data_9M3T
# 
_entry.id   9M3T 
# 
_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   9M3T         pdb_00009m3t 10.2210/pdb9m3t/pdb 
WWPDB D_1300057123 ?            ?                   
# 
_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       2025-06-11 
_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                        9M3T 
_pdbx_database_status.recvd_initial_deposition_date   2025-03-03 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBC 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           N 
# 
_pdbx_database_related.db_name        PDB 
_pdbx_database_related.details        . 
_pdbx_database_related.db_id          9M3O 
_pdbx_database_related.content_type   unspecified 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              bruce.xu@roche.com 
_pdbx_contact_author.name_first         bruce 
_pdbx_contact_author.name_last          xu 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-7301-015X 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Xu, Z.H.' 1 ? 
'Chen, S.' 2 ? 
# 
_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            Bioorg.Med.Chem.Lett. 
_citation.journal_id_ASTM           BMCLE8 
_citation.journal_id_CSD            1127 
_citation.journal_id_ISSN           1464-3405 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            122 
_citation.language                  ? 
_citation.page_first                130190 
_citation.page_last                 130190 
_citation.title                     'Discovery of ATP competitive PDHK1/2 dual inhibitors.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1016/j.bmcl.2025.130190 
_citation.pdbx_database_id_PubMed   40107630 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Xu, H.'         1  ? 
primary 'Ding, D.'       2  ? 
primary 'Han, X.'        3  ? 
primary 'Miao, K.'       4  ? 
primary 'Liang, C.'      5  ? 
primary 'Yun, H.'        6  ? 
primary 'Zhu, W.'        7  ? 
primary 'Dey, F.'        8  ? 
primary 'Zhao, D.'       9  ? 
primary 'Wu, Y.'         10 ? 
primary 'Reutlinger, M.' 11 ? 
primary 'Yang, J.'       12 ? 
primary 'Zhai, G.'       13 ? 
primary 'Lin, Z.'        14 ? 
primary 'Li, C.'         15 ? 
primary 'Wu, W.'         16 ? 
primary 'Xu, B.'         17 ? 
primary 'Han, L.'        18 ? 
primary 'Chen, S.'       19 ? 
primary 'Huang, X.'      20 ? 
primary 'Casagrande, F.' 21 ? 
primary 'Hilbert, M.'    22 ? 
primary 'Strebel, Q.'    23 ? 
primary 'Wichert, M.'    24 ? 
primary 'Westwood, P.'   25 ? 
primary 'Schafer, R.'    26 ? 
primary 'Roth, D.'       27 ? 
primary 'Heer, D.'       28 ? 
primary 'Tian, X.'       29 ? 
primary 'Ma, T.'         30 ? 
primary 'Zhang, T.'      31 ? 
primary 'Zhao, J.'       32 ? 
primary 'Urich, E.'      33 ? 
primary 'Xia, G.'        34 ? 
primary 'Lassen, K.'     35 ? 
primary 'Shen, H.C.'     36 ? 
primary 'Zou, G.'        37 ? 
# 
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 '[Pyruvate dehydrogenase (acetyl-transferring)] kinase isozyme 2, mitochondrial' 41721.609 1   2.7.11.2 ? ? ? 
2 non-polymer syn 'N-(2-AMINOETHYL)-2-{3-CHLORO-4-[(4-ISOPROPYLBENZYL)OXY]PHENYL} ACETAMIDE' 360.878   1   ?        ? ? ? 
3 non-polymer syn 
'2-chloranyl-4-[[(3R)-1-[(3S)-7-(ethylamino)-5-fluoranyl-3-methyl-2-oxidanylidene-1H-indol-3-yl]piperidin-3-yl]amino]benzoic acid' 
460.929   1   ?        ? ? ? 
4 non-polymer syn 'DIMETHYL SULFOXIDE' 78.133    2   ?        ? ? ? 
5 water       nat water 18.015    149 ?        ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Pyruvate dehydrogenase kinase isoform 2,PDH kinase 2,PDKII' 
# 
_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       
;APKYIEHFSKFSPSPLSMKQFLDFGSSNACEKTSFTFLRQELPVRLANIMKEINLLPDRVLSTPSVQLVQSWYVQSLLDI
MEFLDKDPEDHRTLSQFTDALVTIRNRHNDVVPTMAQGVLEYKDTYGDDPVSNQNIQYFLDRFYLSRISIRMLINQHTLI
FDGSTNPAHPKHIGSIDPNCNVSEVVKDAYDMAKLLCDKYYMASPDLEIQEINAANSKQPIHMVYVPSHLYHMLFELFKN
AMRATVESHESSLILPPIKVMVALGEEDLSIKMSDRGGGVPLRKIERLFSYMYSTAPTPQPGTGGTPLAGFGYGLPISRL
YAKYFQGDLQLFSMEGFGTDAVIYLKALSTDSVERLPVYNKSAWRHY
;
_entity_poly.pdbx_seq_one_letter_code_can   
;APKYIEHFSKFSPSPLSMKQFLDFGSSNACEKTSFTFLRQELPVRLANIMKEINLLPDRVLSTPSVQLVQSWYVQSLLDI
MEFLDKDPEDHRTLSQFTDALVTIRNRHNDVVPTMAQGVLEYKDTYGDDPVSNQNIQYFLDRFYLSRISIRMLINQHTLI
FDGSTNPAHPKHIGSIDPNCNVSEVVKDAYDMAKLLCDKYYMASPDLEIQEINAANSKQPIHMVYVPSHLYHMLFELFKN
AMRATVESHESSLILPPIKVMVALGEEDLSIKMSDRGGGVPLRKIERLFSYMYSTAPTPQPGTGGTPLAGFGYGLPISRL
YAKYFQGDLQLFSMEGFGTDAVIYLKALSTDSVERLPVYNKSAWRHY
;
_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 'N-(2-AMINOETHYL)-2-{3-CHLORO-4-[(4-ISOPROPYLBENZYL)OXY]PHENYL} ACETAMIDE' TF3   
3 
'2-chloranyl-4-[[(3R)-1-[(3S)-7-(ethylamino)-5-fluoranyl-3-methyl-2-oxidanylidene-1H-indol-3-yl]piperidin-3-yl]amino]benzoic acid' 
A1EQI 
4 'DIMETHYL SULFOXIDE' DMS   
5 water HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   ALA n 
1 2   PRO n 
1 3   LYS n 
1 4   TYR n 
1 5   ILE n 
1 6   GLU n 
1 7   HIS n 
1 8   PHE n 
1 9   SER n 
1 10  LYS n 
1 11  PHE n 
1 12  SER n 
1 13  PRO n 
1 14  SER n 
1 15  PRO n 
1 16  LEU n 
1 17  SER n 
1 18  MET n 
1 19  LYS n 
1 20  GLN n 
1 21  PHE n 
1 22  LEU n 
1 23  ASP n 
1 24  PHE n 
1 25  GLY n 
1 26  SER n 
1 27  SER n 
1 28  ASN n 
1 29  ALA n 
1 30  CYS n 
1 31  GLU n 
1 32  LYS n 
1 33  THR n 
1 34  SER n 
1 35  PHE n 
1 36  THR n 
1 37  PHE n 
1 38  LEU n 
1 39  ARG n 
1 40  GLN n 
1 41  GLU n 
1 42  LEU n 
1 43  PRO n 
1 44  VAL n 
1 45  ARG n 
1 46  LEU n 
1 47  ALA n 
1 48  ASN n 
1 49  ILE n 
1 50  MET n 
1 51  LYS n 
1 52  GLU n 
1 53  ILE n 
1 54  ASN n 
1 55  LEU n 
1 56  LEU n 
1 57  PRO n 
1 58  ASP n 
1 59  ARG n 
1 60  VAL n 
1 61  LEU n 
1 62  SER n 
1 63  THR n 
1 64  PRO n 
1 65  SER n 
1 66  VAL n 
1 67  GLN n 
1 68  LEU n 
1 69  VAL n 
1 70  GLN n 
1 71  SER n 
1 72  TRP n 
1 73  TYR n 
1 74  VAL n 
1 75  GLN n 
1 76  SER n 
1 77  LEU n 
1 78  LEU n 
1 79  ASP n 
1 80  ILE n 
1 81  MET n 
1 82  GLU n 
1 83  PHE n 
1 84  LEU n 
1 85  ASP n 
1 86  LYS n 
1 87  ASP n 
1 88  PRO n 
1 89  GLU n 
1 90  ASP n 
1 91  HIS n 
1 92  ARG n 
1 93  THR n 
1 94  LEU n 
1 95  SER n 
1 96  GLN n 
1 97  PHE n 
1 98  THR n 
1 99  ASP n 
1 100 ALA n 
1 101 LEU n 
1 102 VAL n 
1 103 THR n 
1 104 ILE n 
1 105 ARG n 
1 106 ASN n 
1 107 ARG n 
1 108 HIS n 
1 109 ASN n 
1 110 ASP n 
1 111 VAL n 
1 112 VAL n 
1 113 PRO n 
1 114 THR n 
1 115 MET n 
1 116 ALA n 
1 117 GLN n 
1 118 GLY n 
1 119 VAL n 
1 120 LEU n 
1 121 GLU n 
1 122 TYR n 
1 123 LYS n 
1 124 ASP n 
1 125 THR n 
1 126 TYR n 
1 127 GLY n 
1 128 ASP n 
1 129 ASP n 
1 130 PRO n 
1 131 VAL n 
1 132 SER n 
1 133 ASN n 
1 134 GLN n 
1 135 ASN n 
1 136 ILE n 
1 137 GLN n 
1 138 TYR n 
1 139 PHE n 
1 140 LEU n 
1 141 ASP n 
1 142 ARG n 
1 143 PHE n 
1 144 TYR n 
1 145 LEU n 
1 146 SER n 
1 147 ARG n 
1 148 ILE n 
1 149 SER n 
1 150 ILE n 
1 151 ARG n 
1 152 MET n 
1 153 LEU n 
1 154 ILE n 
1 155 ASN n 
1 156 GLN n 
1 157 HIS n 
1 158 THR n 
1 159 LEU n 
1 160 ILE n 
1 161 PHE n 
1 162 ASP n 
1 163 GLY n 
1 164 SER n 
1 165 THR n 
1 166 ASN n 
1 167 PRO n 
1 168 ALA n 
1 169 HIS n 
1 170 PRO n 
1 171 LYS n 
1 172 HIS n 
1 173 ILE n 
1 174 GLY n 
1 175 SER n 
1 176 ILE n 
1 177 ASP n 
1 178 PRO n 
1 179 ASN n 
1 180 CYS n 
1 181 ASN n 
1 182 VAL n 
1 183 SER n 
1 184 GLU n 
1 185 VAL n 
1 186 VAL n 
1 187 LYS n 
1 188 ASP n 
1 189 ALA n 
1 190 TYR n 
1 191 ASP n 
1 192 MET n 
1 193 ALA n 
1 194 LYS n 
1 195 LEU n 
1 196 LEU n 
1 197 CYS n 
1 198 ASP n 
1 199 LYS n 
1 200 TYR n 
1 201 TYR n 
1 202 MET n 
1 203 ALA n 
1 204 SER n 
1 205 PRO n 
1 206 ASP n 
1 207 LEU n 
1 208 GLU n 
1 209 ILE n 
1 210 GLN n 
1 211 GLU n 
1 212 ILE n 
1 213 ASN n 
1 214 ALA n 
1 215 ALA n 
1 216 ASN n 
1 217 SER n 
1 218 LYS n 
1 219 GLN n 
1 220 PRO n 
1 221 ILE n 
1 222 HIS n 
1 223 MET n 
1 224 VAL n 
1 225 TYR n 
1 226 VAL n 
1 227 PRO n 
1 228 SER n 
1 229 HIS n 
1 230 LEU n 
1 231 TYR n 
1 232 HIS n 
1 233 MET n 
1 234 LEU n 
1 235 PHE n 
1 236 GLU n 
1 237 LEU n 
1 238 PHE n 
1 239 LYS n 
1 240 ASN n 
1 241 ALA n 
1 242 MET n 
1 243 ARG n 
1 244 ALA n 
1 245 THR n 
1 246 VAL n 
1 247 GLU n 
1 248 SER n 
1 249 HIS n 
1 250 GLU n 
1 251 SER n 
1 252 SER n 
1 253 LEU n 
1 254 ILE n 
1 255 LEU n 
1 256 PRO n 
1 257 PRO n 
1 258 ILE n 
1 259 LYS n 
1 260 VAL n 
1 261 MET n 
1 262 VAL n 
1 263 ALA n 
1 264 LEU n 
1 265 GLY n 
1 266 GLU n 
1 267 GLU n 
1 268 ASP n 
1 269 LEU n 
1 270 SER n 
1 271 ILE n 
1 272 LYS n 
1 273 MET n 
1 274 SER n 
1 275 ASP n 
1 276 ARG n 
1 277 GLY n 
1 278 GLY n 
1 279 GLY n 
1 280 VAL n 
1 281 PRO n 
1 282 LEU n 
1 283 ARG n 
1 284 LYS n 
1 285 ILE n 
1 286 GLU n 
1 287 ARG n 
1 288 LEU n 
1 289 PHE n 
1 290 SER n 
1 291 TYR n 
1 292 MET n 
1 293 TYR n 
1 294 SER n 
1 295 THR n 
1 296 ALA n 
1 297 PRO n 
1 298 THR n 
1 299 PRO n 
1 300 GLN n 
1 301 PRO n 
1 302 GLY n 
1 303 THR n 
1 304 GLY n 
1 305 GLY n 
1 306 THR n 
1 307 PRO n 
1 308 LEU n 
1 309 ALA n 
1 310 GLY n 
1 311 PHE n 
1 312 GLY n 
1 313 TYR n 
1 314 GLY n 
1 315 LEU n 
1 316 PRO n 
1 317 ILE n 
1 318 SER n 
1 319 ARG n 
1 320 LEU n 
1 321 TYR n 
1 322 ALA n 
1 323 LYS n 
1 324 TYR n 
1 325 PHE n 
1 326 GLN n 
1 327 GLY n 
1 328 ASP n 
1 329 LEU n 
1 330 GLN n 
1 331 LEU n 
1 332 PHE n 
1 333 SER n 
1 334 MET n 
1 335 GLU n 
1 336 GLY n 
1 337 PHE n 
1 338 GLY n 
1 339 THR n 
1 340 ASP n 
1 341 ALA n 
1 342 VAL n 
1 343 ILE n 
1 344 TYR n 
1 345 LEU n 
1 346 LYS n 
1 347 ALA n 
1 348 LEU n 
1 349 SER n 
1 350 THR n 
1 351 ASP n 
1 352 SER n 
1 353 VAL n 
1 354 GLU n 
1 355 ARG n 
1 356 LEU n 
1 357 PRO n 
1 358 VAL n 
1 359 TYR n 
1 360 ASN n 
1 361 LYS n 
1 362 SER n 
1 363 ALA n 
1 364 TRP n 
1 365 ARG n 
1 366 HIS n 
1 367 TYR 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                   367 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'PDK2, PDHK2' 
_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 BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_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 
A1EQI non-polymer         . 
'2-chloranyl-4-[[(3R)-1-[(3S)-7-(ethylamino)-5-fluoranyl-3-methyl-2-oxidanylidene-1H-indol-3-yl]piperidin-3-yl]amino]benzoic acid' 
? 'C23 H26 Cl F N4 O3' 460.929 
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 
DMS   non-polymer         . 'DIMETHYL SULFOXIDE' ? 'C2 H6 O S'          78.133  
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 
TF3   non-polymer         . 'N-(2-AMINOETHYL)-2-{3-CHLORO-4-[(4-ISOPROPYLBENZYL)OXY]PHENYL} ACETAMIDE' ? 'C20 H25 Cl N2 O2'   
360.878 
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   ALA 1   16  16  ALA ALA A . n 
A 1 2   PRO 2   17  17  PRO PRO A . n 
A 1 3   LYS 3   18  18  LYS LYS A . n 
A 1 4   TYR 4   19  19  TYR TYR A . n 
A 1 5   ILE 5   20  20  ILE ILE A . n 
A 1 6   GLU 6   21  21  GLU GLU A . n 
A 1 7   HIS 7   22  22  HIS HIS A . n 
A 1 8   PHE 8   23  23  PHE PHE A . n 
A 1 9   SER 9   24  24  SER SER A . n 
A 1 10  LYS 10  25  25  LYS LYS A . n 
A 1 11  PHE 11  26  26  PHE PHE A . n 
A 1 12  SER 12  27  27  SER SER A . n 
A 1 13  PRO 13  28  28  PRO PRO A . n 
A 1 14  SER 14  29  29  SER SER A . n 
A 1 15  PRO 15  30  30  PRO PRO A . n 
A 1 16  LEU 16  31  31  LEU LEU A . n 
A 1 17  SER 17  32  32  SER SER A . n 
A 1 18  MET 18  33  33  MET MET A . n 
A 1 19  LYS 19  34  34  LYS LYS A . n 
A 1 20  GLN 20  35  35  GLN GLN A . n 
A 1 21  PHE 21  36  36  PHE PHE A . n 
A 1 22  LEU 22  37  37  LEU LEU A . n 
A 1 23  ASP 23  38  38  ASP ASP A . n 
A 1 24  PHE 24  39  39  PHE PHE A . n 
A 1 25  GLY 25  40  40  GLY GLY A . n 
A 1 26  SER 26  41  ?   ?   ?   A . n 
A 1 27  SER 27  42  ?   ?   ?   A . n 
A 1 28  ASN 28  43  43  ASN ASN A . n 
A 1 29  ALA 29  44  44  ALA ALA A . n 
A 1 30  CYS 30  45  45  CYS CYS A . n 
A 1 31  GLU 31  46  46  GLU GLU A . n 
A 1 32  LYS 32  47  47  LYS LYS A . n 
A 1 33  THR 33  48  48  THR THR A . n 
A 1 34  SER 34  49  49  SER SER A . n 
A 1 35  PHE 35  50  50  PHE PHE A . n 
A 1 36  THR 36  51  51  THR THR A . n 
A 1 37  PHE 37  52  52  PHE PHE A . n 
A 1 38  LEU 38  53  53  LEU LEU A . n 
A 1 39  ARG 39  54  54  ARG ARG A . n 
A 1 40  GLN 40  55  55  GLN GLN A . n 
A 1 41  GLU 41  56  56  GLU GLU A . n 
A 1 42  LEU 42  57  57  LEU LEU A . n 
A 1 43  PRO 43  58  58  PRO PRO A . n 
A 1 44  VAL 44  59  59  VAL VAL A . n 
A 1 45  ARG 45  60  60  ARG ARG A . n 
A 1 46  LEU 46  61  61  LEU LEU A . n 
A 1 47  ALA 47  62  62  ALA ALA A . n 
A 1 48  ASN 48  63  63  ASN ASN A . n 
A 1 49  ILE 49  64  64  ILE ILE A . n 
A 1 50  MET 50  65  65  MET MET A . n 
A 1 51  LYS 51  66  66  LYS LYS A . n 
A 1 52  GLU 52  67  67  GLU GLU A . n 
A 1 53  ILE 53  68  68  ILE ILE A . n 
A 1 54  ASN 54  69  69  ASN ASN A . n 
A 1 55  LEU 55  70  70  LEU LEU A . n 
A 1 56  LEU 56  71  71  LEU LEU A . n 
A 1 57  PRO 57  72  72  PRO PRO A . n 
A 1 58  ASP 58  73  73  ASP ASP A . n 
A 1 59  ARG 59  74  74  ARG ARG A . n 
A 1 60  VAL 60  75  75  VAL VAL A . n 
A 1 61  LEU 61  76  76  LEU LEU A . n 
A 1 62  SER 62  77  77  SER SER A . n 
A 1 63  THR 63  78  78  THR THR A . n 
A 1 64  PRO 64  79  79  PRO PRO A . n 
A 1 65  SER 65  80  80  SER SER A . n 
A 1 66  VAL 66  81  81  VAL VAL A . n 
A 1 67  GLN 67  82  82  GLN GLN A . n 
A 1 68  LEU 68  83  83  LEU LEU A . n 
A 1 69  VAL 69  84  84  VAL VAL A . n 
A 1 70  GLN 70  85  85  GLN GLN A . n 
A 1 71  SER 71  86  86  SER SER A . n 
A 1 72  TRP 72  87  87  TRP TRP A . n 
A 1 73  TYR 73  88  88  TYR TYR A . n 
A 1 74  VAL 74  89  89  VAL VAL A . n 
A 1 75  GLN 75  90  90  GLN GLN A . n 
A 1 76  SER 76  91  91  SER SER A . n 
A 1 77  LEU 77  92  92  LEU LEU A . n 
A 1 78  LEU 78  93  93  LEU LEU A . n 
A 1 79  ASP 79  94  94  ASP ASP A . n 
A 1 80  ILE 80  95  95  ILE ILE A . n 
A 1 81  MET 81  96  96  MET MET A . n 
A 1 82  GLU 82  97  97  GLU GLU A . n 
A 1 83  PHE 83  98  98  PHE PHE A . n 
A 1 84  LEU 84  99  99  LEU LEU A . n 
A 1 85  ASP 85  100 100 ASP ASP A . n 
A 1 86  LYS 86  101 101 LYS LYS A . n 
A 1 87  ASP 87  102 102 ASP ASP A . n 
A 1 88  PRO 88  103 103 PRO PRO A . n 
A 1 89  GLU 89  104 104 GLU GLU A . n 
A 1 90  ASP 90  105 105 ASP ASP A . n 
A 1 91  HIS 91  106 106 HIS HIS A . n 
A 1 92  ARG 92  107 107 ARG ARG A . n 
A 1 93  THR 93  108 108 THR THR A . n 
A 1 94  LEU 94  109 109 LEU LEU A . n 
A 1 95  SER 95  110 110 SER SER A . n 
A 1 96  GLN 96  111 111 GLN GLN A . n 
A 1 97  PHE 97  112 112 PHE PHE A . n 
A 1 98  THR 98  113 113 THR THR A . n 
A 1 99  ASP 99  114 114 ASP ASP A . n 
A 1 100 ALA 100 115 115 ALA ALA A . n 
A 1 101 LEU 101 116 116 LEU LEU A . n 
A 1 102 VAL 102 117 117 VAL VAL A . n 
A 1 103 THR 103 118 118 THR THR A . n 
A 1 104 ILE 104 119 119 ILE ILE A . n 
A 1 105 ARG 105 120 120 ARG ARG A . n 
A 1 106 ASN 106 121 121 ASN ASN A . n 
A 1 107 ARG 107 122 122 ARG ARG A . n 
A 1 108 HIS 108 123 123 HIS HIS A . n 
A 1 109 ASN 109 124 124 ASN ASN A . n 
A 1 110 ASP 110 125 125 ASP ASP A . n 
A 1 111 VAL 111 126 126 VAL VAL A . n 
A 1 112 VAL 112 127 127 VAL VAL A . n 
A 1 113 PRO 113 128 128 PRO PRO A . n 
A 1 114 THR 114 129 129 THR THR A . n 
A 1 115 MET 115 130 130 MET MET A . n 
A 1 116 ALA 116 131 131 ALA ALA A . n 
A 1 117 GLN 117 132 132 GLN GLN A . n 
A 1 118 GLY 118 133 133 GLY GLY A . n 
A 1 119 VAL 119 134 134 VAL VAL A . n 
A 1 120 LEU 120 135 135 LEU LEU A . n 
A 1 121 GLU 121 136 136 GLU GLU A . n 
A 1 122 TYR 122 137 137 TYR TYR A . n 
A 1 123 LYS 123 138 138 LYS LYS A . n 
A 1 124 ASP 124 139 139 ASP ASP A . n 
A 1 125 THR 125 140 140 THR THR A . n 
A 1 126 TYR 126 141 141 TYR TYR A . n 
A 1 127 GLY 127 142 142 GLY GLY A . n 
A 1 128 ASP 128 143 143 ASP ASP A . n 
A 1 129 ASP 129 144 144 ASP ASP A . n 
A 1 130 PRO 130 145 145 PRO PRO A . n 
A 1 131 VAL 131 146 146 VAL VAL A . n 
A 1 132 SER 132 147 147 SER SER A . n 
A 1 133 ASN 133 148 148 ASN ASN A . n 
A 1 134 GLN 134 149 149 GLN GLN A . n 
A 1 135 ASN 135 150 150 ASN ASN A . n 
A 1 136 ILE 136 151 151 ILE ILE A . n 
A 1 137 GLN 137 152 152 GLN GLN A . n 
A 1 138 TYR 138 153 153 TYR TYR A . n 
A 1 139 PHE 139 154 154 PHE PHE A . n 
A 1 140 LEU 140 155 155 LEU LEU A . n 
A 1 141 ASP 141 156 156 ASP ASP A . n 
A 1 142 ARG 142 157 157 ARG ARG A . n 
A 1 143 PHE 143 158 158 PHE PHE A . n 
A 1 144 TYR 144 159 159 TYR TYR A . n 
A 1 145 LEU 145 160 160 LEU LEU A . n 
A 1 146 SER 146 161 161 SER SER A . n 
A 1 147 ARG 147 162 162 ARG ARG A . n 
A 1 148 ILE 148 163 163 ILE ILE A . n 
A 1 149 SER 149 164 164 SER SER A . n 
A 1 150 ILE 150 165 165 ILE ILE A . n 
A 1 151 ARG 151 166 166 ARG ARG A . n 
A 1 152 MET 152 167 167 MET MET A . n 
A 1 153 LEU 153 168 168 LEU LEU A . n 
A 1 154 ILE 154 169 169 ILE ILE A . n 
A 1 155 ASN 155 170 170 ASN ASN A . n 
A 1 156 GLN 156 171 171 GLN GLN A . n 
A 1 157 HIS 157 172 172 HIS HIS A . n 
A 1 158 THR 158 173 173 THR THR A . n 
A 1 159 LEU 159 174 174 LEU LEU A . n 
A 1 160 ILE 160 175 175 ILE ILE A . n 
A 1 161 PHE 161 176 176 PHE PHE A . n 
A 1 162 ASP 162 177 177 ASP ASP A . n 
A 1 163 GLY 163 178 178 GLY GLY A . n 
A 1 164 SER 164 179 ?   ?   ?   A . n 
A 1 165 THR 165 180 ?   ?   ?   A . n 
A 1 166 ASN 166 181 ?   ?   ?   A . n 
A 1 167 PRO 167 182 ?   ?   ?   A . n 
A 1 168 ALA 168 183 ?   ?   ?   A . n 
A 1 169 HIS 169 184 ?   ?   ?   A . n 
A 1 170 PRO 170 185 185 PRO PRO A . n 
A 1 171 LYS 171 186 186 LYS LYS A . n 
A 1 172 HIS 172 187 187 HIS HIS A . n 
A 1 173 ILE 173 188 188 ILE ILE A . n 
A 1 174 GLY 174 189 189 GLY GLY A . n 
A 1 175 SER 175 190 190 SER SER A . n 
A 1 176 ILE 176 191 191 ILE ILE A . n 
A 1 177 ASP 177 192 192 ASP ASP A . n 
A 1 178 PRO 178 193 193 PRO PRO A . n 
A 1 179 ASN 179 194 194 ASN ASN A . n 
A 1 180 CYS 180 195 195 CYS CYS A . n 
A 1 181 ASN 181 196 196 ASN ASN A . n 
A 1 182 VAL 182 197 197 VAL VAL A . n 
A 1 183 SER 183 198 198 SER SER A . n 
A 1 184 GLU 184 199 199 GLU GLU A . n 
A 1 185 VAL 185 200 200 VAL VAL A . n 
A 1 186 VAL 186 201 201 VAL VAL A . n 
A 1 187 LYS 187 202 202 LYS LYS A . n 
A 1 188 ASP 188 203 203 ASP ASP A . n 
A 1 189 ALA 189 204 204 ALA ALA A . n 
A 1 190 TYR 190 205 205 TYR TYR A . n 
A 1 191 ASP 191 206 206 ASP ASP A . n 
A 1 192 MET 192 207 207 MET MET A . n 
A 1 193 ALA 193 208 208 ALA ALA A . n 
A 1 194 LYS 194 209 209 LYS LYS A . n 
A 1 195 LEU 195 210 210 LEU LEU A . n 
A 1 196 LEU 196 211 211 LEU LEU A . n 
A 1 197 CYS 197 212 212 CYS CYS A . n 
A 1 198 ASP 198 213 213 ASP ASP A . n 
A 1 199 LYS 199 214 214 LYS LYS A . n 
A 1 200 TYR 200 215 215 TYR TYR A . n 
A 1 201 TYR 201 216 216 TYR TYR A . n 
A 1 202 MET 202 217 217 MET MET A . n 
A 1 203 ALA 203 218 218 ALA ALA A . n 
A 1 204 SER 204 219 219 SER SER A . n 
A 1 205 PRO 205 220 220 PRO PRO A . n 
A 1 206 ASP 206 221 221 ASP ASP A . n 
A 1 207 LEU 207 222 222 LEU LEU A . n 
A 1 208 GLU 208 223 223 GLU GLU A . n 
A 1 209 ILE 209 224 224 ILE ILE A . n 
A 1 210 GLN 210 225 225 GLN GLN A . n 
A 1 211 GLU 211 226 226 GLU GLU A . n 
A 1 212 ILE 212 227 227 ILE ILE A . n 
A 1 213 ASN 213 228 228 ASN ASN A . n 
A 1 214 ALA 214 229 229 ALA ALA A . n 
A 1 215 ALA 215 230 230 ALA ALA A . n 
A 1 216 ASN 216 231 231 ASN ASN A . n 
A 1 217 SER 217 232 232 SER SER A . n 
A 1 218 LYS 218 233 233 LYS LYS A . n 
A 1 219 GLN 219 234 234 GLN GLN A . n 
A 1 220 PRO 220 235 235 PRO PRO A . n 
A 1 221 ILE 221 236 236 ILE ILE A . n 
A 1 222 HIS 222 237 237 HIS HIS A . n 
A 1 223 MET 223 238 238 MET MET A . n 
A 1 224 VAL 224 239 239 VAL VAL A . n 
A 1 225 TYR 225 240 240 TYR TYR A . n 
A 1 226 VAL 226 241 241 VAL VAL A . n 
A 1 227 PRO 227 242 242 PRO PRO A . n 
A 1 228 SER 228 243 243 SER SER A . n 
A 1 229 HIS 229 244 244 HIS HIS A . n 
A 1 230 LEU 230 245 245 LEU LEU A . n 
A 1 231 TYR 231 246 246 TYR TYR A . n 
A 1 232 HIS 232 247 247 HIS HIS A . n 
A 1 233 MET 233 248 248 MET MET A . n 
A 1 234 LEU 234 249 249 LEU LEU A . n 
A 1 235 PHE 235 250 250 PHE PHE A . n 
A 1 236 GLU 236 251 251 GLU GLU A . n 
A 1 237 LEU 237 252 252 LEU LEU A . n 
A 1 238 PHE 238 253 253 PHE PHE A . n 
A 1 239 LYS 239 254 254 LYS LYS A . n 
A 1 240 ASN 240 255 255 ASN ASN A . n 
A 1 241 ALA 241 256 256 ALA ALA A . n 
A 1 242 MET 242 257 257 MET MET A . n 
A 1 243 ARG 243 258 258 ARG ARG A . n 
A 1 244 ALA 244 259 259 ALA ALA A . n 
A 1 245 THR 245 260 260 THR THR A . n 
A 1 246 VAL 246 261 261 VAL VAL A . n 
A 1 247 GLU 247 262 262 GLU GLU A . n 
A 1 248 SER 248 263 263 SER SER A . n 
A 1 249 HIS 249 264 264 HIS HIS A . n 
A 1 250 GLU 250 265 265 GLU GLU A . n 
A 1 251 SER 251 266 266 SER SER A . n 
A 1 252 SER 252 267 267 SER SER A . n 
A 1 253 LEU 253 268 268 LEU LEU A . n 
A 1 254 ILE 254 269 269 ILE ILE A . n 
A 1 255 LEU 255 270 270 LEU LEU A . n 
A 1 256 PRO 256 271 271 PRO PRO A . n 
A 1 257 PRO 257 272 272 PRO PRO A . n 
A 1 258 ILE 258 273 273 ILE ILE A . n 
A 1 259 LYS 259 274 274 LYS LYS A . n 
A 1 260 VAL 260 275 275 VAL VAL A . n 
A 1 261 MET 261 276 276 MET MET A . n 
A 1 262 VAL 262 277 277 VAL VAL A . n 
A 1 263 ALA 263 278 278 ALA ALA A . n 
A 1 264 LEU 264 279 279 LEU LEU A . n 
A 1 265 GLY 265 280 280 GLY GLY A . n 
A 1 266 GLU 266 281 281 GLU GLU A . n 
A 1 267 GLU 267 282 282 GLU GLU A . n 
A 1 268 ASP 268 283 283 ASP ASP A . n 
A 1 269 LEU 269 284 284 LEU LEU A . n 
A 1 270 SER 270 285 285 SER SER A . n 
A 1 271 ILE 271 286 286 ILE ILE A . n 
A 1 272 LYS 272 287 287 LYS LYS A . n 
A 1 273 MET 273 288 288 MET MET A . n 
A 1 274 SER 274 289 289 SER SER A . n 
A 1 275 ASP 275 290 290 ASP ASP A . n 
A 1 276 ARG 276 291 291 ARG ARG A . n 
A 1 277 GLY 277 292 292 GLY GLY A . n 
A 1 278 GLY 278 293 293 GLY GLY A . n 
A 1 279 GLY 279 294 294 GLY GLY A . n 
A 1 280 VAL 280 295 295 VAL VAL A . n 
A 1 281 PRO 281 296 296 PRO PRO A . n 
A 1 282 LEU 282 297 297 LEU LEU A . n 
A 1 283 ARG 283 298 298 ARG ARG A . n 
A 1 284 LYS 284 299 299 LYS LYS A . n 
A 1 285 ILE 285 300 300 ILE ILE A . n 
A 1 286 GLU 286 301 301 GLU GLU A . n 
A 1 287 ARG 287 302 302 ARG ARG A . n 
A 1 288 LEU 288 303 303 LEU LEU A . n 
A 1 289 PHE 289 304 304 PHE PHE A . n 
A 1 290 SER 290 305 305 SER SER A . n 
A 1 291 TYR 291 306 306 TYR TYR A . n 
A 1 292 MET 292 307 307 MET MET A . n 
A 1 293 TYR 293 308 308 TYR TYR A . n 
A 1 294 SER 294 309 309 SER SER A . n 
A 1 295 THR 295 310 310 THR THR A . n 
A 1 296 ALA 296 311 311 ALA ALA A . n 
A 1 297 PRO 297 312 312 PRO PRO A . n 
A 1 298 THR 298 313 313 THR THR A . n 
A 1 299 PRO 299 314 ?   ?   ?   A . n 
A 1 300 GLN 300 315 ?   ?   ?   A . n 
A 1 301 PRO 301 316 ?   ?   ?   A . n 
A 1 302 GLY 302 317 ?   ?   ?   A . n 
A 1 303 THR 303 318 ?   ?   ?   A . n 
A 1 304 GLY 304 319 ?   ?   ?   A . n 
A 1 305 GLY 305 320 ?   ?   ?   A . n 
A 1 306 THR 306 321 321 THR THR A . n 
A 1 307 PRO 307 322 322 PRO PRO A . n 
A 1 308 LEU 308 323 323 LEU LEU A . n 
A 1 309 ALA 309 324 324 ALA ALA A . n 
A 1 310 GLY 310 325 325 GLY GLY A . n 
A 1 311 PHE 311 326 326 PHE PHE A . n 
A 1 312 GLY 312 327 327 GLY GLY A . n 
A 1 313 TYR 313 328 328 TYR TYR A . n 
A 1 314 GLY 314 329 329 GLY GLY A . n 
A 1 315 LEU 315 330 330 LEU LEU A . n 
A 1 316 PRO 316 331 331 PRO PRO A . n 
A 1 317 ILE 317 332 332 ILE ILE A . n 
A 1 318 SER 318 333 333 SER SER A . n 
A 1 319 ARG 319 334 334 ARG ARG A . n 
A 1 320 LEU 320 335 335 LEU LEU A . n 
A 1 321 TYR 321 336 336 TYR TYR A . n 
A 1 322 ALA 322 337 337 ALA ALA A . n 
A 1 323 LYS 323 338 338 LYS LYS A . n 
A 1 324 TYR 324 339 339 TYR TYR A . n 
A 1 325 PHE 325 340 340 PHE PHE A . n 
A 1 326 GLN 326 341 341 GLN GLN A . n 
A 1 327 GLY 327 342 342 GLY GLY A . n 
A 1 328 ASP 328 343 343 ASP ASP A . n 
A 1 329 LEU 329 344 344 LEU LEU A . n 
A 1 330 GLN 330 345 345 GLN GLN A . n 
A 1 331 LEU 331 346 346 LEU LEU A . n 
A 1 332 PHE 332 347 347 PHE PHE A . n 
A 1 333 SER 333 348 348 SER SER A . n 
A 1 334 MET 334 349 349 MET MET A . n 
A 1 335 GLU 335 350 350 GLU GLU A . n 
A 1 336 GLY 336 351 351 GLY GLY A . n 
A 1 337 PHE 337 352 352 PHE PHE A . n 
A 1 338 GLY 338 353 353 GLY GLY A . n 
A 1 339 THR 339 354 354 THR THR A . n 
A 1 340 ASP 340 355 355 ASP ASP A . n 
A 1 341 ALA 341 356 356 ALA ALA A . n 
A 1 342 VAL 342 357 357 VAL VAL A . n 
A 1 343 ILE 343 358 358 ILE ILE A . n 
A 1 344 TYR 344 359 359 TYR TYR A . n 
A 1 345 LEU 345 360 360 LEU LEU A . n 
A 1 346 LYS 346 361 361 LYS LYS A . n 
A 1 347 ALA 347 362 362 ALA ALA A . n 
A 1 348 LEU 348 363 363 LEU LEU A . n 
A 1 349 SER 349 364 364 SER SER A . n 
A 1 350 THR 350 365 365 THR THR A . n 
A 1 351 ASP 351 366 366 ASP ASP A . n 
A 1 352 SER 352 367 367 SER SER A . n 
A 1 353 VAL 353 368 368 VAL VAL A . n 
A 1 354 GLU 354 369 369 GLU GLU A . n 
A 1 355 ARG 355 370 370 ARG ARG A . n 
A 1 356 LEU 356 371 371 LEU LEU A . n 
A 1 357 PRO 357 372 372 PRO PRO A . n 
A 1 358 VAL 358 373 373 VAL VAL A . n 
A 1 359 TYR 359 374 374 TYR TYR A . n 
A 1 360 ASN 360 375 375 ASN ASN A . n 
A 1 361 LYS 361 376 376 LYS LYS A . n 
A 1 362 SER 362 377 377 SER SER A . n 
A 1 363 ALA 363 378 378 ALA ALA A . n 
A 1 364 TRP 364 379 379 TRP TRP A . n 
A 1 365 ARG 365 380 380 ARG ARG A . n 
A 1 366 HIS 366 381 381 HIS HIS A . n 
A 1 367 TYR 367 382 382 TYR TYR A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1EQI 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1EQI 
_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 TF3   1   401 401 TF3   TF3 A . 
C 3 A1EQI 1   402 501 A1EQI L0R A . 
D 4 DMS   1   403 601 DMS   DMS A . 
E 4 DMS   1   404 701 DMS   DMS A . 
F 5 HOH   1   501 92  HOH   HOH A . 
F 5 HOH   2   502 33  HOH   HOH A . 
F 5 HOH   3   503 17  HOH   HOH A . 
F 5 HOH   4   504 60  HOH   HOH A . 
F 5 HOH   5   505 105 HOH   HOH A . 
F 5 HOH   6   506 41  HOH   HOH A . 
F 5 HOH   7   507 94  HOH   HOH A . 
F 5 HOH   8   508 109 HOH   HOH A . 
F 5 HOH   9   509 64  HOH   HOH A . 
F 5 HOH   10  510 88  HOH   HOH A . 
F 5 HOH   11  511 114 HOH   HOH A . 
F 5 HOH   12  512 43  HOH   HOH A . 
F 5 HOH   13  513 57  HOH   HOH A . 
F 5 HOH   14  514 34  HOH   HOH A . 
F 5 HOH   15  515 30  HOH   HOH A . 
F 5 HOH   16  516 18  HOH   HOH A . 
F 5 HOH   17  517 25  HOH   HOH A . 
F 5 HOH   18  518 55  HOH   HOH A . 
F 5 HOH   19  519 78  HOH   HOH A . 
F 5 HOH   20  520 52  HOH   HOH A . 
F 5 HOH   21  521 45  HOH   HOH A . 
F 5 HOH   22  522 3   HOH   HOH A . 
F 5 HOH   23  523 128 HOH   HOH A . 
F 5 HOH   24  524 56  HOH   HOH A . 
F 5 HOH   25  525 47  HOH   HOH A . 
F 5 HOH   26  526 80  HOH   HOH A . 
F 5 HOH   27  527 127 HOH   HOH A . 
F 5 HOH   28  528 74  HOH   HOH A . 
F 5 HOH   29  529 93  HOH   HOH A . 
F 5 HOH   30  530 149 HOH   HOH A . 
F 5 HOH   31  531 46  HOH   HOH A . 
F 5 HOH   32  532 23  HOH   HOH A . 
F 5 HOH   33  533 58  HOH   HOH A . 
F 5 HOH   34  534 77  HOH   HOH A . 
F 5 HOH   35  535 131 HOH   HOH A . 
F 5 HOH   36  536 75  HOH   HOH A . 
F 5 HOH   37  537 132 HOH   HOH A . 
F 5 HOH   38  538 103 HOH   HOH A . 
F 5 HOH   39  539 129 HOH   HOH A . 
F 5 HOH   40  540 66  HOH   HOH A . 
F 5 HOH   41  541 37  HOH   HOH A . 
F 5 HOH   42  542 21  HOH   HOH A . 
F 5 HOH   43  543 82  HOH   HOH A . 
F 5 HOH   44  544 24  HOH   HOH A . 
F 5 HOH   45  545 68  HOH   HOH A . 
F 5 HOH   46  546 32  HOH   HOH A . 
F 5 HOH   47  547 83  HOH   HOH A . 
F 5 HOH   48  548 12  HOH   HOH A . 
F 5 HOH   49  549 22  HOH   HOH A . 
F 5 HOH   50  550 67  HOH   HOH A . 
F 5 HOH   51  551 29  HOH   HOH A . 
F 5 HOH   52  552 89  HOH   HOH A . 
F 5 HOH   53  553 62  HOH   HOH A . 
F 5 HOH   54  554 79  HOH   HOH A . 
F 5 HOH   55  555 122 HOH   HOH A . 
F 5 HOH   56  556 120 HOH   HOH A . 
F 5 HOH   57  557 110 HOH   HOH A . 
F 5 HOH   58  558 61  HOH   HOH A . 
F 5 HOH   59  559 48  HOH   HOH A . 
F 5 HOH   60  560 124 HOH   HOH A . 
F 5 HOH   61  561 76  HOH   HOH A . 
F 5 HOH   62  562 100 HOH   HOH A . 
F 5 HOH   63  563 42  HOH   HOH A . 
F 5 HOH   64  564 15  HOH   HOH A . 
F 5 HOH   65  565 104 HOH   HOH A . 
F 5 HOH   66  566 51  HOH   HOH A . 
F 5 HOH   67  567 102 HOH   HOH A . 
F 5 HOH   68  568 115 HOH   HOH A . 
F 5 HOH   69  569 118 HOH   HOH A . 
F 5 HOH   70  570 140 HOH   HOH A . 
F 5 HOH   71  571 35  HOH   HOH A . 
F 5 HOH   72  572 70  HOH   HOH A . 
F 5 HOH   73  573 96  HOH   HOH A . 
F 5 HOH   74  574 144 HOH   HOH A . 
F 5 HOH   75  575 10  HOH   HOH A . 
F 5 HOH   76  576 19  HOH   HOH A . 
F 5 HOH   77  577 71  HOH   HOH A . 
F 5 HOH   78  578 27  HOH   HOH A . 
F 5 HOH   79  579 9   HOH   HOH A . 
F 5 HOH   80  580 145 HOH   HOH A . 
F 5 HOH   81  581 4   HOH   HOH A . 
F 5 HOH   82  582 49  HOH   HOH A . 
F 5 HOH   83  583 40  HOH   HOH A . 
F 5 HOH   84  584 86  HOH   HOH A . 
F 5 HOH   85  585 6   HOH   HOH A . 
F 5 HOH   86  586 130 HOH   HOH A . 
F 5 HOH   87  587 134 HOH   HOH A . 
F 5 HOH   88  588 20  HOH   HOH A . 
F 5 HOH   89  589 8   HOH   HOH A . 
F 5 HOH   90  590 101 HOH   HOH A . 
F 5 HOH   91  591 16  HOH   HOH A . 
F 5 HOH   92  592 117 HOH   HOH A . 
F 5 HOH   93  593 142 HOH   HOH A . 
F 5 HOH   94  594 63  HOH   HOH A . 
F 5 HOH   95  595 28  HOH   HOH A . 
F 5 HOH   96  596 5   HOH   HOH A . 
F 5 HOH   97  597 1   HOH   HOH A . 
F 5 HOH   98  598 108 HOH   HOH A . 
F 5 HOH   99  599 50  HOH   HOH A . 
F 5 HOH   100 600 73  HOH   HOH A . 
F 5 HOH   101 601 13  HOH   HOH A . 
F 5 HOH   102 602 85  HOH   HOH A . 
F 5 HOH   103 603 39  HOH   HOH A . 
F 5 HOH   104 604 91  HOH   HOH A . 
F 5 HOH   105 605 148 HOH   HOH A . 
F 5 HOH   106 606 65  HOH   HOH A . 
F 5 HOH   107 607 84  HOH   HOH A . 
F 5 HOH   108 608 113 HOH   HOH A . 
F 5 HOH   109 609 97  HOH   HOH A . 
F 5 HOH   110 610 135 HOH   HOH A . 
F 5 HOH   111 611 31  HOH   HOH A . 
F 5 HOH   112 612 137 HOH   HOH A . 
F 5 HOH   113 613 111 HOH   HOH A . 
F 5 HOH   114 614 98  HOH   HOH A . 
F 5 HOH   115 615 87  HOH   HOH A . 
F 5 HOH   116 616 106 HOH   HOH A . 
F 5 HOH   117 617 139 HOH   HOH A . 
F 5 HOH   118 618 7   HOH   HOH A . 
F 5 HOH   119 619 112 HOH   HOH A . 
F 5 HOH   120 620 116 HOH   HOH A . 
F 5 HOH   121 621 44  HOH   HOH A . 
F 5 HOH   122 622 2   HOH   HOH A . 
F 5 HOH   123 623 99  HOH   HOH A . 
F 5 HOH   124 624 95  HOH   HOH A . 
F 5 HOH   125 625 133 HOH   HOH A . 
F 5 HOH   126 626 59  HOH   HOH A . 
F 5 HOH   127 627 136 HOH   HOH A . 
F 5 HOH   128 628 53  HOH   HOH A . 
F 5 HOH   129 629 81  HOH   HOH A . 
F 5 HOH   130 630 11  HOH   HOH A . 
F 5 HOH   131 631 38  HOH   HOH A . 
F 5 HOH   132 632 119 HOH   HOH A . 
F 5 HOH   133 633 121 HOH   HOH A . 
F 5 HOH   134 634 69  HOH   HOH A . 
F 5 HOH   135 635 126 HOH   HOH A . 
F 5 HOH   136 636 147 HOH   HOH A . 
F 5 HOH   137 637 125 HOH   HOH A . 
F 5 HOH   138 638 36  HOH   HOH A . 
F 5 HOH   139 639 54  HOH   HOH A . 
F 5 HOH   140 640 146 HOH   HOH A . 
F 5 HOH   141 641 123 HOH   HOH A . 
F 5 HOH   142 642 141 HOH   HOH A . 
F 5 HOH   143 643 26  HOH   HOH A . 
F 5 HOH   144 644 143 HOH   HOH A . 
F 5 HOH   145 645 90  HOH   HOH A . 
F 5 HOH   146 646 14  HOH   HOH A . 
F 5 HOH   147 647 107 HOH   HOH A . 
F 5 HOH   148 648 72  HOH   HOH A . 
F 5 HOH   149 649 138 HOH   HOH A . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX  ? ? ? '(1.19rc4_4035: ???)' 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? .                     2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS     ? ? ? .                     3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? MOLREP  ? ? ? .                     4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  120.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9M3T 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     106.570 
_cell.length_a_esd                 ? 
_cell.length_b                     106.570 
_cell.length_b_esd                 ? 
_cell.length_c                     85.660 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        6 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         9M3T 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                172 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 64' 
_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                   9M3T 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             3.48 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          64.66 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_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    '0.42 M NaK tartrate, 0.1 M Na citrate, pH 5.6' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER X 16M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2020-12-22 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.9793 
_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                        'SSRF BEAMLINE BL17U' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.9793 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL17U 
_diffrn_source.pdbx_synchrotron_site       SSRF 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9M3T 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.08 
_reflns.d_resolution_low                               46.15 
_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                                     33296 
_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                           100.0 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                20.6 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          12.1 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               1.01 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.165 
_reflns.pdbx_Rpim_I_all                                0.037 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       684879 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.995 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.161 
_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                                    2.08 
_reflns_shell.d_res_low                                     2.14 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           54750 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             2623 
_reflns_shell.percent_possible_obs                          100.0 
_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                               20.9 
_reflns_shell.pdbx_chi_squared                              0.93 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     2.4 
_reflns_shell.pdbx_Rrim_I_all                               1.484 
_reflns_shell.pdbx_Rpim_I_all                               0.324 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.847 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  1.448 
_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                                 9M3T 
_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                            2.08 
_refine.ls_d_res_low                             46.15 
_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                     33286 
_refine.ls_number_reflns_R_free                  1579 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.97 
_refine.ls_percent_reflns_R_free                 4.74 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1759 
_refine.ls_R_factor_R_free                       0.2046 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1745 
_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.correlation_coeff_I_to_Fcsqd_work        ? 
_refine.correlation_coeff_I_to_Fcsqd_free        ? 
_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                          1.35 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.11 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 23.66 
_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                            0.20 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       2.08 
_refine_hist.d_res_low                        46.15 
_refine_hist.number_atoms_solvent             149 
_refine_hist.number_atoms_total               3050 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        2836 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         65 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.007  ? 3052 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.878  ? 4142 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 12.780 ? 1184 ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.054  ? 444  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.007  ? 537  ? 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.correlation_coeff_Fo_to_Fc 
_refine_ls_shell.correlation_coeff_Fo_to_Fc_free 
_refine_ls_shell.correlation_coeff_I_to_Fcsqd_work 
_refine_ls_shell.correlation_coeff_I_to_Fcsqd_free 
_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' 2.08 2.15  . . 145 2890 100.00 . . . . 0.2357 . . . . . . . . . . . . . . . 0.2843 
'X-RAY DIFFRACTION' 2.15 2.22  . . 131 2866 100.00 . . . . 0.2013 . . . . . . . . . . . . . . . 0.1993 
'X-RAY DIFFRACTION' 2.22 2.31  . . 161 2874 100.00 . . . . 0.2094 . . . . . . . . . . . . . . . 0.2425 
'X-RAY DIFFRACTION' 2.31 2.42  . . 133 2866 100.00 . . . . 0.1953 . . . . . . . . . . . . . . . 0.2443 
'X-RAY DIFFRACTION' 2.42 2.55  . . 139 2860 100.00 . . . . 0.1932 . . . . . . . . . . . . . . . 0.2149 
'X-RAY DIFFRACTION' 2.55 2.71  . . 110 2911 100.00 . . . . 0.1973 . . . . . . . . . . . . . . . 0.2209 
'X-RAY DIFFRACTION' 2.71 2.91  . . 178 2833 100.00 . . . . 0.2021 . . . . . . . . . . . . . . . 0.2348 
'X-RAY DIFFRACTION' 2.91 3.21  . . 166 2862 100.00 . . . . 0.1987 . . . . . . . . . . . . . . . 0.2285 
'X-RAY DIFFRACTION' 3.21 3.67  . . 155 2883 100.00 . . . . 0.1677 . . . . . . . . . . . . . . . 0.2085 
'X-RAY DIFFRACTION' 3.67 4.62  . . 143 2893 100.00 . . . . 0.1459 . . . . . . . . . . . . . . . 0.1657 
'X-RAY DIFFRACTION' 4.63 46.15 . . 118 2969 100.00 . . . . 0.1649 . . . . . . . . . . . . . . . 0.1932 
# 
_struct.entry_id                     9M3T 
_struct.title                        
'Crystal structure of human pyruvate dehydrogenase kinase isoform 2 in complex with ATP competitive inhibitor 22' 
_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        9M3T 
_struct_keywords.text            'ghkl atpase/kinase family, pyruvate dehydrogenase complex, mitochondrial kinase, transferase' 
_struct_keywords.pdbx_keywords   TRANSFERASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 4 ? 
E N N 4 ? 
F N N 5 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    PDK2_HUMAN 
_struct_ref.pdbx_db_accession          Q15119 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;APKYIEHFSKFSPSPLSMKQFLDFGSSNACEKTSFTFLRQELPVRLANIMKEINLLPDRVLSTPSVQLVQSWYVQSLLDI
MEFLDKDPEDHRTLSQFTDALVTIRNRHNDVVPTMAQGVLEYKDTYGDDPVSNQNIQYFLDRFYLSRISIRMLINQHTLI
FDGSTNPAHPKHIGSIDPNCNVSEVVKDAYDMAKLLCDKYYMASPDLEIQEINAANSKQPIHMVYVPSHLYHMLFELFKN
AMRATVESHESSLILPPIKVMVALGEEDLSIKMSDRGGGVPLRKIERLFSYMYSTAPTPQPGTGGTPLAGFGYGLPISRL
YAKYFQGDLQLFSMEGFGTDAVIYLKALSTDSVERLPVYNKSAWRHY
;
_struct_ref.pdbx_align_begin           16 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              9M3T 
_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                 367 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             Q15119 
_struct_ref_seq.db_align_beg                  16 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  382 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       16 
_struct_ref_seq.pdbx_auth_seq_align_end       382 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 6850  ? 
1 MORE         -13   ? 
1 'SSA (A^2)'  30740 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1,2 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   none 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
loop_
_pdbx_struct_oper_list.id 
_pdbx_struct_oper_list.type 
_pdbx_struct_oper_list.name 
_pdbx_struct_oper_list.symmetry_operation 
_pdbx_struct_oper_list.matrix[1][1] 
_pdbx_struct_oper_list.matrix[1][2] 
_pdbx_struct_oper_list.matrix[1][3] 
_pdbx_struct_oper_list.vector[1] 
_pdbx_struct_oper_list.matrix[2][1] 
_pdbx_struct_oper_list.matrix[2][2] 
_pdbx_struct_oper_list.matrix[2][3] 
_pdbx_struct_oper_list.vector[2] 
_pdbx_struct_oper_list.matrix[3][1] 
_pdbx_struct_oper_list.matrix[3][2] 
_pdbx_struct_oper_list.matrix[3][3] 
_pdbx_struct_oper_list.vector[3] 
1 'identity operation'         1_555 x,y,z     1.0000000000  0.0000000000 0.0000000000 0.0000000000   0.0000000000 1.0000000000  
0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000 0.0000000000 
2 'crystal symmetry operation' 4_655 -x+1,-y,z -1.0000000000 0.0000000000 0.0000000000 106.5700000000 0.0000000000 -1.0000000000 
0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000 0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 PRO A 2   ? LYS A 10  ? PRO A 17  LYS A 25  1 ? 9  
HELX_P HELX_P2  AA2 SER A 17  ? PHE A 24  ? SER A 32  PHE A 39  1 ? 8  
HELX_P HELX_P3  AA3 ALA A 29  ? ASN A 54  ? ALA A 44  ASN A 69  1 ? 26 
HELX_P HELX_P4  AA4 PRO A 57  ? SER A 62  ? PRO A 72  SER A 77  1 ? 6  
HELX_P HELX_P5  AA5 THR A 63  ? GLU A 82  ? THR A 78  GLU A 97  1 ? 20 
HELX_P HELX_P6  AA6 ASP A 90  ? HIS A 108 ? ASP A 105 HIS A 123 1 ? 19 
HELX_P HELX_P7  AA7 ASP A 110 ? TYR A 126 ? ASP A 125 TYR A 141 1 ? 17 
HELX_P HELX_P8  AA8 ASP A 129 ? PHE A 161 ? ASP A 144 PHE A 176 1 ? 33 
HELX_P HELX_P9  AA9 VAL A 182 ? MET A 202 ? VAL A 197 MET A 217 1 ? 21 
HELX_P HELX_P10 AB1 VAL A 226 ? HIS A 249 ? VAL A 241 HIS A 264 1 ? 24 
HELX_P HELX_P11 AB2 PRO A 281 ? ARG A 283 ? PRO A 296 ARG A 298 5 ? 3  
HELX_P HELX_P12 AB3 LYS A 284 ? SER A 290 ? LYS A 299 SER A 305 1 ? 7  
HELX_P HELX_P13 AB4 TYR A 313 ? PHE A 325 ? TYR A 328 PHE A 340 1 ? 13 
HELX_P HELX_P14 AB5 ASN A 360 ? TYR A 367 ? ASN A 375 TYR A 382 1 ? 8  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 2 ? 
AA2 ? 5 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA2 1 2 ? parallel      
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 ASP A 177 ? ASN A 181 ? ASP A 192 ASN A 196 
AA1 2 HIS A 222 ? TYR A 225 ? HIS A 237 TYR A 240 
AA2 1 LEU A 207 ? ASN A 213 ? LEU A 222 ASN A 228 
AA2 2 ILE A 258 ? LEU A 264 ? ILE A 273 LEU A 279 
AA2 3 ASP A 268 ? ASP A 275 ? ASP A 283 ASP A 290 
AA2 4 GLY A 338 ? LYS A 346 ? GLY A 353 LYS A 361 
AA2 5 ASP A 328 ? MET A 334 ? ASP A 343 MET A 349 
# 
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 ASP A 177 ? N ASP A 192 O TYR A 225 ? O TYR A 240 
AA2 1 2 N GLU A 208 ? N GLU A 223 O VAL A 260 ? O VAL A 275 
AA2 2 3 N ALA A 263 ? N ALA A 278 O SER A 270 ? O SER A 285 
AA2 3 4 N MET A 273 ? N MET A 288 O ALA A 341 ? O ALA A 356 
AA2 4 5 O ASP A 340 ? O ASP A 355 N PHE A 332 ? N PHE A 347 
# 
_pdbx_entry_details.entry_id                   9M3T 
_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_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 MET A 217 ? ? 54.64   8.35   
2 1 ARG A 291 ? ? -116.95 50.68  
3 1 PHE A 352 ? ? -129.18 -67.05 
# 
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 32.4140 -19.8899 -42.9165 0.5139 ? 0.0433  ? -0.1773 ? 0.5420 ? -0.0995 ? 0.5536 ? 3.3829 ? 
-0.3054 ? 0.6847  ? 2.5919 ? 0.4900 ? 2.2207 ? 0.2436 ? 0.8701  ? -0.3957 ? -0.4192 ? -0.0551 ? 0.2465  ? 0.3634 ? -0.4672 ? 
-0.0993 ? 
2 'X-RAY DIFFRACTION' ? refined 44.5537 -24.8512 -41.2541 0.4915 ? 0.0454  ? -0.1055 ? 0.3708 ? -0.1199 ? 0.4267 ? 3.9741 ? 
-0.8870 ? -0.3716 ? 1.4087 ? 0.0394 ? 2.3040 ? 0.3323 ? 0.4662  ? -0.7088 ? -0.1720 ? -0.1819 ? 0.1059  ? 0.3626 ? -0.1356 ? 
-0.1305 ? 
3 'X-RAY DIFFRACTION' ? refined 41.7531 -16.3622 -12.8828 0.4847 ? -0.0233 ? 0.1018  ? 0.3329 ? 0.0577  ? 0.3266 ? 2.8396 ? 0.8170 
? 0.7146  ? 4.0311 ? 0.5756 ? 2.6941 ? 0.0519 ? -0.3794 ? -0.1502 ? 0.6494  ? -0.0024 ? 0.1121  ? 0.3426 ? -0.2349 ? -0.0800 ? 
4 'X-RAY DIFFRACTION' ? refined 54.8056 -10.8418 -16.9216 0.4760 ? 0.0557  ? -0.0415 ? 0.3025 ? 0.0148  ? 0.3233 ? 3.0534 ? 1.1658 
? 0.1044  ? 2.2150 ? 0.3839 ? 1.5963 ? 0.0946 ? -0.1272 ? -0.2847 ? 0.2599  ? 0.0594  ? -0.2386 ? 0.2384 ? 0.0576  ? -0.1351 ? 
5 'X-RAY DIFFRACTION' ? refined 49.8534 -10.1583 -30.6678 0.4021 ? 0.0552  ? 0.0063  ? 0.3008 ? 0.0107  ? 0.2992 ? 2.5727 ? 0.2458 
? 0.9768  ? 2.1248 ? 0.6998 ? 1.9280 ? 0.1506 ? 0.4174  ? -0.2047 ? -0.2814 ? -0.0006 ? -0.0880 ? 0.1093 ? 0.1586  ? -0.0901 ? 
# 
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 16 through 70 )
;
2 'X-RAY DIFFRACTION' 2 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 71 through 175 )
;
3 'X-RAY DIFFRACTION' 3 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 176 through 241 )
;
4 'X-RAY DIFFRACTION' 4 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 242 through 304 )
;
5 'X-RAY DIFFRACTION' 5 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 305 through 382 )
;
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A SER 41  ? A SER 26  
2  1 Y 1 A SER 42  ? A SER 27  
3  1 Y 1 A SER 179 ? A SER 164 
4  1 Y 1 A THR 180 ? A THR 165 
5  1 Y 1 A ASN 181 ? A ASN 166 
6  1 Y 1 A PRO 182 ? A PRO 167 
7  1 Y 1 A ALA 183 ? A ALA 168 
8  1 Y 1 A HIS 184 ? A HIS 169 
9  1 Y 1 A PRO 314 ? A PRO 299 
10 1 Y 1 A GLN 315 ? A GLN 300 
11 1 Y 1 A PRO 316 ? A PRO 301 
12 1 Y 1 A GLY 317 ? A GLY 302 
13 1 Y 1 A THR 318 ? A THR 303 
14 1 Y 1 A GLY 319 ? A GLY 304 
15 1 Y 1 A GLY 320 ? A GLY 305 
# 
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 
A1EQI C10  C  N N 1   
A1EQI C11  C  Y N 2   
A1EQI C13  C  N N 3   
A1EQI C15  C  Y N 4   
A1EQI C16  C  Y N 5   
A1EQI C17  C  Y N 6   
A1EQI C18  C  Y N 7   
A1EQI C19  C  N N 8   
A1EQI C20  C  N N 9   
A1EQI C21  C  N N 10  
A1EQI C22  C  Y N 11  
A1EQI N    N  N N 12  
A1EQI C    C  Y N 13  
A1EQI O    O  N N 14  
A1EQI C1   C  Y N 15  
A1EQI C12  C  Y N 16  
A1EQI C14  C  N N 17  
A1EQI C2   C  N N 18  
A1EQI C3   C  Y N 19  
A1EQI C4   C  Y N 20  
A1EQI C5   C  Y N 21  
A1EQI C6   C  N R 22  
A1EQI C7   C  N N 23  
A1EQI C8   C  N S 24  
A1EQI C9   C  N N 25  
A1EQI F    F  N N 26  
A1EQI N1   N  N N 27  
A1EQI N2   N  N N 28  
A1EQI N3   N  N N 29  
A1EQI O1   O  N N 30  
A1EQI O2   O  N N 31  
A1EQI CL   CL N N 32  
A1EQI H1   H  N N 33  
A1EQI H2   H  N N 34  
A1EQI H3   H  N N 35  
A1EQI H4   H  N N 36  
A1EQI H5   H  N N 37  
A1EQI H6   H  N N 38  
A1EQI H7   H  N N 39  
A1EQI H8   H  N N 40  
A1EQI H9   H  N N 41  
A1EQI H10  H  N N 42  
A1EQI H11  H  N N 43  
A1EQI H12  H  N N 44  
A1EQI H13  H  N N 45  
A1EQI H14  H  N N 46  
A1EQI H15  H  N N 47  
A1EQI H16  H  N N 48  
A1EQI H17  H  N N 49  
A1EQI H18  H  N N 50  
A1EQI H19  H  N N 51  
A1EQI H20  H  N N 52  
A1EQI H21  H  N N 53  
A1EQI H22  H  N N 54  
A1EQI H23  H  N N 55  
A1EQI H25  H  N N 56  
A1EQI H26  H  N N 57  
A1EQI H27  H  N N 58  
ALA   N    N  N N 59  
ALA   CA   C  N S 60  
ALA   C    C  N N 61  
ALA   O    O  N N 62  
ALA   CB   C  N N 63  
ALA   OXT  O  N N 64  
ALA   H    H  N N 65  
ALA   H2   H  N N 66  
ALA   HA   H  N N 67  
ALA   HB1  H  N N 68  
ALA   HB2  H  N N 69  
ALA   HB3  H  N N 70  
ALA   HXT  H  N N 71  
ARG   N    N  N N 72  
ARG   CA   C  N S 73  
ARG   C    C  N N 74  
ARG   O    O  N N 75  
ARG   CB   C  N N 76  
ARG   CG   C  N N 77  
ARG   CD   C  N N 78  
ARG   NE   N  N N 79  
ARG   CZ   C  N N 80  
ARG   NH1  N  N N 81  
ARG   NH2  N  N N 82  
ARG   OXT  O  N N 83  
ARG   H    H  N N 84  
ARG   H2   H  N N 85  
ARG   HA   H  N N 86  
ARG   HB2  H  N N 87  
ARG   HB3  H  N N 88  
ARG   HG2  H  N N 89  
ARG   HG3  H  N N 90  
ARG   HD2  H  N N 91  
ARG   HD3  H  N N 92  
ARG   HE   H  N N 93  
ARG   HH11 H  N N 94  
ARG   HH12 H  N N 95  
ARG   HH21 H  N N 96  
ARG   HH22 H  N N 97  
ARG   HXT  H  N N 98  
ASN   N    N  N N 99  
ASN   CA   C  N S 100 
ASN   C    C  N N 101 
ASN   O    O  N N 102 
ASN   CB   C  N N 103 
ASN   CG   C  N N 104 
ASN   OD1  O  N N 105 
ASN   ND2  N  N N 106 
ASN   OXT  O  N N 107 
ASN   H    H  N N 108 
ASN   H2   H  N N 109 
ASN   HA   H  N N 110 
ASN   HB2  H  N N 111 
ASN   HB3  H  N N 112 
ASN   HD21 H  N N 113 
ASN   HD22 H  N N 114 
ASN   HXT  H  N N 115 
ASP   N    N  N N 116 
ASP   CA   C  N S 117 
ASP   C    C  N N 118 
ASP   O    O  N N 119 
ASP   CB   C  N N 120 
ASP   CG   C  N N 121 
ASP   OD1  O  N N 122 
ASP   OD2  O  N N 123 
ASP   OXT  O  N N 124 
ASP   H    H  N N 125 
ASP   H2   H  N N 126 
ASP   HA   H  N N 127 
ASP   HB2  H  N N 128 
ASP   HB3  H  N N 129 
ASP   HD2  H  N N 130 
ASP   HXT  H  N N 131 
CYS   N    N  N N 132 
CYS   CA   C  N R 133 
CYS   C    C  N N 134 
CYS   O    O  N N 135 
CYS   CB   C  N N 136 
CYS   SG   S  N N 137 
CYS   OXT  O  N N 138 
CYS   H    H  N N 139 
CYS   H2   H  N N 140 
CYS   HA   H  N N 141 
CYS   HB2  H  N N 142 
CYS   HB3  H  N N 143 
CYS   HG   H  N N 144 
CYS   HXT  H  N N 145 
DMS   S    S  N N 146 
DMS   O    O  N N 147 
DMS   C1   C  N N 148 
DMS   C2   C  N N 149 
DMS   H11  H  N N 150 
DMS   H12  H  N N 151 
DMS   H13  H  N N 152 
DMS   H21  H  N N 153 
DMS   H22  H  N N 154 
DMS   H23  H  N N 155 
GLN   N    N  N N 156 
GLN   CA   C  N S 157 
GLN   C    C  N N 158 
GLN   O    O  N N 159 
GLN   CB   C  N N 160 
GLN   CG   C  N N 161 
GLN   CD   C  N N 162 
GLN   OE1  O  N N 163 
GLN   NE2  N  N N 164 
GLN   OXT  O  N N 165 
GLN   H    H  N N 166 
GLN   H2   H  N N 167 
GLN   HA   H  N N 168 
GLN   HB2  H  N N 169 
GLN   HB3  H  N N 170 
GLN   HG2  H  N N 171 
GLN   HG3  H  N N 172 
GLN   HE21 H  N N 173 
GLN   HE22 H  N N 174 
GLN   HXT  H  N N 175 
GLU   N    N  N N 176 
GLU   CA   C  N S 177 
GLU   C    C  N N 178 
GLU   O    O  N N 179 
GLU   CB   C  N N 180 
GLU   CG   C  N N 181 
GLU   CD   C  N N 182 
GLU   OE1  O  N N 183 
GLU   OE2  O  N N 184 
GLU   OXT  O  N N 185 
GLU   H    H  N N 186 
GLU   H2   H  N N 187 
GLU   HA   H  N N 188 
GLU   HB2  H  N N 189 
GLU   HB3  H  N N 190 
GLU   HG2  H  N N 191 
GLU   HG3  H  N N 192 
GLU   HE2  H  N N 193 
GLU   HXT  H  N N 194 
GLY   N    N  N N 195 
GLY   CA   C  N N 196 
GLY   C    C  N N 197 
GLY   O    O  N N 198 
GLY   OXT  O  N N 199 
GLY   H    H  N N 200 
GLY   H2   H  N N 201 
GLY   HA2  H  N N 202 
GLY   HA3  H  N N 203 
GLY   HXT  H  N N 204 
HIS   N    N  N N 205 
HIS   CA   C  N S 206 
HIS   C    C  N N 207 
HIS   O    O  N N 208 
HIS   CB   C  N N 209 
HIS   CG   C  Y N 210 
HIS   ND1  N  Y N 211 
HIS   CD2  C  Y N 212 
HIS   CE1  C  Y N 213 
HIS   NE2  N  Y N 214 
HIS   OXT  O  N N 215 
HIS   H    H  N N 216 
HIS   H2   H  N N 217 
HIS   HA   H  N N 218 
HIS   HB2  H  N N 219 
HIS   HB3  H  N N 220 
HIS   HD1  H  N N 221 
HIS   HD2  H  N N 222 
HIS   HE1  H  N N 223 
HIS   HE2  H  N N 224 
HIS   HXT  H  N N 225 
HOH   O    O  N N 226 
HOH   H1   H  N N 227 
HOH   H2   H  N N 228 
ILE   N    N  N N 229 
ILE   CA   C  N S 230 
ILE   C    C  N N 231 
ILE   O    O  N N 232 
ILE   CB   C  N S 233 
ILE   CG1  C  N N 234 
ILE   CG2  C  N N 235 
ILE   CD1  C  N N 236 
ILE   OXT  O  N N 237 
ILE   H    H  N N 238 
ILE   H2   H  N N 239 
ILE   HA   H  N N 240 
ILE   HB   H  N N 241 
ILE   HG12 H  N N 242 
ILE   HG13 H  N N 243 
ILE   HG21 H  N N 244 
ILE   HG22 H  N N 245 
ILE   HG23 H  N N 246 
ILE   HD11 H  N N 247 
ILE   HD12 H  N N 248 
ILE   HD13 H  N N 249 
ILE   HXT  H  N N 250 
LEU   N    N  N N 251 
LEU   CA   C  N S 252 
LEU   C    C  N N 253 
LEU   O    O  N N 254 
LEU   CB   C  N N 255 
LEU   CG   C  N N 256 
LEU   CD1  C  N N 257 
LEU   CD2  C  N N 258 
LEU   OXT  O  N N 259 
LEU   H    H  N N 260 
LEU   H2   H  N N 261 
LEU   HA   H  N N 262 
LEU   HB2  H  N N 263 
LEU   HB3  H  N N 264 
LEU   HG   H  N N 265 
LEU   HD11 H  N N 266 
LEU   HD12 H  N N 267 
LEU   HD13 H  N N 268 
LEU   HD21 H  N N 269 
LEU   HD22 H  N N 270 
LEU   HD23 H  N N 271 
LEU   HXT  H  N N 272 
LYS   N    N  N N 273 
LYS   CA   C  N S 274 
LYS   C    C  N N 275 
LYS   O    O  N N 276 
LYS   CB   C  N N 277 
LYS   CG   C  N N 278 
LYS   CD   C  N N 279 
LYS   CE   C  N N 280 
LYS   NZ   N  N N 281 
LYS   OXT  O  N N 282 
LYS   H    H  N N 283 
LYS   H2   H  N N 284 
LYS   HA   H  N N 285 
LYS   HB2  H  N N 286 
LYS   HB3  H  N N 287 
LYS   HG2  H  N N 288 
LYS   HG3  H  N N 289 
LYS   HD2  H  N N 290 
LYS   HD3  H  N N 291 
LYS   HE2  H  N N 292 
LYS   HE3  H  N N 293 
LYS   HZ1  H  N N 294 
LYS   HZ2  H  N N 295 
LYS   HZ3  H  N N 296 
LYS   HXT  H  N N 297 
MET   N    N  N N 298 
MET   CA   C  N S 299 
MET   C    C  N N 300 
MET   O    O  N N 301 
MET   CB   C  N N 302 
MET   CG   C  N N 303 
MET   SD   S  N N 304 
MET   CE   C  N N 305 
MET   OXT  O  N N 306 
MET   H    H  N N 307 
MET   H2   H  N N 308 
MET   HA   H  N N 309 
MET   HB2  H  N N 310 
MET   HB3  H  N N 311 
MET   HG2  H  N N 312 
MET   HG3  H  N N 313 
MET   HE1  H  N N 314 
MET   HE2  H  N N 315 
MET   HE3  H  N N 316 
MET   HXT  H  N N 317 
PHE   N    N  N N 318 
PHE   CA   C  N S 319 
PHE   C    C  N N 320 
PHE   O    O  N N 321 
PHE   CB   C  N N 322 
PHE   CG   C  Y N 323 
PHE   CD1  C  Y N 324 
PHE   CD2  C  Y N 325 
PHE   CE1  C  Y N 326 
PHE   CE2  C  Y N 327 
PHE   CZ   C  Y N 328 
PHE   OXT  O  N N 329 
PHE   H    H  N N 330 
PHE   H2   H  N N 331 
PHE   HA   H  N N 332 
PHE   HB2  H  N N 333 
PHE   HB3  H  N N 334 
PHE   HD1  H  N N 335 
PHE   HD2  H  N N 336 
PHE   HE1  H  N N 337 
PHE   HE2  H  N N 338 
PHE   HZ   H  N N 339 
PHE   HXT  H  N N 340 
PRO   N    N  N N 341 
PRO   CA   C  N S 342 
PRO   C    C  N N 343 
PRO   O    O  N N 344 
PRO   CB   C  N N 345 
PRO   CG   C  N N 346 
PRO   CD   C  N N 347 
PRO   OXT  O  N N 348 
PRO   H    H  N N 349 
PRO   HA   H  N N 350 
PRO   HB2  H  N N 351 
PRO   HB3  H  N N 352 
PRO   HG2  H  N N 353 
PRO   HG3  H  N N 354 
PRO   HD2  H  N N 355 
PRO   HD3  H  N N 356 
PRO   HXT  H  N N 357 
SER   N    N  N N 358 
SER   CA   C  N S 359 
SER   C    C  N N 360 
SER   O    O  N N 361 
SER   CB   C  N N 362 
SER   OG   O  N N 363 
SER   OXT  O  N N 364 
SER   H    H  N N 365 
SER   H2   H  N N 366 
SER   HA   H  N N 367 
SER   HB2  H  N N 368 
SER   HB3  H  N N 369 
SER   HG   H  N N 370 
SER   HXT  H  N N 371 
TF3   C1   C  Y N 372 
TF3   C2   C  Y N 373 
TF3   C3   C  Y N 374 
TF3   O1   O  N N 375 
TF3   C4   C  Y N 376 
TF3   CL1  CL N N 377 
TF3   C5   C  Y N 378 
TF3   C6   C  N N 379 
TF3   C7   C  Y N 380 
TF3   C8   C  Y N 381 
TF3   C9   C  N N 382 
TF3   C10  C  Y N 383 
TF3   C11  C  Y N 384 
TF3   C12  C  N N 385 
TF3   C13  C  Y N 386 
TF3   C14  C  Y N 387 
TF3   N1   N  N N 388 
TF3   O2   O  N N 389 
TF3   C15  C  Y N 390 
TF3   C16  C  N N 391 
TF3   C17  C  N N 392 
TF3   C18  C  N N 393 
TF3   C19  C  N N 394 
TF3   C20  C  N N 395 
TF3   N2   N  N N 396 
TF3   H3   H  N N 397 
TF3   H4   H  N N 398 
TF3   H5   H  N N 399 
TF3   H6C1 H  N N 400 
TF3   H6C2 H  N N 401 
TF3   H9C1 H  N N 402 
TF3   H9C2 H  N N 403 
TF3   H10  H  N N 404 
TF3   H11  H  N N 405 
TF3   H13  H  N N 406 
TF3   H14  H  N N 407 
TF3   H1   H  N N 408 
TF3   H161 H  N N 409 
TF3   H162 H  N N 410 
TF3   H17  H  N N 411 
TF3   H181 H  N N 412 
TF3   H182 H  N N 413 
TF3   H191 H  N N 414 
TF3   H192 H  N N 415 
TF3   H193 H  N N 416 
TF3   H201 H  N N 417 
TF3   H202 H  N N 418 
TF3   H203 H  N N 419 
TF3   H2N1 H  N N 420 
TF3   H2N2 H  N N 421 
THR   N    N  N N 422 
THR   CA   C  N S 423 
THR   C    C  N N 424 
THR   O    O  N N 425 
THR   CB   C  N R 426 
THR   OG1  O  N N 427 
THR   CG2  C  N N 428 
THR   OXT  O  N N 429 
THR   H    H  N N 430 
THR   H2   H  N N 431 
THR   HA   H  N N 432 
THR   HB   H  N N 433 
THR   HG1  H  N N 434 
THR   HG21 H  N N 435 
THR   HG22 H  N N 436 
THR   HG23 H  N N 437 
THR   HXT  H  N N 438 
TRP   N    N  N N 439 
TRP   CA   C  N S 440 
TRP   C    C  N N 441 
TRP   O    O  N N 442 
TRP   CB   C  N N 443 
TRP   CG   C  Y N 444 
TRP   CD1  C  Y N 445 
TRP   CD2  C  Y N 446 
TRP   NE1  N  Y N 447 
TRP   CE2  C  Y N 448 
TRP   CE3  C  Y N 449 
TRP   CZ2  C  Y N 450 
TRP   CZ3  C  Y N 451 
TRP   CH2  C  Y N 452 
TRP   OXT  O  N N 453 
TRP   H    H  N N 454 
TRP   H2   H  N N 455 
TRP   HA   H  N N 456 
TRP   HB2  H  N N 457 
TRP   HB3  H  N N 458 
TRP   HD1  H  N N 459 
TRP   HE1  H  N N 460 
TRP   HE3  H  N N 461 
TRP   HZ2  H  N N 462 
TRP   HZ3  H  N N 463 
TRP   HH2  H  N N 464 
TRP   HXT  H  N N 465 
TYR   N    N  N N 466 
TYR   CA   C  N S 467 
TYR   C    C  N N 468 
TYR   O    O  N N 469 
TYR   CB   C  N N 470 
TYR   CG   C  Y N 471 
TYR   CD1  C  Y N 472 
TYR   CD2  C  Y N 473 
TYR   CE1  C  Y N 474 
TYR   CE2  C  Y N 475 
TYR   CZ   C  Y N 476 
TYR   OH   O  N N 477 
TYR   OXT  O  N N 478 
TYR   H    H  N N 479 
TYR   H2   H  N N 480 
TYR   HA   H  N N 481 
TYR   HB2  H  N N 482 
TYR   HB3  H  N N 483 
TYR   HD1  H  N N 484 
TYR   HD2  H  N N 485 
TYR   HE1  H  N N 486 
TYR   HE2  H  N N 487 
TYR   HH   H  N N 488 
TYR   HXT  H  N N 489 
VAL   N    N  N N 490 
VAL   CA   C  N S 491 
VAL   C    C  N N 492 
VAL   O    O  N N 493 
VAL   CB   C  N N 494 
VAL   CG1  C  N N 495 
VAL   CG2  C  N N 496 
VAL   OXT  O  N N 497 
VAL   H    H  N N 498 
VAL   H2   H  N N 499 
VAL   HA   H  N N 500 
VAL   HB   H  N N 501 
VAL   HG11 H  N N 502 
VAL   HG12 H  N N 503 
VAL   HG13 H  N N 504 
VAL   HG21 H  N N 505 
VAL   HG22 H  N N 506 
VAL   HG23 H  N N 507 
VAL   HXT  H  N N 508 
# 
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 
A1EQI CL  C    sing N N 1   
A1EQI O   C2   doub N N 2   
A1EQI C2  C1   sing N N 3   
A1EQI C2  O1   sing N N 4   
A1EQI C   C1   doub Y N 5   
A1EQI C   C22  sing Y N 6   
A1EQI C1  C3   sing Y N 7   
A1EQI C22 C5   doub Y N 8   
A1EQI C3  C4   doub Y N 9   
A1EQI C5  C4   sing Y N 10  
A1EQI C5  N    sing N N 11  
A1EQI N   C6   sing N N 12  
A1EQI F   C16  sing N N 13  
A1EQI C6  C7   sing N N 14  
A1EQI C6  C21  sing N N 15  
A1EQI C7  N1   sing N N 16  
A1EQI C17 C16  doub Y N 17  
A1EQI C17 C18  sing Y N 18  
A1EQI C16 C15  sing Y N 19  
A1EQI C21 C20  sing N N 20  
A1EQI C9  C8   sing N N 21  
A1EQI C18 C8   sing N N 22  
A1EQI C18 C11  doub Y N 23  
A1EQI N1  C8   sing N N 24  
A1EQI N1  C19  sing N N 25  
A1EQI C8  C10  sing N N 26  
A1EQI C15 C12  doub Y N 27  
A1EQI C19 C20  sing N N 28  
A1EQI C11 C12  sing Y N 29  
A1EQI C11 N2   sing N N 30  
A1EQI C12 N3   sing N N 31  
A1EQI C10 N2   sing N N 32  
A1EQI C10 O2   doub N N 33  
A1EQI N3  C13  sing N N 34  
A1EQI C13 C14  sing N N 35  
A1EQI C13 H1   sing N N 36  
A1EQI C13 H2   sing N N 37  
A1EQI C15 H3   sing N N 38  
A1EQI C17 H4   sing N N 39  
A1EQI C19 H5   sing N N 40  
A1EQI C19 H6   sing N N 41  
A1EQI C20 H7   sing N N 42  
A1EQI C20 H8   sing N N 43  
A1EQI C21 H9   sing N N 44  
A1EQI C21 H10  sing N N 45  
A1EQI C22 H11  sing N N 46  
A1EQI N   H12  sing N N 47  
A1EQI C14 H13  sing N N 48  
A1EQI C14 H14  sing N N 49  
A1EQI C14 H15  sing N N 50  
A1EQI C3  H16  sing N N 51  
A1EQI C4  H17  sing N N 52  
A1EQI C6  H18  sing N N 53  
A1EQI C7  H19  sing N N 54  
A1EQI C7  H20  sing N N 55  
A1EQI C9  H21  sing N N 56  
A1EQI C9  H22  sing N N 57  
A1EQI C9  H23  sing N N 58  
A1EQI N2  H25  sing N N 59  
A1EQI N3  H26  sing N N 60  
A1EQI O1  H27  sing N N 61  
ALA   N   CA   sing N N 62  
ALA   N   H    sing N N 63  
ALA   N   H2   sing N N 64  
ALA   CA  C    sing N N 65  
ALA   CA  CB   sing N N 66  
ALA   CA  HA   sing N N 67  
ALA   C   O    doub N N 68  
ALA   C   OXT  sing N N 69  
ALA   CB  HB1  sing N N 70  
ALA   CB  HB2  sing N N 71  
ALA   CB  HB3  sing N N 72  
ALA   OXT HXT  sing N N 73  
ARG   N   CA   sing N N 74  
ARG   N   H    sing N N 75  
ARG   N   H2   sing N N 76  
ARG   CA  C    sing N N 77  
ARG   CA  CB   sing N N 78  
ARG   CA  HA   sing N N 79  
ARG   C   O    doub N N 80  
ARG   C   OXT  sing N N 81  
ARG   CB  CG   sing N N 82  
ARG   CB  HB2  sing N N 83  
ARG   CB  HB3  sing N N 84  
ARG   CG  CD   sing N N 85  
ARG   CG  HG2  sing N N 86  
ARG   CG  HG3  sing N N 87  
ARG   CD  NE   sing N N 88  
ARG   CD  HD2  sing N N 89  
ARG   CD  HD3  sing N N 90  
ARG   NE  CZ   sing N N 91  
ARG   NE  HE   sing N N 92  
ARG   CZ  NH1  sing N N 93  
ARG   CZ  NH2  doub N N 94  
ARG   NH1 HH11 sing N N 95  
ARG   NH1 HH12 sing N N 96  
ARG   NH2 HH21 sing N N 97  
ARG   NH2 HH22 sing N N 98  
ARG   OXT HXT  sing N N 99  
ASN   N   CA   sing N N 100 
ASN   N   H    sing N N 101 
ASN   N   H2   sing N N 102 
ASN   CA  C    sing N N 103 
ASN   CA  CB   sing N N 104 
ASN   CA  HA   sing N N 105 
ASN   C   O    doub N N 106 
ASN   C   OXT  sing N N 107 
ASN   CB  CG   sing N N 108 
ASN   CB  HB2  sing N N 109 
ASN   CB  HB3  sing N N 110 
ASN   CG  OD1  doub N N 111 
ASN   CG  ND2  sing N N 112 
ASN   ND2 HD21 sing N N 113 
ASN   ND2 HD22 sing N N 114 
ASN   OXT HXT  sing N N 115 
ASP   N   CA   sing N N 116 
ASP   N   H    sing N N 117 
ASP   N   H2   sing N N 118 
ASP   CA  C    sing N N 119 
ASP   CA  CB   sing N N 120 
ASP   CA  HA   sing N N 121 
ASP   C   O    doub N N 122 
ASP   C   OXT  sing N N 123 
ASP   CB  CG   sing N N 124 
ASP   CB  HB2  sing N N 125 
ASP   CB  HB3  sing N N 126 
ASP   CG  OD1  doub N N 127 
ASP   CG  OD2  sing N N 128 
ASP   OD2 HD2  sing N N 129 
ASP   OXT HXT  sing N N 130 
CYS   N   CA   sing N N 131 
CYS   N   H    sing N N 132 
CYS   N   H2   sing N N 133 
CYS   CA  C    sing N N 134 
CYS   CA  CB   sing N N 135 
CYS   CA  HA   sing N N 136 
CYS   C   O    doub N N 137 
CYS   C   OXT  sing N N 138 
CYS   CB  SG   sing N N 139 
CYS   CB  HB2  sing N N 140 
CYS   CB  HB3  sing N N 141 
CYS   SG  HG   sing N N 142 
CYS   OXT HXT  sing N N 143 
DMS   S   O    doub N N 144 
DMS   S   C1   sing N N 145 
DMS   S   C2   sing N N 146 
DMS   C1  H11  sing N N 147 
DMS   C1  H12  sing N N 148 
DMS   C1  H13  sing N N 149 
DMS   C2  H21  sing N N 150 
DMS   C2  H22  sing N N 151 
DMS   C2  H23  sing N N 152 
GLN   N   CA   sing N N 153 
GLN   N   H    sing N N 154 
GLN   N   H2   sing N N 155 
GLN   CA  C    sing N N 156 
GLN   CA  CB   sing N N 157 
GLN   CA  HA   sing N N 158 
GLN   C   O    doub N N 159 
GLN   C   OXT  sing N N 160 
GLN   CB  CG   sing N N 161 
GLN   CB  HB2  sing N N 162 
GLN   CB  HB3  sing N N 163 
GLN   CG  CD   sing N N 164 
GLN   CG  HG2  sing N N 165 
GLN   CG  HG3  sing N N 166 
GLN   CD  OE1  doub N N 167 
GLN   CD  NE2  sing N N 168 
GLN   NE2 HE21 sing N N 169 
GLN   NE2 HE22 sing N N 170 
GLN   OXT HXT  sing N N 171 
GLU   N   CA   sing N N 172 
GLU   N   H    sing N N 173 
GLU   N   H2   sing N N 174 
GLU   CA  C    sing N N 175 
GLU   CA  CB   sing N N 176 
GLU   CA  HA   sing N N 177 
GLU   C   O    doub N N 178 
GLU   C   OXT  sing N N 179 
GLU   CB  CG   sing N N 180 
GLU   CB  HB2  sing N N 181 
GLU   CB  HB3  sing N N 182 
GLU   CG  CD   sing N N 183 
GLU   CG  HG2  sing N N 184 
GLU   CG  HG3  sing N N 185 
GLU   CD  OE1  doub N N 186 
GLU   CD  OE2  sing N N 187 
GLU   OE2 HE2  sing N N 188 
GLU   OXT HXT  sing N N 189 
GLY   N   CA   sing N N 190 
GLY   N   H    sing N N 191 
GLY   N   H2   sing N N 192 
GLY   CA  C    sing N N 193 
GLY   CA  HA2  sing N N 194 
GLY   CA  HA3  sing N N 195 
GLY   C   O    doub N N 196 
GLY   C   OXT  sing N N 197 
GLY   OXT HXT  sing N N 198 
HIS   N   CA   sing N N 199 
HIS   N   H    sing N N 200 
HIS   N   H2   sing N N 201 
HIS   CA  C    sing N N 202 
HIS   CA  CB   sing N N 203 
HIS   CA  HA   sing N N 204 
HIS   C   O    doub N N 205 
HIS   C   OXT  sing N N 206 
HIS   CB  CG   sing N N 207 
HIS   CB  HB2  sing N N 208 
HIS   CB  HB3  sing N N 209 
HIS   CG  ND1  sing Y N 210 
HIS   CG  CD2  doub Y N 211 
HIS   ND1 CE1  doub Y N 212 
HIS   ND1 HD1  sing N N 213 
HIS   CD2 NE2  sing Y N 214 
HIS   CD2 HD2  sing N N 215 
HIS   CE1 NE2  sing Y N 216 
HIS   CE1 HE1  sing N N 217 
HIS   NE2 HE2  sing N N 218 
HIS   OXT HXT  sing N N 219 
HOH   O   H1   sing N N 220 
HOH   O   H2   sing N N 221 
ILE   N   CA   sing N N 222 
ILE   N   H    sing N N 223 
ILE   N   H2   sing N N 224 
ILE   CA  C    sing N N 225 
ILE   CA  CB   sing N N 226 
ILE   CA  HA   sing N N 227 
ILE   C   O    doub N N 228 
ILE   C   OXT  sing N N 229 
ILE   CB  CG1  sing N N 230 
ILE   CB  CG2  sing N N 231 
ILE   CB  HB   sing N N 232 
ILE   CG1 CD1  sing N N 233 
ILE   CG1 HG12 sing N N 234 
ILE   CG1 HG13 sing N N 235 
ILE   CG2 HG21 sing N N 236 
ILE   CG2 HG22 sing N N 237 
ILE   CG2 HG23 sing N N 238 
ILE   CD1 HD11 sing N N 239 
ILE   CD1 HD12 sing N N 240 
ILE   CD1 HD13 sing N N 241 
ILE   OXT HXT  sing N N 242 
LEU   N   CA   sing N N 243 
LEU   N   H    sing N N 244 
LEU   N   H2   sing N N 245 
LEU   CA  C    sing N N 246 
LEU   CA  CB   sing N N 247 
LEU   CA  HA   sing N N 248 
LEU   C   O    doub N N 249 
LEU   C   OXT  sing N N 250 
LEU   CB  CG   sing N N 251 
LEU   CB  HB2  sing N N 252 
LEU   CB  HB3  sing N N 253 
LEU   CG  CD1  sing N N 254 
LEU   CG  CD2  sing N N 255 
LEU   CG  HG   sing N N 256 
LEU   CD1 HD11 sing N N 257 
LEU   CD1 HD12 sing N N 258 
LEU   CD1 HD13 sing N N 259 
LEU   CD2 HD21 sing N N 260 
LEU   CD2 HD22 sing N N 261 
LEU   CD2 HD23 sing N N 262 
LEU   OXT HXT  sing N N 263 
LYS   N   CA   sing N N 264 
LYS   N   H    sing N N 265 
LYS   N   H2   sing N N 266 
LYS   CA  C    sing N N 267 
LYS   CA  CB   sing N N 268 
LYS   CA  HA   sing N N 269 
LYS   C   O    doub N N 270 
LYS   C   OXT  sing N N 271 
LYS   CB  CG   sing N N 272 
LYS   CB  HB2  sing N N 273 
LYS   CB  HB3  sing N N 274 
LYS   CG  CD   sing N N 275 
LYS   CG  HG2  sing N N 276 
LYS   CG  HG3  sing N N 277 
LYS   CD  CE   sing N N 278 
LYS   CD  HD2  sing N N 279 
LYS   CD  HD3  sing N N 280 
LYS   CE  NZ   sing N N 281 
LYS   CE  HE2  sing N N 282 
LYS   CE  HE3  sing N N 283 
LYS   NZ  HZ1  sing N N 284 
LYS   NZ  HZ2  sing N N 285 
LYS   NZ  HZ3  sing N N 286 
LYS   OXT HXT  sing N N 287 
MET   N   CA   sing N N 288 
MET   N   H    sing N N 289 
MET   N   H2   sing N N 290 
MET   CA  C    sing N N 291 
MET   CA  CB   sing N N 292 
MET   CA  HA   sing N N 293 
MET   C   O    doub N N 294 
MET   C   OXT  sing N N 295 
MET   CB  CG   sing N N 296 
MET   CB  HB2  sing N N 297 
MET   CB  HB3  sing N N 298 
MET   CG  SD   sing N N 299 
MET   CG  HG2  sing N N 300 
MET   CG  HG3  sing N N 301 
MET   SD  CE   sing N N 302 
MET   CE  HE1  sing N N 303 
MET   CE  HE2  sing N N 304 
MET   CE  HE3  sing N N 305 
MET   OXT HXT  sing N N 306 
PHE   N   CA   sing N N 307 
PHE   N   H    sing N N 308 
PHE   N   H2   sing N N 309 
PHE   CA  C    sing N N 310 
PHE   CA  CB   sing N N 311 
PHE   CA  HA   sing N N 312 
PHE   C   O    doub N N 313 
PHE   C   OXT  sing N N 314 
PHE   CB  CG   sing N N 315 
PHE   CB  HB2  sing N N 316 
PHE   CB  HB3  sing N N 317 
PHE   CG  CD1  doub Y N 318 
PHE   CG  CD2  sing Y N 319 
PHE   CD1 CE1  sing Y N 320 
PHE   CD1 HD1  sing N N 321 
PHE   CD2 CE2  doub Y N 322 
PHE   CD2 HD2  sing N N 323 
PHE   CE1 CZ   doub Y N 324 
PHE   CE1 HE1  sing N N 325 
PHE   CE2 CZ   sing Y N 326 
PHE   CE2 HE2  sing N N 327 
PHE   CZ  HZ   sing N N 328 
PHE   OXT HXT  sing N N 329 
PRO   N   CA   sing N N 330 
PRO   N   CD   sing N N 331 
PRO   N   H    sing N N 332 
PRO   CA  C    sing N N 333 
PRO   CA  CB   sing N N 334 
PRO   CA  HA   sing N N 335 
PRO   C   O    doub N N 336 
PRO   C   OXT  sing N N 337 
PRO   CB  CG   sing N N 338 
PRO   CB  HB2  sing N N 339 
PRO   CB  HB3  sing N N 340 
PRO   CG  CD   sing N N 341 
PRO   CG  HG2  sing N N 342 
PRO   CG  HG3  sing N N 343 
PRO   CD  HD2  sing N N 344 
PRO   CD  HD3  sing N N 345 
PRO   OXT HXT  sing N N 346 
SER   N   CA   sing N N 347 
SER   N   H    sing N N 348 
SER   N   H2   sing N N 349 
SER   CA  C    sing N N 350 
SER   CA  CB   sing N N 351 
SER   CA  HA   sing N N 352 
SER   C   O    doub N N 353 
SER   C   OXT  sing N N 354 
SER   CB  OG   sing N N 355 
SER   CB  HB2  sing N N 356 
SER   CB  HB3  sing N N 357 
SER   OG  HG   sing N N 358 
SER   OXT HXT  sing N N 359 
TF3   C1  C2   doub Y N 360 
TF3   C1  C3   sing Y N 361 
TF3   C1  O1   sing N N 362 
TF3   C2  C4   sing Y N 363 
TF3   C2  CL1  sing N N 364 
TF3   C3  C5   doub Y N 365 
TF3   C3  H3   sing N N 366 
TF3   O1  C6   sing N N 367 
TF3   C4  C7   doub Y N 368 
TF3   C4  H4   sing N N 369 
TF3   C5  C7   sing Y N 370 
TF3   C5  H5   sing N N 371 
TF3   C6  C8   sing N N 372 
TF3   C6  H6C1 sing N N 373 
TF3   C6  H6C2 sing N N 374 
TF3   C7  C9   sing N N 375 
TF3   C8  C10  doub Y N 376 
TF3   C8  C11  sing Y N 377 
TF3   C9  C12  sing N N 378 
TF3   C9  H9C1 sing N N 379 
TF3   C9  H9C2 sing N N 380 
TF3   C10 C13  sing Y N 381 
TF3   C10 H10  sing N N 382 
TF3   C11 C14  doub Y N 383 
TF3   C11 H11  sing N N 384 
TF3   C12 N1   sing N N 385 
TF3   C12 O2   doub N N 386 
TF3   C13 C15  doub Y N 387 
TF3   C13 H13  sing N N 388 
TF3   C14 C15  sing Y N 389 
TF3   C14 H14  sing N N 390 
TF3   N1  C16  sing N N 391 
TF3   N1  H1   sing N N 392 
TF3   C15 C17  sing N N 393 
TF3   C16 C18  sing N N 394 
TF3   C16 H161 sing N N 395 
TF3   C16 H162 sing N N 396 
TF3   C17 C19  sing N N 397 
TF3   C17 C20  sing N N 398 
TF3   C17 H17  sing N N 399 
TF3   C18 N2   sing N N 400 
TF3   C18 H181 sing N N 401 
TF3   C18 H182 sing N N 402 
TF3   C19 H191 sing N N 403 
TF3   C19 H192 sing N N 404 
TF3   C19 H193 sing N N 405 
TF3   C20 H201 sing N N 406 
TF3   C20 H202 sing N N 407 
TF3   C20 H203 sing N N 408 
TF3   N2  H2N1 sing N N 409 
TF3   N2  H2N2 sing N N 410 
THR   N   CA   sing N N 411 
THR   N   H    sing N N 412 
THR   N   H2   sing N N 413 
THR   CA  C    sing N N 414 
THR   CA  CB   sing N N 415 
THR   CA  HA   sing N N 416 
THR   C   O    doub N N 417 
THR   C   OXT  sing N N 418 
THR   CB  OG1  sing N N 419 
THR   CB  CG2  sing N N 420 
THR   CB  HB   sing N N 421 
THR   OG1 HG1  sing N N 422 
THR   CG2 HG21 sing N N 423 
THR   CG2 HG22 sing N N 424 
THR   CG2 HG23 sing N N 425 
THR   OXT HXT  sing N N 426 
TRP   N   CA   sing N N 427 
TRP   N   H    sing N N 428 
TRP   N   H2   sing N N 429 
TRP   CA  C    sing N N 430 
TRP   CA  CB   sing N N 431 
TRP   CA  HA   sing N N 432 
TRP   C   O    doub N N 433 
TRP   C   OXT  sing N N 434 
TRP   CB  CG   sing N N 435 
TRP   CB  HB2  sing N N 436 
TRP   CB  HB3  sing N N 437 
TRP   CG  CD1  doub Y N 438 
TRP   CG  CD2  sing Y N 439 
TRP   CD1 NE1  sing Y N 440 
TRP   CD1 HD1  sing N N 441 
TRP   CD2 CE2  doub Y N 442 
TRP   CD2 CE3  sing Y N 443 
TRP   NE1 CE2  sing Y N 444 
TRP   NE1 HE1  sing N N 445 
TRP   CE2 CZ2  sing Y N 446 
TRP   CE3 CZ3  doub Y N 447 
TRP   CE3 HE3  sing N N 448 
TRP   CZ2 CH2  doub Y N 449 
TRP   CZ2 HZ2  sing N N 450 
TRP   CZ3 CH2  sing Y N 451 
TRP   CZ3 HZ3  sing N N 452 
TRP   CH2 HH2  sing N N 453 
TRP   OXT HXT  sing N N 454 
TYR   N   CA   sing N N 455 
TYR   N   H    sing N N 456 
TYR   N   H2   sing N N 457 
TYR   CA  C    sing N N 458 
TYR   CA  CB   sing N N 459 
TYR   CA  HA   sing N N 460 
TYR   C   O    doub N N 461 
TYR   C   OXT  sing N N 462 
TYR   CB  CG   sing N N 463 
TYR   CB  HB2  sing N N 464 
TYR   CB  HB3  sing N N 465 
TYR   CG  CD1  doub Y N 466 
TYR   CG  CD2  sing Y N 467 
TYR   CD1 CE1  sing Y N 468 
TYR   CD1 HD1  sing N N 469 
TYR   CD2 CE2  doub Y N 470 
TYR   CD2 HD2  sing N N 471 
TYR   CE1 CZ   doub Y N 472 
TYR   CE1 HE1  sing N N 473 
TYR   CE2 CZ   sing Y N 474 
TYR   CE2 HE2  sing N N 475 
TYR   CZ  OH   sing N N 476 
TYR   OH  HH   sing N N 477 
TYR   OXT HXT  sing N N 478 
VAL   N   CA   sing N N 479 
VAL   N   H    sing N N 480 
VAL   N   H2   sing N N 481 
VAL   CA  C    sing N N 482 
VAL   CA  CB   sing N N 483 
VAL   CA  HA   sing N N 484 
VAL   C   O    doub N N 485 
VAL   C   OXT  sing N N 486 
VAL   CB  CG1  sing N N 487 
VAL   CB  CG2  sing N N 488 
VAL   CB  HB   sing N N 489 
VAL   CG1 HG11 sing N N 490 
VAL   CG1 HG12 sing N N 491 
VAL   CG1 HG13 sing N N 492 
VAL   CG2 HG21 sing N N 493 
VAL   CG2 HG22 sing N N 494 
VAL   CG2 HG23 sing N N 495 
VAL   OXT HXT  sing N N 496 
# 
_pdbx_audit_support.funding_organization   'Not funded' 
_pdbx_audit_support.country                ? 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_atom_sites.entry_id                    9M3T 
_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]   0.009384 
_atom_sites.fract_transf_matrix[1][2]   0.005418 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.010835 
_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]   0.011674 
_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 
F  
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   . ALA   A 1 1   ? 43.947 -21.563 -58.367 1.00 99.78  ?  16  ALA   A N   1 
ATOM   2    C  CA  . ALA   A 1 1   ? 43.363 -22.409 -57.330 1.00 99.51  ?  16  ALA   A CA  1 
ATOM   3    C  C   . ALA   A 1 1   ? 42.195 -23.205 -57.906 1.00 97.48  ?  16  ALA   A C   1 
ATOM   4    O  O   . ALA   A 1 1   ? 41.613 -22.796 -58.909 1.00 95.59  ?  16  ALA   A O   1 
ATOM   5    C  CB  . ALA   A 1 1   ? 42.909 -21.560 -56.136 1.00 90.43  ?  16  ALA   A CB  1 
ATOM   6    N  N   . PRO   A 1 2   ? 41.855 -24.342 -57.290 1.00 94.81  ?  17  PRO   A N   1 
ATOM   7    C  CA  . PRO   A 1 2   ? 40.720 -25.132 -57.783 1.00 94.41  ?  17  PRO   A CA  1 
ATOM   8    C  C   . PRO   A 1 2   ? 39.397 -24.381 -57.688 1.00 88.26  ?  17  PRO   A C   1 
ATOM   9    O  O   . PRO   A 1 2   ? 39.258 -23.386 -56.967 1.00 69.32  ?  17  PRO   A O   1 
ATOM   10   C  CB  . PRO   A 1 2   ? 40.723 -26.367 -56.874 1.00 87.75  ?  17  PRO   A CB  1 
ATOM   11   C  CG  . PRO   A 1 2   ? 42.118 -26.479 -56.389 1.00 94.05  ?  17  PRO   A CG  1 
ATOM   12   C  CD  . PRO   A 1 2   ? 42.613 -25.064 -56.250 1.00 90.26  ?  17  PRO   A CD  1 
ATOM   13   N  N   . LYS   A 1 3   ? 38.417 -24.892 -58.443 1.00 81.84  ?  18  LYS   A N   1 
ATOM   14   C  CA  . LYS   A 1 3   ? 37.085 -24.287 -58.524 1.00 88.42  ?  18  LYS   A CA  1 
ATOM   15   C  C   . LYS   A 1 3   ? 36.527 -23.966 -57.147 1.00 76.86  ?  18  LYS   A C   1 
ATOM   16   O  O   . LYS   A 1 3   ? 36.049 -22.856 -56.892 1.00 77.04  ?  18  LYS   A O   1 
ATOM   17   C  CB  . LYS   A 1 3   ? 36.122 -25.233 -59.247 1.00 77.71  ?  18  LYS   A CB  1 
ATOM   18   C  CG  . LYS   A 1 3   ? 36.524 -25.595 -60.640 1.00 88.21  ?  18  LYS   A CG  1 
ATOM   19   C  CD  . LYS   A 1 3   ? 35.541 -26.568 -61.269 1.00 84.78  ?  18  LYS   A CD  1 
ATOM   20   C  CE  . LYS   A 1 3   ? 34.192 -25.924 -61.496 1.00 91.40  ?  18  LYS   A CE  1 
ATOM   21   N  NZ  . LYS   A 1 3   ? 34.218 -24.710 -62.359 1.00 97.69  ?  18  LYS   A NZ  1 
ATOM   22   N  N   . TYR   A 1 4   ? 36.560 -24.949 -56.254 1.00 77.88  ?  19  TYR   A N   1 
ATOM   23   C  CA  . TYR   A 1 4   ? 35.869 -24.827 -54.982 1.00 71.03  ?  19  TYR   A CA  1 
ATOM   24   C  C   . TYR   A 1 4   ? 36.533 -23.784 -54.075 1.00 73.79  ?  19  TYR   A C   1 
ATOM   25   O  O   . TYR   A 1 4   ? 35.844 -23.074 -53.330 1.00 64.47  ?  19  TYR   A O   1 
ATOM   26   C  CB  . TYR   A 1 4   ? 35.812 -26.205 -54.330 1.00 76.36  ?  19  TYR   A CB  1 
ATOM   27   C  CG  . TYR   A 1 4   ? 37.125 -26.973 -54.404 1.00 84.30  ?  19  TYR   A CG  1 
ATOM   28   C  CD1 . TYR   A 1 4   ? 37.370 -27.920 -55.407 1.00 87.57  ?  19  TYR   A CD1 1 
ATOM   29   C  CD2 . TYR   A 1 4   ? 38.122 -26.747 -53.466 1.00 78.76  ?  19  TYR   A CD2 1 
ATOM   30   C  CE1 . TYR   A 1 4   ? 38.590 -28.619 -55.445 1.00 87.37  ?  19  TYR   A CE1 1 
ATOM   31   C  CE2 . TYR   A 1 4   ? 39.316 -27.428 -53.504 1.00 70.50  ?  19  TYR   A CE2 1 
ATOM   32   C  CZ  . TYR   A 1 4   ? 39.555 -28.351 -54.467 1.00 80.19  ?  19  TYR   A CZ  1 
ATOM   33   O  OH  . TYR   A 1 4   ? 40.779 -28.978 -54.421 1.00 87.35  ?  19  TYR   A OH  1 
ATOM   34   N  N   . ILE   A 1 5   ? 37.863 -23.655 -54.140 1.00 69.85  ?  20  ILE   A N   1 
ATOM   35   C  CA  . ILE   A 1 5   ? 38.534 -22.602 -53.378 1.00 66.77  ?  20  ILE   A CA  1 
ATOM   36   C  C   . ILE   A 1 5   ? 38.182 -21.232 -53.945 1.00 65.83  ?  20  ILE   A C   1 
ATOM   37   O  O   . ILE   A 1 5   ? 37.982 -20.267 -53.197 1.00 58.00  ?  20  ILE   A O   1 
ATOM   38   C  CB  . ILE   A 1 5   ? 40.056 -22.831 -53.364 1.00 68.26  ?  20  ILE   A CB  1 
ATOM   39   C  CG1 . ILE   A 1 5   ? 40.414 -23.989 -52.437 1.00 73.13  ?  20  ILE   A CG1 1 
ATOM   40   C  CG2 . ILE   A 1 5   ? 40.799 -21.574 -52.910 1.00 61.78  ?  20  ILE   A CG2 1 
ATOM   41   C  CD1 . ILE   A 1 5   ? 41.827 -24.477 -52.634 1.00 70.30  ?  20  ILE   A CD1 1 
ATOM   42   N  N   . GLU   A 1 6   ? 38.080 -21.134 -55.272 1.00 63.38  ?  21  GLU   A N   1 
ATOM   43   C  CA  . GLU   A 1 6   ? 37.751 -19.864 -55.917 1.00 72.26  ?  21  GLU   A CA  1 
ATOM   44   C  C   . GLU   A 1 6   ? 36.373 -19.357 -55.497 1.00 70.35  ?  21  GLU   A C   1 
ATOM   45   O  O   . GLU   A 1 6   ? 36.209 -18.176 -55.167 1.00 69.31  ?  21  GLU   A O   1 
ATOM   46   C  CB  . GLU   A 1 6   ? 37.824 -20.021 -57.441 1.00 75.14  ?  21  GLU   A CB  1 
ATOM   47   C  CG  . GLU   A 1 6   ? 39.171 -19.626 -58.017 1.00 84.62  ?  21  GLU   A CG  1 
ATOM   48   C  CD  . GLU   A 1 6   ? 39.500 -18.170 -57.731 1.00 94.79  ?  21  GLU   A CD  1 
ATOM   49   O  OE1 . GLU   A 1 6   ? 38.672 -17.304 -58.094 1.00 87.23  ?  21  GLU   A OE1 1 
ATOM   50   O  OE2 . GLU   A 1 6   ? 40.562 -17.896 -57.123 1.00 95.64  ?  21  GLU   A OE2 1 
ATOM   51   N  N   . HIS   A 1 7   ? 35.368 -20.235 -55.518 1.00 63.91  ?  22  HIS   A N   1 
ATOM   52   C  CA  . HIS   A 1 7   ? 34.025 -19.854 -55.092 1.00 64.89  ?  22  HIS   A CA  1 
ATOM   53   C  C   . HIS   A 1 7   ? 34.011 -19.299 -53.669 1.00 66.75  ?  22  HIS   A C   1 
ATOM   54   O  O   . HIS   A 1 7   ? 33.566 -18.169 -53.427 1.00 61.36  ?  22  HIS   A O   1 
ATOM   55   C  CB  . HIS   A 1 7   ? 33.097 -21.058 -55.189 1.00 70.68  ?  22  HIS   A CB  1 
ATOM   56   C  CG  . HIS   A 1 7   ? 31.691 -20.761 -54.783 1.00 71.20  ?  22  HIS   A CG  1 
ATOM   57   N  ND1 . HIS   A 1 7   ? 31.135 -21.238 -53.616 1.00 71.06  ?  22  HIS   A ND1 1 
ATOM   58   C  CD2 . HIS   A 1 7   ? 30.730 -20.025 -55.385 1.00 75.09  ?  22  HIS   A CD2 1 
ATOM   59   C  CE1 . HIS   A 1 7   ? 29.887 -20.814 -53.520 1.00 70.83  ?  22  HIS   A CE1 1 
ATOM   60   N  NE2 . HIS   A 1 7   ? 29.618 -20.073 -54.579 1.00 79.90  ?  22  HIS   A NE2 1 
ATOM   61   N  N   . PHE   A 1 8   ? 34.474 -20.091 -52.700 1.00 61.98  ?  23  PHE   A N   1 
ATOM   62   C  CA  . PHE   A 1 8   ? 34.313 -19.682 -51.311 1.00 57.92  ?  23  PHE   A CA  1 
ATOM   63   C  C   . PHE   A 1 8   ? 35.226 -18.525 -50.929 1.00 56.14  ?  23  PHE   A C   1 
ATOM   64   O  O   . PHE   A 1 8   ? 34.922 -17.811 -49.971 1.00 55.14  ?  23  PHE   A O   1 
ATOM   65   C  CB  . PHE   A 1 8   ? 34.540 -20.875 -50.376 1.00 56.00  ?  23  PHE   A CB  1 
ATOM   66   C  CG  . PHE   A 1 8   ? 33.437 -21.893 -50.430 1.00 59.62  ?  23  PHE   A CG  1 
ATOM   67   C  CD1 . PHE   A 1 8   ? 32.181 -21.604 -49.904 1.00 54.56  ?  23  PHE   A CD1 1 
ATOM   68   C  CD2 . PHE   A 1 8   ? 33.652 -23.134 -51.015 1.00 56.96  ?  23  PHE   A CD2 1 
ATOM   69   C  CE1 . PHE   A 1 8   ? 31.159 -22.542 -49.962 1.00 62.17  ?  23  PHE   A CE1 1 
ATOM   70   C  CE2 . PHE   A 1 8   ? 32.637 -24.071 -51.077 1.00 64.77  ?  23  PHE   A CE2 1 
ATOM   71   C  CZ  . PHE   A 1 8   ? 31.389 -23.778 -50.551 1.00 63.79  ?  23  PHE   A CZ  1 
ATOM   72   N  N   . SER   A 1 9   ? 36.321 -18.306 -51.659 1.00 56.82  ?  24  SER   A N   1 
ATOM   73   C  CA  . SER   A 1 9   ? 37.208 -17.196 -51.328 1.00 56.66  ?  24  SER   A CA  1 
ATOM   74   C  C   . SER   A 1 9   ? 36.649 -15.845 -51.748 1.00 63.48  ?  24  SER   A C   1 
ATOM   75   O  O   . SER   A 1 9   ? 37.183 -14.818 -51.320 1.00 68.45  ?  24  SER   A O   1 
ATOM   76   C  CB  . SER   A 1 9   ? 38.570 -17.391 -51.988 1.00 60.93  ?  24  SER   A CB  1 
ATOM   77   O  OG  . SER   A 1 9   ? 38.455 -17.254 -53.397 1.00 56.95  ?  24  SER   A OG  1 
ATOM   78   N  N   . LYS   A 1 10  ? 35.617 -15.811 -52.588 1.00 58.54  ?  25  LYS   A N   1 
ATOM   79   C  CA  . LYS   A 1 10  ? 35.001 -14.539 -52.940 1.00 62.89  ?  25  LYS   A CA  1 
ATOM   80   C  C   . LYS   A 1 10  ? 34.006 -14.052 -51.888 1.00 68.14  ?  25  LYS   A C   1 
ATOM   81   O  O   . LYS   A 1 10  ? 33.514 -12.924 -52.001 1.00 70.94  ?  25  LYS   A O   1 
ATOM   82   C  CB  . LYS   A 1 10  ? 34.331 -14.643 -54.313 1.00 69.62  ?  25  LYS   A CB  1 
ATOM   83   C  CG  . LYS   A 1 10  ? 35.334 -14.928 -55.447 1.00 73.31  ?  25  LYS   A CG  1 
ATOM   84   C  CD  . LYS   A 1 10  ? 34.710 -14.866 -56.837 1.00 88.36  ?  25  LYS   A CD  1 
ATOM   85   C  CE  . LYS   A 1 10  ? 34.338 -13.439 -57.232 1.00 105.59 ?  25  LYS   A CE  1 
ATOM   86   N  NZ  . LYS   A 1 10  ? 34.149 -13.291 -58.715 1.00 101.86 ?  25  LYS   A NZ  1 
ATOM   87   N  N   . PHE   A 1 11  ? 33.696 -14.863 -50.880 1.00 54.52  ?  26  PHE   A N   1 
ATOM   88   C  CA  . PHE   A 1 11  ? 32.938 -14.394 -49.734 1.00 55.04  ?  26  PHE   A CA  1 
ATOM   89   C  C   . PHE   A 1 11  ? 33.916 -13.847 -48.704 1.00 56.02  ?  26  PHE   A C   1 
ATOM   90   O  O   . PHE   A 1 11  ? 35.078 -14.257 -48.644 1.00 57.23  ?  26  PHE   A O   1 
ATOM   91   C  CB  . PHE   A 1 11  ? 32.101 -15.522 -49.110 1.00 55.95  ?  26  PHE   A CB  1 
ATOM   92   C  CG  . PHE   A 1 11  ? 31.057 -16.102 -50.034 1.00 63.20  ?  26  PHE   A CG  1 
ATOM   93   C  CD1 . PHE   A 1 11  ? 31.406 -17.044 -50.992 1.00 64.97  ?  26  PHE   A CD1 1 
ATOM   94   C  CD2 . PHE   A 1 11  ? 29.724 -15.722 -49.933 1.00 56.97  ?  26  PHE   A CD2 1 
ATOM   95   C  CE1 . PHE   A 1 11  ? 30.443 -17.583 -51.853 1.00 71.19  ?  26  PHE   A CE1 1 
ATOM   96   C  CE2 . PHE   A 1 11  ? 28.758 -16.264 -50.782 1.00 66.15  ?  26  PHE   A CE2 1 
ATOM   97   C  CZ  . PHE   A 1 11  ? 29.120 -17.190 -51.743 1.00 68.57  ?  26  PHE   A CZ  1 
ATOM   98   N  N   . SER   A 1 12  ? 33.462 -12.907 -47.915 1.00 48.65  ?  27  SER   A N   1 
ATOM   99   C  CA  . SER   A 1 12  ? 34.419 -12.665 -46.854 1.00 56.45  ?  27  SER   A CA  1 
ATOM   100  C  C   . SER   A 1 12  ? 33.927 -13.313 -45.557 1.00 51.92  ?  27  SER   A C   1 
ATOM   101  O  O   . SER   A 1 12  ? 32.724 -13.545 -45.399 1.00 51.38  ?  27  SER   A O   1 
ATOM   102  C  CB  . SER   A 1 12  ? 34.651 -11.165 -46.648 1.00 61.66  ?  27  SER   A CB  1 
ATOM   103  O  OG  . SER   A 1 12  ? 33.429 -10.474 -46.602 1.00 70.29  ?  27  SER   A OG  1 
ATOM   104  N  N   . PRO   A 1 13  ? 34.824 -13.658 -44.632 1.00 46.60  ?  28  PRO   A N   1 
ATOM   105  C  CA  . PRO   A 1 13  ? 34.372 -14.232 -43.356 1.00 48.10  ?  28  PRO   A CA  1 
ATOM   106  C  C   . PRO   A 1 13  ? 33.374 -13.314 -42.665 1.00 50.95  ?  28  PRO   A C   1 
ATOM   107  O  O   . PRO   A 1 13  ? 33.411 -12.095 -42.831 1.00 47.81  ?  28  PRO   A O   1 
ATOM   108  C  CB  . PRO   A 1 13  ? 35.668 -14.367 -42.547 1.00 44.64  ?  28  PRO   A CB  1 
ATOM   109  C  CG  . PRO   A 1 13  ? 36.762 -14.450 -43.580 1.00 46.28  ?  28  PRO   A CG  1 
ATOM   110  C  CD  . PRO   A 1 13  ? 36.295 -13.556 -44.706 1.00 47.45  ?  28  PRO   A CD  1 
ATOM   111  N  N   . SER   A 1 14  ? 32.434 -13.923 -41.927 1.00 44.93  ?  29  SER   A N   1 
ATOM   112  C  CA  . SER   A 1 14  ? 31.412 -13.178 -41.190 1.00 41.17  ?  29  SER   A CA  1 
ATOM   113  C  C   . SER   A 1 14  ? 31.761 -13.172 -39.705 1.00 43.80  ?  29  SER   A C   1 
ATOM   114  O  O   . SER   A 1 14  ? 31.635 -14.213 -39.038 1.00 45.84  ?  29  SER   A O   1 
ATOM   115  C  CB  . SER   A 1 14  ? 30.023 -13.783 -41.398 1.00 44.98  ?  29  SER   A CB  1 
ATOM   116  O  OG  . SER   A 1 14  ? 29.587 -13.641 -42.739 1.00 63.28  ?  29  SER   A OG  1 
ATOM   117  N  N   . PRO   A 1 15  ? 32.214 -12.061 -39.145 1.00 46.39  ?  30  PRO   A N   1 
ATOM   118  C  CA  . PRO   A 1 15  ? 32.664 -12.078 -37.746 1.00 50.18  ?  30  PRO   A CA  1 
ATOM   119  C  C   . PRO   A 1 15  ? 31.489 -12.071 -36.772 1.00 47.13  ?  30  PRO   A C   1 
ATOM   120  O  O   . PRO   A 1 15  ? 30.472 -11.411 -36.988 1.00 43.92  ?  30  PRO   A O   1 
ATOM   121  C  CB  . PRO   A 1 15  ? 33.516 -10.806 -37.637 1.00 46.27  ?  30  PRO   A CB  1 
ATOM   122  C  CG  . PRO   A 1 15  ? 33.063 -9.925  -38.754 1.00 46.01  ?  30  PRO   A CG  1 
ATOM   123  C  CD  . PRO   A 1 15  ? 32.573 -10.824 -39.854 1.00 47.31  ?  30  PRO   A CD  1 
ATOM   124  N  N   . LEU   A 1 16  ? 31.624 -12.841 -35.698 1.00 49.44  ?  31  LEU   A N   1 
ATOM   125  C  CA  . LEU   A 1 16  ? 30.574 -12.973 -34.694 1.00 48.89  ?  31  LEU   A CA  1 
ATOM   126  C  C   . LEU   A 1 16  ? 30.974 -12.266 -33.402 1.00 48.14  ?  31  LEU   A C   1 
ATOM   127  O  O   . LEU   A 1 16  ? 32.132 -12.328 -32.975 1.00 46.56  ?  31  LEU   A O   1 
ATOM   128  C  CB  . LEU   A 1 16  ? 30.277 -14.453 -34.411 1.00 50.37  ?  31  LEU   A CB  1 
ATOM   129  C  CG  . LEU   A 1 16  ? 29.775 -15.247 -35.632 1.00 53.80  ?  31  LEU   A CG  1 
ATOM   130  C  CD1 . LEU   A 1 16  ? 29.624 -16.720 -35.325 1.00 53.29  ?  31  LEU   A CD1 1 
ATOM   131  C  CD2 . LEU   A 1 16  ? 28.460 -14.685 -36.147 1.00 58.73  ?  31  LEU   A CD2 1 
ATOM   132  N  N   . SER   A 1 17  ? 30.008 -11.614 -32.771 1.00 49.46  ?  32  SER   A N   1 
ATOM   133  C  CA  . SER   A 1 17  ? 30.254 -11.058 -31.451 1.00 45.79  ?  32  SER   A CA  1 
ATOM   134  C  C   . SER   A 1 17  ? 30.105 -12.138 -30.393 1.00 47.84  ?  32  SER   A C   1 
ATOM   135  O  O   . SER   A 1 17  ? 29.433 -13.152 -30.591 1.00 47.91  ?  32  SER   A O   1 
ATOM   136  C  CB  . SER   A 1 17  ? 29.282 -9.929  -31.148 1.00 49.31  ?  32  SER   A CB  1 
ATOM   137  O  OG  . SER   A 1 17  ? 28.053 -10.477 -30.700 1.00 54.29  ?  32  SER   A OG  1 
ATOM   138  N  N   . MET   A 1 18  ? 30.763 -11.915 -29.258 1.00 49.50  ?  33  MET   A N   1 
ATOM   139  C  CA  . MET   A 1 18  ? 30.571 -12.783 -28.101 1.00 53.51  ?  33  MET   A CA  1 
ATOM   140  C  C   . MET   A 1 18  ? 29.105 -12.897 -27.700 1.00 51.15  ?  33  MET   A C   1 
ATOM   141  O  O   . MET   A 1 18  ? 28.675 -13.944 -27.209 1.00 54.90  ?  33  MET   A O   1 
ATOM   142  C  CB  . MET   A 1 18  ? 31.376 -12.252 -26.929 1.00 50.22  ?  33  MET   A CB  1 
ATOM   143  C  CG  . MET   A 1 18  ? 31.479 -13.222 -25.817 1.00 52.83  ?  33  MET   A CG  1 
ATOM   144  S  SD  . MET   A 1 18  ? 33.046 -14.070 -25.891 1.00 65.29  ?  33  MET   A SD  1 
ATOM   145  C  CE  . MET   A 1 18  ? 34.162 -12.780 -25.415 1.00 41.73  ?  33  MET   A CE  1 
ATOM   146  N  N   . LYS   A 1 19  ? 28.327 -11.836 -27.885 1.00 49.12  ?  34  LYS   A N   1 
ATOM   147  C  CA  . LYS   A 1 19  ? 26.909 -11.921 -27.547 1.00 59.09  ?  34  LYS   A CA  1 
ATOM   148  C  C   . LYS   A 1 19  ? 26.172 -12.850 -28.502 1.00 61.02  ?  34  LYS   A C   1 
ATOM   149  O  O   . LYS   A 1 19  ? 25.271 -13.586 -28.084 1.00 60.43  ?  34  LYS   A O   1 
ATOM   150  C  CB  . LYS   A 1 19  ? 26.279 -10.529 -27.552 1.00 53.49  ?  34  LYS   A CB  1 
ATOM   151  C  CG  . LYS   A 1 19  ? 24.802 -10.520 -27.169 1.00 59.16  ?  34  LYS   A CG  1 
ATOM   152  C  CD  . LYS   A 1 19  ? 24.308 -9.105  -26.989 1.00 69.92  ?  34  LYS   A CD  1 
ATOM   153  C  CE  . LYS   A 1 19  ? 22.789 -9.002  -27.026 1.00 68.78  ?  34  LYS   A CE  1 
ATOM   154  N  NZ  . LYS   A 1 19  ? 22.375 -7.571  -27.205 1.00 82.02  ?  34  LYS   A NZ  1 
ATOM   155  N  N   . GLN   A 1 20  ? 26.534 -12.831 -29.785 1.00 57.45  ?  35  GLN   A N   1 
ATOM   156  C  CA  . GLN   A 1 20  ? 25.896 -13.733 -30.737 1.00 56.61  ?  35  GLN   A CA  1 
ATOM   157  C  C   . GLN   A 1 20  ? 26.234 -15.185 -30.421 1.00 61.59  ?  35  GLN   A C   1 
ATOM   158  O  O   . GLN   A 1 20  ? 25.348 -16.048 -30.403 1.00 62.58  ?  35  GLN   A O   1 
ATOM   159  C  CB  . GLN   A 1 20  ? 26.310 -13.373 -32.161 1.00 57.83  ?  35  GLN   A CB  1 
ATOM   160  C  CG  . GLN   A 1 20  ? 25.862 -11.986 -32.591 1.00 53.42  ?  35  GLN   A CG  1 
ATOM   161  C  CD  . GLN   A 1 20  ? 26.412 -11.590 -33.954 1.00 56.23  ?  35  GLN   A CD  1 
ATOM   162  O  OE1 . GLN   A 1 20  ? 27.621 -11.469 -34.139 1.00 59.43  ?  35  GLN   A OE1 1 
ATOM   163  N  NE2 . GLN   A 1 20  ? 25.519 -11.379 -34.911 1.00 66.34  ?  35  GLN   A NE2 1 
ATOM   164  N  N   . PHE   A 1 21  ? 27.519 -15.476 -30.173 1.00 57.68  ?  36  PHE   A N   1 
ATOM   165  C  CA  . PHE   A 1 21  ? 27.913 -16.800 -29.690 1.00 53.21  ?  36  PHE   A CA  1 
ATOM   166  C  C   . PHE   A 1 21  ? 27.057 -17.227 -28.509 1.00 61.78  ?  36  PHE   A C   1 
ATOM   167  O  O   . PHE   A 1 21  ? 26.603 -18.372 -28.435 1.00 63.16  ?  36  PHE   A O   1 
ATOM   168  C  CB  . PHE   A 1 21  ? 29.380 -16.801 -29.255 1.00 51.21  ?  36  PHE   A CB  1 
ATOM   169  C  CG  . PHE   A 1 21  ? 30.365 -16.983 -30.372 1.00 52.41  ?  36  PHE   A CG  1 
ATOM   170  C  CD1 . PHE   A 1 21  ? 30.364 -18.133 -31.145 1.00 49.79  ?  36  PHE   A CD1 1 
ATOM   171  C  CD2 . PHE   A 1 21  ? 31.331 -16.018 -30.619 1.00 47.08  ?  36  PHE   A CD2 1 
ATOM   172  C  CE1 . PHE   A 1 21  ? 31.293 -18.302 -32.167 1.00 54.60  ?  36  PHE   A CE1 1 
ATOM   173  C  CE2 . PHE   A 1 21  ? 32.268 -16.186 -31.628 1.00 50.59  ?  36  PHE   A CE2 1 
ATOM   174  C  CZ  . PHE   A 1 21  ? 32.249 -17.320 -32.403 1.00 46.11  ?  36  PHE   A CZ  1 
ATOM   175  N  N   . LEU   A 1 22  ? 26.824 -16.304 -27.580 1.00 60.66  ?  37  LEU   A N   1 
ATOM   176  C  CA  . LEU   A 1 22  ? 26.113 -16.602 -26.345 1.00 68.29  ?  37  LEU   A CA  1 
ATOM   177  C  C   . LEU   A 1 22  ? 24.620 -16.767 -26.595 1.00 74.25  ?  37  LEU   A C   1 
ATOM   178  O  O   . LEU   A 1 22  ? 24.010 -17.740 -26.137 1.00 77.97  ?  37  LEU   A O   1 
ATOM   179  C  CB  . LEU   A 1 22  ? 26.377 -15.486 -25.334 1.00 65.81  ?  37  LEU   A CB  1 
ATOM   180  C  CG  . LEU   A 1 22  ? 26.517 -15.820 -23.857 1.00 68.26  ?  37  LEU   A CG  1 
ATOM   181  C  CD1 . LEU   A 1 22  ? 27.532 -16.916 -23.666 1.00 63.20  ?  37  LEU   A CD1 1 
ATOM   182  C  CD2 . LEU   A 1 22  ? 26.925 -14.567 -23.100 1.00 61.95  ?  37  LEU   A CD2 1 
ATOM   183  N  N   . ASP   A 1 23  ? 24.018 -15.825 -27.332 1.00 75.77  ?  38  ASP   A N   1 
ATOM   184  C  CA  . ASP   A 1 23  ? 22.598 -15.908 -27.659 1.00 80.62  ?  38  ASP   A CA  1 
ATOM   185  C  C   . ASP   A 1 23  ? 22.256 -17.185 -28.410 1.00 84.77  ?  38  ASP   A C   1 
ATOM   186  O  O   . ASP   A 1 23  ? 21.077 -17.551 -28.485 1.00 98.89  ?  38  ASP   A O   1 
ATOM   187  C  CB  . ASP   A 1 23  ? 22.163 -14.692 -28.489 1.00 84.80  ?  38  ASP   A CB  1 
ATOM   188  C  CG  . ASP   A 1 23  ? 22.146 -13.397 -27.680 1.00 89.73  ?  38  ASP   A CG  1 
ATOM   189  O  OD1 . ASP   A 1 23  ? 22.194 -13.462 -26.430 1.00 88.60  ?  38  ASP   A OD1 1 
ATOM   190  O  OD2 . ASP   A 1 23  ? 22.090 -12.310 -28.304 1.00 82.63  ?  38  ASP   A OD2 1 
ATOM   191  N  N   . PHE   A 1 24  ? 23.252 -17.876 -28.960 1.00 76.47  ?  39  PHE   A N   1 
ATOM   192  C  CA  . PHE   A 1 24  ? 23.023 -19.146 -29.626 1.00 83.43  ?  39  PHE   A CA  1 
ATOM   193  C  C   . PHE   A 1 24  ? 23.016 -20.337 -28.664 1.00 95.50  ?  39  PHE   A C   1 
ATOM   194  O  O   . PHE   A 1 24  ? 23.268 -21.470 -29.093 1.00 94.39  ?  39  PHE   A O   1 
ATOM   195  C  CB  . PHE   A 1 24  ? 24.060 -19.359 -30.722 1.00 77.19  ?  39  PHE   A CB  1 
ATOM   196  C  CG  . PHE   A 1 24  ? 23.632 -20.356 -31.735 1.00 97.88  ?  39  PHE   A CG  1 
ATOM   197  C  CD1 . PHE   A 1 24  ? 22.488 -20.136 -32.486 1.00 108.70 ?  39  PHE   A CD1 1 
ATOM   198  C  CD2 . PHE   A 1 24  ? 24.332 -21.530 -31.913 1.00 97.96  ?  39  PHE   A CD2 1 
ATOM   199  C  CE1 . PHE   A 1 24  ? 22.063 -21.059 -33.412 1.00 97.43  ?  39  PHE   A CE1 1 
ATOM   200  C  CE2 . PHE   A 1 24  ? 23.913 -22.459 -32.840 1.00 97.52  ?  39  PHE   A CE2 1 
ATOM   201  C  CZ  . PHE   A 1 24  ? 22.777 -22.220 -33.593 1.00 90.35  ?  39  PHE   A CZ  1 
ATOM   202  N  N   . GLY   A 1 25  ? 22.725 -20.111 -27.386 1.00 94.18  ?  40  GLY   A N   1 
ATOM   203  C  CA  . GLY   A 1 25  ? 22.561 -21.195 -26.436 1.00 84.26  ?  40  GLY   A CA  1 
ATOM   204  C  C   . GLY   A 1 25  ? 23.763 -22.105 -26.333 1.00 81.71  ?  40  GLY   A C   1 
ATOM   205  O  O   . GLY   A 1 25  ? 23.687 -23.167 -25.721 1.00 90.45  ?  40  GLY   A O   1 
ATOM   206  N  N   . ASN   A 1 28  ? 18.466 -28.232 -30.386 1.00 104.64 ?  43  ASN   A N   1 
ATOM   207  C  CA  . ASN   A 1 28  ? 17.445 -28.819 -31.253 1.00 126.02 ?  43  ASN   A CA  1 
ATOM   208  C  C   . ASN   A 1 28  ? 17.382 -28.079 -32.593 1.00 120.61 ?  43  ASN   A C   1 
ATOM   209  O  O   . ASN   A 1 28  ? 18.136 -28.389 -33.522 1.00 109.14 ?  43  ASN   A O   1 
ATOM   210  C  CB  . ASN   A 1 28  ? 16.070 -28.797 -30.570 1.00 134.38 ?  43  ASN   A CB  1 
ATOM   211  C  CG  . ASN   A 1 28  ? 15.999 -29.702 -29.345 1.00 137.38 ?  43  ASN   A CG  1 
ATOM   212  O  OD1 . ASN   A 1 28  ? 16.413 -30.864 -29.383 1.00 130.93 ?  43  ASN   A OD1 1 
ATOM   213  N  ND2 . ASN   A 1 28  ? 15.467 -29.168 -28.249 1.00 139.91 ?  43  ASN   A ND2 1 
ATOM   214  N  N   . ALA   A 1 29  ? 16.462 -27.112 -32.694 1.00 114.07 ?  44  ALA   A N   1 
ATOM   215  C  CA  . ALA   A 1 29  ? 16.479 -26.200 -33.833 1.00 94.32  ?  44  ALA   A CA  1 
ATOM   216  C  C   . ALA   A 1 29  ? 17.775 -25.409 -33.869 1.00 90.93  ?  44  ALA   A C   1 
ATOM   217  O  O   . ALA   A 1 29  ? 18.216 -24.983 -34.942 1.00 86.01  ?  44  ALA   A O   1 
ATOM   218  C  CB  . ALA   A 1 29  ? 15.277 -25.256 -33.783 1.00 91.50  ?  44  ALA   A CB  1 
ATOM   219  N  N   . CYS   A 1 30  ? 18.402 -25.209 -32.707 1.00 92.60  ?  45  CYS   A N   1 
ATOM   220  C  CA  . CYS   A 1 30  ? 19.715 -24.582 -32.679 1.00 82.96  ?  45  CYS   A CA  1 
ATOM   221  C  C   . CYS   A 1 30  ? 20.730 -25.399 -33.471 1.00 81.82  ?  45  CYS   A C   1 
ATOM   222  O  O   . CYS   A 1 30  ? 21.534 -24.836 -34.221 1.00 77.60  ?  45  CYS   A O   1 
ATOM   223  C  CB  . CYS   A 1 30  ? 20.177 -24.390 -31.233 1.00 87.82  ?  45  CYS   A CB  1 
ATOM   224  S  SG  . CYS   A 1 30  ? 19.397 -23.007 -30.345 1.00 105.22 ?  45  CYS   A SG  1 
ATOM   225  N  N   . GLU   A 1 31  ? 20.699 -26.729 -33.342 1.00 77.70  ?  46  GLU   A N   1 
ATOM   226  C  CA  . GLU   A 1 31  ? 21.749 -27.527 -33.971 1.00 74.90  ?  46  GLU   A CA  1 
ATOM   227  C  C   . GLU   A 1 31  ? 21.672 -27.467 -35.493 1.00 76.66  ?  46  GLU   A C   1 
ATOM   228  O  O   . GLU   A 1 31  ? 22.705 -27.354 -36.165 1.00 70.69  ?  46  GLU   A O   1 
ATOM   229  C  CB  . GLU   A 1 31  ? 21.691 -28.973 -33.494 1.00 77.39  ?  46  GLU   A CB  1 
ATOM   230  C  CG  . GLU   A 1 31  ? 22.747 -29.832 -34.166 1.00 79.62  ?  46  GLU   A CG  1 
ATOM   231  C  CD  . GLU   A 1 31  ? 23.000 -31.132 -33.446 1.00 78.88  ?  46  GLU   A CD  1 
ATOM   232  O  OE1 . GLU   A 1 31  ? 22.269 -31.423 -32.473 1.00 78.79  ?  46  GLU   A OE1 1 
ATOM   233  O  OE2 . GLU   A 1 31  ? 23.936 -31.856 -33.853 1.00 77.96  ?  46  GLU   A OE2 1 
ATOM   234  N  N   . LYS   A 1 32  ? 20.463 -27.546 -36.055 1.00 69.63  ?  47  LYS   A N   1 
ATOM   235  C  CA  . LYS   A 1 32  ? 20.313 -27.379 -37.495 1.00 73.54  ?  47  LYS   A CA  1 
ATOM   236  C  C   . LYS   A 1 32  ? 20.779 -25.999 -37.936 1.00 73.81  ?  47  LYS   A C   1 
ATOM   237  O  O   . LYS   A 1 32  ? 21.387 -25.854 -39.002 1.00 74.55  ?  47  LYS   A O   1 
ATOM   238  C  CB  . LYS   A 1 32  ? 18.859 -27.613 -37.898 1.00 75.66  ?  47  LYS   A CB  1 
ATOM   239  C  CG  . LYS   A 1 32  ? 18.316 -28.934 -37.385 1.00 84.34  ?  47  LYS   A CG  1 
ATOM   240  C  CD  . LYS   A 1 32  ? 16.907 -29.225 -37.900 1.00 94.05  ?  47  LYS   A CD  1 
ATOM   241  C  CE  . LYS   A 1 32  ? 15.887 -28.221 -37.379 1.00 90.54  ?  47  LYS   A CE  1 
ATOM   242  N  NZ  . LYS   A 1 32  ? 14.513 -28.526 -37.879 1.00 98.11  ?  47  LYS   A NZ  1 
ATOM   243  N  N   . THR   A 1 33  ? 20.511 -24.975 -37.116 1.00 70.61  ?  48  THR   A N   1 
ATOM   244  C  CA  . THR   A 1 33  ? 20.936 -23.616 -37.434 1.00 71.87  ?  48  THR   A CA  1 
ATOM   245  C  C   . THR   A 1 33  ? 22.456 -23.498 -37.430 1.00 72.33  ?  48  THR   A C   1 
ATOM   246  O  O   . THR   A 1 33  ? 23.037 -22.796 -38.268 1.00 64.61  ?  48  THR   A O   1 
ATOM   247  C  CB  . THR   A 1 33  ? 20.327 -22.633 -36.430 1.00 71.80  ?  48  THR   A CB  1 
ATOM   248  O  OG1 . THR   A 1 33  ? 18.901 -22.660 -36.535 1.00 79.68  ?  48  THR   A OG1 1 
ATOM   249  C  CG2 . THR   A 1 33  ? 20.826 -21.218 -36.677 1.00 70.01  ?  48  THR   A CG2 1 
ATOM   250  N  N   . SER   A 1 34  ? 23.114 -24.165 -36.484 1.00 67.20  ?  49  SER   A N   1 
ATOM   251  C  CA  . SER   A 1 34  ? 24.568 -24.143 -36.452 1.00 63.34  ?  49  SER   A CA  1 
ATOM   252  C  C   . SER   A 1 34  ? 25.145 -24.851 -37.667 1.00 62.62  ?  49  SER   A C   1 
ATOM   253  O  O   . SER   A 1 34  ? 26.094 -24.359 -38.289 1.00 61.03  ?  49  SER   A O   1 
ATOM   254  C  CB  . SER   A 1 34  ? 25.064 -24.790 -35.160 1.00 67.33  ?  49  SER   A CB  1 
ATOM   255  O  OG  . SER   A 1 34  ? 26.466 -24.679 -35.046 1.00 57.17  ?  49  SER   A OG  1 
ATOM   256  N  N   . PHE   A 1 35  ? 24.568 -26.001 -38.020 1.00 62.92  ?  50  PHE   A N   1 
ATOM   257  C  CA  . PHE   A 1 35  ? 25.025 -26.788 -39.162 1.00 66.43  ?  50  PHE   A CA  1 
ATOM   258  C  C   . PHE   A 1 35  ? 24.973 -25.995 -40.465 1.00 64.42  ?  50  PHE   A C   1 
ATOM   259  O  O   . PHE   A 1 35  ? 25.936 -25.985 -41.240 1.00 60.92  ?  50  PHE   A O   1 
ATOM   260  C  CB  . PHE   A 1 35  ? 24.165 -28.042 -39.284 1.00 61.45  ?  50  PHE   A CB  1 
ATOM   261  C  CG  . PHE   A 1 35  ? 24.305 -28.744 -40.600 1.00 66.49  ?  50  PHE   A CG  1 
ATOM   262  C  CD1 . PHE   A 1 35  ? 25.495 -29.358 -40.944 1.00 67.31  ?  50  PHE   A CD1 1 
ATOM   263  C  CD2 . PHE   A 1 35  ? 23.243 -28.812 -41.482 1.00 65.47  ?  50  PHE   A CD2 1 
ATOM   264  C  CE1 . PHE   A 1 35  ? 25.627 -30.022 -42.148 1.00 72.96  ?  50  PHE   A CE1 1 
ATOM   265  C  CE2 . PHE   A 1 35  ? 23.372 -29.472 -42.695 1.00 71.09  ?  50  PHE   A CE2 1 
ATOM   266  C  CZ  . PHE   A 1 35  ? 24.567 -30.079 -43.027 1.00 67.68  ?  50  PHE   A CZ  1 
ATOM   267  N  N   . THR   A 1 36  ? 23.838 -25.357 -40.748 1.00 63.74  ?  51  THR   A N   1 
ATOM   268  C  CA  . THR   A 1 36  ? 23.714 -24.662 -42.024 1.00 61.84  ?  51  THR   A CA  1 
ATOM   269  C  C   . THR   A 1 36  ? 24.533 -23.379 -42.041 1.00 54.74  ?  51  THR   A C   1 
ATOM   270  O  O   . THR   A 1 36  ? 24.928 -22.913 -43.114 1.00 59.83  ?  51  THR   A O   1 
ATOM   271  C  CB  . THR   A 1 36  ? 22.247 -24.374 -42.330 1.00 63.59  ?  51  THR   A CB  1 
ATOM   272  O  OG1 . THR   A 1 36  ? 21.692 -23.568 -41.288 1.00 69.57  ?  51  THR   A OG1 1 
ATOM   273  C  CG2 . THR   A 1 36  ? 21.478 -25.652 -42.388 1.00 66.02  ?  51  THR   A CG2 1 
ATOM   274  N  N   . PHE   A 1 37  ? 24.801 -22.789 -40.874 1.00 56.70  ?  52  PHE   A N   1 
ATOM   275  C  CA  . PHE   A 1 37  ? 25.724 -21.659 -40.831 1.00 54.92  ?  52  PHE   A CA  1 
ATOM   276  C  C   . PHE   A 1 37  ? 27.159 -22.115 -41.077 1.00 54.53  ?  52  PHE   A C   1 
ATOM   277  O  O   . PHE   A 1 37  ? 27.891 -21.507 -41.867 1.00 58.29  ?  52  PHE   A O   1 
ATOM   278  C  CB  . PHE   A 1 37  ? 25.621 -20.938 -39.487 1.00 53.53  ?  52  PHE   A CB  1 
ATOM   279  C  CG  . PHE   A 1 37  ? 26.715 -19.942 -39.258 1.00 58.12  ?  52  PHE   A CG  1 
ATOM   280  C  CD1 . PHE   A 1 37  ? 26.730 -18.744 -39.952 1.00 63.98  ?  52  PHE   A CD1 1 
ATOM   281  C  CD2 . PHE   A 1 37  ? 27.727 -20.196 -38.347 1.00 55.97  ?  52  PHE   A CD2 1 
ATOM   282  C  CE1 . PHE   A 1 37  ? 27.737 -17.817 -39.742 1.00 53.91  ?  52  PHE   A CE1 1 
ATOM   283  C  CE2 . PHE   A 1 37  ? 28.732 -19.279 -38.133 1.00 53.28  ?  52  PHE   A CE2 1 
ATOM   284  C  CZ  . PHE   A 1 37  ? 28.741 -18.086 -38.832 1.00 52.48  ?  52  PHE   A CZ  1 
ATOM   285  N  N   . LEU   A 1 38  ? 27.574 -23.199 -40.421 1.00 55.40  ?  53  LEU   A N   1 
ATOM   286  C  CA  . LEU   A 1 38  ? 28.976 -23.598 -40.471 1.00 53.74  ?  53  LEU   A CA  1 
ATOM   287  C  C   . LEU   A 1 38  ? 29.324 -24.319 -41.765 1.00 53.70  ?  53  LEU   A C   1 
ATOM   288  O  O   . LEU   A 1 38  ? 30.489 -24.306 -42.170 1.00 55.35  ?  53  LEU   A O   1 
ATOM   289  C  CB  . LEU   A 1 38  ? 29.322 -24.487 -39.270 1.00 59.71  ?  53  LEU   A CB  1 
ATOM   290  C  CG  . LEU   A 1 38  ? 29.328 -23.876 -37.866 1.00 61.64  ?  53  LEU   A CG  1 
ATOM   291  C  CD1 . LEU   A 1 38  ? 29.527 -24.979 -36.823 1.00 54.30  ?  53  LEU   A CD1 1 
ATOM   292  C  CD2 . LEU   A 1 38  ? 30.404 -22.797 -37.714 1.00 46.31  ?  53  LEU   A CD2 1 
ATOM   293  N  N   . ARG   A 1 39  ? 28.350 -24.950 -42.432 1.00 57.03  ?  54  ARG   A N   1 
ATOM   294  C  CA  . ARG   A 1 39  ? 28.696 -25.612 -43.684 1.00 61.03  ?  54  ARG   A CA  1 
ATOM   295  C  C   . ARG   A 1 39  ? 28.984 -24.607 -44.788 1.00 58.07  ?  54  ARG   A C   1 
ATOM   296  O  O   . ARG   A 1 39  ? 29.618 -24.964 -45.780 1.00 63.63  ?  54  ARG   A O   1 
ATOM   297  C  CB  . ARG   A 1 39  ? 27.600 -26.586 -44.110 1.00 59.99  ?  54  ARG   A CB  1 
ATOM   298  C  CG  . ARG   A 1 39  ? 26.282 -25.968 -44.484 1.00 60.03  ?  54  ARG   A CG  1 
ATOM   299  C  CD  . ARG   A 1 39  ? 25.433 -27.019 -45.163 1.00 61.52  ?  54  ARG   A CD  1 
ATOM   300  N  NE  . ARG   A 1 39  ? 24.089 -26.534 -45.427 1.00 66.94  ?  54  ARG   A NE  1 
ATOM   301  C  CZ  . ARG   A 1 39  ? 23.074 -27.307 -45.780 1.00 69.43  ?  54  ARG   A CZ  1 
ATOM   302  N  NH1 . ARG   A 1 39  ? 23.220 -28.615 -45.923 1.00 69.83  ?  54  ARG   A NH1 1 
ATOM   303  N  NH2 . ARG   A 1 39  ? 21.883 -26.755 -45.989 1.00 68.81  ?  54  ARG   A NH2 1 
ATOM   304  N  N   . GLN   A 1 40  ? 28.566 -23.355 -44.617 1.00 60.60  ?  55  GLN   A N   1 
ATOM   305  C  CA  . GLN   A 1 40  ? 28.984 -22.252 -45.472 1.00 56.33  ?  55  GLN   A CA  1 
ATOM   306  C  C   . GLN   A 1 40  ? 30.181 -21.488 -44.908 1.00 55.30  ?  55  GLN   A C   1 
ATOM   307  O  O   . GLN   A 1 40  ? 31.153 -21.246 -45.630 1.00 56.36  ?  55  GLN   A O   1 
ATOM   308  C  CB  . GLN   A 1 40  ? 27.811 -21.287 -45.687 1.00 58.79  ?  55  GLN   A CB  1 
ATOM   309  C  CG  . GLN   A 1 40  ? 28.195 -19.958 -46.338 1.00 61.72  ?  55  GLN   A CG  1 
ATOM   310  C  CD  . GLN   A 1 40  ? 28.433 -20.103 -47.826 1.00 67.30  ?  55  GLN   A CD  1 
ATOM   311  O  OE1 . GLN   A 1 40  ? 28.117 -21.138 -48.409 1.00 61.36  ?  55  GLN   A OE1 1 
ATOM   312  N  NE2 . GLN   A 1 40  ? 28.993 -19.065 -48.448 1.00 63.26  ?  55  GLN   A NE2 1 
ATOM   313  N  N   . GLU   A 1 41  ? 30.160 -21.141 -43.618 1.00 53.66  ?  56  GLU   A N   1 
ATOM   314  C  CA  . GLU   A 1 41  ? 31.175 -20.250 -43.069 1.00 49.64  ?  56  GLU   A CA  1 
ATOM   315  C  C   . GLU   A 1 41  ? 32.534 -20.930 -42.948 1.00 51.88  ?  56  GLU   A C   1 
ATOM   316  O  O   . GLU   A 1 41  ? 33.579 -20.283 -43.121 1.00 48.82  ?  56  GLU   A O   1 
ATOM   317  C  CB  . GLU   A 1 41  ? 30.728 -19.737 -41.703 1.00 48.95  ?  56  GLU   A CB  1 
ATOM   318  C  CG  . GLU   A 1 41  ? 31.711 -18.789 -41.043 1.00 49.03  ?  56  GLU   A CG  1 
ATOM   319  C  CD  . GLU   A 1 41  ? 31.813 -17.460 -41.762 1.00 50.70  ?  56  GLU   A CD  1 
ATOM   320  O  OE1 . GLU   A 1 41  ? 30.977 -17.189 -42.654 1.00 50.76  ?  56  GLU   A OE1 1 
ATOM   321  O  OE2 . GLU   A 1 41  ? 32.733 -16.683 -41.431 1.00 50.53  ?  56  GLU   A OE2 1 
ATOM   322  N  N   . LEU   A 1 42  ? 32.558 -22.207 -42.607 1.00 49.06  ?  57  LEU   A N   1 
ATOM   323  C  CA  . LEU   A 1 42  ? 33.867 -22.830 -42.473 1.00 48.30  ?  57  LEU   A CA  1 
ATOM   324  C  C   . LEU   A 1 42  ? 34.548 -22.917 -43.841 1.00 48.59  ?  57  LEU   A C   1 
ATOM   325  O  O   . LEU   A 1 42  ? 35.748 -22.608 -43.940 1.00 52.31  ?  57  LEU   A O   1 
ATOM   326  C  CB  . LEU   A 1 42  ? 33.748 -24.198 -41.802 1.00 56.79  ?  57  LEU   A CB  1 
ATOM   327  C  CG  . LEU   A 1 42  ? 33.490 -24.159 -40.294 1.00 54.15  ?  57  LEU   A CG  1 
ATOM   328  C  CD1 . LEU   A 1 42  ? 33.117 -25.546 -39.776 1.00 57.61  ?  57  LEU   A CD1 1 
ATOM   329  C  CD2 . LEU   A 1 42  ? 34.691 -23.591 -39.522 1.00 56.19  ?  57  LEU   A CD2 1 
ATOM   330  N  N   . PRO   A 1 43  ? 33.852 -23.304 -44.919 1.00 51.56  ?  58  PRO   A N   1 
ATOM   331  C  CA  . PRO   A 1 43  ? 34.503 -23.213 -46.244 1.00 49.80  ?  58  PRO   A CA  1 
ATOM   332  C  C   . PRO   A 1 43  ? 34.959 -21.809 -46.606 1.00 51.52  ?  58  PRO   A C   1 
ATOM   333  O  O   . PRO   A 1 43  ? 36.012 -21.651 -47.236 1.00 53.33  ?  58  PRO   A O   1 
ATOM   334  C  CB  . PRO   A 1 43  ? 33.414 -23.719 -47.194 1.00 50.92  ?  58  PRO   A CB  1 
ATOM   335  C  CG  . PRO   A 1 43  ? 32.653 -24.683 -46.362 1.00 56.75  ?  58  PRO   A CG  1 
ATOM   336  C  CD  . PRO   A 1 43  ? 32.594 -24.064 -44.994 1.00 51.65  ?  58  PRO   A CD  1 
ATOM   337  N  N   . VAL   A 1 44  ? 34.200 -20.777 -46.227 1.00 49.93  ?  59  VAL   A N   1 
ATOM   338  C  CA  . VAL   A 1 44  ? 34.632 -19.406 -46.503 1.00 51.36  ?  59  VAL   A CA  1 
ATOM   339  C  C   . VAL   A 1 44  ? 35.942 -19.103 -45.777 1.00 48.73  ?  59  VAL   A C   1 
ATOM   340  O  O   . VAL   A 1 44  ? 36.900 -18.595 -46.374 1.00 44.80  ?  59  VAL   A O   1 
ATOM   341  C  CB  . VAL   A 1 44  ? 33.521 -18.408 -46.127 1.00 45.13  ?  59  VAL   A CB  1 
ATOM   342  C  CG1 . VAL   A 1 44  ? 34.060 -16.979 -46.105 1.00 44.38  ?  59  VAL   A CG1 1 
ATOM   343  C  CG2 . VAL   A 1 44  ? 32.381 -18.512 -47.122 1.00 47.38  ?  59  VAL   A CG2 1 
ATOM   344  N  N   . ARG   A 1 45  ? 36.015 -19.430 -44.482 1.00 45.97  ?  60  ARG   A N   1 
ATOM   345  C  CA  . ARG   A 1 45  ? 37.232 -19.114 -43.735 1.00 43.29  ?  60  ARG   A CA  1 
ATOM   346  C  C   . ARG   A 1 45  ? 38.414 -19.940 -44.220 1.00 41.59  ?  60  ARG   A C   1 
ATOM   347  O  O   . ARG   A 1 45  ? 39.530 -19.424 -44.326 1.00 46.43  ?  60  ARG   A O   1 
ATOM   348  C  CB  . ARG   A 1 45  ? 37.005 -19.312 -42.238 1.00 40.75  ?  60  ARG   A CB  1 
ATOM   349  C  CG  . ARG   A 1 45  ? 35.973 -18.339 -41.700 1.00 46.18  ?  60  ARG   A CG  1 
ATOM   350  C  CD  . ARG   A 1 45  ? 35.867 -18.338 -40.181 1.00 42.04  ?  60  ARG   A CD  1 
ATOM   351  N  NE  . ARG   A 1 45  ? 34.788 -17.448 -39.782 1.00 42.94  ?  60  ARG   A NE  1 
ATOM   352  C  CZ  . ARG   A 1 45  ? 34.575 -17.044 -38.538 1.00 43.58  ?  60  ARG   A CZ  1 
ATOM   353  N  NH1 . ARG   A 1 45  ? 35.377 -17.399 -37.550 1.00 39.11  ?  60  ARG   A NH1 1 
ATOM   354  N  NH2 . ARG   A 1 45  ? 33.527 -16.274 -38.277 1.00 43.02  ?  60  ARG   A NH2 1 
ATOM   355  N  N   . LEU   A 1 46  ? 38.185 -21.217 -44.547 1.00 43.14  ?  61  LEU   A N   1 
ATOM   356  C  CA  . LEU   A 1 46  ? 39.262 -22.066 -45.045 1.00 48.54  ?  61  LEU   A CA  1 
ATOM   357  C  C   . LEU   A 1 46  ? 39.794 -21.563 -46.380 1.00 52.71  ?  61  LEU   A C   1 
ATOM   358  O  O   . LEU   A 1 46  ? 41.010 -21.507 -46.598 1.00 49.26  ?  61  LEU   A O   1 
ATOM   359  C  CB  . LEU   A 1 46  ? 38.759 -23.503 -45.191 1.00 48.40  ?  61  LEU   A CB  1 
ATOM   360  C  CG  . LEU   A 1 46  ? 38.615 -24.277 -43.888 1.00 58.23  ?  61  LEU   A CG  1 
ATOM   361  C  CD1 . LEU   A 1 46  ? 37.923 -25.599 -44.162 1.00 54.47  ?  61  LEU   A CD1 1 
ATOM   362  C  CD2 . LEU   A 1 46  ? 40.011 -24.488 -43.283 1.00 48.05  ?  61  LEU   A CD2 1 
ATOM   363  N  N   . ALA   A 1 47  ? 38.889 -21.220 -47.300 1.00 47.43  ?  62  ALA   A N   1 
ATOM   364  C  CA  . ALA   A 1 47  ? 39.306 -20.804 -48.637 1.00 52.03  ?  62  ALA   A CA  1 
ATOM   365  C  C   . ALA   A 1 47  ? 40.038 -19.469 -48.605 1.00 48.12  ?  62  ALA   A C   1 
ATOM   366  O  O   . ALA   A 1 47  ? 41.010 -19.272 -49.347 1.00 50.74  ?  62  ALA   A O   1 
ATOM   367  C  CB  . ALA   A 1 47  ? 38.096 -20.714 -49.569 1.00 50.87  ?  62  ALA   A CB  1 
ATOM   368  N  N   . ASN   A 1 48  ? 39.571 -18.531 -47.777 1.00 46.15  ?  63  ASN   A N   1 
ATOM   369  C  CA  . ASN   A 1 48  ? 40.212 -17.221 -47.732 1.00 52.21  ?  63  ASN   A CA  1 
ATOM   370  C  C   . ASN   A 1 48  ? 41.671 -17.344 -47.302 1.00 49.99  ?  63  ASN   A C   1 
ATOM   371  O  O   . ASN   A 1 48  ? 42.555 -16.726 -47.904 1.00 52.32  ?  63  ASN   A O   1 
ATOM   372  C  CB  . ASN   A 1 48  ? 39.437 -16.277 -46.803 1.00 49.69  ?  63  ASN   A CB  1 
ATOM   373  C  CG  . ASN   A 1 48  ? 38.348 -15.469 -47.548 1.00 55.03  ?  63  ASN   A CG  1 
ATOM   374  O  OD1 . ASN   A 1 48  ? 38.512 -14.272 -47.812 1.00 46.34  ?  63  ASN   A OD1 1 
ATOM   375  N  ND2 . ASN   A 1 48  ? 37.239 -16.132 -47.879 1.00 47.71  ?  63  ASN   A ND2 1 
ATOM   376  N  N   . ILE   A 1 49  ? 41.951 -18.164 -46.287 1.00 44.80  ?  64  ILE   A N   1 
ATOM   377  C  CA  . ILE   A 1 49  ? 43.343 -18.310 -45.866 1.00 47.38  ?  64  ILE   A CA  1 
ATOM   378  C  C   . ILE   A 1 49  ? 44.134 -19.142 -46.879 1.00 50.04  ?  64  ILE   A C   1 
ATOM   379  O  O   . ILE   A 1 49  ? 45.327 -18.903 -47.091 1.00 50.51  ?  64  ILE   A O   1 
ATOM   380  C  CB  . ILE   A 1 49  ? 43.450 -18.893 -44.441 1.00 45.60  ?  64  ILE   A CB  1 
ATOM   381  C  CG1 . ILE   A 1 49  ? 44.895 -18.779 -43.939 1.00 50.24  ?  64  ILE   A CG1 1 
ATOM   382  C  CG2 . ILE   A 1 49  ? 43.029 -20.353 -44.385 1.00 42.81  ?  64  ILE   A CG2 1 
ATOM   383  C  CD1 . ILE   A 1 49  ? 45.375 -17.338 -43.852 1.00 50.21  ?  64  ILE   A CD1 1 
ATOM   384  N  N   . MET   A 1 50  ? 43.501 -20.112 -47.539 1.00 48.23  ?  65  MET   A N   1 
ATOM   385  C  CA  . MET   A 1 50  ? 44.245 -20.882 -48.533 1.00 49.53  ?  65  MET   A CA  1 
ATOM   386  C  C   . MET   A 1 50  ? 44.688 -20.001 -49.689 1.00 52.59  ?  65  MET   A C   1 
ATOM   387  O  O   . MET   A 1 50  ? 45.807 -20.147 -50.192 1.00 52.88  ?  65  MET   A O   1 
ATOM   388  C  CB  . MET   A 1 50  ? 43.419 -22.056 -49.027 1.00 53.39  ?  65  MET   A CB  1 
ATOM   389  C  CG  . MET   A 1 50  ? 43.286 -23.100 -47.951 1.00 67.91  ?  65  MET   A CG  1 
ATOM   390  S  SD  . MET   A 1 50  ? 41.924 -24.226 -48.255 1.00 80.36  ?  65  MET   A SD  1 
ATOM   391  C  CE  . MET   A 1 50  ? 42.729 -25.290 -49.399 1.00 72.02  ?  65  MET   A CE  1 
ATOM   392  N  N   . LYS   A 1 51  ? 43.835 -19.063 -50.108 1.00 53.74  ?  66  LYS   A N   1 
ATOM   393  C  CA  . LYS   A 1 51  ? 44.222 -18.151 -51.182 1.00 58.73  ?  66  LYS   A CA  1 
ATOM   394  C  C   . LYS   A 1 51  ? 45.395 -17.285 -50.757 1.00 65.13  ?  66  LYS   A C   1 
ATOM   395  O  O   . LYS   A 1 51  ? 46.269 -16.961 -51.573 1.00 55.83  ?  66  LYS   A O   1 
ATOM   396  C  CB  . LYS   A 1 51  ? 43.041 -17.259 -51.581 1.00 63.61  ?  66  LYS   A CB  1 
ATOM   397  C  CG  . LYS   A 1 51  ? 42.009 -17.924 -52.480 1.00 62.24  ?  66  LYS   A CG  1 
ATOM   398  C  CD  . LYS   A 1 51  ? 42.549 -18.178 -53.860 1.00 75.81  ?  66  LYS   A CD  1 
ATOM   399  C  CE  . LYS   A 1 51  ? 42.941 -16.886 -54.544 1.00 77.70  ?  66  LYS   A CE  1 
ATOM   400  N  NZ  . LYS   A 1 51  ? 43.164 -17.107 -55.997 1.00 80.61  ?  66  LYS   A NZ  1 
ATOM   401  N  N   . GLU   A 1 52  ? 45.417 -16.890 -49.479 1.00 50.81  ?  67  GLU   A N   1 
ATOM   402  C  CA  . GLU   A 1 52  ? 46.482 -16.039 -48.970 1.00 59.75  ?  67  GLU   A CA  1 
ATOM   403  C  C   . GLU   A 1 52  ? 47.802 -16.800 -48.879 1.00 60.41  ?  67  GLU   A C   1 
ATOM   404  O  O   . GLU   A 1 52  ? 48.863 -16.252 -49.208 1.00 61.06  ?  67  GLU   A O   1 
ATOM   405  C  CB  . GLU   A 1 52  ? 46.070 -15.466 -47.616 1.00 53.52  ?  67  GLU   A CB  1 
ATOM   406  C  CG  . GLU   A 1 52  ? 47.074 -14.499 -47.039 1.00 63.54  ?  67  GLU   A CG  1 
ATOM   407  C  CD  . GLU   A 1 52  ? 46.426 -13.350 -46.285 1.00 63.23  ?  67  GLU   A CD  1 
ATOM   408  O  OE1 . GLU   A 1 52  ? 45.175 -13.276 -46.204 1.00 65.76  ?  67  GLU   A OE1 1 
ATOM   409  O  OE2 . GLU   A 1 52  ? 47.188 -12.504 -45.782 1.00 60.78  ?  67  GLU   A OE2 1 
ATOM   410  N  N   . ILE   A 1 53  ? 47.758 -18.065 -48.442 1.00 56.83  ?  68  ILE   A N   1 
ATOM   411  C  CA  . ILE   A 1 53  ? 48.938 -18.928 -48.508 1.00 51.73  ?  68  ILE   A CA  1 
ATOM   412  C  C   . ILE   A 1 53  ? 49.512 -18.932 -49.920 1.00 60.84  ?  68  ILE   A C   1 
ATOM   413  O  O   . ILE   A 1 53  ? 50.737 -18.934 -50.113 1.00 63.77  ?  68  ILE   A O   1 
ATOM   414  C  CB  . ILE   A 1 53  ? 48.582 -20.355 -48.045 1.00 50.37  ?  68  ILE   A CB  1 
ATOM   415  C  CG1 . ILE   A 1 53  ? 48.230 -20.367 -46.557 1.00 53.40  ?  68  ILE   A CG1 1 
ATOM   416  C  CG2 . ILE   A 1 53  ? 49.706 -21.341 -48.380 1.00 57.99  ?  68  ILE   A CG2 1 
ATOM   417  C  CD1 . ILE   A 1 53  ? 47.573 -21.636 -46.127 1.00 53.84  ?  68  ILE   A CD1 1 
ATOM   418  N  N   . ASN   A 1 54  ? 48.638 -18.928 -50.932 1.00 62.03  ?  69  ASN   A N   1 
ATOM   419  C  CA  . ASN   A 1 54  ? 49.099 -18.990 -52.314 1.00 62.33  ?  69  ASN   A CA  1 
ATOM   420  C  C   . ASN   A 1 54  ? 49.768 -17.708 -52.785 1.00 63.13  ?  69  ASN   A C   1 
ATOM   421  O  O   . ASN   A 1 54  ? 50.327 -17.700 -53.884 1.00 68.06  ?  69  ASN   A O   1 
ATOM   422  C  CB  . ASN   A 1 54  ? 47.939 -19.324 -53.250 1.00 70.48  ?  69  ASN   A CB  1 
ATOM   423  C  CG  . ASN   A 1 54  ? 47.900 -20.778 -53.615 1.00 80.87  ?  69  ASN   A CG  1 
ATOM   424  O  OD1 . ASN   A 1 54  ? 48.720 -21.567 -53.141 1.00 80.00  ?  69  ASN   A OD1 1 
ATOM   425  N  ND2 . ASN   A 1 54  ? 46.945 -21.150 -54.467 1.00 96.24  ?  69  ASN   A ND2 1 
ATOM   426  N  N   . LEU   A 1 55  ? 49.705 -16.626 -52.011 1.00 61.98  ?  70  LEU   A N   1 
ATOM   427  C  CA  . LEU   A 1 55  ? 50.442 -15.411 -52.337 1.00 66.41  ?  70  LEU   A CA  1 
ATOM   428  C  C   . LEU   A 1 55  ? 51.890 -15.442 -51.855 1.00 67.61  ?  70  LEU   A C   1 
ATOM   429  O  O   . LEU   A 1 55  ? 52.651 -14.526 -52.187 1.00 65.11  ?  70  LEU   A O   1 
ATOM   430  C  CB  . LEU   A 1 55  ? 49.743 -14.186 -51.736 1.00 74.76  ?  70  LEU   A CB  1 
ATOM   431  C  CG  . LEU   A 1 55  ? 48.289 -13.879 -52.120 1.00 72.56  ?  70  LEU   A CG  1 
ATOM   432  C  CD1 . LEU   A 1 55  ? 47.767 -12.729 -51.268 1.00 79.73  ?  70  LEU   A CD1 1 
ATOM   433  C  CD2 . LEU   A 1 55  ? 48.172 -13.556 -53.593 1.00 74.99  ?  70  LEU   A CD2 1 
ATOM   434  N  N   . LEU   A 1 56  ? 52.280 -16.437 -51.057 1.00 67.77  ?  71  LEU   A N   1 
ATOM   435  C  CA  . LEU   A 1 56  ? 53.682 -16.581 -50.688 1.00 58.26  ?  71  LEU   A CA  1 
ATOM   436  C  C   . LEU   A 1 56  ? 54.505 -16.903 -51.933 1.00 55.87  ?  71  LEU   A C   1 
ATOM   437  O  O   . LEU   A 1 56  ? 54.039 -17.641 -52.804 1.00 59.27  ?  71  LEU   A O   1 
ATOM   438  C  CB  . LEU   A 1 56  ? 53.859 -17.693 -49.646 1.00 50.24  ?  71  LEU   A CB  1 
ATOM   439  C  CG  . LEU   A 1 56  ? 53.133 -17.452 -48.314 1.00 53.49  ?  71  LEU   A CG  1 
ATOM   440  C  CD1 . LEU   A 1 56  ? 53.159 -18.692 -47.458 1.00 43.15  ?  71  LEU   A CD1 1 
ATOM   441  C  CD2 . LEU   A 1 56  ? 53.767 -16.296 -47.589 1.00 54.72  ?  71  LEU   A CD2 1 
ATOM   442  N  N   . PRO   A 1 57  ? 55.737 -16.399 -52.026 1.00 60.93  ?  72  PRO   A N   1 
ATOM   443  C  CA  . PRO   A 1 57  ? 56.589 -16.737 -53.176 1.00 61.41  ?  72  PRO   A CA  1 
ATOM   444  C  C   . PRO   A 1 57  ? 56.827 -18.239 -53.265 1.00 63.68  ?  72  PRO   A C   1 
ATOM   445  O  O   . PRO   A 1 57  ? 56.701 -18.974 -52.280 1.00 59.10  ?  72  PRO   A O   1 
ATOM   446  C  CB  . PRO   A 1 57  ? 57.901 -15.988 -52.897 1.00 64.83  ?  72  PRO   A CB  1 
ATOM   447  C  CG  . PRO   A 1 57  ? 57.621 -15.067 -51.734 1.00 68.00  ?  72  PRO   A CG  1 
ATOM   448  C  CD  . PRO   A 1 57  ? 56.436 -15.599 -51.005 1.00 59.22  ?  72  PRO   A CD  1 
ATOM   449  N  N   . ASP   A 1 58  ? 57.194 -18.684 -54.473 1.00 64.04  ?  73  ASP   A N   1 
ATOM   450  C  CA  . ASP   A 1 58  ? 57.428 -20.104 -54.732 1.00 57.36  ?  73  ASP   A CA  1 
ATOM   451  C  C   . ASP   A 1 58  ? 58.488 -20.705 -53.815 1.00 53.85  ?  73  ASP   A C   1 
ATOM   452  O  O   . ASP   A 1 58  ? 58.422 -21.899 -53.494 1.00 57.83  ?  73  ASP   A O   1 
ATOM   453  C  CB  . ASP   A 1 58  ? 57.855 -20.314 -56.197 1.00 63.84  ?  73  ASP   A CB  1 
ATOM   454  C  CG  . ASP   A 1 58  ? 56.746 -20.018 -57.181 1.00 76.66  ?  73  ASP   A CG  1 
ATOM   455  O  OD1 . ASP   A 1 58  ? 55.635 -19.651 -56.738 1.00 86.38  ?  73  ASP   A OD1 1 
ATOM   456  O  OD2 . ASP   A 1 58  ? 56.986 -20.154 -58.405 1.00 92.99  ?  73  ASP   A OD2 1 
ATOM   457  N  N   . ARG   A 1 59  ? 59.488 -19.920 -53.406 1.00 59.53  ?  74  ARG   A N   1 
ATOM   458  C  CA  . ARG   A 1 59  ? 60.553 -20.477 -52.570 1.00 56.30  ?  74  ARG   A CA  1 
ATOM   459  C  C   . ARG   A 1 59  ? 60.095 -20.708 -51.131 1.00 50.66  ?  74  ARG   A C   1 
ATOM   460  O  O   . ARG   A 1 59  ? 60.781 -21.408 -50.380 1.00 51.47  ?  74  ARG   A O   1 
ATOM   461  C  CB  . ARG   A 1 59  ? 61.782 -19.568 -52.613 1.00 55.06  ?  74  ARG   A CB  1 
ATOM   462  C  CG  . ARG   A 1 59  ? 61.575 -18.218 -51.917 1.00 52.57  ?  74  ARG   A CG  1 
ATOM   463  C  CD  . ARG   A 1 59  ? 62.790 -17.298 -52.120 1.00 57.39  ?  74  ARG   A CD  1 
ATOM   464  N  NE  . ARG   A 1 59  ? 62.656 -16.005 -51.454 1.00 58.48  ?  74  ARG   A NE  1 
ATOM   465  C  CZ  . ARG   A 1 59  ? 61.951 -14.986 -51.931 1.00 62.36  ?  74  ARG   A CZ  1 
ATOM   466  N  NH1 . ARG   A 1 59  ? 61.264 -15.088 -53.058 1.00 66.11  ?  74  ARG   A NH1 1 
ATOM   467  N  NH2 . ARG   A 1 59  ? 61.940 -13.838 -51.265 1.00 62.10  ?  74  ARG   A NH2 1 
ATOM   468  N  N   . VAL   A 1 60  ? 58.970 -20.123 -50.734 1.00 48.92  ?  75  VAL   A N   1 
ATOM   469  C  CA  . VAL   A 1 60  ? 58.274 -20.465 -49.496 1.00 53.56  ?  75  VAL   A CA  1 
ATOM   470  C  C   . VAL   A 1 60  ? 57.173 -21.481 -49.754 1.00 53.43  ?  75  VAL   A C   1 
ATOM   471  O  O   . VAL   A 1 60  ? 57.082 -22.507 -49.074 1.00 49.01  ?  75  VAL   A O   1 
ATOM   472  C  CB  . VAL   A 1 60  ? 57.704 -19.183 -48.842 1.00 49.21  ?  75  VAL   A CB  1 
ATOM   473  C  CG1 . VAL   A 1 60  ? 56.968 -19.501 -47.528 1.00 47.70  ?  75  VAL   A CG1 1 
ATOM   474  C  CG2 . VAL   A 1 60  ? 58.815 -18.170 -48.599 1.00 51.44  ?  75  VAL   A CG2 1 
ATOM   475  N  N   . LEU   A 1 61  ? 56.351 -21.207 -50.767 1.00 55.92  ?  76  LEU   A N   1 
ATOM   476  C  CA  . LEU   A 1 61  ? 55.186 -22.030 -51.070 1.00 58.89  ?  76  LEU   A CA  1 
ATOM   477  C  C   . LEU   A 1 61  ? 55.557 -23.493 -51.287 1.00 60.49  ?  76  LEU   A C   1 
ATOM   478  O  O   . LEU   A 1 61  ? 54.861 -24.393 -50.801 1.00 62.74  ?  76  LEU   A O   1 
ATOM   479  C  CB  . LEU   A 1 61  ? 54.485 -21.468 -52.310 1.00 63.31  ?  76  LEU   A CB  1 
ATOM   480  C  CG  . LEU   A 1 61  ? 53.105 -22.013 -52.634 1.00 67.12  ?  76  LEU   A CG  1 
ATOM   481  C  CD1 . LEU   A 1 61  ? 52.271 -21.995 -51.372 1.00 62.21  ?  76  LEU   A CD1 1 
ATOM   482  C  CD2 . LEU   A 1 61  ? 52.455 -21.164 -53.726 1.00 71.91  ?  76  LEU   A CD2 1 
ATOM   483  N  N   . SER   A 1 62  ? 56.654 -23.752 -52.000 1.00 46.27  ?  77  SER   A N   1 
ATOM   484  C  CA  . SER   A 1 62  ? 57.034 -25.107 -52.374 1.00 60.74  ?  77  SER   A CA  1 
ATOM   485  C  C   . SER   A 1 62  ? 57.721 -25.893 -51.259 1.00 63.21  ?  77  SER   A C   1 
ATOM   486  O  O   . SER   A 1 62  ? 58.033 -27.069 -51.466 1.00 64.72  ?  77  SER   A O   1 
ATOM   487  C  CB  . SER   A 1 62  ? 57.956 -25.072 -53.596 1.00 63.85  ?  77  SER   A CB  1 
ATOM   488  O  OG  . SER   A 1 62  ? 59.194 -24.455 -53.276 1.00 64.09  ?  77  SER   A OG  1 
ATOM   489  N  N   . THR   A 1 63  ? 57.975 -25.304 -50.096 1.00 57.84  ?  78  THR   A N   1 
ATOM   490  C  CA  . THR   A 1 63  ? 58.683 -26.030 -49.047 1.00 55.32  ?  78  THR   A CA  1 
ATOM   491  C  C   . THR   A 1 63  ? 57.776 -27.110 -48.438 1.00 55.02  ?  78  THR   A C   1 
ATOM   492  O  O   . THR   A 1 63  ? 56.550 -27.031 -48.534 1.00 54.13  ?  78  THR   A O   1 
ATOM   493  C  CB  . THR   A 1 63  ? 59.165 -25.058 -47.973 1.00 56.33  ?  78  THR   A CB  1 
ATOM   494  O  OG1 . THR   A 1 63  ? 58.043 -24.352 -47.438 1.00 52.20  ?  78  THR   A OG1 1 
ATOM   495  C  CG2 . THR   A 1 63  ? 60.160 -24.060 -48.559 1.00 56.62  ?  78  THR   A CG2 1 
ATOM   496  N  N   . PRO   A 1 64  ? 58.352 -28.149 -47.825 1.00 59.12  ?  79  PRO   A N   1 
ATOM   497  C  CA  . PRO   A 1 64  ? 57.501 -29.252 -47.338 1.00 54.52  ?  79  PRO   A CA  1 
ATOM   498  C  C   . PRO   A 1 64  ? 56.499 -28.850 -46.252 1.00 55.67  ?  79  PRO   A C   1 
ATOM   499  O  O   . PRO   A 1 64  ? 55.404 -29.420 -46.192 1.00 43.83  ?  79  PRO   A O   1 
ATOM   500  C  CB  . PRO   A 1 64  ? 58.526 -30.271 -46.820 1.00 54.31  ?  79  PRO   A CB  1 
ATOM   501  C  CG  . PRO   A 1 64  ? 59.778 -29.951 -47.570 1.00 59.98  ?  79  PRO   A CG  1 
ATOM   502  C  CD  . PRO   A 1 64  ? 59.783 -28.464 -47.695 1.00 54.63  ?  79  PRO   A CD  1 
ATOM   503  N  N   . SER   A 1 65  ? 56.832 -27.892 -45.385 1.00 49.63  ?  80  SER   A N   1 
ATOM   504  C  CA  . SER   A 1 65  ? 55.913 -27.516 -44.318 1.00 48.61  ?  80  SER   A CA  1 
ATOM   505  C  C   . SER   A 1 65  ? 54.647 -26.862 -44.870 1.00 52.55  ?  80  SER   A C   1 
ATOM   506  O  O   . SER   A 1 65  ? 53.528 -27.208 -44.469 1.00 47.97  ?  80  SER   A O   1 
ATOM   507  C  CB  . SER   A 1 65  ? 56.626 -26.578 -43.353 1.00 49.48  ?  80  SER   A CB  1 
ATOM   508  O  OG  . SER   A 1 65  ? 57.183 -25.506 -44.089 1.00 46.03  ?  80  SER   A OG  1 
ATOM   509  N  N   . VAL   A 1 66  ? 54.805 -25.904 -45.782 1.00 43.89  ?  81  VAL   A N   1 
ATOM   510  C  CA  . VAL   A 1 66  ? 53.649 -25.187 -46.309 1.00 47.57  ?  81  VAL   A CA  1 
ATOM   511  C  C   . VAL   A 1 66  ? 52.769 -26.134 -47.114 1.00 56.33  ?  81  VAL   A C   1 
ATOM   512  O  O   . VAL   A 1 66  ? 51.534 -26.061 -47.054 1.00 47.65  ?  81  VAL   A O   1 
ATOM   513  C  CB  . VAL   A 1 66  ? 54.114 -23.972 -47.140 1.00 54.18  ?  81  VAL   A CB  1 
ATOM   514  C  CG1 . VAL   A 1 66  ? 52.932 -23.275 -47.845 1.00 52.04  ?  81  VAL   A CG1 1 
ATOM   515  C  CG2 . VAL   A 1 66  ? 54.865 -22.981 -46.228 1.00 47.96  ?  81  VAL   A CG2 1 
ATOM   516  N  N   . GLN   A 1 67  ? 53.392 -27.075 -47.837 1.00 53.38  ?  82  GLN   A N   1 
ATOM   517  C  CA  . GLN   A 1 67  ? 52.622 -28.014 -48.647 1.00 53.46  ?  82  GLN   A CA  1 
ATOM   518  C  C   . GLN   A 1 67  ? 51.829 -28.967 -47.767 1.00 53.61  ?  82  GLN   A C   1 
ATOM   519  O  O   . GLN   A 1 67  ? 50.700 -29.335 -48.103 1.00 53.28  ?  82  GLN   A O   1 
ATOM   520  C  CB  . GLN   A 1 67  ? 53.549 -28.784 -49.595 1.00 55.82  ?  82  GLN   A CB  1 
ATOM   521  C  CG  . GLN   A 1 67  ? 54.066 -27.955 -50.782 1.00 63.27  ?  82  GLN   A CG  1 
ATOM   522  C  CD  . GLN   A 1 67  ? 52.939 -27.407 -51.662 1.00 76.70  ?  82  GLN   A CD  1 
ATOM   523  O  OE1 . GLN   A 1 67  ? 52.099 -28.164 -52.158 1.00 81.95  ?  82  GLN   A OE1 1 
ATOM   524  N  NE2 . GLN   A 1 67  ? 52.917 -26.087 -51.853 1.00 64.42  ?  82  GLN   A NE2 1 
ATOM   525  N  N   . LEU   A 1 68  ? 52.387 -29.360 -46.627 1.00 47.24  ?  83  LEU   A N   1 
ATOM   526  C  CA  . LEU   A 1 68  ? 51.649 -30.244 -45.731 1.00 56.31  ?  83  LEU   A CA  1 
ATOM   527  C  C   . LEU   A 1 68  ? 50.461 -29.519 -45.100 1.00 53.29  ?  83  LEU   A C   1 
ATOM   528  O  O   . LEU   A 1 68  ? 49.372 -30.091 -44.969 1.00 51.90  ?  83  LEU   A O   1 
ATOM   529  C  CB  . LEU   A 1 68  ? 52.582 -30.788 -44.657 1.00 53.79  ?  83  LEU   A CB  1 
ATOM   530  C  CG  . LEU   A 1 68  ? 51.935 -31.610 -43.540 1.00 60.83  ?  83  LEU   A CG  1 
ATOM   531  C  CD1 . LEU   A 1 68  ? 51.339 -32.906 -44.094 1.00 56.63  ?  83  LEU   A CD1 1 
ATOM   532  C  CD2 . LEU   A 1 68  ? 52.971 -31.917 -42.467 1.00 58.46  ?  83  LEU   A CD2 1 
ATOM   533  N  N   . VAL   A 1 69  ? 50.648 -28.262 -44.706 1.00 53.64  ?  84  VAL   A N   1 
ATOM   534  C  CA  . VAL   A 1 69  ? 49.533 -27.492 -44.155 1.00 53.67  ?  84  VAL   A CA  1 
ATOM   535  C  C   . VAL   A 1 69  ? 48.450 -27.294 -45.215 1.00 49.32  ?  84  VAL   A C   1 
ATOM   536  O  O   . VAL   A 1 69  ? 47.259 -27.480 -44.950 1.00 46.68  ?  84  VAL   A O   1 
ATOM   537  C  CB  . VAL   A 1 69  ? 50.020 -26.149 -43.582 1.00 53.01  ?  84  VAL   A CB  1 
ATOM   538  C  CG1 . VAL   A 1 69  ? 48.820 -25.262 -43.241 1.00 51.58  ?  84  VAL   A CG1 1 
ATOM   539  C  CG2 . VAL   A 1 69  ? 50.885 -26.377 -42.341 1.00 44.89  ?  84  VAL   A CG2 1 
ATOM   540  N  N   . GLN   A 1 70  ? 48.845 -26.905 -46.429 1.00 44.58  ?  85  GLN   A N   1 
ATOM   541  C  CA  . GLN   A 1 70  ? 47.881 -26.832 -47.519 1.00 50.42  ?  85  GLN   A CA  1 
ATOM   542  C  C   . GLN   A 1 70  ? 47.131 -28.148 -47.709 1.00 60.79  ?  85  GLN   A C   1 
ATOM   543  O  O   . GLN   A 1 70  ? 45.913 -28.145 -47.914 1.00 61.04  ?  85  GLN   A O   1 
ATOM   544  C  CB  . GLN   A 1 70  ? 48.582 -26.453 -48.819 1.00 63.35  ?  85  GLN   A CB  1 
ATOM   545  C  CG  . GLN   A 1 70  ? 48.795 -24.972 -49.017 1.00 62.85  ?  85  GLN   A CG  1 
ATOM   546  C  CD  . GLN   A 1 70  ? 49.484 -24.676 -50.334 1.00 77.38  ?  85  GLN   A CD  1 
ATOM   547  O  OE1 . GLN   A 1 70  ? 50.296 -25.471 -50.814 1.00 83.35  ?  85  GLN   A OE1 1 
ATOM   548  N  NE2 . GLN   A 1 70  ? 49.153 -23.536 -50.935 1.00 76.43  ?  85  GLN   A NE2 1 
ATOM   549  N  N   . SER   A 1 71  ? 47.837 -29.286 -47.665 1.00 53.46  ?  86  SER   A N   1 
ATOM   550  C  CA  . SER   A 1 71  ? 47.148 -30.554 -47.894 1.00 58.20  ?  86  SER   A CA  1 
ATOM   551  C  C   . SER   A 1 71  ? 46.113 -30.812 -46.810 1.00 57.66  ?  86  SER   A C   1 
ATOM   552  O  O   . SER   A 1 71  ? 45.075 -31.426 -47.076 1.00 59.58  ?  86  SER   A O   1 
ATOM   553  C  CB  . SER   A 1 71  ? 48.147 -31.716 -47.962 1.00 59.41  ?  86  SER   A CB  1 
ATOM   554  O  OG  . SER   A 1 71  ? 48.641 -32.017 -46.662 1.00 62.03  ?  86  SER   A OG  1 
ATOM   555  N  N   . TRP   A 1 72  ? 46.368 -30.338 -45.594 1.00 50.93  ?  87  TRP   A N   1 
ATOM   556  C  CA  . TRP   A 1 72  ? 45.389 -30.491 -44.527 1.00 57.97  ?  87  TRP   A CA  1 
ATOM   557  C  C   . TRP   A 1 72  ? 44.176 -29.609 -44.779 1.00 57.62  ?  87  TRP   A C   1 
ATOM   558  O  O   . TRP   A 1 72  ? 43.034 -30.081 -44.731 1.00 54.57  ?  87  TRP   A O   1 
ATOM   559  C  CB  . TRP   A 1 72  ? 46.010 -30.146 -43.181 1.00 48.14  ?  87  TRP   A CB  1 
ATOM   560  C  CG  . TRP   A 1 72  ? 47.046 -31.081 -42.709 1.00 53.93  ?  87  TRP   A CG  1 
ATOM   561  C  CD1 . TRP   A 1 72  ? 47.265 -32.359 -43.140 1.00 63.21  ?  87  TRP   A CD1 1 
ATOM   562  C  CD2 . TRP   A 1 72  ? 48.026 -30.822 -41.696 1.00 56.17  ?  87  TRP   A CD2 1 
ATOM   563  N  NE1 . TRP   A 1 72  ? 48.325 -32.910 -42.451 1.00 62.40  ?  87  TRP   A NE1 1 
ATOM   564  C  CE2 . TRP   A 1 72  ? 48.810 -31.984 -41.565 1.00 64.30  ?  87  TRP   A CE2 1 
ATOM   565  C  CE3 . TRP   A 1 72  ? 48.324 -29.713 -40.896 1.00 61.63  ?  87  TRP   A CE3 1 
ATOM   566  C  CZ2 . TRP   A 1 72  ? 49.866 -32.074 -40.660 1.00 67.07  ?  87  TRP   A CZ2 1 
ATOM   567  C  CZ3 . TRP   A 1 72  ? 49.371 -29.806 -39.994 1.00 60.77  ?  87  TRP   A CZ3 1 
ATOM   568  C  CH2 . TRP   A 1 72  ? 50.129 -30.974 -39.887 1.00 60.90  ?  87  TRP   A CH2 1 
ATOM   569  N  N   . TYR   A 1 73  ? 44.403 -28.322 -45.047 1.00 47.69  ?  88  TYR   A N   1 
ATOM   570  C  CA  . TYR   A 1 73  ? 43.276 -27.421 -45.264 1.00 51.01  ?  88  TYR   A CA  1 
ATOM   571  C  C   . TYR   A 1 73  ? 42.420 -27.884 -46.433 1.00 58.20  ?  88  TYR   A C   1 
ATOM   572  O  O   . TYR   A 1 73  ? 41.188 -27.814 -46.368 1.00 51.73  ?  88  TYR   A O   1 
ATOM   573  C  CB  . TYR   A 1 73  ? 43.778 -25.994 -45.471 1.00 49.65  ?  88  TYR   A CB  1 
ATOM   574  C  CG  . TYR   A 1 73  ? 44.121 -25.310 -44.158 1.00 48.64  ?  88  TYR   A CG  1 
ATOM   575  C  CD1 . TYR   A 1 73  ? 44.486 -26.049 -43.038 1.00 50.95  ?  88  TYR   A CD1 1 
ATOM   576  C  CD2 . TYR   A 1 73  ? 44.035 -23.933 -44.027 1.00 56.61  ?  88  TYR   A CD2 1 
ATOM   577  C  CE1 . TYR   A 1 73  ? 44.780 -25.418 -41.811 1.00 47.92  ?  88  TYR   A CE1 1 
ATOM   578  C  CE2 . TYR   A 1 73  ? 44.315 -23.298 -42.815 1.00 57.87  ?  88  TYR   A CE2 1 
ATOM   579  C  CZ  . TYR   A 1 73  ? 44.685 -24.050 -41.714 1.00 50.18  ?  88  TYR   A CZ  1 
ATOM   580  O  OH  . TYR   A 1 73  ? 44.968 -23.420 -40.522 1.00 56.22  ?  88  TYR   A OH  1 
ATOM   581  N  N   . VAL   A 1 74  ? 43.053 -28.405 -47.491 1.00 56.95  ?  89  VAL   A N   1 
ATOM   582  C  CA  . VAL   A 1 74  ? 42.310 -28.890 -48.654 1.00 56.49  ?  89  VAL   A CA  1 
ATOM   583  C  C   . VAL   A 1 74  ? 41.367 -30.013 -48.248 1.00 62.28  ?  89  VAL   A C   1 
ATOM   584  O  O   . VAL   A 1 74  ? 40.201 -30.050 -48.657 1.00 58.98  ?  89  VAL   A O   1 
ATOM   585  C  CB  . VAL   A 1 74  ? 43.276 -29.362 -49.754 1.00 60.38  ?  89  VAL   A CB  1 
ATOM   586  C  CG1 . VAL   A 1 74  ? 42.536 -30.201 -50.790 1.00 66.25  ?  89  VAL   A CG1 1 
ATOM   587  C  CG2 . VAL   A 1 74  ? 43.954 -28.195 -50.408 1.00 59.85  ?  89  VAL   A CG2 1 
ATOM   588  N  N   . GLN   A 1 75  ? 41.867 -30.953 -47.444 1.00 60.33  ?  90  GLN   A N   1 
ATOM   589  C  CA  . GLN   A 1 75  ? 41.062 -32.106 -47.062 1.00 66.00  ?  90  GLN   A CA  1 
ATOM   590  C  C   . GLN   A 1 75  ? 39.927 -31.690 -46.141 1.00 62.02  ?  90  GLN   A C   1 
ATOM   591  O  O   . GLN   A 1 75  ? 38.810 -32.218 -46.232 1.00 58.76  ?  90  GLN   A O   1 
ATOM   592  C  CB  . GLN   A 1 75  ? 41.939 -33.159 -46.385 1.00 66.44  ?  90  GLN   A CB  1 
ATOM   593  C  CG  . GLN   A 1 75  ? 41.254 -34.507 -46.212 1.00 62.56  ?  90  GLN   A CG  1 
ATOM   594  C  CD  . GLN   A 1 75  ? 40.843 -35.100 -47.539 1.00 66.66  ?  90  GLN   A CD  1 
ATOM   595  O  OE1 . GLN   A 1 75  ? 41.686 -35.523 -48.327 1.00 66.32  ?  90  GLN   A OE1 1 
ATOM   596  N  NE2 . GLN   A 1 75  ? 39.539 -35.109 -47.811 1.00 64.10  ?  90  GLN   A NE2 1 
ATOM   597  N  N   . SER   A 1 76  ? 40.195 -30.741 -45.251 1.00 54.73  ?  91  SER   A N   1 
ATOM   598  C  CA  . SER   A 1 76  ? 39.135 -30.248 -44.387 1.00 57.98  ?  91  SER   A CA  1 
ATOM   599  C  C   . SER   A 1 76  ? 38.063 -29.533 -45.196 1.00 60.03  ?  91  SER   A C   1 
ATOM   600  O  O   . SER   A 1 76  ? 36.868 -29.702 -44.935 1.00 64.38  ?  91  SER   A O   1 
ATOM   601  C  CB  . SER   A 1 76  ? 39.728 -29.338 -43.316 1.00 52.61  ?  91  SER   A CB  1 
ATOM   602  O  OG  . SER   A 1 76  ? 40.732 -30.043 -42.601 1.00 54.25  ?  91  SER   A OG  1 
ATOM   603  N  N   . LEU   A 1 77  ? 38.469 -28.739 -46.189 1.00 63.20  ?  92  LEU   A N   1 
ATOM   604  C  CA  . LEU   A 1 77  ? 37.498 -28.061 -47.041 1.00 53.36  ?  92  LEU   A CA  1 
ATOM   605  C  C   . LEU   A 1 77  ? 36.637 -29.066 -47.793 1.00 61.02  ?  92  LEU   A C   1 
ATOM   606  O  O   . LEU   A 1 77  ? 35.427 -28.862 -47.962 1.00 62.65  ?  92  LEU   A O   1 
ATOM   607  C  CB  . LEU   A 1 77  ? 38.230 -27.131 -48.012 1.00 59.01  ?  92  LEU   A CB  1 
ATOM   608  C  CG  . LEU   A 1 77  ? 37.405 -26.383 -49.061 1.00 64.59  ?  92  LEU   A CG  1 
ATOM   609  C  CD1 . LEU   A 1 77  ? 36.310 -25.579 -48.368 1.00 54.69  ?  92  LEU   A CD1 1 
ATOM   610  C  CD2 . LEU   A 1 77  ? 38.313 -25.465 -49.859 1.00 60.58  ?  92  LEU   A CD2 1 
ATOM   611  N  N   . LEU   A 1 78  ? 37.243 -30.165 -48.246 1.00 59.20  ?  93  LEU   A N   1 
ATOM   612  C  CA  . LEU   A 1 78  ? 36.488 -31.199 -48.944 1.00 64.25  ?  93  LEU   A CA  1 
ATOM   613  C  C   . LEU   A 1 78  ? 35.581 -31.962 -47.989 1.00 65.92  ?  93  LEU   A C   1 
ATOM   614  O  O   . LEU   A 1 78  ? 34.430 -32.264 -48.328 1.00 61.02  ?  93  LEU   A O   1 
ATOM   615  C  CB  . LEU   A 1 78  ? 37.445 -32.159 -49.645 1.00 67.45  ?  93  LEU   A CB  1 
ATOM   616  C  CG  . LEU   A 1 78  ? 38.316 -31.537 -50.731 1.00 69.68  ?  93  LEU   A CG  1 
ATOM   617  C  CD1 . LEU   A 1 78  ? 39.253 -32.580 -51.322 1.00 70.44  ?  93  LEU   A CD1 1 
ATOM   618  C  CD2 . LEU   A 1 78  ? 37.447 -30.914 -51.821 1.00 76.89  ?  93  LEU   A CD2 1 
ATOM   619  N  N   . ASP   A 1 79  ? 36.091 -32.296 -46.799 1.00 60.37  ?  94  ASP   A N   1 
ATOM   620  C  CA  . ASP   A 1 79  ? 35.255 -32.909 -45.771 1.00 62.08  ?  94  ASP   A CA  1 
ATOM   621  C  C   . ASP   A 1 79  ? 33.961 -32.124 -45.560 1.00 64.18  ?  94  ASP   A C   1 
ATOM   622  O  O   . ASP   A 1 79  ? 32.880 -32.711 -45.458 1.00 65.36  ?  94  ASP   A O   1 
ATOM   623  C  CB  . ASP   A 1 79  ? 36.029 -33.003 -44.452 1.00 62.74  ?  94  ASP   A CB  1 
ATOM   624  C  CG  . ASP   A 1 79  ? 37.113 -34.069 -44.470 1.00 65.34  ?  94  ASP   A CG  1 
ATOM   625  O  OD1 . ASP   A 1 79  ? 37.199 -34.830 -45.454 1.00 62.24  ?  94  ASP   A OD1 1 
ATOM   626  O  OD2 . ASP   A 1 79  ? 37.877 -34.149 -43.478 1.00 62.70  ?  94  ASP   A OD2 1 
ATOM   627  N  N   . ILE   A 1 80  ? 34.050 -30.793 -45.490 1.00 67.97  ?  95  ILE   A N   1 
ATOM   628  C  CA  . ILE   A 1 80  ? 32.857 -29.998 -45.198 1.00 63.27  ?  95  ILE   A CA  1 
ATOM   629  C  C   . ILE   A 1 80  ? 31.946 -29.910 -46.413 1.00 71.28  ?  95  ILE   A C   1 
ATOM   630  O  O   . ILE   A 1 80  ? 30.718 -29.993 -46.286 1.00 64.41  ?  95  ILE   A O   1 
ATOM   631  C  CB  . ILE   A 1 80  ? 33.250 -28.606 -44.688 1.00 59.38  ?  95  ILE   A CB  1 
ATOM   632  C  CG1 . ILE   A 1 80  ? 34.062 -28.744 -43.401 1.00 56.22  ?  95  ILE   A CG1 1 
ATOM   633  C  CG2 . ILE   A 1 80  ? 32.001 -27.761 -44.457 1.00 56.33  ?  95  ILE   A CG2 1 
ATOM   634  C  CD1 . ILE   A 1 80  ? 34.525 -27.444 -42.828 1.00 68.54  ?  95  ILE   A CD1 1 
ATOM   635  N  N   . MET   A 1 81  ? 32.522 -29.747 -47.608 1.00 64.17  ?  96  MET   A N   1 
ATOM   636  C  CA  . MET   A 1 81  ? 31.709 -29.619 -48.812 1.00 71.45  ?  96  MET   A CA  1 
ATOM   637  C  C   . MET   A 1 81  ? 30.792 -30.825 -49.036 1.00 71.32  ?  96  MET   A C   1 
ATOM   638  O  O   . MET   A 1 81  ? 29.799 -30.702 -49.763 1.00 70.31  ?  96  MET   A O   1 
ATOM   639  C  CB  . MET   A 1 81  ? 32.612 -29.391 -50.032 1.00 75.59  ?  96  MET   A CB  1 
ATOM   640  C  CG  . MET   A 1 81  ? 33.161 -27.956 -50.168 1.00 70.71  ?  96  MET   A CG  1 
ATOM   641  S  SD  . MET   A 1 81  ? 34.474 -27.809 -51.429 1.00 81.72  ?  96  MET   A SD  1 
ATOM   642  C  CE  . MET   A 1 81  ? 33.688 -28.567 -52.856 1.00 72.85  ?  96  MET   A CE  1 
ATOM   643  N  N   . GLU   A 1 82  ? 31.074 -31.976 -48.408 1.00 68.81  ?  97  GLU   A N   1 
ATOM   644  C  CA  . GLU   A 1 82  ? 30.168 -33.121 -48.528 1.00 74.49  ?  97  GLU   A CA  1 
ATOM   645  C  C   . GLU   A 1 82  ? 28.789 -32.827 -47.951 1.00 73.57  ?  97  GLU   A C   1 
ATOM   646  O  O   . GLU   A 1 82  ? 27.806 -33.470 -48.340 1.00 76.20  ?  97  GLU   A O   1 
ATOM   647  C  CB  . GLU   A 1 82  ? 30.740 -34.353 -47.819 1.00 75.72  ?  97  GLU   A CB  1 
ATOM   648  C  CG  . GLU   A 1 82  ? 32.053 -34.868 -48.361 1.00 75.15  ?  97  GLU   A CG  1 
ATOM   649  C  CD  . GLU   A 1 82  ? 31.879 -35.895 -49.460 1.00 93.60  ?  97  GLU   A CD  1 
ATOM   650  O  OE1 . GLU   A 1 82  ? 30.781 -36.488 -49.588 1.00 97.81  ?  97  GLU   A OE1 1 
ATOM   651  O  OE2 . GLU   A 1 82  ? 32.859 -36.118 -50.198 1.00 101.43 ?  97  GLU   A OE2 1 
ATOM   652  N  N   . PHE   A 1 83  ? 28.694 -31.899 -47.006 1.00 63.14  ?  98  PHE   A N   1 
ATOM   653  C  CA  . PHE   A 1 83  ? 27.435 -31.642 -46.321 1.00 75.26  ?  98  PHE   A CA  1 
ATOM   654  C  C   . PHE   A 1 83  ? 26.586 -30.574 -46.999 1.00 77.50  ?  98  PHE   A C   1 
ATOM   655  O  O   . PHE   A 1 83  ? 25.480 -30.293 -46.521 1.00 74.64  ?  98  PHE   A O   1 
ATOM   656  C  CB  . PHE   A 1 83  ? 27.707 -31.249 -44.859 1.00 68.88  ?  98  PHE   A CB  1 
ATOM   657  C  CG  . PHE   A 1 83  ? 28.320 -32.358 -44.056 1.00 75.34  ?  98  PHE   A CG  1 
ATOM   658  C  CD1 . PHE   A 1 83  ? 29.691 -32.530 -44.022 1.00 66.21  ?  98  PHE   A CD1 1 
ATOM   659  C  CD2 . PHE   A 1 83  ? 27.519 -33.255 -43.374 1.00 75.51  ?  98  PHE   A CD2 1 
ATOM   660  C  CE1 . PHE   A 1 83  ? 30.254 -33.566 -43.311 1.00 65.90  ?  98  PHE   A CE1 1 
ATOM   661  C  CE2 . PHE   A 1 83  ? 28.076 -34.293 -42.656 1.00 75.02  ?  98  PHE   A CE2 1 
ATOM   662  C  CZ  . PHE   A 1 83  ? 29.451 -34.446 -42.624 1.00 76.21  ?  98  PHE   A CZ  1 
ATOM   663  N  N   . LEU   A 1 84  ? 27.061 -29.996 -48.107 1.00 76.29  ?  99  LEU   A N   1 
ATOM   664  C  CA  . LEU   A 1 84  ? 26.380 -28.847 -48.697 1.00 80.96  ?  99  LEU   A CA  1 
ATOM   665  C  C   . LEU   A 1 84  ? 24.989 -29.217 -49.187 1.00 81.65  ?  99  LEU   A C   1 
ATOM   666  O  O   . LEU   A 1 84  ? 24.047 -28.425 -49.063 1.00 80.99  ?  99  LEU   A O   1 
ATOM   667  C  CB  . LEU   A 1 84  ? 27.216 -28.267 -49.840 1.00 76.06  ?  99  LEU   A CB  1 
ATOM   668  C  CG  . LEU   A 1 84  ? 28.391 -27.396 -49.388 1.00 84.42  ?  99  LEU   A CG  1 
ATOM   669  C  CD1 . LEU   A 1 84  ? 29.394 -27.224 -50.516 1.00 81.75  ?  99  LEU   A CD1 1 
ATOM   670  C  CD2 . LEU   A 1 84  ? 27.899 -26.041 -48.888 1.00 80.79  ?  99  LEU   A CD2 1 
ATOM   671  N  N   . ASP   A 1 85  ? 24.837 -30.415 -49.731 1.00 81.91  ?  100 ASP   A N   1 
ATOM   672  C  CA  . ASP   A 1 85  ? 23.569 -30.852 -50.296 1.00 95.58  ?  100 ASP   A CA  1 
ATOM   673  C  C   . ASP   A 1 85  ? 22.725 -31.649 -49.310 1.00 90.51  ?  100 ASP   A C   1 
ATOM   674  O  O   . ASP   A 1 85  ? 21.595 -32.012 -49.642 1.00 92.86  ?  100 ASP   A O   1 
ATOM   675  C  CB  . ASP   A 1 85  ? 23.816 -31.685 -51.560 1.00 90.51  ?  100 ASP   A CB  1 
ATOM   676  C  CG  . ASP   A 1 85  ? 24.692 -32.904 -51.297 1.00 97.93  ?  100 ASP   A CG  1 
ATOM   677  O  OD1 . ASP   A 1 85  ? 25.439 -32.911 -50.289 1.00 94.73  ?  100 ASP   A OD1 1 
ATOM   678  O  OD2 . ASP   A 1 85  ? 24.639 -33.851 -52.107 1.00 101.74 ?  100 ASP   A OD2 1 
ATOM   679  N  N   . LYS   A 1 86  ? 23.231 -31.913 -48.110 1.00 84.88  ?  101 LYS   A N   1 
ATOM   680  C  CA  . LYS   A 1 86  ? 22.538 -32.813 -47.206 1.00 89.24  ?  101 LYS   A CA  1 
ATOM   681  C  C   . LYS   A 1 86  ? 21.404 -32.091 -46.475 1.00 90.12  ?  101 LYS   A C   1 
ATOM   682  O  O   . LYS   A 1 86  ? 21.289 -30.861 -46.493 1.00 82.25  ?  101 LYS   A O   1 
ATOM   683  C  CB  . LYS   A 1 86  ? 23.525 -33.442 -46.224 1.00 86.79  ?  101 LYS   A CB  1 
ATOM   684  C  CG  . LYS   A 1 86  ? 24.561 -34.303 -46.927 1.00 88.66  ?  101 LYS   A CG  1 
ATOM   685  C  CD  . LYS   A 1 86  ? 25.214 -35.310 -46.006 1.00 88.19  ?  101 LYS   A CD  1 
ATOM   686  C  CE  . LYS   A 1 86  ? 25.724 -36.497 -46.814 1.00 105.97 ?  101 LYS   A CE  1 
ATOM   687  N  NZ  . LYS   A 1 86  ? 26.787 -37.240 -46.087 1.00 110.21 ?  101 LYS   A NZ  1 
ATOM   688  N  N   . ASP   A 1 87  ? 20.566 -32.895 -45.816 1.00 85.62  ?  102 ASP   A N   1 
ATOM   689  C  CA  . ASP   A 1 87  ? 19.298 -32.465 -45.244 1.00 84.35  ?  102 ASP   A CA  1 
ATOM   690  C  C   . ASP   A 1 87  ? 19.474 -32.127 -43.767 1.00 90.32  ?  102 ASP   A C   1 
ATOM   691  O  O   . ASP   A 1 87  ? 19.741 -33.034 -42.964 1.00 85.61  ?  102 ASP   A O   1 
ATOM   692  C  CB  . ASP   A 1 87  ? 18.267 -33.584 -45.424 1.00 85.12  ?  102 ASP   A CB  1 
ATOM   693  C  CG  . ASP   A 1 87  ? 16.851 -33.167 -45.053 1.00 95.11  ?  102 ASP   A CG  1 
ATOM   694  O  OD1 . ASP   A 1 87  ? 16.662 -32.087 -44.451 1.00 96.32  ?  102 ASP   A OD1 1 
ATOM   695  O  OD2 . ASP   A 1 87  ? 15.916 -33.940 -45.372 1.00 95.28  ?  102 ASP   A OD2 1 
ATOM   696  N  N   . PRO   A 1 88  ? 19.334 -30.859 -43.358 1.00 89.23  ?  103 PRO   A N   1 
ATOM   697  C  CA  . PRO   A 1 88  ? 19.490 -30.521 -41.929 1.00 86.35  ?  103 PRO   A CA  1 
ATOM   698  C  C   . PRO   A 1 88  ? 18.450 -31.157 -41.022 1.00 91.64  ?  103 PRO   A C   1 
ATOM   699  O  O   . PRO   A 1 88  ? 18.668 -31.214 -39.806 1.00 90.08  ?  103 PRO   A O   1 
ATOM   700  C  CB  . PRO   A 1 88  ? 19.374 -28.990 -41.913 1.00 82.89  ?  103 PRO   A CB  1 
ATOM   701  C  CG  . PRO   A 1 88  ? 19.711 -28.570 -43.300 1.00 82.80  ?  103 PRO   A CG  1 
ATOM   702  C  CD  . PRO   A 1 88  ? 19.196 -29.655 -44.193 1.00 80.86  ?  103 PRO   A CD  1 
ATOM   703  N  N   . GLU   A 1 89  ? 17.328 -31.630 -41.568 1.00 96.99  ?  104 GLU   A N   1 
ATOM   704  C  CA  . GLU   A 1 89  ? 16.326 -32.301 -40.747 1.00 98.92  ?  104 GLU   A CA  1 
ATOM   705  C  C   . GLU   A 1 89  ? 16.762 -33.711 -40.371 1.00 102.75 ?  104 GLU   A C   1 
ATOM   706  O  O   . GLU   A 1 89  ? 16.383 -34.217 -39.308 1.00 107.86 ?  104 GLU   A O   1 
ATOM   707  C  CB  . GLU   A 1 89  ? 14.990 -32.343 -41.489 1.00 104.37 ?  104 GLU   A CB  1 
ATOM   708  C  CG  . GLU   A 1 89  ? 14.526 -30.994 -42.019 1.00 105.88 ?  104 GLU   A CG  1 
ATOM   709  C  CD  . GLU   A 1 89  ? 14.071 -30.054 -40.916 1.00 113.08 ?  104 GLU   A CD  1 
ATOM   710  O  OE1 . GLU   A 1 89  ? 13.576 -30.543 -39.878 1.00 118.58 ?  104 GLU   A OE1 1 
ATOM   711  O  OE2 . GLU   A 1 89  ? 14.209 -28.824 -41.086 1.00 114.18 ?  104 GLU   A OE2 1 
ATOM   712  N  N   . ASP   A 1 90  ? 17.545 -34.358 -41.230 1.00 98.02  ?  105 ASP   A N   1 
ATOM   713  C  CA  . ASP   A 1 90  ? 18.040 -35.706 -40.974 1.00 102.00 ?  105 ASP   A CA  1 
ATOM   714  C  C   . ASP   A 1 90  ? 19.046 -35.657 -39.829 1.00 98.65  ?  105 ASP   A C   1 
ATOM   715  O  O   . ASP   A 1 90  ? 20.117 -35.056 -39.958 1.00 96.23  ?  105 ASP   A O   1 
ATOM   716  C  CB  . ASP   A 1 90  ? 18.667 -36.267 -42.249 1.00 97.23  ?  105 ASP   A CB  1 
ATOM   717  C  CG  . ASP   A 1 90  ? 18.868 -37.765 -42.199 1.00 97.71  ?  105 ASP   A CG  1 
ATOM   718  O  OD1 . ASP   A 1 90  ? 19.083 -38.306 -41.093 1.00 97.50  ?  105 ASP   A OD1 1 
ATOM   719  O  OD2 . ASP   A 1 90  ? 18.815 -38.402 -43.274 1.00 106.51 ?  105 ASP   A OD2 1 
ATOM   720  N  N   . HIS   A 1 91  ? 18.706 -36.287 -38.700 1.00 103.54 ?  106 HIS   A N   1 
ATOM   721  C  CA  . HIS   A 1 91  ? 19.577 -36.219 -37.533 1.00 100.81 ?  106 HIS   A CA  1 
ATOM   722  C  C   . HIS   A 1 91  ? 20.871 -36.997 -37.725 1.00 93.88  ?  106 HIS   A C   1 
ATOM   723  O  O   . HIS   A 1 91  ? 21.853 -36.707 -37.036 1.00 89.84  ?  106 HIS   A O   1 
ATOM   724  C  CB  . HIS   A 1 91  ? 18.833 -36.704 -36.288 1.00 108.84 ?  106 HIS   A CB  1 
ATOM   725  C  CG  . HIS   A 1 91  ? 18.024 -35.632 -35.622 1.00 127.42 ?  106 HIS   A CG  1 
ATOM   726  N  ND1 . HIS   A 1 91  ? 17.833 -35.575 -34.258 1.00 135.15 ?  106 HIS   A ND1 1 
ATOM   727  C  CD2 . HIS   A 1 91  ? 17.367 -34.564 -36.137 1.00 127.85 ?  106 HIS   A CD2 1 
ATOM   728  C  CE1 . HIS   A 1 91  ? 17.089 -34.523 -33.962 1.00 132.19 ?  106 HIS   A CE1 1 
ATOM   729  N  NE2 . HIS   A 1 91  ? 16.793 -33.893 -35.085 1.00 130.55 ?  106 HIS   A NE2 1 
ATOM   730  N  N   . ARG   A 1 92  ? 20.903 -37.962 -38.648 1.00 93.58  ?  107 ARG   A N   1 
ATOM   731  C  CA  . ARG   A 1 92  ? 22.168 -38.612 -38.978 1.00 88.22  ?  107 ARG   A CA  1 
ATOM   732  C  C   . ARG   A 1 92  ? 23.136 -37.641 -39.644 1.00 84.77  ?  107 ARG   A C   1 
ATOM   733  O  O   . ARG   A 1 92  ? 24.353 -37.747 -39.447 1.00 84.64  ?  107 ARG   A O   1 
ATOM   734  C  CB  . ARG   A 1 92  ? 21.924 -39.822 -39.879 1.00 91.39  ?  107 ARG   A CB  1 
ATOM   735  C  CG  . ARG   A 1 92  ? 20.972 -40.837 -39.278 1.00 110.98 ?  107 ARG   A CG  1 
ATOM   736  C  CD  . ARG   A 1 92  ? 20.976 -42.145 -40.051 1.00 121.09 ?  107 ARG   A CD  1 
ATOM   737  N  NE  . ARG   A 1 92  ? 20.747 -43.277 -39.161 1.00 128.38 ?  107 ARG   A NE  1 
ATOM   738  C  CZ  . ARG   A 1 92  ? 20.707 -44.546 -39.548 1.00 138.33 ?  107 ARG   A CZ  1 
ATOM   739  N  NH1 . ARG   A 1 92  ? 20.866 -44.886 -40.817 1.00 132.45 ?  107 ARG   A NH1 1 
ATOM   740  N  NH2 . ARG   A 1 92  ? 20.502 -45.496 -38.639 1.00 134.77 ?  107 ARG   A NH2 1 
ATOM   741  N  N   . THR   A 1 93  ? 22.620 -36.686 -40.423 1.00 84.68  ?  108 THR   A N   1 
ATOM   742  C  CA  . THR   A 1 93  ? 23.487 -35.678 -41.028 1.00 86.56  ?  108 THR   A CA  1 
ATOM   743  C  C   . THR   A 1 93  ? 24.145 -34.803 -39.967 1.00 75.91  ?  108 THR   A C   1 
ATOM   744  O  O   . THR   A 1 93  ? 25.331 -34.474 -40.072 1.00 71.45  ?  108 THR   A O   1 
ATOM   745  C  CB  . THR   A 1 93  ? 22.691 -34.815 -42.011 1.00 85.89  ?  108 THR   A CB  1 
ATOM   746  O  OG1 . THR   A 1 93  ? 22.195 -35.633 -43.078 1.00 85.13  ?  108 THR   A OG1 1 
ATOM   747  C  CG2 . THR   A 1 93  ? 23.572 -33.701 -42.585 1.00 82.12  ?  108 THR   A CG2 1 
ATOM   748  N  N   . LEU   A 1 94  ? 23.387 -34.410 -38.940 1.00 73.28  ?  109 LEU   A N   1 
ATOM   749  C  CA  . LEU   A 1 94  ? 23.952 -33.568 -37.891 1.00 75.28  ?  109 LEU   A CA  1 
ATOM   750  C  C   . LEU   A 1 94  ? 25.031 -34.315 -37.112 1.00 76.66  ?  109 LEU   A C   1 
ATOM   751  O  O   . LEU   A 1 94  ? 26.067 -33.736 -36.761 1.00 78.67  ?  109 LEU   A O   1 
ATOM   752  C  CB  . LEU   A 1 94  ? 22.838 -33.070 -36.968 1.00 70.96  ?  109 LEU   A CB  1 
ATOM   753  C  CG  . LEU   A 1 94  ? 21.732 -32.269 -37.674 1.00 72.96  ?  109 LEU   A CG  1 
ATOM   754  C  CD1 . LEU   A 1 94  ? 20.659 -31.817 -36.703 1.00 80.62  ?  109 LEU   A CD1 1 
ATOM   755  C  CD2 . LEU   A 1 94  ? 22.285 -31.071 -38.426 1.00 70.23  ?  109 LEU   A CD2 1 
ATOM   756  N  N   . SER   A 1 95  ? 24.823 -35.612 -36.870 1.00 78.99  ?  110 SER   A N   1 
ATOM   757  C  CA  . SER   A 1 95  ? 25.821 -36.417 -36.171 1.00 75.81  ?  110 SER   A CA  1 
ATOM   758  C  C   . SER   A 1 95  ? 27.089 -36.570 -36.998 1.00 71.02  ?  110 SER   A C   1 
ATOM   759  O  O   . SER   A 1 95  ? 28.202 -36.434 -36.477 1.00 70.22  ?  110 SER   A O   1 
ATOM   760  C  CB  . SER   A 1 95  ? 25.235 -37.785 -35.837 1.00 78.03  ?  110 SER   A CB  1 
ATOM   761  O  OG  . SER   A 1 95  ? 24.023 -37.628 -35.136 1.00 91.02  ?  110 SER   A OG  1 
ATOM   762  N  N   . GLN   A 1 96  ? 26.939 -36.881 -38.290 1.00 77.35  ?  111 GLN   A N   1 
ATOM   763  C  CA  . GLN   A 1 96  ? 28.101 -36.972 -39.165 1.00 76.42  ?  111 GLN   A CA  1 
ATOM   764  C  C   . GLN   A 1 96  ? 28.826 -35.648 -39.250 1.00 70.06  ?  111 GLN   A C   1 
ATOM   765  O  O   . GLN   A 1 96  ? 30.059 -35.621 -39.347 1.00 74.30  ?  111 GLN   A O   1 
ATOM   766  C  CB  . GLN   A 1 96  ? 27.684 -37.415 -40.560 1.00 69.76  ?  111 GLN   A CB  1 
ATOM   767  C  CG  . GLN   A 1 96  ? 27.260 -38.852 -40.639 1.00 73.91  ?  111 GLN   A CG  1 
ATOM   768  C  CD  . GLN   A 1 96  ? 26.364 -39.087 -41.820 1.00 82.77  ?  111 GLN   A CD  1 
ATOM   769  O  OE1 . GLN   A 1 96  ? 26.480 -38.406 -42.839 1.00 92.78  ?  111 GLN   A OE1 1 
ATOM   770  N  NE2 . GLN   A 1 96  ? 25.445 -40.034 -41.688 1.00 89.95  ?  111 GLN   A NE2 1 
ATOM   771  N  N   . PHE   A 1 97  ? 28.079 -34.542 -39.219 1.00 72.17  ?  112 PHE   A N   1 
ATOM   772  C  CA  . PHE   A 1 97  ? 28.706 -33.227 -39.249 1.00 67.53  ?  112 PHE   A CA  1 
ATOM   773  C  C   . PHE   A 1 97  ? 29.638 -33.044 -38.057 1.00 69.16  ?  112 PHE   A C   1 
ATOM   774  O  O   . PHE   A 1 97  ? 30.809 -32.678 -38.222 1.00 64.76  ?  112 PHE   A O   1 
ATOM   775  C  CB  . PHE   A 1 97  ? 27.643 -32.128 -39.283 1.00 61.32  ?  112 PHE   A CB  1 
ATOM   776  C  CG  . PHE   A 1 97  ? 28.212 -30.766 -39.514 1.00 63.62  ?  112 PHE   A CG  1 
ATOM   777  C  CD1 . PHE   A 1 97  ? 28.806 -30.455 -40.726 1.00 67.07  ?  112 PHE   A CD1 1 
ATOM   778  C  CD2 . PHE   A 1 97  ? 28.182 -29.801 -38.517 1.00 59.26  ?  112 PHE   A CD2 1 
ATOM   779  C  CE1 . PHE   A 1 97  ? 29.357 -29.206 -40.948 1.00 66.72  ?  112 PHE   A CE1 1 
ATOM   780  C  CE2 . PHE   A 1 97  ? 28.717 -28.546 -38.735 1.00 61.00  ?  112 PHE   A CE2 1 
ATOM   781  C  CZ  . PHE   A 1 97  ? 29.312 -28.251 -39.962 1.00 57.21  ?  112 PHE   A CZ  1 
ATOM   782  N  N   . THR   A 1 98  ? 29.139 -33.316 -36.846 1.00 67.78  ?  113 THR   A N   1 
ATOM   783  C  CA  . THR   A 1 98  ? 29.960 -33.178 -35.643 1.00 65.94  ?  113 THR   A CA  1 
ATOM   784  C  C   . THR   A 1 98  ? 31.192 -34.078 -35.701 1.00 63.76  ?  113 THR   A C   1 
ATOM   785  O  O   . THR   A 1 98  ? 32.310 -33.638 -35.399 1.00 67.19  ?  113 THR   A O   1 
ATOM   786  C  CB  . THR   A 1 98  ? 29.116 -33.495 -34.403 1.00 73.57  ?  113 THR   A CB  1 
ATOM   787  O  OG1 . THR   A 1 98  ? 27.996 -32.603 -34.348 1.00 73.01  ?  113 THR   A OG1 1 
ATOM   788  C  CG2 . THR   A 1 98  ? 29.938 -33.360 -33.125 1.00 70.39  ?  113 THR   A CG2 1 
ATOM   789  N  N   . ASP   A 1 99  ? 31.005 -35.349 -36.080 1.00 63.64  ?  114 ASP   A N   1 
ATOM   790  C  CA  . ASP   A 1 99  ? 32.138 -36.257 -36.255 1.00 71.03  ?  114 ASP   A CA  1 
ATOM   791  C  C   . ASP   A 1 99  ? 33.172 -35.668 -37.212 1.00 72.52  ?  114 ASP   A C   1 
ATOM   792  O  O   . ASP   A 1 99  ? 34.380 -35.720 -36.946 1.00 67.47  ?  114 ASP   A O   1 
ATOM   793  C  CB  . ASP   A 1 99  ? 31.662 -37.623 -36.775 1.00 67.06  ?  114 ASP   A CB  1 
ATOM   794  C  CG  . ASP   A 1 99  ? 30.775 -38.372 -35.777 1.00 83.21  ?  114 ASP   A CG  1 
ATOM   795  O  OD1 . ASP   A 1 99  ? 30.672 -37.926 -34.613 1.00 86.44  ?  114 ASP   A OD1 1 
ATOM   796  O  OD2 . ASP   A 1 99  ? 30.177 -39.412 -36.164 1.00 85.79  ?  114 ASP   A OD2 1 
ATOM   797  N  N   . ALA   A 1 100 ? 32.709 -35.093 -38.329 1.00 67.24  ?  115 ALA   A N   1 
ATOM   798  C  CA  . ALA   A 1 100 ? 33.622 -34.519 -39.312 1.00 63.55  ?  115 ALA   A CA  1 
ATOM   799  C  C   . ALA   A 1 100 ? 34.359 -33.304 -38.759 1.00 63.12  ?  115 ALA   A C   1 
ATOM   800  O  O   . ALA   A 1 100 ? 35.538 -33.098 -39.069 1.00 59.20  ?  115 ALA   A O   1 
ATOM   801  C  CB  . ALA   A 1 100 ? 32.860 -34.143 -40.581 1.00 60.57  ?  115 ALA   A CB  1 
ATOM   802  N  N   . LEU   A 1 101 ? 33.685 -32.468 -37.962 1.00 61.60  ?  116 LEU   A N   1 
ATOM   803  C  CA  . LEU   A 1 101 ? 34.393 -31.339 -37.369 1.00 58.44  ?  116 LEU   A CA  1 
ATOM   804  C  C   . LEU   A 1 101 ? 35.447 -31.809 -36.376 1.00 61.36  ?  116 LEU   A C   1 
ATOM   805  O  O   . LEU   A 1 101 ? 36.496 -31.168 -36.237 1.00 60.68  ?  116 LEU   A O   1 
ATOM   806  C  CB  . LEU   A 1 101 ? 33.413 -30.382 -36.685 1.00 57.26  ?  116 LEU   A CB  1 
ATOM   807  C  CG  . LEU   A 1 101 ? 32.401 -29.639 -37.562 1.00 60.00  ?  116 LEU   A CG  1 
ATOM   808  C  CD1 . LEU   A 1 101 ? 31.805 -28.485 -36.786 1.00 57.37  ?  116 LEU   A CD1 1 
ATOM   809  C  CD2 . LEU   A 1 101 ? 33.027 -29.140 -38.856 1.00 54.70  ?  116 LEU   A CD2 1 
ATOM   810  N  N   . VAL   A 1 102 ? 35.194 -32.918 -35.675 1.00 61.65  ?  117 VAL   A N   1 
ATOM   811  C  CA  . VAL   A 1 102 ? 36.189 -33.418 -34.728 1.00 67.38  ?  117 VAL   A CA  1 
ATOM   812  C  C   . VAL   A 1 102 ? 37.412 -33.934 -35.472 1.00 62.08  ?  117 VAL   A C   1 
ATOM   813  O  O   . VAL   A 1 102 ? 38.555 -33.681 -35.071 1.00 64.89  ?  117 VAL   A O   1 
ATOM   814  C  CB  . VAL   A 1 102 ? 35.582 -34.501 -33.815 1.00 72.43  ?  117 VAL   A CB  1 
ATOM   815  C  CG1 . VAL   A 1 102 ? 36.672 -35.130 -32.946 1.00 72.94  ?  117 VAL   A CG1 1 
ATOM   816  C  CG2 . VAL   A 1 102 ? 34.487 -33.908 -32.934 1.00 67.93  ?  117 VAL   A CG2 1 
ATOM   817  N  N   . THR   A 1 103 ? 37.191 -34.665 -36.566 1.00 60.89  ?  118 THR   A N   1 
ATOM   818  C  CA  . THR   A 1 103 ? 38.300 -35.107 -37.402 1.00 61.24  ?  118 THR   A CA  1 
ATOM   819  C  C   . THR   A 1 103 ? 39.111 -33.922 -37.921 1.00 60.19  ?  118 THR   A C   1 
ATOM   820  O  O   . THR   A 1 103 ? 40.347 -33.960 -37.927 1.00 61.58  ?  118 THR   A O   1 
ATOM   821  C  CB  . THR   A 1 103 ? 37.761 -35.945 -38.555 1.00 66.54  ?  118 THR   A CB  1 
ATOM   822  O  OG1 . THR   A 1 103 ? 37.146 -37.125 -38.026 1.00 67.45  ?  118 THR   A OG1 1 
ATOM   823  C  CG2 . THR   A 1 103 ? 38.880 -36.332 -39.515 1.00 66.46  ?  118 THR   A CG2 1 
ATOM   824  N  N   . ILE   A 1 104 ? 38.435 -32.852 -38.340 1.00 62.55  ?  119 ILE   A N   1 
ATOM   825  C  CA  . ILE   A 1 104 ? 39.141 -31.690 -38.871 1.00 58.57  ?  119 ILE   A CA  1 
ATOM   826  C  C   . ILE   A 1 104 ? 39.986 -31.037 -37.784 1.00 57.98  ?  119 ILE   A C   1 
ATOM   827  O  O   . ILE   A 1 104 ? 41.149 -30.673 -38.012 1.00 51.95  ?  119 ILE   A O   1 
ATOM   828  C  CB  . ILE   A 1 104 ? 38.144 -30.695 -39.489 1.00 59.07  ?  119 ILE   A CB  1 
ATOM   829  C  CG1 . ILE   A 1 104 ? 37.608 -31.250 -40.807 1.00 57.36  ?  119 ILE   A CG1 1 
ATOM   830  C  CG2 . ILE   A 1 104 ? 38.799 -29.331 -39.685 1.00 52.43  ?  119 ILE   A CG2 1 
ATOM   831  C  CD1 . ILE   A 1 104 ? 36.453 -30.458 -41.368 1.00 57.08  ?  119 ILE   A CD1 1 
ATOM   832  N  N   . ARG   A 1 105 ? 39.422 -30.883 -36.582 1.00 52.41  ?  120 ARG   A N   1 
ATOM   833  C  CA  . ARG   A 1 105 ? 40.184 -30.242 -35.514 1.00 58.49  ?  120 ARG   A CA  1 
ATOM   834  C  C   . ARG   A 1 105 ? 41.425 -31.058 -35.180 1.00 57.51  ?  120 ARG   A C   1 
ATOM   835  O  O   . ARG   A 1 105 ? 42.512 -30.501 -34.988 1.00 57.48  ?  120 ARG   A O   1 
ATOM   836  C  CB  . ARG   A 1 105 ? 39.314 -30.047 -34.273 1.00 57.90  ?  120 ARG   A CB  1 
ATOM   837  C  CG  . ARG   A 1 105 ? 40.019 -29.318 -33.117 1.00 60.34  ?  120 ARG   A CG  1 
ATOM   838  C  CD  . ARG   A 1 105 ? 39.108 -29.223 -31.892 1.00 57.53  ?  120 ARG   A CD  1 
ATOM   839  N  NE  . ARG   A 1 105 ? 38.749 -30.540 -31.375 1.00 68.11  ?  120 ARG   A NE  1 
ATOM   840  C  CZ  . ARG   A 1 105 ? 37.558 -30.851 -30.875 1.00 71.85  ?  120 ARG   A CZ  1 
ATOM   841  N  NH1 . ARG   A 1 105 ? 36.583 -29.957 -30.797 1.00 65.82  ?  120 ARG   A NH1 1 
ATOM   842  N  NH2 . ARG   A 1 105 ? 37.339 -32.092 -30.450 1.00 67.51  ?  120 ARG   A NH2 1 
ATOM   843  N  N   . ASN   A 1 106 ? 41.288 -32.386 -35.145 1.00 58.47  ?  121 ASN   A N   1 
ATOM   844  C  CA  . ASN   A 1 106 ? 42.439 -33.235 -34.863 1.00 62.96  ?  121 ASN   A CA  1 
ATOM   845  C  C   . ASN   A 1 106 ? 43.449 -33.178 -35.998 1.00 62.68  ?  121 ASN   A C   1 
ATOM   846  O  O   . ASN   A 1 106 ? 44.660 -33.156 -35.756 1.00 63.13  ?  121 ASN   A O   1 
ATOM   847  C  CB  . ASN   A 1 106 ? 41.988 -34.676 -34.615 1.00 63.34  ?  121 ASN   A CB  1 
ATOM   848  C  CG  . ASN   A 1 106 ? 41.091 -34.807 -33.398 1.00 66.08  ?  121 ASN   A CG  1 
ATOM   849  O  OD1 . ASN   A 1 106 ? 41.078 -33.939 -32.520 1.00 70.31  ?  121 ASN   A OD1 1 
ATOM   850  N  ND2 . ASN   A 1 106 ? 40.333 -35.897 -33.341 1.00 76.25  ?  121 ASN   A ND2 1 
ATOM   851  N  N   . ARG   A 1 107 ? 42.966 -33.138 -37.243 1.00 56.56  ?  122 ARG   A N   1 
ATOM   852  C  CA  . ARG   A 1 107 ? 43.861 -33.057 -38.393 1.00 58.18  ?  122 ARG   A CA  1 
ATOM   853  C  C   . ARG   A 1 107 ? 44.783 -31.840 -38.318 1.00 62.39  ?  122 ARG   A C   1 
ATOM   854  O  O   . ARG   A 1 107 ? 45.931 -31.903 -38.777 1.00 55.71  ?  122 ARG   A O   1 
ATOM   855  C  CB  . ARG   A 1 107 ? 43.045 -33.019 -39.679 1.00 54.25  ?  122 ARG   A CB  1 
ATOM   856  C  CG  . ARG   A 1 107 ? 43.878 -32.937 -40.934 1.00 53.22  ?  122 ARG   A CG  1 
ATOM   857  C  CD  . ARG   A 1 107 ? 43.014 -32.864 -42.177 1.00 55.94  ?  122 ARG   A CD  1 
ATOM   858  N  NE  . ARG   A 1 107 ? 42.241 -34.083 -42.395 1.00 64.20  ?  122 ARG   A NE  1 
ATOM   859  C  CZ  . ARG   A 1 107 ? 40.932 -34.117 -42.610 1.00 62.14  ?  122 ARG   A CZ  1 
ATOM   860  N  NH1 . ARG   A 1 107 ? 40.212 -33.009 -42.654 1.00 57.32  ?  122 ARG   A NH1 1 
ATOM   861  N  NH2 . ARG   A 1 107 ? 40.334 -35.292 -42.797 1.00 59.58  ?  122 ARG   A NH2 1 
ATOM   862  N  N   . HIS   A 1 108 ? 44.316 -30.739 -37.731 1.00 50.56  ?  123 HIS   A N   1 
ATOM   863  C  CA  . HIS   A 1 108 ? 45.059 -29.493 -37.718 1.00 51.31  ?  123 HIS   A CA  1 
ATOM   864  C  C   . HIS   A 1 108 ? 45.852 -29.281 -36.438 1.00 54.11  ?  123 HIS   A C   1 
ATOM   865  O  O   . HIS   A 1 108 ? 46.389 -28.184 -36.237 1.00 50.10  ?  123 HIS   A O   1 
ATOM   866  C  CB  . HIS   A 1 108 ? 44.114 -28.310 -37.896 1.00 52.86  ?  123 HIS   A CB  1 
ATOM   867  C  CG  . HIS   A 1 108 ? 43.444 -28.268 -39.225 1.00 51.39  ?  123 HIS   A CG  1 
ATOM   868  N  ND1 . HIS   A 1 108 ? 42.658 -27.209 -39.619 1.00 57.80  ?  123 HIS   A ND1 1 
ATOM   869  C  CD2 . HIS   A 1 108 ? 43.439 -29.144 -40.254 1.00 55.03  ?  123 HIS   A CD2 1 
ATOM   870  C  CE1 . HIS   A 1 108 ? 42.197 -27.435 -40.836 1.00 54.84  ?  123 HIS   A CE1 1 
ATOM   871  N  NE2 . HIS   A 1 108 ? 42.651 -28.604 -41.242 1.00 50.49  ?  123 HIS   A NE2 1 
ATOM   872  N  N   . ASN   A 1 109 ? 45.915 -30.280 -35.555 1.00 56.07  ?  124 ASN   A N   1 
ATOM   873  C  CA  . ASN   A 1 109 ? 46.472 -30.047 -34.222 1.00 60.98  ?  124 ASN   A CA  1 
ATOM   874  C  C   . ASN   A 1 109 ? 47.929 -29.605 -34.260 1.00 52.78  ?  124 ASN   A C   1 
ATOM   875  O  O   . ASN   A 1 109 ? 48.378 -28.926 -33.331 1.00 55.45  ?  124 ASN   A O   1 
ATOM   876  C  CB  . ASN   A 1 109 ? 46.348 -31.304 -33.346 1.00 68.40  ?  124 ASN   A CB  1 
ATOM   877  C  CG  . ASN   A 1 109 ? 45.092 -31.297 -32.482 1.00 73.18  ?  124 ASN   A CG  1 
ATOM   878  O  OD1 . ASN   A 1 109 ? 44.496 -30.247 -32.243 1.00 72.09  ?  124 ASN   A OD1 1 
ATOM   879  N  ND2 . ASN   A 1 109 ? 44.688 -32.477 -32.007 1.00 79.38  ?  124 ASN   A ND2 1 
ATOM   880  N  N   . ASP   A 1 110 ? 48.672 -29.960 -35.310 1.00 51.15  ?  125 ASP   A N   1 
ATOM   881  C  CA  . ASP   A 1 110 ? 50.100 -29.686 -35.388 1.00 57.57  ?  125 ASP   A CA  1 
ATOM   882  C  C   . ASP   A 1 110 ? 50.437 -28.518 -36.309 1.00 57.81  ?  125 ASP   A C   1 
ATOM   883  O  O   . ASP   A 1 110 ? 51.587 -28.396 -36.737 1.00 52.72  ?  125 ASP   A O   1 
ATOM   884  C  CB  . ASP   A 1 110 ? 50.842 -30.944 -35.833 1.00 54.04  ?  125 ASP   A CB  1 
ATOM   885  C  CG  . ASP   A 1 110 ? 50.807 -32.026 -34.779 1.00 57.54  ?  125 ASP   A CG  1 
ATOM   886  O  OD1 . ASP   A 1 110 ? 50.966 -31.685 -33.587 1.00 72.23  ?  125 ASP   A OD1 1 
ATOM   887  O  OD2 . ASP   A 1 110 ? 50.603 -33.203 -35.132 1.00 74.95  ?  125 ASP   A OD2 1 
ATOM   888  N  N   . VAL   A 1 111 ? 49.466 -27.643 -36.598 1.00 52.26  ?  126 VAL   A N   1 
ATOM   889  C  CA  . VAL   A 1 111 ? 49.668 -26.599 -37.604 1.00 50.27  ?  126 VAL   A CA  1 
ATOM   890  C  C   . VAL   A 1 111 ? 50.672 -25.558 -37.120 1.00 54.91  ?  126 VAL   A C   1 
ATOM   891  O  O   . VAL   A 1 111 ? 51.472 -25.034 -37.906 1.00 44.24  ?  126 VAL   A O   1 
ATOM   892  C  CB  . VAL   A 1 111 ? 48.318 -25.960 -37.989 1.00 54.64  ?  126 VAL   A CB  1 
ATOM   893  C  CG1 . VAL   A 1 111 ? 48.531 -24.592 -38.601 1.00 54.94  ?  126 VAL   A CG1 1 
ATOM   894  C  CG2 . VAL   A 1 111 ? 47.544 -26.856 -38.977 1.00 52.93  ?  126 VAL   A CG2 1 
ATOM   895  N  N   . VAL   A 1 112 ? 50.660 -25.243 -35.831 1.00 51.00  ?  127 VAL   A N   1 
ATOM   896  C  CA  . VAL   A 1 112 ? 51.563 -24.206 -35.338 1.00 43.94  ?  127 VAL   A CA  1 
ATOM   897  C  C   . VAL   A 1 112 ? 53.025 -24.629 -35.518 1.00 53.59  ?  127 VAL   A C   1 
ATOM   898  O  O   . VAL   A 1 112 ? 53.770 -23.897 -36.191 1.00 46.34  ?  127 VAL   A O   1 
ATOM   899  C  CB  . VAL   A 1 112 ? 51.246 -23.820 -33.880 1.00 55.23  ?  127 VAL   A CB  1 
ATOM   900  C  CG1 . VAL   A 1 112 ? 52.284 -22.885 -33.370 1.00 43.88  ?  127 VAL   A CG1 1 
ATOM   901  C  CG2 . VAL   A 1 112 ? 49.879 -23.147 -33.802 1.00 50.59  ?  127 VAL   A CG2 1 
ATOM   902  N  N   . PRO   A 1 113 ? 53.489 -25.770 -34.972 1.00 46.00  ?  128 PRO   A N   1 
ATOM   903  C  CA  . PRO   A 1 113 ? 54.901 -26.145 -35.181 1.00 49.05  ?  128 PRO   A CA  1 
ATOM   904  C  C   . PRO   A 1 113 ? 55.234 -26.484 -36.622 1.00 54.54  ?  128 PRO   A C   1 
ATOM   905  O  O   . PRO   A 1 113 ? 56.399 -26.390 -37.025 1.00 51.09  ?  128 PRO   A O   1 
ATOM   906  C  CB  . PRO   A 1 113 ? 55.099 -27.380 -34.291 1.00 48.72  ?  128 PRO   A CB  1 
ATOM   907  C  CG  . PRO   A 1 113 ? 53.789 -27.707 -33.710 1.00 51.99  ?  128 PRO   A CG  1 
ATOM   908  C  CD  . PRO   A 1 113 ? 52.735 -26.839 -34.295 1.00 55.71  ?  128 PRO   A CD  1 
ATOM   909  N  N   . THR   A 1 114 ? 54.259 -26.920 -37.407 1.00 49.93  ?  129 THR   A N   1 
ATOM   910  C  CA  . THR   A 1 114 ? 54.546 -27.173 -38.807 1.00 48.80  ?  129 THR   A CA  1 
ATOM   911  C  C   . THR   A 1 114 ? 54.919 -25.878 -39.524 1.00 51.74  ?  129 THR   A C   1 
ATOM   912  O  O   . THR   A 1 114 ? 55.911 -25.838 -40.260 1.00 42.98  ?  129 THR   A O   1 
ATOM   913  C  CB  . THR   A 1 114 ? 53.360 -27.867 -39.464 1.00 45.15  ?  129 THR   A CB  1 
ATOM   914  O  OG1 . THR   A 1 114 ? 53.073 -29.072 -38.742 1.00 47.70  ?  129 THR   A OG1 1 
ATOM   915  C  CG2 . THR   A 1 114 ? 53.719 -28.257 -40.875 1.00 42.35  ?  129 THR   A CG2 1 
ATOM   916  N  N   . MET   A 1 115 ? 54.179 -24.792 -39.295 1.00 49.32  ?  130 MET   A N   1 
ATOM   917  C  CA  . MET   A 1 115 ? 54.571 -23.545 -39.936 1.00 49.20  ?  130 MET   A CA  1 
ATOM   918  C  C   . MET   A 1 115 ? 55.892 -23.038 -39.371 1.00 48.64  ?  130 MET   A C   1 
ATOM   919  O  O   . MET   A 1 115 ? 56.655 -22.370 -40.079 1.00 48.36  ?  130 MET   A O   1 
ATOM   920  C  CB  . MET   A 1 115 ? 53.461 -22.505 -39.789 1.00 44.60  ?  130 MET   A CB  1 
ATOM   921  C  CG  . MET   A 1 115 ? 52.299 -22.769 -40.690 1.00 45.04  ?  130 MET   A CG  1 
ATOM   922  S  SD  . MET   A 1 115 ? 52.628 -22.245 -42.384 1.00 59.94  ?  130 MET   A SD  1 
ATOM   923  C  CE  . MET   A 1 115 ? 51.098 -22.704 -43.148 1.00 69.75  ?  130 MET   A CE  1 
ATOM   924  N  N   . ALA   A 1 116 ? 56.189 -23.368 -38.114 1.00 44.96  ?  131 ALA   A N   1 
ATOM   925  C  CA  . ALA   A 1 116 ? 57.486 -23.019 -37.538 1.00 45.57  ?  131 ALA   A CA  1 
ATOM   926  C  C   . ALA   A 1 116 ? 58.640 -23.641 -38.322 1.00 45.52  ?  131 ALA   A C   1 
ATOM   927  O  O   . ALA   A 1 116 ? 59.676 -22.996 -38.510 1.00 46.71  ?  131 ALA   A O   1 
ATOM   928  C  CB  . ALA   A 1 116 ? 57.559 -23.455 -36.076 1.00 42.13  ?  131 ALA   A CB  1 
ATOM   929  N  N   . GLN   A 1 117 ? 58.503 -24.911 -38.729 1.00 46.27  ?  132 GLN   A N   1 
ATOM   930  C  CA  . GLN   A 1 117 ? 59.536 -25.551 -39.543 1.00 44.76  ?  132 GLN   A CA  1 
ATOM   931  C  C   . GLN   A 1 117 ? 59.713 -24.848 -40.880 1.00 45.63  ?  132 GLN   A C   1 
ATOM   932  O  O   . GLN   A 1 117 ? 60.815 -24.849 -41.439 1.00 48.67  ?  132 GLN   A O   1 
ATOM   933  C  CB  . GLN   A 1 117 ? 59.214 -27.029 -39.776 1.00 48.94  ?  132 GLN   A CB  1 
ATOM   934  C  CG  . GLN   A 1 117 ? 59.503 -27.902 -38.567 1.00 47.60  ?  132 GLN   A CG  1 
ATOM   935  C  CD  . GLN   A 1 117 ? 60.960 -27.867 -38.173 1.00 58.69  ?  132 GLN   A CD  1 
ATOM   936  O  OE1 . GLN   A 1 117 ? 61.845 -28.035 -39.020 1.00 55.27  ?  132 GLN   A OE1 1 
ATOM   937  N  NE2 . GLN   A 1 117 ? 61.225 -27.657 -36.883 1.00 50.46  ?  132 GLN   A NE2 1 
ATOM   938  N  N   . GLY   A 1 118 ? 58.645 -24.257 -41.416 1.00 40.83  ?  133 GLY   A N   1 
ATOM   939  C  CA  . GLY   A 1 118 ? 58.791 -23.465 -42.620 1.00 43.49  ?  133 GLY   A CA  1 
ATOM   940  C  C   . GLY   A 1 118 ? 59.545 -22.182 -42.353 1.00 53.63  ?  133 GLY   A C   1 
ATOM   941  O  O   . GLY   A 1 118 ? 60.356 -21.750 -43.174 1.00 42.94  ?  133 GLY   A O   1 
ATOM   942  N  N   . VAL   A 1 119 ? 59.303 -21.561 -41.190 1.00 41.95  ?  134 VAL   A N   1 
ATOM   943  C  CA  . VAL   A 1 119 ? 60.056 -20.364 -40.819 1.00 40.21  ?  134 VAL   A CA  1 
ATOM   944  C  C   . VAL   A 1 119 ? 61.526 -20.705 -40.670 1.00 42.30  ?  134 VAL   A C   1 
ATOM   945  O  O   . VAL   A 1 119 ? 62.408 -19.979 -41.147 1.00 41.57  ?  134 VAL   A O   1 
ATOM   946  C  CB  . VAL   A 1 119 ? 59.499 -19.758 -39.518 1.00 45.32  ?  134 VAL   A CB  1 
ATOM   947  C  CG1 . VAL   A 1 119 ? 60.425 -18.663 -39.017 1.00 37.63  ?  134 VAL   A CG1 1 
ATOM   948  C  CG2 . VAL   A 1 119 ? 58.092 -19.231 -39.757 1.00 41.32  ?  134 VAL   A CG2 1 
ATOM   949  N  N   . LEU   A 1 120 ? 61.802 -21.824 -39.998 1.00 38.69  ?  135 LEU   A N   1 
ATOM   950  C  CA  . LEU   A 1 120 ? 63.168 -22.255 -39.742 1.00 40.83  ?  135 LEU   A CA  1 
ATOM   951  C  C   . LEU   A 1 120 ? 63.909 -22.549 -41.045 1.00 44.77  ?  135 LEU   A C   1 
ATOM   952  O  O   . LEU   A 1 120 ? 65.082 -22.186 -41.203 1.00 44.06  ?  135 LEU   A O   1 
ATOM   953  C  CB  . LEU   A 1 120 ? 63.136 -23.501 -38.859 1.00 43.05  ?  135 LEU   A CB  1 
ATOM   954  C  CG  . LEU   A 1 120 ? 64.460 -24.083 -38.390 1.00 50.19  ?  135 LEU   A CG  1 
ATOM   955  C  CD1 . LEU   A 1 120 ? 65.130 -23.114 -37.409 1.00 49.14  ?  135 LEU   A CD1 1 
ATOM   956  C  CD2 . LEU   A 1 120 ? 64.210 -25.454 -37.746 1.00 52.37  ?  135 LEU   A CD2 1 
ATOM   957  N  N   . GLU   A 1 121 ? 63.255 -23.250 -41.974 1.00 41.81  ?  136 GLU   A N   1 
ATOM   958  C  CA  . GLU   A 1 121 ? 63.914 -23.548 -43.242 1.00 43.19  ?  136 GLU   A CA  1 
ATOM   959  C  C   . GLU   A 1 121 ? 64.231 -22.259 -43.987 1.00 43.00  ?  136 GLU   A C   1 
ATOM   960  O  O   . GLU   A 1 121 ? 65.319 -22.113 -44.557 1.00 49.55  ?  136 GLU   A O   1 
ATOM   961  C  CB  . GLU   A 1 121 ? 63.052 -24.465 -44.119 1.00 41.45  ?  136 GLU   A CB  1 
ATOM   962  C  CG  . GLU   A 1 121 ? 63.549 -24.489 -45.613 1.00 51.76  ?  136 GLU   A CG  1 
ATOM   963  C  CD  . GLU   A 1 121 ? 62.784 -25.448 -46.528 1.00 52.72  ?  136 GLU   A CD  1 
ATOM   964  O  OE1 . GLU   A 1 121 ? 61.706 -25.942 -46.134 1.00 56.55  ?  136 GLU   A OE1 1 
ATOM   965  O  OE2 . GLU   A 1 121 ? 63.271 -25.715 -47.655 1.00 54.76  ?  136 GLU   A OE2 1 
ATOM   966  N  N   . TYR   A 1 122 ? 63.306 -21.300 -43.963 1.00 44.94  ?  137 TYR   A N   1 
ATOM   967  C  CA  . TYR   A 1 122 ? 63.525 -20.048 -44.682 1.00 47.95  ?  137 TYR   A CA  1 
ATOM   968  C  C   . TYR   A 1 122 ? 64.684 -19.272 -44.078 1.00 51.89  ?  137 TYR   A C   1 
ATOM   969  O  O   . TYR   A 1 122 ? 65.528 -18.730 -44.804 1.00 45.90  ?  137 TYR   A O   1 
ATOM   970  C  CB  . TYR   A 1 122 ? 62.254 -19.194 -44.680 1.00 49.25  ?  137 TYR   A CB  1 
ATOM   971  C  CG  . TYR   A 1 122 ? 62.432 -17.911 -45.459 1.00 50.96  ?  137 TYR   A CG  1 
ATOM   972  C  CD1 . TYR   A 1 122 ? 62.931 -16.767 -44.848 1.00 51.83  ?  137 TYR   A CD1 1 
ATOM   973  C  CD2 . TYR   A 1 122 ? 62.136 -17.852 -46.819 1.00 54.53  ?  137 TYR   A CD2 1 
ATOM   974  C  CE1 . TYR   A 1 122 ? 63.116 -15.600 -45.562 1.00 56.01  ?  137 TYR   A CE1 1 
ATOM   975  C  CE2 . TYR   A 1 122 ? 62.317 -16.687 -47.542 1.00 50.65  ?  137 TYR   A CE2 1 
ATOM   976  C  CZ  . TYR   A 1 122 ? 62.808 -15.563 -46.908 1.00 57.34  ?  137 TYR   A CZ  1 
ATOM   977  O  OH  . TYR   A 1 122 ? 62.991 -14.392 -47.611 1.00 61.47  ?  137 TYR   A OH  1 
ATOM   978  N  N   . LYS   A 1 123 ? 64.730 -19.199 -42.739 1.00 47.49  ?  138 LYS   A N   1 
ATOM   979  C  CA  . LYS   A 1 123 ? 65.807 -18.503 -42.040 1.00 46.62  ?  138 LYS   A CA  1 
ATOM   980  C  C   . LYS   A 1 123 ? 67.168 -19.001 -42.468 1.00 45.96  ?  138 LYS   A C   1 
ATOM   981  O  O   . LYS   A 1 123 ? 68.117 -18.218 -42.613 1.00 53.65  ?  138 LYS   A O   1 
ATOM   982  C  CB  . LYS   A 1 123 ? 65.675 -18.696 -40.522 1.00 53.93  ?  138 LYS   A CB  1 
ATOM   983  C  CG  . LYS   A 1 123 ? 64.991 -17.590 -39.777 1.00 65.25  ?  138 LYS   A CG  1 
ATOM   984  C  CD  . LYS   A 1 123 ? 64.972 -17.884 -38.260 1.00 55.00  ?  138 LYS   A CD  1 
ATOM   985  C  CE  . LYS   A 1 123 ? 66.278 -17.526 -37.609 1.00 51.89  ?  138 LYS   A CE  1 
ATOM   986  N  NZ  . LYS   A 1 123 ? 66.089 -17.508 -36.130 1.00 57.06  ?  138 LYS   A NZ  1 
ATOM   987  N  N   . ASP   A 1 124 ? 67.308 -20.304 -42.635 1.00 46.55  ?  139 ASP   A N   1 
ATOM   988  C  CA  . ASP   A 1 124 ? 68.620 -20.836 -42.941 1.00 54.28  ?  139 ASP   A CA  1 
ATOM   989  C  C   . ASP   A 1 124 ? 68.863 -21.037 -44.434 1.00 48.23  ?  139 ASP   A C   1 
ATOM   990  O  O   . ASP   A 1 124 ? 70.016 -21.197 -44.831 1.00 52.50  ?  139 ASP   A O   1 
ATOM   991  C  CB  . ASP   A 1 124 ? 68.838 -22.136 -42.161 1.00 59.49  ?  139 ASP   A CB  1 
ATOM   992  C  CG  . ASP   A 1 124 ? 68.780 -21.912 -40.649 1.00 60.73  ?  139 ASP   A CG  1 
ATOM   993  O  OD1 . ASP   A 1 124 ? 69.266 -20.858 -40.178 1.00 56.10  ?  139 ASP   A OD1 1 
ATOM   994  O  OD2 . ASP   A 1 124 ? 68.223 -22.767 -39.936 1.00 56.26  ?  139 ASP   A OD2 1 
ATOM   995  N  N   . THR   A 1 125 ? 67.830 -20.993 -45.277 1.00 50.78  ?  140 THR   A N   1 
ATOM   996  C  CA  . THR   A 1 125 ? 68.063 -21.125 -46.711 1.00 51.05  ?  140 THR   A CA  1 
ATOM   997  C  C   . THR   A 1 125 ? 68.018 -19.799 -47.467 1.00 52.54  ?  140 THR   A C   1 
ATOM   998  O  O   . THR   A 1 125 ? 68.556 -19.730 -48.581 1.00 49.36  ?  140 THR   A O   1 
ATOM   999  C  CB  . THR   A 1 125 ? 67.049 -22.087 -47.346 1.00 49.09  ?  140 THR   A CB  1 
ATOM   1000 O  OG1 . THR   A 1 125 ? 65.724 -21.590 -47.130 1.00 55.80  ?  140 THR   A OG1 1 
ATOM   1001 C  CG2 . THR   A 1 125 ? 67.186 -23.484 -46.748 1.00 48.54  ?  140 THR   A CG2 1 
ATOM   1002 N  N   . TYR   A 1 126 ? 67.362 -18.771 -46.913 1.00 46.17  ?  141 TYR   A N   1 
ATOM   1003 C  CA  . TYR   A 1 126 ? 67.306 -17.438 -47.512 1.00 55.07  ?  141 TYR   A CA  1 
ATOM   1004 C  C   . TYR   A 1 126 ? 67.689 -16.299 -46.562 1.00 62.68  ?  141 TYR   A C   1 
ATOM   1005 O  O   . TYR   A 1 126 ? 68.067 -15.228 -47.049 1.00 53.91  ?  141 TYR   A O   1 
ATOM   1006 C  CB  . TYR   A 1 126 ? 65.909 -17.183 -48.123 1.00 45.73  ?  141 TYR   A CB  1 
ATOM   1007 C  CG  . TYR   A 1 126 ? 65.697 -18.106 -49.330 1.00 55.31  ?  141 TYR   A CG  1 
ATOM   1008 C  CD1 . TYR   A 1 126 ? 66.396 -17.902 -50.511 1.00 54.73  ?  141 TYR   A CD1 1 
ATOM   1009 C  CD2 . TYR   A 1 126 ? 64.846 -19.206 -49.268 1.00 51.34  ?  141 TYR   A CD2 1 
ATOM   1010 C  CE1 . TYR   A 1 126 ? 66.250 -18.765 -51.607 1.00 55.66  ?  141 TYR   A CE1 1 
ATOM   1011 C  CE2 . TYR   A 1 126 ? 64.688 -20.067 -50.350 1.00 50.84  ?  141 TYR   A CE2 1 
ATOM   1012 C  CZ  . TYR   A 1 126 ? 65.384 -19.838 -51.520 1.00 57.66  ?  141 TYR   A CZ  1 
ATOM   1013 O  OH  . TYR   A 1 126 ? 65.227 -20.700 -52.600 1.00 71.67  ?  141 TYR   A OH  1 
ATOM   1014 N  N   . GLY   A 1 127 ? 67.658 -16.495 -45.249 1.00 52.65  ?  142 GLY   A N   1 
ATOM   1015 C  CA  . GLY   A 1 127 ? 68.238 -15.553 -44.311 1.00 50.48  ?  142 GLY   A CA  1 
ATOM   1016 C  C   . GLY   A 1 127 ? 67.195 -14.910 -43.412 1.00 51.98  ?  142 GLY   A C   1 
ATOM   1017 O  O   . GLY   A 1 127 ? 65.990 -15.103 -43.561 1.00 56.30  ?  142 GLY   A O   1 
ATOM   1018 N  N   . ASP   A 1 128 ? 67.701 -14.125 -42.453 1.00 52.72  ?  143 ASP   A N   1 
ATOM   1019 C  CA  . ASP   A 1 128 ? 66.847 -13.557 -41.408 1.00 60.02  ?  143 ASP   A CA  1 
ATOM   1020 C  C   . ASP   A 1 128 ? 66.949 -12.035 -41.328 1.00 63.22  ?  143 ASP   A C   1 
ATOM   1021 O  O   . ASP   A 1 128 ? 67.162 -11.473 -40.249 1.00 60.96  ?  143 ASP   A O   1 
ATOM   1022 C  CB  . ASP   A 1 128 ? 67.169 -14.187 -40.040 1.00 57.35  ?  143 ASP   A CB  1 
ATOM   1023 C  CG  . ASP   A 1 128 ? 68.606 -13.911 -39.559 1.00 72.75  ?  143 ASP   A CG  1 
ATOM   1024 O  OD1 . ASP   A 1 128 ? 69.390 -13.226 -40.255 1.00 66.01  ?  143 ASP   A OD1 1 
ATOM   1025 O  OD2 . ASP   A 1 128 ? 68.951 -14.387 -38.454 1.00 80.46  ?  143 ASP   A OD2 1 
ATOM   1026 N  N   . ASP   A 1 129 ? 66.773 -11.366 -42.462 1.00 60.78  ?  144 ASP   A N   1 
ATOM   1027 C  CA  . ASP   A 1 129 ? 66.841 -9.915  -42.556 1.00 59.49  ?  144 ASP   A CA  1 
ATOM   1028 C  C   . ASP   A 1 129 ? 65.525 -9.285  -42.103 1.00 60.46  ?  144 ASP   A C   1 
ATOM   1029 O  O   . ASP   A 1 129 ? 64.504 -9.961  -41.981 1.00 59.43  ?  144 ASP   A O   1 
ATOM   1030 C  CB  . ASP   A 1 129 ? 67.144 -9.528  -43.997 1.00 55.26  ?  144 ASP   A CB  1 
ATOM   1031 C  CG  . ASP   A 1 129 ? 66.120 -10.078 -44.944 1.00 57.13  ?  144 ASP   A CG  1 
ATOM   1032 O  OD1 . ASP   A 1 129 ? 66.102 -11.311 -45.146 1.00 61.69  ?  144 ASP   A OD1 1 
ATOM   1033 O  OD2 . ASP   A 1 129 ? 65.291 -9.294  -45.440 1.00 64.81  ?  144 ASP   A OD2 1 
ATOM   1034 N  N   . PRO   A 1 130 ? 65.503 -7.968  -41.862 1.00 60.16  ?  145 PRO   A N   1 
ATOM   1035 C  CA  . PRO   A 1 130 ? 64.264 -7.355  -41.362 1.00 59.05  ?  145 PRO   A CA  1 
ATOM   1036 C  C   . PRO   A 1 130 ? 63.090 -7.449  -42.323 1.00 58.63  ?  145 PRO   A C   1 
ATOM   1037 O  O   . PRO   A 1 130 ? 61.953 -7.588  -41.860 1.00 57.44  ?  145 PRO   A O   1 
ATOM   1038 C  CB  . PRO   A 1 130 ? 64.677 -5.898  -41.107 1.00 58.01  ?  145 PRO   A CB  1 
ATOM   1039 C  CG  . PRO   A 1 130 ? 66.133 -5.964  -40.877 1.00 64.57  ?  145 PRO   A CG  1 
ATOM   1040 C  CD  . PRO   A 1 130 ? 66.620 -7.007  -41.838 1.00 61.92  ?  145 PRO   A CD  1 
ATOM   1041 N  N   . VAL   A 1 131 ? 63.316 -7.390  -43.642 1.00 61.96  ?  146 VAL   A N   1 
ATOM   1042 C  CA  . VAL   A 1 131 ? 62.193 -7.456  -44.580 1.00 56.98  ?  146 VAL   A CA  1 
ATOM   1043 C  C   . VAL   A 1 131 ? 61.536 -8.833  -44.535 1.00 56.19  ?  146 VAL   A C   1 
ATOM   1044 O  O   . VAL   A 1 131 ? 60.304 -8.950  -44.532 1.00 52.02  ?  146 VAL   A O   1 
ATOM   1045 C  CB  . VAL   A 1 131 ? 62.650 -7.086  -46.003 1.00 64.26  ?  146 VAL   A CB  1 
ATOM   1046 C  CG1 . VAL   A 1 131 ? 61.647 -7.574  -47.048 1.00 50.01  ?  146 VAL   A CG1 1 
ATOM   1047 C  CG2 . VAL   A 1 131 ? 62.823 -5.588  -46.113 1.00 64.26  ?  146 VAL   A CG2 1 
ATOM   1048 N  N   . SER   A 1 132 ? 62.349 -9.895  -44.502 1.00 56.97  ?  147 SER   A N   1 
ATOM   1049 C  CA  . SER   A 1 132 ? 61.823 -11.244 -44.304 1.00 59.15  ?  147 SER   A CA  1 
ATOM   1050 C  C   . SER   A 1 132 ? 61.065 -11.356 -42.983 1.00 53.03  ?  147 SER   A C   1 
ATOM   1051 O  O   . SER   A 1 132 ? 60.005 -11.993 -42.920 1.00 48.93  ?  147 SER   A O   1 
ATOM   1052 C  CB  . SER   A 1 132 ? 62.970 -12.257 -44.349 1.00 51.05  ?  147 SER   A CB  1 
ATOM   1053 O  OG  . SER   A 1 132 ? 63.547 -12.330 -45.646 1.00 63.91  ?  147 SER   A OG  1 
ATOM   1054 N  N   . ASN   A 1 133 ? 61.607 -10.758 -41.914 1.00 52.43  ?  148 ASN   A N   1 
ATOM   1055 C  CA  . ASN   A 1 133 ? 60.937 -10.770 -40.614 1.00 50.07  ?  148 ASN   A CA  1 
ATOM   1056 C  C   . ASN   A 1 133 ? 59.557 -10.121 -40.695 1.00 47.75  ?  148 ASN   A C   1 
ATOM   1057 O  O   . ASN   A 1 133 ? 58.571 -10.673 -40.190 1.00 42.48  ?  148 ASN   A O   1 
ATOM   1058 C  CB  . ASN   A 1 133 ? 61.803 -10.064 -39.563 1.00 50.25  ?  148 ASN   A CB  1 
ATOM   1059 C  CG  . ASN   A 1 133 ? 61.128 -10.007 -38.175 1.00 56.51  ?  148 ASN   A CG  1 
ATOM   1060 O  OD1 . ASN   A 1 133 ? 60.896 -11.033 -37.546 1.00 56.20  ?  148 ASN   A OD1 1 
ATOM   1061 N  ND2 . ASN   A 1 133 ? 60.821 -8.803  -37.706 1.00 52.94  ?  148 ASN   A ND2 1 
ATOM   1062 N  N   . GLN   A 1 134 ? 59.469 -8.948  -41.341 1.00 50.64  ?  149 GLN   A N   1 
ATOM   1063 C  CA  . GLN   A 1 134 ? 58.189 -8.249  -41.456 1.00 53.33  ?  149 GLN   A CA  1 
ATOM   1064 C  C   . GLN   A 1 134 ? 57.166 -9.088  -42.201 1.00 48.08  ?  149 GLN   A C   1 
ATOM   1065 O  O   . GLN   A 1 134 ? 55.997 -9.147  -41.808 1.00 46.85  ?  149 GLN   A O   1 
ATOM   1066 C  CB  . GLN   A 1 134 ? 58.366 -6.913  -42.177 1.00 55.63  ?  149 GLN   A CB  1 
ATOM   1067 C  CG  . GLN   A 1 134 ? 58.741 -5.753  -41.292 1.00 69.54  ?  149 GLN   A CG  1 
ATOM   1068 C  CD  . GLN   A 1 134 ? 59.398 -4.633  -42.067 1.00 86.50  ?  149 GLN   A CD  1 
ATOM   1069 O  OE1 . GLN   A 1 134 ? 60.407 -4.075  -41.632 1.00 95.44  ?  149 GLN   A OE1 1 
ATOM   1070 N  NE2 . GLN   A 1 134 ? 58.836 -4.300  -43.230 1.00 89.31  ?  149 GLN   A NE2 1 
ATOM   1071 N  N   . ASN   A 1 135 ? 57.586 -9.744  -43.287 1.00 49.48  ?  150 ASN   A N   1 
ATOM   1072 C  CA  . ASN   A 1 135 ? 56.634 -10.508 -44.083 1.00 43.45  ?  150 ASN   A CA  1 
ATOM   1073 C  C   . ASN   A 1 135 ? 56.163 -11.752 -43.354 1.00 40.20  ?  150 ASN   A C   1 
ATOM   1074 O  O   . ASN   A 1 135 ? 54.989 -12.117 -43.447 1.00 40.60  ?  150 ASN   A O   1 
ATOM   1075 C  CB  . ASN   A 1 135 ? 57.245 -10.886 -45.431 1.00 50.64  ?  150 ASN   A CB  1 
ATOM   1076 C  CG  . ASN   A 1 135 ? 56.989 -9.827  -46.484 1.00 63.00  ?  150 ASN   A CG  1 
ATOM   1077 O  OD1 . ASN   A 1 135 ? 55.885 -9.719  -47.016 1.00 65.23  ?  150 ASN   A OD1 1 
ATOM   1078 N  ND2 . ASN   A 1 135 ? 58.002 -9.027  -46.770 1.00 63.47  ?  150 ASN   A ND2 1 
ATOM   1079 N  N   . ILE   A 1 136 ? 57.071 -12.446 -42.667 1.00 43.46  ?  151 ILE   A N   1 
ATOM   1080 C  CA  . ILE   A 1 136 ? 56.667 -13.582 -41.842 1.00 41.23  ?  151 ILE   A CA  1 
ATOM   1081 C  C   . ILE   A 1 136 ? 55.717 -13.125 -40.738 1.00 40.47  ?  151 ILE   A C   1 
ATOM   1082 O  O   . ILE   A 1 136 ? 54.725 -13.801 -40.428 1.00 39.83  ?  151 ILE   A O   1 
ATOM   1083 C  CB  . ILE   A 1 136 ? 57.911 -14.279 -41.266 1.00 39.44  ?  151 ILE   A CB  1 
ATOM   1084 C  CG1 . ILE   A 1 136 ? 58.658 -14.992 -42.397 1.00 47.78  ?  151 ILE   A CG1 1 
ATOM   1085 C  CG2 . ILE   A 1 136 ? 57.526 -15.262 -40.159 1.00 34.70  ?  151 ILE   A CG2 1 
ATOM   1086 C  CD1 . ILE   A 1 136 ? 59.878 -15.717 -41.946 1.00 47.08  ?  151 ILE   A CD1 1 
ATOM   1087 N  N   . GLN   A 1 137 ? 55.993 -11.964 -40.138 1.00 39.81  ?  152 GLN   A N   1 
ATOM   1088 C  CA  . GLN   A 1 137 ? 55.142 -11.485 -39.050 1.00 39.08  ?  152 GLN   A CA  1 
ATOM   1089 C  C   . GLN   A 1 137 ? 53.742 -11.155 -39.563 1.00 43.52  ?  152 GLN   A C   1 
ATOM   1090 O  O   . GLN   A 1 137 ? 52.732 -11.554 -38.965 1.00 41.08  ?  152 GLN   A O   1 
ATOM   1091 C  CB  . GLN   A 1 137 ? 55.783 -10.268 -38.384 1.00 43.07  ?  152 GLN   A CB  1 
ATOM   1092 C  CG  . GLN   A 1 137 ? 55.174 -9.921  -37.006 1.00 42.45  ?  152 GLN   A CG  1 
ATOM   1093 C  CD  . GLN   A 1 137 ? 55.737 -10.805 -35.917 1.00 41.18  ?  152 GLN   A CD  1 
ATOM   1094 O  OE1 . GLN   A 1 137 ? 56.716 -11.520 -36.138 1.00 44.28  ?  152 GLN   A OE1 1 
ATOM   1095 N  NE2 . GLN   A 1 137 ? 55.116 -10.783 -34.741 1.00 49.47  ?  152 GLN   A NE2 1 
ATOM   1096 N  N   . TYR   A 1 138 ? 53.663 -10.444 -40.691 1.00 40.84  ?  153 TYR   A N   1 
ATOM   1097 C  CA  . TYR   A 1 138 ? 52.361 -10.138 -41.286 1.00 40.70  ?  153 TYR   A CA  1 
ATOM   1098 C  C   . TYR   A 1 138 ? 51.591 -11.414 -41.620 1.00 39.68  ?  153 TYR   A C   1 
ATOM   1099 O  O   . TYR   A 1 138 ? 50.404 -11.541 -41.286 1.00 40.54  ?  153 TYR   A O   1 
ATOM   1100 C  CB  . TYR   A 1 138 ? 52.551 -9.278  -42.538 1.00 46.84  ?  153 TYR   A CB  1 
ATOM   1101 C  CG  . TYR   A 1 138 ? 51.258 -8.879  -43.219 1.00 52.31  ?  153 TYR   A CG  1 
ATOM   1102 C  CD1 . TYR   A 1 138 ? 50.477 -7.844  -42.717 1.00 54.35  ?  153 TYR   A CD1 1 
ATOM   1103 C  CD2 . TYR   A 1 138 ? 50.829 -9.521  -44.379 1.00 55.65  ?  153 TYR   A CD2 1 
ATOM   1104 C  CE1 . TYR   A 1 138 ? 49.299 -7.467  -43.339 1.00 62.46  ?  153 TYR   A CE1 1 
ATOM   1105 C  CE2 . TYR   A 1 138 ? 49.653 -9.151  -45.009 1.00 54.66  ?  153 TYR   A CE2 1 
ATOM   1106 C  CZ  . TYR   A 1 138 ? 48.895 -8.119  -44.489 1.00 63.49  ?  153 TYR   A CZ  1 
ATOM   1107 O  OH  . TYR   A 1 138 ? 47.720 -7.751  -45.103 1.00 65.76  ?  153 TYR   A OH  1 
ATOM   1108 N  N   . PHE   A 1 139 ? 52.262 -12.392 -42.231 1.00 44.65  ?  154 PHE   A N   1 
ATOM   1109 C  CA  . PHE   A 1 139 ? 51.562 -13.592 -42.686 1.00 44.21  ?  154 PHE   A CA  1 
ATOM   1110 C  C   . PHE   A 1 139 ? 51.102 -14.457 -41.518 1.00 43.42  ?  154 PHE   A C   1 
ATOM   1111 O  O   . PHE   A 1 139 ? 49.945 -14.895 -41.485 1.00 44.32  ?  154 PHE   A O   1 
ATOM   1112 C  CB  . PHE   A 1 139 ? 52.440 -14.419 -43.626 1.00 43.24  ?  154 PHE   A CB  1 
ATOM   1113 C  CG  . PHE   A 1 139 ? 51.872 -15.786 -43.892 1.00 44.88  ?  154 PHE   A CG  1 
ATOM   1114 C  CD1 . PHE   A 1 139 ? 50.854 -15.954 -44.823 1.00 43.18  ?  154 PHE   A CD1 1 
ATOM   1115 C  CD2 . PHE   A 1 139 ? 52.308 -16.889 -43.175 1.00 41.59  ?  154 PHE   A CD2 1 
ATOM   1116 C  CE1 . PHE   A 1 139 ? 50.296 -17.205 -45.039 1.00 45.00  ?  154 PHE   A CE1 1 
ATOM   1117 C  CE2 . PHE   A 1 139 ? 51.747 -18.137 -43.382 1.00 42.72  ?  154 PHE   A CE2 1 
ATOM   1118 C  CZ  . PHE   A 1 139 ? 50.739 -18.292 -44.318 1.00 43.12  ?  154 PHE   A CZ  1 
ATOM   1119 N  N   . LEU   A 1 140 ? 51.995 -14.730 -40.552 1.00 40.92  ?  155 LEU   A N   1 
ATOM   1120 C  CA  . LEU   A 1 140 ? 51.665 -15.667 -39.478 1.00 44.61  ?  155 LEU   A CA  1 
ATOM   1121 C  C   . LEU   A 1 140 ? 50.645 -15.082 -38.508 1.00 37.34  ?  155 LEU   A C   1 
ATOM   1122 O  O   . LEU   A 1 140 ? 49.822 -15.819 -37.960 1.00 39.27  ?  155 LEU   A O   1 
ATOM   1123 C  CB  . LEU   A 1 140 ? 52.922 -16.105 -38.702 1.00 36.82  ?  155 LEU   A CB  1 
ATOM   1124 C  CG  . LEU   A 1 140 ? 53.717 -17.279 -39.312 1.00 41.26  ?  155 LEU   A CG  1 
ATOM   1125 C  CD1 . LEU   A 1 140 ? 54.884 -17.757 -38.410 1.00 34.01  ?  155 LEU   A CD1 1 
ATOM   1126 C  CD2 . LEU   A 1 140 ? 52.797 -18.463 -39.711 1.00 41.39  ?  155 LEU   A CD2 1 
ATOM   1127 N  N   . ASP   A 1 141 ? 50.710 -13.780 -38.229 1.00 37.46  ?  156 ASP   A N   1 
ATOM   1128 C  CA  . ASP   A 1 141 ? 49.651 -13.176 -37.421 1.00 37.96  ?  156 ASP   A CA  1 
ATOM   1129 C  C   . ASP   A 1 141 ? 48.287 -13.459 -38.039 1.00 38.21  ?  156 ASP   A C   1 
ATOM   1130 O  O   . ASP   A 1 141 ? 47.376 -13.944 -37.362 1.00 36.26  ?  156 ASP   A O   1 
ATOM   1131 C  CB  . ASP   A 1 141 ? 49.863 -11.667 -37.285 1.00 37.06  ?  156 ASP   A CB  1 
ATOM   1132 C  CG  . ASP   A 1 141 ? 50.840 -11.302 -36.166 1.00 39.60  ?  156 ASP   A CG  1 
ATOM   1133 O  OD1 . ASP   A 1 141 ? 51.220 -12.180 -35.368 1.00 41.41  ?  156 ASP   A OD1 1 
ATOM   1134 O  OD2 . ASP   A 1 141 ? 51.239 -10.125 -36.092 1.00 44.15  ?  156 ASP   A OD2 1 
ATOM   1135 N  N   . ARG   A 1 142 ? 48.153 -13.220 -39.348 1.00 43.70  ?  157 ARG   A N   1 
ATOM   1136 C  CA  . ARG   A 1 142 ? 46.876 -13.456 -40.017 1.00 43.61  ?  157 ARG   A CA  1 
ATOM   1137 C  C   . ARG   A 1 142 ? 46.559 -14.940 -40.111 1.00 39.08  ?  157 ARG   A C   1 
ATOM   1138 O  O   . ARG   A 1 142 ? 45.417 -15.351 -39.865 1.00 39.63  ?  157 ARG   A O   1 
ATOM   1139 C  CB  . ARG   A 1 142 ? 46.882 -12.816 -41.402 1.00 39.47  ?  157 ARG   A CB  1 
ATOM   1140 C  CG  . ARG   A 1 142 ? 46.902 -11.286 -41.346 1.00 42.88  ?  157 ARG   A CG  1 
ATOM   1141 C  CD  . ARG   A 1 142 ? 47.394 -10.674 -42.685 1.00 47.60  ?  157 ARG   A CD  1 
ATOM   1142 N  NE  . ARG   A 1 142 ? 46.491 -10.966 -43.799 1.00 46.37  ?  157 ARG   A NE  1 
ATOM   1143 C  CZ  . ARG   A 1 142 ? 45.327 -10.360 -43.993 1.00 49.00  ?  157 ARG   A CZ  1 
ATOM   1144 N  NH1 . ARG   A 1 142 ? 44.898 -9.400  -43.176 1.00 44.25  ?  157 ARG   A NH1 1 
ATOM   1145 N  NH2 . ARG   A 1 142 ? 44.564 -10.738 -45.013 1.00 54.00  ?  157 ARG   A NH2 1 
ATOM   1146 N  N   . PHE   A 1 143 ? 47.561 -15.763 -40.430 1.00 39.69  ?  158 PHE   A N   1 
ATOM   1147 C  CA  . PHE   A 1 143 ? 47.326 -17.199 -40.552 1.00 35.95  ?  158 PHE   A CA  1 
ATOM   1148 C  C   . PHE   A 1 143 ? 46.901 -17.805 -39.220 1.00 41.35  ?  158 PHE   A C   1 
ATOM   1149 O  O   . PHE   A 1 143 ? 45.949 -18.591 -39.156 1.00 41.48  ?  158 PHE   A O   1 
ATOM   1150 C  CB  . PHE   A 1 143 ? 48.586 -17.899 -41.065 1.00 40.68  ?  158 PHE   A CB  1 
ATOM   1151 C  CG  . PHE   A 1 143 ? 48.466 -19.389 -41.068 1.00 42.97  ?  158 PHE   A CG  1 
ATOM   1152 C  CD1 . PHE   A 1 143 ? 47.862 -20.034 -42.136 1.00 44.58  ?  158 PHE   A CD1 1 
ATOM   1153 C  CD2 . PHE   A 1 143 ? 48.900 -20.145 -39.990 1.00 41.04  ?  158 PHE   A CD2 1 
ATOM   1154 C  CE1 . PHE   A 1 143 ? 47.720 -21.411 -42.138 1.00 49.64  ?  158 PHE   A CE1 1 
ATOM   1155 C  CE2 . PHE   A 1 143 ? 48.759 -21.514 -39.989 1.00 51.31  ?  158 PHE   A CE2 1 
ATOM   1156 C  CZ  . PHE   A 1 143 ? 48.171 -22.148 -41.071 1.00 47.75  ?  158 PHE   A CZ  1 
ATOM   1157 N  N   . TYR   A 1 144 ? 47.619 -17.470 -38.141 1.00 37.14  ?  159 TYR   A N   1 
ATOM   1158 C  CA  . TYR   A 1 144 ? 47.304 -18.030 -36.831 1.00 34.61  ?  159 TYR   A CA  1 
ATOM   1159 C  C   . TYR   A 1 144 ? 45.992 -17.481 -36.286 1.00 39.91  ?  159 TYR   A C   1 
ATOM   1160 O  O   . TYR   A 1 144 ? 45.267 -18.189 -35.571 1.00 38.33  ?  159 TYR   A O   1 
ATOM   1161 C  CB  . TYR   A 1 144 ? 48.440 -17.733 -35.834 1.00 31.72  ?  159 TYR   A CB  1 
ATOM   1162 C  CG  . TYR   A 1 144 ? 49.676 -18.599 -35.998 1.00 39.15  ?  159 TYR   A CG  1 
ATOM   1163 C  CD1 . TYR   A 1 144 ? 49.578 -19.900 -36.484 1.00 42.11  ?  159 TYR   A CD1 1 
ATOM   1164 C  CD2 . TYR   A 1 144 ? 50.939 -18.117 -35.664 1.00 39.80  ?  159 TYR   A CD2 1 
ATOM   1165 C  CE1 . TYR   A 1 144 ? 50.709 -20.706 -36.626 1.00 44.83  ?  159 TYR   A CE1 1 
ATOM   1166 C  CE2 . TYR   A 1 144 ? 52.076 -18.918 -35.800 1.00 41.19  ?  159 TYR   A CE2 1 
ATOM   1167 C  CZ  . TYR   A 1 144 ? 51.952 -20.210 -36.285 1.00 42.59  ?  159 TYR   A CZ  1 
ATOM   1168 O  OH  . TYR   A 1 144 ? 53.070 -21.012 -36.425 1.00 40.48  ?  159 TYR   A OH  1 
ATOM   1169 N  N   . LEU   A 1 145 ? 45.685 -16.213 -36.572 1.00 35.83  ?  160 LEU   A N   1 
ATOM   1170 C  CA  . LEU   A 1 145 ? 44.398 -15.666 -36.148 1.00 42.71  ?  160 LEU   A CA  1 
ATOM   1171 C  C   . LEU   A 1 145 ? 43.241 -16.363 -36.869 1.00 38.91  ?  160 LEU   A C   1 
ATOM   1172 O  O   . LEU   A 1 145 ? 42.230 -16.718 -36.252 1.00 37.36  ?  160 LEU   A O   1 
ATOM   1173 C  CB  . LEU   A 1 145 ? 44.383 -14.159 -36.416 1.00 40.85  ?  160 LEU   A CB  1 
ATOM   1174 C  CG  . LEU   A 1 145 ? 43.361 -13.235 -35.774 1.00 48.66  ?  160 LEU   A CG  1 
ATOM   1175 C  CD1 . LEU   A 1 145 ? 43.184 -13.593 -34.296 1.00 38.93  ?  160 LEU   A CD1 1 
ATOM   1176 C  CD2 . LEU   A 1 145 ? 43.837 -11.795 -35.924 1.00 52.61  ?  160 LEU   A CD2 1 
ATOM   1177 N  N   . SER   A 1 146 ? 43.381 -16.570 -38.172 1.00 34.24  ?  161 SER   A N   1 
ATOM   1178 C  CA  . SER   A 1 146 ? 42.400 -17.347 -38.921 1.00 40.44  ?  161 SER   A CA  1 
ATOM   1179 C  C   . SER   A 1 146 ? 42.203 -18.733 -38.308 1.00 45.07  ?  161 SER   A C   1 
ATOM   1180 O  O   . SER   A 1 146 ? 41.066 -19.189 -38.134 1.00 41.78  ?  161 SER   A O   1 
ATOM   1181 C  CB  . SER   A 1 146 ? 42.855 -17.443 -40.384 1.00 41.64  ?  161 SER   A CB  1 
ATOM   1182 O  OG  . SER   A 1 146 ? 42.401 -18.634 -41.008 1.00 48.31  ?  161 SER   A OG  1 
ATOM   1183 N  N   . ARG   A 1 147 ? 43.305 -19.407 -37.946 1.00 43.60  ?  162 ARG   A N   1 
ATOM   1184 C  CA  . ARG   A 1 147 ? 43.208 -20.731 -37.334 1.00 44.08  ?  162 ARG   A CA  1 
ATOM   1185 C  C   . ARG   A 1 147 ? 42.480 -20.678 -35.994 1.00 42.24  ?  162 ARG   A C   1 
ATOM   1186 O  O   . ARG   A 1 147 ? 41.690 -21.576 -35.664 1.00 39.69  ?  162 ARG   A O   1 
ATOM   1187 C  CB  . ARG   A 1 147 ? 44.605 -21.322 -37.148 1.00 45.25  ?  162 ARG   A CB  1 
ATOM   1188 C  CG  . ARG   A 1 147 ? 44.640 -22.517 -36.210 1.00 47.53  ?  162 ARG   A CG  1 
ATOM   1189 C  CD  . ARG   A 1 147 ? 46.054 -22.922 -35.895 1.00 52.67  ?  162 ARG   A CD  1 
ATOM   1190 N  NE  . ARG   A 1 147 ? 46.143 -23.641 -34.628 1.00 52.57  ?  162 ARG   A NE  1 
ATOM   1191 C  CZ  . ARG   A 1 147 ? 45.837 -24.921 -34.493 1.00 55.50  ?  162 ARG   A CZ  1 
ATOM   1192 N  NH1 . ARG   A 1 147 ? 45.405 -25.635 -35.519 1.00 54.08  ?  162 ARG   A NH1 1 
ATOM   1193 N  NH2 . ARG   A 1 147 ? 45.959 -25.498 -33.303 1.00 53.18  ?  162 ARG   A NH2 1 
ATOM   1194 N  N   . ILE   A 1 148 ? 42.751 -19.641 -35.204 1.00 36.99  ?  163 ILE   A N   1 
ATOM   1195 C  CA  . ILE   A 1 148 ? 42.081 -19.462 -33.921 1.00 34.32  ?  163 ILE   A CA  1 
ATOM   1196 C  C   . ILE   A 1 148 ? 40.579 -19.299 -34.129 1.00 45.21  ?  163 ILE   A C   1 
ATOM   1197 O  O   . ILE   A 1 148 ? 39.770 -19.857 -33.378 1.00 35.86  ?  163 ILE   A O   1 
ATOM   1198 C  CB  . ILE   A 1 148 ? 42.690 -18.255 -33.177 1.00 39.77  ?  163 ILE   A CB  1 
ATOM   1199 C  CG1 . ILE   A 1 148 ? 44.045 -18.625 -32.546 1.00 38.65  ?  163 ILE   A CG1 1 
ATOM   1200 C  CG2 . ILE   A 1 148 ? 41.722 -17.717 -32.092 1.00 35.09  ?  163 ILE   A CG2 1 
ATOM   1201 C  CD1 . ILE   A 1 148 ? 44.866 -17.399 -32.118 1.00 44.48  ?  163 ILE   A CD1 1 
ATOM   1202 N  N   . SER   A 1 149 ? 40.178 -18.530 -35.156 1.00 38.34  ?  164 SER   A N   1 
ATOM   1203 C  CA  . SER   A 1 149 ? 38.754 -18.333 -35.405 1.00 33.61  ?  164 SER   A CA  1 
ATOM   1204 C  C   . SER   A 1 149 ? 38.078 -19.608 -35.918 1.00 37.98  ?  164 SER   A C   1 
ATOM   1205 O  O   . SER   A 1 149 ? 36.901 -19.847 -35.623 1.00 42.65  ?  164 SER   A O   1 
ATOM   1206 C  CB  . SER   A 1 149 ? 38.547 -17.199 -36.407 1.00 35.13  ?  164 SER   A CB  1 
ATOM   1207 O  OG  . SER   A 1 149 ? 38.767 -17.636 -37.748 1.00 40.84  ?  164 SER   A OG  1 
ATOM   1208 N  N   . ILE   A 1 150 ? 38.782 -20.420 -36.705 1.00 42.77  ?  165 ILE   A N   1 
ATOM   1209 C  CA  . ILE   A 1 150 ? 38.201 -21.693 -37.135 1.00 44.77  ?  165 ILE   A CA  1 
ATOM   1210 C  C   . ILE   A 1 150 ? 38.045 -22.641 -35.946 1.00 46.85  ?  165 ILE   A C   1 
ATOM   1211 O  O   . ILE   A 1 150 ? 36.989 -23.256 -35.760 1.00 46.85  ?  165 ILE   A O   1 
ATOM   1212 C  CB  . ILE   A 1 150 ? 39.056 -22.303 -38.259 1.00 46.08  ?  165 ILE   A CB  1 
ATOM   1213 C  CG1 . ILE   A 1 150 ? 38.905 -21.441 -39.520 1.00 48.06  ?  165 ILE   A CG1 1 
ATOM   1214 C  CG2 . ILE   A 1 150 ? 38.659 -23.769 -38.510 1.00 42.64  ?  165 ILE   A CG2 1 
ATOM   1215 C  CD1 . ILE   A 1 150 ? 39.899 -21.758 -40.617 1.00 46.31  ?  165 ILE   A CD1 1 
ATOM   1216 N  N   . ARG   A 1 151 ? 39.071 -22.743 -35.097 1.00 45.39  ?  166 ARG   A N   1 
ATOM   1217 C  CA  . ARG   A 1 151 ? 38.961 -23.604 -33.919 1.00 45.98  ?  166 ARG   A CA  1 
ATOM   1218 C  C   . ARG   A 1 151 ? 37.837 -23.155 -32.995 1.00 41.11  ?  166 ARG   A C   1 
ATOM   1219 O  O   . ARG   A 1 151 ? 37.096 -23.986 -32.462 1.00 48.10  ?  166 ARG   A O   1 
ATOM   1220 C  CB  . ARG   A 1 151 ? 40.284 -23.633 -33.158 1.00 49.75  ?  166 ARG   A CB  1 
ATOM   1221 C  CG  . ARG   A 1 151 ? 41.389 -24.303 -33.928 1.00 58.01  ?  166 ARG   A CG  1 
ATOM   1222 C  CD  . ARG   A 1 151 ? 42.586 -24.534 -33.045 1.00 64.25  ?  166 ARG   A CD  1 
ATOM   1223 N  NE  . ARG   A 1 151 ? 42.191 -25.041 -31.735 1.00 76.13  ?  166 ARG   A NE  1 
ATOM   1224 C  CZ  . ARG   A 1 151 ? 42.281 -26.311 -31.364 1.00 78.16  ?  166 ARG   A CZ  1 
ATOM   1225 N  NH1 . ARG   A 1 151 ? 42.759 -27.239 -32.182 1.00 61.15  ?  166 ARG   A NH1 1 
ATOM   1226 N  NH2 . ARG   A 1 151 ? 41.892 -26.656 -30.137 1.00 76.20  ?  166 ARG   A NH2 1 
ATOM   1227 N  N   . MET   A 1 152 ? 37.699 -21.846 -32.786 1.00 42.23  ?  167 MET   A N   1 
ATOM   1228 C  CA  . MET   A 1 152 ? 36.598 -21.325 -31.977 1.00 44.34  ?  167 MET   A CA  1 
ATOM   1229 C  C   . MET   A 1 152 ? 35.248 -21.808 -32.494 1.00 51.14  ?  167 MET   A C   1 
ATOM   1230 O  O   . MET   A 1 152 ? 34.427 -22.333 -31.729 1.00 46.76  ?  167 MET   A O   1 
ATOM   1231 C  CB  . MET   A 1 152 ? 36.635 -19.798 -31.977 1.00 41.51  ?  167 MET   A CB  1 
ATOM   1232 C  CG  . MET   A 1 152 ? 35.501 -19.137 -31.194 1.00 39.96  ?  167 MET   A CG  1 
ATOM   1233 S  SD  . MET   A 1 152 ? 35.786 -19.293 -29.433 1.00 48.51  ?  167 MET   A SD  1 
ATOM   1234 C  CE  . MET   A 1 152 ? 34.259 -18.598 -28.808 1.00 48.62  ?  167 MET   A CE  1 
ATOM   1235 N  N   . LEU   A 1 153 ? 34.993 -21.618 -33.795 1.00 45.34  ?  168 LEU   A N   1 
ATOM   1236 C  CA  . LEU   A 1 153 ? 33.726 -22.048 -34.369 1.00 44.72  ?  168 LEU   A CA  1 
ATOM   1237 C  C   . LEU   A 1 153 ? 33.501 -23.532 -34.125 1.00 47.11  ?  168 LEU   A C   1 
ATOM   1238 O  O   . LEU   A 1 153 ? 32.418 -23.945 -33.702 1.00 46.63  ?  168 LEU   A O   1 
ATOM   1239 C  CB  . LEU   A 1 153 ? 33.690 -21.744 -35.873 1.00 42.06  ?  168 LEU   A CB  1 
ATOM   1240 C  CG  . LEU   A 1 153 ? 33.641 -20.268 -36.296 1.00 51.27  ?  168 LEU   A CG  1 
ATOM   1241 C  CD1 . LEU   A 1 153 ? 33.343 -20.125 -37.779 1.00 47.07  ?  168 LEU   A CD1 1 
ATOM   1242 C  CD2 . LEU   A 1 153 ? 32.607 -19.531 -35.491 1.00 45.72  ?  168 LEU   A CD2 1 
ATOM   1243 N  N   . ILE   A 1 154 ? 34.523 -24.351 -34.373 1.00 44.87  ?  169 ILE   A N   1 
ATOM   1244 C  CA  . ILE   A 1 154 ? 34.360 -25.793 -34.236 1.00 50.89  ?  169 ILE   A CA  1 
ATOM   1245 C  C   . ILE   A 1 154 ? 34.122 -26.163 -32.782 1.00 51.07  ?  169 ILE   A C   1 
ATOM   1246 O  O   . ILE   A 1 154 ? 33.216 -26.940 -32.465 1.00 49.39  ?  169 ILE   A O   1 
ATOM   1247 C  CB  . ILE   A 1 154 ? 35.580 -26.527 -34.812 1.00 48.05  ?  169 ILE   A CB  1 
ATOM   1248 C  CG1 . ILE   A 1 154 ? 35.615 -26.392 -36.336 1.00 50.68  ?  169 ILE   A CG1 1 
ATOM   1249 C  CG2 . ILE   A 1 154 ? 35.561 -28.002 -34.400 1.00 52.00  ?  169 ILE   A CG2 1 
ATOM   1250 C  CD1 . ILE   A 1 154 ? 36.861 -26.980 -36.949 1.00 51.05  ?  169 ILE   A CD1 1 
ATOM   1251 N  N   . ASN   A 1 155 ? 34.914 -25.590 -31.874 1.00 48.19  ?  170 ASN   A N   1 
ATOM   1252 C  CA  . ASN   A 1 155 ? 34.739 -25.896 -30.455 1.00 54.81  ?  170 ASN   A CA  1 
ATOM   1253 C  C   . ASN   A 1 155 ? 33.338 -25.541 -29.973 1.00 48.51  ?  170 ASN   A C   1 
ATOM   1254 O  O   . ASN   A 1 155 ? 32.724 -26.315 -29.229 1.00 55.88  ?  170 ASN   A O   1 
ATOM   1255 C  CB  . ASN   A 1 155 ? 35.793 -25.171 -29.612 1.00 54.66  ?  170 ASN   A CB  1 
ATOM   1256 C  CG  . ASN   A 1 155 ? 37.170 -25.818 -29.708 1.00 54.72  ?  170 ASN   A CG  1 
ATOM   1257 O  OD1 . ASN   A 1 155 ? 37.303 -26.976 -30.100 1.00 62.39  ?  170 ASN   A OD1 1 
ATOM   1258 N  ND2 . ASN   A 1 155 ? 38.207 -25.064 -29.338 1.00 53.17  ?  170 ASN   A ND2 1 
ATOM   1259 N  N   . GLN   A 1 156 ? 32.800 -24.385 -30.390 1.00 46.73  ?  171 GLN   A N   1 
ATOM   1260 C  CA  . GLN   A 1 156 ? 31.456 -24.017 -29.936 1.00 52.52  ?  171 GLN   A CA  1 
ATOM   1261 C  C   . GLN   A 1 156 ? 30.418 -25.033 -30.397 1.00 57.81  ?  171 GLN   A C   1 
ATOM   1262 O  O   . GLN   A 1 156 ? 29.490 -25.363 -29.652 1.00 54.47  ?  171 GLN   A O   1 
ATOM   1263 C  CB  . GLN   A 1 156 ? 31.073 -22.621 -30.421 1.00 50.03  ?  171 GLN   A CB  1 
ATOM   1264 C  CG  . GLN   A 1 156 ? 31.734 -21.514 -29.617 1.00 50.76  ?  171 GLN   A CG  1 
ATOM   1265 C  CD  . GLN   A 1 156 ? 31.494 -21.667 -28.141 1.00 53.59  ?  171 GLN   A CD  1 
ATOM   1266 O  OE1 . GLN   A 1 156 ? 32.389 -22.078 -27.401 1.00 52.18  ?  171 GLN   A OE1 1 
ATOM   1267 N  NE2 . GLN   A 1 156 ? 30.276 -21.363 -27.700 1.00 49.77  ?  171 GLN   A NE2 1 
ATOM   1268 N  N   . HIS   A 1 157 ? 30.560 -25.551 -31.615 1.00 53.84  ?  172 HIS   A N   1 
ATOM   1269 C  CA  . HIS   A 1 157 ? 29.578 -26.514 -32.093 1.00 54.43  ?  172 HIS   A CA  1 
ATOM   1270 C  C   . HIS   A 1 157 ? 29.729 -27.862 -31.386 1.00 56.69  ?  172 HIS   A C   1 
ATOM   1271 O  O   . HIS   A 1 157 ? 28.749 -28.416 -30.872 1.00 58.78  ?  172 HIS   A O   1 
ATOM   1272 C  CB  . HIS   A 1 157 ? 29.690 -26.682 -33.609 1.00 54.21  ?  172 HIS   A CB  1 
ATOM   1273 C  CG  . HIS   A 1 157 ? 28.640 -27.585 -34.186 1.00 58.60  ?  172 HIS   A CG  1 
ATOM   1274 N  ND1 . HIS   A 1 157 ? 27.436 -27.116 -34.668 1.00 56.65  ?  172 HIS   A ND1 1 
ATOM   1275 C  CD2 . HIS   A 1 157 ? 28.604 -28.932 -34.332 1.00 60.40  ?  172 HIS   A CD2 1 
ATOM   1276 C  CE1 . HIS   A 1 157 ? 26.709 -28.133 -35.098 1.00 62.04  ?  172 HIS   A CE1 1 
ATOM   1277 N  NE2 . HIS   A 1 157 ? 27.396 -29.246 -34.907 1.00 60.46  ?  172 HIS   A NE2 1 
ATOM   1278 N  N   . THR   A 1 158 ? 30.949 -28.406 -31.339 1.00 50.85  ?  173 THR   A N   1 
ATOM   1279 C  CA  . THR   A 1 158 ? 31.102 -29.754 -30.799 1.00 57.07  ?  173 THR   A CA  1 
ATOM   1280 C  C   . THR   A 1 158 ? 30.837 -29.793 -29.300 1.00 63.11  ?  173 THR   A C   1 
ATOM   1281 O  O   . THR   A 1 158 ? 30.338 -30.802 -28.795 1.00 62.82  ?  173 THR   A O   1 
ATOM   1282 C  CB  . THR   A 1 158 ? 32.493 -30.310 -31.113 1.00 56.61  ?  173 THR   A CB  1 
ATOM   1283 O  OG1 . THR   A 1 158 ? 33.492 -29.457 -30.553 1.00 59.85  ?  173 THR   A OG1 1 
ATOM   1284 C  CG2 . THR   A 1 158 ? 32.710 -30.392 -32.630 1.00 55.69  ?  173 THR   A CG2 1 
ATOM   1285 N  N   . LEU   A 1 159 ? 31.131 -28.703 -28.581 1.00 55.25  ?  174 LEU   A N   1 
ATOM   1286 C  CA  . LEU   A 1 159 ? 30.883 -28.662 -27.142 1.00 57.29  ?  174 LEU   A CA  1 
ATOM   1287 C  C   . LEU   A 1 159 ? 29.403 -28.503 -26.825 1.00 64.34  ?  174 LEU   A C   1 
ATOM   1288 O  O   . LEU   A 1 159 ? 28.894 -29.118 -25.880 1.00 68.85  ?  174 LEU   A O   1 
ATOM   1289 C  CB  . LEU   A 1 159 ? 31.678 -27.526 -26.496 1.00 54.40  ?  174 LEU   A CB  1 
ATOM   1290 C  CG  . LEU   A 1 159 ? 33.198 -27.691 -26.462 1.00 55.82  ?  174 LEU   A CG  1 
ATOM   1291 C  CD1 . LEU   A 1 159 ? 33.876 -26.406 -26.007 1.00 54.08  ?  174 LEU   A CD1 1 
ATOM   1292 C  CD2 . LEU   A 1 159 ? 33.593 -28.860 -25.576 1.00 62.95  ?  174 LEU   A CD2 1 
ATOM   1293 N  N   . ILE   A 1 160 ? 28.695 -27.685 -27.592 1.00 57.69  ?  175 ILE   A N   1 
ATOM   1294 C  CA  . ILE   A 1 160 ? 27.281 -27.478 -27.313 1.00 60.24  ?  175 ILE   A CA  1 
ATOM   1295 C  C   . ILE   A 1 160 ? 26.457 -28.659 -27.799 1.00 68.24  ?  175 ILE   A C   1 
ATOM   1296 O  O   . ILE   A 1 160 ? 25.616 -29.193 -27.067 1.00 69.00  ?  175 ILE   A O   1 
ATOM   1297 C  CB  . ILE   A 1 160 ? 26.805 -26.155 -27.935 1.00 66.12  ?  175 ILE   A CB  1 
ATOM   1298 C  CG1 . ILE   A 1 160 ? 27.387 -24.972 -27.159 1.00 65.13  ?  175 ILE   A CG1 1 
ATOM   1299 C  CG2 . ILE   A 1 160 ? 25.294 -26.088 -27.957 1.00 70.48  ?  175 ILE   A CG2 1 
ATOM   1300 C  CD1 . ILE   A 1 160 ? 27.307 -23.681 -27.917 1.00 67.16  ?  175 ILE   A CD1 1 
ATOM   1301 N  N   . PHE   A 1 161 ? 26.696 -29.108 -29.030 1.00 66.71  ?  176 PHE   A N   1 
ATOM   1302 C  CA  . PHE   A 1 161 ? 25.844 -30.121 -29.645 1.00 75.55  ?  176 PHE   A CA  1 
ATOM   1303 C  C   . PHE   A 1 161 ? 26.457 -31.515 -29.608 1.00 71.64  ?  176 PHE   A C   1 
ATOM   1304 O  O   . PHE   A 1 161 ? 26.292 -32.298 -30.544 1.00 81.15  ?  176 PHE   A O   1 
ATOM   1305 C  CB  . PHE   A 1 161 ? 25.493 -29.700 -31.070 1.00 68.48  ?  176 PHE   A CB  1 
ATOM   1306 C  CG  . PHE   A 1 161 ? 24.846 -28.350 -31.140 1.00 70.34  ?  176 PHE   A CG  1 
ATOM   1307 C  CD1 . PHE   A 1 161 ? 23.544 -28.170 -30.692 1.00 73.91  ?  176 PHE   A CD1 1 
ATOM   1308 C  CD2 . PHE   A 1 161 ? 25.540 -27.256 -31.626 1.00 63.25  ?  176 PHE   A CD2 1 
ATOM   1309 C  CE1 . PHE   A 1 161 ? 22.947 -26.923 -30.746 1.00 73.33  ?  176 PHE   A CE1 1 
ATOM   1310 C  CE2 . PHE   A 1 161 ? 24.949 -26.008 -31.683 1.00 69.48  ?  176 PHE   A CE2 1 
ATOM   1311 C  CZ  . PHE   A 1 161 ? 23.648 -25.844 -31.245 1.00 73.05  ?  176 PHE   A CZ  1 
ATOM   1312 N  N   . ASP   A 1 162 ? 27.174 -31.829 -28.538 1.00 87.96  ?  177 ASP   A N   1 
ATOM   1313 C  CA  . ASP   A 1 162 ? 27.402 -33.208 -28.145 1.00 100.29 ?  177 ASP   A CA  1 
ATOM   1314 C  C   . ASP   A 1 162 ? 26.918 -33.475 -26.734 1.00 99.89  ?  177 ASP   A C   1 
ATOM   1315 O  O   . ASP   A 1 162 ? 26.312 -34.525 -26.486 1.00 96.77  ?  177 ASP   A O   1 
ATOM   1316 C  CB  . ASP   A 1 162 ? 28.887 -33.578 -28.268 1.00 110.81 ?  177 ASP   A CB  1 
ATOM   1317 C  CG  . ASP   A 1 162 ? 29.098 -35.074 -28.452 1.00 124.17 ?  177 ASP   A CG  1 
ATOM   1318 O  OD1 . ASP   A 1 162 ? 28.632 -35.854 -27.591 1.00 123.76 ?  177 ASP   A OD1 1 
ATOM   1319 O  OD2 . ASP   A 1 162 ? 29.707 -35.472 -29.470 1.00 122.64 ?  177 ASP   A OD2 1 
ATOM   1320 N  N   . GLY   A 1 163 ? 27.145 -32.537 -25.814 1.00 88.60  ?  178 GLY   A N   1 
ATOM   1321 C  CA  . GLY   A 1 163 ? 26.585 -32.604 -24.477 1.00 96.45  ?  178 GLY   A CA  1 
ATOM   1322 C  C   . GLY   A 1 163 ? 25.065 -32.633 -24.468 1.00 98.48  ?  178 GLY   A C   1 
ATOM   1323 O  O   . GLY   A 1 163 ? 24.448 -33.439 -23.765 1.00 103.09 ?  178 GLY   A O   1 
ATOM   1324 N  N   . PRO   A 1 170 ? 22.869 -24.618 -17.846 1.00 115.20 ?  185 PRO   A N   1 
ATOM   1325 C  CA  . PRO   A 1 170 ? 24.200 -24.424 -18.425 1.00 109.47 ?  185 PRO   A CA  1 
ATOM   1326 C  C   . PRO   A 1 170 ? 24.843 -23.107 -17.997 1.00 104.00 ?  185 PRO   A C   1 
ATOM   1327 O  O   . PRO   A 1 170 ? 24.506 -22.054 -18.541 1.00 104.68 ?  185 PRO   A O   1 
ATOM   1328 C  CB  . PRO   A 1 170 ? 23.920 -24.429 -19.931 1.00 107.48 ?  185 PRO   A CB  1 
ATOM   1329 C  CG  . PRO   A 1 170 ? 22.466 -23.959 -20.058 1.00 116.88 ?  185 PRO   A CG  1 
ATOM   1330 C  CD  . PRO   A 1 170 ? 21.835 -23.977 -18.674 1.00 119.95 ?  185 PRO   A CD  1 
ATOM   1331 N  N   . LYS   A 1 171 ? 25.753 -23.168 -17.022 1.00 85.19  ?  186 LYS   A N   1 
ATOM   1332 C  CA  . LYS   A 1 171 ? 26.456 -21.963 -16.595 1.00 68.60  ?  186 LYS   A CA  1 
ATOM   1333 C  C   . LYS   A 1 171 ? 27.430 -21.494 -17.669 1.00 67.64  ?  186 LYS   A C   1 
ATOM   1334 O  O   . LYS   A 1 171 ? 27.573 -20.290 -17.898 1.00 76.46  ?  186 LYS   A O   1 
ATOM   1335 C  CB  . LYS   A 1 171 ? 27.179 -22.220 -15.271 1.00 68.72  ?  186 LYS   A CB  1 
ATOM   1336 C  CG  . LYS   A 1 171 ? 26.233 -22.611 -14.121 1.00 76.40  ?  186 LYS   A CG  1 
ATOM   1337 C  CD  . LYS   A 1 171 ? 26.988 -23.181 -12.916 1.00 91.47  ?  186 LYS   A CD  1 
ATOM   1338 C  CE  . LYS   A 1 171 ? 27.119 -24.710 -12.970 1.00 85.54  ?  186 LYS   A CE  1 
ATOM   1339 N  NZ  . LYS   A 1 171 ? 26.092 -25.410 -12.140 1.00 88.67  ?  186 LYS   A NZ  1 
ATOM   1340 N  N   . HIS   A 1 172 ? 28.102 -22.426 -18.335 1.00 61.73  ?  187 HIS   A N   1 
ATOM   1341 C  CA  . HIS   A 1 172 ? 28.985 -22.139 -19.454 1.00 60.12  ?  187 HIS   A CA  1 
ATOM   1342 C  C   . HIS   A 1 172 ? 28.279 -22.451 -20.768 1.00 61.66  ?  187 HIS   A C   1 
ATOM   1343 O  O   . HIS   A 1 172 ? 27.405 -23.319 -20.835 1.00 66.15  ?  187 HIS   A O   1 
ATOM   1344 C  CB  . HIS   A 1 172 ? 30.277 -22.958 -19.353 1.00 59.08  ?  187 HIS   A CB  1 
ATOM   1345 C  CG  . HIS   A 1 172 ? 31.193 -22.522 -18.250 1.00 58.73  ?  187 HIS   A CG  1 
ATOM   1346 N  ND1 . HIS   A 1 172 ? 32.501 -22.148 -18.474 1.00 55.55  ?  187 HIS   A ND1 1 
ATOM   1347 C  CD2 . HIS   A 1 172 ? 30.993 -22.411 -16.913 1.00 55.17  ?  187 HIS   A CD2 1 
ATOM   1348 C  CE1 . HIS   A 1 172 ? 33.066 -21.815 -17.327 1.00 54.91  ?  187 HIS   A CE1 1 
ATOM   1349 N  NE2 . HIS   A 1 172 ? 32.175 -21.973 -16.362 1.00 55.43  ?  187 HIS   A NE2 1 
ATOM   1350 N  N   . ILE   A 1 173 ? 28.657 -21.734 -21.818 1.00 58.01  ?  188 ILE   A N   1 
ATOM   1351 C  CA  . ILE   A 1 173 ? 28.087 -21.948 -23.148 1.00 54.88  ?  188 ILE   A CA  1 
ATOM   1352 C  C   . ILE   A 1 173 ? 29.243 -22.351 -24.056 1.00 55.35  ?  188 ILE   A C   1 
ATOM   1353 O  O   . ILE   A 1 173 ? 29.914 -21.507 -24.658 1.00 50.37  ?  188 ILE   A O   1 
ATOM   1354 C  CB  . ILE   A 1 173 ? 27.350 -20.715 -23.674 1.00 65.53  ?  188 ILE   A CB  1 
ATOM   1355 C  CG1 . ILE   A 1 173 ? 26.218 -20.333 -22.714 1.00 56.89  ?  188 ILE   A CG1 1 
ATOM   1356 C  CG2 . ILE   A 1 173 ? 26.804 -20.970 -25.075 1.00 63.49  ?  188 ILE   A CG2 1 
ATOM   1357 C  CD1 . ILE   A 1 173 ? 25.201 -21.437 -22.495 1.00 69.59  ?  188 ILE   A CD1 1 
ATOM   1358 N  N   . GLY   A 1 174 ? 29.481 -23.656 -24.164 1.00 54.16  ?  189 GLY   A N   1 
ATOM   1359 C  CA  . GLY   A 1 174 ? 30.656 -24.121 -24.881 1.00 53.68  ?  189 GLY   A CA  1 
ATOM   1360 C  C   . GLY   A 1 174 ? 31.911 -23.640 -24.173 1.00 51.06  ?  189 GLY   A C   1 
ATOM   1361 O  O   . GLY   A 1 174 ? 32.114 -23.893 -22.977 1.00 52.11  ?  189 GLY   A O   1 
ATOM   1362 N  N   . SER   A 1 175 ? 32.753 -22.909 -24.897 1.00 43.49  ?  190 SER   A N   1 
ATOM   1363 C  CA  . SER   A 1 175 ? 33.996 -22.381 -24.364 1.00 46.65  ?  190 SER   A CA  1 
ATOM   1364 C  C   . SER   A 1 175 ? 33.850 -20.981 -23.770 1.00 51.00  ?  190 SER   A C   1 
ATOM   1365 O  O   . SER   A 1 175 ? 34.857 -20.378 -23.391 1.00 47.40  ?  190 SER   A O   1 
ATOM   1366 C  CB  . SER   A 1 175 ? 35.054 -22.363 -25.454 1.00 46.12  ?  190 SER   A CB  1 
ATOM   1367 O  OG  . SER   A 1 175 ? 34.834 -21.263 -26.317 1.00 59.48  ?  190 SER   A OG  1 
ATOM   1368 N  N   . ILE   A 1 176 ? 32.631 -20.458 -23.674 1.00 49.10  ?  191 ILE   A N   1 
ATOM   1369 C  CA  . ILE   A 1 176 ? 32.380 -19.109 -23.177 1.00 48.73  ?  191 ILE   A CA  1 
ATOM   1370 C  C   . ILE   A 1 176 ? 31.811 -19.196 -21.770 1.00 51.11  ?  191 ILE   A C   1 
ATOM   1371 O  O   . ILE   A 1 176 ? 30.939 -20.032 -21.481 1.00 50.32  ?  191 ILE   A O   1 
ATOM   1372 C  CB  . ILE   A 1 176 ? 31.422 -18.336 -24.095 1.00 52.45  ?  191 ILE   A CB  1 
ATOM   1373 C  CG1 . ILE   A 1 176 ? 32.062 -18.148 -25.467 1.00 49.94  ?  191 ILE   A CG1 1 
ATOM   1374 C  CG2 . ILE   A 1 176 ? 31.071 -16.977 -23.505 1.00 46.49  ?  191 ILE   A CG2 1 
ATOM   1375 C  CD1 . ILE   A 1 176 ? 31.048 -17.812 -26.497 1.00 52.63  ?  191 ILE   A CD1 1 
ATOM   1376 N  N   . ASP   A 1 177 ? 32.312 -18.342 -20.895 1.00 45.02  ?  192 ASP   A N   1 
ATOM   1377 C  CA  . ASP   A 1 177 ? 31.763 -18.230 -19.553 1.00 48.65  ?  192 ASP   A CA  1 
ATOM   1378 C  C   . ASP   A 1 177 ? 31.093 -16.869 -19.472 1.00 42.86  ?  192 ASP   A C   1 
ATOM   1379 O  O   . ASP   A 1 177 ? 31.782 -15.845 -19.580 1.00 42.82  ?  192 ASP   A O   1 
ATOM   1380 C  CB  . ASP   A 1 177 ? 32.876 -18.370 -18.507 1.00 49.69  ?  192 ASP   A CB  1 
ATOM   1381 C  CG  . ASP   A 1 177 ? 32.364 -18.371 -17.073 1.00 50.89  ?  192 ASP   A CG  1 
ATOM   1382 O  OD1 . ASP   A 1 177 ? 31.166 -18.091 -16.858 1.00 45.97  ?  192 ASP   A OD1 1 
ATOM   1383 O  OD2 . ASP   A 1 177 ? 33.177 -18.660 -16.158 1.00 48.43  ?  192 ASP   A OD2 1 
ATOM   1384 N  N   . PRO   A 1 178 ? 29.766 -16.791 -19.350 1.00 44.42  ?  193 PRO   A N   1 
ATOM   1385 C  CA  . PRO   A 1 178 ? 29.117 -15.474 -19.260 1.00 49.38  ?  193 PRO   A CA  1 
ATOM   1386 C  C   . PRO   A 1 178 ? 29.370 -14.774 -17.944 1.00 50.78  ?  193 PRO   A C   1 
ATOM   1387 O  O   . PRO   A 1 178 ? 29.020 -13.593 -17.823 1.00 50.87  ?  193 PRO   A O   1 
ATOM   1388 C  CB  . PRO   A 1 178 ? 27.631 -15.801 -19.439 1.00 47.94  ?  193 PRO   A CB  1 
ATOM   1389 C  CG  . PRO   A 1 178 ? 27.511 -17.208 -18.952 1.00 54.44  ?  193 PRO   A CG  1 
ATOM   1390 C  CD  . PRO   A 1 178 ? 28.788 -17.889 -19.360 1.00 46.99  ?  193 PRO   A CD  1 
ATOM   1391 N  N   . ASN   A 1 179 ? 29.978 -15.456 -16.971 1.00 50.25  ?  194 ASN   A N   1 
ATOM   1392 C  CA  . ASN   A 1 179 ? 30.285 -14.899 -15.652 1.00 48.03  ?  194 ASN   A CA  1 
ATOM   1393 C  C   . ASN   A 1 179 ? 31.702 -15.282 -15.251 1.00 52.52  ?  194 ASN   A C   1 
ATOM   1394 O  O   . ASN   A 1 179 ? 31.939 -15.872 -14.198 1.00 50.16  ?  194 ASN   A O   1 
ATOM   1395 C  CB  . ASN   A 1 179 ? 29.279 -15.373 -14.609 1.00 49.62  ?  194 ASN   A CB  1 
ATOM   1396 C  CG  . ASN   A 1 179 ? 28.266 -14.315 -14.286 1.00 69.62  ?  194 ASN   A CG  1 
ATOM   1397 O  OD1 . ASN   A 1 179 ? 28.577 -13.333 -13.600 1.00 69.33  ?  194 ASN   A OD1 1 
ATOM   1398 N  ND2 . ASN   A 1 179 ? 27.049 -14.485 -14.796 1.00 72.87  ?  194 ASN   A ND2 1 
ATOM   1399 N  N   . CYS   A 1 180 ? 32.657 -14.979 -16.124 1.00 44.27  ?  195 CYS   A N   1 
ATOM   1400 C  CA  . CYS   A 1 180 ? 34.053 -15.316 -15.896 1.00 44.43  ?  195 CYS   A CA  1 
ATOM   1401 C  C   . CYS   A 1 180 ? 34.630 -14.428 -14.798 1.00 53.82  ?  195 CYS   A C   1 
ATOM   1402 O  O   . CYS   A 1 180 ? 34.777 -13.217 -14.993 1.00 45.89  ?  195 CYS   A O   1 
ATOM   1403 C  CB  . CYS   A 1 180 ? 34.838 -15.134 -17.189 1.00 41.87  ?  195 CYS   A CB  1 
ATOM   1404 S  SG  . CYS   A 1 180 ? 36.612 -15.339 -16.938 1.00 47.15  ?  195 CYS   A SG  1 
ATOM   1405 N  N   . ASN   A 1 181 ? 34.963 -15.023 -13.652 1.00 43.99  ?  196 ASN   A N   1 
ATOM   1406 C  CA  . ASN   A 1 181 ? 35.606 -14.297 -12.557 1.00 46.60  ?  196 ASN   A CA  1 
ATOM   1407 C  C   . ASN   A 1 181 ? 37.088 -14.157 -12.895 1.00 45.15  ?  196 ASN   A C   1 
ATOM   1408 O  O   . ASN   A 1 181 ? 37.842 -15.135 -12.859 1.00 43.96  ?  196 ASN   A O   1 
ATOM   1409 C  CB  . ASN   A 1 181 ? 35.380 -15.040 -11.241 1.00 48.72  ?  196 ASN   A CB  1 
ATOM   1410 C  CG  . ASN   A 1 181 ? 36.052 -14.363 -10.042 1.00 55.82  ?  196 ASN   A CG  1 
ATOM   1411 O  OD1 . ASN   A 1 181 ? 37.165 -13.844 -10.136 1.00 52.31  ?  196 ASN   A OD1 1 
ATOM   1412 N  ND2 . ASN   A 1 181 ? 35.378 -14.399 -8.898  1.00 72.29  ?  196 ASN   A ND2 1 
ATOM   1413 N  N   . VAL   A 1 182 ? 37.516 -12.945 -13.242 1.00 40.93  ?  197 VAL   A N   1 
ATOM   1414 C  CA  . VAL   A 1 182 ? 38.847 -12.800 -13.818 1.00 39.11  ?  197 VAL   A CA  1 
ATOM   1415 C  C   . VAL   A 1 182 ? 39.936 -13.148 -12.802 1.00 44.50  ?  197 VAL   A C   1 
ATOM   1416 O  O   . VAL   A 1 182 ? 40.883 -13.871 -13.126 1.00 39.75  ?  197 VAL   A O   1 
ATOM   1417 C  CB  . VAL   A 1 182 ? 39.010 -11.390 -14.401 1.00 48.75  ?  197 VAL   A CB  1 
ATOM   1418 C  CG1 . VAL   A 1 182 ? 40.456 -11.156 -14.846 1.00 33.94  ?  197 VAL   A CG1 1 
ATOM   1419 C  CG2 . VAL   A 1 182 ? 38.050 -11.248 -15.588 1.00 46.52  ?  197 VAL   A CG2 1 
ATOM   1420 N  N   . SER   A 1 183 ? 39.813 -12.666 -11.559 1.00 40.24  ?  198 SER   A N   1 
ATOM   1421 C  CA  . SER   A 1 183 ? 40.849 -12.921 -10.560 1.00 38.29  ?  198 SER   A CA  1 
ATOM   1422 C  C   . SER   A 1 183 ? 41.016 -14.407 -10.283 1.00 41.94  ?  198 SER   A C   1 
ATOM   1423 O  O   . SER   A 1 183 ? 42.118 -14.859 -9.946  1.00 40.80  ?  198 SER   A O   1 
ATOM   1424 C  CB  . SER   A 1 183 ? 40.517 -12.191 -9.254  1.00 44.12  ?  198 SER   A CB  1 
ATOM   1425 O  OG  . SER   A 1 183 ? 40.759 -10.808 -9.436  1.00 55.23  ?  198 SER   A OG  1 
ATOM   1426 N  N   . GLU   A 1 184 ? 39.935 -15.179 -10.403 1.00 43.63  ?  199 GLU   A N   1 
ATOM   1427 C  CA  . GLU   A 1 184 ? 40.024 -16.622 -10.207 1.00 45.70  ?  199 GLU   A CA  1 
ATOM   1428 C  C   . GLU   A 1 184 ? 40.878 -17.271 -11.293 1.00 42.44  ?  199 GLU   A C   1 
ATOM   1429 O  O   . GLU   A 1 184 ? 41.716 -18.141 -11.009 1.00 42.45  ?  199 GLU   A O   1 
ATOM   1430 C  CB  . GLU   A 1 184 ? 38.613 -17.214 -10.176 1.00 47.98  ?  199 GLU   A CB  1 
ATOM   1431 C  CG  . GLU   A 1 184 ? 38.554 -18.737 -10.232 1.00 56.60  ?  199 GLU   A CG  1 
ATOM   1432 C  CD  . GLU   A 1 184 ? 38.995 -19.399 -8.938  1.00 71.79  ?  199 GLU   A CD  1 
ATOM   1433 O  OE1 . GLU   A 1 184 ? 39.127 -18.681 -7.918  1.00 73.57  ?  199 GLU   A OE1 1 
ATOM   1434 O  OE2 . GLU   A 1 184 ? 39.204 -20.637 -8.944  1.00 67.66  ?  199 GLU   A OE2 1 
ATOM   1435 N  N   . VAL   A 1 185 ? 40.691 -16.855 -12.548 1.00 37.79  ?  200 VAL   A N   1 
ATOM   1436 C  CA  . VAL   A 1 185 ? 41.523 -17.384 -13.626 1.00 43.48  ?  200 VAL   A CA  1 
ATOM   1437 C  C   . VAL   A 1 185 ? 42.975 -16.968 -13.429 1.00 40.44  ?  200 VAL   A C   1 
ATOM   1438 O  O   . VAL   A 1 185 ? 43.902 -17.757 -13.660 1.00 38.02  ?  200 VAL   A O   1 
ATOM   1439 C  CB  . VAL   A 1 185 ? 40.990 -16.924 -14.996 1.00 40.17  ?  200 VAL   A CB  1 
ATOM   1440 C  CG1 . VAL   A 1 185 ? 41.895 -17.456 -16.098 1.00 36.20  ?  200 VAL   A CG1 1 
ATOM   1441 C  CG2 . VAL   A 1 185 ? 39.571 -17.424 -15.193 1.00 42.73  ?  200 VAL   A CG2 1 
ATOM   1442 N  N   . VAL   A 1 186 ? 43.194 -15.716 -13.010 1.00 37.76  ?  201 VAL   A N   1 
ATOM   1443 C  CA  . VAL   A 1 186 ? 44.544 -15.265 -12.669 1.00 41.78  ?  201 VAL   A CA  1 
ATOM   1444 C  C   . VAL   A 1 186 ? 45.166 -16.204 -11.636 1.00 37.51  ?  201 VAL   A C   1 
ATOM   1445 O  O   . VAL   A 1 186 ? 46.301 -16.672 -11.798 1.00 36.46  ?  201 VAL   A O   1 
ATOM   1446 C  CB  . VAL   A 1 186 ? 44.510 -13.811 -12.155 1.00 40.33  ?  201 VAL   A CB  1 
ATOM   1447 C  CG1 . VAL   A 1 186 ? 45.875 -13.411 -11.643 1.00 43.22  ?  201 VAL   A CG1 1 
ATOM   1448 C  CG2 . VAL   A 1 186 ? 44.084 -12.859 -13.278 1.00 36.30  ?  201 VAL   A CG2 1 
ATOM   1449 N  N   . LYS   A 1 187 ? 44.420 -16.526 -10.579 1.00 37.92  ?  202 LYS   A N   1 
ATOM   1450 C  CA  . LYS   A 1 187 ? 44.982 -17.379 -9.530  1.00 44.59  ?  202 LYS   A CA  1 
ATOM   1451 C  C   . LYS   A 1 187 ? 45.332 -18.764 -10.062 1.00 43.08  ?  202 LYS   A C   1 
ATOM   1452 O  O   . LYS   A 1 187 ? 46.397 -19.306 -9.737  1.00 45.28  ?  202 LYS   A O   1 
ATOM   1453 C  CB  . LYS   A 1 187 ? 44.006 -17.525 -8.363  1.00 44.22  ?  202 LYS   A CB  1 
ATOM   1454 C  CG  . LYS   A 1 187 ? 43.819 -16.269 -7.549  1.00 50.73  ?  202 LYS   A CG  1 
ATOM   1455 C  CD  . LYS   A 1 187 ? 42.854 -16.526 -6.384  1.00 58.42  ?  202 LYS   A CD  1 
ATOM   1456 C  CE  . LYS   A 1 187 ? 42.354 -15.199 -5.813  1.00 54.48  ?  202 LYS   A CE  1 
ATOM   1457 N  NZ  . LYS   A 1 187 ? 41.524 -15.392 -4.584  1.00 68.19  ?  202 LYS   A NZ  1 
ATOM   1458 N  N   . ASP   A 1 188 ? 44.432 -19.362 -10.856 1.00 44.92  ?  203 ASP   A N   1 
ATOM   1459 C  CA  . ASP   A 1 188 ? 44.678 -20.684 -11.425 1.00 44.72  ?  203 ASP   A CA  1 
ATOM   1460 C  C   . ASP   A 1 188 ? 45.975 -20.693 -12.220 1.00 40.42  ?  203 ASP   A C   1 
ATOM   1461 O  O   . ASP   A 1 188 ? 46.827 -21.573 -12.044 1.00 38.56  ?  203 ASP   A O   1 
ATOM   1462 C  CB  . ASP   A 1 188 ? 43.529 -21.095 -12.360 1.00 49.18  ?  203 ASP   A CB  1 
ATOM   1463 C  CG  . ASP   A 1 188 ? 42.168 -21.208 -11.674 1.00 53.70  ?  203 ASP   A CG  1 
ATOM   1464 O  OD1 . ASP   A 1 188 ? 42.080 -21.220 -10.430 1.00 43.34  ?  203 ASP   A OD1 1 
ATOM   1465 O  OD2 . ASP   A 1 188 ? 41.160 -21.280 -12.427 1.00 49.29  ?  203 ASP   A OD2 1 
ATOM   1466 N  N   . ALA   A 1 189 ? 46.100 -19.748 -13.156 1.00 39.03  ?  204 ALA   A N   1 
ATOM   1467 C  CA  . ALA   A 1 189 ? 47.280 -19.692 -14.013 1.00 36.65  ?  204 ALA   A CA  1 
ATOM   1468 C  C   . ALA   A 1 189 ? 48.543 -19.469 -13.192 1.00 38.10  ?  204 ALA   A C   1 
ATOM   1469 O  O   . ALA   A 1 189 ? 49.583 -20.088 -13.457 1.00 36.66  ?  204 ALA   A O   1 
ATOM   1470 C  CB  . ALA   A 1 189 ? 47.115 -18.582 -15.055 1.00 37.75  ?  204 ALA   A CB  1 
ATOM   1471 N  N   . TYR   A 1 190 ? 48.463 -18.606 -12.177 1.00 37.90  ?  205 TYR   A N   1 
ATOM   1472 C  CA  . TYR   A 1 190 ? 49.596 -18.404 -11.281 1.00 35.48  ?  205 TYR   A CA  1 
ATOM   1473 C  C   . TYR   A 1 190 ? 49.978 -19.709 -10.581 1.00 40.35  ?  205 TYR   A C   1 
ATOM   1474 O  O   . TYR   A 1 190 ? 51.155 -20.099 -10.557 1.00 37.21  ?  205 TYR   A O   1 
ATOM   1475 C  CB  . TYR   A 1 190 ? 49.263 -17.297 -10.264 1.00 40.23  ?  205 TYR   A CB  1 
ATOM   1476 C  CG  . TYR   A 1 190 ? 50.218 -17.301 -9.102  1.00 42.26  ?  205 TYR   A CG  1 
ATOM   1477 C  CD1 . TYR   A 1 190 ? 51.447 -16.670 -9.192  1.00 43.33  ?  205 TYR   A CD1 1 
ATOM   1478 C  CD2 . TYR   A 1 190 ? 49.910 -17.987 -7.927  1.00 49.06  ?  205 TYR   A CD2 1 
ATOM   1479 C  CE1 . TYR   A 1 190 ? 52.353 -16.713 -8.139  1.00 44.91  ?  205 TYR   A CE1 1 
ATOM   1480 C  CE2 . TYR   A 1 190 ? 50.802 -18.033 -6.863  1.00 50.07  ?  205 TYR   A CE2 1 
ATOM   1481 C  CZ  . TYR   A 1 190 ? 52.014 -17.396 -6.984  1.00 47.95  ?  205 TYR   A CZ  1 
ATOM   1482 O  OH  . TYR   A 1 190 ? 52.914 -17.439 -5.959  1.00 55.46  ?  205 TYR   A OH  1 
ATOM   1483 N  N   . ASP   A 1 191 ? 48.988 -20.427 -10.037 1.00 45.56  ?  206 ASP   A N   1 
ATOM   1484 C  CA  . ASP   A 1 191 ? 49.282 -21.668 -9.322  1.00 45.91  ?  206 ASP   A CA  1 
ATOM   1485 C  C   . ASP   A 1 191 ? 50.014 -22.657 -10.219 1.00 46.38  ?  206 ASP   A C   1 
ATOM   1486 O  O   . ASP   A 1 191 ? 50.933 -23.362 -9.777  1.00 44.24  ?  206 ASP   A O   1 
ATOM   1487 C  CB  . ASP   A 1 191 ? 47.995 -22.322 -8.818  1.00 48.60  ?  206 ASP   A CB  1 
ATOM   1488 C  CG  . ASP   A 1 191 ? 47.373 -21.581 -7.685  1.00 59.50  ?  206 ASP   A CG  1 
ATOM   1489 O  OD1 . ASP   A 1 191 ? 48.035 -20.664 -7.161  1.00 50.41  ?  206 ASP   A OD1 1 
ATOM   1490 O  OD2 . ASP   A 1 191 ? 46.214 -21.918 -7.331  1.00 60.39  ?  206 ASP   A OD2 1 
ATOM   1491 N  N   . MET   A 1 192 ? 49.593 -22.742 -11.473 1.00 40.50  ?  207 MET   A N   1 
ATOM   1492 C  CA  . MET   A 1 192 ? 50.175 -23.710 -12.396 1.00 48.26  ?  207 MET   A CA  1 
ATOM   1493 C  C   . MET   A 1 192 ? 51.594 -23.324 -12.788 1.00 39.85  ?  207 MET   A C   1 
ATOM   1494 O  O   . MET   A 1 192 ? 52.466 -24.188 -12.854 1.00 44.12  ?  207 MET   A O   1 
ATOM   1495 C  CB  . MET   A 1 192 ? 49.305 -23.828 -13.639 1.00 39.86  ?  207 MET   A CB  1 
ATOM   1496 C  CG  . MET   A 1 192 ? 49.802 -24.856 -14.623 1.00 41.51  ?  207 MET   A CG  1 
ATOM   1497 S  SD  . MET   A 1 192 ? 49.588 -26.506 -13.952 1.00 48.83  ?  207 MET   A SD  1 
ATOM   1498 C  CE  . MET   A 1 192 ? 51.167 -27.271 -14.278 1.00 44.48  ?  207 MET   A CE  1 
ATOM   1499 N  N   . ALA   A 1 193 ? 51.842 -22.032 -13.053 1.00 38.95  ?  208 ALA   A N   1 
ATOM   1500 C  CA  . ALA   A 1 193 ? 53.204 -21.578 -13.337 1.00 37.50  ?  208 ALA   A CA  1 
ATOM   1501 C  C   . ALA   A 1 193 ? 54.110 -21.775 -12.132 1.00 39.70  ?  208 ALA   A C   1 
ATOM   1502 O  O   . ALA   A 1 193 ? 55.262 -22.207 -12.270 1.00 41.73  ?  208 ALA   A O   1 
ATOM   1503 C  CB  . ALA   A 1 193 ? 53.195 -20.100 -13.734 1.00 35.71  ?  208 ALA   A CB  1 
ATOM   1504 N  N   . LYS   A 1 194 ? 53.603 -21.434 -10.941 1.00 42.10  ?  209 LYS   A N   1 
ATOM   1505 C  CA  . LYS   A 1 194 ? 54.328 -21.645 -9.688  1.00 47.22  ?  209 LYS   A CA  1 
ATOM   1506 C  C   . LYS   A 1 194 ? 54.749 -23.102 -9.523  1.00 53.07  ?  209 LYS   A C   1 
ATOM   1507 O  O   . LYS   A 1 194 ? 55.879 -23.389 -9.101  1.00 52.85  ?  209 LYS   A O   1 
ATOM   1508 C  CB  . LYS   A 1 194 ? 53.440 -21.186 -8.518  1.00 49.68  ?  209 LYS   A CB  1 
ATOM   1509 C  CG  . LYS   A 1 194 ? 53.889 -21.578 -7.106  1.00 60.36  ?  209 LYS   A CG  1 
ATOM   1510 C  CD  . LYS   A 1 194 ? 52.935 -20.956 -6.070  1.00 52.67  ?  209 LYS   A CD  1 
ATOM   1511 C  CE  . LYS   A 1 194 ? 52.877 -21.751 -4.778  1.00 61.44  ?  209 LYS   A CE  1 
ATOM   1512 N  NZ  . LYS   A 1 194 ? 54.149 -21.651 -4.011  1.00 62.72  ?  209 LYS   A NZ  1 
ATOM   1513 N  N   . LEU   A 1 195 ? 53.854 -24.037 -9.852  1.00 53.16  ?  210 LEU   A N   1 
ATOM   1514 C  CA  . LEU   A 1 195 ? 54.170 -25.454 -9.704  1.00 52.91  ?  210 LEU   A CA  1 
ATOM   1515 C  C   . LEU   A 1 195 ? 55.339 -25.843 -10.598 1.00 51.44  ?  210 LEU   A C   1 
ATOM   1516 O  O   . LEU   A 1 195 ? 56.205 -26.631 -10.200 1.00 50.78  ?  210 LEU   A O   1 
ATOM   1517 C  CB  . LEU   A 1 195 ? 52.929 -26.294 -10.033 1.00 58.92  ?  210 LEU   A CB  1 
ATOM   1518 C  CG  . LEU   A 1 195 ? 52.744 -27.675 -9.398  1.00 64.19  ?  210 LEU   A CG  1 
ATOM   1519 C  CD1 . LEU   A 1 195 ? 51.327 -28.166 -9.647  1.00 67.15  ?  210 LEU   A CD1 1 
ATOM   1520 C  CD2 . LEU   A 1 195 ? 53.731 -28.661 -9.962  1.00 73.98  ?  210 LEU   A CD2 1 
ATOM   1521 N  N   . LEU   A 1 196 ? 55.385 -25.294 -11.815 1.00 50.22  ?  211 LEU   A N   1 
ATOM   1522 C  CA  . LEU   A 1 196 ? 56.531 -25.540 -12.686 1.00 53.16  ?  211 LEU   A CA  1 
ATOM   1523 C  C   . LEU   A 1 196 ? 57.775 -24.832 -12.157 1.00 60.23  ?  211 LEU   A C   1 
ATOM   1524 O  O   . LEU   A 1 196 ? 58.877 -25.387 -12.194 1.00 68.98  ?  211 LEU   A O   1 
ATOM   1525 C  CB  . LEU   A 1 196 ? 56.210 -25.090 -14.113 1.00 44.78  ?  211 LEU   A CB  1 
ATOM   1526 C  CG  . LEU   A 1 196 ? 55.240 -25.978 -14.904 1.00 55.46  ?  211 LEU   A CG  1 
ATOM   1527 C  CD1 . LEU   A 1 196 ? 54.755 -25.273 -16.156 1.00 47.18  ?  211 LEU   A CD1 1 
ATOM   1528 C  CD2 . LEU   A 1 196 ? 55.901 -27.315 -15.259 1.00 53.57  ?  211 LEU   A CD2 1 
ATOM   1529 N  N   . CYS   A 1 197 ? 57.607 -23.620 -11.631 1.00 56.95  ?  212 CYS   A N   1 
ATOM   1530 C  CA  . CYS   A 1 197 ? 58.739 -22.859 -11.113 1.00 67.24  ?  212 CYS   A CA  1 
ATOM   1531 C  C   . CYS   A 1 197 ? 59.283 -23.476 -9.825  1.00 65.54  ?  212 CYS   A C   1 
ATOM   1532 O  O   . CYS   A 1 197 ? 60.497 -23.631 -9.681  1.00 71.27  ?  212 CYS   A O   1 
ATOM   1533 C  CB  . CYS   A 1 197 ? 58.318 -21.402 -10.895 1.00 62.40  ?  212 CYS   A CB  1 
ATOM   1534 S  SG  . CYS   A 1 197 ? 59.678 -20.300 -10.481 1.00 62.78  ?  212 CYS   A SG  1 
ATOM   1535 N  N   . ASP   A 1 198 ? 58.397 -23.848 -8.889  1.00 67.40  ?  213 ASP   A N   1 
ATOM   1536 C  CA  . ASP   A 1 198 ? 58.803 -24.591 -7.693  1.00 74.32  ?  213 ASP   A CA  1 
ATOM   1537 C  C   . ASP   A 1 198 ? 59.584 -25.859 -8.046  1.00 82.91  ?  213 ASP   A C   1 
ATOM   1538 O  O   . ASP   A 1 198 ? 60.526 -26.236 -7.340  1.00 91.18  ?  213 ASP   A O   1 
ATOM   1539 C  CB  . ASP   A 1 198 ? 57.571 -24.969 -6.852  1.00 67.76  ?  213 ASP   A CB  1 
ATOM   1540 C  CG  . ASP   A 1 198 ? 57.050 -23.823 -5.990  1.00 66.94  ?  213 ASP   A CG  1 
ATOM   1541 O  OD1 . ASP   A 1 198 ? 57.771 -22.827 -5.811  1.00 69.66  ?  213 ASP   A OD1 1 
ATOM   1542 O  OD2 . ASP   A 1 198 ? 55.906 -23.921 -5.483  1.00 66.34  ?  213 ASP   A OD2 1 
ATOM   1543 N  N   . LYS   A 1 199 ? 59.201 -26.535 -9.132  1.00 80.27  ?  214 LYS   A N   1 
ATOM   1544 C  CA  . LYS   A 1 199 ? 59.830 -27.805 -9.480  1.00 80.77  ?  214 LYS   A CA  1 
ATOM   1545 C  C   . LYS   A 1 199 ? 61.235 -27.597 -10.037 1.00 87.74  ?  214 LYS   A C   1 
ATOM   1546 O  O   . LYS   A 1 199 ? 62.174 -28.311 -9.661  1.00 96.96  ?  214 LYS   A O   1 
ATOM   1547 C  CB  . LYS   A 1 199 ? 58.956 -28.566 -10.483 1.00 84.89  ?  214 LYS   A CB  1 
ATOM   1548 C  CG  . LYS   A 1 199 ? 59.528 -29.907 -10.930 1.00 95.97  ?  214 LYS   A CG  1 
ATOM   1549 C  CD  . LYS   A 1 199 ? 59.278 -30.140 -12.426 1.00 104.89 ?  214 LYS   A CD  1 
ATOM   1550 C  CE  . LYS   A 1 199 ? 59.987 -31.400 -12.940 1.00 96.01  ?  214 LYS   A CE  1 
ATOM   1551 N  NZ  . LYS   A 1 199 ? 59.909 -31.543 -14.426 1.00 93.60  ?  214 LYS   A NZ  1 
ATOM   1552 N  N   . TYR   A 1 200 ? 61.397 -26.633 -10.946 1.00 88.30  ?  215 TYR   A N   1 
ATOM   1553 C  CA  . TYR   A 1 200 ? 62.704 -26.391 -11.546 1.00 91.90  ?  215 TYR   A CA  1 
ATOM   1554 C  C   . TYR   A 1 200 ? 63.627 -25.608 -10.618 1.00 95.50  ?  215 TYR   A C   1 
ATOM   1555 O  O   . TYR   A 1 200 ? 64.851 -25.769 -10.688 1.00 101.06 ?  215 TYR   A O   1 
ATOM   1556 C  CB  . TYR   A 1 200 ? 62.580 -25.619 -12.869 1.00 97.84  ?  215 TYR   A CB  1 
ATOM   1557 C  CG  . TYR   A 1 200 ? 61.834 -26.277 -14.033 1.00 118.13 ?  215 TYR   A CG  1 
ATOM   1558 C  CD1 . TYR   A 1 200 ? 60.914 -27.307 -13.836 1.00 112.77 ?  215 TYR   A CD1 1 
ATOM   1559 C  CD2 . TYR   A 1 200 ? 62.050 -25.840 -15.346 1.00 122.37 ?  215 TYR   A CD2 1 
ATOM   1560 C  CE1 . TYR   A 1 200 ? 60.233 -27.882 -14.915 1.00 112.82 ?  215 TYR   A CE1 1 
ATOM   1561 C  CE2 . TYR   A 1 200 ? 61.378 -26.413 -16.427 1.00 121.21 ?  215 TYR   A CE2 1 
ATOM   1562 C  CZ  . TYR   A 1 200 ? 60.471 -27.432 -16.205 1.00 121.35 ?  215 TYR   A CZ  1 
ATOM   1563 O  OH  . TYR   A 1 200 ? 59.799 -28.010 -17.263 1.00 118.83 ?  215 TYR   A OH  1 
ATOM   1564 N  N   . TYR   A 1 201 ? 63.071 -24.766 -9.738  1.00 91.83  ?  216 TYR   A N   1 
ATOM   1565 C  CA  . TYR   A 1 201 ? 63.860 -23.742 -9.064  1.00 97.35  ?  216 TYR   A CA  1 
ATOM   1566 C  C   . TYR   A 1 201 ? 63.711 -23.716 -7.546  1.00 104.75 ?  216 TYR   A C   1 
ATOM   1567 O  O   . TYR   A 1 201 ? 64.262 -22.809 -6.908  1.00 109.60 ?  216 TYR   A O   1 
ATOM   1568 C  CB  . TYR   A 1 201 ? 63.511 -22.357 -9.619  1.00 90.39  ?  216 TYR   A CB  1 
ATOM   1569 C  CG  . TYR   A 1 201 ? 63.912 -22.168 -11.059 1.00 91.42  ?  216 TYR   A CG  1 
ATOM   1570 C  CD1 . TYR   A 1 201 ? 65.248 -22.050 -11.412 1.00 102.50 ?  216 TYR   A CD1 1 
ATOM   1571 C  CD2 . TYR   A 1 201 ? 62.958 -22.104 -12.066 1.00 92.88  ?  216 TYR   A CD2 1 
ATOM   1572 C  CE1 . TYR   A 1 201 ? 65.627 -21.876 -12.724 1.00 106.62 ?  216 TYR   A CE1 1 
ATOM   1573 C  CE2 . TYR   A 1 201 ? 63.328 -21.930 -13.386 1.00 97.04  ?  216 TYR   A CE2 1 
ATOM   1574 C  CZ  . TYR   A 1 201 ? 64.664 -21.813 -13.705 1.00 104.03 ?  216 TYR   A CZ  1 
ATOM   1575 O  OH  . TYR   A 1 201 ? 65.053 -21.644 -15.011 1.00 110.63 ?  216 TYR   A OH  1 
ATOM   1576 N  N   . MET   A 1 202 ? 62.968 -24.655 -6.953  1.00 105.08 ?  217 MET   A N   1 
ATOM   1577 C  CA  . MET   A 1 202 ? 62.780 -24.738 -5.501  1.00 110.50 ?  217 MET   A CA  1 
ATOM   1578 C  C   . MET   A 1 202 ? 62.255 -23.434 -4.900  1.00 104.87 ?  217 MET   A C   1 
ATOM   1579 O  O   . MET   A 1 202 ? 62.170 -23.297 -3.671  1.00 93.26  ?  217 MET   A O   1 
ATOM   1580 C  CB  . MET   A 1 202 ? 64.088 -25.137 -4.804  1.00 107.31 ?  217 MET   A CB  1 
ATOM   1581 C  CG  . MET   A 1 202 ? 64.778 -26.372 -5.383  1.00 117.79 ?  217 MET   A CG  1 
ATOM   1582 S  SD  . MET   A 1 202 ? 63.783 -27.881 -5.358  1.00 154.35 ?  217 MET   A SD  1 
ATOM   1583 C  CE  . MET   A 1 202 ? 63.542 -28.130 -3.596  1.00 125.74 ?  217 MET   A CE  1 
ATOM   1584 N  N   . ALA   A 1 203 ? 61.881 -22.484 -5.757  1.00 93.60  ?  218 ALA   A N   1 
ATOM   1585 C  CA  . ALA   A 1 203 ? 61.535 -21.144 -5.320  1.00 80.65  ?  218 ALA   A CA  1 
ATOM   1586 C  C   . ALA   A 1 203 ? 60.671 -20.494 -6.383  1.00 81.20  ?  218 ALA   A C   1 
ATOM   1587 O  O   . ALA   A 1 203 ? 60.929 -20.647 -7.580  1.00 67.74  ?  218 ALA   A O   1 
ATOM   1588 C  CB  . ALA   A 1 203 ? 62.785 -20.294 -5.059  1.00 86.82  ?  218 ALA   A CB  1 
ATOM   1589 N  N   . SER   A 1 204 ? 59.651 -19.773 -5.933  1.00 61.11  ?  219 SER   A N   1 
ATOM   1590 C  CA  . SER   A 1 204 ? 58.706 -19.132 -6.820  1.00 70.26  ?  219 SER   A CA  1 
ATOM   1591 C  C   . SER   A 1 204 ? 58.199 -17.875 -6.140  1.00 74.72  ?  219 SER   A C   1 
ATOM   1592 O  O   . SER   A 1 204 ? 58.034 -17.856 -4.911  1.00 68.47  ?  219 SER   A O   1 
ATOM   1593 C  CB  . SER   A 1 204 ? 57.536 -20.060 -7.152  1.00 74.62  ?  219 SER   A CB  1 
ATOM   1594 O  OG  . SER   A 1 204 ? 57.116 -20.730 -5.976  1.00 72.12  ?  219 SER   A OG  1 
ATOM   1595 N  N   . PRO   A 1 205 ? 57.955 -16.816 -6.901  1.00 72.72  ?  220 PRO   A N   1 
ATOM   1596 C  CA  . PRO   A 1 205 ? 57.345 -15.609 -6.329  1.00 72.11  ?  220 PRO   A CA  1 
ATOM   1597 C  C   . PRO   A 1 205 ? 55.924 -15.867 -5.826  1.00 70.15  ?  220 PRO   A C   1 
ATOM   1598 O  O   . PRO   A 1 205 ? 55.176 -16.659 -6.404  1.00 55.67  ?  220 PRO   A O   1 
ATOM   1599 C  CB  . PRO   A 1 205 ? 57.338 -14.622 -7.514  1.00 49.10  ?  220 PRO   A CB  1 
ATOM   1600 C  CG  . PRO   A 1 205 ? 58.388 -15.160 -8.474  1.00 54.89  ?  220 PRO   A CG  1 
ATOM   1601 C  CD  . PRO   A 1 205 ? 58.359 -16.656 -8.310  1.00 54.48  ?  220 PRO   A CD  1 
ATOM   1602 N  N   . ASP   A 1 206 ? 55.553 -15.173 -4.739  1.00 54.48  ?  221 ASP   A N   1 
ATOM   1603 C  CA  . ASP   A 1 206 ? 54.154 -15.097 -4.321  1.00 58.52  ?  221 ASP   A CA  1 
ATOM   1604 C  C   . ASP   A 1 206 ? 53.353 -14.186 -5.261  1.00 62.04  ?  221 ASP   A C   1 
ATOM   1605 O  O   . ASP   A 1 206 ? 53.918 -13.480 -6.106  1.00 46.33  ?  221 ASP   A O   1 
ATOM   1606 C  CB  . ASP   A 1 206 ? 54.051 -14.591 -2.887  1.00 55.69  ?  221 ASP   A CB  1 
ATOM   1607 C  CG  . ASP   A 1 206 ? 54.831 -15.441 -1.942  1.00 60.13  ?  221 ASP   A CG  1 
ATOM   1608 O  OD1 . ASP   A 1 206 ? 54.834 -16.676 -2.142  1.00 76.18  ?  221 ASP   A OD1 1 
ATOM   1609 O  OD2 . ASP   A 1 206 ? 55.473 -14.875 -1.042  1.00 74.58  ?  221 ASP   A OD2 1 
ATOM   1610 N  N   . LEU   A 1 207 ? 52.019 -14.186 -5.089  1.00 49.33  ?  222 LEU   A N   1 
ATOM   1611 C  CA  . LEU   A 1 207 ? 51.105 -13.415 -5.935  1.00 47.56  ?  222 LEU   A CA  1 
ATOM   1612 C  C   . LEU   A 1 207 ? 50.322 -12.396 -5.115  1.00 51.91  ?  222 LEU   A C   1 
ATOM   1613 O  O   . LEU   A 1 207 ? 49.731 -12.752 -4.090  1.00 48.16  ?  222 LEU   A O   1 
ATOM   1614 C  CB  . LEU   A 1 207 ? 50.099 -14.327 -6.646  1.00 43.19  ?  222 LEU   A CB  1 
ATOM   1615 C  CG  . LEU   A 1 207 ? 48.990 -13.661 -7.456  1.00 50.76  ?  222 LEU   A CG  1 
ATOM   1616 C  CD1 . LEU   A 1 207 ? 49.595 -12.978 -8.673  1.00 41.05  ?  222 LEU   A CD1 1 
ATOM   1617 C  CD2 . LEU   A 1 207 ? 47.944 -14.691 -7.883  1.00 51.75  ?  222 LEU   A CD2 1 
ATOM   1618 N  N   . GLU   A 1 208 ? 50.292 -11.145 -5.584  1.00 41.75  ?  223 GLU   A N   1 
ATOM   1619 C  CA  . GLU   A 1 208 ? 49.396 -10.111 -5.065  1.00 43.53  ?  223 GLU   A CA  1 
ATOM   1620 C  C   . GLU   A 1 208 ? 48.423 -9.684  -6.156  1.00 45.42  ?  223 GLU   A C   1 
ATOM   1621 O  O   . GLU   A 1 208 ? 48.851 -9.308  -7.252  1.00 49.41  ?  223 GLU   A O   1 
ATOM   1622 C  CB  . GLU   A 1 208 ? 50.177 -8.889  -4.584  1.00 45.41  ?  223 GLU   A CB  1 
ATOM   1623 C  CG  . GLU   A 1 208 ? 51.166 -9.166  -3.461  1.00 59.45  ?  223 GLU   A CG  1 
ATOM   1624 C  CD  . GLU   A 1 208 ? 51.967 -7.924  -3.098  1.00 57.70  ?  223 GLU   A CD  1 
ATOM   1625 O  OE1 . GLU   A 1 208 ? 51.509 -6.802  -3.421  1.00 65.82  ?  223 GLU   A OE1 1 
ATOM   1626 O  OE2 . GLU   A 1 208 ? 53.050 -8.074  -2.503  1.00 70.90  ?  223 GLU   A OE2 1 
ATOM   1627 N  N   . ILE   A 1 209 ? 47.123 -9.730  -5.860  1.00 40.49  ?  224 ILE   A N   1 
ATOM   1628 C  CA  . ILE   A 1 209 ? 46.086 -9.296  -6.793  1.00 43.71  ?  224 ILE   A CA  1 
ATOM   1629 C  C   . ILE   A 1 209 ? 45.335 -8.130  -6.180  1.00 48.31  ?  224 ILE   A C   1 
ATOM   1630 O  O   . ILE   A 1 209 ? 45.020 -8.144  -4.989  1.00 45.02  ?  224 ILE   A O   1 
ATOM   1631 C  CB  . ILE   A 1 209 ? 45.088 -10.416 -7.157  1.00 50.84  ?  224 ILE   A CB  1 
ATOM   1632 C  CG1 . ILE   A 1 209 ? 45.803 -11.646 -7.694  1.00 54.95  ?  224 ILE   A CG1 1 
ATOM   1633 C  CG2 . ILE   A 1 209 ? 44.109 -9.936  -8.235  1.00 43.63  ?  224 ILE   A CG2 1 
ATOM   1634 C  CD1 . ILE   A 1 209 ? 44.842 -12.812 -7.972  1.00 56.36  ?  224 ILE   A CD1 1 
ATOM   1635 N  N   . GLN   A 1 210 ? 45.047 -7.129  -7.001  1.00 45.65  ?  225 GLN   A N   1 
ATOM   1636 C  CA  . GLN   A 1 210 ? 44.198 -6.009  -6.623  1.00 48.95  ?  225 GLN   A CA  1 
ATOM   1637 C  C   . GLN   A 1 210 ? 43.175 -5.807  -7.730  1.00 48.90  ?  225 GLN   A C   1 
ATOM   1638 O  O   . GLN   A 1 210 ? 43.509 -5.938  -8.906  1.00 45.47  ?  225 GLN   A O   1 
ATOM   1639 C  CB  . GLN   A 1 210 ? 45.023 -4.742  -6.417  1.00 49.76  ?  225 GLN   A CB  1 
ATOM   1640 C  CG  . GLN   A 1 210 ? 44.247 -3.530  -5.956  1.00 74.09  ?  225 GLN   A CG  1 
ATOM   1641 C  CD  . GLN   A 1 210 ? 45.170 -2.395  -5.570  1.00 86.25  ?  225 GLN   A CD  1 
ATOM   1642 O  OE1 . GLN   A 1 210 ? 46.390 -2.503  -5.720  1.00 89.60  ?  225 GLN   A OE1 1 
ATOM   1643 N  NE2 . GLN   A 1 210 ? 44.600 -1.303  -5.067  1.00 84.04  ?  225 GLN   A NE2 1 
ATOM   1644 N  N   . GLU   A 1 211 ? 41.935 -5.513  -7.360  1.00 45.90  ?  226 GLU   A N   1 
ATOM   1645 C  CA  . GLU   A 1 211 ? 40.871 -5.263  -8.324  1.00 46.42  ?  226 GLU   A CA  1 
ATOM   1646 C  C   . GLU   A 1 211 ? 40.418 -3.812  -8.207  1.00 55.17  ?  226 GLU   A C   1 
ATOM   1647 O  O   . GLU   A 1 211 ? 40.383 -3.263  -7.104  1.00 47.81  ?  226 GLU   A O   1 
ATOM   1648 C  CB  . GLU   A 1 211 ? 39.674 -6.198  -8.082  1.00 47.16  ?  226 GLU   A CB  1 
ATOM   1649 C  CG  . GLU   A 1 211 ? 39.868 -7.636  -8.556  1.00 44.73  ?  226 GLU   A CG  1 
ATOM   1650 C  CD  . GLU   A 1 211 ? 38.571 -8.430  -8.566  1.00 54.39  ?  226 GLU   A CD  1 
ATOM   1651 O  OE1 . GLU   A 1 211 ? 37.489 -7.841  -8.339  1.00 51.33  ?  226 GLU   A OE1 1 
ATOM   1652 O  OE2 . GLU   A 1 211 ? 38.629 -9.656  -8.801  1.00 57.94  ?  226 GLU   A OE2 1 
ATOM   1653 N  N   . ILE   A 1 212 ? 40.072 -3.190  -9.340  1.00 43.07  ?  227 ILE   A N   1 
ATOM   1654 C  CA  . ILE   A 1 212 ? 39.487 -1.839  -9.354  1.00 49.21  ?  227 ILE   A CA  1 
ATOM   1655 C  C   . ILE   A 1 212 ? 38.232 -1.900  -10.214 1.00 50.71  ?  227 ILE   A C   1 
ATOM   1656 O  O   . ILE   A 1 212 ? 38.315 -1.818  -11.446 1.00 44.35  ?  227 ILE   A O   1 
ATOM   1657 C  CB  . ILE   A 1 212 ? 40.443 -0.771  -9.903  1.00 43.44  ?  227 ILE   A CB  1 
ATOM   1658 C  CG1 . ILE   A 1 212 ? 41.805 -0.869  -9.230  1.00 54.03  ?  227 ILE   A CG1 1 
ATOM   1659 C  CG2 . ILE   A 1 212 ? 39.851 0.619   -9.651  1.00 46.82  ?  227 ILE   A CG2 1 
ATOM   1660 C  CD1 . ILE   A 1 212 ? 41.798 -0.318  -7.829  1.00 53.84  ?  227 ILE   A CD1 1 
ATOM   1661 N  N   . ASN   A 1 213 ? 37.074 -2.018  -9.586  1.00 46.18  ?  228 ASN   A N   1 
ATOM   1662 C  CA  . ASN   A 1 213 ? 35.807 -2.023  -10.313 1.00 49.15  ?  228 ASN   A CA  1 
ATOM   1663 C  C   . ASN   A 1 213 ? 35.278 -0.599  -10.252 1.00 52.54  ?  228 ASN   A C   1 
ATOM   1664 O  O   . ASN   A 1 213 ? 34.580 -0.230  -9.306  1.00 52.02  ?  228 ASN   A O   1 
ATOM   1665 C  CB  . ASN   A 1 213 ? 34.826 -3.029  -9.714  1.00 49.28  ?  228 ASN   A CB  1 
ATOM   1666 C  CG  . ASN   A 1 213 ? 33.540 -3.140  -10.514 1.00 50.14  ?  228 ASN   A CG  1 
ATOM   1667 O  OD1 . ASN   A 1 213 ? 33.132 -2.204  -11.206 1.00 56.44  ?  228 ASN   A OD1 1 
ATOM   1668 N  ND2 . ASN   A 1 213 ? 32.898 -4.293  -10.433 1.00 48.82  ?  228 ASN   A ND2 1 
ATOM   1669 N  N   . ALA   A 1 214 ? 35.585 0.191   -11.287 1.00 52.46  ?  229 ALA   A N   1 
ATOM   1670 C  CA  . ALA   A 1 214 ? 35.378 1.638   -11.216 1.00 52.27  ?  229 ALA   A CA  1 
ATOM   1671 C  C   . ALA   A 1 214 ? 33.920 2.000   -10.947 1.00 57.31  ?  229 ALA   A C   1 
ATOM   1672 O  O   . ALA   A 1 214 ? 33.632 2.876   -10.117 1.00 56.63  ?  229 ALA   A O   1 
ATOM   1673 C  CB  . ALA   A 1 214 ? 35.870 2.296   -12.510 1.00 48.30  ?  229 ALA   A CB  1 
ATOM   1674 N  N   . ALA   A 1 215 ? 32.982 1.336   -11.631 1.00 56.67  ?  230 ALA   A N   1 
ATOM   1675 C  CA  . ALA   A 1 215 ? 31.575 1.688   -11.466 1.00 63.85  ?  230 ALA   A CA  1 
ATOM   1676 C  C   . ALA   A 1 215 ? 31.000 1.149   -10.158 1.00 61.14  ?  230 ALA   A C   1 
ATOM   1677 O  O   . ALA   A 1 215 ? 30.168 1.808   -9.540  1.00 63.07  ?  230 ALA   A O   1 
ATOM   1678 C  CB  . ALA   A 1 215 ? 30.760 1.179   -12.658 1.00 56.70  ?  230 ALA   A CB  1 
ATOM   1679 N  N   . ASN   A 1 216 ? 31.419 -0.051  -9.718  1.00 66.16  ?  231 ASN   A N   1 
ATOM   1680 C  CA  . ASN   A 1 216 ? 30.863 -0.706  -8.520  1.00 66.69  ?  231 ASN   A CA  1 
ATOM   1681 C  C   . ASN   A 1 216 ? 32.013 -1.236  -7.662  1.00 62.06  ?  231 ASN   A C   1 
ATOM   1682 O  O   . ASN   A 1 216 ? 32.357 -2.418  -7.734  1.00 61.56  ?  231 ASN   A O   1 
ATOM   1683 C  CB  . ASN   A 1 216 ? 29.907 -1.819  -8.922  1.00 70.66  ?  231 ASN   A CB  1 
ATOM   1684 C  CG  . ASN   A 1 216 ? 28.784 -1.326  -9.801  1.00 75.06  ?  231 ASN   A CG  1 
ATOM   1685 O  OD1 . ASN   A 1 216 ? 27.790 -0.788  -9.311  1.00 79.56  ?  231 ASN   A OD1 1 
ATOM   1686 N  ND2 . ASN   A 1 216 ? 28.932 -1.508  -11.110 1.00 61.71  ?  231 ASN   A ND2 1 
ATOM   1687 N  N   . SER   A 1 217 ? 32.577 -0.368  -6.815  1.00 66.85  ?  232 SER   A N   1 
ATOM   1688 C  CA  . SER   A 1 217 ? 33.883 -0.643  -6.214  1.00 68.88  ?  232 SER   A CA  1 
ATOM   1689 C  C   . SER   A 1 217 ? 33.886 -1.843  -5.268  1.00 76.09  ?  232 SER   A C   1 
ATOM   1690 O  O   . SER   A 1 217 ? 34.954 -2.405  -5.001  1.00 61.65  ?  232 SER   A O   1 
ATOM   1691 C  CB  . SER   A 1 217 ? 34.387 0.594   -5.473  1.00 66.48  ?  232 SER   A CB  1 
ATOM   1692 O  OG  . SER   A 1 217 ? 33.498 0.950   -4.442  1.00 77.95  ?  232 SER   A OG  1 
ATOM   1693 N  N   . LYS   A 1 218 ? 32.743 -2.255  -4.743  1.00 84.90  ?  233 LYS   A N   1 
ATOM   1694 C  CA  . LYS   A 1 218 ? 32.757 -3.431  -3.887  1.00 81.70  ?  233 LYS   A CA  1 
ATOM   1695 C  C   . LYS   A 1 218 ? 32.431 -4.721  -4.637  1.00 76.45  ?  233 LYS   A C   1 
ATOM   1696 O  O   . LYS   A 1 218 ? 32.453 -5.793  -4.029  1.00 84.68  ?  233 LYS   A O   1 
ATOM   1697 C  CB  . LYS   A 1 218 ? 31.792 -3.229  -2.709  1.00 89.59  ?  233 LYS   A CB  1 
ATOM   1698 C  CG  . LYS   A 1 218 ? 32.329 -2.261  -1.651  1.00 87.47  ?  233 LYS   A CG  1 
ATOM   1699 C  CD  . LYS   A 1 218 ? 31.218 -1.652  -0.804  1.00 108.06 ?  233 LYS   A CD  1 
ATOM   1700 C  CE  . LYS   A 1 218 ? 30.447 -0.588  -1.578  1.00 109.73 ?  233 LYS   A CE  1 
ATOM   1701 N  NZ  . LYS   A 1 218 ? 29.436 0.112   -0.729  1.00 104.42 ?  233 LYS   A NZ  1 
ATOM   1702 N  N   . GLN   A 1 219 ? 32.168 -4.655  -5.946  1.00 65.40  ?  234 GLN   A N   1 
ATOM   1703 C  CA  . GLN   A 1 219 ? 31.676 -5.855  -6.612  1.00 61.46  ?  234 GLN   A CA  1 
ATOM   1704 C  C   . GLN   A 1 219 ? 32.817 -6.613  -7.275  1.00 60.29  ?  234 GLN   A C   1 
ATOM   1705 O  O   . GLN   A 1 219 ? 33.651 -5.994  -7.953  1.00 58.61  ?  234 GLN   A O   1 
ATOM   1706 C  CB  . GLN   A 1 219 ? 30.623 -5.493  -7.656  1.00 60.51  ?  234 GLN   A CB  1 
ATOM   1707 C  CG  . GLN   A 1 219 ? 29.297 -5.004  -7.062  1.00 81.38  ?  234 GLN   A CG  1 
ATOM   1708 C  CD  . GLN   A 1 219 ? 28.171 -4.985  -8.089  1.00 91.91  ?  234 GLN   A CD  1 
ATOM   1709 O  OE1 . GLN   A 1 219 ? 28.418 -4.916  -9.300  1.00 88.69  ?  234 GLN   A OE1 1 
ATOM   1710 N  NE2 . GLN   A 1 219 ? 26.930 -5.058  -7.611  1.00 90.10  ?  234 GLN   A NE2 1 
ATOM   1711 N  N   . PRO   A 1 220 ? 32.892 -7.933  -7.099  1.00 59.86  ?  235 PRO   A N   1 
ATOM   1712 C  CA  . PRO   A 1 220 ? 33.921 -8.704  -7.806  1.00 57.34  ?  235 PRO   A CA  1 
ATOM   1713 C  C   . PRO   A 1 220 ? 33.768 -8.546  -9.312  1.00 56.77  ?  235 PRO   A C   1 
ATOM   1714 O  O   . PRO   A 1 220 ? 32.656 -8.455  -9.833  1.00 58.80  ?  235 PRO   A O   1 
ATOM   1715 C  CB  . PRO   A 1 220 ? 33.673 -10.151 -7.360  1.00 59.97  ?  235 PRO   A CB  1 
ATOM   1716 C  CG  . PRO   A 1 220 ? 32.345 -10.135 -6.644  1.00 66.92  ?  235 PRO   A CG  1 
ATOM   1717 C  CD  . PRO   A 1 220 ? 32.131 -8.750  -6.137  1.00 60.63  ?  235 PRO   A CD  1 
ATOM   1718 N  N   . ILE   A 1 221 ? 34.897 -8.497  -10.010 1.00 45.53  ?  236 ILE   A N   1 
ATOM   1719 C  CA  . ILE   A 1 221 ? 34.883 -8.206  -11.436 1.00 47.88  ?  236 ILE   A CA  1 
ATOM   1720 C  C   . ILE   A 1 221 ? 34.618 -9.504  -12.192 1.00 52.15  ?  236 ILE   A C   1 
ATOM   1721 O  O   . ILE   A 1 221 ? 35.388 -10.468 -12.082 1.00 46.55  ?  236 ILE   A O   1 
ATOM   1722 C  CB  . ILE   A 1 221 ? 36.202 -7.548  -11.870 1.00 44.93  ?  236 ILE   A CB  1 
ATOM   1723 C  CG1 . ILE   A 1 221 ? 36.333 -6.152  -11.222 1.00 41.76  ?  236 ILE   A CG1 1 
ATOM   1724 C  CG2 . ILE   A 1 221 ? 36.324 -7.476  -13.413 1.00 43.34  ?  236 ILE   A CG2 1 
ATOM   1725 C  CD1 . ILE   A 1 221 ? 37.700 -5.532  -11.442 1.00 40.93  ?  236 ILE   A CD1 1 
ATOM   1726 N  N   A HIS   A 1 222 ? 33.515 -9.539  -12.939 0.52 50.00  ?  237 HIS   A N   1 
ATOM   1727 N  N   B HIS   A 1 222 ? 33.510 -9.538  -12.936 0.48 49.99  ?  237 HIS   A N   1 
ATOM   1728 C  CA  A HIS   A 1 222 ? 33.189 -10.631 -13.849 0.52 49.94  ?  237 HIS   A CA  1 
ATOM   1729 C  CA  B HIS   A 1 222 ? 33.198 -10.621 -13.861 0.48 49.93  ?  237 HIS   A CA  1 
ATOM   1730 C  C   A HIS   A 1 222 ? 33.031 -10.065 -15.257 0.52 47.32  ?  237 HIS   A C   1 
ATOM   1731 C  C   B HIS   A 1 222 ? 33.018 -10.059 -15.265 0.48 47.33  ?  237 HIS   A C   1 
ATOM   1732 O  O   A HIS   A 1 222 ? 32.798 -8.869  -15.437 0.52 49.22  ?  237 HIS   A O   1 
ATOM   1733 O  O   B HIS   A 1 222 ? 32.773 -8.866  -15.448 0.48 49.22  ?  237 HIS   A O   1 
ATOM   1734 C  CB  A HIS   A 1 222 ? 31.893 -11.364 -13.440 0.52 46.18  ?  237 HIS   A CB  1 
ATOM   1735 C  CB  B HIS   A 1 222 ? 31.935 -11.405 -13.443 0.48 46.21  ?  237 HIS   A CB  1 
ATOM   1736 C  CG  A HIS   A 1 222 ? 31.946 -12.033 -12.093 0.52 54.63  ?  237 HIS   A CG  1 
ATOM   1737 C  CG  B HIS   A 1 222 ? 30.809 -10.556 -12.930 0.48 52.27  ?  237 HIS   A CG  1 
ATOM   1738 N  ND1 A HIS   A 1 222 ? 32.283 -11.367 -10.934 0.52 57.56  ?  237 HIS   A ND1 1 
ATOM   1739 N  ND1 B HIS   A 1 222 ? 29.824 -10.043 -13.747 0.48 55.69  ?  237 HIS   A ND1 1 
ATOM   1740 C  CD2 A HIS   A 1 222 ? 31.650 -13.302 -11.719 0.52 50.60  ?  237 HIS   A CD2 1 
ATOM   1741 C  CD2 B HIS   A 1 222 ? 30.490 -10.169 -11.671 0.48 49.98  ?  237 HIS   A CD2 1 
ATOM   1742 C  CE1 A HIS   A 1 222 ? 32.216 -12.200 -9.909  0.52 48.88  ?  237 HIS   A CE1 1 
ATOM   1743 C  CE1 B HIS   A 1 222 ? 28.960 -9.358  -13.016 0.48 55.28  ?  237 HIS   A CE1 1 
ATOM   1744 N  NE2 A HIS   A 1 222 ? 31.833 -13.379 -10.358 0.52 46.58  ?  237 HIS   A NE2 1 
ATOM   1745 N  NE2 B HIS   A 1 222 ? 29.342 -9.418  -11.753 0.48 53.31  ?  237 HIS   A NE2 1 
ATOM   1746 N  N   . MET   A 1 223 ? 33.146 -10.936 -16.259 1.00 47.13  ?  238 MET   A N   1 
ATOM   1747 C  CA  . MET   A 1 223 ? 32.939 -10.552 -17.655 1.00 44.26  ?  238 MET   A CA  1 
ATOM   1748 C  C   . MET   A 1 223 ? 32.462 -11.765 -18.444 1.00 46.38  ?  238 MET   A C   1 
ATOM   1749 O  O   . MET   A 1 223 ? 32.542 -12.904 -17.982 1.00 43.91  ?  238 MET   A O   1 
ATOM   1750 C  CB  . MET   A 1 223 ? 34.223 -10.010 -18.308 1.00 39.94  ?  238 MET   A CB  1 
ATOM   1751 C  CG  . MET   A 1 223 ? 35.300 -11.072 -18.467 1.00 41.72  ?  238 MET   A CG  1 
ATOM   1752 S  SD  . MET   A 1 223 ? 36.828 -10.530 -19.232 1.00 44.79  ?  238 MET   A SD  1 
ATOM   1753 C  CE  . MET   A 1 223 ? 36.236 -9.619  -20.683 1.00 39.04  ?  238 MET   A CE  1 
ATOM   1754 N  N   . VAL   A 1 224 ? 31.990 -11.513 -19.662 1.00 47.44  ?  239 VAL   A N   1 
ATOM   1755 C  CA  . VAL   A 1 224 ? 31.761 -12.572 -20.637 1.00 47.64  ?  239 VAL   A CA  1 
ATOM   1756 C  C   . VAL   A 1 224 ? 33.062 -12.780 -21.414 1.00 52.90  ?  239 VAL   A C   1 
ATOM   1757 O  O   . VAL   A 1 224 ? 33.552 -11.857 -22.077 1.00 47.84  ?  239 VAL   A O   1 
ATOM   1758 C  CB  . VAL   A 1 224 ? 30.596 -12.213 -21.575 1.00 46.51  ?  239 VAL   A CB  1 
ATOM   1759 C  CG1 . VAL   A 1 224 ? 30.352 -13.328 -22.576 1.00 46.57  ?  239 VAL   A CG1 1 
ATOM   1760 C  CG2 . VAL   A 1 224 ? 29.313 -11.913 -20.769 1.00 45.62  ?  239 VAL   A CG2 1 
ATOM   1761 N  N   . TYR   A 1 225 ? 33.644 -13.980 -21.335 1.00 44.84  ?  240 TYR   A N   1 
ATOM   1762 C  CA  . TYR   A 1 225 ? 34.878 -14.215 -22.083 1.00 44.10  ?  240 TYR   A CA  1 
ATOM   1763 C  C   . TYR   A 1 225 ? 35.045 -15.711 -22.346 1.00 42.74  ?  240 TYR   A C   1 
ATOM   1764 O  O   . TYR   A 1 225 ? 34.220 -16.530 -21.935 1.00 42.48  ?  240 TYR   A O   1 
ATOM   1765 C  CB  . TYR   A 1 225 ? 36.102 -13.617 -21.363 1.00 40.83  ?  240 TYR   A CB  1 
ATOM   1766 C  CG  . TYR   A 1 225 ? 37.241 -13.362 -22.337 1.00 39.85  ?  240 TYR   A CG  1 
ATOM   1767 C  CD1 . TYR   A 1 225 ? 37.122 -12.383 -23.332 1.00 39.81  ?  240 TYR   A CD1 1 
ATOM   1768 C  CD2 . TYR   A 1 225 ? 38.413 -14.129 -22.309 1.00 37.31  ?  240 TYR   A CD2 1 
ATOM   1769 C  CE1 . TYR   A 1 225 ? 38.147 -12.160 -24.252 1.00 36.92  ?  240 TYR   A CE1 1 
ATOM   1770 C  CE2 . TYR   A 1 225 ? 39.443 -13.917 -23.229 1.00 34.34  ?  240 TYR   A CE2 1 
ATOM   1771 C  CZ  . TYR   A 1 225 ? 39.305 -12.933 -24.201 1.00 35.86  ?  240 TYR   A CZ  1 
ATOM   1772 O  OH  . TYR   A 1 225 ? 40.310 -12.710 -25.132 1.00 39.42  ?  240 TYR   A OH  1 
ATOM   1773 N  N   . VAL   A 1 226 ? 36.096 -16.049 -23.095 1.00 42.79  ?  241 VAL   A N   1 
ATOM   1774 C  CA  . VAL   A 1 226 ? 36.553 -17.425 -23.317 1.00 42.99  ?  241 VAL   A CA  1 
ATOM   1775 C  C   . VAL   A 1 226 ? 37.660 -17.713 -22.306 1.00 39.05  ?  241 VAL   A C   1 
ATOM   1776 O  O   . VAL   A 1 226 ? 38.834 -17.420 -22.581 1.00 37.81  ?  241 VAL   A O   1 
ATOM   1777 C  CB  . VAL   A 1 226 ? 37.088 -17.637 -24.743 1.00 45.69  ?  241 VAL   A CB  1 
ATOM   1778 C  CG1 . VAL   A 1 226 ? 37.467 -19.105 -24.955 1.00 43.53  ?  241 VAL   A CG1 1 
ATOM   1779 C  CG2 . VAL   A 1 226 ? 36.071 -17.185 -25.800 1.00 47.96  ?  241 VAL   A CG2 1 
ATOM   1780 N  N   . PRO   A 1 227 ? 37.357 -18.297 -21.152 1.00 39.79  ?  242 PRO   A N   1 
ATOM   1781 C  CA  . PRO   A 1 227 ? 38.384 -18.376 -20.094 1.00 41.30  ?  242 PRO   A CA  1 
ATOM   1782 C  C   . PRO   A 1 227 ? 39.600 -19.227 -20.463 1.00 36.55  ?  242 PRO   A C   1 
ATOM   1783 O  O   . PRO   A 1 227 ? 40.703 -18.939 -19.982 1.00 38.51  ?  242 PRO   A O   1 
ATOM   1784 C  CB  . PRO   A 1 227 ? 37.609 -18.943 -18.896 1.00 37.21  ?  242 PRO   A CB  1 
ATOM   1785 C  CG  . PRO   A 1 227 ? 36.369 -19.552 -19.479 1.00 44.92  ?  242 PRO   A CG  1 
ATOM   1786 C  CD  . PRO   A 1 227 ? 36.039 -18.754 -20.693 1.00 39.75  ?  242 PRO   A CD  1 
ATOM   1787 N  N   . SER   A 1 228 ? 39.464 -20.235 -21.328 1.00 36.72  ?  243 SER   A N   1 
ATOM   1788 C  CA  . SER   A 1 228 ? 40.662 -20.970 -21.731 1.00 36.13  ?  243 SER   A CA  1 
ATOM   1789 C  C   . SER   A 1 228 ? 41.655 -20.066 -22.473 1.00 38.00  ?  243 SER   A C   1 
ATOM   1790 O  O   . SER   A 1 228 ? 42.870 -20.210 -22.289 1.00 38.16  ?  243 SER   A O   1 
ATOM   1791 C  CB  . SER   A 1 228 ? 40.282 -22.178 -22.590 1.00 42.19  ?  243 SER   A CB  1 
ATOM   1792 O  OG  . SER   A 1 228 ? 39.654 -21.726 -23.775 1.00 45.43  ?  243 SER   A OG  1 
ATOM   1793 N  N   . HIS   A 1 229 ? 41.173 -19.114 -23.289 1.00 38.90  ?  244 HIS   A N   1 
ATOM   1794 C  CA  . HIS   A 1 229 ? 42.092 -18.152 -23.909 1.00 34.68  ?  244 HIS   A CA  1 
ATOM   1795 C  C   . HIS   A 1 229 ? 42.761 -17.281 -22.862 1.00 41.04  ?  244 HIS   A C   1 
ATOM   1796 O  O   . HIS   A 1 229 ? 43.960 -16.995 -22.962 1.00 36.28  ?  244 HIS   A O   1 
ATOM   1797 C  CB  . HIS   A 1 229 ? 41.369 -17.256 -24.907 1.00 33.47  ?  244 HIS   A CB  1 
ATOM   1798 C  CG  . HIS   A 1 229 ? 40.866 -17.976 -26.122 1.00 34.68  ?  244 HIS   A CG  1 
ATOM   1799 N  ND1 . HIS   A 1 229 ? 40.306 -17.320 -27.198 1.00 45.00  ?  244 HIS   A ND1 1 
ATOM   1800 C  CD2 . HIS   A 1 229 ? 40.817 -19.295 -26.420 1.00 43.38  ?  244 HIS   A CD2 1 
ATOM   1801 C  CE1 . HIS   A 1 229 ? 39.953 -18.206 -28.120 1.00 44.64  ?  244 HIS   A CE1 1 
ATOM   1802 N  NE2 . HIS   A 1 229 ? 40.244 -19.414 -27.668 1.00 48.71  ?  244 HIS   A NE2 1 
ATOM   1803 N  N   . LEU   A 1 230 ? 41.989 -16.828 -21.872 1.00 36.82  ?  245 LEU   A N   1 
ATOM   1804 C  CA  . LEU   A 1 230 ? 42.526 -15.951 -20.834 1.00 38.01  ?  245 LEU   A CA  1 
ATOM   1805 C  C   . LEU   A 1 230 ? 43.547 -16.683 -19.962 1.00 33.25  ?  245 LEU   A C   1 
ATOM   1806 O  O   . LEU   A 1 230 ? 44.612 -16.134 -19.646 1.00 34.70  ?  245 LEU   A O   1 
ATOM   1807 C  CB  . LEU   A 1 230 ? 41.381 -15.395 -19.984 1.00 35.94  ?  245 LEU   A CB  1 
ATOM   1808 C  CG  . LEU   A 1 230 ? 41.793 -14.542 -18.777 1.00 34.87  ?  245 LEU   A CG  1 
ATOM   1809 C  CD1 . LEU   A 1 230 ? 42.578 -13.321 -19.227 1.00 33.65  ?  245 LEU   A CD1 1 
ATOM   1810 C  CD2 . LEU   A 1 230 ? 40.575 -14.113 -17.910 1.00 36.70  ?  245 LEU   A CD2 1 
ATOM   1811 N  N   . TYR   A 1 231 ? 43.246 -17.925 -19.585 1.00 33.38  ?  246 TYR   A N   1 
ATOM   1812 C  CA  . TYR   A 1 231 ? 44.203 -18.756 -18.848 1.00 38.63  ?  246 TYR   A CA  1 
ATOM   1813 C  C   . TYR   A 1 231 ? 45.512 -18.911 -19.619 1.00 37.46  ?  246 TYR   A C   1 
ATOM   1814 O  O   . TYR   A 1 231 ? 46.599 -18.789 -19.040 1.00 39.92  ?  246 TYR   A O   1 
ATOM   1815 C  CB  . TYR   A 1 231 ? 43.587 -20.128 -18.555 1.00 34.93  ?  246 TYR   A CB  1 
ATOM   1816 C  CG  . TYR   A 1 231 ? 44.406 -21.097 -17.685 1.00 40.21  ?  246 TYR   A CG  1 
ATOM   1817 C  CD1 . TYR   A 1 231 ? 45.431 -21.875 -18.231 1.00 44.08  ?  246 TYR   A CD1 1 
ATOM   1818 C  CD2 . TYR   A 1 231 ? 44.119 -21.262 -16.330 1.00 40.22  ?  246 TYR   A CD2 1 
ATOM   1819 C  CE1 . TYR   A 1 231 ? 46.167 -22.777 -17.437 1.00 45.33  ?  246 TYR   A CE1 1 
ATOM   1820 C  CE2 . TYR   A 1 231 ? 44.838 -22.159 -15.538 1.00 43.34  ?  246 TYR   A CE2 1 
ATOM   1821 C  CZ  . TYR   A 1 231 ? 45.864 -22.908 -16.094 1.00 51.27  ?  246 TYR   A CZ  1 
ATOM   1822 O  OH  . TYR   A 1 231 ? 46.568 -23.806 -15.299 1.00 51.10  ?  246 TYR   A OH  1 
ATOM   1823 N  N   . HIS   A 1 232 ? 45.432 -19.211 -20.921 1.00 39.74  ?  247 HIS   A N   1 
ATOM   1824 C  CA  . HIS   A 1 232 ? 46.644 -19.408 -21.720 1.00 37.43  ?  247 HIS   A CA  1 
ATOM   1825 C  C   . HIS   A 1 232 ? 47.529 -18.162 -21.708 1.00 35.59  ?  247 HIS   A C   1 
ATOM   1826 O  O   . HIS   A 1 232 ? 48.747 -18.251 -21.488 1.00 35.80  ?  247 HIS   A O   1 
ATOM   1827 C  CB  . HIS   A 1 232 ? 46.280 -19.766 -23.170 1.00 40.44  ?  247 HIS   A CB  1 
ATOM   1828 C  CG  . HIS   A 1 232 ? 47.476 -19.981 -24.053 1.00 57.58  ?  247 HIS   A CG  1 
ATOM   1829 N  ND1 . HIS   A 1 232 ? 48.224 -21.142 -24.022 1.00 61.59  ?  247 HIS   A ND1 1 
ATOM   1830 C  CD2 . HIS   A 1 232 ? 48.060 -19.182 -24.983 1.00 54.57  ?  247 HIS   A CD2 1 
ATOM   1831 C  CE1 . HIS   A 1 232 ? 49.204 -21.056 -24.909 1.00 59.04  ?  247 HIS   A CE1 1 
ATOM   1832 N  NE2 . HIS   A 1 232 ? 49.129 -19.878 -25.504 1.00 51.89  ?  247 HIS   A NE2 1 
ATOM   1833 N  N   . MET   A 1 233 ? 46.928 -16.989 -21.949 1.00 33.23  ?  248 MET   A N   1 
ATOM   1834 C  CA  . MET   A 1 233 ? 47.679 -15.731 -21.946 1.00 33.84  ?  248 MET   A CA  1 
ATOM   1835 C  C   . MET   A 1 233 ? 48.340 -15.478 -20.601 1.00 36.02  ?  248 MET   A C   1 
ATOM   1836 O  O   . MET   A 1 233 ? 49.528 -15.137 -20.527 1.00 37.93  ?  248 MET   A O   1 
ATOM   1837 C  CB  . MET   A 1 233 ? 46.755 -14.557 -22.297 1.00 34.70  ?  248 MET   A CB  1 
ATOM   1838 C  CG  . MET   A 1 233 ? 46.132 -14.666 -23.679 1.00 40.59  ?  248 MET   A CG  1 
ATOM   1839 S  SD  . MET   A 1 233 ? 45.259 -13.134 -24.111 1.00 44.56  ?  248 MET   A SD  1 
ATOM   1840 C  CE  . MET   A 1 233 ? 43.920 -13.148 -22.960 1.00 41.62  ?  248 MET   A CE  1 
ATOM   1841 N  N   . LEU   A 1 234 ? 47.568 -15.601 -19.519 1.00 35.70  ?  249 LEU   A N   1 
ATOM   1842 C  CA  . LEU   A 1 234 ? 48.119 -15.396 -18.178 1.00 37.72  ?  249 LEU   A CA  1 
ATOM   1843 C  C   . LEU   A 1 234 ? 49.233 -16.393 -17.868 1.00 37.48  ?  249 LEU   A C   1 
ATOM   1844 O  O   . LEU   A 1 234 ? 50.270 -16.022 -17.309 1.00 38.01  ?  249 LEU   A O   1 
ATOM   1845 C  CB  . LEU   A 1 234 ? 46.995 -15.500 -17.136 1.00 36.73  ?  249 LEU   A CB  1 
ATOM   1846 C  CG  . LEU   A 1 234 ? 45.987 -14.336 -17.226 1.00 38.00  ?  249 LEU   A CG  1 
ATOM   1847 C  CD1 . LEU   A 1 234 ? 44.682 -14.602 -16.414 1.00 38.46  ?  249 LEU   A CD1 1 
ATOM   1848 C  CD2 . LEU   A 1 234 ? 46.663 -13.047 -16.735 1.00 36.41  ?  249 LEU   A CD2 1 
ATOM   1849 N  N   . PHE   A 1 235 ? 49.019 -17.671 -18.182 1.00 36.61  ?  250 PHE   A N   1 
ATOM   1850 C  CA  . PHE   A 1 235 ? 50.031 -18.681 -17.890 1.00 33.40  ?  250 PHE   A CA  1 
ATOM   1851 C  C   . PHE   A 1 235 ? 51.330 -18.365 -18.618 1.00 35.98  ?  250 PHE   A C   1 
ATOM   1852 O  O   . PHE   A 1 235 ? 52.425 -18.507 -18.060 1.00 37.29  ?  250 PHE   A O   1 
ATOM   1853 C  CB  . PHE   A 1 235 ? 49.500 -20.051 -18.294 1.00 34.59  ?  250 PHE   A CB  1 
ATOM   1854 C  CG  . PHE   A 1 235 ? 50.490 -21.158 -18.168 1.00 41.18  ?  250 PHE   A CG  1 
ATOM   1855 C  CD1 . PHE   A 1 235 ? 50.892 -21.614 -16.915 1.00 37.12  ?  250 PHE   A CD1 1 
ATOM   1856 C  CD2 . PHE   A 1 235 ? 51.012 -21.761 -19.304 1.00 44.05  ?  250 PHE   A CD2 1 
ATOM   1857 C  CE1 . PHE   A 1 235 ? 51.799 -22.643 -16.798 1.00 47.41  ?  250 PHE   A CE1 1 
ATOM   1858 C  CE2 . PHE   A 1 235 ? 51.919 -22.808 -19.195 1.00 46.97  ?  250 PHE   A CE2 1 
ATOM   1859 C  CZ  . PHE   A 1 235 ? 52.324 -23.241 -17.938 1.00 44.63  ?  250 PHE   A CZ  1 
ATOM   1860 N  N   . GLU   A 1 236 ? 51.224 -17.945 -19.875 1.00 35.54  ?  251 GLU   A N   1 
ATOM   1861 C  CA  . GLU   A 1 236 ? 52.416 -17.617 -20.643 1.00 39.54  ?  251 GLU   A CA  1 
ATOM   1862 C  C   . GLU   A 1 236 ? 53.150 -16.446 -20.006 1.00 37.70  ?  251 GLU   A C   1 
ATOM   1863 O  O   . GLU   A 1 236 ? 54.371 -16.497 -19.829 1.00 34.99  ?  251 GLU   A O   1 
ATOM   1864 C  CB  . GLU   A 1 236 ? 52.012 -17.325 -22.100 1.00 37.94  ?  251 GLU   A CB  1 
ATOM   1865 C  CG  . GLU   A 1 236 ? 53.059 -17.631 -23.131 1.00 51.47  ?  251 GLU   A CG  1 
ATOM   1866 C  CD  . GLU   A 1 236 ? 53.480 -19.097 -23.180 1.00 42.29  ?  251 GLU   A CD  1 
ATOM   1867 O  OE1 . GLU   A 1 236 ? 52.638 -20.013 -22.981 1.00 53.94  ?  251 GLU   A OE1 1 
ATOM   1868 O  OE2 . GLU   A 1 236 ? 54.678 -19.328 -23.426 1.00 58.12  ?  251 GLU   A OE2 1 
ATOM   1869 N  N   . LEU   A 1 237 ? 52.413 -15.407 -19.586 1.00 32.78  ?  252 LEU   A N   1 
ATOM   1870 C  CA  . LEU   A 1 237 ? 53.045 -14.265 -18.926 1.00 32.58  ?  252 LEU   A CA  1 
ATOM   1871 C  C   . LEU   A 1 237 ? 53.648 -14.641 -17.572 1.00 35.27  ?  252 LEU   A C   1 
ATOM   1872 O  O   . LEU   A 1 237 ? 54.764 -14.217 -17.246 1.00 36.80  ?  252 LEU   A O   1 
ATOM   1873 C  CB  . LEU   A 1 237 ? 52.038 -13.123 -18.775 1.00 31.04  ?  252 LEU   A CB  1 
ATOM   1874 C  CG  . LEU   A 1 237 ? 51.544 -12.557 -20.126 1.00 35.94  ?  252 LEU   A CG  1 
ATOM   1875 C  CD1 . LEU   A 1 237 ? 50.395 -11.599 -19.897 1.00 36.12  ?  252 LEU   A CD1 1 
ATOM   1876 C  CD2 . LEU   A 1 237 ? 52.648 -11.859 -20.945 1.00 36.92  ?  252 LEU   A CD2 1 
ATOM   1877 N  N   . PHE   A 1 238 ? 52.933 -15.431 -16.764 1.00 36.21  ?  253 PHE   A N   1 
ATOM   1878 C  CA  . PHE   A 1 238 ? 53.453 -15.837 -15.458 1.00 36.68  ?  253 PHE   A CA  1 
ATOM   1879 C  C   . PHE   A 1 238 ? 54.748 -16.649 -15.587 1.00 37.87  ?  253 PHE   A C   1 
ATOM   1880 O  O   . PHE   A 1 238 ? 55.692 -16.428 -14.824 1.00 38.99  ?  253 PHE   A O   1 
ATOM   1881 C  CB  . PHE   A 1 238 ? 52.392 -16.636 -14.688 1.00 36.40  ?  253 PHE   A CB  1 
ATOM   1882 C  CG  . PHE   A 1 238 ? 51.401 -15.794 -13.905 1.00 36.71  ?  253 PHE   A CG  1 
ATOM   1883 C  CD1 . PHE   A 1 238 ? 51.838 -14.877 -12.940 1.00 36.78  ?  253 PHE   A CD1 1 
ATOM   1884 C  CD2 . PHE   A 1 238 ? 50.030 -15.963 -14.087 1.00 32.84  ?  253 PHE   A CD2 1 
ATOM   1885 C  CE1 . PHE   A 1 238 ? 50.923 -14.130 -12.178 1.00 39.77  ?  253 PHE   A CE1 1 
ATOM   1886 C  CE2 . PHE   A 1 238 ? 49.104 -15.209 -13.349 1.00 35.23  ?  253 PHE   A CE2 1 
ATOM   1887 C  CZ  . PHE   A 1 238 ? 49.556 -14.298 -12.374 1.00 36.08  ?  253 PHE   A CZ  1 
ATOM   1888 N  N   . LYS   A 1 239 ? 54.815 -17.596 -16.538 1.00 36.28  ?  254 LYS   A N   1 
ATOM   1889 C  CA  . LYS   A 1 239 ? 56.044 -18.380 -16.728 1.00 42.22  ?  254 LYS   A CA  1 
ATOM   1890 C  C   . LYS   A 1 239 ? 57.251 -17.475 -16.955 1.00 38.81  ?  254 LYS   A C   1 
ATOM   1891 O  O   . LYS   A 1 239 ? 58.322 -17.685 -16.371 1.00 39.04  ?  254 LYS   A O   1 
ATOM   1892 C  CB  . LYS   A 1 239 ? 55.925 -19.340 -17.922 1.00 41.57  ?  254 LYS   A CB  1 
ATOM   1893 C  CG  . LYS   A 1 239 ? 55.039 -20.561 -17.748 1.00 54.42  ?  254 LYS   A CG  1 
ATOM   1894 C  CD  . LYS   A 1 239 ? 55.226 -21.559 -18.927 1.00 53.30  ?  254 LYS   A CD  1 
ATOM   1895 C  CE  . LYS   A 1 239 ? 54.939 -20.943 -20.292 1.00 59.88  ?  254 LYS   A CE  1 
ATOM   1896 N  NZ  . LYS   A 1 239 ? 55.134 -21.960 -21.381 1.00 68.03  ?  254 LYS   A NZ  1 
ATOM   1897 N  N   . ASN   A 1 240 ? 57.096 -16.472 -17.831 1.00 34.57  ?  255 ASN   A N   1 
ATOM   1898 C  CA  . ASN   A 1 240 ? 58.189 -15.549 -18.124 1.00 35.10  ?  255 ASN   A CA  1 
ATOM   1899 C  C   . ASN   A 1 240 ? 58.545 -14.711 -16.909 1.00 33.31  ?  255 ASN   A C   1 
ATOM   1900 O  O   . ASN   A 1 240 ? 59.730 -14.579 -16.563 1.00 39.72  ?  255 ASN   A O   1 
ATOM   1901 C  CB  . ASN   A 1 240 ? 57.811 -14.652 -19.311 1.00 35.63  ?  255 ASN   A CB  1 
ATOM   1902 C  CG  . ASN   A 1 240 ? 57.941 -15.380 -20.627 1.00 43.78  ?  255 ASN   A CG  1 
ATOM   1903 O  OD1 . ASN   A 1 240 ? 59.048 -15.716 -21.049 1.00 39.07  ?  255 ASN   A OD1 1 
ATOM   1904 N  ND2 . ASN   A 1 240 ? 56.807 -15.665 -21.268 1.00 36.47  ?  255 ASN   A ND2 1 
ATOM   1905 N  N   . ALA   A 1 241 ? 57.528 -14.161 -16.233 1.00 35.26  ?  256 ALA   A N   1 
ATOM   1906 C  CA  . ALA   A 1 241 ? 57.757 -13.324 -15.054 1.00 36.86  ?  256 ALA   A CA  1 
ATOM   1907 C  C   . ALA   A 1 241 ? 58.501 -14.077 -13.957 1.00 37.85  ?  256 ALA   A C   1 
ATOM   1908 O  O   . ALA   A 1 241 ? 59.385 -13.515 -13.296 1.00 41.57  ?  256 ALA   A O   1 
ATOM   1909 C  CB  . ALA   A 1 241 ? 56.422 -12.804 -14.514 1.00 38.51  ?  256 ALA   A CB  1 
ATOM   1910 N  N   . MET   A 1 242 ? 58.132 -15.339 -13.719 1.00 37.12  ?  257 MET   A N   1 
ATOM   1911 C  CA  . MET   A 1 242 ? 58.784 -16.104 -12.662 1.00 37.39  ?  257 MET   A CA  1 
ATOM   1912 C  C   . MET   A 1 242 ? 60.216 -16.435 -13.037 1.00 41.43  ?  257 MET   A C   1 
ATOM   1913 O  O   . MET   A 1 242 ? 61.136 -16.283 -12.220 1.00 40.08  ?  257 MET   A O   1 
ATOM   1914 C  CB  . MET   A 1 242 ? 58.004 -17.386 -12.374 1.00 46.05  ?  257 MET   A CB  1 
ATOM   1915 C  CG  . MET   A 1 242 ? 56.615 -17.103 -11.844 1.00 37.50  ?  257 MET   A CG  1 
ATOM   1916 S  SD  . MET   A 1 242 ? 55.689 -18.599 -11.493 1.00 49.74  ?  257 MET   A SD  1 
ATOM   1917 C  CE  . MET   A 1 242 ? 54.171 -17.805 -10.944 1.00 41.89  ?  257 MET   A CE  1 
ATOM   1918 N  N   . ARG   A 1 243 ? 60.418 -16.918 -14.264 1.00 39.44  ?  258 ARG   A N   1 
ATOM   1919 C  CA  . ARG   A 1 243 ? 61.768 -17.221 -14.717 1.00 45.24  ?  258 ARG   A CA  1 
ATOM   1920 C  C   . ARG   A 1 243 ? 62.669 -16.000 -14.576 1.00 41.79  ?  258 ARG   A C   1 
ATOM   1921 O  O   . ARG   A 1 243 ? 63.770 -16.087 -14.025 1.00 45.21  ?  258 ARG   A O   1 
ATOM   1922 C  CB  . ARG   A 1 243 ? 61.733 -17.693 -16.175 1.00 47.53  ?  258 ARG   A CB  1 
ATOM   1923 C  CG  . ARG   A 1 243 ? 63.098 -18.041 -16.732 1.00 60.18  ?  258 ARG   A CG  1 
ATOM   1924 C  CD  . ARG   A 1 243 ? 63.587 -19.324 -16.091 1.00 75.34  ?  258 ARG   A CD  1 
ATOM   1925 N  NE  . ARG   A 1 243 ? 62.509 -20.304 -15.957 1.00 88.14  ?  258 ARG   A NE  1 
ATOM   1926 C  CZ  . ARG   A 1 243 ? 62.371 -21.398 -16.701 1.00 93.75  ?  258 ARG   A CZ  1 
ATOM   1927 N  NH1 . ARG   A 1 243 ? 63.280 -21.745 -17.600 1.00 88.36  ?  258 ARG   A NH1 1 
ATOM   1928 N  NH2 . ARG   A 1 243 ? 61.289 -22.161 -16.540 1.00 95.76  ?  258 ARG   A NH2 1 
ATOM   1929 N  N   . ALA   A 1 244 ? 62.206 -14.848 -15.065 1.00 40.25  ?  259 ALA   A N   1 
ATOM   1930 C  CA  . ALA   A 1 244 ? 63.003 -13.632 -14.968 1.00 45.96  ?  259 ALA   A CA  1 
ATOM   1931 C  C   . ALA   A 1 244 ? 63.287 -13.280 -13.517 1.00 45.50  ?  259 ALA   A C   1 
ATOM   1932 O  O   . ALA   A 1 244 ? 64.406 -12.877 -13.174 1.00 42.91  ?  259 ALA   A O   1 
ATOM   1933 C  CB  . ALA   A 1 244 ? 62.286 -12.477 -15.657 1.00 38.39  ?  259 ALA   A CB  1 
ATOM   1934 N  N   . THR   A 1 245 ? 62.285 -13.431 -12.647 1.00 43.84  ?  260 THR   A N   1 
ATOM   1935 C  CA  . THR   A 1 245 ? 62.478 -13.085 -11.244 1.00 44.08  ?  260 THR   A CA  1 
ATOM   1936 C  C   . THR   A 1 245 ? 63.506 -14.002 -10.594 1.00 45.87  ?  260 THR   A C   1 
ATOM   1937 O  O   . THR   A 1 245 ? 64.377 -13.541 -9.846  1.00 45.35  ?  260 THR   A O   1 
ATOM   1938 C  CB  . THR   A 1 245 ? 61.139 -13.132 -10.497 1.00 44.16  ?  260 THR   A CB  1 
ATOM   1939 O  OG1 . THR   A 1 245 ? 60.226 -12.194 -11.087 1.00 39.86  ?  260 THR   A OG1 1 
ATOM   1940 C  CG2 . THR   A 1 245 ? 61.330 -12.762 -9.022  1.00 48.82  ?  260 THR   A CG2 1 
ATOM   1941 N  N   . VAL   A 1 246 ? 63.443 -15.300 -10.888 1.00 46.56  ?  261 VAL   A N   1 
ATOM   1942 C  CA  . VAL   A 1 246 ? 64.373 -16.235 -10.265 1.00 47.11  ?  261 VAL   A CA  1 
ATOM   1943 C  C   . VAL   A 1 246 ? 65.797 -15.953 -10.732 1.00 58.24  ?  261 VAL   A C   1 
ATOM   1944 O  O   . VAL   A 1 246 ? 66.732 -15.879 -9.927  1.00 53.38  ?  261 VAL   A O   1 
ATOM   1945 C  CB  . VAL   A 1 246 ? 63.956 -17.685 -10.564 1.00 56.15  ?  261 VAL   A CB  1 
ATOM   1946 C  CG1 . VAL   A 1 246 ? 65.116 -18.631 -10.304 1.00 56.80  ?  261 VAL   A CG1 1 
ATOM   1947 C  CG2 . VAL   A 1 246 ? 62.735 -18.057 -9.732  1.00 44.52  ?  261 VAL   A CG2 1 
ATOM   1948 N  N   . GLU   A 1 247 ? 65.979 -15.738 -12.035 1.00 48.47  ?  262 GLU   A N   1 
ATOM   1949 C  CA  . GLU   A 1 247 ? 67.333 -15.646 -12.568 1.00 55.49  ?  262 GLU   A CA  1 
ATOM   1950 C  C   . GLU   A 1 247 ? 68.001 -14.314 -12.250 1.00 53.04  ?  262 GLU   A C   1 
ATOM   1951 O  O   . GLU   A 1 247 ? 69.221 -14.265 -12.055 1.00 57.18  ?  262 GLU   A O   1 
ATOM   1952 C  CB  . GLU   A 1 247 ? 67.302 -15.894 -14.080 1.00 54.43  ?  262 GLU   A CB  1 
ATOM   1953 C  CG  . GLU   A 1 247 ? 66.898 -17.336 -14.409 1.00 72.90  ?  262 GLU   A CG  1 
ATOM   1954 C  CD  . GLU   A 1 247 ? 67.122 -17.707 -15.862 1.00 89.93  ?  262 GLU   A CD  1 
ATOM   1955 O  OE1 . GLU   A 1 247 ? 67.745 -16.910 -16.594 1.00 92.61  ?  262 GLU   A OE1 1 
ATOM   1956 O  OE2 . GLU   A 1 247 ? 66.669 -18.800 -16.273 1.00 97.38  ?  262 GLU   A OE2 1 
ATOM   1957 N  N   . SER   A 1 248 ? 67.235 -13.233 -12.176 1.00 47.11  ?  263 SER   A N   1 
ATOM   1958 C  CA  . SER   A 1 248 ? 67.817 -11.939 -11.847 1.00 50.45  ?  263 SER   A CA  1 
ATOM   1959 C  C   . SER   A 1 248 ? 68.139 -11.788 -10.369 1.00 56.73  ?  263 SER   A C   1 
ATOM   1960 O  O   . SER   A 1 248 ? 68.865 -10.853 -10.002 1.00 56.89  ?  263 SER   A O   1 
ATOM   1961 C  CB  . SER   A 1 248 ? 66.864 -10.827 -12.250 1.00 50.57  ?  263 SER   A CB  1 
ATOM   1962 O  OG  . SER   A 1 248 ? 65.647 -10.997 -11.549 1.00 51.26  ?  263 SER   A OG  1 
ATOM   1963 N  N   . HIS   A 1 249 ? 67.612 -12.663 -9.511  1.00 53.26  ?  264 HIS   A N   1 
ATOM   1964 C  CA  . HIS   A 1 249 ? 67.829 -12.520 -8.076  1.00 60.94  ?  264 HIS   A CA  1 
ATOM   1965 C  C   . HIS   A 1 249 ? 68.551 -13.724 -7.498  1.00 68.62  ?  264 HIS   A C   1 
ATOM   1966 O  O   . HIS   A 1 249 ? 68.182 -14.219 -6.432  1.00 68.69  ?  264 HIS   A O   1 
ATOM   1967 C  CB  . HIS   A 1 249 ? 66.501 -12.299 -7.350  1.00 59.07  ?  264 HIS   A CB  1 
ATOM   1968 C  CG  . HIS   A 1 249 ? 65.930 -10.936 -7.569  1.00 63.28  ?  264 HIS   A CG  1 
ATOM   1969 N  ND1 . HIS   A 1 249 ? 65.395 -10.537 -8.776  1.00 62.74  ?  264 HIS   A ND1 1 
ATOM   1970 C  CD2 . HIS   A 1 249 ? 65.847 -9.863  -6.748  1.00 62.92  ?  264 HIS   A CD2 1 
ATOM   1971 C  CE1 . HIS   A 1 249 ? 64.993 -9.281  -8.681  1.00 57.11  ?  264 HIS   A CE1 1 
ATOM   1972 N  NE2 . HIS   A 1 249 ? 65.258 -8.849  -7.462  1.00 62.66  ?  264 HIS   A NE2 1 
ATOM   1973 N  N   . GLU   A 1 250 ? 69.591 -14.189 -8.198  1.00 72.45  ?  265 GLU   A N   1 
ATOM   1974 C  CA  . GLU   A 1 250 ? 70.381 -15.313 -7.710  1.00 82.62  ?  265 GLU   A CA  1 
ATOM   1975 C  C   . GLU   A 1 250 ? 70.947 -15.049 -6.324  1.00 80.54  ?  265 GLU   A C   1 
ATOM   1976 O  O   . GLU   A 1 250 ? 71.108 -15.982 -5.534  1.00 86.23  ?  265 GLU   A O   1 
ATOM   1977 C  CB  . GLU   A 1 250 ? 71.526 -15.613 -8.675  1.00 84.49  ?  265 GLU   A CB  1 
ATOM   1978 C  CG  . GLU   A 1 250 ? 71.093 -15.933 -10.088 1.00 83.53  ?  265 GLU   A CG  1 
ATOM   1979 C  CD  . GLU   A 1 250 ? 70.622 -17.361 -10.243 1.00 96.34  ?  265 GLU   A CD  1 
ATOM   1980 O  OE1 . GLU   A 1 250 ? 70.010 -17.897 -9.291  1.00 100.27 ?  265 GLU   A OE1 1 
ATOM   1981 O  OE2 . GLU   A 1 250 ? 70.874 -17.952 -11.319 1.00 95.71  ?  265 GLU   A OE2 1 
ATOM   1982 N  N   . SER   A 1 251 ? 71.243 -13.789 -6.011  1.00 86.91  ?  266 SER   A N   1 
ATOM   1983 C  CA  . SER   A 1 251 ? 71.971 -13.423 -4.810  1.00 85.40  ?  266 SER   A CA  1 
ATOM   1984 C  C   . SER   A 1 251 ? 71.074 -12.953 -3.672  1.00 86.59  ?  266 SER   A C   1 
ATOM   1985 O  O   . SER   A 1 251 ? 71.549 -12.841 -2.536  1.00 94.05  ?  266 SER   A O   1 
ATOM   1986 C  CB  . SER   A 1 251 ? 72.989 -12.332 -5.142  1.00 97.89  ?  266 SER   A CB  1 
ATOM   1987 O  OG  . SER   A 1 251 ? 73.556 -12.568 -6.421  1.00 105.47 ?  266 SER   A OG  1 
ATOM   1988 N  N   . SER   A 1 252 ? 69.804 -12.674 -3.941  1.00 78.43  ?  267 SER   A N   1 
ATOM   1989 C  CA  . SER   A 1 252 ? 68.888 -12.260 -2.893  1.00 83.78  ?  267 SER   A CA  1 
ATOM   1990 C  C   . SER   A 1 252 ? 68.334 -13.477 -2.169  1.00 79.46  ?  267 SER   A C   1 
ATOM   1991 O  O   . SER   A 1 252 ? 68.217 -14.558 -2.740  1.00 77.80  ?  267 SER   A O   1 
ATOM   1992 C  CB  . SER   A 1 252 ? 67.738 -11.441 -3.475  1.00 78.38  ?  267 SER   A CB  1 
ATOM   1993 O  OG  . SER   A 1 252 ? 68.204 -10.594 -4.506  1.00 86.78  ?  267 SER   A OG  1 
ATOM   1994 N  N   . LEU   A 1 253 ? 68.019 -13.297 -0.890  1.00 80.11  ?  268 LEU   A N   1 
ATOM   1995 C  CA  . LEU   A 1 253 ? 67.276 -14.313 -0.157  1.00 74.24  ?  268 LEU   A CA  1 
ATOM   1996 C  C   . LEU   A 1 253 ? 65.792 -14.198 -0.445  1.00 81.56  ?  268 LEU   A C   1 
ATOM   1997 O  O   . LEU   A 1 253 ? 65.056 -15.185 -0.354  1.00 84.52  ?  268 LEU   A O   1 
ATOM   1998 C  CB  . LEU   A 1 253 ? 67.540 -14.168 1.341   1.00 70.67  ?  268 LEU   A CB  1 
ATOM   1999 C  CG  . LEU   A 1 253 ? 69.019 -14.108 1.720   1.00 66.91  ?  268 LEU   A CG  1 
ATOM   2000 C  CD1 . LEU   A 1 253 ? 69.204 -13.851 3.197   1.00 70.69  ?  268 LEU   A CD1 1 
ATOM   2001 C  CD2 . LEU   A 1 253 ? 69.702 -15.400 1.351   1.00 76.60  ?  268 LEU   A CD2 1 
ATOM   2002 N  N   . ILE   A 1 254 ? 65.372 -12.995 -0.798  1.00 97.83  ?  269 ILE   A N   1 
ATOM   2003 C  CA  . ILE   A 1 254 ? 64.002 -12.617 -1.108  1.00 97.28  ?  269 ILE   A CA  1 
ATOM   2004 C  C   . ILE   A 1 254 ? 63.767 -12.808 -2.597  1.00 82.91  ?  269 ILE   A C   1 
ATOM   2005 O  O   . ILE   A 1 254 ? 64.588 -12.381 -3.416  1.00 87.79  ?  269 ILE   A O   1 
ATOM   2006 C  CB  . ILE   A 1 254 ? 63.769 -11.143 -0.709  1.00 109.11 ?  269 ILE   A CB  1 
ATOM   2007 C  CG1 . ILE   A 1 254 ? 63.855 -10.940 0.814   1.00 108.24 ?  269 ILE   A CG1 1 
ATOM   2008 C  CG2 . ILE   A 1 254 ? 62.473 -10.598 -1.331  1.00 101.15 ?  269 ILE   A CG2 1 
ATOM   2009 C  CD1 . ILE   A 1 254 ? 64.214 -9.503  1.245   1.00 108.18 ?  269 ILE   A CD1 1 
ATOM   2010 N  N   . LEU   A 1 255 ? 62.657 -13.447 -2.967  1.00 69.19  ?  270 LEU   A N   1 
ATOM   2011 C  CA  . LEU   A 1 255 ? 62.143 -13.267 -4.325  1.00 63.00  ?  270 LEU   A CA  1 
ATOM   2012 C  C   . LEU   A 1 255 ? 61.020 -12.250 -4.283  1.00 55.14  ?  270 LEU   A C   1 
ATOM   2013 O  O   . LEU   A 1 255 ? 60.050 -12.452 -3.539  1.00 52.38  ?  270 LEU   A O   1 
ATOM   2014 C  CB  . LEU   A 1 255 ? 61.634 -14.575 -4.927  1.00 67.61  ?  270 LEU   A CB  1 
ATOM   2015 C  CG  . LEU   A 1 255 ? 62.681 -15.578 -5.404  1.00 73.76  ?  270 LEU   A CG  1 
ATOM   2016 C  CD1 . LEU   A 1 255 ? 62.012 -16.793 -6.024  1.00 66.71  ?  270 LEU   A CD1 1 
ATOM   2017 C  CD2 . LEU   A 1 255 ? 63.658 -14.933 -6.362  1.00 61.04  ?  270 LEU   A CD2 1 
ATOM   2018 N  N   . PRO   A 1 256 ? 61.096 -11.161 -5.044  1.00 49.60  ?  271 PRO   A N   1 
ATOM   2019 C  CA  . PRO   A 1 256 ? 59.970 -10.234 -5.099  1.00 57.72  ?  271 PRO   A CA  1 
ATOM   2020 C  C   . PRO   A 1 256 ? 58.742 -10.919 -5.671  1.00 57.21  ?  271 PRO   A C   1 
ATOM   2021 O  O   . PRO   A 1 256 ? 58.851 -11.789 -6.556  1.00 59.98  ?  271 PRO   A O   1 
ATOM   2022 C  CB  . PRO   A 1 256 ? 60.467 -9.122  -6.034  1.00 52.37  ?  271 PRO   A CB  1 
ATOM   2023 C  CG  . PRO   A 1 256 ? 61.937 -9.299  -6.132  1.00 64.35  ?  271 PRO   A CG  1 
ATOM   2024 C  CD  . PRO   A 1 256 ? 62.223 -10.742 -5.889  1.00 58.42  ?  271 PRO   A CD  1 
ATOM   2025 N  N   . PRO   A 1 257 ? 57.556 -10.538 -5.215  1.00 50.90  ?  272 PRO   A N   1 
ATOM   2026 C  CA  . PRO   A 1 257 ? 56.331 -11.154 -5.724  1.00 47.64  ?  272 PRO   A CA  1 
ATOM   2027 C  C   . PRO   A 1 257 ? 55.978 -10.611 -7.097  1.00 48.80  ?  272 PRO   A C   1 
ATOM   2028 O  O   . PRO   A 1 257 ? 56.518 -9.612  -7.573  1.00 43.96  ?  272 PRO   A O   1 
ATOM   2029 C  CB  . PRO   A 1 257 ? 55.279 -10.741 -4.696  1.00 53.37  ?  272 PRO   A CB  1 
ATOM   2030 C  CG  . PRO   A 1 257 ? 55.770 -9.396  -4.227  1.00 63.71  ?  272 PRO   A CG  1 
ATOM   2031 C  CD  . PRO   A 1 257 ? 57.277 -9.545  -4.161  1.00 62.58  ?  272 PRO   A CD  1 
ATOM   2032 N  N   . ILE   A 1 258 ? 55.038 -11.290 -7.731  1.00 42.14  ?  273 ILE   A N   1 
ATOM   2033 C  CA  . ILE   A 1 258 ? 54.419 -10.799 -8.948  1.00 45.26  ?  273 ILE   A CA  1 
ATOM   2034 C  C   . ILE   A 1 258 ? 53.102 -10.155 -8.552  1.00 45.10  ?  273 ILE   A C   1 
ATOM   2035 O  O   . ILE   A 1 258 ? 52.344 -10.734 -7.767  1.00 41.77  ?  273 ILE   A O   1 
ATOM   2036 C  CB  . ILE   A 1 258 ? 54.226 -11.945 -9.951  1.00 42.10  ?  273 ILE   A CB  1 
ATOM   2037 C  CG1 . ILE   A 1 258 ? 55.612 -12.538 -10.254 1.00 38.39  ?  273 ILE   A CG1 1 
ATOM   2038 C  CG2 . ILE   A 1 258 ? 53.478 -11.444 -11.187 1.00 36.63  ?  273 ILE   A CG2 1 
ATOM   2039 C  CD1 . ILE   A 1 258 ? 55.601 -13.830 -11.045 1.00 40.00  ?  273 ILE   A CD1 1 
ATOM   2040 N  N   . LYS   A 1 259 ? 52.851 -8.937  -9.037  1.00 40.56  ?  274 LYS   A N   1 
ATOM   2041 C  CA  . LYS   A 1 259 ? 51.639 -8.195  -8.701  1.00 36.33  ?  274 LYS   A CA  1 
ATOM   2042 C  C   . LYS   A 1 259 ? 50.717 -8.166  -9.909  1.00 39.84  ?  274 LYS   A C   1 
ATOM   2043 O  O   . LYS   A 1 259 ? 51.184 -8.050  -11.038 1.00 37.12  ?  274 LYS   A O   1 
ATOM   2044 C  CB  . LYS   A 1 259 ? 51.980 -6.766  -8.254  1.00 40.63  ?  274 LYS   A CB  1 
ATOM   2045 C  CG  . LYS   A 1 259 ? 52.889 -6.704  -7.020  1.00 53.60  ?  274 LYS   A CG  1 
ATOM   2046 C  CD  . LYS   A 1 259 ? 53.103 -5.263  -6.548  1.00 54.29  ?  274 LYS   A CD  1 
ATOM   2047 C  CE  . LYS   A 1 259 ? 54.112 -5.210  -5.409  1.00 69.52  ?  274 LYS   A CE  1 
ATOM   2048 N  NZ  . LYS   A 1 259 ? 54.411 -3.817  -4.973  1.00 85.34  ?  274 LYS   A NZ  1 
ATOM   2049 N  N   . VAL   A 1 260 ? 49.411 -8.317  -9.686  1.00 38.83  ?  275 VAL   A N   1 
ATOM   2050 C  CA  . VAL   A 1 260 ? 48.437 -8.247  -10.771 1.00 37.65  ?  275 VAL   A CA  1 
ATOM   2051 C  C   . VAL   A 1 260 ? 47.365 -7.257  -10.363 1.00 42.05  ?  275 VAL   A C   1 
ATOM   2052 O  O   . VAL   A 1 260 ? 46.877 -7.303  -9.231  1.00 40.05  ?  275 VAL   A O   1 
ATOM   2053 C  CB  . VAL   A 1 260 ? 47.800 -9.608  -11.110 1.00 40.42  ?  275 VAL   A CB  1 
ATOM   2054 C  CG1 . VAL   A 1 260 ? 46.664 -9.399  -12.128 1.00 39.32  ?  275 VAL   A CG1 1 
ATOM   2055 C  CG2 . VAL   A 1 260 ? 48.832 -10.541 -11.744 1.00 36.11  ?  275 VAL   A CG2 1 
ATOM   2056 N  N   . MET   A 1 261 ? 47.007 -6.360  -11.272 1.00 34.72  ?  276 MET   A N   1 
ATOM   2057 C  CA  . MET   A 1 261 ? 45.864 -5.488  -11.071 1.00 39.66  ?  276 MET   A CA  1 
ATOM   2058 C  C   . MET   A 1 261 ? 44.818 -5.826  -12.114 1.00 40.33  ?  276 MET   A C   1 
ATOM   2059 O  O   . MET   A 1 261 ? 45.145 -5.952  -13.292 1.00 38.65  ?  276 MET   A O   1 
ATOM   2060 C  CB  . MET   A 1 261 ? 46.251 -4.011  -11.177 1.00 35.63  ?  276 MET   A CB  1 
ATOM   2061 C  CG  . MET   A 1 261 ? 45.038 -3.150  -11.506 1.00 47.75  ?  276 MET   A CG  1 
ATOM   2062 S  SD  . MET   A 1 261 ? 45.260 -1.423  -11.072 1.00 63.58  ?  276 MET   A SD  1 
ATOM   2063 C  CE  . MET   A 1 261 ? 45.412 -1.621  -9.273  1.00 52.44  ?  276 MET   A CE  1 
ATOM   2064 N  N   . VAL   A 1 262 ? 43.566 -5.985  -11.687 1.00 39.91  ?  277 VAL   A N   1 
ATOM   2065 C  CA  . VAL   A 1 262 ? 42.451 -6.161  -12.617 1.00 38.78  ?  277 VAL   A CA  1 
ATOM   2066 C  C   . VAL   A 1 262 ? 41.581 -4.918  -12.517 1.00 40.32  ?  277 VAL   A C   1 
ATOM   2067 O  O   . VAL   A 1 262 ? 41.051 -4.621  -11.446 1.00 42.80  ?  277 VAL   A O   1 
ATOM   2068 C  CB  . VAL   A 1 262 ? 41.635 -7.427  -12.298 1.00 41.55  ?  277 VAL   A CB  1 
ATOM   2069 C  CG1 . VAL   A 1 262 ? 40.470 -7.554  -13.294 1.00 40.22  ?  277 VAL   A CG1 1 
ATOM   2070 C  CG2 . VAL   A 1 262 ? 42.534 -8.663  -12.326 1.00 39.01  ?  277 VAL   A CG2 1 
ATOM   2071 N  N   . ALA   A 1 263 ? 41.450 -4.181  -13.617 1.00 35.65  ?  278 ALA   A N   1 
ATOM   2072 C  CA  . ALA   A 1 263 ? 40.658 -2.963  -13.670 1.00 38.29  ?  278 ALA   A CA  1 
ATOM   2073 C  C   . ALA   A 1 263 ? 39.475 -3.174  -14.603 1.00 43.85  ?  278 ALA   A C   1 
ATOM   2074 O  O   . ALA   A 1 263 ? 39.647 -3.669  -15.722 1.00 37.46  ?  278 ALA   A O   1 
ATOM   2075 C  CB  . ALA   A 1 263 ? 41.500 -1.778  -14.156 1.00 34.40  ?  278 ALA   A CB  1 
ATOM   2076 N  N   . LEU   A 1 264 ? 38.279 -2.801  -14.150 1.00 39.01  ?  279 LEU   A N   1 
ATOM   2077 C  CA  . LEU   A 1 264 ? 37.085 -2.814  -14.999 1.00 38.64  ?  279 LEU   A CA  1 
ATOM   2078 C  C   . LEU   A 1 264 ? 36.604 -1.386  -15.212 1.00 47.46  ?  279 LEU   A C   1 
ATOM   2079 O  O   . LEU   A 1 264 ? 36.243 -0.703  -14.248 1.00 46.42  ?  279 LEU   A O   1 
ATOM   2080 C  CB  . LEU   A 1 264 ? 35.973 -3.654  -14.379 1.00 42.25  ?  279 LEU   A CB  1 
ATOM   2081 C  CG  . LEU   A 1 264 ? 34.656 -3.638  -15.169 1.00 44.33  ?  279 LEU   A CG  1 
ATOM   2082 C  CD1 . LEU   A 1 264 ? 34.878 -4.178  -16.590 1.00 41.64  ?  279 LEU   A CD1 1 
ATOM   2083 C  CD2 . LEU   A 1 264 ? 33.547 -4.425  -14.439 1.00 39.16  ?  279 LEU   A CD2 1 
ATOM   2084 N  N   . GLY   A 1 265 ? 36.595 -0.936  -16.469 1.00 41.46  ?  280 GLY   A N   1 
ATOM   2085 C  CA  . GLY   A 1 265 ? 36.093 0.369   -16.825 1.00 39.35  ?  280 GLY   A CA  1 
ATOM   2086 C  C   . GLY   A 1 265 ? 34.825 0.279   -17.653 1.00 45.38  ?  280 GLY   A C   1 
ATOM   2087 O  O   . GLY   A 1 265 ? 34.195 -0.773  -17.761 1.00 43.52  ?  280 GLY   A O   1 
ATOM   2088 N  N   . GLU   A 1 266 ? 34.456 1.413   -18.253 1.00 43.30  ?  281 GLU   A N   1 
ATOM   2089 C  CA  . GLU   A 1 266 ? 33.251 1.448   -19.083 1.00 44.84  ?  281 GLU   A CA  1 
ATOM   2090 C  C   . GLU   A 1 266 ? 33.420 0.671   -20.385 1.00 43.72  ?  281 GLU   A C   1 
ATOM   2091 O  O   . GLU   A 1 266 ? 32.443 0.131   -20.913 1.00 46.59  ?  281 GLU   A O   1 
ATOM   2092 C  CB  . GLU   A 1 266 ? 32.856 2.890   -19.400 1.00 47.01  ?  281 GLU   A CB  1 
ATOM   2093 C  CG  . GLU   A 1 266 ? 32.562 3.748   -18.172 1.00 68.60  ?  281 GLU   A CG  1 
ATOM   2094 C  CD  . GLU   A 1 266 ? 31.251 3.374   -17.497 1.00 71.76  ?  281 GLU   A CD  1 
ATOM   2095 O  OE1 . GLU   A 1 266 ? 30.213 3.381   -18.194 1.00 79.49  ?  281 GLU   A OE1 1 
ATOM   2096 O  OE2 . GLU   A 1 266 ? 31.256 3.065   -16.279 1.00 72.90  ?  281 GLU   A OE2 1 
ATOM   2097 N  N   . GLU   A 1 267 ? 34.628 0.604   -20.923 1.00 45.38  ?  282 GLU   A N   1 
ATOM   2098 C  CA  . GLU   A 1 267 ? 34.854 -0.048  -22.211 1.00 42.14  ?  282 GLU   A CA  1 
ATOM   2099 C  C   . GLU   A 1 267 ? 35.868 -1.176  -22.137 1.00 40.19  ?  282 GLU   A C   1 
ATOM   2100 O  O   . GLU   A 1 267 ? 35.673 -2.226  -22.767 1.00 38.81  ?  282 GLU   A O   1 
ATOM   2101 C  CB  . GLU   A 1 267 ? 35.302 1.031   -23.221 1.00 42.89  ?  282 GLU   A CB  1 
ATOM   2102 C  CG  . GLU   A 1 267 ? 35.721 0.563   -24.595 1.00 51.39  ?  282 GLU   A CG  1 
ATOM   2103 C  CD  . GLU   A 1 267 ? 35.839 1.739   -25.561 1.00 55.72  ?  282 GLU   A CD  1 
ATOM   2104 O  OE1 . GLU   A 1 267 ? 35.143 2.761   -25.355 1.00 56.35  ?  282 GLU   A OE1 1 
ATOM   2105 O  OE2 . GLU   A 1 267 ? 36.649 1.653   -26.502 1.00 60.56  ?  282 GLU   A OE2 1 
ATOM   2106 N  N   . ASP   A 1 268 ? 36.929 -1.000  -21.348 1.00 39.67  ?  283 ASP   A N   1 
ATOM   2107 C  CA  . ASP   A 1 268 ? 38.012 -1.957  -21.211 1.00 37.89  ?  283 ASP   A CA  1 
ATOM   2108 C  C   . ASP   A 1 268 ? 37.917 -2.732  -19.902 1.00 41.77  ?  283 ASP   A C   1 
ATOM   2109 O  O   . ASP   A 1 268 ? 37.539 -2.192  -18.858 1.00 37.77  ?  283 ASP   A O   1 
ATOM   2110 C  CB  . ASP   A 1 268 ? 39.371 -1.260  -21.222 1.00 39.20  ?  283 ASP   A CB  1 
ATOM   2111 C  CG  . ASP   A 1 268 ? 39.741 -0.685  -22.562 1.00 41.51  ?  283 ASP   A CG  1 
ATOM   2112 O  OD1 . ASP   A 1 268 ? 38.950 -0.817  -23.519 1.00 41.51  ?  283 ASP   A OD1 1 
ATOM   2113 O  OD2 . ASP   A 1 268 ? 40.851 -0.108  -22.641 1.00 42.09  ?  283 ASP   A OD2 1 
ATOM   2114 N  N   . LEU   A 1 269 ? 38.357 -3.983  -19.951 1.00 36.86  ?  284 LEU   A N   1 
ATOM   2115 C  CA  . LEU   A 1 269 ? 38.752 -4.718  -18.761 1.00 34.97  ?  284 LEU   A CA  1 
ATOM   2116 C  C   . LEU   A 1 269 ? 40.236 -4.998  -18.927 1.00 39.37  ?  284 LEU   A C   1 
ATOM   2117 O  O   . LEU   A 1 269 ? 40.630 -5.681  -19.870 1.00 36.63  ?  284 LEU   A O   1 
ATOM   2118 C  CB  . LEU   A 1 269 ? 37.950 -6.012  -18.606 1.00 37.78  ?  284 LEU   A CB  1 
ATOM   2119 C  CG  . LEU   A 1 269 ? 38.179 -6.754  -17.271 1.00 43.02  ?  284 LEU   A CG  1 
ATOM   2120 C  CD1 . LEU   A 1 269 ? 36.931 -7.488  -16.926 1.00 48.95  ?  284 LEU   A CD1 1 
ATOM   2121 C  CD2 . LEU   A 1 269 ? 39.330 -7.736  -17.430 1.00 43.61  ?  284 LEU   A CD2 1 
ATOM   2122 N  N   . SER   A 1 270 ? 41.057 -4.475  -18.024 1.00 35.29  ?  285 SER   A N   1 
ATOM   2123 C  CA  . SER   A 1 270 ? 42.509 -4.525  -18.181 1.00 33.86  ?  285 SER   A CA  1 
ATOM   2124 C  C   . SER   A 1 270 ? 43.154 -5.333  -17.067 1.00 35.41  ?  285 SER   A C   1 
ATOM   2125 O  O   . SER   A 1 270 ? 42.784 -5.200  -15.897 1.00 34.48  ?  285 SER   A O   1 
ATOM   2126 C  CB  . SER   A 1 270 ? 43.078 -3.112  -18.188 1.00 33.62  ?  285 SER   A CB  1 
ATOM   2127 O  OG  . SER   A 1 270 ? 42.332 -2.312  -19.103 1.00 39.41  ?  285 SER   A OG  1 
ATOM   2128 N  N   . ILE   A 1 271 ? 44.141 -6.144  -17.429 1.00 32.44  ?  286 ILE   A N   1 
ATOM   2129 C  CA  . ILE   A 1 271 ? 44.900 -6.951  -16.474 1.00 35.85  ?  286 ILE   A CA  1 
ATOM   2130 C  C   . ILE   A 1 271 ? 46.369 -6.587  -16.654 1.00 38.61  ?  286 ILE   A C   1 
ATOM   2131 O  O   . ILE   A 1 271 ? 46.954 -6.862  -17.709 1.00 36.07  ?  286 ILE   A O   1 
ATOM   2132 C  CB  . ILE   A 1 271 ? 44.685 -8.458  -16.696 1.00 38.28  ?  286 ILE   A CB  1 
ATOM   2133 C  CG1 . ILE   A 1 271 ? 43.192 -8.793  -16.730 1.00 40.67  ?  286 ILE   A CG1 1 
ATOM   2134 C  CG2 . ILE   A 1 271 ? 45.345 -9.261  -15.584 1.00 35.75  ?  286 ILE   A CG2 1 
ATOM   2135 C  CD1 . ILE   A 1 271 ? 42.871 -10.107 -17.391 1.00 40.86  ?  286 ILE   A CD1 1 
ATOM   2136 N  N   . LYS   A 1 272 ? 46.963 -5.975  -15.636 1.00 33.70  ?  287 LYS   A N   1 
ATOM   2137 C  CA  . LYS   A 1 272 ? 48.383 -5.651  -15.639 1.00 38.19  ?  287 LYS   A CA  1 
ATOM   2138 C  C   . LYS   A 1 272 ? 49.116 -6.605  -14.701 1.00 37.86  ?  287 LYS   A C   1 
ATOM   2139 O  O   . LYS   A 1 272 ? 48.748 -6.739  -13.535 1.00 37.66  ?  287 LYS   A O   1 
ATOM   2140 C  CB  . LYS   A 1 272 ? 48.613 -4.198  -15.208 1.00 37.29  ?  287 LYS   A CB  1 
ATOM   2141 C  CG  . LYS   A 1 272 ? 50.098 -3.783  -15.104 1.00 37.82  ?  287 LYS   A CG  1 
ATOM   2142 C  CD  . LYS   A 1 272 ? 50.233 -2.266  -14.937 1.00 45.96  ?  287 LYS   A CD  1 
ATOM   2143 C  CE  . LYS   A 1 272 ? 50.336 -1.894  -13.476 1.00 49.24  ?  287 LYS   A CE  1 
ATOM   2144 N  NZ  . LYS   A 1 272 ? 50.456 -0.415  -13.261 1.00 66.13  ?  287 LYS   A NZ  1 
ATOM   2145 N  N   . MET   A 1 273 ? 50.133 -7.275  -15.224 1.00 36.32  ?  288 MET   A N   1 
ATOM   2146 C  CA  . MET   A 1 273 ? 51.035 -8.113  -14.449 1.00 34.83  ?  288 MET   A CA  1 
ATOM   2147 C  C   . MET   A 1 273 ? 52.384 -7.411  -14.339 1.00 36.82  ?  288 MET   A C   1 
ATOM   2148 O  O   . MET   A 1 273 ? 52.889 -6.898  -15.339 1.00 36.63  ?  288 MET   A O   1 
ATOM   2149 C  CB  . MET   A 1 273 ? 51.199 -9.479  -15.130 1.00 32.34  ?  288 MET   A CB  1 
ATOM   2150 C  CG  . MET   A 1 273 ? 51.932 -10.494 -14.260 1.00 32.03  ?  288 MET   A CG  1 
ATOM   2151 S  SD  . MET   A 1 273 ? 52.219 -12.017 -15.190 1.00 37.04  ?  288 MET   A SD  1 
ATOM   2152 C  CE  . MET   A 1 273 ? 50.532 -12.519 -15.614 1.00 31.47  ?  288 MET   A CE  1 
ATOM   2153 N  N   . SER   A 1 274 ? 52.965 -7.395  -13.132 1.00 35.12  ?  289 SER   A N   1 
ATOM   2154 C  CA  . SER   A 1 274 ? 54.205 -6.676  -12.837 1.00 35.72  ?  289 SER   A CA  1 
ATOM   2155 C  C   . SER   A 1 274 ? 55.219 -7.605  -12.187 1.00 38.99  ?  289 SER   A C   1 
ATOM   2156 O  O   . SER   A 1 274 ? 54.941 -8.180  -11.131 1.00 38.45  ?  289 SER   A O   1 
ATOM   2157 C  CB  . SER   A 1 274 ? 53.931 -5.491  -11.895 1.00 38.93  ?  289 SER   A CB  1 
ATOM   2158 O  OG  . SER   A 1 274 ? 53.101 -4.522  -12.550 1.00 42.29  ?  289 SER   A OG  1 
ATOM   2159 N  N   . ASP   A 1 275 ? 56.405 -7.722  -12.783 1.00 38.58  ?  290 ASP   A N   1 
ATOM   2160 C  CA  . ASP   A 1 275 ? 57.499 -8.418  -12.116 1.00 37.15  ?  290 ASP   A CA  1 
ATOM   2161 C  C   . ASP   A 1 275 ? 58.627 -7.443  -11.829 1.00 40.28  ?  290 ASP   A C   1 
ATOM   2162 O  O   . ASP   A 1 275 ? 58.669 -6.319  -12.347 1.00 37.40  ?  290 ASP   A O   1 
ATOM   2163 C  CB  . ASP   A 1 275 ? 58.022 -9.639  -12.930 1.00 37.63  ?  290 ASP   A CB  1 
ATOM   2164 C  CG  . ASP   A 1 275 ? 58.812 -9.270  -14.216 1.00 40.08  ?  290 ASP   A CG  1 
ATOM   2165 O  OD1 . ASP   A 1 275 ? 59.780 -8.461  -14.197 1.00 39.96  ?  290 ASP   A OD1 1 
ATOM   2166 O  OD2 . ASP   A 1 275 ? 58.501 -9.861  -15.276 1.00 37.43  ?  290 ASP   A OD2 1 
ATOM   2167 N  N   . ARG   A 1 276 ? 59.520 -7.891  -10.956 1.00 40.27  ?  291 ARG   A N   1 
ATOM   2168 C  CA  . ARG   A 1 276 ? 60.778 -7.232  -10.663 1.00 44.45  ?  291 ARG   A CA  1 
ATOM   2169 C  C   . ARG   A 1 276 ? 61.892 -8.180  -11.076 1.00 46.40  ?  291 ARG   A C   1 
ATOM   2170 O  O   . ARG   A 1 276 ? 62.799 -8.464  -10.286 1.00 47.56  ?  291 ARG   A O   1 
ATOM   2171 C  CB  . ARG   A 1 276 ? 60.870 -6.866  -9.172  1.00 43.42  ?  291 ARG   A CB  1 
ATOM   2172 C  CG  . ARG   A 1 276 ? 59.758 -5.920  -8.755  1.00 54.82  ?  291 ARG   A CG  1 
ATOM   2173 C  CD  . ARG   A 1 276 ? 60.027 -5.222  -7.423  1.00 62.16  ?  291 ARG   A CD  1 
ATOM   2174 N  NE  . ARG   A 1 276 ? 58.914 -4.347  -7.063  1.00 74.01  ?  291 ARG   A NE  1 
ATOM   2175 C  CZ  . ARG   A 1 276 ? 58.995 -3.334  -6.207  1.00 86.38  ?  291 ARG   A CZ  1 
ATOM   2176 N  NH1 . ARG   A 1 276 ? 60.140 -3.012  -5.619  1.00 78.70  ?  291 ARG   A NH1 1 
ATOM   2177 N  NH2 . ARG   A 1 276 ? 57.902 -2.622  -5.938  1.00 86.96  ?  291 ARG   A NH2 1 
ATOM   2178 N  N   . GLY   A 1 277 ? 61.817 -8.687  -12.306 1.00 43.62  ?  292 GLY   A N   1 
ATOM   2179 C  CA  . GLY   A 1 277 ? 62.775 -9.653  -12.797 1.00 43.33  ?  292 GLY   A CA  1 
ATOM   2180 C  C   . GLY   A 1 277 ? 63.923 -9.061  -13.595 1.00 40.55  ?  292 GLY   A C   1 
ATOM   2181 O  O   . GLY   A 1 277 ? 64.554 -9.764  -14.388 1.00 39.53  ?  292 GLY   A O   1 
ATOM   2182 N  N   . GLY   A 1 278 ? 64.199 -7.768  -13.412 1.00 37.18  ?  293 GLY   A N   1 
ATOM   2183 C  CA  . GLY   A 1 278 ? 65.383 -7.156  -13.969 1.00 40.26  ?  293 GLY   A CA  1 
ATOM   2184 C  C   . GLY   A 1 278 ? 65.195 -6.484  -15.319 1.00 38.99  ?  293 GLY   A C   1 
ATOM   2185 O  O   . GLY   A 1 278 ? 66.020 -5.646  -15.694 1.00 44.22  ?  293 GLY   A O   1 
ATOM   2186 N  N   . GLY   A 1 279 ? 64.143 -6.814  -16.053 1.00 35.54  ?  294 GLY   A N   1 
ATOM   2187 C  CA  . GLY   A 1 279 ? 63.833 -6.069  -17.254 1.00 37.12  ?  294 GLY   A CA  1 
ATOM   2188 C  C   . GLY   A 1 279 ? 64.747 -6.435  -18.411 1.00 43.25  ?  294 GLY   A C   1 
ATOM   2189 O  O   . GLY   A 1 279 ? 65.683 -7.221  -18.253 1.00 42.08  ?  294 GLY   A O   1 
ATOM   2190 N  N   . VAL   A 1 280 ? 64.447 -5.884  -19.581 1.00 36.67  ?  295 VAL   A N   1 
ATOM   2191 C  CA  . VAL   A 1 280 ? 65.286 -5.996  -20.773 1.00 38.82  ?  295 VAL   A CA  1 
ATOM   2192 C  C   . VAL   A 1 280 ? 65.305 -4.642  -21.465 1.00 40.84  ?  295 VAL   A C   1 
ATOM   2193 O  O   . VAL   A 1 280 ? 64.372 -3.840  -21.316 1.00 37.87  ?  295 VAL   A O   1 
ATOM   2194 C  CB  . VAL   A 1 280 ? 64.752 -7.074  -21.762 1.00 42.47  ?  295 VAL   A CB  1 
ATOM   2195 C  CG1 . VAL   A 1 280 ? 64.913 -8.475  -21.205 1.00 41.28  ?  295 VAL   A CG1 1 
ATOM   2196 C  CG2 . VAL   A 1 280 ? 63.294 -6.790  -22.134 1.00 43.30  ?  295 VAL   A CG2 1 
ATOM   2197 N  N   . PRO   A 1 281 ? 66.352 -4.357  -22.233 1.00 38.80  ?  296 PRO   A N   1 
ATOM   2198 C  CA  . PRO   A 1 281 ? 66.369 -3.088  -22.967 1.00 39.96  ?  296 PRO   A CA  1 
ATOM   2199 C  C   . PRO   A 1 281 ? 65.244 -3.028  -24.002 1.00 42.91  ?  296 PRO   A C   1 
ATOM   2200 O  O   . PRO   A 1 281 ? 64.820 -4.048  -24.554 1.00 40.62  ?  296 PRO   A O   1 
ATOM   2201 C  CB  . PRO   A 1 281 ? 67.752 -3.068  -23.632 1.00 44.22  ?  296 PRO   A CB  1 
ATOM   2202 C  CG  . PRO   A 1 281 ? 68.213 -4.496  -23.661 1.00 45.81  ?  296 PRO   A CG  1 
ATOM   2203 C  CD  . PRO   A 1 281 ? 67.557 -5.176  -22.491 1.00 45.81  ?  296 PRO   A CD  1 
ATOM   2204 N  N   . LEU   A 1 282 ? 64.767 -1.805  -24.265 1.00 38.33  ?  297 LEU   A N   1 
ATOM   2205 C  CA  . LEU   A 1 282 ? 63.649 -1.612  -25.186 1.00 39.10  ?  297 LEU   A CA  1 
ATOM   2206 C  C   . LEU   A 1 282 ? 63.905 -2.279  -26.540 1.00 40.53  ?  297 LEU   A C   1 
ATOM   2207 O  O   . LEU   A 1 282 ? 63.003 -2.873  -27.143 1.00 38.27  ?  297 LEU   A O   1 
ATOM   2208 C  CB  . LEU   A 1 282 ? 63.402 -0.111  -25.352 1.00 36.74  ?  297 LEU   A CB  1 
ATOM   2209 C  CG  . LEU   A 1 282 ? 62.410 0.273   -26.435 1.00 39.76  ?  297 LEU   A CG  1 
ATOM   2210 C  CD1 . LEU   A 1 282 ? 61.037 -0.161  -25.969 1.00 37.98  ?  297 LEU   A CD1 1 
ATOM   2211 C  CD2 . LEU   A 1 282 ? 62.496 1.783   -26.684 1.00 36.97  ?  297 LEU   A CD2 1 
ATOM   2212 N  N   . ARG   A 1 283 ? 65.145 -2.216  -27.010 1.00 39.89  ?  298 ARG   A N   1 
ATOM   2213 C  CA  . ARG   A 1 283 ? 65.533 -2.826  -28.275 1.00 46.47  ?  298 ARG   A CA  1 
ATOM   2214 C  C   . ARG   A 1 283 ? 65.115 -4.288  -28.383 1.00 48.39  ?  298 ARG   A C   1 
ATOM   2215 O  O   . ARG   A 1 283 ? 64.832 -4.774  -29.485 1.00 44.78  ?  298 ARG   A O   1 
ATOM   2216 C  CB  . ARG   A 1 283 ? 67.043 -2.680  -28.423 1.00 45.90  ?  298 ARG   A CB  1 
ATOM   2217 C  CG  . ARG   A 1 283 ? 67.658 -3.302  -29.624 1.00 62.04  ?  298 ARG   A CG  1 
ATOM   2218 C  CD  . ARG   A 1 283 ? 69.140 -3.019  -29.601 1.00 63.47  ?  298 ARG   A CD  1 
ATOM   2219 N  NE  . ARG   A 1 283 ? 69.807 -3.539  -28.410 1.00 61.14  ?  298 ARG   A NE  1 
ATOM   2220 C  CZ  . ARG   A 1 283 ? 70.310 -4.764  -28.310 1.00 62.93  ?  298 ARG   A CZ  1 
ATOM   2221 N  NH1 . ARG   A 1 283 ? 70.133 -5.665  -29.262 1.00 58.60  ?  298 ARG   A NH1 1 
ATOM   2222 N  NH2 . ARG   A 1 283 ? 71.014 -5.092  -27.230 1.00 53.22  ?  298 ARG   A NH2 1 
ATOM   2223 N  N   . LYS   A 1 284 ? 65.054 -5.008  -27.267 1.00 41.41  ?  299 LYS   A N   1 
ATOM   2224 C  CA  . LYS   A 1 284 ? 64.778 -6.438  -27.346 1.00 43.99  ?  299 LYS   A CA  1 
ATOM   2225 C  C   . LYS   A 1 284 ? 63.290 -6.782  -27.323 1.00 44.73  ?  299 LYS   A C   1 
ATOM   2226 O  O   . LYS   A 1 284 ? 62.942 -7.933  -27.616 1.00 42.91  ?  299 LYS   A O   1 
ATOM   2227 C  CB  . LYS   A 1 284 ? 65.509 -7.176  -26.214 1.00 39.63  ?  299 LYS   A CB  1 
ATOM   2228 C  CG  . LYS   A 1 284 ? 67.001 -7.210  -26.443 1.00 53.28  ?  299 LYS   A CG  1 
ATOM   2229 C  CD  . LYS   A 1 284 ? 67.731 -7.998  -25.383 1.00 55.64  ?  299 LYS   A CD  1 
ATOM   2230 C  CE  . LYS   A 1 284 ? 69.202 -8.143  -25.724 1.00 58.03  ?  299 LYS   A CE  1 
ATOM   2231 N  NZ  . LYS   A 1 284 ? 69.984 -8.610  -24.538 1.00 62.08  ?  299 LYS   A NZ  1 
ATOM   2232 N  N   . ILE   A 1 285 ? 62.405 -5.824  -27.019 1.00 42.66  ?  300 ILE   A N   1 
ATOM   2233 C  CA  . ILE   A 1 285 ? 60.978 -6.143  -26.905 1.00 40.13  ?  300 ILE   A CA  1 
ATOM   2234 C  C   . ILE   A 1 285 ? 60.435 -6.676  -28.224 1.00 47.72  ?  300 ILE   A C   1 
ATOM   2235 O  O   . ILE   A 1 285 ? 59.677 -7.652  -28.243 1.00 40.78  ?  300 ILE   A O   1 
ATOM   2236 C  CB  . ILE   A 1 285 ? 60.177 -4.919  -26.418 1.00 52.28  ?  300 ILE   A CB  1 
ATOM   2237 C  CG1 . ILE   A 1 285 ? 60.476 -4.626  -24.953 1.00 42.73  ?  300 ILE   A CG1 1 
ATOM   2238 C  CG2 . ILE   A 1 285 ? 58.682 -5.158  -26.583 1.00 51.59  ?  300 ILE   A CG2 1 
ATOM   2239 C  CD1 . ILE   A 1 285 ? 60.076 -5.769  -24.023 1.00 49.58  ?  300 ILE   A CD1 1 
ATOM   2240 N  N   . GLU   A 1 286 ? 60.811 -6.048  -29.351 1.00 43.03  ?  301 GLU   A N   1 
ATOM   2241 C  CA  . GLU   A 1 286 ? 60.308 -6.478  -30.656 1.00 45.63  ?  301 GLU   A CA  1 
ATOM   2242 C  C   . GLU   A 1 286 ? 60.785 -7.887  -30.997 1.00 49.08  ?  301 GLU   A C   1 
ATOM   2243 O  O   . GLU   A 1 286 ? 60.065 -8.664  -31.638 1.00 49.07  ?  301 GLU   A O   1 
ATOM   2244 C  CB  . GLU   A 1 286 ? 60.754 -5.488  -31.750 1.00 52.56  ?  301 GLU   A CB  1 
ATOM   2245 C  CG  . GLU   A 1 286 ? 60.477 -5.976  -33.188 1.00 74.27  ?  301 GLU   A CG  1 
ATOM   2246 C  CD  . GLU   A 1 286 ? 61.126 -5.123  -34.298 1.00 87.50  ?  301 GLU   A CD  1 
ATOM   2247 O  OE1 . GLU   A 1 286 ? 61.862 -4.155  -33.986 1.00 86.30  ?  301 GLU   A OE1 1 
ATOM   2248 O  OE2 . GLU   A 1 286 ? 60.890 -5.432  -35.493 1.00 73.91  ?  301 GLU   A OE2 1 
ATOM   2249 N  N   A ARG   A 1 287 ? 62.007 -8.224  -30.581 0.50 49.20  ?  302 ARG   A N   1 
ATOM   2250 N  N   B ARG   A 1 287 ? 62.007 -8.230  -30.593 0.50 49.20  ?  302 ARG   A N   1 
ATOM   2251 C  CA  A ARG   A 1 287 ? 62.530 -9.575  -30.749 0.50 49.39  ?  302 ARG   A CA  1 
ATOM   2252 C  CA  B ARG   A 1 287 ? 62.503 -9.586  -30.795 0.50 49.37  ?  302 ARG   A CA  1 
ATOM   2253 C  C   A ARG   A 1 287 ? 61.619 -10.599 -30.084 0.50 45.14  ?  302 ARG   A C   1 
ATOM   2254 C  C   B ARG   A 1 287 ? 61.626 -10.611 -30.082 0.50 45.13  ?  302 ARG   A C   1 
ATOM   2255 O  O   A ARG   A 1 287 ? 61.396 -11.689 -30.620 0.50 46.33  ?  302 ARG   A O   1 
ATOM   2256 O  O   B ARG   A 1 287 ? 61.437 -11.723 -30.585 0.50 46.36  ?  302 ARG   A O   1 
ATOM   2257 C  CB  A ARG   A 1 287 ? 63.946 -9.630  -30.169 0.50 53.50  ?  302 ARG   A CB  1 
ATOM   2258 C  CB  B ARG   A 1 287 ? 63.954 -9.664  -30.314 0.50 53.55  ?  302 ARG   A CB  1 
ATOM   2259 C  CG  A ARG   A 1 287 ? 64.710 -10.922 -30.365 0.50 63.44  ?  302 ARG   A CG  1 
ATOM   2260 C  CG  B ARG   A 1 287 ? 64.668 -10.944 -30.677 0.50 62.98  ?  302 ARG   A CG  1 
ATOM   2261 C  CD  A ARG   A 1 287 ? 66.116 -10.761 -29.786 0.50 65.85  ?  302 ARG   A CD  1 
ATOM   2262 C  CD  B ARG   A 1 287 ? 65.275 -11.578 -29.437 0.50 63.46  ?  302 ARG   A CD  1 
ATOM   2263 N  NE  A ARG   A 1 287 ? 66.776 -9.566  -30.303 0.50 64.66  ?  302 ARG   A NE  1 
ATOM   2264 N  NE  B ARG   A 1 287 ? 65.784 -12.916 -29.703 0.50 58.05  ?  302 ARG   A NE  1 
ATOM   2265 C  CZ  A ARG   A 1 287 ? 67.968 -9.136  -29.912 0.50 61.10  ?  302 ARG   A CZ  1 
ATOM   2266 C  CZ  B ARG   A 1 287 ? 65.015 -13.981 -29.866 0.50 52.49  ?  302 ARG   A CZ  1 
ATOM   2267 N  NH1 A ARG   A 1 287 ? 68.665 -9.774  -28.985 0.50 53.27  ?  302 ARG   A NH1 1 
ATOM   2268 N  NH1 B ARG   A 1 287 ? 63.697 -13.881 -29.904 0.50 49.98  ?  302 ARG   A NH1 1 
ATOM   2269 N  NH2 A ARG   A 1 287 ? 68.472 -8.038  -30.465 0.50 59.02  ?  302 ARG   A NH2 1 
ATOM   2270 N  NH2 B ARG   A 1 287 ? 65.583 -15.177 -29.990 0.50 61.98  ?  302 ARG   A NH2 1 
ATOM   2271 N  N   . LEU   A 1 288 ? 61.047 -10.241 -28.938 1.00 39.29  ?  303 LEU   A N   1 
ATOM   2272 C  CA  . LEU   A 1 288 ? 60.228 -11.178 -28.169 1.00 39.36  ?  303 LEU   A CA  1 
ATOM   2273 C  C   . LEU   A 1 288 ? 58.906 -11.480 -28.849 1.00 38.16  ?  303 LEU   A C   1 
ATOM   2274 O  O   . LEU   A 1 288 ? 58.331 -12.550 -28.622 1.00 40.50  ?  303 LEU   A O   1 
ATOM   2275 C  CB  . LEU   A 1 288 ? 59.948 -10.603 -26.777 1.00 33.50  ?  303 LEU   A CB  1 
ATOM   2276 C  CG  . LEU   A 1 288 ? 61.154 -10.331 -25.866 1.00 40.31  ?  303 LEU   A CG  1 
ATOM   2277 C  CD1 . LEU   A 1 288 ? 60.687 -9.875  -24.493 1.00 38.94  ?  303 LEU   A CD1 1 
ATOM   2278 C  CD2 . LEU   A 1 288 ? 62.010 -11.586 -25.717 1.00 42.72  ?  303 LEU   A CD2 1 
ATOM   2279 N  N   . PHE   A 1 289 ? 58.378 -10.546 -29.639 1.00 39.29  ?  304 PHE   A N   1 
ATOM   2280 C  CA  . PHE   A 1 289 ? 57.122 -10.805 -30.341 1.00 35.29  ?  304 PHE   A CA  1 
ATOM   2281 C  C   . PHE   A 1 289 ? 57.326 -11.388 -31.727 1.00 38.11  ?  304 PHE   A C   1 
ATOM   2282 O  O   . PHE   A 1 289 ? 56.339 -11.774 -32.372 1.00 40.81  ?  304 PHE   A O   1 
ATOM   2283 C  CB  . PHE   A 1 289 ? 56.294 -9.516  -30.447 1.00 38.43  ?  304 PHE   A CB  1 
ATOM   2284 C  CG  . PHE   A 1 289 ? 55.573 -9.148  -29.165 1.00 36.59  ?  304 PHE   A CG  1 
ATOM   2285 C  CD1 . PHE   A 1 289 ? 54.426 -9.834  -28.776 1.00 30.25  ?  304 PHE   A CD1 1 
ATOM   2286 C  CD2 . PHE   A 1 289 ? 56.021 -8.105  -28.382 1.00 35.78  ?  304 PHE   A CD2 1 
ATOM   2287 C  CE1 . PHE   A 1 289 ? 53.763 -9.488  -27.601 1.00 35.86  ?  304 PHE   A CE1 1 
ATOM   2288 C  CE2 . PHE   A 1 289 ? 55.353 -7.749  -27.206 1.00 38.33  ?  304 PHE   A CE2 1 
ATOM   2289 C  CZ  . PHE   A 1 289 ? 54.228 -8.446  -26.822 1.00 35.86  ?  304 PHE   A CZ  1 
ATOM   2290 N  N   . SER   A 1 290 ? 58.569 -11.461 -32.199 1.00 38.98  ?  305 SER   A N   1 
ATOM   2291 C  CA  . SER   A 1 290 ? 58.854 -11.886 -33.569 1.00 41.33  ?  305 SER   A CA  1 
ATOM   2292 C  C   . SER   A 1 290 ? 58.856 -13.410 -33.685 1.00 38.92  ?  305 SER   A C   1 
ATOM   2293 O  O   . SER   A 1 290 ? 59.627 -14.081 -32.990 1.00 40.88  ?  305 SER   A O   1 
ATOM   2294 C  CB  . SER   A 1 290 ? 60.209 -11.333 -34.015 1.00 38.06  ?  305 SER   A CB  1 
ATOM   2295 O  OG  . SER   A 1 290 ? 60.713 -12.109 -35.092 1.00 46.63  ?  305 SER   A OG  1 
ATOM   2296 N  N   . TYR   A 1 291 ? 58.039 -13.957 -34.603 1.00 36.66  ?  306 TYR   A N   1 
ATOM   2297 C  CA  . TYR   A 1 291 ? 58.120 -15.388 -34.912 1.00 43.68  ?  306 TYR   A CA  1 
ATOM   2298 C  C   . TYR   A 1 291 ? 59.511 -15.760 -35.397 1.00 47.09  ?  306 TYR   A C   1 
ATOM   2299 O  O   . TYR   A 1 291 ? 60.085 -16.779 -34.979 1.00 39.69  ?  306 TYR   A O   1 
ATOM   2300 C  CB  . TYR   A 1 291 ? 57.091 -15.799 -35.986 1.00 37.58  ?  306 TYR   A CB  1 
ATOM   2301 C  CG  . TYR   A 1 291 ? 55.664 -15.474 -35.629 1.00 37.01  ?  306 TYR   A CG  1 
ATOM   2302 C  CD1 . TYR   A 1 291 ? 54.966 -16.245 -34.702 1.00 35.76  ?  306 TYR   A CD1 1 
ATOM   2303 C  CD2 . TYR   A 1 291 ? 55.012 -14.403 -36.220 1.00 40.76  ?  306 TYR   A CD2 1 
ATOM   2304 C  CE1 . TYR   A 1 291 ? 53.666 -15.945 -34.359 1.00 34.33  ?  306 TYR   A CE1 1 
ATOM   2305 C  CE2 . TYR   A 1 291 ? 53.688 -14.079 -35.864 1.00 36.75  ?  306 TYR   A CE2 1 
ATOM   2306 C  CZ  . TYR   A 1 291 ? 53.030 -14.865 -34.937 1.00 40.94  ?  306 TYR   A CZ  1 
ATOM   2307 O  OH  . TYR   A 1 291 ? 51.728 -14.586 -34.578 1.00 37.90  ?  306 TYR   A OH  1 
ATOM   2308 N  N   . MET   A 1 292 ? 60.057 -14.963 -36.319 1.00 42.52  ?  307 MET   A N   1 
ATOM   2309 C  CA  . MET   A 1 292 ? 61.302 -15.361 -36.962 1.00 42.23  ?  307 MET   A CA  1 
ATOM   2310 C  C   . MET   A 1 292 ? 62.440 -15.407 -35.955 1.00 46.78  ?  307 MET   A C   1 
ATOM   2311 O  O   . MET   A 1 292 ? 63.227 -16.358 -35.940 1.00 48.97  ?  307 MET   A O   1 
ATOM   2312 C  CB  . MET   A 1 292 ? 61.657 -14.421 -38.106 1.00 43.54  ?  307 MET   A CB  1 
ATOM   2313 C  CG  . MET   A 1 292 ? 62.950 -14.827 -38.785 1.00 59.83  ?  307 MET   A CG  1 
ATOM   2314 S  SD  . MET   A 1 292 ? 63.552 -13.576 -39.918 1.00 65.77  ?  307 MET   A SD  1 
ATOM   2315 C  CE  . MET   A 1 292 ? 62.696 -14.004 -41.397 1.00 73.49  ?  307 MET   A CE  1 
ATOM   2316 N  N   . TYR   A 1 293 ? 62.552 -14.379 -35.104 1.00 43.39  ?  308 TYR   A N   1 
ATOM   2317 C  CA  . TYR   A 1 293 ? 63.677 -14.354 -34.177 1.00 52.37  ?  308 TYR   A CA  1 
ATOM   2318 C  C   . TYR   A 1 293 ? 63.506 -15.369 -33.056 1.00 54.15  ?  308 TYR   A C   1 
ATOM   2319 O  O   . TYR   A 1 293 ? 64.506 -15.797 -32.473 1.00 54.40  ?  308 TYR   A O   1 
ATOM   2320 C  CB  . TYR   A 1 293 ? 63.876 -12.941 -33.605 1.00 48.16  ?  308 TYR   A CB  1 
ATOM   2321 C  CG  . TYR   A 1 293 ? 64.167 -11.886 -34.670 1.00 53.74  ?  308 TYR   A CG  1 
ATOM   2322 C  CD1 . TYR   A 1 293 ? 65.023 -12.155 -35.737 1.00 54.97  ?  308 TYR   A CD1 1 
ATOM   2323 C  CD2 . TYR   A 1 293 ? 63.563 -10.631 -34.617 1.00 57.87  ?  308 TYR   A CD2 1 
ATOM   2324 C  CE1 . TYR   A 1 293 ? 65.279 -11.185 -36.726 1.00 65.65  ?  308 TYR   A CE1 1 
ATOM   2325 C  CE2 . TYR   A 1 293 ? 63.801 -9.664  -35.591 1.00 58.24  ?  308 TYR   A CE2 1 
ATOM   2326 C  CZ  . TYR   A 1 293 ? 64.658 -9.939  -36.642 1.00 70.12  ?  308 TYR   A CZ  1 
ATOM   2327 O  OH  . TYR   A 1 293 ? 64.892 -8.961  -37.595 1.00 68.08  ?  308 TYR   A OH  1 
ATOM   2328 N  N   . SER   A 1 294 ? 62.269 -15.783 -32.770 1.00 49.94  ?  309 SER   A N   1 
ATOM   2329 C  CA  . SER   A 1 294 ? 61.979 -16.783 -31.751 1.00 45.45  ?  309 SER   A CA  1 
ATOM   2330 C  C   . SER   A 1 294 ? 62.046 -18.217 -32.257 1.00 50.70  ?  309 SER   A C   1 
ATOM   2331 O  O   . SER   A 1 294 ? 61.680 -19.130 -31.507 1.00 46.78  ?  309 SER   A O   1 
ATOM   2332 C  CB  . SER   A 1 294 ? 60.590 -16.533 -31.163 1.00 47.29  ?  309 SER   A CB  1 
ATOM   2333 O  OG  . SER   A 1 294 ? 60.454 -15.207 -30.665 1.00 44.13  ?  309 SER   A OG  1 
ATOM   2334 N  N   . THR   A 1 295 ? 62.487 -18.447 -33.495 1.00 47.84  ?  310 THR   A N   1 
ATOM   2335 C  CA  . THR   A 1 295 ? 62.442 -19.766 -34.121 1.00 46.62  ?  310 THR   A CA  1 
ATOM   2336 C  C   . THR   A 1 295 ? 63.825 -20.408 -34.100 1.00 58.95  ?  310 THR   A C   1 
ATOM   2337 O  O   . THR   A 1 295 ? 64.812 -19.783 -34.527 1.00 60.59  ?  310 THR   A O   1 
ATOM   2338 C  CB  . THR   A 1 295 ? 61.934 -19.679 -35.575 1.00 46.98  ?  310 THR   A CB  1 
ATOM   2339 O  OG1 . THR   A 1 295 ? 60.596 -19.146 -35.604 1.00 47.80  ?  310 THR   A OG1 1 
ATOM   2340 C  CG2 . THR   A 1 295 ? 61.932 -21.060 -36.258 1.00 46.94  ?  310 THR   A CG2 1 
ATOM   2341 N  N   . ALA   A 1 296 ? 63.886 -21.663 -33.646 1.00 64.85  ?  311 ALA   A N   1 
ATOM   2342 C  CA  . ALA   A 1 296 ? 65.122 -22.441 -33.603 1.00 61.49  ?  311 ALA   A CA  1 
ATOM   2343 C  C   . ALA   A 1 296 ? 64.763 -23.915 -33.752 1.00 59.81  ?  311 ALA   A C   1 
ATOM   2344 O  O   . ALA   A 1 296 ? 63.579 -24.280 -33.726 1.00 58.48  ?  311 ALA   A O   1 
ATOM   2345 C  CB  . ALA   A 1 296 ? 65.884 -22.194 -32.293 1.00 65.46  ?  311 ALA   A CB  1 
ATOM   2346 N  N   . PRO   A 1 297 ? 65.752 -24.791 -33.959 1.00 79.20  ?  312 PRO   A N   1 
ATOM   2347 C  CA  . PRO   A 1 297 ? 65.436 -26.223 -34.056 1.00 80.00  ?  312 PRO   A CA  1 
ATOM   2348 C  C   . PRO   A 1 297 ? 64.882 -26.790 -32.750 1.00 83.93  ?  312 PRO   A C   1 
ATOM   2349 O  O   . PRO   A 1 297 ? 65.153 -26.296 -31.653 1.00 85.41  ?  312 PRO   A O   1 
ATOM   2350 C  CB  . PRO   A 1 297 ? 66.787 -26.869 -34.402 1.00 72.33  ?  312 PRO   A CB  1 
ATOM   2351 C  CG  . PRO   A 1 297 ? 67.540 -25.778 -35.077 1.00 72.47  ?  312 PRO   A CG  1 
ATOM   2352 C  CD  . PRO   A 1 297 ? 67.133 -24.508 -34.398 1.00 68.31  ?  312 PRO   A CD  1 
ATOM   2353 N  N   . THR   A 1 298 ? 64.098 -27.864 -32.899 1.00 96.05  ?  313 THR   A N   1 
ATOM   2354 C  CA  . THR   A 1 298 ? 63.249 -28.435 -31.850 1.00 96.43  ?  313 THR   A CA  1 
ATOM   2355 C  C   . THR   A 1 298 ? 63.893 -28.556 -30.461 1.00 97.58  ?  313 THR   A C   1 
ATOM   2356 O  O   . THR   A 1 298 ? 65.025 -29.013 -30.322 1.00 98.43  ?  313 THR   A O   1 
ATOM   2357 C  CB  . THR   A 1 298 ? 62.748 -29.840 -32.262 1.00 100.47 ?  313 THR   A CB  1 
ATOM   2358 O  OG1 . THR   A 1 298 ? 62.124 -29.770 -33.550 1.00 102.21 ?  313 THR   A OG1 1 
ATOM   2359 C  CG2 . THR   A 1 298 ? 61.746 -30.363 -31.258 1.00 108.93 ?  313 THR   A CG2 1 
ATOM   2360 N  N   . THR   A 1 306 ? 59.206 -26.024 -21.777 1.00 98.41  ?  321 THR   A N   1 
ATOM   2361 C  CA  . THR   A 1 306 ? 59.086 -24.689 -21.196 1.00 101.24 ?  321 THR   A CA  1 
ATOM   2362 C  C   . THR   A 1 306 ? 59.721 -23.597 -22.060 1.00 98.14  ?  321 THR   A C   1 
ATOM   2363 O  O   . THR   A 1 306 ? 60.698 -22.983 -21.649 1.00 91.76  ?  321 THR   A O   1 
ATOM   2364 C  CB  . THR   A 1 306 ? 59.741 -24.629 -19.793 1.00 112.30 ?  321 THR   A CB  1 
ATOM   2365 O  OG1 . THR   A 1 306 ? 61.039 -25.242 -19.837 1.00 115.42 ?  321 THR   A OG1 1 
ATOM   2366 C  CG2 . THR   A 1 306 ? 58.875 -25.335 -18.774 1.00 112.62 ?  321 THR   A CG2 1 
ATOM   2367 N  N   . PRO   A 1 307 ? 59.167 -23.347 -23.251 1.00 78.38  ?  322 PRO   A N   1 
ATOM   2368 C  CA  . PRO   A 1 307 ? 59.728 -22.295 -24.122 1.00 75.34  ?  322 PRO   A CA  1 
ATOM   2369 C  C   . PRO   A 1 307 ? 59.310 -20.910 -23.639 1.00 61.81  ?  322 PRO   A C   1 
ATOM   2370 O  O   . PRO   A 1 307 ? 58.124 -20.611 -23.500 1.00 70.75  ?  322 PRO   A O   1 
ATOM   2371 C  CB  . PRO   A 1 307 ? 59.149 -22.626 -25.496 1.00 68.30  ?  322 PRO   A CB  1 
ATOM   2372 C  CG  . PRO   A 1 307 ? 57.840 -23.271 -25.182 1.00 77.00  ?  322 PRO   A CG  1 
ATOM   2373 C  CD  . PRO   A 1 307 ? 57.995 -23.995 -23.861 1.00 83.48  ?  322 PRO   A CD  1 
ATOM   2374 N  N   . LEU   A 1 308 ? 60.299 -20.064 -23.356 1.00 51.18  ?  323 LEU   A N   1 
ATOM   2375 C  CA  . LEU   A 1 308 ? 60.027 -18.730 -22.848 1.00 57.34  ?  323 LEU   A CA  1 
ATOM   2376 C  C   . LEU   A 1 308 ? 59.919 -17.736 -23.996 1.00 48.99  ?  323 LEU   A C   1 
ATOM   2377 O  O   . LEU   A 1 308 ? 60.222 -18.050 -25.150 1.00 46.33  ?  323 LEU   A O   1 
ATOM   2378 C  CB  . LEU   A 1 308 ? 61.121 -18.297 -21.879 1.00 54.08  ?  323 LEU   A CB  1 
ATOM   2379 C  CG  . LEU   A 1 308 ? 61.303 -19.211 -20.670 1.00 64.35  ?  323 LEU   A CG  1 
ATOM   2380 C  CD1 . LEU   A 1 308 ? 62.637 -18.901 -20.029 1.00 66.41  ?  323 LEU   A CD1 1 
ATOM   2381 C  CD2 . LEU   A 1 308 ? 60.165 -19.028 -19.684 1.00 56.80  ?  323 LEU   A CD2 1 
ATOM   2382 N  N   . ALA   A 1 309 ? 59.505 -16.511 -23.663 1.00 43.83  ?  324 ALA   A N   1 
ATOM   2383 C  CA  . ALA   A 1 309 ? 59.517 -15.413 -24.616 1.00 46.39  ?  324 ALA   A CA  1 
ATOM   2384 C  C   . ALA   A 1 309 ? 60.867 -15.352 -25.322 1.00 49.14  ?  324 ALA   A C   1 
ATOM   2385 O  O   . ALA   A 1 309 ? 61.918 -15.512 -24.693 1.00 45.77  ?  324 ALA   A O   1 
ATOM   2386 C  CB  . ALA   A 1 309 ? 59.213 -14.091 -23.892 1.00 37.34  ?  324 ALA   A CB  1 
ATOM   2387 N  N   . GLY   A 1 310 ? 60.831 -15.196 -26.653 1.00 43.14  ?  325 GLY   A N   1 
ATOM   2388 C  CA  . GLY   A 1 310 ? 62.028 -15.198 -27.470 1.00 43.33  ?  325 GLY   A CA  1 
ATOM   2389 C  C   . GLY   A 1 310 ? 62.487 -16.556 -27.980 1.00 51.89  ?  325 GLY   A C   1 
ATOM   2390 O  O   . GLY   A 1 310 ? 63.426 -16.613 -28.791 1.00 51.95  ?  325 GLY   A O   1 
ATOM   2391 N  N   . PHE   A 1 311 ? 61.857 -17.653 -27.557 1.00 46.01  ?  326 PHE   A N   1 
ATOM   2392 C  CA  . PHE   A 1 311 ? 62.324 -18.973 -27.946 1.00 52.43  ?  326 PHE   A CA  1 
ATOM   2393 C  C   . PHE   A 1 311 ? 61.197 -19.877 -28.428 1.00 51.38  ?  326 PHE   A C   1 
ATOM   2394 O  O   . PHE   A 1 311 ? 61.446 -21.044 -28.751 1.00 58.39  ?  326 PHE   A O   1 
ATOM   2395 C  CB  . PHE   A 1 311 ? 63.095 -19.624 -26.788 1.00 52.67  ?  326 PHE   A CB  1 
ATOM   2396 C  CG  . PHE   A 1 311 ? 64.306 -18.821 -26.366 1.00 62.50  ?  326 PHE   A CG  1 
ATOM   2397 C  CD1 . PHE   A 1 311 ? 65.507 -18.938 -27.061 1.00 69.11  ?  326 PHE   A CD1 1 
ATOM   2398 C  CD2 . PHE   A 1 311 ? 64.234 -17.927 -25.307 1.00 57.23  ?  326 PHE   A CD2 1 
ATOM   2399 C  CE1 . PHE   A 1 311 ? 66.624 -18.197 -26.689 1.00 67.14  ?  326 PHE   A CE1 1 
ATOM   2400 C  CE2 . PHE   A 1 311 ? 65.350 -17.174 -24.937 1.00 58.85  ?  326 PHE   A CE2 1 
ATOM   2401 C  CZ  . PHE   A 1 311 ? 66.538 -17.309 -25.628 1.00 55.62  ?  326 PHE   A CZ  1 
ATOM   2402 N  N   . GLY   A 1 312 ? 59.979 -19.367 -28.511 1.00 53.66  ?  327 GLY   A N   1 
ATOM   2403 C  CA  . GLY   A 1 312 ? 58.895 -20.071 -29.151 1.00 43.31  ?  327 GLY   A CA  1 
ATOM   2404 C  C   . GLY   A 1 312 ? 57.833 -19.054 -29.486 1.00 46.28  ?  327 GLY   A C   1 
ATOM   2405 O  O   . GLY   A 1 312 ? 58.063 -17.845 -29.414 1.00 43.41  ?  327 GLY   A O   1 
ATOM   2406 N  N   . TYR   A 1 313 ? 56.649 -19.547 -29.833 1.00 42.66  ?  328 TYR   A N   1 
ATOM   2407 C  CA  . TYR   A 1 313 ? 55.575 -18.664 -30.279 1.00 45.33  ?  328 TYR   A CA  1 
ATOM   2408 C  C   . TYR   A 1 313 ? 54.539 -18.349 -29.185 1.00 43.97  ?  328 TYR   A C   1 
ATOM   2409 O  O   . TYR   A 1 313 ? 53.516 -17.717 -29.474 1.00 36.88  ?  328 TYR   A O   1 
ATOM   2410 C  CB  . TYR   A 1 313 ? 54.896 -19.273 -31.508 1.00 40.24  ?  328 TYR   A CB  1 
ATOM   2411 C  CG  . TYR   A 1 313 ? 55.784 -19.407 -32.746 1.00 41.24  ?  328 TYR   A CG  1 
ATOM   2412 C  CD1 . TYR   A 1 313 ? 57.098 -18.931 -32.767 1.00 36.83  ?  328 TYR   A CD1 1 
ATOM   2413 C  CD2 . TYR   A 1 313 ? 55.285 -19.984 -33.917 1.00 46.33  ?  328 TYR   A CD2 1 
ATOM   2414 C  CE1 . TYR   A 1 313 ? 57.904 -19.061 -33.931 1.00 42.75  ?  328 TYR   A CE1 1 
ATOM   2415 C  CE2 . TYR   A 1 313 ? 56.069 -20.117 -35.062 1.00 42.30  ?  328 TYR   A CE2 1 
ATOM   2416 C  CZ  . TYR   A 1 313 ? 57.374 -19.650 -35.065 1.00 43.70  ?  328 TYR   A CZ  1 
ATOM   2417 O  OH  . TYR   A 1 313 ? 58.133 -19.800 -36.220 1.00 49.56  ?  328 TYR   A OH  1 
ATOM   2418 N  N   . GLY   A 1 314 ? 54.792 -18.733 -27.933 1.00 39.11  ?  329 GLY   A N   1 
ATOM   2419 C  CA  . GLY   A 1 314 ? 53.784 -18.530 -26.894 1.00 40.27  ?  329 GLY   A CA  1 
ATOM   2420 C  C   . GLY   A 1 314 ? 53.345 -17.084 -26.738 1.00 37.07  ?  329 GLY   A C   1 
ATOM   2421 O  O   . GLY   A 1 314 ? 52.147 -16.781 -26.685 1.00 37.41  ?  329 GLY   A O   1 
ATOM   2422 N  N   . LEU   A 1 315 ? 54.307 -16.163 -26.691 1.00 35.10  ?  330 LEU   A N   1 
ATOM   2423 C  CA  . LEU   A 1 315 ? 53.969 -14.752 -26.510 1.00 32.11  ?  330 LEU   A CA  1 
ATOM   2424 C  C   . LEU   A 1 315 ? 53.239 -14.147 -27.711 1.00 34.39  ?  330 LEU   A C   1 
ATOM   2425 O  O   . LEU   A 1 315 ? 52.186 -13.508 -27.514 1.00 33.04  ?  330 LEU   A O   1 
ATOM   2426 C  CB  . LEU   A 1 315 ? 55.237 -13.959 -26.166 1.00 37.07  ?  330 LEU   A CB  1 
ATOM   2427 C  CG  . LEU   A 1 315 ? 55.067 -12.451 -25.897 1.00 43.23  ?  330 LEU   A CG  1 
ATOM   2428 C  CD1 . LEU   A 1 315 ? 54.076 -12.176 -24.725 1.00 38.32  ?  330 LEU   A CD1 1 
ATOM   2429 C  CD2 . LEU   A 1 315 ? 56.434 -11.766 -25.634 1.00 36.73  ?  330 LEU   A CD2 1 
ATOM   2430 N  N   . PRO   A 1 316 ? 53.733 -14.248 -28.948 1.00 32.41  ?  331 PRO   A N   1 
ATOM   2431 C  CA  . PRO   A 1 316 ? 52.972 -13.627 -30.049 1.00 30.49  ?  331 PRO   A CA  1 
ATOM   2432 C  C   . PRO   A 1 316 ? 51.621 -14.297 -30.287 1.00 33.29  ?  331 PRO   A C   1 
ATOM   2433 O  O   . PRO   A 1 316 ? 50.659 -13.610 -30.646 1.00 36.57  ?  331 PRO   A O   1 
ATOM   2434 C  CB  . PRO   A 1 316 ? 53.909 -13.773 -31.249 1.00 33.94  ?  331 PRO   A CB  1 
ATOM   2435 C  CG  . PRO   A 1 316 ? 54.718 -15.024 -30.947 1.00 35.32  ?  331 PRO   A CG  1 
ATOM   2436 C  CD  . PRO   A 1 316 ? 54.989 -14.867 -29.425 1.00 31.96  ?  331 PRO   A CD  1 
ATOM   2437 N  N   . ILE   A 1 317 ? 51.494 -15.602 -30.036 1.00 36.88  ?  332 ILE   A N   1 
ATOM   2438 C  CA  . ILE   A 1 317 ? 50.175 -16.223 -30.145 1.00 35.90  ?  332 ILE   A CA  1 
ATOM   2439 C  C   . ILE   A 1 317 ? 49.267 -15.779 -28.992 1.00 35.15  ?  332 ILE   A C   1 
ATOM   2440 O  O   . ILE   A 1 317 ? 48.066 -15.553 -29.193 1.00 34.24  ?  332 ILE   A O   1 
ATOM   2441 C  CB  . ILE   A 1 317 ? 50.310 -17.752 -30.232 1.00 36.69  ?  332 ILE   A CB  1 
ATOM   2442 C  CG1 . ILE   A 1 317 ? 50.832 -18.140 -31.620 1.00 39.69  ?  332 ILE   A CG1 1 
ATOM   2443 C  CG2 . ILE   A 1 317 ? 48.949 -18.451 -30.026 1.00 38.68  ?  332 ILE   A CG2 1 
ATOM   2444 C  CD1 . ILE   A 1 317 ? 51.054 -19.627 -31.765 1.00 46.31  ?  332 ILE   A CD1 1 
ATOM   2445 N  N   . SER   A 1 318 ? 49.821 -15.600 -27.777 1.00 35.50  ?  333 SER   A N   1 
ATOM   2446 C  CA  . SER   A 1 318 ? 49.017 -15.002 -26.702 1.00 33.68  ?  333 SER   A CA  1 
ATOM   2447 C  C   . SER   A 1 318 ? 48.491 -13.624 -27.104 1.00 34.64  ?  333 SER   A C   1 
ATOM   2448 O  O   . SER   A 1 318 ? 47.335 -13.282 -26.810 1.00 35.68  ?  333 SER   A O   1 
ATOM   2449 C  CB  . SER   A 1 318 ? 49.824 -14.919 -25.392 1.00 29.78  ?  333 SER   A CB  1 
ATOM   2450 O  OG  . SER   A 1 318 ? 50.095 -16.234 -24.895 1.00 34.82  ?  333 SER   A OG  1 
ATOM   2451 N  N   . ARG   A 1 319 ? 49.311 -12.810 -27.791 1.00 32.02  ?  334 ARG   A N   1 
ATOM   2452 C  CA  . ARG   A 1 319 ? 48.798 -11.520 -28.256 1.00 32.67  ?  334 ARG   A CA  1 
ATOM   2453 C  C   . ARG   A 1 319 ? 47.675 -11.688 -29.280 1.00 35.68  ?  334 ARG   A C   1 
ATOM   2454 O  O   . ARG   A 1 319 ? 46.742 -10.876 -29.305 1.00 32.11  ?  334 ARG   A O   1 
ATOM   2455 C  CB  . ARG   A 1 319 ? 49.931 -10.651 -28.836 1.00 31.94  ?  334 ARG   A CB  1 
ATOM   2456 C  CG  . ARG   A 1 319 ? 49.473 -9.257  -29.304 1.00 36.12  ?  334 ARG   A CG  1 
ATOM   2457 C  CD  . ARG   A 1 319 ? 50.653 -8.272  -29.541 1.00 34.73  ?  334 ARG   A CD  1 
ATOM   2458 N  NE  . ARG   A 1 319 ? 51.509 -8.691  -30.656 1.00 38.00  ?  334 ARG   A NE  1 
ATOM   2459 C  CZ  . ARG   A 1 319 ? 52.575 -8.023  -31.088 1.00 39.71  ?  334 ARG   A CZ  1 
ATOM   2460 N  NH1 . ARG   A 1 319 ? 53.013 -6.937  -30.467 1.00 36.51  ?  334 ARG   A NH1 1 
ATOM   2461 N  NH2 . ARG   A 1 319 ? 53.222 -8.457  -32.176 1.00 39.34  ?  334 ARG   A NH2 1 
ATOM   2462 N  N   . LEU   A 1 320 ? 47.739 -12.720 -30.140 1.00 34.00  ?  335 LEU   A N   1 
ATOM   2463 C  CA  . LEU   A 1 320 ? 46.644 -12.927 -31.086 1.00 32.20  ?  335 LEU   A CA  1 
ATOM   2464 C  C   . LEU   A 1 320 ? 45.356 -13.308 -30.365 1.00 33.02  ?  335 LEU   A C   1 
ATOM   2465 O  O   . LEU   A 1 320 ? 44.267 -12.894 -30.777 1.00 32.41  ?  335 LEU   A O   1 
ATOM   2466 C  CB  . LEU   A 1 320 ? 47.007 -14.010 -32.115 1.00 30.87  ?  335 LEU   A CB  1 
ATOM   2467 C  CG  . LEU   A 1 320 ? 48.149 -13.624 -33.069 1.00 41.82  ?  335 LEU   A CG  1 
ATOM   2468 C  CD1 . LEU   A 1 320 ? 48.490 -14.782 -33.975 1.00 36.64  ?  335 LEU   A CD1 1 
ATOM   2469 C  CD2 . LEU   A 1 320 ? 47.776 -12.384 -33.926 1.00 38.30  ?  335 LEU   A CD2 1 
ATOM   2470 N  N   . TYR   A 1 321 ? 45.451 -14.103 -29.290 1.00 34.68  ?  336 TYR   A N   1 
ATOM   2471 C  CA  . TYR   A 1 321 ? 44.241 -14.408 -28.520 1.00 33.69  ?  336 TYR   A CA  1 
ATOM   2472 C  C   . TYR   A 1 321 ? 43.582 -13.135 -28.011 1.00 32.16  ?  336 TYR   A C   1 
ATOM   2473 O  O   . TYR   A 1 321 ? 42.362 -12.982 -28.126 1.00 35.88  ?  336 TYR   A O   1 
ATOM   2474 C  CB  . TYR   A 1 321 ? 44.551 -15.347 -27.353 1.00 33.48  ?  336 TYR   A CB  1 
ATOM   2475 C  CG  . TYR   A 1 321 ? 44.630 -16.797 -27.741 1.00 37.49  ?  336 TYR   A CG  1 
ATOM   2476 C  CD1 . TYR   A 1 321 ? 43.550 -17.437 -28.342 1.00 39.79  ?  336 TYR   A CD1 1 
ATOM   2477 C  CD2 . TYR   A 1 321 ? 45.773 -17.538 -27.501 1.00 48.08  ?  336 TYR   A CD2 1 
ATOM   2478 C  CE1 . TYR   A 1 321 ? 43.621 -18.774 -28.702 1.00 41.68  ?  336 TYR   A CE1 1 
ATOM   2479 C  CE2 . TYR   A 1 321 ? 45.849 -18.873 -27.853 1.00 51.28  ?  336 TYR   A CE2 1 
ATOM   2480 C  CZ  . TYR   A 1 321 ? 44.772 -19.487 -28.452 1.00 53.52  ?  336 TYR   A CZ  1 
ATOM   2481 O  OH  . TYR   A 1 321 ? 44.854 -20.826 -28.793 1.00 52.08  ?  336 TYR   A OH  1 
ATOM   2482 N  N   . ALA   A 1 322 ? 44.374 -12.184 -27.498 1.00 33.84  ?  337 ALA   A N   1 
ATOM   2483 C  CA  . ALA   A 1 322 ? 43.806 -10.915 -27.043 1.00 36.60  ?  337 ALA   A CA  1 
ATOM   2484 C  C   . ALA   A 1 322 ? 43.194 -10.141 -28.197 1.00 36.11  ?  337 ALA   A C   1 
ATOM   2485 O  O   . ALA   A 1 322 ? 42.071 -9.637  -28.091 1.00 37.44  ?  337 ALA   A O   1 
ATOM   2486 C  CB  . ALA   A 1 322 ? 44.873 -10.063 -26.342 1.00 31.66  ?  337 ALA   A CB  1 
ATOM   2487 N  N   . LYS   A 1 323 ? 43.920 -10.029 -29.320 1.00 35.78  ?  338 LYS   A N   1 
ATOM   2488 C  CA  . LYS   A 1 323 ? 43.378 -9.307  -30.473 1.00 35.86  ?  338 LYS   A CA  1 
ATOM   2489 C  C   . LYS   A 1 323 ? 42.153 -9.979  -31.079 1.00 35.41  ?  338 LYS   A C   1 
ATOM   2490 O  O   . LYS   A 1 323 ? 41.340 -9.295  -31.707 1.00 37.39  ?  338 LYS   A O   1 
ATOM   2491 C  CB  . LYS   A 1 323 ? 44.454 -9.149  -31.549 1.00 36.35  ?  338 LYS   A CB  1 
ATOM   2492 C  CG  . LYS   A 1 323 ? 45.548 -8.176  -31.142 1.00 42.39  ?  338 LYS   A CG  1 
ATOM   2493 C  CD  . LYS   A 1 323 ? 46.613 -8.076  -32.216 1.00 46.39  ?  338 LYS   A CD  1 
ATOM   2494 C  CE  . LYS   A 1 323 ? 47.560 -6.915  -31.936 1.00 48.67  ?  338 LYS   A CE  1 
ATOM   2495 N  NZ  . LYS   A 1 323 ? 48.803 -7.012  -32.767 1.00 62.65  ?  338 LYS   A NZ  1 
ATOM   2496 N  N   . TYR   A 1 324 ? 42.008 -11.296 -30.916 1.00 36.98  ?  339 TYR   A N   1 
ATOM   2497 C  CA  . TYR   A 1 324 ? 40.927 -12.019 -31.592 1.00 37.96  ?  339 TYR   A CA  1 
ATOM   2498 C  C   . TYR   A 1 324 ? 39.561 -11.448 -31.252 1.00 37.25  ?  339 TYR   A C   1 
ATOM   2499 O  O   . TYR   A 1 324 ? 38.681 -11.431 -32.112 1.00 38.08  ?  339 TYR   A O   1 
ATOM   2500 C  CB  . TYR   A 1 324 ? 40.994 -13.512 -31.231 1.00 35.55  ?  339 TYR   A CB  1 
ATOM   2501 C  CG  . TYR   A 1 324 ? 39.843 -14.367 -31.749 1.00 36.70  ?  339 TYR   A CG  1 
ATOM   2502 C  CD1 . TYR   A 1 324 ? 39.402 -14.270 -33.070 1.00 36.42  ?  339 TYR   A CD1 1 
ATOM   2503 C  CD2 . TYR   A 1 324 ? 39.226 -15.307 -30.919 1.00 37.94  ?  339 TYR   A CD2 1 
ATOM   2504 C  CE1 . TYR   A 1 324 ? 38.346 -15.080 -33.550 1.00 38.35  ?  339 TYR   A CE1 1 
ATOM   2505 C  CE2 . TYR   A 1 324 ? 38.189 -16.116 -31.382 1.00 41.21  ?  339 TYR   A CE2 1 
ATOM   2506 C  CZ  . TYR   A 1 324 ? 37.752 -15.994 -32.689 1.00 43.25  ?  339 TYR   A CZ  1 
ATOM   2507 O  OH  . TYR   A 1 324 ? 36.722 -16.792 -33.118 1.00 42.21  ?  339 TYR   A OH  1 
ATOM   2508 N  N   . PHE   A 1 325 ? 39.360 -10.946 -30.031 1.00 38.85  ?  340 PHE   A N   1 
ATOM   2509 C  CA  . PHE   A 1 325 ? 38.099 -10.286 -29.673 1.00 38.30  ?  340 PHE   A CA  1 
ATOM   2510 C  C   . PHE   A 1 325 ? 38.284 -8.796  -29.387 1.00 39.92  ?  340 PHE   A C   1 
ATOM   2511 O  O   . PHE   A 1 325 ? 37.673 -8.240  -28.468 1.00 38.26  ?  340 PHE   A O   1 
ATOM   2512 C  CB  . PHE   A 1 325 ? 37.443 -10.986 -28.488 1.00 35.56  ?  340 PHE   A CB  1 
ATOM   2513 C  CG  . PHE   A 1 325 ? 36.712 -12.258 -28.873 1.00 41.08  ?  340 PHE   A CG  1 
ATOM   2514 C  CD1 . PHE   A 1 325 ? 35.558 -12.206 -29.645 1.00 42.06  ?  340 PHE   A CD1 1 
ATOM   2515 C  CD2 . PHE   A 1 325 ? 37.181 -13.494 -28.462 1.00 41.00  ?  340 PHE   A CD2 1 
ATOM   2516 C  CE1 . PHE   A 1 325 ? 34.878 -13.372 -29.985 1.00 41.77  ?  340 PHE   A CE1 1 
ATOM   2517 C  CE2 . PHE   A 1 325 ? 36.509 -14.662 -28.804 1.00 42.33  ?  340 PHE   A CE2 1 
ATOM   2518 C  CZ  . PHE   A 1 325 ? 35.357 -14.598 -29.569 1.00 42.51  ?  340 PHE   A CZ  1 
ATOM   2519 N  N   . GLN   A 1 326 ? 39.154 -8.144  -30.170 1.00 37.39  ?  341 GLN   A N   1 
ATOM   2520 C  CA  . GLN   A 1 326 ? 39.352 -6.688  -30.195 1.00 37.46  ?  341 GLN   A CA  1 
ATOM   2521 C  C   . GLN   A 1 326 ? 40.140 -6.182  -28.993 1.00 40.83  ?  341 GLN   A C   1 
ATOM   2522 O  O   . GLN   A 1 326 ? 40.057 -5.002  -28.663 1.00 38.43  ?  341 GLN   A O   1 
ATOM   2523 C  CB  . GLN   A 1 326 ? 38.029 -5.905  -30.303 1.00 38.26  ?  341 GLN   A CB  1 
ATOM   2524 C  CG  . GLN   A 1 326 ? 37.098 -6.378  -31.452 1.00 43.85  ?  341 GLN   A CG  1 
ATOM   2525 C  CD  . GLN   A 1 326 ? 37.698 -6.200  -32.848 1.00 48.74  ?  341 GLN   A CD  1 
ATOM   2526 O  OE1 . GLN   A 1 326 ? 38.369 -5.212  -33.132 1.00 44.14  ?  341 GLN   A OE1 1 
ATOM   2527 N  NE2 . GLN   A 1 326 ? 37.431 -7.153  -33.735 1.00 44.15  ?  341 GLN   A NE2 1 
ATOM   2528 N  N   . GLY   A 1 327 ? 40.920 -7.054  -28.353 1.00 36.15  ?  342 GLY   A N   1 
ATOM   2529 C  CA  . GLY   A 1 327 ? 41.810 -6.677  -27.272 1.00 35.91  ?  342 GLY   A CA  1 
ATOM   2530 C  C   . GLY   A 1 327 ? 43.238 -6.520  -27.750 1.00 38.72  ?  342 GLY   A C   1 
ATOM   2531 O  O   . GLY   A 1 327 ? 43.511 -6.415  -28.946 1.00 32.81  ?  342 GLY   A O   1 
ATOM   2532 N  N   . ASP   A 1 328 ? 44.166 -6.490  -26.801 1.00 35.12  ?  343 ASP   A N   1 
ATOM   2533 C  CA  . ASP   A 1 328 ? 45.585 -6.402  -27.145 1.00 31.68  ?  343 ASP   A CA  1 
ATOM   2534 C  C   . ASP   A 1 328 ? 46.373 -6.958  -25.974 1.00 35.03  ?  343 ASP   A C   1 
ATOM   2535 O  O   . ASP   A 1 328 ? 45.828 -7.162  -24.886 1.00 33.84  ?  343 ASP   A O   1 
ATOM   2536 C  CB  . ASP   A 1 328 ? 46.016 -4.958  -27.471 1.00 33.12  ?  343 ASP   A CB  1 
ATOM   2537 C  CG  . ASP   A 1 328 ? 47.299 -4.902  -28.333 1.00 37.92  ?  343 ASP   A CG  1 
ATOM   2538 O  OD1 . ASP   A 1 328 ? 47.857 -5.973  -28.654 1.00 34.94  ?  343 ASP   A OD1 1 
ATOM   2539 O  OD2 . ASP   A 1 328 ? 47.749 -3.799  -28.695 1.00 42.70  ?  343 ASP   A OD2 1 
ATOM   2540 N  N   . LEU   A 1 329 ? 47.649 -7.243  -26.218 1.00 30.75  ?  344 LEU   A N   1 
ATOM   2541 C  CA  . LEU   A 1 329 ? 48.573 -7.657  -25.164 1.00 29.45  ?  344 LEU   A CA  1 
ATOM   2542 C  C   . LEU   A 1 329 ? 49.862 -6.878  -25.383 1.00 37.36  ?  344 LEU   A C   1 
ATOM   2543 O  O   . LEU   A 1 329 ? 50.491 -7.013  -26.440 1.00 33.86  ?  344 LEU   A O   1 
ATOM   2544 C  CB  . LEU   A 1 329 ? 48.826 -9.174  -25.195 1.00 29.63  ?  344 LEU   A CB  1 
ATOM   2545 C  CG  . LEU   A 1 329 ? 49.542 -9.860  -24.014 1.00 36.17  ?  344 LEU   A CG  1 
ATOM   2546 C  CD1 . LEU   A 1 329 ? 49.410 -11.388 -24.088 1.00 34.03  ?  344 LEU   A CD1 1 
ATOM   2547 C  CD2 . LEU   A 1 329 ? 51.048 -9.485  -23.899 1.00 34.98  ?  344 LEU   A CD2 1 
ATOM   2548 N  N   . GLN   A 1 330 ? 50.250 -6.048  -24.408 1.00 30.64  ?  345 GLN   A N   1 
ATOM   2549 C  CA  . GLN   A 1 330 ? 51.397 -5.161  -24.572 1.00 32.97  ?  345 GLN   A CA  1 
ATOM   2550 C  C   . GLN   A 1 330 ? 52.414 -5.363  -23.450 1.00 33.91  ?  345 GLN   A C   1 
ATOM   2551 O  O   . GLN   A 1 330 ? 52.060 -5.697  -22.324 1.00 30.70  ?  345 GLN   A O   1 
ATOM   2552 C  CB  . GLN   A 1 330 ? 50.947 -3.682  -24.629 1.00 38.27  ?  345 GLN   A CB  1 
ATOM   2553 C  CG  . GLN   A 1 330 ? 49.956 -3.377  -25.778 1.00 35.40  ?  345 GLN   A CG  1 
ATOM   2554 C  CD  . GLN   A 1 330 ? 49.473 -1.907  -25.829 1.00 42.40  ?  345 GLN   A CD  1 
ATOM   2555 O  OE1 . GLN   A 1 330 ? 49.801 -1.093  -24.966 1.00 39.37  ?  345 GLN   A OE1 1 
ATOM   2556 N  NE2 . GLN   A 1 330 ? 48.692 -1.577  -26.845 1.00 42.72  ?  345 GLN   A NE2 1 
ATOM   2557 N  N   . LEU   A 1 331 ? 53.686 -5.142  -23.766 1.00 31.89  ?  346 LEU   A N   1 
ATOM   2558 C  CA  . LEU   A 1 331 ? 54.780 -5.304  -22.817 1.00 34.15  ?  346 LEU   A CA  1 
ATOM   2559 C  C   . LEU   A 1 331 ? 55.540 -3.997  -22.700 1.00 37.93  ?  346 LEU   A C   1 
ATOM   2560 O  O   . LEU   A 1 331 ? 55.794 -3.329  -23.713 1.00 33.45  ?  346 LEU   A O   1 
ATOM   2561 C  CB  . LEU   A 1 331 ? 55.787 -6.376  -23.259 1.00 38.18  ?  346 LEU   A CB  1 
ATOM   2562 C  CG  . LEU   A 1 331 ? 55.635 -7.872  -23.152 1.00 46.37  ?  346 LEU   A CG  1 
ATOM   2563 C  CD1 . LEU   A 1 331 ? 56.966 -8.549  -23.585 1.00 40.26  ?  346 LEU   A CD1 1 
ATOM   2564 C  CD2 . LEU   A 1 331 ? 55.239 -8.278  -21.762 1.00 45.13  ?  346 LEU   A CD2 1 
ATOM   2565 N  N   A PHE   A 1 332 ? 55.940 -3.673  -21.466 0.49 30.97  ?  347 PHE   A N   1 
ATOM   2566 N  N   B PHE   A 1 332 ? 55.891 -3.602  -21.479 0.51 31.28  ?  347 PHE   A N   1 
ATOM   2567 C  CA  A PHE   A 1 332 ? 56.714 -2.474  -21.154 0.49 32.24  ?  347 PHE   A CA  1 
ATOM   2568 C  CA  B PHE   A 1 332 ? 56.829 -2.498  -21.322 0.51 31.87  ?  347 PHE   A CA  1 
ATOM   2569 C  C   A PHE   A 1 332 ? 57.745 -2.845  -20.092 0.49 35.93  ?  347 PHE   A C   1 
ATOM   2570 C  C   B PHE   A 1 332 ? 57.743 -2.791  -20.151 0.51 36.32  ?  347 PHE   A C   1 
ATOM   2571 O  O   A PHE   A 1 332 ? 57.380 -3.141  -18.947 0.49 37.17  ?  347 PHE   A O   1 
ATOM   2572 O  O   B PHE   A 1 332 ? 57.291 -2.972  -19.015 0.51 37.41  ?  347 PHE   A O   1 
ATOM   2573 C  CB  A PHE   A 1 332 ? 55.804 -1.343  -20.656 0.49 34.69  ?  347 PHE   A CB  1 
ATOM   2574 C  CB  B PHE   A 1 332 ? 56.149 -1.131  -21.161 0.51 36.54  ?  347 PHE   A CB  1 
ATOM   2575 C  CG  A PHE   A 1 332 ? 54.709 -0.964  -21.627 0.49 36.37  ?  347 PHE   A CG  1 
ATOM   2576 C  CG  B PHE   A 1 332 ? 55.025 -1.092  -20.175 0.51 35.26  ?  347 PHE   A CG  1 
ATOM   2577 C  CD1 A PHE   A 1 332 ? 54.963 -0.083  -22.672 0.49 33.32  ?  347 PHE   A CD1 1 
ATOM   2578 C  CD1 B PHE   A 1 332 ? 53.801 -1.675  -20.469 0.51 37.78  ?  347 PHE   A CD1 1 
ATOM   2579 C  CD2 A PHE   A 1 332 ? 53.427 -1.480  -21.488 0.49 34.28  ?  347 PHE   A CD2 1 
ATOM   2580 C  CD2 B PHE   A 1 332 ? 55.158 -0.383  -18.991 0.51 39.04  ?  347 PHE   A CD2 1 
ATOM   2581 C  CE1 A PHE   A 1 332 ? 53.957 0.270   -23.566 0.49 34.57  ?  347 PHE   A CE1 1 
ATOM   2582 C  CE1 B PHE   A 1 332 ? 52.754 -1.601  -19.571 0.51 37.16  ?  347 PHE   A CE1 1 
ATOM   2583 C  CE2 A PHE   A 1 332 ? 52.418 -1.130  -22.370 0.49 34.23  ?  347 PHE   A CE2 1 
ATOM   2584 C  CE2 B PHE   A 1 332 ? 54.111 -0.306  -18.087 0.51 37.27  ?  347 PHE   A CE2 1 
ATOM   2585 C  CZ  A PHE   A 1 332 ? 52.681 -0.258  -23.414 0.49 34.90  ?  347 PHE   A CZ  1 
ATOM   2586 C  CZ  B PHE   A 1 332 ? 52.909 -0.912  -18.379 0.51 37.95  ?  347 PHE   A CZ  1 
ATOM   2587 N  N   . SER   A 1 333 ? 59.024 -2.826  -20.448 1.00 34.09  ?  348 SER   A N   1 
ATOM   2588 C  CA  . SER   A 1 333 ? 60.055 -3.224  -19.513 1.00 34.59  ?  348 SER   A CA  1 
ATOM   2589 C  C   . SER   A 1 333 ? 60.826 -1.992  -19.038 1.00 40.22  ?  348 SER   A C   1 
ATOM   2590 O  O   . SER   A 1 333 ? 60.770 -0.918  -19.646 1.00 37.68  ?  348 SER   A O   1 
ATOM   2591 C  CB  . SER   A 1 333 ? 60.992 -4.233  -20.182 1.00 34.12  ?  348 SER   A CB  1 
ATOM   2592 O  OG  . SER   A 1 333 ? 61.771 -4.873  -19.191 1.00 36.59  ?  348 SER   A OG  1 
ATOM   2593 N  N   A MET   A 1 334 ? 61.545 -2.150  -17.928 0.54 36.35  ?  349 MET   A N   1 
ATOM   2594 N  N   B MET   A 1 334 ? 61.503 -2.152  -17.900 0.46 36.24  ?  349 MET   A N   1 
ATOM   2595 C  CA  A MET   A 1 334 ? 62.475 -1.132  -17.445 0.54 35.15  ?  349 MET   A CA  1 
ATOM   2596 C  CA  B MET   A 1 334 ? 62.466 -1.176  -17.390 0.46 35.16  ?  349 MET   A CA  1 
ATOM   2597 C  C   A MET   A 1 334 ? 63.762 -1.863  -17.094 0.54 37.13  ?  349 MET   A C   1 
ATOM   2598 C  C   B MET   A 1 334 ? 63.748 -1.948  -17.127 0.46 36.99  ?  349 MET   A C   1 
ATOM   2599 O  O   A MET   A 1 334 ? 63.851 -2.504  -16.042 0.54 37.56  ?  349 MET   A O   1 
ATOM   2600 O  O   B MET   A 1 334 ? 63.819 -2.716  -16.161 0.46 37.71  ?  349 MET   A O   1 
ATOM   2601 C  CB  A MET   A 1 334 ? 61.921 -0.369  -16.252 0.54 37.85  ?  349 MET   A CB  1 
ATOM   2602 C  CB  B MET   A 1 334 ? 61.975 -0.497  -16.112 0.46 38.07  ?  349 MET   A CB  1 
ATOM   2603 C  CG  A MET   A 1 334 ? 60.618 0.350   -16.519 0.54 38.48  ?  349 MET   A CG  1 
ATOM   2604 C  CG  B MET   A 1 334 ? 60.595 0.124   -16.195 0.46 39.70  ?  349 MET   A CG  1 
ATOM   2605 S  SD  A MET   A 1 334 ? 60.035 1.140   -15.020 0.54 36.38  ?  349 MET   A SD  1 
ATOM   2606 S  SD  B MET   A 1 334 ? 60.634 1.873   -16.596 0.46 39.16  ?  349 MET   A SD  1 
ATOM   2607 C  CE  A MET   A 1 334 ? 61.245 2.453   -14.881 0.54 38.51  ?  349 MET   A CE  1 
ATOM   2608 C  CE  B MET   A 1 334 ? 61.371 2.589   -15.123 0.46 38.84  ?  349 MET   A CE  1 
ATOM   2609 N  N   . GLU   A 1 335 ? 64.744 -1.766  -17.984 1.00 36.94  ?  350 GLU   A N   1 
ATOM   2610 C  CA  . GLU   A 1 335 ? 65.970 -2.525  -17.837 1.00 40.77  ?  350 GLU   A CA  1 
ATOM   2611 C  C   . GLU   A 1 335 ? 66.636 -2.143  -16.527 1.00 42.00  ?  350 GLU   A C   1 
ATOM   2612 O  O   . GLU   A 1 335 ? 66.759 -0.960  -16.208 1.00 36.99  ?  350 GLU   A O   1 
ATOM   2613 C  CB  . GLU   A 1 335 ? 66.910 -2.271  -19.015 1.00 33.85  ?  350 GLU   A CB  1 
ATOM   2614 C  CG  . GLU   A 1 335 ? 68.081 -3.255  -19.051 1.00 36.48  ?  350 GLU   A CG  1 
ATOM   2615 C  CD  . GLU   A 1 335 ? 69.260 -2.794  -19.882 1.00 43.55  ?  350 GLU   A CD  1 
ATOM   2616 O  OE1 . GLU   A 1 335 ? 69.344 -1.594  -20.224 1.00 47.87  ?  350 GLU   A OE1 1 
ATOM   2617 O  OE2 . GLU   A 1 335 ? 70.127 -3.638  -20.192 1.00 49.64  ?  350 GLU   A OE2 1 
ATOM   2618 N  N   . GLY   A 1 336 ? 67.024 -3.153  -15.750 1.00 41.76  ?  351 GLY   A N   1 
ATOM   2619 C  CA  . GLY   A 1 336 ? 67.554 -2.927  -14.431 1.00 38.52  ?  351 GLY   A CA  1 
ATOM   2620 C  C   . GLY   A 1 336 ? 66.523 -3.033  -13.332 1.00 45.06  ?  351 GLY   A C   1 
ATOM   2621 O  O   . GLY   A 1 336 ? 66.902 -3.050  -12.160 1.00 43.40  ?  351 GLY   A O   1 
ATOM   2622 N  N   . PHE   A 1 337 ? 65.235 -3.108  -13.667 1.00 40.12  ?  352 PHE   A N   1 
ATOM   2623 C  CA  . PHE   A 1 337 ? 64.218 -3.219  -12.629 1.00 39.92  ?  352 PHE   A CA  1 
ATOM   2624 C  C   . PHE   A 1 337 ? 63.232 -4.370  -12.858 1.00 45.23  ?  352 PHE   A C   1 
ATOM   2625 O  O   . PHE   A 1 337 ? 63.193 -5.319  -12.069 1.00 38.24  ?  352 PHE   A O   1 
ATOM   2626 C  CB  . PHE   A 1 337 ? 63.439 -1.905  -12.496 1.00 39.68  ?  352 PHE   A CB  1 
ATOM   2627 C  CG  . PHE   A 1 337 ? 62.366 -1.963  -11.442 1.00 45.15  ?  352 PHE   A CG  1 
ATOM   2628 C  CD1 . PHE   A 1 337 ? 62.706 -2.127  -10.106 1.00 54.49  ?  352 PHE   A CD1 1 
ATOM   2629 C  CD2 . PHE   A 1 337 ? 61.032 -1.898  -11.780 1.00 50.72  ?  352 PHE   A CD2 1 
ATOM   2630 C  CE1 . PHE   A 1 337 ? 61.732 -2.194  -9.123  1.00 51.78  ?  352 PHE   A CE1 1 
ATOM   2631 C  CE2 . PHE   A 1 337 ? 60.051 -1.954  -10.804 1.00 55.15  ?  352 PHE   A CE2 1 
ATOM   2632 C  CZ  . PHE   A 1 337 ? 60.404 -2.104  -9.474  1.00 50.44  ?  352 PHE   A CZ  1 
ATOM   2633 N  N   . GLY   A 1 338 ? 62.408 -4.286  -13.896 1.00 36.10  ?  353 GLY   A N   1 
ATOM   2634 C  CA  . GLY   A 1 338 ? 61.354 -5.270  -14.087 1.00 31.39  ?  353 GLY   A CA  1 
ATOM   2635 C  C   . GLY   A 1 338 ? 60.584 -4.994  -15.362 1.00 38.12  ?  353 GLY   A C   1 
ATOM   2636 O  O   . GLY   A 1 338 ? 60.991 -4.162  -16.187 1.00 34.81  ?  353 GLY   A O   1 
ATOM   2637 N  N   . THR   A 1 339 ? 59.436 -5.676  -15.493 1.00 32.96  ?  354 THR   A N   1 
ATOM   2638 C  CA  . THR   A 1 339 ? 58.634 -5.667  -16.710 1.00 36.34  ?  354 THR   A CA  1 
ATOM   2639 C  C   . THR   A 1 339 ? 57.159 -5.692  -16.338 1.00 39.14  ?  354 THR   A C   1 
ATOM   2640 O  O   . THR   A 1 339 ? 56.751 -6.414  -15.426 1.00 38.18  ?  354 THR   A O   1 
ATOM   2641 C  CB  . THR   A 1 339 ? 58.957 -6.884  -17.627 1.00 33.80  ?  354 THR   A CB  1 
ATOM   2642 O  OG1 . THR   A 1 339 ? 60.354 -6.893  -17.906 1.00 34.11  ?  354 THR   A OG1 1 
ATOM   2643 C  CG2 . THR   A 1 339 ? 58.170 -6.829  -18.962 1.00 31.36  ?  354 THR   A CG2 1 
ATOM   2644 N  N   . ASP   A 1 340 ? 56.361 -4.905  -17.057 1.00 35.06  ?  355 ASP   A N   1 
ATOM   2645 C  CA  . ASP   A 1 340 ? 54.912 -4.944  -16.954 1.00 34.93  ?  355 ASP   A CA  1 
ATOM   2646 C  C   . ASP   A 1 340 ? 54.344 -5.530  -18.237 1.00 37.61  ?  355 ASP   A C   1 
ATOM   2647 O  O   . ASP   A 1 340 ? 54.851 -5.259  -19.331 1.00 32.14  ?  355 ASP   A O   1 
ATOM   2648 C  CB  . ASP   A 1 340 ? 54.308 -3.553  -16.769 1.00 37.32  ?  355 ASP   A CB  1 
ATOM   2649 C  CG  . ASP   A 1 340 ? 54.608 -2.940  -15.401 1.00 40.36  ?  355 ASP   A CG  1 
ATOM   2650 O  OD1 . ASP   A 1 340 ? 55.038 -3.653  -14.488 1.00 42.56  ?  355 ASP   A OD1 1 
ATOM   2651 O  OD2 . ASP   A 1 340 ? 54.408 -1.727  -15.263 1.00 48.83  ?  355 ASP   A OD2 1 
ATOM   2652 N  N   . ALA   A 1 341 ? 53.275 -6.303  -18.099 1.00 32.23  ?  356 ALA   A N   1 
ATOM   2653 C  CA  . ALA   A 1 341 ? 52.473 -6.750  -19.231 1.00 34.62  ?  356 ALA   A CA  1 
ATOM   2654 C  C   . ALA   A 1 341 ? 51.023 -6.374  -18.977 1.00 37.63  ?  356 ALA   A C   1 
ATOM   2655 O  O   . ALA   A 1 341 ? 50.534 -6.536  -17.859 1.00 33.27  ?  356 ALA   A O   1 
ATOM   2656 C  CB  . ALA   A 1 341 ? 52.589 -8.263  -19.423 1.00 31.40  ?  356 ALA   A CB  1 
ATOM   2657 N  N   . VAL   A 1 342 ? 50.336 -5.868  -20.005 1.00 31.64  ?  357 VAL   A N   1 
ATOM   2658 C  CA  . VAL   A 1 342 ? 48.916 -5.550  -19.903 1.00 32.88  ?  357 VAL   A CA  1 
ATOM   2659 C  C   . VAL   A 1 342 ? 48.139 -6.331  -20.955 1.00 34.44  ?  357 VAL   A C   1 
ATOM   2660 O  O   . VAL   A 1 342 ? 48.431 -6.238  -22.155 1.00 33.71  ?  357 VAL   A O   1 
ATOM   2661 C  CB  . VAL   A 1 342 ? 48.648 -4.036  -20.030 1.00 39.18  ?  357 VAL   A CB  1 
ATOM   2662 C  CG1 . VAL   A 1 342 ? 47.182 -3.738  -19.705 1.00 34.66  ?  357 VAL   A CG1 1 
ATOM   2663 C  CG2 . VAL   A 1 342 ? 49.561 -3.253  -19.068 1.00 35.66  ?  357 VAL   A CG2 1 
ATOM   2664 N  N   . ILE   A 1 343 ? 47.139 -7.073  -20.498 1.00 33.29  ?  358 ILE   A N   1 
ATOM   2665 C  CA  . ILE   A 1 343 ? 46.114 -7.654  -21.357 1.00 29.97  ?  358 ILE   A CA  1 
ATOM   2666 C  C   . ILE   A 1 343 ? 44.926 -6.697  -21.381 1.00 37.50  ?  358 ILE   A C   1 
ATOM   2667 O  O   . ILE   A 1 343 ? 44.357 -6.373  -20.329 1.00 33.32  ?  358 ILE   A O   1 
ATOM   2668 C  CB  . ILE   A 1 343 ? 45.682 -9.036  -20.853 1.00 33.36  ?  358 ILE   A CB  1 
ATOM   2669 C  CG1 . ILE   A 1 343 ? 46.854 -10.023 -20.864 1.00 35.55  ?  358 ILE   A CG1 1 
ATOM   2670 C  CG2 . ILE   A 1 343 ? 44.563 -9.602  -21.740 1.00 40.84  ?  358 ILE   A CG2 1 
ATOM   2671 C  CD1 . ILE   A 1 343 ? 46.566 -11.291 -20.084 1.00 34.92  ?  358 ILE   A CD1 1 
ATOM   2672 N  N   . TYR   A 1 344 ? 44.552 -6.247  -22.569 1.00 34.63  ?  359 TYR   A N   1 
ATOM   2673 C  CA  . TYR   A 1 344 ? 43.413 -5.359  -22.757 1.00 33.16  ?  359 TYR   A CA  1 
ATOM   2674 C  C   . TYR   A 1 344 ? 42.278 -6.183  -23.332 1.00 40.89  ?  359 TYR   A C   1 
ATOM   2675 O  O   . TYR   A 1 344 ? 42.449 -6.804  -24.379 1.00 33.10  ?  359 TYR   A O   1 
ATOM   2676 C  CB  . TYR   A 1 344 ? 43.753 -4.212  -23.715 1.00 34.32  ?  359 TYR   A CB  1 
ATOM   2677 C  CG  . TYR   A 1 344 ? 44.753 -3.244  -23.149 1.00 34.20  ?  359 TYR   A CG  1 
ATOM   2678 C  CD1 . TYR   A 1 344 ? 44.356 -2.282  -22.240 1.00 36.15  ?  359 TYR   A CD1 1 
ATOM   2679 C  CD2 . TYR   A 1 344 ? 46.095 -3.292  -23.527 1.00 34.56  ?  359 TYR   A CD2 1 
ATOM   2680 C  CE1 . TYR   A 1 344 ? 45.257 -1.398  -21.693 1.00 34.33  ?  359 TYR   A CE1 1 
ATOM   2681 C  CE2 . TYR   A 1 344 ? 47.016 -2.399  -22.998 1.00 37.26  ?  359 TYR   A CE2 1 
ATOM   2682 C  CZ  . TYR   A 1 344 ? 46.585 -1.457  -22.073 1.00 41.19  ?  359 TYR   A CZ  1 
ATOM   2683 O  OH  . TYR   A 1 344 ? 47.456 -0.551  -21.522 1.00 37.35  ?  359 TYR   A OH  1 
ATOM   2684 N  N   . LEU   A 1 345 ? 41.141 -6.219  -22.647 1.00 31.77  ?  360 LEU   A N   1 
ATOM   2685 C  CA  . LEU   A 1 345 ? 39.974 -6.924  -23.162 1.00 34.67  ?  360 LEU   A CA  1 
ATOM   2686 C  C   . LEU   A 1 345 ? 38.808 -5.953  -23.290 1.00 39.00  ?  360 LEU   A C   1 
ATOM   2687 O  O   . LEU   A 1 345 ? 38.759 -4.937  -22.598 1.00 35.19  ?  360 LEU   A O   1 
ATOM   2688 C  CB  . LEU   A 1 345 ? 39.566 -8.094  -22.242 1.00 35.36  ?  360 LEU   A CB  1 
ATOM   2689 C  CG  . LEU   A 1 345 ? 40.679 -9.089  -21.890 1.00 37.96  ?  360 LEU   A CG  1 
ATOM   2690 C  CD1 . LEU   A 1 345 ? 40.189 -10.167 -20.917 1.00 34.93  ?  360 LEU   A CD1 1 
ATOM   2691 C  CD2 . LEU   A 1 345 ? 41.228 -9.743  -23.169 1.00 36.80  ?  360 LEU   A CD2 1 
ATOM   2692 N  N   . LYS   A 1 346 ? 37.861 -6.250  -24.184 1.00 34.22  ?  361 LYS   A N   1 
ATOM   2693 C  CA  . LYS   A 1 346 ? 36.632 -5.465  -24.204 1.00 36.11  ?  361 LYS   A CA  1 
ATOM   2694 C  C   . LYS   A 1 346 ? 35.738 -5.885  -23.042 1.00 41.92  ?  361 LYS   A C   1 
ATOM   2695 O  O   . LYS   A 1 346 ? 35.569 -7.080  -22.781 1.00 41.35  ?  361 LYS   A O   1 
ATOM   2696 C  CB  . LYS   A 1 346 ? 35.902 -5.653  -25.526 1.00 37.93  ?  361 LYS   A CB  1 
ATOM   2697 C  CG  . LYS   A 1 346 ? 36.661 -5.105  -26.720 1.00 38.65  ?  361 LYS   A CG  1 
ATOM   2698 C  CD  . LYS   A 1 346 ? 36.728 -3.573  -26.690 1.00 41.52  ?  361 LYS   A CD  1 
ATOM   2699 C  CE  . LYS   A 1 346 ? 37.355 -3.090  -28.015 1.00 48.62  ?  361 LYS   A CE  1 
ATOM   2700 N  NZ  . LYS   A 1 346 ? 37.409 -1.628  -28.119 1.00 48.40  ?  361 LYS   A NZ  1 
ATOM   2701 N  N   . ALA   A 1 347 ? 35.159 -4.897  -22.344 1.00 38.60  ?  362 ALA   A N   1 
ATOM   2702 C  CA  . ALA   A 1 347 ? 34.345 -5.202  -21.173 1.00 38.99  ?  362 ALA   A CA  1 
ATOM   2703 C  C   . ALA   A 1 347 ? 32.953 -5.700  -21.541 1.00 44.49  ?  362 ALA   A C   1 
ATOM   2704 O  O   . ALA   A 1 347 ? 32.348 -6.444  -20.762 1.00 47.77  ?  362 ALA   A O   1 
ATOM   2705 C  CB  . ALA   A 1 347 ? 34.230 -3.977  -20.255 1.00 39.88  ?  362 ALA   A CB  1 
ATOM   2706 N  N   . LEU   A 1 348 ? 32.424 -5.304  -22.695 1.00 41.17  ?  363 LEU   A N   1 
ATOM   2707 C  CA  . LEU   A 1 348 ? 31.051 -5.613  -23.080 1.00 50.91  ?  363 LEU   A CA  1 
ATOM   2708 C  C   . LEU   A 1 348 ? 31.024 -6.686  -24.159 1.00 47.94  ?  363 LEU   A C   1 
ATOM   2709 O  O   . LEU   A 1 348 ? 31.827 -6.654  -25.099 1.00 43.61  ?  363 LEU   A O   1 
ATOM   2710 C  CB  . LEU   A 1 348 ? 30.329 -4.357  -23.575 1.00 48.98  ?  363 LEU   A CB  1 
ATOM   2711 C  CG  . LEU   A 1 348 ? 30.397 -3.216  -22.555 1.00 53.29  ?  363 LEU   A CG  1 
ATOM   2712 C  CD1 . LEU   A 1 348 ? 29.885 -1.918  -23.146 1.00 55.00  ?  363 LEU   A CD1 1 
ATOM   2713 C  CD2 . LEU   A 1 348 ? 29.607 -3.598  -21.312 1.00 56.84  ?  363 LEU   A CD2 1 
ATOM   2714 N  N   . SER   A 1 349 ? 30.077 -7.623  -24.032 1.00 42.93  ?  364 SER   A N   1 
ATOM   2715 C  CA  . SER   A 1 349 ? 29.978 -8.723  -24.980 1.00 45.64  ?  364 SER   A CA  1 
ATOM   2716 C  C   . SER   A 1 349 ? 29.610 -8.255  -26.382 1.00 51.67  ?  364 SER   A C   1 
ATOM   2717 O  O   . SER   A 1 349 ? 29.876 -8.971  -27.352 1.00 53.68  ?  364 SER   A O   1 
ATOM   2718 C  CB  . SER   A 1 349 ? 28.940 -9.737  -24.504 1.00 44.86  ?  364 SER   A CB  1 
ATOM   2719 O  OG  . SER   A 1 349 ? 27.678 -9.101  -24.393 1.00 53.51  ?  364 SER   A OG  1 
ATOM   2720 N  N   . THR   A 1 350 ? 28.965 -7.097  -26.516 1.00 50.83  ?  365 THR   A N   1 
ATOM   2721 C  CA  . THR   A 1 350 ? 28.662 -6.595  -27.849 1.00 49.62  ?  365 THR   A CA  1 
ATOM   2722 C  C   . THR   A 1 350 ? 29.874 -5.961  -28.522 1.00 48.50  ?  365 THR   A C   1 
ATOM   2723 O  O   . THR   A 1 350 ? 29.899 -5.871  -29.754 1.00 48.22  ?  365 THR   A O   1 
ATOM   2724 C  CB  . THR   A 1 350 ? 27.520 -5.588  -27.782 1.00 50.52  ?  365 THR   A CB  1 
ATOM   2725 O  OG1 . THR   A 1 350 ? 27.821 -4.608  -26.785 1.00 50.62  ?  365 THR   A OG1 1 
ATOM   2726 C  CG2 . THR   A 1 350 ? 26.246 -6.282  -27.402 1.00 50.72  ?  365 THR   A CG2 1 
ATOM   2727 N  N   . ASP   A 1 351 ? 30.874 -5.515  -27.756 1.00 46.18  ?  366 ASP   A N   1 
ATOM   2728 C  CA  . ASP   A 1 351 ? 32.114 -5.050  -28.373 1.00 46.72  ?  366 ASP   A CA  1 
ATOM   2729 C  C   . ASP   A 1 351 ? 33.093 -6.181  -28.663 1.00 44.94  ?  366 ASP   A C   1 
ATOM   2730 O  O   . ASP   A 1 351 ? 34.082 -5.951  -29.367 1.00 43.63  ?  366 ASP   A O   1 
ATOM   2731 C  CB  . ASP   A 1 351 ? 32.833 -4.016  -27.487 1.00 43.86  ?  366 ASP   A CB  1 
ATOM   2732 C  CG  . ASP   A 1 351 ? 32.071 -2.707  -27.352 1.00 56.75  ?  366 ASP   A CG  1 
ATOM   2733 O  OD1 . ASP   A 1 351 ? 31.196 -2.421  -28.198 1.00 51.27  ?  366 ASP   A OD1 1 
ATOM   2734 O  OD2 . ASP   A 1 351 ? 32.364 -1.958  -26.390 1.00 54.06  ?  366 ASP   A OD2 1 
ATOM   2735 N  N   . SER   A 1 352 ? 32.877 -7.374  -28.109 1.00 45.08  ?  367 SER   A N   1 
ATOM   2736 C  CA  . SER   A 1 352 ? 33.820 -8.490  -28.246 1.00 43.63  ?  367 SER   A CA  1 
ATOM   2737 C  C   . SER   A 1 352 ? 33.481 -9.220  -29.533 1.00 43.13  ?  367 SER   A C   1 
ATOM   2738 O  O   . SER   A 1 352 ? 32.734 -10.198 -29.539 1.00 46.88  ?  367 SER   A O   1 
ATOM   2739 C  CB  . SER   A 1 352 ? 33.757 -9.427  -27.044 1.00 40.29  ?  367 SER   A CB  1 
ATOM   2740 O  OG  . SER   A 1 352 ? 34.133 -8.726  -25.868 1.00 49.57  ?  367 SER   A OG  1 
ATOM   2741 N  N   . VAL   A 1 353 ? 34.058 -8.748  -30.632 1.00 44.30  ?  368 VAL   A N   1 
ATOM   2742 C  CA  . VAL   A 1 353 ? 33.730 -9.206  -31.976 1.00 45.91  ?  368 VAL   A CA  1 
ATOM   2743 C  C   . VAL   A 1 353 ? 34.978 -9.839  -32.578 1.00 39.89  ?  368 VAL   A C   1 
ATOM   2744 O  O   . VAL   A 1 353 ? 36.072 -9.266  -32.479 1.00 40.07  ?  368 VAL   A O   1 
ATOM   2745 C  CB  . VAL   A 1 353 ? 33.251 -8.027  -32.849 1.00 46.11  ?  368 VAL   A CB  1 
ATOM   2746 C  CG1 . VAL   A 1 353 ? 33.012 -8.470  -34.280 1.00 45.82  ?  368 VAL   A CG1 1 
ATOM   2747 C  CG2 . VAL   A 1 353 ? 32.003 -7.375  -32.233 1.00 47.48  ?  368 VAL   A CG2 1 
ATOM   2748 N  N   . GLU   A 1 354 ? 34.816 -11.006 -33.201 1.00 42.77  ?  369 GLU   A N   1 
ATOM   2749 C  CA  . GLU   A 1 354 ? 35.920 -11.669 -33.895 1.00 45.60  ?  369 GLU   A CA  1 
ATOM   2750 C  C   . GLU   A 1 354 ? 36.681 -10.708 -34.798 1.00 44.33  ?  369 GLU   A C   1 
ATOM   2751 O  O   . GLU   A 1 354 ? 36.079 -9.952  -35.561 1.00 41.23  ?  369 GLU   A O   1 
ATOM   2752 C  CB  . GLU   A 1 354 ? 35.396 -12.821 -34.761 1.00 44.28  ?  369 GLU   A CB  1 
ATOM   2753 C  CG  . GLU   A 1 354 ? 34.838 -14.007 -34.016 1.00 44.95  ?  369 GLU   A CG  1 
ATOM   2754 C  CD  . GLU   A 1 354 ? 34.526 -15.114 -34.976 1.00 46.52  ?  369 GLU   A CD  1 
ATOM   2755 O  OE1 . GLU   A 1 354 ? 33.574 -14.949 -35.779 1.00 48.07  ?  369 GLU   A OE1 1 
ATOM   2756 O  OE2 . GLU   A 1 354 ? 35.265 -16.126 -34.965 1.00 43.23  ?  369 GLU   A OE2 1 
ATOM   2757 N  N   . ARG   A 1 355 ? 38.010 -10.782 -34.745 1.00 39.85  ?  370 ARG   A N   1 
ATOM   2758 C  CA  . ARG   A 1 355 ? 38.890 -10.053 -35.657 1.00 44.67  ?  370 ARG   A CA  1 
ATOM   2759 C  C   . ARG   A 1 355 ? 39.409 -11.068 -36.664 1.00 41.96  ?  370 ARG   A C   1 
ATOM   2760 O  O   . ARG   A 1 355 ? 40.171 -11.968 -36.297 1.00 43.32  ?  370 ARG   A O   1 
ATOM   2761 C  CB  . ARG   A 1 355 ? 40.041 -9.384  -34.894 1.00 45.53  ?  370 ARG   A CB  1 
ATOM   2762 C  CG  . ARG   A 1 355 ? 41.214 -8.903  -35.791 1.00 50.38  ?  370 ARG   A CG  1 
ATOM   2763 C  CD  . ARG   A 1 355 ? 41.562 -7.443  -35.547 1.00 48.78  ?  370 ARG   A CD  1 
ATOM   2764 N  NE  . ARG   A 1 355 ? 42.118 -7.231  -34.215 1.00 70.71  ?  370 ARG   A NE  1 
ATOM   2765 C  CZ  . ARG   A 1 355 ? 41.935 -6.137  -33.486 1.00 60.95  ?  370 ARG   A CZ  1 
ATOM   2766 N  NH1 . ARG   A 1 355 ? 41.185 -5.138  -33.920 1.00 65.02  ?  370 ARG   A NH1 1 
ATOM   2767 N  NH2 . ARG   A 1 355 ? 42.503 -6.053  -32.284 1.00 71.14  ?  370 ARG   A NH2 1 
ATOM   2768 N  N   . LEU   A 1 356 ? 38.969 -10.953 -37.918 1.00 37.60  ?  371 LEU   A N   1 
ATOM   2769 C  CA  . LEU   A 1 356 ? 39.254 -11.961 -38.925 1.00 45.78  ?  371 LEU   A CA  1 
ATOM   2770 C  C   . LEU   A 1 356 ? 40.018 -11.360 -40.098 1.00 50.53  ?  371 LEU   A C   1 
ATOM   2771 O  O   . LEU   A 1 356 ? 39.543 -10.393 -40.701 1.00 48.09  ?  371 LEU   A O   1 
ATOM   2772 C  CB  . LEU   A 1 356 ? 37.952 -12.588 -39.441 1.00 45.19  ?  371 LEU   A CB  1 
ATOM   2773 C  CG  . LEU   A 1 356 ? 36.987 -13.060 -38.359 1.00 49.09  ?  371 LEU   A CG  1 
ATOM   2774 C  CD1 . LEU   A 1 356 ? 35.729 -13.625 -38.987 1.00 43.50  ?  371 LEU   A CD1 1 
ATOM   2775 C  CD2 . LEU   A 1 356 ? 37.679 -14.116 -37.529 1.00 48.74  ?  371 LEU   A CD2 1 
ATOM   2776 N  N   . PRO   A 1 357 ? 41.162 -11.928 -40.480 1.00 49.80  ?  372 PRO   A N   1 
ATOM   2777 C  CA  . PRO   A 1 357 ? 41.780 -11.569 -41.769 1.00 42.44  ?  372 PRO   A CA  1 
ATOM   2778 C  C   . PRO   A 1 357 ? 40.888 -11.899 -42.958 1.00 51.44  ?  372 PRO   A C   1 
ATOM   2779 O  O   . PRO   A 1 357 ? 40.159 -12.894 -42.958 1.00 48.04  ?  372 PRO   A O   1 
ATOM   2780 C  CB  . PRO   A 1 357 ? 43.053 -12.423 -41.803 1.00 50.74  ?  372 PRO   A CB  1 
ATOM   2781 C  CG  . PRO   A 1 357 ? 42.730 -13.597 -40.877 1.00 59.16  ?  372 PRO   A CG  1 
ATOM   2782 C  CD  . PRO   A 1 357 ? 41.895 -12.995 -39.770 1.00 48.09  ?  372 PRO   A CD  1 
ATOM   2783 N  N   . VAL   A 1 358 ? 40.998 -11.083 -44.015 1.00 55.40  ?  373 VAL   A N   1 
ATOM   2784 C  CA  . VAL   A 1 358 ? 40.232 -11.268 -45.250 1.00 53.16  ?  373 VAL   A CA  1 
ATOM   2785 C  C   . VAL   A 1 358 ? 41.193 -11.283 -46.433 1.00 56.92  ?  373 VAL   A C   1 
ATOM   2786 O  O   . VAL   A 1 358 ? 42.175 -10.533 -46.458 1.00 57.56  ?  373 VAL   A O   1 
ATOM   2787 C  CB  . VAL   A 1 358 ? 39.181 -10.158 -45.454 1.00 52.86  ?  373 VAL   A CB  1 
ATOM   2788 C  CG1 . VAL   A 1 358 ? 38.279 -10.482 -46.626 1.00 57.83  ?  373 VAL   A CG1 1 
ATOM   2789 C  CG2 . VAL   A 1 358 ? 38.368 -9.950  -44.193 1.00 62.59  ?  373 VAL   A CG2 1 
ATOM   2790 N  N   . TYR   A 1 359 ? 40.908 -12.129 -47.416 1.00 55.19  ?  374 TYR   A N   1 
ATOM   2791 C  CA  . TYR   A 1 359 ? 41.631 -12.103 -48.682 1.00 74.37  ?  374 TYR   A CA  1 
ATOM   2792 C  C   . TYR   A 1 359 ? 40.926 -11.144 -49.638 1.00 77.31  ?  374 TYR   A C   1 
ATOM   2793 O  O   . TYR   A 1 359 ? 39.781 -11.391 -50.043 1.00 76.08  ?  374 TYR   A O   1 
ATOM   2794 C  CB  . TYR   A 1 359 ? 41.732 -13.503 -49.294 1.00 61.84  ?  374 TYR   A CB  1 
ATOM   2795 C  CG  . TYR   A 1 359 ? 42.387 -13.514 -50.661 1.00 70.41  ?  374 TYR   A CG  1 
ATOM   2796 C  CD1 . TYR   A 1 359 ? 43.763 -13.364 -50.797 1.00 66.28  ?  374 TYR   A CD1 1 
ATOM   2797 C  CD2 . TYR   A 1 359 ? 41.627 -13.669 -51.821 1.00 68.01  ?  374 TYR   A CD2 1 
ATOM   2798 C  CE1 . TYR   A 1 359 ? 44.370 -13.371 -52.052 1.00 84.34  ?  374 TYR   A CE1 1 
ATOM   2799 C  CE2 . TYR   A 1 359 ? 42.224 -13.681 -53.078 1.00 81.05  ?  374 TYR   A CE2 1 
ATOM   2800 C  CZ  . TYR   A 1 359 ? 43.599 -13.530 -53.189 1.00 84.07  ?  374 TYR   A CZ  1 
ATOM   2801 O  OH  . TYR   A 1 359 ? 44.200 -13.540 -54.431 1.00 84.26  ?  374 TYR   A OH  1 
ATOM   2802 N  N   . ASN   A 1 360 ? 41.604 -10.051 -49.987 1.00 95.96  ?  375 ASN   A N   1 
ATOM   2803 C  CA  . ASN   A 1 360 ? 41.118 -9.082  -50.971 1.00 96.13  ?  375 ASN   A CA  1 
ATOM   2804 C  C   . ASN   A 1 360 ? 42.321 -8.512  -51.718 1.00 110.42 ?  375 ASN   A C   1 
ATOM   2805 O  O   . ASN   A 1 360 ? 43.437 -9.032  -51.618 1.00 112.26 ?  375 ASN   A O   1 
ATOM   2806 C  CB  . ASN   A 1 360 ? 40.277 -7.989  -50.297 1.00 94.58  ?  375 ASN   A CB  1 
ATOM   2807 C  CG  . ASN   A 1 360 ? 40.881 -7.506  -48.995 1.00 95.91  ?  375 ASN   A CG  1 
ATOM   2808 O  OD1 . ASN   A 1 360 ? 42.063 -7.718  -48.726 1.00 104.28 ?  375 ASN   A OD1 1 
ATOM   2809 N  ND2 . ASN   A 1 360 ? 40.069 -6.856  -48.173 1.00 100.52 ?  375 ASN   A ND2 1 
ATOM   2810 N  N   . LYS   A 1 361 ? 42.095 -7.443  -52.490 1.00 118.45 ?  376 LYS   A N   1 
ATOM   2811 C  CA  . LYS   A 1 361 ? 43.209 -6.759  -53.141 1.00 116.83 ?  376 LYS   A CA  1 
ATOM   2812 C  C   . LYS   A 1 361 ? 44.036 -5.939  -52.155 1.00 120.46 ?  376 LYS   A C   1 
ATOM   2813 O  O   . LYS   A 1 361 ? 45.197 -5.629  -52.449 1.00 121.78 ?  376 LYS   A O   1 
ATOM   2814 C  CB  . LYS   A 1 361 ? 42.703 -5.856  -54.268 1.00 109.15 ?  376 LYS   A CB  1 
ATOM   2815 C  CG  . LYS   A 1 361 ? 42.183 -6.596  -55.487 1.00 114.46 ?  376 LYS   A CG  1 
ATOM   2816 C  CD  . LYS   A 1 361 ? 41.503 -5.632  -56.452 1.00 121.73 ?  376 LYS   A CD  1 
ATOM   2817 C  CE  . LYS   A 1 361 ? 40.018 -5.952  -56.609 1.00 124.11 ?  376 LYS   A CE  1 
ATOM   2818 N  NZ  . LYS   A 1 361 ? 39.275 -4.902  -57.372 1.00 122.62 ?  376 LYS   A NZ  1 
ATOM   2819 N  N   . SER   A 1 362 ? 43.469 -5.586  -50.994 1.00 120.19 ?  377 SER   A N   1 
ATOM   2820 C  CA  . SER   A 1 362 ? 44.232 -4.861  -49.977 1.00 126.66 ?  377 SER   A CA  1 
ATOM   2821 C  C   . SER   A 1 362 ? 45.226 -5.778  -49.265 1.00 127.00 ?  377 SER   A C   1 
ATOM   2822 O  O   . SER   A 1 362 ? 46.324 -5.343  -48.888 1.00 121.98 ?  377 SER   A O   1 
ATOM   2823 C  CB  . SER   A 1 362 ? 43.281 -4.207  -48.969 1.00 120.63 ?  377 SER   A CB  1 
ATOM   2824 O  OG  . SER   A 1 362 ? 42.465 -3.221  -49.582 1.00 119.36 ?  377 SER   A OG  1 
ATOM   2825 N  N   . ALA   A 1 363 ? 44.856 -7.046  -49.060 1.00 116.94 ?  378 ALA   A N   1 
ATOM   2826 C  CA  . ALA   A 1 363 ? 45.797 -8.030  -48.533 1.00 109.05 ?  378 ALA   A CA  1 
ATOM   2827 C  C   . ALA   A 1 363 ? 46.775 -8.492  -49.608 1.00 113.40 ?  378 ALA   A C   1 
ATOM   2828 O  O   . ALA   A 1 363 ? 47.951 -8.737  -49.320 1.00 113.26 ?  378 ALA   A O   1 
ATOM   2829 C  CB  . ALA   A 1 363 ? 45.037 -9.225  -47.958 1.00 86.03  ?  378 ALA   A CB  1 
ATOM   2830 N  N   . TRP   A 1 364 ? 46.297 -8.615  -50.849 1.00 114.83 ?  379 TRP   A N   1 
ATOM   2831 C  CA  . TRP   A 1 364 ? 47.153 -9.013  -51.962 1.00 117.68 ?  379 TRP   A CA  1 
ATOM   2832 C  C   . TRP   A 1 364 ? 48.329 -8.063  -52.147 1.00 120.89 ?  379 TRP   A C   1 
ATOM   2833 O  O   . TRP   A 1 364 ? 49.416 -8.494  -52.546 1.00 122.52 ?  379 TRP   A O   1 
ATOM   2834 C  CB  . TRP   A 1 364 ? 46.320 -9.089  -53.244 1.00 120.39 ?  379 TRP   A CB  1 
ATOM   2835 C  CG  . TRP   A 1 364 ? 47.123 -9.063  -54.517 1.00 130.42 ?  379 TRP   A CG  1 
ATOM   2836 C  CD1 . TRP   A 1 364 ? 47.629 -10.138 -55.188 1.00 129.54 ?  379 TRP   A CD1 1 
ATOM   2837 C  CD2 . TRP   A 1 364 ? 47.495 -7.903  -55.281 1.00 136.20 ?  379 TRP   A CD2 1 
ATOM   2838 N  NE1 . TRP   A 1 364 ? 48.299 -9.721  -56.314 1.00 134.83 ?  379 TRP   A NE1 1 
ATOM   2839 C  CE2 . TRP   A 1 364 ? 48.232 -8.355  -56.394 1.00 138.24 ?  379 TRP   A CE2 1 
ATOM   2840 C  CE3 . TRP   A 1 364 ? 47.282 -6.528  -55.128 1.00 135.94 ?  379 TRP   A CE3 1 
ATOM   2841 C  CZ2 . TRP   A 1 364 ? 48.756 -7.481  -57.350 1.00 141.96 ?  379 TRP   A CZ2 1 
ATOM   2842 C  CZ3 . TRP   A 1 364 ? 47.805 -5.661  -56.079 1.00 139.80 ?  379 TRP   A CZ3 1 
ATOM   2843 C  CH2 . TRP   A 1 364 ? 48.533 -6.142  -57.174 1.00 137.63 ?  379 TRP   A CH2 1 
ATOM   2844 N  N   . ARG   A 1 365 ? 48.138 -6.774  -51.859 1.00 123.61 ?  380 ARG   A N   1 
ATOM   2845 C  CA  . ARG   A 1 365 ? 49.170 -5.791  -52.172 1.00 129.12 ?  380 ARG   A CA  1 
ATOM   2846 C  C   . ARG   A 1 365 ? 50.359 -5.890  -51.224 1.00 121.59 ?  380 ARG   A C   1 
ATOM   2847 O  O   . ARG   A 1 365 ? 51.497 -5.634  -51.635 1.00 125.10 ?  380 ARG   A O   1 
ATOM   2848 C  CB  . ARG   A 1 365 ? 48.579 -4.382  -52.138 1.00 130.83 ?  380 ARG   A CB  1 
ATOM   2849 C  CG  . ARG   A 1 365 ? 49.103 -3.466  -53.231 1.00 138.01 ?  380 ARG   A CG  1 
ATOM   2850 C  CD  . ARG   A 1 365 ? 48.499 -2.077  -53.118 1.00 146.40 ?  380 ARG   A CD  1 
ATOM   2851 N  NE  . ARG   A 1 365 ? 47.052 -2.122  -52.941 1.00 143.25 ?  380 ARG   A NE  1 
ATOM   2852 C  CZ  . ARG   A 1 365 ? 46.176 -2.228  -53.933 1.00 143.95 ?  380 ARG   A CZ  1 
ATOM   2853 N  NH1 . ARG   A 1 365 ? 46.566 -2.318  -55.195 1.00 143.44 ?  380 ARG   A NH1 1 
ATOM   2854 N  NH2 . ARG   A 1 365 ? 44.876 -2.246  -53.652 1.00 136.72 ?  380 ARG   A NH2 1 
ATOM   2855 N  N   . HIS   A 1 366 ? 50.121 -6.261  -49.963 1.00 121.11 ?  381 HIS   A N   1 
ATOM   2856 C  CA  . HIS   A 1 366 ? 51.207 -6.342  -48.991 1.00 117.50 ?  381 HIS   A CA  1 
ATOM   2857 C  C   . HIS   A 1 366 ? 52.314 -7.289  -49.444 1.00 119.24 ?  381 HIS   A C   1 
ATOM   2858 O  O   . HIS   A 1 366 ? 53.468 -7.138  -49.024 1.00 117.44 ?  381 HIS   A O   1 
ATOM   2859 C  CB  . HIS   A 1 366 ? 50.663 -6.786  -47.635 1.00 105.43 ?  381 HIS   A CB  1 
ATOM   2860 C  CG  . HIS   A 1 366 ? 50.098 -5.668  -46.816 1.00 106.55 ?  381 HIS   A CG  1 
ATOM   2861 N  ND1 . HIS   A 1 366 ? 48.828 -5.167  -47.012 1.00 107.56 ?  381 HIS   A ND1 1 
ATOM   2862 C  CD2 . HIS   A 1 366 ? 50.632 -4.955  -45.796 1.00 102.93 ?  381 HIS   A CD2 1 
ATOM   2863 C  CE1 . HIS   A 1 366 ? 48.605 -4.194  -46.146 1.00 119.17 ?  381 HIS   A CE1 1 
ATOM   2864 N  NE2 . HIS   A 1 366 ? 49.684 -4.045  -45.398 1.00 112.17 ?  381 HIS   A NE2 1 
ATOM   2865 N  N   . TYR   A 1 367 ? 51.986 -8.261  -50.293 1.00 119.14 ?  382 TYR   A N   1 
ATOM   2866 C  CA  . TYR   A 1 367 ? 52.963 -9.228  -50.791 1.00 112.84 ?  382 TYR   A CA  1 
ATOM   2867 C  C   . TYR   A 1 367 ? 53.530 -8.783  -52.141 1.00 113.68 ?  382 TYR   A C   1 
ATOM   2868 O  O   . TYR   A 1 367 ? 54.581 -8.142  -52.211 1.00 109.62 ?  382 TYR   A O   1 
ATOM   2869 C  CB  . TYR   A 1 367 ? 52.326 -10.622 -50.918 1.00 103.33 ?  382 TYR   A CB  1 
ATOM   2870 C  CG  . TYR   A 1 367 ? 51.697 -11.154 -49.638 1.00 103.44 ?  382 TYR   A CG  1 
ATOM   2871 C  CD1 . TYR   A 1 367 ? 50.374 -10.863 -49.314 1.00 99.55  ?  382 TYR   A CD1 1 
ATOM   2872 C  CD2 . TYR   A 1 367 ? 52.424 -11.951 -48.759 1.00 93.76  ?  382 TYR   A CD2 1 
ATOM   2873 C  CE1 . TYR   A 1 367 ? 49.798 -11.346 -48.148 1.00 77.06  ?  382 TYR   A CE1 1 
ATOM   2874 C  CE2 . TYR   A 1 367 ? 51.855 -12.438 -47.595 1.00 76.81  ?  382 TYR   A CE2 1 
ATOM   2875 C  CZ  . TYR   A 1 367 ? 50.542 -12.135 -47.296 1.00 72.39  ?  382 TYR   A CZ  1 
ATOM   2876 O  OH  . TYR   A 1 367 ? 49.973 -12.617 -46.135 1.00 67.06  ?  382 TYR   A OH  1 
HETATM 2877 C  C1  . TF3   B 2 .   ? 58.635 -13.480 -47.662 1.00 55.97  ?  401 TF3   A C1  1 
HETATM 2878 C  C2  . TF3   B 2 .   ? 57.741 -12.762 -48.451 1.00 59.99  ?  401 TF3   A C2  1 
HETATM 2879 C  C3  . TF3   B 2 .   ? 59.978 -13.136 -47.689 1.00 65.86  ?  401 TF3   A C3  1 
HETATM 2880 O  O1  . TF3   B 2 .   ? 58.103 -14.491 -46.905 1.00 54.91  ?  401 TF3   A O1  1 
HETATM 2881 C  C4  . TF3   B 2 .   ? 58.175 -11.728 -49.255 1.00 62.76  ?  401 TF3   A C4  1 
HETATM 2882 CL CL1 . TF3   B 2 .   ? 56.048 -13.136 -48.388 1.00 76.00  ?  401 TF3   A CL1 1 
HETATM 2883 C  C5  . TF3   B 2 .   ? 60.408 -12.091 -48.493 1.00 64.90  ?  401 TF3   A C5  1 
HETATM 2884 C  C6  . TF3   B 2 .   ? 58.999 -15.240 -46.065 1.00 51.16  ?  401 TF3   A C6  1 
HETATM 2885 C  C7  . TF3   B 2 .   ? 59.518 -11.374 -49.283 1.00 68.44  ?  401 TF3   A C7  1 
HETATM 2886 C  C8  . TF3   B 2 .   ? 58.207 -16.322 -45.389 1.00 48.02  ?  401 TF3   A C8  1 
HETATM 2887 C  C9  . TF3   B 2 .   ? 59.991 -10.232 -50.154 1.00 83.27  ?  401 TF3   A C9  1 
HETATM 2888 C  C10 . TF3   B 2 .   ? 58.822 -17.460 -44.888 1.00 43.43  ?  401 TF3   A C10 1 
HETATM 2889 C  C11 . TF3   B 2 .   ? 56.835 -16.195 -45.231 1.00 47.00  ?  401 TF3   A C11 1 
HETATM 2890 C  C12 . TF3   B 2 .   ? 60.225 -10.666 -51.588 1.00 88.91  ?  401 TF3   A C12 1 
HETATM 2891 C  C13 . TF3   B 2 .   ? 58.085 -18.442 -44.249 1.00 41.90  ?  401 TF3   A C13 1 
HETATM 2892 C  C14 . TF3   B 2 .   ? 56.098 -17.182 -44.603 1.00 44.78  ?  401 TF3   A C14 1 
HETATM 2893 N  N1  . TF3   B 2 .   ? 59.157 -11.133 -52.237 1.00 91.32  ?  401 TF3   A N1  1 
HETATM 2894 O  O2  . TF3   B 2 .   ? 61.339 -10.596 -52.102 1.00 100.27 ?  401 TF3   A O2  1 
HETATM 2895 C  C15 . TF3   B 2 .   ? 56.710 -18.324 -44.108 1.00 46.96  ?  401 TF3   A C15 1 
HETATM 2896 C  C16 . TF3   B 2 .   ? 59.212 -11.715 -53.573 1.00 81.64  ?  401 TF3   A C16 1 
HETATM 2897 C  C17 . TF3   B 2 .   ? 55.873 -19.444 -43.510 1.00 55.26  ?  401 TF3   A C17 1 
HETATM 2898 C  C18 . TF3   B 2 .   ? 57.748 -12.042 -54.035 1.00 85.84  ?  401 TF3   A C18 1 
HETATM 2899 C  C19 . TF3   B 2 .   ? 55.432 -19.146 -42.080 1.00 44.48  ?  401 TF3   A C19 1 
HETATM 2900 C  C20 . TF3   B 2 .   ? 56.586 -20.788 -43.578 1.00 56.95  ?  401 TF3   A C20 1 
HETATM 2901 N  N2  . TF3   B 2 .   ? 57.782 -13.027 -55.131 1.00 80.12  ?  401 TF3   A N2  1 
HETATM 2902 C  C10 A A1EQI C 3 .   ? 60.975 -10.410 -18.367 0.52 36.00  ?  402 A1EQI A C10 1 
HETATM 2903 C  C10 B A1EQI C 3 .   ? 60.999 -10.416 -18.385 0.48 36.77  ?  402 A1EQI A C10 1 
HETATM 2904 C  C11 A A1EQI C 3 .   ? 58.771 -10.730 -18.794 0.52 33.46  ?  402 A1EQI A C11 1 
HETATM 2905 C  C11 B A1EQI C 3 .   ? 58.792 -10.735 -18.805 0.48 34.91  ?  402 A1EQI A C11 1 
HETATM 2906 C  C13 A A1EQI C 3 .   ? 55.351 -10.535 -17.236 0.52 39.32  ?  402 A1EQI A C13 1 
HETATM 2907 C  C13 B A1EQI C 3 .   ? 55.374 -10.537 -17.245 0.48 39.28  ?  402 A1EQI A C13 1 
HETATM 2908 C  C15 A A1EQI C 3 .   ? 56.609 -11.223 -19.767 0.52 37.05  ?  402 A1EQI A C15 1 
HETATM 2909 C  C15 B A1EQI C 3 .   ? 56.628 -11.227 -19.775 0.48 37.03  ?  402 A1EQI A C15 1 
HETATM 2910 C  C16 A A1EQI C 3 .   ? 57.261 -11.524 -20.938 0.52 37.69  ?  402 A1EQI A C16 1 
HETATM 2911 C  C16 B A1EQI C 3 .   ? 57.278 -11.530 -20.947 0.48 37.80  ?  402 A1EQI A C16 1 
HETATM 2912 C  C17 A A1EQI C 3 .   ? 58.626 -11.449 -21.097 0.52 34.42  ?  402 A1EQI A C17 1 
HETATM 2913 C  C17 B A1EQI C 3 .   ? 58.642 -11.457 -21.107 0.48 34.52  ?  402 A1EQI A C17 1 
HETATM 2914 C  C18 A A1EQI C 3 .   ? 59.389 -11.055 -19.998 0.52 38.28  ?  402 A1EQI A C18 1 
HETATM 2915 C  C18 B A1EQI C 3 .   ? 59.405 -11.062 -20.013 0.48 37.86  ?  402 A1EQI A C18 1 
HETATM 2916 C  C19 A A1EQI C 3 .   ? 61.197 -13.297 -19.369 0.52 40.75  ?  402 A1EQI A C19 1 
HETATM 2917 C  C19 B A1EQI C 3 .   ? 61.214 -13.291 -19.316 0.48 40.75  ?  402 A1EQI A C19 1 
HETATM 2918 C  C20 A A1EQI C 3 .   ? 62.218 -14.416 -19.314 0.52 40.41  ?  402 A1EQI A C20 1 
HETATM 2919 C  C20 B A1EQI C 3 .   ? 62.230 -14.413 -19.261 0.48 40.50  ?  402 A1EQI A C20 1 
HETATM 2920 C  C21 A A1EQI C 3 .   ? 62.770 -14.710 -20.707 0.52 42.68  ?  402 A1EQI A C21 1 
HETATM 2921 C  C21 B A1EQI C 3 .   ? 62.720 -14.764 -20.664 0.48 42.68  ?  402 A1EQI A C21 1 
HETATM 2922 C  C22 A A1EQI C 3 .   ? 65.010 -13.510 -24.719 0.52 49.47  ?  402 A1EQI A C22 1 
HETATM 2923 C  C22 B A1EQI C 3 .   ? 65.474 -12.424 -22.893 0.48 48.49  ?  402 A1EQI A C22 1 
HETATM 2924 N  N   A A1EQI C 3 .   ? 63.666 -13.717 -22.739 0.52 44.71  ?  402 A1EQI A N   1 
HETATM 2925 N  N   B A1EQI C 3 .   ? 63.535 -13.854 -22.771 0.48 44.72  ?  402 A1EQI A N   1 
HETATM 2926 C  C   A A1EQI C 3 .   ? 66.104 -12.972 -25.372 0.52 51.03  ?  402 A1EQI A C   1 
HETATM 2927 C  C   B A1EQI C 3 .   ? 66.534 -11.913 -23.620 0.48 51.51  ?  402 A1EQI A C   1 
HETATM 2928 O  O   A A1EQI C 3 .   ? 68.123 -11.211 -26.617 0.52 58.49  ?  402 A1EQI A O   1 
HETATM 2929 O  O   B A1EQI C 3 .   ? 68.953 -11.418 -25.262 0.48 54.55  ?  402 A1EQI A O   1 
HETATM 2930 C  C1  A A1EQI C 3 .   ? 66.977 -12.096 -24.732 0.52 50.95  ?  402 A1EQI A C1  1 
HETATM 2931 C  C1  B A1EQI C 3 .   ? 66.754 -12.284 -24.948 0.48 50.67  ?  402 A1EQI A C1  1 
HETATM 2932 C  C12 A A1EQI C 3 .   ? 57.381 -10.823 -18.681 0.52 35.14  ?  402 A1EQI A C12 1 
HETATM 2933 C  C12 B A1EQI C 3 .   ? 57.401 -10.826 -18.690 0.48 35.42  ?  402 A1EQI A C12 1 
HETATM 2934 C  C14 A A1EQI C 3 .   ? 54.973 -9.537  -16.173 0.52 37.24  ?  402 A1EQI A C14 1 
HETATM 2935 C  C14 B A1EQI C 3 .   ? 54.991 -9.539  -16.185 0.48 37.29  ?  402 A1EQI A C14 1 
HETATM 2936 C  C2  A A1EQI C 3 .   ? 68.190 -11.480 -25.390 0.52 55.99  ?  402 A1EQI A C2  1 
HETATM 2937 C  C2  B A1EQI C 3 .   ? 67.880 -11.775 -25.816 0.48 55.10  ?  402 A1EQI A C2  1 
HETATM 2938 C  C3  A A1EQI C 3 .   ? 66.714 -11.767 -23.403 0.52 51.77  ?  402 A1EQI A C3  1 
HETATM 2939 C  C3  B A1EQI C 3 .   ? 65.863 -13.183 -25.530 0.48 50.80  ?  402 A1EQI A C3  1 
HETATM 2940 C  C4  A A1EQI C 3 .   ? 65.623 -12.296 -22.739 0.52 48.59  ?  402 A1EQI A C4  1 
HETATM 2941 C  C4  B A1EQI C 3 .   ? 64.803 -13.703 -24.814 0.48 49.41  ?  402 A1EQI A C4  1 
HETATM 2942 C  C5  A A1EQI C 3 .   ? 64.766 -13.172 -23.392 0.52 46.79  ?  402 A1EQI A C5  1 
HETATM 2943 C  C5  B A1EQI C 3 .   ? 64.603 -13.330 -23.491 0.48 46.92  ?  402 A1EQI A C5  1 
HETATM 2944 C  C6  A A1EQI C 3 .   ? 63.285 -13.444 -21.363 0.52 43.69  ?  402 A1EQI A C6  1 
HETATM 2945 C  C6  B A1EQI C 3 .   ? 63.215 -13.529 -21.390 0.48 43.65  ?  402 A1EQI A C6  1 
HETATM 2946 C  C7  A A1EQI C 3 .   ? 62.202 -12.374 -21.337 0.52 42.83  ?  402 A1EQI A C7  1 
HETATM 2947 C  C7  B A1EQI C 3 .   ? 62.145 -12.447 -21.354 0.48 42.81  ?  402 A1EQI A C7  1 
HETATM 2948 C  C8  A A1EQI C 3 .   ? 60.879 -10.866 -19.843 0.52 39.13  ?  402 A1EQI A C8  1 
HETATM 2949 C  C8  B A1EQI C 3 .   ? 60.895 -10.876 -19.857 0.48 39.16  ?  402 A1EQI A C8  1 
HETATM 2950 C  C9  A A1EQI C 3 .   ? 61.350 -9.665  -20.669 0.52 37.34  ?  402 A1EQI A C9  1 
HETATM 2951 C  C9  B A1EQI C 3 .   ? 61.374 -9.686  -20.696 0.48 37.68  ?  402 A1EQI A C9  1 
HETATM 2952 F  F   A A1EQI C 3 .   ? 56.510 -11.929 -21.997 0.52 40.04  ?  402 A1EQI A F   1 
HETATM 2953 F  F   B A1EQI C 3 .   ? 56.525 -11.934 -22.004 0.48 40.05  ?  402 A1EQI A F   1 
HETATM 2954 N  N1  A A1EQI C 3 .   ? 61.751 -12.074 -19.972 0.52 40.68  ?  402 A1EQI A N1  1 
HETATM 2955 N  N1  B A1EQI C 3 .   ? 61.754 -12.095 -19.982 0.48 40.69  ?  402 A1EQI A N1  1 
HETATM 2956 N  N2  A A1EQI C 3 .   ? 59.723 -10.365 -17.851 0.52 36.02  ?  402 A1EQI A N2  1 
HETATM 2957 N  N2  B A1EQI C 3 .   ? 59.745 -10.369 -17.866 0.48 35.80  ?  402 A1EQI A N2  1 
HETATM 2958 N  N3  A A1EQI C 3 .   ? 56.804 -10.498 -17.474 0.52 37.60  ?  402 A1EQI A N3  1 
HETATM 2959 N  N3  B A1EQI C 3 .   ? 56.827 -10.500 -17.484 0.48 37.52  ?  402 A1EQI A N3  1 
HETATM 2960 O  O1  A A1EQI C 3 .   ? 69.198 -11.251 -24.675 0.52 52.48  -1 402 A1EQI A O1  1 
HETATM 2961 O  O1  B A1EQI C 3 .   ? 67.691 -11.758 -27.057 0.48 58.42  -1 402 A1EQI A O1  1 
HETATM 2962 O  O2  A A1EQI C 3 .   ? 62.010 -10.126 -17.779 0.52 38.62  ?  402 A1EQI A O2  1 
HETATM 2963 O  O2  B A1EQI C 3 .   ? 62.033 -10.134 -17.799 0.48 38.61  ?  402 A1EQI A O2  1 
HETATM 2964 CL CL  A A1EQI C 3 .   ? 66.363 -13.431 -27.023 0.52 63.10  ?  402 A1EQI A CL  1 
HETATM 2965 CL CL  B A1EQI C 3 .   ? 67.587 -10.793 -22.813 0.48 56.62  ?  402 A1EQI A CL  1 
HETATM 2966 S  S   . DMS   D 4 .   ? 28.065 -21.553 -33.237 1.00 102.20 ?  403 DMS   A S   1 
HETATM 2967 O  O   . DMS   D 4 .   ? 27.097 -21.470 -34.371 1.00 79.80  ?  403 DMS   A O   1 
HETATM 2968 C  C1  . DMS   D 4 .   ? 29.612 -22.252 -33.878 1.00 56.04  ?  403 DMS   A C1  1 
HETATM 2969 C  C2  . DMS   D 4 .   ? 27.588 -22.807 -32.017 1.00 80.88  ?  403 DMS   A C2  1 
HETATM 2970 S  S   . DMS   E 4 .   ? 54.850 -3.318  -26.899 1.00 70.30  ?  404 DMS   A S   1 
HETATM 2971 O  O   . DMS   E 4 .   ? 54.028 -4.517  -26.523 1.00 37.79  ?  404 DMS   A O   1 
HETATM 2972 C  C1  . DMS   E 4 .   ? 53.851 -1.791  -27.042 1.00 52.61  ?  404 DMS   A C1  1 
HETATM 2973 C  C2  . DMS   E 4 .   ? 55.426 -3.489  -28.619 1.00 52.88  ?  404 DMS   A C2  1 
HETATM 2974 O  O   . HOH   F 5 .   ? 42.897 -27.650 -34.511 1.00 61.67  ?  501 HOH   A O   1 
HETATM 2975 O  O   . HOH   F 5 .   ? 52.904 -8.901  -34.885 1.00 52.22  ?  502 HOH   A O   1 
HETATM 2976 O  O   . HOH   F 5 .   ? 32.708 -18.736 -13.757 1.00 54.55  ?  503 HOH   A O   1 
HETATM 2977 O  O   . HOH   F 5 .   ? 56.188 -17.395 -23.525 1.00 49.69  ?  504 HOH   A O   1 
HETATM 2978 O  O   . HOH   F 5 .   ? 28.773 -2.111  -27.887 1.00 60.01  ?  505 HOH   A O   1 
HETATM 2979 O  O   . HOH   F 5 .   ? 32.101 -2.116  -17.678 1.00 40.48  ?  506 HOH   A O   1 
HETATM 2980 O  O   . HOH   F 5 .   ? 58.236 -21.525 -3.725  1.00 64.48  ?  507 HOH   A O   1 
HETATM 2981 O  O   . HOH   F 5 .   ? 44.859 -21.644 -53.148 1.00 55.69  ?  508 HOH   A O   1 
HETATM 2982 O  O   . HOH   F 5 .   ? 61.678 -8.401  -15.949 1.00 33.30  ?  509 HOH   A O   1 
HETATM 2983 O  O   . HOH   F 5 .   ? 69.138 -8.073  -22.203 1.00 62.98  ?  510 HOH   A O   1 
HETATM 2984 O  O   . HOH   F 5 .   ? 36.069 -5.550  -7.288  1.00 51.49  ?  511 HOH   A O   1 
HETATM 2985 O  O   . HOH   F 5 .   ? 37.847 -10.804 -10.945 1.00 47.13  ?  512 HOH   A O   1 
HETATM 2986 O  O   . HOH   F 5 .   ? 40.192 -10.476 -26.569 1.00 33.34  ?  513 HOH   A O   1 
HETATM 2987 O  O   . HOH   F 5 .   ? 49.861 -9.268  -33.420 1.00 44.81  ?  514 HOH   A O   1 
HETATM 2988 O  O   . HOH   F 5 .   ? 33.359 -22.285 -20.900 1.00 52.25  ?  515 HOH   A O   1 
HETATM 2989 O  O   . HOH   F 5 .   ? 72.522 -21.674 -44.447 1.00 42.77  ?  516 HOH   A O   1 
HETATM 2990 O  O   . HOH   F 5 .   ? 49.167 -26.480 -33.592 1.00 52.55  ?  517 HOH   A O   1 
HETATM 2991 O  O   . HOH   F 5 .   ? 36.103 -9.318  -24.299 1.00 43.08  ?  518 HOH   A O   1 
HETATM 2992 O  O   . HOH   F 5 .   ? 66.256 1.098   -17.699 1.00 37.88  ?  519 HOH   A O   1 
HETATM 2993 O  O   . HOH   F 5 .   ? 33.594 3.055   -15.125 1.00 54.89  ?  520 HOH   A O   1 
HETATM 2994 O  O   . HOH   F 5 .   ? 31.486 -8.930  -20.847 1.00 56.34  ?  521 HOH   A O   1 
HETATM 2995 O  O   . HOH   F 5 .   ? 37.422 -12.736 -49.666 1.00 46.93  ?  522 HOH   A O   1 
HETATM 2996 O  O   . HOH   F 5 .   ? 30.843 -15.171 -44.494 1.00 55.70  ?  523 HOH   A O   1 
HETATM 2997 O  O   . HOH   F 5 .   ? 38.333 -8.460  -25.904 1.00 40.24  ?  524 HOH   A O   1 
HETATM 2998 O  O   . HOH   F 5 .   ? 33.601 -3.049  -24.301 1.00 39.67  ?  525 HOH   A O   1 
HETATM 2999 O  O   . HOH   F 5 .   ? 38.350 -0.650  -30.416 1.00 52.28  ?  526 HOH   A O   1 
HETATM 3000 O  O   . HOH   F 5 .   ? 30.926 -2.393  -12.709 1.00 56.62  ?  527 HOH   A O   1 
HETATM 3001 O  O   . HOH   F 5 .   ? 42.351 0.191   -20.436 1.00 34.60  ?  528 HOH   A O   1 
HETATM 3002 O  O   . HOH   F 5 .   ? 51.088 -24.105 -7.197  1.00 54.49  ?  529 HOH   A O   1 
HETATM 3003 O  O   . HOH   F 5 .   ? 66.992 -8.933  -39.379 1.00 65.24  ?  530 HOH   A O   1 
HETATM 3004 O  O   . HOH   F 5 .   ? 32.807 -9.699  -23.516 1.00 48.74  ?  531 HOH   A O   1 
HETATM 3005 O  O   . HOH   F 5 .   ? 62.907 -22.857 -51.213 1.00 58.14  ?  532 HOH   A O   1 
HETATM 3006 O  O   . HOH   F 5 .   ? 40.451 -14.610 -27.117 1.00 38.30  ?  533 HOH   A O   1 
HETATM 3007 O  O   . HOH   F 5 .   ? 48.927 1.459   -24.734 1.00 36.21  ?  534 HOH   A O   1 
HETATM 3008 O  O   . HOH   F 5 .   ? 25.584 -31.193 -35.958 1.00 63.81  ?  535 HOH   A O   1 
HETATM 3009 O  O   . HOH   F 5 .   ? 62.707 -1.854  -22.117 1.00 41.17  ?  536 HOH   A O   1 
HETATM 3010 O  O   . HOH   F 5 .   ? 61.771 -3.311  -29.525 1.00 48.15  ?  537 HOH   A O   1 
HETATM 3011 O  O   . HOH   F 5 .   ? 39.990 -3.129  -24.516 1.00 48.22  ?  538 HOH   A O   1 
HETATM 3012 O  O   . HOH   F 5 .   ? 59.541 -26.759 -44.695 1.00 52.42  ?  539 HOH   A O   1 
HETATM 3013 O  O   . HOH   F 5 .   ? 64.606 -5.617  -9.758  1.00 45.22  ?  540 HOH   A O   1 
HETATM 3014 O  O   . HOH   F 5 .   ? 43.094 -21.906 -30.573 1.00 43.70  ?  541 HOH   A O   1 
HETATM 3015 O  O   . HOH   F 5 .   ? 40.404 -17.521 -42.569 1.00 45.28  ?  542 HOH   A O   1 
HETATM 3016 O  O   . HOH   F 5 .   ? 52.032 -5.597  -28.207 1.00 33.80  ?  543 HOH   A O   1 
HETATM 3017 O  O   . HOH   F 5 .   ? 62.756 -26.930 -41.363 1.00 46.36  ?  544 HOH   A O   1 
HETATM 3018 O  O   . HOH   F 5 .   ? 57.391 -3.867  -13.077 1.00 42.16  ?  545 HOH   A O   1 
HETATM 3019 O  O   . HOH   F 5 .   ? 58.563 -12.815 -37.715 1.00 42.11  ?  546 HOH   A O   1 
HETATM 3020 O  O   . HOH   F 5 .   ? 50.382 -3.907  -29.491 1.00 42.07  ?  547 HOH   A O   1 
HETATM 3021 O  O   . HOH   F 5 .   ? 25.954 -10.884 -23.190 1.00 54.66  ?  548 HOH   A O   1 
HETATM 3022 O  O   . HOH   F 5 .   ? 44.436 -20.730 -40.903 1.00 42.86  ?  549 HOH   A O   1 
HETATM 3023 O  O   . HOH   F 5 .   ? 58.847 -10.309 -9.590  1.00 43.05  ?  550 HOH   A O   1 
HETATM 3024 O  O   . HOH   F 5 .   ? 37.104 -21.629 -22.351 1.00 44.31  ?  551 HOH   A O   1 
HETATM 3025 O  O   . HOH   F 5 .   ? 65.686 -9.764  -16.923 1.00 43.76  ?  552 HOH   A O   1 
HETATM 3026 O  O   . HOH   F 5 .   ? 58.542 -15.335 -28.221 1.00 39.25  ?  553 HOH   A O   1 
HETATM 3027 O  O   . HOH   F 5 .   ? 39.219 0.344   -26.037 1.00 43.69  ?  554 HOH   A O   1 
HETATM 3028 O  O   . HOH   F 5 .   ? 45.013 -33.312 -49.128 1.00 60.57  ?  555 HOH   A O   1 
HETATM 3029 O  O   . HOH   F 5 .   ? 62.203 -27.337 -49.684 1.00 55.66  ?  556 HOH   A O   1 
HETATM 3030 O  O   . HOH   F 5 .   ? 35.479 -17.795 -13.516 1.00 50.56  ?  557 HOH   A O   1 
HETATM 3031 O  O   . HOH   F 5 .   ? 57.053 -16.853 -26.703 1.00 43.19  ?  558 HOH   A O   1 
HETATM 3032 O  O   . HOH   F 5 .   ? 31.500 0.685   -25.842 1.00 62.04  ?  559 HOH   A O   1 
HETATM 3033 O  O   . HOH   F 5 .   ? 50.742 -8.199  -38.112 1.00 54.91  ?  560 HOH   A O   1 
HETATM 3034 O  O   . HOH   F 5 .   ? 59.939 -2.133  -23.045 1.00 36.40  ?  561 HOH   A O   1 
HETATM 3035 O  O   . HOH   F 5 .   ? 71.397 -11.371 -7.824  1.00 74.20  ?  562 HOH   A O   1 
HETATM 3036 O  O   . HOH   F 5 .   ? 30.360 -5.023  -11.492 1.00 60.67  ?  563 HOH   A O   1 
HETATM 3037 O  O   . HOH   F 5 .   ? 29.788 -11.126 -16.631 1.00 50.47  ?  564 HOH   A O   1 
HETATM 3038 O  O   . HOH   F 5 .   ? 28.097 -6.414  -31.895 1.00 58.24  ?  565 HOH   A O   1 
HETATM 3039 O  O   . HOH   F 5 .   ? 33.358 0.080   -14.168 1.00 56.57  ?  566 HOH   A O   1 
HETATM 3040 O  O   . HOH   F 5 .   ? 42.783 -3.567  -30.897 1.00 73.73  ?  567 HOH   A O   1 
HETATM 3041 O  O   . HOH   F 5 .   ? 37.236 -1.588  -6.538  1.00 62.22  ?  568 HOH   A O   1 
HETATM 3042 O  O   . HOH   F 5 .   ? 66.591 -8.836  -33.075 1.00 65.39  ?  569 HOH   A O   1 
HETATM 3043 O  O   . HOH   F 5 .   ? 57.884 -8.337  -33.480 1.00 50.33  ?  570 HOH   A O   1 
HETATM 3044 O  O   . HOH   F 5 .   ? 51.163 -11.348 -32.348 1.00 39.84  ?  571 HOH   A O   1 
HETATM 3045 O  O   . HOH   F 5 .   ? 57.416 -1.346  -16.640 1.00 48.37  ?  572 HOH   A O   1 
HETATM 3046 O  O   . HOH   F 5 .   ? 58.574 -16.488 -2.425  1.00 70.16  ?  573 HOH   A O   1 
HETATM 3047 O  O   . HOH   F 5 .   ? 57.575 -13.824 -2.915  1.00 61.43  ?  574 HOH   A O   1 
HETATM 3048 O  O   . HOH   F 5 .   ? 26.129 -8.310  -30.824 1.00 56.38  ?  575 HOH   A O   1 
HETATM 3049 O  O   . HOH   F 5 .   ? 21.023 -23.984 -45.928 1.00 64.34  ?  576 HOH   A O   1 
HETATM 3050 O  O   . HOH   F 5 .   ? 50.351 -4.958  -11.724 1.00 38.18  ?  577 HOH   A O   1 
HETATM 3051 O  O   . HOH   F 5 .   ? 58.696 -27.127 -35.394 1.00 53.28  ?  578 HOH   A O   1 
HETATM 3052 O  O   . HOH   F 5 .   ? 28.948 -16.788 -46.620 1.00 63.41  ?  579 HOH   A O   1 
HETATM 3053 O  O   . HOH   F 5 .   ? 50.460 -4.665  -32.220 1.00 61.82  ?  580 HOH   A O   1 
HETATM 3054 O  O   . HOH   F 5 .   ? 30.643 -12.250 -48.336 1.00 60.38  ?  581 HOH   A O   1 
HETATM 3055 O  O   . HOH   F 5 .   ? 31.228 1.274   -23.326 1.00 56.98  ?  582 HOH   A O   1 
HETATM 3056 O  O   . HOH   F 5 .   ? 38.321 -22.189 -28.732 1.00 59.11  ?  583 HOH   A O   1 
HETATM 3057 O  O   . HOH   F 5 .   ? 56.501 -22.476 -30.059 1.00 62.27  ?  584 HOH   A O   1 
HETATM 3058 O  O   . HOH   F 5 .   ? 37.025 -8.941  -41.158 1.00 57.79  ?  585 HOH   A O   1 
HETATM 3059 O  O   . HOH   F 5 .   ? 32.742 -35.563 -44.725 1.00 63.57  ?  586 HOH   A O   1 
HETATM 3060 O  O   . HOH   F 5 .   ? 46.374 -1.839  -30.423 1.00 69.35  ?  587 HOH   A O   1 
HETATM 3061 O  O   . HOH   F 5 .   ? 41.326 -15.450 -43.871 1.00 48.15  ?  588 HOH   A O   1 
HETATM 3062 O  O   . HOH   F 5 .   ? 42.215 -8.167  -43.527 1.00 49.30  ?  589 HOH   A O   1 
HETATM 3063 O  O   . HOH   F 5 .   ? 71.307 -12.502 -10.402 1.00 69.77  ?  590 HOH   A O   1 
HETATM 3064 O  O   . HOH   F 5 .   ? 22.358 -19.200 -24.124 1.00 74.15  ?  591 HOH   A O   1 
HETATM 3065 O  O   . HOH   F 5 .   ? 36.718 -11.580 -7.540  1.00 64.90  ?  592 HOH   A O   1 
HETATM 3066 O  O   . HOH   F 5 .   ? 66.082 -16.329 -19.018 1.00 68.86  ?  593 HOH   A O   1 
HETATM 3067 O  O   . HOH   F 5 .   ? 64.614 -11.474 -18.683 1.00 48.43  ?  594 HOH   A O   1 
HETATM 3068 O  O   . HOH   F 5 .   ? 62.054 -21.447 -47.619 1.00 52.39  ?  595 HOH   A O   1 
HETATM 3069 O  O   . HOH   F 5 .   ? 36.936 -8.719  -38.269 1.00 54.96  ?  596 HOH   A O   1 
HETATM 3070 O  O   . HOH   F 5 .   ? 60.556 -17.281 -55.058 1.00 46.58  ?  597 HOH   A O   1 
HETATM 3071 O  O   . HOH   F 5 .   ? 59.141 -20.424 -15.243 1.00 59.01  ?  598 HOH   A O   1 
HETATM 3072 O  O   . HOH   F 5 .   ? 29.523 0.549   -16.154 1.00 66.44  ?  599 HOH   A O   1 
HETATM 3073 O  O   . HOH   F 5 .   ? 49.784 -0.413  -10.278 1.00 71.50  ?  600 HOH   A O   1 
HETATM 3074 O  O   . HOH   F 5 .   ? 28.695 -7.939  -21.317 1.00 47.95  ?  601 HOH   A O   1 
HETATM 3075 O  O   . HOH   F 5 .   ? 34.455 -3.393  -31.010 1.00 58.05  ?  602 HOH   A O   1 
HETATM 3076 O  O   . HOH   F 5 .   ? 40.470 -20.788 -30.541 1.00 50.85  ?  603 HOH   A O   1 
HETATM 3077 O  O   . HOH   F 5 .   ? 68.737 -19.706 -37.377 1.00 65.86  ?  604 HOH   A O   1 
HETATM 3078 O  O   . HOH   F 5 .   ? 58.529 -8.058  -35.752 1.00 59.62  ?  605 HOH   A O   1 
HETATM 3079 O  O   . HOH   F 5 .   ? 68.758 -6.815  -18.159 1.00 65.71  ?  606 HOH   A O   1 
HETATM 3080 O  O   . HOH   F 5 .   ? 48.690 1.479   -27.394 1.00 40.82  ?  607 HOH   A O   1 
HETATM 3081 O  O   . HOH   F 5 .   ? 41.052 -6.017  -4.418  1.00 53.63  ?  608 HOH   A O   1 
HETATM 3082 O  O   . HOH   F 5 .   ? 50.499 -16.140 -3.202  1.00 61.43  ?  609 HOH   A O   1 
HETATM 3083 O  O   . HOH   F 5 .   ? 38.643 -16.117 -40.477 1.00 50.08  ?  610 HOH   A O   1 
HETATM 3084 O  O   . HOH   F 5 .   ? 55.721 -6.228  -31.865 1.00 63.61  ?  611 HOH   A O   1 
HETATM 3085 O  O   . HOH   F 5 .   ? 32.229 4.661   -7.952  1.00 77.99  ?  612 HOH   A O   1 
HETATM 3086 O  O   . HOH   F 5 .   ? 51.475 -2.830  -4.450  1.00 68.72  ?  613 HOH   A O   1 
HETATM 3087 O  O   . HOH   F 5 .   ? 46.264 -19.185 -5.025  1.00 52.24  ?  614 HOH   A O   1 
HETATM 3088 O  O   . HOH   F 5 .   ? 57.343 -19.822 -26.443 1.00 50.32  ?  615 HOH   A O   1 
HETATM 3089 O  O   . HOH   F 5 .   ? 55.835 -21.550 -26.995 1.00 63.76  ?  616 HOH   A O   1 
HETATM 3090 O  O   . HOH   F 5 .   ? 34.617 -0.575  -29.202 1.00 73.21  ?  617 HOH   A O   1 
HETATM 3091 O  O   . HOH   F 5 .   ? 38.312 -6.229  -36.668 1.00 48.63  ?  618 HOH   A O   1 
HETATM 3092 O  O   . HOH   F 5 .   ? 48.648 -5.537  -7.234  1.00 53.34  ?  619 HOH   A O   1 
HETATM 3093 O  O   . HOH   F 5 .   ? 31.342 -7.148  -12.806 1.00 56.93  ?  620 HOH   A O   1 
HETATM 3094 O  O   . HOH   F 5 .   ? 29.691 -1.175  -5.094  1.00 64.82  ?  621 HOH   A O   1 
HETATM 3095 O  O   . HOH   F 5 .   ? 57.828 -16.121 -56.396 1.00 63.21  ?  622 HOH   A O   1 
HETATM 3096 O  O   . HOH   F 5 .   ? 61.130 -22.346 -31.894 1.00 64.51  ?  623 HOH   A O   1 
HETATM 3097 O  O   . HOH   F 5 .   ? 60.497 -19.788 -2.755  1.00 70.90  ?  624 HOH   A O   1 
HETATM 3098 O  O   . HOH   F 5 .   ? 47.145 -5.980  -35.417 1.00 72.50  ?  625 HOH   A O   1 
HETATM 3099 O  O   . HOH   F 5 .   ? 47.799 -22.895 -21.266 1.00 42.02  ?  626 HOH   A O   1 
HETATM 3100 O  O   . HOH   F 5 .   ? 57.753 -19.095 -1.868  1.00 66.70  ?  627 HOH   A O   1 
HETATM 3101 O  O   . HOH   F 5 .   ? 35.862 3.887   -16.543 1.00 57.25  ?  628 HOH   A O   1 
HETATM 3102 O  O   . HOH   F 5 .   ? 71.910 -8.374  -28.466 1.00 65.90  ?  629 HOH   A O   1 
HETATM 3103 O  O   . HOH   F 5 .   ? 31.175 -2.622  -31.530 1.00 73.93  ?  630 HOH   A O   1 
HETATM 3104 O  O   . HOH   F 5 .   ? 46.573 -21.994 -31.493 1.00 59.30  ?  631 HOH   A O   1 
HETATM 3105 O  O   . HOH   F 5 .   ? 51.361 -20.972 -27.865 1.00 59.83  ?  632 HOH   A O   1 
HETATM 3106 O  O   . HOH   F 5 .   ? 45.169 -22.841 -23.734 1.00 64.49  ?  633 HOH   A O   1 
HETATM 3107 O  O   . HOH   F 5 .   ? 47.987 1.919   -14.197 1.00 54.23  ?  634 HOH   A O   1 
HETATM 3108 O  O   . HOH   F 5 .   ? 31.197 -4.747  -17.888 1.00 57.52  ?  635 HOH   A O   1 
HETATM 3109 O  O   . HOH   F 5 .   ? 65.659 -13.981 -17.614 1.00 60.45  ?  636 HOH   A O   1 
HETATM 3110 O  O   . HOH   F 5 .   ? 42.013 -7.600  -40.153 1.00 66.36  ?  637 HOH   A O   1 
HETATM 3111 O  O   . HOH   F 5 .   ? 41.057 -26.486 -36.261 1.00 46.32  ?  638 HOH   A O   1 
HETATM 3112 O  O   . HOH   F 5 .   ? 32.876 5.315   -13.004 1.00 63.23  ?  639 HOH   A O   1 
HETATM 3113 O  O   . HOH   F 5 .   ? 52.727 -7.048  -38.875 1.00 65.67  ?  640 HOH   A O   1 
HETATM 3114 O  O   . HOH   F 5 .   ? 44.394 -9.667  -39.045 1.00 55.97  ?  641 HOH   A O   1 
HETATM 3115 O  O   . HOH   F 5 .   ? 67.040 -15.819 -21.405 1.00 65.31  ?  642 HOH   A O   1 
HETATM 3116 O  O   . HOH   F 5 .   ? 49.537 -25.587 -31.074 1.00 58.95  ?  643 HOH   A O   1 
HETATM 3117 O  O   . HOH   F 5 .   ? 37.970 -29.027 -59.123 1.00 71.00  ?  644 HOH   A O   1 
HETATM 3118 O  O   . HOH   F 5 .   ? 68.374 -10.722 -16.017 1.00 69.06  ?  645 HOH   A O   1 
HETATM 3119 O  O   . HOH   F 5 .   ? 29.121 -8.786  -17.863 1.00 63.57  ?  646 HOH   A O   1 
HETATM 3120 O  O   . HOH   F 5 .   ? 58.378 -22.822 -32.122 1.00 66.87  ?  647 HOH   A O   1 
HETATM 3121 O  O   . HOH   F 5 .   ? 49.806 -3.467  -9.432  1.00 56.72  ?  648 HOH   A O   1 
HETATM 3122 O  O   . HOH   F 5 .   ? 30.133 5.303   -12.485 1.00 70.90  ?  649 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   . ALA A 1   ? 1.2879 1.5775 0.9258 0.1974  -0.0372 -0.2924 16  ALA A N   
2    C CA  . ALA A 1   ? 1.2856 1.5336 0.9616 0.1893  -0.0625 -0.3092 16  ALA A CA  
3    C C   . ALA A 1   ? 1.2677 1.5176 0.9185 0.1877  -0.0913 -0.3347 16  ALA A C   
4    O O   . ALA A 1   ? 1.2481 1.5294 0.8546 0.1909  -0.0947 -0.3279 16  ALA A O   
5    C CB  . ALA A 1   ? 1.1673 1.3903 0.8784 0.1771  -0.0657 -0.2705 16  ALA A CB  
6    N N   . PRO A 2   ? 1.2358 1.4520 0.9144 0.1825  -0.1129 -0.3637 17  PRO A N   
7    C CA  . PRO A 2   ? 1.2365 1.4527 0.8979 0.1785  -0.1420 -0.3893 17  PRO A CA  
8    C C   . PRO A 2   ? 1.1577 1.3822 0.8135 0.1679  -0.1573 -0.3585 17  PRO A C   
9    O O   . PRO A 2   ? 0.9134 1.1324 0.5881 0.1619  -0.1488 -0.3192 17  PRO A O   
10   C CB  . PRO A 2   ? 1.1533 1.3240 0.8570 0.1720  -0.1591 -0.4175 17  PRO A CB  
11   C CG  . PRO A 2   ? 1.2296 1.3870 0.9570 0.1805  -0.1376 -0.4219 17  PRO A CG  
12   C CD  . PRO A 2   ? 1.1754 1.3539 0.9001 0.1816  -0.1116 -0.3789 17  PRO A CD  
13   N N   . LYS A 3   ? 1.0800 1.3187 0.7110 0.1665  -0.1813 -0.3797 18  LYS A N   
14   C CA  . LYS A 3   ? 1.1607 1.4138 0.7852 0.1584  -0.1994 -0.3564 18  LYS A CA  
15   C C   . LYS A 3   ? 1.0074 1.2314 0.6816 0.1438  -0.2044 -0.3296 18  LYS A C   
16   O O   . LYS A 3   ? 1.0052 1.2400 0.6821 0.1415  -0.2004 -0.2917 18  LYS A O   
17   C CB  . LYS A 3   ? 1.0275 1.2899 0.6351 0.1557  -0.2300 -0.3925 18  LYS A CB  
18   C CG  . LYS A 3   ? 1.1678 1.4601 0.7237 0.1699  -0.2278 -0.4213 18  LYS A CG  
19   C CD  . LYS A 3   ? 1.1243 1.4134 0.6838 0.1611  -0.2527 -0.4449 18  LYS A CD  
20   C CE  . LYS A 3   ? 1.2034 1.5145 0.7550 0.1542  -0.2726 -0.4222 18  LYS A CE  
21   N NZ  . LYS A 3   ? 1.2863 1.6383 0.7873 0.1666  -0.2623 -0.3934 18  LYS A NZ  
22   N N   . TYR A 4   ? 1.0198 1.2064 0.7328 0.1344  -0.2136 -0.3494 19  TYR A N   
23   C CA  . TYR A 4   ? 0.9271 1.0879 0.6837 0.1191  -0.2214 -0.3287 19  TYR A CA  
24   C C   . TYR A 4   ? 0.9591 1.1096 0.7348 0.1204  -0.1979 -0.2917 19  TYR A C   
25   O O   . TYR A 4   ? 0.8352 0.9829 0.6317 0.1124  -0.1997 -0.2626 19  TYR A O   
26   C CB  . TYR A 4   ? 0.9970 1.1191 0.7854 0.1087  -0.2368 -0.3590 19  TYR A CB  
27   C CG  . TYR A 4   ? 1.1043 1.2063 0.8925 0.1190  -0.2260 -0.3864 19  TYR A CG  
28   C CD1 . TYR A 4   ? 1.1513 1.2597 0.9162 0.1274  -0.2352 -0.4288 19  TYR A CD1 
29   C CD2 . TYR A 4   ? 1.0340 1.1118 0.8467 0.1215  -0.2075 -0.3717 19  TYR A CD2 
30   C CE1 . TYR A 4   ? 1.1533 1.2442 0.9221 0.1389  -0.2249 -0.4554 19  TYR A CE1 
31   C CE2 . TYR A 4   ? 0.9333 0.9949 0.7505 0.1321  -0.1986 -0.3966 19  TYR A CE2 
32   C CZ  . TYR A 4   ? 1.0607 1.1286 0.8576 0.1411  -0.2065 -0.4376 19  TYR A CZ  
33   O OH  . TYR A 4   ? 1.1534 1.2055 0.9600 0.1534  -0.1965 -0.4615 19  TYR A OH  
34   N N   . ILE A 5   ? 0.9121 1.0592 0.6827 0.1309  -0.1758 -0.2934 20  ILE A N   
35   C CA  . ILE A 5   ? 0.8694 1.0099 0.6575 0.1323  -0.1541 -0.2595 20  ILE A CA  
36   C C   . ILE A 5   ? 0.8550 1.0271 0.6190 0.1365  -0.1454 -0.2254 20  ILE A C   
37   O O   . ILE A 5   ? 0.7515 0.9172 0.5351 0.1326  -0.1392 -0.1929 20  ILE A O   
38   C CB  . ILE A 5   ? 0.8894 1.0224 0.6817 0.1421  -0.1335 -0.2717 20  ILE A CB  
39   C CG1 . ILE A 5   ? 0.9531 1.0457 0.7797 0.1376  -0.1426 -0.2956 20  ILE A CG1 
40   C CG2 . ILE A 5   ? 0.8024 0.9393 0.6056 0.1447  -0.1098 -0.2366 20  ILE A CG2 
41   C CD1 . ILE A 5   ? 0.9173 1.0066 0.7471 0.1499  -0.1276 -0.3178 20  ILE A CD1 
42   N N   . GLU A 6   ? 0.8275 1.0331 0.5476 0.1452  -0.1459 -0.2325 21  GLU A N   
43   C CA  . GLU A 6   ? 0.9394 1.1742 0.6318 0.1503  -0.1392 -0.1987 21  GLU A CA  
44   C C   . GLU A 6   ? 0.9101 1.1458 0.6169 0.1428  -0.1583 -0.1779 21  GLU A C   
45   O O   . GLU A 6   ? 0.8936 1.1314 0.6083 0.1434  -0.1503 -0.1417 21  GLU A O   
46   C CB  . GLU A 6   ? 0.9822 1.2530 0.6199 0.1610  -0.1395 -0.2135 21  GLU A CB  
47   C CG  . GLU A 6   ? 1.1045 1.3906 0.7200 0.1709  -0.1097 -0.2084 21  GLU A CG  
48   C CD  . GLU A 6   ? 1.2304 1.5189 0.8524 0.1707  -0.0898 -0.1611 21  GLU A CD  
49   O OE1 . GLU A 6   ? 1.1359 1.4390 0.7394 0.1713  -0.0977 -0.1328 21  GLU A OE1 
50   O OE2 . GLU A 6   ? 1.2368 1.5116 0.8853 0.1699  -0.0682 -0.1529 21  GLU A OE2 
51   N N   . HIS A 7   ? 0.8269 1.0617 0.5398 0.1357  -0.1837 -0.2012 22  HIS A N   
52   C CA  . HIS A 7   ? 0.8312 1.0706 0.5636 0.1280  -0.2021 -0.1849 22  HIS A CA  
53   C C   . HIS A 7   ? 0.8486 1.0619 0.6256 0.1205  -0.1932 -0.1605 22  HIS A C   
54   O O   . HIS A 7   ? 0.7752 0.9970 0.5591 0.1228  -0.1902 -0.1287 22  HIS A O   
55   C CB  . HIS A 7   ? 0.9018 1.1406 0.6433 0.1184  -0.2291 -0.2178 22  HIS A CB  
56   C CG  . HIS A 7   ? 0.8968 1.1457 0.6627 0.1096  -0.2480 -0.2044 22  HIS A CG  
57   N ND1 . HIS A 7   ? 0.8873 1.1136 0.6990 0.0945  -0.2552 -0.2069 22  HIS A ND1 
58   C CD2 . HIS A 7   ? 0.9400 1.2212 0.6919 0.1143  -0.2610 -0.1878 22  HIS A CD2 
59   C CE1 . HIS A 7   ? 0.8723 1.1194 0.6995 0.0899  -0.2703 -0.1939 22  HIS A CE1 
60   N NE2 . HIS A 7   ? 0.9876 1.2676 0.7804 0.1025  -0.2752 -0.1826 22  HIS A NE2 
61   N N   . PHE A 8   ? 0.7889 0.9697 0.5962 0.1123  -0.1902 -0.1758 23  PHE A N   
62   C CA  . PHE A 8   ? 0.7320 0.8894 0.5791 0.1043  -0.1852 -0.1559 23  PHE A CA  
63   C C   . PHE A 8   ? 0.7105 0.8618 0.5608 0.1117  -0.1619 -0.1277 23  PHE A C   
64   O O   . PHE A 8   ? 0.6926 0.8335 0.5689 0.1083  -0.1584 -0.1056 23  PHE A O   
65   C CB  . PHE A 8   ? 0.7099 0.8329 0.5850 0.0934  -0.1900 -0.1781 23  PHE A CB  
66   C CG  . PHE A 8   ? 0.7523 0.8759 0.6372 0.0812  -0.2137 -0.1996 23  PHE A CG  
67   C CD1 . PHE A 8   ? 0.6775 0.8103 0.5850 0.0713  -0.2250 -0.1857 23  PHE A CD1 
68   C CD2 . PHE A 8   ? 0.7246 0.8406 0.5990 0.0797  -0.2249 -0.2348 23  PHE A CD2 
69   C CE1 . PHE A 8   ? 0.7684 0.9044 0.6895 0.0580  -0.2465 -0.2051 23  PHE A CE1 
70   C CE2 . PHE A 8   ? 0.8197 0.9348 0.7064 0.0668  -0.2479 -0.2551 23  PHE A CE2 
71   C CZ  . PHE A 8   ? 0.7957 0.9214 0.7066 0.0549  -0.2585 -0.2395 23  PHE A CZ  
72   N N   . SER A 9   ? 0.7245 0.8838 0.5505 0.1215  -0.1458 -0.1284 24  SER A N   
73   C CA  . SER A 9   ? 0.7219 0.8761 0.5547 0.1266  -0.1238 -0.1015 24  SER A CA  
74   C C   . SER A 9   ? 0.8058 0.9799 0.6261 0.1318  -0.1218 -0.0677 24  SER A C   
75   O O   . SER A 9   ? 0.8673 1.0332 0.7003 0.1340  -0.1065 -0.0423 24  SER A O   
76   C CB  . SER A 9   ? 0.7802 0.9401 0.5946 0.1342  -0.1053 -0.1124 24  SER A CB  
77   O OG  . SER A 9   ? 0.7335 0.9261 0.5041 0.1420  -0.1049 -0.1137 24  SER A OG  
78   N N   . LYS A 10  ? 0.7427 0.9419 0.5395 0.1343  -0.1381 -0.0671 25  LYS A N   
79   C CA  . LYS A 10  ? 0.7955 1.0112 0.5828 0.1405  -0.1396 -0.0339 25  LYS A CA  
80   C C   . LYS A 10  ? 0.8529 1.0587 0.6776 0.1359  -0.1498 -0.0196 25  LYS A C   
81   O O   . LYS A 10  ? 0.8852 1.0999 0.7101 0.1422  -0.1510 0.0085  25  LYS A O   
82   C CB  . LYS A 10  ? 0.8838 1.1330 0.6284 0.1472  -0.1542 -0.0378 25  LYS A CB  
83   C CG  . LYS A 10  ? 0.9400 1.2043 0.6412 0.1540  -0.1408 -0.0483 25  LYS A CG  
84   C CD  . LYS A 10  ? 1.1355 1.4346 0.7874 0.1622  -0.1543 -0.0480 25  LYS A CD  
85   C CE  . LYS A 10  ? 1.3545 1.6660 0.9915 0.1700  -0.1527 -0.0051 25  LYS A CE  
86   N NZ  . LYS A 10  ? 1.3157 1.6609 0.8935 0.1801  -0.1589 -0.0005 25  LYS A NZ  
87   N N   . PHE A 11  ? 0.6759 0.8638 0.5317 0.1256  -0.1568 -0.0378 26  PHE A N   
88   C CA  . PHE A 11  ? 0.6736 0.8514 0.5663 0.1210  -0.1610 -0.0248 26  PHE A CA  
89   C C   . PHE A 11  ? 0.6882 0.8376 0.6029 0.1206  -0.1418 -0.0128 26  PHE A C   
90   O O   . PHE A 11  ? 0.7099 0.8441 0.6206 0.1198  -0.1293 -0.0230 26  PHE A O   
91   C CB  . PHE A 11  ? 0.6791 0.8527 0.5941 0.1083  -0.1765 -0.0478 26  PHE A CB  
92   C CG  . PHE A 11  ? 0.7663 0.9683 0.6667 0.1067  -0.1982 -0.0624 26  PHE A CG  
93   C CD1 . PHE A 11  ? 0.7961 1.0045 0.6678 0.1066  -0.2044 -0.0875 26  PHE A CD1 
94   C CD2 . PHE A 11  ? 0.6744 0.8981 0.5920 0.1057  -0.2132 -0.0534 26  PHE A CD2 
95   C CE1 . PHE A 11  ? 0.8706 1.1055 0.7287 0.1050  -0.2266 -0.1035 26  PHE A CE1 
96   C CE2 . PHE A 11  ? 0.7847 1.0368 0.6920 0.1037  -0.2353 -0.0683 26  PHE A CE2 
97   C CZ  . PHE A 11  ? 0.8239 1.0809 0.7006 0.1030  -0.2426 -0.0934 26  PHE A CZ  
98   N N   . SER A 12  ? 0.5886 0.7324 0.5276 0.1222  -0.1402 0.0074  27  SER A N   
99   C CA  . SER A 12  ? 0.6898 0.8048 0.6501 0.1200  -0.1250 0.0108  27  SER A CA  
100  C C   . SER A 12  ? 0.6283 0.7272 0.6172 0.1100  -0.1308 -0.0014 27  SER A C   
101  O O   . SER A 12  ? 0.6136 0.7262 0.6123 0.1058  -0.1439 -0.0043 27  SER A O   
102  C CB  . SER A 12  ? 0.7543 0.8643 0.7241 0.1281  -0.1146 0.0397  27  SER A CB  
103  O OG  . SER A 12  ? 0.8558 0.9799 0.8350 0.1327  -0.1257 0.0536  27  SER A OG  
104  N N   . PRO A 13  ? 0.5655 0.6372 0.5678 0.1056  -0.1217 -0.0087 28  PRO A N   
105  C CA  . PRO A 13  ? 0.5822 0.6377 0.6078 0.0960  -0.1264 -0.0168 28  PRO A CA  
106  C C   . PRO A 13  ? 0.6089 0.6726 0.6542 0.0978  -0.1281 -0.0007 28  PRO A C   
107  O O   . PRO A 13  ? 0.5667 0.6358 0.6142 0.1076  -0.1225 0.0179  28  PRO A O   
108  C CB  . PRO A 13  ? 0.5454 0.5713 0.5792 0.0955  -0.1151 -0.0207 28  PRO A CB  
109  C CG  . PRO A 13  ? 0.5713 0.6010 0.5861 0.1015  -0.1074 -0.0255 28  PRO A CG  
110  C CD  . PRO A 13  ? 0.5829 0.6395 0.5805 0.1091  -0.1070 -0.0095 28  PRO A CD  
111  N N   . SER A 14  ? 0.5269 0.5926 0.5877 0.0881  -0.1359 -0.0082 29  SER A N   
112  C CA  . SER A 14  ? 0.4681 0.5456 0.5507 0.0896  -0.1367 0.0034  29  SER A CA  
113  C C   . SER A 14  ? 0.5043 0.5573 0.6028 0.0853  -0.1281 0.0032  29  SER A C   
114  O O   . SER A 14  ? 0.5324 0.5743 0.6349 0.0729  -0.1306 -0.0081 29  SER A O   
115  C CB  . SER A 14  ? 0.5045 0.6086 0.5960 0.0815  -0.1502 -0.0038 29  SER A CB  
116  O OG  . SER A 14  ? 0.7325 0.8627 0.8091 0.0875  -0.1606 -0.0028 29  SER A OG  
117  N N   . PRO A 15  ? 0.5379 0.5803 0.6446 0.0946  -0.1187 0.0152  30  PRO A N   
118  C CA  . PRO A 15  ? 0.5903 0.6087 0.7076 0.0914  -0.1116 0.0129  30  PRO A CA  
119  C C   . PRO A 15  ? 0.5419 0.5726 0.6761 0.0867  -0.1125 0.0132  30  PRO A C   
120  O O   . PRO A 15  ? 0.4888 0.5450 0.6350 0.0924  -0.1151 0.0200  30  PRO A O   
121  C CB  . PRO A 15  ? 0.5436 0.5494 0.6651 0.1035  -0.1028 0.0243  30  PRO A CB  
122  C CG  . PRO A 15  ? 0.5340 0.5610 0.6532 0.1132  -0.1053 0.0374  30  PRO A CG  
123  C CD  . PRO A 15  ? 0.5492 0.5962 0.6523 0.1080  -0.1145 0.0306  30  PRO A CD  
124  N N   . LEU A 16  ? 0.5765 0.5902 0.7117 0.0765  -0.1103 0.0061  31  LEU A N   
125  C CA  . LEU A 16  ? 0.5610 0.5869 0.7098 0.0696  -0.1085 0.0062  31  LEU A CA  
126  C C   . LEU A 16  ? 0.5554 0.5652 0.7084 0.0756  -0.0992 0.0093  31  LEU A C   
127  O O   . LEU A 16  ? 0.5483 0.5292 0.6916 0.0772  -0.0966 0.0070  31  LEU A O   
128  C CB  . LEU A 16  ? 0.5830 0.6029 0.7279 0.0512  -0.1132 -0.0023 31  LEU A CB  
129  C CG  . LEU A 16  ? 0.6217 0.6581 0.7644 0.0438  -0.1246 -0.0092 31  LEU A CG  
130  C CD1 . LEU A 16  ? 0.6204 0.6431 0.7612 0.0250  -0.1301 -0.0183 31  LEU A CD1 
131  C CD2 . LEU A 16  ? 0.6650 0.7421 0.8243 0.0469  -0.1288 -0.0050 31  LEU A CD2 
132  N N   . SER A 17  ? 0.5602 0.5905 0.7286 0.0795  -0.0947 0.0126  32  SER A N   
133  C CA  . SER A 17  ? 0.5174 0.5349 0.6876 0.0844  -0.0862 0.0121  32  SER A CA  
134  C C   . SER A 17  ? 0.5492 0.5579 0.7105 0.0692  -0.0833 0.0082  32  SER A C   
135  O O   . SER A 17  ? 0.5459 0.5662 0.7082 0.0546  -0.0865 0.0072  32  SER A O   
136  C CB  . SER A 17  ? 0.5466 0.5902 0.7368 0.0962  -0.0817 0.0150  32  SER A CB  
137  O OG  . SER A 17  ? 0.5968 0.6686 0.7973 0.0864  -0.0790 0.0130  32  SER A OG  
138  N N   . MET A 18  ? 0.5805 0.5674 0.7327 0.0722  -0.0781 0.0065  33  MET A N   
139  C CA  . MET A 18  ? 0.6379 0.6168 0.7783 0.0595  -0.0742 0.0058  33  MET A CA  
140  C C   . MET A 18  ? 0.5920 0.6062 0.7455 0.0518  -0.0672 0.0080  33  MET A C   
141  O O   . MET A 18  ? 0.6413 0.6559 0.7887 0.0348  -0.0653 0.0105  33  MET A O   
142  C CB  . MET A 18  ? 0.6076 0.5642 0.7362 0.0677  -0.0702 0.0032  33  MET A CB  
143  C CG  . MET A 18  ? 0.6527 0.5931 0.7615 0.0554  -0.0685 0.0046  33  MET A CG  
144  S SD  . MET A 18  ? 0.8314 0.7274 0.9219 0.0527  -0.0798 0.0026  33  MET A SD  
145  C CE  . MET A 18  ? 0.5381 0.4185 0.6287 0.0717  -0.0801 -0.0037 33  MET A CE  
146  N N   . LYS A 19  ? 0.5496 0.5936 0.7230 0.0640  -0.0630 0.0077  34  LYS A N   
147  C CA  . LYS A 19  ? 0.6569 0.7403 0.8481 0.0578  -0.0558 0.0084  34  LYS A CA  
148  C C   . LYS A 19  ? 0.6709 0.7739 0.8735 0.0427  -0.0632 0.0103  34  LYS A C   
149  O O   . LYS A 19  ? 0.6536 0.7775 0.8648 0.0266  -0.0583 0.0118  34  LYS A O   
150  C CB  . LYS A 19  ? 0.5696 0.6800 0.7829 0.0773  -0.0514 0.0060  34  LYS A CB  
151  C CG  . LYS A 19  ? 0.6181 0.7750 0.8549 0.0735  -0.0427 0.0048  34  LYS A CG  
152  C CD  . LYS A 19  ? 0.7400 0.9185 0.9981 0.0961  -0.0382 0.0001  34  LYS A CD  
153  C CE  . LYS A 19  ? 0.6970 0.9288 0.9875 0.0958  -0.0330 -0.0018 34  LYS A CE  
154  N NZ  . LYS A 19  ? 0.8506 1.1000 1.1657 0.1216  -0.0339 -0.0062 34  LYS A NZ  
155  N N   . GLN A 20  ? 0.6272 0.7251 0.8303 0.0470  -0.0749 0.0099  35  GLN A N   
156  C CA  . GLN A 20  ? 0.6080 0.7231 0.8197 0.0334  -0.0844 0.0087  35  GLN A CA  
157  C C   . GLN A 20  ? 0.6842 0.7744 0.8814 0.0122  -0.0868 0.0075  35  GLN A C   
158  O O   . GLN A 20  ? 0.6868 0.7946 0.8963 -0.0057 -0.0880 0.0073  35  GLN A O   
159  C CB  . GLN A 20  ? 0.6249 0.7386 0.8337 0.0441  -0.0961 0.0080  35  GLN A CB  
160  C CG  . GLN A 20  ? 0.5558 0.6935 0.7805 0.0642  -0.0962 0.0121  35  GLN A CG  
161  C CD  . GLN A 20  ? 0.5964 0.7284 0.8118 0.0748  -0.1064 0.0150  35  GLN A CD  
162  O OE1 . GLN A 20  ? 0.6535 0.7542 0.8503 0.0794  -0.1056 0.0160  35  GLN A OE1 
163  N NE2 . GLN A 20  ? 0.7092 0.8737 0.9377 0.0788  -0.1158 0.0167  35  GLN A NE2 
164  N N   . PHE A 21  ? 0.6566 0.7049 0.8302 0.0139  -0.0883 0.0067  36  PHE A N   
165  C CA  . PHE A 21  ? 0.6146 0.6335 0.7738 -0.0037 -0.0909 0.0067  36  PHE A CA  
166  C C   . PHE A 21  ? 0.7176 0.7484 0.8812 -0.0187 -0.0807 0.0133  36  PHE A C   
167  O O   . PHE A 21  ? 0.7352 0.7629 0.9018 -0.0392 -0.0835 0.0154  36  PHE A O   
168  C CB  . PHE A 21  ? 0.6110 0.5874 0.7473 0.0043  -0.0921 0.0059  36  PHE A CB  
169  C CG  . PHE A 21  ? 0.6348 0.5923 0.7641 0.0110  -0.1022 -0.0010 36  PHE A CG  
170  C CD1 . PHE A 21  ? 0.6049 0.5539 0.7330 -0.0007 -0.1125 -0.0072 36  PHE A CD1 
171  C CD2 . PHE A 21  ? 0.5719 0.5201 0.6967 0.0287  -0.1008 -0.0021 36  PHE A CD2 
172  C CE1 . PHE A 21  ? 0.6733 0.6078 0.7935 0.0068  -0.1202 -0.0156 36  PHE A CE1 
173  C CE2 . PHE A 21  ? 0.6231 0.5575 0.7416 0.0344  -0.1074 -0.0080 36  PHE A CE2 
174  C CZ  . PHE A 21  ? 0.5693 0.4982 0.6844 0.0243  -0.1165 -0.0153 36  PHE A CZ  
175  N N   . LEU A 22  ? 0.6986 0.7432 0.8629 -0.0088 -0.0683 0.0163  37  LEU A N   
176  C CA  . LEU A 22  ? 0.7913 0.8486 0.9547 -0.0209 -0.0553 0.0229  37  LEU A CA  
177  C C   . LEU A 22  ? 0.8408 0.9457 1.0346 -0.0329 -0.0506 0.0239  37  LEU A C   
178  O O   . LEU A 22  ? 0.8848 0.9952 1.0823 -0.0551 -0.0461 0.0302  37  LEU A O   
179  C CB  . LEU A 22  ? 0.7626 0.8217 0.9162 -0.0037 -0.0441 0.0219  37  LEU A CB  
180  C CG  . LEU A 22  ? 0.8060 0.8518 0.9358 -0.0109 -0.0333 0.0280  37  LEU A CG  
181  C CD1 . LEU A 22  ? 0.7665 0.7646 0.8701 -0.0216 -0.0430 0.0331  37  LEU A CD1 
182  C CD2 . LEU A 22  ? 0.7291 0.7750 0.8497 0.0106  -0.0263 0.0218  37  LEU A CD2 
183  N N   . ASP A 23  ? 0.8405 0.9803 1.0581 -0.0187 -0.0522 0.0186  38  ASP A N   
184  C CA  . ASP A 23  ? 0.8740 1.0637 1.1256 -0.0276 -0.0500 0.0180  38  ASP A CA  
185  C C   . ASP A 23  ? 0.9239 1.1124 1.1846 -0.0504 -0.0618 0.0175  38  ASP A C   
186  O O   . ASP A 23  ? 1.0801 1.3074 1.3699 -0.0649 -0.0596 0.0178  38  ASP A O   
187  C CB  . ASP A 23  ? 0.9090 1.1302 1.1827 -0.0056 -0.0549 0.0126  38  ASP A CB  
188  C CG  . ASP A 23  ? 0.9674 1.1991 1.2430 0.0156  -0.0424 0.0112  38  ASP A CG  
189  O OD1 . ASP A 23  ? 0.9587 1.1856 1.2221 0.0116  -0.0280 0.0129  38  ASP A OD1 
190  O OD2 . ASP A 23  ? 0.8694 1.1127 1.1575 0.0368  -0.0477 0.0082  38  ASP A OD2 
191  N N   . PHE A 24  ? 0.8400 0.9861 1.0792 -0.0538 -0.0744 0.0153  39  PHE A N   
192  C CA  . PHE A 24  ? 0.9285 1.0669 1.1746 -0.0749 -0.0868 0.0122  39  PHE A CA  
193  C C   . PHE A 24  ? 1.0923 1.2062 1.3301 -0.0996 -0.0812 0.0207  39  PHE A C   
194  O O   . PHE A 24  ? 1.0883 1.1752 1.3229 -0.1151 -0.0932 0.0181  39  PHE A O   
195  C CB  . PHE A 24  ? 0.8661 0.9725 1.0943 -0.0660 -0.1029 0.0037  39  PHE A CB  
196  C CG  . PHE A 24  ? 1.1224 1.2334 1.3632 -0.0814 -0.1184 -0.0051 39  PHE A CG  
197  C CD1 . PHE A 24  ? 1.2342 1.3921 1.5037 -0.0836 -0.1246 -0.0100 39  PHE A CD1 
198  C CD2 . PHE A 24  ? 1.1423 1.2115 1.3683 -0.0935 -0.1282 -0.0097 39  PHE A CD2 
199  C CE1 . PHE A 24  ? 1.0855 1.2490 1.3672 -0.0983 -0.1408 -0.0204 39  PHE A CE1 
200  C CE2 . PHE A 24  ? 1.1314 1.2038 1.3700 -0.1076 -0.1436 -0.0207 39  PHE A CE2 
201  C CZ  . PHE A 24  ? 1.0156 1.1357 1.2815 -0.1105 -0.1501 -0.0265 39  PHE A CZ  
202  N N   . GLY A 25  ? 1.0742 1.1964 1.3077 -0.1031 -0.0636 0.0309  40  GLY A N   
203  C CA  . GLY A 25  ? 0.9571 1.0613 1.1829 -0.1279 -0.0566 0.0429  40  GLY A CA  
204  C C   . GLY A 25  ? 0.9555 0.9980 1.1510 -0.1326 -0.0675 0.0455  40  GLY A C   
205  O O   . GLY A 25  ? 1.0761 1.0956 1.2651 -0.1545 -0.0662 0.0564  40  GLY A O   
206  N N   . ASN A 28  ? 1.1541 1.2707 1.5511 -0.2905 -0.1378 0.0120  43  ASN A N   
207  C CA  . ASN A 28  ? 1.4001 1.5476 1.8407 -0.3108 -0.1532 -0.0017 43  ASN A CA  
208  C C   . ASN A 28  ? 1.3194 1.4989 1.7642 -0.2868 -0.1699 -0.0241 43  ASN A C   
209  O O   . ASN A 28  ? 1.1914 1.3391 1.6164 -0.2761 -0.1891 -0.0408 43  ASN A O   
210  C CB  . ASN A 28  ? 1.4732 1.6757 1.9570 -0.3347 -0.1362 0.0111  43  ASN A CB  
211  C CG  . ASN A 28  ? 1.5217 1.6942 2.0038 -0.3645 -0.1208 0.0348  43  ASN A CG  
212  O OD1 . ASN A 28  ? 1.4599 1.5787 1.9361 -0.3833 -0.1331 0.0361  43  ASN A OD1 
213  N ND2 . ASN A 28  ? 1.5408 1.7477 2.0273 -0.3682 -0.0938 0.0536  43  ASN A ND2 
214  N N   . ALA A 29  ? 1.2065 1.4503 1.6774 -0.2780 -0.1626 -0.0242 44  ALA A N   
215  C CA  . ALA A 29  ? 0.9477 1.2206 1.4155 -0.2505 -0.1761 -0.0399 44  ALA A CA  
216  C C   . ALA A 29  ? 0.9321 1.1709 1.3517 -0.2190 -0.1722 -0.0381 44  ALA A C   
217  O O   . ALA A 29  ? 0.8751 1.1139 1.2788 -0.1983 -0.1868 -0.0513 44  ALA A O   
218  C CB  . ALA A 29  ? 0.8752 1.2209 1.3806 -0.2448 -0.1680 -0.0376 44  ALA A CB  
219  N N   . CYS A 30  ? 0.9705 1.1813 1.3665 -0.2156 -0.1528 -0.0217 45  CYS A N   
220  C CA  . CYS A 30  ? 0.8751 1.0490 1.2281 -0.1889 -0.1502 -0.0205 45  CYS A CA  
221  C C   . CYS A 30  ? 0.8853 1.0092 1.2143 -0.1876 -0.1685 -0.0338 45  CYS A C   
222  O O   . CYS A 30  ? 0.8428 0.9571 1.1484 -0.1639 -0.1752 -0.0426 45  CYS A O   
223  C CB  . CYS A 30  ? 0.9508 1.1020 1.2839 -0.1888 -0.1288 -0.0021 45  CYS A CB  
224  S SG  . CYS A 30  ? 1.1483 1.3540 1.4956 -0.1756 -0.1051 0.0090  45  CYS A SG  
225  N N   . GLU A 31  ? 0.8413 0.9336 1.1774 -0.2128 -0.1766 -0.0358 46  GLU A N   
226  C CA  . GLU A 31  ? 0.8309 0.8714 1.1438 -0.2094 -0.1928 -0.0496 46  GLU A CA  
227  C C   . GLU A 31  ? 0.8460 0.9053 1.1614 -0.1989 -0.2128 -0.0732 46  GLU A C   
228  O O   . GLU A 31  ? 0.7880 0.8229 1.0750 -0.1795 -0.2200 -0.0846 46  GLU A O   
229  C CB  . GLU A 31  ? 0.8729 0.8723 1.1953 -0.2385 -0.1987 -0.0467 46  GLU A CB  
230  C CG  . GLU A 31  ? 0.9257 0.8717 1.2279 -0.2334 -0.2168 -0.0639 46  GLU A CG  
231  C CD  . GLU A 31  ? 0.9339 0.8254 1.2376 -0.2563 -0.2205 -0.0560 46  GLU A CD  
232  O OE1 . GLU A 31  ? 0.9253 0.8223 1.2460 -0.2795 -0.2090 -0.0359 46  GLU A OE1 
233  O OE2 . GLU A 31  ? 0.9438 0.7869 1.2315 -0.2504 -0.2346 -0.0695 46  GLU A OE2 
234  N N   . LYS A 32  ? 0.7306 0.8353 1.0797 -0.2115 -0.2219 -0.0810 47  LYS A N   
235  C CA  . LYS A 32  ? 0.7724 0.9010 1.1209 -0.1996 -0.2416 -0.1026 47  LYS A CA  
236  C C   . LYS A 32  ? 0.7770 0.9264 1.1012 -0.1671 -0.2357 -0.0994 47  LYS A C   
237  O O   . LYS A 32  ? 0.7963 0.9399 1.0965 -0.1501 -0.2475 -0.1137 47  LYS A O   
238  C CB  . LYS A 32  ? 0.7677 0.9467 1.1603 -0.2186 -0.2527 -0.1099 47  LYS A CB  
239  C CG  . LYS A 32  ? 0.8739 1.0342 1.2964 -0.2542 -0.2567 -0.1101 47  LYS A CG  
240  C CD  . LYS A 32  ? 0.9636 1.1755 1.4343 -0.2743 -0.2704 -0.1207 47  LYS A CD  
241  C CE  . LYS A 32  ? 0.8886 1.1630 1.3887 -0.2719 -0.2546 -0.1053 47  LYS A CE  
242  N NZ  . LYS A 32  ? 0.9490 1.2773 1.5013 -0.2917 -0.2690 -0.1166 47  LYS A NZ  
243  N N   . THR A 33  ? 0.7268 0.8997 1.0564 -0.1582 -0.2169 -0.0807 48  THR A N   
244  C CA  . THR A 33  ? 0.7440 0.9329 1.0538 -0.1283 -0.2107 -0.0753 48  THR A CA  
245  C C   . THR A 33  ? 0.7792 0.9200 1.0488 -0.1117 -0.2062 -0.0751 48  THR A C   
246  O O   . THR A 33  ? 0.6876 0.8317 0.9356 -0.0899 -0.2099 -0.0792 48  THR A O   
247  C CB  . THR A 33  ? 0.7270 0.9466 1.0543 -0.1235 -0.1916 -0.0575 48  THR A CB  
248  O OG1 . THR A 33  ? 0.7957 1.0674 1.1645 -0.1364 -0.1959 -0.0593 48  THR A OG1 
249  C CG2 . THR A 33  ? 0.7076 0.9364 1.0160 -0.0929 -0.1855 -0.0512 48  THR A CG2 
250  N N   . SER A 34  ? 0.7321 0.8292 0.9919 -0.1218 -0.1980 -0.0691 49  SER A N   
251  C CA  . SER A 34  ? 0.7091 0.7619 0.9356 -0.1069 -0.1952 -0.0704 49  SER A CA  
252  C C   . SER A 34  ? 0.7107 0.7457 0.9229 -0.1036 -0.2126 -0.0917 49  SER A C   
253  O O   . SER A 34  ? 0.7016 0.7280 0.8892 -0.0832 -0.2123 -0.0967 49  SER A O   
254  C CB  . SER A 34  ? 0.7754 0.7864 0.9963 -0.1190 -0.1858 -0.0593 49  SER A CB  
255  O OG  . SER A 34  ? 0.6692 0.6414 0.8618 -0.1029 -0.1832 -0.0602 49  SER A OG  
256  N N   . PHE A 35  ? 0.7105 0.7412 0.9390 -0.1240 -0.2273 -0.1050 50  PHE A N   
257  C CA  . PHE A 35  ? 0.7645 0.7785 0.9810 -0.1221 -0.2453 -0.1294 50  PHE A CA  
258  C C   . PHE A 35  ? 0.7317 0.7819 0.9342 -0.1025 -0.2525 -0.1396 50  PHE A C   
259  O O   . PHE A 35  ? 0.7013 0.7368 0.8764 -0.0865 -0.2558 -0.1519 50  PHE A O   
260  C CB  . PHE A 35  ? 0.6938 0.7038 0.9373 -0.1494 -0.2609 -0.1418 50  PHE A CB  
261  C CG  . PHE A 35  ? 0.7615 0.7675 0.9974 -0.1476 -0.2824 -0.1710 50  PHE A CG  
262  C CD1 . PHE A 35  ? 0.7944 0.7570 1.0061 -0.1380 -0.2873 -0.1865 50  PHE A CD1 
263  C CD2 . PHE A 35  ? 0.7288 0.7759 0.9827 -0.1549 -0.2983 -0.1848 50  PHE A CD2 
264  C CE1 . PHE A 35  ? 0.8697 0.8295 1.0730 -0.1353 -0.3064 -0.2163 50  PHE A CE1 
265  C CE2 . PHE A 35  ? 0.8044 0.8484 1.0484 -0.1527 -0.3192 -0.2142 50  PHE A CE2 
266  C CZ  . PHE A 35  ? 0.7846 0.7846 1.0022 -0.1427 -0.3226 -0.2305 50  PHE A CZ  
267  N N   . THR A 36  ? 0.7004 0.7997 0.9218 -0.1035 -0.2554 -0.1348 51  THR A N   
268  C CA  . THR A 36  ? 0.6699 0.8033 0.8765 -0.0855 -0.2652 -0.1431 51  THR A CA  
269  C C   . THR A 36  ? 0.5880 0.7226 0.7692 -0.0599 -0.2502 -0.1278 51  THR A C   
270  O O   . THR A 36  ? 0.6569 0.8031 0.8133 -0.0428 -0.2555 -0.1337 51  THR A O   
271  C CB  . THR A 36  ? 0.6644 0.8503 0.9013 -0.0931 -0.2754 -0.1425 51  THR A CB  
272  O OG1 . THR A 36  ? 0.7264 0.9318 0.9852 -0.0935 -0.2591 -0.1203 51  THR A OG1 
273  C CG2 . THR A 36  ? 0.6863 0.8713 0.9510 -0.1199 -0.2912 -0.1589 51  THR A CG2 
274  N N   . PHE A 37  ? 0.6153 0.7379 0.8013 -0.0574 -0.2317 -0.1082 52  PHE A N   
275  C CA  . PHE A 37  ? 0.6023 0.7182 0.7661 -0.0349 -0.2182 -0.0955 52  PHE A CA  
276  C C   . PHE A 37  ? 0.6201 0.6956 0.7562 -0.0277 -0.2159 -0.1049 52  PHE A C   
277  O O   . PHE A 37  ? 0.6744 0.7530 0.7872 -0.0100 -0.2137 -0.1056 52  PHE A O   
278  C CB  . PHE A 37  ? 0.5810 0.6946 0.7583 -0.0342 -0.2006 -0.0755 52  PHE A CB  
279  C CG  . PHE A 37  ? 0.6514 0.7481 0.8087 -0.0145 -0.1872 -0.0644 52  PHE A CG  
280  C CD1 . PHE A 37  ? 0.7206 0.8404 0.8701 0.0045  -0.1858 -0.0565 52  PHE A CD1 
281  C CD2 . PHE A 37  ? 0.6406 0.6977 0.7885 -0.0153 -0.1770 -0.0612 52  PHE A CD2 
282  C CE1 . PHE A 37  ? 0.6034 0.7066 0.7384 0.0206  -0.1735 -0.0459 52  PHE A CE1 
283  C CE2 . PHE A 37  ? 0.6158 0.6591 0.7496 0.0016  -0.1659 -0.0525 52  PHE A CE2 
284  C CZ  . PHE A 37  ? 0.5998 0.6658 0.7283 0.0187  -0.1635 -0.0449 52  PHE A CZ  
285  N N   . LEU A 38  ? 0.6425 0.6807 0.7819 -0.0412 -0.2166 -0.1118 53  LEU A N   
286  C CA  . LEU A 38  ? 0.6413 0.6409 0.7597 -0.0327 -0.2134 -0.1199 53  LEU A CA  
287  C C   . LEU A 38  ? 0.6468 0.6444 0.7493 -0.0292 -0.2272 -0.1446 53  LEU A C   
288  O O   . LEU A 38  ? 0.6801 0.6609 0.7622 -0.0154 -0.2229 -0.1522 53  LEU A O   
289  C CB  . LEU A 38  ? 0.7280 0.6859 0.8549 -0.0464 -0.2108 -0.1171 53  LEU A CB  
290  C CG  . LEU A 38  ? 0.7525 0.7032 0.8863 -0.0476 -0.1955 -0.0946 53  LEU A CG  
291  C CD1 . LEU A 38  ? 0.6713 0.5812 0.8106 -0.0639 -0.1971 -0.0926 53  LEU A CD1 
292  C CD2 . LEU A 38  ? 0.5655 0.5110 0.6832 -0.0265 -0.1828 -0.0859 53  LEU A CD2 
293  N N   . ARG A 39  ? 0.6794 0.6959 0.7918 -0.0410 -0.2436 -0.1590 54  ARG A N   
294  C CA  . ARG A 39  ? 0.7363 0.7520 0.8305 -0.0360 -0.2573 -0.1855 54  ARG A CA  
295  C C   . ARG A 39  ? 0.6973 0.7447 0.7644 -0.0150 -0.2542 -0.1841 54  ARG A C   
296  O O   . ARG A 39  ? 0.7763 0.8216 0.8196 -0.0055 -0.2593 -0.2037 54  ARG A O   
297  C CB  . ARG A 39  ? 0.7135 0.7396 0.8261 -0.0548 -0.2780 -0.2037 54  ARG A CB  
298  C CG  . ARG A 39  ? 0.6928 0.7684 0.8197 -0.0586 -0.2854 -0.1969 54  ARG A CG  
299  C CD  . ARG A 39  ? 0.7038 0.7887 0.8451 -0.0749 -0.3089 -0.2219 54  ARG A CD  
300  N NE  . ARG A 39  ? 0.7490 0.8829 0.9116 -0.0808 -0.3181 -0.2163 54  ARG A NE  
301  C CZ  . ARG A 39  ? 0.7666 0.9170 0.9542 -0.0992 -0.3381 -0.2331 54  ARG A CZ  
302  N NH1 . ARG A 39  ? 0.7801 0.8990 0.9740 -0.1143 -0.3515 -0.2568 54  ARG A NH1 
303  N NH2 . ARG A 39  ? 0.7352 0.9345 0.9448 -0.1023 -0.3459 -0.2267 54  ARG A NH2 
304  N N   . GLN A 40  ? 0.7193 0.7945 0.7889 -0.0071 -0.2452 -0.1610 55  GLN A N   
305  C CA  . GLN A 40  ? 0.6661 0.7643 0.7099 0.0133  -0.2387 -0.1521 55  GLN A CA  
306  C C   . GLN A 40  ? 0.6630 0.7403 0.6978 0.0257  -0.2181 -0.1360 55  GLN A C   
307  O O   . GLN A 40  ? 0.6854 0.7608 0.6952 0.0392  -0.2116 -0.1399 55  GLN A O   
308  C CB  . GLN A 40  ? 0.6800 0.8198 0.7340 0.0162  -0.2433 -0.1361 55  GLN A CB  
309  C CG  . GLN A 40  ? 0.7184 0.8772 0.7493 0.0369  -0.2348 -0.1185 55  GLN A CG  
310  C CD  . GLN A 40  ? 0.7948 0.9711 0.7911 0.0467  -0.2446 -0.1325 55  GLN A CD  
311  O OE1 . GLN A 40  ? 0.7199 0.8997 0.7119 0.0386  -0.2606 -0.1573 55  GLN A OE1 
312  N NE2 . GLN A 40  ? 0.7487 0.9357 0.7193 0.0638  -0.2350 -0.1166 55  GLN A NE2 
313  N N   . GLU A 41  ? 0.6406 0.7027 0.6957 0.0210  -0.2075 -0.1193 56  GLU A N   
314  C CA  . GLU A 41  ? 0.5964 0.6434 0.6462 0.0330  -0.1899 -0.1033 56  GLU A CA  
315  C C   . GLU A 41  ? 0.6395 0.6523 0.6792 0.0358  -0.1847 -0.1158 56  GLU A C   
316  O O   . GLU A 41  ? 0.6062 0.6145 0.6343 0.0488  -0.1726 -0.1099 56  GLU A O   
317  C CB  . GLU A 41  ? 0.5819 0.6235 0.6547 0.0275  -0.1817 -0.0854 56  GLU A CB  
318  C CG  . GLU A 41  ? 0.5890 0.6146 0.6594 0.0391  -0.1656 -0.0704 56  GLU A CG  
319  C CD  . GLU A 41  ? 0.6057 0.6539 0.6665 0.0548  -0.1596 -0.0564 56  GLU A CD  
320  O OE1 . GLU A 41  ? 0.5979 0.6764 0.6544 0.0575  -0.1682 -0.0551 56  GLU A OE1 
321  O OE2 . GLU A 41  ? 0.6088 0.6438 0.6674 0.0643  -0.1472 -0.0460 56  GLU A OE2 
322  N N   . LEU A 42  ? 0.6097 0.5974 0.6568 0.0238  -0.1936 -0.1322 57  LEU A N   
323  C CA  . LEU A 42  ? 0.6132 0.5683 0.6535 0.0289  -0.1898 -0.1444 57  LEU A CA  
324  C C   . LEU A 42  ? 0.6204 0.5886 0.6373 0.0417  -0.1901 -0.1615 57  LEU A C   
325  O O   . LEU A 42  ? 0.6728 0.6332 0.6816 0.0539  -0.1783 -0.1617 57  LEU A O   
326  C CB  . LEU A 42  ? 0.7277 0.6487 0.7815 0.0140  -0.2007 -0.1570 57  LEU A CB  
327  C CG  . LEU A 42  ? 0.6951 0.5958 0.7664 0.0034  -0.1960 -0.1386 57  LEU A CG  
328  C CD1 . LEU A 42  ? 0.7449 0.6152 0.8287 -0.0145 -0.2087 -0.1481 57  LEU A CD1 
329  C CD2 . LEU A 42  ? 0.7287 0.6093 0.7971 0.0151  -0.1830 -0.1279 57  LEU A CD2 
330  N N   . PRO A 43  ? 0.6543 0.6448 0.6598 0.0397  -0.2027 -0.1766 58  PRO A N   
331  C CA  . PRO A 43  ? 0.6355 0.6441 0.6128 0.0538  -0.2003 -0.1906 58  PRO A CA  
332  C C   . PRO A 43  ? 0.6544 0.6859 0.6172 0.0676  -0.1838 -0.1684 58  PRO A C   
333  O O   . PRO A 43  ? 0.6821 0.7171 0.6272 0.0795  -0.1729 -0.1741 58  PRO A O   
334  C CB  . PRO A 43  ? 0.6446 0.6770 0.6130 0.0478  -0.2191 -0.2069 58  PRO A CB  
335  C CG  . PRO A 43  ? 0.7166 0.7269 0.7127 0.0289  -0.2324 -0.2138 58  PRO A CG  
336  C CD  . PRO A 43  ? 0.6493 0.6463 0.6669 0.0239  -0.2207 -0.1867 58  PRO A CD  
337  N N   . VAL A 44  ? 0.6260 0.6734 0.5976 0.0664  -0.1812 -0.1433 59  VAL A N   
338  C CA  . VAL A 44  ? 0.6423 0.7058 0.6033 0.0789  -0.1663 -0.1201 59  VAL A CA  
339  C C   . VAL A 44  ? 0.6142 0.6533 0.5842 0.0839  -0.1494 -0.1135 59  VAL A C   
340  O O   . VAL A 44  ? 0.5667 0.6130 0.5225 0.0942  -0.1364 -0.1099 59  VAL A O   
341  C CB  . VAL A 44  ? 0.5532 0.6344 0.5271 0.0774  -0.1688 -0.0964 59  VAL A CB  
342  C CG1 . VAL A 44  ? 0.5430 0.6293 0.5138 0.0891  -0.1531 -0.0705 59  VAL A CG1 
343  C CG2 . VAL A 44  ? 0.5750 0.6885 0.5368 0.0767  -0.1853 -0.1016 59  VAL A CG2 
344  N N   . ARG A 45  ? 0.5806 0.5918 0.5743 0.0761  -0.1495 -0.1120 60  ARG A N   
345  C CA  . ARG A 45  ? 0.5506 0.5398 0.5545 0.0812  -0.1362 -0.1062 60  ARG A CA  
346  C C   . ARG A 45  ? 0.5353 0.5135 0.5314 0.0869  -0.1333 -0.1280 60  ARG A C   
347  O O   . ARG A 45  ? 0.5965 0.5752 0.5926 0.0959  -0.1194 -0.1240 60  ARG A O   
348  C CB  . ARG A 45  ? 0.5197 0.4825 0.5461 0.0724  -0.1386 -0.1000 60  ARG A CB  
349  C CG  . ARG A 45  ? 0.5806 0.5572 0.6169 0.0696  -0.1376 -0.0789 60  ARG A CG  
350  C CD  . ARG A 45  ? 0.5295 0.4835 0.5844 0.0629  -0.1362 -0.0710 60  ARG A CD  
351  N NE  . ARG A 45  ? 0.5316 0.5040 0.5961 0.0616  -0.1350 -0.0545 60  ARG A NE  
352  C CZ  . ARG A 45  ? 0.5385 0.5006 0.6167 0.0590  -0.1306 -0.0442 60  ARG A CZ  
353  N NH1 . ARG A 45  ? 0.4904 0.4234 0.5721 0.0572  -0.1278 -0.0465 60  ARG A NH1 
354  N NH2 . ARG A 45  ? 0.5212 0.5040 0.6094 0.0592  -0.1297 -0.0322 60  ARG A NH2 
355  N N   . LEU A 46  ? 0.5593 0.5287 0.5510 0.0820  -0.1464 -0.1523 61  LEU A N   
356  C CA  . LEU A 46  ? 0.6331 0.5924 0.6188 0.0893  -0.1449 -0.1767 61  LEU A CA  
357  C C   . LEU A 46  ? 0.6834 0.6746 0.6447 0.1013  -0.1337 -0.1803 61  LEU A C   
358  O O   . LEU A 46  ? 0.6395 0.6313 0.6009 0.1110  -0.1207 -0.1866 61  LEU A O   
359  C CB  . LEU A 46  ? 0.6367 0.5794 0.6230 0.0815  -0.1635 -0.2028 61  LEU A CB  
360  C CG  . LEU A 46  ? 0.7665 0.6701 0.7761 0.0704  -0.1730 -0.2025 61  LEU A CG  
361  C CD1 . LEU A 46  ? 0.7231 0.6124 0.7341 0.0600  -0.1922 -0.2254 61  LEU A CD1 
362  C CD2 . LEU A 46  ? 0.6421 0.5202 0.6632 0.0794  -0.1656 -0.2069 61  LEU A CD2 
363  N N   . ALA A 47  ? 0.6140 0.6340 0.5540 0.1009  -0.1386 -0.1764 62  ALA A N   
364  C CA  . ALA A 47  ? 0.6718 0.7234 0.5818 0.1119  -0.1289 -0.1790 62  ALA A CA  
365  C C   . ALA A 47  ? 0.6182 0.6812 0.5289 0.1186  -0.1080 -0.1516 62  ALA A C   
366  O O   . ALA A 47  ? 0.6509 0.7295 0.5475 0.1275  -0.0927 -0.1552 62  ALA A O   
367  C CB  . ALA A 47  ? 0.6560 0.7351 0.5419 0.1101  -0.1421 -0.1791 62  ALA A CB  
368  N N   . ASN A 48  ? 0.5897 0.6464 0.5174 0.1141  -0.1065 -0.1247 63  ASN A N   
369  C CA  . ASN A 48  ? 0.6628 0.7270 0.5941 0.1194  -0.0884 -0.0984 63  ASN A CA  
370  C C   . ASN A 48  ? 0.6335 0.6837 0.5822 0.1231  -0.0740 -0.1053 63  ASN A C   
371  O O   . ASN A 48  ? 0.6598 0.7263 0.6020 0.1292  -0.0566 -0.0972 63  ASN A O   
372  C CB  . ASN A 48  ? 0.6271 0.6831 0.5776 0.1148  -0.0915 -0.0729 63  ASN A CB  
373  C CG  . ASN A 48  ? 0.6924 0.7738 0.6247 0.1170  -0.0971 -0.0543 63  ASN A CG  
374  O OD1 . ASN A 48  ? 0.5803 0.6711 0.5093 0.1221  -0.0868 -0.0295 63  ASN A OD1 
375  N ND2 . ASN A 48  ? 0.5994 0.6911 0.5224 0.1129  -0.1147 -0.0662 63  ASN A ND2 
376  N N   . ILE A 49  ? 0.5697 0.5911 0.5413 0.1193  -0.0813 -0.1199 64  ILE A N   
377  C CA  . ILE A 49  ? 0.6000 0.6096 0.5908 0.1242  -0.0702 -0.1277 64  ILE A CA  
378  C C   . ILE A 49  ? 0.6336 0.6572 0.6105 0.1323  -0.0649 -0.1541 64  ILE A C   
379  O O   . ILE A 49  ? 0.6334 0.6667 0.6191 0.1391  -0.0487 -0.1564 64  ILE A O   
380  C CB  . ILE A 49  ? 0.5805 0.5541 0.5980 0.1193  -0.0808 -0.1333 64  ILE A CB  
381  C CG1 . ILE A 49  ? 0.6345 0.5990 0.6754 0.1254  -0.0701 -0.1367 64  ILE A CG1 
382  C CG2 . ILE A 49  ? 0.5524 0.5079 0.5664 0.1158  -0.0980 -0.1585 64  ILE A CG2 
383  C CD1 . ILE A 49  ? 0.6262 0.6038 0.6775 0.1266  -0.0539 -0.1119 64  ILE A CD1 
384  N N   . MET A 50  ? 0.6162 0.6433 0.5731 0.1321  -0.0778 -0.1757 65  MET A N   
385  C CA  . MET A 50  ? 0.6326 0.6746 0.5748 0.1416  -0.0724 -0.2038 65  MET A CA  
386  C C   . MET A 50  ? 0.6665 0.7474 0.5842 0.1485  -0.0522 -0.1923 65  MET A C   
387  O O   . MET A 50  ? 0.6649 0.7611 0.5830 0.1571  -0.0364 -0.2052 65  MET A O   
388  C CB  . MET A 50  ? 0.6888 0.7258 0.6141 0.1396  -0.0921 -0.2306 65  MET A CB  
389  C CG  . MET A 50  ? 0.8776 0.8737 0.8290 0.1335  -0.1093 -0.2448 65  MET A CG  
390  S SD  . MET A 50  ? 1.0429 1.0283 0.9823 0.1238  -0.1356 -0.2656 65  MET A SD  
391  C CE  . MET A 50  ? 0.9397 0.9338 0.8631 0.1374  -0.1353 -0.3076 65  MET A CE  
392  N N   . LYS A 51  ? 0.6820 0.7802 0.5796 0.1449  -0.0518 -0.1669 66  LYS A N   
393  C CA  . LYS A 51  ? 0.7423 0.8751 0.6142 0.1503  -0.0326 -0.1503 66  LYS A CA  
394  C C   . LYS A 51  ? 0.8146 0.9480 0.7120 0.1511  -0.0106 -0.1319 66  LYS A C   
395  O O   . LYS A 51  ? 0.6917 0.8518 0.5776 0.1565  0.0102  -0.1300 66  LYS A O   
396  C CB  . LYS A 51  ? 0.8073 0.9532 0.6565 0.1469  -0.0395 -0.1231 66  LYS A CB  
397  C CG  . LYS A 51  ? 0.7962 0.9576 0.6109 0.1481  -0.0572 -0.1399 66  LYS A CG  
398  C CD  . LYS A 51  ? 0.9704 1.1642 0.7460 0.1575  -0.0461 -0.1548 66  LYS A CD  
399  C CE  . LYS A 51  ? 0.9926 1.2122 0.7476 0.1608  -0.0250 -0.1212 66  LYS A CE  
400  N NZ  . LYS A 51  ? 1.0335 1.2894 0.7398 0.1694  -0.0167 -0.1330 66  LYS A NZ  
401  N N   . GLU A 52  ? 0.6308 0.7366 0.5633 0.1452  -0.0147 -0.1184 67  GLU A N   
402  C CA  . GLU A 52  ? 0.7350 0.8390 0.6964 0.1446  0.0030  -0.1019 67  GLU A CA  
403  C C   . GLU A 52  ? 0.7359 0.8411 0.7181 0.1508  0.0121  -0.1275 67  GLU A C   
404  O O   . GLU A 52  ? 0.7339 0.8588 0.7272 0.1530  0.0334  -0.1207 67  GLU A O   
405  C CB  . GLU A 52  ? 0.6564 0.7306 0.6465 0.1377  -0.0067 -0.0844 67  GLU A CB  
406  C CG  . GLU A 52  ? 0.7740 0.8446 0.7957 0.1362  0.0083  -0.0673 67  GLU A CG  
407  C CD  . GLU A 52  ? 0.7711 0.8263 0.8052 0.1305  0.0041  -0.0391 67  GLU A CD  
408  O OE1 . GLU A 52  ? 0.8100 0.8598 0.8290 0.1284  -0.0096 -0.0319 67  GLU A OE1 
409  O OE2 . GLU A 52  ? 0.7327 0.7827 0.7941 0.1284  0.0144  -0.0256 67  GLU A OE2 
410  N N   . ILE A 53  ? 0.6949 0.7796 0.6848 0.1534  -0.0037 -0.1567 68  ILE A N   
411  C CA  . ILE A 53  ? 0.6237 0.7111 0.6309 0.1623  0.0024  -0.1853 68  ILE A CA  
412  C C   . ILE A 53  ? 0.7336 0.8621 0.7160 0.1702  0.0223  -0.1953 68  ILE A C   
413  O O   . ILE A 53  ? 0.7584 0.9050 0.7597 0.1766  0.0401  -0.2044 68  ILE A O   
414  C CB  . ILE A 53  ? 0.6151 0.6726 0.6261 0.1644  -0.0205 -0.2149 68  ILE A CB  
415  C CG1 . ILE A 53  ? 0.6579 0.6761 0.6950 0.1568  -0.0368 -0.2040 68  ILE A CG1 
416  C CG2 . ILE A 53  ? 0.7054 0.7689 0.7289 0.1769  -0.0156 -0.2488 68  ILE A CG2 
417  C CD1 . ILE A 53  ? 0.6744 0.6615 0.7097 0.1547  -0.0601 -0.2245 68  ILE A CD1 
418  N N   . ASN A 54  ? 0.7569 0.9036 0.6966 0.1702  0.0197  -0.1940 69  ASN A N   
419  C CA  . ASN A 54  ? 0.7576 0.9448 0.6658 0.1783  0.0377  -0.2047 69  ASN A CA  
420  C C   . ASN A 54  ? 0.7583 0.9753 0.6649 0.1760  0.0655  -0.1738 69  ASN A C   
421  O O   . ASN A 54  ? 0.8164 1.0703 0.6991 0.1822  0.0852  -0.1804 69  ASN A O   
422  C CB  . ASN A 54  ? 0.8730 1.0715 0.7333 0.1790  0.0245  -0.2116 69  ASN A CB  
423  C CG  . ASN A 54  ? 1.0094 1.2033 0.8599 0.1872  0.0110  -0.2559 69  ASN A CG  
424  O OD1 . ASN A 54  ? 0.9933 1.1729 0.8734 0.1932  0.0107  -0.2811 69  ASN A OD1 
425  N ND2 . ASN A 54  ? 1.2138 1.4190 1.0238 0.1881  -0.0021 -0.2669 69  ASN A ND2 
426  N N   . LEU A 55  ? 0.7408 0.9432 0.6711 0.1668  0.0678  -0.1406 70  LEU A N   
427  C CA  . LEU A 55  ? 0.7869 1.0119 0.7246 0.1627  0.0937  -0.1109 70  LEU A CA  
428  C C   . LEU A 55  ? 0.7848 1.0155 0.7687 0.1642  0.1102  -0.1204 70  LEU A C   
429  O O   . LEU A 55  ? 0.7418 0.9955 0.7366 0.1599  0.1342  -0.0990 70  LEU A O   
430  C CB  . LEU A 55  ? 0.8966 1.1018 0.8422 0.1527  0.0878  -0.0723 70  LEU A CB  
431  C CG  . LEU A 55  ? 0.8827 1.0839 0.7905 0.1509  0.0717  -0.0558 70  LEU A CG  
432  C CD1 . LEU A 55  ? 0.9743 1.1515 0.9034 0.1431  0.0656  -0.0228 70  LEU A CD1 
433  C CD2 . LEU A 55  ? 0.9173 1.1551 0.7767 0.1544  0.0854  -0.0446 70  LEU A CD2 
434  N N   . LEU A 56  ? 0.8924 0.9905 0.6920 0.1910  0.0341  -0.0563 71  LEU A N   
435  C CA  . LEU A 56  ? 0.7670 0.8633 0.5831 0.1863  0.0408  -0.0562 71  LEU A CA  
436  C C   . LEU A 56  ? 0.7292 0.8599 0.5338 0.2067  0.0483  -0.0606 71  LEU A C   
437  O O   . LEU A 56  ? 0.7724 0.9208 0.5588 0.2223  0.0386  -0.0773 71  LEU A O   
438  C CB  . LEU A 56  ? 0.6682 0.7410 0.4996 0.1747  0.0236  -0.0751 71  LEU A CB  
439  C CG  . LEU A 56  ? 0.7159 0.7579 0.5586 0.1547  0.0166  -0.0708 71  LEU A CG  
440  C CD1 . LEU A 56  ? 0.5877 0.6103 0.4416 0.1470  -0.0011 -0.0880 71  LEU A CD1 
441  C CD2 . LEU A 56  ? 0.7292 0.7633 0.5866 0.1418  0.0315  -0.0522 71  LEU A CD2 
442  N N   . PRO A 57  ? 0.7855 0.9283 0.6015 0.2068  0.0649  -0.0477 72  PRO A N   
443  C CA  . PRO A 57  ? 0.7827 0.9619 0.5888 0.2269  0.0733  -0.0517 72  PRO A CA  
444  C C   . PRO A 57  ? 0.8114 0.9921 0.6161 0.2358  0.0555  -0.0830 72  PRO A C   
445  O O   . PRO A 57  ? 0.7583 0.9101 0.5771 0.2236  0.0399  -0.0971 72  PRO A O   
446  C CB  . PRO A 57  ? 0.8163 1.0023 0.6447 0.2188  0.0926  -0.0331 72  PRO A CB  
447  C CG  . PRO A 57  ? 0.8608 1.0147 0.7080 0.1952  0.0956  -0.0182 72  PRO A CG  
448  C CD  . PRO A 57  ? 0.7612 0.8864 0.6026 0.1874  0.0752  -0.0324 72  PRO A CD  
449  N N   . ASP A 58  ? 0.8101 1.0255 0.5977 0.2584  0.0590  -0.0932 73  ASP A N   
450  C CA  . ASP A 58  ? 0.7251 0.9436 0.5105 0.2704  0.0433  -0.1255 73  ASP A CA  
451  C C   . ASP A 58  ? 0.6774 0.8788 0.4899 0.2620  0.0399  -0.1325 73  ASP A C   
452  O O   . ASP A 58  ? 0.7317 0.9150 0.5504 0.2638  0.0225  -0.1570 73  ASP A O   
453  C CB  . ASP A 58  ? 0.7992 1.0640 0.5622 0.2977  0.0517  -0.1337 73  ASP A CB  
454  C CG  . ASP A 58  ? 0.9645 1.2511 0.6973 0.3105  0.0499  -0.1337 73  ASP A CG  
455  O OD1 . ASP A 58  ? 1.0952 1.3606 0.8263 0.2982  0.0421  -0.1273 73  ASP A OD1 
456  O OD2 . ASP A 58  ? 1.1642 1.4883 0.8808 0.3290  0.0536  -0.1370 73  ASP A OD2 
457  N N   . ARG A 59  ? 0.7411 0.9492 0.5715 0.2535  0.0561  -0.1114 74  ARG A N   
458  C CA  . ARG A 59  ? 0.6945 0.8937 0.5509 0.2475  0.0526  -0.1177 74  ARG A CA  
459  C C   . ARG A 59  ? 0.6315 0.7890 0.5042 0.2262  0.0375  -0.1190 74  ARG A C   
460  O O   . ARG A 59  ? 0.6391 0.7861 0.5306 0.2232  0.0294  -0.1273 74  ARG A O   
461  C CB  . ARG A 59  ? 0.6645 0.8896 0.5379 0.2443  0.0742  -0.0963 74  ARG A CB  
462  C CG  . ARG A 59  ? 0.6339 0.8446 0.5191 0.2218  0.0851  -0.0701 74  ARG A CG  
463  C CD  . ARG A 59  ? 0.6790 0.9179 0.5837 0.2184  0.1081  -0.0496 74  ARG A CD  
464  N NE  . ARG A 59  ? 0.6930 0.9157 0.6133 0.1962  0.1189  -0.0271 74  ARG A NE  
465  C CZ  . ARG A 59  ? 0.7471 0.9671 0.6552 0.1947  0.1314  -0.0075 74  ARG A CZ  
466  N NH1 . ARG A 59  ? 0.7993 1.0348 0.6777 0.2140  0.1337  -0.0063 74  ARG A NH1 
467  N NH2 . ARG A 59  ? 0.7434 0.9459 0.6703 0.1744  0.1415  0.0106  74  ARG A NH2 
468  N N   . VAL A 60  ? 0.6188 0.7554 0.4843 0.2128  0.0342  -0.1098 75  VAL A N   
469  C CA  . VAL A 60  ? 0.6868 0.7865 0.5618 0.1954  0.0186  -0.1134 75  VAL A CA  
470  C C   . VAL A 60  ? 0.6944 0.7792 0.5565 0.2012  0.0007  -0.1338 75  VAL A C   
471  O O   . VAL A 60  ? 0.6426 0.7040 0.5155 0.1973  -0.0146 -0.1472 75  VAL A O   
472  C CB  . VAL A 60  ? 0.6350 0.7219 0.5126 0.1771  0.0267  -0.0919 75  VAL A CB  
473  C CG1 . VAL A 60  ? 0.6245 0.6775 0.5103 0.1598  0.0118  -0.0949 75  VAL A CG1 
474  C CG2 . VAL A 60  ? 0.6532 0.7536 0.5479 0.1694  0.0445  -0.0741 75  VAL A CG2 
475  N N   . LEU A 61  ? 0.7280 0.8281 0.5685 0.2109  0.0026  -0.1357 76  LEU A N   
476  C CA  . LEU A 61  ? 0.7726 0.8629 0.6022 0.2143  -0.0144 -0.1556 76  LEU A CA  
477  C C   . LEU A 61  ? 0.7928 0.8773 0.6281 0.2252  -0.0281 -0.1838 76  LEU A C   
478  O O   . LEU A 61  ? 0.8276 0.8852 0.6708 0.2181  -0.0448 -0.1986 76  LEU A O   
479  C CB  . LEU A 61  ? 0.8273 0.9469 0.6314 0.2279  -0.0087 -0.1538 76  LEU A CB  
480  C CG  . LEU A 61  ? 0.8805 0.9962 0.6737 0.2288  -0.0252 -0.1712 76  LEU A CG  
481  C CD1 . LEU A 61  ? 0.8250 0.9055 0.6333 0.2063  -0.0344 -0.1647 76  LEU A CD1 
482  C CD2 . LEU A 61  ? 0.9383 1.0874 0.7064 0.2417  -0.0171 -0.1616 76  LEU A CD2 
483  N N   . SER A 62  ? 0.6053 0.7140 0.4387 0.2427  -0.0205 -0.1911 77  SER A N   
484  C CA  . SER A 62  ? 0.7882 0.8939 0.6257 0.2573  -0.0319 -0.2202 77  SER A CA  
485  C C   . SER A 62  ? 0.8206 0.8966 0.6844 0.2500  -0.0395 -0.2225 77  SER A C   
486  O O   . SER A 62  ? 0.8403 0.9075 0.7112 0.2621  -0.0494 -0.2459 77  SER A O   
487  C CB  . SER A 62  ? 0.8181 0.9655 0.6425 0.2814  -0.0197 -0.2275 77  SER A CB  
488  O OG  . SER A 62  ? 0.8121 0.9739 0.6492 0.2803  -0.0035 -0.2073 77  SER A OG  
489  N N   . THR A 63  ? 0.7526 0.8140 0.6311 0.2322  -0.0355 -0.1999 78  THR A N   
490  C CA  . THR A 63  ? 0.7202 0.7596 0.6221 0.2277  -0.0427 -0.2000 78  THR A CA  
491  C C   . THR A 63  ? 0.7267 0.7270 0.6369 0.2202  -0.0615 -0.2126 78  THR A C   
492  O O   . THR A 63  ? 0.7221 0.7114 0.6232 0.2113  -0.0679 -0.2155 78  THR A O   
493  C CB  . THR A 63  ? 0.7290 0.7683 0.6429 0.2107  -0.0340 -0.1741 78  THR A CB  
494  O OG1 . THR A 63  ? 0.6840 0.7077 0.5915 0.1924  -0.0355 -0.1616 78  THR A OG1 
495  C CG2 . THR A 63  ? 0.7208 0.7974 0.6333 0.2167  -0.0147 -0.1618 78  THR A CG2 
496  N N   . PRO A 64  ? 0.7793 0.7587 0.7085 0.2240  -0.0702 -0.2193 79  PRO A N   
497  C CA  . PRO A 64  ? 0.7304 0.6710 0.6701 0.2176  -0.0868 -0.2306 79  PRO A CA  
498  C C   . PRO A 64  ? 0.7513 0.6701 0.6939 0.1937  -0.0911 -0.2121 79  PRO A C   
499  O O   . PRO A 64  ? 0.6081 0.5043 0.5531 0.1858  -0.1018 -0.2209 79  PRO A O   
500  C CB  . PRO A 64  ? 0.7258 0.6512 0.6866 0.2281  -0.0918 -0.2345 79  PRO A CB  
501  C CG  . PRO A 64  ? 0.7866 0.7487 0.7436 0.2469  -0.0798 -0.2382 79  PRO A CG  
502  C CD  . PRO A 64  ? 0.7135 0.7055 0.6566 0.2371  -0.0655 -0.2189 79  PRO A CD  
503  N N   . SER A 65  ? 0.6718 0.5984 0.6157 0.1818  -0.0829 -0.1881 80  SER A N   
504  C CA  . SER A 65  ? 0.6642 0.5727 0.6099 0.1609  -0.0863 -0.1719 80  SER A CA  
505  C C   . SER A 65  ? 0.7176 0.6316 0.6474 0.1535  -0.0849 -0.1733 80  SER A C   
506  O O   . SER A 65  ? 0.6652 0.5595 0.5980 0.1419  -0.0936 -0.1739 80  SER A O   
507  C CB  . SER A 65  ? 0.6702 0.5900 0.6200 0.1517  -0.0777 -0.1502 80  SER A CB  
508  O OG  . SER A 65  ? 0.6196 0.5697 0.5597 0.1566  -0.0635 -0.1469 80  SER A OG  
509  N N   . VAL A 66  ? 0.6037 0.5463 0.5176 0.1605  -0.0733 -0.1721 81  VAL A N   
510  C CA  . VAL A 66  ? 0.6526 0.6041 0.5508 0.1559  -0.0711 -0.1705 81  VAL A CA  
511  C C   . VAL A 66  ? 0.7663 0.7129 0.6609 0.1622  -0.0838 -0.1941 81  VAL A C   
512  O O   . VAL A 66  ? 0.6592 0.6001 0.5511 0.1525  -0.0899 -0.1949 81  VAL A O   
513  C CB  . VAL A 66  ? 0.7308 0.7142 0.6137 0.1642  -0.0545 -0.1609 81  VAL A CB  
514  C CG1 . VAL A 66  ? 0.7053 0.7013 0.5705 0.1643  -0.0523 -0.1589 81  VAL A CG1 
515  C CG2 . VAL A 66  ? 0.6486 0.6335 0.5402 0.1533  -0.0428 -0.1389 81  VAL A CG2 
516  N N   . GLN A 67  ? 0.7274 0.6767 0.6243 0.1783  -0.0885 -0.2153 82  GLN A N   
517  C CA  . GLN A 67  ? 0.7302 0.6756 0.6256 0.1847  -0.1014 -0.2428 82  GLN A CA  
518  C C   . GLN A 67  ? 0.7375 0.6455 0.6540 0.1691  -0.1157 -0.2469 82  GLN A C   
519  O O   . GLN A 67  ? 0.7342 0.6382 0.6518 0.1632  -0.1257 -0.2609 82  GLN A O   
520  C CB  . GLN A 67  ? 0.7568 0.7135 0.6505 0.2069  -0.1023 -0.2666 82  GLN A CB  
521  C CG  . GLN A 67  ? 0.8445 0.8452 0.7143 0.2246  -0.0890 -0.2669 82  GLN A CG  
522  C CD  . GLN A 67  ? 1.0138 1.0382 0.8624 0.2261  -0.0903 -0.2719 82  GLN A CD  
523  O OE1 . GLN A 67  ? 1.0815 1.1025 0.9297 0.2278  -0.1044 -0.2970 82  GLN A OE1 
524  N NE2 . GLN A 67  ? 0.8554 0.9043 0.6882 0.2256  -0.0758 -0.2481 82  GLN A NE2 
525  N N   . LEU A 68  ? 0.6594 0.5421 0.5936 0.1619  -0.1165 -0.2335 83  LEU A N   
526  C CA  . LEU A 68  ? 0.7791 0.6265 0.7340 0.1469  -0.1279 -0.2322 83  LEU A CA  
527  C C   . LEU A 68  ? 0.7417 0.5894 0.6935 0.1273  -0.1271 -0.2151 83  LEU A C   
528  O O   . LEU A 68  ? 0.7254 0.5579 0.6886 0.1159  -0.1368 -0.2220 83  LEU A O   
529  C CB  . LEU A 68  ? 0.7489 0.5738 0.7210 0.1467  -0.1280 -0.2184 83  LEU A CB  
530  C CG  . LEU A 68  ? 0.8429 0.6320 0.8365 0.1311  -0.1368 -0.2083 83  LEU A CG  
531  C CD1 . LEU A 68  ? 0.7925 0.5562 0.8032 0.1325  -0.1494 -0.2337 83  LEU A CD1 
532  C CD2 . LEU A 68  ? 0.8132 0.5894 0.8185 0.1339  -0.1350 -0.1895 83  LEU A CD2 
533  N N   . VAL A 69  ? 0.7446 0.6100 0.6835 0.1231  -0.1154 -0.1937 84  VAL A N   
534  C CA  . VAL A 69  ? 0.7454 0.6135 0.6803 0.1072  -0.1134 -0.1788 84  VAL A CA  
535  C C   . VAL A 69  ? 0.6879 0.5739 0.6122 0.1095  -0.1171 -0.1933 84  VAL A C   
536  O O   . VAL A 69  ? 0.6539 0.5340 0.5858 0.0970  -0.1240 -0.1939 84  VAL A O   
537  C CB  . VAL A 69  ? 0.7360 0.6181 0.6602 0.1038  -0.0995 -0.1561 84  VAL A CB  
538  C CG1 . VAL A 69  ? 0.7180 0.6061 0.6356 0.0914  -0.0964 -0.1442 84  VAL A CG1 
539  C CG2 . VAL A 69  ? 0.6340 0.5011 0.5704 0.0985  -0.0987 -0.1418 84  VAL A CG2 
540  N N   . GLN A 70  ? 0.6248 0.5371 0.5319 0.1261  -0.1124 -0.2044 85  GLN A N   
541  C CA  . GLN A 70  ? 0.6953 0.6293 0.5910 0.1316  -0.1178 -0.2205 85  GLN A CA  
542  C C   . GLN A 70  ? 0.8263 0.7442 0.7394 0.1265  -0.1349 -0.2456 85  GLN A C   
543  O O   . GLN A 70  ? 0.8259 0.7522 0.7412 0.1185  -0.1423 -0.2520 85  GLN A O   
544  C CB  . GLN A 70  ? 0.8557 0.8210 0.7303 0.1533  -0.1108 -0.2302 85  GLN A CB  
545  C CG  . GLN A 70  ? 0.8475 0.8371 0.7034 0.1578  -0.0942 -0.2070 85  GLN A CG  
546  C CD  . GLN A 70  ? 1.0272 1.0499 0.8630 0.1798  -0.0863 -0.2145 85  GLN A CD  
547  O OE1 . GLN A 70  ? 1.1017 1.1261 0.9390 0.1919  -0.0892 -0.2324 85  GLN A OE1 
548  N NE2 . GLN A 70  ? 1.0124 1.0625 0.8292 0.1865  -0.0757 -0.2000 85  GLN A NE2 
549  N N   . SER A 71  ? 0.7361 0.6313 0.6640 0.1311  -0.1414 -0.2607 86  SER A N   
550  C CA  . SER A 71  ? 0.7957 0.6721 0.7437 0.1257  -0.1573 -0.2866 86  SER A CA  
551  C C   . SER A 71  ? 0.7893 0.6425 0.7590 0.1021  -0.1626 -0.2730 86  SER A C   
552  O O   . SER A 71  ? 0.8099 0.6598 0.7942 0.0926  -0.1742 -0.2903 86  SER A O   
553  C CB  . SER A 71  ? 0.8145 0.6656 0.7771 0.1361  -0.1620 -0.3034 86  SER A CB  
554  O OG  . SER A 71  ? 0.8526 0.6718 0.8326 0.1267  -0.1591 -0.2807 86  SER A OG  
555  N N   . TRP A 72  ? 0.7074 0.5479 0.6799 0.0922  -0.1540 -0.2429 87  TRP A N   
556  C CA  . TRP A 72  ? 0.7961 0.6200 0.7864 0.0708  -0.1568 -0.2269 87  TRP A CA  
557  C C   . TRP A 72  ? 0.7857 0.6374 0.7662 0.0636  -0.1557 -0.2233 87  TRP A C   
558  O O   . TRP A 72  ? 0.7421 0.5916 0.7396 0.0503  -0.1645 -0.2307 87  TRP A O   
559  C CB  . TRP A 72  ? 0.6760 0.4854 0.6678 0.0646  -0.1477 -0.1968 87  TRP A CB  
560  C CG  . TRP A 72  ? 0.7539 0.5356 0.7597 0.0699  -0.1498 -0.1956 87  TRP A CG  
561  C CD1 . TRP A 72  ? 0.8730 0.6314 0.8972 0.0753  -0.1596 -0.2164 87  TRP A CD1 
562  C CD2 . TRP A 72  ? 0.7850 0.5601 0.7889 0.0715  -0.1424 -0.1726 87  TRP A CD2 
563  N NE1 . TRP A 72  ? 0.8669 0.6034 0.9007 0.0815  -0.1579 -0.2054 87  TRP A NE1 
564  C CE2 . TRP A 72  ? 0.8910 0.6399 0.9120 0.0793  -0.1480 -0.1786 87  TRP A CE2 
565  C CE3 . TRP A 72  ? 0.8538 0.6438 0.8440 0.0677  -0.1321 -0.1493 87  TRP A CE3 
566  C CZ2 . TRP A 72  ? 0.9279 0.6686 0.9519 0.0842  -0.1440 -0.1601 87  TRP A CZ2 
567  C CZ3 . TRP A 72  ? 0.8444 0.6268 0.8379 0.0708  -0.1288 -0.1337 87  TRP A CZ3 
568  C CH2 . TRP A 72  ? 0.8482 0.6080 0.8579 0.0795  -0.1350 -0.1382 87  TRP A CH2 
569  N N   . TYR A 73  ? 0.6595 0.5377 0.6149 0.0723  -0.1446 -0.2113 88  TYR A N   
570  C CA  . TYR A 73  ? 0.6959 0.6003 0.6419 0.0682  -0.1426 -0.2054 88  TYR A CA  
571  C C   . TYR A 73  ? 0.7797 0.7044 0.7273 0.0723  -0.1549 -0.2326 88  TYR A C   
572  O O   . TYR A 73  ? 0.6908 0.6275 0.6473 0.0616  -0.1604 -0.2334 88  TYR A O   
573  C CB  . TYR A 73  ? 0.6800 0.6061 0.6004 0.0793  -0.1278 -0.1887 88  TYR A CB  
574  C CG  . TYR A 73  ? 0.6714 0.5837 0.5930 0.0697  -0.1169 -0.1618 88  TYR A CG  
575  C CD1 . TYR A 73  ? 0.7043 0.5887 0.6429 0.0587  -0.1195 -0.1544 88  TYR A CD1 
576  C CD2 . TYR A 73  ? 0.7723 0.7000 0.6785 0.0719  -0.1043 -0.1443 88  TYR A CD2 
577  C CE1 . TYR A 73  ? 0.6688 0.5456 0.6066 0.0507  -0.1106 -0.1317 88  TYR A CE1 
578  C CE2 . TYR A 73  ? 0.7915 0.7079 0.6993 0.0628  -0.0952 -0.1239 88  TYR A CE2 
579  C CZ  . TYR A 73  ? 0.6970 0.5902 0.6195 0.0523  -0.0990 -0.1186 88  TYR A CZ  
580  O OH  . TYR A 73  ? 0.7757 0.6628 0.6976 0.0445  -0.0910 -0.1004 88  TYR A OH  
581  N N   . VAL A 74  ? 0.7642 0.6954 0.7044 0.0879  -0.1599 -0.2568 89  VAL A N   
582  C CA  . VAL A 74  ? 0.7507 0.7048 0.6911 0.0933  -0.1731 -0.2873 89  VAL A CA  
583  C C   . VAL A 74  ? 0.8197 0.7531 0.7936 0.0737  -0.1875 -0.3019 89  VAL A C   
584  O O   . VAL A 74  ? 0.7682 0.7237 0.7493 0.0670  -0.1969 -0.3143 89  VAL A O   
585  C CB  . VAL A 74  ? 0.8015 0.7638 0.7290 0.1142  -0.1757 -0.3125 89  VAL A CB  
586  C CG1 . VAL A 74  ? 0.8674 0.8467 0.8032 0.1163  -0.1911 -0.3470 89  VAL A CG1 
587  C CG2 . VAL A 74  ? 0.7953 0.7889 0.6898 0.1337  -0.1617 -0.2995 89  VAL A CG2 
588  N N   . GLN A 75  ? 0.8011 0.6930 0.7981 0.0643  -0.1893 -0.2998 90  GLN A N   
589  C CA  . GLN A 75  ? 0.8692 0.7364 0.9022 0.0451  -0.2016 -0.3122 90  GLN A CA  
590  C C   . GLN A 75  ? 0.8129 0.6844 0.8590 0.0245  -0.1991 -0.2890 90  GLN A C   
591  O O   . GLN A 75  ? 0.7621 0.6382 0.8325 0.0095  -0.2095 -0.3019 90  GLN A O   
592  C CB  . GLN A 75  ? 0.8834 0.7036 0.9373 0.0425  -0.2020 -0.3102 90  GLN A CB  
593  C CG  . GLN A 75  ? 0.8306 0.6220 0.9243 0.0252  -0.2135 -0.3255 90  GLN A CG  
594  C CD  . GLN A 75  ? 0.8736 0.6886 0.9707 0.0307  -0.2204 -0.3559 90  GLN A CD  
595  O OE1 . GLN A 75  ? 0.8717 0.6881 0.9599 0.0478  -0.2196 -0.3717 90  GLN A OE1 
596  N NE2 . GLN A 75  ? 0.8295 0.6665 0.9395 0.0169  -0.2274 -0.3645 90  GLN A NE2 
597  N N   . SER A 76  ? 0.7251 0.5975 0.7569 0.0236  -0.1852 -0.2561 91  SER A N   
598  C CA  . SER A 76  ? 0.7604 0.6413 0.8014 0.0069  -0.1812 -0.2343 91  SER A CA  
599  C C   . SER A 76  ? 0.7752 0.6989 0.8066 0.0097  -0.1848 -0.2436 91  SER A C   
600  O O   . SER A 76  ? 0.8199 0.7544 0.8721 -0.0058 -0.1901 -0.2434 91  SER A O   
601  C CB  . SER A 76  ? 0.6997 0.5742 0.7248 0.0078  -0.1658 -0.2012 91  SER A CB  
602  O OG  . SER A 76  ? 0.7292 0.5688 0.7632 0.0069  -0.1640 -0.1932 91  SER A OG  
603  N N   . LEU A 77  ? 0.8162 0.7674 0.8175 0.0302  -0.1817 -0.2504 92  LEU A N   
604  C CA  . LEU A 77  ? 0.6808 0.6758 0.6709 0.0367  -0.1855 -0.2582 92  LEU A CA  
605  C C   . LEU A 77  ? 0.7661 0.7739 0.7784 0.0297  -0.2041 -0.2914 92  LEU A C   
606  O O   . LEU A 77  ? 0.7736 0.8110 0.7957 0.0225  -0.2103 -0.2948 92  LEU A O   
607  C CB  . LEU A 77  ? 0.7562 0.7761 0.7100 0.0616  -0.1779 -0.2579 92  LEU A CB  
608  C CG  . LEU A 77  ? 0.8164 0.8850 0.7527 0.0747  -0.1810 -0.2643 92  LEU A CG  
609  C CD1 . LEU A 77  ? 0.6842 0.7666 0.6270 0.0650  -0.1759 -0.2420 92  LEU A CD1 
610  C CD2 . LEU A 77  ? 0.7713 0.8579 0.6726 0.0991  -0.1697 -0.2566 92  LEU A CD2 
611  N N   . LEU A 78  ? 0.7467 0.7335 0.7693 0.0317  -0.2134 -0.3175 93  LEU A N   
612  C CA  . LEU A 78  ? 0.7996 0.7946 0.8469 0.0236  -0.2312 -0.3524 93  LEU A CA  
613  C C   . LEU A 78  ? 0.8140 0.7862 0.9042 -0.0050 -0.2371 -0.3484 93  LEU A C   
614  O O   . LEU A 78  ? 0.7373 0.7335 0.8477 -0.0164 -0.2450 -0.3598 93  LEU A O   
615  C CB  . LEU A 78  ? 0.8463 0.8227 0.8938 0.0346  -0.2315 -0.3710 93  LEU A CB  
616  C CG  . LEU A 78  ? 0.8780 0.8822 0.8874 0.0626  -0.2254 -0.3764 93  LEU A CG  
617  C CD1 . LEU A 78  ? 0.8920 0.8777 0.9068 0.0722  -0.2262 -0.3953 93  LEU A CD1 
618  C CD2 . LEU A 78  ? 0.9563 1.0157 0.9494 0.0728  -0.2292 -0.3850 93  LEU A CD2 
619  N N   . ASP A 79  ? 0.7536 0.6826 0.8574 -0.0160 -0.2281 -0.3244 94  ASP A N   
620  C CA  . ASP A 79  ? 0.7691 0.6782 0.9115 -0.0426 -0.2292 -0.3114 94  ASP A CA  
621  C C   . ASP A 79  ? 0.7813 0.7301 0.9271 -0.0522 -0.2276 -0.2985 94  ASP A C   
622  O O   . ASP A 79  ? 0.7821 0.7383 0.9628 -0.0721 -0.2364 -0.3076 94  ASP A O   
623  C CB  . ASP A 79  ? 0.7903 0.6587 0.9350 -0.0477 -0.2160 -0.2782 94  ASP A CB  
624  C CG  . ASP A 79  ? 0.8345 0.6587 0.9895 -0.0430 -0.2192 -0.2896 94  ASP A CG  
625  O OD1 . ASP A 79  ? 0.7931 0.6152 0.9566 -0.0378 -0.2301 -0.3227 94  ASP A OD1 
626  O OD2 . ASP A 79  ? 0.8114 0.6058 0.9653 -0.0433 -0.2094 -0.2634 94  ASP A OD2 
627  N N   . ILE A 80  ? 0.8319 0.8065 0.9442 -0.0384 -0.2160 -0.2773 95  ILE A N   
628  C CA  . ILE A 80  ? 0.7594 0.7699 0.8748 -0.0452 -0.2128 -0.2625 95  ILE A CA  
629  C C   . ILE A 80  ? 0.8446 0.9022 0.9614 -0.0398 -0.2268 -0.2902 95  ILE A C   
630  O O   . ILE A 80  ? 0.7407 0.8240 0.8827 -0.0543 -0.2326 -0.2921 95  ILE A O   
631  C CB  . ILE A 80  ? 0.7186 0.7372 0.8004 -0.0318 -0.1954 -0.2316 95  ILE A CB  
632  C CG1 . ILE A 80  ? 0.6919 0.6691 0.7752 -0.0390 -0.1835 -0.2061 95  ILE A CG1 
633  C CG2 . ILE A 80  ? 0.6663 0.7230 0.7512 -0.0356 -0.1920 -0.2183 95  ILE A CG2 
634  C CD1 . ILE A 80  ? 0.8563 0.8379 0.9100 -0.0279 -0.1671 -0.1794 95  ILE A CD1 
635  N N   . MET A 81  ? 0.7580 0.8319 0.8482 -0.0183 -0.2324 -0.3117 96  MET A N   
636  C CA  . MET A 81  ? 0.8344 0.9591 0.9211 -0.0098 -0.2463 -0.3381 96  MET A CA  
637  C C   . MET A 81  ? 0.8181 0.9453 0.9465 -0.0306 -0.2604 -0.3629 96  MET A C   
638  O O   . MET A 81  ? 0.7892 0.9606 0.9217 -0.0292 -0.2675 -0.3742 96  MET A O   
639  C CB  . MET A 81  ? 0.8946 1.0328 0.9447 0.0174  -0.2470 -0.3543 96  MET A CB  
640  C CG  . MET A 81  ? 0.8413 0.9968 0.8488 0.0407  -0.2318 -0.3283 96  MET A CG  
641  S SD  . MET A 81  ? 0.9913 1.1546 0.9592 0.0707  -0.2290 -0.3424 96  MET A SD  
642  C CE  . MET A 81  ? 0.8625 1.0646 0.8408 0.0751  -0.2408 -0.3722 96  MET A CE  
643  N N   . GLU A 82  ? 0.7919 0.8713 0.9512 -0.0494 -0.2610 -0.3657 97  GLU A N   
644  C CA  . GLU A 82  ? 0.8510 0.9280 1.0515 -0.0710 -0.2695 -0.3819 97  GLU A CA  
645  C C   . GLU A 82  ? 0.8200 0.9270 1.0485 -0.0907 -0.2722 -0.3713 97  GLU A C   
646  O O   . GLU A 82  ? 0.8376 0.9634 1.0942 -0.1046 -0.2804 -0.3868 97  GLU A O   
647  C CB  . GLU A 82  ? 0.8770 0.8939 1.1060 -0.0870 -0.2669 -0.3800 97  GLU A CB  
648  C CG  . GLU A 82  ? 0.8864 0.8728 1.0962 -0.0693 -0.2647 -0.3924 97  GLU A CG  
649  C CD  . GLU A 82  ? 1.1145 1.1056 1.3364 -0.0676 -0.2737 -0.4249 97  GLU A CD  
650  O OE1 . GLU A 82  ? 1.1531 1.1565 1.4066 -0.0860 -0.2814 -0.4368 97  GLU A OE1 
651  O OE2 . GLU A 82  ? 1.2232 1.2066 1.4239 -0.0478 -0.2730 -0.4391 97  GLU A OE2 
652  N N   . PHE A 83  ? 0.6873 0.8003 0.9114 -0.0928 -0.2655 -0.3456 98  PHE A N   
653  C CA  . PHE A 83  ? 0.8225 0.9627 1.0744 -0.1110 -0.2633 -0.3291 98  PHE A CA  
654  C C   . PHE A 83  ? 0.8356 1.0400 1.0692 -0.0960 -0.2665 -0.3307 98  PHE A C   
655  O O   . PHE A 83  ? 0.7820 1.0164 1.0378 -0.1083 -0.2646 -0.3178 98  PHE A O   
656  C CB  . PHE A 83  ? 0.7528 0.8628 1.0017 -0.1180 -0.2430 -0.2858 98  PHE A CB  
657  C CG  . PHE A 83  ? 0.8455 0.8978 1.1193 -0.1352 -0.2400 -0.2793 98  PHE A CG  
658  C CD1 . PHE A 83  ? 0.7518 0.7621 1.0017 -0.1219 -0.2352 -0.2773 98  PHE A CD1 
659  C CD2 . PHE A 83  ? 0.8347 0.8762 1.1579 -0.1641 -0.2419 -0.2749 98  PHE A CD2 
660  C CE1 . PHE A 83  ? 0.7574 0.7158 1.0307 -0.1352 -0.2330 -0.2704 98  PHE A CE1 
661  C CE2 . PHE A 83  ? 0.8387 0.8259 1.1858 -0.1785 -0.2386 -0.2663 98  PHE A CE2 
662  C CZ  . PHE A 83  ? 0.8764 0.8217 1.1976 -0.1630 -0.2344 -0.2639 98  PHE A CZ  
663  N N   . LEU A 84  ? 0.8252 1.0534 1.0201 -0.0690 -0.2709 -0.3451 99  LEU A N   
664  C CA  . LEU A 84  ? 0.8726 1.1590 1.0445 -0.0500 -0.2709 -0.3393 99  LEU A CA  
665  C C   . LEU A 84  ? 0.8568 1.1872 1.0582 -0.0612 -0.2817 -0.3538 99  LEU A C   
666  O O   . LEU A 84  ? 0.8320 1.2083 1.0370 -0.0582 -0.2813 -0.3420 99  LEU A O   
667  C CB  . LEU A 84  ? 0.8226 1.1208 0.9464 -0.0183 -0.2693 -0.3463 99  LEU A CB  
668  C CG  . LEU A 84  ? 0.9511 1.2190 1.0376 -0.0016 -0.2512 -0.3185 99  LEU A CG  
669  C CD1 . LEU A 84  ? 0.9282 1.2010 0.9770 0.0241  -0.2532 -0.3336 99  LEU A CD1 
670  C CD2 . LEU A 84  ? 0.9030 1.1927 0.9739 0.0081  -0.2362 -0.2842 99  LEU A CD2 
671  N N   . ASP A 85  ? 0.8573 1.1743 1.0805 -0.0736 -0.2904 -0.3783 100 ASP A N   
672  C CA  . ASP A 85  ? 1.0080 1.3649 1.2585 -0.0843 -0.3013 -0.3949 100 ASP A CA  
673  C C   . ASP A 85  ? 0.9301 1.2742 1.2345 -0.1193 -0.3026 -0.3902 100 ASP A C   
674  O O   . ASP A 85  ? 0.9393 1.3172 1.2716 -0.1317 -0.3113 -0.4018 100 ASP A O   
675  C CB  . ASP A 85  ? 0.9464 1.3023 1.1903 -0.0766 -0.3107 -0.4271 100 ASP A CB  
676  C CG  . ASP A 85  ? 1.0560 1.3497 1.3151 -0.0898 -0.3100 -0.4387 100 ASP A CG  
677  O OD1 . ASP A 85  ? 1.0300 1.2791 1.2901 -0.0964 -0.3006 -0.4197 100 ASP A OD1 
678  O OD2 . ASP A 85  ? 1.1018 1.3922 1.3719 -0.0923 -0.3189 -0.4669 100 ASP A OD2 
679  N N   . LYS A 86  ? 0.8688 1.1670 1.1891 -0.1353 -0.2937 -0.3718 101 LYS A N   
680  C CA  . LYS A 86  ? 0.9127 1.1929 1.2851 -0.1690 -0.2927 -0.3651 101 LYS A CA  
681  C C   . LYS A 86  ? 0.9012 1.2270 1.2961 -0.1792 -0.2889 -0.3444 101 LYS A C   
682  O O   . LYS A 86  ? 0.7973 1.1613 1.1666 -0.1596 -0.2855 -0.3325 101 LYS A O   
683  C CB  . LYS A 86  ? 0.9011 1.1141 1.2826 -0.1808 -0.2834 -0.3509 101 LYS A CB  
684  C CG  . LYS A 86  ? 0.9442 1.1138 1.3105 -0.1718 -0.2868 -0.3721 101 LYS A CG  
685  C CD  . LYS A 86  ? 0.9522 1.0565 1.3421 -0.1892 -0.2793 -0.3603 101 LYS A CD  
686  C CE  . LYS A 86  ? 1.1870 1.2589 1.5804 -0.1873 -0.2855 -0.3877 101 LYS A CE  
687  N NZ  . LYS A 86  ? 1.2606 1.2673 1.6596 -0.1910 -0.2769 -0.3752 101 LYS A NZ  
688  N N   . ASP A 87  ? 0.8288 1.1507 1.2735 -0.2099 -0.2882 -0.3390 102 ASP A N   
689  C CA  . ASP A 87  ? 0.7859 1.1571 1.2618 -0.2234 -0.2854 -0.3233 102 ASP A CA  
690  C C   . ASP A 87  ? 0.8619 1.2162 1.3536 -0.2350 -0.2696 -0.2900 102 ASP A C   
691  O O   . ASP A 87  ? 0.8090 1.1155 1.3283 -0.2575 -0.2628 -0.2783 102 ASP A O   
692  C CB  . ASP A 87  ? 0.7775 1.1565 1.3003 -0.2510 -0.2930 -0.3365 102 ASP A CB  
693  C CG  . ASP A 87  ? 0.8729 1.3123 1.4285 -0.2632 -0.2920 -0.3241 102 ASP A CG  
694  O OD1 . ASP A 87  ? 0.8806 1.3514 1.4276 -0.2529 -0.2827 -0.3020 102 ASP A OD1 
695  O OD2 . ASP A 87  ? 0.8574 1.3141 1.4486 -0.2829 -0.3003 -0.3373 102 ASP A OD2 
696  N N   . PRO A 88  ? 0.8498 1.2308 1.3097 -0.2155 -0.2560 -0.2631 103 PRO A N   
697  C CA  . PRO A 88  ? 0.8235 1.1792 1.2783 -0.2204 -0.2327 -0.2210 103 PRO A CA  
698  C C   . PRO A 88  ? 0.8673 1.2369 1.3779 -0.2522 -0.2271 -0.2061 103 PRO A C   
699  O O   . PRO A 88  ? 0.8563 1.1975 1.3687 -0.2609 -0.2090 -0.1735 103 PRO A O   
700  C CB  . PRO A 88  ? 0.7828 1.1727 1.1940 -0.1909 -0.2218 -0.2028 103 PRO A CB  
701  C CG  . PRO A 88  ? 0.7857 1.1949 1.1655 -0.1662 -0.2364 -0.2300 103 PRO A CG  
702  C CD  . PRO A 88  ? 0.7417 1.1695 1.1611 -0.1839 -0.2592 -0.2681 103 PRO A CD  
703  N N   . GLU A 89  ? 0.9041 1.3197 1.4611 -0.2697 -0.2417 -0.2287 104 GLU A N   
704  C CA  . GLU A 89  ? 0.9040 1.3345 1.5201 -0.3027 -0.2361 -0.2148 104 GLU A CA  
705  C C   . GLU A 89  ? 0.9608 1.3311 1.6120 -0.3306 -0.2367 -0.2163 104 GLU A C   
706  O O   . GLU A 89  ? 1.0176 1.3762 1.7043 -0.3544 -0.2231 -0.1891 104 GLU A O   
707  C CB  . GLU A 89  ? 0.9396 1.4372 1.5888 -0.3108 -0.2503 -0.2359 104 GLU A CB  
708  C CG  . GLU A 89  ? 0.9461 1.5096 1.5673 -0.2818 -0.2534 -0.2394 104 GLU A CG  
709  C CD  . GLU A 89  ? 1.0336 1.6187 1.6444 -0.2740 -0.2303 -0.1991 104 GLU A CD  
710  O OE1 . GLU A 89  ? 1.0914 1.6735 1.7406 -0.2993 -0.2177 -0.1768 104 GLU A OE1 
711  O OE2 . GLU A 89  ? 1.0563 1.6612 1.6209 -0.2421 -0.2241 -0.1894 104 GLU A OE2 
712  N N   . ASP A 90  ? 0.9221 1.2502 1.5519 -0.3235 -0.2478 -0.2418 105 ASP A N   
713  C CA  . ASP A 90  ? 0.9882 1.2516 1.6357 -0.3422 -0.2450 -0.2414 105 ASP A CA  
714  C C   . ASP A 90  ? 0.9660 1.1786 1.6038 -0.3411 -0.2293 -0.2095 105 ASP A C   
715  O O   . ASP A 90  ? 0.9552 1.1474 1.5538 -0.3182 -0.2302 -0.2109 105 ASP A O   
716  C CB  . ASP A 90  ? 0.9442 1.1821 1.5678 -0.3292 -0.2604 -0.2785 105 ASP A CB  
717  C CG  . ASP A 90  ? 0.9597 1.1426 1.6101 -0.3493 -0.2601 -0.2855 105 ASP A CG  
718  O OD1 . ASP A 90  ? 0.9634 1.1067 1.6346 -0.3655 -0.2455 -0.2570 105 ASP A OD1 
719  O OD2 . ASP A 90  ? 1.0723 1.2523 1.7224 -0.3474 -0.2738 -0.3190 105 ASP A OD2 
720  N N   . HIS A 91  ? 1.0227 1.2164 1.6948 -0.3650 -0.2144 -0.1787 106 HIS A N   
721  C CA  . HIS A 91  ? 1.0059 1.1567 1.6678 -0.3632 -0.1986 -0.1426 106 HIS A CA  
722  C C   . HIS A 91  ? 0.9484 1.0289 1.5897 -0.3549 -0.2007 -0.1503 106 HIS A C   
723  O O   . HIS A 91  ? 0.9164 0.9638 1.5333 -0.3437 -0.1920 -0.1269 106 HIS A O   
724  C CB  . HIS A 91  ? 1.0941 1.2476 1.7937 -0.3884 -0.1801 -0.1046 106 HIS A CB  
725  C CG  . HIS A 91  ? 1.3103 1.5228 2.0082 -0.3856 -0.1684 -0.0795 106 HIS A CG  
726  N ND1 . HIS A 91  ? 1.4067 1.6194 2.1091 -0.3935 -0.1462 -0.0350 106 HIS A ND1 
727  C CD2 . HIS A 91  ? 1.3019 1.5747 1.9810 -0.3698 -0.1725 -0.0916 106 HIS A CD2 
728  C CE1 . HIS A 91  ? 1.3549 1.6251 2.0425 -0.3832 -0.1372 -0.0232 106 HIS A CE1 
729  N NE2 . HIS A 91  ? 1.3267 1.6327 2.0010 -0.3687 -0.1528 -0.0563 106 HIS A NE2 
730  N N   . ARG A 92  ? 0.9493 1.0084 1.5979 -0.3586 -0.2119 -0.1819 107 ARG A N   
731  C CA  . ARG A 92  ? 0.9087 0.9075 1.5356 -0.3457 -0.2150 -0.1934 107 ARG A CA  
732  C C   . ARG A 92  ? 0.8801 0.8833 1.4577 -0.3153 -0.2231 -0.2097 107 ARG A C   
733  O O   . ARG A 92  ? 0.9016 0.8594 1.4550 -0.3015 -0.2198 -0.2032 107 ARG A O   
734  C CB  . ARG A 92  ? 0.9482 0.9286 1.5955 -0.3552 -0.2256 -0.2256 107 ARG A CB  
735  C CG  . ARG A 92  ? 1.1818 1.1555 1.8794 -0.3862 -0.2181 -0.2115 107 ARG A CG  
736  C CD  . ARG A 92  ? 1.3140 1.2549 2.0321 -0.3948 -0.2276 -0.2412 107 ARG A CD  
737  N NE  . ARG A 92  ? 1.4064 1.3077 2.1637 -0.4182 -0.2150 -0.2170 107 ARG A NE  
738  C CZ  . ARG A 92  ? 1.5355 1.4006 2.3197 -0.4301 -0.2195 -0.2349 107 ARG A CZ  
739  N NH1 . ARG A 92  ? 1.4637 1.3280 2.2408 -0.4215 -0.2365 -0.2786 107 ARG A NH1 
740  N NH2 . ARG A 92  ? 1.4906 1.3203 2.3097 -0.4503 -0.2061 -0.2077 107 ARG A NH2 
741  N N   . THR A 93  ? 0.8655 0.9244 1.4274 -0.3036 -0.2331 -0.2292 108 THR A N   
742  C CA  . THR A 93  ? 0.9026 0.9699 1.4163 -0.2739 -0.2390 -0.2418 108 THR A CA  
743  C C   . THR A 93  ? 0.7844 0.8390 1.2608 -0.2598 -0.2198 -0.2016 108 THR A C   
744  O O   . THR A 93  ? 0.7514 0.7777 1.1857 -0.2380 -0.2165 -0.1997 108 THR A O   
745  C CB  . THR A 93  ? 0.8763 1.0100 1.3771 -0.2618 -0.2500 -0.2643 108 THR A CB  
746  O OG1 . THR A 93  ? 0.8599 1.0024 1.3721 -0.2667 -0.2621 -0.2958 108 THR A OG1 
747  C CG2 . THR A 93  ? 0.8460 0.9882 1.2862 -0.2272 -0.2495 -0.2681 108 THR A CG2 
748  N N   . LEU A 94  ? 0.7395 0.8171 1.2275 -0.2705 -0.2055 -0.1690 109 LEU A N   
749  C CA  . LEU A 94  ? 0.7808 0.8498 1.2299 -0.2563 -0.1861 -0.1318 109 LEU A CA  
750  C C   . LEU A 94  ? 0.8191 0.8273 1.2663 -0.2593 -0.1785 -0.1126 109 LEU A C   
751  O O   . LEU A 94  ? 0.8655 0.8542 1.2693 -0.2392 -0.1702 -0.0987 109 LEU A O   
752  C CB  . LEU A 94  ? 0.7071 0.8171 1.1719 -0.2674 -0.1727 -0.1038 109 LEU A CB  
753  C CG  . LEU A 94  ? 0.7101 0.8846 1.1775 -0.2620 -0.1794 -0.1197 109 LEU A CG  
754  C CD1 . LEU A 94  ? 0.7878 1.0028 1.2727 -0.2720 -0.1648 -0.0914 109 LEU A CD1 
755  C CD2 . LEU A 94  ? 0.6887 0.8781 1.1018 -0.2294 -0.1817 -0.1311 109 LEU A CD2 
756  N N   . SER A 95  ? 0.8426 0.8203 1.3383 -0.2838 -0.1817 -0.1123 110 SER A N   
757  C CA  . SER A 95  ? 0.8212 0.7402 1.3191 -0.2857 -0.1753 -0.0933 110 SER A CA  
758  C C   . SER A 95  ? 0.7818 0.6655 1.2510 -0.2650 -0.1854 -0.1186 110 SER A C   
759  O O   . SER A 95  ? 0.7920 0.6454 1.2305 -0.2498 -0.1774 -0.1006 110 SER A O   
760  C CB  . SER A 95  ? 0.8367 0.7302 1.3981 -0.3168 -0.1766 -0.0885 110 SER A CB  
761  O OG  . SER A 95  ? 0.9788 0.9109 1.5686 -0.3363 -0.1668 -0.0657 110 SER A OG  
762  N N   . GLN A 96  ? 0.8562 0.7466 1.3363 -0.2641 -0.2033 -0.1613 111 GLN A N   
763  C CA  . GLN A 96  ? 0.8628 0.7270 1.3139 -0.2425 -0.2125 -0.1876 111 GLN A CA  
764  C C   . GLN A 96  ? 0.7958 0.6796 1.1865 -0.2137 -0.2053 -0.1791 111 GLN A C   
765  O O   . GLN A 96  ? 0.8691 0.7233 1.2309 -0.1955 -0.2038 -0.1798 111 GLN A O   
766  C CB  . GLN A 96  ? 0.7700 0.6517 1.2288 -0.2410 -0.2278 -0.2316 111 GLN A CB  
767  C CG  . GLN A 96  ? 0.8189 0.6739 1.3155 -0.2595 -0.2281 -0.2394 111 GLN A CG  
768  C CD  . GLN A 96  ? 0.9155 0.8066 1.4228 -0.2636 -0.2411 -0.2756 111 GLN A CD  
769  O OE1 . GLN A 96  ? 1.0415 0.9651 1.5187 -0.2447 -0.2507 -0.3005 111 GLN A OE1 
770  N NE2 . GLN A 96  ? 0.9933 0.8815 1.5430 -0.2881 -0.2412 -0.2772 111 GLN A NE2 
771  N N   . PHE A 97  ? 0.8116 0.7451 1.1853 -0.2091 -0.2006 -0.1711 112 PHE A N   
772  C CA  . PHE A 97  ? 0.7651 0.7154 1.0852 -0.1832 -0.1922 -0.1611 112 PHE A CA  
773  C C   . PHE A 97  ? 0.8032 0.7222 1.1023 -0.1777 -0.1768 -0.1272 112 PHE A C   
774  O O   . PHE A 97  ? 0.7650 0.6659 1.0296 -0.1581 -0.1746 -0.1281 112 PHE A O   
775  C CB  . PHE A 97  ? 0.6709 0.6766 0.9825 -0.1806 -0.1883 -0.1551 112 PHE A CB  
776  C CG  . PHE A 97  ? 0.7114 0.7339 0.9719 -0.1538 -0.1810 -0.1495 112 PHE A CG  
777  C CD1 . PHE A 97  ? 0.7621 0.7899 0.9962 -0.1339 -0.1900 -0.1748 112 PHE A CD1 
778  C CD2 . PHE A 97  ? 0.6599 0.6923 0.8995 -0.1483 -0.1646 -0.1192 112 PHE A CD2 
779  C CE1 . PHE A 97  ? 0.7681 0.8088 0.9583 -0.1101 -0.1819 -0.1673 112 PHE A CE1 
780  C CE2 . PHE A 97  ? 0.6924 0.7362 0.8891 -0.1249 -0.1576 -0.1151 112 PHE A CE2 
781  C CZ  . PHE A 97  ? 0.6513 0.6981 0.8244 -0.1063 -0.1659 -0.1380 112 PHE A CZ  
782  N N   . THR A 98  ? 0.7799 0.6951 1.1004 -0.1946 -0.1660 -0.0969 113 THR A N   
783  C CA  . THR A 98  ? 0.7710 0.6621 1.0721 -0.1895 -0.1520 -0.0639 113 THR A CA  
784  C C   . THR A 98  ? 0.7602 0.6006 1.0616 -0.1841 -0.1563 -0.0677 113 THR A C   
785  O O   . THR A 98  ? 0.8197 0.6460 1.0872 -0.1667 -0.1507 -0.0581 113 THR A O   
786  C CB  . THR A 98  ? 0.8560 0.7547 1.1846 -0.2097 -0.1405 -0.0317 113 THR A CB  
787  O OG1 . THR A 98  ? 0.8326 0.7815 1.1599 -0.2122 -0.1359 -0.0288 113 THR A OG1 
788  C CG2 . THR A 98  ? 0.8295 0.7090 1.1360 -0.2032 -0.1266 0.0026  113 THR A CG2 
789  N N   . ASP A 99  ? 0.7544 0.5671 1.0964 -0.1989 -0.1661 -0.0824 114 ASP A N   
790  C CA  . ASP A 99  ? 0.8632 0.6266 1.2089 -0.1919 -0.1711 -0.0898 114 ASP A CA  
791  C C   . ASP A 99  ? 0.8950 0.6598 1.2007 -0.1661 -0.1770 -0.1143 114 ASP A C   
792  O O   . ASP A 99  ? 0.8465 0.5854 1.1316 -0.1512 -0.1735 -0.1059 114 ASP A O   
793  C CB  . ASP A 99  ? 0.8049 0.5410 1.2022 -0.2109 -0.1828 -0.1113 114 ASP A CB  
794  C CG  . ASP A 99  ? 0.9973 0.7240 1.4402 -0.2381 -0.1753 -0.0831 114 ASP A CG  
795  O OD1 . ASP A 99  ? 1.0384 0.7765 1.4695 -0.2397 -0.1605 -0.0446 114 ASP A OD1 
796  O OD2 . ASP A 99  ? 1.0210 0.7335 1.5053 -0.2551 -0.1812 -0.0988 114 ASP A OD2 
797  N N   . ALA A 100 ? 0.8204 0.6190 1.1153 -0.1599 -0.1856 -0.1434 115 ALA A N   
798  C CA  . ALA A 100 ? 0.7840 0.5887 1.0419 -0.1354 -0.1901 -0.1655 115 ALA A CA  
799  C C   . ALA A 100 ? 0.7892 0.6056 1.0035 -0.1182 -0.1769 -0.1421 115 ALA A C   
800  O O   . ALA A 100 ? 0.7525 0.5558 0.9409 -0.0998 -0.1761 -0.1472 115 ALA A O   
801  C CB  . ALA A 100 ? 0.7339 0.5778 0.9896 -0.1321 -0.2015 -0.1979 115 ALA A CB  
802  N N   . LEU A 101 ? 0.7638 0.6062 0.9706 -0.1237 -0.1665 -0.1179 116 LEU A N   
803  C CA  . LEU A 101 ? 0.7338 0.5843 0.9025 -0.1089 -0.1541 -0.0978 116 LEU A CA  
804  C C   . LEU A 101 ? 0.7832 0.5994 0.9488 -0.1072 -0.1479 -0.0763 116 LEU A C   
805  O O   . LEU A 101 ? 0.7856 0.5989 0.9211 -0.0914 -0.1426 -0.0710 116 LEU A O   
806  C CB  . LEU A 101 ? 0.7092 0.5941 0.8723 -0.1145 -0.1442 -0.0787 116 LEU A CB  
807  C CG  . LEU A 101 ? 0.7312 0.6571 0.8914 -0.1116 -0.1481 -0.0947 116 LEU A CG  
808  C CD1 . LEU A 101 ? 0.6931 0.6480 0.8386 -0.1099 -0.1352 -0.0734 116 LEU A CD1 
809  C CD2 . LEU A 101 ? 0.6702 0.6035 0.8045 -0.0915 -0.1545 -0.1188 116 LEU A CD2 
810  N N   . VAL A 102 ? 0.7844 0.5759 0.9822 -0.1231 -0.1484 -0.0627 117 VAL A N   
811  C CA  . VAL A 102 ? 0.8681 0.6287 1.0633 -0.1195 -0.1430 -0.0400 117 VAL A CA  
812  C C   . VAL A 102 ? 0.8124 0.5446 1.0017 -0.1042 -0.1507 -0.0595 117 VAL A C   
813  O O   . VAL A 102 ? 0.8585 0.5816 1.0256 -0.0900 -0.1463 -0.0489 117 VAL A O   
814  C CB  . VAL A 102 ? 0.9261 0.6669 1.1589 -0.1394 -0.1403 -0.0172 117 VAL A CB  
815  C CG1 . VAL A 102 ? 0.9443 0.6520 1.1751 -0.1327 -0.1363 0.0060  117 VAL A CG1 
816  C CG2 . VAL A 102 ? 0.8575 0.6312 1.0922 -0.1521 -0.1299 0.0061  117 VAL A CG2 
817  N N   . THR A 103 ? 0.7943 0.5148 1.0042 -0.1065 -0.1626 -0.0896 118 THR A N   
818  C CA  . THR A 103 ? 0.8085 0.5068 1.0114 -0.0898 -0.1698 -0.1126 118 THR A CA  
819  C C   . THR A 103 ? 0.8011 0.5240 0.9618 -0.0688 -0.1662 -0.1199 118 THR A C   
820  O O   . THR A 103 ? 0.8285 0.5372 0.9742 -0.0532 -0.1646 -0.1193 118 THR A O   
821  C CB  . THR A 103 ? 0.8695 0.5596 1.0993 -0.0958 -0.1835 -0.1484 118 THR A CB  
822  O OG1 . THR A 103 ? 0.8761 0.5365 1.1502 -0.1163 -0.1860 -0.1405 118 THR A OG1 
823  C CG2 . THR A 103 ? 0.8776 0.5503 1.0972 -0.0760 -0.1907 -0.1759 118 THR A CG2 
824  N N   . ILE A 104 ? 0.8244 0.5848 0.9672 -0.0680 -0.1641 -0.1253 119 ILE A N   
825  C CA  . ILE A 104 ? 0.7791 0.5618 0.8847 -0.0492 -0.1593 -0.1304 119 ILE A CA  
826  C C   . ILE A 104 ? 0.7791 0.5592 0.8647 -0.0436 -0.1476 -0.1030 119 ILE A C   
827  O O   . ILE A 104 ? 0.7102 0.4882 0.7757 -0.0281 -0.1448 -0.1056 119 ILE A O   
828  C CB  . ILE A 104 ? 0.7762 0.5982 0.8699 -0.0492 -0.1587 -0.1384 119 ILE A CB  
829  C CG1 . ILE A 104 ? 0.7474 0.5785 0.8536 -0.0485 -0.1721 -0.1716 119 ILE A CG1 
830  C CG2 . ILE A 104 ? 0.6975 0.5401 0.7546 -0.0324 -0.1492 -0.1325 119 ILE A CG2 
831  C CD1 . ILE A 104 ? 0.7320 0.6040 0.8328 -0.0500 -0.1737 -0.1784 119 ILE A CD1 
832  N N   . ARG A 105 ? 0.7056 0.4887 0.7971 -0.0562 -0.1407 -0.0773 120 ARG A N   
833  C CA  . ARG A 105 ? 0.7886 0.5737 0.8603 -0.0509 -0.1307 -0.0538 120 ARG A CA  
834  C C   . ARG A 105 ? 0.7842 0.5409 0.8600 -0.0432 -0.1330 -0.0486 120 ARG A C   
835  O O   . ARG A 105 ? 0.7895 0.5500 0.8446 -0.0307 -0.1288 -0.0446 120 ARG A O   
836  C CB  . ARG A 105 ? 0.7755 0.5714 0.8531 -0.0650 -0.1232 -0.0283 120 ARG A CB  
837  C CG  . ARG A 105 ? 0.8112 0.6149 0.8666 -0.0595 -0.1135 -0.0067 120 ARG A CG  
838  C CD  . ARG A 105 ? 0.7693 0.5863 0.8304 -0.0724 -0.1060 0.0176  120 ARG A CD  
839  N NE  . ARG A 105 ? 0.9005 0.6967 0.9907 -0.0846 -0.1087 0.0322  120 ARG A NE  
840  C CZ  . ARG A 105 ? 0.9383 0.7435 1.0484 -0.1004 -0.1053 0.0455  120 ARG A CZ  
841  N NH1 . ARG A 105 ? 0.8536 0.6902 0.9570 -0.1049 -0.0995 0.0453  120 ARG A NH1 
842  N NH2 . ARG A 105 ? 0.8811 0.6634 1.0205 -0.1115 -0.1070 0.0601  120 ARG A NH2 
843  N N   . ASN A 106 ? 0.7965 0.5243 0.9010 -0.0501 -0.1397 -0.0493 121 ASN A N   
844  C CA  . ASN A 106 ? 0.8607 0.5597 0.9718 -0.0407 -0.1422 -0.0438 121 ASN A CA  
845  C C   . ASN A 106 ? 0.8620 0.5585 0.9612 -0.0225 -0.1469 -0.0698 121 ASN A C   
846  O O   . ASN A 106 ? 0.8729 0.5644 0.9615 -0.0089 -0.1451 -0.0642 121 ASN A O   
847  C CB  . ASN A 106 ? 0.8646 0.5294 1.0129 -0.0522 -0.1475 -0.0385 121 ASN A CB  
848  C CG  . ASN A 106 ? 0.8938 0.5618 1.0550 -0.0695 -0.1408 -0.0077 121 ASN A CG  
849  O OD1 . ASN A 106 ? 0.9464 0.6388 1.0863 -0.0694 -0.1321 0.0128  121 ASN A OD1 
850  N ND2 . ASN A 106 ? 1.0184 0.6627 1.2161 -0.0848 -0.1443 -0.0049 121 ASN A ND2 
851  N N   . ARG A 107 ? 0.7813 0.4859 0.8819 -0.0214 -0.1530 -0.0982 122 ARG A N   
852  C CA  . ARG A 107 ? 0.8051 0.5128 0.8925 -0.0032 -0.1565 -0.1234 122 ARG A CA  
853  C C   . ARG A 107 ? 0.8609 0.5927 0.9171 0.0098  -0.1475 -0.1155 122 ARG A C   
854  O O   . ARG A 107 ? 0.7797 0.5094 0.8277 0.0257  -0.1474 -0.1246 122 ARG A O   
855  C CB  . ARG A 107 ? 0.7498 0.4725 0.8388 -0.0041 -0.1637 -0.1529 122 ARG A CB  
856  C CG  . ARG A 107 ? 0.7391 0.4703 0.8126 0.0156  -0.1668 -0.1796 122 ARG A CG  
857  C CD  . ARG A 107 ? 0.7670 0.5194 0.8392 0.0158  -0.1745 -0.2081 122 ARG A CD  
858  N NE  . ARG A 107 ? 0.8677 0.5986 0.9730 0.0034  -0.1864 -0.2264 122 ARG A NE  
859  C CZ  . ARG A 107 ? 0.8323 0.5772 0.9516 -0.0117 -0.1923 -0.2346 122 ARG A CZ  
860  N NH1 . ARG A 107 ? 0.7651 0.5458 0.8670 -0.0143 -0.1876 -0.2257 122 ARG A NH1 
861  N NH2 . ARG A 107 ? 0.7957 0.5183 0.9496 -0.0242 -0.2032 -0.2528 122 ARG A NH2 
862  N N   . HIS A 108 ? 0.7086 0.4630 0.7495 0.0031  -0.1394 -0.0992 123 HIS A N   
863  C CA  . HIS A 108 ? 0.7195 0.4961 0.7341 0.0128  -0.1304 -0.0940 123 HIS A CA  
864  C C   . HIS A 108 ? 0.7573 0.5314 0.7672 0.0127  -0.1248 -0.0709 123 HIS A C   
865  O O   . HIS A 108 ? 0.7065 0.4993 0.6978 0.0172  -0.1170 -0.0656 123 HIS A O   
866  C CB  . HIS A 108 ? 0.7349 0.5379 0.7355 0.0076  -0.1246 -0.0925 123 HIS A CB  
867  C CG  . HIS A 108 ? 0.7125 0.5282 0.7118 0.0113  -0.1296 -0.1147 123 HIS A CG  
868  N ND1 . HIS A 108 ? 0.7896 0.6311 0.7756 0.0112  -0.1250 -0.1150 123 HIS A ND1 
869  C CD2 . HIS A 108 ? 0.7579 0.5662 0.7670 0.0166  -0.1394 -0.1382 123 HIS A CD2 
870  C CE1 . HIS A 108 ? 0.7481 0.6007 0.7347 0.0165  -0.1320 -0.1363 123 HIS A CE1 
871  N NE2 . HIS A 108 ? 0.6950 0.5283 0.6951 0.0194  -0.1411 -0.1522 123 HIS A NE2 
872  N N   . ASN A 109 ? 0.7836 0.5362 0.8107 0.0076  -0.1283 -0.0567 124 ASN A N   
873  C CA  . ASN A 109 ? 0.8465 0.6032 0.8674 0.0068  -0.1235 -0.0325 124 ASN A CA  
874  C C   . ASN A 109 ? 0.7437 0.5099 0.7517 0.0213  -0.1212 -0.0347 124 ASN A C   
875  O O   . ASN A 109 ? 0.7761 0.5581 0.7725 0.0208  -0.1163 -0.0205 124 ASN A O   
876  C CB  . ASN A 109 ? 0.9416 0.6734 0.9839 0.0015  -0.1276 -0.0144 124 ASN A CB  
877  C CG  . ASN A 109 ? 0.9986 0.7346 1.0473 -0.0155 -0.1240 0.0040  124 ASN A CG  
878  O OD1 . ASN A 109 ? 0.9816 0.7421 1.0152 -0.0214 -0.1178 0.0066  124 ASN A OD1 
879  N ND2 . ASN A 109 ? 1.0771 0.7889 1.1501 -0.0229 -0.1271 0.0176  124 ASN A ND2 
880  N N   . ASP A 110 ? 0.7243 0.4844 0.7349 0.0341  -0.1248 -0.0534 125 ASP A N   
881  C CA  . ASP A 110 ? 0.8046 0.5749 0.8080 0.0482  -0.1227 -0.0554 125 ASP A CA  
882  C C   . ASP A 110 ? 0.8052 0.5996 0.7917 0.0538  -0.1159 -0.0692 125 ASP A C   
883  O O   . ASP A 110 ? 0.7385 0.5419 0.7226 0.0662  -0.1141 -0.0760 125 ASP A O   
884  C CB  . ASP A 110 ? 0.7617 0.5100 0.7815 0.0611  -0.1299 -0.0643 125 ASP A CB  
885  C CG  . ASP A 110 ? 0.8082 0.5327 0.8454 0.0585  -0.1347 -0.0449 125 ASP A CG  
886  O OD1 . ASP A 110 ? 0.9925 0.7281 1.0238 0.0542  -0.1318 -0.0225 125 ASP A OD1 
887  O OD2 . ASP A 110 ? 1.0318 0.7270 1.0888 0.0608  -0.1411 -0.0516 125 ASP A OD2 
888  N N   . VAL A 111 ? 0.7345 0.5407 0.7105 0.0454  -0.1112 -0.0715 126 VAL A N   
889  C CA  . VAL A 111 ? 0.7075 0.5336 0.6688 0.0517  -0.1041 -0.0828 126 VAL A CA  
890  C C   . VAL A 111 ? 0.7633 0.6072 0.7158 0.0537  -0.0955 -0.0744 126 VAL A C   
891  O O   . VAL A 111 ? 0.6256 0.4830 0.5725 0.0630  -0.0898 -0.0821 126 VAL A O   
892  C CB  . VAL A 111 ? 0.7626 0.5967 0.7166 0.0437  -0.1017 -0.0851 126 VAL A CB  
893  C CG1 . VAL A 111 ? 0.7648 0.6202 0.7024 0.0486  -0.0911 -0.0868 126 VAL A CG1 
894  C CG2 . VAL A 111 ? 0.7412 0.5665 0.7035 0.0454  -0.1105 -0.1022 126 VAL A CG2 
895  N N   . VAL A 112 ? 0.7132 0.5595 0.6652 0.0447  -0.0941 -0.0592 127 VAL A N   
896  C CA  . VAL A 112 ? 0.6197 0.4842 0.5654 0.0446  -0.0868 -0.0546 127 VAL A CA  
897  C C   . VAL A 112 ? 0.7375 0.6077 0.6909 0.0561  -0.0887 -0.0582 127 VAL A C   
898  O O   . VAL A 112 ? 0.6416 0.5270 0.5923 0.0613  -0.0815 -0.0649 127 VAL A O   
899  C CB  . VAL A 112 ? 0.7621 0.6316 0.7047 0.0336  -0.0861 -0.0405 127 VAL A CB  
900  C CG1 . VAL A 112 ? 0.6130 0.5016 0.5527 0.0334  -0.0809 -0.0398 127 VAL A CG1 
901  C CG2 . VAL A 112 ? 0.7059 0.5756 0.6406 0.0240  -0.0814 -0.0384 127 VAL A CG2 
902  N N   . PRO A 113 ? 0.6413 0.5010 0.6054 0.0612  -0.0973 -0.0530 128 PRO A N   
903  C CA  . PRO A 113 ? 0.6742 0.5426 0.6467 0.0744  -0.0989 -0.0569 128 PRO A CA  
904  C C   . PRO A 113 ? 0.7437 0.6101 0.7184 0.0871  -0.0977 -0.0736 128 PRO A C   
905  O O   . PRO A 113 ? 0.6933 0.5755 0.6723 0.0978  -0.0947 -0.0789 128 PRO A O   
906  C CB  . PRO A 113 ? 0.6712 0.5247 0.6551 0.0784  -0.1086 -0.0454 128 PRO A CB  
907  C CG  . PRO A 113 ? 0.7191 0.5549 0.7014 0.0666  -0.1113 -0.0355 128 PRO A CG  
908  C CD  . PRO A 113 ? 0.7689 0.6075 0.7405 0.0568  -0.1052 -0.0431 128 PRO A CD  
909  N N   . THR A 114 ? 0.6913 0.5419 0.6639 0.0869  -0.1003 -0.0831 129 THR A N   
910  C CA  . THR A 114 ? 0.6763 0.5301 0.6476 0.1000  -0.0991 -0.1014 129 THR A CA  
911  C C   . THR A 114 ? 0.7087 0.5892 0.6679 0.1018  -0.0870 -0.1040 129 THR A C   
912  O O   . THR A 114 ? 0.5923 0.4882 0.5527 0.1144  -0.0825 -0.1116 129 THR A O   
913  C CB  . THR A 114 ? 0.6362 0.4712 0.6080 0.0983  -0.1057 -0.1131 129 THR A CB  
914  O OG1 . THR A 114 ? 0.6724 0.4801 0.6599 0.0952  -0.1155 -0.1083 129 THR A OG1 
915  C CG2 . THR A 114 ? 0.5996 0.4402 0.5692 0.1141  -0.1061 -0.1348 129 THR A CG2 
916  N N   . MET A 115 ? 0.6795 0.5661 0.6285 0.0898  -0.0806 -0.0963 130 MET A N   
917  C CA  . MET A 115 ? 0.6735 0.5820 0.6140 0.0913  -0.0677 -0.0958 130 MET A CA  
918  C C   . MET A 115 ? 0.6580 0.5829 0.6072 0.0910  -0.0621 -0.0894 130 MET A C   
919  O O   . MET A 115 ? 0.6481 0.5922 0.5972 0.0965  -0.0519 -0.0911 130 MET A O   
920  C CB  . MET A 115 ? 0.6188 0.5271 0.5488 0.0799  -0.0619 -0.0888 130 MET A CB  
921  C CG  . MET A 115 ? 0.6288 0.5323 0.5501 0.0830  -0.0651 -0.0969 130 MET A CG  
922  S SD  . MET A 115 ? 0.8143 0.7398 0.7235 0.0986  -0.0556 -0.1054 130 MET A SD  
923  C CE  . MET A 115 ? 0.9428 0.8644 0.8431 0.1003  -0.0641 -0.1161 130 MET A CE  
924  N N   . ALA A 116 ? 0.6102 0.5305 0.5677 0.0849  -0.0687 -0.0817 131 ALA A N   
925  C CA  . ALA A 116 ? 0.6078 0.5478 0.5759 0.0852  -0.0661 -0.0779 131 ALA A CA  
926  C C   . ALA A 116 ? 0.5999 0.5521 0.5774 0.1016  -0.0659 -0.0858 131 ALA A C   
927  O O   . ALA A 116 ? 0.6044 0.5808 0.5896 0.1032  -0.0578 -0.0859 131 ALA A O   
928  C CB  . ALA A 116 ? 0.5639 0.4998 0.5372 0.0791  -0.0755 -0.0684 131 ALA A CB  
929  N N   . GLN A 117 ? 0.6141 0.5502 0.5939 0.1137  -0.0745 -0.0931 132 GLN A N   
930  C CA  . GLN A 117 ? 0.5885 0.5357 0.5766 0.1318  -0.0740 -0.1032 132 GLN A CA  
931  C C   . GLN A 117 ? 0.5958 0.5622 0.5756 0.1381  -0.0617 -0.1112 132 GLN A C   
932  O O   . GLN A 117 ? 0.6242 0.6134 0.6116 0.1500  -0.0557 -0.1156 132 GLN A O   
933  C CB  . GLN A 117 ? 0.6486 0.5698 0.6411 0.1434  -0.0853 -0.1122 132 GLN A CB  
934  C CG  . GLN A 117 ? 0.6319 0.5391 0.6375 0.1441  -0.0958 -0.1017 132 GLN A CG  
935  C CD  . GLN A 117 ? 0.7594 0.6924 0.7780 0.1534  -0.0947 -0.0974 132 GLN A CD  
936  O OE1 . GLN A 117 ? 0.7087 0.6581 0.7332 0.1685  -0.0904 -0.1079 132 GLN A OE1 
937  N NE2 . GLN A 117 ? 0.6511 0.5918 0.6743 0.1453  -0.0986 -0.0824 132 GLN A NE2 
938  N N   . GLY A 118 ? 0.5421 0.5025 0.5069 0.1316  -0.0573 -0.1119 133 GLY A N   
939  C CA  . GLY A 118 ? 0.5719 0.5533 0.5272 0.1377  -0.0443 -0.1148 133 GLY A CA  
940  C C   . GLY A 118 ? 0.6909 0.6941 0.6528 0.1289  -0.0309 -0.1028 133 GLY A C   
941  O O   . GLY A 118 ? 0.5464 0.5742 0.5109 0.1369  -0.0192 -0.1029 133 GLY A O   
942  N N   . VAL A 119 ? 0.5440 0.5398 0.5103 0.1119  -0.0320 -0.0929 134 VAL A N   
943  C CA  . VAL A 119 ? 0.5120 0.5265 0.4891 0.1013  -0.0206 -0.0845 134 VAL A CA  
944  C C   . VAL A 119 ? 0.5244 0.5625 0.5205 0.1080  -0.0206 -0.0867 134 VAL A C   
945  O O   . VAL A 119 ? 0.5033 0.5662 0.5101 0.1079  -0.0079 -0.0840 134 VAL A O   
946  C CB  . VAL A 119 ? 0.5806 0.5828 0.5584 0.0832  -0.0242 -0.0778 134 VAL A CB  
947  C CG1 . VAL A 119 ? 0.4714 0.4931 0.4654 0.0717  -0.0150 -0.0737 134 VAL A CG1 
948  C CG2 . VAL A 119 ? 0.5415 0.5255 0.5028 0.0775  -0.0212 -0.0747 134 VAL A CG2 
949  N N   . LEU A 120 ? 0.4787 0.5103 0.4810 0.1141  -0.0345 -0.0902 135 LEU A N   
950  C CA  . LEU A 120 ? 0.4915 0.5468 0.5129 0.1224  -0.0367 -0.0918 135 LEU A CA  
951  C C   . LEU A 120 ? 0.5339 0.6087 0.5584 0.1402  -0.0283 -0.0992 135 LEU A C   
952  O O   . LEU A 120 ? 0.5088 0.6151 0.5501 0.1428  -0.0203 -0.0980 135 LEU A O   
953  C CB  . LEU A 120 ? 0.5238 0.5633 0.5486 0.1288  -0.0533 -0.0920 135 LEU A CB  
954  C CG  . LEU A 120 ? 0.5999 0.6624 0.6445 0.1394  -0.0587 -0.0918 135 LEU A CG  
955  C CD1 . LEU A 120 ? 0.5735 0.6625 0.6310 0.1243  -0.0569 -0.0855 135 LEU A CD1 
956  C CD2 . LEU A 120 ? 0.6354 0.6740 0.6804 0.1496  -0.0742 -0.0900 135 LEU A CD2 
957  N N   . GLU A 121 ? 0.5064 0.5659 0.5161 0.1531  -0.0304 -0.1081 136 GLU A N   
958  C CA  . GLU A 121 ? 0.5170 0.5977 0.5265 0.1721  -0.0223 -0.1171 136 GLU A CA  
959  C C   . GLU A 121 ? 0.5060 0.6135 0.5144 0.1670  -0.0032 -0.1091 136 GLU A C   
960  O O   . GLU A 121 ? 0.5742 0.7139 0.5944 0.1762  0.0072  -0.1092 136 GLU A O   
961  C CB  . GLU A 121 ? 0.5075 0.5680 0.4996 0.1858  -0.0288 -0.1313 136 GLU A CB  
962  C CG  . GLU A 121 ? 0.6314 0.7193 0.6162 0.2051  -0.0174 -0.1413 136 GLU A CG  
963  C CD  . GLU A 121 ? 0.6541 0.7267 0.6224 0.2204  -0.0252 -0.1606 136 GLU A CD  
964  O OE1 . GLU A 121 ? 0.7155 0.7554 0.6778 0.2131  -0.0378 -0.1650 136 GLU A OE1 
965  O OE2 . GLU A 121 ? 0.6741 0.7699 0.6365 0.2396  -0.0186 -0.1725 136 GLU A OE2 
966  N N   . TYR A 122 ? 0.5386 0.6338 0.5351 0.1525  0.0024  -0.1006 137 TYR A N   
967  C CA  . TYR A 122 ? 0.5698 0.6857 0.5662 0.1479  0.0217  -0.0899 137 TYR A CA  
968  C C   . TYR A 122 ? 0.6032 0.7424 0.6262 0.1358  0.0303  -0.0815 137 TYR A C   
969  O O   . TYR A 122 ? 0.5139 0.6828 0.5475 0.1394  0.0461  -0.0759 137 TYR A O   
970  C CB  . TYR A 122 ? 0.5989 0.6935 0.5790 0.1359  0.0251  -0.0818 137 TYR A CB  
971  C CG  . TYR A 122 ? 0.6146 0.7269 0.5949 0.1328  0.0460  -0.0679 137 TYR A CG  
972  C CD1 . TYR A 122 ? 0.6173 0.7344 0.6174 0.1148  0.0565  -0.0564 137 TYR A CD1 
973  C CD2 . TYR A 122 ? 0.6614 0.7869 0.6234 0.1484  0.0555  -0.0662 137 TYR A CD2 
974  C CE1 . TYR A 122 ? 0.6647 0.7946 0.6688 0.1115  0.0771  -0.0415 137 TYR A CE1 
975  C CE2 . TYR A 122 ? 0.6066 0.7488 0.5691 0.1470  0.0761  -0.0494 137 TYR A CE2 
976  C CZ  . TYR A 122 ? 0.6838 0.8259 0.6688 0.1280  0.0874  -0.0360 137 TYR A CZ  
977  O OH  . TYR A 122 ? 0.7304 0.8854 0.7197 0.1256  0.1092  -0.0171 137 TYR A OH  
978  N N   . LYS A 123 ? 0.5471 0.6757 0.5818 0.1210  0.0201  -0.0807 138 LYS A N   
979  C CA  . LYS A 123 ? 0.5190 0.6714 0.5810 0.1079  0.0251  -0.0764 138 LYS A CA  
980  C C   . LYS A 123 ? 0.4923 0.6807 0.5734 0.1213  0.0286  -0.0800 138 LYS A C   
981  O O   . LYS A 123 ? 0.5721 0.7905 0.6759 0.1139  0.0417  -0.0746 138 LYS A O   
982  C CB  . LYS A 123 ? 0.6137 0.7539 0.6816 0.0957  0.0091  -0.0789 138 LYS A CB  
983  C CG  . LYS A 123 ? 0.7628 0.8871 0.8291 0.0743  0.0117  -0.0743 138 LYS A CG  
984  C CD  . LYS A 123 ? 0.6330 0.7530 0.7036 0.0652  -0.0046 -0.0778 138 LYS A CD  
985  C CE  . LYS A 123 ? 0.5728 0.7270 0.6717 0.0574  -0.0050 -0.0807 138 LYS A CE  
986  N NZ  . LYS A 123 ? 0.6391 0.7908 0.7382 0.0463  -0.0190 -0.0838 138 LYS A NZ  
987  N N   . ASP A 124 ? 0.5023 0.6887 0.5778 0.1408  0.0174  -0.0893 139 ASP A N   
988  C CA  . ASP A 124 ? 0.5819 0.8035 0.6770 0.1556  0.0197  -0.0936 139 ASP A CA  
989  C C   . ASP A 124 ? 0.5020 0.7418 0.5886 0.1749  0.0330  -0.0969 139 ASP A C   
990  O O   . ASP A 124 ? 0.5378 0.8143 0.6427 0.1859  0.0404  -0.0983 139 ASP A O   
991  C CB  . ASP A 124 ? 0.6496 0.8619 0.7488 0.1676  0.0004  -0.1013 139 ASP A CB  
992  C CG  . ASP A 124 ? 0.6647 0.8698 0.7730 0.1504  -0.0118 -0.0964 139 ASP A CG  
993  O OD1 . ASP A 124 ? 0.5934 0.8197 0.7185 0.1325  -0.0052 -0.0914 139 ASP A OD1 
994  O OD2 . ASP A 124 ? 0.6200 0.7987 0.7189 0.1542  -0.0275 -0.0977 139 ASP A OD2 
995  N N   . THR A 125 ? 0.5499 0.7701 0.6095 0.1800  0.0366  -0.0981 140 THR A N   
996  C CA  . THR A 125 ? 0.5493 0.7924 0.5980 0.1993  0.0496  -0.1014 140 THR A CA  
997  C C   . THR A 125 ? 0.5631 0.8240 0.6092 0.1907  0.0714  -0.0854 140 THR A C   
998  O O   . THR A 125 ? 0.5130 0.8059 0.5566 0.2056  0.0862  -0.0836 140 THR A O   
999  C CB  . THR A 125 ? 0.5424 0.7601 0.5627 0.2156  0.0391  -0.1161 140 THR A CB  
1000 O OG1 . THR A 125 ? 0.6440 0.8302 0.6460 0.2014  0.0353  -0.1108 140 THR A OG1 
1001 C CG2 . THR A 125 ? 0.5395 0.7388 0.5659 0.2270  0.0198  -0.1313 140 THR A CG2 
1002 N N   . TYR A 126 ? 0.4893 0.7298 0.5351 0.1686  0.0743  -0.0733 141 TYR A N   
1003 C CA  . TYR A 126 ? 0.5978 0.8495 0.6450 0.1589  0.0956  -0.0552 141 TYR A CA  
1004 C C   . TYR A 126 ? 0.6855 0.9354 0.7605 0.1321  0.1018  -0.0440 141 TYR A C   
1005 O O   . TYR A 126 ? 0.5646 0.8310 0.6527 0.1240  0.1222  -0.0283 141 TYR A O   
1006 C CB  . TYR A 126 ? 0.4985 0.7255 0.5134 0.1624  0.0963  -0.0514 141 TYR A CB  
1007 C CG  . TYR A 126 ? 0.6238 0.8641 0.6135 0.1893  0.0948  -0.0628 141 TYR A CG  
1008 C CD1 . TYR A 126 ? 0.6041 0.8836 0.5919 0.2047  0.1130  -0.0563 141 TYR A CD1 
1009 C CD2 . TYR A 126 ? 0.5883 0.8042 0.5583 0.1993  0.0752  -0.0812 141 TYR A CD2 
1010 C CE1 . TYR A 126 ? 0.6184 0.9140 0.5823 0.2308  0.1110  -0.0702 141 TYR A CE1 
1011 C CE2 . TYR A 126 ? 0.5846 0.8132 0.5340 0.2233  0.0726  -0.0961 141 TYR A CE2 
1012 C CZ  . TYR A 126 ? 0.6589 0.9280 0.6037 0.2397  0.0901  -0.0916 141 TYR A CZ  
1013 O OH  . TYR A 126 ? 0.8386 1.1233 0.7612 0.2650  0.0870  -0.1096 141 TYR A OH  
1014 N N   . GLY A 127 ? 0.5604 0.7935 0.6465 0.1188  0.0858  -0.0516 142 GLY A N   
1015 C CA  . GLY A 127 ? 0.5209 0.7604 0.6368 0.0951  0.0895  -0.0467 142 GLY A CA  
1016 C C   . GLY A 127 ? 0.5549 0.7575 0.6626 0.0767  0.0829  -0.0457 142 GLY A C   
1017 O O   . GLY A 127 ? 0.6288 0.8019 0.7087 0.0816  0.0773  -0.0459 142 GLY A O   
1018 N N   . ASP A 128 ? 0.5537 0.7613 0.6881 0.0553  0.0835  -0.0462 143 ASP A N   
1019 C CA  . ASP A 128 ? 0.6580 0.8348 0.7875 0.0381  0.0757  -0.0491 143 ASP A CA  
1020 C C   . ASP A 128 ? 0.6929 0.8655 0.8438 0.0168  0.0926  -0.0412 143 ASP A C   
1021 O O   . ASP A 128 ? 0.6586 0.8292 0.8282 -0.0021 0.0875  -0.0490 143 ASP A O   
1022 C CB  . ASP A 128 ? 0.6201 0.8016 0.7574 0.0329  0.0550  -0.0622 143 ASP A CB  
1023 C CG  . ASP A 128 ? 0.7896 1.0101 0.9644 0.0228  0.0562  -0.0669 143 ASP A CG  
1024 O OD1 . ASP A 128 ? 0.6889 0.9322 0.8871 0.0178  0.0738  -0.0602 143 ASP A OD1 
1025 O OD2 . ASP A 128 ? 0.8815 1.1122 1.0633 0.0199  0.0393  -0.0767 143 ASP A OD2 
1026 N N   . ASP A 129 ? 0.6635 0.8343 0.8116 0.0204  0.1127  -0.0258 144 ASP A N   
1027 C CA  . ASP A 129 ? 0.6427 0.8053 0.8125 0.0022  0.1318  -0.0145 144 ASP A CA  
1028 C C   . ASP A 129 ? 0.6748 0.7954 0.8270 -0.0050 0.1296  -0.0137 144 ASP A C   
1029 O O   . ASP A 129 ? 0.6787 0.7801 0.7994 0.0062  0.1163  -0.0182 144 ASP A O   
1030 C CB  . ASP A 129 ? 0.5833 0.7620 0.7545 0.0124  0.1550  0.0056  144 ASP A CB  
1031 C CG  . ASP A 129 ? 0.6245 0.7912 0.7549 0.0353  0.1543  0.0123  144 ASP A CG  
1032 O OD1 . ASP A 129 ? 0.6852 0.8626 0.7961 0.0530  0.1406  0.0018  144 ASP A OD1 
1033 O OD2 . ASP A 129 ? 0.7330 0.8784 0.8513 0.0357  0.1662  0.0269  144 ASP A OD2 
1034 N N   . PRO A 130 ? 0.6688 0.7740 0.8429 -0.0237 0.1433  -0.0080 145 PRO A N   
1035 C CA  . PRO A 130 ? 0.6730 0.7388 0.8319 -0.0293 0.1411  -0.0089 145 PRO A CA  
1036 C C   . PRO A 130 ? 0.6852 0.7326 0.8100 -0.0107 0.1465  0.0059  145 PRO A C   
1037 O O   . PRO A 130 ? 0.6859 0.7085 0.7879 -0.0078 0.1358  0.0005  145 PRO A O   
1038 C CB  . PRO A 130 ? 0.6512 0.7065 0.8465 -0.0516 0.1581  -0.0050 145 PRO A CB  
1039 C CG  . PRO A 130 ? 0.7104 0.8013 0.9415 -0.0634 0.1590  -0.0123 145 PRO A CG  
1040 C CD  . PRO A 130 ? 0.6710 0.7930 0.8887 -0.0427 0.1591  -0.0041 145 PRO A CD  
1041 N N   . VAL A 131 ? 0.7239 0.7863 0.8441 0.0027  0.1625  0.0242  146 VAL A N   
1042 C CA  . VAL A 131 ? 0.6760 0.7261 0.7629 0.0216  0.1666  0.0376  146 VAL A CA  
1043 C C   . VAL A 131 ? 0.6761 0.7283 0.7306 0.0375  0.1448  0.0236  146 VAL A C   
1044 O O   . VAL A 131 ? 0.6383 0.6701 0.6680 0.0446  0.1376  0.0233  146 VAL A O   
1045 C CB  . VAL A 131 ? 0.7605 0.8323 0.8487 0.0336  0.1890  0.0609  146 VAL A CB  
1046 C CG1 . VAL A 131 ? 0.5928 0.6663 0.6412 0.0584  0.1876  0.0694  146 VAL A CG1 
1047 C CG2 . VAL A 131 ? 0.7566 0.8130 0.8720 0.0192  0.2123  0.0802  146 VAL A CG2 
1048 N N   . SER A 132 ? 0.6769 0.7539 0.7338 0.0435  0.1344  0.0119  147 SER A N   
1049 C CA  . SER A 132 ? 0.7133 0.7881 0.7460 0.0560  0.1130  -0.0032 147 SER A CA  
1050 C C   . SER A 132 ? 0.6458 0.6944 0.6747 0.0441  0.0964  -0.0150 147 SER A C   
1051 O O   . SER A 132 ? 0.6070 0.6403 0.6118 0.0520  0.0841  -0.0199 147 SER A O   
1052 C CB  . SER A 132 ? 0.5977 0.7014 0.6405 0.0631  0.1059  -0.0134 147 SER A CB  
1053 O OG  . SER A 132 ? 0.7522 0.8832 0.7929 0.0782  0.1202  -0.0041 147 SER A OG  
1054 N N   . ASN A 133 ? 0.6310 0.6770 0.6841 0.0250  0.0959  -0.0204 148 ASN A N   
1055 C CA  . ASN A 133 ? 0.6093 0.6348 0.6583 0.0140  0.0818  -0.0315 148 ASN A CA  
1056 C C   . ASN A 133 ? 0.5953 0.5923 0.6268 0.0144  0.0861  -0.0249 148 ASN A C   
1057 O O   . ASN A 133 ? 0.5396 0.5225 0.5518 0.0174  0.0727  -0.0308 148 ASN A O   
1058 C CB  . ASN A 133 ? 0.5993 0.6316 0.6783 -0.0063 0.0825  -0.0398 148 ASN A CB  
1059 C CG  . ASN A 133 ? 0.6863 0.7016 0.7592 -0.0169 0.0687  -0.0522 148 ASN A CG  
1060 O OD1 . ASN A 133 ? 0.6861 0.7040 0.7452 -0.0116 0.0513  -0.0598 148 ASN A OD1 
1061 N ND2 . ASN A 133 ? 0.6431 0.6413 0.7271 -0.0311 0.0772  -0.0538 148 ASN A ND2 
1062 N N   . GLN A 134 ? 0.6318 0.6209 0.6713 0.0119  0.1055  -0.0109 149 GLN A N   
1063 C CA  . GLN A 134 ? 0.6792 0.6426 0.7044 0.0143  0.1109  -0.0029 149 GLN A CA  
1064 C C   . GLN A 134 ? 0.6231 0.5869 0.6168 0.0333  0.1031  0.0004  149 GLN A C   
1065 O O   . GLN A 134 ? 0.6184 0.5654 0.5965 0.0348  0.0953  -0.0024 149 GLN A O   
1066 C CB  . GLN A 134 ? 0.7058 0.6617 0.7463 0.0116  0.1347  0.0154  149 GLN A CB  
1067 C CG  . GLN A 134 ? 0.8776 0.8170 0.9476 -0.0093 0.1429  0.0107  149 GLN A CG  
1068 C CD  . GLN A 134 ? 1.0843 1.0227 1.1794 -0.0142 0.1674  0.0292  149 GLN A CD  
1069 O OE1 . GLN A 134 ? 1.1850 1.1281 1.3133 -0.0320 0.1739  0.0240  149 GLN A OE1 
1070 N NE2 . GLN A 134 ? 1.1261 1.0607 1.2066 0.0015  0.1813  0.0518  149 GLN A NE2 
1071 N N   . ASN A 135 ? 0.6366 0.6218 0.6216 0.0480  0.1050  0.0050  150 ASN A N   
1072 C CA  . ASN A 135 ? 0.5687 0.5570 0.5254 0.0660  0.0974  0.0054  150 ASN A CA  
1073 C C   . ASN A 135 ? 0.5328 0.5159 0.4788 0.0660  0.0750  -0.0119 150 ASN A C   
1074 O O   . ASN A 135 ? 0.5469 0.5210 0.4747 0.0722  0.0664  -0.0141 150 ASN A O   
1075 C CB  . ASN A 135 ? 0.6531 0.6684 0.6027 0.0826  0.1053  0.0119  150 ASN A CB  
1076 C CG  . ASN A 135 ? 0.8099 0.8291 0.7547 0.0910  0.1257  0.0341  150 ASN A CG  
1077 O OD1 . ASN A 135 ? 0.8466 0.8614 0.7703 0.1024  0.1249  0.0404  150 ASN A OD1 
1078 N ND2 . ASN A 135 ? 0.8056 0.8342 0.7715 0.0853  0.1443  0.0474  150 ASN A ND2 
1079 N N   . ILE A 136 ? 0.5673 0.5580 0.5259 0.0600  0.0656  -0.0231 151 ILE A N   
1080 C CA  . ILE A 136 ? 0.5440 0.5270 0.4957 0.0590  0.0456  -0.0361 151 ILE A CA  
1081 C C   . ILE A 136 ? 0.5420 0.5042 0.4915 0.0468  0.0408  -0.0372 151 ILE A C   
1082 O O   . ILE A 136 ? 0.5417 0.4938 0.4778 0.0489  0.0288  -0.0415 151 ILE A O   
1083 C CB  . ILE A 136 ? 0.5114 0.5081 0.4790 0.0560  0.0381  -0.0446 151 ILE A CB  
1084 C CG1 . ILE A 136 ? 0.6106 0.6281 0.5767 0.0721  0.0404  -0.0462 151 ILE A CG1 
1085 C CG2 . ILE A 136 ? 0.4562 0.4421 0.4200 0.0524  0.0192  -0.0539 151 ILE A CG2 
1086 C CD1 . ILE A 136 ? 0.5910 0.6245 0.5734 0.0727  0.0336  -0.0539 151 ILE A CD1 
1087 N N   . GLN A 137 ? 0.5308 0.4871 0.4947 0.0337  0.0507  -0.0341 152 GLN A N   
1088 C CA  . GLN A 137 ? 0.5280 0.4668 0.4898 0.0232  0.0469  -0.0374 152 GLN A CA  
1089 C C   . GLN A 137 ? 0.5944 0.5201 0.5392 0.0308  0.0504  -0.0300 152 GLN A C   
1090 O O   . GLN A 137 ? 0.5699 0.4872 0.5037 0.0300  0.0404  -0.0339 152 GLN A O   
1091 C CB  . GLN A 137 ? 0.5728 0.5080 0.5557 0.0082  0.0573  -0.0390 152 GLN A CB  
1092 C CG  . GLN A 137 ? 0.5693 0.4922 0.5515 -0.0032 0.0507  -0.0483 152 GLN A CG  
1093 C CD  . GLN A 137 ? 0.5479 0.4842 0.5325 -0.0088 0.0346  -0.0596 152 GLN A CD  
1094 O OE1 . GLN A 137 ? 0.5792 0.5324 0.5709 -0.0057 0.0297  -0.0610 152 GLN A OE1 
1095 N NE2 . GLN A 137 ? 0.6569 0.5877 0.6350 -0.0153 0.0267  -0.0668 152 GLN A NE2 
1096 N N   . TYR A 138 ? 0.5607 0.4876 0.5036 0.0392  0.0650  -0.0178 153 TYR A N   
1097 C CA  . TYR A 138 ? 0.5667 0.4864 0.4934 0.0494  0.0680  -0.0094 153 TYR A CA  
1098 C C   . TYR A 138 ? 0.5573 0.4845 0.4659 0.0592  0.0522  -0.0159 153 TYR A C   
1099 O O   . TYR A 138 ? 0.5736 0.4937 0.4730 0.0596  0.0453  -0.0175 153 TYR A O   
1100 C CB  . TYR A 138 ? 0.6428 0.5676 0.5693 0.0596  0.0861  0.0074  153 TYR A CB  
1101 C CG  . TYR A 138 ? 0.7185 0.6402 0.6286 0.0726  0.0899  0.0183  153 TYR A CG  
1102 C CD1 . TYR A 138 ? 0.7495 0.6518 0.6636 0.0689  0.0973  0.0242  153 TYR A CD1 
1103 C CD2 . TYR A 138 ? 0.7610 0.7014 0.6520 0.0898  0.0858  0.0215  153 TYR A CD2 
1104 C CE1 . TYR A 138 ? 0.8570 0.7592 0.7572 0.0826  0.1006  0.0353  153 TYR A CE1 
1105 C CE2 . TYR A 138 ? 0.7525 0.6954 0.6288 0.1026  0.0882  0.0313  153 TYR A CE2 
1106 C CZ  . TYR A 138 ? 0.8688 0.7930 0.7503 0.0993  0.0957  0.0394  153 TYR A CZ  
1107 O OH  . TYR A 138 ? 0.9005 0.8298 0.7685 0.1138  0.0977  0.0500  153 TYR A OH  
1108 N N   . PHE A 139 ? 0.6161 0.5582 0.5220 0.0666  0.0461  -0.0212 154 PHE A N   
1109 C CA  . PHE A 139 ? 0.6135 0.5612 0.5050 0.0762  0.0317  -0.0295 154 PHE A CA  
1110 C C   . PHE A 139 ? 0.6066 0.5430 0.5004 0.0664  0.0158  -0.0395 154 PHE A C   
1111 O O   . PHE A 139 ? 0.6220 0.5547 0.5073 0.0678  0.0072  -0.0421 154 PHE A O   
1112 C CB  . PHE A 139 ? 0.5962 0.5614 0.4854 0.0877  0.0297  -0.0351 154 PHE A CB  
1113 C CG  . PHE A 139 ? 0.6196 0.5864 0.4993 0.0947  0.0128  -0.0488 154 PHE A CG  
1114 C CD1 . PHE A 139 ? 0.6004 0.5755 0.4646 0.1058  0.0097  -0.0505 154 PHE A CD1 
1115 C CD2 . PHE A 139 ? 0.5774 0.5373 0.4656 0.0898  -0.0002 -0.0598 154 PHE A CD2 
1116 C CE1 . PHE A 139 ? 0.6249 0.6004 0.4845 0.1099  -0.0065 -0.0658 154 PHE A CE1 
1117 C CE2 . PHE A 139 ? 0.5944 0.5509 0.4780 0.0947  -0.0151 -0.0723 154 PHE A CE2 
1118 C CZ  . PHE A 139 ? 0.6014 0.5652 0.4718 0.1037  -0.0184 -0.0767 154 PHE A CZ  
1119 N N   . LEU A 140 ? 0.5717 0.5054 0.4778 0.0567  0.0118  -0.0440 155 LEU A N   
1120 C CA  . LEU A 140 ? 0.6206 0.5462 0.5280 0.0496  -0.0030 -0.0505 155 LEU A CA  
1121 C C   . LEU A 140 ? 0.5328 0.4481 0.4379 0.0399  -0.0027 -0.0473 155 LEU A C   
1122 O O   . LEU A 140 ? 0.5601 0.4703 0.4616 0.0370  -0.0132 -0.0492 155 LEU A O   
1123 C CB  . LEU A 140 ? 0.5163 0.4464 0.4364 0.0443  -0.0076 -0.0545 155 LEU A CB  
1124 C CG  . LEU A 140 ? 0.5691 0.5069 0.4919 0.0548  -0.0149 -0.0607 155 LEU A CG  
1125 C CD1 . LEU A 140 ? 0.4706 0.4146 0.4069 0.0509  -0.0209 -0.0633 155 LEU A CD1 
1126 C CD2 . LEU A 140 ? 0.5763 0.5056 0.4906 0.0616  -0.0269 -0.0665 155 LEU A CD2 
1127 N N   . ASP A 141 ? 0.5341 0.4461 0.4432 0.0345  0.0095  -0.0428 156 ASP A N   
1128 C CA  . ASP A 141 ? 0.5445 0.4476 0.4502 0.0283  0.0109  -0.0412 156 ASP A CA  
1129 C C   . ASP A 141 ? 0.5514 0.4546 0.4458 0.0361  0.0078  -0.0380 156 ASP A C   
1130 O O   . ASP A 141 ? 0.5283 0.4298 0.4196 0.0320  -0.0003 -0.0394 156 ASP A O   
1131 C CB  . ASP A 141 ? 0.5329 0.4293 0.4458 0.0241  0.0262  -0.0379 156 ASP A CB  
1132 C CG  . ASP A 141 ? 0.5607 0.4575 0.4864 0.0114  0.0264  -0.0455 156 ASP A CG  
1133 O OD1 . ASP A 141 ? 0.5811 0.4850 0.5071 0.0069  0.0143  -0.0513 156 ASP A OD1 
1134 O OD2 . ASP A 141 ? 0.6168 0.5075 0.5533 0.0062  0.0386  -0.0456 156 ASP A OD2 
1135 N N   . ARG A 142 ? 0.6209 0.5299 0.5096 0.0478  0.0137  -0.0333 157 ARG A N   
1136 C CA  . ARG A 142 ? 0.6213 0.5359 0.4999 0.0563  0.0097  -0.0315 157 ARG A CA  
1137 C C   . ARG A 142 ? 0.5629 0.4821 0.4398 0.0565  -0.0065 -0.0407 157 ARG A C   
1138 O O   . ARG A 142 ? 0.5699 0.4904 0.4456 0.0542  -0.0141 -0.0422 157 ARG A O   
1139 C CB  . ARG A 142 ? 0.5681 0.4922 0.4394 0.0705  0.0200  -0.0236 157 ARG A CB  
1140 C CG  . ARG A 142 ? 0.6128 0.5283 0.4880 0.0710  0.0373  -0.0115 157 ARG A CG  
1141 C CD  . ARG A 142 ? 0.6710 0.5958 0.5418 0.0843  0.0503  0.0003  157 ARG A CD  
1142 N NE  . ARG A 142 ? 0.6547 0.5971 0.5102 0.1002  0.0464  0.0036  157 ARG A NE  
1143 C CZ  . ARG A 142 ? 0.6891 0.6338 0.5388 0.1078  0.0494  0.0119  157 ARG A CZ  
1144 N NH1 . ARG A 142 ? 0.6321 0.5596 0.4897 0.1020  0.0576  0.0177  157 ARG A NH1 
1145 N NH2 . ARG A 142 ? 0.7497 0.7161 0.5857 0.1223  0.0434  0.0126  157 ARG A NH2 
1146 N N   . PHE A 143 ? 0.5690 0.4903 0.4487 0.0588  -0.0118 -0.0471 158 PHE A N   
1147 C CA  . PHE A 143 ? 0.5212 0.4423 0.4023 0.0594  -0.0268 -0.0570 158 PHE A CA  
1148 C C   . PHE A 143 ? 0.5907 0.5009 0.4794 0.0467  -0.0354 -0.0567 158 PHE A C   
1149 O O   . PHE A 143 ? 0.5922 0.5008 0.4830 0.0438  -0.0449 -0.0600 158 PHE A O   
1150 C CB  . PHE A 143 ? 0.5792 0.5032 0.4633 0.0659  -0.0293 -0.0640 158 PHE A CB  
1151 C CG  . PHE A 143 ? 0.6085 0.5265 0.4976 0.0663  -0.0443 -0.0751 158 PHE A CG  
1152 C CD1 . PHE A 143 ? 0.6284 0.5532 0.5124 0.0751  -0.0514 -0.0858 158 PHE A CD1 
1153 C CD2 . PHE A 143 ? 0.5846 0.4903 0.4843 0.0582  -0.0517 -0.0748 158 PHE A CD2 
1154 C CE1 . PHE A 143 ? 0.6928 0.6083 0.5851 0.0744  -0.0651 -0.0981 158 PHE A CE1 
1155 C CE2 . PHE A 143 ? 0.7155 0.6113 0.6226 0.0588  -0.0644 -0.0832 158 PHE A CE2 
1156 C CZ  . PHE A 143 ? 0.6703 0.5690 0.5751 0.0662  -0.0710 -0.0957 158 PHE A CZ  
1157 N N   . TYR A 144 ? 0.5375 0.4424 0.4312 0.0386  -0.0322 -0.0527 159 TYR A N   
1158 C CA  . TYR A 144 ? 0.5060 0.4046 0.4045 0.0281  -0.0395 -0.0502 159 TYR A CA  
1159 C C   . TYR A 144 ? 0.5739 0.4737 0.4690 0.0226  -0.0366 -0.0452 159 TYR A C   
1160 O O   . TYR A 144 ? 0.5532 0.4514 0.4517 0.0159  -0.0436 -0.0425 159 TYR A O   
1161 C CB  . TYR A 144 ? 0.4678 0.3669 0.3707 0.0226  -0.0372 -0.0485 159 TYR A CB  
1162 C CG  . TYR A 144 ? 0.5594 0.4591 0.4690 0.0271  -0.0433 -0.0522 159 TYR A CG  
1163 C CD1 . TYR A 144 ? 0.5978 0.4913 0.5108 0.0324  -0.0535 -0.0561 159 TYR A CD1 
1164 C CD2 . TYR A 144 ? 0.5634 0.4705 0.4784 0.0260  -0.0391 -0.0530 159 TYR A CD2 
1165 C CE1 . TYR A 144 ? 0.6300 0.5233 0.5501 0.0387  -0.0587 -0.0598 159 TYR A CE1 
1166 C CE2 . TYR A 144 ? 0.5771 0.4882 0.4998 0.0317  -0.0447 -0.0560 159 TYR A CE2 
1167 C CZ  . TYR A 144 ? 0.5968 0.5002 0.5213 0.0390  -0.0541 -0.0590 159 TYR A CZ  
1168 O OH  . TYR A 144 ? 0.5662 0.4728 0.4992 0.0468  -0.0592 -0.0624 159 TYR A OH  
1169 N N   . LEU A 145 ? 0.5228 0.4258 0.4128 0.0256  -0.0253 -0.0426 160 LEU A N   
1170 C CA  . LEU A 145 ? 0.6098 0.5157 0.4972 0.0231  -0.0219 -0.0385 160 LEU A CA  
1171 C C   . LEU A 145 ? 0.5591 0.4723 0.4469 0.0266  -0.0294 -0.0396 160 LEU A C   
1172 O O   . LEU A 145 ? 0.5370 0.4541 0.4284 0.0204  -0.0334 -0.0372 160 LEU A O   
1173 C CB  . LEU A 145 ? 0.5877 0.4926 0.4717 0.0280  -0.0077 -0.0354 160 LEU A CB  
1174 C CG  . LEU A 145 ? 0.6870 0.5925 0.5695 0.0267  -0.0004 -0.0320 160 LEU A CG  
1175 C CD1 . LEU A 145 ? 0.5628 0.4695 0.4468 0.0159  -0.0048 -0.0335 160 LEU A CD1 
1176 C CD2 . LEU A 145 ? 0.7395 0.6364 0.6228 0.0303  0.0142  -0.0303 160 LEU A CD2 
1177 N N   . SER A 146 ? 0.4995 0.4175 0.3841 0.0364  -0.0312 -0.0439 161 SER A N   
1178 C CA  . SER A 146 ? 0.5741 0.5019 0.4605 0.0394  -0.0408 -0.0493 161 SER A CA  
1179 C C   . SER A 146 ? 0.6312 0.5521 0.5291 0.0289  -0.0534 -0.0534 161 SER A C   
1180 O O   . SER A 146 ? 0.5850 0.5120 0.4904 0.0231  -0.0592 -0.0535 161 SER A O   
1181 C CB  . SER A 146 ? 0.5889 0.5249 0.4681 0.0527  -0.0416 -0.0558 161 SER A CB  
1182 O OG  . SER A 146 ? 0.6699 0.6117 0.5538 0.0535  -0.0551 -0.0677 161 SER A OG  
1183 N N   . ARG A 147 ? 0.6155 0.5240 0.5171 0.0264  -0.0571 -0.0553 162 ARG A N   
1184 C CA  . ARG A 147 ? 0.6209 0.5190 0.5350 0.0176  -0.0678 -0.0562 162 ARG A CA  
1185 C C   . ARG A 147 ? 0.5959 0.4943 0.5145 0.0059  -0.0662 -0.0447 162 ARG A C   
1186 O O   . ARG A 147 ? 0.5604 0.4567 0.4910 -0.0024 -0.0731 -0.0426 162 ARG A O   
1187 C CB  . ARG A 147 ? 0.6388 0.5252 0.5553 0.0200  -0.0706 -0.0580 162 ARG A CB  
1188 C CG  . ARG A 147 ? 0.6679 0.5410 0.5971 0.0116  -0.0790 -0.0529 162 ARG A CG  
1189 C CD  . ARG A 147 ? 0.7351 0.6002 0.6659 0.0161  -0.0806 -0.0522 162 ARG A CD  
1190 N NE  . ARG A 147 ? 0.7341 0.5908 0.6727 0.0086  -0.0848 -0.0400 162 ARG A NE  
1191 C CZ  . ARG A 147 ? 0.7714 0.6131 0.7243 0.0053  -0.0933 -0.0379 162 ARG A CZ  
1192 N NH1 . ARG A 147 ? 0.7533 0.5865 0.7152 0.0074  -0.0997 -0.0507 162 ARG A NH1 
1193 N NH2 . ARG A 147 ? 0.7420 0.5777 0.7008 -0.0001 -0.0954 -0.0228 162 ARG A NH2 
1194 N N   . ILE A 148 ? 0.5311 0.4328 0.4414 0.0048  -0.0567 -0.0379 163 ILE A N   
1195 C CA  . ILE A 148 ? 0.4954 0.4021 0.4066 -0.0041 -0.0537 -0.0282 163 ILE A CA  
1196 C C   . ILE A 148 ? 0.6278 0.5467 0.5430 -0.0061 -0.0528 -0.0267 163 ILE A C   
1197 O O   . ILE A 148 ? 0.5051 0.4288 0.4288 -0.0151 -0.0551 -0.0195 163 ILE A O   
1198 C CB  . ILE A 148 ? 0.5669 0.4763 0.4680 -0.0032 -0.0437 -0.0265 163 ILE A CB  
1199 C CG1 . ILE A 148 ? 0.5547 0.4583 0.4556 -0.0047 -0.0469 -0.0259 163 ILE A CG1 
1200 C CG2 . ILE A 148 ? 0.5049 0.4250 0.4033 -0.0087 -0.0380 -0.0200 163 ILE A CG2 
1201 C CD1 . ILE A 148 ? 0.6296 0.5366 0.5238 -0.0037 -0.0382 -0.0296 163 ILE A CD1 
1202 N N   . SER A 149 ? 0.5400 0.4667 0.4501 0.0027  -0.0489 -0.0320 164 SER A N   
1203 C CA  . SER A 149 ? 0.4731 0.4161 0.3879 0.0027  -0.0486 -0.0308 164 SER A CA  
1204 C C   . SER A 149 ? 0.5222 0.4689 0.4520 -0.0031 -0.0609 -0.0360 164 SER A C   
1205 O O   . SER A 149 ? 0.5730 0.5333 0.5140 -0.0100 -0.0626 -0.0326 164 SER A O   
1206 C CB  . SER A 149 ? 0.4926 0.4443 0.3978 0.0161  -0.0415 -0.0333 164 SER A CB  
1207 O OG  . SER A 149 ? 0.5644 0.5190 0.4684 0.0239  -0.0483 -0.0419 164 SER A OG  
1208 N N   . ILE A 150 ? 0.5855 0.5218 0.5178 -0.0005 -0.0693 -0.0456 165 ILE A N   
1209 C CA  . ILE A 150 ? 0.6051 0.5411 0.5549 -0.0074 -0.0817 -0.0537 165 ILE A CA  
1210 C C   . ILE A 150 ? 0.6301 0.5544 0.5955 -0.0222 -0.0846 -0.0436 165 ILE A C   
1211 O O   . ILE A 150 ? 0.6217 0.5534 0.6051 -0.0328 -0.0890 -0.0419 165 ILE A O   
1212 C CB  . ILE A 150 ? 0.6254 0.5524 0.5731 0.0010  -0.0894 -0.0687 165 ILE A CB  
1213 C CG1 . ILE A 150 ? 0.6489 0.5948 0.5822 0.0157  -0.0868 -0.0766 165 ILE A CG1 
1214 C CG2 . ILE A 150 ? 0.5774 0.4960 0.5466 -0.0080 -0.1028 -0.0793 165 ILE A CG2 
1215 C CD1 . ILE A 150 ? 0.6308 0.5730 0.5559 0.0275  -0.0906 -0.0897 165 ILE A CD1 
1216 N N   . ARG A 151 ? 0.6186 0.5276 0.5784 -0.0231 -0.0815 -0.0353 166 ARG A N   
1217 C CA  . ARG A 151 ? 0.6248 0.5249 0.5972 -0.0349 -0.0830 -0.0217 166 ARG A CA  
1218 C C   . ARG A 151 ? 0.5562 0.4747 0.5310 -0.0430 -0.0759 -0.0089 166 ARG A C   
1219 O O   . ARG A 151 ? 0.6385 0.5580 0.6313 -0.0549 -0.0782 0.0003  166 ARG A O   
1220 C CB  . ARG A 151 ? 0.6801 0.5673 0.6428 -0.0315 -0.0808 -0.0144 166 ARG A CB  
1221 C CG  . ARG A 151 ? 0.7900 0.6596 0.7547 -0.0241 -0.0879 -0.0251 166 ARG A CG  
1222 C CD  . ARG A 151 ? 0.8736 0.7337 0.8340 -0.0218 -0.0873 -0.0156 166 ARG A CD  
1223 N NE  . ARG A 151 ? 1.0219 0.8818 0.9889 -0.0313 -0.0864 0.0031  166 ARG A NE  
1224 C CZ  . ARG A 151 ? 1.0478 0.8909 1.0311 -0.0357 -0.0925 0.0124  166 ARG A CZ  
1225 N NH1 . ARG A 151 ? 0.8350 0.6577 0.8308 -0.0315 -0.1007 0.0020  166 ARG A NH1 
1226 N NH2 . ARG A 151 ? 1.0203 0.8673 1.0076 -0.0435 -0.0896 0.0331  166 ARG A NH2 
1227 N N   . MET A 152 ? 0.5710 0.5040 0.5295 -0.0366 -0.0663 -0.0079 167 MET A N   
1228 C CA  . MET A 152 ? 0.5905 0.5439 0.5503 -0.0415 -0.0586 0.0019  167 MET A CA  
1229 C C   . MET A 152 ? 0.6650 0.6334 0.6447 -0.0483 -0.0631 0.0000  167 MET A C   
1230 O O   . MET A 152 ? 0.6013 0.5797 0.5957 -0.0596 -0.0617 0.0115  167 MET A O   
1231 C CB  . MET A 152 ? 0.5575 0.5208 0.4990 -0.0308 -0.0483 -0.0015 167 MET A CB  
1232 C CG  . MET A 152 ? 0.5303 0.5159 0.4720 -0.0326 -0.0393 0.0059  167 MET A CG  
1233 S SD  . MET A 152 ? 0.6395 0.6289 0.5749 -0.0397 -0.0335 0.0198  167 MET A SD  
1234 C CE  . MET A 152 ? 0.6296 0.6498 0.5679 -0.0399 -0.0231 0.0257  167 MET A CE  
1235 N N   . LEU A 153 ? 0.5895 0.5631 0.5702 -0.0412 -0.0683 -0.0141 168 LEU A N   
1236 C CA  . LEU A 153 ? 0.5686 0.5613 0.5692 -0.0472 -0.0744 -0.0191 168 LEU A CA  
1237 C C   . LEU A 153 ? 0.5939 0.5756 0.6206 -0.0634 -0.0831 -0.0170 168 LEU A C   
1238 O O   . LEU A 153 ? 0.5755 0.5729 0.6232 -0.0757 -0.0829 -0.0099 168 LEU A O   
1239 C CB  . LEU A 153 ? 0.5341 0.5347 0.5294 -0.0353 -0.0807 -0.0361 168 LEU A CB  
1240 C CG  . LEU A 153 ? 0.6531 0.6675 0.6277 -0.0188 -0.0716 -0.0360 168 LEU A CG  
1241 C CD1 . LEU A 153 ? 0.5954 0.6255 0.5676 -0.0074 -0.0787 -0.0495 168 LEU A CD1 
1242 C CD2 . LEU A 153 ? 0.5748 0.6102 0.5522 -0.0200 -0.0622 -0.0250 168 LEU A CD2 
1243 N N   . ILE A 154 ? 0.5742 0.5286 0.6021 -0.0635 -0.0900 -0.0224 169 ILE A N   
1244 C CA  . ILE A 154 ? 0.6468 0.5848 0.7020 -0.0778 -0.0984 -0.0214 169 ILE A CA  
1245 C C   . ILE A 154 ? 0.6467 0.5827 0.7110 -0.0897 -0.0909 0.0029  169 ILE A C   
1246 O O   . ILE A 154 ? 0.6147 0.5555 0.7063 -0.1050 -0.0924 0.0105  169 ILE A O   
1247 C CB  . ILE A 154 ? 0.6214 0.5294 0.6747 -0.0720 -0.1064 -0.0328 169 ILE A CB  
1248 C CG1 . ILE A 154 ? 0.6541 0.5689 0.7028 -0.0617 -0.1149 -0.0580 169 ILE A CG1 
1249 C CG2 . ILE A 154 ? 0.6701 0.5537 0.7521 -0.0859 -0.1126 -0.0271 169 ILE A CG2 
1250 C CD1 . ILE A 154 ? 0.6689 0.5585 0.7124 -0.0528 -0.1212 -0.0708 169 ILE A CD1 
1251 N N   . ASN A 155 ? 0.6189 0.5511 0.6610 -0.0830 -0.0825 0.0157  170 ASN A N   
1252 C CA  . ASN A 155 ? 0.7003 0.6357 0.7463 -0.0918 -0.0750 0.0397  170 ASN A CA  
1253 C C   . ASN A 155 ? 0.6069 0.5733 0.6632 -0.1001 -0.0676 0.0491  170 ASN A C   
1254 O O   . ASN A 155 ? 0.6920 0.6624 0.7687 -0.1136 -0.0649 0.0665  170 ASN A O   
1255 C CB  . ASN A 155 ? 0.7086 0.6423 0.7261 -0.0814 -0.0681 0.0475  170 ASN A CB  
1256 C CG  . ASN A 155 ? 0.7200 0.6256 0.7336 -0.0759 -0.0747 0.0461  170 ASN A CG  
1257 O OD1 . ASN A 155 ? 0.8175 0.7018 0.8513 -0.0811 -0.0827 0.0449  170 ASN A OD1 
1258 N ND2 . ASN A 155 ? 0.7081 0.6144 0.6978 -0.0654 -0.0711 0.0451  170 ASN A ND2 
1259 N N   . GLN A 156 ? 0.5807 0.5702 0.6248 -0.0917 -0.0634 0.0391  171 GLN A N   
1260 C CA  . GLN A 156 ? 0.6394 0.6618 0.6942 -0.0976 -0.0559 0.0475  171 GLN A CA  
1261 C C   . GLN A 156 ? 0.6918 0.7218 0.7831 -0.1135 -0.0630 0.0463  171 GLN A C   
1262 O O   . GLN A 156 ? 0.6366 0.6861 0.7470 -0.1257 -0.0569 0.0620  171 GLN A O   
1263 C CB  . GLN A 156 ? 0.6066 0.6500 0.6441 -0.0835 -0.0508 0.0362  171 GLN A CB  
1264 C CG  . GLN A 156 ? 0.6258 0.6691 0.6338 -0.0718 -0.0401 0.0403  171 GLN A CG  
1265 C CD  . GLN A 156 ? 0.6578 0.7137 0.6645 -0.0785 -0.0308 0.0594  171 GLN A CD  
1266 O OE1 . GLN A 156 ? 0.6481 0.6890 0.6456 -0.0802 -0.0306 0.0684  171 GLN A OE1 
1267 N NE2 . GLN A 156 ? 0.5958 0.6831 0.6120 -0.0814 -0.0229 0.0665  171 GLN A NE2 
1268 N N   . HIS A 157 ? 0.6421 0.6588 0.7448 -0.1139 -0.0757 0.0271  172 HIS A N   
1269 C CA  . HIS A 157 ? 0.6343 0.6590 0.7746 -0.1302 -0.0839 0.0216  172 HIS A CA  
1270 C C   . HIS A 157 ? 0.6625 0.6627 0.8286 -0.1475 -0.0848 0.0373  172 HIS A C   
1271 O O   . HIS A 157 ? 0.6741 0.6891 0.8701 -0.1644 -0.0813 0.0506  172 HIS A O   
1272 C CB  . HIS A 157 ? 0.6319 0.6522 0.7758 -0.1247 -0.0981 -0.0065 172 HIS A CB  
1273 C CG  . HIS A 157 ? 0.6700 0.7030 0.8535 -0.1414 -0.1084 -0.0177 172 HIS A CG  
1274 N ND1 . HIS A 157 ? 0.6276 0.7017 0.8232 -0.1425 -0.1103 -0.0257 172 HIS A ND1 
1275 C CD2 . HIS A 157 ? 0.6892 0.6999 0.9057 -0.1581 -0.1173 -0.0227 172 HIS A CD2 
1276 C CE1 . HIS A 157 ? 0.6811 0.7603 0.9158 -0.1604 -0.1208 -0.0366 172 HIS A CE1 
1277 N NE2 . HIS A 157 ? 0.6699 0.7088 0.9186 -0.1707 -0.1249 -0.0355 172 HIS A NE2 
1278 N N   . THR A 158 ? 0.6039 0.5673 0.7608 -0.1431 -0.0885 0.0377  173 THR A N   
1279 C CA  . THR A 158 ? 0.6828 0.6188 0.8670 -0.1578 -0.0901 0.0525  173 THR A CA  
1280 C C   . THR A 158 ? 0.7555 0.7024 0.9398 -0.1646 -0.0763 0.0861  173 THR A C   
1281 O O   . THR A 158 ? 0.7435 0.6832 0.9600 -0.1816 -0.0742 0.1036  173 THR A O   
1282 C CB  . THR A 158 ? 0.6936 0.5893 0.8679 -0.1485 -0.0973 0.0453  173 THR A CB  
1283 O OG1 . THR A 158 ? 0.7471 0.6431 0.8836 -0.1322 -0.0906 0.0533  173 THR A OG1 
1284 C CG2 . THR A 158 ? 0.6842 0.5716 0.8600 -0.1418 -0.1108 0.0115  173 THR A CG2 
1285 N N   . LEU A 159 ? 0.6611 0.6269 0.8111 -0.1518 -0.0663 0.0952  174 LEU A N   
1286 C CA  . LEU A 159 ? 0.6830 0.6655 0.8284 -0.1557 -0.0530 0.1252  174 LEU A CA  
1287 C C   . LEU A 159 ? 0.7526 0.7729 0.9191 -0.1678 -0.0448 0.1343  174 LEU A C   
1288 O O   . LEU A 159 ? 0.8006 0.8301 0.9851 -0.1802 -0.0361 0.1609  174 LEU A O   
1289 C CB  . LEU A 159 ? 0.6572 0.6497 0.7599 -0.1380 -0.0460 0.1270  174 LEU A CB  
1290 C CG  . LEU A 159 ? 0.6922 0.6542 0.7744 -0.1267 -0.0514 0.1247  174 LEU A CG  
1291 C CD1 . LEU A 159 ? 0.6783 0.6545 0.7221 -0.1108 -0.0457 0.1196  174 LEU A CD1 
1292 C CD2 . LEU A 159 ? 0.7843 0.7284 0.8790 -0.1335 -0.0501 0.1515  174 LEU A CD2 
1293 N N   . ILE A 160 ? 0.6606 0.7056 0.8259 -0.1636 -0.0468 0.1146  175 ILE A N   
1294 C CA  . ILE A 160 ? 0.6723 0.7580 0.8585 -0.1733 -0.0392 0.1223  175 ILE A CA  
1295 C C   . ILE A 160 ? 0.7582 0.8415 0.9932 -0.1954 -0.0462 0.1217  175 ILE A C   
1296 O O   . ILE A 160 ? 0.7524 0.8541 1.0152 -0.2116 -0.0376 0.1434  175 ILE A O   
1297 C CB  . ILE A 160 ? 0.7430 0.8576 0.9114 -0.1587 -0.0385 0.1030  175 ILE A CB  
1298 C CG1 . ILE A 160 ? 0.7421 0.8636 0.8690 -0.1405 -0.0277 0.1077  175 ILE A CG1 
1299 C CG2 . ILE A 160 ? 0.7744 0.9317 0.9720 -0.1689 -0.0344 0.1059  175 ILE A CG2 
1300 C CD1 . ILE A 160 ? 0.7706 0.9044 0.8768 -0.1229 -0.0284 0.0871  175 ILE A CD1 
1301 N N   . PHE A 161 ? 0.8385 0.7344 0.9618 -0.2852 -0.0307 -0.0033 176 PHE A N   
1302 C CA  . PHE A 161 ? 0.9485 0.8357 1.0862 -0.3115 -0.0479 -0.0118 176 PHE A CA  
1303 C C   . PHE A 161 ? 0.9286 0.7582 1.0352 -0.3209 -0.0448 -0.0193 176 PHE A C   
1304 O O   . PHE A 161 ? 1.0615 0.8667 1.1550 -0.3350 -0.0631 -0.0341 176 PHE A O   
1305 C CB  . PHE A 161 ? 0.8565 0.7572 0.9882 -0.3136 -0.0766 -0.0236 176 PHE A CB  
1306 C CG  . PHE A 161 ? 0.8512 0.8048 1.0165 -0.3038 -0.0838 -0.0153 176 PHE A CG  
1307 C CD1 . PHE A 161 ? 0.8603 0.8596 1.0884 -0.3165 -0.0861 -0.0083 176 PHE A CD1 
1308 C CD2 . PHE A 161 ? 0.7694 0.7270 0.9067 -0.2818 -0.0876 -0.0145 176 PHE A CD2 
1309 C CE1 . PHE A 161 ? 0.8250 0.8722 1.0891 -0.3046 -0.0937 -0.0020 176 PHE A CE1 
1310 C CE2 . PHE A 161 ? 0.8234 0.8244 0.9922 -0.2716 -0.0962 -0.0063 176 PHE A CE2 
1311 C CZ  . PHE A 161 ? 0.8322 0.8777 1.0656 -0.2816 -0.1001 -0.0007 176 PHE A CZ  
1312 N N   . ASP A 162 ? 1.1479 0.9530 1.2412 -0.3124 -0.0235 -0.0097 177 ASP A N   
1313 C CA  . ASP A 162 ? 1.3252 1.0799 1.4054 -0.3257 -0.0196 -0.0103 177 ASP A CA  
1314 C C   . ASP A 162 ? 1.3106 1.0707 1.4140 -0.3375 0.0000  0.0098  177 ASP A C   
1315 O O   . ASP A 162 ? 1.2740 1.0128 1.3899 -0.3628 -0.0010 0.0129  177 ASP A O   
1316 C CB  . ASP A 162 ? 1.4901 1.1964 1.5239 -0.3046 -0.0158 -0.0186 177 ASP A CB  
1317 C CG  . ASP A 162 ? 1.6843 1.3318 1.7018 -0.3176 -0.0225 -0.0282 177 ASP A CG  
1318 O OD1 . ASP A 162 ? 1.6806 1.3095 1.7122 -0.3352 -0.0163 -0.0154 177 ASP A OD1 
1319 O OD2 . ASP A 162 ? 1.6838 1.3023 1.6736 -0.3113 -0.0336 -0.0491 177 ASP A OD2 
1320 N N   . GLY A 163 ? 1.1572 0.9445 1.2648 -0.3216 0.0180  0.0231  178 GLY A N   
1321 C CA  . GLY A 163 ? 1.2455 1.0462 1.3731 -0.3334 0.0390  0.0416  178 GLY A CA  
1322 C C   . GLY A 163 ? 1.2391 1.0833 1.4195 -0.3601 0.0390  0.0442  178 GLY A C   
1323 O O   . GLY A 163 ? 1.2956 1.1307 1.4905 -0.3850 0.0498  0.0545  178 GLY A O   
1324 N N   . PRO A 170 ? 1.3014 1.4539 1.6217 -0.2741 0.1991  0.0742  185 PRO A N   
1325 C CA  . PRO A 170 ? 1.2596 1.3693 1.5304 -0.2531 0.1780  0.0734  185 PRO A CA  
1326 C C   . PRO A 170 ? 1.1932 1.3100 1.4483 -0.2246 0.1840  0.0693  185 PRO A C   
1327 O O   . PRO A 170 ? 1.1795 1.3292 1.4688 -0.2088 0.1745  0.0604  185 PRO A O   
1328 C CB  . PRO A 170 ? 1.2221 1.3414 1.5202 -0.2523 0.1467  0.0650  185 PRO A CB  
1329 C CG  . PRO A 170 ? 1.2961 1.4773 1.6674 -0.2599 0.1497  0.0591  185 PRO A CG  
1330 C CD  . PRO A 170 ? 1.3209 1.5271 1.7094 -0.2711 0.1861  0.0634  185 PRO A CD  
1331 N N   . LYS A 171 ? 0.9830 1.0670 1.1867 -0.2188 0.1977  0.0761  186 LYS A N   
1332 C CA  . LYS A 171 ? 0.7787 0.8643 0.9635 -0.1935 0.2016  0.0715  186 LYS A CA  
1333 C C   . LYS A 171 ? 0.7782 0.8448 0.9471 -0.1741 0.1748  0.0668  186 LYS A C   
1334 O O   . LYS A 171 ? 0.8802 0.9642 1.0608 -0.1546 0.1698  0.0598  186 LYS A O   
1335 C CB  . LYS A 171 ? 0.8085 0.8625 0.9399 -0.1945 0.2202  0.0802  186 LYS A CB  
1336 C CG  . LYS A 171 ? 0.8973 0.9692 1.0361 -0.2155 0.2511  0.0856  186 LYS A CG  
1337 C CD  . LYS A 171 ? 1.1241 1.1528 1.1984 -0.2220 0.2640  0.0986  186 LYS A CD  
1338 C CE  . LYS A 171 ? 1.0702 1.0590 1.1210 -0.2421 0.2543  0.1132  186 LYS A CE  
1339 N NZ  . LYS A 171 ? 1.1024 1.1059 1.1606 -0.2617 0.2695  0.1219  186 LYS A NZ  
1340 N N   . HIS A 172 ? 0.7243 0.7545 0.8668 -0.1797 0.1585  0.0701  187 HIS A N   
1341 C CA  . HIS A 172 ? 0.7146 0.7279 0.8419 -0.1654 0.1355  0.0648  187 HIS A CA  
1342 C C   . HIS A 172 ? 0.7198 0.7466 0.8765 -0.1751 0.1161  0.0594  187 HIS A C   
1343 O O   . HIS A 172 ? 0.7671 0.8008 0.9457 -0.1957 0.1172  0.0610  187 HIS A O   
1344 C CB  . HIS A 172 ? 0.7340 0.6983 0.8127 -0.1631 0.1308  0.0689  187 HIS A CB  
1345 C CG  . HIS A 172 ? 0.7456 0.6942 0.7916 -0.1500 0.1419  0.0733  187 HIS A CG  
1346 N ND1 . HIS A 172 ? 0.7213 0.6492 0.7402 -0.1326 0.1321  0.0705  187 HIS A ND1 
1347 C CD2 . HIS A 172 ? 0.7035 0.6544 0.7383 -0.1532 0.1614  0.0797  187 HIS A CD2 
1348 C CE1 . HIS A 172 ? 0.7245 0.6427 0.7192 -0.1251 0.1424  0.0751  187 HIS A CE1 
1349 N NE2 . HIS A 172 ? 0.7254 0.6553 0.7253 -0.1373 0.1601  0.0807  187 HIS A NE2 
1350 N N   . ILE A 173 ? 0.6731 0.7027 0.8284 -0.1618 0.0976  0.0535  188 ILE A N   
1351 C CA  . ILE A 173 ? 0.6242 0.6629 0.7982 -0.1700 0.0753  0.0483  188 ILE A CA  
1352 C C   . ILE A 173 ? 0.6572 0.6580 0.7878 -0.1655 0.0615  0.0442  188 ILE A C   
1353 O O   . ILE A 173 ? 0.6004 0.5987 0.7149 -0.1509 0.0527  0.0417  188 ILE A O   
1354 C CB  . ILE A 173 ? 0.7337 0.8109 0.9452 -0.1600 0.0639  0.0455  188 ILE A CB  
1355 C CG1 . ILE A 173 ? 0.5945 0.7125 0.8547 -0.1626 0.0812  0.0464  188 ILE A CG1 
1356 C CG2 . ILE A 173 ? 0.7018 0.7848 0.9259 -0.1694 0.0369  0.0412  188 ILE A CG2 
1357 C CD1 . ILE A 173 ? 0.7408 0.8727 1.0307 -0.1874 0.0875  0.0474  188 ILE A CD1 
1358 N N   . GLY A 174 ? 0.6585 0.6288 0.7705 -0.1788 0.0605  0.0429  189 GLY A N   
1359 C CA  . GLY A 174 ? 0.6779 0.6115 0.7500 -0.1730 0.0520  0.0366  189 GLY A CA  
1360 C C   . GLY A 174 ? 0.6587 0.5772 0.7041 -0.1544 0.0634  0.0396  189 GLY A C   
1361 O O   . GLY A 174 ? 0.6769 0.5863 0.7168 -0.1536 0.0778  0.0471  189 GLY A O   
1362 N N   . SER A 175 ? 0.5694 0.4858 0.5973 -0.1408 0.0565  0.0345  190 SER A N   
1363 C CA  . SER A 175 ? 0.6201 0.5255 0.6269 -0.1239 0.0647  0.0359  190 SER A CA  
1364 C C   . SER A 175 ? 0.6621 0.5934 0.6822 -0.1126 0.0705  0.0412  190 SER A C   
1365 O O   . SER A 175 ? 0.6238 0.5486 0.6285 -0.0994 0.0752  0.0417  190 SER A O   
1366 C CB  . SER A 175 ? 0.6269 0.5165 0.6088 -0.1172 0.0571  0.0266  190 SER A CB  
1367 O OG  . SER A 175 ? 0.7884 0.6981 0.7735 -0.1142 0.0482  0.0258  190 SER A OG  
1368 N N   . ILE A 176 ? 0.6178 0.5784 0.6693 -0.1172 0.0699  0.0439  191 ILE A N   
1369 C CA  . ILE A 176 ? 0.5993 0.5840 0.6680 -0.1053 0.0745  0.0464  191 ILE A CA  
1370 C C   . ILE A 176 ? 0.6211 0.6170 0.7039 -0.1077 0.0931  0.0504  191 ILE A C   
1371 O O   . ILE A 176 ? 0.6033 0.6060 0.7025 -0.1227 0.0988  0.0524  191 ILE A O   
1372 C CB  . ILE A 176 ? 0.6280 0.6391 0.7257 -0.1054 0.0595  0.0453  191 ILE A CB  
1373 C CG1 . ILE A 176 ? 0.6091 0.6058 0.6824 -0.1040 0.0420  0.0428  191 ILE A CG1 
1374 C CG2 . ILE A 176 ? 0.5371 0.5710 0.6581 -0.0918 0.0644  0.0468  191 ILE A CG2 
1375 C CD1 . ILE A 176 ? 0.6297 0.6453 0.7248 -0.1094 0.0222  0.0429  191 ILE A CD1 
1376 N N   . ASP A 177 ? 0.5465 0.5432 0.6207 -0.0949 0.1031  0.0512  192 ASP A N   
1377 C CA  . ASP A 177 ? 0.5856 0.5946 0.6684 -0.0964 0.1225  0.0532  192 ASP A CA  
1378 C C   . ASP A 177 ? 0.4916 0.5311 0.6059 -0.0851 0.1243  0.0484  192 ASP A C   
1379 O O   . ASP A 177 ? 0.4961 0.5302 0.6007 -0.0704 0.1188  0.0460  192 ASP A O   
1380 C CB  . ASP A 177 ? 0.6207 0.6029 0.6646 -0.0906 0.1316  0.0563  192 ASP A CB  
1381 C CG  . ASP A 177 ? 0.6346 0.6238 0.6752 -0.0948 0.1527  0.0589  192 ASP A CG  
1382 O OD1 . ASP A 177 ? 0.5511 0.5709 0.6246 -0.1000 0.1636  0.0563  192 ASP A OD1 
1383 O OD2 . ASP A 177 ? 0.6237 0.5882 0.6282 -0.0932 0.1582  0.0633  192 ASP A OD2 
1384 N N   . PRO A 178 ? 0.4865 0.5587 0.6426 -0.0910 0.1306  0.0463  193 PRO A N   
1385 C CA  . PRO A 178 ? 0.5278 0.6290 0.7195 -0.0772 0.1316  0.0401  193 PRO A CA  
1386 C C   . PRO A 178 ? 0.5496 0.6504 0.7293 -0.0670 0.1521  0.0355  193 PRO A C   
1387 O O   . PRO A 178 ? 0.5368 0.6549 0.7413 -0.0525 0.1529  0.0283  193 PRO A O   
1388 C CB  . PRO A 178 ? 0.4795 0.6182 0.7238 -0.0880 0.1340  0.0380  193 PRO A CB  
1389 C CG  . PRO A 178 ? 0.5701 0.6989 0.7993 -0.1089 0.1469  0.0433  193 PRO A CG  
1390 C CD  . PRO A 178 ? 0.5075 0.5926 0.6853 -0.1107 0.1357  0.0487  193 PRO A CD  
1391 N N   . ASN A 179 ? 0.5633 0.6423 0.7038 -0.0739 0.1668  0.0393  194 ASN A N   
1392 C CA  . ASN A 179 ? 0.5441 0.6181 0.6626 -0.0667 0.1856  0.0349  194 ASN A CA  
1393 C C   . ASN A 179 ? 0.6324 0.6669 0.6963 -0.0656 0.1810  0.0407  194 ASN A C   
1394 O O   . ASN A 179 ? 0.6183 0.6376 0.6500 -0.0731 0.1944  0.0450  194 ASN A O   
1395 C CB  . ASN A 179 ? 0.5539 0.6483 0.6833 -0.0794 0.2123  0.0338  194 ASN A CB  
1396 C CG  . ASN A 179 ? 0.7796 0.9120 0.9537 -0.0694 0.2258  0.0209  194 ASN A CG  
1397 O OD1 . ASN A 179 ? 0.7810 0.9101 0.9431 -0.0552 0.2340  0.0118  194 ASN A OD1 
1398 N ND2 . ASN A 179 ? 0.7903 0.9593 1.0193 -0.0758 0.2270  0.0186  194 ASN A ND2 
1399 N N   . CYS A 180 ? 0.5367 0.5548 0.5905 -0.0570 0.1611  0.0415  195 CYS A N   
1400 C CA  . CYS A 180 ? 0.5635 0.5490 0.5754 -0.0545 0.1541  0.0456  195 CYS A CA  
1401 C C   . CYS A 180 ? 0.6925 0.6703 0.6822 -0.0442 0.1613  0.0405  195 CYS A C   
1402 O O   . CYS A 180 ? 0.5860 0.5704 0.5874 -0.0321 0.1566  0.0332  195 CYS A O   
1403 C CB  . CYS A 180 ? 0.5337 0.5104 0.5469 -0.0491 0.1342  0.0458  195 CYS A CB  
1404 S SG  . CYS A 180 ? 0.6241 0.5692 0.5983 -0.0430 0.1262  0.0476  195 CYS A SG  
1405 N N   . ASN A 181 ? 0.5852 0.5459 0.5403 -0.0497 0.1710  0.0446  196 ASN A N   
1406 C CA  . ASN A 181 ? 0.6321 0.5810 0.5576 -0.0417 0.1753  0.0395  196 ASN A CA  
1407 C C   . ASN A 181 ? 0.6272 0.5540 0.5345 -0.0337 0.1556  0.0409  196 ASN A C   
1408 O O   . ASN A 181 ? 0.6260 0.5322 0.5122 -0.0377 0.1473  0.0491  196 ASN A O   
1409 C CB  . ASN A 181 ? 0.6746 0.6117 0.5647 -0.0526 0.1911  0.0451  196 ASN A CB  
1410 C CG  . ASN A 181 ? 0.7827 0.7044 0.6338 -0.0461 0.1940  0.0395  196 ASN A CG  
1411 O OD1 . ASN A 181 ? 0.7469 0.6542 0.5864 -0.0361 0.1774  0.0367  196 ASN A OD1 
1412 N ND2 . ASN A 181 ? 0.9976 0.9223 0.8269 -0.0536 0.2155  0.0375  196 ASN A ND2 
1413 N N   . VAL A 182 ? 0.5684 0.4997 0.4872 -0.0224 0.1479  0.0328  197 VAL A N   
1414 C CA  . VAL A 182 ? 0.5521 0.4695 0.4644 -0.0171 0.1305  0.0339  197 VAL A CA  
1415 C C   . VAL A 182 ? 0.6398 0.5350 0.5161 -0.0162 0.1252  0.0361  197 VAL A C   
1416 O O   . VAL A 182 ? 0.5861 0.4687 0.4556 -0.0164 0.1135  0.0413  197 VAL A O   
1417 C CB  . VAL A 182 ? 0.6651 0.5902 0.5972 -0.0082 0.1240  0.0264  197 VAL A CB  
1418 C CG1 . VAL A 182 ? 0.4841 0.3967 0.4088 -0.0050 0.1091  0.0269  197 VAL A CG1 
1419 C CG2 . VAL A 182 ? 0.6195 0.5627 0.5852 -0.0094 0.1228  0.0278  197 VAL A CG2 
1420 N N   . SER A 183 ? 0.5955 0.4854 0.4481 -0.0149 0.1331  0.0312  198 SER A N   
1421 C CA  . SER A 183 ? 0.5907 0.4584 0.4059 -0.0142 0.1242  0.0335  198 SER A CA  
1422 C C   . SER A 183 ? 0.6496 0.5003 0.4437 -0.0219 0.1213  0.0469  198 SER A C   
1423 O O   . SER A 183 ? 0.6478 0.4795 0.4227 -0.0192 0.1055  0.0517  198 SER A O   
1424 C CB  . SER A 183 ? 0.6754 0.5389 0.4622 -0.0136 0.1349  0.0250  198 SER A CB  
1425 O OG  . SER A 183 ? 0.8088 0.6785 0.6112 -0.0046 0.1309  0.0120  198 SER A OG  
1426 N N   . GLU A 184 ? 0.6674 0.5236 0.4668 -0.0316 0.1350  0.0532  199 GLU A N   
1427 C CA  . GLU A 184 ? 0.7067 0.5424 0.4874 -0.0403 0.1318  0.0669  199 GLU A CA  
1428 C C   . GLU A 184 ? 0.6612 0.4899 0.4614 -0.0356 0.1145  0.0696  199 GLU A C   
1429 O O   . GLU A 184 ? 0.6753 0.4799 0.4575 -0.0343 0.1013  0.0773  199 GLU A O   
1430 C CB  . GLU A 184 ? 0.7297 0.5757 0.5178 -0.0541 0.1514  0.0718  199 GLU A CB  
1431 C CG  . GLU A 184 ? 0.8500 0.6738 0.6266 -0.0655 0.1480  0.0862  199 GLU A CG  
1432 C CD  . GLU A 184 ? 1.0705 0.8614 0.7957 -0.0712 0.1453  0.0986  199 GLU A CD  
1433 O OE1 . GLU A 184 ? 1.1036 0.8928 0.7991 -0.0691 0.1502  0.0951  199 GLU A OE1 
1434 O OE2 . GLU A 184 ? 1.0315 0.7956 0.7438 -0.0780 0.1369  0.1118  199 GLU A OE2 
1435 N N   . VAL A 185 ? 0.5837 0.4324 0.4198 -0.0325 0.1141  0.0627  200 VAL A N   
1436 C CA  . VAL A 185 ? 0.6519 0.4960 0.5043 -0.0283 0.1010  0.0622  200 VAL A CA  
1437 C C   . VAL A 185 ? 0.6173 0.4546 0.4647 -0.0175 0.0865  0.0584  200 VAL A C   
1438 O O   . VAL A 185 ? 0.5906 0.4149 0.4392 -0.0132 0.0748  0.0604  200 VAL A O   
1439 C CB  . VAL A 185 ? 0.5920 0.4580 0.4764 -0.0291 0.1037  0.0559  200 VAL A CB  
1440 C CG1 . VAL A 185 ? 0.5396 0.4006 0.4351 -0.0256 0.0931  0.0532  200 VAL A CG1 
1441 C CG2 . VAL A 185 ? 0.6179 0.4929 0.5127 -0.0403 0.1147  0.0593  200 VAL A CG2 
1442 N N   . VAL A 186 ? 0.5808 0.4276 0.4264 -0.0127 0.0867  0.0518  201 VAL A N   
1443 C CA  . VAL A 186 ? 0.6347 0.4764 0.4763 -0.0047 0.0722  0.0480  201 VAL A CA  
1444 C C   . VAL A 186 ? 0.5980 0.4156 0.4115 -0.0035 0.0608  0.0561  201 VAL A C   
1445 O O   . VAL A 186 ? 0.5840 0.3952 0.4060 0.0033  0.0454  0.0565  201 VAL A O   
1446 C CB  . VAL A 186 ? 0.6149 0.4646 0.4527 -0.0022 0.0743  0.0396  201 VAL A CB  
1447 C CG1 . VAL A 186 ? 0.6556 0.4990 0.4877 0.0036  0.0576  0.0358  201 VAL A CG1 
1448 C CG2 . VAL A 186 ? 0.5475 0.4165 0.4153 -0.0018 0.0804  0.0334  201 VAL A CG2 
1449 N N   . LYS A 187 ? 0.6188 0.4226 0.3992 -0.0102 0.0681  0.0632  202 LYS A N   
1450 C CA  . LYS A 187 ? 0.7242 0.4999 0.4701 -0.0103 0.0550  0.0737  202 LYS A CA  
1451 C C   . LYS A 187 ? 0.7070 0.4667 0.4630 -0.0090 0.0457  0.0823  202 LYS A C   
1452 O O   . LYS A 187 ? 0.7422 0.4849 0.4931 -0.0013 0.0256  0.0865  202 LYS A O   
1453 C CB  . LYS A 187 ? 0.7380 0.5006 0.4415 -0.0212 0.0685  0.0810  202 LYS A CB  
1454 C CG  . LYS A 187 ? 0.8243 0.5950 0.5082 -0.0208 0.0756  0.0710  202 LYS A CG  
1455 C CD  . LYS A 187 ? 0.9410 0.6991 0.5795 -0.0329 0.0927  0.0774  202 LYS A CD  
1456 C CE  . LYS A 187 ? 0.8896 0.6623 0.5183 -0.0321 0.1076  0.0621  202 LYS A CE  
1457 N NZ  . LYS A 187 ? 1.0832 0.8447 0.6629 -0.0441 0.1265  0.0658  202 LYS A NZ  
1458 N N   . ASP A 188 ? 0.7238 0.4877 0.4952 -0.0163 0.0586  0.0843  203 ASP A N   
1459 C CA  . ASP A 188 ? 0.7241 0.4698 0.5053 -0.0157 0.0508  0.0900  203 ASP A CA  
1460 C C   . ASP A 188 ? 0.6573 0.4097 0.4688 -0.0017 0.0362  0.0808  203 ASP A C   
1461 O O   . ASP A 188 ? 0.6407 0.3723 0.4523 0.0062  0.0199  0.0848  203 ASP A O   
1462 C CB  . ASP A 188 ? 0.7715 0.5265 0.5706 -0.0261 0.0662  0.0890  203 ASP A CB  
1463 C CG  . ASP A 188 ? 0.8360 0.5896 0.6148 -0.0417 0.0834  0.0974  203 ASP A CG  
1464 O OD1 . ASP A 188 ? 0.7218 0.4602 0.4646 -0.0462 0.0849  0.1062  203 ASP A OD1 
1465 O OD2 . ASP A 188 ? 0.7677 0.5374 0.5676 -0.0504 0.0957  0.0944  203 ASP A OD2 
1466 N N   . ALA A 189 ? 0.6206 0.4022 0.4602 0.0011  0.0426  0.0683  204 ALA A N   
1467 C CA  . ALA A 189 ? 0.5762 0.3695 0.4467 0.0117  0.0340  0.0581  204 ALA A CA  
1468 C C   . ALA A 189 ? 0.5964 0.3858 0.4656 0.0220  0.0158  0.0579  204 ALA A C   
1469 O O   . ALA A 189 ? 0.5722 0.3586 0.4622 0.0323  0.0033  0.0544  204 ALA A O   
1470 C CB  . ALA A 189 ? 0.5729 0.3957 0.4655 0.0093  0.0452  0.0476  204 ALA A CB  
1471 N N   . TYR A 190 ? 0.6012 0.3910 0.4476 0.0197  0.0132  0.0603  205 TYR A N   
1472 C CA  . TYR A 190 ? 0.5745 0.3584 0.4151 0.0277  -0.0075 0.0607  205 TYR A CA  
1473 C C   . TYR A 190 ? 0.6525 0.4051 0.4757 0.0329  -0.0253 0.0727  205 TYR A C   
1474 O O   . TYR A 190 ? 0.6062 0.3573 0.4504 0.0448  -0.0450 0.0707  205 TYR A O   
1475 C CB  . TYR A 190 ? 0.6446 0.4291 0.4550 0.0223  -0.0060 0.0602  205 TYR A CB  
1476 C CG  . TYR A 190 ? 0.6820 0.4517 0.4719 0.0277  -0.0301 0.0636  205 TYR A CG  
1477 C CD1 . TYR A 190 ? 0.6806 0.4671 0.4986 0.0350  -0.0461 0.0542  205 TYR A CD1 
1478 C CD2 . TYR A 190 ? 0.7945 0.5328 0.5367 0.0242  -0.0384 0.0773  205 TYR A CD2 
1479 C CE1 . TYR A 190 ? 0.7101 0.4840 0.5123 0.0401  -0.0725 0.0572  205 TYR A CE1 
1480 C CE2 . TYR A 190 ? 0.8206 0.5424 0.5396 0.0290  -0.0646 0.0817  205 TYR A CE2 
1481 C CZ  . TYR A 190 ? 0.7768 0.5174 0.5276 0.0376  -0.0827 0.0712  205 TYR A CZ  
1482 O OH  . TYR A 190 ? 0.8831 0.6093 0.6147 0.0423  -0.1121 0.0751  205 TYR A OH  
1483 N N   . ASP A 191 ? 0.7389 0.4658 0.5263 0.0238  -0.0187 0.0857  206 ASP A N   
1484 C CA  . ASP A 191 ? 0.7632 0.4532 0.5278 0.0268  -0.0367 0.1004  206 ASP A CA  
1485 C C   . ASP A 191 ? 0.7577 0.4432 0.5614 0.0389  -0.0467 0.0963  206 ASP A C   
1486 O O   . ASP A 191 ? 0.7363 0.4017 0.5430 0.0506  -0.0709 0.1018  206 ASP A O   
1487 C CB  . ASP A 191 ? 0.8191 0.4839 0.5436 0.0113  -0.0230 0.1151  206 ASP A CB  
1488 C CG  . ASP A 191 ? 0.9731 0.6354 0.6520 0.0005  -0.0146 0.1201  206 ASP A CG  
1489 O OD1 . ASP A 191 ? 0.8567 0.5291 0.5293 0.0062  -0.0248 0.1135  206 ASP A OD1 
1490 O OD2 . ASP A 191 ? 0.9975 0.6487 0.6483 -0.0144 0.0031  0.1294  206 ASP A OD2 
1491 N N   . MET A 192 ? 0.6676 0.3704 0.5006 0.0366  -0.0290 0.0861  207 MET A N   
1492 C CA  . MET A 192 ? 0.7562 0.4537 0.6235 0.0471  -0.0342 0.0790  207 MET A CA  
1493 C C   . MET A 192 ? 0.6274 0.3498 0.5368 0.0632  -0.0457 0.0649  207 MET A C   
1494 O O   . MET A 192 ? 0.6781 0.3883 0.6101 0.0775  -0.0619 0.0627  207 MET A O   
1495 C CB  . MET A 192 ? 0.6413 0.3507 0.5225 0.0383  -0.0121 0.0704  207 MET A CB  
1496 C CG  . MET A 192 ? 0.6550 0.3562 0.5661 0.0478  -0.0147 0.0603  207 MET A CG  
1497 S SD  . MET A 192 ? 0.7734 0.4192 0.6627 0.0488  -0.0304 0.0761  207 MET A SD  
1498 C CE  . MET A 192 ? 0.7065 0.3456 0.6381 0.0744  -0.0509 0.0643  207 MET A CE  
1499 N N   . ALA A 193 ? 0.5997 0.3572 0.5231 0.0608  -0.0376 0.0550  208 ALA A N   
1500 C CA  . ALA A 193 ? 0.5585 0.3430 0.5234 0.0728  -0.0475 0.0423  208 ALA A CA  
1501 C C   . ALA A 193 ? 0.5926 0.3633 0.5527 0.0832  -0.0769 0.0499  208 ALA A C   
1502 O O   . ALA A 193 ? 0.6027 0.3812 0.6017 0.0983  -0.0928 0.0429  208 ALA A O   
1503 C CB  . ALA A 193 ? 0.5213 0.3401 0.4955 0.0645  -0.0339 0.0334  208 ALA A CB  
1504 N N   . LYS A 194 ? 0.6451 0.3965 0.5579 0.0752  -0.0845 0.0632  209 LYS A N   
1505 C CA  . LYS A 194 ? 0.7225 0.4541 0.6174 0.0826  -0.1151 0.0732  209 LYS A CA  
1506 C C   . LYS A 194 ? 0.8053 0.5050 0.7061 0.0954  -0.1353 0.0822  209 LYS A C   
1507 O O   . LYS A 194 ? 0.7954 0.4936 0.7189 0.1103  -0.1637 0.0822  209 LYS A O   
1508 C CB  . LYS A 194 ? 0.7822 0.4922 0.6130 0.0686  -0.1135 0.0862  209 LYS A CB  
1509 C CG  . LYS A 194 ? 0.9419 0.6191 0.7323 0.0718  -0.1443 0.1013  209 LYS A CG  
1510 C CD  . LYS A 194 ? 0.8715 0.5332 0.5964 0.0554  -0.1347 0.1097  209 LYS A CD  
1511 C CE  . LYS A 194 ? 1.0178 0.6333 0.6834 0.0526  -0.1564 0.1310  209 LYS A CE  
1512 N NZ  . LYS A 194 ? 1.0356 0.6456 0.7018 0.0640  -0.1950 0.1326  209 LYS A NZ  
1513 N N   . LEU A 195 ? 0.8211 0.4942 0.7047 0.0900  -0.1229 0.0899  210 LEU A N   
1514 C CA  . LEU A 195 ? 0.8294 0.4648 0.7162 0.1014  -0.1422 0.0993  210 LEU A CA  
1515 C C   . LEU A 195 ? 0.7813 0.4379 0.7353 0.1220  -0.1501 0.0814  210 LEU A C   
1516 O O   . LEU A 195 ? 0.7733 0.4107 0.7454 0.1393  -0.1784 0.0854  210 LEU A O   
1517 C CB  . LEU A 195 ? 0.9243 0.5300 0.7842 0.0886  -0.1240 0.1081  210 LEU A CB  
1518 C CG  . LEU A 195 ? 1.0196 0.5688 0.8507 0.0899  -0.1425 0.1281  210 LEU A CG  
1519 C CD1 . LEU A 195 ? 1.0742 0.6025 0.8747 0.0697  -0.1190 0.1366  210 LEU A CD1 
1520 C CD2 . LEU A 195 ? 1.1312 0.6693 1.0106 0.1122  -0.1607 0.1195  210 LEU A CD2 
1521 N N   . LEU A 196 ? 0.7399 0.4364 0.7318 0.1207  -0.1254 0.0612  211 LEU A N   
1522 C CA  . LEU A 196 ? 0.7465 0.4701 0.8032 0.1387  -0.1277 0.0413  211 LEU A CA  
1523 C C   . LEU A 196 ? 0.8155 0.5686 0.9045 0.1490  -0.1486 0.0362  211 LEU A C   
1524 O O   . LEU A 196 ? 0.9082 0.6679 1.0447 0.1689  -0.1677 0.0285  211 LEU A O   
1525 C CB  . LEU A 196 ? 0.6218 0.3786 0.7011 0.1309  -0.0941 0.0226  211 LEU A CB  
1526 C CG  . LEU A 196 ? 0.7703 0.5026 0.8345 0.1247  -0.0766 0.0213  211 LEU A CG  
1527 C CD1 . LEU A 196 ? 0.6524 0.4168 0.7236 0.1123  -0.0458 0.0068  211 LEU A CD1 
1528 C CD2 . LEU A 196 ? 0.7423 0.4534 0.8395 0.1442  -0.0881 0.0127  211 LEU A CD2 
1529 N N   . CYS A 197 ? 0.7760 0.5462 0.8418 0.1361  -0.1466 0.0397  212 CYS A N   
1530 C CA  . CYS A 197 ? 0.8872 0.6856 0.9821 0.1425  -0.1671 0.0342  212 CYS A CA  
1531 C C   . CYS A 197 ? 0.8816 0.6485 0.9603 0.1541  -0.2076 0.0496  212 CYS A C   
1532 O O   . CYS A 197 ? 0.9319 0.7163 1.0599 0.1707  -0.2321 0.0426  212 CYS A O   
1533 C CB  . CYS A 197 ? 0.8276 0.6461 0.8970 0.1243  -0.1541 0.0333  212 CYS A CB  
1534 S SG  . CYS A 197 ? 0.8054 0.6638 0.9163 0.1274  -0.1746 0.0225  212 CYS A SG  
1535 N N   . ASP A 198 ? 0.9432 0.6639 0.9537 0.1452  -0.2154 0.0708  213 ASP A N   
1536 C CA  . ASP A 198 ? 1.0530 0.7338 1.0370 0.1547  -0.2545 0.0893  213 ASP A CA  
1537 C C   . ASP A 198 ? 1.1500 0.8177 1.1826 0.1781  -0.2743 0.0872  213 ASP A C   
1538 O O   . ASP A 198 ? 1.2526 0.9102 1.3015 0.1940  -0.3127 0.0933  213 ASP A O   
1539 C CB  . ASP A 198 ? 1.0144 0.6448 0.9153 0.1384  -0.2510 0.1127  213 ASP A CB  
1540 C CG  . ASP A 198 ? 1.0212 0.6550 0.8671 0.1202  -0.2457 0.1175  213 ASP A CG  
1541 O OD1 . ASP A 198 ? 1.0382 0.7039 0.9048 0.1217  -0.2551 0.1061  213 ASP A OD1 
1542 O OD2 . ASP A 198 ? 1.0444 0.6488 0.8273 0.1037  -0.2312 0.1316  213 ASP A OD2 
1543 N N   . LYS A 199 ? 1.1092 0.7752 1.1655 0.1811  -0.2501 0.0778  214 LYS A N   
1544 C CA  . LYS A 199 ? 1.1074 0.7546 1.2068 0.2038  -0.2667 0.0742  214 LYS A CA  
1545 C C   . LYS A 199 ? 1.1506 0.8475 1.3357 0.2248  -0.2752 0.0508  214 LYS A C   
1546 O O   . LYS A 199 ? 1.2584 0.9450 1.4807 0.2476  -0.3087 0.0519  214 LYS A O   
1547 C CB  . LYS A 199 ? 1.1670 0.7959 1.2624 0.1990  -0.2373 0.0687  214 LYS A CB  
1548 C CG  . LYS A 199 ? 1.3008 0.9058 1.4399 0.2226  -0.2512 0.0616  214 LYS A CG  
1549 C CD  . LYS A 199 ? 1.3952 1.0212 1.5689 0.2227  -0.2154 0.0368  214 LYS A CD  
1550 C CE  . LYS A 199 ? 1.2716 0.8790 1.4975 0.2492  -0.2274 0.0232  214 LYS A CE  
1551 N NZ  . LYS A 199 ? 1.2206 0.8538 1.4819 0.2503  -0.1921 -0.0058 214 LYS A NZ  
1552 N N   . TYR A 200 ? 1.1281 0.8794 1.3476 0.2172  -0.2452 0.0298  215 TYR A N   
1553 C CA  . TYR A 200 ? 1.1281 0.9321 1.4315 0.2336  -0.2472 0.0063  215 TYR A CA  
1554 C C   . TYR A 200 ? 1.1596 0.9883 1.4808 0.2363  -0.2782 0.0094  215 TYR A C   
1555 O O   . TYR A 200 ? 1.1958 1.0556 1.5884 0.2557  -0.2971 -0.0036 215 TYR A O   
1556 C CB  . TYR A 200 ? 1.1783 1.0304 1.5086 0.2215  -0.2034 -0.0159 215 TYR A CB  
1557 C CG  . TYR A 200 ? 1.4416 1.2813 1.7654 0.2187  -0.1707 -0.0258 215 TYR A CG  
1558 C CD1 . TYR A 200 ? 1.4077 1.1912 1.6858 0.2182  -0.1744 -0.0116 215 TYR A CD1 
1559 C CD2 . TYR A 200 ? 1.4682 1.3520 1.8292 0.2142  -0.1359 -0.0494 215 TYR A CD2 
1560 C CE1 . TYR A 200 ? 1.4138 1.1863 1.6864 0.2141  -0.1463 -0.0223 215 TYR A CE1 
1561 C CE2 . TYR A 200 ? 1.4609 1.3328 1.8115 0.2105  -0.1076 -0.0597 215 TYR A CE2 
1562 C CZ  . TYR A 200 ? 1.4955 1.3121 1.8033 0.2108  -0.1139 -0.0469 215 TYR A CZ  
1563 O OH  . TYR A 200 ? 1.4715 1.2750 1.7687 0.2060  -0.0885 -0.0581 215 TYR A OH  
1564 N N   . TYR A 201 ? 1.1378 0.9540 1.3974 0.2173  -0.2842 0.0249  216 TYR A N   
1565 C CA  . TYR A 201 ? 1.1922 1.0393 1.4674 0.2139  -0.3055 0.0226  216 TYR A CA  
1566 C C   . TYR A 201 ? 1.3208 1.1269 1.5325 0.2102  -0.3434 0.0458  216 TYR A C   
1567 O O   . TYR A 201 ? 1.3745 1.2014 1.5884 0.2046  -0.3622 0.0439  216 TYR A O   
1568 C CB  . TYR A 201 ? 1.0931 0.9779 1.3635 0.1917  -0.2718 0.0113  216 TYR A CB  
1569 C CG  . TYR A 201 ? 1.0684 1.0011 1.4039 0.1932  -0.2382 -0.0122 216 TYR A CG  
1570 C CD1 . TYR A 201 ? 1.1649 1.1463 1.5835 0.2059  -0.2467 -0.0301 216 TYR A CD1 
1571 C CD2 . TYR A 201 ? 1.0950 1.0255 1.4085 0.1809  -0.1980 -0.0165 216 TYR A CD2 
1572 C CE1 . TYR A 201 ? 1.1837 1.2095 1.6579 0.2052  -0.2128 -0.0519 216 TYR A CE1 
1573 C CE2 . TYR A 201 ? 1.1168 1.0885 1.4817 0.1806  -0.1673 -0.0374 216 TYR A CE2 
1574 C CZ  . TYR A 201 ? 1.1636 1.1824 1.6066 0.1921  -0.1732 -0.0550 216 TYR A CZ  
1575 O OH  . TYR A 201 ? 1.2173 1.2779 1.7083 0.1900  -0.1398 -0.0761 216 TYR A OH  
1576 N N   . MET A 202 ? 1.3646 1.1119 1.5162 0.2109  -0.3542 0.0674  217 MET A N   
1577 C CA  . MET A 202 ? 1.4718 1.1740 1.5529 0.2058  -0.3890 0.0915  217 MET A CA  
1578 C C   . MET A 202 ? 1.4163 1.1263 1.4419 0.1823  -0.3788 0.0929  217 MET A C   
1579 O O   . MET A 202 ? 1.3001 0.9787 1.2646 0.1758  -0.4060 0.1092  217 MET A O   
1580 C CB  . MET A 202 ? 1.4175 1.1221 1.5377 0.2260  -0.4390 0.0940  217 MET A CB  
1581 C CG  . MET A 202 ? 1.5278 1.2367 1.7108 0.2462  -0.4408 0.0857  217 MET A CG  
1582 S SD  . MET A 202 ? 2.0309 1.6733 2.1602 0.2451  -0.4310 0.1051  217 MET A SD  
1583 C CE  . MET A 202 ? 1.7173 1.3064 1.7538 0.2314  -0.4646 0.1356  217 MET A CE  
1584 N N   . ALA A 203 ? 1.2549 1.0032 1.2982 0.1693  -0.3399 0.0760  218 ALA A N   
1585 C CA  . ALA A 203 ? 1.0988 0.8602 1.1054 0.1500  -0.3303 0.0723  218 ALA A CA  
1586 C C   . ALA A 203 ? 1.0969 0.8808 1.1076 0.1361  -0.2823 0.0606  218 ALA A C   
1587 O O   . ALA A 203 ? 0.8971 0.7111 0.9657 0.1421  -0.2617 0.0468  218 ALA A O   
1588 C CB  . ALA A 203 ? 1.1477 0.9484 1.2026 0.1537  -0.3558 0.0590  218 ALA A CB  
1589 N N   . SER A 204 ? 0.8685 0.6370 0.8165 0.1179  -0.2653 0.0658  219 SER A N   
1590 C CA  . SER A 204 ? 0.9799 0.7645 0.9250 0.1047  -0.2236 0.0575  219 SER A CA  
1591 C C   . SER A 204 ? 1.0520 0.8355 0.9517 0.0888  -0.2176 0.0555  219 SER A C   
1592 O O   . SER A 204 ? 1.0016 0.7553 0.8446 0.0847  -0.2368 0.0660  219 SER A O   
1593 C CB  . SER A 204 ? 1.0557 0.8108 0.9689 0.1015  -0.2019 0.0687  219 SER A CB  
1594 O OG  . SER A 204 ? 1.0601 0.7690 0.9109 0.0993  -0.2202 0.0886  219 SER A OG  
1595 N N   . PRO A 205 ? 1.0097 0.8224 0.9307 0.0796  -0.1919 0.0419  220 PRO A N   
1596 C CA  . PRO A 205 ? 1.0175 0.8258 0.8966 0.0655  -0.1830 0.0382  220 PRO A CA  
1597 C C   . PRO A 205 ? 1.0256 0.8013 0.8386 0.0569  -0.1649 0.0495  220 PRO A C   
1598 O O   . PRO A 205 ? 0.8453 0.6129 0.6569 0.0573  -0.1461 0.0565  220 PRO A O   
1599 C CB  . PRO A 205 ? 0.6994 0.5433 0.6230 0.0592  -0.1575 0.0235  220 PRO A CB  
1600 C CG  . PRO A 205 ? 0.7398 0.6132 0.7326 0.0697  -0.1615 0.0171  220 PRO A CG  
1601 C CD  . PRO A 205 ? 0.7445 0.5950 0.7306 0.0823  -0.1724 0.0286  220 PRO A CD  
1602 N N   . ASP A 206 ? 0.8510 0.6091 0.6100 0.0482  -0.1696 0.0496  221 ASP A N   
1603 C CA  . ASP A 206 ? 0.9279 0.6648 0.6306 0.0378  -0.1450 0.0551  221 ASP A CA  
1604 C C   . ASP A 206 ? 0.9572 0.7173 0.6829 0.0317  -0.1119 0.0433  221 ASP A C   
1605 O O   . ASP A 206 ? 0.7324 0.5204 0.5075 0.0333  -0.1097 0.0317  221 ASP A O   
1606 C CB  . ASP A 206 ? 0.9220 0.6343 0.5596 0.0307  -0.1583 0.0556  221 ASP A CB  
1607 C CG  . ASP A 206 ? 0.9962 0.6826 0.6057 0.0359  -0.1946 0.0691  221 ASP A CG  
1608 O OD1 . ASP A 206 ? 1.2027 0.8748 0.8171 0.0420  -0.2001 0.0842  221 ASP A OD1 
1609 O OD2 . ASP A 206 ? 1.1899 0.8690 0.7747 0.0343  -0.2199 0.0643  221 ASP A OD2 
1610 N N   . LEU A 207 ? 0.8122 0.5605 0.5017 0.0239  -0.0866 0.0469  222 LEU A N   
1611 C CA  . LEU A 207 ? 0.7768 0.5441 0.4863 0.0193  -0.0571 0.0379  222 LEU A CA  
1612 C C   . LEU A 207 ? 0.8478 0.6072 0.5173 0.0123  -0.0446 0.0292  222 LEU A C   
1613 O O   . LEU A 207 ? 0.8254 0.5626 0.4416 0.0072  -0.0410 0.0354  222 LEU A O   
1614 C CB  . LEU A 207 ? 0.7196 0.4864 0.4350 0.0173  -0.0357 0.0472  222 LEU A CB  
1615 C CG  . LEU A 207 ? 0.8038 0.5882 0.5364 0.0126  -0.0075 0.0403  222 LEU A CG  
1616 C CD1 . LEU A 207 ? 0.6550 0.4650 0.4396 0.0162  -0.0077 0.0308  222 LEU A CD1 
1617 C CD2 . LEU A 207 ? 0.8189 0.5988 0.5487 0.0084  0.0097  0.0507  222 LEU A CD2 
1618 N N   . GLU A 208 ? 0.7052 0.4814 0.3998 0.0116  -0.0366 0.0148  223 GLU A N   
1619 C CA  . GLU A 208 ? 0.7380 0.5094 0.4065 0.0073  -0.0198 0.0033  223 GLU A CA  
1620 C C   . GLU A 208 ? 0.7444 0.5342 0.4472 0.0074  0.0054  -0.0001 223 GLU A C   
1621 O O   . GLU A 208 ? 0.7741 0.5810 0.5221 0.0094  0.0036  -0.0024 223 GLU A O   
1622 C CB  . GLU A 208 ? 0.7633 0.5324 0.4298 0.0068  -0.0357 -0.0119 223 GLU A CB  
1623 C CG  . GLU A 208 ? 0.9585 0.7100 0.5905 0.0062  -0.0651 -0.0103 223 GLU A CG  
1624 C CD  . GLU A 208 ? 0.9349 0.6859 0.5714 0.0040  -0.0824 -0.0270 223 GLU A CD  
1625 O OE1 . GLU A 208 ? 1.0318 0.7874 0.6815 0.0023  -0.0677 -0.0404 223 GLU A OE1 
1626 O OE2 . GLU A 208 ? 1.1065 0.8518 0.7356 0.0040  -0.1123 -0.0265 223 GLU A OE2 
1627 N N   . ILE A 209 ? 0.6900 0.4769 0.3716 0.0046  0.0284  -0.0004 224 ILE A N   
1628 C CA  . ILE A 209 ? 0.7141 0.5185 0.4280 0.0055  0.0499  -0.0039 224 ILE A CA  
1629 C C   . ILE A 209 ? 0.7781 0.5798 0.4776 0.0064  0.0636  -0.0197 224 ILE A C   
1630 O O   . ILE A 209 ? 0.7562 0.5438 0.4105 0.0036  0.0693  -0.0244 224 ILE A O   
1631 C CB  . ILE A 209 ? 0.8020 0.6119 0.5180 0.0019  0.0666  0.0083  224 ILE A CB  
1632 C CG1 . ILE A 209 ? 0.8510 0.6584 0.5783 0.0020  0.0532  0.0221  224 ILE A CG1 
1633 C CG2 . ILE A 209 ? 0.6906 0.5211 0.4462 0.0034  0.0833  0.0046  224 ILE A CG2 
1634 C CD1 . ILE A 209 ? 0.8695 0.6768 0.5951 -0.0035 0.0676  0.0340  224 ILE A CD1 
1635 N N   . GLN A 210 ? 0.7283 0.5415 0.4645 0.0103  0.0688  -0.0281 225 GLN A N   
1636 C CA  . GLN A 210 ? 0.7714 0.5832 0.5054 0.0141  0.0831  -0.0442 225 GLN A CA  
1637 C C   . GLN A 210 ? 0.7502 0.5809 0.5270 0.0178  0.0974  -0.0421 225 GLN A C   
1638 O O   . GLN A 210 ? 0.6927 0.5328 0.5022 0.0175  0.0895  -0.0330 225 GLN A O   
1639 C CB  . GLN A 210 ? 0.7851 0.5845 0.5209 0.0163  0.0680  -0.0583 225 GLN A CB  
1640 C CG  . GLN A 210 ? 1.0968 0.8890 0.8294 0.0218  0.0805  -0.0778 225 GLN A CG  
1641 C CD  . GLN A 210 ? 1.2592 1.0326 0.9852 0.0216  0.0628  -0.0922 225 GLN A CD  
1642 O OE1 . GLN A 210 ? 1.3017 1.0719 1.0309 0.0164  0.0412  -0.0865 225 GLN A OE1 
1643 N NE2 . GLN A 210 ? 1.2374 0.9987 0.9570 0.0272  0.0716  -0.1122 225 GLN A NE2 
1644 N N   . GLU A 211 ? 0.7100 0.5474 0.4867 0.0211  0.1182  -0.0509 226 GLU A N   
1645 C CA  . GLU A 211 ? 0.6956 0.5523 0.5157 0.0258  0.1294  -0.0501 226 GLU A CA  
1646 C C   . GLU A 211 ? 0.8022 0.6550 0.6389 0.0357  0.1334  -0.0683 226 GLU A C   
1647 O O   . GLU A 211 ? 0.7225 0.5628 0.5311 0.0383  0.1399  -0.0844 226 GLU A O   
1648 C CB  . GLU A 211 ? 0.6999 0.5733 0.5186 0.0219  0.1510  -0.0453 226 GLU A CB  
1649 C CG  . GLU A 211 ? 0.6686 0.5463 0.4845 0.0127  0.1471  -0.0260 226 GLU A CG  
1650 C CD  . GLU A 211 ? 0.7811 0.6776 0.6078 0.0072  0.1677  -0.0212 226 GLU A CD  
1651 O OE1 . GLU A 211 ? 0.7312 0.6433 0.5758 0.0116  0.1854  -0.0327 226 GLU A OE1 
1652 O OE2 . GLU A 211 ? 0.8284 0.7242 0.6486 -0.0016 0.1661  -0.0065 226 GLU A OE2 
1653 N N   . ILE A 212 ? 0.6320 0.4926 0.5118 0.0415  0.1284  -0.0660 227 ILE A N   
1654 C CA  . ILE A 212 ? 0.7038 0.5591 0.6068 0.0530  0.1310  -0.0817 227 ILE A CA  
1655 C C   . ILE A 212 ? 0.7005 0.5790 0.6474 0.0592  0.1392  -0.0771 227 ILE A C   
1656 O O   . ILE A 212 ? 0.6098 0.4914 0.5838 0.0586  0.1258  -0.0642 227 ILE A O   
1657 C CB  . ILE A 212 ? 0.6346 0.4687 0.5472 0.0540  0.1100  -0.0825 227 ILE A CB  
1658 C CG1 . ILE A 212 ? 0.7866 0.6032 0.6632 0.0455  0.0976  -0.0841 227 ILE A CG1 
1659 C CG2 . ILE A 212 ? 0.6760 0.4969 0.6059 0.0667  0.1126  -0.1013 227 ILE A CG2 
1660 C CD1 . ILE A 212 ? 0.8009 0.6009 0.6440 0.0487  0.1036  -0.1052 227 ILE A CD1 
1661 N N   . ASN A 213 ? 0.6349 0.5304 0.5893 0.0644  0.1609  -0.0879 228 ASN A N   
1662 C CA  . ASN A 213 ? 0.6476 0.5693 0.6506 0.0712  0.1679  -0.0860 228 ASN A CA  
1663 C C   . ASN A 213 ? 0.6828 0.5978 0.7156 0.0882  0.1675  -0.1041 228 ASN A C   
1664 O O   . ASN A 213 ? 0.6736 0.5953 0.7077 0.0964  0.1876  -0.1243 228 ASN A O   
1665 C CB  . ASN A 213 ? 0.6405 0.5894 0.6425 0.0656  0.1927  -0.0871 228 ASN A CB  
1666 C CG  . ASN A 213 ? 0.6222 0.6029 0.6800 0.0707  0.1975  -0.0843 228 ASN A CG  
1667 O OD1 . ASN A 213 ? 0.6878 0.6703 0.7862 0.0837  0.1865  -0.0883 228 ASN A OD1 
1668 N ND2 . ASN A 213 ? 0.5965 0.6011 0.6575 0.0598  0.2119  -0.0765 228 ASN A ND2 
1669 N N   . ALA A 214 ? 0.6785 0.5793 0.7354 0.0934  0.1453  -0.0968 229 ALA A N   
1670 C CA  . ALA A 214 ? 0.6753 0.5570 0.7537 0.1090  0.1391  -0.1125 229 ALA A CA  
1671 C C   . ALA A 214 ? 0.7168 0.6220 0.8386 0.1255  0.1558  -0.1289 229 ALA A C   
1672 O O   . ALA A 214 ? 0.7108 0.6057 0.8354 0.1384  0.1662  -0.1529 229 ALA A O   
1673 C CB  . ALA A 214 ? 0.6255 0.4876 0.7221 0.1089  0.1117  -0.0965 229 ALA A CB  
1674 N N   . ALA A 215 ? 0.6856 0.6237 0.8438 0.1255  0.1586  -0.1181 230 ALA A N   
1675 C CA  . ALA A 215 ? 0.7498 0.7162 0.9602 0.1418  0.1729  -0.1336 230 ALA A CA  
1676 C C   . ALA A 215 ? 0.7121 0.7023 0.9088 0.1396  0.2081  -0.1521 230 ALA A C   
1677 O O   . ALA A 215 ? 0.7229 0.7252 0.9482 0.1552  0.2257  -0.1758 230 ALA A O   
1678 C CB  . ALA A 215 ? 0.6341 0.6293 0.8911 0.1413  0.1611  -0.1160 230 ALA A CB  
1679 N N   . ASN A 216 ? 0.7883 0.7846 0.9411 0.1201  0.2196  -0.1417 231 ASN A N   
1680 C CA  . ASN A 216 ? 0.7946 0.8122 0.9273 0.1134  0.2536  -0.1543 231 ASN A CA  
1681 C C   . ASN A 216 ? 0.7702 0.7601 0.8277 0.0979  0.2557  -0.1504 231 ASN A C   
1682 O O   . ASN A 216 ? 0.7718 0.7648 0.8023 0.0809  0.2551  -0.1315 231 ASN A O   
1683 C CB  . ASN A 216 ? 0.8206 0.8791 0.9851 0.1035  0.2653  -0.1420 231 ASN A CB  
1684 C CG  . ASN A 216 ? 0.8406 0.9287 1.0826 0.1186  0.2587  -0.1450 231 ASN A CG  
1685 O OD1 . ASN A 216 ? 0.8759 0.9888 1.1583 0.1323  0.2788  -0.1666 231 ASN A OD1 
1686 N ND2 . ASN A 216 ? 0.6651 0.7512 0.9285 0.1165  0.2299  -0.1241 231 ASN A ND2 
1687 N N   . SER A 217 ? 0.8514 0.8131 0.8757 0.1043  0.2571  -0.1692 232 SER A N   
1688 C CA  . SER A 217 ? 0.9099 0.8394 0.8677 0.0919  0.2470  -0.1639 232 SER A CA  
1689 C C   . SER A 217 ? 1.0158 0.9520 0.9231 0.0749  0.2668  -0.1582 232 SER A C   
1690 O O   . SER A 217 ? 0.8567 0.7707 0.7151 0.0628  0.2532  -0.1457 232 SER A O   
1691 C CB  . SER A 217 ? 0.8976 0.7957 0.8325 0.1018  0.2436  -0.1880 232 SER A CB  
1692 O OG  . SER A 217 ? 1.0406 0.9497 0.9716 0.1095  0.2742  -0.2148 232 SER A OG  
1693 N N   . LYS A 218 ? 1.1140 1.0796 1.0321 0.0729  0.2979  -0.1664 233 LYS A N   
1694 C CA  . LYS A 218 ? 1.0901 1.0578 0.9563 0.0539  0.3158  -0.1572 233 LYS A CA  
1695 C C   . LYS A 218 ? 1.0098 0.9986 0.8963 0.0404  0.3140  -0.1311 233 LYS A C   
1696 O O   . LYS A 218 ? 1.1284 1.1154 0.9737 0.0231  0.3261  -0.1194 233 LYS A O   
1697 C CB  . LYS A 218 ? 1.1889 1.1734 1.0418 0.0543  0.3551  -0.1810 233 LYS A CB  
1698 C CG  . LYS A 218 ? 1.1888 1.1426 0.9923 0.0611  0.3584  -0.2063 233 LYS A CG  
1699 C CD  . LYS A 218 ? 1.4354 1.4150 1.2556 0.0698  0.3812  -0.2292 233 LYS A CD  
1700 C CE  . LYS A 218 ? 1.4232 1.4222 1.3237 0.0933  0.3799  -0.2456 233 LYS A CE  
1701 N NZ  . LYS A 218 ? 1.3438 1.3642 1.2596 0.1049  0.4009  -0.2701 233 LYS A NZ  
1702 N N   . GLN A 219 ? 0.8452 0.8495 0.7901 0.0470  0.2971  -0.1210 234 GLN A N   
1703 C CA  . GLN A 219 ? 0.7806 0.8072 0.7475 0.0340  0.2983  -0.1007 234 GLN A CA  
1704 C C   . GLN A 219 ? 0.7824 0.7847 0.7238 0.0247  0.2705  -0.0775 234 GLN A C   
1705 O O   . GLN A 219 ? 0.7653 0.7496 0.7120 0.0331  0.2453  -0.0753 234 GLN A O   
1706 C CB  . GLN A 219 ? 0.7316 0.7919 0.7755 0.0444  0.2961  -0.1030 234 GLN A CB  
1707 C CG  . GLN A 219 ? 0.9712 1.0665 1.0544 0.0526  0.3271  -0.1252 234 GLN A CG  
1708 C CD  . GLN A 219 ? 1.0648 1.1996 1.2277 0.0591  0.3235  -0.1232 234 GLN A CD  
1709 O OE1 . GLN A 219 ? 1.0172 1.1469 1.2057 0.0631  0.2938  -0.1095 234 GLN A OE1 
1710 N NE2 . GLN A 219 ? 1.0153 1.1909 1.2173 0.0593  0.3537  -0.1371 234 GLN A NE2 
1711 N N   . PRO A 220 ? 0.7863 0.7870 0.7012 0.0074  0.2750  -0.0606 235 PRO A N   
1712 C CA  . PRO A 220 ? 0.7667 0.7467 0.6654 0.0008  0.2493  -0.0405 235 PRO A CA  
1713 C C   . PRO A 220 ? 0.7376 0.7309 0.6885 0.0068  0.2309  -0.0341 235 PRO A C   
1714 O O   . PRO A 220 ? 0.7376 0.7601 0.7363 0.0089  0.2387  -0.0371 235 PRO A O   
1715 C CB  . PRO A 220 ? 0.8094 0.7885 0.6809 -0.0181 0.2613  -0.0254 235 PRO A CB  
1716 C CG  . PRO A 220 ? 0.8838 0.8907 0.7683 -0.0234 0.2947  -0.0359 235 PRO A CG  
1717 C CD  . PRO A 220 ? 0.7994 0.8122 0.6920 -0.0074 0.3046  -0.0598 235 PRO A CD  
1718 N N   . ILE A 221 ? 0.6052 0.5780 0.5468 0.0089  0.2060  -0.0256 236 ILE A N   
1719 C CA  . ILE A 221 ? 0.6192 0.5995 0.6003 0.0140  0.1878  -0.0200 236 ILE A CA  
1720 C C   . ILE A 221 ? 0.6673 0.6564 0.6576 0.0017  0.1846  -0.0049 236 ILE A C   
1721 O O   . ILE A 221 ? 0.6126 0.5844 0.5717 -0.0072 0.1793  0.0054  236 ILE A O   
1722 C CB  . ILE A 221 ? 0.5944 0.5508 0.5618 0.0196  0.1660  -0.0186 236 ILE A CB  
1723 C CG1 . ILE A 221 ? 0.5584 0.5050 0.5233 0.0314  0.1675  -0.0352 236 ILE A CG1 
1724 C CG2 . ILE A 221 ? 0.5633 0.5237 0.5598 0.0202  0.1477  -0.0089 236 ILE A CG2 
1725 C CD1 . ILE A 221 ? 0.5617 0.4836 0.5097 0.0334  0.1476  -0.0343 236 ILE A CD1 
1726 N N   A HIS A 222 ? 0.6167 0.6318 0.6512 0.0016  0.1865  -0.0045 237 HIS A N   
1727 N N   B HIS A 222 ? 0.6166 0.6318 0.6512 0.0016  0.1866  -0.0045 237 HIS A N   
1728 C CA  A HIS A 222 ? 0.6084 0.6319 0.6571 -0.0098 0.1798  0.0076  237 HIS A CA  
1729 C CA  B HIS A 222 ? 0.6084 0.6317 0.6571 -0.0097 0.1796  0.0076  237 HIS A CA  
1730 C C   A HIS A 222 ? 0.5615 0.5925 0.6440 -0.0033 0.1598  0.0098  237 HIS A C   
1731 C C   B HIS A 222 ? 0.5613 0.5926 0.6443 -0.0033 0.1597  0.0097  237 HIS A C   
1732 O O   A HIS A 222 ? 0.5764 0.6124 0.6812 0.0096  0.1548  0.0024  237 HIS A O   
1733 O O   B HIS A 222 ? 0.5759 0.6125 0.6816 0.0096  0.1547  0.0023  237 HIS A O   
1734 C CB  A HIS A 222 ? 0.5448 0.5948 0.6152 -0.0205 0.1998  0.0073  237 HIS A CB  
1735 C CB  B HIS A 222 ? 0.5461 0.5949 0.6147 -0.0209 0.1994  0.0078  237 HIS A CB  
1736 C CG  A HIS A 222 ? 0.6676 0.7085 0.6996 -0.0309 0.2210  0.0082  237 HIS A CG  
1737 C CG  B HIS A 222 ? 0.6010 0.6792 0.7059 -0.0127 0.2169  -0.0063 237 HIS A CG  
1738 N ND1 A HIS A 222 ? 0.7182 0.7487 0.7200 -0.0245 0.2332  -0.0015 237 HIS A ND1 
1739 N ND1 B HIS A 222 ? 0.6157 0.7228 0.7775 -0.0056 0.2106  -0.0106 237 HIS A ND1 
1740 C CD2 A HIS A 222 ? 0.6226 0.6613 0.6389 -0.0485 0.2319  0.0182  237 HIS A CD2 
1741 C CD2 B HIS A 222 ? 0.5739 0.6579 0.6671 -0.0103 0.2409  -0.0181 237 HIS A CD2 
1742 C CE1 A HIS A 222 ? 0.6232 0.6454 0.5887 -0.0380 0.2503  0.0035  237 HIS A CE1 
1743 C CE1 B HIS A 222 ? 0.5933 0.7245 0.7827 0.0027  0.2302  -0.0254 237 HIS A CE1 
1744 N NE2 A HIS A 222 ? 0.5898 0.6160 0.5641 -0.0528 0.2500  0.0163  237 HIS A NE2 
1745 N NE2 B HIS A 222 ? 0.5870 0.7047 0.7339 -0.0004 0.2505  -0.0311 237 HIS A NE2 
1746 N N   . MET A 223 ? 0.5593 0.5883 0.6430 -0.0127 0.1475  0.0200  238 MET A N   
1747 C CA  . MET A 223 ? 0.5129 0.5476 0.6211 -0.0099 0.1278  0.0237  238 MET A CA  
1748 C C   . MET A 223 ? 0.5343 0.5770 0.6508 -0.0239 0.1225  0.0309  238 MET A C   
1749 O O   . MET A 223 ? 0.5108 0.5477 0.6100 -0.0353 0.1321  0.0342  238 MET A O   
1750 C CB  . MET A 223 ? 0.4746 0.4845 0.5586 -0.0055 0.1119  0.0273  238 MET A CB  
1751 C CG  . MET A 223 ? 0.5147 0.5056 0.5647 -0.0148 0.1097  0.0332  238 MET A CG  
1752 S SD  . MET A 223 ? 0.5685 0.5375 0.5959 -0.0118 0.0955  0.0358  238 MET A SD  
1753 C CE  . MET A 223 ? 0.4856 0.4616 0.5359 -0.0098 0.0787  0.0399  238 MET A CE  
1754 N N   . VAL A 224 ? 0.5368 0.5889 0.6769 -0.0235 0.1049  0.0338  239 VAL A N   
1755 C CA  . VAL A 224 ? 0.5390 0.5919 0.6792 -0.0368 0.0944  0.0395  239 VAL A CA  
1756 C C   . VAL A 224 ? 0.6277 0.6525 0.7297 -0.0387 0.0831  0.0437  239 VAL A C   
1757 O O   . VAL A 224 ? 0.5683 0.5848 0.6645 -0.0317 0.0710  0.0453  239 VAL A O   
1758 C CB  . VAL A 224 ? 0.5029 0.5799 0.6846 -0.0364 0.0787  0.0401  239 VAL A CB  
1759 C CG1 . VAL A 224 ? 0.5051 0.5810 0.6832 -0.0519 0.0664  0.0442  239 VAL A CG1 
1760 C CG2 . VAL A 224 ? 0.4645 0.5755 0.6935 -0.0324 0.0920  0.0334  239 VAL A CG2 
1761 N N   . TYR A 225 ? 0.5391 0.5485 0.6162 -0.0483 0.0876  0.0452  240 TYR A N   
1762 C CA  . TYR A 225 ? 0.5474 0.5343 0.5939 -0.0490 0.0794  0.0464  240 TYR A CA  
1763 C C   . TYR A 225 ? 0.5391 0.5136 0.5714 -0.0607 0.0801  0.0464  240 TYR A C   
1764 O O   . TYR A 225 ? 0.5295 0.5105 0.5739 -0.0696 0.0860  0.0473  240 TYR A O   
1765 C CB  . TYR A 225 ? 0.5178 0.4901 0.5433 -0.0396 0.0851  0.0451  240 TYR A CB  
1766 C CG  . TYR A 225 ? 0.5164 0.4749 0.5228 -0.0388 0.0760  0.0454  240 TYR A CG  
1767 C CD1 . TYR A 225 ? 0.5133 0.4749 0.5245 -0.0374 0.0645  0.0480  240 TYR A CD1 
1768 C CD2 . TYR A 225 ? 0.4966 0.4395 0.4814 -0.0402 0.0789  0.0435  240 TYR A CD2 
1769 C CE1 . TYR A 225 ? 0.4873 0.4372 0.4781 -0.0398 0.0591  0.0490  240 TYR A CE1 
1770 C CE2 . TYR A 225 ? 0.4661 0.4014 0.4373 -0.0406 0.0742  0.0420  240 TYR A CE2 
1771 C CZ  . TYR A 225 ? 0.4837 0.4228 0.4560 -0.0417 0.0658  0.0450  240 TYR A CZ  
1772 O OH  . TYR A 225 ? 0.5367 0.4688 0.4923 -0.0450 0.0640  0.0442  240 TYR A OH  
1773 N N   . VAL A 226 ? 0.5535 0.5102 0.5621 -0.0612 0.0744  0.0447  241 VAL A N   
1774 C CA  . VAL A 226 ? 0.5675 0.5060 0.5598 -0.0686 0.0753  0.0421  241 VAL A CA  
1775 C C   . VAL A 226 ? 0.5286 0.4508 0.5044 -0.0615 0.0838  0.0422  241 VAL A C   
1776 O O   . VAL A 226 ? 0.5198 0.4339 0.4829 -0.0546 0.0821  0.0391  241 VAL A O   
1777 C CB  . VAL A 226 ? 0.6098 0.5395 0.5866 -0.0721 0.0657  0.0371  241 VAL A CB  
1778 C CG1 . VAL A 226 ? 0.5936 0.5030 0.5572 -0.0784 0.0670  0.0314  241 VAL A CG1 
1779 C CG2 . VAL A 226 ? 0.6302 0.5741 0.6178 -0.0786 0.0527  0.0384  241 VAL A CG2 
1780 N N   . PRO A 227 ? 0.5830 0.4603 0.4684 -0.0668 -0.0022 0.0407  242 PRO A N   
1781 C CA  . PRO A 227 ? 0.6153 0.4691 0.4848 -0.0600 -0.0005 0.0455  242 PRO A CA  
1782 C C   . PRO A 227 ? 0.5666 0.3941 0.4280 -0.0562 -0.0073 0.0409  242 PRO A C   
1783 O O   . PRO A 227 ? 0.5986 0.4138 0.4509 -0.0460 -0.0090 0.0427  242 PRO A O   
1784 C CB  . PRO A 227 ? 0.5666 0.4147 0.4324 -0.0712 0.0066  0.0540  242 PRO A CB  
1785 C CG  . PRO A 227 ? 0.6549 0.5160 0.5357 -0.0849 0.0075  0.0514  242 PRO A CG  
1786 C CD  . PRO A 227 ? 0.5759 0.4633 0.4712 -0.0802 0.0032  0.0444  242 PRO A CD  
1787 N N   . SER A 228 ? 0.5696 0.3894 0.4364 -0.0638 -0.0112 0.0334  243 SER A N   
1788 C CA  . SER A 228 ? 0.5708 0.3672 0.4348 -0.0584 -0.0164 0.0260  243 SER A CA  
1789 C C   . SER A 228 ? 0.5915 0.3984 0.4540 -0.0461 -0.0183 0.0185  243 SER A C   
1790 O O   . SER A 228 ? 0.5998 0.3908 0.4594 -0.0368 -0.0207 0.0162  243 SER A O   
1791 C CB  . SER A 228 ? 0.6480 0.4353 0.5198 -0.0697 -0.0187 0.0159  243 SER A CB  
1792 O OG  . SER A 228 ? 0.6784 0.4925 0.5553 -0.0746 -0.0195 0.0072  243 SER A OG  
1793 N N   . HIS A 229 ? 0.5928 0.4268 0.4583 -0.0462 -0.0179 0.0159  244 HIS A N   
1794 C CA  . HIS A 229 ? 0.5372 0.3810 0.3995 -0.0361 -0.0191 0.0117  244 HIS A CA  
1795 C C   . HIS A 229 ? 0.6206 0.4606 0.4782 -0.0250 -0.0170 0.0197  244 HIS A C   
1796 O O   . HIS A 229 ? 0.5633 0.3974 0.4178 -0.0161 -0.0182 0.0158  244 HIS A O   
1797 C CB  . HIS A 229 ? 0.5111 0.3834 0.3771 -0.0393 -0.0206 0.0114  244 HIS A CB  
1798 C CG  . HIS A 229 ? 0.5234 0.4037 0.3908 -0.0508 -0.0241 0.0017  244 HIS A CG  
1799 N ND1 . HIS A 229 ? 0.6453 0.5512 0.5135 -0.0555 -0.0283 0.0015  244 HIS A ND1 
1800 C CD2 . HIS A 229 ? 0.6381 0.5039 0.5063 -0.0596 -0.0247 -0.0082 244 HIS A CD2 
1801 C CE1 . HIS A 229 ? 0.6401 0.5490 0.5071 -0.0675 -0.0313 -0.0092 244 HIS A CE1 
1802 N NE2 . HIS A 229 ? 0.6996 0.5837 0.5675 -0.0702 -0.0285 -0.0163 244 HIS A NE2 
1803 N N   . LEU A 230 ? 0.5653 0.4107 0.4230 -0.0262 -0.0132 0.0294  245 LEU A N   
1804 C CA  . LEU A 230 ? 0.5829 0.4265 0.4347 -0.0176 -0.0105 0.0352  245 LEU A CA  
1805 C C   . LEU A 230 ? 0.5341 0.3528 0.3765 -0.0141 -0.0133 0.0374  245 LEU A C   
1806 O O   . LEU A 230 ? 0.5551 0.3701 0.3933 -0.0049 -0.0151 0.0369  245 LEU A O   
1807 C CB  . LEU A 230 ? 0.5514 0.4078 0.4063 -0.0215 -0.0039 0.0421  245 LEU A CB  
1808 C CG  . LEU A 230 ? 0.5410 0.3958 0.3881 -0.0152 0.0005  0.0461  245 LEU A CG  
1809 C CD1 . LEU A 230 ? 0.5219 0.3845 0.3721 -0.0044 -0.0008 0.0425  245 LEU A CD1 
1810 C CD2 . LEU A 230 ? 0.5581 0.4267 0.4095 -0.0209 0.0097  0.0499  245 LEU A CD2 
1811 N N   . TYR A 231 ? 0.5421 0.3436 0.3826 -0.0218 -0.0148 0.0406  246 TYR A N   
1812 C CA  . TYR A 231 ? 0.6192 0.3949 0.4535 -0.0186 -0.0203 0.0448  246 TYR A CA  
1813 C C   . TYR A 231 ? 0.6044 0.3732 0.4458 -0.0086 -0.0256 0.0348  246 TYR A C   
1814 O O   . TYR A 231 ? 0.6393 0.3990 0.4783 0.0001  -0.0301 0.0371  246 TYR A O   
1815 C CB  . TYR A 231 ? 0.5787 0.3352 0.4133 -0.0297 -0.0216 0.0500  246 TYR A CB  
1816 C CG  . TYR A 231 ? 0.6572 0.3839 0.4867 -0.0277 -0.0291 0.0587  246 TYR A CG  
1817 C CD1 . TYR A 231 ? 0.7085 0.4169 0.5494 -0.0204 -0.0363 0.0516  246 TYR A CD1 
1818 C CD2 . TYR A 231 ? 0.6655 0.3828 0.4797 -0.0339 -0.0290 0.0743  246 TYR A CD2 
1819 C CE1 . TYR A 231 ? 0.7337 0.4141 0.5745 -0.0175 -0.0452 0.0613  246 TYR A CE1 
1820 C CE2 . TYR A 231 ? 0.7161 0.4057 0.5249 -0.0329 -0.0383 0.0855  246 TYR A CE2 
1821 C CZ  . TYR A 231 ? 0.8178 0.4884 0.6417 -0.0238 -0.0473 0.0797  246 TYR A CZ  
1822 O OH  . TYR A 231 ? 0.8255 0.4679 0.6482 -0.0217 -0.0584 0.0925  246 TYR A OH  
1823 N N   . HIS A 232 ? 0.6282 0.4029 0.4789 -0.0108 -0.0251 0.0228  247 HIS A N   
1824 C CA  . HIS A 232 ? 0.5976 0.3684 0.4562 -0.0030 -0.0276 0.0104  247 HIS A CA  
1825 C C   . HIS A 232 ? 0.5705 0.3551 0.4268 0.0069  -0.0268 0.0096  247 HIS A C   
1826 O O   . HIS A 232 ? 0.5742 0.3507 0.4355 0.0158  -0.0303 0.0066  247 HIS A O   
1827 C CB  . HIS A 232 ? 0.6306 0.4109 0.4950 -0.0098 -0.0253 -0.0038 247 HIS A CB  
1828 C CG  . HIS A 232 ? 0.8455 0.6246 0.7178 -0.0037 -0.0251 -0.0193 247 HIS A CG  
1829 N ND1 . HIS A 232 ? 0.8995 0.6564 0.7842 -0.0001 -0.0278 -0.0275 247 HIS A ND1 
1830 C CD2 . HIS A 232 ? 0.8014 0.5995 0.6726 -0.0010 -0.0220 -0.0284 247 HIS A CD2 
1831 C CE1 . HIS A 232 ? 0.8621 0.6264 0.7546 0.0049  -0.0250 -0.0433 247 HIS A CE1 
1832 N NE2 . HIS A 232 ? 0.7666 0.5561 0.6490 0.0035  -0.0211 -0.0437 247 HIS A NE2 
1833 N N   . MET A 233 ? 0.5351 0.3408 0.3867 0.0053  -0.0228 0.0124  248 MET A N   
1834 C CA  . MET A 233 ? 0.5392 0.3570 0.3894 0.0131  -0.0216 0.0122  248 MET A CA  
1835 C C   . MET A 233 ? 0.5717 0.3795 0.4173 0.0196  -0.0241 0.0195  248 MET A C   
1836 O O   . MET A 233 ? 0.5951 0.4023 0.4438 0.0273  -0.0264 0.0158  248 MET A O   
1837 C CB  . MET A 233 ? 0.5437 0.3821 0.3925 0.0101  -0.0178 0.0164  248 MET A CB  
1838 C CG  . MET A 233 ? 0.6129 0.4649 0.4643 0.0029  -0.0176 0.0110  248 MET A CG  
1839 S SD  . MET A 233 ? 0.6544 0.5304 0.5083 0.0022  -0.0163 0.0187  248 MET A SD  
1840 C CE  . MET A 233 ? 0.6154 0.4922 0.4736 -0.0006 -0.0136 0.0277  248 MET A CE  
1841 N N   . LEU A 234 ? 0.5722 0.3744 0.4097 0.0154  -0.0235 0.0295  249 LEU A N   
1842 C CA  . LEU A 234 ? 0.6037 0.3975 0.4320 0.0190  -0.0264 0.0369  249 LEU A CA  
1843 C C   . LEU A 234 ? 0.6058 0.3806 0.4375 0.0241  -0.0354 0.0375  249 LEU A C   
1844 O O   . LEU A 234 ? 0.6133 0.3867 0.4441 0.0310  -0.0404 0.0383  249 LEU A O   
1845 C CB  . LEU A 234 ? 0.5955 0.3878 0.4124 0.0105  -0.0226 0.0468  249 LEU A CB  
1846 C CG  . LEU A 234 ? 0.6041 0.4172 0.4225 0.0080  -0.0136 0.0457  249 LEU A CG  
1847 C CD1 . LEU A 234 ? 0.6112 0.4266 0.4233 -0.0022 -0.0072 0.0525  249 LEU A CD1 
1848 C CD2 . LEU A 234 ? 0.5824 0.4032 0.3977 0.0150  -0.0121 0.0436  249 LEU A CD2 
1849 N N   . PHE A 235 ? 0.5979 0.3573 0.4356 0.0206  -0.0384 0.0371  250 PHE A N   
1850 C CA  . PHE A 235 ? 0.5612 0.3003 0.4074 0.0265  -0.0478 0.0382  250 PHE A CA  
1851 C C   . PHE A 235 ? 0.5864 0.3329 0.4480 0.0372  -0.0495 0.0256  250 PHE A C   
1852 O O   . PHE A 235 ? 0.6030 0.3426 0.4713 0.0454  -0.0577 0.0277  250 PHE A O   
1853 C CB  . PHE A 235 ? 0.5798 0.3007 0.4338 0.0205  -0.0491 0.0372  250 PHE A CB  
1854 C CG  . PHE A 235 ? 0.6657 0.3638 0.5351 0.0277  -0.0587 0.0367  250 PHE A CG  
1855 C CD1 . PHE A 235 ? 0.6222 0.3021 0.4861 0.0297  -0.0693 0.0529  250 PHE A CD1 
1856 C CD2 . PHE A 235 ? 0.6961 0.3911 0.5865 0.0321  -0.0575 0.0199  250 PHE A CD2 
1857 C CE1 . PHE A 235 ? 0.7536 0.4116 0.6361 0.0376  -0.0801 0.0541  250 PHE A CE1 
1858 C CE2 . PHE A 235 ? 0.7336 0.4069 0.6443 0.0401  -0.0661 0.0179  250 PHE A CE2 
1859 C CZ  . PHE A 235 ? 0.7110 0.3652 0.6196 0.0438  -0.0783 0.0359  250 PHE A CZ  
1860 N N   . GLU A 236 ? 0.5735 0.3355 0.4412 0.0362  -0.0421 0.0127  251 GLU A N   
1861 C CA  . GLU A 236 ? 0.6164 0.3883 0.4977 0.0439  -0.0412 -0.0002 251 GLU A CA  
1862 C C   . GLU A 236 ? 0.5907 0.3737 0.4680 0.0496  -0.0427 0.0037  251 GLU A C   
1863 O O   . GLU A 236 ? 0.5523 0.3348 0.4422 0.0578  -0.0477 -0.0003 251 GLU A O   
1864 C CB  . GLU A 236 ? 0.5904 0.3785 0.4727 0.0382  -0.0324 -0.0126 251 GLU A CB  
1865 C CG  . GLU A 236 ? 0.7548 0.5481 0.6527 0.0422  -0.0296 -0.0299 251 GLU A CG  
1866 C CD  . GLU A 236 ? 0.6393 0.4127 0.5550 0.0457  -0.0334 -0.0380 251 GLU A CD  
1867 O OE1 . GLU A 236 ? 0.7930 0.5498 0.7066 0.0402  -0.0357 -0.0339 251 GLU A OE1 
1868 O OE2 . GLU A 236 ? 0.8331 0.6075 0.7676 0.0540  -0.0338 -0.0493 251 GLU A OE2 
1869 N N   . LEU A 237 ? 0.5300 0.3230 0.3923 0.0453  -0.0387 0.0112  252 LEU A N   
1870 C CA  . LEU A 237 ? 0.5259 0.3278 0.3841 0.0493  -0.0396 0.0136  252 LEU A CA  
1871 C C   . LEU A 237 ? 0.5654 0.3552 0.4195 0.0530  -0.0496 0.0222  252 LEU A C   
1872 O O   . LEU A 237 ? 0.5811 0.3756 0.4415 0.0590  -0.0546 0.0198  252 LEU A O   
1873 C CB  . LEU A 237 ? 0.5066 0.3198 0.3529 0.0440  -0.0325 0.0181  252 LEU A CB  
1874 C CG  . LEU A 237 ? 0.5624 0.3899 0.4132 0.0408  -0.0253 0.0123  252 LEU A CG  
1875 C CD1 . LEU A 237 ? 0.5640 0.4002 0.4083 0.0368  -0.0201 0.0185  252 LEU A CD1 
1876 C CD2 . LEU A 237 ? 0.5682 0.4069 0.4277 0.0445  -0.0235 0.0038  252 LEU A CD2 
1877 N N   . PHE A 238 ? 0.5859 0.3610 0.4289 0.0482  -0.0533 0.0331  253 PHE A N   
1878 C CA  . PHE A 238 ? 0.5985 0.3616 0.4336 0.0497  -0.0644 0.0442  253 PHE A CA  
1879 C C   . PHE A 238 ? 0.6097 0.3638 0.4654 0.0594  -0.0757 0.0417  253 PHE A C   
1880 O O   . PHE A 238 ? 0.6230 0.3786 0.4799 0.0644  -0.0855 0.0456  253 PHE A O   
1881 C CB  . PHE A 238 ? 0.6053 0.3535 0.4241 0.0405  -0.0654 0.0576  253 PHE A CB  
1882 C CG  . PHE A 238 ? 0.6135 0.3712 0.4102 0.0315  -0.0573 0.0628  253 PHE A CG  
1883 C CD1 . PHE A 238 ? 0.6162 0.3821 0.3993 0.0316  -0.0590 0.0646  253 PHE A CD1 
1884 C CD2 . PHE A 238 ? 0.5659 0.3249 0.3568 0.0224  -0.0479 0.0648  253 PHE A CD2 
1885 C CE1 . PHE A 238 ? 0.6574 0.4321 0.4216 0.0231  -0.0499 0.0667  253 PHE A CE1 
1886 C CE2 . PHE A 238 ? 0.5981 0.3677 0.3729 0.0146  -0.0389 0.0677  253 PHE A CE2 
1887 C CZ  . PHE A 238 ? 0.6110 0.3878 0.3722 0.0151  -0.0394 0.0681  253 PHE A CZ  
1888 N N   . LYS A 239 ? 0.5862 0.3319 0.4605 0.0622  -0.0748 0.0340  254 LYS A N   
1889 C CA  . LYS A 239 ? 0.6552 0.3933 0.5557 0.0728  -0.0842 0.0288  254 LYS A CA  
1890 C C   . LYS A 239 ? 0.6010 0.3589 0.5148 0.0804  -0.0844 0.0188  254 LYS A C   
1891 O O   . LYS A 239 ? 0.5997 0.3561 0.5274 0.0886  -0.0964 0.0216  254 LYS A O   
1892 C CB  . LYS A 239 ? 0.6428 0.3733 0.5632 0.0739  -0.0789 0.0157  254 LYS A CB  
1893 C CG  . LYS A 239 ? 0.8148 0.5209 0.7322 0.0680  -0.0816 0.0237  254 LYS A CG  
1894 C CD  . LYS A 239 ? 0.7948 0.4926 0.7377 0.0708  -0.0775 0.0066  254 LYS A CD  
1895 C CE  . LYS A 239 ? 0.8713 0.5908 0.8131 0.0661  -0.0629 -0.0119 254 LYS A CE  
1896 N NZ  . LYS A 239 ? 0.9696 0.6815 0.9337 0.0671  -0.0584 -0.0307 254 LYS A NZ  
1897 N N   . ASN A 240 ? 0.5417 0.3188 0.4528 0.0773  -0.0718 0.0077  255 ASN A N   
1898 C CA  . ASN A 240 ? 0.5381 0.3345 0.4612 0.0822  -0.0701 -0.0019 255 ASN A CA  
1899 C C   . ASN A 240 ? 0.5178 0.3191 0.4287 0.0822  -0.0775 0.0075  255 ASN A C   
1900 O O   . ASN A 240 ? 0.5916 0.3998 0.5179 0.0888  -0.0858 0.0049  255 ASN A O   
1901 C CB  . ASN A 240 ? 0.5404 0.3537 0.4595 0.0765  -0.0554 -0.0123 255 ASN A CB  
1902 C CG  . ASN A 240 ? 0.6378 0.4529 0.5727 0.0768  -0.0485 -0.0266 255 ASN A CG  
1903 O OD1 . ASN A 240 ? 0.5684 0.3893 0.5269 0.0834  -0.0489 -0.0384 255 ASN A OD1 
1904 N ND2 . ASN A 240 ? 0.5504 0.3618 0.4736 0.0692  -0.0420 -0.0270 255 ASN A ND2 
1905 N N   . ALA A 241 ? 0.5521 0.3510 0.4366 0.0743  -0.0746 0.0170  256 ALA A N   
1906 C CA  . ALA A 241 ? 0.5758 0.3796 0.4451 0.0721  -0.0798 0.0236  256 ALA A CA  
1907 C C   . ALA A 241 ? 0.5911 0.3853 0.4617 0.0762  -0.0972 0.0337  256 ALA A C   
1908 O O   . ALA A 241 ? 0.6348 0.4382 0.5064 0.0781  -0.1053 0.0337  256 ALA A O   
1909 C CB  . ALA A 241 ? 0.6062 0.4079 0.4489 0.0627  -0.0722 0.0304  256 ALA A CB  
1910 N N   . MET A 242 ? 0.5885 0.3636 0.4585 0.0765  -0.1041 0.0437  257 MET A N   
1911 C CA  . MET A 242 ? 0.5955 0.3590 0.4661 0.0799  -0.1228 0.0571  257 MET A CA  
1912 C C   . MET A 242 ? 0.6330 0.4023 0.5390 0.0926  -0.1329 0.0496  257 MET A C   
1913 O O   . MET A 242 ? 0.6127 0.3877 0.5226 0.0962  -0.1475 0.0552  257 MET A O   
1914 C CB  . MET A 242 ? 0.7159 0.4548 0.5789 0.0764  -0.1275 0.0710  257 MET A CB  
1915 C CG  . MET A 242 ? 0.6201 0.3557 0.4493 0.0628  -0.1181 0.0792  257 MET A CG  
1916 S SD  . MET A 242 ? 0.7875 0.4946 0.6078 0.0559  -0.1227 0.0962  257 MET A SD  
1917 C CE  . MET A 242 ? 0.6973 0.4132 0.4811 0.0398  -0.1070 0.0997  257 MET A CE  
1918 N N   . ARG A 243 ? 0.5987 0.3680 0.5317 0.0988  -0.1253 0.0361  258 ARG A N   
1919 C CA  . ARG A 243 ? 0.6566 0.4345 0.6279 0.1109  -0.1318 0.0254  258 ARG A CA  
1920 C C   . ARG A 243 ? 0.6031 0.4061 0.5787 0.1117  -0.1316 0.0179  258 ARG A C   
1921 O O   . ARG A 243 ? 0.6376 0.4477 0.6324 0.1189  -0.1463 0.0199  258 ARG A O   
1922 C CB  . ARG A 243 ? 0.6775 0.4565 0.6721 0.1143  -0.1181 0.0074  258 ARG A CB  
1923 C CG  . ARG A 243 ? 0.8196 0.6098 0.8573 0.1265  -0.1213 -0.0073 258 ARG A CG  
1924 C CD  . ARG A 243 ? 1.0103 0.7806 1.0717 0.1368  -0.1400 0.0028  258 ARG A CD  
1925 N NE  . ARG A 243 ? 1.1868 0.9285 1.2336 0.1324  -0.1411 0.0137  258 ARG A NE  
1926 C CZ  . ARG A 243 ? 1.2556 0.9814 1.3252 0.1366  -0.1374 0.0047  258 ARG A CZ  
1927 N NH1 . ARG A 243 ? 1.1707 0.9060 1.2806 0.1467  -0.1325 -0.0162 258 ARG A NH1 
1928 N NH2 . ARG A 243 ? 1.2951 0.9957 1.3475 0.1296  -0.1375 0.0153  258 ARG A NH2 
1929 N N   . ALA A 244 ? 0.5844 0.4009 0.5440 0.1039  -0.1161 0.0098  259 ALA A N   
1930 C CA  . ALA A 244 ? 0.6482 0.4865 0.6117 0.1029  -0.1146 0.0023  259 ALA A CA  
1931 C C   . ALA A 244 ? 0.6476 0.4864 0.5947 0.1004  -0.1298 0.0144  259 ALA A C   
1932 O O   . ALA A 244 ? 0.6044 0.4583 0.5676 0.1039  -0.1389 0.0106  259 ALA A O   
1933 C CB  . ALA A 244 ? 0.5549 0.4022 0.5017 0.0941  -0.0964 -0.0048 259 ALA A CB  
1934 N N   . THR A 245 ? 0.6424 0.4665 0.5569 0.0931  -0.1324 0.0284  260 THR A N   
1935 C CA  . THR A 245 ? 0.6521 0.4777 0.5448 0.0880  -0.1458 0.0393  260 THR A CA  
1936 C C   . THR A 245 ? 0.6699 0.4922 0.5806 0.0961  -0.1688 0.0492  260 THR A C   
1937 O O   . THR A 245 ? 0.6584 0.4939 0.5707 0.0960  -0.1818 0.0506  260 THR A O   
1938 C CB  . THR A 245 ? 0.6707 0.4826 0.5245 0.0771  -0.1415 0.0512  260 THR A CB  
1939 O OG1 . THR A 245 ? 0.6182 0.4355 0.4609 0.0709  -0.1213 0.0415  260 THR A OG1 
1940 C CG2 . THR A 245 ? 0.7378 0.5528 0.5644 0.0694  -0.1541 0.0610  260 THR A CG2 
1941 N N   . VAL A 246 ? 0.6789 0.4840 0.6063 0.1034  -0.1750 0.0560  261 VAL A N   
1942 C CA  . VAL A 246 ? 0.6808 0.4801 0.6291 0.1125  -0.1987 0.0678  261 VAL A CA  
1943 C C   . VAL A 246 ? 0.8003 0.6218 0.7910 0.1234  -0.2038 0.0536  261 VAL A C   
1944 O O   . VAL A 246 ? 0.7322 0.5641 0.7321 0.1266  -0.2232 0.0601  261 VAL A O   
1945 C CB  . VAL A 246 ? 0.7999 0.5727 0.7610 0.1183  -0.2027 0.0768  261 VAL A CB  
1946 C CG1 . VAL A 246 ? 0.7965 0.5652 0.7963 0.1322  -0.2253 0.0837  261 VAL A CG1 
1947 C CG2 . VAL A 246 ? 0.6736 0.4254 0.5925 0.1060  -0.2039 0.0963  261 VAL A CG2 
1948 N N   . GLU A 247 ? 0.6647 0.4963 0.6806 0.1278  -0.1863 0.0336  262 GLU A N   
1949 C CA  . GLU A 247 ? 0.7315 0.5846 0.7925 0.1382  -0.1893 0.0190  262 GLU A CA  
1950 C C   . GLU A 247 ? 0.6930 0.5721 0.7502 0.1324  -0.1890 0.0117  262 GLU A C   
1951 O O   . GLU A 247 ? 0.7286 0.6261 0.8179 0.1394  -0.2014 0.0074  262 GLU A O   
1952 C CB  . GLU A 247 ? 0.7084 0.5648 0.7949 0.1426  -0.1692 -0.0007 262 GLU A CB  
1953 C CG  . GLU A 247 ? 0.9458 0.7774 1.0466 0.1500  -0.1718 0.0030  262 GLU A CG  
1954 C CD  . GLU A 247 ? 1.1489 0.9867 1.2811 0.1552  -0.1543 -0.0196 262 GLU A CD  
1955 O OE1 . GLU A 247 ? 1.1697 1.0330 1.3161 0.1540  -0.1418 -0.0370 262 GLU A OE1 
1956 O OE2 . GLU A 247 ? 1.2471 1.0642 1.3888 0.1592  -0.1526 -0.0205 262 GLU A OE2 
1957 N N   . SER A 248 ? 0.6291 0.5103 0.6507 0.1199  -0.1755 0.0099  263 SER A N   
1958 C CA  . SER A 248 ? 0.6655 0.5683 0.6831 0.1132  -0.1746 0.0023  263 SER A CA  
1959 C C   . SER A 248 ? 0.7503 0.6554 0.7496 0.1090  -0.1960 0.0154  263 SER A C   
1960 O O   . SER A 248 ? 0.7447 0.6694 0.7474 0.1044  -0.1998 0.0083  263 SER A O   
1961 C CB  . SER A 248 ? 0.6769 0.5788 0.6655 0.1017  -0.1536 -0.0040 263 SER A CB  
1962 O OG  . SER A 248 ? 0.7050 0.5877 0.6549 0.0950  -0.1535 0.0091  263 SER A OG  
1963 N N   . HIS A 249 ? 0.7199 0.6056 0.6980 0.1088  -0.2100 0.0343  264 HIS A N   
1964 C CA  . HIS A 249 ? 0.8247 0.7128 0.7779 0.1020  -0.2303 0.0481  264 HIS A CA  
1965 C C   . HIS A 249 ? 0.9170 0.7994 0.8909 0.1120  -0.2575 0.0647  264 HIS A C   
1966 O O   . HIS A 249 ? 0.9321 0.8012 0.8764 0.1065  -0.2734 0.0850  264 HIS A O   
1967 C CB  . HIS A 249 ? 0.8239 0.6960 0.7244 0.0883  -0.2233 0.0582  264 HIS A CB  
1968 C CG  . HIS A 249 ? 0.8812 0.7616 0.7614 0.0779  -0.2020 0.0433  264 HIS A CG  
1969 N ND1 . HIS A 249 ? 0.8715 0.7506 0.7617 0.0795  -0.1791 0.0304  264 HIS A ND1 
1970 C CD2 . HIS A 249 ? 0.8825 0.7727 0.7354 0.0658  -0.2007 0.0387  264 HIS A CD2 
1971 C CE1 . HIS A 249 ? 0.8040 0.6901 0.6758 0.0698  -0.1656 0.0205  264 HIS A CE1 
1972 N NE2 . HIS A 249 ? 0.8795 0.7719 0.7295 0.0616  -0.1774 0.0239  264 HIS A NE2 
1973 N N   . GLU A 250 ? 0.9445 0.8377 0.9706 0.1264  -0.2630 0.0563  265 GLU A N   
1974 C CA  . GLU A 250 ? 1.0648 0.9539 1.1206 0.1385  -0.2901 0.0711  265 GLU A CA  
1975 C C   . GLU A 250 ? 1.0407 0.9410 1.0787 0.1323  -0.3169 0.0862  265 GLU A C   
1976 O O   . GLU A 250 ? 1.1170 1.0048 1.1544 0.1362  -0.3419 0.1087  265 GLU A O   
1977 C CB  . GLU A 250 ? 1.0613 0.9678 1.1811 0.1545  -0.2894 0.0544  265 GLU A CB  
1978 C CG  . GLU A 250 ? 1.0455 0.9438 1.1844 0.1600  -0.2639 0.0376  265 GLU A CG  
1979 C CD  . GLU A 250 ? 1.2141 1.0827 1.3636 0.1692  -0.2695 0.0490  265 GLU A CD  
1980 O OE1 . GLU A 250 ? 1.2817 1.1278 1.4002 0.1647  -0.2844 0.0726  265 GLU A OE1 
1981 O OE2 . GLU A 250 ? 1.1933 1.0609 1.3823 0.1799  -0.2584 0.0338  265 GLU A OE2 
1982 N N   . SER A 251 ? 1.1188 1.0419 1.1415 0.1216  -0.3126 0.0748  266 SER A N   
1983 C CA  . SER A 251 ? 1.0976 1.0380 1.1091 0.1150  -0.3378 0.0838  266 SER A CA  
1984 C C   . SER A 251 ? 1.1376 1.0690 1.0836 0.0960  -0.3391 0.0952  266 SER A C   
1985 O O   . SER A 251 ? 1.2346 1.1766 1.1623 0.0886  -0.3628 0.1068  266 SER A O   
1986 C CB  . SER A 251 ? 1.2353 1.2088 1.2752 0.1140  -0.3335 0.0618  266 SER A CB  
1987 O OG  . SER A 251 ? 1.3105 1.2926 1.4044 0.1280  -0.3209 0.0456  266 SER A OG  
1988 N N   . SER A 252 ? 1.0516 0.9657 0.9625 0.0875  -0.3147 0.0916  267 SER A N   
1989 C CA  . SER A 252 ? 1.1419 1.0484 0.9929 0.0694  -0.3127 0.1000  267 SER A CA  
1990 C C   . SER A 252 ? 1.1033 0.9862 0.9296 0.0677  -0.3286 0.1280  267 SER A C   
1991 O O   . SER A 252 ? 1.0801 0.9446 0.9313 0.0799  -0.3308 0.1375  267 SER A O   
1992 C CB  . SER A 252 ? 1.0833 0.9829 0.9119 0.0615  -0.2799 0.0842  267 SER A CB  
1993 O OG  . SER A 252 ? 1.1737 1.0885 1.0351 0.0668  -0.2637 0.0613  267 SER A OG  
1994 N N   . LEU A 253 ? 1.1279 1.0112 0.9047 0.0513  -0.3397 0.1411  268 LEU A N   
1995 C CA  . LEU A 253 ? 1.0729 0.9325 0.8153 0.0446  -0.3501 0.1682  268 LEU A CA  
1996 C C   . LEU A 253 ? 1.1817 1.0241 0.8929 0.0356  -0.3210 0.1636  268 LEU A C   
1997 O O   . LEU A 253 ? 1.2315 1.0501 0.9297 0.0343  -0.3218 0.1821  268 LEU A O   
1998 C CB  . LEU A 253 ? 1.0392 0.9086 0.7373 0.0282  -0.3736 0.1843  268 LEU A CB  
1999 C CG  . LEU A 253 ? 0.9734 0.8668 0.7022 0.0349  -0.4014 0.1862  268 LEU A CG  
2000 C CD1 . LEU A 253 ? 1.0297 0.9396 0.7165 0.0162  -0.4122 0.1952  268 LEU A CD1 
2001 C CD2 . LEU A 253 ? 1.0816 0.9664 0.8625 0.0540  -0.4155 0.2012  268 LEU A CD2 
2002 N N   . ILE A 254 ? 1.3867 1.2413 1.0892 0.0295  -0.2960 0.1393  269 ILE A N   
2003 C CA  . ILE A 254 ? 1.3912 1.2358 1.0693 0.0213  -0.2669 0.1304  269 ILE A CA  
2004 C C   . ILE A 254 ? 1.1983 1.0349 0.9168 0.0360  -0.2491 0.1188  269 ILE A C   
2005 O O   . ILE A 254 ? 1.2430 1.0925 1.0001 0.0470  -0.2472 0.1034  269 ILE A O   
2006 C CB  . ILE A 254 ? 1.5434 1.4061 1.1964 0.0081  -0.2511 0.1093  269 ILE A CB  
2007 C CG1 . ILE A 254 ? 1.5454 1.4167 1.1506 -0.0100 -0.2658 0.1184  269 ILE A CG1 
2008 C CG2 . ILE A 254 ? 1.4477 1.3034 1.0923 0.0046  -0.2192 0.0952  269 ILE A CG2 
2009 C CD1 . ILE A 254 ? 1.5411 1.4348 1.1344 -0.0202 -0.2593 0.0951  269 ILE A CD1 
2010 N N   . LEU A 255 ? 1.0341 0.8510 0.7436 0.0349  -0.2360 0.1255  270 LEU A N   
2011 C CA  . LEU A 255 ? 0.9483 0.7618 0.6837 0.0431  -0.2132 0.1098  270 LEU A CA  
2012 C C   . LEU A 255 ? 0.8564 0.6746 0.5643 0.0314  -0.1888 0.0972  270 LEU A C   
2013 O O   . LEU A 255 ? 0.8360 0.6460 0.5080 0.0189  -0.1841 0.1068  270 LEU A O   
2014 C CB  . LEU A 255 ? 1.0096 0.8001 0.7591 0.0499  -0.2132 0.1217  270 LEU A CB  
2015 C CG  . LEU A 255 ? 1.0754 0.8596 0.8675 0.0660  -0.2314 0.1277  270 LEU A CG  
2016 C CD1 . LEU A 255 ? 0.9905 0.7497 0.7945 0.0708  -0.2276 0.1361  270 LEU A CD1 
2017 C CD2 . LEU A 255 ? 0.8943 0.6981 0.7268 0.0777  -0.2266 0.1064  270 LEU A CD2 
2018 N N   . PRO A 256 ? 0.7764 0.6074 0.5009 0.0344  -0.1729 0.0764  271 PRO A N   
2019 C CA  . PRO A 256 ? 0.8848 0.7183 0.5902 0.0255  -0.1498 0.0649  271 PRO A CA  
2020 C C   . PRO A 256 ? 0.8841 0.7026 0.5872 0.0256  -0.1368 0.0709  271 PRO A C   
2021 O O   . PRO A 256 ? 0.9141 0.7228 0.6419 0.0354  -0.1394 0.0753  271 PRO A O   
2022 C CB  . PRO A 256 ? 0.8033 0.6499 0.5366 0.0318  -0.1390 0.0450  271 PRO A CB  
2023 C CG  . PRO A 256 ? 0.9433 0.7993 0.7025 0.0400  -0.1569 0.0446  271 PRO A CG  
2024 C CD  . PRO A 256 ? 0.8708 0.7148 0.6343 0.0457  -0.1754 0.0634  271 PRO A CD  
2025 N N   . PRO A 257 ? 0.8133 0.6310 0.4897 0.0144  -0.1218 0.0693  272 PRO A N   
2026 C CA  . PRO A 257 ? 0.7762 0.5825 0.4516 0.0131  -0.1092 0.0744  272 PRO A CA  
2027 C C   . PRO A 257 ? 0.7800 0.5904 0.4837 0.0213  -0.0937 0.0605  272 PRO A C   
2028 O O   . PRO A 257 ? 0.7097 0.5312 0.4292 0.0260  -0.0894 0.0468  272 PRO A O   
2029 C CB  . PRO A 257 ? 0.8595 0.6693 0.4991 -0.0023 -0.0976 0.0744  272 PRO A CB  
2030 C CG  . PRO A 257 ? 0.9870 0.8128 0.6209 -0.0054 -0.0941 0.0582  272 PRO A CG  
2031 C CD  . PRO A 257 ? 0.9674 0.7962 0.6140 0.0017  -0.1153 0.0613  272 PRO A CD  
2032 N N   . ILE A 258 ? 0.6971 0.4982 0.4059 0.0216  -0.0857 0.0651  273 ILE A N   
2033 C CA  . ILE A 258 ? 0.7284 0.5341 0.4573 0.0262  -0.0706 0.0543  273 ILE A CA  
2034 C C   . ILE A 258 ? 0.7298 0.5411 0.4429 0.0170  -0.0541 0.0504  273 ILE A C   
2035 O O   . ILE A 258 ? 0.6965 0.5025 0.3879 0.0075  -0.0525 0.0595  273 ILE A O   
2036 C CB  . ILE A 258 ? 0.6863 0.4806 0.4330 0.0318  -0.0727 0.0597  273 ILE A CB  
2037 C CG1 . ILE A 258 ? 0.6340 0.4244 0.4003 0.0418  -0.0882 0.0610  273 ILE A CG1 
2038 C CG2 . ILE A 258 ? 0.6093 0.4103 0.3722 0.0342  -0.0580 0.0499  273 ILE A CG2 
2039 C CD1 . ILE A 258 ? 0.6531 0.4295 0.4371 0.0473  -0.0925 0.0655  273 ILE A CD1 
2040 N N   . LYS A 259 ? 0.6647 0.4871 0.3895 0.0192  -0.0420 0.0370  274 LYS A N   
2041 C CA  . LYS A 259 ? 0.6112 0.4407 0.3285 0.0125  -0.0258 0.0306  274 LYS A CA  
2042 C C   . LYS A 259 ? 0.6478 0.4793 0.3865 0.0168  -0.0160 0.0289  274 LYS A C   
2043 O O   . LYS A 259 ? 0.6065 0.4383 0.3657 0.0248  -0.0187 0.0266  274 LYS A O   
2044 C CB  . LYS A 259 ? 0.6624 0.5019 0.3794 0.0117  -0.0199 0.0164  274 LYS A CB  
2045 C CG  . LYS A 259 ? 0.8341 0.6746 0.5280 0.0056  -0.0302 0.0164  274 LYS A CG  
2046 C CD  . LYS A 259 ? 0.8398 0.6897 0.5332 0.0028  -0.0224 -0.0005 274 LYS A CD  
2047 C CE  . LYS A 259 ? 1.0392 0.8922 0.7101 -0.0040 -0.0349 -0.0013 274 LYS A CE  
2048 N NZ  . LYS A 259 ? 1.2366 1.0979 0.9081 -0.0076 -0.0279 -0.0199 274 LYS A NZ  
2049 N N   . VAL A 260 ? 0.6357 0.4701 0.3694 0.0103  -0.0052 0.0305  275 VAL A N   
2050 C CA  . VAL A 260 ? 0.6124 0.4515 0.3669 0.0133  0.0030  0.0292  275 VAL A CA  
2051 C C   . VAL A 260 ? 0.6626 0.5139 0.4211 0.0098  0.0182  0.0206  275 VAL A C   
2052 O O   . VAL A 260 ? 0.6425 0.4967 0.3826 0.0008  0.0249  0.0194  275 VAL A O   
2053 C CB  . VAL A 260 ? 0.6503 0.4821 0.4033 0.0094  0.0004  0.0398  275 VAL A CB  
2054 C CG1 . VAL A 260 ? 0.6263 0.4675 0.4001 0.0106  0.0091  0.0373  275 VAL A CG1 
2055 C CG2 . VAL A 260 ? 0.5983 0.4178 0.3560 0.0151  -0.0135 0.0454  275 VAL A CG2 
2056 N N   . MET A 261 ? 0.5592 0.4178 0.3421 0.0166  0.0238  0.0145  276 MET A N   
2057 C CA  . MET A 261 ? 0.6135 0.4838 0.4094 0.0155  0.0378  0.0066  276 MET A CA  
2058 C C   . MET A 261 ? 0.6130 0.4898 0.4295 0.0174  0.0398  0.0120  276 MET A C   
2059 O O   . MET A 261 ? 0.5885 0.4630 0.4169 0.0231  0.0321  0.0165  276 MET A O   
2060 C CB  . MET A 261 ? 0.5564 0.4296 0.3678 0.0219  0.0418  -0.0044 276 MET A CB  
2061 C CG  . MET A 261 ? 0.6974 0.5814 0.5356 0.0252  0.0534  -0.0101 276 MET A CG  
2062 S SD  . MET A 261 ? 0.8923 0.7772 0.7463 0.0297  0.0622  -0.0261 276 MET A SD  
2063 C CE  . MET A 261 ? 0.7618 0.6483 0.5823 0.0178  0.0700  -0.0369 276 MET A CE  
2064 N N   . VAL A 262 ? 0.6032 0.4899 0.4234 0.0116  0.0503  0.0108  277 VAL A N   
2065 C CA  . VAL A 262 ? 0.5776 0.4747 0.4213 0.0129  0.0525  0.0144  277 VAL A CA  
2066 C C   . VAL A 262 ? 0.5835 0.4951 0.4533 0.0172  0.0641  0.0048  277 VAL A C   
2067 O O   . VAL A 262 ? 0.6137 0.5326 0.4800 0.0121  0.0768  -0.0039 277 VAL A O   
2068 C CB  . VAL A 262 ? 0.6155 0.5142 0.4490 0.0023  0.0549  0.0212  277 VAL A CB  
2069 C CG1 . VAL A 262 ? 0.5851 0.4975 0.4456 0.0030  0.0562  0.0238  277 VAL A CG1 
2070 C CG2 . VAL A 262 ? 0.5969 0.4779 0.4076 -0.0012 0.0428  0.0306  277 VAL A CG2 
2071 N N   . ALA A 263 ? 0.5142 0.4299 0.4105 0.0263  0.0600  0.0063  278 ALA A N   
2072 C CA  . ALA A 263 ? 0.5333 0.4606 0.4611 0.0328  0.0684  -0.0010 278 ALA A CA  
2073 C C   . ALA A 263 ? 0.5896 0.5319 0.5445 0.0344  0.0663  0.0059  278 ALA A C   
2074 O O   . ALA A 263 ? 0.5095 0.4499 0.4641 0.0352  0.0544  0.0164  278 ALA A O   
2075 C CB  . ALA A 263 ? 0.4832 0.4018 0.4221 0.0419  0.0637  -0.0030 278 ALA A CB  
2076 N N   . LEU A 264 ? 0.5148 0.4737 0.4937 0.0344  0.0780  -0.0010 279 LEU A N   
2077 C CA  . LEU A 264 ? 0.4931 0.4700 0.5050 0.0371  0.0755  0.0048  279 LEU A CA  
2078 C C   . LEU A 264 ? 0.5888 0.5736 0.6409 0.0489  0.0787  -0.0003 279 LEU A C   
2079 O O   . LEU A 264 ? 0.5694 0.5595 0.6347 0.0506  0.0934  -0.0145 279 LEU A O   
2080 C CB  . LEU A 264 ? 0.5327 0.5258 0.5467 0.0270  0.0858  0.0018  279 LEU A CB  
2081 C CG  . LEU A 264 ? 0.5386 0.5546 0.5914 0.0293  0.0835  0.0061  279 LEU A CG  
2082 C CD1 . LEU A 264 ? 0.5065 0.5193 0.5564 0.0297  0.0647  0.0207  279 LEU A CD1 
2083 C CD2 . LEU A 264 ? 0.4656 0.4997 0.5225 0.0177  0.0964  0.0012  279 LEU A CD2 
2084 N N   . GLY A 265 ? 0.5060 0.4914 0.5778 0.0565  0.0651  0.0112  280 GLY A N   
2085 C CA  . GLY A 265 ? 0.4633 0.4546 0.5770 0.0683  0.0647  0.0107  280 GLY A CA  
2086 C C   . GLY A 265 ? 0.5205 0.5340 0.6697 0.0711  0.0578  0.0198  280 GLY A C   
2087 O O   . GLY A 265 ? 0.4944 0.5215 0.6378 0.0627  0.0570  0.0227  280 GLY A O   
2088 N N   . GLU A 266 ? 0.4800 0.4971 0.6682 0.0828  0.0515  0.0251  281 GLU A N   
2089 C CA  . GLU A 266 ? 0.4790 0.5189 0.7057 0.0867  0.0419  0.0355  281 GLU A CA  
2090 C C   . GLU A 266 ? 0.4707 0.5130 0.6774 0.0801  0.0227  0.0537  281 GLU A C   
2091 O O   . GLU A 266 ? 0.4941 0.5582 0.7177 0.0768  0.0159  0.0600  281 GLU A O   
2092 C CB  . GLU A 266 ? 0.4899 0.5308 0.7654 0.1017  0.0379  0.0387  281 GLU A CB  
2093 C CG  . GLU A 266 ? 0.7542 0.7947 1.0574 0.1092  0.0579  0.0176  281 GLU A CG  
2094 C CD  . GLU A 266 ? 0.7749 0.8438 1.1079 0.1078  0.0718  0.0049  281 GLU A CD  
2095 O OE1 . GLU A 266 ? 0.8524 0.9436 1.2243 0.1124  0.0622  0.0145  281 GLU A OE1 
2096 O OE2 . GLU A 266 ? 0.7940 0.8648 1.1113 0.1009  0.0919  -0.0142 281 GLU A OE2 
2097 N N   . GLU A 267 ? 0.5098 0.5321 0.6822 0.0773  0.0144  0.0609  282 GLU A N   
2098 C CA  . GLU A 267 ? 0.4746 0.4993 0.6272 0.0704  -0.0025 0.0760  282 GLU A CA  
2099 C C   . GLU A 267 ? 0.4705 0.4814 0.5750 0.0597  -0.0009 0.0721  282 GLU A C   
2100 O O   . GLU A 267 ? 0.4556 0.4742 0.5448 0.0505  -0.0080 0.0763  282 GLU A O   
2101 C CB  . GLU A 267 ? 0.4836 0.5001 0.6457 0.0770  -0.0163 0.0911  282 GLU A CB  
2102 C CG  . GLU A 267 ? 0.5992 0.6169 0.7365 0.0688  -0.0330 0.1062  282 GLU A CG  
2103 C CD  . GLU A 267 ? 0.6496 0.6638 0.8035 0.0747  -0.0470 0.1241  282 GLU A CD  
2104 O OE1 . GLU A 267 ? 0.6423 0.6603 0.8384 0.0859  -0.0480 0.1277  282 GLU A OE1 
2105 O OE2 . GLU A 267 ? 0.7228 0.7299 0.8484 0.0677  -0.0564 0.1343  282 GLU A OE2 
2106 N N   . ASP A 268 ? 0.4778 0.4689 0.5606 0.0606  0.0082  0.0631  283 ASP A N   
2107 C CA  . ASP A 268 ? 0.4738 0.4503 0.5157 0.0527  0.0090  0.0595  283 ASP A CA  
2108 C C   . ASP A 268 ? 0.5285 0.5025 0.5563 0.0477  0.0220  0.0475  283 ASP A C   
2109 O O   . ASP A 268 ? 0.4726 0.4489 0.5137 0.0510  0.0341  0.0381  283 ASP A O   
2110 C CB  . ASP A 268 ? 0.5018 0.4590 0.5284 0.0563  0.0084  0.0589  283 ASP A CB  
2111 C CG  . ASP A 268 ? 0.5306 0.4870 0.5598 0.0575  -0.0045 0.0723  283 ASP A CG  
2112 O OD1 . ASP A 268 ? 0.5217 0.4927 0.5628 0.0557  -0.0145 0.0830  283 ASP A OD1 
2113 O OD2 . ASP A 268 ? 0.5464 0.4883 0.5645 0.0589  -0.0046 0.0724  283 ASP A OD2 
2114 N N   . LEU A 269 ? 0.4780 0.4455 0.4771 0.0390  0.0198  0.0475  284 LEU A N   
2115 C CA  . LEU A 269 ? 0.4653 0.4224 0.4410 0.0336  0.0289  0.0395  284 LEU A CA  
2116 C C   . LEU A 269 ? 0.5365 0.4747 0.4846 0.0334  0.0234  0.0398  284 LEU A C   
2117 O O   . LEU A 269 ? 0.5063 0.4416 0.4438 0.0302  0.0145  0.0446  284 LEU A O   
2118 C CB  . LEU A 269 ? 0.5002 0.4646 0.4706 0.0234  0.0306  0.0403  284 LEU A CB  
2119 C CG  . LEU A 269 ? 0.5777 0.5321 0.5249 0.0162  0.0402  0.0347  284 LEU A CG  
2120 C CD1 . LEU A 269 ? 0.6451 0.6135 0.6013 0.0071  0.0467  0.0346  284 LEU A CD1 
2121 C CD2 . LEU A 269 ? 0.6017 0.5363 0.5191 0.0126  0.0325  0.0377  284 LEU A CD2 
2122 N N   . SER A 270 ? 0.4921 0.4190 0.4298 0.0364  0.0288  0.0333  285 SER A N   
2123 C CA  . SER A 270 ? 0.4855 0.3974 0.4036 0.0377  0.0233  0.0330  285 SER A CA  
2124 C C   . SER A 270 ? 0.5173 0.4178 0.4103 0.0331  0.0260  0.0286  285 SER A C   
2125 O O   . SER A 270 ? 0.5064 0.4081 0.3955 0.0307  0.0347  0.0233  285 SER A O   
2126 C CB  . SER A 270 ? 0.4801 0.3883 0.4090 0.0448  0.0245  0.0304  285 SER A CB  
2127 O OG  . SER A 270 ? 0.5415 0.4595 0.4962 0.0492  0.0215  0.0368  285 SER A OG  
2128 N N   . ILE A 271 ? 0.4885 0.3788 0.3653 0.0317  0.0183  0.0308  286 ILE A N   
2129 C CA  . ILE A 271 ? 0.5431 0.4211 0.3980 0.0285  0.0171  0.0293  286 ILE A CA  
2130 C C   . ILE A 271 ? 0.5825 0.4524 0.4319 0.0333  0.0113  0.0267  286 ILE A C   
2131 O O   . ILE A 271 ? 0.5499 0.4187 0.4021 0.0351  0.0052  0.0281  286 ILE A O   
2132 C CB  . ILE A 271 ? 0.5788 0.4511 0.4247 0.0225  0.0125  0.0342  286 ILE A CB  
2133 C CG1 . ILE A 271 ? 0.6023 0.4854 0.4576 0.0165  0.0180  0.0367  286 ILE A CG1 
2134 C CG2 . ILE A 271 ? 0.5583 0.4168 0.3834 0.0191  0.0102  0.0357  286 ILE A CG2 
2135 C CD1 . ILE A 271 ? 0.6066 0.4860 0.4599 0.0104  0.0128  0.0406  286 ILE A CD1 
2136 N N   . LYS A 272 ? 0.5241 0.3903 0.3660 0.0344  0.0136  0.0217  287 LYS A N   
2137 C CA  . LYS A 272 ? 0.5843 0.4447 0.4220 0.0378  0.0080  0.0185  287 LYS A CA  
2138 C C   . LYS A 272 ? 0.5895 0.4408 0.4082 0.0352  0.0019  0.0198  287 LYS A C   
2139 O O   . LYS A 272 ? 0.5920 0.4420 0.3969 0.0303  0.0050  0.0197  287 LYS A O   
2140 C CB  . LYS A 272 ? 0.5697 0.4324 0.4145 0.0403  0.0133  0.0114  287 LYS A CB  
2141 C CG  . LYS A 272 ? 0.5790 0.4373 0.4206 0.0423  0.0078  0.0070  287 LYS A CG  
2142 C CD  . LYS A 272 ? 0.6779 0.5373 0.5311 0.0440  0.0134  -0.0001 287 LYS A CD  
2143 C CE  . LYS A 272 ? 0.7240 0.5820 0.5649 0.0404  0.0174  -0.0091 287 LYS A CE  
2144 N NZ  . LYS A 272 ? 0.9338 0.7911 0.7879 0.0415  0.0238  -0.0188 287 LYS A NZ  
2145 N N   . MET A 273 ? 0.5718 0.4178 0.3906 0.0380  -0.0068 0.0211  288 MET A N   
2146 C CA  . MET A 273 ? 0.5598 0.3970 0.3665 0.0377  -0.0156 0.0234  288 MET A CA  
2147 C C   . MET A 273 ? 0.5828 0.4224 0.3936 0.0418  -0.0204 0.0176  288 MET A C   
2148 O O   . MET A 273 ? 0.5740 0.4186 0.3990 0.0454  -0.0194 0.0134  288 MET A O   
2149 C CB  . MET A 273 ? 0.5297 0.3592 0.3400 0.0388  -0.0221 0.0278  288 MET A CB  
2150 C CG  . MET A 273 ? 0.5330 0.3508 0.3334 0.0389  -0.0327 0.0333  288 MET A CG  
2151 S SD  . MET A 273 ? 0.5961 0.4027 0.4085 0.0419  -0.0395 0.0352  288 MET A SD  
2152 C CE  . MET A 273 ? 0.5269 0.3325 0.3362 0.0340  -0.0311 0.0390  288 MET A CE  
2153 N N   . SER A 274 ? 0.5667 0.4036 0.3641 0.0398  -0.0258 0.0176  289 SER A N   
2154 C CA  . SER A 274 ? 0.5718 0.4129 0.3727 0.0420  -0.0309 0.0112  289 SER A CA  
2155 C C   . SER A 274 ? 0.6167 0.4532 0.4115 0.0434  -0.0451 0.0160  289 SER A C   
2156 O O   . SER A 274 ? 0.6183 0.4491 0.3937 0.0385  -0.0499 0.0231  289 SER A O   
2157 C CB  . SER A 274 ? 0.6140 0.4595 0.4055 0.0372  -0.0242 0.0043  289 SER A CB  
2158 O OG  . SER A 274 ? 0.6511 0.5003 0.4552 0.0380  -0.0123 -0.0002 289 SER A OG  
2159 N N   . ASP A 275 ? 0.6046 0.4446 0.4165 0.0493  -0.0521 0.0126  290 ASP A N   
2160 C CA  . ASP A 275 ? 0.5870 0.4253 0.3992 0.0520  -0.0672 0.0163  290 ASP A CA  
2161 C C   . ASP A 275 ? 0.6204 0.4702 0.4401 0.0523  -0.0711 0.0078  290 ASP A C   
2162 O O   . ASP A 275 ? 0.5786 0.4357 0.4067 0.0512  -0.0616 -0.0011 290 ASP A O   
2163 C CB  . ASP A 275 ? 0.5885 0.4217 0.4196 0.0595  -0.0740 0.0189  290 ASP A CB  
2164 C CG  . ASP A 275 ? 0.6073 0.4512 0.4644 0.0649  -0.0693 0.0080  290 ASP A CG  
2165 O OD1 . ASP A 275 ? 0.5985 0.4540 0.4659 0.0657  -0.0707 0.0007  290 ASP A OD1 
2166 O OD2 . ASP A 275 ? 0.5712 0.4125 0.4384 0.0671  -0.0640 0.0062  290 ASP A OD2 
2167 N N   . ARG A 276 ? 0.6208 0.4717 0.4376 0.0531  -0.0863 0.0118  291 ARG A N   
2168 C CA  . ARG A 276 ? 0.6659 0.5293 0.4937 0.0538  -0.0941 0.0044  291 ARG A CA  
2169 C C   . ARG A 276 ? 0.6811 0.5477 0.5343 0.0629  -0.1069 0.0065  291 ARG A C   
2170 O O   . ARG A 276 ? 0.6932 0.5647 0.5491 0.0643  -0.1232 0.0100  291 ARG A O   
2171 C CB  . ARG A 276 ? 0.6606 0.5263 0.4630 0.0456  -0.1025 0.0064  291 ARG A CB  
2172 C CG  . ARG A 276 ? 0.8128 0.6764 0.5936 0.0368  -0.0876 0.0008  291 ARG A CG  
2173 C CD  . ARG A 276 ? 0.9110 0.7811 0.6697 0.0271  -0.0924 -0.0043 291 ARG A CD  
2174 N NE  . ARG A 276 ? 1.0673 0.9354 0.8094 0.0195  -0.0758 -0.0123 291 ARG A NE  
2175 C CZ  . ARG A 276 ? 1.2264 1.1006 0.9551 0.0107  -0.0724 -0.0242 291 ARG A CZ  
2176 N NH1 . ARG A 276 ? 1.1264 1.0099 0.8541 0.0073  -0.0851 -0.0292 291 ARG A NH1 
2177 N NH2 . ARG A 276 ? 1.2380 1.1098 0.9562 0.0052  -0.0557 -0.0327 291 ARG A NH2 
2178 N N   . GLY A 277 ? 0.6401 0.5046 0.5128 0.0691  -0.0999 0.0038  292 GLY A N   
2179 C CA  . GLY A 277 ? 0.6263 0.4932 0.5270 0.0785  -0.1090 0.0029  292 GLY A CA  
2180 C C   . GLY A 277 ? 0.5751 0.4605 0.5051 0.0817  -0.1055 -0.0106 292 GLY A C   
2181 O O   . GLY A 277 ? 0.5516 0.4413 0.5088 0.0892  -0.1061 -0.0159 292 GLY A O   
2182 N N   . GLY A 278 ? 0.5300 0.4266 0.4562 0.0753  -0.1007 -0.0173 293 GLY A N   
2183 C CA  . GLY A 278 ? 0.5538 0.4691 0.5069 0.0761  -0.0989 -0.0290 293 GLY A CA  
2184 C C   . GLY A 278 ? 0.5332 0.4539 0.4944 0.0728  -0.0805 -0.0374 293 GLY A C   
2185 O O   . GLY A 278 ? 0.5892 0.5248 0.5663 0.0693  -0.0760 -0.0463 293 GLY A O   
2186 N N   . GLY A 279 ? 0.4968 0.4065 0.4470 0.0725  -0.0703 -0.0340 294 GLY A N   
2187 C CA  . GLY A 279 ? 0.5147 0.4290 0.4665 0.0673  -0.0546 -0.0389 294 GLY A CA  
2188 C C   . GLY A 279 ? 0.5790 0.5076 0.5566 0.0695  -0.0491 -0.0488 294 GLY A C   
2189 O O   . GLY A 279 ? 0.5544 0.4905 0.5538 0.0765  -0.0573 -0.0536 294 GLY A O   
2190 N N   . VAL A 280 ? 0.4948 0.4279 0.4704 0.0633  -0.0352 -0.0516 295 VAL A N   
2191 C CA  . VAL A 280 ? 0.5098 0.4595 0.5056 0.0615  -0.0262 -0.0624 295 VAL A CA  
2192 C C   . VAL A 280 ? 0.5348 0.4916 0.5254 0.0505  -0.0147 -0.0622 295 VAL A C   
2193 O O   . VAL A 280 ? 0.5074 0.4528 0.4786 0.0458  -0.0125 -0.0531 295 VAL A O   
2194 C CB  . VAL A 280 ? 0.5577 0.5039 0.5520 0.0635  -0.0202 -0.0652 295 VAL A CB  
2195 C CG1 . VAL A 280 ? 0.5413 0.4797 0.5475 0.0745  -0.0310 -0.0666 295 VAL A CG1 
2196 C CG2 . VAL A 280 ? 0.5817 0.5150 0.5486 0.0579  -0.0149 -0.0552 295 VAL A CG2 
2197 N N   . PRO A 281 ? 0.4963 0.4720 0.5058 0.0458  -0.0071 -0.0720 296 PRO A N   
2198 C CA  . PRO A 281 ? 0.5114 0.4922 0.5148 0.0335  0.0040  -0.0696 296 PRO A CA  
2199 C C   . PRO A 281 ? 0.5585 0.5316 0.5402 0.0278  0.0124  -0.0616 296 PRO A C   
2200 O O   . PRO A 281 ? 0.5312 0.5037 0.5085 0.0309  0.0140  -0.0640 296 PRO A O   
2201 C CB  . PRO A 281 ? 0.5486 0.5538 0.5779 0.0291  0.0114  -0.0828 296 PRO A CB  
2202 C CG  . PRO A 281 ? 0.5600 0.5727 0.6079 0.0398  0.0077  -0.0934 296 PRO A CG  
2203 C CD  . PRO A 281 ? 0.5693 0.5629 0.6085 0.0510  -0.0074 -0.0856 296 PRO A CD  
2204 N N   . LEU A 282 ? 0.5065 0.4737 0.4761 0.0190  0.0168  -0.0519 297 LEU A N   
2205 C CA  . LEU A 282 ? 0.5253 0.4855 0.4750 0.0134  0.0219  -0.0413 297 LEU A CA  
2206 C C   . LEU A 282 ? 0.5390 0.5142 0.4869 0.0073  0.0310  -0.0476 297 LEU A C   
2207 O O   . LEU A 282 ? 0.5166 0.4880 0.4496 0.0068  0.0317  -0.0440 297 LEU A O   
2208 C CB  . LEU A 282 ? 0.4993 0.4529 0.4436 0.0044  0.0251  -0.0303 297 LEU A CB  
2209 C CG  . LEU A 282 ? 0.5448 0.4941 0.4717 -0.0030 0.0291  -0.0169 297 LEU A CG  
2210 C CD1 . LEU A 282 ? 0.5307 0.4658 0.4464 0.0054  0.0221  -0.0097 297 LEU A CD1 
2211 C CD2 . LEU A 282 ? 0.5110 0.4547 0.4390 -0.0127 0.0322  -0.0063 297 LEU A CD2 
2212 N N   . ARG A 283 ? 0.5194 0.5132 0.4831 0.0018  0.0386  -0.0588 298 ARG A N   
2213 C CA  . ARG A 283 ? 0.5969 0.6083 0.5604 -0.0055 0.0498  -0.0687 298 ARG A CA  
2214 C C   . ARG A 283 ? 0.6222 0.6313 0.5853 0.0033  0.0475  -0.0775 298 ARG A C   
2215 O O   . ARG A 283 ? 0.5777 0.5945 0.5292 -0.0037 0.0555  -0.0821 298 ARG A O   
2216 C CB  . ARG A 283 ? 0.5740 0.6074 0.5628 -0.0095 0.0575  -0.0831 298 ARG A CB  
2217 C CG  . ARG A 283 ? 0.7691 0.8249 0.7631 -0.0171 0.0715  -0.0981 298 ARG A CG  
2218 C CD  . ARG A 283 ? 0.7697 0.8484 0.7932 -0.0208 0.0788  -0.1117 298 ARG A CD  
2219 N NE  . ARG A 283 ? 0.7301 0.8092 0.7837 -0.0051 0.0676  -0.1204 298 ARG A NE  
2220 C CZ  . ARG A 283 ? 0.7418 0.8298 0.8196 0.0064  0.0664  -0.1365 298 ARG A CZ  
2221 N NH1 . ARG A 283 ? 0.6857 0.7804 0.7605 0.0050  0.0762  -0.1478 298 ARG A NH1 
2222 N NH2 . ARG A 283 ? 0.6084 0.6986 0.7150 0.0192  0.0544  -0.1416 298 ARG A NH2 
2223 N N   . LYS A 284 ? 0.5337 0.5318 0.5080 0.0174  0.0364  -0.0797 299 LYS A N   
2224 C CA  . LYS A 284 ? 0.5663 0.5604 0.5446 0.0256  0.0341  -0.0884 299 LYS A CA  
2225 C C   . LYS A 284 ? 0.5897 0.5656 0.5440 0.0265  0.0290  -0.0769 299 LYS A C   
2226 O O   . LYS A 284 ? 0.5679 0.5401 0.5225 0.0299  0.0289  -0.0841 299 LYS A O   
2227 C CB  . LYS A 284 ? 0.5035 0.4946 0.5075 0.0398  0.0237  -0.0952 299 LYS A CB  
2228 C CG  . LYS A 284 ? 0.6586 0.6723 0.6934 0.0402  0.0294  -0.1111 299 LYS A CG  
2229 C CD  . LYS A 284 ? 0.6795 0.6918 0.7429 0.0550  0.0167  -0.1166 299 LYS A CD  
2230 C CE  . LYS A 284 ? 0.6888 0.7270 0.7892 0.0563  0.0229  -0.1345 299 LYS A CE  
2231 N NZ  . LYS A 284 ? 0.7301 0.7688 0.8598 0.0702  0.0068  -0.1357 299 LYS A NZ  
2232 N N   . ILE A 285 ? 0.5731 0.5383 0.5096 0.0231  0.0253  -0.0605 300 ILE A N   
2233 C CA  . ILE A 285 ? 0.5520 0.5024 0.4703 0.0246  0.0201  -0.0501 300 ILE A CA  
2234 C C   . ILE A 285 ? 0.6501 0.6076 0.5553 0.0162  0.0265  -0.0534 300 ILE A C   
2235 O O   . ILE A 285 ? 0.5666 0.5162 0.4665 0.0190  0.0233  -0.0550 300 ILE A O   
2236 C CB  . ILE A 285 ? 0.7129 0.6535 0.6199 0.0227  0.0164  -0.0338 300 ILE A CB  
2237 C CG1 . ILE A 285 ? 0.5921 0.5235 0.5080 0.0310  0.0091  -0.0325 300 ILE A CG1 
2238 C CG2 . ILE A 285 ? 0.7126 0.6439 0.6036 0.0221  0.0131  -0.0236 300 ILE A CG2 
2239 C CD1 . ILE A 285 ? 0.6826 0.6026 0.5987 0.0405  0.0009  -0.0336 300 ILE A CD1 
2240 N N   . GLU A 286 ? 0.5880 0.5607 0.4862 0.0040  0.0357  -0.0544 301 GLU A N   
2241 C CA  . GLU A 286 ? 0.6235 0.6054 0.5047 -0.0068 0.0416  -0.0575 301 GLU A CA  
2242 C C   . GLU A 286 ? 0.6617 0.6493 0.5537 -0.0039 0.0466  -0.0788 301 GLU A C   
2243 O O   . GLU A 286 ? 0.6657 0.6529 0.5457 -0.0081 0.0474  -0.0833 301 GLU A O   
2244 C CB  . GLU A 286 ? 0.7097 0.7078 0.5794 -0.0222 0.0506  -0.0536 301 GLU A CB  
2245 C CG  . GLU A 286 ? 0.9864 0.9992 0.8362 -0.0363 0.0582  -0.0600 301 GLU A CG  
2246 C CD  . GLU A 286 ? 1.1520 1.1836 0.9891 -0.0539 0.0690  -0.0579 301 GLU A CD  
2247 O OE1 . GLU A 286 ? 1.1330 1.1661 0.9798 -0.0552 0.0714  -0.0521 301 GLU A OE1 
2248 O OE2 . GLU A 286 ? 0.9823 1.0276 0.7984 -0.0679 0.0752  -0.0622 301 GLU A OE2 
2249 N N   A ARG A 287 ? 0.6528 0.6463 0.5702 0.0034  0.0497  -0.0929 302 ARG A N   
2250 N N   B ARG A 287 ? 0.6528 0.6464 0.5701 0.0033  0.0498  -0.0930 302 ARG A N   
2251 C CA  A ARG A 287 ? 0.6481 0.6444 0.5840 0.0094  0.0535  -0.1138 302 ARG A CA  
2252 C CA  B ARG A 287 ? 0.6481 0.6447 0.5832 0.0089  0.0538  -0.1140 302 ARG A CA  
2253 C C   A ARG A 287 ? 0.6015 0.5764 0.5371 0.0190  0.0430  -0.1108 302 ARG A C   
2254 C C   B ARG A 287 ? 0.6014 0.5763 0.5372 0.0191  0.0430  -0.1110 302 ARG A C   
2255 O O   A ARG A 287 ? 0.6165 0.5898 0.5540 0.0183  0.0463  -0.1241 302 ARG A O   
2256 O O   B ARG A 287 ? 0.6165 0.5895 0.5554 0.0189  0.0462  -0.1246 302 ARG A O   
2257 C CB  A ARG A 287 ? 0.6864 0.6914 0.6550 0.0183  0.0547  -0.1253 302 ARG A CB  
2258 C CB  B ARG A 287 ? 0.6868 0.6934 0.6545 0.0170  0.0562  -0.1268 302 ARG A CB  
2259 C CG  A ARG A 287 ? 0.8009 0.8115 0.7978 0.0259  0.0593  -0.1485 302 ARG A CG  
2260 C CG  B ARG A 287 ? 0.7952 0.8090 0.7886 0.0228  0.0625  -0.1510 302 ARG A CG  
2261 C CD  A ARG A 287 ? 0.8158 0.8387 0.8476 0.0343  0.0590  -0.1571 302 ARG A CD  
2262 C CD  B ARG A 287 ? 0.7944 0.7973 0.8197 0.0408  0.0507  -0.1530 302 ARG A CD  
2263 N NE  A ARG A 287 ? 0.7950 0.8389 0.8230 0.0222  0.0692  -0.1564 302 ARG A NE  
2264 N NE  B ARG A 287 ? 0.7162 0.7200 0.7696 0.0488  0.0542  -0.1743 302 ARG A NE  
2265 C CZ  A ARG A 287 ? 0.7358 0.7947 0.7910 0.0252  0.0703  -0.1622 302 ARG A CZ  
2266 C CZ  B ARG A 287 ? 0.6528 0.6402 0.7015 0.0512  0.0520  -0.1786 302 ARG A CZ  
2267 N NH1 A ARG A 287 ? 0.6261 0.6828 0.7149 0.0409  0.0604  -0.1685 302 ARG A NH1 
2268 N NH1 B ARG A 287 ? 0.6367 0.6094 0.6528 0.0448  0.0475  -0.1639 302 ARG A NH1 
2269 N NH2 A ARG A 287 ? 0.7056 0.7824 0.7547 0.0114  0.0807  -0.1607 302 ARG A NH2 
2270 N NH2 B ARG A 287 ? 0.7629 0.7486 0.8433 0.0603  0.0543  -0.1985 302 ARG A NH2 
2271 N N   . LEU A 288 ? 0.5342 0.4926 0.4661 0.0263  0.0313  -0.0939 303 LEU A N   
2272 C CA  . LEU A 288 ? 0.5419 0.4799 0.4736 0.0345  0.0216  -0.0893 303 LEU A CA  
2273 C C   . LEU A 288 ? 0.5354 0.4693 0.4452 0.0260  0.0222  -0.0849 303 LEU A C   
2274 O O   . LEU A 288 ? 0.5689 0.4894 0.4807 0.0294  0.0180  -0.0876 303 LEU A O   
2275 C CB  . LEU A 288 ? 0.4727 0.3975 0.4027 0.0418  0.0108  -0.0728 303 LEU A CB  
2276 C CG  . LEU A 288 ? 0.5513 0.4787 0.5017 0.0503  0.0062  -0.0750 303 LEU A CG  
2277 C CD1 . LEU A 288 ? 0.5410 0.4546 0.4837 0.0553  -0.0044 -0.0598 303 LEU A CD1 
2278 C CD2 . LEU A 288 ? 0.5736 0.4994 0.5502 0.0598  0.0037  -0.0890 303 LEU A CD2 
2279 N N   . PHE A 289 ? 0.5529 0.4974 0.4427 0.0147  0.0260  -0.0765 304 PHE A N   
2280 C CA  . PHE A 289 ? 0.5089 0.4530 0.3791 0.0059  0.0249  -0.0718 304 PHE A CA  
2281 C C   . PHE A 289 ? 0.5422 0.5010 0.4050 -0.0055 0.0342  -0.0885 304 PHE A C   
2282 O O   . PHE A 289 ? 0.5812 0.5412 0.4282 -0.0139 0.0328  -0.0878 304 PHE A O   
2283 C CB  . PHE A 289 ? 0.5532 0.5004 0.4067 0.0000  0.0212  -0.0516 304 PHE A CB  
2284 C CG  . PHE A 289 ? 0.5339 0.4656 0.3906 0.0091  0.0124  -0.0368 304 PHE A CG  
2285 C CD1 . PHE A 289 ? 0.4582 0.3796 0.3114 0.0108  0.0066  -0.0323 304 PHE A CD1 
2286 C CD2 . PHE A 289 ? 0.5225 0.4515 0.3855 0.0142  0.0110  -0.0286 304 PHE A CD2 
2287 C CE1 . PHE A 289 ? 0.5325 0.4423 0.3879 0.0176  0.0007  -0.0202 304 PHE A CE1 
2288 C CE2 . PHE A 289 ? 0.5585 0.4749 0.4231 0.0211  0.0047  -0.0177 304 PHE A CE2 
2289 C CZ  . PHE A 289 ? 0.5314 0.4390 0.3919 0.0227  0.0001  -0.0136 304 PHE A CZ  
2290 N N   . SER A 290 ? 0.5051 0.5071 0.4689 0.0837  0.0505  -0.0491 305 SER A N   
2291 C CA  . SER A 290 ? 0.5320 0.5524 0.4861 0.0892  0.0589  -0.0635 305 SER A CA  
2292 C C   . SER A 290 ? 0.5007 0.5142 0.4639 0.1030  0.0470  -0.0830 305 SER A C   
2293 O O   . SER A 290 ? 0.5169 0.5310 0.5053 0.1108  0.0399  -0.0923 305 SER A O   
2294 C CB  . SER A 290 ? 0.4756 0.5291 0.4415 0.0871  0.0758  -0.0690 305 SER A CB  
2295 O OG  . SER A 290 ? 0.5776 0.6520 0.5424 0.0963  0.0823  -0.0894 305 SER A OG  
2296 N N   . TYR A 291 ? 0.4808 0.4876 0.4243 0.1064  0.0436  -0.0901 306 TYR A N   
2297 C CA  . TYR A 291 ? 0.5687 0.5703 0.5208 0.1198  0.0330  -0.1116 306 TYR A CA  
2298 C C   . TYR A 291 ? 0.5958 0.6270 0.5663 0.1298  0.0422  -0.1324 306 TYR A C   
2299 O O   . TYR A 291 ? 0.4953 0.5226 0.4902 0.1419  0.0316  -0.1478 306 TYR A O   
2300 C CB  . TYR A 291 ? 0.5023 0.4965 0.4289 0.1212  0.0294  -0.1180 306 TYR A CB  
2301 C CG  . TYR A 291 ? 0.5086 0.4777 0.4199 0.1121  0.0202  -0.1001 306 TYR A CG  
2302 C CD1 . TYR A 291 ? 0.4983 0.4398 0.4205 0.1124  0.0032  -0.0970 306 TYR A CD1 
2303 C CD2 . TYR A 291 ? 0.5628 0.5365 0.4494 0.1029  0.0281  -0.0863 306 TYR A CD2 
2304 C CE1 . TYR A 291 ? 0.4899 0.4133 0.4013 0.1035  -0.0037 -0.0821 306 TYR A CE1 
2305 C CE2 . TYR A 291 ? 0.5220 0.4754 0.3989 0.0957  0.0191  -0.0715 306 TYR A CE2 
2306 C CZ  . TYR A 291 ? 0.5781 0.5088 0.4686 0.0961  0.0042  -0.0705 306 TYR A CZ  
2307 O OH  . TYR A 291 ? 0.5469 0.4620 0.4309 0.0887  -0.0033 -0.0578 306 TYR A OH  
2308 N N   . MET A 292 ? 0.5317 0.5932 0.4908 0.1251  0.0619  -0.1335 307 MET A N   
2309 C CA  . MET A 292 ? 0.5114 0.6068 0.4865 0.1344  0.0732  -0.1563 307 MET A CA  
2310 C C   . MET A 292 ? 0.5530 0.6586 0.5659 0.1385  0.0715  -0.1594 307 MET A C   
2311 O O   . MET A 292 ? 0.5685 0.6848 0.6072 0.1531  0.0665  -0.1819 307 MET A O   
2312 C CB  . MET A 292 ? 0.5244 0.6520 0.4779 0.1253  0.0964  -0.1538 307 MET A CB  
2313 C CG  . MET A 292 ? 0.7112 0.8795 0.6823 0.1341  0.1107  -0.1789 307 MET A CG  
2314 S SD  . MET A 292 ? 0.7803 0.9897 0.7289 0.1187  0.1407  -0.1712 307 MET A SD  
2315 C CE  . MET A 292 ? 0.8929 1.1024 0.7970 0.1219  0.1430  -0.1816 307 MET A CE  
2316 N N   . TYR A 293 ? 0.5095 0.6119 0.5272 0.1264  0.0744  -0.1382 308 TYR A N   
2317 C CA  . TYR A 293 ? 0.6074 0.7220 0.6606 0.1296  0.0724  -0.1416 308 TYR A CA  
2318 C C   . TYR A 293 ? 0.6338 0.7186 0.7050 0.1401  0.0484  -0.1445 308 TYR A C   
2319 O O   . TYR A 293 ? 0.6230 0.7179 0.7260 0.1492  0.0422  -0.1554 308 TYR A O   
2320 C CB  . TYR A 293 ? 0.5523 0.6721 0.6054 0.1133  0.0817  -0.1196 308 TYR A CB  
2321 C CG  . TYR A 293 ? 0.6189 0.7671 0.6559 0.1010  0.1051  -0.1143 308 TYR A CG  
2322 C CD1 . TYR A 293 ? 0.6202 0.8057 0.6627 0.1055  0.1210  -0.1333 308 TYR A CD1 
2323 C CD2 . TYR A 293 ? 0.6821 0.8191 0.6975 0.0847  0.1109  -0.0901 308 TYR A CD2 
2324 C CE1 . TYR A 293 ? 0.7530 0.9644 0.7769 0.0919  0.1432  -0.1260 308 TYR A CE1 
2325 C CE2 . TYR A 293 ? 0.6854 0.8438 0.6835 0.0722  0.1306  -0.0823 308 TYR A CE2 
2326 C CZ  . TYR A 293 ? 0.8226 1.0181 0.8235 0.0748  0.1471  -0.0990 308 TYR A CZ  
2327 O OH  . TYR A 293 ? 0.7966 1.0130 0.7773 0.0600  0.1672  -0.0887 308 TYR A OH  
2328 N N   . SER A 294 ? 0.5989 0.6480 0.6508 0.1386  0.0344  -0.1350 309 SER A N   
2329 C CA  . SER A 294 ? 0.5485 0.5659 0.6124 0.1459  0.0116  -0.1349 309 SER A CA  
2330 C C   . SER A 294 ? 0.6145 0.6240 0.6878 0.1622  -0.0005 -0.1579 309 SER A C   
2331 O O   . SER A 294 ? 0.5731 0.5511 0.6531 0.1672  -0.0210 -0.1565 309 SER A O   
2332 C CB  . SER A 294 ? 0.5906 0.5752 0.6311 0.1346  0.0033  -0.1133 309 SER A CB  
2333 O OG  . SER A 294 ? 0.5518 0.5409 0.5841 0.1208  0.0128  -0.0936 309 SER A OG  
2334 N N   . THR A 295 ? 0.5695 0.6057 0.6426 0.1700  0.0113  -0.1790 310 THR A N   
2335 C CA  . THR A 295 ? 0.5546 0.5832 0.6337 0.1857  0.0004  -0.2035 310 THR A CA  
2336 C C   . THR A 295 ? 0.6907 0.7421 0.8069 0.2027  -0.0017 -0.2280 310 THR A C   
2337 O O   . THR A 295 ? 0.6940 0.7863 0.8219 0.2027  0.0170  -0.2362 310 THR A O   
2338 C CB  . THR A 295 ? 0.5633 0.6069 0.6149 0.1846  0.0136  -0.2141 310 THR A CB  
2339 O OG1 . THR A 295 ? 0.5917 0.6132 0.6114 0.1704  0.0125  -0.1925 310 THR A OG1 
2340 C CG2 . THR A 295 ? 0.5627 0.5995 0.6215 0.2019  0.0018  -0.2433 310 THR A CG2 
2341 N N   . ALA A 296 ? 0.7677 0.7929 0.9034 0.2171  -0.0248 -0.2403 311 ALA A N   
2342 C CA  . ALA A 296 ? 0.7067 0.7486 0.8812 0.2367  -0.0318 -0.2662 311 ALA A CA  
2343 C C   . ALA A 296 ? 0.6936 0.7032 0.8757 0.2524  -0.0550 -0.2845 311 ALA A C   
2344 O O   . ALA A 296 ? 0.6965 0.6701 0.8553 0.2456  -0.0660 -0.2737 311 ALA A O   
2345 C CB  . ALA A 296 ? 0.7491 0.7884 0.9498 0.2368  -0.0416 -0.2541 311 ALA A CB  
2346 N N   . PRO A 297 ? 0.9253 0.9480 1.1361 0.2661  -0.0624 -0.3058 312 PRO A N   
2347 C CA  . PRO A 297 ? 0.9448 0.9351 1.1597 0.2730  -0.0858 -0.3147 312 PRO A CA  
2348 C C   . PRO A 297 ? 1.0112 0.9501 1.2275 0.2689  -0.1129 -0.2930 312 PRO A C   
2349 O O   . PRO A 297 ? 1.0296 0.9618 1.2536 0.2649  -0.1176 -0.2751 312 PRO A O   
2350 C CB  . PRO A 297 ? 0.8269 0.8468 1.0744 0.2862  -0.0870 -0.3383 312 PRO A CB  
2351 C CG  . PRO A 297 ? 0.8099 0.8843 1.0594 0.2840  -0.0568 -0.3467 312 PRO A CG  
2352 C CD  . PRO A 297 ? 0.7621 0.8353 0.9981 0.2719  -0.0463 -0.3228 312 PRO A CD  
2353 N N   . THR A 298 ? 1.1792 1.0827 1.3873 0.2689  -0.1311 -0.2945 313 THR A N   
2354 C CA  . THR A 298 ? 1.2037 1.0561 1.4041 0.2603  -0.1544 -0.2716 313 THR A CA  
2355 C C   . THR A 298 ? 1.2176 1.0552 1.4350 0.2598  -0.1703 -0.2551 313 THR A C   
2356 O O   . THR A 298 ? 1.2146 1.0668 1.4586 0.2708  -0.1773 -0.2675 313 THR A O   
2357 C CB  . THR A 298 ? 1.2639 1.0880 1.4654 0.2634  -0.1739 -0.2819 313 THR A CB  
2358 O OG1 . THR A 298 ? 1.2875 1.1244 1.4716 0.2638  -0.1612 -0.2978 313 THR A OG1 
2359 C CG2 . THR A 298 ? 1.3917 1.1656 1.5818 0.2506  -0.1946 -0.2564 313 THR A CG2 
2360 N N   . THR A 306 ? 1.3340 0.9889 1.4163 0.1493  -0.2144 -0.0434 321 THR A N   
2361 C CA  . THR A 306 ? 1.3676 1.0446 1.4344 0.1378  -0.1975 -0.0291 321 THR A CA  
2362 C C   . THR A 306 ? 1.3095 1.0321 1.3873 0.1445  -0.1746 -0.0454 321 THR A C   
2363 O O   . THR A 306 ? 1.2181 0.9612 1.3071 0.1496  -0.1721 -0.0473 321 THR A O   
2364 C CB  . THR A 306 ? 1.5120 1.1781 1.5767 0.1367  -0.2120 -0.0137 321 THR A CB  
2365 O OG1 . THR A 306 ? 1.5408 1.2118 1.6327 0.1545  -0.2260 -0.0294 321 THR A OG1 
2366 C CG2 . THR A 306 ? 1.5357 1.1663 1.5772 0.1201  -0.2254 0.0101  321 THR A CG2 
2367 N N   . PRO A 307 ? 1.0554 0.7936 1.1292 0.1435  -0.1585 -0.0564 322 PRO A N   
2368 C CA  . PRO A 307 ? 1.0007 0.7809 1.0812 0.1477  -0.1361 -0.0694 322 PRO A CA  
2369 C C   . PRO A 307 ? 0.8298 0.6261 0.8924 0.1321  -0.1192 -0.0523 322 PRO A C   
2370 O O   . PRO A 307 ? 0.9536 0.7400 0.9948 0.1182  -0.1139 -0.0386 322 PRO A O   
2371 C CB  . PRO A 307 ? 0.9110 0.6960 0.9880 0.1509  -0.1283 -0.0847 322 PRO A CB  
2372 C CG  . PRO A 307 ? 1.0385 0.7891 1.0982 0.1394  -0.1390 -0.0712 322 PRO A CG  
2373 C CD  . PRO A 307 ? 1.1305 0.8488 1.1927 0.1375  -0.1607 -0.0567 322 PRO A CD  
2374 N N   . LEU A 308 ? 0.6832 0.5046 0.7570 0.1347  -0.1117 -0.0542 323 LEU A N   
2375 C CA  . LEU A 308 ? 0.7612 0.5964 0.8212 0.1213  -0.0977 -0.0399 323 LEU A CA  
2376 C C   . LEU A 308 ? 0.6468 0.5110 0.7035 0.1185  -0.0749 -0.0466 323 LEU A C   
2377 O O   . LEU A 308 ? 0.6057 0.4836 0.6709 0.1273  -0.0689 -0.0630 323 LEU A O   
2378 C CB  . LEU A 308 ? 0.7120 0.5571 0.7856 0.1239  -0.1033 -0.0375 323 LEU A CB  
2379 C CG  . LEU A 308 ? 0.8518 0.6676 0.9256 0.1266  -0.1277 -0.0287 323 LEU A CG  
2380 C CD1 . LEU A 308 ? 0.8657 0.6972 0.9603 0.1342  -0.1347 -0.0333 323 LEU A CD1 
2381 C CD2 . LEU A 308 ? 0.7734 0.5669 0.8179 0.1103  -0.1300 -0.0066 323 LEU A CD2 
2382 N N   . ALA A 309 ? 0.5829 0.4560 0.6263 0.1062  -0.0626 -0.0339 324 ALA A N   
2383 C CA  . ALA A 309 ? 0.6079 0.5066 0.6479 0.1023  -0.0424 -0.0369 324 ALA A CA  
2384 C C   . ALA A 309 ? 0.6258 0.5528 0.6886 0.1122  -0.0355 -0.0535 324 ALA A C   
2385 O O   . ALA A 309 ? 0.5739 0.5076 0.6574 0.1184  -0.0431 -0.0582 324 ALA A O   
2386 C CB  . ALA A 309 ? 0.4954 0.3982 0.5251 0.0898  -0.0343 -0.0222 324 ALA A CB  
2387 N N   . GLY A 310 ? 0.5452 0.4896 0.6044 0.1141  -0.0218 -0.0633 325 GLY A N   
2388 C CA  . GLY A 310 ? 0.5306 0.5058 0.6099 0.1227  -0.0123 -0.0807 325 GLY A CA  
2389 C C   . GLY A 310 ? 0.6340 0.6086 0.7291 0.1390  -0.0221 -0.1013 325 GLY A C   
2390 O O   . GLY A 310 ? 0.6193 0.6235 0.7311 0.1470  -0.0123 -0.1190 325 GLY A O   
2391 N N   . PHE A 311 ? 0.5715 0.5141 0.6625 0.1438  -0.0407 -0.1005 326 PHE A N   
2392 C CA  . PHE A 311 ? 0.6486 0.5861 0.7575 0.1603  -0.0532 -0.1208 326 PHE A CA  
2393 C C   . PHE A 311 ? 0.6499 0.5601 0.7420 0.1611  -0.0621 -0.1230 326 PHE A C   
2394 O O   . PHE A 311 ? 0.7376 0.6376 0.8433 0.1747  -0.0750 -0.1402 326 PHE A O   
2395 C CB  . PHE A 311 ? 0.6485 0.5722 0.7804 0.1689  -0.0737 -0.1210 326 PHE A CB  
2396 C CG  . PHE A 311 ? 0.7559 0.7094 0.9093 0.1697  -0.0669 -0.1227 326 PHE A CG  
2397 C CD1 . PHE A 311 ? 0.8185 0.8066 1.0007 0.1822  -0.0596 -0.1453 326 PHE A CD1 
2398 C CD2 . PHE A 311 ? 0.6931 0.6426 0.8390 0.1575  -0.0669 -0.1032 326 PHE A CD2 
2399 C CE1 . PHE A 311 ? 0.7758 0.7938 0.9813 0.1816  -0.0532 -0.1474 326 PHE A CE1 
2400 C CE2 . PHE A 311 ? 0.6972 0.6744 0.8645 0.1574  -0.0615 -0.1057 326 PHE A CE2 
2401 C CZ  . PHE A 311 ? 0.6346 0.6460 0.8326 0.1689  -0.0548 -0.1272 326 PHE A CZ  
2402 N N   . GLY A 312 ? 0.6914 0.5904 0.7569 0.1475  -0.0564 -0.1075 327 GLY A N   
2403 C CA  . GLY A 312 ? 0.5718 0.4516 0.6223 0.1468  -0.0620 -0.1110 327 GLY A CA  
2404 C C   . GLY A 312 ? 0.6164 0.5007 0.6412 0.1324  -0.0486 -0.0965 327 GLY A C   
2405 O O   . GLY A 312 ? 0.5753 0.4791 0.5951 0.1251  -0.0341 -0.0871 327 GLY A O   
2406 N N   . TYR A 313 ? 0.5818 0.4470 0.5922 0.1282  -0.0550 -0.0947 328 TYR A N   
2407 C CA  . TYR A 313 ? 0.6214 0.4915 0.6094 0.1167  -0.0444 -0.0835 328 TYR A CA  
2408 C C   . TYR A 313 ? 0.6133 0.4641 0.5931 0.1031  -0.0495 -0.0620 328 TYR A C   
2409 O O   . TYR A 313 ? 0.5281 0.3806 0.4926 0.0943  -0.0436 -0.0534 328 TYR A O   
2410 C CB  . TYR A 313 ? 0.5613 0.4292 0.5385 0.1206  -0.0467 -0.0973 328 TYR A CB  
2411 C CG  . TYR A 313 ? 0.5651 0.4578 0.5440 0.1326  -0.0377 -0.1194 328 TYR A CG  
2412 C CD1 . TYR A 313 ? 0.4964 0.4149 0.4880 0.1381  -0.0262 -0.1253 328 TYR A CD1 
2413 C CD2 . TYR A 313 ? 0.6333 0.5262 0.6007 0.1376  -0.0399 -0.1352 328 TYR A CD2 
2414 C CE1 . TYR A 313 ? 0.5618 0.5076 0.5550 0.1481  -0.0156 -0.1467 328 TYR A CE1 
2415 C CE2 . TYR A 313 ? 0.5744 0.4924 0.5405 0.1483  -0.0305 -0.1568 328 TYR A CE2 
2416 C CZ  . TYR A 313 ? 0.5787 0.5241 0.5576 0.1533  -0.0173 -0.1623 328 TYR A CZ  
2417 O OH  . TYR A 313 ? 0.6437 0.6179 0.6213 0.1630  -0.0060 -0.1847 328 TYR A OH  
2418 N N   . GLY A 314 ? 0.5541 0.3885 0.5435 0.1013  -0.0601 -0.0533 329 GLY A N   
2419 C CA  . GLY A 314 ? 0.5773 0.3954 0.5574 0.0879  -0.0640 -0.0343 329 GLY A CA  
2420 C C   . GLY A 314 ? 0.5351 0.3694 0.5040 0.0785  -0.0493 -0.0223 329 GLY A C   
2421 O O   . GLY A 314 ? 0.5444 0.3744 0.5025 0.0692  -0.0475 -0.0136 329 GLY A O   
2422 N N   . LEU A 315 ? 0.5023 0.3558 0.4757 0.0810  -0.0392 -0.0226 330 LEU A N   
2423 C CA  . LEU A 315 ? 0.4633 0.3291 0.4278 0.0725  -0.0268 -0.0116 330 LEU A CA  
2424 C C   . LEU A 315 ? 0.4930 0.3688 0.4447 0.0708  -0.0176 -0.0131 330 LEU A C   
2425 O O   . LEU A 315 ? 0.4800 0.3529 0.4224 0.0629  -0.0152 -0.0032 330 LEU A O   
2426 C CB  . LEU A 315 ? 0.5171 0.3993 0.4919 0.0747  -0.0198 -0.0120 330 LEU A CB  
2427 C CG  . LEU A 315 ? 0.5937 0.4864 0.5623 0.0662  -0.0085 -0.0015 330 LEU A CG  
2428 C CD1 . LEU A 315 ? 0.5387 0.4177 0.4995 0.0573  -0.0129 0.0111  330 LEU A CD1 
2429 C CD2 . LEU A 315 ? 0.5014 0.4107 0.4837 0.0679  -0.0027 -0.0038 330 LEU A CD2 
2430 N N   . PRO A 316 ? 0.4642 0.3530 0.4142 0.0778  -0.0120 -0.0250 331 PRO A N   
2431 C CA  . PRO A 316 ? 0.4429 0.3393 0.3763 0.0752  -0.0049 -0.0240 331 PRO A CA  
2432 C C   . PRO A 316 ? 0.4858 0.3674 0.4116 0.0730  -0.0146 -0.0243 331 PRO A C   
2433 O O   . PRO A 316 ? 0.5306 0.4138 0.4451 0.0678  -0.0121 -0.0174 331 PRO A O   
2434 C CB  . PRO A 316 ? 0.4810 0.3955 0.4130 0.0832  0.0028  -0.0380 331 PRO A CB  
2435 C CG  . PRO A 316 ? 0.4943 0.4041 0.4438 0.0927  -0.0061 -0.0517 331 PRO A CG  
2436 C CD  . PRO A 316 ? 0.4507 0.3504 0.4131 0.0884  -0.0114 -0.0403 331 PRO A CD  
2437 N N   . ILE A 317 ? 0.5338 0.3999 0.4674 0.0761  -0.0269 -0.0315 332 ILE A N   
2438 C CA  . ILE A 317 ? 0.5276 0.3795 0.4571 0.0714  -0.0365 -0.0306 332 ILE A CA  
2439 C C   . ILE A 317 ? 0.5201 0.3648 0.4507 0.0600  -0.0374 -0.0145 332 ILE A C   
2440 O O   . ILE A 317 ? 0.5102 0.3547 0.4359 0.0541  -0.0386 -0.0105 332 ILE A O   
2441 C CB  . ILE A 317 ? 0.5402 0.3751 0.4787 0.0770  -0.0503 -0.0428 332 ILE A CB  
2442 C CG1 . ILE A 317 ? 0.5762 0.4215 0.5105 0.0882  -0.0488 -0.0620 332 ILE A CG1 
2443 C CG2 . ILE A 317 ? 0.5713 0.3885 0.5099 0.0686  -0.0615 -0.0389 332 ILE A CG2 
2444 C CD1 . ILE A 317 ? 0.6620 0.4900 0.6074 0.0960  -0.0633 -0.0773 332 ILE A CD1 
2445 N N   . SER A 318 ? 0.5236 0.3647 0.4608 0.0571  -0.0368 -0.0062 333 SER A N   
2446 C CA  . SER A 318 ? 0.5016 0.3409 0.4373 0.0466  -0.0347 0.0076  333 SER A CA  
2447 C C   . SER A 318 ? 0.5110 0.3654 0.4399 0.0443  -0.0244 0.0120  333 SER A C   
2448 O O   . SER A 318 ? 0.5243 0.3794 0.4520 0.0375  -0.0243 0.0180  333 SER A O   
2449 C CB  . SER A 318 ? 0.4519 0.2871 0.3923 0.0447  -0.0354 0.0146  333 SER A CB  
2450 O OG  . SER A 318 ? 0.5202 0.3368 0.4660 0.0455  -0.0481 0.0135  333 SER A OG  
2451 N N   . ARG A 319 ? 0.4748 0.3416 0.4001 0.0498  -0.0161 0.0093  334 ARG A N   
2452 C CA  . ARG A 319 ? 0.4823 0.3589 0.4001 0.0478  -0.0086 0.0147  334 ARG A CA  
2453 C C   . ARG A 319 ? 0.5229 0.3997 0.4330 0.0482  -0.0128 0.0116  334 ARG A C   
2454 O O   . ARG A 319 ? 0.4774 0.3574 0.3852 0.0450  -0.0119 0.0175  334 ARG A O   
2455 C CB  . ARG A 319 ? 0.4702 0.3586 0.3847 0.0514  0.0010  0.0141  334 ARG A CB  
2456 C CG  . ARG A 319 ? 0.5241 0.4183 0.4300 0.0487  0.0071  0.0220  334 ARG A CG  
2457 C CD  . ARG A 319 ? 0.5035 0.4073 0.4088 0.0484  0.0172  0.0251  334 ARG A CD  
2458 N NE  . ARG A 319 ? 0.5436 0.4573 0.4429 0.0528  0.0219  0.0172  334 ARG A NE  
2459 C CZ  . ARG A 319 ? 0.5614 0.4873 0.4599 0.0516  0.0320  0.0184  334 ARG A CZ  
2460 N NH1 . ARG A 319 ? 0.5182 0.4454 0.4235 0.0461  0.0371  0.0271  334 ARG A NH1 
2461 N NH2 . ARG A 319 ? 0.5551 0.4933 0.4465 0.0555  0.0375  0.0098  334 ARG A NH2 
2462 N N   . LEU A 320 ? 0.5038 0.3774 0.4107 0.0530  -0.0185 0.0010  335 LEU A N   
2463 C CA  . LEU A 320 ? 0.4834 0.3570 0.3830 0.0532  -0.0245 -0.0030 335 LEU A CA  
2464 C C   . LEU A 320 ? 0.4929 0.3597 0.4021 0.0456  -0.0319 0.0011  335 LEU A C   
2465 O O   . LEU A 320 ? 0.4842 0.3557 0.3917 0.0436  -0.0347 0.0026  335 LEU A O   
2466 C CB  . LEU A 320 ? 0.4691 0.3404 0.3636 0.0602  -0.0300 -0.0177 335 LEU A CB  
2467 C CG  . LEU A 320 ? 0.6074 0.4914 0.4904 0.0673  -0.0209 -0.0238 335 LEU A CG  
2468 C CD1 . LEU A 320 ? 0.5431 0.4262 0.4229 0.0751  -0.0264 -0.0414 335 LEU A CD1 
2469 C CD2 . LEU A 320 ? 0.5651 0.4594 0.4305 0.0661  -0.0149 -0.0165 335 LEU A CD2 
2470 N N   . TYR A 321 ? 0.5138 0.3703 0.4335 0.0408  -0.0356 0.0032  336 TYR A N   
2471 C CA  . TYR A 321 ? 0.4994 0.3525 0.4280 0.0309  -0.0401 0.0086  336 TYR A CA  
2472 C C   . TYR A 321 ? 0.4754 0.3408 0.4057 0.0271  -0.0327 0.0169  336 TYR A C   
2473 O O   . TYR A 321 ? 0.5185 0.3903 0.4545 0.0229  -0.0353 0.0172  336 TYR A O   
2474 C CB  . TYR A 321 ? 0.4991 0.3382 0.4347 0.0248  -0.0441 0.0129  336 TYR A CB  
2475 C CG  . TYR A 321 ? 0.5542 0.3769 0.4934 0.0258  -0.0560 0.0050  336 TYR A CG  
2476 C CD1 . TYR A 321 ? 0.5830 0.4024 0.5264 0.0217  -0.0642 -0.0003 336 TYR A CD1 
2477 C CD2 . TYR A 321 ? 0.6921 0.5019 0.6329 0.0313  -0.0605 0.0016  336 TYR A CD2 
2478 C CE1 . TYR A 321 ? 0.6113 0.4131 0.5592 0.0225  -0.0765 -0.0088 336 TYR A CE1 
2479 C CE2 . TYR A 321 ? 0.7368 0.5289 0.6828 0.0335  -0.0731 -0.0070 336 TYR A CE2 
2480 C CZ  . TYR A 321 ? 0.7658 0.5529 0.7149 0.0287  -0.0811 -0.0122 336 TYR A CZ  
2481 O OH  . TYR A 321 ? 0.7522 0.5190 0.7076 0.0307  -0.0950 -0.0218 336 TYR A OH  
2482 N N   . ALA A 322 ? 0.4961 0.3659 0.4236 0.0291  -0.0242 0.0221  337 ALA A N   
2483 C CA  . ALA A 322 ? 0.5269 0.4068 0.4569 0.0270  -0.0182 0.0279  337 ALA A CA  
2484 C C   . ALA A 322 ? 0.5198 0.4066 0.4455 0.0320  -0.0195 0.0262  337 ALA A C   
2485 O O   . ALA A 322 ? 0.5318 0.4260 0.4647 0.0301  -0.0210 0.0273  337 ALA A O   
2486 C CB  . ALA A 322 ? 0.4645 0.3456 0.3927 0.0284  -0.0105 0.0324  337 ALA A CB  
2487 N N   . LYS A 323 ? 0.5201 0.4058 0.4336 0.0386  -0.0192 0.0234  338 LYS A N   
2488 C CA  . LYS A 323 ? 0.5226 0.4128 0.4271 0.0430  -0.0219 0.0236  338 LYS A CA  
2489 C C   . LYS A 323 ? 0.5155 0.4071 0.4228 0.0425  -0.0323 0.0178  338 LYS A C   
2490 O O   . LYS A 323 ? 0.5398 0.4362 0.4447 0.0452  -0.0370 0.0192  338 LYS A O   
2491 C CB  . LYS A 323 ? 0.5345 0.4247 0.4220 0.0483  -0.0182 0.0222  338 LYS A CB  
2492 C CG  . LYS A 323 ? 0.6110 0.5026 0.4971 0.0479  -0.0081 0.0290  338 LYS A CG  
2493 C CD  . LYS A 323 ? 0.6654 0.5611 0.5362 0.0512  -0.0026 0.0274  338 LYS A CD  
2494 C CE  . LYS A 323 ? 0.6935 0.5915 0.5641 0.0488  0.0071  0.0359  338 LYS A CE  
2495 N NZ  . LYS A 323 ? 0.8714 0.7775 0.7317 0.0501  0.0153  0.0330  338 LYS A NZ  
2496 N N   . TYR A 324 ? 0.5351 0.4216 0.4483 0.0393  -0.0376 0.0114  339 TYR A N   
2497 C CA  . TYR A 324 ? 0.5461 0.4333 0.4628 0.0382  -0.0486 0.0043  339 TYR A CA  
2498 C C   . TYR A 324 ? 0.5289 0.4265 0.4600 0.0343  -0.0516 0.0072  339 TYR A C   
2499 O O   . TYR A 324 ? 0.5376 0.4403 0.4689 0.0367  -0.0608 0.0027  339 TYR A O   
2500 C CB  . TYR A 324 ? 0.5163 0.3932 0.4411 0.0332  -0.0541 -0.0017 339 TYR A CB  
2501 C CG  . TYR A 324 ? 0.5283 0.4047 0.4613 0.0294  -0.0663 -0.0093 339 TYR A CG  
2502 C CD1 . TYR A 324 ? 0.5266 0.4075 0.4498 0.0356  -0.0743 -0.0170 339 TYR A CD1 
2503 C CD2 . TYR A 324 ? 0.5402 0.4113 0.4900 0.0186  -0.0704 -0.0087 339 TYR A CD2 
2504 C CE1 . TYR A 324 ? 0.5479 0.4288 0.4804 0.0319  -0.0872 -0.0255 339 TYR A CE1 
2505 C CE2 . TYR A 324 ? 0.5783 0.4491 0.5385 0.0135  -0.0820 -0.0159 339 TYR A CE2 
2506 C CZ  . TYR A 324 ? 0.6048 0.4808 0.5576 0.0205  -0.0907 -0.0251 339 TYR A CZ  
2507 O OH  . TYR A 324 ? 0.5874 0.4637 0.5525 0.0150  -0.1034 -0.0334 339 TYR A OH  
2508 N N   . PHE A 325 ? 0.5433 0.4460 0.4868 0.0292  -0.0445 0.0134  340 PHE A N   
2509 C CA  . PHE A 325 ? 0.5263 0.4428 0.4860 0.0270  -0.0458 0.0141  340 PHE A CA  
2510 C C   . PHE A 325 ? 0.5457 0.4667 0.5043 0.0325  -0.0396 0.0196  340 PHE A C   
2511 O O   . PHE A 325 ? 0.5161 0.4476 0.4899 0.0297  -0.0353 0.0204  340 PHE A O   
2512 C CB  . PHE A 325 ? 0.4837 0.4062 0.4613 0.0154  -0.0430 0.0144  340 PHE A CB  
2513 C CG  . PHE A 325 ? 0.5512 0.4723 0.5374 0.0086  -0.0525 0.0086  340 PHE A CG  
2514 C CD1 . PHE A 325 ? 0.5562 0.4885 0.5534 0.0099  -0.0620 0.0023  340 PHE A CD1 
2515 C CD2 . PHE A 325 ? 0.5554 0.4627 0.5399 0.0011  -0.0536 0.0093  340 PHE A CD2 
2516 C CE1 . PHE A 325 ? 0.5496 0.4807 0.5568 0.0026  -0.0715 -0.0038 340 PHE A CE1 
2517 C CE2 . PHE A 325 ? 0.5705 0.4736 0.5643 -0.0061 -0.0635 0.0039  340 PHE A CE2 
2518 C CZ  . PHE A 325 ? 0.5647 0.4804 0.5703 -0.0058 -0.0721 -0.0030 340 PHE A CZ  
2519 N N   . GLN A 326 ? 0.5222 0.4355 0.4630 0.0397  -0.0388 0.0230  341 GLN A N   
2520 C CA  . GLN A 326 ? 0.5242 0.4371 0.4619 0.0451  -0.0358 0.0290  341 GLN A CA  
2521 C C   . GLN A 326 ? 0.5662 0.4774 0.5077 0.0422  -0.0251 0.0329  341 GLN A C   
2522 O O   . GLN A 326 ? 0.5340 0.4460 0.4803 0.0452  -0.0231 0.0359  341 GLN A O   
2523 C CB  . GLN A 326 ? 0.5263 0.4487 0.4787 0.0490  -0.0432 0.0275  341 GLN A CB  
2524 C CG  . GLN A 326 ? 0.5962 0.5224 0.5475 0.0520  -0.0566 0.0227  341 GLN A CG  
2525 C CD  . GLN A 326 ? 0.6707 0.5863 0.5950 0.0578  -0.0620 0.0263  341 GLN A CD  
2526 O OE1 . GLN A 326 ? 0.6196 0.5272 0.5304 0.0614  -0.0590 0.0345  341 GLN A OE1 
2527 N NE2 . GLN A 326 ? 0.6151 0.5311 0.5312 0.0579  -0.0703 0.0201  341 GLN A NE2 
2528 N N   . GLY A 327 ? 0.5089 0.4163 0.4483 0.0371  -0.0197 0.0324  342 GLY A N   
2529 C CA  . GLY A 327 ? 0.5064 0.4114 0.4466 0.0345  -0.0112 0.0357  342 GLY A CA  
2530 C C   . GLY A 327 ? 0.5491 0.4462 0.4759 0.0373  -0.0074 0.0386  342 GLY A C   
2531 O O   . GLY A 327 ? 0.4788 0.3736 0.3941 0.0415  -0.0096 0.0391  342 GLY A O   
2532 N N   . ASP A 328 ? 0.5036 0.3987 0.4320 0.0346  -0.0015 0.0402  343 ASP A N   
2533 C CA  . ASP A 328 ? 0.4638 0.3552 0.3845 0.0366  0.0027  0.0416  343 ASP A CA  
2534 C C   . ASP A 328 ? 0.5053 0.3948 0.4308 0.0332  0.0050  0.0409  343 ASP A C   
2535 O O   . ASP A 328 ? 0.4880 0.3785 0.4194 0.0287  0.0045  0.0413  343 ASP A O   
2536 C CB  . ASP A 328 ? 0.4834 0.3740 0.4011 0.0383  0.0067  0.0470  343 ASP A CB  
2537 C CG  . ASP A 328 ? 0.5473 0.4379 0.4554 0.0395  0.0114  0.0485  343 ASP A CG  
2538 O OD1 . ASP A 328 ? 0.5100 0.4026 0.4150 0.0407  0.0116  0.0433  343 ASP A OD1 
2539 O OD2 . ASP A 328 ? 0.6095 0.4987 0.5140 0.0388  0.0150  0.0545  343 ASP A OD2 
2540 N N   . LEU A 329 ? 0.4523 0.3407 0.3752 0.0352  0.0073  0.0397  344 LEU A N   
2541 C CA  . LEU A 329 ? 0.4349 0.3213 0.3628 0.0335  0.0077  0.0393  344 LEU A CA  
2542 C C   . LEU A 329 ? 0.5330 0.4240 0.4625 0.0352  0.0135  0.0399  344 LEU A C   
2543 O O   . LEU A 329 ? 0.4884 0.3835 0.4145 0.0385  0.0161  0.0373  344 LEU A O   
2544 C CB  . LEU A 329 ? 0.4389 0.3195 0.3673 0.0348  0.0015  0.0349  344 LEU A CB  
2545 C CG  . LEU A 329 ? 0.5223 0.3969 0.4551 0.0331  -0.0025 0.0357  344 LEU A CG  
2546 C CD1 . LEU A 329 ? 0.4987 0.3624 0.4320 0.0338  -0.0115 0.0326  344 LEU A CD1 
2547 C CD2 . LEU A 329 ? 0.5038 0.3835 0.4420 0.0369  0.0004  0.0336  344 LEU A CD2 
2548 N N   . GLN A 330 ? 0.4458 0.3376 0.3807 0.0323  0.0158  0.0424  345 GLN A N   
2549 C CA  . GLN A 330 ? 0.4723 0.3689 0.4116 0.0320  0.0211  0.0434  345 GLN A CA  
2550 C C   . GLN A 330 ? 0.4808 0.3789 0.4287 0.0309  0.0193  0.0412  345 GLN A C   
2551 O O   . GLN A 330 ? 0.4417 0.3356 0.3891 0.0290  0.0147  0.0413  345 GLN A O   
2552 C CB  . GLN A 330 ? 0.5401 0.4347 0.4793 0.0296  0.0240  0.0483  345 GLN A CB  
2553 C CG  . GLN A 330 ? 0.5075 0.3995 0.4380 0.0315  0.0235  0.0515  345 GLN A CG  
2554 C CD  . GLN A 330 ? 0.5976 0.4841 0.5294 0.0304  0.0235  0.0567  345 GLN A CD  
2555 O OE1 . GLN A 330 ? 0.5572 0.4415 0.4972 0.0281  0.0243  0.0565  345 GLN A OE1 
2556 N NE2 . GLN A 330 ? 0.6055 0.4885 0.5294 0.0327  0.0210  0.0606  345 GLN A NE2 
2557 N N   . LEU A 331 ? 0.4502 0.3559 0.4057 0.0315  0.0229  0.0393  346 LEU A N   
2558 C CA  . LEU A 331 ? 0.4740 0.3832 0.4403 0.0313  0.0198  0.0362  346 LEU A CA  
2559 C C   . LEU A 331 ? 0.5170 0.4321 0.4923 0.0269  0.0248  0.0377  346 LEU A C   
2560 O O   . LEU A 331 ? 0.4583 0.3785 0.4341 0.0247  0.0322  0.0402  346 LEU A O   
2561 C CB  . LEU A 331 ? 0.5201 0.4364 0.4943 0.0369  0.0180  0.0297  346 LEU A CB  
2562 C CG  . LEU A 331 ? 0.6267 0.5361 0.5992 0.0424  0.0095  0.0257  346 LEU A CG  
2563 C CD1 . LEU A 331 ? 0.5407 0.4612 0.5278 0.0493  0.0087  0.0166  346 LEU A CD1 
2564 C CD2 . LEU A 331 ? 0.6161 0.5138 0.5847 0.0401  0.0002  0.0294  346 LEU A CD2 
2565 N N   A PHE A 332 ? 0.4270 0.3412 0.4086 0.0247  0.0202  0.0362  347 PHE A N   
2566 N N   B PHE A 332 ? 0.4311 0.3450 0.4123 0.0245  0.0204  0.0365  347 PHE A N   
2567 C CA  A PHE A 332 ? 0.4379 0.3563 0.4307 0.0198  0.0226  0.0360  347 PHE A CA  
2568 C CA  B PHE A 332 ? 0.4324 0.3523 0.4262 0.0199  0.0234  0.0360  347 PHE A CA  
2569 C C   A PHE A 332 ? 0.4793 0.4031 0.4829 0.0206  0.0153  0.0307  347 PHE A C   
2570 C C   B PHE A 332 ? 0.4841 0.4080 0.4879 0.0204  0.0158  0.0309  347 PHE A C   
2571 O O   A PHE A 332 ? 0.4996 0.4167 0.4961 0.0211  0.0077  0.0298  347 PHE A O   
2572 O O   B PHE A 332 ? 0.5028 0.4196 0.4991 0.0206  0.0088  0.0302  347 PHE A O   
2573 C CB  A PHE A 332 ? 0.4739 0.3826 0.4613 0.0164  0.0225  0.0385  347 PHE A CB  
2574 C CB  B PHE A 332 ? 0.4953 0.4068 0.4863 0.0153  0.0255  0.0397  347 PHE A CB  
2575 C CG  A PHE A 332 ? 0.5005 0.4029 0.4784 0.0169  0.0266  0.0437  347 PHE A CG  
2576 C CG  B PHE A 332 ? 0.4852 0.3880 0.4668 0.0163  0.0206  0.0385  347 PHE A CG  
2577 C CD1 A PHE A 332 ? 0.4614 0.3633 0.4413 0.0136  0.0323  0.0490  347 PHE A CD1 
2578 C CD1 B PHE A 332 ? 0.5223 0.4208 0.4922 0.0192  0.0206  0.0405  347 PHE A CD1 
2579 C CD2 A PHE A 332 ? 0.4793 0.3765 0.4465 0.0199  0.0242  0.0439  347 PHE A CD2 
2580 C CD2 B PHE A 332 ? 0.5325 0.4332 0.5177 0.0139  0.0167  0.0344  347 PHE A CD2 
2581 C CE1 A PHE A 332 ? 0.4831 0.3777 0.4526 0.0147  0.0337  0.0546  347 PHE A CE1 
2582 C CE1 B PHE A 332 ? 0.5179 0.4127 0.4813 0.0191  0.0181  0.0387  347 PHE A CE1 
2583 C CE2 A PHE A 332 ? 0.4824 0.3750 0.4430 0.0213  0.0260  0.0478  347 PHE A CE2 
2584 C CE2 B PHE A 332 ? 0.5147 0.4110 0.4906 0.0146  0.0142  0.0318  347 PHE A CE2 
2585 C CZ  A PHE A 332 ? 0.4915 0.3819 0.4524 0.0194  0.0298  0.0532  347 PHE A CZ  
2586 C CZ  B PHE A 332 ? 0.5272 0.4217 0.4929 0.0169  0.0157  0.0342  347 PHE A CZ  
2587 N N   . SER A 333 ? 0.4459 0.3830 0.4664 0.0204  0.0174  0.0271  348 SER A N   
2588 C CA  . SER A 333 ? 0.4456 0.3894 0.4792 0.0224  0.0085  0.0212  348 SER A CA  
2589 C C   . SER A 333 ? 0.5099 0.4599 0.5583 0.0155  0.0089  0.0192  348 SER A C   
2590 O O   . SER A 333 ? 0.4766 0.4269 0.5283 0.0089  0.0173  0.0227  348 SER A O   
2591 C CB  . SER A 333 ? 0.4307 0.3881 0.4779 0.0287  0.0086  0.0155  348 SER A CB  
2592 O OG  . SER A 333 ? 0.4576 0.4174 0.5151 0.0333  -0.0040 0.0103  348 SER A OG  
2593 N N   A MET A 334 ? 0.4570 0.4101 0.5140 0.0167  -0.0018 0.0140  349 MET A N   
2594 N N   B MET A 334 ? 0.4561 0.4086 0.5123 0.0167  -0.0019 0.0141  349 MET A N   
2595 C CA  A MET A 334 ? 0.4329 0.3942 0.5084 0.0105  -0.0038 0.0097  349 MET A CA  
2596 C CA  B MET A 334 ? 0.4334 0.3944 0.5083 0.0108  -0.0044 0.0095  349 MET A CA  
2597 C C   A MET A 334 ? 0.4461 0.4230 0.5418 0.0151  -0.0124 0.0023  349 MET A C   
2598 C C   B MET A 334 ? 0.4445 0.4214 0.5397 0.0157  -0.0124 0.0024  349 MET A C   
2599 O O   A MET A 334 ? 0.4552 0.4269 0.5451 0.0201  -0.0260 -0.0001 349 MET A O   
2600 O O   B MET A 334 ? 0.4573 0.4290 0.5464 0.0214  -0.0258 0.0002  349 MET A O   
2601 C CB  A MET A 334 ? 0.4752 0.4238 0.5394 0.0072  -0.0106 0.0086  349 MET A CB  
2602 C CB  B MET A 334 ? 0.4779 0.4268 0.5418 0.0080  -0.0124 0.0080  349 MET A CB  
2603 C CG  A MET A 334 ? 0.4933 0.4277 0.5410 0.0046  -0.0037 0.0136  349 MET A CG  
2604 C CG  B MET A 334 ? 0.5099 0.4437 0.5547 0.0059  -0.0067 0.0126  349 MET A CG  
2605 S SD  A MET A 334 ? 0.4741 0.3978 0.5104 0.0027  -0.0118 0.0079  349 MET A SD  
2606 S SD  B MET A 334 ? 0.5006 0.4302 0.5572 -0.0030 -0.0002 0.0130  349 MET A SD  
2607 C CE  A MET A 334 ? 0.4904 0.4199 0.5528 -0.0051 -0.0141 0.0018  349 MET A CE  
2608 C CE  B MET A 334 ? 0.4928 0.4235 0.5594 -0.0064 -0.0123 0.0026  349 MET A CE  
2609 N N   . GLU A 335 ? 0.4292 0.4259 0.5486 0.0134  -0.0047 -0.0010 350 GLU A N   
2610 C CA  . GLU A 335 ? 0.4634 0.4790 0.6069 0.0196  -0.0119 -0.0099 350 GLU A CA  
2611 C C   . GLU A 335 ? 0.4748 0.4919 0.6293 0.0180  -0.0265 -0.0152 350 GLU A C   
2612 O O   . GLU A 335 ? 0.4096 0.4262 0.5697 0.0085  -0.0250 -0.0153 350 GLU A O   
2613 C CB  . GLU A 335 ? 0.3584 0.4000 0.5277 0.0157  0.0019  -0.0138 350 GLU A CB  
2614 C CG  . GLU A 335 ? 0.3750 0.4396 0.5716 0.0252  -0.0043 -0.0254 350 GLU A CG  
2615 C CD  . GLU A 335 ? 0.4424 0.5400 0.6721 0.0190  0.0084  -0.0321 350 GLU A CD  
2616 O OE1 . GLU A 335 ? 0.4945 0.5961 0.7283 0.0049  0.0196  -0.0266 350 GLU A OE1 
2617 O OE2 . GLU A 335 ? 0.5043 0.6245 0.7575 0.0279  0.0071  -0.0431 350 GLU A OE2 
2618 N N   . GLY A 336 ? 0.4714 0.4878 0.6274 0.0276  -0.0425 -0.0195 351 GLY A N   
2619 C CA  . GLY A 336 ? 0.4293 0.4447 0.5895 0.0274  -0.0593 -0.0240 351 GLY A CA  
2620 C C   . GLY A 336 ? 0.5320 0.5229 0.6570 0.0276  -0.0687 -0.0180 351 GLY A C   
2621 O O   . GLY A 336 ? 0.5130 0.5014 0.6348 0.0288  -0.0847 -0.0212 351 GLY A O   
2622 N N   . PHE A 337 ? 0.4838 0.4585 0.5823 0.0262  -0.0593 -0.0098 352 PHE A N   
2623 C CA  . PHE A 337 ? 0.4984 0.4539 0.5645 0.0253  -0.0659 -0.0048 352 PHE A CA  
2624 C C   . PHE A 337 ? 0.5780 0.5192 0.6214 0.0299  -0.0650 0.0035  352 PHE A C   
2625 O O   . PHE A 337 ? 0.4975 0.4288 0.5267 0.0340  -0.0785 0.0069  352 PHE A O   
2626 C CB  . PHE A 337 ? 0.5007 0.4503 0.5568 0.0170  -0.0566 -0.0047 352 PHE A CB  
2627 C CG  . PHE A 337 ? 0.5855 0.5204 0.6097 0.0159  -0.0609 -0.0019 352 PHE A CG  
2628 C CD1 . PHE A 337 ? 0.7083 0.6411 0.7210 0.0164  -0.0759 -0.0050 352 PHE A CD1 
2629 C CD2 . PHE A 337 ? 0.6655 0.5907 0.6710 0.0143  -0.0501 0.0036  352 PHE A CD2 
2630 C CE1 . PHE A 337 ? 0.6881 0.6104 0.6691 0.0142  -0.0782 -0.0025 352 PHE A CE1 
2631 C CE2 . PHE A 337 ? 0.7336 0.6501 0.7119 0.0125  -0.0522 0.0050  352 PHE A CE2 
2632 C CZ  . PHE A 337 ? 0.6787 0.5942 0.6437 0.0120  -0.0653 0.0021  352 PHE A CZ  
2633 N N   . GLY A 338 ? 0.4649 0.4033 0.5034 0.0284  -0.0505 0.0076  353 GLY A N   
2634 C CA  . GLY A 338 ? 0.4169 0.3414 0.4344 0.0310  -0.0496 0.0148  353 GLY A CA  
2635 C C   . GLY A 338 ? 0.5023 0.4273 0.5190 0.0294  -0.0340 0.0173  353 GLY A C   
2636 O O   . GLY A 338 ? 0.4516 0.3874 0.4838 0.0269  -0.0242 0.0145  353 GLY A O   
2637 N N   . THR A 339 ? 0.4473 0.3601 0.4449 0.0298  -0.0323 0.0234  354 THR A N   
2638 C CA  . THR A 339 ? 0.4913 0.4033 0.4861 0.0297  -0.0207 0.0257  354 THR A CA  
2639 C C   . THR A 339 ? 0.5377 0.4384 0.5110 0.0257  -0.0184 0.0314  354 THR A C   
2640 O O   . THR A 339 ? 0.5331 0.4251 0.4923 0.0246  -0.0261 0.0351  354 THR A O   
2641 C CB  . THR A 339 ? 0.4566 0.3694 0.4583 0.0368  -0.0224 0.0240  354 THR A CB  
2642 O OG1 . THR A 339 ? 0.4480 0.3754 0.4725 0.0411  -0.0241 0.0168  354 THR A OG1 
2643 C CG2 . THR A 339 ? 0.4270 0.3403 0.4243 0.0368  -0.0109 0.0253  354 THR A CG2 
2644 N N   . ASP A 340 ? 0.4862 0.3881 0.4578 0.0233  -0.0080 0.0323  355 ASP A N   
2645 C CA  . ASP A 340 ? 0.4917 0.3871 0.4484 0.0207  -0.0046 0.0360  355 ASP A CA  
2646 C C   . ASP A 340 ? 0.5263 0.4202 0.4826 0.0234  -0.0003 0.0381  355 ASP A C   
2647 O O   . ASP A 340 ? 0.4522 0.3515 0.4174 0.0258  0.0047  0.0365  355 ASP A O   
2648 C CB  . ASP A 340 ? 0.5214 0.4186 0.4778 0.0175  0.0015  0.0340  355 ASP A CB  
2649 C CG  . ASP A 340 ? 0.5605 0.4589 0.5140 0.0146  -0.0029 0.0299  355 ASP A CG  
2650 O OD1 . ASP A 340 ? 0.5912 0.4882 0.5376 0.0141  -0.0108 0.0305  355 ASP A OD1 
2651 O OD2 . ASP A 340 ? 0.6661 0.5655 0.6238 0.0131  0.0006  0.0257  355 ASP A OD2 
2652 N N   . ALA A 341 ? 0.4641 0.3515 0.4092 0.0219  -0.0018 0.0414  356 ALA A N   
2653 C CA  . ALA A 341 ? 0.4954 0.3811 0.4389 0.0235  0.0014  0.0424  356 ALA A CA  
2654 C C   . ALA A 341 ? 0.5358 0.4216 0.4722 0.0193  0.0051  0.0443  356 ALA A C   
2655 O O   . ALA A 341 ? 0.4834 0.3684 0.4125 0.0146  0.0034  0.0460  356 ALA A O   
2656 C CB  . ALA A 341 ? 0.4577 0.3357 0.3994 0.0259  -0.0059 0.0431  356 ALA A CB  
2657 N N   . VAL A 342 ? 0.4585 0.3469 0.3969 0.0211  0.0098  0.0439  357 VAL A N   
2658 C CA  . VAL A 342 ? 0.4741 0.3650 0.4102 0.0187  0.0123  0.0440  357 VAL A CA  
2659 C C   . VAL A 342 ? 0.4947 0.3841 0.4297 0.0200  0.0108  0.0448  357 VAL A C   
2660 O O   . VAL A 342 ? 0.4854 0.3742 0.4212 0.0243  0.0113  0.0442  357 VAL A O   
2661 C CB  . VAL A 342 ? 0.5509 0.4455 0.4924 0.0204  0.0166  0.0419  357 VAL A CB  
2662 C CG1 . VAL A 342 ? 0.4914 0.3915 0.4341 0.0192  0.0183  0.0396  357 VAL A CG1 
2663 C CG2 . VAL A 342 ? 0.5054 0.4003 0.4493 0.0191  0.0168  0.0395  357 VAL A CG2 
2664 N N   . ILE A 343 ? 0.4808 0.3706 0.4135 0.0152  0.0091  0.0458  358 ILE A N   
2665 C CA  . ILE A 343 ? 0.4380 0.3283 0.3722 0.0151  0.0072  0.0453  358 ILE A CA  
2666 C C   . ILE A 343 ? 0.5281 0.4285 0.4682 0.0151  0.0108  0.0430  358 ILE A C   
2667 O O   . ILE A 343 ? 0.4719 0.3799 0.4141 0.0107  0.0143  0.0419  358 ILE A O   
2668 C CB  . ILE A 343 ? 0.4836 0.3686 0.4151 0.0083  0.0025  0.0480  358 ILE A CB  
2669 C CG1 . ILE A 343 ? 0.5167 0.3892 0.4447 0.0104  -0.0038 0.0492  358 ILE A CG1 
2670 C CG2 . ILE A 343 ? 0.5765 0.4630 0.5124 0.0072  -0.0003 0.0461  358 ILE A CG2 
2671 C CD1 . ILE A 343 ? 0.5135 0.3759 0.4374 0.0026  -0.0100 0.0544  358 ILE A CD1 
2672 N N   . TYR A 344 ? 0.4906 0.3919 0.4333 0.0204  0.0095  0.0417  359 TYR A N   
2673 C CA  . TYR A 344 ? 0.4666 0.3762 0.4173 0.0226  0.0100  0.0391  359 TYR A CA  
2674 C C   . TYR A 344 ? 0.5614 0.4758 0.5164 0.0209  0.0057  0.0374  359 TYR A C   
2675 O O   . TYR A 344 ? 0.4665 0.3748 0.4163 0.0231  0.0009  0.0378  359 TYR A O   
2676 C CB  . TYR A 344 ? 0.4831 0.3882 0.4328 0.0297  0.0091  0.0404  359 TYR A CB  
2677 C CG  . TYR A 344 ? 0.4830 0.3840 0.4324 0.0302  0.0129  0.0415  359 TYR A CG  
2678 C CD1 . TYR A 344 ? 0.5036 0.4088 0.4610 0.0306  0.0149  0.0377  359 TYR A CD1 
2679 C CD2 . TYR A 344 ? 0.4919 0.3865 0.4349 0.0304  0.0144  0.0449  359 TYR A CD2 
2680 C CE1 . TYR A 344 ? 0.4819 0.3823 0.4400 0.0307  0.0170  0.0373  359 TYR A CE1 
2681 C CE2 . TYR A 344 ? 0.5261 0.4180 0.4717 0.0296  0.0172  0.0455  359 TYR A CE2 
2682 C CZ  . TYR A 344 ? 0.5730 0.4665 0.5257 0.0296  0.0178  0.0418  359 TYR A CZ  
2683 O OH  . TYR A 344 ? 0.5244 0.4141 0.4806 0.0286  0.0192  0.0410  359 TYR A OH  
2684 N N   . LEU A 345 ? 0.4384 0.3651 0.4036 0.0163  0.0075  0.0343  360 LEU A N   
2685 C CA  . LEU A 345 ? 0.4699 0.4040 0.4436 0.0135  0.0031  0.0319  360 LEU A CA  
2686 C C   . LEU A 345 ? 0.5146 0.4636 0.5036 0.0181  0.0027  0.0262  360 LEU A C   
2687 O O   . LEU A 345 ? 0.4624 0.4177 0.4569 0.0209  0.0074  0.0232  360 LEU A O   
2688 C CB  . LEU A 345 ? 0.4768 0.4147 0.4522 0.0015  0.0052  0.0336  360 LEU A CB  
2689 C CG  . LEU A 345 ? 0.5197 0.4412 0.4816 -0.0028 0.0037  0.0395  360 LEU A CG  
2690 C CD1 . LEU A 345 ? 0.4808 0.4035 0.4429 -0.0162 0.0048  0.0437  360 LEU A CD1 
2691 C CD2 . LEU A 345 ? 0.5112 0.4192 0.4678 0.0028  -0.0041 0.0388  360 LEU A CD2 
2692 N N   . LYS A 346 ? 0.4493 0.4040 0.4469 0.0197  -0.0044 0.0233  361 LYS A N   
2693 C CA  . LYS A 346 ? 0.4610 0.4329 0.4780 0.0240  -0.0062 0.0165  361 LYS A CA  
2694 C C   . LYS A 346 ? 0.5226 0.5154 0.5548 0.0141  0.0015  0.0118  361 LYS A C   
2695 O O   . LYS A 346 ? 0.5153 0.5093 0.5464 0.0030  0.0027  0.0145  361 LYS A O   
2696 C CB  . LYS A 346 ? 0.4821 0.4549 0.5041 0.0291  -0.0178 0.0145  361 LYS A CB  
2697 C CG  . LYS A 346 ? 0.5030 0.4580 0.5076 0.0384  -0.0247 0.0195  361 LYS A CG  
2698 C CD  . LYS A 346 ? 0.5392 0.4915 0.5470 0.0477  -0.0253 0.0202  361 LYS A CD  
2699 C CE  . LYS A 346 ? 0.6411 0.5761 0.6300 0.0546  -0.0329 0.0274  361 LYS A CE  
2700 N NZ  . LYS A 346 ? 0.6402 0.5677 0.6312 0.0627  -0.0361 0.0303  361 LYS A NZ  
2701 N N   . ALA A 347 ? 0.4701 0.4795 0.5170 0.0178  0.0067  0.0045  362 ALA A N   
2702 C CA  . ALA A 347 ? 0.4626 0.4961 0.5226 0.0078  0.0167  -0.0009 362 ALA A CA  
2703 C C   . ALA A 347 ? 0.5173 0.5726 0.6007 0.0038  0.0135  -0.0069 362 ALA A C   
2704 O O   . ALA A 347 ? 0.5503 0.6233 0.6415 -0.0098 0.0216  -0.0078 362 ALA A O   
2705 C CB  . ALA A 347 ? 0.4669 0.5132 0.5350 0.0139  0.0241  -0.0098 362 ALA A CB  
2706 N N   . LEU A 348 ? 0.4713 0.5266 0.5663 0.0143  0.0017  -0.0107 363 LEU A N   
2707 C CA  . LEU A 348 ? 0.5778 0.6567 0.6997 0.0124  -0.0033 -0.0186 363 LEU A CA  
2708 C C   . LEU A 348 ? 0.5466 0.6128 0.6621 0.0083  -0.0145 -0.0136 363 LEU A C   
2709 O O   . LEU A 348 ? 0.5067 0.5484 0.6019 0.0156  -0.0231 -0.0078 363 LEU A O   
2710 C CB  . LEU A 348 ? 0.5428 0.6328 0.6856 0.0286  -0.0115 -0.0284 363 LEU A CB  
2711 C CG  . LEU A 348 ? 0.5916 0.6915 0.7417 0.0349  -0.0021 -0.0359 363 LEU A CG  
2712 C CD1 . LEU A 348 ? 0.6066 0.7083 0.7747 0.0533  -0.0135 -0.0442 363 LEU A CD1 
2713 C CD2 . LEU A 348 ? 0.6193 0.7528 0.7875 0.0230  0.0130  -0.0445 363 LEU A CD2 
2714 N N   . SER A 349 ? 0.4710 0.5556 0.6047 -0.0039 -0.0141 -0.0169 364 SER A N   
2715 C CA  . SER A 349 ? 0.5104 0.5835 0.6404 -0.0091 -0.0255 -0.0143 364 SER A CA  
2716 C C   . SER A 349 ? 0.5865 0.6562 0.7205 0.0052  -0.0423 -0.0191 364 SER A C   
2717 O O   . SER A 349 ? 0.6218 0.6748 0.7429 0.0052  -0.0530 -0.0170 364 SER A O   
2718 C CB  . SER A 349 ? 0.4855 0.5805 0.6385 -0.0265 -0.0220 -0.0173 364 SER A CB  
2719 O OG  . SER A 349 ? 0.5725 0.7018 0.7590 -0.0235 -0.0215 -0.0288 364 SER A OG  
2720 N N   . THR A 350 ? 0.5648 0.6499 0.7165 0.0175  -0.0460 -0.0263 365 THR A N   
2721 C CA  . THR A 350 ? 0.5517 0.6305 0.7032 0.0315  -0.0639 -0.0286 365 THR A CA  
2722 C C   . THR A 350 ? 0.5589 0.6069 0.6770 0.0422  -0.0678 -0.0193 365 THR A C   
2723 O O   . THR A 350 ? 0.5635 0.5994 0.6693 0.0503  -0.0822 -0.0176 365 THR A O   
2724 C CB  . THR A 350 ? 0.5436 0.6481 0.7277 0.0418  -0.0691 -0.0394 365 THR A CB  
2725 O OG1 . THR A 350 ? 0.5426 0.6511 0.7296 0.0464  -0.0570 -0.0408 365 THR A OG1 
2726 C CG2 . THR A 350 ? 0.5230 0.6614 0.7426 0.0311  -0.0675 -0.0496 365 THR A CG2 
2727 N N   . ASP A 351 ? 0.5385 0.5747 0.6414 0.0418  -0.0555 -0.0134 366 ASP A N   
2728 C CA  . ASP A 351 ? 0.5648 0.5733 0.6370 0.0488  -0.0574 -0.0040 366 ASP A CA  
2729 C C   . ASP A 351 ? 0.5562 0.5473 0.6040 0.0410  -0.0548 0.0020  366 ASP A C   
2730 O O   . ASP A 351 ? 0.5543 0.5260 0.5774 0.0461  -0.0568 0.0085  366 ASP A O   
2731 C CB  . ASP A 351 ? 0.5319 0.5346 0.5999 0.0522  -0.0470 -0.0011 366 ASP A CB  
2732 C CG  . ASP A 351 ? 0.6847 0.6978 0.7738 0.0637  -0.0518 -0.0075 366 ASP A CG  
2733 O OD1 . ASP A 351 ? 0.6094 0.6282 0.7106 0.0718  -0.0659 -0.0111 366 ASP A OD1 
2734 O OD2 . ASP A 351 ? 0.6484 0.6633 0.7423 0.0652  -0.0427 -0.0097 366 ASP A OD2 
2735 N N   . SER A 352 ? 0.5534 0.5511 0.6082 0.0285  -0.0502 0.0000  367 SER A N   
2736 C CA  . SER A 352 ? 0.5477 0.5274 0.5827 0.0218  -0.0485 0.0044  367 SER A CA  
2737 C C   . SER A 352 ? 0.5445 0.5194 0.5750 0.0236  -0.0624 0.0003  367 SER A C   
2738 O O   . SER A 352 ? 0.5848 0.5670 0.6293 0.0150  -0.0671 -0.0047 367 SER A O   
2739 C CB  . SER A 352 ? 0.5011 0.4857 0.5441 0.0072  -0.0392 0.0057  367 SER A CB  
2740 O OG  . SER A 352 ? 0.6170 0.6063 0.6600 0.0060  -0.0268 0.0088  367 SER A OG  
2741 N N   . VAL A 353 ? 0.5705 0.5327 0.5800 0.0340  -0.0689 0.0023  368 VAL A N   
2742 C CA  . VAL A 353 ? 0.5950 0.5535 0.5957 0.0383  -0.0832 -0.0025 368 VAL A CA  
2743 C C   . VAL A 353 ? 0.5343 0.4742 0.5073 0.0394  -0.0817 -0.0010 368 VAL A C   
2744 O O   . VAL A 353 ? 0.5453 0.4757 0.5015 0.0430  -0.0731 0.0056  368 VAL A O   
2745 C CB  . VAL A 353 ? 0.5977 0.5593 0.5949 0.0501  -0.0934 -0.0013 368 VAL A CB  
2746 C CG1 . VAL A 353 ? 0.6008 0.5578 0.5825 0.0548  -0.1088 -0.0056 368 VAL A CG1 
2747 C CG2 . VAL A 353 ? 0.5974 0.5798 0.6268 0.0512  -0.0957 -0.0053 368 VAL A CG2 
2748 N N   . GLU A 354 ? 0.5731 0.5088 0.5433 0.0363  -0.0901 -0.0086 369 GLU A N   
2749 C CA  . GLU A 354 ? 0.6220 0.5425 0.5680 0.0392  -0.0901 -0.0111 369 GLU A CA  
2750 C C   . GLU A 354 ? 0.6165 0.5324 0.5356 0.0492  -0.0886 -0.0063 369 GLU A C   
2751 O O   . GLU A 354 ? 0.5775 0.4981 0.4909 0.0552  -0.0971 -0.0049 369 GLU A O   
2752 C CB  . GLU A 354 ? 0.6060 0.5243 0.5521 0.0378  -0.1038 -0.0229 369 GLU A CB  
2753 C CG  . GLU A 354 ? 0.6069 0.5245 0.5763 0.0258  -0.1062 -0.0274 369 GLU A CG  
2754 C CD  . GLU A 354 ? 0.6298 0.5411 0.5966 0.0255  -0.1206 -0.0401 369 GLU A CD  
2755 O OE1 . GLU A 354 ? 0.6448 0.5660 0.6155 0.0282  -0.1332 -0.0463 369 GLU A OE1 
2756 O OE2 . GLU A 354 ? 0.5954 0.4912 0.5561 0.0237  -0.1208 -0.0450 369 GLU A OE2 
2757 N N   . ARG A 355 ? 0.5681 0.4750 0.4710 0.0505  -0.0785 -0.0037 370 ARG A N   
2758 C CA  . ARG A 355 ? 0.6395 0.5428 0.5152 0.0575  -0.0751 0.0007  370 ARG A CA  
2759 C C   . ARG A 355 ? 0.6124 0.5118 0.4700 0.0603  -0.0789 -0.0102 370 ARG A C   
2760 O O   . ARG A 355 ? 0.6303 0.5246 0.4910 0.0586  -0.0739 -0.0161 370 ARG A O   
2761 C CB  . ARG A 355 ? 0.6522 0.5521 0.5257 0.0565  -0.0603 0.0097  370 ARG A CB  
2762 C CG  . ARG A 355 ? 0.7234 0.6207 0.5700 0.0607  -0.0536 0.0132  370 ARG A CG  
2763 C CD  . ARG A 355 ? 0.7048 0.6007 0.5478 0.0609  -0.0469 0.0267  370 ARG A CD  
2764 N NE  . ARG A 355 ? 0.9772 0.8721 0.8372 0.0568  -0.0368 0.0302  370 ARG A NE  
2765 C CZ  . ARG A 355 ? 0.8505 0.7444 0.7208 0.0559  -0.0341 0.0382  370 ARG A CZ  
2766 N NH1 . ARG A 355 ? 0.9034 0.7957 0.7715 0.0593  -0.0412 0.0442  370 ARG A NH1 
2767 N NH2 . ARG A 355 ? 0.9754 0.8690 0.8587 0.0521  -0.0255 0.0396  370 ARG A NH2 
2768 N N   . LEU A 356 ? 0.5627 0.4644 0.4017 0.0653  -0.0892 -0.0139 371 LEU A N   
2769 C CA  . LEU A 356 ? 0.6724 0.5723 0.4946 0.0685  -0.0950 -0.0277 371 LEU A CA  
2770 C C   . LEU A 356 ? 0.7437 0.6459 0.5304 0.0742  -0.0910 -0.0252 371 LEU A C   
2771 O O   . LEU A 356 ? 0.7171 0.6210 0.4891 0.0764  -0.0965 -0.0160 371 LEU A O   
2772 C CB  . LEU A 356 ? 0.6615 0.5638 0.4918 0.0682  -0.1130 -0.0378 371 LEU A CB  
2773 C CG  . LEU A 356 ? 0.6984 0.6022 0.5645 0.0604  -0.1173 -0.0387 371 LEU A CG  
2774 C CD1 . LEU A 356 ? 0.6229 0.5316 0.4981 0.0595  -0.1355 -0.0493 371 LEU A CD1 
2775 C CD2 . LEU A 356 ? 0.6928 0.5878 0.5713 0.0551  -0.1102 -0.0432 371 LEU A CD2 
2776 N N   . PRO A 357 ? 0.7391 0.6418 0.5113 0.0765  -0.0822 -0.0334 372 PRO A N   
2777 C CA  . PRO A 357 ? 0.6561 0.5647 0.3919 0.0808  -0.0787 -0.0343 372 PRO A CA  
2778 C C   . PRO A 357 ? 0.7760 0.6863 0.4923 0.0847  -0.0953 -0.0436 372 PRO A C   
2779 O O   . PRO A 357 ? 0.7290 0.6368 0.4596 0.0852  -0.1080 -0.0575 372 PRO A O   
2780 C CB  . PRO A 357 ? 0.7608 0.6728 0.4943 0.0832  -0.0673 -0.0473 372 PRO A CB  
2781 C CG  . PRO A 357 ? 0.8597 0.7631 0.6252 0.0818  -0.0738 -0.0579 372 PRO A CG  
2782 C CD  . PRO A 357 ? 0.7131 0.6118 0.5024 0.0755  -0.0763 -0.0434 372 PRO A CD  
2783 N N   . VAL A 358 ? 0.8363 0.7506 0.5179 0.0868  -0.0957 -0.0358 373 VAL A N   
2784 C CA  . VAL A 358 ? 0.8158 0.7323 0.4717 0.0909  -0.1121 -0.0432 373 VAL A CA  
2785 C C   . VAL A 358 ? 0.8748 0.7997 0.4883 0.0934  -0.1033 -0.0480 373 VAL A C   
2786 O O   . VAL A 358 ? 0.8866 0.8153 0.4853 0.0905  -0.0866 -0.0357 373 VAL A O   
2787 C CB  . VAL A 358 ? 0.8149 0.7275 0.4662 0.0911  -0.1256 -0.0268 373 VAL A CB  
2788 C CG1 . VAL A 358 ? 0.8843 0.7991 0.5138 0.0958  -0.1462 -0.0362 373 VAL A CG1 
2789 C CG2 . VAL A 358 ? 0.9250 0.8339 0.6194 0.0884  -0.1296 -0.0212 373 VAL A CG2 
2790 N N   . TYR A 359 ? 0.8579 0.7870 0.4521 0.0982  -0.1142 -0.0667 374 TYR A N   
2791 C CA  . TYR A 359 ? 1.1125 1.0524 0.6609 0.1007  -0.1076 -0.0724 374 TYR A CA  
2792 C C   . TYR A 359 ? 1.1624 1.1005 0.6746 0.1005  -0.1203 -0.0573 374 TYR A C   
2793 O O   . TYR A 359 ? 1.1485 1.0826 0.6598 0.1038  -0.1422 -0.0633 374 TYR A O   
2794 C CB  . TYR A 359 ? 0.9537 0.8991 0.4968 0.1070  -0.1134 -0.1026 374 TYR A CB  
2795 C CG  . TYR A 359 ? 1.0740 1.0339 0.5674 0.1101  -0.1069 -0.1116 374 TYR A CG  
2796 C CD1 . TYR A 359 ? 1.0216 0.9955 0.5013 0.1091  -0.0830 -0.1122 374 TYR A CD1 
2797 C CD2 . TYR A 359 ? 1.0542 1.0160 0.5139 0.1138  -0.1247 -0.1200 374 TYR A CD2 
2798 C CE1 . TYR A 359 ? 1.2602 1.2513 0.6933 0.1109  -0.0748 -0.1211 374 TYR A CE1 
2799 C CE2 . TYR A 359 ? 1.2309 1.2077 0.6409 0.1161  -0.1180 -0.1286 374 TYR A CE2 
2800 C CZ  . TYR A 359 ? 1.2685 1.2607 0.6649 0.1143  -0.0919 -0.1291 374 TYR A CZ  
2801 O OH  . TYR A 359 ? 1.2814 1.2921 0.6278 0.1155  -0.0830 -0.1382 374 TYR A OH  
2802 N N   . ASN A 360 ? 1.4074 1.3478 0.8908 0.0961  -0.1075 -0.0373 375 ASN A N   
2803 C CA  . ASN A 360 ? 1.4246 1.3610 0.8668 0.0951  -0.1186 -0.0199 375 ASN A CA  
2804 C C   . ASN A 360 ? 1.6166 1.5629 1.0159 0.0894  -0.0984 -0.0097 375 ASN A C   
2805 O O   . ASN A 360 ? 1.6345 1.5947 1.0362 0.0881  -0.0779 -0.0216 375 ASN A O   
2806 C CB  . ASN A 360 ? 1.4031 1.3239 0.8667 0.0935  -0.1299 0.0030  375 ASN A CB  
2807 C CG  . ASN A 360 ? 1.4093 1.3258 0.9089 0.0885  -0.1130 0.0141  375 ASN A CG  
2808 O OD1 . ASN A 360 ? 1.5121 1.4369 1.0133 0.0849  -0.0916 0.0107  375 ASN A OD1 
2809 N ND2 . ASN A 360 ? 1.4614 1.3666 0.9915 0.0889  -0.1229 0.0258  375 ASN A ND2 
2810 N N   . LYS A 361 ? 1.7337 1.6734 1.0937 0.0856  -0.1048 0.0127  376 LYS A N   
2811 C CA  . LYS A 361 ? 1.7238 1.6721 1.0433 0.0770  -0.0847 0.0274  376 LYS A CA  
2812 C C   . LYS A 361 ? 1.7624 1.7064 1.1082 0.0686  -0.0654 0.0457  376 LYS A C   
2813 O O   . LYS A 361 ? 1.7815 1.7381 1.1074 0.0604  -0.0430 0.0520  376 LYS A O   
2814 C CB  . LYS A 361 ? 1.6472 1.5862 0.9138 0.0740  -0.0989 0.0485  376 LYS A CB  
2815 C CG  . LYS A 361 ? 1.7239 1.6724 0.9526 0.0797  -0.1137 0.0308  376 LYS A CG  
2816 C CD  . LYS A 361 ? 1.8283 1.7686 1.0282 0.0726  -0.1304 0.0543  376 LYS A CD  
2817 C CE  . LYS A 361 ? 1.8572 1.7881 1.0703 0.0827  -0.1628 0.0458  376 LYS A CE  
2818 N NZ  . LYS A 361 ? 1.8479 1.7695 1.0415 0.0784  -0.1814 0.0707  376 LYS A NZ  
2819 N N   . SER A 362 ? 1.7492 1.6777 1.1397 0.0702  -0.0733 0.0532  377 SER A N   
2820 C CA  . SER A 362 ? 1.8235 1.7477 1.2415 0.0630  -0.0565 0.0676  377 SER A CA  
2821 C C   . SER A 362 ? 1.8124 1.7530 1.2601 0.0634  -0.0368 0.0479  377 SER A C   
2822 O O   . SER A 362 ? 1.7444 1.6918 1.1986 0.0559  -0.0166 0.0557  377 SER A O   
2823 C CB  . SER A 362 ? 1.7414 1.6456 1.1963 0.0656  -0.0716 0.0793  377 SER A CB  
2824 O OG  . SER A 362 ? 1.7390 1.6266 1.1695 0.0659  -0.0901 0.0993  377 SER A OG  
2825 N N   . ALA A 363 ? 1.6764 1.6227 1.1442 0.0719  -0.0437 0.0225  378 ALA A N   
2826 C CA  . ALA A 363 ? 1.5636 1.5240 1.0557 0.0740  -0.0280 0.0021  378 ALA A CA  
2827 C C   . ALA A 363 ? 1.6227 1.6053 1.0806 0.0739  -0.0131 -0.0113 378 ALA A C   
2828 O O   . ALA A 363 ? 1.6118 1.6099 1.0818 0.0721  0.0069  -0.0188 378 ALA A O   
2829 C CB  . ALA A 363 ? 1.2629 1.2180 0.7878 0.0823  -0.0423 -0.0191 378 ALA A CB  
2830 N N   . TRP A 364 ? 1.6537 1.6401 1.0691 0.0762  -0.0228 -0.0155 379 TRP A N   
2831 C CA  . TRP A 364 ? 1.6946 1.7046 1.0720 0.0759  -0.0084 -0.0291 379 TRP A CA  
2832 C C   . TRP A 364 ? 1.7368 1.7601 1.0964 0.0641  0.0162  -0.0105 379 TRP A C   
2833 O O   . TRP A 364 ? 1.7518 1.8009 1.1026 0.0633  0.0365  -0.0252 379 TRP A O   
2834 C CB  . TRP A 364 ? 1.7453 1.7541 1.0749 0.0790  -0.0254 -0.0319 379 TRP A CB  
2835 C CG  . TRP A 364 ? 1.8820 1.9144 1.1591 0.0752  -0.0099 -0.0366 379 TRP A CG  
2836 C CD1 . TRP A 364 ? 1.8679 1.9231 1.1311 0.0821  -0.0022 -0.0676 379 TRP A CD1 
2837 C CD2 . TRP A 364 ? 1.9696 2.0054 1.2001 0.0629  -0.0001 -0.0096 379 TRP A CD2 
2838 N NE1 . TRP A 364 ? 1.9427 2.0137 1.1666 0.0702  0.0135  -0.0614 379 TRP A NE1 
2839 C CE2 . TRP A 364 ? 1.9969 2.0554 1.2003 0.0569  0.0150  -0.0253 379 TRP A CE2 
2840 C CE3 . TRP A 364 ? 1.9759 1.9928 1.1964 0.0523  -0.0030 0.0265  379 TRP A CE3 
2841 C CZ2 . TRP A 364 ? 2.0568 2.1177 1.2195 0.0400  0.0279  -0.0052 379 TRP A CZ2 
2842 C CZ3 . TRP A 364 ? 2.0360 2.0567 1.2189 0.0347  0.0082  0.0467  379 TRP A CZ3 
2843 C CH2 . TRP A 364 ? 2.0122 2.0528 1.1642 0.0285  0.0239  0.0311  379 TRP A CH2 
2844 N N   . ARG A 365 ? 1.7779 1.7847 1.1341 0.0547  0.0146  0.0207  380 ARG A N   
2845 C CA  . ARG A 365 ? 1.8514 1.8685 1.1859 0.0409  0.0360  0.0412  380 ARG A CA  
2846 C C   . ARG A 365 ? 1.7379 1.7692 1.1130 0.0374  0.0579  0.0356  380 ARG A C   
2847 O O   . ARG A 365 ? 1.7793 1.8336 1.1402 0.0283  0.0810  0.0378  380 ARG A O   
2848 C CB  . ARG A 365 ? 1.8865 1.8772 1.2071 0.0322  0.0248  0.0761  380 ARG A CB  
2849 C CG  . ARG A 365 ? 1.9935 1.9897 1.2604 0.0183  0.0357  0.0988  380 ARG A CG  
2850 C CD  . ARG A 365 ? 2.1135 2.0781 1.3711 0.0107  0.0214  0.1337  380 ARG A CD  
2851 N NE  . ARG A 365 ? 2.0785 2.0191 1.3453 0.0225  -0.0090 0.1335  380 ARG A NE  
2852 C CZ  . ARG A 365 ? 2.1015 2.0368 1.3312 0.0271  -0.0286 0.1341  380 ARG A CZ  
2853 N NH1 . ARG A 365 ? 2.1007 2.0572 1.2923 0.0176  -0.0216 0.1334  380 ARG A NH1 
2854 N NH2 . ARG A 365 ? 2.0119 1.9266 1.2564 0.0383  -0.0561 0.1333  380 ARG A NH2 
2855 N N   . HIS A 366 ? 1.7189 1.7386 1.1442 0.0439  0.0511  0.0283  381 HIS A N   
2856 C CA  . HIS A 366 ? 1.6562 1.6872 1.1209 0.0413  0.0687  0.0236  381 HIS A CA  
2857 C C   . HIS A 366 ? 1.6676 1.7314 1.1317 0.0451  0.0871  -0.0023 381 HIS A C   
2858 O O   . HIS A 366 ? 1.6319 1.7135 1.1167 0.0399  0.1064  -0.0034 381 HIS A O   
2859 C CB  . HIS A 366 ? 1.4931 1.5065 1.0064 0.0491  0.0558  0.0170  381 HIS A CB  
2860 C CG  . HIS A 366 ? 1.5103 1.4994 1.0387 0.0433  0.0472  0.0419  381 HIS A CG  
2861 N ND1 . HIS A 366 ? 1.5346 1.5020 1.0501 0.0449  0.0270  0.0548  381 HIS A ND1 
2862 C CD2 . HIS A 366 ? 1.4567 1.4405 1.0137 0.0367  0.0551  0.0544  381 HIS A CD2 
2863 C CE1 . HIS A 366 ? 1.6807 1.6306 1.2167 0.0402  0.0236  0.0733  381 HIS A CE1 
2864 N NE2 . HIS A 366 ? 1.5809 1.5397 1.1412 0.0349  0.0404  0.0735  381 HIS A NE2 
2865 N N   . TYR A 367 ? 1.6705 1.7435 1.1129 0.0546  0.0809  -0.0249 382 TYR A N   
2866 C CA  . TYR A 367 ? 1.5802 1.6849 1.0221 0.0607  0.0968  -0.0537 382 TYR A CA  
2867 C C   . TYR A 367 ? 1.5996 1.7300 0.9898 0.0520  0.1139  -0.0497 382 TYR A C   
2868 O O   . TYR A 367 ? 1.5419 1.6929 0.9302 0.0405  0.1366  -0.0394 382 TYR A O   
2869 C CB  . TYR A 367 ? 1.4587 1.5587 0.9088 0.0767  0.0799  -0.0842 382 TYR A CB  
2870 C CG  . TYR A 367 ? 1.4526 1.5272 0.9502 0.0838  0.0626  -0.0878 382 TYR A CG  
2871 C CD1 . TYR A 367 ? 1.4125 1.4586 0.9113 0.0834  0.0408  -0.0736 382 TYR A CD1 
2872 C CD2 . TYR A 367 ? 1.3138 1.3939 0.8547 0.0907  0.0679  -0.1054 382 TYR A CD2 
2873 C CE1 . TYR A 367 ? 1.1205 1.1465 0.6610 0.0880  0.0271  -0.0765 382 TYR A CE1 
2874 C CE2 . TYR A 367 ? 1.0940 1.1504 0.6739 0.0955  0.0524  -0.1066 382 TYR A CE2 
2875 C CZ  . TYR A 367 ? 1.0471 1.0775 0.6259 0.0933  0.0332  -0.0920 382 TYR A CZ  
2876 O OH  . TYR A 367 ? 0.9740 0.9838 0.5904 0.0962  0.0199  -0.0928 382 TYR A OH  
# 
