   A CE2  1 
ATOM   445  C  CZ   . PHE   A 1 50  ? -30.626 -37.588 -14.955 1.00 44.28  ? 568  PHE   A CZ   1 
ATOM   446  N  N    . LEU   A 1 51  ? -27.288 -33.943 -9.420  1.00 34.42  ? 569  LEU   A N    1 
ATOM   447  C  CA   . LEU   A 1 51  ? -26.440 -32.951 -8.756  1.00 36.82  ? 569  LEU   A CA   1 
ATOM   448  C  C    . LEU   A 1 51  ? -25.388 -33.576 -7.838  1.00 33.90  ? 569  LEU   A C    1 
ATOM   449  O  O    . LEU   A 1 51  ? -24.603 -32.865 -7.226  1.00 36.20  ? 569  LEU   A O    1 
ATOM   450  C  CB   . LEU   A 1 51  ? -27.304 -31.976 -7.959  1.00 38.22  ? 569  LEU   A CB   1 
ATOM   451  C  CG   . LEU   A 1 51  ? -28.423 -31.319 -8.761  1.00 34.61  ? 569  LEU   A CG   1 
ATOM   452  C  CD1  . LEU   A 1 51  ? -29.357 -30.652 -7.789  1.00 36.49  ? 569  LEU   A CD1  1 
ATOM   453  C  CD2  . LEU   A 1 51  ? -27.846 -30.303 -9.773  1.00 29.11  ? 569  LEU   A CD2  1 
ATOM   454  N  N    . LYS   A 1 52  ? -25.373 -34.901 -7.761  1.00 35.88  ? 570  LYS   A N    1 
ATOM   455  C  CA   . LYS   A 1 52  ? -24.426 -35.625 -6.922  1.00 41.22  ? 570  LYS   A CA   1 
ATOM   456  C  C    . LYS   A 1 52  ? -23.190 -36.050 -7.700  1.00 45.73  ? 570  LYS   A C    1 
ATOM   457  O  O    . LYS   A 1 52  ? -22.212 -36.518 -7.118  1.00 47.05  ? 570  LYS   A O    1 
ATOM   458  C  CB   . LYS   A 1 52  ? -25.099 -36.856 -6.302  1.00 34.04  ? 570  LYS   A CB   1 
ATOM   459  C  CG   . LYS   A 1 52  ? -26.244 -36.479 -5.360  1.00 34.48  ? 570  LYS   A CG   1 
ATOM   460  C  CD   . LYS   A 1 52  ? -26.967 -37.700 -4.855  1.00 38.24  ? 570  LYS   A CD   1 
ATOM   461  C  CE   . LYS   A 1 52  ? -27.981 -37.309 -3.787  1.00 39.14  ? 570  LYS   A CE   1 
ATOM   462  N  NZ   . LYS   A 1 52  ? -28.931 -38.435 -3.585  1.00 43.40  ? 570  LYS   A NZ   1 
ATOM   463  N  N    . ALA   A 1 53  ? -23.248 -35.903 -9.019  1.00 43.03  ? 571  ALA   A N    1 
ATOM   464  C  CA   . ALA   A 1 53  ? -22.102 -36.211 -9.859  1.00 43.21  ? 571  ALA   A CA   1 
ATOM   465  C  C    . ALA   A 1 53  ? -21.030 -35.135 -9.685  1.00 44.65  ? 571  ALA   A C    1 
ATOM   466  O  O    . ALA   A 1 53  ? -21.301 -34.062 -9.141  1.00 36.01  ? 571  ALA   A O    1 
ATOM   467  C  CB   . ALA   A 1 53  ? -22.522 -36.324 -11.310 1.00 38.55  ? 571  ALA   A CB   1 
ATOM   468  N  N    . ARG   A 1 54  ? -19.820 -35.437 -10.141 1.00 45.24  ? 572  ARG   A N    1 
ATOM   469  C  CA   . ARG   A 1 54  ? -18.700 -34.511 -10.070 1.00 49.57  ? 572  ARG   A CA   1 
ATOM   470  C  C    . ARG   A 1 54  ? -19.034 -33.211 -10.786 1.00 47.46  ? 572  ARG   A C    1 
ATOM   471  O  O    . ARG   A 1 54  ? -19.400 -33.220 -11.964 1.00 44.64  ? 572  ARG   A O    1 
ATOM   472  C  CB   . ARG   A 1 54  ? -17.441 -35.138 -10.680 1.00 60.26  ? 572  ARG   A CB   1 
ATOM   473  C  CG   . ARG   A 1 54  ? -16.211 -34.241 -10.589 1.00 70.73  ? 572  ARG   A CG   1 
ATOM   474  C  CD   . ARG   A 1 54  ? -14.979 -34.939 -11.125 1.00 77.71  ? 572  ARG   A CD   1 
ATOM   475  N  NE   . ARG   A 1 54  ? -14.703 -36.162 -10.381 1.00 87.09  ? 572  ARG   A NE   1 
ATOM   476  C  CZ   . ARG   A 1 54  ? -13.707 -36.998 -10.658 1.00 87.32  ? 572  ARG   A CZ   1 
ATOM   477  N  NH1  . ARG   A 1 54  ? -12.885 -36.750 -11.672 1.00 90.69  ? 572  ARG   A NH1  1 
ATOM   478  N  NH2  . ARG   A 1 54  ? -13.536 -38.087 -9.919  1.00 88.05  ? 572  ARG   A NH2  1 
ATOM   479  N  N    . LEU   A 1 55  ? -18.917 -32.097 -10.070 1.00 48.22  ? 573  LEU   A N    1 
ATOM   480  C  CA   . LEU   A 1 55  ? -19.302 -30.806 -10.623 1.00 45.01  ? 573  LEU   A CA   1 
ATOM   481  C  C    . LEU   A 1 55  ? -18.344 -30.410 -11.729 1.00 40.33  ? 573  LEU   A C    1 
ATOM   482  O  O    . LEU   A 1 55  ? -17.122 -30.378 -11.552 1.00 39.28  ? 573  LEU   A O    1 
ATOM   483  C  CB   . LEU   A 1 55  ? -19.343 -29.732 -9.538  1.00 42.55  ? 573  LEU   A CB   1 
ATOM   484  C  CG   . LEU   A 1 55  ? -20.185 -30.074 -8.313  1.00 42.65  ? 573  LEU   A CG   1 
ATOM   485  C  CD1  . LEU   A 1 55  ? -20.139 -28.935 -7.319  1.00 41.97  ? 573  LEU   A CD1  1 
ATOM   486  C  CD2  . LEU   A 1 55  ? -21.627 -30.388 -8.710  1.00 47.02  ? 573  LEU   A CD2  1 
ATOM   487  N  N    . TRP   A 1 56  ? -18.932 -30.125 -12.882 1.00 40.05  ? 574  TRP   A N    1 
ATOM   488  C  CA   . TRP   A 1 56  ? -18.203 -29.786 -14.090 1.00 51.30  ? 574  TRP   A CA   1 
ATOM   489  C  C    . TRP   A 1 56  ? -18.597 -28.378 -14.528 1.00 47.66  ? 574  TRP   A C    1 
ATOM   490  O  O    . TRP   A 1 56  ? -19.372 -28.213 -15.469 1.00 43.97  ? 574  TRP   A O    1 
ATOM   491  C  CB   . TRP   A 1 56  ? -18.518 -30.808 -15.187 1.00 59.16  ? 574  TRP   A CB   1 
ATOM   492  C  CG   . TRP   A 1 56  ? -17.337 -31.280 -15.967 1.00 64.55  ? 574  TRP   A CG   1 
ATOM   493  C  CD1  . TRP   A 1 56  ? -17.084 -31.053 -17.294 1.00 70.09  ? 574  TRP   A CD1  1 
ATOM   494  C  CD2  . TRP   A 1 56  ? -16.251 -32.084 -15.483 1.00 67.91  ? 574  TRP   A CD2  1 
ATOM   495  N  NE1  . TRP   A 1 56  ? -15.902 -31.658 -17.660 1.00 68.26  ? 574  TRP   A NE1  1 
ATOM   496  C  CE2  . TRP   A 1 56  ? -15.372 -32.296 -16.566 1.00 70.26  ? 574  TRP   A CE2  1 
ATOM   497  C  CE3  . TRP   A 1 56  ? -15.932 -32.637 -14.237 1.00 62.80  ? 574  TRP   A CE3  1 
ATOM   498  C  CZ2  . TRP   A 1 56  ? -14.200 -33.036 -16.441 1.00 77.48  ? 574  TRP   A CZ2  1 
ATOM   499  C  CZ3  . TRP   A 1 56  ? -14.774 -33.364 -14.114 1.00 64.50  ? 574  TRP   A CZ3  1 
ATOM   500  C  CH2  . TRP   A 1 56  ? -13.920 -33.562 -15.208 1.00 76.86  ? 574  TRP   A CH2  1 
ATOM   501  N  N    . ILE   A 1 57  ? -18.074 -27.367 -13.836 1.00 51.46  ? 575  ILE   A N    1 
ATOM   502  C  CA   . ILE   A 1 57  ? -18.542 -25.988 -14.014 1.00 43.92  ? 575  ILE   A CA   1 
ATOM   503  C  C    . ILE   A 1 57  ? -17.586 -25.171 -14.875 1.00 49.29  ? 575  ILE   A C    1 
ATOM   504  O  O    . ILE   A 1 57  ? -16.369 -25.301 -14.772 1.00 47.23  ? 575  ILE   A O    1 
ATOM   505  C  CB   . ILE   A 1 57  ? -18.736 -25.295 -12.646 1.00 46.33  ? 575  ILE   A CB   1 
ATOM   506  C  CG1  . ILE   A 1 57  ? -19.707 -26.106 -11.775 1.00 39.80  ? 575  ILE   A CG1  1 
ATOM   507  C  CG2  . ILE   A 1 57  ? -19.222 -23.854 -12.822 1.00 49.65  ? 575  ILE   A CG2  1 
ATOM   508  C  CD1  . ILE   A 1 57  ? -19.807 -25.619 -10.320 1.00 38.83  ? 575  ILE   A CD1  1 
ATOM   509  N  N    . GLU   A 1 58  ? -18.152 -24.337 -15.735 1.00 44.36  ? 576  GLU   A N    1 
ATOM   510  C  CA   . GLU   A 1 58  ? -17.377 -23.528 -16.655 1.00 44.13  ? 576  GLU   A CA   1 
ATOM   511  C  C    . GLU   A 1 58  ? -17.890 -22.087 -16.642 1.00 49.14  ? 576  GLU   A C    1 
ATOM   512  O  O    . GLU   A 1 58  ? -19.079 -21.851 -16.822 1.00 46.03  ? 576  GLU   A O    1 
ATOM   513  C  CB   . GLU   A 1 58  ? -17.484 -24.116 -18.053 1.00 46.61  ? 576  GLU   A CB   1 
ATOM   514  C  CG   . GLU   A 1 58  ? -16.503 -23.614 -19.055 1.00 59.85  ? 576  GLU   A CG   1 
ATOM   515  C  CD   . GLU   A 1 58  ? -16.811 -24.169 -20.424 1.00 74.57  ? 576  GLU   A CD   1 
ATOM   516  O  OE1  . GLU   A 1 58  ? -17.457 -23.451 -21.219 1.00 76.89  ? 576  GLU   A OE1  1 
ATOM   517  O  OE2  . GLU   A 1 58  ? -16.439 -25.332 -20.690 1.00 79.75  ? 576  GLU   A OE2  1 
ATOM   518  N  N    . PHE   A 1 59  ? -17.001 -21.127 -16.428 1.00 55.87  ? 577  PHE   A N    1 
ATOM   519  C  CA   . PHE   A 1 59  ? -17.401 -19.723 -16.418 1.00 49.49  ? 577  PHE   A CA   1 
ATOM   520  C  C    . PHE   A 1 59  ? -17.025 -19.015 -17.710 1.00 48.36  ? 577  PHE   A C    1 
ATOM   521  O  O    . PHE   A 1 59  ? -15.871 -19.055 -18.136 1.00 47.33  ? 577  PHE   A O    1 
ATOM   522  C  CB   . PHE   A 1 59  ? -16.768 -18.987 -15.237 1.00 54.45  ? 577  PHE   A CB   1 
ATOM   523  C  CG   . PHE   A 1 59  ? -17.525 -19.129 -13.947 1.00 43.65  ? 577  PHE   A CG   1 
ATOM   524  C  CD1  . PHE   A 1 59  ? -18.718 -18.457 -13.751 1.00 48.15  ? 577  PHE   A CD1  1 
ATOM   525  C  CD2  . PHE   A 1 59  ? -17.024 -19.906 -12.917 1.00 44.91  ? 577  PHE   A CD2  1 
ATOM   526  C  CE1  . PHE   A 1 59  ? -19.412 -18.573 -12.550 1.00 43.33  ? 577  PHE   A CE1  1 
ATOM   527  C  CE2  . PHE   A 1 59  ? -17.711 -20.028 -11.710 1.00 41.05  ? 577  PHE   A CE2  1 
ATOM   528  C  CZ   . PHE   A 1 59  ? -18.907 -19.369 -11.530 1.00 33.33  ? 577  PHE   A CZ   1 
ATOM   529  N  N    . ASP   A 1 60  ? -18.018 -18.379 -18.325 1.00 44.16  ? 578  ASP   A N    1 
ATOM   530  C  CA   . ASP   A 1 60  ? -17.811 -17.487 -19.468 1.00 52.36  ? 578  ASP   A CA   1 
ATOM   531  C  C    . ASP   A 1 60  ? -16.968 -18.100 -20.574 1.00 51.60  ? 578  ASP   A C    1 
ATOM   532  O  O    . ASP   A 1 60  ? -16.210 -17.398 -21.255 1.00 55.09  ? 578  ASP   A O    1 
ATOM   533  C  CB   . ASP   A 1 60  ? -17.192 -16.166 -18.986 1.00 49.06  ? 578  ASP   A CB   1 
ATOM   534  C  CG   . ASP   A 1 60  ? -18.129 -15.398 -18.045 1.00 55.26  ? 578  ASP   A CG   1 
ATOM   535  O  OD1  . ASP   A 1 60  ? -19.082 -14.784 -18.558 1.00 54.16  ? 578  ASP   A OD1  1 
ATOM   536  O  OD2  . ASP   A 1 60  ? -17.937 -15.422 -16.803 1.00 54.16  ? 578  ASP   A OD2  1 
ATOM   537  N  N    . GLY   A 1 61  ? -17.109 -19.412 -20.754 1.00 49.55  ? 579  GLY   A N    1 
ATOM   538  C  CA   . GLY   A 1 61  ? -16.446 -20.115 -21.844 1.00 52.95  ? 579  GLY   A CA   1 
ATOM   539  C  C    . GLY   A 1 61  ? -14.957 -20.298 -21.612 1.00 59.93  ? 579  GLY   A C    1 
ATOM   540  O  O    . GLY   A 1 61  ? -14.193 -20.556 -22.543 1.00 60.44  ? 579  GLY   A O    1 
ATOM   541  N  N    . GLU   A 1 62  ? -14.542 -20.166 -20.357 1.00 55.98  ? 580  GLU   A N    1 
ATOM   542  C  CA   . GLU   A 1 62  ? -13.140 -20.324 -20.008 1.00 62.46  ? 580  GLU   A CA   1 
ATOM   543  C  C    . GLU   A 1 62  ? -12.799 -21.804 -19.899 1.00 55.79  ? 580  GLU   A C    1 
ATOM   544  O  O    . GLU   A 1 62  ? -13.118 -22.467 -18.911 1.00 55.98  ? 580  GLU   A O    1 
ATOM   545  C  CB   . GLU   A 1 62  ? -12.825 -19.584 -18.700 1.00 66.10  ? 580  GLU   A CB   1 
ATOM   546  C  CG   . GLU   A 1 62  ? -12.812 -18.058 -18.845 1.00 64.09  ? 580  GLU   A CG   1 
ATOM   547  C  CD   . GLU   A 1 62  ? -13.097 -17.317 -17.541 1.00 58.72  ? 580  GLU   A CD   1 
ATOM   548  O  OE1  . GLU   A 1 62  ? -13.220 -17.964 -16.475 1.00 56.94  ? 580  GLU   A OE1  1 
ATOM   549  O  OE2  . GLU   A 1 62  ? -13.211 -16.074 -17.591 1.00 64.22  ? 580  GLU   A OE2  1 
ATOM   550  N  N    . LYS   A 1 63  ? -12.167 -22.321 -20.939 1.00 62.18  ? 581  LYS   A N    1 
ATOM   551  C  CA   . LYS   A 1 63  ? -11.725 -23.705 -20.956 1.00 72.20  ? 581  LYS   A CA   1 
ATOM   552  C  C    . LYS   A 1 63  ? -10.341 -23.851 -20.329 1.00 77.81  ? 581  LYS   A C    1 
ATOM   553  O  O    . LYS   A 1 63  ? -9.569  -22.894 -20.275 1.00 82.79  ? 581  LYS   A O    1 
ATOM   554  C  CB   . LYS   A 1 63  ? -11.705 -24.250 -22.392 1.00 75.86  ? 581  LYS   A CB   1 
ATOM   555  C  CG   . LYS   A 1 63  ? -12.977 -24.975 -22.827 1.00 75.12  ? 581  LYS   A CG   1 
ATOM   556  C  CD   . LYS   A 1 63  ? -14.096 -24.033 -23.217 1.00 75.47  ? 581  LYS   A CD   1 
ATOM   557  C  CE   . LYS   A 1 63  ? -15.260 -24.800 -23.837 1.00 72.53  ? 581  LYS   A CE   1 
ATOM   558  N  NZ   . LYS   A 1 63  ? -15.818 -25.835 -22.911 1.00 63.70  ? 581  LYS   A NZ   1 
ATOM   559  N  N    . GLY   A 1 64  ? -10.037 -25.056 -19.858 1.00 81.02  ? 582  GLY   A N    1 
ATOM   560  C  CA   . GLY   A 1 64  ? -8.689  -25.393 -19.434 1.00 88.55  ? 582  GLY   A CA   1 
ATOM   561  C  C    . GLY   A 1 64  ? -8.396  -25.075 -17.982 1.00 87.08  ? 582  GLY   A C    1 
ATOM   562  O  O    . GLY   A 1 64  ? -7.239  -24.873 -17.606 1.00 92.35  ? 582  GLY   A O    1 
ATOM   563  N  N    . LEU   A 1 65  ? -9.444  -25.029 -17.165 1.00 74.21  ? 583  LEU   A N    1 
ATOM   564  C  CA   . LEU   A 1 65  ? -9.274  -24.763 -15.744 1.00 72.47  ? 583  LEU   A CA   1 
ATOM   565  C  C    . LEU   A 1 65  ? -9.628  -25.992 -14.917 1.00 76.13  ? 583  LEU   A C    1 
ATOM   566  O  O    . LEU   A 1 65  ? -10.486 -26.783 -15.303 1.00 80.43  ? 583  LEU   A O    1 
ATOM   567  C  CB   . LEU   A 1 65  ? -10.125 -23.562 -15.296 1.00 59.72  ? 583  LEU   A CB   1 
ATOM   568  C  CG   . LEU   A 1 65  ? -9.680  -22.154 -15.719 1.00 65.48  ? 583  LEU   A CG   1 
ATOM   569  C  CD1  . LEU   A 1 65  ? -8.149  -22.001 -15.616 1.00 63.05  ? 583  LEU   A CD1  1 
ATOM   570  C  CD2  . LEU   A 1 65  ? -10.174 -21.802 -17.113 1.00 71.36  ? 583  LEU   A CD2  1 
ATOM   571  N  N    . ASP   A 1 66  ? -8.951  -26.138 -13.781 1.00 81.96  ? 584  ASP   A N    1 
ATOM   572  C  CA   . ASP   A 1 66  ? -9.204  -27.220 -12.834 1.00 76.09  ? 584  ASP   A CA   1 
ATOM   573  C  C    . ASP   A 1 66  ? -10.636 -27.171 -12.325 1.00 81.49  ? 584  ASP   A C    1 
ATOM   574  O  O    . ASP   A 1 66  ? -11.010 -26.244 -11.601 1.00 85.51  ? 584  ASP   A O    1 
ATOM   575  C  CB   . ASP   A 1 66  ? -8.228  -27.128 -11.660 1.00 68.64  ? 584  ASP   A CB   1 
ATOM   576  C  CG   . ASP   A 1 66  ? -8.445  -28.209 -10.633 1.00 73.19  ? 584  ASP   A CG   1 
ATOM   577  O  OD1  . ASP   A 1 66  ? -7.995  -29.350 -10.879 1.00 83.86  ? 584  ASP   A OD1  1 
ATOM   578  O  OD2  . ASP   A 1 66  ? -9.049  -27.916 -9.574  1.00 69.67  ? 584  ASP   A OD2  1 
ATOM   579  N  N    . TYR   A 1 67  ? -11.434 -28.172 -12.689 1.00 76.97  ? 585  TYR   A N    1 
ATOM   580  C  CA   . TYR   A 1 67  ? -12.849 -28.177 -12.318 1.00 73.57  ? 585  TYR   A CA   1 
ATOM   581  C  C    . TYR   A 1 67  ? -13.070 -28.167 -10.806 1.00 74.40  ? 585  TYR   A C    1 
ATOM   582  O  O    . TYR   A 1 67  ? -14.115 -27.722 -10.332 1.00 70.98  ? 585  TYR   A O    1 
ATOM   583  C  CB   . TYR   A 1 67  ? -13.564 -29.376 -12.945 1.00 76.37  ? 585  TYR   A CB   1 
ATOM   584  C  CG   . TYR   A 1 67  ? -13.670 -29.291 -14.453 1.00 80.39  ? 585  TYR   A CG   1 
ATOM   585  C  CD1  . TYR   A 1 67  ? -14.739 -28.632 -15.058 1.00 72.51  ? 585  TYR   A CD1  1 
ATOM   586  C  CD2  . TYR   A 1 67  ? -12.704 -29.861 -15.273 1.00 87.43  ? 585  TYR   A CD2  1 
ATOM   587  C  CE1  . TYR   A 1 67  ? -14.845 -28.546 -16.437 1.00 75.54  ? 585  TYR   A CE1  1 
ATOM   588  C  CE2  . TYR   A 1 67  ? -12.799 -29.779 -16.658 1.00 93.22  ? 585  TYR   A CE2  1 
ATOM   589  C  CZ   . TYR   A 1 67  ? -13.874 -29.121 -17.233 1.00 86.75  ? 585  TYR   A CZ   1 
ATOM   590  O  OH   . TYR   A 1 67  ? -13.985 -29.036 -18.603 1.00 90.38  ? 585  TYR   A OH   1 
ATOM   591  N  N    . GLY   A 1 68  ? -12.084 -28.636 -10.048 1.00 80.50  ? 586  GLY   A N    1 
ATOM   592  C  CA   . GLY   A 1 68  ? -12.172 -28.612 -8.598  1.00 79.13  ? 586  GLY   A CA   1 
ATOM   593  C  C    . GLY   A 1 68  ? -12.122 -27.196 -8.050  1.00 73.47  ? 586  GLY   A C    1 
ATOM   594  O  O    . GLY   A 1 68  ? -12.871 -26.835 -7.138  1.00 67.53  ? 586  GLY   A O    1 
ATOM   595  N  N    . GLY   A 1 69  ? -11.234 -26.387 -8.616  1.00 70.81  ? 587  GLY   A N    1 
ATOM   596  C  CA   . GLY   A 1 69  ? -11.100 -25.008 -8.192  1.00 63.67  ? 587  GLY   A CA   1 
ATOM   597  C  C    . GLY   A 1 69  ? -12.282 -24.151 -8.599  1.00 53.58  ? 587  GLY   A C    1 
ATOM   598  O  O    . GLY   A 1 69  ? -12.739 -23.306 -7.830  1.00 51.53  ? 587  GLY   A O    1 
ATOM   599  N  N    . VAL   A 1 70  ? -12.769 -24.364 -9.818  1.00 51.94  ? 588  VAL   A N    1 
ATOM   600  C  CA   . VAL   A 1 70  ? -13.890 -23.600 -10.334 1.00 49.46  ? 588  VAL   A CA   1 
ATOM   601  C  C    . VAL   A 1 70  ? -15.127 -23.829 -9.464  1.00 46.52  ? 588  VAL   A C    1 
ATOM   602  O  O    . VAL   A 1 70  ? -15.854 -22.889 -9.155  1.00 43.89  ? 588  VAL   A O    1 
ATOM   603  C  CB   . VAL   A 1 70  ? -14.212 -23.970 -11.791 1.00 49.93  ? 588  VAL   A CB   1 
ATOM   604  C  CG1  . VAL   A 1 70  ? -15.407 -23.169 -12.299 1.00 44.96  ? 588  VAL   A CG1  1 
ATOM   605  C  CG2  . VAL   A 1 70  ? -13.017 -23.724 -12.667 1.00 54.50  ? 588  VAL   A CG2  1 
ATOM   606  N  N    . ALA   A 1 71  ? -15.349 -25.073 -9.048  1.00 38.79  ? 589  ALA   A N    1 
ATOM   607  C  CA   . ALA   A 1 71  ? -16.508 -25.382 -8.225  1.00 38.98  ? 589  ALA   A CA   1 
ATOM   608  C  C    . ALA   A 1 71  ? -16.475 -24.596 -6.929  1.00 42.56  ? 589  ALA   A C    1 
ATOM   609  O  O    . ALA   A 1 71  ? -17.491 -24.053 -6.494  1.00 44.78  ? 589  ALA   A O    1 
ATOM   610  C  CB   . ALA   A 1 71  ? -16.576 -26.873 -7.932  1.00 44.64  ? 589  ALA   A CB   1 
ATOM   611  N  N    . ARG   A 1 72  ? -15.295 -24.542 -6.321  1.00 49.53  ? 590  ARG   A N    1 
ATOM   612  C  CA   . ARG   A 1 72  ? -15.116 -23.861 -5.046  1.00 55.12  ? 590  ARG   A CA   1 
ATOM   613  C  C    . ARG   A 1 72  ? -15.420 -22.369 -5.217  1.00 50.71  ? 590  ARG   A C    1 
ATOM   614  O  O    . ARG   A 1 72  ? -16.039 -21.740 -4.358  1.00 46.10  ? 590  ARG   A O    1 
ATOM   615  C  CB   . ARG   A 1 72  ? -13.693 -24.089 -4.519  1.00 61.90  ? 590  ARG   A CB   1 
ATOM   616  C  CG   . ARG   A 1 72  ? -13.582 -24.030 -3.004  1.00 66.99  ? 590  ARG   A CG   1 
ATOM   617  C  CD   . ARG   A 1 72  ? -12.499 -24.959 -2.460  1.00 72.26  ? 590  ARG   A CD   1 
ATOM   618  N  NE   . ARG   A 1 72  ? -11.159 -24.502 -2.805  1.00 81.63  ? 590  ARG   A NE   1 
ATOM   619  C  CZ   . ARG   A 1 72  ? -10.037 -25.004 -2.290  1.00 88.81  ? 590  ARG   A CZ   1 
ATOM   620  N  NH1  . ARG   A 1 72  ? -10.094 -25.983 -1.391  1.00 92.20  ? 590  ARG   A NH1  1 
ATOM   621  N  NH2  . ARG   A 1 72  ? -8.855  -24.520 -2.664  1.00 87.16  ? 590  ARG   A NH2  1 
ATOM   622  N  N    . GLU   A 1 73  ? -14.997 -21.817 -6.346  1.00 44.83  ? 591  GLU   A N    1 
ATOM   623  C  CA   . GLU   A 1 73  ? -15.261 -20.419 -6.657  1.00 42.09  ? 591  GLU   A CA   1 
ATOM   624  C  C    . GLU   A 1 73  ? -16.758 -20.209 -6.831  1.00 50.26  ? 591  GLU   A C    1 
ATOM   625  O  O    . GLU   A 1 73  ? -17.311 -19.186 -6.405  1.00 46.68  ? 591  GLU   A O    1 
ATOM   626  C  CB   . GLU   A 1 73  ? -14.494 -20.003 -7.914  1.00 46.46  ? 591  GLU   A CB   1 
ATOM   627  C  CG   . GLU   A 1 73  ? -14.756 -18.580 -8.395  1.00 60.29  ? 591  GLU   A CG   1 
ATOM   628  C  CD   . GLU   A 1 73  ? -13.833 -18.175 -9.533  1.00 71.45  ? 591  GLU   A CD   1 
ATOM   629  O  OE1  . GLU   A 1 73  ? -12.688 -18.683 -9.575  1.00 76.37  ? 591  GLU   A OE1  1 
ATOM   630  O  OE2  . GLU   A 1 73  ? -14.255 -17.364 -10.390 1.00 78.08  ? 591  GLU   A OE2  1 
ATOM   631  N  N    . TRP   A 1 74  ? -17.419 -21.193 -7.438  1.00 40.00  ? 592  TRP   A N    1 
ATOM   632  C  CA   . TRP   A 1 74  ? -18.849 -21.089 -7.682  1.00 40.18  ? 592  TRP   A CA   1 
ATOM   633  C  C    . TRP   A 1 74  ? -19.629 -21.048 -6.373  1.00 44.52  ? 592  TRP   A C    1 
ATOM   634  O  O    . TRP   A 1 74  ? -20.551 -20.244 -6.215  1.00 39.35  ? 592  TRP   A O    1 
ATOM   635  C  CB   . TRP   A 1 74  ? -19.349 -22.247 -8.552  1.00 38.80  ? 592  TRP   A CB   1 
ATOM   636  C  CG   . TRP   A 1 74  ? -20.842 -22.250 -8.696  1.00 35.97  ? 592  TRP   A CG   1 
ATOM   637  C  CD1  . TRP   A 1 74  ? -21.606 -21.383 -9.434  1.00 32.12  ? 592  TRP   A CD1  1 
ATOM   638  C  CD2  . TRP   A 1 74  ? -21.758 -23.152 -8.064  1.00 38.05  ? 592  TRP   A CD2  1 
ATOM   639  N  NE1  . TRP   A 1 74  ? -22.945 -21.698 -9.300  1.00 30.99  ? 592  TRP   A NE1  1 
ATOM   640  C  CE2  . TRP   A 1 74  ? -23.058 -22.769 -8.459  1.00 32.44  ? 592  TRP   A CE2  1 
ATOM   641  C  CE3  . TRP   A 1 74  ? -21.600 -24.240 -7.203  1.00 40.39  ? 592  TRP   A CE3  1 
ATOM   642  C  CZ2  . TRP   A 1 74  ? -24.188 -23.459 -8.033  1.00 34.46  ? 592  TRP   A CZ2  1 
ATOM   643  C  CZ3  . TRP   A 1 74  ? -22.725 -24.913 -6.780  1.00 39.52  ? 592  TRP   A CZ3  1 
ATOM   644  C  CH2  . TRP   A 1 74  ? -24.003 -24.524 -7.197  1.00 27.94  ? 592  TRP   A CH2  1 
ATOM   645  N  N    . PHE   A 1 75  ? -19.267 -21.921 -5.438  1.00 35.55  ? 593  PHE   A N    1 
ATOM   646  C  CA   . PHE   A 1 75  ? -19.964 -21.963 -4.162  1.00 38.94  ? 593  PHE   A CA   1 
ATOM   647  C  C    . PHE   A 1 75  ? -19.828 -20.636 -3.441  1.00 42.57  ? 593  PHE   A C    1 
ATOM   648  O  O    . PHE   A 1 75  ? -20.741 -20.187 -2.753  1.00 48.44  ? 593  PHE   A O    1 
ATOM   649  C  CB   . PHE   A 1 75  ? -19.434 -23.094 -3.290  1.00 37.86  ? 593  PHE   A CB   1 
ATOM   650  C  CG   . PHE   A 1 75  ? -20.048 -24.431 -3.601  1.00 38.87  ? 593  PHE   A CG   1 
ATOM   651  C  CD1  . PHE   A 1 75  ? -21.377 -24.682 -3.295  1.00 29.03  ? 593  PHE   A CD1  1 
ATOM   652  C  CD2  . PHE   A 1 75  ? -19.307 -25.423 -4.206  1.00 41.20  ? 593  PHE   A CD2  1 
ATOM   653  C  CE1  . PHE   A 1 75  ? -21.938 -25.908 -3.561  1.00 34.25  ? 593  PHE   A CE1  1 
ATOM   654  C  CE2  . PHE   A 1 75  ? -19.880 -26.655 -4.490  1.00 37.29  ? 593  PHE   A CE2  1 
ATOM   655  C  CZ   . PHE   A 1 75  ? -21.183 -26.891 -4.170  1.00 28.86  ? 593  PHE   A CZ   1 
ATOM   656  N  N    . PHE   A 1 76  ? -18.679 -20.014 -3.607  1.00 33.48  ? 594  PHE   A N    1 
ATOM   657  C  CA   . PHE   A 1 76  ? -18.454 -18.699 -3.052  1.00 38.07  ? 594  PHE   A CA   1 
ATOM   658  C  C    . PHE   A 1 76  ? -19.328 -17.650 -3.736  1.00 44.67  ? 594  PHE   A C    1 
ATOM   659  O  O    . PHE   A 1 76  ? -20.015 -16.872 -3.062  1.00 37.93  ? 594  PHE   A O    1 
ATOM   660  C  CB   . PHE   A 1 76  ? -16.987 -18.316 -3.181  1.00 42.58  ? 594  PHE   A CB   1 
ATOM   661  C  CG   . PHE   A 1 76  ? -16.667 -16.981 -2.596  1.00 55.13  ? 594  PHE   A CG   1 
ATOM   662  C  CD1  . PHE   A 1 76  ? -16.489 -16.841 -1.231  1.00 54.05  ? 594  PHE   A CD1  1 
ATOM   663  C  CD2  . PHE   A 1 76  ? -16.542 -15.867 -3.407  1.00 53.58  ? 594  PHE   A CD2  1 
ATOM   664  C  CE1  . PHE   A 1 76  ? -16.194 -15.619 -0.684  1.00 52.76  ? 594  PHE   A CE1  1 
ATOM   665  C  CE2  . PHE   A 1 76  ? -16.238 -14.636 -2.864  1.00 56.60  ? 594  PHE   A CE2  1 
ATOM   666  C  CZ   . PHE   A 1 76  ? -16.067 -14.512 -1.501  1.00 54.60  ? 594  PHE   A CZ   1 
ATOM   667  N  N    . LEU   A 1 77  ? -19.296 -17.622 -5.067  1.00 34.98  ? 595  LEU   A N    1 
ATOM   668  C  CA   . LEU   A 1 77  ? -20.058 -16.622 -5.809  1.00 39.96  ? 595  LEU   A CA   1 
ATOM   669  C  C    . LEU   A 1 77  ? -21.571 -16.814 -5.641  1.00 33.81  ? 595  LEU   A C    1 
ATOM   670  O  O    . LEU   A 1 77  ? -22.320 -15.842 -5.506  1.00 42.26  ? 595  LEU   A O    1 
ATOM   671  C  CB   . LEU   A 1 77  ? -19.694 -16.643 -7.299  1.00 41.42  ? 595  LEU   A CB   1 
ATOM   672  C  CG   . LEU   A 1 77  ? -18.307 -16.190 -7.745  1.00 43.62  ? 595  LEU   A CG   1 
ATOM   673  C  CD1  . LEU   A 1 77  ? -18.167 -16.323 -9.262  1.00 44.52  ? 595  LEU   A CD1  1 
ATOM   674  C  CD2  . LEU   A 1 77  ? -18.018 -14.752 -7.301  1.00 46.77  ? 595  LEU   A CD2  1 
ATOM   675  N  N    . ILE   A 1 78  ? -22.028 -18.057 -5.630  1.00 31.15  ? 596  ILE   A N    1 
ATOM   676  C  CA   . ILE   A 1 78  ? -23.461 -18.291 -5.562  1.00 26.47  ? 596  ILE   A CA   1 
ATOM   677  C  C    . ILE   A 1 78  ? -23.956 -17.963 -4.137  1.00 31.82  ? 596  ILE   A C    1 
ATOM   678  O  O    . ILE   A 1 78  ? -25.086 -17.521 -3.957  1.00 41.25  ? 596  ILE   A O    1 
ATOM   679  C  CB   . ILE   A 1 78  ? -23.830 -19.773 -5.980  1.00 31.71  ? 596  ILE   A CB   1 
ATOM   680  C  CG1  . ILE   A 1 78  ? -25.308 -19.912 -6.395  1.00 31.07  ? 596  ILE   A CG1  1 
ATOM   681  C  CG2  . ILE   A 1 78  ? -23.551 -20.737 -4.859  1.00 31.34  ? 596  ILE   A CG2  1 
ATOM   682  C  CD1  . ILE   A 1 78  ? -25.791 -18.936 -7.496  1.00 29.38  ? 596  ILE   A CD1  1 
ATOM   683  N  N    . SER   A 1 79  ? -23.110 -18.178 -3.131  1.00 32.64  ? 597  SER   A N    1 
ATOM   684  C  CA   . SER   A 1 79  ? -23.433 -17.813 -1.744  1.00 33.59  ? 597  SER   A CA   1 
ATOM   685  C  C    . SER   A 1 79  ? -23.657 -16.303 -1.600  1.00 34.79  ? 597  SER   A C    1 
ATOM   686  O  O    . SER   A 1 79  ? -24.623 -15.864 -0.989  1.00 39.40  ? 597  SER   A O    1 
ATOM   687  C  CB   . SER   A 1 79  ? -22.308 -18.257 -0.795  1.00 31.85  ? 597  SER   A CB   1 
ATOM   688  O  OG   . SER   A 1 79  ? -22.350 -19.667 -0.588  1.00 36.58  ? 597  SER   A OG   1 
ATOM   689  N  N    . LYS   A 1 80  ? -22.751 -15.526 -2.185  1.00 34.29  ? 598  LYS   A N    1 
ATOM   690  C  CA   . LYS   A 1 80  ? -22.801 -14.071 -2.130  1.00 36.99  ? 598  LYS   A CA   1 
ATOM   691  C  C    . LYS   A 1 80  ? -24.108 -13.539 -2.689  1.00 38.82  ? 598  LYS   A C    1 
ATOM   692  O  O    . LYS   A 1 80  ? -24.706 -12.617 -2.134  1.00 39.26  ? 598  LYS   A O    1 
ATOM   693  C  CB   . LYS   A 1 80  ? -21.636 -13.476 -2.905  1.00 40.18  ? 598  LYS   A CB   1 
ATOM   694  C  CG   . LYS   A 1 80  ? -20.519 -12.999 -2.025  1.00 61.32  ? 598  LYS   A CG   1 
ATOM   695  C  CD   . LYS   A 1 80  ? -20.105 -14.073 -1.030  1.00 64.82  ? 598  LYS   A CD   1 
ATOM   696  C  CE   . LYS   A 1 80  ? -19.074 -13.520 -0.051  1.00 68.30  ? 598  LYS   A CE   1 
ATOM   697  N  NZ   . LYS   A 1 80  ? -19.633 -12.446 0.817   1.00 73.81  ? 598  LYS   A NZ   1 
ATOM   698  N  N    . GLU   A 1 81  ? -24.520 -14.114 -3.813  1.00 36.21  ? 599  GLU   A N    1 
ATOM   699  C  CA   . GLU   A 1 81  ? -25.774 -13.763 -4.466  1.00 36.05  ? 599  GLU   A CA   1 
ATOM   700  C  C    . GLU   A 1 81  ? -27.006 -14.244 -3.665  1.00 32.56  ? 599  GLU   A C    1 
ATOM   701  O  O    . GLU   A 1 81  ? -27.857 -13.445 -3.316  1.00 37.69  ? 599  GLU   A O    1 
ATOM   702  C  CB   . GLU   A 1 81  ? -25.794 -14.349 -5.884  1.00 31.98  ? 599  GLU   A CB   1 
ATOM   703  C  CG   . GLU   A 1 81  ? -25.040 -13.518 -6.907  1.00 31.66  ? 599  GLU   A CG   1 
ATOM   704  C  CD   . GLU   A 1 81  ? -25.702 -12.166 -7.125  1.00 45.52  ? 599  GLU   A CD   1 
ATOM   705  O  OE1  . GLU   A 1 81  ? -26.634 -12.090 -7.952  1.00 47.55  ? 599  GLU   A OE1  1 
ATOM   706  O  OE2  . GLU   A 1 81  ? -25.319 -11.181 -6.456  1.00 42.26  ? 599  GLU   A OE2  1 
ATOM   707  N  N    . MET   A 1 82  ? -27.092 -15.546 -3.399  1.00 27.09  ? 600  MET   A N    1 
ATOM   708  C  CA   . MET   A 1 82  ? -28.235 -16.148 -2.701  1.00 35.02  ? 600  MET   A CA   1 
ATOM   709  C  C    . MET   A 1 82  ? -28.566 -15.496 -1.367  1.00 31.98  ? 600  MET   A C    1 
ATOM   710  O  O    . MET   A 1 82  ? -29.728 -15.354 -0.989  1.00 35.87  ? 600  MET   A O    1 
ATOM   711  C  CB   . MET   A 1 82  ? -27.976 -17.621 -2.411  1.00 35.42  ? 600  MET   A CB   1 
ATOM   712  C  CG   . MET   A 1 82  ? -28.055 -18.545 -3.557  1.00 40.19  ? 600  MET   A CG   1 
ATOM   713  S  SD   . MET   A 1 82  ? -27.566 -20.144 -2.913  1.00 39.41  ? 600  MET   A SD   1 
ATOM   714  C  CE   . MET   A 1 82  ? -28.538 -21.120 -3.952  1.00 51.61  ? 600  MET   A CE   1 
ATOM   715  N  N    . PHE   A 1 83  ? -27.521 -15.158 -0.629  1.00 30.82  ? 601  PHE   A N    1 
ATOM   716  C  CA   . PHE   A 1 83  ? -27.699 -14.662 0.720   1.00 39.49  ? 601  PHE   A CA   1 
ATOM   717  C  C    . PHE   A 1 83  ? -27.688 -13.138 0.782   1.00 37.52  ? 601  PHE   A C    1 
ATOM   718  O  O    . PHE   A 1 83  ? -27.709 -12.562 1.862   1.00 42.45  ? 601  PHE   A O    1 
ATOM   719  C  CB   . PHE   A 1 83  ? -26.618 -15.275 1.606   1.00 37.50  ? 601  PHE   A CB   1 
ATOM   720  C  CG   . PHE   A 1 83  ? -26.699 -16.776 1.660   1.00 33.79  ? 601  PHE   A CG   1 
ATOM   721  C  CD1  . PHE   A 1 83  ? -25.560 -17.560 1.566   1.00 31.84  ? 601  PHE   A CD1  1 
ATOM   722  C  CD2  . PHE   A 1 83  ? -27.935 -17.400 1.775   1.00 33.12  ? 601  PHE   A CD2  1 
ATOM   723  C  CE1  . PHE   A 1 83  ? -25.656 -18.946 1.596   1.00 38.13  ? 601  PHE   A CE1  1 
ATOM   724  C  CE2  . PHE   A 1 83  ? -28.036 -18.775 1.810   1.00 33.30  ? 601  PHE   A CE2  1 
ATOM   725  C  CZ   . PHE   A 1 83  ? -26.879 -19.552 1.714   1.00 30.83  ? 601  PHE   A CZ   1 
ATOM   726  N  N    . ASN   A 1 84  ? -27.649 -12.492 -0.382  1.00 31.79  ? 602  ASN   A N    1 
ATOM   727  C  CA   . ASN   A 1 84  ? -27.648 -11.027 -0.438  1.00 25.74  ? 602  ASN   A CA   1 
ATOM   728  C  C    . ASN   A 1 84  ? -29.019 -10.512 -0.037  1.00 30.61  ? 602  ASN   A C    1 
ATOM   729  O  O    . ASN   A 1 84  ? -29.996 -10.798 -0.726  1.00 34.95  ? 602  ASN   A O    1 
ATOM   730  C  CB   . ASN   A 1 84  ? -27.296 -10.537 -1.848  1.00 29.61  ? 602  ASN   A CB   1 
ATOM   731  C  CG   . ASN   A 1 84  ? -27.039 -9.033  -1.906  1.00 43.09  ? 602  ASN   A CG   1 
ATOM   732  O  OD1  . ASN   A 1 84  ? -27.584 -8.261  -1.113  1.00 39.55  ? 602  ASN   A OD1  1 
ATOM   733  N  ND2  . ASN   A 1 84  ? -26.213 -8.612  -2.860  1.00 44.70  ? 602  ASN   A ND2  1 
ATOM   734  N  N    . PRO   A 1 85  ? -29.110 -9.766  1.079   1.00 35.43  ? 603  PRO   A N    1 
ATOM   735  C  CA   . PRO   A 1 85  ? -30.424 -9.279  1.540   1.00 29.99  ? 603  PRO   A CA   1 
ATOM   736  C  C    . PRO   A 1 85  ? -31.131 -8.399  0.506   1.00 33.50  ? 603  PRO   A C    1 
ATOM   737  O  O    . PRO   A 1 85  ? -32.336 -8.203  0.602   1.00 36.19  ? 603  PRO   A O    1 
ATOM   738  C  CB   . PRO   A 1 85  ? -30.089 -8.475  2.795   1.00 31.40  ? 603  PRO   A CB   1 
ATOM   739  C  CG   . PRO   A 1 85  ? -28.743 -8.973  3.214   1.00 43.05  ? 603  PRO   A CG   1 
ATOM   740  C  CD   . PRO   A 1 85  ? -28.021 -9.330  1.962   1.00 37.64  ? 603  PRO   A CD   1 
ATOM   741  N  N    . TYR   A 1 86  ? -30.394 -7.896  -0.479  1.00 35.88  ? 604  TYR   A N    1 
ATOM   742  C  CA   . TYR   A 1 86  ? -30.990 -7.092  -1.549  1.00 35.53  ? 604  TYR   A CA   1 
ATOM   743  C  C    . TYR   A 1 86  ? -32.085 -7.861  -2.296  1.00 32.53  ? 604  TYR   A C    1 
ATOM   744  O  O    . TYR   A 1 86  ? -33.043 -7.269  -2.789  1.00 34.23  ? 604  TYR   A O    1 
ATOM   745  C  CB   . TYR   A 1 86  ? -29.906 -6.626  -2.529  1.00 44.24  ? 604  TYR   A CB   1 
ATOM   746  C  CG   . TYR   A 1 86  ? -30.404 -6.152  -3.890  1.00 48.24  ? 604  TYR   A CG   1 
ATOM   747  C  CD1  . TYR   A 1 86  ? -30.971 -4.889  -4.050  1.00 47.06  ? 604  TYR   A CD1  1 
ATOM   748  C  CD2  . TYR   A 1 86  ? -30.271 -6.955  -5.022  1.00 47.62  ? 604  TYR   A CD2  1 
ATOM   749  C  CE1  . TYR   A 1 86  ? -31.413 -4.443  -5.307  1.00 49.22  ? 604  TYR   A CE1  1 
ATOM   750  C  CE2  . TYR   A 1 86  ? -30.710 -6.522  -6.289  1.00 48.31  ? 604  TYR   A CE2  1 
ATOM   751  C  CZ   . TYR   A 1 86  ? -31.278 -5.267  -6.422  1.00 55.46  ? 604  TYR   A CZ   1 
ATOM   752  O  OH   . TYR   A 1 86  ? -31.708 -4.828  -7.668  1.00 50.16  ? 604  TYR   A OH   1 
ATOM   753  N  N    . TYR   A 1 87  ? -31.960 -9.180  -2.377  1.00 30.32  ? 605  TYR   A N    1 
ATOM   754  C  CA   . TYR   A 1 87  ? -32.950 -9.953  -3.122  1.00 31.43  ? 605  TYR   A CA   1 
ATOM   755  C  C    . TYR   A 1 87  ? -34.187 -10.233 -2.258  1.00 34.34  ? 605  TYR   A C    1 
ATOM   756  O  O    . TYR   A 1 87  ? -35.248 -10.554 -2.765  1.00 43.03  ? 605  TYR   A O    1 
ATOM   757  C  CB   . TYR   A 1 87  ? -32.330 -11.248 -3.648  1.00 35.47  ? 605  TYR   A CB   1 
ATOM   758  C  CG   . TYR   A 1 87  ? -31.333 -11.014 -4.763  1.00 40.17  ? 605  TYR   A CG   1 
ATOM   759  C  CD1  . TYR   A 1 87  ? -30.023 -11.465 -4.656  1.00 44.34  ? 605  TYR   A CD1  1 
ATOM   760  C  CD2  . TYR   A 1 87  ? -31.700 -10.331 -5.919  1.00 34.51  ? 605  TYR   A CD2  1 
ATOM   761  C  CE1  . TYR   A 1 87  ? -29.095 -11.246 -5.671  1.00 42.80  ? 605  TYR   A CE1  1 
ATOM   762  C  CE2  . TYR   A 1 87  ? -30.779 -10.103 -6.937  1.00 42.06  ? 605  TYR   A CE2  1 
ATOM   763  C  CZ   . TYR   A 1 87  ? -29.479 -10.565 -6.802  1.00 44.74  ? 605  TYR   A CZ   1 
ATOM   764  O  OH   . TYR   A 1 87  ? -28.563 -10.348 -7.795  1.00 52.33  ? 605  TYR   A OH   1 
ATOM   765  N  N    . GLY   A 1 88  ? -34.050 -10.078 -0.950  1.00 35.70  ? 606  GLY   A N    1 
ATOM   766  C  CA   . GLY   A 1 88  ? -35.198 -10.143 -0.070  1.00 35.12  ? 606  GLY   A CA   1 
ATOM   767  C  C    . GLY   A 1 88  ? -35.575 -11.524 0.444   1.00 38.26  ? 606  GLY   A C    1 
ATOM   768  O  O    . GLY   A 1 88  ? -36.593 -11.633 1.125   1.00 32.20  ? 606  GLY   A O    1 
ATOM   769  N  N    . LEU   A 1 89  ? -34.774 -12.558 0.138   1.00 29.67  ? 607  LEU   A N    1 
ATOM   770  C  CA   . LEU   A 1 89  ? -35.003 -13.915 0.676   1.00 27.75  ? 607  LEU   A CA   1 
ATOM   771  C  C    . LEU   A 1 89  ? -34.484 -14.069 2.112   1.00 27.56  ? 607  LEU   A C    1 
ATOM   772  O  O    . LEU   A 1 89  ? -35.201 -14.531 2.986   1.00 32.35  ? 607  LEU   A O    1 
ATOM   773  C  CB   . LEU   A 1 89  ? -34.342 -14.950 -0.223  1.00 26.17  ? 607  LEU   A CB   1 
ATOM   774  C  CG   . LEU   A 1 89  ? -34.814 -14.783 -1.672  1.00 32.02  ? 607  LEU   A CG   1 
ATOM   775  C  CD1  . LEU   A 1 89  ? -34.136 -15.793 -2.536  1.00 42.82  ? 607  LEU   A CD1  1 
ATOM   776  C  CD2  . LEU   A 1 89  ? -36.326 -14.952 -1.755  1.00 35.03  ? 607  LEU   A CD2  1 
ATOM   777  N  N    . PHE   A 1 90  ? -33.227 -13.693 2.330   1.00 30.61  ? 608  PHE   A N    1 
ATOM   778  C  CA   . PHE   A 1 90  ? -32.632 -13.629 3.665   1.00 30.42  ? 608  PHE   A CA   1 
ATOM   779  C  C    . PHE   A 1 90  ? -32.419 -12.181 4.068   1.00 36.37  ? 608  PHE   A C    1 
ATOM   780  O  O    . PHE   A 1 90  ? -32.385 -11.286 3.218   1.00 37.55  ? 608  PHE   A O    1 
ATOM   781  C  CB   . PHE   A 1 90  ? -31.298 -14.396 3.709   1.00 30.04  ? 608  PHE   A CB   1 
ATOM   782  C  CG   . PHE   A 1 90  ? -31.466 -15.893 3.623   1.00 28.00  ? 608  PHE   A CG   1 
ATOM   783  C  CD1  . PHE   A 1 90  ? -31.569 -16.520 2.402   1.00 28.37  ? 608  PHE   A CD1  1 
ATOM   784  C  CD2  . PHE   A 1 90  ? -31.553 -16.664 4.778   1.00 30.84  ? 608  PHE   A CD2  1 
ATOM   785  C  CE1  . PHE   A 1 90  ? -31.744 -17.905 2.325   1.00 24.91  ? 608  PHE   A CE1  1 
ATOM   786  C  CE2  . PHE   A 1 90  ? -31.728 -18.040 4.709   1.00 34.54  ? 608  PHE   A CE2  1 
ATOM   787  C  CZ   . PHE   A 1 90  ? -31.833 -18.657 3.472   1.00 29.38  ? 608  PHE   A CZ   1 
ATOM   788  N  N    . GLU   A 1 91  ? -32.282 -11.958 5.370   1.00 32.54  ? 609  GLU   A N    1 
ATOM   789  C  CA   . GLU   A 1 91  ? -31.989 -10.644 5.915   1.00 34.06  ? 609  GLU   A CA   1 
ATOM   790  C  C    . GLU   A 1 91  ? -31.155 -10.839 7.171   1.00 34.92  ? 609  GLU   A C    1 
ATOM   791  O  O    . GLU   A 1 91  ? -31.178 -11.919 7.772   1.00 31.32  ? 609  GLU   A O    1 
ATOM   792  C  CB   . GLU   A 1 91  ? -33.276 -9.879  6.236   1.00 36.22  ? 609  GLU   A CB   1 
ATOM   793  C  CG   . GLU   A 1 91  ? -33.996 -10.400 7.490   1.00 39.73  ? 609  GLU   A CG   1 
ATOM   794  C  CD   . GLU   A 1 91  ? -35.390 -9.816  7.675   1.00 44.67  ? 609  GLU   A CD   1 
ATOM   795  O  OE1  . GLU   A 1 91  ? -35.812 -8.977  6.857   1.00 48.39  ? 609  GLU   A OE1  1 
ATOM   796  O  OE2  . GLU   A 1 91  ? -36.063 -10.185 8.660   1.00 54.64  ? 609  GLU   A OE2  1 
ATOM   797  N  N    . TYR   A 1 92  ? -30.412 -9.806  7.554   1.00 33.01  ? 610  TYR   A N    1 
ATOM   798  C  CA   . TYR   A 1 92  ? -29.689 -9.822  8.815   1.00 35.10  ? 610  TYR   A CA   1 
ATOM   799  C  C    . TYR   A 1 92  ? -30.653 -9.912  9.977   1.00 33.64  ? 610  TYR   A C    1 
ATOM   800  O  O    . TYR   A 1 92  ? -31.700 -9.275  9.963   1.00 37.14  ? 610  TYR   A O    1 
ATOM   801  C  CB   . TYR   A 1 92  ? -28.828 -8.572  8.963   1.00 37.72  ? 610  TYR   A CB   1 
ATOM   802  C  CG   . TYR   A 1 92  ? -27.763 -8.485  7.925   1.00 37.20  ? 610  TYR   A CG   1 
ATOM   803  C  CD1  . TYR   A 1 92  ? -26.733 -9.421  7.882   1.00 36.67  ? 610  TYR   A CD1  1 
ATOM   804  C  CD2  . TYR   A 1 92  ? -27.791 -7.476  6.972   1.00 40.24  ? 610  TYR   A CD2  1 
ATOM   805  C  CE1  . TYR   A 1 92  ? -25.755 -9.346  6.916   1.00 43.08  ? 610  TYR   A CE1  1 
ATOM   806  C  CE2  . TYR   A 1 92  ? -26.817 -7.389  6.010   1.00 46.56  ? 610  TYR   A CE2  1 
ATOM   807  C  CZ   . TYR   A 1 92  ? -25.805 -8.318  5.984   1.00 46.36  ? 610  TYR   A CZ   1 
ATOM   808  O  OH   . TYR   A 1 92  ? -24.846 -8.204  5.016   1.00 51.61  ? 610  TYR   A OH   1 
ATOM   809  N  N    . SER   A 1 93  ? -30.274 -10.673 10.996  1.00 36.67  ? 611  SER   A N    1 
ATOM   810  C  CA   . SER   A 1 93  ? -31.158 -10.945 12.125  1.00 37.76  ? 611  SER   A CA   1 
ATOM   811  C  C    . SER   A 1 93  ? -31.380 -9.732  13.027  1.00 41.80  ? 611  SER   A C    1 
ATOM   812  O  O    . SER   A 1 93  ? -32.347 -9.681  13.788  1.00 52.72  ? 611  SER   A O    1 
ATOM   813  C  CB   . SER   A 1 93  ? -30.612 -12.108 12.946  1.00 35.50  ? 611  SER   A CB   1 
ATOM   814  O  OG   . SER   A 1 93  ? -29.309 -11.828 13.423  1.00 34.31  ? 611  SER   A OG   1 
ATOM   815  N  N    . ALA   A 1 94  ? -30.477 -8.764  12.945  1.00 39.11  ? 612  ALA   A N    1 
ATOM   816  C  CA   . ALA   A 1 94  ? -30.602 -7.519  13.674  1.00 36.64  ? 612  ALA   A CA   1 
ATOM   817  C  C    . ALA   A 1 94  ? -29.628 -6.538  13.076  1.00 52.24  ? 612  ALA   A C    1 
ATOM   818  O  O    . ALA   A 1 94  ? -28.648 -6.926  12.429  1.00 43.10  ? 612  ALA   A O    1 
ATOM   819  C  CB   . ALA   A 1 94  ? -30.322 -7.685  15.188  1.00 37.93  ? 612  ALA   A CB   1 
ATOM   820  N  N    . THR   A 1 95  ? -29.886 -5.265  13.336  1.00 51.30  ? 613  THR   A N    1 
ATOM   821  C  CA   . THR   A 1 95  ? -29.064 -4.193  12.805  1.00 53.80  ? 613  THR   A CA   1 
ATOM   822  C  C    . THR   A 1 95  ? -27.601 -4.403  13.221  1.00 52.06  ? 613  THR   A C    1 
ATOM   823  O  O    . THR   A 1 95  ? -26.693 -4.178  12.429  1.00 47.67  ? 613  THR   A O    1 
ATOM   824  C  CB   . THR   A 1 95  ? -29.596 -2.838  13.266  1.00 54.62  ? 613  THR   A CB   1 
ATOM   825  O  OG1  . THR   A 1 95  ? -28.704 -1.799  12.848  1.00 71.79  ? 613  THR   A OG1  1 
ATOM   826  C  CG2  . THR   A 1 95  ? -29.730 -2.812  14.778  1.00 64.11  ? 613  THR   A CG2  1 
ATOM   827  N  N    . ASP   A 1 96  ? -27.387 -4.922  14.429  1.00 49.08  ? 614  ASP   A N    1 
ATOM   828  C  CA   . ASP   A 1 96  ? -26.042 -5.075  14.979  1.00 45.57  ? 614  ASP   A CA   1 
ATOM   829  C  C    . ASP   A 1 96  ? -25.458 -6.469  14.802  1.00 40.66  ? 614  ASP   A C    1 
ATOM   830  O  O    . ASP   A 1 96  ? -24.392 -6.742  15.325  1.00 42.66  ? 614  ASP   A O    1 
ATOM   831  C  CB   . ASP   A 1 96  ? -26.045 -4.712  16.465  1.00 48.54  ? 614  ASP   A CB   1 
ATOM   832  C  CG   . ASP   A 1 96  ? -26.474 -3.283  16.706  1.00 69.53  ? 614  ASP   A CG   1 
ATOM   833  O  OD1  . ASP   A 1 96  ? -25.983 -2.383  15.985  1.00 74.05  ? 614  ASP   A OD1  1 
ATOM   834  O  OD2  . ASP   A 1 96  ? -27.309 -3.054  17.611  1.00 79.27  ? 614  ASP   A OD2  1 
ATOM   835  N  N    . ASN   A 1 97  ? -26.159 -7.344  14.082  1.00 38.07  ? 615  ASN   A N    1 
ATOM   836  C  CA   . ASN   A 1 97  ? -25.674 -8.706  13.820  1.00 43.86  ? 615  ASN   A CA   1 
ATOM   837  C  C    . ASN   A 1 97  ? -25.272 -8.913  12.373  1.00 46.44  ? 615  ASN   A C    1 
ATOM   838  O  O    . ASN   A 1 97  ? -25.764 -8.227  11.498  1.00 35.61  ? 615  ASN   A O    1 
ATOM   839  C  CB   . ASN   A 1 97  ? -26.734 -9.773  14.146  1.00 42.64  ? 615  ASN   A CB   1 
ATOM   840  C  CG   . ASN   A 1 97  ? -27.171 -9.761  15.592  1.00 49.41  ? 615  ASN   A CG   1 
ATOM   841  O  OD1  . ASN   A 1 97  ? -26.566 -9.106  16.439  1.00 46.17  ? 615  ASN   A OD1  1 
ATOM   842  N  ND2  . ASN   A 1 97  ? -28.234 -10.513 15.884  1.00 53.94  ? 615  ASN   A ND2  1 
ATOM   843  N  N    . TYR   A 1 98  ? -24.437 -9.919  12.130  1.00 47.93  ? 616  TYR   A N    1 
ATOM   844  C  CA   . TYR   A 1 98  ? -24.053 -10.305 10.779  1.00 47.27  ? 616  TYR   A CA   1 
ATOM   845  C  C    . TYR   A 1 98  ? -24.713 -11.631 10.397  1.00 40.85  ? 616  TYR   A C    1 
ATOM   846  O  O    . TYR   A 1 98  ? -24.648 -12.064 9.247   1.00 42.07  ? 616  TYR   A O    1 
ATOM   847  C  CB   . TYR   A 1 98  ? -22.534 -10.418 10.669  1.00 60.30  ? 616  TYR   A CB   1 
ATOM   848  C  CG   . TYR   A 1 98  ? -21.934 -11.258 11.785  1.00 78.26  ? 616  TYR   A CG   1 
ATOM   849  C  CD1  . TYR   A 1 98  ? -21.835 -12.645 11.665  1.00 77.73  ? 616  TYR   A CD1  1 
ATOM   850  C  CD2  . TYR   A 1 98  ? -21.482 -10.669 12.966  1.00 78.39  ? 616  TYR   A CD2  1 
ATOM   851  C  CE1  . TYR   A 1 98  ? -21.300 -13.421 12.688  1.00 81.95  ? 616  TYR   A CE1  1 
ATOM   852  C  CE2  . TYR   A 1 98  ? -20.944 -11.437 13.991  1.00 79.93  ? 616  TYR   A CE2  1 
ATOM   853  C  CZ   . TYR   A 1 98  ? -20.854 -12.809 13.845  1.00 83.55  ? 616  TYR   A CZ   1 
ATOM   854  O  OH   . TYR   A 1 98  ? -20.319 -13.569 14.863  1.00 94.21  ? 616  TYR   A OH   1 
ATOM   855  N  N    . THR   A 1 99  ? -25.342 -12.288 11.370  1.00 36.16  ? 617  THR   A N    1 
ATOM   856  C  CA   . THR   A 1 99  ? -26.056 -13.532 11.098  1.00 33.25  ? 617  THR   A CA   1 
ATOM   857  C  C    . THR   A 1 99  ? -27.321 -13.267 10.281  1.00 30.44  ? 617  THR   A C    1 
ATOM   858  O  O    . THR   A 1 99  ? -27.964 -12.220 10.429  1.00 31.62  ? 617  THR   A O    1 
ATOM   859  C  CB   . THR   A 1 99  ? -26.435 -14.284 12.403  1.00 37.44  ? 617  THR   A CB   1 
ATOM   860  O  OG1  . THR   A 1 99  ? -26.994 -13.359 13.352  1.00 36.32  ? 617  THR   A OG1  1 
ATOM   861  C  CG2  . THR   A 1 99  ? -25.209 -14.953 13.024  1.00 42.73  ? 617  THR   A CG2  1 
ATOM   862  N  N    . LEU   A 1 100 ? -27.663 -14.232 9.427   1.00 26.08  ? 618  LEU   A N    1 
ATOM   863  C  CA   . LEU   A 1 100 ? -28.802 -14.152 8.520   1.00 28.00  ? 618  LEU   A CA   1 
ATOM   864  C  C    . LEU   A 1 100 ? -29.986 -14.958 9.035   1.00 32.60  ? 618  LEU   A C    1 
ATOM   865  O  O    . LEU   A 1 100 ? -29.817 -15.960 9.735   1.00 35.91  ? 618  LEU   A O    1 
ATOM   866  C  CB   . LEU   A 1 100 ? -28.427 -14.672 7.120   1.00 32.28  ? 618  LEU   A CB   1 
ATOM   867  C  CG   . LEU   A 1 100 ? -27.300 -13.948 6.380   1.00 40.35  ? 618  LEU   A CG   1 
ATOM   868  C  CD1  . LEU   A 1 100 ? -26.881 -14.732 5.150   1.00 43.26  ? 618  LEU   A CD1  1 
ATOM   869  C  CD2  . LEU   A 1 100 ? -27.725 -12.533 5.985   1.00 33.57  ? 618  LEU   A CD2  1 
ATOM   870  N  N    . GLN   A 1 101 ? -31.185 -14.519 8.676   1.00 30.84  ? 619  GLN   A N    1 
ATOM   871  C  CA   . GLN   A 1 101 ? -32.409 -15.276 8.938   1.00 25.72  ? 619  GLN   A CA   1 
ATOM   872  C  C    . GLN   A 1 101 ? -33.283 -15.173 7.706   1.00 30.89  ? 619  GLN   A C    1 
ATOM   873  O  O    . GLN   A 1 101 ? -33.082 -14.284 6.886   1.00 29.73  ? 619  GLN   A O    1 
ATOM   874  C  CB   . GLN   A 1 101 ? -33.146 -14.729 10.165  1.00 25.16  ? 619  GLN   A CB   1 
ATOM   875  C  CG   . GLN   A 1 101 ? -33.728 -13.331 9.944   1.00 29.08  ? 619  GLN   A CG   1 
ATOM   876  C  CD   . GLN   A 1 101 ? -34.285 -12.723 11.214  1.00 37.22  ? 619  GLN   A CD   1 
ATOM   877  O  OE1  . GLN   A 1 101 ? -34.032 -13.209 12.311  1.00 35.84  ? 619  GLN   A OE1  1 
ATOM   878  N  NE2  . GLN   A 1 101 ? -35.069 -11.671 11.064  1.00 33.42  ? 619  GLN   A NE2  1 
ATOM   879  N  N    . ILE   A 1 102 ? -34.246 -16.071 7.565   1.00 31.69  ? 620  ILE   A N    1 
ATOM   880  C  CA   . ILE   A 1 102 ? -35.211 -15.958 6.476   1.00 35.56  ? 620  ILE   A CA   1 
ATOM   881  C  C    . ILE   A 1 102 ? -36.085 -14.713 6.650   1.00 34.54  ? 620  ILE   A C    1 
ATOM   882  O  O    . ILE   A 1 102 ? -36.622 -14.486 7.730   1.00 29.47  ? 620  ILE   A O    1 
ATOM   883  C  CB   . ILE   A 1 102 ? -36.133 -17.186 6.376   1.00 30.45  ? 620  ILE   A CB   1 
ATOM   884  C  CG1  . ILE   A 1 102 ? -35.316 -18.462 6.112   1.00 29.98  ? 620  ILE   A CG1  1 
ATOM   885  C  CG2  . ILE   A 1 102 ? -37.193 -16.957 5.286   1.00 23.53  ? 620  ILE   A CG2  1 
ATOM   886  C  CD1  . ILE   A 1 102 ? -36.177 -19.678 5.921   1.00 34.07  ? 620  ILE   A CD1  1 
ATOM   887  N  N    . ASN   A 1 103 ? -36.242 -13.929 5.580   1.00 27.45  ? 621  ASN   A N    1 
ATOM   888  C  CA   . ASN   A 1 103 ? -37.090 -12.745 5.640   1.00 28.95  ? 621  ASN   A CA   1 
ATOM   889  C  C    . ASN   A 1 103 ? -38.559 -13.154 5.604   1.00 36.25  ? 621  ASN   A C    1 
ATOM   890  O  O    . ASN   A 1 103 ? -38.993 -13.808 4.656   1.00 44.14  ? 621  ASN   A O    1 
ATOM   891  C  CB   . ASN   A 1 103 ? -36.755 -11.801 4.479   1.00 31.08  ? 621  ASN   A CB   1 
ATOM   892  C  CG   . ASN   A 1 103 ? -37.697 -10.623 4.381   1.00 36.65  ? 621  ASN   A CG   1 
ATOM   893  O  OD1  . ASN   A 1 103 ? -38.352 -10.241 5.352   1.00 45.39  ? 621  ASN   A OD1  1 
ATOM   894  N  ND2  . ASN   A 1 103 ? -37.772 -10.032 3.192   1.00 43.91  ? 621  ASN   A ND2  1 
ATOM   895  N  N    . PRO   A 1 104 ? -39.327 -12.776 6.638   1.00 36.25  ? 622  PRO   A N    1 
ATOM   896  C  CA   . PRO   A 1 104 ? -40.755 -13.115 6.667   1.00 40.29  ? 622  PRO   A CA   1 
ATOM   897  C  C    . PRO   A 1 104 ? -41.509 -12.556 5.470   1.00 40.82  ? 622  PRO   A C    1 
ATOM   898  O  O    . PRO   A 1 104 ? -42.456 -13.194 5.006   1.00 46.13  ? 622  PRO   A O    1 
ATOM   899  C  CB   . PRO   A 1 104 ? -41.247 -12.484 7.978   1.00 39.56  ? 622  PRO   A CB   1 
ATOM   900  C  CG   . PRO   A 1 104 ? -40.183 -11.494 8.360   1.00 40.85  ? 622  PRO   A CG   1 
ATOM   901  C  CD   . PRO   A 1 104 ? -38.904 -12.073 7.863   1.00 36.08  ? 622  PRO   A CD   1 
ATOM   902  N  N    . ASN   A 1 105 ? -41.078 -11.400 4.970   1.00 41.18  ? 623  ASN   A N    1 
ATOM   903  C  CA   . ASN   A 1 105 ? -41.688 -10.782 3.787   1.00 40.27  ? 623  ASN   A CA   1 
ATOM   904  C  C    . ASN   A 1 105 ? -41.053 -11.193 2.467   1.00 31.98  ? 623  ASN   A C    1 
ATOM   905  O  O    . ASN   A 1 105 ? -41.256 -10.520 1.467   1.00 34.07  ? 623  ASN   A O    1 
ATOM   906  C  CB   . ASN   A 1 105 ? -41.628 -9.250  3.866   1.00 46.14  ? 623  ASN   A CB   1 
ATOM   907  C  CG   . ASN   A 1 105 ? -42.244 -8.709  5.124   1.00 64.11  ? 623  ASN   A CG   1 
ATOM   908  O  OD1  . ASN   A 1 105 ? -43.264 -9.215  5.592   1.00 64.63  ? 623  ASN   A OD1  1 
ATOM   909  N  ND2  . ASN   A 1 105 ? -41.629 -7.670  5.687   1.00 64.44  ? 623  ASN   A ND2  1 
ATOM   910  N  N    . SER   A 1 106 ? -40.299 -12.288 2.458   1.00 29.86  ? 624  SER   A N    1 
ATOM   911  C  CA   . SER   A 1 106 ? -39.641 -12.763 1.234   1.00 28.41  ? 624  SER   A CA   1 
ATOM   912  C  C    . SER   A 1 106 ? -40.608 -12.892 0.059   1.00 31.04  ? 624  SER   A C    1 
ATOM   913  O  O    . SER   A 1 106 ? -40.228 -12.716 -1.089  1.00 33.94  ? 624  SER   A O    1 
ATOM   914  C  CB   . SER   A 1 106 ? -38.978 -14.135 1.465   1.00 26.46  ? 624  SER   A CB   1 
ATOM   915  O  OG   . SER   A 1 106 ? -39.922 -15.048 1.998   1.00 32.02  ? 624  SER   A OG   1 
ATOM   916  N  N    . GLY   A 1 107 ? -41.851 -13.231 0.365   1.00 31.97  ? 625  GLY   A N    1 
ATOM   917  C  CA   . GLY   A 1 107 ? -42.870 -13.437 -0.645  1.00 34.08  ? 625  GLY   A CA   1 
ATOM   918  C  C    . GLY   A 1 107 ? -43.412 -12.199 -1.303  1.00 38.37  ? 625  GLY   A C    1 
ATOM   919  O  O    . GLY   A 1 107 ? -43.814 -12.240 -2.463  1.00 38.76  ? 625  GLY   A O    1 
ATOM   920  N  N    . LEU   A 1 108 ? -43.437 -11.103 -0.555  1.00 40.74  ? 626  LEU   A N    1 
ATOM   921  C  CA   . LEU   A 1 108 ? -43.847 -9.812  -1.088  1.00 43.55  ? 626  LEU   A CA   1 
ATOM   922  C  C    . LEU   A 1 108 ? -42.948 -9.423  -2.236  1.00 38.34  ? 626  LEU   A C    1 
ATOM   923  O  O    . LEU   A 1 108 ? -43.404 -9.047  -3.299  1.00 50.50  ? 626  LEU   A O    1 
ATOM   924  C  CB   . LEU   A 1 108 ? -43.781 -8.740  -0.003  1.00 46.95  ? 626  LEU   A CB   1 
ATOM   925  C  CG   . LEU   A 1 108 ? -45.100 -8.134  0.446   1.00 52.94  ? 626  LEU   A CG   1 
ATOM   926  C  CD1  . LEU   A 1 108 ? -44.842 -6.933  1.336   1.00 55.98  ? 626  LEU   A CD1  1 
ATOM   927  C  CD2  . LEU   A 1 108 ? -45.869 -7.753  -0.761  1.00 43.33  ? 626  LEU   A CD2  1 
ATOM   928  N  N    . CYS   A 1 109 ? -41.649 -9.521  -1.979  1.00 50.41  ? 627  CYS   A N    1 
ATOM   929  C  CA   . CYS   A 1 109 ? -40.606 -9.204  -2.949  1.00 64.00  ? 627  CYS   A CA   1 
ATOM   930  C  C    . CYS   A 1 109 ? -40.627 -10.164 -4.156  1.00 61.35  ? 627  CYS   A C    1 
ATOM   931  O  O    . CYS   A 1 109 ? -40.435 -9.748  -5.304  1.00 63.41  ? 627  CYS   A O    1 
ATOM   932  C  CB   . CYS   A 1 109 ? -39.220 -9.261  -2.263  1.00 75.55  ? 627  CYS   A CB   1 
ATOM   933  S  SG   . CYS   A 1 109 ? -39.072 -8.591  -0.540  1.00 77.63  ? 627  CYS   A SG   1 
ATOM   934  N  N    . ASN   A 1 110 ? -40.849 -11.450 -3.879  1.00 51.77  ? 628  ASN   A N    1 
ATOM   935  C  CA   . ASN   A 1 110 ? -40.719 -12.518 -4.876  1.00 41.27  ? 628  ASN   A CA   1 
ATOM   936  C  C    . ASN   A 1 110 ? -41.874 -13.507 -4.809  1.00 31.11  ? 628  ASN   A C    1 
ATOM   937  O  O    . ASN   A 1 110 ? -41.919 -14.340 -3.913  1.00 36.08  ? 628  ASN   A O    1 
ATOM   938  C  CB   . ASN   A 1 110 ? -39.421 -13.280 -4.668  1.00 37.66  ? 628  ASN   A CB   1 
ATOM   939  C  CG   . ASN   A 1 110 ? -38.269 -12.381 -4.292  1.00 50.30  ? 628  ASN   A CG   1 
ATOM   940  O  OD1  . ASN   A 1 110 ? -37.590 -11.841 -5.162  1.00 48.27  ? 628  ASN   A OD1  1 
ATOM   941  N  ND2  . ASN   A 1 110 ? -38.025 -12.229 -2.987  1.00 48.86  ? 628  ASN   A ND2  1 
ATOM   942  N  N    . GLU   A 1 111 ? -42.808 -13.408 -5.738  1.00 32.82  ? 629  GLU   A N    1 
ATOM   943  C  CA   . GLU   A 1 111 ? -43.937 -14.328 -5.773  1.00 43.36  ? 629  GLU   A CA   1 
ATOM   944  C  C    . GLU   A 1 111 ? -43.455 -15.782 -5.847  1.00 43.11  ? 629  GLU   A C    1 
ATOM   945  O  O    . GLU   A 1 111 ? -44.032 -16.676 -5.228  1.00 39.40  ? 629  GLU   A O    1 
ATOM   946  C  CB   . GLU   A 1 111 ? -44.845 -14.009 -6.963  1.00 47.17  ? 629  GLU   A CB   1 
ATOM   947  C  CG   . GLU   A 1 111 ? -46.242 -14.591 -6.831  1.00 62.60  ? 629  GLU   A CG   1 
ATOM   948  C  CD   . GLU   A 1 111 ? -47.165 -14.206 -7.982  1.00 71.43  ? 629  GLU   A CD   1 
ATOM   949  O  OE1  . GLU   A 1 111 ? -46.756 -13.399 -8.851  1.00 68.12  ? 629  GLU   A OE1  1 
ATOM   950  O  OE2  . GLU   A 1 111 ? -48.305 -14.720 -8.013  1.00 78.04  ? 629  GLU   A OE2  1 
ATOM   951  N  N    . ASP   A 1 112 ? -42.365 -16.004 -6.572  1.00 43.50  ? 630  ASP   A N    1 
ATOM   952  C  CA   . ASP   A 1 112 ? -41.849 -17.354 -6.771  1.00 40.56  ? 630  ASP   A CA   1 
ATOM   953  C  C    . ASP   A 1 112 ? -40.812 -17.761 -5.705  1.00 37.77  ? 630  ASP   A C    1 
ATOM   954  O  O    . ASP   A 1 112 ? -39.950 -18.606 -5.966  1.00 34.29  ? 630  ASP   A O    1 
ATOM   955  C  CB   . ASP   A 1 112 ? -41.242 -17.475 -8.177  1.00 41.17  ? 630  ASP   A CB   1 
ATOM   956  C  CG   . ASP   A 1 112 ? -41.260 -18.913 -8.704  1.00 54.22  ? 630  ASP   A CG   1 
ATOM   957  O  OD1  . ASP   A 1 112 ? -41.976 -19.770 -8.123  1.00 42.11  ? 630  ASP   A OD1  1 
ATOM   958  O  OD2  . ASP   A 1 112 ? -40.555 -19.183 -9.701  1.00 57.87  ? 630  ASP   A OD2  1 
ATOM   959  N  N    . HIS   A 1 113 ? -40.916 -17.202 -4.504  1.00 33.60  ? 631  HIS   A N    1 
ATOM   960  C  CA   . HIS   A 1 113 ? -39.872 -17.373 -3.501  1.00 29.63  ? 631  HIS   A CA   1 
ATOM   961  C  C    . HIS   A 1 113 ? -39.675 -18.830 -3.023  1.00 24.62  ? 631  HIS   A C    1 
ATOM   962  O  O    . HIS   A 1 113 ? -38.574 -19.226 -2.670  1.00 30.70  ? 631  HIS   A O    1 
ATOM   963  C  CB   . HIS   A 1 113 ? -40.170 -16.396 -2.344  1.00 37.81  ? 631  HIS   A CB   1 
ATOM   964  C  CG   . HIS   A 1 113 ? -41.280 -16.811 -1.432  1.00 50.58  ? 631  HIS   A CG   1 
ATOM   965  N  ND1  . HIS   A 1 113 ? -41.300 -18.010 -0.755  1.00 69.14  ? 631  HIS   A ND1  1 
ATOM   966  C  CD2  . HIS   A 1 113 ? -42.521 -16.291 -1.268  1.00 52.27  ? 631  HIS   A CD2  1 
ATOM   967  C  CE1  . HIS   A 1 113 ? -42.429 -18.116 -0.087  1.00 63.88  ? 631  HIS   A CE1  1 
ATOM   968  N  NE2  . HIS   A 1 113 ? -43.197 -17.093 -0.396  1.00 50.78  ? 631  HIS   A NE2  1 
ATOM   969  N  N    . LEU   A 1 114 ? -40.725 -19.642 -3.030  1.00 29.51  ? 632  LEU   A N    1 
ATOM   970  C  CA   . LEU   A 1 114 ? -40.567 -21.027 -2.575  1.00 35.01  ? 632  LEU   A CA   1 
ATOM   971  C  C    . LEU   A 1 114 ? -39.622 -21.829 -3.480  1.00 27.48  ? 632  LEU   A C    1 
ATOM   972  O  O    . LEU   A 1 114 ? -38.786 -22.583 -3.002  1.00 28.44  ? 632  LEU   A O    1 
ATOM   973  C  CB   . LEU   A 1 114 ? -41.918 -21.745 -2.474  1.00 26.70  ? 632  LEU   A CB   1 
ATOM   974  C  CG   . LEU   A 1 114 ? -42.841 -21.241 -1.359  1.00 31.95  ? 632  LEU   A CG   1 
ATOM   975  C  CD1  . LEU   A 1 114 ? -44.069 -22.136 -1.156  1.00 29.86  ? 632  LEU   A CD1  1 
ATOM   976  C  CD2  . LEU   A 1 114 ? -42.030 -21.132 -0.081  1.00 31.54  ? 632  LEU   A CD2  1 
ATOM   977  N  N    . SER   A 1 115 ? -39.722 -21.647 -4.785  1.00 29.60  ? 633  SER   A N    1 
ATOM   978  C  CA   . SER   A 1 115 ? -38.767 -22.310 -5.658  1.00 34.02  ? 633  SER   A CA   1 
ATOM   979  C  C    . SER   A 1 115 ? -37.364 -21.719 -5.441  1.00 28.08  ? 633  SER   A C    1 
ATOM   980  O  O    . SER   A 1 115 ? -36.383 -22.451 -5.469  1.00 33.44  ? 633  SER   A O    1 
ATOM   981  C  CB   . SER   A 1 115 ? -39.204 -22.215 -7.133  1.00 43.69  ? 633  SER   A CB   1 
ATOM   982  O  OG   . SER   A 1 115 ? -39.002 -20.929 -7.658  1.00 55.51  ? 633  SER   A OG   1 
ATOM   983  N  N    . TYR   A 1 116 ? -37.244 -20.417 -5.167  1.00 27.39  ? 634  TYR   A N    1 
ATOM   984  C  CA   . TYR   A 1 116 ? -35.905 -19.895 -4.900  1.00 21.50  ? 634  TYR   A CA   1 
ATOM   985  C  C    . TYR   A 1 116 ? -35.312 -20.519 -3.624  1.00 20.46  ? 634  TYR   A C    1 
ATOM   986  O  O    . TYR   A 1 116 ? -34.112 -20.785 -3.561  1.00 24.91  ? 634  TYR   A O    1 
ATOM   987  C  CB   . TYR   A 1 116 ? -35.882 -18.368 -4.756  1.00 22.16  ? 634  TYR   A CB   1 
ATOM   988  C  CG   . TYR   A 1 116 ? -36.475 -17.610 -5.927  1.00 25.97  ? 634  TYR   A CG   1 
ATOM   989  C  CD1  . TYR   A 1 116 ? -36.488 -18.157 -7.208  1.00 23.70  ? 634  TYR   A CD1  1 
ATOM   990  C  CD2  . TYR   A 1 116 ? -37.037 -16.348 -5.738  1.00 29.00  ? 634  TYR   A CD2  1 
ATOM   991  C  CE1  . TYR   A 1 116 ? -37.075 -17.466 -8.281  1.00 33.30  ? 634  TYR   A CE1  1 
ATOM   992  C  CE2  . TYR   A 1 116 ? -37.595 -15.639 -6.788  1.00 32.73  ? 634  TYR   A CE2  1 
ATOM   993  C  CZ   . TYR   A 1 116 ? -37.616 -16.198 -8.059  1.00 32.70  ? 634  TYR   A CZ   1 
ATOM   994  O  OH   . TYR   A 1 116 ? -38.177 -15.492 -9.092  1.00 40.31  ? 634  TYR   A OH   1 
ATOM   995  N  N    . PHE   A 1 117 ? -36.141 -20.703 -2.597  1.00 25.02  ? 635  PHE   A N    1 
ATOM   996  C  CA   . PHE   A 1 117 ? -35.630 -21.294 -1.357  1.00 28.65  ? 635  PHE   A CA   1 
ATOM   997  C  C    . PHE   A 1 117 ? -35.258 -22.767 -1.589  1.00 26.60  ? 635  PHE   A C    1 
ATOM   998  O  O    . PHE   A 1 117 ? -34.266 -23.245 -1.044  1.00 28.65  ? 635  PHE   A O    1 
ATOM   999  C  CB   . PHE   A 1 117 ? -36.648 -21.160 -0.213  1.00 22.06  ? 635  PHE   A CB   1 
ATOM   1000 C  CG   . PHE   A 1 117 ? -36.657 -19.791 0.430   1.00 28.48  ? 635  PHE   A CG   1 
ATOM   1001 C  CD1  . PHE   A 1 117 ? -35.624 -19.394 1.267   1.00 25.13  ? 635  PHE   A CD1  1 
ATOM   1002 C  CD2  . PHE   A 1 117 ? -37.691 -18.901 0.185   1.00 28.56  ? 635  PHE   A CD2  1 
ATOM   1003 C  CE1  . PHE   A 1 117 ? -35.624 -18.128 1.853   1.00 27.79  ? 635  PHE   A CE1  1 
ATOM   1004 C  CE2  . PHE   A 1 117 ? -37.694 -17.628 0.768   1.00 30.12  ? 635  PHE   A CE2  1 
ATOM   1005 C  CZ   . PHE   A 1 117 ? -36.667 -17.252 1.609   1.00 24.66  ? 635  PHE   A CZ   1 
ATOM   1006 N  N    . LYS   A 1 118 ? -36.071 -23.482 -2.376  1.00 27.87  ? 636  LYS   A N    1 
ATOM   1007 C  CA   . LYS   A 1 118 ? -35.756 -24.880 -2.694  1.00 30.50  ? 636  LYS   A CA   1 
ATOM   1008 C  C    . LYS   A 1 118 ? -34.407 -24.952 -3.405  1.00 31.29  ? 636  LYS   A C    1 
ATOM   1009 O  O    . LYS   A 1 118 ? -33.591 -25.822 -3.125  1.00 29.48  ? 636  LYS   A O    1 
ATOM   1010 C  CB   . LYS   A 1 118 ? -36.845 -25.527 -3.558  1.00 31.67  ? 636  LYS   A CB   1 
ATOM   1011 C  CG   . LYS   A 1 118 ? -36.554 -27.003 -3.910  1.00 32.74  ? 636  LYS   A CG   1 
ATOM   1012 C  CD   . LYS   A 1 118 ? -37.699 -27.634 -4.687  1.00 35.11  ? 636  LYS   A CD   1 
ATOM   1013 C  CE   . LYS   A 1 118 ? -37.532 -29.134 -4.812  1.00 38.90  ? 636  LYS   A CE   1 
ATOM   1014 N  NZ   . LYS   A 1 118 ? -38.583 -29.673 -5.716  1.00 40.52  ? 636  LYS   A NZ   1 
ATOM   1015 N  N    . PHE   A 1 119 ? -34.178 -24.011 -4.313  1.00 31.16  ? 637  PHE   A N    1 
ATOM   1016 C  CA   . PHE   A 1 119 ? -32.903 -23.890 -5.004  1.00 30.93  ? 637  PHE   A CA   1 
ATOM   1017 C  C    . PHE   A 1 119 ? -31.772 -23.655 -4.019  1.00 30.85  ? 637  PHE   A C    1 
ATOM   1018 O  O    . PHE   A 1 119 ? -30.729 -24.298 -4.103  1.00 30.58  ? 637  PHE   A O    1 
ATOM   1019 C  CB   . PHE   A 1 119 ? -32.958 -22.754 -6.025  1.00 28.23  ? 637  PHE   A CB   1 
ATOM   1020 C  CG   . PHE   A 1 119 ? -31.611 -22.267 -6.485  1.00 28.86  ? 637  PHE   A CG   1 
ATOM   1021 C  CD1  . PHE   A 1 119 ? -30.770 -23.082 -7.232  1.00 25.96  ? 637  PHE   A CD1  1 
ATOM   1022 C  CD2  . PHE   A 1 119 ? -31.211 -20.965 -6.221  1.00 32.30  ? 637  PHE   A CD2  1 
ATOM   1023 C  CE1  . PHE   A 1 119 ? -29.538 -22.616 -7.678  1.00 30.71  ? 637  PHE   A CE1  1 
ATOM   1024 C  CE2  . PHE   A 1 119 ? -29.994 -20.488 -6.677  1.00 32.93  ? 637  PHE   A CE2  1 
ATOM   1025 C  CZ   . PHE   A 1 119 ? -29.145 -21.313 -7.388  1.00 24.99  ? 637  PHE   A CZ   1 
ATOM   1026 N  N    . ILE   A 1 120 ? -31.979 -22.726 -3.088  1.00 25.60  ? 638  ILE   A N    1 
ATOM   1027 C  CA   . ILE   A 1 120 ? -30.966 -22.459 -2.080  1.00 27.89  ? 638  ILE   A CA   1 
ATOM   1028 C  C    . ILE   A 1 120 ? -30.692 -23.728 -1.277  1.00 17.74  ? 638  ILE   A C    1 
ATOM   1029 O  O    . ILE   A 1 120 ? -29.553 -24.021 -0.966  1.00 24.63  ? 638  ILE   A O    1 
ATOM   1030 C  CB   . ILE   A 1 120 ? -31.380 -21.303 -1.147  1.00 30.31  ? 638  ILE   A CB   1 
ATOM   1031 C  CG1  . ILE   A 1 120 ? -31.519 -20.013 -1.967  1.00 31.35  ? 638  ILE   A CG1  1 
ATOM   1032 C  CG2  . ILE   A 1 120 ? -30.342 -21.124 -0.070  1.00 26.33  ? 638  ILE   A CG2  1 
ATOM   1033 C  CD1  . ILE   A 1 120 ? -32.006 -18.813 -1.208  1.00 31.91  ? 638  ILE   A CD1  1 
ATOM   1034 N  N    . GLY   A 1 121 ? -31.745 -24.467 -0.967  1.00 22.27  ? 639  GLY   A N    1 
ATOM   1035 C  CA   . GLY   A 1 121 ? -31.607 -25.748 -0.272  1.00 33.13  ? 639  GLY   A CA   1 
ATOM   1036 C  C    . GLY   A 1 121 ? -30.797 -26.783 -1.057  1.00 34.21  ? 639  GLY   A C    1 
ATOM   1037 O  O    . GLY   A 1 121 ? -29.918 -27.432 -0.499  1.00 30.34  ? 639  GLY   A O    1 
ATOM   1038 N  N    . ARG   A 1 122 ? -31.097 -26.928 -2.353  1.00 27.86  ? 640  ARG   A N    1 
ATOM   1039 C  CA   . ARG   A 1 122 ? -30.318 -27.787 -3.238  1.00 24.34  ? 640  ARG   A CA   1 
ATOM   1040 C  C    . ARG   A 1 122 ? -28.842 -27.403 -3.237  1.00 30.61  ? 640  ARG   A C    1 
ATOM   1041 O  O    . ARG   A 1 122 ? -27.984 -28.268 -3.156  1.00 28.50  ? 640  ARG   A O    1 
ATOM   1042 C  CB   . ARG   A 1 122 ? -30.874 -27.751 -4.675  1.00 21.71  ? 640  ARG   A CB   1 
ATOM   1043 C  CG   . ARG   A 1 122 ? -32.162 -28.580 -4.868  1.00 21.97  ? 640  ARG   A CG   1 
ATOM   1044 C  CD   . ARG   A 1 122 ? -32.555 -28.748 -6.332  1.00 24.63  ? 640  ARG   A CD   1 
ATOM   1045 N  NE   . ARG   A 1 122 ? -33.723 -29.618 -6.476  1.00 26.93  ? 640  ARG   A NE   1 
ATOM   1046 C  CZ   . ARG   A 1 122 ? -34.207 -30.041 -7.645  1.00 31.70  ? 640  ARG   A CZ   1 
ATOM   1047 N  NH1  . ARG   A 1 122 ? -33.620 -29.686 -8.787  1.00 35.12  ? 640  ARG   A NH1  1 
ATOM   1048 N  NH2  . ARG   A 1 122 ? -35.282 -30.803 -7.679  1.00 25.21  ? 640  ARG   A NH2  1 
ATOM   1049 N  N    . VAL   A 1 123 ? -28.534 -26.105 -3.304  1.00 27.87  ? 641  VAL   A N    1 
ATOM   1050 C  CA   . VAL   A 1 123 ? -27.138 -25.695 -3.358  1.00 22.89  ? 641  VAL   A CA   1 
ATOM   1051 C  C    . VAL   A 1 123 ? -26.428 -25.949 -2.025  1.00 29.57  ? 641  VAL   A C    1 
ATOM   1052 O  O    . VAL   A 1 123 ? -25.305 -26.443 -2.000  1.00 30.64  ? 641  VAL   A O    1 
ATOM   1053 C  CB   . VAL   A 1 123 ? -27.010 -24.212 -3.748  1.00 33.44  ? 641  VAL   A CB   1 
ATOM   1054 C  CG1  . VAL   A 1 123 ? -25.601 -23.686 -3.449  1.00 26.05  ? 641  VAL   A CG1  1 
ATOM   1055 C  CG2  . VAL   A 1 123 ? -27.392 -24.028 -5.233  1.00 32.92  ? 641  VAL   A CG2  1 
ATOM   1056 N  N    . ALA   A 1 124 ? -27.091 -25.614 -0.921  1.00 27.53  ? 642  ALA   A N    1 
ATOM   1057 C  CA   . ALA   A 1 124 ? -26.583 -25.968 0.411   1.00 28.29  ? 642  ALA   A CA   1 
ATOM   1058 C  C    . ALA   A 1 124 ? -26.327 -27.468 0.477   1.00 29.52  ? 642  ALA   A C    1 
ATOM   1059 O  O    . ALA   A 1 124 ? -25.255 -27.885 0.874   1.00 34.47  ? 642  ALA   A O    1 
ATOM   1060 C  CB   . ALA   A 1 124 ? -27.572 -25.542 1.492   1.00 22.49  ? 642  ALA   A CB   1 
ATOM   1061 N  N    . GLY   A 1 125 ? -27.322 -28.263 0.067   1.00 36.13  ? 643  GLY   A N    1 
ATOM   1062 C  CA   . GLY   A 1 125 ? -27.172 -29.710 -0.059  1.00 30.72  ? 643  GLY   A CA   1 
ATOM   1063 C  C    . GLY   A 1 125 ? -25.970 -30.111 -0.902  1.00 28.97  ? 643  GLY   A C    1 
ATOM   1064 O  O    . GLY   A 1 125 ? -25.187 -30.976 -0.513  1.00 37.81  ? 643  GLY   A O    1 
ATOM   1065 N  N    . MET   A 1 126 ? -25.812 -29.487 -2.064  1.00 31.39  ? 644  MET   A N    1 
ATOM   1066 C  CA   . MET   A 1 126 ? -24.669 -29.788 -2.913  1.00 32.86  ? 644  MET   A CA   1 
ATOM   1067 C  C    . MET   A 1 126 ? -23.331 -29.489 -2.241  1.00 32.72  ? 644  MET   A C    1 
ATOM   1068 O  O    . MET   A 1 126 ? -22.351 -30.204 -2.467  1.00 32.12  ? 644  MET   A O    1 
ATOM   1069 C  CB   . MET   A 1 126 ? -24.758 -29.022 -4.234  1.00 31.29  ? 644  MET   A CB   1 
ATOM   1070 C  CG   . MET   A 1 126 ? -25.805 -29.568 -5.193  1.00 29.52  ? 644  MET   A CG   1 
ATOM   1071 S  SD   . MET   A 1 126 ? -26.148 -28.375 -6.507  1.00 34.39  ? 644  MET   A SD   1 
ATOM   1072 C  CE   . MET   A 1 126 ? -24.580 -28.394 -7.360  1.00 31.29  ? 644  MET   A CE   1 
ATOM   1073 N  N    . ALA   A 1 127 ? -23.280 -28.432 -1.431  1.00 30.19  ? 645  ALA   A N    1 
ATOM   1074 C  CA   . ALA   A 1 127 ? -22.049 -28.084 -0.732  1.00 30.62  ? 645  ALA   A CA   1 
ATOM   1075 C  C    . ALA   A 1 127 ? -21.659 -29.184 0.240   1.00 31.11  ? 645  ALA   A C    1 
ATOM   1076 O  O    . ALA   A 1 127 ? -20.548 -29.656 0.219   1.00 34.80  ? 645  ALA   A O    1 
ATOM   1077 C  CB   . ALA   A 1 127 ? -22.205 -26.754 0.011   1.00 35.10  ? 645  ALA   A CB   1 
ATOM   1078 N  N    . VAL   A 1 128 ? -22.589 -29.571 1.102   1.00 35.67  ? 646  VAL   A N    1 
ATOM   1079 C  CA   . VAL   A 1 128 ? -22.349 -30.646 2.070   1.00 40.04  ? 646  VAL   A CA   1 
ATOM   1080 C  C    . VAL   A 1 128 ? -21.966 -31.955 1.365   1.00 38.98  ? 646  VAL   A C    1 
ATOM   1081 O  O    . VAL   A 1 128 ? -20.992 -32.617 1.744   1.00 33.97  ? 646  VAL   A O    1 
ATOM   1082 C  CB   . VAL   A 1 128 ? -23.587 -30.890 2.961   1.00 36.50  ? 646  VAL   A CB   1 
ATOM   1083 C  CG1  . VAL   A 1 128 ? -23.372 -32.091 3.838   1.00 29.29  ? 646  VAL   A CG1  1 
ATOM   1084 C  CG2  . VAL   A 1 128 ? -23.888 -29.649 3.820   1.00 32.90  ? 646  VAL   A CG2  1 
ATOM   1085 N  N    . TYR   A 1 129 ? -22.705 -32.295 0.313   1.00 34.37  ? 647  TYR   A N    1 
ATOM   1086 C  CA   . TYR   A 1 129 ? -22.464 -33.532 -0.427  1.00 34.18  ? 647  TYR   A CA   1 
ATOM   1087 C  C    . TYR   A 1 129 ? -21.058 -33.596 -1.029  1.00 35.42  ? 647  TYR   A C    1 
ATOM   1088 O  O    . TYR   A 1 129 ? -20.412 -34.643 -0.998  1.00 40.67  ? 647  TYR   A O    1 
ATOM   1089 C  CB   . TYR   A 1 129 ? -23.515 -33.719 -1.540  1.00 29.09  ? 647  TYR   A CB   1 
ATOM   1090 C  CG   . TYR   A 1 129 ? -23.497 -35.123 -2.124  1.00 35.39  ? 647  TYR   A CG   1 
ATOM   1091 C  CD1  . TYR   A 1 129 ? -24.302 -36.117 -1.598  1.00 34.30  ? 647  TYR   A CD1  1 
ATOM   1092 C  CD2  . TYR   A 1 129 ? -22.651 -35.457 -3.189  1.00 27.54  ? 647  TYR   A CD2  1 
ATOM   1093 C  CE1  . TYR   A 1 129 ? -24.278 -37.421 -2.112  1.00 39.22  ? 647  TYR   A CE1  1 
ATOM   1094 C  CE2  . TYR   A 1 129 ? -22.616 -36.747 -3.708  1.00 35.85  ? 647  TYR   A CE2  1 
ATOM   1095 C  CZ   . TYR   A 1 129 ? -23.435 -37.722 -3.163  1.00 39.65  ? 647  TYR   A CZ   1 
ATOM   1096 O  OH   . TYR   A 1 129 ? -23.418 -38.991 -3.669  1.00 45.97  ? 647  TYR   A OH   1 
ATOM   1097 N  N    . HIS   A 1 130 ? -20.585 -32.490 -1.582  1.00 34.09  ? 648  HIS   A N    1 
ATOM   1098 C  CA   . HIS   A 1 130 ? -19.294 -32.470 -2.283  1.00 33.27  ? 648  HIS   A CA   1 
ATOM   1099 C  C    . HIS   A 1 130 ? -18.154 -31.963 -1.404  1.00 35.63  ? 648  HIS   A C    1 
ATOM   1100 O  O    . HIS   A 1 130 ? -17.052 -31.725 -1.891  1.00 39.92  ? 648  HIS   A O    1 
ATOM   1101 C  CB   . HIS   A 1 130 ? -19.373 -31.598 -3.548  1.00 30.20  ? 648  HIS   A CB   1 
ATOM   1102 C  CG   . HIS   A 1 130 ? -20.242 -32.164 -4.633  1.00 39.96  ? 648  HIS   A CG   1 
ATOM   1103 N  ND1  . HIS   A 1 130 ? -21.580 -31.834 -4.768  1.00 38.27  ? 648  HIS   A ND1  1 
ATOM   1104 C  CD2  . HIS   A 1 130 ? -19.968 -33.024 -5.640  1.00 31.84  ? 648  HIS   A CD2  1 
ATOM   1105 C  CE1  . HIS   A 1 130 ? -22.081 -32.467 -5.811  1.00 41.14  ? 648  HIS   A CE1  1 
ATOM   1106 N  NE2  . HIS   A 1 130 ? -21.128 -33.203 -6.357  1.00 38.10  ? 648  HIS   A NE2  1 
ATOM   1107 N  N    . GLY   A 1 131 ? -18.424 -31.750 -0.119  1.00 36.87  ? 649  GLY   A N    1 
ATOM   1108 C  CA   . GLY   A 1 131 ? -17.373 -31.337 0.803   1.00 34.69  ? 649  GLY   A CA   1 
ATOM   1109 C  C    . GLY   A 1 131 ? -16.922 -29.898 0.632   1.00 40.50  ? 649  GLY   A C    1 
ATOM   1110 O  O    . GLY   A 1 131 ? -15.767 -29.565 0.880   1.00 42.25  ? 649  GLY   A O    1 
ATOM   1111 N  N    . LYS   A 1 132 ? -17.837 -29.029 0.216   1.00 41.70  ? 650  LYS   A N    1 
ATOM   1112 C  CA   . LYS   A 1 132 ? -17.498 -27.620 0.054   1.00 41.11  ? 650  LYS   A CA   1 
ATOM   1113 C  C    . LYS   A 1 132 ? -18.292 -26.783 1.046   1.00 41.54  ? 650  LYS   A C    1 
ATOM   1114 O  O    . LYS   A 1 132 ? -19.253 -27.257 1.645   1.00 45.70  ? 650  LYS   A O    1 
ATOM   1115 C  CB   . LYS   A 1 132 ? -17.771 -27.154 -1.382  1.00 45.77  ? 650  LYS   A CB   1 
ATOM   1116 C  CG   . LYS   A 1 132 ? -17.069 -27.974 -2.469  1.00 47.59  ? 650  LYS   A CG   1 
ATOM   1117 C  CD   . LYS   A 1 132 ? -15.564 -27.971 -2.287  1.00 58.57  ? 650  LYS   A CD   1 
ATOM   1118 C  CE   . LYS   A 1 132 ? -14.882 -29.014 -3.185  1.00 57.70  ? 650  LYS   A CE   1 
ATOM   1119 N  NZ   . LYS   A 1 132 ? -15.000 -28.658 -4.621  1.00 59.21  ? 650  LYS   A NZ   1 
ATOM   1120 N  N    . LEU   A 1 133 ? -17.901 -25.532 1.215   1.00 50.50  ? 651  LEU   A N    1 
ATOM   1121 C  CA   . LEU   A 1 133 ? -18.567 -24.682 2.184   1.00 50.29  ? 651  LEU   A CA   1 
ATOM   1122 C  C    . LEU   A 1 133 ? -19.412 -23.606 1.538   1.00 48.98  ? 651  LEU   A C    1 
ATOM   1123 O  O    . LEU   A 1 133 ? -19.037 -23.042 0.518   1.00 50.86  ? 651  LEU   A O    1 
ATOM   1124 C  CB   . LEU   A 1 133 ? -17.543 -24.030 3.104   1.00 51.69  ? 651  LEU   A CB   1 
ATOM   1125 C  CG   . LEU   A 1 133 ? -16.800 -24.974 4.035   1.00 49.44  ? 651  LEU   A CG   1 
ATOM   1126 C  CD1  . LEU   A 1 133 ? -15.807 -24.179 4.840   1.00 49.64  ? 651  LEU   A CD1  1 
ATOM   1127 C  CD2  . LEU   A 1 133 ? -17.782 -25.671 4.937   1.00 56.06  ? 651  LEU   A CD2  1 
ATOM   1128 N  N    . LEU   A 1 134 ? -20.560 -23.331 2.145   1.00 41.64  ? 652  LEU   A N    1 
ATOM   1129 C  CA   . LEU   A 1 134 ? -21.306 -22.123 1.845   1.00 39.30  ? 652  LEU   A CA   1 
ATOM   1130 C  C    . LEU   A 1 134 ? -20.675 -20.957 2.573   1.00 49.56  ? 652  LEU   A C    1 
ATOM   1131 O  O    . LEU   A 1 134 ? -20.154 -21.113 3.674   1.00 54.13  ? 652  LEU   A O    1 
ATOM   1132 C  CB   . LEU   A 1 134 ? -22.757 -22.250 2.276   1.00 38.35  ? 652  LEU   A CB   1 
ATOM   1133 C  CG   . LEU   A 1 134 ? -23.625 -23.224 1.505   1.00 45.79  ? 652  LEU   A CG   1 
ATOM   1134 C  CD1  . LEU   A 1 134 ? -25.048 -23.027 1.972   1.00 43.95  ? 652  LEU   A CD1  1 
ATOM   1135 C  CD2  . LEU   A 1 134 ? -23.494 -22.966 0.022   1.00 45.81  ? 652  LEU   A CD2  1 
ATOM   1136 N  N    . ASP   A 1 135 ? -20.727 -19.781 1.969   1.00 44.69  ? 653  ASP   A N    1 
ATOM   1137 C  CA   . ASP   A 1 135 ? -20.256 -18.600 2.649   1.00 43.25  ? 653  ASP   A CA   1 
ATOM   1138 C  C    . ASP   A 1 135 ? -21.474 -17.839 3.156   1.00 56.06  ? 653  ASP   A C    1 
ATOM   1139 O  O    . ASP   A 1 135 ? -22.116 -17.105 2.409   1.00 58.60  ? 653  ASP   A O    1 
ATOM   1140 C  CB   . ASP   A 1 135 ? -19.402 -17.741 1.722   1.00 42.69  ? 653  ASP   A CB   1 
ATOM   1141 C  CG   . ASP   A 1 135 ? -18.585 -16.716 2.478   1.00 66.06  ? 653  ASP   A CG   1 
ATOM   1142 O  OD1  . ASP   A 1 135 ? -18.411 -16.881 3.704   1.00 70.46  ? 653  ASP   A OD1  1 
ATOM   1143 O  OD2  . ASP   A 1 135 ? -18.103 -15.753 1.848   1.00 83.41  ? 653  ASP   A OD2  1 
ATOM   1144 N  N    . GLY   A 1 136 ? -21.805 -18.051 4.422   1.00 55.98  ? 654  GLY   A N    1 
ATOM   1145 C  CA   . GLY   A 1 136 ? -22.936 -17.389 5.041   1.00 55.92  ? 654  GLY   A CA   1 
ATOM   1146 C  C    . GLY   A 1 136 ? -23.200 -17.993 6.402   1.00 58.37  ? 654  GLY   A C    1 
ATOM   1147 O  O    . GLY   A 1 136 ? -23.153 -19.212 6.570   1.00 62.82  ? 654  GLY   A O    1 
ATOM   1148 N  N    . PHE   A 1 137 ? -23.470 -17.139 7.379   1.00 46.34  ? 655  PHE   A N    1 
ATOM   1149 C  CA   . PHE   A 1 137 ? -23.740 -17.592 8.738   1.00 48.27  ? 655  PHE   A CA   1 
ATOM   1150 C  C    . PHE   A 1 137 ? -25.180 -17.294 9.107   1.00 37.71  ? 655  PHE   A C    1 
ATOM   1151 O  O    . PHE   A 1 137 ? -25.622 -16.140 9.082   1.00 37.91  ? 655  PHE   A O    1 
ATOM   1152 C  CB   . PHE   A 1 137 ? -22.793 -16.924 9.740   1.00 62.42  ? 655  PHE   A CB   1 
ATOM   1153 C  CG   . PHE   A 1 137 ? -21.700 -16.108 9.101   1.00 75.13  ? 655  PHE   A CG   1 
ATOM   1154 C  CD1  . PHE   A 1 137 ? -20.584 -16.723 8.545   1.00 81.92  ? 655  PHE   A CD1  1 
ATOM   1155 C  CD2  . PHE   A 1 137 ? -21.785 -14.722 9.061   1.00 78.29  ? 655  PHE   A CD2  1 
ATOM   1156 C  CE1  . PHE   A 1 137 ? -19.576 -15.966 7.955   1.00 84.01  ? 655  PHE   A CE1  1 
ATOM   1157 C  CE2  . PHE   A 1 137 ? -20.782 -13.960 8.479   1.00 79.11  ? 655  PHE   A CE2  1 
ATOM   1158 C  CZ   . PHE   A 1 137 ? -19.678 -14.582 7.922   1.00 82.80  ? 655  PHE   A CZ   1 
ATOM   1159 N  N    . PHE   A 1 138 ? -25.912 -18.339 9.443   1.00 32.40  ? 656  PHE   A N    1 
ATOM   1160 C  CA   . PHE   A 1 138 ? -27.322 -18.202 9.770   1.00 33.14  ? 656  PHE   A CA   1 
ATOM   1161 C  C    . PHE   A 1 138 ? -27.523 -18.148 11.275  1.00 34.85  ? 656  PHE   A C    1 
ATOM   1162 O  O    . PHE   A 1 138 ? -26.636 -18.531 12.035  1.00 31.98  ? 656  PHE   A O    1 
ATOM   1163 C  CB   . PHE   A 1 138 ? -28.112 -19.356 9.181   1.00 37.97  ? 656  PHE   A CB   1 
ATOM   1164 C  CG   . PHE   A 1 138 ? -27.872 -19.556 7.719   1.00 52.21  ? 656  PHE   A CG   1 
ATOM   1165 C  CD1  . PHE   A 1 138 ? -28.198 -18.562 6.814   1.00 56.31  ? 656  PHE   A CD1  1 
ATOM   1166 C  CD2  . PHE   A 1 138 ? -27.344 -20.746 7.244   1.00 61.64  ? 656  PHE   A CD2  1 
ATOM   1167 C  CE1  . PHE   A 1 138 ? -27.983 -18.733 5.458   1.00 56.12  ? 656  PHE   A CE1  1 
ATOM   1168 C  CE2  . PHE   A 1 138 ? -27.133 -20.930 5.886   1.00 65.44  ? 656  PHE   A CE2  1 
ATOM   1169 C  CZ   . PHE   A 1 138 ? -27.454 -19.916 4.995   1.00 63.21  ? 656  PHE   A CZ   1 
ATOM   1170 N  N    . ILE   A 1 139 ? -28.690 -17.687 11.702  1.00 30.56  ? 657  ILE   A N    1 
ATOM   1171 C  CA   . ILE   A 1 139 ? -28.996 -17.694 13.121  1.00 31.80  ? 657  ILE   A CA   1 
ATOM   1172 C  C    . ILE   A 1 139 ? -29.174 -19.133 13.577  1.00 35.80  ? 657  ILE   A C    1 
ATOM   1173 O  O    . ILE   A 1 139 ? -29.511 -20.016 12.783  1.00 31.13  ? 657  ILE   A O    1 
ATOM   1174 C  CB   . ILE   A 1 139 ? -30.253 -16.901 13.444  1.00 29.37  ? 657  ILE   A CB   1 
ATOM   1175 C  CG1  . ILE   A 1 139 ? -31.459 -17.499 12.723  1.00 27.62  ? 657  ILE   A CG1  1 
ATOM   1176 C  CG2  . ILE   A 1 139 ? -30.058 -15.458 13.042  1.00 32.93  ? 657  ILE   A CG2  1 
ATOM   1177 C  CD1  . ILE   A 1 139 ? -32.798 -16.886 13.170  1.00 30.33  ? 657  ILE   A CD1  1 
ATOM   1178 N  N    . ARG   A 1 140 ? -28.938 -19.367 14.857  1.00 30.75  ? 658  ARG   A N    1 
ATOM   1179 C  CA   . ARG   A 1 140 ? -28.974 -20.720 15.409  1.00 29.84  ? 658  ARG   A CA   1 
ATOM   1180 C  C    . ARG   A 1 140 ? -30.326 -21.443 15.204  1.00 29.97  ? 658  ARG   A C    1 
ATOM   1181 O  O    . ARG   A 1 140 ? -30.343 -22.627 14.886  1.00 34.24  ? 658  ARG   A O    1 
ATOM   1182 C  CB   . ARG   A 1 140 ? -28.608 -20.646 16.886  1.00 41.60  ? 658  ARG   A CB   1 
ATOM   1183 C  CG   . ARG   A 1 140 ? -28.129 -21.927 17.491  1.00 58.97  ? 658  ARG   A CG   1 
ATOM   1184 C  CD   . ARG   A 1 140 ? -27.520 -21.627 18.858  1.00 59.43  ? 658  ARG   A CD   1 
ATOM   1185 N  NE   . ARG   A 1 140 ? -26.641 -22.706 19.279  1.00 69.68  ? 658  ARG   A NE   1 
ATOM   1186 C  CZ   . ARG   A 1 140 ? -27.013 -23.684 20.098  1.00 80.31  ? 658  ARG   A CZ   1 
ATOM   1187 N  NH1  . ARG   A 1 140 ? -28.246 -23.701 20.592  1.00 85.95  ? 658  ARG   A NH1  1 
ATOM   1188 N  NH2  . ARG   A 1 140 ? -26.152 -24.641 20.424  1.00 77.79  ? 658  ARG   A NH2  1 
ATOM   1189 N  N    . PRO   A 1 141 ? -31.468 -20.742 15.366  1.00 32.02  ? 659  PRO   A N    1 
ATOM   1190 C  CA   . PRO   A 1 141 ? -32.725 -21.430 15.009  1.00 30.50  ? 659  PRO   A CA   1 
ATOM   1191 C  C    . PRO   A 1 141 ? -32.813 -21.967 13.557  1.00 26.42  ? 659  PRO   A C    1 
ATOM   1192 O  O    . PRO   A 1 141 ? -33.579 -22.886 13.302  1.00 29.35  ? 659  PRO   A O    1 
ATOM   1193 C  CB   . PRO   A 1 141 ? -33.784 -20.344 15.227  1.00 32.22  ? 659  PRO   A CB   1 
ATOM   1194 C  CG   . PRO   A 1 141 ? -33.202 -19.507 16.336  1.00 32.26  ? 659  PRO   A CG   1 
ATOM   1195 C  CD   . PRO   A 1 141 ? -31.731 -19.446 16.025  1.00 31.09  ? 659  PRO   A CD   1 
ATOM   1196 N  N    . PHE   A 1 142 ? -32.030 -21.427 12.634  1.00 32.70  ? 660  PHE   A N    1 
ATOM   1197 C  CA   . PHE   A 1 142 ? -32.070 -21.932 11.279  1.00 25.34  ? 660  PHE   A CA   1 
ATOM   1198 C  C    . PHE   A 1 142 ? -31.565 -23.376 11.304  1.00 27.08  ? 660  PHE   A C    1 
ATOM   1199 O  O    . PHE   A 1 142 ? -32.198 -24.276 10.768  1.00 28.32  ? 660  PHE   A O    1 
ATOM   1200 C  CB   . PHE   A 1 142 ? -31.223 -21.066 10.346  1.00 26.72  ? 660  PHE   A CB   1 
ATOM   1201 C  CG   . PHE   A 1 142 ? -31.386 -21.401 8.882   1.00 27.48  ? 660  PHE   A CG   1 
ATOM   1202 C  CD1  . PHE   A 1 142 ? -32.239 -20.658 8.077   1.00 31.07  ? 660  PHE   A CD1  1 
ATOM   1203 C  CD2  . PHE   A 1 142 ? -30.670 -22.438 8.311   1.00 33.12  ? 660  PHE   A CD2  1 
ATOM   1204 C  CE1  . PHE   A 1 142 ? -32.381 -20.944 6.730   1.00 30.32  ? 660  PHE   A CE1  1 
ATOM   1205 C  CE2  . PHE   A 1 142 ? -30.814 -22.744 6.953   1.00 33.82  ? 660  PHE   A CE2  1 
ATOM   1206 C  CZ   . PHE   A 1 142 ? -31.679 -21.998 6.170   1.00 36.36  ? 660  PHE   A CZ   1 
ATOM   1207 N  N    . TYR   A 1 143 ? -30.435 -23.585 11.964  1.00 28.88  ? 661  TYR   A N    1 
ATOM   1208 C  CA   . TYR   A 1 143 ? -29.821 -24.899 11.999  1.00 32.79  ? 661  TYR   A CA   1 
ATOM   1209 C  C    . TYR   A 1 143 ? -30.691 -25.892 12.744  1.00 34.64  ? 661  TYR   A C    1 
ATOM   1210 O  O    . TYR   A 1 143 ? -30.868 -27.016 12.306  1.00 31.09  ? 661  TYR   A O    1 
ATOM   1211 C  CB   . TYR   A 1 143 ? -28.425 -24.819 12.609  1.00 28.52  ? 661  TYR   A CB   1 
ATOM   1212 C  CG   . TYR   A 1 143 ? -27.494 -23.908 11.821  1.00 32.33  ? 661  TYR   A CG   1 
ATOM   1213 C  CD1  . TYR   A 1 143 ? -27.112 -22.668 12.317  1.00 39.57  ? 661  TYR   A CD1  1 
ATOM   1214 C  CD2  . TYR   A 1 143 ? -27.008 -24.288 10.577  1.00 37.12  ? 661  TYR   A CD2  1 
ATOM   1215 C  CE1  . TYR   A 1 143 ? -26.258 -21.839 11.597  1.00 45.85  ? 661  TYR   A CE1  1 
ATOM   1216 C  CE2  . TYR   A 1 143 ? -26.172 -23.454 9.832   1.00 37.29  ? 661  TYR   A CE2  1 
ATOM   1217 C  CZ   . TYR   A 1 143 ? -25.799 -22.238 10.350  1.00 43.44  ? 661  TYR   A CZ   1 
ATOM   1218 O  OH   . TYR   A 1 143 ? -24.955 -21.416 9.627   1.00 53.75  ? 661  TYR   A OH   1 
ATOM   1219 N  N    . LYS   A 1 144 ? -31.262 -25.462 13.858  1.00 33.33  ? 662  LYS   A N    1 
ATOM   1220 C  CA   . LYS   A 1 144 ? -32.173 -26.319 14.596  1.00 30.09  ? 662  LYS   A CA   1 
ATOM   1221 C  C    . LYS   A 1 144 ? -33.409 -26.752 13.794  1.00 27.62  ? 662  LYS   A C    1 
ATOM   1222 O  O    . LYS   A 1 144 ? -33.857 -27.892 13.924  1.00 32.25  ? 662  LYS   A O    1 
ATOM   1223 C  CB   . LYS   A 1 144 ? -32.623 -25.618 15.861  1.00 38.75  ? 662  LYS   A CB   1 
ATOM   1224 C  CG   . LYS   A 1 144 ? -31.537 -25.490 16.929  1.00 36.51  ? 662  LYS   A CG   1 
ATOM   1225 C  CD   . LYS   A 1 144 ? -32.176 -24.959 18.178  1.00 36.37  ? 662  LYS   A CD   1 
ATOM   1226 C  CE   . LYS   A 1 144 ? -31.264 -24.993 19.377  1.00 47.87  ? 662  LYS   A CE   1 
ATOM   1227 N  NZ   . LYS   A 1 144 ? -32.070 -24.614 20.587  1.00 49.06  ? 662  LYS   A NZ   1 
ATOM   1228 N  N    . MET   A 1 145 ? -33.983 -25.852 12.992  1.00 27.70  ? 663  MET   A N    1 
ATOM   1229 C  CA   . MET   A 1 145 ? -35.150 -26.219 12.179  1.00 28.29  ? 663  MET   A CA   1 
ATOM   1230 C  C    . MET   A 1 145 ? -34.767 -27.312 11.187  1.00 30.08  ? 663  MET   A C    1 
ATOM   1231 O  O    . MET   A 1 145 ? -35.518 -28.270 10.989  1.00 31.19  ? 663  MET   A O    1 
ATOM   1232 C  CB   . MET   A 1 145 ? -35.738 -25.006 11.433  1.00 31.70  ? 663  MET   A CB   1 
ATOM   1233 C  CG   . MET   A 1 145 ? -36.421 -24.010 12.365  1.00 35.78  ? 663  MET   A CG   1 
ATOM   1234 S  SD   . MET   A 1 145 ? -37.295 -22.651 11.586  1.00 40.63  ? 663  MET   A SD   1 
ATOM   1235 C  CE   . MET   A 1 145 ? -38.758 -23.504 10.991  1.00 34.31  ? 663  MET   A CE   1 
ATOM   1236 N  N    . MET   A 1 146 ? -33.590 -27.163 10.579  1.00 30.25  ? 664  MET   A N    1 
ATOM   1237 C  CA   . MET   A 1 146 ? -33.042 -28.179 9.683   1.00 30.37  ? 664  MET   A CA   1 
ATOM   1238 C  C    . MET   A 1 146 ? -33.001 -29.546 10.346  1.00 33.49  ? 664  MET   A C    1 
ATOM   1239 O  O    . MET   A 1 146 ? -33.253 -30.558 9.706   1.00 40.19  ? 664  MET   A O    1 
ATOM   1240 C  CB   . MET   A 1 146 ? -31.637 -27.781 9.237   1.00 32.70  ? 664  MET   A CB   1 
ATOM   1241 C  CG   . MET   A 1 146 ? -31.618 -26.781 8.113   1.00 30.24  ? 664  MET   A CG   1 
ATOM   1242 S  SD   . MET   A 1 146 ? -29.955 -26.525 7.469   1.00 36.34  ? 664  MET   A SD   1 
ATOM   1243 C  CE   . MET   A 1 146 ? -29.232 -25.484 8.667   1.00 48.80  ? 664  MET   A CE   1 
ATOM   1244 N  N    . LEU   A 1 147 ? -32.683 -29.556 11.643  1.00 29.98  ? 665  LEU   A N    1 
ATOM   1245 C  CA   . LEU   A 1 147 ? -32.496 -30.790 12.397  1.00 32.89  ? 665  LEU   A CA   1 
ATOM   1246 C  C    . LEU   A 1 147 ? -33.764 -31.165 13.137  1.00 40.54  ? 665  LEU   A C    1 
ATOM   1247 O  O    . LEU   A 1 147 ? -33.771 -32.124 13.916  1.00 37.82  ? 665  LEU   A O    1 
ATOM   1248 C  CB   . LEU   A 1 147 ? -31.359 -30.646 13.401  1.00 30.89  ? 665  LEU   A CB   1 
ATOM   1249 C  CG   . LEU   A 1 147 ? -29.954 -30.464 12.837  1.00 36.91  ? 665  LEU   A CG   1 
ATOM   1250 C  CD1  . LEU   A 1 147 ? -29.001 -30.161 13.983  1.00 35.33  ? 665  LEU   A CD1  1 
ATOM   1251 C  CD2  . LEU   A 1 147 ? -29.531 -31.730 12.112  1.00 34.69  ? 665  LEU   A CD2  1 
ATOM   1252 N  N    . HIS   A 1 148 ? -34.827 -30.396 12.912  1.00 31.31  ? 666  HIS   A N    1 
ATOM   1253 C  CA   . HIS   A 1 148 ? -36.077 -30.633 13.615  1.00 31.37  ? 666  HIS   A CA   1 
ATOM   1254 C  C    . HIS   A 1 148 ? -35.832 -30.609 15.130  1.00 34.29  ? 666  HIS   A C    1 
ATOM   1255 O  O    . HIS   A 1 148 ? -36.316 -31.465 15.857  1.00 38.29  ? 666  HIS   A O    1 
ATOM   1256 C  CB   . HIS   A 1 148 ? -36.699 -31.980 13.178  1.00 34.16  ? 666  HIS   A CB   1 
ATOM   1257 C  CG   . HIS   A 1 148 ? -38.087 -32.199 13.695  1.00 44.41  ? 666  HIS   A CG   1 
ATOM   1258 N  ND1  . HIS   A 1 148 ? -39.140 -31.366 13.381  1.00 52.26  ? 666  HIS   A ND1  1 
ATOM   1259 C  CD2  . HIS   A 1 148 ? -38.588 -33.145 14.522  1.00 52.62  ? 666  HIS   A CD2  1 
ATOM   1260 C  CE1  . HIS   A 1 148 ? -40.231 -31.792 13.989  1.00 56.36  ? 666  HIS   A CE1  1 
ATOM   1261 N  NE2  . HIS   A 1 148 ? -39.926 -32.872 14.686  1.00 61.77  ? 666  HIS   A NE2  1 
ATOM   1262 N  N    . LYS   A 1 149 ? -35.030 -29.651 15.584  1.00 33.29  ? 667  LYS   A N    1 
ATOM   1263 C  CA   . LYS   A 1 149 ? -34.860 -29.410 17.009  1.00 31.53  ? 667  LYS   A CA   1 
ATOM   1264 C  C    . LYS   A 1 149 ? -35.742 -28.241 17.439  1.00 33.84  ? 667  LYS   A C    1 
ATOM   1265 O  O    . LYS   A 1 149 ? -35.960 -27.309 16.677  1.00 32.99  ? 667  LYS   A O    1 
ATOM   1266 C  CB   . LYS   A 1 149 ? -33.387 -29.133 17.350  1.00 29.76  ? 667  LYS   A CB   1 
ATOM   1267 C  CG   . LYS   A 1 149 ? -32.528 -30.388 17.308  1.00 43.02  ? 667  LYS   A CG   1 
ATOM   1268 C  CD   . LYS   A 1 149 ? -31.138 -30.160 17.835  1.00 51.38  ? 667  LYS   A CD   1 
ATOM   1269 C  CE   . LYS   A 1 149 ? -30.313 -31.445 17.749  1.00 53.80  ? 667  LYS   A CE   1 
ATOM   1270 N  NZ   . LYS   A 1 149 ? -30.922 -32.566 18.514  1.00 59.41  ? 667  LYS   A NZ   1 
ATOM   1271 N  N    . PRO   A 1 150 ? -36.243 -28.295 18.673  1.00 41.80  ? 668  PRO   A N    1 
ATOM   1272 C  CA   . PRO   A 1 150 ? -37.093 -27.246 19.227  1.00 41.80  ? 668  PRO   A CA   1 
ATOM   1273 C  C    . PRO   A 1 150 ? -36.317 -25.949 19.368  1.00 38.23  ? 668  PRO   A C    1 
ATOM   1274 O  O    . PRO   A 1 150 ? -35.181 -25.969 19.840  1.00 38.43  ? 668  PRO   A O    1 
ATOM   1275 C  CB   . PRO   A 1 150 ? -37.474 -27.781 20.620  1.00 35.99  ? 668  PRO   A CB   1 
ATOM   1276 C  CG   . PRO   A 1 150 ? -37.022 -29.198 20.641  1.00 47.58  ? 668  PRO   A CG   1 
ATOM   1277 C  CD   . PRO   A 1 150 ? -35.894 -29.307 19.680  1.00 36.83  ? 668  PRO   A CD   1 
ATOM   1278 N  N    . ILE   A 1 151 ? -36.930 -24.839 18.987  1.00 36.20  ? 669  ILE   A N    1 
ATOM   1279 C  CA   . ILE   A 1 151 ? -36.360 -23.524 19.266  1.00 27.66  ? 669  ILE   A CA   1 
ATOM   1280 C  C    . ILE   A 1 151 ? -36.677 -23.096 20.701  1.00 32.00  ? 669  ILE   A C    1 
ATOM   1281 O  O    . ILE   A 1 151 ? -37.832 -23.114 21.120  1.00 32.08  ? 669  ILE   A O    1 
ATOM   1282 C  CB   . ILE   A 1 151 ? -36.906 -22.459 18.318  1.00 30.31  ? 669  ILE   A CB   1 
ATOM   1283 C  CG1  . ILE   A 1 151 ? -36.876 -22.955 16.861  1.00 40.16  ? 669  ILE   A CG1  1 
ATOM   1284 C  CG2  . ILE   A 1 151 ? -36.174 -21.134 18.534  1.00 29.88  ? 669  ILE   A CG2  1 
ATOM   1285 C  CD1  . ILE   A 1 151 ? -35.546 -23.497 16.421  1.00 39.41  ? 669  ILE   A CD1  1 
ATOM   1286 N  N    . THR   A 1 152 ? -35.667 -22.680 21.444  1.00 38.97  ? 670  THR   A N    1 
ATOM   1287 C  CA   . THR   A 1 152 ? -35.885 -22.357 22.846  1.00 47.79  ? 670  THR   A CA   1 
ATOM   1288 C  C    . THR   A 1 152 ? -35.604 -20.893 23.162  1.00 47.82  ? 670  THR   A C    1 
ATOM   1289 O  O    . THR   A 1 152 ? -35.029 -20.164 22.350  1.00 42.38  ? 670  THR   A O    1 
ATOM   1290 C  CB   . THR   A 1 152 ? -35.005 -23.218 23.758  1.00 41.63  ? 670  THR   A CB   1 
ATOM   1291 O  OG1  . THR   A 1 152 ? -33.624 -22.943 23.480  1.00 41.05  ? 670  THR   A OG1  1 
ATOM   1292 C  CG2  . THR   A 1 152 ? -35.297 -24.704 23.553  1.00 48.34  ? 670  THR   A CG2  1 
ATOM   1293 N  N    . LEU   A 1 153 ? -35.992 -20.494 24.370  1.00 45.26  ? 671  LEU   A N    1 
ATOM   1294 C  CA   . LEU   A 1 153 ? -35.738 -19.157 24.879  1.00 42.91  ? 671  LEU   A CA   1 
ATOM   1295 C  C    . LEU   A 1 153 ? -34.262 -18.814 24.798  1.00 46.64  ? 671  LEU   A C    1 
ATOM   1296 O  O    . LEU   A 1 153 ? -33.894 -17.682 24.490  1.00 44.27  ? 671  LEU   A O    1 
ATOM   1297 C  CB   . LEU   A 1 153 ? -36.223 -19.044 26.326  1.00 40.44  ? 671  LEU   A CB   1 
ATOM   1298 C  CG   . LEU   A 1 153 ? -35.998 -17.681 26.953  1.00 32.82  ? 671  LEU   A CG   1 
ATOM   1299 C  CD1  . LEU   A 1 153 ? -36.634 -16.616 26.062  1.00 33.42  ? 671  LEU   A CD1  1 
ATOM   1300 C  CD2  . LEU   A 1 153 ? -36.583 -17.655 28.363  1.00 40.87  ? 671  LEU   A CD2  1 
ATOM   1301 N  N    . HIS   A 1 154 ? -33.419 -19.806 25.071  1.00 45.61  ? 672  HIS   A N    1 
ATOM   1302 C  CA   . HIS   A 1 154 ? -31.972 -19.615 25.019  1.00 54.15  ? 672  HIS   A CA   1 
ATOM   1303 C  C    . HIS   A 1 154 ? -31.502 -19.189 23.629  1.00 57.69  ? 672  HIS   A C    1 
ATOM   1304 O  O    . HIS   A 1 154 ? -30.556 -18.410 23.495  1.00 63.68  ? 672  HIS   A O    1 
ATOM   1305 C  CB   . HIS   A 1 154 ? -31.255 -20.894 25.441  1.00 63.98  ? 672  HIS   A CB   1 
ATOM   1306 C  CG   . HIS   A 1 154 ? -29.785 -20.715 25.663  1.00 79.11  ? 672  HIS   A CG   1 
ATOM   1307 N  ND1  . HIS   A 1 154 ? -28.888 -21.758 25.583  1.00 83.88  ? 672  HIS   A ND1  1 
ATOM   1308 C  CD2  . HIS   A 1 154 ? -29.059 -19.616 25.976  1.00 85.08  ? 672  HIS   A CD2  1 
ATOM   1309 C  CE1  . HIS   A 1 154 ? -27.671 -21.308 25.833  1.00 87.47  ? 672  HIS   A CE1  1 
ATOM   1310 N  NE2  . HIS   A 1 154 ? -27.747 -20.011 26.073  1.00 89.90  ? 672  HIS   A NE2  1 
ATOM   1311 N  N    . ASP   A 1 155 ? -32.173 -19.689 22.595  1.00 51.00  ? 673  ASP   A N    1 
ATOM   1312 C  CA   . ASP   A 1 155 ? -31.812 -19.344 21.223  1.00 48.51  ? 673  ASP   A CA   1 
ATOM   1313 C  C    . ASP   A 1 155 ? -32.000 -17.865 20.980  1.00 46.55  ? 673  ASP   A C    1 
ATOM   1314 O  O    . ASP   A 1 155 ? -31.303 -17.263 20.166  1.00 48.18  ? 673  ASP   A O    1 
ATOM   1315 C  CB   . ASP   A 1 155 ? -32.639 -20.155 20.228  1.00 43.06  ? 673  ASP   A CB   1 
ATOM   1316 C  CG   . ASP   A 1 155 ? -32.262 -21.610 20.230  1.00 49.76  ? 673  ASP   A CG   1 
ATOM   1317 O  OD1  . ASP   A 1 155 ? -31.044 -21.902 20.272  1.00 58.00  ? 673  ASP   A OD1  1 
ATOM   1318 O  OD2  . ASP   A 1 155 ? -33.176 -22.462 20.228  1.00 44.58  ? 673  ASP   A OD2  1 
ATOM   1319 N  N    . MET   A 1 156 ? -32.941 -17.279 21.708  1.00 49.62  ? 674  MET   A N    1 
ATOM   1320 C  CA   . MET   A 1 156 ? -33.205 -15.848 21.604  1.00 43.48  ? 674  MET   A CA   1 
ATOM   1321 C  C    . MET   A 1 156 ? -32.020 -15.009 22.123  1.00 46.53  ? 674  MET   A C    1 
ATOM   1322 O  O    . MET   A 1 156 ? -31.858 -13.853 21.740  1.00 51.30  ? 674  MET   A O    1 
ATOM   1323 C  CB   . MET   A 1 156 ? -34.490 -15.508 22.370  1.00 41.70  ? 674  MET   A CB   1 
ATOM   1324 C  CG   . MET   A 1 156 ? -34.853 -14.043 22.410  1.00 36.94  ? 674  MET   A CG   1 
ATOM   1325 S  SD   . MET   A 1 156 ? -35.499 -13.512 20.821  1.00 50.15  ? 674  MET   A SD   1 
ATOM   1326 C  CE   . MET   A 1 156 ? -37.150 -14.214 20.884  1.00 46.86  ? 674  MET   A CE   1 
ATOM   1327 N  N    . GLU   A 1 157 ? -31.188 -15.580 22.993  1.00 47.48  ? 675  GLU   A N    1 
ATOM   1328 C  CA   . GLU   A 1 157 ? -30.104 -14.792 23.582  1.00 49.86  ? 675  GLU   A CA   1 
ATOM   1329 C  C    . GLU   A 1 157 ? -29.098 -14.376 22.518  1.00 58.79  ? 675  GLU   A C    1 
ATOM   1330 O  O    . GLU   A 1 157 ? -28.756 -13.200 22.391  1.00 56.27  ? 675  GLU   A O    1 
ATOM   1331 C  CB   . GLU   A 1 157 ? -29.382 -15.553 24.690  1.00 45.12  ? 675  GLU   A CB   1 
ATOM   1332 C  CG   . GLU   A 1 157 ? -28.378 -14.665 25.412  1.00 56.68  ? 675  GLU   A CG   1 
ATOM   1333 C  CD   . GLU   A 1 157 ? -27.678 -15.339 26.582  1.00 62.37  ? 675  GLU   A CD   1 
ATOM   1334 O  OE1  . GLU   A 1 157 ? -27.641 -16.586 26.651  1.00 69.20  ? 675  GLU   A OE1  1 
ATOM   1335 O  OE2  . GLU   A 1 157 ? -27.170 -14.603 27.448  1.00 64.76  ? 675  GLU   A OE2  1 
ATOM   1336 N  N    . SER   A 1 158 ? -28.646 -15.351 21.737  1.00 63.23  ? 676  SER   A N    1 
ATOM   1337 C  CA   . SER   A 1 158 ? -27.646 -15.100 20.711  1.00 65.05  ? 676  SER   A CA   1 
ATOM   1338 C  C    . SER   A 1 158 ? -28.129 -14.103 19.654  1.00 57.24  ? 676  SER   A C    1 
ATOM   1339 O  O    . SER   A 1 158 ? -27.319 -13.515 18.956  1.00 61.83  ? 676  SER   A O    1 
ATOM   1340 C  CB   . SER   A 1 158 ? -27.220 -16.420 20.050  1.00 71.48  ? 676  SER   A CB   1 
ATOM   1341 O  OG   . SER   A 1 158 ? -28.332 -17.179 19.589  1.00 75.03  ? 676  SER   A OG   1 
ATOM   1342 N  N    . VAL   A 1 159 ? -29.439 -13.897 19.549  1.00 51.64  ? 677  VAL   A N    1 
ATOM   1343 C  CA   . VAL   A 1 159 ? -29.982 -13.049 18.485  1.00 54.22  ? 677  VAL   A CA   1 
ATOM   1344 C  C    . VAL   A 1 159 ? -30.492 -11.685 18.951  1.00 47.23  ? 677  VAL   A C    1 
ATOM   1345 O  O    . VAL   A 1 159 ? -30.254 -10.674 18.301  1.00 48.54  ? 677  VAL   A O    1 
ATOM   1346 C  CB   . VAL   A 1 159 ? -31.136 -13.755 17.754  1.00 54.31  ? 677  VAL   A CB   1 
ATOM   1347 C  CG1  . VAL   A 1 159 ? -31.746 -12.832 16.706  1.00 55.81  ? 677  VAL   A CG1  1 
ATOM   1348 C  CG2  . VAL   A 1 159 ? -30.656 -15.061 17.130  1.00 52.75  ? 677  VAL   A CG2  1 
ATOM   1349 N  N    . ASP   A 1 160 ? -31.225 -11.668 20.057  1.00 49.10  ? 678  ASP   A N    1 
ATOM   1350 C  CA   . ASP   A 1 160 ? -31.748 -10.422 20.624  1.00 44.87  ? 678  ASP   A CA   1 
ATOM   1351 C  C    . ASP   A 1 160 ? -31.684 -10.526 22.140  1.00 56.82  ? 678  ASP   A C    1 
ATOM   1352 O  O    . ASP   A 1 160 ? -32.502 -11.209 22.753  1.00 50.30  ? 678  ASP   A O    1 
ATOM   1353 C  CB   . ASP   A 1 160 ? -33.182 -10.169 20.166  1.00 49.29  ? 678  ASP   A CB   1 
ATOM   1354 C  CG   . ASP   A 1 160 ? -33.736 -8.834  20.657  1.00 58.98  ? 678  ASP   A CG   1 
ATOM   1355 O  OD1  . ASP   A 1 160 ? -33.035 -8.106  21.404  1.00 55.25  ? 678  ASP   A OD1  1 
ATOM   1356 O  OD2  . ASP   A 1 160 ? -34.898 -8.528  20.308  1.00 62.93  ? 678  ASP   A OD2  1 
ATOM   1357 N  N    . SER   A 1 161 ? -30.704 -9.846  22.726  1.00 63.86  ? 679  SER   A N    1 
ATOM   1358 C  CA   . SER   A 1 161 ? -30.427 -9.914  24.155  1.00 67.03  ? 679  SER   A CA   1 
ATOM   1359 C  C    . SER   A 1 161 ? -31.455 -9.171  25.008  1.00 63.93  ? 679  SER   A C    1 
ATOM   1360 O  O    . SER   A 1 161 ? -31.778 -9.611  26.113  1.00 50.34  ? 679  SER   A O    1 
ATOM   1361 C  CB   . SER   A 1 161 ? -29.032 -9.355  24.437  1.00 70.40  ? 679  SER   A CB   1 
ATOM   1362 O  OG   . SER   A 1 161 ? -28.953 -8.002  24.031  1.00 77.60  ? 679  SER   A OG   1 
ATOM   1363 N  N    . GLU   A 1 162 ? -31.945 -8.038  24.509  1.00 74.68  ? 680  GLU   A N    1 
ATOM   1364 C  CA   . GLU   A 1 162 ? -32.980 -7.282  25.213  1.00 80.02  ? 680  GLU   A CA   1 
ATOM   1365 C  C    . GLU   A 1 162 ? -34.248 -8.104  25.368  1.00 72.02  ? 680  GLU   A C    1 
ATOM   1366 O  O    . GLU   A 1 162 ? -34.810 -8.205  26.459  1.00 71.36  ? 680  GLU   A O    1 
ATOM   1367 C  CB   . GLU   A 1 162 ? -33.308 -5.980  24.484  1.00 86.03  ? 680  GLU   A CB   1 
ATOM   1368 C  CG   . GLU   A 1 162 ? -32.443 -4.803  24.878  1.00 92.03  ? 680  GLU   A CG   1 
ATOM   1369 C  CD   . GLU   A 1 162 ? -32.989 -3.481  24.356  1.00 93.65  ? 680  GLU   A CD   1 
ATOM   1370 O  OE1  . GLU   A 1 162 ? -33.848 -3.495  23.446  1.00 91.76  ? 680  GLU   A OE1  1 
ATOM   1371 O  OE2  . GLU   A 1 162 ? -32.569 -2.426  24.869  1.00 97.79  ? 680  GLU   A OE2  1 
ATOM   1372 N  N    . TYR   A 1 163 ? -34.689 -8.683  24.259  1.00 63.96  ? 681  TYR   A N    1 
ATOM   1373 C  CA   . TYR   A 1 163 ? -35.862 -9.537  24.243  1.00 54.88  ? 681  TYR   A CA   1 
ATOM   1374 C  C    . TYR   A 1 163 ? -35.660 -10.749 25.139  1.00 56.48  ? 681  TYR   A C    1 
ATOM   1375 O  O    . TYR   A 1 163 ? -36.527 -11.085 25.946  1.00 54.64  ? 681  TYR   A O    1 
ATOM   1376 C  CB   . TYR   A 1 163 ? -36.156 -10.002 22.829  1.00 53.04  ? 681  TYR   A CB   1 
ATOM   1377 C  CG   . TYR   A 1 163 ? -37.624 -10.138 22.498  1.00 51.16  ? 681  TYR   A CG   1 
ATOM   1378 C  CD1  . TYR   A 1 163 ? -38.605 -9.896  23.453  1.00 53.46  ? 681  TYR   A CD1  1 
ATOM   1379 C  CD2  . TYR   A 1 163 ? -38.024 -10.505 21.222  1.00 53.14  ? 681  TYR   A CD2  1 
ATOM   1380 C  CE1  . TYR   A 1 163 ? -39.946 -10.014 23.143  1.00 55.25  ? 681  TYR   A CE1  1 
ATOM   1381 C  CE2  . TYR   A 1 163 ? -39.362 -10.624 20.899  1.00 60.72  ? 681  TYR   A CE2  1 
ATOM   1382 C  CZ   . TYR   A 1 163 ? -40.317 -10.377 21.863  1.00 61.19  ? 681  TYR   A CZ   1 
ATOM   1383 O  OH   . TYR   A 1 163 ? -41.644 -10.500 21.529  1.00 68.79  ? 681  TYR   A OH   1 
ATOM   1384 N  N    . TYR   A 1 164 ? -34.513 -11.408 24.979  1.00 44.37  ? 682  TYR   A N    1 
ATOM   1385 C  CA   . TYR   A 1 164 ? -34.189 -12.571 25.786  1.00 41.00  ? 682  TYR   A CA   1 
ATOM   1386 C  C    . TYR   A 1 164 ? -34.331 -12.262 27.268  1.00 45.25  ? 682  TYR   A C    1 
ATOM   1387 O  O    . TYR   A 1 164 ? -34.916 -13.050 28.016  1.00 39.06  ? 682  TYR   A O    1 
ATOM   1388 C  CB   . TYR   A 1 164 ? -32.772 -13.046 25.499  1.00 44.83  ? 682  TYR   A CB   1 
ATOM   1389 C  CG   . TYR   A 1 164 ? -32.253 -14.071 26.491  1.00 40.22  ? 682  TYR   A CG   1 
ATOM   1390 C  CD1  . TYR   A 1 164 ? -32.675 -15.391 26.436  1.00 32.05  ? 682  TYR   A CD1  1 
ATOM   1391 C  CD2  . TYR   A 1 164 ? -31.341 -13.714 27.480  1.00 47.13  ? 682  TYR   A CD2  1 
ATOM   1392 C  CE1  . TYR   A 1 164 ? -32.205 -16.335 27.330  1.00 36.74  ? 682  TYR   A CE1  1 
ATOM   1393 C  CE2  . TYR   A 1 164 ? -30.866 -14.649 28.389  1.00 50.47  ? 682  TYR   A CE2  1 
ATOM   1394 C  CZ   . TYR   A 1 164 ? -31.303 -15.961 28.302  1.00 42.55  ? 682  TYR   A CZ   1 
ATOM   1395 O  OH   . TYR   A 1 164 ? -30.837 -16.896 29.189  1.00 52.20  ? 682  TYR   A OH   1 
ATOM   1396 N  N    . ASN   A 1 165 ? -33.797 -11.112 27.685  1.00 39.85  ? 683  ASN   A N    1 
ATOM   1397 C  CA   . ASN   A 1 165 ? -33.781 -10.745 29.102  1.00 41.78  ? 683  ASN   A CA   1 
ATOM   1398 C  C    . ASN   A 1 165 ? -35.177 -10.484 29.638  1.00 37.58  ? 683  ASN   A C    1 
ATOM   1399 O  O    . ASN   A 1 165 ? -35.452 -10.707 30.817  1.00 48.26  ? 683  ASN   A O    1 
ATOM   1400 C  CB   . ASN   A 1 165 ? -32.905 -9.508  29.338  1.00 51.63  ? 683  ASN   A CB   1 
ATOM   1401 C  CG   . ASN   A 1 165 ? -31.423 -9.818  29.268  1.00 60.40  ? 683  ASN   A CG   1 
ATOM   1402 O  OD1  . ASN   A 1 165 ? -31.006 -10.956 29.493  1.00 64.73  ? 683  ASN   A OD1  1 
ATOM   1403 N  ND2  . ASN   A 1 165 ? -30.615 -8.803  28.964  1.00 55.27  ? 683  ASN   A ND2  1 
ATOM   1404 N  N    . SER   A 1 166 ? -36.051 -9.988  28.774  1.00 43.21  ? 684  SER   A N    1 
ATOM   1405 C  CA   . SER   A 1 166 ? -37.436 -9.710  29.152  1.00 48.03  ? 684  SER   A CA   1 
ATOM   1406 C  C    . SER   A 1 166 ? -38.250 -10.986 29.340  1.00 37.93  ? 684  SER   A C    1 
ATOM   1407 O  O    . SER   A 1 166 ? -38.974 -11.117 30.323  1.00 38.96  ? 684  SER   A O    1 
ATOM   1408 C  CB   . SER   A 1 166 ? -38.113 -8.833  28.099  1.00 50.76  ? 684  SER   A CB   1 
ATOM   1409 O  OG   . SER   A 1 166 ? -37.473 -7.583  28.015  1.00 57.23  ? 684  SER   A OG   1 
ATOM   1410 N  N    . LEU   A 1 167 ? -38.149 -11.909 28.382  1.00 33.70  ? 685  LEU   A N    1 
ATOM   1411 C  CA   . LEU   A 1 167 ? -38.811 -13.204 28.498  1.00 31.10  ? 685  LEU   A CA   1 
ATOM   1412 C  C    . LEU   A 1 167 ? -38.259 -14.012 29.657  1.00 35.76  ? 685  LEU   A C    1 
ATOM   1413 O  O    . LEU   A 1 167 ? -38.983 -14.769 30.296  1.00 42.48  ? 685  LEU   A O    1 
ATOM   1414 C  CB   . LEU   A 1 167 ? -38.671 -14.007 27.213  1.00 28.83  ? 685  LEU   A CB   1 
ATOM   1415 C  CG   . LEU   A 1 167 ? -39.295 -13.272 26.015  1.00 46.76  ? 685  LEU   A CG   1 
ATOM   1416 C  CD1  . LEU   A 1 167 ? -39.024 -14.046 24.736  1.00 35.59  ? 685  LEU   A CD1  1 
ATOM   1417 C  CD2  . LEU   A 1 167 ? -40.795 -13.043 26.231  1.00 44.66  ? 685  LEU   A CD2  1 
ATOM   1418 N  N    . ARG   A 1 168 ? -36.975 -13.857 29.928  1.00 32.92  ? 686  ARG   A N    1 
ATOM   1419 C  CA   . ARG   A 1 168 ? -36.380 -14.570 31.051  1.00 42.38  ? 686  ARG   A CA   1 
ATOM   1420 C  C    . ARG   A 1 168 ? -36.905 -14.013 32.367  1.00 43.59  ? 686  ARG   A C    1 
ATOM   1421 O  O    . ARG   A 1 168 ? -37.196 -14.780 33.285  1.00 37.94  ? 686  ARG   A O    1 
ATOM   1422 C  CB   . ARG   A 1 168 ? -34.854 -14.504 31.009  1.00 47.84  ? 686  ARG   A CB   1 
ATOM   1423 C  CG   . ARG   A 1 168 ? -34.188 -15.459 31.983  1.00 65.55  ? 686  ARG   A CG   1 
ATOM   1424 C  CD   . ARG   A 1 168 ? -32.678 -15.411 31.848  1.00 75.77  ? 686  ARG   A CD   1 
ATOM   1425 N  NE   . ARG   A 1 168 ? -32.200 -14.037 31.958  1.00 83.50  ? 686  ARG   A NE   1 
ATOM   1426 C  CZ   . ARG   A 1 168 ? -30.925 -13.672 31.908  1.00 84.65  ? 686  ARG   A CZ   1 
ATOM   1427 N  NH1  . ARG   A 1 168 ? -29.970 -14.586 31.758  1.00 86.56  ? 686  ARG   A NH1  1 
ATOM   1428 N  NH2  . ARG   A 1 168 ? -30.608 -12.386 32.015  1.00 81.75  ? 686  ARG   A NH2  1 
ATOM   1429 N  N    . TRP   A 1 169 ? -37.028 -12.686 32.466  1.00 36.39  ? 687  TRP   A N    1 
ATOM   1430 C  CA   . TRP   A 1 169 ? -37.652 -12.099 33.655  1.00 41.15  ? 687  TRP   A CA   1 
ATOM   1431 C  C    . TRP   A 1 169 ? -39.053 -12.669 33.852  1.00 36.75  ? 687  TRP   A C    1 
ATOM   1432 O  O    . TRP   A 1 169 ? -39.453 -13.003 34.962  1.00 51.62  ? 687  TRP   A O    1 
ATOM   1433 C  CB   . TRP   A 1 169 ? -37.741 -10.573 33.561  1.00 37.82  ? 687  TRP   A CB   1 
ATOM   1434 C  CG   . TRP   A 1 169 ? -38.270 -9.950  34.833  1.00 44.81  ? 687  TRP   A CG   1 
ATOM   1435 C  CD1  . TRP   A 1 169 ? -37.530 -9.431  35.867  1.00 46.89  ? 687  TRP   A CD1  1 
ATOM   1436 C  CD2  . TRP   A 1 169 ? -39.644 -9.792  35.209  1.00 38.81  ? 687  TRP   A CD2  1 
ATOM   1437 N  NE1  . TRP   A 1 169 ? -38.360 -8.960  36.851  1.00 45.36  ? 687  TRP   A NE1  1 
ATOM   1438 C  CE2  . TRP   A 1 169 ? -39.662 -9.174  36.474  1.00 45.59  ? 687  TRP   A CE2  1 
ATOM   1439 C  CE3  . TRP   A 1 169 ? -40.862 -10.114 34.594  1.00 39.58  ? 687  TRP   A CE3  1 
ATOM   1440 C  CZ2  . TRP   A 1 169 ? -40.852 -8.874  37.146  1.00 47.99  ? 687  TRP   A CZ2  1 
ATOM   1441 C  CZ3  . TRP   A 1 169 ? -42.038 -9.820  35.256  1.00 37.28  ? 687  TRP   A CZ3  1 
ATOM   1442 C  CH2  . TRP   A 1 169 ? -42.024 -9.194  36.520  1.00 39.25  ? 687  TRP   A CH2  1 
ATOM   1443 N  N    . ILE   A 1 170 ? -39.800 -12.754 32.760  1.00 36.42  ? 688  ILE   A N    1 
ATOM   1444 C  CA   . ILE   A 1 170 ? -41.148 -13.303 32.802  1.00 37.22  ? 688  ILE   A CA   1 
ATOM   1445 C  C    . ILE   A 1 170 ? -41.136 -14.744 33.327  1.00 41.37  ? 688  ILE   A C    1 
ATOM   1446 O  O    . ILE   A 1 170 ? -41.982 -15.133 34.140  1.00 35.54  ? 688  ILE   A O    1 
ATOM   1447 C  CB   . ILE   A 1 170 ? -41.794 -13.256 31.418  1.00 35.60  ? 688  ILE   A CB   1 
ATOM   1448 C  CG1  . ILE   A 1 170 ? -42.110 -11.802 31.040  1.00 31.80  ? 688  ILE   A CG1  1 
ATOM   1449 C  CG2  . ILE   A 1 170 ? -43.041 -14.133 31.377  1.00 35.80  ? 688  ILE   A CG2  1 
ATOM   1450 C  CD1  . ILE   A 1 170 ? -42.626 -11.639 29.649  1.00 35.58  ? 688  ILE   A CD1  1 
ATOM   1451 N  N    . LEU   A 1 171 ? -40.153 -15.518 32.889  1.00 34.73  ? 689  LEU   A N    1 
ATOM   1452 C  CA   . LEU   A 1 171 ? -40.074 -16.918 33.287  1.00 45.99  ? 689  LEU   A CA   1 
ATOM   1453 C  C    . LEU   A 1 171 ? -39.786 -17.057 34.779  1.00 47.10  ? 689  LEU   A C    1 
ATOM   1454 O  O    . LEU   A 1 171 ? -40.284 -17.976 35.419  1.00 51.54  ? 689  LEU   A O    1 
ATOM   1455 C  CB   . LEU   A 1 171 ? -39.002 -17.650 32.474  1.00 40.06  ? 689  LEU   A CB   1 
ATOM   1456 C  CG   . LEU   A 1 171 ? -38.751 -19.138 32.764  1.00 50.84  ? 689  LEU   A CG   1 
ATOM   1457 C  CD1  . LEU   A 1 171 ? -39.973 -19.955 32.423  1.00 55.71  ? 689  LEU   A CD1  1 
ATOM   1458 C  CD2  . LEU   A 1 171 ? -37.545 -19.672 31.988  1.00 45.52  ? 689  LEU   A CD2  1 
ATOM   1459 N  N    . GLU   A 1 172 ? -39.005 -16.136 35.335  1.00 39.16  ? 690  GLU   A N    1 
ATOM   1460 C  CA   . GLU   A 1 172 ? -38.486 -16.323 36.681  1.00 42.57  ? 690  GLU   A CA   1 
ATOM   1461 C  C    . GLU   A 1 172 ? -39.300 -15.608 37.744  1.00 47.51  ? 690  GLU   A C    1 
ATOM   1462 O  O    . GLU   A 1 172 ? -39.154 -15.891 38.937  1.00 57.10  ? 690  GLU   A O    1 
ATOM   1463 C  CB   . GLU   A 1 172 ? -37.031 -15.866 36.731  1.00 48.39  ? 690  GLU   A CB   1 
ATOM   1464 C  CG   . GLU   A 1 172 ? -36.157 -16.592 35.731  1.00 55.56  ? 690  GLU   A CG   1 
ATOM   1465 C  CD   . GLU   A 1 172 ? -34.704 -16.139 35.751  1.00 61.63  ? 690  GLU   A CD   1 
ATOM   1466 O  OE1  . GLU   A 1 172 ? -34.392 -15.150 36.438  1.00 63.77  ? 690  GLU   A OE1  1 
ATOM   1467 O  OE2  . GLU   A 1 172 ? -33.871 -16.780 35.074  1.00 64.45  ? 690  GLU   A OE2  1 
ATOM   1468 N  N    . ASN   A 1 173 ? -40.159 -14.683 37.322  1.00 45.57  ? 691  ASN   A N    1 
ATOM   1469 C  CA   . ASN   A 1 173 ? -40.970 -13.900 38.271  1.00 42.27  ? 691  ASN   A CA   1 
ATOM   1470 C  C    . ASN   A 1 173 ? -42.440 -14.055 37.905  1.00 46.23  ? 691  ASN   A C    1 
ATOM   1471 O  O    . ASN   A 1 173 ? -42.749 -14.410 36.768  1.00 45.60  ? 691  ASN   A O    1 
ATOM   1472 C  CB   . ASN   A 1 173 ? -40.590 -12.405 38.254  1.00 45.17  ? 691  ASN   A CB   1 
ATOM   1473 C  CG   . ASN   A 1 173 ? -39.090 -12.159 38.405  1.00 47.41  ? 691  ASN   A CG   1 
ATOM   1474 O  OD1  . ASN   A 1 173 ? -38.350 -12.096 37.416  1.00 47.32  ? 691  ASN   A OD1  1 
ATOM   1475 N  ND2  . ASN   A 1 173 ? -38.644 -11.988 39.638  1.00 46.37  ? 691  ASN   A ND2  1 
ATOM   1476 N  N    . ASP   A 1 174 ? -43.347 -13.783 38.842  1.00 43.25  ? 692  ASP   A N    1 
ATOM   1477 C  CA   . ASP   A 1 174 ? -44.776 -13.796 38.532  1.00 40.73  ? 692  ASP   A CA   1 
ATOM   1478 C  C    . ASP   A 1 174 ? -45.098 -12.541 37.727  1.00 51.58  ? 692  ASP   A C    1 
ATOM   1479 O  O    . ASP   A 1 174 ? -45.007 -11.434 38.239  1.00 47.09  ? 692  ASP   A O    1 
ATOM   1480 C  CB   . ASP   A 1 174 ? -45.627 -13.850 39.806  1.00 42.51  ? 692  ASP   A CB   1 
ATOM   1481 C  CG   . ASP   A 1 174 ? -47.111 -14.116 39.524  1.00 48.45  ? 692  ASP   A CG   1 
ATOM   1482 O  OD1  . ASP   A 1 174 ? -47.569 -13.954 38.366  1.00 47.66  ? 692  ASP   A OD1  1 
ATOM   1483 O  OD2  . ASP   A 1 174 ? -47.831 -14.489 40.474  1.00 52.74  ? 692  ASP   A OD2  1 
ATOM   1484 N  N    . PRO   A 1 175 ? -45.497 -12.711 36.467  1.00 37.27  ? 693  PRO   A N    1 
ATOM   1485 C  CA   . PRO   A 1 175 ? -45.697 -11.537 35.610  1.00 40.00  ? 693  PRO   A CA   1 
ATOM   1486 C  C    . PRO   A 1 175 ? -47.096 -10.950 35.672  1.00 40.40  ? 693  PRO   A C    1 
ATOM   1487 O  O    . PRO   A 1 175 ? -47.378 -9.973  34.971  1.00 40.86  ? 693  PRO   A O    1 
ATOM   1488 C  CB   . PRO   A 1 175 ? -45.432 -12.088 34.207  1.00 34.32  ? 693  PRO   A CB   1 
ATOM   1489 C  CG   . PRO   A 1 175 ? -45.739 -13.582 34.299  1.00 34.45  ? 693  PRO   A CG   1 
ATOM   1490 C  CD   . PRO   A 1 175 ? -45.824 -13.966 35.774  1.00 36.42  ? 693  PRO   A CD   1 
ATOM   1491 N  N    . THR   A 1 176 ? -47.956 -11.552 36.477  1.00 36.77  ? 694  THR   A N    1 
ATOM   1492 C  CA   . THR   A 1 176 ? -49.387 -11.248 36.468  1.00 43.08  ? 694  THR   A CA   1 
ATOM   1493 C  C    . THR   A 1 176 ? -49.744 -9.750  36.570  1.00 41.45  ? 694  THR   A C    1 
ATOM   1494 O  O    . THR   A 1 176 ? -50.604 -9.253  35.828  1.00 40.99  ? 694  THR   A O    1 
ATOM   1495 C  CB   . THR   A 1 176 ? -50.084 -12.006 37.616  1.00 44.57  ? 694  THR   A CB   1 
ATOM   1496 O  OG1  . THR   A 1 176 ? -49.842 -13.416 37.473  1.00 42.76  ? 694  THR   A OG1  1 
ATOM   1497 C  CG2  . THR   A 1 176 ? -51.581 -11.726 37.611  1.00 40.73  ? 694  THR   A CG2  1 
ATOM   1498 N  N    . GLU   A 1 177 ? -49.071 -9.033  37.468  1.00 37.99  ? 695  GLU   A N    1 
ATOM   1499 C  CA   . GLU   A 1 177 ? -49.401 -7.640  37.739  1.00 38.50  ? 695  GLU   A CA   1 
ATOM   1500 C  C    . GLU   A 1 177 ? -48.972 -6.676  36.631  1.00 38.54  ? 695  GLU   A C    1 
ATOM   1501 O  O    . GLU   A 1 177 ? -49.420 -5.526  36.595  1.00 41.42  ? 695  GLU   A O    1 
ATOM   1502 C  CB   . GLU   A 1 177 ? -48.766 -7.203  39.058  1.00 40.36  ? 695  GLU   A CB   1 
ATOM   1503 C  CG   . GLU   A 1 177 ? -49.239 -8.000  40.249  1.00 49.85  ? 695  GLU   A CG   1 
ATOM   1504 C  CD   . GLU   A 1 177 ? -48.719 -7.446  41.550  1.00 55.92  ? 695  GLU   A CD   1 
ATOM   1505 O  OE1  . GLU   A 1 177 ? -49.551 -6.931  42.326  1.00 55.40  ? 695  GLU   A OE1  1 
ATOM   1506 O  OE2  . GLU   A 1 177 ? -47.490 -7.525  41.792  1.00 58.50  ? 695  GLU   A OE2  1 
ATOM   1507 N  N    . LEU   A 1 178 ? -48.085 -7.127  35.752  1.00 36.48  ? 696  LEU   A N    1 
ATOM   1508 C  CA   . LEU   A 1 178 ? -47.681 -6.314  34.606  1.00 35.63  ? 696  LEU   A CA   1 
ATOM   1509 C  C    . LEU   A 1 178 ? -48.820 -6.239  33.624  1.00 37.34  ? 696  LEU   A C    1 
ATOM   1510 O  O    . LEU   A 1 178 ? -48.837 -5.368  32.752  1.00 42.97  ? 696  LEU   A O    1 
ATOM   1511 C  CB   . LEU   A 1 178 ? -46.438 -6.878  33.916  1.00 36.48  ? 696  LEU   A CB   1 
ATOM   1512 C  CG   . LEU   A 1 178 ? -45.062 -6.407  34.393  1.00 53.40  ? 696  LEU   A CG   1 
ATOM   1513 C  CD1  . LEU   A 1 178 ? -44.925 -6.541  35.889  1.00 60.34  ? 696  LEU   A CD1  1 
ATOM   1514 C  CD2  . LEU   A 1 178 ? -44.010 -7.264  33.699  1.00 51.49  ? 696  LEU   A CD2  1 
ATOM   1515 N  N    . ASP   A 1 179 ? -49.755 -7.179  33.750  1.00 37.92  ? 697  ASP   A N    1 
ATOM   1516 C  CA   . ASP   A 1 179 ? -50.946 -7.167  32.917  1.00 36.86  ? 697  ASP   A CA   1 
ATOM   1517 C  C    . ASP   A 1 179 ? -50.559 -7.284  31.435  1.00 36.62  ? 697  ASP   A C    1 
ATOM   1518 O  O    . ASP   A 1 179 ? -51.109 -6.597  30.571  1.00 35.69  ? 697  ASP   A O    1 
ATOM   1519 C  CB   . ASP   A 1 179 ? -51.747 -5.885  33.189  1.00 48.80  ? 697  ASP   A CB   1 
ATOM   1520 C  CG   . ASP   A 1 179 ? -53.154 -5.952  32.672  1.00 52.83  ? 697  ASP   A CG   1 
ATOM   1521 O  OD1  . ASP   A 1 179 ? -53.614 -7.071  32.354  1.00 50.18  ? 697  ASP   A OD1  1 
ATOM   1522 O  OD2  . ASP   A 1 179 ? -53.803 -4.885  32.607  1.00 57.40  ? 697  ASP   A OD2  1 
ATOM   1523 N  N    . LEU   A 1 180 ? -49.576 -8.135  31.153  1.00 34.99  ? 698  LEU   A N    1 
ATOM   1524 C  CA   . LEU   A 1 180 ? -49.238 -8.463  29.774  1.00 39.17  ? 698  LEU   A CA   1 
ATOM   1525 C  C    . LEU   A 1 180 ? -50.352 -9.291  29.152  1.00 32.74  ? 698  LEU   A C    1 
ATOM   1526 O  O    . LEU   A 1 180 ? -51.013 -10.052 29.843  1.00 33.20  ? 698  LEU   A O    1 
ATOM   1527 C  CB   . LEU   A 1 180 ? -47.928 -9.237  29.704  1.00 30.18  ? 698  LEU   A CB   1 
ATOM   1528 C  CG   . LEU   A 1 180 ? -46.780 -8.583  30.447  1.00 33.62  ? 698  LEU   A CG   1 
ATOM   1529 C  CD1  . LEU   A 1 180 ? -45.541 -9.456  30.336  1.00 30.72  ? 698  LEU   A CD1  1 
ATOM   1530 C  CD2  . LEU   A 1 180 ? -46.551 -7.198  29.868  1.00 34.17  ? 698  LEU   A CD2  1 
ATOM   1531 N  N    . ARG   A 1 181 ? -50.530 -9.156  27.842  1.00 30.08  ? 699  ARG   A N    1 
ATOM   1532 C  CA   . ARG   A 1 181 ? -51.543 -9.907  27.109  1.00 29.66  ? 699  ARG   A CA   1 
ATOM   1533 C  C    . ARG   A 1 181 ? -50.881 -10.838 26.097  1.00 33.11  ? 699  ARG   A C    1 
ATOM   1534 O  O    . ARG   A 1 181 ? -49.698 -10.671 25.786  1.00 27.72  ? 699  ARG   A O    1 
ATOM   1535 C  CB   . ARG   A 1 181 ? -52.515 -8.955  26.385  1.00 29.75  ? 699  ARG   A CB   1 
ATOM   1536 C  CG   . ARG   A 1 181 ? -53.134 -7.877  27.273  1.00 30.81  ? 699  ARG   A CG   1 
ATOM   1537 C  CD   . ARG   A 1 181 ? -54.010 -8.486  28.374  1.00 31.57  ? 699  ARG   A CD   1 
ATOM   1538 N  NE   . ARG   A 1 181 ? -54.410 -7.468  29.365  1.00 32.58  ? 699  ARG   A NE   1 
ATOM   1539 C  CZ   . ARG   A 1 181 ? -55.554 -6.791  29.315  1.00 43.68  ? 699  ARG   A CZ   1 
ATOM   1540 N  NH1  . ARG   A 1 181 ? -56.408 -7.012  28.322  1.00 43.01  ? 699  ARG   A NH1  1 
ATOM   1541 N  NH2  . ARG   A 1 181 ? -55.843 -5.883  30.245  1.00 40.10  ? 699  ARG   A NH2  1 
ATOM   1542 N  N    . PHE   A 1 182 ? -51.632 -11.802 25.561  1.00 29.01  ? 700  PHE   A N    1 
ATOM   1543 C  CA   . PHE   A 1 182 ? -51.065 -12.696 24.548  1.00 28.57  ? 700  PHE   A CA   1 
ATOM   1544 C  C    . PHE   A 1 182 ? -51.026 -11.980 23.187  1.00 33.06  ? 700  PHE   A C    1 
ATOM   1545 O  O    . PHE   A 1 182 ? -51.724 -12.336 22.234  1.00 31.47  ? 700  PHE   A O    1 
ATOM   1546 C  CB   . PHE   A 1 182 ? -51.853 -14.018 24.476  1.00 27.77  ? 700  PHE   A CB   1 
ATOM   1547 C  CG   . PHE   A 1 182 ? -51.427 -15.032 25.520  1.00 28.04  ? 700  PHE   A CG   1 
ATOM   1548 C  CD1  . PHE   A 1 182 ? -51.454 -14.710 26.869  1.00 28.78  ? 700  PHE   A CD1  1 
ATOM   1549 C  CD2  . PHE   A 1 182 ? -50.976 -16.299 25.150  1.00 27.76  ? 700  PHE   A CD2  1 
ATOM   1550 C  CE1  . PHE   A 1 182 ? -51.056 -15.643 27.845  1.00 32.41  ? 700  PHE   A CE1  1 
ATOM   1551 C  CE2  . PHE   A 1 182 ? -50.582 -17.232 26.120  1.00 28.33  ? 700  PHE   A CE2  1 
ATOM   1552 C  CZ   . PHE   A 1 182 ? -50.632 -16.896 27.470  1.00 29.19  ? 700  PHE   A CZ   1 
ATOM   1553 N  N    . ILE   A 1 183 ? -50.193 -10.958 23.120  1.00 26.84  ? 701  ILE   A N    1 
ATOM   1554 C  CA   . ILE   A 1 183 ? -50.004 -10.192 21.898  1.00 34.04  ? 701  ILE   A CA   1 
ATOM   1555 C  C    . ILE   A 1 183 ? -48.526 -9.950  21.741  1.00 35.22  ? 701  ILE   A C    1 
ATOM   1556 O  O    . ILE   A 1 183 ? -47.781 -10.109 22.692  1.00 33.48  ? 701  ILE   A O    1 
ATOM   1557 C  CB   . ILE   A 1 183 ? -50.721 -8.835  21.928  1.00 30.19  ? 701  ILE   A CB   1 
ATOM   1558 C  CG1  . ILE   A 1 183 ? -50.196 -7.994  23.096  1.00 28.12  ? 701  ILE   A CG1  1 
ATOM   1559 C  CG2  . ILE   A 1 183 ? -52.222 -9.008  22.063  1.00 33.83  ? 701  ILE   A CG2  1 
ATOM   1560 C  CD1  . ILE   A 1 183 ? -50.842 -6.618  23.187  1.00 52.17  ? 701  ILE   A CD1  1 
ATOM   1561 N  N    . ILE   A 1 184 ? -48.097 -9.571  20.544  1.00 30.59  ? 702  ILE   A N    1 
ATOM   1562 C  CA   . ILE   A 1 184 ? -46.724 -9.123  20.354  1.00 31.22  ? 702  ILE   A CA   1 
ATOM   1563 C  C    . ILE   A 1 184 ? -46.746 -7.773  19.642  1.00 36.30  ? 702  ILE   A C    1 
ATOM   1564 O  O    . ILE   A 1 184 ? -47.450 -7.608  18.640  1.00 30.63  ? 702  ILE   A O    1 
ATOM   1565 C  CB   . ILE   A 1 184 ? -45.890 -10.132 19.545  1.00 41.62  ? 702  ILE   A CB   1 
ATOM   1566 C  CG1  . ILE   A 1 184 ? -45.280 -11.166 20.480  1.00 57.43  ? 702  ILE   A CG1  1 
ATOM   1567 C  CG2  . ILE   A 1 184 ? -44.763 -9.434  18.812  1.00 55.90  ? 702  ILE   A CG2  1 
ATOM   1568 C  CD1  . ILE   A 1 184 ? -44.226 -12.026 19.812  1.00 66.32  ? 702  ILE   A CD1  1 
ATOM   1569 N  N    . ASP   A 1 185 ? -45.998 -6.812  20.171  1.00 34.09  ? 703  ASP   A N    1 
ATOM   1570 C  CA   . ASP   A 1 185 ? -45.884 -5.498  19.531  1.00 46.20  ? 703  ASP   A CA   1 
ATOM   1571 C  C    . ASP   A 1 185 ? -44.543 -5.413  18.832  1.00 52.87  ? 703  ASP   A C    1 
ATOM   1572 O  O    . ASP   A 1 185 ? -43.502 -5.544  19.468  1.00 61.02  ? 703  ASP   A O    1 
ATOM   1573 C  CB   . ASP   A 1 185 ? -46.025 -4.342  20.540  1.00 48.05  ? 703  ASP   A CB   1 
ATOM   1574 C  CG   . ASP   A 1 185 ? -47.467 -4.123  21.014  1.00 62.07  ? 703  ASP   A CG   1 
ATOM   1575 O  OD1  . ASP   A 1 185 ? -47.660 -3.843  22.216  1.00 77.55  ? 703  ASP   A OD1  1 
ATOM   1576 O  OD2  . ASP   A 1 185 ? -48.412 -4.213  20.200  1.00 63.37  ? 703  ASP   A OD2  1 
ATOM   1577 N  N    . GLU   A 1 186 ? -44.574 -5.202  17.521  1.00 52.25  ? 704  GLU   A N    1 
ATOM   1578 C  CA   . GLU   A 1 186 ? -43.363 -5.007  16.731  1.00 51.34  ? 704  GLU   A CA   1 
ATOM   1579 C  C    . GLU   A 1 186 ? -43.276 -3.576  16.181  1.00 48.21  ? 704  GLU   A C    1 
ATOM   1580 O  O    . GLU   A 1 186 ? -44.245 -3.046  15.642  1.00 47.46  ? 704  GLU   A O    1 
ATOM   1581 C  CB   . GLU   A 1 186 ? -43.319 -6.013  15.586  1.00 51.18  ? 704  GLU   A CB   1 
ATOM   1582 C  CG   . GLU   A 1 186 ? -42.071 -5.926  14.749  1.00 59.01  ? 704  GLU   A CG   1 
ATOM   1583 C  CD   . GLU   A 1 186 ? -42.119 -6.853  13.548  1.00 61.33  ? 704  GLU   A CD   1 
ATOM   1584 O  OE1  . GLU   A 1 186 ? -43.245 -7.223  13.136  1.00 56.72  ? 704  GLU   A OE1  1 
ATOM   1585 O  OE2  . GLU   A 1 186 ? -41.034 -7.205  13.025  1.00 60.09  ? 704  GLU   A OE2  1 
ATOM   1586 N  N    . GLU   A 1 187 ? -42.115 -2.947  16.332  1.00 53.65  ? 705  GLU   A N    1 
ATOM   1587 C  CA   . GLU   A 1 187 ? -41.901 -1.605  15.805  1.00 51.64  ? 705  GLU   A CA   1 
ATOM   1588 C  C    . GLU   A 1 187 ? -41.460 -1.689  14.352  1.00 49.23  ? 705  GLU   A C    1 
ATOM   1589 O  O    . GLU   A 1 187 ? -40.440 -2.304  14.059  1.00 45.54  ? 705  GLU   A O    1 
ATOM   1590 C  CB   . GLU   A 1 187 ? -40.849 -0.854  16.625  1.00 61.45  ? 705  GLU   A CB   1 
ATOM   1591 C  CG   . GLU   A 1 187 ? -41.380 -0.184  17.876  1.00 69.02  ? 705  GLU   A CG   1 
ATOM   1592 C  CD   . GLU   A 1 187 ? -41.679 1.276   17.644  1.00 85.56  ? 705  GLU   A CD   1 
ATOM   1593 O  OE1  . GLU   A 1 187 ? -40.738 2.039   17.316  1.00 90.61  ? 705  GLU   A OE1  1 
ATOM   1594 O  OE2  . GLU   A 1 187 ? -42.863 1.656   17.775  1.00 93.17  ? 705  GLU   A OE2  1 
ATOM   1595 N  N    . LEU   A 1 188 ? -42.216 -1.073  13.445  1.00 52.50  ? 706  LEU   A N    1 
ATOM   1596 C  CA   . LEU   A 1 188 ? -41.859 -1.082  12.020  1.00 49.42  ? 706  LEU   A CA   1 
ATOM   1597 C  C    . LEU   A 1 188 ? -42.333 0.169   11.325  1.00 46.93  ? 706  LEU   A C    1 
ATOM   1598 O  O    . LEU   A 1 188 ? -43.462 0.608   11.533  1.00 46.10  ? 706  LEU   A O    1 
ATOM   1599 C  CB   . LEU   A 1 188 ? -42.441 -2.306  11.299  1.00 42.80  ? 706  LEU   A CB   1 
ATOM   1600 C  CG   . LEU   A 1 188 ? -41.628 -3.597  11.421  1.00 61.40  ? 706  LEU   A CG   1 
ATOM   1601 C  CD1  . LEU   A 1 188 ? -42.279 -4.765  10.675  1.00 65.73  ? 706  LEU   A CD1  1 
ATOM   1602 C  CD2  . LEU   A 1 188 ? -40.205 -3.355  10.932  1.00 60.14  ? 706  LEU   A CD2  1 
ATOM   1603 N  N    . PHE   A 1 189 ? -41.453 0.730   10.500  1.00 44.13  ? 707  PHE   A N    1 
ATOM   1604 C  CA   . PHE   A 1 189 ? -41.740 1.905   9.689   1.00 45.69  ? 707  PHE   A CA   1 
ATOM   1605 C  C    . PHE   A 1 189 ? -42.330 3.049   10.482  1.00 51.83  ? 707  PHE   A C    1 
ATOM   1606 O  O    . PHE   A 1 189 ? -43.171 3.793   9.975   1.00 62.86  ? 707  PHE   A O    1 
ATOM   1607 C  CB   . PHE   A 1 189 ? -42.667 1.533   8.543   1.00 48.32  ? 707  PHE   A CB   1 
ATOM   1608 C  CG   . PHE   A 1 189 ? -42.110 0.461   7.658   1.00 53.42  ? 707  PHE   A CG   1 
ATOM   1609 C  CD1  . PHE   A 1 189 ? -41.170 0.767   6.689   1.00 59.52  ? 707  PHE   A CD1  1 
ATOM   1610 C  CD2  . PHE   A 1 189 ? -42.506 -0.857  7.811   1.00 57.19  ? 707  PHE   A CD2  1 
ATOM   1611 C  CE1  . PHE   A 1 189 ? -40.655 -0.223  5.874   1.00 56.02  ? 707  PHE   A CE1  1 
ATOM   1612 C  CE2  . PHE   A 1 189 ? -41.983 -1.855  7.004   1.00 57.30  ? 707  PHE   A CE2  1 
ATOM   1613 C  CZ   . PHE   A 1 189 ? -41.061 -1.533  6.036   1.00 58.00  ? 707  PHE   A CZ   1 
ATOM   1614 N  N    . GLY   A 1 190 ? -41.886 3.194   11.727  1.00 54.81  ? 708  GLY   A N    1 
ATOM   1615 C  CA   . GLY   A 1 190 ? -42.329 4.308   12.549  1.00 49.16  ? 708  GLY   A CA   1 
ATOM   1616 C  C    . GLY   A 1 190 ? -43.713 4.064   13.105  1.00 44.57  ? 708  GLY   A C    1 
ATOM   1617 O  O    . GLY   A 1 190 ? -44.403 4.993   13.511  1.00 47.50  ? 708  GLY   A O    1 
ATOM   1618 N  N    . GLN   A 1 191 ? -44.123 2.799   13.116  1.00 47.81  ? 709  GLN   A N    1 
ATOM   1619 C  CA   . GLN   A 1 191 ? -45.407 2.428   13.695  1.00 48.69  ? 709  GLN   A CA   1 
ATOM   1620 C  C    . GLN   A 1 191 ? -45.269 1.161   14.538  1.00 47.44  ? 709  GLN   A C    1 
ATOM   1621 O  O    . GLN   A 1 191 ? -44.263 0.446   14.465  1.00 44.66  ? 709  GLN   A O    1 
ATOM   1622 C  CB   . GLN   A 1 191 ? -46.463 2.221   12.604  1.00 50.31  ? 709  GLN   A CB   1 
ATOM   1623 C  CG   . GLN   A 1 191 ? -46.655 3.408   11.668  1.00 48.45  ? 709  GLN   A CG   1 
ATOM   1624 C  CD   . GLN   A 1 191 ? -47.273 4.609   12.354  1.00 54.01  ? 709  GLN   A CD   1 
ATOM   1625 O  OE1  . GLN   A 1 191 ? -48.231 4.488   13.123  1.00 56.14  ? 709  GLN   A OE1  1 
ATOM   1626 N  NE2  . GLN   A 1 191 ? -46.720 5.780   12.084  1.00 53.24  ? 709  GLN   A NE2  1 
ATOM   1627 N  N    . THR   A 1 192 ? -46.293 0.899   15.339  1.00 48.21  ? 710  THR   A N    1 
ATOM   1628 C  CA   . THR   A 1 192 ? -46.333 -0.282  16.194  1.00 48.51  ? 710  THR   A CA   1 
ATOM   1629 C  C    . THR   A 1 192 ? -47.304 -1.297  15.616  1.00 45.01  ? 710  THR   A C    1 
ATOM   1630 O  O    . THR   A 1 192 ? -48.484 -0.997  15.446  1.00 48.82  ? 710  THR   A O    1 
ATOM   1631 C  CB   . THR   A 1 192 ? -46.749 0.091   17.631  1.00 53.39  ? 710  THR   A CB   1 
ATOM   1632 O  OG1  . THR   A 1 192 ? -45.710 0.883   18.220  1.00 50.90  ? 710  THR   A OG1  1 
ATOM   1633 C  CG2  . THR   A 1 192 ? -46.983 -1.160  18.486  1.00 57.98  ? 710  THR   A CG2  1 
ATOM   1634 N  N    . HIS   A 1 193 ? -46.810 -2.489  15.296  1.00 41.30  ? 711  HIS   A N    1 
ATOM   1635 C  CA   . HIS   A 1 193 ? -47.682 -3.534  14.773  1.00 40.93  ? 711  HIS   A CA   1 
ATOM   1636 C  C    . HIS   A 1 193 ? -48.019 -4.511  15.868  1.00 32.43  ? 711  HIS   A C    1 
ATOM   1637 O  O    . HIS   A 1 193 ? -47.137 -5.147  16.426  1.00 40.81  ? 711  HIS   A O    1 
ATOM   1638 C  CB   . HIS   A 1 193 ? -47.028 -4.283  13.618  1.00 45.11  ? 711  HIS   A CB   1 
ATOM   1639 C  CG   . HIS   A 1 193 ? -46.761 -3.434  12.420  1.00 54.75  ? 711  HIS   A CG   1 
ATOM   1640 N  ND1  . HIS   A 1 193 ? -46.177 -2.196  12.506  1.00 67.35  ? 711  HIS   A ND1  1 
ATOM   1641 C  CD2  . HIS   A 1 193 ? -46.966 -3.671  11.101  1.00 65.81  ? 711  HIS   A CD2  1 
ATOM   1642 C  CE1  . HIS   A 1 193 ? -46.052 -1.687  11.290  1.00 72.60  ? 711  HIS   A CE1  1 
ATOM   1643 N  NE2  . HIS   A 1 193 ? -46.524 -2.564  10.425  1.00 69.34  ? 711  HIS   A NE2  1 
ATOM   1644 N  N    . GLN   A 1 194 ? -49.297 -4.652  16.170  1.00 33.43  ? 712  GLN   A N    1 
ATOM   1645 C  CA   . GLN   A 1 194 ? -49.699 -5.598  17.195  1.00 30.58  ? 712  GLN   A CA   1 
ATOM   1646 C  C    . GLN   A 1 194 ? -50.238 -6.875  16.550  1.00 32.55  ? 712  GLN   A C    1 
ATOM   1647 O  O    . GLN   A 1 194 ? -51.030 -6.817  15.627  1.00 34.29  ? 712  GLN   A O    1 
ATOM   1648 C  CB   . GLN   A 1 194 ? -50.738 -4.966  18.111  1.00 32.50  ? 712  GLN   A CB   1 
ATOM   1649 C  CG   . GLN   A 1 194 ? -51.270 -5.857  19.207  1.00 48.37  ? 712  GLN   A CG   1 
ATOM   1650 C  CD   . GLN   A 1 194 ? -52.103 -5.072  20.218  1.00 59.32  ? 712  GLN   A CD   1 
ATOM   1651 O  OE1  . GLN   A 1 194 ? -51.641 -4.072  20.774  1.00 55.65  ? 712  GLN   A OE1  1 
ATOM   1652 N  NE2  . GLN   A 1 194 ? -53.344 -5.512  20.442  1.00 64.08  ? 712  GLN   A NE2  1 
ATOM   1653 N  N    A HIS   A 1 195 ? -49.776 -8.025  17.025  0.51 30.64  ? 713  HIS   A N    1 
ATOM   1654 N  N    B HIS   A 1 195 ? -49.795 -8.019  17.056  0.49 31.20  ? 713  HIS   A N    1 
ATOM   1655 C  CA   A HIS   A 1 195 ? -50.280 -9.306  16.538  0.51 35.86  ? 713  HIS   A CA   1 
ATOM   1656 C  CA   B HIS   A 1 195 ? -50.258 -9.313  16.571  0.49 36.00  ? 713  HIS   A CA   1 
ATOM   1657 C  C    A HIS   A 1 195 ? -50.717 -10.179 17.721  0.51 35.82  ? 713  HIS   A C    1 
ATOM   1658 C  C    B HIS   A 1 195 ? -50.720 -10.178 17.744  0.49 35.85  ? 713  HIS   A C    1 
ATOM   1659 O  O    A HIS   A 1 195 ? -49.961 -10.354 18.668  0.51 34.03  ? 713  HIS   A O    1 
ATOM   1660 O  O    B HIS   A 1 195 ? -49.984 -10.350 18.706  0.49 34.16  ? 713  HIS   A O    1 
ATOM   1661 C  CB   A HIS   A 1 195 ? -49.215 -10.033 15.703  0.51 34.43  ? 713  HIS   A CB   1 
ATOM   1662 C  CB   B HIS   A 1 195 ? -49.143 -10.021 15.798  0.49 34.06  ? 713  HIS   A CB   1 
ATOM   1663 C  CG   A HIS   A 1 195 ? -48.909 -9.375  14.391  0.51 39.84  ? 713  HIS   A CG   1 
ATOM   1664 C  CG   B HIS   A 1 195 ? -49.495 -11.414 15.363  0.49 35.18  ? 713  HIS   A CG   1 
ATOM   1665 N  ND1  A HIS   A 1 195 ? -47.811 -8.567  14.196  0.51 38.01  ? 713  HIS   A ND1  1 
ATOM   1666 N  ND1  B HIS   A 1 195 ? -50.377 -11.672 14.345  0.49 34.95  ? 713  HIS   A ND1  1 
ATOM   1667 C  CD2  A HIS   A 1 195 ? -49.561 -9.410  13.200  0.51 41.08  ? 713  HIS   A CD2  1 
ATOM   1668 C  CD2  B HIS   A 1 195 ? -49.067 -12.613 15.817  0.49 33.99  ? 713  HIS   A CD2  1 
ATOM   1669 C  CE1  A HIS   A 1 195 ? -47.793 -8.135  12.949  0.51 30.27  ? 713  HIS   A CE1  1 
ATOM   1670 C  CE1  B HIS   A 1 195 ? -50.482 -12.984 14.183  0.49 31.15  ? 713  HIS   A CE1  1 
ATOM   1671 N  NE2  A HIS   A 1 195 ? -48.844 -8.636  12.324  0.51 41.45  ? 713  HIS   A NE2  1 
ATOM   1672 N  NE2  B HIS   A 1 195 ? -49.701 -13.573 15.059  0.49 25.31  ? 713  HIS   A NE2  1 
ATOM   1673 N  N    . GLU   A 1 196 ? -51.931 -10.721 17.662  1.00 27.68  ? 714  GLU   A N    1 
ATOM   1674 C  CA   . GLU   A 1 196 ? -52.430 -11.605 18.719  1.00 36.94  ? 714  GLU   A CA   1 
ATOM   1675 C  C    . GLU   A 1 196 ? -51.723 -12.963 18.612  1.00 36.49  ? 714  GLU   A C    1 
ATOM   1676 O  O    . GLU   A 1 196 ? -51.566 -13.500 17.514  1.00 37.16  ? 714  GLU   A O    1 
ATOM   1677 C  CB   . GLU   A 1 196 ? -53.953 -11.763 18.638  1.00 32.26  ? 714  GLU   A CB   1 
ATOM   1678 C  CG   . GLU   A 1 196 ? -54.440 -12.598 17.448  1.00 42.04  ? 714  GLU   A CG   1 
ATOM   1679 C  CD   . GLU   A 1 196 ? -55.953 -12.821 17.456  1.00 47.70  ? 714  GLU   A CD   1 
ATOM   1680 O  OE1  . GLU   A 1 196 ? -56.613 -12.397 18.436  1.00 35.23  ? 714  GLU   A OE1  1 
ATOM   1681 O  OE2  . GLU   A 1 196 ? -56.477 -13.427 16.491  1.00 50.50  ? 714  GLU   A OE2  1 
ATOM   1682 N  N    . LEU   A 1 197 ? -51.262 -13.500 19.742  1.00 33.53  ? 715  LEU   A N    1 
ATOM   1683 C  CA   . LEU   A 1 197 ? -50.499 -14.759 19.729  1.00 25.53  ? 715  LEU   A CA   1 
ATOM   1684 C  C    . LEU   A 1 197 ? -51.419 -15.960 19.661  1.00 31.00  ? 715  LEU   A C    1 
ATOM   1685 O  O    . LEU   A 1 197 ? -50.997 -17.057 19.329  1.00 34.70  ? 715  LEU   A O    1 
ATOM   1686 C  CB   . LEU   A 1 197 ? -49.605 -14.876 20.964  1.00 29.90  ? 715  LEU   A CB   1 
ATOM   1687 C  CG   . LEU   A 1 197 ? -48.375 -13.980 20.959  1.00 33.21  ? 715  LEU   A CG   1 
ATOM   1688 C  CD1  . LEU   A 1 197 ? -47.656 -14.077 22.303  1.00 30.73  ? 715  LEU   A CD1  1 
ATOM   1689 C  CD2  . LEU   A 1 197 ? -47.477 -14.370 19.807  1.00 31.66  ? 715  LEU   A CD2  1 
ATOM   1690 N  N    . LYS   A 1 198 ? -52.679 -15.748 20.009  1.00 32.06  ? 716  LYS   A N    1 
ATOM   1691 C  CA   . LYS   A 1 198 ? -53.697 -16.765 19.836  1.00 43.76  ? 716  LYS   A CA   1 
ATOM   1692 C  C    . LYS   A 1 198 ? -55.032 -16.046 19.796  1.00 48.19  ? 716  LYS   A C    1 
ATOM   1693 O  O    . LYS   A 1 198 ? -55.108 -14.872 20.166  1.00 40.52  ? 716  LYS   A O    1 
ATOM   1694 C  CB   . LYS   A 1 198 ? -53.656 -17.796 20.961  1.00 44.38  ? 716  LYS   A CB   1 
ATOM   1695 C  CG   . LYS   A 1 198 ? -53.973 -17.213 22.312  1.00 38.32  ? 716  LYS   A CG   1 
ATOM   1696 C  CD   . LYS   A 1 198 ? -53.669 -18.200 23.431  1.00 43.72  ? 716  LYS   A CD   1 
ATOM   1697 C  CE   . LYS   A 1 198 ? -54.415 -19.510 23.230  1.00 48.18  ? 716  LYS   A CE   1 
ATOM   1698 N  NZ   . LYS   A 1 198 ? -54.298 -20.375 24.444  1.00 48.03  ? 716  LYS   A NZ   1 
ATOM   1699 N  N    . ASN   A 1 199 ? -56.069 -16.742 19.335  1.00 48.92  ? 717  ASN   A N    1 
ATOM   1700 C  CA   . ASN   A 1 199 ? -57.394 -16.158 19.199  1.00 44.74  ? 717  ASN   A CA   1 
ATOM   1701 C  C    . ASN   A 1 199 ? -57.848 -15.471 20.478  1.00 44.73  ? 717  ASN   A C    1 
ATOM   1702 O  O    . ASN   A 1 199 ? -57.770 -16.047 21.558  1.00 48.16  ? 717  ASN   A O    1 
ATOM   1703 C  CB   . ASN   A 1 199 ? -58.407 -17.226 18.795  1.00 55.23  ? 717  ASN   A CB   1 
ATOM   1704 C  CG   . ASN   A 1 199 ? -59.772 -16.641 18.491  1.00 68.51  ? 717  ASN   A CG   1 
ATOM   1705 O  OD1  . ASN   A 1 199 ? -59.874 -15.580 17.875  1.00 65.73  ? 717  ASN   A OD1  1 
ATOM   1706 N  ND2  . ASN   A 1 199 ? -60.829 -17.315 18.946  1.00 76.16  ? 717  ASN   A ND2  1 
ATOM   1707 N  N    . GLY   A 1 200 ? -58.314 -14.229 20.353  1.00 45.86  ? 718  GLY   A N    1 
ATOM   1708 C  CA   . GLY   A 1 200 ? -58.650 -13.414 21.509  1.00 42.79  ? 718  GLY   A CA   1 
ATOM   1709 C  C    . GLY   A 1 200 ? -57.444 -13.056 22.376  1.00 41.01  ? 718  GLY   A C    1 
ATOM   1710 O  O    . GLY   A 1 200 ? -57.593 -12.719 23.561  1.00 43.54  ? 718  GLY   A O    1 
ATOM   1711 N  N    . GLY   A 1 201 ? -56.250 -13.112 21.786  1.00 34.00  ? 719  GLY   A N    1 
ATOM   1712 C  CA   . GLY   A 1 201 ? -55.017 -12.897 22.524  1.00 31.32  ? 719  GLY   A CA   1 
ATOM   1713 C  C    . GLY   A 1 201 ? -54.989 -11.599 23.323  1.00 38.86  ? 719  GLY   A C    1 
ATOM   1714 O  O    . GLY   A 1 201 ? -54.419 -11.550 24.402  1.00 32.05  ? 719  GLY   A O    1 
ATOM   1715 N  N    . SER   A 1 202 ? -55.628 -10.556 22.804  1.00 41.09  ? 720  SER   A N    1 
ATOM   1716 C  CA   . SER   A 1 202 ? -55.603 -9.245  23.452  1.00 37.09  ? 720  SER   A CA   1 
ATOM   1717 C  C    . SER   A 1 202 ? -56.227 -9.248  24.839  1.00 37.80  ? 720  SER   A C    1 
ATOM   1718 O  O    . SER   A 1 202 ? -55.869 -8.430  25.671  1.00 37.26  ? 720  SER   A O    1 
ATOM   1719 C  CB   . SER   A 1 202 ? -56.311 -8.209  22.587  1.00 36.55  ? 720  SER   A CB   1 
ATOM   1720 O  OG   . SER   A 1 202 ? -57.648 -8.593  22.345  1.00 49.19  ? 720  SER   A OG   1 
ATOM   1721 N  N    . GLU   A 1 203 ? -57.152 -10.169 25.090  1.00 37.05  ? 721  GLU   A N    1 
ATOM   1722 C  CA   . GLU   A 1 203 ? -57.904 -10.151 26.338  1.00 35.98  ? 721  GLU   A CA   1 
ATOM   1723 C  C    . GLU   A 1 203 ? -57.452 -11.215 27.329  1.00 37.33  ? 721  GLU   A C    1 
ATOM   1724 O  O    . GLU   A 1 203 ? -58.132 -11.486 28.312  1.00 47.65  ? 721  GLU   A O    1 
ATOM   1725 C  CB   . GLU   A 1 203 ? -59.402 -10.325 26.050  1.00 46.77  ? 721  GLU   A CB   1 
ATOM   1726 C  CG   . GLU   A 1 203 ? -59.962 -9.350  25.011  1.00 60.07  ? 721  GLU   A CG   1 
ATOM   1727 C  CD   . GLU   A 1 203 ? -59.827 -7.874  25.415  1.00 76.96  ? 721  GLU   A CD   1 
ATOM   1728 O  OE1  . GLU   A 1 203 ? -59.802 -7.569  26.630  1.00 79.52  ? 721  GLU   A OE1  1 
ATOM   1729 O  OE2  . GLU   A 1 203 ? -59.761 -7.010  24.510  1.00 85.09  ? 721  GLU   A OE2  1 
ATOM   1730 N  N    . ILE   A 1 204 ? -56.306 -11.820 27.068  1.00 38.34  ? 722  ILE   A N    1 
ATOM   1731 C  CA   . ILE   A 1 204 ? -55.825 -12.943 27.863  1.00 38.08  ? 722  ILE   A CA   1 
ATOM   1732 C  C    . ILE   A 1 204 ? -54.583 -12.518 28.613  1.00 32.27  ? 722  ILE   A C    1 
ATOM   1733 O  O    . ILE   A 1 204 ? -53.588 -12.132 28.005  1.00 31.75  ? 722  ILE   A O    1 
ATOM   1734 C  CB   . ILE   A 1 204 ? -55.516 -14.164 26.967  1.00 42.44  ? 722  ILE   A CB   1 
ATOM   1735 C  CG1  . ILE   A 1 204 ? -56.760 -14.555 26.169  1.00 32.50  ? 722  ILE   A CG1  1 
ATOM   1736 C  CG2  . ILE   A 1 204 ? -54.984 -15.348 27.791  1.00 41.04  ? 722  ILE   A CG2  1 
ATOM   1737 C  CD1  . ILE   A 1 204 ? -56.486 -15.689 25.229  1.00 35.72  ? 722  ILE   A CD1  1 
ATOM   1738 N  N    . VAL   A 1 205 ? -54.652 -12.555 29.937  1.00 32.44  ? 723  VAL   A N    1 
ATOM   1739 C  CA   . VAL   A 1 205 ? -53.580 -12.040 30.766  1.00 35.98  ? 723  VAL   A CA   1 
ATOM   1740 C  C    . VAL   A 1 205 ? -52.508 -13.106 30.960  1.00 39.04  ? 723  VAL   A C    1 
ATOM   1741 O  O    . VAL   A 1 205 ? -52.825 -14.262 31.250  1.00 32.62  ? 723  VAL   A O    1 
ATOM   1742 C  CB   . VAL   A 1 205 ? -54.114 -11.570 32.155  1.00 43.65  ? 723  VAL   A CB   1 
ATOM   1743 C  CG1  . VAL   A 1 205 ? -52.975 -11.083 33.031  1.00 37.15  ? 723  VAL   A CG1  1 
ATOM   1744 C  CG2  . VAL   A 1 205 ? -55.174 -10.469 31.995  1.00 36.74  ? 723  VAL   A CG2  1 
ATOM   1745 N  N    . VAL   A 1 206 ? -51.245 -12.714 30.806  1.00 31.32  ? 724  VAL   A N    1 
ATOM   1746 C  CA   . VAL   A 1 206 ? -50.128 -13.621 31.069  1.00 40.35  ? 724  VAL   A CA   1 
ATOM   1747 C  C    . VAL   A 1 206 ? -49.943 -13.806 32.586  1.00 45.91  ? 724  VAL   A C    1 
ATOM   1748 O  O    . VAL   A 1 206 ? -49.850 -12.827 33.323  1.00 33.29  ? 724  VAL   A O    1 
ATOM   1749 C  CB   . VAL   A 1 206 ? -48.821 -13.105 30.443  1.00 36.26  ? 724  VAL   A CB   1 
ATOM   1750 C  CG1  . VAL   A 1 206 ? -47.701 -14.109 30.663  1.00 30.43  ? 724  VAL   A CG1  1 
ATOM   1751 C  CG2  . VAL   A 1 206 ? -49.012 -12.838 28.923  1.00 29.13  ? 724  VAL   A CG2  1 
ATOM   1752 N  N    . THR   A 1 207 ? -49.934 -15.062 33.034  1.00 41.13  ? 725  THR   A N    1 
ATOM   1753 C  CA   . THR   A 1 207 ? -49.768 -15.423 34.447  1.00 35.12  ? 725  THR   A CA   1 
ATOM   1754 C  C    . THR   A 1 207 ? -48.830 -16.615 34.579  1.00 35.58  ? 725  THR   A C    1 
ATOM   1755 O  O    . THR   A 1 207 ? -48.336 -17.140 33.581  1.00 36.58  ? 725  THR   A O    1 
ATOM   1756 C  CB   . THR   A 1 207 ? -51.104 -15.816 35.127  1.00 36.98  ? 725  THR   A CB   1 
ATOM   1757 O  OG1  . THR   A 1 207 ? -51.475 -17.133 34.699  1.00 44.73  ? 725  THR   A OG1  1 
ATOM   1758 C  CG2  . THR   A 1 207 ? -52.217 -14.857 34.782  1.00 38.14  ? 725  THR   A CG2  1 
ATOM   1759 N  N    . ASN   A 1 208 ? -48.633 -17.096 35.798  1.00 37.38  ? 726  ASN   A N    1 
ATOM   1760 C  CA   . ASN   A 1 208 ? -47.775 -18.268 36.003  1.00 42.98  ? 726  ASN   A CA   1 
ATOM   1761 C  C    . ASN   A 1 208 ? -48.380 -19.547 35.419  1.00 40.53  ? 726  ASN   A C    1 
ATOM   1762 O  O    . ASN   A 1 208 ? -47.659 -20.482 35.076  1.00 44.10  ? 726  ASN   A O    1 
ATOM   1763 C  CB   . ASN   A 1 208 ? -47.472 -18.466 37.502  1.00 42.72  ? 726  ASN   A CB   1 
ATOM   1764 C  CG   . ASN   A 1 208 ? -46.297 -17.615 37.981  1.00 44.33  ? 726  ASN   A CG   1 
ATOM   1765 O  OD1  . ASN   A 1 208 ? -45.476 -17.162 37.179  1.00 44.27  ? 726  ASN   A OD1  1 
ATOM   1766 N  ND2  . ASN   A 1 208 ? -46.216 -17.394 39.285  1.00 50.71  ? 726  ASN   A ND2  1 
ATOM   1767 N  N    . LYS   A 1 209 ? -49.705 -19.592 35.311  1.00 42.41  ? 727  LYS   A N    1 
ATOM   1768 C  CA   . LYS   A 1 209 ? -50.381 -20.775 34.763  1.00 43.06  ? 727  LYS   A CA   1 
ATOM   1769 C  C    . LYS   A 1 209 ? -50.232 -20.911 33.245  1.00 47.39  ? 727  LYS   A C    1 
ATOM   1770 O  O    . LYS   A 1 209 ? -50.276 -22.018 32.713  1.00 37.40  ? 727  LYS   A O    1 
ATOM   1771 C  CB   . LYS   A 1 209 ? -51.864 -20.754 35.113  1.00 47.76  ? 727  LYS   A CB   1 
ATOM   1772 C  CG   . LYS   A 1 209 ? -52.192 -21.057 36.568  1.00 56.66  ? 727  LYS   A CG   1 
ATOM   1773 C  CD   . LYS   A 1 209 ? -53.623 -20.631 36.876  1.00 61.11  ? 727  LYS   A CD   1 
ATOM   1774 C  CE   . LYS   A 1 209 ? -53.997 -20.893 38.324  1.00 72.13  ? 727  LYS   A CE   1 
ATOM   1775 N  NZ   . LYS   A 1 209 ? -55.375 -20.408 38.619  1.00 75.60  ? 727  LYS   A NZ   1 
ATOM   1776 N  N    . ASN   A 1 210 ? -50.068 -19.796 32.536  1.00 39.88  ? 728  ASN   A N    1 
ATOM   1777 C  CA   . ASN   A 1 210 ? -49.944 -19.884 31.081  1.00 33.48  ? 728  ASN   A CA   1 
ATOM   1778 C  C    . ASN   A 1 210 ? -48.660 -19.283 30.483  1.00 32.04  ? 728  ASN   A C    1 
ATOM   1779 O  O    . ASN   A 1 210 ? -48.525 -19.230 29.260  1.00 33.86  ? 728  ASN   A O    1 
ATOM   1780 C  CB   . ASN   A 1 210 ? -51.168 -19.233 30.411  1.00 40.43  ? 728  ASN   A CB   1 
ATOM   1781 C  CG   . ASN   A 1 210 ? -51.318 -17.742 30.749  1.00 38.44  ? 728  ASN   A CG   1 
ATOM   1782 O  OD1  . ASN   A 1 210 ? -50.358 -17.067 31.112  1.00 37.30  ? 728  ASN   A OD1  1 
ATOM   1783 N  ND2  . ASN   A 1 210 ? -52.536 -17.237 30.639  1.00 34.66  ? 728  ASN   A ND2  1 
ATOM   1784 N  N    . LYS   A 1 211 ? -47.705 -18.862 31.310  1.00 35.93  ? 729  LYS   A N    1 
ATOM   1785 C  CA   . LYS   A 1 211 ? -46.547 -18.141 30.761  1.00 38.72  ? 729  LYS   A CA   1 
ATOM   1786 C  C    . LYS   A 1 211 ? -45.617 -19.037 29.941  1.00 33.94  ? 729  LYS   A C    1 
ATOM   1787 O  O    . LYS   A 1 211 ? -44.980 -18.552 29.014  1.00 33.44  ? 729  LYS   A O    1 
ATOM   1788 C  CB   . LYS   A 1 211 ? -45.745 -17.435 31.864  1.00 34.72  ? 729  LYS   A CB   1 
ATOM   1789 C  CG   . LYS   A 1 211 ? -45.080 -18.338 32.897  1.00 37.79  ? 729  LYS   A CG   1 
ATOM   1790 C  CD   . LYS   A 1 211 ? -44.370 -17.473 33.917  1.00 39.68  ? 729  LYS   A CD   1 
ATOM   1791 C  CE   . LYS   A 1 211 ? -43.513 -18.291 34.871  1.00 37.03  ? 729  LYS   A CE   1 
ATOM   1792 N  NZ   . LYS   A 1 211 ? -42.941 -17.397 35.942  1.00 38.45  ? 729  LYS   A NZ   1 
ATOM   1793 N  N    . LYS   A 1 212 ? -45.536 -20.327 30.256  1.00 31.73  ? 730  LYS   A N    1 
ATOM   1794 C  CA   . LYS   A 1 212 ? -44.746 -21.232 29.410  1.00 31.19  ? 730  LYS   A CA   1 
ATOM   1795 C  C    . LYS   A 1 212 ? -45.300 -21.263 27.983  1.00 29.69  ? 730  LYS   A C    1 
ATOM   1796 O  O    . LYS   A 1 212 ? -44.546 -21.282 27.008  1.00 32.59  ? 730  LYS   A O    1 
ATOM   1797 C  CB   . LYS   A 1 212 ? -44.708 -22.649 29.997  1.00 38.08  ? 730  LYS   A CB   1 
ATOM   1798 C  CG   . LYS   A 1 212 ? -43.981 -22.742 31.338  1.00 40.27  ? 730  LYS   A CG   1 
ATOM   1799 C  CD   . LYS   A 1 212 ? -42.478 -22.507 31.195  1.00 34.34  ? 730  LYS   A CD   1 
ATOM   1800 C  CE   . LYS   A 1 212 ? -41.799 -23.669 30.484  1.00 35.43  ? 730  LYS   A CE   1 
ATOM   1801 N  NZ   . LYS   A 1 212 ? -40.306 -23.615 30.513  1.00 37.74  ? 730  LYS   A NZ   1 
ATOM   1802 N  N    . GLU   A 1 213 ? -46.622 -21.269 27.865  1.00 32.21  ? 731  GLU   A N    1 
ATOM   1803 C  CA   . GLU   A 1 213 ? -47.265 -21.162 26.561  1.00 30.77  ? 731  GLU   A CA   1 
ATOM   1804 C  C    . GLU   A 1 213 ? -46.977 -19.791 25.910  1.00 28.98  ? 731  GLU   A C    1 
ATOM   1805 O  O    . GLU   A 1 213 ? -46.672 -19.722 24.717  1.00 26.42  ? 731  GLU   A O    1 
ATOM   1806 C  CB   . GLU   A 1 213 ? -48.768 -21.376 26.702  1.00 34.06  ? 731  GLU   A CB   1 
ATOM   1807 C  CG   . GLU   A 1 213 ? -49.526 -21.429 25.381  1.00 36.18  ? 731  GLU   A CG   1 
ATOM   1808 C  CD   . GLU   A 1 213 ? -51.022 -21.411 25.599  1.00 38.44  ? 731  GLU   A CD   1 
ATOM   1809 O  OE1  . GLU   A 1 213 ? -51.436 -21.494 26.770  1.00 47.17  ? 731  GLU   A OE1  1 
ATOM   1810 O  OE2  . GLU   A 1 213 ? -51.787 -21.307 24.617  1.00 43.21  ? 731  GLU   A OE2  1 
ATOM   1811 N  N    . TYR   A 1 214 ? -47.078 -18.715 26.701  1.00 28.79  ? 732  TYR   A N    1 
ATOM   1812 C  CA   . TYR   A 1 214 ? -46.771 -17.358 26.213  1.00 27.46  ? 732  TYR   A CA   1 
ATOM   1813 C  C    . TYR   A 1 214 ? -45.408 -17.320 25.571  1.00 32.75  ? 732  TYR   A C    1 
ATOM   1814 O  O    . TYR   A 1 214 ? -45.267 -16.880 24.418  1.00 29.79  ? 732  TYR   A O    1 
ATOM   1815 C  CB   . TYR   A 1 214 ? -46.816 -16.333 27.345  1.00 27.62  ? 732  TYR   A CB   1 
ATOM   1816 C  CG   . TYR   A 1 214 ? -46.428 -14.909 26.949  1.00 31.79  ? 732  TYR   A CG   1 
ATOM   1817 C  CD1  . TYR   A 1 214 ? -47.290 -14.098 26.200  1.00 28.57  ? 732  TYR   A CD1  1 
ATOM   1818 C  CD2  . TYR   A 1 214 ? -45.210 -14.367 27.344  1.00 30.16  ? 732  TYR   A CD2  1 
ATOM   1819 C  CE1  . TYR   A 1 214 ? -46.938 -12.783 25.858  1.00 31.68  ? 732  TYR   A CE1  1 
ATOM   1820 C  CE2  . TYR   A 1 214 ? -44.849 -13.073 27.003  1.00 32.29  ? 732  TYR   A CE2  1 
ATOM   1821 C  CZ   . TYR   A 1 214 ? -45.714 -12.286 26.267  1.00 36.73  ? 732  TYR   A CZ   1 
ATOM   1822 O  OH   . TYR   A 1 214 ? -45.335 -11.008 25.954  1.00 41.63  ? 732  TYR   A OH   1 
ATOM   1823 N  N    . ILE   A 1 215 ? -44.411 -17.818 26.312  1.00 26.72  ? 733  ILE   A N    1 
ATOM   1824 C  CA   . ILE   A 1 215 ? -43.024 -17.772 25.863  1.00 29.70  ? 733  ILE   A CA   1 
ATOM   1825 C  C    . ILE   A 1 215 ? -42.854 -18.609 24.604  1.00 31.51  ? 733  ILE   A C    1 
ATOM   1826 O  O    . ILE   A 1 215 ? -42.200 -18.188 23.658  1.00 32.45  ? 733  ILE   A O    1 
ATOM   1827 C  CB   . ILE   A 1 215 ? -42.061 -18.254 26.962  1.00 33.16  ? 733  ILE   A CB   1 
ATOM   1828 C  CG1  . ILE   A 1 215 ? -41.966 -17.188 28.057  1.00 31.65  ? 733  ILE   A CG1  1 
ATOM   1829 C  CG2  . ILE   A 1 215 ? -40.668 -18.490 26.380  1.00 30.88  ? 733  ILE   A CG2  1 
ATOM   1830 C  CD1  . ILE   A 1 215 ? -41.555 -17.749 29.426  1.00 35.83  ? 733  ILE   A CD1  1 
ATOM   1831 N  N    . TYR   A 1 216 ? -43.477 -19.784 24.584  1.00 27.28  ? 734  TYR   A N    1 
ATOM   1832 C  CA   . TYR   A 1 216 ? -43.440 -20.620 23.395  1.00 28.67  ? 734  TYR   A CA   1 
ATOM   1833 C  C    . TYR   A 1 216 ? -43.984 -19.871 22.164  1.00 24.00  ? 734  TYR   A C    1 
ATOM   1834 O  O    . TYR   A 1 216 ? -43.371 -19.886 21.095  1.00 31.93  ? 734  TYR   A O    1 
ATOM   1835 C  CB   . TYR   A 1 216 ? -44.232 -21.913 23.654  1.00 26.97  ? 734  TYR   A CB   1 
ATOM   1836 C  CG   . TYR   A 1 216 ? -44.769 -22.585 22.432  1.00 29.38  ? 734  TYR   A CG   1 
ATOM   1837 C  CD1  . TYR   A 1 216 ? -46.135 -22.604 22.176  1.00 35.38  ? 734  TYR   A CD1  1 
ATOM   1838 C  CD2  . TYR   A 1 216 ? -43.922 -23.223 21.536  1.00 37.13  ? 734  TYR   A CD2  1 
ATOM   1839 C  CE1  . TYR   A 1 216 ? -46.644 -23.234 21.049  1.00 35.51  ? 734  TYR   A CE1  1 
ATOM   1840 C  CE2  . TYR   A 1 216 ? -44.424 -23.864 20.409  1.00 41.31  ? 734  TYR   A CE2  1 
ATOM   1841 C  CZ   . TYR   A 1 216 ? -45.783 -23.858 20.170  1.00 39.30  ? 734  TYR   A CZ   1 
ATOM   1842 O  OH   . TYR   A 1 216 ? -46.283 -24.476 19.044  1.00 45.10  ? 734  TYR   A OH   1 
ATOM   1843 N  N    . LEU   A 1 217 ? -45.145 -19.240 22.316  1.00 30.38  ? 735  LEU   A N    1 
ATOM   1844 C  CA   . LEU   A 1 217 ? -45.786 -18.505 21.218  1.00 23.68  ? 735  LEU   A CA   1 
ATOM   1845 C  C    . LEU   A 1 217 ? -44.954 -17.295 20.745  1.00 23.10  ? 735  LEU   A C    1 
ATOM   1846 O  O    . LEU   A 1 217 ? -44.896 -16.993 19.548  1.00 26.29  ? 735  LEU   A O    1 
ATOM   1847 C  CB   . LEU   A 1 217 ? -47.197 -18.055 21.640  1.00 33.00  ? 735  LEU   A CB   1 
ATOM   1848 C  CG   . LEU   A 1 217 ? -48.205 -19.211 21.855  1.00 25.18  ? 735  LEU   A CG   1 
ATOM   1849 C  CD1  . LEU   A 1 217 ? -49.523 -18.759 22.451  1.00 26.09  ? 735  LEU   A CD1  1 
ATOM   1850 C  CD2  . LEU   A 1 217 ? -48.454 -19.994 20.532  1.00 24.97  ? 735  LEU   A CD2  1 
ATOM   1851 N  N    . VAL   A 1 218 ? -44.297 -16.616 21.675  1.00 23.41  ? 736  VAL   A N    1 
ATOM   1852 C  CA   . VAL   A 1 218 ? -43.439 -15.479 21.317  1.00 29.48  ? 736  VAL   A CA   1 
ATOM   1853 C  C    . VAL   A 1 218 ? -42.248 -15.977 20.503  1.00 33.57  ? 736  VAL   A C    1 
ATOM   1854 O  O    . VAL   A 1 218 ? -41.887 -15.408 19.471  1.00 31.81  ? 736  VAL   A O    1 
ATOM   1855 C  CB   . VAL   A 1 218 ? -42.938 -14.705 22.574  1.00 27.78  ? 736  VAL   A CB   1 
ATOM   1856 C  CG1  . VAL   A 1 218 ? -41.781 -13.750 22.222  1.00 24.54  ? 736  VAL   A CG1  1 
ATOM   1857 C  CG2  . VAL   A 1 218 ? -44.087 -13.940 23.221  1.00 29.01  ? 736  VAL   A CG2  1 
ATOM   1858 N  N    . ILE   A 1 219 ? -41.653 -17.066 20.969  1.00 32.44  ? 737  ILE   A N    1 
ATOM   1859 C  CA   . ILE   A 1 219 ? -40.521 -17.666 20.281  1.00 27.93  ? 737  ILE   A CA   1 
ATOM   1860 C  C    . ILE   A 1 219 ? -40.906 -18.149 18.869  1.00 25.90  ? 737  ILE   A C    1 
ATOM   1861 O  O    . ILE   A 1 219 ? -40.173 -17.902 17.908  1.00 29.22  ? 737  ILE   A O    1 
ATOM   1862 C  CB   . ILE   A 1 219 ? -39.937 -18.834 21.108  1.00 33.38  ? 737  ILE   A CB   1 
ATOM   1863 C  CG1  . ILE   A 1 219 ? -39.231 -18.285 22.348  1.00 36.39  ? 737  ILE   A CG1  1 
ATOM   1864 C  CG2  . ILE   A 1 219 ? -38.938 -19.639 20.285  1.00 34.67  ? 737  ILE   A CG2  1 
ATOM   1865 C  CD1  . ILE   A 1 219 ? -38.870 -19.362 23.319  1.00 49.43  ? 737  ILE   A CD1  1 
ATOM   1866 N  N    . GLN   A 1 220 ? -42.052 -18.822 18.755  1.00 25.49  ? 738  GLN   A N    1 
ATOM   1867 C  CA   . GLN   A 1 220 ? -42.525 -19.299 17.467  1.00 24.31  ? 738  GLN   A CA   1 
ATOM   1868 C  C    . GLN   A 1 220 ? -42.798 -18.105 16.554  1.00 33.27  ? 738  GLN   A C    1 
ATOM   1869 O  O    . GLN   A 1 220 ? -42.530 -18.168 15.356  1.00 25.97  ? 738  GLN   A O    1 
ATOM   1870 C  CB   . GLN   A 1 220 ? -43.784 -20.143 17.599  1.00 22.80  ? 738  GLN   A CB   1 
ATOM   1871 C  CG   . GLN   A 1 220 ? -43.579 -21.463 18.301  1.00 29.48  ? 738  GLN   A CG   1 
ATOM   1872 C  CD   . GLN   A 1 220 ? -42.542 -22.325 17.614  1.00 41.65  ? 738  GLN   A CD   1 
ATOM   1873 O  OE1  . GLN   A 1 220 ? -42.688 -22.671 16.436  1.00 39.43  ? 738  GLN   A OE1  1 
ATOM   1874 N  NE2  . GLN   A 1 220 ? -41.480 -22.667 18.338  1.00 39.43  ? 738  GLN   A NE2  1 
ATOM   1875 N  N    . TRP   A 1 221 ? -43.325 -17.018 17.118  1.00 21.46  ? 739  TRP   A N    1 
ATOM   1876 C  CA   . TRP   A 1 221 ? -43.557 -15.806 16.304  1.00 34.37  ? 739  TRP   A CA   1 
ATOM   1877 C  C    . TRP   A 1 221 ? -42.241 -15.230 15.797  1.00 32.77  ? 739  TRP   A C    1 
ATOM   1878 O  O    . TRP   A 1 221 ? -42.147 -14.785 14.649  1.00 31.09  ? 739  TRP   A O    1 
ATOM   1879 C  CB   . TRP   A 1 221 ? -44.326 -14.701 17.072  1.00 28.27  ? 739  TRP   A CB   1 
ATOM   1880 C  CG   . TRP   A 1 221 ? -44.488 -13.438 16.232  1.00 32.92  ? 739  TRP   A CG   1 
ATOM   1881 C  CD1  . TRP   A 1 221 ? -45.487 -13.167 15.343  1.00 34.08  ? 739  TRP   A CD1  1 
ATOM   1882 C  CD2  . TRP   A 1 221 ? -43.598 -12.302 16.190  1.00 34.67  ? 739  TRP   A CD2  1 
ATOM   1883 N  NE1  . TRP   A 1 221 ? -45.289 -11.931 14.764  1.00 39.05  ? 739  TRP   A NE1  1 
ATOM   1884 C  CE2  . TRP   A 1 221 ? -44.131 -11.386 15.259  1.00 41.99  ? 739  TRP   A CE2  1 
ATOM   1885 C  CE3  . TRP   A 1 221 ? -42.403 -11.978 16.848  1.00 40.57  ? 739  TRP   A CE3  1 
ATOM   1886 C  CZ2  . TRP   A 1 221 ? -43.516 -10.157 14.974  1.00 56.27  ? 739  TRP   A CZ2  1 
ATOM   1887 C  CZ3  . TRP   A 1 221 ? -41.786 -10.752 16.562  1.00 44.61  ? 739  TRP   A CZ3  1 
ATOM   1888 C  CH2  . TRP   A 1 221 ? -42.347 -9.862  15.627  1.00 51.37  ? 739  TRP   A CH2  1 
ATOM   1889 N  N    . ARG   A 1 222 ? -41.222 -15.219 16.648  1.00 32.63  ? 740  ARG   A N    1 
ATOM   1890 C  CA   . ARG   A 1 222 ? -39.993 -14.532 16.273  1.00 33.85  ? 740  ARG   A CA   1 
ATOM   1891 C  C    . ARG   A 1 222 ? -39.232 -15.326 15.205  1.00 29.06  ? 740  ARG   A C    1 
ATOM   1892 O  O    . ARG   A 1 222 ? -38.609 -14.732 14.319  1.00 32.72  ? 740  ARG   A O    1 
ATOM   1893 C  CB   . ARG   A 1 222 ? -39.101 -14.281 17.508  1.00 30.55  ? 740  ARG   A CB   1 
ATOM   1894 C  CG   . ARG   A 1 222 ? -37.719 -13.700 17.189  1.00 27.09  ? 740  ARG   A CG   1 
ATOM   1895 C  CD   . ARG   A 1 222 ? -37.827 -12.377 16.394  1.00 29.90  ? 740  ARG   A CD   1 
ATOM   1896 N  NE   . ARG   A 1 222 ? -36.522 -11.758 16.123  1.00 32.71  ? 740  ARG   A NE   1 
ATOM   1897 C  CZ   . ARG   A 1 222 ? -35.706 -12.123 15.138  1.00 34.77  ? 740  ARG   A CZ   1 
ATOM   1898 N  NH1  . ARG   A 1 222 ? -36.046 -13.110 14.316  1.00 32.42  ? 740  ARG   A NH1  1 
ATOM   1899 N  NH2  . ARG   A 1 222 ? -34.550 -11.501 14.966  1.00 32.01  ? 740  ARG   A NH2  1 
ATOM   1900 N  N    . PHE   A 1 223 ? -39.302 -16.652 15.282  1.00 28.95  ? 741  PHE   A N    1 
ATOM   1901 C  CA   . PHE   A 1 223 ? -38.391 -17.510 14.507  1.00 34.33  ? 741  PHE   A CA   1 
ATOM   1902 C  C    . PHE   A 1 223 ? -39.040 -18.491 13.543  1.00 38.11  ? 741  PHE   A C    1 
ATOM   1903 O  O    . PHE   A 1 223 ? -38.365 -19.000 12.644  1.00 39.17  ? 741  PHE   A O    1 
ATOM   1904 C  CB   . PHE   A 1 223 ? -37.487 -18.325 15.451  1.00 26.81  ? 741  PHE   A CB   1 
ATOM   1905 C  CG   . PHE   A 1 223 ? -36.490 -17.490 16.206  1.00 32.00  ? 741  PHE   A CG   1 
ATOM   1906 C  CD1  . PHE   A 1 223 ? -35.560 -16.707 15.528  1.00 34.01  ? 741  PHE   A CD1  1 
ATOM   1907 C  CD2  . PHE   A 1 223 ? -36.482 -17.484 17.599  1.00 26.89  ? 741  PHE   A CD2  1 
ATOM   1908 C  CE1  . PHE   A 1 223 ? -34.624 -15.909 16.241  1.00 30.79  ? 741  PHE   A CE1  1 
ATOM   1909 C  CE2  . PHE   A 1 223 ? -35.559 -16.703 18.313  1.00 27.55  ? 741  PHE   A CE2  1 
ATOM   1910 C  CZ   . PHE   A 1 223 ? -34.636 -15.915 17.643  1.00 28.71  ? 741  PHE   A CZ   1 
ATOM   1911 N  N    . VAL   A 1 224 ? -40.324 -18.790 13.723  1.00 34.40  ? 742  VAL   A N    1 
ATOM   1912 C  CA   . VAL   A 1 224 ? -40.912 -19.912 12.989  1.00 28.93  ? 742  VAL   A CA   1 
ATOM   1913 C  C    . VAL   A 1 224 ? -42.154 -19.592 12.171  1.00 43.72  ? 742  VAL   A C    1 
ATOM   1914 O  O    . VAL   A 1 224 ? -42.205 -19.879 10.971  1.00 46.23  ? 742  VAL   A O    1 
ATOM   1915 C  CB   . VAL   A 1 224 ? -41.278 -21.057 13.940  1.00 26.39  ? 742  VAL   A CB   1 
ATOM   1916 C  CG1  . VAL   A 1 224 ? -41.971 -22.220 13.154  1.00 28.19  ? 742  VAL   A CG1  1 
ATOM   1917 C  CG2  . VAL   A 1 224 ? -40.037 -21.538 14.652  1.00 31.67  ? 742  VAL   A CG2  1 
ATOM   1918 N  N    . ASN   A 1 225 ? -43.149 -19.013 12.838  1.00 45.55  ? 743  ASN   A N    1 
ATOM   1919 C  CA   . ASN   A 1 225 ? -44.501 -18.894 12.307  1.00 43.45  ? 743  ASN   A CA   1 
ATOM   1920 C  C    . ASN   A 1 225 ? -44.554 -18.325 10.909  1.00 39.53  ? 743  ASN   A C    1 
ATOM   1921 O  O    . ASN   A 1 225 ? -45.274 -18.821 10.061  1.00 39.96  ? 743  ASN   A O    1 
ATOM   1922 C  CB   . ASN   A 1 225 ? -45.363 -18.010 13.232  1.00 39.26  ? 743  ASN   A CB   1 
ATOM   1923 C  CG   . ASN   A 1 225 ? -45.907 -18.764 14.417  1.00 40.60  ? 743  ASN   A CG   1 
ATOM   1924 O  OD1  . ASN   A 1 225 ? -45.816 -19.995 14.496  1.00 41.56  ? 743  ASN   A OD1  1 
ATOM   1925 N  ND2  . ASN   A 1 225 ? -46.509 -18.035 15.332  1.00 42.19  ? 743  ASN   A ND2  1 
ATOM   1926 N  N    . ARG   A 1 226 ? -43.806 -17.258 10.680  1.00 41.55  ? 744  ARG   A N    1 
ATOM   1927 C  CA   . ARG   A 1 226 ? -43.967 -16.516 9.445   1.00 35.42  ? 744  ARG   A CA   1 
ATOM   1928 C  C    . ARG   A 1 226 ? -43.090 -17.057 8.302   1.00 39.47  ? 744  ARG   A C    1 
ATOM   1929 O  O    . ARG   A 1 226 ? -43.203 -16.588 7.180   1.00 32.17  ? 744  ARG   A O    1 
ATOM   1930 C  CB   . ARG   A 1 226 ? -43.667 -15.037 9.687   1.00 37.07  ? 744  ARG   A CB   1 
ATOM   1931 C  CG   . ARG   A 1 226 ? -44.748 -14.278 10.440  1.00 43.14  ? 744  ARG   A CG   1 
ATOM   1932 C  CD   . ARG   A 1 226 ? -44.218 -12.931 10.897  1.00 41.72  ? 744  ARG   A CD   1 
ATOM   1933 N  NE   . ARG   A 1 226 ? -43.124 -13.092 11.859  1.00 39.00  ? 744  ARG   A NE   1 
ATOM   1934 C  CZ   . ARG   A 1 226 ? -42.271 -12.128 12.194  1.00 43.13  ? 744  ARG   A CZ   1 
ATOM   1935 N  NH1  . ARG   A 1 226 ? -42.383 -10.921 11.652  1.00 47.40  ? 744  ARG   A NH1  1 
ATOM   1936 N  NH2  . ARG   A 1 226 ? -41.299 -12.372 13.069  1.00 41.89  ? 744  ARG   A NH2  1 
ATOM   1937 N  N    . ILE   A 1 227 ? -42.238 -18.041 8.585   1.00 38.95  ? 745  ILE   A N    1 
ATOM   1938 C  CA   . ILE   A 1 227 ? -41.261 -18.513 7.591   1.00 40.61  ? 745  ILE   A CA   1 
ATOM   1939 C  C    . ILE   A 1 227 ? -41.332 -20.045 7.366   1.00 37.98  ? 745  ILE   A C    1 
ATOM   1940 O  O    . ILE   A 1 227 ? -40.410 -20.656 6.812   1.00 35.82  ? 745  ILE   A O    1 
ATOM   1941 C  CB   . ILE   A 1 227 ? -39.795 -18.080 7.990   1.00 28.06  ? 745  ILE   A CB   1 
ATOM   1942 C  CG1  . ILE   A 1 227 ? -39.407 -18.522 9.414   1.00 25.03  ? 745  ILE   A CG1  1 
ATOM   1943 C  CG2  . ILE   A 1 227 ? -39.653 -16.575 7.927   1.00 31.51  ? 745  ILE   A CG2  1 
ATOM   1944 C  CD1  . ILE   A 1 227 ? -39.210 -20.028 9.620   1.00 24.75  ? 745  ILE   A CD1  1 
ATOM   1945 N  N    . GLN   A 1 228 ? -42.430 -20.649 7.804   1.00 35.27  ? 746  GLN   A N    1 
ATOM   1946 C  CA   . GLN   A 1 228 ? -42.634 -22.090 7.701   1.00 34.91  ? 746  GLN   A CA   1 
ATOM   1947 C  C    . GLN   A 1 228 ? -42.548 -22.637 6.272   1.00 34.03  ? 746  GLN   A C    1 
ATOM   1948 O  O    . GLN   A 1 228 ? -41.886 -23.638 6.034   1.00 36.76  ? 746  GLN   A O    1 
ATOM   1949 C  CB   . GLN   A 1 228 ? -44.003 -22.470 8.292   1.00 41.32  ? 746  GLN   A CB   1 
ATOM   1950 C  CG   . GLN   A 1 228 ? -44.009 -22.562 9.798   1.00 47.88  ? 746  GLN   A CG   1 
ATOM   1951 C  CD   . GLN   A 1 228 ? -45.408 -22.688 10.385  1.00 63.80  ? 746  GLN   A CD   1 
ATOM   1952 O  OE1  . GLN   A 1 228 ? -46.407 -22.540 9.676   1.00 67.38  ? 746  GLN   A OE1  1 
ATOM   1953 N  NE2  . GLN   A 1 228 ? -45.484 -22.952 11.693  1.00 64.30  ? 746  GLN   A NE2  1 
ATOM   1954 N  N    . LYS   A 1 229 ? -43.230 -21.990 5.331   1.00 30.09  ? 747  LYS   A N    1 
ATOM   1955 C  CA   . LYS   A 1 229 ? -43.234 -22.450 3.941   1.00 33.08  ? 747  LYS   A CA   1 
ATOM   1956 C  C    . LYS   A 1 229 ? -41.841 -22.289 3.309   1.00 30.21  ? 747  LYS   A C    1 
ATOM   1957 O  O    . LYS   A 1 229 ? -41.296 -23.240 2.728   1.00 30.99  ? 747  LYS   A O    1 
ATOM   1958 C  CB   . LYS   A 1 229 ? -44.322 -21.711 3.152   1.00 33.05  ? 747  LYS   A CB   1 
ATOM   1959 C  CG   . LYS   A 1 229 ? -45.697 -22.390 3.282   1.00 49.09  ? 747  LYS   A CG   1 
ATOM   1960 C  CD   . LYS   A 1 229 ? -45.632 -23.826 2.707   1.00 63.05  ? 747  LYS   A CD   1 
ATOM   1961 C  CE   . LYS   A 1 229 ? -46.730 -24.780 3.220   1.00 62.44  ? 747  LYS   A CE   1 
ATOM   1962 N  NZ   . LYS   A 1 229 ? -48.124 -24.386 2.868   1.00 66.37  ? 747  LYS   A NZ   1 
ATOM   1963 N  N    . GLN   A 1 230 ? -41.239 -21.118 3.495   1.00 30.21  ? 748  GLN   A N    1 
ATOM   1964 C  CA   . GLN   A 1 230 ? -39.853 -20.878 3.077   1.00 26.91  ? 748  GLN   A CA   1 
ATOM   1965 C  C    . GLN   A 1 230 ? -38.873 -21.946 3.556   1.00 32.11  ? 748  GLN   A C    1 
ATOM   1966 O  O    . GLN   A 1 230 ? -38.083 -22.494 2.768   1.00 26.03  ? 748  GLN   A O    1 
ATOM   1967 C  CB   . GLN   A 1 230 ? -39.376 -19.506 3.576   1.00 31.84  ? 748  GLN   A CB   1 
ATOM   1968 C  CG   . GLN   A 1 230 ? -40.146 -18.345 2.935   1.00 34.03  ? 748  GLN   A CG   1 
ATOM   1969 C  CD   . GLN   A 1 230 ? -41.229 -17.836 3.839   1.00 36.13  ? 748  GLN   A CD   1 
ATOM   1970 O  OE1  . GLN   A 1 230 ? -41.854 -18.616 4.553   1.00 34.05  ? 748  GLN   A OE1  1 
ATOM   1971 N  NE2  . GLN   A 1 230 ? -41.437 -16.513 3.844   1.00 31.55  ? 748  GLN   A NE2  1 
ATOM   1972 N  N    . MET   A 1 231 ? -38.904 -22.223 4.855   1.00 27.11  ? 749  MET   A N    1 
ATOM   1973 C  CA   . MET   A 1 231 ? -37.975 -23.189 5.429   1.00 23.35  ? 749  MET   A CA   1 
ATOM   1974 C  C    . MET   A 1 231 ? -38.309 -24.595 4.952   1.00 26.44  ? 749  MET   A C    1 
ATOM   1975 O  O    . MET   A 1 231 ? -37.422 -25.417 4.760   1.00 31.71  ? 749  MET   A O    1 
ATOM   1976 C  CB   . MET   A 1 231 ? -37.997 -23.151 6.959   1.00 30.07  ? 749  MET   A CB   1 
ATOM   1977 C  CG   . MET   A 1 231 ? -36.958 -24.074 7.590   1.00 36.24  ? 749  MET   A CG   1 
ATOM   1978 S  SD   . MET   A 1 231 ? -35.288 -23.443 7.302   1.00 46.32  ? 749  MET   A SD   1 
ATOM   1979 C  CE   . MET   A 1 231 ? -34.326 -24.680 8.122   1.00 49.16  ? 749  MET   A CE   1 
ATOM   1980 N  N    . ALA   A 1 232 ? -39.601 -24.863 4.785   1.00 30.01  ? 750  ALA   A N    1 
ATOM   1981 C  CA   . ALA   A 1 232 ? -40.043 -26.141 4.278   1.00 27.37  ? 750  ALA   A CA   1 
ATOM   1982 C  C    . ALA   A 1 232 ? -39.467 -26.346 2.886   1.00 34.35  ? 750  ALA   A C    1 
ATOM   1983 O  O    . ALA   A 1 232 ? -39.039 -27.444 2.540   1.00 31.60  ? 750  ALA   A O    1 
ATOM   1984 C  CB   . ALA   A 1 232 ? -41.562 -26.216 4.256   1.00 26.29  ? 750  ALA   A CB   1 
ATOM   1985 N  N    . ALA   A 1 233 ? -39.451 -25.281 2.087   1.00 29.22  ? 751  ALA   A N    1 
ATOM   1986 C  CA   . ALA   A 1 233 ? -38.953 -25.381 0.711   1.00 23.08  ? 751  ALA   A CA   1 
ATOM   1987 C  C    . ALA   A 1 233 ? -37.432 -25.582 0.689   1.00 30.30  ? 751  ALA   A C    1 
ATOM   1988 O  O    . ALA   A 1 233 ? -36.909 -26.346 -0.120  1.00 31.88  ? 751  ALA   A O    1 
ATOM   1989 C  CB   . ALA   A 1 233 ? -39.348 -24.132 -0.093  1.00 22.28  ? 751  ALA   A CB   1 
ATOM   1990 N  N    . PHE   A 1 234 ? -36.733 -24.895 1.590   1.00 31.64  ? 752  PHE   A N    1 
ATOM   1991 C  CA   . PHE   A 1 234 ? -35.285 -25.028 1.718   1.00 29.76  ? 752  PHE   A CA   1 
ATOM   1992 C  C    . PHE   A 1 234 ? -34.943 -26.457 2.138   1.00 31.79  ? 752  PHE   A C    1 
ATOM   1993 O  O    . PHE   A 1 234 ? -34.064 -27.091 1.564   1.00 26.21  ? 752  PHE   A O    1 
ATOM   1994 C  CB   . PHE   A 1 234 ? -34.735 -24.019 2.732   1.00 24.53  ? 752  PHE   A CB   1 
ATOM   1995 C  CG   . PHE   A 1 234 ? -33.268 -24.199 3.049   1.00 26.06  ? 752  PHE   A CG   1 
ATOM   1996 C  CD1  . PHE   A 1 234 ? -32.302 -23.504 2.330   1.00 26.61  ? 752  PHE   A CD1  1 
ATOM   1997 C  CD2  . PHE   A 1 234 ? -32.858 -25.043 4.069   1.00 24.06  ? 752  PHE   A CD2  1 
ATOM   1998 C  CE1  . PHE   A 1 234 ? -30.956 -23.656 2.610   1.00 27.74  ? 752  PHE   A CE1  1 
ATOM   1999 C  CE2  . PHE   A 1 234 ? -31.494 -25.195 4.371   1.00 26.58  ? 752  PHE   A CE2  1 
ATOM   2000 C  CZ   . PHE   A 1 234 ? -30.553 -24.505 3.635   1.00 33.02  ? 752  PHE   A CZ   1 
ATOM   2001 N  N    . LYS   A 1 235 ? -35.639 -26.958 3.155   1.00 27.66  ? 753  LYS   A N    1 
ATOM   2002 C  CA   . LYS   A 1 235 ? -35.383 -28.315 3.617   1.00 28.54  ? 753  LYS   A CA   1 
ATOM   2003 C  C    . LYS   A 1 235 ? -35.652 -29.347 2.517   1.00 33.83  ? 753  LYS   A C    1 
ATOM   2004 O  O    . LYS   A 1 235 ? -34.891 -30.313 2.347   1.00 34.38  ? 753  LYS   A O    1 
ATOM   2005 C  CB   . LYS   A 1 235 ? -36.209 -28.590 4.871   1.00 27.87  ? 753  LYS   A CB   1 
ATOM   2006 C  CG   . LYS   A 1 235 ? -35.644 -27.824 6.083   1.00 26.67  ? 753  LYS   A CG   1 
ATOM   2007 C  CD   . LYS   A 1 235 ? -36.628 -27.805 7.237   1.00 37.95  ? 753  LYS   A CD   1 
ATOM   2008 C  CE   . LYS   A 1 235 ? -36.687 -29.150 7.925   1.00 43.57  ? 753  LYS   A CE   1 
ATOM   2009 N  NZ   . LYS   A 1 235 ? -37.459 -29.047 9.200   1.00 50.02  ? 753  LYS   A NZ   1 
ATOM   2010 N  N    . GLU   A 1 236 ? -36.711 -29.127 1.744   1.00 31.85  ? 754  GLU   A N    1 
ATOM   2011 C  CA   . GLU   A 1 236 ? -37.009 -30.029 0.642   1.00 30.21  ? 754  GLU   A CA   1 
ATOM   2012 C  C    . GLU   A 1 236 ? -35.812 -30.147 -0.303  1.00 30.96  ? 754  GLU   A C    1 
ATOM   2013 O  O    . GLU   A 1 236 ? -35.383 -31.252 -0.638  1.00 34.86  ? 754  GLU   A O    1 
ATOM   2014 C  CB   . GLU   A 1 236 ? -38.251 -29.559 -0.118  1.00 32.73  ? 754  GLU   A CB   1 
ATOM   2015 C  CG   . GLU   A 1 236 ? -38.643 -30.510 -1.213  1.00 40.23  ? 754  GLU   A CG   1 
ATOM   2016 C  CD   . GLU   A 1 236 ? -40.059 -30.295 -1.682  1.00 58.10  ? 754  GLU   A CD   1 
ATOM   2017 O  OE1  . GLU   A 1 236 ? -40.257 -29.589 -2.699  1.00 68.26  ? 754  GLU   A OE1  1 
ATOM   2018 O  OE2  . GLU   A 1 236 ? -40.975 -30.833 -1.023  1.00 64.13  ? 754  GLU   A OE2  1 
ATOM   2019 N  N    . GLY   A 1 237 ? -35.248 -29.007 -0.698  1.00 32.81  ? 755  GLY   A N    1 
ATOM   2020 C  CA   . GLY   A 1 237 ? -34.125 -29.008 -1.612  1.00 26.14  ? 755  GLY   A CA   1 
ATOM   2021 C  C    . GLY   A 1 237 ? -32.912 -29.657 -0.962  1.00 29.27  ? 755  GLY   A C    1 
ATOM   2022 O  O    . GLY   A 1 237 ? -32.200 -30.443 -1.592  1.00 28.06  ? 755  GLY   A O    1 
ATOM   2023 N  N    . PHE   A 1 238 ? -32.685 -29.321 0.303   1.00 25.51  ? 756  PHE   A N    1 
ATOM   2024 C  CA   . PHE   A 1 238 ? -31.509 -29.801 1.028   1.00 28.52  ? 756  PHE   A CA   1 
ATOM   2025 C  C    . PHE   A 1 238 ? -31.558 -31.322 1.137   1.00 28.69  ? 756  PHE   A C    1 
ATOM   2026 O  O    . PHE   A 1 238 ? -30.563 -32.006 0.903   1.00 32.75  ? 756  PHE   A O    1 
ATOM   2027 C  CB   . PHE   A 1 238 ? -31.421 -29.171 2.435   1.00 28.28  ? 756  PHE   A CB   1 
ATOM   2028 C  CG   . PHE   A 1 238 ? -30.141 -29.510 3.182   1.00 26.49  ? 756  PHE   A CG   1 
ATOM   2029 C  CD1  . PHE   A 1 238 ? -28.957 -28.852 2.894   1.00 25.46  ? 756  PHE   A CD1  1 
ATOM   2030 C  CD2  . PHE   A 1 238 ? -30.129 -30.494 4.164   1.00 30.01  ? 756  PHE   A CD2  1 
ATOM   2031 C  CE1  . PHE   A 1 238 ? -27.764 -29.168 3.578   1.00 26.05  ? 756  PHE   A CE1  1 
ATOM   2032 C  CE2  . PHE   A 1 238 ? -28.952 -30.816 4.853   1.00 31.67  ? 756  PHE   A CE2  1 
ATOM   2033 C  CZ   . PHE   A 1 238 ? -27.764 -30.154 4.551   1.00 24.09  ? 756  PHE   A CZ   1 
ATOM   2034 N  N    . PHE   A 1 239 ? -32.730 -31.844 1.480   1.00 25.63  ? 757  PHE   A N    1 
ATOM   2035 C  CA   . PHE   A 1 239 ? -32.871 -33.276 1.729   1.00 28.63  ? 757  PHE   A CA   1 
ATOM   2036 C  C    . PHE   A 1 239 ? -32.871 -34.096 0.441   1.00 32.81  ? 757  PHE   A C    1 
ATOM   2037 O  O    . PHE   A 1 239 ? -32.730 -35.312 0.482   1.00 42.83  ? 757  PHE   A O    1 
ATOM   2038 C  CB   . PHE   A 1 239 ? -34.130 -33.544 2.541   1.00 26.69  ? 757  PHE   A CB   1 
ATOM   2039 C  CG   . PHE   A 1 239 ? -34.089 -32.948 3.934   1.00 31.37  ? 757  PHE   A CG   1 
ATOM   2040 C  CD1  . PHE   A 1 239 ? -32.903 -32.900 4.645   1.00 32.92  ? 757  PHE   A CD1  1 
ATOM   2041 C  CD2  . PHE   A 1 239 ? -35.233 -32.445 4.525   1.00 35.40  ? 757  PHE   A CD2  1 
ATOM   2042 C  CE1  . PHE   A 1 239 ? -32.857 -32.368 5.926   1.00 31.67  ? 757  PHE   A CE1  1 
ATOM   2043 C  CE2  . PHE   A 1 239 ? -35.191 -31.904 5.798   1.00 37.99  ? 757  PHE   A CE2  1 
ATOM   2044 C  CZ   . PHE   A 1 239 ? -33.997 -31.873 6.498   1.00 32.92  ? 757  PHE   A CZ   1 
ATOM   2045 N  N    . GLU   A 1 240 ? -32.979 -33.433 -0.704  1.00 30.68  ? 758  GLU   A N    1 
ATOM   2046 C  CA   . GLU   A 1 240 ? -32.832 -34.125 -1.978  1.00 35.82  ? 758  GLU   A CA   1 
ATOM   2047 C  C    . GLU   A 1 240 ? -31.369 -34.512 -2.185  1.00 40.25  ? 758  GLU   A C    1 
ATOM   2048 O  O    . GLU   A 1 240 ? -31.057 -35.435 -2.924  1.00 34.32  ? 758  GLU   A O    1 
ATOM   2049 C  CB   . GLU   A 1 240 ? -33.347 -33.259 -3.146  1.00 25.52  ? 758  GLU   A CB   1 
ATOM   2050 C  CG   . GLU   A 1 240 ? -34.892 -33.274 -3.259  1.00 33.46  ? 758  GLU   A CG   1 
ATOM   2051 C  CD   . GLU   A 1 240 ? -35.427 -32.282 -4.298  1.00 43.94  ? 758  GLU   A CD   1 
ATOM   2052 O  OE1  . GLU   A 1 240 ? -34.735 -31.291 -4.606  1.00 41.74  ? 758  GLU   A OE1  1 
ATOM   2053 O  OE2  . GLU   A 1 240 ? -36.548 -32.486 -4.794  1.00 44.16  ? 758  GLU   A OE2  1 
ATOM   2054 N  N    . LEU   A 1 241 ? -30.468 -33.814 -1.507  1.00 35.99  ? 759  LEU   A N    1 
ATOM   2055 C  CA   . LEU   A 1 241 ? -29.060 -34.176 -1.574  1.00 35.55  ? 759  LEU   A CA   1 
ATOM   2056 C  C    . LEU   A 1 241 ? -28.571 -34.935 -0.354  1.00 28.55  ? 759  LEU   A C    1 
ATOM   2057 O  O    . LEU   A 1 241 ? -27.777 -35.857 -0.465  1.00 36.69  ? 759  LEU   A O    1 
ATOM   2058 C  CB   . LEU   A 1 241 ? -28.214 -32.928 -1.782  1.00 36.43  ? 759  LEU   A CB   1 
ATOM   2059 C  CG   . LEU   A 1 241 ? -28.226 -32.762 -3.294  1.00 38.64  ? 759  LEU   A CG   1 
ATOM   2060 C  CD1  . LEU   A 1 241 ? -29.265 -31.738 -3.754  1.00 28.55  ? 759  LEU   A CD1  1 
ATOM   2061 C  CD2  . LEU   A 1 241 ? -26.876 -32.493 -3.792  1.00 42.17  ? 759  LEU   A CD2  1 
ATOM   2062 N  N    . ILE   A 1 242 ? -29.035 -34.529 0.814   1.00 29.10  ? 760  ILE   A N    1 
ATOM   2063 C  CA   . ILE   A 1 242 ? -28.559 -35.133 2.053   1.00 32.22  ? 760  ILE   A CA   1 
ATOM   2064 C  C    . ILE   A 1 242 ? -29.777 -35.700 2.772   1.00 32.38  ? 760  ILE   A C    1 
ATOM   2065 O  O    . ILE   A 1 242 ? -30.633 -34.936 3.216   1.00 39.55  ? 760  ILE   A O    1 
ATOM   2066 C  CB   . ILE   A 1 242 ? -27.831 -34.101 2.975   1.00 33.01  ? 760  ILE   A CB   1 
ATOM   2067 C  CG1  . ILE   A 1 242 ? -26.781 -33.260 2.199   1.00 27.27  ? 760  ILE   A CG1  1 
ATOM   2068 C  CG2  . ILE   A 1 242 ? -27.230 -34.802 4.209   1.00 43.74  ? 760  ILE   A CG2  1 
ATOM   2069 C  CD1  . ILE   A 1 242 ? -25.522 -34.039 1.751   1.00 39.25  ? 760  ILE   A CD1  1 
ATOM   2070 N  N    . PRO   A 1 243 ? -29.874 -37.032 2.862   1.00 37.92  ? 761  PRO   A N    1 
ATOM   2071 C  CA   . PRO   A 1 243 ? -30.963 -37.661 3.619   1.00 41.99  ? 761  PRO   A CA   1 
ATOM   2072 C  C    . PRO   A 1 243 ? -31.125 -37.030 4.993   1.00 39.89  ? 761  PRO   A C    1 
ATOM   2073 O  O    . PRO   A 1 243 ? -30.146 -36.825 5.705   1.00 43.64  ? 761  PRO   A O    1 
ATOM   2074 C  CB   . PRO   A 1 243 ? -30.515 -39.110 3.732   1.00 39.28  ? 761  PRO   A CB   1 
ATOM   2075 C  CG   . PRO   A 1 243 ? -29.685 -39.319 2.517   1.00 47.20  ? 761  PRO   A CG   1 
ATOM   2076 C  CD   . PRO   A 1 243 ? -28.946 -38.029 2.304   1.00 39.50  ? 761  PRO   A CD   1 
ATOM   2077 N  N    . GLN   A 1 244 ? -32.355 -36.702 5.346   1.00 33.89  ? 762  GLN   A N    1 
ATOM   2078 C  CA   . GLN   A 1 244 ? -32.607 -35.955 6.556   1.00 38.47  ? 762  GLN   A CA   1 
ATOM   2079 C  C    . GLN   A 1 244 ? -32.168 -36.746 7.789   1.00 41.83  ? 762  GLN   A C    1 
ATOM   2080 O  O    . GLN   A 1 244 ? -31.714 -36.185 8.788   1.00 44.37  ? 762  GLN   A O    1 
ATOM   2081 C  CB   . GLN   A 1 244 ? -34.088 -35.589 6.617   1.00 28.79  ? 762  GLN   A CB   1 
ATOM   2082 C  CG   . GLN   A 1 244 ? -34.694 -35.674 7.965   1.00 42.67  ? 762  GLN   A CG   1 
ATOM   2083 C  CD   . GLN   A 1 244 ? -35.964 -34.861 8.058   1.00 45.06  ? 762  GLN   A CD   1 
ATOM   2084 O  OE1  . GLN   A 1 244 ? -36.168 -34.120 9.022   1.00 49.41  ? 762  GLN   A OE1  1 
ATOM   2085 N  NE2  . GLN   A 1 244 ? -36.811 -34.970 7.038   1.00 38.82  ? 762  GLN   A NE2  1 
ATOM   2086 N  N    . ASP   A 1 245 ? -32.281 -38.058 7.697   1.00 40.57  ? 763  ASP   A N    1 
ATOM   2087 C  CA   . ASP   A 1 245 ? -31.887 -38.947 8.787   1.00 53.79  ? 763  ASP   A CA   1 
ATOM   2088 C  C    . ASP   A 1 245 ? -30.378 -38.938 9.019   1.00 52.76  ? 763  ASP   A C    1 
ATOM   2089 O  O    . ASP   A 1 245 ? -29.921 -39.048 10.149  1.00 59.29  ? 763  ASP   A O    1 
ATOM   2090 C  CB   . ASP   A 1 245 ? -32.368 -40.367 8.498   1.00 59.24  ? 763  ASP   A CB   1 
ATOM   2091 C  CG   . ASP   A 1 245 ? -33.873 -40.518 8.686   1.00 75.47  ? 763  ASP   A CG   1 
ATOM   2092 O  OD1  . ASP   A 1 245 ? -34.444 -39.790 9.532   1.00 74.65  ? 763  ASP   A OD1  1 
ATOM   2093 O  OD2  . ASP   A 1 245 ? -34.484 -41.362 7.988   1.00 81.97  ? 763  ASP   A OD2  1 
ATOM   2094 N  N    . LEU   A 1 246 ? -29.615 -38.802 7.940   1.00 41.57  ? 764  LEU   A N    1 
ATOM   2095 C  CA   . LEU   A 1 246 ? -28.164 -38.703 8.025   1.00 35.22  ? 764  LEU   A CA   1 
ATOM   2096 C  C    . LEU   A 1 246 ? -27.723 -37.398 8.671   1.00 38.76  ? 764  LEU   A C    1 
ATOM   2097 O  O    . LEU   A 1 246 ? -26.774 -37.370 9.434   1.00 37.39  ? 764  LEU   A O    1 
ATOM   2098 C  CB   . LEU   A 1 246 ? -27.537 -38.805 6.633   1.00 43.21  ? 764  LEU   A CB   1 
ATOM   2099 C  CG   . LEU   A 1 246 ? -26.890 -40.154 6.343   1.00 44.01  ? 764  LEU   A CG   1 
ATOM   2100 C  CD1  . LEU   A 1 246 ? -27.881 -41.247 6.631   1.00 35.28  ? 764  LEU   A CD1  1 
ATOM   2101 C  CD2  . LEU   A 1 246 ? -26.416 -40.210 4.907   1.00 44.28  ? 764  LEU   A CD2  1 
ATOM   2102 N  N    . ILE   A 1 247 ? -28.391 -36.305 8.344   1.00 36.12  ? 765  ILE   A N    1 
ATOM   2103 C  CA   . ILE   A 1 247 ? -27.940 -35.017 8.863   1.00 40.60  ? 765  ILE   A CA   1 
ATOM   2104 C  C    . ILE   A 1 247 ? -28.208 -34.952 10.378  1.00 47.65  ? 765  ILE   A C    1 
ATOM   2105 O  O    . ILE   A 1 247 ? -27.540 -34.226 11.104  1.00 43.84  ? 765  ILE   A O    1 
ATOM   2106 C  CB   . ILE   A 1 247 ? -28.605 -33.836 8.114   1.00 31.39  ? 765  ILE   A CB   1 
ATOM   2107 C  CG1  . ILE   A 1 247 ? -27.706 -32.601 8.173   1.00 39.12  ? 765  ILE   A CG1  1 
ATOM   2108 C  CG2  . ILE   A 1 247 ? -30.016 -33.529 8.630   1.00 33.25  ? 765  ILE   A CG2  1 
ATOM   2109 C  CD1  . ILE   A 1 247 ? -26.416 -32.741 7.410   1.00 38.05  ? 765  ILE   A CD1  1 
ATOM   2110 N  N    . LYS   A 1 248 ? -29.148 -35.771 10.846  1.00 53.89  ? 766  LYS   A N    1 
ATOM   2111 C  CA   . LYS   A 1 248 ? -29.517 -35.836 12.259  1.00 50.51  ? 766  LYS   A CA   1 
ATOM   2112 C  C    . LYS   A 1 248 ? -28.402 -36.346 13.185  1.00 46.10  ? 766  LYS   A C    1 
ATOM   2113 O  O    . LYS   A 1 248 ? -28.549 -36.306 14.398  1.00 41.79  ? 766  LYS   A O    1 
ATOM   2114 C  CB   . LYS   A 1 248 ? -30.747 -36.744 12.451  1.00 60.15  ? 766  LYS   A CB   1 
ATOM   2115 C  CG   . LYS   A 1 248 ? -32.076 -36.243 11.867  1.00 60.70  ? 766  LYS   A CG   1 
ATOM   2116 C  CD   . LYS   A 1 248 ? -32.635 -35.049 12.613  1.00 56.17  ? 766  LYS   A CD   1 
ATOM   2117 C  CE   . LYS   A 1 248 ? -34.158 -35.150 12.759  1.00 60.70  ? 766  LYS   A CE   1 
ATOM   2118 N  NZ   . LYS   A 1 248 ? -34.895 -35.339 11.481  1.00 60.12  ? 766  LYS   A NZ   1 
ATOM   2119 N  N    . ILE   A 1 249 ? -27.293 -36.850 12.657  1.00 43.18  ? 767  ILE   A N    1 
ATOM   2120 C  CA   . ILE   A 1 249 ? -26.268 -37.290 13.597  1.00 44.54  ? 767  ILE   A CA   1 
ATOM   2121 C  C    . ILE   A 1 249 ? -25.543 -36.075 14.208  1.00 35.80  ? 767  ILE   A C    1 
ATOM   2122 O  O    . ILE   A 1 249 ? -24.879 -36.191 15.225  1.00 45.00  ? 767  ILE   A O    1 
ATOM   2123 C  CB   . ILE   A 1 249 ? -25.251 -38.243 12.951  1.00 50.26  ? 767  ILE   A CB   1 
ATOM   2124 C  CG1  . ILE   A 1 249 ? -24.148 -37.484 12.253  1.00 54.23  ? 767  ILE   A CG1  1 
ATOM   2125 C  CG2  . ILE   A 1 249 ? -25.928 -39.168 11.953  1.00 57.16  ? 767  ILE   A CG2  1 
ATOM   2126 C  CD1  . ILE   A 1 249 ? -23.115 -38.407 11.694  1.00 61.81  ? 767  ILE   A CD1  1 
ATOM   2127 N  N    . PHE   A 1 250 ? -25.704 -34.909 13.587  1.00 35.82  ? 768  PHE   A N    1 
ATOM   2128 C  CA   . PHE   A 1 250 ? -25.060 -33.674 14.034  1.00 40.65  ? 768  PHE   A CA   1 
ATOM   2129 C  C    . PHE   A 1 250 ? -25.977 -32.834 14.912  1.00 41.68  ? 768  PHE   A C    1 
ATOM   2130 O  O    . PHE   A 1 250 ? -27.187 -32.831 14.698  1.00 42.74  ? 768  PHE   A O    1 
ATOM   2131 C  CB   . PHE   A 1 250 ? -24.620 -32.851 12.825  1.00 33.16  ? 768  PHE   A CB   1 
ATOM   2132 C  CG   . PHE   A 1 250 ? -23.645 -33.571 11.933  1.00 38.18  ? 768  PHE   A CG   1 
ATOM   2133 C  CD1  . PHE   A 1 250 ? -22.361 -33.802 12.354  1.00 30.52  ? 768  PHE   A CD1  1 
ATOM   2134 C  CD2  . PHE   A 1 250 ? -24.021 -34.015 10.677  1.00 41.69  ? 768  PHE   A CD2  1 
ATOM   2135 C  CE1  . PHE   A 1 250 ? -21.445 -34.468 11.538  1.00 34.23  ? 768  PHE   A CE1  1 
ATOM   2136 C  CE2  . PHE   A 1 250 ? -23.114 -34.670 9.855   1.00 32.78  ? 768  PHE   A CE2  1 
ATOM   2137 C  CZ   . PHE   A 1 250 ? -21.828 -34.886 10.282  1.00 35.08  ? 768  PHE   A CZ   1 
ATOM   2138 N  N    . ASP   A 1 251 ? -25.417 -32.130 15.898  1.00 41.55  ? 769  ASP   A N    1 
ATOM   2139 C  CA   . ASP   A 1 251 ? -26.190 -31.096 16.586  1.00 38.10  ? 769  ASP   A CA   1 
ATOM   2140 C  C    . ASP   A 1 251 ? -26.040 -29.792 15.805  1.00 42.16  ? 769  ASP   A C    1 
ATOM   2141 O  O    . ASP   A 1 251 ? -25.424 -29.764 14.728  1.00 34.48  ? 769  ASP   A O    1 
ATOM   2142 C  CB   . ASP   A 1 251 ? -25.777 -30.927 18.061  1.00 40.95  ? 769  ASP   A CB   1 
ATOM   2143 C  CG   . ASP   A 1 251 ? -24.339 -30.474 18.247  1.00 43.83  ? 769  ASP   A CG   1 
ATOM   2144 O  OD1  . ASP   A 1 251 ? -23.800 -29.705 17.426  1.00 49.75  ? 769  ASP   A OD1  1 
ATOM   2145 O  OD2  . ASP   A 1 251 ? -23.745 -30.869 19.266  1.00 47.64  ? 769  ASP   A OD2  1 
ATOM   2146 N  N    . GLU   A 1 252 ? -26.588 -28.710 16.340  1.00 38.19  ? 770  GLU   A N    1 
ATOM   2147 C  CA   . GLU   A 1 252 ? -26.722 -27.495 15.541  1.00 37.18  ? 770  GLU   A CA   1 
ATOM   2148 C  C    . GLU   A 1 252 ? -25.387 -26.773 15.393  1.00 38.46  ? 770  GLU   A C    1 
ATOM   2149 O  O    . GLU   A 1 252 ? -25.179 -26.073 14.416  1.00 39.74  ? 770  GLU   A O    1 
ATOM   2150 C  CB   . GLU   A 1 252 ? -27.776 -26.560 16.140  1.00 43.58  ? 770  GLU   A CB   1 
ATOM   2151 C  CG   . GLU   A 1 252 ? -27.540 -26.173 17.597  1.00 44.11  ? 770  GLU   A CG   1 
ATOM   2152 C  CD   . GLU   A 1 252 ? -27.955 -27.249 18.578  1.00 52.80  ? 770  GLU   A CD   1 
ATOM   2153 O  OE1  . GLU   A 1 252 ? -28.960 -27.931 18.320  1.00 55.67  ? 770  GLU   A OE1  1 
ATOM   2154 O  OE2  . GLU   A 1 252 ? -27.277 -27.406 19.616  1.00 73.51  ? 770  GLU   A OE2  1 
ATOM   2155 N  N    . ASN   A 1 253 ? -24.475 -26.964 16.347  1.00 33.47  ? 771  ASN   A N    1 
ATOM   2156 C  CA   . ASN   A 1 253 ? -23.142 -26.377 16.234  1.00 36.07  ? 771  ASN   A CA   1 
ATOM   2157 C  C    . ASN   A 1 253 ? -22.285 -27.108 15.196  1.00 47.56  ? 771  ASN   A C    1 
ATOM   2158 O  O    . ASN   A 1 253 ? -21.538 -26.492 14.421  1.00 40.22  ? 771  ASN   A O    1 
ATOM   2159 C  CB   . ASN   A 1 253 ? -22.438 -26.379 17.593  1.00 44.30  ? 771  ASN   A CB   1 
ATOM   2160 C  CG   . ASN   A 1 253 ? -23.110 -25.449 18.598  1.00 52.40  ? 771  ASN   A CG   1 
ATOM   2161 O  OD1  . ASN   A 1 253 ? -23.738 -24.462 18.219  1.00 62.54  ? 771  ASN   A OD1  1 
ATOM   2162 N  ND2  . ASN   A 1 253 ? -22.982 -25.764 19.875  1.00 55.37  ? 771  ASN   A ND2  1 
ATOM   2163 N  N    . GLU   A 1 254 ? -22.409 -28.434 15.199  1.00 45.21  ? 772  GLU   A N    1 
ATOM   2164 C  CA   . GLU   A 1 254 ? -21.687 -29.290 14.277  1.00 39.53  ? 772  GLU   A CA   1 
ATOM   2165 C  C    . GLU   A 1 254 ? -22.186 -29.057 12.845  1.00 36.23  ? 772  GLU   A C    1 
ATOM   2166 O  O    . GLU   A 1 254 ? -21.396 -28.931 11.911  1.00 35.93  ? 772  GLU   A O    1 
ATOM   2167 C  CB   . GLU   A 1 254 ? -21.838 -30.762 14.704  1.00 38.25  ? 772  GLU   A CB   1 
ATOM   2168 C  CG   . GLU   A 1 254 ? -21.017 -31.100 15.931  1.00 39.75  ? 772  GLU   A CG   1 
ATOM   2169 C  CD   . GLU   A 1 254 ? -21.442 -32.384 16.631  1.00 48.36  ? 772  GLU   A CD   1 
ATOM   2170 O  OE1  . GLU   A 1 254 ? -22.577 -32.849 16.401  1.00 45.30  ? 772  GLU   A OE1  1 
ATOM   2171 O  OE2  . GLU   A 1 254 ? -20.630 -32.923 17.419  1.00 50.13  ? 772  GLU   A OE2  1 
ATOM   2172 N  N    . LEU   A 1 255 ? -23.498 -28.962 12.688  1.00 35.63  ? 773  LEU   A N    1 
ATOM   2173 C  CA   . LEU   A 1 255 ? -24.096 -28.722 11.385  1.00 36.83  ? 773  LEU   A CA   1 
ATOM   2174 C  C    . LEU   A 1 255 ? -23.630 -27.401 10.770  1.00 38.75  ? 773  LEU   A C    1 
ATOM   2175 O  O    . LEU   A 1 255 ? -23.344 -27.327 9.571   1.00 37.13  ? 773  LEU   A O    1 
ATOM   2176 C  CB   . LEU   A 1 255 ? -25.626 -28.743 11.492  1.00 32.33  ? 773  LEU   A CB   1 
ATOM   2177 C  CG   . LEU   A 1 255 ? -26.380 -28.454 10.195  1.00 35.44  ? 773  LEU   A CG   1 
ATOM   2178 C  CD1  . LEU   A 1 255 ? -25.893 -29.350 9.054   1.00 38.04  ? 773  LEU   A CD1  1 
ATOM   2179 C  CD2  . LEU   A 1 255 ? -27.890 -28.625 10.397  1.00 36.92  ? 773  LEU   A CD2  1 
ATOM   2180 N  N    . GLU   A 1 256 ? -23.563 -26.357 11.586  1.00 36.13  ? 774  GLU   A N    1 
ATOM   2181 C  CA   . GLU   A 1 256 ? -23.125 -25.047 11.106  1.00 39.69  ? 774  GLU   A CA   1 
ATOM   2182 C  C    . GLU   A 1 256 ? -21.666 -25.093 10.653  1.00 44.94  ? 774  GLU   A C    1 
ATOM   2183 O  O    . GLU   A 1 256 ? -21.290 -24.508 9.636   1.00 43.94  ? 774  GLU   A O    1 
ATOM   2184 C  CB   . GLU   A 1 256 ? -23.293 -23.984 12.196  1.00 35.95  ? 774  GLU   A CB   1 
ATOM   2185 C  CG   . GLU   A 1 256 ? -22.602 -22.662 11.861  1.00 44.67  ? 774  GLU   A CG   1 
ATOM   2186 C  CD   . GLU   A 1 256 ? -22.901 -21.547 12.866  1.00 53.71  ? 774  GLU   A CD   1 
ATOM   2187 O  OE1  . GLU   A 1 256 ? -23.093 -21.844 14.066  1.00 56.18  ? 774  GLU   A OE1  1 
ATOM   2188 O  OE2  . GLU   A 1 256 ? -22.951 -20.370 12.446  1.00 61.12  ? 774  GLU   A OE2  1 
ATOM   2189 N  N    . LEU   A 1 257 ? -20.845 -25.787 11.428  1.00 41.85  ? 775  LEU   A N    1 
ATOM   2190 C  CA   . LEU   A 1 257 ? -19.446 -25.949 11.086  1.00 45.61  ? 775  LEU   A CA   1 
ATOM   2191 C  C    . LEU   A 1 257 ? -19.341 -26.765 9.794   1.00 42.20  ? 775  LEU   A C    1 
ATOM   2192 O  O    . LEU   A 1 257 ? -18.573 -26.435 8.900   1.00 45.58  ? 775  LEU   A O    1 
ATOM   2193 C  CB   . LEU   A 1 257 ? -18.698 -26.625 12.232  1.00 51.52  ? 775  LEU   A CB   1 
ATOM   2194 C  CG   . LEU   A 1 257 ? -17.179 -26.725 12.154  1.00 56.56  ? 775  LEU   A CG   1 
ATOM   2195 C  CD1  . LEU   A 1 257 ? -16.550 -25.353 12.008  1.00 61.48  ? 775  LEU   A CD1  1 
ATOM   2196 C  CD2  . LEU   A 1 257 ? -16.660 -27.422 13.399  1.00 56.72  ? 775  LEU   A CD2  1 
ATOM   2197 N  N    . LEU   A 1 258 ? -20.146 -27.813 9.697   1.00 39.47  ? 776  LEU   A N    1 
ATOM   2198 C  CA   . LEU   A 1 258 ? -20.165 -28.656 8.509   1.00 51.42  ? 776  LEU   A CA   1 
ATOM   2199 C  C    . LEU   A 1 258 ? -20.510 -27.851 7.257   1.00 47.81  ? 776  LEU   A C    1 
ATOM   2200 O  O    . LEU   A 1 258 ? -19.797 -27.911 6.266   1.00 48.53  ? 776  LEU   A O    1 
ATOM   2201 C  CB   . LEU   A 1 258 ? -21.161 -29.811 8.689   1.00 53.48  ? 776  LEU   A CB   1 
ATOM   2202 C  CG   . LEU   A 1 258 ? -21.571 -30.611 7.447   1.00 55.94  ? 776  LEU   A CG   1 
ATOM   2203 C  CD1  . LEU   A 1 258 ? -20.375 -31.319 6.869   1.00 55.72  ? 776  LEU   A CD1  1 
ATOM   2204 C  CD2  . LEU   A 1 258 ? -22.658 -31.622 7.764   1.00 53.81  ? 776  LEU   A CD2  1 
ATOM   2205 N  N    . MET   A 1 259 ? -21.591 -27.083 7.313   1.00 38.80  ? 777  MET   A N    1 
ATOM   2206 C  CA   . MET   A 1 259 ? -22.093 -26.396 6.127   1.00 35.35  ? 777  MET   A CA   1 
ATOM   2207 C  C    . MET   A 1 259 ? -21.359 -25.114 5.766   1.00 38.97  ? 777  MET   A C    1 
ATOM   2208 O  O    . MET   A 1 259 ? -21.242 -24.767 4.595   1.00 46.12  ? 777  MET   A O    1 
ATOM   2209 C  CB   . MET   A 1 259 ? -23.561 -26.036 6.306   1.00 39.64  ? 777  MET   A CB   1 
ATOM   2210 C  CG   . MET   A 1 259 ? -24.483 -27.196 6.445   1.00 48.89  ? 777  MET   A CG   1 
ATOM   2211 S  SD   . MET   A 1 259 ? -26.165 -26.571 6.650   1.00 53.83  ? 777  MET   A SD   1 
ATOM   2212 C  CE   . MET   A 1 259 ? -26.383 -25.762 5.071   1.00 37.04  ? 777  MET   A CE   1 
ATOM   2213 N  N    . CYS   A 1 260 ? -20.918 -24.379 6.776   1.00 36.46  ? 778  CYS   A N    1 
ATOM   2214 C  CA   . CYS   A 1 260 ? -20.493 -23.012 6.543   1.00 38.76  ? 778  CYS   A CA   1 
ATOM   2215 C  C    . CYS   A 1 260 ? -19.111 -22.757 7.116   1.00 38.22  ? 778  CYS   A C    1 
ATOM   2216 O  O    . CYS   A 1 260 ? -18.539 -21.706 6.884   1.00 42.47  ? 778  CYS   A O    1 
ATOM   2217 C  CB   . CYS   A 1 260 ? -21.511 -22.037 7.138   1.00 39.66  ? 778  CYS   A CB   1 
ATOM   2218 S  SG   . CYS   A 1 260 ? -23.220 -22.337 6.608   1.00 55.96  ? 778  CYS   A SG   1 
ATOM   2219 N  N    . GLY   A 1 261 ? -18.580 -23.727 7.853   1.00 45.19  ? 779  GLY   A N    1 
ATOM   2220 C  CA   . GLY   A 1 261 ? -17.248 -23.609 8.434   1.00 50.73  ? 779  GLY   A CA   1 
ATOM   2221 C  C    . GLY   A 1 261 ? -17.120 -22.561 9.533   1.00 59.60  ? 779  GLY   A C    1 
ATOM   2222 O  O    . GLY   A 1 261 ? -16.019 -22.176 9.896   1.00 62.34  ? 779  GLY   A O    1 
ATOM   2223 N  N    . LEU   A 1 262 ? -18.241 -22.092 10.071  1.00 75.21  ? 780  LEU   A N    1 
ATOM   2224 C  CA   . LEU   A 1 262 ? -18.194 -21.028 11.072  1.00 81.71  ? 780  LEU   A CA   1 
ATOM   2225 C  C    . LEU   A 1 262 ? -18.503 -21.554 12.472  1.00 76.34  ? 780  LEU   A C    1 
ATOM   2226 O  O    . LEU   A 1 262 ? -19.263 -22.505 12.642  1.00 79.26  ? 780  LEU   A O    1 
ATOM   2227 C  CB   . LEU   A 1 262 ? -19.171 -19.900 10.714  1.00 87.44  ? 780  LEU   A CB   1 
ATOM   2228 C  CG   . LEU   A 1 262 ? -18.970 -18.617 11.533  1.00 98.70  ? 780  LEU   A CG   1 
ATOM   2229 C  CD1  . LEU   A 1 262 ? -18.028 -17.635 10.831  1.00 102.81 ? 780  LEU   A CD1  1 
ATOM   2230 C  CD2  . LEU   A 1 262 ? -20.284 -17.950 11.915  1.00 97.64  ? 780  LEU   A CD2  1 
ATOM   2231 N  N    . GLY   A 1 263 ? -17.907 -20.923 13.473  1.00 67.30  ? 781  GLY   A N    1 
ATOM   2232 C  CA   . GLY   A 1 263 ? -18.129 -21.304 14.852  1.00 64.49  ? 781  GLY   A CA   1 
ATOM   2233 C  C    . GLY   A 1 263 ? -17.370 -20.350 15.745  1.00 74.03  ? 781  GLY   A C    1 
ATOM   2234 O  O    . GLY   A 1 263 ? -16.628 -19.491 15.261  1.00 76.95  ? 781  GLY   A O    1 
ATOM   2235 N  N    . ASP   A 1 264 ? -17.552 -20.497 17.050  1.00 78.66  ? 782  ASP   A N    1 
ATOM   2236 C  CA   . ASP   A 1 264 ? -16.917 -19.589 17.989  1.00 88.45  ? 782  ASP   A CA   1 
ATOM   2237 C  C    . ASP   A 1 264 ? -15.473 -20.009 18.221  1.00 88.48  ? 782  ASP   A C    1 
ATOM   2238 O  O    . ASP   A 1 264 ? -15.199 -21.133 18.644  1.00 89.26  ? 782  ASP   A O    1 
ATOM   2239 C  CB   . ASP   A 1 264 ? -17.698 -19.549 19.302  1.00 94.72  ? 782  ASP   A CB   1 
ATOM   2240 C  CG   . ASP   A 1 264 ? -19.060 -18.890 19.143  1.00 103.00 ? 782  ASP   A CG   1 
ATOM   2241 O  OD1  . ASP   A 1 264 ? -19.279 -18.196 18.124  1.00 101.89 ? 782  ASP   A OD1  1 
ATOM   2242 O  OD2  . ASP   A 1 264 ? -19.922 -19.084 20.024  1.00 109.82 ? 782  ASP   A OD2  1 
ATOM   2243 N  N    . VAL   A 1 265 ? -14.554 -19.099 17.921  1.00 81.38  ? 783  VAL   A N    1 
ATOM   2244 C  CA   . VAL   A 1 265 ? -13.132 -19.356 18.086  1.00 71.28  ? 783  VAL   A CA   1 
ATOM   2245 C  C    . VAL   A 1 265 ? -12.679 -19.003 19.496  1.00 69.97  ? 783  VAL   A C    1 
ATOM   2246 O  O    . VAL   A 1 265 ? -12.801 -17.854 19.927  1.00 68.88  ? 783  VAL   A O    1 
ATOM   2247 C  CB   . VAL   A 1 265 ? -12.302 -18.557 17.063  1.00 67.06  ? 783  VAL   A CB   1 
ATOM   2248 C  CG1  . VAL   A 1 265 ? -10.820 -18.820 17.255  1.00 61.85  ? 783  VAL   A CG1  1 
ATOM   2249 C  CG2  . VAL   A 1 265 ? -12.735 -18.908 15.655  1.00 60.29  ? 783  VAL   A CG2  1 
ATOM   2250 N  N    . ASP   A 1 266 ? -12.163 -19.993 20.217  1.00 64.87  ? 784  ASP   A N    1 
ATOM   2251 C  CA   . ASP   A 1 266 ? -11.677 -19.755 21.569  1.00 73.90  ? 784  ASP   A CA   1 
ATOM   2252 C  C    . ASP   A 1 266 ? -10.335 -19.030 21.514  1.00 74.36  ? 784  ASP   A C    1 
ATOM   2253 O  O    . ASP   A 1 266 ? -9.283  -19.660 21.450  1.00 73.43  ? 784  ASP   A O    1 
ATOM   2254 C  CB   . ASP   A 1 266 ? -11.550 -21.074 22.342  1.00 81.15  ? 784  ASP   A CB   1 
ATOM   2255 C  CG   . ASP   A 1 266 ? -11.165 -20.865 23.799  1.00 89.64  ? 784  ASP   A CG   1 
ATOM   2256 O  OD1  . ASP   A 1 266 ? -11.361 -19.744 24.323  1.00 92.90  ? 784  ASP   A OD1  1 
ATOM   2257 O  OD2  . ASP   A 1 266 ? -10.686 -21.833 24.427  1.00 93.18  ? 784  ASP   A OD2  1 
ATOM   2258 N  N    . VAL   A 1 267 ? -10.385 -17.702 21.532  1.00 61.25  ? 785  VAL   A N    1 
ATOM   2259 C  CA   . VAL   A 1 267 ? -9.188  -16.879 21.388  1.00 54.56  ? 785  VAL   A CA   1 
ATOM   2260 C  C    . VAL   A 1 267 ? -8.197  -17.116 22.521  1.00 59.33  ? 785  VAL   A C    1 
ATOM   2261 O  O    . VAL   A 1 267 ? -7.000  -16.923 22.343  1.00 60.37  ? 785  VAL   A O    1 
ATOM   2262 C  CB   . VAL   A 1 267 ? -9.539  -15.381 21.327  1.00 61.41  ? 785  VAL   A CB   1 
ATOM   2263 C  CG1  . VAL   A 1 267 ? -10.250 -15.061 20.020  1.00 63.62  ? 785  VAL   A CG1  1 
ATOM   2264 C  CG2  . VAL   A 1 267 ? -10.403 -14.985 22.517  1.00 68.68  ? 785  VAL   A CG2  1 
ATOM   2265 N  N    . ASN   A 1 268 ? -8.700  -17.545 23.676  1.00 60.62  ? 786  ASN   A N    1 
ATOM   2266 C  CA   . ASN   A 1 268 ? -7.854  -17.912 24.804  1.00 62.19  ? 786  ASN   A CA   1 
ATOM   2267 C  C    . ASN   A 1 268 ? -6.947  -19.084 24.470  1.00 64.31  ? 786  ASN   A C    1 
ATOM   2268 O  O    . ASN   A 1 268 ? -5.738  -19.037 24.691  1.00 67.25  ? 786  ASN   A O    1 
ATOM   2269 C  CB   . ASN   A 1 268 ? -8.708  -18.267 26.021  1.00 67.42  ? 786  ASN   A CB   1 
ATOM   2270 C  CG   . ASN   A 1 268 ? -9.636  -17.150 26.418  1.00 73.97  ? 786  ASN   A CG   1 
ATOM   2271 O  OD1  . ASN   A 1 268 ? -9.237  -16.226 27.122  1.00 79.01  ? 786  ASN   A OD1  1 
ATOM   2272 N  ND2  . ASN   A 1 268 ? -10.885 -17.222 25.965  1.00 76.05  ? 786  ASN   A ND2  1 
ATOM   2273 N  N    . ASP   A 1 269 ? -7.547  -20.143 23.943  1.00 63.95  ? 787  ASP   A N    1 
ATOM   2274 C  CA   . ASP   A 1 269 ? -6.811  -21.344 23.575  1.00 65.40  ? 787  ASP   A CA   1 
ATOM   2275 C  C    . ASP   A 1 269 ? -5.856  -21.035 22.418  1.00 56.19  ? 787  ASP   A C    1 
ATOM   2276 O  O    . ASP   A 1 269 ? -4.717  -21.489 22.393  1.00 50.47  ? 787  ASP   A O    1 
ATOM   2277 C  CB   . ASP   A 1 269 ? -7.795  -22.463 23.219  1.00 66.75  ? 787  ASP   A CB   1 
ATOM   2278 C  CG   . ASP   A 1 269 ? -7.112  -23.765 22.876  1.00 67.73  ? 787  ASP   A CG   1 
ATOM   2279 O  OD1  . ASP   A 1 269 ? -6.586  -24.430 23.790  1.00 69.98  ? 787  ASP   A OD1  1 
ATOM   2280 O  OD2  . ASP   A 1 269 ? -7.155  -24.149 21.694  1.00 65.82  ? 787  ASP   A OD2  1 
ATOM   2281 N  N    . TRP   A 1 270 ? -6.324  -20.230 21.477  1.00 49.36  ? 788  TRP   A N    1 
ATOM   2282 C  CA   . TRP   A 1 270 ? -5.504  -19.782 20.365  1.00 50.93  ? 788  TRP   A CA   1 
ATOM   2283 C  C    . TRP   A 1 270 ? -4.258  -19.049 20.882  1.00 52.06  ? 788  TRP   A C    1 
ATOM   2284 O  O    . TRP   A 1 270 ? -3.138  -19.313 20.447  1.00 52.69  ? 788  TRP   A O    1 
ATOM   2285 C  CB   . TRP   A 1 270 ? -6.347  -18.883 19.463  1.00 52.59  ? 788  TRP   A CB   1 
ATOM   2286 C  CG   . TRP   A 1 270 ? -5.712  -18.440 18.198  1.00 48.80  ? 788  TRP   A CG   1 
ATOM   2287 C  CD1  . TRP   A 1 270 ? -4.481  -18.781 17.723  1.00 50.21  ? 788  TRP   A CD1  1 
ATOM   2288 C  CD2  . TRP   A 1 270 ? -6.288  -17.556 17.231  1.00 49.78  ? 788  TRP   A CD2  1 
ATOM   2289 N  NE1  . TRP   A 1 270 ? -4.255  -18.162 16.512  1.00 47.76  ? 788  TRP   A NE1  1 
ATOM   2290 C  CE2  . TRP   A 1 270 ? -5.352  -17.403 16.190  1.00 50.02  ? 788  TRP   A CE2  1 
ATOM   2291 C  CE3  . TRP   A 1 270 ? -7.512  -16.878 17.143  1.00 49.40  ? 788  TRP   A CE3  1 
ATOM   2292 C  CZ2  . TRP   A 1 270 ? -5.595  -16.596 15.075  1.00 49.28  ? 788  TRP   A CZ2  1 
ATOM   2293 C  CZ3  . TRP   A 1 270 ? -7.754  -16.085 16.034  1.00 45.64  ? 788  TRP   A CZ3  1 
ATOM   2294 C  CH2  . TRP   A 1 270 ? -6.800  -15.955 15.013  1.00 42.35  ? 788  TRP   A CH2  1 
ATOM   2295 N  N    . ARG   A 1 271 ? -4.478  -18.158 21.841  1.00 50.19  ? 789  ARG   A N    1 
ATOM   2296 C  CA   . ARG   A 1 271 ? -3.456  -17.294 22.426  1.00 48.14  ? 789  ARG   A CA   1 
ATOM   2297 C  C    . ARG   A 1 271 ? -2.396  -18.074 23.217  1.00 53.22  ? 789  ARG   A C    1 
ATOM   2298 O  O    . ARG   A 1 271 ? -1.194  -17.809 23.115  1.00 54.00  ? 789  ARG   A O    1 
ATOM   2299 C  CB   . ARG   A 1 271 ? -4.155  -16.263 23.328  1.00 54.68  ? 789  ARG   A CB   1 
ATOM   2300 C  CG   . ARG   A 1 271 ? -3.323  -15.134 23.880  1.00 52.91  ? 789  ARG   A CG   1 
ATOM   2301 C  CD   . ARG   A 1 271 ? -4.226  -14.141 24.612  1.00 54.53  ? 789  ARG   A CD   1 
ATOM   2302 N  NE   . ARG   A 1 271 ? -3.499  -12.918 24.941  1.00 67.94  ? 789  ARG   A NE   1 
ATOM   2303 C  CZ   . ARG   A 1 271 ? -4.057  -11.787 25.368  1.00 71.04  ? 789  ARG   A CZ   1 
ATOM   2304 N  NH1  . ARG   A 1 271 ? -5.372  -11.698 25.515  1.00 72.87  ? 789  ARG   A NH1  1 
ATOM   2305 N  NH2  . ARG   A 1 271 ? -3.295  -10.733 25.638  1.00 73.18  ? 789  ARG   A NH2  1 
ATOM   2306 N  N    . GLU   A 1 272 ? -2.836  -19.050 23.996  1.00 47.84  ? 790  GLU   A N    1 
ATOM   2307 C  CA   . GLU   A 1 272 ? -1.913  -19.766 24.860  1.00 53.11  ? 790  GLU   A CA   1 
ATOM   2308 C  C    . GLU   A 1 272 ? -1.030  -20.740 24.082  1.00 59.25  ? 790  GLU   A C    1 
ATOM   2309 O  O    . GLU   A 1 272 ? 0.046   -21.110 24.548  1.00 67.63  ? 790  GLU   A O    1 
ATOM   2310 C  CB   . GLU   A 1 272 ? -2.690  -20.486 25.961  1.00 59.92  ? 790  GLU   A CB   1 
ATOM   2311 C  CG   . GLU   A 1 272 ? -3.408  -19.506 26.887  1.00 72.32  ? 790  GLU   A CG   1 
ATOM   2312 C  CD   . GLU   A 1 272 ? -4.150  -20.179 28.022  1.00 84.76  ? 790  GLU   A CD   1 
ATOM   2313 O  OE1  . GLU   A 1 272 ? -5.397  -20.247 27.956  1.00 88.75  ? 790  GLU   A OE1  1 
ATOM   2314 O  OE2  . GLU   A 1 272 ? -3.489  -20.632 28.982  1.00 89.18  ? 790  GLU   A OE2  1 
ATOM   2315 N  N    . HIS   A 1 273 ? -1.469  -21.134 22.888  1.00 51.17  ? 791  HIS   A N    1 
ATOM   2316 C  CA   . HIS   A 1 273 ? -0.688  -22.051 22.064  1.00 49.93  ? 791  HIS   A CA   1 
ATOM   2317 C  C    . HIS   A 1 273 ? -0.105  -21.353 20.830  1.00 47.60  ? 791  HIS   A C    1 
ATOM   2318 O  O    . HIS   A 1 273 ? 0.025   -21.950 19.763  1.00 48.01  ? 791  HIS   A O    1 
ATOM   2319 C  CB   . HIS   A 1 273 ? -1.547  -23.245 21.665  1.00 51.89  ? 791  HIS   A CB   1 
ATOM   2320 C  CG   . HIS   A 1 273 ? -2.079  -24.004 22.838  1.00 55.47  ? 791  HIS   A CG   1 
ATOM   2321 N  ND1  . HIS   A 1 273 ? -3.384  -23.891 23.271  1.00 58.86  ? 791  HIS   A ND1  1 
ATOM   2322 C  CD2  . HIS   A 1 273 ? -1.472  -24.861 23.694  1.00 64.66  ? 791  HIS   A CD2  1 
ATOM   2323 C  CE1  . HIS   A 1 273 ? -3.563  -24.662 24.329  1.00 68.36  ? 791  HIS   A CE1  1 
ATOM   2324 N  NE2  . HIS   A 1 273 ? -2.419  -25.267 24.603  1.00 67.76  ? 791  HIS   A NE2  1 
ATOM   2325 N  N    . THR   A 1 274 ? 0.252   -20.082 20.993  1.00 45.85  ? 792  THR   A N    1 
ATOM   2326 C  CA   . THR   A 1 274 ? 0.965   -19.346 19.951  1.00 44.54  ? 792  THR   A CA   1 
ATOM   2327 C  C    . THR   A 1 274 ? 2.449   -19.287 20.309  1.00 47.94  ? 792  THR   A C    1 
ATOM   2328 O  O    . THR   A 1 274 ? 2.806   -19.102 21.474  1.00 52.23  ? 792  THR   A O    1 
ATOM   2329 C  CB   . THR   A 1 274 ? 0.398   -17.919 19.763  1.00 44.30  ? 792  THR   A CB   1 
ATOM   2330 O  OG1  . THR   A 1 274 ? -0.900  -17.994 19.172  1.00 41.46  ? 792  THR   A OG1  1 
ATOM   2331 C  CG2  . THR   A 1 274 ? 1.292   -17.072 18.846  1.00 45.79  ? 792  THR   A CG2  1 
ATOM   2332 N  N    . LYS   A 1 275 ? 3.306   -19.478 19.307  1.00 48.59  ? 793  LYS   A N    1 
ATOM   2333 C  CA   . LYS   A 1 275 ? 4.744   -19.265 19.464  1.00 49.12  ? 793  LYS   A CA   1 
ATOM   2334 C  C    . LYS   A 1 275 ? 5.163   -17.904 18.877  1.00 52.52  ? 793  LYS   A C    1 
ATOM   2335 O  O    . LYS   A 1 275 ? 4.435   -17.305 18.077  1.00 48.97  ? 793  LYS   A O    1 
ATOM   2336 C  CB   . LYS   A 1 275 ? 5.532   -20.395 18.802  1.00 51.88  ? 793  LYS   A CB   1 
ATOM   2337 C  CG   . LYS   A 1 275 ? 5.199   -21.789 19.325  1.00 62.92  ? 793  LYS   A CG   1 
ATOM   2338 C  CD   . LYS   A 1 275 ? 5.313   -21.853 20.836  1.00 63.78  ? 793  LYS   A CD   1 
ATOM   2339 C  CE   . LYS   A 1 275 ? 5.630   -23.259 21.317  1.00 74.49  ? 793  LYS   A CE   1 
ATOM   2340 N  NZ   . LYS   A 1 275 ? 4.671   -24.285 20.809  1.00 77.93  ? 793  LYS   A NZ   1 
ATOM   2341 N  N    . TYR   A 1 276 ? 6.338   -17.420 19.276  1.00 54.60  ? 794  TYR   A N    1 
ATOM   2342 C  CA   . TYR   A 1 276 ? 6.794   -16.092 18.859  1.00 53.65  ? 794  TYR   A CA   1 
ATOM   2343 C  C    . TYR   A 1 276 ? 8.233   -16.111 18.380  1.00 54.56  ? 794  TYR   A C    1 
ATOM   2344 O  O    . TYR   A 1 276 ? 9.058   -16.857 18.909  1.00 57.35  ? 794  TYR   A O    1 
ATOM   2345 C  CB   . TYR   A 1 276 ? 6.635   -15.096 20.003  1.00 53.45  ? 794  TYR   A CB   1 
ATOM   2346 C  CG   . TYR   A 1 276 ? 5.208   -14.974 20.459  1.00 47.55  ? 794  TYR   A CG   1 
ATOM   2347 C  CD1  . TYR   A 1 276 ? 4.272   -14.292 19.688  1.00 46.89  ? 794  TYR   A CD1  1 
ATOM   2348 C  CD2  . TYR   A 1 276 ? 4.791   -15.540 21.655  1.00 51.99  ? 794  TYR   A CD2  1 
ATOM   2349 C  CE1  . TYR   A 1 276 ? 2.952   -14.184 20.092  1.00 43.37  ? 794  TYR   A CE1  1 
ATOM   2350 C  CE2  . TYR   A 1 276 ? 3.472   -15.425 22.080  1.00 45.96  ? 794  TYR   A CE2  1 
ATOM   2351 C  CZ   . TYR   A 1 276 ? 2.557   -14.749 21.291  1.00 46.27  ? 794  TYR   A CZ   1 
ATOM   2352 O  OH   . TYR   A 1 276 ? 1.243   -14.640 21.697  1.00 42.59  ? 794  TYR   A OH   1 
ATOM   2353 N  N    . LYS   A 1 277 ? 8.530   -15.294 17.373  1.00 55.30  ? 795  LYS   A N    1 
ATOM   2354 C  CA   . LYS   A 1 277 ? 9.839   -15.338 16.720  1.00 59.74  ? 795  LYS   A CA   1 
ATOM   2355 C  C    . LYS   A 1 277 ? 10.468  -13.961 16.545  1.00 62.43  ? 795  LYS   A C    1 
ATOM   2356 O  O    . LYS   A 1 277 ? 9.767   -12.953 16.375  1.00 63.56  ? 795  LYS   A O    1 
ATOM   2357 C  CB   . LYS   A 1 277 ? 9.731   -15.998 15.343  1.00 60.26  ? 795  LYS   A CB   1 
ATOM   2358 C  CG   . LYS   A 1 277 ? 9.491   -17.490 15.334  1.00 69.35  ? 795  LYS   A CG   1 
ATOM   2359 C  CD   . LYS   A 1 277 ? 9.261   -17.955 13.908  1.00 73.98  ? 795  LYS   A CD   1 
ATOM   2360 C  CE   . LYS   A 1 277 ? 10.191  -19.071 13.540  1.00 79.20  ? 795  LYS   A CE   1 
ATOM   2361 N  NZ   . LYS   A 1 277 ? 11.587  -18.642 13.771  1.00 90.35  ? 795  LYS   A NZ   1 
ATOM   2362 N  N    . ASN   A 1 278 ? 11.795  -13.949 16.587  1.00 67.90  ? 796  ASN   A N    1 
ATOM   2363 C  CA   . ASN   A 1 278 ? 12.606  -12.781 16.262  1.00 75.72  ? 796  ASN   A CA   1 
ATOM   2364 C  C    . ASN   A 1 278 ? 12.244  -11.534 17.074  1.00 75.16  ? 796  ASN   A C    1 
ATOM   2365 O  O    . ASN   A 1 278 ? 11.908  -10.485 16.514  1.00 69.34  ? 796  ASN   A O    1 
ATOM   2366 C  CB   . ASN   A 1 278 ? 12.497  -12.480 14.767  1.00 73.36  ? 796  ASN   A CB   1 
ATOM   2367 C  CG   . ASN   A 1 278 ? 13.543  -11.492 14.297  1.00 82.43  ? 796  ASN   A CG   1 
ATOM   2368 O  OD1  . ASN   A 1 278 ? 14.696  -11.545 14.723  1.00 82.03  ? 796  ASN   A OD1  1 
ATOM   2369 N  ND2  . ASN   A 1 278 ? 13.132  -10.557 13.445  1.00 77.22  ? 796  ASN   A ND2  1 
ATOM   2370 N  N    . GLY   A 1 279 ? 12.312  -11.652 18.395  1.00 70.07  ? 797  GLY   A N    1 
ATOM   2371 C  CA   . GLY   A 1 279 ? 12.079  -10.506 19.255  1.00 72.24  ? 797  GLY   A CA   1 
ATOM   2372 C  C    . GLY   A 1 279 ? 10.715  -10.482 19.918  1.00 65.85  ? 797  GLY   A C    1 
ATOM   2373 O  O    . GLY   A 1 279 ? 10.587  -9.974  21.032  1.00 65.10  ? 797  GLY   A O    1 
ATOM   2374 N  N    . TYR   A 1 280 ? 9.699   -11.026 19.247  1.00 60.31  ? 798  TYR   A N    1 
ATOM   2375 C  CA   . TYR   A 1 280 ? 8.348   -11.018 19.806  1.00 62.18  ? 798  TYR   A CA   1 
ATOM   2376 C  C    . TYR   A 1 280 ? 8.210   -12.007 20.958  1.00 55.74  ? 798  TYR   A C    1 
ATOM   2377 O  O    . TYR   A 1 280 ? 8.947   -12.986 21.063  1.00 61.30  ? 798  TYR   A O    1 
ATOM   2378 C  CB   . TYR   A 1 280 ? 7.284   -11.326 18.738  1.00 57.29  ? 798  TYR   A CB   1 
ATOM   2379 C  CG   . TYR   A 1 280 ? 6.961   -10.170 17.802  1.00 67.77  ? 798  TYR   A CG   1 
ATOM   2380 C  CD1  . TYR   A 1 280 ? 6.257   -10.386 16.618  1.00 66.72  ? 798  TYR   A CD1  1 
ATOM   2381 C  CD2  . TYR   A 1 280 ? 7.363   -8.867  18.093  1.00 72.01  ? 798  TYR   A CD2  1 
ATOM   2382 C  CE1  . TYR   A 1 280 ? 5.957   -9.344  15.751  1.00 51.47  ? 798  TYR   A CE1  1 
ATOM   2383 C  CE2  . TYR   A 1 280 ? 7.071   -7.814  17.227  1.00 71.55  ? 798  TYR   A CE2  1 
ATOM   2384 C  CZ   . TYR   A 1 280 ? 6.371   -8.063  16.057  1.00 69.66  ? 798  TYR   A CZ   1 
ATOM   2385 O  OH   . TYR   A 1 280 ? 6.083   -7.037  15.187  1.00 62.86  ? 798  TYR   A OH   1 
ATOM   2386 N  N    . SER   A 1 281 ? 7.239   -11.720 21.814  1.00 54.33  ? 799  SER   A N    1 
ATOM   2387 C  CA   . SER   A 1 281 ? 6.925   -12.533 22.972  1.00 59.00  ? 799  SER   A CA   1 
ATOM   2388 C  C    . SER   A 1 281 ? 5.500   -12.208 23.367  1.00 60.04  ? 799  SER   A C    1 
ATOM   2389 O  O    . SER   A 1 281 ? 4.901   -11.269 22.830  1.00 52.60  ? 799  SER   A O    1 
ATOM   2390 C  CB   . SER   A 1 281 ? 7.889   -12.249 24.124  1.00 69.03  ? 799  SER   A CB   1 
ATOM   2391 O  OG   . SER   A 1 281 ? 7.806   -10.891 24.528  1.00 67.45  ? 799  SER   A OG   1 
ATOM   2392 N  N    . ALA   A 1 282 ? 4.956   -12.976 24.303  1.00 56.06  ? 800  ALA   A N    1 
ATOM   2393 C  CA   . ALA   A 1 282 ? 3.595   -12.750 24.774  1.00 53.48  ? 800  ALA   A CA   1 
ATOM   2394 C  C    . ALA   A 1 282 ? 3.386   -11.331 25.356  1.00 58.12  ? 800  ALA   A C    1 
ATOM   2395 O  O    . ALA   A 1 282 ? 2.305   -10.755 25.222  1.00 53.90  ? 800  ALA   A O    1 
ATOM   2396 C  CB   . ALA   A 1 282 ? 3.231   -13.812 25.808  1.00 50.99  ? 800  ALA   A CB   1 
ATOM   2397 N  N    . ASN   A 1 283 ? 4.419   -10.772 25.987  1.00 60.30  ? 801  ASN   A N    1 
ATOM   2398 C  CA   . ASN   A 1 283 ? 4.310   -9.472  26.652  1.00 69.65  ? 801  ASN   A CA   1 
ATOM   2399 C  C    . ASN   A 1 283 ? 4.657   -8.295  25.755  1.00 62.87  ? 801  ASN   A C    1 
ATOM   2400 O  O    . ASN   A 1 283 ? 4.514   -7.147  26.158  1.00 61.54  ? 801  ASN   A O    1 
ATOM   2401 C  CB   . ASN   A 1 283 ? 5.215   -9.424  27.885  1.00 83.08  ? 801  ASN   A CB   1 
ATOM   2402 C  CG   . ASN   A 1 283 ? 4.814   -10.427 28.946  1.00 90.09  ? 801  ASN   A CG   1 
ATOM   2403 O  OD1  . ASN   A 1 283 ? 5.637   -11.217 29.411  1.00 94.53  ? 801  ASN   A OD1  1 
ATOM   2404 N  ND2  . ASN   A 1 283 ? 3.544   -10.399 29.338  1.00 88.51  ? 801  ASN   A ND2  1 
ATOM   2405 N  N    . HIS   A 1 284 ? 5.134   -8.584  24.551  1.00 60.47  ? 802  HIS   A N    1 
ATOM   2406 C  CA   . HIS   A 1 284 ? 5.588   -7.549  23.625  1.00 64.18  ? 802  HIS   A CA   1 
ATOM   2407 C  C    . HIS   A 1 284 ? 4.434   -6.619  23.248  1.00 54.77  ? 802  HIS   A C    1 
ATOM   2408 O  O    . HIS   A 1 284 ? 3.309   -7.075  23.051  1.00 51.72  ? 802  HIS   A O    1 
ATOM   2409 C  CB   . HIS   A 1 284 ? 6.198   -8.201  22.381  1.00 66.65  ? 802  HIS   A CB   1 
ATOM   2410 C  CG   . HIS   A 1 284 ? 6.944   -7.253  21.490  1.00 63.58  ? 802  HIS   A CG   1 
ATOM   2411 N  ND1  . HIS   A 1 284 ? 6.313   -6.430  20.584  1.00 60.47  ? 802  HIS   A ND1  1 
ATOM   2412 C  CD2  . HIS   A 1 284 ? 8.270   -7.025  21.348  1.00 63.45  ? 802  HIS   A CD2  1 
ATOM   2413 C  CE1  . HIS   A 1 284 ? 7.219   -5.724  19.929  1.00 60.77  ? 802  HIS   A CE1  1 
ATOM   2414 N  NE2  . HIS   A 1 284 ? 8.411   -6.066  20.374  1.00 63.20  ? 802  HIS   A NE2  1 
ATOM   2415 N  N    . GLN   A 1 285 ? 4.709   -5.321  23.160  1.00 57.54  ? 803  GLN   A N    1 
ATOM   2416 C  CA   . GLN   A 1 285 ? 3.655   -4.343  22.911  1.00 57.13  ? 803  GLN   A CA   1 
ATOM   2417 C  C    . GLN   A 1 285 ? 2.839   -4.655  21.652  1.00 57.73  ? 803  GLN   A C    1 
ATOM   2418 O  O    . GLN   A 1 285 ? 1.605   -4.668  21.684  1.00 51.75  ? 803  GLN   A O    1 
ATOM   2419 C  CB   . GLN   A 1 285 ? 4.236   -2.936  22.797  1.00 66.92  ? 803  GLN   A CB   1 
ATOM   2420 C  CG   . GLN   A 1 285 ? 3.168   -1.878  22.575  1.00 62.88  ? 803  GLN   A CG   1 
ATOM   2421 C  CD   . GLN   A 1 285 ? 2.179   -1.801  23.724  1.00 69.60  ? 803  GLN   A CD   1 
ATOM   2422 O  OE1  . GLN   A 1 285 ? 2.437   -1.154  24.740  1.00 76.03  ? 803  GLN   A OE1  1 
ATOM   2423 N  NE2  . GLN   A 1 285 ? 1.047   -2.477  23.575  1.00 66.06  ? 803  GLN   A NE2  1 
ATOM   2424 N  N    . VAL   A 1 286 ? 3.536   -4.914  20.551  1.00 57.93  ? 804  VAL   A N    1 
ATOM   2425 C  CA   . VAL   A 1 286 ? 2.877   -5.242  19.291  1.00 57.16  ? 804  VAL   A CA   1 
ATOM   2426 C  C    . VAL   A 1 286 ? 1.998   -6.490  19.428  1.00 47.85  ? 804  VAL   A C    1 
ATOM   2427 O  O    . VAL   A 1 286 ? 0.875   -6.513  18.931  1.00 45.58  ? 804  VAL   A O    1 
ATOM   2428 C  CB   . VAL   A 1 286 ? 3.907   -5.453  18.157  1.00 62.31  ? 804  VAL   A CB   1 
ATOM   2429 C  CG1  . VAL   A 1 286 ? 3.222   -5.974  16.893  1.00 63.53  ? 804  VAL   A CG1  1 
ATOM   2430 C  CG2  . VAL   A 1 286 ? 4.675   -4.158  17.878  1.00 56.29  ? 804  VAL   A CG2  1 
ATOM   2431 N  N    . ILE   A 1 287 ? 2.504   -7.517  20.109  1.00 48.11  ? 805  ILE   A N    1 
ATOM   2432 C  CA   . ILE   A 1 287 ? 1.731   -8.748  20.339  1.00 46.88  ? 805  ILE   A CA   1 
ATOM   2433 C  C    . ILE   A 1 287 ? 0.488   -8.460  21.194  1.00 53.73  ? 805  ILE   A C    1 
ATOM   2434 O  O    . ILE   A 1 287 ? -0.600  -8.979  20.911  1.00 54.50  ? 805  ILE   A O    1 
ATOM   2435 C  CB   . ILE   A 1 287 ? 2.596   -9.849  21.016  1.00 45.10  ? 805  ILE   A CB   1 
ATOM   2436 C  CG1  . ILE   A 1 287 ? 3.715   -10.315 20.071  1.00 49.70  ? 805  ILE   A CG1  1 
ATOM   2437 C  CG2  . ILE   A 1 287 ? 1.740   -11.036 21.466  1.00 46.19  ? 805  ILE   A CG2  1 
ATOM   2438 C  CD1  . ILE   A 1 287 ? 3.229   -10.784 18.698  1.00 44.11  ? 805  ILE   A CD1  1 
ATOM   2439 N  N    . GLN   A 1 288 ? 0.646   -7.615  22.216  1.00 53.70  ? 806  GLN   A N    1 
ATOM   2440 C  CA   . GLN   A 1 288 ? -0.477  -7.228  23.069  1.00 50.03  ? 806  GLN   A CA   1 
ATOM   2441 C  C    . GLN   A 1 288 ? -1.557  -6.571  22.242  1.00 46.73  ? 806  GLN   A C    1 
ATOM   2442 O  O    . GLN   A 1 288 ? -2.755  -6.728  22.518  1.00 50.06  ? 806  GLN   A O    1 
ATOM   2443 C  CB   . GLN   A 1 288 ? -0.028  -6.284  24.191  1.00 50.54  ? 806  GLN   A CB   1 
ATOM   2444 C  CG   . GLN   A 1 288 ? 0.791   -6.981  25.262  1.00 58.51  ? 806  GLN   A CG   1 
ATOM   2445 C  CD   . GLN   A 1 288 ? 0.972   -6.129  26.495  1.00 76.99  ? 806  GLN   A CD   1 
ATOM   2446 O  OE1  . GLN   A 1 288 ? 0.560   -4.971  26.528  1.00 87.00  ? 806  GLN   A OE1  1 
ATOM   2447 N  NE2  . GLN   A 1 288 ? 1.589   -6.699  27.523  1.00 86.07  ? 806  GLN   A NE2  1 
ATOM   2448 N  N    . TRP   A 1 289 ? -1.128  -5.833  21.223  1.00 46.50  ? 807  TRP   A N    1 
ATOM   2449 C  CA   . TRP   A 1 289 ? -2.060  -5.172  20.313  1.00 46.34  ? 807  TRP   A CA   1 
ATOM   2450 C  C    . TRP   A 1 289 ? -2.672  -6.165  19.345  1.00 43.83  ? 807  TRP   A C    1 
ATOM   2451 O  O    . TRP   A 1 289 ? -3.827  -6.020  18.954  1.00 43.72  ? 807  TRP   A O    1 
ATOM   2452 C  CB   . TRP   A 1 289 ? -1.363  -4.051  19.545  1.00 48.29  ? 807  TRP   A CB   1 
ATOM   2453 C  CG   . TRP   A 1 289 ? -1.198  -2.802  20.352  1.00 51.70  ? 807  TRP   A CG   1 
ATOM   2454 C  CD1  . TRP   A 1 289 ? -1.965  -2.399  21.415  1.00 59.51  ? 807  TRP   A CD1  1 
ATOM   2455 C  CD2  . TRP   A 1 289 ? -0.212  -1.781  20.161  1.00 58.70  ? 807  TRP   A CD2  1 
ATOM   2456 N  NE1  . TRP   A 1 289 ? -1.517  -1.186  21.891  1.00 57.07  ? 807  TRP   A NE1  1 
ATOM   2457 C  CE2  . TRP   A 1 289 ? -0.436  -0.790  21.143  1.00 58.18  ? 807  TRP   A CE2  1 
ATOM   2458 C  CE3  . TRP   A 1 289 ? 0.836   -1.604  19.255  1.00 60.16  ? 807  TRP   A CE3  1 
ATOM   2459 C  CZ2  . TRP   A 1 289 ? 0.354   0.353   21.245  1.00 64.88  ? 807  TRP   A CZ2  1 
ATOM   2460 C  CZ3  . TRP   A 1 289 ? 1.621   -0.461  19.362  1.00 60.33  ? 807  TRP   A CZ3  1 
ATOM   2461 C  CH2  . TRP   A 1 289 ? 1.372   0.499   20.347  1.00 65.05  ? 807  TRP   A CH2  1 
ATOM   2462 N  N    . PHE   A 1 290 ? -1.885  -7.167  18.950  1.00 42.66  ? 808  PHE   A N    1 
ATOM   2463 C  CA   . PHE   A 1 290 ? -2.397  -8.228  18.102  1.00 42.55  ? 808  PHE   A CA   1 
ATOM   2464 C  C    . PHE   A 1 290 ? -3.568  -8.939  18.777  1.00 50.42  ? 808  PHE   A C    1 
ATOM   2465 O  O    . PHE   A 1 290 ? -4.640  -9.095  18.174  1.00 43.98  ? 808  PHE   A O    1 
ATOM   2466 C  CB   . PHE   A 1 290 ? -1.306  -9.240  17.761  1.00 40.07  ? 808  PHE   A CB   1 
ATOM   2467 C  CG   . PHE   A 1 290 ? -1.804  -10.394 16.951  1.00 47.25  ? 808  PHE   A CG   1 
ATOM   2468 C  CD1  . PHE   A 1 290 ? -2.083  -10.237 15.596  1.00 41.26  ? 808  PHE   A CD1  1 
ATOM   2469 C  CD2  . PHE   A 1 290 ? -2.008  -11.636 17.540  1.00 44.18  ? 808  PHE   A CD2  1 
ATOM   2470 C  CE1  . PHE   A 1 290 ? -2.549  -11.306 14.845  1.00 49.36  ? 808  PHE   A CE1  1 
ATOM   2471 C  CE2  . PHE   A 1 290 ? -2.468  -12.715 16.793  1.00 40.68  ? 808  PHE   A CE2  1 
ATOM   2472 C  CZ   . PHE   A 1 290 ? -2.739  -12.552 15.446  1.00 43.11  ? 808  PHE   A CZ   1 
ATOM   2473 N  N    . TRP   A 1 291 ? -3.379  -9.361  20.027  1.00 41.88  ? 809  TRP   A N    1 
ATOM   2474 C  CA   . TRP   A 1 291 ? -4.451  -10.081 20.689  1.00 40.80  ? 809  TRP   A CA   1 
ATOM   2475 C  C    . TRP   A 1 291 ? -5.611  -9.153  21.006  1.00 53.25  ? 809  TRP   A C    1 
ATOM   2476 O  O    . TRP   A 1 291 ? -6.770  -9.570  20.944  1.00 55.39  ? 809  TRP   A O    1 
ATOM   2477 C  CB   . TRP   A 1 291 ? -3.936  -10.800 21.932  1.00 41.61  ? 809  TRP   A CB   1 
ATOM   2478 C  CG   . TRP   A 1 291 ? -3.038  -11.936 21.527  1.00 43.80  ? 809  TRP   A CG   1 
ATOM   2479 C  CD1  . TRP   A 1 291 ? -1.703  -12.044 21.756  1.00 44.06  ? 809  TRP   A CD1  1 
ATOM   2480 C  CD2  . TRP   A 1 291 ? -3.407  -13.083 20.746  1.00 42.24  ? 809  TRP   A CD2  1 
ATOM   2481 N  NE1  . TRP   A 1 291 ? -1.219  -13.212 21.208  1.00 49.85  ? 809  TRP   A NE1  1 
ATOM   2482 C  CE2  . TRP   A 1 291 ? -2.246  -13.863 20.575  1.00 41.82  ? 809  TRP   A CE2  1 
ATOM   2483 C  CE3  . TRP   A 1 291 ? -4.614  -13.535 20.193  1.00 43.47  ? 809  TRP   A CE3  1 
ATOM   2484 C  CZ2  . TRP   A 1 291 ? -2.248  -15.064 19.864  1.00 42.32  ? 809  TRP   A CZ2  1 
ATOM   2485 C  CZ3  . TRP   A 1 291 ? -4.619  -14.736 19.493  1.00 39.51  ? 809  TRP   A CZ3  1 
ATOM   2486 C  CH2  . TRP   A 1 291 ? -3.441  -15.486 19.335  1.00 46.29  ? 809  TRP   A CH2  1 
ATOM   2487 N  N    . LYS   A 1 292 ? -5.317  -7.889  21.291  1.00 43.69  ? 810  LYS   A N    1 
ATOM   2488 C  CA   . LYS   A 1 292 ? -6.384  -6.904  21.451  1.00 45.76  ? 810  LYS   A CA   1 
ATOM   2489 C  C    . LYS   A 1 292 ? -7.231  -6.809  20.172  1.00 47.20  ? 810  LYS   A C    1 
ATOM   2490 O  O    . LYS   A 1 292 ? -8.460  -6.731  20.231  1.00 46.88  ? 810  LYS   A O    1 
ATOM   2491 C  CB   . LYS   A 1 292 ? -5.808  -5.531  21.817  1.00 47.76  ? 810  LYS   A CB   1 
ATOM   2492 C  CG   . LYS   A 1 292 ? -6.864  -4.417  21.911  1.00 50.57  ? 810  LYS   A CG   1 
ATOM   2493 C  CD   . LYS   A 1 292 ? -6.295  -3.127  22.511  1.00 53.48  ? 810  LYS   A CD   1 
ATOM   2494 C  CE   . LYS   A 1 292 ? -7.363  -2.035  22.547  1.00 64.58  ? 810  LYS   A CE   1 
ATOM   2495 N  NZ   . LYS   A 1 292 ? -6.845  -0.731  23.052  1.00 73.63  ? 810  LYS   A NZ   1 
ATOM   2496 N  N    . ALA   A 1 293 ? -6.570  -6.825  19.018  1.00 49.44  ? 811  ALA   A N    1 
ATOM   2497 C  CA   . ALA   A 1 293 ? -7.271  -6.736  17.734  1.00 47.79  ? 811  ALA   A CA   1 
ATOM   2498 C  C    . ALA   A 1 293 ? -8.161  -7.951  17.513  1.00 43.45  ? 811  ALA   A C    1 
ATOM   2499 O  O    . ALA   A 1 293 ? -9.338  -7.814  17.174  1.00 46.65  ? 811  ALA   A O    1 
ATOM   2500 C  CB   . ALA   A 1 293 ? -6.274  -6.602  16.591  1.00 43.10  ? 811  ALA   A CB   1 
ATOM   2501 N  N    . VAL   A 1 294 ? -7.588  -9.137  17.713  1.00 48.49  ? 812  VAL   A N    1 
ATOM   2502 C  CA   . VAL   A 1 294 ? -8.285  -10.397 17.467  1.00 49.51  ? 812  VAL   A CA   1 
ATOM   2503 C  C    . VAL   A 1 294 ? -9.522  -10.471 18.332  1.00 51.80  ? 812  VAL   A C    1 
ATOM   2504 O  O    . VAL   A 1 294 ? -10.600 -10.847 17.876  1.00 51.33  ? 812  VAL   A O    1 
ATOM   2505 C  CB   . VAL   A 1 294 ? -7.392  -11.636 17.756  1.00 52.84  ? 812  VAL   A CB   1 
ATOM   2506 C  CG1  . VAL   A 1 294 ? -8.213  -12.927 17.644  1.00 55.56  ? 812  VAL   A CG1  1 
ATOM   2507 C  CG2  . VAL   A 1 294 ? -6.185  -11.684 16.819  1.00 41.45  ? 812  VAL   A CG2  1 
ATOM   2508 N  N    . LEU   A 1 295 ? -9.349  -10.082 19.587  1.00 62.98  ? 813  LEU   A N    1 
ATOM   2509 C  CA   . LEU   A 1 295 ? -10.418 -10.107 20.570  1.00 63.79  ? 813  LEU   A CA   1 
ATOM   2510 C  C    . LEU   A 1 295 ? -11.598 -9.237  20.156  1.00 67.17  ? 813  LEU   A C    1 
ATOM   2511 O  O    . LEU   A 1 295 ? -12.742 -9.530  20.517  1.00 69.94  ? 813  LEU   A O    1 
ATOM   2512 C  CB   . LEU   A 1 295 ? -9.887  -9.648  21.926  1.00 66.69  ? 813  LEU   A CB   1 
ATOM   2513 C  CG   . LEU   A 1 295 ? -10.724 -9.993  23.151  1.00 78.47  ? 813  LEU   A CG   1 
ATOM   2514 C  CD1  . LEU   A 1 295 ? -10.722 -11.497 23.366  1.00 86.31  ? 813  LEU   A CD1  1 
ATOM   2515 C  CD2  . LEU   A 1 295 ? -10.187 -9.270  24.370  1.00 82.23  ? 813  LEU   A CD2  1 
ATOM   2516 N  N    . MET   A 1 296 ? -11.339 -8.171  19.402  1.00 62.11  ? 814  MET   A N    1 
ATOM   2517 C  CA   . MET   A 1 296 ? -12.434 -7.278  19.037  1.00 68.14  ? 814  MET   A CA   1 
ATOM   2518 C  C    . MET   A 1 296 ? -12.887 -7.469  17.581  1.00 67.95  ? 814  MET   A C    1 
ATOM   2519 O  O    . MET   A 1 296 ? -13.723 -6.718  17.075  1.00 69.95  ? 814  MET   A O    1 
ATOM   2520 C  CB   . MET   A 1 296 ? -12.057 -5.814  19.307  1.00 67.62  ? 814  MET   A CB   1 
ATOM   2521 C  CG   . MET   A 1 296 ? -11.175 -5.143  18.283  1.00 67.75  ? 814  MET   A CG   1 
ATOM   2522 S  SD   . MET   A 1 296 ? -11.103 -3.349  18.541  1.00 73.55  ? 814  MET   A SD   1 
ATOM   2523 C  CE   . MET   A 1 296 ? -10.329 -3.328  20.150  1.00 65.95  ? 814  MET   A CE   1 
ATOM   2524 N  N    . MET   A 1 297 ? -12.351 -8.488  16.915  1.00 63.40  ? 815  MET   A N    1 
ATOM   2525 C  CA   . MET   A 1 297 ? -12.855 -8.864  15.597  1.00 62.68  ? 815  MET   A CA   1 
ATOM   2526 C  C    . MET   A 1 297 ? -14.111 -9.717  15.735  1.00 64.88  ? 815  MET   A C    1 
ATOM   2527 O  O    . MET   A 1 297 ? -14.276 -10.428 16.725  1.00 61.31  ? 815  MET   A O    1 
ATOM   2528 C  CB   . MET   A 1 297 ? -11.795 -9.624  14.802  1.00 60.76  ? 815  MET   A CB   1 
ATOM   2529 C  CG   . MET   A 1 297 ? -10.586 -8.797  14.405  1.00 59.32  ? 815  MET   A CG   1 
ATOM   2530 S  SD   . MET   A 1 297 ? -9.390  -9.759  13.454  1.00 64.06  ? 815  MET   A SD   1 
ATOM   2531 C  CE   . MET   A 1 297 ? -9.504  -11.335 14.267  1.00 74.36  ? 815  MET   A CE   1 
ATOM   2532 N  N    . ASP   A 1 298 ? -14.993 -9.633  14.742  1.00 71.14  ? 816  ASP   A N    1 
ATOM   2533 C  CA   . ASP   A 1 298 ? -16.155 -10.517 14.653  1.00 79.23  ? 816  ASP   A CA   1 
ATOM   2534 C  C    . ASP   A 1 298 ? -15.710 -11.967 14.484  1.00 78.36  ? 816  ASP   A C    1 
ATOM   2535 O  O    . ASP   A 1 298 ? -14.589 -12.219 14.040  1.00 75.20  ? 816  ASP   A O    1 
ATOM   2536 C  CB   . ASP   A 1 298 ? -17.056 -10.107 13.484  1.00 84.02  ? 816  ASP   A CB   1 
ATOM   2537 C  CG   . ASP   A 1 298 ? -17.717 -8.757  13.702  1.00 98.69  ? 816  ASP   A CG   1 
ATOM   2538 O  OD1  . ASP   A 1 298 ? -18.068 -8.441  14.860  1.00 101.81 ? 816  ASP   A OD1  1 
ATOM   2539 O  OD2  . ASP   A 1 298 ? -17.883 -8.009  12.716  1.00 105.52 ? 816  ASP   A OD2  1 
ATOM   2540 N  N    . SER   A 1 299 ? -16.583 -12.912 14.839  1.00 80.33  ? 817  SER   A N    1 
ATOM   2541 C  CA   . SER   A 1 299 ? -16.299 -14.337 14.651  1.00 78.58  ? 817  SER   A CA   1 
ATOM   2542 C  C    . SER   A 1 299 ? -15.911 -14.611 13.210  1.00 75.96  ? 817  SER   A C    1 
ATOM   2543 O  O    . SER   A 1 299 ? -15.006 -15.402 12.943  1.00 75.00  ? 817  SER   A O    1 
ATOM   2544 C  CB   . SER   A 1 299 ? -17.501 -15.206 15.032  1.00 90.27  ? 817  SER   A CB   1 
ATOM   2545 O  OG   . SER   A 1 299 ? -17.768 -15.153 16.423  1.00 94.81  ? 817  SER   A OG   1 
ATOM   2546 N  N    . GLU   A 1 300 ? -16.594 -13.937 12.289  1.00 74.11  ? 818  GLU   A N    1 
ATOM   2547 C  CA   . GLU   A 1 300 ? -16.267 -14.013 10.870  1.00 82.20  ? 818  GLU   A CA   1 
ATOM   2548 C  C    . GLU   A 1 300 ? -14.834 -13.561 10.569  1.00 80.55  ? 818  GLU   A C    1 
ATOM   2549 O  O    . GLU   A 1 300 ? -14.136 -14.193 9.773   1.00 79.26  ? 818  GLU   A O    1 
ATOM   2550 C  CB   . GLU   A 1 300 ? -17.263 -13.177 10.054  1.00 92.03  ? 818  GLU   A CB   1 
ATOM   2551 C  CG   . GLU   A 1 300 ? -16.703 -12.554 8.765   1.00 97.95  ? 818  GLU   A CG   1 
ATOM   2552 C  CD   . GLU   A 1 300 ? -16.371 -13.571 7.677   1.00 106.05 ? 818  GLU   A CD   1 
ATOM   2553 O  OE1  . GLU   A 1 300 ? -15.937 -13.146 6.583   1.00 107.68 ? 818  GLU   A OE1  1 
ATOM   2554 O  OE2  . GLU   A 1 300 ? -16.533 -14.789 7.907   1.00 111.46 ? 818  GLU   A OE2  1 
ATOM   2555 N  N    . LYS   A 1 301 ? -14.396 -12.477 11.204  1.00 75.48  ? 819  LYS   A N    1 
ATOM   2556 C  CA   . LYS   A 1 301 ? -13.066 -11.934 10.932  1.00 64.92  ? 819  LYS   A CA   1 
ATOM   2557 C  C    . LYS   A 1 301 ? -11.987 -12.766 11.603  1.00 56.74  ? 819  LYS   A C    1 
ATOM   2558 O  O    . LYS   A 1 301 ? -10.901 -12.950 11.053  1.00 50.76  ? 819  LYS   A O    1 
ATOM   2559 C  CB   . LYS   A 1 301 ? -12.969 -10.475 11.380  1.00 66.01  ? 819  LYS   A CB   1 
ATOM   2560 C  CG   . LYS   A 1 301 ? -13.261 -9.483  10.264  1.00 74.61  ? 819  LYS   A CG   1 
ATOM   2561 C  CD   . LYS   A 1 301 ? -14.693 -9.626  9.767   1.00 84.13  ? 819  LYS   A CD   1 
ATOM   2562 C  CE   . LYS   A 1 301 ? -14.898 -8.881  8.462   1.00 89.53  ? 819  LYS   A CE   1 
ATOM   2563 N  NZ   . LYS   A 1 301 ? -13.896 -9.299  7.438   1.00 86.58  ? 819  LYS   A NZ   1 
ATOM   2564 N  N    . ARG   A 1 302 ? -12.289 -13.269 12.794  1.00 59.58  ? 820  ARG   A N    1 
ATOM   2565 C  CA   . ARG   A 1 302 ? -11.396 -14.207 13.471  1.00 57.45  ? 820  ARG   A CA   1 
ATOM   2566 C  C    . ARG   A 1 302 ? -11.138 -15.449 12.610  1.00 62.05  ? 820  ARG   A C    1 
ATOM   2567 O  O    . ARG   A 1 302 ? -9.991  -15.878 12.458  1.00 49.22  ? 820  ARG   A O    1 
ATOM   2568 C  CB   . ARG   A 1 302 ? -11.972 -14.619 14.826  1.00 49.07  ? 820  ARG   A CB   1 
ATOM   2569 C  CG   . ARG   A 1 302 ? -11.956 -13.523 15.874  1.00 50.45  ? 820  ARG   A CG   1 
ATOM   2570 C  CD   . ARG   A 1 302 ? -12.469 -14.052 17.193  1.00 55.65  ? 820  ARG   A CD   1 
ATOM   2571 N  NE   . ARG   A 1 302 ? -12.822 -12.974 18.109  1.00 64.75  ? 820  ARG   A NE   1 
ATOM   2572 C  CZ   . ARG   A 1 302 ? -13.559 -13.144 19.202  1.00 68.74  ? 820  ARG   A CZ   1 
ATOM   2573 N  NH1  . ARG   A 1 302 ? -14.018 -14.349 19.508  1.00 69.92  ? 820  ARG   A NH1  1 
ATOM   2574 N  NH2  . ARG   A 1 302 ? -13.844 -12.112 19.984  1.00 68.46  ? 820  ARG   A NH2  1 
ATOM   2575 N  N    . ILE   A 1 303 ? -12.210 -16.015 12.053  1.00 68.48  ? 821  ILE   A N    1 
ATOM   2576 C  CA   . ILE   A 1 303 ? -12.107 -17.168 11.161  1.00 71.30  ? 821  ILE   A CA   1 
ATOM   2577 C  C    . ILE   A 1 303 ? -11.223 -16.853 9.959   1.00 67.33  ? 821  ILE   A C    1 
ATOM   2578 O  O    . ILE   A 1 303 ? -10.313 -17.621 9.628   1.00 67.25  ? 821  ILE   A O    1 
ATOM   2579 C  CB   . ILE   A 1 303 ? -13.497 -17.630 10.658  1.00 74.81  ? 821  ILE   A CB   1 
ATOM   2580 C  CG1  . ILE   A 1 303 ? -14.271 -18.324 11.781  1.00 76.55  ? 821  ILE   A CG1  1 
ATOM   2581 C  CG2  . ILE   A 1 303 ? -13.357 -18.560 9.462   1.00 75.92  ? 821  ILE   A CG2  1 
ATOM   2582 C  CD1  . ILE   A 1 303 ? -13.687 -19.650 12.198  1.00 80.83  ? 821  ILE   A CD1  1 
ATOM   2583 N  N    . ARG   A 1 304 ? -11.479 -15.716 9.316   1.00 58.39  ? 822  ARG   A N    1 
ATOM   2584 C  CA   . ARG   A 1 304 ? -10.752 -15.374 8.102   1.00 59.75  ? 822  ARG   A CA   1 
ATOM   2585 C  C    . ARG   A 1 304 ? -9.279  -15.045 8.380   1.00 57.37  ? 822  ARG   A C    1 
ATOM   2586 O  O    . ARG   A 1 304 ? -8.423  -15.291 7.531   1.00 63.74  ? 822  ARG   A O    1 
ATOM   2587 C  CB   . ARG   A 1 304 ? -11.435 -14.218 7.366   1.00 64.59  ? 822  ARG   A CB   1 
ATOM   2588 C  CG   . ARG   A 1 304 ? -11.143 -14.234 5.869   1.00 73.37  ? 822  ARG   A CG   1 
ATOM   2589 C  CD   . ARG   A 1 304 ? -12.308 -13.718 5.032   1.00 83.96  ? 822  ARG   A CD   1 
ATOM   2590 N  NE   . ARG   A 1 304 ? -12.488 -12.278 5.178   1.00 89.27  ? 822  ARG   A NE   1 
ATOM   2591 C  CZ   . ARG   A 1 304 ? -13.313 -11.545 4.438   1.00 93.51  ? 822  ARG   A CZ   1 
ATOM   2592 N  NH1  . ARG   A 1 304 ? -14.040 -12.116 3.483   1.00 94.75  ? 822  ARG   A NH1  1 
ATOM   2593 N  NH2  . ARG   A 1 304 ? -13.404 -10.237 4.651   1.00 93.59  ? 822  ARG   A NH2  1 
ATOM   2594 N  N    . LEU   A 1 305 ? -8.972  -14.514 9.562   1.00 50.60  ? 823  LEU   A N    1 
ATOM   2595 C  CA   . LEU   A 1 305 ? -7.570  -14.329 9.952   1.00 49.04  ? 823  LEU   A CA   1 
ATOM   2596 C  C    . LEU   A 1 305 ? -6.875  -15.674 10.071  1.00 46.02  ? 823  LEU   A C    1 
ATOM   2597 O  O    . LEU   A 1 305 ? -5.776  -15.858 9.562   1.00 52.59  ? 823  LEU   A O    1 
ATOM   2598 C  CB   . LEU   A 1 305 ? -7.457  -13.573 11.274  1.00 59.25  ? 823  LEU   A CB   1 
ATOM   2599 C  CG   . LEU   A 1 305 ? -6.103  -13.616 11.996  1.00 52.56  ? 823  LEU   A CG   1 
ATOM   2600 C  CD1  . LEU   A 1 305 ? -4.978  -13.002 11.155  1.00 48.16  ? 823  LEU   A CD1  1 
ATOM   2601 C  CD2  . LEU   A 1 305 ? -6.225  -12.914 13.341  1.00 52.54  ? 823  LEU   A CD2  1 
ATOM   2602 N  N    . LEU   A 1 306 ? -7.531  -16.605 10.755  1.00 52.88  ? 824  LEU   A N    1 
ATOM   2603 C  CA   . LEU   A 1 306 ? -7.050  -17.974 10.879  1.00 55.39  ? 824  LEU   A CA   1 
ATOM   2604 C  C    . LEU   A 1 306 ? -6.846  -18.601 9.499   1.00 63.46  ? 824  LEU   A C    1 
ATOM   2605 O  O    . LEU   A 1 306 ? -5.864  -19.300 9.254   1.00 58.16  ? 824  LEU   A O    1 
ATOM   2606 C  CB   . LEU   A 1 306 ? -8.038  -18.796 11.701  1.00 62.28  ? 824  LEU   A CB   1 
ATOM   2607 C  CG   . LEU   A 1 306 ? -7.474  -19.938 12.544  1.00 69.46  ? 824  LEU   A CG   1 
ATOM   2608 C  CD1  . LEU   A 1 306 ? -6.295  -19.468 13.355  1.00 59.95  ? 824  LEU   A CD1  1 
ATOM   2609 C  CD2  . LEU   A 1 306 ? -8.550  -20.497 13.456  1.00 79.99  ? 824  LEU   A CD2  1 
ATOM   2610 N  N    . GLN   A 1 307 ? -7.783  -18.326 8.600   1.00 68.45  ? 825  GLN   A N    1 
ATOM   2611 C  CA   . GLN   A 1 307 ? -7.735  -18.819 7.228   1.00 73.51  ? 825  GLN   A CA   1 
ATOM   2612 C  C    . GLN   A 1 307 ? -6.491  -18.295 6.505   1.00 68.38  ? 825  GLN   A C    1 
ATOM   2613 O  O    . GLN   A 1 307 ? -5.784  -19.041 5.816   1.00 63.26  ? 825  GLN   A O    1 
ATOM   2614 C  CB   . GLN   A 1 307 ? -9.008  -18.396 6.489   1.00 80.59  ? 825  GLN   A CB   1 
ATOM   2615 C  CG   . GLN   A 1 307 ? -9.659  -19.460 5.637   1.00 87.41  ? 825  GLN   A CG   1 
ATOM   2616 C  CD   . GLN   A 1 307 ? -11.075 -19.079 5.239   1.00 91.25  ? 825  GLN   A CD   1 
ATOM   2617 O  OE1  . GLN   A 1 307 ? -11.589 -18.034 5.650   1.00 82.30  ? 825  GLN   A OE1  1 
ATOM   2618 N  NE2  . GLN   A 1 307 ? -11.712 -19.925 4.436   1.00 99.34  ? 825  GLN   A NE2  1 
ATOM   2619 N  N    . PHE   A 1 308 ? -6.235  -17.002 6.687   1.00 59.63  ? 826  PHE   A N    1 
ATOM   2620 C  CA   . PHE   A 1 308 ? -5.110  -16.308 6.067   1.00 59.65  ? 826  PHE   A CA   1 
ATOM   2621 C  C    . PHE   A 1 308 ? -3.765  -16.904 6.491   1.00 59.20  ? 826  PHE   A C    1 
ATOM   2622 O  O    . PHE   A 1 308 ? -2.881  -17.140 5.659   1.00 58.77  ? 826  PHE   A O    1 
ATOM   2623 C  CB   . PHE   A 1 308 ? -5.174  -14.817 6.427   1.00 57.39  ? 826  PHE   A CB   1 
ATOM   2624 C  CG   . PHE   A 1 308 ? -4.000  -14.014 5.946   1.00 58.76  ? 826  PHE   A CG   1 
ATOM   2625 C  CD1  . PHE   A 1 308 ? -3.782  -13.818 4.588   1.00 63.77  ? 826  PHE   A CD1  1 
ATOM   2626 C  CD2  . PHE   A 1 308 ? -3.130  -13.424 6.856   1.00 56.68  ? 826  PHE   A CD2  1 
ATOM   2627 C  CE1  . PHE   A 1 308 ? -2.703  -13.064 4.146   1.00 69.36  ? 826  PHE   A CE1  1 
ATOM   2628 C  CE2  . PHE   A 1 308 ? -2.050  -12.668 6.423   1.00 54.65  ? 826  PHE   A CE2  1 
ATOM   2629 C  CZ   . PHE   A 1 308 ? -1.835  -12.485 5.066   1.00 63.61  ? 826  PHE   A CZ   1 
ATOM   2630 N  N    . VAL   A 1 309 ? -3.620  -17.158 7.787   1.00 53.35  ? 827  VAL   A N    1 
ATOM   2631 C  CA   . VAL   A 1 309 ? -2.335  -17.565 8.328   1.00 57.93  ? 827  VAL   A CA   1 
ATOM   2632 C  C    . VAL   A 1 309 ? -2.070  -19.056 8.111   1.00 60.51  ? 827  VAL   A C    1 
ATOM   2633 O  O    . VAL   A 1 309 ? -0.950  -19.452 7.793   1.00 65.38  ? 827  VAL   A O    1 
ATOM   2634 C  CB   . VAL   A 1 309 ? -2.235  -17.245 9.826   1.00 50.85  ? 827  VAL   A CB   1 
ATOM   2635 C  CG1  . VAL   A 1 309 ? -0.890  -17.711 10.367  1.00 51.47  ? 827  VAL   A CG1  1 
ATOM   2636 C  CG2  . VAL   A 1 309 ? -2.421  -15.751 10.056  1.00 49.89  ? 827  VAL   A CG2  1 
ATOM   2637 N  N    . THR   A 1 310 ? -3.108  -19.872 8.267   1.00 56.64  ? 828  THR   A N    1 
ATOM   2638 C  CA   . THR   A 1 310 ? -2.970  -21.321 8.187   1.00 65.58  ? 828  THR   A CA   1 
ATOM   2639 C  C    . THR   A 1 310 ? -3.125  -21.843 6.760   1.00 75.01  ? 828  THR   A C    1 
ATOM   2640 O  O    . THR   A 1 310 ? -2.465  -22.810 6.365   1.00 73.28  ? 828  THR   A O    1 
ATOM   2641 C  CB   . THR   A 1 310 ? -4.000  -22.013 9.108   1.00 66.25  ? 828  THR   A CB   1 
ATOM   2642 O  OG1  . THR   A 1 310 ? -3.716  -21.675 10.473  1.00 60.73  ? 828  THR   A OG1  1 
ATOM   2643 C  CG2  . THR   A 1 310 ? -3.948  -23.522 8.957   1.00 75.31  ? 828  THR   A CG2  1 
ATOM   2644 N  N    . GLY   A 1 311 ? -3.984  -21.189 5.985   1.00 80.71  ? 829  GLY   A N    1 
ATOM   2645 C  CA   . GLY   A 1 311 ? -4.326  -21.659 4.655   1.00 90.59  ? 829  GLY   A CA   1 
ATOM   2646 C  C    . GLY   A 1 311 ? -5.718  -22.265 4.637   1.00 103.90 ? 829  GLY   A C    1 
ATOM   2647 O  O    . GLY   A 1 311 ? -6.319  -22.436 3.576   1.00 109.62 ? 829  GLY   A O    1 
ATOM   2648 N  N    . THR   A 1 312 ? -6.225  -22.596 5.824   1.00 110.87 ? 830  THR   A N    1 
ATOM   2649 C  CA   . THR   A 1 312 ? -7.565  -23.168 5.983   1.00 118.11 ? 830  THR   A CA   1 
ATOM   2650 C  C    . THR   A 1 312 ? -8.303  -22.517 7.156   1.00 119.11 ? 830  THR   A C    1 
ATOM   2651 O  O    . THR   A 1 312 ? -7.682  -21.902 8.022   1.00 116.05 ? 830  THR   A O    1 
ATOM   2652 C  CB   . THR   A 1 312 ? -7.513  -24.698 6.208   1.00 120.80 ? 830  THR   A CB   1 
ATOM   2653 O  OG1  . THR   A 1 312 ? -6.645  -24.997 7.309   1.00 112.40 ? 830  THR   A OG1  1 
ATOM   2654 C  CG2  . THR   A 1 312 ? -7.011  -25.414 4.960   1.00 127.04 ? 830  THR   A CG2  1 
ATOM   2655 N  N    . SER   A 1 313 ? -9.626  -22.663 7.185   1.00 121.59 ? 831  SER   A N    1 
ATOM   2656 C  CA   . SER   A 1 313 ? -10.449 -22.055 8.233   1.00 116.14 ? 831  SER   A CA   1 
ATOM   2657 C  C    . SER   A 1 313 ? -10.723 -23.010 9.400   1.00 112.71 ? 831  SER   A C    1 
ATOM   2658 O  O    . SER   A 1 313 ? -11.192 -22.588 10.461  1.00 108.72 ? 831  SER   A O    1 
ATOM   2659 C  CB   . SER   A 1 313 ? -11.775 -21.561 7.640   1.00 118.37 ? 831  SER   A CB   1 
ATOM   2660 O  OG   . SER   A 1 313 ? -12.422 -22.583 6.897   1.00 122.38 ? 831  SER   A OG   1 
ATOM   2661 N  N    . ARG   A 1 314 ? -10.419 -24.290 9.196   1.00 110.52 ? 832  ARG   A N    1 
ATOM   2662 C  CA   . ARG   A 1 314 ? -10.705 -25.329 10.182  1.00 104.87 ? 832  ARG   A CA   1 
ATOM   2663 C  C    . ARG   A 1 314 ? -9.876  -25.171 11.458  1.00 100.73 ? 832  ARG   A C    1 
ATOM   2664 O  O    . ARG   A 1 314 ? -8.651  -25.068 11.412  1.00 95.61  ? 832  ARG   A O    1 
ATOM   2665 C  CB   . ARG   A 1 314 ? -10.466 -26.715 9.574   1.00 102.26 ? 832  ARG   A CB   1 
ATOM   2666 N  N    . VAL   A 1 315 ? -10.558 -25.142 12.597  1.00 104.15 ? 833  VAL   A N    1 
ATOM   2667 C  CA   . VAL   A 1 315 ? -9.886  -25.116 13.889  1.00 105.67 ? 833  VAL   A CA   1 
ATOM   2668 C  C    . VAL   A 1 315 ? -9.685  -26.551 14.360  1.00 115.55 ? 833  VAL   A C    1 
ATOM   2669 O  O    . VAL   A 1 315 ? -10.645 -27.321 14.431  1.00 119.75 ? 833  VAL   A O    1 
ATOM   2670 C  CB   . VAL   A 1 315 ? -10.692 -24.325 14.939  1.00 103.59 ? 833  VAL   A CB   1 
ATOM   2671 C  CG1  . VAL   A 1 315 ? -9.938  -24.263 16.254  1.00 101.41 ? 833  VAL   A CG1  1 
ATOM   2672 C  CG2  . VAL   A 1 315 ? -11.001 -22.930 14.431  1.00 97.97  ? 833  VAL   A CG2  1 
ATOM   2673 N  N    . PRO   A 1 316 ? -8.433  -26.921 14.672  1.00 119.51 ? 834  PRO   A N    1 
ATOM   2674 C  CA   . PRO   A 1 316 ? -8.098  -28.301 15.055  1.00 124.68 ? 834  PRO   A CA   1 
ATOM   2675 C  C    . PRO   A 1 316 ? -8.804  -28.767 16.330  1.00 118.37 ? 834  PRO   A C    1 
ATOM   2676 O  O    . PRO   A 1 316 ? -8.928  -28.007 17.294  1.00 116.98 ? 834  PRO   A O    1 
ATOM   2677 C  CB   . PRO   A 1 316 ? -6.578  -28.249 15.263  1.00 124.07 ? 834  PRO   A CB   1 
ATOM   2678 C  CG   . PRO   A 1 316 ? -6.273  -26.813 15.519  1.00 119.29 ? 834  PRO   A CG   1 
ATOM   2679 C  CD   . PRO   A 1 316 ? -7.251  -26.044 14.684  1.00 117.83 ? 834  PRO   A CD   1 
ATOM   2680 N  N    . MET   A 1 317 ? -9.270  -30.012 16.314  1.00 118.24 ? 835  MET   A N    1 
ATOM   2681 C  CA   . MET   A 1 317 ? -9.892  -30.625 17.480  1.00 115.67 ? 835  MET   A CA   1 
ATOM   2682 C  C    . MET   A 1 317 ? -8.904  -30.661 18.642  1.00 116.71 ? 835  MET   A C    1 
ATOM   2683 O  O    . MET   A 1 317 ? -7.692  -30.749 18.429  1.00 117.91 ? 835  MET   A O    1 
ATOM   2684 C  CB   . MET   A 1 317 ? -10.386 -32.032 17.140  1.00 118.56 ? 835  MET   A CB   1 
ATOM   2685 C  CG   . MET   A 1 317 ? -11.265 -32.656 18.200  1.00 121.71 ? 835  MET   A CG   1 
ATOM   2686 S  SD   . MET   A 1 317 ? -12.282 -33.971 17.516  1.00 132.48 ? 835  MET   A SD   1 
ATOM   2687 C  CE   . MET   A 1 317 ? -13.403 -33.025 16.494  1.00 127.24 ? 835  MET   A CE   1 
ATOM   2688 N  N    . ASN   A 1 318 ? -9.431  -30.576 19.863  1.00 115.55 ? 836  ASN   A N    1 
ATOM   2689 C  CA   . ASN   A 1 318 ? -8.620  -30.455 21.074  1.00 111.27 ? 836  ASN   A CA   1 
ATOM   2690 C  C    . ASN   A 1 318 ? -7.750  -29.193 21.045  1.00 102.77 ? 836  ASN   A C    1 
ATOM   2691 O  O    . ASN   A 1 318 ? -6.677  -29.141 21.650  1.00 103.79 ? 836  ASN   A O    1 
ATOM   2692 C  CB   . ASN   A 1 318 ? -7.761  -31.705 21.280  1.00 114.28 ? 836  ASN   A CB   1 
ATOM   2693 C  CG   . ASN   A 1 318 ? -8.595  -32.948 21.515  1.00 123.59 ? 836  ASN   A CG   1 
ATOM   2694 O  OD1  . ASN   A 1 318 ? -9.708  -32.869 22.037  1.00 124.55 ? 836  ASN   A OD1  1 
ATOM   2695 N  ND2  . ASN   A 1 318 ? -8.065  -34.105 21.126  1.00 130.75 ? 836  ASN   A ND2  1 
ATOM   2696 N  N    . GLY   A 1 319 ? -8.225  -28.181 20.325  1.00 88.34  ? 837  GLY   A N    1 
ATOM   2697 C  CA   . GLY   A 1 319 ? -7.634  -26.865 20.370  1.00 74.24  ? 837  GLY   A CA   1 
ATOM   2698 C  C    . GLY   A 1 319 ? -6.404  -26.632 19.515  1.00 62.45  ? 837  GLY   A C    1 
ATOM   2699 O  O    . GLY   A 1 319 ? -6.002  -27.470 18.715  1.00 64.18  ? 837  GLY   A O    1 
ATOM   2700 N  N    . PHE   A 1 320 ? -5.803  -25.466 19.707  1.00 60.78  ? 838  PHE   A N    1 
ATOM   2701 C  CA   . PHE   A 1 320 ? -4.680  -25.006 18.893  1.00 60.27  ? 838  PHE   A CA   1 
ATOM   2702 C  C    . PHE   A 1 320 ? -3.352  -25.624 19.307  1.00 58.36  ? 838  PHE   A C    1 
ATOM   2703 O  O    . PHE   A 1 320 ? -2.350  -25.438 18.623  1.00 58.43  ? 838  PHE   A O    1 
ATOM   2704 C  CB   . PHE   A 1 320 ? -4.573  -23.479 18.951  1.00 51.61  ? 838  PHE   A CB   1 
ATOM   2705 C  CG   . PHE   A 1 320 ? -5.681  -22.773 18.234  1.00 58.45  ? 838  PHE   A CG   1 
ATOM   2706 C  CD1  . PHE   A 1 320 ? -5.465  -22.203 16.987  1.00 63.06  ? 838  PHE   A CD1  1 
ATOM   2707 C  CD2  . PHE   A 1 320 ? -6.943  -22.677 18.802  1.00 63.37  ? 838  PHE   A CD2  1 
ATOM   2708 C  CE1  . PHE   A 1 320 ? -6.490  -21.551 16.319  1.00 60.06  ? 838  PHE   A CE1  1 
ATOM   2709 C  CE2  . PHE   A 1 320 ? -7.973  -22.029 18.139  1.00 65.49  ? 838  PHE   A CE2  1 
ATOM   2710 C  CZ   . PHE   A 1 320 ? -7.744  -21.466 16.895  1.00 64.33  ? 838  PHE   A CZ   1 
ATOM   2711 N  N    . ALA   A 1 321 ? -3.349  -26.346 20.428  1.00 60.32  ? 839  ALA   A N    1 
ATOM   2712 C  CA   . ALA   A 1 321 ? -2.184  -27.107 20.864  1.00 61.54  ? 839  ALA   A CA   1 
ATOM   2713 C  C    . ALA   A 1 321 ? -1.811  -28.188 19.850  1.00 66.65  ? 839  ALA   A C    1 
ATOM   2714 O  O    . ALA   A 1 321 ? -0.677  -28.665 19.839  1.00 69.65  ? 839  ALA   A O    1 
ATOM   2715 C  CB   . ALA   A 1 321 ? -2.439  -27.742 22.231  1.00 65.09  ? 839  ALA   A CB   1 
ATOM   2716 N  N    . GLU   A 1 322 ? -2.763  -28.573 19.003  1.00 65.35  ? 840  GLU   A N    1 
ATOM   2717 C  CA   . GLU   A 1 322 ? -2.546  -29.668 18.058  1.00 76.06  ? 840  GLU   A CA   1 
ATOM   2718 C  C    . GLU   A 1 322 ? -2.643  -29.229 16.596  1.00 74.45  ? 840  GLU   A C    1 
ATOM   2719 O  O    . GLU   A 1 322 ? -2.900  -30.042 15.708  1.00 76.95  ? 840  GLU   A O    1 
ATOM   2720 C  CB   . GLU   A 1 322 ? -3.543  -30.794 18.315  1.00 73.81  ? 840  GLU   A CB   1 
ATOM   2721 C  CG   . GLU   A 1 322 ? -3.389  -31.469 19.656  1.00 77.95  ? 840  GLU   A CG   1 
ATOM   2722 C  CD   . GLU   A 1 322 ? -4.249  -32.704 19.751  1.00 100.47 ? 840  GLU   A CD   1 
ATOM   2723 O  OE1  . GLU   A 1 322 ? -4.980  -32.979 18.775  1.00 102.47 ? 840  GLU   A OE1  1 
ATOM   2724 O  OE2  . GLU   A 1 322 ? -4.188  -33.409 20.785  1.00 112.72 ? 840  GLU   A OE2  1 
ATOM   2725 N  N    . LEU   A 1 323 ? -2.423  -27.942 16.357  1.00 67.33  ? 841  LEU   A N    1 
ATOM   2726 C  CA   . LEU   A 1 323 ? -2.433  -27.386 15.010  1.00 67.25  ? 841  LEU   A CA   1 
ATOM   2727 C  C    . LEU   A 1 323 ? -1.290  -27.953 14.164  1.00 70.62  ? 841  LEU   A C    1 
ATOM   2728 O  O    . LEU   A 1 323 ? -0.149  -28.009 14.623  1.00 67.20  ? 841  LEU   A O    1 
ATOM   2729 C  CB   . LEU   A 1 323 ? -2.328  -25.863 15.092  1.00 59.63  ? 841  LEU   A CB   1 
ATOM   2730 C  CG   . LEU   A 1 323 ? -2.522  -24.968 13.872  1.00 59.70  ? 841  LEU   A CG   1 
ATOM   2731 C  CD1  . LEU   A 1 323 ? -3.887  -25.191 13.264  1.00 65.34  ? 841  LEU   A CD1  1 
ATOM   2732 C  CD2  . LEU   A 1 323 ? -2.375  -23.512 14.303  1.00 51.18  ? 841  LEU   A CD2  1 
ATOM   2733 N  N    . TYR   A 1 324 ? -1.586  -28.363 12.932  1.00 66.33  ? 842  TYR   A N    1 
ATOM   2734 C  CA   . TYR   A 1 324 ? -0.538  -28.828 12.022  1.00 73.53  ? 842  TYR   A CA   1 
ATOM   2735 C  C    . TYR   A 1 324 ? -0.145  -27.815 10.950  1.00 79.34  ? 842  TYR   A C    1 
ATOM   2736 O  O    . TYR   A 1 324 ? -0.981  -27.077 10.427  1.00 65.72  ? 842  TYR   A O    1 
ATOM   2737 C  CB   . TYR   A 1 324 ? -0.962  -30.132 11.349  1.00 74.79  ? 842  TYR   A CB   1 
ATOM   2738 C  CG   . TYR   A 1 324 ? -0.424  -31.342 12.062  1.00 78.67  ? 842  TYR   A CG   1 
ATOM   2739 C  CD1  . TYR   A 1 324 ? -0.744  -31.585 13.392  1.00 78.59  ? 842  TYR   A CD1  1 
ATOM   2740 C  CD2  . TYR   A 1 324 ? 0.411   -32.244 11.413  1.00 84.40  ? 842  TYR   A CD2  1 
ATOM   2741 C  CE1  . TYR   A 1 324 ? -0.247  -32.702 14.058  1.00 82.23  ? 842  TYR   A CE1  1 
ATOM   2742 C  CE2  . TYR   A 1 324 ? 0.912   -33.352 12.069  1.00 87.78  ? 842  TYR   A CE2  1 
ATOM   2743 C  CZ   . TYR   A 1 324 ? 0.583   -33.574 13.392  1.00 87.01  ? 842  TYR   A CZ   1 
ATOM   2744 O  OH   . TYR   A 1 324 ? 1.080   -34.687 14.045  1.00 92.69  ? 842  TYR   A OH   1 
ATOM   2745 N  N    . GLY   A 1 325 ? 1.145   -27.789 10.632  1.00 86.54  ? 843  GLY   A N    1 
ATOM   2746 C  CA   . GLY   A 1 325 ? 1.635   -27.024 9.503   1.00 91.01  ? 843  GLY   A CA   1 
ATOM   2747 C  C    . GLY   A 1 325 ? 1.719   -27.908 8.271   1.00 97.93  ? 843  GLY   A C    1 
ATOM   2748 O  O    . GLY   A 1 325 ? 0.852   -28.754 8.031   1.00 100.72 ? 843  GLY   A O    1 
ATOM   2749 N  N    . SER   A 1 326 ? 2.778   -27.725 7.494   1.00 91.87  ? 844  SER   A N    1 
ATOM   2750 C  CA   . SER   A 1 326 ? 2.948   -28.471 6.255   1.00 90.22  ? 844  SER   A CA   1 
ATOM   2751 C  C    . SER   A 1 326 ? 3.825   -29.718 6.444   1.00 88.15  ? 844  SER   A C    1 
ATOM   2752 O  O    . SER   A 1 326 ? 3.707   -30.690 5.694   1.00 94.87  ? 844  SER   A O    1 
ATOM   2753 C  CB   . SER   A 1 326 ? 3.538   -27.554 5.183   1.00 85.03  ? 844  SER   A CB   1 
ATOM   2754 O  OG   . SER   A 1 326 ? 3.673   -28.233 3.953   1.00 96.02  ? 844  SER   A OG   1 
ATOM   2755 N  N    . ASN   A 1 327 ? 4.692   -29.691 7.454   1.00 86.82  ? 845  ASN   A N    1 
ATOM   2756 C  CA   . ASN   A 1 327 ? 5.646   -30.776 7.692   1.00 94.35  ? 845  ASN   A CA   1 
ATOM   2757 C  C    . ASN   A 1 327 ? 5.514   -31.435 9.070   1.00 96.85  ? 845  ASN   A C    1 
ATOM   2758 O  O    . ASN   A 1 327 ? 6.473   -32.024 9.577   1.00 106.21 ? 845  ASN   A O    1 
ATOM   2759 C  CB   . ASN   A 1 327 ? 7.078   -30.259 7.521   1.00 96.52  ? 845  ASN   A CB   1 
ATOM   2760 C  CG   . ASN   A 1 327 ? 7.346   -29.717 6.129   1.00 103.64 ? 845  ASN   A CG   1 
ATOM   2761 O  OD1  . ASN   A 1 327 ? 6.828   -30.230 5.135   1.00 106.93 ? 845  ASN   A OD1  1 
ATOM   2762 N  ND2  . ASN   A 1 327 ? 8.156   -28.665 6.054   1.00 104.33 ? 845  ASN   A ND2  1 
ATOM   2763 N  N    . GLY   A 1 328 ? 4.330   -31.344 9.668   1.00 87.24  ? 846  GLY   A N    1 
ATOM   2764 C  CA   . GLY   A 1 328 ? 4.096   -31.889 10.995  1.00 86.56  ? 846  GLY   A CA   1 
ATOM   2765 C  C    . GLY   A 1 328 ? 3.509   -30.858 11.949  1.00 82.52  ? 846  GLY   A C    1 
ATOM   2766 O  O    . GLY   A 1 328 ? 3.048   -29.791 11.518  1.00 76.26  ? 846  GLY   A O    1 
ATOM   2767 N  N    . PRO   A 1 329 ? 3.509   -31.172 13.257  1.00 79.68  ? 847  PRO   A N    1 
ATOM   2768 C  CA   . PRO   A 1 329 ? 3.015   -30.253 14.291  1.00 74.54  ? 847  PRO   A CA   1 
ATOM   2769 C  C    . PRO   A 1 329 ? 3.668   -28.872 14.213  1.00 75.51  ? 847  PRO   A C    1 
ATOM   2770 O  O    . PRO   A 1 329 ? 4.892   -28.744 14.270  1.00 78.63  ? 847  PRO   A O    1 
ATOM   2771 C  CB   . PRO   A 1 329 ? 3.389   -30.959 15.592  1.00 76.71  ? 847  PRO   A CB   1 
ATOM   2772 C  CG   . PRO   A 1 329 ? 3.381   -32.426 15.225  1.00 82.78  ? 847  PRO   A CG   1 
ATOM   2773 C  CD   . PRO   A 1 329 ? 3.898   -32.482 13.815  1.00 84.85  ? 847  PRO   A CD   1 
ATOM   2774 N  N    . GLN   A 1 330 ? 2.842   -27.845 14.071  1.00 66.29  ? 848  GLN   A N    1 
ATOM   2775 C  CA   . GLN   A 1 330 ? 3.330   -26.477 13.988  1.00 69.44  ? 848  GLN   A CA   1 
ATOM   2776 C  C    . GLN   A 1 330 ? 2.339   -25.507 14.622  1.00 58.46  ? 848  GLN   A C    1 
ATOM   2777 O  O    . GLN   A 1 330 ? 1.273   -25.238 14.071  1.00 59.72  ? 848  GLN   A O    1 
ATOM   2778 C  CB   . GLN   A 1 330 ? 3.597   -26.081 12.538  1.00 63.81  ? 848  GLN   A CB   1 
ATOM   2779 C  CG   . GLN   A 1 330 ? 4.137   -24.665 12.403  1.00 73.72  ? 848  GLN   A CG   1 
ATOM   2780 C  CD   . GLN   A 1 330 ? 5.533   -24.505 12.988  1.00 76.90  ? 848  GLN   A CD   1 
ATOM   2781 O  OE1  . GLN   A 1 330 ? 6.532   -24.673 12.286  1.00 85.32  ? 848  GLN   A OE1  1 
ATOM   2782 N  NE2  . GLN   A 1 330 ? 5.607   -24.166 14.276  1.00 71.36  ? 848  GLN   A NE2  1 
ATOM   2783 N  N    . SER   A 1 331 ? 2.696   -24.994 15.790  1.00 56.83  ? 849  SER   A N    1 
ATOM   2784 C  CA   . SER   A 1 331 ? 1.833   -24.065 16.498  1.00 53.36  ? 849  SER   A CA   1 
ATOM   2785 C  C    . SER   A 1 331 ? 1.640   -22.817 15.654  1.00 62.82  ? 849  SER   A C    1 
ATOM   2786 O  O    . SER   A 1 331 ? 2.500   -22.481 14.831  1.00 56.64  ? 849  SER   A O    1 
ATOM   2787 C  CB   . SER   A 1 331 ? 2.424   -23.684 17.856  1.00 52.93  ? 849  SER   A CB   1 
ATOM   2788 O  OG   . SER   A 1 331 ? 2.671   -24.824 18.657  1.00 66.16  ? 849  SER   A OG   1 
ATOM   2789 N  N    . PHE   A 1 332 ? 0.504   -22.150 15.846  1.00 48.35  ? 850  PHE   A N    1 
ATOM   2790 C  CA   . PHE   A 1 332 ? 0.300   -20.823 15.289  1.00 46.07  ? 850  PHE   A CA   1 
ATOM   2791 C  C    . PHE   A 1 332 ? 1.467   -19.937 15.726  1.00 52.17  ? 850  PHE   A C    1 
ATOM   2792 O  O    . PHE   A 1 332 ? 1.830   -19.924 16.907  1.00 49.00  ? 850  PHE   A O    1 
ATOM   2793 C  CB   . PHE   A 1 332 ? -1.043  -20.259 15.755  1.00 44.24  ? 850  PHE   A CB   1 
ATOM   2794 C  CG   . PHE   A 1 332 ? -1.380  -18.929 15.164  1.00 49.92  ? 850  PHE   A CG   1 
ATOM   2795 C  CD1  . PHE   A 1 332 ? -2.046  -18.846 13.951  1.00 59.47  ? 850  PHE   A CD1  1 
ATOM   2796 C  CD2  . PHE   A 1 332 ? -1.038  -17.759 15.818  1.00 45.10  ? 850  PHE   A CD2  1 
ATOM   2797 C  CE1  . PHE   A 1 332 ? -2.368  -17.614 13.404  1.00 58.10  ? 850  PHE   A CE1  1 
ATOM   2798 C  CE2  . PHE   A 1 332 ? -1.352  -16.530 15.272  1.00 49.48  ? 850  PHE   A CE2  1 
ATOM   2799 C  CZ   . PHE   A 1 332 ? -2.016  -16.459 14.062  1.00 51.71  ? 850  PHE   A CZ   1 
ATOM   2800 N  N    . THR   A 1 333 ? 2.060   -19.217 14.774  1.00 45.74  ? 851  THR   A N    1 
ATOM   2801 C  CA   . THR   A 1 333 ? 3.285   -18.462 15.028  1.00 48.44  ? 851  THR   A CA   1 
ATOM   2802 C  C    . THR   A 1 333 ? 3.202   -16.981 14.598  1.00 48.41  ? 851  THR   A C    1 
ATOM   2803 O  O    . THR   A 1 333 ? 2.654   -16.665 13.539  1.00 45.14  ? 851  THR   A O    1 
ATOM   2804 C  CB   . THR   A 1 333 ? 4.486   -19.102 14.298  1.00 51.28  ? 851  THR   A CB   1 
ATOM   2805 O  OG1  . THR   A 1 333 ? 4.477   -20.521 14.482  1.00 53.31  ? 851  THR   A OG1  1 
ATOM   2806 C  CG2  . THR   A 1 333 ? 5.803   -18.517 14.819  1.00 55.95  ? 851  THR   A CG2  1 
ATOM   2807 N  N    . VAL   A 1 334 ? 3.752   -16.085 15.418  1.00 45.09  ? 852  VAL   A N    1 
ATOM   2808 C  CA   . VAL   A 1 334 ? 3.902   -14.672 15.031  1.00 45.11  ? 852  VAL   A CA   1 
ATOM   2809 C  C    . VAL   A 1 334 ? 5.374   -14.262 15.050  1.00 49.97  ? 852  VAL   A C    1 
ATOM   2810 O  O    . VAL   A 1 334 ? 6.012   -14.270 16.105  1.00 51.80  ? 852  VAL   A O    1 
ATOM   2811 C  CB   . VAL   A 1 334 ? 3.112   -13.725 15.958  1.00 43.15  ? 852  VAL   A CB   1 
ATOM   2812 C  CG1  . VAL   A 1 334 ? 3.213   -12.282 15.459  1.00 43.79  ? 852  VAL   A CG1  1 
ATOM   2813 C  CG2  . VAL   A 1 334 ? 1.652   -14.156 16.051  1.00 47.89  ? 852  VAL   A CG2  1 
ATOM   2814 N  N    . GLU   A 1 335 ? 5.910   -13.924 13.877  1.00 56.07  ? 853  GLU   A N    1 
ATOM   2815 C  CA   . GLU   A 1 335 ? 7.307   -13.499 13.734  1.00 54.13  ? 853  GLU   A CA   1 
ATOM   2816 C  C    . GLU   A 1 335 ? 7.413   -12.016 13.367  1.00 60.95  ? 853  GLU   A C    1 
ATOM   2817 O  O    . GLU   A 1 335 ? 6.627   -11.510 12.554  1.00 54.42  ? 853  GLU   A O    1 
ATOM   2818 C  CB   . GLU   A 1 335 ? 8.015   -14.329 12.668  1.00 57.40  ? 853  GLU   A CB   1 
ATOM   2819 C  CG   . GLU   A 1 335 ? 9.447   -13.888 12.362  1.00 62.43  ? 853  GLU   A CG   1 
ATOM   2820 C  CD   . GLU   A 1 335 ? 10.156  -14.838 11.409  1.00 81.69  ? 853  GLU   A CD   1 
ATOM   2821 O  OE1  . GLU   A 1 335 ? 9.527   -15.839 11.010  1.00 78.89  ? 853  GLU   A OE1  1 
ATOM   2822 O  OE2  . GLU   A 1 335 ? 11.340  -14.601 11.070  1.00 88.60  ? 853  GLU   A OE2  1 
ATOM   2823 N  N    . GLN   A 1 336 ? 8.382   -11.326 13.965  1.00 62.90  ? 854  GLN   A N    1 
ATOM   2824 C  CA   . GLN   A 1 336 ? 8.648   -9.941  13.611  1.00 68.21  ? 854  GLN   A CA   1 
ATOM   2825 C  C    . GLN   A 1 336 ? 9.312   -9.869  12.244  1.00 72.73  ? 854  GLN   A C    1 
ATOM   2826 O  O    . GLN   A 1 336 ? 10.420  -10.372 12.063  1.00 74.82  ? 854  GLN   A O    1 
ATOM   2827 C  CB   . GLN   A 1 336 ? 9.523   -9.269  14.676  1.00 69.02  ? 854  GLN   A CB   1 
ATOM   2828 C  CG   . GLN   A 1 336 ? 9.510   -7.746  14.635  1.00 66.98  ? 854  GLN   A CG   1 
ATOM   2829 C  CD   . GLN   A 1 336 ? 10.564  -7.131  15.511  1.00 72.08  ? 854  GLN   A CD   1 
ATOM   2830 O  OE1  . GLN   A 1 336 ? 11.549  -7.775  15.849  1.00 85.17  ? 854  GLN   A OE1  1 
ATOM   2831 N  NE2  . GLN   A 1 336 ? 10.340  -5.887  15.930  1.00 81.57  ? 854  GLN   A NE2  1 
ATOM   2832 N  N    . TRP   A 1 337 ? 8.636   -9.227  11.291  1.00 64.39  ? 855  TRP   A N    1 
ATOM   2833 C  CA   . TRP   A 1 337 ? 9.153   -9.115  9.923   1.00 75.61  ? 855  TRP   A CA   1 
ATOM   2834 C  C    . TRP   A 1 337 ? 8.764   -7.788  9.272   1.00 76.83  ? 855  TRP   A C    1 
ATOM   2835 O  O    . TRP   A 1 337 ? 7.639   -7.314  9.428   1.00 67.24  ? 855  TRP   A O    1 
ATOM   2836 C  CB   . TRP   A 1 337 ? 8.651   -10.284 9.060   1.00 72.77  ? 855  TRP   A CB   1 
ATOM   2837 C  CG   . TRP   A 1 337 ? 8.834   -10.065 7.573   1.00 85.66  ? 855  TRP   A CG   1 
ATOM   2838 C  CD1  . TRP   A 1 337 ? 9.933   -10.390 6.825   1.00 90.38  ? 855  TRP   A CD1  1 
ATOM   2839 C  CD2  . TRP   A 1 337 ? 7.893   -9.465  6.661   1.00 87.30  ? 855  TRP   A CD2  1 
ATOM   2840 N  NE1  . TRP   A 1 337 ? 9.735   -10.030 5.510   1.00 97.80  ? 855  TRP   A NE1  1 
ATOM   2841 C  CE2  . TRP   A 1 337 ? 8.493   -9.462  5.384   1.00 93.86  ? 855  TRP   A CE2  1 
ATOM   2842 C  CE3  . TRP   A 1 337 ? 6.606   -8.931  6.802   1.00 87.40  ? 855  TRP   A CE3  1 
ATOM   2843 C  CZ2  . TRP   A 1 337 ? 7.847   -8.945  4.253   1.00 92.23  ? 855  TRP   A CZ2  1 
ATOM   2844 C  CZ3  . TRP   A 1 337 ? 5.968   -8.415  5.672   1.00 86.88  ? 855  TRP   A CZ3  1 
ATOM   2845 C  CH2  . TRP   A 1 337 ? 6.593   -8.428  4.418   1.00 84.56  ? 855  TRP   A CH2  1 
ATOM   2846 N  N    . GLY   A 1 338 ? 9.703   -7.195  8.544   1.00 78.13  ? 856  GLY   A N    1 
ATOM   2847 C  CA   . GLY   A 1 338 ? 9.419   -6.018  7.744   1.00 81.93  ? 856  GLY   A CA   1 
ATOM   2848 C  C    . GLY   A 1 338 ? 9.376   -4.713  8.518   1.00 83.69  ? 856  GLY   A C    1 
ATOM   2849 O  O    . GLY   A 1 338 ? 9.562   -4.693  9.735   1.00 83.48  ? 856  GLY   A O    1 
ATOM   2850 N  N    . THR   A 1 339 ? 9.131   -3.620  7.800   1.00 83.46  ? 857  THR   A N    1 
ATOM   2851 C  CA   . THR   A 1 339 ? 8.967   -2.305  8.409   1.00 84.70  ? 857  THR   A CA   1 
ATOM   2852 C  C    . THR   A 1 339 ? 7.469   -1.987  8.542   1.00 87.20  ? 857  THR   A C    1 
ATOM   2853 O  O    . THR   A 1 339 ? 6.637   -2.670  7.942   1.00 79.32  ? 857  THR   A O    1 
ATOM   2854 C  CB   . THR   A 1 339 ? 9.677   -1.224  7.580   1.00 92.53  ? 857  THR   A CB   1 
ATOM   2855 O  OG1  . THR   A 1 339 ? 9.209   -1.281  6.228   1.00 94.70  ? 857  THR   A OG1  1 
ATOM   2856 C  CG2  . THR   A 1 339 ? 11.189  -1.441  7.604   1.00 98.10  ? 857  THR   A CG2  1 
ATOM   2857 N  N    . PRO   A 1 340 ? 7.112   -0.963  9.342   1.00 90.57  ? 858  PRO   A N    1 
ATOM   2858 C  CA   . PRO   A 1 340 ? 5.690   -0.621  9.486   1.00 86.04  ? 858  PRO   A CA   1 
ATOM   2859 C  C    . PRO   A 1 340 ? 4.980   -0.220  8.184   1.00 83.02  ? 858  PRO   A C    1 
ATOM   2860 O  O    . PRO   A 1 340 ? 3.755   -0.141  8.187   1.00 76.67  ? 858  PRO   A O    1 
ATOM   2861 C  CB   . PRO   A 1 340 ? 5.721   0.563   10.455  1.00 91.27  ? 858  PRO   A CB   1 
ATOM   2862 C  CG   . PRO   A 1 340 ? 6.944   0.342   11.264  1.00 94.09  ? 858  PRO   A CG   1 
ATOM   2863 C  CD   . PRO   A 1 340 ? 7.947   -0.218  10.303  1.00 95.80  ? 858  PRO   A CD   1 
ATOM   2864 N  N    . GLU   A 1 341 ? 5.717   0.009   7.100   1.00 83.82  ? 859  GLU   A N    1 
ATOM   2865 C  CA   . GLU   A 1 341 ? 5.105   0.439   5.844   1.00 86.84  ? 859  GLU   A CA   1 
ATOM   2866 C  C    . GLU   A 1 341 ? 4.281   -0.633  5.133   1.00 83.43  ? 859  GLU   A C    1 
ATOM   2867 O  O    . GLU   A 1 341 ? 3.262   -0.326  4.525   1.00 83.67  ? 859  GLU   A O    1 
ATOM   2868 C  CB   . GLU   A 1 341 ? 6.178   0.967   4.890   1.00 94.66  ? 859  GLU   A CB   1 
ATOM   2869 C  CG   . GLU   A 1 341 ? 6.637   2.380   5.220   1.00 101.37 ? 859  GLU   A CG   1 
ATOM   2870 C  CD   . GLU   A 1 341 ? 7.578   2.441   6.409   1.00 100.01 ? 859  GLU   A CD   1 
ATOM   2871 O  OE1  . GLU   A 1 341 ? 8.000   1.372   6.890   1.00 104.51 ? 859  GLU   A OE1  1 
ATOM   2872 O  OE2  . GLU   A 1 341 ? 7.887   3.560   6.870   1.00 106.35 ? 859  GLU   A OE2  1 
ATOM   2873 N  N    . LYS   A 1 342 ? 4.705   -1.889  5.203   1.00 94.72  ? 860  LYS   A N    1 
ATOM   2874 C  CA   . LYS   A 1 342 ? 3.980   -2.932  4.482   1.00 87.90  ? 860  LYS   A CA   1 
ATOM   2875 C  C    . LYS   A 1 342 ? 2.985   -3.699  5.351   1.00 76.33  ? 860  LYS   A C    1 
ATOM   2876 O  O    . LYS   A 1 342 ? 2.995   -3.623  6.583   1.00 68.55  ? 860  LYS   A O    1 
ATOM   2877 C  CB   . LYS   A 1 342 ? 4.955   -3.911  3.820   1.00 95.59  ? 860  LYS   A CB   1 
ATOM   2878 C  CG   . LYS   A 1 342 ? 5.760   -4.766  4.780   1.00 94.85  ? 860  LYS   A CG   1 
ATOM   2879 C  CD   . LYS   A 1 342 ? 7.107   -4.125  5.135   1.00 104.00 ? 860  LYS   A CD   1 
ATOM   2880 C  CE   . LYS   A 1 342 ? 8.079   -4.096  3.952   1.00 106.26 ? 860  LYS   A CE   1 
ATOM   2881 N  NZ   . LYS   A 1 342 ? 7.972   -2.865  3.122   1.00 109.00 ? 860  LYS   A NZ   1 
ATOM   2882 N  N    . LEU   A 1 343 ? 2.100   -4.418  4.672   1.00 73.52  ? 861  LEU   A N    1 
ATOM   2883 C  CA   . LEU   A 1 343 ? 1.070   -5.222  5.310   1.00 65.25  ? 861  LEU   A CA   1 
ATOM   2884 C  C    . LEU   A 1 343 ? 1.658   -6.547  5.811   1.00 69.07  ? 861  LEU   A C    1 
ATOM   2885 O  O    . LEU   A 1 343 ? 2.692   -6.986  5.312   1.00 65.32  ? 861  LEU   A O    1 
ATOM   2886 C  CB   . LEU   A 1 343 ? -0.064  -5.477  4.317   1.00 66.10  ? 861  LEU   A CB   1 
ATOM   2887 C  CG   . LEU   A 1 343 ? -0.729  -4.238  3.719   1.00 73.77  ? 861  LEU   A CG   1 
ATOM   2888 C  CD1  . LEU   A 1 343 ? -1.523  -4.617  2.490   1.00 76.04  ? 861  LEU   A CD1  1 
ATOM   2889 C  CD2  . LEU   A 1 343 ? -1.638  -3.599  4.747   1.00 72.41  ? 861  LEU   A CD2  1 
ATOM   2890 N  N    . PRO   A 1 344 ? 1.003   -7.181  6.805   1.00 62.41  ? 862  PRO   A N    1 
ATOM   2891 C  CA   . PRO   A 1 344 ? 1.403   -8.511  7.296   1.00 60.08  ? 862  PRO   A CA   1 
ATOM   2892 C  C    . PRO   A 1 344 ? 1.343   -9.583  6.211   1.00 63.23  ? 862  PRO   A C    1 
ATOM   2893 O  O    . PRO   A 1 344 ? 0.394   -9.580  5.431   1.00 64.39  ? 862  PRO   A O    1 
ATOM   2894 C  CB   . PRO   A 1 344 ? 0.368   -8.814  8.391   1.00 51.38  ? 862  PRO   A CB   1 
ATOM   2895 C  CG   . PRO   A 1 344 ? -0.175  -7.494  8.794   1.00 58.24  ? 862  PRO   A CG   1 
ATOM   2896 C  CD   . PRO   A 1 344 ? -0.139  -6.637  7.562   1.00 63.69  ? 862  PRO   A CD   1 
ATOM   2897 N  N    . ARG   A 1 345 ? 2.326   -10.481 6.163   1.00 63.60  ? 863  ARG   A N    1 
ATOM   2898 C  CA   . ARG   A 1 345 ? 2.300   -11.579 5.197   1.00 70.87  ? 863  ARG   A CA   1 
ATOM   2899 C  C    . ARG   A 1 345 ? 2.181   -12.908 5.925   1.00 73.50  ? 863  ARG   A C    1 
ATOM   2900 O  O    . ARG   A 1 345 ? 2.541   -13.025 7.098   1.00 63.12  ? 863  ARG   A O    1 
ATOM   2901 C  CB   . ARG   A 1 345 ? 3.543   -11.576 4.297   1.00 74.80  ? 863  ARG   A CB   1 
ATOM   2902 C  CG   . ARG   A 1 345 ? 4.863   -11.814 5.012   1.00 81.55  ? 863  ARG   A CG   1 
ATOM   2903 C  CD   . ARG   A 1 345 ? 6.006   -12.141 4.032   1.00 91.05  ? 863  ARG   A CD   1 
ATOM   2904 N  NE   . ARG   A 1 345 ? 7.276   -12.349 4.731   1.00 93.30  ? 863  ARG   A NE   1 
ATOM   2905 C  CZ   . ARG   A 1 345 ? 8.409   -12.755 4.158   1.00 98.97  ? 863  ARG   A CZ   1 
ATOM   2906 N  NH1  . ARG   A 1 345 ? 8.459   -13.012 2.860   1.00 103.14 ? 863  ARG   A NH1  1 
ATOM   2907 N  NH2  . ARG   A 1 345 ? 9.503   -12.910 4.892   1.00 98.72  ? 863  ARG   A NH2  1 
ATOM   2908 N  N    . ALA   A 1 346 ? 1.672   -13.911 5.220   1.00 81.40  ? 864  ALA   A N    1 
ATOM   2909 C  CA   . ALA   A 1 346 ? 1.433   -15.214 5.819   1.00 78.68  ? 864  ALA   A CA   1 
ATOM   2910 C  C    . ALA   A 1 346 ? 2.248   -16.312 5.147   1.00 82.73  ? 864  ALA   A C    1 
ATOM   2911 O  O    . ALA   A 1 346 ? 2.318   -16.394 3.919   1.00 88.19  ? 864  ALA   A O    1 
ATOM   2912 C  CB   . ALA   A 1 346 ? -0.045  -15.550 5.761   1.00 80.27  ? 864  ALA   A CB   1 
ATOM   2913 N  N    . HIS   A 1 347 ? 2.872   -17.149 5.967   1.00 76.09  ? 865  HIS   A N    1 
ATOM   2914 C  CA   . HIS   A 1 347 ? 3.509   -18.365 5.486   1.00 75.30  ? 865  HIS   A CA   1 
ATOM   2915 C  C    . HIS   A 1 347 ? 2.664   -19.546 5.930   1.00 74.12  ? 865  HIS   A C    1 
ATOM   2916 O  O    . HIS   A 1 347 ? 2.855   -20.088 7.026   1.00 70.02  ? 865  HIS   A O    1 
ATOM   2917 C  CB   . HIS   A 1 347 ? 4.928   -18.498 6.020   1.00 80.49  ? 865  HIS   A CB   1 
ATOM   2918 C  CG   . HIS   A 1 347 ? 5.849   -17.407 5.580   1.00 83.79  ? 865  HIS   A CG   1 
ATOM   2919 N  ND1  . HIS   A 1 347 ? 6.881   -17.619 4.695   1.00 93.82  ? 865  HIS   A ND1  1 
ATOM   2920 C  CD2  . HIS   A 1 347 ? 5.905   -16.096 5.917   1.00 86.92  ? 865  HIS   A CD2  1 
ATOM   2921 C  CE1  . HIS   A 1 347 ? 7.532   -16.486 4.498   1.00 93.95  ? 865  HIS   A CE1  1 
ATOM   2922 N  NE2  . HIS   A 1 347 ? 6.959   -15.549 5.230   1.00 90.75  ? 865  HIS   A NE2  1 
ATOM   2923 N  N    . THR   A 1 348 ? 1.720   -19.925 5.075   1.00 74.90  ? 866  THR   A N    1 
ATOM   2924 C  CA   . THR   A 1 348 ? 0.723   -20.939 5.401   1.00 73.11  ? 866  THR   A CA   1 
ATOM   2925 C  C    . THR   A 1 348 ? 1.340   -22.297 5.732   1.00 67.54  ? 866  THR   A C    1 
ATOM   2926 O  O    . THR   A 1 348 ? 0.853   -23.004 6.617   1.00 67.36  ? 866  THR   A O    1 
ATOM   2927 C  CB   . THR   A 1 348 ? -0.294  -21.098 4.249   1.00 73.17  ? 866  THR   A CB   1 
ATOM   2928 O  OG1  . THR   A 1 348 ? 0.400   -21.342 3.015   1.00 71.83  ? 866  THR   A OG1  1 
ATOM   2929 C  CG2  . THR   A 1 348 ? -1.140  -19.827 4.122   1.00 66.33  ? 866  THR   A CG2  1 
ATOM   2930 N  N    . CYS   A 1 349 ? 2.420   -22.649 5.042   1.00 74.59  ? 867  CYS   A N    1 
ATOM   2931 C  CA   . CYS   A 1 349 ? 3.107   -23.914 5.298   1.00 80.78  ? 867  CYS   A CA   1 
ATOM   2932 C  C    . CYS   A 1 349 ? 3.591   -24.041 6.747   1.00 79.18  ? 867  CYS   A C    1 
ATOM   2933 O  O    . CYS   A 1 349 ? 3.793   -25.153 7.250   1.00 71.95  ? 867  CYS   A O    1 
ATOM   2934 C  CB   . CYS   A 1 349 ? 4.287   -24.072 4.344   1.00 90.58  ? 867  CYS   A CB   1 
ATOM   2935 S  SG   . CYS   A 1 349 ? 3.793   -24.186 2.629   1.00 103.38 ? 867  CYS   A SG   1 
ATOM   2936 N  N    . PHE   A 1 350 ? 3.758   -22.900 7.414   1.00 67.52  ? 868  PHE   A N    1 
ATOM   2937 C  CA   . PHE   A 1 350 ? 4.278   -22.882 8.772   1.00 63.96  ? 868  PHE   A CA   1 
ATOM   2938 C  C    . PHE   A 1 350 ? 3.288   -22.253 9.740   1.00 63.66  ? 868  PHE   A C    1 
ATOM   2939 O  O    . PHE   A 1 350 ? 3.612   -22.023 10.906  1.00 63.67  ? 868  PHE   A O    1 
ATOM   2940 C  CB   . PHE   A 1 350 ? 5.615   -22.144 8.800   1.00 65.22  ? 868  PHE   A CB   1 
ATOM   2941 C  CG   . PHE   A 1 350 ? 6.566   -22.603 7.724   1.00 78.38  ? 868  PHE   A CG   1 
ATOM   2942 C  CD1  . PHE   A 1 350 ? 7.145   -23.855 7.790   1.00 83.09  ? 868  PHE   A CD1  1 
ATOM   2943 C  CD2  . PHE   A 1 350 ? 6.860   -21.791 6.641   1.00 78.49  ? 868  PHE   A CD2  1 
ATOM   2944 C  CE1  . PHE   A 1 350 ? 8.008   -24.295 6.796   1.00 90.60  ? 868  PHE   A CE1  1 
ATOM   2945 C  CE2  . PHE   A 1 350 ? 7.721   -22.215 5.648   1.00 80.40  ? 868  PHE   A CE2  1 
ATOM   2946 C  CZ   . PHE   A 1 350 ? 8.301   -23.470 5.726   1.00 91.19  ? 868  PHE   A CZ   1 
ATOM   2947 N  N    . ASN   A 1 351 ? 2.080   -21.987 9.245   1.00 59.78  ? 869  ASN   A N    1 
ATOM   2948 C  CA   . ASN   A 1 351 ? 1.044   -21.327 10.025  1.00 53.77  ? 869  ASN   A CA   1 
ATOM   2949 C  C    . ASN   A 1 351 ? 1.613   -20.078 10.708  1.00 59.60  ? 869  ASN   A C    1 
ATOM   2950 O  O    . ASN   A 1 351 ? 1.323   -19.791 11.870  1.00 48.66  ? 869  ASN   A O    1 
ATOM   2951 C  CB   . ASN   A 1 351 ? 0.443   -22.289 11.058  1.00 53.28  ? 869  ASN   A CB   1 
ATOM   2952 C  CG   . ASN   A 1 351 ? -0.147  -23.545 10.427  1.00 63.44  ? 869  ASN   A CG   1 
ATOM   2953 O  OD1  . ASN   A 1 351 ? -0.664  -23.511 9.310   1.00 67.48  ? 869  ASN   A OD1  1 
ATOM   2954 N  ND2  . ASN   A 1 351 ? -0.057  -24.669 11.142  1.00 58.20  ? 869  ASN   A ND2  1 
ATOM   2955 N  N    . ARG   A 1 352 ? 2.445   -19.350 9.975   1.00 61.80  ? 870  ARG   A N    1 
ATOM   2956 C  CA   . ARG   A 1 352 ? 3.183   -18.227 10.542  1.00 62.21  ? 870  ARG   A CA   1 
ATOM   2957 C  C    . ARG   A 1 352 ? 2.724   -16.871 10.021  1.00 57.22  ? 870  ARG   A C    1 
ATOM   2958 O  O    . ARG   A 1 352 ? 2.649   -16.649 8.810   1.00 55.41  ? 870  ARG   A O    1 
ATOM   2959 C  CB   . ARG   A 1 352 ? 4.683   -18.399 10.264  1.00 67.38  ? 870  ARG   A CB   1 
ATOM   2960 C  CG   . ARG   A 1 352 ? 5.528   -17.212 10.704  1.00 60.07  ? 870  ARG   A CG   1 
ATOM   2961 C  CD   . ARG   A 1 352 ? 6.991   -17.483 10.489  1.00 60.69  ? 870  ARG   A CD   1 
ATOM   2962 N  NE   . ARG   A 1 352 ? 7.281   -17.769 9.090   1.00 78.55  ? 870  ARG   A NE   1 
ATOM   2963 C  CZ   . ARG   A 1 352 ? 8.383   -18.378 8.665   1.00 85.53  ? 870  ARG   A CZ   1 
ATOM   2964 N  NH1  . ARG   A 1 352 ? 9.304   -18.777 9.535   1.00 88.59  ? 870  ARG   A NH1  1 
ATOM   2965 N  NH2  . ARG   A 1 352 ? 8.560   -18.596 7.370   1.00 92.99  ? 870  ARG   A NH2  1 
ATOM   2966 N  N    . LEU   A 1 353 ? 2.428   -15.965 10.948  1.00 52.00  ? 871  LEU   A N    1 
ATOM   2967 C  CA   . LEU   A 1 353 ? 2.129   -14.580 10.608  1.00 52.34  ? 871  LEU   A CA   1 
ATOM   2968 C  C    . LEU   A 1 353 ? 3.379   -13.718 10.751  1.00 60.69  ? 871  LEU   A C    1 
ATOM   2969 O  O    . LEU   A 1 353 ? 3.936   -13.590 11.847  1.00 56.14  ? 871  LEU   A O    1 
ATOM   2970 C  CB   . LEU   A 1 353 ? 1.009   -14.026 11.498  1.00 44.35  ? 871  LEU   A CB   1 
ATOM   2971 C  CG   . LEU   A 1 353 ? 0.633   -12.551 11.314  1.00 49.90  ? 871  LEU   A CG   1 
ATOM   2972 C  CD1  . LEU   A 1 353 ? -0.149  -12.317 10.021  1.00 50.16  ? 871  LEU   A CD1  1 
ATOM   2973 C  CD2  . LEU   A 1 353 ? -0.161  -12.052 12.521  1.00 44.76  ? 871  LEU   A CD2  1 
ATOM   2974 N  N    . ASP   A 1 354 ? 3.820   -13.134 9.641   1.00 60.34  ? 872  ASP   A N    1 
ATOM   2975 C  CA   . ASP   A 1 354 ? 4.903   -12.165 9.672   1.00 59.74  ? 872  ASP   A CA   1 
ATOM   2976 C  C    . ASP   A 1 354 ? 4.310   -10.791 9.922   1.00 58.88  ? 872  ASP   A C    1 
ATOM   2977 O  O    . ASP   A 1 354 ? 3.628   -10.229 9.061   1.00 60.09  ? 872  ASP   A O    1 
ATOM   2978 C  CB   . ASP   A 1 354 ? 5.702   -12.199 8.377   1.00 68.96  ? 872  ASP   A CB   1 
ATOM   2979 C  CG   . ASP   A 1 354 ? 6.527   -13.471 8.238   1.00 76.75  ? 872  ASP   A CG   1 
ATOM   2980 O  OD1  . ASP   A 1 354 ? 7.482   -13.476 7.431   1.00 83.13  ? 872  ASP   A OD1  1 
ATOM   2981 O  OD2  . ASP   A 1 354 ? 6.233   -14.458 8.950   1.00 71.49  ? 872  ASP   A OD2  1 
ATOM   2982 N  N    . LEU   A 1 355 ? 4.557   -10.272 11.119  1.00 53.69  ? 873  LEU   A N    1 
ATOM   2983 C  CA   . LEU   A 1 355 ? 3.905   -9.058  11.592  1.00 55.05  ? 873  LEU   A CA   1 
ATOM   2984 C  C    . LEU   A 1 355 ? 4.922   -7.952  11.855  1.00 54.44  ? 873  LEU   A C    1 
ATOM   2985 O  O    . LEU   A 1 355 ? 5.763   -8.077  12.747  1.00 55.16  ? 873  LEU   A O    1 
ATOM   2986 C  CB   . LEU   A 1 355 ? 3.098   -9.358  12.864  1.00 56.63  ? 873  LEU   A CB   1 
ATOM   2987 C  CG   . LEU   A 1 355 ? 2.305   -8.208  13.493  1.00 58.93  ? 873  LEU   A CG   1 
ATOM   2988 C  CD1  . LEU   A 1 355 ? 1.256   -7.667  12.524  1.00 62.09  ? 873  LEU   A CD1  1 
ATOM   2989 C  CD2  . LEU   A 1 355 ? 1.666   -8.625  14.816  1.00 51.11  ? 873  LEU   A CD2  1 
ATOM   2990 N  N    . PRO   A 1 356 ? 4.862   -6.865  11.059  1.00 63.59  ? 874  PRO   A N    1 
ATOM   2991 C  CA   . PRO   A 1 356 ? 5.723   -5.699  11.299  1.00 60.89  ? 874  PRO   A CA   1 
ATOM   2992 C  C    . PRO   A 1 356 ? 5.466   -5.085  12.672  1.00 59.44  ? 874  PRO   A C    1 
ATOM   2993 O  O    . PRO   A 1 356 ? 4.345   -5.183  13.168  1.00 55.93  ? 874  PRO   A O    1 
ATOM   2994 C  CB   . PRO   A 1 356 ? 5.328   -4.729  10.175  1.00 63.77  ? 874  PRO   A CB   1 
ATOM   2995 C  CG   . PRO   A 1 356 ? 4.753   -5.591  9.102   1.00 64.34  ? 874  PRO   A CG   1 
ATOM   2996 C  CD   . PRO   A 1 356 ? 4.069   -6.722  9.823   1.00 57.65  ? 874  PRO   A CD   1 
ATOM   2997 N  N    . PRO   A 1 357 ? 6.484   -4.448  13.271  1.00 62.82  ? 875  PRO   A N    1 
ATOM   2998 C  CA   . PRO   A 1 357 ? 6.339   -3.840  14.594  1.00 68.21  ? 875  PRO   A CA   1 
ATOM   2999 C  C    . PRO   A 1 357 ? 5.652   -2.478  14.523  1.00 63.97  ? 875  PRO   A C    1 
ATOM   3000 O  O    . PRO   A 1 357 ? 6.307   -1.439  14.589  1.00 71.38  ? 875  PRO   A O    1 
ATOM   3001 C  CB   . PRO   A 1 357 ? 7.786   -3.688  15.074  1.00 72.33  ? 875  PRO   A CB   1 
ATOM   3002 C  CG   . PRO   A 1 357 ? 8.659   -3.937  13.848  1.00 78.14  ? 875  PRO   A CG   1 
ATOM   3003 C  CD   . PRO   A 1 357 ? 7.768   -4.083  12.659  1.00 71.62  ? 875  PRO   A CD   1 
ATOM   3004 N  N    . TYR   A 1 358 ? 4.334   -2.490  14.383  1.00 64.58  ? 876  TYR   A N    1 
ATOM   3005 C  CA   . TYR   A 1 358 ? 3.571   -1.253  14.265  1.00 66.30  ? 876  TYR   A CA   1 
ATOM   3006 C  C    . TYR   A 1 358 ? 3.650   -0.409  15.531  1.00 64.23  ? 876  TYR   A C    1 
ATOM   3007 O  O    . TYR   A 1 358 ? 3.810   -0.939  16.631  1.00 62.63  ? 876  TYR   A O    1 
ATOM   3008 C  CB   . TYR   A 1 358 ? 2.119   -1.573  13.918  1.00 65.27  ? 876  TYR   A CB   1 
ATOM   3009 C  CG   . TYR   A 1 358 ? 1.993   -2.311  12.604  1.00 66.31  ? 876  TYR   A CG   1 
ATOM   3010 C  CD1  . TYR   A 1 358 ? 2.434   -1.728  11.419  1.00 67.67  ? 876  TYR   A CD1  1 
ATOM   3011 C  CD2  . TYR   A 1 358 ? 1.450   -3.589  12.546  1.00 54.34  ? 876  TYR   A CD2  1 
ATOM   3012 C  CE1  . TYR   A 1 358 ? 2.331   -2.396  10.210  1.00 70.26  ? 876  TYR   A CE1  1 
ATOM   3013 C  CE2  . TYR   A 1 358 ? 1.334   -4.263  11.339  1.00 58.42  ? 876  TYR   A CE2  1 
ATOM   3014 C  CZ   . TYR   A 1 358 ? 1.778   -3.661  10.174  1.00 65.14  ? 876  TYR   A CZ   1 
ATOM   3015 O  OH   . TYR   A 1 358 ? 1.678   -4.325  8.970   1.00 63.80  ? 876  TYR   A OH   1 
ATOM   3016 N  N    . GLU   A 1 359 ? 3.537   0.909   15.356  1.00 70.40  ? 877  GLU   A N    1 
ATOM   3017 C  CA   . GLU   A 1 359 ? 3.714   1.870   16.440  1.00 75.09  ? 877  GLU   A CA   1 
ATOM   3018 C  C    . GLU   A 1 359 ? 2.405   2.407   17.001  1.00 74.96  ? 877  GLU   A C    1 
ATOM   3019 O  O    . GLU   A 1 359 ? 2.398   3.451   17.660  1.00 74.35  ? 877  GLU   A O    1 
ATOM   3020 C  CB   . GLU   A 1 359 ? 4.564   3.050   15.970  1.00 82.49  ? 877  GLU   A CB   1 
ATOM   3021 C  CG   . GLU   A 1 359 ? 5.983   2.685   15.584  1.00 88.81  ? 877  GLU   A CG   1 
ATOM   3022 C  CD   . GLU   A 1 359 ? 6.703   3.834   14.916  1.00 98.59  ? 877  GLU   A CD   1 
ATOM   3023 O  OE1  . GLU   A 1 359 ? 6.267   4.256   13.824  1.00 98.75  ? 877  GLU   A OE1  1 
ATOM   3024 O  OE2  . GLU   A 1 359 ? 7.704   4.317   15.482  1.00 110.20 ? 877  GLU   A OE2  1 
ATOM   3025 N  N    . SER   A 1 360 ? 1.307   1.706   16.726  1.00 66.20  ? 878  SER   A N    1 
ATOM   3026 C  CA   . SER   A 1 360 ? 0.003   2.053   17.276  1.00 65.52  ? 878  SER   A CA   1 
ATOM   3027 C  C    . SER   A 1 360 ? -0.994  0.924   17.076  1.00 60.71  ? 878  SER   A C    1 
ATOM   3028 O  O    . SER   A 1 360 ? -0.946  0.206   16.068  1.00 58.67  ? 878  SER   A O    1 
ATOM   3029 C  CB   . SER   A 1 360 ? -0.544  3.338   16.640  1.00 69.47  ? 878  SER   A CB   1 
ATOM   3030 O  OG   . SER   A 1 360 ? -1.818  3.649   17.170  1.00 82.13  ? 878  SER   A OG   1 
ATOM   3031 N  N    . PHE   A 1 361 ? -1.903  0.772   18.033  1.00 67.25  ? 879  PHE   A N    1 
ATOM   3032 C  CA   . PHE   A 1 361 ? -2.926  -0.262  17.935  1.00 65.41  ? 879  PHE   A CA   1 
ATOM   3033 C  C    . PHE   A 1 361 ? -3.734  -0.094  16.652  1.00 64.74  ? 879  PHE   A C    1 
ATOM   3034 O  O    . PHE   A 1 361 ? -3.915  -1.048  15.884  1.00 53.53  ? 879  PHE   A O    1 
ATOM   3035 C  CB   . PHE   A 1 361 ? -3.872  -0.236  19.135  1.00 60.32  ? 879  PHE   A CB   1 
ATOM   3036 C  CG   . PHE   A 1 361 ? -5.110  -1.044  18.914  1.00 59.76  ? 879  PHE   A CG   1 
ATOM   3037 C  CD1  . PHE   A 1 361 ? -5.046  -2.441  18.915  1.00 50.72  ? 879  PHE   A CD1  1 
ATOM   3038 C  CD2  . PHE   A 1 361 ? -6.325  -0.422  18.652  1.00 56.13  ? 879  PHE   A CD2  1 
ATOM   3039 C  CE1  . PHE   A 1 361 ? -6.176  -3.202  18.682  1.00 49.41  ? 879  PHE   A CE1  1 
ATOM   3040 C  CE2  . PHE   A 1 361 ? -7.458  -1.174  18.418  1.00 62.29  ? 879  PHE   A CE2  1 
ATOM   3041 C  CZ   . PHE   A 1 361 ? -7.381  -2.580  18.433  1.00 59.79  ? 879  PHE   A CZ   1 
ATOM   3042 N  N    . GLU   A 1 362 ? -4.189  1.134   16.425  1.00 59.66  ? 880  GLU   A N    1 
ATOM   3043 C  CA   . GLU   A 1 362 ? -5.056  1.454   15.296  1.00 66.10  ? 880  GLU   A CA   1 
ATOM   3044 C  C    . GLU   A 1 362 ? -4.363  1.186   13.952  1.00 66.72  ? 880  GLU   A C    1 
ATOM   3045 O  O    . GLU   A 1 362 ? -4.988  0.692   13.012  1.00 64.50  ? 880  GLU   A O    1 
ATOM   3046 C  CB   . GLU   A 1 362 ? -5.524  2.906   15.398  1.00 71.47  ? 880  GLU   A CB   1 
ATOM   3047 C  CG   . GLU   A 1 362 ? -7.032  3.083   15.245  1.00 78.76  ? 880  GLU   A CG   1 
ATOM   3048 C  CD   . GLU   A 1 362 ? -7.852  2.322   16.284  1.00 80.12  ? 880  GLU   A CD   1 
ATOM   3049 O  OE1  . GLU   A 1 362 ? -7.579  2.450   17.492  1.00 79.92  ? 880  GLU   A OE1  1 
ATOM   3050 O  OE2  . GLU   A 1 362 ? -8.774  1.583   15.886  1.00 83.22  ? 880  GLU   A OE2  1 
ATOM   3051 N  N    . GLU   A 1 363 ? -3.070  1.482   13.866  1.00 63.34  ? 881  GLU   A N    1 
ATOM   3052 C  CA   . GLU   A 1 363 ? -2.288  1.095   12.694  1.00 64.40  ? 881  GLU   A CA   1 
ATOM   3053 C  C    . GLU   A 1 363 ? -2.239  -0.432  12.525  1.00 62.06  ? 881  GLU   A C    1 
ATOM   3054 O  O    . GLU   A 1 363 ? -2.365  -0.957  11.411  1.00 57.83  ? 881  GLU   A O    1 
ATOM   3055 C  CB   . GLU   A 1 363 ? -0.859  1.644   12.777  1.00 65.35  ? 881  GLU   A CB   1 
ATOM   3056 C  CG   . GLU   A 1 363 ? -0.007  1.228   11.591  1.00 66.46  ? 881  GLU   A CG   1 
ATOM   3057 C  CD   . GLU   A 1 363 ? 1.405   1.785   11.623  1.00 77.89  ? 881  GLU   A CD   1 
ATOM   3058 O  OE1  . GLU   A 1 363 ? 1.859   2.225   12.702  1.00 84.87  ? 881  GLU   A OE1  1 
ATOM   3059 O  OE2  . GLU   A 1 363 ? 2.058   1.786   10.554  1.00 73.29  ? 881  GLU   A OE2  1 
ATOM   3060 N  N    . LEU   A 1 364 ? -2.043  -1.145  13.624  1.00 55.20  ? 882  LEU   A N    1 
ATOM   3061 C  CA   . LEU   A 1 364 ? -2.025  -2.599  13.547  1.00 55.18  ? 882  LEU   A CA   1 
ATOM   3062 C  C    . LEU   A 1 364 ? -3.388  -3.073  13.056  1.00 51.02  ? 882  LEU   A C    1 
ATOM   3063 O  O    . LEU   A 1 364 ? -3.474  -3.901  12.153  1.00 49.52  ? 882  LEU   A O    1 
ATOM   3064 C  CB   . LEU   A 1 364 ? -1.680  -3.224  14.897  1.00 49.59  ? 882  LEU   A CB   1 
ATOM   3065 C  CG   . LEU   A 1 364 ? -1.507  -4.744  14.924  1.00 46.61  ? 882  LEU   A CG   1 
ATOM   3066 C  CD1  . LEU   A 1 364 ? -0.483  -5.122  15.980  1.00 46.34  ? 882  LEU   A CD1  1 
ATOM   3067 C  CD2  . LEU   A 1 364 ? -2.839  -5.476  15.178  1.00 44.51  ? 882  LEU   A CD2  1 
ATOM   3068 N  N    . TRP   A 1 365 ? -4.445  -2.520  13.649  1.00 57.27  ? 883  TRP   A N    1 
ATOM   3069 C  CA   . TRP   A 1 365 ? -5.818  -2.869  13.282  1.00 53.13  ? 883  TRP   A CA   1 
ATOM   3070 C  C    . TRP   A 1 365 ? -6.044  -2.694  11.785  1.00 53.26  ? 883  TRP   A C    1 
ATOM   3071 O  O    . TRP   A 1 365 ? -6.502  -3.628  11.113  1.00 54.53  ? 883  TRP   A O    1 
ATOM   3072 C  CB   . TRP   A 1 365 ? -6.830  -2.024  14.074  1.00 59.40  ? 883  TRP   A CB   1 
ATOM   3073 C  CG   . TRP   A 1 365 ? -8.245  -2.274  13.662  1.00 57.25  ? 883  TRP   A CG   1 
ATOM   3074 C  CD1  . TRP   A 1 365 ? -8.978  -1.545  12.779  1.00 56.27  ? 883  TRP   A CD1  1 
ATOM   3075 C  CD2  . TRP   A 1 365 ? -9.087  -3.353  14.087  1.00 61.04  ? 883  TRP   A CD2  1 
ATOM   3076 N  NE1  . TRP   A 1 365 ? -10.234 -2.083  12.640  1.00 62.82  ? 883  TRP   A NE1  1 
ATOM   3077 C  CE2  . TRP   A 1 365 ? -10.327 -3.197  13.427  1.00 63.83  ? 883  TRP   A CE2  1 
ATOM   3078 C  CE3  . TRP   A 1 365 ? -8.914  -4.431  14.963  1.00 49.10  ? 883  TRP   A CE3  1 
ATOM   3079 C  CZ2  . TRP   A 1 365 ? -11.396 -4.083  13.616  1.00 58.86  ? 883  TRP   A CZ2  1 
ATOM   3080 C  CZ3  . TRP   A 1 365 ? -9.976  -5.310  15.150  1.00 56.89  ? 883  TRP   A CZ3  1 
ATOM   3081 C  CH2  . TRP   A 1 365 ? -11.208 -5.124  14.479  1.00 51.67  ? 883  TRP   A CH2  1 
ATOM   3082 N  N    . ASP   A 1 366 ? -5.693  -1.514  11.272  1.00 55.77  ? 884  ASP   A N    1 
ATOM   3083 C  CA   . ASP   A 1 366 ? -5.814  -1.198  9.847   1.00 58.64  ? 884  ASP   A CA   1 
ATOM   3084 C  C    . ASP   A 1 366 ? -4.986  -2.116  8.935   1.00 59.52  ? 884  ASP   A C    1 
ATOM   3085 O  O    . ASP   A 1 366 ? -5.469  -2.564  7.898   1.00 58.98  ? 884  ASP   A O    1 
ATOM   3086 C  CB   . ASP   A 1 366 ? -5.398  0.251   9.590   1.00 62.90  ? 884  ASP   A CB   1 
ATOM   3087 C  CG   . ASP   A 1 366 ? -6.368  1.258   10.190  1.00 70.25  ? 884  ASP   A CG   1 
ATOM   3088 O  OD1  . ASP   A 1 366 ? -7.526  0.871   10.464  1.00 66.77  ? 884  ASP   A OD1  1 
ATOM   3089 O  OD2  . ASP   A 1 366 ? -5.976  2.433   10.378  1.00 68.43  ? 884  ASP   A OD2  1 
ATOM   3090 N  N    . LYS   A 1 367 ? -3.739  -2.379  9.311   1.00 56.87  ? 885  LYS   A N    1 
ATOM   3091 C  CA   . LYS   A 1 367 ? -2.840  -3.152  8.455   1.00 57.21  ? 885  LYS   A CA   1 
ATOM   3092 C  C    . LYS   A 1 367 ? -3.233  -4.631  8.393   1.00 65.67  ? 885  LYS   A C    1 
ATOM   3093 O  O    . LYS   A 1 367 ? -3.227  -5.252  7.331   1.00 63.85  ? 885  LYS   A O    1 
ATOM   3094 C  CB   . LYS   A 1 367 ? -1.398  -3.014  8.947   1.00 57.63  ? 885  LYS   A CB   1 
ATOM   3095 C  CG   . LYS   A 1 367 ? -0.788  -1.617  8.755   1.00 62.01  ? 885  LYS   A CG   1 
ATOM   3096 C  CD   . LYS   A 1 367 ? -0.645  -1.288  7.292   1.00 66.25  ? 885  LYS   A CD   1 
ATOM   3097 C  CE   . LYS   A 1 367 ? 0.563   -0.378  7.021   1.00 81.34  ? 885  LYS   A CE   1 
ATOM   3098 N  NZ   . LYS   A 1 367 ? 0.570   0.909   7.791   1.00 73.19  ? 885  LYS   A NZ   1 
ATOM   3099 N  N    . LEU   A 1 368 ? -3.573  -5.184  9.550   1.00 60.48  ? 886  LEU   A N    1 
ATOM   3100 C  CA   . LEU   A 1 368 ? -3.983  -6.572  9.663   1.00 55.90  ? 886  LEU   A CA   1 
ATOM   3101 C  C    . LEU   A 1 368 ? -5.297  -6.829  8.917   1.00 59.54  ? 886  LEU   A C    1 
ATOM   3102 O  O    . LEU   A 1 368 ? -5.424  -7.814  8.192   1.00 52.87  ? 886  LEU   A O    1 
ATOM   3103 C  CB   . LEU   A 1 368 ? -4.122  -6.941  11.133  1.00 50.86  ? 886  LEU   A CB   1 
ATOM   3104 C  CG   . LEU   A 1 368 ? -4.515  -8.367  11.488  1.00 56.24  ? 886  LEU   A CG   1 
ATOM   3105 C  CD1  . LEU   A 1 368 ? -3.438  -9.330  11.007  1.00 54.90  ? 886  LEU   A CD1  1 
ATOM   3106 C  CD2  . LEU   A 1 368 ? -4.737  -8.474  13.003  1.00 52.53  ? 886  LEU   A CD2  1 
ATOM   3107 N  N    . GLN   A 1 369 ? -6.263  -5.929  9.090   1.00 60.29  ? 887  GLN   A N    1 
ATOM   3108 C  CA   . GLN   A 1 369 ? -7.566  -6.052  8.440   1.00 61.59  ? 887  GLN   A CA   1 
ATOM   3109 C  C    . GLN   A 1 369 ? -7.445  -5.979  6.918   1.00 65.66  ? 887  GLN   A C    1 
ATOM   3110 O  O    . GLN   A 1 369 ? -8.154  -6.684  6.196   1.00 63.33  ? 887  GLN   A O    1 
ATOM   3111 C  CB   . GLN   A 1 369 ? -8.521  -4.960  8.943   1.00 59.98  ? 887  GLN   A CB   1 
ATOM   3112 C  CG   . GLN   A 1 369 ? -9.993  -5.188  8.601   1.00 74.07  ? 887  GLN   A CG   1 
ATOM   3113 C  CD   . GLN   A 1 369 ? -10.731 -6.007  9.661   1.00 81.72  ? 887  GLN   A CD   1 
ATOM   3114 O  OE1  . GLN   A 1 369 ? -11.737 -6.665  9.373   1.00 88.01  ? 887  GLN   A OE1  1 
ATOM   3115 N  NE2  . GLN   A 1 369 ? -10.228 -5.972  10.889  1.00 78.90  ? 887  GLN   A NE2  1 
ATOM   3116 N  N    . MET   A 1 370 ? -6.546  -5.123  6.436   1.00 61.62  ? 888  MET   A N    1 
ATOM   3117 C  CA   . MET   A 1 370 ? -6.328  -4.979  5.001   1.00 64.07  ? 888  MET   A CA   1 
ATOM   3118 C  C    . MET   A 1 370 ? -5.809  -6.281  4.414   1.00 61.31  ? 888  MET   A C    1 
ATOM   3119 O  O    . MET   A 1 370 ? -6.258  -6.738  3.361   1.00 68.16  ? 888  MET   A O    1 
ATOM   3120 C  CB   . MET   A 1 370 ? -5.344  -3.848  4.714   1.00 68.52  ? 888  MET   A CB   1 
ATOM   3121 C  CG   . MET   A 1 370 ? -5.261  -3.466  3.244   1.00 84.25  ? 888  MET   A CG   1 
ATOM   3122 S  SD   . MET   A 1 370 ? -6.813  -2.810  2.580   1.00 92.44  ? 888  MET   A SD   1 
ATOM   3123 C  CE   . MET   A 1 370 ? -7.120  -1.428  3.685   1.00 89.30  ? 888  MET   A CE   1 
ATOM   3124 N  N    . ALA   A 1 371 ? -4.853  -6.873  5.115   1.00 59.18  ? 889  ALA   A N    1 
ATOM   3125 C  CA   . ALA   A 1 371 ? -4.237  -8.118  4.681   1.00 58.93  ? 889  ALA   A CA   1 
ATOM   3126 C  C    . ALA   A 1 371 ? -5.270  -9.238  4.542   1.00 58.45  ? 889  ALA   A C    1 
ATOM   3127 O  O    . ALA   A 1 371 ? -5.265  -9.966  3.553   1.00 62.08  ? 889  ALA   A O    1 
ATOM   3128 C  CB   . ALA   A 1 371 ? -3.152  -8.515  5.644   1.00 55.43  ? 889  ALA   A CB   1 
ATOM   3129 N  N    . ILE   A 1 372 ? -6.167  -9.344  5.520   1.00 58.59  ? 890  ILE   A N    1 
ATOM   3130 C  CA   . ILE   A 1 372 ? -7.169  -10.415 5.561   1.00 64.14  ? 890  ILE   A CA   1 
ATOM   3131 C  C    . ILE   A 1 372 ? -8.199  -10.354 4.431   1.00 68.49  ? 890  ILE   A C    1 
ATOM   3132 O  O    . ILE   A 1 372 ? -8.535  -11.378 3.840   1.00 74.01  ? 890  ILE   A O    1 
ATOM   3133 C  CB   . ILE   A 1 372 ? -7.945  -10.412 6.907   1.00 63.64  ? 890  ILE   A CB   1 
ATOM   3134 C  CG1  . ILE   A 1 372 ? -6.980  -10.507 8.086   1.00 60.85  ? 890  ILE   A CG1  1 
ATOM   3135 C  CG2  . ILE   A 1 372 ? -8.939  -11.568 6.964   1.00 67.87  ? 890  ILE   A CG2  1 
ATOM   3136 C  CD1  . ILE   A 1 372 ? -5.886  -11.530 7.886   1.00 63.26  ? 890  ILE   A CD1  1 
ATOM   3137 N  N    . GLU   A 1 373 ? -8.701  -9.160  4.128   1.00 74.16  ? 891  GLU   A N    1 
ATOM   3138 C  CA   . GLU   A 1 373 ? -9.811  -9.034  3.188   1.00 88.71  ? 891  GLU   A CA   1 
ATOM   3139 C  C    . GLU   A 1 373 ? -9.374  -9.236  1.735   1.00 99.10  ? 891  GLU   A C    1 
ATOM   3140 O  O    . GLU   A 1 373 ? -10.175 -9.078  0.815   1.00 99.45  ? 891  GLU   A O    1 
ATOM   3141 C  CB   . GLU   A 1 373 ? -10.499 -7.676  3.341   1.00 87.91  ? 891  GLU   A CB   1 
ATOM   3142 C  CG   . GLU   A 1 373 ? -9.708  -6.505  2.791   1.00 94.23  ? 891  GLU   A CG   1 
ATOM   3143 C  CD   . GLU   A 1 373 ? -10.464 -5.193  2.897   1.00 102.51 ? 891  GLU   A CD   1 
ATOM   3144 O  OE1  . GLU   A 1 373 ? -11.179 -4.992  3.904   1.00 103.48 ? 891  GLU   A OE1  1 
ATOM   3145 O  OE2  . GLU   A 1 373 ? -10.355 -4.368  1.966   1.00 106.50 ? 891  GLU   A OE2  1 
ATOM   3146 N  N    . ASN   A 1 374 ? -8.107  -9.586  1.530   1.00 108.46 ? 892  ASN   A N    1 
ATOM   3147 C  CA   . ASN   A 1 374 ? -7.654  -10.016 0.213   1.00 119.48 ? 892  ASN   A CA   1 
ATOM   3148 C  C    . ASN   A 1 374 ? -7.860  -11.523 0.044   1.00 121.73 ? 892  ASN   A C    1 
ATOM   3149 O  O    . ASN   A 1 374 ? -7.948  -12.021 -1.074  1.00 128.85 ? 892  ASN   A O    1 
ATOM   3150 C  CB   . ASN   A 1 374 ? -6.184  -9.647  -0.011  1.00 122.40 ? 892  ASN   A CB   1 
ATOM   3151 C  CG   . ASN   A 1 374 ? -5.240  -10.823 0.199   1.00 122.52 ? 892  ASN   A CG   1 
ATOM   3152 O  OD1  . ASN   A 1 374 ? -5.250  -11.474 1.248   1.00 122.07 ? 892  ASN   A OD1  1 
ATOM   3153 N  ND2  . ASN   A 1 374 ? -4.417  -11.102 -0.807  1.00 122.79 ? 892  ASN   A ND2  1 
ATOM   3154 N  N    . THR   A 1 375 ? -7.934  -12.239 1.165   1.00 113.11 ? 893  THR   A N    1 
ATOM   3155 C  CA   . THR   A 1 375 ? -8.116  -13.689 1.158   1.00 106.93 ? 893  THR   A CA   1 
ATOM   3156 C  C    . THR   A 1 375 ? -9.592  -14.063 1.254   1.00 107.53 ? 893  THR   A C    1 
ATOM   3157 O  O    . THR   A 1 375 ? -10.275 -13.689 2.209   1.00 104.16 ? 893  THR   A O    1 
ATOM   3158 C  CB   . THR   A 1 375 ? -7.351  -14.360 2.319   1.00 98.34  ? 893  THR   A CB   1 
HETATM 3159 C  C1   . EDO   B 2 .   ? -36.882 -14.786 11.116  1.00 47.82  ? 901  EDO   A C1   1 
HETATM 3160 O  O1   . EDO   B 2 .   ? -36.771 -15.882 10.202  1.00 45.77  ? 901  EDO   A O1   1 
HETATM 3161 C  C2   . EDO   B 2 .   ? -38.327 -14.323 11.184  1.00 44.78  ? 901  EDO   A C2   1 
HETATM 3162 O  O2   . EDO   B 2 .   ? -39.133 -15.485 11.382  1.00 51.44  ? 901  EDO   A O2   1 
HETATM 3163 C  C1   . EDO   C 2 .   ? -31.971 -27.409 -18.251 1.00 59.57  ? 902  EDO   A C1   1 
HETATM 3164 O  O1   . EDO   C 2 .   ? -33.330 -26.983 -18.443 1.00 60.59  ? 902  EDO   A O1   1 
HETATM 3165 C  C2   . EDO   C 2 .   ? -31.552 -27.161 -16.806 1.00 61.08  ? 902  EDO   A C2   1 
HETATM 3166 O  O2   . EDO   C 2 .   ? -30.572 -28.124 -16.373 1.00 58.18  ? 902  EDO   A O2   1 
HETATM 3167 C  C1   . EDO   D 2 .   ? -34.381 -18.974 10.230  1.00 51.86  ? 903  EDO   A C1   1 
HETATM 3168 O  O1   . EDO   D 2 .   ? -34.973 -17.864 9.553   1.00 41.43  ? 903  EDO   A O1   1 
HETATM 3169 C  C2   . EDO   D 2 .   ? -35.222 -19.449 11.417  1.00 46.80  ? 903  EDO   A C2   1 
HETATM 3170 O  O2   . EDO   D 2 .   ? -35.665 -18.346 12.225  1.00 40.34  ? 903  EDO   A O2   1 
HETATM 3171 C  C1   . EDO   E 2 .   ? -51.740 -3.456  13.549  1.00 53.12  ? 904  EDO   A C1   1 
HETATM 3172 O  O1   . EDO   E 2 .   ? -51.364 -3.394  14.935  1.00 46.56  ? 904  EDO   A O1   1 
HETATM 3173 C  C2   . EDO   E 2 .   ? -50.539 -3.723  12.647  1.00 59.77  ? 904  EDO   A C2   1 
HETATM 3174 O  O2   . EDO   E 2 .   ? -50.242 -5.128  12.638  1.00 68.14  ? 904  EDO   A O2   1 
HETATM 3175 C  C01  . A1ITH F 3 .   ? -37.915 -9.653  -8.505  1.00 56.64  ? 905  A1ITH A C01  1 
HETATM 3176 N  N02  . A1ITH F 3 .   ? -37.621 -11.018 -8.102  1.00 58.75  ? 905  A1ITH A N02  1 
HETATM 3177 C  C03  . A1ITH F 3 .   ? -36.189 -11.159 -7.871  1.00 60.44  ? 905  A1ITH A C03  1 
HETATM 3178 C  C04  . A1ITH F 3 .   ? -35.819 -12.635 -7.829  1.00 56.03  ? 905  A1ITH A C04  1 
HETATM 3179 C  C05  . A1ITH F 3 .   ? -34.454 -12.964 -7.212  1.00 44.78  ? 905  A1ITH A C05  1 
HETATM 3180 N  N06  . A1ITH F 3 .   ? -33.729 -13.841 -8.130  1.00 38.43  ? 905  A1ITH A N06  1 
HETATM 3181 C  C07  . A1ITH F 3 .   ? -32.981 -13.231 -9.227  1.00 50.42  ? 905  A1ITH A C07  1 
HETATM 3182 C  C08  . A1ITH F 3 .   ? -31.910 -12.325 -9.026  1.00 49.04  ? 905  A1ITH A C08  1 
HETATM 3183 C  C09  . A1ITH F 3 .   ? -31.232 -11.809 -10.115 1.00 50.98  ? 905  A1ITH A C09  1 
HETATM 3184 C  C10  . A1ITH F 3 .   ? -31.596 -12.192 -11.391 1.00 56.81  ? 905  A1ITH A C10  1 
HETATM 3185 C  C11  . A1ITH F 3 .   ? -32.633 -13.092 -11.583 1.00 59.53  ? 905  A1ITH A C11  1 
HETATM 3186 C  C12  . A1ITH F 3 .   ? -33.318 -13.612 -10.461 1.00 56.18  ? 905  A1ITH A C12  1 
HETATM 3187 C  C13  . A1ITH F 3 .   ? -34.473 -14.613 -10.590 1.00 57.14  ? 905  A1ITH A C13  1 
HETATM 3188 C  C14  . A1ITH F 3 .   ? -34.011 -16.023 -10.239 1.00 44.24  ? 905  A1ITH A C14  1 
HETATM 3189 C  C15  . A1ITH F 3 .   ? -33.535 -16.218 -8.767  1.00 40.62  ? 905  A1ITH A C15  1 
HETATM 3190 C  C16  . A1ITH F 3 .   ? -33.439 -15.227 -7.788  1.00 41.38  ? 905  A1ITH A C16  1 
HETATM 3191 C  C17  . A1ITH F 3 .   ? -32.971 -15.508 -6.477  1.00 38.27  ? 905  A1ITH A C17  1 
HETATM 3192 C  C18  . A1ITH F 3 .   ? -32.665 -16.834 -6.207  1.00 39.67  ? 905  A1ITH A C18  1 
HETATM 3193 C  C19  . A1ITH F 3 .   ? -32.773 -17.831 -7.172  1.00 37.75  ? 905  A1ITH A C19  1 
HETATM 3194 C  C20  . A1ITH F 3 .   ? -33.211 -17.545 -8.466  1.00 34.78  ? 905  A1ITH A C20  1 
HETATM 3195 CL CL21 . A1ITH F 3 .   ? -32.094 -17.332 -4.622  1.00 55.46  ? 905  A1ITH A CL21 1 
HETATM 3196 O  O    . HOH   G 4 .   ? -46.263 -7.587  15.337  1.00 67.27  ? 1001 HOH   A O    1 
HETATM 3197 O  O    . HOH   G 4 .   ? -51.189 -5.493  42.219  1.00 44.55  ? 1002 HOH   A O    1 
HETATM 3198 O  O    . HOH   G 4 .   ? -44.676 -14.974 6.217   1.00 50.06  ? 1003 HOH   A O    1 
HETATM 3199 O  O    . HOH   G 4 .   ? -46.655 -11.694 12.797  1.00 51.73  ? 1004 HOH   A O    1 
HETATM 3200 O  O    . HOH   G 4 .   ? -29.955 -12.324 -14.282 1.00 46.09  ? 1005 HOH   A O    1 
HETATM 3201 O  O    . HOH   G 4 .   ? 0.562   -15.963 23.620  1.00 44.49  ? 1006 HOH   A O    1 
HETATM 3202 O  O    . HOH   G 4 .   ? -37.527 -27.274 14.810  1.00 44.40  ? 1007 HOH   A O    1 
HETATM 3203 O  O    . HOH   G 4 .   ? -56.826 -10.597 20.067  1.00 48.49  ? 1008 HOH   A O    1 
HETATM 3204 O  O    . HOH   G 4 .   ? -8.374  2.619   19.795  1.00 62.63  ? 1009 HOH   A O    1 
HETATM 3205 O  O    . HOH   G 4 .   ? -46.962 -17.579 17.698  1.00 32.25  ? 1010 HOH   A O    1 
HETATM 3206 O  O    . HOH   G 4 .   ? -39.927 2.118   12.773  1.00 44.70  ? 1011 HOH   A O    1 
HETATM 3207 O  O    . HOH   G 4 .   ? -43.643 -18.970 -4.392  1.00 37.39  ? 1012 HOH   A O    1 
HETATM 3208 O  O    . HOH   G 4 .   ? 8.455   -0.203  14.512  1.00 48.24  ? 1013 HOH   A O    1 
HETATM 3209 O  O    . HOH   G 4 .   ? -29.691 -34.274 15.326  1.00 43.30  ? 1014 HOH   A O    1 
HETATM 3210 O  O    . HOH   G 4 .   ? -48.455 -15.417 16.219  1.00 69.23  ? 1015 HOH   A O    1 
HETATM 3211 O  O    . HOH   G 4 .   ? 5.975   -0.683  17.890  1.00 59.26  ? 1016 HOH   A O    1 
HETATM 3212 O  O    . HOH   G 4 .   ? -19.130 -31.410 18.802  1.00 40.17  ? 1017 HOH   A O    1 
HETATM 3213 O  O    . HOH   G 4 .   ? -13.537 -14.308 -19.395 1.00 48.78  ? 1018 HOH   A O    1 
HETATM 3214 O  O    . HOH   G 4 .   ? -42.603 -20.924 -5.911  1.00 35.93  ? 1019 HOH   A O    1 
HETATM 3215 O  O    . HOH   G 4 .   ? -35.031 -30.342 -10.842 1.00 33.92  ? 1020 HOH   A O    1 
HETATM 3216 O  O    . HOH   G 4 .   ? 5.849   -21.524 12.529  1.00 65.93  ? 1021 HOH   A O    1 
HETATM 3217 O  O    . HOH   G 4 .   ? -47.285 -9.307  25.854  1.00 40.84  ? 1022 HOH   A O    1 
HETATM 3218 O  O    . HOH   G 4 .   ? -19.588 -31.949 3.828   1.00 49.16  ? 1023 HOH   A O    1 
HETATM 3219 O  O    . HOH   G 4 .   ? -31.565 -12.818 -0.243  1.00 30.09  ? 1024 HOH   A O    1 
HETATM 3220 O  O    . HOH   G 4 .   ? -43.468 -13.649 2.647   1.00 48.62  ? 1025 HOH   A O    1 
HETATM 3221 O  O    . HOH   G 4 .   ? -27.422 -14.309 15.753  1.00 42.00  ? 1026 HOH   A O    1 
HETATM 3222 O  O    . HOH   G 4 .   ? -45.066 5.891   10.052  1.00 48.37  ? 1027 HOH   A O    1 
HETATM 3223 O  O    . HOH   G 4 .   ? -33.862 -9.004  2.580   1.00 35.14  ? 1028 HOH   A O    1 
HETATM 3224 O  O    . HOH   G 4 .   ? -36.259 -9.607  18.319  1.00 58.95  ? 1029 HOH   A O    1 
HETATM 3225 O  O    . HOH   G 4 .   ? -26.117 -45.015 -4.106  1.00 58.08  ? 1030 HOH   A O    1 
HETATM 3226 O  O    . HOH   G 4 .   ? -26.195 -12.882 -10.440 1.00 36.43  ? 1031 HOH   A O    1 
HETATM 3227 O  O    . HOH   G 4 .   ? -42.020 -22.117 26.963  1.00 30.78  ? 1032 HOH   A O    1 
HETATM 3228 O  O    . HOH   G 4 .   ? -36.222 -9.532  -5.199  1.00 51.27  ? 1033 HOH   A O    1 
HETATM 3229 O  O    . HOH   G 4 .   ? -36.656 -33.566 -0.112  1.00 41.00  ? 1034 HOH   A O    1 
HETATM 3230 O  O    . HOH   G 4 .   ? -16.504 -27.714 -11.648 1.00 53.58  ? 1035 HOH   A O    1 
HETATM 3231 O  O    . HOH   G 4 .   ? -49.078 -10.261 32.863  1.00 33.21  ? 1036 HOH   A O    1 
HETATM 3232 O  O    . HOH   G 4 .   ? -1.394  -23.104 17.602  1.00 43.48  ? 1037 HOH   A O    1 
HETATM 3233 O  O    . HOH   G 4 .   ? -24.200 -33.018 -16.919 1.00 42.07  ? 1038 HOH   A O    1 
HETATM 3234 O  O    . HOH   G 4 .   ? -48.409 -3.502  24.820  1.00 56.01  ? 1039 HOH   A O    1 
HETATM 3235 O  O    . HOH   G 4 .   ? -35.909 -39.588 -18.449 1.00 59.75  ? 1040 HOH   A O    1 
HETATM 3236 O  O    . HOH   G 4 .   ? -37.836 -16.781 -11.480 1.00 48.31  ? 1041 HOH   A O    1 
HETATM 3237 O  O    . HOH   G 4 .   ? -20.557 -23.960 14.765  1.00 44.19  ? 1042 HOH   A O    1 
HETATM 3238 O  O    . HOH   G 4 .   ? -32.662 -36.848 -4.637  1.00 43.90  ? 1043 HOH   A O    1 
HETATM 3239 O  O    . HOH   G 4 .   ? 6.006   -15.383 25.090  1.00 49.09  ? 1044 HOH   A O    1 
HETATM 3240 O  O    . HOH   G 4 .   ? -0.767  -13.141 25.093  1.00 60.90  ? 1045 HOH   A O    1 
HETATM 3241 O  O    . HOH   G 4 .   ? -55.190 -15.342 32.141  1.00 46.72  ? 1046 HOH   A O    1 
HETATM 3242 O  O    . HOH   G 4 .   ? -28.200 -22.256 -17.016 1.00 38.06  ? 1047 HOH   A O    1 
HETATM 3243 O  O    . HOH   G 4 .   ? -47.363 -20.656 16.686  1.00 49.86  ? 1048 HOH   A O    1 
HETATM 3244 O  O    . HOH   G 4 .   ? 8.171   -20.464 11.416  1.00 46.84  ? 1049 HOH   A O    1 
HETATM 3245 O  O    . HOH   G 4 .   ? -53.004 -2.744  34.187  1.00 35.43  ? 1050 HOH   A O    1 
HETATM 3246 O  O    . HOH   G 4 .   ? -41.649 -16.328 12.234  1.00 45.75  ? 1051 HOH   A O    1 
HETATM 3247 O  O    . HOH   G 4 .   ? -34.376 -37.305 3.512   1.00 45.76  ? 1052 HOH   A O    1 
HETATM 3248 O  O    . HOH   G 4 .   ? -39.983 -29.778 3.757   1.00 41.67  ? 1053 HOH   A O    1 
HETATM 3249 O  O    . HOH   G 4 .   ? -24.092 -10.977 0.050   1.00 42.04  ? 1054 HOH   A O    1 
HETATM 3250 O  O    . HOH   G 4 .   ? -13.899 -20.412 -15.298 1.00 62.26  ? 1055 HOH   A O    1 
HETATM 3251 O  O    . HOH   G 4 .   ? -48.628 2.734   15.290  1.00 37.33  ? 1056 HOH   A O    1 
HETATM 3252 O  O    . HOH   G 4 .   ? -19.488 -29.171 3.700   1.00 40.35  ? 1057 HOH   A O    1 
HETATM 3253 O  O    . HOH   G 4 .   ? -47.234 -10.249 39.500  1.00 46.48  ? 1058 HOH   A O    1 
HETATM 3254 O  O    . HOH   G 4 .   ? -40.591 -22.525 21.054  1.00 53.81  ? 1059 HOH   A O    1 
HETATM 3255 O  O    . HOH   G 4 .   ? -25.281 -35.402 -13.532 1.00 37.49  ? 1060 HOH   A O    1 
HETATM 3256 O  O    . HOH   G 4 .   ? -17.955 -20.578 -0.348  1.00 48.27  ? 1061 HOH   A O    1 
HETATM 3257 O  O    . HOH   G 4 .   ? -44.429 -19.364 5.450   1.00 39.50  ? 1062 HOH   A O    1 
HETATM 3258 O  O    . HOH   G 4 .   ? 7.114   -18.573 21.748  1.00 42.18  ? 1063 HOH   A O    1 
HETATM 3259 O  O    . HOH   G 4 .   ? -53.198 -8.099  35.809  1.00 41.11  ? 1064 HOH   A O    1 
HETATM 3260 O  O    . HOH   G 4 .   ? -28.124 -13.684 -12.486 1.00 38.13  ? 1065 HOH   A O    1 
HETATM 3261 O  O    . HOH   G 4 .   ? -47.087 -21.779 32.578  1.00 34.04  ? 1066 HOH   A O    1 
HETATM 3262 O  O    . HOH   G 4 .   ? -16.709 -32.690 19.009  1.00 44.28  ? 1067 HOH   A O    1 
HETATM 3263 O  O    . HOH   G 4 .   ? -50.744 -22.830 29.266  1.00 39.81  ? 1068 HOH   A O    1 
HETATM 3264 O  O    . HOH   G 4 .   ? -40.681 -14.007 -7.889  1.00 43.36  ? 1069 HOH   A O    1 
HETATM 3265 O  O    . HOH   G 4 .   ? -24.066 -11.339 14.667  1.00 52.97  ? 1070 HOH   A O    1 
HETATM 3266 O  O    . HOH   G 4 .   ? -39.846 -21.524 28.468  1.00 44.84  ? 1071 HOH   A O    1 
HETATM 3267 O  O    . HOH   G 4 .   ? -15.963 -42.634 12.472  1.00 45.09  ? 1072 HOH   A O    1 
HETATM 3268 O  O    . HOH   G 4 .   ? -33.432 -37.401 -7.735  1.00 42.25  ? 1073 HOH   A O    1 
HETATM 3269 O  O    . HOH   G 4 .   ? -16.538 -30.517 -6.362  1.00 57.08  ? 1074 HOH   A O    1 
HETATM 3270 O  O    . HOH   G 4 .   ? -27.692 -17.200 16.491  1.00 39.95  ? 1075 HOH   A O    1 
HETATM 3271 O  O    . HOH   G 4 .   ? -24.794 -12.085 2.408   1.00 52.43  ? 1076 HOH   A O    1 
HETATM 3272 O  O    . HOH   G 4 .   ? -55.981 -19.633 18.490  1.00 36.51  ? 1077 HOH   A O    1 
HETATM 3273 O  O    . HOH   G 4 .   ? -50.422 -3.011  35.260  1.00 40.49  ? 1078 HOH   A O    1 
HETATM 3274 O  O    . HOH   G 4 .   ? -49.194 -6.795  26.500  1.00 39.01  ? 1079 HOH   A O    1 
HETATM 3275 O  O    . HOH   G 4 .   ? -39.207 -10.404 14.052  1.00 50.01  ? 1080 HOH   A O    1 
HETATM 3276 O  O    . HOH   G 4 .   ? -24.621 -12.854 -18.789 1.00 49.45  ? 1081 HOH   A O    1 
HETATM 3277 O  O    . HOH   G 4 .   ? -48.313 -22.487 30.081  1.00 39.65  ? 1082 HOH   A O    1 
HETATM 3278 O  O    . HOH   G 4 .   ? -21.667 -39.801 -6.045  1.00 53.49  ? 1083 HOH   A O    1 
HETATM 3279 O  O    . HOH   G 4 .   ? -38.450 -7.043  3.456   1.00 52.98  ? 1084 HOH   A O    1 
HETATM 3280 O  O    . HOH   G 4 .   ? -54.742 -19.354 31.342  1.00 50.07  ? 1085 HOH   A O    1 
HETATM 3281 O  O    . HOH   G 4 .   ? -30.978 -7.182  5.918   1.00 33.47  ? 1086 HOH   A O    1 
HETATM 3282 O  O    . HOH   G 4 .   ? -15.252 -40.297 19.249  1.00 48.50  ? 1087 HOH   A O    1 
HETATM 3283 O  O    . HOH   G 4 .   ? -52.166 -24.467 25.031  1.00 58.24  ? 1088 HOH   A O    1 
HETATM 3284 O  O    . HOH   G 4 .   ? -42.644 -9.004  26.442  1.00 57.37  ? 1089 HOH   A O    1 
HETATM 3285 O  O    . HOH   G 4 .   ? -20.359 -39.073 -1.703  1.00 53.37  ? 1090 HOH   A O    1 
HETATM 3286 O  O    . HOH   G 4 .   ? -45.993 -19.448 -2.744  1.00 46.35  ? 1091 HOH   A O    1 
HETATM 3287 O  O    . HOH   G 4 .   ? -55.510 -8.707  35.785  1.00 46.29  ? 1092 HOH   A O    1 
HETATM 3288 O  O    . HOH   G 4 .   ? -38.138 -33.634 2.032   1.00 42.88  ? 1093 HOH   A O    1 
HETATM 3289 O  O    . HOH   G 4 .   ? -50.018 -25.847 27.529  1.00 52.81  ? 1094 HOH   A O    1 
HETATM 3290 O  O    . HOH   G 4 .   ? -12.901 -17.860 -3.973  1.00 52.76  ? 1095 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   ? 1.3629 0.9761 1.0677 0.0755  -0.2562 0.1385  519 SER A N   
2    C CA  . SER A 1   ? 1.3259 0.9805 1.0775 0.0595  -0.2353 0.1254  519 SER A CA  
3    C C   . SER A 1   ? 1.2663 0.9709 1.0785 0.0767  -0.2429 0.1104  519 SER A C   
4    O O   . SER A 1   ? 1.2807 0.9915 1.1038 0.1022  -0.2640 0.1102  519 SER A O   
5    C CB  . SER A 1   ? 1.2933 0.9757 1.0434 0.0369  -0.2214 0.1224  519 SER A CB  
6    O OG  . SER A 1   ? 1.1944 0.9143 0.9871 0.0231  -0.2024 0.1105  519 SER A OG  
7    N N   . ARG A 2   ? 1.0997 0.8420 0.9514 0.0629  -0.2250 0.0988  520 ARG A N   
8    C CA  . ARG A 2   ? 0.9148 0.7060 0.8237 0.0753  -0.2271 0.0857  520 ARG A CA  
9    C C   . ARG A 2   ? 0.7501 0.5931 0.6903 0.0635  -0.2264 0.0765  520 ARG A C   
10   O O   . ARG A 2   ? 0.6932 0.5385 0.6222 0.0423  -0.2124 0.0752  520 ARG A O   
11   C CB  . ARG A 2   ? 0.8637 0.6516 0.7908 0.0714  -0.2082 0.0794  520 ARG A CB  
12   C CG  . ARG A 2   ? 0.9370 0.6767 0.8420 0.0900  -0.2129 0.0844  520 ARG A CG  
13   C CD  . ARG A 2   ? 0.9609 0.6994 0.8838 0.0873  -0.1961 0.0753  520 ARG A CD  
14   N NE  . ARG A 2   ? 1.0160 0.7112 0.9035 0.0630  -0.1835 0.0810  520 ARG A NE  
15   C CZ  . ARG A 2   ? 1.0216 0.6566 0.8727 0.0658  -0.1850 0.0868  520 ARG A CZ  
16   N NH1 . ARG A 2   ? 1.1013 0.7089 0.9436 0.0960  -0.1978 0.0868  520 ARG A NH1 
17   N NH2 . ARG A 2   ? 1.0439 0.6462 0.8676 0.0384  -0.1741 0.0927  520 ARG A NH2 
18   N N   . ASP A 3   ? 0.6330 0.5171 0.6122 0.0774  -0.2418 0.0704  521 ASP A N   
19   C CA  . ASP A 3   ? 0.6408 0.5723 0.6536 0.0646  -0.2417 0.0609  521 ASP A CA  
20   C C   . ASP A 3   ? 0.5846 0.5427 0.6349 0.0556  -0.2194 0.0517  521 ASP A C   
21   O O   . ASP A 3   ? 0.5436 0.4824 0.5907 0.0592  -0.2056 0.0522  521 ASP A O   
22   C CB  . ASP A 3   ? 0.6541 0.6235 0.6988 0.0788  -0.2672 0.0587  521 ASP A CB  
23   C CG  . ASP A 3   ? 0.6834 0.6787 0.7707 0.1024  -0.2702 0.0571  521 ASP A CG  
24   O OD1 . ASP A 3   ? 0.6186 0.5993 0.7084 0.1080  -0.2521 0.0559  521 ASP A OD1 
25   O OD2 . ASP A 3   ? 0.6853 0.7172 0.8036 0.1157  -0.2912 0.0567  521 ASP A OD2 
26   N N   . TYR A 4   ? 0.5160 0.5141 0.5979 0.0435  -0.2171 0.0434  522 TYR A N   
27   C CA  . TYR A 4   ? 0.4377 0.4570 0.5476 0.0327  -0.1955 0.0357  522 TYR A CA  
28   C C   . TYR A 4   ? 0.3860 0.4224 0.5297 0.0492  -0.1892 0.0330  522 TYR A C   
29   O O   . TYR A 4   ? 0.4969 0.5201 0.6376 0.0471  -0.1712 0.0305  522 TYR A O   
30   C CB  . TYR A 4   ? 0.3654 0.4206 0.5010 0.0176  -0.1966 0.0284  522 TYR A CB  
31   C CG  . TYR A 4   ? 0.4613 0.5379 0.6256 0.0090  -0.1757 0.0216  522 TYR A CG  
32   C CD1 . TYR A 4   ? 0.4556 0.5103 0.5995 -0.0005 -0.1564 0.0207  522 TYR A CD1 
33   C CD2 . TYR A 4   ? 0.5678 0.6880 0.7795 0.0101  -0.1754 0.0172  522 TYR A CD2 
34   C CE1 . TYR A 4   ? 0.5042 0.5753 0.6695 -0.0072 -0.1392 0.0149  522 TYR A CE1 
35   C CE2 . TYR A 4   ? 0.4548 0.5905 0.6868 0.0025  -0.1554 0.0121  522 TYR A CE2 
36   C CZ  . TYR A 4   ? 0.4500 0.5587 0.6564 -0.0052 -0.1383 0.0107  522 TYR A CZ  
37   O OH  . TYR A 4   ? 0.5626 0.6835 0.7843 -0.0116 -0.1203 0.0060  522 TYR A OH  
38   N N   . LYS A 5   ? 0.4610 0.5286 0.6366 0.0664  -0.2043 0.0331  523 LYS A N   
39   C CA  . LYS A 5   ? 0.4650 0.5544 0.6745 0.0862  -0.1968 0.0302  523 LYS A CA  
40   C C   . LYS A 5   ? 0.4933 0.5329 0.6691 0.1027  -0.1912 0.0334  523 LYS A C   
41   O O   . LYS A 5   ? 0.4406 0.4764 0.6235 0.1088  -0.1746 0.0286  523 LYS A O   
42   C CB  . LYS A 5   ? 0.3912 0.5265 0.6416 0.1039  -0.2155 0.0315  523 LYS A CB  
43   C CG  . LYS A 5   ? 0.3905 0.5587 0.6815 0.1269  -0.2053 0.0284  523 LYS A CG  
44   C CD  . LYS A 5   ? 0.3939 0.6131 0.7281 0.1460  -0.2259 0.0313  523 LYS A CD  
45   C CE  . LYS A 5   ? 0.3880 0.6490 0.7671 0.1708  -0.2129 0.0284  523 LYS A CE  
46   N NZ  . LYS A 5   ? 0.3942 0.7170 0.8166 0.1809  -0.2241 0.0325  523 LYS A NZ  
47   N N   . ARG A 6   ? 0.5255 0.5219 0.6600 0.1088  -0.2053 0.0418  524 ARG A N   
48   C CA  . ARG A 6   ? 0.5593 0.5004 0.6568 0.1215  -0.2016 0.0458  524 ARG A CA  
49   C C   . ARG A 6   ? 0.5750 0.4835 0.6458 0.0981  -0.1819 0.0443  524 ARG A C   
50   O O   . ARG A 6   ? 0.5103 0.3901 0.5692 0.1041  -0.1720 0.0417  524 ARG A O   
51   C CB  . ARG A 6   ? 0.5570 0.4571 0.6141 0.1328  -0.2221 0.0570  524 ARG A CB  
52   C CG  . ARG A 6   ? 0.6327 0.5329 0.7001 0.1689  -0.2369 0.0589  524 ARG A CG  
53   C CD  . ARG A 6   ? 0.6611 0.6362 0.7925 0.1826  -0.2431 0.0527  524 ARG A CD  
54   N NE  . ARG A 6   ? 0.5446 0.5543 0.6900 0.1708  -0.2612 0.0550  524 ARG A NE  
55   C CZ  . ARG A 6   ? 0.6197 0.6926 0.8173 0.1796  -0.2740 0.0524  524 ARG A CZ  
56   N NH1 . ARG A 6   ? 0.6466 0.7600 0.8901 0.2024  -0.2684 0.0484  524 ARG A NH1 
57   N NH2 . ARG A 6   ? 0.6054 0.7015 0.8088 0.1657  -0.2928 0.0538  524 ARG A NH2 
58   N N   . LYS A 7   ? 0.4922 0.4072 0.5545 0.0724  -0.1768 0.0451  525 LYS A N   
59   C CA  . LYS A 7   ? 0.5023 0.4005 0.5493 0.0501  -0.1583 0.0433  525 LYS A CA  
60   C C   . LYS A 7   ? 0.4762 0.3985 0.5538 0.0500  -0.1427 0.0328  525 LYS A C   
61   O O   . LYS A 7   ? 0.5097 0.4057 0.5720 0.0437  -0.1315 0.0307  525 LYS A O   
62   C CB  . LYS A 7   ? 0.5596 0.4710 0.5991 0.0278  -0.1548 0.0446  525 LYS A CB  
63   C CG  . LYS A 7   ? 0.5794 0.4566 0.5750 0.0209  -0.1617 0.0557  525 LYS A CG  
64   C CD  . LYS A 7   ? 0.6529 0.5476 0.6437 0.0014  -0.1534 0.0543  525 LYS A CD  
65   C CE  . LYS A 7   ? 0.6674 0.5320 0.6128 -0.0063 -0.1553 0.0653  525 LYS A CE  
66   N NZ  . LYS A 7   ? 0.5837 0.4639 0.5247 -0.0234 -0.1411 0.0631  525 LYS A NZ  
67   N N   . TYR A 8   ? 0.4228 0.3943 0.5421 0.0554  -0.1424 0.0266  526 TYR A N   
68   C CA  . TYR A 8   ? 0.4692 0.4653 0.6156 0.0551  -0.1262 0.0178  526 TYR A CA  
69   C C   . TYR A 8   ? 0.4180 0.3940 0.5608 0.0777  -0.1222 0.0147  526 TYR A C   
70   O O   . TYR A 8   ? 0.4212 0.3859 0.5585 0.0749  -0.1082 0.0087  526 TYR A O   
71   C CB  . TYR A 8   ? 0.4383 0.4909 0.6298 0.0545  -0.1263 0.0138  526 TYR A CB  
72   C CG  . TYR A 8   ? 0.4873 0.5622 0.7014 0.0527  -0.1075 0.0064  526 TYR A CG  
73   C CD1 . TYR A 8   ? 0.4770 0.5492 0.6831 0.0320  -0.0951 0.0032  526 TYR A CD1 
74   C CD2 . TYR A 8   ? 0.5100 0.6071 0.7502 0.0738  -0.1014 0.0030  526 TYR A CD2 
75   C CE1 . TYR A 8   ? 0.5072 0.5952 0.7280 0.0307  -0.0787 -0.0027 526 TYR A CE1 
76   C CE2 . TYR A 8   ? 0.3990 0.5137 0.6540 0.0723  -0.0824 -0.0032 526 TYR A CE2 
77   C CZ  . TYR A 8   ? 0.5671 0.6751 0.8105 0.0498  -0.0719 -0.0058 526 TYR A CZ  
78   O OH  . TYR A 8   ? 0.6088 0.7298 0.8610 0.0478  -0.0541 -0.0111 526 TYR A OH  
79   N N   . GLU A 9   ? 0.4339 0.4035 0.5767 0.1018  -0.1357 0.0185  527 GLU A N   
80   C CA  . GLU A 9   ? 0.5169 0.4622 0.6514 0.1288  -0.1334 0.0154  527 GLU A CA  
81   C C   . GLU A 9   ? 0.5877 0.4641 0.6709 0.1212  -0.1309 0.0167  527 GLU A C   
82   O O   . GLU A 9   ? 0.5135 0.3689 0.5858 0.1251  -0.1197 0.0095  527 GLU A O   
83   C CB  . GLU A 9   ? 0.5536 0.5050 0.6966 0.1580  -0.1511 0.0205  527 GLU A CB  
84   C CG  . GLU A 9   ? 0.5791 0.6038 0.7786 0.1652  -0.1554 0.0194  527 GLU A CG  
85   C CD  . GLU A 9   ? 0.6156 0.6537 0.8290 0.1970  -0.1743 0.0242  527 GLU A CD  
86   O OE1 . GLU A 9   ? 0.7752 0.7618 0.9523 0.2184  -0.1827 0.0278  527 GLU A OE1 
87   O OE2 . GLU A 9   ? 0.6658 0.7660 0.9267 0.2004  -0.1821 0.0249  527 GLU A OE2 
88   N N   . PHE A 10  ? 0.5181 0.3593 0.5684 0.1087  -0.1417 0.0263  528 PHE A N   
89   C CA  . PHE A 10  ? 0.5508 0.3330 0.5557 0.0913  -0.1393 0.0302  528 PHE A CA  
90   C C   . PHE A 10  ? 0.5204 0.3097 0.5292 0.0678  -0.1230 0.0230  528 PHE A C   
91   O O   . PHE A 10  ? 0.5913 0.3425 0.5777 0.0666  -0.1184 0.0186  528 PHE A O   
92   C CB  . PHE A 10  ? 0.5648 0.3293 0.5442 0.0748  -0.1488 0.0428  528 PHE A CB  
93   C CG  . PHE A 10  ? 0.6803 0.3842 0.6131 0.0569  -0.1480 0.0506  528 PHE A CG  
94   C CD1 . PHE A 10  ? 0.7027 0.3454 0.5970 0.0717  -0.1585 0.0565  528 PHE A CD1 
95   C CD2 . PHE A 10  ? 0.7447 0.4527 0.6720 0.0251  -0.1373 0.0528  528 PHE A CD2 
96   C CE1 . PHE A 10  ? 0.7877 0.3719 0.6380 0.0512  -0.1584 0.0650  528 PHE A CE1 
97   C CE2 . PHE A 10  ? 0.7797 0.4379 0.6687 0.0051  -0.1365 0.0614  528 PHE A CE2 
98   C CZ  . PHE A 10  ? 0.8222 0.4166 0.6718 0.0162  -0.1472 0.0679  528 PHE A CZ  
99   N N   . PHE A 11  ? 0.6242 0.4592 0.6587 0.0499  -0.1162 0.0217  529 PHE A N   
100  C CA  . PHE A 11  ? 0.4373 0.2867 0.4797 0.0304  -0.1021 0.0151  529 PHE A CA  
101  C C   . PHE A 11  ? 0.4646 0.3141 0.5149 0.0435  -0.0925 0.0040  529 PHE A C   
102  O O   . PHE A 11  ? 0.5172 0.3391 0.5474 0.0330  -0.0873 -0.0002 529 PHE A O   
103  C CB  . PHE A 11  ? 0.4419 0.3422 0.5134 0.0186  -0.0980 0.0146  529 PHE A CB  
104  C CG  . PHE A 11  ? 0.4404 0.3615 0.5241 0.0038  -0.0845 0.0078  529 PHE A CG  
105  C CD1 . PHE A 11  ? 0.5177 0.4220 0.5827 -0.0169 -0.0799 0.0095  529 PHE A CD1 
106  C CD2 . PHE A 11  ? 0.4095 0.3702 0.5248 0.0097  -0.0770 0.0010  529 PHE A CD2 
107  C CE1 . PHE A 11  ? 0.5180 0.4435 0.5944 -0.0283 -0.0696 0.0036  529 PHE A CE1 
108  C CE2 . PHE A 11  ? 0.3953 0.3718 0.5177 -0.0030 -0.0655 -0.0042 529 PHE A CE2 
109  C CZ  . PHE A 11  ? 0.3907 0.3490 0.4930 -0.0204 -0.0627 -0.0033 529 PHE A CZ  
110  N N   . ARG A 12  ? 0.4649 0.3471 0.5442 0.0659  -0.0903 -0.0006 530 ARG A N   
111  C CA  . ARG A 12  ? 0.5043 0.3885 0.5890 0.0820  -0.0789 -0.0107 530 ARG A CA  
112  C C   . ARG A 12  ? 0.6335 0.4563 0.6786 0.0976  -0.0826 -0.0138 530 ARG A C   
113  O O   . ARG A 12  ? 0.6437 0.4453 0.6723 0.0995  -0.0741 -0.0226 530 ARG A O   
114  C CB  . ARG A 12  ? 0.6163 0.5522 0.7427 0.1039  -0.0751 -0.0127 530 ARG A CB  
115  C CG  . ARG A 12  ? 0.6267 0.6182 0.7900 0.0872  -0.0726 -0.0104 530 ARG A CG  
116  C CD  . ARG A 12  ? 0.6824 0.6828 0.8457 0.0665  -0.0589 -0.0150 530 ARG A CD  
117  N NE  . ARG A 12  ? 0.7144 0.7183 0.8796 0.0793  -0.0438 -0.0231 530 ARG A NE  
118  C CZ  . ARG A 12  ? 0.7638 0.7851 0.9352 0.0673  -0.0306 -0.0271 530 ARG A CZ  
119  N NH1 . ARG A 12  ? 0.6591 0.6963 0.8373 0.0437  -0.0312 -0.0241 530 ARG A NH1 
120  N NH2 . ARG A 12  ? 0.8499 0.8705 1.0171 0.0811  -0.0165 -0.0341 530 ARG A NH2 
121  N N   . ARG A 13  ? 0.5327 0.3233 0.5590 0.1099  -0.0963 -0.0069 531 ARG A N   
122  C CA  . ARG A 13  ? 0.7132 0.4345 0.6946 0.1230  -0.1024 -0.0085 531 ARG A CA  
123  C C   . ARG A 13  ? 0.8000 0.4751 0.7454 0.0930  -0.1019 -0.0091 531 ARG A C   
124  O O   . ARG A 13  ? 0.7866 0.4118 0.6989 0.0992  -0.1017 -0.0165 531 ARG A O   
125  C CB  . ARG A 13  ? 0.6803 0.3718 0.6438 0.1372  -0.1188 0.0019  531 ARG A CB  
126  C CG  . ARG A 13  ? 0.8837 0.5594 0.8430 0.1799  -0.1230 -0.0020 531 ARG A CG  
127  C CD  . ARG A 13  ? 0.9769 0.6835 0.9595 0.1990  -0.1360 0.0068  531 ARG A CD  
128  N NE  . ARG A 13  ? 1.1030 0.7782 1.0583 0.1806  -0.1506 0.0201  531 ARG A NE  
129  C CZ  . ARG A 13  ? 1.1233 0.8251 1.0939 0.1873  -0.1638 0.0290  531 ARG A CZ  
130  N NH1 . ARG A 13  ? 1.0732 0.8373 1.0913 0.2098  -0.1659 0.0262  531 ARG A NH1 
131  N NH2 . ARG A 13  ? 1.1359 0.8037 1.0742 0.1704  -0.1750 0.0412  531 ARG A NH2 
132  N N   . LYS A 14  ? 0.5851 0.2770 0.5363 0.0611  -0.1023 -0.0017 532 LYS A N   
133  C CA  . LYS A 14  ? 0.6790 0.3359 0.6027 0.0314  -0.1026 -0.0009 532 LYS A CA  
134  C C   . LYS A 14  ? 0.6315 0.3138 0.5689 0.0216  -0.0916 -0.0116 532 LYS A C   
135  O O   . LYS A 14  ? 0.6467 0.2956 0.5595 0.0050  -0.0932 -0.0152 532 LYS A O   
136  C CB  . LYS A 14  ? 0.6529 0.3184 0.5761 0.0031  -0.1059 0.0122  532 LYS A CB  
137  C CG  . LYS A 14  ? 0.6385 0.2563 0.5294 0.0047  -0.1178 0.0245  532 LYS A CG  
138  C CD  . LYS A 14  ? 0.6300 0.2537 0.5150 -0.0264 -0.1173 0.0376  532 LYS A CD  
139  C CE  . LYS A 14  ? 0.7662 0.3316 0.6098 -0.0295 -0.1280 0.0513  532 LYS A CE  
140  N NZ  . LYS A 14  ? 0.7333 0.3028 0.5682 -0.0626 -0.1242 0.0648  532 LYS A NZ  
141  N N   . LEU A 15  ? 0.5572 0.2971 0.5324 0.0307  -0.0816 -0.0160 533 LEU A N   
142  C CA  . LEU A 15  ? 0.6052 0.3683 0.5909 0.0241  -0.0707 -0.0252 533 LEU A CA  
143  C C   . LEU A 15  ? 0.7198 0.4510 0.6837 0.0464  -0.0666 -0.0370 533 LEU A C   
144  O O   . LEU A 15  ? 0.8625 0.6207 0.8451 0.0706  -0.0570 -0.0424 533 LEU A O   
145  C CB  . LEU A 15  ? 0.6074 0.4357 0.6360 0.0264  -0.0614 -0.0247 533 LEU A CB  
146  C CG  . LEU A 15  ? 0.5763 0.4368 0.6193 0.0096  -0.0522 -0.0282 533 LEU A CG  
147  C CD1 . LEU A 15  ? 0.4584 0.3129 0.4915 -0.0191 -0.0571 -0.0230 533 LEU A CD1 
148  C CD2 . LEU A 15  ? 0.4261 0.3409 0.5072 0.0143  -0.0456 -0.0261 533 LEU A CD2 
149  N N   . LYS A 16  ? 0.8371 0.5094 0.7596 0.0378  -0.0740 -0.0408 534 LYS A N   
150  C CA  . LYS A 16  ? 0.8123 0.4395 0.7017 0.0596  -0.0724 -0.0531 534 LYS A CA  
151  C C   . LYS A 16  ? 0.8466 0.4993 0.7424 0.0634  -0.0592 -0.0640 534 LYS A C   
152  O O   . LYS A 16  ? 1.0094 0.6992 0.9249 0.0417  -0.0555 -0.0622 534 LYS A O   
153  C CB  . LYS A 16  ? 0.8343 0.3867 0.6739 0.0433  -0.0866 -0.0541 534 LYS A CB  
154  C CG  . LYS A 16  ? 0.9661 0.4823 0.7903 0.0406  -0.0990 -0.0423 534 LYS A CG  
155  C CD  . LYS A 16  ? 1.0154 0.5297 0.8436 0.0809  -0.0974 -0.0427 534 LYS A CD  
156  C CE  . LYS A 16  ? 1.1876 0.6356 0.9776 0.0857  -0.1123 -0.0349 534 LYS A CE  
157  N NZ  . LYS A 16  ? 1.1506 0.6032 0.9448 0.0519  -0.1197 -0.0194 534 LYS A NZ  
158  N N   . LYS A 17  ? 0.9515 0.5842 0.8287 0.0932  -0.0514 -0.0748 535 LYS A N   
159  C CA  . LYS A 17  ? 1.0720 0.7257 0.9495 0.0997  -0.0370 -0.0847 535 LYS A CA  
160  C C   . LYS A 17  ? 1.1297 0.7340 0.9623 0.0811  -0.0451 -0.0936 535 LYS A C   
161  O O   . LYS A 17  ? 1.0841 0.6204 0.8726 0.0806  -0.0584 -0.0980 535 LYS A O   
162  C CB  . LYS A 17  ? 1.0720 0.7305 0.9489 0.1414  -0.0223 -0.0921 535 LYS A CB  
163  C CG  . LYS A 17  ? 1.2151 0.8016 1.0439 0.1670  -0.0297 -0.0999 535 LYS A CG  
164  C CD  . LYS A 17  ? 1.2526 0.8546 1.0871 0.2127  -0.0126 -0.1066 535 LYS A CD  
165  C CE  . LYS A 17  ? 1.4128 0.9360 1.1928 0.2421  -0.0200 -0.1158 535 LYS A CE  
166  N NZ  . LYS A 17  ? 1.4447 0.9329 1.2177 0.2352  -0.0401 -0.1063 535 LYS A NZ  
167  N N   . GLN A 18  ? 1.1066 0.7409 0.9477 0.0650  -0.0395 -0.0959 536 GLN A N   
168  C CA  . GLN A 18  ? 1.2110 0.7996 1.0071 0.0524  -0.0480 -0.1065 536 GLN A CA  
169  C C   . GLN A 18  ? 1.1870 0.7330 0.9385 0.0818  -0.0402 -0.1216 536 GLN A C   
170  O O   . GLN A 18  ? 1.1886 0.7667 0.9506 0.1028  -0.0213 -0.1250 536 GLN A O   
171  C CB  . GLN A 18  ? 1.2971 0.9214 1.1054 0.0307  -0.0466 -0.1060 536 GLN A CB  
172  C CG  . GLN A 18  ? 1.2587 0.9262 1.1045 0.0004  -0.0533 -0.0938 536 GLN A CG  
173  C CD  . GLN A 18  ? 1.2441 0.8801 1.0772 -0.0265 -0.0726 -0.0894 536 GLN A CD  
174  O OE1 . GLN A 18  ? 1.3877 0.9626 1.1825 -0.0261 -0.0838 -0.0944 536 GLN A OE1 
175  N NE2 . GLN A 18  ? 1.1999 0.8749 1.0614 -0.0522 -0.0771 -0.0803 536 GLN A NE2 
176  N N   . ASN A 19  ? 1.2447 0.7161 0.9425 0.0801  -0.0551 -0.1308 537 ASN A N   
177  C CA  . ASN A 19  ? 1.3239 0.7479 0.9703 0.1080  -0.0485 -0.1471 537 ASN A CA  
178  C C   . ASN A 19  ? 1.2818 0.6845 0.8922 0.0913  -0.0553 -0.1571 537 ASN A C   
179  O O   . ASN A 19  ? 1.2962 0.6935 0.8808 0.1131  -0.0425 -0.1662 537 ASN A O   
180  C CB  . ASN A 19  ? 1.4682 0.8304 1.0776 0.1211  -0.0583 -0.1497 537 ASN A CB  
181  C CG  . ASN A 19  ? 1.4885 0.8634 1.1202 0.1544  -0.0479 -0.1452 537 ASN A CG  
182  O OD1 . ASN A 19  ? 1.4090 0.8407 1.0798 0.1756  -0.0289 -0.1432 537 ASN A OD1 
183  N ND2 . ASN A 19  ? 1.5446 0.8783 1.1579 0.1567  -0.0601 -0.1406 537 ASN A ND2 
184  N N   . ASP A 20  ? 1.1528 0.5599 0.7709 0.0518  -0.0738 -0.1517 538 ASP A N   
185  C CA  . ASP A 20  ? 1.0787 0.4790 0.6727 0.0325  -0.0840 -0.1568 538 ASP A CA  
186  C C   . ASP A 20  ? 1.1309 0.5825 0.7460 0.0304  -0.0731 -0.1568 538 ASP A C   
187  O O   . ASP A 20  ? 1.0790 0.5427 0.6953 0.0041  -0.0865 -0.1557 538 ASP A O   
188  C CB  . ASP A 20  ? 0.9738 0.3670 0.5741 -0.0077 -0.1081 -0.1481 538 ASP A CB  
189  C CG  . ASP A 20  ? 1.0464 0.4869 0.6977 -0.0323 -0.1112 -0.1352 538 ASP A CG  
190  O OD1 . ASP A 20  ? 1.0155 0.5016 0.7030 -0.0179 -0.0945 -0.1302 538 ASP A OD1 
191  O OD2 . ASP A 20  ? 1.0473 0.4970 0.7129 -0.0646 -0.1265 -0.1257 538 ASP A OD2 
192  N N   . ILE A 21  ? 1.0865 0.5800 0.7262 0.0579  -0.0474 -0.1541 539 ILE A N   
193  C CA  . ILE A 21  ? 1.0495 0.6089 0.7256 0.0561  -0.0318 -0.1466 539 ILE A CA  
194  C C   . ILE A 21  ? 1.0678 0.6291 0.7225 0.0889  -0.0073 -0.1541 539 ILE A C   
195  O O   . ILE A 21  ? 0.9590 0.4941 0.5949 0.1174  0.0029  -0.1607 539 ILE A O   
196  C CB  . ILE A 21  ? 0.9967 0.6186 0.7391 0.0497  -0.0242 -0.1307 539 ILE A CB  
197  C CG1 . ILE A 21  ? 0.9918 0.6199 0.7547 0.0162  -0.0450 -0.1223 539 ILE A CG1 
198  C CG2 . ILE A 21  ? 1.0092 0.6920 0.7861 0.0535  -0.0051 -0.1235 539 ILE A CG2 
199  C CD1 . ILE A 21  ? 0.9968 0.6314 0.7516 -0.0075 -0.0577 -0.1231 539 ILE A CD1 
200  N N   . PRO A 22  ? 1.1057 0.6963 0.7604 0.0867  0.0031  -0.1525 540 PRO A N   
201  C CA  . PRO A 22  ? 1.0857 0.6862 0.7263 0.1176  0.0312  -0.1564 540 PRO A CA  
202  C C   . PRO A 22  ? 0.9414 0.5938 0.6364 0.1344  0.0523  -0.1466 540 PRO A C   
203  O O   . PRO A 22  ? 0.9190 0.6090 0.6647 0.1179  0.0460  -0.1351 540 PRO A O   
204  C CB  . PRO A 22  ? 1.0851 0.7120 0.7225 0.1062  0.0367  -0.1522 540 PRO A CB  
205  C CG  . PRO A 22  ? 1.1369 0.7435 0.7617 0.0760  0.0066  -0.1535 540 PRO A CG  
206  C CD  . PRO A 22  ? 1.0926 0.7007 0.7508 0.0599  -0.0098 -0.1484 540 PRO A CD  
207  N N   . ASN A 23  ? 0.8185 0.4745 0.5030 0.1671  0.0765  -0.1511 541 ASN A N   
208  C CA  . ASN A 23  ? 0.8811 0.5832 0.6159 0.1857  0.0930  -0.1434 541 ASN A CA  
209  C C   . ASN A 23  ? 0.8504 0.6276 0.6445 0.1724  0.1075  -0.1280 541 ASN A C   
210  O O   . ASN A 23  ? 0.8929 0.7167 0.7391 0.1781  0.1151  -0.1192 541 ASN A O   
211  C CB  . ASN A 23  ? 1.0532 0.7409 0.7607 0.2275  0.1158  -0.1529 541 ASN A CB  
212  C CG  . ASN A 23  ? 1.2734 0.9826 0.9642 0.2385  0.1429  -0.1533 541 ASN A CG  
213  O OD1 . ASN A 23  ? 1.3834 1.0716 1.0390 0.2222  0.1377  -0.1559 541 ASN A OD1 
214  N ND2 . ASN A 23  ? 1.2943 1.0474 1.0107 0.2665  0.1722  -0.1498 541 ASN A ND2 
215  N N   . LYS A 24  ? 0.7134 0.4992 0.4972 0.1543  0.1095  -0.1249 542 LYS A N   
216  C CA  . LYS A 24  ? 0.7626 0.6083 0.5958 0.1371  0.1190  -0.1103 542 LYS A CA  
217  C C   . LYS A 24  ? 0.7403 0.5798 0.5644 0.1082  0.1029  -0.1066 542 LYS A C   
218  O O   . LYS A 24  ? 0.7699 0.5657 0.5460 0.1034  0.0898  -0.1152 542 LYS A O   
219  C CB  . LYS A 24  ? 0.8369 0.7173 0.6756 0.1538  0.1514  -0.1061 542 LYS A CB  
220  C CG  . LYS A 24  ? 1.0152 0.8560 0.7890 0.1688  0.1632  -0.1160 542 LYS A CG  
221  C CD  . LYS A 24  ? 0.9951 0.8739 0.7770 0.1896  0.1997  -0.1110 542 LYS A CD  
222  C CE  . LYS A 24  ? 1.0782 0.9181 0.7909 0.2035  0.2136  -0.1193 542 LYS A CE  
223  N NZ  . LYS A 24  ? 1.0794 0.9603 0.8007 0.2229  0.2526  -0.1126 542 LYS A NZ  
224  N N   . PHE A 25  ? 0.5630 0.4461 0.4335 0.0896  0.1021  -0.0942 543 PHE A N   
225  C CA  . PHE A 25  ? 0.6265 0.5112 0.4921 0.0672  0.0912  -0.0892 543 PHE A CA  
226  C C   . PHE A 25  ? 0.6464 0.5585 0.5160 0.0664  0.1127  -0.0805 543 PHE A C   
227  O O   . PHE A 25  ? 0.5281 0.4819 0.4410 0.0612  0.1238  -0.0701 543 PHE A O   
228  C CB  . PHE A 25  ? 0.5502 0.4556 0.4560 0.0470  0.0738  -0.0819 543 PHE A CB  
229  C CG  . PHE A 25  ? 0.6276 0.5386 0.5316 0.0279  0.0639  -0.0765 543 PHE A CG  
230  C CD1 . PHE A 25  ? 0.5914 0.4707 0.4580 0.0215  0.0475  -0.0829 543 PHE A CD1 
231  C CD2 . PHE A 25  ? 0.5062 0.4524 0.4434 0.0175  0.0699  -0.0654 543 PHE A CD2 
232  C CE1 . PHE A 25  ? 0.6055 0.4931 0.4714 0.0077  0.0379  -0.0777 543 PHE A CE1 
233  C CE2 . PHE A 25  ? 0.5195 0.4668 0.4510 0.0040  0.0608  -0.0608 543 PHE A CE2 
234  C CZ  . PHE A 25  ? 0.5037 0.4239 0.4008 0.0006  0.0453  -0.0667 543 PHE A CZ  
235  N N   . GLU A 26  ? 0.7102 0.5962 0.5319 0.0706  0.1177  -0.0843 544 GLU A N   
236  C CA  . GLU A 26  ? 0.6798 0.5852 0.4976 0.0699  0.1395  -0.0749 544 GLU A CA  
237  C C   . GLU A 26  ? 0.6116 0.5233 0.4357 0.0485  0.1277  -0.0657 544 GLU A C   
238  O O   . GLU A 26  ? 0.6073 0.4950 0.4100 0.0403  0.1052  -0.0701 544 GLU A O   
239  C CB  . GLU A 26  ? 0.6527 0.5250 0.4102 0.0871  0.1531  -0.0822 544 GLU A CB  
240  C CG  . GLU A 26  ? 0.8158 0.6897 0.5685 0.1131  0.1742  -0.0888 544 GLU A CG  
241  C CD  . GLU A 26  ? 1.0306 0.8809 0.7262 0.1310  0.1957  -0.0930 544 GLU A CD  
242  O OE1 . GLU A 26  ? 1.0831 0.8877 0.7221 0.1295  0.1816  -0.1006 544 GLU A OE1 
243  O OE2 . GLU A 26  ? 1.1316 1.0111 0.8389 0.1467  0.2266  -0.0882 544 GLU A OE2 
244  N N   . MET A 27  ? 0.5274 0.4723 0.3818 0.0396  0.1425  -0.0528 545 MET A N   
245  C CA  . MET A 27  ? 0.4919 0.4399 0.3517 0.0216  0.1327  -0.0435 545 MET A CA  
246  C C   . MET A 27  ? 0.6086 0.5712 0.4679 0.0168  0.1562  -0.0307 545 MET A C   
247  O O   . MET A 27  ? 0.6792 0.6768 0.5792 0.0118  0.1712  -0.0229 545 MET A O   
248  C CB  . MET A 27  ? 0.5582 0.5286 0.4658 0.0085  0.1166  -0.0407 545 MET A CB  
249  C CG  . MET A 27  ? 0.6237 0.5928 0.5332 -0.0065 0.1044  -0.0331 545 MET A CG  
250  S SD  . MET A 27  ? 0.5803 0.5636 0.5282 -0.0175 0.0814  -0.0336 545 MET A SD  
251  C CE  . MET A 27  ? 0.4184 0.4343 0.4138 -0.0168 0.0921  -0.0317 545 MET A CE  
252  N N   . LYS A 28  ? 0.5809 0.5162 0.3928 0.0174  0.1589  -0.0280 546 LYS A N   
253  C CA  . LYS A 28  ? 0.5542 0.4956 0.3577 0.0106  0.1808  -0.0141 546 LYS A CA  
254  C C   . LYS A 28  ? 0.7651 0.7004 0.5742 -0.0066 0.1667  -0.0046 546 LYS A C   
255  O O   . LYS A 28  ? 0.7082 0.6189 0.4936 -0.0060 0.1444  -0.0087 546 LYS A O   
256  C CB  . LYS A 28  ? 0.6689 0.5794 0.4100 0.0234  0.1946  -0.0154 546 LYS A CB  
257  C CG  . LYS A 28  ? 0.6913 0.6003 0.4174 0.0442  0.2087  -0.0266 546 LYS A CG  
258  C CD  . LYS A 28  ? 0.8427 0.7234 0.5048 0.0570  0.2284  -0.0258 546 LYS A CD  
259  C CE  . LYS A 28  ? 0.8352 0.7125 0.4789 0.0812  0.2451  -0.0377 546 LYS A CE  
260  N NZ  . LYS A 28  ? 0.9409 0.7760 0.5074 0.0962  0.2551  -0.0420 546 LYS A NZ  
261  N N   . LEU A 29  ? 0.5756 0.5337 0.4167 -0.0215 0.1789  0.0078  547 LEU A N   
262  C CA  . LEU A 29  ? 0.5855 0.5353 0.4341 -0.0369 0.1652  0.0157  547 LEU A CA  
263  C C   . LEU A 29  ? 0.5897 0.5357 0.4290 -0.0509 0.1847  0.0319  547 LEU A C   
264  O O   . LEU A 29  ? 0.5879 0.5568 0.4394 -0.0537 0.2099  0.0382  547 LEU A O   
265  C CB  . LEU A 29  ? 0.5735 0.5507 0.4763 -0.0457 0.1521  0.0132  547 LEU A CB  
266  C CG  . LEU A 29  ? 0.4754 0.4618 0.3974 -0.0361 0.1349  -0.0001 547 LEU A CG  
267  C CD1 . LEU A 29  ? 0.4638 0.4824 0.4393 -0.0451 0.1312  0.0009  547 LEU A CD1 
268  C CD2 . LEU A 29  ? 0.4406 0.4029 0.3405 -0.0331 0.1105  -0.0059 547 LEU A CD2 
269  N N   . ARG A 30  ? 0.6100 0.5276 0.4282 -0.0596 0.1733  0.0391  548 ARG A N   
270  C CA  . ARG A 30  ? 0.6397 0.5472 0.4508 -0.0778 0.1875  0.0556  548 ARG A CA  
271  C C   . ARG A 30  ? 0.5677 0.4819 0.4156 -0.0944 0.1733  0.0583  548 ARG A C   
272  O O   . ARG A 30  ? 0.5327 0.4356 0.3819 -0.0884 0.1497  0.0506  548 ARG A O   
273  C CB  . ARG A 30  ? 0.7704 0.6289 0.5173 -0.0733 0.1859  0.0628  548 ARG A CB  
274  C CG  . ARG A 30  ? 0.8543 0.7001 0.5555 -0.0568 0.1990  0.0600  548 ARG A CG  
275  C CD  . ARG A 30  ? 0.9656 0.7625 0.6038 -0.0457 0.1836  0.0611  548 ARG A CD  
276  N NE  . ARG A 30  ? 1.0837 0.8779 0.7291 -0.0344 0.1521  0.0480  548 ARG A NE  
277  C CZ  . ARG A 30  ? 1.0783 0.8405 0.6834 -0.0235 0.1313  0.0469  548 ARG A CZ  
278  N NH1 . ARG A 30  ? 0.9538 0.6771 0.5028 -0.0209 0.1371  0.0581  548 ARG A NH1 
279  N NH2 . ARG A 30  ? 1.0173 0.7883 0.6391 -0.0151 0.1047  0.0356  548 ARG A NH2 
280  N N   . ARG A 31  ? 0.5456 0.4805 0.4240 -0.1151 0.1876  0.0688  549 ARG A N   
281  C CA  . ARG A 31  ? 0.6975 0.6364 0.6083 -0.1327 0.1736  0.0708  549 ARG A CA  
282  C C   . ARG A 31  ? 0.6195 0.5073 0.4927 -0.1347 0.1555  0.0736  549 ARG A C   
283  O O   . ARG A 31  ? 0.5872 0.4706 0.4747 -0.1346 0.1355  0.0670  549 ARG A O   
284  C CB  . ARG A 31  ? 0.6892 0.6549 0.6329 -0.1585 0.1917  0.0838  549 ARG A CB  
285  C CG  . ARG A 31  ? 0.6704 0.6973 0.6692 -0.1567 0.2036  0.0799  549 ARG A CG  
286  C CD  . ARG A 31  ? 0.6817 0.7413 0.7176 -0.1845 0.2203  0.0944  549 ARG A CD  
287  N NE  . ARG A 31  ? 0.6959 0.8195 0.7894 -0.1801 0.2294  0.0911  549 ARG A NE  
288  C CZ  . ARG A 31  ? 0.7464 0.9066 0.8507 -0.1700 0.2520  0.0960  549 ARG A CZ  
289  N NH1 . ARG A 31  ? 0.6447 0.7830 0.7049 -0.1669 0.2710  0.1043  549 ARG A NH1 
290  N NH2 . ARG A 31  ? 0.7927 1.0108 0.9486 -0.1613 0.2545  0.0925  549 ARG A NH2 
291  N N   . ALA A 32  ? 0.6344 0.4823 0.4566 -0.1344 0.1630  0.0834  550 ALA A N   
292  C CA  . ALA A 32  ? 0.7059 0.5010 0.4870 -0.1323 0.1463  0.0869  550 ALA A CA  
293  C C   . ALA A 32  ? 0.7927 0.5828 0.5664 -0.1077 0.1227  0.0729  550 ALA A C   
294  O O   . ALA A 32  ? 0.8725 0.6342 0.6316 -0.1030 0.1051  0.0717  550 ALA A O   
295  C CB  . ALA A 32  ? 0.7157 0.4679 0.4389 -0.1334 0.1590  0.1007  550 ALA A CB  
296  N N   . THR A 33  ? 0.7180 0.5360 0.5020 -0.0922 0.1225  0.0624  551 THR A N   
297  C CA  . THR A 33  ? 0.6400 0.4597 0.4218 -0.0725 0.1008  0.0501  551 THR A CA  
298  C C   . THR A 33  ? 0.6862 0.5494 0.5129 -0.0687 0.0974  0.0377  551 THR A C   
299  O O   . THR A 33  ? 0.5655 0.4353 0.3853 -0.0544 0.0892  0.0286  551 THR A O   
300  C CB  . THR A 33  ? 0.7697 0.5662 0.5033 -0.0551 0.0970  0.0494  551 THR A CB  
301  O OG1 . THR A 33  ? 0.7127 0.5210 0.4387 -0.0547 0.1156  0.0493  551 THR A OG1 
302  C CG2 . THR A 33  ? 0.9356 0.6829 0.6184 -0.0540 0.0953  0.0615  551 THR A CG2 
303  N N   . VAL A 34  ? 0.6348 0.5248 0.5050 -0.0821 0.1020  0.0375  552 VAL A N   
304  C CA  . VAL A 34  ? 0.4976 0.4255 0.4078 -0.0781 0.0995  0.0273  552 VAL A CA  
305  C C   . VAL A 34  ? 0.3981 0.3281 0.3127 -0.0661 0.0783  0.0170  552 VAL A C   
306  O O   . VAL A 34  ? 0.4679 0.4140 0.3921 -0.0576 0.0746  0.0084  552 VAL A O   
307  C CB  . VAL A 34  ? 0.5548 0.5111 0.5115 -0.0935 0.1030  0.0290  552 VAL A CB  
308  C CG1 . VAL A 34  ? 0.4694 0.4618 0.4602 -0.0863 0.1046  0.0204  552 VAL A CG1 
309  C CG2 . VAL A 34  ? 0.8639 0.8228 0.8241 -0.1104 0.1214  0.0409  552 VAL A CG2 
310  N N   . LEU A 35  ? 0.4443 0.3579 0.3520 -0.0658 0.0650  0.0182  553 LEU A N   
311  C CA  . LEU A 35  ? 0.4609 0.3840 0.3786 -0.0554 0.0473  0.0099  553 LEU A CA  
312  C C   . LEU A 35  ? 0.5001 0.4188 0.3944 -0.0415 0.0395  0.0056  553 LEU A C   
313  O O   . LEU A 35  ? 0.4188 0.3572 0.3286 -0.0372 0.0320  -0.0021 553 LEU A O   
314  C CB  . LEU A 35  ? 0.4955 0.4008 0.4064 -0.0541 0.0366  0.0120  553 LEU A CB  
315  C CG  . LEU A 35  ? 0.4219 0.3412 0.3451 -0.0429 0.0213  0.0049  553 LEU A CG  
316  C CD1 . LEU A 35  ? 0.4330 0.3844 0.3938 -0.0484 0.0205  -0.0011 553 LEU A CD1 
317  C CD2 . LEU A 35  ? 0.4527 0.3493 0.3631 -0.0392 0.0144  0.0070  553 LEU A CD2 
318  N N   . GLU A 36  ? 0.5274 0.4181 0.3824 -0.0355 0.0399  0.0112  554 GLU A N   
319  C CA  . GLU A 36  ? 0.6372 0.5233 0.4678 -0.0222 0.0288  0.0071  554 GLU A CA  
320  C C   . GLU A 36  ? 0.5618 0.4567 0.3899 -0.0226 0.0357  0.0013  554 GLU A C   
321  O O   . GLU A 36  ? 0.4909 0.3961 0.3209 -0.0170 0.0231  -0.0069 554 GLU A O   
322  C CB  . GLU A 36  ? 0.7179 0.5684 0.5020 -0.0140 0.0266  0.0150  554 GLU A CB  
323  C CG  . GLU A 36  ? 0.9715 0.8212 0.7349 0.0018  0.0075  0.0108  554 GLU A CG  
324  C CD  . GLU A 36  ? 1.1560 0.9783 0.8875 0.0152  -0.0031 0.0179  554 GLU A CD  
325  O OE1 . GLU A 36  ? 1.0540 0.8473 0.7692 0.0112  0.0059  0.0267  554 GLU A OE1 
326  O OE2 . GLU A 36  ? 1.2476 1.0771 0.9705 0.0297  -0.0217 0.0148  554 GLU A OE2 
327  N N   . ASP A 37  ? 0.5718 0.4623 0.3948 -0.0291 0.0558  0.0054  555 ASP A N   
328  C CA  . ASP A 37  ? 0.5842 0.4801 0.4009 -0.0256 0.0643  -0.0010 555 ASP A CA  
329  C C   . ASP A 37  ? 0.4924 0.4151 0.3476 -0.0269 0.0586  -0.0107 555 ASP A C   
330  O O   . ASP A 37  ? 0.4849 0.4054 0.3301 -0.0208 0.0529  -0.0195 555 ASP A O   
331  C CB  . ASP A 37  ? 0.5798 0.4731 0.3888 -0.0308 0.0902  0.0063  555 ASP A CB  
332  C CG  . ASP A 37  ? 0.6314 0.4926 0.3934 -0.0299 0.0982  0.0168  555 ASP A CG  
333  O OD1 . ASP A 37  ? 0.6345 0.4723 0.3621 -0.0209 0.0828  0.0164  555 ASP A OD1 
334  O OD2 . ASP A 37  ? 0.6824 0.5433 0.4422 -0.0386 0.1202  0.0264  555 ASP A OD2 
335  N N   . SER A 38  ? 0.4766 0.4197 0.3714 -0.0351 0.0596  -0.0089 556 SER A N   
336  C CA  . SER A 38  ? 0.4171 0.3821 0.3454 -0.0362 0.0539  -0.0163 556 SER A CA  
337  C C   . SER A 38  ? 0.3852 0.3516 0.3134 -0.0331 0.0331  -0.0224 556 SER A C   
338  O O   . SER A 38  ? 0.4241 0.3944 0.3573 -0.0318 0.0266  -0.0298 556 SER A O   
339  C CB  . SER A 38  ? 0.3704 0.3549 0.3367 -0.0455 0.0568  -0.0124 556 SER A CB  
340  O OG  . SER A 38  ? 0.3989 0.3900 0.3737 -0.0516 0.0748  -0.0060 556 SER A OG  
341  N N   . TYR A 39  ? 0.4690 0.4326 0.3923 -0.0321 0.0228  -0.0188 557 TYR A N   
342  C CA  . TYR A 39  ? 0.4284 0.4019 0.3568 -0.0292 0.0042  -0.0227 557 TYR A CA  
343  C C   . TYR A 39  ? 0.4112 0.3751 0.3146 -0.0250 -0.0051 -0.0286 557 TYR A C   
344  O O   . TYR A 39  ? 0.4266 0.4008 0.3408 -0.0283 -0.0170 -0.0345 557 TYR A O   
345  C CB  . TYR A 39  ? 0.3542 0.3252 0.2766 -0.0237 -0.0031 -0.0173 557 TYR A CB  
346  C CG  . TYR A 39  ? 0.3995 0.3868 0.3267 -0.0180 -0.0213 -0.0201 557 TYR A CG  
347  C CD1 . TYR A 39  ? 0.3436 0.3576 0.3028 -0.0218 -0.0276 -0.0222 557 TYR A CD1 
348  C CD2 . TYR A 39  ? 0.3869 0.3652 0.2871 -0.0088 -0.0322 -0.0196 557 TYR A CD2 
349  C CE1 . TYR A 39  ? 0.2928 0.3295 0.2617 -0.0180 -0.0427 -0.0232 557 TYR A CE1 
350  C CE2 . TYR A 39  ? 0.4796 0.4808 0.3903 -0.0039 -0.0498 -0.0213 557 TYR A CE2 
351  C CZ  . TYR A 39  ? 0.3389 0.3719 0.2866 -0.0094 -0.0541 -0.0229 557 TYR A CZ  
352  O OH  . TYR A 39  ? 0.3887 0.4516 0.3518 -0.0064 -0.0700 -0.0234 557 TYR A OH  
353  N N   . ARG A 40  ? 0.3902 0.3312 0.2566 -0.0190 -0.0006 -0.0266 558 ARG A N   
354  C CA  . ARG A 40  ? 0.4219 0.3488 0.2569 -0.0144 -0.0116 -0.0326 558 ARG A CA  
355  C C   . ARG A 40  ? 0.5130 0.4347 0.3471 -0.0171 -0.0076 -0.0415 558 ARG A C   
356  O O   . ARG A 40  ? 0.5255 0.4434 0.3516 -0.0191 -0.0235 -0.0492 558 ARG A O   
357  C CB  . ARG A 40  ? 0.5865 0.4853 0.3756 -0.0063 -0.0053 -0.0277 558 ARG A CB  
358  C CG  . ARG A 40  ? 0.6756 0.5704 0.4540 0.0003  -0.0153 -0.0199 558 ARG A CG  
359  C CD  . ARG A 40  ? 0.8592 0.7199 0.5860 0.0082  -0.0091 -0.0136 558 ARG A CD  
360  N NE  . ARG A 40  ? 1.0661 0.9178 0.7779 0.0175  -0.0211 -0.0063 558 ARG A NE  
361  C CZ  . ARG A 40  ? 1.1156 0.9338 0.7821 0.0249  -0.0171 0.0023  558 ARG A CZ  
362  N NH1 . ARG A 40  ? 1.1912 0.9850 0.8237 0.0224  0.0007  0.0051  558 ARG A NH1 
363  N NH2 . ARG A 40  ? 1.1089 0.9171 0.7619 0.0362  -0.0299 0.0085  558 ARG A NH2 
364  N N   . ARG A 41  ? 0.4719 0.3927 0.3139 -0.0172 0.0127  -0.0403 559 ARG A N   
365  C CA  . ARG A 41  ? 0.4788 0.3926 0.3186 -0.0153 0.0173  -0.0489 559 ARG A CA  
366  C C   . ARG A 41  ? 0.4331 0.3622 0.3064 -0.0229 0.0050  -0.0531 559 ARG A C   
367  O O   . ARG A 41  ? 0.5015 0.4179 0.3636 -0.0247 -0.0073 -0.0613 559 ARG A O   
368  C CB  . ARG A 41  ? 0.5277 0.4449 0.3735 -0.0111 0.0430  -0.0456 559 ARG A CB  
369  C CG  . ARG A 41  ? 0.5044 0.4134 0.3457 -0.0036 0.0498  -0.0546 559 ARG A CG  
370  C CD  . ARG A 41  ? 0.5502 0.4260 0.3386 0.0064  0.0495  -0.0626 559 ARG A CD  
371  N NE  . ARG A 41  ? 0.6481 0.5118 0.4280 0.0174  0.0590  -0.0714 559 ARG A NE  
372  C CZ  . ARG A 41  ? 0.7966 0.6340 0.5556 0.0198  0.0439  -0.0832 559 ARG A CZ  
373  N NH1 . ARG A 41  ? 0.7738 0.5996 0.5221 0.0092  0.0181  -0.0869 559 ARG A NH1 
374  N NH2 . ARG A 41  ? 0.7470 0.5693 0.4951 0.0333  0.0543  -0.0911 559 ARG A NH2 
375  N N   . ILE A 42  ? 0.3792 0.3322 0.2904 -0.0286 0.0076  -0.0472 560 ILE A N   
376  C CA  . ILE A 42  ? 0.3626 0.3278 0.3027 -0.0352 -0.0001 -0.0497 560 ILE A CA  
377  C C   . ILE A 42  ? 0.4264 0.3978 0.3698 -0.0431 -0.0211 -0.0515 560 ILE A C   
378  O O   . ILE A 42  ? 0.4279 0.3963 0.3778 -0.0498 -0.0302 -0.0556 560 ILE A O   
379  C CB  . ILE A 42  ? 0.4481 0.4351 0.4229 -0.0383 0.0084  -0.0429 560 ILE A CB  
380  C CG1 . ILE A 42  ? 0.4507 0.4379 0.4301 -0.0328 0.0270  -0.0420 560 ILE A CG1 
381  C CG2 . ILE A 42  ? 0.3455 0.3462 0.3470 -0.0456 -0.0018 -0.0429 560 ILE A CG2 
382  C CD1 . ILE A 42  ? 0.3844 0.3927 0.3958 -0.0375 0.0339  -0.0353 560 ILE A CD1 
383  N N   . MET A 43  ? 0.3674 0.3470 0.3053 -0.0421 -0.0290 -0.0478 561 MET A N   
384  C CA  . MET A 43  ? 0.3571 0.3507 0.3023 -0.0490 -0.0486 -0.0489 561 MET A CA  
385  C C   . MET A 43  ? 0.4287 0.4024 0.3421 -0.0502 -0.0628 -0.0562 561 MET A C   
386  O O   . MET A 43  ? 0.5107 0.4953 0.4314 -0.0599 -0.0810 -0.0582 561 MET A O   
387  C CB  . MET A 43  ? 0.3363 0.3516 0.2925 -0.0442 -0.0525 -0.0420 561 MET A CB  
388  C CG  . MET A 43  ? 0.3533 0.3847 0.3375 -0.0444 -0.0421 -0.0365 561 MET A CG  
389  S SD  . MET A 43  ? 0.4652 0.5140 0.4813 -0.0571 -0.0450 -0.0372 561 MET A SD  
390  C CE  . MET A 43  ? 0.3772 0.4567 0.4078 -0.0621 -0.0624 -0.0352 561 MET A CE  
391  N N   . GLY A 44  ? 0.4075 0.3523 0.2848 -0.0414 -0.0545 -0.0600 562 GLY A N   
392  C CA  . GLY A 44  ? 0.4480 0.3674 0.2866 -0.0410 -0.0685 -0.0681 562 GLY A CA  
393  C C   . GLY A 44  ? 0.4735 0.3657 0.2968 -0.0458 -0.0717 -0.0781 562 GLY A C   
394  O O   . GLY A 44  ? 0.5355 0.4041 0.3265 -0.0488 -0.0879 -0.0862 562 GLY A O   
395  N N   . VAL A 45  ? 0.5406 0.4327 0.3835 -0.0456 -0.0581 -0.0780 563 VAL A N   
396  C CA  . VAL A 45  ? 0.5635 0.4231 0.3872 -0.0456 -0.0592 -0.0875 563 VAL A CA  
397  C C   . VAL A 45  ? 0.5746 0.4235 0.3943 -0.0629 -0.0847 -0.0928 563 VAL A C   
398  O O   . VAL A 45  ? 0.5648 0.4445 0.4165 -0.0770 -0.0967 -0.0865 563 VAL A O   
399  C CB  . VAL A 45  ? 0.5693 0.4360 0.4211 -0.0419 -0.0433 -0.0847 563 VAL A CB  
400  C CG1 . VAL A 45  ? 0.5619 0.4378 0.4164 -0.0268 -0.0188 -0.0806 563 VAL A CG1 
401  C CG2 . VAL A 45  ? 0.4596 0.3592 0.3570 -0.0553 -0.0493 -0.0764 563 VAL A CG2 
402  N N   . LYS A 46  ? 0.5605 0.3650 0.3395 -0.0620 -0.0927 -0.1041 564 LYS A N   
403  C CA  . LYS A 46  ? 0.5874 0.3745 0.3569 -0.0817 -0.1189 -0.1097 564 LYS A CA  
404  C C   . LYS A 46  ? 0.6005 0.4011 0.4083 -0.0965 -0.1205 -0.1037 564 LYS A C   
405  O O   . LYS A 46  ? 0.6245 0.4433 0.4537 -0.1181 -0.1381 -0.0997 564 LYS A O   
406  C CB  . LYS A 46  ? 0.6585 0.3849 0.3691 -0.0757 -0.1257 -0.1244 564 LYS A CB  
407  C CG  . LYS A 46  ? 0.9819 0.6851 0.6660 -0.0957 -0.1579 -0.1322 564 LYS A CG  
408  C CD  . LYS A 46  ? 0.9090 0.6146 0.6204 -0.1199 -0.1722 -0.1287 564 LYS A CD  
409  C CE  . LYS A 46  ? 0.9192 0.6408 0.6393 -0.1389 -0.1950 -0.1264 564 LYS A CE  
410  N NZ  . LYS A 46  ? 1.0669 0.7435 0.7350 -0.1334 -0.2059 -0.1372 564 LYS A NZ  
411  N N   . ARG A 47  ? 0.5813 0.3756 0.3981 -0.0845 -0.1016 -0.1022 565 ARG A N   
412  C CA  . ARG A 47  ? 0.6155 0.4159 0.4614 -0.0950 -0.1016 -0.0962 565 ARG A CA  
413  C C   . ARG A 47  ? 0.6115 0.4421 0.4896 -0.0813 -0.0800 -0.0881 565 ARG A C   
414  O O   . ARG A 47  ? 0.6242 0.4502 0.4923 -0.0615 -0.0630 -0.0906 565 ARG A O   
415  C CB  . ARG A 47  ? 0.5917 0.3361 0.4047 -0.0945 -0.1073 -0.1049 565 ARG A CB  
416  C CG  . ARG A 47  ? 0.6653 0.3701 0.4422 -0.1120 -0.1320 -0.1139 565 ARG A CG  
417  C CD  . ARG A 47  ? 0.7800 0.4176 0.5138 -0.1049 -0.1347 -0.1243 565 ARG A CD  
418  N NE  . ARG A 47  ? 0.8888 0.5257 0.6453 -0.1033 -0.1261 -0.1170 565 ARG A NE  
419  C CZ  . ARG A 47  ? 0.9020 0.4936 0.6322 -0.0846 -0.1189 -0.1230 565 ARG A CZ  
420  N NH1 . ARG A 47  ? 0.8294 0.3732 0.5094 -0.0651 -0.1171 -0.1372 565 ARG A NH1 
421  N NH2 . ARG A 47  ? 0.8196 0.4134 0.5716 -0.0831 -0.1133 -0.1149 565 ARG A NH2 
422  N N   . ALA A 48  ? 0.5557 0.4179 0.4717 -0.0926 -0.0805 -0.0781 566 ALA A N   
423  C CA  . ALA A 48  ? 0.4575 0.3463 0.4025 -0.0818 -0.0633 -0.0708 566 ALA A CA  
424  C C   . ALA A 48  ? 0.4716 0.3338 0.4072 -0.0672 -0.0535 -0.0743 566 ALA A C   
425  O O   . ALA A 48  ? 0.4871 0.3661 0.4379 -0.0530 -0.0381 -0.0716 566 ALA A O   
426  C CB  . ALA A 48  ? 0.4789 0.4004 0.4589 -0.0962 -0.0670 -0.0604 566 ALA A CB  
427  N N   . ASP A 49  ? 0.5232 0.3433 0.4331 -0.0706 -0.0635 -0.0804 567 ASP A N   
428  C CA  . ASP A 49  ? 0.5987 0.3879 0.4942 -0.0529 -0.0560 -0.0848 567 ASP A CA  
429  C C   . ASP A 49  ? 0.6468 0.4328 0.5270 -0.0279 -0.0390 -0.0916 567 ASP A C   
430  O O   . ASP A 49  ? 0.6133 0.3995 0.5004 -0.0091 -0.0266 -0.0917 567 ASP A O   
431  C CB  . ASP A 49  ? 0.6993 0.4324 0.5587 -0.0607 -0.0719 -0.0917 567 ASP A CB  
432  C CG  . ASP A 49  ? 0.7518 0.4853 0.6270 -0.0852 -0.0852 -0.0827 567 ASP A CG  
433  O OD1 . ASP A 49  ? 0.7361 0.5011 0.6444 -0.0856 -0.0783 -0.0723 567 ASP A OD1 
434  O OD2 . ASP A 49  ? 0.7733 0.4740 0.6255 -0.1049 -0.1026 -0.0857 567 ASP A OD2 
435  N N   . PHE A 50  ? 0.6996 0.4852 0.5596 -0.0274 -0.0383 -0.0964 568 PHE A N   
436  C CA  . PHE A 50  ? 0.6796 0.4668 0.5247 -0.0057 -0.0192 -0.1006 568 PHE A CA  
437  C C   . PHE A 50  ? 0.5622 0.3952 0.4488 0.0027  -0.0004 -0.0911 568 PHE A C   
438  O O   . PHE A 50  ? 0.5358 0.3749 0.4217 0.0218  0.0181  -0.0925 568 PHE A O   
439  C CB  . PHE A 50  ? 0.5341 0.3190 0.3534 -0.0096 -0.0223 -0.1037 568 PHE A CB  
440  C CG  . PHE A 50  ? 0.5940 0.3293 0.3637 -0.0138 -0.0398 -0.1157 568 PHE A CG  
441  C CD1 . PHE A 50  ? 0.6357 0.3270 0.3830 -0.0132 -0.0496 -0.1234 568 PHE A CD1 
442  C CD2 . PHE A 50  ? 0.7938 0.5225 0.5352 -0.0180 -0.0480 -0.1193 568 PHE A CD2 
443  C CE1 . PHE A 50  ? 0.8745 0.5143 0.5720 -0.0191 -0.0679 -0.1352 568 PHE A CE1 
444  C CE2 . PHE A 50  ? 0.8106 0.4917 0.5035 -0.0232 -0.0671 -0.1312 568 PHE A CE2 
445  C CZ  . PHE A 50  ? 0.7918 0.4278 0.4628 -0.0248 -0.0772 -0.1395 568 PHE A CZ  
446  N N   . LEU A 51  ? 0.5064 0.3722 0.4292 -0.0121 -0.0053 -0.0815 569 LEU A N   
447  C CA  . LEU A 51  ? 0.5109 0.4171 0.4711 -0.0083 0.0084  -0.0727 569 LEU A CA  
448  C C   . LEU A 51  ? 0.4648 0.3767 0.4465 0.0022  0.0131  -0.0708 569 LEU A C   
449  O O   . LEU A 51  ? 0.4721 0.4175 0.4860 0.0045  0.0219  -0.0641 569 LEU A O   
450  C CB  . LEU A 51  ? 0.5112 0.4449 0.4961 -0.0255 0.0007  -0.0644 569 LEU A CB  
451  C CG  . LEU A 51  ? 0.4716 0.4041 0.4392 -0.0340 -0.0064 -0.0651 569 LEU A CG  
452  C CD1 . LEU A 51  ? 0.4789 0.4364 0.4712 -0.0478 -0.0155 -0.0578 569 LEU A CD1 
453  C CD2 . LEU A 51  ? 0.4037 0.3423 0.3601 -0.0248 0.0085  -0.0642 569 LEU A CD2 
454  N N   . LYS A 52  ? 0.5082 0.3851 0.4699 0.0085  0.0055  -0.0768 570 LYS A N   
455  C CA  . LYS A 52  ? 0.5711 0.4473 0.5477 0.0217  0.0072  -0.0752 570 LYS A CA  
456  C C   . LYS A 52  ? 0.6335 0.5041 0.5999 0.0490  0.0231  -0.0815 570 LYS A C   
457  O O   . LYS A 52  ? 0.6417 0.5206 0.6253 0.0652  0.0270  -0.0799 570 LYS A O   
458  C CB  . LYS A 52  ? 0.4998 0.3360 0.4577 0.0141  -0.0104 -0.0767 570 LYS A CB  
459  C CG  . LYS A 52  ? 0.4954 0.3453 0.4694 -0.0119 -0.0231 -0.0684 570 LYS A CG  
460  C CD  . LYS A 52  ? 0.5633 0.3730 0.5167 -0.0235 -0.0391 -0.0683 570 LYS A CD  
461  C CE  . LYS A 52  ? 0.5602 0.3922 0.5347 -0.0474 -0.0475 -0.0581 570 LYS A CE  
462  N NZ  . LYS A 52  ? 0.6347 0.4281 0.5861 -0.0653 -0.0627 -0.0575 570 LYS A NZ  
463  N N   . ALA A 53  ? 0.6137 0.4708 0.5506 0.0556  0.0321  -0.0885 571 ALA A N   
464  C CA  . ALA A 53  ? 0.6204 0.4761 0.5455 0.0829  0.0512  -0.0942 571 ALA A CA  
465  C C   . ALA A 53  ? 0.6040 0.5186 0.5740 0.0874  0.0703  -0.0849 571 ALA A C   
466  O O   . ALA A 53  ? 0.4742 0.4208 0.4735 0.0681  0.0678  -0.0759 571 ALA A O   
467  C CB  . ALA A 53  ? 0.5891 0.4111 0.4644 0.0877  0.0555  -0.1039 571 ALA A CB  
468  N N   . ARG A 54  ? 0.6054 0.5336 0.5799 0.1130  0.0892  -0.0872 572 ARG A N   
469  C CA  . ARG A 54  ? 0.6258 0.6130 0.6448 0.1166  0.1085  -0.0781 572 ARG A CA  
470  C C   . ARG A 54  ? 0.5946 0.5981 0.6105 0.0990  0.1184  -0.0727 572 ARG A C   
471  O O   . ARG A 54  ? 0.5819 0.5586 0.5555 0.1034  0.1260  -0.0784 572 ARG A O   
472  C CB  . ARG A 54  ? 0.7572 0.7562 0.7763 0.1495  0.1298  -0.0823 572 ARG A CB  
473  C CG  . ARG A 54  ? 0.8491 0.9172 0.9212 0.1516  0.1503  -0.0715 572 ARG A CG  
474  C CD  . ARG A 54  ? 0.9295 1.0164 1.0069 0.1869  0.1721  -0.0751 572 ARG A CD  
475  N NE  . ARG A 54  ? 1.0539 1.1223 1.1328 0.2090  0.1588  -0.0807 572 ARG A NE  
476  C CZ  . ARG A 54  ? 1.0533 1.1303 1.1341 0.2456  0.1727  -0.0854 572 ARG A CZ  
477  N NH1 . ARG A 54  ? 1.0845 1.1931 1.1681 0.2638  0.2025  -0.0853 572 ARG A NH1 
478  N NH2 . ARG A 54  ? 1.0715 1.1245 1.1496 0.2653  0.1575  -0.0898 572 ARG A NH2 
479  N N   . LEU A 55  ? 0.5778 0.6203 0.6340 0.0796  0.1170  -0.0617 573 LEU A N   
480  C CA  . LEU A 55  ? 0.5359 0.5874 0.5869 0.0617  0.1235  -0.0555 573 LEU A CA  
481  C C   . LEU A 55  ? 0.4709 0.5429 0.5186 0.0727  0.1514  -0.0526 573 LEU A C   
482  O O   . LEU A 55  ? 0.4314 0.5452 0.5160 0.0820  0.1668  -0.0475 573 LEU A O   
483  C CB  . LEU A 55  ? 0.4813 0.5632 0.5722 0.0396  0.1148  -0.0453 573 LEU A CB  
484  C CG  . LEU A 55  ? 0.4849 0.5531 0.5823 0.0297  0.0903  -0.0465 573 LEU A CG  
485  C CD1 . LEU A 55  ? 0.4561 0.5518 0.5866 0.0107  0.0840  -0.0374 573 LEU A CD1 
486  C CD2 . LEU A 55  ? 0.5677 0.5944 0.6245 0.0234  0.0767  -0.0528 573 LEU A CD2 
487  N N   . TRP A 56  ? 0.4918 0.5354 0.4945 0.0718  0.1575  -0.0553 574 TRP A N   
488  C CA  . TRP A 56  ? 0.6367 0.6902 0.6224 0.0823  0.1851  -0.0526 574 TRP A CA  
489  C C   . TRP A 56  ? 0.5925 0.6486 0.5697 0.0610  0.1893  -0.0424 574 TRP A C   
490  O O   . TRP A 56  ? 0.5743 0.5944 0.5021 0.0607  0.1877  -0.0457 574 TRP A O   
491  C CB  . TRP A 56  ? 0.7715 0.7784 0.6979 0.1042  0.1887  -0.0660 574 TRP A CB  
492  C CG  . TRP A 56  ? 0.8366 0.8588 0.7570 0.1310  0.2178  -0.0681 574 TRP A CG  
493  C CD1 . TRP A 56  ? 0.9239 0.9359 0.8034 0.1417  0.2412  -0.0684 574 TRP A CD1 
494  C CD2 . TRP A 56  ? 0.8583 0.9094 0.8124 0.1533  0.2276  -0.0700 574 TRP A CD2 
495  N NE1 . TRP A 56  ? 0.8902 0.9258 0.7776 0.1695  0.2671  -0.0705 574 TRP A NE1 
496  C CE2 . TRP A 56  ? 0.8913 0.9524 0.8260 0.1780  0.2586  -0.0716 574 TRP A CE2 
497  C CE3 . TRP A 56  ? 0.7730 0.8427 0.7703 0.1564  0.2131  -0.0701 574 TRP A CE3 
498  C CZ2 . TRP A 56  ? 0.9632 1.0562 0.9244 0.2070  0.2758  -0.0736 574 TRP A CZ2 
499  C CZ3 . TRP A 56  ? 0.7769 0.8750 0.7986 0.1844  0.2277  -0.0718 574 TRP A CZ3 
500  C CH2 . TRP A 56  ? 0.9345 1.0459 0.9401 0.2103  0.2589  -0.0737 574 TRP A CH2 
501  N N   . ILE A 57  ? 0.6127 0.7075 0.6350 0.0432  0.1926  -0.0302 575 ILE A N   
502  C CA  . ILE A 57  ? 0.5216 0.6114 0.5358 0.0210  0.1914  -0.0202 575 ILE A CA  
503  C C   . ILE A 57  ? 0.5816 0.6941 0.5970 0.0171  0.2205  -0.0085 575 ILE A C   
504  O O   . ILE A 57  ? 0.5286 0.6845 0.5815 0.0217  0.2391  -0.0035 575 ILE A O   
505  C CB  . ILE A 57  ? 0.5331 0.6397 0.5877 0.0006  0.1729  -0.0145 575 ILE A CB  
506  C CG1 . ILE A 57  ? 0.4579 0.5440 0.5104 0.0036  0.1465  -0.0243 575 ILE A CG1 
507  C CG2 . ILE A 57  ? 0.5836 0.6780 0.6248 -0.0197 0.1710  -0.0049 575 ILE A CG2 
508  C CD1 . ILE A 57  ? 0.4270 0.5305 0.5177 -0.0120 0.1296  -0.0201 575 ILE A CD1 
509  N N   . GLU A 58  ? 0.5424 0.6267 0.5164 0.0087  0.2244  -0.0034 576 GLU A N   
510  C CA  . GLU A 58  ? 0.5383 0.6354 0.5030 0.0030  0.2526  0.0092  576 GLU A CA  
511  C C   . GLU A 58  ? 0.6120 0.6907 0.5643 -0.0212 0.2459  0.0210  576 GLU A C   
512  O O   . GLU A 58  ? 0.5991 0.6367 0.5131 -0.0218 0.2271  0.0169  576 GLU A O   
513  C CB  . GLU A 58  ? 0.5984 0.6672 0.5053 0.0242  0.2689  0.0031  576 GLU A CB  
514  C CG  . GLU A 58  ? 0.7631 0.8508 0.6599 0.0247  0.3044  0.0151  576 GLU A CG  
515  C CD  . GLU A 58  ? 0.9859 1.0344 0.8131 0.0466  0.3166  0.0075  576 GLU A CD  
516  O OE1 . GLU A 58  ? 1.0448 1.0558 0.8210 0.0397  0.3156  0.0127  576 GLU A OE1 
517  O OE2 . GLU A 58  ? 1.0531 1.1042 0.8727 0.0721  0.3253  -0.0043 576 GLU A OE2 
518  N N   . PHE A 59  ? 0.6766 0.7851 0.6610 -0.0410 0.2600  0.0356  577 PHE A N   
519  C CA  . PHE A 59  ? 0.6091 0.6936 0.5777 -0.0641 0.2542  0.0474  577 PHE A CA  
520  C C   . PHE A 59  ? 0.6123 0.6832 0.5420 -0.0692 0.2807  0.0606  577 PHE A C   
521  O O   . PHE A 59  ? 0.5801 0.6879 0.5302 -0.0715 0.3091  0.0693  577 PHE A O   
522  C CB  . PHE A 59  ? 0.6432 0.7586 0.6669 -0.0883 0.2474  0.0556  577 PHE A CB  
523  C CG  . PHE A 59  ? 0.5030 0.6104 0.5453 -0.0896 0.2162  0.0461  577 PHE A CG  
524  C CD1 . PHE A 59  ? 0.5854 0.6492 0.5951 -0.0940 0.1957  0.0446  577 PHE A CD1 
525  C CD2 . PHE A 59  ? 0.4902 0.6346 0.5817 -0.0855 0.2081  0.0396  577 PHE A CD2 
526  C CE1 . PHE A 59  ? 0.5201 0.5796 0.5465 -0.0944 0.1699  0.0366  577 PHE A CE1 
527  C CE2 . PHE A 59  ? 0.4397 0.5755 0.5445 -0.0871 0.1810  0.0320  577 PHE A CE2 
528  C CZ  . PHE A 59  ? 0.3664 0.4609 0.4389 -0.0917 0.1632  0.0305  577 PHE A CZ  
529  N N   . ASP A 60  ? 0.5950 0.6144 0.4686 -0.0701 0.2714  0.0627  578 ASP A N   
530  C CA  . ASP A 60  ? 0.7220 0.7171 0.5503 -0.0782 0.2925  0.0776  578 ASP A CA  
531  C C   . ASP A 60  ? 0.7116 0.7253 0.5237 -0.0644 0.3260  0.0800  578 ASP A C   
532  O O   . ASP A 60  ? 0.7529 0.7782 0.5621 -0.0753 0.3410  0.0943  578 ASP A O   
533  C CB  . ASP A 60  ? 0.6687 0.6722 0.5231 -0.1098 0.2977  0.0953  578 ASP A CB  
534  C CG  . ASP A 60  ? 0.7581 0.7296 0.6118 -0.1205 0.2656  0.0932  578 ASP A CG  
535  O OD1 . ASP A 60  ? 0.7793 0.6995 0.5791 -0.1168 0.2548  0.0954  578 ASP A OD1 
536  O OD2 . ASP A 60  ? 0.7191 0.7158 0.6231 -0.1300 0.2507  0.0890  578 ASP A OD2 
537  N N   . GLY A 61  ? 0.6856 0.7047 0.4921 -0.0381 0.3245  0.0636  579 GLY A N   
538  C CA  . GLY A 61  ? 0.7320 0.7628 0.5170 -0.0182 0.3473  0.0611  579 GLY A CA  
539  C C   . GLY A 61  ? 0.7771 0.8756 0.6243 -0.0218 0.3657  0.0670  579 GLY A C   
540  O O   . GLY A 61  ? 0.7810 0.8981 0.6173 -0.0116 0.3858  0.0689  579 GLY A O   
541  N N   . GLU A 62  ? 0.6926 0.8295 0.6047 -0.0363 0.3571  0.0692  580 GLU A N   
542  C CA  . GLU A 62  ? 0.7307 0.9367 0.7060 -0.0410 0.3689  0.0743  580 GLU A CA  
543  C C   . GLU A 62  ? 0.6333 0.8620 0.6245 -0.0100 0.3727  0.0578  580 GLU A C   
544  O O   . GLU A 62  ? 0.6259 0.8574 0.6437 -0.0020 0.3569  0.0478  580 GLU A O   
545  C CB  . GLU A 62  ? 0.7472 0.9824 0.7821 -0.0690 0.3531  0.0825  580 GLU A CB  
546  C CG  . GLU A 62  ? 0.7306 0.9495 0.7549 -0.1010 0.3512  0.1010  580 GLU A CG  
547  C CD  . GLU A 62  ? 0.6535 0.8669 0.7104 -0.1248 0.3267  0.1044  580 GLU A CD  
548  O OE1 . GLU A 62  ? 0.6134 0.8433 0.7068 -0.1188 0.3116  0.0932  580 GLU A OE1 
549  O OE2 . GLU A 62  ? 0.7365 0.9246 0.7790 -0.1488 0.3215  0.1180  580 GLU A OE2 
550  N N   . LYS A 63  ? 0.7170 0.9574 0.6882 0.0081  0.3934  0.0549  581 LYS A N   
551  C CA  . LYS A 63  ? 0.8346 1.0925 0.8160 0.0395  0.3984  0.0394  581 LYS A CA  
552  C C   . LYS A 63  ? 0.8563 1.1883 0.9116 0.0357  0.4064  0.0424  581 LYS A C   
553  O O   . LYS A 63  ? 0.8951 1.2668 0.9836 0.0090  0.4148  0.0564  581 LYS A O   
554  C CB  . LYS A 63  ? 0.9104 1.1408 0.8312 0.0631  0.4159  0.0326  581 LYS A CB  
555  C CG  . LYS A 63  ? 0.9474 1.1071 0.7998 0.0839  0.4013  0.0175  581 LYS A CG  
556  C CD  . LYS A 63  ? 0.9859 1.0937 0.7878 0.0669  0.3907  0.0243  581 LYS A CD  
557  C CE  . LYS A 63  ? 0.9947 1.0359 0.7251 0.0874  0.3754  0.0080  581 LYS A CE  
558  N NZ  . LYS A 63  ? 0.8833 0.9115 0.6256 0.1005  0.3554  -0.0082 581 LYS A NZ  
559  N N   . GLY A 64  ? 0.8842 1.2318 0.9625 0.0619  0.4022  0.0287  582 GLY A N   
560  C CA  . GLY A 64  ? 0.9361 1.3505 1.0777 0.0660  0.4109  0.0285  582 GLY A CA  
561  C C   . GLY A 64  ? 0.8830 1.3348 1.0908 0.0466  0.3908  0.0324  582 GLY A C   
562  O O   . GLY A 64  ? 0.9114 1.4218 1.1758 0.0366  0.3965  0.0365  582 GLY A O   
563  N N   . LEU A 65  ? 0.7341 1.1512 0.9344 0.0410  0.3669  0.0306  583 LEU A N   
564  C CA  . LEU A 65  ? 0.6839 1.1293 0.9405 0.0237  0.3445  0.0333  583 LEU A CA  
565  C C   . LEU A 65  ? 0.7306 1.1652 0.9967 0.0503  0.3275  0.0204  583 LEU A C   
566  O O   . LEU A 65  ? 0.8169 1.2032 1.0358 0.0733  0.3268  0.0104  583 LEU A O   
567  C CB  . LEU A 65  ? 0.5353 0.9521 0.7818 -0.0090 0.3291  0.0436  583 LEU A CB  
568  C CG  . LEU A 65  ? 0.6034 1.0331 0.8514 -0.0431 0.3381  0.0592  583 LEU A CG  
569  C CD1 . LEU A 65  ? 0.5322 1.0286 0.8348 -0.0538 0.3496  0.0618  583 LEU A CD1 
570  C CD2 . LEU A 65  ? 0.7124 1.1020 0.8971 -0.0400 0.3572  0.0642  583 LEU A CD2 
571  N N   . ASP A 66  ? 0.7710 1.2478 1.0952 0.0461  0.3126  0.0203  584 ASP A N   
572  C CA  . ASP A 66  ? 0.6946 1.1642 1.0325 0.0684  0.2935  0.0107  584 ASP A CA  
573  C C   . ASP A 66  ? 0.7902 1.2071 1.0991 0.0625  0.2758  0.0090  584 ASP A C   
574  O O   . ASP A 66  ? 0.8360 1.2518 1.1612 0.0335  0.2606  0.0164  584 ASP A O   
575  C CB  . ASP A 66  ? 0.5603 1.0834 0.9643 0.0588  0.2780  0.0131  584 ASP A CB  
576  C CG  . ASP A 66  ? 0.6162 1.1314 1.0332 0.0814  0.2568  0.0050  584 ASP A CG  
577  O OD1 . ASP A 66  ? 0.7512 1.2693 1.1658 0.1150  0.2636  -0.0035 584 ASP A OD1 
578  O OD2 . ASP A 66  ? 0.5722 1.0755 0.9994 0.0657  0.2330  0.0074  584 ASP A OD2 
579  N N   . TYR A 67  ? 0.7645 1.1326 1.0275 0.0886  0.2754  -0.0028 585 TYR A N   
580  C CA  . TYR A 67  ? 0.7560 1.0617 0.9778 0.0770  0.2475  -0.0105 585 TYR A CA  
581  C C   . TYR A 67  ? 0.7529 1.0648 1.0093 0.0640  0.2177  -0.0104 585 TYR A C   
582  O O   . TYR A 67  ? 0.7276 1.0047 0.9648 0.0452  0.1970  -0.0116 585 TYR A O   
583  C CB  . TYR A 67  ? 0.8294 1.0791 0.9933 0.1035  0.2443  -0.0259 585 TYR A CB  
584  C CG  . TYR A 67  ? 0.9053 1.1316 1.0178 0.1134  0.2683  -0.0278 585 TYR A CG  
585  C CD1 . TYR A 67  ? 0.8359 1.0182 0.9008 0.0965  0.2620  -0.0277 585 TYR A CD1 
586  C CD2 . TYR A 67  ? 0.9879 1.2364 1.0974 0.1416  0.2973  -0.0296 585 TYR A CD2 
587  C CE1 . TYR A 67  ? 0.8999 1.0576 0.9127 0.1059  0.2823  -0.0291 585 TYR A CE1 
588  C CE2 . TYR A 67  ? 1.0873 1.3110 1.1435 0.1506  0.3186  -0.0316 585 TYR A CE2 
589  C CZ  . TYR A 67  ? 1.0375 1.2145 1.0440 0.1329  0.3117  -0.0310 585 TYR A CZ  
590  O OH  . TYR A 67  ? 1.1118 1.2611 1.0610 0.1420  0.3304  -0.0327 585 TYR A OH  
591  N N   . GLY A 68  ? 0.7981 1.1559 1.1047 0.0751  0.2158  -0.0086 586 GLY A N   
592  C CA  . GLY A 68  ? 0.7675 1.1335 1.1056 0.0637  0.1880  -0.0075 586 GLY A CA  
593  C C   . GLY A 68  ? 0.6798 1.0667 1.0449 0.0280  0.1808  0.0034  586 GLY A C   
594  O O   . GLY A 68  ? 0.6150 0.9772 0.9738 0.0113  0.1570  0.0024  586 GLY A O   
595  N N   . GLY A 69  ? 0.6222 1.0531 1.0153 0.0161  0.2021  0.0142  587 GLY A N   
596  C CA  . GLY A 69  ? 0.5226 0.9651 0.9316 -0.0199 0.1933  0.0238  587 GLY A CA  
597  C C   . GLY A 69  ? 0.4273 0.8172 0.7913 -0.0381 0.1921  0.0252  587 GLY A C   
598  O O   . GLY A 69  ? 0.4068 0.7802 0.7709 -0.0613 0.1733  0.0277  587 GLY A O   
599  N N   . VAL A 70  ? 0.4321 0.7914 0.7500 -0.0259 0.2094  0.0220  588 VAL A N   
600  C CA  . VAL A 70  ? 0.4350 0.7421 0.7022 -0.0393 0.2057  0.0223  588 VAL A CA  
601  C C   . VAL A 70  ? 0.4190 0.6841 0.6646 -0.0399 0.1763  0.0131  588 VAL A C   
602  O O   . VAL A 70  ? 0.3994 0.6388 0.6293 -0.0586 0.1638  0.0159  588 VAL A O   
603  C CB  . VAL A 70  ? 0.4664 0.7466 0.6840 -0.0222 0.2264  0.0190  588 VAL A CB  
604  C CG1 . VAL A 70  ? 0.4386 0.6658 0.6040 -0.0347 0.2192  0.0197  588 VAL A CG1 
605  C CG2 . VAL A 70  ? 0.5040 0.8268 0.7400 -0.0210 0.2589  0.0292  588 VAL A CG2 
606  N N   . ALA A 71  ? 0.3237 0.5820 0.5683 -0.0192 0.1658  0.0027  589 ALA A N   
607  C CA  . ALA A 71  ? 0.3442 0.5668 0.5701 -0.0204 0.1403  -0.0047 589 ALA A CA  
608  C C   . ALA A 71  ? 0.3761 0.6108 0.6304 -0.0406 0.1224  0.0002  589 ALA A C   
609  O O   . ALA A 71  ? 0.4211 0.6260 0.6544 -0.0517 0.1076  -0.0010 589 ALA A O   
610  C CB  . ALA A 71  ? 0.4198 0.6339 0.6425 0.0029  0.1330  -0.0145 589 ALA A CB  
611  N N   . ARG A 72  ? 0.4337 0.7131 0.7351 -0.0440 0.1234  0.0054  590 ARG A N   
612  C CA  . ARG A 72  ? 0.4917 0.7831 0.8196 -0.0626 0.1045  0.0091  590 ARG A CA  
613  C C   . ARG A 72  ? 0.4457 0.7208 0.7601 -0.0883 0.1051  0.0160  590 ARG A C   
614  O O   . ARG A 72  ? 0.3984 0.6508 0.7025 -0.1009 0.0870  0.0150  590 ARG A O   
615  C CB  . ARG A 72  ? 0.5403 0.8882 0.9235 -0.0614 0.1054  0.0140  590 ARG A CB  
616  C CG  . ARG A 72  ? 0.5949 0.9501 1.0002 -0.0694 0.0794  0.0133  590 ARG A CG  
617  C CD  . ARG A 72  ? 0.6333 1.0326 1.0797 -0.0526 0.0748  0.0133  590 ARG A CD  
618  N NE  . ARG A 72  ? 0.7274 1.1741 1.2002 -0.0597 0.0842  0.0190  590 ARG A NE  
619  C CZ  . ARG A 72  ? 0.7924 1.2822 1.3000 -0.0498 0.0780  0.0178  590 ARG A CZ  
620  N NH1 . ARG A 72  ? 0.8329 1.3216 1.3486 -0.0308 0.0613  0.0144  590 ARG A NH1 
621  N NH2 . ARG A 72  ? 0.7479 1.2799 1.2840 -0.0590 0.0886  0.0190  590 ARG A NH2 
622  N N   . GLU A 73  ? 0.3702 0.6531 0.6798 -0.0945 0.1267  0.0230  591 GLU A N   
623  C CA  . GLU A 73  ? 0.3496 0.6100 0.6398 -0.1178 0.1289  0.0307  591 GLU A CA  
624  C C   . GLU A 73  ? 0.4886 0.6941 0.7270 -0.1130 0.1191  0.0247  591 GLU A C   
625  O O   . GLU A 73  ? 0.4582 0.6358 0.6797 -0.1278 0.1074  0.0269  591 GLU A O   
626  C CB  . GLU A 73  ? 0.3981 0.6771 0.6900 -0.1238 0.1567  0.0407  591 GLU A CB  
627  C CG  . GLU A 73  ? 0.5928 0.8411 0.8570 -0.1475 0.1611  0.0504  591 GLU A CG  
628  C CD  . GLU A 73  ? 0.7255 0.9965 0.9929 -0.1548 0.1871  0.0635  591 GLU A CD  
629  O OE1 . GLU A 73  ? 0.7580 1.0818 1.0620 -0.1493 0.1946  0.0674  591 GLU A OE1 
630  O OE2 . GLU A 73  ? 0.8344 1.0701 1.0621 -0.1641 0.1979  0.0701  591 GLU A OE2 
631  N N   . TRP A 74  ? 0.3722 0.5621 0.5854 -0.0916 0.1227  0.0170  592 TRP A N   
632  C CA  . TRP A 74  ? 0.4040 0.5497 0.5729 -0.0864 0.1129  0.0116  592 TRP A CA  
633  C C   . TRP A 74  ? 0.4622 0.5955 0.6338 -0.0892 0.0895  0.0066  592 TRP A C   
634  O O   . TRP A 74  ? 0.4146 0.5193 0.5615 -0.0949 0.0802  0.0069  592 TRP A O   
635  C CB  . TRP A 74  ? 0.3993 0.5322 0.5427 -0.0653 0.1186  0.0036  592 TRP A CB  
636  C CG  . TRP A 74  ? 0.3886 0.4839 0.4941 -0.0612 0.1048  -0.0021 592 TRP A CG  
637  C CD1 . TRP A 74  ? 0.3611 0.4282 0.4309 -0.0649 0.1053  0.0010  592 TRP A CD1 
638  C CD2 . TRP A 74  ? 0.4199 0.5045 0.5212 -0.0530 0.0878  -0.0108 592 TRP A CD2 
639  N NE1 . TRP A 74  ? 0.3614 0.4067 0.4096 -0.0584 0.0889  -0.0058 592 TRP A NE1 
640  C CE2 . TRP A 74  ? 0.3694 0.4259 0.4374 -0.0529 0.0789  -0.0126 592 TRP A CE2 
641  C CE3 . TRP A 74  ? 0.4388 0.5349 0.5610 -0.0461 0.0792  -0.0161 592 TRP A CE3 
642  C CZ2 . TRP A 74  ? 0.4014 0.4469 0.4612 -0.0483 0.0629  -0.0193 592 TRP A CZ2 
643  C CZ3 . TRP A 74  ? 0.4382 0.5164 0.5468 -0.0425 0.0638  -0.0223 592 TRP A CZ3 
644  C CH2 . TRP A 74  ? 0.3085 0.3645 0.3886 -0.0447 0.0563  -0.0237 592 TRP A CH2 
645  N N   . PHE A 75  ? 0.3326 0.4864 0.5317 -0.0832 0.0805  0.0025  593 PHE A N   
646  C CA  . PHE A 75  ? 0.3792 0.5219 0.5784 -0.0850 0.0603  -0.0015 593 PHE A CA  
647  C C   . PHE A 75  ? 0.4258 0.5629 0.6287 -0.1033 0.0520  0.0032  593 PHE A C   
648  O O   . PHE A 75  ? 0.5141 0.6279 0.6986 -0.1051 0.0392  0.0006  593 PHE A O   
649  C CB  . PHE A 75  ? 0.3494 0.5136 0.5754 -0.0759 0.0526  -0.0049 593 PHE A CB  
650  C CG  . PHE A 75  ? 0.3718 0.5230 0.5819 -0.0585 0.0521  -0.0118 593 PHE A CG  
651  C CD1 . PHE A 75  ? 0.2645 0.3891 0.4495 -0.0570 0.0410  -0.0160 593 PHE A CD1 
652  C CD2 . PHE A 75  ? 0.3937 0.5587 0.6129 -0.0438 0.0628  -0.0139 593 PHE A CD2 
653  C CE1 . PHE A 75  ? 0.3403 0.4507 0.5104 -0.0454 0.0387  -0.0217 593 PHE A CE1 
654  C CE2 . PHE A 75  ? 0.3580 0.5022 0.5566 -0.0289 0.0605  -0.0209 593 PHE A CE2 
655  C CZ  . PHE A 75  ? 0.2687 0.3849 0.4431 -0.0319 0.0477  -0.0245 593 PHE A CZ  
656  N N   . PHE A 76  ? 0.2959 0.4542 0.5219 -0.1169 0.0597  0.0102  594 PHE A N   
657  C CA  . PHE A 76  ? 0.3578 0.5051 0.5836 -0.1376 0.0517  0.0150  594 PHE A CA  
658  C C   . PHE A 76  ? 0.4691 0.5749 0.6530 -0.1419 0.0551  0.0175  594 PHE A C   
659  O O   . PHE A 76  ? 0.4010 0.4767 0.5635 -0.1461 0.0418  0.0155  594 PHE A O   
660  C CB  . PHE A 76  ? 0.3904 0.5737 0.6537 -0.1546 0.0597  0.0234  594 PHE A CB  
661  C CG  . PHE A 76  ? 0.5550 0.7228 0.8172 -0.1787 0.0489  0.0284  594 PHE A CG  
662  C CD1 . PHE A 76  ? 0.5395 0.7036 0.8104 -0.1807 0.0284  0.0219  594 PHE A CD1 
663  C CD2 . PHE A 76  ? 0.5487 0.6947 0.7922 -0.1933 0.0590  0.0368  594 PHE A CD2 
664  C CE1 . PHE A 76  ? 0.5346 0.6746 0.7956 -0.1969 0.0181  0.0223  594 PHE A CE1 
665  C CE2 . PHE A 76  ? 0.5978 0.7184 0.8344 -0.2099 0.0477  0.0392  594 PHE A CE2 
666  C CZ  . PHE A 76  ? 0.5705 0.6881 0.8158 -0.2116 0.0273  0.0310  594 PHE A CZ  
667  N N   . LEU A 77  ? 0.3524 0.4549 0.5217 -0.1389 0.0728  0.0218  595 LEU A N   
668  C CA  . LEU A 77  ? 0.4432 0.5050 0.5703 -0.1416 0.0758  0.0256  595 LEU A CA  
669  C C   . LEU A 77  ? 0.3848 0.4188 0.4810 -0.1247 0.0637  0.0177  595 LEU A C   
670  O O   . LEU A 77  ? 0.5127 0.5128 0.5801 -0.1260 0.0559  0.0186  595 LEU A O   
671  C CB  . LEU A 77  ? 0.4653 0.5292 0.5793 -0.1403 0.0976  0.0323  595 LEU A CB  
672  C CG  . LEU A 77  ? 0.4765 0.5660 0.6147 -0.1591 0.1148  0.0435  595 LEU A CG  
673  C CD1 . LEU A 77  ? 0.4963 0.5834 0.6117 -0.1527 0.1382  0.0493  595 LEU A CD1 
674  C CD2 . LEU A 77  ? 0.5257 0.5927 0.6588 -0.1849 0.1080  0.0518  595 LEU A CD2 
675  N N   . ILE A 78  ? 0.3444 0.3926 0.4466 -0.1089 0.0618  0.0104  596 ILE A N   
676  C CA  . ILE A 78  ? 0.2996 0.3286 0.3775 -0.0955 0.0514  0.0044  596 ILE A CA  
677  C C   . ILE A 78  ? 0.3675 0.3914 0.4502 -0.0970 0.0354  0.0010  596 ILE A C   
678  O O   . ILE A 78  ? 0.5009 0.5053 0.5612 -0.0896 0.0276  -0.0012 596 ILE A O   
679  C CB  . ILE A 78  ? 0.3607 0.4028 0.4415 -0.0815 0.0527  -0.0022 596 ILE A CB  
680  C CG1 . ILE A 78  ? 0.3681 0.3918 0.4207 -0.0708 0.0446  -0.0063 596 ILE A CG1 
681  C CG2 . ILE A 78  ? 0.3395 0.4026 0.4488 -0.0797 0.0450  -0.0067 596 ILE A CG2 
682  C CD1 . ILE A 78  ? 0.3668 0.3650 0.3846 -0.0689 0.0484  -0.0018 596 ILE A CD1 
683  N N   . SER A 79  ? 0.3623 0.4049 0.4731 -0.1048 0.0308  0.0005  597 SER A N   
684  C CA  . SER A 79  ? 0.3770 0.4117 0.4877 -0.1069 0.0162  -0.0026 597 SER A CA  
685  C C   . SER A 79  ? 0.4119 0.4132 0.4968 -0.1144 0.0119  -0.0001 597 SER A C   
686  O O   . SER A 79  ? 0.4841 0.4652 0.5477 -0.1062 0.0033  -0.0038 597 SER A O   
687  C CB  . SER A 79  ? 0.3355 0.3954 0.4792 -0.1151 0.0107  -0.0028 597 SER A CB  
688  O OG  . SER A 79  ? 0.3829 0.4641 0.5429 -0.1040 0.0102  -0.0063 597 SER A OG  
689  N N   . LYS A 80  ? 0.4074 0.4024 0.4932 -0.1296 0.0188  0.0066  598 LYS A N   
690  C CA  . LYS A 80  ? 0.4638 0.4198 0.5218 -0.1399 0.0146  0.0101  598 LYS A CA  
691  C C   . LYS A 80  ? 0.5114 0.4341 0.5294 -0.1240 0.0145  0.0093  598 LYS A C   
692  O O   . LYS A 80  ? 0.5376 0.4261 0.5280 -0.1201 0.0051  0.0071  598 LYS A O   
693  C CB  . LYS A 80  ? 0.5009 0.4584 0.5673 -0.1608 0.0254  0.0198  598 LYS A CB  
694  C CG  . LYS A 80  ? 0.7586 0.7236 0.8478 -0.1835 0.0169  0.0218  598 LYS A CG  
695  C CD  . LYS A 80  ? 0.7772 0.7822 0.9035 -0.1793 0.0086  0.0158  598 LYS A CD  
696  C CE  . LYS A 80  ? 0.8129 0.8233 0.9588 -0.2008 -0.0048 0.0168  598 LYS A CE  
697  N NZ  . LYS A 80  ? 0.9119 0.8724 1.0201 -0.2045 -0.0210 0.0121  598 LYS A NZ  
698  N N   . GLU A 81  ? 0.4768 0.4087 0.4901 -0.1137 0.0241  0.0108  599 GLU A N   
699  C CA  . GLU A 81  ? 0.4941 0.4022 0.4734 -0.0969 0.0225  0.0103  599 GLU A CA  
700  C C   . GLU A 81  ? 0.4466 0.3639 0.4266 -0.0791 0.0119  0.0023  599 GLU A C   
701  O O   . GLU A 81  ? 0.5276 0.4209 0.4834 -0.0684 0.0047  0.0008  599 GLU A O   
702  C CB  . GLU A 81  ? 0.4413 0.3585 0.4152 -0.0922 0.0341  0.0134  599 GLU A CB  
703  C CG  . GLU A 81  ? 0.4508 0.3463 0.4056 -0.1045 0.0461  0.0235  599 GLU A CG  
704  C CD  . GLU A 81  ? 0.6570 0.5038 0.5687 -0.1006 0.0402  0.0279  599 GLU A CD  
705  O OE1 . GLU A 81  ? 0.6974 0.5289 0.5804 -0.0845 0.0387  0.0285  599 GLU A OE1 
706  O OE2 . GLU A 81  ? 0.6267 0.4480 0.5309 -0.1127 0.0351  0.0305  599 GLU A OE2 
707  N N   . MET A 82  ? 0.3572 0.3086 0.3637 -0.0757 0.0119  -0.0021 600 MET A N   
708  C CA  . MET A 82  ? 0.4514 0.4170 0.4621 -0.0624 0.0041  -0.0077 600 MET A CA  
709  C C   . MET A 82  ? 0.4189 0.3732 0.4229 -0.0591 -0.0041 -0.0106 600 MET A C   
710  O O   . MET A 82  ? 0.4716 0.4261 0.4651 -0.0445 -0.0085 -0.0132 600 MET A O   
711  C CB  . MET A 82  ? 0.4364 0.4336 0.4759 -0.0647 0.0049  -0.0108 600 MET A CB  
712  C CG  . MET A 82  ? 0.4925 0.5004 0.5343 -0.0620 0.0104  -0.0111 600 MET A CG  
713  S SD  . MET A 82  ? 0.4639 0.4981 0.5354 -0.0649 0.0095  -0.0147 600 MET A SD  
714  C CE  . MET A 82  ? 0.6207 0.6579 0.6822 -0.0574 0.0084  -0.0178 600 MET A CE  
715  N N   . PHE A 83  ? 0.4041 0.3516 0.4153 -0.0725 -0.0062 -0.0104 601 PHE A N   
716  C CA  . PHE A 83  ? 0.5212 0.4559 0.5232 -0.0702 -0.0150 -0.0145 601 PHE A CA  
717  C C   . PHE A 83  ? 0.5227 0.4124 0.4906 -0.0709 -0.0190 -0.0139 601 PHE A C   
718  O O   . PHE A 83  ? 0.5970 0.4665 0.5496 -0.0698 -0.0270 -0.0181 601 PHE A O   
719  C CB  . PHE A 83  ? 0.4816 0.4342 0.5092 -0.0837 -0.0190 -0.0156 601 PHE A CB  
720  C CG  . PHE A 83  ? 0.4137 0.4020 0.4681 -0.0803 -0.0163 -0.0163 601 PHE A CG  
721  C CD1 . PHE A 83  ? 0.3723 0.3825 0.4549 -0.0904 -0.0146 -0.0145 601 PHE A CD1 
722  C CD2 . PHE A 83  ? 0.4024 0.4022 0.4537 -0.0667 -0.0157 -0.0182 601 PHE A CD2 
723  C CE1 . PHE A 83  ? 0.4376 0.4722 0.5388 -0.0853 -0.0130 -0.0154 601 PHE A CE1 
724  C CE2 . PHE A 83  ? 0.3895 0.4148 0.4609 -0.0660 -0.0144 -0.0183 601 PHE A CE2 
725  C CZ  . PHE A 83  ? 0.3464 0.3851 0.4401 -0.0746 -0.0133 -0.0173 601 PHE A CZ  
726  N N   . ASN A 84  ? 0.4625 0.3317 0.4138 -0.0726 -0.0139 -0.0086 602 ASN A N   
727  C CA  . ASN A 84  ? 0.4156 0.2337 0.3289 -0.0736 -0.0180 -0.0068 602 ASN A CA  
728  C C   . ASN A 84  ? 0.4932 0.2926 0.3775 -0.0473 -0.0230 -0.0117 602 ASN A C   
729  O O   . ASN A 84  ? 0.5439 0.3576 0.4265 -0.0300 -0.0199 -0.0107 602 ASN A O   
730  C CB  . ASN A 84  ? 0.4752 0.2750 0.3749 -0.0814 -0.0101 0.0019  602 ASN A CB  
731  C CG  . ASN A 84  ? 0.6790 0.4197 0.5385 -0.0888 -0.0145 0.0057  602 ASN A CG  
732  O OD1 . ASN A 84  ? 0.6552 0.3615 0.4860 -0.0775 -0.0239 0.0004  602 ASN A OD1 
733  N ND2 . ASN A 84  ? 0.7061 0.4321 0.5603 -0.1076 -0.0069 0.0152  602 ASN A ND2 
734  N N   . PRO A 85  ? 0.5718 0.3411 0.4332 -0.0429 -0.0311 -0.0172 603 PRO A N   
735  C CA  . PRO A 85  ? 0.5169 0.2718 0.3510 -0.0137 -0.0338 -0.0223 603 PRO A CA  
736  C C   . PRO A 85  ? 0.5824 0.3058 0.3845 0.0029  -0.0330 -0.0182 603 PRO A C   
737  O O   . PRO A 85  ? 0.6197 0.3464 0.4088 0.0308  -0.0336 -0.0209 603 PRO A O   
738  C CB  . PRO A 85  ? 0.5574 0.2722 0.3635 -0.0156 -0.0426 -0.0290 603 PRO A CB  
739  C CG  . PRO A 85  ? 0.6913 0.4203 0.5244 -0.0454 -0.0460 -0.0282 603 PRO A CG  
740  C CD  . PRO A 85  ? 0.6082 0.3555 0.4663 -0.0636 -0.0389 -0.0195 603 PRO A CD  
741  N N   . TYR A 86  ? 0.6257 0.3217 0.4160 -0.0135 -0.0313 -0.0108 604 TYR A N   
742  C CA  . TYR A 86  ? 0.6439 0.3061 0.4000 0.0012  -0.0312 -0.0052 604 TYR A CA  
743  C C   . TYR A 86  ? 0.5857 0.2914 0.3588 0.0221  -0.0282 -0.0042 604 TYR A C   
744  O O   . TYR A 86  ? 0.6220 0.3100 0.3686 0.0465  -0.0317 -0.0028 604 TYR A O   
745  C CB  . TYR A 86  ? 0.7678 0.4004 0.5126 -0.0246 -0.0270 0.0046  604 TYR A CB  
746  C CG  . TYR A 86  ? 0.8363 0.4450 0.5517 -0.0128 -0.0244 0.0129  604 TYR A CG  
747  C CD1 . TYR A 86  ? 0.8591 0.4066 0.5222 0.0049  -0.0312 0.0149  604 TYR A CD1 
748  C CD2 . TYR A 86  ? 0.8107 0.4531 0.5456 -0.0185 -0.0159 0.0187  604 TYR A CD2 
749  C CE1 . TYR A 86  ? 0.9053 0.4276 0.5375 0.0168  -0.0303 0.0236  604 TYR A CE1 
750  C CE2 . TYR A 86  ? 0.8382 0.4561 0.5411 -0.0076 -0.0147 0.0266  604 TYR A CE2 
751  C CZ  . TYR A 86  ? 0.9654 0.5241 0.6177 0.0098  -0.0223 0.0296  604 TYR A CZ  
752  O OH  . TYR A 86  ? 0.9191 0.4506 0.5361 0.0219  -0.0226 0.0383  604 TYR A OH  
753  N N   . TYR A 87  ? 0.5250 0.2861 0.3410 0.0129  -0.0234 -0.0050 605 TYR A N   
754  C CA  . TYR A 87  ? 0.5208 0.3210 0.3525 0.0279  -0.0229 -0.0043 605 TYR A CA  
755  C C   . TYR A 87  ? 0.5432 0.3746 0.3869 0.0508  -0.0265 -0.0102 605 TYR A C   
756  O O   . TYR A 87  ? 0.6413 0.5007 0.4928 0.0677  -0.0291 -0.0095 605 TYR A O   
757  C CB  . TYR A 87  ? 0.5474 0.3866 0.4139 0.0089  -0.0169 -0.0030 605 TYR A CB  
758  C CG  . TYR A 87  ? 0.6185 0.4351 0.4726 -0.0080 -0.0104 0.0042  605 TYR A CG  
759  C CD1 . TYR A 87  ? 0.6610 0.4870 0.5366 -0.0322 -0.0031 0.0056  605 TYR A CD1 
760  C CD2 . TYR A 87  ? 0.5678 0.3551 0.3881 0.0014  -0.0110 0.0102  605 TYR A CD2 
761  C CE1 . TYR A 87  ? 0.6496 0.4605 0.5161 -0.0476 0.0059  0.0133  605 TYR A CE1 
762  C CE2 . TYR A 87  ? 0.6755 0.4415 0.4812 -0.0146 -0.0026 0.0181  605 TYR A CE2 
763  C CZ  . TYR A 87  ? 0.6965 0.4765 0.5268 -0.0395 0.0071  0.0197  605 TYR A CZ  
764  O OH  . TYR A 87  ? 0.8016 0.5667 0.6201 -0.0552 0.0184  0.0285  605 TYR A OH  
765  N N   . GLY A 88  ? 0.5617 0.3889 0.4059 0.0511  -0.0267 -0.0156 606 GLY A N   
766  C CA  . GLY A 88  ? 0.5447 0.3963 0.3935 0.0747  -0.0273 -0.0202 606 GLY A CA  
767  C C   . GLY A 88  ? 0.5500 0.4619 0.4416 0.0693  -0.0235 -0.0216 606 GLY A C   
768  O O   . GLY A 88  ? 0.4619 0.4010 0.3606 0.0877  -0.0218 -0.0237 606 GLY A O   
769  N N   . LEU A 89  ? 0.4260 0.3574 0.3441 0.0451  -0.0215 -0.0198 607 LEU A N   
770  C CA  . LEU A 89  ? 0.3737 0.3529 0.3277 0.0370  -0.0188 -0.0205 607 LEU A CA  
771  C C   . LEU A 89  ? 0.3719 0.3479 0.3274 0.0304  -0.0172 -0.0239 607 LEU A C   
772  O O   . LEU A 89  ? 0.4199 0.4232 0.3860 0.0381  -0.0143 -0.0249 607 LEU A O   
773  C CB  . LEU A 89  ? 0.3417 0.3358 0.3170 0.0175  -0.0179 -0.0180 607 LEU A CB  
774  C CG  . LEU A 89  ? 0.4192 0.4113 0.3860 0.0239  -0.0206 -0.0150 607 LEU A CG  
775  C CD1 . LEU A 89  ? 0.5480 0.5498 0.5293 0.0069  -0.0187 -0.0139 607 LEU A CD1 
776  C CD2 . LEU A 89  ? 0.4431 0.4687 0.4193 0.0421  -0.0248 -0.0148 607 LEU A CD2 
777  N N   . PHE A 90  ? 0.4245 0.3689 0.3697 0.0150  -0.0192 -0.0250 608 PHE A N   
778  C CA  . PHE A 90  ? 0.4280 0.3607 0.3673 0.0089  -0.0215 -0.0288 608 PHE A CA  
779  C C   . PHE A 90  ? 0.5338 0.4150 0.4330 0.0159  -0.0263 -0.0326 608 PHE A C   
780  O O   . PHE A 90  ? 0.5659 0.4163 0.4444 0.0190  -0.0278 -0.0308 608 PHE A O   
781  C CB  . PHE A 90  ? 0.4131 0.3532 0.3750 -0.0155 -0.0232 -0.0273 608 PHE A CB  
782  C CG  . PHE A 90  ? 0.3623 0.3445 0.3571 -0.0209 -0.0198 -0.0250 608 PHE A CG  
783  C CD1 . PHE A 90  ? 0.3559 0.3552 0.3668 -0.0246 -0.0167 -0.0219 608 PHE A CD1 
784  C CD2 . PHE A 90  ? 0.3895 0.3889 0.3933 -0.0221 -0.0202 -0.0258 608 PHE A CD2 
785  C CE1 . PHE A 90  ? 0.2935 0.3238 0.3293 -0.0300 -0.0150 -0.0205 608 PHE A CE1 
786  C CE2 . PHE A 90  ? 0.4174 0.4483 0.4468 -0.0280 -0.0178 -0.0229 608 PHE A CE2 
787  C CZ  . PHE A 90  ? 0.3420 0.3871 0.3873 -0.0322 -0.0157 -0.0207 608 PHE A CZ  
788  N N   . GLU A 91  ? 0.4953 0.3624 0.3787 0.0184  -0.0294 -0.0378 609 GLU A N   
789  C CA  . GLU A 91  ? 0.5476 0.3587 0.3877 0.0230  -0.0364 -0.0431 609 GLU A CA  
790  C C   . GLU A 91  ? 0.5631 0.3648 0.3989 0.0096  -0.0434 -0.0477 609 GLU A C   
791  O O   . GLU A 91  ? 0.4970 0.3361 0.3570 0.0062  -0.0408 -0.0468 609 GLU A O   
792  C CB  . GLU A 91  ? 0.5903 0.3870 0.3988 0.0558  -0.0329 -0.0472 609 GLU A CB  
793  C CG  . GLU A 91  ? 0.6255 0.4491 0.4349 0.0709  -0.0271 -0.0509 609 GLU A CG  
794  C CD  . GLU A 91  ? 0.6939 0.5205 0.4827 0.1066  -0.0198 -0.0534 609 GLU A CD  
795  O OE1 . GLU A 91  ? 0.7542 0.5586 0.5259 0.1217  -0.0213 -0.0529 609 GLU A OE1 
796  O OE2 . GLU A 91  ? 0.8119 0.6636 0.6006 0.1209  -0.0120 -0.0554 609 GLU A OE2 
797  N N   . TYR A 92  ? 0.5673 0.3168 0.3703 0.0008  -0.0540 -0.0521 610 TYR A N   
798  C CA  . TYR A 92  ? 0.6030 0.3369 0.3937 -0.0098 -0.0643 -0.0578 610 TYR A CA  
799  C C   . TYR A 92  ? 0.5923 0.3276 0.3584 0.0152  -0.0602 -0.0639 610 TYR A C   
800  O O   . TYR A 92  ? 0.6509 0.3708 0.3896 0.0416  -0.0536 -0.0669 610 TYR A O   
801  C CB  . TYR A 92  ? 0.6689 0.3406 0.4237 -0.0244 -0.0784 -0.0620 610 TYR A CB  
802  C CG  . TYR A 92  ? 0.6529 0.3267 0.4336 -0.0527 -0.0812 -0.0546 610 TYR A CG  
803  C CD1 . TYR A 92  ? 0.6171 0.3326 0.4434 -0.0762 -0.0834 -0.0500 610 TYR A CD1 
804  C CD2 . TYR A 92  ? 0.7119 0.3466 0.4705 -0.0546 -0.0803 -0.0513 610 TYR A CD2 
805  C CE1 . TYR A 92  ? 0.6872 0.4104 0.5393 -0.1005 -0.0829 -0.0425 610 TYR A CE1 
806  C CE2 . TYR A 92  ? 0.7833 0.4215 0.5643 -0.0814 -0.0800 -0.0430 610 TYR A CE2 
807  C CZ  . TYR A 92  ? 0.7493 0.4341 0.5782 -0.1041 -0.0804 -0.0387 610 TYR A CZ  
808  O OH  . TYR A 92  ? 0.8056 0.4979 0.6575 -0.1289 -0.0774 -0.0299 610 TYR A OH  
809  N N   . SER A 93  ? 0.6223 0.3750 0.3961 0.0079  -0.0638 -0.0653 611 SER A N   
810  C CA  . SER A 93  ? 0.6402 0.4012 0.3932 0.0297  -0.0569 -0.0690 611 SER A CA  
811  C C   . SER A 93  ? 0.7319 0.4336 0.4227 0.0469  -0.0628 -0.0798 611 SER A C   
812  O O   . SER A 93  ? 0.8779 0.5817 0.5435 0.0729  -0.0528 -0.0834 611 SER A O   
813  C CB  . SER A 93  ? 0.5951 0.3853 0.3684 0.0162  -0.0602 -0.0662 611 SER A CB  
814  O OG  . SER A 93  ? 0.5931 0.3540 0.3565 -0.0050 -0.0788 -0.0701 611 SER A OG  
815  N N   . ALA A 94  ? 0.7244 0.3723 0.3893 0.0319  -0.0787 -0.0848 612 ALA A N   
816  C CA  . ALA A 94  ? 0.7378 0.3169 0.3374 0.0460  -0.0873 -0.0961 612 ALA A CA  
817  C C   . ALA A 94  ? 0.9574 0.4848 0.5428 0.0225  -0.1034 -0.0974 612 ALA A C   
818  O O   . ALA A 94  ? 0.8204 0.3699 0.4472 -0.0080 -0.1094 -0.0902 612 ALA A O   
819  C CB  . ALA A 94  ? 0.7711 0.3325 0.3377 0.0473  -0.0961 -0.1041 612 ALA A CB  
820  N N   . THR A 95  ? 0.9893 0.4460 0.5138 0.0368  -0.1100 -0.1064 613 THR A N   
821  C CA  . THR A 95  ? 1.0408 0.4511 0.5525 0.0146  -0.1229 -0.1031 613 THR A CA  
822  C C   . THR A 95  ? 1.0068 0.4273 0.5440 -0.0246 -0.1397 -0.0998 613 THR A C   
823  O O   . THR A 95  ? 0.9403 0.3655 0.5054 -0.0533 -0.1448 -0.0916 613 THR A O   
824  C CB  . THR A 95  ? 1.0899 0.4423 0.5433 0.0377  -0.1251 -0.1068 613 THR A CB  
825  O OG1 . THR A 95  ? 1.3245 0.6365 0.7668 0.0123  -0.1382 -0.1013 613 THR A OG1 
826  C CG2 . THR A 95  ? 1.2252 0.5649 0.6457 0.0510  -0.1296 -0.1147 613 THR A CG2 
827  N N   . ASP A 96  ? 0.9670 0.3987 0.4989 -0.0241 -0.1465 -0.1050 614 ASP A N   
828  C CA  . ASP A 96  ? 0.9116 0.3545 0.4653 -0.0558 -0.1639 -0.1022 614 ASP A CA  
829  C C   . ASP A 96  ? 0.8090 0.3149 0.4208 -0.0735 -0.1640 -0.0973 614 ASP A C   
830  O O   . ASP A 96  ? 0.8207 0.3453 0.4550 -0.0946 -0.1774 -0.0947 614 ASP A O   
831  C CB  . ASP A 96  ? 0.9750 0.3862 0.4832 -0.0451 -0.1745 -0.1099 614 ASP A CB  
832  C CG  . ASP A 96  ? 1.2820 0.6280 0.7318 -0.0295 -0.1771 -0.1141 614 ASP A CG  
833  O OD1 . ASP A 96  ? 1.3482 0.6684 0.7970 -0.0461 -0.1829 -0.1093 614 ASP A OD1 
834  O OD2 . ASP A 96  ? 1.4290 0.7499 0.8329 0.0001  -0.1726 -0.1214 614 ASP A OD2 
835  N N   . ASN A 97  ? 0.7574 0.2964 0.3928 -0.0632 -0.1496 -0.0958 615 ASN A N   
836  C CA  . ASN A 97  ? 0.7857 0.3959 0.4849 -0.0758 -0.1447 -0.0863 615 ASN A CA  
837  C C   . ASN A 97  ? 0.7910 0.4337 0.5397 -0.0918 -0.1360 -0.0758 615 ASN A C   
838  O O   . ASN A 97  ? 0.6650 0.2864 0.4014 -0.0851 -0.1272 -0.0740 615 ASN A O   
839  C CB  . ASN A 97  ? 0.7522 0.4057 0.4624 -0.0498 -0.1268 -0.0838 615 ASN A CB  
840  C CG  . ASN A 97  ? 0.8610 0.4917 0.5247 -0.0324 -0.1309 -0.0922 615 ASN A CG  
841  O OD1 . ASN A 97  ? 0.8484 0.4331 0.4729 -0.0406 -0.1502 -0.1008 615 ASN A OD1 
842  N ND2 . ASN A 97  ? 0.9063 0.5698 0.5732 -0.0092 -0.1127 -0.0893 615 ASN A ND2 
843  N N   . TYR A 98  ? 0.7748 0.4695 0.5770 -0.1093 -0.1371 -0.0686 616 TYR A N   
844  C CA  . TYR A 98  ? 0.7381 0.4699 0.5881 -0.1215 -0.1261 -0.0586 616 TYR A CA  
845  C C   . TYR A 98  ? 0.6275 0.4130 0.5114 -0.1055 -0.1091 -0.0533 616 TYR A C   
846  O O   . TYR A 98  ? 0.6221 0.4372 0.5393 -0.1092 -0.0973 -0.0462 616 TYR A O   
847  C CB  . TYR A 98  ? 0.8840 0.6358 0.7712 -0.1531 -0.1391 -0.0542 616 TYR A CB  
848  C CG  . TYR A 98  ? 1.0961 0.8772 1.0003 -0.1541 -0.1507 -0.0557 616 TYR A CG  
849  C CD1 . TYR A 98  ? 1.0585 0.8913 1.0035 -0.1501 -0.1451 -0.0507 616 TYR A CD1 
850  C CD2 . TYR A 98  ? 1.1158 0.8706 0.9920 -0.1567 -0.1668 -0.0612 616 TYR A CD2 
851  C CE1 . TYR A 98  ? 1.1016 0.9552 1.0570 -0.1497 -0.1573 -0.0515 616 TYR A CE1 
852  C CE2 . TYR A 98  ? 1.1238 0.9019 1.0111 -0.1565 -0.1784 -0.0620 616 TYR A CE2 
853  C CZ  . TYR A 98  ? 1.1404 0.9673 1.0668 -0.1525 -0.1737 -0.0569 616 TYR A CZ  
854  O OH  . TYR A 98  ? 1.2667 1.1125 1.2002 -0.1506 -0.1862 -0.0569 616 TYR A OH  
855  N N   . THR A 99  ? 0.5686 0.3642 0.4412 -0.0889 -0.1080 -0.0565 617 THR A N   
856  C CA  . THR A 99  ? 0.5076 0.3483 0.4075 -0.0758 -0.0930 -0.0512 617 THR A CA  
857  C C   . THR A 99  ? 0.4749 0.3156 0.3662 -0.0574 -0.0769 -0.0500 617 THR A C   
858  O O   . THR A 99  ? 0.5150 0.3188 0.3677 -0.0443 -0.0763 -0.0551 617 THR A O   
859  C CB  . THR A 99  ? 0.5624 0.4114 0.4489 -0.0646 -0.0952 -0.0531 617 THR A CB  
860  O OG1 . THR A 99  ? 0.5799 0.3864 0.4137 -0.0512 -0.0991 -0.0613 617 THR A OG1 
861  C CG2 . THR A 99  ? 0.6178 0.4813 0.5244 -0.0807 -0.1106 -0.0516 617 THR A CG2 
862  N N   . LEU A 100 ? 0.3946 0.2756 0.3207 -0.0555 -0.0652 -0.0436 618 LEU A N   
863  C CA  . LEU A 100 ? 0.4158 0.3061 0.3421 -0.0405 -0.0522 -0.0414 618 LEU A CA  
864  C C   . LEU A 100 ? 0.4639 0.3820 0.3926 -0.0238 -0.0429 -0.0403 618 LEU A C   
865  O O   . LEU A 100 ? 0.4947 0.4336 0.4363 -0.0280 -0.0437 -0.0383 618 LEU A O   
866  C CB  . LEU A 100 ? 0.4506 0.3649 0.4108 -0.0509 -0.0463 -0.0353 618 LEU A CB  
867  C CG  . LEU A 100 ? 0.5581 0.4534 0.5217 -0.0689 -0.0507 -0.0335 618 LEU A CG  
868  C CD1 . LEU A 100 ? 0.5734 0.4992 0.5712 -0.0772 -0.0426 -0.0275 618 LEU A CD1 
869  C CD2 . LEU A 100 ? 0.4989 0.3506 0.4260 -0.0624 -0.0512 -0.0353 618 LEU A CD2 
870  N N   . GLN A 101 ? 0.4452 0.3648 0.3619 -0.0052 -0.0344 -0.0407 619 GLN A N   
871  C CA  . GLN A 101 ? 0.3648 0.3205 0.2920 0.0086  -0.0237 -0.0376 619 GLN A CA  
872  C C   . GLN A 101 ? 0.4197 0.3936 0.3604 0.0176  -0.0173 -0.0346 619 GLN A C   
873  O O   . GLN A 101 ? 0.4173 0.3661 0.3461 0.0193  -0.0204 -0.0359 619 GLN A O   
874  C CB  . GLN A 101 ? 0.3734 0.3161 0.2666 0.0281  -0.0201 -0.0421 619 GLN A CB  
875  C CG  . GLN A 101 ? 0.4449 0.3554 0.3048 0.0489  -0.0192 -0.0475 619 GLN A CG  
876  C CD  . GLN A 101 ? 0.5684 0.4580 0.3876 0.0701  -0.0157 -0.0538 619 GLN A CD  
877  O OE1 . GLN A 101 ? 0.5535 0.4445 0.3637 0.0660  -0.0162 -0.0546 619 GLN A OE1 
878  N NE2 . GLN A 101 ? 0.5365 0.4055 0.3279 0.0952  -0.0118 -0.0580 619 GLN A NE2 
879  N N   . ILE A 102 ? 0.4082 0.4240 0.3721 0.0220  -0.0097 -0.0300 620 ILE A N   
880  C CA  . ILE A 102 ? 0.4463 0.4829 0.4222 0.0322  -0.0061 -0.0275 620 ILE A CA  
881  C C   . ILE A 102 ? 0.4474 0.4693 0.3956 0.0587  -0.0034 -0.0309 620 ILE A C   
882  O O   . ILE A 102 ? 0.3876 0.4119 0.3203 0.0732  0.0023  -0.0331 620 ILE A O   
883  C CB  . ILE A 102 ? 0.3541 0.4411 0.3619 0.0291  -0.0003 -0.0216 620 ILE A CB  
884  C CG1 . ILE A 102 ? 0.3377 0.4330 0.3684 0.0056  -0.0037 -0.0186 620 ILE A CG1 
885  C CG2 . ILE A 102 ? 0.2548 0.3651 0.2741 0.0408  0.0002  -0.0196 620 ILE A CG2 
886  C CD1 . ILE A 102 ? 0.3670 0.5028 0.4249 -0.0013 -0.0003 -0.0129 620 ILE A CD1 
887  N N   . ASN A 103 ? 0.3662 0.3714 0.3054 0.0669  -0.0068 -0.0312 621 ASN A N   
888  C CA  . ASN A 103 ? 0.4004 0.3883 0.3114 0.0956  -0.0053 -0.0342 621 ASN A CA  
889  C C   . ASN A 103 ? 0.4667 0.5096 0.4011 0.1143  0.0021  -0.0306 621 ASN A C   
890  O O   . ASN A 103 ? 0.5449 0.6230 0.5093 0.1080  0.0003  -0.0256 621 ASN A O   
891  C CB  . ASN A 103 ? 0.4470 0.3958 0.3380 0.0979  -0.0124 -0.0340 621 ASN A CB  
892  C CG  . ASN A 103 ? 0.5342 0.4633 0.3952 0.1306  -0.0123 -0.0363 621 ASN A CG  
893  O OD1 . ASN A 103 ? 0.6496 0.5800 0.4948 0.1528  -0.0070 -0.0403 621 ASN A OD1 
894  N ND2 . ASN A 103 ? 0.6366 0.5454 0.4863 0.1360  -0.0178 -0.0334 621 ASN A ND2 
895  N N   . PRO A 104 ? 0.4682 0.5201 0.3889 0.1370  0.0103  -0.0330 622 PRO A N   
896  C CA  . PRO A 104 ? 0.4903 0.6026 0.4378 0.1553  0.0191  -0.0285 622 PRO A CA  
897  C C   . PRO A 104 ? 0.4915 0.6146 0.4450 0.1735  0.0134  -0.0266 622 PRO A C   
898  O O   . PRO A 104 ? 0.5266 0.7083 0.5179 0.1750  0.0147  -0.0208 622 PRO A O   
899  C CB  . PRO A 104 ? 0.4929 0.5983 0.4120 0.1814  0.0299  -0.0330 622 PRO A CB  
900  C CG  . PRO A 104 ? 0.5517 0.5802 0.4201 0.1819  0.0224  -0.0416 622 PRO A CG  
901  C CD  . PRO A 104 ? 0.4938 0.5031 0.3738 0.1461  0.0122  -0.0400 622 PRO A CD  
902  N N   . ASN A 105 ? 0.5276 0.5937 0.4434 0.1852  0.0058  -0.0309 623 ASN A N   
903  C CA  . ASN A 105 ? 0.5173 0.5827 0.4301 0.2036  -0.0016 -0.0286 623 ASN A CA  
904  C C   . ASN A 105 ? 0.4117 0.4681 0.3353 0.1792  -0.0116 -0.0247 623 ASN A C   
905  O O   . ASN A 105 ? 0.4504 0.4863 0.3578 0.1918  -0.0193 -0.0231 623 ASN A O   
906  C CB  . ASN A 105 ? 0.6312 0.6320 0.4901 0.2316  -0.0048 -0.0340 623 ASN A CB  
907  C CG  . ASN A 105 ? 0.8659 0.8660 0.7039 0.2611  0.0053  -0.0396 623 ASN A CG  
908  O OD1 . ASN A 105 ? 0.8411 0.9048 0.7096 0.2754  0.0154  -0.0370 623 ASN A OD1 
909  N ND2 . ASN A 105 ? 0.9123 0.8395 0.6965 0.2700  0.0029  -0.0472 623 ASN A ND2 
910  N N   . SER A 106 ? 0.3725 0.4419 0.3199 0.1468  -0.0111 -0.0231 624 SER A N   
911  C CA  . SER A 106 ? 0.3542 0.4153 0.3100 0.1246  -0.0183 -0.0201 624 SER A CA  
912  C C   . SER A 106 ? 0.3721 0.4646 0.3428 0.1353  -0.0255 -0.0161 624 SER A C   
913  O O   . SER A 106 ? 0.4210 0.4898 0.3790 0.1297  -0.0324 -0.0143 624 SER A O   
914  C CB  . SER A 106 ? 0.3120 0.3959 0.2973 0.0940  -0.0158 -0.0190 624 SER A CB  
915  O OG  . SER A 106 ? 0.3527 0.4929 0.3709 0.0942  -0.0115 -0.0165 624 SER A OG  
916  N N   . GLY A 107 ? 0.3560 0.5045 0.3543 0.1497  -0.0238 -0.0141 625 GLY A N   
917  C CA  . GLY A 107 ? 0.3626 0.5509 0.3814 0.1591  -0.0331 -0.0103 625 GLY A CA  
918  C C   . GLY A 107 ? 0.4335 0.5999 0.4245 0.1910  -0.0405 -0.0098 625 GLY A C   
919  O O   . GLY A 107 ? 0.4343 0.6102 0.4281 0.1942  -0.0523 -0.0068 625 GLY A O   
920  N N   . LEU A 108 ? 0.4848 0.6182 0.4450 0.2157  -0.0347 -0.0130 626 LEU A N   
921  C CA  . LEU A 108 ? 0.5443 0.6422 0.4682 0.2487  -0.0416 -0.0129 626 LEU A CA  
922  C C   . LEU A 108 ? 0.5091 0.5480 0.3996 0.2354  -0.0505 -0.0109 626 LEU A C   
923  O O   . LEU A 108 ? 0.6687 0.7025 0.5476 0.2496  -0.0614 -0.0071 626 LEU A O   
924  C CB  . LEU A 108 ? 0.6135 0.6698 0.5006 0.2733  -0.0335 -0.0184 626 LEU A CB  
925  C CG  . LEU A 108 ? 0.6773 0.7668 0.5672 0.3172  -0.0304 -0.0191 626 LEU A CG  
926  C CD1 . LEU A 108 ? 0.7551 0.7801 0.5919 0.3422  -0.0245 -0.0261 626 LEU A CD1 
927  C CD2 . LEU A 108 ? 0.5512 0.6532 0.4420 0.3390  -0.0440 -0.0142 626 LEU A CD2 
928  N N   . CYS A 109 ? 0.6814 0.6773 0.5565 0.2078  -0.0452 -0.0129 627 CYS A N   
929  C CA  . CYS A 109 ? 0.8816 0.8229 0.7271 0.1898  -0.0493 -0.0100 627 CYS A CA  
930  C C   . CYS A 109 ? 0.8305 0.8020 0.6984 0.1725  -0.0553 -0.0060 627 CYS A C   
931  O O   . CYS A 109 ? 0.8762 0.8159 0.7172 0.1738  -0.0618 -0.0017 627 CYS A O   
932  C CB  . CYS A 109 ? 1.0430 0.9480 0.8795 0.1618  -0.0416 -0.0129 627 CYS A CB  
933  S SG  . CYS A 109 ? 1.0839 0.9637 0.9019 0.1725  -0.0350 -0.0203 627 CYS A SG  
934  N N   . ASN A 110 ? 0.6757 0.7035 0.5880 0.1561  -0.0532 -0.0072 628 ASN A N   
935  C CA  . ASN A 110 ? 0.5289 0.5793 0.4600 0.1354  -0.0585 -0.0055 628 ASN A CA  
936  C C   . ASN A 110 ? 0.3624 0.4824 0.3371 0.1363  -0.0643 -0.0053 628 ASN A C   
937  O O   . ASN A 110 ? 0.4038 0.5574 0.4095 0.1230  -0.0576 -0.0068 628 ASN A O   
938  C CB  . ASN A 110 ? 0.4856 0.5218 0.4234 0.1040  -0.0500 -0.0072 628 ASN A CB  
939  C CG  . ASN A 110 ? 0.6748 0.6548 0.5817 0.0987  -0.0427 -0.0075 628 ASN A CG  
940  O OD1 . ASN A 110 ? 0.6726 0.6111 0.5504 0.0937  -0.0430 -0.0042 628 ASN A OD1 
941  N ND2 . ASN A 110 ? 0.6555 0.6336 0.5673 0.0980  -0.0365 -0.0109 628 ASN A ND2 
942  N N   . GLU A 111 ? 0.3763 0.5177 0.3529 0.1509  -0.0775 -0.0027 629 GLU A N   
943  C CA  . GLU A 111 ? 0.4721 0.6827 0.4928 0.1486  -0.0858 -0.0017 629 GLU A CA  
944  C C   . GLU A 111 ? 0.4559 0.6822 0.5000 0.1137  -0.0849 -0.0035 629 GLU A C   
945  O O   . GLU A 111 ? 0.3793 0.6554 0.4622 0.1023  -0.0838 -0.0030 629 GLU A O   
946  C CB  . GLU A 111 ? 0.5177 0.7425 0.5322 0.1667  -0.1042 0.0012  629 GLU A CB  
947  C CG  . GLU A 111 ? 0.6705 0.9744 0.7337 0.1722  -0.1141 0.0032  629 GLU A CG  
948  C CD  . GLU A 111 ? 0.7783 1.0993 0.8364 0.1925  -0.1356 0.0062  629 GLU A CD  
949  O OE1 . GLU A 111 ? 0.7703 1.0364 0.7815 0.2058  -0.1417 0.0071  629 GLU A OE1 
950  O OE2 . GLU A 111 ? 0.8244 1.2149 0.9259 0.1943  -0.1468 0.0084  629 GLU A OE2 
951  N N   . ASP A 112 ? 0.4843 0.6657 0.5027 0.0973  -0.0840 -0.0052 630 ASP A N   
952  C CA  . ASP A 112 ? 0.4400 0.6277 0.4732 0.0683  -0.0839 -0.0078 630 ASP A CA  
953  C C   . ASP A 112 ? 0.4072 0.5807 0.4472 0.0520  -0.0684 -0.0097 630 ASP A C   
954  O O   . ASP A 112 ? 0.3691 0.5266 0.4073 0.0321  -0.0656 -0.0120 630 ASP A O   
955  C CB  . ASP A 112 ? 0.4708 0.6213 0.4721 0.0617  -0.0903 -0.0090 630 ASP A CB  
956  C CG  . ASP A 112 ? 0.6265 0.7921 0.6414 0.0392  -0.0980 -0.0126 630 ASP A CG  
957  O OD1 . ASP A 112 ? 0.4467 0.6556 0.4975 0.0286  -0.1024 -0.0128 630 ASP A OD1 
958  O OD2 . ASP A 112 ? 0.6933 0.8251 0.6804 0.0319  -0.0990 -0.0149 630 ASP A OD2 
959  N N   . HIS A 113 ? 0.3501 0.5298 0.3966 0.0620  -0.0593 -0.0090 631 HIS A N   
960  C CA  . HIS A 113 ? 0.3069 0.4665 0.3525 0.0496  -0.0470 -0.0107 631 HIS A CA  
961  C C   . HIS A 113 ? 0.2265 0.4094 0.2996 0.0261  -0.0448 -0.0113 631 HIS A C   
962  O O   . HIS A 113 ? 0.3123 0.4726 0.3815 0.0123  -0.0384 -0.0129 631 HIS A O   
963  C CB  . HIS A 113 ? 0.4128 0.5712 0.4527 0.0685  -0.0398 -0.0106 631 HIS A CB  
964  C CG  . HIS A 113 ? 0.5468 0.7578 0.6171 0.0746  -0.0370 -0.0088 631 HIS A CG  
965  N ND1 . HIS A 113 ? 0.7632 1.0031 0.8608 0.0546  -0.0328 -0.0075 631 HIS A ND1 
966  C CD2 . HIS A 113 ? 0.5531 0.7992 0.6338 0.0978  -0.0385 -0.0067 631 HIS A CD2 
967  C CE1 . HIS A 113 ? 0.6726 0.9604 0.7941 0.0638  -0.0294 -0.0041 631 HIS A CE1 
968  N NE2 . HIS A 113 ? 0.5063 0.8025 0.6206 0.0908  -0.0325 -0.0039 631 HIS A NE2 
969  N N   . LEU A 114 ? 0.2644 0.4917 0.3650 0.0208  -0.0510 -0.0093 632 LEU A N   
970  C CA  . LEU A 114 ? 0.3221 0.5642 0.4438 -0.0027 -0.0497 -0.0089 632 LEU A CA  
971  C C   . LEU A 114 ? 0.2417 0.4523 0.3501 -0.0189 -0.0537 -0.0126 632 LEU A C   
972  O O   . LEU A 114 ? 0.2582 0.4541 0.3682 -0.0326 -0.0482 -0.0137 632 LEU A O   
973  C CB  . LEU A 114 ? 0.1882 0.4839 0.3424 -0.0093 -0.0566 -0.0049 632 LEU A CB  
974  C CG  . LEU A 114 ? 0.2345 0.5710 0.4084 0.0046  -0.0483 -0.0001 632 LEU A CG  
975  C CD1 . LEU A 114 ? 0.1754 0.5710 0.3880 -0.0085 -0.0525 0.0058  632 LEU A CD1 
976  C CD2 . LEU A 114 ? 0.2400 0.5548 0.4037 0.0039  -0.0337 -0.0003 632 LEU A CD2 
977  N N   . SER A 115 ? 0.2781 0.4763 0.3702 -0.0151 -0.0629 -0.0147 633 SER A N   
978  C CA  . SER A 115 ? 0.3511 0.5164 0.4249 -0.0265 -0.0638 -0.0188 633 SER A CA  
979  C C   . SER A 115 ? 0.2938 0.4233 0.3499 -0.0236 -0.0506 -0.0195 633 SER A C   
980  O O   . SER A 115 ? 0.3682 0.4805 0.4220 -0.0344 -0.0454 -0.0220 633 SER A O   
981  C CB  . SER A 115 ? 0.4828 0.6404 0.5370 -0.0219 -0.0765 -0.0209 633 SER A CB  
982  O OG  . SER A 115 ? 0.6478 0.7842 0.6770 -0.0044 -0.0742 -0.0191 633 SER A OG  
983  N N   . TYR A 116 ? 0.2926 0.4110 0.3371 -0.0096 -0.0455 -0.0173 634 TYR A N   
984  C CA  . TYR A 116 ? 0.2327 0.3199 0.2643 -0.0119 -0.0347 -0.0173 634 TYR A CA  
985  C C   . TYR A 116 ? 0.2106 0.3052 0.2616 -0.0222 -0.0286 -0.0179 634 TYR A C   
986  O O   . TYR A 116 ? 0.2729 0.3509 0.3227 -0.0306 -0.0224 -0.0189 634 TYR A O   
987  C CB  . TYR A 116 ? 0.2545 0.3213 0.2662 0.0025  -0.0321 -0.0148 634 TYR A CB  
988  C CG  . TYR A 116 ? 0.3149 0.3693 0.3025 0.0160  -0.0388 -0.0128 634 TYR A CG  
989  C CD1 . TYR A 116 ? 0.2913 0.3412 0.2678 0.0120  -0.0439 -0.0136 634 TYR A CD1 
990  C CD2 . TYR A 116 ? 0.3622 0.4059 0.3338 0.0347  -0.0410 -0.0105 634 TYR A CD2 
991  C CE1 . TYR A 116 ? 0.4259 0.4631 0.3764 0.0255  -0.0520 -0.0112 634 TYR A CE1 
992  C CE2 . TYR A 116 ? 0.4224 0.4521 0.3690 0.0495  -0.0486 -0.0078 634 TYR A CE2 
993  C CZ  . TYR A 116 ? 0.4261 0.4536 0.3626 0.0444  -0.0545 -0.0077 634 TYR A CZ  
994  O OH  . TYR A 116 ? 0.5372 0.5491 0.4454 0.0599  -0.0636 -0.0045 634 TYR A OH  
995  N N   . PHE A 117 ? 0.2539 0.3747 0.3221 -0.0204 -0.0298 -0.0166 635 PHE A N   
996  C CA  . PHE A 117 ? 0.2942 0.4191 0.3754 -0.0293 -0.0247 -0.0162 635 PHE A CA  
997  C C   . PHE A 117 ? 0.2640 0.3907 0.3558 -0.0447 -0.0268 -0.0173 635 PHE A C   
998  O O   . PHE A 117 ? 0.2930 0.4081 0.3874 -0.0515 -0.0229 -0.0178 635 PHE A O   
999  C CB  . PHE A 117 ? 0.1976 0.3498 0.2906 -0.0231 -0.0233 -0.0136 635 PHE A CB  
1000 C CG  . PHE A 117 ? 0.2885 0.4280 0.3656 -0.0070 -0.0192 -0.0141 635 PHE A CG  
1001 C CD1 . PHE A 117 ? 0.2581 0.3726 0.3241 -0.0094 -0.0153 -0.0157 635 PHE A CD1 
1002 C CD2 . PHE A 117 ? 0.2877 0.4383 0.3590 0.0113  -0.0210 -0.0134 635 PHE A CD2 
1003 C CE1 . PHE A 117 ? 0.3052 0.4002 0.3505 0.0043  -0.0134 -0.0173 635 PHE A CE1 
1004 C CE2 . PHE A 117 ? 0.3212 0.4519 0.3715 0.0285  -0.0177 -0.0148 635 PHE A CE2 
1005 C CZ  . PHE A 117 ? 0.2671 0.3674 0.3025 0.0239  -0.0141 -0.0172 635 PHE A CZ  
1006 N N   . LYS A 118 ? 0.2743 0.4140 0.3705 -0.0494 -0.0344 -0.0178 636 LYS A N   
1007 C CA  . LYS A 118 ? 0.3093 0.4414 0.4083 -0.0633 -0.0379 -0.0199 636 LYS A CA  
1008 C C   . LYS A 118 ? 0.3346 0.4364 0.4179 -0.0622 -0.0330 -0.0238 636 LYS A C   
1009 O O   . LYS A 118 ? 0.3147 0.4049 0.4004 -0.0681 -0.0304 -0.0251 636 LYS A O   
1010 C CB  . LYS A 118 ? 0.3189 0.4645 0.4201 -0.0699 -0.0497 -0.0209 636 LYS A CB  
1011 C CG  . LYS A 118 ? 0.3395 0.4678 0.4365 -0.0847 -0.0551 -0.0241 636 LYS A CG  
1012 C CD  . LYS A 118 ? 0.3649 0.5054 0.4636 -0.0948 -0.0699 -0.0254 636 LYS A CD  
1013 C CE  . LYS A 118 ? 0.4223 0.5411 0.5145 -0.1115 -0.0765 -0.0283 636 LYS A CE  
1014 N NZ  . LYS A 118 ? 0.4416 0.5671 0.5310 -0.1231 -0.0938 -0.0307 636 LYS A NZ  
1015 N N   . PHE A 119 ? 0.3423 0.4323 0.4093 -0.0534 -0.0309 -0.0247 637 PHE A N   
1016 C CA  . PHE A 119 ? 0.3517 0.4183 0.4052 -0.0519 -0.0229 -0.0267 637 PHE A CA  
1017 C C   . PHE A 119 ? 0.3477 0.4118 0.4126 -0.0537 -0.0146 -0.0249 637 PHE A C   
1018 O O   . PHE A 119 ? 0.3456 0.4023 0.4139 -0.0564 -0.0095 -0.0265 637 PHE A O   
1019 C CB  . PHE A 119 ? 0.3290 0.3829 0.3607 -0.0433 -0.0212 -0.0254 637 PHE A CB  
1020 C CG  . PHE A 119 ? 0.3470 0.3817 0.3680 -0.0430 -0.0092 -0.0243 637 PHE A CG  
1021 C CD1 . PHE A 119 ? 0.3157 0.3406 0.3302 -0.0450 -0.0029 -0.0273 637 PHE A CD1 
1022 C CD2 . PHE A 119 ? 0.3953 0.4210 0.4110 -0.0406 -0.0038 -0.0199 637 PHE A CD2 
1023 C CE1 . PHE A 119 ? 0.3811 0.3958 0.3898 -0.0450 0.0105  -0.0249 637 PHE A CE1 
1024 C CE2 . PHE A 119 ? 0.4104 0.4218 0.4189 -0.0441 0.0075  -0.0171 637 PHE A CE2 
1025 C CZ  . PHE A 119 ? 0.3104 0.3206 0.3185 -0.0465 0.0157  -0.0191 637 PHE A CZ  
1026 N N   . ILE A 120 ? 0.2777 0.3476 0.3473 -0.0509 -0.0142 -0.0220 638 ILE A N   
1027 C CA  . ILE A 120 ? 0.3047 0.3715 0.3833 -0.0539 -0.0098 -0.0208 638 ILE A CA  
1028 C C   . ILE A 120 ? 0.1686 0.2433 0.2622 -0.0599 -0.0118 -0.0213 638 ILE A C   
1029 O O   . ILE A 120 ? 0.2544 0.3255 0.3559 -0.0623 -0.0090 -0.0214 638 ILE A O   
1030 C CB  . ILE A 120 ? 0.3371 0.4033 0.4113 -0.0489 -0.0111 -0.0190 638 ILE A CB  
1031 C CG1 . ILE A 120 ? 0.3624 0.4119 0.4166 -0.0420 -0.0096 -0.0180 638 ILE A CG1 
1032 C CG2 . ILE A 120 ? 0.2860 0.3473 0.3671 -0.0539 -0.0100 -0.0187 638 ILE A CG2 
1033 C CD1 . ILE A 120 ? 0.3765 0.4172 0.4187 -0.0334 -0.0115 -0.0173 638 ILE A CD1 
1034 N N   . GLY A 121 ? 0.2208 0.3069 0.3186 -0.0623 -0.0171 -0.0207 639 GLY A N   
1035 C CA  . GLY A 121 ? 0.3551 0.4423 0.4616 -0.0692 -0.0196 -0.0199 639 GLY A CA  
1036 C C   . GLY A 121 ? 0.3747 0.4470 0.4781 -0.0706 -0.0192 -0.0234 639 GLY A C   
1037 O O   . GLY A 121 ? 0.3259 0.3920 0.4349 -0.0707 -0.0186 -0.0231 639 GLY A O   
1038 N N   . ARG A 122 ? 0.3007 0.3656 0.3923 -0.0694 -0.0201 -0.0270 640 ARG A N   
1039 C CA  . ARG A 122 ? 0.2653 0.3122 0.3473 -0.0669 -0.0179 -0.0316 640 ARG A CA  
1040 C C   . ARG A 122 ? 0.3429 0.3887 0.4312 -0.0602 -0.0079 -0.0315 640 ARG A C   
1041 O O   . ARG A 122 ? 0.3175 0.3564 0.4092 -0.0566 -0.0057 -0.0333 640 ARG A O   
1042 C CB  . ARG A 122 ? 0.2419 0.2791 0.3039 -0.0652 -0.0202 -0.0358 640 ARG A CB  
1043 C CG  . ARG A 122 ? 0.2472 0.2837 0.3040 -0.0743 -0.0331 -0.0374 640 ARG A CG  
1044 C CD  . ARG A 122 ? 0.2941 0.3155 0.3265 -0.0726 -0.0385 -0.0432 640 ARG A CD  
1045 N NE  . ARG A 122 ? 0.3241 0.3452 0.3538 -0.0849 -0.0536 -0.0448 640 ARG A NE  
1046 C CZ  . ARG A 122 ? 0.3976 0.4025 0.4042 -0.0871 -0.0637 -0.0508 640 ARG A CZ  
1047 N NH1 . ARG A 122 ? 0.4559 0.4418 0.4365 -0.0756 -0.0584 -0.0557 640 ARG A NH1 
1048 N NH2 . ARG A 122 ? 0.3140 0.3217 0.3222 -0.1019 -0.0794 -0.0516 640 ARG A NH2 
1049 N N   . VAL A 123 ? 0.3052 0.3581 0.3958 -0.0588 -0.0023 -0.0289 641 VAL A N   
1050 C CA  . VAL A 123 ? 0.2375 0.2942 0.3380 -0.0564 0.0070  -0.0275 641 VAL A CA  
1051 C C   . VAL A 123 ? 0.3119 0.3787 0.4330 -0.0582 0.0037  -0.0253 641 VAL A C   
1052 O O   . VAL A 123 ? 0.3194 0.3917 0.4531 -0.0543 0.0077  -0.0256 641 VAL A O   
1053 C CB  . VAL A 123 ? 0.3730 0.4296 0.4678 -0.0582 0.0125  -0.0241 641 VAL A CB  
1054 C CG1 . VAL A 123 ? 0.2704 0.3365 0.3826 -0.0615 0.0198  -0.0208 641 VAL A CG1 
1055 C CG2 . VAL A 123 ? 0.3787 0.4227 0.4496 -0.0542 0.0171  -0.0255 641 VAL A CG2 
1056 N N   . ALA A 124 ? 0.2841 0.3543 0.4075 -0.0624 -0.0036 -0.0231 642 ALA A N   
1057 C CA  . ALA A 124 ? 0.2878 0.3633 0.4238 -0.0637 -0.0091 -0.0210 642 ALA A CA  
1058 C C   . ALA A 124 ? 0.3048 0.3742 0.4427 -0.0601 -0.0117 -0.0222 642 ALA A C   
1059 O O   . ALA A 124 ? 0.3619 0.4357 0.5123 -0.0557 -0.0124 -0.0215 642 ALA A O   
1060 C CB  . ALA A 124 ? 0.2159 0.2925 0.3460 -0.0670 -0.0149 -0.0188 642 ALA A CB  
1061 N N   . GLY A 125 ? 0.3965 0.4548 0.5213 -0.0619 -0.0144 -0.0237 643 GLY A N   
1062 C CA  . GLY A 125 ? 0.3354 0.3775 0.4541 -0.0591 -0.0176 -0.0256 643 GLY A CA  
1063 C C   . GLY A 125 ? 0.3142 0.3519 0.4347 -0.0477 -0.0108 -0.0296 643 GLY A C   
1064 O O   . GLY A 125 ? 0.4267 0.4583 0.5515 -0.0398 -0.0126 -0.0297 643 GLY A O   
1065 N N   . MET A 126 ? 0.3454 0.3863 0.4611 -0.0450 -0.0022 -0.0325 644 MET A N   
1066 C CA  . MET A 126 ? 0.3633 0.4046 0.4806 -0.0330 0.0079  -0.0357 644 MET A CA  
1067 C C   . MET A 126 ? 0.3442 0.4094 0.4897 -0.0282 0.0117  -0.0319 644 MET A C   
1068 O O   . MET A 126 ? 0.3330 0.4014 0.4859 -0.0151 0.0167  -0.0337 644 MET A O   
1069 C CB  . MET A 126 ? 0.3477 0.3890 0.4521 -0.0325 0.0181  -0.0375 644 MET A CB  
1070 C CG  . MET A 126 ? 0.3437 0.3602 0.4178 -0.0330 0.0137  -0.0431 644 MET A CG  
1071 S SD  . MET A 126 ? 0.4116 0.4279 0.4673 -0.0341 0.0217  -0.0428 644 MET A SD  
1072 C CE  . MET A 126 ? 0.3697 0.3922 0.4270 -0.0212 0.0416  -0.0435 644 MET A CE  
1073 N N   . ALA A 127 ? 0.3015 0.3833 0.4621 -0.0378 0.0085  -0.0271 645 ALA A N   
1074 C CA  . ALA A 127 ? 0.2897 0.3956 0.4781 -0.0368 0.0082  -0.0235 645 ALA A CA  
1075 C C   . ALA A 127 ? 0.2944 0.3979 0.4899 -0.0285 -0.0016 -0.0230 645 ALA A C   
1076 O O   . ALA A 127 ? 0.3301 0.4485 0.5437 -0.0173 0.0008  -0.0228 645 ALA A O   
1077 C CB  . ALA A 127 ? 0.3414 0.4558 0.5362 -0.0501 0.0033  -0.0197 645 ALA A CB  
1078 N N   . VAL A 128 ? 0.3628 0.4487 0.5438 -0.0336 -0.0122 -0.0219 646 VAL A N   
1079 C CA  . VAL A 128 ? 0.4218 0.4976 0.6019 -0.0268 -0.0224 -0.0200 646 VAL A CA  
1080 C C   . VAL A 128 ? 0.4169 0.4756 0.5884 -0.0115 -0.0194 -0.0238 646 VAL A C   
1081 O O   . VAL A 128 ? 0.3484 0.4114 0.5310 0.0024  -0.0228 -0.0228 646 VAL A O   
1082 C CB  . VAL A 128 ? 0.3898 0.4466 0.5503 -0.0369 -0.0310 -0.0170 646 VAL A CB  
1083 C CG1 . VAL A 128 ? 0.3071 0.3461 0.4598 -0.0304 -0.0405 -0.0137 646 VAL A CG1 
1084 C CG2 . VAL A 128 ? 0.3382 0.4087 0.5030 -0.0472 -0.0341 -0.0140 646 VAL A CG2 
1085 N N   . TYR A 129 ? 0.3725 0.4108 0.5226 -0.0126 -0.0139 -0.0285 647 TYR A N   
1086 C CA  . TYR A 129 ? 0.3847 0.3970 0.5172 0.0019  -0.0118 -0.0339 647 TYR A CA  
1087 C C   . TYR A 129 ? 0.3878 0.4202 0.5379 0.0215  -0.0008 -0.0364 647 TYR A C   
1088 O O   . TYR A 129 ? 0.4600 0.4792 0.6059 0.0400  -0.0022 -0.0386 647 TYR A O   
1089 C CB  . TYR A 129 ? 0.3377 0.3254 0.4420 -0.0048 -0.0093 -0.0396 647 TYR A CB  
1090 C CG  . TYR A 129 ? 0.4404 0.3879 0.5164 0.0070  -0.0116 -0.0461 647 TYR A CG  
1091 C CD1 . TYR A 129 ? 0.4455 0.3578 0.5000 -0.0013 -0.0244 -0.0450 647 TYR A CD1 
1092 C CD2 . TYR A 129 ? 0.3454 0.2878 0.4134 0.0267  -0.0004 -0.0530 647 TYR A CD2 
1093 C CE1 . TYR A 129 ? 0.5335 0.4000 0.5566 0.0085  -0.0285 -0.0513 647 TYR A CE1 
1094 C CE2 . TYR A 129 ? 0.4758 0.3745 0.5117 0.0401  -0.0032 -0.0603 647 TYR A CE2 
1095 C CZ  . TYR A 129 ? 0.5455 0.4034 0.5578 0.0304  -0.0184 -0.0597 647 TYR A CZ  
1096 O OH  . TYR A 129 ? 0.6550 0.4615 0.6304 0.0422  -0.0230 -0.0673 647 TYR A OH  
1097 N N   . HIS A 130 ? 0.3627 0.4618 0.4708 0.0089  -0.0032 0.0243  648 HIS A N   
1098 C CA  . HIS A 130 ? 0.3394 0.4552 0.4697 0.0100  0.0017  0.0196  648 HIS A CA  
1099 C C   . HIS A 130 ? 0.3542 0.4908 0.5086 0.0131  -0.0063 0.0111  648 HIS A C   
1100 O O   . HIS A 130 ? 0.3942 0.5493 0.5733 0.0116  -0.0015 0.0039  648 HIS A O   
1101 C CB  . HIS A 130 ? 0.2985 0.4160 0.4332 0.0005  0.0142  0.0217  648 HIS A CB  
1102 C CG  . HIS A 130 ? 0.4324 0.5390 0.5469 0.0004  0.0213  0.0261  648 HIS A CG  
1103 N ND1 . HIS A 130 ? 0.4207 0.5179 0.5156 -0.0025 0.0210  0.0301  648 HIS A ND1 
1104 C CD2 . HIS A 130 ? 0.3301 0.4374 0.4424 0.0033  0.0284  0.0248  648 HIS A CD2 
1105 C CE1 . HIS A 130 ? 0.4617 0.5573 0.5442 -0.0011 0.0268  0.0294  648 HIS A CE1 
1106 N NE2 . HIS A 130 ? 0.4185 0.5186 0.5105 0.0018  0.0317  0.0264  648 HIS A NE2 
1107 N N   . GLY A 131 ? 0.3722 0.5081 0.5207 0.0172  -0.0178 0.0098  649 GLY A N   
1108 C CA  . GLY A 131 ? 0.3287 0.4897 0.4995 0.0223  -0.0280 -0.0018 649 GLY A CA  
1109 C C   . GLY A 131 ? 0.3878 0.5650 0.5860 0.0077  -0.0225 -0.0108 649 GLY A C   
1110 O O   . GLY A 131 ? 0.3904 0.5958 0.6190 0.0078  -0.0251 -0.0255 649 GLY A O   
1111 N N   . LYS A 132 ? 0.4123 0.5717 0.6004 -0.0044 -0.0136 -0.0035 650 LYS A N   
1112 C CA  . LYS A 132 ? 0.3955 0.5613 0.6051 -0.0183 -0.0038 -0.0104 650 LYS A CA  
1113 C C   . LYS A 132 ? 0.4070 0.5643 0.6071 -0.0223 -0.0101 -0.0101 650 LYS A C   
1114 O O   . LYS A 132 ? 0.4728 0.6164 0.6470 -0.0155 -0.0196 -0.0020 650 LYS A O   
1115 C CB  . LYS A 132 ? 0.4618 0.6113 0.6659 -0.0266 0.0159  -0.0014 650 LYS A CB  
1116 C CG  . LYS A 132 ? 0.4807 0.6362 0.6911 -0.0230 0.0239  -0.0010 650 LYS A CG  
1117 C CD  . LYS A 132 ? 0.5976 0.7823 0.8457 -0.0244 0.0246  -0.0176 650 LYS A CD  
1118 C CE  . LYS A 132 ? 0.5825 0.7746 0.8354 -0.0176 0.0293  -0.0175 650 LYS A CE  
1119 N NZ  . LYS A 132 ? 0.6093 0.7854 0.8550 -0.0247 0.0504  -0.0094 650 LYS A NZ  
1120 N N   . LEU A 133 ? 0.5112 0.6749 0.7327 -0.0342 -0.0025 -0.0197 651 LEU A N   
1121 C CA  . LEU A 133 ? 0.5131 0.6696 0.7280 -0.0383 -0.0077 -0.0214 651 LEU A CA  
1122 C C   . LEU A 133 ? 0.5096 0.6393 0.7120 -0.0479 0.0089  -0.0110 651 LEU A C   
1123 O O   . LEU A 133 ? 0.5330 0.6552 0.7444 -0.0553 0.0278  -0.0095 651 LEU A O   
1124 C CB  . LEU A 133 ? 0.5103 0.6952 0.7586 -0.0437 -0.0129 -0.0436 651 LEU A CB  
1125 C CG  . LEU A 133 ? 0.4692 0.6841 0.7253 -0.0288 -0.0337 -0.0553 651 LEU A CG  
1126 C CD1 . LEU A 133 ? 0.4479 0.6973 0.7407 -0.0350 -0.0384 -0.0816 651 LEU A CD1 
1127 C CD2 . LEU A 133 ? 0.5703 0.7699 0.7899 -0.0147 -0.0492 -0.0437 651 LEU A CD2 
1128 N N   . LEU A 134 ? 0.4296 0.5436 0.6091 -0.0458 0.0026  -0.0035 652 LEU A N   
1129 C CA  . LEU A 134 ? 0.4107 0.5022 0.5803 -0.0527 0.0163  0.0033  652 LEU A CA  
1130 C C   . LEU A 134 ? 0.5301 0.6278 0.7252 -0.0644 0.0218  -0.0121 652 LEU A C   
1131 O O   . LEU A 134 ? 0.5752 0.6952 0.7861 -0.0643 0.0074  -0.0270 652 LEU A O   
1132 C CB  . LEU A 134 ? 0.4139 0.4901 0.5531 -0.0460 0.0075  0.0145  652 LEU A CB  
1133 C CG  . LEU A 134 ? 0.5188 0.5878 0.6334 -0.0370 0.0053  0.0270  652 LEU A CG  
1134 C CD1 . LEU A 134 ? 0.5073 0.5639 0.5988 -0.0336 0.0001  0.0337  652 LEU A CD1 
1135 C CD2 . LEU A 134 ? 0.5230 0.5837 0.6339 -0.0367 0.0217  0.0344  652 LEU A CD2 
1136 N N   . ASP A 135 ? 0.4745 0.5517 0.6719 -0.0734 0.0436  -0.0096 653 ASP A N   
1137 C CA  . ASP A 135 ? 0.4480 0.5261 0.6690 -0.0867 0.0526  -0.0254 653 ASP A CA  
1138 C C   . ASP A 135 ? 0.6264 0.6804 0.8232 -0.0850 0.0527  -0.0165 653 ASP A C   
1139 O O   . ASP A 135 ? 0.6751 0.6987 0.8527 -0.0839 0.0706  -0.0026 653 ASP A O   
1140 C CB  . ASP A 135 ? 0.4377 0.5047 0.6798 -0.0996 0.0820  -0.0307 653 ASP A CB  
1141 C CG  . ASP A 135 ? 0.7177 0.7954 0.9968 -0.1170 0.0918  -0.0555 653 ASP A CG  
1142 O OD1 . ASP A 135 ? 0.7596 0.8648 1.0529 -0.1174 0.0710  -0.0720 653 ASP A OD1 
1143 O OD2 . ASP A 135 ? 0.9392 0.9975 1.2326 -0.1302 0.1217  -0.0599 653 ASP A OD2 
1144 N N   . GLY A 136 ? 0.6216 0.6889 0.8165 -0.0823 0.0325  -0.0238 654 GLY A N   
1145 C CA  . GLY A 136 ? 0.6343 0.6822 0.8084 -0.0806 0.0310  -0.0175 654 GLY A CA  
1146 C C   . GLY A 136 ? 0.6609 0.7269 0.8300 -0.0747 0.0065  -0.0247 654 GLY A C   
1147 O O   . GLY A 136 ? 0.7151 0.7954 0.8763 -0.0647 -0.0093 -0.0218 654 GLY A O   
1148 N N   . PHE A 137 ? 0.5089 0.5715 0.6804 -0.0800 0.0052  -0.0339 655 PHE A N   
1149 C CA  . PHE A 137 ? 0.5313 0.6083 0.6942 -0.0732 -0.0162 -0.0409 655 PHE A CA  
1150 C C   . PHE A 137 ? 0.4154 0.4686 0.5489 -0.0686 -0.0169 -0.0277 655 PHE A C   
1151 O O   . PHE A 137 ? 0.4245 0.4586 0.5574 -0.0754 -0.0036 -0.0273 655 PHE A O   
1152 C CB  . PHE A 137 ? 0.6932 0.7937 0.8849 -0.0820 -0.0205 -0.0674 655 PHE A CB  
1153 C CG  . PHE A 137 ? 0.8397 0.9470 1.0680 -0.0979 -0.0014 -0.0829 655 PHE A CG  
1154 C CD1 . PHE A 137 ? 0.9098 1.0414 1.1615 -0.0985 -0.0019 -0.0910 655 PHE A CD1 
1155 C CD2 . PHE A 137 ? 0.8825 0.9698 1.1222 -0.1128 0.0195  -0.0901 655 PHE A CD2 
1156 C CE1 . PHE A 137 ? 0.9222 1.0597 1.2101 -0.1149 0.0189  -0.1070 655 PHE A CE1 
1157 C CE2 . PHE A 137 ? 0.8809 0.9700 1.1550 -0.1294 0.0420  -0.1055 655 PHE A CE2 
1158 C CZ  . PHE A 137 ? 0.9106 1.0256 1.2097 -0.1312 0.0420  -0.1145 655 PHE A CZ  
1159 N N   . PHE A 138 ? 0.3563 0.4092 0.4657 -0.0570 -0.0304 -0.0176 656 PHE A N   
1160 C CA  . PHE A 138 ? 0.3805 0.4146 0.4641 -0.0526 -0.0310 -0.0065 656 PHE A CA  
1161 C C   . PHE A 138 ? 0.4030 0.4422 0.4790 -0.0502 -0.0435 -0.0158 656 PHE A C   
1162 O O   . PHE A 138 ? 0.3571 0.4163 0.4418 -0.0473 -0.0554 -0.0285 656 PHE A O   
1163 C CB  . PHE A 138 ? 0.4501 0.4794 0.5133 -0.0437 -0.0340 0.0081  656 PHE A CB  
1164 C CG  . PHE A 138 ? 0.6292 0.6571 0.6974 -0.0438 -0.0239 0.0159  656 PHE A CG  
1165 C CD1 . PHE A 138 ? 0.6863 0.6997 0.7536 -0.0461 -0.0087 0.0223  656 PHE A CD1 
1166 C CD2 . PHE A 138 ? 0.7445 0.7832 0.8144 -0.0395 -0.0287 0.0175  656 PHE A CD2 
1167 C CE1 . PHE A 138 ? 0.6847 0.6956 0.7519 -0.0437 0.0012  0.0302  656 PHE A CE1 
1168 C CE2 . PHE A 138 ? 0.7919 0.8296 0.8649 -0.0392 -0.0192 0.0241  656 PHE A CE2 
1169 C CZ  . PHE A 138 ? 0.7688 0.7932 0.8396 -0.0410 -0.0046 0.0304  656 PHE A CZ  
1170 N N   . ILE A 139 ? 0.3600 0.3827 0.4184 -0.0492 -0.0413 -0.0100 657 ILE A N   
1171 C CA  . ILE A 139 ? 0.3791 0.4037 0.4254 -0.0457 -0.0521 -0.0171 657 ILE A CA  
1172 C C   . ILE A 139 ? 0.4355 0.4633 0.4615 -0.0339 -0.0634 -0.0112 657 ILE A C   
1173 O O   . ILE A 139 ? 0.3804 0.4033 0.3990 -0.0305 -0.0604 0.0001  657 ILE A O   
1174 C CB  . ILE A 139 ? 0.3594 0.3649 0.3916 -0.0471 -0.0455 -0.0120 657 ILE A CB  
1175 C CG1 . ILE A 139 ? 0.3469 0.3410 0.3615 -0.0415 -0.0411 0.0042  657 ILE A CG1 
1176 C CG2 . ILE A 139 ? 0.4022 0.3982 0.4508 -0.0569 -0.0314 -0.0171 657 ILE A CG2 
1177 C CD1 . ILE A 139 ? 0.3908 0.3708 0.3907 -0.0402 -0.0368 0.0080  657 ILE A CD1 
1178 N N   . ARG A 140 ? 0.3729 0.4073 0.3882 -0.0269 -0.0750 -0.0196 658 ARG A N   
1179 C CA  . ARG A 140 ? 0.3700 0.4024 0.3615 -0.0129 -0.0832 -0.0138 658 ARG A CA  
1180 C C   . ARG A 140 ? 0.3873 0.3963 0.3553 -0.0111 -0.0749 0.0016  658 ARG A C   
1181 O O   . ARG A 140 ? 0.4469 0.4502 0.4040 -0.0048 -0.0735 0.0094  658 ARG A O   
1182 C CB  . ARG A 140 ? 0.5205 0.5613 0.4990 -0.0031 -0.0957 -0.0251 658 ARG A CB  
1183 C CG  . ARG A 140 ? 0.7473 0.7904 0.7031 0.0158  -0.1054 -0.0224 658 ARG A CG  
1184 C CD  . ARG A 140 ? 0.7504 0.8106 0.6972 0.0277  -0.1201 -0.0378 658 ARG A CD  
1185 N NE  . ARG A 140 ? 0.8814 0.9531 0.8130 0.0494  -0.1317 -0.0388 658 ARG A NE  
1186 C CZ  . ARG A 140 ? 1.0370 1.0881 0.9264 0.0693  -0.1330 -0.0280 658 ARG A CZ  
1187 N NH1 . ARG A 140 ? 1.1278 1.1479 0.9901 0.0672  -0.1228 -0.0172 658 ARG A NH1 
1188 N NH2 . ARG A 140 ? 1.0073 1.0675 0.8809 0.0923  -0.1427 -0.0281 658 ARG A NH2 
1189 N N   . PRO A 141 ? 0.4195 0.4158 0.3813 -0.0170 -0.0680 0.0043  659 PRO A N   
1190 C CA  . PRO A 141 ? 0.4101 0.3913 0.3573 -0.0171 -0.0591 0.0149  659 PRO A CA  
1191 C C   . PRO A 141 ? 0.3536 0.3385 0.3117 -0.0203 -0.0527 0.0213  659 PRO A C   
1192 O O   . PRO A 141 ? 0.3968 0.3739 0.3446 -0.0195 -0.0468 0.0262  659 PRO A O   
1193 C CB  . PRO A 141 ? 0.4343 0.4088 0.3811 -0.0228 -0.0535 0.0140  659 PRO A CB  
1194 C CG  . PRO A 141 ? 0.4337 0.4115 0.3805 -0.0222 -0.0607 0.0039  659 PRO A CG  
1195 C CD  . PRO A 141 ? 0.4068 0.4020 0.3726 -0.0224 -0.0677 -0.0036 659 PRO A CD  
1196 N N   . PHE A 142 ? 0.4226 0.4188 0.4012 -0.0241 -0.0525 0.0199  660 PHE A N   
1197 C CA  . PHE A 142 ? 0.3256 0.3257 0.3115 -0.0253 -0.0470 0.0256  660 PHE A CA  
1198 C C   . PHE A 142 ? 0.3501 0.3502 0.3288 -0.0196 -0.0498 0.0273  660 PHE A C   
1199 O O   . PHE A 142 ? 0.3696 0.3648 0.3417 -0.0195 -0.0440 0.0313  660 PHE A O   
1200 C CB  . PHE A 142 ? 0.3336 0.3419 0.3397 -0.0296 -0.0437 0.0243  660 PHE A CB  
1201 C CG  . PHE A 142 ? 0.3410 0.3521 0.3509 -0.0291 -0.0368 0.0308  660 PHE A CG  
1202 C CD1 . PHE A 142 ? 0.3886 0.3961 0.3958 -0.0284 -0.0290 0.0358  660 PHE A CD1 
1203 C CD2 . PHE A 142 ? 0.4087 0.4268 0.4228 -0.0272 -0.0383 0.0316  660 PHE A CD2 
1204 C CE1 . PHE A 142 ? 0.3774 0.3898 0.3848 -0.0251 -0.0238 0.0408  660 PHE A CE1 
1205 C CE2 . PHE A 142 ? 0.4156 0.4374 0.4319 -0.0263 -0.0321 0.0364  660 PHE A CE2 
1206 C CZ  . PHE A 142 ? 0.4498 0.4697 0.4620 -0.0250 -0.0254 0.0406  660 PHE A CZ  
1207 N N   . TYR A 143 ? 0.3703 0.3766 0.3506 -0.0140 -0.0583 0.0226  661 TYR A N   
1208 C CA  . TYR A 143 ? 0.4230 0.4280 0.3948 -0.0050 -0.0608 0.0248  661 TYR A CA  
1209 C C   . TYR A 143 ? 0.4630 0.4463 0.4068 0.0009  -0.0560 0.0303  661 TYR A C   
1210 O O   . TYR A 143 ? 0.4241 0.3972 0.3599 0.0031  -0.0488 0.0349  661 TYR A O   
1211 C CB  . TYR A 143 ? 0.3608 0.3822 0.3404 0.0031  -0.0726 0.0166  661 TYR A CB  
1212 C CG  . TYR A 143 ? 0.3915 0.4337 0.4029 -0.0055 -0.0731 0.0087  661 TYR A CG  
1213 C CD1 . TYR A 143 ? 0.4743 0.5279 0.5012 -0.0116 -0.0764 -0.0026 661 TYR A CD1 
1214 C CD2 . TYR A 143 ? 0.4454 0.4936 0.4712 -0.0083 -0.0677 0.0117  661 TYR A CD2 
1215 C CE1 . TYR A 143 ? 0.5390 0.6074 0.5958 -0.0214 -0.0720 -0.0110 661 TYR A CE1 
1216 C CE2 . TYR A 143 ? 0.4334 0.4965 0.4868 -0.0168 -0.0642 0.0050  661 TYR A CE2 
1217 C CZ  . TYR A 143 ? 0.5031 0.5750 0.5723 -0.0237 -0.0652 -0.0063 661 TYR A CZ  
1218 O OH  . TYR A 143 ? 0.6207 0.7035 0.7181 -0.0338 -0.0571 -0.0142 661 TYR A OH  
1219 N N   . LYS A 144 ? 0.4545 0.4287 0.3833 0.0027  -0.0573 0.0289  662 LYS A N   
1220 C CA  . LYS A 144 ? 0.4308 0.3804 0.3319 0.0070  -0.0485 0.0340  662 LYS A CA  
1221 C C   . LYS A 144 ? 0.4013 0.3426 0.3055 -0.0038 -0.0342 0.0361  662 LYS A C   
1222 O O   . LYS A 144 ? 0.4718 0.3936 0.3601 -0.0021 -0.0227 0.0391  662 LYS A O   
1223 C CB  . LYS A 144 ? 0.5479 0.4906 0.4339 0.0095  -0.0515 0.0313  662 LYS A CB  
1224 C CG  . LYS A 144 ? 0.5211 0.4706 0.3955 0.0240  -0.0652 0.0268  662 LYS A CG  
1225 C CD  . LYS A 144 ? 0.5297 0.4684 0.3838 0.0269  -0.0655 0.0247  662 LYS A CD  
1226 C CE  . LYS A 144 ? 0.6799 0.6243 0.5145 0.0452  -0.0789 0.0194  662 LYS A CE  
1227 N NZ  . LYS A 144 ? 0.7090 0.6373 0.5178 0.0485  -0.0761 0.0189  662 LYS A NZ  
1228 N N   . MET A 145 ? 0.3910 0.3469 0.3147 -0.0138 -0.0336 0.0333  663 MET A N   
1229 C CA  . MET A 145 ? 0.3961 0.3532 0.3255 -0.0219 -0.0227 0.0316  663 MET A CA  
1230 C C   . MET A 145 ? 0.4163 0.3753 0.3512 -0.0223 -0.0181 0.0321  663 MET A C   
1231 O O   . MET A 145 ? 0.4348 0.3850 0.3654 -0.0268 -0.0062 0.0291  663 MET A O   
1232 C CB  . MET A 145 ? 0.4279 0.4026 0.3739 -0.0269 -0.0248 0.0291  663 MET A CB  
1233 C CG  . MET A 145 ? 0.4829 0.4534 0.4232 -0.0275 -0.0256 0.0275  663 MET A CG  
1234 S SD  . MET A 145 ? 0.5349 0.5205 0.4886 -0.0292 -0.0251 0.0258  663 MET A SD  
1235 C CE  . MET A 145 ? 0.4503 0.4461 0.4071 -0.0327 -0.0157 0.0189  663 MET A CE  
1236 N N   . MET A 146 ? 0.4111 0.3814 0.3569 -0.0187 -0.0261 0.0342  664 MET A N   
1237 C CA  . MET A 146 ? 0.4106 0.3824 0.3610 -0.0177 -0.0225 0.0349  664 MET A CA  
1238 C C   . MET A 146 ? 0.4649 0.4126 0.3951 -0.0123 -0.0141 0.0371  664 MET A C   
1239 O O   . MET A 146 ? 0.5517 0.4930 0.4823 -0.0156 -0.0036 0.0352  664 MET A O   
1240 C CB  . MET A 146 ? 0.4310 0.4168 0.3947 -0.0132 -0.0321 0.0364  664 MET A CB  
1241 C CG  . MET A 146 ? 0.3877 0.3913 0.3700 -0.0187 -0.0332 0.0355  664 MET A CG  
1242 S SD  . MET A 146 ? 0.4544 0.4718 0.4546 -0.0161 -0.0384 0.0355  664 MET A SD  
1243 C CE  . MET A 146 ? 0.6092 0.6308 0.6142 -0.0146 -0.0475 0.0310  664 MET A CE  
1244 N N   . LEU A 147 ? 0.4319 0.3647 0.3427 -0.0028 -0.0175 0.0407  665 LEU A N   
1245 C CA  . LEU A 147 ? 0.4871 0.3912 0.3711 0.0079  -0.0087 0.0457  665 LEU A CA  
1246 C C   . LEU A 147 ? 0.5989 0.4774 0.4640 0.0030  0.0073  0.0455  665 LEU A C   
1247 O O   . LEU A 147 ? 0.5845 0.4310 0.4213 0.0122  0.0192  0.0509  665 LEU A O   
1248 C CB  . LEU A 147 ? 0.4671 0.3708 0.3359 0.0258  -0.0219 0.0494  665 LEU A CB  
1249 C CG  . LEU A 147 ? 0.5287 0.4575 0.4162 0.0324  -0.0360 0.0473  665 LEU A CG  
1250 C CD1 . LEU A 147 ? 0.5104 0.4465 0.3855 0.0500  -0.0507 0.0459  665 LEU A CD1 
1251 C CD2 . LEU A 147 ? 0.5050 0.4233 0.3898 0.0372  -0.0274 0.0509  665 LEU A CD2 
1252 N N   . HIS A 148 ? 0.4730 0.3642 0.3524 -0.0102 0.0091  0.0392  666 HIS A N   
1253 C CA  . HIS A 148 ? 0.4846 0.3563 0.3512 -0.0166 0.0247  0.0363  666 HIS A CA  
1254 C C   . HIS A 148 ? 0.5406 0.3873 0.3749 -0.0033 0.0244  0.0437  666 HIS A C   
1255 O O   . HIS A 148 ? 0.6110 0.4242 0.4197 -0.0007 0.0425  0.0466  666 HIS A O   
1256 C CB  . HIS A 148 ? 0.5270 0.3795 0.3914 -0.0247 0.0472  0.0317  666 HIS A CB  
1257 C CG  . HIS A 148 ? 0.6632 0.5010 0.5233 -0.0360 0.0667  0.0241  666 HIS A CG  
1258 N ND1 . HIS A 148 ? 0.7464 0.6106 0.6286 -0.0477 0.0645  0.0134  666 HIS A ND1 
1259 C CD2 . HIS A 148 ? 0.7884 0.5868 0.6242 -0.0366 0.0905  0.0253  666 HIS A CD2 
1260 C CE1 . HIS A 148 ? 0.8064 0.6527 0.6822 -0.0565 0.0850  0.0064  666 HIS A CE1 
1261 N NE2 . HIS A 148 ? 0.8984 0.7026 0.7458 -0.0511 0.1026  0.0136  666 HIS A NE2 
1262 N N   . LYS A 149 ? 0.5227 0.3850 0.3573 0.0056  0.0050  0.0456  667 LYS A N   
1263 C CA  . LYS A 149 ? 0.5152 0.3619 0.3210 0.0187  0.0013  0.0494  667 LYS A CA  
1264 C C   . LYS A 149 ? 0.5388 0.3950 0.3521 0.0095  -0.0011 0.0441  667 LYS A C   
1265 O O   . LYS A 149 ? 0.5099 0.3917 0.3517 -0.0013 -0.0082 0.0386  667 LYS A O   
1266 C CB  . LYS A 149 ? 0.4889 0.3507 0.2912 0.0354  -0.0188 0.0506  667 LYS A CB  
1267 C CG  . LYS A 149 ? 0.6681 0.5143 0.4521 0.0515  -0.0156 0.0574  667 LYS A CG  
1268 C CD  . LYS A 149 ? 0.7699 0.6342 0.5481 0.0714  -0.0360 0.0560  667 LYS A CD  
1269 C CE  . LYS A 149 ? 0.8122 0.6609 0.5710 0.0904  -0.0323 0.0634  667 LYS A CE  
1270 N NZ  . LYS A 149 ? 0.9146 0.7143 0.6284 0.1025  -0.0111 0.0746  667 LYS A NZ  
1271 N N   . PRO A 150 ? 0.6569 0.4898 0.4413 0.0157  0.0063  0.0464  668 PRO A N   
1272 C CA  . PRO A 150 ? 0.6540 0.4924 0.4417 0.0086  0.0056  0.0414  668 PRO A CA  
1273 C C   . PRO A 150 ? 0.5953 0.4604 0.3969 0.0117  -0.0161 0.0369  668 PRO A C   
1274 O O   . PRO A 150 ? 0.5998 0.4695 0.3909 0.0254  -0.0291 0.0374  668 PRO A O   
1275 C CB  . PRO A 150 ? 0.6061 0.4092 0.3521 0.0194  0.0183  0.0467  668 PRO A CB  
1276 C CG  . PRO A 150 ? 0.7704 0.5453 0.4920 0.0304  0.0303  0.0551  668 PRO A CG  
1277 C CD  . PRO A 150 ? 0.6194 0.4180 0.3621 0.0336  0.0150  0.0550  668 PRO A CD  
1278 N N   . ILE A 151 ? 0.5561 0.4384 0.3809 -0.0001 -0.0186 0.0311  669 ILE A N   
1279 C CA  . ILE A 151 ? 0.4381 0.3387 0.2743 0.0006  -0.0337 0.0253  669 ILE A CA  
1280 C C   . ILE A 151 ? 0.5054 0.3934 0.3170 0.0070  -0.0343 0.0228  669 ILE A C   
1281 O O   . ILE A 151 ? 0.5148 0.3881 0.3160 0.0026  -0.0218 0.0236  669 ILE A O   
1282 C CB  . ILE A 151 ? 0.4559 0.3739 0.3217 -0.0117 -0.0335 0.0216  669 ILE A CB  
1283 C CG1 . ILE A 151 ? 0.5706 0.4993 0.4561 -0.0172 -0.0302 0.0241  669 ILE A CG1 
1284 C CG2 . ILE A 151 ? 0.4415 0.3735 0.3202 -0.0122 -0.0452 0.0150  669 ILE A CG2 
1285 C CD1 . ILE A 151 ? 0.5573 0.4928 0.4474 -0.0118 -0.0380 0.0261  669 ILE A CD1 
1286 N N   . THR A 152 ? 0.5933 0.4901 0.3973 0.0172  -0.0487 0.0177  670 THR A N   
1287 C CA  . THR A 152 ? 0.7179 0.6037 0.4943 0.0260  -0.0504 0.0145  670 THR A CA  
1288 C C   . THR A 152 ? 0.7057 0.6113 0.4998 0.0208  -0.0616 0.0018  670 THR A C   
1289 O O   . THR A 152 ? 0.6192 0.5457 0.4454 0.0119  -0.0681 -0.0043 670 THR A O   
1290 C CB  . THR A 152 ? 0.6541 0.5315 0.3962 0.0479  -0.0573 0.0170  670 THR A CB  
1291 O OG1 . THR A 152 ? 0.6306 0.5376 0.3915 0.0535  -0.0758 0.0084  670 THR A OG1 
1292 C CG2 . THR A 152 ? 0.7562 0.6053 0.4754 0.0545  -0.0418 0.0303  670 THR A CG2 
1293 N N   . LEU A 153 ? 0.6842 0.5804 0.4552 0.0265  -0.0617 -0.0024 671 LEU A N   
1294 C CA  . LEU A 153 ? 0.6452 0.5569 0.4284 0.0224  -0.0709 -0.0166 671 LEU A CA  
1295 C C   . LEU A 153 ? 0.6768 0.6172 0.4783 0.0261  -0.0882 -0.0296 671 LEU A C   
1296 O O   . LEU A 153 ? 0.6310 0.5886 0.4625 0.0145  -0.0919 -0.0419 671 LEU A O   
1297 C CB  . LEU A 153 ? 0.6305 0.5274 0.3785 0.0325  -0.0696 -0.0194 671 LEU A CB  
1298 C CG  . LEU A 153 ? 0.5253 0.4374 0.2842 0.0282  -0.0783 -0.0365 671 LEU A CG  
1299 C CD1 . LEU A 153 ? 0.5206 0.4349 0.3141 0.0088  -0.0697 -0.0379 671 LEU A CD1 
1300 C CD2 . LEU A 153 ? 0.6458 0.5411 0.3661 0.0390  -0.0756 -0.0382 671 LEU A CD2 
1301 N N   . HIS A 154 ? 0.6681 0.6131 0.4518 0.0428  -0.0969 -0.0276 672 HIS A N   
1302 C CA  . HIS A 154 ? 0.7590 0.7370 0.5615 0.0485  -0.1143 -0.0423 672 HIS A CA  
1303 C C   . HIS A 154 ? 0.7835 0.7778 0.6309 0.0312  -0.1122 -0.0448 672 HIS A C   
1304 O O   . HIS A 154 ? 0.8403 0.8622 0.7172 0.0250  -0.1209 -0.0623 672 HIS A O   
1305 C CB  . HIS A 154 ? 0.8935 0.8713 0.6662 0.0729  -0.1224 -0.0367 672 HIS A CB  
1306 C CG  . HIS A 154 ? 1.0668 1.0843 0.8548 0.0837  -0.1429 -0.0557 672 HIS A CG  
1307 N ND1 . HIS A 154 ? 1.1277 1.1548 0.9045 0.1037  -0.1516 -0.0525 672 HIS A ND1 
1308 C CD2 . HIS A 154 ? 1.1215 1.1738 0.9373 0.0774  -0.1555 -0.0805 672 HIS A CD2 
1309 C CE1 . HIS A 154 ? 1.1517 1.2219 0.9500 0.1100  -0.1705 -0.0752 672 HIS A CE1 
1310 N NE2 . HIS A 154 ? 1.1686 1.2552 0.9921 0.0930  -0.1726 -0.0937 672 HIS A NE2 
1311 N N   . ASP A 155 ? 0.7027 0.6801 0.5551 0.0231  -0.0993 -0.0288 673 ASP A N   
1312 C CA  . ASP A 155 ? 0.6551 0.6441 0.5439 0.0092  -0.0956 -0.0286 673 ASP A CA  
1313 C C   . ASP A 155 ? 0.6202 0.6139 0.5345 -0.0065 -0.0909 -0.0382 673 ASP A C   
1314 O O   . ASP A 155 ? 0.6262 0.6334 0.5711 -0.0164 -0.0896 -0.0449 673 ASP A O   
1315 C CB  . ASP A 155 ? 0.5931 0.5643 0.4787 0.0054  -0.0830 -0.0114 673 ASP A CB  
1316 C CG  . ASP A 155 ? 0.6866 0.6515 0.5527 0.0187  -0.0844 -0.0029 673 ASP A CG  
1317 O OD1 . ASP A 155 ? 0.7830 0.7661 0.6548 0.0278  -0.0959 -0.0091 673 ASP A OD1 
1318 O OD2 . ASP A 155 ? 0.6356 0.5772 0.4811 0.0205  -0.0729 0.0087  673 ASP A OD2 
1319 N N   . MET A 156 ? 0.6685 0.6481 0.5688 -0.0083 -0.0861 -0.0388 674 MET A N   
1320 C CA  . MET A 156 ? 0.5845 0.5631 0.5044 -0.0211 -0.0796 -0.0475 674 MET A CA  
1321 C C   . MET A 156 ? 0.6090 0.6102 0.5488 -0.0250 -0.0885 -0.0704 674 MET A C   
1322 O O   . MET A 156 ? 0.6609 0.6625 0.6257 -0.0383 -0.0804 -0.0796 674 MET A O   
1323 C CB  . MET A 156 ? 0.5756 0.5348 0.4740 -0.0202 -0.0729 -0.0437 674 MET A CB  
1324 C CG  . MET A 156 ? 0.5121 0.4661 0.4254 -0.0307 -0.0651 -0.0521 674 MET A CG  
1325 S SD  . MET A 156 ? 0.6764 0.6194 0.6096 -0.0391 -0.0496 -0.0390 674 MET A SD  
1326 C CE  . MET A 156 ? 0.6472 0.5759 0.5572 -0.0329 -0.0430 -0.0240 674 MET A CE  
1327 N N   . GLU A 157 ? 0.6183 0.6386 0.5472 -0.0126 -0.1040 -0.0811 675 GLU A N   
1328 C CA  . GLU A 157 ? 0.6320 0.6808 0.5819 -0.0159 -0.1138 -0.1082 675 GLU A CA  
1329 C C   . GLU A 157 ? 0.7250 0.7917 0.7169 -0.0294 -0.1098 -0.1179 675 GLU A C   
1330 O O   . GLU A 157 ? 0.6816 0.7539 0.7024 -0.0452 -0.1020 -0.1349 675 GLU A O   
1331 C CB  . GLU A 157 ? 0.5717 0.6430 0.4996 0.0049  -0.1335 -0.1188 675 GLU A CB  
1332 C CG  . GLU A 157 ? 0.6986 0.8056 0.6495 0.0017  -0.1450 -0.1520 675 GLU A CG  
1333 C CD  . GLU A 157 ? 0.7698 0.9041 0.6957 0.0268  -0.1670 -0.1651 675 GLU A CD  
1334 O OE1 . GLU A 157 ? 0.8686 0.9965 0.7641 0.0477  -0.1733 -0.1483 675 GLU A OE1 
1335 O OE2 . GLU A 157 ? 0.7878 0.9497 0.7230 0.0270  -0.1773 -0.1932 675 GLU A OE2 
1336 N N   . SER A 158 ? 0.7784 0.8509 0.7730 -0.0236 -0.1124 -0.1069 676 SER A N   
1337 C CA  . SER A 158 ? 0.7831 0.8728 0.8157 -0.0349 -0.1079 -0.1152 676 SER A CA  
1338 C C   . SER A 158 ? 0.6855 0.7522 0.7373 -0.0534 -0.0864 -0.1082 676 SER A C   
1339 O O   . SER A 158 ? 0.7295 0.8057 0.8140 -0.0662 -0.0776 -0.1192 676 SER A O   
1340 C CB  . SER A 158 ? 0.8644 0.9602 0.8913 -0.0236 -0.1136 -0.1017 676 SER A CB  
1341 O OG  . SER A 158 ? 0.9284 0.9941 0.9284 -0.0187 -0.1061 -0.0752 676 SER A OG  
1342 N N   . VAL A 159 ? 0.6316 0.6680 0.6624 -0.0535 -0.0766 -0.0906 677 VAL A N   
1343 C CA  . VAL A 159 ? 0.6683 0.6814 0.7102 -0.0647 -0.0567 -0.0805 677 VAL A CA  
1344 C C   . VAL A 159 ? 0.5843 0.5809 0.6293 -0.0737 -0.0453 -0.0891 677 VAL A C   
1345 O O   . VAL A 159 ? 0.5982 0.5829 0.6632 -0.0854 -0.0282 -0.0933 677 VAL A O   
1346 C CB  . VAL A 159 ? 0.6834 0.6770 0.7031 -0.0571 -0.0520 -0.0547 677 VAL A CB  
1347 C CG1 . VAL A 159 ? 0.7076 0.6791 0.7336 -0.0632 -0.0332 -0.0446 677 VAL A CG1 
1348 C CG2 . VAL A 159 ? 0.6602 0.6655 0.6784 -0.0501 -0.0593 -0.0460 677 VAL A CG2 
1349 N N   . ASP A 160 ? 0.6169 0.6090 0.6398 -0.0674 -0.0522 -0.0907 678 ASP A N   
1350 C CA  . ASP A 160 ? 0.5684 0.5448 0.5919 -0.0746 -0.0422 -0.0999 678 ASP A CA  
1351 C C   . ASP A 160 ? 0.7196 0.7105 0.7288 -0.0688 -0.0573 -0.1159 678 ASP A C   
1352 O O   . ASP A 160 ? 0.6493 0.6336 0.6283 -0.0569 -0.0645 -0.1047 678 ASP A O   
1353 C CB  . ASP A 160 ? 0.6402 0.5873 0.6453 -0.0705 -0.0299 -0.0788 678 ASP A CB  
1354 C CG  . ASP A 160 ? 0.7692 0.6969 0.7748 -0.0766 -0.0173 -0.0867 678 ASP A CG  
1355 O OD1 . ASP A 160 ? 0.7145 0.6502 0.7346 -0.0857 -0.0175 -0.1098 678 ASP A OD1 
1356 O OD2 . ASP A 160 ? 0.8310 0.7371 0.8228 -0.0713 -0.0073 -0.0713 678 ASP A OD2 
1357 N N   . SER A 161 ? 0.7947 0.8058 0.8259 -0.0773 -0.0607 -0.1435 679 SER A N   
1358 C CA  . SER A 161 ? 0.8317 0.8641 0.8511 -0.0701 -0.0774 -0.1636 679 SER A CA  
1359 C C   . SER A 161 ? 0.8057 0.8172 0.8060 -0.0705 -0.0715 -0.1649 679 SER A C   
1360 O O   . SER A 161 ? 0.6414 0.6581 0.6130 -0.0576 -0.0843 -0.1671 679 SER A O   
1361 C CB  . SER A 161 ? 0.8508 0.9180 0.9059 -0.0804 -0.0827 -0.1979 679 SER A CB  
1362 O OG  . SER A 161 ? 0.9373 0.9895 1.0216 -0.1012 -0.0611 -0.2106 679 SER A OG  
1363 N N   . GLU A 162 ? 0.9459 0.9318 0.9597 -0.0837 -0.0509 -0.1635 680 GLU A N   
1364 C CA  . GLU A 162 ? 1.0267 0.9902 1.0236 -0.0838 -0.0430 -0.1634 680 GLU A CA  
1365 C C   . GLU A 162 ? 0.9427 0.8901 0.9038 -0.0691 -0.0462 -0.1378 680 GLU A C   
1366 O O   . GLU A 162 ? 0.9431 0.8885 0.8797 -0.0614 -0.0524 -0.1409 680 GLU A O   
1367 C CB  . GLU A 162 ? 1.1065 1.0405 1.1216 -0.0973 -0.0178 -0.1623 680 GLU A CB  
1368 C CG  . GLU A 162 ? 1.1707 1.1106 1.2153 -0.1144 -0.0085 -0.1942 680 GLU A CG  
1369 C CD  . GLU A 162 ? 1.2019 1.1020 1.2545 -0.1245 0.0201  -0.1906 680 GLU A CD  
1370 O OE1 . GLU A 162 ? 1.1917 1.0639 1.2308 -0.1170 0.0319  -0.1627 680 GLU A OE1 
1371 O OE2 . GLU A 162 ? 1.2491 1.1459 1.3205 -0.1387 0.0313  -0.2168 680 GLU A OE2 
1372 N N   . TYR A 163 ? 0.8447 0.7814 0.8042 -0.0658 -0.0405 -0.1144 681 TYR A N   
1373 C CA  . TYR A 163 ? 0.7426 0.6676 0.6749 -0.0545 -0.0412 -0.0928 681 TYR A CA  
1374 C C   . TYR A 163 ? 0.7667 0.7051 0.6743 -0.0424 -0.0574 -0.0929 681 TYR A C   
1375 O O   . TYR A 163 ? 0.7560 0.6839 0.6363 -0.0346 -0.0577 -0.0876 681 TYR A O   
1376 C CB  . TYR A 163 ? 0.7190 0.6379 0.6585 -0.0536 -0.0342 -0.0729 681 TYR A CB  
1377 C CG  . TYR A 163 ? 0.7054 0.6082 0.6301 -0.0475 -0.0255 -0.0556 681 TYR A CG  
1378 C CD1 . TYR A 163 ? 0.7438 0.6369 0.6504 -0.0439 -0.0232 -0.0571 681 TYR A CD1 
1379 C CD2 . TYR A 163 ? 0.7294 0.6301 0.6595 -0.0449 -0.0198 -0.0399 681 TYR A CD2 
1380 C CE1 . TYR A 163 ? 0.7727 0.6564 0.6703 -0.0386 -0.0151 -0.0446 681 TYR A CE1 
1381 C CE2 . TYR A 163 ? 0.8311 0.7247 0.7515 -0.0386 -0.0131 -0.0283 681 TYR A CE2 
1382 C CZ  . TYR A 163 ? 0.8444 0.7305 0.7502 -0.0359 -0.0107 -0.0312 681 TYR A CZ  
1383 O OH  . TYR A 163 ? 0.9430 0.8273 0.8436 -0.0298 -0.0039 -0.0227 681 TYR A OH  
1384 N N   . TYR A 164 ? 0.6034 0.5631 0.5193 -0.0397 -0.0692 -0.0985 682 TYR A N   
1385 C CA  . TYR A 164 ? 0.5660 0.5366 0.4553 -0.0243 -0.0840 -0.0978 682 TYR A CA  
1386 C C   . TYR A 164 ? 0.6270 0.5994 0.4927 -0.0168 -0.0910 -0.1117 682 TYR A C   
1387 O O   . TYR A 164 ? 0.5646 0.5253 0.3941 -0.0031 -0.0930 -0.1019 682 TYR A O   
1388 C CB  . TYR A 164 ? 0.5995 0.5982 0.5056 -0.0215 -0.0967 -0.1079 682 TYR A CB  
1389 C CG  . TYR A 164 ? 0.5464 0.5590 0.4230 -0.0013 -0.1136 -0.1113 682 TYR A CG  
1390 C CD1 . TYR A 164 ? 0.4580 0.4551 0.3045 0.0126  -0.1132 -0.0903 682 TYR A CD1 
1391 C CD2 . TYR A 164 ? 0.6241 0.6650 0.5017 0.0053  -0.1289 -0.1367 682 TYR A CD2 
1392 C CE1 . TYR A 164 ? 0.5263 0.5298 0.3400 0.0347  -0.1258 -0.0908 682 TYR A CE1 
1393 C CE2 . TYR A 164 ? 0.6728 0.7266 0.5181 0.0291  -0.1450 -0.1390 682 TYR A CE2 
1394 C CZ  . TYR A 164 ? 0.5912 0.6233 0.4024 0.0448  -0.1425 -0.1141 682 TYR A CZ  
1395 O OH  . TYR A 164 ? 0.7237 0.7623 0.4972 0.0716  -0.1557 -0.1139 682 TYR A OH  
1396 N N   . ASN A 165 ? 0.5476 0.5331 0.4333 -0.0260 -0.0926 -0.1355 683 ASN A N   
1397 C CA  . ASN A 165 ? 0.5763 0.5693 0.4421 -0.0189 -0.1011 -0.1535 683 ASN A CA  
1398 C C   . ASN A 165 ? 0.5416 0.5049 0.3815 -0.0174 -0.0895 -0.1422 683 ASN A C   
1399 O O   . ASN A 165 ? 0.6884 0.6497 0.4955 -0.0050 -0.0955 -0.1465 683 ASN A O   
1400 C CB  . ASN A 165 ? 0.6825 0.6974 0.5817 -0.0327 -0.1029 -0.1854 683 ASN A CB  
1401 C CG  . ASN A 165 ? 0.7729 0.8278 0.6941 -0.0304 -0.1188 -0.2055 683 ASN A CG  
1402 O OD1 . ASN A 165 ? 0.8299 0.8992 0.7304 -0.0120 -0.1338 -0.1990 683 ASN A OD1 
1403 N ND2 . ASN A 165 ? 0.6879 0.7604 0.6517 -0.0488 -0.1140 -0.2310 683 ASN A ND2 
1404 N N   . SER A 166 ? 0.6155 0.5570 0.4694 -0.0285 -0.0726 -0.1287 684 SER A N   
1405 C CA  . SER A 166 ? 0.6912 0.6075 0.5260 -0.0275 -0.0603 -0.1185 684 SER A CA  
1406 C C   . SER A 166 ? 0.5783 0.4818 0.3809 -0.0152 -0.0589 -0.0983 684 SER A C   
1407 O O   . SER A 166 ? 0.6053 0.4963 0.3788 -0.0079 -0.0558 -0.0973 684 SER A O   
1408 C CB  . SER A 166 ? 0.7233 0.6233 0.5820 -0.0391 -0.0434 -0.1103 684 SER A CB  
1409 O OG  . SER A 166 ? 0.7957 0.6985 0.6805 -0.0510 -0.0389 -0.1288 684 SER A OG  
1410 N N   . LEU A 167 ? 0.5224 0.4271 0.3307 -0.0140 -0.0585 -0.0830 685 LEU A N   
1411 C CA  . LEU A 167 ? 0.5031 0.3946 0.2839 -0.0043 -0.0544 -0.0660 685 LEU A CA  
1412 C C   . LEU A 167 ? 0.5738 0.4664 0.3185 0.0122  -0.0648 -0.0693 685 LEU A C   
1413 O O   . LEU A 167 ? 0.6768 0.5494 0.3879 0.0214  -0.0570 -0.0592 685 LEU A O   
1414 C CB  . LEU A 167 ? 0.4680 0.3628 0.2646 -0.0070 -0.0523 -0.0525 685 LEU A CB  
1415 C CG  . LEU A 167 ? 0.6857 0.5791 0.5120 -0.0188 -0.0419 -0.0474 685 LEU A CG  
1416 C CD1 . LEU A 167 ? 0.5370 0.4370 0.3782 -0.0204 -0.0417 -0.0364 685 LEU A CD1 
1417 C CD2 . LEU A 167 ? 0.6670 0.5453 0.4846 -0.0197 -0.0284 -0.0420 685 LEU A CD2 
1418 N N   . ARG A 168 ? 0.5280 0.4440 0.2788 0.0172  -0.0812 -0.0842 686 ARG A N   
1419 C CA  . ARG A 168 ? 0.6586 0.5796 0.3720 0.0380  -0.0935 -0.0888 686 ARG A CA  
1420 C C   . ARG A 168 ? 0.6862 0.5984 0.3715 0.0442  -0.0924 -0.0984 686 ARG A C   
1421 O O   . ARG A 168 ? 0.6353 0.5310 0.2752 0.0622  -0.0910 -0.0907 686 ARG A O   
1422 C CB  . ARG A 168 ? 0.7101 0.6667 0.4410 0.0433  -0.1134 -0.1065 686 ARG A CB  
1423 C CG  . ARG A 168 ? 0.9456 0.9098 0.6352 0.0708  -0.1276 -0.1080 686 ARG A CG  
1424 C CD  . ARG A 168 ? 1.0532 1.0597 0.7658 0.0766  -0.1482 -0.1279 686 ARG A CD  
1425 N NE  . ARG A 168 ? 1.1293 1.1636 0.8797 0.0602  -0.1541 -0.1566 686 ARG A NE  
1426 C CZ  . ARG A 168 ? 1.1197 1.1964 0.9005 0.0591  -0.1698 -0.1825 686 ARG A CZ  
1427 N NH1 . ARG A 168 ? 1.1375 1.2369 0.9146 0.0762  -0.1840 -0.1827 686 ARG A NH1 
1428 N NH2 . ARG A 168 ? 1.0645 1.1610 0.8808 0.0408  -0.1699 -0.2098 686 ARG A NH2 
1429 N N   . TRP A 169 ? 0.5843 0.5042 0.2940 0.0301  -0.0911 -0.1147 687 TRP A N   
1430 C CA  . TRP A 169 ? 0.6565 0.5659 0.3412 0.0342  -0.0877 -0.1237 687 TRP A CA  
1431 C C   . TRP A 169 ? 0.6218 0.4967 0.2780 0.0371  -0.0692 -0.1027 687 TRP A C   
1432 O O   . TRP A 169 ? 0.8290 0.6891 0.4434 0.0509  -0.0664 -0.1012 687 TRP A O   
1433 C CB  . TRP A 169 ? 0.6010 0.5169 0.3192 0.0160  -0.0837 -0.1421 687 TRP A CB  
1434 C CG  . TRP A 169 ? 0.7006 0.6084 0.3934 0.0207  -0.0817 -0.1544 687 TRP A CG  
1435 C CD1 . TRP A 169 ? 0.7226 0.6521 0.4068 0.0272  -0.0957 -0.1806 687 TRP A CD1 
1436 C CD2 . TRP A 169 ? 0.6407 0.5196 0.3144 0.0196  -0.0647 -0.1430 687 TRP A CD2 
1437 N NE1 . TRP A 169 ? 0.7173 0.6303 0.3758 0.0304  -0.0882 -0.1848 687 TRP A NE1 
1438 C CE2 . TRP A 169 ? 0.7331 0.6141 0.3849 0.0257  -0.0687 -0.1614 687 TRP A CE2 
1439 C CE3 . TRP A 169 ? 0.6580 0.5129 0.3329 0.0143  -0.0467 -0.1214 687 TRP A CE3 
1440 C CZ2 . TRP A 169 ? 0.7789 0.6356 0.4087 0.0265  -0.0541 -0.1569 687 TRP A CZ2 
1441 C CZ3 . TRP A 169 ? 0.6420 0.4763 0.2982 0.0148  -0.0327 -0.1186 687 TRP A CZ3 
1442 C CH2 . TRP A 169 ? 0.6748 0.5084 0.3082 0.0207  -0.0359 -0.1354 687 TRP A CH2 
1443 N N   . ILE A 170 ? 0.6134 0.4772 0.2932 0.0240  -0.0555 -0.0881 688 ILE A N   
1444 C CA  . ILE A 170 ? 0.6382 0.4755 0.3005 0.0237  -0.0366 -0.0718 688 ILE A CA  
1445 C C   . ILE A 170 ? 0.7106 0.5305 0.3308 0.0401  -0.0331 -0.0586 688 ILE A C   
1446 O O   . ILE A 170 ? 0.6561 0.4516 0.2427 0.0466  -0.0192 -0.0524 688 ILE A O   
1447 C CB  . ILE A 170 ? 0.6059 0.4431 0.3035 0.0094  -0.0261 -0.0613 688 ILE A CB  
1448 C CG1 . ILE A 170 ? 0.5455 0.3887 0.2742 -0.0028 -0.0232 -0.0709 688 ILE A CG1 
1449 C CG2 . ILE A 170 ? 0.6202 0.4369 0.3030 0.0095  -0.0075 -0.0472 688 ILE A CG2 
1450 C CD1 . ILE A 170 ? 0.5816 0.4278 0.3423 -0.0122 -0.0153 -0.0617 688 ILE A CD1 
1451 N N   . LEU A 171 ? 0.6230 0.4532 0.2433 0.0476  -0.0439 -0.0545 689 LEU A N   
1452 C CA  . LEU A 171 ? 0.7862 0.5956 0.3655 0.0649  -0.0385 -0.0403 689 LEU A CA  
1453 C C   . LEU A 171 ? 0.8205 0.6207 0.3485 0.0875  -0.0439 -0.0452 689 LEU A C   
1454 O O   . LEU A 171 ? 0.9023 0.6704 0.3857 0.1011  -0.0291 -0.0319 689 LEU A O   
1455 C CB  . LEU A 171 ? 0.7020 0.5263 0.2938 0.0698  -0.0501 -0.0360 689 LEU A CB  
1456 C CG  . LEU A 171 ? 0.8602 0.6616 0.4101 0.0898  -0.0444 -0.0207 689 LEU A CG  
1457 C CD1 . LEU A 171 ? 0.9358 0.7030 0.4778 0.0811  -0.0170 -0.0044 689 LEU A CD1 
1458 C CD2 . LEU A 171 ? 0.7802 0.6026 0.3466 0.0956  -0.0594 -0.0201 689 LEU A CD2 
1459 N N   . GLU A 172 ? 0.7090 0.5365 0.2424 0.0919  -0.0634 -0.0654 690 GLU A N   
1460 C CA  . GLU A 172 ? 0.7684 0.5964 0.2528 0.1179  -0.0742 -0.0729 690 GLU A CA  
1461 C C   . GLU A 172 ? 0.8433 0.6575 0.3046 0.1183  -0.0661 -0.0803 690 GLU A C   
1462 O O   . GLU A 172 ? 0.9810 0.7890 0.3997 0.1400  -0.0684 -0.0812 690 GLU A O   
1463 C CB  . GLU A 172 ? 0.8209 0.6939 0.3240 0.1253  -0.1024 -0.0952 690 GLU A CB  
1464 C CG  . GLU A 172 ? 0.8994 0.7876 0.4241 0.1267  -0.1108 -0.0888 690 GLU A CG  
1465 C CD  . GLU A 172 ? 0.9516 0.8890 0.5011 0.1324  -0.1374 -0.1137 690 GLU A CD  
1466 O OE1 . GLU A 172 ? 0.9657 0.9282 0.5291 0.1290  -0.1467 -0.1365 690 GLU A OE1 
1467 O OE2 . GLU A 172 ? 0.9768 0.9299 0.5421 0.1371  -0.1453 -0.1098 690 GLU A OE2 
1468 N N   . ASN A 173 ? 0.8077 0.6198 0.3039 0.0944  -0.0550 -0.0841 691 ASN A N   
1469 C CA  . ASN A 173 ? 0.7756 0.5756 0.2549 0.0928  -0.0464 -0.0924 691 ASN A CA  
1470 C C   . ASN A 173 ? 0.8336 0.6041 0.3189 0.0786  -0.0194 -0.0769 691 ASN A C   
1471 O O   . ASN A 173 ? 0.8156 0.5852 0.3317 0.0654  -0.0117 -0.0659 691 ASN A O   
1472 C CB  . ASN A 173 ? 0.7899 0.6188 0.3076 0.0786  -0.0587 -0.1176 691 ASN A CB  
1473 C CG  . ASN A 173 ? 0.8023 0.6694 0.3298 0.0868  -0.0849 -0.1387 691 ASN A CG  
1474 O OD1 . ASN A 173 ? 0.7807 0.6694 0.3479 0.0768  -0.0934 -0.1420 691 ASN A OD1 
1475 N ND2 . ASN A 173 ? 0.7968 0.6752 0.2899 0.1052  -0.0975 -0.1553 691 ASN A ND2 
1476 N N   . ASP A 174 ? 0.8119 0.5615 0.2698 0.0813  -0.0054 -0.0779 692 ASP A N   
1477 C CA  . ASP A 174 ? 0.7832 0.5115 0.2529 0.0667  0.0200  -0.0681 692 ASP A CA  
1478 C C   . ASP A 174 ? 0.8957 0.6445 0.4195 0.0463  0.0173  -0.0786 692 ASP A C   
1479 O O   . ASP A 174 ? 0.8341 0.5920 0.3632 0.0442  0.0108  -0.0944 692 ASP A O   
1480 C CB  . ASP A 174 ? 0.8302 0.5303 0.2546 0.0761  0.0373  -0.0672 692 ASP A CB  
1481 C CG  . ASP A 174 ? 0.9092 0.5877 0.3441 0.0623  0.0664  -0.0576 692 ASP A CG  
1482 O OD1 . ASP A 174 ? 0.8789 0.5708 0.3614 0.0449  0.0703  -0.0558 692 ASP A OD1 
1483 O OD2 . ASP A 174 ? 0.9864 0.6359 0.3816 0.0698  0.0863  -0.0532 692 ASP A OD2 
1484 N N   . PRO A 175 ? 0.7001 0.4544 0.2618 0.0326  0.0237  -0.0700 693 PRO A N   
1485 C CA  . PRO A 175 ? 0.7131 0.4848 0.3219 0.0177  0.0210  -0.0777 693 PRO A CA  
1486 C C   . PRO A 175 ? 0.7178 0.4803 0.3369 0.0102  0.0391  -0.0783 693 PRO A C   
1487 O O   . PRO A 175 ? 0.7086 0.4817 0.3622 0.0013  0.0393  -0.0829 693 PRO A O   
1488 C CB  . PRO A 175 ? 0.6271 0.4104 0.2666 0.0108  0.0183  -0.0675 693 PRO A CB  
1489 C CG  . PRO A 175 ? 0.6431 0.4093 0.2565 0.0170  0.0295  -0.0533 693 PRO A CG  
1490 C CD  . PRO A 175 ? 0.6928 0.4365 0.2545 0.0312  0.0354  -0.0537 693 PRO A CD  
1491 N N   . THR A 176 ? 0.6888 0.4307 0.2775 0.0148  0.0558  -0.0735 694 THR A N   
1492 C CA  . THR A 176 ? 0.7668 0.5025 0.3676 0.0076  0.0758  -0.0737 694 THR A CA  
1493 C C   . THR A 176 ? 0.7368 0.4802 0.3578 0.0034  0.0742  -0.0860 694 THR A C   
1494 O O   . THR A 176 ? 0.7174 0.4696 0.3703 -0.0033 0.0822  -0.0860 694 THR A O   
1495 C CB  . THR A 176 ? 0.8089 0.5175 0.3670 0.0142  0.0952  -0.0699 694 THR A CB  
1496 O OG1 . THR A 176 ? 0.7971 0.4922 0.3354 0.0182  0.1018  -0.0574 694 THR A OG1 
1497 C CG2 . THR A 176 ? 0.7556 0.4616 0.3302 0.0056  0.1172  -0.0728 694 THR A CG2 
1498 N N   . GLU A 177 ? 0.6999 0.4410 0.3025 0.0086  0.0639  -0.0977 695 GLU A N   
1499 C CA  . GLU A 177 ? 0.7014 0.4438 0.3177 0.0048  0.0655  -0.1108 695 GLU A CA  
1500 C C   . GLU A 177 ? 0.6832 0.4400 0.3414 -0.0031 0.0575  -0.1146 695 GLU A C   
1501 O O   . GLU A 177 ? 0.7151 0.4692 0.3893 -0.0063 0.0636  -0.1223 695 GLU A O   
1502 C CB  . GLU A 177 ? 0.7375 0.4745 0.3212 0.0122  0.0572  -0.1253 695 GLU A CB  
1503 C CG  . GLU A 177 ? 0.8804 0.5979 0.4158 0.0231  0.0678  -0.1213 695 GLU A CG  
1504 C CD  . GLU A 177 ? 0.9692 0.6840 0.4714 0.0326  0.0594  -0.1376 695 GLU A CD  
1505 O OE1 . GLU A 177 ? 0.9717 0.6734 0.4597 0.0333  0.0725  -0.1436 695 GLU A OE1 
1506 O OE2 . GLU A 177 ? 1.0010 0.7295 0.4922 0.0397  0.0394  -0.1461 695 GLU A OE2 
1507 N N   . LEU A 178 ? 0.6480 0.4169 0.3213 -0.0052 0.0458  -0.1089 696 LEU A N   
1508 C CA  . LEU A 178 ? 0.6216 0.4001 0.3320 -0.0121 0.0417  -0.1100 696 LEU A CA  
1509 C C   . LEU A 178 ? 0.6352 0.4153 0.3682 -0.0131 0.0540  -0.0992 696 LEU A C   
1510 O O   . LEU A 178 ? 0.6973 0.4794 0.4558 -0.0150 0.0558  -0.0989 696 LEU A O   
1511 C CB  . LEU A 178 ? 0.6248 0.4166 0.3448 -0.0138 0.0270  -0.1070 696 LEU A CB  
1512 C CG  . LEU A 178 ? 0.8363 0.6371 0.5555 -0.0154 0.0124  -0.1237 696 LEU A CG  
1513 C CD1 . LEU A 178 ? 0.9373 0.7350 0.6202 -0.0073 0.0076  -0.1353 696 LEU A CD1 
1514 C CD2 . LEU A 178 ? 0.8045 0.6203 0.5314 -0.0149 -0.0005 -0.1181 696 LEU A CD2 
1515 N N   . ASP A 179 ? 0.6462 0.4256 0.3692 -0.0108 0.0635  -0.0913 697 ASP A N   
1516 C CA  . ASP A 179 ? 0.6222 0.4103 0.3680 -0.0106 0.0747  -0.0856 697 ASP A CA  
1517 C C   . ASP A 179 ? 0.6050 0.4083 0.3782 -0.0115 0.0675  -0.0774 697 ASP A C   
1518 O O   . ASP A 179 ? 0.5832 0.3942 0.3787 -0.0080 0.0713  -0.0756 697 ASP A O   
1519 C CB  . ASP A 179 ? 0.7727 0.5554 0.5261 -0.0077 0.0840  -0.0932 697 ASP A CB  
1520 C CG  . ASP A 179 ? 0.8137 0.6087 0.5849 -0.0042 0.0964  -0.0908 697 ASP A CG  
1521 O OD1 . ASP A 179 ? 0.7750 0.5816 0.5501 -0.0065 0.1005  -0.0863 697 ASP A OD1 
1522 O OD2 . ASP A 179 ? 0.8684 0.6622 0.6502 0.0013  0.1030  -0.0952 697 ASP A OD2 
1523 N N   . LEU A 180 ? 0.5847 0.3915 0.3534 -0.0140 0.0572  -0.0723 698 LEU A N   
1524 C CA  . LEU A 180 ? 0.6253 0.4463 0.4167 -0.0149 0.0515  -0.0640 698 LEU A CA  
1525 C C   . LEU A 180 ? 0.5355 0.3700 0.3384 -0.0144 0.0605  -0.0591 698 LEU A C   
1526 O O   . LEU A 180 ? 0.5473 0.3776 0.3367 -0.0163 0.0702  -0.0607 698 LEU A O   
1527 C CB  . LEU A 180 ? 0.5137 0.3358 0.2971 -0.0172 0.0389  -0.0609 698 LEU A CB  
1528 C CG  . LEU A 180 ? 0.5628 0.3786 0.3361 -0.0181 0.0289  -0.0707 698 LEU A CG  
1529 C CD1 . LEU A 180 ? 0.5257 0.3485 0.2928 -0.0178 0.0157  -0.0686 698 LEU A CD1 
1530 C CD2 . LEU A 180 ? 0.5625 0.3772 0.3586 -0.0209 0.0300  -0.0759 698 LEU A CD2 
1531 N N   . ARG A 181 ? 0.4882 0.3393 0.3155 -0.0118 0.0583  -0.0545 699 ARG A N   
1532 C CA  . ARG A 181 ? 0.4704 0.3424 0.3140 -0.0112 0.0648  -0.0540 699 ARG A CA  
1533 C C   . ARG A 181 ? 0.5074 0.3906 0.3598 -0.0140 0.0571  -0.0473 699 ARG A C   
1534 O O   . ARG A 181 ? 0.4423 0.3189 0.2922 -0.0145 0.0466  -0.0420 699 ARG A O   
1535 C CB  . ARG A 181 ? 0.4595 0.3476 0.3234 -0.0012 0.0685  -0.0565 699 ARG A CB  
1536 C CG  . ARG A 181 ? 0.4793 0.3553 0.3362 0.0034  0.0763  -0.0628 699 ARG A CG  
1537 C CD  . ARG A 181 ? 0.4927 0.3669 0.3398 -0.0024 0.0884  -0.0708 699 ARG A CD  
1538 N NE  . ARG A 181 ? 0.5144 0.3731 0.3504 0.0011  0.0952  -0.0768 699 ARG A NE  
1539 C CZ  . ARG A 181 ? 0.6469 0.5170 0.4958 0.0092  0.1037  -0.0830 699 ARG A CZ  
1540 N NH1 . ARG A 181 ? 0.6200 0.5207 0.4937 0.0159  0.1050  -0.0851 699 ARG A NH1 
1541 N NH2 . ARG A 181 ? 0.6110 0.4644 0.4483 0.0119  0.1104  -0.0885 699 ARG A NH2 
1542 N N   . PHE A 182 ? 0.4451 0.3467 0.3103 -0.0166 0.0632  -0.0495 700 PHE A N   
1543 C CA  . PHE A 182 ? 0.4327 0.3456 0.3072 -0.0193 0.0569  -0.0444 700 PHE A CA  
1544 C C   . PHE A 182 ? 0.4764 0.4087 0.3710 -0.0100 0.0487  -0.0412 700 PHE A C   
1545 O O   . PHE A 182 ? 0.4410 0.4002 0.3545 -0.0065 0.0496  -0.0450 700 PHE A O   
1546 C CB  . PHE A 182 ? 0.4164 0.3407 0.2979 -0.0271 0.0686  -0.0506 700 PHE A CB  
1547 C CG  . PHE A 182 ? 0.4378 0.3348 0.2928 -0.0346 0.0767  -0.0478 700 PHE A CG  
1548 C CD1 . PHE A 182 ? 0.4637 0.3366 0.2931 -0.0337 0.0824  -0.0481 700 PHE A CD1 
1549 C CD2 . PHE A 182 ? 0.4363 0.3298 0.2887 -0.0403 0.0791  -0.0443 700 PHE A CD2 
1550 C CE1 . PHE A 182 ? 0.5293 0.3745 0.3274 -0.0360 0.0905  -0.0440 700 PHE A CE1 
1551 C CE2 . PHE A 182 ? 0.4635 0.3270 0.2858 -0.0431 0.0884  -0.0397 700 PHE A CE2 
1552 C CZ  . PHE A 182 ? 0.4921 0.3313 0.2856 -0.0397 0.0940  -0.0391 700 PHE A CZ  
1553 N N   . ILE A 183 ? 0.4043 0.3222 0.2935 -0.0054 0.0419  -0.0354 701 ILE A N   
1554 C CA  . ILE A 183 ? 0.4888 0.4148 0.3897 0.0049  0.0374  -0.0297 701 ILE A CA  
1555 C C   . ILE A 183 ? 0.5115 0.4201 0.4067 0.0007  0.0304  -0.0230 701 ILE A C   
1556 O O   . ILE A 183 ? 0.4984 0.3918 0.3817 -0.0077 0.0279  -0.0252 701 ILE A O   
1557 C CB  . ILE A 183 ? 0.4410 0.3631 0.3431 0.0173  0.0431  -0.0310 701 ILE A CB  
1558 C CG1 . ILE A 183 ? 0.4293 0.3223 0.3170 0.0121  0.0459  -0.0332 701 ILE A CG1 
1559 C CG2 . ILE A 183 ? 0.4763 0.4213 0.3878 0.0230  0.0496  -0.0401 701 ILE A CG2 
1560 C CD1 . ILE A 183 ? 0.7374 0.6204 0.6245 0.0238  0.0539  -0.0345 701 ILE A CD1 
1561 N N   . ILE A 184 ? 0.4489 0.3612 0.3523 0.0076  0.0278  -0.0159 702 ILE A N   
1562 C CA  . ILE A 184 ? 0.4631 0.3583 0.3649 0.0030  0.0247  -0.0116 702 ILE A CA  
1563 C C   . ILE A 184 ? 0.5312 0.4133 0.4347 0.0142  0.0322  -0.0064 702 ILE A C   
1564 O O   . ILE A 184 ? 0.4546 0.3483 0.3611 0.0286  0.0345  -0.0008 702 ILE A O   
1565 C CB  . ILE A 184 ? 0.5894 0.4953 0.4968 -0.0014 0.0172  -0.0067 702 ILE A CB  
1566 C CG1 . ILE A 184 ? 0.7927 0.6969 0.6924 -0.0125 0.0113  -0.0107 702 ILE A CG1 
1567 C CG2 . ILE A 184 ? 0.7728 0.6665 0.6847 -0.0012 0.0178  -0.0013 702 ILE A CG2 
1568 C CD1 . ILE A 184 ? 0.9018 0.8121 0.8060 -0.0166 0.0041  -0.0063 702 ILE A CD1 
1569 N N   . ASP A 185 ? 0.5123 0.3701 0.4128 0.0087  0.0371  -0.0094 703 ASP A N   
1570 C CA  . ASP A 185 ? 0.6733 0.5092 0.5731 0.0178  0.0492  -0.0040 703 ASP A CA  
1571 C C   . ASP A 185 ? 0.7590 0.5846 0.6651 0.0107  0.0507  -0.0005 703 ASP A C   
1572 O O   . ASP A 185 ? 0.8616 0.6837 0.7732 -0.0047 0.0468  -0.0093 703 ASP A O   
1573 C CB  . ASP A 185 ? 0.7064 0.5183 0.6010 0.0154  0.0590  -0.0121 703 ASP A CB  
1574 C CG  . ASP A 185 ? 0.8839 0.7021 0.7722 0.0268  0.0620  -0.0138 703 ASP A CG  
1575 O OD1 . ASP A 185 ? 1.0841 0.8947 0.9678 0.0198  0.0636  -0.0238 703 ASP A OD1 
1576 O OD2 . ASP A 185 ? 0.8953 0.7286 0.7838 0.0435  0.0626  -0.0068 703 ASP A OD2 
1577 N N   . GLU A 186 ? 0.7525 0.5754 0.6575 0.0233  0.0565  0.0114  704 GLU A N   
1578 C CA  . GLU A 186 ? 0.7436 0.5531 0.6539 0.0180  0.0623  0.0158  704 GLU A CA  
1579 C C   . GLU A 186 ? 0.7187 0.4918 0.6213 0.0277  0.0839  0.0225  704 GLU A C   
1580 O O   . GLU A 186 ? 0.7159 0.4822 0.6050 0.0490  0.0912  0.0323  704 GLU A O   
1581 C CB  . GLU A 186 ? 0.7337 0.5654 0.6454 0.0246  0.0540  0.0249  704 GLU A CB  
1582 C CG  . GLU A 186 ? 0.8349 0.6548 0.7523 0.0189  0.0602  0.0295  704 GLU A CG  
1583 C CD  . GLU A 186 ? 0.8576 0.6986 0.7739 0.0279  0.0530  0.0388  704 GLU A CD  
1584 O OE1 . GLU A 186 ? 0.7951 0.6557 0.7044 0.0433  0.0472  0.0428  704 GLU A OE1 
1585 O OE2 . GLU A 186 ? 0.8396 0.6798 0.7636 0.0193  0.0533  0.0402  704 GLU A OE2 
1586 N N   . GLU A 187 ? 0.7926 0.5420 0.7038 0.0127  0.0955  0.0161  705 GLU A N   
1587 C CA  . GLU A 187 ? 0.7835 0.4910 0.6874 0.0191  0.1213  0.0219  705 GLU A CA  
1588 C C   . GLU A 187 ? 0.7580 0.4567 0.6559 0.0292  0.1303  0.0371  705 GLU A C   
1589 O O   . GLU A 187 ? 0.7029 0.4128 0.6147 0.0152  0.1254  0.0335  705 GLU A O   
1590 C CB  . GLU A 187 ? 0.9097 0.5958 0.8292 -0.0042 0.1334  0.0040  705 GLU A CB  
1591 C CG  . GLU A 187 ? 1.0092 0.6861 0.9271 -0.0084 0.1358  -0.0087 705 GLU A CG  
1592 C CD  . GLU A 187 ? 1.2383 0.8679 1.1448 0.0008  0.1647  -0.0041 705 GLU A CD  
1593 O OE1 . GLU A 187 ? 1.3100 0.9083 1.2246 -0.0105 0.1871  -0.0088 705 GLU A OE1 
1594 O OE2 . GLU A 187 ? 1.3425 0.9654 1.2321 0.0197  0.1668  0.0037  705 GLU A OE2 
1595 N N   . LEU A 188 ? 0.8134 0.4924 0.6888 0.0555  0.1433  0.0538  706 LEU A N   
1596 C CA  . LEU A 188 ? 0.7826 0.4496 0.6456 0.0696  0.1537  0.0698  706 LEU A CA  
1597 C C   . LEU A 188 ? 0.7755 0.3975 0.6102 0.0955  0.1802  0.0856  706 LEU A C   
1598 O O   . LEU A 188 ? 0.7704 0.3912 0.5898 0.1162  0.1798  0.0898  706 LEU A O   
1599 C CB  . LEU A 188 ? 0.6853 0.3962 0.5446 0.0835  0.1309  0.0768  706 LEU A CB  
1600 C CG  . LEU A 188 ? 0.9026 0.6466 0.7838 0.0617  0.1122  0.0678  706 LEU A CG  
1601 C CD1 . LEU A 188 ? 0.9453 0.7294 0.8227 0.0753  0.0931  0.0731  706 LEU A CD1 
1602 C CD2 . LEU A 188 ? 0.8914 0.6123 0.7813 0.0471  0.1274  0.0681  706 LEU A CD2 
1603 N N   . PHE A 189 ? 0.7552 0.3392 0.5824 0.0952  0.2049  0.0942  707 PHE A N   
1604 C CA  . PHE A 189 ? 0.8034 0.3351 0.5976 0.1220  0.2355  0.1124  707 PHE A CA  
1605 C C   . PHE A 189 ? 0.8953 0.3931 0.6808 0.1272  0.2520  0.1093  707 PHE A C   
1606 O O   . PHE A 189 ? 1.0477 0.5355 0.8053 0.1564  0.2616  0.1215  707 PHE A O   
1607 C CB  . PHE A 189 ? 0.8406 0.3905 0.6049 0.1606  0.2256  0.1317  707 PHE A CB  
1608 C CG  . PHE A 189 ? 0.8935 0.4730 0.6631 0.1576  0.2120  0.1352  707 PHE A CG  
1609 C CD1 . PHE A 189 ? 0.9824 0.5355 0.7435 0.1563  0.2332  0.1432  707 PHE A CD1 
1610 C CD2 . PHE A 189 ? 0.9152 0.5556 0.7022 0.1525  0.1781  0.1265  707 PHE A CD2 
1611 C CE1 . PHE A 189 ? 0.9294 0.5052 0.6937 0.1549  0.2222  0.1475  707 PHE A CE1 
1612 C CE2 . PHE A 189 ? 0.9061 0.5724 0.6985 0.1492  0.1666  0.1287  707 PHE A CE2 
1613 C CZ  . PHE A 189 ? 0.9301 0.5633 0.7102 0.1515  0.1882  0.1402  707 PHE A CZ  
1614 N N   . GLY A 190 ? 0.9233 0.4230 0.7364 0.0962  0.2503  0.0878  708 GLY A N   
1615 C CA  . GLY A 190 ? 0.8644 0.3312 0.6724 0.0969  0.2675  0.0817  708 GLY A CA  
1616 C C   . GLY A 190 ? 0.7988 0.2959 0.5986 0.1157  0.2459  0.0823  708 GLY A C   
1617 O O   . GLY A 190 ? 0.8500 0.3193 0.6357 0.1290  0.2600  0.0838  708 GLY A O   
1618 N N   . GLN A 191 ? 0.8174 0.3720 0.6271 0.1163  0.2130  0.0800  709 GLN A N   
1619 C CA  . GLN A 191 ? 0.8171 0.4075 0.6254 0.1294  0.1923  0.0765  709 GLN A CA  
1620 C C   . GLN A 191 ? 0.7756 0.4163 0.6104 0.1044  0.1633  0.0602  709 GLN A C   
1621 O O   . GLN A 191 ? 0.7308 0.3844 0.5817 0.0834  0.1555  0.0547  709 GLN A O   
1622 C CB  . GLN A 191 ? 0.8391 0.4484 0.6240 0.1681  0.1853  0.0934  709 GLN A CB  
1623 C CG  . GLN A 191 ? 0.8439 0.4028 0.5941 0.2007  0.2136  0.1132  709 GLN A CG  
1624 C CD  . GLN A 191 ? 0.9307 0.4529 0.6686 0.2115  0.2322  0.1125  709 GLN A CD  
1625 O OE1 . GLN A 191 ? 0.9460 0.4963 0.6909 0.2157  0.2177  0.1033  709 GLN A OE1 
1626 N NE2 . GLN A 191 ? 0.9408 0.4168 0.6654 0.2085  0.2621  0.1179  709 GLN A NE2 
1627 N N   . THR A 192 ? 0.7758 0.4427 0.6134 0.1083  0.1492  0.0527  710 THR A N   
1628 C CA  . THR A 192 ? 0.7592 0.4683 0.6157 0.0885  0.1253  0.0389  710 THR A CA  
1629 C C   . THR A 192 ? 0.7001 0.4539 0.5560 0.1048  0.1070  0.0432  710 THR A C   
1630 O O   . THR A 192 ? 0.7482 0.5121 0.5948 0.1280  0.1071  0.0464  710 THR A O   
1631 C CB  . THR A 192 ? 0.8207 0.5262 0.6818 0.0775  0.1251  0.0245  710 THR A CB  
1632 O OG1 . THR A 192 ? 0.7986 0.4699 0.6655 0.0577  0.1396  0.0150  710 THR A OG1 
1633 C CG2 . THR A 192 ? 0.8612 0.6072 0.7346 0.0627  0.1027  0.0130  710 THR A CG2 
1634 N N   . HIS A 193 ? 0.6400 0.4220 0.5072 0.0930  0.0920  0.0416  711 HIS A N   
1635 C CA  . HIS A 193 ? 0.6195 0.4456 0.4902 0.1043  0.0759  0.0416  711 HIS A CA  
1636 C C   . HIS A 193 ? 0.4980 0.3514 0.3829 0.0859  0.0624  0.0275  711 HIS A C   
1637 O O   . HIS A 193 ? 0.6015 0.4544 0.4948 0.0638  0.0566  0.0220  711 HIS A O   
1638 C CB  . HIS A 193 ? 0.6677 0.5065 0.5397 0.1053  0.0702  0.0489  711 HIS A CB  
1639 C CG  . HIS A 193 ? 0.8049 0.6172 0.6582 0.1267  0.0847  0.0644  711 HIS A CG  
1640 N ND1 . HIS A 193 ? 0.9843 0.7478 0.8267 0.1270  0.1062  0.0707  711 HIS A ND1 
1641 C CD2 . HIS A 193 ? 0.9444 0.7702 0.7860 0.1487  0.0826  0.0746  711 HIS A CD2 
1642 C CE1 . HIS A 193 ? 1.0642 0.8077 0.8864 0.1493  0.1190  0.0862  711 HIS A CE1 
1643 N NE2 . HIS A 193 ? 1.0109 0.7928 0.8310 0.1640  0.1036  0.0892  711 HIS A NE2 
1644 N N   . GLN A 194 ? 0.5021 0.3793 0.3889 0.0964  0.0584  0.0215  712 GLN A N   
1645 C CA  . GLN A 194 ? 0.4550 0.3542 0.3529 0.0796  0.0497  0.0087  712 GLN A CA  
1646 C C   . GLN A 194 ? 0.4622 0.4030 0.3716 0.0812  0.0389  0.0044  712 GLN A C   
1647 O O   . GLN A 194 ? 0.4757 0.4405 0.3865 0.1015  0.0369  0.0052  712 GLN A O   
1648 C CB  . GLN A 194 ? 0.4804 0.3778 0.3764 0.0854  0.0555  0.0013  712 GLN A CB  
1649 C CG  . GLN A 194 ? 0.6727 0.5883 0.5767 0.0699  0.0509  -0.0115 712 GLN A CG  
1650 C CD  . GLN A 194 ? 0.8158 0.7221 0.7158 0.0737  0.0590  -0.0184 712 GLN A CD  
1651 O OE1 . GLN A 194 ? 0.7836 0.6570 0.6739 0.0717  0.0668  -0.0168 712 GLN A OE1 
1652 N NE2 . GLN A 194 ? 0.8630 0.7991 0.7726 0.0785  0.0586  -0.0281 712 GLN A NE2 
1653 N N   A HIS A 195 ? 0.4328 0.3819 0.3496 0.0607  0.0325  -0.0012 713 HIS A N   
1654 N N   B HIS A 195 ? 0.4399 0.3889 0.3566 0.0606  0.0326  -0.0014 713 HIS A N   
1655 C CA  A HIS A 195 ? 0.4828 0.4676 0.4120 0.0582  0.0255  -0.0080 713 HIS A CA  
1656 C CA  B HIS A 195 ? 0.4848 0.4690 0.4139 0.0576  0.0255  -0.0080 713 HIS A CA  
1657 C C   A HIS A 195 ? 0.4786 0.4695 0.4130 0.0410  0.0269  -0.0195 713 HIS A C   
1658 C C   B HIS A 195 ? 0.4790 0.4696 0.4133 0.0408  0.0270  -0.0196 713 HIS A C   
1659 O O   A HIS A 195 ? 0.4665 0.4340 0.3924 0.0264  0.0276  -0.0184 713 HIS A O   
1660 O O   B HIS A 195 ? 0.4682 0.4356 0.3940 0.0262  0.0278  -0.0187 713 HIS A O   
1661 C CB  A HIS A 195 ? 0.4641 0.4496 0.3946 0.0519  0.0195  -0.0014 713 HIS A CB  
1662 C CB  B HIS A 195 ? 0.4603 0.4433 0.3903 0.0505  0.0198  -0.0013 713 HIS A CB  
1663 C CG  A HIS A 195 ? 0.5355 0.5185 0.4598 0.0701  0.0200  0.0095  713 HIS A CG  
1664 C CG  B HIS A 195 ? 0.4598 0.4743 0.4024 0.0443  0.0143  -0.0092 713 HIS A CG  
1665 N ND1 A HIS A 195 ? 0.5269 0.4763 0.4411 0.0697  0.0257  0.0207  713 HIS A ND1 
1666 N ND1 B HIS A 195 ? 0.4417 0.4919 0.3942 0.0583  0.0110  -0.0152 713 HIS A ND1 
1667 C CD2 A HIS A 195 ? 0.5419 0.5517 0.4671 0.0903  0.0167  0.0102  713 HIS A CD2 
1668 C CD2 B HIS A 195 ? 0.4436 0.4582 0.3898 0.0263  0.0127  -0.0133 713 HIS A CD2 
1669 C CE1 A HIS A 195 ? 0.4312 0.3813 0.3375 0.0889  0.0281  0.0302  713 HIS A CE1 
1670 C CE1 B HIS A 195 ? 0.3823 0.4539 0.3472 0.0461  0.0086  -0.0245 713 HIS A CE1 
1671 N NE2 A HIS A 195 ? 0.5588 0.5463 0.4699 0.1032  0.0213  0.0245  713 HIS A NE2 
1672 N NE2 B HIS A 195 ? 0.3181 0.3656 0.2780 0.0271  0.0107  -0.0221 713 HIS A NE2 
1673 N N   . GLU A 196 ? 0.3605 0.3831 0.3081 0.0437  0.0284  -0.0316 714 GLU A N   
1674 C CA  . GLU A 196 ? 0.4755 0.5010 0.4273 0.0272  0.0345  -0.0427 714 GLU A CA  
1675 C C   . GLU A 196 ? 0.4698 0.4940 0.4225 0.0116  0.0328  -0.0423 714 GLU A C   
1676 O O   . GLU A 196 ? 0.4684 0.5125 0.4309 0.0144  0.0274  -0.0423 714 GLU A O   
1677 C CB  . GLU A 196 ? 0.3978 0.4597 0.3682 0.0333  0.0396  -0.0589 714 GLU A CB  
1678 C CG  . GLU A 196 ? 0.5006 0.6050 0.4917 0.0370  0.0351  -0.0691 714 GLU A CG  
1679 C CD  . GLU A 196 ? 0.5501 0.6970 0.5652 0.0405  0.0406  -0.0909 714 GLU A CD  
1680 O OE1 . GLU A 196 ? 0.3945 0.5349 0.4093 0.0387  0.0493  -0.0966 714 GLU A OE1 
1681 O OE2 . GLU A 196 ? 0.5646 0.7538 0.6003 0.0447  0.0366  -0.1043 714 GLU A OE2 
1682 N N   . LEU A 197 ? 0.4450 0.4444 0.3847 -0.0027 0.0374  -0.0414 715 LEU A N   
1683 C CA  . LEU A 197 ? 0.3476 0.3393 0.2829 -0.0146 0.0370  -0.0389 715 LEU A CA  
1684 C C   . LEU A 197 ? 0.4061 0.4168 0.3549 -0.0237 0.0475  -0.0517 715 LEU A C   
1685 O O   . LEU A 197 ? 0.4529 0.4628 0.4029 -0.0318 0.0491  -0.0516 715 LEU A O   
1686 C CB  . LEU A 197 ? 0.4224 0.3798 0.3339 -0.0219 0.0377  -0.0327 715 LEU A CB  
1687 C CG  . LEU A 197 ? 0.4729 0.4137 0.3753 -0.0177 0.0272  -0.0234 715 LEU A CG  
1688 C CD1 . LEU A 197 ? 0.4576 0.3727 0.3375 -0.0228 0.0268  -0.0224 715 LEU A CD1 
1689 C CD2 . LEU A 197 ? 0.4480 0.3967 0.3584 -0.0170 0.0190  -0.0169 715 LEU A CD2 
1690 N N   . LYS A 198 ? 0.4104 0.4373 0.3705 -0.0231 0.0567  -0.0643 716 LYS A N   
1691 C CA  . LYS A 198 ? 0.5435 0.5952 0.5241 -0.0326 0.0691  -0.0817 716 LYS A CA  
1692 C C   . LYS A 198 ? 0.5826 0.6658 0.5826 -0.0244 0.0723  -0.0962 716 LYS A C   
1693 O O   . LYS A 198 ? 0.4913 0.5660 0.4821 -0.0129 0.0679  -0.0901 716 LYS A O   
1694 C CB  . LYS A 198 ? 0.5665 0.5878 0.5320 -0.0489 0.0864  -0.0830 716 LYS A CB  
1695 C CG  . LYS A 198 ? 0.5040 0.5009 0.4511 -0.0489 0.0950  -0.0814 716 LYS A CG  
1696 C CD  . LYS A 198 ? 0.5940 0.5521 0.5149 -0.0602 0.1112  -0.0774 716 LYS A CD  
1697 C CE  . LYS A 198 ? 0.6424 0.6087 0.5796 -0.0748 0.1321  -0.0917 716 LYS A CE  
1698 N NZ  . LYS A 198 ? 0.6657 0.5871 0.5720 -0.0832 0.1537  -0.0869 716 LYS A NZ  
1699 N N   . ASN A 199 ? 0.5698 0.6907 0.5981 -0.0299 0.0805  -0.1172 717 ASN A N   
1700 C CA  . ASN A 199 ? 0.4955 0.6565 0.5477 -0.0206 0.0826  -0.1352 717 ASN A CA  
1701 C C   . ASN A 199 ? 0.5069 0.6457 0.5471 -0.0211 0.0927  -0.1339 717 ASN A C   
1702 O O   . ASN A 199 ? 0.5653 0.6724 0.5919 -0.0370 0.1083  -0.1330 717 ASN A O   
1703 C CB  . ASN A 199 ? 0.6029 0.8057 0.6899 -0.0331 0.0946  -0.1630 717 ASN A CB  
1704 C CG  . ASN A 199 ? 0.7433 0.9994 0.8604 -0.0207 0.0937  -0.1855 717 ASN A CG  
1705 O OD1 . ASN A 199 ? 0.7021 0.9779 0.8175 0.0040  0.0772  -0.1801 717 ASN A OD1 
1706 N ND2 . ASN A 199 ? 0.8239 1.1021 0.9678 -0.0368 0.1132  -0.2113 717 ASN A ND2 
1707 N N   . GLY A 200 ? 0.5157 0.6688 0.5580 -0.0018 0.0846  -0.1332 718 GLY A N   
1708 C CA  . GLY A 200 ? 0.4889 0.6190 0.5178 0.0001  0.0924  -0.1305 718 GLY A CA  
1709 C C   . GLY A 200 ? 0.4967 0.5719 0.4896 -0.0041 0.0904  -0.1092 718 GLY A C   
1710 O O   . GLY A 200 ? 0.5425 0.5920 0.5198 -0.0085 0.0999  -0.1082 718 GLY A O   
1711 N N   . GLY A 201 ? 0.4172 0.4770 0.3976 -0.0023 0.0779  -0.0941 719 GLY A N   
1712 C CA  . GLY A 201 ? 0.4078 0.4233 0.3588 -0.0070 0.0745  -0.0779 719 GLY A CA  
1713 C C   . GLY A 201 ? 0.5157 0.5093 0.4515 0.0009  0.0744  -0.0732 719 GLY A C   
1714 O O   . GLY A 201 ? 0.4476 0.4093 0.3609 -0.0062 0.0774  -0.0684 719 GLY A O   
1715 N N   . SER A 202 ? 0.5346 0.5455 0.4812 0.0173  0.0716  -0.0754 720 SER A N   
1716 C CA  . SER A 202 ? 0.4961 0.4842 0.4291 0.0259  0.0731  -0.0712 720 SER A CA  
1717 C C   . SER A 202 ? 0.5119 0.4874 0.4367 0.0177  0.0857  -0.0796 720 SER A C   
1718 O O   . SER A 202 ? 0.5204 0.4678 0.4274 0.0184  0.0872  -0.0760 720 SER A O   
1719 C CB  . SER A 202 ? 0.4785 0.4873 0.4230 0.0485  0.0704  -0.0718 720 SER A CB  
1720 O OG  . SER A 202 ? 0.6171 0.6673 0.5846 0.0537  0.0748  -0.0876 720 SER A OG  
1721 N N   . GLU A 203 ? 0.4914 0.4870 0.4294 0.0091  0.0963  -0.0924 721 GLU A N   
1722 C CA  . GLU A 203 ? 0.4835 0.4688 0.4148 0.0026  0.1116  -0.1014 721 GLU A CA  
1723 C C   . GLU A 203 ? 0.5173 0.4742 0.4269 -0.0146 0.1216  -0.0994 721 GLU A C   
1724 O O   . GLU A 203 ? 0.6531 0.6011 0.5561 -0.0216 0.1380  -0.1073 721 GLU A O   
1725 C CB  . GLU A 203 ? 0.5960 0.6229 0.5582 0.0056  0.1215  -0.1200 721 GLU A CB  
1726 C CG  . GLU A 203 ? 0.7468 0.8070 0.7287 0.0281  0.1112  -0.1228 721 GLU A CG  
1727 C CD  . GLU A 203 ? 0.9743 1.0105 0.9394 0.0432  0.1088  -0.1141 721 GLU A CD  
1728 O OE1 . GLU A 203 ? 1.0223 1.0292 0.9698 0.0359  0.1180  -0.1141 721 GLU A OE1 
1729 O OE2 . GLU A 203 ? 1.0736 1.1182 1.0413 0.0634  0.0992  -0.1076 721 GLU A OE2 
1730 N N   . ILE A 204 ? 0.5395 0.4811 0.4360 -0.0194 0.1128  -0.0885 722 ILE A N   
1731 C CA  . ILE A 204 ? 0.5530 0.4678 0.4260 -0.0314 0.1218  -0.0849 722 ILE A CA  
1732 C C   . ILE A 204 ? 0.5014 0.3832 0.3417 -0.0283 0.1115  -0.0734 722 ILE A C   
1733 O O   . ILE A 204 ? 0.4945 0.3764 0.3355 -0.0239 0.0952  -0.0656 722 ILE A O   
1734 C CB  . ILE A 204 ? 0.6006 0.5269 0.4853 -0.0387 0.1211  -0.0838 722 ILE A CB  
1735 C CG1 . ILE A 204 ? 0.4488 0.4154 0.3707 -0.0421 0.1302  -0.1002 722 ILE A CG1 
1736 C CG2 . ILE A 204 ? 0.6037 0.4963 0.4592 -0.0479 0.1327  -0.0780 722 ILE A CG2 
1737 C CD1 . ILE A 204 ? 0.4803 0.4606 0.4162 -0.0496 0.1296  -0.1018 722 ILE A CD1 
1738 N N   . VAL A 205 ? 0.5216 0.3771 0.3338 -0.0301 0.1216  -0.0743 723 VAL A N   
1739 C CA  . VAL A 205 ? 0.5850 0.4152 0.3669 -0.0255 0.1111  -0.0683 723 VAL A CA  
1740 C C   . VAL A 205 ? 0.6376 0.4506 0.3953 -0.0268 0.1065  -0.0595 723 VAL A C   
1741 O O   . VAL A 205 ? 0.5643 0.3655 0.3095 -0.0314 0.1214  -0.0579 723 VAL A O   
1742 C CB  . VAL A 205 ? 0.6966 0.5072 0.4546 -0.0238 0.1228  -0.0740 723 VAL A CB  
1743 C CG1 . VAL A 205 ? 0.6318 0.4212 0.3586 -0.0184 0.1106  -0.0715 723 VAL A CG1 
1744 C CG2 . VAL A 205 ? 0.5958 0.4230 0.3774 -0.0206 0.1277  -0.0830 723 VAL A CG2 
1745 N N   . VAL A 206 ? 0.5427 0.3533 0.2941 -0.0225 0.0877  -0.0547 724 VAL A N   
1746 C CA  . VAL A 206 ? 0.6698 0.4666 0.3966 -0.0201 0.0808  -0.0473 724 VAL A CA  
1747 C C   . VAL A 206 ? 0.7637 0.5337 0.4468 -0.0135 0.0861  -0.0478 724 VAL A C   
1748 O O   . VAL A 206 ? 0.6084 0.3749 0.2818 -0.0097 0.0812  -0.0545 724 VAL A O   
1749 C CB  . VAL A 206 ? 0.6110 0.4185 0.3484 -0.0176 0.0593  -0.0453 724 VAL A CB  
1750 C CG1 . VAL A 206 ? 0.5479 0.3460 0.2623 -0.0130 0.0515  -0.0389 724 VAL A CG1 
1751 C CG2 . VAL A 206 ? 0.5001 0.3309 0.2758 -0.0214 0.0553  -0.0435 724 VAL A CG2 
1752 N N   . THR A 207 ? 0.7193 0.4688 0.3746 -0.0112 0.0980  -0.0410 725 THR A N   
1753 C CA  . THR A 207 ? 0.6696 0.3895 0.2753 -0.0009 0.1056  -0.0388 725 THR A CA  
1754 C C   . THR A 207 ? 0.6914 0.3941 0.2663 0.0088  0.1031  -0.0280 725 THR A C   
1755 O O   . THR A 207 ? 0.6935 0.4078 0.2883 0.0054  0.0960  -0.0233 725 THR A O   
1756 C CB  . THR A 207 ? 0.7043 0.4041 0.2967 -0.0053 0.1348  -0.0404 725 THR A CB  
1757 O OG1 . THR A 207 ? 0.8063 0.4940 0.3992 -0.0115 0.1540  -0.0343 725 THR A OG1 
1758 C CG2 . THR A 207 ? 0.6995 0.4204 0.3291 -0.0151 0.1404  -0.0512 725 THR A CG2 
1759 N N   . ASN A 208 ? 0.7412 0.4144 0.2646 0.0226  0.1108  -0.0236 726 ASN A N   
1760 C CA  . ASN A 208 ? 0.8312 0.4838 0.3183 0.0367  0.1104  -0.0118 726 ASN A CA  
1761 C C   . ASN A 208 ? 0.8052 0.4384 0.2963 0.0281  0.1357  -0.0030 726 ASN A C   
1762 O O   . ASN A 208 ? 0.8577 0.4813 0.3365 0.0351  0.1337  0.0064  726 ASN A O   
1763 C CB  . ASN A 208 ? 0.8588 0.4818 0.2827 0.0584  0.1141  -0.0085 726 ASN A CB  
1764 C CG  . ASN A 208 ? 0.8749 0.5206 0.2889 0.0725  0.0826  -0.0176 726 ASN A CG  
1765 O OD1 . ASN A 208 ? 0.8517 0.5294 0.3008 0.0679  0.0596  -0.0235 726 ASN A OD1 
1766 N ND2 . ASN A 208 ? 0.9764 0.6068 0.3435 0.0895  0.0826  -0.0207 726 ASN A ND2 
1767 N N   . LYS A 209 ? 0.8242 0.4530 0.3343 0.0126  0.1603  -0.0079 727 LYS A N   
1768 C CA  . LYS A 209 ? 0.8343 0.4476 0.3542 0.0007  0.1876  -0.0048 727 LYS A CA  
1769 C C   . LYS A 209 ? 0.8608 0.5078 0.4321 -0.0122 0.1759  -0.0082 727 LYS A C   
1770 O O   . LYS A 209 ? 0.7372 0.3723 0.3116 -0.0178 0.1908  -0.0043 727 LYS A O   
1771 C CB  . LYS A 209 ? 0.8933 0.4980 0.4234 -0.0133 0.2180  -0.0137 727 LYS A CB  
1772 C CG  . LYS A 209 ? 1.0389 0.5991 0.5149 -0.0026 0.2409  -0.0082 727 LYS A CG  
1773 C CD  . LYS A 209 ? 1.0851 0.6511 0.5856 -0.0174 0.2624  -0.0208 727 LYS A CD  
1774 C CE  . LYS A 209 ? 1.2486 0.7783 0.7138 -0.0073 0.2777  -0.0145 727 LYS A CE  
1775 N NZ  . LYS A 209 ? 1.2811 0.8192 0.7720 -0.0219 0.2972  -0.0276 727 LYS A NZ  
1776 N N   . ASN A 210 ? 0.7396 0.4262 0.3495 -0.0163 0.1515  -0.0155 728 ASN A N   
1777 C CA  . ASN A 210 ? 0.6332 0.3511 0.2879 -0.0260 0.1410  -0.0182 728 ASN A CA  
1778 C C   . ASN A 210 ? 0.6043 0.3437 0.2695 -0.0187 0.1097  -0.0148 728 ASN A C   
1779 O O   . ASN A 210 ? 0.6070 0.3721 0.3076 -0.0254 0.1003  -0.0164 728 ASN A O   
1780 C CB  . ASN A 210 ? 0.6957 0.4446 0.3958 -0.0395 0.1466  -0.0314 728 ASN A CB  
1781 C CG  . ASN A 210 ? 0.6629 0.4272 0.3706 -0.0351 0.1327  -0.0369 728 ASN A CG  
1782 O OD1 . ASN A 210 ? 0.6543 0.4163 0.3466 -0.0256 0.1135  -0.0332 728 ASN A OD1 
1783 N ND2 . ASN A 210 ? 0.6011 0.3820 0.3339 -0.0422 0.1436  -0.0478 728 ASN A ND2 
1784 N N   . LYS A 211 ? 0.6663 0.3969 0.3019 -0.0051 0.0943  -0.0116 729 LYS A N   
1785 C CA  . LYS A 211 ? 0.6879 0.4428 0.3406 -0.0013 0.0669  -0.0130 729 LYS A CA  
1786 C C   . LYS A 211 ? 0.6245 0.3834 0.2818 0.0011  0.0589  -0.0056 729 LYS A C   
1787 O O   . LYS A 211 ? 0.6001 0.3837 0.2868 -0.0022 0.0424  -0.0076 729 LYS A O   
1788 C CB  . LYS A 211 ? 0.6478 0.3989 0.2725 0.0116  0.0519  -0.0170 729 LYS A CB  
1789 C CG  . LYS A 211 ? 0.7123 0.4380 0.2856 0.0296  0.0530  -0.0100 729 LYS A CG  
1790 C CD  . LYS A 211 ? 0.7411 0.4733 0.2933 0.0419  0.0356  -0.0191 729 LYS A CD  
1791 C CE  . LYS A 211 ? 0.7307 0.4455 0.2307 0.0655  0.0305  -0.0135 729 LYS A CE  
1792 N NZ  . LYS A 211 ? 0.7518 0.4778 0.2314 0.0780  0.0135  -0.0267 729 LYS A NZ  
1793 N N   . LYS A 212 ? 0.6151 0.3475 0.2430 0.0073  0.0727  0.0032  730 LYS A N   
1794 C CA  . LYS A 212 ? 0.6053 0.3403 0.2393 0.0091  0.0676  0.0100  730 LYS A CA  
1795 C C   . LYS A 212 ? 0.5629 0.3215 0.2438 -0.0078 0.0707  0.0061  730 LYS A C   
1796 O O   . LYS A 212 ? 0.5858 0.3639 0.2884 -0.0088 0.0563  0.0074  730 LYS A O   
1797 C CB  . LYS A 212 ? 0.7199 0.4155 0.3117 0.0190  0.0874  0.0207  730 LYS A CB  
1798 C CG  . LYS A 212 ? 0.7729 0.4459 0.3113 0.0424  0.0817  0.0264  730 LYS A CG  
1799 C CD  . LYS A 212 ? 0.6903 0.3861 0.2282 0.0568  0.0518  0.0259  730 LYS A CD  
1800 C CE  . LYS A 212 ? 0.7074 0.3958 0.2431 0.0623  0.0533  0.0353  730 LYS A CE  
1801 N NZ  . LYS A 212 ? 0.7322 0.4405 0.2612 0.0802  0.0265  0.0346  730 LYS A NZ  
1802 N N   . GLU A 213 ? 0.5894 0.3486 0.2858 -0.0200 0.0895  -0.0001 731 GLU A N   
1803 C CA  . GLU A 213 ? 0.5465 0.3352 0.2876 -0.0333 0.0904  -0.0073 731 GLU A CA  
1804 C C   . GLU A 213 ? 0.5040 0.3240 0.2730 -0.0326 0.0685  -0.0111 731 GLU A C   
1805 O O   . GLU A 213 ? 0.4554 0.2977 0.2510 -0.0354 0.0587  -0.0111 731 GLU A O   
1806 C CB  . GLU A 213 ? 0.5845 0.3724 0.3373 -0.0448 0.1146  -0.0171 731 GLU A CB  
1807 C CG  . GLU A 213 ? 0.5847 0.4074 0.3826 -0.0565 0.1165  -0.0280 731 GLU A CG  
1808 C CD  . GLU A 213 ? 0.6048 0.4362 0.4196 -0.0668 0.1374  -0.0422 731 GLU A CD  
1809 O OE1 . GLU A 213 ? 0.7329 0.5370 0.5221 -0.0665 0.1537  -0.0417 731 GLU A OE1 
1810 O OE2 . GLU A 213 ? 0.6407 0.5076 0.4936 -0.0740 0.1377  -0.0550 731 GLU A OE2 
1811 N N   . TYR A 214 ? 0.5050 0.3234 0.2656 -0.0284 0.0631  -0.0141 732 TYR A N   
1812 C CA  . TYR A 214 ? 0.4737 0.3134 0.2563 -0.0273 0.0466  -0.0174 732 TYR A CA  
1813 C C   . TYR A 214 ? 0.5359 0.3840 0.3247 -0.0239 0.0291  -0.0128 732 TYR A C   
1814 O O   . TYR A 214 ? 0.4827 0.3503 0.2988 -0.0266 0.0222  -0.0128 732 TYR A O   
1815 C CB  . TYR A 214 ? 0.4843 0.3145 0.2507 -0.0228 0.0440  -0.0219 732 TYR A CB  
1816 C CG  . TYR A 214 ? 0.5257 0.3704 0.3118 -0.0222 0.0309  -0.0260 732 TYR A CG  
1817 C CD1 . TYR A 214 ? 0.4713 0.3309 0.2834 -0.0245 0.0345  -0.0291 732 TYR A CD1 
1818 C CD2 . TYR A 214 ? 0.5082 0.3512 0.2864 -0.0183 0.0166  -0.0282 732 TYR A CD2 
1819 C CE1 . TYR A 214 ? 0.5044 0.3692 0.3300 -0.0226 0.0268  -0.0314 732 TYR A CE1 
1820 C CE2 . TYR A 214 ? 0.5262 0.3777 0.3231 -0.0200 0.0094  -0.0336 732 TYR A CE2 
1821 C CZ  . TYR A 214 ? 0.5729 0.4313 0.3914 -0.0220 0.0160  -0.0337 732 TYR A CZ  
1822 O OH  . TYR A 214 ? 0.6300 0.4892 0.4625 -0.0224 0.0128  -0.0376 732 TYR A OH  
1823 N N   . ILE A 215 ? 0.4731 0.3070 0.2351 -0.0163 0.0227  -0.0093 733 ILE A N   
1824 C CA  . ILE A 215 ? 0.5052 0.3498 0.2734 -0.0123 0.0056  -0.0077 733 ILE A CA  
1825 C C   . ILE A 215 ? 0.5190 0.3728 0.3054 -0.0164 0.0068  -0.0020 733 ILE A C   
1826 O O   . ILE A 215 ? 0.5176 0.3884 0.3269 -0.0186 -0.0035 -0.0022 733 ILE A O   
1827 C CB  . ILE A 215 ? 0.5648 0.3965 0.2986 0.0004  -0.0019 -0.0067 733 ILE A CB  
1828 C CG1 . ILE A 215 ? 0.5499 0.3811 0.2715 0.0045  -0.0084 -0.0161 733 ILE A CG1 
1829 C CG2 . ILE A 215 ? 0.5277 0.3743 0.2713 0.0047  -0.0178 -0.0061 733 ILE A CG2 
1830 C CD1 . ILE A 215 ? 0.6236 0.4377 0.3003 0.0203  -0.0102 -0.0156 733 ILE A CD1 
1831 N N   . TYR A 216 ? 0.4731 0.3139 0.2495 -0.0183 0.0217  0.0019  734 TYR A N   
1832 C CA  . TYR A 216 ? 0.4817 0.3315 0.2762 -0.0234 0.0248  0.0047  734 TYR A CA  
1833 C C   . TYR A 216 ? 0.4015 0.2785 0.2319 -0.0306 0.0216  0.0001  734 TYR A C   
1834 O O   . TYR A 216 ? 0.4911 0.3831 0.3391 -0.0311 0.0131  0.0023  734 TYR A O   
1835 C CB  . TYR A 216 ? 0.4718 0.3010 0.2520 -0.0272 0.0465  0.0059  734 TYR A CB  
1836 C CG  . TYR A 216 ? 0.4885 0.3323 0.2955 -0.0374 0.0549  0.0021  734 TYR A CG  
1837 C CD1 . TYR A 216 ? 0.5546 0.4092 0.3804 -0.0477 0.0697  -0.0081 734 TYR A CD1 
1838 C CD2 . TYR A 216 ? 0.5821 0.4319 0.3969 -0.0363 0.0482  0.0064  734 TYR A CD2 
1839 C CE1 . TYR A 216 ? 0.5410 0.4148 0.3933 -0.0568 0.0764  -0.0157 734 TYR A CE1 
1840 C CE2 . TYR A 216 ? 0.6220 0.4867 0.4608 -0.0456 0.0559  0.0008  734 TYR A CE2 
1841 C CZ  . TYR A 216 ? 0.5858 0.4638 0.4435 -0.0557 0.0694  -0.0111 734 TYR A CZ  
1842 O OH  . TYR A 216 ? 0.6436 0.5426 0.5273 -0.0644 0.0756  -0.0206 734 TYR A OH  
1843 N N   . LEU A 217 ? 0.4774 0.3605 0.3165 -0.0341 0.0292  -0.0061 735 LEU A N   
1844 C CA  . LEU A 217 ? 0.3741 0.2831 0.2423 -0.0359 0.0268  -0.0105 735 LEU A CA  
1845 C C   . LEU A 217 ? 0.3614 0.2777 0.2386 -0.0309 0.0126  -0.0072 735 LEU A C   
1846 O O   . LEU A 217 ? 0.3900 0.3231 0.2856 -0.0292 0.0084  -0.0057 735 LEU A O   
1847 C CB  . LEU A 217 ? 0.4887 0.4030 0.3622 -0.0378 0.0380  -0.0189 735 LEU A CB  
1848 C CG  . LEU A 217 ? 0.3902 0.3024 0.2644 -0.0461 0.0566  -0.0262 735 LEU A CG  
1849 C CD1 . LEU A 217 ? 0.3983 0.3155 0.2776 -0.0484 0.0687  -0.0361 735 LEU A CD1 
1850 C CD2 . LEU A 217 ? 0.3713 0.3074 0.2700 -0.0509 0.0583  -0.0315 735 LEU A CD2 
1851 N N   . VAL A 218 ? 0.3743 0.2773 0.2377 -0.0284 0.0068  -0.0070 736 VAL A N   
1852 C CA  . VAL A 218 ? 0.4468 0.3533 0.3202 -0.0265 -0.0027 -0.0067 736 VAL A CA  
1853 C C   . VAL A 218 ? 0.4937 0.4067 0.3749 -0.0270 -0.0108 -0.0023 736 VAL A C   
1854 O O   . VAL A 218 ? 0.4632 0.3846 0.3609 -0.0267 -0.0132 0.0000  736 VAL A O   
1855 C CB  . VAL A 218 ? 0.4341 0.3280 0.2934 -0.0256 -0.0068 -0.0123 736 VAL A CB  
1856 C CG1 . VAL A 218 ? 0.3876 0.2848 0.2600 -0.0269 -0.0148 -0.0153 736 VAL A CG1 
1857 C CG2 . VAL A 218 ? 0.4530 0.3410 0.3081 -0.0249 0.0017  -0.0168 736 VAL A CG2 
1858 N N   . ILE A 219 ? 0.4862 0.3932 0.3532 -0.0261 -0.0135 -0.0006 737 ILE A N   
1859 C CA  . ILE A 219 ? 0.4247 0.3383 0.2982 -0.0254 -0.0210 0.0030  737 ILE A CA  
1860 C C   . ILE A 219 ? 0.3893 0.3151 0.2798 -0.0278 -0.0169 0.0071  737 ILE A C   
1861 O O   . ILE A 219 ? 0.4233 0.3586 0.3284 -0.0280 -0.0219 0.0095  737 ILE A O   
1862 C CB  . ILE A 219 ? 0.5053 0.4075 0.3553 -0.0200 -0.0231 0.0050  737 ILE A CB  
1863 C CG1 . ILE A 219 ? 0.5502 0.4480 0.3844 -0.0141 -0.0320 -0.0011 737 ILE A CG1 
1864 C CG2 . ILE A 219 ? 0.5167 0.4264 0.3742 -0.0183 -0.0287 0.0091  737 ILE A CG2 
1865 C CD1 . ILE A 219 ? 0.7306 0.6143 0.5331 -0.0034 -0.0328 0.0019  737 ILE A CD1 
1866 N N   . GLN A 220 ? 0.3841 0.3108 0.2734 -0.0300 -0.0069 0.0062  738 GLN A N   
1867 C CA  . GLN A 220 ? 0.3580 0.3014 0.2642 -0.0319 -0.0036 0.0060  738 GLN A CA  
1868 C C   . GLN A 220 ? 0.4614 0.4195 0.3833 -0.0279 -0.0067 0.0062  738 GLN A C   
1869 O O   . GLN A 220 ? 0.3609 0.3318 0.2942 -0.0256 -0.0094 0.0088  738 GLN A O   
1870 C CB  . GLN A 220 ? 0.3381 0.2837 0.2445 -0.0367 0.0092  -0.0004 738 GLN A CB  
1871 C CG  . GLN A 220 ? 0.4355 0.3606 0.3240 -0.0399 0.0179  0.0010  738 GLN A CG  
1872 C CD  . GLN A 220 ? 0.5896 0.5139 0.4789 -0.0389 0.0134  0.0062  738 GLN A CD  
1873 O OE1 . GLN A 220 ? 0.5497 0.4916 0.4568 -0.0419 0.0137  0.0035  738 GLN A OE1 
1874 N NE2 . GLN A 220 ? 0.5742 0.4804 0.4435 -0.0331 0.0085  0.0127  738 GLN A NE2 
1875 N N   . TRP A 221 ? 0.3140 0.2678 0.2336 -0.0253 -0.0051 0.0041  739 TRP A N   
1876 C CA  . TRP A 221 ? 0.4719 0.4329 0.4011 -0.0182 -0.0056 0.0062  739 TRP A CA  
1877 C C   . TRP A 221 ? 0.4530 0.4067 0.3856 -0.0177 -0.0101 0.0119  739 TRP A C   
1878 O O   . TRP A 221 ? 0.4274 0.3870 0.3669 -0.0116 -0.0090 0.0167  739 TRP A O   
1879 C CB  . TRP A 221 ? 0.3987 0.3522 0.3234 -0.0148 -0.0012 0.0029  739 TRP A CB  
1880 C CG  . TRP A 221 ? 0.4555 0.4098 0.3854 -0.0045 0.0007  0.0071  739 TRP A CG  
1881 C CD1 . TRP A 221 ? 0.4626 0.4341 0.3979 0.0073  0.0032  0.0072  739 TRP A CD1 
1882 C CD2 . TRP A 221 ? 0.4843 0.4201 0.4129 -0.0035 0.0023  0.0113  739 TRP A CD2 
1883 N NE1 . TRP A 221 ? 0.5303 0.4907 0.4625 0.0182  0.0067  0.0142  739 TRP A NE1 
1884 C CE2 . TRP A 221 ? 0.5767 0.5129 0.5059 0.0100  0.0081  0.0166  739 TRP A CE2 
1885 C CE3 . TRP A 221 ? 0.5646 0.4848 0.4922 -0.0123 0.0004  0.0091  739 TRP A CE3 
1886 C CZ2 . TRP A 221 ? 0.7658 0.6798 0.6925 0.0137  0.0157  0.0218  739 TRP A CZ2 
1887 C CZ3 . TRP A 221 ? 0.6200 0.5240 0.5511 -0.0115 0.0069  0.0106  739 TRP A CZ3 
1888 C CH2 . TRP A 221 ? 0.7082 0.6057 0.6378 0.0008  0.0163  0.0179  739 TRP A CH2 
1889 N N   . ARG A 222 ? 0.4568 0.3987 0.3842 -0.0232 -0.0144 0.0102  740 ARG A N   
1890 C CA  . ARG A 222 ? 0.4712 0.4083 0.4067 -0.0250 -0.0165 0.0113  740 ARG A CA  
1891 C C   . ARG A 222 ? 0.4045 0.3514 0.3482 -0.0254 -0.0195 0.0160  740 ARG A C   
1892 O O   . ARG A 222 ? 0.4482 0.3938 0.4010 -0.0246 -0.0165 0.0193  740 ARG A O   
1893 C CB  . ARG A 222 ? 0.4333 0.3628 0.3647 -0.0302 -0.0218 0.0033  740 ARG A CB  
1894 C CG  . ARG A 222 ? 0.3845 0.3144 0.3302 -0.0350 -0.0234 -0.0008 740 ARG A CG  
1895 C CD  . ARG A 222 ? 0.4206 0.3396 0.3757 -0.0349 -0.0117 0.0018  740 ARG A CD  
1896 N NE  . ARG A 222 ? 0.4518 0.3681 0.4230 -0.0424 -0.0083 -0.0044 740 ARG A NE  
1897 C CZ  . ARG A 222 ? 0.4721 0.3946 0.4543 -0.0439 -0.0074 -0.0008 740 ARG A CZ  
1898 N NH1 . ARG A 222 ? 0.4410 0.3726 0.4183 -0.0378 -0.0108 0.0094  740 ARG A NH1 
1899 N NH2 . ARG A 222 ? 0.4322 0.3525 0.4317 -0.0525 -0.0017 -0.0091 740 ARG A NH2 
1900 N N   . PHE A 223 ? 0.4024 0.3559 0.3415 -0.0264 -0.0229 0.0163  741 PHE A N   
1901 C CA  . PHE A 223 ? 0.4662 0.4268 0.4114 -0.0274 -0.0265 0.0194  741 PHE A CA  
1902 C C   . PHE A 223 ? 0.5095 0.4815 0.4571 -0.0257 -0.0238 0.0218  741 PHE A C   
1903 O O   . PHE A 223 ? 0.5184 0.4971 0.4727 -0.0255 -0.0254 0.0247  741 PHE A O   
1904 C CB  . PHE A 223 ? 0.3750 0.3316 0.3121 -0.0287 -0.0333 0.0165  741 PHE A CB  
1905 C CG  . PHE A 223 ? 0.4404 0.3949 0.3806 -0.0302 -0.0390 0.0100  741 PHE A CG  
1906 C CD1 . PHE A 223 ? 0.4582 0.4176 0.4164 -0.0338 -0.0385 0.0079  741 PHE A CD1 
1907 C CD2 . PHE A 223 ? 0.3827 0.3311 0.3081 -0.0283 -0.0434 0.0042  741 PHE A CD2 
1908 C CE1 . PHE A 223 ? 0.4141 0.3751 0.3805 -0.0378 -0.0422 -0.0031 741 PHE A CE1 
1909 C CE2 . PHE A 223 ? 0.3880 0.3402 0.3186 -0.0298 -0.0498 -0.0062 741 PHE A CE2 
1910 C CZ  . PHE A 223 ? 0.3925 0.3525 0.3459 -0.0356 -0.0492 -0.0113 741 PHE A CZ  
1911 N N   . VAL A 224 ? 0.4623 0.4386 0.4064 -0.0253 -0.0190 0.0184  742 VAL A N   
1912 C CA  . VAL A 224 ? 0.3871 0.3765 0.3358 -0.0265 -0.0156 0.0155  742 VAL A CA  
1913 C C   . VAL A 224 ? 0.5646 0.5745 0.5220 -0.0215 -0.0125 0.0106  742 VAL A C   
1914 O O   . VAL A 224 ? 0.5882 0.6151 0.5533 -0.0177 -0.0136 0.0098  742 VAL A O   
1915 C CB  . VAL A 224 ? 0.3616 0.3406 0.3004 -0.0324 -0.0097 0.0114  742 VAL A CB  
1916 C CG1 . VAL A 224 ? 0.3771 0.3694 0.3246 -0.0367 -0.0024 0.0046  742 VAL A CG1 
1917 C CG2 . VAL A 224 ? 0.4383 0.4001 0.3649 -0.0322 -0.0141 0.0164  742 VAL A CG2 
1918 N N   . ASN A 225 ? 0.5883 0.5987 0.5438 -0.0202 -0.0091 0.0060  743 ASN A N   
1919 C CA  . ASN A 225 ? 0.5505 0.5851 0.5153 -0.0149 -0.0061 -0.0028 743 ASN A CA  
1920 C C   . ASN A 225 ? 0.4929 0.5464 0.4626 -0.0017 -0.0106 -0.0001 743 ASN A C   
1921 O O   . ASN A 225 ? 0.4859 0.5671 0.4651 0.0024  -0.0111 -0.0091 743 ASN A O   
1922 C CB  . ASN A 225 ? 0.5002 0.5303 0.4613 -0.0123 -0.0028 -0.0059 743 ASN A CB  
1923 C CG  . ASN A 225 ? 0.5213 0.5424 0.4790 -0.0232 0.0053  -0.0134 743 ASN A CG  
1924 O OD1 . ASN A 225 ? 0.5342 0.5528 0.4923 -0.0322 0.0105  -0.0173 743 ASN A OD1 
1925 N ND2 . ASN A 225 ? 0.5458 0.5593 0.4982 -0.0220 0.0087  -0.0154 743 ASN A ND2 
1926 N N   . ARG A 226 ? 0.5262 0.5642 0.4884 0.0056  -0.0124 0.0113  744 ARG A N   
1927 C CA  . ARG A 226 ? 0.4458 0.4945 0.4055 0.0222  -0.0132 0.0163  744 ARG A CA  
1928 C C   . ARG A 226 ? 0.4953 0.5486 0.4558 0.0234  -0.0154 0.0213  744 ARG A C   
1929 O O   . ARG A 226 ? 0.4017 0.4640 0.3566 0.0389  -0.0154 0.0258  744 ARG A O   
1930 C CB  . ARG A 226 ? 0.4782 0.5025 0.4277 0.0301  -0.0088 0.0263  744 ARG A CB  
1931 C CG  . ARG A 226 ? 0.5559 0.5803 0.5028 0.0360  -0.0061 0.0219  744 ARG A CG  
1932 C CD  . ARG A 226 ? 0.5518 0.5443 0.4892 0.0385  0.0006  0.0306  744 ARG A CD  
1933 N NE  . ARG A 226 ? 0.5232 0.4954 0.4631 0.0206  0.0003  0.0301  744 ARG A NE  
1934 C CZ  . ARG A 226 ? 0.5850 0.5315 0.5223 0.0171  0.0061  0.0340  744 ARG A CZ  
1935 N NH1 . ARG A 226 ? 0.6470 0.5774 0.5767 0.0293  0.0159  0.0411  744 ARG A NH1 
1936 N NH2 . ARG A 226 ? 0.5709 0.5079 0.5128 0.0022  0.0031  0.0296  744 ARG A NH2 
1937 N N   . ILE A 227 ? 0.4895 0.5359 0.4546 0.0095  -0.0167 0.0207  745 ILE A N   
1938 C CA  . ILE A 227 ? 0.5097 0.5573 0.4760 0.0097  -0.0180 0.0257  745 ILE A CA  
1939 C C   . ILE A 227 ? 0.4687 0.5314 0.4431 0.0009  -0.0195 0.0168  745 ILE A C   
1940 O O   . ILE A 227 ? 0.4414 0.5019 0.4177 -0.0023 -0.0203 0.0200  745 ILE A O   
1941 C CB  . ILE A 227 ? 0.3598 0.3817 0.3248 0.0029  -0.0167 0.0346  745 ILE A CB  
1942 C CG1 . ILE A 227 ? 0.3252 0.3346 0.2911 -0.0096 -0.0190 0.0309  745 ILE A CG1 
1943 C CG2 . ILE A 227 ? 0.4112 0.4163 0.3697 0.0107  -0.0110 0.0421  745 ILE A CG2 
1944 C CD1 . ILE A 227 ? 0.3196 0.3335 0.2875 -0.0174 -0.0211 0.0263  745 ILE A CD1 
1945 N N   . GLN A 228 ? 0.4276 0.5043 0.4080 -0.0037 -0.0177 0.0045  746 GLN A N   
1946 C CA  . GLN A 228 ? 0.4170 0.5036 0.4057 -0.0141 -0.0143 -0.0064 746 GLN A CA  
1947 C C   . GLN A 228 ? 0.3961 0.5058 0.3911 -0.0092 -0.0167 -0.0112 746 GLN A C   
1948 O O   . GLN A 228 ? 0.4317 0.5361 0.4290 -0.0169 -0.0147 -0.0119 746 GLN A O   
1949 C CB  . GLN A 228 ? 0.4908 0.5913 0.4880 -0.0200 -0.0083 -0.0219 746 GLN A CB  
1950 C CG  . GLN A 228 ? 0.5855 0.6588 0.5747 -0.0295 -0.0021 -0.0195 746 GLN A CG  
1951 C CD  . GLN A 228 ? 0.7802 0.8661 0.7777 -0.0344 0.0060  -0.0343 746 GLN A CD  
1952 O OE1 . GLN A 228 ? 0.8096 0.9292 0.8215 -0.0292 0.0049  -0.0476 746 GLN A OE1 
1953 N NE2 . GLN A 228 ? 0.7982 0.8585 0.7863 -0.0430 0.0145  -0.0331 746 GLN A NE2 
1954 N N   . LYS A 229 ? 0.3374 0.4728 0.3330 0.0056  -0.0209 -0.0149 747 LYS A N   
1955 C CA  . LYS A 229 ? 0.3657 0.5270 0.3644 0.0134  -0.0242 -0.0210 747 LYS A CA  
1956 C C   . LYS A 229 ? 0.3392 0.4809 0.3277 0.0168  -0.0250 -0.0049 747 LYS A C   
1957 O O   . LYS A 229 ? 0.3464 0.4920 0.3392 0.0111  -0.0243 -0.0081 747 LYS A O   
1958 C CB  . LYS A 229 ? 0.3546 0.5495 0.3517 0.0336  -0.0297 -0.0286 747 LYS A CB  
1959 C CG  . LYS A 229 ? 0.5387 0.7709 0.5555 0.0283  -0.0292 -0.0544 747 LYS A CG  
1960 C CD  . LYS A 229 ? 0.7046 0.9546 0.7363 0.0153  -0.0263 -0.0711 747 LYS A CD  
1961 C CE  . LYS A 229 ? 0.6814 0.9536 0.7373 -0.0016 -0.0182 -0.0979 747 LYS A CE  
1962 N NZ  . LYS A 229 ? 0.7101 1.0313 0.7803 0.0101  -0.0234 -0.1195 747 LYS A NZ  
1963 N N   . GLN A 230 ? 0.3507 0.4695 0.3275 0.0240  -0.0244 0.0111  748 GLN A N   
1964 C CA  . GLN A 230 ? 0.3180 0.4155 0.2888 0.0239  -0.0220 0.0249  748 GLN A CA  
1965 C C   . GLN A 230 ? 0.3851 0.4707 0.3644 0.0076  -0.0215 0.0242  748 GLN A C   
1966 O O   . GLN A 230 ? 0.3072 0.3942 0.2878 0.0072  -0.0208 0.0262  748 GLN A O   
1967 C CB  . GLN A 230 ? 0.3922 0.4630 0.3545 0.0277  -0.0178 0.0378  748 GLN A CB  
1968 C CG  . GLN A 230 ? 0.4234 0.4981 0.3714 0.0484  -0.0155 0.0429  748 GLN A CG  
1969 C CD  . GLN A 230 ? 0.4487 0.5269 0.3973 0.0504  -0.0170 0.0375  748 GLN A CD  
1970 O OE1 . GLN A 230 ? 0.4139 0.5058 0.3742 0.0396  -0.0208 0.0254  748 GLN A OE1 
1971 N NE2 . GLN A 230 ? 0.4004 0.4626 0.3359 0.0640  -0.0115 0.0468  748 GLN A NE2 
1972 N N   . MET A 231 ? 0.3250 0.3975 0.3074 -0.0035 -0.0212 0.0218  749 MET A N   
1973 C CA  . MET A 231 ? 0.2810 0.3397 0.2665 -0.0143 -0.0208 0.0225  749 MET A CA  
1974 C C   . MET A 231 ? 0.3142 0.3851 0.3051 -0.0195 -0.0180 0.0123  749 MET A C   
1975 O O   . MET A 231 ? 0.3828 0.4467 0.3751 -0.0232 -0.0169 0.0141  749 MET A O   
1976 C CB  . MET A 231 ? 0.3733 0.4142 0.3549 -0.0211 -0.0207 0.0226  749 MET A CB  
1977 C CG  . MET A 231 ? 0.4573 0.4830 0.4368 -0.0267 -0.0211 0.0248  749 MET A CG  
1978 S SD  . MET A 231 ? 0.5850 0.6055 0.5695 -0.0242 -0.0258 0.0330  749 MET A SD  
1979 C CE  . MET A 231 ? 0.6260 0.6354 0.6065 -0.0261 -0.0280 0.0327  749 MET A CE  
1980 N N   . ALA A 232 ? 0.3514 0.4416 0.3471 -0.0199 -0.0159 -0.0003 750 ALA A N   
1981 C CA  . ALA A 232 ? 0.3103 0.4149 0.3148 -0.0267 -0.0108 -0.0145 750 ALA A CA  
1982 C C   . ALA A 232 ? 0.3936 0.5125 0.3993 -0.0202 -0.0139 -0.0138 750 ALA A C   
1983 O O   . ALA A 232 ? 0.3579 0.4748 0.3677 -0.0267 -0.0096 -0.0186 750 ALA A O   
1984 C CB  . ALA A 232 ? 0.2848 0.4152 0.2991 -0.0282 -0.0082 -0.0323 750 ALA A CB  
1985 N N   . ALA A 233 ? 0.3269 0.4570 0.3264 -0.0060 -0.0195 -0.0071 751 ALA A N   
1986 C CA  . ALA A 233 ? 0.2460 0.3888 0.2423 0.0029  -0.0212 -0.0055 751 ALA A CA  
1987 C C   . ALA A 233 ? 0.3460 0.4650 0.3403 -0.0013 -0.0190 0.0074  751 ALA A C   
1988 O O   . ALA A 233 ? 0.3634 0.4879 0.3598 -0.0021 -0.0175 0.0047  751 ALA A O   
1989 C CB  . ALA A 233 ? 0.2358 0.3910 0.2197 0.0226  -0.0250 0.0005  751 ALA A CB  
1990 N N   . PHE A 234 ? 0.3717 0.4670 0.3634 -0.0040 -0.0189 0.0191  752 PHE A N   
1991 C CA  . PHE A 234 ? 0.3530 0.4308 0.3471 -0.0081 -0.0177 0.0280  752 PHE A CA  
1992 C C   . PHE A 234 ? 0.3786 0.4512 0.3780 -0.0173 -0.0163 0.0221  752 PHE A C   
1993 O O   . PHE A 234 ? 0.3073 0.3789 0.3097 -0.0178 -0.0147 0.0234  752 PHE A O   
1994 C CB  . PHE A 234 ? 0.2931 0.3523 0.2867 -0.0100 -0.0185 0.0362  752 PHE A CB  
1995 C CG  . PHE A 234 ? 0.3139 0.3617 0.3146 -0.0148 -0.0187 0.0404  752 PHE A CG  
1996 C CD1 . PHE A 234 ? 0.3206 0.3654 0.3252 -0.0123 -0.0145 0.0465  752 PHE A CD1 
1997 C CD2 . PHE A 234 ? 0.2904 0.3306 0.2930 -0.0203 -0.0219 0.0377  752 PHE A CD2 
1998 C CE1 . PHE A 234 ? 0.3325 0.3729 0.3485 -0.0171 -0.0146 0.0468  752 PHE A CE1 
1999 C CE2 . PHE A 234 ? 0.3213 0.3571 0.3314 -0.0214 -0.0241 0.0394  752 PHE A CE2 
2000 C CZ  . PHE A 234 ? 0.3987 0.4376 0.4182 -0.0208 -0.0211 0.0425  752 PHE A CZ  
2001 N N   . LYS A 235 ? 0.3287 0.3949 0.3272 -0.0238 -0.0148 0.0162  753 LYS A N   
2002 C CA  . LYS A 235 ? 0.3441 0.3979 0.3424 -0.0306 -0.0095 0.0121  753 LYS A CA  
2003 C C   . LYS A 235 ? 0.4046 0.4721 0.4087 -0.0331 -0.0042 0.0015  753 LYS A C   
2004 O O   . LYS A 235 ? 0.4148 0.4724 0.4192 -0.0350 -0.0001 0.0020  753 LYS A O   
2005 C CB  . LYS A 235 ? 0.3419 0.3826 0.3346 -0.0362 -0.0049 0.0080  753 LYS A CB  
2006 C CG  . LYS A 235 ? 0.3350 0.3587 0.3196 -0.0333 -0.0104 0.0180  753 LYS A CG  
2007 C CD  . LYS A 235 ? 0.4840 0.4970 0.4609 -0.0371 -0.0059 0.0144  753 LYS A CD  
2008 C CE  . LYS A 235 ? 0.5660 0.5569 0.5327 -0.0411 0.0051  0.0120  753 LYS A CE  
2009 N NZ  . LYS A 235 ? 0.6570 0.6315 0.6118 -0.0434 0.0111  0.0110  753 LYS A NZ  
2010 N N   . GLU A 236 ? 0.3695 0.4622 0.3785 -0.0316 -0.0046 -0.0093 754 GLU A N   
2011 C CA  . GLU A 236 ? 0.3400 0.4517 0.3560 -0.0337 -0.0007 -0.0231 754 GLU A CA  
2012 C C   . GLU A 236 ? 0.3506 0.4613 0.3645 -0.0279 -0.0026 -0.0150 754 GLU A C   
2013 O O   . GLU A 236 ? 0.4004 0.5063 0.4177 -0.0329 0.0034  -0.0203 754 GLU A O   
2014 C CB  . GLU A 236 ? 0.3586 0.5054 0.3795 -0.0281 -0.0047 -0.0369 754 GLU A CB  
2015 C CG  . GLU A 236 ? 0.4422 0.6144 0.4721 -0.0306 -0.0015 -0.0561 754 GLU A CG  
2016 C CD  . GLU A 236 ? 0.6521 0.8642 0.6912 -0.0270 -0.0049 -0.0768 754 GLU A CD  
2017 O OE1 . GLU A 236 ? 0.7741 1.0129 0.8065 -0.0104 -0.0143 -0.0773 754 GLU A OE1 
2018 O OE2 . GLU A 236 ? 0.7226 0.9393 0.7747 -0.0395 0.0026  -0.0933 754 GLU A OE2 
2019 N N   . GLY A 237 ? 0.3755 0.4875 0.3836 -0.0179 -0.0086 -0.0022 755 GLY A N   
2020 C CA  . GLY A 237 ? 0.2920 0.4028 0.2986 -0.0128 -0.0081 0.0052  755 GLY A CA  
2021 C C   . GLY A 237 ? 0.3375 0.4265 0.3481 -0.0185 -0.0057 0.0117  755 GLY A C   
2022 O O   . GLY A 237 ? 0.3213 0.4101 0.3349 -0.0188 -0.0023 0.0103  755 GLY A O   
2023 N N   . PHE A 238 ? 0.2956 0.3682 0.3055 -0.0211 -0.0080 0.0179  756 PHE A N   
2024 C CA  . PHE A 238 ? 0.3387 0.3946 0.3505 -0.0220 -0.0083 0.0236  756 PHE A CA  
2025 C C   . PHE A 238 ? 0.3446 0.3908 0.3544 -0.0255 -0.0015 0.0171  756 PHE A C   
2026 O O   . PHE A 238 ? 0.3973 0.4377 0.4091 -0.0229 0.0003  0.0193  756 PHE A O   
2027 C CB  . PHE A 238 ? 0.3409 0.3843 0.3495 -0.0222 -0.0131 0.0286  756 PHE A CB  
2028 C CG  . PHE A 238 ? 0.3211 0.3541 0.3312 -0.0190 -0.0164 0.0329  756 PHE A CG  
2029 C CD1 . PHE A 238 ? 0.3018 0.3423 0.3231 -0.0166 -0.0199 0.0362  756 PHE A CD1 
2030 C CD2 . PHE A 238 ? 0.3749 0.3911 0.3745 -0.0169 -0.0147 0.0326  756 PHE A CD2 
2031 C CE1 . PHE A 238 ? 0.3083 0.3471 0.3344 -0.0119 -0.0248 0.0365  756 PHE A CE1 
2032 C CE2 . PHE A 238 ? 0.3983 0.4085 0.3965 -0.0090 -0.0196 0.0359  756 PHE A CE2 
2033 C CZ  . PHE A 238 ? 0.2923 0.3175 0.3057 -0.0063 -0.0261 0.0366  756 PHE A CZ  
2034 N N   . PHE A 239 ? 0.3079 0.3514 0.3143 -0.0315 0.0043  0.0081  757 PHE A N   
2035 C CA  . PHE A 239 ? 0.3528 0.3794 0.3557 -0.0364 0.0158  0.0014  757 PHE A CA  
2036 C C   . PHE A 239 ? 0.3992 0.4381 0.4094 -0.0393 0.0219  -0.0090 757 PHE A C   
2037 O O   . PHE A 239 ? 0.5323 0.5545 0.5404 -0.0428 0.0332  -0.0139 757 PHE A O   
2038 C CB  . PHE A 239 ? 0.3325 0.3502 0.3315 -0.0443 0.0240  -0.0068 757 PHE A CB  
2039 C CG  . PHE A 239 ? 0.4012 0.4016 0.3891 -0.0409 0.0201  0.0032  757 PHE A CG  
2040 C CD1 . PHE A 239 ? 0.4292 0.4136 0.4078 -0.0317 0.0143  0.0157  757 PHE A CD1 
2041 C CD2 . PHE A 239 ? 0.4516 0.4549 0.4388 -0.0460 0.0217  -0.0019 757 PHE A CD2 
2042 C CE1 . PHE A 239 ? 0.4215 0.3930 0.3887 -0.0273 0.0097  0.0225  757 PHE A CE1 
2043 C CE2 . PHE A 239 ? 0.4936 0.4808 0.4690 -0.0425 0.0184  0.0066  757 PHE A CE2 
2044 C CZ  . PHE A 239 ? 0.4383 0.4095 0.4029 -0.0330 0.0121  0.0187  757 PHE A CZ  
2045 N N   . GLU A 240 ? 0.3612 0.4268 0.3776 -0.0362 0.0156  -0.0117 758 GLU A N   
2046 C CA  . GLU A 240 ? 0.4201 0.4994 0.4414 -0.0366 0.0197  -0.0212 758 GLU A CA  
2047 C C   . GLU A 240 ? 0.4808 0.5470 0.5014 -0.0314 0.0204  -0.0109 758 GLU A C   
2048 O O   . GLU A 240 ? 0.4046 0.4714 0.4279 -0.0327 0.0270  -0.0177 758 GLU A O   
2049 C CB  . GLU A 240 ? 0.2788 0.3899 0.3010 -0.0303 0.0125  -0.0258 758 GLU A CB  
2050 C CG  . GLU A 240 ? 0.3701 0.5043 0.3971 -0.0346 0.0129  -0.0441 758 GLU A CG  
2051 C CD  . GLU A 240 ? 0.4936 0.6598 0.5161 -0.0221 0.0037  -0.0467 758 GLU A CD  
2052 O OE1 . GLU A 240 ? 0.4705 0.6323 0.4831 -0.0111 -0.0014 -0.0300 758 GLU A OE1 
2053 O OE2 . GLU A 240 ? 0.4847 0.6803 0.5129 -0.0224 0.0026  -0.0664 758 GLU A OE2 
2054 N N   . LEU A 241 ? 0.4306 0.4871 0.4496 -0.0257 0.0137  0.0034  759 LEU A N   
2055 C CA  . LEU A 241 ? 0.4269 0.4752 0.4488 -0.0202 0.0137  0.0107  759 LEU A CA  
2056 C C   . LEU A 241 ? 0.3486 0.3724 0.3639 -0.0170 0.0159  0.0152  759 LEU A C   
2057 O O   . LEU A 241 ? 0.4553 0.4689 0.4699 -0.0123 0.0207  0.0160  759 LEU A O   
2058 C CB  . LEU A 241 ? 0.4324 0.4912 0.4605 -0.0153 0.0062  0.0200  759 LEU A CB  
2059 C CG  . LEU A 241 ? 0.4544 0.5298 0.4841 -0.0139 0.0095  0.0170  759 LEU A CG  
2060 C CD1 . LEU A 241 ? 0.3241 0.4131 0.3474 -0.0125 0.0068  0.0161  759 LEU A CD1 
2061 C CD2 . LEU A 241 ? 0.4956 0.5733 0.5334 -0.0099 0.0106  0.0232  759 LEU A CD2 
2062 N N   . ILE A 242 ? 0.3613 0.3750 0.3693 -0.0172 0.0127  0.0186  760 ILE A N   
2063 C CA  . ILE A 242 ? 0.4129 0.4026 0.4087 -0.0098 0.0139  0.0245  760 ILE A CA  
2064 C C   . ILE A 242 ? 0.4263 0.3952 0.4089 -0.0159 0.0247  0.0201  760 ILE A C   
2065 O O   . ILE A 242 ? 0.5155 0.4897 0.4976 -0.0211 0.0216  0.0188  760 ILE A O   
2066 C CB  . ILE A 242 ? 0.4205 0.4159 0.4176 -0.0024 0.0005  0.0320  760 ILE A CB  
2067 C CG1 . ILE A 242 ? 0.3337 0.3529 0.3495 -0.0010 -0.0073 0.0331  760 ILE A CG1 
2068 C CG2 . ILE A 242 ? 0.5690 0.5433 0.5498 0.0107  -0.0001 0.0374  760 ILE A CG2 
2069 C CD1 . ILE A 242 ? 0.4824 0.5040 0.5049 0.0070  -0.0062 0.0333  760 ILE A CD1 
2070 N N   . PRO A 243 ? 0.5082 0.4522 0.4806 -0.0159 0.0399  0.0171  761 PRO A N   
2071 C CA  . PRO A 243 ? 0.5728 0.4908 0.5321 -0.0227 0.0555  0.0124  761 PRO A CA  
2072 C C   . PRO A 243 ? 0.5551 0.4609 0.4996 -0.0166 0.0497  0.0213  761 PRO A C   
2073 O O   . PRO A 243 ? 0.6080 0.5079 0.5421 -0.0018 0.0399  0.0322  761 PRO A O   
2074 C CB  . PRO A 243 ? 0.5545 0.4385 0.4995 -0.0170 0.0727  0.0138  761 PRO A CB  
2075 C CG  . PRO A 243 ? 0.6437 0.5467 0.6032 -0.0151 0.0681  0.0112  761 PRO A CG  
2076 C CD  . PRO A 243 ? 0.5312 0.4663 0.5032 -0.0092 0.0460  0.0179  761 PRO A CD  
2077 N N   . GLN A 244 ? 0.4789 0.3849 0.4239 -0.0275 0.0552  0.0147  762 GLN A N   
2078 C CA  . GLN A 244 ? 0.5435 0.4421 0.4762 -0.0231 0.0490  0.0217  762 GLN A CA  
2079 C C   . GLN A 244 ? 0.6096 0.4678 0.5121 -0.0095 0.0582  0.0322  762 GLN A C   
2080 O O   . GLN A 244 ? 0.6477 0.5019 0.5362 0.0027  0.0472  0.0413  762 GLN A O   
2081 C CB  . GLN A 244 ? 0.4157 0.3222 0.3560 -0.0377 0.0560  0.0106  762 GLN A CB  
2082 C CG  . GLN A 244 ? 0.6075 0.4859 0.5278 -0.0370 0.0658  0.0141  762 GLN A CG  
2083 C CD  . GLN A 244 ? 0.6275 0.5248 0.5599 -0.0487 0.0653  0.0044  762 GLN A CD  
2084 O OE1 . GLN A 244 ? 0.6875 0.5800 0.6097 -0.0448 0.0596  0.0104  762 GLN A OE1 
2085 N NE2 . GLN A 244 ? 0.5327 0.4549 0.4873 -0.0616 0.0701  -0.0120 762 GLN A NE2 
2086 N N   . ASP A 245 ? 0.6077 0.4353 0.4986 -0.0102 0.0792  0.0302  763 ASP A N   
2087 C CA  . ASP A 245 ? 0.8019 0.5840 0.6579 0.0061  0.0923  0.0417  763 ASP A CA  
2088 C C   . ASP A 245 ? 0.7910 0.5768 0.6367 0.0299  0.0757  0.0537  763 ASP A C   
2089 O O   . ASP A 245 ? 0.8905 0.6550 0.7072 0.0497  0.0735  0.0646  763 ASP A O   
2090 C CB  . ASP A 245 ? 0.8861 0.6312 0.7334 -0.0014 0.1229  0.0357  763 ASP A CB  
2091 C CG  . ASP A 245 ? 1.0939 0.8275 0.9460 -0.0226 0.1442  0.0225  763 ASP A CG  
2092 O OD1 . ASP A 245 ? 1.0855 0.8201 0.9307 -0.0235 0.1400  0.0250  763 ASP A OD1 
2093 O OD2 . ASP A 245 ? 1.1748 0.9003 1.0395 -0.0389 0.1657  0.0077  763 ASP A OD2 
2094 N N   . LEU A 246 ? 0.6316 0.4468 0.5010 0.0289  0.0642  0.0503  764 LEU A N   
2095 C CA  . LEU A 246 ? 0.5470 0.3755 0.4155 0.0490  0.0475  0.0575  764 LEU A CA  
2096 C C   . LEU A 246 ? 0.5802 0.4374 0.4552 0.0551  0.0241  0.0594  764 LEU A C   
2097 O O   . LEU A 246 ? 0.5666 0.4254 0.4288 0.0759  0.0127  0.0649  764 LEU A O   
2098 C CB  . LEU A 246 ? 0.6307 0.4849 0.5263 0.0431  0.0434  0.0516  764 LEU A CB  
2099 C CG  . LEU A 246 ? 0.6534 0.4823 0.5365 0.0552  0.0569  0.0547  764 LEU A CG  
2100 C CD1 . LEU A 246 ? 0.5655 0.3485 0.4266 0.0491  0.0849  0.0537  764 LEU A CD1 
2101 C CD2 . LEU A 246 ? 0.6388 0.4941 0.5495 0.0466  0.0542  0.0472  764 LEU A CD2 
2102 N N   . ILE A 247 ? 0.5317 0.4133 0.4273 0.0380  0.0170  0.0533  765 ILE A N   
2103 C CA  . ILE A 247 ? 0.5765 0.4846 0.4816 0.0414  -0.0028 0.0531  765 ILE A CA  
2104 C C   . ILE A 247 ? 0.6825 0.5696 0.5585 0.0532  -0.0038 0.0584  765 ILE A C   
2105 O O   . ILE A 247 ? 0.6288 0.5325 0.5043 0.0639  -0.0201 0.0581  765 ILE A O   
2106 C CB  . ILE A 247 ? 0.4425 0.3769 0.3733 0.0223  -0.0077 0.0467  765 ILE A CB  
2107 C CG1 . ILE A 247 ? 0.5242 0.4885 0.4736 0.0246  -0.0254 0.0447  765 ILE A CG1 
2108 C CG2 . ILE A 247 ? 0.4732 0.3955 0.3949 0.0119  -0.0001 0.0450  765 ILE A CG2 
2109 C CD1 . ILE A 247 ? 0.4984 0.4819 0.4657 0.0300  -0.0311 0.0429  765 ILE A CD1 
2110 N N   . LYS A 248 ? 0.7821 0.6323 0.6334 0.0518  0.0155  0.0619  766 LYS A N   
2111 C CA  . LYS A 248 ? 0.7594 0.5824 0.5773 0.0635  0.0196  0.0682  766 LYS A CA  
2112 C C   . LYS A 248 ? 0.7177 0.5281 0.5058 0.0940  0.0124  0.0767  766 LYS A C   
2113 O O   . LYS A 248 ? 0.6799 0.4713 0.4368 0.1084  0.0125  0.0823  766 LYS A O   
2114 C CB  . LYS A 248 ? 0.9018 0.6832 0.7003 0.0541  0.0479  0.0692  766 LYS A CB  
2115 C CG  . LYS A 248 ? 0.8964 0.6906 0.7191 0.0271  0.0555  0.0582  766 LYS A CG  
2116 C CD  . LYS A 248 ? 0.8343 0.6420 0.6580 0.0232  0.0449  0.0570  766 LYS A CD  
2117 C CE  . LYS A 248 ? 0.8961 0.6897 0.7204 0.0054  0.0645  0.0497  766 LYS A CE  
2118 N NZ  . LYS A 248 ? 0.8723 0.6849 0.7271 -0.0149 0.0726  0.0365  766 LYS A NZ  
2119 N N   . ILE A 249 ? 0.6749 0.4959 0.4697 0.1065  0.0063  0.0775  767 ILE A N   
2120 C CA  . ILE A 249 ? 0.7044 0.5181 0.4697 0.1394  -0.0025 0.0842  767 ILE A CA  
2121 C C   . ILE A 249 ? 0.5748 0.4318 0.3537 0.1473  -0.0303 0.0765  767 ILE A C   
2122 O O   . ILE A 249 ? 0.6998 0.5573 0.4528 0.1748  -0.0411 0.0789  767 ILE A O   
2123 C CB  . ILE A 249 ? 0.7766 0.5894 0.5434 0.1544  -0.0008 0.0866  767 ILE A CB  
2124 C CG1 . ILE A 249 ? 0.7951 0.6623 0.6030 0.1521  -0.0237 0.0761  767 ILE A CG1 
2125 C CG2 . ILE A 249 ? 0.8721 0.6564 0.6433 0.1369  0.0244  0.0877  767 ILE A CG2 
2126 C CD1 . ILE A 249 ? 0.8902 0.7587 0.6995 0.1689  -0.0226 0.0778  767 ILE A CD1 
2127 N N   . PHE A 250 ? 0.5502 0.4425 0.3685 0.1236  -0.0404 0.0664  768 PHE A N   
2128 C CA  . PHE A 250 ? 0.5911 0.5243 0.4292 0.1252  -0.0629 0.0557  768 PHE A CA  
2129 C C   . PHE A 250 ? 0.6101 0.5366 0.4371 0.1174  -0.0639 0.0547  768 PHE A C   
2130 O O   . PHE A 250 ? 0.6321 0.5363 0.4555 0.1001  -0.0487 0.0588  768 PHE A O   
2131 C CB  . PHE A 250 ? 0.4677 0.4383 0.3537 0.1048  -0.0697 0.0457  768 PHE A CB  
2132 C CG  . PHE A 250 ? 0.5228 0.5044 0.4233 0.1115  -0.0695 0.0450  768 PHE A CG  
2133 C CD1 . PHE A 250 ? 0.4181 0.4221 0.3195 0.1345  -0.0836 0.0396  768 PHE A CD1 
2134 C CD2 . PHE A 250 ? 0.5660 0.5383 0.4795 0.0958  -0.0556 0.0480  768 PHE A CD2 
2135 C CE1 . PHE A 250 ? 0.4564 0.4718 0.3723 0.1416  -0.0830 0.0383  768 PHE A CE1 
2136 C CE2 . PHE A 250 ? 0.4457 0.4278 0.3722 0.1020  -0.0548 0.0469  768 PHE A CE2 
2137 C CZ  . PHE A 250 ? 0.4672 0.4700 0.3955 0.1244  -0.0680 0.0426  768 PHE A CZ  
2138 N N   . ASP A 251 ? 0.6024 0.5509 0.4255 0.1304  -0.0815 0.0473  769 ASP A N   
2139 C CA  . ASP A 251 ? 0.5588 0.5086 0.3802 0.1195  -0.0843 0.0431  769 ASP A CA  
2140 C C   . ASP A 251 ? 0.5828 0.5681 0.4510 0.0957  -0.0920 0.0309  769 ASP A C   
2141 O O   . ASP A 251 ? 0.4691 0.4738 0.3674 0.0875  -0.0929 0.0271  769 ASP A O   
2142 C CB  . ASP A 251 ? 0.6032 0.5575 0.3952 0.1442  -0.0979 0.0396  769 ASP A CB  
2143 C CG  . ASP A 251 ? 0.6164 0.6188 0.4301 0.1581  -0.1213 0.0235  769 ASP A CG  
2144 O OD1 . ASP A 251 ? 0.6646 0.7017 0.5241 0.1403  -0.1279 0.0110  769 ASP A OD1 
2145 O OD2 . ASP A 251 ? 0.6734 0.6796 0.4572 0.1881  -0.1325 0.0221  769 ASP A OD2 
2146 N N   . GLU A 252 ? 0.5292 0.5202 0.4017 0.0854  -0.0955 0.0250  770 GLU A N   
2147 C CA  . GLU A 252 ? 0.4968 0.5086 0.4073 0.0619  -0.0959 0.0170  770 GLU A CA  
2148 C C   . GLU A 252 ? 0.4887 0.5404 0.4320 0.0621  -0.1099 0.0010  770 GLU A C   
2149 O O   . GLU A 252 ? 0.4893 0.5554 0.4653 0.0450  -0.1063 -0.0039 770 GLU A O   
2150 C CB  . GLU A 252 ? 0.5832 0.5853 0.4875 0.0512  -0.0928 0.0159  770 GLU A CB  
2151 C CG  . GLU A 252 ? 0.5944 0.6019 0.4795 0.0650  -0.1047 0.0083  770 GLU A CG  
2152 C CD  . GLU A 252 ? 0.7304 0.7072 0.5685 0.0852  -0.1002 0.0193  770 GLU A CD  
2153 O OE1 . GLU A 252 ? 0.7830 0.7276 0.6044 0.0799  -0.0830 0.0317  770 GLU A OE1 
2154 O OE2 . GLU A 252 ? 0.9971 0.9820 0.8141 0.1072  -0.1126 0.0144  770 GLU A OE2 
2155 N N   . ASN A 253 ? 0.4223 0.4926 0.3566 0.0824  -0.1248 -0.0082 771 ASN A N   
2156 C CA  . ASN A 253 ? 0.4287 0.5431 0.3986 0.0828  -0.1381 -0.0280 771 ASN A CA  
2157 C C   . ASN A 253 ? 0.5642 0.6903 0.5526 0.0857  -0.1362 -0.0267 771 ASN A C   
2158 O O   . ASN A 253 ? 0.4488 0.6022 0.4774 0.0721  -0.1361 -0.0389 771 ASN A O   
2159 C CB  . ASN A 253 ? 0.5301 0.6678 0.4851 0.1065  -0.1569 -0.0417 771 ASN A CB  
2160 C CG  . ASN A 253 ? 0.6379 0.7716 0.5816 0.1015  -0.1600 -0.0481 771 ASN A CG  
2161 O OD1 . ASN A 253 ? 0.7620 0.8895 0.7247 0.0773  -0.1509 -0.0497 771 ASN A OD1 
2162 N ND2 . ASN A 253 ? 0.6859 0.8220 0.5960 0.1264  -0.1722 -0.0513 771 ASN A ND2 
2163 N N   . GLU A 254 ? 0.5525 0.6549 0.5103 0.1033  -0.1323 -0.0119 772 GLU A N   
2164 C CA  . GLU A 254 ? 0.4751 0.5828 0.4440 0.1088  -0.1292 -0.0087 772 GLU A CA  
2165 C C   . GLU A 254 ? 0.4290 0.5267 0.4210 0.0830  -0.1136 -0.0024 772 GLU A C   
2166 O O   . GLU A 254 ? 0.4076 0.5269 0.4307 0.0759  -0.1127 -0.0090 772 GLU A O   
2167 C CB  . GLU A 254 ? 0.4841 0.5601 0.4091 0.1343  -0.1250 0.0068  772 GLU A CB  
2168 C CG  . GLU A 254 ? 0.5053 0.5974 0.4075 0.1671  -0.1420 0.0002  772 GLU A CG  
2169 C CD  . GLU A 254 ? 0.6480 0.6955 0.4939 0.1940  -0.1337 0.0187  772 GLU A CD  
2170 O OE1 . GLU A 254 ? 0.6313 0.6337 0.4560 0.1828  -0.1138 0.0344  772 GLU A OE1 
2171 O OE2 . GLU A 254 ? 0.6748 0.7328 0.4973 0.2276  -0.1461 0.0164  772 GLU A OE2 
2172 N N   . LEU A 255 ? 0.4367 0.5040 0.4132 0.0702  -0.1014 0.0089  773 LEU A N   
2173 C CA  . LEU A 255 ? 0.4488 0.5084 0.4420 0.0495  -0.0881 0.0142  773 LEU A CA  
2174 C C   . LEU A 255 ? 0.4524 0.5374 0.4825 0.0328  -0.0890 0.0032  773 LEU A C   
2175 O O   . LEU A 255 ? 0.4232 0.5142 0.4733 0.0232  -0.0814 0.0039  773 LEU A O   
2176 C CB  . LEU A 255 ? 0.4091 0.4386 0.3808 0.0407  -0.0772 0.0241  773 LEU A CB  
2177 C CG  . LEU A 255 ? 0.4451 0.4705 0.4308 0.0227  -0.0654 0.0280  773 LEU A CG  
2178 C CD1 . LEU A 255 ? 0.4748 0.5019 0.4687 0.0236  -0.0594 0.0307  773 LEU A CD1 
2179 C CD2 . LEU A 255 ? 0.4785 0.4798 0.4443 0.0166  -0.0557 0.0343  773 LEU A CD2 
2180 N N   . GLU A 256 ? 0.4128 0.5099 0.4501 0.0294  -0.0961 -0.0071 774 GLU A N   
2181 C CA  . GLU A 256 ? 0.4404 0.5561 0.5116 0.0126  -0.0929 -0.0187 774 GLU A CA  
2182 C C   . GLU A 256 ? 0.4859 0.6330 0.5887 0.0139  -0.0965 -0.0322 774 GLU A C   
2183 O O   . GLU A 256 ? 0.4623 0.6158 0.5915 -0.0003 -0.0857 -0.0355 774 GLU A O   
2184 C CB  . GLU A 256 ? 0.3903 0.5126 0.4631 0.0091  -0.0992 -0.0300 774 GLU A CB  
2185 C CG  . GLU A 256 ? 0.4815 0.6238 0.5920 -0.0075 -0.0943 -0.0465 774 GLU A CG  
2186 C CD  . GLU A 256 ? 0.5946 0.7393 0.7069 -0.0136 -0.0974 -0.0582 774 GLU A CD  
2187 O OE1 . GLU A 256 ? 0.6322 0.7794 0.7230 -0.0005 -0.1104 -0.0612 774 GLU A OE1 
2188 O OE2 . GLU A 256 ? 0.6828 0.8240 0.8157 -0.0308 -0.0851 -0.0641 774 GLU A OE2 
2189 N N   . LEU A 257 ? 0.4414 0.6083 0.5403 0.0327  -0.1108 -0.0403 775 LEU A N   
2190 C CA  . LEU A 257 ? 0.4672 0.6690 0.5969 0.0369  -0.1159 -0.0552 775 LEU A CA  
2191 C C   . LEU A 257 ? 0.4271 0.6174 0.5589 0.0355  -0.1048 -0.0428 775 LEU A C   
2192 O O   . LEU A 257 ? 0.4534 0.6612 0.6171 0.0250  -0.0977 -0.0509 775 LEU A O   
2193 C CB  . LEU A 257 ? 0.5379 0.7633 0.6562 0.0634  -0.1354 -0.0652 775 LEU A CB  
2194 C CG  . LEU A 257 ? 0.5744 0.8472 0.7274 0.0718  -0.1453 -0.0868 775 LEU A CG  
2195 C CD1 . LEU A 257 ? 0.6099 0.9153 0.8108 0.0495  -0.1422 -0.1117 775 LEU A CD1 
2196 C CD2 . LEU A 257 ? 0.5772 0.8701 0.7080 0.1041  -0.1662 -0.0941 775 LEU A CD2 
2197 N N   . LEU A 258 ? 0.4142 0.5736 0.5119 0.0447  -0.1012 -0.0242 776 LEU A N   
2198 C CA  . LEU A 258 ? 0.5703 0.7168 0.6668 0.0434  -0.0904 -0.0134 776 LEU A CA  
2199 C C   . LEU A 258 ? 0.5200 0.6615 0.6351 0.0215  -0.0757 -0.0108 776 LEU A C   
2200 O O   . LEU A 258 ? 0.5182 0.6713 0.6544 0.0168  -0.0689 -0.0137 776 LEU A O   
2201 C CB  . LEU A 258 ? 0.6214 0.7321 0.6786 0.0531  -0.0857 0.0034  776 LEU A CB  
2202 C CG  . LEU A 258 ? 0.6601 0.7522 0.7131 0.0473  -0.0718 0.0139  776 LEU A CG  
2203 C CD1 . LEU A 258 ? 0.6469 0.7556 0.7148 0.0569  -0.0729 0.0098  776 LEU A CD1 
2204 C CD2 . LEU A 258 ? 0.6568 0.7134 0.6744 0.0530  -0.0644 0.0260  776 LEU A CD2 
2205 N N   . MET A 259 ? 0.4151 0.5389 0.5203 0.0102  -0.0701 -0.0051 777 MET A N   
2206 C CA  . MET A 259 ? 0.3722 0.4861 0.4850 -0.0050 -0.0557 0.0007  777 MET A CA  
2207 C C   . MET A 259 ? 0.4027 0.5316 0.5462 -0.0179 -0.0487 -0.0103 777 MET A C   
2208 O O   . MET A 259 ? 0.4916 0.6161 0.6447 -0.0262 -0.0349 -0.0067 777 MET A O   
2209 C CB  . MET A 259 ? 0.4417 0.5324 0.5319 -0.0096 -0.0521 0.0103  777 MET A CB  
2210 C CG  . MET A 259 ? 0.5742 0.6463 0.6370 -0.0022 -0.0524 0.0200  777 MET A CG  
2211 S SD  . MET A 259 ? 0.6492 0.7025 0.6938 -0.0094 -0.0476 0.0264  777 MET A SD  
2212 C CE  . MET A 259 ? 0.4318 0.4874 0.4882 -0.0187 -0.0357 0.0300  777 MET A CE  
2213 N N   . CYS A 260 ? 0.3614 0.5056 0.5185 -0.0199 -0.0561 -0.0242 778 CYS A N   
2214 C CA  . CYS A 260 ? 0.3793 0.5299 0.5633 -0.0356 -0.0450 -0.0354 778 CYS A CA  
2215 C C   . CYS A 260 ? 0.3487 0.5359 0.5675 -0.0368 -0.0519 -0.0595 778 CYS A C   
2216 O O   . CYS A 260 ? 0.3900 0.5857 0.6380 -0.0519 -0.0399 -0.0733 778 CYS A O   
2217 C CB  . CYS A 260 ? 0.4014 0.5335 0.5720 -0.0419 -0.0427 -0.0324 778 CYS A CB  
2218 S SG  . CYS A 260 ? 0.6321 0.7297 0.7645 -0.0384 -0.0374 -0.0085 778 CYS A SG  
2219 N N   . GLY A 261 ? 0.4311 0.6396 0.6462 -0.0200 -0.0699 -0.0656 779 GLY A N   
2220 C CA  . GLY A 261 ? 0.4758 0.7275 0.7241 -0.0166 -0.0802 -0.0913 779 GLY A CA  
2221 C C   . GLY A 261 ? 0.5773 0.8469 0.8402 -0.0230 -0.0868 -0.1119 779 GLY A C   
2222 O O   . GLY A 261 ? 0.5866 0.8963 0.8858 -0.0258 -0.0920 -0.1388 779 GLY A O   
2223 N N   . LEU A 262 ? 0.7926 1.0354 1.0296 -0.0257 -0.0866 -0.1018 780 LEU A N   
2224 C CA  . LEU A 262 ? 0.8662 1.1224 1.1161 -0.0334 -0.0908 -0.1214 780 LEU A CA  
2225 C C   . LEU A 262 ? 0.8052 1.0693 1.0262 -0.0129 -0.1132 -0.1230 780 LEU A C   
2226 O O   . LEU A 262 ? 0.8634 1.1032 1.0450 0.0026  -0.1187 -0.1016 780 LEU A O   
2227 C CB  . LEU A 262 ? 0.9525 1.1732 1.1965 -0.0519 -0.0719 -0.1118 780 LEU A CB  
2228 C CG  . LEU A 262 ? 1.0837 1.3167 1.3497 -0.0653 -0.0697 -0.1355 780 LEU A CG  
2229 C CD1 . LEU A 262 ? 1.1165 1.3613 1.4286 -0.0874 -0.0489 -0.1554 780 LEU A CD1 
2230 C CD2 . LEU A 262 ? 1.0914 1.2888 1.3295 -0.0692 -0.0643 -0.1220 780 LEU A CD2 
2231 N N   . GLY A 263 ? 0.6732 0.9705 0.9134 -0.0128 -0.1244 -0.1498 781 GLY A N   
2232 C CA  . GLY A 263 ? 0.6441 0.9508 0.8554 0.0085  -0.1455 -0.1536 781 GLY A CA  
2233 C C   . GLY A 263 ? 0.7402 1.0896 0.9832 0.0029  -0.1549 -0.1893 781 GLY A C   
2234 O O   . GLY A 263 ? 0.7560 1.1242 1.0434 -0.0179 -0.1422 -0.2099 781 GLY A O   
2235 N N   . ASP A 264 ? 0.8054 1.1626 1.0206 0.0216  -0.1721 -0.1945 782 ASP A N   
2236 C CA  . ASP A 264 ? 0.9154 1.2979 1.1475 0.0178  -0.1739 -0.2218 782 ASP A CA  
2237 C C   . ASP A 264 ? 0.8963 1.3193 1.1463 0.0326  -0.1814 -0.2411 782 ASP A C   
2238 O O   . ASP A 264 ? 0.9136 1.3427 1.1350 0.0614  -0.1956 -0.2326 782 ASP A O   
2239 C CB  . ASP A 264 ? 1.0123 1.3828 1.2040 0.0326  -0.1860 -0.2180 782 ASP A CB  
2240 C CG  . ASP A 264 ? 1.1328 1.4676 1.3129 0.0149  -0.1773 -0.2056 782 ASP A CG  
2241 O OD1 . ASP A 264 ? 1.1155 1.4337 1.3222 -0.0110 -0.1577 -0.2028 782 ASP A OD1 
2242 O OD2 . ASP A 264 ? 1.2390 1.5550 1.3785 0.0282  -0.1859 -0.1953 782 ASP A OD2 
2243 N N   . VAL A 265 ? 0.7826 1.2305 1.0789 0.0130  -0.1696 -0.2675 783 VAL A N   
2244 C CA  . VAL A 265 ? 0.6326 1.1231 0.9525 0.0241  -0.1750 -0.2912 783 VAL A CA  
2245 C C   . VAL A 265 ? 0.6074 1.1283 0.9228 0.0386  -0.1880 -0.3160 783 VAL A C   
2246 O O   . VAL A 265 ? 0.5865 1.1110 0.9195 0.0213  -0.1803 -0.3340 783 VAL A O   
2247 C CB  . VAL A 265 ? 0.5576 1.0603 0.9300 -0.0039 -0.1533 -0.3099 783 VAL A CB  
2248 C CG1 . VAL A 265 ? 0.4674 1.0171 0.8654 0.0076  -0.1592 -0.3377 783 VAL A CG1 
2249 C CG2 . VAL A 265 ? 0.4806 0.9537 0.8564 -0.0168 -0.1394 -0.2854 783 VAL A CG2 
2250 N N   . ASP A 266 ? 0.5442 1.0858 0.8347 0.0717  -0.2066 -0.3171 784 ASP A N   
2251 C CA  . ASP A 266 ? 0.6498 1.2239 0.9340 0.0900  -0.2199 -0.3413 784 ASP A CA  
2252 C C   . ASP A 266 ? 0.6218 1.2447 0.9589 0.0789  -0.2145 -0.3816 784 ASP A C   
2253 O O   . ASP A 266 ? 0.5957 1.2512 0.9429 0.0957  -0.2218 -0.3948 784 ASP A O   
2254 C CB  . ASP A 266 ? 0.7565 1.3334 0.9933 0.1316  -0.2390 -0.3286 784 ASP A CB  
2255 C CG  . ASP A 266 ? 0.8581 1.4660 1.0820 0.1542  -0.2531 -0.3513 784 ASP A CG  
2256 O OD1 . ASP A 266 ? 0.8903 1.5077 1.1319 0.1378  -0.2495 -0.3700 784 ASP A OD1 
2257 O OD2 . ASP A 266 ? 0.9081 1.5296 1.1025 0.1897  -0.2669 -0.3503 784 ASP A OD2 
2258 N N   . VAL A 267 ? 0.6452 0.9373 0.7447 -0.1147 0.0589  0.0266  785 VAL A N   
2259 C CA  . VAL A 267 ? 0.5803 0.8256 0.6672 -0.0750 0.0487  0.0120  785 VAL A CA  
2260 C C   . VAL A 267 ? 0.6652 0.8733 0.7157 -0.0675 0.0487  0.0241  785 VAL A C   
2261 O O   . VAL A 267 ? 0.6977 0.8520 0.7442 -0.0473 0.0360  0.0200  785 VAL A O   
2262 C CB  . VAL A 267 ? 0.6418 0.9385 0.7530 -0.0386 0.0485  -0.0135 785 VAL A CB  
2263 C CG1 . VAL A 267 ? 0.6536 0.9687 0.7949 -0.0363 0.0392  -0.0250 785 VAL A CG1 
2264 C CG2 . VAL A 267 ? 0.7073 1.0832 0.8190 -0.0334 0.0662  -0.0170 785 VAL A CG2 
2265 N N   . ASN A 268 ? 0.6793 0.9196 0.7042 -0.0838 0.0627  0.0410  786 ASN A N   
2266 C CA  . ASN A 268 ? 0.7285 0.9298 0.7047 -0.0781 0.0582  0.0568  786 ASN A CA  
2267 C C   . ASN A 268 ? 0.7894 0.9040 0.7500 -0.0922 0.0435  0.0779  786 ASN A C   
2268 O O   . ASN A 268 ? 0.8464 0.9128 0.7962 -0.0692 0.0254  0.0768  786 ASN A O   
2269 C CB  . ASN A 268 ? 0.7905 1.0410 0.7301 -0.0963 0.0819  0.0774  786 ASN A CB  
2270 C CG  . ASN A 268 ? 0.8382 1.1800 0.7924 -0.0755 0.1012  0.0541  786 ASN A CG  
2271 O OD1 . ASN A 268 ? 0.9089 1.2571 0.8362 -0.0387 0.0955  0.0329  786 ASN A OD1 
2272 N ND2 . ASN A 268 ? 0.8256 1.2384 0.8257 -0.0968 0.1209  0.0551  786 ASN A ND2 
2273 N N   . ASP A 269 ? 0.7900 0.8856 0.7542 -0.1294 0.0490  0.0954  787 ASP A N   
2274 C CA  . ASP A 269 ? 0.8451 0.8492 0.7906 -0.1414 0.0351  0.1129  787 ASP A CA  
2275 C C   . ASP A 269 ? 0.7340 0.6961 0.7047 -0.1123 0.0219  0.0897  787 ASP A C   
2276 O O   . ASP A 269 ? 0.6856 0.5851 0.6468 -0.0943 0.0098  0.0950  787 ASP A O   
2277 C CB  . ASP A 269 ? 0.8667 0.8568 0.8126 -0.1912 0.0410  0.1318  787 ASP A CB  
2278 C CG  . ASP A 269 ? 0.9242 0.8060 0.8433 -0.2026 0.0246  0.1479  787 ASP A CG  
2279 O OD1 . ASP A 269 ? 0.9828 0.8154 0.8607 -0.2036 0.0202  0.1763  787 ASP A OD1 
2280 O OD2 . ASP A 269 ? 0.9086 0.7504 0.8417 -0.2089 0.0146  0.1319  787 ASP A OD2 
2281 N N   . TRP A 270 ? 0.6240 0.6246 0.6270 -0.1049 0.0259  0.0659  788 TRP A N   
2282 C CA  . TRP A 270 ? 0.6481 0.6174 0.6694 -0.0772 0.0212  0.0472  788 TRP A CA  
2283 C C   . TRP A 270 ? 0.6595 0.6243 0.6943 -0.0431 0.0160  0.0432  788 TRP A C   
2284 O O   . TRP A 270 ? 0.6795 0.5980 0.7245 -0.0251 0.0123  0.0435  788 TRP A O   
2285 C CB  . TRP A 270 ? 0.6455 0.6628 0.6898 -0.0737 0.0249  0.0272  788 TRP A CB  
2286 C CG  . TRP A 270 ? 0.6063 0.5909 0.6570 -0.0496 0.0248  0.0131  788 TRP A CG  
2287 C CD1 . TRP A 270 ? 0.6454 0.5710 0.6915 -0.0313 0.0276  0.0148  788 TRP A CD1 
2288 C CD2 . TRP A 270 ? 0.6063 0.6180 0.6670 -0.0387 0.0247  -0.0021 788 TRP A CD2 
2289 N NE1 . TRP A 270 ? 0.6169 0.5323 0.6654 -0.0121 0.0350  0.0032  788 TRP A NE1 
2290 C CE2 . TRP A 270 ? 0.6289 0.5908 0.6809 -0.0164 0.0307  -0.0061 788 TRP A CE2 
2291 C CE3 . TRP A 270 ? 0.5750 0.6504 0.6516 -0.0425 0.0204  -0.0114 788 TRP A CE3 
2292 C CZ2 . TRP A 270 ? 0.6206 0.5850 0.6668 -0.0002 0.0322  -0.0155 788 TRP A CZ2 
2293 C CZ3 . TRP A 270 ? 0.5267 0.6041 0.6035 -0.0234 0.0157  -0.0231 788 TRP A CZ3 
2294 C CH2 . TRP A 270 ? 0.5121 0.5297 0.5675 -0.0037 0.0214  -0.0234 788 TRP A CH2 
2295 N N   . ARG A 271 ? 0.6180 0.6336 0.6553 -0.0344 0.0148  0.0378  789 ARG A N   
2296 C CA  . ARG A 271 ? 0.5858 0.6040 0.6393 -0.0063 0.0023  0.0285  789 ARG A CA  
2297 C C   . ARG A 271 ? 0.6693 0.6453 0.7073 -0.0002 -0.0146 0.0451  789 ARG A C   
2298 O O   . ARG A 271 ? 0.6739 0.6320 0.7460 0.0209  -0.0277 0.0405  789 ARG A O   
2299 C CB  . ARG A 271 ? 0.6529 0.7281 0.6968 0.0014  0.0025  0.0142  789 ARG A CB  
2300 C CG  . ARG A 271 ? 0.6239 0.7021 0.6844 0.0284  -0.0160 -0.0044 789 ARG A CG  
2301 C CD  . ARG A 271 ? 0.6340 0.7620 0.6759 0.0398  -0.0129 -0.0248 789 ARG A CD  
2302 N NE  . ARG A 271 ? 0.8002 0.9197 0.8613 0.0648  -0.0350 -0.0494 789 ARG A NE  
2303 C CZ  . ARG A 271 ? 0.8335 0.9793 0.8866 0.0843  -0.0379 -0.0761 789 ARG A CZ  
2304 N NH1 . ARG A 271 ? 0.8471 1.0425 0.8792 0.0858  -0.0157 -0.0812 789 ARG A NH1 
2305 N NH2 . ARG A 271 ? 0.8620 0.9845 0.9341 0.1029  -0.0641 -0.0991 789 ARG A NH2 
2306 N N   . GLU A 272 ? 0.6218 0.5834 0.6124 -0.0191 -0.0149 0.0672  790 GLU A N   
2307 C CA  . GLU A 272 ? 0.7114 0.6299 0.6766 -0.0095 -0.0360 0.0862  790 GLU A CA  
2308 C C   . GLU A 272 ? 0.8039 0.6588 0.7884 -0.0023 -0.0418 0.0955  790 GLU A C   
2309 O O   . GLU A 272 ? 0.9189 0.7428 0.9080 0.0187  -0.0640 0.1045  790 GLU A O   
2310 C CB  . GLU A 272 ? 0.8209 0.7370 0.7187 -0.0320 -0.0316 0.1130  790 GLU A CB  
2311 C CG  . GLU A 272 ? 0.9649 0.9465 0.8366 -0.0283 -0.0235 0.1013  790 GLU A CG  
2312 C CD  . GLU A 272 ? 1.1450 1.1313 0.9443 -0.0491 -0.0106 0.1317  790 GLU A CD  
2313 O OE1 . GLU A 272 ? 1.1807 1.2135 0.9780 -0.0760 0.0201  0.1379  790 GLU A OE1 
2314 O OE2 . GLU A 272 ? 1.2319 1.1788 0.9779 -0.0382 -0.0311 0.1514  790 GLU A OE2 
2315 N N   . HIS A 273 ? 0.7044 0.5404 0.6995 -0.0152 -0.0245 0.0904  791 HIS A N   
2316 C CA  . HIS A 273 ? 0.7069 0.4782 0.7118 -0.0029 -0.0260 0.0931  791 HIS A CA  
2317 C C   . HIS A 273 ? 0.6565 0.4412 0.7108 0.0194  -0.0118 0.0705  791 HIS A C   
2318 O O   . HIS A 273 ? 0.6773 0.4195 0.7274 0.0243  -0.0005 0.0646  791 HIS A O   
2319 C CB  . HIS A 273 ? 0.7633 0.4818 0.7266 -0.0340 -0.0208 0.1048  791 HIS A CB  
2320 C CG  . HIS A 273 ? 0.8312 0.5300 0.7463 -0.0604 -0.0293 0.1353  791 HIS A CG  
2321 N ND1 . HIS A 273 ? 0.8661 0.6089 0.7614 -0.0981 -0.0165 0.1448  791 HIS A ND1 
2322 C CD2 . HIS A 273 ? 0.9775 0.6198 0.8595 -0.0532 -0.0475 0.1620  791 HIS A CD2 
2323 C CE1 . HIS A 273 ? 1.0120 0.7249 0.8603 -0.1165 -0.0214 0.1784  791 HIS A CE1 
2324 N NE2 . HIS A 273 ? 1.0317 0.6773 0.8655 -0.0894 -0.0428 0.1901  791 HIS A NE2 
2325 N N   . THR A 274 ? 0.6028 0.4412 0.6980 0.0330  -0.0122 0.0584  792 THR A N   
2326 C CA  . THR A 274 ? 0.5650 0.4162 0.7112 0.0529  0.0035  0.0450  792 THR A CA  
2327 C C   . THR A 274 ? 0.5879 0.4424 0.7911 0.0794  -0.0084 0.0487  792 THR A C   
2328 O O   . THR A 274 ? 0.6340 0.5050 0.8454 0.0828  -0.0359 0.0529  792 THR A O   
2329 C CB  . THR A 274 ? 0.5396 0.4409 0.7028 0.0482  0.0103  0.0311  792 THR A CB  
2330 O OG1 . THR A 274 ? 0.5155 0.4199 0.6400 0.0295  0.0212  0.0263  792 THR A OG1 
2331 C CG2 . THR A 274 ? 0.5368 0.4476 0.7553 0.0662  0.0262  0.0253  792 THR A CG2 
2332 N N   . LYS A 275 ? 0.5876 0.4293 0.8294 0.0999  0.0116  0.0466  793 LYS A N   
2333 C CA  . LYS A 275 ? 0.5598 0.4251 0.8813 0.1252  0.0061  0.0492  793 LYS A CA  
2334 C C   . LYS A 275 ? 0.5652 0.4783 0.9520 0.1252  0.0246  0.0426  793 LYS A C   
2335 O O   . LYS A 275 ? 0.5290 0.4422 0.8895 0.1137  0.0474  0.0374  793 LYS A O   
2336 C CB  . LYS A 275 ? 0.6039 0.4310 0.9365 0.1529  0.0212  0.0532  793 LYS A CB  
2337 C CG  . LYS A 275 ? 0.7866 0.5487 1.0554 0.1537  0.0007  0.0623  793 LYS A CG  
2338 C CD  . LYS A 275 ? 0.7963 0.5669 1.0600 0.1493  -0.0417 0.0754  793 LYS A CD  
2339 C CE  . LYS A 275 ? 0.9655 0.6698 1.1951 0.1658  -0.0634 0.0914  793 LYS A CE  
2340 N NZ  . LYS A 275 ? 1.0604 0.6899 1.2109 0.1475  -0.0507 0.0947  793 LYS A NZ  
2341 N N   . TYR A 276 ? 0.5496 0.5012 1.0237 0.1367  0.0116  0.0447  794 TYR A N   
2342 C CA  . TYR A 276 ? 0.4999 0.4931 1.0454 0.1295  0.0248  0.0425  794 TYR A CA  
2343 C C   . TYR A 276 ? 0.4647 0.4932 1.1153 0.1479  0.0432  0.0512  794 TYR A C   
2344 O O   . TYR A 276 ? 0.4825 0.5214 1.1752 0.1678  0.0230  0.0544  794 TYR A O   
2345 C CB  . TYR A 276 ? 0.4852 0.5010 1.0447 0.1139  -0.0169 0.0323  794 TYR A CB  
2346 C CG  . TYR A 276 ? 0.4491 0.4439 0.9136 0.0996  -0.0268 0.0232  794 TYR A CG  
2347 C CD1 . TYR A 276 ? 0.4538 0.4430 0.8850 0.0890  -0.0023 0.0186  794 TYR A CD1 
2348 C CD2 . TYR A 276 ? 0.5272 0.5117 0.9363 0.0987  -0.0591 0.0214  794 TYR A CD2 
2349 C CE1 . TYR A 276 ? 0.4350 0.4190 0.7940 0.0789  -0.0097 0.0096  794 TYR A CE1 
2350 C CE2 . TYR A 276 ? 0.4791 0.4574 0.8098 0.0856  -0.0605 0.0151  794 TYR A CE2 
2351 C CZ  . TYR A 276 ? 0.4872 0.4705 0.8005 0.0763  -0.0356 0.0078  794 TYR A CZ  
2352 O OH  . TYR A 276 ? 0.4590 0.4497 0.7095 0.0662  -0.0355 0.0009  794 TYR A OH  
2353 N N   . LYS A 277 ? 0.4525 0.5015 1.1472 0.1426  0.0828  0.0577  795 LYS A N   
2354 C CA  . LYS A 277 ? 0.4605 0.5519 1.2573 0.1595  0.1162  0.0700  795 LYS A CA  
2355 C C   . LYS A 277 ? 0.4458 0.5844 1.3419 0.1373  0.1255  0.0797  795 LYS A C   
2356 O O   . LYS A 277 ? 0.4776 0.5973 1.3400 0.1137  0.1262  0.0793  795 LYS A O   
2357 C CB  . LYS A 277 ? 0.4937 0.5570 1.2389 0.1805  0.1750  0.0750  795 LYS A CB  
2358 C CG  . LYS A 277 ? 0.6485 0.6633 1.3230 0.2072  0.1711  0.0659  795 LYS A CG  
2359 C CD  . LYS A 277 ? 0.7421 0.7193 1.3494 0.2259  0.2257  0.0641  795 LYS A CD  
2360 C CE  . LYS A 277 ? 0.8059 0.7801 1.4231 0.2608  0.2425  0.0599  795 LYS A CE  
2361 N NZ  . LYS A 277 ? 0.8815 0.9345 1.6168 0.2627  0.2457  0.0708  795 LYS A NZ  
2362 N N   . ASN A 278 ? 0.4626 0.6540 1.4633 0.1400  0.1285  0.0880  796 ASN A N   
2363 C CA  . ASN A 278 ? 0.5147 0.7481 1.6140 0.1139  0.1443  0.1023  796 ASN A CA  
2364 C C   . ASN A 278 ? 0.4962 0.7285 1.6311 0.0826  0.0980  0.0939  796 ASN A C   
2365 O O   . ASN A 278 ? 0.4219 0.6438 1.5690 0.0613  0.1210  0.1046  796 ASN A O   
2366 C CB  . ASN A 278 ? 0.4973 0.7195 1.5706 0.1143  0.2178  0.1230  796 ASN A CB  
2367 C CG  . ASN A 278 ? 0.5640 0.8282 1.7397 0.0901  0.2445  0.1459  796 ASN A CG  
2368 O OD1 . ASN A 278 ? 0.5113 0.8250 1.7806 0.0866  0.2274  0.1472  796 ASN A OD1 
2369 N ND2 . ASN A 278 ? 0.5113 0.7536 1.6691 0.0727  0.2838  0.1657  796 ASN A ND2 
2370 N N   . GLY A 279 ? 0.4265 0.6641 1.5716 0.0820  0.0310  0.0743  797 GLY A N   
2371 C CA  . GLY A 279 ? 0.4457 0.6791 1.6200 0.0561  -0.0210 0.0589  797 GLY A CA  
2372 C C   . GLY A 279 ? 0.4304 0.6048 1.4666 0.0580  -0.0513 0.0373  797 GLY A C   
2373 O O   . GLY A 279 ? 0.4267 0.5924 1.4544 0.0497  -0.1090 0.0153  797 GLY A O   
2374 N N   . TYR A 280 ? 0.4091 0.5454 1.3369 0.0695  -0.0132 0.0419  798 TYR A N   
2375 C CA  . TYR A 280 ? 0.4873 0.5805 1.2946 0.0698  -0.0347 0.0241  798 TYR A CA  
2376 C C   . TYR A 280 ? 0.4235 0.5132 1.1813 0.0844  -0.0751 0.0133  798 TYR A C   
2377 O O   . TYR A 280 ? 0.4779 0.5835 1.2678 0.1008  -0.0780 0.0224  798 TYR A O   
2378 C CB  . TYR A 280 ? 0.4669 0.5269 1.1831 0.0746  0.0122  0.0322  798 TYR A CB  
2379 C CG  . TYR A 280 ? 0.6039 0.6479 1.3233 0.0615  0.0408  0.0406  798 TYR A CG  
2380 C CD1 . TYR A 280 ? 0.6217 0.6402 1.2734 0.0682  0.0840  0.0520  798 TYR A CD1 
2381 C CD2 . TYR A 280 ? 0.6348 0.6812 1.4201 0.0429  0.0202  0.0377  798 TYR A CD2 
2382 C CE1 . TYR A 280 ? 0.4382 0.4351 1.0821 0.0598  0.1074  0.0641  798 TYR A CE1 
2383 C CE2 . TYR A 280 ? 0.6387 0.6582 1.4218 0.0315  0.0454  0.0504  798 TYR A CE2 
2384 C CZ  . TYR A 280 ? 0.6471 0.6428 1.3570 0.0417  0.0897  0.0656  798 TYR A CZ  
2385 O OH  . TYR A 280 ? 0.5760 0.5388 1.2737 0.0340  0.1122  0.0825  798 TYR A OH  
2386 N N   . SER A 281 ? 0.4404 0.5075 1.1164 0.0807  -0.1041 -0.0046 799 SER A N   
2387 C CA  . SER A 281 ? 0.5257 0.5830 1.1332 0.0914  -0.1391 -0.0112 799 SER A CA  
2388 C C   . SER A 281 ? 0.5800 0.6160 1.0853 0.0866  -0.1383 -0.0250 799 SER A C   
2389 O O   . SER A 281 ? 0.4889 0.5196 0.9900 0.0787  -0.1209 -0.0331 799 SER A O   
2390 C CB  . SER A 281 ? 0.6288 0.7053 1.2886 0.0949  -0.1983 -0.0235 799 SER A CB  
2391 O OG  . SER A 281 ? 0.6036 0.6782 1.2809 0.0817  -0.2254 -0.0469 799 SER A OG  
2392 N N   . ALA A 282 ? 0.5599 0.5853 0.9849 0.0928  -0.1558 -0.0252 800 ALA A N   
2393 C CA  . ALA A 282 ? 0.5596 0.5788 0.8937 0.0895  -0.1503 -0.0365 800 ALA A CA  
2394 C C   . ALA A 282 ? 0.6171 0.6403 0.9510 0.0915  -0.1753 -0.0666 800 ALA A C   
2395 O O   . ALA A 282 ? 0.5772 0.6015 0.8692 0.0919  -0.1580 -0.0787 800 ALA A O   
2396 C CB  . ALA A 282 ? 0.5585 0.5674 0.8115 0.0938  -0.1644 -0.0261 800 ALA A CB  
2397 N N   . ASN A 283 ? 0.6276 0.6515 1.0119 0.0943  -0.2192 -0.0808 801 ASN A N   
2398 C CA  . ASN A 283 ? 0.7515 0.7652 1.1297 0.0973  -0.2527 -0.1148 801 ASN A CA  
2399 C C   . ASN A 283 ? 0.6406 0.6456 1.1025 0.0848  -0.2452 -0.1208 801 ASN A C   
2400 O O   . ASN A 283 ? 0.6317 0.6152 1.0912 0.0864  -0.2716 -0.1496 801 ASN A O   
2401 C CB  . ASN A 283 ? 0.9213 0.9323 1.3033 0.1047  -0.3152 -0.1317 801 ASN A CB  
2402 C CG  . ASN A 283 ? 1.0459 1.0541 1.3232 0.1196  -0.3276 -0.1253 801 ASN A CG  
2403 O OD1 . ASN A 283 ? 1.0975 1.1082 1.3859 0.1254  -0.3568 -0.1112 801 ASN A OD1 
2404 N ND2 . ASN A 283 ? 1.0604 1.0651 1.2373 0.1270  -0.3043 -0.1331 801 ASN A ND2 
2405 N N   . HIS A 284 ? 0.5837 0.5993 1.1145 0.0736  -0.2090 -0.0929 802 HIS A N   
2406 C CA  . HIS A 284 ? 0.6066 0.6130 1.2191 0.0584  -0.1955 -0.0880 802 HIS A CA  
2407 C C   . HIS A 284 ? 0.5146 0.4913 1.0749 0.0624  -0.1792 -0.1001 802 HIS A C   
2408 O O   . HIS A 284 ? 0.5005 0.4804 0.9844 0.0739  -0.1532 -0.0978 802 HIS A O   
2409 C CB  . HIS A 284 ? 0.6112 0.6372 1.2840 0.0515  -0.1488 -0.0529 802 HIS A CB  
2410 C CG  . HIS A 284 ? 0.5411 0.5652 1.3096 0.0326  -0.1317 -0.0389 802 HIS A CG  
2411 N ND1 . HIS A 284 ? 0.5185 0.5117 1.2674 0.0273  -0.1015 -0.0310 802 HIS A ND1 
2412 C CD2 . HIS A 284 ? 0.4904 0.5423 1.3781 0.0168  -0.1386 -0.0271 802 HIS A CD2 
2413 C CE1 . HIS A 284 ? 0.4904 0.4846 1.3340 0.0068  -0.0879 -0.0120 802 HIS A CE1 
2414 N NE2 . HIS A 284 ? 0.4770 0.5120 1.4123 -0.0018 -0.1080 -0.0097 802 HIS A NE2 
2415 N N   . GLN A 285 ? 0.5443 0.4914 1.1506 0.0530  -0.1978 -0.1128 803 GLN A N   
2416 C CA  . GLN A 285 ? 0.5674 0.4780 1.1252 0.0636  -0.1912 -0.1274 803 GLN A CA  
2417 C C   . GLN A 285 ? 0.5846 0.4983 1.1106 0.0686  -0.1383 -0.1004 803 GLN A C   
2418 O O   . GLN A 285 ? 0.5324 0.4477 0.9862 0.0875  -0.1286 -0.1115 803 GLN A O   
2419 C CB  . GLN A 285 ? 0.6849 0.5492 1.3086 0.0484  -0.2169 -0.1370 803 GLN A CB  
2420 C CG  . GLN A 285 ? 0.6671 0.4825 1.2393 0.0659  -0.2156 -0.1535 803 GLN A CG  
2421 C CD  . GLN A 285 ? 0.7827 0.5975 1.2642 0.0978  -0.2410 -0.1966 803 GLN A CD  
2422 O OE1 . GLN A 285 ? 0.8764 0.6617 1.3508 0.1035  -0.2888 -0.2344 803 GLN A OE1 
2423 N NE2 . GLN A 285 ? 0.7496 0.5990 1.1614 0.1183  -0.2087 -0.1920 803 GLN A NE2 
2424 N N   . VAL A 286 ? 0.5671 0.4860 1.1479 0.0530  -0.1048 -0.0662 804 VAL A N   
2425 C CA  . VAL A 286 ? 0.5709 0.4868 1.1141 0.0586  -0.0585 -0.0412 804 VAL A CA  
2426 C C   . VAL A 286 ? 0.4675 0.4129 0.9378 0.0713  -0.0458 -0.0440 804 VAL A C   
2427 O O   . VAL A 286 ? 0.4585 0.4015 0.8720 0.0823  -0.0309 -0.0442 804 VAL A O   
2428 C CB  . VAL A 286 ? 0.6139 0.5336 1.2198 0.0430  -0.0205 -0.0047 804 VAL A CB  
2429 C CG1 . VAL A 286 ? 0.6517 0.5650 1.1971 0.0532  0.0238  0.0170  804 VAL A CG1 
2430 C CG2 . VAL A 286 ? 0.5225 0.4116 1.2046 0.0232  -0.0258 0.0064  804 VAL A CG2 
2431 N N   . ILE A 287 ? 0.4602 0.4318 0.9361 0.0689  -0.0552 -0.0449 805 ILE A N   
2432 C CA  . ILE A 287 ? 0.4602 0.4510 0.8700 0.0750  -0.0458 -0.0442 805 ILE A CA  
2433 C C   . ILE A 287 ? 0.5650 0.5656 0.9108 0.0858  -0.0617 -0.0681 805 ILE A C   
2434 O O   . ILE A 287 ? 0.5863 0.6020 0.8825 0.0884  -0.0438 -0.0653 805 ILE A O   
2435 C CB  . ILE A 287 ? 0.4272 0.4327 0.8537 0.0728  -0.0585 -0.0380 805 ILE A CB  
2436 C CG1 . ILE A 287 ? 0.4639 0.4707 0.9540 0.0692  -0.0335 -0.0146 805 ILE A CG1 
2437 C CG2 . ILE A 287 ? 0.4630 0.4763 0.8155 0.0750  -0.0546 -0.0360 805 ILE A CG2 
2438 C CD1 . ILE A 287 ? 0.4085 0.4021 0.8653 0.0714  0.0107  0.0020  805 ILE A CD1 
2439 N N   . GLN A 288 ? 0.5655 0.5596 0.9153 0.0926  -0.0953 -0.0932 806 GLN A N   
2440 C CA  . GLN A 288 ? 0.5356 0.5413 0.8240 0.1097  -0.1061 -0.1196 806 GLN A CA  
2441 C C   . GLN A 288 ? 0.4988 0.5034 0.7733 0.1211  -0.0867 -0.1221 806 GLN A C   
2442 O O   . GLN A 288 ? 0.5458 0.5822 0.7740 0.1338  -0.0769 -0.1321 806 GLN A O   
2443 C CB  . GLN A 288 ? 0.5483 0.5334 0.8388 0.1197  -0.1483 -0.1520 806 GLN A CB  
2444 C CG  . GLN A 288 ? 0.6493 0.6421 0.9316 0.1154  -0.1768 -0.1546 806 GLN A CG  
2445 C CD  . GLN A 288 ? 0.8991 0.8715 1.1547 0.1302  -0.2228 -0.1936 806 GLN A CD  
2446 O OE1 . GLN A 288 ? 1.0362 0.9827 1.2866 0.1434  -0.2333 -0.2209 806 GLN A OE1 
2447 N NE2 . GLN A 288 ? 1.0206 0.9976 1.2522 0.1312  -0.2542 -0.1982 806 GLN A NE2 
2448 N N   . TRP A 289 ? 0.4929 0.4637 0.8102 0.1170  -0.0807 -0.1101 807 TRP A N   
2449 C CA  . TRP A 289 ? 0.4995 0.4594 0.8018 0.1308  -0.0670 -0.1075 807 TRP A CA  
2450 C C   . TRP A 289 ? 0.4675 0.4525 0.7452 0.1251  -0.0374 -0.0847 807 TRP A C   
2451 O O   . TRP A 289 ? 0.4697 0.4725 0.7191 0.1393  -0.0319 -0.0890 807 TRP A O   
2452 C CB  . TRP A 289 ? 0.5278 0.4325 0.8746 0.1266  -0.0702 -0.0960 807 TRP A CB  
2453 C CG  . TRP A 289 ? 0.5789 0.4454 0.9400 0.1370  -0.1053 -0.1254 807 TRP A CG  
2454 C CD1 . TRP A 289 ? 0.6884 0.5632 1.0094 0.1626  -0.1278 -0.1638 807 TRP A CD1 
2455 C CD2 . TRP A 289 ? 0.6673 0.4773 1.0856 0.1222  -0.1219 -0.1205 807 TRP A CD2 
2456 N NE1 . TRP A 289 ? 0.6697 0.4872 1.0115 0.1680  -0.1619 -0.1880 807 TRP A NE1 
2457 C CE2 . TRP A 289 ? 0.6760 0.4520 1.0824 0.1397  -0.1612 -0.1608 807 TRP A CE2 
2458 C CE3 . TRP A 289 ? 0.6735 0.4589 1.1533 0.0950  -0.1053 -0.0855 807 TRP A CE3 
2459 C CZ2 . TRP A 289 ? 0.7662 0.4764 1.2225 0.1265  -0.1910 -0.1683 807 TRP A CZ2 
2460 C CZ3 . TRP A 289 ? 0.6747 0.4053 1.2124 0.0789  -0.1293 -0.0876 807 TRP A CZ3 
2461 C CH2 . TRP A 289 ? 0.7518 0.4413 1.2784 0.0927  -0.1750 -0.1293 807 TRP A CH2 
2462 N N   . PHE A 290 ? 0.4482 0.4336 0.7393 0.1065  -0.0218 -0.0631 808 PHE A N   
2463 C CA  . PHE A 290 ? 0.4525 0.4513 0.7128 0.1003  0.0010  -0.0470 808 PHE A CA  
2464 C C   . PHE A 290 ? 0.5504 0.5935 0.7718 0.1001  -0.0024 -0.0589 808 PHE A C   
2465 O O   . PHE A 290 ? 0.4699 0.5328 0.6684 0.1030  0.0041  -0.0585 808 PHE A O   
2466 C CB  . PHE A 290 ? 0.4188 0.4064 0.6973 0.0863  0.0163  -0.0279 808 PHE A CB  
2467 C CG  . PHE A 290 ? 0.5228 0.5111 0.7613 0.0810  0.0348  -0.0174 808 PHE A CG  
2468 C CD1 . PHE A 290 ? 0.4619 0.4286 0.6774 0.0863  0.0521  -0.0066 808 PHE A CD1 
2469 C CD2 . PHE A 290 ? 0.4866 0.4887 0.7032 0.0704  0.0317  -0.0180 808 PHE A CD2 
2470 C CE1 . PHE A 290 ? 0.5813 0.5410 0.7531 0.0817  0.0622  -0.0028 808 PHE A CE1 
2471 C CE2 . PHE A 290 ? 0.4580 0.4494 0.6383 0.0623  0.0434  -0.0113 808 PHE A CE2 
2472 C CZ  . PHE A 290 ? 0.5030 0.4737 0.6610 0.0682  0.0567  -0.0068 808 PHE A CZ  
2473 N N   . TRP A 291 ? 0.4383 0.4997 0.6532 0.0957  -0.0134 -0.0677 809 TRP A N   
2474 C CA  . TRP A 291 ? 0.4220 0.5276 0.6008 0.0909  -0.0091 -0.0720 809 TRP A CA  
2475 C C   . TRP A 291 ? 0.5704 0.7125 0.7405 0.1116  -0.0120 -0.0935 809 TRP A C   
2476 O O   . TRP A 291 ? 0.5856 0.7754 0.7436 0.1083  -0.0010 -0.0932 809 TRP A O   
2477 C CB  . TRP A 291 ? 0.4371 0.5462 0.5975 0.0827  -0.0179 -0.0701 809 TRP A CB  
2478 C CG  . TRP A 291 ? 0.4722 0.5515 0.6406 0.0663  -0.0133 -0.0474 809 TRP A CG  
2479 C CD1 . TRP A 291 ? 0.4750 0.5272 0.6717 0.0679  -0.0261 -0.0421 809 TRP A CD1 
2480 C CD2 . TRP A 291 ? 0.4598 0.5319 0.6130 0.0495  0.0032  -0.0303 809 TRP A CD2 
2481 N NE1 . TRP A 291 ? 0.5551 0.5856 0.7534 0.0582  -0.0150 -0.0224 809 TRP A NE1 
2482 C CE2 . TRP A 291 ? 0.4625 0.4975 0.6288 0.0464  0.0023  -0.0162 809 TRP A CE2 
2483 C CE3 . TRP A 291 ? 0.4748 0.5687 0.6082 0.0371  0.0149  -0.0278 809 TRP A CE3 
2484 C CZ2 . TRP A 291 ? 0.4836 0.4912 0.6333 0.0349  0.0140  -0.0023 809 TRP A CZ2 
2485 C CZ3 . TRP A 291 ? 0.4388 0.5051 0.5575 0.0192  0.0222  -0.0137 809 TRP A CZ3 
2486 C CH2 . TRP A 291 ? 0.5397 0.5578 0.6613 0.0199  0.0225  -0.0023 809 TRP A CH2 
2487 N N   . LYS A 292 ? 0.4524 0.5723 0.6352 0.1334  -0.0278 -0.1129 810 LYS A N   
2488 C CA  . LYS A 292 ? 0.4723 0.6173 0.6492 0.1622  -0.0314 -0.1360 810 LYS A CA  
2489 C C   . LYS A 292 ? 0.4829 0.6404 0.6701 0.1671  -0.0229 -0.1253 810 LYS A C   
2490 O O   . LYS A 292 ? 0.4609 0.6741 0.6463 0.1817  -0.0185 -0.1356 810 LYS A O   
2491 C CB  . LYS A 292 ? 0.5102 0.6059 0.6984 0.1844  -0.0550 -0.1590 810 LYS A CB  
2492 C CG  . LYS A 292 ? 0.5441 0.6517 0.7257 0.2229  -0.0613 -0.1859 810 LYS A CG  
2493 C CD  . LYS A 292 ? 0.6006 0.6478 0.7837 0.2446  -0.0898 -0.2151 810 LYS A CD  
2494 C CE  . LYS A 292 ? 0.7430 0.7933 0.9175 0.2901  -0.0963 -0.2434 810 LYS A CE  
2495 N NZ  . LYS A 292 ? 0.8838 0.8578 1.0561 0.3124  -0.1285 -0.2749 810 LYS A NZ  
2496 N N   . ALA A 293 ? 0.5237 0.6336 0.7213 0.1566  -0.0208 -0.1042 811 ALA A N   
2497 C CA  . ALA A 293 ? 0.5045 0.6146 0.6969 0.1632  -0.0179 -0.0928 811 ALA A CA  
2498 C C   . ALA A 293 ? 0.4352 0.5994 0.6162 0.1451  -0.0095 -0.0869 811 ALA A C   
2499 O O   . ALA A 293 ? 0.4594 0.6686 0.6444 0.1571  -0.0154 -0.0935 811 ALA A O   
2500 C CB  . ALA A 293 ? 0.4668 0.5118 0.6590 0.1549  -0.0112 -0.0687 811 ALA A CB  
2501 N N   . VAL A 294 ? 0.5040 0.6622 0.6762 0.1161  0.0009  -0.0746 812 VAL A N   
2502 C CA  . VAL A 294 ? 0.5098 0.7006 0.6709 0.0911  0.0063  -0.0667 812 VAL A CA  
2503 C C   . VAL A 294 ? 0.5077 0.7785 0.6820 0.0909  0.0077  -0.0785 812 VAL A C   
2504 O O   . VAL A 294 ? 0.4819 0.8004 0.6680 0.0822  0.0047  -0.0785 812 VAL A O   
2505 C CB  . VAL A 294 ? 0.5667 0.7265 0.7143 0.0639  0.0153  -0.0522 812 VAL A CB  
2506 C CG1 . VAL A 294 ? 0.5963 0.7820 0.7328 0.0343  0.0174  -0.0452 812 VAL A CG1 
2507 C CG2 . VAL A 294 ? 0.4465 0.5398 0.5887 0.0664  0.0208  -0.0403 812 VAL A CG2 
2508 N N   . LEU A 295 ? 0.6438 0.9320 0.8171 0.1015  0.0120  -0.0895 813 LEU A N   
2509 C CA  . LEU A 295 ? 0.6255 0.9932 0.8051 0.1056  0.0228  -0.1003 813 LEU A CA  
2510 C C   . LEU A 295 ? 0.6395 1.0633 0.8494 0.1350  0.0178  -0.1169 813 LEU A C   
2511 O O   . LEU A 295 ? 0.6380 1.1478 0.8718 0.1312  0.0297  -0.1200 813 LEU A O   
2512 C CB  . LEU A 295 ? 0.6725 1.0332 0.8283 0.1218  0.0252  -0.1140 813 LEU A CB  
2513 C CG  . LEU A 295 ? 0.8021 1.2365 0.9430 0.1204  0.0461  -0.1181 813 LEU A CG  
2514 C CD1 . LEU A 295 ? 0.9036 1.3454 1.0303 0.0748  0.0602  -0.0875 813 LEU A CD1 
2515 C CD2 . LEU A 295 ? 0.8688 1.2840 0.9715 0.1483  0.0415  -0.1400 813 LEU A CD2 
2516 N N   . MET A 296 ? 0.5894 0.9676 0.8030 0.1646  0.0006  -0.1252 814 MET A N   
2517 C CA  . MET A 296 ? 0.6413 1.0657 0.8820 0.2006  -0.0094 -0.1410 814 MET A CA  
2518 C C   . MET A 296 ? 0.6377 1.0570 0.8872 0.1958  -0.0263 -0.1278 814 MET A C   
2519 O O   . MET A 296 ? 0.6465 1.0943 0.9170 0.2286  -0.0426 -0.1373 814 MET A O   
2520 C CB  . MET A 296 ? 0.6534 1.0287 0.8872 0.2449  -0.0218 -0.1617 814 MET A CB  
2521 C CG  . MET A 296 ? 0.6915 0.9701 0.9124 0.2508  -0.0387 -0.1491 814 MET A CG  
2522 S SD  . MET A 296 ? 0.7830 1.0063 1.0051 0.3034  -0.0587 -0.1739 814 MET A SD  
2523 C CE  . MET A 296 ? 0.6952 0.9085 0.9021 0.2978  -0.0526 -0.1971 814 MET A CE  
2524 N N   . MET A 297 ? 0.5998 0.9808 0.8283 0.1589  -0.0252 -0.1077 815 MET A N   
2525 C CA  . MET A 297 ? 0.5932 0.9715 0.8170 0.1514  -0.0433 -0.0989 815 MET A CA  
2526 C C   . MET A 297 ? 0.5759 1.0497 0.8393 0.1278  -0.0468 -0.1023 815 MET A C   
2527 O O   . MET A 297 ? 0.5096 1.0295 0.7902 0.1011  -0.0265 -0.1004 815 MET A O   
2528 C CB  . MET A 297 ? 0.6113 0.9068 0.7905 0.1258  -0.0398 -0.0810 815 MET A CB  
2529 C CG  . MET A 297 ? 0.6309 0.8404 0.7827 0.1449  -0.0345 -0.0720 815 MET A CG  
2530 S SD  . MET A 297 ? 0.7328 0.8627 0.8387 0.1205  -0.0211 -0.0520 815 MET A SD  
2531 C CE  . MET A 297 ? 0.8490 1.0122 0.9641 0.0800  -0.0131 -0.0539 815 MET A CE  
2532 N N   . ASP A 298 ? 0.6404 1.1436 0.9191 0.1363  -0.0740 -0.1052 816 ASP A N   
2533 C CA  . ASP A 298 ? 0.6973 1.2892 1.0240 0.1059  -0.0850 -0.1072 816 ASP A CA  
2534 C C   . ASP A 298 ? 0.7091 1.2594 1.0088 0.0510  -0.0806 -0.0942 816 ASP A C   
2535 O O   . ASP A 298 ? 0.7222 1.1735 0.9616 0.0467  -0.0765 -0.0859 816 ASP A O   
2536 C CB  . ASP A 298 ? 0.7438 1.3625 1.0863 0.1288  -0.1263 -0.1142 816 ASP A CB  
2537 C CG  . ASP A 298 ? 0.8988 1.5706 1.2804 0.1861  -0.1344 -0.1279 816 ASP A CG  
2538 O OD1 . ASP A 298 ? 0.8997 1.6420 1.3266 0.1981  -0.1085 -0.1381 816 ASP A OD1 
2539 O OD2 . ASP A 298 ? 1.0039 1.6415 1.3639 0.2227  -0.1668 -0.1285 816 ASP A OD2 
2540 N N   . SER A 299 ? 0.6928 1.3181 1.0412 0.0096  -0.0802 -0.0918 817 SER A N   
2541 C CA  . SER A 299 ? 0.6937 1.2728 1.0192 -0.0444 -0.0821 -0.0805 817 SER A CA  
2542 C C   . SER A 299 ? 0.7093 1.2002 0.9765 -0.0423 -0.1145 -0.0855 817 SER A C   
2543 O O   . SER A 299 ? 0.7462 1.1461 0.9572 -0.0609 -0.1090 -0.0793 817 SER A O   
2544 C CB  . SER A 299 ? 0.7850 1.4617 1.1832 -0.0923 -0.0852 -0.0764 817 SER A CB  
2545 O OG  . SER A 299 ? 0.8047 1.5559 1.2418 -0.0994 -0.0453 -0.0666 817 SER A OG  
2546 N N   . GLU A 300 ? 0.6745 1.1916 0.9499 -0.0145 -0.1483 -0.0972 818 GLU A N   
2547 C CA  . GLU A 300 ? 0.8291 1.2616 1.0324 -0.0025 -0.1794 -0.1022 818 GLU A CA  
2548 C C   . GLU A 300 ? 0.8709 1.1947 0.9949 0.0259  -0.1546 -0.0924 818 GLU A C   
2549 O O   . GLU A 300 ? 0.9069 1.1434 0.9613 0.0183  -0.1570 -0.0916 818 GLU A O   
2550 C CB  . GLU A 300 ? 0.9300 1.4136 1.1532 0.0316  -0.2216 -0.1129 818 GLU A CB  
2551 C CG  . GLU A 300 ? 1.0679 1.4562 1.1977 0.0717  -0.2412 -0.1109 818 GLU A CG  
2552 C CD  . GLU A 300 ? 1.2261 1.5295 1.2739 0.0494  -0.2634 -0.1168 818 GLU A CD  
2553 O OE1 . GLU A 300 ? 1.3021 1.5277 1.2615 0.0816  -0.2758 -0.1137 818 GLU A OE1 
2554 O OE2 . GLU A 300 ? 1.2876 1.5950 1.3526 0.0011  -0.2675 -0.1241 818 GLU A OE2 
2555 N N   . LYS A 301 ? 0.8000 1.1303 0.9377 0.0585  -0.1306 -0.0865 819 LYS A N   
2556 C CA  . LYS A 301 ? 0.7156 0.9543 0.7969 0.0818  -0.1080 -0.0750 819 LYS A CA  
2557 C C   . LYS A 301 ? 0.6297 0.8259 0.7001 0.0553  -0.0767 -0.0672 819 LYS A C   
2558 O O   . LYS A 301 ? 0.5971 0.7142 0.6175 0.0601  -0.0620 -0.0588 819 LYS A O   
2559 C CB  . LYS A 301 ? 0.7176 0.9690 0.8215 0.1220  -0.1001 -0.0733 819 LYS A CB  
2560 C CG  . LYS A 301 ? 0.8478 1.0694 0.9178 0.1612  -0.1250 -0.0694 819 LYS A CG  
2561 C CD  . LYS A 301 ? 0.9358 1.2288 1.0318 0.1655  -0.1666 -0.0822 819 LYS A CD  
2562 C CE  . LYS A 301 ? 1.0394 1.2844 1.0781 0.2030  -0.1982 -0.0749 819 LYS A CE  
2563 N NZ  . LYS A 301 ? 1.0690 1.2092 1.0114 0.1964  -0.1875 -0.0606 819 LYS A NZ  
2564 N N   . ARG A 302 ? 0.6319 0.8831 0.7489 0.0300  -0.0653 -0.0682 820 ARG A N   
2565 C CA  . ARG A 302 ? 0.6220 0.8339 0.7271 0.0041  -0.0432 -0.0589 820 ARG A CA  
2566 C C   . ARG A 302 ? 0.7168 0.8640 0.7768 -0.0202 -0.0527 -0.0589 820 ARG A C   
2567 O O   . ARG A 302 ? 0.5903 0.6657 0.6142 -0.0173 -0.0365 -0.0527 820 ARG A O   
2568 C CB  . ARG A 302 ? 0.4770 0.7594 0.6280 -0.0212 -0.0320 -0.0561 820 ARG A CB  
2569 C CG  . ARG A 302 ? 0.4698 0.7987 0.6482 0.0062  -0.0170 -0.0599 820 ARG A CG  
2570 C CD  . ARG A 302 ? 0.5054 0.8982 0.7108 -0.0181 0.0001  -0.0544 820 ARG A CD  
2571 N NE  . ARG A 302 ? 0.5927 1.0459 0.8217 0.0130  0.0116  -0.0658 820 ARG A NE  
2572 C CZ  . ARG A 302 ? 0.6088 1.1406 0.8624 0.0031  0.0307  -0.0646 820 ARG A CZ  
2573 N NH1 . ARG A 302 ? 0.6113 1.1702 0.8751 -0.0433 0.0403  -0.0468 820 ARG A NH1 
2574 N NH2 . ARG A 302 ? 0.5856 1.1651 0.8505 0.0396  0.0416  -0.0806 820 ARG A NH2 
2575 N N   . ILE A 303 ? 0.7872 0.9614 0.8533 -0.0423 -0.0813 -0.0685 821 ILE A N   
2576 C CA  . ILE A 303 ? 0.8623 0.9678 0.8788 -0.0641 -0.0991 -0.0758 821 ILE A CA  
2577 C C   . ILE A 303 ? 0.8656 0.8870 0.8055 -0.0291 -0.0960 -0.0793 821 ILE A C   
2578 O O   . ILE A 303 ? 0.9073 0.8498 0.7982 -0.0301 -0.0829 -0.0798 821 ILE A O   
2579 C CB  . ILE A 303 ? 0.8823 1.0362 0.9240 -0.0924 -0.1407 -0.0896 821 ILE A CB  
2580 C CG1 . ILE A 303 ? 0.8561 1.0817 0.9708 -0.1402 -0.1367 -0.0812 821 ILE A CG1 
2581 C CG2 . ILE A 303 ? 0.9496 1.0153 0.9197 -0.1029 -0.1686 -0.1054 821 ILE A CG2 
2582 C CD1 . ILE A 303 ? 0.9419 1.0967 1.0327 -0.1774 -0.1258 -0.0719 821 ILE A CD1 
2583 N N   . ARG A 304 ? 0.7511 0.7883 0.6790 0.0047  -0.1052 -0.0798 822 ARG A N   
2584 C CA  . ARG A 304 ? 0.8210 0.7812 0.6681 0.0369  -0.0994 -0.0779 822 ARG A CA  
2585 C C   . ARG A 304 ? 0.8091 0.7234 0.6472 0.0548  -0.0534 -0.0611 822 ARG A C   
2586 O O   . ARG A 304 ? 0.9344 0.7788 0.7087 0.0706  -0.0353 -0.0585 822 ARG A O   
2587 C CB  . ARG A 304 ? 0.8795 0.8625 0.7121 0.0684  -0.1232 -0.0767 822 ARG A CB  
2588 C CG  . ARG A 304 ? 1.0522 0.9561 0.7796 0.0926  -0.1327 -0.0782 822 ARG A CG  
2589 C CD  . ARG A 304 ? 1.1856 1.1147 0.8899 0.1099  -0.1830 -0.0862 822 ARG A CD  
2590 N NE  . ARG A 304 ? 1.2335 1.1931 0.9653 0.1432  -0.1810 -0.0690 822 ARG A NE  
2591 C CZ  . ARG A 304 ? 1.2913 1.2630 0.9986 0.1719  -0.2209 -0.0685 822 ARG A CZ  
2592 N NH1 . ARG A 304 ? 1.3281 1.2898 0.9821 0.1700  -0.2688 -0.0855 822 ARG A NH1 
2593 N NH2 . ARG A 304 ? 1.2783 1.2658 1.0118 0.2044  -0.2175 -0.0521 822 ARG A NH2 
2594 N N   . LEU A 305 ? 0.6880 0.6441 0.5906 0.0531  -0.0348 -0.0513 823 LEU A N   
2595 C CA  . LEU A 305 ? 0.6769 0.5985 0.5878 0.0633  0.0015  -0.0375 823 LEU A CA  
2596 C C   . LEU A 305 ? 0.6588 0.5369 0.5528 0.0468  0.0134  -0.0402 823 LEU A C   
2597 O O   . LEU A 305 ? 0.7685 0.5949 0.6346 0.0628  0.0390  -0.0343 823 LEU A O   
2598 C CB  . LEU A 305 ? 0.7669 0.7391 0.7452 0.0630  0.0087  -0.0324 823 LEU A CB  
2599 C CG  . LEU A 305 ? 0.6803 0.6314 0.6852 0.0637  0.0346  -0.0222 823 LEU A CG  
2600 C CD1 . LEU A 305 ? 0.6457 0.5491 0.6349 0.0856  0.0595  -0.0082 823 LEU A CD1 
2601 C CD2 . LEU A 305 ? 0.6458 0.6465 0.7040 0.0629  0.0304  -0.0243 823 LEU A CD2 
2602 N N   . LEU A 306 ? 0.7317 0.6318 0.6456 0.0157  -0.0037 -0.0475 824 LEU A N   
2603 C CA  . LEU A 306 ? 0.7874 0.6358 0.6812 -0.0016 -0.0005 -0.0502 824 LEU A CA  
2604 C C   . LEU A 306 ? 0.9399 0.7139 0.7574 0.0105  -0.0044 -0.0642 824 LEU A C   
2605 O O   . LEU A 306 ? 0.9030 0.6157 0.6911 0.0226  0.0146  -0.0657 824 LEU A O   
2606 C CB  . LEU A 306 ? 0.8538 0.7357 0.7769 -0.0428 -0.0218 -0.0518 824 LEU A CB  
2607 C CG  . LEU A 306 ? 0.9558 0.7999 0.8834 -0.0628 -0.0145 -0.0425 824 LEU A CG  
2608 C CD1 . LEU A 306 ? 0.8258 0.6733 0.7787 -0.0402 0.0105  -0.0282 824 LEU A CD1 
2609 C CD2 . LEU A 306 ? 1.0622 0.9528 1.0243 -0.1067 -0.0292 -0.0353 824 LEU A CD2 
2610 N N   . GLN A 307 ? 1.0125 0.7930 0.7952 0.0117  -0.0308 -0.0764 825 GLN A N   
2611 C CA  . GLN A 307 ? 1.1304 0.8392 0.8235 0.0264  -0.0412 -0.0938 825 GLN A CA  
2612 C C   . GLN A 307 ? 1.0959 0.7599 0.7425 0.0683  0.0009  -0.0834 825 GLN A C   
2613 O O   . GLN A 307 ? 1.0755 0.6691 0.6591 0.0848  0.0171  -0.0941 825 GLN A O   
2614 C CB  . GLN A 307 ? 1.2179 0.9554 0.8887 0.0235  -0.0837 -0.1059 825 GLN A CB  
2615 C CG  . GLN A 307 ? 1.3423 1.0280 0.9507 0.0067  -0.1251 -0.1342 825 GLN A CG  
2616 C CD  . GLN A 307 ? 1.3677 1.1096 0.9897 -0.0054 -0.1773 -0.1453 825 GLN A CD  
2617 O OE1 . GLN A 307 ? 1.2080 1.0298 0.8891 0.0020  -0.1791 -0.1313 825 GLN A OE1 
2618 N NE2 . GLN A 307 ? 1.5017 1.2013 1.0714 -0.0219 -0.2237 -0.1730 825 GLN A NE2 
2619 N N   . PHE A 308 ? 0.9598 0.6650 0.6409 0.0851  0.0201  -0.0625 826 PHE A N   
2620 C CA  . PHE A 308 ? 0.9785 0.6548 0.6332 0.1178  0.0633  -0.0445 826 PHE A CA  
2621 C C   . PHE A 308 ? 0.9699 0.6255 0.6537 0.1240  0.1025  -0.0388 826 PHE A C   
2622 O O   . PHE A 308 ? 0.9962 0.6060 0.6309 0.1499  0.1370  -0.0371 826 PHE A O   
2623 C CB  . PHE A 308 ? 0.9173 0.6408 0.6223 0.1251  0.0691  -0.0224 826 PHE A CB  
2624 C CG  . PHE A 308 ? 0.9445 0.6447 0.6435 0.1488  0.1152  0.0030  826 PHE A CG  
2625 C CD1 . PHE A 308 ? 1.0554 0.7046 0.6628 0.1741  0.1341  0.0115  826 PHE A CD1 
2626 C CD2 . PHE A 308 ? 0.8795 0.6100 0.6642 0.1440  0.1387  0.0197  826 PHE A CD2 
2627 C CE1 . PHE A 308 ? 1.1316 0.7647 0.7392 0.1914  0.1835  0.0412  826 PHE A CE1 
2628 C CE2 . PHE A 308 ? 0.8552 0.5708 0.6506 0.1586  0.1810  0.0459  826 PHE A CE2 
2629 C CZ  . PHE A 308 ? 1.0126 0.6818 0.7226 0.1809  0.2073  0.0593  826 PHE A CZ  
2630 N N   . VAL A 309 ? 0.8578 0.5497 0.6196 0.1034  0.0971  -0.0358 827 VAL A N   
2631 C CA  . VAL A 309 ? 0.9040 0.5880 0.7090 0.1121  0.1272  -0.0275 827 VAL A CA  
2632 C C   . VAL A 309 ? 0.9703 0.5946 0.7340 0.1147  0.1254  -0.0453 827 VAL A C   
2633 O O   . VAL A 309 ? 1.0431 0.6380 0.8029 0.1409  0.1583  -0.0441 827 VAL A O   
2634 C CB  . VAL A 309 ? 0.7669 0.5057 0.6594 0.0934  0.1171  -0.0173 827 VAL A CB  
2635 C CG1 . VAL A 309 ? 0.7616 0.4934 0.7005 0.1050  0.1397  -0.0093 827 VAL A CG1 
2636 C CG2 . VAL A 309 ? 0.7263 0.5118 0.6575 0.0951  0.1176  -0.0045 827 VAL A CG2 
2637 N N   . THR A 310 ? 0.9361 0.5424 0.6734 0.0881  0.0871  -0.0620 828 THR A N   
2638 C CA  . THR A 310 ? 1.0848 0.6222 0.7849 0.0845  0.0769  -0.0794 828 THR A CA  
2639 C C   . THR A 310 ? 1.2627 0.7268 0.8605 0.1042  0.0739  -0.1053 828 THR A C   
2640 O O   . THR A 310 ? 1.2788 0.6723 0.8333 0.1255  0.0857  -0.1212 828 THR A O   
2641 C CB  . THR A 310 ? 1.0813 0.6287 0.8070 0.0387  0.0369  -0.0814 828 THR A CB  
2642 O OG1 . THR A 310 ? 0.9673 0.5704 0.7697 0.0270  0.0431  -0.0587 828 THR A OG1 
2643 C CG2 . THR A 310 ? 1.2403 0.6994 0.9217 0.0306  0.0204  -0.0986 828 THR A CG2 
2644 N N   . GLY A 311 ? 1.3449 0.8226 0.8990 0.1018  0.0561  -0.1112 829 GLY A N   
2645 C CA  . GLY A 311 ? 1.5301 0.9376 0.9742 0.1177  0.0411  -0.1389 829 GLY A CA  
2646 C C   . GLY A 311 ? 1.7069 1.1052 1.1358 0.0773  -0.0207 -0.1610 829 GLY A C   
2647 O O   . GLY A 311 ? 1.8216 1.1776 1.1656 0.0831  -0.0502 -0.1853 829 GLY A O   
2648 N N   . THR A 312 ? 1.7535 1.1936 1.2655 0.0352  -0.0406 -0.1514 830 THR A N   
2649 C CA  . THR A 312 ? 1.8373 1.2873 1.3631 -0.0127 -0.0947 -0.1656 830 THR A CA  
2650 C C   . THR A 312 ? 1.7796 1.3372 1.4089 -0.0458 -0.1006 -0.1410 830 THR A C   
2651 O O   . THR A 312 ? 1.7073 1.3107 1.3913 -0.0351 -0.0669 -0.1167 830 THR A O   
2652 C CB  . THR A 312 ? 1.9055 1.2710 1.4133 -0.0384 -0.1142 -0.1821 830 THR A CB  
2653 O OG1 . THR A 312 ? 1.7812 1.1473 1.3423 -0.0372 -0.0825 -0.1586 830 THR A OG1 
2654 C CG2 . THR A 312 ? 2.0604 1.3124 1.4541 -0.0044 -0.1177 -0.2169 830 THR A CG2 
2655 N N   . SER A 313 ? 1.7874 1.3875 1.4449 -0.0848 -0.1441 -0.1495 831 SER A N   
2656 C CA  . SER A 313 ? 1.6493 1.3602 1.4032 -0.1125 -0.1468 -0.1295 831 SER A CA  
2657 C C   . SER A 313 ? 1.5844 1.3040 1.3942 -0.1616 -0.1481 -0.1159 831 SER A C   
2658 O O   . SER A 313 ? 1.4799 1.2872 1.3636 -0.1807 -0.1370 -0.0954 831 SER A O   
2659 C CB  . SER A 313 ? 1.6512 1.4254 1.4211 -0.1237 -0.1897 -0.1427 831 SER A CB  
2660 O OG  . SER A 313 ? 1.7317 1.4536 1.4645 -0.1533 -0.2372 -0.1692 831 SER A OG  
2661 N N   . ARG A 314 ? 1.6033 1.2255 1.3705 -0.1792 -0.1604 -0.1268 832 ARG A N   
2662 C CA  . ARG A 314 ? 1.5232 1.1313 1.3302 -0.2297 -0.1661 -0.1107 832 ARG A CA  
2663 C C   . ARG A 314 ? 1.4536 1.0807 1.2931 -0.2191 -0.1252 -0.0785 832 ARG A C   
2664 O O   . ARG A 314 ? 1.4153 0.9948 1.2227 -0.1763 -0.0994 -0.0769 832 ARG A O   
2665 C CB  . ARG A 314 ? 1.5555 1.0320 1.2978 -0.2436 -0.1920 -0.1324 832 ARG A CB  
2666 N N   . VAL A 315 ? 1.4502 1.1524 1.3545 -0.2575 -0.1196 -0.0529 833 VAL A N   
2667 C CA  . VAL A 315 ? 1.4590 1.1732 1.3827 -0.2522 -0.0885 -0.0224 833 VAL A CA  
2668 C C   . VAL A 315 ? 1.6221 1.2439 1.5243 -0.2860 -0.0972 -0.0069 833 VAL A C   
2669 O O   . VAL A 315 ? 1.6712 1.2872 1.5918 -0.3414 -0.1187 -0.0015 833 VAL A O   
2670 C CB  . VAL A 315 ? 1.3695 1.2079 1.3585 -0.2699 -0.0728 -0.0019 833 VAL A CB  
2671 C CG1 . VAL A 315 ? 1.3400 1.1823 1.3307 -0.2589 -0.0449 0.0262  833 VAL A CG1 
2672 C CG2 . VAL A 315 ? 1.2640 1.1836 1.2746 -0.2358 -0.0706 -0.0188 833 VAL A CG2 
2673 N N   . PRO A 316 ? 1.7083 1.2562 1.5765 -0.2532 -0.0828 0.0015  834 PRO A N   
2674 C CA  . PRO A 316 ? 1.8197 1.2596 1.6578 -0.2744 -0.0940 0.0161  834 PRO A CA  
2675 C C   . PRO A 316 ? 1.7196 1.1892 1.5885 -0.3290 -0.0909 0.0568  834 PRO A C   
2676 O O   . PRO A 316 ? 1.6605 1.2227 1.5614 -0.3269 -0.0676 0.0792  834 PRO A O   
2677 C CB  . PRO A 316 ? 1.8360 1.2280 1.6501 -0.2159 -0.0752 0.0193  834 PRO A CB  
2678 C CG  . PRO A 316 ? 1.7285 1.2258 1.5783 -0.1831 -0.0508 0.0205  834 PRO A CG  
2679 C CD  . PRO A 316 ? 1.6832 1.2466 1.5470 -0.1939 -0.0573 -0.0012 834 PRO A CD  
2680 N N   . MET A 317 ? 1.7507 1.1369 1.6051 -0.3777 -0.1136 0.0660  835 MET A N   
2681 C CA  . MET A 317 ? 1.7078 1.1038 1.5833 -0.4347 -0.1075 0.1117  835 MET A CA  
2682 C C   . MET A 317 ? 1.7376 1.1108 1.5862 -0.4040 -0.0859 0.1462  835 MET A C   
2683 O O   . MET A 317 ? 1.7876 1.0919 1.6003 -0.3493 -0.0882 0.1343  835 MET A O   
2684 C CB  . MET A 317 ? 1.7879 1.0698 1.6468 -0.4910 -0.1400 0.1149  835 MET A CB  
2685 C CG  . MET A 317 ? 1.8061 1.1179 1.7002 -0.5556 -0.1292 0.1630  835 MET A CG  
2686 S SD  . MET A 317 ? 1.9523 1.2100 1.8715 -0.6080 -0.1625 0.1481  835 MET A SD  
2687 C CE  . MET A 317 ? 1.8251 1.2021 1.8075 -0.6313 -0.1821 0.1083  835 MET A CE  
2688 N N   . ASN A 318 ? 1.6956 1.1325 1.5622 -0.4373 -0.0650 0.1885  836 ASN A N   
2689 C CA  . ASN A 318 ? 1.6531 1.0859 1.4886 -0.4082 -0.0474 0.2219  836 ASN A CA  
2690 C C   . ASN A 318 ? 1.5213 1.0195 1.3640 -0.3403 -0.0358 0.1967  836 ASN A C   
2691 O O   . ASN A 318 ? 1.5539 1.0205 1.3694 -0.2990 -0.0357 0.2078  836 ASN A O   
2692 C CB  . ASN A 318 ? 1.7605 1.0415 1.5401 -0.4007 -0.0673 0.2427  836 ASN A CB  
2693 C CG  . ASN A 318 ? 1.9023 1.1179 1.6758 -0.4671 -0.0764 0.2736  836 ASN A CG  
2694 O OD1 . ASN A 318 ? 1.8743 1.1744 1.6835 -0.5180 -0.0573 0.2970  836 ASN A OD1 
2695 N ND2 . ASN A 318 ? 2.0434 1.1370 1.7874 -0.4499 -0.0992 0.2645  836 ASN A ND2 
2696 N N   . GLY A 319 ? 1.2954 0.8826 1.1785 -0.3306 -0.0300 0.1636  837 GLY A N   
2697 C CA  . GLY A 319 ? 1.0875 0.7471 0.9862 -0.2782 -0.0170 0.1441  837 GLY A CA  
2698 C C   . GLY A 319 ? 0.9588 0.5667 0.8472 -0.2234 -0.0245 0.1160  837 GLY A C   
2699 O O   . GLY A 319 ? 1.0198 0.5349 0.8838 -0.2177 -0.0387 0.1039  837 GLY A O   
2700 N N   . PHE A 320 ? 0.9107 0.5799 0.8189 -0.1826 -0.0130 0.1054  838 PHE A N   
2701 C CA  . PHE A 320 ? 0.9096 0.5561 0.8243 -0.1330 -0.0117 0.0816  838 PHE A CA  
2702 C C   . PHE A 320 ? 0.9126 0.4907 0.8141 -0.1011 -0.0180 0.0933  838 PHE A C   
2703 O O   . PHE A 320 ? 0.9163 0.4735 0.8302 -0.0607 -0.0135 0.0764  838 PHE A O   
2704 C CB  . PHE A 320 ? 0.7581 0.4944 0.7084 -0.1076 0.0008  0.0682  838 PHE A CB  
2705 C CG  . PHE A 320 ? 0.8195 0.6154 0.7860 -0.1222 0.0041  0.0506  838 PHE A CG  
2706 C CD1 . PHE A 320 ? 0.8786 0.6701 0.8474 -0.0980 0.0067  0.0271  838 PHE A CD1 
2707 C CD2 . PHE A 320 ? 0.8561 0.7157 0.8358 -0.1577 0.0056  0.0595  838 PHE A CD2 
2708 C CE1 . PHE A 320 ? 0.8203 0.6625 0.7994 -0.1071 0.0033  0.0124  838 PHE A CE1 
2709 C CE2 . PHE A 320 ? 0.8542 0.7756 0.8584 -0.1665 0.0040  0.0425  838 PHE A CE2 
2710 C CZ  . PHE A 320 ? 0.8447 0.7536 0.8461 -0.1400 -0.0008 0.0188  838 PHE A CZ  
2711 N N   . ALA A 321 ? 0.9556 0.5029 0.8334 -0.1177 -0.0274 0.1245  839 ALA A N   
2712 C CA  . ALA A 321 ? 1.0014 0.4742 0.8627 -0.0876 -0.0413 0.1394  839 ALA A CA  
2713 C C   . ALA A 321 ? 1.1073 0.4766 0.9486 -0.0762 -0.0492 0.1258  839 ALA A C   
2714 O O   . ALA A 321 ? 1.1634 0.4778 1.0053 -0.0347 -0.0571 0.1260  839 ALA A O   
2715 C CB  . ALA A 321 ? 1.0670 0.5158 0.8902 -0.1120 -0.0517 0.1806  839 ALA A CB  
2716 N N   . GLU A 322 ? 1.1050 0.4484 0.9295 -0.1102 -0.0498 0.1112  840 GLU A N   
2717 C CA  . GLU A 322 ? 1.2894 0.5207 1.0801 -0.1027 -0.0618 0.0934  840 GLU A CA  
2718 C C   . GLU A 322 ? 1.2662 0.5072 1.0555 -0.0857 -0.0525 0.0514  840 GLU A C   
2719 O O   . GLU A 322 ? 1.3389 0.4957 1.0890 -0.0926 -0.0654 0.0297  840 GLU A O   
2720 C CB  . GLU A 322 ? 1.2961 0.4549 1.0533 -0.1614 -0.0812 0.1126  840 GLU A CB  
2721 C CG  . GLU A 322 ? 1.3686 0.4865 1.1066 -0.1767 -0.0902 0.1596  840 GLU A CG  
2722 C CD  . GLU A 322 ? 1.6964 0.7200 1.4012 -0.2355 -0.1084 0.1804  840 GLU A CD  
2723 O OE1 . GLU A 322 ? 1.7302 0.7290 1.4344 -0.2652 -0.1178 0.1533  840 GLU A OE1 
2724 O OE2 . GLU A 322 ? 1.8773 0.8498 1.5558 -0.2522 -0.1156 0.2240  840 GLU A OE2 
2725 N N   . LEU A 323 ? 1.1325 0.4683 0.9573 -0.0629 -0.0323 0.0403  841 LEU A N   
2726 C CA  . LEU A 323 ? 1.1301 0.4788 0.9464 -0.0420 -0.0198 0.0072  841 LEU A CA  
2727 C C   . LEU A 323 ? 1.2067 0.4785 0.9980 0.0099  -0.0095 -0.0133 841 LEU A C   
2728 O O   . LEU A 323 ? 1.1545 0.4244 0.9744 0.0476  0.0003  -0.0028 841 LEU A O   
2729 C CB  . LEU A 323 ? 0.9820 0.4401 0.8436 -0.0278 0.0002  0.0079  841 LEU A CB  
2730 C CG  . LEU A 323 ? 0.9743 0.4656 0.8285 -0.0122 0.0145  -0.0157 841 LEU A CG  
2731 C CD1 . LEU A 323 ? 1.0585 0.5435 0.8806 -0.0502 -0.0062 -0.0299 841 LEU A CD1 
2732 C CD2 . LEU A 323 ? 0.8170 0.4051 0.7225 -0.0026 0.0296  -0.0064 841 LEU A CD2 
2733 N N   . TYR A 324 ? 1.1899 0.4021 0.9285 0.0150  -0.0124 -0.0443 842 TYR A N   
2734 C CA  . TYR A 324 ? 1.3142 0.4589 1.0206 0.0710  0.0050  -0.0687 842 TYR A CA  
2735 C C   . TYR A 324 ? 1.3719 0.5685 1.0740 0.1066  0.0393  -0.0865 842 TYR A C   
2736 O O   . TYR A 324 ? 1.1901 0.4301 0.8768 0.0850  0.0368  -0.0936 842 TYR A O   
2737 C CB  . TYR A 324 ? 1.3978 0.4152 1.0289 0.0624  -0.0212 -0.0954 842 TYR A CB  
2738 C CG  . TYR A 324 ? 1.4794 0.4036 1.1059 0.0714  -0.0380 -0.0830 842 TYR A CG  
2739 C CD1 . TYR A 324 ? 1.4634 0.3994 1.1232 0.0320  -0.0570 -0.0437 842 TYR A CD1 
2740 C CD2 . TYR A 324 ? 1.5881 0.4349 1.1839 0.1207  -0.0327 -0.1076 842 TYR A CD2 
2741 C CE1 . TYR A 324 ? 1.5403 0.3916 1.1927 0.0416  -0.0743 -0.0267 842 TYR A CE1 
2742 C CE2 . TYR A 324 ? 1.6421 0.4389 1.2541 0.1293  -0.0483 -0.0928 842 TYR A CE2 
2743 C CZ  . TYR A 324 ? 1.6234 0.4203 1.2622 0.0903  -0.0697 -0.0515 842 TYR A CZ  
2744 O OH  . TYR A 324 ? 1.7114 0.4526 1.3579 0.1013  -0.0852 -0.0338 842 TYR A OH  
2745 N N   . GLY A 325 ? 1.4585 0.6521 1.1772 0.1623  0.0721  -0.0908 843 GLY A N   
2746 C CA  . GLY A 325 ? 1.5097 0.7350 1.2133 0.1993  0.1122  -0.1051 843 GLY A CA  
2747 C C   . GLY A 325 ? 1.6627 0.7869 1.2715 0.2317  0.1181  -0.1427 843 GLY A C   
2748 O O   . GLY A 325 ? 1.7477 0.7890 1.2902 0.2058  0.0806  -0.1634 843 GLY A O   
2749 N N   . SER A 326 ? 1.5858 0.7163 1.1887 0.2884  0.1658  -0.1525 844 SER A N   
2750 C CA  . SER A 326 ? 1.6112 0.6839 1.1327 0.3180  0.1730  -0.1860 844 SER A CA  
2751 C C   . SER A 326 ? 1.5908 0.6238 1.1347 0.3481  0.1679  -0.1957 844 SER A C   
2752 O O   . SER A 326 ? 1.7250 0.6817 1.1978 0.3611  0.1547  -0.2268 844 SER A O   
2753 C CB  . SER A 326 ? 1.5308 0.6632 1.0369 0.3520  0.2269  -0.1849 844 SER A CB  
2754 O OG  . SER A 326 ? 1.7182 0.7958 1.1344 0.3812  0.2348  -0.2164 844 SER A OG  
2755 N N   . ASN A 327 ? 1.5245 0.6074 1.1670 0.3603  0.1743  -0.1702 845 ASN A N   
2756 C CA  . ASN A 327 ? 1.6175 0.6733 1.2939 0.3955  0.1698  -0.1769 845 ASN A CA  
2757 C C   . ASN A 327 ? 1.6457 0.6681 1.3660 0.3722  0.1259  -0.1551 845 ASN A C   
2758 O O   . ASN A 327 ? 1.7430 0.7706 1.5217 0.4035  0.1230  -0.1485 845 ASN A O   
2759 C CB  . ASN A 327 ? 1.5854 0.7370 1.3450 0.4428  0.2172  -0.1678 845 ASN A CB  
2760 C CG  . ASN A 327 ? 1.6814 0.8631 1.3936 0.4680  0.2671  -0.1832 845 ASN A CG  
2761 O OD1 . ASN A 327 ? 1.7815 0.8912 1.3901 0.4736  0.2645  -0.2129 845 ASN A OD1 
2762 N ND2 . ASN A 327 ? 1.6304 0.9175 1.4163 0.4807  0.3111  -0.1607 845 ASN A ND2 
2763 N N   . GLY A 328 ? 1.5451 0.5340 1.2359 0.3174  0.0918  -0.1424 846 GLY A N   
2764 C CA  . GLY A 328 ? 1.5365 0.4955 1.2567 0.2881  0.0535  -0.1141 846 GLY A CA  
2765 C C   . GLY A 328 ? 1.4570 0.4712 1.2074 0.2482  0.0466  -0.0823 846 GLY A C   
2766 O O   . GLY A 328 ? 1.3610 0.4304 1.1061 0.2339  0.0657  -0.0857 846 GLY A O   
2767 N N   . PRO A 329 ? 1.4134 0.4195 1.1945 0.2289  0.0185  -0.0499 847 PRO A N   
2768 C CA  . PRO A 329 ? 1.3088 0.3951 1.1284 0.1877  0.0096  -0.0182 847 PRO A CA  
2769 C C   . PRO A 329 ? 1.2555 0.4660 1.1475 0.2085  0.0415  -0.0151 847 PRO A C   
2770 O O   . PRO A 329 ? 1.2651 0.5071 1.2152 0.2566  0.0581  -0.0131 847 PRO A O   
2771 C CB  . PRO A 329 ? 1.3431 0.3927 1.1786 0.1886  -0.0204 0.0139  847 PRO A CB  
2772 C CG  . PRO A 329 ? 1.4712 0.4127 1.2612 0.1951  -0.0369 0.0014  847 PRO A CG  
2773 C CD  . PRO A 329 ? 1.5005 0.4406 1.2830 0.2378  -0.0080 -0.0403 847 PRO A CD  
2774 N N   . GLN A 330 ? 1.1150 0.3950 1.0089 0.1716  0.0482  -0.0143 848 GLN A N   
2775 C CA  . GLN A 330 ? 1.0986 0.4840 1.0560 0.1832  0.0747  -0.0098 848 GLN A CA  
2776 C C   . GLN A 330 ? 0.9329 0.3871 0.9014 0.1359  0.0619  0.0035  848 GLN A C   
2777 O O   . GLN A 330 ? 0.9616 0.4177 0.8898 0.1073  0.0607  -0.0068 848 GLN A O   
2778 C CB  . GLN A 330 ? 1.0328 0.4216 0.9698 0.2113  0.1136  -0.0330 848 GLN A CB  
2779 C CG  . GLN A 330 ? 1.1026 0.5913 1.1072 0.2197  0.1436  -0.0229 848 GLN A CG  
2780 C CD  . GLN A 330 ? 1.0946 0.6329 1.1943 0.2531  0.1544  -0.0090 848 GLN A CD  
2781 O OE1 . GLN A 330 ? 1.1912 0.7331 1.3174 0.2969  0.1894  -0.0163 848 GLN A OE1 
2782 N NE2 . GLN A 330 ? 0.9923 0.5741 1.1451 0.2341  0.1241  0.0101  848 GLN A NE2 
2783 N N   . SER A 331 ? 0.8755 0.3860 0.8976 0.1316  0.0496  0.0239  849 SER A N   
2784 C CA  . SER A 331 ? 0.8072 0.3820 0.8381 0.0950  0.0391  0.0335  849 SER A CA  
2785 C C   . SER A 331 ? 0.9023 0.5336 0.9509 0.0963  0.0628  0.0212  849 SER A C   
2786 O O   . SER A 331 ? 0.8128 0.4521 0.8871 0.1271  0.0894  0.0142  849 SER A O   
2787 C CB  . SER A 331 ? 0.7717 0.3906 0.8488 0.0993  0.0205  0.0521  849 SER A CB  
2788 O OG  . SER A 331 ? 0.9662 0.5274 1.0202 0.1026  -0.0036 0.0686  849 SER A OG  
2789 N N   . PHE A 332 ? 0.7111 0.3806 0.7455 0.0646  0.0551  0.0209  850 PHE A N   
2790 C CA  . PHE A 332 ? 0.6576 0.3810 0.7120 0.0669  0.0705  0.0143  850 PHE A CA  
2791 C C   . PHE A 332 ? 0.6961 0.4646 0.8213 0.0881  0.0789  0.0218  850 PHE A C   
2792 O O   . PHE A 332 ? 0.6393 0.4278 0.7949 0.0861  0.0590  0.0309  850 PHE A O   
2793 C CB  . PHE A 332 ? 0.6245 0.3900 0.6662 0.0352  0.0555  0.0139  850 PHE A CB  
2794 C CG  . PHE A 332 ? 0.6775 0.4866 0.7325 0.0404  0.0658  0.0070  850 PHE A CG  
2795 C CD1 . PHE A 332 ? 0.8172 0.6104 0.8320 0.0400  0.0713  -0.0037 850 PHE A CD1 
2796 C CD2 . PHE A 332 ? 0.5846 0.4424 0.6867 0.0469  0.0652  0.0108  850 PHE A CD2 
2797 C CE1 . PHE A 332 ? 0.7873 0.6125 0.8079 0.0479  0.0778  -0.0059 850 PHE A CE1 
2798 C CE2 . PHE A 332 ? 0.6279 0.5124 0.7395 0.0527  0.0724  0.0065  850 PHE A CE2 
2799 C CZ  . PHE A 332 ? 0.6755 0.5435 0.7458 0.0542  0.0796  0.0005  850 PHE A CZ  
2800 N N   . THR A 333 ? 0.6021 0.3846 0.7515 0.1069  0.1068  0.0194  851 THR A N   
2801 C CA  . THR A 333 ? 0.5954 0.4194 0.8259 0.1234  0.1173  0.0279  851 THR A CA  
2802 C C   . THR A 333 ? 0.5733 0.4348 0.8313 0.1176  0.1315  0.0309  851 THR A C   
2803 O O   . THR A 333 ? 0.5521 0.3978 0.7651 0.1181  0.1510  0.0287  851 THR A O   
2804 C CB  . THR A 333 ? 0.6281 0.4348 0.8853 0.1561  0.1469  0.0295  851 THR A CB  
2805 O OG1 . THR A 333 ? 0.6852 0.4374 0.9030 0.1663  0.1341  0.0245  851 THR A OG1 
2806 C CG2 . THR A 333 ? 0.6335 0.4952 0.9970 0.1688  0.1495  0.0403  851 THR A CG2 
2807 N N   . VAL A 334 ? 0.4943 0.3976 0.8215 0.1129  0.1175  0.0357  852 VAL A N   
2808 C CA  . VAL A 334 ? 0.4737 0.4013 0.8390 0.1076  0.1301  0.0411  852 VAL A CA  
2809 C C   . VAL A 334 ? 0.4913 0.4510 0.9565 0.1154  0.1440  0.0529  852 VAL A C   
2810 O O   . VAL A 334 ? 0.4858 0.4717 1.0108 0.1138  0.1146  0.0506  852 VAL A O   
2811 C CB  . VAL A 334 ? 0.4439 0.3893 0.8063 0.0909  0.0970  0.0320  852 VAL A CB  
2812 C CG1 . VAL A 334 ? 0.4393 0.3912 0.8334 0.0869  0.1078  0.0379  852 VAL A CG1 
2813 C CG2 . VAL A 334 ? 0.5348 0.4674 0.8175 0.0822  0.0846  0.0218  852 VAL A CG2 
2814 N N   . GLU A 335 ? 0.5624 0.5228 1.0452 0.1238  0.1886  0.0666  853 GLU A N   
2815 C CA  . GLU A 335 ? 0.4877 0.4900 1.0788 0.1277  0.2119  0.0824  853 GLU A CA  
2816 C C   . GLU A 335 ? 0.5574 0.5699 1.1886 0.1076  0.2249  0.0980  853 GLU A C   
2817 O O   . GLU A 335 ? 0.5095 0.4882 1.0699 0.1049  0.2425  0.1041  853 GLU A O   
2818 C CB  . GLU A 335 ? 0.5306 0.5308 1.1196 0.1553  0.2637  0.0907  853 GLU A CB  
2819 C CG  . GLU A 335 ? 0.5345 0.5924 1.2452 0.1599  0.3004  0.1111  853 GLU A CG  
2820 C CD  . GLU A 335 ? 0.7814 0.8412 1.4811 0.1936  0.3514  0.1145  853 GLU A CD  
2821 O OE1 . GLU A 335 ? 0.7970 0.8040 1.3966 0.2161  0.3557  0.0983  853 GLU A OE1 
2822 O OE2 . GLU A 335 ? 0.8272 0.9348 1.6045 0.1933  0.3796  0.1306  853 GLU A OE2 
2823 N N   . GLN A 336 ? 0.5302 0.5846 1.2753 0.0933  0.2119  0.1051  854 GLN A N   
2824 C CA  . GLN A 336 ? 0.5788 0.6364 1.3764 0.0700  0.2247  0.1236  854 GLN A CA  
2825 C C   . GLN A 336 ? 0.6268 0.6937 1.4430 0.0763  0.2951  0.1546  854 GLN A C   
2826 O O   . GLN A 336 ? 0.6095 0.7255 1.5077 0.0867  0.3248  0.1649  854 GLN A O   
2827 C CB  . GLN A 336 ? 0.5349 0.6325 1.4552 0.0483  0.1840  0.1193  854 GLN A CB  
2828 C CG  . GLN A 336 ? 0.5020 0.5808 1.4622 0.0181  0.1753  0.1296  854 GLN A CG  
2829 C CD  . GLN A 336 ? 0.5080 0.6272 1.6036 -0.0066 0.1377  0.1261  854 GLN A CD  
2830 O OE1 . GLN A 336 ? 0.6251 0.8025 1.8086 -0.0009 0.1337  0.1264  854 GLN A OE1 
2831 N NE2 . GLN A 336 ? 0.6335 0.7192 1.7466 -0.0321 0.1030  0.1193  854 GLN A NE2 
2832 N N   . TRP A 337 ? 0.5618 0.5839 1.3008 0.0731  0.3222  0.1703  855 TRP A N   
2833 C CA  . TRP A 337 ? 0.7075 0.7289 1.4366 0.0810  0.3937  0.2033  855 TRP A CA  
2834 C C   . TRP A 337 ? 0.7473 0.7258 1.4463 0.0612  0.4081  0.2315  855 TRP A C   
2835 O O   . TRP A 337 ? 0.6680 0.5974 1.2894 0.0590  0.3710  0.2195  855 TRP A O   
2836 C CB  . TRP A 337 ? 0.7214 0.7130 1.3304 0.1165  0.4228  0.1927  855 TRP A CB  
2837 C CG  . TRP A 337 ? 0.9121 0.8821 1.4606 0.1295  0.4921  0.2229  855 TRP A CG  
2838 C CD1 . TRP A 337 ? 0.9448 0.9524 1.5366 0.1456  0.5598  0.2442  855 TRP A CD1 
2839 C CD2 . TRP A 337 ? 0.9938 0.9010 1.4224 0.1311  0.5011  0.2366  855 TRP A CD2 
2840 N NE1 . TRP A 337 ? 1.0869 1.0516 1.5774 0.1551  0.6068  0.2690  855 TRP A NE1 
2841 C CE2 . TRP A 337 ? 1.0901 0.9933 1.4829 0.1473  0.5755  0.2676  855 TRP A CE2 
2842 C CE3 . TRP A 337 ? 1.0382 0.8956 1.3870 0.1240  0.4533  0.2259  855 TRP A CE3 
2843 C CZ2 . TRP A 337 ? 1.1312 0.9736 1.3996 0.1556  0.5992  0.2898  855 TRP A CZ2 
2844 C CZ3 . TRP A 337 ? 1.0866 0.8891 1.3252 0.1335  0.4737  0.2467  855 TRP A CZ3 
2845 C CH2 . TRP A 337 ? 1.0759 0.8671 1.2699 0.1487  0.5439  0.2791  855 TRP A CH2 
2846 N N   . GLY A 338 ? 0.7352 0.7338 1.4994 0.0478  0.4634  0.2713  856 GLY A N   
2847 C CA  . GLY A 338 ? 0.8139 0.7612 1.5378 0.0312  0.4873  0.3077  856 GLY A CA  
2848 C C   . GLY A 338 ? 0.8189 0.7451 1.6157 -0.0061 0.4404  0.3117  856 GLY A C   
2849 O O   . GLY A 338 ? 0.7802 0.7347 1.6572 -0.0194 0.3860  0.2823  856 GLY A O   
2850 N N   . THR A 339 ? 0.8482 0.7170 1.6058 -0.0197 0.4574  0.3461  857 THR A N   
2851 C CA  . THR A 339 ? 0.8633 0.6916 1.6633 -0.0488 0.4074  0.3451  857 THR A CA  
2852 C C   . THR A 339 ? 0.9586 0.7113 1.6433 -0.0297 0.3640  0.3262  857 THR A C   
2853 O O   . THR A 339 ? 0.9035 0.6415 1.4689 0.0036  0.3737  0.3178  857 THR A O   
2854 C CB  . THR A 339 ? 0.9609 0.7739 1.7808 -0.0711 0.4383  0.3862  857 THR A CB  
2855 O OG1 . THR A 339 ? 1.0453 0.8152 1.7378 -0.0483 0.4877  0.4173  857 THR A OG1 
2856 C CG2 . THR A 339 ? 0.9621 0.8585 1.9065 -0.0881 0.4670  0.3966  857 THR A CG2 
2857 N N   . PRO A 340 ? 1.0052 0.7157 1.7202 -0.0457 0.3081  0.3108  858 PRO A N   
2858 C CA  . PRO A 340 ? 1.0028 0.6555 1.6108 -0.0188 0.2635  0.2859  858 PRO A CA  
2859 C C   . PRO A 340 ? 1.0252 0.6122 1.5168 0.0011  0.2920  0.3221  858 PRO A C   
2860 O O   . PRO A 340 ? 0.9855 0.5403 1.3875 0.0303  0.2572  0.3007  858 PRO A O   
2861 C CB  . PRO A 340 ? 1.0600 0.6723 1.7354 -0.0404 0.2091  0.2694  858 PRO A CB  
2862 C CG  . PRO A 340 ? 1.0310 0.7069 1.8372 -0.0715 0.2016  0.2585  858 PRO A CG  
2863 C CD  . PRO A 340 ? 1.0237 0.7535 1.8627 -0.0807 0.2702  0.2982  858 PRO A CD  
2864 N N   . GLU A 341 ? 1.0398 0.6171 1.5279 -0.0118 0.3510  0.3727  859 GLU A N   
2865 C CA  . GLU A 341 ? 1.1408 0.6543 1.5044 0.0082  0.3730  0.4070  859 GLU A CA  
2866 C C   . GLU A 341 ? 1.1396 0.6521 1.3782 0.0493  0.3896  0.4001  859 GLU A C   
2867 O O   . GLU A 341 ? 1.1986 0.6547 1.3256 0.0762  0.3709  0.4059  859 GLU A O   
2868 C CB  . GLU A 341 ? 1.2320 0.7504 1.6143 -0.0158 0.4268  0.4538  859 GLU A CB  
2869 C CG  . GLU A 341 ? 1.3055 0.7871 1.7591 -0.0532 0.4008  0.4685  859 GLU A CG  
2870 C CD  . GLU A 341 ? 1.2173 0.7585 1.8242 -0.0875 0.3773  0.4430  859 GLU A CD  
2871 O OE1 . GLU A 341 ? 1.2297 0.8474 1.8938 -0.0824 0.3876  0.4200  859 GLU A OE1 
2872 O OE2 . GLU A 341 ? 1.2898 0.7963 1.9549 -0.1180 0.3440  0.4445  859 GLU A OE2 
2873 N N   . LYS A 342 ? 1.2551 0.8361 1.5076 0.0561  0.4134  0.3786  860 LYS A N   
2874 C CA  . LYS A 342 ? 1.2099 0.7916 1.3383 0.0923  0.4206  0.3619  860 LYS A CA  
2875 C C   . LYS A 342 ? 1.0591 0.6701 1.1711 0.1078  0.3606  0.3037  860 LYS A C   
2876 O O   . LYS A 342 ? 0.9214 0.5648 1.1185 0.0935  0.3215  0.2741  860 LYS A O   
2877 C CB  . LYS A 342 ? 1.2938 0.9165 1.4216 0.0980  0.4879  0.3747  860 LYS A CB  
2878 C CG  . LYS A 342 ? 1.2198 0.9207 1.4636 0.0869  0.4871  0.3446  860 LYS A CG  
2879 C CD  . LYS A 342 ? 1.2729 1.0130 1.6657 0.0512  0.5183  0.3751  860 LYS A CD  
2880 C CE  . LYS A 342 ? 1.2995 1.0554 1.6825 0.0547  0.5903  0.4128  860 LYS A CE  
2881 N NZ  . LYS A 342 ? 1.3702 1.0695 1.7018 0.0434  0.6002  0.4521  860 LYS A NZ  
2882 N N   . LEU A 343 ? 1.0667 0.6636 1.0633 0.1363  0.3531  0.2891  861 LEU A N   
2883 C CA  . LEU A 343 ? 0.9603 0.5852 0.9335 0.1481  0.3023  0.2402  861 LEU A CA  
2884 C C   . LEU A 343 ? 0.9771 0.6547 0.9925 0.1432  0.3153  0.2138  861 LEU A C   
2885 O O   . LEU A 343 ? 0.9219 0.6091 0.9511 0.1435  0.3667  0.2312  861 LEU A O   
2886 C CB  . LEU A 343 ? 1.0272 0.6158 0.8686 0.1762  0.2853  0.2361  861 LEU A CB  
2887 C CG  . LEU A 343 ? 1.1627 0.6930 0.9473 0.1899  0.2671  0.2638  861 LEU A CG  
2888 C CD1 . LEU A 343 ? 1.2502 0.7436 0.8955 0.2195  0.2605  0.2672  861 LEU A CD1 
2889 C CD2 . LEU A 343 ? 1.1237 0.6684 0.9591 0.1906  0.2080  0.2375  861 LEU A CD2 
2890 N N   . PRO A 344 ? 0.8746 0.5860 0.9106 0.1407  0.2707  0.1739  862 PRO A N   
2891 C CA  . PRO A 344 ? 0.8246 0.5725 0.8856 0.1387  0.2750  0.1496  862 PRO A CA  
2892 C C   . PRO A 344 ? 0.9035 0.6280 0.8710 0.1586  0.3010  0.1456  862 PRO A C   
2893 O O   . PRO A 344 ? 0.9616 0.6525 0.8324 0.1723  0.2859  0.1420  862 PRO A O   
2894 C CB  . PRO A 344 ? 0.7024 0.4765 0.7732 0.1327  0.2203  0.1148  862 PRO A CB  
2895 C CG  . PRO A 344 ? 0.7845 0.5514 0.8771 0.1300  0.1927  0.1186  862 PRO A CG  
2896 C CD  . PRO A 344 ? 0.8879 0.6046 0.9274 0.1410  0.2163  0.1520  862 PRO A CD  
2897 N N   . ARG A 345 ? 0.8942 0.6339 0.8884 0.1636  0.3353  0.1433  863 ARG A N   
2898 C CA  . ARG A 345 ? 1.0277 0.7368 0.9282 0.1871  0.3579  0.1317  863 ARG A CA  
2899 C C   . ARG A 345 ? 1.0524 0.7731 0.9671 0.1859  0.3323  0.0973  863 ARG A C   
2900 O O   . ARG A 345 ? 0.8774 0.6368 0.8842 0.1708  0.3147  0.0913  863 ARG A O   
2901 C CB  . ARG A 345 ? 1.0786 0.7848 0.9789 0.2041  0.4288  0.1585  863 ARG A CB  
2902 C CG  . ARG A 345 ? 1.1030 0.8641 1.1316 0.1980  0.4564  0.1644  863 ARG A CG  
2903 C CD  . ARG A 345 ? 1.2233 0.9909 1.2451 0.2230  0.5320  0.1837  863 ARG A CD  
2904 N NE  . ARG A 345 ? 1.1829 1.0164 1.3458 0.2191  0.5547  0.1894  863 ARG A NE  
2905 C CZ  . ARG A 345 ? 1.2344 1.0968 1.4293 0.2408  0.6147  0.2012  863 ARG A CZ  
2906 N NH1 . ARG A 345 ? 1.3376 1.1610 1.4204 0.2656  0.6521  0.2065  863 ARG A NH1 
2907 N NH2 . ARG A 345 ? 1.1652 1.0912 1.4947 0.2316  0.6106  0.2030  863 ARG A NH2 
2908 N N   . ALA A 346 ? 1.1989 0.8782 1.0159 0.2018  0.3270  0.0752  864 ALA A N   
2909 C CA  . ALA A 346 ? 1.1665 0.8392 0.9839 0.1981  0.2990  0.0445  864 ALA A CA  
2910 C C   . ALA A 346 ? 1.2429 0.8811 1.0196 0.2272  0.3360  0.0328  864 ALA A C   
2911 O O   . ALA A 346 ? 1.3566 0.9539 1.0402 0.2522  0.3659  0.0326  864 ALA A O   
2912 C CB  . ALA A 346 ? 1.2167 0.8674 0.9659 0.1850  0.2466  0.0214  864 ALA A CB  
2913 N N   . HIS A 347 ? 1.1327 0.7844 0.9740 0.2281  0.3331  0.0228  865 HIS A N   
2914 C CA  . HIS A 347 ? 1.1487 0.7601 0.9523 0.2596  0.3574  0.0041  865 HIS A CA  
2915 C C   . HIS A 347 ? 1.1639 0.7277 0.9246 0.2470  0.3060  -0.0263 865 HIS A C   
2916 O O   . HIS A 347 ? 1.0858 0.6630 0.9119 0.2351  0.2828  -0.0282 865 HIS A O   
2917 C CB  . HIS A 347 ? 1.1624 0.8202 1.0755 0.2760  0.3919  0.0171  865 HIS A CB  
2918 C CG  . HIS A 347 ? 1.1674 0.8769 1.1394 0.2828  0.4464  0.0497  865 HIS A CG  
2919 N ND1 . HIS A 347 ? 1.2935 1.0099 1.2613 0.3169  0.5081  0.0573  865 HIS A ND1 
2920 C CD2 . HIS A 347 ? 1.1689 0.9251 1.2086 0.2560  0.4465  0.0780  865 HIS A CD2 
2921 C CE1 . HIS A 347 ? 1.2552 1.0245 1.2899 0.3049  0.5443  0.0933  865 HIS A CE1 
2922 N NE2 . HIS A 347 ? 1.1935 0.9814 1.2732 0.2707  0.5107  0.1054  865 HIS A NE2 
2923 N N   . THR A 348 ? 1.2302 0.7362 0.8795 0.2476  0.2857  -0.0479 866 THR A N   
2924 C CA  . THR A 348 ? 1.2362 0.6963 0.8455 0.2248  0.2319  -0.0748 866 THR A CA  
2925 C C   . THR A 348 ? 1.1808 0.5909 0.7944 0.2405  0.2318  -0.0926 866 THR A C   
2926 O O   . THR A 348 ? 1.1756 0.5707 0.8132 0.2127  0.1916  -0.0983 866 THR A O   
2927 C CB  . THR A 348 ? 1.2959 0.7005 0.7838 0.2258  0.2082  -0.0980 866 THR A CB  
2928 O OG1 . THR A 348 ? 1.3258 0.6787 0.7249 0.2713  0.2508  -0.1094 866 THR A OG1 
2929 C CG2 . THR A 348 ? 1.1921 0.6454 0.6828 0.2071  0.1917  -0.0803 866 THR A CG2 
2930 N N   . CYS A 349 ? 1.2860 0.6705 0.8778 0.2868  0.2790  -0.0990 867 CYS A N   
2931 C CA  . CYS A 349 ? 1.3795 0.7126 0.9771 0.3129  0.2813  -0.1170 867 CYS A CA  
2932 C C   . CYS A 349 ? 1.3049 0.6840 1.0198 0.2977  0.2653  -0.0965 867 CYS A C   
2933 O O   . CYS A 349 ? 1.2294 0.5568 0.9476 0.3055  0.2445  -0.1080 867 CYS A O   
2934 C CB  . CYS A 349 ? 1.5077 0.8445 1.0892 0.3635  0.3370  -0.1206 867 CYS A CB  
2935 S SG  . CYS A 349 ? 1.7423 1.0174 1.1683 0.3832  0.3468  -0.1457 867 CYS A SG  
2936 N N   . PHE A 350 ? 1.0982 0.5660 0.9012 0.2770  0.2708  -0.0667 868 PHE A N   
2937 C CA  . PHE A 350 ? 1.0022 0.5179 0.9099 0.2658  0.2540  -0.0480 868 PHE A CA  
2938 C C   . PHE A 350 ? 0.9775 0.5316 0.9098 0.2164  0.2127  -0.0351 868 PHE A C   
2939 O O   . PHE A 350 ? 0.9375 0.5361 0.9458 0.2044  0.1961  -0.0190 868 PHE A O   
2940 C CB  . PHE A 350 ? 0.9612 0.5508 0.9661 0.2917  0.2981  -0.0278 868 PHE A CB  
2941 C CG  . PHE A 350 ? 1.1399 0.7150 1.1233 0.3391  0.3474  -0.0379 868 PHE A CG  
2942 C CD1 . PHE A 350 ? 1.2127 0.7527 1.1918 0.3654  0.3369  -0.0547 868 PHE A CD1 
2943 C CD2 . PHE A 350 ? 1.1380 0.7436 1.1006 0.3484  0.3944  -0.0279 868 PHE A CD2 
2944 C CE1 . PHE A 350 ? 1.3137 0.8555 1.2730 0.4030  0.3737  -0.0661 868 PHE A CE1 
2945 C CE2 . PHE A 350 ? 1.1702 0.7767 1.1080 0.3824  0.4336  -0.0344 868 PHE A CE2 
2946 C CZ  . PHE A 350 ? 1.3160 0.8940 1.2547 0.4111  0.4239  -0.0557 868 PHE A CZ  
2947 N N   . ASN A 351 ? 0.9558 0.4941 0.8215 0.1917  0.1951  -0.0441 869 ASN A N   
2948 C CA  . ASN A 351 ? 0.8579 0.4402 0.7449 0.1505  0.1620  -0.0347 869 ASN A CA  
2949 C C   . ASN A 351 ? 0.8770 0.5367 0.8508 0.1488  0.1739  -0.0127 869 ASN A C   
2950 O O   . ASN A 351 ? 0.7111 0.4083 0.7296 0.1262  0.1486  -0.0041 869 ASN A O   
2951 C CB  . ASN A 351 ? 0.8594 0.4179 0.7470 0.1217  0.1229  -0.0361 869 ASN A CB  
2952 C CG  . ASN A 351 ? 1.0435 0.5155 0.8516 0.1159  0.1045  -0.0584 869 ASN A CG  
2953 O OD1 . ASN A 351 ? 1.1262 0.5689 0.8687 0.1198  0.1051  -0.0770 869 ASN A OD1 
2954 N ND2 . ASN A 351 ? 0.9931 0.4161 0.8020 0.1070  0.0841  -0.0566 869 ASN A ND2 
2955 N N   . ARG A 352 ? 0.8914 0.5711 0.8858 0.1725  0.2135  -0.0037 870 ARG A N   
2956 C CA  . ARG A 352 ? 0.8446 0.5885 0.9307 0.1700  0.2252  0.0165  870 ARG A CA  
2957 C C   . ARG A 352 ? 0.7767 0.5430 0.8545 0.1603  0.2344  0.0275  870 ARG A C   
2958 O O   . ARG A 352 ? 0.7817 0.5228 0.8008 0.1746  0.2621  0.0296  870 ARG A O   
2959 C CB  . ARG A 352 ? 0.8845 0.6447 1.0311 0.2009  0.2654  0.0254  870 ARG A CB  
2960 C CG  . ARG A 352 ? 0.7343 0.5616 0.9864 0.1940  0.2779  0.0468  870 ARG A CG  
2961 C CD  . ARG A 352 ? 0.7058 0.5639 1.0361 0.2223  0.3160  0.0559  870 ARG A CD  
2962 N NE  . ARG A 352 ? 0.9598 0.7914 1.2331 0.2517  0.3704  0.0554  870 ARG A NE  
2963 C CZ  . ARG A 352 ? 1.0323 0.8789 1.3387 0.2837  0.4065  0.0555  870 ARG A CZ  
2964 N NH1 . ARG A 352 ? 1.0255 0.9151 1.4254 0.2879  0.3863  0.0568  870 ARG A NH1 
2965 N NH2 . ARG A 352 ? 1.1598 0.9810 1.3922 0.3061  0.4505  0.0534  870 ARG A NH2 
2966 N N   . LEU A 353 ? 0.6798 0.4868 0.8091 0.1392  0.2098  0.0341  871 LEU A N   
2967 C CA  . LEU A 353 ? 0.6765 0.5000 0.8122 0.1326  0.2151  0.0462  871 LEU A CA  
2968 C C   . LEU A 353 ? 0.7414 0.5972 0.9676 0.1346  0.2401  0.0664  871 LEU A C   
2969 O O   . LEU A 353 ? 0.6466 0.5357 0.9508 0.1256  0.2208  0.0659  871 LEU A O   
2970 C CB  . LEU A 353 ? 0.5680 0.4125 0.7045 0.1124  0.1734  0.0373  871 LEU A CB  
2971 C CG  . LEU A 353 ? 0.6317 0.4862 0.7779 0.1096  0.1704  0.0467  871 LEU A CG  
2972 C CD1 . LEU A 353 ? 0.6728 0.4954 0.7377 0.1199  0.1786  0.0499  871 LEU A CD1 
2973 C CD2 . LEU A 353 ? 0.5486 0.4338 0.7183 0.0967  0.1321  0.0337  871 LEU A CD2 
2974 N N   . ASP A 354 ? 0.7442 0.5897 0.9588 0.1446  0.2817  0.0856  872 ASP A N   
2975 C CA  . ASP A 354 ? 0.6953 0.5726 1.0019 0.1381  0.3077  0.1102  872 ASP A CA  
2976 C C   . ASP A 354 ? 0.6831 0.5558 0.9984 0.1191  0.2845  0.1184  872 ASP A C   
2977 O O   . ASP A 354 ? 0.7333 0.5719 0.9780 0.1233  0.2930  0.1285  872 ASP A O   
2978 C CB  . ASP A 354 ? 0.8198 0.6895 1.1110 0.1566  0.3713  0.1324  872 ASP A CB  
2979 C CG  . ASP A 354 ? 0.9099 0.7908 1.2156 0.1819  0.3976  0.1223  872 ASP A CG  
2980 O OD1 . ASP A 354 ? 0.9776 0.8745 1.3064 0.1992  0.4553  0.1407  872 ASP A OD1 
2981 O OD2 . ASP A 354 ? 0.8493 0.7224 1.1446 0.1860  0.3622  0.0975  872 ASP A OD2 
2982 N N   . LEU A 355 ? 0.5809 0.4823 0.9767 0.1019  0.2509  0.1118  873 LEU A N   
2983 C CA  . LEU A 355 ? 0.5999 0.4907 1.0010 0.0883  0.2188  0.1093  873 LEU A CA  
2984 C C   . LEU A 355 ? 0.5545 0.4575 1.0566 0.0697  0.2236  0.1276  873 LEU A C   
2985 O O   . LEU A 355 ? 0.5225 0.4617 1.1118 0.0597  0.2069  0.1204  873 LEU A O   
2986 C CB  . LEU A 355 ? 0.6189 0.5239 1.0090 0.0850  0.1682  0.0787  873 LEU A CB  
2987 C CG  . LEU A 355 ? 0.6517 0.5480 1.0393 0.0797  0.1328  0.0667  873 LEU A CG  
2988 C CD1 . LEU A 355 ? 0.7272 0.5907 1.0413 0.0906  0.1389  0.0737  873 LEU A CD1 
2989 C CD2 . LEU A 355 ? 0.5479 0.4685 0.9257 0.0791  0.0930  0.0378  873 LEU A CD2 
2990 N N   . PRO A 356 ? 0.6852 0.5544 1.1765 0.0637  0.2435  0.1530  874 PRO A N   
2991 C CA  . PRO A 356 ? 0.6185 0.4879 1.2073 0.0386  0.2436  0.1723  874 PRO A CA  
2992 C C   . PRO A 356 ? 0.5859 0.4557 1.2168 0.0269  0.1822  0.1422  874 PRO A C   
2993 O O   . PRO A 356 ? 0.5683 0.4253 1.1316 0.0411  0.1484  0.1148  874 PRO A O   
2994 C CB  . PRO A 356 ? 0.6926 0.5054 1.2250 0.0387  0.2698  0.2047  874 PRO A CB  
2995 C CG  . PRO A 356 ? 0.7412 0.5406 1.1627 0.0654  0.3013  0.2096  874 PRO A CG  
2996 C CD  . PRO A 356 ? 0.6597 0.4844 1.0464 0.0793  0.2671  0.1687  874 PRO A CD  
2997 N N   . PRO A 357 ? 0.5864 0.4725 1.3279 0.0018  0.1679  0.1461  875 PRO A N   
2998 C CA  . PRO A 357 ? 0.6457 0.5251 1.4208 -0.0075 0.1059  0.1129  875 PRO A CA  
2999 C C   . PRO A 357 ? 0.6243 0.4367 1.3698 -0.0112 0.0848  0.1119  875 PRO A C   
3000 O O   . PRO A 357 ? 0.7024 0.4877 1.5219 -0.0374 0.0750  0.1241  875 PRO A O   
3001 C CB  . PRO A 357 ? 0.6389 0.5597 1.5497 -0.0347 0.0980  0.1197  875 PRO A CB  
3002 C CG  . PRO A 357 ? 0.6879 0.6350 1.6459 -0.0426 0.1662  0.1644  875 PRO A CG  
3003 C CD  . PRO A 357 ? 0.6583 0.5646 1.4984 -0.0216 0.2093  0.1834  875 PRO A CD  
3004 N N   . TYR A 358 ? 0.6751 0.4606 1.3182 0.0151  0.0759  0.0976  876 TYR A N   
3005 C CA  . TYR A 358 ? 0.7306 0.4508 1.3379 0.0222  0.0551  0.0952  876 TYR A CA  
3006 C C   . TYR A 358 ? 0.6975 0.3959 1.3472 0.0155  -0.0007 0.0592  876 TYR A C   
3007 O O   . TYR A 358 ? 0.6581 0.3966 1.3249 0.0167  -0.0302 0.0263  876 TYR A O   
3008 C CB  . TYR A 358 ? 0.7552 0.4696 1.2553 0.0563  0.0537  0.0834  876 TYR A CB  
3009 C CG  . TYR A 358 ? 0.7846 0.5055 1.2296 0.0641  0.1006  0.1149  876 TYR A CG  
3010 C CD1 . TYR A 358 ? 0.8180 0.4958 1.2575 0.0562  0.1374  0.1593  876 TYR A CD1 
3011 C CD2 . TYR A 358 ? 0.6360 0.3998 1.0289 0.0784  0.1078  0.1006  876 TYR A CD2 
3012 C CE1 . TYR A 358 ? 0.8727 0.5511 1.2458 0.0677  0.1800  0.1851  876 TYR A CE1 
3013 C CE2 . TYR A 358 ? 0.7087 0.4688 1.0423 0.0874  0.1451  0.1231  876 TYR A CE2 
3014 C CZ  . TYR A 358 ? 0.8126 0.5306 1.1316 0.0846  0.1811  0.1635  876 TYR A CZ  
3015 O OH  . TYR A 358 ? 0.8234 0.5326 1.0681 0.0979  0.2179  0.1830  876 TYR A OH  
3016 N N   . GLU A 359 ? 0.7969 0.4230 1.4548 0.0102  -0.0167 0.0656  877 GLU A N   
3017 C CA  . GLU A 359 ? 0.8565 0.4421 1.5546 0.0024  -0.0716 0.0305  877 GLU A CA  
3018 C C   . GLU A 359 ? 0.8940 0.4421 1.5119 0.0424  -0.1071 -0.0100 877 GLU A C   
3019 O O   . GLU A 359 ? 0.9015 0.3952 1.5285 0.0431  -0.1488 -0.0373 877 GLU A O   
3020 C CB  . GLU A 359 ? 0.9476 0.4782 1.7083 -0.0331 -0.0700 0.0608  877 GLU A CB  
3021 C CG  . GLU A 359 ? 0.9768 0.5598 1.8377 -0.0742 -0.0376 0.0965  877 GLU A CG  
3022 C CD  . GLU A 359 ? 1.1003 0.6443 2.0012 -0.1073 -0.0240 0.1334  877 GLU A CD  
3023 O OE1 . GLU A 359 ? 1.1385 0.6347 1.9790 -0.1006 0.0104  0.1703  877 GLU A OE1 
3024 O OE2 . GLU A 359 ? 1.2128 0.7721 2.2023 -0.1395 -0.0501 0.1263  877 GLU A OE2 
3025 N N   . SER A 360 ? 0.7974 0.3820 1.3359 0.0755  -0.0897 -0.0148 878 SER A N   
3026 C CA  . SER A 360 ? 0.8141 0.3893 1.2862 0.1175  -0.1166 -0.0535 878 SER A CA  
3027 C C   . SER A 360 ? 0.7498 0.3964 1.1607 0.1407  -0.0942 -0.0563 878 SER A C   
3028 O O   . SER A 360 ? 0.7211 0.3901 1.1179 0.1325  -0.0585 -0.0219 878 SER A O   
3029 C CB  . SER A 360 ? 0.9007 0.3892 1.3496 0.1366  -0.1267 -0.0429 878 SER A CB  
3030 O OG  . SER A 360 ? 1.0791 0.5693 1.4721 0.1840  -0.1507 -0.0825 878 SER A OG  
3031 N N   . PHE A 361 ? 0.8334 0.5146 1.2072 0.1691  -0.1148 -0.0978 879 PHE A N   
3032 C CA  . PHE A 361 ? 0.8019 0.5547 1.1286 0.1860  -0.0963 -0.1010 879 PHE A CA  
3033 C C   . PHE A 361 ? 0.8088 0.5489 1.1021 0.2034  -0.0804 -0.0753 879 PHE A C   
3034 O O   . PHE A 361 ? 0.6618 0.4375 0.9344 0.1949  -0.0553 -0.0527 879 PHE A O   
3035 C CB  . PHE A 361 ? 0.7349 0.5270 1.0301 0.2163  -0.1160 -0.1465 879 PHE A CB  
3036 C CG  . PHE A 361 ? 0.7159 0.5797 0.9749 0.2334  -0.0977 -0.1467 879 PHE A CG  
3037 C CD1 . PHE A 361 ? 0.5842 0.5067 0.8363 0.2100  -0.0762 -0.1327 879 PHE A CD1 
3038 C CD2 . PHE A 361 ? 0.6744 0.5454 0.9128 0.2720  -0.1042 -0.1593 879 PHE A CD2 
3039 C CE1 . PHE A 361 ? 0.5545 0.5406 0.7822 0.2178  -0.0623 -0.1315 879 PHE A CE1 
3040 C CE2 . PHE A 361 ? 0.7328 0.6802 0.9539 0.2830  -0.0902 -0.1585 879 PHE A CE2 
3041 C CZ  . PHE A 361 ? 0.6834 0.6880 0.9004 0.2520  -0.0693 -0.1442 879 PHE A CZ  
3042 N N   . GLU A 362 ? 0.7673 0.4481 1.0514 0.2295  -0.0995 -0.0800 880 GLU A N   
3043 C CA  . GLU A 362 ? 0.8677 0.5300 1.1139 0.2550  -0.0952 -0.0584 880 GLU A CA  
3044 C C   . GLU A 362 ? 0.8895 0.5194 1.1263 0.2295  -0.0655 -0.0066 880 GLU A C   
3045 O O   . GLU A 362 ? 0.8696 0.5190 1.0622 0.2406  -0.0535 0.0117  880 GLU A O   
3046 C CB  . GLU A 362 ? 0.9619 0.5512 1.2026 0.2905  -0.1259 -0.0725 880 GLU A CB  
3047 C CG  . GLU A 362 ? 1.0536 0.6782 1.2609 0.3418  -0.1398 -0.0905 880 GLU A CG  
3048 C CD  . GLU A 362 ? 1.0350 0.7643 1.2450 0.3571  -0.1390 -0.1318 880 GLU A CD  
3049 O OE1 . GLU A 362 ? 1.0257 0.7631 1.2480 0.3561  -0.1471 -0.1662 880 GLU A OE1 
3050 O OE2 . GLU A 362 ? 1.0534 0.8579 1.2507 0.3671  -0.1299 -0.1282 880 GLU A OE2 
3051 N N   . GLU A 363 ? 0.8476 0.4327 1.1261 0.1955  -0.0533 0.0159  881 GLU A N   
3052 C CA  . GLU A 363 ? 0.8681 0.4375 1.1415 0.1704  -0.0141 0.0644  881 GLU A CA  
3053 C C   . GLU A 363 ? 0.8186 0.4633 1.0762 0.1602  0.0118  0.0640  881 GLU A C   
3054 O O   . GLU A 363 ? 0.7813 0.4254 0.9907 0.1628  0.0376  0.0907  881 GLU A O   
3055 C CB  . GLU A 363 ? 0.8708 0.3979 1.2143 0.1321  -0.0028 0.0869  881 GLU A CB  
3056 C CG  . GLU A 363 ? 0.8865 0.4092 1.2295 0.1084  0.0477  0.1381  881 GLU A CG  
3057 C CD  . GLU A 363 ? 1.0115 0.5066 1.4415 0.0669  0.0640  0.1653  881 GLU A CD  
3058 O OE1 . GLU A 363 ? 1.0777 0.5703 1.5768 0.0508  0.0310  0.1377  881 GLU A OE1 
3059 O OE2 . GLU A 363 ? 0.9593 0.4372 1.3882 0.0502  0.1102  0.2144  881 GLU A OE2 
3060 N N   . LEU A 364 ? 0.7022 0.4028 0.9925 0.1499  0.0029  0.0337  882 LEU A N   
3061 C CA  . LEU A 364 ? 0.6873 0.4474 0.9618 0.1409  0.0229  0.0326  882 LEU A CA  
3062 C C   . LEU A 364 ? 0.6470 0.4338 0.8575 0.1641  0.0175  0.0248  882 LEU A C   
3063 O O   . LEU A 364 ? 0.6386 0.4332 0.8099 0.1613  0.0376  0.0409  882 LEU A O   
3064 C CB  . LEU A 364 ? 0.5884 0.3956 0.9002 0.1293  0.0086  0.0036  882 LEU A CB  
3065 C CG  . LEU A 364 ? 0.5382 0.3937 0.8391 0.1178  0.0267  0.0051  882 LEU A CG  
3066 C CD1 . LEU A 364 ? 0.5100 0.3859 0.8647 0.1006  0.0178  -0.0049 882 LEU A CD1 
3067 C CD2 . LEU A 364 ? 0.5134 0.4128 0.7651 0.1306  0.0172  -0.0145 882 LEU A CD2 
3068 N N   . TRP A 365 ? 0.7238 0.5255 0.9269 0.1887  -0.0114 -0.0019 883 TRP A N   
3069 C CA  . TRP A 365 ? 0.6715 0.5132 0.8340 0.2111  -0.0221 -0.0119 883 TRP A CA  
3070 C C   . TRP A 365 ? 0.7036 0.5042 0.8157 0.2219  -0.0155 0.0187  883 TRP A C   
3071 O O   . TRP A 365 ? 0.7233 0.5512 0.7975 0.2192  -0.0104 0.0228  883 TRP A O   
3072 C CB  . TRP A 365 ? 0.7409 0.6020 0.9140 0.2437  -0.0508 -0.0430 883 TRP A CB  
3073 C CG  . TRP A 365 ? 0.7038 0.6173 0.8541 0.2683  -0.0636 -0.0516 883 TRP A CG  
3074 C CD1 . TRP A 365 ? 0.7082 0.5961 0.8336 0.3000  -0.0814 -0.0418 883 TRP A CD1 
3075 C CD2 . TRP A 365 ? 0.7202 0.7227 0.8762 0.2607  -0.0621 -0.0689 883 TRP A CD2 
3076 N NE1 . TRP A 365 ? 0.7665 0.7306 0.8899 0.3145  -0.0947 -0.0555 883 TRP A NE1 
3077 C CE2 . TRP A 365 ? 0.7479 0.7841 0.8933 0.2875  -0.0811 -0.0714 883 TRP A CE2 
3078 C CE3 . TRP A 365 ? 0.5469 0.6014 0.7174 0.2328  -0.0482 -0.0796 883 TRP A CE3 
3079 C CZ2 . TRP A 365 ? 0.6489 0.7774 0.8100 0.2821  -0.0854 -0.0855 883 TRP A CZ2 
3080 C CZ3 . TRP A 365 ? 0.6167 0.7522 0.7927 0.2269  -0.0491 -0.0899 883 TRP A CZ3 
3081 C CH2 . TRP A 365 ? 0.5367 0.7125 0.7140 0.2492  -0.0671 -0.0934 883 TRP A CH2 
3082 N N   . ASP A 366 ? 0.7616 0.4896 0.8679 0.2327  -0.0175 0.0409  884 ASP A N   
3083 C CA  . ASP A 366 ? 0.8361 0.5103 0.8815 0.2453  -0.0103 0.0767  884 ASP A CA  
3084 C C   . ASP A 366 ? 0.8613 0.5270 0.8730 0.2221  0.0286  0.1043  884 ASP A C   
3085 O O   . ASP A 366 ? 0.8798 0.5392 0.8222 0.2341  0.0302  0.1162  884 ASP A O   
3086 C CB  . ASP A 366 ? 0.9179 0.5043 0.9678 0.2541  -0.0148 0.1018  884 ASP A CB  
3087 C CG  . ASP A 366 ? 1.0106 0.5863 1.0724 0.2910  -0.0562 0.0756  884 ASP A CG  
3088 O OD1 . ASP A 366 ? 0.9466 0.5884 1.0019 0.3162  -0.0782 0.0461  884 ASP A OD1 
3089 O OD2 . ASP A 366 ? 1.0058 0.5072 1.0872 0.2951  -0.0665 0.0841  884 ASP A OD2 
3090 N N   . LYS A 367 ? 0.8119 0.4772 0.8717 0.1925  0.0577  0.1124  885 LYS A N   
3091 C CA  . LYS A 367 ? 0.8272 0.4841 0.8625 0.1765  0.1009  0.1386  885 LYS A CA  
3092 C C   . LYS A 367 ? 0.9282 0.6353 0.9318 0.1751  0.1023  0.1165  885 LYS A C   
3093 O O   . LYS A 367 ? 0.9334 0.6236 0.8690 0.1811  0.1213  0.1294  885 LYS A O   
3094 C CB  . LYS A 367 ? 0.8062 0.4622 0.9214 0.1474  0.1287  0.1514  885 LYS A CB  
3095 C CG  . LYS A 367 ? 0.8715 0.4652 1.0194 0.1385  0.1352  0.1830  885 LYS A CG  
3096 C CD  . LYS A 367 ? 0.9678 0.5053 1.0441 0.1460  0.1693  0.2304  885 LYS A CD  
3097 C CE  . LYS A 367 ? 1.1556 0.6479 1.2869 0.1185  0.2034  0.2746  885 LYS A CE  
3098 N NZ  . LYS A 367 ? 1.0467 0.4947 1.2395 0.1086  0.1678  0.2704  885 LYS A NZ  
3099 N N   . LEU A 368 ? 0.8294 0.5916 0.8770 0.1670  0.0814  0.0832  886 LEU A N   
3100 C CA  . LEU A 368 ? 0.7642 0.5687 0.7912 0.1599  0.0786  0.0630  886 LEU A CA  
3101 C C   . LEU A 368 ? 0.8296 0.6411 0.7917 0.1764  0.0541  0.0546  886 LEU A C   
3102 O O   . LEU A 368 ? 0.7641 0.5704 0.6744 0.1735  0.0596  0.0528  886 LEU A O   
3103 C CB  . LEU A 368 ? 0.6638 0.5207 0.7480 0.1474  0.0615  0.0356  886 LEU A CB  
3104 C CG  . LEU A 368 ? 0.7224 0.6190 0.7956 0.1337  0.0576  0.0183  886 LEU A CG  
3105 C CD1 . LEU A 368 ? 0.7168 0.5895 0.7796 0.1231  0.0874  0.0304  886 LEU A CD1 
3106 C CD2 . LEU A 368 ? 0.6439 0.5880 0.7639 0.1247  0.0414  -0.0027 886 LEU A CD2 
3107 N N   . GLN A 369 ? 0.8339 0.6559 0.8011 0.1960  0.0235  0.0472  887 GLN A N   
3108 C CA  . GLN A 369 ? 0.8590 0.6996 0.7815 0.2145  -0.0077 0.0382  887 GLN A CA  
3109 C C   . GLN A 369 ? 0.9604 0.7395 0.7949 0.2288  -0.0014 0.0637  887 GLN A C   
3110 O O   . GLN A 369 ? 0.9460 0.7337 0.7267 0.2332  -0.0209 0.0547  887 GLN A O   
3111 C CB  . GLN A 369 ? 0.8199 0.6843 0.7746 0.2411  -0.0397 0.0265  887 GLN A CB  
3112 C CG  . GLN A 369 ? 0.9852 0.9022 0.9270 0.2589  -0.0777 0.0097  887 GLN A CG  
3113 C CD  . GLN A 369 ? 1.0315 1.0421 1.0315 0.2412  -0.0860 -0.0206 887 GLN A CD  
3114 O OE1 . GLN A 369 ? 1.0933 1.1573 1.0933 0.2375  -0.1095 -0.0332 887 GLN A OE1 
3115 N NE2 . GLN A 369 ? 0.9729 1.0031 1.0218 0.2283  -0.0678 -0.0308 887 GLN A NE2 
3116 N N   . MET A 370 ? 0.9362 0.6514 0.7535 0.2347  0.0252  0.0963  888 MET A N   
3117 C CA  . MET A 370 ? 1.0205 0.6713 0.7425 0.2498  0.0399  0.1271  888 MET A CA  
3118 C C   . MET A 370 ? 1.0032 0.6506 0.6756 0.2373  0.0673  0.1228  888 MET A C   
3119 O O   . MET A 370 ? 1.1294 0.7515 0.7088 0.2520  0.0566  0.1226  888 MET A O   
3120 C CB  . MET A 370 ? 1.0972 0.6835 0.8227 0.2502  0.0727  0.1685  888 MET A CB  
3121 C CG  . MET A 370 ? 1.3572 0.8709 0.9729 0.2706  0.0876  0.2080  888 MET A CG  
3122 S SD  . MET A 370 ? 1.4927 0.9852 1.0343 0.3130  0.0243  0.2071  888 MET A SD  
3123 C CE  . MET A 370 ? 1.4211 0.9131 1.0587 0.3216  -0.0033 0.2035  888 MET A CE  
3124 N N   . ALA A 371 ? 0.9490 0.6182 0.6815 0.2134  0.0990  0.1168  889 ALA A N   
3125 C CA  . ALA A 371 ? 0.9601 0.6228 0.6563 0.2057  0.1278  0.1102  889 ALA A CA  
3126 C C   . ALA A 371 ? 0.9609 0.6446 0.6153 0.2043  0.0904  0.0761  889 ALA A C   
3127 O O   . ALA A 371 ? 1.0480 0.6955 0.6151 0.2136  0.0958  0.0716  889 ALA A O   
3128 C CB  . ALA A 371 ? 0.8768 0.5680 0.6612 0.1840  0.1568  0.1070  889 ALA A CB  
3129 N N   . ILE A 372 ? 0.9233 0.6642 0.6389 0.1923  0.0526  0.0520  890 ILE A N   
3130 C CA  . ILE A 372 ? 0.9878 0.7600 0.6892 0.1806  0.0165  0.0217  890 ILE A CA  
3131 C C   . ILE A 372 ? 1.0757 0.8304 0.6963 0.1993  -0.0221 0.0164  890 ILE A C   
3132 O O   . ILE A 372 ? 1.1692 0.9082 0.7345 0.1927  -0.0395 -0.0027 890 ILE A O   
3133 C CB  . ILE A 372 ? 0.9258 0.7743 0.7179 0.1633  -0.0087 0.0030  890 ILE A CB  
3134 C CG1 . ILE A 372 ? 0.8623 0.7259 0.7236 0.1466  0.0205  0.0058  890 ILE A CG1 
3135 C CG2 . ILE A 372 ? 0.9683 0.8526 0.7580 0.1423  -0.0411 -0.0227 890 ILE A CG2 
3136 C CD1 . ILE A 372 ? 0.9117 0.7386 0.7533 0.1358  0.0520  0.0086  890 ILE A CD1 
3137 N N   . GLU A 373 ? 1.1514 0.9033 0.7632 0.2240  -0.0408 0.0317  891 GLU A N   
3138 C CA  . GLU A 373 ? 1.3589 1.1059 0.9056 0.2451  -0.0894 0.0255  891 GLU A CA  
3139 C C   . GLU A 373 ? 1.5623 1.2266 0.9764 0.2644  -0.0784 0.0396  891 GLU A C   
3140 O O   . GLU A 373 ? 1.5981 1.2437 0.9369 0.2867  -0.1207 0.0376  891 GLU A O   
3141 C CB  . GLU A 373 ? 1.3322 1.0979 0.9101 0.2727  -0.1163 0.0380  891 GLU A CB  
3142 C CG  . GLU A 373 ? 1.4532 1.1433 0.9839 0.2966  -0.0872 0.0784  891 GLU A CG  
3143 C CD  . GLU A 373 ? 1.5490 1.2429 1.1030 0.3284  -0.1212 0.0890  891 GLU A CD  
3144 O OE1 . GLU A 373 ? 1.5068 1.2724 1.1527 0.3282  -0.1445 0.0655  891 GLU A OE1 
3145 O OE2 . GLU A 373 ? 1.6493 1.2720 1.1252 0.3564  -0.1235 0.1217  891 GLU A OE2 
3146 N N   . ASN A 374 ? 1.7062 1.3245 1.0903 0.2590  -0.0220 0.0533  892 ASN A N   
3147 C CA  . ASN A 374 ? 1.9140 1.4591 1.1665 0.2777  -0.0030 0.0604  892 ASN A CA  
3148 C C   . ASN A 374 ? 1.9554 1.4965 1.1734 0.2629  -0.0203 0.0200  892 ASN A C   
3149 O O   . ASN A 374 ? 2.1050 1.5892 1.2015 0.2808  -0.0303 0.0097  892 ASN A O   
3150 C CB  . ASN A 374 ? 1.9694 1.4725 1.2087 0.2831  0.0719  0.0959  892 ASN A CB  
3151 C CG  . ASN A 374 ? 1.9671 1.4685 1.2196 0.2692  0.1136  0.0786  892 ASN A CG  
3152 O OD1 . ASN A 374 ? 1.9154 1.4635 1.2593 0.2438  0.1046  0.0552  892 ASN A OD1 
3153 N ND2 . ASN A 374 ? 2.0212 1.4667 1.1775 0.2896  0.1608  0.0915  892 ASN A ND2 
3154 N N   . THR A 375 ? 1.7953 1.3889 1.1135 0.2307  -0.0254 -0.0024 893 THR A N   
3155 C CA  . THR A 375 ? 1.7268 1.3098 1.0263 0.2107  -0.0431 -0.0385 893 THR A CA  
3156 C C   . THR A 375 ? 1.7124 1.3395 1.0335 0.1922  -0.1149 -0.0668 893 THR A C   
3157 O O   . THR A 375 ? 1.6096 1.3138 1.0344 0.1747  -0.1351 -0.0665 893 THR A O   
3158 C CB  . THR A 375 ? 1.5790 1.1868 0.9706 0.1842  -0.0095 -0.0427 893 THR A CB  
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